data_9ILT
# 
_entry.id   9ILT 
# 
_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   9ILT         pdb_00009ilt 10.2210/pdb9ilt/pdb 
WWPDB D_1300049004 ?            ?                   
# 
_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       2025-03-19 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        9ILT 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-01 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              xuxl@hznu.edu.cn 
_pdbx_contact_author.name_first         Xiaoling 
_pdbx_contact_author.name_last          Xu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8995-1213 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, X.' 1 0000-0001-8995-1213 
'Wu, W.' 2 0000-0002-4905-6705 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            33 
_citation.language                  ? 
_citation.page_first                29 
_citation.page_last                 38.e2 
_citation.title                     
'Crystal structure of the alternative complex III from the phototrophic bacterium Chloroflexus aurantiacus.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2024.10.014 
_citation.pdbx_database_id_PubMed   39500318 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wu, W.'   1 ? 
primary 'Fang, H.' 2 ? 
primary 'He, H.'   3 ? 
primary 'Wu, J.'   4 ? 
primary 'Gong, Z.' 5 ? 
primary 'Li, C.'   6 ? 
primary 'Pei, X.'  7 ? 
primary 'Xu, X.'   8 ? 
# 
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 'Cytochrome c7-like domain-containing protein'                  25247.039  1 ? ? ? ? 
2  polymer     nat 'Fe-S-cluster-containing hydrogenase components 1-like protein' 113115.359 1 ? ? ? ? 
3  polymer     nat 'Polysulphide reductase NrfD'                                   55223.520  1 ? ? ? ? 
4  polymer     nat 'Quinol:cytochrome c oxidoreductase membrane protein'           19648.570  1 ? ? ? ? 
5  polymer     nat 'Cytochrome c domain-containing protein'                        23017.016  1 ? ? ? ? 
6  polymer     nat 'Quinol:cytochrome c oxidoreductase quinone-binding subunit 2'  45721.672  1 ? ? ? ? 
7  polymer     nat ActG                                                            12485.551  1 ? ? ? ? 
8  polymer     nat 'subunit I'                                                     4322.134   1 ? ? ? ? 
9  non-polymer syn 'HEME C'                                                        618.503    6 ? ? ? ? 
10 non-polymer syn 'IRON/SULFUR CLUSTER'                                           351.640    3 ? ? ? ? 
11 non-polymer syn 'FE3-S4 CLUSTER'                                                295.795    1 ? ? ? ? 
# 
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 
;MAQIFPRNANLLSRLSIFALVLLVVEGILILGVYFRSNYFRQVNVAIEQPVAFSHQLHVNVVGIDCRYCHTSVDQSYFAN
IPATETCMTCHSQIKTYSPLLEKVRESYATGKPIEWVKVYDLPNFVYFNHSIHVNKGIGCSTCHGQVNNMPVVWQQQALY
MGWCLNCHRNPELYVRPREEVYNMDYVPPSNQLEIGRQLVAEYGIMPPDQLTNCYVCHR
;
;MAQIFPRNANLLSRLSIFALVLLVVEGILILGVYFRSNYFRQVNVAIEQPVAFSHQLHVNVVGIDCRYCHTSVDQSYFAN
IPATETCMTCHSQIKTYSPLLEKVRESYATGKPIEWVKVYDLPNFVYFNHSIHVNKGIGCSTCHGQVNNMPVVWQQQALY
MGWCLNCHRNPELYVRPREEVYNMDYVPPSNQLEIGRQLVAEYGIMPPDQLTNCYVCHR
;
A ? 
2 'polypeptide(L)' no no 
;MTQQQPDLEAIRAQLRDARGPQFWRSLDQLADAPAFRELIEREFPRGASELEDGISRRTFLKLMGASLALAGVTACTYQP
RQYIAPFDRQPEGRVPGIPQYFASTLTLGGYGTGVLVRSNEGRPTKVEGNPRHPASLGGTDLFAQAEILTMYDPDRSTTV
LRQGVPSTWAEFTTTLGNALTAARATQGAGVRLLTTTITSPSLAAQIEQFLQAYPQARWYQYEPINRDNVVAGARLAFGR
DVTTRYDLSAAQVVVSLDADFLAPGPGFVAYARAFAERRKVRKDSTTMNRLYVVEASPSTTGTAADHRLPLRADAIAAFT
GALANELGVGGAPATLSPKAEEFLRAIARDLEEHRGQSVVIAGDQQPPIVHALAHLINAELGNVGQTVFYHEPVEARPTN
QTEELVALVSEMAAGRVETLIMIGGNPVYNAPGDLRFADRMASVPLTIHLSQFVDETSARATWHIPQAHPLESWGDARAF
DGTASIVQPLIEPLYGGKTANELLAAMLGQPEAESYDLVRSFWLEQIGETGWQVALANGVIAETVAPVIEPTLNEGAIRA
TPIPQPGDGVEIVFRPDPSLFDGFYANNGWLQELPRPLTKLVWDNAALMSPRTAIKLLGLPFNADRLIGTEADDRERQQY
LEQLSKVNGTIARIEYRGGIIEIPIWLLPGHAEDSITLNLGYGRTHAGRVGNNVGIDVYPIRTSDSPWFGAGARVTNTGR
TYLLVSTQDHWTLEGRDIYRVGEFKKFKEDPKYIAKEVYQEEYGRETPNYQSLQPGDDYTGRNAWGMTINLNACIGCNAC
VVACQAENNIAVVGKDQVSRGREMHWIRIDRYFAGEDLDNPSIYMMPVNCMQCEKAPCEVVCPVAATVHDYEGLNNMVYN
RCVGTKYCSNNCPYKVRRFNFLQYSDTTTETFKLAFNPDVTVRIRGVMEKCTYCVQRISGARIAAKRAAVQAGQSSYVIS
DGAIQTACEQACPTGAIVFGDINDSNSRVAKWKAEGHNYGLLGFLNTVPRTTYLARVRNPSEELEKVEG
;
;MTQQQPDLEAIRAQLRDARGPQFWRSLDQLADAPAFRELIEREFPRGASELEDGISRRTFLKLMGASLALAGVTACTYQP
RQYIAPFDRQPEGRVPGIPQYFASTLTLGGYGTGVLVRSNEGRPTKVEGNPRHPASLGGTDLFAQAEILTMYDPDRSTTV
LRQGVPSTWAEFTTTLGNALTAARATQGAGVRLLTTTITSPSLAAQIEQFLQAYPQARWYQYEPINRDNVVAGARLAFGR
DVTTRYDLSAAQVVVSLDADFLAPGPGFVAYARAFAERRKVRKDSTTMNRLYVVEASPSTTGTAADHRLPLRADAIAAFT
GALANELGVGGAPATLSPKAEEFLRAIARDLEEHRGQSVVIAGDQQPPIVHALAHLINAELGNVGQTVFYHEPVEARPTN
QTEELVALVSEMAAGRVETLIMIGGNPVYNAPGDLRFADRMASVPLTIHLSQFVDETSARATWHIPQAHPLESWGDARAF
DGTASIVQPLIEPLYGGKTANELLAAMLGQPEAESYDLVRSFWLEQIGETGWQVALANGVIAETVAPVIEPTLNEGAIRA
TPIPQPGDGVEIVFRPDPSLFDGFYANNGWLQELPRPLTKLVWDNAALMSPRTAIKLLGLPFNADRLIGTEADDRERQQY
LEQLSKVNGTIARIEYRGGIIEIPIWLLPGHAEDSITLNLGYGRTHAGRVGNNVGIDVYPIRTSDSPWFGAGARVTNTGR
TYLLVSTQDHWTLEGRDIYRVGEFKKFKEDPKYIAKEVYQEEYGRETPNYQSLQPGDDYTGRNAWGMTINLNACIGCNAC
VVACQAENNIAVVGKDQVSRGREMHWIRIDRYFAGEDLDNPSIYMMPVNCMQCEKAPCEVVCPVAATVHDYEGLNNMVYN
RCVGTKYCSNNCPYKVRRFNFLQYSDTTTETFKLAFNPDVTVRIRGVMEKCTYCVQRISGARIAAKRAAVQAGQSSYVIS
DGAIQTACEQACPTGAIVFGDINDSNSRVAKWKAEGHNYGLLGFLNTVPRTTYLARVRNPSEELEKVEG
;
B ? 
3 'polypeptide(L)' no no 
;MAQAQPLRTRPQDDGEAYLLPGETYTSISAKIGDVPLTPPLKTPKGWLAGFSVAFFMLMIFFVSVTWLFIRGVGIWGINI
PVGWGMDIINFVWWIGIGHAGTLISAILLLLNQGWRNSINRFAEAMTLFAVACAGLYPILHLGRPWLFYWLIPYPNTHGM
WPQFRSALAWDVFAISTYATVSLVFWLVGLIPDFATLRDRAKNIWVKRLYGIAALGWRGSARHWHRYEMASILLAGLSTP
LVVSVHSIISLDFAISQVPGWQVTVFPPYFVAGAVFAGFAMVLLLMIPVRTFYGFENYITLHHLDVMAKVMLTTGMIVVY
GYFMEVFASLYSGNEFEEYLLYNRLFGPSSWAYWGLLFCNAVAIQPLWFKKVRQNIPALLIISLIVSVGMWLERYVIIVI
SLERDFLPSSWDIYIPTIWDWSLYIGTFGLFFTLLFLFIRVLPMINIFEMRLFLYQETEKAKQRAGHGAHGHGHEQSPAH
GAATAD
;
;MAQAQPLRTRPQDDGEAYLLPGETYTSISAKIGDVPLTPPLKTPKGWLAGFSVAFFMLMIFFVSVTWLFIRGVGIWGINI
PVGWGMDIINFVWWIGIGHAGTLISAILLLLNQGWRNSINRFAEAMTLFAVACAGLYPILHLGRPWLFYWLIPYPNTHGM
WPQFRSALAWDVFAISTYATVSLVFWLVGLIPDFATLRDRAKNIWVKRLYGIAALGWRGSARHWHRYEMASILLAGLSTP
LVVSVHSIISLDFAISQVPGWQVTVFPPYFVAGAVFAGFAMVLLLMIPVRTFYGFENYITLHHLDVMAKVMLTTGMIVVY
GYFMEVFASLYSGNEFEEYLLYNRLFGPSSWAYWGLLFCNAVAIQPLWFKKVRQNIPALLIISLIVSVGMWLERYVIIVI
SLERDFLPSSWDIYIPTIWDWSLYIGTFGLFFTLLFLFIRVLPMINIFEMRLFLYQETEKAKQRAGHGAHGHGHEQSPAH
GAATAD
;
C ? 
4 'polypeptide(L)' no no 
;MRNDVYGVMAEFPTPEALIEATRKAKAAGYTKMDAFSPFPIEEVIEEIAHGDTGVPRLVLLFGLIGAASGFILQYIGNLV
DYPLNVGGRPLDITNWPAMIPITFESGILLASFAAAIGMIVLNGLPSPYHPVFNVPRFQYASQDAFFLCIEATDPLFDRS
RTSQFLRSLNPMQVSEVAY
;
;MRNDVYGVMAEFPTPEALIEATRKAKAAGYTKMDAFSPFPIEEVIEEIAHGDTGVPRLVLLFGLIGAASGFILQYIGNLV
DYPLNVGGRPLDITNWPAMIPITFESGILLASFAAAIGMIVLNGLPSPYHPVFNVPRFQYASQDAFFLCIEATDPLFDRS
RTSQFLRSLNPMQVSEVAY
;
D ? 
5 'polypeptide(L)' no no 
;MQKPRLTSRMIRFGWVGLLVLLLTACHQDMYDQQKYTTYEPSSFFADGRSSRPNVPGTTPFEVVKTDEFLYTGLIDGQEV
DAMPFPVTKDLLLRGQLKYNIYCAVCHGEAGYGASMVAERGGIVPANFHQQRLREAPLSHFFVVITNGVYRGDPENGGYQ
SMYGYASRITPEDRWAIAAYIRALQLSQNATIDDVPPDQRAQLGN
;
;MQKPRLTSRMIRFGWVGLLVLLLTACHQDMYDQQKYTTYEPSSFFADGRSSRPNVPGTTPFEVVKTDEFLYTGLIDGQEV
DAMPFPVTKDLLLRGQLKYNIYCAVCHGEAGYGASMVAERGGIVPANFHQQRLREAPLSHFFVVITNGVYRGDPENGGYQ
SMYGYASRITPEDRWAIAAYIRALQLSQNATIDDVPPDQRAQLGN
;
E ? 
6 'polypeptide(L)' no no 
;MATTSISQTRIPQLGQVQMLGLAAAVIGIGVLAAGYFLSPTSFFESYIYGYYVAMTIPLGCLGFLMVQHLTGGAWGVTVR
RMLEAGAATLPIMGLLFIPIALGYFDTYKALGLEHPLYEWANPEVVTPGGAEFDPIIAHKVPWLSPLWVTARIAIFFIIW
SALALTLRAWSRQQDAGGDAKKLATRMRRLSGIGVALFVITVTFFSFDVAMSLDPHWFSTIYGAHYMANAGLMTLAFLAL
MMSRVRDAALFREYVSVKPIHDIGKLIFAFTVLWTYMSYGQLVIIWSGDVAEFTPWYVHRTQHGWVFVALALMLFAFALP
FFVLLFRGTKRNLNTLATIAGWIVVMRFVDMAWIILPEFREHLWDIAITDVAAPIGLIGLVIALFAANVQQAPLLPLRDP
NMEQLQNSGHH
;
;MATTSISQTRIPQLGQVQMLGLAAAVIGIGVLAAGYFLSPTSFFESYIYGYYVAMTIPLGCLGFLMVQHLTGGAWGVTVR
RMLEAGAATLPIMGLLFIPIALGYFDTYKALGLEHPLYEWANPEVVTPGGAEFDPIIAHKVPWLSPLWVTARIAIFFIIW
SALALTLRAWSRQQDAGGDAKKLATRMRRLSGIGVALFVITVTFFSFDVAMSLDPHWFSTIYGAHYMANAGLMTLAFLAL
MMSRVRDAALFREYVSVKPIHDIGKLIFAFTVLWTYMSYGQLVIIWSGDVAEFTPWYVHRTQHGWVFVALALMLFAFALP
FFVLLFRGTKRNLNTLATIAGWIVVMRFVDMAWIILPEFREHLWDIAITDVAAPIGLIGLVIALFAANVQQAPLLPLRDP
NMEQLQNSGHH
;
F ? 
7 'polypeptide(L)' no no 
;MSYRPNYSASRYTAGRPAQPVRTARTMAEPSLSRLMIAGLMVFLVLSLVVLLAGRLPFTPQPAPVTGNTYRTYVNDARTL
LNSYGYTMEGKVHIPIDRAMDLIVERGLPVRE
;
;MSYRPNYSASRYTAGRPAQPVRTARTMAEPSLSRLMIAGLMVFLVLSLVVLLAGRLPFTPQPAPVTGNTYRTYVNDARTL
LNSYGYTMEGKVHIPIDRAMDLIVERGLPVRE
;
G ? 
8 'polypeptide(L)' no no MQPEWSGDPEVKPVFLAVTLTGMVAFLLMVWLFAFYW MQPEWSGDPEVKPVFLAVTLTGMVAFLLMVWLFAFYW I ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
9  'HEME C'              HEC 
10 'IRON/SULFUR CLUSTER' SF4 
11 'FE3-S4 CLUSTER'      F3S 
# 
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    ALA n 
1 3    GLN n 
1 4    ILE n 
1 5    PHE n 
1 6    PRO n 
1 7    ARG n 
1 8    ASN n 
1 9    ALA n 
1 10   ASN n 
1 11   LEU n 
1 12   LEU n 
1 13   SER n 
1 14   ARG n 
1 15   LEU n 
1 16   SER n 
1 17   ILE n 
1 18   PHE n 
1 19   ALA n 
1 20   LEU n 
1 21   VAL n 
1 22   LEU n 
1 23   LEU n 
1 24   VAL n 
1 25   VAL n 
1 26   GLU n 
1 27   GLY n 
1 28   ILE n 
1 29   LEU n 
1 30   ILE n 
1 31   LEU n 
1 32   GLY n 
1 33   VAL n 
1 34   TYR n 
1 35   PHE n 
1 36   ARG n 
1 37   SER n 
1 38   ASN n 
1 39   TYR n 
1 40   PHE n 
1 41   ARG n 
1 42   GLN n 
1 43   VAL n 
1 44   ASN n 
1 45   VAL n 
1 46   ALA n 
1 47   ILE n 
1 48   GLU n 
1 49   GLN n 
1 50   PRO n 
1 51   VAL n 
1 52   ALA n 
1 53   PHE n 
1 54   SER n 
1 55   HIS n 
1 56   GLN n 
1 57   LEU n 
1 58   HIS n 
1 59   VAL n 
1 60   ASN n 
1 61   VAL n 
1 62   VAL n 
1 63   GLY n 
1 64   ILE n 
1 65   ASP n 
1 66   CYS n 
1 67   ARG n 
1 68   TYR n 
1 69   CYS n 
1 70   HIS n 
1 71   THR n 
1 72   SER n 
1 73   VAL n 
1 74   ASP n 
1 75   GLN n 
1 76   SER n 
1 77   TYR n 
1 78   PHE n 
1 79   ALA n 
1 80   ASN n 
1 81   ILE n 
1 82   PRO n 
1 83   ALA n 
1 84   THR n 
1 85   GLU n 
1 86   THR n 
1 87   CYS n 
1 88   MET n 
1 89   THR n 
1 90   CYS n 
1 91   HIS n 
1 92   SER n 
1 93   GLN n 
1 94   ILE n 
1 95   LYS n 
1 96   THR n 
1 97   TYR n 
1 98   SER n 
1 99   PRO n 
1 100  LEU n 
1 101  LEU n 
1 102  GLU n 
1 103  LYS n 
1 104  VAL n 
1 105  ARG n 
1 106  GLU n 
1 107  SER n 
1 108  TYR n 
1 109  ALA n 
1 110  THR n 
1 111  GLY n 
1 112  LYS n 
1 113  PRO n 
1 114  ILE n 
1 115  GLU n 
1 116  TRP n 
1 117  VAL n 
1 118  LYS n 
1 119  VAL n 
1 120  TYR n 
1 121  ASP n 
1 122  LEU n 
1 123  PRO n 
1 124  ASN n 
1 125  PHE n 
1 126  VAL n 
1 127  TYR n 
1 128  PHE n 
1 129  ASN n 
1 130  HIS n 
1 131  SER n 
1 132  ILE n 
1 133  HIS n 
1 134  VAL n 
1 135  ASN n 
1 136  LYS n 
1 137  GLY n 
1 138  ILE n 
1 139  GLY n 
1 140  CYS n 
1 141  SER n 
1 142  THR n 
1 143  CYS n 
1 144  HIS n 
1 145  GLY n 
1 146  GLN n 
1 147  VAL n 
1 148  ASN n 
1 149  ASN n 
1 150  MET n 
1 151  PRO n 
1 152  VAL n 
1 153  VAL n 
1 154  TRP n 
1 155  GLN n 
1 156  GLN n 
1 157  GLN n 
1 158  ALA n 
1 159  LEU n 
1 160  TYR n 
1 161  MET n 
1 162  GLY n 
1 163  TRP n 
1 164  CYS n 
1 165  LEU n 
1 166  ASN n 
1 167  CYS n 
1 168  HIS n 
1 169  ARG n 
1 170  ASN n 
1 171  PRO n 
1 172  GLU n 
1 173  LEU n 
1 174  TYR n 
1 175  VAL n 
1 176  ARG n 
1 177  PRO n 
1 178  ARG n 
1 179  GLU n 
1 180  GLU n 
1 181  VAL n 
1 182  TYR n 
1 183  ASN n 
1 184  MET n 
1 185  ASP n 
1 186  TYR n 
1 187  VAL n 
1 188  PRO n 
1 189  PRO n 
1 190  SER n 
1 191  ASN n 
1 192  GLN n 
1 193  LEU n 
1 194  GLU n 
1 195  ILE n 
1 196  GLY n 
1 197  ARG n 
1 198  GLN n 
1 199  LEU n 
1 200  VAL n 
1 201  ALA n 
1 202  GLU n 
1 203  TYR n 
1 204  GLY n 
1 205  ILE n 
1 206  MET n 
1 207  PRO n 
1 208  PRO n 
1 209  ASP n 
1 210  GLN n 
1 211  LEU n 
1 212  THR n 
1 213  ASN n 
1 214  CYS n 
1 215  TYR n 
1 216  VAL n 
1 217  CYS n 
1 218  HIS n 
1 219  ARG n 
2 1    MET n 
2 2    THR n 
2 3    GLN n 
2 4    GLN n 
2 5    GLN n 
2 6    PRO n 
2 7    ASP n 
2 8    LEU n 
2 9    GLU n 
2 10   ALA n 
2 11   ILE n 
2 12   ARG n 
2 13   ALA n 
2 14   GLN n 
2 15   LEU n 
2 16   ARG n 
2 17   ASP n 
2 18   ALA n 
2 19   ARG n 
2 20   GLY n 
2 21   PRO n 
2 22   GLN n 
2 23   PHE n 
2 24   TRP n 
2 25   ARG n 
2 26   SER n 
2 27   LEU n 
2 28   ASP n 
2 29   GLN n 
2 30   LEU n 
2 31   ALA n 
2 32   ASP n 
2 33   ALA n 
2 34   PRO n 
2 35   ALA n 
2 36   PHE n 
2 37   ARG n 
2 38   GLU n 
2 39   LEU n 
2 40   ILE n 
2 41   GLU n 
2 42   ARG n 
2 43   GLU n 
2 44   PHE n 
2 45   PRO n 
2 46   ARG n 
2 47   GLY n 
2 48   ALA n 
2 49   SER n 
2 50   GLU n 
2 51   LEU n 
2 52   GLU n 
2 53   ASP n 
2 54   GLY n 
2 55   ILE n 
2 56   SER n 
2 57   ARG n 
2 58   ARG n 
2 59   THR n 
2 60   PHE n 
2 61   LEU n 
2 62   LYS n 
2 63   LEU n 
2 64   MET n 
2 65   GLY n 
2 66   ALA n 
2 67   SER n 
2 68   LEU n 
2 69   ALA n 
2 70   LEU n 
2 71   ALA n 
2 72   GLY n 
2 73   VAL n 
2 74   THR n 
2 75   ALA n 
2 76   CYS n 
2 77   THR n 
2 78   TYR n 
2 79   GLN n 
2 80   PRO n 
2 81   ARG n 
2 82   GLN n 
2 83   TYR n 
2 84   ILE n 
2 85   ALA n 
2 86   PRO n 
2 87   PHE n 
2 88   ASP n 
2 89   ARG n 
2 90   GLN n 
2 91   PRO n 
2 92   GLU n 
2 93   GLY n 
2 94   ARG n 
2 95   VAL n 
2 96   PRO n 
2 97   GLY n 
2 98   ILE n 
2 99   PRO n 
2 100  GLN n 
2 101  TYR n 
2 102  PHE n 
2 103  ALA n 
2 104  SER n 
2 105  THR n 
2 106  LEU n 
2 107  THR n 
2 108  LEU n 
2 109  GLY n 
2 110  GLY n 
2 111  TYR n 
2 112  GLY n 
2 113  THR n 
2 114  GLY n 
2 115  VAL n 
2 116  LEU n 
2 117  VAL n 
2 118  ARG n 
2 119  SER n 
2 120  ASN n 
2 121  GLU n 
2 122  GLY n 
2 123  ARG n 
2 124  PRO n 
2 125  THR n 
2 126  LYS n 
2 127  VAL n 
2 128  GLU n 
2 129  GLY n 
2 130  ASN n 
2 131  PRO n 
2 132  ARG n 
2 133  HIS n 
2 134  PRO n 
2 135  ALA n 
2 136  SER n 
2 137  LEU n 
2 138  GLY n 
2 139  GLY n 
2 140  THR n 
2 141  ASP n 
2 142  LEU n 
2 143  PHE n 
2 144  ALA n 
2 145  GLN n 
2 146  ALA n 
2 147  GLU n 
2 148  ILE n 
2 149  LEU n 
2 150  THR n 
2 151  MET n 
2 152  TYR n 
2 153  ASP n 
2 154  PRO n 
2 155  ASP n 
2 156  ARG n 
2 157  SER n 
2 158  THR n 
2 159  THR n 
2 160  VAL n 
2 161  LEU n 
2 162  ARG n 
2 163  GLN n 
2 164  GLY n 
2 165  VAL n 
2 166  PRO n 
2 167  SER n 
2 168  THR n 
2 169  TRP n 
2 170  ALA n 
2 171  GLU n 
2 172  PHE n 
2 173  THR n 
2 174  THR n 
2 175  THR n 
2 176  LEU n 
2 177  GLY n 
2 178  ASN n 
2 179  ALA n 
2 180  LEU n 
2 181  THR n 
2 182  ALA n 
2 183  ALA n 
2 184  ARG n 
2 185  ALA n 
2 186  THR n 
2 187  GLN n 
2 188  GLY n 
2 189  ALA n 
2 190  GLY n 
2 191  VAL n 
2 192  ARG n 
2 193  LEU n 
2 194  LEU n 
2 195  THR n 
2 196  THR n 
2 197  THR n 
2 198  ILE n 
2 199  THR n 
2 200  SER n 
2 201  PRO n 
2 202  SER n 
2 203  LEU n 
2 204  ALA n 
2 205  ALA n 
2 206  GLN n 
2 207  ILE n 
2 208  GLU n 
2 209  GLN n 
2 210  PHE n 
2 211  LEU n 
2 212  GLN n 
2 213  ALA n 
2 214  TYR n 
2 215  PRO n 
2 216  GLN n 
2 217  ALA n 
2 218  ARG n 
2 219  TRP n 
2 220  TYR n 
2 221  GLN n 
2 222  TYR n 
2 223  GLU n 
2 224  PRO n 
2 225  ILE n 
2 226  ASN n 
2 227  ARG n 
2 228  ASP n 
2 229  ASN n 
2 230  VAL n 
2 231  VAL n 
2 232  ALA n 
2 233  GLY n 
2 234  ALA n 
2 235  ARG n 
2 236  LEU n 
2 237  ALA n 
2 238  PHE n 
2 239  GLY n 
2 240  ARG n 
2 241  ASP n 
2 242  VAL n 
2 243  THR n 
2 244  THR n 
2 245  ARG n 
2 246  TYR n 
2 247  ASP n 
2 248  LEU n 
2 249  SER n 
2 250  ALA n 
2 251  ALA n 
2 252  GLN n 
2 253  VAL n 
2 254  VAL n 
2 255  VAL n 
2 256  SER n 
2 257  LEU n 
2 258  ASP n 
2 259  ALA n 
2 260  ASP n 
2 261  PHE n 
2 262  LEU n 
2 263  ALA n 
2 264  PRO n 
2 265  GLY n 
2 266  PRO n 
2 267  GLY n 
2 268  PHE n 
2 269  VAL n 
2 270  ALA n 
2 271  TYR n 
2 272  ALA n 
2 273  ARG n 
2 274  ALA n 
2 275  PHE n 
2 276  ALA n 
2 277  GLU n 
2 278  ARG n 
2 279  ARG n 
2 280  LYS n 
2 281  VAL n 
2 282  ARG n 
2 283  LYS n 
2 284  ASP n 
2 285  SER n 
2 286  THR n 
2 287  THR n 
2 288  MET n 
2 289  ASN n 
2 290  ARG n 
2 291  LEU n 
2 292  TYR n 
2 293  VAL n 
2 294  VAL n 
2 295  GLU n 
2 296  ALA n 
2 297  SER n 
2 298  PRO n 
2 299  SER n 
2 300  THR n 
2 301  THR n 
2 302  GLY n 
2 303  THR n 
2 304  ALA n 
2 305  ALA n 
2 306  ASP n 
2 307  HIS n 
2 308  ARG n 
2 309  LEU n 
2 310  PRO n 
2 311  LEU n 
2 312  ARG n 
2 313  ALA n 
2 314  ASP n 
2 315  ALA n 
2 316  ILE n 
2 317  ALA n 
2 318  ALA n 
2 319  PHE n 
2 320  THR n 
2 321  GLY n 
2 322  ALA n 
2 323  LEU n 
2 324  ALA n 
2 325  ASN n 
2 326  GLU n 
2 327  LEU n 
2 328  GLY n 
2 329  VAL n 
2 330  GLY n 
2 331  GLY n 
2 332  ALA n 
2 333  PRO n 
2 334  ALA n 
2 335  THR n 
2 336  LEU n 
2 337  SER n 
2 338  PRO n 
2 339  LYS n 
2 340  ALA n 
2 341  GLU n 
2 342  GLU n 
2 343  PHE n 
2 344  LEU n 
2 345  ARG n 
2 346  ALA n 
2 347  ILE n 
2 348  ALA n 
2 349  ARG n 
2 350  ASP n 
2 351  LEU n 
2 352  GLU n 
2 353  GLU n 
2 354  HIS n 
2 355  ARG n 
2 356  GLY n 
2 357  GLN n 
2 358  SER n 
2 359  VAL n 
2 360  VAL n 
2 361  ILE n 
2 362  ALA n 
2 363  GLY n 
2 364  ASP n 
2 365  GLN n 
2 366  GLN n 
2 367  PRO n 
2 368  PRO n 
2 369  ILE n 
2 370  VAL n 
2 371  HIS n 
2 372  ALA n 
2 373  LEU n 
2 374  ALA n 
2 375  HIS n 
2 376  LEU n 
2 377  ILE n 
2 378  ASN n 
2 379  ALA n 
2 380  GLU n 
2 381  LEU n 
2 382  GLY n 
2 383  ASN n 
2 384  VAL n 
2 385  GLY n 
2 386  GLN n 
2 387  THR n 
2 388  VAL n 
2 389  PHE n 
2 390  TYR n 
2 391  HIS n 
2 392  GLU n 
2 393  PRO n 
2 394  VAL n 
2 395  GLU n 
2 396  ALA n 
2 397  ARG n 
2 398  PRO n 
2 399  THR n 
2 400  ASN n 
2 401  GLN n 
2 402  THR n 
2 403  GLU n 
2 404  GLU n 
2 405  LEU n 
2 406  VAL n 
2 407  ALA n 
2 408  LEU n 
2 409  VAL n 
2 410  SER n 
2 411  GLU n 
2 412  MET n 
2 413  ALA n 
2 414  ALA n 
2 415  GLY n 
2 416  ARG n 
2 417  VAL n 
2 418  GLU n 
2 419  THR n 
2 420  LEU n 
2 421  ILE n 
2 422  MET n 
2 423  ILE n 
2 424  GLY n 
2 425  GLY n 
2 426  ASN n 
2 427  PRO n 
2 428  VAL n 
2 429  TYR n 
2 430  ASN n 
2 431  ALA n 
2 432  PRO n 
2 433  GLY n 
2 434  ASP n 
2 435  LEU n 
2 436  ARG n 
2 437  PHE n 
2 438  ALA n 
2 439  ASP n 
2 440  ARG n 
2 441  MET n 
2 442  ALA n 
2 443  SER n 
2 444  VAL n 
2 445  PRO n 
2 446  LEU n 
2 447  THR n 
2 448  ILE n 
2 449  HIS n 
2 450  LEU n 
2 451  SER n 
2 452  GLN n 
2 453  PHE n 
2 454  VAL n 
2 455  ASP n 
2 456  GLU n 
2 457  THR n 
2 458  SER n 
2 459  ALA n 
2 460  ARG n 
2 461  ALA n 
2 462  THR n 
2 463  TRP n 
2 464  HIS n 
2 465  ILE n 
2 466  PRO n 
2 467  GLN n 
2 468  ALA n 
2 469  HIS n 
2 470  PRO n 
2 471  LEU n 
2 472  GLU n 
2 473  SER n 
2 474  TRP n 
2 475  GLY n 
2 476  ASP n 
2 477  ALA n 
2 478  ARG n 
2 479  ALA n 
2 480  PHE n 
2 481  ASP n 
2 482  GLY n 
2 483  THR n 
2 484  ALA n 
2 485  SER n 
2 486  ILE n 
2 487  VAL n 
2 488  GLN n 
2 489  PRO n 
2 490  LEU n 
2 491  ILE n 
2 492  GLU n 
2 493  PRO n 
2 494  LEU n 
2 495  TYR n 
2 496  GLY n 
2 497  GLY n 
2 498  LYS n 
2 499  THR n 
2 500  ALA n 
2 501  ASN n 
2 502  GLU n 
2 503  LEU n 
2 504  LEU n 
2 505  ALA n 
2 506  ALA n 
2 507  MET n 
2 508  LEU n 
2 509  GLY n 
2 510  GLN n 
2 511  PRO n 
2 512  GLU n 
2 513  ALA n 
2 514  GLU n 
2 515  SER n 
2 516  TYR n 
2 517  ASP n 
2 518  LEU n 
2 519  VAL n 
2 520  ARG n 
2 521  SER n 
2 522  PHE n 
2 523  TRP n 
2 524  LEU n 
2 525  GLU n 
2 526  GLN n 
2 527  ILE n 
2 528  GLY n 
2 529  GLU n 
2 530  THR n 
2 531  GLY n 
2 532  TRP n 
2 533  GLN n 
2 534  VAL n 
2 535  ALA n 
2 536  LEU n 
2 537  ALA n 
2 538  ASN n 
2 539  GLY n 
2 540  VAL n 
2 541  ILE n 
2 542  ALA n 
2 543  GLU n 
2 544  THR n 
2 545  VAL n 
2 546  ALA n 
2 547  PRO n 
2 548  VAL n 
2 549  ILE n 
2 550  GLU n 
2 551  PRO n 
2 552  THR n 
2 553  LEU n 
2 554  ASN n 
2 555  GLU n 
2 556  GLY n 
2 557  ALA n 
2 558  ILE n 
2 559  ARG n 
2 560  ALA n 
2 561  THR n 
2 562  PRO n 
2 563  ILE n 
2 564  PRO n 
2 565  GLN n 
2 566  PRO n 
2 567  GLY n 
2 568  ASP n 
2 569  GLY n 
2 570  VAL n 
2 571  GLU n 
2 572  ILE n 
2 573  VAL n 
2 574  PHE n 
2 575  ARG n 
2 576  PRO n 
2 577  ASP n 
2 578  PRO n 
2 579  SER n 
2 580  LEU n 
2 581  PHE n 
2 582  ASP n 
2 583  GLY n 
2 584  PHE n 
2 585  TYR n 
2 586  ALA n 
2 587  ASN n 
2 588  ASN n 
2 589  GLY n 
2 590  TRP n 
2 591  LEU n 
2 592  GLN n 
2 593  GLU n 
2 594  LEU n 
2 595  PRO n 
2 596  ARG n 
2 597  PRO n 
2 598  LEU n 
2 599  THR n 
2 600  LYS n 
2 601  LEU n 
2 602  VAL n 
2 603  TRP n 
2 604  ASP n 
2 605  ASN n 
2 606  ALA n 
2 607  ALA n 
2 608  LEU n 
2 609  MET n 
2 610  SER n 
2 611  PRO n 
2 612  ARG n 
2 613  THR n 
2 614  ALA n 
2 615  ILE n 
2 616  LYS n 
2 617  LEU n 
2 618  LEU n 
2 619  GLY n 
2 620  LEU n 
2 621  PRO n 
2 622  PHE n 
2 623  ASN n 
2 624  ALA n 
2 625  ASP n 
2 626  ARG n 
2 627  LEU n 
2 628  ILE n 
2 629  GLY n 
2 630  THR n 
2 631  GLU n 
2 632  ALA n 
2 633  ASP n 
2 634  ASP n 
2 635  ARG n 
2 636  GLU n 
2 637  ARG n 
2 638  GLN n 
2 639  GLN n 
2 640  TYR n 
2 641  LEU n 
2 642  GLU n 
2 643  GLN n 
2 644  LEU n 
2 645  SER n 
2 646  LYS n 
2 647  VAL n 
2 648  ASN n 
2 649  GLY n 
2 650  THR n 
2 651  ILE n 
2 652  ALA n 
2 653  ARG n 
2 654  ILE n 
2 655  GLU n 
2 656  TYR n 
2 657  ARG n 
2 658  GLY n 
2 659  GLY n 
2 660  ILE n 
2 661  ILE n 
2 662  GLU n 
2 663  ILE n 
2 664  PRO n 
2 665  ILE n 
2 666  TRP n 
2 667  LEU n 
2 668  LEU n 
2 669  PRO n 
2 670  GLY n 
2 671  HIS n 
2 672  ALA n 
2 673  GLU n 
2 674  ASP n 
2 675  SER n 
2 676  ILE n 
2 677  THR n 
2 678  LEU n 
2 679  ASN n 
2 680  LEU n 
2 681  GLY n 
2 682  TYR n 
2 683  GLY n 
2 684  ARG n 
2 685  THR n 
2 686  HIS n 
2 687  ALA n 
2 688  GLY n 
2 689  ARG n 
2 690  VAL n 
2 691  GLY n 
2 692  ASN n 
2 693  ASN n 
2 694  VAL n 
2 695  GLY n 
2 696  ILE n 
2 697  ASP n 
2 698  VAL n 
2 699  TYR n 
2 700  PRO n 
2 701  ILE n 
2 702  ARG n 
2 703  THR n 
2 704  SER n 
2 705  ASP n 
2 706  SER n 
2 707  PRO n 
2 708  TRP n 
2 709  PHE n 
2 710  GLY n 
2 711  ALA n 
2 712  GLY n 
2 713  ALA n 
2 714  ARG n 
2 715  VAL n 
2 716  THR n 
2 717  ASN n 
2 718  THR n 
2 719  GLY n 
2 720  ARG n 
2 721  THR n 
2 722  TYR n 
2 723  LEU n 
2 724  LEU n 
2 725  VAL n 
2 726  SER n 
2 727  THR n 
2 728  GLN n 
2 729  ASP n 
2 730  HIS n 
2 731  TRP n 
2 732  THR n 
2 733  LEU n 
2 734  GLU n 
2 735  GLY n 
2 736  ARG n 
2 737  ASP n 
2 738  ILE n 
2 739  TYR n 
2 740  ARG n 
2 741  VAL n 
2 742  GLY n 
2 743  GLU n 
2 744  PHE n 
2 745  LYS n 
2 746  LYS n 
2 747  PHE n 
2 748  LYS n 
2 749  GLU n 
2 750  ASP n 
2 751  PRO n 
2 752  LYS n 
2 753  TYR n 
2 754  ILE n 
2 755  ALA n 
2 756  LYS n 
2 757  GLU n 
2 758  VAL n 
2 759  TYR n 
2 760  GLN n 
2 761  GLU n 
2 762  GLU n 
2 763  TYR n 
2 764  GLY n 
2 765  ARG n 
2 766  GLU n 
2 767  THR n 
2 768  PRO n 
2 769  ASN n 
2 770  TYR n 
2 771  GLN n 
2 772  SER n 
2 773  LEU n 
2 774  GLN n 
2 775  PRO n 
2 776  GLY n 
2 777  ASP n 
2 778  ASP n 
2 779  TYR n 
2 780  THR n 
2 781  GLY n 
2 782  ARG n 
2 783  ASN n 
2 784  ALA n 
2 785  TRP n 
2 786  GLY n 
2 787  MET n 
2 788  THR n 
2 789  ILE n 
2 790  ASN n 
2 791  LEU n 
2 792  ASN n 
2 793  ALA n 
2 794  CYS n 
2 795  ILE n 
2 796  GLY n 
2 797  CYS n 
2 798  ASN n 
2 799  ALA n 
2 800  CYS n 
2 801  VAL n 
2 802  VAL n 
2 803  ALA n 
2 804  CYS n 
2 805  GLN n 
2 806  ALA n 
2 807  GLU n 
2 808  ASN n 
2 809  ASN n 
2 810  ILE n 
2 811  ALA n 
2 812  VAL n 
2 813  VAL n 
2 814  GLY n 
2 815  LYS n 
2 816  ASP n 
2 817  GLN n 
2 818  VAL n 
2 819  SER n 
2 820  ARG n 
2 821  GLY n 
2 822  ARG n 
2 823  GLU n 
2 824  MET n 
2 825  HIS n 
2 826  TRP n 
2 827  ILE n 
2 828  ARG n 
2 829  ILE n 
2 830  ASP n 
2 831  ARG n 
2 832  TYR n 
2 833  PHE n 
2 834  ALA n 
2 835  GLY n 
2 836  GLU n 
2 837  ASP n 
2 838  LEU n 
2 839  ASP n 
2 840  ASN n 
2 841  PRO n 
2 842  SER n 
2 843  ILE n 
2 844  TYR n 
2 845  MET n 
2 846  MET n 
2 847  PRO n 
2 848  VAL n 
2 849  ASN n 
2 850  CYS n 
2 851  MET n 
2 852  GLN n 
2 853  CYS n 
2 854  GLU n 
2 855  LYS n 
2 856  ALA n 
2 857  PRO n 
2 858  CYS n 
2 859  GLU n 
2 860  VAL n 
2 861  VAL n 
2 862  CYS n 
2 863  PRO n 
2 864  VAL n 
2 865  ALA n 
2 866  ALA n 
2 867  THR n 
2 868  VAL n 
2 869  HIS n 
2 870  ASP n 
2 871  TYR n 
2 872  GLU n 
2 873  GLY n 
2 874  LEU n 
2 875  ASN n 
2 876  ASN n 
2 877  MET n 
2 878  VAL n 
2 879  TYR n 
2 880  ASN n 
2 881  ARG n 
2 882  CYS n 
2 883  VAL n 
2 884  GLY n 
2 885  THR n 
2 886  LYS n 
2 887  TYR n 
2 888  CYS n 
2 889  SER n 
2 890  ASN n 
2 891  ASN n 
2 892  CYS n 
2 893  PRO n 
2 894  TYR n 
2 895  LYS n 
2 896  VAL n 
2 897  ARG n 
2 898  ARG n 
2 899  PHE n 
2 900  ASN n 
2 901  PHE n 
2 902  LEU n 
2 903  GLN n 
2 904  TYR n 
2 905  SER n 
2 906  ASP n 
2 907  THR n 
2 908  THR n 
2 909  THR n 
2 910  GLU n 
2 911  THR n 
2 912  PHE n 
2 913  LYS n 
2 914  LEU n 
2 915  ALA n 
2 916  PHE n 
2 917  ASN n 
2 918  PRO n 
2 919  ASP n 
2 920  VAL n 
2 921  THR n 
2 922  VAL n 
2 923  ARG n 
2 924  ILE n 
2 925  ARG n 
2 926  GLY n 
2 927  VAL n 
2 928  MET n 
2 929  GLU n 
2 930  LYS n 
2 931  CYS n 
2 932  THR n 
2 933  TYR n 
2 934  CYS n 
2 935  VAL n 
2 936  GLN n 
2 937  ARG n 
2 938  ILE n 
2 939  SER n 
2 940  GLY n 
2 941  ALA n 
2 942  ARG n 
2 943  ILE n 
2 944  ALA n 
2 945  ALA n 
2 946  LYS n 
2 947  ARG n 
2 948  ALA n 
2 949  ALA n 
2 950  VAL n 
2 951  GLN n 
2 952  ALA n 
2 953  GLY n 
2 954  GLN n 
2 955  SER n 
2 956  SER n 
2 957  TYR n 
2 958  VAL n 
2 959  ILE n 
2 960  SER n 
2 961  ASP n 
2 962  GLY n 
2 963  ALA n 
2 964  ILE n 
2 965  GLN n 
2 966  THR n 
2 967  ALA n 
2 968  CYS n 
2 969  GLU n 
2 970  GLN n 
2 971  ALA n 
2 972  CYS n 
2 973  PRO n 
2 974  THR n 
2 975  GLY n 
2 976  ALA n 
2 977  ILE n 
2 978  VAL n 
2 979  PHE n 
2 980  GLY n 
2 981  ASP n 
2 982  ILE n 
2 983  ASN n 
2 984  ASP n 
2 985  SER n 
2 986  ASN n 
2 987  SER n 
2 988  ARG n 
2 989  VAL n 
2 990  ALA n 
2 991  LYS n 
2 992  TRP n 
2 993  LYS n 
2 994  ALA n 
2 995  GLU n 
2 996  GLY n 
2 997  HIS n 
2 998  ASN n 
2 999  TYR n 
2 1000 GLY n 
2 1001 LEU n 
2 1002 LEU n 
2 1003 GLY n 
2 1004 PHE n 
2 1005 LEU n 
2 1006 ASN n 
2 1007 THR n 
2 1008 VAL n 
2 1009 PRO n 
2 1010 ARG n 
2 1011 THR n 
2 1012 THR n 
2 1013 TYR n 
2 1014 LEU n 
2 1015 ALA n 
2 1016 ARG n 
2 1017 VAL n 
2 1018 ARG n 
2 1019 ASN n 
2 1020 PRO n 
2 1021 SER n 
2 1022 GLU n 
2 1023 GLU n 
2 1024 LEU n 
2 1025 GLU n 
2 1026 LYS n 
2 1027 VAL n 
2 1028 GLU n 
2 1029 GLY n 
3 1    MET n 
3 2    ALA n 
3 3    GLN n 
3 4    ALA n 
3 5    GLN n 
3 6    PRO n 
3 7    LEU n 
3 8    ARG n 
3 9    THR n 
3 10   ARG n 
3 11   PRO n 
3 12   GLN n 
3 13   ASP n 
3 14   ASP n 
3 15   GLY n 
3 16   GLU n 
3 17   ALA n 
3 18   TYR n 
3 19   LEU n 
3 20   LEU n 
3 21   PRO n 
3 22   GLY n 
3 23   GLU n 
3 24   THR n 
3 25   TYR n 
3 26   THR n 
3 27   SER n 
3 28   ILE n 
3 29   SER n 
3 30   ALA n 
3 31   LYS n 
3 32   ILE n 
3 33   GLY n 
3 34   ASP n 
3 35   VAL n 
3 36   PRO n 
3 37   LEU n 
3 38   THR n 
3 39   PRO n 
3 40   PRO n 
3 41   LEU n 
3 42   LYS n 
3 43   THR n 
3 44   PRO n 
3 45   LYS n 
3 46   GLY n 
3 47   TRP n 
3 48   LEU n 
3 49   ALA n 
3 50   GLY n 
3 51   PHE n 
3 52   SER n 
3 53   VAL n 
3 54   ALA n 
3 55   PHE n 
3 56   PHE n 
3 57   MET n 
3 58   LEU n 
3 59   MET n 
3 60   ILE n 
3 61   PHE n 
3 62   PHE n 
3 63   VAL n 
3 64   SER n 
3 65   VAL n 
3 66   THR n 
3 67   TRP n 
3 68   LEU n 
3 69   PHE n 
3 70   ILE n 
3 71   ARG n 
3 72   GLY n 
3 73   VAL n 
3 74   GLY n 
3 75   ILE n 
3 76   TRP n 
3 77   GLY n 
3 78   ILE n 
3 79   ASN n 
3 80   ILE n 
3 81   PRO n 
3 82   VAL n 
3 83   GLY n 
3 84   TRP n 
3 85   GLY n 
3 86   MET n 
3 87   ASP n 
3 88   ILE n 
3 89   ILE n 
3 90   ASN n 
3 91   PHE n 
3 92   VAL n 
3 93   TRP n 
3 94   TRP n 
3 95   ILE n 
3 96   GLY n 
3 97   ILE n 
3 98   GLY n 
3 99   HIS n 
3 100  ALA n 
3 101  GLY n 
3 102  THR n 
3 103  LEU n 
3 104  ILE n 
3 105  SER n 
3 106  ALA n 
3 107  ILE n 
3 108  LEU n 
3 109  LEU n 
3 110  LEU n 
3 111  LEU n 
3 112  ASN n 
3 113  GLN n 
3 114  GLY n 
3 115  TRP n 
3 116  ARG n 
3 117  ASN n 
3 118  SER n 
3 119  ILE n 
3 120  ASN n 
3 121  ARG n 
3 122  PHE n 
3 123  ALA n 
3 124  GLU n 
3 125  ALA n 
3 126  MET n 
3 127  THR n 
3 128  LEU n 
3 129  PHE n 
3 130  ALA n 
3 131  VAL n 
3 132  ALA n 
3 133  CYS n 
3 134  ALA n 
3 135  GLY n 
3 136  LEU n 
3 137  TYR n 
3 138  PRO n 
3 139  ILE n 
3 140  LEU n 
3 141  HIS n 
3 142  LEU n 
3 143  GLY n 
3 144  ARG n 
3 145  PRO n 
3 146  TRP n 
3 147  LEU n 
3 148  PHE n 
3 149  TYR n 
3 150  TRP n 
3 151  LEU n 
3 152  ILE n 
3 153  PRO n 
3 154  TYR n 
3 155  PRO n 
3 156  ASN n 
3 157  THR n 
3 158  HIS n 
3 159  GLY n 
3 160  MET n 
3 161  TRP n 
3 162  PRO n 
3 163  GLN n 
3 164  PHE n 
3 165  ARG n 
3 166  SER n 
3 167  ALA n 
3 168  LEU n 
3 169  ALA n 
3 170  TRP n 
3 171  ASP n 
3 172  VAL n 
3 173  PHE n 
3 174  ALA n 
3 175  ILE n 
3 176  SER n 
3 177  THR n 
3 178  TYR n 
3 179  ALA n 
3 180  THR n 
3 181  VAL n 
3 182  SER n 
3 183  LEU n 
3 184  VAL n 
3 185  PHE n 
3 186  TRP n 
3 187  LEU n 
3 188  VAL n 
3 189  GLY n 
3 190  LEU n 
3 191  ILE n 
3 192  PRO n 
3 193  ASP n 
3 194  PHE n 
3 195  ALA n 
3 196  THR n 
3 197  LEU n 
3 198  ARG n 
3 199  ASP n 
3 200  ARG n 
3 201  ALA n 
3 202  LYS n 
3 203  ASN n 
3 204  ILE n 
3 205  TRP n 
3 206  VAL n 
3 207  LYS n 
3 208  ARG n 
3 209  LEU n 
3 210  TYR n 
3 211  GLY n 
3 212  ILE n 
3 213  ALA n 
3 214  ALA n 
3 215  LEU n 
3 216  GLY n 
3 217  TRP n 
3 218  ARG n 
3 219  GLY n 
3 220  SER n 
3 221  ALA n 
3 222  ARG n 
3 223  HIS n 
3 224  TRP n 
3 225  HIS n 
3 226  ARG n 
3 227  TYR n 
3 228  GLU n 
3 229  MET n 
3 230  ALA n 
3 231  SER n 
3 232  ILE n 
3 233  LEU n 
3 234  LEU n 
3 235  ALA n 
3 236  GLY n 
3 237  LEU n 
3 238  SER n 
3 239  THR n 
3 240  PRO n 
3 241  LEU n 
3 242  VAL n 
3 243  VAL n 
3 244  SER n 
3 245  VAL n 
3 246  HIS n 
3 247  SER n 
3 248  ILE n 
3 249  ILE n 
3 250  SER n 
3 251  LEU n 
3 252  ASP n 
3 253  PHE n 
3 254  ALA n 
3 255  ILE n 
3 256  SER n 
3 257  GLN n 
3 258  VAL n 
3 259  PRO n 
3 260  GLY n 
3 261  TRP n 
3 262  GLN n 
3 263  VAL n 
3 264  THR n 
3 265  VAL n 
3 266  PHE n 
3 267  PRO n 
3 268  PRO n 
3 269  TYR n 
3 270  PHE n 
3 271  VAL n 
3 272  ALA n 
3 273  GLY n 
3 274  ALA n 
3 275  VAL n 
3 276  PHE n 
3 277  ALA n 
3 278  GLY n 
3 279  PHE n 
3 280  ALA n 
3 281  MET n 
3 282  VAL n 
3 283  LEU n 
3 284  LEU n 
3 285  LEU n 
3 286  MET n 
3 287  ILE n 
3 288  PRO n 
3 289  VAL n 
3 290  ARG n 
3 291  THR n 
3 292  PHE n 
3 293  TYR n 
3 294  GLY n 
3 295  PHE n 
3 296  GLU n 
3 297  ASN n 
3 298  TYR n 
3 299  ILE n 
3 300  THR n 
3 301  LEU n 
3 302  HIS n 
3 303  HIS n 
3 304  LEU n 
3 305  ASP n 
3 306  VAL n 
3 307  MET n 
3 308  ALA n 
3 309  LYS n 
3 310  VAL n 
3 311  MET n 
3 312  LEU n 
3 313  THR n 
3 314  THR n 
3 315  GLY n 
3 316  MET n 
3 317  ILE n 
3 318  VAL n 
3 319  VAL n 
3 320  TYR n 
3 321  GLY n 
3 322  TYR n 
3 323  PHE n 
3 324  MET n 
3 325  GLU n 
3 326  VAL n 
3 327  PHE n 
3 328  ALA n 
3 329  SER n 
3 330  LEU n 
3 331  TYR n 
3 332  SER n 
3 333  GLY n 
3 334  ASN n 
3 335  GLU n 
3 336  PHE n 
3 337  GLU n 
3 338  GLU n 
3 339  TYR n 
3 340  LEU n 
3 341  LEU n 
3 342  TYR n 
3 343  ASN n 
3 344  ARG n 
3 345  LEU n 
3 346  PHE n 
3 347  GLY n 
3 348  PRO n 
3 349  SER n 
3 350  SER n 
3 351  TRP n 
3 352  ALA n 
3 353  TYR n 
3 354  TRP n 
3 355  GLY n 
3 356  LEU n 
3 357  LEU n 
3 358  PHE n 
3 359  CYS n 
3 360  ASN n 
3 361  ALA n 
3 362  VAL n 
3 363  ALA n 
3 364  ILE n 
3 365  GLN n 
3 366  PRO n 
3 367  LEU n 
3 368  TRP n 
3 369  PHE n 
3 370  LYS n 
3 371  LYS n 
3 372  VAL n 
3 373  ARG n 
3 374  GLN n 
3 375  ASN n 
3 376  ILE n 
3 377  PRO n 
3 378  ALA n 
3 379  LEU n 
3 380  LEU n 
3 381  ILE n 
3 382  ILE n 
3 383  SER n 
3 384  LEU n 
3 385  ILE n 
3 386  VAL n 
3 387  SER n 
3 388  VAL n 
3 389  GLY n 
3 390  MET n 
3 391  TRP n 
3 392  LEU n 
3 393  GLU n 
3 394  ARG n 
3 395  TYR n 
3 396  VAL n 
3 397  ILE n 
3 398  ILE n 
3 399  VAL n 
3 400  ILE n 
3 401  SER n 
3 402  LEU n 
3 403  GLU n 
3 404  ARG n 
3 405  ASP n 
3 406  PHE n 
3 407  LEU n 
3 408  PRO n 
3 409  SER n 
3 410  SER n 
3 411  TRP n 
3 412  ASP n 
3 413  ILE n 
3 414  TYR n 
3 415  ILE n 
3 416  PRO n 
3 417  THR n 
3 418  ILE n 
3 419  TRP n 
3 420  ASP n 
3 421  TRP n 
3 422  SER n 
3 423  LEU n 
3 424  TYR n 
3 425  ILE n 
3 426  GLY n 
3 427  THR n 
3 428  PHE n 
3 429  GLY n 
3 430  LEU n 
3 431  PHE n 
3 432  PHE n 
3 433  THR n 
3 434  LEU n 
3 435  LEU n 
3 436  PHE n 
3 437  LEU n 
3 438  PHE n 
3 439  ILE n 
3 440  ARG n 
3 441  VAL n 
3 442  LEU n 
3 443  PRO n 
3 444  MET n 
3 445  ILE n 
3 446  ASN n 
3 447  ILE n 
3 448  PHE n 
3 449  GLU n 
3 450  MET n 
3 451  ARG n 
3 452  LEU n 
3 453  PHE n 
3 454  LEU n 
3 455  TYR n 
3 456  GLN n 
3 457  GLU n 
3 458  THR n 
3 459  GLU n 
3 460  LYS n 
3 461  ALA n 
3 462  LYS n 
3 463  GLN n 
3 464  ARG n 
3 465  ALA n 
3 466  GLY n 
3 467  HIS n 
3 468  GLY n 
3 469  ALA n 
3 470  HIS n 
3 471  GLY n 
3 472  HIS n 
3 473  GLY n 
3 474  HIS n 
3 475  GLU n 
3 476  GLN n 
3 477  SER n 
3 478  PRO n 
3 479  ALA n 
3 480  HIS n 
3 481  GLY n 
3 482  ALA n 
3 483  ALA n 
3 484  THR n 
3 485  ALA n 
3 486  ASP n 
4 1    MET n 
4 2    ARG n 
4 3    ASN n 
4 4    ASP n 
4 5    VAL n 
4 6    TYR n 
4 7    GLY n 
4 8    VAL n 
4 9    MET n 
4 10   ALA n 
4 11   GLU n 
4 12   PHE n 
4 13   PRO n 
4 14   THR n 
4 15   PRO n 
4 16   GLU n 
4 17   ALA n 
4 18   LEU n 
4 19   ILE n 
4 20   GLU n 
4 21   ALA n 
4 22   THR n 
4 23   ARG n 
4 24   LYS n 
4 25   ALA n 
4 26   LYS n 
4 27   ALA n 
4 28   ALA n 
4 29   GLY n 
4 30   TYR n 
4 31   THR n 
4 32   LYS n 
4 33   MET n 
4 34   ASP n 
4 35   ALA n 
4 36   PHE n 
4 37   SER n 
4 38   PRO n 
4 39   PHE n 
4 40   PRO n 
4 41   ILE n 
4 42   GLU n 
4 43   GLU n 
4 44   VAL n 
4 45   ILE n 
4 46   GLU n 
4 47   GLU n 
4 48   ILE n 
4 49   ALA n 
4 50   HIS n 
4 51   GLY n 
4 52   ASP n 
4 53   THR n 
4 54   GLY n 
4 55   VAL n 
4 56   PRO n 
4 57   ARG n 
4 58   LEU n 
4 59   VAL n 
4 60   LEU n 
4 61   LEU n 
4 62   PHE n 
4 63   GLY n 
4 64   LEU n 
4 65   ILE n 
4 66   GLY n 
4 67   ALA n 
4 68   ALA n 
4 69   SER n 
4 70   GLY n 
4 71   PHE n 
4 72   ILE n 
4 73   LEU n 
4 74   GLN n 
4 75   TYR n 
4 76   ILE n 
4 77   GLY n 
4 78   ASN n 
4 79   LEU n 
4 80   VAL n 
4 81   ASP n 
4 82   TYR n 
4 83   PRO n 
4 84   LEU n 
4 85   ASN n 
4 86   VAL n 
4 87   GLY n 
4 88   GLY n 
4 89   ARG n 
4 90   PRO n 
4 91   LEU n 
4 92   ASP n 
4 93   ILE n 
4 94   THR n 
4 95   ASN n 
4 96   TRP n 
4 97   PRO n 
4 98   ALA n 
4 99   MET n 
4 100  ILE n 
4 101  PRO n 
4 102  ILE n 
4 103  THR n 
4 104  PHE n 
4 105  GLU n 
4 106  SER n 
4 107  GLY n 
4 108  ILE n 
4 109  LEU n 
4 110  LEU n 
4 111  ALA n 
4 112  SER n 
4 113  PHE n 
4 114  ALA n 
4 115  ALA n 
4 116  ALA n 
4 117  ILE n 
4 118  GLY n 
4 119  MET n 
4 120  ILE n 
4 121  VAL n 
4 122  LEU n 
4 123  ASN n 
4 124  GLY n 
4 125  LEU n 
4 126  PRO n 
4 127  SER n 
4 128  PRO n 
4 129  TYR n 
4 130  HIS n 
4 131  PRO n 
4 132  VAL n 
4 133  PHE n 
4 134  ASN n 
4 135  VAL n 
4 136  PRO n 
4 137  ARG n 
4 138  PHE n 
4 139  GLN n 
4 140  TYR n 
4 141  ALA n 
4 142  SER n 
4 143  GLN n 
4 144  ASP n 
4 145  ALA n 
4 146  PHE n 
4 147  PHE n 
4 148  LEU n 
4 149  CYS n 
4 150  ILE n 
4 151  GLU n 
4 152  ALA n 
4 153  THR n 
4 154  ASP n 
4 155  PRO n 
4 156  LEU n 
4 157  PHE n 
4 158  ASP n 
4 159  ARG n 
4 160  SER n 
4 161  ARG n 
4 162  THR n 
4 163  SER n 
4 164  GLN n 
4 165  PHE n 
4 166  LEU n 
4 167  ARG n 
4 168  SER n 
4 169  LEU n 
4 170  ASN n 
4 171  PRO n 
4 172  MET n 
4 173  GLN n 
4 174  VAL n 
4 175  SER n 
4 176  GLU n 
4 177  VAL n 
4 178  ALA n 
4 179  TYR n 
5 1    MET n 
5 2    GLN n 
5 3    LYS n 
5 4    PRO n 
5 5    ARG n 
5 6    LEU n 
5 7    THR n 
5 8    SER n 
5 9    ARG n 
5 10   MET n 
5 11   ILE n 
5 12   ARG n 
5 13   PHE n 
5 14   GLY n 
5 15   TRP n 
5 16   VAL n 
5 17   GLY n 
5 18   LEU n 
5 19   LEU n 
5 20   VAL n 
5 21   LEU n 
5 22   LEU n 
5 23   LEU n 
5 24   THR n 
5 25   ALA n 
5 26   CYS n 
5 27   HIS n 
5 28   GLN n 
5 29   ASP n 
5 30   MET n 
5 31   TYR n 
5 32   ASP n 
5 33   GLN n 
5 34   GLN n 
5 35   LYS n 
5 36   TYR n 
5 37   THR n 
5 38   THR n 
5 39   TYR n 
5 40   GLU n 
5 41   PRO n 
5 42   SER n 
5 43   SER n 
5 44   PHE n 
5 45   PHE n 
5 46   ALA n 
5 47   ASP n 
5 48   GLY n 
5 49   ARG n 
5 50   SER n 
5 51   SER n 
5 52   ARG n 
5 53   PRO n 
5 54   ASN n 
5 55   VAL n 
5 56   PRO n 
5 57   GLY n 
5 58   THR n 
5 59   THR n 
5 60   PRO n 
5 61   PHE n 
5 62   GLU n 
5 63   VAL n 
5 64   VAL n 
5 65   LYS n 
5 66   THR n 
5 67   ASP n 
5 68   GLU n 
5 69   PHE n 
5 70   LEU n 
5 71   TYR n 
5 72   THR n 
5 73   GLY n 
5 74   LEU n 
5 75   ILE n 
5 76   ASP n 
5 77   GLY n 
5 78   GLN n 
5 79   GLU n 
5 80   VAL n 
5 81   ASP n 
5 82   ALA n 
5 83   MET n 
5 84   PRO n 
5 85   PHE n 
5 86   PRO n 
5 87   VAL n 
5 88   THR n 
5 89   LYS n 
5 90   ASP n 
5 91   LEU n 
5 92   LEU n 
5 93   LEU n 
5 94   ARG n 
5 95   GLY n 
5 96   GLN n 
5 97   LEU n 
5 98   LYS n 
5 99   TYR n 
5 100  ASN n 
5 101  ILE n 
5 102  TYR n 
5 103  CYS n 
5 104  ALA n 
5 105  VAL n 
5 106  CYS n 
5 107  HIS n 
5 108  GLY n 
5 109  GLU n 
5 110  ALA n 
5 111  GLY n 
5 112  TYR n 
5 113  GLY n 
5 114  ALA n 
5 115  SER n 
5 116  MET n 
5 117  VAL n 
5 118  ALA n 
5 119  GLU n 
5 120  ARG n 
5 121  GLY n 
5 122  GLY n 
5 123  ILE n 
5 124  VAL n 
5 125  PRO n 
5 126  ALA n 
5 127  ASN n 
5 128  PHE n 
5 129  HIS n 
5 130  GLN n 
5 131  GLN n 
5 132  ARG n 
5 133  LEU n 
5 134  ARG n 
5 135  GLU n 
5 136  ALA n 
5 137  PRO n 
5 138  LEU n 
5 139  SER n 
5 140  HIS n 
5 141  PHE n 
5 142  PHE n 
5 143  VAL n 
5 144  VAL n 
5 145  ILE n 
5 146  THR n 
5 147  ASN n 
5 148  GLY n 
5 149  VAL n 
5 150  TYR n 
5 151  ARG n 
5 152  GLY n 
5 153  ASP n 
5 154  PRO n 
5 155  GLU n 
5 156  ASN n 
5 157  GLY n 
5 158  GLY n 
5 159  TYR n 
5 160  GLN n 
5 161  SER n 
5 162  MET n 
5 163  TYR n 
5 164  GLY n 
5 165  TYR n 
5 166  ALA n 
5 167  SER n 
5 168  ARG n 
5 169  ILE n 
5 170  THR n 
5 171  PRO n 
5 172  GLU n 
5 173  ASP n 
5 174  ARG n 
5 175  TRP n 
5 176  ALA n 
5 177  ILE n 
5 178  ALA n 
5 179  ALA n 
5 180  TYR n 
5 181  ILE n 
5 182  ARG n 
5 183  ALA n 
5 184  LEU n 
5 185  GLN n 
5 186  LEU n 
5 187  SER n 
5 188  GLN n 
5 189  ASN n 
5 190  ALA n 
5 191  THR n 
5 192  ILE n 
5 193  ASP n 
5 194  ASP n 
5 195  VAL n 
5 196  PRO n 
5 197  PRO n 
5 198  ASP n 
5 199  GLN n 
5 200  ARG n 
5 201  ALA n 
5 202  GLN n 
5 203  LEU n 
5 204  GLY n 
5 205  ASN n 
6 1    MET n 
6 2    ALA n 
6 3    THR n 
6 4    THR n 
6 5    SER n 
6 6    ILE n 
6 7    SER n 
6 8    GLN n 
6 9    THR n 
6 10   ARG n 
6 11   ILE n 
6 12   PRO n 
6 13   GLN n 
6 14   LEU n 
6 15   GLY n 
6 16   GLN n 
6 17   VAL n 
6 18   GLN n 
6 19   MET n 
6 20   LEU n 
6 21   GLY n 
6 22   LEU n 
6 23   ALA n 
6 24   ALA n 
6 25   ALA n 
6 26   VAL n 
6 27   ILE n 
6 28   GLY n 
6 29   ILE n 
6 30   GLY n 
6 31   VAL n 
6 32   LEU n 
6 33   ALA n 
6 34   ALA n 
6 35   GLY n 
6 36   TYR n 
6 37   PHE n 
6 38   LEU n 
6 39   SER n 
6 40   PRO n 
6 41   THR n 
6 42   SER n 
6 43   PHE n 
6 44   PHE n 
6 45   GLU n 
6 46   SER n 
6 47   TYR n 
6 48   ILE n 
6 49   TYR n 
6 50   GLY n 
6 51   TYR n 
6 52   TYR n 
6 53   VAL n 
6 54   ALA n 
6 55   MET n 
6 56   THR n 
6 57   ILE n 
6 58   PRO n 
6 59   LEU n 
6 60   GLY n 
6 61   CYS n 
6 62   LEU n 
6 63   GLY n 
6 64   PHE n 
6 65   LEU n 
6 66   MET n 
6 67   VAL n 
6 68   GLN n 
6 69   HIS n 
6 70   LEU n 
6 71   THR n 
6 72   GLY n 
6 73   GLY n 
6 74   ALA n 
6 75   TRP n 
6 76   GLY n 
6 77   VAL n 
6 78   THR n 
6 79   VAL n 
6 80   ARG n 
6 81   ARG n 
6 82   MET n 
6 83   LEU n 
6 84   GLU n 
6 85   ALA n 
6 86   GLY n 
6 87   ALA n 
6 88   ALA n 
6 89   THR n 
6 90   LEU n 
6 91   PRO n 
6 92   ILE n 
6 93   MET n 
6 94   GLY n 
6 95   LEU n 
6 96   LEU n 
6 97   PHE n 
6 98   ILE n 
6 99   PRO n 
6 100  ILE n 
6 101  ALA n 
6 102  LEU n 
6 103  GLY n 
6 104  TYR n 
6 105  PHE n 
6 106  ASP n 
6 107  THR n 
6 108  TYR n 
6 109  LYS n 
6 110  ALA n 
6 111  LEU n 
6 112  GLY n 
6 113  LEU n 
6 114  GLU n 
6 115  HIS n 
6 116  PRO n 
6 117  LEU n 
6 118  TYR n 
6 119  GLU n 
6 120  TRP n 
6 121  ALA n 
6 122  ASN n 
6 123  PRO n 
6 124  GLU n 
6 125  VAL n 
6 126  VAL n 
6 127  THR n 
6 128  PRO n 
6 129  GLY n 
6 130  GLY n 
6 131  ALA n 
6 132  GLU n 
6 133  PHE n 
6 134  ASP n 
6 135  PRO n 
6 136  ILE n 
6 137  ILE n 
6 138  ALA n 
6 139  HIS n 
6 140  LYS n 
6 141  VAL n 
6 142  PRO n 
6 143  TRP n 
6 144  LEU n 
6 145  SER n 
6 146  PRO n 
6 147  LEU n 
6 148  TRP n 
6 149  VAL n 
6 150  THR n 
6 151  ALA n 
6 152  ARG n 
6 153  ILE n 
6 154  ALA n 
6 155  ILE n 
6 156  PHE n 
6 157  PHE n 
6 158  ILE n 
6 159  ILE n 
6 160  TRP n 
6 161  SER n 
6 162  ALA n 
6 163  LEU n 
6 164  ALA n 
6 165  LEU n 
6 166  THR n 
6 167  LEU n 
6 168  ARG n 
6 169  ALA n 
6 170  TRP n 
6 171  SER n 
6 172  ARG n 
6 173  GLN n 
6 174  GLN n 
6 175  ASP n 
6 176  ALA n 
6 177  GLY n 
6 178  GLY n 
6 179  ASP n 
6 180  ALA n 
6 181  LYS n 
6 182  LYS n 
6 183  LEU n 
6 184  ALA n 
6 185  THR n 
6 186  ARG n 
6 187  MET n 
6 188  ARG n 
6 189  ARG n 
6 190  LEU n 
6 191  SER n 
6 192  GLY n 
6 193  ILE n 
6 194  GLY n 
6 195  VAL n 
6 196  ALA n 
6 197  LEU n 
6 198  PHE n 
6 199  VAL n 
6 200  ILE n 
6 201  THR n 
6 202  VAL n 
6 203  THR n 
6 204  PHE n 
6 205  PHE n 
6 206  SER n 
6 207  PHE n 
6 208  ASP n 
6 209  VAL n 
6 210  ALA n 
6 211  MET n 
6 212  SER n 
6 213  LEU n 
6 214  ASP n 
6 215  PRO n 
6 216  HIS n 
6 217  TRP n 
6 218  PHE n 
6 219  SER n 
6 220  THR n 
6 221  ILE n 
6 222  TYR n 
6 223  GLY n 
6 224  ALA n 
6 225  HIS n 
6 226  TYR n 
6 227  MET n 
6 228  ALA n 
6 229  ASN n 
6 230  ALA n 
6 231  GLY n 
6 232  LEU n 
6 233  MET n 
6 234  THR n 
6 235  LEU n 
6 236  ALA n 
6 237  PHE n 
6 238  LEU n 
6 239  ALA n 
6 240  LEU n 
6 241  MET n 
6 242  MET n 
6 243  SER n 
6 244  ARG n 
6 245  VAL n 
6 246  ARG n 
6 247  ASP n 
6 248  ALA n 
6 249  ALA n 
6 250  LEU n 
6 251  PHE n 
6 252  ARG n 
6 253  GLU n 
6 254  TYR n 
6 255  VAL n 
6 256  SER n 
6 257  VAL n 
6 258  LYS n 
6 259  PRO n 
6 260  ILE n 
6 261  HIS n 
6 262  ASP n 
6 263  ILE n 
6 264  GLY n 
6 265  LYS n 
6 266  LEU n 
6 267  ILE n 
6 268  PHE n 
6 269  ALA n 
6 270  PHE n 
6 271  THR n 
6 272  VAL n 
6 273  LEU n 
6 274  TRP n 
6 275  THR n 
6 276  TYR n 
6 277  MET n 
6 278  SER n 
6 279  TYR n 
6 280  GLY n 
6 281  GLN n 
6 282  LEU n 
6 283  VAL n 
6 284  ILE n 
6 285  ILE n 
6 286  TRP n 
6 287  SER n 
6 288  GLY n 
6 289  ASP n 
6 290  VAL n 
6 291  ALA n 
6 292  GLU n 
6 293  PHE n 
6 294  THR n 
6 295  PRO n 
6 296  TRP n 
6 297  TYR n 
6 298  VAL n 
6 299  HIS n 
6 300  ARG n 
6 301  THR n 
6 302  GLN n 
6 303  HIS n 
6 304  GLY n 
6 305  TRP n 
6 306  VAL n 
6 307  PHE n 
6 308  VAL n 
6 309  ALA n 
6 310  LEU n 
6 311  ALA n 
6 312  LEU n 
6 313  MET n 
6 314  LEU n 
6 315  PHE n 
6 316  ALA n 
6 317  PHE n 
6 318  ALA n 
6 319  LEU n 
6 320  PRO n 
6 321  PHE n 
6 322  PHE n 
6 323  VAL n 
6 324  LEU n 
6 325  LEU n 
6 326  PHE n 
6 327  ARG n 
6 328  GLY n 
6 329  THR n 
6 330  LYS n 
6 331  ARG n 
6 332  ASN n 
6 333  LEU n 
6 334  ASN n 
6 335  THR n 
6 336  LEU n 
6 337  ALA n 
6 338  THR n 
6 339  ILE n 
6 340  ALA n 
6 341  GLY n 
6 342  TRP n 
6 343  ILE n 
6 344  VAL n 
6 345  VAL n 
6 346  MET n 
6 347  ARG n 
6 348  PHE n 
6 349  VAL n 
6 350  ASP n 
6 351  MET n 
6 352  ALA n 
6 353  TRP n 
6 354  ILE n 
6 355  ILE n 
6 356  LEU n 
6 357  PRO n 
6 358  GLU n 
6 359  PHE n 
6 360  ARG n 
6 361  GLU n 
6 362  HIS n 
6 363  LEU n 
6 364  TRP n 
6 365  ASP n 
6 366  ILE n 
6 367  ALA n 
6 368  ILE n 
6 369  THR n 
6 370  ASP n 
6 371  VAL n 
6 372  ALA n 
6 373  ALA n 
6 374  PRO n 
6 375  ILE n 
6 376  GLY n 
6 377  LEU n 
6 378  ILE n 
6 379  GLY n 
6 380  LEU n 
6 381  VAL n 
6 382  ILE n 
6 383  ALA n 
6 384  LEU n 
6 385  PHE n 
6 386  ALA n 
6 387  ALA n 
6 388  ASN n 
6 389  VAL n 
6 390  GLN n 
6 391  GLN n 
6 392  ALA n 
6 393  PRO n 
6 394  LEU n 
6 395  LEU n 
6 396  PRO n 
6 397  LEU n 
6 398  ARG n 
6 399  ASP n 
6 400  PRO n 
6 401  ASN n 
6 402  MET n 
6 403  GLU n 
6 404  GLN n 
6 405  LEU n 
6 406  GLN n 
6 407  ASN n 
6 408  SER n 
6 409  GLY n 
6 410  HIS n 
6 411  HIS n 
7 1    MET n 
7 2    SER n 
7 3    TYR n 
7 4    ARG n 
7 5    PRO n 
7 6    ASN n 
7 7    TYR n 
7 8    SER n 
7 9    ALA n 
7 10   SER n 
7 11   ARG n 
7 12   TYR n 
7 13   THR n 
7 14   ALA n 
7 15   GLY n 
7 16   ARG n 
7 17   PRO n 
7 18   ALA n 
7 19   GLN n 
7 20   PRO n 
7 21   VAL n 
7 22   ARG n 
7 23   THR n 
7 24   ALA n 
7 25   ARG n 
7 26   THR n 
7 27   MET n 
7 28   ALA n 
7 29   GLU n 
7 30   PRO n 
7 31   SER n 
7 32   LEU n 
7 33   SER n 
7 34   ARG n 
7 35   LEU n 
7 36   MET n 
7 37   ILE n 
7 38   ALA n 
7 39   GLY n 
7 40   LEU n 
7 41   MET n 
7 42   VAL n 
7 43   PHE n 
7 44   LEU n 
7 45   VAL n 
7 46   LEU n 
7 47   SER n 
7 48   LEU n 
7 49   VAL n 
7 50   VAL n 
7 51   LEU n 
7 52   LEU n 
7 53   ALA n 
7 54   GLY n 
7 55   ARG n 
7 56   LEU n 
7 57   PRO n 
7 58   PHE n 
7 59   THR n 
7 60   PRO n 
7 61   GLN n 
7 62   PRO n 
7 63   ALA n 
7 64   PRO n 
7 65   VAL n 
7 66   THR n 
7 67   GLY n 
7 68   ASN n 
7 69   THR n 
7 70   TYR n 
7 71   ARG n 
7 72   THR n 
7 73   TYR n 
7 74   VAL n 
7 75   ASN n 
7 76   ASP n 
7 77   ALA n 
7 78   ARG n 
7 79   THR n 
7 80   LEU n 
7 81   LEU n 
7 82   ASN n 
7 83   SER n 
7 84   TYR n 
7 85   GLY n 
7 86   TYR n 
7 87   THR n 
7 88   MET n 
7 89   GLU n 
7 90   GLY n 
7 91   LYS n 
7 92   VAL n 
7 93   HIS n 
7 94   ILE n 
7 95   PRO n 
7 96   ILE n 
7 97   ASP n 
7 98   ARG n 
7 99   ALA n 
7 100  MET n 
7 101  ASP n 
7 102  LEU n 
7 103  ILE n 
7 104  VAL n 
7 105  GLU n 
7 106  ARG n 
7 107  GLY n 
7 108  LEU n 
7 109  PRO n 
7 110  VAL n 
7 111  ARG n 
7 112  GLU n 
8 1    MET n 
8 2    GLN n 
8 3    PRO n 
8 4    GLU n 
8 5    TRP n 
8 6    SER n 
8 7    GLY n 
8 8    ASP n 
8 9    PRO n 
8 10   GLU n 
8 11   VAL n 
8 12   LYS n 
8 13   PRO n 
8 14   VAL n 
8 15   PHE n 
8 16   LEU n 
8 17   ALA n 
8 18   VAL n 
8 19   THR n 
8 20   LEU n 
8 21   THR n 
8 22   GLY n 
8 23   MET n 
8 24   VAL n 
8 25   ALA n 
8 26   PHE n 
8 27   LEU n 
8 28   LEU n 
8 29   MET n 
8 30   VAL n 
8 31   TRP n 
8 32   LEU n 
8 33   PHE n 
8 34   ALA n 
8 35   PHE n 
8 36   TYR n 
8 37   TRP 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 1 219  ? 'Chloroflexus aurantiacus J-10-fl' 324602 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 1 1029 ? 'Chloroflexus aurantiacus J-10-fl' 324602 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 1 486  ? 'Chloroflexus aurantiacus J-10-fl' 324602 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 1 179  ? 'Chloroflexus aurantiacus J-10-fl' 324602 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
5 1 sample 1 205  ? 'Chloroflexus aurantiacus J-10-fl' 324602 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
6 1 sample 1 411  ? 'Chloroflexus aurantiacus J-10-fl' 324602 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
7 1 sample 1 112  ? 'Chloroflexus aurantiacus J-10-fl' 324602 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
8 1 sample 1 37   ? 'Chloroflexus aurantiacus J-10-fl' 324602 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
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 
F3S non-polymer         . 'FE3-S4 CLUSTER'      ? 'Fe3 S4'           295.795 
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  
HEC non-polymer         . 'HEME C'              ? 'C34 H34 Fe N4 O4' 618.503 
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 
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 
SF4 non-polymer         . 'IRON/SULFUR CLUSTER' ? 'Fe4 S4'           351.640 
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    ?    ?   ?   A . n 
A 1 2    ALA 2    2    2    ALA ALA A . n 
A 1 3    GLN 3    3    3    GLN GLN A . n 
A 1 4    ILE 4    4    4    ILE ILE A . n 
A 1 5    PHE 5    5    5    PHE PHE A . n 
A 1 6    PRO 6    6    6    PRO PRO A . n 
A 1 7    ARG 7    7    7    ARG ARG A . n 
A 1 8    ASN 8    8    8    ASN ASN A . n 
A 1 9    ALA 9    9    9    ALA ALA A . n 
A 1 10   ASN 10   10   10   ASN ASN A . n 
A 1 11   LEU 11   11   11   LEU LEU A . n 
A 1 12   LEU 12   12   12   LEU LEU A . n 
A 1 13   SER 13   13   13   SER SER A . n 
A 1 14   ARG 14   14   14   ARG ARG A . n 
A 1 15   LEU 15   15   15   LEU LEU A . n 
A 1 16   SER 16   16   16   SER SER A . n 
A 1 17   ILE 17   17   17   ILE ILE A . n 
A 1 18   PHE 18   18   18   PHE PHE A . n 
A 1 19   ALA 19   19   19   ALA ALA A . n 
A 1 20   LEU 20   20   20   LEU LEU A . n 
A 1 21   VAL 21   21   21   VAL VAL A . n 
A 1 22   LEU 22   22   22   LEU LEU A . n 
A 1 23   LEU 23   23   23   LEU LEU A . n 
A 1 24   VAL 24   24   24   VAL VAL A . n 
A 1 25   VAL 25   25   25   VAL VAL A . n 
A 1 26   GLU 26   26   26   GLU GLU A . n 
A 1 27   GLY 27   27   27   GLY GLY A . n 
A 1 28   ILE 28   28   28   ILE ILE A . n 
A 1 29   LEU 29   29   29   LEU LEU A . n 
A 1 30   ILE 30   30   30   ILE ILE A . n 
A 1 31   LEU 31   31   31   LEU LEU A . n 
A 1 32   GLY 32   32   32   GLY GLY A . n 
A 1 33   VAL 33   33   33   VAL VAL A . n 
A 1 34   TYR 34   34   34   TYR TYR A . n 
A 1 35   PHE 35   35   35   PHE PHE A . n 
A 1 36   ARG 36   36   36   ARG ARG A . n 
A 1 37   SER 37   37   37   SER SER A . n 
A 1 38   ASN 38   38   38   ASN ASN A . n 
A 1 39   TYR 39   39   39   TYR TYR A . n 
A 1 40   PHE 40   40   40   PHE PHE A . n 
A 1 41   ARG 41   41   41   ARG ARG A . n 
A 1 42   GLN 42   42   42   GLN GLN A . n 
A 1 43   VAL 43   43   43   VAL VAL A . n 
A 1 44   ASN 44   44   44   ASN ASN A . n 
A 1 45   VAL 45   45   45   VAL VAL A . n 
A 1 46   ALA 46   46   46   ALA ALA A . n 
A 1 47   ILE 47   47   47   ILE ILE A . n 
A 1 48   GLU 48   48   48   GLU GLU A . n 
A 1 49   GLN 49   49   49   GLN GLN A . n 
A 1 50   PRO 50   50   50   PRO PRO A . n 
A 1 51   VAL 51   51   51   VAL VAL A . n 
A 1 52   ALA 52   52   52   ALA ALA A . n 
A 1 53   PHE 53   53   53   PHE PHE A . n 
A 1 54   SER 54   54   54   SER SER A . n 
A 1 55   HIS 55   55   55   HIS HIS A . n 
A 1 56   GLN 56   56   56   GLN GLN A . n 
A 1 57   LEU 57   57   57   LEU LEU A . n 
A 1 58   HIS 58   58   58   HIS HIS A . n 
A 1 59   VAL 59   59   59   VAL VAL A . n 
A 1 60   ASN 60   60   60   ASN ASN A . n 
A 1 61   VAL 61   61   61   VAL VAL A . n 
A 1 62   VAL 62   62   62   VAL VAL A . n 
A 1 63   GLY 63   63   63   GLY GLY A . n 
A 1 64   ILE 64   64   64   ILE ILE A . n 
A 1 65   ASP 65   65   65   ASP ASP A . n 
A 1 66   CYS 66   66   66   CYS CYS A . n 
A 1 67   ARG 67   67   67   ARG ARG A . n 
A 1 68   TYR 68   68   68   TYR TYR A . n 
A 1 69   CYS 69   69   69   CYS CYS A . n 
A 1 70   HIS 70   70   70   HIS HIS A . n 
A 1 71   THR 71   71   71   THR THR A . n 
A 1 72   SER 72   72   72   SER SER A . n 
A 1 73   VAL 73   73   73   VAL VAL A . n 
A 1 74   ASP 74   74   74   ASP ASP A . n 
A 1 75   GLN 75   75   75   GLN GLN A . n 
A 1 76   SER 76   76   76   SER SER A . n 
A 1 77   TYR 77   77   77   TYR TYR A . n 
A 1 78   PHE 78   78   78   PHE PHE A . n 
A 1 79   ALA 79   79   79   ALA ALA A . n 
A 1 80   ASN 80   80   80   ASN ASN A . n 
A 1 81   ILE 81   81   81   ILE ILE A . n 
A 1 82   PRO 82   82   82   PRO PRO A . n 
A 1 83   ALA 83   83   83   ALA ALA A . n 
A 1 84   THR 84   84   84   THR THR A . n 
A 1 85   GLU 85   85   85   GLU GLU A . n 
A 1 86   THR 86   86   86   THR THR A . n 
A 1 87   CYS 87   87   87   CYS CYS A . n 
A 1 88   MET 88   88   88   MET MET A . n 
A 1 89   THR 89   89   89   THR THR A . n 
A 1 90   CYS 90   90   90   CYS CYS A . n 
A 1 91   HIS 91   91   91   HIS HIS A . n 
A 1 92   SER 92   92   92   SER SER A . n 
A 1 93   GLN 93   93   93   GLN GLN A . n 
A 1 94   ILE 94   94   94   ILE ILE A . n 
A 1 95   LYS 95   95   95   LYS LYS A . n 
A 1 96   THR 96   96   96   THR THR A . n 
A 1 97   TYR 97   97   97   TYR TYR A . n 
A 1 98   SER 98   98   98   SER SER A . n 
A 1 99   PRO 99   99   99   PRO PRO A . n 
A 1 100  LEU 100  100  100  LEU LEU A . n 
A 1 101  LEU 101  101  101  LEU LEU A . n 
A 1 102  GLU 102  102  102  GLU GLU A . n 
A 1 103  LYS 103  103  103  LYS LYS A . n 
A 1 104  VAL 104  104  104  VAL VAL A . n 
A 1 105  ARG 105  105  105  ARG ARG A . n 
A 1 106  GLU 106  106  106  GLU GLU A . n 
A 1 107  SER 107  107  107  SER SER A . n 
A 1 108  TYR 108  108  108  TYR TYR A . n 
A 1 109  ALA 109  109  109  ALA ALA A . n 
A 1 110  THR 110  110  110  THR THR A . n 
A 1 111  GLY 111  111  111  GLY GLY A . n 
A 1 112  LYS 112  112  112  LYS LYS A . n 
A 1 113  PRO 113  113  113  PRO PRO A . n 
A 1 114  ILE 114  114  114  ILE ILE A . n 
A 1 115  GLU 115  115  115  GLU GLU A . n 
A 1 116  TRP 116  116  116  TRP TRP A . n 
A 1 117  VAL 117  117  117  VAL VAL A . n 
A 1 118  LYS 118  118  118  LYS LYS A . n 
A 1 119  VAL 119  119  119  VAL VAL A . n 
A 1 120  TYR 120  120  120  TYR TYR A . n 
A 1 121  ASP 121  121  121  ASP ASP A . n 
A 1 122  LEU 122  122  122  LEU LEU A . n 
A 1 123  PRO 123  123  123  PRO PRO A . n 
A 1 124  ASN 124  124  124  ASN ASN A . n 
A 1 125  PHE 125  125  125  PHE PHE A . n 
A 1 126  VAL 126  126  126  VAL VAL A . n 
A 1 127  TYR 127  127  127  TYR TYR A . n 
A 1 128  PHE 128  128  128  PHE PHE A . n 
A 1 129  ASN 129  129  129  ASN ASN A . n 
A 1 130  HIS 130  130  130  HIS HIS A . n 
A 1 131  SER 131  131  131  SER SER A . n 
A 1 132  ILE 132  132  132  ILE ILE A . n 
A 1 133  HIS 133  133  133  HIS HIS A . n 
A 1 134  VAL 134  134  134  VAL VAL A . n 
A 1 135  ASN 135  135  135  ASN ASN A . n 
A 1 136  LYS 136  136  136  LYS LYS A . n 
A 1 137  GLY 137  137  137  GLY GLY A . n 
A 1 138  ILE 138  138  138  ILE ILE A . n 
A 1 139  GLY 139  139  139  GLY GLY A . n 
A 1 140  CYS 140  140  140  CYS CYS A . n 
A 1 141  SER 141  141  141  SER SER A . n 
A 1 142  THR 142  142  142  THR THR A . n 
A 1 143  CYS 143  143  143  CYS CYS A . n 
A 1 144  HIS 144  144  144  HIS HIS A . n 
A 1 145  GLY 145  145  145  GLY GLY A . n 
A 1 146  GLN 146  146  146  GLN GLN A . n 
A 1 147  VAL 147  147  147  VAL VAL A . n 
A 1 148  ASN 148  148  148  ASN ASN A . n 
A 1 149  ASN 149  149  149  ASN ASN A . n 
A 1 150  MET 150  150  150  MET MET A . n 
A 1 151  PRO 151  151  151  PRO PRO A . n 
A 1 152  VAL 152  152  152  VAL VAL A . n 
A 1 153  VAL 153  153  153  VAL VAL A . n 
A 1 154  TRP 154  154  154  TRP TRP A . n 
A 1 155  GLN 155  155  155  GLN GLN A . n 
A 1 156  GLN 156  156  156  GLN GLN A . n 
A 1 157  GLN 157  157  157  GLN GLN A . n 
A 1 158  ALA 158  158  158  ALA ALA A . n 
A 1 159  LEU 159  159  159  LEU LEU A . n 
A 1 160  TYR 160  160  160  TYR TYR A . n 
A 1 161  MET 161  161  161  MET MET A . n 
A 1 162  GLY 162  162  162  GLY GLY A . n 
A 1 163  TRP 163  163  163  TRP TRP A . n 
A 1 164  CYS 164  164  164  CYS CYS A . n 
A 1 165  LEU 165  165  165  LEU LEU A . n 
A 1 166  ASN 166  166  166  ASN ASN A . n 
A 1 167  CYS 167  167  167  CYS CYS A . n 
A 1 168  HIS 168  168  168  HIS HIS A . n 
A 1 169  ARG 169  169  169  ARG ARG A . n 
A 1 170  ASN 170  170  170  ASN ASN A . n 
A 1 171  PRO 171  171  171  PRO PRO A . n 
A 1 172  GLU 172  172  172  GLU GLU A . n 
A 1 173  LEU 173  173  173  LEU LEU A . n 
A 1 174  TYR 174  174  174  TYR TYR A . n 
A 1 175  VAL 175  175  175  VAL VAL A . n 
A 1 176  ARG 176  176  176  ARG ARG A . n 
A 1 177  PRO 177  177  177  PRO PRO A . n 
A 1 178  ARG 178  178  178  ARG ARG A . n 
A 1 179  GLU 179  179  179  GLU GLU A . n 
A 1 180  GLU 180  180  180  GLU GLU A . n 
A 1 181  VAL 181  181  181  VAL VAL A . n 
A 1 182  TYR 182  182  182  TYR TYR A . n 
A 1 183  ASN 183  183  183  ASN ASN A . n 
A 1 184  MET 184  184  184  MET MET A . n 
A 1 185  ASP 185  185  185  ASP ASP A . n 
A 1 186  TYR 186  186  186  TYR TYR A . n 
A 1 187  VAL 187  187  187  VAL VAL A . n 
A 1 188  PRO 188  188  188  PRO PRO A . n 
A 1 189  PRO 189  189  189  PRO PRO A . n 
A 1 190  SER 190  190  190  SER SER A . n 
A 1 191  ASN 191  191  191  ASN ASN A . n 
A 1 192  GLN 192  192  192  GLN GLN A . n 
A 1 193  LEU 193  193  193  LEU LEU A . n 
A 1 194  GLU 194  194  194  GLU GLU A . n 
A 1 195  ILE 195  195  195  ILE ILE A . n 
A 1 196  GLY 196  196  196  GLY GLY A . n 
A 1 197  ARG 197  197  197  ARG ARG A . n 
A 1 198  GLN 198  198  198  GLN GLN A . n 
A 1 199  LEU 199  199  199  LEU LEU A . n 
A 1 200  VAL 200  200  200  VAL VAL A . n 
A 1 201  ALA 201  201  201  ALA ALA A . n 
A 1 202  GLU 202  202  202  GLU GLU A . n 
A 1 203  TYR 203  203  203  TYR TYR A . n 
A 1 204  GLY 204  204  204  GLY GLY A . n 
A 1 205  ILE 205  205  205  ILE ILE A . n 
A 1 206  MET 206  206  206  MET MET A . n 
A 1 207  PRO 207  207  207  PRO PRO A . n 
A 1 208  PRO 208  208  208  PRO PRO A . n 
A 1 209  ASP 209  209  209  ASP ASP A . n 
A 1 210  GLN 210  210  210  GLN GLN A . n 
A 1 211  LEU 211  211  211  LEU LEU A . n 
A 1 212  THR 212  212  212  THR THR A . n 
A 1 213  ASN 213  213  213  ASN ASN A . n 
A 1 214  CYS 214  214  214  CYS CYS A . n 
A 1 215  TYR 215  215  215  TYR TYR A . n 
A 1 216  VAL 216  216  216  VAL VAL A . n 
A 1 217  CYS 217  217  217  CYS CYS A . n 
A 1 218  HIS 218  218  218  HIS HIS A . n 
A 1 219  ARG 219  219  219  ARG ARG A . n 
B 2 1    MET 1    1    ?    ?   ?   B . n 
B 2 2    THR 2    2    ?    ?   ?   B . n 
B 2 3    GLN 3    3    ?    ?   ?   B . n 
B 2 4    GLN 4    4    ?    ?   ?   B . n 
B 2 5    GLN 5    5    ?    ?   ?   B . n 
B 2 6    PRO 6    6    ?    ?   ?   B . n 
B 2 7    ASP 7    7    ?    ?   ?   B . n 
B 2 8    LEU 8    8    ?    ?   ?   B . n 
B 2 9    GLU 9    9    ?    ?   ?   B . n 
B 2 10   ALA 10   10   ?    ?   ?   B . n 
B 2 11   ILE 11   11   ?    ?   ?   B . n 
B 2 12   ARG 12   12   ?    ?   ?   B . n 
B 2 13   ALA 13   13   ?    ?   ?   B . n 
B 2 14   GLN 14   14   ?    ?   ?   B . n 
B 2 15   LEU 15   15   ?    ?   ?   B . n 
B 2 16   ARG 16   16   ?    ?   ?   B . n 
B 2 17   ASP 17   17   ?    ?   ?   B . n 
B 2 18   ALA 18   18   ?    ?   ?   B . n 
B 2 19   ARG 19   19   ?    ?   ?   B . n 
B 2 20   GLY 20   20   ?    ?   ?   B . n 
B 2 21   PRO 21   21   ?    ?   ?   B . n 
B 2 22   GLN 22   22   ?    ?   ?   B . n 
B 2 23   PHE 23   23   ?    ?   ?   B . n 
B 2 24   TRP 24   24   ?    ?   ?   B . n 
B 2 25   ARG 25   25   ?    ?   ?   B . n 
B 2 26   SER 26   26   ?    ?   ?   B . n 
B 2 27   LEU 27   27   ?    ?   ?   B . n 
B 2 28   ASP 28   28   ?    ?   ?   B . n 
B 2 29   GLN 29   29   ?    ?   ?   B . n 
B 2 30   LEU 30   30   ?    ?   ?   B . n 
B 2 31   ALA 31   31   ?    ?   ?   B . n 
B 2 32   ASP 32   32   ?    ?   ?   B . n 
B 2 33   ALA 33   33   ?    ?   ?   B . n 
B 2 34   PRO 34   34   ?    ?   ?   B . n 
B 2 35   ALA 35   35   ?    ?   ?   B . n 
B 2 36   PHE 36   36   ?    ?   ?   B . n 
B 2 37   ARG 37   37   ?    ?   ?   B . n 
B 2 38   GLU 38   38   ?    ?   ?   B . n 
B 2 39   LEU 39   39   ?    ?   ?   B . n 
B 2 40   ILE 40   40   ?    ?   ?   B . n 
B 2 41   GLU 41   41   ?    ?   ?   B . n 
B 2 42   ARG 42   42   ?    ?   ?   B . n 
B 2 43   GLU 43   43   ?    ?   ?   B . n 
B 2 44   PHE 44   44   ?    ?   ?   B . n 
B 2 45   PRO 45   45   ?    ?   ?   B . n 
B 2 46   ARG 46   46   ?    ?   ?   B . n 
B 2 47   GLY 47   47   ?    ?   ?   B . n 
B 2 48   ALA 48   48   ?    ?   ?   B . n 
B 2 49   SER 49   49   ?    ?   ?   B . n 
B 2 50   GLU 50   50   ?    ?   ?   B . n 
B 2 51   LEU 51   51   ?    ?   ?   B . n 
B 2 52   GLU 52   52   ?    ?   ?   B . n 
B 2 53   ASP 53   53   ?    ?   ?   B . n 
B 2 54   GLY 54   54   ?    ?   ?   B . n 
B 2 55   ILE 55   55   ?    ?   ?   B . n 
B 2 56   SER 56   56   ?    ?   ?   B . n 
B 2 57   ARG 57   57   ?    ?   ?   B . n 
B 2 58   ARG 58   58   ?    ?   ?   B . n 
B 2 59   THR 59   59   ?    ?   ?   B . n 
B 2 60   PHE 60   60   ?    ?   ?   B . n 
B 2 61   LEU 61   61   ?    ?   ?   B . n 
B 2 62   LYS 62   62   ?    ?   ?   B . n 
B 2 63   LEU 63   63   ?    ?   ?   B . n 
B 2 64   MET 64   64   ?    ?   ?   B . n 
B 2 65   GLY 65   65   ?    ?   ?   B . n 
B 2 66   ALA 66   66   ?    ?   ?   B . n 
B 2 67   SER 67   67   ?    ?   ?   B . n 
B 2 68   LEU 68   68   ?    ?   ?   B . n 
B 2 69   ALA 69   69   ?    ?   ?   B . n 
B 2 70   LEU 70   70   ?    ?   ?   B . n 
B 2 71   ALA 71   71   ?    ?   ?   B . n 
B 2 72   GLY 72   72   ?    ?   ?   B . n 
B 2 73   VAL 73   73   ?    ?   ?   B . n 
B 2 74   THR 74   74   ?    ?   ?   B . n 
B 2 75   ALA 75   75   75   ALA ALA B . n 
B 2 76   CYS 76   76   76   CYS CYS B . n 
B 2 77   THR 77   77   77   THR THR B . n 
B 2 78   TYR 78   78   78   TYR TYR B . n 
B 2 79   GLN 79   79   79   GLN GLN B . n 
B 2 80   PRO 80   80   80   PRO PRO B . n 
B 2 81   ARG 81   81   81   ARG ARG B . n 
B 2 82   GLN 82   82   82   GLN GLN B . n 
B 2 83   TYR 83   83   83   TYR TYR B . n 
B 2 84   ILE 84   84   84   ILE ILE B . n 
B 2 85   ALA 85   85   85   ALA ALA B . n 
B 2 86   PRO 86   86   86   PRO PRO B . n 
B 2 87   PHE 87   87   87   PHE PHE B . n 
B 2 88   ASP 88   88   88   ASP ASP B . n 
B 2 89   ARG 89   89   89   ARG ARG B . n 
B 2 90   GLN 90   90   90   GLN GLN B . n 
B 2 91   PRO 91   91   91   PRO PRO B . n 
B 2 92   GLU 92   92   92   GLU GLU B . n 
B 2 93   GLY 93   93   93   GLY GLY B . n 
B 2 94   ARG 94   94   94   ARG ARG B . n 
B 2 95   VAL 95   95   95   VAL VAL B . n 
B 2 96   PRO 96   96   96   PRO PRO B . n 
B 2 97   GLY 97   97   97   GLY GLY B . n 
B 2 98   ILE 98   98   98   ILE ILE B . n 
B 2 99   PRO 99   99   99   PRO PRO B . n 
B 2 100  GLN 100  100  100  GLN GLN B . n 
B 2 101  TYR 101  101  101  TYR TYR B . n 
B 2 102  PHE 102  102  102  PHE PHE B . n 
B 2 103  ALA 103  103  103  ALA ALA B . n 
B 2 104  SER 104  104  104  SER SER B . n 
B 2 105  THR 105  105  105  THR THR B . n 
B 2 106  LEU 106  106  106  LEU LEU B . n 
B 2 107  THR 107  107  107  THR THR B . n 
B 2 108  LEU 108  108  108  LEU LEU B . n 
B 2 109  GLY 109  109  109  GLY GLY B . n 
B 2 110  GLY 110  110  110  GLY GLY B . n 
B 2 111  TYR 111  111  111  TYR TYR B . n 
B 2 112  GLY 112  112  112  GLY GLY B . n 
B 2 113  THR 113  113  113  THR THR B . n 
B 2 114  GLY 114  114  114  GLY GLY B . n 
B 2 115  VAL 115  115  115  VAL VAL B . n 
B 2 116  LEU 116  116  116  LEU LEU B . n 
B 2 117  VAL 117  117  117  VAL VAL B . n 
B 2 118  ARG 118  118  118  ARG ARG B . n 
B 2 119  SER 119  119  119  SER SER B . n 
B 2 120  ASN 120  120  120  ASN ASN B . n 
B 2 121  GLU 121  121  121  GLU GLU B . n 
B 2 122  GLY 122  122  122  GLY GLY B . n 
B 2 123  ARG 123  123  123  ARG ARG B . n 
B 2 124  PRO 124  124  124  PRO PRO B . n 
B 2 125  THR 125  125  125  THR THR B . n 
B 2 126  LYS 126  126  126  LYS LYS B . n 
B 2 127  VAL 127  127  127  VAL VAL B . n 
B 2 128  GLU 128  128  128  GLU GLU B . n 
B 2 129  GLY 129  129  129  GLY GLY B . n 
B 2 130  ASN 130  130  130  ASN ASN B . n 
B 2 131  PRO 131  131  131  PRO PRO B . n 
B 2 132  ARG 132  132  132  ARG ARG B . n 
B 2 133  HIS 133  133  133  HIS HIS B . n 
B 2 134  PRO 134  134  134  PRO PRO B . n 
B 2 135  ALA 135  135  135  ALA ALA B . n 
B 2 136  SER 136  136  136  SER SER B . n 
B 2 137  LEU 137  137  137  LEU LEU B . n 
B 2 138  GLY 138  138  138  GLY GLY B . n 
B 2 139  GLY 139  139  139  GLY GLY B . n 
B 2 140  THR 140  140  140  THR THR B . n 
B 2 141  ASP 141  141  141  ASP ASP B . n 
B 2 142  LEU 142  142  142  LEU LEU B . n 
B 2 143  PHE 143  143  143  PHE PHE B . n 
B 2 144  ALA 144  144  144  ALA ALA B . n 
B 2 145  GLN 145  145  145  GLN GLN B . n 
B 2 146  ALA 146  146  146  ALA ALA B . n 
B 2 147  GLU 147  147  147  GLU GLU B . n 
B 2 148  ILE 148  148  148  ILE ILE B . n 
B 2 149  LEU 149  149  149  LEU LEU B . n 
B 2 150  THR 150  150  150  THR THR B . n 
B 2 151  MET 151  151  151  MET MET B . n 
B 2 152  TYR 152  152  152  TYR TYR B . n 
B 2 153  ASP 153  153  153  ASP ASP B . n 
B 2 154  PRO 154  154  154  PRO PRO B . n 
B 2 155  ASP 155  155  155  ASP ASP B . n 
B 2 156  ARG 156  156  156  ARG ARG B . n 
B 2 157  SER 157  157  157  SER SER B . n 
B 2 158  THR 158  158  158  THR THR B . n 
B 2 159  THR 159  159  159  THR THR B . n 
B 2 160  VAL 160  160  160  VAL VAL B . n 
B 2 161  LEU 161  161  161  LEU LEU B . n 
B 2 162  ARG 162  162  162  ARG ARG B . n 
B 2 163  GLN 163  163  163  GLN GLN B . n 
B 2 164  GLY 164  164  164  GLY GLY B . n 
B 2 165  VAL 165  165  165  VAL VAL B . n 
B 2 166  PRO 166  166  166  PRO PRO B . n 
B 2 167  SER 167  167  167  SER SER B . n 
B 2 168  THR 168  168  168  THR THR B . n 
B 2 169  TRP 169  169  169  TRP TRP B . n 
B 2 170  ALA 170  170  170  ALA ALA B . n 
B 2 171  GLU 171  171  171  GLU GLU B . n 
B 2 172  PHE 172  172  172  PHE PHE B . n 
B 2 173  THR 173  173  173  THR THR B . n 
B 2 174  THR 174  174  174  THR THR B . n 
B 2 175  THR 175  175  175  THR THR B . n 
B 2 176  LEU 176  176  176  LEU LEU B . n 
B 2 177  GLY 177  177  177  GLY GLY B . n 
B 2 178  ASN 178  178  178  ASN ASN B . n 
B 2 179  ALA 179  179  179  ALA ALA B . n 
B 2 180  LEU 180  180  180  LEU LEU B . n 
B 2 181  THR 181  181  181  THR THR B . n 
B 2 182  ALA 182  182  182  ALA ALA B . n 
B 2 183  ALA 183  183  183  ALA ALA B . n 
B 2 184  ARG 184  184  184  ARG ARG B . n 
B 2 185  ALA 185  185  185  ALA ALA B . n 
B 2 186  THR 186  186  186  THR THR B . n 
B 2 187  GLN 187  187  187  GLN GLN B . n 
B 2 188  GLY 188  188  188  GLY GLY B . n 
B 2 189  ALA 189  189  189  ALA ALA B . n 
B 2 190  GLY 190  190  190  GLY GLY B . n 
B 2 191  VAL 191  191  191  VAL VAL B . n 
B 2 192  ARG 192  192  192  ARG ARG B . n 
B 2 193  LEU 193  193  193  LEU LEU B . n 
B 2 194  LEU 194  194  194  LEU LEU B . n 
B 2 195  THR 195  195  195  THR THR B . n 
B 2 196  THR 196  196  196  THR THR B . n 
B 2 197  THR 197  197  197  THR THR B . n 
B 2 198  ILE 198  198  198  ILE ILE B . n 
B 2 199  THR 199  199  199  THR THR B . n 
B 2 200  SER 200  200  200  SER SER B . n 
B 2 201  PRO 201  201  201  PRO PRO B . n 
B 2 202  SER 202  202  202  SER SER B . n 
B 2 203  LEU 203  203  203  LEU LEU B . n 
B 2 204  ALA 204  204  204  ALA ALA B . n 
B 2 205  ALA 205  205  205  ALA ALA B . n 
B 2 206  GLN 206  206  206  GLN GLN B . n 
B 2 207  ILE 207  207  207  ILE ILE B . n 
B 2 208  GLU 208  208  208  GLU GLU B . n 
B 2 209  GLN 209  209  209  GLN GLN B . n 
B 2 210  PHE 210  210  210  PHE PHE B . n 
B 2 211  LEU 211  211  211  LEU LEU B . n 
B 2 212  GLN 212  212  212  GLN GLN B . n 
B 2 213  ALA 213  213  213  ALA ALA B . n 
B 2 214  TYR 214  214  214  TYR TYR B . n 
B 2 215  PRO 215  215  215  PRO PRO B . n 
B 2 216  GLN 216  216  216  GLN GLN B . n 
B 2 217  ALA 217  217  217  ALA ALA B . n 
B 2 218  ARG 218  218  218  ARG ARG B . n 
B 2 219  TRP 219  219  219  TRP TRP B . n 
B 2 220  TYR 220  220  220  TYR TYR B . n 
B 2 221  GLN 221  221  221  GLN GLN B . n 
B 2 222  TYR 222  222  222  TYR TYR B . n 
B 2 223  GLU 223  223  223  GLU GLU B . n 
B 2 224  PRO 224  224  224  PRO PRO B . n 
B 2 225  ILE 225  225  225  ILE ILE B . n 
B 2 226  ASN 226  226  226  ASN ASN B . n 
B 2 227  ARG 227  227  227  ARG ARG B . n 
B 2 228  ASP 228  228  228  ASP ASP B . n 
B 2 229  ASN 229  229  229  ASN ASN B . n 
B 2 230  VAL 230  230  230  VAL VAL B . n 
B 2 231  VAL 231  231  231  VAL VAL B . n 
B 2 232  ALA 232  232  232  ALA ALA B . n 
B 2 233  GLY 233  233  233  GLY GLY B . n 
B 2 234  ALA 234  234  234  ALA ALA B . n 
B 2 235  ARG 235  235  235  ARG ARG B . n 
B 2 236  LEU 236  236  236  LEU LEU B . n 
B 2 237  ALA 237  237  237  ALA ALA B . n 
B 2 238  PHE 238  238  238  PHE PHE B . n 
B 2 239  GLY 239  239  239  GLY GLY B . n 
B 2 240  ARG 240  240  240  ARG ARG B . n 
B 2 241  ASP 241  241  241  ASP ASP B . n 
B 2 242  VAL 242  242  242  VAL VAL B . n 
B 2 243  THR 243  243  243  THR THR B . n 
B 2 244  THR 244  244  244  THR THR B . n 
B 2 245  ARG 245  245  245  ARG ARG B . n 
B 2 246  TYR 246  246  246  TYR TYR B . n 
B 2 247  ASP 247  247  247  ASP ASP B . n 
B 2 248  LEU 248  248  248  LEU LEU B . n 
B 2 249  SER 249  249  249  SER SER B . n 
B 2 250  ALA 250  250  250  ALA ALA B . n 
B 2 251  ALA 251  251  251  ALA ALA B . n 
B 2 252  GLN 252  252  252  GLN GLN B . n 
B 2 253  VAL 253  253  253  VAL VAL B . n 
B 2 254  VAL 254  254  254  VAL VAL B . n 
B 2 255  VAL 255  255  255  VAL VAL B . n 
B 2 256  SER 256  256  256  SER SER B . n 
B 2 257  LEU 257  257  257  LEU LEU B . n 
B 2 258  ASP 258  258  258  ASP ASP B . n 
B 2 259  ALA 259  259  259  ALA ALA B . n 
B 2 260  ASP 260  260  260  ASP ASP B . n 
B 2 261  PHE 261  261  261  PHE PHE B . n 
B 2 262  LEU 262  262  262  LEU LEU B . n 
B 2 263  ALA 263  263  263  ALA ALA B . n 
B 2 264  PRO 264  264  264  PRO PRO B . n 
B 2 265  GLY 265  265  265  GLY GLY B . n 
B 2 266  PRO 266  266  266  PRO PRO B . n 
B 2 267  GLY 267  267  267  GLY GLY B . n 
B 2 268  PHE 268  268  268  PHE PHE B . n 
B 2 269  VAL 269  269  269  VAL VAL B . n 
B 2 270  ALA 270  270  270  ALA ALA B . n 
B 2 271  TYR 271  271  271  TYR TYR B . n 
B 2 272  ALA 272  272  272  ALA ALA B . n 
B 2 273  ARG 273  273  273  ARG ARG B . n 
B 2 274  ALA 274  274  274  ALA ALA B . n 
B 2 275  PHE 275  275  275  PHE PHE B . n 
B 2 276  ALA 276  276  276  ALA ALA B . n 
B 2 277  GLU 277  277  277  GLU GLU B . n 
B 2 278  ARG 278  278  278  ARG ARG B . n 
B 2 279  ARG 279  279  279  ARG ARG B . n 
B 2 280  LYS 280  280  280  LYS LYS B . n 
B 2 281  VAL 281  281  281  VAL VAL B . n 
B 2 282  ARG 282  282  282  ARG ARG B . n 
B 2 283  LYS 283  283  283  LYS LYS B . n 
B 2 284  ASP 284  284  284  ASP ASP B . n 
B 2 285  SER 285  285  285  SER SER B . n 
B 2 286  THR 286  286  286  THR THR B . n 
B 2 287  THR 287  287  287  THR THR B . n 
B 2 288  MET 288  288  288  MET MET B . n 
B 2 289  ASN 289  289  289  ASN ASN B . n 
B 2 290  ARG 290  290  290  ARG ARG B . n 
B 2 291  LEU 291  291  291  LEU LEU B . n 
B 2 292  TYR 292  292  292  TYR TYR B . n 
B 2 293  VAL 293  293  293  VAL VAL B . n 
B 2 294  VAL 294  294  294  VAL VAL B . n 
B 2 295  GLU 295  295  295  GLU GLU B . n 
B 2 296  ALA 296  296  296  ALA ALA B . n 
B 2 297  SER 297  297  297  SER SER B . n 
B 2 298  PRO 298  298  298  PRO PRO B . n 
B 2 299  SER 299  299  299  SER SER B . n 
B 2 300  THR 300  300  300  THR THR B . n 
B 2 301  THR 301  301  301  THR THR B . n 
B 2 302  GLY 302  302  302  GLY GLY B . n 
B 2 303  THR 303  303  303  THR THR B . n 
B 2 304  ALA 304  304  304  ALA ALA B . n 
B 2 305  ALA 305  305  305  ALA ALA B . n 
B 2 306  ASP 306  306  306  ASP ASP B . n 
B 2 307  HIS 307  307  307  HIS HIS B . n 
B 2 308  ARG 308  308  308  ARG ARG B . n 
B 2 309  LEU 309  309  309  LEU LEU B . n 
B 2 310  PRO 310  310  310  PRO PRO B . n 
B 2 311  LEU 311  311  311  LEU LEU B . n 
B 2 312  ARG 312  312  312  ARG ARG B . n 
B 2 313  ALA 313  313  313  ALA ALA B . n 
B 2 314  ASP 314  314  314  ASP ASP B . n 
B 2 315  ALA 315  315  315  ALA ALA B . n 
B 2 316  ILE 316  316  316  ILE ILE B . n 
B 2 317  ALA 317  317  317  ALA ALA B . n 
B 2 318  ALA 318  318  318  ALA ALA B . n 
B 2 319  PHE 319  319  319  PHE PHE B . n 
B 2 320  THR 320  320  320  THR THR B . n 
B 2 321  GLY 321  321  321  GLY GLY B . n 
B 2 322  ALA 322  322  322  ALA ALA B . n 
B 2 323  LEU 323  323  323  LEU LEU B . n 
B 2 324  ALA 324  324  324  ALA ALA B . n 
B 2 325  ASN 325  325  325  ASN ASN B . n 
B 2 326  GLU 326  326  326  GLU GLU B . n 
B 2 327  LEU 327  327  327  LEU LEU B . n 
B 2 328  GLY 328  328  328  GLY GLY B . n 
B 2 329  VAL 329  329  329  VAL VAL B . n 
B 2 330  GLY 330  330  330  GLY GLY B . n 
B 2 331  GLY 331  331  331  GLY GLY B . n 
B 2 332  ALA 332  332  332  ALA ALA B . n 
B 2 333  PRO 333  333  333  PRO PRO B . n 
B 2 334  ALA 334  334  334  ALA ALA B . n 
B 2 335  THR 335  335  335  THR THR B . n 
B 2 336  LEU 336  336  336  LEU LEU B . n 
B 2 337  SER 337  337  337  SER SER B . n 
B 2 338  PRO 338  338  338  PRO PRO B . n 
B 2 339  LYS 339  339  339  LYS LYS B . n 
B 2 340  ALA 340  340  340  ALA ALA B . n 
B 2 341  GLU 341  341  341  GLU GLU B . n 
B 2 342  GLU 342  342  342  GLU GLU B . n 
B 2 343  PHE 343  343  343  PHE PHE B . n 
B 2 344  LEU 344  344  344  LEU LEU B . n 
B 2 345  ARG 345  345  345  ARG ARG B . n 
B 2 346  ALA 346  346  346  ALA ALA B . n 
B 2 347  ILE 347  347  347  ILE ILE B . n 
B 2 348  ALA 348  348  348  ALA ALA B . n 
B 2 349  ARG 349  349  349  ARG ARG B . n 
B 2 350  ASP 350  350  350  ASP ASP B . n 
B 2 351  LEU 351  351  351  LEU LEU B . n 
B 2 352  GLU 352  352  352  GLU GLU B . n 
B 2 353  GLU 353  353  353  GLU GLU B . n 
B 2 354  HIS 354  354  354  HIS HIS B . n 
B 2 355  ARG 355  355  355  ARG ARG B . n 
B 2 356  GLY 356  356  356  GLY GLY B . n 
B 2 357  GLN 357  357  357  GLN GLN B . n 
B 2 358  SER 358  358  358  SER SER B . n 
B 2 359  VAL 359  359  359  VAL VAL B . n 
B 2 360  VAL 360  360  360  VAL VAL B . n 
B 2 361  ILE 361  361  361  ILE ILE B . n 
B 2 362  ALA 362  362  362  ALA ALA B . n 
B 2 363  GLY 363  363  363  GLY GLY B . n 
B 2 364  ASP 364  364  364  ASP ASP B . n 
B 2 365  GLN 365  365  365  GLN GLN B . n 
B 2 366  GLN 366  366  366  GLN GLN B . n 
B 2 367  PRO 367  367  367  PRO PRO B . n 
B 2 368  PRO 368  368  368  PRO PRO B . n 
B 2 369  ILE 369  369  369  ILE ILE B . n 
B 2 370  VAL 370  370  370  VAL VAL B . n 
B 2 371  HIS 371  371  371  HIS HIS B . n 
B 2 372  ALA 372  372  372  ALA ALA B . n 
B 2 373  LEU 373  373  373  LEU LEU B . n 
B 2 374  ALA 374  374  374  ALA ALA B . n 
B 2 375  HIS 375  375  375  HIS HIS B . n 
B 2 376  LEU 376  376  376  LEU LEU B . n 
B 2 377  ILE 377  377  377  ILE ILE B . n 
B 2 378  ASN 378  378  378  ASN ASN B . n 
B 2 379  ALA 379  379  379  ALA ALA B . n 
B 2 380  GLU 380  380  380  GLU GLU B . n 
B 2 381  LEU 381  381  381  LEU LEU B . n 
B 2 382  GLY 382  382  382  GLY GLY B . n 
B 2 383  ASN 383  383  383  ASN ASN B . n 
B 2 384  VAL 384  384  384  VAL VAL B . n 
B 2 385  GLY 385  385  385  GLY GLY B . n 
B 2 386  GLN 386  386  386  GLN GLN B . n 
B 2 387  THR 387  387  387  THR THR B . n 
B 2 388  VAL 388  388  388  VAL VAL B . n 
B 2 389  PHE 389  389  389  PHE PHE B . n 
B 2 390  TYR 390  390  390  TYR TYR B . n 
B 2 391  HIS 391  391  391  HIS HIS B . n 
B 2 392  GLU 392  392  392  GLU GLU B . n 
B 2 393  PRO 393  393  393  PRO PRO B . n 
B 2 394  VAL 394  394  394  VAL VAL B . n 
B 2 395  GLU 395  395  395  GLU GLU B . n 
B 2 396  ALA 396  396  396  ALA ALA B . n 
B 2 397  ARG 397  397  397  ARG ARG B . n 
B 2 398  PRO 398  398  398  PRO PRO B . n 
B 2 399  THR 399  399  399  THR THR B . n 
B 2 400  ASN 400  400  400  ASN ASN B . n 
B 2 401  GLN 401  401  401  GLN GLN B . n 
B 2 402  THR 402  402  402  THR THR B . n 
B 2 403  GLU 403  403  403  GLU GLU B . n 
B 2 404  GLU 404  404  404  GLU GLU B . n 
B 2 405  LEU 405  405  405  LEU LEU B . n 
B 2 406  VAL 406  406  406  VAL VAL B . n 
B 2 407  ALA 407  407  407  ALA ALA B . n 
B 2 408  LEU 408  408  408  LEU LEU B . n 
B 2 409  VAL 409  409  409  VAL VAL B . n 
B 2 410  SER 410  410  410  SER SER B . n 
B 2 411  GLU 411  411  411  GLU GLU B . n 
B 2 412  MET 412  412  412  MET MET B . n 
B 2 413  ALA 413  413  413  ALA ALA B . n 
B 2 414  ALA 414  414  414  ALA ALA B . n 
B 2 415  GLY 415  415  415  GLY GLY B . n 
B 2 416  ARG 416  416  416  ARG ARG B . n 
B 2 417  VAL 417  417  417  VAL VAL B . n 
B 2 418  GLU 418  418  418  GLU GLU B . n 
B 2 419  THR 419  419  419  THR THR B . n 
B 2 420  LEU 420  420  420  LEU LEU B . n 
B 2 421  ILE 421  421  421  ILE ILE B . n 
B 2 422  MET 422  422  422  MET MET B . n 
B 2 423  ILE 423  423  423  ILE ILE B . n 
B 2 424  GLY 424  424  424  GLY GLY B . n 
B 2 425  GLY 425  425  425  GLY GLY B . n 
B 2 426  ASN 426  426  426  ASN ASN B . n 
B 2 427  PRO 427  427  427  PRO PRO B . n 
B 2 428  VAL 428  428  428  VAL VAL B . n 
B 2 429  TYR 429  429  429  TYR TYR B . n 
B 2 430  ASN 430  430  430  ASN ASN B . n 
B 2 431  ALA 431  431  431  ALA ALA B . n 
B 2 432  PRO 432  432  432  PRO PRO B . n 
B 2 433  GLY 433  433  433  GLY GLY B . n 
B 2 434  ASP 434  434  434  ASP ASP B . n 
B 2 435  LEU 435  435  435  LEU LEU B . n 
B 2 436  ARG 436  436  436  ARG ARG B . n 
B 2 437  PHE 437  437  437  PHE PHE B . n 
B 2 438  ALA 438  438  438  ALA ALA B . n 
B 2 439  ASP 439  439  439  ASP ASP B . n 
B 2 440  ARG 440  440  440  ARG ARG B . n 
B 2 441  MET 441  441  441  MET MET B . n 
B 2 442  ALA 442  442  442  ALA ALA B . n 
B 2 443  SER 443  443  443  SER SER B . n 
B 2 444  VAL 444  444  444  VAL VAL B . n 
B 2 445  PRO 445  445  445  PRO PRO B . n 
B 2 446  LEU 446  446  446  LEU LEU B . n 
B 2 447  THR 447  447  447  THR THR B . n 
B 2 448  ILE 448  448  448  ILE ILE B . n 
B 2 449  HIS 449  449  449  HIS HIS B . n 
B 2 450  LEU 450  450  450  LEU LEU B . n 
B 2 451  SER 451  451  451  SER SER B . n 
B 2 452  GLN 452  452  452  GLN GLN B . n 
B 2 453  PHE 453  453  453  PHE PHE B . n 
B 2 454  VAL 454  454  454  VAL VAL B . n 
B 2 455  ASP 455  455  455  ASP ASP B . n 
B 2 456  GLU 456  456  456  GLU GLU B . n 
B 2 457  THR 457  457  457  THR THR B . n 
B 2 458  SER 458  458  458  SER SER B . n 
B 2 459  ALA 459  459  459  ALA ALA B . n 
B 2 460  ARG 460  460  460  ARG ARG B . n 
B 2 461  ALA 461  461  461  ALA ALA B . n 
B 2 462  THR 462  462  462  THR THR B . n 
B 2 463  TRP 463  463  463  TRP TRP B . n 
B 2 464  HIS 464  464  464  HIS HIS B . n 
B 2 465  ILE 465  465  465  ILE ILE B . n 
B 2 466  PRO 466  466  466  PRO PRO B . n 
B 2 467  GLN 467  467  467  GLN GLN B . n 
B 2 468  ALA 468  468  468  ALA ALA B . n 
B 2 469  HIS 469  469  469  HIS HIS B . n 
B 2 470  PRO 470  470  470  PRO PRO B . n 
B 2 471  LEU 471  471  471  LEU LEU B . n 
B 2 472  GLU 472  472  472  GLU GLU B . n 
B 2 473  SER 473  473  473  SER SER B . n 
B 2 474  TRP 474  474  474  TRP TRP B . n 
B 2 475  GLY 475  475  475  GLY GLY B . n 
B 2 476  ASP 476  476  476  ASP ASP B . n 
B 2 477  ALA 477  477  477  ALA ALA B . n 
B 2 478  ARG 478  478  478  ARG ARG B . n 
B 2 479  ALA 479  479  479  ALA ALA B . n 
B 2 480  PHE 480  480  480  PHE PHE B . n 
B 2 481  ASP 481  481  481  ASP ASP B . n 
B 2 482  GLY 482  482  482  GLY GLY B . n 
B 2 483  THR 483  483  483  THR THR B . n 
B 2 484  ALA 484  484  484  ALA ALA B . n 
B 2 485  SER 485  485  485  SER SER B . n 
B 2 486  ILE 486  486  486  ILE ILE B . n 
B 2 487  VAL 487  487  487  VAL VAL B . n 
B 2 488  GLN 488  488  488  GLN GLN B . n 
B 2 489  PRO 489  489  489  PRO PRO B . n 
B 2 490  LEU 490  490  490  LEU LEU B . n 
B 2 491  ILE 491  491  491  ILE ILE B . n 
B 2 492  GLU 492  492  492  GLU GLU B . n 
B 2 493  PRO 493  493  493  PRO PRO B . n 
B 2 494  LEU 494  494  494  LEU LEU B . n 
B 2 495  TYR 495  495  495  TYR TYR B . n 
B 2 496  GLY 496  496  496  GLY GLY B . n 
B 2 497  GLY 497  497  497  GLY GLY B . n 
B 2 498  LYS 498  498  498  LYS LYS B . n 
B 2 499  THR 499  499  499  THR THR B . n 
B 2 500  ALA 500  500  500  ALA ALA B . n 
B 2 501  ASN 501  501  501  ASN ASN B . n 
B 2 502  GLU 502  502  502  GLU GLU B . n 
B 2 503  LEU 503  503  503  LEU LEU B . n 
B 2 504  LEU 504  504  504  LEU LEU B . n 
B 2 505  ALA 505  505  505  ALA ALA B . n 
B 2 506  ALA 506  506  506  ALA ALA B . n 
B 2 507  MET 507  507  507  MET MET B . n 
B 2 508  LEU 508  508  508  LEU LEU B . n 
B 2 509  GLY 509  509  509  GLY GLY B . n 
B 2 510  GLN 510  510  510  GLN GLN B . n 
B 2 511  PRO 511  511  511  PRO PRO B . n 
B 2 512  GLU 512  512  512  GLU GLU B . n 
B 2 513  ALA 513  513  513  ALA ALA B . n 
B 2 514  GLU 514  514  514  GLU GLU B . n 
B 2 515  SER 515  515  515  SER SER B . n 
B 2 516  TYR 516  516  516  TYR TYR B . n 
B 2 517  ASP 517  517  517  ASP ASP B . n 
B 2 518  LEU 518  518  518  LEU LEU B . n 
B 2 519  VAL 519  519  519  VAL VAL B . n 
B 2 520  ARG 520  520  520  ARG ARG B . n 
B 2 521  SER 521  521  521  SER SER B . n 
B 2 522  PHE 522  522  522  PHE PHE B . n 
B 2 523  TRP 523  523  523  TRP TRP B . n 
B 2 524  LEU 524  524  524  LEU LEU B . n 
B 2 525  GLU 525  525  525  GLU GLU B . n 
B 2 526  GLN 526  526  526  GLN GLN B . n 
B 2 527  ILE 527  527  527  ILE ILE B . n 
B 2 528  GLY 528  528  528  GLY GLY B . n 
B 2 529  GLU 529  529  529  GLU GLU B . n 
B 2 530  THR 530  530  530  THR THR B . n 
B 2 531  GLY 531  531  531  GLY GLY B . n 
B 2 532  TRP 532  532  532  TRP TRP B . n 
B 2 533  GLN 533  533  533  GLN GLN B . n 
B 2 534  VAL 534  534  534  VAL VAL B . n 
B 2 535  ALA 535  535  535  ALA ALA B . n 
B 2 536  LEU 536  536  536  LEU LEU B . n 
B 2 537  ALA 537  537  537  ALA ALA B . n 
B 2 538  ASN 538  538  538  ASN ASN B . n 
B 2 539  GLY 539  539  539  GLY GLY B . n 
B 2 540  VAL 540  540  540  VAL VAL B . n 
B 2 541  ILE 541  541  541  ILE ILE B . n 
B 2 542  ALA 542  542  542  ALA ALA B . n 
B 2 543  GLU 543  543  543  GLU GLU B . n 
B 2 544  THR 544  544  544  THR THR B . n 
B 2 545  VAL 545  545  545  VAL VAL B . n 
B 2 546  ALA 546  546  546  ALA ALA B . n 
B 2 547  PRO 547  547  547  PRO PRO B . n 
B 2 548  VAL 548  548  548  VAL VAL B . n 
B 2 549  ILE 549  549  549  ILE ILE B . n 
B 2 550  GLU 550  550  550  GLU GLU B . n 
B 2 551  PRO 551  551  551  PRO PRO B . n 
B 2 552  THR 552  552  552  THR THR B . n 
B 2 553  LEU 553  553  553  LEU LEU B . n 
B 2 554  ASN 554  554  554  ASN ASN B . n 
B 2 555  GLU 555  555  555  GLU GLU B . n 
B 2 556  GLY 556  556  556  GLY GLY B . n 
B 2 557  ALA 557  557  557  ALA ALA B . n 
B 2 558  ILE 558  558  558  ILE ILE B . n 
B 2 559  ARG 559  559  559  ARG ARG B . n 
B 2 560  ALA 560  560  560  ALA ALA B . n 
B 2 561  THR 561  561  561  THR THR B . n 
B 2 562  PRO 562  562  562  PRO PRO B . n 
B 2 563  ILE 563  563  563  ILE ILE B . n 
B 2 564  PRO 564  564  564  PRO PRO B . n 
B 2 565  GLN 565  565  565  GLN GLN B . n 
B 2 566  PRO 566  566  566  PRO PRO B . n 
B 2 567  GLY 567  567  567  GLY GLY B . n 
B 2 568  ASP 568  568  568  ASP ASP B . n 
B 2 569  GLY 569  569  569  GLY GLY B . n 
B 2 570  VAL 570  570  570  VAL VAL B . n 
B 2 571  GLU 571  571  571  GLU GLU B . n 
B 2 572  ILE 572  572  572  ILE ILE B . n 
B 2 573  VAL 573  573  573  VAL VAL B . n 
B 2 574  PHE 574  574  574  PHE PHE B . n 
B 2 575  ARG 575  575  575  ARG ARG B . n 
B 2 576  PRO 576  576  576  PRO PRO B . n 
B 2 577  ASP 577  577  577  ASP ASP B . n 
B 2 578  PRO 578  578  578  PRO PRO B . n 
B 2 579  SER 579  579  579  SER SER B . n 
B 2 580  LEU 580  580  580  LEU LEU B . n 
B 2 581  PHE 581  581  581  PHE PHE B . n 
B 2 582  ASP 582  582  582  ASP ASP B . n 
B 2 583  GLY 583  583  583  GLY GLY B . n 
B 2 584  PHE 584  584  584  PHE PHE B . n 
B 2 585  TYR 585  585  585  TYR TYR B . n 
B 2 586  ALA 586  586  586  ALA ALA B . n 
B 2 587  ASN 587  587  587  ASN ASN B . n 
B 2 588  ASN 588  588  588  ASN ASN B . n 
B 2 589  GLY 589  589  589  GLY GLY B . n 
B 2 590  TRP 590  590  590  TRP TRP B . n 
B 2 591  LEU 591  591  591  LEU LEU B . n 
B 2 592  GLN 592  592  592  GLN GLN B . n 
B 2 593  GLU 593  593  593  GLU GLU B . n 
B 2 594  LEU 594  594  594  LEU LEU B . n 
B 2 595  PRO 595  595  595  PRO PRO B . n 
B 2 596  ARG 596  596  596  ARG ARG B . n 
B 2 597  PRO 597  597  597  PRO PRO B . n 
B 2 598  LEU 598  598  598  LEU LEU B . n 
B 2 599  THR 599  599  599  THR THR B . n 
B 2 600  LYS 600  600  600  LYS LYS B . n 
B 2 601  LEU 601  601  601  LEU LEU B . n 
B 2 602  VAL 602  602  602  VAL VAL B . n 
B 2 603  TRP 603  603  603  TRP TRP B . n 
B 2 604  ASP 604  604  604  ASP ASP B . n 
B 2 605  ASN 605  605  605  ASN ASN B . n 
B 2 606  ALA 606  606  606  ALA ALA B . n 
B 2 607  ALA 607  607  607  ALA ALA B . n 
B 2 608  LEU 608  608  608  LEU LEU B . n 
B 2 609  MET 609  609  609  MET MET B . n 
B 2 610  SER 610  610  610  SER SER B . n 
B 2 611  PRO 611  611  611  PRO PRO B . n 
B 2 612  ARG 612  612  612  ARG ARG B . n 
B 2 613  THR 613  613  613  THR THR B . n 
B 2 614  ALA 614  614  614  ALA ALA B . n 
B 2 615  ILE 615  615  615  ILE ILE B . n 
B 2 616  LYS 616  616  616  LYS LYS B . n 
B 2 617  LEU 617  617  617  LEU LEU B . n 
B 2 618  LEU 618  618  618  LEU LEU B . n 
B 2 619  GLY 619  619  619  GLY GLY B . n 
B 2 620  LEU 620  620  620  LEU LEU B . n 
B 2 621  PRO 621  621  621  PRO PRO B . n 
B 2 622  PHE 622  622  622  PHE PHE B . n 
B 2 623  ASN 623  623  623  ASN ASN B . n 
B 2 624  ALA 624  624  624  ALA ALA B . n 
B 2 625  ASP 625  625  625  ASP ASP B . n 
B 2 626  ARG 626  626  626  ARG ARG B . n 
B 2 627  LEU 627  627  627  LEU LEU B . n 
B 2 628  ILE 628  628  628  ILE ILE B . n 
B 2 629  GLY 629  629  629  GLY GLY B . n 
B 2 630  THR 630  630  630  THR THR B . n 
B 2 631  GLU 631  631  631  GLU GLU B . n 
B 2 632  ALA 632  632  632  ALA ALA B . n 
B 2 633  ASP 633  633  633  ASP ASP B . n 
B 2 634  ASP 634  634  634  ASP ASP B . n 
B 2 635  ARG 635  635  635  ARG ARG B . n 
B 2 636  GLU 636  636  636  GLU GLU B . n 
B 2 637  ARG 637  637  637  ARG ARG B . n 
B 2 638  GLN 638  638  638  GLN GLN B . n 
B 2 639  GLN 639  639  639  GLN GLN B . n 
B 2 640  TYR 640  640  640  TYR TYR B . n 
B 2 641  LEU 641  641  641  LEU LEU B . n 
B 2 642  GLU 642  642  642  GLU GLU B . n 
B 2 643  GLN 643  643  643  GLN GLN B . n 
B 2 644  LEU 644  644  644  LEU LEU B . n 
B 2 645  SER 645  645  645  SER SER B . n 
B 2 646  LYS 646  646  646  LYS LYS B . n 
B 2 647  VAL 647  647  647  VAL VAL B . n 
B 2 648  ASN 648  648  648  ASN ASN B . n 
B 2 649  GLY 649  649  649  GLY GLY B . n 
B 2 650  THR 650  650  650  THR THR B . n 
B 2 651  ILE 651  651  651  ILE ILE B . n 
B 2 652  ALA 652  652  652  ALA ALA B . n 
B 2 653  ARG 653  653  653  ARG ARG B . n 
B 2 654  ILE 654  654  654  ILE ILE B . n 
B 2 655  GLU 655  655  655  GLU GLU B . n 
B 2 656  TYR 656  656  656  TYR TYR B . n 
B 2 657  ARG 657  657  657  ARG ARG B . n 
B 2 658  GLY 658  658  658  GLY GLY B . n 
B 2 659  GLY 659  659  659  GLY GLY B . n 
B 2 660  ILE 660  660  660  ILE ILE B . n 
B 2 661  ILE 661  661  661  ILE ILE B . n 
B 2 662  GLU 662  662  662  GLU GLU B . n 
B 2 663  ILE 663  663  663  ILE ILE B . n 
B 2 664  PRO 664  664  664  PRO PRO B . n 
B 2 665  ILE 665  665  665  ILE ILE B . n 
B 2 666  TRP 666  666  666  TRP TRP B . n 
B 2 667  LEU 667  667  667  LEU LEU B . n 
B 2 668  LEU 668  668  668  LEU LEU B . n 
B 2 669  PRO 669  669  669  PRO PRO B . n 
B 2 670  GLY 670  670  670  GLY GLY B . n 
B 2 671  HIS 671  671  671  HIS HIS B . n 
B 2 672  ALA 672  672  672  ALA ALA B . n 
B 2 673  GLU 673  673  673  GLU GLU B . n 
B 2 674  ASP 674  674  674  ASP ASP B . n 
B 2 675  SER 675  675  675  SER SER B . n 
B 2 676  ILE 676  676  676  ILE ILE B . n 
B 2 677  THR 677  677  677  THR THR B . n 
B 2 678  LEU 678  678  678  LEU LEU B . n 
B 2 679  ASN 679  679  679  ASN ASN B . n 
B 2 680  LEU 680  680  680  LEU LEU B . n 
B 2 681  GLY 681  681  681  GLY GLY B . n 
B 2 682  TYR 682  682  682  TYR TYR B . n 
B 2 683  GLY 683  683  683  GLY GLY B . n 
B 2 684  ARG 684  684  684  ARG ARG B . n 
B 2 685  THR 685  685  685  THR THR B . n 
B 2 686  HIS 686  686  686  HIS HIS B . n 
B 2 687  ALA 687  687  687  ALA ALA B . n 
B 2 688  GLY 688  688  688  GLY GLY B . n 
B 2 689  ARG 689  689  689  ARG ARG B . n 
B 2 690  VAL 690  690  690  VAL VAL B . n 
B 2 691  GLY 691  691  691  GLY GLY B . n 
B 2 692  ASN 692  692  692  ASN ASN B . n 
B 2 693  ASN 693  693  693  ASN ASN B . n 
B 2 694  VAL 694  694  694  VAL VAL B . n 
B 2 695  GLY 695  695  695  GLY GLY B . n 
B 2 696  ILE 696  696  696  ILE ILE B . n 
B 2 697  ASP 697  697  697  ASP ASP B . n 
B 2 698  VAL 698  698  698  VAL VAL B . n 
B 2 699  TYR 699  699  699  TYR TYR B . n 
B 2 700  PRO 700  700  700  PRO PRO B . n 
B 2 701  ILE 701  701  701  ILE ILE B . n 
B 2 702  ARG 702  702  702  ARG ARG B . n 
B 2 703  THR 703  703  703  THR THR B . n 
B 2 704  SER 704  704  704  SER SER B . n 
B 2 705  ASP 705  705  705  ASP ASP B . n 
B 2 706  SER 706  706  706  SER SER B . n 
B 2 707  PRO 707  707  707  PRO PRO B . n 
B 2 708  TRP 708  708  708  TRP TRP B . n 
B 2 709  PHE 709  709  709  PHE PHE B . n 
B 2 710  GLY 710  710  710  GLY GLY B . n 
B 2 711  ALA 711  711  711  ALA ALA B . n 
B 2 712  GLY 712  712  712  GLY GLY B . n 
B 2 713  ALA 713  713  713  ALA ALA B . n 
B 2 714  ARG 714  714  714  ARG ARG B . n 
B 2 715  VAL 715  715  715  VAL VAL B . n 
B 2 716  THR 716  716  716  THR THR B . n 
B 2 717  ASN 717  717  717  ASN ASN B . n 
B 2 718  THR 718  718  718  THR THR B . n 
B 2 719  GLY 719  719  719  GLY GLY B . n 
B 2 720  ARG 720  720  720  ARG ARG B . n 
B 2 721  THR 721  721  721  THR THR B . n 
B 2 722  TYR 722  722  722  TYR TYR B . n 
B 2 723  LEU 723  723  723  LEU LEU B . n 
B 2 724  LEU 724  724  724  LEU LEU B . n 
B 2 725  VAL 725  725  725  VAL VAL B . n 
B 2 726  SER 726  726  726  SER SER B . n 
B 2 727  THR 727  727  727  THR THR B . n 
B 2 728  GLN 728  728  728  GLN GLN B . n 
B 2 729  ASP 729  729  729  ASP ASP B . n 
B 2 730  HIS 730  730  730  HIS HIS B . n 
B 2 731  TRP 731  731  731  TRP TRP B . n 
B 2 732  THR 732  732  732  THR THR B . n 
B 2 733  LEU 733  733  733  LEU LEU B . n 
B 2 734  GLU 734  734  734  GLU GLU B . n 
B 2 735  GLY 735  735  735  GLY GLY B . n 
B 2 736  ARG 736  736  736  ARG ARG B . n 
B 2 737  ASP 737  737  737  ASP ASP B . n 
B 2 738  ILE 738  738  738  ILE ILE B . n 
B 2 739  TYR 739  739  739  TYR TYR B . n 
B 2 740  ARG 740  740  740  ARG ARG B . n 
B 2 741  VAL 741  741  741  VAL VAL B . n 
B 2 742  GLY 742  742  742  GLY GLY B . n 
B 2 743  GLU 743  743  743  GLU GLU B . n 
B 2 744  PHE 744  744  744  PHE PHE B . n 
B 2 745  LYS 745  745  745  LYS LYS B . n 
B 2 746  LYS 746  746  746  LYS LYS B . n 
B 2 747  PHE 747  747  747  PHE PHE B . n 
B 2 748  LYS 748  748  748  LYS LYS B . n 
B 2 749  GLU 749  749  749  GLU GLU B . n 
B 2 750  ASP 750  750  750  ASP ASP B . n 
B 2 751  PRO 751  751  751  PRO PRO B . n 
B 2 752  LYS 752  752  752  LYS LYS B . n 
B 2 753  TYR 753  753  753  TYR TYR B . n 
B 2 754  ILE 754  754  754  ILE ILE B . n 
B 2 755  ALA 755  755  755  ALA ALA B . n 
B 2 756  LYS 756  756  756  LYS LYS B . n 
B 2 757  GLU 757  757  757  GLU GLU B . n 
B 2 758  VAL 758  758  758  VAL VAL B . n 
B 2 759  TYR 759  759  759  TYR TYR B . n 
B 2 760  GLN 760  760  760  GLN GLN B . n 
B 2 761  GLU 761  761  761  GLU GLU B . n 
B 2 762  GLU 762  762  762  GLU GLU B . n 
B 2 763  TYR 763  763  763  TYR TYR B . n 
B 2 764  GLY 764  764  764  GLY GLY B . n 
B 2 765  ARG 765  765  765  ARG ARG B . n 
B 2 766  GLU 766  766  766  GLU GLU B . n 
B 2 767  THR 767  767  767  THR THR B . n 
B 2 768  PRO 768  768  768  PRO PRO B . n 
B 2 769  ASN 769  769  769  ASN ASN B . n 
B 2 770  TYR 770  770  770  TYR TYR B . n 
B 2 771  GLN 771  771  771  GLN GLN B . n 
B 2 772  SER 772  772  772  SER SER B . n 
B 2 773  LEU 773  773  773  LEU LEU B . n 
B 2 774  GLN 774  774  774  GLN GLN B . n 
B 2 775  PRO 775  775  775  PRO PRO B . n 
B 2 776  GLY 776  776  776  GLY GLY B . n 
B 2 777  ASP 777  777  777  ASP ASP B . n 
B 2 778  ASP 778  778  778  ASP ASP B . n 
B 2 779  TYR 779  779  779  TYR TYR B . n 
B 2 780  THR 780  780  780  THR THR B . n 
B 2 781  GLY 781  781  781  GLY GLY B . n 
B 2 782  ARG 782  782  782  ARG ARG B . n 
B 2 783  ASN 783  783  783  ASN ASN B . n 
B 2 784  ALA 784  784  784  ALA ALA B . n 
B 2 785  TRP 785  785  785  TRP TRP B . n 
B 2 786  GLY 786  786  786  GLY GLY B . n 
B 2 787  MET 787  787  787  MET MET B . n 
B 2 788  THR 788  788  788  THR THR B . n 
B 2 789  ILE 789  789  789  ILE ILE B . n 
B 2 790  ASN 790  790  790  ASN ASN B . n 
B 2 791  LEU 791  791  791  LEU LEU B . n 
B 2 792  ASN 792  792  792  ASN ASN B . n 
B 2 793  ALA 793  793  793  ALA ALA B . n 
B 2 794  CYS 794  794  794  CYS CYS B . n 
B 2 795  ILE 795  795  795  ILE ILE B . n 
B 2 796  GLY 796  796  796  GLY GLY B . n 
B 2 797  CYS 797  797  797  CYS CYS B . n 
B 2 798  ASN 798  798  798  ASN ASN B . n 
B 2 799  ALA 799  799  799  ALA ALA B . n 
B 2 800  CYS 800  800  800  CYS CYS B . n 
B 2 801  VAL 801  801  801  VAL VAL B . n 
B 2 802  VAL 802  802  802  VAL VAL B . n 
B 2 803  ALA 803  803  803  ALA ALA B . n 
B 2 804  CYS 804  804  804  CYS CYS B . n 
B 2 805  GLN 805  805  805  GLN GLN B . n 
B 2 806  ALA 806  806  806  ALA ALA B . n 
B 2 807  GLU 807  807  807  GLU GLU B . n 
B 2 808  ASN 808  808  808  ASN ASN B . n 
B 2 809  ASN 809  809  809  ASN ASN B . n 
B 2 810  ILE 810  810  810  ILE ILE B . n 
B 2 811  ALA 811  811  811  ALA ALA B . n 
B 2 812  VAL 812  812  812  VAL VAL B . n 
B 2 813  VAL 813  813  813  VAL VAL B . n 
B 2 814  GLY 814  814  814  GLY GLY B . n 
B 2 815  LYS 815  815  815  LYS LYS B . n 
B 2 816  ASP 816  816  816  ASP ASP B . n 
B 2 817  GLN 817  817  817  GLN GLN B . n 
B 2 818  VAL 818  818  818  VAL VAL B . n 
B 2 819  SER 819  819  819  SER SER B . n 
B 2 820  ARG 820  820  820  ARG ARG B . n 
B 2 821  GLY 821  821  821  GLY GLY B . n 
B 2 822  ARG 822  822  822  ARG ARG B . n 
B 2 823  GLU 823  823  823  GLU GLU B . n 
B 2 824  MET 824  824  824  MET MET B . n 
B 2 825  HIS 825  825  825  HIS HIS B . n 
B 2 826  TRP 826  826  826  TRP TRP B . n 
B 2 827  ILE 827  827  827  ILE ILE B . n 
B 2 828  ARG 828  828  828  ARG ARG B . n 
B 2 829  ILE 829  829  829  ILE ILE B . n 
B 2 830  ASP 830  830  830  ASP ASP B . n 
B 2 831  ARG 831  831  831  ARG ARG B . n 
B 2 832  TYR 832  832  832  TYR TYR B . n 
B 2 833  PHE 833  833  833  PHE PHE B . n 
B 2 834  ALA 834  834  834  ALA ALA B . n 
B 2 835  GLY 835  835  835  GLY GLY B . n 
B 2 836  GLU 836  836  836  GLU GLU B . n 
B 2 837  ASP 837  837  837  ASP ASP B . n 
B 2 838  LEU 838  838  838  LEU LEU B . n 
B 2 839  ASP 839  839  839  ASP ASP B . n 
B 2 840  ASN 840  840  840  ASN ASN B . n 
B 2 841  PRO 841  841  841  PRO PRO B . n 
B 2 842  SER 842  842  842  SER SER B . n 
B 2 843  ILE 843  843  843  ILE ILE B . n 
B 2 844  TYR 844  844  844  TYR TYR B . n 
B 2 845  MET 845  845  845  MET MET B . n 
B 2 846  MET 846  846  846  MET MET B . n 
B 2 847  PRO 847  847  847  PRO PRO B . n 
B 2 848  VAL 848  848  848  VAL VAL B . n 
B 2 849  ASN 849  849  849  ASN ASN B . n 
B 2 850  CYS 850  850  850  CYS CYS B . n 
B 2 851  MET 851  851  851  MET MET B . n 
B 2 852  GLN 852  852  852  GLN GLN B . n 
B 2 853  CYS 853  853  853  CYS CYS B . n 
B 2 854  GLU 854  854  854  GLU GLU B . n 
B 2 855  LYS 855  855  855  LYS LYS B . n 
B 2 856  ALA 856  856  856  ALA ALA B . n 
B 2 857  PRO 857  857  857  PRO PRO B . n 
B 2 858  CYS 858  858  858  CYS CYS B . n 
B 2 859  GLU 859  859  859  GLU GLU B . n 
B 2 860  VAL 860  860  860  VAL VAL B . n 
B 2 861  VAL 861  861  861  VAL VAL B . n 
B 2 862  CYS 862  862  862  CYS CYS B . n 
B 2 863  PRO 863  863  863  PRO PRO B . n 
B 2 864  VAL 864  864  864  VAL VAL B . n 
B 2 865  ALA 865  865  865  ALA ALA B . n 
B 2 866  ALA 866  866  866  ALA ALA B . n 
B 2 867  THR 867  867  867  THR THR B . n 
B 2 868  VAL 868  868  868  VAL VAL B . n 
B 2 869  HIS 869  869  869  HIS HIS B . n 
B 2 870  ASP 870  870  870  ASP ASP B . n 
B 2 871  TYR 871  871  871  TYR TYR B . n 
B 2 872  GLU 872  872  872  GLU GLU B . n 
B 2 873  GLY 873  873  873  GLY GLY B . n 
B 2 874  LEU 874  874  874  LEU LEU B . n 
B 2 875  ASN 875  875  875  ASN ASN B . n 
B 2 876  ASN 876  876  876  ASN ASN B . n 
B 2 877  MET 877  877  877  MET MET B . n 
B 2 878  VAL 878  878  878  VAL VAL B . n 
B 2 879  TYR 879  879  879  TYR TYR B . n 
B 2 880  ASN 880  880  880  ASN ASN B . n 
B 2 881  ARG 881  881  881  ARG ARG B . n 
B 2 882  CYS 882  882  882  CYS CYS B . n 
B 2 883  VAL 883  883  883  VAL VAL B . n 
B 2 884  GLY 884  884  884  GLY GLY B . n 
B 2 885  THR 885  885  885  THR THR B . n 
B 2 886  LYS 886  886  886  LYS LYS B . n 
B 2 887  TYR 887  887  887  TYR TYR B . n 
B 2 888  CYS 888  888  888  CYS CYS B . n 
B 2 889  SER 889  889  889  SER SER B . n 
B 2 890  ASN 890  890  890  ASN ASN B . n 
B 2 891  ASN 891  891  891  ASN ASN B . n 
B 2 892  CYS 892  892  892  CYS CYS B . n 
B 2 893  PRO 893  893  893  PRO PRO B . n 
B 2 894  TYR 894  894  894  TYR TYR B . n 
B 2 895  LYS 895  895  895  LYS LYS B . n 
B 2 896  VAL 896  896  896  VAL VAL B . n 
B 2 897  ARG 897  897  897  ARG ARG B . n 
B 2 898  ARG 898  898  898  ARG ARG B . n 
B 2 899  PHE 899  899  899  PHE PHE B . n 
B 2 900  ASN 900  900  900  ASN ASN B . n 
B 2 901  PHE 901  901  901  PHE PHE B . n 
B 2 902  LEU 902  902  902  LEU LEU B . n 
B 2 903  GLN 903  903  903  GLN GLN B . n 
B 2 904  TYR 904  904  904  TYR TYR B . n 
B 2 905  SER 905  905  905  SER SER B . n 
B 2 906  ASP 906  906  906  ASP ASP B . n 
B 2 907  THR 907  907  907  THR THR B . n 
B 2 908  THR 908  908  908  THR THR B . n 
B 2 909  THR 909  909  909  THR THR B . n 
B 2 910  GLU 910  910  910  GLU GLU B . n 
B 2 911  THR 911  911  911  THR THR B . n 
B 2 912  PHE 912  912  912  PHE PHE B . n 
B 2 913  LYS 913  913  913  LYS LYS B . n 
B 2 914  LEU 914  914  914  LEU LEU B . n 
B 2 915  ALA 915  915  915  ALA ALA B . n 
B 2 916  PHE 916  916  916  PHE PHE B . n 
B 2 917  ASN 917  917  917  ASN ASN B . n 
B 2 918  PRO 918  918  918  PRO PRO B . n 
B 2 919  ASP 919  919  919  ASP ASP B . n 
B 2 920  VAL 920  920  920  VAL VAL B . n 
B 2 921  THR 921  921  921  THR THR B . n 
B 2 922  VAL 922  922  922  VAL VAL B . n 
B 2 923  ARG 923  923  923  ARG ARG B . n 
B 2 924  ILE 924  924  924  ILE ILE B . n 
B 2 925  ARG 925  925  925  ARG ARG B . n 
B 2 926  GLY 926  926  926  GLY GLY B . n 
B 2 927  VAL 927  927  927  VAL VAL B . n 
B 2 928  MET 928  928  928  MET MET B . n 
B 2 929  GLU 929  929  929  GLU GLU B . n 
B 2 930  LYS 930  930  930  LYS LYS B . n 
B 2 931  CYS 931  931  931  CYS CYS B . n 
B 2 932  THR 932  932  932  THR THR B . n 
B 2 933  TYR 933  933  933  TYR TYR B . n 
B 2 934  CYS 934  934  934  CYS CYS B . n 
B 2 935  VAL 935  935  935  VAL VAL B . n 
B 2 936  GLN 936  936  936  GLN GLN B . n 
B 2 937  ARG 937  937  937  ARG ARG B . n 
B 2 938  ILE 938  938  938  ILE ILE B . n 
B 2 939  SER 939  939  939  SER SER B . n 
B 2 940  GLY 940  940  940  GLY GLY B . n 
B 2 941  ALA 941  941  941  ALA ALA B . n 
B 2 942  ARG 942  942  942  ARG ARG B . n 
B 2 943  ILE 943  943  943  ILE ILE B . n 
B 2 944  ALA 944  944  944  ALA ALA B . n 
B 2 945  ALA 945  945  945  ALA ALA B . n 
B 2 946  LYS 946  946  946  LYS LYS B . n 
B 2 947  ARG 947  947  947  ARG ARG B . n 
B 2 948  ALA 948  948  948  ALA ALA B . n 
B 2 949  ALA 949  949  949  ALA ALA B . n 
B 2 950  VAL 950  950  950  VAL VAL B . n 
B 2 951  GLN 951  951  951  GLN GLN B . n 
B 2 952  ALA 952  952  952  ALA ALA B . n 
B 2 953  GLY 953  953  953  GLY GLY B . n 
B 2 954  GLN 954  954  954  GLN GLN B . n 
B 2 955  SER 955  955  955  SER SER B . n 
B 2 956  SER 956  956  956  SER SER B . n 
B 2 957  TYR 957  957  957  TYR TYR B . n 
B 2 958  VAL 958  958  958  VAL VAL B . n 
B 2 959  ILE 959  959  959  ILE ILE B . n 
B 2 960  SER 960  960  960  SER SER B . n 
B 2 961  ASP 961  961  961  ASP ASP B . n 
B 2 962  GLY 962  962  962  GLY GLY B . n 
B 2 963  ALA 963  963  963  ALA ALA B . n 
B 2 964  ILE 964  964  964  ILE ILE B . n 
B 2 965  GLN 965  965  965  GLN GLN B . n 
B 2 966  THR 966  966  966  THR THR B . n 
B 2 967  ALA 967  967  967  ALA ALA B . n 
B 2 968  CYS 968  968  968  CYS CYS B . n 
B 2 969  GLU 969  969  969  GLU GLU B . n 
B 2 970  GLN 970  970  970  GLN GLN B . n 
B 2 971  ALA 971  971  971  ALA ALA B . n 
B 2 972  CYS 972  972  972  CYS CYS B . n 
B 2 973  PRO 973  973  973  PRO PRO B . n 
B 2 974  THR 974  974  974  THR THR B . n 
B 2 975  GLY 975  975  975  GLY GLY B . n 
B 2 976  ALA 976  976  976  ALA ALA B . n 
B 2 977  ILE 977  977  977  ILE ILE B . n 
B 2 978  VAL 978  978  978  VAL VAL B . n 
B 2 979  PHE 979  979  979  PHE PHE B . n 
B 2 980  GLY 980  980  980  GLY GLY B . n 
B 2 981  ASP 981  981  981  ASP ASP B . n 
B 2 982  ILE 982  982  982  ILE ILE B . n 
B 2 983  ASN 983  983  983  ASN ASN B . n 
B 2 984  ASP 984  984  984  ASP ASP B . n 
B 2 985  SER 985  985  985  SER SER B . n 
B 2 986  ASN 986  986  986  ASN ASN B . n 
B 2 987  SER 987  987  987  SER SER B . n 
B 2 988  ARG 988  988  988  ARG ARG B . n 
B 2 989  VAL 989  989  989  VAL VAL B . n 
B 2 990  ALA 990  990  990  ALA ALA B . n 
B 2 991  LYS 991  991  991  LYS LYS B . n 
B 2 992  TRP 992  992  992  TRP TRP B . n 
B 2 993  LYS 993  993  993  LYS LYS B . n 
B 2 994  ALA 994  994  994  ALA ALA B . n 
B 2 995  GLU 995  995  995  GLU GLU B . n 
B 2 996  GLY 996  996  996  GLY GLY B . n 
B 2 997  HIS 997  997  997  HIS HIS B . n 
B 2 998  ASN 998  998  998  ASN ASN B . n 
B 2 999  TYR 999  999  999  TYR TYR B . n 
B 2 1000 GLY 1000 1000 1000 GLY GLY B . n 
B 2 1001 LEU 1001 1001 1001 LEU LEU B . n 
B 2 1002 LEU 1002 1002 1002 LEU LEU B . n 
B 2 1003 GLY 1003 1003 1003 GLY GLY B . n 
B 2 1004 PHE 1004 1004 1004 PHE PHE B . n 
B 2 1005 LEU 1005 1005 1005 LEU LEU B . n 
B 2 1006 ASN 1006 1006 1006 ASN ASN B . n 
B 2 1007 THR 1007 1007 1007 THR THR B . n 
B 2 1008 VAL 1008 1008 1008 VAL VAL B . n 
B 2 1009 PRO 1009 1009 1009 PRO PRO B . n 
B 2 1010 ARG 1010 1010 1010 ARG ARG B . n 
B 2 1011 THR 1011 1011 1011 THR THR B . n 
B 2 1012 THR 1012 1012 1012 THR THR B . n 
B 2 1013 TYR 1013 1013 1013 TYR TYR B . n 
B 2 1014 LEU 1014 1014 1014 LEU LEU B . n 
B 2 1015 ALA 1015 1015 1015 ALA ALA B . n 
B 2 1016 ARG 1016 1016 1016 ARG ARG B . n 
B 2 1017 VAL 1017 1017 1017 VAL VAL B . n 
B 2 1018 ARG 1018 1018 1018 ARG ARG B . n 
B 2 1019 ASN 1019 1019 1019 ASN ASN B . n 
B 2 1020 PRO 1020 1020 1020 PRO PRO B . n 
B 2 1021 SER 1021 1021 1021 SER SER B . n 
B 2 1022 GLU 1022 1022 1022 GLU GLU B . n 
B 2 1023 GLU 1023 1023 1023 GLU GLU B . n 
B 2 1024 LEU 1024 1024 1024 LEU LEU B . n 
B 2 1025 GLU 1025 1025 1025 GLU GLU B . n 
B 2 1026 LYS 1026 1026 1026 LYS LYS B . n 
B 2 1027 VAL 1027 1027 ?    ?   ?   B . n 
B 2 1028 GLU 1028 1028 ?    ?   ?   B . n 
B 2 1029 GLY 1029 1029 ?    ?   ?   B . n 
C 3 1    MET 1    1    ?    ?   ?   C . n 
C 3 2    ALA 2    2    ?    ?   ?   C . n 
C 3 3    GLN 3    3    ?    ?   ?   C . n 
C 3 4    ALA 4    4    ?    ?   ?   C . n 
C 3 5    GLN 5    5    ?    ?   ?   C . n 
C 3 6    PRO 6    6    ?    ?   ?   C . n 
C 3 7    LEU 7    7    ?    ?   ?   C . n 
C 3 8    ARG 8    8    ?    ?   ?   C . n 
C 3 9    THR 9    9    ?    ?   ?   C . n 
C 3 10   ARG 10   10   ?    ?   ?   C . n 
C 3 11   PRO 11   11   ?    ?   ?   C . n 
C 3 12   GLN 12   12   ?    ?   ?   C . n 
C 3 13   ASP 13   13   ?    ?   ?   C . n 
C 3 14   ASP 14   14   ?    ?   ?   C . n 
C 3 15   GLY 15   15   ?    ?   ?   C . n 
C 3 16   GLU 16   16   16   GLU GLU C . n 
C 3 17   ALA 17   17   17   ALA ALA C . n 
C 3 18   TYR 18   18   18   TYR TYR C . n 
C 3 19   LEU 19   19   19   LEU LEU C . n 
C 3 20   LEU 20   20   20   LEU LEU C . n 
C 3 21   PRO 21   21   21   PRO PRO C . n 
C 3 22   GLY 22   22   22   GLY GLY C . n 
C 3 23   GLU 23   23   23   GLU GLU C . n 
C 3 24   THR 24   24   24   THR THR C . n 
C 3 25   TYR 25   25   25   TYR TYR C . n 
C 3 26   THR 26   26   26   THR THR C . n 
C 3 27   SER 27   27   27   SER SER C . n 
C 3 28   ILE 28   28   28   ILE ILE C . n 
C 3 29   SER 29   29   29   SER SER C . n 
C 3 30   ALA 30   30   30   ALA ALA C . n 
C 3 31   LYS 31   31   31   LYS LYS C . n 
C 3 32   ILE 32   32   32   ILE ILE C . n 
C 3 33   GLY 33   33   33   GLY GLY C . n 
C 3 34   ASP 34   34   34   ASP ASP C . n 
C 3 35   VAL 35   35   35   VAL VAL C . n 
C 3 36   PRO 36   36   36   PRO PRO C . n 
C 3 37   LEU 37   37   37   LEU LEU C . n 
C 3 38   THR 38   38   38   THR THR C . n 
C 3 39   PRO 39   39   39   PRO PRO C . n 
C 3 40   PRO 40   40   40   PRO PRO C . n 
C 3 41   LEU 41   41   41   LEU LEU C . n 
C 3 42   LYS 42   42   42   LYS LYS C . n 
C 3 43   THR 43   43   43   THR THR C . n 
C 3 44   PRO 44   44   44   PRO PRO C . n 
C 3 45   LYS 45   45   45   LYS LYS C . n 
C 3 46   GLY 46   46   46   GLY GLY C . n 
C 3 47   TRP 47   47   47   TRP TRP C . n 
C 3 48   LEU 48   48   48   LEU LEU C . n 
C 3 49   ALA 49   49   49   ALA ALA C . n 
C 3 50   GLY 50   50   50   GLY GLY C . n 
C 3 51   PHE 51   51   51   PHE PHE C . n 
C 3 52   SER 52   52   52   SER SER C . n 
C 3 53   VAL 53   53   53   VAL VAL C . n 
C 3 54   ALA 54   54   54   ALA ALA C . n 
C 3 55   PHE 55   55   55   PHE PHE C . n 
C 3 56   PHE 56   56   56   PHE PHE C . n 
C 3 57   MET 57   57   57   MET MET C . n 
C 3 58   LEU 58   58   58   LEU LEU C . n 
C 3 59   MET 59   59   59   MET MET C . n 
C 3 60   ILE 60   60   60   ILE ILE C . n 
C 3 61   PHE 61   61   61   PHE PHE C . n 
C 3 62   PHE 62   62   62   PHE PHE C . n 
C 3 63   VAL 63   63   63   VAL VAL C . n 
C 3 64   SER 64   64   64   SER SER C . n 
C 3 65   VAL 65   65   65   VAL VAL C . n 
C 3 66   THR 66   66   66   THR THR C . n 
C 3 67   TRP 67   67   67   TRP TRP C . n 
C 3 68   LEU 68   68   68   LEU LEU C . n 
C 3 69   PHE 69   69   69   PHE PHE C . n 
C 3 70   ILE 70   70   70   ILE ILE C . n 
C 3 71   ARG 71   71   71   ARG ARG C . n 
C 3 72   GLY 72   72   72   GLY GLY C . n 
C 3 73   VAL 73   73   73   VAL VAL C . n 
C 3 74   GLY 74   74   74   GLY GLY C . n 
C 3 75   ILE 75   75   75   ILE ILE C . n 
C 3 76   TRP 76   76   76   TRP TRP C . n 
C 3 77   GLY 77   77   77   GLY GLY C . n 
C 3 78   ILE 78   78   78   ILE ILE C . n 
C 3 79   ASN 79   79   79   ASN ASN C . n 
C 3 80   ILE 80   80   80   ILE ILE C . n 
C 3 81   PRO 81   81   81   PRO PRO C . n 
C 3 82   VAL 82   82   82   VAL VAL C . n 
C 3 83   GLY 83   83   83   GLY GLY C . n 
C 3 84   TRP 84   84   84   TRP TRP C . n 
C 3 85   GLY 85   85   85   GLY GLY C . n 
C 3 86   MET 86   86   86   MET MET C . n 
C 3 87   ASP 87   87   87   ASP ASP C . n 
C 3 88   ILE 88   88   88   ILE ILE C . n 
C 3 89   ILE 89   89   89   ILE ILE C . n 
C 3 90   ASN 90   90   90   ASN ASN C . n 
C 3 91   PHE 91   91   91   PHE PHE C . n 
C 3 92   VAL 92   92   92   VAL VAL C . n 
C 3 93   TRP 93   93   93   TRP TRP C . n 
C 3 94   TRP 94   94   94   TRP TRP C . n 
C 3 95   ILE 95   95   95   ILE ILE C . n 
C 3 96   GLY 96   96   96   GLY GLY C . n 
C 3 97   ILE 97   97   97   ILE ILE C . n 
C 3 98   GLY 98   98   98   GLY GLY C . n 
C 3 99   HIS 99   99   99   HIS HIS C . n 
C 3 100  ALA 100  100  100  ALA ALA C . n 
C 3 101  GLY 101  101  101  GLY GLY C . n 
C 3 102  THR 102  102  102  THR THR C . n 
C 3 103  LEU 103  103  103  LEU LEU C . n 
C 3 104  ILE 104  104  104  ILE ILE C . n 
C 3 105  SER 105  105  105  SER SER C . n 
C 3 106  ALA 106  106  106  ALA ALA C . n 
C 3 107  ILE 107  107  107  ILE ILE C . n 
C 3 108  LEU 108  108  108  LEU LEU C . n 
C 3 109  LEU 109  109  109  LEU LEU C . n 
C 3 110  LEU 110  110  110  LEU LEU C . n 
C 3 111  LEU 111  111  111  LEU LEU C . n 
C 3 112  ASN 112  112  112  ASN ASN C . n 
C 3 113  GLN 113  113  113  GLN GLN C . n 
C 3 114  GLY 114  114  114  GLY GLY C . n 
C 3 115  TRP 115  115  115  TRP TRP C . n 
C 3 116  ARG 116  116  116  ARG ARG C . n 
C 3 117  ASN 117  117  117  ASN ASN C . n 
C 3 118  SER 118  118  118  SER SER C . n 
C 3 119  ILE 119  119  119  ILE ILE C . n 
C 3 120  ASN 120  120  120  ASN ASN C . n 
C 3 121  ARG 121  121  121  ARG ARG C . n 
C 3 122  PHE 122  122  122  PHE PHE C . n 
C 3 123  ALA 123  123  123  ALA ALA C . n 
C 3 124  GLU 124  124  124  GLU GLU C . n 
C 3 125  ALA 125  125  125  ALA ALA C . n 
C 3 126  MET 126  126  126  MET MET C . n 
C 3 127  THR 127  127  127  THR THR C . n 
C 3 128  LEU 128  128  128  LEU LEU C . n 
C 3 129  PHE 129  129  129  PHE PHE C . n 
C 3 130  ALA 130  130  130  ALA ALA C . n 
C 3 131  VAL 131  131  131  VAL VAL C . n 
C 3 132  ALA 132  132  132  ALA ALA C . n 
C 3 133  CYS 133  133  133  CYS CYS C . n 
C 3 134  ALA 134  134  134  ALA ALA C . n 
C 3 135  GLY 135  135  135  GLY GLY C . n 
C 3 136  LEU 136  136  136  LEU LEU C . n 
C 3 137  TYR 137  137  137  TYR TYR C . n 
C 3 138  PRO 138  138  138  PRO PRO C . n 
C 3 139  ILE 139  139  139  ILE ILE C . n 
C 3 140  LEU 140  140  140  LEU LEU C . n 
C 3 141  HIS 141  141  141  HIS HIS C . n 
C 3 142  LEU 142  142  142  LEU LEU C . n 
C 3 143  GLY 143  143  143  GLY GLY C . n 
C 3 144  ARG 144  144  144  ARG ARG C . n 
C 3 145  PRO 145  145  145  PRO PRO C . n 
C 3 146  TRP 146  146  146  TRP TRP C . n 
C 3 147  LEU 147  147  147  LEU LEU C . n 
C 3 148  PHE 148  148  148  PHE PHE C . n 
C 3 149  TYR 149  149  149  TYR TYR C . n 
C 3 150  TRP 150  150  150  TRP TRP C . n 
C 3 151  LEU 151  151  151  LEU LEU C . n 
C 3 152  ILE 152  152  152  ILE ILE C . n 
C 3 153  PRO 153  153  153  PRO PRO C . n 
C 3 154  TYR 154  154  154  TYR TYR C . n 
C 3 155  PRO 155  155  155  PRO PRO C . n 
C 3 156  ASN 156  156  156  ASN ASN C . n 
C 3 157  THR 157  157  157  THR THR C . n 
C 3 158  HIS 158  158  158  HIS HIS C . n 
C 3 159  GLY 159  159  159  GLY GLY C . n 
C 3 160  MET 160  160  160  MET MET C . n 
C 3 161  TRP 161  161  161  TRP TRP C . n 
C 3 162  PRO 162  162  162  PRO PRO C . n 
C 3 163  GLN 163  163  163  GLN GLN C . n 
C 3 164  PHE 164  164  164  PHE PHE C . n 
C 3 165  ARG 165  165  165  ARG ARG C . n 
C 3 166  SER 166  166  166  SER SER C . n 
C 3 167  ALA 167  167  167  ALA ALA C . n 
C 3 168  LEU 168  168  168  LEU LEU C . n 
C 3 169  ALA 169  169  169  ALA ALA C . n 
C 3 170  TRP 170  170  170  TRP TRP C . n 
C 3 171  ASP 171  171  171  ASP ASP C . n 
C 3 172  VAL 172  172  172  VAL VAL C . n 
C 3 173  PHE 173  173  173  PHE PHE C . n 
C 3 174  ALA 174  174  174  ALA ALA C . n 
C 3 175  ILE 175  175  175  ILE ILE C . n 
C 3 176  SER 176  176  176  SER SER C . n 
C 3 177  THR 177  177  177  THR THR C . n 
C 3 178  TYR 178  178  178  TYR TYR C . n 
C 3 179  ALA 179  179  179  ALA ALA C . n 
C 3 180  THR 180  180  180  THR THR C . n 
C 3 181  VAL 181  181  181  VAL VAL C . n 
C 3 182  SER 182  182  182  SER SER C . n 
C 3 183  LEU 183  183  183  LEU LEU C . n 
C 3 184  VAL 184  184  184  VAL VAL C . n 
C 3 185  PHE 185  185  185  PHE PHE C . n 
C 3 186  TRP 186  186  186  TRP TRP C . n 
C 3 187  LEU 187  187  187  LEU LEU C . n 
C 3 188  VAL 188  188  188  VAL VAL C . n 
C 3 189  GLY 189  189  189  GLY GLY C . n 
C 3 190  LEU 190  190  190  LEU LEU C . n 
C 3 191  ILE 191  191  191  ILE ILE C . n 
C 3 192  PRO 192  192  192  PRO PRO C . n 
C 3 193  ASP 193  193  193  ASP ASP C . n 
C 3 194  PHE 194  194  194  PHE PHE C . n 
C 3 195  ALA 195  195  195  ALA ALA C . n 
C 3 196  THR 196  196  196  THR THR C . n 
C 3 197  LEU 197  197  197  LEU LEU C . n 
C 3 198  ARG 198  198  198  ARG ARG C . n 
C 3 199  ASP 199  199  199  ASP ASP C . n 
C 3 200  ARG 200  200  200  ARG ARG C . n 
C 3 201  ALA 201  201  201  ALA ALA C . n 
C 3 202  LYS 202  202  202  LYS LYS C . n 
C 3 203  ASN 203  203  203  ASN ASN C . n 
C 3 204  ILE 204  204  204  ILE ILE C . n 
C 3 205  TRP 205  205  205  TRP TRP C . n 
C 3 206  VAL 206  206  206  VAL VAL C . n 
C 3 207  LYS 207  207  207  LYS LYS C . n 
C 3 208  ARG 208  208  208  ARG ARG C . n 
C 3 209  LEU 209  209  209  LEU LEU C . n 
C 3 210  TYR 210  210  210  TYR TYR C . n 
C 3 211  GLY 211  211  211  GLY GLY C . n 
C 3 212  ILE 212  212  212  ILE ILE C . n 
C 3 213  ALA 213  213  213  ALA ALA C . n 
C 3 214  ALA 214  214  214  ALA ALA C . n 
C 3 215  LEU 215  215  215  LEU LEU C . n 
C 3 216  GLY 216  216  216  GLY GLY C . n 
C 3 217  TRP 217  217  217  TRP TRP C . n 
C 3 218  ARG 218  218  218  ARG ARG C . n 
C 3 219  GLY 219  219  219  GLY GLY C . n 
C 3 220  SER 220  220  220  SER SER C . n 
C 3 221  ALA 221  221  221  ALA ALA C . n 
C 3 222  ARG 222  222  222  ARG ARG C . n 
C 3 223  HIS 223  223  223  HIS HIS C . n 
C 3 224  TRP 224  224  224  TRP TRP C . n 
C 3 225  HIS 225  225  225  HIS HIS C . n 
C 3 226  ARG 226  226  226  ARG ARG C . n 
C 3 227  TYR 227  227  227  TYR TYR C . n 
C 3 228  GLU 228  228  228  GLU GLU C . n 
C 3 229  MET 229  229  229  MET MET C . n 
C 3 230  ALA 230  230  230  ALA ALA C . n 
C 3 231  SER 231  231  231  SER SER C . n 
C 3 232  ILE 232  232  232  ILE ILE C . n 
C 3 233  LEU 233  233  233  LEU LEU C . n 
C 3 234  LEU 234  234  234  LEU LEU C . n 
C 3 235  ALA 235  235  235  ALA ALA C . n 
C 3 236  GLY 236  236  236  GLY GLY C . n 
C 3 237  LEU 237  237  237  LEU LEU C . n 
C 3 238  SER 238  238  238  SER SER C . n 
C 3 239  THR 239  239  239  THR THR C . n 
C 3 240  PRO 240  240  240  PRO PRO C . n 
C 3 241  LEU 241  241  241  LEU LEU C . n 
C 3 242  VAL 242  242  242  VAL VAL C . n 
C 3 243  VAL 243  243  243  VAL VAL C . n 
C 3 244  SER 244  244  244  SER SER C . n 
C 3 245  VAL 245  245  245  VAL VAL C . n 
C 3 246  HIS 246  246  246  HIS HIS C . n 
C 3 247  SER 247  247  247  SER SER C . n 
C 3 248  ILE 248  248  248  ILE ILE C . n 
C 3 249  ILE 249  249  249  ILE ILE C . n 
C 3 250  SER 250  250  250  SER SER C . n 
C 3 251  LEU 251  251  251  LEU LEU C . n 
C 3 252  ASP 252  252  252  ASP ASP C . n 
C 3 253  PHE 253  253  253  PHE PHE C . n 
C 3 254  ALA 254  254  254  ALA ALA C . n 
C 3 255  ILE 255  255  255  ILE ILE C . n 
C 3 256  SER 256  256  256  SER SER C . n 
C 3 257  GLN 257  257  257  GLN GLN C . n 
C 3 258  VAL 258  258  258  VAL VAL C . n 
C 3 259  PRO 259  259  259  PRO PRO C . n 
C 3 260  GLY 260  260  260  GLY GLY C . n 
C 3 261  TRP 261  261  261  TRP TRP C . n 
C 3 262  GLN 262  262  262  GLN GLN C . n 
C 3 263  VAL 263  263  263  VAL VAL C . n 
C 3 264  THR 264  264  264  THR THR C . n 
C 3 265  VAL 265  265  265  VAL VAL C . n 
C 3 266  PHE 266  266  266  PHE PHE C . n 
C 3 267  PRO 267  267  267  PRO PRO C . n 
C 3 268  PRO 268  268  268  PRO PRO C . n 
C 3 269  TYR 269  269  269  TYR TYR C . n 
C 3 270  PHE 270  270  270  PHE PHE C . n 
C 3 271  VAL 271  271  271  VAL VAL C . n 
C 3 272  ALA 272  272  272  ALA ALA C . n 
C 3 273  GLY 273  273  273  GLY GLY C . n 
C 3 274  ALA 274  274  274  ALA ALA C . n 
C 3 275  VAL 275  275  275  VAL VAL C . n 
C 3 276  PHE 276  276  276  PHE PHE C . n 
C 3 277  ALA 277  277  277  ALA ALA C . n 
C 3 278  GLY 278  278  278  GLY GLY C . n 
C 3 279  PHE 279  279  279  PHE PHE C . n 
C 3 280  ALA 280  280  280  ALA ALA C . n 
C 3 281  MET 281  281  281  MET MET C . n 
C 3 282  VAL 282  282  282  VAL VAL C . n 
C 3 283  LEU 283  283  283  LEU LEU C . n 
C 3 284  LEU 284  284  284  LEU LEU C . n 
C 3 285  LEU 285  285  285  LEU LEU C . n 
C 3 286  MET 286  286  286  MET MET C . n 
C 3 287  ILE 287  287  287  ILE ILE C . n 
C 3 288  PRO 288  288  288  PRO PRO C . n 
C 3 289  VAL 289  289  289  VAL VAL C . n 
C 3 290  ARG 290  290  290  ARG ARG C . n 
C 3 291  THR 291  291  291  THR THR C . n 
C 3 292  PHE 292  292  292  PHE PHE C . n 
C 3 293  TYR 293  293  293  TYR TYR C . n 
C 3 294  GLY 294  294  294  GLY GLY C . n 
C 3 295  PHE 295  295  295  PHE PHE C . n 
C 3 296  GLU 296  296  296  GLU GLU C . n 
C 3 297  ASN 297  297  297  ASN ASN C . n 
C 3 298  TYR 298  298  298  TYR TYR C . n 
C 3 299  ILE 299  299  299  ILE ILE C . n 
C 3 300  THR 300  300  300  THR THR C . n 
C 3 301  LEU 301  301  301  LEU LEU C . n 
C 3 302  HIS 302  302  302  HIS HIS C . n 
C 3 303  HIS 303  303  303  HIS HIS C . n 
C 3 304  LEU 304  304  304  LEU LEU C . n 
C 3 305  ASP 305  305  305  ASP ASP C . n 
C 3 306  VAL 306  306  306  VAL VAL C . n 
C 3 307  MET 307  307  307  MET MET C . n 
C 3 308  ALA 308  308  308  ALA ALA C . n 
C 3 309  LYS 309  309  309  LYS LYS C . n 
C 3 310  VAL 310  310  310  VAL VAL C . n 
C 3 311  MET 311  311  311  MET MET C . n 
C 3 312  LEU 312  312  312  LEU LEU C . n 
C 3 313  THR 313  313  313  THR THR C . n 
C 3 314  THR 314  314  314  THR THR C . n 
C 3 315  GLY 315  315  315  GLY GLY C . n 
C 3 316  MET 316  316  316  MET MET C . n 
C 3 317  ILE 317  317  317  ILE ILE C . n 
C 3 318  VAL 318  318  318  VAL VAL C . n 
C 3 319  VAL 319  319  319  VAL VAL C . n 
C 3 320  TYR 320  320  320  TYR TYR C . n 
C 3 321  GLY 321  321  321  GLY GLY C . n 
C 3 322  TYR 322  322  322  TYR TYR C . n 
C 3 323  PHE 323  323  323  PHE PHE C . n 
C 3 324  MET 324  324  324  MET MET C . n 
C 3 325  GLU 325  325  325  GLU GLU C . n 
C 3 326  VAL 326  326  326  VAL VAL C . n 
C 3 327  PHE 327  327  327  PHE PHE C . n 
C 3 328  ALA 328  328  328  ALA ALA C . n 
C 3 329  SER 329  329  329  SER SER C . n 
C 3 330  LEU 330  330  330  LEU LEU C . n 
C 3 331  TYR 331  331  331  TYR TYR C . n 
C 3 332  SER 332  332  332  SER SER C . n 
C 3 333  GLY 333  333  333  GLY GLY C . n 
C 3 334  ASN 334  334  334  ASN ASN C . n 
C 3 335  GLU 335  335  335  GLU GLU C . n 
C 3 336  PHE 336  336  336  PHE PHE C . n 
C 3 337  GLU 337  337  337  GLU GLU C . n 
C 3 338  GLU 338  338  338  GLU GLU C . n 
C 3 339  TYR 339  339  339  TYR TYR C . n 
C 3 340  LEU 340  340  340  LEU LEU C . n 
C 3 341  LEU 341  341  341  LEU LEU C . n 
C 3 342  TYR 342  342  342  TYR TYR C . n 
C 3 343  ASN 343  343  343  ASN ASN C . n 
C 3 344  ARG 344  344  344  ARG ARG C . n 
C 3 345  LEU 345  345  345  LEU LEU C . n 
C 3 346  PHE 346  346  346  PHE PHE C . n 
C 3 347  GLY 347  347  347  GLY GLY C . n 
C 3 348  PRO 348  348  348  PRO PRO C . n 
C 3 349  SER 349  349  349  SER SER C . n 
C 3 350  SER 350  350  350  SER SER C . n 
C 3 351  TRP 351  351  351  TRP TRP C . n 
C 3 352  ALA 352  352  352  ALA ALA C . n 
C 3 353  TYR 353  353  353  TYR TYR C . n 
C 3 354  TRP 354  354  354  TRP TRP C . n 
C 3 355  GLY 355  355  355  GLY GLY C . n 
C 3 356  LEU 356  356  356  LEU LEU C . n 
C 3 357  LEU 357  357  357  LEU LEU C . n 
C 3 358  PHE 358  358  358  PHE PHE C . n 
C 3 359  CYS 359  359  359  CYS CYS C . n 
C 3 360  ASN 360  360  360  ASN ASN C . n 
C 3 361  ALA 361  361  361  ALA ALA C . n 
C 3 362  VAL 362  362  362  VAL VAL C . n 
C 3 363  ALA 363  363  363  ALA ALA C . n 
C 3 364  ILE 364  364  364  ILE ILE C . n 
C 3 365  GLN 365  365  365  GLN GLN C . n 
C 3 366  PRO 366  366  366  PRO PRO C . n 
C 3 367  LEU 367  367  367  LEU LEU C . n 
C 3 368  TRP 368  368  368  TRP TRP C . n 
C 3 369  PHE 369  369  369  PHE PHE C . n 
C 3 370  LYS 370  370  370  LYS LYS C . n 
C 3 371  LYS 371  371  371  LYS LYS C . n 
C 3 372  VAL 372  372  372  VAL VAL C . n 
C 3 373  ARG 373  373  373  ARG ARG C . n 
C 3 374  GLN 374  374  374  GLN GLN C . n 
C 3 375  ASN 375  375  375  ASN ASN C . n 
C 3 376  ILE 376  376  376  ILE ILE C . n 
C 3 377  PRO 377  377  377  PRO PRO C . n 
C 3 378  ALA 378  378  378  ALA ALA C . n 
C 3 379  LEU 379  379  379  LEU LEU C . n 
C 3 380  LEU 380  380  380  LEU LEU C . n 
C 3 381  ILE 381  381  381  ILE ILE C . n 
C 3 382  ILE 382  382  382  ILE ILE C . n 
C 3 383  SER 383  383  383  SER SER C . n 
C 3 384  LEU 384  384  384  LEU LEU C . n 
C 3 385  ILE 385  385  385  ILE ILE C . n 
C 3 386  VAL 386  386  386  VAL VAL C . n 
C 3 387  SER 387  387  387  SER SER C . n 
C 3 388  VAL 388  388  388  VAL VAL C . n 
C 3 389  GLY 389  389  389  GLY GLY C . n 
C 3 390  MET 390  390  390  MET MET C . n 
C 3 391  TRP 391  391  391  TRP TRP C . n 
C 3 392  LEU 392  392  392  LEU LEU C . n 
C 3 393  GLU 393  393  393  GLU GLU C . n 
C 3 394  ARG 394  394  394  ARG ARG C . n 
C 3 395  TYR 395  395  395  TYR TYR C . n 
C 3 396  VAL 396  396  396  VAL VAL C . n 
C 3 397  ILE 397  397  397  ILE ILE C . n 
C 3 398  ILE 398  398  398  ILE ILE C . n 
C 3 399  VAL 399  399  399  VAL VAL C . n 
C 3 400  ILE 400  400  400  ILE ILE C . n 
C 3 401  SER 401  401  401  SER SER C . n 
C 3 402  LEU 402  402  402  LEU LEU C . n 
C 3 403  GLU 403  403  403  GLU GLU C . n 
C 3 404  ARG 404  404  404  ARG ARG C . n 
C 3 405  ASP 405  405  405  ASP ASP C . n 
C 3 406  PHE 406  406  406  PHE PHE C . n 
C 3 407  LEU 407  407  407  LEU LEU C . n 
C 3 408  PRO 408  408  408  PRO PRO C . n 
C 3 409  SER 409  409  409  SER SER C . n 
C 3 410  SER 410  410  410  SER SER C . n 
C 3 411  TRP 411  411  411  TRP TRP C . n 
C 3 412  ASP 412  412  412  ASP ASP C . n 
C 3 413  ILE 413  413  413  ILE ILE C . n 
C 3 414  TYR 414  414  414  TYR TYR C . n 
C 3 415  ILE 415  415  415  ILE ILE C . n 
C 3 416  PRO 416  416  416  PRO PRO C . n 
C 3 417  THR 417  417  417  THR THR C . n 
C 3 418  ILE 418  418  418  ILE ILE C . n 
C 3 419  TRP 419  419  419  TRP TRP C . n 
C 3 420  ASP 420  420  420  ASP ASP C . n 
C 3 421  TRP 421  421  421  TRP TRP C . n 
C 3 422  SER 422  422  422  SER SER C . n 
C 3 423  LEU 423  423  423  LEU LEU C . n 
C 3 424  TYR 424  424  424  TYR TYR C . n 
C 3 425  ILE 425  425  425  ILE ILE C . n 
C 3 426  GLY 426  426  426  GLY GLY C . n 
C 3 427  THR 427  427  427  THR THR C . n 
C 3 428  PHE 428  428  428  PHE PHE C . n 
C 3 429  GLY 429  429  429  GLY GLY C . n 
C 3 430  LEU 430  430  430  LEU LEU C . n 
C 3 431  PHE 431  431  431  PHE PHE C . n 
C 3 432  PHE 432  432  432  PHE PHE C . n 
C 3 433  THR 433  433  433  THR THR C . n 
C 3 434  LEU 434  434  434  LEU LEU C . n 
C 3 435  LEU 435  435  435  LEU LEU C . n 
C 3 436  PHE 436  436  436  PHE PHE C . n 
C 3 437  LEU 437  437  437  LEU LEU C . n 
C 3 438  PHE 438  438  438  PHE PHE C . n 
C 3 439  ILE 439  439  439  ILE ILE C . n 
C 3 440  ARG 440  440  440  ARG ARG C . n 
C 3 441  VAL 441  441  441  VAL VAL C . n 
C 3 442  LEU 442  442  442  LEU LEU C . n 
C 3 443  PRO 443  443  443  PRO PRO C . n 
C 3 444  MET 444  444  444  MET MET C . n 
C 3 445  ILE 445  445  445  ILE ILE C . n 
C 3 446  ASN 446  446  446  ASN ASN C . n 
C 3 447  ILE 447  447  447  ILE ILE C . n 
C 3 448  PHE 448  448  448  PHE PHE C . n 
C 3 449  GLU 449  449  449  GLU GLU C . n 
C 3 450  MET 450  450  450  MET MET C . n 
C 3 451  ARG 451  451  451  ARG ARG C . n 
C 3 452  LEU 452  452  452  LEU LEU C . n 
C 3 453  PHE 453  453  453  PHE PHE C . n 
C 3 454  LEU 454  454  454  LEU LEU C . n 
C 3 455  TYR 455  455  455  TYR TYR C . n 
C 3 456  GLN 456  456  456  GLN GLN C . n 
C 3 457  GLU 457  457  457  GLU GLU C . n 
C 3 458  THR 458  458  458  THR THR C . n 
C 3 459  GLU 459  459  459  GLU GLU C . n 
C 3 460  LYS 460  460  460  LYS LYS C . n 
C 3 461  ALA 461  461  461  ALA ALA C . n 
C 3 462  LYS 462  462  462  LYS LYS C . n 
C 3 463  GLN 463  463  463  GLN GLN C . n 
C 3 464  ARG 464  464  464  ARG ARG C . n 
C 3 465  ALA 465  465  ?    ?   ?   C . n 
C 3 466  GLY 466  466  ?    ?   ?   C . n 
C 3 467  HIS 467  467  ?    ?   ?   C . n 
C 3 468  GLY 468  468  ?    ?   ?   C . n 
C 3 469  ALA 469  469  ?    ?   ?   C . n 
C 3 470  HIS 470  470  ?    ?   ?   C . n 
C 3 471  GLY 471  471  ?    ?   ?   C . n 
C 3 472  HIS 472  472  ?    ?   ?   C . n 
C 3 473  GLY 473  473  ?    ?   ?   C . n 
C 3 474  HIS 474  474  ?    ?   ?   C . n 
C 3 475  GLU 475  475  ?    ?   ?   C . n 
C 3 476  GLN 476  476  ?    ?   ?   C . n 
C 3 477  SER 477  477  ?    ?   ?   C . n 
C 3 478  PRO 478  478  ?    ?   ?   C . n 
C 3 479  ALA 479  479  ?    ?   ?   C . n 
C 3 480  HIS 480  480  ?    ?   ?   C . n 
C 3 481  GLY 481  481  ?    ?   ?   C . n 
C 3 482  ALA 482  482  ?    ?   ?   C . n 
C 3 483  ALA 483  483  ?    ?   ?   C . n 
C 3 484  THR 484  484  ?    ?   ?   C . n 
C 3 485  ALA 485  485  ?    ?   ?   C . n 
C 3 486  ASP 486  486  ?    ?   ?   C . n 
D 4 1    MET 1    1    ?    ?   ?   D . n 
D 4 2    ARG 2    2    ?    ?   ?   D . n 
D 4 3    ASN 3    3    ?    ?   ?   D . n 
D 4 4    ASP 4    4    ?    ?   ?   D . n 
D 4 5    VAL 5    5    5    VAL VAL D . n 
D 4 6    TYR 6    6    6    TYR TYR D . n 
D 4 7    GLY 7    7    7    GLY GLY D . n 
D 4 8    VAL 8    8    8    VAL VAL D . n 
D 4 9    MET 9    9    9    MET MET D . n 
D 4 10   ALA 10   10   10   ALA ALA D . n 
D 4 11   GLU 11   11   11   GLU GLU D . n 
D 4 12   PHE 12   12   12   PHE PHE D . n 
D 4 13   PRO 13   13   13   PRO PRO D . n 
D 4 14   THR 14   14   14   THR THR D . n 
D 4 15   PRO 15   15   15   PRO PRO D . n 
D 4 16   GLU 16   16   16   GLU GLU D . n 
D 4 17   ALA 17   17   17   ALA ALA D . n 
D 4 18   LEU 18   18   18   LEU LEU D . n 
D 4 19   ILE 19   19   19   ILE ILE D . n 
D 4 20   GLU 20   20   20   GLU GLU D . n 
D 4 21   ALA 21   21   21   ALA ALA D . n 
D 4 22   THR 22   22   22   THR THR D . n 
D 4 23   ARG 23   23   23   ARG ARG D . n 
D 4 24   LYS 24   24   24   LYS LYS D . n 
D 4 25   ALA 25   25   25   ALA ALA D . n 
D 4 26   LYS 26   26   26   LYS LYS D . n 
D 4 27   ALA 27   27   27   ALA ALA D . n 
D 4 28   ALA 28   28   28   ALA ALA D . n 
D 4 29   GLY 29   29   29   GLY GLY D . n 
D 4 30   TYR 30   30   30   TYR TYR D . n 
D 4 31   THR 31   31   31   THR THR D . n 
D 4 32   LYS 32   32   32   LYS LYS D . n 
D 4 33   MET 33   33   33   MET MET D . n 
D 4 34   ASP 34   34   34   ASP ASP D . n 
D 4 35   ALA 35   35   35   ALA ALA D . n 
D 4 36   PHE 36   36   36   PHE PHE D . n 
D 4 37   SER 37   37   37   SER SER D . n 
D 4 38   PRO 38   38   38   PRO PRO D . n 
D 4 39   PHE 39   39   39   PHE PHE D . n 
D 4 40   PRO 40   40   40   PRO PRO D . n 
D 4 41   ILE 41   41   41   ILE ILE D . n 
D 4 42   GLU 42   42   42   GLU GLU D . n 
D 4 43   GLU 43   43   43   GLU GLU D . n 
D 4 44   VAL 44   44   44   VAL VAL D . n 
D 4 45   ILE 45   45   45   ILE ILE D . n 
D 4 46   GLU 46   46   46   GLU GLU D . n 
D 4 47   GLU 47   47   47   GLU GLU D . n 
D 4 48   ILE 48   48   48   ILE ILE D . n 
D 4 49   ALA 49   49   49   ALA ALA D . n 
D 4 50   HIS 50   50   50   HIS HIS D . n 
D 4 51   GLY 51   51   51   GLY GLY D . n 
D 4 52   ASP 52   52   52   ASP ASP D . n 
D 4 53   THR 53   53   53   THR THR D . n 
D 4 54   GLY 54   54   54   GLY GLY D . n 
D 4 55   VAL 55   55   55   VAL VAL D . n 
D 4 56   PRO 56   56   56   PRO PRO D . n 
D 4 57   ARG 57   57   57   ARG ARG D . n 
D 4 58   LEU 58   58   58   LEU LEU D . n 
D 4 59   VAL 59   59   59   VAL VAL D . n 
D 4 60   LEU 60   60   60   LEU LEU D . n 
D 4 61   LEU 61   61   61   LEU LEU D . n 
D 4 62   PHE 62   62   62   PHE PHE D . n 
D 4 63   GLY 63   63   63   GLY GLY D . n 
D 4 64   LEU 64   64   64   LEU LEU D . n 
D 4 65   ILE 65   65   65   ILE ILE D . n 
D 4 66   GLY 66   66   66   GLY GLY D . n 
D 4 67   ALA 67   67   67   ALA ALA D . n 
D 4 68   ALA 68   68   68   ALA ALA D . n 
D 4 69   SER 69   69   69   SER SER D . n 
D 4 70   GLY 70   70   70   GLY GLY D . n 
D 4 71   PHE 71   71   71   PHE PHE D . n 
D 4 72   ILE 72   72   72   ILE ILE D . n 
D 4 73   LEU 73   73   73   LEU LEU D . n 
D 4 74   GLN 74   74   74   GLN GLN D . n 
D 4 75   TYR 75   75   75   TYR TYR D . n 
D 4 76   ILE 76   76   76   ILE ILE D . n 
D 4 77   GLY 77   77   77   GLY GLY D . n 
D 4 78   ASN 78   78   78   ASN ASN D . n 
D 4 79   LEU 79   79   79   LEU LEU D . n 
D 4 80   VAL 80   80   80   VAL VAL D . n 
D 4 81   ASP 81   81   81   ASP ASP D . n 
D 4 82   TYR 82   82   82   TYR TYR D . n 
D 4 83   PRO 83   83   83   PRO PRO D . n 
D 4 84   LEU 84   84   84   LEU LEU D . n 
D 4 85   ASN 85   85   85   ASN ASN D . n 
D 4 86   VAL 86   86   86   VAL VAL D . n 
D 4 87   GLY 87   87   87   GLY GLY D . n 
D 4 88   GLY 88   88   88   GLY GLY D . n 
D 4 89   ARG 89   89   89   ARG ARG D . n 
D 4 90   PRO 90   90   90   PRO PRO D . n 
D 4 91   LEU 91   91   91   LEU LEU D . n 
D 4 92   ASP 92   92   92   ASP ASP D . n 
D 4 93   ILE 93   93   93   ILE ILE D . n 
D 4 94   THR 94   94   94   THR THR D . n 
D 4 95   ASN 95   95   95   ASN ASN D . n 
D 4 96   TRP 96   96   96   TRP TRP D . n 
D 4 97   PRO 97   97   97   PRO PRO D . n 
D 4 98   ALA 98   98   98   ALA ALA D . n 
D 4 99   MET 99   99   99   MET MET D . n 
D 4 100  ILE 100  100  100  ILE ILE D . n 
D 4 101  PRO 101  101  101  PRO PRO D . n 
D 4 102  ILE 102  102  102  ILE ILE D . n 
D 4 103  THR 103  103  103  THR THR D . n 
D 4 104  PHE 104  104  104  PHE PHE D . n 
D 4 105  GLU 105  105  105  GLU GLU D . n 
D 4 106  SER 106  106  106  SER SER D . n 
D 4 107  GLY 107  107  107  GLY GLY D . n 
D 4 108  ILE 108  108  108  ILE ILE D . n 
D 4 109  LEU 109  109  109  LEU LEU D . n 
D 4 110  LEU 110  110  110  LEU LEU D . n 
D 4 111  ALA 111  111  111  ALA ALA D . n 
D 4 112  SER 112  112  112  SER SER D . n 
D 4 113  PHE 113  113  113  PHE PHE D . n 
D 4 114  ALA 114  114  114  ALA ALA D . n 
D 4 115  ALA 115  115  115  ALA ALA D . n 
D 4 116  ALA 116  116  116  ALA ALA D . n 
D 4 117  ILE 117  117  117  ILE ILE D . n 
D 4 118  GLY 118  118  118  GLY GLY D . n 
D 4 119  MET 119  119  119  MET MET D . n 
D 4 120  ILE 120  120  120  ILE ILE D . n 
D 4 121  VAL 121  121  121  VAL VAL D . n 
D 4 122  LEU 122  122  122  LEU LEU D . n 
D 4 123  ASN 123  123  123  ASN ASN D . n 
D 4 124  GLY 124  124  124  GLY GLY D . n 
D 4 125  LEU 125  125  125  LEU LEU D . n 
D 4 126  PRO 126  126  126  PRO PRO D . n 
D 4 127  SER 127  127  127  SER SER D . n 
D 4 128  PRO 128  128  128  PRO PRO D . n 
D 4 129  TYR 129  129  129  TYR TYR D . n 
D 4 130  HIS 130  130  130  HIS HIS D . n 
D 4 131  PRO 131  131  131  PRO PRO D . n 
D 4 132  VAL 132  132  132  VAL VAL D . n 
D 4 133  PHE 133  133  133  PHE PHE D . n 
D 4 134  ASN 134  134  134  ASN ASN D . n 
D 4 135  VAL 135  135  135  VAL VAL D . n 
D 4 136  PRO 136  136  136  PRO PRO D . n 
D 4 137  ARG 137  137  137  ARG ARG D . n 
D 4 138  PHE 138  138  138  PHE PHE D . n 
D 4 139  GLN 139  139  139  GLN GLN D . n 
D 4 140  TYR 140  140  140  TYR TYR D . n 
D 4 141  ALA 141  141  141  ALA ALA D . n 
D 4 142  SER 142  142  142  SER SER D . n 
D 4 143  GLN 143  143  143  GLN GLN D . n 
D 4 144  ASP 144  144  144  ASP ASP D . n 
D 4 145  ALA 145  145  145  ALA ALA D . n 
D 4 146  PHE 146  146  146  PHE PHE D . n 
D 4 147  PHE 147  147  147  PHE PHE D . n 
D 4 148  LEU 148  148  148  LEU LEU D . n 
D 4 149  CYS 149  149  149  CYS CYS D . n 
D 4 150  ILE 150  150  150  ILE ILE D . n 
D 4 151  GLU 151  151  151  GLU GLU D . n 
D 4 152  ALA 152  152  152  ALA ALA D . n 
D 4 153  THR 153  153  153  THR THR D . n 
D 4 154  ASP 154  154  154  ASP ASP D . n 
D 4 155  PRO 155  155  155  PRO PRO D . n 
D 4 156  LEU 156  156  156  LEU LEU D . n 
D 4 157  PHE 157  157  157  PHE PHE D . n 
D 4 158  ASP 158  158  158  ASP ASP D . n 
D 4 159  ARG 159  159  159  ARG ARG D . n 
D 4 160  SER 160  160  160  SER SER D . n 
D 4 161  ARG 161  161  161  ARG ARG D . n 
D 4 162  THR 162  162  162  THR THR D . n 
D 4 163  SER 163  163  163  SER SER D . n 
D 4 164  GLN 164  164  164  GLN GLN D . n 
D 4 165  PHE 165  165  165  PHE PHE D . n 
D 4 166  LEU 166  166  166  LEU LEU D . n 
D 4 167  ARG 167  167  167  ARG ARG D . n 
D 4 168  SER 168  168  168  SER SER D . n 
D 4 169  LEU 169  169  169  LEU LEU D . n 
D 4 170  ASN 170  170  170  ASN ASN D . n 
D 4 171  PRO 171  171  171  PRO PRO D . n 
D 4 172  MET 172  172  172  MET MET D . n 
D 4 173  GLN 173  173  173  GLN GLN D . n 
D 4 174  VAL 174  174  174  VAL VAL D . n 
D 4 175  SER 175  175  175  SER SER D . n 
D 4 176  GLU 176  176  176  GLU GLU D . n 
D 4 177  VAL 177  177  177  VAL VAL D . n 
D 4 178  ALA 178  178  178  ALA ALA D . n 
D 4 179  TYR 179  179  179  TYR TYR D . n 
E 5 1    MET 1    1    ?    ?   ?   E . n 
E 5 2    GLN 2    2    ?    ?   ?   E . n 
E 5 3    LYS 3    3    ?    ?   ?   E . n 
E 5 4    PRO 4    4    ?    ?   ?   E . n 
E 5 5    ARG 5    5    ?    ?   ?   E . n 
E 5 6    LEU 6    6    ?    ?   ?   E . n 
E 5 7    THR 7    7    ?    ?   ?   E . n 
E 5 8    SER 8    8    ?    ?   ?   E . n 
E 5 9    ARG 9    9    ?    ?   ?   E . n 
E 5 10   MET 10   10   ?    ?   ?   E . n 
E 5 11   ILE 11   11   ?    ?   ?   E . n 
E 5 12   ARG 12   12   ?    ?   ?   E . n 
E 5 13   PHE 13   13   ?    ?   ?   E . n 
E 5 14   GLY 14   14   ?    ?   ?   E . n 
E 5 15   TRP 15   15   ?    ?   ?   E . n 
E 5 16   VAL 16   16   ?    ?   ?   E . n 
E 5 17   GLY 17   17   ?    ?   ?   E . n 
E 5 18   LEU 18   18   ?    ?   ?   E . n 
E 5 19   LEU 19   19   ?    ?   ?   E . n 
E 5 20   VAL 20   20   ?    ?   ?   E . n 
E 5 21   LEU 21   21   ?    ?   ?   E . n 
E 5 22   LEU 22   22   ?    ?   ?   E . n 
E 5 23   LEU 23   23   ?    ?   ?   E . n 
E 5 24   THR 24   24   ?    ?   ?   E . n 
E 5 25   ALA 25   25   ?    ?   ?   E . n 
E 5 26   CYS 26   26   26   CYS CYS E . n 
E 5 27   HIS 27   27   27   HIS HIS E . n 
E 5 28   GLN 28   28   28   GLN GLN E . n 
E 5 29   ASP 29   29   29   ASP ASP E . n 
E 5 30   MET 30   30   30   MET MET E . n 
E 5 31   TYR 31   31   31   TYR TYR E . n 
E 5 32   ASP 32   32   32   ASP ASP E . n 
E 5 33   GLN 33   33   33   GLN GLN E . n 
E 5 34   GLN 34   34   34   GLN GLN E . n 
E 5 35   LYS 35   35   35   LYS LYS E . n 
E 5 36   TYR 36   36   36   TYR TYR E . n 
E 5 37   THR 37   37   37   THR THR E . n 
E 5 38   THR 38   38   38   THR THR E . n 
E 5 39   TYR 39   39   39   TYR TYR E . n 
E 5 40   GLU 40   40   40   GLU GLU E . n 
E 5 41   PRO 41   41   41   PRO PRO E . n 
E 5 42   SER 42   42   42   SER SER E . n 
E 5 43   SER 43   43   43   SER SER E . n 
E 5 44   PHE 44   44   44   PHE PHE E . n 
E 5 45   PHE 45   45   45   PHE PHE E . n 
E 5 46   ALA 46   46   46   ALA ALA E . n 
E 5 47   ASP 47   47   47   ASP ASP E . n 
E 5 48   GLY 48   48   48   GLY GLY E . n 
E 5 49   ARG 49   49   49   ARG ARG E . n 
E 5 50   SER 50   50   50   SER SER E . n 
E 5 51   SER 51   51   51   SER SER E . n 
E 5 52   ARG 52   52   52   ARG ARG E . n 
E 5 53   PRO 53   53   53   PRO PRO E . n 
E 5 54   ASN 54   54   54   ASN ASN E . n 
E 5 55   VAL 55   55   55   VAL VAL E . n 
E 5 56   PRO 56   56   56   PRO PRO E . n 
E 5 57   GLY 57   57   57   GLY GLY E . n 
E 5 58   THR 58   58   58   THR THR E . n 
E 5 59   THR 59   59   59   THR THR E . n 
E 5 60   PRO 60   60   60   PRO PRO E . n 
E 5 61   PHE 61   61   61   PHE PHE E . n 
E 5 62   GLU 62   62   62   GLU GLU E . n 
E 5 63   VAL 63   63   63   VAL VAL E . n 
E 5 64   VAL 64   64   64   VAL VAL E . n 
E 5 65   LYS 65   65   65   LYS LYS E . n 
E 5 66   THR 66   66   66   THR THR E . n 
E 5 67   ASP 67   67   67   ASP ASP E . n 
E 5 68   GLU 68   68   68   GLU GLU E . n 
E 5 69   PHE 69   69   69   PHE PHE E . n 
E 5 70   LEU 70   70   70   LEU LEU E . n 
E 5 71   TYR 71   71   71   TYR TYR E . n 
E 5 72   THR 72   72   72   THR THR E . n 
E 5 73   GLY 73   73   73   GLY GLY E . n 
E 5 74   LEU 74   74   74   LEU LEU E . n 
E 5 75   ILE 75   75   75   ILE ILE E . n 
E 5 76   ASP 76   76   76   ASP ASP E . n 
E 5 77   GLY 77   77   77   GLY GLY E . n 
E 5 78   GLN 78   78   78   GLN GLN E . n 
E 5 79   GLU 79   79   79   GLU GLU E . n 
E 5 80   VAL 80   80   80   VAL VAL E . n 
E 5 81   ASP 81   81   81   ASP ASP E . n 
E 5 82   ALA 82   82   82   ALA ALA E . n 
E 5 83   MET 83   83   83   MET MET E . n 
E 5 84   PRO 84   84   84   PRO PRO E . n 
E 5 85   PHE 85   85   85   PHE PHE E . n 
E 5 86   PRO 86   86   86   PRO PRO E . n 
E 5 87   VAL 87   87   87   VAL VAL E . n 
E 5 88   THR 88   88   88   THR THR E . n 
E 5 89   LYS 89   89   89   LYS LYS E . n 
E 5 90   ASP 90   90   90   ASP ASP E . n 
E 5 91   LEU 91   91   91   LEU LEU E . n 
E 5 92   LEU 92   92   92   LEU LEU E . n 
E 5 93   LEU 93   93   93   LEU LEU E . n 
E 5 94   ARG 94   94   94   ARG ARG E . n 
E 5 95   GLY 95   95   95   GLY GLY E . n 
E 5 96   GLN 96   96   96   GLN GLN E . n 
E 5 97   LEU 97   97   97   LEU LEU E . n 
E 5 98   LYS 98   98   98   LYS LYS E . n 
E 5 99   TYR 99   99   99   TYR TYR E . n 
E 5 100  ASN 100  100  100  ASN ASN E . n 
E 5 101  ILE 101  101  101  ILE ILE E . n 
E 5 102  TYR 102  102  102  TYR TYR E . n 
E 5 103  CYS 103  103  103  CYS CYS E . n 
E 5 104  ALA 104  104  104  ALA ALA E . n 
E 5 105  VAL 105  105  105  VAL VAL E . n 
E 5 106  CYS 106  106  106  CYS CYS E . n 
E 5 107  HIS 107  107  107  HIS HIS E . n 
E 5 108  GLY 108  108  108  GLY GLY E . n 
E 5 109  GLU 109  109  109  GLU GLU E . n 
E 5 110  ALA 110  110  110  ALA ALA E . n 
E 5 111  GLY 111  111  111  GLY GLY E . n 
E 5 112  TYR 112  112  112  TYR TYR E . n 
E 5 113  GLY 113  113  113  GLY GLY E . n 
E 5 114  ALA 114  114  114  ALA ALA E . n 
E 5 115  SER 115  115  115  SER SER E . n 
E 5 116  MET 116  116  116  MET MET E . n 
E 5 117  VAL 117  117  117  VAL VAL E . n 
E 5 118  ALA 118  118  118  ALA ALA E . n 
E 5 119  GLU 119  119  119  GLU GLU E . n 
E 5 120  ARG 120  120  120  ARG ARG E . n 
E 5 121  GLY 121  121  121  GLY GLY E . n 
E 5 122  GLY 122  122  122  GLY GLY E . n 
E 5 123  ILE 123  123  123  ILE ILE E . n 
E 5 124  VAL 124  124  124  VAL VAL E . n 
E 5 125  PRO 125  125  125  PRO PRO E . n 
E 5 126  ALA 126  126  126  ALA ALA E . n 
E 5 127  ASN 127  127  127  ASN ASN E . n 
E 5 128  PHE 128  128  128  PHE PHE E . n 
E 5 129  HIS 129  129  129  HIS HIS E . n 
E 5 130  GLN 130  130  130  GLN GLN E . n 
E 5 131  GLN 131  131  131  GLN GLN E . n 
E 5 132  ARG 132  132  132  ARG ARG E . n 
E 5 133  LEU 133  133  133  LEU LEU E . n 
E 5 134  ARG 134  134  134  ARG ARG E . n 
E 5 135  GLU 135  135  135  GLU GLU E . n 
E 5 136  ALA 136  136  136  ALA ALA E . n 
E 5 137  PRO 137  137  137  PRO PRO E . n 
E 5 138  LEU 138  138  138  LEU LEU E . n 
E 5 139  SER 139  139  139  SER SER E . n 
E 5 140  HIS 140  140  140  HIS HIS E . n 
E 5 141  PHE 141  141  141  PHE PHE E . n 
E 5 142  PHE 142  142  142  PHE PHE E . n 
E 5 143  VAL 143  143  143  VAL VAL E . n 
E 5 144  VAL 144  144  144  VAL VAL E . n 
E 5 145  ILE 145  145  145  ILE ILE E . n 
E 5 146  THR 146  146  146  THR THR E . n 
E 5 147  ASN 147  147  147  ASN ASN E . n 
E 5 148  GLY 148  148  148  GLY GLY E . n 
E 5 149  VAL 149  149  149  VAL VAL E . n 
E 5 150  TYR 150  150  150  TYR TYR E . n 
E 5 151  ARG 151  151  151  ARG ARG E . n 
E 5 152  GLY 152  152  152  GLY GLY E . n 
E 5 153  ASP 153  153  153  ASP ASP E . n 
E 5 154  PRO 154  154  154  PRO PRO E . n 
E 5 155  GLU 155  155  155  GLU GLU E . n 
E 5 156  ASN 156  156  156  ASN ASN E . n 
E 5 157  GLY 157  157  157  GLY GLY E . n 
E 5 158  GLY 158  158  158  GLY GLY E . n 
E 5 159  TYR 159  159  159  TYR TYR E . n 
E 5 160  GLN 160  160  160  GLN GLN E . n 
E 5 161  SER 161  161  161  SER SER E . n 
E 5 162  MET 162  162  162  MET MET E . n 
E 5 163  TYR 163  163  163  TYR TYR E . n 
E 5 164  GLY 164  164  164  GLY GLY E . n 
E 5 165  TYR 165  165  165  TYR TYR E . n 
E 5 166  ALA 166  166  166  ALA ALA E . n 
E 5 167  SER 167  167  167  SER SER E . n 
E 5 168  ARG 168  168  168  ARG ARG E . n 
E 5 169  ILE 169  169  169  ILE ILE E . n 
E 5 170  THR 170  170  170  THR THR E . n 
E 5 171  PRO 171  171  171  PRO PRO E . n 
E 5 172  GLU 172  172  172  GLU GLU E . n 
E 5 173  ASP 173  173  173  ASP ASP E . n 
E 5 174  ARG 174  174  174  ARG ARG E . n 
E 5 175  TRP 175  175  175  TRP TRP E . n 
E 5 176  ALA 176  176  176  ALA ALA E . n 
E 5 177  ILE 177  177  177  ILE ILE E . n 
E 5 178  ALA 178  178  178  ALA ALA E . n 
E 5 179  ALA 179  179  179  ALA ALA E . n 
E 5 180  TYR 180  180  180  TYR TYR E . n 
E 5 181  ILE 181  181  181  ILE ILE E . n 
E 5 182  ARG 182  182  182  ARG ARG E . n 
E 5 183  ALA 183  183  183  ALA ALA E . n 
E 5 184  LEU 184  184  184  LEU LEU E . n 
E 5 185  GLN 185  185  185  GLN GLN E . n 
E 5 186  LEU 186  186  186  LEU LEU E . n 
E 5 187  SER 187  187  187  SER SER E . n 
E 5 188  GLN 188  188  188  GLN GLN E . n 
E 5 189  ASN 189  189  189  ASN ASN E . n 
E 5 190  ALA 190  190  ?    ?   ?   E . n 
E 5 191  THR 191  191  ?    ?   ?   E . n 
E 5 192  ILE 192  192  ?    ?   ?   E . n 
E 5 193  ASP 193  193  ?    ?   ?   E . n 
E 5 194  ASP 194  194  ?    ?   ?   E . n 
E 5 195  VAL 195  195  ?    ?   ?   E . n 
E 5 196  PRO 196  196  ?    ?   ?   E . n 
E 5 197  PRO 197  197  ?    ?   ?   E . n 
E 5 198  ASP 198  198  ?    ?   ?   E . n 
E 5 199  GLN 199  199  ?    ?   ?   E . n 
E 5 200  ARG 200  200  ?    ?   ?   E . n 
E 5 201  ALA 201  201  ?    ?   ?   E . n 
E 5 202  GLN 202  202  ?    ?   ?   E . n 
E 5 203  LEU 203  203  ?    ?   ?   E . n 
E 5 204  GLY 204  204  ?    ?   ?   E . n 
E 5 205  ASN 205  205  ?    ?   ?   E . n 
F 6 1    MET 1    1    ?    ?   ?   F . n 
F 6 2    ALA 2    2    ?    ?   ?   F . n 
F 6 3    THR 3    3    ?    ?   ?   F . n 
F 6 4    THR 4    4    ?    ?   ?   F . n 
F 6 5    SER 5    5    ?    ?   ?   F . n 
F 6 6    ILE 6    6    ?    ?   ?   F . n 
F 6 7    SER 7    7    ?    ?   ?   F . n 
F 6 8    GLN 8    8    ?    ?   ?   F . n 
F 6 9    THR 9    9    ?    ?   ?   F . n 
F 6 10   ARG 10   10   ?    ?   ?   F . n 
F 6 11   ILE 11   11   11   ILE ILE F . n 
F 6 12   PRO 12   12   12   PRO PRO F . n 
F 6 13   GLN 13   13   13   GLN GLN F . n 
F 6 14   LEU 14   14   14   LEU LEU F . n 
F 6 15   GLY 15   15   15   GLY GLY F . n 
F 6 16   GLN 16   16   16   GLN GLN F . n 
F 6 17   VAL 17   17   17   VAL VAL F . n 
F 6 18   GLN 18   18   18   GLN GLN F . n 
F 6 19   MET 19   19   19   MET MET F . n 
F 6 20   LEU 20   20   20   LEU LEU F . n 
F 6 21   GLY 21   21   21   GLY GLY F . n 
F 6 22   LEU 22   22   22   LEU LEU F . n 
F 6 23   ALA 23   23   23   ALA ALA F . n 
F 6 24   ALA 24   24   24   ALA ALA F . n 
F 6 25   ALA 25   25   25   ALA ALA F . n 
F 6 26   VAL 26   26   26   VAL VAL F . n 
F 6 27   ILE 27   27   27   ILE ILE F . n 
F 6 28   GLY 28   28   28   GLY GLY F . n 
F 6 29   ILE 29   29   29   ILE ILE F . n 
F 6 30   GLY 30   30   30   GLY GLY F . n 
F 6 31   VAL 31   31   31   VAL VAL F . n 
F 6 32   LEU 32   32   32   LEU LEU F . n 
F 6 33   ALA 33   33   33   ALA ALA F . n 
F 6 34   ALA 34   34   34   ALA ALA F . n 
F 6 35   GLY 35   35   35   GLY GLY F . n 
F 6 36   TYR 36   36   36   TYR TYR F . n 
F 6 37   PHE 37   37   37   PHE PHE F . n 
F 6 38   LEU 38   38   38   LEU LEU F . n 
F 6 39   SER 39   39   39   SER SER F . n 
F 6 40   PRO 40   40   40   PRO PRO F . n 
F 6 41   THR 41   41   41   THR THR F . n 
F 6 42   SER 42   42   42   SER SER F . n 
F 6 43   PHE 43   43   43   PHE PHE F . n 
F 6 44   PHE 44   44   44   PHE PHE F . n 
F 6 45   GLU 45   45   45   GLU GLU F . n 
F 6 46   SER 46   46   46   SER SER F . n 
F 6 47   TYR 47   47   47   TYR TYR F . n 
F 6 48   ILE 48   48   48   ILE ILE F . n 
F 6 49   TYR 49   49   49   TYR TYR F . n 
F 6 50   GLY 50   50   50   GLY GLY F . n 
F 6 51   TYR 51   51   51   TYR TYR F . n 
F 6 52   TYR 52   52   52   TYR TYR F . n 
F 6 53   VAL 53   53   53   VAL VAL F . n 
F 6 54   ALA 54   54   54   ALA ALA F . n 
F 6 55   MET 55   55   55   MET MET F . n 
F 6 56   THR 56   56   56   THR THR F . n 
F 6 57   ILE 57   57   57   ILE ILE F . n 
F 6 58   PRO 58   58   58   PRO PRO F . n 
F 6 59   LEU 59   59   59   LEU LEU F . n 
F 6 60   GLY 60   60   60   GLY GLY F . n 
F 6 61   CYS 61   61   61   CYS CYS F . n 
F 6 62   LEU 62   62   62   LEU LEU F . n 
F 6 63   GLY 63   63   63   GLY GLY F . n 
F 6 64   PHE 64   64   64   PHE PHE F . n 
F 6 65   LEU 65   65   65   LEU LEU F . n 
F 6 66   MET 66   66   66   MET MET F . n 
F 6 67   VAL 67   67   67   VAL VAL F . n 
F 6 68   GLN 68   68   68   GLN GLN F . n 
F 6 69   HIS 69   69   69   HIS HIS F . n 
F 6 70   LEU 70   70   70   LEU LEU F . n 
F 6 71   THR 71   71   71   THR THR F . n 
F 6 72   GLY 72   72   72   GLY GLY F . n 
F 6 73   GLY 73   73   73   GLY GLY F . n 
F 6 74   ALA 74   74   74   ALA ALA F . n 
F 6 75   TRP 75   75   75   TRP TRP F . n 
F 6 76   GLY 76   76   76   GLY GLY F . n 
F 6 77   VAL 77   77   77   VAL VAL F . n 
F 6 78   THR 78   78   78   THR THR F . n 
F 6 79   VAL 79   79   79   VAL VAL F . n 
F 6 80   ARG 80   80   80   ARG ARG F . n 
F 6 81   ARG 81   81   81   ARG ARG F . n 
F 6 82   MET 82   82   82   MET MET F . n 
F 6 83   LEU 83   83   83   LEU LEU F . n 
F 6 84   GLU 84   84   84   GLU GLU F . n 
F 6 85   ALA 85   85   85   ALA ALA F . n 
F 6 86   GLY 86   86   86   GLY GLY F . n 
F 6 87   ALA 87   87   87   ALA ALA F . n 
F 6 88   ALA 88   88   88   ALA ALA F . n 
F 6 89   THR 89   89   89   THR THR F . n 
F 6 90   LEU 90   90   90   LEU LEU F . n 
F 6 91   PRO 91   91   91   PRO PRO F . n 
F 6 92   ILE 92   92   92   ILE ILE F . n 
F 6 93   MET 93   93   93   MET MET F . n 
F 6 94   GLY 94   94   94   GLY GLY F . n 
F 6 95   LEU 95   95   95   LEU LEU F . n 
F 6 96   LEU 96   96   96   LEU LEU F . n 
F 6 97   PHE 97   97   97   PHE PHE F . n 
F 6 98   ILE 98   98   98   ILE ILE F . n 
F 6 99   PRO 99   99   99   PRO PRO F . n 
F 6 100  ILE 100  100  100  ILE ILE F . n 
F 6 101  ALA 101  101  101  ALA ALA F . n 
F 6 102  LEU 102  102  102  LEU LEU F . n 
F 6 103  GLY 103  103  103  GLY GLY F . n 
F 6 104  TYR 104  104  104  TYR TYR F . n 
F 6 105  PHE 105  105  105  PHE PHE F . n 
F 6 106  ASP 106  106  106  ASP ASP F . n 
F 6 107  THR 107  107  107  THR THR F . n 
F 6 108  TYR 108  108  108  TYR TYR F . n 
F 6 109  LYS 109  109  109  LYS LYS F . n 
F 6 110  ALA 110  110  110  ALA ALA F . n 
F 6 111  LEU 111  111  111  LEU LEU F . n 
F 6 112  GLY 112  112  112  GLY GLY F . n 
F 6 113  LEU 113  113  113  LEU LEU F . n 
F 6 114  GLU 114  114  114  GLU GLU F . n 
F 6 115  HIS 115  115  115  HIS HIS F . n 
F 6 116  PRO 116  116  116  PRO PRO F . n 
F 6 117  LEU 117  117  117  LEU LEU F . n 
F 6 118  TYR 118  118  118  TYR TYR F . n 
F 6 119  GLU 119  119  119  GLU GLU F . n 
F 6 120  TRP 120  120  120  TRP TRP F . n 
F 6 121  ALA 121  121  121  ALA ALA F . n 
F 6 122  ASN 122  122  122  ASN ASN F . n 
F 6 123  PRO 123  123  123  PRO PRO F . n 
F 6 124  GLU 124  124  124  GLU GLU F . n 
F 6 125  VAL 125  125  125  VAL VAL F . n 
F 6 126  VAL 126  126  126  VAL VAL F . n 
F 6 127  THR 127  127  127  THR THR F . n 
F 6 128  PRO 128  128  128  PRO PRO F . n 
F 6 129  GLY 129  129  129  GLY GLY F . n 
F 6 130  GLY 130  130  130  GLY GLY F . n 
F 6 131  ALA 131  131  131  ALA ALA F . n 
F 6 132  GLU 132  132  132  GLU GLU F . n 
F 6 133  PHE 133  133  133  PHE PHE F . n 
F 6 134  ASP 134  134  134  ASP ASP F . n 
F 6 135  PRO 135  135  135  PRO PRO F . n 
F 6 136  ILE 136  136  136  ILE ILE F . n 
F 6 137  ILE 137  137  137  ILE ILE F . n 
F 6 138  ALA 138  138  138  ALA ALA F . n 
F 6 139  HIS 139  139  139  HIS HIS F . n 
F 6 140  LYS 140  140  140  LYS LYS F . n 
F 6 141  VAL 141  141  141  VAL VAL F . n 
F 6 142  PRO 142  142  142  PRO PRO F . n 
F 6 143  TRP 143  143  143  TRP TRP F . n 
F 6 144  LEU 144  144  144  LEU LEU F . n 
F 6 145  SER 145  145  145  SER SER F . n 
F 6 146  PRO 146  146  146  PRO PRO F . n 
F 6 147  LEU 147  147  147  LEU LEU F . n 
F 6 148  TRP 148  148  148  TRP TRP F . n 
F 6 149  VAL 149  149  149  VAL VAL F . n 
F 6 150  THR 150  150  150  THR THR F . n 
F 6 151  ALA 151  151  151  ALA ALA F . n 
F 6 152  ARG 152  152  152  ARG ARG F . n 
F 6 153  ILE 153  153  153  ILE ILE F . n 
F 6 154  ALA 154  154  154  ALA ALA F . n 
F 6 155  ILE 155  155  155  ILE ILE F . n 
F 6 156  PHE 156  156  156  PHE PHE F . n 
F 6 157  PHE 157  157  157  PHE PHE F . n 
F 6 158  ILE 158  158  158  ILE ILE F . n 
F 6 159  ILE 159  159  159  ILE ILE F . n 
F 6 160  TRP 160  160  160  TRP TRP F . n 
F 6 161  SER 161  161  161  SER SER F . n 
F 6 162  ALA 162  162  162  ALA ALA F . n 
F 6 163  LEU 163  163  163  LEU LEU F . n 
F 6 164  ALA 164  164  164  ALA ALA F . n 
F 6 165  LEU 165  165  165  LEU LEU F . n 
F 6 166  THR 166  166  166  THR THR F . n 
F 6 167  LEU 167  167  167  LEU LEU F . n 
F 6 168  ARG 168  168  168  ARG ARG F . n 
F 6 169  ALA 169  169  169  ALA ALA F . n 
F 6 170  TRP 170  170  170  TRP TRP F . n 
F 6 171  SER 171  171  171  SER SER F . n 
F 6 172  ARG 172  172  172  ARG ARG F . n 
F 6 173  GLN 173  173  173  GLN GLN F . n 
F 6 174  GLN 174  174  174  GLN GLN F . n 
F 6 175  ASP 175  175  175  ASP ASP F . n 
F 6 176  ALA 176  176  176  ALA ALA F . n 
F 6 177  GLY 177  177  177  GLY GLY F . n 
F 6 178  GLY 178  178  178  GLY GLY F . n 
F 6 179  ASP 179  179  179  ASP ASP F . n 
F 6 180  ALA 180  180  180  ALA ALA F . n 
F 6 181  LYS 181  181  181  LYS LYS F . n 
F 6 182  LYS 182  182  182  LYS LYS F . n 
F 6 183  LEU 183  183  183  LEU LEU F . n 
F 6 184  ALA 184  184  184  ALA ALA F . n 
F 6 185  THR 185  185  185  THR THR F . n 
F 6 186  ARG 186  186  186  ARG ARG F . n 
F 6 187  MET 187  187  187  MET MET F . n 
F 6 188  ARG 188  188  188  ARG ARG F . n 
F 6 189  ARG 189  189  189  ARG ARG F . n 
F 6 190  LEU 190  190  190  LEU LEU F . n 
F 6 191  SER 191  191  191  SER SER F . n 
F 6 192  GLY 192  192  192  GLY GLY F . n 
F 6 193  ILE 193  193  193  ILE ILE F . n 
F 6 194  GLY 194  194  194  GLY GLY F . n 
F 6 195  VAL 195  195  195  VAL VAL F . n 
F 6 196  ALA 196  196  196  ALA ALA F . n 
F 6 197  LEU 197  197  197  LEU LEU F . n 
F 6 198  PHE 198  198  198  PHE PHE F . n 
F 6 199  VAL 199  199  199  VAL VAL F . n 
F 6 200  ILE 200  200  200  ILE ILE F . n 
F 6 201  THR 201  201  201  THR THR F . n 
F 6 202  VAL 202  202  202  VAL VAL F . n 
F 6 203  THR 203  203  203  THR THR F . n 
F 6 204  PHE 204  204  204  PHE PHE F . n 
F 6 205  PHE 205  205  205  PHE PHE F . n 
F 6 206  SER 206  206  206  SER SER F . n 
F 6 207  PHE 207  207  207  PHE PHE F . n 
F 6 208  ASP 208  208  208  ASP ASP F . n 
F 6 209  VAL 209  209  209  VAL VAL F . n 
F 6 210  ALA 210  210  210  ALA ALA F . n 
F 6 211  MET 211  211  211  MET MET F . n 
F 6 212  SER 212  212  212  SER SER F . n 
F 6 213  LEU 213  213  213  LEU LEU F . n 
F 6 214  ASP 214  214  214  ASP ASP F . n 
F 6 215  PRO 215  215  215  PRO PRO F . n 
F 6 216  HIS 216  216  216  HIS HIS F . n 
F 6 217  TRP 217  217  217  TRP TRP F . n 
F 6 218  PHE 218  218  218  PHE PHE F . n 
F 6 219  SER 219  219  219  SER SER F . n 
F 6 220  THR 220  220  220  THR THR F . n 
F 6 221  ILE 221  221  221  ILE ILE F . n 
F 6 222  TYR 222  222  222  TYR TYR F . n 
F 6 223  GLY 223  223  223  GLY GLY F . n 
F 6 224  ALA 224  224  224  ALA ALA F . n 
F 6 225  HIS 225  225  225  HIS HIS F . n 
F 6 226  TYR 226  226  226  TYR TYR F . n 
F 6 227  MET 227  227  227  MET MET F . n 
F 6 228  ALA 228  228  228  ALA ALA F . n 
F 6 229  ASN 229  229  229  ASN ASN F . n 
F 6 230  ALA 230  230  230  ALA ALA F . n 
F 6 231  GLY 231  231  231  GLY GLY F . n 
F 6 232  LEU 232  232  232  LEU LEU F . n 
F 6 233  MET 233  233  233  MET MET F . n 
F 6 234  THR 234  234  234  THR THR F . n 
F 6 235  LEU 235  235  235  LEU LEU F . n 
F 6 236  ALA 236  236  236  ALA ALA F . n 
F 6 237  PHE 237  237  237  PHE PHE F . n 
F 6 238  LEU 238  238  238  LEU LEU F . n 
F 6 239  ALA 239  239  239  ALA ALA F . n 
F 6 240  LEU 240  240  240  LEU LEU F . n 
F 6 241  MET 241  241  241  MET MET F . n 
F 6 242  MET 242  242  242  MET MET F . n 
F 6 243  SER 243  243  243  SER SER F . n 
F 6 244  ARG 244  244  244  ARG ARG F . n 
F 6 245  VAL 245  245  245  VAL VAL F . n 
F 6 246  ARG 246  246  246  ARG ARG F . n 
F 6 247  ASP 247  247  247  ASP ASP F . n 
F 6 248  ALA 248  248  248  ALA ALA F . n 
F 6 249  ALA 249  249  249  ALA ALA F . n 
F 6 250  LEU 250  250  250  LEU LEU F . n 
F 6 251  PHE 251  251  251  PHE PHE F . n 
F 6 252  ARG 252  252  252  ARG ARG F . n 
F 6 253  GLU 253  253  253  GLU GLU F . n 
F 6 254  TYR 254  254  254  TYR TYR F . n 
F 6 255  VAL 255  255  255  VAL VAL F . n 
F 6 256  SER 256  256  256  SER SER F . n 
F 6 257  VAL 257  257  257  VAL VAL F . n 
F 6 258  LYS 258  258  258  LYS LYS F . n 
F 6 259  PRO 259  259  259  PRO PRO F . n 
F 6 260  ILE 260  260  260  ILE ILE F . n 
F 6 261  HIS 261  261  261  HIS HIS F . n 
F 6 262  ASP 262  262  262  ASP ASP F . n 
F 6 263  ILE 263  263  263  ILE ILE F . n 
F 6 264  GLY 264  264  264  GLY GLY F . n 
F 6 265  LYS 265  265  265  LYS LYS F . n 
F 6 266  LEU 266  266  266  LEU LEU F . n 
F 6 267  ILE 267  267  267  ILE ILE F . n 
F 6 268  PHE 268  268  268  PHE PHE F . n 
F 6 269  ALA 269  269  269  ALA ALA F . n 
F 6 270  PHE 270  270  270  PHE PHE F . n 
F 6 271  THR 271  271  271  THR THR F . n 
F 6 272  VAL 272  272  272  VAL VAL F . n 
F 6 273  LEU 273  273  273  LEU LEU F . n 
F 6 274  TRP 274  274  274  TRP TRP F . n 
F 6 275  THR 275  275  275  THR THR F . n 
F 6 276  TYR 276  276  276  TYR TYR F . n 
F 6 277  MET 277  277  277  MET MET F . n 
F 6 278  SER 278  278  278  SER SER F . n 
F 6 279  TYR 279  279  279  TYR TYR F . n 
F 6 280  GLY 280  280  280  GLY GLY F . n 
F 6 281  GLN 281  281  281  GLN GLN F . n 
F 6 282  LEU 282  282  282  LEU LEU F . n 
F 6 283  VAL 283  283  283  VAL VAL F . n 
F 6 284  ILE 284  284  284  ILE ILE F . n 
F 6 285  ILE 285  285  285  ILE ILE F . n 
F 6 286  TRP 286  286  286  TRP TRP F . n 
F 6 287  SER 287  287  287  SER SER F . n 
F 6 288  GLY 288  288  288  GLY GLY F . n 
F 6 289  ASP 289  289  289  ASP ASP F . n 
F 6 290  VAL 290  290  290  VAL VAL F . n 
F 6 291  ALA 291  291  291  ALA ALA F . n 
F 6 292  GLU 292  292  292  GLU GLU F . n 
F 6 293  PHE 293  293  293  PHE PHE F . n 
F 6 294  THR 294  294  294  THR THR F . n 
F 6 295  PRO 295  295  295  PRO PRO F . n 
F 6 296  TRP 296  296  296  TRP TRP F . n 
F 6 297  TYR 297  297  297  TYR TYR F . n 
F 6 298  VAL 298  298  298  VAL VAL F . n 
F 6 299  HIS 299  299  299  HIS HIS F . n 
F 6 300  ARG 300  300  300  ARG ARG F . n 
F 6 301  THR 301  301  301  THR THR F . n 
F 6 302  GLN 302  302  302  GLN GLN F . n 
F 6 303  HIS 303  303  303  HIS HIS F . n 
F 6 304  GLY 304  304  304  GLY GLY F . n 
F 6 305  TRP 305  305  305  TRP TRP F . n 
F 6 306  VAL 306  306  306  VAL VAL F . n 
F 6 307  PHE 307  307  307  PHE PHE F . n 
F 6 308  VAL 308  308  308  VAL VAL F . n 
F 6 309  ALA 309  309  309  ALA ALA F . n 
F 6 310  LEU 310  310  310  LEU LEU F . n 
F 6 311  ALA 311  311  311  ALA ALA F . n 
F 6 312  LEU 312  312  312  LEU LEU F . n 
F 6 313  MET 313  313  313  MET MET F . n 
F 6 314  LEU 314  314  314  LEU LEU F . n 
F 6 315  PHE 315  315  315  PHE PHE F . n 
F 6 316  ALA 316  316  316  ALA ALA F . n 
F 6 317  PHE 317  317  317  PHE PHE F . n 
F 6 318  ALA 318  318  318  ALA ALA F . n 
F 6 319  LEU 319  319  319  LEU LEU F . n 
F 6 320  PRO 320  320  320  PRO PRO F . n 
F 6 321  PHE 321  321  321  PHE PHE F . n 
F 6 322  PHE 322  322  322  PHE PHE F . n 
F 6 323  VAL 323  323  323  VAL VAL F . n 
F 6 324  LEU 324  324  324  LEU LEU F . n 
F 6 325  LEU 325  325  325  LEU LEU F . n 
F 6 326  PHE 326  326  326  PHE PHE F . n 
F 6 327  ARG 327  327  327  ARG ARG F . n 
F 6 328  GLY 328  328  328  GLY GLY F . n 
F 6 329  THR 329  329  329  THR THR F . n 
F 6 330  LYS 330  330  330  LYS LYS F . n 
F 6 331  ARG 331  331  331  ARG ARG F . n 
F 6 332  ASN 332  332  332  ASN ASN F . n 
F 6 333  LEU 333  333  333  LEU LEU F . n 
F 6 334  ASN 334  334  334  ASN ASN F . n 
F 6 335  THR 335  335  335  THR THR F . n 
F 6 336  LEU 336  336  336  LEU LEU F . n 
F 6 337  ALA 337  337  337  ALA ALA F . n 
F 6 338  THR 338  338  338  THR THR F . n 
F 6 339  ILE 339  339  339  ILE ILE F . n 
F 6 340  ALA 340  340  340  ALA ALA F . n 
F 6 341  GLY 341  341  341  GLY GLY F . n 
F 6 342  TRP 342  342  342  TRP TRP F . n 
F 6 343  ILE 343  343  343  ILE ILE F . n 
F 6 344  VAL 344  344  344  VAL VAL F . n 
F 6 345  VAL 345  345  345  VAL VAL F . n 
F 6 346  MET 346  346  346  MET MET F . n 
F 6 347  ARG 347  347  347  ARG ARG F . n 
F 6 348  PHE 348  348  348  PHE PHE F . n 
F 6 349  VAL 349  349  349  VAL VAL F . n 
F 6 350  ASP 350  350  350  ASP ASP F . n 
F 6 351  MET 351  351  351  MET MET F . n 
F 6 352  ALA 352  352  352  ALA ALA F . n 
F 6 353  TRP 353  353  353  TRP TRP F . n 
F 6 354  ILE 354  354  354  ILE ILE F . n 
F 6 355  ILE 355  355  355  ILE ILE F . n 
F 6 356  LEU 356  356  356  LEU LEU F . n 
F 6 357  PRO 357  357  357  PRO PRO F . n 
F 6 358  GLU 358  358  358  GLU GLU F . n 
F 6 359  PHE 359  359  359  PHE PHE F . n 
F 6 360  ARG 360  360  360  ARG ARG F . n 
F 6 361  GLU 361  361  361  GLU GLU F . n 
F 6 362  HIS 362  362  362  HIS HIS F . n 
F 6 363  LEU 363  363  363  LEU LEU F . n 
F 6 364  TRP 364  364  364  TRP TRP F . n 
F 6 365  ASP 365  365  365  ASP ASP F . n 
F 6 366  ILE 366  366  366  ILE ILE F . n 
F 6 367  ALA 367  367  367  ALA ALA F . n 
F 6 368  ILE 368  368  368  ILE ILE F . n 
F 6 369  THR 369  369  369  THR THR F . n 
F 6 370  ASP 370  370  370  ASP ASP F . n 
F 6 371  VAL 371  371  371  VAL VAL F . n 
F 6 372  ALA 372  372  372  ALA ALA F . n 
F 6 373  ALA 373  373  373  ALA ALA F . n 
F 6 374  PRO 374  374  374  PRO PRO F . n 
F 6 375  ILE 375  375  375  ILE ILE F . n 
F 6 376  GLY 376  376  376  GLY GLY F . n 
F 6 377  LEU 377  377  377  LEU LEU F . n 
F 6 378  ILE 378  378  378  ILE ILE F . n 
F 6 379  GLY 379  379  379  GLY GLY F . n 
F 6 380  LEU 380  380  380  LEU LEU F . n 
F 6 381  VAL 381  381  381  VAL VAL F . n 
F 6 382  ILE 382  382  382  ILE ILE F . n 
F 6 383  ALA 383  383  383  ALA ALA F . n 
F 6 384  LEU 384  384  384  LEU LEU F . n 
F 6 385  PHE 385  385  385  PHE PHE F . n 
F 6 386  ALA 386  386  386  ALA ALA F . n 
F 6 387  ALA 387  387  387  ALA ALA F . n 
F 6 388  ASN 388  388  388  ASN ASN F . n 
F 6 389  VAL 389  389  389  VAL VAL F . n 
F 6 390  GLN 390  390  390  GLN GLN F . n 
F 6 391  GLN 391  391  391  GLN GLN F . n 
F 6 392  ALA 392  392  392  ALA ALA F . n 
F 6 393  PRO 393  393  393  PRO PRO F . n 
F 6 394  LEU 394  394  394  LEU LEU F . n 
F 6 395  LEU 395  395  395  LEU LEU F . n 
F 6 396  PRO 396  396  396  PRO PRO F . n 
F 6 397  LEU 397  397  397  LEU LEU F . n 
F 6 398  ARG 398  398  398  ARG ARG F . n 
F 6 399  ASP 399  399  399  ASP ASP F . n 
F 6 400  PRO 400  400  400  PRO PRO F . n 
F 6 401  ASN 401  401  401  ASN ASN F . n 
F 6 402  MET 402  402  402  MET MET F . n 
F 6 403  GLU 403  403  403  GLU GLU F . n 
F 6 404  GLN 404  404  404  GLN GLN F . n 
F 6 405  LEU 405  405  405  LEU LEU F . n 
F 6 406  GLN 406  406  406  GLN GLN F . n 
F 6 407  ASN 407  407  ?    ?   ?   F . n 
F 6 408  SER 408  408  ?    ?   ?   F . n 
F 6 409  GLY 409  409  ?    ?   ?   F . n 
F 6 410  HIS 410  410  ?    ?   ?   F . n 
F 6 411  HIS 411  411  ?    ?   ?   F . n 
G 7 1    MET 1    1    ?    ?   ?   G . n 
G 7 2    SER 2    2    ?    ?   ?   G . n 
G 7 3    TYR 3    3    ?    ?   ?   G . n 
G 7 4    ARG 4    4    ?    ?   ?   G . n 
G 7 5    PRO 5    5    ?    ?   ?   G . n 
G 7 6    ASN 6    6    ?    ?   ?   G . n 
G 7 7    TYR 7    7    ?    ?   ?   G . n 
G 7 8    SER 8    8    ?    ?   ?   G . n 
G 7 9    ALA 9    9    ?    ?   ?   G . n 
G 7 10   SER 10   10   ?    ?   ?   G . n 
G 7 11   ARG 11   11   ?    ?   ?   G . n 
G 7 12   TYR 12   12   ?    ?   ?   G . n 
G 7 13   THR 13   13   ?    ?   ?   G . n 
G 7 14   ALA 14   14   ?    ?   ?   G . n 
G 7 15   GLY 15   15   ?    ?   ?   G . n 
G 7 16   ARG 16   16   ?    ?   ?   G . n 
G 7 17   PRO 17   17   ?    ?   ?   G . n 
G 7 18   ALA 18   18   ?    ?   ?   G . n 
G 7 19   GLN 19   19   ?    ?   ?   G . n 
G 7 20   PRO 20   20   ?    ?   ?   G . n 
G 7 21   VAL 21   21   ?    ?   ?   G . n 
G 7 22   ARG 22   22   ?    ?   ?   G . n 
G 7 23   THR 23   23   ?    ?   ?   G . n 
G 7 24   ALA 24   24   ?    ?   ?   G . n 
G 7 25   ARG 25   25   ?    ?   ?   G . n 
G 7 26   THR 26   26   ?    ?   ?   G . n 
G 7 27   MET 27   27   ?    ?   ?   G . n 
G 7 28   ALA 28   28   ?    ?   ?   G . n 
G 7 29   GLU 29   29   ?    ?   ?   G . n 
G 7 30   PRO 30   30   ?    ?   ?   G . n 
G 7 31   SER 31   31   ?    ?   ?   G . n 
G 7 32   LEU 32   32   32   LEU LEU G . n 
G 7 33   SER 33   33   33   SER SER G . n 
G 7 34   ARG 34   34   34   ARG ARG G . n 
G 7 35   LEU 35   35   35   LEU LEU G . n 
G 7 36   MET 36   36   36   MET MET G . n 
G 7 37   ILE 37   37   37   ILE ILE G . n 
G 7 38   ALA 38   38   38   ALA ALA G . n 
G 7 39   GLY 39   39   39   GLY GLY G . n 
G 7 40   LEU 40   40   40   LEU LEU G . n 
G 7 41   MET 41   41   41   MET MET G . n 
G 7 42   VAL 42   42   42   VAL VAL G . n 
G 7 43   PHE 43   43   43   PHE PHE G . n 
G 7 44   LEU 44   44   44   LEU LEU G . n 
G 7 45   VAL 45   45   45   VAL VAL G . n 
G 7 46   LEU 46   46   46   LEU LEU G . n 
G 7 47   SER 47   47   47   SER SER G . n 
G 7 48   LEU 48   48   48   LEU LEU G . n 
G 7 49   VAL 49   49   49   VAL VAL G . n 
G 7 50   VAL 50   50   50   VAL VAL G . n 
G 7 51   LEU 51   51   51   LEU LEU G . n 
G 7 52   LEU 52   52   52   LEU LEU G . n 
G 7 53   ALA 53   53   53   ALA ALA G . n 
G 7 54   GLY 54   54   54   GLY GLY G . n 
G 7 55   ARG 55   55   55   ARG ARG G . n 
G 7 56   LEU 56   56   56   LEU LEU G . n 
G 7 57   PRO 57   57   57   PRO PRO G . n 
G 7 58   PHE 58   58   58   PHE PHE G . n 
G 7 59   THR 59   59   59   THR THR G . n 
G 7 60   PRO 60   60   60   PRO PRO G . n 
G 7 61   GLN 61   61   61   GLN GLN G . n 
G 7 62   PRO 62   62   62   PRO PRO G . n 
G 7 63   ALA 63   63   63   ALA ALA G . n 
G 7 64   PRO 64   64   64   PRO PRO G . n 
G 7 65   VAL 65   65   65   VAL VAL G . n 
G 7 66   THR 66   66   66   THR THR G . n 
G 7 67   GLY 67   67   67   GLY GLY G . n 
G 7 68   ASN 68   68   68   ASN ASN G . n 
G 7 69   THR 69   69   69   THR THR G . n 
G 7 70   TYR 70   70   70   TYR TYR G . n 
G 7 71   ARG 71   71   71   ARG ARG G . n 
G 7 72   THR 72   72   72   THR THR G . n 
G 7 73   TYR 73   73   73   TYR TYR G . n 
G 7 74   VAL 74   74   74   VAL VAL G . n 
G 7 75   ASN 75   75   75   ASN ASN G . n 
G 7 76   ASP 76   76   76   ASP ASP G . n 
G 7 77   ALA 77   77   77   ALA ALA G . n 
G 7 78   ARG 78   78   78   ARG ARG G . n 
G 7 79   THR 79   79   79   THR THR G . n 
G 7 80   LEU 80   80   80   LEU LEU G . n 
G 7 81   LEU 81   81   81   LEU LEU G . n 
G 7 82   ASN 82   82   82   ASN ASN G . n 
G 7 83   SER 83   83   83   SER SER G . n 
G 7 84   TYR 84   84   84   TYR TYR G . n 
G 7 85   GLY 85   85   85   GLY GLY G . n 
G 7 86   TYR 86   86   86   TYR TYR G . n 
G 7 87   THR 87   87   87   THR THR G . n 
G 7 88   MET 88   88   88   MET MET G . n 
G 7 89   GLU 89   89   89   GLU GLU G . n 
G 7 90   GLY 90   90   90   GLY GLY G . n 
G 7 91   LYS 91   91   91   LYS LYS G . n 
G 7 92   VAL 92   92   92   VAL VAL G . n 
G 7 93   HIS 93   93   93   HIS HIS G . n 
G 7 94   ILE 94   94   94   ILE ILE G . n 
G 7 95   PRO 95   95   95   PRO PRO G . n 
G 7 96   ILE 96   96   96   ILE ILE G . n 
G 7 97   ASP 97   97   97   ASP ASP G . n 
G 7 98   ARG 98   98   98   ARG ARG G . n 
G 7 99   ALA 99   99   99   ALA ALA G . n 
G 7 100  MET 100  100  100  MET MET G . n 
G 7 101  ASP 101  101  101  ASP ASP G . n 
G 7 102  LEU 102  102  102  LEU LEU G . n 
G 7 103  ILE 103  103  103  ILE ILE G . n 
G 7 104  VAL 104  104  104  VAL VAL G . n 
G 7 105  GLU 105  105  105  GLU GLU G . n 
G 7 106  ARG 106  106  106  ARG ARG G . n 
G 7 107  GLY 107  107  107  GLY GLY G . n 
G 7 108  LEU 108  108  108  LEU LEU G . n 
G 7 109  PRO 109  109  109  PRO PRO G . n 
G 7 110  VAL 110  110  110  VAL VAL G . n 
G 7 111  ARG 111  111  111  ARG ARG G . n 
G 7 112  GLU 112  112  ?    ?   ?   G . n 
H 8 1    MET 1    1    ?    ?   ?   I . n 
H 8 2    GLN 2    2    ?    ?   ?   I . n 
H 8 3    PRO 3    3    ?    ?   ?   I . n 
H 8 4    GLU 4    4    ?    ?   ?   I . n 
H 8 5    TRP 5    5    ?    ?   ?   I . n 
H 8 6    SER 6    6    ?    ?   ?   I . n 
H 8 7    GLY 7    7    ?    ?   ?   I . n 
H 8 8    ASP 8    8    ?    ?   ?   I . n 
H 8 9    PRO 9    9    ?    ?   ?   I . n 
H 8 10   GLU 10   10   ?    ?   ?   I . n 
H 8 11   VAL 11   11   11   VAL VAL I . n 
H 8 12   LYS 12   12   12   LYS LYS I . n 
H 8 13   PRO 13   13   13   PRO PRO I . n 
H 8 14   VAL 14   14   14   VAL VAL I . n 
H 8 15   PHE 15   15   15   PHE PHE I . n 
H 8 16   LEU 16   16   16   LEU LEU I . n 
H 8 17   ALA 17   17   17   ALA ALA I . n 
H 8 18   VAL 18   18   18   VAL VAL I . n 
H 8 19   THR 19   19   19   THR THR I . n 
H 8 20   LEU 20   20   20   LEU LEU I . n 
H 8 21   THR 21   21   21   THR THR I . n 
H 8 22   GLY 22   22   22   GLY GLY I . n 
H 8 23   MET 23   23   23   MET MET I . n 
H 8 24   VAL 24   24   24   VAL VAL I . n 
H 8 25   ALA 25   25   25   ALA ALA I . n 
H 8 26   PHE 26   26   26   PHE PHE I . n 
H 8 27   LEU 27   27   27   LEU LEU I . n 
H 8 28   LEU 28   28   28   LEU LEU I . n 
H 8 29   MET 29   29   29   MET MET I . n 
H 8 30   VAL 30   30   30   VAL VAL I . n 
H 8 31   TRP 31   31   31   TRP TRP I . n 
H 8 32   LEU 32   32   32   LEU LEU I . n 
H 8 33   PHE 33   33   33   PHE PHE I . n 
H 8 34   ALA 34   34   34   ALA ALA I . n 
H 8 35   PHE 35   35   35   PHE PHE I . n 
H 8 36   TYR 36   36   36   TYR TYR I . n 
H 8 37   TRP 37   37   37   TRP TRP I . n 
# 
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 
I 9  HEC 1 301  294  HEC HEC A . 
J 9  HEC 1 302  295  HEC HEC A . 
K 9  HEC 1 303  296  HEC HEC A . 
L 9  HEC 1 304  297  HEC HEC A . 
M 9  HEC 1 305  298  HEC HEC A . 
N 10 SF4 1 1101 1121 SF4 SF4 B . 
O 10 SF4 1 1102 1122 SF4 SF4 B . 
P 10 SF4 1 1103 1123 SF4 SF4 B . 
Q 11 F3S 1 1104 1124 F3S F3S B . 
R 9  HEC 1 301  217  HEC HEC E . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 E ARG 151 ? CG  ? E ARG 151 CG  
2  1 Y 1 E ARG 151 ? CD  ? E ARG 151 CD  
3  1 Y 1 E ARG 151 ? NE  ? E ARG 151 NE  
4  1 Y 1 E ARG 151 ? CZ  ? E ARG 151 CZ  
5  1 Y 1 E ARG 151 ? NH1 ? E ARG 151 NH1 
6  1 Y 1 E ARG 151 ? NH2 ? E ARG 151 NH2 
7  1 Y 1 G LYS 91  ? CG  ? G LYS 91  CG  
8  1 Y 1 G LYS 91  ? CD  ? G LYS 91  CD  
9  1 Y 1 G LYS 91  ? CE  ? G LYS 91  CE  
10 1 Y 1 G LYS 91  ? NZ  ? G LYS 91  NZ  
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.19.2_4158)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .               2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .               3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .               4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9ILT 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     142.016 
_cell.length_a_esd                 ? 
_cell.length_b                     153.063 
_cell.length_b_esd                 ? 
_cell.length_c                     173.381 
_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                         9ILT 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9ILT 
_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             3.15 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.00 
_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              ? 
_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    '100 mM glycine at pH 9.0 and 26% (w/v) PEG 400' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-09-26 
_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                    ? 
_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   0.979 
_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                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9ILT 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.25 
_reflns.d_resolution_low                               40.3 
_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                                     57488 
_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                           89.82 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.44 
_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                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    3.25 
_reflns_shell.d_res_low                                     3.366 
_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                             5927 
_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                               ? 
_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                                  0.748 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 9ILT 
_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                            3.25 
_refine.ls_d_res_low                             40.3 
_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                     54042 
_refine.ls_number_reflns_R_free                  2651 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    89.82 
_refine.ls_percent_reflns_R_free                 4.91 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2507 
_refine.ls_R_factor_R_free                       0.2858 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.249 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.34 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      8K9F 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 32.35 
_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                             ? 
_refine.overall_SU_ML                            0.56 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.25 
_refine_hist.d_res_low                        40.3 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               19668 
_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        19379 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         289 
_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 ? 20277 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.921 ? 27777 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.894 ? 2749  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.068 ? 3034  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004 ? 3513  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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 
_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 
_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 
'X-RAY DIFFRACTION' 3.25 3.31 . . 149 2990 100.00 . . . . 0.3688 . . . . . . . . . . . 0.4215 
'X-RAY DIFFRACTION' 3.31 3.37 . . 126 2964 100.00 . . . . 0.3498 . . . . . . . . . . . 0.4154 
'X-RAY DIFFRACTION' 3.37 3.43 . . 128 2304 89.00  . . . . 0.3410 . . . . . . . . . . . 0.3693 
'X-RAY DIFFRACTION' 3.48 3.52 . . 73  1278 82.00  . . . . 0.3387 . . . . . . . . . . . 0.3608 
'X-RAY DIFFRACTION' 3.52 3.60 . . 160 2963 100.00 . . . . 0.3242 . . . . . . . . . . . 0.3550 
'X-RAY DIFFRACTION' 3.60 3.66 . . 103 1950 90.00  . . . . 0.3224 . . . . . . . . . . . 0.3317 
'X-RAY DIFFRACTION' 3.70 3.79 . . 102 2190 88.00  . . . . 0.3108 . . . . . . . . . . . 0.3394 
'X-RAY DIFFRACTION' 3.79 3.89 . . 125 2628 94.00  . . . . 0.2882 . . . . . . . . . . . 0.3115 
'X-RAY DIFFRACTION' 3.94 4.02 . . 93  1835 92.00  . . . . 0.2999 . . . . . . . . . . . 0.3468 
'X-RAY DIFFRACTION' 4.02 4.17 . . 169 2978 100.00 . . . . 0.2677 . . . . . . . . . . . 0.3234 
'X-RAY DIFFRACTION' 4.17 4.34 . . 155 2977 100.00 . . . . 0.2546 . . . . . . . . . . . 0.2943 
'X-RAY DIFFRACTION' 4.34 4.53 . . 171 2984 100.00 . . . . 0.2315 . . . . . . . . . . . 0.2875 
'X-RAY DIFFRACTION' 4.53 4.77 . . 163 2993 100.00 . . . . 0.2256 . . . . . . . . . . . 0.2602 
'X-RAY DIFFRACTION' 4.77 5.07 . . 161 3006 100.00 . . . . 0.2196 . . . . . . . . . . . 0.2634 
'X-RAY DIFFRACTION' 5.07 5.46 . . 168 3018 100.00 . . . . 0.2198 . . . . . . . . . . . 0.2672 
'X-RAY DIFFRACTION' 5.46 6.01 . . 154 3030 100.00 . . . . 0.2352 . . . . . . . . . . . 0.2765 
'X-RAY DIFFRACTION' 6.01 6.87 . . 146 3050 100.00 . . . . 0.2317 . . . . . . . . . . . 0.2627 
'X-RAY DIFFRACTION' 6.87 8.65 . . 161 3088 100.00 . . . . 0.2122 . . . . . . . . . . . 0.2337 
'X-RAY DIFFRACTION' 8    10   . . 144 3165 98.00  . . . . 0.2159 . . . . . . . . . . . 0.2382 
# 
_struct.entry_id                     9ILT 
_struct.title                        'Crystal structure of alternative complex III from Chloroflexus aurantiacus' 
_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        9ILT 
_struct_keywords.text            
;alternative complex III, Chloroflexus aurantiacus, photosynthetic electron transport chains, quinol: electron acceptor oxidoreductase, MEMBRANE PROTEIN
;
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
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 9  ? 
K N N 9  ? 
L N N 9  ? 
M N N 9  ? 
N N N 10 ? 
O N N 10 ? 
P N N 10 ? 
Q N N 11 ? 
R N N 9  ? 
# 
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 A9WEV2_CHLAA A9WEV2 ? 1 
;MAQIFPRNANLLSRLSIFALVLLVVEGILILGVYFRSNYFRQVNVAIEQPVAFSHQLHVNVVGIDCRYCHTSVDQSYFAN
IPATETCMTCHSQIKTYSPLLEKVRESYATGKPIEWVKVYDLPNFVYFNHSIHVNKGIGCSTCHGQVNNMPVVWQQQALY
MGWCLNCHRNPELYVRPREEVYNMDYVPPSNQLEIGRQLVAEYGIMPPDQLTNCYVCHR
;
1 
2 UNP A9WEV3_CHLAA A9WEV3 ? 2 
;MTQQQPDLEAIRAQLRDARGPQFWRSLDQLADAPAFRELIEREFPRGASELEDGISRRTFLKLMGASLALAGVTACTYQP
RQYIAPFDRQPEGRVPGIPQYFASTLTLGGYGTGVLVRSNEGRPTKVEGNPRHPASLGGTDLFAQAEILTMYDPDRSTTV
LRQGVPSTWAEFTTTLGNALTAARATQGAGVRLLTTTITSPSLAAQIEQFLQAYPQARWYQYEPINRDNVVAGARLAFGR
DVTTRYDLSAAQVVVSLDADFLAPGPGFVAYARAFAERRKVRKDSTTMNRLYVVEASPSTTGTAADHRLPLRADAIAAFT
GALANELGVGGAPATLSPKAEEFLRAIARDLEEHRGQSVVIAGDQQPPIVHALAHLINAELGNVGQTVFYHEPVEARPTN
QTEELVALVSEMAAGRVETLIMIGGNPVYNAPGDLRFADRMASVPLTIHLSQFVDETSARATWHIPQAHPLESWGDARAF
DGTASIVQPLIEPLYGGKTANELLAAMLGQPEAESYDLVRSFWLEQIGETGWQVALANGVIAETVAPVIEPTLNEGAIRA
TPIPQPGDGVEIVFRPDPSLFDGFYANNGWLQELPRPLTKLVWDNAALMSPRTAIKLLGLPFNADRLIGTEADDRERQQY
LEQLSKVNGTIARIEYRGGIIEIPIWLLPGHAEDSITLNLGYGRTHAGRVGNNVGIDVYPIRTSDSPWFGAGARVTNTGR
TYLLVSTQDHWTLEGRDIYRVGEFKKFKEDPKYIAKEVYQEEYGRETPNYQSLQPGDDYTGRNAWGMTINLNACIGCNAC
VVACQAENNIAVVGKDQVSRGREMHWIRIDRYFAGEDLDNPSIYMMPVNCMQCEKAPCEVVCPVAATVHDYEGLNNMVYN
RCVGTKYCSNNCPYKVRRFNFLQYSDTTTETFKLAFNPDVTVRIRGVMEKCTYCVQRISGARIAAKRAAVQAGQSSYVIS
DGAIQTACEQACPTGAIVFGDINDSNSRVAKWKAEGHNYGLLGFLNTVPRTTYLARVRNPSEELEKVEG
;
1 
3 UNP A9WEV4_CHLAA A9WEV4 ? 3 
;MAQAQPLRTRPQDDGEAYLLPGETYTSISAKIGDVPLTPPLKTPKGWLAGFSVAFFMLMIFFVSVTWLFIRGVGIWGINI
PVGWGMDIINFVWWIGIGHAGTLISAILLLLNQGWRNSINRFAEAMTLFAVACAGLYPILHLGRPWLFYWLIPYPNTHGM
WPQFRSALAWDVFAISTYATVSLVFWLVGLIPDFATLRDRAKNIWVKRLYGIAALGWRGSARHWHRYEMASILLAGLSTP
LVVSVHSIISLDFAISQVPGWQVTVFPPYFVAGAVFAGFAMVLLLMIPVRTFYGFENYITLHHLDVMAKVMLTTGMIVVY
GYFMEVFASLYSGNEFEEYLLYNRLFGPSSWAYWGLLFCNAVAIQPLWFKKVRQNIPALLIISLIVSVGMWLERYVIIVI
SLERDFLPSSWDIYIPTIWDWSLYIGTFGLFFTLLFLFIRVLPMINIFEMRLFLYQETEKAKQRAGHGAHGHGHEQSPAH
GAATAD
;
1 
4 UNP A9WEV5_CHLAA A9WEV5 ? 4 
;MRNDVYGVMAEFPTPEALIEATRKAKAAGYTKMDAFSPFPIEEVIEEIAHGDTGVPRLVLLFGLIGAASGFILQYIGNLV
DYPLNVGGRPLDITNWPAMIPITFESGILLASFAAAIGMIVLNGLPSPYHPVFNVPRFQYASQDAFFLCIEATDPLFDRS
RTSQFLRSLNPMQVSEVAY
;
1 
5 UNP A9WEV6_CHLAA A9WEV6 ? 5 
;MQKPRLTSRMIRFGWVGLLVLLLTACHQDMYDQQKYTTYEPSSFFADGRSSRPNVPGTTPFEVVKTDEFLYTGLIDGQEV
DAMPFPVTKDLLLRGQLKYNIYCAVCHGEAGYGASMVAERGGIVPANFHQQRLREAPLSHFFVVITNGVYRGDPENGGYQ
SMYGYASRITPEDRWAIAAYIRALQLSQNATIDDVPPDQRAQLGN
;
1 
6 UNP A9WEV7_CHLAA A9WEV7 ? 6 
;MATTSISQTRIPQLGQVQMLGLAAAVIGIGVLAAGYFLSPTSFFESYIYGYYVAMTIPLGCLGFLMVQHLTGGAWGVTVR
RMLEAGAATLPIMGLLFIPIALGYFDTYKALGLEHPLYEWANPEVVTPGGAEFDPIIAHKVPWLSPLWVTARIAIFFIIW
SALALTLRAWSRQQDAGGDAKKLATRMRRLSGIGVALFVITVTFFSFDVAMSLDPHWFSTIYGAHYMANAGLMTLAFLAL
MMSRVRDAALFREYVSVKPIHDIGKLIFAFTVLWTYMSYGQLVIIWSGDVAEFTPWYVHRTQHGWVFVALALMLFAFALP
FFVLLFRGTKRNLNTLATIAGWIVVMRFVDMAWIILPEFREHLWDIAITDVAAPIGLIGLVIALFAANVQQAPLLPLRDP
NMEQLQNSGHH
;
1 
7 UNP A9WEV8_CHLAA A9WEV8 ? 7 
;MSYRPNYSASRYTAGRPAQPVRTARTMAEPSLSRLMIAGLMVFLVLSLVVLLAGRLPFTPQPAPVTGNTYRTYVNDARTL
LNSYGYTMEGKVHIPIDRAMDLIVERGLPVRE
;
1 
8 PDB 9ILT         9ILT   ? 8 ? 1 
# 
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 9ILT A 1 ? 219  ? A9WEV2 1 ? 219  ? 1 219  
2 2 9ILT B 1 ? 1029 ? A9WEV3 1 ? 1029 ? 1 1029 
3 3 9ILT C 1 ? 486  ? A9WEV4 1 ? 486  ? 1 486  
4 4 9ILT D 1 ? 179  ? A9WEV5 1 ? 179  ? 1 179  
5 5 9ILT E 1 ? 205  ? A9WEV6 1 ? 205  ? 1 205  
6 6 9ILT F 1 ? 411  ? A9WEV7 1 ? 411  ? 1 411  
7 7 9ILT G 1 ? 112  ? A9WEV8 1 ? 112  ? 1 112  
8 8 9ILT I 1 ? 37   ? 9ILT   1 ? 37   ? 1 37   
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   octameric 
_pdbx_struct_assembly.oligomeric_count     8 
# 
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)' 45190 ? 
1 MORE         -448  ? 
1 'SSA (A^2)'  85790 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'mass spectrometry' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 ASN A 8    ? PHE A 35   ? ASN A 8    PHE A 35   1 ? 28 
HELX_P HELX_P2   AA2 SER A 54   ? ASN A 60   ? SER A 54   ASN A 60   1 ? 7  
HELX_P HELX_P3   AA3 ASP A 65   ? CYS A 69   ? ASP A 65   CYS A 69   5 ? 5  
HELX_P HELX_P4   AA4 ALA A 83   ? SER A 92   ? ALA A 83   SER A 92   1 ? 10 
HELX_P HELX_P5   AA5 SER A 98   ? LEU A 100  ? SER A 98   LEU A 100  5 ? 3  
HELX_P HELX_P6   AA6 LEU A 101  ? SER A 107  ? LEU A 101  SER A 107  1 ? 7  
HELX_P HELX_P7   AA7 ASN A 129  ? LYS A 136  ? ASN A 129  LYS A 136  1 ? 8  
HELX_P HELX_P8   AA8 GLN A 146  ? MET A 150  ? GLN A 146  MET A 150  5 ? 5  
HELX_P HELX_P9   AA9 TYR A 160  ? ASN A 170  ? TYR A 160  ASN A 170  1 ? 11 
HELX_P HELX_P10  AB1 PRO A 171  ? TYR A 174  ? PRO A 171  TYR A 174  5 ? 4  
HELX_P HELX_P11  AB2 ASN A 191  ? GLY A 204  ? ASN A 191  GLY A 204  1 ? 14 
HELX_P HELX_P12  AB3 PRO A 207  ? THR A 212  ? PRO A 207  THR A 212  1 ? 6  
HELX_P HELX_P13  AB4 ASN A 213  ? CYS A 217  ? ASN A 213  CYS A 217  5 ? 5  
HELX_P HELX_P14  AB5 ASP B 141  ? TYR B 152  ? ASP B 141  TYR B 152  1 ? 12 
HELX_P HELX_P15  AB6 THR B 168  ? THR B 186  ? THR B 168  THR B 186  1 ? 19 
HELX_P HELX_P16  AB7 SER B 200  ? TYR B 214  ? SER B 200  TYR B 214  1 ? 15 
HELX_P HELX_P17  AB8 ARG B 227  ? GLY B 239  ? ARG B 227  GLY B 239  1 ? 13 
HELX_P HELX_P18  AB9 LEU B 248  ? ALA B 251  ? LEU B 248  ALA B 251  5 ? 4  
HELX_P HELX_P19  AC1 GLY B 267  ? LYS B 280  ? GLY B 267  LYS B 280  1 ? 14 
HELX_P HELX_P20  AC2 SER B 299  ? ALA B 304  ? SER B 299  ALA B 304  1 ? 6  
HELX_P HELX_P21  AC3 ASP B 314  ? LEU B 327  ? ASP B 314  LEU B 327  1 ? 14 
HELX_P HELX_P22  AC4 SER B 337  ? LEU B 351  ? SER B 337  LEU B 351  1 ? 15 
HELX_P HELX_P23  AC5 PRO B 367  ? LEU B 381  ? PRO B 367  LEU B 381  1 ? 15 
HELX_P HELX_P24  AC6 ASN B 400  ? ALA B 414  ? ASN B 400  ALA B 414  1 ? 15 
HELX_P HELX_P25  AC7 ASN B 426  ? ALA B 431  ? ASN B 426  ALA B 431  1 ? 6  
HELX_P HELX_P26  AC8 PRO B 432  ? LEU B 435  ? PRO B 432  LEU B 435  5 ? 4  
HELX_P HELX_P27  AC9 ARG B 436  ? ALA B 442  ? ARG B 436  ALA B 442  1 ? 7  
HELX_P HELX_P28  AD1 ASP B 455  ? ARG B 460  ? ASP B 455  ARG B 460  1 ? 6  
HELX_P HELX_P29  AD2 THR B 499  ? LEU B 508  ? THR B 499  LEU B 508  1 ? 10 
HELX_P HELX_P30  AD3 GLU B 514  ? LEU B 524  ? GLU B 514  LEU B 524  1 ? 11 
HELX_P HELX_P31  AD4 GLY B 528  ? ASN B 538  ? GLY B 528  ASN B 538  1 ? 11 
HELX_P HELX_P32  AD5 ASN B 554  ? ALA B 560  ? ASN B 554  ALA B 560  1 ? 7  
HELX_P HELX_P33  AD6 GLY B 583  ? ASN B 587  ? GLY B 583  ASN B 587  5 ? 5  
HELX_P HELX_P34  AD7 ASN B 588  ? LEU B 594  ? ASN B 588  LEU B 594  1 ? 7  
HELX_P HELX_P35  AD8 SER B 610  ? GLY B 619  ? SER B 610  GLY B 619  1 ? 10 
HELX_P HELX_P36  AD9 THR B 630  ? ALA B 632  ? THR B 630  ALA B 632  5 ? 3  
HELX_P HELX_P37  AE1 ASP B 633  ? SER B 645  ? ASP B 633  SER B 645  1 ? 13 
HELX_P HELX_P38  AE2 LYS B 646  ? ASN B 648  ? LYS B 646  ASN B 648  5 ? 3  
HELX_P HELX_P39  AE3 PHE B 744  ? ASP B 750  ? PHE B 744  ASP B 750  1 ? 7  
HELX_P HELX_P40  AE4 LYS B 752  ? GLY B 764  ? LYS B 752  GLY B 764  1 ? 13 
HELX_P HELX_P41  AE5 ASN B 798  ? ASN B 808  ? ASN B 798  ASN B 808  1 ? 11 
HELX_P HELX_P42  AE6 GLY B 814  ? ARG B 820  ? GLY B 814  ARG B 820  1 ? 7  
HELX_P HELX_P43  AE7 TYR B 879  ? CYS B 882  ? TYR B 879  CYS B 882  5 ? 4  
HELX_P HELX_P44  AE8 LYS B 886  ? ASN B 891  ? LYS B 886  ASN B 891  1 ? 6  
HELX_P HELX_P45  AE9 THR B 909  ? PHE B 916  ? THR B 909  PHE B 916  1 ? 8  
HELX_P HELX_P46  AF1 CYS B 934  ? ALA B 952  ? CYS B 934  ALA B 952  1 ? 19 
HELX_P HELX_P47  AF2 THR B 966  ? CYS B 972  ? THR B 966  CYS B 972  1 ? 7  
HELX_P HELX_P48  AF3 SER B 987  ? ALA B 994  ? SER B 987  ALA B 994  1 ? 8  
HELX_P HELX_P49  AF4 SER B 1021 ? LYS B 1026 ? SER B 1021 LYS B 1026 1 ? 6  
HELX_P HELX_P50  AF5 THR C 24   ? ASP C 34   ? THR C 24   ASP C 34   1 ? 11 
HELX_P HELX_P51  AF6 PRO C 39   ? THR C 43   ? PRO C 39   THR C 43   5 ? 5  
HELX_P HELX_P52  AF7 PRO C 44   ? GLY C 72   ? PRO C 44   GLY C 72   1 ? 29 
HELX_P HELX_P53  AF8 VAL C 73   ? TRP C 76   ? VAL C 73   TRP C 76   5 ? 4  
HELX_P HELX_P54  AF9 GLY C 85   ? ASN C 112  ? GLY C 85   ASN C 112  1 ? 28 
HELX_P HELX_P55  AG1 GLN C 113  ? ASN C 117  ? GLN C 113  ASN C 117  5 ? 5  
HELX_P HELX_P56  AG2 ILE C 119  ? GLY C 135  ? ILE C 119  GLY C 135  1 ? 17 
HELX_P HELX_P57  AG3 LEU C 136  ? HIS C 141  ? LEU C 136  HIS C 141  1 ? 6  
HELX_P HELX_P58  AG4 LEU C 142  ? GLY C 143  ? LEU C 142  GLY C 143  5 ? 2  
HELX_P HELX_P59  AG5 ARG C 144  ? ILE C 152  ? ARG C 144  ILE C 152  5 ? 9  
HELX_P HELX_P60  AG6 SER C 166  ? ALA C 201  ? SER C 166  ALA C 201  1 ? 36 
HELX_P HELX_P61  AG7 ARG C 208  ? LEU C 215  ? ARG C 208  LEU C 215  1 ? 8  
HELX_P HELX_P62  AG8 HIS C 223  ? ILE C 255  ? HIS C 223  ILE C 255  1 ? 33 
HELX_P HELX_P63  AG9 VAL C 265  ? TYR C 293  ? VAL C 265  TYR C 293  1 ? 29 
HELX_P HELX_P64  AH1 THR C 300  ? SER C 332  ? THR C 300  SER C 332  1 ? 33 
HELX_P HELX_P65  AH2 ASN C 334  ? GLY C 347  ? ASN C 334  GLY C 347  1 ? 14 
HELX_P HELX_P66  AH3 SER C 349  ? ASN C 360  ? SER C 349  ASN C 360  1 ? 12 
HELX_P HELX_P67  AH4 ILE C 364  ? TRP C 368  ? ILE C 364  TRP C 368  5 ? 5  
HELX_P HELX_P68  AH5 PHE C 369  ? GLN C 374  ? PHE C 369  GLN C 374  1 ? 6  
HELX_P HELX_P69  AH6 ASN C 375  ? ARG C 404  ? ASN C 375  ARG C 404  1 ? 30 
HELX_P HELX_P70  AH7 LEU C 407  ? TRP C 411  ? LEU C 407  TRP C 411  5 ? 5  
HELX_P HELX_P71  AH8 ILE C 418  ? LEU C 442  ? ILE C 418  LEU C 442  1 ? 25 
HELX_P HELX_P72  AH9 ASN C 446  ? GLN C 463  ? ASN C 446  GLN C 463  1 ? 18 
HELX_P HELX_P73  AI1 THR D 14   ? ALA D 28   ? THR D 14   ALA D 28   1 ? 15 
HELX_P HELX_P74  AI2 GLU D 43   ? ALA D 49   ? GLU D 43   ALA D 49   1 ? 7  
HELX_P HELX_P75  AI3 GLY D 54   ? VAL D 80   ? GLY D 54   VAL D 80   1 ? 27 
HELX_P HELX_P76  AI4 ASP D 92   ? TRP D 96   ? ASP D 92   TRP D 96   5 ? 5  
HELX_P HELX_P77  AI5 MET D 99   ? ASN D 123  ? MET D 99   ASN D 123  1 ? 25 
HELX_P HELX_P78  AI6 HIS D 130  ? GLN D 143  ? HIS D 130  GLN D 143  5 ? 14 
HELX_P HELX_P79  AI7 ARG D 159  ? LEU D 169  ? ARG D 159  LEU D 169  1 ? 11 
HELX_P HELX_P80  AI8 THR E 88   ? CYS E 103  ? THR E 88   CYS E 103  1 ? 16 
HELX_P HELX_P81  AI9 SER E 115  ? ARG E 120  ? SER E 115  ARG E 120  1 ? 6  
HELX_P HELX_P82  AJ1 GLN E 130  ? GLU E 135  ? GLN E 130  GLU E 135  1 ? 6  
HELX_P HELX_P83  AJ2 PRO E 137  ? ASN E 147  ? PRO E 137  ASN E 147  1 ? 11 
HELX_P HELX_P84  AJ3 THR E 170  ? GLN E 188  ? THR E 170  GLN E 188  1 ? 19 
HELX_P HELX_P85  AJ4 PRO F 12   ? SER F 39   ? PRO F 12   SER F 39   1 ? 28 
HELX_P HELX_P86  AJ5 SER F 39   ? MET F 55   ? SER F 39   MET F 55   1 ? 17 
HELX_P HELX_P87  AJ6 MET F 55   ? THR F 71   ? MET F 55   THR F 71   1 ? 17 
HELX_P HELX_P88  AJ7 GLY F 73   ? VAL F 79   ? GLY F 73   VAL F 79   1 ? 7  
HELX_P HELX_P89  AJ8 VAL F 79   ? ALA F 88   ? VAL F 79   ALA F 88   1 ? 10 
HELX_P HELX_P90  AJ9 THR F 89   ? PHE F 97   ? THR F 89   PHE F 97   1 ? 9  
HELX_P HELX_P91  AK1 PHE F 97   ? PHE F 105  ? PHE F 97   PHE F 105  1 ? 9  
HELX_P HELX_P92  AK2 TYR F 118  ? ALA F 121  ? TYR F 118  ALA F 121  5 ? 4  
HELX_P HELX_P93  AK3 ASN F 122  ? THR F 127  ? ASN F 122  THR F 127  1 ? 6  
HELX_P HELX_P94  AK4 ASP F 134  ? HIS F 139  ? ASP F 134  HIS F 139  1 ? 6  
HELX_P HELX_P95  AK5 SER F 145  ? ASP F 175  ? SER F 145  ASP F 175  1 ? 31 
HELX_P HELX_P96  AK6 THR F 185  ? ALA F 210  ? THR F 185  ALA F 210  1 ? 26 
HELX_P HELX_P97  AK7 MET F 211  ? ASP F 214  ? MET F 211  ASP F 214  5 ? 4  
HELX_P HELX_P98  AK8 GLY F 223  ? VAL F 245  ? GLY F 223  VAL F 245  1 ? 23 
HELX_P HELX_P99  AK9 LEU F 250  ? VAL F 255  ? LEU F 250  VAL F 255  1 ? 6  
HELX_P HELX_P100 AL1 SER F 256  ? GLY F 288  ? SER F 256  GLY F 288  1 ? 33 
HELX_P HELX_P101 AL2 PHE F 293  ? ARG F 300  ? PHE F 293  ARG F 300  1 ? 8  
HELX_P HELX_P102 AL3 GLY F 304  ? ALA F 316  ? GLY F 304  ALA F 316  1 ? 13 
HELX_P HELX_P103 AL4 PHE F 317  ? LEU F 324  ? PHE F 317  LEU F 324  1 ? 8  
HELX_P HELX_P104 AL5 ASN F 332  ? GLU F 361  ? ASN F 332  GLU F 361  1 ? 30 
HELX_P HELX_P105 AL6 ILE F 368  ? ALA F 392  ? ILE F 368  ALA F 392  1 ? 25 
HELX_P HELX_P106 AL7 ASP F 399  ? GLN F 406  ? ASP F 399  GLN F 406  5 ? 8  
HELX_P HELX_P107 AL8 SER G 33   ? ARG G 55   ? SER G 33   ARG G 55   1 ? 23 
HELX_P HELX_P108 AL9 TYR G 70   ? LEU G 81   ? TYR G 70   LEU G 81   1 ? 12 
HELX_P HELX_P109 AM1 ARG G 98   ? GLY G 107  ? ARG G 98   GLY G 107  1 ? 10 
HELX_P HELX_P110 AM2 LYS H 12   ? ALA H 34   ? LYS I 12   ALA I 34   1 ? 23 
# 
_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 none ? A CYS 66  SG  ? ? ? 1_555 L HEC . CAB ? ? A CYS 66  A HEC 304  1_555 ? ? ? ? ? ? ? 1.766 ? ? 
covale2  covale none ? A CYS 87  SG  ? ? ? 1_555 M HEC . CAB ? ? A CYS 87  A HEC 305  1_555 ? ? ? ? ? ? ? 1.767 ? ? 
covale3  covale none ? A CYS 164 SG  ? ? ? 1_555 J HEC . CAB ? ? A CYS 164 A HEC 302  1_555 ? ? ? ? ? ? ? 1.766 ? ? 
covale4  covale none ? A CYS 167 SG  ? ? ? 1_555 J HEC . CAC ? ? A CYS 167 A HEC 302  1_555 ? ? ? ? ? ? ? 1.766 ? ? 
covale5  covale none ? A CYS 214 SG  ? ? ? 1_555 I HEC . CAB ? ? A CYS 214 A HEC 301  1_555 ? ? ? ? ? ? ? 1.765 ? ? 
covale6  covale none ? E CYS 103 SG  ? ? ? 1_555 R HEC . CAB ? ? E CYS 103 E HEC 301  1_555 ? ? ? ? ? ? ? 1.766 ? ? 
covale7  covale none ? E CYS 106 SG  ? ? ? 1_555 R HEC . CAC ? ? E CYS 106 E HEC 301  1_555 ? ? ? ? ? ? ? 1.767 ? ? 
metalc1  metalc ?    ? A HIS 55  NE2 ? ? ? 1_555 L HEC . FE  ? ? A HIS 55  A HEC 304  1_555 ? ? ? ? ? ? ? 2.114 ? ? 
metalc2  metalc ?    ? A HIS 58  NE2 ? ? ? 1_555 M HEC . FE  ? ? A HIS 58  A HEC 305  1_555 ? ? ? ? ? ? ? 2.100 ? ? 
metalc3  metalc ?    ? A HIS 70  NE2 ? ? ? 1_555 L HEC . FE  ? ? A HIS 70  A HEC 304  1_555 ? ? ? ? ? ? ? 2.153 ? ? 
metalc4  metalc ?    ? A HIS 91  NE2 ? ? ? 1_555 M HEC . FE  ? ? A HIS 91  A HEC 305  1_555 ? ? ? ? ? ? ? 2.104 ? ? 
metalc5  metalc ?    ? A HIS 130 NE2 ? ? ? 1_555 K HEC . FE  ? ? A HIS 130 A HEC 303  1_555 ? ? ? ? ? ? ? 2.101 ? ? 
metalc6  metalc ?    ? A HIS 133 NE2 ? ? ? 1_555 J HEC . FE  ? ? A HIS 133 A HEC 302  1_555 ? ? ? ? ? ? ? 2.124 ? ? 
metalc7  metalc ?    ? A HIS 144 NE2 ? ? ? 1_555 K HEC . FE  ? ? A HIS 144 A HEC 303  1_555 ? ? ? ? ? ? ? 2.092 ? ? 
metalc8  metalc ?    ? A MET 161 SD  ? ? ? 1_555 I HEC . FE  ? ? A MET 161 A HEC 301  1_555 ? ? ? ? ? ? ? 2.096 ? ? 
metalc9  metalc ?    ? A HIS 168 NE2 ? ? ? 1_555 J HEC . FE  ? ? A HIS 168 A HEC 302  1_555 ? ? ? ? ? ? ? 2.159 ? ? 
metalc10 metalc ?    ? A HIS 218 NE2 ? ? ? 1_555 I HEC . FE  ? ? A HIS 218 A HEC 301  1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc11 metalc ?    ? B CYS 794 SG  ? ? ? 1_555 N SF4 . FE4 ? ? B CYS 794 B SF4 1101 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc12 metalc ?    ? B CYS 797 SG  ? ? ? 1_555 N SF4 . FE1 ? ? B CYS 797 B SF4 1101 1_555 ? ? ? ? ? ? ? 2.264 ? ? 
metalc13 metalc ?    ? B CYS 800 SG  ? ? ? 1_555 N SF4 . FE3 ? ? B CYS 800 B SF4 1101 1_555 ? ? ? ? ? ? ? 2.275 ? ? 
metalc14 metalc ?    ? B CYS 804 SG  ? ? ? 1_555 O SF4 . FE3 ? ? B CYS 804 B SF4 1102 1_555 ? ? ? ? ? ? ? 2.271 ? ? 
metalc15 metalc ?    ? B CYS 850 SG  ? ? ? 1_555 P SF4 . FE1 ? ? B CYS 850 B SF4 1103 1_555 ? ? ? ? ? ? ? 2.270 ? ? 
metalc16 metalc ?    ? B CYS 853 SG  ? ? ? 1_555 P SF4 . FE4 ? ? B CYS 853 B SF4 1103 1_555 ? ? ? ? ? ? ? 2.272 ? ? 
metalc17 metalc ?    ? B CYS 858 SG  ? ? ? 1_555 P SF4 . FE2 ? ? B CYS 858 B SF4 1103 1_555 ? ? ? ? ? ? ? 2.266 ? ? 
metalc18 metalc ?    ? B CYS 862 SG  ? ? ? 1_555 Q F3S . FE1 ? ? B CYS 862 B F3S 1104 1_555 ? ? ? ? ? ? ? 2.010 ? ? 
metalc19 metalc ?    ? B CYS 892 SG  ? ? ? 1_555 P SF4 . FE3 ? ? B CYS 892 B SF4 1103 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc20 metalc ?    ? B CYS 931 SG  ? ? ? 1_555 O SF4 . FE2 ? ? B CYS 931 B SF4 1102 1_555 ? ? ? ? ? ? ? 2.267 ? ? 
metalc21 metalc ?    ? B CYS 934 SG  ? ? ? 1_555 O SF4 . FE1 ? ? B CYS 934 B SF4 1102 1_555 ? ? ? ? ? ? ? 2.273 ? ? 
metalc22 metalc ?    ? B CYS 968 SG  ? ? ? 1_555 O SF4 . FE4 ? ? B CYS 968 B SF4 1102 1_555 ? ? ? ? ? ? ? 2.273 ? ? 
metalc23 metalc ?    ? B CYS 972 SG  ? ? ? 1_555 N SF4 . FE2 ? ? B CYS 972 B SF4 1101 1_555 ? ? ? ? ? ? ? 2.264 ? ? 
metalc24 metalc ?    ? E HIS 107 ND1 ? ? ? 1_555 R HEC . FE  ? ? E HIS 107 E HEC 301  1_555 ? ? ? ? ? ? ? 2.386 ? ? 
metalc25 metalc ?    ? E HIS 107 NE2 ? ? ? 1_555 R HEC . FE  ? ? E HIS 107 E HEC 301  1_555 ? ? ? ? ? ? ? 2.251 ? ? 
metalc26 metalc ?    ? E MET 162 SD  ? ? ? 1_555 R HEC . FE  ? ? E MET 162 E HEC 301  1_555 ? ? ? ? ? ? ? 2.253 ? ? 
# 
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   NE2 ? A HIS 55  ? A HIS 55   ? 1_555 FE  ? L HEC . ? A HEC 304  ? 1_555 NA  ? L HEC .   ? A HEC 304  ? 1_555 102.4 ? 
2   NE2 ? A HIS 55  ? A HIS 55   ? 1_555 FE  ? L HEC . ? A HEC 304  ? 1_555 NB  ? L HEC .   ? A HEC 304  ? 1_555 98.3  ? 
3   NA  ? L HEC .   ? A HEC 304  ? 1_555 FE  ? L HEC . ? A HEC 304  ? 1_555 NB  ? L HEC .   ? A HEC 304  ? 1_555 90.1  ? 
4   NE2 ? A HIS 55  ? A HIS 55   ? 1_555 FE  ? L HEC . ? A HEC 304  ? 1_555 NC  ? L HEC .   ? A HEC 304  ? 1_555 84.2  ? 
5   NA  ? L HEC .   ? A HEC 304  ? 1_555 FE  ? L HEC . ? A HEC 304  ? 1_555 NC  ? L HEC .   ? A HEC 304  ? 1_555 173.4 ? 
6   NB  ? L HEC .   ? A HEC 304  ? 1_555 FE  ? L HEC . ? A HEC 304  ? 1_555 NC  ? L HEC .   ? A HEC 304  ? 1_555 88.9  ? 
7   NE2 ? A HIS 55  ? A HIS 55   ? 1_555 FE  ? L HEC . ? A HEC 304  ? 1_555 ND  ? L HEC .   ? A HEC 304  ? 1_555 87.7  ? 
8   NA  ? L HEC .   ? A HEC 304  ? 1_555 FE  ? L HEC . ? A HEC 304  ? 1_555 ND  ? L HEC .   ? A HEC 304  ? 1_555 90.1  ? 
9   NB  ? L HEC .   ? A HEC 304  ? 1_555 FE  ? L HEC . ? A HEC 304  ? 1_555 ND  ? L HEC .   ? A HEC 304  ? 1_555 173.7 ? 
10  NC  ? L HEC .   ? A HEC 304  ? 1_555 FE  ? L HEC . ? A HEC 304  ? 1_555 ND  ? L HEC .   ? A HEC 304  ? 1_555 90.1  ? 
11  NE2 ? A HIS 55  ? A HIS 55   ? 1_555 FE  ? L HEC . ? A HEC 304  ? 1_555 NE2 ? A HIS 70  ? A HIS 70   ? 1_555 174.2 ? 
12  NA  ? L HEC .   ? A HEC 304  ? 1_555 FE  ? L HEC . ? A HEC 304  ? 1_555 NE2 ? A HIS 70  ? A HIS 70   ? 1_555 83.2  ? 
13  NB  ? L HEC .   ? A HEC 304  ? 1_555 FE  ? L HEC . ? A HEC 304  ? 1_555 NE2 ? A HIS 70  ? A HIS 70   ? 1_555 83.2  ? 
14  NC  ? L HEC .   ? A HEC 304  ? 1_555 FE  ? L HEC . ? A HEC 304  ? 1_555 NE2 ? A HIS 70  ? A HIS 70   ? 1_555 90.2  ? 
15  ND  ? L HEC .   ? A HEC 304  ? 1_555 FE  ? L HEC . ? A HEC 304  ? 1_555 NE2 ? A HIS 70  ? A HIS 70   ? 1_555 90.6  ? 
16  NE2 ? A HIS 58  ? A HIS 58   ? 1_555 FE  ? M HEC . ? A HEC 305  ? 1_555 NA  ? M HEC .   ? A HEC 305  ? 1_555 88.4  ? 
17  NE2 ? A HIS 58  ? A HIS 58   ? 1_555 FE  ? M HEC . ? A HEC 305  ? 1_555 NB  ? M HEC .   ? A HEC 305  ? 1_555 84.0  ? 
18  NA  ? M HEC .   ? A HEC 305  ? 1_555 FE  ? M HEC . ? A HEC 305  ? 1_555 NB  ? M HEC .   ? A HEC 305  ? 1_555 89.1  ? 
19  NE2 ? A HIS 58  ? A HIS 58   ? 1_555 FE  ? M HEC . ? A HEC 305  ? 1_555 NC  ? M HEC .   ? A HEC 305  ? 1_555 95.8  ? 
20  NA  ? M HEC .   ? A HEC 305  ? 1_555 FE  ? M HEC . ? A HEC 305  ? 1_555 NC  ? M HEC .   ? A HEC 305  ? 1_555 175.8 ? 
21  NB  ? M HEC .   ? A HEC 305  ? 1_555 FE  ? M HEC . ? A HEC 305  ? 1_555 NC  ? M HEC .   ? A HEC 305  ? 1_555 90.4  ? 
22  NE2 ? A HIS 58  ? A HIS 58   ? 1_555 FE  ? M HEC . ? A HEC 305  ? 1_555 ND  ? M HEC .   ? A HEC 305  ? 1_555 98.7  ? 
23  NA  ? M HEC .   ? A HEC 305  ? 1_555 FE  ? M HEC . ? A HEC 305  ? 1_555 ND  ? M HEC .   ? A HEC 305  ? 1_555 90.9  ? 
24  NB  ? M HEC .   ? A HEC 305  ? 1_555 FE  ? M HEC . ? A HEC 305  ? 1_555 ND  ? M HEC .   ? A HEC 305  ? 1_555 177.4 ? 
25  NC  ? M HEC .   ? A HEC 305  ? 1_555 FE  ? M HEC . ? A HEC 305  ? 1_555 ND  ? M HEC .   ? A HEC 305  ? 1_555 89.4  ? 
26  NE2 ? A HIS 58  ? A HIS 58   ? 1_555 FE  ? M HEC . ? A HEC 305  ? 1_555 NE2 ? A HIS 91  ? A HIS 91   ? 1_555 147.4 ? 
27  NA  ? M HEC .   ? A HEC 305  ? 1_555 FE  ? M HEC . ? A HEC 305  ? 1_555 NE2 ? A HIS 91  ? A HIS 91   ? 1_555 82.6  ? 
28  NB  ? M HEC .   ? A HEC 305  ? 1_555 FE  ? M HEC . ? A HEC 305  ? 1_555 NE2 ? A HIS 91  ? A HIS 91   ? 1_555 64.7  ? 
29  NC  ? M HEC .   ? A HEC 305  ? 1_555 FE  ? M HEC . ? A HEC 305  ? 1_555 NE2 ? A HIS 91  ? A HIS 91   ? 1_555 93.4  ? 
30  ND  ? M HEC .   ? A HEC 305  ? 1_555 FE  ? M HEC . ? A HEC 305  ? 1_555 NE2 ? A HIS 91  ? A HIS 91   ? 1_555 112.7 ? 
31  NE2 ? A HIS 130 ? A HIS 130  ? 1_555 FE  ? K HEC . ? A HEC 303  ? 1_555 NA  ? K HEC .   ? A HEC 303  ? 1_555 91.2  ? 
32  NE2 ? A HIS 130 ? A HIS 130  ? 1_555 FE  ? K HEC . ? A HEC 303  ? 1_555 NB  ? K HEC .   ? A HEC 303  ? 1_555 108.7 ? 
33  NA  ? K HEC .   ? A HEC 303  ? 1_555 FE  ? K HEC . ? A HEC 303  ? 1_555 NB  ? K HEC .   ? A HEC 303  ? 1_555 90.6  ? 
34  NE2 ? A HIS 130 ? A HIS 130  ? 1_555 FE  ? K HEC . ? A HEC 303  ? 1_555 NC  ? K HEC .   ? A HEC 303  ? 1_555 101.1 ? 
35  NA  ? K HEC .   ? A HEC 303  ? 1_555 FE  ? K HEC . ? A HEC 303  ? 1_555 NC  ? K HEC .   ? A HEC 303  ? 1_555 167.6 ? 
36  NB  ? K HEC .   ? A HEC 303  ? 1_555 FE  ? K HEC . ? A HEC 303  ? 1_555 NC  ? K HEC .   ? A HEC 303  ? 1_555 86.6  ? 
37  NE2 ? A HIS 130 ? A HIS 130  ? 1_555 FE  ? K HEC . ? A HEC 303  ? 1_555 ND  ? K HEC .   ? A HEC 303  ? 1_555 83.6  ? 
38  NA  ? K HEC .   ? A HEC 303  ? 1_555 FE  ? K HEC . ? A HEC 303  ? 1_555 ND  ? K HEC .   ? A HEC 303  ? 1_555 88.5  ? 
39  NB  ? K HEC .   ? A HEC 303  ? 1_555 FE  ? K HEC . ? A HEC 303  ? 1_555 ND  ? K HEC .   ? A HEC 303  ? 1_555 167.7 ? 
40  NC  ? K HEC .   ? A HEC 303  ? 1_555 FE  ? K HEC . ? A HEC 303  ? 1_555 ND  ? K HEC .   ? A HEC 303  ? 1_555 91.7  ? 
41  NE2 ? A HIS 130 ? A HIS 130  ? 1_555 FE  ? K HEC . ? A HEC 303  ? 1_555 NE2 ? A HIS 144 ? A HIS 144  ? 1_555 158.6 ? 
42  NA  ? K HEC .   ? A HEC 303  ? 1_555 FE  ? K HEC . ? A HEC 303  ? 1_555 NE2 ? A HIS 144 ? A HIS 144  ? 1_555 73.2  ? 
43  NB  ? K HEC .   ? A HEC 303  ? 1_555 FE  ? K HEC . ? A HEC 303  ? 1_555 NE2 ? A HIS 144 ? A HIS 144  ? 1_555 86.6  ? 
44  NC  ? K HEC .   ? A HEC 303  ? 1_555 FE  ? K HEC . ? A HEC 303  ? 1_555 NE2 ? A HIS 144 ? A HIS 144  ? 1_555 94.5  ? 
45  ND  ? K HEC .   ? A HEC 303  ? 1_555 FE  ? K HEC . ? A HEC 303  ? 1_555 NE2 ? A HIS 144 ? A HIS 144  ? 1_555 81.5  ? 
46  NE2 ? A HIS 133 ? A HIS 133  ? 1_555 FE  ? J HEC . ? A HEC 302  ? 1_555 NA  ? J HEC .   ? A HEC 302  ? 1_555 96.7  ? 
47  NE2 ? A HIS 133 ? A HIS 133  ? 1_555 FE  ? J HEC . ? A HEC 302  ? 1_555 NB  ? J HEC .   ? A HEC 302  ? 1_555 82.2  ? 
48  NA  ? J HEC .   ? A HEC 302  ? 1_555 FE  ? J HEC . ? A HEC 302  ? 1_555 NB  ? J HEC .   ? A HEC 302  ? 1_555 89.7  ? 
49  NE2 ? A HIS 133 ? A HIS 133  ? 1_555 FE  ? J HEC . ? A HEC 302  ? 1_555 NC  ? J HEC .   ? A HEC 302  ? 1_555 75.6  ? 
50  NA  ? J HEC .   ? A HEC 302  ? 1_555 FE  ? J HEC . ? A HEC 302  ? 1_555 NC  ? J HEC .   ? A HEC 302  ? 1_555 172.3 ? 
51  NB  ? J HEC .   ? A HEC 302  ? 1_555 FE  ? J HEC . ? A HEC 302  ? 1_555 NC  ? J HEC .   ? A HEC 302  ? 1_555 88.5  ? 
52  NE2 ? A HIS 133 ? A HIS 133  ? 1_555 FE  ? J HEC . ? A HEC 302  ? 1_555 ND  ? J HEC .   ? A HEC 302  ? 1_555 88.8  ? 
53  NA  ? J HEC .   ? A HEC 302  ? 1_555 FE  ? J HEC . ? A HEC 302  ? 1_555 ND  ? J HEC .   ? A HEC 302  ? 1_555 90.4  ? 
54  NB  ? J HEC .   ? A HEC 302  ? 1_555 FE  ? J HEC . ? A HEC 302  ? 1_555 ND  ? J HEC .   ? A HEC 302  ? 1_555 171.0 ? 
55  NC  ? J HEC .   ? A HEC 302  ? 1_555 FE  ? J HEC . ? A HEC 302  ? 1_555 ND  ? J HEC .   ? A HEC 302  ? 1_555 90.3  ? 
56  NE2 ? A HIS 133 ? A HIS 133  ? 1_555 FE  ? J HEC . ? A HEC 302  ? 1_555 NE2 ? A HIS 168 ? A HIS 168  ? 1_555 166.2 ? 
57  NA  ? J HEC .   ? A HEC 302  ? 1_555 FE  ? J HEC . ? A HEC 302  ? 1_555 NE2 ? A HIS 168 ? A HIS 168  ? 1_555 87.4  ? 
58  NB  ? J HEC .   ? A HEC 302  ? 1_555 FE  ? J HEC . ? A HEC 302  ? 1_555 NE2 ? A HIS 168 ? A HIS 168  ? 1_555 84.6  ? 
59  NC  ? J HEC .   ? A HEC 302  ? 1_555 FE  ? J HEC . ? A HEC 302  ? 1_555 NE2 ? A HIS 168 ? A HIS 168  ? 1_555 99.9  ? 
60  ND  ? J HEC .   ? A HEC 302  ? 1_555 FE  ? J HEC . ? A HEC 302  ? 1_555 NE2 ? A HIS 168 ? A HIS 168  ? 1_555 104.4 ? 
61  SD  ? A MET 161 ? A MET 161  ? 1_555 FE  ? I HEC . ? A HEC 301  ? 1_555 NA  ? I HEC .   ? A HEC 301  ? 1_555 100.5 ? 
62  SD  ? A MET 161 ? A MET 161  ? 1_555 FE  ? I HEC . ? A HEC 301  ? 1_555 NB  ? I HEC .   ? A HEC 301  ? 1_555 90.7  ? 
63  NA  ? I HEC .   ? A HEC 301  ? 1_555 FE  ? I HEC . ? A HEC 301  ? 1_555 NB  ? I HEC .   ? A HEC 301  ? 1_555 87.5  ? 
64  SD  ? A MET 161 ? A MET 161  ? 1_555 FE  ? I HEC . ? A HEC 301  ? 1_555 NC  ? I HEC .   ? A HEC 301  ? 1_555 95.0  ? 
65  NA  ? I HEC .   ? A HEC 301  ? 1_555 FE  ? I HEC . ? A HEC 301  ? 1_555 NC  ? I HEC .   ? A HEC 301  ? 1_555 164.1 ? 
66  NB  ? I HEC .   ? A HEC 301  ? 1_555 FE  ? I HEC . ? A HEC 301  ? 1_555 NC  ? I HEC .   ? A HEC 301  ? 1_555 88.9  ? 
67  SD  ? A MET 161 ? A MET 161  ? 1_555 FE  ? I HEC . ? A HEC 301  ? 1_555 ND  ? I HEC .   ? A HEC 301  ? 1_555 100.1 ? 
68  NA  ? I HEC .   ? A HEC 301  ? 1_555 FE  ? I HEC . ? A HEC 301  ? 1_555 ND  ? I HEC .   ? A HEC 301  ? 1_555 91.1  ? 
69  NB  ? I HEC .   ? A HEC 301  ? 1_555 FE  ? I HEC . ? A HEC 301  ? 1_555 ND  ? I HEC .   ? A HEC 301  ? 1_555 169.2 ? 
70  NC  ? I HEC .   ? A HEC 301  ? 1_555 FE  ? I HEC . ? A HEC 301  ? 1_555 ND  ? I HEC .   ? A HEC 301  ? 1_555 89.5  ? 
71  SD  ? A MET 161 ? A MET 161  ? 1_555 FE  ? I HEC . ? A HEC 301  ? 1_555 NE2 ? A HIS 218 ? A HIS 218  ? 1_555 175.9 ? 
72  NA  ? I HEC .   ? A HEC 301  ? 1_555 FE  ? I HEC . ? A HEC 301  ? 1_555 NE2 ? A HIS 218 ? A HIS 218  ? 1_555 78.5  ? 
73  NB  ? I HEC .   ? A HEC 301  ? 1_555 FE  ? I HEC . ? A HEC 301  ? 1_555 NE2 ? A HIS 218 ? A HIS 218  ? 1_555 85.2  ? 
74  NC  ? I HEC .   ? A HEC 301  ? 1_555 FE  ? I HEC . ? A HEC 301  ? 1_555 NE2 ? A HIS 218 ? A HIS 218  ? 1_555 85.8  ? 
75  ND  ? I HEC .   ? A HEC 301  ? 1_555 FE  ? I HEC . ? A HEC 301  ? 1_555 NE2 ? A HIS 218 ? A HIS 218  ? 1_555 84.0  ? 
76  SG  ? B CYS 794 ? B CYS 794  ? 1_555 FE4 ? N SF4 . ? B SF4 1101 ? 1_555 S1  ? N SF4 .   ? B SF4 1101 ? 1_555 112.1 ? 
77  SG  ? B CYS 794 ? B CYS 794  ? 1_555 FE4 ? N SF4 . ? B SF4 1101 ? 1_555 S2  ? N SF4 .   ? B SF4 1101 ? 1_555 113.2 ? 
78  S1  ? N SF4 .   ? B SF4 1101 ? 1_555 FE4 ? N SF4 . ? B SF4 1101 ? 1_555 S2  ? N SF4 .   ? B SF4 1101 ? 1_555 104.0 ? 
79  SG  ? B CYS 794 ? B CYS 794  ? 1_555 FE4 ? N SF4 . ? B SF4 1101 ? 1_555 S3  ? N SF4 .   ? B SF4 1101 ? 1_555 118.0 ? 
80  S1  ? N SF4 .   ? B SF4 1101 ? 1_555 FE4 ? N SF4 . ? B SF4 1101 ? 1_555 S3  ? N SF4 .   ? B SF4 1101 ? 1_555 104.0 ? 
81  S2  ? N SF4 .   ? B SF4 1101 ? 1_555 FE4 ? N SF4 . ? B SF4 1101 ? 1_555 S3  ? N SF4 .   ? B SF4 1101 ? 1_555 104.0 ? 
82  SG  ? B CYS 797 ? B CYS 797  ? 1_555 FE1 ? N SF4 . ? B SF4 1101 ? 1_555 S2  ? N SF4 .   ? B SF4 1101 ? 1_555 132.4 ? 
83  SG  ? B CYS 797 ? B CYS 797  ? 1_555 FE1 ? N SF4 . ? B SF4 1101 ? 1_555 S3  ? N SF4 .   ? B SF4 1101 ? 1_555 110.5 ? 
84  S2  ? N SF4 .   ? B SF4 1101 ? 1_555 FE1 ? N SF4 . ? B SF4 1101 ? 1_555 S3  ? N SF4 .   ? B SF4 1101 ? 1_555 104.1 ? 
85  SG  ? B CYS 797 ? B CYS 797  ? 1_555 FE1 ? N SF4 . ? B SF4 1101 ? 1_555 S4  ? N SF4 .   ? B SF4 1101 ? 1_555 98.1  ? 
86  S2  ? N SF4 .   ? B SF4 1101 ? 1_555 FE1 ? N SF4 . ? B SF4 1101 ? 1_555 S4  ? N SF4 .   ? B SF4 1101 ? 1_555 104.1 ? 
87  S3  ? N SF4 .   ? B SF4 1101 ? 1_555 FE1 ? N SF4 . ? B SF4 1101 ? 1_555 S4  ? N SF4 .   ? B SF4 1101 ? 1_555 104.4 ? 
88  SG  ? B CYS 800 ? B CYS 800  ? 1_555 FE3 ? N SF4 . ? B SF4 1101 ? 1_555 S1  ? N SF4 .   ? B SF4 1101 ? 1_555 123.6 ? 
89  SG  ? B CYS 800 ? B CYS 800  ? 1_555 FE3 ? N SF4 . ? B SF4 1101 ? 1_555 S2  ? N SF4 .   ? B SF4 1101 ? 1_555 112.9 ? 
90  S1  ? N SF4 .   ? B SF4 1101 ? 1_555 FE3 ? N SF4 . ? B SF4 1101 ? 1_555 S2  ? N SF4 .   ? B SF4 1101 ? 1_555 104.0 ? 
91  SG  ? B CYS 800 ? B CYS 800  ? 1_555 FE3 ? N SF4 . ? B SF4 1101 ? 1_555 S4  ? N SF4 .   ? B SF4 1101 ? 1_555 106.2 ? 
92  S1  ? N SF4 .   ? B SF4 1101 ? 1_555 FE3 ? N SF4 . ? B SF4 1101 ? 1_555 S4  ? N SF4 .   ? B SF4 1101 ? 1_555 104.2 ? 
93  S2  ? N SF4 .   ? B SF4 1101 ? 1_555 FE3 ? N SF4 . ? B SF4 1101 ? 1_555 S4  ? N SF4 .   ? B SF4 1101 ? 1_555 104.2 ? 
94  SG  ? B CYS 804 ? B CYS 804  ? 1_555 FE3 ? O SF4 . ? B SF4 1102 ? 1_555 S1  ? O SF4 .   ? B SF4 1102 ? 1_555 118.6 ? 
95  SG  ? B CYS 804 ? B CYS 804  ? 1_555 FE3 ? O SF4 . ? B SF4 1102 ? 1_555 S2  ? O SF4 .   ? B SF4 1102 ? 1_555 113.6 ? 
96  S1  ? O SF4 .   ? B SF4 1102 ? 1_555 FE3 ? O SF4 . ? B SF4 1102 ? 1_555 S2  ? O SF4 .   ? B SF4 1102 ? 1_555 104.0 ? 
97  SG  ? B CYS 804 ? B CYS 804  ? 1_555 FE3 ? O SF4 . ? B SF4 1102 ? 1_555 S4  ? O SF4 .   ? B SF4 1102 ? 1_555 110.9 ? 
98  S1  ? O SF4 .   ? B SF4 1102 ? 1_555 FE3 ? O SF4 . ? B SF4 1102 ? 1_555 S4  ? O SF4 .   ? B SF4 1102 ? 1_555 104.3 ? 
99  S2  ? O SF4 .   ? B SF4 1102 ? 1_555 FE3 ? O SF4 . ? B SF4 1102 ? 1_555 S4  ? O SF4 .   ? B SF4 1102 ? 1_555 104.1 ? 
100 SG  ? B CYS 850 ? B CYS 850  ? 1_555 FE1 ? P SF4 . ? B SF4 1103 ? 1_555 S2  ? P SF4 .   ? B SF4 1103 ? 1_555 119.4 ? 
101 SG  ? B CYS 850 ? B CYS 850  ? 1_555 FE1 ? P SF4 . ? B SF4 1103 ? 1_555 S3  ? P SF4 .   ? B SF4 1103 ? 1_555 108.2 ? 
102 S2  ? P SF4 .   ? B SF4 1103 ? 1_555 FE1 ? P SF4 . ? B SF4 1103 ? 1_555 S3  ? P SF4 .   ? B SF4 1103 ? 1_555 104.2 ? 
103 SG  ? B CYS 850 ? B CYS 850  ? 1_555 FE1 ? P SF4 . ? B SF4 1103 ? 1_555 S4  ? P SF4 .   ? B SF4 1103 ? 1_555 115.1 ? 
104 S2  ? P SF4 .   ? B SF4 1103 ? 1_555 FE1 ? P SF4 . ? B SF4 1103 ? 1_555 S4  ? P SF4 .   ? B SF4 1103 ? 1_555 104.1 ? 
105 S3  ? P SF4 .   ? B SF4 1103 ? 1_555 FE1 ? P SF4 . ? B SF4 1103 ? 1_555 S4  ? P SF4 .   ? B SF4 1103 ? 1_555 104.3 ? 
106 SG  ? B CYS 853 ? B CYS 853  ? 1_555 FE4 ? P SF4 . ? B SF4 1103 ? 1_555 S1  ? P SF4 .   ? B SF4 1103 ? 1_555 121.4 ? 
107 SG  ? B CYS 853 ? B CYS 853  ? 1_555 FE4 ? P SF4 . ? B SF4 1103 ? 1_555 S2  ? P SF4 .   ? B SF4 1103 ? 1_555 115.1 ? 
108 S1  ? P SF4 .   ? B SF4 1103 ? 1_555 FE4 ? P SF4 . ? B SF4 1103 ? 1_555 S2  ? P SF4 .   ? B SF4 1103 ? 1_555 104.0 ? 
109 SG  ? B CYS 853 ? B CYS 853  ? 1_555 FE4 ? P SF4 . ? B SF4 1103 ? 1_555 S3  ? P SF4 .   ? B SF4 1103 ? 1_555 106.3 ? 
110 S1  ? P SF4 .   ? B SF4 1103 ? 1_555 FE4 ? P SF4 . ? B SF4 1103 ? 1_555 S3  ? P SF4 .   ? B SF4 1103 ? 1_555 104.2 ? 
111 S2  ? P SF4 .   ? B SF4 1103 ? 1_555 FE4 ? P SF4 . ? B SF4 1103 ? 1_555 S3  ? P SF4 .   ? B SF4 1103 ? 1_555 104.1 ? 
112 SG  ? B CYS 858 ? B CYS 858  ? 1_555 FE2 ? P SF4 . ? B SF4 1103 ? 1_555 S1  ? P SF4 .   ? B SF4 1103 ? 1_555 113.0 ? 
113 SG  ? B CYS 858 ? B CYS 858  ? 1_555 FE2 ? P SF4 . ? B SF4 1103 ? 1_555 S3  ? P SF4 .   ? B SF4 1103 ? 1_555 120.6 ? 
114 S1  ? P SF4 .   ? B SF4 1103 ? 1_555 FE2 ? P SF4 . ? B SF4 1103 ? 1_555 S3  ? P SF4 .   ? B SF4 1103 ? 1_555 104.0 ? 
115 SG  ? B CYS 858 ? B CYS 858  ? 1_555 FE2 ? P SF4 . ? B SF4 1103 ? 1_555 S4  ? P SF4 .   ? B SF4 1103 ? 1_555 109.2 ? 
116 S1  ? P SF4 .   ? B SF4 1103 ? 1_555 FE2 ? P SF4 . ? B SF4 1103 ? 1_555 S4  ? P SF4 .   ? B SF4 1103 ? 1_555 104.3 ? 
117 S3  ? P SF4 .   ? B SF4 1103 ? 1_555 FE2 ? P SF4 . ? B SF4 1103 ? 1_555 S4  ? P SF4 .   ? B SF4 1103 ? 1_555 104.2 ? 
118 SG  ? B CYS 862 ? B CYS 862  ? 1_555 FE1 ? Q F3S . ? B F3S 1104 ? 1_555 S1  ? Q F3S .   ? B F3S 1104 ? 1_555 114.7 ? 
119 SG  ? B CYS 862 ? B CYS 862  ? 1_555 FE1 ? Q F3S . ? B F3S 1104 ? 1_555 S2  ? Q F3S .   ? B F3S 1104 ? 1_555 101.3 ? 
120 S1  ? Q F3S .   ? B F3S 1104 ? 1_555 FE1 ? Q F3S . ? B F3S 1104 ? 1_555 S2  ? Q F3S .   ? B F3S 1104 ? 1_555 103.6 ? 
121 SG  ? B CYS 862 ? B CYS 862  ? 1_555 FE1 ? Q F3S . ? B F3S 1104 ? 1_555 S3  ? Q F3S .   ? B F3S 1104 ? 1_555 111.1 ? 
122 S1  ? Q F3S .   ? B F3S 1104 ? 1_555 FE1 ? Q F3S . ? B F3S 1104 ? 1_555 S3  ? Q F3S .   ? B F3S 1104 ? 1_555 114.7 ? 
123 S2  ? Q F3S .   ? B F3S 1104 ? 1_555 FE1 ? Q F3S . ? B F3S 1104 ? 1_555 S3  ? Q F3S .   ? B F3S 1104 ? 1_555 110.1 ? 
124 SG  ? B CYS 892 ? B CYS 892  ? 1_555 FE3 ? P SF4 . ? B SF4 1103 ? 1_555 S1  ? P SF4 .   ? B SF4 1103 ? 1_555 107.1 ? 
125 SG  ? B CYS 892 ? B CYS 892  ? 1_555 FE3 ? P SF4 . ? B SF4 1103 ? 1_555 S2  ? P SF4 .   ? B SF4 1103 ? 1_555 124.4 ? 
126 S1  ? P SF4 .   ? B SF4 1103 ? 1_555 FE3 ? P SF4 . ? B SF4 1103 ? 1_555 S2  ? P SF4 .   ? B SF4 1103 ? 1_555 103.9 ? 
127 SG  ? B CYS 892 ? B CYS 892  ? 1_555 FE3 ? P SF4 . ? B SF4 1103 ? 1_555 S4  ? P SF4 .   ? B SF4 1103 ? 1_555 111.1 ? 
128 S1  ? P SF4 .   ? B SF4 1103 ? 1_555 FE3 ? P SF4 . ? B SF4 1103 ? 1_555 S4  ? P SF4 .   ? B SF4 1103 ? 1_555 104.3 ? 
129 S2  ? P SF4 .   ? B SF4 1103 ? 1_555 FE3 ? P SF4 . ? B SF4 1103 ? 1_555 S4  ? P SF4 .   ? B SF4 1103 ? 1_555 104.1 ? 
130 SG  ? B CYS 931 ? B CYS 931  ? 1_555 FE2 ? O SF4 . ? B SF4 1102 ? 1_555 S1  ? O SF4 .   ? B SF4 1102 ? 1_555 109.8 ? 
131 SG  ? B CYS 931 ? B CYS 931  ? 1_555 FE2 ? O SF4 . ? B SF4 1102 ? 1_555 S3  ? O SF4 .   ? B SF4 1102 ? 1_555 118.6 ? 
132 S1  ? O SF4 .   ? B SF4 1102 ? 1_555 FE2 ? O SF4 . ? B SF4 1102 ? 1_555 S3  ? O SF4 .   ? B SF4 1102 ? 1_555 104.2 ? 
133 SG  ? B CYS 931 ? B CYS 931  ? 1_555 FE2 ? O SF4 . ? B SF4 1102 ? 1_555 S4  ? O SF4 .   ? B SF4 1102 ? 1_555 114.4 ? 
134 S1  ? O SF4 .   ? B SF4 1102 ? 1_555 FE2 ? O SF4 . ? B SF4 1102 ? 1_555 S4  ? O SF4 .   ? B SF4 1102 ? 1_555 104.3 ? 
135 S3  ? O SF4 .   ? B SF4 1102 ? 1_555 FE2 ? O SF4 . ? B SF4 1102 ? 1_555 S4  ? O SF4 .   ? B SF4 1102 ? 1_555 104.1 ? 
136 SG  ? B CYS 934 ? B CYS 934  ? 1_555 FE1 ? O SF4 . ? B SF4 1102 ? 1_555 S2  ? O SF4 .   ? B SF4 1102 ? 1_555 97.1  ? 
137 SG  ? B CYS 934 ? B CYS 934  ? 1_555 FE1 ? O SF4 . ? B SF4 1102 ? 1_555 S3  ? O SF4 .   ? B SF4 1102 ? 1_555 122.9 ? 
138 S2  ? O SF4 .   ? B SF4 1102 ? 1_555 FE1 ? O SF4 . ? B SF4 1102 ? 1_555 S3  ? O SF4 .   ? B SF4 1102 ? 1_555 104.2 ? 
139 SG  ? B CYS 934 ? B CYS 934  ? 1_555 FE1 ? O SF4 . ? B SF4 1102 ? 1_555 S4  ? O SF4 .   ? B SF4 1102 ? 1_555 121.1 ? 
140 S2  ? O SF4 .   ? B SF4 1102 ? 1_555 FE1 ? O SF4 . ? B SF4 1102 ? 1_555 S4  ? O SF4 .   ? B SF4 1102 ? 1_555 104.1 ? 
141 S3  ? O SF4 .   ? B SF4 1102 ? 1_555 FE1 ? O SF4 . ? B SF4 1102 ? 1_555 S4  ? O SF4 .   ? B SF4 1102 ? 1_555 104.0 ? 
142 SG  ? B CYS 968 ? B CYS 968  ? 1_555 FE4 ? O SF4 . ? B SF4 1102 ? 1_555 S1  ? O SF4 .   ? B SF4 1102 ? 1_555 126.8 ? 
143 SG  ? B CYS 968 ? B CYS 968  ? 1_555 FE4 ? O SF4 . ? B SF4 1102 ? 1_555 S2  ? O SF4 .   ? B SF4 1102 ? 1_555 111.6 ? 
144 S1  ? O SF4 .   ? B SF4 1102 ? 1_555 FE4 ? O SF4 . ? B SF4 1102 ? 1_555 S2  ? O SF4 .   ? B SF4 1102 ? 1_555 104.0 ? 
145 SG  ? B CYS 968 ? B CYS 968  ? 1_555 FE4 ? O SF4 . ? B SF4 1102 ? 1_555 S3  ? O SF4 .   ? B SF4 1102 ? 1_555 103.7 ? 
146 S1  ? O SF4 .   ? B SF4 1102 ? 1_555 FE4 ? O SF4 . ? B SF4 1102 ? 1_555 S3  ? O SF4 .   ? B SF4 1102 ? 1_555 104.2 ? 
147 S2  ? O SF4 .   ? B SF4 1102 ? 1_555 FE4 ? O SF4 . ? B SF4 1102 ? 1_555 S3  ? O SF4 .   ? B SF4 1102 ? 1_555 104.2 ? 
148 SG  ? B CYS 972 ? B CYS 972  ? 1_555 FE2 ? N SF4 . ? B SF4 1101 ? 1_555 S1  ? N SF4 .   ? B SF4 1101 ? 1_555 128.3 ? 
149 SG  ? B CYS 972 ? B CYS 972  ? 1_555 FE2 ? N SF4 . ? B SF4 1101 ? 1_555 S3  ? N SF4 .   ? B SF4 1101 ? 1_555 107.9 ? 
150 S1  ? N SF4 .   ? B SF4 1101 ? 1_555 FE2 ? N SF4 . ? B SF4 1101 ? 1_555 S3  ? N SF4 .   ? B SF4 1101 ? 1_555 104.0 ? 
151 SG  ? B CYS 972 ? B CYS 972  ? 1_555 FE2 ? N SF4 . ? B SF4 1101 ? 1_555 S4  ? N SF4 .   ? B SF4 1101 ? 1_555 105.9 ? 
152 S1  ? N SF4 .   ? B SF4 1101 ? 1_555 FE2 ? N SF4 . ? B SF4 1101 ? 1_555 S4  ? N SF4 .   ? B SF4 1101 ? 1_555 104.1 ? 
153 S3  ? N SF4 .   ? B SF4 1101 ? 1_555 FE2 ? N SF4 . ? B SF4 1101 ? 1_555 S4  ? N SF4 .   ? B SF4 1101 ? 1_555 104.4 ? 
154 ND1 ? E HIS 107 ? E HIS 107  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 NA  ? R HEC .   ? E HEC 301  ? 1_555 122.0 ? 
155 ND1 ? E HIS 107 ? E HIS 107  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 NB  ? R HEC .   ? E HEC 301  ? 1_555 102.0 ? 
156 NA  ? R HEC .   ? E HEC 301  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 NB  ? R HEC .   ? E HEC 301  ? 1_555 90.4  ? 
157 ND1 ? E HIS 107 ? E HIS 107  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 NC  ? R HEC .   ? E HEC 301  ? 1_555 68.6  ? 
158 NA  ? R HEC .   ? E HEC 301  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 NC  ? R HEC .   ? E HEC 301  ? 1_555 169.3 ? 
159 NB  ? R HEC .   ? E HEC 301  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 NC  ? R HEC .   ? E HEC 301  ? 1_555 88.5  ? 
160 ND1 ? E HIS 107 ? E HIS 107  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 ND  ? R HEC .   ? E HEC 301  ? 1_555 84.1  ? 
161 NA  ? R HEC .   ? E HEC 301  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 ND  ? R HEC .   ? E HEC 301  ? 1_555 91.1  ? 
162 NB  ? R HEC .   ? E HEC 301  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 ND  ? R HEC .   ? E HEC 301  ? 1_555 171.7 ? 
163 NC  ? R HEC .   ? E HEC 301  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 ND  ? R HEC .   ? E HEC 301  ? 1_555 88.5  ? 
164 ND1 ? E HIS 107 ? E HIS 107  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 NE2 ? E HIS 107 ? E HIS 107  ? 1_555 54.9  ? 
165 NA  ? R HEC .   ? E HEC 301  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 NE2 ? E HIS 107 ? E HIS 107  ? 1_555 72.6  ? 
166 NB  ? R HEC .   ? E HEC 301  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 NE2 ? E HIS 107 ? E HIS 107  ? 1_555 80.1  ? 
167 NC  ? R HEC .   ? E HEC 301  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 NE2 ? E HIS 107 ? E HIS 107  ? 1_555 117.7 ? 
168 ND  ? R HEC .   ? E HEC 301  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 NE2 ? E HIS 107 ? E HIS 107  ? 1_555 108.1 ? 
169 ND1 ? E HIS 107 ? E HIS 107  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 SD  ? E MET 162 ? E MET 162  ? 1_555 142.7 ? 
170 NA  ? R HEC .   ? E HEC 301  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 SD  ? E MET 162 ? E MET 162  ? 1_555 91.8  ? 
171 NB  ? R HEC .   ? E HEC 301  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 SD  ? E MET 162 ? E MET 162  ? 1_555 92.2  ? 
172 NC  ? R HEC .   ? E HEC 301  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 SD  ? E MET 162 ? E MET 162  ? 1_555 77.6  ? 
173 ND  ? R HEC .   ? E HEC 301  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 SD  ? E MET 162 ? E MET 162  ? 1_555 79.7  ? 
174 NE2 ? E HIS 107 ? E HIS 107  ? 1_555 FE  ? R HEC . ? E HEC 301  ? 1_555 SD  ? E MET 162 ? E MET 162  ? 1_555 162.4 ? 
# 
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 HEC I . ? CYS A 214 ? HEC A 301 ? 1_555 CYS A 214 ? 1_555 CAB SG CYS 2 HEC None Heme/heme-like 
2 HEC J . ? CYS A 164 ? HEC A 302 ? 1_555 CYS A 164 ? 1_555 CAB SG CYS 2 HEC None Heme/heme-like 
3 HEC J . ? CYS A 167 ? HEC A 302 ? 1_555 CYS A 167 ? 1_555 CAC SG CYS 3 HEC None Heme/heme-like 
4 HEC L . ? CYS A 66  ? HEC A 304 ? 1_555 CYS A 66  ? 1_555 CAB SG CYS 2 HEC None Heme/heme-like 
5 HEC M . ? CYS A 87  ? HEC A 305 ? 1_555 CYS A 87  ? 1_555 CAB SG CYS 2 HEC None Heme/heme-like 
6 HEC R . ? CYS E 103 ? HEC E 301 ? 1_555 CYS E 103 ? 1_555 CAB SG CYS 2 HEC None Heme/heme-like 
7 HEC R . ? CYS E 106 ? HEC E 301 ? 1_555 CYS E 106 ? 1_555 CAC SG CYS 3 HEC None Heme/heme-like 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 2 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 5 ? 
AA9 ? 2 ? 
AB1 ? 4 ? 
AB2 ? 2 ? 
AB3 ? 2 ? 
AB4 ? 2 ? 
AB5 ? 4 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA7 1 2 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? parallel      
AA8 4 5 ? anti-parallel 
AA9 1 2 ? parallel      
AB1 1 2 ? anti-parallel 
AB1 2 3 ? parallel      
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? 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 TRP A 116  ? VAL A 117  ? TRP A 116  VAL A 117  
AA1 2 TYR B 83   ? ILE B 84   ? TYR B 83   ILE B 84   
AA2 1 GLN B 100  ? THR B 107  ? GLN B 100  THR B 107  
AA2 2 GLY B 112  ? SER B 119  ? GLY B 112  SER B 119  
AA2 3 PRO B 124  ? GLY B 129  ? PRO B 124  GLY B 129  
AA3 1 VAL B 160  ? LEU B 161  ? VAL B 160  LEU B 161  
AA3 2 PRO B 166  ? SER B 167  ? PRO B 166  SER B 167  
AA4 1 VAL B 191  ? LEU B 194  ? VAL B 191  LEU B 194  
AA4 2 THR B 419  ? ILE B 423  ? THR B 419  ILE B 423  
AA4 3 LEU B 446  ? LEU B 450  ? LEU B 446  LEU B 450  
AA4 4 HIS B 464  ? ILE B 465  ? HIS B 464  ILE B 465  
AA5 1 THR B 243  ? TYR B 246  ? THR B 243  TYR B 246  
AA5 2 VAL B 388  ? HIS B 391  ? VAL B 388  HIS B 391  
AA6 1 HIS B 307  ? PRO B 310  ? HIS B 307  PRO B 310  
AA6 2 ARG B 290  ? GLU B 295  ? ARG B 290  GLU B 295  
AA6 3 VAL B 253  ? LEU B 257  ? VAL B 253  LEU B 257  
AA6 4 SER B 358  ? ALA B 362  ? SER B 358  ALA B 362  
AA7 1 GLY B 475  ? ALA B 477  ? GLY B 475  ALA B 477  
AA7 2 SER B 485  ? VAL B 487  ? SER B 485  VAL B 487  
AA8 1 GLU B 571  ? PRO B 576  ? GLU B 571  PRO B 576  
AA8 2 SER B 675  ? LEU B 680  ? SER B 675  LEU B 680  
AA8 3 ALA B 607  ? MET B 609  ? ALA B 607  MET B 609  
AA8 4 ILE B 663  ? LEU B 667  ? ILE B 663  LEU B 667  
AA8 5 ILE B 651  ? ALA B 652  ? ILE B 651  ALA B 652  
AA9 1 VAL B 741  ? GLU B 743  ? VAL B 741  GLU B 743  
AA9 2 ARG B 1016 ? ARG B 1018 ? ARG B 1016 ARG B 1018 
AB1 1 ILE B 977  ? ASP B 981  ? ILE B 977  ASP B 981  
AB1 2 TRP B 785  ? ASN B 790  ? TRP B 785  ASN B 790  
AB1 3 THR B 1011 ? LEU B 1014 ? THR B 1011 LEU B 1014 
AB1 4 ASN B 998  ? TYR B 999  ? ASN B 998  TYR B 999  
AB2 1 ARG B 828  ? ASP B 830  ? ARG B 828  ASP B 830  
AB2 2 MET B 846  ? VAL B 848  ? MET B 846  VAL B 848  
AB3 1 THR B 867  ? HIS B 869  ? THR B 867  HIS B 869  
AB3 2 ASN B 875  ? MET B 877  ? ASN B 875  MET B 877  
AB4 1 ARG B 898  ? PHE B 899  ? ARG B 898  PHE B 899  
AB4 2 MET B 928  ? GLU B 929  ? MET B 928  GLU B 929  
AB5 1 MET D 33   ? PHE D 36   ? MET D 33   PHE D 36   
AB5 2 PHE D 147  ? GLU D 151  ? PHE D 147  GLU D 151  
AB5 3 GLY D 7    ? MET D 9    ? GLY D 7    MET D 9    
AB5 4 SER D 175  ? VAL D 177  ? SER D 175  VAL D 177  
# 
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 N TRP A 116  ? N TRP A 116  O ILE B 84   ? O ILE B 84   
AA2 1 2 N GLN B 100  ? N GLN B 100  O SER B 119  ? O SER B 119  
AA2 2 3 N LEU B 116  ? N LEU B 116  O GLU B 128  ? O GLU B 128  
AA3 1 2 N VAL B 160  ? N VAL B 160  O SER B 167  ? O SER B 167  
AA4 1 2 N ARG B 192  ? N ARG B 192  O ILE B 421  ? O ILE B 421  
AA4 2 3 N MET B 422  ? N MET B 422  O ILE B 448  ? O ILE B 448  
AA4 3 4 N HIS B 449  ? N HIS B 449  O ILE B 465  ? O ILE B 465  
AA5 1 2 N ARG B 245  ? N ARG B 245  O PHE B 389  ? O PHE B 389  
AA6 1 2 O LEU B 309  ? O LEU B 309  N VAL B 293  ? N VAL B 293  
AA6 2 3 O TYR B 292  ? O TYR B 292  N SER B 256  ? N SER B 256  
AA6 3 4 N VAL B 255  ? N VAL B 255  O ILE B 361  ? O ILE B 361  
AA7 1 2 N GLY B 475  ? N GLY B 475  O VAL B 487  ? O VAL B 487  
AA8 1 2 N VAL B 573  ? N VAL B 573  O ILE B 676  ? O ILE B 676  
AA8 2 3 O THR B 677  ? O THR B 677  N LEU B 608  ? N LEU B 608  
AA8 3 4 N ALA B 607  ? N ALA B 607  O PRO B 664  ? O PRO B 664  
AA8 4 5 O ILE B 663  ? O ILE B 663  N ALA B 652  ? N ALA B 652  
AA9 1 2 N GLY B 742  ? N GLY B 742  O ARG B 1018 ? O ARG B 1018 
AB1 1 2 O GLY B 980  ? O GLY B 980  N GLY B 786  ? N GLY B 786  
AB1 2 3 N ILE B 789  ? N ILE B 789  O LEU B 1014 ? O LEU B 1014 
AB1 3 4 O TYR B 1013 ? O TYR B 1013 N TYR B 999  ? N TYR B 999  
AB2 1 2 N ARG B 828  ? N ARG B 828  O VAL B 848  ? O VAL B 848  
AB3 1 2 N VAL B 868  ? N VAL B 868  O ASN B 876  ? O ASN B 876  
AB4 1 2 N ARG B 898  ? N ARG B 898  O GLU B 929  ? O GLU B 929  
AB5 1 2 N PHE D 36   ? N PHE D 36   O PHE D 147  ? O PHE D 147  
AB5 2 3 O ILE D 150  ? O ILE D 150  N VAL D 8    ? N VAL D 8    
AB5 3 4 N MET D 9    ? N MET D 9    O SER D 175  ? O SER D 175  
# 
_pdbx_entry_details.entry_id                   9ILT 
_pdbx_entry_details.has_ligand_of_interest     N 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 SG  A CYS 217 ? ? CBC A HEC 301  ? ? 1.76 
2 1 SG  A CYS 143 ? ? CBC A HEC 303  ? ? 1.76 
3 1 SG  A CYS 90  ? ? CBC A HEC 305  ? ? 1.76 
4 1 SG  A CYS 69  ? ? CBC A HEC 304  ? ? 1.77 
5 1 SG  A CYS 140 ? ? CBB A HEC 303  ? ? 1.77 
6 1 CE1 E HIS 107 ? ? FE  E HEC 301  ? ? 1.80 
7 1 SG  B CYS 888 ? ? FE3 B F3S 1104 ? ? 1.87 
8 1 SG  B CYS 882 ? ? FE4 B F3S 1104 ? ? 1.89 
9 1 OG1 B THR 499 ? ? OD1 B ASN 501  ? ? 2.16 
# 
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 TYR A 108  ? ? 65.89   -37.54  
2  1 PRO A 123  ? ? -76.42  31.74   
3  1 ASN A 124  ? ? 60.24   -7.58   
4  1 TYR A 127  ? ? 56.47   78.64   
5  1 TYR A 182  ? ? -104.61 -156.44 
6  1 ASN A 191  ? ? -98.68  58.68   
7  1 CYS A 217  ? ? -112.99 -70.80  
8  1 TYR B 78   ? ? 65.49   -46.25  
9  1 PRO B 80   ? ? -71.28  -161.52 
10 1 GLN B 82   ? ? 55.53   85.27   
11 1 SER B 104  ? ? -128.54 -164.82 
12 1 LEU B 108  ? ? -98.89  -72.50  
13 1 THR B 125  ? ? -132.15 -38.68  
14 1 SER B 136  ? ? -160.01 49.67   
15 1 LEU B 137  ? ? -67.59  69.25   
16 1 GLN B 163  ? ? -146.73 54.00   
17 1 THR B 186  ? ? -81.90  -159.03 
18 1 LEU B 194  ? ? -163.61 90.49   
19 1 THR B 196  ? ? -97.66  -158.68 
20 1 TYR B 220  ? ? 56.18   88.57   
21 1 PRO B 264  ? ? -54.64  107.89  
22 1 GLU B 352  ? ? 69.37   -22.97  
23 1 ALA B 396  ? ? 55.29   -97.39  
24 1 ASN B 426  ? ? 53.28   71.51   
25 1 GLN B 452  ? ? 66.71   -9.47   
26 1 ASP B 481  ? ? 69.18   -2.37   
27 1 ALA B 484  ? ? 59.11   70.76   
28 1 GLU B 512  ? ? 36.44   42.88   
29 1 GLU B 525  ? ? 53.21   9.67    
30 1 ASN B 538  ? ? -78.39  -162.95 
31 1 ILE B 563  ? ? 57.03   88.65   
32 1 PHE B 581  ? ? 57.20   -124.74 
33 1 LEU B 598  ? ? 67.72   -14.91  
34 1 TRP B 603  ? ? 59.46   12.48   
35 1 ALA B 624  ? ? 65.76   -12.52  
36 1 THR B 630  ? ? -104.54 -168.78 
37 1 TYR B 656  ? ? -103.27 -75.04  
38 1 ALA B 711  ? ? -107.34 -80.75  
39 1 THR B 716  ? ? 53.04   80.82   
40 1 GLN B 728  ? ? -121.26 -51.35  
41 1 ASP B 729  ? ? 68.02   -5.31   
42 1 ASP B 737  ? ? -91.17  57.78   
43 1 VAL B 758  ? ? 67.02   -59.97  
44 1 THR B 780  ? ? -102.86 -65.67  
45 1 PHE B 833  ? ? 30.18   75.52   
46 1 ASP B 837  ? ? 70.25   -47.63  
47 1 LEU B 838  ? ? 55.26   6.02    
48 1 ASN B 849  ? ? -134.52 -159.00 
49 1 LYS B 855  ? ? -107.75 69.08   
50 1 LYS B 886  ? ? 58.34   17.24   
51 1 LEU B 902  ? ? -128.15 -169.32 
52 1 TYR B 957  ? ? 57.02   82.06   
53 1 VAL B 1008 ? ? 52.69   70.21   
54 1 ASN C 79   ? ? -131.30 -156.35 
55 1 ALA C 106  ? ? -129.35 -54.20  
56 1 PRO C 153  ? ? -68.94  94.45   
57 1 PHE C 164  ? ? 65.18   -9.89   
58 1 LYS C 202  ? ? 60.19   -67.60  
59 1 ARG C 208  ? ? 66.39   -13.97  
60 1 ARG C 222  ? ? 65.16   -7.43   
61 1 ALA C 361  ? ? -130.35 -40.71  
62 1 ASP C 405  ? ? -106.27 -150.79 
63 1 SER C 410  ? ? -90.81  37.14   
64 1 ALA D 25   ? ? -68.61  -177.49 
65 1 LYS D 26   ? ? 64.85   -52.76  
66 1 GLU D 42   ? ? 67.88   -3.13   
67 1 VAL D 80   ? ? -135.95 -67.19  
68 1 ASP D 92   ? ? -101.06 -162.71 
69 1 PRO D 126  ? ? -62.50  72.04   
70 1 ASP D 144  ? ? 58.87   -139.81 
71 1 ARG D 159  ? ? 59.49   -98.41  
72 1 HIS E 27   ? ? -144.95 -78.06  
73 1 ASP E 29   ? ? -93.14  -74.70  
74 1 THR E 37   ? ? -74.93  -162.58 
75 1 PRO E 60   ? ? -67.61  -175.80 
76 1 ASP E 76   ? ? -152.67 24.15   
77 1 HIS E 107  ? ? -157.73 -6.85   
78 1 VAL E 124  ? ? 34.16   76.08   
79 1 TYR E 150  ? ? -171.90 136.78  
80 1 TYR E 163  ? ? 68.88   -11.46  
81 1 TYR E 165  ? ? -143.15 50.35   
82 1 LYS F 109  ? ? 75.72   -21.94  
83 1 LEU F 183  ? ? 59.07   7.51    
84 1 ALA F 184  ? ? -130.46 -33.82  
85 1 ALA F 249  ? ? 64.61   -5.72   
86 1 SER F 256  ? ? -111.59 -162.84 
87 1 PHE F 317  ? ? -121.40 -70.41  
88 1 THR F 329  ? ? 72.19   -12.55  
89 1 PHE F 359  ? ? -93.03  -61.46  
90 1 GLU F 361  ? ? 64.24   -3.05   
91 1 LEU F 395  ? ? 59.79   93.94   
92 1 PRO G 57   ? ? -64.95  88.06   
93 1 TYR G 84   ? ? 54.64   -138.56 
94 1 LYS G 91   ? ? -105.94 -61.62  
95 1 ALA I 34   ? ? -127.96 -84.48  
96 1 PHE I 35   ? ? -90.74  53.89   
97 1 TYR I 36   ? ? -124.68 -70.93  
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -37.1225 
_pdbx_refine_tls.origin_y         -35.2494 
_pdbx_refine_tls.origin_z         41.8978 
_pdbx_refine_tls.T[1][1]          0.2531 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.1076 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0070 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.3972 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0459 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.3868 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.2004 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.1930 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.1273 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.4421 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.1227 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.6057 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0195 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0156 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0298 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0563 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0494 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0157 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0762 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.1986 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0007 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   all 
# 
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 A MET 1    ? A MET 1    
2   1 Y 1 B MET 1    ? B MET 1    
3   1 Y 1 B THR 2    ? B THR 2    
4   1 Y 1 B GLN 3    ? B GLN 3    
5   1 Y 1 B GLN 4    ? B GLN 4    
6   1 Y 1 B GLN 5    ? B GLN 5    
7   1 Y 1 B PRO 6    ? B PRO 6    
8   1 Y 1 B ASP 7    ? B ASP 7    
9   1 Y 1 B LEU 8    ? B LEU 8    
10  1 Y 1 B GLU 9    ? B GLU 9    
11  1 Y 1 B ALA 10   ? B ALA 10   
12  1 Y 1 B ILE 11   ? B ILE 11   
13  1 Y 1 B ARG 12   ? B ARG 12   
14  1 Y 1 B ALA 13   ? B ALA 13   
15  1 Y 1 B GLN 14   ? B GLN 14   
16  1 Y 1 B LEU 15   ? B LEU 15   
17  1 Y 1 B ARG 16   ? B ARG 16   
18  1 Y 1 B ASP 17   ? B ASP 17   
19  1 Y 1 B ALA 18   ? B ALA 18   
20  1 Y 1 B ARG 19   ? B ARG 19   
21  1 Y 1 B GLY 20   ? B GLY 20   
22  1 Y 1 B PRO 21   ? B PRO 21   
23  1 Y 1 B GLN 22   ? B GLN 22   
24  1 Y 1 B PHE 23   ? B PHE 23   
25  1 Y 1 B TRP 24   ? B TRP 24   
26  1 Y 1 B ARG 25   ? B ARG 25   
27  1 Y 1 B SER 26   ? B SER 26   
28  1 Y 1 B LEU 27   ? B LEU 27   
29  1 Y 1 B ASP 28   ? B ASP 28   
30  1 Y 1 B GLN 29   ? B GLN 29   
31  1 Y 1 B LEU 30   ? B LEU 30   
32  1 Y 1 B ALA 31   ? B ALA 31   
33  1 Y 1 B ASP 32   ? B ASP 32   
34  1 Y 1 B ALA 33   ? B ALA 33   
35  1 Y 1 B PRO 34   ? B PRO 34   
36  1 Y 1 B ALA 35   ? B ALA 35   
37  1 Y 1 B PHE 36   ? B PHE 36   
38  1 Y 1 B ARG 37   ? B ARG 37   
39  1 Y 1 B GLU 38   ? B GLU 38   
40  1 Y 1 B LEU 39   ? B LEU 39   
41  1 Y 1 B ILE 40   ? B ILE 40   
42  1 Y 1 B GLU 41   ? B GLU 41   
43  1 Y 1 B ARG 42   ? B ARG 42   
44  1 Y 1 B GLU 43   ? B GLU 43   
45  1 Y 1 B PHE 44   ? B PHE 44   
46  1 Y 1 B PRO 45   ? B PRO 45   
47  1 Y 1 B ARG 46   ? B ARG 46   
48  1 Y 1 B GLY 47   ? B GLY 47   
49  1 Y 1 B ALA 48   ? B ALA 48   
50  1 Y 1 B SER 49   ? B SER 49   
51  1 Y 1 B GLU 50   ? B GLU 50   
52  1 Y 1 B LEU 51   ? B LEU 51   
53  1 Y 1 B GLU 52   ? B GLU 52   
54  1 Y 1 B ASP 53   ? B ASP 53   
55  1 Y 1 B GLY 54   ? B GLY 54   
56  1 Y 1 B ILE 55   ? B ILE 55   
57  1 Y 1 B SER 56   ? B SER 56   
58  1 Y 1 B ARG 57   ? B ARG 57   
59  1 Y 1 B ARG 58   ? B ARG 58   
60  1 Y 1 B THR 59   ? B THR 59   
61  1 Y 1 B PHE 60   ? B PHE 60   
62  1 Y 1 B LEU 61   ? B LEU 61   
63  1 Y 1 B LYS 62   ? B LYS 62   
64  1 Y 1 B LEU 63   ? B LEU 63   
65  1 Y 1 B MET 64   ? B MET 64   
66  1 Y 1 B GLY 65   ? B GLY 65   
67  1 Y 1 B ALA 66   ? B ALA 66   
68  1 Y 1 B SER 67   ? B SER 67   
69  1 Y 1 B LEU 68   ? B LEU 68   
70  1 Y 1 B ALA 69   ? B ALA 69   
71  1 Y 1 B LEU 70   ? B LEU 70   
72  1 Y 1 B ALA 71   ? B ALA 71   
73  1 Y 1 B GLY 72   ? B GLY 72   
74  1 Y 1 B VAL 73   ? B VAL 73   
75  1 Y 1 B THR 74   ? B THR 74   
76  1 Y 1 B VAL 1027 ? B VAL 1027 
77  1 Y 1 B GLU 1028 ? B GLU 1028 
78  1 Y 1 B GLY 1029 ? B GLY 1029 
79  1 Y 1 C MET 1    ? C MET 1    
80  1 Y 1 C ALA 2    ? C ALA 2    
81  1 Y 1 C GLN 3    ? C GLN 3    
82  1 Y 1 C ALA 4    ? C ALA 4    
83  1 Y 1 C GLN 5    ? C GLN 5    
84  1 Y 1 C PRO 6    ? C PRO 6    
85  1 Y 1 C LEU 7    ? C LEU 7    
86  1 Y 1 C ARG 8    ? C ARG 8    
87  1 Y 1 C THR 9    ? C THR 9    
88  1 Y 1 C ARG 10   ? C ARG 10   
89  1 Y 1 C PRO 11   ? C PRO 11   
90  1 Y 1 C GLN 12   ? C GLN 12   
91  1 Y 1 C ASP 13   ? C ASP 13   
92  1 Y 1 C ASP 14   ? C ASP 14   
93  1 Y 1 C GLY 15   ? C GLY 15   
94  1 Y 1 C ALA 465  ? C ALA 465  
95  1 Y 1 C GLY 466  ? C GLY 466  
96  1 Y 1 C HIS 467  ? C HIS 467  
97  1 Y 1 C GLY 468  ? C GLY 468  
98  1 Y 1 C ALA 469  ? C ALA 469  
99  1 Y 1 C HIS 470  ? C HIS 470  
100 1 Y 1 C GLY 471  ? C GLY 471  
101 1 Y 1 C HIS 472  ? C HIS 472  
102 1 Y 1 C GLY 473  ? C GLY 473  
103 1 Y 1 C HIS 474  ? C HIS 474  
104 1 Y 1 C GLU 475  ? C GLU 475  
105 1 Y 1 C GLN 476  ? C GLN 476  
106 1 Y 1 C SER 477  ? C SER 477  
107 1 Y 1 C PRO 478  ? C PRO 478  
108 1 Y 1 C ALA 479  ? C ALA 479  
109 1 Y 1 C HIS 480  ? C HIS 480  
110 1 Y 1 C GLY 481  ? C GLY 481  
111 1 Y 1 C ALA 482  ? C ALA 482  
112 1 Y 1 C ALA 483  ? C ALA 483  
113 1 Y 1 C THR 484  ? C THR 484  
114 1 Y 1 C ALA 485  ? C ALA 485  
115 1 Y 1 C ASP 486  ? C ASP 486  
116 1 Y 1 D MET 1    ? D MET 1    
117 1 Y 1 D ARG 2    ? D ARG 2    
118 1 Y 1 D ASN 3    ? D ASN 3    
119 1 Y 1 D ASP 4    ? D ASP 4    
120 1 Y 1 E MET 1    ? E MET 1    
121 1 Y 1 E GLN 2    ? E GLN 2    
122 1 Y 1 E LYS 3    ? E LYS 3    
123 1 Y 1 E PRO 4    ? E PRO 4    
124 1 Y 1 E ARG 5    ? E ARG 5    
125 1 Y 1 E LEU 6    ? E LEU 6    
126 1 Y 1 E THR 7    ? E THR 7    
127 1 Y 1 E SER 8    ? E SER 8    
128 1 Y 1 E ARG 9    ? E ARG 9    
129 1 Y 1 E MET 10   ? E MET 10   
130 1 Y 1 E ILE 11   ? E ILE 11   
131 1 Y 1 E ARG 12   ? E ARG 12   
132 1 Y 1 E PHE 13   ? E PHE 13   
133 1 Y 1 E GLY 14   ? E GLY 14   
134 1 Y 1 E TRP 15   ? E TRP 15   
135 1 Y 1 E VAL 16   ? E VAL 16   
136 1 Y 1 E GLY 17   ? E GLY 17   
137 1 Y 1 E LEU 18   ? E LEU 18   
138 1 Y 1 E LEU 19   ? E LEU 19   
139 1 Y 1 E VAL 20   ? E VAL 20   
140 1 Y 1 E LEU 21   ? E LEU 21   
141 1 Y 1 E LEU 22   ? E LEU 22   
142 1 Y 1 E LEU 23   ? E LEU 23   
143 1 Y 1 E THR 24   ? E THR 24   
144 1 Y 1 E ALA 25   ? E ALA 25   
145 1 Y 1 E ALA 190  ? E ALA 190  
146 1 Y 1 E THR 191  ? E THR 191  
147 1 Y 1 E ILE 192  ? E ILE 192  
148 1 Y 1 E ASP 193  ? E ASP 193  
149 1 Y 1 E ASP 194  ? E ASP 194  
150 1 Y 1 E VAL 195  ? E VAL 195  
151 1 Y 1 E PRO 196  ? E PRO 196  
152 1 Y 1 E PRO 197  ? E PRO 197  
153 1 Y 1 E ASP 198  ? E ASP 198  
154 1 Y 1 E GLN 199  ? E GLN 199  
155 1 Y 1 E ARG 200  ? E ARG 200  
156 1 Y 1 E ALA 201  ? E ALA 201  
157 1 Y 1 E GLN 202  ? E GLN 202  
158 1 Y 1 E LEU 203  ? E LEU 203  
159 1 Y 1 E GLY 204  ? E GLY 204  
160 1 Y 1 E ASN 205  ? E ASN 205  
161 1 Y 1 F MET 1    ? F MET 1    
162 1 Y 1 F ALA 2    ? F ALA 2    
163 1 Y 1 F THR 3    ? F THR 3    
164 1 Y 1 F THR 4    ? F THR 4    
165 1 Y 1 F SER 5    ? F SER 5    
166 1 Y 1 F ILE 6    ? F ILE 6    
167 1 Y 1 F SER 7    ? F SER 7    
168 1 Y 1 F GLN 8    ? F GLN 8    
169 1 Y 1 F THR 9    ? F THR 9    
170 1 Y 1 F ARG 10   ? F ARG 10   
171 1 Y 1 F ASN 407  ? F ASN 407  
172 1 Y 1 F SER 408  ? F SER 408  
173 1 Y 1 F GLY 409  ? F GLY 409  
174 1 Y 1 F HIS 410  ? F HIS 410  
175 1 Y 1 F HIS 411  ? F HIS 411  
176 1 Y 1 G MET 1    ? G MET 1    
177 1 Y 1 G SER 2    ? G SER 2    
178 1 Y 1 G TYR 3    ? G TYR 3    
179 1 Y 1 G ARG 4    ? G ARG 4    
180 1 Y 1 G PRO 5    ? G PRO 5    
181 1 Y 1 G ASN 6    ? G ASN 6    
182 1 Y 1 G TYR 7    ? G TYR 7    
183 1 Y 1 G SER 8    ? G SER 8    
184 1 Y 1 G ALA 9    ? G ALA 9    
185 1 Y 1 G SER 10   ? G SER 10   
186 1 Y 1 G ARG 11   ? G ARG 11   
187 1 Y 1 G TYR 12   ? G TYR 12   
188 1 Y 1 G THR 13   ? G THR 13   
189 1 Y 1 G ALA 14   ? G ALA 14   
190 1 Y 1 G GLY 15   ? G GLY 15   
191 1 Y 1 G ARG 16   ? G ARG 16   
192 1 Y 1 G PRO 17   ? G PRO 17   
193 1 Y 1 G ALA 18   ? G ALA 18   
194 1 Y 1 G GLN 19   ? G GLN 19   
195 1 Y 1 G PRO 20   ? G PRO 20   
196 1 Y 1 G VAL 21   ? G VAL 21   
197 1 Y 1 G ARG 22   ? G ARG 22   
198 1 Y 1 G THR 23   ? G THR 23   
199 1 Y 1 G ALA 24   ? G ALA 24   
200 1 Y 1 G ARG 25   ? G ARG 25   
201 1 Y 1 G THR 26   ? G THR 26   
202 1 Y 1 G MET 27   ? G MET 27   
203 1 Y 1 G ALA 28   ? G ALA 28   
204 1 Y 1 G GLU 29   ? G GLU 29   
205 1 Y 1 G PRO 30   ? G PRO 30   
206 1 Y 1 G SER 31   ? G SER 31   
207 1 Y 1 G GLU 112  ? G GLU 112  
208 1 Y 1 I MET 1    ? H MET 1    
209 1 Y 1 I GLN 2    ? H GLN 2    
210 1 Y 1 I PRO 3    ? H PRO 3    
211 1 Y 1 I GLU 4    ? H GLU 4    
212 1 Y 1 I TRP 5    ? H TRP 5    
213 1 Y 1 I SER 6    ? H SER 6    
214 1 Y 1 I GLY 7    ? H GLY 7    
215 1 Y 1 I ASP 8    ? H ASP 8    
216 1 Y 1 I PRO 9    ? H PRO 9    
217 1 Y 1 I GLU 10   ? H GLU 10   
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
F3S FE1  FE N N 88  
F3S FE3  FE N N 89  
F3S FE4  FE N N 90  
F3S S1   S  N N 91  
F3S S2   S  N N 92  
F3S S3   S  N N 93  
F3S S4   S  N N 94  
GLN N    N  N N 95  
GLN CA   C  N S 96  
GLN C    C  N N 97  
GLN O    O  N N 98  
GLN CB   C  N N 99  
GLN CG   C  N N 100 
GLN CD   C  N N 101 
GLN OE1  O  N N 102 
GLN NE2  N  N N 103 
GLN OXT  O  N N 104 
GLN H    H  N N 105 
GLN H2   H  N N 106 
GLN HA   H  N N 107 
GLN HB2  H  N N 108 
GLN HB3  H  N N 109 
GLN HG2  H  N N 110 
GLN HG3  H  N N 111 
GLN HE21 H  N N 112 
GLN HE22 H  N N 113 
GLN HXT  H  N N 114 
GLU N    N  N N 115 
GLU CA   C  N S 116 
GLU C    C  N N 117 
GLU O    O  N N 118 
GLU CB   C  N N 119 
GLU CG   C  N N 120 
GLU CD   C  N N 121 
GLU OE1  O  N N 122 
GLU OE2  O  N N 123 
GLU OXT  O  N N 124 
GLU H    H  N N 125 
GLU H2   H  N N 126 
GLU HA   H  N N 127 
GLU HB2  H  N N 128 
GLU HB3  H  N N 129 
GLU HG2  H  N N 130 
GLU HG3  H  N N 131 
GLU HE2  H  N N 132 
GLU HXT  H  N N 133 
GLY N    N  N N 134 
GLY CA   C  N N 135 
GLY C    C  N N 136 
GLY O    O  N N 137 
GLY OXT  O  N N 138 
GLY H    H  N N 139 
GLY H2   H  N N 140 
GLY HA2  H  N N 141 
GLY HA3  H  N N 142 
GLY HXT  H  N N 143 
HEC FE   FE N N 144 
HEC CHA  C  N N 145 
HEC CHB  C  N N 146 
HEC CHC  C  N N 147 
HEC CHD  C  N N 148 
HEC NA   N  Y N 149 
HEC C1A  C  Y N 150 
HEC C2A  C  Y N 151 
HEC C3A  C  Y N 152 
HEC C4A  C  Y N 153 
HEC CMA  C  N N 154 
HEC CAA  C  N N 155 
HEC CBA  C  N N 156 
HEC CGA  C  N N 157 
HEC O1A  O  N N 158 
HEC O2A  O  N N 159 
HEC NB   N  Y N 160 
HEC C1B  C  Y N 161 
HEC C2B  C  Y N 162 
HEC C3B  C  Y N 163 
HEC C4B  C  Y N 164 
HEC CMB  C  N N 165 
HEC CAB  C  N N 166 
HEC CBB  C  N N 167 
HEC NC   N  Y N 168 
HEC C1C  C  Y N 169 
HEC C2C  C  Y N 170 
HEC C3C  C  Y N 171 
HEC C4C  C  Y N 172 
HEC CMC  C  N N 173 
HEC CAC  C  N N 174 
HEC CBC  C  N N 175 
HEC ND   N  Y N 176 
HEC C1D  C  Y N 177 
HEC C2D  C  Y N 178 
HEC C3D  C  Y N 179 
HEC C4D  C  Y N 180 
HEC CMD  C  N N 181 
HEC CAD  C  N N 182 
HEC CBD  C  N N 183 
HEC CGD  C  N N 184 
HEC O1D  O  N N 185 
HEC O2D  O  N N 186 
HEC HHA  H  N N 187 
HEC HHB  H  N N 188 
HEC HHC  H  N N 189 
HEC HHD  H  N N 190 
HEC HMA1 H  N N 191 
HEC HMA2 H  N N 192 
HEC HMA3 H  N N 193 
HEC HAA1 H  N N 194 
HEC HAA2 H  N N 195 
HEC HBA1 H  N N 196 
HEC HBA2 H  N N 197 
HEC H2A  H  N N 198 
HEC HMB1 H  N N 199 
HEC HMB2 H  N N 200 
HEC HMB3 H  N N 201 
HEC HAB  H  N N 202 
HEC HBB1 H  N N 203 
HEC HBB2 H  N N 204 
HEC HBB3 H  N N 205 
HEC HMC1 H  N N 206 
HEC HMC2 H  N N 207 
HEC HMC3 H  N N 208 
HEC HAC  H  N N 209 
HEC HBC1 H  N N 210 
HEC HBC2 H  N N 211 
HEC HBC3 H  N N 212 
HEC HMD1 H  N N 213 
HEC HMD2 H  N N 214 
HEC HMD3 H  N N 215 
HEC HAD1 H  N N 216 
HEC HAD2 H  N N 217 
HEC HBD1 H  N N 218 
HEC HBD2 H  N N 219 
HEC H2D  H  N N 220 
HIS N    N  N N 221 
HIS CA   C  N S 222 
HIS C    C  N N 223 
HIS O    O  N N 224 
HIS CB   C  N N 225 
HIS CG   C  Y N 226 
HIS ND1  N  Y N 227 
HIS CD2  C  Y N 228 
HIS CE1  C  Y N 229 
HIS NE2  N  Y N 230 
HIS OXT  O  N N 231 
HIS H    H  N N 232 
HIS H2   H  N N 233 
HIS HA   H  N N 234 
HIS HB2  H  N N 235 
HIS HB3  H  N N 236 
HIS HD1  H  N N 237 
HIS HD2  H  N N 238 
HIS HE1  H  N N 239 
HIS HE2  H  N N 240 
HIS HXT  H  N N 241 
ILE N    N  N N 242 
ILE CA   C  N S 243 
ILE C    C  N N 244 
ILE O    O  N N 245 
ILE CB   C  N S 246 
ILE CG1  C  N N 247 
ILE CG2  C  N N 248 
ILE CD1  C  N N 249 
ILE OXT  O  N N 250 
ILE H    H  N N 251 
ILE H2   H  N N 252 
ILE HA   H  N N 253 
ILE HB   H  N N 254 
ILE HG12 H  N N 255 
ILE HG13 H  N N 256 
ILE HG21 H  N N 257 
ILE HG22 H  N N 258 
ILE HG23 H  N N 259 
ILE HD11 H  N N 260 
ILE HD12 H  N N 261 
ILE HD13 H  N N 262 
ILE HXT  H  N N 263 
LEU N    N  N N 264 
LEU CA   C  N S 265 
LEU C    C  N N 266 
LEU O    O  N N 267 
LEU CB   C  N N 268 
LEU CG   C  N N 269 
LEU CD1  C  N N 270 
LEU CD2  C  N N 271 
LEU OXT  O  N N 272 
LEU H    H  N N 273 
LEU H2   H  N N 274 
LEU HA   H  N N 275 
LEU HB2  H  N N 276 
LEU HB3  H  N N 277 
LEU HG   H  N N 278 
LEU HD11 H  N N 279 
LEU HD12 H  N N 280 
LEU HD13 H  N N 281 
LEU HD21 H  N N 282 
LEU HD22 H  N N 283 
LEU HD23 H  N N 284 
LEU HXT  H  N N 285 
LYS N    N  N N 286 
LYS CA   C  N S 287 
LYS C    C  N N 288 
LYS O    O  N N 289 
LYS CB   C  N N 290 
LYS CG   C  N N 291 
LYS CD   C  N N 292 
LYS CE   C  N N 293 
LYS NZ   N  N N 294 
LYS OXT  O  N N 295 
LYS H    H  N N 296 
LYS H2   H  N N 297 
LYS HA   H  N N 298 
LYS HB2  H  N N 299 
LYS HB3  H  N N 300 
LYS HG2  H  N N 301 
LYS HG3  H  N N 302 
LYS HD2  H  N N 303 
LYS HD3  H  N N 304 
LYS HE2  H  N N 305 
LYS HE3  H  N N 306 
LYS HZ1  H  N N 307 
LYS HZ2  H  N N 308 
LYS HZ3  H  N N 309 
LYS HXT  H  N N 310 
MET N    N  N N 311 
MET CA   C  N S 312 
MET C    C  N N 313 
MET O    O  N N 314 
MET CB   C  N N 315 
MET CG   C  N N 316 
MET SD   S  N N 317 
MET CE   C  N N 318 
MET OXT  O  N N 319 
MET H    H  N N 320 
MET H2   H  N N 321 
MET HA   H  N N 322 
MET HB2  H  N N 323 
MET HB3  H  N N 324 
MET HG2  H  N N 325 
MET HG3  H  N N 326 
MET HE1  H  N N 327 
MET HE2  H  N N 328 
MET HE3  H  N N 329 
MET HXT  H  N N 330 
PHE N    N  N N 331 
PHE CA   C  N S 332 
PHE C    C  N N 333 
PHE O    O  N N 334 
PHE CB   C  N N 335 
PHE CG   C  Y N 336 
PHE CD1  C  Y N 337 
PHE CD2  C  Y N 338 
PHE CE1  C  Y N 339 
PHE CE2  C  Y N 340 
PHE CZ   C  Y N 341 
PHE OXT  O  N N 342 
PHE H    H  N N 343 
PHE H2   H  N N 344 
PHE HA   H  N N 345 
PHE HB2  H  N N 346 
PHE HB3  H  N N 347 
PHE HD1  H  N N 348 
PHE HD2  H  N N 349 
PHE HE1  H  N N 350 
PHE HE2  H  N N 351 
PHE HZ   H  N N 352 
PHE HXT  H  N N 353 
PRO N    N  N N 354 
PRO CA   C  N S 355 
PRO C    C  N N 356 
PRO O    O  N N 357 
PRO CB   C  N N 358 
PRO CG   C  N N 359 
PRO CD   C  N N 360 
PRO OXT  O  N N 361 
PRO H    H  N N 362 
PRO HA   H  N N 363 
PRO HB2  H  N N 364 
PRO HB3  H  N N 365 
PRO HG2  H  N N 366 
PRO HG3  H  N N 367 
PRO HD2  H  N N 368 
PRO HD3  H  N N 369 
PRO HXT  H  N N 370 
SER N    N  N N 371 
SER CA   C  N S 372 
SER C    C  N N 373 
SER O    O  N N 374 
SER CB   C  N N 375 
SER OG   O  N N 376 
SER OXT  O  N N 377 
SER H    H  N N 378 
SER H2   H  N N 379 
SER HA   H  N N 380 
SER HB2  H  N N 381 
SER HB3  H  N N 382 
SER HG   H  N N 383 
SER HXT  H  N N 384 
SF4 FE1  FE N N 385 
SF4 FE2  FE N N 386 
SF4 FE3  FE N N 387 
SF4 FE4  FE N N 388 
SF4 S1   S  N N 389 
SF4 S2   S  N N 390 
SF4 S3   S  N N 391 
SF4 S4   S  N N 392 
THR N    N  N N 393 
THR CA   C  N S 394 
THR C    C  N N 395 
THR O    O  N N 396 
THR CB   C  N R 397 
THR OG1  O  N N 398 
THR CG2  C  N N 399 
THR OXT  O  N N 400 
THR H    H  N N 401 
THR H2   H  N N 402 
THR HA   H  N N 403 
THR HB   H  N N 404 
THR HG1  H  N N 405 
THR HG21 H  N N 406 
THR HG22 H  N N 407 
THR HG23 H  N N 408 
THR HXT  H  N N 409 
TRP N    N  N N 410 
TRP CA   C  N S 411 
TRP C    C  N N 412 
TRP O    O  N N 413 
TRP CB   C  N N 414 
TRP CG   C  Y N 415 
TRP CD1  C  Y N 416 
TRP CD2  C  Y N 417 
TRP NE1  N  Y N 418 
TRP CE2  C  Y N 419 
TRP CE3  C  Y N 420 
TRP CZ2  C  Y N 421 
TRP CZ3  C  Y N 422 
TRP CH2  C  Y N 423 
TRP OXT  O  N N 424 
TRP H    H  N N 425 
TRP H2   H  N N 426 
TRP HA   H  N N 427 
TRP HB2  H  N N 428 
TRP HB3  H  N N 429 
TRP HD1  H  N N 430 
TRP HE1  H  N N 431 
TRP HE3  H  N N 432 
TRP HZ2  H  N N 433 
TRP HZ3  H  N N 434 
TRP HH2  H  N N 435 
TRP HXT  H  N N 436 
TYR N    N  N N 437 
TYR CA   C  N S 438 
TYR C    C  N N 439 
TYR O    O  N N 440 
TYR CB   C  N N 441 
TYR CG   C  Y N 442 
TYR CD1  C  Y N 443 
TYR CD2  C  Y N 444 
TYR CE1  C  Y N 445 
TYR CE2  C  Y N 446 
TYR CZ   C  Y N 447 
TYR OH   O  N N 448 
TYR OXT  O  N N 449 
TYR H    H  N N 450 
TYR H2   H  N N 451 
TYR HA   H  N N 452 
TYR HB2  H  N N 453 
TYR HB3  H  N N 454 
TYR HD1  H  N N 455 
TYR HD2  H  N N 456 
TYR HE1  H  N N 457 
TYR HE2  H  N N 458 
TYR HH   H  N N 459 
TYR HXT  H  N N 460 
VAL N    N  N N 461 
VAL CA   C  N S 462 
VAL C    C  N N 463 
VAL O    O  N N 464 
VAL CB   C  N N 465 
VAL CG1  C  N N 466 
VAL CG2  C  N N 467 
VAL OXT  O  N N 468 
VAL H    H  N N 469 
VAL H2   H  N N 470 
VAL HA   H  N N 471 
VAL HB   H  N N 472 
VAL HG11 H  N N 473 
VAL HG12 H  N N 474 
VAL HG13 H  N N 475 
VAL HG21 H  N N 476 
VAL HG22 H  N N 477 
VAL HG23 H  N N 478 
VAL HXT  H  N N 479 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
F3S FE1 S1   sing N N 83  
F3S FE1 S2   sing N N 84  
F3S FE1 S3   sing N N 85  
F3S FE3 S1   sing N N 86  
F3S FE3 S3   sing N N 87  
F3S FE3 S4   sing N N 88  
F3S FE4 S2   sing N N 89  
F3S FE4 S3   sing N N 90  
F3S FE4 S4   sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HEC FE  NA   sing N N 138 
HEC FE  NB   sing N N 139 
HEC FE  NC   sing N N 140 
HEC FE  ND   sing N N 141 
HEC CHA C1A  doub N N 142 
HEC CHA C4D  sing N N 143 
HEC CHA HHA  sing N N 144 
HEC CHB C4A  doub N N 145 
HEC CHB C1B  sing N N 146 
HEC CHB HHB  sing N N 147 
HEC CHC C4B  doub N N 148 
HEC CHC C1C  sing N N 149 
HEC CHC HHC  sing N N 150 
HEC CHD C4C  doub N N 151 
HEC CHD C1D  sing N N 152 
HEC CHD HHD  sing N N 153 
HEC NA  C1A  sing Y N 154 
HEC NA  C4A  sing Y N 155 
HEC C1A C2A  sing Y N 156 
HEC C2A C3A  doub Y N 157 
HEC C2A CAA  sing N N 158 
HEC C3A C4A  sing Y N 159 
HEC C3A CMA  sing N N 160 
HEC CMA HMA1 sing N N 161 
HEC CMA HMA2 sing N N 162 
HEC CMA HMA3 sing N N 163 
HEC CAA CBA  sing N N 164 
HEC CAA HAA1 sing N N 165 
HEC CAA HAA2 sing N N 166 
HEC CBA CGA  sing N N 167 
HEC CBA HBA1 sing N N 168 
HEC CBA HBA2 sing N N 169 
HEC CGA O1A  doub N N 170 
HEC CGA O2A  sing N N 171 
HEC O2A H2A  sing N N 172 
HEC NB  C1B  sing Y N 173 
HEC NB  C4B  sing Y N 174 
HEC C1B C2B  doub Y N 175 
HEC C2B C3B  sing Y N 176 
HEC C2B CMB  sing N N 177 
HEC C3B C4B  sing Y N 178 
HEC C3B CAB  doub N E 179 
HEC CMB HMB1 sing N N 180 
HEC CMB HMB2 sing N N 181 
HEC CMB HMB3 sing N N 182 
HEC CAB CBB  sing N N 183 
HEC CAB HAB  sing N N 184 
HEC CBB HBB1 sing N N 185 
HEC CBB HBB2 sing N N 186 
HEC CBB HBB3 sing N N 187 
HEC NC  C1C  sing Y N 188 
HEC NC  C4C  sing Y N 189 
HEC C1C C2C  doub Y N 190 
HEC C2C C3C  sing Y N 191 
HEC C2C CMC  sing N N 192 
HEC C3C C4C  sing Y N 193 
HEC C3C CAC  doub N E 194 
HEC CMC HMC1 sing N N 195 
HEC CMC HMC2 sing N N 196 
HEC CMC HMC3 sing N N 197 
HEC CAC CBC  sing N N 198 
HEC CAC HAC  sing N N 199 
HEC CBC HBC1 sing N N 200 
HEC CBC HBC2 sing N N 201 
HEC CBC HBC3 sing N N 202 
HEC ND  C1D  sing Y N 203 
HEC ND  C4D  sing Y N 204 
HEC C1D C2D  doub Y N 205 
HEC C2D C3D  sing Y N 206 
HEC C2D CMD  sing N N 207 
HEC C3D C4D  doub Y N 208 
HEC C3D CAD  sing N N 209 
HEC CMD HMD1 sing N N 210 
HEC CMD HMD2 sing N N 211 
HEC CMD HMD3 sing N N 212 
HEC CAD CBD  sing N N 213 
HEC CAD HAD1 sing N N 214 
HEC CAD HAD2 sing N N 215 
HEC CBD CGD  sing N N 216 
HEC CBD HBD1 sing N N 217 
HEC CBD HBD2 sing N N 218 
HEC CGD O1D  doub N N 219 
HEC CGD O2D  sing N N 220 
HEC O2D H2D  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 
SF4 FE1 S2   sing N N 381 
SF4 FE1 S3   sing N N 382 
SF4 FE1 S4   sing N N 383 
SF4 FE2 S1   sing N N 384 
SF4 FE2 S3   sing N N 385 
SF4 FE2 S4   sing N N 386 
SF4 FE3 S1   sing N N 387 
SF4 FE3 S2   sing N N 388 
SF4 FE3 S4   sing N N 389 
SF4 FE4 S1   sing N N 390 
SF4 FE4 S2   sing N N 391 
SF4 FE4 S3   sing N N 392 
THR N   CA   sing N N 393 
THR N   H    sing N N 394 
THR N   H2   sing N N 395 
THR CA  C    sing N N 396 
THR CA  CB   sing N N 397 
THR CA  HA   sing N N 398 
THR C   O    doub N N 399 
THR C   OXT  sing N N 400 
THR CB  OG1  sing N N 401 
THR CB  CG2  sing N N 402 
THR CB  HB   sing N N 403 
THR OG1 HG1  sing N N 404 
THR CG2 HG21 sing N N 405 
THR CG2 HG22 sing N N 406 
THR CG2 HG23 sing N N 407 
THR OXT HXT  sing N N 408 
TRP N   CA   sing N N 409 
TRP N   H    sing N N 410 
TRP N   H2   sing N N 411 
TRP CA  C    sing N N 412 
TRP CA  CB   sing N N 413 
TRP CA  HA   sing N N 414 
TRP C   O    doub N N 415 
TRP C   OXT  sing N N 416 
TRP CB  CG   sing N N 417 
TRP CB  HB2  sing N N 418 
TRP CB  HB3  sing N N 419 
TRP CG  CD1  doub Y N 420 
TRP CG  CD2  sing Y N 421 
TRP CD1 NE1  sing Y N 422 
TRP CD1 HD1  sing N N 423 
TRP CD2 CE2  doub Y N 424 
TRP CD2 CE3  sing Y N 425 
TRP NE1 CE2  sing Y N 426 
TRP NE1 HE1  sing N N 427 
TRP CE2 CZ2  sing Y N 428 
TRP CE3 CZ3  doub Y N 429 
TRP CE3 HE3  sing N N 430 
TRP CZ2 CH2  doub Y N 431 
TRP CZ2 HZ2  sing N N 432 
TRP CZ3 CH2  sing Y N 433 
TRP CZ3 HZ3  sing N N 434 
TRP CH2 HH2  sing N N 435 
TRP OXT HXT  sing N N 436 
TYR N   CA   sing N N 437 
TYR N   H    sing N N 438 
TYR N   H2   sing N N 439 
TYR CA  C    sing N N 440 
TYR CA  CB   sing N N 441 
TYR CA  HA   sing N N 442 
TYR C   O    doub N N 443 
TYR C   OXT  sing N N 444 
TYR CB  CG   sing N N 445 
TYR CB  HB2  sing N N 446 
TYR CB  HB3  sing N N 447 
TYR CG  CD1  doub Y N 448 
TYR CG  CD2  sing Y N 449 
TYR CD1 CE1  sing Y N 450 
TYR CD1 HD1  sing N N 451 
TYR CD2 CE2  doub Y N 452 
TYR CD2 HD2  sing N N 453 
TYR CE1 CZ   doub Y N 454 
TYR CE1 HE1  sing N N 455 
TYR CE2 CZ   sing Y N 456 
TYR CE2 HE2  sing N N 457 
TYR CZ  OH   sing N N 458 
TYR OH  HH   sing N N 459 
TYR OXT HXT  sing N N 460 
VAL N   CA   sing N N 461 
VAL N   H    sing N N 462 
VAL N   H2   sing N N 463 
VAL CA  C    sing N N 464 
VAL CA  CB   sing N N 465 
VAL CA  HA   sing N N 466 
VAL C   O    doub N N 467 
VAL C   OXT  sing N N 468 
VAL CB  CG1  sing N N 469 
VAL CB  CG2  sing N N 470 
VAL CB  HB   sing N N 471 
VAL CG1 HG11 sing N N 472 
VAL CG1 HG12 sing N N 473 
VAL CG1 HG13 sing N N 474 
VAL CG2 HG21 sing N N 475 
VAL CG2 HG22 sing N N 476 
VAL CG2 HG23 sing N N 477 
VAL OXT HXT  sing N N 478 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           '31870740, 32171227, 31570738, 32000034, 82101628' 
_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   8K9F 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9ILT 
_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]   0.007041 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006533 
_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]   0.005768 
_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  
FE 
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   . ALA A 1  2    ? -72.547 -16.041  87.719  1.00 112.85 ?  2    ALA A N   1 
ATOM   2     C  CA  . ALA A 1  2    ? -73.751 -16.195  88.527  1.00 117.31 ?  2    ALA A CA  1 
ATOM   3     C  C   . ALA A 1  2    ? -74.991 -15.809  87.735  1.00 118.81 ?  2    ALA A C   1 
ATOM   4     O  O   . ALA A 1  2    ? -76.118 -15.993  88.194  1.00 121.89 ?  2    ALA A O   1 
ATOM   5     C  CB  . ALA A 1  2    ? -73.649 -15.364  89.788  1.00 118.08 ?  2    ALA A CB  1 
ATOM   6     N  N   . GLN A 1  3    ? -74.772 -15.271  86.536  1.00 138.31 ?  3    GLN A N   1 
ATOM   7     C  CA  . GLN A 1  3    ? -75.886 -14.880  85.681  1.00 138.00 ?  3    GLN A CA  1 
ATOM   8     C  C   . GLN A 1  3    ? -76.522 -16.092  85.012  1.00 144.16 ?  3    GLN A C   1 
ATOM   9     O  O   . GLN A 1  3    ? -77.736 -16.300  85.110  1.00 153.25 ?  3    GLN A O   1 
ATOM   10    C  CB  . GLN A 1  3    ? -75.411 -13.878  84.626  1.00 136.41 ?  3    GLN A CB  1 
ATOM   11    C  CG  . GLN A 1  3    ? -76.516 -12.994  84.067  1.00 134.67 ?  3    GLN A CG  1 
ATOM   12    C  CD  . GLN A 1  3    ? -76.645 -11.679  84.813  1.00 136.61 ?  3    GLN A CD  1 
ATOM   13    O  OE1 . GLN A 1  3    ? -75.651 -11.107  85.260  1.00 134.80 ?  3    GLN A OE1 1 
ATOM   14    N  NE2 . GLN A 1  3    ? -77.875 -11.197  84.956  1.00 136.66 ?  3    GLN A NE2 1 
ATOM   15    N  N   . ILE A 1  4    ? -75.713 -16.904  84.333  1.00 112.51 ?  4    ILE A N   1 
ATOM   16    C  CA  . ILE A 1  4    ? -76.225 -17.995  83.511  1.00 108.37 ?  4    ILE A CA  1 
ATOM   17    C  C   . ILE A 1  4    ? -75.453 -19.278  83.785  1.00 102.68 ?  4    ILE A C   1 
ATOM   18    O  O   . ILE A 1  4    ? -75.567 -20.252  83.032  1.00 102.32 ?  4    ILE A O   1 
ATOM   19    C  CB  . ILE A 1  4    ? -76.153 -17.632  82.016  1.00 107.26 ?  4    ILE A CB  1 
ATOM   20    C  CG1 . ILE A 1  4    ? -74.720 -17.248  81.641  1.00 108.46 ?  4    ILE A CG1 1 
ATOM   21    C  CG2 . ILE A 1  4    ? -77.117 -16.503  81.690  1.00 113.21 ?  4    ILE A CG2 1 
ATOM   22    C  CD1 . ILE A 1  4    ? -74.562 -16.749  80.224  1.00 113.21 ?  4    ILE A CD1 1 
ATOM   23    N  N   . PHE A 1  5    ? -74.668 -19.298  84.862  1.00 122.84 ?  5    PHE A N   1 
ATOM   24    C  CA  . PHE A 1  5    ? -73.807 -20.436  85.137  1.00 122.36 ?  5    PHE A CA  1 
ATOM   25    C  C   . PHE A 1  5    ? -73.886 -20.841  86.602  1.00 119.71 ?  5    PHE A C   1 
ATOM   26    O  O   . PHE A 1  5    ? -73.974 -19.975  87.484  1.00 120.33 ?  5    PHE A O   1 
ATOM   27    C  CB  . PHE A 1  5    ? -72.350 -20.122  84.770  1.00 125.84 ?  5    PHE A CB  1 
ATOM   28    C  CG  . PHE A 1  5    ? -72.052 -20.262  83.306  1.00 132.57 ?  5    PHE A CG  1 
ATOM   29    C  CD1 . PHE A 1  5    ? -71.970 -21.514  82.718  1.00 129.69 ?  5    PHE A CD1 1 
ATOM   30    C  CD2 . PHE A 1  5    ? -71.852 -19.142  82.516  1.00 129.46 ?  5    PHE A CD2 1 
ATOM   31    C  CE1 . PHE A 1  5    ? -71.696 -21.645  81.369  1.00 118.42 ?  5    PHE A CE1 1 
ATOM   32    C  CE2 . PHE A 1  5    ? -71.577 -19.267  81.167  1.00 118.14 ?  5    PHE A CE2 1 
ATOM   33    C  CZ  . PHE A 1  5    ? -71.498 -20.519  80.594  1.00 114.09 ?  5    PHE A CZ  1 
ATOM   34    N  N   . PRO A 1  6    ? -73.864 -22.141  86.888  1.00 83.68  ?  6    PRO A N   1 
ATOM   35    C  CA  . PRO A 1  6    ? -73.826 -22.597  88.282  1.00 85.01  ?  6    PRO A CA  1 
ATOM   36    C  C   . PRO A 1  6    ? -72.468 -22.324  88.915  1.00 90.33  ?  6    PRO A C   1 
ATOM   37    O  O   . PRO A 1  6    ? -71.494 -21.963  88.252  1.00 89.90  ?  6    PRO A O   1 
ATOM   38    C  CB  . PRO A 1  6    ? -74.106 -24.101  88.176  1.00 87.97  ?  6    PRO A CB  1 
ATOM   39    C  CG  . PRO A 1  6    ? -74.673 -24.301  86.791  1.00 92.38  ?  6    PRO A CG  1 
ATOM   40    C  CD  . PRO A 1  6    ? -74.001 -23.266  85.950  1.00 87.21  ?  6    PRO A CD  1 
ATOM   41    N  N   . ARG A 1  7    ? -72.415 -22.517  90.236  1.00 122.87 ?  7    ARG A N   1 
ATOM   42    C  CA  . ARG A 1  7    ? -71.210 -22.181  90.990  1.00 124.93 ?  7    ARG A CA  1 
ATOM   43    C  C   . ARG A 1  7    ? -70.047 -23.103  90.639  1.00 128.05 ?  7    ARG A C   1 
ATOM   44    O  O   . ARG A 1  7    ? -68.893 -22.663  90.593  1.00 133.90 ?  7    ARG A O   1 
ATOM   45    C  CB  . ARG A 1  7    ? -71.497 -22.236  92.491  1.00 123.77 ?  7    ARG A CB  1 
ATOM   46    C  CG  . ARG A 1  7    ? -70.419 -21.589  93.349  1.00 128.32 ?  7    ARG A CG  1 
ATOM   47    C  CD  . ARG A 1  7    ? -70.837 -21.488  94.812  1.00 134.72 ?  7    ARG A CD  1 
ATOM   48    N  NE  . ARG A 1  7    ? -71.969 -20.589  95.011  1.00 132.92 ?  7    ARG A NE  1 
ATOM   49    C  CZ  . ARG A 1  7    ? -73.213 -20.987  95.239  1.00 127.66 ?  7    ARG A CZ  1 
ATOM   50    N  NH1 . ARG A 1  7    ? -73.527 -22.270  95.306  1.00 123.80 ?  7    ARG A NH1 1 
ATOM   51    N  NH2 . ARG A 1  7    ? -74.165 -20.074  95.407  1.00 117.58 ?  7    ARG A NH2 1 
ATOM   52    N  N   . ASN A 1  8    ? -70.328 -24.383  90.388  1.00 134.99 ?  8    ASN A N   1 
ATOM   53    C  CA  . ASN A 1  8    ? -69.268 -25.359  90.162  1.00 134.78 ?  8    ASN A CA  1 
ATOM   54    C  C   . ASN A 1  8    ? -68.574 -25.198  88.816  1.00 134.48 ?  8    ASN A C   1 
ATOM   55    O  O   . ASN A 1  8    ? -67.510 -25.795  88.618  1.00 131.69 ?  8    ASN A O   1 
ATOM   56    C  CB  . ASN A 1  8    ? -69.833 -26.778  90.278  1.00 136.76 ?  8    ASN A CB  1 
ATOM   57    C  CG  . ASN A 1  8    ? -70.846 -27.096  89.192  1.00 136.59 ?  8    ASN A CG  1 
ATOM   58    O  OD1 . ASN A 1  8    ? -71.388 -26.198  88.547  1.00 134.41 ?  8    ASN A OD1 1 
ATOM   59    N  ND2 . ASN A 1  8    ? -71.106 -28.382  88.984  1.00 136.58 ?  8    ASN A ND2 1 
ATOM   60    N  N   . ALA A 1  9    ? -69.135 -24.404  87.899  1.00 158.97 ?  9    ALA A N   1 
ATOM   61    C  CA  . ALA A 1  9    ? -68.613 -24.348  86.536  1.00 154.60 ?  9    ALA A CA  1 
ATOM   62    C  C   . ALA A 1  9    ? -67.183 -23.822  86.486  1.00 158.59 ?  9    ALA A C   1 
ATOM   63    O  O   . ALA A 1  9    ? -66.414 -24.216  85.601  1.00 161.44 ?  9    ALA A O   1 
ATOM   64    C  CB  . ALA A 1  9    ? -69.523 -23.487  85.661  1.00 155.62 ?  9    ALA A CB  1 
ATOM   65    N  N   . ASN A 1  10   ? -66.811 -22.933  87.411  1.00 160.05 ?  10   ASN A N   1 
ATOM   66    C  CA  . ASN A 1  10   ? -65.450 -22.405  87.422  1.00 158.67 ?  10   ASN A CA  1 
ATOM   67    C  C   . ASN A 1  10   ? -64.426 -23.520  87.591  1.00 158.73 ?  10   ASN A C   1 
ATOM   68    O  O   . ASN A 1  10   ? -63.365 -23.502  86.957  1.00 160.47 ?  10   ASN A O   1 
ATOM   69    C  CB  . ASN A 1  10   ? -65.299 -21.363  88.530  1.00 162.33 ?  10   ASN A CB  1 
ATOM   70    C  CG  . ASN A 1  10   ? -66.231 -20.185  88.350  1.00 160.99 ?  10   ASN A CG  1 
ATOM   71    O  OD1 . ASN A 1  10   ? -66.820 -20.005  87.285  1.00 161.48 ?  10   ASN A OD1 1 
ATOM   72    N  ND2 . ASN A 1  10   ? -66.374 -19.375  89.394  1.00 154.34 ?  10   ASN A ND2 1 
ATOM   73    N  N   . LEU A 1  11   ? -64.730 -24.503  88.440  1.00 123.68 ?  11   LEU A N   1 
ATOM   74    C  CA  . LEU A 1  11   ? -63.850 -25.658  88.586  1.00 121.14 ?  11   LEU A CA  1 
ATOM   75    C  C   . LEU A 1  11   ? -63.943 -26.574  87.371  1.00 125.76 ?  11   LEU A C   1 
ATOM   76    O  O   . LEU A 1  11   ? -62.922 -27.051  86.860  1.00 125.16 ?  11   LEU A O   1 
ATOM   77    C  CB  . LEU A 1  11   ? -64.201 -26.417  89.865  1.00 114.80 ?  11   LEU A CB  1 
ATOM   78    C  CG  . LEU A 1  11   ? -63.368 -27.653  90.206  1.00 112.25 ?  11   LEU A CG  1 
ATOM   79    C  CD1 . LEU A 1  11   ? -61.880 -27.334  90.190  1.00 114.57 ?  11   LEU A CD1 1 
ATOM   80    C  CD2 . LEU A 1  11   ? -63.788 -28.199  91.559  1.00 110.51 ?  11   LEU A CD2 1 
ATOM   81    N  N   . LEU A 1  12   ? -65.165 -26.825  86.893  1.00 123.04 ?  12   LEU A N   1 
ATOM   82    C  CA  . LEU A 1  12   ? -65.364 -27.729  85.762  1.00 122.73 ?  12   LEU A CA  1 
ATOM   83    C  C   . LEU A 1  12   ? -64.640 -27.231  84.516  1.00 116.51 ?  12   LEU A C   1 
ATOM   84    O  O   . LEU A 1  12   ? -63.997 -28.012  83.805  1.00 111.90 ?  12   LEU A O   1 
ATOM   85    C  CB  . LEU A 1  12   ? -66.859 -27.892  85.480  1.00 120.25 ?  12   LEU A CB  1 
ATOM   86    C  CG  . LEU A 1  12   ? -67.593 -29.061  86.140  1.00 116.44 ?  12   LEU A CG  1 
ATOM   87    C  CD1 . LEU A 1  12   ? -67.760 -28.837  87.634  1.00 122.68 ?  12   LEU A CD1 1 
ATOM   88    C  CD2 . LEU A 1  12   ? -68.943 -29.274  85.473  1.00 113.01 ?  12   LEU A CD2 1 
ATOM   89    N  N   . SER A 1  13   ? -64.741 -25.929  84.234  1.00 133.25 ?  13   SER A N   1 
ATOM   90    C  CA  . SER A 1  13   ? -64.120 -25.373  83.034  1.00 135.04 ?  13   SER A CA  1 
ATOM   91    C  C   . SER A 1  13   ? -62.614 -25.604  83.037  1.00 135.21 ?  13   SER A C   1 
ATOM   92    O  O   . SER A 1  13   ? -62.045 -26.075  82.046  1.00 129.05 ?  13   SER A O   1 
ATOM   93    C  CB  . SER A 1  13   ? -64.437 -23.882  82.924  1.00 136.75 ?  13   SER A CB  1 
ATOM   94    O  OG  . SER A 1  13   ? -63.707 -23.137  83.883  1.00 133.49 ?  13   SER A OG  1 
ATOM   95    N  N   . ARG A 1  14   ? -61.951 -25.278  84.150  1.00 139.05 ?  14   ARG A N   1 
ATOM   96    C  CA  . ARG A 1  14   ? -60.517 -25.526  84.255  1.00 137.33 ?  14   ARG A CA  1 
ATOM   97    C  C   . ARG A 1  14   ? -60.210 -27.016  84.177  1.00 125.27 ?  14   ARG A C   1 
ATOM   98    O  O   . ARG A 1  14   ? -59.245 -27.426  83.521  1.00 128.85 ?  14   ARG A O   1 
ATOM   99    C  CB  . ARG A 1  14   ? -59.979 -24.937  85.558  1.00 132.38 ?  14   ARG A CB  1 
ATOM   100   C  CG  . ARG A 1  14   ? -59.991 -23.419  85.608  1.00 137.88 ?  14   ARG A CG  1 
ATOM   101   C  CD  . ARG A 1  14   ? -60.168 -22.930  87.032  1.00 140.30 ?  14   ARG A CD  1 
ATOM   102   N  NE  . ARG A 1  14   ? -60.421 -21.496  87.095  1.00 149.91 ?  14   ARG A NE  1 
ATOM   103   C  CZ  . ARG A 1  14   ? -60.687 -20.833  88.211  1.00 155.87 ?  14   ARG A CZ  1 
ATOM   104   N  NH1 . ARG A 1  14   ? -60.742 -21.446  89.383  1.00 165.25 ?  14   ARG A NH1 1 
ATOM   105   N  NH2 . ARG A 1  14   ? -60.907 -19.523  88.151  1.00 148.47 ?  14   ARG A NH2 1 
ATOM   106   N  N   . LEU A 1  15   ? -61.025 -27.842  84.837  1.00 98.97  ?  15   LEU A N   1 
ATOM   107   C  CA  . LEU A 1  15   ? -60.835 -29.286  84.764  1.00 100.24 ?  15   LEU A CA  1 
ATOM   108   C  C   . LEU A 1  15   ? -61.054 -29.800  83.348  1.00 104.72 ?  15   LEU A C   1 
ATOM   109   O  O   . LEU A 1  15   ? -60.353 -30.713  82.895  1.00 103.91 ?  15   LEU A O   1 
ATOM   110   C  CB  . LEU A 1  15   ? -61.781 -29.990  85.737  1.00 102.35 ?  15   LEU A CB  1 
ATOM   111   C  CG  . LEU A 1  15   ? -61.297 -31.295  86.371  1.00 96.73  ?  15   LEU A CG  1 
ATOM   112   C  CD1 . LEU A 1  15   ? -59.975 -31.089  87.091  1.00 95.48  ?  15   LEU A CD1 1 
ATOM   113   C  CD2 . LEU A 1  15   ? -62.350 -31.843  87.322  1.00 95.47  ?  15   LEU A CD2 1 
ATOM   114   N  N   . SER A 1  16   ? -62.026 -29.226  82.634  1.00 120.62 ?  16   SER A N   1 
ATOM   115   C  CA  . SER A 1  16   ? -62.302 -29.656  81.266  1.00 112.97 ?  16   SER A CA  1 
ATOM   116   C  C   . SER A 1  16   ? -61.112 -29.382  80.355  1.00 106.59 ?  16   SER A C   1 
ATOM   117   O  O   . SER A 1  16   ? -60.734 -30.229  79.537  1.00 100.78 ?  16   SER A O   1 
ATOM   118   C  CB  . SER A 1  16   ? -63.557 -28.958  80.742  1.00 116.00 ?  16   SER A CB  1 
ATOM   119   O  OG  . SER A 1  16   ? -63.273 -27.624  80.356  1.00 120.12 ?  16   SER A OG  1 
ATOM   120   N  N   . ILE A 1  17   ? -60.514 -28.194  80.478  1.00 104.12 ?  17   ILE A N   1 
ATOM   121   C  CA  . ILE A 1  17   ? -59.315 -27.875  79.705  1.00 97.14  ?  17   ILE A CA  1 
ATOM   122   C  C   . ILE A 1  17   ? -58.209 -28.875  80.014  1.00 91.05  ?  17   ILE A C   1 
ATOM   123   O  O   . ILE A 1  17   ? -57.538 -29.389  79.111  1.00 91.35  ?  17   ILE A O   1 
ATOM   124   C  CB  . ILE A 1  17   ? -58.862 -26.431  79.985  1.00 95.61  ?  17   ILE A CB  1 
ATOM   125   C  CG1 . ILE A 1  17   ? -59.967 -25.440  79.614  1.00 98.93  ?  17   ILE A CG1 1 
ATOM   126   C  CG2 . ILE A 1  17   ? -57.582 -26.117  79.228  1.00 102.70 ?  17   ILE A CG2 1 
ATOM   127   C  CD1 . ILE A 1  17   ? -60.461 -25.576  78.191  1.00 92.93  ?  17   ILE A CD1 1 
ATOM   128   N  N   . PHE A 1  18   ? -58.006 -29.166  81.302  1.00 100.56 ?  18   PHE A N   1 
ATOM   129   C  CA  . PHE A 1  18   ? -57.034 -30.179  81.698  1.00 99.62  ?  18   PHE A CA  1 
ATOM   130   C  C   . PHE A 1  18   ? -57.368 -31.535  81.091  1.00 95.98  ?  18   PHE A C   1 
ATOM   131   O  O   . PHE A 1  18   ? -56.495 -32.212  80.534  1.00 96.19  ?  18   PHE A O   1 
ATOM   132   C  CB  . PHE A 1  18   ? -56.978 -30.276  83.222  1.00 100.58 ?  18   PHE A CB  1 
ATOM   133   C  CG  . PHE A 1  18   ? -55.987 -31.280  83.722  1.00 100.29 ?  18   PHE A CG  1 
ATOM   134   C  CD1 . PHE A 1  18   ? -54.628 -31.031  83.647  1.00 104.75 ?  18   PHE A CD1 1 
ATOM   135   C  CD2 . PHE A 1  18   ? -56.417 -32.478  84.262  1.00 102.75 ?  18   PHE A CD2 1 
ATOM   136   C  CE1 . PHE A 1  18   ? -53.717 -31.961  84.106  1.00 107.14 ?  18   PHE A CE1 1 
ATOM   137   C  CE2 . PHE A 1  18   ? -55.515 -33.409  84.722  1.00 103.35 ?  18   PHE A CE2 1 
ATOM   138   C  CZ  . PHE A 1  18   ? -54.164 -33.153  84.644  1.00 107.05 ?  18   PHE A CZ  1 
ATOM   139   N  N   . ALA A 1  19   ? -58.632 -31.953  81.197  1.00 76.40  ?  19   ALA A N   1 
ATOM   140   C  CA  . ALA A 1  19   ? -59.039 -33.236  80.633  1.00 72.56  ?  19   ALA A CA  1 
ATOM   141   C  C   . ALA A 1  19   ? -58.854 -33.260  79.121  1.00 72.20  ?  19   ALA A C   1 
ATOM   142   O  O   . ALA A 1  19   ? -58.483 -34.292  78.549  1.00 68.75  ?  19   ALA A O   1 
ATOM   143   C  CB  . ALA A 1  19   ? -60.493 -33.530  81.001  1.00 68.56  ?  19   ALA A CB  1 
ATOM   144   N  N   . LEU A 1  20   ? -59.110 -32.130  78.457  1.00 95.23  ?  20   LEU A N   1 
ATOM   145   C  CA  . LEU A 1  20   ? -58.913 -32.050  77.013  1.00 92.48  ?  20   LEU A CA  1 
ATOM   146   C  C   . LEU A 1  20   ? -57.459 -32.319  76.643  1.00 93.50  ?  20   LEU A C   1 
ATOM   147   O  O   . LEU A 1  20   ? -57.174 -33.091  75.721  1.00 89.08  ?  20   LEU A O   1 
ATOM   148   C  CB  . LEU A 1  20   ? -59.356 -30.678  76.502  1.00 97.59  ?  20   LEU A CB  1 
ATOM   149   C  CG  . LEU A 1  20   ? -59.333 -30.467  74.986  1.00 91.86  ?  20   LEU A CG  1 
ATOM   150   C  CD1 . LEU A 1  20   ? -60.312 -31.403  74.292  1.00 86.31  ?  20   LEU A CD1 1 
ATOM   151   C  CD2 . LEU A 1  20   ? -59.636 -29.015  74.645  1.00 82.74  ?  20   LEU A CD2 1 
ATOM   152   N  N   . VAL A 1  21   ? -56.523 -31.693  77.363  1.00 81.53  ?  21   VAL A N   1 
ATOM   153   C  CA  . VAL A 1  21   ? -55.104 -31.878  77.071  1.00 73.36  ?  21   VAL A CA  1 
ATOM   154   C  C   . VAL A 1  21   ? -54.702 -33.335  77.264  1.00 76.75  ?  21   VAL A C   1 
ATOM   155   O  O   . VAL A 1  21   ? -53.968 -33.906  76.448  1.00 79.18  ?  21   VAL A O   1 
ATOM   156   C  CB  . VAL A 1  21   ? -54.256 -30.933  77.942  1.00 70.91  ?  21   VAL A CB  1 
ATOM   157   C  CG1 . VAL A 1  21   ? -52.781 -31.289  77.844  1.00 63.48  ?  21   VAL A CG1 1 
ATOM   158   C  CG2 . VAL A 1  21   ? -54.492 -29.482  77.534  1.00 79.90  ?  21   VAL A CG2 1 
ATOM   159   N  N   . LEU A 1  22   ? -55.184 -33.960  78.341  1.00 84.78  ?  22   LEU A N   1 
ATOM   160   C  CA  . LEU A 1  22   ? -54.898 -35.372  78.576  1.00 78.29  ?  22   LEU A CA  1 
ATOM   161   C  C   . LEU A 1  22   ? -55.435 -36.240  77.447  1.00 85.30  ?  22   LEU A C   1 
ATOM   162   O  O   . LEU A 1  22   ? -54.743 -37.143  76.960  1.00 83.44  ?  22   LEU A O   1 
ATOM   163   C  CB  . LEU A 1  22   ? -55.491 -35.811  79.914  1.00 85.42  ?  22   LEU A CB  1 
ATOM   164   C  CG  . LEU A 1  22   ? -54.748 -35.316  81.151  1.00 94.19  ?  22   LEU A CG  1 
ATOM   165   C  CD1 . LEU A 1  22   ? -55.145 -36.120  82.375  1.00 96.44  ?  22   LEU A CD1 1 
ATOM   166   C  CD2 . LEU A 1  22   ? -53.259 -35.434  80.902  1.00 92.84  ?  22   LEU A CD2 1 
ATOM   167   N  N   . LEU A 1  23   ? -56.675 -35.985  77.022  1.00 81.53  ?  23   LEU A N   1 
ATOM   168   C  CA  . LEU A 1  23   ? -57.260 -36.762  75.935  1.00 77.83  ?  23   LEU A CA  1 
ATOM   169   C  C   . LEU A 1  23   ? -56.456 -36.608  74.651  1.00 80.68  ?  23   LEU A C   1 
ATOM   170   O  O   . LEU A 1  23   ? -56.245 -37.585  73.923  1.00 77.81  ?  23   LEU A O   1 
ATOM   171   C  CB  . LEU A 1  23   ? -58.711 -36.339  75.712  1.00 86.07  ?  23   LEU A CB  1 
ATOM   172   C  CG  . LEU A 1  23   ? -59.704 -36.713  76.814  1.00 88.96  ?  23   LEU A CG  1 
ATOM   173   C  CD1 . LEU A 1  23   ? -61.082 -36.147  76.507  1.00 88.63  ?  23   LEU A CD1 1 
ATOM   174   C  CD2 . LEU A 1  23   ? -59.762 -38.221  76.995  1.00 83.09  ?  23   LEU A CD2 1 
ATOM   175   N  N   . VAL A 1  24   ? -55.997 -35.388  74.357  1.00 108.38 ?  24   VAL A N   1 
ATOM   176   C  CA  . VAL A 1  24   ? -55.173 -35.167  73.171  1.00 103.29 ?  24   VAL A CA  1 
ATOM   177   C  C   . VAL A 1  24   ? -53.892 -35.987  73.256  1.00 100.38 ?  24   VAL A C   1 
ATOM   178   O  O   . VAL A 1  24   ? -53.539 -36.718  72.324  1.00 96.44  ?  24   VAL A O   1 
ATOM   179   C  CB  . VAL A 1  24   ? -54.875 -33.668  72.990  1.00 110.91 ?  24   VAL A CB  1 
ATOM   180   C  CG1 . VAL A 1  24   ? -53.905 -33.458  71.840  1.00 104.43 ?  24   VAL A CG1 1 
ATOM   181   C  CG2 . VAL A 1  24   ? -56.161 -32.901  72.738  1.00 115.48 ?  24   VAL A CG2 1 
ATOM   182   N  N   . VAL A 1  25   ? -53.185 -35.891  74.386  1.00 85.28  ?  25   VAL A N   1 
ATOM   183   C  CA  . VAL A 1  25   ? -51.953 -36.657  74.570  1.00 81.94  ?  25   VAL A CA  1 
ATOM   184   C  C   . VAL A 1  25   ? -52.231 -38.151  74.462  1.00 77.74  ?  25   VAL A C   1 
ATOM   185   O  O   . VAL A 1  25   ? -51.461 -38.899  73.844  1.00 78.73  ?  25   VAL A O   1 
ATOM   186   C  CB  . VAL A 1  25   ? -51.299 -36.296  75.918  1.00 89.90  ?  25   VAL A CB  1 
ATOM   187   C  CG1 . VAL A 1  25   ? -50.263 -37.337  76.309  1.00 89.51  ?  25   VAL A CG1 1 
ATOM   188   C  CG2 . VAL A 1  25   ? -50.670 -34.910  75.848  1.00 85.84  ?  25   VAL A CG2 1 
ATOM   189   N  N   . GLU A 1  26   ? -53.341 -38.607  75.047  1.00 101.38 ?  26   GLU A N   1 
ATOM   190   C  CA  . GLU A 1  26   ? -53.697 -40.020  74.961  1.00 106.22 ?  26   GLU A CA  1 
ATOM   191   C  C   . GLU A 1  26   ? -53.943 -40.439  73.517  1.00 103.97 ?  26   GLU A C   1 
ATOM   192   O  O   . GLU A 1  26   ? -53.649 -41.579  73.135  1.00 107.00 ?  26   GLU A O   1 
ATOM   193   C  CB  . GLU A 1  26   ? -54.931 -40.300  75.821  1.00 111.52 ?  26   GLU A CB  1 
ATOM   194   C  CG  . GLU A 1  26   ? -55.359 -41.762  75.870  1.00 104.87 ?  26   GLU A CG  1 
ATOM   195   C  CD  . GLU A 1  26   ? -54.340 -42.648  76.565  1.00 111.53 ?  26   GLU A CD  1 
ATOM   196   O  OE1 . GLU A 1  26   ? -53.599 -42.143  77.434  1.00 110.76 ?  26   GLU A OE1 1 
ATOM   197   O  OE2 . GLU A 1  26   ? -54.284 -43.854  76.242  1.00 115.99 -1 26   GLU A OE2 1 
ATOM   198   N  N   . GLY A 1  27   ? -54.478 -39.529  72.700  1.00 79.80  ?  27   GLY A N   1 
ATOM   199   C  CA  . GLY A 1  27   ? -54.728 -39.856  71.305  1.00 74.28  ?  27   GLY A CA  1 
ATOM   200   C  C   . GLY A 1  27   ? -53.453 -40.152  70.538  1.00 65.95  ?  27   GLY A C   1 
ATOM   201   O  O   . GLY A 1  27   ? -53.351 -41.171  69.850  1.00 64.05  ?  27   GLY A O   1 
ATOM   202   N  N   . ILE A 1  28   ? -52.464 -39.259  70.642  1.00 82.51  ?  28   ILE A N   1 
ATOM   203   C  CA  . ILE A 1  28   ? -51.173 -39.497  70.000  1.00 81.43  ?  28   ILE A CA  1 
ATOM   204   C  C   . ILE A 1  28   ? -50.540 -40.777  70.532  1.00 87.70  ?  28   ILE A C   1 
ATOM   205   O  O   . ILE A 1  28   ? -49.928 -41.545  69.779  1.00 98.19  ?  28   ILE A O   1 
ATOM   206   C  CB  . ILE A 1  28   ? -50.242 -38.281  70.187  1.00 86.68  ?  28   ILE A CB  1 
ATOM   207   C  CG1 . ILE A 1  28   ? -50.691 -37.102  69.316  1.00 106.35 ?  28   ILE A CG1 1 
ATOM   208   C  CG2 . ILE A 1  28   ? -48.796 -38.649  69.877  1.00 88.75  ?  28   ILE A CG2 1 
ATOM   209   C  CD1 . ILE A 1  28   ? -51.578 -36.108  70.013  1.00 107.05 ?  28   ILE A CD1 1 
ATOM   210   N  N   . LEU A 1  29   ? -50.690 -41.035  71.834  1.00 69.72  ?  29   LEU A N   1 
ATOM   211   C  CA  . LEU A 1  29   ? -50.125 -42.246  72.421  1.00 70.96  ?  29   LEU A CA  1 
ATOM   212   C  C   . LEU A 1  29   ? -50.723 -43.493  71.784  1.00 63.99  ?  29   LEU A C   1 
ATOM   213   O  O   . LEU A 1  29   ? -49.996 -44.399  71.362  1.00 60.31  ?  29   LEU A O   1 
ATOM   214   C  CB  . LEU A 1  29   ? -50.351 -42.246  73.935  1.00 73.35  ?  29   LEU A CB  1 
ATOM   215   C  CG  . LEU A 1  29   ? -49.539 -43.236  74.772  1.00 71.05  ?  29   LEU A CG  1 
ATOM   216   C  CD1 . LEU A 1  29   ? -49.175 -42.621  76.111  1.00 97.45  ?  29   LEU A CD1 1 
ATOM   217   C  CD2 . LEU A 1  29   ? -50.302 -44.536  74.978  1.00 70.26  ?  29   LEU A CD2 1 
ATOM   218   N  N   . ILE A 1  30   ? -52.054 -43.546  71.692  1.00 62.42  ?  30   ILE A N   1 
ATOM   219   C  CA  . ILE A 1  30   ? -52.723 -44.697  71.093  1.00 61.46  ?  30   ILE A CA  1 
ATOM   220   C  C   . ILE A 1  30   ? -52.262 -44.893  69.654  1.00 61.05  ?  30   ILE A C   1 
ATOM   221   O  O   . ILE A 1  30   ? -52.042 -46.024  69.204  1.00 65.72  ?  30   ILE A O   1 
ATOM   222   C  CB  . ILE A 1  30   ? -54.251 -44.524  71.178  1.00 64.06  ?  30   ILE A CB  1 
ATOM   223   C  CG1 . ILE A 1  30   ? -54.727 -44.691  72.622  1.00 71.07  ?  30   ILE A CG1 1 
ATOM   224   C  CG2 . ILE A 1  30   ? -54.957 -45.515  70.265  1.00 63.28  ?  30   ILE A CG2 1 
ATOM   225   C  CD1 . ILE A 1  30   ? -56.233 -44.694  72.772  1.00 73.60  ?  30   ILE A CD1 1 
ATOM   226   N  N   . LEU A 1  31   ? -52.096 -43.793  68.917  1.00 71.41  ?  31   LEU A N   1 
ATOM   227   C  CA  . LEU A 1  31   ? -51.679 -43.883  67.520  1.00 68.84  ?  31   LEU A CA  1 
ATOM   228   C  C   . LEU A 1  31   ? -50.304 -44.529  67.395  1.00 63.84  ?  31   LEU A C   1 
ATOM   229   O  O   . LEU A 1  31   ? -50.105 -45.440  66.584  1.00 63.42  ?  31   LEU A O   1 
ATOM   230   C  CB  . LEU A 1  31   ? -51.683 -42.490  66.888  1.00 61.20  ?  31   LEU A CB  1 
ATOM   231   C  CG  . LEU A 1  31   ? -51.547 -42.424  65.367  1.00 63.01  ?  31   LEU A CG  1 
ATOM   232   C  CD1 . LEU A 1  31   ? -52.672 -43.195  64.694  1.00 60.71  ?  31   LEU A CD1 1 
ATOM   233   C  CD2 . LEU A 1  31   ? -51.526 -40.977  64.899  1.00 56.72  ?  31   LEU A CD2 1 
ATOM   234   N  N   . GLY A 1  32   ? -49.342 -44.072  68.199  1.00 62.98  ?  32   GLY A N   1 
ATOM   235   C  CA  . GLY A 1  32   ? -48.001 -44.626  68.115  1.00 60.59  ?  32   GLY A CA  1 
ATOM   236   C  C   . GLY A 1  32   ? -47.927 -46.067  68.581  1.00 67.69  ?  32   GLY A C   1 
ATOM   237   O  O   . GLY A 1  32   ? -47.160 -46.866  68.036  1.00 72.08  ?  32   GLY A O   1 
ATOM   238   N  N   . VAL A 1  33   ? -48.720 -46.420  69.596  1.00 83.71  ?  33   VAL A N   1 
ATOM   239   C  CA  . VAL A 1  33   ? -48.718 -47.792  70.099  1.00 79.10  ?  33   VAL A CA  1 
ATOM   240   C  C   . VAL A 1  33   ? -49.231 -48.751  69.031  1.00 82.45  ?  33   VAL A C   1 
ATOM   241   O  O   . VAL A 1  33   ? -48.736 -49.877  68.896  1.00 80.17  ?  33   VAL A O   1 
ATOM   242   C  CB  . VAL A 1  33   ? -49.545 -47.889  71.395  1.00 84.38  ?  33   VAL A CB  1 
ATOM   243   C  CG1 . VAL A 1  33   ? -49.684 -49.336  71.833  1.00 86.39  ?  33   VAL A CG1 1 
ATOM   244   C  CG2 . VAL A 1  33   ? -48.897 -47.077  72.497  1.00 88.63  ?  33   VAL A CG2 1 
ATOM   245   N  N   . TYR A 1  34   ? -50.220 -48.317  68.243  1.00 72.50  ?  34   TYR A N   1 
ATOM   246   C  CA  . TYR A 1  34   ? -50.777 -49.193  67.217  1.00 67.70  ?  34   TYR A CA  1 
ATOM   247   C  C   . TYR A 1  34   ? -49.763 -49.477  66.114  1.00 72.49  ?  34   TYR A C   1 
ATOM   248   O  O   . TYR A 1  34   ? -49.618 -50.625  65.679  1.00 70.57  ?  34   TYR A O   1 
ATOM   249   C  CB  . TYR A 1  34   ? -52.047 -48.580  66.630  1.00 73.66  ?  34   TYR A CB  1 
ATOM   250   C  CG  . TYR A 1  34   ? -52.709 -49.472  65.609  1.00 81.34  ?  34   TYR A CG  1 
ATOM   251   C  CD1 . TYR A 1  34   ? -53.317 -50.660  65.991  1.00 81.30  ?  34   TYR A CD1 1 
ATOM   252   C  CD2 . TYR A 1  34   ? -52.713 -49.137  64.262  1.00 76.86  ?  34   TYR A CD2 1 
ATOM   253   C  CE1 . TYR A 1  34   ? -53.920 -51.487  65.060  1.00 74.02  ?  34   TYR A CE1 1 
ATOM   254   C  CE2 . TYR A 1  34   ? -53.313 -49.956  63.323  1.00 79.65  ?  34   TYR A CE2 1 
ATOM   255   C  CZ  . TYR A 1  34   ? -53.916 -51.131  63.728  1.00 74.89  ?  34   TYR A CZ  1 
ATOM   256   O  OH  . TYR A 1  34   ? -54.514 -51.949  62.796  1.00 83.96  ?  34   TYR A OH  1 
ATOM   257   N  N   . PHE A 1  35   ? -49.049 -48.451  65.656  1.00 87.16  ?  35   PHE A N   1 
ATOM   258   C  CA  . PHE A 1  35   ? -48.100 -48.611  64.561  1.00 80.65  ?  35   PHE A CA  1 
ATOM   259   C  C   . PHE A 1  35   ? -46.796 -49.271  64.988  1.00 82.26  ?  35   PHE A C   1 
ATOM   260   O  O   . PHE A 1  35   ? -45.913 -49.461  64.145  1.00 87.38  ?  35   PHE A O   1 
ATOM   261   C  CB  . PHE A 1  35   ? -47.807 -47.252  63.918  1.00 80.53  ?  35   PHE A CB  1 
ATOM   262   C  CG  . PHE A 1  35   ? -48.827 -46.835  62.896  1.00 83.14  ?  35   PHE A CG  1 
ATOM   263   C  CD1 . PHE A 1  35   ? -50.110 -46.487  63.281  1.00 84.71  ?  35   PHE A CD1 1 
ATOM   264   C  CD2 . PHE A 1  35   ? -48.503 -46.798  61.549  1.00 91.63  ?  35   PHE A CD2 1 
ATOM   265   C  CE1 . PHE A 1  35   ? -51.051 -46.105  62.345  1.00 92.74  ?  35   PHE A CE1 1 
ATOM   266   C  CE2 . PHE A 1  35   ? -49.440 -46.417  60.607  1.00 86.24  ?  35   PHE A CE2 1 
ATOM   267   C  CZ  . PHE A 1  35   ? -50.716 -46.070  61.006  1.00 88.03  ?  35   PHE A CZ  1 
ATOM   268   N  N   . ARG A 1  36   ? -46.651 -49.624  66.267  1.00 65.82  ?  36   ARG A N   1 
ATOM   269   C  CA  . ARG A 1  36   ? -45.463 -50.311  66.757  1.00 63.53  ?  36   ARG A CA  1 
ATOM   270   C  C   . ARG A 1  36   ? -45.809 -51.611  67.472  1.00 64.22  ?  36   ARG A C   1 
ATOM   271   O  O   . ARG A 1  36   ? -44.911 -52.259  68.025  1.00 64.84  ?  36   ARG A O   1 
ATOM   272   C  CB  . ARG A 1  36   ? -44.662 -49.399  67.692  1.00 66.64  ?  36   ARG A CB  1 
ATOM   273   C  CG  . ARG A 1  36   ? -44.047 -48.198  67.002  1.00 67.33  ?  36   ARG A CG  1 
ATOM   274   C  CD  . ARG A 1  36   ? -43.793 -47.072  67.986  1.00 65.51  ?  36   ARG A CD  1 
ATOM   275   N  NE  . ARG A 1  36   ? -42.906 -46.058  67.430  1.00 62.76  ?  36   ARG A NE  1 
ATOM   276   C  CZ  . ARG A 1  36   ? -43.303 -45.078  66.629  1.00 66.98  ?  36   ARG A CZ  1 
ATOM   277   N  NH1 . ARG A 1  36   ? -44.568 -44.957  66.262  1.00 62.28  ?  36   ARG A NH1 1 
ATOM   278   N  NH2 . ARG A 1  36   ? -42.407 -44.200  66.185  1.00 63.50  ?  36   ARG A NH2 1 
ATOM   279   N  N   . SER A 1  37   ? -47.078 -52.007  67.471  1.00 62.94  ?  37   SER A N   1 
ATOM   280   C  CA  . SER A 1  37   ? -47.517 -53.186  68.199  1.00 67.43  ?  37   SER A CA  1 
ATOM   281   C  C   . SER A 1  37   ? -47.035 -54.460  67.509  1.00 67.74  ?  37   SER A C   1 
ATOM   282   O  O   . SER A 1  37   ? -46.586 -54.454  66.359  1.00 73.41  ?  37   SER A O   1 
ATOM   283   C  CB  . SER A 1  37   ? -49.040 -53.200  68.319  1.00 70.49  ?  37   SER A CB  1 
ATOM   284   O  OG  . SER A 1  37   ? -49.642 -53.517  67.075  1.00 66.43  ?  37   SER A OG  1 
ATOM   285   N  N   . ASN A 1  38   ? -47.137 -55.573  68.237  1.00 86.52  ?  38   ASN A N   1 
ATOM   286   C  CA  . ASN A 1  38   ? -46.804 -56.880  67.689  1.00 85.43  ?  38   ASN A CA  1 
ATOM   287   C  C   . ASN A 1  38   ? -47.923 -57.469  66.844  1.00 87.07  ?  38   ASN A C   1 
ATOM   288   O  O   . ASN A 1  38   ? -47.690 -58.454  66.135  1.00 80.72  ?  38   ASN A O   1 
ATOM   289   C  CB  . ASN A 1  38   ? -46.451 -57.850  68.818  1.00 82.55  ?  38   ASN A CB  1 
ATOM   290   C  CG  . ASN A 1  38   ? -45.111 -57.544  69.445  1.00 87.73  ?  38   ASN A CG  1 
ATOM   291   O  OD1 . ASN A 1  38   ? -44.429 -56.599  69.048  1.00 93.42  ?  38   ASN A OD1 1 
ATOM   292   N  ND2 . ASN A 1  38   ? -44.723 -58.342  70.433  1.00 89.53  ?  38   ASN A ND2 1 
ATOM   293   N  N   . TYR A 1  39   ? -49.128 -56.901  66.908  1.00 76.04  ?  39   TYR A N   1 
ATOM   294   C  CA  . TYR A 1  39   ? -50.206 -57.350  66.035  1.00 75.73  ?  39   TYR A CA  1 
ATOM   295   C  C   . TYR A 1  39   ? -50.137 -56.664  64.677  1.00 76.74  ?  39   TYR A C   1 
ATOM   296   O  O   . TYR A 1  39   ? -50.364 -57.302  63.643  1.00 75.65  ?  39   TYR A O   1 
ATOM   297   C  CB  . TYR A 1  39   ? -51.560 -57.095  66.698  1.00 76.68  ?  39   TYR A CB  1 
ATOM   298   C  CG  . TYR A 1  39   ? -52.726 -57.082  65.735  1.00 75.97  ?  39   TYR A CG  1 
ATOM   299   C  CD1 . TYR A 1  39   ? -53.274 -58.268  65.263  1.00 77.08  ?  39   TYR A CD1 1 
ATOM   300   C  CD2 . TYR A 1  39   ? -53.285 -55.885  65.306  1.00 78.69  ?  39   TYR A CD2 1 
ATOM   301   C  CE1 . TYR A 1  39   ? -54.342 -58.261  64.383  1.00 86.99  ?  39   TYR A CE1 1 
ATOM   302   C  CE2 . TYR A 1  39   ? -54.353 -55.869  64.427  1.00 86.72  ?  39   TYR A CE2 1 
ATOM   303   C  CZ  . TYR A 1  39   ? -54.877 -57.059  63.969  1.00 94.34  ?  39   TYR A CZ  1 
ATOM   304   O  OH  . TYR A 1  39   ? -55.940 -57.047  63.094  1.00 97.83  ?  39   TYR A OH  1 
ATOM   305   N  N   . PHE A 1  40   ? -49.823 -55.366  64.662  1.00 86.04  ?  40   PHE A N   1 
ATOM   306   C  CA  . PHE A 1  40   ? -49.702 -54.645  63.400  1.00 87.82  ?  40   PHE A CA  1 
ATOM   307   C  C   . PHE A 1  40   ? -48.505 -55.135  62.595  1.00 84.92  ?  40   PHE A C   1 
ATOM   308   O  O   . PHE A 1  40   ? -48.600 -55.315  61.376  1.00 83.63  ?  40   PHE A O   1 
ATOM   309   C  CB  . PHE A 1  40   ? -49.591 -53.144  63.665  1.00 82.69  ?  40   PHE A CB  1 
ATOM   310   C  CG  . PHE A 1  40   ? -49.631 -52.304  62.423  1.00 86.84  ?  40   PHE A CG  1 
ATOM   311   C  CD1 . PHE A 1  40   ? -50.723 -52.351  61.572  1.00 89.79  ?  40   PHE A CD1 1 
ATOM   312   C  CD2 . PHE A 1  40   ? -48.576 -51.464  62.106  1.00 87.78  ?  40   PHE A CD2 1 
ATOM   313   C  CE1 . PHE A 1  40   ? -50.762 -51.575  60.428  1.00 89.36  ?  40   PHE A CE1 1 
ATOM   314   C  CE2 . PHE A 1  40   ? -48.608 -50.687  60.965  1.00 83.55  ?  40   PHE A CE2 1 
ATOM   315   C  CZ  . PHE A 1  40   ? -49.702 -50.742  60.124  1.00 85.02  ?  40   PHE A CZ  1 
ATOM   316   N  N   . ARG A 1  41   ? -47.373 -55.354  63.257  1.00 64.85  ?  41   ARG A N   1 
ATOM   317   C  CA  . ARG A 1  41   ? -46.166 -55.827  62.596  1.00 59.69  ?  41   ARG A CA  1 
ATOM   318   C  C   . ARG A 1  41   ? -46.068 -57.346  62.553  1.00 65.80  ?  41   ARG A C   1 
ATOM   319   O  O   . ARG A 1  41   ? -45.104 -57.870  61.984  1.00 72.89  ?  41   ARG A O   1 
ATOM   320   C  CB  . ARG A 1  41   ? -44.927 -55.248  63.286  1.00 52.99  ?  41   ARG A CB  1 
ATOM   321   C  CG  . ARG A 1  41   ? -44.907 -53.729  63.356  1.00 56.06  ?  41   ARG A CG  1 
ATOM   322   C  CD  . ARG A 1  41   ? -45.130 -53.109  61.982  1.00 68.13  ?  41   ARG A CD  1 
ATOM   323   N  NE  . ARG A 1  41   ? -44.123 -53.528  61.014  1.00 65.46  ?  41   ARG A NE  1 
ATOM   324   C  CZ  . ARG A 1  41   ? -43.343 -52.699  60.333  1.00 61.04  ?  41   ARG A CZ  1 
ATOM   325   N  NH1 . ARG A 1  41   ? -43.426 -51.387  60.489  1.00 64.86  ?  41   ARG A NH1 1 
ATOM   326   N  NH2 . ARG A 1  41   ? -42.459 -53.197  59.474  1.00 64.32  ?  41   ARG A NH2 1 
ATOM   327   N  N   . GLN A 1  42   ? -47.038 -58.057  63.134  1.00 76.79  ?  42   GLN A N   1 
ATOM   328   C  CA  . GLN A 1  42   ? -47.056 -59.521  63.155  1.00 86.33  ?  42   GLN A CA  1 
ATOM   329   C  C   . GLN A 1  42   ? -45.772 -60.080  63.771  1.00 79.54  ?  42   GLN A C   1 
ATOM   330   O  O   . GLN A 1  42   ? -45.104 -60.947  63.203  1.00 76.96  ?  42   GLN A O   1 
ATOM   331   C  CB  . GLN A 1  42   ? -47.291 -60.090  61.752  1.00 80.70  ?  42   GLN A CB  1 
ATOM   332   C  CG  . GLN A 1  42   ? -48.694 -59.845  61.217  1.00 81.73  ?  42   GLN A CG  1 
ATOM   333   C  CD  . GLN A 1  42   ? -49.772 -60.441  62.105  1.00 89.08  ?  42   GLN A CD  1 
ATOM   334   O  OE1 . GLN A 1  42   ? -50.781 -59.798  62.393  1.00 86.45  ?  42   GLN A OE1 1 
ATOM   335   N  NE2 . GLN A 1  42   ? -49.565 -61.679  62.538  1.00 85.40  ?  42   GLN A NE2 1 
ATOM   336   N  N   . VAL A 1  43   ? -45.433 -59.569  64.951  1.00 73.16  ?  43   VAL A N   1 
ATOM   337   C  CA  . VAL A 1  43   ? -44.246 -59.983  65.691  1.00 74.08  ?  43   VAL A CA  1 
ATOM   338   C  C   . VAL A 1  43   ? -44.667 -60.958  66.780  1.00 72.82  ?  43   VAL A C   1 
ATOM   339   O  O   . VAL A 1  43   ? -45.703 -60.768  67.432  1.00 76.90  ?  43   VAL A O   1 
ATOM   340   C  CB  . VAL A 1  43   ? -43.511 -58.765  66.285  1.00 75.77  ?  43   VAL A CB  1 
ATOM   341   C  CG1 . VAL A 1  43   ? -42.364 -59.206  67.187  1.00 68.32  ?  43   VAL A CG1 1 
ATOM   342   C  CG2 . VAL A 1  43   ? -43.005 -57.861  65.173  1.00 72.26  ?  43   VAL A CG2 1 
ATOM   343   N  N   . ASN A 1  44   ? -43.869 -62.011  66.971  1.00 67.05  ?  44   ASN A N   1 
ATOM   344   C  CA  . ASN A 1  44   ? -44.131 -63.070  67.945  1.00 70.27  ?  44   ASN A CA  1 
ATOM   345   C  C   . ASN A 1  44   ? -45.440 -63.801  67.669  1.00 71.62  ?  44   ASN A C   1 
ATOM   346   O  O   . ASN A 1  44   ? -46.021 -64.408  68.575  1.00 73.81  ?  44   ASN A O   1 
ATOM   347   C  CB  . ASN A 1  44   ? -44.120 -62.530  69.380  1.00 73.71  ?  44   ASN A CB  1 
ATOM   348   C  CG  . ASN A 1  44   ? -42.738 -62.102  69.830  1.00 78.54  ?  44   ASN A CG  1 
ATOM   349   O  OD1 . ASN A 1  44   ? -41.731 -62.492  69.238  1.00 71.71  ?  44   ASN A OD1 1 
ATOM   350   N  ND2 . ASN A 1  44   ? -42.681 -61.292  70.881  1.00 82.18  ?  44   ASN A ND2 1 
ATOM   351   N  N   . VAL A 1  45   ? -45.915 -63.757  66.428  1.00 93.94  ?  45   VAL A N   1 
ATOM   352   C  CA  . VAL A 1  45   ? -47.117 -64.467  66.013  1.00 94.41  ?  45   VAL A CA  1 
ATOM   353   C  C   . VAL A 1  45   ? -46.684 -65.696  65.228  1.00 97.66  ?  45   VAL A C   1 
ATOM   354   O  O   . VAL A 1  45   ? -45.954 -65.583  64.236  1.00 103.17 ?  45   VAL A O   1 
ATOM   355   C  CB  . VAL A 1  45   ? -48.039 -63.570  65.173  1.00 90.42  ?  45   VAL A CB  1 
ATOM   356   C  CG1 . VAL A 1  45   ? -49.301 -64.324  64.783  1.00 91.78  ?  45   VAL A CG1 1 
ATOM   357   C  CG2 . VAL A 1  45   ? -48.381 -62.299  65.934  1.00 85.38  ?  45   VAL A CG2 1 
ATOM   358   N  N   . ALA A 1  46   ? -47.123 -66.870  65.672  1.00 70.75  ?  46   ALA A N   1 
ATOM   359   C  CA  . ALA A 1  46   ? -46.772 -68.124  65.012  1.00 72.41  ?  46   ALA A CA  1 
ATOM   360   C  C   . ALA A 1  46   ? -47.714 -68.330  63.833  1.00 80.11  ?  46   ALA A C   1 
ATOM   361   O  O   . ALA A 1  46   ? -48.839 -68.806  63.998  1.00 82.32  ?  46   ALA A O   1 
ATOM   362   C  CB  . ALA A 1  46   ? -46.845 -69.286  65.994  1.00 70.40  ?  46   ALA A CB  1 
ATOM   363   N  N   . ILE A 1  47   ? -47.255 -67.966  62.635  1.00 73.42  ?  47   ILE A N   1 
ATOM   364   C  CA  . ILE A 1  47   ? -48.077 -68.109  61.440  1.00 80.53  ?  47   ILE A CA  1 
ATOM   365   C  C   . ILE A 1  47   ? -48.250 -69.586  61.115  1.00 82.66  ?  47   ILE A C   1 
ATOM   366   O  O   . ILE A 1  47   ? -47.272 -70.342  61.037  1.00 71.82  ?  47   ILE A O   1 
ATOM   367   C  CB  . ILE A 1  47   ? -47.457 -67.349  60.258  1.00 87.06  ?  47   ILE A CB  1 
ATOM   368   C  CG1 . ILE A 1  47   ? -47.457 -65.839  60.517  1.00 75.62  ?  47   ILE A CG1 1 
ATOM   369   C  CG2 . ILE A 1  47   ? -48.201 -67.671  58.972  1.00 93.79  ?  47   ILE A CG2 1 
ATOM   370   C  CD1 . ILE A 1  47   ? -46.159 -65.308  61.084  1.00 71.63  ?  47   ILE A CD1 1 
ATOM   371   N  N   . GLU A 1  48   ? -49.499 -70.003  60.919  1.00 98.46  ?  48   GLU A N   1 
ATOM   372   C  CA  . GLU A 1  48   ? -49.801 -71.396  60.617  1.00 103.22 ?  48   GLU A CA  1 
ATOM   373   C  C   . GLU A 1  48   ? -49.429 -71.718  59.175  1.00 101.56 ?  48   GLU A C   1 
ATOM   374   O  O   . GLU A 1  48   ? -49.785 -70.980  58.250  1.00 95.66  ?  48   GLU A O   1 
ATOM   375   C  CB  . GLU A 1  48   ? -51.283 -71.684  60.859  1.00 105.31 ?  48   GLU A CB  1 
ATOM   376   C  CG  . GLU A 1  48   ? -51.669 -73.141  60.666  1.00 112.92 ?  48   GLU A CG  1 
ATOM   377   C  CD  . GLU A 1  48   ? -53.124 -73.408  61.002  1.00 122.33 ?  48   GLU A CD  1 
ATOM   378   O  OE1 . GLU A 1  48   ? -53.840 -72.448  61.358  1.00 124.10 ?  48   GLU A OE1 1 
ATOM   379   O  OE2 . GLU A 1  48   ? -53.550 -74.579  60.912  1.00 123.58 -1 48   GLU A OE2 1 
ATOM   380   N  N   . GLN A 1  49   ? -48.709 -72.836  58.986  1.00 81.42  ?  49   GLN A N   1 
ATOM   381   C  CA  . GLN A 1  49   ? -48.250 -73.297  57.688  1.00 73.50  ?  49   GLN A CA  1 
ATOM   382   C  C   . GLN A 1  49   ? -49.163 -74.395  57.156  1.00 80.69  ?  49   GLN A C   1 
ATOM   383   O  O   . GLN A 1  49   ? -49.820 -75.094  57.933  1.00 89.25  ?  49   GLN A O   1 
ATOM   384   C  CB  . GLN A 1  49   ? -46.815 -73.825  57.783  1.00 77.36  ?  49   GLN A CB  1 
ATOM   385   C  CG  . GLN A 1  49   ? -45.798 -72.778  58.202  1.00 68.76  ?  49   GLN A CG  1 
ATOM   386   C  CD  . GLN A 1  49   ? -45.646 -71.668  57.182  1.00 62.61  ?  49   GLN A CD  1 
ATOM   387   O  OE1 . GLN A 1  49   ? -45.940 -71.847  56.001  1.00 69.45  ?  49   GLN A OE1 1 
ATOM   388   N  NE2 . GLN A 1  49   ? -45.178 -70.511  57.634  1.00 66.28  ?  49   GLN A NE2 1 
ATOM   389   N  N   . PRO A 1  50   ? -49.232 -74.567  55.833  1.00 83.37  ?  50   PRO A N   1 
ATOM   390   C  CA  . PRO A 1  50   ? -50.150 -75.578  55.282  1.00 81.19  ?  50   PRO A CA  1 
ATOM   391   C  C   . PRO A 1  50   ? -49.747 -77.009  55.591  1.00 86.13  ?  50   PRO A C   1 
ATOM   392   O  O   . PRO A 1  50   ? -50.621 -77.883  55.645  1.00 90.74  ?  50   PRO A O   1 
ATOM   393   C  CB  . PRO A 1  50   ? -50.116 -75.298  53.772  1.00 76.41  ?  50   PRO A CB  1 
ATOM   394   C  CG  . PRO A 1  50   ? -48.820 -74.590  53.549  1.00 80.45  ?  50   PRO A CG  1 
ATOM   395   C  CD  . PRO A 1  50   ? -48.604 -73.758  54.775  1.00 81.97  ?  50   PRO A CD  1 
ATOM   396   N  N   . VAL A 1  51   ? -48.459 -77.284  55.792  1.00 98.67  ?  51   VAL A N   1 
ATOM   397   C  CA  . VAL A 1  51   ? -47.981 -78.640  56.040  1.00 97.93  ?  51   VAL A CA  1 
ATOM   398   C  C   . VAL A 1  51   ? -47.550 -78.854  57.480  1.00 102.95 ?  51   VAL A C   1 
ATOM   399   O  O   . VAL A 1  51   ? -47.188 -79.984  57.842  1.00 103.88 ?  51   VAL A O   1 
ATOM   400   C  CB  . VAL A 1  51   ? -46.837 -79.019  55.081  1.00 102.22 ?  51   VAL A CB  1 
ATOM   401   C  CG1 . VAL A 1  51   ? -47.306 -78.938  53.637  1.00 111.56 ?  51   VAL A CG1 1 
ATOM   402   C  CG2 . VAL A 1  51   ? -45.632 -78.121  55.311  1.00 107.06 ?  51   VAL A CG2 1 
ATOM   403   N  N   . ALA A 1  52   ? -47.573 -77.811  58.312  1.00 69.83  ?  52   ALA A N   1 
ATOM   404   C  CA  . ALA A 1  52   ? -47.211 -77.893  59.728  1.00 70.63  ?  52   ALA A CA  1 
ATOM   405   C  C   . ALA A 1  52   ? -45.800 -78.466  59.898  1.00 63.53  ?  52   ALA A C   1 
ATOM   406   O  O   . ALA A 1  52   ? -45.589 -79.569  60.407  1.00 57.14  ?  52   ALA A O   1 
ATOM   407   C  CB  . ALA A 1  52   ? -48.243 -78.714  60.512  1.00 61.33  ?  52   ALA A CB  1 
ATOM   408   N  N   . PHE A 1  53   ? -44.832 -77.673  59.449  1.00 97.30  ?  53   PHE A N   1 
ATOM   409   C  CA  . PHE A 1  53   ? -43.427 -78.039  59.545  1.00 90.06  ?  53   PHE A CA  1 
ATOM   410   C  C   . PHE A 1  53   ? -42.848 -77.533  60.859  1.00 88.05  ?  53   PHE A C   1 
ATOM   411   O  O   . PHE A 1  53   ? -43.034 -76.367  61.220  1.00 84.00  ?  53   PHE A O   1 
ATOM   412   C  CB  . PHE A 1  53   ? -42.634 -77.471  58.369  1.00 87.57  ?  53   PHE A CB  1 
ATOM   413   C  CG  . PHE A 1  53   ? -41.172 -77.788  58.426  1.00 84.90  ?  53   PHE A CG  1 
ATOM   414   C  CD1 . PHE A 1  53   ? -40.714 -79.060  58.129  1.00 81.67  ?  53   PHE A CD1 1 
ATOM   415   C  CD2 . PHE A 1  53   ? -40.255 -76.818  58.795  1.00 85.96  ?  53   PHE A CD2 1 
ATOM   416   C  CE1 . PHE A 1  53   ? -39.367 -79.355  58.188  1.00 82.80  ?  53   PHE A CE1 1 
ATOM   417   C  CE2 . PHE A 1  53   ? -38.908 -77.109  58.857  1.00 86.10  ?  53   PHE A CE2 1 
ATOM   418   C  CZ  . PHE A 1  53   ? -38.465 -78.379  58.556  1.00 82.66  ?  53   PHE A CZ  1 
ATOM   419   N  N   . SER A 1  54   ? -42.139 -78.410  61.564  1.00 80.17  ?  54   SER A N   1 
ATOM   420   C  CA  . SER A 1  54   ? -41.553 -78.098  62.862  1.00 84.64  ?  54   SER A CA  1 
ATOM   421   C  C   . SER A 1  54   ? -40.039 -78.026  62.710  1.00 79.27  ?  54   SER A C   1 
ATOM   422   O  O   . SER A 1  54   ? -39.383 -79.049  62.484  1.00 76.47  ?  54   SER A O   1 
ATOM   423   C  CB  . SER A 1  54   ? -41.952 -79.142  63.903  1.00 94.00  ?  54   SER A CB  1 
ATOM   424   O  OG  . SER A 1  54   ? -41.050 -79.144  64.996  1.00 87.84  ?  54   SER A OG  1 
ATOM   425   N  N   . HIS A 1  55   ? -39.487 -76.817  62.835  1.00 66.09  ?  55   HIS A N   1 
ATOM   426   C  CA  . HIS A 1  55   ? -38.036 -76.665  62.808  1.00 68.45  ?  55   HIS A CA  1 
ATOM   427   C  C   . HIS A 1  55   ? -37.386 -77.290  64.036  1.00 66.57  ?  55   HIS A C   1 
ATOM   428   O  O   . HIS A 1  55   ? -36.237 -77.742  63.964  1.00 62.33  ?  55   HIS A O   1 
ATOM   429   C  CB  . HIS A 1  55   ? -37.660 -75.185  62.710  1.00 70.11  ?  55   HIS A CB  1 
ATOM   430   C  CG  . HIS A 1  55   ? -37.609 -74.661  61.308  1.00 63.09  ?  55   HIS A CG  1 
ATOM   431   N  ND1 . HIS A 1  55   ? -38.734 -74.255  60.623  1.00 64.26  ?  55   HIS A ND1 1 
ATOM   432   C  CD2 . HIS A 1  55   ? -36.565 -74.465  60.466  1.00 75.25  ?  55   HIS A CD2 1 
ATOM   433   C  CE1 . HIS A 1  55   ? -38.387 -73.835  59.419  1.00 77.28  ?  55   HIS A CE1 1 
ATOM   434   N  NE2 . HIS A 1  55   ? -37.076 -73.952  59.298  1.00 75.10  ?  55   HIS A NE2 1 
ATOM   435   N  N   . GLN A 1  56   ? -38.099 -77.326  65.164  1.00 86.89  ?  56   GLN A N   1 
ATOM   436   C  CA  . GLN A 1  56   ? -37.539 -77.910  66.379  1.00 86.67  ?  56   GLN A CA  1 
ATOM   437   C  C   . GLN A 1  56   ? -37.289 -79.403  66.213  1.00 83.08  ?  56   GLN A C   1 
ATOM   438   O  O   . GLN A 1  56   ? -36.304 -79.939  66.735  1.00 76.99  ?  56   GLN A O   1 
ATOM   439   C  CB  . GLN A 1  56   ? -38.474 -77.656  67.560  1.00 76.34  ?  56   GLN A CB  1 
ATOM   440   C  CG  . GLN A 1  56   ? -37.903 -78.076  68.899  1.00 82.11  ?  56   GLN A CG  1 
ATOM   441   C  CD  . GLN A 1  56   ? -38.896 -77.907  70.029  1.00 92.93  ?  56   GLN A CD  1 
ATOM   442   O  OE1 . GLN A 1  56   ? -40.019 -78.405  69.961  1.00 89.72  ?  56   GLN A OE1 1 
ATOM   443   N  NE2 . GLN A 1  56   ? -38.486 -77.200  71.077  1.00 100.70 ?  56   GLN A NE2 1 
ATOM   444   N  N   . LEU A 1  57   ? -38.174 -80.092  65.491  1.00 70.39  ?  57   LEU A N   1 
ATOM   445   C  CA  . LEU A 1  57   ? -38.009 -81.527  65.292  1.00 70.15  ?  57   LEU A CA  1 
ATOM   446   C  C   . LEU A 1  57   ? -36.896 -81.823  64.297  1.00 75.77  ?  57   LEU A C   1 
ATOM   447   O  O   . LEU A 1  57   ? -36.152 -82.797  64.461  1.00 78.42  ?  57   LEU A O   1 
ATOM   448   C  CB  . LEU A 1  57   ? -39.326 -82.144  64.822  1.00 66.64  ?  57   LEU A CB  1 
ATOM   449   C  CG  . LEU A 1  57   ? -39.339 -83.653  64.571  1.00 63.34  ?  57   LEU A CG  1 
ATOM   450   C  CD1 . LEU A 1  57   ? -38.805 -84.407  65.778  1.00 69.40  ?  57   LEU A CD1 1 
ATOM   451   C  CD2 . LEU A 1  57   ? -40.742 -84.121  64.220  1.00 60.88  ?  57   LEU A CD2 1 
ATOM   452   N  N   . HIS A 1  58   ? -36.759 -80.995  63.263  1.00 63.69  ?  58   HIS A N   1 
ATOM   453   C  CA  . HIS A 1  58   ? -35.818 -81.281  62.190  1.00 58.47  ?  58   HIS A CA  1 
ATOM   454   C  C   . HIS A 1  58   ? -34.414 -80.752  62.448  1.00 62.04  ?  58   HIS A C   1 
ATOM   455   O  O   . HIS A 1  58   ? -33.470 -81.218  61.803  1.00 69.10  ?  58   HIS A O   1 
ATOM   456   C  CB  . HIS A 1  58   ? -36.346 -80.716  60.868  1.00 61.82  ?  58   HIS A CB  1 
ATOM   457   C  CG  . HIS A 1  58   ? -37.500 -81.486  60.304  1.00 65.69  ?  58   HIS A CG  1 
ATOM   458   N  ND1 . HIS A 1  58   ? -38.795 -81.320  60.746  1.00 65.73  ?  58   HIS A ND1 1 
ATOM   459   C  CD2 . HIS A 1  58   ? -37.553 -82.430  59.334  1.00 73.23  ?  58   HIS A CD2 1 
ATOM   460   C  CE1 . HIS A 1  58   ? -39.596 -82.127  60.073  1.00 72.01  ?  58   HIS A CE1 1 
ATOM   461   N  NE2 . HIS A 1  58   ? -38.867 -82.810  59.209  1.00 68.85  ?  58   HIS A NE2 1 
ATOM   462   N  N   . VAL A 1  59   ? -34.241 -79.813  63.372  1.00 92.28  ?  59   VAL A N   1 
ATOM   463   C  CA  . VAL A 1  59   ? -32.936 -79.235  63.670  1.00 90.31  ?  59   VAL A CA  1 
ATOM   464   C  C   . VAL A 1  59   ? -32.402 -79.723  65.014  1.00 99.45  ?  59   VAL A C   1 
ATOM   465   O  O   . VAL A 1  59   ? -31.259 -80.171  65.109  1.00 105.23 ?  59   VAL A O   1 
ATOM   466   C  CB  . VAL A 1  59   ? -32.986 -77.692  63.621  1.00 89.93  ?  59   VAL A CB  1 
ATOM   467   C  CG1 . VAL A 1  59   ? -31.607 -77.114  63.896  1.00 93.30  ?  59   VAL A CG1 1 
ATOM   468   C  CG2 . VAL A 1  59   ? -33.505 -77.221  62.273  1.00 90.96  ?  59   VAL A CG2 1 
ATOM   469   N  N   . ASN A 1  60   ? -33.219 -79.643  66.067  1.00 76.66  ?  60   ASN A N   1 
ATOM   470   C  CA  . ASN A 1  60   ? -32.746 -80.017  67.396  1.00 75.03  ?  60   ASN A CA  1 
ATOM   471   C  C   . ASN A 1  60   ? -32.858 -81.513  67.661  1.00 79.86  ?  60   ASN A C   1 
ATOM   472   O  O   . ASN A 1  60   ? -32.123 -82.041  68.504  1.00 89.50  ?  60   ASN A O   1 
ATOM   473   C  CB  . ASN A 1  60   ? -33.515 -79.251  68.474  1.00 79.87  ?  60   ASN A CB  1 
ATOM   474   C  CG  . ASN A 1  60   ? -33.044 -77.819  68.623  1.00 73.78  ?  60   ASN A CG  1 
ATOM   475   O  OD1 . ASN A 1  60   ? -31.863 -77.518  68.446  1.00 76.26  ?  60   ASN A OD1 1 
ATOM   476   N  ND2 . ASN A 1  60   ? -33.962 -76.931  68.978  1.00 65.28  ?  60   ASN A ND2 1 
ATOM   477   N  N   . VAL A 1  61   ? -33.761 -82.210  66.973  1.00 77.13  ?  61   VAL A N   1 
ATOM   478   C  CA  . VAL A 1  61   ? -33.969 -83.632  67.224  1.00 82.30  ?  61   VAL A CA  1 
ATOM   479   C  C   . VAL A 1  61   ? -33.308 -84.456  66.127  1.00 78.48  ?  61   VAL A C   1 
ATOM   480   O  O   . VAL A 1  61   ? -32.430 -85.282  66.401  1.00 83.10  ?  61   VAL A O   1 
ATOM   481   C  CB  . VAL A 1  61   ? -35.467 -83.965  67.337  1.00 74.68  ?  61   VAL A CB  1 
ATOM   482   C  CG1 . VAL A 1  61   ? -35.666 -85.466  67.480  1.00 84.19  ?  61   VAL A CG1 1 
ATOM   483   C  CG2 . VAL A 1  61   ? -36.087 -83.223  68.509  1.00 81.53  ?  61   VAL A CG2 1 
ATOM   484   N  N   . VAL A 1  62   ? -33.727 -84.242  64.878  1.00 58.75  ?  62   VAL A N   1 
ATOM   485   C  CA  . VAL A 1  62   ? -33.161 -85.006  63.770  1.00 62.84  ?  62   VAL A CA  1 
ATOM   486   C  C   . VAL A 1  62   ? -31.734 -84.551  63.482  1.00 65.21  ?  62   VAL A C   1 
ATOM   487   O  O   . VAL A 1  62   ? -30.843 -85.375  63.242  1.00 68.48  ?  62   VAL A O   1 
ATOM   488   C  CB  . VAL A 1  62   ? -34.061 -84.891  62.527  1.00 58.71  ?  62   VAL A CB  1 
ATOM   489   C  CG1 . VAL A 1  62   ? -33.457 -85.655  61.363  1.00 57.33  ?  62   VAL A CG1 1 
ATOM   490   C  CG2 . VAL A 1  62   ? -35.455 -85.411  62.835  1.00 49.90  ?  62   VAL A CG2 1 
ATOM   491   N  N   . GLY A 1  63   ? -31.492 -83.243  63.506  1.00 49.06  ?  63   GLY A N   1 
ATOM   492   C  CA  . GLY A 1  63   ? -30.148 -82.722  63.349  1.00 52.65  ?  63   GLY A CA  1 
ATOM   493   C  C   . GLY A 1  63   ? -29.766 -82.387  61.922  1.00 45.43  ?  63   GLY A C   1 
ATOM   494   O  O   . GLY A 1  63   ? -28.657 -82.703  61.480  1.00 38.76  ?  63   GLY A O   1 
ATOM   495   N  N   . ILE A 1  64   ? -30.669 -81.741  61.194  1.00 107.29 ?  64   ILE A N   1 
ATOM   496   C  CA  . ILE A 1  64   ? -30.422 -81.347  59.812  1.00 102.24 ?  64   ILE A CA  1 
ATOM   497   C  C   . ILE A 1  64   ? -29.795 -79.960  59.805  1.00 98.51  ?  64   ILE A C   1 
ATOM   498   O  O   . ILE A 1  64   ? -30.250 -79.060  60.522  1.00 106.34 ?  64   ILE A O   1 
ATOM   499   C  CB  . ILE A 1  64   ? -31.724 -81.361  58.996  1.00 93.89  ?  64   ILE A CB  1 
ATOM   500   C  CG1 . ILE A 1  64   ? -32.457 -82.690  59.172  1.00 97.15  ?  64   ILE A CG1 1 
ATOM   501   C  CG2 . ILE A 1  64   ? -31.437 -81.108  57.527  1.00 100.77 ?  64   ILE A CG2 1 
ATOM   502   C  CD1 . ILE A 1  64   ? -33.905 -82.628  58.756  1.00 99.57  ?  64   ILE A CD1 1 
ATOM   503   N  N   . ASP A 1  65   ? -28.755 -79.783  58.995  1.00 70.47  ?  65   ASP A N   1 
ATOM   504   C  CA  . ASP A 1  65   ? -28.135 -78.474  58.855  1.00 71.90  ?  65   ASP A CA  1 
ATOM   505   C  C   . ASP A 1  65   ? -29.058 -77.525  58.094  1.00 72.94  ?  65   ASP A C   1 
ATOM   506   O  O   . ASP A 1  65   ? -29.902 -77.946  57.299  1.00 76.64  ?  65   ASP A O   1 
ATOM   507   C  CB  . ASP A 1  65   ? -26.790 -78.598  58.137  1.00 72.56  ?  65   ASP A CB  1 
ATOM   508   C  CG  . ASP A 1  65   ? -26.026 -77.289  58.094  1.00 71.26  ?  65   ASP A CG  1 
ATOM   509   O  OD1 . ASP A 1  65   ? -25.512 -76.865  59.151  1.00 74.67  ?  65   ASP A OD1 1 
ATOM   510   O  OD2 . ASP A 1  65   ? -25.931 -76.691  57.001  1.00 70.43  -1 65   ASP A OD2 1 
ATOM   511   N  N   . CYS A 1  66   ? -28.895 -76.225  58.357  1.00 70.73  ?  66   CYS A N   1 
ATOM   512   C  CA  . CYS A 1  66   ? -29.729 -75.227  57.694  1.00 69.52  ?  66   CYS A CA  1 
ATOM   513   C  C   . CYS A 1  66   ? -29.439 -75.160  56.200  1.00 74.57  ?  66   CYS A C   1 
ATOM   514   O  O   . CYS A 1  66   ? -30.353 -74.942  55.395  1.00 70.92  ?  66   CYS A O   1 
ATOM   515   C  CB  . CYS A 1  66   ? -29.522 -73.858  58.339  1.00 70.83  ?  66   CYS A CB  1 
ATOM   516   S  SG  . CYS A 1  66   ? -29.685 -73.851  60.135  1.00 71.54  ?  66   CYS A SG  1 
ATOM   517   N  N   . ARG A 1  67   ? -28.175 -75.340  55.808  1.00 78.64  ?  67   ARG A N   1 
ATOM   518   C  CA  . ARG A 1  67   ? -27.814 -75.297  54.397  1.00 68.25  ?  67   ARG A CA  1 
ATOM   519   C  C   . ARG A 1  67   ? -28.298 -76.519  53.629  1.00 71.82  ?  67   ARG A C   1 
ATOM   520   O  O   . ARG A 1  67   ? -28.279 -76.498  52.394  1.00 71.97  ?  67   ARG A O   1 
ATOM   521   C  CB  . ARG A 1  67   ? -26.299 -75.154  54.247  1.00 65.54  ?  67   ARG A CB  1 
ATOM   522   C  CG  . ARG A 1  67   ? -25.777 -73.781  54.630  1.00 66.54  ?  67   ARG A CG  1 
ATOM   523   C  CD  . ARG A 1  67   ? -24.267 -73.785  54.781  1.00 89.91  ?  67   ARG A CD  1 
ATOM   524   N  NE  . ARG A 1  67   ? -23.830 -74.590  55.916  1.00 88.80  ?  67   ARG A NE  1 
ATOM   525   C  CZ  . ARG A 1  67   ? -22.572 -74.683  56.326  1.00 90.07  ?  67   ARG A CZ  1 
ATOM   526   N  NH1 . ARG A 1  67   ? -21.596 -74.029  55.716  1.00 97.20  ?  67   ARG A NH1 1 
ATOM   527   N  NH2 . ARG A 1  67   ? -22.287 -75.449  57.374  1.00 79.66  ?  67   ARG A NH2 1 
ATOM   528   N  N   . TYR A 1  68   ? -28.720 -77.578  54.324  1.00 73.73  ?  68   TYR A N   1 
ATOM   529   C  CA  . TYR A 1  68   ? -29.364 -78.704  53.658  1.00 66.26  ?  68   TYR A CA  1 
ATOM   530   C  C   . TYR A 1  68   ? -30.699 -78.311  53.044  1.00 62.83  ?  68   TYR A C   1 
ATOM   531   O  O   . TYR A 1  68   ? -31.166 -78.980  52.116  1.00 72.39  ?  68   TYR A O   1 
ATOM   532   C  CB  . TYR A 1  68   ? -29.562 -79.854  54.650  1.00 66.30  ?  68   TYR A CB  1 
ATOM   533   C  CG  . TYR A 1  68   ? -30.038 -81.150  54.026  1.00 70.88  ?  68   TYR A CG  1 
ATOM   534   C  CD1 . TYR A 1  68   ? -29.132 -82.096  53.564  1.00 74.43  ?  68   TYR A CD1 1 
ATOM   535   C  CD2 . TYR A 1  68   ? -31.393 -81.435  53.916  1.00 68.73  ?  68   TYR A CD2 1 
ATOM   536   C  CE1 . TYR A 1  68   ? -29.563 -83.282  52.997  1.00 73.84  ?  68   TYR A CE1 1 
ATOM   537   C  CE2 . TYR A 1  68   ? -31.831 -82.615  53.350  1.00 73.67  ?  68   TYR A CE2 1 
ATOM   538   C  CZ  . TYR A 1  68   ? -30.913 -83.535  52.894  1.00 73.76  ?  68   TYR A CZ  1 
ATOM   539   O  OH  . TYR A 1  68   ? -31.352 -84.711  52.333  1.00 73.94  ?  68   TYR A OH  1 
ATOM   540   N  N   . CYS A 1  69   ? -31.311 -77.235  53.530  1.00 74.67  ?  69   CYS A N   1 
ATOM   541   C  CA  . CYS A 1  69   ? -32.630 -76.810  53.084  1.00 78.31  ?  69   CYS A CA  1 
ATOM   542   C  C   . CYS A 1  69   ? -32.611 -75.434  52.442  1.00 77.57  ?  69   CYS A C   1 
ATOM   543   O  O   . CYS A 1  69   ? -33.179 -75.251  51.358  1.00 74.41  ?  69   CYS A O   1 
ATOM   544   C  CB  . CYS A 1  69   ? -33.598 -76.832  54.274  1.00 83.74  ?  69   CYS A CB  1 
ATOM   545   S  SG  . CYS A 1  69   ? -34.082 -78.499  54.752  1.00 84.33  ?  69   CYS A SG  1 
ATOM   546   N  N   . HIS A 1  70   ? -31.973 -74.457  53.080  1.00 57.70  ?  70   HIS A N   1 
ATOM   547   C  CA  . HIS A 1  70   ? -31.798 -73.132  52.492  1.00 59.25  ?  70   HIS A CA  1 
ATOM   548   C  C   . HIS A 1  70   ? -30.401 -73.043  51.877  1.00 64.81  ?  70   HIS A C   1 
ATOM   549   O  O   . HIS A 1  70   ? -29.491 -72.385  52.383  1.00 59.22  ?  70   HIS A O   1 
ATOM   550   C  CB  . HIS A 1  70   ? -32.042 -72.050  53.544  1.00 66.55  ?  70   HIS A CB  1 
ATOM   551   C  CG  . HIS A 1  70   ? -33.256 -72.291  54.395  1.00 60.97  ?  70   HIS A CG  1 
ATOM   552   N  ND1 . HIS A 1  70   ? -34.531 -72.355  53.876  1.00 63.36  ?  70   HIS A ND1 1 
ATOM   553   C  CD2 . HIS A 1  70   ? -33.387 -72.476  55.731  1.00 67.84  ?  70   HIS A CD2 1 
ATOM   554   C  CE1 . HIS A 1  70   ? -35.394 -72.573  54.853  1.00 70.01  ?  70   HIS A CE1 1 
ATOM   555   N  NE2 . HIS A 1  70   ? -34.726 -72.652  55.990  1.00 74.84  ?  70   HIS A NE2 1 
ATOM   556   N  N   . THR A 1  71   ? -30.253 -73.735  50.744  1.00 72.94  ?  71   THR A N   1 
ATOM   557   C  CA  . THR A 1  71   ? -28.946 -73.955  50.133  1.00 63.27  ?  71   THR A CA  1 
ATOM   558   C  C   . THR A 1  71   ? -28.375 -72.717  49.456  1.00 54.73  ?  71   THR A C   1 
ATOM   559   O  O   . THR A 1  71   ? -27.181 -72.706  49.139  1.00 56.15  ?  71   THR A O   1 
ATOM   560   C  CB  . THR A 1  71   ? -29.033 -75.089  49.110  1.00 68.75  ?  71   THR A CB  1 
ATOM   561   O  OG1 . THR A 1  71   ? -29.578 -74.586  47.884  1.00 79.94  ?  71   THR A OG1 1 
ATOM   562   C  CG2 . THR A 1  71   ? -29.929 -76.202  49.625  1.00 67.48  ?  71   THR A CG2 1 
ATOM   563   N  N   . SER A 1  72   ? -29.181 -71.681  49.229  1.00 69.29  ?  72   SER A N   1 
ATOM   564   C  CA  . SER A 1  72   ? -28.753 -70.519  48.461  1.00 75.06  ?  72   SER A CA  1 
ATOM   565   C  C   . SER A 1  72   ? -28.520 -69.292  49.335  1.00 75.94  ?  72   SER A C   1 
ATOM   566   O  O   . SER A 1  72   ? -28.534 -68.165  48.830  1.00 70.70  ?  72   SER A O   1 
ATOM   567   C  CB  . SER A 1  72   ? -29.780 -70.204  47.374  1.00 69.23  ?  72   SER A CB  1 
ATOM   568   O  OG  . SER A 1  72   ? -29.328 -69.152  46.543  1.00 77.76  ?  72   SER A OG  1 
ATOM   569   N  N   . VAL A 1  73   ? -28.285 -69.485  50.632  1.00 93.49  ?  73   VAL A N   1 
ATOM   570   C  CA  . VAL A 1  73   ? -28.237 -68.341  51.535  1.00 91.94  ?  73   VAL A CA  1 
ATOM   571   C  C   . VAL A 1  73   ? -26.877 -67.647  51.497  1.00 94.88  ?  73   VAL A C   1 
ATOM   572   O  O   . VAL A 1  73   ? -26.802 -66.419  51.622  1.00 93.76  ?  73   VAL A O   1 
ATOM   573   C  CB  . VAL A 1  73   ? -28.612 -68.782  52.961  1.00 83.45  ?  73   VAL A CB  1 
ATOM   574   C  CG1 . VAL A 1  73   ? -27.678 -69.881  53.451  1.00 90.41  ?  73   VAL A CG1 1 
ATOM   575   C  CG2 . VAL A 1  73   ? -28.609 -67.592  53.905  1.00 81.69  ?  73   VAL A CG2 1 
ATOM   576   N  N   . ASP A 1  74   ? -25.790 -68.394  51.316  1.00 96.65  ?  74   ASP A N   1 
ATOM   577   C  CA  . ASP A 1  74   ? -24.453 -67.817  51.304  1.00 95.89  ?  74   ASP A CA  1 
ATOM   578   C  C   . ASP A 1  74   ? -23.964 -67.488  49.901  1.00 94.89  ?  74   ASP A C   1 
ATOM   579   O  O   . ASP A 1  74   ? -22.793 -67.133  49.734  1.00 95.02  ?  74   ASP A O   1 
ATOM   580   C  CB  . ASP A 1  74   ? -23.461 -68.764  51.982  1.00 102.29 ?  74   ASP A CB  1 
ATOM   581   C  CG  . ASP A 1  74   ? -23.349 -70.093  51.268  1.00 105.37 ?  74   ASP A CG  1 
ATOM   582   O  OD1 . ASP A 1  74   ? -24.365 -70.554  50.705  1.00 106.72 ?  74   ASP A OD1 1 
ATOM   583   O  OD2 . ASP A 1  74   ? -22.243 -70.673  51.264  1.00 115.06 -1 74   ASP A OD2 1 
ATOM   584   N  N   . GLN A 1  75   ? -24.826 -67.597  48.895  1.00 59.55  ?  75   GLN A N   1 
ATOM   585   C  CA  . GLN A 1  75   ? -24.440 -67.357  47.513  1.00 58.29  ?  75   GLN A CA  1 
ATOM   586   C  C   . GLN A 1  75   ? -25.266 -66.288  46.818  1.00 58.03  ?  75   GLN A C   1 
ATOM   587   O  O   . GLN A 1  75   ? -24.765 -65.655  45.886  1.00 52.39  ?  75   GLN A O   1 
ATOM   588   C  CB  . GLN A 1  75   ? -24.534 -68.660  46.704  1.00 68.22  ?  75   GLN A CB  1 
ATOM   589   C  CG  . GLN A 1  75   ? -23.634 -68.703  45.481  1.00 68.32  ?  75   GLN A CG  1 
ATOM   590   C  CD  . GLN A 1  75   ? -23.306 -70.119  45.054  1.00 66.67  ?  75   GLN A CD  1 
ATOM   591   O  OE1 . GLN A 1  75   ? -23.993 -71.068  45.433  1.00 76.93  ?  75   GLN A OE1 1 
ATOM   592   N  NE2 . GLN A 1  75   ? -22.254 -70.269  44.257  1.00 82.65  ?  75   GLN A NE2 1 
ATOM   593   N  N   . SER A 1  76   ? -26.509 -66.064  47.240  1.00 51.71  ?  76   SER A N   1 
ATOM   594   C  CA  . SER A 1  76   ? -27.383 -65.094  46.598  1.00 52.72  ?  76   SER A CA  1 
ATOM   595   C  C   . SER A 1  76   ? -28.085 -64.266  47.665  1.00 49.54  ?  76   SER A C   1 
ATOM   596   O  O   . SER A 1  76   ? -27.920 -64.488  48.869  1.00 50.20  ?  76   SER A O   1 
ATOM   597   C  CB  . SER A 1  76   ? -28.410 -65.782  45.693  1.00 44.04  ?  76   SER A CB  1 
ATOM   598   O  OG  . SER A 1  76   ? -29.538 -66.202  46.440  1.00 45.27  ?  76   SER A OG  1 
ATOM   599   N  N   . TYR A 1  77   ? -28.887 -63.303  47.205  1.00 48.54  ?  77   TYR A N   1 
ATOM   600   C  CA  . TYR A 1  77   ? -29.705 -62.502  48.105  1.00 50.58  ?  77   TYR A CA  1 
ATOM   601   C  C   . TYR A 1  77   ? -30.860 -63.300  48.698  1.00 54.59  ?  77   TYR A C   1 
ATOM   602   O  O   . TYR A 1  77   ? -31.450 -62.866  49.694  1.00 56.58  ?  77   TYR A O   1 
ATOM   603   C  CB  . TYR A 1  77   ? -30.247 -61.276  47.362  1.00 45.58  ?  77   TYR A CB  1 
ATOM   604   C  CG  . TYR A 1  77   ? -31.564 -61.524  46.657  1.00 42.34  ?  77   TYR A CG  1 
ATOM   605   C  CD1 . TYR A 1  77   ? -31.607 -62.196  45.442  1.00 44.10  ?  77   TYR A CD1 1 
ATOM   606   C  CD2 . TYR A 1  77   ? -32.764 -61.088  47.207  1.00 40.69  ?  77   TYR A CD2 1 
ATOM   607   C  CE1 . TYR A 1  77   ? -32.807 -62.429  44.797  1.00 51.96  ?  77   TYR A CE1 1 
ATOM   608   C  CE2 . TYR A 1  77   ? -33.967 -61.317  46.570  1.00 40.89  ?  77   TYR A CE2 1 
ATOM   609   C  CZ  . TYR A 1  77   ? -33.983 -61.987  45.365  1.00 50.65  ?  77   TYR A CZ  1 
ATOM   610   O  OH  . TYR A 1  77   ? -35.182 -62.214  44.727  1.00 65.97  ?  77   TYR A OH  1 
ATOM   611   N  N   . PHE A 1  78   ? -31.184 -64.452  48.120  1.00 73.49  ?  78   PHE A N   1 
ATOM   612   C  CA  . PHE A 1  78   ? -32.372 -65.216  48.471  1.00 74.29  ?  78   PHE A CA  1 
ATOM   613   C  C   . PHE A 1  78   ? -31.975 -66.516  49.157  1.00 73.77  ?  78   PHE A C   1 
ATOM   614   O  O   . PHE A 1  78   ? -31.175 -67.288  48.619  1.00 69.71  ?  78   PHE A O   1 
ATOM   615   C  CB  . PHE A 1  78   ? -33.204 -65.511  47.220  1.00 71.91  ?  78   PHE A CB  1 
ATOM   616   C  CG  . PHE A 1  78   ? -34.541 -66.128  47.508  1.00 71.71  ?  78   PHE A CG  1 
ATOM   617   C  CD1 . PHE A 1  78   ? -35.596 -65.350  47.955  1.00 74.76  ?  78   PHE A CD1 1 
ATOM   618   C  CD2 . PHE A 1  78   ? -34.744 -67.486  47.326  1.00 71.77  ?  78   PHE A CD2 1 
ATOM   619   C  CE1 . PHE A 1  78   ? -36.830 -65.917  48.218  1.00 85.91  ?  78   PHE A CE1 1 
ATOM   620   C  CE2 . PHE A 1  78   ? -35.974 -68.059  47.587  1.00 78.50  ?  78   PHE A CE2 1 
ATOM   621   C  CZ  . PHE A 1  78   ? -37.019 -67.273  48.033  1.00 83.92  ?  78   PHE A CZ  1 
ATOM   622   N  N   . ALA A 1  79   ? -32.533 -66.752  50.341  1.00 104.40 ?  79   ALA A N   1 
ATOM   623   C  CA  . ALA A 1  79   ? -32.381 -68.035  51.013  1.00 107.32 ?  79   ALA A CA  1 
ATOM   624   C  C   . ALA A 1  79   ? -33.393 -69.016  50.434  1.00 114.11 ?  79   ALA A C   1 
ATOM   625   O  O   . ALA A 1  79   ? -34.605 -68.790  50.525  1.00 121.52 ?  79   ALA A O   1 
ATOM   626   C  CB  . ALA A 1  79   ? -32.572 -67.880  52.520  1.00 104.51 ?  79   ALA A CB  1 
ATOM   627   N  N   . ASN A 1  80   ? -32.897 -70.097  49.837  1.00 83.46  ?  80   ASN A N   1 
ATOM   628   C  CA  . ASN A 1  80   ? -33.764 -71.029  49.130  1.00 83.48  ?  80   ASN A CA  1 
ATOM   629   C  C   . ASN A 1  80   ? -34.782 -71.654  50.076  1.00 85.65  ?  80   ASN A C   1 
ATOM   630   O  O   . ASN A 1  80   ? -34.459 -72.033  51.204  1.00 85.63  ?  80   ASN A O   1 
ATOM   631   C  CB  . ASN A 1  80   ? -32.927 -72.123  48.463  1.00 76.99  ?  80   ASN A CB  1 
ATOM   632   C  CG  . ASN A 1  80   ? -33.744 -73.006  47.538  1.00 73.21  ?  80   ASN A CG  1 
ATOM   633   O  OD1 . ASN A 1  80   ? -34.924 -72.752  47.297  1.00 81.01  ?  80   ASN A OD1 1 
ATOM   634   N  ND2 . ASN A 1  80   ? -33.118 -74.056  47.021  1.00 78.43  ?  80   ASN A ND2 1 
ATOM   635   N  N   . ILE A 1  81   ? -36.023 -71.750  49.612  1.00 66.54  ?  81   ILE A N   1 
ATOM   636   C  CA  . ILE A 1  81   ? -37.067 -72.470  50.334  1.00 59.08  ?  81   ILE A CA  1 
ATOM   637   C  C   . ILE A 1  81   ? -37.092 -73.891  49.782  1.00 64.63  ?  81   ILE A C   1 
ATOM   638   O  O   . ILE A 1  81   ? -37.138 -74.075  48.557  1.00 70.99  ?  81   ILE A O   1 
ATOM   639   C  CB  . ILE A 1  81   ? -38.429 -71.771  50.202  1.00 57.66  ?  81   ILE A CB  1 
ATOM   640   C  CG1 . ILE A 1  81   ? -38.431 -70.469  51.005  1.00 56.67  ?  81   ILE A CG1 1 
ATOM   641   C  CG2 . ILE A 1  81   ? -39.554 -72.679  50.672  1.00 52.25  ?  81   ILE A CG2 1 
ATOM   642   C  CD1 . ILE A 1  81   ? -38.451 -70.671  52.503  1.00 63.89  ?  81   ILE A CD1 1 
ATOM   643   N  N   . PRO A 1  82   ? -37.054 -74.913  50.636  1.00 65.86  ?  82   PRO A N   1 
ATOM   644   C  CA  . PRO A 1  82   ? -36.831 -76.282  50.149  1.00 59.70  ?  82   PRO A CA  1 
ATOM   645   C  C   . PRO A 1  82   ? -37.929 -76.744  49.203  1.00 60.33  ?  82   PRO A C   1 
ATOM   646   O  O   . PRO A 1  82   ? -39.121 -76.584  49.476  1.00 56.78  ?  82   PRO A O   1 
ATOM   647   C  CB  . PRO A 1  82   ? -36.816 -77.116  51.435  1.00 64.48  ?  82   PRO A CB  1 
ATOM   648   C  CG  . PRO A 1  82   ? -36.502 -76.144  52.515  1.00 70.15  ?  82   PRO A CG  1 
ATOM   649   C  CD  . PRO A 1  82   ? -37.136 -74.857  52.104  1.00 69.42  ?  82   PRO A CD  1 
ATOM   650   N  N   . ALA A 1  83   ? -37.512 -77.325  48.082  1.00 57.02  ?  83   ALA A N   1 
ATOM   651   C  CA  . ALA A 1  83   ? -38.452 -77.945  47.166  1.00 51.01  ?  83   ALA A CA  1 
ATOM   652   C  C   . ALA A 1  83   ? -38.988 -79.244  47.767  1.00 55.70  ?  83   ALA A C   1 
ATOM   653   O  O   . ALA A 1  83   ? -38.451 -79.783  48.738  1.00 53.71  ?  83   ALA A O   1 
ATOM   654   C  CB  . ALA A 1  83   ? -37.787 -78.212  45.817  1.00 44.18  ?  83   ALA A CB  1 
ATOM   655   N  N   . THR A 1  84   ? -40.069 -79.751  47.169  1.00 65.91  ?  84   THR A N   1 
ATOM   656   C  CA  . THR A 1  84   ? -40.663 -80.997  47.642  1.00 63.64  ?  84   THR A CA  1 
ATOM   657   C  C   . THR A 1  84   ? -39.717 -82.180  47.481  1.00 62.60  ?  84   THR A C   1 
ATOM   658   O  O   . THR A 1  84   ? -39.890 -83.198  48.161  1.00 69.39  ?  84   THR A O   1 
ATOM   659   C  CB  . THR A 1  84   ? -41.977 -81.261  46.900  1.00 67.38  ?  84   THR A CB  1 
ATOM   660   O  OG1 . THR A 1  84   ? -42.718 -80.039  46.798  1.00 60.56  ?  84   THR A OG1 1 
ATOM   661   C  CG2 . THR A 1  84   ? -42.822 -82.283  47.645  1.00 73.32  ?  84   THR A CG2 1 
ATOM   662   N  N   . GLU A 1  85   ? -38.714 -82.065  46.606  1.00 89.89  ?  85   GLU A N   1 
ATOM   663   C  CA  . GLU A 1  85   ? -37.744 -83.142  46.436  1.00 93.89  ?  85   GLU A CA  1 
ATOM   664   C  C   . GLU A 1  85   ? -36.950 -83.378  47.715  1.00 97.75  ?  85   GLU A C   1 
ATOM   665   O  O   . GLU A 1  85   ? -36.673 -84.528  48.078  1.00 99.36  ?  85   GLU A O   1 
ATOM   666   C  CB  . GLU A 1  85   ? -36.804 -82.817  45.276  1.00 97.24  ?  85   GLU A CB  1 
ATOM   667   C  CG  . GLU A 1  85   ? -36.325 -84.026  44.494  1.00 105.30 ?  85   GLU A CG  1 
ATOM   668   C  CD  . GLU A 1  85   ? -35.276 -83.662  43.462  1.00 107.26 ?  85   GLU A CD  1 
ATOM   669   O  OE1 . GLU A 1  85   ? -34.908 -82.470  43.386  1.00 92.05  ?  85   GLU A OE1 1 
ATOM   670   O  OE2 . GLU A 1  85   ? -34.821 -84.564  42.728  1.00 121.06 -1 85   GLU A OE2 1 
ATOM   671   N  N   . THR A 1  86   ? -36.573 -82.303  48.410  1.00 76.20  ?  86   THR A N   1 
ATOM   672   C  CA  . THR A 1  86   ? -35.817 -82.455  49.650  1.00 72.51  ?  86   THR A CA  1 
ATOM   673   C  C   . THR A 1  86   ? -36.659 -83.124  50.728  1.00 73.88  ?  86   THR A C   1 
ATOM   674   O  O   . THR A 1  86   ? -36.139 -83.906  51.533  1.00 78.48  ?  86   THR A O   1 
ATOM   675   C  CB  . THR A 1  86   ? -35.316 -81.095  50.134  1.00 68.82  ?  86   THR A CB  1 
ATOM   676   O  OG1 . THR A 1  86   ? -36.434 -80.258  50.451  1.00 76.73  ?  86   THR A OG1 1 
ATOM   677   C  CG2 . THR A 1  86   ? -34.482 -80.421  49.058  1.00 71.05  ?  86   THR A CG2 1 
ATOM   678   N  N   . CYS A 1  87   ? -37.960 -82.829  50.761  1.00 73.40  ?  87   CYS A N   1 
ATOM   679   C  CA  . CYS A 1  87   ? -38.836 -83.470  51.737  1.00 77.86  ?  87   CYS A CA  1 
ATOM   680   C  C   . CYS A 1  87   ? -39.060 -84.937  51.398  1.00 77.32  ?  87   CYS A C   1 
ATOM   681   O  O   . CYS A 1  87   ? -39.079 -85.791  52.292  1.00 81.90  ?  87   CYS A O   1 
ATOM   682   C  CB  . CYS A 1  87   ? -40.169 -82.728  51.813  1.00 79.87  ?  87   CYS A CB  1 
ATOM   683   S  SG  . CYS A 1  87   ? -40.014 -80.935  51.935  1.00 75.20  ?  87   CYS A SG  1 
ATOM   684   N  N   . MET A 1  88   ? -39.231 -85.250  50.112  1.00 100.01 ?  88   MET A N   1 
ATOM   685   C  CA  . MET A 1  88   ? -39.454 -86.632  49.705  1.00 104.03 ?  88   MET A CA  1 
ATOM   686   C  C   . MET A 1  88   ? -38.196 -87.481  49.820  1.00 107.71 ?  88   MET A C   1 
ATOM   687   O  O   . MET A 1  88   ? -38.298 -88.712  49.844  1.00 106.55 ?  88   MET A O   1 
ATOM   688   C  CB  . MET A 1  88   ? -39.986 -86.680  48.272  1.00 99.23  ?  88   MET A CB  1 
ATOM   689   C  CG  . MET A 1  88   ? -41.458 -86.316  48.145  1.00 105.77 ?  88   MET A CG  1 
ATOM   690   S  SD  . MET A 1  88   ? -42.439 -86.810  49.577  1.00 107.99 ?  88   MET A SD  1 
ATOM   691   C  CE  . MET A 1  88   ? -42.526 -88.585  49.343  1.00 120.75 ?  88   MET A CE  1 
ATOM   692   N  N   . THR A 1  89   ? -37.017 -86.856  49.889  1.00 98.24  ?  89   THR A N   1 
ATOM   693   C  CA  . THR A 1  89   ? -35.785 -87.615  50.075  1.00 90.03  ?  89   THR A CA  1 
ATOM   694   C  C   . THR A 1  89   ? -35.823 -88.426  51.362  1.00 88.27  ?  89   THR A C   1 
ATOM   695   O  O   . THR A 1  89   ? -35.260 -89.525  51.423  1.00 101.43 ?  89   THR A O   1 
ATOM   696   C  CB  . THR A 1  89   ? -34.581 -86.669  50.077  1.00 94.11  ?  89   THR A CB  1 
ATOM   697   O  OG1 . THR A 1  89   ? -34.587 -85.885  48.878  1.00 107.11 ?  89   THR A OG1 1 
ATOM   698   C  CG2 . THR A 1  89   ? -33.279 -87.454  50.149  1.00 90.86  ?  89   THR A CG2 1 
ATOM   699   N  N   . CYS A 1  90   ? -36.496 -87.913  52.390  1.00 86.82  ?  90   CYS A N   1 
ATOM   700   C  CA  . CYS A 1  90   ? -36.642 -88.603  53.664  1.00 92.71  ?  90   CYS A CA  1 
ATOM   701   C  C   . CYS A 1  90   ? -38.018 -89.223  53.852  1.00 93.74  ?  90   CYS A C   1 
ATOM   702   O  O   . CYS A 1  90   ? -38.120 -90.361  54.320  1.00 100.85 ?  90   CYS A O   1 
ATOM   703   C  CB  . CYS A 1  90   ? -36.368 -87.640  54.822  1.00 86.73  ?  90   CYS A CB  1 
ATOM   704   S  SG  . CYS A 1  90   ? -34.623 -87.346  55.142  1.00 87.85  ?  90   CYS A SG  1 
ATOM   705   N  N   . HIS A 1  91   ? -39.079 -88.504  53.497  1.00 78.32  ?  91   HIS A N   1 
ATOM   706   C  CA  . HIS A 1  91   ? -40.437 -88.955  53.765  1.00 80.98  ?  91   HIS A CA  1 
ATOM   707   C  C   . HIS A 1  91   ? -40.964 -89.933  52.724  1.00 92.54  ?  91   HIS A C   1 
ATOM   708   O  O   . HIS A 1  91   ? -42.141 -90.306  52.789  1.00 95.95  ?  91   HIS A O   1 
ATOM   709   C  CB  . HIS A 1  91   ? -41.367 -87.746  53.881  1.00 77.77  ?  91   HIS A CB  1 
ATOM   710   C  CG  . HIS A 1  91   ? -41.043 -86.856  55.041  1.00 80.71  ?  91   HIS A CG  1 
ATOM   711   N  ND1 . HIS A 1  91   ? -41.134 -87.279  56.349  1.00 83.90  ?  91   HIS A ND1 1 
ATOM   712   C  CD2 . HIS A 1  91   ? -40.610 -85.574  55.090  1.00 89.52  ?  91   HIS A CD2 1 
ATOM   713   C  CE1 . HIS A 1  91   ? -40.781 -86.294  57.155  1.00 80.15  ?  91   HIS A CE1 1 
ATOM   714   N  NE2 . HIS A 1  91   ? -40.458 -85.248  56.416  1.00 85.02  ?  91   HIS A NE2 1 
ATOM   715   N  N   . SER A 1  92   ? -40.135 -90.357  51.768  1.00 103.58 ?  92   SER A N   1 
ATOM   716   C  CA  . SER A 1  92   ? -40.502 -91.497  50.938  1.00 100.56 ?  92   SER A CA  1 
ATOM   717   C  C   . SER A 1  92   ? -40.440 -92.802  51.718  1.00 102.42 ?  92   SER A C   1 
ATOM   718   O  O   . SER A 1  92   ? -41.028 -93.799  51.288  1.00 111.84 ?  92   SER A O   1 
ATOM   719   C  CB  . SER A 1  92   ? -39.594 -91.578  49.711  1.00 102.12 ?  92   SER A CB  1 
ATOM   720   O  OG  . SER A 1  92   ? -39.879 -90.531  48.799  1.00 102.13 ?  92   SER A OG  1 
ATOM   721   N  N   . GLN A 1  93   ? -39.746 -92.812  52.856  1.00 104.82 ?  93   GLN A N   1 
ATOM   722   C  CA  . GLN A 1  93   ? -39.634 -94.003  53.687  1.00 112.84 ?  93   GLN A CA  1 
ATOM   723   C  C   . GLN A 1  93   ? -40.009 -93.691  55.131  1.00 117.02 ?  93   GLN A C   1 
ATOM   724   O  O   . GLN A 1  93   ? -40.476 -94.571  55.860  1.00 120.42 ?  93   GLN A O   1 
ATOM   725   C  CB  . GLN A 1  93   ? -38.214 -94.569  53.620  1.00 116.61 ?  93   GLN A CB  1 
ATOM   726   C  CG  . GLN A 1  93   ? -37.790 -95.029  52.238  1.00 107.88 ?  93   GLN A CG  1 
ATOM   727   C  CD  . GLN A 1  93   ? -36.459 -95.754  52.254  1.00 116.05 ?  93   GLN A CD  1 
ATOM   728   O  OE1 . GLN A 1  93   ? -35.805 -95.852  53.291  1.00 124.20 ?  93   GLN A OE1 1 
ATOM   729   N  NE2 . GLN A 1  93   ? -36.056 -96.274  51.102  1.00 121.40 ?  93   GLN A NE2 1 
ATOM   730   N  N   . ILE A 1  94   ? -39.805 -92.445  55.552  1.00 107.69 ?  94   ILE A N   1 
ATOM   731   C  CA  . ILE A 1  94   ? -40.095 -92.024  56.918  1.00 96.94  ?  94   ILE A CA  1 
ATOM   732   C  C   . ILE A 1  94   ? -41.534 -91.541  56.999  1.00 98.32  ?  94   ILE A C   1 
ATOM   733   O  O   . ILE A 1  94   ? -41.941 -90.646  56.248  1.00 101.84 ?  94   ILE A O   1 
ATOM   734   C  CB  . ILE A 1  94   ? -39.129 -90.920  57.373  1.00 89.29  ?  94   ILE A CB  1 
ATOM   735   C  CG1 . ILE A 1  94   ? -37.751 -91.501  57.667  1.00 96.26  ?  94   ILE A CG1 1 
ATOM   736   C  CG2 . ILE A 1  94   ? -39.675 -90.207  58.604  1.00 80.91  ?  94   ILE A CG2 1 
ATOM   737   C  CD1 . ILE A 1  94   ? -36.765 -90.463  58.114  1.00 91.26  ?  94   ILE A CD1 1 
ATOM   738   N  N   . LYS A 1  95   ? -42.300 -92.128  57.921  1.00 91.92  ?  95   LYS A N   1 
ATOM   739   C  CA  . LYS A 1  95   ? -43.674 -91.707  58.196  1.00 91.19  ?  95   LYS A CA  1 
ATOM   740   C  C   . LYS A 1  95   ? -44.517 -91.675  56.925  1.00 96.62  ?  95   LYS A C   1 
ATOM   741   O  O   . LYS A 1  95   ? -45.420 -90.848  56.782  1.00 90.60  ?  95   LYS A O   1 
ATOM   742   C  CB  . LYS A 1  95   ? -43.703 -90.347  58.898  1.00 82.56  ?  95   LYS A CB  1 
ATOM   743   C  CG  . LYS A 1  95   ? -43.494 -90.419  60.403  1.00 80.88  ?  95   LYS A CG  1 
ATOM   744   C  CD  . LYS A 1  95   ? -44.506 -91.345  61.058  1.00 87.93  ?  95   LYS A CD  1 
ATOM   745   C  CE  . LYS A 1  95   ? -44.303 -91.407  62.564  1.00 98.07  ?  95   LYS A CE  1 
ATOM   746   N  NZ  . LYS A 1  95   ? -45.318 -92.271  63.228  1.00 95.19  ?  95   LYS A NZ  1 
ATOM   747   N  N   . THR A 1  96   ? -44.216 -92.566  55.987  1.00 150.40 ?  96   THR A N   1 
ATOM   748   C  CA  . THR A 1  96   ? -45.005 -92.652  54.769  1.00 154.27 ?  96   THR A CA  1 
ATOM   749   C  C   . THR A 1  96   ? -46.408 -93.154  55.090  1.00 159.86 ?  96   THR A C   1 
ATOM   750   O  O   . THR A 1  96   ? -46.627 -93.869  56.073  1.00 164.55 ?  96   THR A O   1 
ATOM   751   C  CB  . THR A 1  96   ? -44.325 -93.570  53.751  1.00 152.70 ?  96   THR A CB  1 
ATOM   752   O  OG1 . THR A 1  96   ? -45.085 -93.590  52.537  1.00 165.05 ?  96   THR A OG1 1 
ATOM   753   C  CG2 . THR A 1  96   ? -44.202 -94.986  54.298  1.00 154.46 ?  96   THR A CG2 1 
ATOM   754   N  N   . TYR A 1  97   ? -47.367 -92.753  54.253  1.00 138.67 ?  97   TYR A N   1 
ATOM   755   C  CA  . TYR A 1  97   ? -48.784 -93.059  54.461  1.00 143.17 ?  97   TYR A CA  1 
ATOM   756   C  C   . TYR A 1  97   ? -49.276 -92.485  55.791  1.00 135.46 ?  97   TYR A C   1 
ATOM   757   O  O   . TYR A 1  97   ? -49.895 -93.174  56.605  1.00 132.59 ?  97   TYR A O   1 
ATOM   758   C  CB  . TYR A 1  97   ? -49.046 -94.566  54.374  1.00 147.99 ?  97   TYR A CB  1 
ATOM   759   C  CG  . TYR A 1  97   ? -48.403 -95.237  53.179  1.00 159.03 ?  97   TYR A CG  1 
ATOM   760   C  CD1 . TYR A 1  97   ? -48.452 -94.652  51.919  1.00 164.02 ?  97   TYR A CD1 1 
ATOM   761   C  CD2 . TYR A 1  97   ? -47.742 -96.451  53.312  1.00 165.05 ?  97   TYR A CD2 1 
ATOM   762   C  CE1 . TYR A 1  97   ? -47.865 -95.261  50.824  1.00 161.19 ?  97   TYR A CE1 1 
ATOM   763   C  CE2 . TYR A 1  97   ? -47.151 -97.068  52.222  1.00 170.36 ?  97   TYR A CE2 1 
ATOM   764   C  CZ  . TYR A 1  97   ? -47.216 -96.468  50.981  1.00 164.84 ?  97   TYR A CZ  1 
ATOM   765   O  OH  . TYR A 1  97   ? -46.630 -97.076  49.894  1.00 160.18 ?  97   TYR A OH  1 
ATOM   766   N  N   . SER A 1  98   ? -48.990 -91.201  56.007  1.00 112.99 ?  98   SER A N   1 
ATOM   767   C  CA  . SER A 1  98   ? -49.397 -90.460  57.190  1.00 106.15 ?  98   SER A CA  1 
ATOM   768   C  C   . SER A 1  98   ? -50.176 -89.212  56.786  1.00 101.85 ?  98   SER A C   1 
ATOM   769   O  O   . SER A 1  98   ? -49.887 -88.606  55.749  1.00 105.68 ?  98   SER A O   1 
ATOM   770   C  CB  . SER A 1  98   ? -48.183 -90.055  58.035  1.00 98.09  ?  98   SER A CB  1 
ATOM   771   O  OG  . SER A 1  98   ? -48.556 -89.219  59.117  1.00 87.91  ?  98   SER A OG  1 
ATOM   772   N  N   . PRO A 1  99   ? -51.171 -88.806  57.580  1.00 90.01  ?  99   PRO A N   1 
ATOM   773   C  CA  . PRO A 1  99   ? -51.980 -87.640  57.188  1.00 92.47  ?  99   PRO A CA  1 
ATOM   774   C  C   . PRO A 1  99   ? -51.216 -86.328  57.220  1.00 87.45  ?  99   PRO A C   1 
ATOM   775   O  O   . PRO A 1  99   ? -51.498 -85.445  56.400  1.00 97.71  ?  99   PRO A O   1 
ATOM   776   C  CB  . PRO A 1  99   ? -53.125 -87.647  58.211  1.00 89.99  ?  99   PRO A CB  1 
ATOM   777   C  CG  . PRO A 1  99   ? -52.582 -88.393  59.380  1.00 82.55  ?  99   PRO A CG  1 
ATOM   778   C  CD  . PRO A 1  99   ? -51.677 -89.441  58.808  1.00 86.23  ?  99   PRO A CD  1 
ATOM   779   N  N   . LEU A 1  100  ? -50.261 -86.168  58.139  1.00 85.59  ?  100  LEU A N   1 
ATOM   780   C  CA  . LEU A 1  100  ? -49.539 -84.906  58.254  1.00 89.09  ?  100  LEU A CA  1 
ATOM   781   C  C   . LEU A 1  100  ? -48.678 -84.608  57.033  1.00 86.53  ?  100  LEU A C   1 
ATOM   782   O  O   . LEU A 1  100  ? -48.336 -83.443  56.802  1.00 82.09  ?  100  LEU A O   1 
ATOM   783   C  CB  . LEU A 1  100  ? -48.669 -84.910  59.512  1.00 90.93  ?  100  LEU A CB  1 
ATOM   784   C  CG  . LEU A 1  100  ? -49.411 -84.735  60.838  1.00 73.20  ?  100  LEU A CG  1 
ATOM   785   C  CD1 . LEU A 1  100  ? -48.459 -84.895  62.011  1.00 71.15  ?  100  LEU A CD1 1 
ATOM   786   C  CD2 . LEU A 1  100  ? -50.111 -83.384  60.886  1.00 66.51  ?  100  LEU A CD2 1 
ATOM   787   N  N   . LEU A 1  101  ? -48.324 -85.625  56.250  1.00 81.94  ?  101  LEU A N   1 
ATOM   788   C  CA  . LEU A 1  101  ? -47.507 -85.451  55.057  1.00 77.22  ?  101  LEU A CA  1 
ATOM   789   C  C   . LEU A 1  101  ? -48.313 -85.591  53.773  1.00 76.69  ?  101  LEU A C   1 
ATOM   790   O  O   . LEU A 1  101  ? -47.724 -85.768  52.701  1.00 73.86  ?  101  LEU A O   1 
ATOM   791   C  CB  . LEU A 1  101  ? -46.353 -86.457  55.061  1.00 75.85  ?  101  LEU A CB  1 
ATOM   792   C  CG  . LEU A 1  101  ? -45.138 -86.098  55.917  1.00 69.30  ?  101  LEU A CG  1 
ATOM   793   C  CD1 . LEU A 1  101  ? -44.438 -87.358  56.398  1.00 70.88  ?  101  LEU A CD1 1 
ATOM   794   C  CD2 . LEU A 1  101  ? -44.176 -85.208  55.144  1.00 74.72  ?  101  LEU A CD2 1 
ATOM   795   N  N   . GLU A 1  102  ? -49.644 -85.515  53.856  1.00 118.18 ?  102  GLU A N   1 
ATOM   796   C  CA  . GLU A 1  102  ? -50.483 -85.724  52.680  1.00 124.17 ?  102  GLU A CA  1 
ATOM   797   C  C   . GLU A 1  102  ? -50.222 -84.658  51.622  1.00 120.05 ?  102  GLU A C   1 
ATOM   798   O  O   . GLU A 1  102  ? -50.097 -84.965  50.431  1.00 122.78 ?  102  GLU A O   1 
ATOM   799   C  CB  . GLU A 1  102  ? -51.958 -85.728  53.087  1.00 127.62 ?  102  GLU A CB  1 
ATOM   800   C  CG  . GLU A 1  102  ? -52.962 -85.993  51.959  1.00 138.81 ?  102  GLU A CG  1 
ATOM   801   C  CD  . GLU A 1  102  ? -52.646 -87.233  51.132  1.00 153.18 ?  102  GLU A CD  1 
ATOM   802   O  OE1 . GLU A 1  102  ? -51.735 -87.189  50.278  1.00 149.74 ?  102  GLU A OE1 1 
ATOM   803   O  OE2 . GLU A 1  102  ? -53.323 -88.262  51.339  1.00 164.44 -1 102  GLU A OE2 1 
ATOM   804   N  N   . LYS A 1  103  ? -50.132 -83.394  52.043  1.00 86.50  ?  103  LYS A N   1 
ATOM   805   C  CA  . LYS A 1  103  ? -49.881 -82.312  51.096  1.00 77.33  ?  103  LYS A CA  1 
ATOM   806   C  C   . LYS A 1  103  ? -48.538 -82.484  50.400  1.00 77.15  ?  103  LYS A C   1 
ATOM   807   O  O   . LYS A 1  103  ? -48.421 -82.246  49.192  1.00 84.51  ?  103  LYS A O   1 
ATOM   808   C  CB  . LYS A 1  103  ? -49.938 -80.962  51.810  1.00 84.96  ?  103  LYS A CB  1 
ATOM   809   C  CG  . LYS A 1  103  ? -51.279 -80.645  52.445  1.00 89.64  ?  103  LYS A CG  1 
ATOM   810   C  CD  . LYS A 1  103  ? -52.280 -80.164  51.409  1.00 94.03  ?  103  LYS A CD  1 
ATOM   811   C  CE  . LYS A 1  103  ? -53.536 -79.634  52.075  1.00 102.14 ?  103  LYS A CE  1 
ATOM   812   N  NZ  . LYS A 1  103  ? -53.215 -78.582  53.080  1.00 110.36 ?  103  LYS A NZ  1 
ATOM   813   N  N   . VAL A 1  104  ? -47.511 -82.896  51.147  1.00 58.79  ?  104  VAL A N   1 
ATOM   814   C  CA  . VAL A 1  104  ? -46.187 -83.084  50.558  1.00 57.20  ?  104  VAL A CA  1 
ATOM   815   C  C   . VAL A 1  104  ? -46.212 -84.226  49.549  1.00 65.24  ?  104  VAL A C   1 
ATOM   816   O  O   . VAL A 1  104  ? -45.557 -84.164  48.501  1.00 65.48  ?  104  VAL A O   1 
ATOM   817   C  CB  . VAL A 1  104  ? -45.142 -83.321  51.665  1.00 52.17  ?  104  VAL A CB  1 
ATOM   818   C  CG1 . VAL A 1  104  ? -43.789 -83.682  51.065  1.00 44.82  ?  104  VAL A CG1 1 
ATOM   819   C  CG2 . VAL A 1  104  ? -45.028 -82.094  52.557  1.00 51.66  ?  104  VAL A CG2 1 
ATOM   820   N  N   . ARG A 1  105  ? -46.974 -85.282  49.842  1.00 104.84 ?  105  ARG A N   1 
ATOM   821   C  CA  . ARG A 1  105  ? -47.101 -86.392  48.907  1.00 103.78 ?  105  ARG A CA  1 
ATOM   822   C  C   . ARG A 1  105  ? -48.024 -86.074  47.738  1.00 103.62 ?  105  ARG A C   1 
ATOM   823   O  O   . ARG A 1  105  ? -47.908 -86.713  46.687  1.00 111.94 ?  105  ARG A O   1 
ATOM   824   C  CB  . ARG A 1  105  ? -47.597 -87.645  49.633  1.00 104.06 ?  105  ARG A CB  1 
ATOM   825   C  CG  . ARG A 1  105  ? -46.552 -88.292  50.526  1.00 104.95 ?  105  ARG A CG  1 
ATOM   826   C  CD  . ARG A 1  105  ? -46.990 -89.673  50.982  1.00 108.87 ?  105  ARG A CD  1 
ATOM   827   N  NE  . ARG A 1  105  ? -48.391 -89.696  51.385  1.00 112.25 ?  105  ARG A NE  1 
ATOM   828   C  CZ  . ARG A 1  105  ? -48.814 -89.515  52.628  1.00 115.50 ?  105  ARG A CZ  1 
ATOM   829   N  NH1 . ARG A 1  105  ? -47.967 -89.294  53.621  1.00 117.06 ?  105  ARG A NH1 1 
ATOM   830   N  NH2 . ARG A 1  105  ? -50.118 -89.557  52.883  1.00 108.98 ?  105  ARG A NH2 1 
ATOM   831   N  N   . GLU A 1  106  ? -48.937 -85.111  47.893  1.00 78.62  ?  106  GLU A N   1 
ATOM   832   C  CA  . GLU A 1  106  ? -49.761 -84.702  46.760  1.00 82.91  ?  106  GLU A CA  1 
ATOM   833   C  C   . GLU A 1  106  ? -48.933 -83.929  45.741  1.00 91.10  ?  106  GLU A C   1 
ATOM   834   O  O   . GLU A 1  106  ? -49.083 -84.129  44.529  1.00 95.11  ?  106  GLU A O   1 
ATOM   835   C  CB  . GLU A 1  106  ? -50.952 -83.873  47.239  1.00 86.25  ?  106  GLU A CB  1 
ATOM   836   C  CG  . GLU A 1  106  ? -51.895 -83.459  46.121  1.00 94.19  ?  106  GLU A CG  1 
ATOM   837   C  CD  . GLU A 1  106  ? -53.350 -83.488  46.540  1.00 112.41 ?  106  GLU A CD  1 
ATOM   838   O  OE1 . GLU A 1  106  ? -53.618 -83.645  47.750  1.00 115.63 ?  106  GLU A OE1 1 
ATOM   839   O  OE2 . GLU A 1  106  ? -54.228 -83.362  45.660  1.00 119.27 -1 106  GLU A OE2 1 
ATOM   840   N  N   . SER A 1  107  ? -48.049 -83.052  46.211  1.00 98.49  ?  107  SER A N   1 
ATOM   841   C  CA  . SER A 1  107  ? -47.021 -82.493  45.347  1.00 93.54  ?  107  SER A CA  1 
ATOM   842   C  C   . SER A 1  107  ? -46.029 -83.591  44.967  1.00 96.63  ?  107  SER A C   1 
ATOM   843   O  O   . SER A 1  107  ? -46.159 -84.751  45.373  1.00 105.11 ?  107  SER A O   1 
ATOM   844   C  CB  . SER A 1  107  ? -46.320 -81.325  46.036  1.00 79.09  ?  107  SER A CB  1 
ATOM   845   O  OG  . SER A 1  107  ? -47.241 -80.298  46.361  1.00 81.57  ?  107  SER A OG  1 
ATOM   846   N  N   . TYR A 1  108  ? -45.035 -83.223  44.155  1.00 97.53  ?  108  TYR A N   1 
ATOM   847   C  CA  . TYR A 1  108  ? -44.024 -84.152  43.651  1.00 109.04 ?  108  TYR A CA  1 
ATOM   848   C  C   . TYR A 1  108  ? -44.645 -85.193  42.720  1.00 110.35 ?  108  TYR A C   1 
ATOM   849   O  O   . TYR A 1  108  ? -44.027 -85.584  41.724  1.00 101.36 ?  108  TYR A O   1 
ATOM   850   C  CB  . TYR A 1  108  ? -43.281 -84.826  44.811  1.00 104.40 ?  108  TYR A CB  1 
ATOM   851   C  CG  . TYR A 1  108  ? -42.031 -85.572  44.406  1.00 104.84 ?  108  TYR A CG  1 
ATOM   852   C  CD1 . TYR A 1  108  ? -40.831 -84.899  44.217  1.00 104.40 ?  108  TYR A CD1 1 
ATOM   853   C  CD2 . TYR A 1  108  ? -42.046 -86.948  44.225  1.00 96.71  ?  108  TYR A CD2 1 
ATOM   854   C  CE1 . TYR A 1  108  ? -39.683 -85.575  43.852  1.00 100.48 ?  108  TYR A CE1 1 
ATOM   855   C  CE2 . TYR A 1  108  ? -40.903 -87.633  43.859  1.00 104.42 ?  108  TYR A CE2 1 
ATOM   856   C  CZ  . TYR A 1  108  ? -39.725 -86.941  43.674  1.00 108.55 ?  108  TYR A CZ  1 
ATOM   857   O  OH  . TYR A 1  108  ? -38.583 -87.617  43.310  1.00 120.13 ?  108  TYR A OH  1 
ATOM   858   N  N   . ALA A 1  109  ? -45.858 -85.655  43.035  1.00 114.62 ?  109  ALA A N   1 
ATOM   859   C  CA  . ALA A 1  109  ? -46.631 -86.441  42.080  1.00 117.98 ?  109  ALA A CA  1 
ATOM   860   C  C   . ALA A 1  109  ? -47.258 -85.545  41.020  1.00 120.56 ?  109  ALA A C   1 
ATOM   861   O  O   . ALA A 1  109  ? -47.232 -85.874  39.828  1.00 127.76 ?  109  ALA A O   1 
ATOM   862   C  CB  . ALA A 1  109  ? -47.707 -87.248  42.807  1.00 123.84 ?  109  ALA A CB  1 
ATOM   863   N  N   . THR A 1  110  ? -47.827 -84.418  41.436  1.00 118.53 ?  110  THR A N   1 
ATOM   864   C  CA  . THR A 1  110  ? -48.273 -83.370  40.533  1.00 118.64 ?  110  THR A CA  1 
ATOM   865   C  C   . THR A 1  110  ? -47.382 -82.147  40.707  1.00 117.52 ?  110  THR A C   1 
ATOM   866   O  O   . THR A 1  110  ? -46.827 -81.911  41.784  1.00 120.13 ?  110  THR A O   1 
ATOM   867   C  CB  . THR A 1  110  ? -49.735 -82.989  40.791  1.00 122.33 ?  110  THR A CB  1 
ATOM   868   O  OG1 . THR A 1  110  ? -49.847 -82.351  42.069  1.00 115.99 ?  110  THR A OG1 1 
ATOM   869   C  CG2 . THR A 1  110  ? -50.621 -84.225  40.765  1.00 127.50 ?  110  THR A CG2 1 
ATOM   870   N  N   . GLY A 1  111  ? -47.250 -81.367  39.637  1.00 125.38 ?  111  GLY A N   1 
ATOM   871   C  CA  . GLY A 1  111  ? -46.356 -80.224  39.640  1.00 126.26 ?  111  GLY A CA  1 
ATOM   872   C  C   . GLY A 1  111  ? -46.755 -79.080  40.546  1.00 122.44 ?  111  GLY A C   1 
ATOM   873   O  O   . GLY A 1  111  ? -46.039 -78.075  40.590  1.00 116.80 ?  111  GLY A O   1 
ATOM   874   N  N   . LYS A 1  112  ? -47.864 -79.198  41.271  1.00 125.13 ?  112  LYS A N   1 
ATOM   875   C  CA  . LYS A 1  112  ? -48.320 -78.104  42.114  1.00 119.60 ?  112  LYS A CA  1 
ATOM   876   C  C   . LYS A 1  112  ? -47.337 -77.868  43.259  1.00 120.32 ?  112  LYS A C   1 
ATOM   877   O  O   . LYS A 1  112  ? -46.802 -78.824  43.830  1.00 127.19 ?  112  LYS A O   1 
ATOM   878   C  CB  . LYS A 1  112  ? -49.710 -78.401  42.675  1.00 120.32 ?  112  LYS A CB  1 
ATOM   879   C  CG  . LYS A 1  112  ? -50.775 -78.618  41.616  1.00 121.61 ?  112  LYS A CG  1 
ATOM   880   C  CD  . LYS A 1  112  ? -51.268 -77.297  41.049  1.00 114.32 ?  112  LYS A CD  1 
ATOM   881   C  CE  . LYS A 1  112  ? -51.587 -77.422  39.569  1.00 122.49 ?  112  LYS A CE  1 
ATOM   882   N  NZ  . LYS A 1  112  ? -52.851 -78.173  39.340  1.00 113.12 ?  112  LYS A NZ  1 
ATOM   883   N  N   . PRO A 1  113  ? -47.076 -76.609  43.616  1.00 84.45  ?  113  PRO A N   1 
ATOM   884   C  CA  . PRO A 1  113  ? -46.158 -76.331  44.726  1.00 77.85  ?  113  PRO A CA  1 
ATOM   885   C  C   . PRO A 1  113  ? -46.856 -76.348  46.075  1.00 76.50  ?  113  PRO A C   1 
ATOM   886   O  O   . PRO A 1  113  ? -48.071 -76.558  46.155  1.00 76.11  ?  113  PRO A O   1 
ATOM   887   C  CB  . PRO A 1  113  ? -45.633 -74.932  44.389  1.00 71.82  ?  113  PRO A CB  1 
ATOM   888   C  CG  . PRO A 1  113  ? -46.797 -74.279  43.710  1.00 69.30  ?  113  PRO A CG  1 
ATOM   889   C  CD  . PRO A 1  113  ? -47.546 -75.371  42.969  1.00 83.04  ?  113  PRO A CD  1 
ATOM   890   N  N   . ILE A 1  114  ? -46.094 -76.126  47.141  1.00 89.52  ?  114  ILE A N   1 
ATOM   891   C  CA  . ILE A 1  114  ? -46.637 -75.985  48.485  1.00 93.32  ?  114  ILE A CA  1 
ATOM   892   C  C   . ILE A 1  114  ? -46.647 -74.502  48.825  1.00 92.01  ?  114  ILE A C   1 
ATOM   893   O  O   . ILE A 1  114  ? -45.597 -73.849  48.822  1.00 91.99  ?  114  ILE A O   1 
ATOM   894   C  CB  . ILE A 1  114  ? -45.822 -76.788  49.510  1.00 90.13  ?  114  ILE A CB  1 
ATOM   895   C  CG1 . ILE A 1  114  ? -45.816 -78.273  49.139  1.00 80.00  ?  114  ILE A CG1 1 
ATOM   896   C  CG2 . ILE A 1  114  ? -46.384 -76.584  50.908  1.00 89.34  ?  114  ILE A CG2 1 
ATOM   897   C  CD1 . ILE A 1  114  ? -45.049 -79.144  50.110  1.00 75.53  ?  114  ILE A CD1 1 
ATOM   898   N  N   . GLU A 1  115  ? -47.833 -73.968  49.117  1.00 114.01 ?  115  GLU A N   1 
ATOM   899   C  CA  . GLU A 1  115  ? -48.009 -72.528  49.302  1.00 112.87 ?  115  GLU A CA  1 
ATOM   900   C  C   . GLU A 1  115  ? -47.768 -72.175  50.767  1.00 108.55 ?  115  GLU A C   1 
ATOM   901   O  O   . GLU A 1  115  ? -48.695 -71.964  51.552  1.00 113.80 ?  115  GLU A O   1 
ATOM   902   C  CB  . GLU A 1  115  ? -49.397 -72.098  48.842  1.00 122.50 ?  115  GLU A CB  1 
ATOM   903   C  CG  . GLU A 1  115  ? -49.684 -72.380  47.375  1.00 130.24 ?  115  GLU A CG  1 
ATOM   904   C  CD  . GLU A 1  115  ? -48.977 -71.416  46.444  1.00 129.22 ?  115  GLU A CD  1 
ATOM   905   O  OE1 . GLU A 1  115  ? -48.758 -70.253  46.844  1.00 123.91 ?  115  GLU A OE1 1 
ATOM   906   O  OE2 . GLU A 1  115  ? -48.643 -71.822  45.311  1.00 126.02 -1 115  GLU A OE2 1 
ATOM   907   N  N   . TRP A 1  116  ? -46.491 -72.107  51.137  1.00 75.19  ?  116  TRP A N   1 
ATOM   908   C  CA  . TRP A 1  116  ? -46.144 -71.642  52.470  1.00 72.59  ?  116  TRP A CA  1 
ATOM   909   C  C   . TRP A 1  116  ? -46.412 -70.145  52.599  1.00 72.30  ?  116  TRP A C   1 
ATOM   910   O  O   . TRP A 1  116  ? -46.502 -69.412  51.610  1.00 73.78  ?  116  TRP A O   1 
ATOM   911   C  CB  . TRP A 1  116  ? -44.678 -71.938  52.798  1.00 63.01  ?  116  TRP A CB  1 
ATOM   912   C  CG  . TRP A 1  116  ? -44.402 -73.370  53.148  1.00 79.05  ?  116  TRP A CG  1 
ATOM   913   C  CD1 . TRP A 1  116  ? -44.675 -73.986  54.335  1.00 74.23  ?  116  TRP A CD1 1 
ATOM   914   C  CD2 . TRP A 1  116  ? -43.761 -74.352  52.326  1.00 73.15  ?  116  TRP A CD2 1 
ATOM   915   N  NE1 . TRP A 1  116  ? -44.265 -75.295  54.295  1.00 66.39  ?  116  TRP A NE1 1 
ATOM   916   C  CE2 . TRP A 1  116  ? -43.700 -75.545  53.073  1.00 72.21  ?  116  TRP A CE2 1 
ATOM   917   C  CE3 . TRP A 1  116  ? -43.243 -74.342  51.029  1.00 65.20  ?  116  TRP A CE3 1 
ATOM   918   C  CZ2 . TRP A 1  116  ? -43.142 -76.715  52.566  1.00 76.46  ?  116  TRP A CZ2 1 
ATOM   919   C  CZ3 . TRP A 1  116  ? -42.689 -75.507  50.528  1.00 76.38  ?  116  TRP A CZ3 1 
ATOM   920   C  CH2 . TRP A 1  116  ? -42.643 -76.676  51.295  1.00 80.00  ?  116  TRP A CH2 1 
ATOM   921   N  N   . VAL A 1  117  ? -46.545 -69.694  53.843  1.00 78.09  ?  117  VAL A N   1 
ATOM   922   C  CA  . VAL A 1  117  ? -46.795 -68.292  54.153  1.00 76.14  ?  117  VAL A CA  1 
ATOM   923   C  C   . VAL A 1  117  ? -45.487 -67.658  54.599  1.00 73.79  ?  117  VAL A C   1 
ATOM   924   O  O   . VAL A 1  117  ? -44.755 -68.231  55.416  1.00 72.50  ?  117  VAL A O   1 
ATOM   925   C  CB  . VAL A 1  117  ? -47.878 -68.142  55.236  1.00 76.81  ?  117  VAL A CB  1 
ATOM   926   C  CG1 . VAL A 1  117  ? -48.215 -66.673  55.449  1.00 75.33  ?  117  VAL A CG1 1 
ATOM   927   C  CG2 . VAL A 1  117  ? -49.121 -68.931  54.853  1.00 83.05  ?  117  VAL A CG2 1 
ATOM   928   N  N   . LYS A 1  118  ? -45.188 -66.480  54.058  1.00 75.47  ?  118  LYS A N   1 
ATOM   929   C  CA  . LYS A 1  118  ? -43.962 -65.770  54.399  1.00 77.30  ?  118  LYS A CA  1 
ATOM   930   C  C   . LYS A 1  118  ? -44.100 -65.150  55.784  1.00 71.45  ?  118  LYS A C   1 
ATOM   931   O  O   . LYS A 1  118  ? -45.042 -64.393  56.041  1.00 64.18  ?  118  LYS A O   1 
ATOM   932   C  CB  . LYS A 1  118  ? -43.659 -64.696  53.355  1.00 74.84  ?  118  LYS A CB  1 
ATOM   933   C  CG  . LYS A 1  118  ? -42.179 -64.528  53.040  1.00 74.18  ?  118  LYS A CG  1 
ATOM   934   C  CD  . LYS A 1  118  ? -41.965 -63.566  51.880  1.00 81.23  ?  118  LYS A CD  1 
ATOM   935   C  CE  . LYS A 1  118  ? -40.495 -63.204  51.722  1.00 79.44  ?  118  LYS A CE  1 
ATOM   936   N  NZ  . LYS A 1  118  ? -39.613 -64.404  51.761  1.00 70.89  ?  118  LYS A NZ  1 
ATOM   937   N  N   . VAL A 1  119  ? -43.169 -65.477  56.675  1.00 59.72  ?  119  VAL A N   1 
ATOM   938   C  CA  . VAL A 1  119  ? -43.133 -64.866  58.000  1.00 61.96  ?  119  VAL A CA  1 
ATOM   939   C  C   . VAL A 1  119  ? -42.372 -63.547  57.975  1.00 60.28  ?  119  VAL A C   1 
ATOM   940   O  O   . VAL A 1  119  ? -42.865 -62.521  58.450  1.00 59.65  ?  119  VAL A O   1 
ATOM   941   C  CB  . VAL A 1  119  ? -42.524 -65.850  59.021  1.00 57.61  ?  119  VAL A CB  1 
ATOM   942   C  CG1 . VAL A 1  119  ? -42.417 -65.198  60.391  1.00 46.41  ?  119  VAL A CG1 1 
ATOM   943   C  CG2 . VAL A 1  119  ? -43.356 -67.122  59.094  1.00 52.37  ?  119  VAL A CG2 1 
ATOM   944   N  N   . TYR A 1  120  ? -41.167 -63.552  57.412  1.00 70.22  ?  120  TYR A N   1 
ATOM   945   C  CA  . TYR A 1  120  ? -40.357 -62.345  57.289  1.00 66.18  ?  120  TYR A CA  1 
ATOM   946   C  C   . TYR A 1  120  ? -40.661 -61.697  55.944  1.00 65.73  ?  120  TYR A C   1 
ATOM   947   O  O   . TYR A 1  120  ? -40.294 -62.229  54.891  1.00 63.65  ?  120  TYR A O   1 
ATOM   948   C  CB  . TYR A 1  120  ? -38.875 -62.677  57.431  1.00 65.55  ?  120  TYR A CB  1 
ATOM   949   C  CG  . TYR A 1  120  ? -38.478 -63.016  58.849  1.00 65.35  ?  120  TYR A CG  1 
ATOM   950   C  CD1 . TYR A 1  120  ? -38.700 -64.284  59.367  1.00 67.30  ?  120  TYR A CD1 1 
ATOM   951   C  CD2 . TYR A 1  120  ? -37.889 -62.065  59.672  1.00 62.78  ?  120  TYR A CD2 1 
ATOM   952   C  CE1 . TYR A 1  120  ? -38.345 -64.598  60.663  1.00 74.68  ?  120  TYR A CE1 1 
ATOM   953   C  CE2 . TYR A 1  120  ? -37.529 -62.370  60.970  1.00 68.66  ?  120  TYR A CE2 1 
ATOM   954   C  CZ  . TYR A 1  120  ? -37.759 -63.637  61.460  1.00 74.48  ?  120  TYR A CZ  1 
ATOM   955   O  OH  . TYR A 1  120  ? -37.404 -63.947  62.753  1.00 73.99  ?  120  TYR A OH  1 
ATOM   956   N  N   . ASP A 1  121  ? -41.332 -60.550  55.980  1.00 73.42  ?  121  ASP A N   1 
ATOM   957   C  CA  . ASP A 1  121  ? -41.829 -59.884  54.786  1.00 69.47  ?  121  ASP A CA  1 
ATOM   958   C  C   . ASP A 1  121  ? -41.183 -58.513  54.647  1.00 70.59  ?  121  ASP A C   1 
ATOM   959   O  O   . ASP A 1  121  ? -40.960 -57.817  55.643  1.00 83.64  ?  121  ASP A O   1 
ATOM   960   C  CB  . ASP A 1  121  ? -43.354 -59.744  54.842  1.00 75.51  ?  121  ASP A CB  1 
ATOM   961   C  CG  . ASP A 1  121  ? -43.964 -59.447  53.490  1.00 67.64  ?  121  ASP A CG  1 
ATOM   962   O  OD1 . ASP A 1  121  ? -43.222 -59.445  52.485  1.00 69.31  ?  121  ASP A OD1 1 
ATOM   963   O  OD2 . ASP A 1  121  ? -45.190 -59.215  53.434  1.00 71.79  -1 121  ASP A OD2 1 
ATOM   964   N  N   . LEU A 1  122  ? -40.889 -58.130  53.409  1.00 51.62  ?  122  LEU A N   1 
ATOM   965   C  CA  . LEU A 1  122  ? -40.289 -56.844  53.103  1.00 47.99  ?  122  LEU A CA  1 
ATOM   966   C  C   . LEU A 1  122  ? -41.095 -56.147  52.018  1.00 51.95  ?  122  LEU A C   1 
ATOM   967   O  O   . LEU A 1  122  ? -41.637 -56.801  51.122  1.00 60.04  ?  122  LEU A O   1 
ATOM   968   C  CB  . LEU A 1  122  ? -38.832 -57.004  52.644  1.00 55.24  ?  122  LEU A CB  1 
ATOM   969   C  CG  . LEU A 1  122  ? -37.801 -57.105  53.771  1.00 52.30  ?  122  LEU A CG  1 
ATOM   970   C  CD1 . LEU A 1  122  ? -36.410 -57.362  53.211  1.00 49.89  ?  122  LEU A CD1 1 
ATOM   971   C  CD2 . LEU A 1  122  ? -37.815 -55.859  54.648  1.00 53.03  ?  122  LEU A CD2 1 
ATOM   972   N  N   . PRO A 1  123  ? -41.198 -54.817  52.079  1.00 90.49  ?  123  PRO A N   1 
ATOM   973   C  CA  . PRO A 1  123  ? -42.060 -54.095  51.130  1.00 96.89  ?  123  PRO A CA  1 
ATOM   974   C  C   . PRO A 1  123  ? -41.479 -53.945  49.729  1.00 98.35  ?  123  PRO A C   1 
ATOM   975   O  O   . PRO A 1  123  ? -41.738 -52.939  49.061  1.00 108.93 ?  123  PRO A O   1 
ATOM   976   C  CB  . PRO A 1  123  ? -42.240 -52.725  51.800  1.00 85.58  ?  123  PRO A CB  1 
ATOM   977   C  CG  . PRO A 1  123  ? -41.868 -52.936  53.238  1.00 83.44  ?  123  PRO A CG  1 
ATOM   978   C  CD  . PRO A 1  123  ? -40.783 -53.960  53.200  1.00 89.99  ?  123  PRO A CD  1 
ATOM   979   N  N   . ASN A 1  124  ? -40.684 -54.918  49.281  1.00 69.51  ?  124  ASN A N   1 
ATOM   980   C  CA  . ASN A 1  124  ? -40.240 -55.027  47.891  1.00 71.39  ?  124  ASN A CA  1 
ATOM   981   C  C   . ASN A 1  124  ? -39.432 -53.841  47.367  1.00 72.25  ?  124  ASN A C   1 
ATOM   982   O  O   . ASN A 1  124  ? -38.908 -53.903  46.250  1.00 63.08  ?  124  ASN A O   1 
ATOM   983   C  CB  . ASN A 1  124  ? -41.442 -55.263  46.971  1.00 68.88  ?  124  ASN A CB  1 
ATOM   984   C  CG  . ASN A 1  124  ? -41.963 -56.683  47.051  1.00 79.95  ?  124  ASN A CG  1 
ATOM   985   O  OD1 . ASN A 1  124  ? -43.171 -56.916  47.073  1.00 86.80  ?  124  ASN A OD1 1 
ATOM   986   N  ND2 . ASN A 1  124  ? -41.047 -57.645  47.099  1.00 68.79  ?  124  ASN A ND2 1 
ATOM   987   N  N   . PHE A 1  125  ? -39.325 -52.756  48.134  1.00 68.14  ?  125  PHE A N   1 
ATOM   988   C  CA  . PHE A 1  125  ? -38.407 -51.673  47.803  1.00 61.56  ?  125  PHE A CA  1 
ATOM   989   C  C   . PHE A 1  125  ? -37.227 -51.633  48.770  1.00 67.41  ?  125  PHE A C   1 
ATOM   990   O  O   . PHE A 1  125  ? -36.630 -50.577  48.995  1.00 69.20  ?  125  PHE A O   1 
ATOM   991   C  CB  . PHE A 1  125  ? -39.122 -50.321  47.765  1.00 53.78  ?  125  PHE A CB  1 
ATOM   992   C  CG  . PHE A 1  125  ? -39.992 -50.036  48.963  1.00 62.13  ?  125  PHE A CG  1 
ATOM   993   C  CD1 . PHE A 1  125  ? -39.454 -49.954  50.238  1.00 57.41  ?  125  PHE A CD1 1 
ATOM   994   C  CD2 . PHE A 1  125  ? -41.347 -49.802  48.803  1.00 62.91  ?  125  PHE A CD2 1 
ATOM   995   C  CE1 . PHE A 1  125  ? -40.253 -49.673  51.329  1.00 48.84  ?  125  PHE A CE1 1 
ATOM   996   C  CE2 . PHE A 1  125  ? -42.152 -49.520  49.891  1.00 60.82  ?  125  PHE A CE2 1 
ATOM   997   C  CZ  . PHE A 1  125  ? -41.603 -49.453  51.155  1.00 50.59  ?  125  PHE A CZ  1 
ATOM   998   N  N   . VAL A 1  126  ? -36.887 -52.784  49.343  1.00 84.83  ?  126  VAL A N   1 
ATOM   999   C  CA  . VAL A 1  126  ? -35.869 -52.879  50.375  1.00 88.90  ?  126  VAL A CA  1 
ATOM   1000  C  C   . VAL A 1  126  ? -34.611 -53.572  49.865  1.00 86.40  ?  126  VAL A C   1 
ATOM   1001  O  O   . VAL A 1  126  ? -33.497 -53.127  50.152  1.00 94.84  ?  126  VAL A O   1 
ATOM   1002  C  CB  . VAL A 1  126  ? -36.437 -53.600  51.617  1.00 86.56  ?  126  VAL A CB  1 
ATOM   1003  C  CG1 . VAL A 1  126  ? -35.342 -53.900  52.612  1.00 76.85  ?  126  VAL A CG1 1 
ATOM   1004  C  CG2 . VAL A 1  126  ? -37.521 -52.754  52.260  1.00 90.28  ?  126  VAL A CG2 1 
ATOM   1005  N  N   . TYR A 1  127  ? -34.771 -54.660  49.108  1.00 56.52  ?  127  TYR A N   1 
ATOM   1006  C  CA  . TYR A 1  127  ? -33.662 -55.393  48.505  1.00 59.94  ?  127  TYR A CA  1 
ATOM   1007  C  C   . TYR A 1  127  ? -32.646 -55.858  49.540  1.00 54.89  ?  127  TYR A C   1 
ATOM   1008  O  O   . TYR A 1  127  ? -31.582 -55.249  49.699  1.00 56.91  ?  127  TYR A O   1 
ATOM   1009  C  CB  . TYR A 1  127  ? -32.978 -54.540  47.433  1.00 56.49  ?  127  TYR A CB  1 
ATOM   1010  C  CG  . TYR A 1  127  ? -33.885 -54.234  46.268  1.00 59.28  ?  127  TYR A CG  1 
ATOM   1011  C  CD1 . TYR A 1  127  ? -34.295 -55.240  45.405  1.00 60.50  ?  127  TYR A CD1 1 
ATOM   1012  C  CD2 . TYR A 1  127  ? -34.348 -52.947  46.043  1.00 59.53  ?  127  TYR A CD2 1 
ATOM   1013  C  CE1 . TYR A 1  127  ? -35.131 -54.972  44.344  1.00 54.49  ?  127  TYR A CE1 1 
ATOM   1014  C  CE2 . TYR A 1  127  ? -35.184 -52.668  44.984  1.00 59.76  ?  127  TYR A CE2 1 
ATOM   1015  C  CZ  . TYR A 1  127  ? -35.573 -53.685  44.138  1.00 59.25  ?  127  TYR A CZ  1 
ATOM   1016  O  OH  . TYR A 1  127  ? -36.406 -53.415  43.080  1.00 68.96  ?  127  TYR A OH  1 
ATOM   1017  N  N   . PHE A 1  128  ? -32.967 -56.938  50.242  1.00 47.03  ?  128  PHE A N   1 
ATOM   1018  C  CA  . PHE A 1  128  ? -32.054 -57.542  51.197  1.00 53.00  ?  128  PHE A CA  1 
ATOM   1019  C  C   . PHE A 1  128  ? -31.183 -58.587  50.509  1.00 57.00  ?  128  PHE A C   1 
ATOM   1020  O  O   . PHE A 1  128  ? -31.561 -59.163  49.485  1.00 61.05  ?  128  PHE A O   1 
ATOM   1021  C  CB  . PHE A 1  128  ? -32.827 -58.179  52.352  1.00 58.41  ?  128  PHE A CB  1 
ATOM   1022  C  CG  . PHE A 1  128  ? -31.947 -58.794  53.395  1.00 56.71  ?  128  PHE A CG  1 
ATOM   1023  C  CD1 . PHE A 1  128  ? -31.277 -57.999  54.310  1.00 53.74  ?  128  PHE A CD1 1 
ATOM   1024  C  CD2 . PHE A 1  128  ? -31.775 -60.166  53.450  1.00 52.29  ?  128  PHE A CD2 1 
ATOM   1025  C  CE1 . PHE A 1  128  ? -30.460 -58.563  55.266  1.00 51.74  ?  128  PHE A CE1 1 
ATOM   1026  C  CE2 . PHE A 1  128  ? -30.960 -60.734  54.402  1.00 54.68  ?  128  PHE A CE2 1 
ATOM   1027  C  CZ  . PHE A 1  128  ? -30.301 -59.933  55.309  1.00 54.95  ?  128  PHE A CZ  1 
ATOM   1028  N  N   . ASN A 1  129  ? -30.006 -58.828  51.085  1.00 63.97  ?  129  ASN A N   1 
ATOM   1029  C  CA  . ASN A 1  129  ? -29.029 -59.761  50.530  1.00 58.43  ?  129  ASN A CA  1 
ATOM   1030  C  C   . ASN A 1  129  ? -28.492 -60.640  51.653  1.00 57.14  ?  129  ASN A C   1 
ATOM   1031  O  O   . ASN A 1  129  ? -27.778 -60.155  52.537  1.00 60.88  ?  129  ASN A O   1 
ATOM   1032  C  CB  . ASN A 1  129  ? -27.896 -59.009  49.831  1.00 61.33  ?  129  ASN A CB  1 
ATOM   1033  C  CG  . ASN A 1  129  ? -27.121 -59.883  48.867  1.00 59.36  ?  129  ASN A CG  1 
ATOM   1034  O  OD1 . ASN A 1  129  ? -26.714 -60.993  49.208  1.00 66.37  ?  129  ASN A OD1 1 
ATOM   1035  N  ND2 . ASN A 1  129  ? -26.914 -59.387  47.653  1.00 52.86  ?  129  ASN A ND2 1 
ATOM   1036  N  N   . HIS A 1  130  ? -28.828 -61.935  51.613  1.00 41.03  ?  130  HIS A N   1 
ATOM   1037  C  CA  . HIS A 1  130  ? -28.356 -62.857  52.643  1.00 39.54  ?  130  HIS A CA  1 
ATOM   1038  C  C   . HIS A 1  130  ? -26.867 -63.158  52.512  1.00 36.61  ?  130  HIS A C   1 
ATOM   1039  O  O   . HIS A 1  130  ? -26.202 -63.419  53.521  1.00 40.09  ?  130  HIS A O   1 
ATOM   1040  C  CB  . HIS A 1  130  ? -29.142 -64.168  52.596  1.00 42.58  ?  130  HIS A CB  1 
ATOM   1041  C  CG  . HIS A 1  130  ? -30.475 -64.109  53.276  1.00 45.83  ?  130  HIS A CG  1 
ATOM   1042  N  ND1 . HIS A 1  130  ? -31.627 -63.716  52.630  1.00 50.66  ?  130  HIS A ND1 1 
ATOM   1043  C  CD2 . HIS A 1  130  ? -30.838 -64.406  54.547  1.00 50.47  ?  130  HIS A CD2 1 
ATOM   1044  C  CE1 . HIS A 1  130  ? -32.643 -63.770  53.474  1.00 61.66  ?  130  HIS A CE1 1 
ATOM   1045  N  NE2 . HIS A 1  130  ? -32.191 -64.185  54.644  1.00 58.21  ?  130  HIS A NE2 1 
ATOM   1046  N  N   . SER A 1  131  ? -26.330 -63.138  51.291  1.00 49.58  ?  131  SER A N   1 
ATOM   1047  C  CA  . SER A 1  131  ? -24.958 -63.592  51.077  1.00 48.24  ?  131  SER A CA  1 
ATOM   1048  C  C   . SER A 1  131  ? -23.951 -62.653  51.731  1.00 53.16  ?  131  SER A C   1 
ATOM   1049  O  O   . SER A 1  131  ? -23.018 -63.102  52.407  1.00 51.31  ?  131  SER A O   1 
ATOM   1050  C  CB  . SER A 1  131  ? -24.679 -63.726  49.581  1.00 46.69  ?  131  SER A CB  1 
ATOM   1051  O  OG  . SER A 1  131  ? -23.329 -64.089  49.346  1.00 49.32  ?  131  SER A OG  1 
ATOM   1052  N  N   . ILE A 1  132  ? -24.123 -61.342  51.541  1.00 66.67  ?  132  ILE A N   1 
ATOM   1053  C  CA  . ILE A 1  132  ? -23.155 -60.394  52.083  1.00 64.62  ?  132  ILE A CA  1 
ATOM   1054  C  C   . ILE A 1  132  ? -23.214 -60.367  53.606  1.00 62.39  ?  132  ILE A C   1 
ATOM   1055  O  O   . ILE A 1  132  ? -22.183 -60.199  54.269  1.00 65.85  ?  132  ILE A O   1 
ATOM   1056  C  CB  . ILE A 1  132  ? -23.376 -58.995  51.473  1.00 60.47  ?  132  ILE A CB  1 
ATOM   1057  C  CG1 . ILE A 1  132  ? -22.422 -57.970  52.095  1.00 59.18  ?  132  ILE A CG1 1 
ATOM   1058  C  CG2 . ILE A 1  132  ? -24.821 -58.556  51.639  1.00 62.23  ?  132  ILE A CG2 1 
ATOM   1059  C  CD1 . ILE A 1  132  ? -20.972 -58.171  51.708  1.00 58.22  ?  132  ILE A CD1 1 
ATOM   1060  N  N   . HIS A 1  133  ? -24.402 -60.550  54.190  1.00 33.78  ?  133  HIS A N   1 
ATOM   1061  C  CA  . HIS A 1  133  ? -24.507 -60.537  55.646  1.00 30.76  ?  133  HIS A CA  1 
ATOM   1062  C  C   . HIS A 1  133  ? -23.861 -61.773  56.259  1.00 40.41  ?  133  HIS A C   1 
ATOM   1063  O  O   . HIS A 1  133  ? -23.140 -61.671  57.258  1.00 36.60  ?  133  HIS A O   1 
ATOM   1064  C  CB  . HIS A 1  133  ? -25.972 -60.420  56.076  1.00 30.54  ?  133  HIS A CB  1 
ATOM   1065  C  CG  . HIS A 1  133  ? -26.530 -59.036  55.950  1.00 35.03  ?  133  HIS A CG  1 
ATOM   1066  N  ND1 . HIS A 1  133  ? -26.584 -58.361  54.750  1.00 41.18  ?  133  HIS A ND1 1 
ATOM   1067  C  CD2 . HIS A 1  133  ? -27.028 -58.187  56.881  1.00 45.05  ?  133  HIS A CD2 1 
ATOM   1068  C  CE1 . HIS A 1  133  ? -27.111 -57.165  54.944  1.00 42.81  ?  133  HIS A CE1 1 
ATOM   1069  N  NE2 . HIS A 1  133  ? -27.384 -57.032  56.229  1.00 37.38  ?  133  HIS A NE2 1 
ATOM   1070  N  N   . VAL A 1  134  ? -24.092 -62.946  55.665  1.00 55.19  ?  134  VAL A N   1 
ATOM   1071  C  CA  . VAL A 1  134  ? -23.530 -64.178  56.210  1.00 47.39  ?  134  VAL A CA  1 
ATOM   1072  C  C   . VAL A 1  134  ? -22.012 -64.187  56.069  1.00 49.55  ?  134  VAL A C   1 
ATOM   1073  O  O   . VAL A 1  134  ? -21.291 -64.562  57.001  1.00 44.09  ?  134  VAL A O   1 
ATOM   1074  C  CB  . VAL A 1  134  ? -24.175 -65.402  55.533  1.00 46.31  ?  134  VAL A CB  1 
ATOM   1075  C  CG1 . VAL A 1  134  ? -23.289 -66.634  55.673  1.00 60.08  ?  134  VAL A CG1 1 
ATOM   1076  C  CG2 . VAL A 1  134  ? -25.552 -65.667  56.123  1.00 44.09  ?  134  VAL A CG2 1 
ATOM   1077  N  N   . ASN A 1  135  ? -21.499 -63.766  54.911  1.00 64.57  ?  135  ASN A N   1 
ATOM   1078  C  CA  . ASN A 1  135  ? -20.060 -63.782  54.674  1.00 63.00  ?  135  ASN A CA  1 
ATOM   1079  C  C   . ASN A 1  135  ? -19.303 -62.747  55.499  1.00 54.24  ?  135  ASN A C   1 
ATOM   1080  O  O   . ASN A 1  135  ? -18.072 -62.826  55.572  1.00 51.30  ?  135  ASN A O   1 
ATOM   1081  C  CB  . ASN A 1  135  ? -19.772 -63.567  53.187  1.00 62.29  ?  135  ASN A CB  1 
ATOM   1082  C  CG  . ASN A 1  135  ? -19.960 -64.829  52.372  1.00 52.54  ?  135  ASN A CG  1 
ATOM   1083  O  OD1 . ASN A 1  135  ? -19.206 -65.790  52.517  1.00 41.32  ?  135  ASN A OD1 1 
ATOM   1084  N  ND2 . ASN A 1  135  ? -20.975 -64.837  51.515  1.00 59.39  ?  135  ASN A ND2 1 
ATOM   1085  N  N   . LYS A 1  136  ? -19.994 -61.788  56.115  1.00 37.55  ?  136  LYS A N   1 
ATOM   1086  C  CA  . LYS A 1  136  ? -19.351 -60.767  56.933  1.00 42.18  ?  136  LYS A CA  1 
ATOM   1087  C  C   . LYS A 1  136  ? -19.518 -61.021  58.428  1.00 47.64  ?  136  LYS A C   1 
ATOM   1088  O  O   . LYS A 1  136  ? -19.378 -60.090  59.228  1.00 50.81  ?  136  LYS A O   1 
ATOM   1089  C  CB  . LYS A 1  136  ? -19.886 -59.382  56.567  1.00 52.70  ?  136  LYS A CB  1 
ATOM   1090  C  CG  . LYS A 1  136  ? -19.418 -58.870  55.212  1.00 43.58  ?  136  LYS A CG  1 
ATOM   1091  C  CD  . LYS A 1  136  ? -18.031 -58.260  55.309  1.00 36.30  ?  136  LYS A CD  1 
ATOM   1092  C  CE  . LYS A 1  136  ? -17.500 -57.865  53.942  1.00 35.12  ?  136  LYS A CE  1 
ATOM   1093  N  NZ  . LYS A 1  136  ? -16.481 -56.781  54.032  1.00 37.88  ?  136  LYS A NZ  1 
ATOM   1094  N  N   . GLY A 1  137  ? -19.814 -62.258  58.819  1.00 44.86  ?  137  GLY A N   1 
ATOM   1095  C  CA  . GLY A 1  137  ? -19.888 -62.610  60.222  1.00 44.69  ?  137  GLY A CA  1 
ATOM   1096  C  C   . GLY A 1  137  ? -21.150 -62.158  60.927  1.00 49.61  ?  137  GLY A C   1 
ATOM   1097  O  O   . GLY A 1  137  ? -21.082 -61.517  61.980  1.00 49.92  ?  137  GLY A O   1 
ATOM   1098  N  N   . ILE A 1  138  ? -22.306 -62.488  60.359  1.00 77.88  ?  138  ILE A N   1 
ATOM   1099  C  CA  . ILE A 1  138  ? -23.601 -62.185  60.958  1.00 70.12  ?  138  ILE A CA  1 
ATOM   1100  C  C   . ILE A 1  138  ? -24.420 -63.465  60.951  1.00 74.63  ?  138  ILE A C   1 
ATOM   1101  O  O   . ILE A 1  138  ? -24.639 -64.058  59.889  1.00 80.91  ?  138  ILE A O   1 
ATOM   1102  C  CB  . ILE A 1  138  ? -24.341 -61.064  60.212  1.00 67.35  ?  138  ILE A CB  1 
ATOM   1103  C  CG1 . ILE A 1  138  ? -23.491 -59.793  60.179  1.00 66.94  ?  138  ILE A CG1 1 
ATOM   1104  C  CG2 . ILE A 1  138  ? -25.686 -60.798  60.862  1.00 68.06  ?  138  ILE A CG2 1 
ATOM   1105  C  CD1 . ILE A 1  138  ? -23.411 -59.078  61.503  1.00 66.65  ?  138  ILE A CD1 1 
ATOM   1106  N  N   . GLY A 1  139  ? -24.870 -63.890  62.127  1.00 67.13  ?  139  GLY A N   1 
ATOM   1107  C  CA  . GLY A 1  139  ? -25.576 -65.144  62.246  1.00 67.96  ?  139  GLY A CA  1 
ATOM   1108  C  C   . GLY A 1  139  ? -27.082 -64.999  62.209  1.00 68.88  ?  139  GLY A C   1 
ATOM   1109  O  O   . GLY A 1  139  ? -27.629 -63.908  62.357  1.00 70.12  ?  139  GLY A O   1 
ATOM   1110  N  N   . CYS A 1  140  ? -27.756 -66.134  62.001  1.00 65.67  ?  140  CYS A N   1 
ATOM   1111  C  CA  . CYS A 1  140  ? -29.215 -66.149  62.008  1.00 67.54  ?  140  CYS A CA  1 
ATOM   1112  C  C   . CYS A 1  140  ? -29.791 -65.881  63.391  1.00 77.09  ?  140  CYS A C   1 
ATOM   1113  O  O   . CYS A 1  140  ? -30.955 -65.479  63.496  1.00 75.15  ?  140  CYS A O   1 
ATOM   1114  C  CB  . CYS A 1  140  ? -29.731 -67.493  61.493  1.00 64.17  ?  140  CYS A CB  1 
ATOM   1115  S  SG  . CYS A 1  140  ? -28.858 -68.130  60.054  1.00 66.89  ?  140  CYS A SG  1 
ATOM   1116  N  N   . SER A 1  141  ? -29.008 -66.103  64.448  1.00 98.93  ?  141  SER A N   1 
ATOM   1117  C  CA  . SER A 1  141  ? -29.499 -65.858  65.800  1.00 87.75  ?  141  SER A CA  1 
ATOM   1118  C  C   . SER A 1  141  ? -29.784 -64.378  66.025  1.00 96.20  ?  141  SER A C   1 
ATOM   1119  O  O   . SER A 1  141  ? -30.779 -64.022  66.668  1.00 97.40  ?  141  SER A O   1 
ATOM   1120  C  CB  . SER A 1  141  ? -28.487 -66.373  66.823  1.00 99.18  ?  141  SER A CB  1 
ATOM   1121  O  OG  . SER A 1  141  ? -28.924 -66.123  68.148  1.00 118.83 ?  141  SER A OG  1 
ATOM   1122  N  N   . THR A 1  142  ? -28.927 -63.501  65.498  1.00 68.05  ?  142  THR A N   1 
ATOM   1123  C  CA  . THR A 1  142  ? -29.115 -62.065  65.667  1.00 64.07  ?  142  THR A CA  1 
ATOM   1124  C  C   . THR A 1  142  ? -30.240 -61.510  64.804  1.00 64.31  ?  142  THR A C   1 
ATOM   1125  O  O   . THR A 1  142  ? -30.616 -60.346  64.982  1.00 71.26  ?  142  THR A O   1 
ATOM   1126  C  CB  . THR A 1  142  ? -27.817 -61.318  65.347  1.00 50.34  ?  142  THR A CB  1 
ATOM   1127  O  OG1 . THR A 1  142  ? -27.570 -61.367  63.937  1.00 54.82  ?  142  THR A OG1 1 
ATOM   1128  C  CG2 . THR A 1  142  ? -26.643 -61.947  66.080  1.00 54.91  ?  142  THR A CG2 1 
ATOM   1129  N  N   . CYS A 1  143  ? -30.786 -62.307  63.883  1.00 53.63  ?  143  CYS A N   1 
ATOM   1130  C  CA  . CYS A 1  143  ? -31.819 -61.834  62.965  1.00 60.62  ?  143  CYS A CA  1 
ATOM   1131  C  C   . CYS A 1  143  ? -33.109 -62.625  63.141  1.00 56.63  ?  143  CYS A C   1 
ATOM   1132  O  O   . CYS A 1  143  ? -34.122 -62.052  63.549  1.00 55.97  ?  143  CYS A O   1 
ATOM   1133  C  CB  . CYS A 1  143  ? -31.310 -61.909  61.525  1.00 68.01  ?  143  CYS A CB  1 
ATOM   1134  S  SG  . CYS A 1  143  ? -30.264 -60.523  61.033  1.00 56.20  ?  143  CYS A SG  1 
ATOM   1135  N  N   . HIS A 1  144  ? -33.105 -63.922  62.844  1.00 66.04  ?  144  HIS A N   1 
ATOM   1136  C  CA  . HIS A 1  144  ? -34.293 -64.755  62.950  1.00 72.04  ?  144  HIS A CA  1 
ATOM   1137  C  C   . HIS A 1  144  ? -34.469 -65.373  64.331  1.00 70.13  ?  144  HIS A C   1 
ATOM   1138  O  O   . HIS A 1  144  ? -35.484 -66.035  64.571  1.00 69.28  ?  144  HIS A O   1 
ATOM   1139  C  CB  . HIS A 1  144  ? -34.244 -65.867  61.897  1.00 67.48  ?  144  HIS A CB  1 
ATOM   1140  C  CG  . HIS A 1  144  ? -34.188 -65.366  60.488  1.00 58.81  ?  144  HIS A CG  1 
ATOM   1141  N  ND1 . HIS A 1  144  ? -35.014 -64.366  60.021  1.00 61.61  ?  144  HIS A ND1 1 
ATOM   1142  C  CD2 . HIS A 1  144  ? -33.403 -65.724  59.444  1.00 70.66  ?  144  HIS A CD2 1 
ATOM   1143  C  CE1 . HIS A 1  144  ? -34.743 -64.132  58.749  1.00 82.07  ?  144  HIS A CE1 1 
ATOM   1144  N  NE2 . HIS A 1  144  ? -33.768 -64.942  58.375  1.00 81.01  ?  144  HIS A NE2 1 
ATOM   1145  N  N   . GLY A 1  145  ? -33.510 -65.182  65.233  1.00 50.12  ?  145  GLY A N   1 
ATOM   1146  C  CA  . GLY A 1  145  ? -33.618 -65.735  66.566  1.00 59.92  ?  145  GLY A CA  1 
ATOM   1147  C  C   . GLY A 1  145  ? -33.188 -67.190  66.626  1.00 53.01  ?  145  GLY A C   1 
ATOM   1148  O  O   . GLY A 1  145  ? -32.413 -67.686  65.801  1.00 43.08  ?  145  GLY A O   1 
ATOM   1149  N  N   . GLN A 1  146  ? -33.709 -67.882  67.639  1.00 75.59  ?  146  GLN A N   1 
ATOM   1150  C  CA  . GLN A 1  146  ? -33.411 -69.298  67.854  1.00 74.19  ?  146  GLN A CA  1 
ATOM   1151  C  C   . GLN A 1  146  ? -34.413 -70.150  67.073  1.00 76.87  ?  146  GLN A C   1 
ATOM   1152  O  O   . GLN A 1  146  ? -35.329 -70.765  67.620  1.00 77.92  ?  146  GLN A O   1 
ATOM   1153  C  CB  . GLN A 1  146  ? -33.430 -69.623  69.342  1.00 69.54  ?  146  GLN A CB  1 
ATOM   1154  C  CG  . GLN A 1  146  ? -32.357 -68.911  70.149  1.00 76.05  ?  146  GLN A CG  1 
ATOM   1155  C  CD  . GLN A 1  146  ? -30.962 -69.415  69.837  1.00 86.00  ?  146  GLN A CD  1 
ATOM   1156  O  OE1 . GLN A 1  146  ? -30.768 -70.596  69.549  1.00 90.44  ?  146  GLN A OE1 1 
ATOM   1157  N  NE2 . GLN A 1  146  ? -29.980 -68.522  69.895  1.00 89.83  ?  146  GLN A NE2 1 
ATOM   1158  N  N   . VAL A 1  147  ? -34.215 -70.171  65.753  1.00 82.79  ?  147  VAL A N   1 
ATOM   1159  C  CA  . VAL A 1  147  ? -35.124 -70.899  64.872  1.00 85.14  ?  147  VAL A CA  1 
ATOM   1160  C  C   . VAL A 1  147  ? -35.035 -72.398  65.116  1.00 85.98  ?  147  VAL A C   1 
ATOM   1161  O  O   . VAL A 1  147  ? -35.992 -73.136  64.850  1.00 86.86  ?  147  VAL A O   1 
ATOM   1162  C  CB  . VAL A 1  147  ? -34.827 -70.551  63.402  1.00 85.41  ?  147  VAL A CB  1 
ATOM   1163  C  CG1 . VAL A 1  147  ? -35.927 -71.078  62.488  1.00 79.66  ?  147  VAL A CG1 1 
ATOM   1164  C  CG2 . VAL A 1  147  ? -34.667 -69.055  63.245  1.00 89.91  ?  147  VAL A CG2 1 
ATOM   1165  N  N   . ASN A 1  148  ? -33.899 -72.873  65.629  1.00 71.05  ?  148  ASN A N   1 
ATOM   1166  C  CA  . ASN A 1  148  ? -33.717 -74.300  65.853  1.00 70.05  ?  148  ASN A CA  1 
ATOM   1167  C  C   . ASN A 1  148  ? -34.694 -74.862  66.876  1.00 83.26  ?  148  ASN A C   1 
ATOM   1168  O  O   . ASN A 1  148  ? -34.892 -76.081  66.920  1.00 91.64  ?  148  ASN A O   1 
ATOM   1169  C  CB  . ASN A 1  148  ? -32.280 -74.575  66.297  1.00 74.34  ?  148  ASN A CB  1 
ATOM   1170  C  CG  . ASN A 1  148  ? -31.822 -73.640  67.398  1.00 79.99  ?  148  ASN A CG  1 
ATOM   1171  O  OD1 . ASN A 1  148  ? -31.627 -72.446  67.171  1.00 74.67  ?  148  ASN A OD1 1 
ATOM   1172  N  ND2 . ASN A 1  148  ? -31.642 -74.180  68.598  1.00 88.26  ?  148  ASN A ND2 1 
ATOM   1173  N  N   . ASN A 1  149  ? -35.313 -74.009  67.695  1.00 71.48  ?  149  ASN A N   1 
ATOM   1174  C  CA  . ASN A 1  149  ? -36.221 -74.458  68.745  1.00 73.43  ?  149  ASN A CA  1 
ATOM   1175  C  C   . ASN A 1  149  ? -37.651 -73.978  68.523  1.00 68.84  ?  149  ASN A C   1 
ATOM   1176  O  O   . ASN A 1  149  ? -38.431 -73.907  69.478  1.00 75.37  ?  149  ASN A O   1 
ATOM   1177  C  CB  . ASN A 1  149  ? -35.720 -74.001  70.116  1.00 75.45  ?  149  ASN A CB  1 
ATOM   1178  C  CG  . ASN A 1  149  ? -36.035 -74.998  71.212  1.00 78.65  ?  149  ASN A CG  1 
ATOM   1179  O  OD1 . ASN A 1  149  ? -35.738 -76.186  71.090  1.00 77.36  ?  149  ASN A OD1 1 
ATOM   1180  N  ND2 . ASN A 1  149  ? -36.644 -74.519  72.290  1.00 80.36  ?  149  ASN A ND2 1 
ATOM   1181  N  N   . MET A 1  150  ? -38.019 -73.651  67.285  1.00 84.19  ?  150  MET A N   1 
ATOM   1182  C  CA  . MET A 1  150  ? -39.359 -73.165  67.001  1.00 89.43  ?  150  MET A CA  1 
ATOM   1183  C  C   . MET A 1  150  ? -40.180 -74.273  66.364  1.00 94.38  ?  150  MET A C   1 
ATOM   1184  O  O   . MET A 1  150  ? -39.907 -74.646  65.213  1.00 88.57  ?  150  MET A O   1 
ATOM   1185  C  CB  . MET A 1  150  ? -39.310 -71.949  66.078  1.00 88.13  ?  150  MET A CB  1 
ATOM   1186  C  CG  . MET A 1  150  ? -38.375 -70.843  66.524  1.00 87.77  ?  150  MET A CG  1 
ATOM   1187  S  SD  . MET A 1  150  ? -38.349 -69.475  65.347  1.00 85.37  ?  150  MET A SD  1 
ATOM   1188  C  CE  . MET A 1  150  ? -38.101 -68.082  66.442  1.00 88.33  ?  150  MET A CE  1 
ATOM   1189  N  N   . PRO A 1  151  ? -41.177 -74.832  67.054  1.00 99.26  ?  151  PRO A N   1 
ATOM   1190  C  CA  . PRO A 1  151  ? -42.107 -75.740  66.363  1.00 88.81  ?  151  PRO A CA  1 
ATOM   1191  C  C   . PRO A 1  151  ? -42.892 -75.037  65.272  1.00 80.86  ?  151  PRO A C   1 
ATOM   1192  O  O   . PRO A 1  151  ? -43.183 -75.639  64.232  1.00 88.58  ?  151  PRO A O   1 
ATOM   1193  C  CB  . PRO A 1  151  ? -43.017 -76.244  67.493  1.00 92.12  ?  151  PRO A CB  1 
ATOM   1194  C  CG  . PRO A 1  151  ? -42.873 -75.235  68.589  1.00 97.17  ?  151  PRO A CG  1 
ATOM   1195  C  CD  . PRO A 1  151  ? -41.478 -74.706  68.489  1.00 97.31  ?  151  PRO A CD  1 
ATOM   1196  N  N   . VAL A 1  152  ? -43.249 -73.772  65.491  1.00 56.08  ?  152  VAL A N   1 
ATOM   1197  C  CA  . VAL A 1  152  ? -43.839 -72.911  64.473  1.00 58.53  ?  152  VAL A CA  1 
ATOM   1198  C  C   . VAL A 1  152  ? -43.031 -71.622  64.431  1.00 67.22  ?  152  VAL A C   1 
ATOM   1199  O  O   . VAL A 1  152  ? -42.767 -71.017  65.476  1.00 57.14  ?  152  VAL A O   1 
ATOM   1200  C  CB  . VAL A 1  152  ? -45.324 -72.609  64.753  1.00 46.03  ?  152  VAL A CB  1 
ATOM   1201  C  CG1 . VAL A 1  152  ? -45.948 -71.909  63.561  1.00 58.27  ?  152  VAL A CG1 1 
ATOM   1202  C  CG2 . VAL A 1  152  ? -46.082 -73.887  65.076  1.00 43.34  ?  152  VAL A CG2 1 
ATOM   1203  N  N   . VAL A 1  153  ? -42.642 -71.204  63.230  1.00 78.43  ?  153  VAL A N   1 
ATOM   1204  C  CA  . VAL A 1  153  ? -41.760 -70.053  63.070  1.00 66.08  ?  153  VAL A CA  1 
ATOM   1205  C  C   . VAL A 1  153  ? -42.557 -68.770  63.265  1.00 58.40  ?  153  VAL A C   1 
ATOM   1206  O  O   . VAL A 1  153  ? -43.661 -68.620  62.728  1.00 63.31  ?  153  VAL A O   1 
ATOM   1207  C  CB  . VAL A 1  153  ? -41.079 -70.080  61.692  1.00 57.32  ?  153  VAL A CB  1 
ATOM   1208  C  CG1 . VAL A 1  153  ? -40.122 -68.905  61.547  1.00 48.94  ?  153  VAL A CG1 1 
ATOM   1209  C  CG2 . VAL A 1  153  ? -40.351 -71.400  61.488  1.00 59.85  ?  153  VAL A CG2 1 
ATOM   1210  N  N   . TRP A 1  154  ? -41.996 -67.840  64.037  1.00 60.69  ?  154  TRP A N   1 
ATOM   1211  C  CA  . TRP A 1  154  ? -42.584 -66.526  64.247  1.00 61.45  ?  154  TRP A CA  1 
ATOM   1212  C  C   . TRP A 1  154  ? -41.537 -65.455  63.975  1.00 61.19  ?  154  TRP A C   1 
ATOM   1213  O  O   . TRP A 1  154  ? -40.331 -65.711  64.011  1.00 57.74  ?  154  TRP A O   1 
ATOM   1214  C  CB  . TRP A 1  154  ? -43.140 -66.373  65.672  1.00 56.49  ?  154  TRP A CB  1 
ATOM   1215  C  CG  . TRP A 1  154  ? -42.089 -66.371  66.743  1.00 65.47  ?  154  TRP A CG  1 
ATOM   1216  C  CD1 . TRP A 1  154  ? -41.303 -65.319  67.123  1.00 70.55  ?  154  TRP A CD1 1 
ATOM   1217  C  CD2 . TRP A 1  154  ? -41.714 -67.472  67.581  1.00 65.84  ?  154  TRP A CD2 1 
ATOM   1218  N  NE1 . TRP A 1  154  ? -40.461 -65.699  68.139  1.00 70.17  ?  154  TRP A NE1 1 
ATOM   1219  C  CE2 . TRP A 1  154  ? -40.694 -67.015  68.440  1.00 63.58  ?  154  TRP A CE2 1 
ATOM   1220  C  CE3 . TRP A 1  154  ? -42.141 -68.799  67.687  1.00 58.14  ?  154  TRP A CE3 1 
ATOM   1221  C  CZ2 . TRP A 1  154  ? -40.095 -67.838  69.390  1.00 58.52  ?  154  TRP A CZ2 1 
ATOM   1222  C  CZ3 . TRP A 1  154  ? -41.545 -69.614  68.631  1.00 60.17  ?  154  TRP A CZ3 1 
ATOM   1223  C  CH2 . TRP A 1  154  ? -40.533 -69.132  69.469  1.00 63.88  ?  154  TRP A CH2 1 
ATOM   1224  N  N   . GLN A 1  155  ? -42.014 -64.243  63.701  1.00 76.57  ?  155  GLN A N   1 
ATOM   1225  C  CA  . GLN A 1  155  ? -41.128 -63.115  63.443  1.00 78.06  ?  155  GLN A CA  1 
ATOM   1226  C  C   . GLN A 1  155  ? -40.582 -62.596  64.768  1.00 75.29  ?  155  GLN A C   1 
ATOM   1227  O  O   . GLN A 1  155  ? -41.344 -62.116  65.614  1.00 77.56  ?  155  GLN A O   1 
ATOM   1228  C  CB  . GLN A 1  155  ? -41.870 -62.016  62.686  1.00 82.56  ?  155  GLN A CB  1 
ATOM   1229  C  CG  . GLN A 1  155  ? -40.975 -60.910  62.154  1.00 80.87  ?  155  GLN A CG  1 
ATOM   1230  C  CD  . GLN A 1  155  ? -41.616 -60.141  61.014  1.00 86.26  ?  155  GLN A CD  1 
ATOM   1231  O  OE1 . GLN A 1  155  ? -42.661 -60.536  60.497  1.00 90.57  ?  155  GLN A OE1 1 
ATOM   1232  N  NE2 . GLN A 1  155  ? -40.989 -59.042  60.613  1.00 80.37  ?  155  GLN A NE2 1 
ATOM   1233  N  N   . GLN A 1  156  ? -39.261 -62.694  64.946  1.00 64.31  ?  156  GLN A N   1 
ATOM   1234  C  CA  . GLN A 1  156  ? -38.654 -62.364  66.233  1.00 74.77  ?  156  GLN A CA  1 
ATOM   1235  C  C   . GLN A 1  156  ? -38.795 -60.881  66.556  1.00 72.65  ?  156  GLN A C   1 
ATOM   1236  O  O   . GLN A 1  156  ? -38.994 -60.510  67.719  1.00 69.83  ?  156  GLN A O   1 
ATOM   1237  C  CB  . GLN A 1  156  ? -37.184 -62.785  66.236  1.00 69.56  ?  156  GLN A CB  1 
ATOM   1238  C  CG  . GLN A 1  156  ? -36.573 -62.939  67.619  1.00 68.69  ?  156  GLN A CG  1 
ATOM   1239  C  CD  . GLN A 1  156  ? -35.067 -62.757  67.611  1.00 69.58  ?  156  GLN A CD  1 
ATOM   1240  O  OE1 . GLN A 1  156  ? -34.504 -62.169  66.687  1.00 70.53  ?  156  GLN A OE1 1 
ATOM   1241  N  NE2 . GLN A 1  156  ? -34.405 -63.272  68.640  1.00 71.28  ?  156  GLN A NE2 1 
ATOM   1242  N  N   . GLN A 1  157  ? -38.694 -60.021  65.546  1.00 80.45  ?  157  GLN A N   1 
ATOM   1243  C  CA  . GLN A 1  157  ? -38.901 -58.591  65.726  1.00 76.84  ?  157  GLN A CA  1 
ATOM   1244  C  C   . GLN A 1  157  ? -39.243 -57.983  64.376  1.00 73.28  ?  157  GLN A C   1 
ATOM   1245  O  O   . GLN A 1  157  ? -38.930 -58.548  63.324  1.00 83.89  ?  157  GLN A O   1 
ATOM   1246  C  CB  . GLN A 1  157  ? -37.671 -57.908  66.334  1.00 78.07  ?  157  GLN A CB  1 
ATOM   1247  C  CG  . GLN A 1  157  ? -36.564 -57.611  65.337  1.00 74.50  ?  157  GLN A CG  1 
ATOM   1248  C  CD  . GLN A 1  157  ? -35.672 -58.810  65.082  1.00 76.90  ?  157  GLN A CD  1 
ATOM   1249  O  OE1 . GLN A 1  157  ? -36.044 -59.948  65.362  1.00 79.80  ?  157  GLN A OE1 1 
ATOM   1250  N  NE2 . GLN A 1  157  ? -34.484 -58.559  64.550  1.00 73.51  ?  157  GLN A NE2 1 
ATOM   1251  N  N   . ALA A 1  158  ? -39.893 -56.825  64.418  1.00 51.87  ?  158  ALA A N   1 
ATOM   1252  C  CA  . ALA A 1  158  ? -40.319 -56.171  63.190  1.00 63.14  ?  158  ALA A CA  1 
ATOM   1253  C  C   . ALA A 1  158  ? -39.118 -55.627  62.426  1.00 60.10  ?  158  ALA A C   1 
ATOM   1254  O  O   . ALA A 1  158  ? -38.165 -55.113  63.018  1.00 52.72  ?  158  ALA A O   1 
ATOM   1255  C  CB  . ALA A 1  158  ? -41.302 -55.046  63.499  1.00 60.51  ?  158  ALA A CB  1 
ATOM   1256  N  N   . LEU A 1  159  ? -39.174 -55.740  61.100  1.00 78.28  ?  159  LEU A N   1 
ATOM   1257  C  CA  . LEU A 1  159  ? -38.069 -55.324  60.235  1.00 71.90  ?  159  LEU A CA  1 
ATOM   1258  C  C   . LEU A 1  159  ? -38.203 -53.837  59.900  1.00 66.78  ?  159  LEU A C   1 
ATOM   1259  O  O   . LEU A 1  159  ? -38.512 -53.434  58.777  1.00 61.89  ?  159  LEU A O   1 
ATOM   1260  C  CB  . LEU A 1  159  ? -38.026 -56.186  58.980  1.00 66.71  ?  159  LEU A CB  1 
ATOM   1261  C  CG  . LEU A 1  159  ? -38.141 -57.694  59.218  1.00 59.20  ?  159  LEU A CG  1 
ATOM   1262  C  CD1 . LEU A 1  159  ? -38.463 -58.423  57.926  1.00 69.00  ?  159  LEU A CD1 1 
ATOM   1263  C  CD2 . LEU A 1  159  ? -36.860 -58.234  59.832  1.00 52.42  ?  159  LEU A CD2 1 
ATOM   1264  N  N   . TYR A 1  160  ? -37.954 -53.015  60.918  1.00 65.14  ?  160  TYR A N   1 
ATOM   1265  C  CA  . TYR A 1  160  ? -37.961 -51.570  60.750  1.00 61.11  ?  160  TYR A CA  1 
ATOM   1266  C  C   . TYR A 1  160  ? -36.710 -51.118  59.998  1.00 59.66  ?  160  TYR A C   1 
ATOM   1267  O  O   . TYR A 1  160  ? -35.770 -51.886  59.775  1.00 61.31  ?  160  TYR A O   1 
ATOM   1268  C  CB  . TYR A 1  160  ? -38.029 -50.869  62.106  1.00 66.89  ?  160  TYR A CB  1 
ATOM   1269  C  CG  . TYR A 1  160  ? -39.235 -51.219  62.946  1.00 68.15  ?  160  TYR A CG  1 
ATOM   1270  C  CD1 . TYR A 1  160  ? -40.523 -51.023  62.467  1.00 66.65  ?  160  TYR A CD1 1 
ATOM   1271  C  CD2 . TYR A 1  160  ? -39.083 -51.729  64.229  1.00 75.82  ?  160  TYR A CD2 1 
ATOM   1272  C  CE1 . TYR A 1  160  ? -41.625 -51.336  63.237  1.00 73.32  ?  160  TYR A CE1 1 
ATOM   1273  C  CE2 . TYR A 1  160  ? -40.178 -52.044  65.007  1.00 74.53  ?  160  TYR A CE2 1 
ATOM   1274  C  CZ  . TYR A 1  160  ? -41.447 -51.844  64.507  1.00 74.71  ?  160  TYR A CZ  1 
ATOM   1275  O  OH  . TYR A 1  160  ? -42.544 -52.159  65.277  1.00 80.02  ?  160  TYR A OH  1 
ATOM   1276  N  N   . MET A 1  161  ? -36.703 -49.842  59.604  1.00 57.17  ?  161  MET A N   1 
ATOM   1277  C  CA  . MET A 1  161  ? -35.509 -49.289  58.975  1.00 56.98  ?  161  MET A CA  1 
ATOM   1278  C  C   . MET A 1  161  ? -34.446 -48.942  60.008  1.00 56.56  ?  161  MET A C   1 
ATOM   1279  O  O   . MET A 1  161  ? -33.251 -49.156  59.770  1.00 52.64  ?  161  MET A O   1 
ATOM   1280  C  CB  . MET A 1  161  ? -35.865 -48.063  58.133  1.00 65.60  ?  161  MET A CB  1 
ATOM   1281  C  CG  . MET A 1  161  ? -34.709 -47.578  57.272  1.00 69.58  ?  161  MET A CG  1 
ATOM   1282  S  SD  . MET A 1  161  ? -35.092 -46.171  56.215  1.00 89.17  ?  161  MET A SD  1 
ATOM   1283  C  CE  . MET A 1  161  ? -34.750 -44.812  57.325  1.00 75.81  ?  161  MET A CE  1 
ATOM   1284  N  N   . GLY A 1  162  ? -34.865 -48.404  61.156  1.00 49.50  ?  162  GLY A N   1 
ATOM   1285  C  CA  . GLY A 1  162  ? -33.953 -48.171  62.260  1.00 51.71  ?  162  GLY A CA  1 
ATOM   1286  C  C   . GLY A 1  162  ? -33.296 -49.429  62.786  1.00 50.90  ?  162  GLY A C   1 
ATOM   1287  O  O   . GLY A 1  162  ? -32.190 -49.355  63.329  1.00 50.19  ?  162  GLY A O   1 
ATOM   1288  N  N   . TRP A 1  163  ? -33.946 -50.584  62.633  1.00 66.48  ?  163  TRP A N   1 
ATOM   1289  C  CA  . TRP A 1  163  ? -33.328 -51.836  63.055  1.00 72.17  ?  163  TRP A CA  1 
ATOM   1290  C  C   . TRP A 1  163  ? -32.134 -52.184  62.175  1.00 70.00  ?  163  TRP A C   1 
ATOM   1291  O  O   . TRP A 1  163  ? -31.099 -52.637  62.677  1.00 73.48  ?  163  TRP A O   1 
ATOM   1292  C  CB  . TRP A 1  163  ? -34.361 -52.960  63.038  1.00 68.53  ?  163  TRP A CB  1 
ATOM   1293  C  CG  . TRP A 1  163  ? -33.762 -54.314  63.212  1.00 69.79  ?  163  TRP A CG  1 
ATOM   1294  C  CD1 . TRP A 1  163  ? -33.240 -54.841  64.358  1.00 68.77  ?  163  TRP A CD1 1 
ATOM   1295  C  CD2 . TRP A 1  163  ? -33.611 -55.318  62.203  1.00 68.69  ?  163  TRP A CD2 1 
ATOM   1296  N  NE1 . TRP A 1  163  ? -32.779 -56.114  64.125  1.00 68.88  ?  163  TRP A NE1 1 
ATOM   1297  C  CE2 . TRP A 1  163  ? -32.995 -56.430  62.809  1.00 72.82  ?  163  TRP A CE2 1 
ATOM   1298  C  CE3 . TRP A 1  163  ? -33.940 -55.385  60.846  1.00 58.35  ?  163  TRP A CE3 1 
ATOM   1299  C  CZ2 . TRP A 1  163  ? -32.702 -57.595  62.105  1.00 69.90  ?  163  TRP A CZ2 1 
ATOM   1300  C  CZ3 . TRP A 1  163  ? -33.648 -56.540  60.150  1.00 57.98  ?  163  TRP A CZ3 1 
ATOM   1301  C  CH2 . TRP A 1  163  ? -33.036 -57.630  60.779  1.00 70.12  ?  163  TRP A CH2 1 
ATOM   1302  N  N   . CYS A 1  164  ? -32.262 -51.992  60.859  1.00 55.41  ?  164  CYS A N   1 
ATOM   1303  C  CA  . CYS A 1  164  ? -31.107 -52.149  59.981  1.00 54.96  ?  164  CYS A CA  1 
ATOM   1304  C  C   . CYS A 1  164  ? -30.067 -51.067  60.244  1.00 53.50  ?  164  CYS A C   1 
ATOM   1305  O  O   . CYS A 1  164  ? -28.863 -51.345  60.258  1.00 54.04  ?  164  CYS A O   1 
ATOM   1306  C  CB  . CYS A 1  164  ? -31.543 -52.119  58.515  1.00 54.50  ?  164  CYS A CB  1 
ATOM   1307  S  SG  . CYS A 1  164  ? -32.988 -53.123  58.108  1.00 56.04  ?  164  CYS A SG  1 
ATOM   1308  N  N   . LEU A 1  165  ? -30.518 -49.828  60.457  1.00 45.40  ?  165  LEU A N   1 
ATOM   1309  C  CA  . LEU A 1  165  ? -29.593 -48.725  60.696  1.00 43.30  ?  165  LEU A CA  1 
ATOM   1310  C  C   . LEU A 1  165  ? -28.795 -48.919  61.979  1.00 57.11  ?  165  LEU A C   1 
ATOM   1311  O  O   . LEU A 1  165  ? -27.662 -48.436  62.083  1.00 54.07  ?  165  LEU A O   1 
ATOM   1312  C  CB  . LEU A 1  165  ? -30.364 -47.407  60.740  1.00 48.08  ?  165  LEU A CB  1 
ATOM   1313  C  CG  . LEU A 1  165  ? -30.814 -46.869  59.383  1.00 45.09  ?  165  LEU A CG  1 
ATOM   1314  C  CD1 . LEU A 1  165  ? -31.598 -45.582  59.543  1.00 56.35  ?  165  LEU A CD1 1 
ATOM   1315  C  CD2 . LEU A 1  165  ? -29.592 -46.630  58.527  1.00 47.86  ?  165  LEU A CD2 1 
ATOM   1316  N  N   . ASN A 1  166  ? -29.362 -49.625  62.961  1.00 67.68  ?  166  ASN A N   1 
ATOM   1317  C  CA  . ASN A 1  166  ? -28.661 -49.826  64.224  1.00 64.09  ?  166  ASN A CA  1 
ATOM   1318  C  C   . ASN A 1  166  ? -27.419 -50.689  64.034  1.00 61.20  ?  166  ASN A C   1 
ATOM   1319  O  O   . ASN A 1  166  ? -26.353 -50.382  64.581  1.00 64.82  ?  166  ASN A O   1 
ATOM   1320  C  CB  . ASN A 1  166  ? -29.603 -50.453  65.251  1.00 64.63  ?  166  ASN A CB  1 
ATOM   1321  C  CG  . ASN A 1  166  ? -28.941 -50.666  66.596  1.00 67.47  ?  166  ASN A CG  1 
ATOM   1322  O  OD1 . ASN A 1  166  ? -29.221 -51.644  67.287  1.00 83.39  ?  166  ASN A OD1 1 
ATOM   1323  N  ND2 . ASN A 1  166  ? -28.064 -49.745  66.979  1.00 66.70  ?  166  ASN A ND2 1 
ATOM   1324  N  N   . CYS A 1  167  ? -27.534 -51.770  63.258  1.00 51.29  ?  167  CYS A N   1 
ATOM   1325  C  CA  . CYS A 1  167  ? -26.366 -52.601  62.988  1.00 53.75  ?  167  CYS A CA  1 
ATOM   1326  C  C   . CYS A 1  167  ? -25.421 -51.922  62.004  1.00 49.48  ?  167  CYS A C   1 
ATOM   1327  O  O   . CYS A 1  167  ? -24.197 -51.995  62.159  1.00 45.64  ?  167  CYS A O   1 
ATOM   1328  C  CB  . CYS A 1  167  ? -26.798 -53.964  62.453  1.00 46.59  ?  167  CYS A CB  1 
ATOM   1329  S  SG  . CYS A 1  167  ? -25.539 -55.248  62.613  1.00 44.47  ?  167  CYS A SG  1 
ATOM   1330  N  N   . HIS A 1  168  ? -25.967 -51.260  60.982  1.00 72.01  ?  168  HIS A N   1 
ATOM   1331  C  CA  . HIS A 1  168  ? -25.120 -50.634  59.972  1.00 70.88  ?  168  HIS A CA  1 
ATOM   1332  C  C   . HIS A 1  168  ? -24.292 -49.502  60.567  1.00 73.39  ?  168  HIS A C   1 
ATOM   1333  O  O   . HIS A 1  168  ? -23.123 -49.323  60.206  1.00 70.03  ?  168  HIS A O   1 
ATOM   1334  C  CB  . HIS A 1  168  ? -25.987 -50.144  58.814  1.00 71.90  ?  168  HIS A CB  1 
ATOM   1335  C  CG  . HIS A 1  168  ? -26.360 -51.227  57.850  1.00 69.77  ?  168  HIS A CG  1 
ATOM   1336  N  ND1 . HIS A 1  168  ? -25.448 -51.803  56.995  1.00 71.63  ?  168  HIS A ND1 1 
ATOM   1337  C  CD2 . HIS A 1  168  ? -27.535 -51.867  57.634  1.00 70.89  ?  168  HIS A CD2 1 
ATOM   1338  C  CE1 . HIS A 1  168  ? -26.049 -52.735  56.278  1.00 69.72  ?  168  HIS A CE1 1 
ATOM   1339  N  NE2 . HIS A 1  168  ? -27.313 -52.802  56.651  1.00 68.01  ?  168  HIS A NE2 1 
ATOM   1340  N  N   . ARG A 1  169  ? -24.872 -48.738  61.495  1.00 54.79  ?  169  ARG A N   1 
ATOM   1341  C  CA  . ARG A 1  169  ? -24.129 -47.659  62.134  1.00 60.39  ?  169  ARG A CA  1 
ATOM   1342  C  C   . ARG A 1  169  ? -23.196 -48.168  63.226  1.00 68.44  ?  169  ARG A C   1 
ATOM   1343  O  O   . ARG A 1  169  ? -22.134 -47.577  63.451  1.00 65.23  ?  169  ARG A O   1 
ATOM   1344  C  CB  . ARG A 1  169  ? -25.098 -46.628  62.711  1.00 61.76  ?  169  ARG A CB  1 
ATOM   1345  C  CG  . ARG A 1  169  ? -25.856 -45.847  61.657  1.00 62.59  ?  169  ARG A CG  1 
ATOM   1346  C  CD  . ARG A 1  169  ? -26.184 -44.444  62.129  1.00 70.22  ?  169  ARG A CD  1 
ATOM   1347  N  NE  . ARG A 1  169  ? -27.425 -43.959  61.539  1.00 64.56  ?  169  ARG A NE  1 
ATOM   1348  C  CZ  . ARG A 1  169  ? -28.617 -44.067  62.109  1.00 70.55  ?  169  ARG A CZ  1 
ATOM   1349  N  NH1 . ARG A 1  169  ? -28.769 -44.636  63.294  1.00 79.82  ?  169  ARG A NH1 1 
ATOM   1350  N  NH2 . ARG A 1  169  ? -29.685 -43.596  61.472  1.00 56.42  ?  169  ARG A NH2 1 
ATOM   1351  N  N   . ASN A 1  170  ? -23.565 -49.250  63.909  1.00 74.19  ?  170  ASN A N   1 
ATOM   1352  C  CA  . ASN A 1  170  ? -22.766 -49.816  64.996  1.00 71.34  ?  170  ASN A CA  1 
ATOM   1353  C  C   . ASN A 1  170  ? -22.667 -51.326  64.818  1.00 73.41  ?  170  ASN A C   1 
ATOM   1354  O  O   . ASN A 1  170  ? -23.316 -52.096  65.537  1.00 74.83  ?  170  ASN A O   1 
ATOM   1355  C  CB  . ASN A 1  170  ? -23.368 -49.459  66.355  1.00 67.79  ?  170  ASN A CB  1 
ATOM   1356  C  CG  . ASN A 1  170  ? -23.401 -47.963  66.604  1.00 71.89  ?  170  ASN A CG  1 
ATOM   1357  O  OD1 . ASN A 1  170  ? -24.416 -47.417  67.036  1.00 72.23  ?  170  ASN A OD1 1 
ATOM   1358  N  ND2 . ASN A 1  170  ? -22.286 -47.293  66.336  1.00 75.04  ?  170  ASN A ND2 1 
ATOM   1359  N  N   . PRO A 1  171  ? -21.852 -51.788  63.864  1.00 74.75  ?  171  PRO A N   1 
ATOM   1360  C  CA  . PRO A 1  171  ? -21.720 -53.235  63.643  1.00 77.83  ?  171  PRO A CA  1 
ATOM   1361  C  C   . PRO A 1  171  ? -20.795 -53.932  64.624  1.00 72.96  ?  171  PRO A C   1 
ATOM   1362  O  O   . PRO A 1  171  ? -20.741 -55.170  64.620  1.00 68.54  ?  171  PRO A O   1 
ATOM   1363  C  CB  . PRO A 1  171  ? -21.162 -53.311  62.217  1.00 66.50  ?  171  PRO A CB  1 
ATOM   1364  C  CG  . PRO A 1  171  ? -20.334 -52.077  62.097  1.00 65.57  ?  171  PRO A CG  1 
ATOM   1365  C  CD  . PRO A 1  171  ? -21.041 -51.011  62.908  1.00 75.13  ?  171  PRO A CD  1 
ATOM   1366  N  N   . GLU A 1  172  ? -20.070 -53.186  65.461  1.00 71.20  ?  172  GLU A N   1 
ATOM   1367  C  CA  . GLU A 1  172  ? -19.165 -53.814  66.418  1.00 77.11  ?  172  GLU A CA  1 
ATOM   1368  C  C   . GLU A 1  172  ? -19.925 -54.633  67.451  1.00 80.47  ?  172  GLU A C   1 
ATOM   1369  O  O   . GLU A 1  172  ? -19.366 -55.568  68.036  1.00 80.93  ?  172  GLU A O   1 
ATOM   1370  C  CB  . GLU A 1  172  ? -18.319 -52.749  67.116  1.00 80.41  ?  172  GLU A CB  1 
ATOM   1371  C  CG  . GLU A 1  172  ? -19.106 -51.516  67.533  1.00 86.99  ?  172  GLU A CG  1 
ATOM   1372  C  CD  . GLU A 1  172  ? -19.044 -50.401  66.508  1.00 88.22  ?  172  GLU A CD  1 
ATOM   1373  O  OE1 . GLU A 1  172  ? -18.886 -50.705  65.306  1.00 87.39  ?  172  GLU A OE1 1 
ATOM   1374  O  OE2 . GLU A 1  172  ? -19.162 -49.222  66.902  1.00 79.06  -1 172  GLU A OE2 1 
ATOM   1375  N  N   . LEU A 1  173  ? -21.196 -54.305  67.686  1.00 70.88  ?  173  LEU A N   1 
ATOM   1376  C  CA  . LEU A 1  173  ? -21.962 -54.963  68.735  1.00 73.90  ?  173  LEU A CA  1 
ATOM   1377  C  C   . LEU A 1  173  ? -22.540 -56.304  68.300  1.00 69.95  ?  173  LEU A C   1 
ATOM   1378  O  O   . LEU A 1  173  ? -22.802 -57.155  69.157  1.00 75.52  ?  173  LEU A O   1 
ATOM   1379  C  CB  . LEU A 1  173  ? -23.096 -54.047  69.209  1.00 75.53  ?  173  LEU A CB  1 
ATOM   1380  C  CG  . LEU A 1  173  ? -22.771 -52.559  69.383  1.00 67.59  ?  173  LEU A CG  1 
ATOM   1381  C  CD1 . LEU A 1  173  ? -24.040 -51.755  69.623  1.00 56.97  ?  173  LEU A CD1 1 
ATOM   1382  C  CD2 . LEU A 1  173  ? -21.781 -52.346  70.517  1.00 67.07  ?  173  LEU A CD2 1 
ATOM   1383  N  N   . TYR A 1  174  ? -22.733 -56.523  66.998  1.00 57.87  ?  174  TYR A N   1 
ATOM   1384  C  CA  . TYR A 1  174  ? -23.437 -57.706  66.519  1.00 55.56  ?  174  TYR A CA  1 
ATOM   1385  C  C   . TYR A 1  174  ? -22.611 -58.609  65.613  1.00 56.68  ?  174  TYR A C   1 
ATOM   1386  O  O   . TYR A 1  174  ? -23.114 -59.661  65.200  1.00 64.42  ?  174  TYR A O   1 
ATOM   1387  C  CB  . TYR A 1  174  ? -24.719 -57.297  65.779  1.00 56.86  ?  174  TYR A CB  1 
ATOM   1388  C  CG  . TYR A 1  174  ? -25.544 -56.254  66.498  1.00 57.57  ?  174  TYR A CG  1 
ATOM   1389  C  CD1 . TYR A 1  174  ? -26.495 -56.622  67.441  1.00 49.94  ?  174  TYR A CD1 1 
ATOM   1390  C  CD2 . TYR A 1  174  ? -25.376 -54.901  66.231  1.00 53.91  ?  174  TYR A CD2 1 
ATOM   1391  C  CE1 . TYR A 1  174  ? -27.251 -55.672  68.100  1.00 44.28  ?  174  TYR A CE1 1 
ATOM   1392  C  CE2 . TYR A 1  174  ? -26.128 -53.945  66.886  1.00 49.89  ?  174  TYR A CE2 1 
ATOM   1393  C  CZ  . TYR A 1  174  ? -27.063 -54.337  67.818  1.00 53.60  ?  174  TYR A CZ  1 
ATOM   1394  O  OH  . TYR A 1  174  ? -27.814 -53.388  68.472  1.00 76.85  ?  174  TYR A OH  1 
ATOM   1395  N  N   . VAL A 1  175  ? -21.375 -58.246  65.288  1.00 54.66  ?  175  VAL A N   1 
ATOM   1396  C  CA  . VAL A 1  175  ? -20.562 -59.067  64.397  1.00 54.09  ?  175  VAL A CA  1 
ATOM   1397  C  C   . VAL A 1  175  ? -20.060 -60.295  65.149  1.00 66.44  ?  175  VAL A C   1 
ATOM   1398  O  O   . VAL A 1  175  ? -19.824 -60.259  66.362  1.00 71.70  ?  175  VAL A O   1 
ATOM   1399  C  CB  . VAL A 1  175  ? -19.402 -58.242  63.803  1.00 54.37  ?  175  VAL A CB  1 
ATOM   1400  C  CG1 . VAL A 1  175  ? -18.410 -57.857  64.880  1.00 60.68  ?  175  VAL A CG1 1 
ATOM   1401  C  CG2 . VAL A 1  175  ? -18.711 -59.007  62.681  1.00 53.58  ?  175  VAL A CG2 1 
ATOM   1402  N  N   . ARG A 1  176  ? -19.908 -61.399  64.423  1.00 65.46  ?  176  ARG A N   1 
ATOM   1403  C  CA  . ARG A 1  176  ? -19.497 -62.679  64.975  1.00 62.99  ?  176  ARG A CA  1 
ATOM   1404  C  C   . ARG A 1  176  ? -18.387 -63.273  64.119  1.00 69.26  ?  176  ARG A C   1 
ATOM   1405  O  O   . ARG A 1  176  ? -18.275 -62.952  62.932  1.00 70.47  ?  176  ARG A O   1 
ATOM   1406  C  CB  . ARG A 1  176  ? -20.693 -63.641  65.052  1.00 63.94  ?  176  ARG A CB  1 
ATOM   1407  C  CG  . ARG A 1  176  ? -20.770 -64.664  63.937  1.00 75.80  ?  176  ARG A CG  1 
ATOM   1408  C  CD  . ARG A 1  176  ? -21.895 -65.655  64.185  1.00 73.99  ?  176  ARG A CD  1 
ATOM   1409  N  NE  . ARG A 1  176  ? -23.082 -65.000  64.722  1.00 76.00  ?  176  ARG A NE  1 
ATOM   1410  C  CZ  . ARG A 1  176  ? -24.037 -65.614  65.407  1.00 76.93  ?  176  ARG A CZ  1 
ATOM   1411  N  NH1 . ARG A 1  176  ? -24.000 -66.918  65.627  1.00 78.62  ?  176  ARG A NH1 1 
ATOM   1412  N  NH2 . ARG A 1  176  ? -25.059 -64.904  65.876  1.00 74.56  ?  176  ARG A NH2 1 
ATOM   1413  N  N   . PRO A 1  177  ? -17.531 -64.128  64.700  1.00 84.38  ?  177  PRO A N   1 
ATOM   1414  C  CA  . PRO A 1  177  ? -16.339 -64.616  63.962  1.00 89.23  ?  177  PRO A CA  1 
ATOM   1415  C  C   . PRO A 1  177  ? -16.592 -65.846  63.093  1.00 100.65 ?  177  PRO A C   1 
ATOM   1416  O  O   . PRO A 1  177  ? -16.052 -66.939  63.320  1.00 115.03 ?  177  PRO A O   1 
ATOM   1417  C  CB  . PRO A 1  177  ? -15.351 -64.898  65.096  1.00 72.23  ?  177  PRO A CB  1 
ATOM   1418  C  CG  . PRO A 1  177  ? -16.210 -65.293  66.245  1.00 90.94  ?  177  PRO A CG  1 
ATOM   1419  C  CD  . PRO A 1  177  ? -17.510 -64.539  66.116  1.00 84.50  ?  177  PRO A CD  1 
ATOM   1420  N  N   . ARG A 1  178  ? -17.424 -65.663  62.064  1.00 79.59  ?  178  ARG A N   1 
ATOM   1421  C  CA  . ARG A 1  178  ? -17.621 -66.652  61.000  1.00 83.92  ?  178  ARG A CA  1 
ATOM   1422  C  C   . ARG A 1  178  ? -18.016 -68.021  61.551  1.00 98.80  ?  178  ARG A C   1 
ATOM   1423  O  O   . ARG A 1  178  ? -17.558 -69.063  61.077  1.00 96.13  ?  178  ARG A O   1 
ATOM   1424  C  CB  . ARG A 1  178  ? -16.379 -66.766  60.116  1.00 84.60  ?  178  ARG A CB  1 
ATOM   1425  C  CG  . ARG A 1  178  ? -16.015 -65.474  59.401  1.00 85.27  ?  178  ARG A CG  1 
ATOM   1426  C  CD  . ARG A 1  178  ? -17.002 -65.135  58.290  1.00 78.72  ?  178  ARG A CD  1 
ATOM   1427  N  NE  . ARG A 1  178  ? -16.748 -65.883  57.063  1.00 83.35  ?  178  ARG A NE  1 
ATOM   1428  C  CZ  . ARG A 1  178  ? -15.885 -65.512  56.126  1.00 73.87  ?  178  ARG A CZ  1 
ATOM   1429  N  NH1 . ARG A 1  178  ? -15.165 -64.409  56.246  1.00 69.37  ?  178  ARG A NH1 1 
ATOM   1430  N  NH2 . ARG A 1  178  ? -15.742 -66.266  55.039  1.00 57.60  ?  178  ARG A NH2 1 
ATOM   1431  N  N   . GLU A 1  179  ? -18.874 -68.025  62.569  1.00 99.91  ?  179  GLU A N   1 
ATOM   1432  C  CA  . GLU A 1  179  ? -19.495 -69.270  63.001  1.00 94.13  ?  179  GLU A CA  1 
ATOM   1433  C  C   . GLU A 1  179  ? -21.007 -69.106  62.959  1.00 94.75  ?  179  GLU A C   1 
ATOM   1434  O  O   . GLU A 1  179  ? -21.706 -69.476  63.907  1.00 97.30  ?  179  GLU A O   1 
ATOM   1435  C  CB  . GLU A 1  179  ? -19.044 -69.658  64.416  1.00 98.23  ?  179  GLU A CB  1 
ATOM   1436  C  CG  . GLU A 1  179  ? -18.915 -68.490  65.369  1.00 91.43  ?  179  GLU A CG  1 
ATOM   1437  C  CD  . GLU A 1  179  ? -18.247 -68.880  66.673  1.00 94.61  ?  179  GLU A CD  1 
ATOM   1438  O  OE1 . GLU A 1  179  ? -17.855 -70.058  66.813  1.00 85.27  ?  179  GLU A OE1 1 
ATOM   1439  O  OE2 . GLU A 1  179  ? -18.125 -68.012  67.563  1.00 105.50 -1 179  GLU A OE2 1 
ATOM   1440  N  N   . GLU A 1  180  ? -21.507 -68.547  61.859  1.00 113.23 ?  180  GLU A N   1 
ATOM   1441  C  CA  . GLU A 1  180  ? -22.904 -68.154  61.713  1.00 111.90 ?  180  GLU A CA  1 
ATOM   1442  C  C   . GLU A 1  180  ? -23.818 -69.289  61.265  1.00 115.63 ?  180  GLU A C   1 
ATOM   1443  O  O   . GLU A 1  180  ? -24.960 -69.373  61.728  1.00 111.15 ?  180  GLU A O   1 
ATOM   1444  C  CB  . GLU A 1  180  ? -23.018 -66.995  60.711  1.00 107.72 ?  180  GLU A CB  1 
ATOM   1445  C  CG  . GLU A 1  180  ? -22.464 -67.297  59.325  1.00 104.43 ?  180  GLU A CG  1 
ATOM   1446  C  CD  . GLU A 1  180  ? -21.069 -66.750  59.115  1.00 116.74 ?  180  GLU A CD  1 
ATOM   1447  O  OE1 . GLU A 1  180  ? -20.611 -65.961  59.964  1.00 113.46 ?  180  GLU A OE1 1 
ATOM   1448  O  OE2 . GLU A 1  180  ? -20.433 -67.107  58.101  1.00 124.72 -1 180  GLU A OE2 1 
ATOM   1449  N  N   . VAL A 1  181  ? -23.344 -70.156  60.367  1.00 105.31 ?  181  VAL A N   1 
ATOM   1450  C  CA  . VAL A 1  181  ? -24.205 -71.199  59.811  1.00 102.99 ?  181  VAL A CA  1 
ATOM   1451  C  C   . VAL A 1  181  ? -24.675 -72.146  60.910  1.00 110.28 ?  181  VAL A C   1 
ATOM   1452  O  O   . VAL A 1  181  ? -25.866 -72.465  61.012  1.00 113.99 ?  181  VAL A O   1 
ATOM   1453  C  CB  . VAL A 1  181  ? -23.486 -71.951  58.676  1.00 91.53  ?  181  VAL A CB  1 
ATOM   1454  C  CG1 . VAL A 1  181  ? -23.477 -71.113  57.408  1.00 80.05  ?  181  VAL A CG1 1 
ATOM   1455  C  CG2 . VAL A 1  181  ? -22.059 -72.297  59.079  1.00 97.80  ?  181  VAL A CG2 1 
ATOM   1456  N  N   . TYR A 1  182  ? -23.752 -72.612  61.745  1.00 153.76 ?  182  TYR A N   1 
ATOM   1457  C  CA  . TYR A 1  182  ? -24.103 -73.384  62.920  1.00 152.02 ?  182  TYR A CA  1 
ATOM   1458  C  C   . TYR A 1  182  ? -23.947 -72.484  64.146  1.00 147.73 ?  182  TYR A C   1 
ATOM   1459  O  O   . TYR A 1  182  ? -24.003 -71.250  64.033  1.00 142.09 ?  182  TYR A O   1 
ATOM   1460  C  CB  . TYR A 1  182  ? -23.247 -74.655  62.988  1.00 160.37 ?  182  TYR A CB  1 
ATOM   1461  C  CG  . TYR A 1  182  ? -21.773 -74.427  63.260  1.00 168.86 ?  182  TYR A CG  1 
ATOM   1462  C  CD1 . TYR A 1  182  ? -20.955 -73.805  62.324  1.00 169.13 ?  182  TYR A CD1 1 
ATOM   1463  C  CD2 . TYR A 1  182  ? -21.197 -74.848  64.453  1.00 163.40 ?  182  TYR A CD2 1 
ATOM   1464  C  CE1 . TYR A 1  182  ? -19.610 -73.603  62.571  1.00 169.29 ?  182  TYR A CE1 1 
ATOM   1465  C  CE2 . TYR A 1  182  ? -19.853 -74.650  64.709  1.00 159.60 ?  182  TYR A CE2 1 
ATOM   1466  C  CZ  . TYR A 1  182  ? -19.065 -74.027  63.764  1.00 164.89 ?  182  TYR A CZ  1 
ATOM   1467  O  OH  . TYR A 1  182  ? -17.727 -73.828  64.014  1.00 166.32 ?  182  TYR A OH  1 
ATOM   1468  N  N   . ASN A 1  183  ? -23.748 -73.099  65.311  1.00 126.04 ?  183  ASN A N   1 
ATOM   1469  C  CA  . ASN A 1  183  ? -23.559 -72.369  66.564  1.00 118.61 ?  183  ASN A CA  1 
ATOM   1470  C  C   . ASN A 1  183  ? -24.727 -71.421  66.836  1.00 120.59 ?  183  ASN A C   1 
ATOM   1471  O  O   . ASN A 1  183  ? -24.543 -70.248  67.166  1.00 123.78 ?  183  ASN A O   1 
ATOM   1472  C  CB  . ASN A 1  183  ? -22.226 -71.616  66.570  1.00 117.43 ?  183  ASN A CB  1 
ATOM   1473  C  CG  . ASN A 1  183  ? -21.107 -72.414  67.210  1.00 121.88 ?  183  ASN A CG  1 
ATOM   1474  O  OD1 . ASN A 1  183  ? -21.352 -73.316  68.011  1.00 126.20 ?  183  ASN A OD1 1 
ATOM   1475  N  ND2 . ASN A 1  183  ? -19.869 -72.083  66.861  1.00 118.99 ?  183  ASN A ND2 1 
ATOM   1476  N  N   . MET A 1  184  ? -25.948 -71.939  66.678  1.00 106.49 ?  184  MET A N   1 
ATOM   1477  C  CA  . MET A 1  184  ? -27.115 -71.198  67.146  1.00 100.60 ?  184  MET A CA  1 
ATOM   1478  C  C   . MET A 1  184  ? -27.066 -71.013  68.655  1.00 99.13  ?  184  MET A C   1 
ATOM   1479  O  O   . MET A 1  184  ? -27.653 -70.063  69.188  1.00 92.48  ?  184  MET A O   1 
ATOM   1480  C  CB  . MET A 1  184  ? -28.400 -71.918  66.735  1.00 91.99  ?  184  MET A CB  1 
ATOM   1481  C  CG  . MET A 1  184  ? -28.568 -72.093  65.232  1.00 92.95  ?  184  MET A CG  1 
ATOM   1482  S  SD  . MET A 1  184  ? -28.899 -70.542  64.372  1.00 110.49 ?  184  MET A SD  1 
ATOM   1483  C  CE  . MET A 1  184  ? -30.564 -70.193  64.930  1.00 89.92  ?  184  MET A CE  1 
ATOM   1484  N  N   . ASP A 1  185  ? -26.369 -71.912  69.355  1.00 116.04 ?  185  ASP A N   1 
ATOM   1485  C  CA  . ASP A 1  185  ? -26.125 -71.773  70.782  1.00 122.08 ?  185  ASP A CA  1 
ATOM   1486  C  C   . ASP A 1  185  ? -25.054 -70.737  71.097  1.00 124.08 ?  185  ASP A C   1 
ATOM   1487  O  O   . ASP A 1  185  ? -24.958 -70.299  72.248  1.00 129.38 ?  185  ASP A O   1 
ATOM   1488  C  CB  . ASP A 1  185  ? -25.716 -73.123  71.378  1.00 131.86 ?  185  ASP A CB  1 
ATOM   1489  C  CG  . ASP A 1  185  ? -26.668 -74.239  71.000  1.00 134.80 ?  185  ASP A CG  1 
ATOM   1490  O  OD1 . ASP A 1  185  ? -27.808 -73.933  70.592  1.00 135.27 ?  185  ASP A OD1 1 
ATOM   1491  O  OD2 . ASP A 1  185  ? -26.278 -75.422  71.109  1.00 129.87 -1 185  ASP A OD2 1 
ATOM   1492  N  N   . TYR A 1  186  ? -24.245 -70.350  70.112  1.00 92.09  ?  186  TYR A N   1 
ATOM   1493  C  CA  . TYR A 1  186  ? -23.243 -69.316  70.335  1.00 90.83  ?  186  TYR A CA  1 
ATOM   1494  C  C   . TYR A 1  186  ? -23.919 -68.002  70.697  1.00 88.23  ?  186  TYR A C   1 
ATOM   1495  O  O   . TYR A 1  186  ? -24.969 -67.650  70.152  1.00 84.18  ?  186  TYR A O   1 
ATOM   1496  C  CB  . TYR A 1  186  ? -22.370 -69.130  69.090  1.00 85.53  ?  186  TYR A CB  1 
ATOM   1497  C  CG  . TYR A 1  186  ? -21.704 -67.771  68.990  1.00 75.21  ?  186  TYR A CG  1 
ATOM   1498  C  CD1 . TYR A 1  186  ? -20.518 -67.507  69.662  1.00 83.06  ?  186  TYR A CD1 1 
ATOM   1499  C  CD2 . TYR A 1  186  ? -22.262 -66.752  68.224  1.00 69.00  ?  186  TYR A CD2 1 
ATOM   1500  C  CE1 . TYR A 1  186  ? -19.906 -66.271  69.575  1.00 69.37  ?  186  TYR A CE1 1 
ATOM   1501  C  CE2 . TYR A 1  186  ? -21.658 -65.511  68.135  1.00 64.45  ?  186  TYR A CE2 1 
ATOM   1502  C  CZ  . TYR A 1  186  ? -20.480 -65.278  68.812  1.00 63.65  ?  186  TYR A CZ  1 
ATOM   1503  O  OH  . TYR A 1  186  ? -19.870 -64.047  68.727  1.00 64.88  ?  186  TYR A OH  1 
ATOM   1504  N  N   . VAL A 1  187  ? -23.303 -67.272  71.620  1.00 95.52  ?  187  VAL A N   1 
ATOM   1505  C  CA  . VAL A 1  187  ? -23.849 -66.001  72.090  1.00 91.68  ?  187  VAL A CA  1 
ATOM   1506  C  C   . VAL A 1  187  ? -22.716 -64.987  72.157  1.00 87.53  ?  187  VAL A C   1 
ATOM   1507  O  O   . VAL A 1  187  ? -21.536 -65.360  72.255  1.00 85.72  ?  187  VAL A O   1 
ATOM   1508  C  CB  . VAL A 1  187  ? -24.552 -66.159  73.458  1.00 102.05 ?  187  VAL A CB  1 
ATOM   1509  C  CG1 . VAL A 1  187  ? -25.898 -66.833  73.260  1.00 108.32 ?  187  VAL A CG1 1 
ATOM   1510  C  CG2 . VAL A 1  187  ? -23.677 -66.959  74.407  1.00 105.55 ?  187  VAL A CG2 1 
ATOM   1511  N  N   . PRO A 1  188  ? -23.039 -63.697  72.083  1.00 89.44  ?  188  PRO A N   1 
ATOM   1512  C  CA  . PRO A 1  188  ? -21.996 -62.663  72.095  1.00 86.38  ?  188  PRO A CA  1 
ATOM   1513  C  C   . PRO A 1  188  ? -21.115 -62.783  73.324  1.00 93.28  ?  188  PRO A C   1 
ATOM   1514  O  O   . PRO A 1  188  ? -21.616 -62.867  74.456  1.00 102.55 ?  188  PRO A O   1 
ATOM   1515  C  CB  . PRO A 1  188  ? -22.795 -61.349  72.107  1.00 91.36  ?  188  PRO A CB  1 
ATOM   1516  C  CG  . PRO A 1  188  ? -24.190 -61.736  72.502  1.00 94.99  ?  188  PRO A CG  1 
ATOM   1517  C  CD  . PRO A 1  188  ? -24.383 -63.107  71.952  1.00 93.36  ?  188  PRO A CD  1 
ATOM   1518  N  N   . PRO A 1  189  ? -19.798 -62.806  73.141  1.00 84.25  ?  189  PRO A N   1 
ATOM   1519  C  CA  . PRO A 1  189  ? -18.891 -62.899  74.289  1.00 84.31  ?  189  PRO A CA  1 
ATOM   1520  C  C   . PRO A 1  189  ? -18.973 -61.650  75.155  1.00 90.48  ?  189  PRO A C   1 
ATOM   1521  O  O   . PRO A 1  189  ? -19.536 -60.622  74.774  1.00 87.77  ?  189  PRO A O   1 
ATOM   1522  C  CB  . PRO A 1  189  ? -17.512 -63.046  73.639  1.00 85.24  ?  189  PRO A CB  1 
ATOM   1523  C  CG  . PRO A 1  189  ? -17.663 -62.388  72.304  1.00 91.43  ?  189  PRO A CG  1 
ATOM   1524  C  CD  . PRO A 1  189  ? -19.068 -62.704  71.866  1.00 91.24  ?  189  PRO A CD  1 
ATOM   1525  N  N   . SER A 1  190  ? -18.396 -61.761  76.353  1.00 91.47  ?  190  SER A N   1 
ATOM   1526  C  CA  . SER A 1  190  ? -18.416 -60.640  77.287  1.00 91.32  ?  190  SER A CA  1 
ATOM   1527  C  C   . SER A 1  190  ? -17.660 -59.441  76.727  1.00 88.34  ?  190  SER A C   1 
ATOM   1528  O  O   . SER A 1  190  ? -18.073 -58.291  76.920  1.00 82.83  ?  190  SER A O   1 
ATOM   1529  C  CB  . SER A 1  190  ? -17.830 -61.069  78.633  1.00 85.20  ?  190  SER A CB  1 
ATOM   1530  O  OG  . SER A 1  190  ? -17.617 -59.952  79.478  1.00 98.17  ?  190  SER A OG  1 
ATOM   1531  N  N   . ASN A 1  191  ? -16.562 -59.689  76.022  1.00 114.81 ?  191  ASN A N   1 
ATOM   1532  C  CA  . ASN A 1  191  ? -15.763 -58.625  75.413  1.00 112.32 ?  191  ASN A CA  1 
ATOM   1533  C  C   . ASN A 1  191  ? -16.114 -58.477  73.933  1.00 117.47 ?  191  ASN A C   1 
ATOM   1534  O  O   . ASN A 1  191  ? -15.273 -58.604  73.042  1.00 129.93 ?  191  ASN A O   1 
ATOM   1535  C  CB  . ASN A 1  191  ? -14.277 -58.909  75.605  1.00 115.70 ?  191  ASN A CB  1 
ATOM   1536  C  CG  . ASN A 1  191  ? -13.900 -60.325  75.212  1.00 125.41 ?  191  ASN A CG  1 
ATOM   1537  O  OD1 . ASN A 1  191  ? -14.748 -61.217  75.172  1.00 122.91 ?  191  ASN A OD1 1 
ATOM   1538  N  ND2 . ASN A 1  191  ? -12.623 -60.538  74.917  1.00 131.08 ?  191  ASN A ND2 1 
ATOM   1539  N  N   . GLN A 1  192  ? -17.395 -58.199  73.679  1.00 89.28  ?  192  GLN A N   1 
ATOM   1540  C  CA  . GLN A 1  192  ? -17.874 -58.113  72.304  1.00 80.31  ?  192  GLN A CA  1 
ATOM   1541  C  C   . GLN A 1  192  ? -17.338 -56.875  71.594  1.00 78.57  ?  192  GLN A C   1 
ATOM   1542  O  O   . GLN A 1  192  ? -17.096 -56.916  70.382  1.00 79.46  ?  192  GLN A O   1 
ATOM   1543  C  CB  . GLN A 1  192  ? -19.404 -58.129  72.284  1.00 79.24  ?  192  GLN A CB  1 
ATOM   1544  C  CG  . GLN A 1  192  ? -20.028 -57.768  70.946  1.00 73.09  ?  192  GLN A CG  1 
ATOM   1545  C  CD  . GLN A 1  192  ? -19.807 -58.833  69.890  1.00 74.83  ?  192  GLN A CD  1 
ATOM   1546  O  OE1 . GLN A 1  192  ? -20.139 -60.002  70.092  1.00 85.90  ?  192  GLN A OE1 1 
ATOM   1547  N  NE2 . GLN A 1  192  ? -19.246 -58.434  68.755  1.00 68.90  ?  192  GLN A NE2 1 
ATOM   1548  N  N   . LEU A 1  193  ? -17.128 -55.778  72.327  1.00 80.16  ?  193  LEU A N   1 
ATOM   1549  C  CA  . LEU A 1  193  ? -16.665 -54.545  71.697  1.00 74.83  ?  193  LEU A CA  1 
ATOM   1550  C  C   . LEU A 1  193  ? -15.256 -54.701  71.137  1.00 77.07  ?  193  LEU A C   1 
ATOM   1551  O  O   . LEU A 1  193  ? -14.980 -54.292  70.003  1.00 86.26  ?  193  LEU A O   1 
ATOM   1552  C  CB  . LEU A 1  193  ? -16.723 -53.389  72.696  1.00 68.09  ?  193  LEU A CB  1 
ATOM   1553  C  CG  . LEU A 1  193  ? -16.586 -51.992  72.084  1.00 72.28  ?  193  LEU A CG  1 
ATOM   1554  C  CD1 . LEU A 1  193  ? -17.629 -51.775  70.997  1.00 82.37  ?  193  LEU A CD1 1 
ATOM   1555  C  CD2 . LEU A 1  193  ? -16.692 -50.919  73.154  1.00 78.13  ?  193  LEU A CD2 1 
ATOM   1556  N  N   . GLU A 1  194  ? -14.346 -55.287  71.918  1.00 92.28  ?  194  GLU A N   1 
ATOM   1557  C  CA  . GLU A 1  194  ? -12.981 -55.487  71.440  1.00 99.10  ?  194  GLU A CA  1 
ATOM   1558  C  C   . GLU A 1  194  ? -12.943 -56.466  70.273  1.00 96.57  ?  194  GLU A C   1 
ATOM   1559  O  O   . GLU A 1  194  ? -12.301 -56.202  69.249  1.00 96.55  ?  194  GLU A O   1 
ATOM   1560  C  CB  . GLU A 1  194  ? -12.090 -55.980  72.579  1.00 110.62 ?  194  GLU A CB  1 
ATOM   1561  C  CG  . GLU A 1  194  ? -10.648 -56.219  72.164  1.00 118.46 ?  194  GLU A CG  1 
ATOM   1562  C  CD  . GLU A 1  194  ? -9.772  -56.657  73.320  1.00 134.53 ?  194  GLU A CD  1 
ATOM   1563  O  OE1 . GLU A 1  194  ? -10.314 -56.889  74.420  1.00 128.14 ?  194  GLU A OE1 1 
ATOM   1564  O  OE2 . GLU A 1  194  ? -8.543  -56.774  73.125  1.00 150.99 -1 194  GLU A OE2 1 
ATOM   1565  N  N   . ILE A 1  195  ? -13.620 -57.608  70.414  1.00 72.45  ?  195  ILE A N   1 
ATOM   1566  C  CA  . ILE A 1  195  ? -13.672 -58.582  69.328  1.00 68.87  ?  195  ILE A CA  1 
ATOM   1567  C  C   . ILE A 1  195  ? -14.374 -57.987  68.115  1.00 66.51  ?  195  ILE A C   1 
ATOM   1568  O  O   . ILE A 1  195  ? -13.979 -58.228  66.968  1.00 69.09  ?  195  ILE A O   1 
ATOM   1569  C  CB  . ILE A 1  195  ? -14.359 -59.877  69.804  1.00 67.73  ?  195  ILE A CB  1 
ATOM   1570  C  CG1 . ILE A 1  195  ? -13.579 -60.505  70.960  1.00 74.43  ?  195  ILE A CG1 1 
ATOM   1571  C  CG2 . ILE A 1  195  ? -14.491 -60.871  68.661  1.00 75.48  ?  195  ILE A CG2 1 
ATOM   1572  C  CD1 . ILE A 1  195  ? -12.180 -60.944  70.583  1.00 85.77  ?  195  ILE A CD1 1 
ATOM   1573  N  N   . GLY A 1  196  ? -15.416 -57.186  68.350  1.00 81.05  ?  196  GLY A N   1 
ATOM   1574  C  CA  . GLY A 1  196  ? -16.160 -56.610  67.242  1.00 78.48  ?  196  GLY A CA  1 
ATOM   1575  C  C   . GLY A 1  196  ? -15.351 -55.613  66.435  1.00 80.71  ?  196  GLY A C   1 
ATOM   1576  O  O   . GLY A 1  196  ? -15.388 -55.626  65.201  1.00 78.67  ?  196  GLY A O   1 
ATOM   1577  N  N   . ARG A 1  197  ? -14.617 -54.730  67.116  1.00 89.84  ?  197  ARG A N   1 
ATOM   1578  C  CA  . ARG A 1  197  ? -13.789 -53.758  66.410  1.00 89.46  ?  197  ARG A CA  1 
ATOM   1579  C  C   . ARG A 1  197  ? -12.687 -54.450  65.618  1.00 86.59  ?  197  ARG A C   1 
ATOM   1580  O  O   . ARG A 1  197  ? -12.359 -54.034  64.500  1.00 87.19  ?  197  ARG A O   1 
ATOM   1581  C  CB  . ARG A 1  197  ? -13.193 -52.761  67.404  1.00 96.31  ?  197  ARG A CB  1 
ATOM   1582  C  CG  . ARG A 1  197  ? -14.220 -51.850  68.057  1.00 96.46  ?  197  ARG A CG  1 
ATOM   1583  C  CD  . ARG A 1  197  ? -13.631 -50.488  68.376  1.00 101.03 ?  197  ARG A CD  1 
ATOM   1584  N  NE  . ARG A 1  197  ? -14.626 -49.591  68.950  1.00 111.58 ?  197  ARG A NE  1 
ATOM   1585  C  CZ  . ARG A 1  197  ? -14.725 -49.316  70.243  1.00 113.03 ?  197  ARG A CZ  1 
ATOM   1586  N  NH1 . ARG A 1  197  ? -13.904 -49.854  71.130  1.00 104.86 ?  197  ARG A NH1 1 
ATOM   1587  N  NH2 . ARG A 1  197  ? -15.673 -48.480  70.658  1.00 113.78 ?  197  ARG A NH2 1 
ATOM   1588  N  N   . GLN A 1  198  ? -12.107 -55.511  66.182  1.00 95.57  ?  198  GLN A N   1 
ATOM   1589  C  CA  . GLN A 1  198  ? -11.095 -56.277  65.464  1.00 97.64  ?  198  GLN A CA  1 
ATOM   1590  C  C   . GLN A 1  198  ? -11.692 -56.975  64.247  1.00 102.18 ?  198  GLN A C   1 
ATOM   1591  O  O   . GLN A 1  198  ? -11.067 -57.017  63.181  1.00 106.89 ?  198  GLN A O   1 
ATOM   1592  C  CB  . GLN A 1  198  ? -10.448 -57.292  66.405  1.00 108.11 ?  198  GLN A CB  1 
ATOM   1593  C  CG  . GLN A 1  198  ? -9.388  -58.167  65.758  1.00 121.52 ?  198  GLN A CG  1 
ATOM   1594  C  CD  . GLN A 1  198  ? -8.903  -59.267  66.681  1.00 133.71 ?  198  GLN A CD  1 
ATOM   1595  O  OE1 . GLN A 1  198  ? -9.486  -59.508  67.738  1.00 127.15 ?  198  GLN A OE1 1 
ATOM   1596  N  NE2 . GLN A 1  198  ? -7.829  -59.943  66.286  1.00 136.66 ?  198  GLN A NE2 1 
ATOM   1597  N  N   . LEU A 1  199  ? -12.901 -57.525  64.387  1.00 68.91  ?  199  LEU A N   1 
ATOM   1598  C  CA  . LEU A 1  199  ? -13.536 -58.210  63.265  1.00 66.14  ?  199  LEU A CA  1 
ATOM   1599  C  C   . LEU A 1  199  ? -13.931 -57.231  62.167  1.00 64.85  ?  199  LEU A C   1 
ATOM   1600  O  O   . LEU A 1  199  ? -13.847 -57.558  60.977  1.00 62.53  ?  199  LEU A O   1 
ATOM   1601  C  CB  . LEU A 1  199  ? -14.757 -58.991  63.749  1.00 56.38  ?  199  LEU A CB  1 
ATOM   1602  C  CG  . LEU A 1  199  ? -14.469 -60.273  64.531  1.00 54.38  ?  199  LEU A CG  1 
ATOM   1603  C  CD1 . LEU A 1  199  ? -15.765 -60.962  64.929  1.00 59.45  ?  199  LEU A CD1 1 
ATOM   1604  C  CD2 . LEU A 1  199  ? -13.590 -61.208  63.716  1.00 63.42  ?  199  LEU A CD2 1 
ATOM   1605  N  N   . VAL A 1  200  ? -14.371 -56.029  62.544  1.00 54.00  ?  200  VAL A N   1 
ATOM   1606  C  CA  . VAL A 1  200  ? -14.715 -55.021  61.545  1.00 49.82  ?  200  VAL A CA  1 
ATOM   1607  C  C   . VAL A 1  200  ? -13.476 -54.618  60.754  1.00 47.13  ?  200  VAL A C   1 
ATOM   1608  O  O   . VAL A 1  200  ? -13.532 -54.433  59.532  1.00 47.45  ?  200  VAL A O   1 
ATOM   1609  C  CB  . VAL A 1  200  ? -15.385 -53.810  62.221  1.00 42.94  ?  200  VAL A CB  1 
ATOM   1610  C  CG1 . VAL A 1  200  ? -15.327 -52.585  61.321  1.00 37.20  ?  200  VAL A CG1 1 
ATOM   1611  C  CG2 . VAL A 1  200  ? -16.824 -54.140  62.587  1.00 45.93  ?  200  VAL A CG2 1 
ATOM   1612  N  N   . ALA A 1  201  ? -12.334 -54.500  61.433  1.00 55.74  ?  201  ALA A N   1 
ATOM   1613  C  CA  . ALA A 1  201  ? -11.101 -54.140  60.743  1.00 56.43  ?  201  ALA A CA  1 
ATOM   1614  C  C   . ALA A 1  201  ? -10.593 -55.289  59.879  1.00 53.77  ?  201  ALA A C   1 
ATOM   1615  O  O   . ALA A 1  201  ? -10.060 -55.061  58.787  1.00 45.71  ?  201  ALA A O   1 
ATOM   1616  C  CB  . ALA A 1  201  ? -10.038 -53.716  61.755  1.00 57.07  ?  201  ALA A CB  1 
ATOM   1617  N  N   . GLU A 1  202  ? -10.750 -56.530  60.347  1.00 78.13  ?  202  GLU A N   1 
ATOM   1618  C  CA  . GLU A 1  202  ? -10.238 -57.670  59.592  1.00 89.38  ?  202  GLU A CA  1 
ATOM   1619  C  C   . GLU A 1  202  ? -11.113 -57.977  58.383  1.00 81.59  ?  202  GLU A C   1 
ATOM   1620  O  O   . GLU A 1  202  ? -10.599 -58.271  57.298  1.00 70.93  ?  202  GLU A O   1 
ATOM   1621  C  CB  . GLU A 1  202  ? -10.129 -58.897  60.496  1.00 84.52  ?  202  GLU A CB  1 
ATOM   1622  C  CG  . GLU A 1  202  ? -9.594  -60.136  59.790  1.00 93.55  ?  202  GLU A CG  1 
ATOM   1623  C  CD  . GLU A 1  202  ? -9.749  -61.396  60.618  1.00 103.86 ?  202  GLU A CD  1 
ATOM   1624  O  OE1 . GLU A 1  202  ? -10.005 -61.283  61.836  1.00 104.74 ?  202  GLU A OE1 1 
ATOM   1625  O  OE2 . GLU A 1  202  ? -9.616  -62.501  60.050  1.00 105.93 -1 202  GLU A OE2 1 
ATOM   1626  N  N   . TYR A 1  203  ? -12.435 -57.926  58.549  1.00 65.55  ?  203  TYR A N   1 
ATOM   1627  C  CA  . TYR A 1  203  ? -13.348 -58.225  57.453  1.00 56.82  ?  203  TYR A CA  1 
ATOM   1628  C  C   . TYR A 1  203  ? -13.595 -57.031  56.542  1.00 58.65  ?  203  TYR A C   1 
ATOM   1629  O  O   . TYR A 1  203  ? -14.247 -57.190  55.505  1.00 68.86  ?  203  TYR A O   1 
ATOM   1630  C  CB  . TYR A 1  203  ? -14.686 -58.732  57.998  1.00 60.78  ?  203  TYR A CB  1 
ATOM   1631  C  CG  . TYR A 1  203  ? -14.580 -59.991  58.828  1.00 64.60  ?  203  TYR A CG  1 
ATOM   1632  C  CD1 . TYR A 1  203  ? -13.540 -60.891  58.634  1.00 64.32  ?  203  TYR A CD1 1 
ATOM   1633  C  CD2 . TYR A 1  203  ? -15.522 -60.280  59.807  1.00 65.19  ?  203  TYR A CD2 1 
ATOM   1634  C  CE1 . TYR A 1  203  ? -13.440 -62.043  59.393  1.00 68.37  ?  203  TYR A CE1 1 
ATOM   1635  C  CE2 . TYR A 1  203  ? -15.431 -61.429  60.570  1.00 63.56  ?  203  TYR A CE2 1 
ATOM   1636  C  CZ  . TYR A 1  203  ? -14.389 -62.306  60.358  1.00 67.86  ?  203  TYR A CZ  1 
ATOM   1637  O  OH  . TYR A 1  203  ? -14.294 -63.450  61.116  1.00 72.64  ?  203  TYR A OH  1 
ATOM   1638  N  N   . GLY A 1  204  ? -13.098 -55.850  56.899  1.00 61.95  ?  204  GLY A N   1 
ATOM   1639  C  CA  . GLY A 1  204  ? -13.280 -54.685  56.055  1.00 62.99  ?  204  GLY A CA  1 
ATOM   1640  C  C   . GLY A 1  204  ? -14.703 -54.185  55.975  1.00 64.37  ?  204  GLY A C   1 
ATOM   1641  O  O   . GLY A 1  204  ? -15.115 -53.680  54.926  1.00 71.97  ?  204  GLY A O   1 
ATOM   1642  N  N   . ILE A 1  205  ? -15.475 -54.325  57.054  1.00 55.81  ?  205  ILE A N   1 
ATOM   1643  C  CA  . ILE A 1  205  ? -16.820 -53.762  57.086  1.00 58.48  ?  205  ILE A CA  1 
ATOM   1644  C  C   . ILE A 1  205  ? -16.716 -52.250  56.958  1.00 63.57  ?  205  ILE A C   1 
ATOM   1645  O  O   . ILE A 1  205  ? -16.020 -51.593  57.741  1.00 57.40  ?  205  ILE A O   1 
ATOM   1646  C  CB  . ILE A 1  205  ? -17.549 -54.174  58.369  1.00 61.05  ?  205  ILE A CB  1 
ATOM   1647  C  CG1 . ILE A 1  205  ? -17.612 -55.700  58.476  1.00 58.86  ?  205  ILE A CG1 1 
ATOM   1648  C  CG2 . ILE A 1  205  ? -18.945 -53.568  58.407  1.00 63.45  ?  205  ILE A CG2 1 
ATOM   1649  C  CD1 . ILE A 1  205  ? -18.506 -56.202  59.590  1.00 54.58  ?  205  ILE A CD1 1 
ATOM   1650  N  N   . MET A 1  206  ? -17.403 -51.692  55.964  1.00 74.15  ?  206  MET A N   1 
ATOM   1651  C  CA  . MET A 1  206  ? -17.225 -50.290  55.635  1.00 68.45  ?  206  MET A CA  1 
ATOM   1652  C  C   . MET A 1  206  ? -17.828 -49.403  56.722  1.00 72.13  ?  206  MET A C   1 
ATOM   1653  O  O   . MET A 1  206  ? -18.727 -49.824  57.452  1.00 74.70  ?  206  MET A O   1 
ATOM   1654  C  CB  . MET A 1  206  ? -17.852 -49.980  54.277  1.00 60.99  ?  206  MET A CB  1 
ATOM   1655  C  CG  . MET A 1  206  ? -16.980 -50.386  53.101  1.00 67.28  ?  206  MET A CG  1 
ATOM   1656  S  SD  . MET A 1  206  ? -15.478 -49.393  52.965  1.00 71.77  ?  206  MET A SD  1 
ATOM   1657  C  CE  . MET A 1  206  ? -16.105 -47.866  52.270  1.00 75.53  ?  206  MET A CE  1 
ATOM   1658  N  N   . PRO A 1  207  ? -17.344 -48.168  56.849  1.00 54.20  ?  207  PRO A N   1 
ATOM   1659  C  CA  . PRO A 1  207  ? -17.822 -47.278  57.916  1.00 54.00  ?  207  PRO A CA  1 
ATOM   1660  C  C   . PRO A 1  207  ? -19.286 -46.923  57.733  1.00 58.53  ?  207  PRO A C   1 
ATOM   1661  O  O   . PRO A 1  207  ? -19.876 -47.201  56.677  1.00 56.40  ?  207  PRO A O   1 
ATOM   1662  C  CB  . PRO A 1  207  ? -16.922 -46.042  57.759  1.00 62.21  ?  207  PRO A CB  1 
ATOM   1663  C  CG  . PRO A 1  207  ? -16.542 -46.056  56.317  1.00 69.68  ?  207  PRO A CG  1 
ATOM   1664  C  CD  . PRO A 1  207  ? -16.313 -47.510  56.026  1.00 62.46  ?  207  PRO A CD  1 
ATOM   1665  N  N   . PRO A 1  208  ? -19.914 -46.311  58.743  1.00 63.42  ?  208  PRO A N   1 
ATOM   1666  C  CA  . PRO A 1  208  ? -21.339 -45.956  58.622  1.00 62.39  ?  208  PRO A CA  1 
ATOM   1667  C  C   . PRO A 1  208  ? -21.648 -44.958  57.516  1.00 60.80  ?  208  PRO A C   1 
ATOM   1668  O  O   . PRO A 1  208  ? -22.824 -44.812  57.161  1.00 52.16  ?  208  PRO A O   1 
ATOM   1669  C  CB  . PRO A 1  208  ? -21.669 -45.365  59.999  1.00 56.99  ?  208  PRO A CB  1 
ATOM   1670  C  CG  . PRO A 1  208  ? -20.683 -45.997  60.914  1.00 70.77  ?  208  PRO A CG  1 
ATOM   1671  C  CD  . PRO A 1  208  ? -19.417 -46.090  60.113  1.00 73.17  ?  208  PRO A CD  1 
ATOM   1672  N  N   . ASP A 1  209  ? -20.648 -44.266  56.967  1.00 81.98  ?  209  ASP A N   1 
ATOM   1673  C  CA  . ASP A 1  209  ? -20.923 -43.263  55.942  1.00 72.70  ?  209  ASP A CA  1 
ATOM   1674  C  C   . ASP A 1  209  ? -21.523 -43.893  54.692  1.00 79.17  ?  209  ASP A C   1 
ATOM   1675  O  O   . ASP A 1  209  ? -22.460 -43.343  54.100  1.00 88.97  ?  209  ASP A O   1 
ATOM   1676  C  CB  . ASP A 1  209  ? -19.645 -42.497  55.599  1.00 77.68  ?  209  ASP A CB  1 
ATOM   1677  C  CG  . ASP A 1  209  ? -18.935 -41.966  56.829  1.00 98.19  ?  209  ASP A CG  1 
ATOM   1678  O  OD1 . ASP A 1  209  ? -19.522 -42.034  57.930  1.00 99.34  ?  209  ASP A OD1 1 
ATOM   1679  O  OD2 . ASP A 1  209  ? -17.792 -41.480  56.695  1.00 106.86 -1 209  ASP A OD2 1 
ATOM   1680  N  N   . GLN A 1  210  ? -20.999 -45.045  54.271  1.00 53.94  ?  210  GLN A N   1 
ATOM   1681  C  CA  . GLN A 1  210  ? -21.548 -45.715  53.098  1.00 40.94  ?  210  GLN A CA  1 
ATOM   1682  C  C   . GLN A 1  210  ? -22.756 -46.577  53.450  1.00 40.85  ?  210  GLN A C   1 
ATOM   1683  O  O   . GLN A 1  210  ? -23.762 -46.560  52.732  1.00 41.56  ?  210  GLN A O   1 
ATOM   1684  C  CB  . GLN A 1  210  ? -20.474 -46.570  52.424  1.00 42.55  ?  210  GLN A CB  1 
ATOM   1685  C  CG  . GLN A 1  210  ? -21.014 -47.409  51.283  1.00 49.04  ?  210  GLN A CG  1 
ATOM   1686  C  CD  . GLN A 1  210  ? -20.299 -48.732  51.138  1.00 52.01  ?  210  GLN A CD  1 
ATOM   1687  O  OE1 . GLN A 1  210  ? -20.930 -49.785  51.066  1.00 62.89  ?  210  GLN A OE1 1 
ATOM   1688  N  NE2 . GLN A 1  210  ? -18.976 -48.686  51.080  1.00 53.29  ?  210  GLN A NE2 1 
ATOM   1689  N  N   . LEU A 1  211  ? -22.679 -47.334  54.549  1.00 46.56  ?  211  LEU A N   1 
ATOM   1690  C  CA  . LEU A 1  211  ? -23.743 -48.273  54.887  1.00 48.33  ?  211  LEU A CA  1 
ATOM   1691  C  C   . LEU A 1  211  ? -25.064 -47.582  55.201  1.00 45.67  ?  211  LEU A C   1 
ATOM   1692  O  O   . LEU A 1  211  ? -26.110 -48.238  55.179  1.00 39.40  ?  211  LEU A O   1 
ATOM   1693  C  CB  . LEU A 1  211  ? -23.322 -49.145  56.071  1.00 38.78  ?  211  LEU A CB  1 
ATOM   1694  C  CG  . LEU A 1  211  ? -22.139 -50.078  55.809  1.00 36.67  ?  211  LEU A CG  1 
ATOM   1695  C  CD1 . LEU A 1  211  ? -21.872 -50.967  57.013  1.00 40.96  ?  211  LEU A CD1 1 
ATOM   1696  C  CD2 . LEU A 1  211  ? -22.378 -50.909  54.558  1.00 42.51  ?  211  LEU A CD2 1 
ATOM   1697  N  N   . THR A 1  212  ? -25.043 -46.285  55.493  1.00 78.50  ?  212  THR A N   1 
ATOM   1698  C  CA  . THR A 1  212  ? -26.265 -45.528  55.728  1.00 79.16  ?  212  THR A CA  1 
ATOM   1699  C  C   . THR A 1  212  ? -26.809 -44.873  54.467  1.00 78.80  ?  212  THR A C   1 
ATOM   1700  O  O   . THR A 1  212  ? -27.803 -44.143  54.547  1.00 73.24  ?  212  THR A O   1 
ATOM   1701  C  CB  . THR A 1  212  ? -26.031 -44.455  56.795  1.00 71.56  ?  212  THR A CB  1 
ATOM   1702  O  OG1 . THR A 1  212  ? -24.841 -43.721  56.481  1.00 77.11  ?  212  THR A OG1 1 
ATOM   1703  C  CG2 . THR A 1  212  ? -25.885 -45.094  58.163  1.00 72.17  ?  212  THR A CG2 1 
ATOM   1704  N  N   . ASN A 1  213  ? -26.187 -45.108  53.315  1.00 58.26  ?  213  ASN A N   1 
ATOM   1705  C  CA  . ASN A 1  213  ? -26.678 -44.530  52.073  1.00 53.66  ?  213  ASN A CA  1 
ATOM   1706  C  C   . ASN A 1  213  ? -28.007 -45.158  51.677  1.00 49.41  ?  213  ASN A C   1 
ATOM   1707  O  O   . ASN A 1  213  ? -28.317 -46.298  52.033  1.00 49.49  ?  213  ASN A O   1 
ATOM   1708  C  CB  . ASN A 1  213  ? -25.658 -44.715  50.953  1.00 47.04  ?  213  ASN A CB  1 
ATOM   1709  C  CG  . ASN A 1  213  ? -24.393 -43.918  51.183  1.00 52.78  ?  213  ASN A CG  1 
ATOM   1710  O  OD1 . ASN A 1  213  ? -23.324 -44.280  50.697  1.00 46.66  ?  213  ASN A OD1 1 
ATOM   1711  N  ND2 . ASN A 1  213  ? -24.508 -42.822  51.925  1.00 63.00  ?  213  ASN A ND2 1 
ATOM   1712  N  N   . CYS A 1  214  ? -28.796 -44.392  50.925  1.00 40.71  ?  214  CYS A N   1 
ATOM   1713  C  CA  . CYS A 1  214  ? -30.133 -44.843  50.559  1.00 36.21  ?  214  CYS A CA  1 
ATOM   1714  C  C   . CYS A 1  214  ? -30.081 -46.011  49.583  1.00 39.68  ?  214  CYS A C   1 
ATOM   1715  O  O   . CYS A 1  214  ? -30.845 -46.974  49.719  1.00 36.56  ?  214  CYS A O   1 
ATOM   1716  C  CB  . CYS A 1  214  ? -30.924 -43.685  49.957  1.00 42.10  ?  214  CYS A CB  1 
ATOM   1717  S  SG  . CYS A 1  214  ? -31.051 -42.229  51.011  1.00 46.25  ?  214  CYS A SG  1 
ATOM   1718  N  N   . TYR A 1  215  ? -29.190 -45.944  48.593  1.00 61.66  ?  215  TYR A N   1 
ATOM   1719  C  CA  . TYR A 1  215  ? -29.165 -46.932  47.523  1.00 60.54  ?  215  TYR A CA  1 
ATOM   1720  C  C   . TYR A 1  215  ? -28.533 -48.252  47.935  1.00 59.39  ?  215  TYR A C   1 
ATOM   1721  O  O   . TYR A 1  215  ? -28.536 -49.193  47.134  1.00 67.44  ?  215  TYR A O   1 
ATOM   1722  C  CB  . TYR A 1  215  ? -28.436 -46.368  46.302  1.00 58.71  ?  215  TYR A CB  1 
ATOM   1723  C  CG  . TYR A 1  215  ? -29.353 -45.628  45.355  1.00 56.04  ?  215  TYR A CG  1 
ATOM   1724  C  CD1 . TYR A 1  215  ? -30.724 -45.598  45.572  1.00 52.18  ?  215  TYR A CD1 1 
ATOM   1725  C  CD2 . TYR A 1  215  ? -28.851 -44.960  44.248  1.00 55.99  ?  215  TYR A CD2 1 
ATOM   1726  C  CE1 . TYR A 1  215  ? -31.568 -44.927  44.713  1.00 52.98  ?  215  TYR A CE1 1 
ATOM   1727  C  CE2 . TYR A 1  215  ? -29.688 -44.286  43.382  1.00 52.36  ?  215  TYR A CE2 1 
ATOM   1728  C  CZ  . TYR A 1  215  ? -31.045 -44.272  43.621  1.00 52.72  ?  215  TYR A CZ  1 
ATOM   1729  O  OH  . TYR A 1  215  ? -31.884 -43.600  42.762  1.00 54.94  ?  215  TYR A OH  1 
ATOM   1730  N  N   . VAL A 1  216  ? -27.991 -48.351  49.151  1.00 37.64  ?  216  VAL A N   1 
ATOM   1731  C  CA  . VAL A 1  216  ? -27.563 -49.654  49.647  1.00 37.76  ?  216  VAL A CA  1 
ATOM   1732  C  C   . VAL A 1  216  ? -28.767 -50.573  49.805  1.00 51.48  ?  216  VAL A C   1 
ATOM   1733  O  O   . VAL A 1  216  ? -28.660 -51.791  49.622  1.00 61.64  ?  216  VAL A O   1 
ATOM   1734  C  CB  . VAL A 1  216  ? -26.781 -49.491  50.966  1.00 35.23  ?  216  VAL A CB  1 
ATOM   1735  C  CG1 . VAL A 1  216  ? -26.439 -50.847  51.566  1.00 38.24  ?  216  VAL A CG1 1 
ATOM   1736  C  CG2 . VAL A 1  216  ? -25.516 -48.678  50.732  1.00 40.29  ?  216  VAL A CG2 1 
ATOM   1737  N  N   . CYS A 1  217  ? -29.935 -50.007  50.109  1.00 49.69  ?  217  CYS A N   1 
ATOM   1738  C  CA  . CYS A 1  217  ? -31.161 -50.781  50.273  1.00 50.14  ?  217  CYS A CA  1 
ATOM   1739  C  C   . CYS A 1  217  ? -32.161 -50.458  49.169  1.00 57.76  ?  217  CYS A C   1 
ATOM   1740  O  O   . CYS A 1  217  ? -32.403 -51.291  48.293  1.00 69.00  ?  217  CYS A O   1 
ATOM   1741  C  CB  . CYS A 1  217  ? -31.767 -50.523  51.651  1.00 58.49  ?  217  CYS A CB  1 
ATOM   1742  S  SG  . CYS A 1  217  ? -30.609 -50.793  52.991  1.00 63.64  ?  217  CYS A SG  1 
ATOM   1743  N  N   . HIS A 1  218  ? -32.749 -49.266  49.186  1.00 54.36  ?  218  HIS A N   1 
ATOM   1744  C  CA  . HIS A 1  218  ? -33.775 -48.922  48.213  1.00 57.59  ?  218  HIS A CA  1 
ATOM   1745  C  C   . HIS A 1  218  ? -33.161 -48.678  46.842  1.00 55.04  ?  218  HIS A C   1 
ATOM   1746  O  O   . HIS A 1  218  ? -32.062 -48.128  46.723  1.00 47.80  ?  218  HIS A O   1 
ATOM   1747  C  CB  . HIS A 1  218  ? -34.541 -47.683  48.671  1.00 52.82  ?  218  HIS A CB  1 
ATOM   1748  C  CG  . HIS A 1  218  ? -34.972 -47.741  50.102  1.00 59.34  ?  218  HIS A CG  1 
ATOM   1749  N  ND1 . HIS A 1  218  ? -35.973 -48.580  50.542  1.00 60.96  ?  218  HIS A ND1 1 
ATOM   1750  C  CD2 . HIS A 1  218  ? -34.529 -47.076  51.195  1.00 67.70  ?  218  HIS A CD2 1 
ATOM   1751  C  CE1 . HIS A 1  218  ? -36.133 -48.423  51.844  1.00 72.56  ?  218  HIS A CE1 1 
ATOM   1752  N  NE2 . HIS A 1  218  ? -35.269 -47.517  52.264  1.00 67.44  ?  218  HIS A NE2 1 
ATOM   1753  N  N   . ARG A 1  219  ? -33.879 -49.094  45.805  1.00 60.78  ?  219  ARG A N   1 
ATOM   1754  C  CA  . ARG A 1  219  ? -33.439 -48.897  44.431  1.00 53.43  ?  219  ARG A CA  1 
ATOM   1755  C  C   . ARG A 1  219  ? -34.618 -48.487  43.558  1.00 55.36  ?  219  ARG A C   1 
ATOM   1756  O  O   . ARG A 1  219  ? -35.150 -49.297  42.801  1.00 61.35  ?  219  ARG A O   1 
ATOM   1757  C  CB  . ARG A 1  219  ? -32.788 -50.168  43.881  1.00 50.69  ?  219  ARG A CB  1 
ATOM   1758  C  CG  . ARG A 1  219  ? -31.522 -50.584  44.611  1.00 52.12  ?  219  ARG A CG  1 
ATOM   1759  C  CD  . ARG A 1  219  ? -30.601 -51.378  43.710  1.00 53.86  ?  219  ARG A CD  1 
ATOM   1760  N  NE  . ARG A 1  219  ? -31.191 -52.654  43.327  1.00 60.01  ?  219  ARG A NE  1 
ATOM   1761  C  CZ  . ARG A 1  219  ? -30.980 -53.797  43.966  1.00 63.33  ?  219  ARG A CZ  1 
ATOM   1762  N  NH1 . ARG A 1  219  ? -30.207 -53.856  45.039  1.00 52.31  ?  219  ARG A NH1 1 
ATOM   1763  N  NH2 . ARG A 1  219  ? -31.559 -54.906  43.518  1.00 66.83  ?  219  ARG A NH2 1 
ATOM   1764  N  N   . ALA B 2  75   ? -57.006 -53.910  56.084  1.00 191.55 ?  75   ALA B N   1 
ATOM   1765  C  CA  . ALA B 2  75   ? -57.075 -52.680  56.863  1.00 191.17 ?  75   ALA B CA  1 
ATOM   1766  C  C   . ALA B 2  75   ? -56.013 -52.666  57.959  1.00 191.21 ?  75   ALA B C   1 
ATOM   1767  O  O   . ALA B 2  75   ? -55.506 -51.608  58.330  1.00 197.70 ?  75   ALA B O   1 
ATOM   1768  C  CB  . ALA B 2  75   ? -58.463 -52.511  57.466  1.00 192.58 ?  75   ALA B CB  1 
ATOM   1769  N  N   . CYS B 2  76   ? -55.678 -53.846  58.469  1.00 121.26 ?  76   CYS B N   1 
ATOM   1770  C  CA  . CYS B 2  76   ? -54.718 -54.001  59.553  1.00 113.07 ?  76   CYS B CA  1 
ATOM   1771  C  C   . CYS B 2  76   ? -53.537 -54.849  59.086  1.00 105.59 ?  76   CYS B C   1 
ATOM   1772  O  O   . CYS B 2  76   ? -53.419 -55.204  57.910  1.00 103.56 ?  76   CYS B O   1 
ATOM   1773  C  CB  . CYS B 2  76   ? -55.384 -54.629  60.782  1.00 106.54 ?  76   CYS B CB  1 
ATOM   1774  S  SG  . CYS B 2  76   ? -56.955 -53.872  61.260  1.00 102.97 ?  76   CYS B SG  1 
ATOM   1775  N  N   . THR B 2  77   ? -52.655 -55.164  60.034  1.00 124.51 ?  77   THR B N   1 
ATOM   1776  C  CA  . THR B 2  77   ? -51.507 -56.053  59.865  1.00 124.24 ?  77   THR B CA  1 
ATOM   1777  C  C   . THR B 2  77   ? -50.483 -55.546  58.853  1.00 123.82 ?  77   THR B C   1 
ATOM   1778  O  O   . THR B 2  77   ? -49.631 -56.327  58.408  1.00 124.13 ?  77   THR B O   1 
ATOM   1779  C  CB  . THR B 2  77   ? -51.938 -57.477  59.483  1.00 127.30 ?  77   THR B CB  1 
ATOM   1780  O  OG1 . THR B 2  77   ? -52.302 -57.516  58.096  1.00 131.80 ?  77   THR B OG1 1 
ATOM   1781  C  CG2 . THR B 2  77   ? -53.115 -57.937  60.342  1.00 122.69 ?  77   THR B CG2 1 
ATOM   1782  N  N   . TYR B 2  78   ? -50.551 -54.269  58.463  1.00 92.53  ?  78   TYR B N   1 
ATOM   1783  C  CA  . TYR B 2  78   ? -49.494 -53.613  57.692  1.00 82.71  ?  78   TYR B CA  1 
ATOM   1784  C  C   . TYR B 2  78   ? -49.317 -54.198  56.292  1.00 77.27  ?  78   TYR B C   1 
ATOM   1785  O  O   . TYR B 2  78   ? -49.211 -53.449  55.316  1.00 79.52  ?  78   TYR B O   1 
ATOM   1786  C  CB  . TYR B 2  78   ? -48.176 -53.673  58.474  1.00 85.10  ?  78   TYR B CB  1 
ATOM   1787  C  CG  . TYR B 2  78   ? -46.995 -52.994  57.816  1.00 76.53  ?  78   TYR B CG  1 
ATOM   1788  C  CD1 . TYR B 2  78   ? -46.744 -51.644  58.019  1.00 76.51  ?  78   TYR B CD1 1 
ATOM   1789  C  CD2 . TYR B 2  78   ? -46.109 -53.714  57.025  1.00 77.91  ?  78   TYR B CD2 1 
ATOM   1790  C  CE1 . TYR B 2  78   ? -45.655 -51.024  57.432  1.00 75.67  ?  78   TYR B CE1 1 
ATOM   1791  C  CE2 . TYR B 2  78   ? -45.019 -53.104  56.435  1.00 76.84  ?  78   TYR B CE2 1 
ATOM   1792  C  CZ  . TYR B 2  78   ? -44.795 -51.760  56.641  1.00 69.81  ?  78   TYR B CZ  1 
ATOM   1793  O  OH  . TYR B 2  78   ? -43.709 -51.151  56.054  1.00 64.35  ?  78   TYR B OH  1 
ATOM   1794  N  N   . GLN B 2  79   ? -49.278 -55.522  56.178  1.00 83.33  ?  79   GLN B N   1 
ATOM   1795  C  CA  . GLN B 2  79   ? -49.089 -56.212  54.911  1.00 79.60  ?  79   GLN B CA  1 
ATOM   1796  C  C   . GLN B 2  79   ? -49.919 -57.487  54.907  1.00 85.63  ?  79   GLN B C   1 
ATOM   1797  O  O   . GLN B 2  79   ? -50.197 -58.049  55.973  1.00 86.18  ?  79   GLN B O   1 
ATOM   1798  C  CB  . GLN B 2  79   ? -47.611 -56.557  54.671  1.00 83.61  ?  79   GLN B CB  1 
ATOM   1799  C  CG  . GLN B 2  79   ? -47.043 -56.008  53.372  1.00 78.59  ?  79   GLN B CG  1 
ATOM   1800  C  CD  . GLN B 2  79   ? -45.540 -56.168  53.280  1.00 72.10  ?  79   GLN B CD  1 
ATOM   1801  O  OE1 . GLN B 2  79   ? -44.853 -56.280  54.296  1.00 72.12  ?  79   GLN B OE1 1 
ATOM   1802  N  NE2 . GLN B 2  79   ? -45.022 -56.203  52.057  1.00 70.29  ?  79   GLN B NE2 1 
ATOM   1803  N  N   . PRO B 2  80   ? -50.330 -57.969  53.723  1.00 84.34  ?  80   PRO B N   1 
ATOM   1804  C  CA  . PRO B 2  80   ? -51.099 -59.220  53.669  1.00 83.04  ?  80   PRO B CA  1 
ATOM   1805  C  C   . PRO B 2  80   ? -50.248 -60.439  53.985  1.00 95.39  ?  80   PRO B C   1 
ATOM   1806  O  O   . PRO B 2  80   ? -49.163 -60.315  54.560  1.00 107.34 ?  80   PRO B O   1 
ATOM   1807  C  CB  . PRO B 2  80   ? -51.611 -59.259  52.224  1.00 85.48  ?  80   PRO B CB  1 
ATOM   1808  C  CG  . PRO B 2  80   ? -50.653 -58.414  51.463  1.00 87.92  ?  80   PRO B CG  1 
ATOM   1809  C  CD  . PRO B 2  80   ? -50.228 -57.329  52.401  1.00 82.99  ?  80   PRO B CD  1 
ATOM   1810  N  N   . ARG B 2  81   ? -50.726 -61.623  53.603  1.00 112.75 ?  81   ARG B N   1 
ATOM   1811  C  CA  . ARG B 2  81   ? -50.011 -62.845  53.952  1.00 124.10 ?  81   ARG B CA  1 
ATOM   1812  C  C   . ARG B 2  81   ? -48.788 -63.060  53.067  1.00 122.29 ?  81   ARG B C   1 
ATOM   1813  O  O   . ARG B 2  81   ? -47.730 -63.463  53.564  1.00 133.83 ?  81   ARG B O   1 
ATOM   1814  C  CB  . ARG B 2  81   ? -50.952 -64.048  53.870  1.00 126.40 ?  81   ARG B CB  1 
ATOM   1815  C  CG  . ARG B 2  81   ? -52.076 -64.011  54.892  1.00 135.56 ?  81   ARG B CG  1 
ATOM   1816  C  CD  . ARG B 2  81   ? -52.800 -65.341  54.981  1.00 140.19 ?  81   ARG B CD  1 
ATOM   1817  N  NE  . ARG B 2  81   ? -52.028 -66.324  55.731  1.00 145.40 ?  81   ARG B NE  1 
ATOM   1818  C  CZ  . ARG B 2  81   ? -52.046 -66.439  57.052  1.00 137.30 ?  81   ARG B CZ  1 
ATOM   1819  N  NH1 . ARG B 2  81   ? -52.784 -65.640  57.806  1.00 126.93 ?  81   ARG B NH1 1 
ATOM   1820  N  NH2 . ARG B 2  81   ? -51.303 -67.378  57.632  1.00 136.02 ?  81   ARG B NH2 1 
ATOM   1821  N  N   . GLN B 2  82   ? -48.914 -62.792  51.764  1.00 72.91  ?  82   GLN B N   1 
ATOM   1822  C  CA  . GLN B 2  82   ? -47.836 -62.990  50.799  1.00 72.76  ?  82   GLN B CA  1 
ATOM   1823  C  C   . GLN B 2  82   ? -47.316 -64.423  50.830  1.00 72.59  ?  82   GLN B C   1 
ATOM   1824  O  O   . GLN B 2  82   ? -46.330 -64.716  51.513  1.00 76.44  ?  82   GLN B O   1 
ATOM   1825  C  CB  . GLN B 2  82   ? -46.683 -62.012  51.055  1.00 80.48  ?  82   GLN B CB  1 
ATOM   1826  C  CG  . GLN B 2  82   ? -46.958 -60.567  50.659  1.00 88.58  ?  82   GLN B CG  1 
ATOM   1827  C  CD  . GLN B 2  82   ? -45.696 -59.721  50.643  1.00 75.73  ?  82   GLN B CD  1 
ATOM   1828  O  OE1 . GLN B 2  82   ? -45.726 -58.530  50.953  1.00 55.43  ?  82   GLN B OE1 1 
ATOM   1829  N  NE2 . GLN B 2  82   ? -44.577 -60.338  50.280  1.00 82.35  ?  82   GLN B NE2 1 
ATOM   1830  N  N   . TYR B 2  83   ? -47.965 -65.320  50.091  1.00 74.94  ?  83   TYR B N   1 
ATOM   1831  C  CA  . TYR B 2  83   ? -47.525 -66.706  50.050  1.00 68.20  ?  83   TYR B CA  1 
ATOM   1832  C  C   . TYR B 2  83   ? -46.262 -66.844  49.200  1.00 54.28  ?  83   TYR B C   1 
ATOM   1833  O  O   . TYR B 2  83   ? -45.883 -65.951  48.438  1.00 50.14  ?  83   TYR B O   1 
ATOM   1834  C  CB  . TYR B 2  83   ? -48.633 -67.611  49.508  1.00 71.81  ?  83   TYR B CB  1 
ATOM   1835  C  CG  . TYR B 2  83   ? -49.907 -67.598  50.327  1.00 81.00  ?  83   TYR B CG  1 
ATOM   1836  C  CD1 . TYR B 2  83   ? -50.851 -66.591  50.168  1.00 85.28  ?  83   TYR B CD1 1 
ATOM   1837  C  CD2 . TYR B 2  83   ? -50.163 -68.593  51.262  1.00 83.18  ?  83   TYR B CD2 1 
ATOM   1838  C  CE1 . TYR B 2  83   ? -52.014 -66.576  50.916  1.00 88.78  ?  83   TYR B CE1 1 
ATOM   1839  C  CE2 . TYR B 2  83   ? -51.323 -68.586  52.014  1.00 89.88  ?  83   TYR B CE2 1 
ATOM   1840  C  CZ  . TYR B 2  83   ? -52.245 -67.575  51.837  1.00 92.75  ?  83   TYR B CZ  1 
ATOM   1841  O  OH  . TYR B 2  83   ? -53.401 -67.563  52.583  1.00 97.65  ?  83   TYR B OH  1 
ATOM   1842  N  N   . ILE B 2  84   ? -45.606 -67.992  49.343  1.00 61.40  ?  84   ILE B N   1 
ATOM   1843  C  CA  . ILE B 2  84   ? -44.390 -68.305  48.602  1.00 55.40  ?  84   ILE B CA  1 
ATOM   1844  C  C   . ILE B 2  84   ? -44.488 -69.740  48.103  1.00 62.89  ?  84   ILE B C   1 
ATOM   1845  O  O   . ILE B 2  84   ? -44.795 -70.654  48.875  1.00 71.16  ?  84   ILE B O   1 
ATOM   1846  C  CB  . ILE B 2  84   ? -43.125 -68.097  49.461  1.00 59.32  ?  84   ILE B CB  1 
ATOM   1847  C  CG1 . ILE B 2  84   ? -41.886 -68.618  48.732  1.00 55.38  ?  84   ILE B CG1 1 
ATOM   1848  C  CG2 . ILE B 2  84   ? -43.282 -68.744  50.834  1.00 71.15  ?  84   ILE B CG2 1 
ATOM   1849  C  CD1 . ILE B 2  84   ? -40.587 -68.142  49.333  1.00 64.24  ?  84   ILE B CD1 1 
ATOM   1850  N  N   . ALA B 2  85   ? -44.242 -69.935  46.811  1.00 51.17  ?  85   ALA B N   1 
ATOM   1851  C  CA  . ALA B 2  85   ? -44.391 -71.242  46.170  1.00 53.17  ?  85   ALA B CA  1 
ATOM   1852  C  C   . ALA B 2  85   ? -43.066 -71.676  45.562  1.00 45.91  ?  85   ALA B C   1 
ATOM   1853  O  O   . ALA B 2  85   ? -42.703 -71.218  44.464  1.00 43.77  ?  85   ALA B O   1 
ATOM   1854  C  CB  . ALA B 2  85   ? -45.480 -71.195  45.100  1.00 51.83  ?  85   ALA B CB  1 
ATOM   1855  N  N   . PRO B 2  86   ? -42.309 -72.549  46.228  1.00 64.41  ?  86   PRO B N   1 
ATOM   1856  C  CA  . PRO B 2  86   ? -41.037 -73.006  45.655  1.00 67.01  ?  86   PRO B CA  1 
ATOM   1857  C  C   . PRO B 2  86   ? -41.230 -74.125  44.646  1.00 63.00  ?  86   PRO B C   1 
ATOM   1858  O  O   . PRO B 2  86   ? -42.355 -74.402  44.221  1.00 58.80  ?  86   PRO B O   1 
ATOM   1859  C  CB  . PRO B 2  86   ? -40.260 -73.486  46.884  1.00 67.37  ?  86   PRO B CB  1 
ATOM   1860  C  CG  . PRO B 2  86   ? -41.323 -73.980  47.799  1.00 62.77  ?  86   PRO B CG  1 
ATOM   1861  C  CD  . PRO B 2  86   ? -42.543 -73.115  47.568  1.00 63.02  ?  86   PRO B CD  1 
ATOM   1862  N  N   . PHE B 2  87   ? -40.137 -74.780  44.267  1.00 81.97  ?  87   PHE B N   1 
ATOM   1863  C  CA  . PHE B 2  87   ? -40.191 -75.852  43.287  1.00 84.57  ?  87   PHE B CA  1 
ATOM   1864  C  C   . PHE B 2  87   ? -40.642 -77.153  43.947  1.00 89.53  ?  87   PHE B C   1 
ATOM   1865  O  O   . PHE B 2  87   ? -40.865 -77.229  45.158  1.00 92.04  ?  87   PHE B O   1 
ATOM   1866  C  CB  . PHE B 2  87   ? -38.827 -76.039  42.625  1.00 81.49  ?  87   PHE B CB  1 
ATOM   1867  C  CG  . PHE B 2  87   ? -38.574 -75.105  41.480  1.00 78.90  ?  87   PHE B CG  1 
ATOM   1868  C  CD1 . PHE B 2  87   ? -39.198 -75.298  40.261  1.00 84.17  ?  87   PHE B CD1 1 
ATOM   1869  C  CD2 . PHE B 2  87   ? -37.701 -74.040  41.621  1.00 79.82  ?  87   PHE B CD2 1 
ATOM   1870  C  CE1 . PHE B 2  87   ? -38.963 -74.439  39.205  1.00 72.92  ?  87   PHE B CE1 1 
ATOM   1871  C  CE2 . PHE B 2  87   ? -37.461 -73.178  40.570  1.00 66.76  ?  87   PHE B CE2 1 
ATOM   1872  C  CZ  . PHE B 2  87   ? -38.093 -73.378  39.360  1.00 67.87  ?  87   PHE B CZ  1 
ATOM   1873  N  N   . ASP B 2  88   ? -40.791 -78.191  43.128  1.00 96.39  ?  88   ASP B N   1 
ATOM   1874  C  CA  . ASP B 2  88   ? -40.877 -79.563  43.607  1.00 99.41  ?  88   ASP B CA  1 
ATOM   1875  C  C   . ASP B 2  88   ? -39.620 -80.361  43.313  1.00 101.11 ?  88   ASP B C   1 
ATOM   1876  O  O   . ASP B 2  88   ? -39.313 -81.305  44.043  1.00 97.81  ?  88   ASP B O   1 
ATOM   1877  C  CB  . ASP B 2  88   ? -42.082 -80.277  42.984  1.00 107.08 ?  88   ASP B CB  1 
ATOM   1878  C  CG  . ASP B 2  88   ? -41.979 -80.380  41.477  1.00 109.90 ?  88   ASP B CG  1 
ATOM   1879  O  OD1 . ASP B 2  88   ? -41.495 -79.416  40.848  1.00 106.61 ?  88   ASP B OD1 1 
ATOM   1880  O  OD2 . ASP B 2  88   ? -42.379 -81.425  40.921  1.00 108.40 -1 88   ASP B OD2 1 
ATOM   1881  N  N   . ARG B 2  89   ? -38.896 -79.998  42.255  1.00 79.77  ?  89   ARG B N   1 
ATOM   1882  C  CA  . ARG B 2  89   ? -37.578 -80.535  41.951  1.00 78.11  ?  89   ARG B CA  1 
ATOM   1883  C  C   . ARG B 2  89   ? -36.699 -79.378  41.504  1.00 72.54  ?  89   ARG B C   1 
ATOM   1884  O  O   . ARG B 2  89   ? -37.062 -78.644  40.581  1.00 63.02  ?  89   ARG B O   1 
ATOM   1885  C  CB  . ARG B 2  89   ? -37.643 -81.613  40.863  1.00 83.11  ?  89   ARG B CB  1 
ATOM   1886  C  CG  . ARG B 2  89   ? -38.307 -82.906  41.304  1.00 84.87  ?  89   ARG B CG  1 
ATOM   1887  C  CD  . ARG B 2  89   ? -38.611 -83.804  40.116  1.00 88.54  ?  89   ARG B CD  1 
ATOM   1888  N  NE  . ARG B 2  89   ? -39.351 -84.996  40.510  1.00 99.17  ?  89   ARG B NE  1 
ATOM   1889  C  CZ  . ARG B 2  89   ? -40.673 -85.071  40.570  1.00 93.67  ?  89   ARG B CZ  1 
ATOM   1890  N  NH1 . ARG B 2  89   ? -41.438 -84.032  40.275  1.00 88.13  ?  89   ARG B NH1 1 
ATOM   1891  N  NH2 . ARG B 2  89   ? -41.243 -86.215  40.937  1.00 92.71  ?  89   ARG B NH2 1 
ATOM   1892  N  N   . GLN B 2  90   ? -35.558 -79.213  42.161  1.00 80.85  ?  90   GLN B N   1 
ATOM   1893  C  CA  . GLN B 2  90   ? -34.716 -78.059  41.894  1.00 75.61  ?  90   GLN B CA  1 
ATOM   1894  C  C   . GLN B 2  90   ? -34.010 -78.208  40.548  1.00 76.48  ?  90   GLN B C   1 
ATOM   1895  O  O   . GLN B 2  90   ? -33.611 -79.316  40.174  1.00 79.82  ?  90   GLN B O   1 
ATOM   1896  C  CB  . GLN B 2  90   ? -33.681 -77.885  43.005  1.00 82.03  ?  90   GLN B CB  1 
ATOM   1897  C  CG  . GLN B 2  90   ? -34.208 -77.175  44.241  1.00 85.69  ?  90   GLN B CG  1 
ATOM   1898  C  CD  . GLN B 2  90   ? -34.269 -75.671  44.065  1.00 81.79  ?  90   GLN B CD  1 
ATOM   1899  O  OE1 . GLN B 2  90   ? -35.036 -74.986  44.742  1.00 88.39  ?  90   GLN B OE1 1 
ATOM   1900  N  NE2 . GLN B 2  90   ? -33.458 -75.149  43.153  1.00 71.60  ?  90   GLN B NE2 1 
ATOM   1901  N  N   . PRO B 2  91   ? -33.862 -77.122  39.790  1.00 100.88 ?  91   PRO B N   1 
ATOM   1902  C  CA  . PRO B 2  91   ? -32.997 -77.168  38.605  1.00 102.56 ?  91   PRO B CA  1 
ATOM   1903  C  C   . PRO B 2  91   ? -31.554 -77.440  39.005  1.00 103.53 ?  91   PRO B C   1 
ATOM   1904  O  O   . PRO B 2  91   ? -31.083 -76.981  40.047  1.00 108.13 ?  91   PRO B O   1 
ATOM   1905  C  CB  . PRO B 2  91   ? -33.163 -75.774  37.990  1.00 93.43  ?  91   PRO B CB  1 
ATOM   1906  C  CG  . PRO B 2  91   ? -34.491 -75.302  38.489  1.00 88.42  ?  91   PRO B CG  1 
ATOM   1907  C  CD  . PRO B 2  91   ? -34.617 -75.861  39.876  1.00 91.57  ?  91   PRO B CD  1 
ATOM   1908  N  N   . GLU B 2  92   ? -30.849 -78.191  38.156  1.00 112.53 ?  92   GLU B N   1 
ATOM   1909  C  CA  . GLU B 2  92   ? -29.532 -78.700  38.530  1.00 118.64 ?  92   GLU B CA  1 
ATOM   1910  C  C   . GLU B 2  92   ? -28.510 -77.576  38.666  1.00 115.69 ?  92   GLU B C   1 
ATOM   1911  O  O   . GLU B 2  92   ? -27.776 -77.510  39.659  1.00 104.86 ?  92   GLU B O   1 
ATOM   1912  C  CB  . GLU B 2  92   ? -29.060 -79.735  37.506  1.00 119.24 ?  92   GLU B CB  1 
ATOM   1913  C  CG  . GLU B 2  92   ? -29.411 -81.177  37.856  1.00 119.28 ?  92   GLU B CG  1 
ATOM   1914  C  CD  . GLU B 2  92   ? -30.862 -81.531  37.570  1.00 135.45 ?  92   GLU B CD  1 
ATOM   1915  O  OE1 . GLU B 2  92   ? -31.668 -80.617  37.290  1.00 131.57 ?  92   GLU B OE1 1 
ATOM   1916  O  OE2 . GLU B 2  92   ? -31.198 -82.733  37.630  1.00 137.85 -1 92   GLU B OE2 1 
ATOM   1917  N  N   . GLY B 2  93   ? -28.443 -76.686  37.681  1.00 71.09  ?  93   GLY B N   1 
ATOM   1918  C  CA  . GLY B 2  93   ? -27.412 -75.672  37.631  1.00 63.32  ?  93   GLY B CA  1 
ATOM   1919  C  C   . GLY B 2  93   ? -27.830 -74.266  38.000  1.00 67.46  ?  93   GLY B C   1 
ATOM   1920  O  O   . GLY B 2  93   ? -27.072 -73.327  37.732  1.00 78.04  ?  93   GLY B O   1 
ATOM   1921  N  N   . ARG B 2  94   ? -28.998 -74.082  38.608  1.00 67.34  ?  94   ARG B N   1 
ATOM   1922  C  CA  . ARG B 2  94   ? -29.499 -72.759  38.957  1.00 65.42  ?  94   ARG B CA  1 
ATOM   1923  C  C   . ARG B 2  94   ? -29.394 -72.536  40.458  1.00 66.45  ?  94   ARG B C   1 
ATOM   1924  O  O   . ARG B 2  94   ? -29.836 -73.376  41.249  1.00 75.63  ?  94   ARG B O   1 
ATOM   1925  C  CB  . ARG B 2  94   ? -30.952 -72.578  38.511  1.00 68.33  ?  94   ARG B CB  1 
ATOM   1926  C  CG  . ARG B 2  94   ? -31.146 -72.414  37.015  1.00 59.82  ?  94   ARG B CG  1 
ATOM   1927  C  CD  . ARG B 2  94   ? -32.088 -71.258  36.715  1.00 62.61  ?  94   ARG B CD  1 
ATOM   1928  N  NE  . ARG B 2  94   ? -33.260 -71.267  37.583  1.00 57.28  ?  94   ARG B NE  1 
ATOM   1929  C  CZ  . ARG B 2  94   ? -34.427 -71.811  37.265  1.00 56.03  ?  94   ARG B CZ  1 
ATOM   1930  N  NH1 . ARG B 2  94   ? -34.618 -72.407  36.099  1.00 65.83  ?  94   ARG B NH1 1 
ATOM   1931  N  NH2 . ARG B 2  94   ? -35.428 -71.756  38.139  1.00 59.61  ?  94   ARG B NH2 1 
ATOM   1932  N  N   . VAL B 2  95   ? -28.817 -71.404  40.841  1.00 58.75  ?  95   VAL B N   1 
ATOM   1933  C  CA  . VAL B 2  95   ? -28.814 -70.938  42.224  1.00 52.48  ?  95   VAL B CA  1 
ATOM   1934  C  C   . VAL B 2  95   ? -29.961 -69.944  42.375  1.00 55.57  ?  95   VAL B C   1 
ATOM   1935  O  O   . VAL B 2  95   ? -29.970 -68.922  41.672  1.00 59.54  ?  95   VAL B O   1 
ATOM   1936  C  CB  . VAL B 2  95   ? -27.471 -70.293  42.599  1.00 57.63  ?  95   VAL B CB  1 
ATOM   1937  C  CG1 . VAL B 2  95   ? -27.439 -69.946  44.079  1.00 50.83  ?  95   VAL B CG1 1 
ATOM   1938  C  CG2 . VAL B 2  95   ? -26.317 -71.218  42.236  1.00 56.87  ?  95   VAL B CG2 1 
ATOM   1939  N  N   . PRO B 2  96   ? -30.937 -70.201  43.245  1.00 53.96  ?  96   PRO B N   1 
ATOM   1940  C  CA  . PRO B 2  96   ? -32.099 -69.306  43.346  1.00 59.99  ?  96   PRO B CA  1 
ATOM   1941  C  C   . PRO B 2  96   ? -31.689 -67.888  43.713  1.00 58.83  ?  96   PRO B C   1 
ATOM   1942  O  O   . PRO B 2  96   ? -30.901 -67.666  44.635  1.00 61.58  ?  96   PRO B O   1 
ATOM   1943  C  CB  . PRO B 2  96   ? -32.947 -69.951  44.448  1.00 49.18  ?  96   PRO B CB  1 
ATOM   1944  C  CG  . PRO B 2  96   ? -32.527 -71.382  44.461  1.00 46.90  ?  96   PRO B CG  1 
ATOM   1945  C  CD  . PRO B 2  96   ? -31.064 -71.373  44.126  1.00 45.31  ?  96   PRO B CD  1 
ATOM   1946  N  N   . GLY B 2  97   ? -32.237 -66.921  42.982  1.00 66.61  ?  97   GLY B N   1 
ATOM   1947  C  CA  . GLY B 2  97   ? -31.889 -65.531  43.175  1.00 64.16  ?  97   GLY B CA  1 
ATOM   1948  C  C   . GLY B 2  97   ? -30.682 -65.055  42.397  1.00 58.95  ?  97   GLY B C   1 
ATOM   1949  O  O   . GLY B 2  97   ? -30.288 -63.894  42.552  1.00 53.74  ?  97   GLY B O   1 
ATOM   1950  N  N   . ILE B 2  98   ? -30.081 -65.909  41.574  1.00 42.53  ?  98   ILE B N   1 
ATOM   1951  C  CA  . ILE B 2  98   ? -28.932 -65.529  40.754  1.00 33.66  ?  98   ILE B CA  1 
ATOM   1952  C  C   . ILE B 2  98   ? -29.323 -65.602  39.283  1.00 42.32  ?  98   ILE B C   1 
ATOM   1953  O  O   . ILE B 2  98   ? -29.616 -66.694  38.774  1.00 40.77  ?  98   ILE B O   1 
ATOM   1954  C  CB  . ILE B 2  98   ? -27.717 -66.427  41.035  1.00 31.39  ?  98   ILE B CB  1 
ATOM   1955  C  CG1 . ILE B 2  98   ? -27.162 -66.166  42.433  1.00 49.40  ?  98   ILE B CG1 1 
ATOM   1956  C  CG2 . ILE B 2  98   ? -26.643 -66.192  39.991  1.00 38.00  ?  98   ILE B CG2 1 
ATOM   1957  C  CD1 . ILE B 2  98   ? -25.817 -66.799  42.684  1.00 47.82  ?  98   ILE B CD1 1 
ATOM   1958  N  N   . PRO B 2  99   ? -29.352 -64.482  38.563  1.00 52.71  ?  99   PRO B N   1 
ATOM   1959  C  CA  . PRO B 2  99   ? -29.655 -64.546  37.131  1.00 51.60  ?  99   PRO B CA  1 
ATOM   1960  C  C   . PRO B 2  99   ? -28.532 -65.215  36.357  1.00 55.80  ?  99   PRO B C   1 
ATOM   1961  O  O   . PRO B 2  99   ? -27.361 -65.168  36.741  1.00 56.65  ?  99   PRO B O   1 
ATOM   1962  C  CB  . PRO B 2  99   ? -29.807 -63.073  36.729  1.00 53.65  ?  99   PRO B CB  1 
ATOM   1963  C  CG  . PRO B 2  99   ? -30.016 -62.332  38.014  1.00 58.64  ?  99   PRO B CG  1 
ATOM   1964  C  CD  . PRO B 2  99   ? -29.230 -63.094  39.036  1.00 54.44  ?  99   PRO B CD  1 
ATOM   1965  N  N   . GLN B 2  100  ? -28.907 -65.844  35.247  1.00 58.62  ?  100  GLN B N   1 
ATOM   1966  C  CA  . GLN B 2  100  ? -27.970 -66.519  34.364  1.00 55.22  ?  100  GLN B CA  1 
ATOM   1967  C  C   . GLN B 2  100  ? -28.047 -65.905  32.972  1.00 54.15  ?  100  GLN B C   1 
ATOM   1968  O  O   . GLN B 2  100  ? -28.997 -65.194  32.635  1.00 51.88  ?  100  GLN B O   1 
ATOM   1969  C  CB  . GLN B 2  100  ? -28.255 -68.025  34.294  1.00 54.29  ?  100  GLN B CB  1 
ATOM   1970  C  CG  . GLN B 2  100  ? -27.504 -68.850  35.325  1.00 48.85  ?  100  GLN B CG  1 
ATOM   1971  C  CD  . GLN B 2  100  ? -27.726 -70.338  35.148  1.00 56.85  ?  100  GLN B CD  1 
ATOM   1972  O  OE1 . GLN B 2  100  ? -28.823 -70.775  34.798  1.00 60.95  ?  100  GLN B OE1 1 
ATOM   1973  N  NE2 . GLN B 2  100  ? -26.684 -71.126  35.388  1.00 56.51  ?  100  GLN B NE2 1 
ATOM   1974  N  N   . TYR B 2  101  ? -27.030 -66.186  32.163  1.00 48.55  ?  101  TYR B N   1 
ATOM   1975  C  CA  . TYR B 2  101  ? -26.947 -65.672  30.805  1.00 44.59  ?  101  TYR B CA  1 
ATOM   1976  C  C   . TYR B 2  101  ? -26.849 -66.825  29.817  1.00 48.32  ?  101  TYR B C   1 
ATOM   1977  O  O   . TYR B 2  101  ? -26.139 -67.807  30.058  1.00 43.62  ?  101  TYR B O   1 
ATOM   1978  C  CB  . TYR B 2  101  ? -25.747 -64.735  30.636  1.00 34.38  ?  101  TYR B CB  1 
ATOM   1979  C  CG  . TYR B 2  101  ? -25.898 -63.414  31.354  1.00 47.29  ?  101  TYR B CG  1 
ATOM   1980  C  CD1 . TYR B 2  101  ? -25.727 -63.322  32.730  1.00 56.26  ?  101  TYR B CD1 1 
ATOM   1981  C  CD2 . TYR B 2  101  ? -26.217 -62.257  30.656  1.00 48.86  ?  101  TYR B CD2 1 
ATOM   1982  C  CE1 . TYR B 2  101  ? -25.867 -62.112  33.389  1.00 57.94  ?  101  TYR B CE1 1 
ATOM   1983  C  CE2 . TYR B 2  101  ? -26.358 -61.045  31.305  1.00 48.37  ?  101  TYR B CE2 1 
ATOM   1984  C  CZ  . TYR B 2  101  ? -26.182 -60.978  32.670  1.00 52.42  ?  101  TYR B CZ  1 
ATOM   1985  O  OH  . TYR B 2  101  ? -26.323 -59.772  33.317  1.00 56.58  ?  101  TYR B OH  1 
ATOM   1986  N  N   . PHE B 2  102  ? -27.568 -66.699  28.706  1.00 68.24  ?  102  PHE B N   1 
ATOM   1987  C  CA  . PHE B 2  102  ? -27.554 -67.688  27.642  1.00 63.46  ?  102  PHE B CA  1 
ATOM   1988  C  C   . PHE B 2  102  ? -27.241 -67.004  26.320  1.00 58.83  ?  102  PHE B C   1 
ATOM   1989  O  O   . PHE B 2  102  ? -27.604 -65.845  26.099  1.00 55.69  ?  102  PHE B O   1 
ATOM   1990  C  CB  . PHE B 2  102  ? -28.892 -68.433  27.548  1.00 59.50  ?  102  PHE B CB  1 
ATOM   1991  C  CG  . PHE B 2  102  ? -29.239 -69.213  28.783  1.00 65.91  ?  102  PHE B CG  1 
ATOM   1992  C  CD1 . PHE B 2  102  ? -29.918 -68.614  29.830  1.00 66.81  ?  102  PHE B CD1 1 
ATOM   1993  C  CD2 . PHE B 2  102  ? -28.883 -70.545  28.898  1.00 68.48  ?  102  PHE B CD2 1 
ATOM   1994  C  CE1 . PHE B 2  102  ? -30.237 -69.332  30.966  1.00 70.86  ?  102  PHE B CE1 1 
ATOM   1995  C  CE2 . PHE B 2  102  ? -29.199 -71.268  30.032  1.00 62.43  ?  102  PHE B CE2 1 
ATOM   1996  C  CZ  . PHE B 2  102  ? -29.876 -70.661  31.066  1.00 67.20  ?  102  PHE B CZ  1 
ATOM   1997  N  N   . ALA B 2  103  ? -26.557 -67.732  25.443  1.00 72.13  ?  103  ALA B N   1 
ATOM   1998  C  CA  . ALA B 2  103  ? -26.154 -67.218  24.141  1.00 74.98  ?  103  ALA B CA  1 
ATOM   1999  C  C   . ALA B 2  103  ? -27.163 -67.666  23.092  1.00 71.28  ?  103  ALA B C   1 
ATOM   2000  O  O   . ALA B 2  103  ? -27.298 -68.865  22.826  1.00 69.76  ?  103  ALA B O   1 
ATOM   2001  C  CB  . ALA B 2  103  ? -24.749 -67.694  23.778  1.00 81.21  ?  103  ALA B CB  1 
ATOM   2002  N  N   . SER B 2  104  ? -27.871 -66.702  22.505  1.00 53.50  ?  104  SER B N   1 
ATOM   2003  C  CA  . SER B 2  104  ? -28.831 -66.993  21.448  1.00 59.20  ?  104  SER B CA  1 
ATOM   2004  C  C   . SER B 2  104  ? -28.568 -66.107  20.238  1.00 63.29  ?  104  SER B C   1 
ATOM   2005  O  O   . SER B 2  104  ? -27.500 -65.494  20.131  1.00 56.60  ?  104  SER B O   1 
ATOM   2006  C  CB  . SER B 2  104  ? -30.265 -66.805  21.950  1.00 60.04  ?  104  SER B CB  1 
ATOM   2007  O  OG  . SER B 2  104  ? -31.202 -67.285  21.000  1.00 57.11  ?  104  SER B OG  1 
ATOM   2008  N  N   . THR B 2  105  ? -29.533 -66.031  19.325  1.00 62.30  ?  105  THR B N   1 
ATOM   2009  C  CA  . THR B 2  105  ? -29.388 -65.243  18.111  1.00 55.24  ?  105  THR B CA  1 
ATOM   2010  C  C   . THR B 2  105  ? -30.721 -64.601  17.761  1.00 59.13  ?  105  THR B C   1 
ATOM   2011  O  O   . THR B 2  105  ? -31.772 -65.242  17.852  1.00 60.57  ?  105  THR B O   1 
ATOM   2012  C  CB  . THR B 2  105  ? -28.896 -66.107  16.942  1.00 56.77  ?  105  THR B CB  1 
ATOM   2013  O  OG1 . THR B 2  105  ? -27.637 -66.696  17.286  1.00 64.71  ?  105  THR B OG1 1 
ATOM   2014  C  CG2 . THR B 2  105  ? -28.727 -65.268  15.685  1.00 56.60  ?  105  THR B CG2 1 
ATOM   2015  N  N   . LEU B 2  106  ? -30.672 -63.333  17.366  1.00 66.56  ?  106  LEU B N   1 
ATOM   2016  C  CA  . LEU B 2  106  ? -31.852 -62.585  16.958  1.00 66.63  ?  106  LEU B CA  1 
ATOM   2017  C  C   . LEU B 2  106  ? -31.668 -62.127  15.520  1.00 74.17  ?  106  LEU B C   1 
ATOM   2018  O  O   . LEU B 2  106  ? -30.625 -61.562  15.175  1.00 76.67  ?  106  LEU B O   1 
ATOM   2019  C  CB  . LEU B 2  106  ? -32.085 -61.387  17.880  1.00 61.14  ?  106  LEU B CB  1 
ATOM   2020  C  CG  . LEU B 2  106  ? -32.571 -61.748  19.284  1.00 54.90  ?  106  LEU B CG  1 
ATOM   2021  C  CD1 . LEU B 2  106  ? -32.821 -60.498  20.111  1.00 58.79  ?  106  LEU B CD1 1 
ATOM   2022  C  CD2 . LEU B 2  106  ? -33.822 -62.612  19.214  1.00 60.32  ?  106  LEU B CD2 1 
ATOM   2023  N  N   . THR B 2  107  ? -32.673 -62.373  14.687  1.00 94.06  ?  107  THR B N   1 
ATOM   2024  C  CA  . THR B 2  107  ? -32.610 -62.038  13.272  1.00 92.57  ?  107  THR B CA  1 
ATOM   2025  C  C   . THR B 2  107  ? -33.443 -60.797  12.985  1.00 86.33  ?  107  THR B C   1 
ATOM   2026  O  O   . THR B 2  107  ? -34.537 -60.628  13.532  1.00 94.92  ?  107  THR B O   1 
ATOM   2027  C  CB  . THR B 2  107  ? -33.104 -63.202  12.413  1.00 98.67  ?  107  THR B CB  1 
ATOM   2028  O  OG1 . THR B 2  107  ? -34.520 -63.350  12.576  1.00 110.80 ?  107  THR B OG1 1 
ATOM   2029  C  CG2 . THR B 2  107  ? -32.413 -64.491  12.827  1.00 96.93  ?  107  THR B CG2 1 
ATOM   2030  N  N   . LEU B 2  108  ? -32.915 -59.929  12.124  1.00 71.74  ?  108  LEU B N   1 
ATOM   2031  C  CA  . LEU B 2  108  ? -33.626 -58.722  11.724  1.00 77.66  ?  108  LEU B CA  1 
ATOM   2032  C  C   . LEU B 2  108  ? -34.308 -58.926  10.377  1.00 80.20  ?  108  LEU B C   1 
ATOM   2033  O  O   . LEU B 2  108  ? -35.536 -59.042  10.305  1.00 81.15  ?  108  LEU B O   1 
ATOM   2034  C  CB  . LEU B 2  108  ? -32.669 -57.530  11.667  1.00 77.81  ?  108  LEU B CB  1 
ATOM   2035  C  CG  . LEU B 2  108  ? -33.290 -56.185  11.287  1.00 76.10  ?  108  LEU B CG  1 
ATOM   2036  C  CD1 . LEU B 2  108  ? -34.456 -55.857  12.205  1.00 70.79  ?  108  LEU B CD1 1 
ATOM   2037  C  CD2 . LEU B 2  108  ? -32.245 -55.081  11.327  1.00 74.82  ?  108  LEU B CD2 1 
ATOM   2038  N  N   . GLY B 2  109  ? -33.521 -58.967  9.306   1.00 43.88  ?  109  GLY B N   1 
ATOM   2039  C  CA  . GLY B 2  109  ? -34.060 -59.216  7.984   1.00 51.76  ?  109  GLY B CA  1 
ATOM   2040  C  C   . GLY B 2  109  ? -33.609 -60.554  7.440   1.00 54.91  ?  109  GLY B C   1 
ATOM   2041  O  O   . GLY B 2  109  ? -33.259 -60.671  6.262   1.00 43.38  ?  109  GLY B O   1 
ATOM   2042  N  N   . GLY B 2  110  ? -33.612 -61.573  8.297   1.00 73.47  ?  110  GLY B N   1 
ATOM   2043  C  CA  . GLY B 2  110  ? -33.121 -62.885  7.957   1.00 66.08  ?  110  GLY B CA  1 
ATOM   2044  C  C   . GLY B 2  110  ? -31.685 -63.140  8.363   1.00 66.94  ?  110  GLY B C   1 
ATOM   2045  O  O   . GLY B 2  110  ? -31.269 -64.303  8.424   1.00 77.18  ?  110  GLY B O   1 
ATOM   2046  N  N   . TYR B 2  111  ? -30.920 -62.088  8.640   1.00 65.73  ?  111  TYR B N   1 
ATOM   2047  C  CA  . TYR B 2  111  ? -29.535 -62.223  9.064   1.00 70.88  ?  111  TYR B CA  1 
ATOM   2048  C  C   . TYR B 2  111  ? -29.456 -62.206  10.583  1.00 74.06  ?  111  TYR B C   1 
ATOM   2049  O  O   . TYR B 2  111  ? -30.111 -61.393  11.243  1.00 73.59  ?  111  TYR B O   1 
ATOM   2050  C  CB  . TYR B 2  111  ? -28.679 -61.104  8.473   1.00 75.69  ?  111  TYR B CB  1 
ATOM   2051  C  CG  . TYR B 2  111  ? -28.675 -61.089  6.963   1.00 70.63  ?  111  TYR B CG  1 
ATOM   2052  C  CD1 . TYR B 2  111  ? -27.824 -61.917  6.245   1.00 74.16  ?  111  TYR B CD1 1 
ATOM   2053  C  CD2 . TYR B 2  111  ? -29.528 -60.253  6.256   1.00 64.07  ?  111  TYR B CD2 1 
ATOM   2054  C  CE1 . TYR B 2  111  ? -27.818 -61.911  4.864   1.00 79.88  ?  111  TYR B CE1 1 
ATOM   2055  C  CE2 . TYR B 2  111  ? -29.530 -60.239  4.875   1.00 80.68  ?  111  TYR B CE2 1 
ATOM   2056  C  CZ  . TYR B 2  111  ? -28.673 -61.070  4.183   1.00 89.38  ?  111  TYR B CZ  1 
ATOM   2057  O  OH  . TYR B 2  111  ? -28.672 -61.059  2.807   1.00 95.09  ?  111  TYR B OH  1 
ATOM   2058  N  N   . GLY B 2  112  ? -28.646 -63.111  11.134  1.00 70.74  ?  112  GLY B N   1 
ATOM   2059  C  CA  . GLY B 2  112  ? -28.606 -63.288  12.568  1.00 73.74  ?  112  GLY B CA  1 
ATOM   2060  C  C   . GLY B 2  112  ? -27.693 -62.303  13.275  1.00 70.67  ?  112  GLY B C   1 
ATOM   2061  O  O   . GLY B 2  112  ? -26.833 -61.653  12.681  1.00 72.04  ?  112  GLY B O   1 
ATOM   2062  N  N   . THR B 2  113  ? -27.900 -62.199  14.586  1.00 69.65  ?  113  THR B N   1 
ATOM   2063  C  CA  . THR B 2  113  ? -27.081 -61.352  15.446  1.00 67.01  ?  113  THR B CA  1 
ATOM   2064  C  C   . THR B 2  113  ? -26.973 -62.030  16.802  1.00 61.29  ?  113  THR B C   1 
ATOM   2065  O  O   . THR B 2  113  ? -27.991 -62.259  17.462  1.00 58.94  ?  113  THR B O   1 
ATOM   2066  C  CB  . THR B 2  113  ? -27.682 -59.950  15.586  1.00 64.92  ?  113  THR B CB  1 
ATOM   2067  O  OG1 . THR B 2  113  ? -27.911 -59.392  14.286  1.00 67.08  ?  113  THR B OG1 1 
ATOM   2068  C  CG2 . THR B 2  113  ? -26.744 -59.042  16.361  1.00 56.78  ?  113  THR B CG2 1 
ATOM   2069  N  N   . GLY B 2  114  ? -25.749 -62.357  17.209  1.00 60.58  ?  114  GLY B N   1 
ATOM   2070  C  CA  . GLY B 2  114  ? -25.553 -63.060  18.467  1.00 62.79  ?  114  GLY B CA  1 
ATOM   2071  C  C   . GLY B 2  114  ? -25.855 -62.160  19.651  1.00 59.12  ?  114  GLY B C   1 
ATOM   2072  O  O   . GLY B 2  114  ? -25.331 -61.044  19.753  1.00 58.78  ?  114  GLY B O   1 
ATOM   2073  N  N   . VAL B 2  115  ? -26.698 -62.644  20.559  1.00 55.28  ?  115  VAL B N   1 
ATOM   2074  C  CA  . VAL B 2  115  ? -27.124 -61.872  21.718  1.00 54.48  ?  115  VAL B CA  1 
ATOM   2075  C  C   . VAL B 2  115  ? -26.885 -62.686  22.981  1.00 64.51  ?  115  VAL B C   1 
ATOM   2076  O  O   . VAL B 2  115  ? -27.010 -63.915  22.988  1.00 73.26  ?  115  VAL B O   1 
ATOM   2077  C  CB  . VAL B 2  115  ? -28.608 -61.457  21.620  1.00 53.20  ?  115  VAL B CB  1 
ATOM   2078  C  CG1 . VAL B 2  115  ? -28.783 -60.356  20.591  1.00 55.20  ?  115  VAL B CG1 1 
ATOM   2079  C  CG2 . VAL B 2  115  ? -29.476 -62.659  21.277  1.00 63.81  ?  115  VAL B CG2 1 
ATOM   2080  N  N   . LEU B 2  116  ? -26.533 -61.987  24.055  1.00 75.10  ?  116  LEU B N   1 
ATOM   2081  C  CA  . LEU B 2  116  ? -26.402 -62.585  25.377  1.00 71.18  ?  116  LEU B CA  1 
ATOM   2082  C  C   . LEU B 2  116  ? -27.616 -62.155  26.194  1.00 74.03  ?  116  LEU B C   1 
ATOM   2083  O  O   . LEU B 2  116  ? -27.714 -60.996  26.608  1.00 81.09  ?  116  LEU B O   1 
ATOM   2084  C  CB  . LEU B 2  116  ? -25.098 -62.160  26.046  1.00 73.61  ?  116  LEU B CB  1 
ATOM   2085  C  CG  . LEU B 2  116  ? -24.754 -62.876  27.353  1.00 75.99  ?  116  LEU B CG  1 
ATOM   2086  C  CD1 . LEU B 2  116  ? -24.554 -64.362  27.104  1.00 84.78  ?  116  LEU B CD1 1 
ATOM   2087  C  CD2 . LEU B 2  116  ? -23.519 -62.263  27.996  1.00 79.84  ?  116  LEU B CD2 1 
ATOM   2088  N  N   . VAL B 2  117  ? -28.540 -63.086  26.413  1.00 50.57  ?  117  VAL B N   1 
ATOM   2089  C  CA  . VAL B 2  117  ? -29.830 -62.800  27.028  1.00 51.80  ?  117  VAL B CA  1 
ATOM   2090  C  C   . VAL B 2  117  ? -29.838 -63.341  28.453  1.00 56.33  ?  117  VAL B C   1 
ATOM   2091  O  O   . VAL B 2  117  ? -29.317 -64.430  28.723  1.00 56.06  ?  117  VAL B O   1 
ATOM   2092  C  CB  . VAL B 2  117  ? -30.977 -63.387  26.181  1.00 47.05  ?  117  VAL B CB  1 
ATOM   2093  C  CG1 . VAL B 2  117  ? -30.740 -64.857  25.918  1.00 53.92  ?  117  VAL B CG1 1 
ATOM   2094  C  CG2 . VAL B 2  117  ? -32.325 -63.161  26.850  1.00 48.36  ?  117  VAL B CG2 1 
ATOM   2095  N  N   . ARG B 2  118  ? -30.423 -62.567  29.366  1.00 77.70  ?  118  ARG B N   1 
ATOM   2096  C  CA  . ARG B 2  118  ? -30.402 -62.857  30.794  1.00 75.30  ?  118  ARG B CA  1 
ATOM   2097  C  C   . ARG B 2  118  ? -31.707 -63.517  31.221  1.00 76.46  ?  118  ARG B C   1 
ATOM   2098  O  O   . ARG B 2  118  ? -32.791 -62.981  30.968  1.00 77.17  ?  118  ARG B O   1 
ATOM   2099  C  CB  . ARG B 2  118  ? -30.173 -61.574  31.594  1.00 72.93  ?  118  ARG B CB  1 
ATOM   2100  C  CG  . ARG B 2  118  ? -30.236 -61.749  33.100  1.00 73.60  ?  118  ARG B CG  1 
ATOM   2101  C  CD  . ARG B 2  118  ? -30.152 -60.404  33.805  1.00 77.74  ?  118  ARG B CD  1 
ATOM   2102  N  NE  . ARG B 2  118  ? -31.362 -59.610  33.628  1.00 73.02  ?  118  ARG B NE  1 
ATOM   2103  C  CZ  . ARG B 2  118  ? -31.422 -58.292  33.765  1.00 75.08  ?  118  ARG B CZ  1 
ATOM   2104  N  NH1 . ARG B 2  118  ? -30.350 -57.580  34.075  1.00 74.77  ?  118  ARG B NH1 1 
ATOM   2105  N  NH2 . ARG B 2  118  ? -32.585 -57.672  33.587  1.00 71.39  ?  118  ARG B NH2 1 
ATOM   2106  N  N   . SER B 2  119  ? -31.598 -64.674  31.869  1.00 69.22  ?  119  SER B N   1 
ATOM   2107  C  CA  . SER B 2  119  ? -32.740 -65.375  32.446  1.00 75.61  ?  119  SER B CA  1 
ATOM   2108  C  C   . SER B 2  119  ? -32.666 -65.251  33.962  1.00 76.94  ?  119  SER B C   1 
ATOM   2109  O  O   . SER B 2  119  ? -31.697 -65.708  34.578  1.00 70.28  ?  119  SER B O   1 
ATOM   2110  C  CB  . SER B 2  119  ? -32.761 -66.846  32.028  1.00 76.55  ?  119  SER B CB  1 
ATOM   2111  O  OG  . SER B 2  119  ? -31.990 -67.638  32.914  1.00 77.38  ?  119  SER B OG  1 
ATOM   2112  N  N   . ASN B 2  120  ? -33.687 -64.634  34.558  1.00 88.72  ?  120  ASN B N   1 
ATOM   2113  C  CA  . ASN B 2  120  ? -33.691 -64.422  36.002  1.00 89.60  ?  120  ASN B CA  1 
ATOM   2114  C  C   . ASN B 2  120  ? -34.002 -65.716  36.747  1.00 97.32  ?  120  ASN B C   1 
ATOM   2115  O  O   . ASN B 2  120  ? -33.180 -66.211  37.526  1.00 99.59  ?  120  ASN B O   1 
ATOM   2116  C  CB  . ASN B 2  120  ? -34.696 -63.327  36.367  1.00 81.24  ?  120  ASN B CB  1 
ATOM   2117  C  CG  . ASN B 2  120  ? -34.089 -61.937  36.313  1.00 87.70  ?  120  ASN B CG  1 
ATOM   2118  O  OD1 . ASN B 2  120  ? -34.304 -61.190  35.358  1.00 83.92  ?  120  ASN B OD1 1 
ATOM   2119  N  ND2 . ASN B 2  120  ? -33.323 -61.585  37.339  1.00 91.19  ?  120  ASN B ND2 1 
ATOM   2120  N  N   . GLU B 2  121  ? -35.187 -66.274  36.521  1.00 83.10  ?  121  GLU B N   1 
ATOM   2121  C  CA  . GLU B 2  121  ? -35.593 -67.553  37.094  1.00 82.91  ?  121  GLU B CA  1 
ATOM   2122  C  C   . GLU B 2  121  ? -36.213 -68.429  36.015  1.00 93.43  ?  121  GLU B C   1 
ATOM   2123  O  O   . GLU B 2  121  ? -37.268 -69.040  36.194  1.00 94.94  ?  121  GLU B O   1 
ATOM   2124  C  CB  . GLU B 2  121  ? -36.563 -67.353  38.256  1.00 86.49  ?  121  GLU B CB  1 
ATOM   2125  C  CG  . GLU B 2  121  ? -35.898 -66.932  39.559  1.00 86.51  ?  121  GLU B CG  1 
ATOM   2126  C  CD  . GLU B 2  121  ? -35.148 -68.065  40.234  1.00 91.76  ?  121  GLU B CD  1 
ATOM   2127  O  OE1 . GLU B 2  121  ? -35.730 -69.161  40.386  1.00 91.32  ?  121  GLU B OE1 1 
ATOM   2128  O  OE2 . GLU B 2  121  ? -33.977 -67.857  40.618  1.00 88.03  -1 121  GLU B OE2 1 
ATOM   2129  N  N   . GLY B 2  122  ? -35.547 -68.495  34.865  1.00 97.73  ?  122  GLY B N   1 
ATOM   2130  C  CA  . GLY B 2  122  ? -36.079 -69.186  33.711  1.00 91.08  ?  122  GLY B CA  1 
ATOM   2131  C  C   . GLY B 2  122  ? -36.889 -68.324  32.772  1.00 93.95  ?  122  GLY B C   1 
ATOM   2132  O  O   . GLY B 2  122  ? -37.592 -68.867  31.911  1.00 89.16  ?  122  GLY B O   1 
ATOM   2133  N  N   . ARG B 2  123  ? -36.818 -67.000  32.908  1.00 106.16 ?  123  ARG B N   1 
ATOM   2134  C  CA  . ARG B 2  123  ? -37.581 -66.080  32.080  1.00 102.77 ?  123  ARG B CA  1 
ATOM   2135  C  C   . ARG B 2  123  ? -36.631 -65.059  31.467  1.00 95.82  ?  123  ARG B C   1 
ATOM   2136  O  O   . ARG B 2  123  ? -35.801 -64.478  32.186  1.00 94.82  ?  123  ARG B O   1 
ATOM   2137  C  CB  . ARG B 2  123  ? -38.662 -65.362  32.897  1.00 98.19  ?  123  ARG B CB  1 
ATOM   2138  C  CG  . ARG B 2  123  ? -39.513 -66.266  33.764  1.00 108.72 ?  123  ARG B CG  1 
ATOM   2139  C  CD  . ARG B 2  123  ? -40.589 -65.463  34.472  1.00 111.38 ?  123  ARG B CD  1 
ATOM   2140  N  NE  . ARG B 2  123  ? -40.053 -64.696  35.591  1.00 114.06 ?  123  ARG B NE  1 
ATOM   2141  C  CZ  . ARG B 2  123  ? -39.847 -63.386  35.570  1.00 104.33 ?  123  ARG B CZ  1 
ATOM   2142  N  NH1 . ARG B 2  123  ? -40.108 -62.662  34.494  1.00 88.31  ?  123  ARG B NH1 1 
ATOM   2143  N  NH2 . ARG B 2  123  ? -39.367 -62.787  36.657  1.00 101.86 ?  123  ARG B NH2 1 
ATOM   2144  N  N   . PRO B 2  124  ? -36.715 -64.807  30.162  1.00 50.94  ?  124  PRO B N   1 
ATOM   2145  C  CA  . PRO B 2  124  ? -35.885 -63.754  29.566  1.00 54.53  ?  124  PRO B CA  1 
ATOM   2146  C  C   . PRO B 2  124  ? -36.336 -62.378  30.031  1.00 51.69  ?  124  PRO B C   1 
ATOM   2147  O  O   . PRO B 2  124  ? -37.532 -62.082  30.086  1.00 44.13  ?  124  PRO B O   1 
ATOM   2148  C  CB  . PRO B 2  124  ? -36.101 -63.935  28.057  1.00 59.31  ?  124  PRO B CB  1 
ATOM   2149  C  CG  . PRO B 2  124  ? -36.756 -65.282  27.902  1.00 59.42  ?  124  PRO B CG  1 
ATOM   2150  C  CD  . PRO B 2  124  ? -37.531 -65.505  29.157  1.00 49.55  ?  124  PRO B CD  1 
ATOM   2151  N  N   . THR B 2  125  ? -35.366 -61.538  30.366  1.00 67.66  ?  125  THR B N   1 
ATOM   2152  C  CA  . THR B 2  125  ? -35.651 -60.193  30.859  1.00 67.53  ?  125  THR B CA  1 
ATOM   2153  C  C   . THR B 2  125  ? -34.824 -59.119  30.171  1.00 64.19  ?  125  THR B C   1 
ATOM   2154  O  O   . THR B 2  125  ? -35.345 -58.035  29.892  1.00 63.48  ?  125  THR B O   1 
ATOM   2155  C  CB  . THR B 2  125  ? -35.418 -60.130  32.380  1.00 65.50  ?  125  THR B CB  1 
ATOM   2156  O  OG1 . THR B 2  125  ? -36.221 -61.123  33.028  1.00 71.28  ?  125  THR B OG1 1 
ATOM   2157  C  CG2 . THR B 2  125  ? -35.787 -58.758  32.924  1.00 62.40  ?  125  THR B CG2 1 
ATOM   2158  N  N   . LYS B 2  126  ? -33.554 -59.391  29.883  1.00 73.38  ?  126  LYS B N   1 
ATOM   2159  C  CA  . LYS B 2  126  ? -32.669 -58.408  29.277  1.00 75.65  ?  126  LYS B CA  1 
ATOM   2160  C  C   . LYS B 2  126  ? -31.877 -59.062  28.155  1.00 77.41  ?  126  LYS B C   1 
ATOM   2161  O  O   . LYS B 2  126  ? -31.524 -60.242  28.227  1.00 73.21  ?  126  LYS B O   1 
ATOM   2162  C  CB  . LYS B 2  126  ? -31.714 -57.803  30.316  1.00 74.46  ?  126  LYS B CB  1 
ATOM   2163  C  CG  . LYS B 2  126  ? -30.917 -56.609  29.820  1.00 67.79  ?  126  LYS B CG  1 
ATOM   2164  C  CD  . LYS B 2  126  ? -31.799 -55.387  29.640  1.00 71.84  ?  126  LYS B CD  1 
ATOM   2165  C  CE  . LYS B 2  126  ? -30.963 -54.157  29.329  1.00 81.32  ?  126  LYS B CE  1 
ATOM   2166  N  NZ  . LYS B 2  126  ? -30.046 -54.388  28.178  1.00 85.41  ?  126  LYS B NZ  1 
ATOM   2167  N  N   . VAL B 2  127  ? -31.606 -58.280  27.114  1.00 67.78  ?  127  VAL B N   1 
ATOM   2168  C  CA  . VAL B 2  127  ? -30.811 -58.716  25.973  1.00 67.38  ?  127  VAL B CA  1 
ATOM   2169  C  C   . VAL B 2  127  ? -29.621 -57.776  25.845  1.00 63.66  ?  127  VAL B C   1 
ATOM   2170  O  O   . VAL B 2  127  ? -29.786 -56.551  25.895  1.00 60.72  ?  127  VAL B O   1 
ATOM   2171  C  CB  . VAL B 2  127  ? -31.642 -58.736  24.676  1.00 62.83  ?  127  VAL B CB  1 
ATOM   2172  C  CG1 . VAL B 2  127  ? -30.739 -58.895  23.462  1.00 60.49  ?  127  VAL B CG1 1 
ATOM   2173  C  CG2 . VAL B 2  127  ? -32.679 -59.846  24.726  1.00 57.05  ?  127  VAL B CG2 1 
ATOM   2174  N  N   . GLU B 2  128  ? -28.426 -58.348  25.700  1.00 63.75  ?  128  GLU B N   1 
ATOM   2175  C  CA  . GLU B 2  128  ? -27.206 -57.573  25.521  1.00 68.69  ?  128  GLU B CA  1 
ATOM   2176  C  C   . GLU B 2  128  ? -26.370 -58.219  24.423  1.00 69.22  ?  128  GLU B C   1 
ATOM   2177  O  O   . GLU B 2  128  ? -26.728 -59.264  23.871  1.00 66.01  ?  128  GLU B O   1 
ATOM   2178  C  CB  . GLU B 2  128  ? -26.419 -57.461  26.832  1.00 79.19  ?  128  GLU B CB  1 
ATOM   2179  C  CG  . GLU B 2  128  ? -27.094 -56.599  27.890  1.00 82.20  ?  128  GLU B CG  1 
ATOM   2180  C  CD  . GLU B 2  128  ? -27.057 -57.227  29.269  1.00 88.65  ?  128  GLU B CD  1 
ATOM   2181  O  OE1 . GLU B 2  128  ? -26.513 -58.344  29.402  1.00 98.51  ?  128  GLU B OE1 1 
ATOM   2182  O  OE2 . GLU B 2  128  ? -27.572 -56.603  30.221  1.00 80.75  -1 128  GLU B OE2 1 
ATOM   2183  N  N   . GLY B 2  129  ? -25.242 -57.581  24.105  1.00 76.67  ?  129  GLY B N   1 
ATOM   2184  C  CA  . GLY B 2  129  ? -24.406 -58.050  23.024  1.00 75.56  ?  129  GLY B CA  1 
ATOM   2185  C  C   . GLY B 2  129  ? -23.575 -59.262  23.396  1.00 78.74  ?  129  GLY B C   1 
ATOM   2186  O  O   . GLY B 2  129  ? -23.253 -59.509  24.558  1.00 81.08  ?  129  GLY B O   1 
ATOM   2187  N  N   . ASN B 2  130  ? -23.221 -60.034  22.365  1.00 69.77  ?  130  ASN B N   1 
ATOM   2188  C  CA  . ASN B 2  130  ? -22.381 -61.212  22.519  1.00 63.48  ?  130  ASN B CA  1 
ATOM   2189  C  C   . ASN B 2  130  ? -20.974 -60.869  22.049  1.00 64.10  ?  130  ASN B C   1 
ATOM   2190  O  O   . ASN B 2  130  ? -20.719 -60.856  20.835  1.00 69.14  ?  130  ASN B O   1 
ATOM   2191  C  CB  . ASN B 2  130  ? -22.948 -62.385  21.719  1.00 61.79  ?  130  ASN B CB  1 
ATOM   2192  C  CG  . ASN B 2  130  ? -22.288 -63.703  22.068  1.00 65.13  ?  130  ASN B CG  1 
ATOM   2193  O  OD1 . ASN B 2  130  ? -21.062 -63.807  22.120  1.00 61.39  ?  130  ASN B OD1 1 
ATOM   2194  N  ND2 . ASN B 2  130  ? -23.102 -64.723  22.309  1.00 78.45  ?  130  ASN B ND2 1 
ATOM   2195  N  N   . PRO B 2  131  ? -20.029 -60.601  22.953  1.00 50.04  ?  131  PRO B N   1 
ATOM   2196  C  CA  . PRO B 2  131  ? -18.690 -60.167  22.516  1.00 51.91  ?  131  PRO B CA  1 
ATOM   2197  C  C   . PRO B 2  131  ? -17.978 -61.168  21.623  1.00 48.14  ?  131  PRO B C   1 
ATOM   2198  O  O   . PRO B 2  131  ? -17.048 -60.781  20.905  1.00 40.59  ?  131  PRO B O   1 
ATOM   2199  C  CB  . PRO B 2  131  ? -17.938 -59.965  23.839  1.00 52.30  ?  131  PRO B CB  1 
ATOM   2200  C  CG  . PRO B 2  131  ? -19.015 -59.754  24.859  1.00 54.79  ?  131  PRO B CG  1 
ATOM   2201  C  CD  . PRO B 2  131  ? -20.148 -60.630  24.420  1.00 53.04  ?  131  PRO B CD  1 
ATOM   2202  N  N   . ARG B 2  132  ? -18.386 -62.436  21.637  1.00 70.76  ?  132  ARG B N   1 
ATOM   2203  C  CA  . ARG B 2  132  ? -17.739 -63.467  20.839  1.00 65.95  ?  132  ARG B CA  1 
ATOM   2204  C  C   . ARG B 2  132  ? -18.309 -63.574  19.434  1.00 62.83  ?  132  ARG B C   1 
ATOM   2205  O  O   . ARG B 2  132  ? -17.760 -64.321  18.618  1.00 62.25  ?  132  ARG B O   1 
ATOM   2206  C  CB  . ARG B 2  132  ? -17.859 -64.826  21.537  1.00 62.64  ?  132  ARG B CB  1 
ATOM   2207  C  CG  . ARG B 2  132  ? -17.537 -64.786  23.019  1.00 65.39  ?  132  ARG B CG  1 
ATOM   2208  C  CD  . ARG B 2  132  ? -17.623 -66.169  23.633  1.00 82.59  ?  132  ARG B CD  1 
ATOM   2209  N  NE  . ARG B 2  132  ? -16.646 -67.078  23.048  1.00 84.16  ?  132  ARG B NE  1 
ATOM   2210  C  CZ  . ARG B 2  132  ? -15.497 -67.406  23.620  1.00 88.81  ?  132  ARG B CZ  1 
ATOM   2211  N  NH1 . ARG B 2  132  ? -15.155 -66.931  24.806  1.00 90.34  ?  132  ARG B NH1 1 
ATOM   2212  N  NH2 . ARG B 2  132  ? -14.667 -68.227  22.982  1.00 88.15  ?  132  ARG B NH2 1 
ATOM   2213  N  N   . HIS B 2  133  ? -19.382 -62.844  19.133  1.00 58.90  ?  133  HIS B N   1 
ATOM   2214  C  CA  . HIS B 2  133  ? -20.071 -62.969  17.854  1.00 64.55  ?  133  HIS B CA  1 
ATOM   2215  C  C   . HIS B 2  133  ? -19.760 -61.779  16.967  1.00 67.99  ?  133  HIS B C   1 
ATOM   2216  O  O   . HIS B 2  133  ? -19.929 -60.630  17.403  1.00 68.25  ?  133  HIS B O   1 
ATOM   2217  C  CB  . HIS B 2  133  ? -21.580 -63.072  18.060  1.00 65.23  ?  133  HIS B CB  1 
ATOM   2218  C  CG  . HIS B 2  133  ? -22.337 -63.486  16.833  1.00 68.46  ?  133  HIS B CG  1 
ATOM   2219  N  ND1 . HIS B 2  133  ? -23.000 -62.582  16.031  1.00 69.90  ?  133  HIS B ND1 1 
ATOM   2220  C  CD2 . HIS B 2  133  ? -22.556 -64.704  16.284  1.00 68.07  ?  133  HIS B CD2 1 
ATOM   2221  C  CE1 . HIS B 2  133  ? -23.581 -63.223  15.032  1.00 75.65  ?  133  HIS B CE1 1 
ATOM   2222  N  NE2 . HIS B 2  133  ? -23.328 -64.513  15.163  1.00 69.10  ?  133  HIS B NE2 1 
ATOM   2223  N  N   . PRO B 2  134  ? -19.309 -61.996  15.732  1.00 70.27  ?  134  PRO B N   1 
ATOM   2224  C  CA  . PRO B 2  134  ? -19.206 -60.881  14.787  1.00 67.85  ?  134  PRO B CA  1 
ATOM   2225  C  C   . PRO B 2  134  ? -20.584 -60.305  14.510  1.00 72.31  ?  134  PRO B C   1 
ATOM   2226  O  O   . PRO B 2  134  ? -21.600 -60.999  14.608  1.00 74.68  ?  134  PRO B O   1 
ATOM   2227  C  CB  . PRO B 2  134  ? -18.594 -61.528  13.536  1.00 60.54  ?  134  PRO B CB  1 
ATOM   2228  C  CG  . PRO B 2  134  ? -17.945 -62.773  14.037  1.00 79.04  ?  134  PRO B CG  1 
ATOM   2229  C  CD  . PRO B 2  134  ? -18.818 -63.255  15.149  1.00 68.38  ?  134  PRO B CD  1 
ATOM   2230  N  N   . ALA B 2  135  ? -20.604 -59.012  14.186  1.00 81.14  ?  135  ALA B N   1 
ATOM   2231  C  CA  . ALA B 2  135  ? -21.806 -58.211  13.966  1.00 88.36  ?  135  ALA B CA  1 
ATOM   2232  C  C   . ALA B 2  135  ? -22.541 -57.905  15.262  1.00 84.35  ?  135  ALA B C   1 
ATOM   2233  O  O   . ALA B 2  135  ? -23.662 -57.397  15.216  1.00 87.43  ?  135  ALA B O   1 
ATOM   2234  C  CB  . ALA B 2  135  ? -22.782 -58.853  12.965  1.00 90.68  ?  135  ALA B CB  1 
ATOM   2235  N  N   . SER B 2  136  ? -21.943 -58.202  16.419  1.00 107.04 ?  136  SER B N   1 
ATOM   2236  C  CA  . SER B 2  136  ? -22.523 -57.845  17.711  1.00 105.55 ?  136  SER B CA  1 
ATOM   2237  C  C   . SER B 2  136  ? -21.432 -57.855  18.776  1.00 96.24  ?  136  SER B C   1 
ATOM   2238  O  O   . SER B 2  136  ? -21.596 -58.458  19.838  1.00 101.28 ?  136  SER B O   1 
ATOM   2239  C  CB  . SER B 2  136  ? -23.667 -58.796  18.104  1.00 112.13 ?  136  SER B CB  1 
ATOM   2240  O  OG  . SER B 2  136  ? -24.202 -58.445  19.375  1.00 117.53 ?  136  SER B OG  1 
ATOM   2241  N  N   . LEU B 2  137  ? -20.315 -57.190  18.507  1.00 63.70  ?  137  LEU B N   1 
ATOM   2242  C  CA  . LEU B 2  137  ? -19.189 -57.195  19.432  1.00 59.70  ?  137  LEU B CA  1 
ATOM   2243  C  C   . LEU B 2  137  ? -19.519 -56.455  20.725  1.00 66.11  ?  137  LEU B C   1 
ATOM   2244  O  O   . LEU B 2  137  ? -18.983 -55.372  20.976  1.00 78.04  ?  137  LEU B O   1 
ATOM   2245  C  CB  . LEU B 2  137  ? -17.977 -56.551  18.756  1.00 67.07  ?  137  LEU B CB  1 
ATOM   2246  C  CG  . LEU B 2  137  ? -17.710 -57.098  17.358  1.00 67.14  ?  137  LEU B CG  1 
ATOM   2247  C  CD1 . LEU B 2  137  ? -16.921 -56.091  16.504  1.00 62.89  ?  137  LEU B CD1 1 
ATOM   2248  C  CD2 . LEU B 2  137  ? -17.013 -58.428  17.429  1.00 57.43  ?  137  LEU B CD2 1 
ATOM   2249  N  N   . GLY B 2  138  ? -20.403 -57.015  21.543  1.00 69.82  ?  138  GLY B N   1 
ATOM   2250  C  CA  . GLY B 2  138  ? -20.825 -56.321  22.740  1.00 68.18  ?  138  GLY B CA  1 
ATOM   2251  C  C   . GLY B 2  138  ? -21.852 -55.238  22.513  1.00 72.66  ?  138  GLY B C   1 
ATOM   2252  O  O   . GLY B 2  138  ? -22.005 -54.359  23.365  1.00 79.33  ?  138  GLY B O   1 
ATOM   2253  N  N   . GLY B 2  139  ? -22.566 -55.271  21.388  1.00 92.59  ?  139  GLY B N   1 
ATOM   2254  C  CA  . GLY B 2  139  ? -23.528 -54.235  21.075  1.00 92.57  ?  139  GLY B CA  1 
ATOM   2255  C  C   . GLY B 2  139  ? -24.756 -54.824  20.413  1.00 87.59  ?  139  GLY B C   1 
ATOM   2256  O  O   . GLY B 2  139  ? -24.709 -55.897  19.809  1.00 89.31  ?  139  GLY B O   1 
ATOM   2257  N  N   . THR B 2  140  ? -25.871 -54.104  20.552  1.00 58.84  ?  140  THR B N   1 
ATOM   2258  C  CA  . THR B 2  140  ? -27.150 -54.522  19.993  1.00 62.89  ?  140  THR B CA  1 
ATOM   2259  C  C   . THR B 2  140  ? -27.837 -53.332  19.339  1.00 63.28  ?  140  THR B C   1 
ATOM   2260  O  O   . THR B 2  140  ? -27.475 -52.176  19.568  1.00 60.44  ?  140  THR B O   1 
ATOM   2261  C  CB  . THR B 2  140  ? -28.087 -55.117  21.055  1.00 57.67  ?  140  THR B CB  1 
ATOM   2262  O  OG1 . THR B 2  140  ? -28.733 -54.054  21.765  1.00 57.70  ?  140  THR B OG1 1 
ATOM   2263  C  CG2 . THR B 2  140  ? -27.331 -55.990  22.032  1.00 62.42  ?  140  THR B CG2 1 
ATOM   2264  N  N   . ASP B 2  141  ? -28.830 -53.631  18.508  1.00 78.70  ?  141  ASP B N   1 
ATOM   2265  C  CA  . ASP B 2  141  ? -29.701 -52.619  17.933  1.00 70.54  ?  141  ASP B CA  1 
ATOM   2266  C  C   . ASP B 2  141  ? -30.996 -52.545  18.730  1.00 73.36  ?  141  ASP B C   1 
ATOM   2267  O  O   . ASP B 2  141  ? -31.272 -53.379  19.595  1.00 78.76  ?  141  ASP B O   1 
ATOM   2268  C  CB  . ASP B 2  141  ? -29.993 -52.917  16.460  1.00 78.58  ?  141  ASP B CB  1 
ATOM   2269  C  CG  . ASP B 2  141  ? -30.633 -54.277  16.252  1.00 87.67  ?  141  ASP B CG  1 
ATOM   2270  O  OD1 . ASP B 2  141  ? -30.289 -55.225  16.993  1.00 103.89 ?  141  ASP B OD1 1 
ATOM   2271  O  OD2 . ASP B 2  141  ? -31.487 -54.394  15.349  1.00 81.65  -1 141  ASP B OD2 1 
ATOM   2272  N  N   . LEU B 2  142  ? -31.801 -51.526  18.418  1.00 57.74  ?  142  LEU B N   1 
ATOM   2273  C  CA  . LEU B 2  142  ? -33.022 -51.285  19.180  1.00 59.98  ?  142  LEU B CA  1 
ATOM   2274  C  C   . LEU B 2  142  ? -34.002 -52.446  19.073  1.00 62.06  ?  142  LEU B C   1 
ATOM   2275  O  O   . LEU B 2  142  ? -34.791 -52.677  19.996  1.00 66.45  ?  142  LEU B O   1 
ATOM   2276  C  CB  . LEU B 2  142  ? -33.694 -49.990  18.718  1.00 64.48  ?  142  LEU B CB  1 
ATOM   2277  C  CG  . LEU B 2  142  ? -34.382 -49.961  17.349  1.00 64.53  ?  142  LEU B CG  1 
ATOM   2278  C  CD1 . LEU B 2  142  ? -35.335 -48.784  17.259  1.00 71.90  ?  142  LEU B CD1 1 
ATOM   2279  C  CD2 . LEU B 2  142  ? -33.370 -49.889  16.220  1.00 66.98  ?  142  LEU B CD2 1 
ATOM   2280  N  N   . PHE B 2  143  ? -33.974 -53.186  17.963  1.00 68.98  ?  143  PHE B N   1 
ATOM   2281  C  CA  . PHE B 2  143  ? -34.902 -54.300  17.802  1.00 76.75  ?  143  PHE B CA  1 
ATOM   2282  C  C   . PHE B 2  143  ? -34.512 -55.479  18.686  1.00 75.24  ?  143  PHE B C   1 
ATOM   2283  O  O   . PHE B 2  143  ? -35.382 -56.180  19.216  1.00 71.24  ?  143  PHE B O   1 
ATOM   2284  C  CB  . PHE B 2  143  ? -34.967 -54.716  16.334  1.00 72.81  ?  143  PHE B CB  1 
ATOM   2285  C  CG  . PHE B 2  143  ? -35.287 -53.584  15.404  1.00 69.87  ?  143  PHE B CG  1 
ATOM   2286  C  CD1 . PHE B 2  143  ? -36.513 -52.945  15.473  1.00 71.88  ?  143  PHE B CD1 1 
ATOM   2287  C  CD2 . PHE B 2  143  ? -34.360 -53.149  14.473  1.00 76.00  ?  143  PHE B CD2 1 
ATOM   2288  C  CE1 . PHE B 2  143  ? -36.814 -51.899  14.622  1.00 74.19  ?  143  PHE B CE1 1 
ATOM   2289  C  CE2 . PHE B 2  143  ? -34.655 -52.104  13.619  1.00 74.25  ?  143  PHE B CE2 1 
ATOM   2290  C  CZ  . PHE B 2  143  ? -35.884 -51.478  13.694  1.00 74.39  ?  143  PHE B CZ  1 
ATOM   2291  N  N   . ALA B 2  144  ? -33.209 -55.714  18.860  1.00 44.66  ?  144  ALA B N   1 
ATOM   2292  C  CA  . ALA B 2  144  ? -32.772 -56.772  19.762  1.00 38.32  ?  144  ALA B CA  1 
ATOM   2293  C  C   . ALA B 2  144  ? -33.112 -56.446  21.211  1.00 54.61  ?  144  ALA B C   1 
ATOM   2294  O  O   . ALA B 2  144  ? -33.360 -57.358  22.007  1.00 67.42  ?  144  ALA B O   1 
ATOM   2295  C  CB  . ALA B 2  144  ? -31.271 -57.012  19.608  1.00 37.43  ?  144  ALA B CB  1 
ATOM   2296  N  N   . GLN B 2  145  ? -33.123 -55.161  21.573  1.00 69.00  ?  145  GLN B N   1 
ATOM   2297  C  CA  . GLN B 2  145  ? -33.524 -54.781  22.924  1.00 72.11  ?  145  GLN B CA  1 
ATOM   2298  C  C   . GLN B 2  145  ? -35.031 -54.894  23.106  1.00 71.05  ?  145  GLN B C   1 
ATOM   2299  O  O   . GLN B 2  145  ? -35.507 -55.270  24.184  1.00 77.07  ?  145  GLN B O   1 
ATOM   2300  C  CB  . GLN B 2  145  ? -33.056 -53.361  23.236  1.00 67.77  ?  145  GLN B CB  1 
ATOM   2301  C  CG  . GLN B 2  145  ? -31.571 -53.136  23.049  1.00 69.11  ?  145  GLN B CG  1 
ATOM   2302  C  CD  . GLN B 2  145  ? -30.740 -53.931  24.034  1.00 71.44  ?  145  GLN B CD  1 
ATOM   2303  O  OE1 . GLN B 2  145  ? -29.948 -54.791  23.645  1.00 76.42  ?  145  GLN B OE1 1 
ATOM   2304  N  NE2 . GLN B 2  145  ? -30.924 -53.656  25.316  1.00 66.37  ?  145  GLN B NE2 1 
ATOM   2305  N  N   . ALA B 2  146  ? -35.799 -54.571  22.066  1.00 45.71  ?  146  ALA B N   1 
ATOM   2306  C  CA  . ALA B 2  146  ? -37.252 -54.570  22.162  1.00 44.25  ?  146  ALA B CA  1 
ATOM   2307  C  C   . ALA B 2  146  ? -37.867 -55.945  21.948  1.00 43.50  ?  146  ALA B C   1 
ATOM   2308  O  O   . ALA B 2  146  ? -39.072 -56.104  22.168  1.00 46.69  ?  146  ALA B O   1 
ATOM   2309  C  CB  . ALA B 2  146  ? -37.841 -53.588  21.153  1.00 45.53  ?  146  ALA B CB  1 
ATOM   2310  N  N   . GLU B 2  147  ? -37.078 -56.934  21.524  1.00 66.08  ?  147  GLU B N   1 
ATOM   2311  C  CA  . GLU B 2  147  ? -37.606 -58.284  21.376  1.00 71.14  ?  147  GLU B CA  1 
ATOM   2312  C  C   . GLU B 2  147  ? -38.070 -58.860  22.706  1.00 72.36  ?  147  GLU B C   1 
ATOM   2313  O  O   . GLU B 2  147  ? -38.860 -59.810  22.717  1.00 77.78  ?  147  GLU B O   1 
ATOM   2314  C  CB  . GLU B 2  147  ? -36.551 -59.191  20.742  1.00 73.58  ?  147  GLU B CB  1 
ATOM   2315  C  CG  . GLU B 2  147  ? -37.117 -60.226  19.784  1.00 73.35  ?  147  GLU B CG  1 
ATOM   2316  C  CD  . GLU B 2  147  ? -37.627 -59.615  18.493  1.00 80.90  ?  147  GLU B CD  1 
ATOM   2317  O  OE1 . GLU B 2  147  ? -36.995 -58.660  17.993  1.00 74.59  ?  147  GLU B OE1 1 
ATOM   2318  O  OE2 . GLU B 2  147  ? -38.661 -60.090  17.977  1.00 97.00  -1 147  GLU B OE2 1 
ATOM   2319  N  N   . ILE B 2  148  ? -37.601 -58.302  23.825  1.00 57.16  ?  148  ILE B N   1 
ATOM   2320  C  CA  . ILE B 2  148  ? -38.071 -58.742  25.135  1.00 61.66  ?  148  ILE B CA  1 
ATOM   2321  C  C   . ILE B 2  148  ? -39.560 -58.457  25.282  1.00 60.02  ?  148  ILE B C   1 
ATOM   2322  O  O   . ILE B 2  148  ? -40.356 -59.352  25.592  1.00 59.33  ?  148  ILE B O   1 
ATOM   2323  C  CB  . ILE B 2  148  ? -37.255 -58.066  26.252  1.00 45.57  ?  148  ILE B CB  1 
ATOM   2324  C  CG1 . ILE B 2  148  ? -35.862 -58.690  26.347  1.00 43.06  ?  148  ILE B CG1 1 
ATOM   2325  C  CG2 . ILE B 2  148  ? -37.977 -58.180  27.584  1.00 46.43  ?  148  ILE B CG2 1 
ATOM   2326  C  CD1 . ILE B 2  148  ? -35.877 -60.163  26.678  1.00 50.95  ?  148  ILE B CD1 1 
ATOM   2327  N  N   . LEU B 2  149  ? -39.960 -57.204  25.049  1.00 52.77  ?  149  LEU B N   1 
ATOM   2328  C  CA  . LEU B 2  149  ? -41.369 -56.844  25.160  1.00 56.25  ?  149  LEU B CA  1 
ATOM   2329  C  C   . LEU B 2  149  ? -42.195 -57.439  24.026  1.00 57.44  ?  149  LEU B C   1 
ATOM   2330  O  O   . LEU B 2  149  ? -43.389 -57.702  24.207  1.00 59.76  ?  149  LEU B O   1 
ATOM   2331  C  CB  . LEU B 2  149  ? -41.522 -55.323  25.187  1.00 55.18  ?  149  LEU B CB  1 
ATOM   2332  C  CG  . LEU B 2  149  ? -42.845 -54.786  25.738  1.00 39.98  ?  149  LEU B CG  1 
ATOM   2333  C  CD1 . LEU B 2  149  ? -42.993 -55.152  27.203  1.00 43.02  ?  149  LEU B CD1 1 
ATOM   2334  C  CD2 . LEU B 2  149  ? -42.938 -53.280  25.549  1.00 42.62  ?  149  LEU B CD2 1 
ATOM   2335  N  N   . THR B 2  150  ? -41.586 -57.655  22.857  1.00 75.87  ?  150  THR B N   1 
ATOM   2336  C  CA  . THR B 2  150  ? -42.310 -58.278  21.753  1.00 81.78  ?  150  THR B CA  1 
ATOM   2337  C  C   . THR B 2  150  ? -42.719 -59.703  22.105  1.00 81.14  ?  150  THR B C   1 
ATOM   2338  O  O   . THR B 2  150  ? -43.803 -60.161  21.724  1.00 85.32  ?  150  THR B O   1 
ATOM   2339  C  CB  . THR B 2  150  ? -41.455 -58.258  20.484  1.00 79.90  ?  150  THR B CB  1 
ATOM   2340  O  OG1 . THR B 2  150  ? -41.170 -56.902  20.119  1.00 83.51  ?  150  THR B OG1 1 
ATOM   2341  C  CG2 . THR B 2  150  ? -42.178 -58.941  19.331  1.00 73.23  ?  150  THR B CG2 1 
ATOM   2342  N  N   . MET B 2  151  ? -41.869 -60.416  22.846  1.00 80.15  ?  151  MET B N   1 
ATOM   2343  C  CA  . MET B 2  151  ? -42.218 -61.766  23.274  1.00 81.09  ?  151  MET B CA  1 
ATOM   2344  C  C   . MET B 2  151  ? -43.323 -61.746  24.323  1.00 88.40  ?  151  MET B C   1 
ATOM   2345  O  O   . MET B 2  151  ? -44.182 -62.636  24.348  1.00 87.51  ?  151  MET B O   1 
ATOM   2346  C  CB  . MET B 2  151  ? -40.981 -62.479  23.816  1.00 74.24  ?  151  MET B CB  1 
ATOM   2347  C  CG  . MET B 2  151  ? -41.239 -63.899  24.276  1.00 68.66  ?  151  MET B CG  1 
ATOM   2348  S  SD  . MET B 2  151  ? -40.159 -64.380  25.631  1.00 69.10  ?  151  MET B SD  1 
ATOM   2349  C  CE  . MET B 2  151  ? -41.039 -65.796  26.282  1.00 71.23  ?  151  MET B CE  1 
ATOM   2350  N  N   . TYR B 2  152  ? -43.320 -60.740  25.195  1.00 81.92  ?  152  TYR B N   1 
ATOM   2351  C  CA  . TYR B 2  152  ? -44.305 -60.625  26.260  1.00 75.87  ?  152  TYR B CA  1 
ATOM   2352  C  C   . TYR B 2  152  ? -45.546 -59.848  25.834  1.00 81.07  ?  152  TYR B C   1 
ATOM   2353  O  O   . TYR B 2  152  ? -46.242 -59.294  26.692  1.00 80.82  ?  152  TYR B O   1 
ATOM   2354  C  CB  . TYR B 2  152  ? -43.671 -59.972  27.489  1.00 67.46  ?  152  TYR B CB  1 
ATOM   2355  C  CG  . TYR B 2  152  ? -42.709 -60.871  28.230  1.00 63.84  ?  152  TYR B CG  1 
ATOM   2356  C  CD1 . TYR B 2  152  ? -43.160 -61.993  28.911  1.00 65.84  ?  152  TYR B CD1 1 
ATOM   2357  C  CD2 . TYR B 2  152  ? -41.347 -60.600  28.243  1.00 59.11  ?  152  TYR B CD2 1 
ATOM   2358  C  CE1 . TYR B 2  152  ? -42.281 -62.817  29.589  1.00 60.82  ?  152  TYR B CE1 1 
ATOM   2359  C  CE2 . TYR B 2  152  ? -40.462 -61.416  28.917  1.00 53.54  ?  152  TYR B CE2 1 
ATOM   2360  C  CZ  . TYR B 2  152  ? -40.933 -62.523  29.588  1.00 56.90  ?  152  TYR B CZ  1 
ATOM   2361  O  OH  . TYR B 2  152  ? -40.051 -63.338  30.259  1.00 52.61  ?  152  TYR B OH  1 
ATOM   2362  N  N   . ASP B 2  153  ? -45.835 -59.790  24.539  1.00 116.08 ?  153  ASP B N   1 
ATOM   2363  C  CA  . ASP B 2  153  ? -47.046 -59.120  24.082  1.00 118.15 ?  153  ASP B CA  1 
ATOM   2364  C  C   . ASP B 2  153  ? -48.268 -59.946  24.462  1.00 122.84 ?  153  ASP B C   1 
ATOM   2365  O  O   . ASP B 2  153  ? -48.289 -61.160  24.225  1.00 120.03 ?  153  ASP B O   1 
ATOM   2366  C  CB  . ASP B 2  153  ? -47.011 -58.903  22.571  1.00 121.23 ?  153  ASP B CB  1 
ATOM   2367  C  CG  . ASP B 2  153  ? -46.038 -57.818  22.160  1.00 129.61 ?  153  ASP B CG  1 
ATOM   2368  O  OD1 . ASP B 2  153  ? -45.812 -56.888  22.962  1.00 124.62 ?  153  ASP B OD1 1 
ATOM   2369  O  OD2 . ASP B 2  153  ? -45.500 -57.894  21.036  1.00 135.64 -1 153  ASP B OD2 1 
ATOM   2370  N  N   . PRO B 2  154  ? -49.302 -59.336  25.049  1.00 73.73  ?  154  PRO B N   1 
ATOM   2371  C  CA  . PRO B 2  154  ? -50.523 -60.088  25.366  1.00 75.64  ?  154  PRO B CA  1 
ATOM   2372  C  C   . PRO B 2  154  ? -51.373 -60.415  24.150  1.00 77.66  ?  154  PRO B C   1 
ATOM   2373  O  O   . PRO B 2  154  ? -52.382 -61.115  24.295  1.00 79.67  ?  154  PRO B O   1 
ATOM   2374  C  CB  . PRO B 2  154  ? -51.268 -59.148  26.323  1.00 67.00  ?  154  PRO B CB  1 
ATOM   2375  C  CG  . PRO B 2  154  ? -50.823 -57.786  25.917  1.00 60.95  ?  154  PRO B CG  1 
ATOM   2376  C  CD  . PRO B 2  154  ? -49.394 -57.923  25.460  1.00 61.74  ?  154  PRO B CD  1 
ATOM   2377  N  N   . ASP B 2  155  ? -51.001 -59.936  22.964  1.00 91.75  ?  155  ASP B N   1 
ATOM   2378  C  CA  . ASP B 2  155  ? -51.754 -60.174  21.741  1.00 84.17  ?  155  ASP B CA  1 
ATOM   2379  C  C   . ASP B 2  155  ? -51.117 -61.232  20.849  1.00 92.10  ?  155  ASP B C   1 
ATOM   2380  O  O   . ASP B 2  155  ? -51.543 -61.397  19.702  1.00 106.80 ?  155  ASP B O   1 
ATOM   2381  C  CB  . ASP B 2  155  ? -51.918 -58.867  20.961  1.00 92.00  ?  155  ASP B CB  1 
ATOM   2382  C  CG  . ASP B 2  155  ? -52.535 -57.765  21.797  1.00 92.99  ?  155  ASP B CG  1 
ATOM   2383  O  OD1 . ASP B 2  155  ? -53.663 -57.960  22.296  1.00 89.33  ?  155  ASP B OD1 1 
ATOM   2384  O  OD2 . ASP B 2  155  ? -51.891 -56.708  21.960  1.00 99.07  -1 155  ASP B OD2 1 
ATOM   2385  N  N   . ARG B 2  156  ? -50.109 -61.945  21.342  1.00 67.96  ?  156  ARG B N   1 
ATOM   2386  C  CA  . ARG B 2  156  ? -49.515 -63.024  20.568  1.00 71.71  ?  156  ARG B CA  1 
ATOM   2387  C  C   . ARG B 2  156  ? -50.489 -64.191  20.446  1.00 71.22  ?  156  ARG B C   1 
ATOM   2388  O  O   . ARG B 2  156  ? -51.300 -64.451  21.339  1.00 67.40  ?  156  ARG B O   1 
ATOM   2389  C  CB  . ARG B 2  156  ? -48.209 -63.490  21.211  1.00 66.17  ?  156  ARG B CB  1 
ATOM   2390  C  CG  . ARG B 2  156  ? -47.004 -62.627  20.867  1.00 59.11  ?  156  ARG B CG  1 
ATOM   2391  C  CD  . ARG B 2  156  ? -45.760 -63.112  21.592  1.00 56.98  ?  156  ARG B CD  1 
ATOM   2392  N  NE  . ARG B 2  156  ? -45.481 -64.518  21.325  1.00 69.25  ?  156  ARG B NE  1 
ATOM   2393  C  CZ  . ARG B 2  156  ? -44.813 -65.318  22.145  1.00 62.25  ?  156  ARG B CZ  1 
ATOM   2394  N  NH1 . ARG B 2  156  ? -44.338 -64.883  23.301  1.00 56.34  ?  156  ARG B NH1 1 
ATOM   2395  N  NH2 . ARG B 2  156  ? -44.623 -66.588  21.801  1.00 64.89  ?  156  ARG B NH2 1 
ATOM   2396  N  N   . SER B 2  157  ? -50.406 -64.893  19.317  1.00 92.53  ?  157  SER B N   1 
ATOM   2397  C  CA  . SER B 2  157  ? -51.324 -65.993  19.052  1.00 98.48  ?  157  SER B CA  1 
ATOM   2398  C  C   . SER B 2  157  ? -51.122 -67.115  20.061  1.00 95.03  ?  157  SER B C   1 
ATOM   2399  O  O   . SER B 2  157  ? -49.992 -67.465  20.411  1.00 87.38  ?  157  SER B O   1 
ATOM   2400  C  CB  . SER B 2  157  ? -51.126 -66.520  17.630  1.00 103.48 ?  157  SER B CB  1 
ATOM   2401  O  OG  . SER B 2  157  ? -49.750 -66.660  17.325  1.00 107.45 ?  157  SER B OG  1 
ATOM   2402  N  N   . THR B 2  158  ? -52.236 -67.679  20.533  1.00 88.42  ?  158  THR B N   1 
ATOM   2403  C  CA  . THR B 2  158  ? -52.206 -68.718  21.549  1.00 77.11  ?  158  THR B CA  1 
ATOM   2404  C  C   . THR B 2  158  ? -52.760 -70.059  21.094  1.00 79.06  ?  158  THR B C   1 
ATOM   2405  O  O   . THR B 2  158  ? -52.472 -71.071  21.742  1.00 82.92  ?  158  THR B O   1 
ATOM   2406  C  CB  . THR B 2  158  ? -52.985 -68.274  22.800  1.00 68.81  ?  158  THR B CB  1 
ATOM   2407  O  OG1 . THR B 2  158  ? -54.392 -68.406  22.563  1.00 80.31  ?  158  THR B OG1 1 
ATOM   2408  C  CG2 . THR B 2  158  ? -52.665 -66.829  23.148  1.00 62.77  ?  158  THR B CG2 1 
ATOM   2409  N  N   . THR B 2  159  ? -53.534 -70.104  20.012  1.00 79.15  ?  159  THR B N   1 
ATOM   2410  C  CA  . THR B 2  159  ? -54.168 -71.339  19.580  1.00 89.40  ?  159  THR B CA  1 
ATOM   2411  C  C   . THR B 2  159  ? -54.210 -71.398  18.060  1.00 91.09  ?  159  THR B C   1 
ATOM   2412  O  O   . THR B 2  159  ? -54.103 -70.381  17.371  1.00 88.09  ?  159  THR B O   1 
ATOM   2413  C  CB  . THR B 2  159  ? -55.589 -71.473  20.149  1.00 94.74  ?  159  THR B CB  1 
ATOM   2414  O  OG1 . THR B 2  159  ? -56.185 -72.689  19.679  1.00 102.86 ?  159  THR B OG1 1 
ATOM   2415  C  CG2 . THR B 2  159  ? -56.449 -70.290  19.723  1.00 87.05  ?  159  THR B CG2 1 
ATOM   2416  N  N   . VAL B 2  160  ? -54.366 -72.616  17.548  1.00 93.19  ?  160  VAL B N   1 
ATOM   2417  C  CA  . VAL B 2  160  ? -54.521 -72.844  16.117  1.00 93.06  ?  160  VAL B CA  1 
ATOM   2418  C  C   . VAL B 2  160  ? -55.940 -72.483  15.706  1.00 102.64 ?  160  VAL B C   1 
ATOM   2419  O  O   . VAL B 2  160  ? -56.913 -72.850  16.378  1.00 105.91 ?  160  VAL B O   1 
ATOM   2420  C  CB  . VAL B 2  160  ? -54.191 -74.307  15.769  1.00 97.23  ?  160  VAL B CB  1 
ATOM   2421  C  CG1 . VAL B 2  160  ? -54.523 -74.601  14.316  1.00 105.56 ?  160  VAL B CG1 1 
ATOM   2422  C  CG2 . VAL B 2  160  ? -52.727 -74.601  16.054  1.00 96.69  ?  160  VAL B CG2 1 
ATOM   2423  N  N   . LEU B 2  161  ? -56.068 -71.757  14.597  1.00 99.08  ?  161  LEU B N   1 
ATOM   2424  C  CA  . LEU B 2  161  ? -57.363 -71.308  14.094  1.00 105.99 ?  161  LEU B CA  1 
ATOM   2425  C  C   . LEU B 2  161  ? -57.573 -71.858  12.689  1.00 106.75 ?  161  LEU B C   1 
ATOM   2426  O  O   . LEU B 2  161  ? -56.873 -71.460  11.752  1.00 114.49 ?  161  LEU B O   1 
ATOM   2427  C  CB  . LEU B 2  161  ? -57.457 -69.783  14.109  1.00 100.03 ?  161  LEU B CB  1 
ATOM   2428  C  CG  . LEU B 2  161  ? -57.136 -69.124  15.450  1.00 85.66  ?  161  LEU B CG  1 
ATOM   2429  C  CD1 . LEU B 2  161  ? -56.902 -67.632  15.275  1.00 88.97  ?  161  LEU B CD1 1 
ATOM   2430  C  CD2 . LEU B 2  161  ? -58.249 -69.385  16.456  1.00 87.92  ?  161  LEU B CD2 1 
ATOM   2431  N  N   . ARG B 2  162  ? -58.542 -72.767  12.542  1.00 107.01 ?  162  ARG B N   1 
ATOM   2432  C  CA  . ARG B 2  162  ? -58.847 -73.313  11.223  1.00 115.13 ?  162  ARG B CA  1 
ATOM   2433  C  C   . ARG B 2  162  ? -59.450 -72.249  10.317  1.00 122.13 ?  162  ARG B C   1 
ATOM   2434  O  O   . ARG B 2  162  ? -59.023 -72.083  9.170   1.00 126.25 ?  162  ARG B O   1 
ATOM   2435  C  CB  . ARG B 2  162  ? -59.793 -74.509  11.343  1.00 116.10 ?  162  ARG B CB  1 
ATOM   2436  C  CG  . ARG B 2  162  ? -59.956 -75.283  10.040  1.00 125.26 ?  162  ARG B CG  1 
ATOM   2437  C  CD  . ARG B 2  162  ? -61.004 -76.377  10.143  1.00 133.56 ?  162  ARG B CD  1 
ATOM   2438  N  NE  . ARG B 2  162  ? -62.350 -75.853  9.948   1.00 151.21 ?  162  ARG B NE  1 
ATOM   2439  C  CZ  . ARG B 2  162  ? -62.985 -75.833  8.784   1.00 147.06 ?  162  ARG B CZ  1 
ATOM   2440  N  NH1 . ARG B 2  162  ? -62.424 -76.303  7.682   1.00 137.56 ?  162  ARG B NH1 1 
ATOM   2441  N  NH2 . ARG B 2  162  ? -64.215 -75.329  8.725   1.00 148.39 ?  162  ARG B NH2 1 
ATOM   2442  N  N   . GLN B 2  163  ? -60.448 -71.526  10.812  1.00 103.45 ?  163  GLN B N   1 
ATOM   2443  C  CA  . GLN B 2  163  ? -61.073 -70.444  10.061  1.00 111.50 ?  163  GLN B CA  1 
ATOM   2444  C  C   . GLN B 2  163  ? -61.506 -69.358  11.043  1.00 106.57 ?  163  GLN B C   1 
ATOM   2445  O  O   . GLN B 2  163  ? -62.660 -68.925  11.068  1.00 104.01 ?  163  GLN B O   1 
ATOM   2446  C  CB  . GLN B 2  163  ? -62.253 -70.960  9.237   1.00 123.38 ?  163  GLN B CB  1 
ATOM   2447  C  CG  . GLN B 2  163  ? -61.873 -71.553  7.883   1.00 116.78 ?  163  GLN B CG  1 
ATOM   2448  C  CD  . GLN B 2  163  ? -62.991 -71.453  6.862   1.00 118.72 ?  163  GLN B CD  1 
ATOM   2449  O  OE1 . GLN B 2  163  ? -64.020 -70.823  7.108   1.00 124.01 ?  163  GLN B OE1 1 
ATOM   2450  N  NE2 . GLN B 2  163  ? -62.796 -72.083  5.710   1.00 126.81 ?  163  GLN B NE2 1 
ATOM   2451  N  N   . GLY B 2  164  ? -60.559 -68.892  11.859  1.00 102.21 ?  164  GLY B N   1 
ATOM   2452  C  CA  . GLY B 2  164  ? -60.868 -68.131  13.054  1.00 94.39  ?  164  GLY B CA  1 
ATOM   2453  C  C   . GLY B 2  164  ? -61.394 -68.976  14.188  1.00 95.68  ?  164  GLY B C   1 
ATOM   2454  O  O   . GLY B 2  164  ? -61.500 -68.480  15.316  1.00 91.68  ?  164  GLY B O   1 
ATOM   2455  N  N   . VAL B 2  165  ? -61.698 -70.238  13.933  1.00 144.77 ?  165  VAL B N   1 
ATOM   2456  C  CA  . VAL B 2  165  ? -62.195 -71.129  14.976  1.00 141.78 ?  165  VAL B CA  1 
ATOM   2457  C  C   . VAL B 2  165  ? -61.011 -71.755  15.710  1.00 138.72 ?  165  VAL B C   1 
ATOM   2458  O  O   . VAL B 2  165  ? -60.059 -72.220  15.061  1.00 140.03 ?  165  VAL B O   1 
ATOM   2459  C  CB  . VAL B 2  165  ? -63.089 -72.185  14.361  1.00 157.24 ?  165  VAL B CB  1 
ATOM   2460  C  CG1 . VAL B 2  165  ? -62.368 -72.885  13.251  1.00 160.22 ?  165  VAL B CG1 1 
ATOM   2461  C  CG2 . VAL B 2  165  ? -63.483 -73.168  15.416  1.00 159.09 ?  165  VAL B CG2 1 
ATOM   2462  N  N   . PRO B 2  166  ? -61.018 -71.778  17.041  1.00 93.93  ?  166  PRO B N   1 
ATOM   2463  C  CA  . PRO B 2  166  ? -59.971 -72.512  17.761  1.00 88.86  ?  166  PRO B CA  1 
ATOM   2464  C  C   . PRO B 2  166  ? -59.982 -73.988  17.387  1.00 87.49  ?  166  PRO B C   1 
ATOM   2465  O  O   . PRO B 2  166  ? -61.014 -74.660  17.457  1.00 85.40  ?  166  PRO B O   1 
ATOM   2466  C  CB  . PRO B 2  166  ? -60.328 -72.293  19.235  1.00 82.80  ?  166  PRO B CB  1 
ATOM   2467  C  CG  . PRO B 2  166  ? -61.110 -71.031  19.240  1.00 78.71  ?  166  PRO B CG  1 
ATOM   2468  C  CD  . PRO B 2  166  ? -61.891 -71.028  17.957  1.00 90.59  ?  166  PRO B CD  1 
ATOM   2469  N  N   . SER B 2  167  ? -58.818 -74.491  16.971  1.00 106.91 ?  167  SER B N   1 
ATOM   2470  C  CA  . SER B 2  167  ? -58.695 -75.894  16.597  1.00 113.05 ?  167  SER B CA  1 
ATOM   2471  C  C   . SER B 2  167  ? -57.494 -76.533  17.285  1.00 105.00 ?  167  SER B C   1 
ATOM   2472  O  O   . SER B 2  167  ? -56.944 -75.971  18.238  1.00 100.02 ?  167  SER B O   1 
ATOM   2473  C  CB  . SER B 2  167  ? -58.585 -76.033  15.077  1.00 117.03 ?  167  SER B CB  1 
ATOM   2474  O  OG  . SER B 2  167  ? -58.894 -77.352  14.657  1.00 131.30 ?  167  SER B OG  1 
ATOM   2475  N  N   . THR B 2  168  ? -57.080 -77.706  16.815  1.00 129.20 ?  168  THR B N   1 
ATOM   2476  C  CA  . THR B 2  168  ? -55.979 -78.447  17.415  1.00 129.12 ?  168  THR B CA  1 
ATOM   2477  C  C   . THR B 2  168  ? -54.854 -78.635  16.404  1.00 126.83 ?  168  THR B C   1 
ATOM   2478  O  O   . THR B 2  168  ? -54.999 -78.356  15.211  1.00 132.43 ?  168  THR B O   1 
ATOM   2479  C  CB  . THR B 2  168  ? -56.452 -79.810  17.939  1.00 130.14 ?  168  THR B CB  1 
ATOM   2480  O  OG1 . THR B 2  168  ? -56.970 -80.588  16.853  1.00 139.94 ?  168  THR B OG1 1 
ATOM   2481  C  CG2 . THR B 2  168  ? -57.537 -79.627  18.990  1.00 136.81 ?  168  THR B CG2 1 
ATOM   2482  N  N   . TRP B 2  169  ? -53.715 -79.116  16.907  1.00 97.71  ?  169  TRP B N   1 
ATOM   2483  C  CA  . TRP B 2  169  ? -52.554 -79.356  16.057  1.00 95.82  ?  169  TRP B CA  1 
ATOM   2484  C  C   . TRP B 2  169  ? -52.643 -80.696  15.337  1.00 98.89  ?  169  TRP B C   1 
ATOM   2485  O  O   . TRP B 2  169  ? -52.132 -80.828  14.219  1.00 102.87 ?  169  TRP B O   1 
ATOM   2486  C  CB  . TRP B 2  169  ? -51.275 -79.281  16.895  1.00 92.15  ?  169  TRP B CB  1 
ATOM   2487  C  CG  . TRP B 2  169  ? -50.039 -79.810  16.220  1.00 92.05  ?  169  TRP B CG  1 
ATOM   2488  C  CD1 . TRP B 2  169  ? -49.414 -80.997  16.472  1.00 89.56  ?  169  TRP B CD1 1 
ATOM   2489  C  CD2 . TRP B 2  169  ? -49.269 -79.161  15.199  1.00 92.60  ?  169  TRP B CD2 1 
ATOM   2490  N  NE1 . TRP B 2  169  ? -48.309 -81.132  15.666  1.00 83.51  ?  169  TRP B NE1 1 
ATOM   2491  C  CE2 . TRP B 2  169  ? -48.197 -80.019  14.876  1.00 80.88  ?  169  TRP B CE2 1 
ATOM   2492  C  CE3 . TRP B 2  169  ? -49.383 -77.941  14.524  1.00 91.54  ?  169  TRP B CE3 1 
ATOM   2493  C  CZ2 . TRP B 2  169  ? -47.248 -79.696  13.908  1.00 72.06  ?  169  TRP B CZ2 1 
ATOM   2494  C  CZ3 . TRP B 2  169  ? -48.439 -77.623  13.562  1.00 82.71  ?  169  TRP B CZ3 1 
ATOM   2495  C  CH2 . TRP B 2  169  ? -47.385 -78.498  13.263  1.00 78.82  ?  169  TRP B CH2 1 
ATOM   2496  N  N   . ALA B 2  170  ? -53.288 -81.691  15.950  1.00 78.43  ?  170  ALA B N   1 
ATOM   2497  C  CA  . ALA B 2  170  ? -53.437 -82.988  15.298  1.00 78.47  ?  170  ALA B CA  1 
ATOM   2498  C  C   . ALA B 2  170  ? -54.410 -82.910  14.128  1.00 90.94  ?  170  ALA B C   1 
ATOM   2499  O  O   . ALA B 2  170  ? -54.221 -83.585  13.110  1.00 100.75 ?  170  ALA B O   1 
ATOM   2500  C  CB  . ALA B 2  170  ? -53.895 -84.037  16.310  1.00 74.31  ?  170  ALA B CB  1 
ATOM   2501  N  N   . GLU B 2  171  ? -55.461 -82.095  14.257  1.00 111.29 ?  171  GLU B N   1 
ATOM   2502  C  CA  . GLU B 2  171  ? -56.395 -81.915  13.150  1.00 120.49 ?  171  GLU B CA  1 
ATOM   2503  C  C   . GLU B 2  171  ? -55.715 -81.248  11.961  1.00 122.87 ?  171  GLU B C   1 
ATOM   2504  O  O   . GLU B 2  171  ? -55.943 -81.634  10.808  1.00 126.28 ?  171  GLU B O   1 
ATOM   2505  C  CB  . GLU B 2  171  ? -57.600 -81.092  13.608  1.00 123.11 ?  171  GLU B CB  1 
ATOM   2506  C  CG  . GLU B 2  171  ? -58.731 -81.028  12.594  1.00 135.04 ?  171  GLU B CG  1 
ATOM   2507  C  CD  . GLU B 2  171  ? -60.097 -80.958  13.247  1.00 144.08 ?  171  GLU B CD  1 
ATOM   2508  O  OE1 . GLU B 2  171  ? -60.409 -79.917  13.862  1.00 134.32 ?  171  GLU B OE1 1 
ATOM   2509  O  OE2 . GLU B 2  171  ? -60.861 -81.941  13.141  1.00 159.01 -1 171  GLU B OE2 1 
ATOM   2510  N  N   . PHE B 2  172  ? -54.875 -80.245  12.224  1.00 106.55 ?  172  PHE B N   1 
ATOM   2511  C  CA  . PHE B 2  172  ? -54.141 -79.590  11.146  1.00 106.73 ?  172  PHE B CA  1 
ATOM   2512  C  C   . PHE B 2  172  ? -53.137 -80.541  10.506  1.00 109.53 ?  172  PHE B C   1 
ATOM   2513  O  O   . PHE B 2  172  ? -52.932 -80.508  9.287   1.00 115.05 ?  172  PHE B O   1 
ATOM   2514  C  CB  . PHE B 2  172  ? -53.437 -78.342  11.678  1.00 96.50  ?  172  PHE B CB  1 
ATOM   2515  C  CG  . PHE B 2  172  ? -52.368 -77.812  10.767  1.00 97.01  ?  172  PHE B CG  1 
ATOM   2516  C  CD1 . PHE B 2  172  ? -52.702 -77.169  9.586   1.00 99.68  ?  172  PHE B CD1 1 
ATOM   2517  C  CD2 . PHE B 2  172  ? -51.028 -77.953  11.092  1.00 94.60  ?  172  PHE B CD2 1 
ATOM   2518  C  CE1 . PHE B 2  172  ? -51.720 -76.679  8.745   1.00 97.00  ?  172  PHE B CE1 1 
ATOM   2519  C  CE2 . PHE B 2  172  ? -50.042 -77.465  10.255  1.00 86.43  ?  172  PHE B CE2 1 
ATOM   2520  C  CZ  . PHE B 2  172  ? -50.389 -76.828  9.080   1.00 86.15  ?  172  PHE B CZ  1 
ATOM   2521  N  N   . THR B 2  173  ? -52.503 -81.395  11.313  1.00 89.37  ?  173  THR B N   1 
ATOM   2522  C  CA  . THR B 2  173  ? -51.556 -82.363  10.771  1.00 89.57  ?  173  THR B CA  1 
ATOM   2523  C  C   . THR B 2  173  ? -52.251 -83.360  9.851   1.00 93.97  ?  173  THR B C   1 
ATOM   2524  O  O   . THR B 2  173  ? -51.742 -83.679  8.770   1.00 93.68  ?  173  THR B O   1 
ATOM   2525  C  CB  . THR B 2  173  ? -50.838 -83.086  11.912  1.00 83.29  ?  173  THR B CB  1 
ATOM   2526  O  OG1 . THR B 2  173  ? -49.875 -82.205  12.504  1.00 71.73  ?  173  THR B OG1 1 
ATOM   2527  C  CG2 . THR B 2  173  ? -50.135 -84.339  11.408  1.00 86.30  ?  173  THR B CG2 1 
ATOM   2528  N  N   . THR B 2  174  ? -53.421 -83.855  10.259  1.00 103.49 ?  174  THR B N   1 
ATOM   2529  C  CA  . THR B 2  174  ? -54.165 -84.784  9.413   1.00 110.77 ?  174  THR B CA  1 
ATOM   2530  C  C   . THR B 2  174  ? -54.635 -84.107  8.131   1.00 105.19 ?  174  THR B C   1 
ATOM   2531  O  O   . THR B 2  174  ? -54.610 -84.717  7.055   1.00 109.15 ?  174  THR B O   1 
ATOM   2532  C  CB  . THR B 2  174  ? -55.354 -85.360  10.182  1.00 108.21 ?  174  THR B CB  1 
ATOM   2533  O  OG1 . THR B 2  174  ? -54.956 -85.669  11.524  1.00 92.47  ?  174  THR B OG1 1 
ATOM   2534  C  CG2 . THR B 2  174  ? -55.862 -86.624  9.506   1.00 112.80 ?  174  THR B CG2 1 
ATOM   2535  N  N   . THR B 2  175  ? -55.065 -82.847  8.223   1.00 99.62  ?  175  THR B N   1 
ATOM   2536  C  CA  . THR B 2  175  ? -55.495 -82.127  7.028   1.00 108.60 ?  175  THR B CA  1 
ATOM   2537  C  C   . THR B 2  175  ? -54.321 -81.857  6.095   1.00 109.21 ?  175  THR B C   1 
ATOM   2538  O  O   . THR B 2  175  ? -54.465 -81.933  4.869   1.00 112.68 ?  175  THR B O   1 
ATOM   2539  C  CB  . THR B 2  175  ? -56.181 -80.817  7.420   1.00 106.08 ?  175  THR B CB  1 
ATOM   2540  O  OG1 . THR B 2  175  ? -57.217 -81.085  8.373   1.00 110.44 ?  175  THR B OG1 1 
ATOM   2541  C  CG2 . THR B 2  175  ? -56.791 -80.144  6.198   1.00 103.52 ?  175  THR B CG2 1 
ATOM   2542  N  N   . LEU B 2  176  ? -53.149 -81.546  6.656   1.00 96.55  ?  176  LEU B N   1 
ATOM   2543  C  CA  . LEU B 2  176  ? -51.971 -81.317  5.825   1.00 92.35  ?  176  LEU B CA  1 
ATOM   2544  C  C   . LEU B 2  176  ? -51.527 -82.599  5.132   1.00 98.75  ?  176  LEU B C   1 
ATOM   2545  O  O   . LEU B 2  176  ? -51.150 -82.576  3.955   1.00 108.07 ?  176  LEU B O   1 
ATOM   2546  C  CB  . LEU B 2  176  ? -50.834 -80.744  6.670   1.00 87.73  ?  176  LEU B CB  1 
ATOM   2547  C  CG  . LEU B 2  176  ? -49.551 -80.393  5.914   1.00 87.32  ?  176  LEU B CG  1 
ATOM   2548  C  CD1 . LEU B 2  176  ? -49.748 -79.142  5.069   1.00 76.66  ?  176  LEU B CD1 1 
ATOM   2549  C  CD2 . LEU B 2  176  ? -48.387 -80.219  6.876   1.00 89.96  ?  176  LEU B CD2 1 
ATOM   2550  N  N   . GLY B 2  177  ? -51.564 -83.726  5.846   1.00 87.03  ?  177  GLY B N   1 
ATOM   2551  C  CA  . GLY B 2  177  ? -51.183 -84.988  5.233   1.00 89.84  ?  177  GLY B CA  1 
ATOM   2552  C  C   . GLY B 2  177  ? -52.150 -85.427  4.151   1.00 92.10  ?  177  GLY B C   1 
ATOM   2553  O  O   . GLY B 2  177  ? -51.742 -86.009  3.141   1.00 93.28  ?  177  GLY B O   1 
ATOM   2554  N  N   . ASN B 2  178  ? -53.443 -85.157  4.344   1.00 96.69  ?  178  ASN B N   1 
ATOM   2555  C  CA  . ASN B 2  178  ? -54.425 -85.482  3.315   1.00 102.75 ?  178  ASN B CA  1 
ATOM   2556  C  C   . ASN B 2  178  ? -54.273 -84.570  2.105   1.00 103.77 ?  178  ASN B C   1 
ATOM   2557  O  O   . ASN B 2  178  ? -54.426 -85.016  0.961   1.00 105.69 ?  178  ASN B O   1 
ATOM   2558  C  CB  . ASN B 2  178  ? -55.838 -85.385  3.887   1.00 106.43 ?  178  ASN B CB  1 
ATOM   2559  C  CG  . ASN B 2  178  ? -56.227 -86.611  4.687   1.00 108.29 ?  178  ASN B CG  1 
ATOM   2560  O  OD1 . ASN B 2  178  ? -55.541 -87.632  4.653   1.00 98.32  ?  178  ASN B OD1 1 
ATOM   2561  N  ND2 . ASN B 2  178  ? -57.337 -86.518  5.410   1.00 105.39 ?  178  ASN B ND2 1 
ATOM   2562  N  N   . ALA B 2  179  ? -53.973 -83.289  2.336   1.00 113.86 ?  179  ALA B N   1 
ATOM   2563  C  CA  . ALA B 2  179  ? -53.773 -82.365  1.226   1.00 113.42 ?  179  ALA B CA  1 
ATOM   2564  C  C   . ALA B 2  179  ? -52.498 -82.691  0.460   1.00 107.61 ?  179  ALA B C   1 
ATOM   2565  O  O   . ALA B 2  179  ? -52.458 -82.574  -0.770  1.00 112.96 ?  179  ALA B O   1 
ATOM   2566  C  CB  . ALA B 2  179  ? -53.740 -80.925  1.738   1.00 105.05 ?  179  ALA B CB  1 
ATOM   2567  N  N   . LEU B 2  180  ? -51.446 -83.103  1.168   1.00 69.05  ?  180  LEU B N   1 
ATOM   2568  C  CA  . LEU B 2  180  ? -50.201 -83.457  0.500   1.00 77.81  ?  180  LEU B CA  1 
ATOM   2569  C  C   . LEU B 2  180  ? -50.300 -84.799  -0.214  1.00 87.55  ?  180  LEU B C   1 
ATOM   2570  O  O   . LEU B 2  180  ? -49.537 -85.045  -1.154  1.00 87.13  ?  180  LEU B O   1 
ATOM   2571  C  CB  . LEU B 2  180  ? -49.051 -83.472  1.508   1.00 76.74  ?  180  LEU B CB  1 
ATOM   2572  C  CG  . LEU B 2  180  ? -48.103 -82.270  1.462   1.00 69.18  ?  180  LEU B CG  1 
ATOM   2573  C  CD1 . LEU B 2  180  ? -48.882 -80.969  1.536   1.00 63.62  ?  180  LEU B CD1 1 
ATOM   2574  C  CD2 . LEU B 2  180  ? -47.088 -82.348  2.585   1.00 63.32  ?  180  LEU B CD2 1 
ATOM   2575  N  N   . THR B 2  181  ? -51.223 -85.668  0.208   1.00 131.55 ?  181  THR B N   1 
ATOM   2576  C  CA  . THR B 2  181  ? -51.472 -86.898  -0.536  1.00 130.74 ?  181  THR B CA  1 
ATOM   2577  C  C   . THR B 2  181  ? -52.029 -86.591  -1.919  1.00 126.93 ?  181  THR B C   1 
ATOM   2578  O  O   . THR B 2  181  ? -51.634 -87.217  -2.910  1.00 133.18 ?  181  THR B O   1 
ATOM   2579  C  CB  . THR B 2  181  ? -52.427 -87.804  0.239   1.00 130.21 ?  181  THR B CB  1 
ATOM   2580  O  OG1 . THR B 2  181  ? -51.842 -88.147  1.500   1.00 136.01 ?  181  THR B OG1 1 
ATOM   2581  C  CG2 . THR B 2  181  ? -52.707 -89.075  -0.542  1.00 128.87 ?  181  THR B CG2 1 
ATOM   2582  N  N   . ALA B 2  182  ? -52.946 -85.622  -2.006  1.00 94.96  ?  182  ALA B N   1 
ATOM   2583  C  CA  . ALA B 2  182  ? -53.431 -85.176  -3.308  1.00 101.09 ?  182  ALA B CA  1 
ATOM   2584  C  C   . ALA B 2  182  ? -52.300 -84.586  -4.139  1.00 106.10 ?  182  ALA B C   1 
ATOM   2585  O  O   . ALA B 2  182  ? -52.238 -84.795  -5.356  1.00 111.09 ?  182  ALA B O   1 
ATOM   2586  C  CB  . ALA B 2  182  ? -54.558 -84.158  -3.131  1.00 103.68 ?  182  ALA B CB  1 
ATOM   2587  N  N   . ALA B 2  183  ? -51.393 -83.845  -3.497  1.00 95.62  ?  183  ALA B N   1 
ATOM   2588  C  CA  . ALA B 2  183  ? -50.238 -83.311  -4.210  1.00 90.68  ?  183  ALA B CA  1 
ATOM   2589  C  C   . ALA B 2  183  ? -49.312 -84.423  -4.683  1.00 87.81  ?  183  ALA B C   1 
ATOM   2590  O  O   . ALA B 2  183  ? -48.640 -84.277  -5.710  1.00 89.18  ?  183  ALA B O   1 
ATOM   2591  C  CB  . ALA B 2  183  ? -49.479 -82.331  -3.316  1.00 84.64  ?  183  ALA B CB  1 
ATOM   2592  N  N   . ARG B 2  184  ? -49.266 -85.541  -3.953  1.00 108.78 ?  184  ARG B N   1 
ATOM   2593  C  CA  . ARG B 2  184  ? -48.412 -86.652  -4.358  1.00 109.68 ?  184  ARG B CA  1 
ATOM   2594  C  C   . ARG B 2  184  ? -48.875 -87.264  -5.672  1.00 117.18 ?  184  ARG B C   1 
ATOM   2595  O  O   . ARG B 2  184  ? -48.066 -87.857  -6.396  1.00 116.61 ?  184  ARG B O   1 
ATOM   2596  C  CB  . ARG B 2  184  ? -48.376 -87.720  -3.265  1.00 111.38 ?  184  ARG B CB  1 
ATOM   2597  C  CG  . ARG B 2  184  ? -47.065 -87.794  -2.505  1.00 107.31 ?  184  ARG B CG  1 
ATOM   2598  C  CD  . ARG B 2  184  ? -47.142 -88.821  -1.384  1.00 112.90 ?  184  ARG B CD  1 
ATOM   2599  N  NE  . ARG B 2  184  ? -48.143 -88.473  -0.381  1.00 117.71 ?  184  ARG B NE  1 
ATOM   2600  C  CZ  . ARG B 2  184  ? -47.890 -87.794  0.731   1.00 120.80 ?  184  ARG B CZ  1 
ATOM   2601  N  NH1 . ARG B 2  184  ? -46.671 -87.368  1.019   1.00 125.77 ?  184  ARG B NH1 1 
ATOM   2602  N  NH2 . ARG B 2  184  ? -48.885 -87.539  1.576   1.00 112.14 ?  184  ARG B NH2 1 
ATOM   2603  N  N   . ALA B 2  185  ? -50.167 -87.143  -5.992  1.00 160.21 ?  185  ALA B N   1 
ATOM   2604  C  CA  . ALA B 2  185  ? -50.647 -87.590  -7.296  1.00 161.02 ?  185  ALA B CA  1 
ATOM   2605  C  C   . ALA B 2  185  ? -50.039 -86.750  -8.413  1.00 163.43 ?  185  ALA B C   1 
ATOM   2606  O  O   . ALA B 2  185  ? -49.636 -87.282  -9.453  1.00 163.89 ?  185  ALA B O   1 
ATOM   2607  C  CB  . ALA B 2  185  ? -52.174 -87.540  -7.344  1.00 157.61 ?  185  ALA B CB  1 
ATOM   2608  N  N   . THR B 2  186  ? -49.965 -85.436  -8.214  1.00 110.90 ?  186  THR B N   1 
ATOM   2609  C  CA  . THR B 2  186  ? -49.139 -84.583  -9.056  1.00 104.23 ?  186  THR B CA  1 
ATOM   2610  C  C   . THR B 2  186  ? -47.704 -84.665  -8.551  1.00 102.59 ?  186  THR B C   1 
ATOM   2611  O  O   . THR B 2  186  ? -47.339 -85.624  -7.863  1.00 101.90 ?  186  THR B O   1 
ATOM   2612  C  CB  . THR B 2  186  ? -49.653 -83.143  -9.042  1.00 107.99 ?  186  THR B CB  1 
ATOM   2613  O  OG1 . THR B 2  186  ? -49.303 -82.530  -7.795  1.00 114.40 ?  186  THR B OG1 1 
ATOM   2614  C  CG2 . THR B 2  186  ? -51.158 -83.111  -9.204  1.00 105.57 ?  186  THR B CG2 1 
ATOM   2615  N  N   . GLN B 2  187  ? -46.876 -83.678  -8.875  1.00 101.88 ?  187  GLN B N   1 
ATOM   2616  C  CA  . GLN B 2  187  ? -45.533 -83.599  -8.319  1.00 100.93 ?  187  GLN B CA  1 
ATOM   2617  C  C   . GLN B 2  187  ? -45.379 -82.381  -7.416  1.00 96.25  ?  187  GLN B C   1 
ATOM   2618  O  O   . GLN B 2  187  ? -44.282 -81.838  -7.279  1.00 98.01  ?  187  GLN B O   1 
ATOM   2619  C  CB  . GLN B 2  187  ? -44.486 -83.576  -9.429  1.00 105.32 ?  187  GLN B CB  1 
ATOM   2620  C  CG  . GLN B 2  187  ? -44.576 -84.739  -10.385 1.00 104.75 ?  187  GLN B CG  1 
ATOM   2621  C  CD  . GLN B 2  187  ? -44.120 -86.052  -9.774  1.00 108.51 ?  187  GLN B CD  1 
ATOM   2622  O  OE1 . GLN B 2  187  ? -43.216 -86.086  -8.938  1.00 111.92 ?  187  GLN B OE1 1 
ATOM   2623  N  NE2 . GLN B 2  187  ? -44.751 -87.143  -10.191 1.00 107.13 ?  187  GLN B NE2 1 
ATOM   2624  N  N   . GLY B 2  188  ? -46.476 -81.941  -6.803  1.00 70.50  ?  188  GLY B N   1 
ATOM   2625  C  CA  . GLY B 2  188  ? -46.470 -80.734  -6.004  1.00 74.47  ?  188  GLY B CA  1 
ATOM   2626  C  C   . GLY B 2  188  ? -46.651 -79.453  -6.785  1.00 79.05  ?  188  GLY B C   1 
ATOM   2627  O  O   . GLY B 2  188  ? -46.265 -78.385  -6.291  1.00 77.46  ?  188  GLY B O   1 
ATOM   2628  N  N   . ALA B 2  189  ? -47.226 -79.524  -7.990  1.00 104.88 ?  189  ALA B N   1 
ATOM   2629  C  CA  . ALA B 2  189  ? -47.379 -78.332  -8.820  1.00 100.71 ?  189  ALA B CA  1 
ATOM   2630  C  C   . ALA B 2  189  ? -48.264 -77.294  -8.144  1.00 98.11  ?  189  ALA B C   1 
ATOM   2631  O  O   . ALA B 2  189  ? -48.014 -76.089  -8.254  1.00 94.74  ?  189  ALA B O   1 
ATOM   2632  C  CB  . ALA B 2  189  ? -47.951 -78.711  -10.185 1.00 105.59 ?  189  ALA B CB  1 
ATOM   2633  N  N   . GLY B 2  190  ? -49.310 -77.742  -7.446  1.00 103.76 ?  190  GLY B N   1 
ATOM   2634  C  CA  . GLY B 2  190  ? -50.157 -76.824  -6.707  1.00 107.09 ?  190  GLY B CA  1 
ATOM   2635  C  C   . GLY B 2  190  ? -49.570 -76.342  -5.399  1.00 110.26 ?  190  GLY B C   1 
ATOM   2636  O  O   . GLY B 2  190  ? -50.014 -75.315  -4.876  1.00 104.38 ?  190  GLY B O   1 
ATOM   2637  N  N   . VAL B 2  191  ? -48.581 -77.054  -4.863  1.00 114.16 ?  191  VAL B N   1 
ATOM   2638  C  CA  . VAL B 2  191  ? -47.972 -76.692  -3.588  1.00 96.80  ?  191  VAL B CA  1 
ATOM   2639  C  C   . VAL B 2  191  ? -47.009 -75.533  -3.801  1.00 99.50  ?  191  VAL B C   1 
ATOM   2640  O  O   . VAL B 2  191  ? -46.132 -75.587  -4.672  1.00 104.73 ?  191  VAL B O   1 
ATOM   2641  C  CB  . VAL B 2  191  ? -47.256 -77.900  -2.965  1.00 101.89 ?  191  VAL B CB  1 
ATOM   2642  C  CG1 . VAL B 2  191  ? -46.545 -77.493  -1.685  1.00 95.30  ?  191  VAL B CG1 1 
ATOM   2643  C  CG2 . VAL B 2  191  ? -48.248 -79.014  -2.692  1.00 107.20 ?  191  VAL B CG2 1 
ATOM   2644  N  N   . ARG B 2  192  ? -47.170 -74.481  -3.002  1.00 86.95  ?  192  ARG B N   1 
ATOM   2645  C  CA  . ARG B 2  192  ? -46.319 -73.304  -3.080  1.00 84.89  ?  192  ARG B CA  1 
ATOM   2646  C  C   . ARG B 2  192  ? -45.933 -72.863  -1.676  1.00 89.87  ?  192  ARG B C   1 
ATOM   2647  O  O   . ARG B 2  192  ? -46.742 -72.941  -0.747  1.00 90.11  ?  192  ARG B O   1 
ATOM   2648  C  CB  . ARG B 2  192  ? -47.021 -72.153  -3.811  1.00 75.87  ?  192  ARG B CB  1 
ATOM   2649  C  CG  . ARG B 2  192  ? -47.109 -72.326  -5.317  1.00 93.48  ?  192  ARG B CG  1 
ATOM   2650  C  CD  . ARG B 2  192  ? -45.732 -72.332  -5.955  1.00 93.06  ?  192  ARG B CD  1 
ATOM   2651  N  NE  . ARG B 2  192  ? -45.809 -72.294  -7.411  1.00 98.37  ?  192  ARG B NE  1 
ATOM   2652  C  CZ  . ARG B 2  192  ? -45.932 -73.365  -8.184  1.00 101.89 ?  192  ARG B CZ  1 
ATOM   2653  N  NH1 . ARG B 2  192  ? -45.989 -74.584  -7.672  1.00 99.65  ?  192  ARG B NH1 1 
ATOM   2654  N  NH2 . ARG B 2  192  ? -45.999 -73.209  -9.503  1.00 99.32  ?  192  ARG B NH2 1 
ATOM   2655  N  N   . LEU B 2  193  ? -44.697 -72.401  -1.530  1.00 104.19 ?  193  LEU B N   1 
ATOM   2656  C  CA  . LEU B 2  193  ? -44.197 -71.854  -0.279  1.00 92.06  ?  193  LEU B CA  1 
ATOM   2657  C  C   . LEU B 2  193  ? -44.092 -70.338  -0.383  1.00 92.06  ?  193  LEU B C   1 
ATOM   2658  O  O   . LEU B 2  193  ? -44.189 -69.756  -1.467  1.00 108.01 ?  193  LEU B O   1 
ATOM   2659  C  CB  . LEU B 2  193  ? -42.836 -72.462  0.079   1.00 90.91  ?  193  LEU B CB  1 
ATOM   2660  C  CG  . LEU B 2  193  ? -42.854 -73.694  0.984   1.00 96.33  ?  193  LEU B CG  1 
ATOM   2661  C  CD1 . LEU B 2  193  ? -41.501 -74.387  0.974   1.00 102.37 ?  193  LEU B CD1 1 
ATOM   2662  C  CD2 . LEU B 2  193  ? -43.247 -73.306  2.399   1.00 92.09  ?  193  LEU B CD2 1 
ATOM   2663  N  N   . LEU B 2  194  ? -43.891 -69.696  0.769   1.00 61.42  ?  194  LEU B N   1 
ATOM   2664  C  CA  . LEU B 2  194  ? -43.737 -68.239  0.803   1.00 54.59  ?  194  LEU B CA  1 
ATOM   2665  C  C   . LEU B 2  194  ? -43.123 -67.873  2.159   1.00 61.82  ?  194  LEU B C   1 
ATOM   2666  O  O   . LEU B 2  194  ? -43.841 -67.637  3.131   1.00 65.93  ?  194  LEU B O   1 
ATOM   2667  C  CB  . LEU B 2  194  ? -45.055 -67.525  0.579   1.00 52.84  ?  194  LEU B CB  1 
ATOM   2668  C  CG  . LEU B 2  194  ? -44.986 -66.004  0.426   1.00 47.39  ?  194  LEU B CG  1 
ATOM   2669  C  CD1 . LEU B 2  194  ? -43.994 -65.616  -0.658  1.00 45.41  ?  194  LEU B CD1 1 
ATOM   2670  C  CD2 . LEU B 2  194  ? -46.364 -65.436  0.122   1.00 53.68  ?  194  LEU B CD2 1 
ATOM   2671  N  N   . THR B 2  195  ? -41.798 -67.830  2.200   1.00 80.54  ?  195  THR B N   1 
ATOM   2672  C  CA  . THR B 2  195  ? -41.048 -67.458  3.389   1.00 72.83  ?  195  THR B CA  1 
ATOM   2673  C  C   . THR B 2  195  ? -40.401 -66.092  3.180   1.00 73.27  ?  195  THR B C   1 
ATOM   2674  O  O   . THR B 2  195  ? -40.609 -65.424  2.164   1.00 78.47  ?  195  THR B O   1 
ATOM   2675  C  CB  . THR B 2  195  ? -39.998 -68.521  3.715   1.00 69.26  ?  195  THR B CB  1 
ATOM   2676  O  OG1 . THR B 2  195  ? -38.965 -68.492  2.722   1.00 74.47  ?  195  THR B OG1 1 
ATOM   2677  C  CG2 . THR B 2  195  ? -40.631 -69.903  3.737   1.00 73.84  ?  195  THR B CG2 1 
ATOM   2678  N  N   . THR B 2  196  ? -39.611 -65.675  4.162   1.00 83.03  ?  196  THR B N   1 
ATOM   2679  C  CA  . THR B 2  196  ? -38.854 -64.438  4.080   1.00 82.31  ?  196  THR B CA  1 
ATOM   2680  C  C   . THR B 2  196  ? -37.421 -64.756  3.645   1.00 78.74  ?  196  THR B C   1 
ATOM   2681  O  O   . THR B 2  196  ? -37.157 -65.810  3.054   1.00 77.91  ?  196  THR B O   1 
ATOM   2682  C  CB  . THR B 2  196  ? -38.915 -63.708  5.427   1.00 81.16  ?  196  THR B CB  1 
ATOM   2683  O  OG1 . THR B 2  196  ? -38.240 -64.484  6.425   1.00 80.41  ?  196  THR B OG1 1 
ATOM   2684  C  CG2 . THR B 2  196  ? -40.358 -63.495  5.850   1.00 75.22  ?  196  THR B CG2 1 
ATOM   2685  N  N   . THR B 2  197  ? -36.488 -63.850  3.929   1.00 54.56  ?  197  THR B N   1 
ATOM   2686  C  CA  . THR B 2  197  ? -35.078 -64.080  3.621   1.00 49.61  ?  197  THR B CA  1 
ATOM   2687  C  C   . THR B 2  197  ? -34.561 -65.184  4.533   1.00 43.46  ?  197  THR B C   1 
ATOM   2688  O  O   . THR B 2  197  ? -34.315 -64.963  5.720   1.00 58.84  ?  197  THR B O   1 
ATOM   2689  C  CB  . THR B 2  197  ? -34.272 -62.796  3.792   1.00 45.90  ?  197  THR B CB  1 
ATOM   2690  O  OG1 . THR B 2  197  ? -34.787 -61.785  2.917   1.00 41.78  ?  197  THR B OG1 1 
ATOM   2691  C  CG2 . THR B 2  197  ? -32.804 -63.039  3.465   1.00 37.92  ?  197  THR B CG2 1 
ATOM   2692  N  N   . ILE B 2  198  ? -34.402 -66.383  3.982   1.00 53.54  ?  198  ILE B N   1 
ATOM   2693  C  CA  . ILE B 2  198  ? -34.024 -67.558  4.758   1.00 57.41  ?  198  ILE B CA  1 
ATOM   2694  C  C   . ILE B 2  198  ? -32.510 -67.709  4.736   1.00 59.79  ?  198  ILE B C   1 
ATOM   2695  O  O   . ILE B 2  198  ? -31.894 -67.751  3.666   1.00 74.15  ?  198  ILE B O   1 
ATOM   2696  C  CB  . ILE B 2  198  ? -34.711 -68.822  4.213   1.00 57.17  ?  198  ILE B CB  1 
ATOM   2697  C  CG1 . ILE B 2  198  ? -36.229 -68.709  4.348   1.00 54.80  ?  198  ILE B CG1 1 
ATOM   2698  C  CG2 . ILE B 2  198  ? -34.200 -70.061  4.930   1.00 61.89  ?  198  ILE B CG2 1 
ATOM   2699  C  CD1 . ILE B 2  198  ? -36.703 -68.512  5.769   1.00 60.94  ?  198  ILE B CD1 1 
ATOM   2700  N  N   . THR B 2  199  ? -31.907 -67.781  5.924   1.00 63.97  ?  199  THR B N   1 
ATOM   2701  C  CA  . THR B 2  199  ? -30.485 -68.056  6.050   1.00 70.63  ?  199  THR B CA  1 
ATOM   2702  C  C   . THR B 2  199  ? -30.191 -69.244  6.956   1.00 75.29  ?  199  THR B C   1 
ATOM   2703  O  O   . THR B 2  199  ? -29.027 -69.644  7.063   1.00 72.02  ?  199  THR B O   1 
ATOM   2704  C  CB  . THR B 2  199  ? -29.731 -66.824  6.577   1.00 70.88  ?  199  THR B CB  1 
ATOM   2705  O  OG1 . THR B 2  199  ? -30.131 -66.554  7.927   1.00 71.11  ?  199  THR B OG1 1 
ATOM   2706  C  CG2 . THR B 2  199  ? -30.021 -65.604  5.709   1.00 74.09  ?  199  THR B CG2 1 
ATOM   2707  N  N   . SER B 2  200  ? -31.201 -69.816  7.599   1.00 85.76  ?  200  SER B N   1 
ATOM   2708  C  CA  . SER B 2  200  ? -30.993 -70.948  8.495   1.00 83.54  ?  200  SER B CA  1 
ATOM   2709  C  C   . SER B 2  200  ? -30.602 -72.185  7.698   1.00 90.80  ?  200  SER B C   1 
ATOM   2710  O  O   . SER B 2  200  ? -31.351 -72.595  6.802   1.00 97.13  ?  200  SER B O   1 
ATOM   2711  C  CB  . SER B 2  200  ? -32.258 -71.214  9.304   1.00 84.71  ?  200  SER B CB  1 
ATOM   2712  O  OG  . SER B 2  200  ? -32.194 -72.478  9.938   1.00 90.60  ?  200  SER B OG  1 
ATOM   2713  N  N   . PRO B 2  201  ? -29.451 -72.801  7.974   1.00 81.93  ?  201  PRO B N   1 
ATOM   2714  C  CA  . PRO B 2  201  ? -29.068 -74.010  7.227   1.00 81.77  ?  201  PRO B CA  1 
ATOM   2715  C  C   . PRO B 2  201  ? -30.021 -75.177  7.422   1.00 83.57  ?  201  PRO B C   1 
ATOM   2716  O  O   . PRO B 2  201  ? -30.236 -75.956  6.484   1.00 93.74  ?  201  PRO B O   1 
ATOM   2717  C  CB  . PRO B 2  201  ? -27.670 -74.329  7.777   1.00 80.48  ?  201  PRO B CB  1 
ATOM   2718  C  CG  . PRO B 2  201  ? -27.178 -73.042  8.348   1.00 78.53  ?  201  PRO B CG  1 
ATOM   2719  C  CD  . PRO B 2  201  ? -28.391 -72.363  8.897   1.00 80.03  ?  201  PRO B CD  1 
ATOM   2720  N  N   . SER B 2  202  ? -30.596 -75.327  8.617   1.00 69.08  ?  202  SER B N   1 
ATOM   2721  C  CA  . SER B 2  202  ? -31.519 -76.432  8.862   1.00 75.55  ?  202  SER B CA  1 
ATOM   2722  C  C   . SER B 2  202  ? -32.799 -76.268  8.053   1.00 81.75  ?  202  SER B C   1 
ATOM   2723  O  O   . SER B 2  202  ? -33.271 -77.219  7.420   1.00 93.45  ?  202  SER B O   1 
ATOM   2724  C  CB  . SER B 2  202  ? -31.836 -76.535  10.353  1.00 79.73  ?  202  SER B CB  1 
ATOM   2725  O  OG  . SER B 2  202  ? -30.654 -76.669  11.121  1.00 87.02  ?  202  SER B OG  1 
ATOM   2726  N  N   . LEU B 2  203  ? -33.378 -75.065  8.066   1.00 81.66  ?  203  LEU B N   1 
ATOM   2727  C  CA  . LEU B 2  203  ? -34.593 -74.824  7.295   1.00 85.04  ?  203  LEU B CA  1 
ATOM   2728  C  C   . LEU B 2  203  ? -34.327 -74.921  5.798   1.00 92.09  ?  203  LEU B C   1 
ATOM   2729  O  O   . LEU B 2  203  ? -35.160 -75.443  5.047   1.00 95.07  ?  203  LEU B O   1 
ATOM   2730  C  CB  . LEU B 2  203  ? -35.177 -73.456  7.648   1.00 75.56  ?  203  LEU B CB  1 
ATOM   2731  C  CG  . LEU B 2  203  ? -36.576 -73.168  7.100   1.00 70.31  ?  203  LEU B CG  1 
ATOM   2732  C  CD1 . LEU B 2  203  ? -37.553 -74.245  7.540   1.00 68.65  ?  203  LEU B CD1 1 
ATOM   2733  C  CD2 . LEU B 2  203  ? -37.054 -71.792  7.535   1.00 69.72  ?  203  LEU B CD2 1 
ATOM   2734  N  N   . ALA B 2  204  ? -33.173 -74.425  5.346   1.00 72.82  ?  204  ALA B N   1 
ATOM   2735  C  CA  . ALA B 2  204  ? -32.840 -74.500  3.928   1.00 72.70  ?  204  ALA B CA  1 
ATOM   2736  C  C   . ALA B 2  204  ? -32.646 -75.943  3.481   1.00 80.30  ?  204  ALA B C   1 
ATOM   2737  O  O   . ALA B 2  204  ? -33.029 -76.310  2.364   1.00 87.59  ?  204  ALA B O   1 
ATOM   2738  C  CB  . ALA B 2  204  ? -31.587 -73.675  3.637   1.00 69.20  ?  204  ALA B CB  1 
ATOM   2739  N  N   . ALA B 2  205  ? -32.054 -76.777  4.339   1.00 74.66  ?  205  ALA B N   1 
ATOM   2740  C  CA  . ALA B 2  205  ? -31.858 -78.179  3.986   1.00 77.19  ?  205  ALA B CA  1 
ATOM   2741  C  C   . ALA B 2  205  ? -33.181 -78.933  3.964   1.00 78.52  ?  205  ALA B C   1 
ATOM   2742  O  O   . ALA B 2  205  ? -33.385 -79.815  3.121   1.00 93.55  ?  205  ALA B O   1 
ATOM   2743  C  CB  . ALA B 2  205  ? -30.881 -78.835  4.961   1.00 67.97  ?  205  ALA B CB  1 
ATOM   2744  N  N   . GLN B 2  206  ? -34.091 -78.602  4.882   1.00 85.70  ?  206  GLN B N   1 
ATOM   2745  C  CA  . GLN B 2  206  ? -35.391 -79.263  4.903   1.00 92.06  ?  206  GLN B CA  1 
ATOM   2746  C  C   . GLN B 2  206  ? -36.273 -78.803  3.751   1.00 92.76  ?  206  GLN B C   1 
ATOM   2747  O  O   . GLN B 2  206  ? -37.059 -79.596  3.220   1.00 93.07  ?  206  GLN B O   1 
ATOM   2748  C  CB  . GLN B 2  206  ? -36.084 -79.011  6.241   1.00 96.73  ?  206  GLN B CB  1 
ATOM   2749  C  CG  . GLN B 2  206  ? -35.538 -79.851  7.383   1.00 90.88  ?  206  GLN B CG  1 
ATOM   2750  C  CD  . GLN B 2  206  ? -36.395 -79.768  8.628   1.00 93.24  ?  206  GLN B CD  1 
ATOM   2751  O  OE1 . GLN B 2  206  ? -37.344 -78.988  8.690   1.00 90.89  ?  206  GLN B OE1 1 
ATOM   2752  N  NE2 . GLN B 2  206  ? -36.063 -80.573  9.631   1.00 97.76  ?  206  GLN B NE2 1 
ATOM   2753  N  N   . ILE B 2  207  ? -36.162 -77.534  3.353   1.00 57.27  ?  207  ILE B N   1 
ATOM   2754  C  CA  . ILE B 2  207  ? -36.902 -77.052  2.192   1.00 54.99  ?  207  ILE B CA  1 
ATOM   2755  C  C   . ILE B 2  207  ? -36.379 -77.705  0.918   1.00 53.15  ?  207  ILE B C   1 
ATOM   2756  O  O   . ILE B 2  207  ? -37.157 -78.079  0.032   1.00 57.67  ?  207  ILE B O   1 
ATOM   2757  C  CB  . ILE B 2  207  ? -36.839 -75.514  2.118   1.00 46.10  ?  207  ILE B CB  1 
ATOM   2758  C  CG1 . ILE B 2  207  ? -37.712 -74.896  3.210   1.00 42.27  ?  207  ILE B CG1 1 
ATOM   2759  C  CG2 . ILE B 2  207  ? -37.272 -75.012  0.751   1.00 47.99  ?  207  ILE B CG2 1 
ATOM   2760  C  CD1 . ILE B 2  207  ? -37.568 -73.400  3.335   1.00 39.37  ?  207  ILE B CD1 1 
ATOM   2761  N  N   . GLU B 2  208  ? -35.057 -77.864  0.808   1.00 103.84 ?  208  GLU B N   1 
ATOM   2762  C  CA  . GLU B 2  208  ? -34.496 -78.542  -0.357  1.00 113.31 ?  208  GLU B CA  1 
ATOM   2763  C  C   . GLU B 2  208  ? -34.923 -80.003  -0.399  1.00 114.84 ?  208  GLU B C   1 
ATOM   2764  O  O   . GLU B 2  208  ? -35.209 -80.542  -1.475  1.00 125.25 ?  208  GLU B O   1 
ATOM   2765  C  CB  . GLU B 2  208  ? -32.972 -78.431  -0.353  1.00 119.58 ?  208  GLU B CB  1 
ATOM   2766  C  CG  . GLU B 2  208  ? -32.321 -78.873  -1.655  1.00 126.07 ?  208  GLU B CG  1 
ATOM   2767  C  CD  . GLU B 2  208  ? -30.814 -78.986  -1.544  1.00 152.71 ?  208  GLU B CD  1 
ATOM   2768  O  OE1 . GLU B 2  208  ? -30.297 -78.966  -0.407  1.00 159.41 ?  208  GLU B OE1 1 
ATOM   2769  O  OE2 . GLU B 2  208  ? -30.147 -79.099  -2.594  1.00 160.62 -1 208  GLU B OE2 1 
ATOM   2770  N  N   . GLN B 2  209  ? -34.972 -80.662  0.762   1.00 83.06  ?  209  GLN B N   1 
ATOM   2771  C  CA  . GLN B 2  209  ? -35.444 -82.042  0.808   1.00 87.29  ?  209  GLN B CA  1 
ATOM   2772  C  C   . GLN B 2  209  ? -36.913 -82.132  0.418   1.00 86.82  ?  209  GLN B C   1 
ATOM   2773  O  O   . GLN B 2  209  ? -37.323 -83.065  -0.283  1.00 90.55  ?  209  GLN B O   1 
ATOM   2774  C  CB  . GLN B 2  209  ? -35.223 -82.627  2.203   1.00 93.19  ?  209  GLN B CB  1 
ATOM   2775  C  CG  . GLN B 2  209  ? -35.556 -84.105  2.312   1.00 98.16  ?  209  GLN B CG  1 
ATOM   2776  C  CD  . GLN B 2  209  ? -35.313 -84.657  3.701   1.00 103.82 ?  209  GLN B CD  1 
ATOM   2777  O  OE1 . GLN B 2  209  ? -34.797 -83.963  4.578   1.00 91.91  ?  209  GLN B OE1 1 
ATOM   2778  N  NE2 . GLN B 2  209  ? -35.686 -85.915  3.911   1.00 114.05 ?  209  GLN B NE2 1 
ATOM   2779  N  N   . PHE B 2  210  ? -37.722 -81.168  0.865   1.00 68.59  ?  210  PHE B N   1 
ATOM   2780  C  CA  . PHE B 2  210  ? -39.122 -81.129  0.459   1.00 71.37  ?  210  PHE B CA  1 
ATOM   2781  C  C   . PHE B 2  210  ? -39.258 -80.879  -1.037  1.00 75.34  ?  210  PHE B C   1 
ATOM   2782  O  O   . PHE B 2  210  ? -40.182 -81.401  -1.671  1.00 80.46  ?  210  PHE B O   1 
ATOM   2783  C  CB  . PHE B 2  210  ? -39.866 -80.054  1.252   1.00 65.30  ?  210  PHE B CB  1 
ATOM   2784  C  CG  . PHE B 2  210  ? -41.311 -79.906  0.871   1.00 65.38  ?  210  PHE B CG  1 
ATOM   2785  C  CD1 . PHE B 2  210  ? -42.236 -80.877  1.217   1.00 70.01  ?  210  PHE B CD1 1 
ATOM   2786  C  CD2 . PHE B 2  210  ? -41.744 -78.797  0.164   1.00 65.99  ?  210  PHE B CD2 1 
ATOM   2787  C  CE1 . PHE B 2  210  ? -43.567 -80.741  0.869   1.00 68.89  ?  210  PHE B CE1 1 
ATOM   2788  C  CE2 . PHE B 2  210  ? -43.072 -78.657  -0.189  1.00 66.34  ?  210  PHE B CE2 1 
ATOM   2789  C  CZ  . PHE B 2  210  ? -43.984 -79.631  0.164   1.00 69.31  ?  210  PHE B CZ  1 
ATOM   2790  N  N   . LEU B 2  211  ? -38.348 -80.093  -1.618  1.00 86.30  ?  211  LEU B N   1 
ATOM   2791  C  CA  . LEU B 2  211  ? -38.382 -79.858  -3.058  1.00 87.53  ?  211  LEU B CA  1 
ATOM   2792  C  C   . LEU B 2  211  ? -37.950 -81.094  -3.838  1.00 89.60  ?  211  LEU B C   1 
ATOM   2793  O  O   . LEU B 2  211  ? -38.460 -81.339  -4.938  1.00 92.80  ?  211  LEU B O   1 
ATOM   2794  C  CB  . LEU B 2  211  ? -37.500 -78.662  -3.419  1.00 82.24  ?  211  LEU B CB  1 
ATOM   2795  C  CG  . LEU B 2  211  ? -38.218 -77.336  -3.689  1.00 71.78  ?  211  LEU B CG  1 
ATOM   2796  C  CD1 . LEU B 2  211  ? -39.136 -76.964  -2.535  1.00 64.80  ?  211  LEU B CD1 1 
ATOM   2797  C  CD2 . LEU B 2  211  ? -37.215 -76.226  -3.959  1.00 71.83  ?  211  LEU B CD2 1 
ATOM   2798  N  N   . GLN B 2  212  ? -37.014 -81.879  -3.298  1.00 142.88 ?  212  GLN B N   1 
ATOM   2799  C  CA  . GLN B 2  212  ? -36.664 -83.143  -3.939  1.00 145.79 ?  212  GLN B CA  1 
ATOM   2800  C  C   . GLN B 2  212  ? -37.816 -84.137  -3.875  1.00 144.85 ?  212  GLN B C   1 
ATOM   2801  O  O   . GLN B 2  212  ? -37.996 -84.936  -4.802  1.00 148.39 ?  212  GLN B O   1 
ATOM   2802  C  CB  . GLN B 2  212  ? -35.410 -83.738  -3.296  1.00 144.05 ?  212  GLN B CB  1 
ATOM   2803  C  CG  . GLN B 2  212  ? -34.176 -82.853  -3.381  1.00 150.73 ?  212  GLN B CG  1 
ATOM   2804  C  CD  . GLN B 2  212  ? -33.406 -83.051  -4.672  1.00 157.12 ?  212  GLN B CD  1 
ATOM   2805  O  OE1 . GLN B 2  212  ? -33.256 -84.174  -5.152  1.00 162.29 ?  212  GLN B OE1 1 
ATOM   2806  N  NE2 . GLN B 2  212  ? -32.911 -81.957  -5.241  1.00 155.21 ?  212  GLN B NE2 1 
ATOM   2807  N  N   . ALA B 2  213  ? -38.605 -84.104  -2.798  1.00 119.72 ?  213  ALA B N   1 
ATOM   2808  C  CA  . ALA B 2  213  ? -39.766 -84.983  -2.702  1.00 126.15 ?  213  ALA B CA  1 
ATOM   2809  C  C   . ALA B 2  213  ? -40.894 -84.528  -3.620  1.00 123.64 ?  213  ALA B C   1 
ATOM   2810  O  O   . ALA B 2  213  ? -41.627 -85.363  -4.161  1.00 125.95 ?  213  ALA B O   1 
ATOM   2811  C  CB  . ALA B 2  213  ? -40.252 -85.048  -1.254  1.00 121.04 ?  213  ALA B CB  1 
ATOM   2812  N  N   . TYR B 2  214  ? -41.050 -83.217  -3.808  1.00 103.54 ?  214  TYR B N   1 
ATOM   2813  C  CA  . TYR B 2  214  ? -42.087 -82.645  -4.665  1.00 106.05 ?  214  TYR B CA  1 
ATOM   2814  C  C   . TYR B 2  214  ? -41.400 -81.785  -5.717  1.00 109.79 ?  214  TYR B C   1 
ATOM   2815  O  O   . TYR B 2  214  ? -41.157 -80.588  -5.492  1.00 101.13 ?  214  TYR B O   1 
ATOM   2816  C  CB  . TYR B 2  214  ? -43.092 -81.830  -3.852  1.00 98.00  ?  214  TYR B CB  1 
ATOM   2817  C  CG  . TYR B 2  214  ? -44.040 -82.673  -3.028  1.00 104.12 ?  214  TYR B CG  1 
ATOM   2818  C  CD1 . TYR B 2  214  ? -45.226 -83.159  -3.568  1.00 121.15 ?  214  TYR B CD1 1 
ATOM   2819  C  CD2 . TYR B 2  214  ? -43.745 -82.989  -1.709  1.00 98.07  ?  214  TYR B CD2 1 
ATOM   2820  C  CE1 . TYR B 2  214  ? -46.090 -83.935  -2.812  1.00 123.97 ?  214  TYR B CE1 1 
ATOM   2821  C  CE2 . TYR B 2  214  ? -44.600 -83.761  -0.947  1.00 97.91  ?  214  TYR B CE2 1 
ATOM   2822  C  CZ  . TYR B 2  214  ? -45.771 -84.232  -1.503  1.00 111.47 ?  214  TYR B CZ  1 
ATOM   2823  O  OH  . TYR B 2  214  ? -46.627 -85.002  -0.750  1.00 111.49 ?  214  TYR B OH  1 
ATOM   2824  N  N   . PRO B 2  215  ? -41.071 -82.351  -6.884  1.00 95.05  ?  215  PRO B N   1 
ATOM   2825  C  CA  . PRO B 2  215  ? -40.254 -81.600  -7.856  1.00 90.78  ?  215  PRO B CA  1 
ATOM   2826  C  C   . PRO B 2  215  ? -40.906 -80.330  -8.376  1.00 87.23  ?  215  PRO B C   1 
ATOM   2827  O  O   . PRO B 2  215  ? -40.212 -79.323  -8.565  1.00 89.27  ?  215  PRO B O   1 
ATOM   2828  C  CB  . PRO B 2  215  ? -40.029 -82.622  -8.980  1.00 94.76  ?  215  PRO B CB  1 
ATOM   2829  C  CG  . PRO B 2  215  ? -40.203 -83.954  -8.326  1.00 91.33  ?  215  PRO B CG  1 
ATOM   2830  C  CD  . PRO B 2  215  ? -41.265 -83.754  -7.287  1.00 90.58  ?  215  PRO B CD  1 
ATOM   2831  N  N   . GLN B 2  216  ? -42.214 -80.340  -8.616  1.00 124.79 ?  216  GLN B N   1 
ATOM   2832  C  CA  . GLN B 2  216  ? -42.886 -79.184  -9.196  1.00 131.61 ?  216  GLN B CA  1 
ATOM   2833  C  C   . GLN B 2  216  ? -43.232 -78.109  -8.170  1.00 127.94 ?  216  GLN B C   1 
ATOM   2834  O  O   . GLN B 2  216  ? -43.959 -77.169  -8.509  1.00 127.36 ?  216  GLN B O   1 
ATOM   2835  C  CB  . GLN B 2  216  ? -44.156 -79.620  -9.932  1.00 137.36 ?  216  GLN B CB  1 
ATOM   2836  C  CG  . GLN B 2  216  ? -43.920 -80.609  -11.061 1.00 133.94 ?  216  GLN B CG  1 
ATOM   2837  C  CD  . GLN B 2  216  ? -43.119 -80.022  -12.204 1.00 143.26 ?  216  GLN B CD  1 
ATOM   2838  O  OE1 . GLN B 2  216  ? -43.192 -78.824  -12.479 1.00 150.71 ?  216  GLN B OE1 1 
ATOM   2839  N  NE2 . GLN B 2  216  ? -42.349 -80.866  -12.880 1.00 141.24 ?  216  GLN B NE2 1 
ATOM   2840  N  N   . ALA B 2  217  ? -42.739 -78.217  -6.940  1.00 110.61 ?  217  ALA B N   1 
ATOM   2841  C  CA  . ALA B 2  217  ? -42.989 -77.189  -5.944  1.00 103.26 ?  217  ALA B CA  1 
ATOM   2842  C  C   . ALA B 2  217  ? -42.003 -76.034  -6.109  1.00 100.77 ?  217  ALA B C   1 
ATOM   2843  O  O   . ALA B 2  217  ? -40.908 -76.190  -6.655  1.00 109.45 ?  217  ALA B O   1 
ATOM   2844  C  CB  . ALA B 2  217  ? -42.890 -77.769  -4.533  1.00 101.32 ?  217  ALA B CB  1 
ATOM   2845  N  N   . ARG B 2  218  ? -42.409 -74.860  -5.627  1.00 89.08  ?  218  ARG B N   1 
ATOM   2846  C  CA  . ARG B 2  218  ? -41.593 -73.658  -5.716  1.00 95.69  ?  218  ARG B CA  1 
ATOM   2847  C  C   . ARG B 2  218  ? -41.449 -73.024  -4.340  1.00 85.95  ?  218  ARG B C   1 
ATOM   2848  O  O   . ARG B 2  218  ? -42.363 -73.078  -3.512  1.00 82.59  ?  218  ARG B O   1 
ATOM   2849  C  CB  . ARG B 2  218  ? -42.190 -72.643  -6.702  1.00 96.15  ?  218  ARG B CB  1 
ATOM   2850  C  CG  . ARG B 2  218  ? -42.413 -73.196  -8.101  1.00 92.15  ?  218  ARG B CG  1 
ATOM   2851  C  CD  . ARG B 2  218  ? -41.166 -73.051  -8.960  1.00 94.45  ?  218  ARG B CD  1 
ATOM   2852  N  NE  . ARG B 2  218  ? -41.356 -73.601  -10.297 1.00 117.53 ?  218  ARG B NE  1 
ATOM   2853  C  CZ  . ARG B 2  218  ? -40.653 -74.606  -10.803 1.00 110.46 ?  218  ARG B CZ  1 
ATOM   2854  N  NH1 . ARG B 2  218  ? -39.695 -75.199  -10.108 1.00 106.18 ?  218  ARG B NH1 1 
ATOM   2855  N  NH2 . ARG B 2  218  ? -40.918 -75.027  -12.036 1.00 99.44  ?  218  ARG B NH2 1 
ATOM   2856  N  N   . TRP B 2  219  ? -40.285 -72.414  -4.108  1.00 97.06  ?  219  TRP B N   1 
ATOM   2857  C  CA  . TRP B 2  219  ? -39.985 -71.827  -2.805  1.00 96.57  ?  219  TRP B CA  1 
ATOM   2858  C  C   . TRP B 2  219  ? -40.583 -70.430  -2.671  1.00 98.66  ?  219  TRP B C   1 
ATOM   2859  O  O   . TRP B 2  219  ? -41.429 -70.190  -1.803  1.00 101.70 ?  219  TRP B O   1 
ATOM   2860  C  CB  . TRP B 2  219  ? -38.469 -71.796  -2.587  1.00 94.28  ?  219  TRP B CB  1 
ATOM   2861  C  CG  . TRP B 2  219  ? -38.054 -71.501  -1.176  1.00 88.17  ?  219  TRP B CG  1 
ATOM   2862  C  CD1 . TRP B 2  219  ? -38.871 -71.227  -0.116  1.00 84.51  ?  219  TRP B CD1 1 
ATOM   2863  C  CD2 . TRP B 2  219  ? -36.715 -71.456  -0.671  1.00 84.03  ?  219  TRP B CD2 1 
ATOM   2864  N  NE1 . TRP B 2  219  ? -38.122 -71.009  1.014   1.00 86.98  ?  219  TRP B NE1 1 
ATOM   2865  C  CE2 . TRP B 2  219  ? -36.795 -71.145  0.701   1.00 83.51  ?  219  TRP B CE2 1 
ATOM   2866  C  CE3 . TRP B 2  219  ? -35.455 -71.647  -1.246  1.00 82.87  ?  219  TRP B CE3 1 
ATOM   2867  C  CZ2 . TRP B 2  219  ? -35.665 -71.022  1.505   1.00 87.48  ?  219  TRP B CZ2 1 
ATOM   2868  C  CZ3 . TRP B 2  219  ? -34.334 -71.524  -0.446  1.00 87.01  ?  219  TRP B CZ3 1 
ATOM   2869  C  CH2 . TRP B 2  219  ? -34.446 -71.215  0.915   1.00 90.32  ?  219  TRP B CH2 1 
ATOM   2870  N  N   . TYR B 2  220  ? -40.144 -69.494  -3.518  1.00 76.63  ?  220  TYR B N   1 
ATOM   2871  C  CA  . TYR B 2  220  ? -40.647 -68.122  -3.531  1.00 73.01  ?  220  TYR B CA  1 
ATOM   2872  C  C   . TYR B 2  220  ? -40.506 -67.442  -2.172  1.00 68.37  ?  220  TYR B C   1 
ATOM   2873  O  O   . TYR B 2  220  ? -41.429 -67.484  -1.353  1.00 67.11  ?  220  TYR B O   1 
ATOM   2874  C  CB  . TYR B 2  220  ? -42.114 -68.084  -3.976  1.00 70.35  ?  220  TYR B CB  1 
ATOM   2875  C  CG  . TYR B 2  220  ? -42.346 -68.487  -5.415  1.00 71.96  ?  220  TYR B CG  1 
ATOM   2876  C  CD1 . TYR B 2  220  ? -41.360 -68.314  -6.376  1.00 76.67  ?  220  TYR B CD1 1 
ATOM   2877  C  CD2 . TYR B 2  220  ? -43.559 -69.036  -5.813  1.00 78.89  ?  220  TYR B CD2 1 
ATOM   2878  C  CE1 . TYR B 2  220  ? -41.572 -68.682  -7.693  1.00 88.67  ?  220  TYR B CE1 1 
ATOM   2879  C  CE2 . TYR B 2  220  ? -43.781 -69.406  -7.126  1.00 87.55  ?  220  TYR B CE2 1 
ATOM   2880  C  CZ  . TYR B 2  220  ? -42.784 -69.227  -8.062  1.00 93.84  ?  220  TYR B CZ  1 
ATOM   2881  O  OH  . TYR B 2  220  ? -42.999 -69.594  -9.371  1.00 98.24  ?  220  TYR B OH  1 
ATOM   2882  N  N   . GLN B 2  221  ? -39.366 -66.806  -1.927  1.00 74.30  ?  221  GLN B N   1 
ATOM   2883  C  CA  . GLN B 2  221  ? -39.140 -66.055  -0.700  1.00 70.09  ?  221  GLN B CA  1 
ATOM   2884  C  C   . GLN B 2  221  ? -39.243 -64.561  -0.979  1.00 65.17  ?  221  GLN B C   1 
ATOM   2885  O  O   . GLN B 2  221  ? -38.784 -64.080  -2.019  1.00 64.69  ?  221  GLN B O   1 
ATOM   2886  C  CB  . GLN B 2  221  ? -37.773 -66.384  -0.100  1.00 68.05  ?  221  GLN B CB  1 
ATOM   2887  C  CG  . GLN B 2  221  ? -36.664 -66.508  -1.128  1.00 79.59  ?  221  GLN B CG  1 
ATOM   2888  C  CD  . GLN B 2  221  ? -35.365 -66.998  -0.525  1.00 82.32  ?  221  GLN B CD  1 
ATOM   2889  O  OE1 . GLN B 2  221  ? -34.470 -67.452  -1.237  1.00 88.27  ?  221  GLN B OE1 1 
ATOM   2890  N  NE2 . GLN B 2  221  ? -35.250 -66.900  0.794   1.00 59.83  ?  221  GLN B NE2 1 
ATOM   2891  N  N   . TYR B 2  222  ? -39.851 -63.831  -0.045  1.00 69.45  ?  222  TYR B N   1 
ATOM   2892  C  CA  . TYR B 2  222  ? -40.020 -62.393  -0.200  1.00 67.57  ?  222  TYR B CA  1 
ATOM   2893  C  C   . TYR B 2  222  ? -40.204 -61.747  1.166   1.00 72.19  ?  222  TYR B C   1 
ATOM   2894  O  O   . TYR B 2  222  ? -40.776 -62.345  2.081   1.00 77.62  ?  222  TYR B O   1 
ATOM   2895  C  CB  . TYR B 2  222  ? -41.212 -62.057  -1.107  1.00 70.08  ?  222  TYR B CB  1 
ATOM   2896  C  CG  . TYR B 2  222  ? -41.574 -60.586  -1.105  1.00 68.83  ?  222  TYR B CG  1 
ATOM   2897  C  CD1 . TYR B 2  222  ? -40.913 -59.687  -1.930  1.00 73.32  ?  222  TYR B CD1 1 
ATOM   2898  C  CD2 . TYR B 2  222  ? -42.577 -60.097  -0.275  1.00 68.79  ?  222  TYR B CD2 1 
ATOM   2899  C  CE1 . TYR B 2  222  ? -41.237 -58.341  -1.927  1.00 72.28  ?  222  TYR B CE1 1 
ATOM   2900  C  CE2 . TYR B 2  222  ? -42.907 -58.755  -0.264  1.00 66.71  ?  222  TYR B CE2 1 
ATOM   2901  C  CZ  . TYR B 2  222  ? -42.235 -57.882  -1.094  1.00 69.97  ?  222  TYR B CZ  1 
ATOM   2902  O  OH  . TYR B 2  222  ? -42.563 -56.546  -1.088  1.00 72.82  ?  222  TYR B OH  1 
ATOM   2903  N  N   . GLU B 2  223  ? -39.710 -60.518  1.285   1.00 77.49  ?  223  GLU B N   1 
ATOM   2904  C  CA  . GLU B 2  223  ? -39.948 -59.661  2.436   1.00 72.78  ?  223  GLU B CA  1 
ATOM   2905  C  C   . GLU B 2  223  ? -39.823 -58.221  1.967   1.00 78.98  ?  223  GLU B C   1 
ATOM   2906  O  O   . GLU B 2  223  ? -39.070 -57.945  1.025   1.00 77.28  ?  223  GLU B O   1 
ATOM   2907  C  CB  . GLU B 2  223  ? -38.965 -59.946  3.582   1.00 76.77  ?  223  GLU B CB  1 
ATOM   2908  C  CG  . GLU B 2  223  ? -37.516 -59.606  3.279   1.00 79.93  ?  223  GLU B CG  1 
ATOM   2909  C  CD  . GLU B 2  223  ? -36.633 -59.696  4.511   1.00 85.92  ?  223  GLU B CD  1 
ATOM   2910  O  OE1 . GLU B 2  223  ? -37.155 -60.031  5.596   1.00 76.63  ?  223  GLU B OE1 1 
ATOM   2911  O  OE2 . GLU B 2  223  ? -35.417 -59.436  4.394   1.00 97.21  -1 223  GLU B OE2 1 
ATOM   2912  N  N   . PRO B 2  224  ? -40.553 -57.286  2.583   1.00 75.68  ?  224  PRO B N   1 
ATOM   2913  C  CA  . PRO B 2  224  ? -40.558 -55.907  2.059   1.00 68.18  ?  224  PRO B CA  1 
ATOM   2914  C  C   . PRO B 2  224  ? -39.202 -55.216  2.105   1.00 68.82  ?  224  PRO B C   1 
ATOM   2915  O  O   . PRO B 2  224  ? -38.907 -54.400  1.223   1.00 68.07  ?  224  PRO B O   1 
ATOM   2916  C  CB  . PRO B 2  224  ? -41.585 -55.198  2.954   1.00 63.91  ?  224  PRO B CB  1 
ATOM   2917  C  CG  . PRO B 2  224  ? -41.652 -56.025  4.194   1.00 68.20  ?  224  PRO B CG  1 
ATOM   2918  C  CD  . PRO B 2  224  ? -41.439 -57.438  3.749   1.00 75.55  ?  224  PRO B CD  1 
ATOM   2919  N  N   . ILE B 2  225  ? -38.375 -55.505  3.102   1.00 73.17  ?  225  ILE B N   1 
ATOM   2920  C  CA  . ILE B 2  225  ? -37.048 -54.910  3.216   1.00 71.10  ?  225  ILE B CA  1 
ATOM   2921  C  C   . ILE B 2  225  ? -36.075 -56.017  2.833   1.00 74.24  ?  225  ILE B C   1 
ATOM   2922  O  O   . ILE B 2  225  ? -35.666 -56.830  3.662   1.00 79.62  ?  225  ILE B O   1 
ATOM   2923  C  CB  . ILE B 2  225  ? -36.794 -54.363  4.622   1.00 63.23  ?  225  ILE B CB  1 
ATOM   2924  C  CG1 . ILE B 2  225  ? -37.880 -53.344  5.007   1.00 67.11  ?  225  ILE B CG1 1 
ATOM   2925  C  CG2 . ILE B 2  225  ? -35.419 -53.704  4.729   1.00 56.91  ?  225  ILE B CG2 1 
ATOM   2926  C  CD1 . ILE B 2  225  ? -37.939 -52.120  4.114   1.00 69.64  ?  225  ILE B CD1 1 
ATOM   2927  N  N   . ASN B 2  226  ? -35.712 -56.054  1.564   1.00 72.27  ?  226  ASN B N   1 
ATOM   2928  C  CA  . ASN B 2  226  ? -34.852 -57.093  1.017   1.00 73.10  ?  226  ASN B CA  1 
ATOM   2929  C  C   . ASN B 2  226  ? -33.618 -56.454  0.395   1.00 71.84  ?  226  ASN B C   1 
ATOM   2930  O  O   . ASN B 2  226  ? -33.415 -55.240  0.467   1.00 73.77  ?  226  ASN B O   1 
ATOM   2931  C  CB  . ASN B 2  226  ? -35.610 -57.952  0.001   1.00 71.62  ?  226  ASN B CB  1 
ATOM   2932  C  CG  . ASN B 2  226  ? -36.477 -57.124  -0.933  1.00 72.86  ?  226  ASN B CG  1 
ATOM   2933  O  OD1 . ASN B 2  226  ? -36.292 -55.916  -1.067  1.00 90.10  ?  226  ASN B OD1 1 
ATOM   2934  N  ND2 . ASN B 2  226  ? -37.430 -57.779  -1.590  1.00 69.55  ?  226  ASN B ND2 1 
ATOM   2935  N  N   . ARG B 2  227  ? -32.791 -57.298  -0.217  1.00 79.79  ?  227  ARG B N   1 
ATOM   2936  C  CA  . ARG B 2  227  ? -31.565 -56.856  -0.868  1.00 88.52  ?  227  ARG B CA  1 
ATOM   2937  C  C   . ARG B 2  227  ? -31.540 -57.292  -2.329  1.00 95.94  ?  227  ARG B C   1 
ATOM   2938  O  O   . ARG B 2  227  ? -30.530 -57.820  -2.804  1.00 91.33  ?  227  ARG B O   1 
ATOM   2939  C  CB  . ARG B 2  227  ? -30.341 -57.410  -0.134  1.00 84.85  ?  227  ARG B CB  1 
ATOM   2940  C  CG  . ARG B 2  227  ? -30.435 -57.353  1.381   1.00 79.68  ?  227  ARG B CG  1 
ATOM   2941  C  CD  . ARG B 2  227  ? -29.052 -57.467  2.009   1.00 75.48  ?  227  ARG B CD  1 
ATOM   2942  N  NE  . ARG B 2  227  ? -28.235 -56.288  1.746   1.00 73.36  ?  227  ARG B NE  1 
ATOM   2943  C  CZ  . ARG B 2  227  ? -26.986 -56.132  2.166   1.00 74.82  ?  227  ARG B CZ  1 
ATOM   2944  N  NH1 . ARG B 2  227  ? -26.373 -57.068  2.873   1.00 83.28  ?  227  ARG B NH1 1 
ATOM   2945  N  NH2 . ARG B 2  227  ? -26.338 -55.008  1.875   1.00 67.62  ?  227  ARG B NH2 1 
ATOM   2946  N  N   . ASP B 2  228  ? -32.643 -57.069  -3.049  1.00 107.11 ?  228  ASP B N   1 
ATOM   2947  C  CA  . ASP B 2  228  ? -32.719 -57.500  -4.442  1.00 102.37 ?  228  ASP B CA  1 
ATOM   2948  C  C   . ASP B 2  228  ? -31.760 -56.710  -5.325  1.00 93.78  ?  228  ASP B C   1 
ATOM   2949  O  O   . ASP B 2  228  ? -31.175 -57.263  -6.264  1.00 82.53  ?  228  ASP B O   1 
ATOM   2950  C  CB  . ASP B 2  228  ? -34.153 -57.363  -4.954  1.00 105.38 ?  228  ASP B CB  1 
ATOM   2951  C  CG  . ASP B 2  228  ? -35.160 -58.040  -4.048  1.00 107.38 ?  228  ASP B CG  1 
ATOM   2952  O  OD1 . ASP B 2  228  ? -34.735 -58.752  -3.114  1.00 104.65 ?  228  ASP B OD1 1 
ATOM   2953  O  OD2 . ASP B 2  228  ? -36.376 -57.855  -4.268  1.00 109.17 -1 228  ASP B OD2 1 
ATOM   2954  N  N   . ASN B 2  229  ? -31.592 -55.415  -5.048  1.00 100.26 ?  229  ASN B N   1 
ATOM   2955  C  CA  . ASN B 2  229  ? -30.693 -54.602  -5.859  1.00 98.04  ?  229  ASN B CA  1 
ATOM   2956  C  C   . ASN B 2  229  ? -29.237 -55.002  -5.660  1.00 94.76  ?  229  ASN B C   1 
ATOM   2957  O  O   . ASN B 2  229  ? -28.424 -54.852  -6.579  1.00 97.38  ?  229  ASN B O   1 
ATOM   2958  C  CB  . ASN B 2  229  ? -30.883 -53.121  -5.534  1.00 96.19  ?  229  ASN B CB  1 
ATOM   2959  C  CG  . ASN B 2  229  ? -32.225 -52.591  -5.998  1.00 99.75  ?  229  ASN B CG  1 
ATOM   2960  O  OD1 . ASN B 2  229  ? -32.880 -53.187  -6.852  1.00 113.10 ?  229  ASN B OD1 1 
ATOM   2961  N  ND2 . ASN B 2  229  ? -32.642 -51.463  -5.435  1.00 101.53 ?  229  ASN B ND2 1 
ATOM   2962  N  N   . VAL B 2  230  ? -28.889 -55.511  -4.477  1.00 57.86  ?  230  VAL B N   1 
ATOM   2963  C  CA  . VAL B 2  230  ? -27.507 -55.898  -4.210  1.00 58.48  ?  230  VAL B CA  1 
ATOM   2964  C  C   . VAL B 2  230  ? -27.134 -57.132  -5.021  1.00 62.72  ?  230  VAL B C   1 
ATOM   2965  O  O   . VAL B 2  230  ? -26.076 -57.179  -5.660  1.00 64.89  ?  230  VAL B O   1 
ATOM   2966  C  CB  . VAL B 2  230  ? -27.295 -56.129  -2.704  1.00 50.60  ?  230  VAL B CB  1 
ATOM   2967  C  CG1 . VAL B 2  230  ? -25.846 -56.491  -2.426  1.00 49.64  ?  230  VAL B CG1 1 
ATOM   2968  C  CG2 . VAL B 2  230  ? -27.705 -54.897  -1.915  1.00 54.56  ?  230  VAL B CG2 1 
ATOM   2969  N  N   . VAL B 2  231  ? -27.997 -58.152  -5.006  1.00 76.09  ?  231  VAL B N   1 
ATOM   2970  C  CA  . VAL B 2  231  ? -27.706 -59.369  -5.756  1.00 72.97  ?  231  VAL B CA  1 
ATOM   2971  C  C   . VAL B 2  231  ? -27.832 -59.121  -7.255  1.00 79.27  ?  231  VAL B C   1 
ATOM   2972  O  O   . VAL B 2  231  ? -27.127 -59.748  -8.056  1.00 83.09  ?  231  VAL B O   1 
ATOM   2973  C  CB  . VAL B 2  231  ? -28.617 -60.520  -5.283  1.00 66.41  ?  231  VAL B CB  1 
ATOM   2974  C  CG1 . VAL B 2  231  ? -30.082 -60.201  -5.545  1.00 71.76  ?  231  VAL B CG1 1 
ATOM   2975  C  CG2 . VAL B 2  231  ? -28.218 -61.833  -5.946  1.00 76.28  ?  231  VAL B CG2 1 
ATOM   2976  N  N   . ALA B 2  232  ? -28.711 -58.202  -7.662  1.00 77.58  ?  232  ALA B N   1 
ATOM   2977  C  CA  . ALA B 2  232  ? -28.818 -57.869  -9.078  1.00 76.23  ?  232  ALA B CA  1 
ATOM   2978  C  C   . ALA B 2  232  ? -27.565 -57.157  -9.571  1.00 72.91  ?  232  ALA B C   1 
ATOM   2979  O  O   . ALA B 2  232  ? -27.067 -57.451  -10.664 1.00 78.92  ?  232  ALA B O   1 
ATOM   2980  C  CB  . ALA B 2  232  ? -30.058 -57.011  -9.326  1.00 76.83  ?  232  ALA B CB  1 
ATOM   2981  N  N   . GLY B 2  233  ? -27.040 -56.220  -8.779  1.00 69.52  ?  233  GLY B N   1 
ATOM   2982  C  CA  . GLY B 2  233  ? -25.791 -55.573  -9.140  1.00 72.21  ?  233  GLY B CA  1 
ATOM   2983  C  C   . GLY B 2  233  ? -24.607 -56.517  -9.117  1.00 72.87  ?  233  GLY B C   1 
ATOM   2984  O  O   . GLY B 2  233  ? -23.673 -56.366  -9.911  1.00 79.04  ?  233  GLY B O   1 
ATOM   2985  N  N   . ALA B 2  234  ? -24.626 -57.502  -8.216  1.00 55.62  ?  234  ALA B N   1 
ATOM   2986  C  CA  . ALA B 2  234  ? -23.550 -58.487  -8.173  1.00 60.89  ?  234  ALA B CA  1 
ATOM   2987  C  C   . ALA B 2  234  ? -23.592 -59.402  -9.391  1.00 67.04  ?  234  ALA B C   1 
ATOM   2988  O  O   . ALA B 2  234  ? -22.544 -59.777  -9.929  1.00 63.13  ?  234  ALA B O   1 
ATOM   2989  C  CB  . ALA B 2  234  ? -23.634 -59.302  -6.883  1.00 60.20  ?  234  ALA B CB  1 
ATOM   2990  N  N   . ARG B 2  235  ? -24.795 -59.775  -9.836  1.00 83.69  ?  235  ARG B N   1 
ATOM   2991  C  CA  . ARG B 2  235  ? -24.918 -60.588  -11.041 1.00 82.42  ?  235  ARG B CA  1 
ATOM   2992  C  C   . ARG B 2  235  ? -24.548 -59.797  -12.288 1.00 83.17  ?  235  ARG B C   1 
ATOM   2993  O  O   . ARG B 2  235  ? -23.994 -60.362  -13.238 1.00 83.18  ?  235  ARG B O   1 
ATOM   2994  C  CB  . ARG B 2  235  ? -26.341 -61.134  -11.167 1.00 71.49  ?  235  ARG B CB  1 
ATOM   2995  C  CG  . ARG B 2  235  ? -26.681 -62.223  -10.166 1.00 74.44  ?  235  ARG B CG  1 
ATOM   2996  C  CD  . ARG B 2  235  ? -28.160 -62.575  -10.208 1.00 72.54  ?  235  ARG B CD  1 
ATOM   2997  N  NE  . ARG B 2  235  ? -28.488 -63.655  -9.285  1.00 78.20  ?  235  ARG B NE  1 
ATOM   2998  C  CZ  . ARG B 2  235  ? -29.719 -64.079  -9.033  1.00 80.22  ?  235  ARG B CZ  1 
ATOM   2999  N  NH1 . ARG B 2  235  ? -30.772 -63.532  -9.618  1.00 71.58  ?  235  ARG B NH1 1 
ATOM   3000  N  NH2 . ARG B 2  235  ? -29.897 -65.074  -8.169  1.00 82.04  ?  235  ARG B NH2 1 
ATOM   3001  N  N   . LEU B 2  236  ? -24.846 -58.497  -12.306 1.00 77.75  ?  236  LEU B N   1 
ATOM   3002  C  CA  . LEU B 2  236  ? -24.520 -57.680  -13.469 1.00 71.61  ?  236  LEU B CA  1 
ATOM   3003  C  C   . LEU B 2  236  ? -23.017 -57.463  -13.589 1.00 70.85  ?  236  LEU B C   1 
ATOM   3004  O  O   . LEU B 2  236  ? -22.477 -57.416  -14.701 1.00 74.91  ?  236  LEU B O   1 
ATOM   3005  C  CB  . LEU B 2  236  ? -25.250 -56.339  -13.384 1.00 65.13  ?  236  LEU B CB  1 
ATOM   3006  C  CG  . LEU B 2  236  ? -25.045 -55.373  -14.551 1.00 63.75  ?  236  LEU B CG  1 
ATOM   3007  C  CD1 . LEU B 2  236  ? -25.562 -55.983  -15.843 1.00 78.84  ?  236  LEU B CD1 1 
ATOM   3008  C  CD2 . LEU B 2  236  ? -25.724 -54.042  -14.276 1.00 66.10  ?  236  LEU B CD2 1 
ATOM   3009  N  N   . ALA B 2  237  ? -22.323 -57.340  -12.458 1.00 88.90  ?  237  ALA B N   1 
ATOM   3010  C  CA  . ALA B 2  237  ? -20.899 -57.017  -12.458 1.00 90.95  ?  237  ALA B CA  1 
ATOM   3011  C  C   . ALA B 2  237  ? -20.027 -58.266  -12.573 1.00 89.91  ?  237  ALA B C   1 
ATOM   3012  O  O   . ALA B 2  237  ? -19.179 -58.358  -13.466 1.00 91.36  ?  237  ALA B O   1 
ATOM   3013  C  CB  . ALA B 2  237  ? -20.545 -56.228  -11.193 1.00 80.02  ?  237  ALA B CB  1 
ATOM   3014  N  N   . PHE B 2  238  ? -20.224 -59.232  -11.677 1.00 85.06  ?  238  PHE B N   1 
ATOM   3015  C  CA  . PHE B 2  238  ? -19.369 -60.408  -11.612 1.00 84.55  ?  238  PHE B CA  1 
ATOM   3016  C  C   . PHE B 2  238  ? -19.944 -61.623  -12.330 1.00 85.34  ?  238  PHE B C   1 
ATOM   3017  O  O   . PHE B 2  238  ? -19.226 -62.614  -12.503 1.00 82.94  ?  238  PHE B O   1 
ATOM   3018  C  CB  . PHE B 2  238  ? -19.087 -60.771  -10.147 1.00 88.81  ?  238  PHE B CB  1 
ATOM   3019  C  CG  . PHE B 2  238  ? -18.491 -59.647  -9.348  1.00 78.68  ?  238  PHE B CG  1 
ATOM   3020  C  CD1 . PHE B 2  238  ? -17.180 -59.252  -9.554  1.00 89.37  ?  238  PHE B CD1 1 
ATOM   3021  C  CD2 . PHE B 2  238  ? -19.242 -58.983  -8.392  1.00 73.03  ?  238  PHE B CD2 1 
ATOM   3022  C  CE1 . PHE B 2  238  ? -16.627 -58.218  -8.821  1.00 89.75  ?  238  PHE B CE1 1 
ATOM   3023  C  CE2 . PHE B 2  238  ? -18.696 -57.948  -7.655  1.00 77.97  ?  238  PHE B CE2 1 
ATOM   3024  C  CZ  . PHE B 2  238  ? -17.387 -57.565  -7.871  1.00 82.75  ?  238  PHE B CZ  1 
ATOM   3025  N  N   . GLY B 2  239  ? -21.205 -61.574  -12.755 1.00 83.28  ?  239  GLY B N   1 
ATOM   3026  C  CA  . GLY B 2  239  ? -21.818 -62.726  -13.386 1.00 87.09  ?  239  GLY B CA  1 
ATOM   3027  C  C   . GLY B 2  239  ? -22.193 -63.843  -12.442 1.00 86.75  ?  239  GLY B C   1 
ATOM   3028  O  O   . GLY B 2  239  ? -22.564 -64.927  -12.903 1.00 83.02  ?  239  GLY B O   1 
ATOM   3029  N  N   . ARG B 2  240  ? -22.109 -63.613  -11.134 1.00 119.77 ?  240  ARG B N   1 
ATOM   3030  C  CA  . ARG B 2  240  ? -22.427 -64.626  -10.140 1.00 120.17 ?  240  ARG B CA  1 
ATOM   3031  C  C   . ARG B 2  240  ? -22.890 -63.928  -8.869  1.00 121.04 ?  240  ARG B C   1 
ATOM   3032  O  O   . ARG B 2  240  ? -22.864 -62.698  -8.765  1.00 117.22 ?  240  ARG B O   1 
ATOM   3033  C  CB  . ARG B 2  240  ? -21.222 -65.533  -9.863  1.00 115.53 ?  240  ARG B CB  1 
ATOM   3034  C  CG  . ARG B 2  240  ? -19.988 -64.785  -9.377  1.00 118.98 ?  240  ARG B CG  1 
ATOM   3035  C  CD  . ARG B 2  240  ? -18.984 -65.716  -8.713  1.00 124.76 ?  240  ARG B CD  1 
ATOM   3036  N  NE  . ARG B 2  240  ? -19.600 -66.567  -7.702  1.00 126.10 ?  240  ARG B NE  1 
ATOM   3037  C  CZ  . ARG B 2  240  ? -18.958 -67.510  -7.027  1.00 128.09 ?  240  ARG B CZ  1 
ATOM   3038  N  NH1 . ARG B 2  240  ? -17.673 -67.751  -7.229  1.00 124.99 ?  240  ARG B NH1 1 
ATOM   3039  N  NH2 . ARG B 2  240  ? -19.621 -68.228  -6.125  1.00 129.19 ?  240  ARG B NH2 1 
ATOM   3040  N  N   . ASP B 2  241  ? -23.320 -64.728  -7.897  1.00 105.33 ?  241  ASP B N   1 
ATOM   3041  C  CA  . ASP B 2  241  ? -23.764 -64.212  -6.608  1.00 95.10  ?  241  ASP B CA  1 
ATOM   3042  C  C   . ASP B 2  241  ? -22.569 -64.119  -5.666  1.00 90.07  ?  241  ASP B C   1 
ATOM   3043  O  O   . ASP B 2  241  ? -21.863 -65.110  -5.449  1.00 94.57  ?  241  ASP B O   1 
ATOM   3044  C  CB  . ASP B 2  241  ? -24.854 -65.102  -6.012  1.00 96.35  ?  241  ASP B CB  1 
ATOM   3045  C  CG  . ASP B 2  241  ? -26.056 -65.247  -6.927  1.00 101.67 ?  241  ASP B CG  1 
ATOM   3046  O  OD1 . ASP B 2  241  ? -26.322 -64.315  -7.715  1.00 96.60  ?  241  ASP B OD1 1 
ATOM   3047  O  OD2 . ASP B 2  241  ? -26.737 -66.292  -6.857  1.00 104.76 -1 241  ASP B OD2 1 
ATOM   3048  N  N   . VAL B 2  242  ? -22.340 -62.925  -5.114  1.00 84.51  ?  242  VAL B N   1 
ATOM   3049  C  CA  . VAL B 2  242  ? -21.268 -62.689  -4.157  1.00 84.09  ?  242  VAL B CA  1 
ATOM   3050  C  C   . VAL B 2  242  ? -21.815 -61.867  -2.997  1.00 73.36  ?  242  VAL B C   1 
ATOM   3051  O  O   . VAL B 2  242  ? -22.852 -61.209  -3.102  1.00 71.93  ?  242  VAL B O   1 
ATOM   3052  C  CB  . VAL B 2  242  ? -20.053 -61.974  -4.790  1.00 81.60  ?  242  VAL B CB  1 
ATOM   3053  C  CG1 . VAL B 2  242  ? -19.421 -62.839  -5.872  1.00 85.61  ?  242  VAL B CG1 1 
ATOM   3054  C  CG2 . VAL B 2  242  ? -20.464 -60.620  -5.348  1.00 83.82  ?  242  VAL B CG2 1 
ATOM   3055  N  N   . THR B 2  243  ? -21.095 -61.915  -1.879  1.00 87.70  ?  243  THR B N   1 
ATOM   3056  C  CA  . THR B 2  243  ? -21.437 -61.161  -0.679  1.00 85.93  ?  243  THR B CA  1 
ATOM   3057  C  C   . THR B 2  243  ? -20.327 -60.155  -0.411  1.00 81.92  ?  243  THR B C   1 
ATOM   3058  O  O   . THR B 2  243  ? -19.162 -60.538  -0.263  1.00 82.93  ?  243  THR B O   1 
ATOM   3059  C  CB  . THR B 2  243  ? -21.630 -62.088  0.524   1.00 87.17  ?  243  THR B CB  1 
ATOM   3060  O  OG1 . THR B 2  243  ? -22.871 -62.793  0.393   1.00 85.96  ?  243  THR B OG1 1 
ATOM   3061  C  CG2 . THR B 2  243  ? -21.643 -61.289  1.818   1.00 87.74  ?  243  THR B CG2 1 
ATOM   3062  N  N   . THR B 2  244  ? -20.688 -58.877  -0.347  1.00 73.59  ?  244  THR B N   1 
ATOM   3063  C  CA  . THR B 2  244  ? -19.725 -57.793  -0.202  1.00 74.68  ?  244  THR B CA  1 
ATOM   3064  C  C   . THR B 2  244  ? -19.638 -57.375  1.262   1.00 74.33  ?  244  THR B C   1 
ATOM   3065  O  O   . THR B 2  244  ? -20.645 -56.983  1.861   1.00 69.25  ?  244  THR B O   1 
ATOM   3066  C  CB  . THR B 2  244  ? -20.113 -56.601  -1.074  1.00 78.29  ?  244  THR B CB  1 
ATOM   3067  O  OG1 . THR B 2  244  ? -20.282 -57.034  -2.430  1.00 68.43  ?  244  THR B OG1 1 
ATOM   3068  C  CG2 . THR B 2  244  ? -19.035 -55.529  -1.018  1.00 78.10  ?  244  THR B CG2 1 
ATOM   3069  N  N   . ARG B 2  245  ? -18.436 -57.453  1.826   1.00 62.95  ?  245  ARG B N   1 
ATOM   3070  C  CA  . ARG B 2  245  ? -18.171 -57.056  3.201   1.00 57.39  ?  245  ARG B CA  1 
ATOM   3071  C  C   . ARG B 2  245  ? -17.202 -55.883  3.210   1.00 60.24  ?  245  ARG B C   1 
ATOM   3072  O  O   . ARG B 2  245  ? -16.270 -55.831  2.401   1.00 64.20  ?  245  ARG B O   1 
ATOM   3073  C  CB  . ARG B 2  245  ? -17.590 -58.219  4.014   1.00 65.66  ?  245  ARG B CB  1 
ATOM   3074  C  CG  . ARG B 2  245  ? -17.388 -57.906  5.489   1.00 66.04  ?  245  ARG B CG  1 
ATOM   3075  C  CD  . ARG B 2  245  ? -16.878 -59.115  6.254   1.00 67.39  ?  245  ARG B CD  1 
ATOM   3076  N  NE  . ARG B 2  245  ? -15.540 -59.504  5.826   1.00 71.75  ?  245  ARG B NE  1 
ATOM   3077  C  CZ  . ARG B 2  245  ? -14.420 -58.965  6.289   1.00 68.76  ?  245  ARG B CZ  1 
ATOM   3078  N  NH1 . ARG B 2  245  ? -14.440 -57.998  7.192   1.00 66.22  ?  245  ARG B NH1 1 
ATOM   3079  N  NH2 . ARG B 2  245  ? -13.251 -59.406  5.834   1.00 69.81  ?  245  ARG B NH2 1 
ATOM   3080  N  N   . TYR B 2  246  ? -17.421 -54.945  4.129   1.00 70.98  ?  246  TYR B N   1 
ATOM   3081  C  CA  . TYR B 2  246  ? -16.615 -53.736  4.228   1.00 68.97  ?  246  TYR B CA  1 
ATOM   3082  C  C   . TYR B 2  246  ? -15.872 -53.721  5.555   1.00 67.12  ?  246  TYR B C   1 
ATOM   3083  O  O   . TYR B 2  246  ? -16.487 -53.862  6.617   1.00 64.82  ?  246  TYR B O   1 
ATOM   3084  C  CB  . TYR B 2  246  ? -17.487 -52.484  4.094   1.00 65.35  ?  246  TYR B CB  1 
ATOM   3085  C  CG  . TYR B 2  246  ? -18.322 -52.450  2.833   1.00 65.53  ?  246  TYR B CG  1 
ATOM   3086  C  CD1 . TYR B 2  246  ? -17.724 -52.337  1.586   1.00 70.18  ?  246  TYR B CD1 1 
ATOM   3087  C  CD2 . TYR B 2  246  ? -19.708 -52.520  2.891   1.00 63.03  ?  246  TYR B CD2 1 
ATOM   3088  C  CE1 . TYR B 2  246  ? -18.480 -52.300  0.429   1.00 74.89  ?  246  TYR B CE1 1 
ATOM   3089  C  CE2 . TYR B 2  246  ? -20.475 -52.485  1.738   1.00 70.15  ?  246  TYR B CE2 1 
ATOM   3090  C  CZ  . TYR B 2  246  ? -19.854 -52.375  0.510   1.00 75.48  ?  246  TYR B CZ  1 
ATOM   3091  O  OH  . TYR B 2  246  ? -20.608 -52.338  -0.641  1.00 77.42  ?  246  TYR B OH  1 
ATOM   3092  N  N   . ASP B 2  247  ? -14.553 -53.549  5.491   1.00 75.70  ?  247  ASP B N   1 
ATOM   3093  C  CA  . ASP B 2  247  ? -13.709 -53.437  6.680   1.00 68.26  ?  247  ASP B CA  1 
ATOM   3094  C  C   . ASP B 2  247  ? -13.352 -51.963  6.847   1.00 74.49  ?  247  ASP B C   1 
ATOM   3095  O  O   . ASP B 2  247  ? -12.312 -51.498  6.377   1.00 79.08  ?  247  ASP B O   1 
ATOM   3096  C  CB  . ASP B 2  247  ? -12.467 -54.312  6.558   1.00 81.21  ?  247  ASP B CB  1 
ATOM   3097  C  CG  . ASP B 2  247  ? -11.685 -54.397  7.854   1.00 85.46  ?  247  ASP B CG  1 
ATOM   3098  O  OD1 . ASP B 2  247  ? -12.222 -53.981  8.902   1.00 89.78  ?  247  ASP B OD1 1 
ATOM   3099  O  OD2 . ASP B 2  247  ? -10.532 -54.876  7.824   1.00 84.42  -1 247  ASP B OD2 1 
ATOM   3100  N  N   . LEU B 2  248  ? -14.229 -51.225  7.530   1.00 59.93  ?  248  LEU B N   1 
ATOM   3101  C  CA  . LEU B 2  248  ? -14.051 -49.789  7.706   1.00 54.77  ?  248  LEU B CA  1 
ATOM   3102  C  C   . LEU B 2  248  ? -12.864 -49.435  8.593   1.00 61.76  ?  248  LEU B C   1 
ATOM   3103  O  O   . LEU B 2  248  ? -12.458 -48.268  8.611   1.00 66.97  ?  248  LEU B O   1 
ATOM   3104  C  CB  . LEU B 2  248  ? -15.326 -49.175  8.286   1.00 51.15  ?  248  LEU B CB  1 
ATOM   3105  C  CG  . LEU B 2  248  ? -16.616 -49.461  7.516   1.00 45.86  ?  248  LEU B CG  1 
ATOM   3106  C  CD1 . LEU B 2  248  ? -17.794 -48.748  8.157   1.00 56.80  ?  248  LEU B CD1 1 
ATOM   3107  C  CD2 . LEU B 2  248  ? -16.468 -49.049  6.061   1.00 54.78  ?  248  LEU B CD2 1 
ATOM   3108  N  N   . SER B 2  249  ? -12.300 -50.402  9.321   1.00 70.06  ?  249  SER B N   1 
ATOM   3109  C  CA  . SER B 2  249  ? -11.168 -50.117  10.196  1.00 73.25  ?  249  SER B CA  1 
ATOM   3110  C  C   . SER B 2  249  ? -9.927  -49.685  9.426   1.00 73.95  ?  249  SER B C   1 
ATOM   3111  O  O   . SER B 2  249  ? -9.022  -49.089  10.020  1.00 72.41  ?  249  SER B O   1 
ATOM   3112  C  CB  . SER B 2  249  ? -10.846 -51.343  11.051  1.00 69.19  ?  249  SER B CB  1 
ATOM   3113  O  OG  . SER B 2  249  ? -10.120 -52.306  10.307  1.00 68.96  ?  249  SER B OG  1 
ATOM   3114  N  N   . ALA B 2  250  ? -9.859  -49.975  8.126   1.00 86.33  ?  250  ALA B N   1 
ATOM   3115  C  CA  . ALA B 2  250  ? -8.736  -49.580  7.285   1.00 89.16  ?  250  ALA B CA  1 
ATOM   3116  C  C   . ALA B 2  250  ? -9.184  -48.658  6.157   1.00 91.59  ?  250  ALA B C   1 
ATOM   3117  O  O   . ALA B 2  250  ? -8.546  -48.598  5.105   1.00 99.27  ?  250  ALA B O   1 
ATOM   3118  C  CB  . ALA B 2  250  ? -8.023  -50.805  6.717   1.00 95.27  ?  250  ALA B CB  1 
ATOM   3119  N  N   . ALA B 2  251  ? -10.281 -47.935  6.362   1.00 61.34  ?  251  ALA B N   1 
ATOM   3120  C  CA  . ALA B 2  251  ? -10.842 -47.036  5.358   1.00 59.20  ?  251  ALA B CA  1 
ATOM   3121  C  C   . ALA B 2  251  ? -10.701 -45.606  5.869   1.00 66.93  ?  251  ALA B C   1 
ATOM   3122  O  O   . ALA B 2  251  ? -11.430 -45.186  6.772   1.00 66.54  ?  251  ALA B O   1 
ATOM   3123  C  CB  . ALA B 2  251  ? -12.296 -47.388  5.067   1.00 54.12  ?  251  ALA B CB  1 
ATOM   3124  N  N   . GLN B 2  252  ? -9.756  -44.863  5.289   1.00 84.44  ?  252  GLN B N   1 
ATOM   3125  C  CA  . GLN B 2  252  ? -9.582  -43.461  5.651   1.00 74.85  ?  252  GLN B CA  1 
ATOM   3126  C  C   . GLN B 2  252  ? -10.613 -42.567  4.977   1.00 71.38  ?  252  GLN B C   1 
ATOM   3127  O  O   . GLN B 2  252  ? -10.965 -41.515  5.521   1.00 72.87  ?  252  GLN B O   1 
ATOM   3128  C  CB  . GLN B 2  252  ? -8.170  -42.995  5.293   1.00 77.23  ?  252  GLN B CB  1 
ATOM   3129  C  CG  . GLN B 2  252  ? -7.065  -43.856  5.882   1.00 92.07  ?  252  GLN B CG  1 
ATOM   3130  C  CD  . GLN B 2  252  ? -6.871  -43.610  7.367   1.00 103.11 ?  252  GLN B CD  1 
ATOM   3131  O  OE1 . GLN B 2  252  ? -6.424  -44.491  8.103   1.00 110.48 ?  252  GLN B OE1 1 
ATOM   3132  N  NE2 . GLN B 2  252  ? -7.208  -42.405  7.815   1.00 87.70  ?  252  GLN B NE2 1 
ATOM   3133  N  N   . VAL B 2  253  ? -11.103 -42.963  3.806   1.00 81.29  ?  253  VAL B N   1 
ATOM   3134  C  CA  . VAL B 2  253  ? -12.118 -42.215  3.076   1.00 83.40  ?  253  VAL B CA  1 
ATOM   3135  C  C   . VAL B 2  253  ? -13.239 -43.179  2.722   1.00 82.19  ?  253  VAL B C   1 
ATOM   3136  O  O   . VAL B 2  253  ? -13.000 -44.195  2.060   1.00 86.77  ?  253  VAL B O   1 
ATOM   3137  C  CB  . VAL B 2  253  ? -11.551 -41.555  1.807   1.00 87.58  ?  253  VAL B CB  1 
ATOM   3138  C  CG1 . VAL B 2  253  ? -12.681 -41.034  0.933   1.00 87.91  ?  253  VAL B CG1 1 
ATOM   3139  C  CG2 . VAL B 2  253  ? -10.591 -40.435  2.175   1.00 86.82  ?  253  VAL B CG2 1 
ATOM   3140  N  N   . VAL B 2  254  ? -14.454 -42.871  3.164   1.00 68.00  ?  254  VAL B N   1 
ATOM   3141  C  CA  . VAL B 2  254  ? -15.627 -43.690  2.885   1.00 72.49  ?  254  VAL B CA  1 
ATOM   3142  C  C   . VAL B 2  254  ? -16.676 -42.815  2.212   1.00 71.81  ?  254  VAL B C   1 
ATOM   3143  O  O   . VAL B 2  254  ? -16.958 -41.702  2.674   1.00 68.62  ?  254  VAL B O   1 
ATOM   3144  C  CB  . VAL B 2  254  ? -16.175 -44.354  4.163   1.00 74.11  ?  254  VAL B CB  1 
ATOM   3145  C  CG1 . VAL B 2  254  ? -16.411 -43.324  5.252   1.00 67.15  ?  254  VAL B CG1 1 
ATOM   3146  C  CG2 . VAL B 2  254  ? -17.457 -45.113  3.862   1.00 72.91  ?  254  VAL B CG2 1 
ATOM   3147  N  N   . VAL B 2  255  ? -17.231 -43.307  1.107   1.00 59.46  ?  255  VAL B N   1 
ATOM   3148  C  CA  . VAL B 2  255  ? -18.237 -42.594  0.331   1.00 60.02  ?  255  VAL B CA  1 
ATOM   3149  C  C   . VAL B 2  255  ? -19.497 -43.445  0.290   1.00 62.02  ?  255  VAL B C   1 
ATOM   3150  O  O   . VAL B 2  255  ? -19.441 -44.626  -0.069  1.00 65.82  ?  255  VAL B O   1 
ATOM   3151  C  CB  . VAL B 2  255  ? -17.743 -42.281  -1.093  1.00 58.03  ?  255  VAL B CB  1 
ATOM   3152  C  CG1 . VAL B 2  255  ? -18.819 -41.544  -1.879  1.00 62.61  ?  255  VAL B CG1 1 
ATOM   3153  C  CG2 . VAL B 2  255  ? -16.459 -41.468  -1.045  1.00 57.65  ?  255  VAL B CG2 1 
ATOM   3154  N  N   . SER B 2  256  ? -20.625 -42.846  0.657   1.00 64.07  ?  256  SER B N   1 
ATOM   3155  C  CA  . SER B 2  256  ? -21.913 -43.524  0.671   1.00 59.85  ?  256  SER B CA  1 
ATOM   3156  C  C   . SER B 2  256  ? -22.823 -42.913  -0.384  1.00 69.50  ?  256  SER B C   1 
ATOM   3157  O  O   . SER B 2  256  ? -23.034 -41.696  -0.399  1.00 73.71  ?  256  SER B O   1 
ATOM   3158  C  CB  . SER B 2  256  ? -22.569 -43.429  2.049   1.00 58.77  ?  256  SER B CB  1 
ATOM   3159  O  OG  . SER B 2  256  ? -23.961 -43.676  1.961   1.00 53.09  ?  256  SER B OG  1 
ATOM   3160  N  N   . LEU B 2  257  ? -23.360 -43.759  -1.257  1.00 60.88  ?  257  LEU B N   1 
ATOM   3161  C  CA  . LEU B 2  257  ? -24.292 -43.344  -2.301  1.00 53.82  ?  257  LEU B CA  1 
ATOM   3162  C  C   . LEU B 2  257  ? -25.681 -43.816  -1.881  1.00 54.81  ?  257  LEU B C   1 
ATOM   3163  O  O   . LEU B 2  257  ? -26.151 -44.881  -2.287  1.00 53.25  ?  257  LEU B O   1 
ATOM   3164  C  CB  . LEU B 2  257  ? -23.872 -43.915  -3.652  1.00 53.55  ?  257  LEU B CB  1 
ATOM   3165  C  CG  . LEU B 2  257  ? -22.456 -43.546  -4.097  1.00 53.88  ?  257  LEU B CG  1 
ATOM   3166  C  CD1 . LEU B 2  257  ? -21.980 -44.469  -5.206  1.00 47.27  ?  257  LEU B CD1 1 
ATOM   3167  C  CD2 . LEU B 2  257  ? -22.393 -42.094  -4.540  1.00 70.36  ?  257  LEU B CD2 1 
ATOM   3168  N  N   . ASP B 2  258  ? -26.336 -43.003  -1.046  1.00 78.99  ?  258  ASP B N   1 
ATOM   3169  C  CA  . ASP B 2  258  ? -27.633 -43.339  -0.456  1.00 84.52  ?  258  ASP B CA  1 
ATOM   3170  C  C   . ASP B 2  258  ? -27.558 -44.670  0.289   1.00 91.36  ?  258  ASP B C   1 
ATOM   3171  O  O   . ASP B 2  258  ? -28.472 -45.494  0.228   1.00 94.25  ?  258  ASP B O   1 
ATOM   3172  C  CB  . ASP B 2  258  ? -28.738 -43.358  -1.518  1.00 85.26  ?  258  ASP B CB  1 
ATOM   3173  C  CG  . ASP B 2  258  ? -30.133 -43.301  -0.919  1.00 97.36  ?  258  ASP B CG  1 
ATOM   3174  O  OD1 . ASP B 2  258  ? -30.247 -43.269  0.323   1.00 100.58 ?  258  ASP B OD1 1 
ATOM   3175  O  OD2 . ASP B 2  258  ? -31.115 -43.289  -1.693  1.00 99.01  -1 258  ASP B OD2 1 
ATOM   3176  N  N   . ALA B 2  259  ? -26.445 -44.885  0.987   1.00 76.20  ?  259  ALA B N   1 
ATOM   3177  C  CA  . ALA B 2  259  ? -26.202 -46.106  1.746   1.00 74.35  ?  259  ALA B CA  1 
ATOM   3178  C  C   . ALA B 2  259  ? -26.249 -45.767  3.229   1.00 76.50  ?  259  ALA B C   1 
ATOM   3179  O  O   . ALA B 2  259  ? -25.328 -45.134  3.757   1.00 70.33  ?  259  ALA B O   1 
ATOM   3180  C  CB  . ALA B 2  259  ? -24.862 -46.733  1.365   1.00 78.70  ?  259  ALA B CB  1 
ATOM   3181  N  N   . ASP B 2  260  ? -27.320 -46.188  3.897   1.00 93.83  ?  260  ASP B N   1 
ATOM   3182  C  CA  . ASP B 2  260  ? -27.497 -45.934  5.326   1.00 89.49  ?  260  ASP B CA  1 
ATOM   3183  C  C   . ASP B 2  260  ? -26.909 -47.087  6.142   1.00 88.71  ?  260  ASP B C   1 
ATOM   3184  O  O   . ASP B 2  260  ? -27.603 -47.811  6.854   1.00 85.36  ?  260  ASP B O   1 
ATOM   3185  C  CB  . ASP B 2  260  ? -28.974 -45.719  5.639   1.00 82.93  ?  260  ASP B CB  1 
ATOM   3186  C  CG  . ASP B 2  260  ? -29.194 -45.032  6.971   1.00 93.76  ?  260  ASP B CG  1 
ATOM   3187  O  OD1 . ASP B 2  260  ? -28.196 -44.726  7.656   1.00 91.18  ?  260  ASP B OD1 1 
ATOM   3188  O  OD2 . ASP B 2  260  ? -30.368 -44.799  7.333   1.00 96.40  -1 260  ASP B OD2 1 
ATOM   3189  N  N   . PHE B 2  261  ? -25.589 -47.248  6.017   1.00 80.63  ?  261  PHE B N   1 
ATOM   3190  C  CA  . PHE B 2  261  ? -24.896 -48.355  6.666   1.00 73.67  ?  261  PHE B CA  1 
ATOM   3191  C  C   . PHE B 2  261  ? -24.748 -48.168  8.171   1.00 72.64  ?  261  PHE B C   1 
ATOM   3192  O  O   . PHE B 2  261  ? -24.373 -49.123  8.858   1.00 74.83  ?  261  PHE B O   1 
ATOM   3193  C  CB  . PHE B 2  261  ? -23.523 -48.564  6.019   1.00 68.80  ?  261  PHE B CB  1 
ATOM   3194  C  CG  . PHE B 2  261  ? -22.520 -47.490  6.345   1.00 70.49  ?  261  PHE B CG  1 
ATOM   3195  C  CD1 . PHE B 2  261  ? -22.493 -46.308  5.623   1.00 71.62  ?  261  PHE B CD1 1 
ATOM   3196  C  CD2 . PHE B 2  261  ? -21.589 -47.672  7.357   1.00 65.91  ?  261  PHE B CD2 1 
ATOM   3197  C  CE1 . PHE B 2  261  ? -21.569 -45.321  5.913   1.00 64.56  ?  261  PHE B CE1 1 
ATOM   3198  C  CE2 . PHE B 2  261  ? -20.663 -46.687  7.652   1.00 67.76  ?  261  PHE B CE2 1 
ATOM   3199  C  CZ  . PHE B 2  261  ? -20.653 -45.511  6.928   1.00 68.51  ?  261  PHE B CZ  1 
ATOM   3200  N  N   . LEU B 2  262  ? -25.028 -46.975  8.697   1.00 68.59  ?  262  LEU B N   1 
ATOM   3201  C  CA  . LEU B 2  262  ? -25.049 -46.737  10.134  1.00 72.23  ?  262  LEU B CA  1 
ATOM   3202  C  C   . LEU B 2  262  ? -26.451 -46.868  10.719  1.00 74.63  ?  262  LEU B C   1 
ATOM   3203  O  O   . LEU B 2  262  ? -26.736 -46.291  11.774  1.00 71.80  ?  262  LEU B O   1 
ATOM   3204  C  CB  . LEU B 2  262  ? -24.461 -45.362  10.455  1.00 71.32  ?  262  LEU B CB  1 
ATOM   3205  C  CG  . LEU B 2  262  ? -22.960 -45.204  10.207  1.00 62.94  ?  262  LEU B CG  1 
ATOM   3206  C  CD1 . LEU B 2  262  ? -22.476 -43.841  10.673  1.00 61.63  ?  262  LEU B CD1 1 
ATOM   3207  C  CD2 . LEU B 2  262  ? -22.192 -46.312  10.909  1.00 48.60  ?  262  LEU B CD2 1 
ATOM   3208  N  N   . ALA B 2  263  ? -27.327 -47.610  10.053  1.00 69.68  ?  263  ALA B N   1 
ATOM   3209  C  CA  . ALA B 2  263  ? -28.678 -47.900  10.499  1.00 65.22  ?  263  ALA B CA  1 
ATOM   3210  C  C   . ALA B 2  263  ? -28.837 -49.403  10.687  1.00 70.42  ?  263  ALA B C   1 
ATOM   3211  O  O   . ALA B 2  263  ? -28.065 -50.189  10.125  1.00 69.63  ?  263  ALA B O   1 
ATOM   3212  C  CB  . ALA B 2  263  ? -29.712 -47.386  9.486   1.00 68.84  ?  263  ALA B CB  1 
ATOM   3213  N  N   . PRO B 2  264  ? -29.820 -49.841  11.489  1.00 80.11  ?  264  PRO B N   1 
ATOM   3214  C  CA  . PRO B 2  264  ? -30.018 -51.284  11.695  1.00 75.71  ?  264  PRO B CA  1 
ATOM   3215  C  C   . PRO B 2  264  ? -30.190 -52.063  10.401  1.00 77.92  ?  264  PRO B C   1 
ATOM   3216  O  O   . PRO B 2  264  ? -31.226 -51.968  9.735   1.00 84.39  ?  264  PRO B O   1 
ATOM   3217  C  CB  . PRO B 2  264  ? -31.288 -51.339  12.552  1.00 83.75  ?  264  PRO B CB  1 
ATOM   3218  C  CG  . PRO B 2  264  ? -31.265 -50.064  13.309  1.00 88.09  ?  264  PRO B CG  1 
ATOM   3219  C  CD  . PRO B 2  264  ? -30.687 -49.039  12.372  1.00 87.36  ?  264  PRO B CD  1 
ATOM   3220  N  N   . GLY B 2  265  ? -29.169 -52.836  10.041  1.00 58.11  ?  265  GLY B N   1 
ATOM   3221  C  CA  . GLY B 2  265  ? -29.199 -53.649  8.851   1.00 48.73  ?  265  GLY B CA  1 
ATOM   3222  C  C   . GLY B 2  265  ? -28.172 -54.760  8.915   1.00 55.62  ?  265  GLY B C   1 
ATOM   3223  O  O   . GLY B 2  265  ? -27.705 -55.141  9.993   1.00 67.52  ?  265  GLY B O   1 
ATOM   3224  N  N   . PRO B 2  266  ? -27.803 -55.308  7.757   1.00 54.12  ?  266  PRO B N   1 
ATOM   3225  C  CA  . PRO B 2  266  ? -26.791 -56.377  7.729   1.00 57.26  ?  266  PRO B CA  1 
ATOM   3226  C  C   . PRO B 2  266  ? -25.432 -55.845  8.160   1.00 64.50  ?  266  PRO B C   1 
ATOM   3227  O  O   . PRO B 2  266  ? -24.857 -54.971  7.507   1.00 59.38  ?  266  PRO B O   1 
ATOM   3228  C  CB  . PRO B 2  266  ? -26.788 -56.827  6.262   1.00 52.79  ?  266  PRO B CB  1 
ATOM   3229  C  CG  . PRO B 2  266  ? -28.086 -56.323  5.696   1.00 52.06  ?  266  PRO B CG  1 
ATOM   3230  C  CD  . PRO B 2  266  ? -28.370 -55.049  6.425   1.00 57.07  ?  266  PRO B CD  1 
ATOM   3231  N  N   . GLY B 2  267  ? -24.923 -56.375  9.270   1.00 114.02 ?  267  GLY B N   1 
ATOM   3232  C  CA  . GLY B 2  267  ? -23.632 -55.954  9.779   1.00 111.86 ?  267  GLY B CA  1 
ATOM   3233  C  C   . GLY B 2  267  ? -23.593 -54.536  10.299  1.00 106.67 ?  267  GLY B C   1 
ATOM   3234  O  O   . GLY B 2  267  ? -22.555 -53.876  10.201  1.00 109.96 ?  267  GLY B O   1 
ATOM   3235  N  N   . PHE B 2  268  ? -24.702 -54.049  10.860  1.00 86.38  ?  268  PHE B N   1 
ATOM   3236  C  CA  . PHE B 2  268  ? -24.757 -52.664  11.314  1.00 86.89  ?  268  PHE B CA  1 
ATOM   3237  C  C   . PHE B 2  268  ? -23.847 -52.429  12.513  1.00 85.73  ?  268  PHE B C   1 
ATOM   3238  O  O   . PHE B 2  268  ? -23.135 -51.420  12.569  1.00 83.39  ?  268  PHE B O   1 
ATOM   3239  C  CB  . PHE B 2  268  ? -26.198 -52.286  11.657  1.00 85.01  ?  268  PHE B CB  1 
ATOM   3240  C  CG  . PHE B 2  268  ? -26.312 -51.199  12.687  1.00 86.02  ?  268  PHE B CG  1 
ATOM   3241  C  CD1 . PHE B 2  268  ? -25.899 -49.906  12.405  1.00 87.18  ?  268  PHE B CD1 1 
ATOM   3242  C  CD2 . PHE B 2  268  ? -26.831 -51.472  13.942  1.00 87.26  ?  268  PHE B CD2 1 
ATOM   3243  C  CE1 . PHE B 2  268  ? -26.002 -48.908  13.356  1.00 87.72  ?  268  PHE B CE1 1 
ATOM   3244  C  CE2 . PHE B 2  268  ? -26.937 -50.477  14.896  1.00 84.65  ?  268  PHE B CE2 1 
ATOM   3245  C  CZ  . PHE B 2  268  ? -26.523 -49.193  14.602  1.00 80.65  ?  268  PHE B CZ  1 
ATOM   3246  N  N   . VAL B 2  269  ? -23.858 -53.345  13.483  1.00 74.24  ?  269  VAL B N   1 
ATOM   3247  C  CA  . VAL B 2  269  ? -23.093 -53.135  14.708  1.00 66.51  ?  269  VAL B CA  1 
ATOM   3248  C  C   . VAL B 2  269  ? -21.597 -53.153  14.419  1.00 67.36  ?  269  VAL B C   1 
ATOM   3249  O  O   . VAL B 2  269  ? -20.837 -52.342  14.962  1.00 63.23  ?  269  VAL B O   1 
ATOM   3250  C  CB  . VAL B 2  269  ? -23.483 -54.186  15.763  1.00 72.29  ?  269  VAL B CB  1 
ATOM   3251  C  CG1 . VAL B 2  269  ? -22.608 -54.054  17.002  1.00 68.35  ?  269  VAL B CG1 1 
ATOM   3252  C  CG2 . VAL B 2  269  ? -24.955 -54.054  16.123  1.00 72.99  ?  269  VAL B CG2 1 
ATOM   3253  N  N   . ALA B 2  270  ? -21.151 -54.069  13.555  1.00 56.38  ?  270  ALA B N   1 
ATOM   3254  C  CA  . ALA B 2  270  ? -19.726 -54.170  13.255  1.00 50.94  ?  270  ALA B CA  1 
ATOM   3255  C  C   . ALA B 2  270  ? -19.232 -52.957  12.476  1.00 54.42  ?  270  ALA B C   1 
ATOM   3256  O  O   . ALA B 2  270  ? -18.137 -52.447  12.742  1.00 61.83  ?  270  ALA B O   1 
ATOM   3257  C  CB  . ALA B 2  270  ? -19.441 -55.456  12.482  1.00 48.26  ?  270  ALA B CB  1 
ATOM   3258  N  N   . TYR B 2  271  ? -20.021 -52.484  11.509  1.00 56.26  ?  271  TYR B N   1 
ATOM   3259  C  CA  . TYR B 2  271  ? -19.625 -51.301  10.749  1.00 57.51  ?  271  TYR B CA  1 
ATOM   3260  C  C   . TYR B 2  271  ? -19.613 -50.058  11.631  1.00 58.23  ?  271  TYR B C   1 
ATOM   3261  O  O   . TYR B 2  271  ? -18.689 -49.240  11.549  1.00 48.63  ?  271  TYR B O   1 
ATOM   3262  C  CB  . TYR B 2  271  ? -20.561 -51.098  9.556   1.00 53.08  ?  271  TYR B CB  1 
ATOM   3263  C  CG  . TYR B 2  271  ? -20.521 -52.207  8.527   1.00 58.83  ?  271  TYR B CG  1 
ATOM   3264  C  CD1 . TYR B 2  271  ? -19.452 -53.092  8.465   1.00 63.78  ?  271  TYR B CD1 1 
ATOM   3265  C  CD2 . TYR B 2  271  ? -21.555 -52.368  7.612   1.00 58.33  ?  271  TYR B CD2 1 
ATOM   3266  C  CE1 . TYR B 2  271  ? -19.416 -54.107  7.526   1.00 64.38  ?  271  TYR B CE1 1 
ATOM   3267  C  CE2 . TYR B 2  271  ? -21.527 -53.379  6.669   1.00 63.88  ?  271  TYR B CE2 1 
ATOM   3268  C  CZ  . TYR B 2  271  ? -20.455 -54.245  6.630   1.00 69.18  ?  271  TYR B CZ  1 
ATOM   3269  O  OH  . TYR B 2  271  ? -20.422 -55.252  5.692   1.00 72.36  ?  271  TYR B OH  1 
ATOM   3270  N  N   . ALA B 2  272  ? -20.630 -49.901  12.481  1.00 61.42  ?  272  ALA B N   1 
ATOM   3271  C  CA  . ALA B 2  272  ? -20.696 -48.731  13.351  1.00 53.34  ?  272  ALA B CA  1 
ATOM   3272  C  C   . ALA B 2  272  ? -19.558 -48.728  14.361  1.00 52.94  ?  272  ALA B C   1 
ATOM   3273  O  O   . ALA B 2  272  ? -19.013 -47.667  14.688  1.00 56.69  ?  272  ALA B O   1 
ATOM   3274  C  CB  . ALA B 2  272  ? -22.046 -48.682  14.064  1.00 53.73  ?  272  ALA B CB  1 
ATOM   3275  N  N   . ARG B 2  273  ? -19.186 -49.905  14.870  1.00 80.38  ?  273  ARG B N   1 
ATOM   3276  C  CA  . ARG B 2  273  ? -18.087 -49.984  15.825  1.00 80.17  ?  273  ARG B CA  1 
ATOM   3277  C  C   . ARG B 2  273  ? -16.765 -49.606  15.169  1.00 81.01  ?  273  ARG B C   1 
ATOM   3278  O  O   . ARG B 2  273  ? -16.020 -48.770  15.691  1.00 80.48  ?  273  ARG B O   1 
ATOM   3279  C  CB  . ARG B 2  273  ? -18.008 -51.387  16.424  1.00 78.46  ?  273  ARG B CB  1 
ATOM   3280  C  CG  . ARG B 2  273  ? -16.871 -51.571  17.419  1.00 79.67  ?  273  ARG B CG  1 
ATOM   3281  C  CD  . ARG B 2  273  ? -17.318 -51.252  18.837  1.00 75.99  ?  273  ARG B CD  1 
ATOM   3282  N  NE  . ARG B 2  273  ? -18.582 -51.902  19.164  1.00 82.67  ?  273  ARG B NE  1 
ATOM   3283  C  CZ  . ARG B 2  273  ? -19.064 -52.030  20.392  1.00 86.66  ?  273  ARG B CZ  1 
ATOM   3284  N  NH1 . ARG B 2  273  ? -18.408 -51.567  21.444  1.00 93.02  ?  273  ARG B NH1 1 
ATOM   3285  N  NH2 . ARG B 2  273  ? -20.233 -52.638  20.570  1.00 88.16  ?  273  ARG B NH2 1 
ATOM   3286  N  N   . ALA B 2  274  ? -16.461 -50.210  14.018  1.00 70.51  ?  274  ALA B N   1 
ATOM   3287  C  CA  . ALA B 2  274  ? -15.215 -49.900  13.324  1.00 72.16  ?  274  ALA B CA  1 
ATOM   3288  C  C   . ALA B 2  274  ? -15.142 -48.426  12.946  1.00 80.57  ?  274  ALA B C   1 
ATOM   3289  O  O   . ALA B 2  274  ? -14.095 -47.787  13.107  1.00 81.43  ?  274  ALA B O   1 
ATOM   3290  C  CB  . ALA B 2  274  ? -15.073 -50.780  12.083  1.00 81.45  ?  274  ALA B CB  1 
ATOM   3291  N  N   . PHE B 2  275  ? -16.246 -47.868  12.443  1.00 77.92  ?  275  PHE B N   1 
ATOM   3292  C  CA  . PHE B 2  275  ? -16.269 -46.452  12.087  1.00 71.73  ?  275  PHE B CA  1 
ATOM   3293  C  C   . PHE B 2  275  ? -16.031 -45.565  13.303  1.00 69.49  ?  275  PHE B C   1 
ATOM   3294  O  O   . PHE B 2  275  ? -15.271 -44.592  13.230  1.00 69.48  ?  275  PHE B O   1 
ATOM   3295  C  CB  . PHE B 2  275  ? -17.600 -46.102  11.423  1.00 63.41  ?  275  PHE B CB  1 
ATOM   3296  C  CG  . PHE B 2  275  ? -17.588 -44.787  10.700  1.00 65.14  ?  275  PHE B CG  1 
ATOM   3297  C  CD1 . PHE B 2  275  ? -16.782 -44.595  9.592   1.00 66.98  ?  275  PHE B CD1 1 
ATOM   3298  C  CD2 . PHE B 2  275  ? -18.392 -43.743  11.128  1.00 64.54  ?  275  PHE B CD2 1 
ATOM   3299  C  CE1 . PHE B 2  275  ? -16.775 -43.382  8.929   1.00 70.93  ?  275  PHE B CE1 1 
ATOM   3300  C  CE2 . PHE B 2  275  ? -18.391 -42.532  10.469  1.00 60.88  ?  275  PHE B CE2 1 
ATOM   3301  C  CZ  . PHE B 2  275  ? -17.581 -42.351  9.368   1.00 67.68  ?  275  PHE B CZ  1 
ATOM   3302  N  N   . ALA B 2  276  ? -16.671 -45.884  14.429  1.00 50.01  ?  276  ALA B N   1 
ATOM   3303  C  CA  . ALA B 2  276  ? -16.523 -45.058  15.623  1.00 47.74  ?  276  ALA B CA  1 
ATOM   3304  C  C   . ALA B 2  276  ? -15.099 -45.116  16.163  1.00 56.40  ?  276  ALA B C   1 
ATOM   3305  O  O   . ALA B 2  276  ? -14.509 -44.081  16.493  1.00 53.18  ?  276  ALA B O   1 
ATOM   3306  C  CB  . ALA B 2  276  ? -17.525 -45.496  16.689  1.00 58.57  ?  276  ALA B CB  1 
ATOM   3307  N  N   . GLU B 2  277  ? -14.529 -46.321  16.263  1.00 94.94  ?  277  GLU B N   1 
ATOM   3308  C  CA  . GLU B 2  277  ? -13.154 -46.452  16.737  1.00 95.75  ?  277  GLU B CA  1 
ATOM   3309  C  C   . GLU B 2  277  ? -12.162 -45.740  15.827  1.00 86.49  ?  277  GLU B C   1 
ATOM   3310  O  O   . GLU B 2  277  ? -11.064 -45.395  16.276  1.00 86.98  ?  277  GLU B O   1 
ATOM   3311  C  CB  . GLU B 2  277  ? -12.775 -47.928  16.878  1.00 93.38  ?  277  GLU B CB  1 
ATOM   3312  C  CG  . GLU B 2  277  ? -13.723 -48.737  17.748  1.00 94.55  ?  277  GLU B CG  1 
ATOM   3313  C  CD  . GLU B 2  277  ? -13.255 -48.841  19.186  1.00 110.49 ?  277  GLU B CD  1 
ATOM   3314  O  OE1 . GLU B 2  277  ? -12.556 -47.919  19.658  1.00 116.21 ?  277  GLU B OE1 1 
ATOM   3315  O  OE2 . GLU B 2  277  ? -13.589 -49.845  19.847  1.00 120.31 -1 277  GLU B OE2 1 
ATOM   3316  N  N   . ARG B 2  278  ? -12.520 -45.511  14.564  1.00 73.09  ?  278  ARG B N   1 
ATOM   3317  C  CA  . ARG B 2  278  ? -11.683 -44.708  13.683  1.00 82.75  ?  278  ARG B CA  1 
ATOM   3318  C  C   . ARG B 2  278  ? -11.920 -43.213  13.855  1.00 85.65  ?  278  ARG B C   1 
ATOM   3319  O  O   . ARG B 2  278  ? -11.085 -42.413  13.421  1.00 78.75  ?  278  ARG B O   1 
ATOM   3320  C  CB  . ARG B 2  278  ? -11.922 -45.099  12.222  1.00 86.98  ?  278  ARG B CB  1 
ATOM   3321  C  CG  . ARG B 2  278  ? -11.429 -46.489  11.851  1.00 88.32  ?  278  ARG B CG  1 
ATOM   3322  C  CD  . ARG B 2  278  ? -9.941  -46.648  12.116  1.00 87.48  ?  278  ARG B CD  1 
ATOM   3323  N  NE  . ARG B 2  278  ? -9.184  -45.471  11.707  1.00 89.88  ?  278  ARG B NE  1 
ATOM   3324  C  CZ  . ARG B 2  278  ? -8.643  -45.306  10.508  1.00 110.31 ?  278  ARG B CZ  1 
ATOM   3325  N  NH1 . ARG B 2  278  ? -8.764  -46.224  9.562   1.00 107.83 ?  278  ARG B NH1 1 
ATOM   3326  N  NH2 . ARG B 2  278  ? -7.967  -44.191  10.250  1.00 113.39 ?  278  ARG B NH2 1 
ATOM   3327  N  N   . ARG B 2  279  ? -13.034 -42.821  14.476  1.00 72.26  ?  279  ARG B N   1 
ATOM   3328  C  CA  . ARG B 2  279  ? -13.360 -41.418  14.694  1.00 61.40  ?  279  ARG B CA  1 
ATOM   3329  C  C   . ARG B 2  279  ? -13.006 -40.929  16.092  1.00 60.02  ?  279  ARG B C   1 
ATOM   3330  O  O   . ARG B 2  279  ? -13.026 -39.716  16.327  1.00 66.42  ?  279  ARG B O   1 
ATOM   3331  C  CB  . ARG B 2  279  ? -14.855 -41.174  14.443  1.00 57.91  ?  279  ARG B CB  1 
ATOM   3332  C  CG  . ARG B 2  279  ? -15.289 -41.349  12.996  1.00 65.95  ?  279  ARG B CG  1 
ATOM   3333  C  CD  . ARG B 2  279  ? -16.557 -40.564  12.694  1.00 66.60  ?  279  ARG B CD  1 
ATOM   3334  N  NE  . ARG B 2  279  ? -16.280 -39.196  12.273  1.00 73.97  ?  279  ARG B NE  1 
ATOM   3335  C  CZ  . ARG B 2  279  ? -15.962 -38.843  11.035  1.00 70.80  ?  279  ARG B CZ  1 
ATOM   3336  N  NH1 . ARG B 2  279  ? -15.856 -39.737  10.066  1.00 65.67  ?  279  ARG B NH1 1 
ATOM   3337  N  NH2 . ARG B 2  279  ? -15.745 -37.560  10.762  1.00 78.84  ?  279  ARG B NH2 1 
ATOM   3338  N  N   . LYS B 2  280  ? -12.692 -41.830  17.018  1.00 60.99  ?  280  LYS B N   1 
ATOM   3339  C  CA  . LYS B 2  280  ? -12.365 -41.451  18.391  1.00 67.06  ?  280  LYS B CA  1 
ATOM   3340  C  C   . LYS B 2  280  ? -10.955 -40.873  18.407  1.00 68.33  ?  280  LYS B C   1 
ATOM   3341  O  O   . LYS B 2  280  ? -9.968  -41.608  18.333  1.00 75.99  ?  280  LYS B O   1 
ATOM   3342  C  CB  . LYS B 2  280  ? -12.488 -42.651  19.322  1.00 61.28  ?  280  LYS B CB  1 
ATOM   3343  C  CG  . LYS B 2  280  ? -13.923 -43.065  19.616  1.00 50.26  ?  280  LYS B CG  1 
ATOM   3344  C  CD  . LYS B 2  280  ? -13.992 -44.445  20.253  1.00 63.04  ?  280  LYS B CD  1 
ATOM   3345  C  CE  . LYS B 2  280  ? -15.424 -44.958  20.294  1.00 63.13  ?  280  LYS B CE  1 
ATOM   3346  N  NZ  . LYS B 2  280  ? -15.495 -46.394  20.679  1.00 57.95  ?  280  LYS B NZ  1 
ATOM   3347  N  N   . VAL B 2  281  ? -10.859 -39.550  18.508  1.00 53.18  ?  281  VAL B N   1 
ATOM   3348  C  CA  . VAL B 2  281  ? -9.582  -38.849  18.455  1.00 55.31  ?  281  VAL B CA  1 
ATOM   3349  C  C   . VAL B 2  281  ? -9.129  -38.527  19.869  1.00 59.90  ?  281  VAL B C   1 
ATOM   3350  O  O   . VAL B 2  281  ? -9.940  -38.267  20.766  1.00 64.15  ?  281  VAL B O   1 
ATOM   3351  C  CB  . VAL B 2  281  ? -9.676  -37.571  17.596  1.00 61.46  ?  281  VAL B CB  1 
ATOM   3352  C  CG1 . VAL B 2  281  ? -9.694  -37.926  16.119  1.00 66.56  ?  281  VAL B CG1 1 
ATOM   3353  C  CG2 . VAL B 2  281  ? -10.913 -36.770  17.969  1.00 64.64  ?  281  VAL B CG2 1 
ATOM   3354  N  N   . ARG B 2  282  ? -7.811  -38.545  20.069  1.00 82.60  ?  282  ARG B N   1 
ATOM   3355  C  CA  . ARG B 2  282  ? -7.214  -38.255  21.366  1.00 81.01  ?  282  ARG B CA  1 
ATOM   3356  C  C   . ARG B 2  282  ? -6.084  -37.242  21.227  1.00 88.19  ?  282  ARG B C   1 
ATOM   3357  O  O   . ARG B 2  282  ? -5.939  -36.600  20.182  1.00 86.69  ?  282  ARG B O   1 
ATOM   3358  C  CB  . ARG B 2  282  ? -6.687  -39.537  22.015  1.00 69.97  ?  282  ARG B CB  1 
ATOM   3359  C  CG  . ARG B 2  282  ? -7.761  -40.483  22.520  1.00 70.08  ?  282  ARG B CG  1 
ATOM   3360  C  CD  . ARG B 2  282  ? -7.139  -41.755  23.075  1.00 86.90  ?  282  ARG B CD  1 
ATOM   3361  N  NE  . ARG B 2  282  ? -8.085  -42.538  23.863  1.00 95.15  ?  282  ARG B NE  1 
ATOM   3362  C  CZ  . ARG B 2  282  ? -8.210  -42.458  25.181  1.00 79.94  ?  282  ARG B CZ  1 
ATOM   3363  N  NH1 . ARG B 2  282  ? -7.473  -41.625  25.897  1.00 70.92  ?  282  ARG B NH1 1 
ATOM   3364  N  NH2 . ARG B 2  282  ? -9.099  -43.234  25.796  1.00 70.82  ?  282  ARG B NH2 1 
ATOM   3365  N  N   . LYS B 2  283  ? -5.278  -37.093  22.280  1.00 101.81 ?  283  LYS B N   1 
ATOM   3366  C  CA  . LYS B 2  283  ? -4.104  -36.231  22.197  1.00 102.40 ?  283  LYS B CA  1 
ATOM   3367  C  C   . LYS B 2  283  ? -3.050  -36.841  21.280  1.00 109.93 ?  283  LYS B C   1 
ATOM   3368  O  O   . LYS B 2  283  ? -2.519  -36.166  20.391  1.00 111.32 ?  283  LYS B O   1 
ATOM   3369  C  CB  . LYS B 2  283  ? -3.532  -35.989  23.596  1.00 102.51 ?  283  LYS B CB  1 
ATOM   3370  C  CG  . LYS B 2  283  ? -2.377  -34.990  23.669  1.00 105.58 ?  283  LYS B CG  1 
ATOM   3371  C  CD  . LYS B 2  283  ? -2.530  -33.848  22.675  1.00 123.92 ?  283  LYS B CD  1 
ATOM   3372  C  CE  . LYS B 2  283  ? -1.496  -32.762  22.921  1.00 126.05 ?  283  LYS B CE  1 
ATOM   3373  N  NZ  . LYS B 2  283  ? -1.178  -32.006  21.680  1.00 117.21 ?  283  LYS B NZ  1 
ATOM   3374  N  N   . ASP B 2  284  ? -2.740  -38.121  21.481  1.00 99.20  ?  284  ASP B N   1 
ATOM   3375  C  CA  . ASP B 2  284  ? -1.750  -38.808  20.663  1.00 96.42  ?  284  ASP B CA  1 
ATOM   3376  C  C   . ASP B 2  284  ? -2.265  -39.158  19.275  1.00 93.11  ?  284  ASP B C   1 
ATOM   3377  O  O   . ASP B 2  284  ? -1.476  -39.610  18.438  1.00 90.92  ?  284  ASP B O   1 
ATOM   3378  C  CB  . ASP B 2  284  ? -1.283  -40.084  21.368  1.00 99.95  ?  284  ASP B CB  1 
ATOM   3379  C  CG  . ASP B 2  284  ? -0.971  -39.860  22.833  1.00 115.59 ?  284  ASP B CG  1 
ATOM   3380  O  OD1 . ASP B 2  284  ? 0.148   -39.397  23.140  1.00 128.00 ?  284  ASP B OD1 1 
ATOM   3381  O  OD2 . ASP B 2  284  ? -1.846  -40.145  23.678  1.00 126.34 -1 284  ASP B OD2 1 
ATOM   3382  N  N   . SER B 2  285  ? -3.556  -38.963  19.012  1.00 64.52  ?  285  SER B N   1 
ATOM   3383  C  CA  . SER B 2  285  ? -4.124  -39.317  17.719  1.00 54.37  ?  285  SER B CA  1 
ATOM   3384  C  C   . SER B 2  285  ? -3.497  -38.482  16.609  1.00 61.09  ?  285  SER B C   1 
ATOM   3385  O  O   . SER B 2  285  ? -3.119  -37.324  16.807  1.00 71.61  ?  285  SER B O   1 
ATOM   3386  C  CB  . SER B 2  285  ? -5.640  -39.118  17.735  1.00 44.11  ?  285  SER B CB  1 
ATOM   3387  O  OG  . SER B 2  285  ? -6.216  -39.445  16.484  1.00 53.63  ?  285  SER B OG  1 
ATOM   3388  N  N   . THR B 2  286  ? -3.386  -39.086  15.427  1.00 71.39  ?  286  THR B N   1 
ATOM   3389  C  CA  . THR B 2  286  ? -2.791  -38.418  14.277  1.00 75.41  ?  286  THR B CA  1 
ATOM   3390  C  C   . THR B 2  286  ? -3.611  -38.518  12.999  1.00 73.51  ?  286  THR B C   1 
ATOM   3391  O  O   . THR B 2  286  ? -3.419  -37.683  12.106  1.00 66.07  ?  286  THR B O   1 
ATOM   3392  C  CB  . THR B 2  286  ? -1.383  -38.971  14.002  1.00 74.12  ?  286  THR B CB  1 
ATOM   3393  O  OG1 . THR B 2  286  ? -0.773  -38.228  12.939  1.00 79.17  ?  286  THR B OG1 1 
ATOM   3394  C  CG2 . THR B 2  286  ? -1.447  -40.443  13.619  1.00 68.16  ?  286  THR B CG2 1 
ATOM   3395  N  N   . THR B 2  287  ? -4.511  -39.491  12.875  1.00 103.22 ?  287  THR B N   1 
ATOM   3396  C  CA  . THR B 2  287  ? -5.323  -39.657  11.679  1.00 106.34 ?  287  THR B CA  1 
ATOM   3397  C  C   . THR B 2  287  ? -6.796  -39.678  12.058  1.00 102.39 ?  287  THR B C   1 
ATOM   3398  O  O   . THR B 2  287  ? -7.163  -39.945  13.205  1.00 98.52  ?  287  THR B O   1 
ATOM   3399  C  CB  . THR B 2  287  ? -4.965  -40.944  10.923  1.00 108.73 ?  287  THR B CB  1 
ATOM   3400  O  OG1 . THR B 2  287  ? -5.136  -42.074  11.788  1.00 103.30 ?  287  THR B OG1 1 
ATOM   3401  C  CG2 . THR B 2  287  ? -3.524  -40.894  10.441  1.00 105.57 ?  287  THR B CG2 1 
ATOM   3402  N  N   . MET B 2  288  ? -7.643  -39.392  11.071  1.00 74.92  ?  288  MET B N   1 
ATOM   3403  C  CA  . MET B 2  288  ? -9.085  -39.398  11.275  1.00 70.04  ?  288  MET B CA  1 
ATOM   3404  C  C   . MET B 2  288  ? -9.759  -39.611  9.929   1.00 76.34  ?  288  MET B C   1 
ATOM   3405  O  O   . MET B 2  288  ? -9.446  -38.908  8.964   1.00 87.45  ?  288  MET B O   1 
ATOM   3406  C  CB  . MET B 2  288  ? -9.563  -38.090  11.912  1.00 69.92  ?  288  MET B CB  1 
ATOM   3407  C  CG  . MET B 2  288  ? -11.070 -37.917  11.896  1.00 70.96  ?  288  MET B CG  1 
ATOM   3408  S  SD  . MET B 2  288  ? -11.648 -36.794  13.178  1.00 79.36  ?  288  MET B SD  1 
ATOM   3409  C  CE  . MET B 2  288  ? -13.175 -36.214  12.451  1.00 71.21  ?  288  MET B CE  1 
ATOM   3410  N  N   . ASN B 2  289  ? -10.675 -40.574  9.868   1.00 59.71  ?  289  ASN B N   1 
ATOM   3411  C  CA  . ASN B 2  289  ? -11.341 -40.877  8.612   1.00 58.43  ?  289  ASN B CA  1 
ATOM   3412  C  C   . ASN B 2  289  ? -12.383 -39.811  8.279   1.00 58.99  ?  289  ASN B C   1 
ATOM   3413  O  O   . ASN B 2  289  ? -12.854 -39.066  9.143   1.00 61.55  ?  289  ASN B O   1 
ATOM   3414  C  CB  . ASN B 2  289  ? -11.996 -42.258  8.666   1.00 57.76  ?  289  ASN B CB  1 
ATOM   3415  C  CG  . ASN B 2  289  ? -13.000 -42.386  9.794   1.00 44.47  ?  289  ASN B CG  1 
ATOM   3416  O  OD1 . ASN B 2  289  ? -13.123 -41.498  10.637  1.00 48.23  ?  289  ASN B OD1 1 
ATOM   3417  N  ND2 . ASN B 2  289  ? -13.722 -43.499  9.816   1.00 41.89  ?  289  ASN B ND2 1 
ATOM   3418  N  N   . ARG B 2  290  ? -12.743 -39.749  7.000   1.00 56.45  ?  290  ARG B N   1 
ATOM   3419  C  CA  . ARG B 2  290  ? -13.706 -38.784  6.492   1.00 57.84  ?  290  ARG B CA  1 
ATOM   3420  C  C   . ARG B 2  290  ? -14.831 -39.520  5.780   1.00 59.47  ?  290  ARG B C   1 
ATOM   3421  O  O   . ARG B 2  290  ? -14.595 -40.519  5.094   1.00 64.93  ?  290  ARG B O   1 
ATOM   3422  C  CB  . ARG B 2  290  ? -13.028 -37.788  5.543   1.00 63.83  ?  290  ARG B CB  1 
ATOM   3423  C  CG  . ARG B 2  290  ? -13.966 -36.779  4.905   1.00 68.89  ?  290  ARG B CG  1 
ATOM   3424  C  CD  . ARG B 2  290  ? -13.229 -35.910  3.901   1.00 74.66  ?  290  ARG B CD  1 
ATOM   3425  N  NE  . ARG B 2  290  ? -12.186 -35.111  4.534   1.00 74.19  ?  290  ARG B NE  1 
ATOM   3426  C  CZ  . ARG B 2  290  ? -10.888 -35.260  4.311   1.00 74.19  ?  290  ARG B CZ  1 
ATOM   3427  N  NH1 . ARG B 2  290  ? -10.431 -36.177  3.474   1.00 72.77  ?  290  ARG B NH1 1 
ATOM   3428  N  NH2 . ARG B 2  290  ? -10.027 -34.470  4.945   1.00 82.53  ?  290  ARG B NH2 1 
ATOM   3429  N  N   . LEU B 2  291  ? -16.056 -39.025  5.946   1.00 45.89  ?  291  LEU B N   1 
ATOM   3430  C  CA  . LEU B 2  291  ? -17.249 -39.669  5.411   1.00 42.32  ?  291  LEU B CA  1 
ATOM   3431  C  C   . LEU B 2  291  ? -17.960 -38.728  4.449   1.00 49.57  ?  291  LEU B C   1 
ATOM   3432  O  O   . LEU B 2  291  ? -18.281 -37.591  4.810   1.00 56.34  ?  291  LEU B O   1 
ATOM   3433  C  CB  . LEU B 2  291  ? -18.199 -40.083  6.540   1.00 32.87  ?  291  LEU B CB  1 
ATOM   3434  C  CG  . LEU B 2  291  ? -19.614 -40.532  6.160   1.00 32.07  ?  291  LEU B CG  1 
ATOM   3435  C  CD1 . LEU B 2  291  ? -19.595 -41.641  5.116   1.00 37.24  ?  291  LEU B CD1 1 
ATOM   3436  C  CD2 . LEU B 2  291  ? -20.386 -40.970  7.394   1.00 32.72  ?  291  LEU B CD2 1 
ATOM   3437  N  N   . TYR B 2  292  ? -18.206 -39.207  3.232   1.00 76.96  ?  292  TYR B N   1 
ATOM   3438  C  CA  . TYR B 2  292  ? -19.042 -38.523  2.254   1.00 74.47  ?  292  TYR B CA  1 
ATOM   3439  C  C   . TYR B 2  292  ? -20.334 -39.308  2.083   1.00 72.51  ?  292  TYR B C   1 
ATOM   3440  O  O   . TYR B 2  292  ? -20.299 -40.528  1.885   1.00 65.12  ?  292  TYR B O   1 
ATOM   3441  C  CB  . TYR B 2  292  ? -18.333 -38.394  0.903   1.00 75.91  ?  292  TYR B CB  1 
ATOM   3442  C  CG  . TYR B 2  292  ? -17.178 -37.421  0.876   1.00 80.85  ?  292  TYR B CG  1 
ATOM   3443  C  CD1 . TYR B 2  292  ? -17.396 -36.057  0.739   1.00 85.84  ?  292  TYR B CD1 1 
ATOM   3444  C  CD2 . TYR B 2  292  ? -15.866 -37.869  0.964   1.00 82.55  ?  292  TYR B CD2 1 
ATOM   3445  C  CE1 . TYR B 2  292  ? -16.342 -35.165  0.705   1.00 91.43  ?  292  TYR B CE1 1 
ATOM   3446  C  CE2 . TYR B 2  292  ? -14.806 -36.986  0.931   1.00 82.55  ?  292  TYR B CE2 1 
ATOM   3447  C  CZ  . TYR B 2  292  ? -15.049 -35.636  0.802   1.00 89.10  ?  292  TYR B CZ  1 
ATOM   3448  O  OH  . TYR B 2  292  ? -13.994 -34.754  0.769   1.00 96.54  ?  292  TYR B OH  1 
ATOM   3449  N  N   . VAL B 2  293  ? -21.468 -38.618  2.156   1.00 65.05  ?  293  VAL B N   1 
ATOM   3450  C  CA  . VAL B 2  293  ? -22.770 -39.249  1.981   1.00 66.55  ?  293  VAL B CA  1 
ATOM   3451  C  C   . VAL B 2  293  ? -23.595 -38.410  1.013   1.00 70.22  ?  293  VAL B C   1 
ATOM   3452  O  O   . VAL B 2  293  ? -23.524 -37.176  1.024   1.00 75.18  ?  293  VAL B O   1 
ATOM   3453  C  CB  . VAL B 2  293  ? -23.509 -39.432  3.327   1.00 62.15  ?  293  VAL B CB  1 
ATOM   3454  C  CG1 . VAL B 2  293  ? -23.847 -38.091  3.948   1.00 62.01  ?  293  VAL B CG1 1 
ATOM   3455  C  CG2 . VAL B 2  293  ? -24.762 -40.283  3.149   1.00 65.62  ?  293  VAL B CG2 1 
ATOM   3456  N  N   . VAL B 2  294  ? -24.355 -39.088  0.158   1.00 45.04  ?  294  VAL B N   1 
ATOM   3457  C  CA  . VAL B 2  294  ? -25.274 -38.458  -0.783  1.00 43.75  ?  294  VAL B CA  1 
ATOM   3458  C  C   . VAL B 2  294  ? -26.612 -39.161  -0.616  1.00 52.39  ?  294  VAL B C   1 
ATOM   3459  O  O   . VAL B 2  294  ? -26.761 -40.321  -1.020  1.00 63.60  ?  294  VAL B O   1 
ATOM   3460  C  CB  . VAL B 2  294  ? -24.780 -38.552  -2.233  1.00 55.72  ?  294  VAL B CB  1 
ATOM   3461  C  CG1 . VAL B 2  294  ? -25.821 -37.992  -3.187  1.00 65.21  ?  294  VAL B CG1 1 
ATOM   3462  C  CG2 . VAL B 2  294  ? -23.455 -37.824  -2.394  1.00 54.62  ?  294  VAL B CG2 1 
ATOM   3463  N  N   . GLU B 2  295  ? -27.582 -38.473  -0.019  1.00 77.98  ?  295  GLU B N   1 
ATOM   3464  C  CA  . GLU B 2  295  ? -28.854 -39.088  0.326   1.00 83.05  ?  295  GLU B CA  1 
ATOM   3465  C  C   . GLU B 2  295  ? -29.992 -38.123  0.032   1.00 88.58  ?  295  GLU B C   1 
ATOM   3466  O  O   . GLU B 2  295  ? -29.807 -36.904  -0.014  1.00 91.34  ?  295  GLU B O   1 
ATOM   3467  C  CB  . GLU B 2  295  ? -28.887 -39.503  1.802   1.00 81.91  ?  295  GLU B CB  1 
ATOM   3468  C  CG  . GLU B 2  295  ? -28.544 -38.369  2.756   1.00 94.20  ?  295  GLU B CG  1 
ATOM   3469  C  CD  . GLU B 2  295  ? -28.467 -38.819  4.200   1.00 101.72 ?  295  GLU B CD  1 
ATOM   3470  O  OE1 . GLU B 2  295  ? -28.558 -40.040  4.449   1.00 106.61 ?  295  GLU B OE1 1 
ATOM   3471  O  OE2 . GLU B 2  295  ? -28.318 -37.951  5.086   1.00 95.52  -1 295  GLU B OE2 1 
ATOM   3472  N  N   . ALA B 2  296  ? -31.185 -38.690  -0.164  1.00 69.84  ?  296  ALA B N   1 
ATOM   3473  C  CA  . ALA B 2  296  ? -32.375 -37.876  -0.385  1.00 67.40  ?  296  ALA B CA  1 
ATOM   3474  C  C   . ALA B 2  296  ? -32.976 -37.409  0.935   1.00 71.04  ?  296  ALA B C   1 
ATOM   3475  O  O   . ALA B 2  296  ? -33.199 -36.210  1.137   1.00 77.34  ?  296  ALA B O   1 
ATOM   3476  C  CB  . ALA B 2  296  ? -33.405 -38.660  -1.200  1.00 75.46  ?  296  ALA B CB  1 
ATOM   3477  N  N   . SER B 2  297  ? -33.246 -38.342  1.842   1.00 95.01  ?  297  SER B N   1 
ATOM   3478  C  CA  . SER B 2  297  ? -33.716 -38.002  3.177   1.00 89.82  ?  297  SER B CA  1 
ATOM   3479  C  C   . SER B 2  297  ? -32.587 -38.180  4.174   1.00 89.11  ?  297  SER B C   1 
ATOM   3480  O  O   . SER B 2  297  ? -31.892 -39.206  4.135   1.00 82.72  ?  297  SER B O   1 
ATOM   3481  C  CB  . SER B 2  297  ? -34.901 -38.879  3.575   1.00 82.42  ?  297  SER B CB  1 
ATOM   3482  O  OG  . SER B 2  297  ? -34.545 -40.251  3.589   1.00 77.72  ?  297  SER B OG  1 
ATOM   3483  N  N   . PRO B 2  298  ? -32.361 -37.217  5.066   1.00 91.75  ?  298  PRO B N   1 
ATOM   3484  C  CA  . PRO B 2  298  ? -31.286 -37.370  6.052   1.00 91.58  ?  298  PRO B CA  1 
ATOM   3485  C  C   . PRO B 2  298  ? -31.558 -38.540  6.985   1.00 86.02  ?  298  PRO B C   1 
ATOM   3486  O  O   . PRO B 2  298  ? -32.705 -38.930  7.215   1.00 73.50  ?  298  PRO B O   1 
ATOM   3487  C  CB  . PRO B 2  298  ? -31.297 -36.033  6.804   1.00 86.19  ?  298  PRO B CB  1 
ATOM   3488  C  CG  . PRO B 2  298  ? -32.659 -35.469  6.566   1.00 84.32  ?  298  PRO B CG  1 
ATOM   3489  C  CD  . PRO B 2  298  ? -33.057 -35.926  5.197   1.00 81.89  ?  298  PRO B CD  1 
ATOM   3490  N  N   . SER B 2  299  ? -30.481 -39.106  7.520   1.00 82.42  ?  299  SER B N   1 
ATOM   3491  C  CA  . SER B 2  299  ? -30.572 -40.294  8.356   1.00 75.44  ?  299  SER B CA  1 
ATOM   3492  C  C   . SER B 2  299  ? -29.470 -40.236  9.408   1.00 68.44  ?  299  SER B C   1 
ATOM   3493  O  O   . SER B 2  299  ? -28.822 -39.203  9.600   1.00 66.12  ?  299  SER B O   1 
ATOM   3494  C  CB  . SER B 2  299  ? -30.479 -41.563  7.499   1.00 87.91  ?  299  SER B CB  1 
ATOM   3495  O  OG  . SER B 2  299  ? -29.229 -41.633  6.833   1.00 88.70  ?  299  SER B OG  1 
ATOM   3496  N  N   . THR B 2  300  ? -29.259 -41.362  10.094  1.00 76.42  ?  300  THR B N   1 
ATOM   3497  C  CA  . THR B 2  300  ? -28.211 -41.429  11.106  1.00 73.72  ?  300  THR B CA  1 
ATOM   3498  C  C   . THR B 2  300  ? -26.826 -41.350  10.474  1.00 75.14  ?  300  THR B C   1 
ATOM   3499  O  O   . THR B 2  300  ? -25.906 -40.762  11.054  1.00 74.03  ?  300  THR B O   1 
ATOM   3500  C  CB  . THR B 2  300  ? -28.353 -42.714  11.923  1.00 72.92  ?  300  THR B CB  1 
ATOM   3501  O  OG1 . THR B 2  300  ? -28.184 -43.848  11.065  1.00 85.12  ?  300  THR B OG1 1 
ATOM   3502  C  CG2 . THR B 2  300  ? -29.727 -42.780  12.577  1.00 67.70  ?  300  THR B CG2 1 
ATOM   3503  N  N   . THR B 2  301  ? -26.661 -41.937  9.285   1.00 63.59  ?  301  THR B N   1 
ATOM   3504  C  CA  . THR B 2  301  ? -25.369 -41.894  8.607   1.00 60.15  ?  301  THR B CA  1 
ATOM   3505  C  C   . THR B 2  301  ? -24.999 -40.468  8.219   1.00 52.90  ?  301  THR B C   1 
ATOM   3506  O  O   . THR B 2  301  ? -23.844 -40.053  8.377   1.00 50.13  ?  301  THR B O   1 
ATOM   3507  C  CB  . THR B 2  301  ? -25.393 -42.795  7.371   1.00 73.04  ?  301  THR B CB  1 
ATOM   3508  O  OG1 . THR B 2  301  ? -25.692 -44.141  7.762   1.00 60.59  ?  301  THR B OG1 1 
ATOM   3509  C  CG2 . THR B 2  301  ? -24.047 -42.768  6.660   1.00 77.31  ?  301  THR B CG2 1 
ATOM   3510  N  N   . GLY B 2  302  ? -25.967 -39.702  7.712   1.00 60.21  ?  302  GLY B N   1 
ATOM   3511  C  CA  . GLY B 2  302  ? -25.716 -38.316  7.361   1.00 72.09  ?  302  GLY B CA  1 
ATOM   3512  C  C   . GLY B 2  302  ? -25.331 -37.445  8.538   1.00 65.75  ?  302  GLY B C   1 
ATOM   3513  O  O   . GLY B 2  302  ? -24.687 -36.408  8.346   1.00 66.75  ?  302  GLY B O   1 
ATOM   3514  N  N   . THR B 2  303  ? -25.712 -37.841  9.754   1.00 69.73  ?  303  THR B N   1 
ATOM   3515  C  CA  . THR B 2  303  ? -25.324 -37.084  10.939  1.00 70.27  ?  303  THR B CA  1 
ATOM   3516  C  C   . THR B 2  303  ? -23.817 -37.141  11.157  1.00 68.96  ?  303  THR B C   1 
ATOM   3517  O  O   . THR B 2  303  ? -23.167 -36.107  11.353  1.00 69.11  ?  303  THR B O   1 
ATOM   3518  C  CB  . THR B 2  303  ? -26.065 -37.618  12.167  1.00 74.43  ?  303  THR B CB  1 
ATOM   3519  O  OG1 . THR B 2  303  ? -27.447 -37.249  12.092  1.00 74.56  ?  303  THR B OG1 1 
ATOM   3520  C  CG2 . THR B 2  303  ? -25.456 -37.058  13.446  1.00 79.83  ?  303  THR B CG2 1 
ATOM   3521  N  N   . ALA B 2  304  ? -23.243 -38.341  11.117  1.00 53.79  ?  304  ALA B N   1 
ATOM   3522  C  CA  . ALA B 2  304  ? -21.815 -38.535  11.332  1.00 53.81  ?  304  ALA B CA  1 
ATOM   3523  C  C   . ALA B 2  304  ? -20.974 -38.190  10.110  1.00 60.00  ?  304  ALA B C   1 
ATOM   3524  O  O   . ALA B 2  304  ? -19.785 -38.523  10.084  1.00 64.12  ?  304  ALA B O   1 
ATOM   3525  C  CB  . ALA B 2  304  ? -21.541 -39.981  11.753  1.00 58.44  ?  304  ALA B CB  1 
ATOM   3526  N  N   . ALA B 2  305  ? -21.554 -37.532  9.110   1.00 72.09  ?  305  ALA B N   1 
ATOM   3527  C  CA  . ALA B 2  305  ? -20.846 -37.212  7.879   1.00 69.88  ?  305  ALA B CA  1 
ATOM   3528  C  C   . ALA B 2  305  ? -20.195 -35.839  7.981   1.00 73.51  ?  305  ALA B C   1 
ATOM   3529  O  O   . ALA B 2  305  ? -20.820 -34.879  8.444   1.00 75.42  ?  305  ALA B O   1 
ATOM   3530  C  CB  . ALA B 2  305  ? -21.800 -37.250  6.687   1.00 72.54  ?  305  ALA B CB  1 
ATOM   3531  N  N   . ASP B 2  306  ? -18.938 -35.752  7.541   1.00 94.20  ?  306  ASP B N   1 
ATOM   3532  C  CA  . ASP B 2  306  ? -18.261 -34.462  7.498   1.00 104.55 ?  306  ASP B CA  1 
ATOM   3533  C  C   . ASP B 2  306  ? -18.804 -33.587  6.376   1.00 103.85 ?  306  ASP B C   1 
ATOM   3534  O  O   . ASP B 2  306  ? -18.804 -32.356  6.493   1.00 100.67 ?  306  ASP B O   1 
ATOM   3535  C  CB  . ASP B 2  306  ? -16.755 -34.667  7.336   1.00 99.61  ?  306  ASP B CB  1 
ATOM   3536  C  CG  . ASP B 2  306  ? -16.090 -35.125  8.620   1.00 110.04 ?  306  ASP B CG  1 
ATOM   3537  O  OD1 . ASP B 2  306  ? -16.683 -34.929  9.702   1.00 104.84 ?  306  ASP B OD1 1 
ATOM   3538  O  OD2 . ASP B 2  306  ? -14.976 -35.685  8.545   1.00 118.85 -1 306  ASP B OD2 1 
ATOM   3539  N  N   . HIS B 2  307  ? -19.267 -34.200  5.288   1.00 69.84  ?  307  HIS B N   1 
ATOM   3540  C  CA  . HIS B 2  307  ? -19.888 -33.486  4.180   1.00 72.53  ?  307  HIS B CA  1 
ATOM   3541  C  C   . HIS B 2  307  ? -21.113 -34.263  3.725   1.00 74.13  ?  307  HIS B C   1 
ATOM   3542  O  O   . HIS B 2  307  ? -21.023 -35.466  3.458   1.00 71.99  ?  307  HIS B O   1 
ATOM   3543  C  CB  . HIS B 2  307  ? -18.911 -33.302  3.012   1.00 76.14  ?  307  HIS B CB  1 
ATOM   3544  C  CG  . HIS B 2  307  ? -17.686 -32.517  3.363   1.00 79.84  ?  307  HIS B CG  1 
ATOM   3545  N  ND1 . HIS B 2  307  ? -17.717 -31.162  3.611   1.00 76.05  ?  307  HIS B ND1 1 
ATOM   3546  C  CD2 . HIS B 2  307  ? -16.393 -32.895  3.502   1.00 80.93  ?  307  HIS B CD2 1 
ATOM   3547  C  CE1 . HIS B 2  307  ? -16.497 -30.739  3.890   1.00 82.52  ?  307  HIS B CE1 1 
ATOM   3548  N  NE2 . HIS B 2  307  ? -15.675 -31.771  3.830   1.00 76.73  ?  307  HIS B NE2 1 
ATOM   3549  N  N   . ARG B 2  308  ? -22.250 -33.577  3.636   1.00 74.69  ?  308  ARG B N   1 
ATOM   3550  C  CA  . ARG B 2  308  ? -23.514 -34.195  3.260   1.00 69.01  ?  308  ARG B CA  1 
ATOM   3551  C  C   . ARG B 2  308  ? -24.123 -33.419  2.102   1.00 69.98  ?  308  ARG B C   1 
ATOM   3552  O  O   . ARG B 2  308  ? -24.198 -32.187  2.149   1.00 73.58  ?  308  ARG B O   1 
ATOM   3553  C  CB  . ARG B 2  308  ? -24.484 -34.233  4.446   1.00 71.64  ?  308  ARG B CB  1 
ATOM   3554  C  CG  . ARG B 2  308  ? -25.718 -35.088  4.219   1.00 72.15  ?  308  ARG B CG  1 
ATOM   3555  C  CD  . ARG B 2  308  ? -26.647 -35.029  5.416   1.00 67.18  ?  308  ARG B CD  1 
ATOM   3556  N  NE  . ARG B 2  308  ? -27.329 -33.743  5.487   1.00 70.47  ?  308  ARG B NE  1 
ATOM   3557  C  CZ  . ARG B 2  308  ? -28.468 -33.467  4.869   1.00 76.01  ?  308  ARG B CZ  1 
ATOM   3558  N  NH1 . ARG B 2  308  ? -29.107 -34.381  4.156   1.00 69.22  ?  308  ARG B NH1 1 
ATOM   3559  N  NH2 . ARG B 2  308  ? -28.978 -32.243  4.966   1.00 80.03  ?  308  ARG B NH2 1 
ATOM   3560  N  N   . LEU B 2  309  ? -24.555 -34.138  1.073   1.00 74.06  ?  309  LEU B N   1 
ATOM   3561  C  CA  . LEU B 2  309  ? -25.140 -33.526  -0.120  1.00 76.46  ?  309  LEU B CA  1 
ATOM   3562  C  C   . LEU B 2  309  ? -26.583 -33.979  -0.283  1.00 73.26  ?  309  LEU B C   1 
ATOM   3563  O  O   . LEU B 2  309  ? -26.827 -35.161  -0.593  1.00 73.28  ?  309  LEU B O   1 
ATOM   3564  C  CB  . LEU B 2  309  ? -24.326 -33.885  -1.363  1.00 80.18  ?  309  LEU B CB  1 
ATOM   3565  C  CG  . LEU B 2  309  ? -24.852 -33.354  -2.698  1.00 83.09  ?  309  LEU B CG  1 
ATOM   3566  C  CD1 . LEU B 2  309  ? -24.567 -31.866  -2.841  1.00 84.42  ?  309  LEU B CD1 1 
ATOM   3567  C  CD2 . LEU B 2  309  ? -24.253 -34.134  -3.858  1.00 82.53  ?  309  LEU B CD2 1 
ATOM   3568  N  N   . PRO B 2  310  ? -27.568 -33.099  -0.088  1.00 65.44  ?  310  PRO B N   1 
ATOM   3569  C  CA  . PRO B 2  310  ? -28.990 -33.483  -0.246  1.00 70.88  ?  310  PRO B CA  1 
ATOM   3570  C  C   . PRO B 2  310  ? -29.430 -33.548  -1.708  1.00 82.86  ?  310  PRO B C   1 
ATOM   3571  O  O   . PRO B 2  310  ? -30.094 -32.665  -2.251  1.00 87.07  ?  310  PRO B O   1 
ATOM   3572  C  CB  . PRO B 2  310  ? -29.727 -32.380  0.522   1.00 75.62  ?  310  PRO B CB  1 
ATOM   3573  C  CG  . PRO B 2  310  ? -28.661 -31.568  1.231   1.00 84.47  ?  310  PRO B CG  1 
ATOM   3574  C  CD  . PRO B 2  310  ? -27.428 -31.727  0.417   1.00 71.18  ?  310  PRO B CD  1 
ATOM   3575  N  N   . LEU B 2  311  ? -29.045 -34.632  -2.371  1.00 74.10  ?  311  LEU B N   1 
ATOM   3576  C  CA  . LEU B 2  311  ? -29.434 -34.875  -3.752  1.00 80.20  ?  311  LEU B CA  1 
ATOM   3577  C  C   . LEU B 2  311  ? -30.752 -35.641  -3.804  1.00 79.64  ?  311  LEU B C   1 
ATOM   3578  O  O   . LEU B 2  311  ? -31.154 -36.298  -2.842  1.00 74.40  ?  311  LEU B O   1 
ATOM   3579  C  CB  . LEU B 2  311  ? -28.343 -35.654  -4.487  1.00 80.95  ?  311  LEU B CB  1 
ATOM   3580  C  CG  . LEU B 2  311  ? -28.318 -35.558  -6.014  1.00 78.04  ?  311  LEU B CG  1 
ATOM   3581  C  CD1 . LEU B 2  311  ? -28.236 -34.107  -6.462  1.00 78.76  ?  311  LEU B CD1 1 
ATOM   3582  C  CD2 . LEU B 2  311  ? -27.163 -36.370  -6.580  1.00 74.72  ?  311  LEU B CD2 1 
ATOM   3583  N  N   . ARG B 2  312  ? -31.428 -35.547  -4.945  1.00 85.63  ?  312  ARG B N   1 
ATOM   3584  C  CA  . ARG B 2  312  ? -32.672 -36.280  -5.118  1.00 82.78  ?  312  ARG B CA  1 
ATOM   3585  C  C   . ARG B 2  312  ? -32.396 -37.777  -5.212  1.00 87.63  ?  312  ARG B C   1 
ATOM   3586  O  O   . ARG B 2  312  ? -31.284 -38.214  -5.514  1.00 93.24  ?  312  ARG B O   1 
ATOM   3587  C  CB  . ARG B 2  312  ? -33.417 -35.802  -6.364  1.00 85.25  ?  312  ARG B CB  1 
ATOM   3588  C  CG  . ARG B 2  312  ? -34.615 -34.918  -6.053  1.00 98.87  ?  312  ARG B CG  1 
ATOM   3589  C  CD  . ARG B 2  312  ? -35.375 -34.529  -7.308  1.00 85.28  ?  312  ARG B CD  1 
ATOM   3590  N  NE  . ARG B 2  312  ? -35.913 -35.698  -7.991  1.00 82.86  ?  312  ARG B NE  1 
ATOM   3591  C  CZ  . ARG B 2  312  ? -36.834 -35.651  -8.943  1.00 88.50  ?  312  ARG B CZ  1 
ATOM   3592  N  NH1 . ARG B 2  312  ? -37.354 -34.503  -9.346  1.00 102.92 ?  312  ARG B NH1 1 
ATOM   3593  N  NH2 . ARG B 2  312  ? -37.247 -36.785  -9.501  1.00 88.13  ?  312  ARG B NH2 1 
ATOM   3594  N  N   . ALA B 2  313  ? -33.438 -38.570  -4.949  1.00 84.56  ?  313  ALA B N   1 
ATOM   3595  C  CA  . ALA B 2  313  ? -33.267 -40.018  -4.905  1.00 80.37  ?  313  ALA B CA  1 
ATOM   3596  C  C   . ALA B 2  313  ? -33.016 -40.608  -6.288  1.00 85.60  ?  313  ALA B C   1 
ATOM   3597  O  O   . ALA B 2  313  ? -32.341 -41.636  -6.407  1.00 82.48  ?  313  ALA B O   1 
ATOM   3598  C  CB  . ALA B 2  313  ? -34.491 -40.670  -4.264  1.00 75.31  ?  313  ALA B CB  1 
ATOM   3599  N  N   . ASP B 2  314  ? -33.543 -39.978  -7.340  1.00 100.93 ?  314  ASP B N   1 
ATOM   3600  C  CA  . ASP B 2  314  ? -33.365 -40.510  -8.687  1.00 88.07  ?  314  ASP B CA  1 
ATOM   3601  C  C   . ASP B 2  314  ? -32.032 -40.102  -9.299  1.00 90.93  ?  314  ASP B C   1 
ATOM   3602  O  O   . ASP B 2  314  ? -31.474 -40.851  -10.108 1.00 100.97 ?  314  ASP B O   1 
ATOM   3603  C  CB  . ASP B 2  314  ? -34.511 -40.053  -9.591  1.00 91.77  ?  314  ASP B CB  1 
ATOM   3604  C  CG  . ASP B 2  314  ? -35.868 -40.487  -9.076  1.00 109.06 ?  314  ASP B CG  1 
ATOM   3605  O  OD1 . ASP B 2  314  ? -35.917 -41.393  -8.217  1.00 103.57 ?  314  ASP B OD1 1 
ATOM   3606  O  OD2 . ASP B 2  314  ? -36.885 -39.923  -9.533  1.00 113.14 -1 314  ASP B OD2 1 
ATOM   3607  N  N   . ALA B 2  315  ? -31.509 -38.934  -8.934  1.00 108.33 ?  315  ALA B N   1 
ATOM   3608  C  CA  . ALA B 2  315  ? -30.272 -38.428  -9.517  1.00 108.44 ?  315  ALA B CA  1 
ATOM   3609  C  C   . ALA B 2  315  ? -29.024 -39.085  -8.943  1.00 108.63 ?  315  ALA B C   1 
ATOM   3610  O  O   . ALA B 2  315  ? -27.914 -38.711  -9.337  1.00 112.07 ?  315  ALA B O   1 
ATOM   3611  C  CB  . ALA B 2  315  ? -30.185 -36.911  -9.328  1.00 102.59 ?  315  ALA B CB  1 
ATOM   3612  N  N   . ILE B 2  316  ? -29.171 -40.048  -8.034  1.00 90.80  ?  316  ILE B N   1 
ATOM   3613  C  CA  . ILE B 2  316  ? -28.001 -40.679  -7.434  1.00 88.81  ?  316  ILE B CA  1 
ATOM   3614  C  C   . ILE B 2  316  ? -27.364 -41.679  -8.396  1.00 86.89  ?  316  ILE B C   1 
ATOM   3615  O  O   . ILE B 2  316  ? -26.143 -41.876  -8.372  1.00 82.42  ?  316  ILE B O   1 
ATOM   3616  C  CB  . ILE B 2  316  ? -28.392 -41.328  -6.095  1.00 85.26  ?  316  ILE B CB  1 
ATOM   3617  C  CG1 . ILE B 2  316  ? -28.881 -40.247  -5.128  1.00 85.01  ?  316  ILE B CG1 1 
ATOM   3618  C  CG2 . ILE B 2  316  ? -27.214 -42.075  -5.486  1.00 79.29  ?  316  ILE B CG2 1 
ATOM   3619  C  CD1 . ILE B 2  316  ? -29.511 -40.777  -3.867  1.00 82.31  ?  316  ILE B CD1 1 
ATOM   3620  N  N   . ALA B 2  317  ? -28.160 -42.308  -9.263  1.00 86.75  ?  317  ALA B N   1 
ATOM   3621  C  CA  . ALA B 2  317  ? -27.589 -43.182  -10.284 1.00 85.18  ?  317  ALA B CA  1 
ATOM   3622  C  C   . ALA B 2  317  ? -26.745 -42.387  -11.271 1.00 85.98  ?  317  ALA B C   1 
ATOM   3623  O  O   . ALA B 2  317  ? -25.641 -42.807  -11.638 1.00 85.21  ?  317  ALA B O   1 
ATOM   3624  C  CB  . ALA B 2  317  ? -28.701 -43.937  -11.012 1.00 79.09  ?  317  ALA B CB  1 
ATOM   3625  N  N   . ALA B 2  318  ? -27.252 -41.234  -11.713 1.00 79.81  ?  318  ALA B N   1 
ATOM   3626  C  CA  . ALA B 2  318  ? -26.465 -40.361  -12.575 1.00 80.78  ?  318  ALA B CA  1 
ATOM   3627  C  C   . ALA B 2  318  ? -25.273 -39.774  -11.832 1.00 79.77  ?  318  ALA B C   1 
ATOM   3628  O  O   . ALA B 2  318  ? -24.225 -39.525  -12.440 1.00 83.14  ?  318  ALA B O   1 
ATOM   3629  C  CB  . ALA B 2  318  ? -27.346 -39.246  -13.138 1.00 85.16  ?  318  ALA B CB  1 
ATOM   3630  N  N   . PHE B 2  319  ? -25.413 -39.548  -10.523 1.00 93.99  ?  319  PHE B N   1 
ATOM   3631  C  CA  . PHE B 2  319  ? -24.286 -39.082  -9.721  1.00 95.87  ?  319  PHE B CA  1 
ATOM   3632  C  C   . PHE B 2  319  ? -23.171 -40.120  -9.690  1.00 91.56  ?  319  PHE B C   1 
ATOM   3633  O  O   . PHE B 2  319  ? -21.990 -39.780  -9.826  1.00 89.63  ?  319  PHE B O   1 
ATOM   3634  C  CB  . PHE B 2  319  ? -24.765 -38.748  -8.306  1.00 85.32  ?  319  PHE B CB  1 
ATOM   3635  C  CG  . PHE B 2  319  ? -23.711 -38.128  -7.430  1.00 78.21  ?  319  PHE B CG  1 
ATOM   3636  C  CD1 . PHE B 2  319  ? -22.867 -38.921  -6.667  1.00 80.34  ?  319  PHE B CD1 1 
ATOM   3637  C  CD2 . PHE B 2  319  ? -23.571 -36.752  -7.362  1.00 78.77  ?  319  PHE B CD2 1 
ATOM   3638  C  CE1 . PHE B 2  319  ? -21.900 -38.352  -5.859  1.00 81.53  ?  319  PHE B CE1 1 
ATOM   3639  C  CE2 . PHE B 2  319  ? -22.607 -36.177  -6.556  1.00 87.81  ?  319  PHE B CE2 1 
ATOM   3640  C  CZ  . PHE B 2  319  ? -21.771 -36.978  -5.802  1.00 86.78  ?  319  PHE B CZ  1 
ATOM   3641  N  N   . THR B 2  320  ? -23.530 -41.395  -9.516  1.00 87.94  ?  320  THR B N   1 
ATOM   3642  C  CA  . THR B 2  320  ? -22.530 -42.458  -9.526  1.00 89.70  ?  320  THR B CA  1 
ATOM   3643  C  C   . THR B 2  320  ? -21.872 -42.585  -10.894 1.00 91.53  ?  320  THR B C   1 
ATOM   3644  O  O   . THR B 2  320  ? -20.667 -42.847  -10.991 1.00 83.40  ?  320  THR B O   1 
ATOM   3645  C  CB  . THR B 2  320  ? -23.172 -43.783  -9.117  1.00 84.45  ?  320  THR B CB  1 
ATOM   3646  O  OG1 . THR B 2  320  ? -23.948 -43.592  -7.927  1.00 83.63  ?  320  THR B OG1 1 
ATOM   3647  C  CG2 . THR B 2  320  ? -22.106 -44.839  -8.864  1.00 80.94  ?  320  THR B CG2 1 
ATOM   3648  N  N   . GLY B 2  321  ? -22.649 -42.409  -11.965 1.00 117.06 ?  321  GLY B N   1 
ATOM   3649  C  CA  . GLY B 2  321  ? -22.068 -42.449  -13.297 1.00 116.08 ?  321  GLY B CA  1 
ATOM   3650  C  C   . GLY B 2  321  ? -21.091 -41.315  -13.537 1.00 119.80 ?  321  GLY B C   1 
ATOM   3651  O  O   . GLY B 2  321  ? -20.041 -41.507  -14.154 1.00 125.44 ?  321  GLY B O   1 
ATOM   3652  N  N   . ALA B 2  322  ? -21.421 -40.117  -13.047 1.00 96.33  ?  322  ALA B N   1 
ATOM   3653  C  CA  . ALA B 2  322  ? -20.506 -38.989  -13.180 1.00 97.05  ?  322  ALA B CA  1 
ATOM   3654  C  C   . ALA B 2  322  ? -19.261 -39.185  -12.324 1.00 95.45  ?  322  ALA B C   1 
ATOM   3655  O  O   . ALA B 2  322  ? -18.161 -38.777  -12.714 1.00 98.40  ?  322  ALA B O   1 
ATOM   3656  C  CB  . ALA B 2  322  ? -21.219 -37.690  -12.806 1.00 101.45 ?  322  ALA B CB  1 
ATOM   3657  N  N   . LEU B 2  323  ? -19.416 -39.808  -11.153 1.00 94.43  ?  323  LEU B N   1 
ATOM   3658  C  CA  . LEU B 2  323  ? -18.262 -40.091  -10.306 1.00 95.94  ?  323  LEU B CA  1 
ATOM   3659  C  C   . LEU B 2  323  ? -17.323 -41.094  -10.964 1.00 90.54  ?  323  LEU B C   1 
ATOM   3660  O  O   . LEU B 2  323  ? -16.101 -40.907  -10.953 1.00 91.78  ?  323  LEU B O   1 
ATOM   3661  C  CB  . LEU B 2  323  ? -18.722 -40.605  -8.942  1.00 90.97  ?  323  LEU B CB  1 
ATOM   3662  C  CG  . LEU B 2  323  ? -17.597 -40.824  -7.930  1.00 76.08  ?  323  LEU B CG  1 
ATOM   3663  C  CD1 . LEU B 2  323  ? -16.717 -39.587  -7.822  1.00 76.45  ?  323  LEU B CD1 1 
ATOM   3664  C  CD2 . LEU B 2  323  ? -18.163 -41.207  -6.572  1.00 82.95  ?  323  LEU B CD2 1 
ATOM   3665  N  N   . ALA B 2  324  ? -17.873 -42.168  -11.537 1.00 58.85  ?  324  ALA B N   1 
ATOM   3666  C  CA  . ALA B 2  324  ? -17.041 -43.126  -12.256 1.00 65.67  ?  324  ALA B CA  1 
ATOM   3667  C  C   . ALA B 2  324  ? -16.375 -42.489  -13.469 1.00 74.65  ?  324  ALA B C   1 
ATOM   3668  O  O   . ALA B 2  324  ? -15.233 -42.827  -13.799 1.00 75.88  ?  324  ALA B O   1 
ATOM   3669  C  CB  . ALA B 2  324  ? -17.878 -44.332  -12.680 1.00 65.60  ?  324  ALA B CB  1 
ATOM   3670  N  N   . ASN B 2  325  ? -17.065 -41.559  -14.134 1.00 108.46 ?  325  ASN B N   1 
ATOM   3671  C  CA  . ASN B 2  325  ? -16.500 -40.908  -15.312 1.00 105.42 ?  325  ASN B CA  1 
ATOM   3672  C  C   . ASN B 2  325  ? -15.353 -39.975  -14.947 1.00 108.84 ?  325  ASN B C   1 
ATOM   3673  O  O   . ASN B 2  325  ? -14.395 -39.847  -15.716 1.00 114.29 ?  325  ASN B O   1 
ATOM   3674  C  CB  . ASN B 2  325  ? -17.597 -40.145  -16.060 1.00 109.13 ?  325  ASN B CB  1 
ATOM   3675  C  CG  . ASN B 2  325  ? -17.121 -39.575  -17.389 1.00 112.57 ?  325  ASN B CG  1 
ATOM   3676  O  OD1 . ASN B 2  325  ? -16.350 -38.615  -17.429 1.00 116.22 ?  325  ASN B OD1 1 
ATOM   3677  N  ND2 . ASN B 2  325  ? -17.586 -40.163  -18.485 1.00 108.26 ?  325  ASN B ND2 1 
ATOM   3678  N  N   . GLU B 2  326  ? -15.426 -39.323  -13.784 1.00 102.91 ?  326  GLU B N   1 
ATOM   3679  C  CA  . GLU B 2  326  ? -14.388 -38.368  -13.410 1.00 102.38 ?  326  GLU B CA  1 
ATOM   3680  C  C   . GLU B 2  326  ? -13.087 -39.062  -13.025 1.00 102.87 ?  326  GLU B C   1 
ATOM   3681  O  O   . GLU B 2  326  ? -12.002 -38.523  -13.274 1.00 99.83  ?  326  GLU B O   1 
ATOM   3682  C  CB  . GLU B 2  326  ? -14.878 -37.480  -12.266 1.00 102.22 ?  326  GLU B CB  1 
ATOM   3683  C  CG  . GLU B 2  326  ? -13.892 -36.395  -11.863 1.00 111.13 ?  326  GLU B CG  1 
ATOM   3684  C  CD  . GLU B 2  326  ? -14.557 -35.055  -11.627 1.00 117.09 ?  326  GLU B CD  1 
ATOM   3685  O  OE1 . GLU B 2  326  ? -15.803 -34.991  -11.680 1.00 120.00 ?  326  GLU B OE1 1 
ATOM   3686  O  OE2 . GLU B 2  326  ? -13.833 -34.063  -11.393 1.00 112.29 -1 326  GLU B OE2 1 
ATOM   3687  N  N   . LEU B 2  327  ? -13.170 -40.250  -12.426 1.00 92.41  ?  327  LEU B N   1 
ATOM   3688  C  CA  . LEU B 2  327  ? -11.979 -40.991  -12.030 1.00 94.41  ?  327  LEU B CA  1 
ATOM   3689  C  C   . LEU B 2  327  ? -11.266 -41.645  -13.207 1.00 95.83  ?  327  LEU B C   1 
ATOM   3690  O  O   . LEU B 2  327  ? -10.283 -42.364  -12.992 1.00 99.78  ?  327  LEU B O   1 
ATOM   3691  C  CB  . LEU B 2  327  ? -12.342 -42.061  -10.995 1.00 95.51  ?  327  LEU B CB  1 
ATOM   3692  C  CG  . LEU B 2  327  ? -12.919 -41.585  -9.657  1.00 88.67  ?  327  LEU B CG  1 
ATOM   3693  C  CD1 . LEU B 2  327  ? -13.440 -42.763  -8.841  1.00 74.20  ?  327  LEU B CD1 1 
ATOM   3694  C  CD2 . LEU B 2  327  ? -11.885 -40.800  -8.865  1.00 82.67  ?  327  LEU B CD2 1 
ATOM   3695  N  N   . GLY B 2  328  ? -11.727 -41.416  -14.433 1.00 106.67 ?  328  GLY B N   1 
ATOM   3696  C  CA  . GLY B 2  328  ? -11.129 -42.029  -15.600 1.00 107.11 ?  328  GLY B CA  1 
ATOM   3697  C  C   . GLY B 2  328  ? -11.642 -43.409  -15.934 1.00 106.13 ?  328  GLY B C   1 
ATOM   3698  O  O   . GLY B 2  328  ? -11.025 -44.100  -16.752 1.00 105.24 ?  328  GLY B O   1 
ATOM   3699  N  N   . VAL B 2  329  ? -12.745 -43.835  -15.329 1.00 117.84 ?  329  VAL B N   1 
ATOM   3700  C  CA  . VAL B 2  329  ? -13.302 -45.158  -15.557 1.00 122.06 ?  329  VAL B CA  1 
ATOM   3701  C  C   . VAL B 2  329  ? -14.596 -45.001  -16.348 1.00 123.16 ?  329  VAL B C   1 
ATOM   3702  O  O   . VAL B 2  329  ? -15.229 -43.941  -16.348 1.00 123.71 ?  329  VAL B O   1 
ATOM   3703  C  CB  . VAL B 2  329  ? -13.539 -45.908  -14.227 1.00 113.65 ?  329  VAL B CB  1 
ATOM   3704  C  CG1 . VAL B 2  329  ? -13.812 -47.384  -14.472 1.00 111.42 ?  329  VAL B CG1 1 
ATOM   3705  C  CG2 . VAL B 2  329  ? -12.346 -45.726  -13.294 1.00 103.64 ?  329  VAL B CG2 1 
ATOM   3706  N  N   . GLY B 2  330  ? -14.983 -46.073  -17.039 1.00 144.03 ?  330  GLY B N   1 
ATOM   3707  C  CA  . GLY B 2  330  ? -16.178 -46.070  -17.861 1.00 149.89 ?  330  GLY B CA  1 
ATOM   3708  C  C   . GLY B 2  330  ? -17.443 -45.657  -17.135 1.00 125.10 ?  330  GLY B C   1 
ATOM   3709  O  O   . GLY B 2  330  ? -17.818 -46.261  -16.127 1.00 125.18 ?  330  GLY B O   1 
ATOM   3710  N  N   . GLY B 2  331  ? -18.101 -44.630  -17.640 1.00 87.59  ?  331  GLY B N   1 
ATOM   3711  C  CA  . GLY B 2  331  ? -19.329 -44.138  -17.047 1.00 84.27  ?  331  GLY B CA  1 
ATOM   3712  C  C   . GLY B 2  331  ? -20.055 -43.232  -18.015 1.00 95.65  ?  331  GLY B C   1 
ATOM   3713  O  O   . GLY B 2  331  ? -19.963 -43.396  -19.234 1.00 114.99 ?  331  GLY B O   1 
ATOM   3714  N  N   . ALA B 2  332  ? -20.781 -42.262  -17.467 1.00 88.91  ?  332  ALA B N   1 
ATOM   3715  C  CA  . ALA B 2  332  ? -21.533 -41.325  -18.292 1.00 96.56  ?  332  ALA B CA  1 
ATOM   3716  C  C   . ALA B 2  332  ? -21.624 -39.969  -17.604 1.00 89.87  ?  332  ALA B C   1 
ATOM   3717  O  O   . ALA B 2  332  ? -22.083 -39.884  -16.458 1.00 93.55  ?  332  ALA B O   1 
ATOM   3718  C  CB  . ALA B 2  332  ? -22.932 -41.869  -18.585 1.00 98.32  ?  332  ALA B CB  1 
ATOM   3719  N  N   . PRO B 2  333  ? -21.191 -38.894  -18.260 1.00 82.82  ?  333  PRO B N   1 
ATOM   3720  C  CA  . PRO B 2  333  ? -21.329 -37.563  -17.661 1.00 84.35  ?  333  PRO B CA  1 
ATOM   3721  C  C   . PRO B 2  333  ? -22.791 -37.172  -17.521 1.00 83.96  ?  333  PRO B C   1 
ATOM   3722  O  O   . PRO B 2  333  ? -23.646 -37.565  -18.319 1.00 85.86  ?  333  PRO B O   1 
ATOM   3723  C  CB  . PRO B 2  333  ? -20.601 -36.645  -18.652 1.00 92.72  ?  333  PRO B CB  1 
ATOM   3724  C  CG  . PRO B 2  333  ? -19.727 -37.558  -19.458 1.00 90.87  ?  333  PRO B CG  1 
ATOM   3725  C  CD  . PRO B 2  333  ? -20.472 -38.852  -19.543 1.00 89.22  ?  333  PRO B CD  1 
ATOM   3726  N  N   . ALA B 2  334  ? -23.072 -36.385  -16.486 1.00 85.08  ?  334  ALA B N   1 
ATOM   3727  C  CA  . ALA B 2  334  ? -24.429 -35.962  -16.177 1.00 97.44  ?  334  ALA B CA  1 
ATOM   3728  C  C   . ALA B 2  334  ? -24.450 -34.472  -15.875 1.00 96.08  ?  334  ALA B C   1 
ATOM   3729  O  O   . ALA B 2  334  ? -23.528 -33.942  -15.248 1.00 91.19  ?  334  ALA B O   1 
ATOM   3730  C  CB  . ALA B 2  334  ? -24.998 -36.744  -14.987 1.00 93.55  ?  334  ALA B CB  1 
ATOM   3731  N  N   . THR B 2  335  ? -25.506 -33.801  -16.329 1.00 128.34 ?  335  THR B N   1 
ATOM   3732  C  CA  . THR B 2  335  ? -25.711 -32.389  -16.028 1.00 134.70 ?  335  THR B CA  1 
ATOM   3733  C  C   . THR B 2  335  ? -26.197 -32.270  -14.589 1.00 127.25 ?  335  THR B C   1 
ATOM   3734  O  O   . THR B 2  335  ? -27.317 -32.681  -14.268 1.00 124.89 ?  335  THR B O   1 
ATOM   3735  C  CB  . THR B 2  335  ? -26.711 -31.769  -17.001 1.00 135.82 ?  335  THR B CB  1 
ATOM   3736  O  OG1 . THR B 2  335  ? -27.900 -32.568  -17.040 1.00 140.75 ?  335  THR B OG1 1 
ATOM   3737  C  CG2 . THR B 2  335  ? -26.114 -31.692  -18.400 1.00 128.82 ?  335  THR B CG2 1 
ATOM   3738  N  N   . LEU B 2  336  ? -25.358 -31.713  -13.720 1.00 115.67 ?  336  LEU B N   1 
ATOM   3739  C  CA  . LEU B 2  336  ? -25.650 -31.628  -12.298 1.00 112.50 ?  336  LEU B CA  1 
ATOM   3740  C  C   . LEU B 2  336  ? -25.507 -30.187  -11.826 1.00 113.77 ?  336  LEU B C   1 
ATOM   3741  O  O   . LEU B 2  336  ? -24.955 -29.329  -12.522 1.00 117.58 ?  336  LEU B O   1 
ATOM   3742  C  CB  . LEU B 2  336  ? -24.731 -32.550  -11.487 1.00 104.23 ?  336  LEU B CB  1 
ATOM   3743  C  CG  . LEU B 2  336  ? -24.955 -34.049  -11.696 1.00 99.80  ?  336  LEU B CG  1 
ATOM   3744  C  CD1 . LEU B 2  336  ? -24.007 -34.862  -10.830 1.00 99.40  ?  336  LEU B CD1 1 
ATOM   3745  C  CD2 . LEU B 2  336  ? -26.402 -34.422  -11.412 1.00 91.23  ?  336  LEU B CD2 1 
ATOM   3746  N  N   . SER B 2  337  ? -26.016 -29.931  -10.624 1.00 89.20  ?  337  SER B N   1 
ATOM   3747  C  CA  . SER B 2  337  ? -25.939 -28.608  -10.033 1.00 89.58  ?  337  SER B CA  1 
ATOM   3748  C  C   . SER B 2  337  ? -24.490 -28.259  -9.697  1.00 90.63  ?  337  SER B C   1 
ATOM   3749  O  O   . SER B 2  337  ? -23.646 -29.146  -9.547  1.00 95.72  ?  337  SER B O   1 
ATOM   3750  C  CB  . SER B 2  337  ? -26.807 -28.543  -8.777  1.00 98.46  ?  337  SER B CB  1 
ATOM   3751  O  OG  . SER B 2  337  ? -26.148 -29.125  -7.666  1.00 94.65  ?  337  SER B OG  1 
ATOM   3752  N  N   . PRO B 2  338  ? -24.172 -26.965  -9.593  1.00 101.75 ?  338  PRO B N   1 
ATOM   3753  C  CA  . PRO B 2  338  ? -22.803 -26.582  -9.206  1.00 102.97 ?  338  PRO B CA  1 
ATOM   3754  C  C   . PRO B 2  338  ? -22.380 -27.130  -7.854  1.00 104.23 ?  338  PRO B C   1 
ATOM   3755  O  O   . PRO B 2  338  ? -21.196 -27.437  -7.667  1.00 103.26 ?  338  PRO B O   1 
ATOM   3756  C  CB  . PRO B 2  338  ? -22.859 -25.048  -9.204  1.00 104.81 ?  338  PRO B CB  1 
ATOM   3757  C  CG  . PRO B 2  338  ? -23.962 -24.715  -10.151 1.00 102.68 ?  338  PRO B CG  1 
ATOM   3758  C  CD  . PRO B 2  338  ? -24.988 -25.793  -9.957  1.00 103.57 ?  338  PRO B CD  1 
ATOM   3759  N  N   . LYS B 2  339  ? -23.309 -27.260  -6.902  1.00 100.76 ?  339  LYS B N   1 
ATOM   3760  C  CA  . LYS B 2  339  ? -22.969 -27.881  -5.626  1.00 97.68  ?  339  LYS B CA  1 
ATOM   3761  C  C   . LYS B 2  339  ? -22.604 -29.348  -5.810  1.00 97.09  ?  339  LYS B C   1 
ATOM   3762  O  O   . LYS B 2  339  ? -21.629 -29.832  -5.223  1.00 101.13 ?  339  LYS B O   1 
ATOM   3763  C  CB  . LYS B 2  339  ? -24.128 -27.739  -4.638  1.00 113.41 ?  339  LYS B CB  1 
ATOM   3764  C  CG  . LYS B 2  339  ? -24.102 -26.456  -3.822  1.00 127.86 ?  339  LYS B CG  1 
ATOM   3765  C  CD  . LYS B 2  339  ? -24.862 -26.625  -2.514  1.00 118.30 ?  339  LYS B CD  1 
ATOM   3766  C  CE  . LYS B 2  339  ? -24.647 -25.439  -1.588  1.00 120.09 ?  339  LYS B CE  1 
ATOM   3767  N  NZ  . LYS B 2  339  ? -25.824 -24.529  -1.562  1.00 139.20 ?  339  LYS B NZ  1 
ATOM   3768  N  N   . ALA B 2  340  ? -23.377 -30.073  -6.623  1.00 74.03  ?  340  ALA B N   1 
ATOM   3769  C  CA  . ALA B 2  340  ? -23.050 -31.466  -6.904  1.00 66.89  ?  340  ALA B CA  1 
ATOM   3770  C  C   . ALA B 2  340  ? -21.758 -31.589  -7.702  1.00 73.93  ?  340  ALA B C   1 
ATOM   3771  O  O   . ALA B 2  340  ? -21.042 -32.588  -7.570  1.00 71.98  ?  340  ALA B O   1 
ATOM   3772  C  CB  . ALA B 2  340  ? -24.204 -32.139  -7.647  1.00 62.81  ?  340  ALA B CB  1 
ATOM   3773  N  N   . GLU B 2  341  ? -21.444 -30.590  -8.531  1.00 119.44 ?  341  GLU B N   1 
ATOM   3774  C  CA  . GLU B 2  341  ? -20.185 -30.610  -9.269  1.00 116.27 ?  341  GLU B CA  1 
ATOM   3775  C  C   . GLU B 2  341  ? -18.996 -30.430  -8.334  1.00 115.28 ?  341  GLU B C   1 
ATOM   3776  O  O   . GLU B 2  341  ? -17.985 -31.131  -8.465  1.00 115.79 ?  341  GLU B O   1 
ATOM   3777  C  CB  . GLU B 2  341  ? -20.192 -29.525  -10.346 1.00 131.43 ?  341  GLU B CB  1 
ATOM   3778  C  CG  . GLU B 2  341  ? -19.255 -29.797  -11.511 1.00 133.75 ?  341  GLU B CG  1 
ATOM   3779  C  CD  . GLU B 2  341  ? -19.900 -30.644  -12.589 1.00 136.53 ?  341  GLU B CD  1 
ATOM   3780  O  OE1 . GLU B 2  341  ? -21.131 -30.845  -12.530 1.00 134.20 ?  341  GLU B OE1 1 
ATOM   3781  O  OE2 . GLU B 2  341  ? -19.177 -31.107  -13.497 1.00 147.01 -1 341  GLU B OE2 1 
ATOM   3782  N  N   . GLU B 2  342  ? -19.097 -29.495  -7.385  1.00 107.27 ?  342  GLU B N   1 
ATOM   3783  C  CA  . GLU B 2  342  ? -18.033 -29.319  -6.402  1.00 109.01 ?  342  GLU B CA  1 
ATOM   3784  C  C   . GLU B 2  342  ? -17.915 -30.530  -5.486  1.00 103.65 ?  342  GLU B C   1 
ATOM   3785  O  O   . GLU B 2  342  ? -16.818 -30.841  -5.008  1.00 100.09 ?  342  GLU B O   1 
ATOM   3786  C  CB  . GLU B 2  342  ? -18.282 -28.054  -5.580  1.00 105.86 ?  342  GLU B CB  1 
ATOM   3787  C  CG  . GLU B 2  342  ? -17.992 -26.761  -6.323  1.00 116.37 ?  342  GLU B CG  1 
ATOM   3788  C  CD  . GLU B 2  342  ? -18.076 -25.544  -5.424  1.00 128.30 ?  342  GLU B CD  1 
ATOM   3789  O  OE1 . GLU B 2  342  ? -18.472 -25.699  -4.249  1.00 131.55 ?  342  GLU B OE1 1 
ATOM   3790  O  OE2 . GLU B 2  342  ? -17.750 -24.432  -5.892  1.00 125.59 -1 342  GLU B OE2 1 
ATOM   3791  N  N   . PHE B 2  343  ? -19.029 -31.220  -5.231  1.00 96.00  ?  343  PHE B N   1 
ATOM   3792  C  CA  . PHE B 2  343  ? -18.987 -32.419  -4.402  1.00 90.73  ?  343  PHE B CA  1 
ATOM   3793  C  C   . PHE B 2  343  ? -18.316 -33.571  -5.142  1.00 92.91  ?  343  PHE B C   1 
ATOM   3794  O  O   . PHE B 2  343  ? -17.517 -34.311  -4.555  1.00 92.94  ?  343  PHE B O   1 
ATOM   3795  C  CB  . PHE B 2  343  ? -20.404 -32.793  -3.967  1.00 92.34  ?  343  PHE B CB  1 
ATOM   3796  C  CG  . PHE B 2  343  ? -20.464 -33.601  -2.703  1.00 84.92  ?  343  PHE B CG  1 
ATOM   3797  C  CD1 . PHE B 2  343  ? -20.351 -32.983  -1.469  1.00 82.27  ?  343  PHE B CD1 1 
ATOM   3798  C  CD2 . PHE B 2  343  ? -20.651 -34.972  -2.745  1.00 91.28  ?  343  PHE B CD2 1 
ATOM   3799  C  CE1 . PHE B 2  343  ? -20.413 -33.716  -0.301  1.00 79.80  ?  343  PHE B CE1 1 
ATOM   3800  C  CE2 . PHE B 2  343  ? -20.714 -35.712  -1.577  1.00 93.15  ?  343  PHE B CE2 1 
ATOM   3801  C  CZ  . PHE B 2  343  ? -20.594 -35.082  -0.355  1.00 85.41  ?  343  PHE B CZ  1 
ATOM   3802  N  N   . LEU B 2  344  ? -18.626 -33.735  -6.432  1.00 68.72  ?  344  LEU B N   1 
ATOM   3803  C  CA  . LEU B 2  344  ? -17.915 -34.709  -7.256  1.00 60.92  ?  344  LEU B CA  1 
ATOM   3804  C  C   . LEU B 2  344  ? -16.426 -34.396  -7.314  1.00 68.54  ?  344  LEU B C   1 
ATOM   3805  O  O   . LEU B 2  344  ? -15.590 -35.307  -7.280  1.00 64.76  ?  344  LEU B O   1 
ATOM   3806  C  CB  . LEU B 2  344  ? -18.500 -34.735  -8.668  1.00 73.04  ?  344  LEU B CB  1 
ATOM   3807  C  CG  . LEU B 2  344  ? -19.869 -35.375  -8.891  1.00 77.10  ?  344  LEU B CG  1 
ATOM   3808  C  CD1 . LEU B 2  344  ? -20.353 -35.084  -10.298 1.00 78.41  ?  344  LEU B CD1 1 
ATOM   3809  C  CD2 . LEU B 2  344  ? -19.778 -36.873  -8.668  1.00 74.71  ?  344  LEU B CD2 1 
ATOM   3810  N  N   . ARG B 2  345  ? -16.078 -33.110  -7.412  1.00 104.67 ?  345  ARG B N   1 
ATOM   3811  C  CA  . ARG B 2  345  ? -14.674 -32.714  -7.438  1.00 108.74 ?  345  ARG B CA  1 
ATOM   3812  C  C   . ARG B 2  345  ? -13.950 -33.200  -6.190  1.00 107.79 ?  345  ARG B C   1 
ATOM   3813  O  O   . ARG B 2  345  ? -12.903 -33.851  -6.279  1.00 106.18 ?  345  ARG B O   1 
ATOM   3814  C  CB  . ARG B 2  345  ? -14.563 -31.193  -7.557  1.00 112.11 ?  345  ARG B CB  1 
ATOM   3815  C  CG  . ARG B 2  345  ? -13.285 -30.692  -8.219  1.00 125.23 ?  345  ARG B CG  1 
ATOM   3816  C  CD  . ARG B 2  345  ? -13.181 -31.153  -9.665  1.00 127.30 ?  345  ARG B CD  1 
ATOM   3817  N  NE  . ARG B 2  345  ? -14.407 -30.885  -10.410 1.00 125.00 ?  345  ARG B NE  1 
ATOM   3818  C  CZ  . ARG B 2  345  ? -14.663 -29.746  -11.037 1.00 122.50 ?  345  ARG B CZ  1 
ATOM   3819  N  NH1 . ARG B 2  345  ? -13.801 -28.742  -11.026 1.00 121.20 ?  345  ARG B NH1 1 
ATOM   3820  N  NH2 . ARG B 2  345  ? -15.815 -29.607  -11.688 1.00 118.48 ?  345  ARG B NH2 1 
ATOM   3821  N  N   . ALA B 2  346  ? -14.511 -32.906  -5.013  1.00 92.02  ?  346  ALA B N   1 
ATOM   3822  C  CA  . ALA B 2  346  ? -13.837 -33.240  -3.762  1.00 89.06  ?  346  ALA B CA  1 
ATOM   3823  C  C   . ALA B 2  346  ? -13.787 -34.746  -3.538  1.00 86.96  ?  346  ALA B C   1 
ATOM   3824  O  O   . ALA B 2  346  ? -12.764 -35.273  -3.086  1.00 87.36  ?  346  ALA B O   1 
ATOM   3825  C  CB  . ALA B 2  346  ? -14.525 -32.545  -2.587  1.00 87.26  ?  346  ALA B CB  1 
ATOM   3826  N  N   . ILE B 2  347  ? -14.882 -35.453  -3.834  1.00 83.69  ?  347  ILE B N   1 
ATOM   3827  C  CA  . ILE B 2  347  ? -14.879 -36.911  -3.712  1.00 79.49  ?  347  ILE B CA  1 
ATOM   3828  C  C   . ILE B 2  347  ? -13.778 -37.512  -4.578  1.00 81.99  ?  347  ILE B C   1 
ATOM   3829  O  O   . ILE B 2  347  ? -13.001 -38.361  -4.125  1.00 89.32  ?  347  ILE B O   1 
ATOM   3830  C  CB  . ILE B 2  347  ? -16.258 -37.492  -4.077  1.00 71.75  ?  347  ILE B CB  1 
ATOM   3831  C  CG1 . ILE B 2  347  ? -17.296 -37.164  -3.004  1.00 70.72  ?  347  ILE B CG1 1 
ATOM   3832  C  CG2 . ILE B 2  347  ? -16.163 -38.997  -4.263  1.00 60.96  ?  347  ILE B CG2 1 
ATOM   3833  C  CD1 . ILE B 2  347  ? -18.600 -37.901  -3.204  1.00 66.21  ?  347  ILE B CD1 1 
ATOM   3834  N  N   . ALA B 2  348  ? -13.688 -37.071  -5.836  1.00 74.77  ?  348  ALA B N   1 
ATOM   3835  C  CA  . ALA B 2  348  ? -12.666 -37.599  -6.734  1.00 75.78  ?  348  ALA B CA  1 
ATOM   3836  C  C   . ALA B 2  348  ? -11.260 -37.219  -6.287  1.00 78.01  ?  348  ALA B C   1 
ATOM   3837  O  O   . ALA B 2  348  ? -10.316 -37.987  -6.505  1.00 81.03  ?  348  ALA B O   1 
ATOM   3838  C  CB  . ALA B 2  348  ? -12.915 -37.108  -8.159  1.00 86.10  ?  348  ALA B CB  1 
ATOM   3839  N  N   . ARG B 2  349  ? -11.094 -36.049  -5.668  1.00 96.04  ?  349  ARG B N   1 
ATOM   3840  C  CA  . ARG B 2  349  ? -9.758  -35.626  -5.260  1.00 102.16 ?  349  ARG B CA  1 
ATOM   3841  C  C   . ARG B 2  349  ? -9.295  -36.357  -4.005  1.00 99.11  ?  349  ARG B C   1 
ATOM   3842  O  O   . ARG B 2  349  ? -8.117  -36.716  -3.897  1.00 101.51 ?  349  ARG B O   1 
ATOM   3843  C  CB  . ARG B 2  349  ? -9.714  -34.112  -5.046  1.00 102.00 ?  349  ARG B CB  1 
ATOM   3844  C  CG  . ARG B 2  349  ? -9.850  -33.281  -6.319  1.00 107.36 ?  349  ARG B CG  1 
ATOM   3845  C  CD  . ARG B 2  349  ? -9.058  -33.882  -7.474  1.00 114.92 ?  349  ARG B CD  1 
ATOM   3846  N  NE  . ARG B 2  349  ? -9.917  -34.514  -8.470  1.00 115.96 ?  349  ARG B NE  1 
ATOM   3847  C  CZ  . ARG B 2  349  ? -9.492  -35.370  -9.389  1.00 113.18 ?  349  ARG B CZ  1 
ATOM   3848  N  NH1 . ARG B 2  349  ? -8.220  -35.724  -9.469  1.00 114.85 ?  349  ARG B NH1 1 
ATOM   3849  N  NH2 . ARG B 2  349  ? -10.365 -35.883  -10.252 1.00 109.59 ?  349  ARG B NH2 1 
ATOM   3850  N  N   . ASP B 2  350  ? -10.196 -36.564  -3.036  1.00 123.91 ?  350  ASP B N   1 
ATOM   3851  C  CA  . ASP B 2  350  ? -9.834  -37.342  -1.853  1.00 121.63 ?  350  ASP B CA  1 
ATOM   3852  C  C   . ASP B 2  350  ? -9.625  -38.809  -2.211  1.00 125.03 ?  350  ASP B C   1 
ATOM   3853  O  O   . ASP B 2  350  ? -8.688  -39.446  -1.716  1.00 133.20 ?  350  ASP B O   1 
ATOM   3854  C  CB  . ASP B 2  350  ? -10.897 -37.189  -0.767  1.00 117.00 ?  350  ASP B CB  1 
ATOM   3855  C  CG  . ASP B 2  350  ? -10.815 -35.852  -0.064  1.00 125.31 ?  350  ASP B CG  1 
ATOM   3856  O  OD1 . ASP B 2  350  ? -9.978  -35.015  -0.462  1.00 128.89 ?  350  ASP B OD1 1 
ATOM   3857  O  OD2 . ASP B 2  350  ? -11.583 -35.645  0.896   1.00 121.77 -1 350  ASP B OD2 1 
ATOM   3858  N  N   . LEU B 2  351  ? -10.474 -39.356  -3.081  1.00 80.87  ?  351  LEU B N   1 
ATOM   3859  C  CA  . LEU B 2  351  ? -10.151 -40.617  -3.728  1.00 74.26  ?  351  LEU B CA  1 
ATOM   3860  C  C   . LEU B 2  351  ? -8.935  -40.406  -4.628  1.00 86.44  ?  351  LEU B C   1 
ATOM   3861  O  O   . LEU B 2  351  ? -8.496  -39.275  -4.853  1.00 88.61  ?  351  LEU B O   1 
ATOM   3862  C  CB  . LEU B 2  351  ? -11.351 -41.129  -4.526  1.00 70.49  ?  351  LEU B CB  1 
ATOM   3863  C  CG  . LEU B 2  351  ? -12.590 -41.496  -3.699  1.00 57.92  ?  351  LEU B CG  1 
ATOM   3864  C  CD1 . LEU B 2  351  ? -13.727 -41.968  -4.593  1.00 46.98  ?  351  LEU B CD1 1 
ATOM   3865  C  CD2 . LEU B 2  351  ? -12.254 -42.548  -2.656  1.00 73.03  ?  351  LEU B CD2 1 
ATOM   3866  N  N   . GLU B 2  352  ? -8.362  -41.511  -5.114  1.00 124.84 ?  352  GLU B N   1 
ATOM   3867  C  CA  . GLU B 2  352  ? -7.167  -41.493  -5.958  1.00 131.58 ?  352  GLU B CA  1 
ATOM   3868  C  C   . GLU B 2  352  ? -5.933  -41.066  -5.170  1.00 125.98 ?  352  GLU B C   1 
ATOM   3869  O  O   . GLU B 2  352  ? -4.805  -41.364  -5.575  1.00 134.09 ?  352  GLU B O   1 
ATOM   3870  C  CB  . GLU B 2  352  ? -7.357  -40.577  -7.173  1.00 138.24 ?  352  GLU B CB  1 
ATOM   3871  C  CG  . GLU B 2  352  ? -8.249  -41.151  -8.252  1.00 140.16 ?  352  GLU B CG  1 
ATOM   3872  C  CD  . GLU B 2  352  ? -8.453  -40.180  -9.394  1.00 146.28 ?  352  GLU B CD  1 
ATOM   3873  O  OE1 . GLU B 2  352  ? -8.384  -38.961  -9.142  1.00 144.83 ?  352  GLU B OE1 1 
ATOM   3874  O  OE2 . GLU B 2  352  ? -8.677  -40.630  -10.539 1.00 150.72 -1 352  GLU B OE2 1 
ATOM   3875  N  N   . GLU B 2  353  ? -6.130  -40.347  -4.064  1.00 90.90  ?  353  GLU B N   1 
ATOM   3876  C  CA  . GLU B 2  353  ? -5.067  -40.032  -3.122  1.00 99.72  ?  353  GLU B CA  1 
ATOM   3877  C  C   . GLU B 2  353  ? -5.070  -40.973  -1.925  1.00 86.88  ?  353  GLU B C   1 
ATOM   3878  O  O   . GLU B 2  353  ? -4.121  -40.954  -1.134  1.00 79.10  ?  353  GLU B O   1 
ATOM   3879  C  CB  . GLU B 2  353  ? -5.197  -38.573  -2.650  1.00 105.06 ?  353  GLU B CB  1 
ATOM   3880  C  CG  . GLU B 2  353  ? -3.957  -37.989  -1.979  1.00 110.99 ?  353  GLU B CG  1 
ATOM   3881  C  CD  . GLU B 2  353  ? -4.202  -36.604  -1.410  1.00 121.05 ?  353  GLU B CD  1 
ATOM   3882  O  OE1 . GLU B 2  353  ? -5.377  -36.181  -1.341  1.00 119.21 ?  353  GLU B OE1 1 
ATOM   3883  O  OE2 . GLU B 2  353  ? -3.216  -35.932  -1.048  1.00 130.73 -1 353  GLU B OE2 1 
ATOM   3884  N  N   . HIS B 2  354  ? -6.108  -41.806  -1.791  1.00 117.96 ?  354  HIS B N   1 
ATOM   3885  C  CA  . HIS B 2  354  ? -6.220  -42.804  -0.729  1.00 127.81 ?  354  HIS B CA  1 
ATOM   3886  C  C   . HIS B 2  354  ? -6.617  -44.134  -1.378  1.00 124.38 ?  354  HIS B C   1 
ATOM   3887  O  O   . HIS B 2  354  ? -7.733  -44.628  -1.197  1.00 121.31 ?  354  HIS B O   1 
ATOM   3888  C  CB  . HIS B 2  354  ? -7.234  -42.373  0.333   1.00 122.66 ?  354  HIS B CB  1 
ATOM   3889  C  CG  . HIS B 2  354  ? -6.826  -41.155  1.100   1.00 126.05 ?  354  HIS B CG  1 
ATOM   3890  N  ND1 . HIS B 2  354  ? -7.319  -39.900  0.814   1.00 125.23 ?  354  HIS B ND1 1 
ATOM   3891  C  CD2 . HIS B 2  354  ? -5.978  -40.998  2.143   1.00 126.87 ?  354  HIS B CD2 1 
ATOM   3892  C  CE1 . HIS B 2  354  ? -6.788  -39.021  1.645   1.00 126.67 ?  354  HIS B CE1 1 
ATOM   3893  N  NE2 . HIS B 2  354  ? -5.971  -39.661  2.462   1.00 130.30 ?  354  HIS B NE2 1 
ATOM   3894  N  N   . ARG B 2  355  ? -5.692  -44.710  -2.142  1.00 112.02 ?  355  ARG B N   1 
ATOM   3895  C  CA  . ARG B 2  355  ? -5.950  -45.939  -2.879  1.00 107.17 ?  355  ARG B CA  1 
ATOM   3896  C  C   . ARG B 2  355  ? -5.676  -47.140  -1.985  1.00 111.93 ?  355  ARG B C   1 
ATOM   3897  O  O   . ARG B 2  355  ? -4.610  -47.230  -1.369  1.00 121.74 ?  355  ARG B O   1 
ATOM   3898  C  CB  . ARG B 2  355  ? -5.088  -46.005  -4.139  1.00 110.52 ?  355  ARG B CB  1 
ATOM   3899  C  CG  . ARG B 2  355  ? -5.496  -45.009  -5.208  1.00 123.65 ?  355  ARG B CG  1 
ATOM   3900  C  CD  . ARG B 2  355  ? -4.681  -45.177  -6.479  1.00 131.76 ?  355  ARG B CD  1 
ATOM   3901  N  NE  . ARG B 2  355  ? -5.134  -44.273  -7.530  1.00 133.95 ?  355  ARG B NE  1 
ATOM   3902  C  CZ  . ARG B 2  355  ? -5.968  -44.609  -8.506  1.00 134.66 ?  355  ARG B CZ  1 
ATOM   3903  N  NH1 . ARG B 2  355  ? -6.475  -45.829  -8.596  1.00 127.21 ?  355  ARG B NH1 1 
ATOM   3904  N  NH2 . ARG B 2  355  ? -6.300  -43.698  -9.417  1.00 129.26 ?  355  ARG B NH2 1 
ATOM   3905  N  N   . GLY B 2  356  ? -6.636  -48.062  -1.922  1.00 85.55  ?  356  GLY B N   1 
ATOM   3906  C  CA  . GLY B 2  356  ? -6.600  -49.127  -0.943  1.00 80.66  ?  356  GLY B CA  1 
ATOM   3907  C  C   . GLY B 2  356  ? -6.964  -48.697  0.460   1.00 84.75  ?  356  GLY B C   1 
ATOM   3908  O  O   . GLY B 2  356  ? -7.055  -49.552  1.352   1.00 82.57  ?  356  GLY B O   1 
ATOM   3909  N  N   . GLN B 2  357  ? -7.160  -47.397  0.686   1.00 91.91  ?  357  GLN B N   1 
ATOM   3910  C  CA  . GLN B 2  357  ? -7.601  -46.856  1.965   1.00 91.77  ?  357  GLN B CA  1 
ATOM   3911  C  C   . GLN B 2  357  ? -8.972  -46.206  1.840   1.00 89.18  ?  357  GLN B C   1 
ATOM   3912  O  O   . GLN B 2  357  ? -9.310  -45.311  2.623   1.00 94.38  ?  357  GLN B O   1 
ATOM   3913  C  CB  . GLN B 2  357  ? -6.577  -45.851  2.497   1.00 93.02  ?  357  GLN B CB  1 
ATOM   3914  C  CG  . GLN B 2  357  ? -5.269  -46.485  2.932   1.00 88.02  ?  357  GLN B CG  1 
ATOM   3915  C  CD  . GLN B 2  357  ? -4.242  -45.463  3.370   1.00 98.72  ?  357  GLN B CD  1 
ATOM   3916  O  OE1 . GLN B 2  357  ? -4.451  -44.258  3.235   1.00 111.73 ?  357  GLN B OE1 1 
ATOM   3917  N  NE2 . GLN B 2  357  ? -3.119  -45.942  3.892   1.00 93.71  ?  357  GLN B NE2 1 
ATOM   3918  N  N   . SER B 2  358  ? -9.762  -46.637  0.859   1.00 58.62  ?  358  SER B N   1 
ATOM   3919  C  CA  . SER B 2  358  ? -11.050 -46.032  0.568   1.00 54.81  ?  358  SER B CA  1 
ATOM   3920  C  C   . SER B 2  358  ? -12.077 -47.122  0.299   1.00 60.34  ?  358  SER B C   1 
ATOM   3921  O  O   . SER B 2  358  ? -11.738 -48.288  0.086   1.00 66.88  ?  358  SER B O   1 
ATOM   3922  C  CB  . SER B 2  358  ? -10.972 -45.081  -0.634  1.00 62.80  ?  358  SER B CB  1 
ATOM   3923  O  OG  . SER B 2  358  ? -10.413 -45.719  -1.770  1.00 54.79  ?  358  SER B OG  1 
ATOM   3924  N  N   . VAL B 2  359  ? -13.346 -46.722  0.318   1.00 82.55  ?  359  VAL B N   1 
ATOM   3925  C  CA  . VAL B 2  359  ? -14.451 -47.627  0.025   1.00 79.98  ?  359  VAL B CA  1 
ATOM   3926  C  C   . VAL B 2  359  ? -15.638 -46.802  -0.453  1.00 85.15  ?  359  VAL B C   1 
ATOM   3927  O  O   . VAL B 2  359  ? -15.911 -45.716  0.067   1.00 91.84  ?  359  VAL B O   1 
ATOM   3928  C  CB  . VAL B 2  359  ? -14.811 -48.501  1.248   1.00 73.92  ?  359  VAL B CB  1 
ATOM   3929  C  CG1 . VAL B 2  359  ? -15.350 -47.653  2.385   1.00 79.71  ?  359  VAL B CG1 1 
ATOM   3930  C  CG2 . VAL B 2  359  ? -15.822 -49.556  0.853   1.00 76.25  ?  359  VAL B CG2 1 
ATOM   3931  N  N   . VAL B 2  360  ? -16.322 -47.310  -1.473  1.00 58.42  ?  360  VAL B N   1 
ATOM   3932  C  CA  . VAL B 2  360  ? -17.541 -46.708  -1.998  1.00 49.12  ?  360  VAL B CA  1 
ATOM   3933  C  C   . VAL B 2  360  ? -18.677 -47.686  -1.743  1.00 56.16  ?  360  VAL B C   1 
ATOM   3934  O  O   . VAL B 2  360  ? -18.631 -48.834  -2.202  1.00 63.36  ?  360  VAL B O   1 
ATOM   3935  C  CB  . VAL B 2  360  ? -17.418 -46.380  -3.492  1.00 62.78  ?  360  VAL B CB  1 
ATOM   3936  C  CG1 . VAL B 2  360  ? -18.733 -45.826  -4.021  1.00 62.62  ?  360  VAL B CG1 1 
ATOM   3937  C  CG2 . VAL B 2  360  ? -16.276 -45.399  -3.726  1.00 61.40  ?  360  VAL B CG2 1 
ATOM   3938  N  N   . ILE B 2  361  ? -19.692 -47.236  -1.010  1.00 56.31  ?  361  ILE B N   1 
ATOM   3939  C  CA  . ILE B 2  361  ? -20.797 -48.080  -0.572  1.00 61.49  ?  361  ILE B CA  1 
ATOM   3940  C  C   . ILE B 2  361  ? -22.068 -47.615  -1.266  1.00 60.30  ?  361  ILE B C   1 
ATOM   3941  O  O   . ILE B 2  361  ? -22.368 -46.415  -1.288  1.00 57.31  ?  361  ILE B O   1 
ATOM   3942  C  CB  . ILE B 2  361  ? -20.960 -48.042  0.957   1.00 60.62  ?  361  ILE B CB  1 
ATOM   3943  C  CG1 . ILE B 2  361  ? -19.606 -48.247  1.640   1.00 61.03  ?  361  ILE B CG1 1 
ATOM   3944  C  CG2 . ILE B 2  361  ? -21.961 -49.088  1.414   1.00 57.54  ?  361  ILE B CG2 1 
ATOM   3945  C  CD1 . ILE B 2  361  ? -19.676 -48.287  3.149   1.00 57.18  ?  361  ILE B CD1 1 
ATOM   3946  N  N   . ALA B 2  362  ? -22.811 -48.562  -1.829  1.00 77.37  ?  362  ALA B N   1 
ATOM   3947  C  CA  . ALA B 2  362  ? -24.075 -48.290  -2.498  1.00 77.81  ?  362  ALA B CA  1 
ATOM   3948  C  C   . ALA B 2  362  ? -25.218 -48.848  -1.663  1.00 79.47  ?  362  ALA B C   1 
ATOM   3949  O  O   . ALA B 2  362  ? -25.159 -49.996  -1.211  1.00 73.77  ?  362  ALA B O   1 
ATOM   3950  C  CB  . ALA B 2  362  ? -24.092 -48.900  -3.900  1.00 73.92  ?  362  ALA B CB  1 
ATOM   3951  N  N   . GLY B 2  363  ? -26.254 -48.036  -1.464  1.00 76.04  ?  363  GLY B N   1 
ATOM   3952  C  CA  . GLY B 2  363  ? -27.379 -48.467  -0.660  1.00 75.70  ?  363  GLY B CA  1 
ATOM   3953  C  C   . GLY B 2  363  ? -28.238 -49.489  -1.377  1.00 74.97  ?  363  GLY B C   1 
ATOM   3954  O  O   . GLY B 2  363  ? -28.286 -49.550  -2.606  1.00 75.53  ?  363  GLY B O   1 
ATOM   3955  N  N   . ASP B 2  364  ? -28.922 -50.314  -0.581  1.00 70.29  ?  364  ASP B N   1 
ATOM   3956  C  CA  . ASP B 2  364  ? -29.816 -51.317  -1.148  1.00 68.88  ?  364  ASP B CA  1 
ATOM   3957  C  C   . ASP B 2  364  ? -30.952 -50.676  -1.933  1.00 71.78  ?  364  ASP B C   1 
ATOM   3958  O  O   . ASP B 2  364  ? -31.497 -51.296  -2.853  1.00 75.59  ?  364  ASP B O   1 
ATOM   3959  C  CB  . ASP B 2  364  ? -30.375 -52.204  -0.036  1.00 68.16  ?  364  ASP B CB  1 
ATOM   3960  C  CG  . ASP B 2  364  ? -29.285 -52.869  0.783   1.00 70.98  ?  364  ASP B CG  1 
ATOM   3961  O  OD1 . ASP B 2  364  ? -28.093 -52.640  0.491   1.00 68.13  ?  364  ASP B OD1 1 
ATOM   3962  O  OD2 . ASP B 2  364  ? -29.623 -53.625  1.721   1.00 76.11  -1 364  ASP B OD2 1 
ATOM   3963  N  N   . GLN B 2  365  ? -31.319 -49.439  -1.592  1.00 94.50  ?  365  GLN B N   1 
ATOM   3964  C  CA  . GLN B 2  365  ? -32.402 -48.765  -2.299  1.00 96.56  ?  365  GLN B CA  1 
ATOM   3965  C  C   . GLN B 2  365  ? -31.990 -48.364  -3.710  1.00 101.17 ?  365  GLN B C   1 
ATOM   3966  O  O   . GLN B 2  365  ? -32.837 -48.304  -4.609  1.00 108.82 ?  365  GLN B O   1 
ATOM   3967  C  CB  . GLN B 2  365  ? -32.855 -47.540  -1.506  1.00 97.92  ?  365  GLN B CB  1 
ATOM   3968  C  CG  . GLN B 2  365  ? -31.702 -46.714  -0.962  1.00 95.00  ?  365  GLN B CG  1 
ATOM   3969  C  CD  . GLN B 2  365  ? -31.487 -46.924  0.526   1.00 107.30 ?  365  GLN B CD  1 
ATOM   3970  O  OE1 . GLN B 2  365  ? -31.787 -47.991  1.065   1.00 120.13 ?  365  GLN B OE1 1 
ATOM   3971  N  NE2 . GLN B 2  365  ? -30.957 -45.908  1.197   1.00 102.91 ?  365  GLN B NE2 1 
ATOM   3972  N  N   . GLN B 2  366  ? -30.705 -48.098  -3.926  1.00 79.83  ?  366  GLN B N   1 
ATOM   3973  C  CA  . GLN B 2  366  ? -30.246 -47.622  -5.219  1.00 76.00  ?  366  GLN B CA  1 
ATOM   3974  C  C   . GLN B 2  366  ? -30.346 -48.730  -6.269  1.00 84.12  ?  366  GLN B C   1 
ATOM   3975  O  O   . GLN B 2  366  ? -30.285 -49.917  -5.938  1.00 92.47  ?  366  GLN B O   1 
ATOM   3976  C  CB  . GLN B 2  366  ? -28.811 -47.116  -5.117  1.00 75.71  ?  366  GLN B CB  1 
ATOM   3977  C  CG  . GLN B 2  366  ? -28.691 -45.755  -4.451  1.00 77.87  ?  366  GLN B CG  1 
ATOM   3978  C  CD  . GLN B 2  366  ? -29.480 -44.680  -5.181  1.00 80.91  ?  366  GLN B CD  1 
ATOM   3979  O  OE1 . GLN B 2  366  ? -29.392 -44.549  -6.402  1.00 81.28  ?  366  GLN B OE1 1 
ATOM   3980  N  NE2 . GLN B 2  366  ? -30.255 -43.905  -4.433  1.00 85.17  ?  366  GLN B NE2 1 
ATOM   3981  N  N   . PRO B 2  367  ? -30.502 -48.367  -7.541  1.00 68.15  ?  367  PRO B N   1 
ATOM   3982  C  CA  . PRO B 2  367  ? -30.701 -49.375  -8.595  1.00 61.65  ?  367  PRO B CA  1 
ATOM   3983  C  C   . PRO B 2  367  ? -29.483 -50.268  -8.755  1.00 61.53  ?  367  PRO B C   1 
ATOM   3984  O  O   . PRO B 2  367  ? -28.393 -49.944  -8.260  1.00 63.19  ?  367  PRO B O   1 
ATOM   3985  C  CB  . PRO B 2  367  ? -30.942 -48.522  -9.852  1.00 62.16  ?  367  PRO B CB  1 
ATOM   3986  C  CG  . PRO B 2  367  ? -31.429 -47.212  -9.319  1.00 68.78  ?  367  PRO B CG  1 
ATOM   3987  C  CD  . PRO B 2  367  ? -30.625 -47.001  -8.077  1.00 65.90  ?  367  PRO B CD  1 
ATOM   3988  N  N   . PRO B 2  368  ? -29.635 -51.411  -9.433  1.00 61.49  ?  368  PRO B N   1 
ATOM   3989  C  CA  . PRO B 2  368  ? -28.507 -52.353  -9.553  1.00 62.51  ?  368  PRO B CA  1 
ATOM   3990  C  C   . PRO B 2  368  ? -27.282 -51.776  -10.238 1.00 61.95  ?  368  PRO B C   1 
ATOM   3991  O  O   . PRO B 2  368  ? -26.161 -52.198  -9.927  1.00 58.64  ?  368  PRO B O   1 
ATOM   3992  C  CB  . PRO B 2  368  ? -29.112 -53.503  -10.369 1.00 60.57  ?  368  PRO B CB  1 
ATOM   3993  C  CG  . PRO B 2  368  ? -30.560 -53.471  -10.011 1.00 65.34  ?  368  PRO B CG  1 
ATOM   3994  C  CD  . PRO B 2  368  ? -30.895 -52.006  -9.912  1.00 64.32  ?  368  PRO B CD  1 
ATOM   3995  N  N   . ILE B 2  369  ? -27.458 -50.831  -11.165 1.00 65.92  ?  369  ILE B N   1 
ATOM   3996  C  CA  . ILE B 2  369  ? -26.312 -50.268  -11.875 1.00 67.43  ?  369  ILE B CA  1 
ATOM   3997  C  C   . ILE B 2  369  ? -25.404 -49.513  -10.909 1.00 73.36  ?  369  ILE B C   1 
ATOM   3998  O  O   . ILE B 2  369  ? -24.177 -49.507  -11.065 1.00 68.83  ?  369  ILE B O   1 
ATOM   3999  C  CB  . ILE B 2  369  ? -26.789 -49.372  -13.036 1.00 63.05  ?  369  ILE B CB  1 
ATOM   4000  C  CG1 . ILE B 2  369  ? -25.603 -48.686  -13.725 1.00 67.15  ?  369  ILE B CG1 1 
ATOM   4001  C  CG2 . ILE B 2  369  ? -27.804 -48.346  -12.542 1.00 72.05  ?  369  ILE B CG2 1 
ATOM   4002  C  CD1 . ILE B 2  369  ? -24.601 -49.642  -14.333 1.00 68.34  ?  369  ILE B CD1 1 
ATOM   4003  N  N   . VAL B 2  370  ? -25.988 -48.886  -9.883  1.00 58.40  ?  370  VAL B N   1 
ATOM   4004  C  CA  . VAL B 2  370  ? -25.190 -48.142  -8.910  1.00 56.23  ?  370  VAL B CA  1 
ATOM   4005  C  C   . VAL B 2  370  ? -24.277 -49.086  -8.138  1.00 58.29  ?  370  VAL B C   1 
ATOM   4006  O  O   . VAL B 2  370  ? -23.115 -48.762  -7.858  1.00 56.95  ?  370  VAL B O   1 
ATOM   4007  C  CB  . VAL B 2  370  ? -26.108 -47.348  -7.964  1.00 54.10  ?  370  VAL B CB  1 
ATOM   4008  C  CG1 . VAL B 2  370  ? -25.284 -46.631  -6.908  1.00 48.52  ?  370  VAL B CG1 1 
ATOM   4009  C  CG2 . VAL B 2  370  ? -26.967 -46.370  -8.753  1.00 56.99  ?  370  VAL B CG2 1 
ATOM   4010  N  N   . HIS B 2  371  ? -24.790 -50.265  -7.780  1.00 69.02  ?  371  HIS B N   1 
ATOM   4011  C  CA  . HIS B 2  371  ? -23.963 -51.266  -7.116  1.00 67.16  ?  371  HIS B CA  1 
ATOM   4012  C  C   . HIS B 2  371  ? -22.813 -51.703  -8.013  1.00 72.85  ?  371  HIS B C   1 
ATOM   4013  O  O   . HIS B 2  371  ? -21.663 -51.791  -7.569  1.00 69.79  ?  371  HIS B O   1 
ATOM   4014  C  CB  . HIS B 2  371  ? -24.813 -52.473  -6.717  1.00 72.72  ?  371  HIS B CB  1 
ATOM   4015  C  CG  . HIS B 2  371  ? -25.787 -52.194  -5.617  1.00 72.12  ?  371  HIS B CG  1 
ATOM   4016  N  ND1 . HIS B 2  371  ? -27.073 -51.764  -5.857  1.00 78.45  ?  371  HIS B ND1 1 
ATOM   4017  C  CD2 . HIS B 2  371  ? -25.673 -52.304  -4.272  1.00 65.08  ?  371  HIS B CD2 1 
ATOM   4018  C  CE1 . HIS B 2  371  ? -27.706 -51.609  -4.709  1.00 72.23  ?  371  HIS B CE1 1 
ATOM   4019  N  NE2 . HIS B 2  371  ? -26.879 -51.930  -3.730  1.00 70.20  ?  371  HIS B NE2 1 
ATOM   4020  N  N   . ALA B 2  372  ? -23.108 -51.968  -9.289  1.00 87.35  ?  372  ALA B N   1 
ATOM   4021  C  CA  . ALA B 2  372  ? -22.085 -52.448  -10.212 1.00 88.20  ?  372  ALA B CA  1 
ATOM   4022  C  C   . ALA B 2  372  ? -21.010 -51.394  -10.451 1.00 83.42  ?  372  ALA B C   1 
ATOM   4023  O  O   . ALA B 2  372  ? -19.816 -51.716  -10.498 1.00 82.69  ?  372  ALA B O   1 
ATOM   4024  C  CB  . ALA B 2  372  ? -22.731 -52.870  -11.531 1.00 86.82  ?  372  ALA B CB  1 
ATOM   4025  N  N   . LEU B 2  373  ? -21.411 -50.130  -10.602 1.00 51.76  ?  373  LEU B N   1 
ATOM   4026  C  CA  . LEU B 2  373  ? -20.430 -49.062  -10.768 1.00 61.01  ?  373  LEU B CA  1 
ATOM   4027  C  C   . LEU B 2  373  ? -19.577 -48.901  -9.516  1.00 57.53  ?  373  LEU B C   1 
ATOM   4028  O  O   . LEU B 2  373  ? -18.386 -48.577  -9.604  1.00 47.63  ?  373  LEU B O   1 
ATOM   4029  C  CB  . LEU B 2  373  ? -21.134 -47.749  -11.112 1.00 58.79  ?  373  LEU B CB  1 
ATOM   4030  C  CG  . LEU B 2  373  ? -21.756 -47.667  -12.505 1.00 60.54  ?  373  LEU B CG  1 
ATOM   4031  C  CD1 . LEU B 2  373  ? -22.511 -46.359  -12.678 1.00 65.08  ?  373  LEU B CD1 1 
ATOM   4032  C  CD2 . LEU B 2  373  ? -20.689 -47.827  -13.579 1.00 55.21  ?  373  LEU B CD2 1 
ATOM   4033  N  N   . ALA B 2  374  ? -20.169 -49.128  -8.341  1.00 84.61  ?  374  ALA B N   1 
ATOM   4034  C  CA  . ALA B 2  374  ? -19.408 -49.045  -7.099  1.00 88.64  ?  374  ALA B CA  1 
ATOM   4035  C  C   . ALA B 2  374  ? -18.364 -50.152  -7.014  1.00 88.51  ?  374  ALA B C   1 
ATOM   4036  O  O   . ALA B 2  374  ? -17.227 -49.909  -6.595  1.00 91.44  ?  374  ALA B O   1 
ATOM   4037  C  CB  . ALA B 2  374  ? -20.354 -49.104  -5.901  1.00 88.84  ?  374  ALA B CB  1 
ATOM   4038  N  N   . HIS B 2  375  ? -18.735 -51.378  -7.399  1.00 73.41  ?  375  HIS B N   1 
ATOM   4039  C  CA  . HIS B 2  375  ? -17.759 -52.462  -7.451  1.00 76.24  ?  375  HIS B CA  1 
ATOM   4040  C  C   . HIS B 2  375  ? -16.629 -52.130  -8.416  1.00 78.89  ?  375  HIS B C   1 
ATOM   4041  O  O   . HIS B 2  375  ? -15.456 -52.392  -8.128  1.00 79.62  ?  375  HIS B O   1 
ATOM   4042  C  CB  . HIS B 2  375  ? -18.439 -53.768  -7.865  1.00 69.70  ?  375  HIS B CB  1 
ATOM   4043  C  CG  . HIS B 2  375  ? -19.376 -54.319  -6.836  1.00 73.40  ?  375  HIS B CG  1 
ATOM   4044  N  ND1 . HIS B 2  375  ? -20.663 -54.709  -7.138  1.00 75.84  ?  375  HIS B ND1 1 
ATOM   4045  C  CD2 . HIS B 2  375  ? -19.214 -54.552  -5.513  1.00 76.08  ?  375  HIS B CD2 1 
ATOM   4046  C  CE1 . HIS B 2  375  ? -21.254 -55.156  -6.045  1.00 68.51  ?  375  HIS B CE1 1 
ATOM   4047  N  NE2 . HIS B 2  375  ? -20.396 -55.071  -5.044  1.00 79.22  ?  375  HIS B NE2 1 
ATOM   4048  N  N   . LEU B 2  376  ? -16.970 -51.541  -9.564  1.00 88.61  ?  376  LEU B N   1 
ATOM   4049  C  CA  . LEU B 2  376  ? -15.961 -51.164  -10.550 1.00 95.15  ?  376  LEU B CA  1 
ATOM   4050  C  C   . LEU B 2  376  ? -15.033 -50.084  -10.005 1.00 96.98  ?  376  LEU B C   1 
ATOM   4051  O  O   . LEU B 2  376  ? -13.809 -50.165  -10.164 1.00 100.75 ?  376  LEU B O   1 
ATOM   4052  C  CB  . LEU B 2  376  ? -16.649 -50.693  -11.831 1.00 97.01  ?  376  LEU B CB  1 
ATOM   4053  C  CG  . LEU B 2  376  ? -15.796 -49.993  -12.887 1.00 86.48  ?  376  LEU B CG  1 
ATOM   4054  C  CD1 . LEU B 2  376  ? -14.693 -50.907  -13.402 1.00 93.21  ?  376  LEU B CD1 1 
ATOM   4055  C  CD2 . LEU B 2  376  ? -16.677 -49.507  -14.026 1.00 85.81  ?  376  LEU B CD2 1 
ATOM   4056  N  N   . ILE B 2  377  ? -15.601 -49.059  -9.363  1.00 60.16  ?  377  ILE B N   1 
ATOM   4057  C  CA  . ILE B 2  377  ? -14.785 -47.995  -8.782  1.00 61.78  ?  377  ILE B CA  1 
ATOM   4058  C  C   . ILE B 2  377  ? -13.849 -48.555  -7.718  1.00 66.91  ?  377  ILE B C   1 
ATOM   4059  O  O   . ILE B 2  377  ? -12.663 -48.207  -7.668  1.00 69.03  ?  377  ILE B O   1 
ATOM   4060  C  CB  . ILE B 2  377  ? -15.687 -46.882  -8.215  1.00 60.42  ?  377  ILE B CB  1 
ATOM   4061  C  CG1 . ILE B 2  377  ? -16.341 -46.090  -9.347  1.00 59.65  ?  377  ILE B CG1 1 
ATOM   4062  C  CG2 . ILE B 2  377  ? -14.895 -45.957  -7.315  1.00 67.63  ?  377  ILE B CG2 1 
ATOM   4063  C  CD1 . ILE B 2  377  ? -17.286 -45.016  -8.864  1.00 53.88  ?  377  ILE B CD1 1 
ATOM   4064  N  N   . ASN B 2  378  ? -14.361 -49.441  -6.859  1.00 79.89  ?  378  ASN B N   1 
ATOM   4065  C  CA  . ASN B 2  378  ? -13.536 -50.000  -5.791  1.00 77.19  ?  378  ASN B CA  1 
ATOM   4066  C  C   . ASN B 2  378  ? -12.416 -50.865  -6.352  1.00 79.12  ?  378  ASN B C   1 
ATOM   4067  O  O   . ASN B 2  378  ? -11.291 -50.850  -5.836  1.00 82.54  ?  378  ASN B O   1 
ATOM   4068  C  CB  . ASN B 2  378  ? -14.401 -50.809  -4.825  1.00 74.95  ?  378  ASN B CB  1 
ATOM   4069  C  CG  . ASN B 2  378  ? -15.238 -49.932  -3.911  1.00 77.76  ?  378  ASN B CG  1 
ATOM   4070  O  OD1 . ASN B 2  378  ? -14.821 -48.840  -3.521  1.00 78.53  ?  378  ASN B OD1 1 
ATOM   4071  N  ND2 . ASN B 2  378  ? -16.432 -50.404  -3.574  1.00 72.11  ?  378  ASN B ND2 1 
ATOM   4072  N  N   . ALA B 2  379  ? -12.702 -51.626  -7.411  1.00 64.85  ?  379  ALA B N   1 
ATOM   4073  C  CA  . ALA B 2  379  ? -11.685 -52.486  -8.005  1.00 58.32  ?  379  ALA B CA  1 
ATOM   4074  C  C   . ALA B 2  379  ? -10.567 -51.662  -8.632  1.00 66.26  ?  379  ALA B C   1 
ATOM   4075  O  O   . ALA B 2  379  ? -9.381  -51.959  -8.443  1.00 66.20  ?  379  ALA B O   1 
ATOM   4076  C  CB  . ALA B 2  379  ? -12.323 -53.412  -9.041  1.00 48.90  ?  379  ALA B CB  1 
ATOM   4077  N  N   . GLU B 2  380  ? -10.928 -50.617  -9.382  1.00 84.22  ?  380  GLU B N   1 
ATOM   4078  C  CA  . GLU B 2  380  ? -9.921  -49.782  -10.032 1.00 86.97  ?  380  GLU B CA  1 
ATOM   4079  C  C   . GLU B 2  380  ? -9.046  -49.067  -9.011  1.00 88.18  ?  380  GLU B C   1 
ATOM   4080  O  O   . GLU B 2  380  ? -7.824  -48.980  -9.182  1.00 93.69  ?  380  GLU B O   1 
ATOM   4081  C  CB  . GLU B 2  380  ? -10.599 -48.773  -10.958 1.00 103.67 ?  380  GLU B CB  1 
ATOM   4082  C  CG  . GLU B 2  380  ? -9.772  -48.396  -12.175 1.00 119.11 ?  380  GLU B CG  1 
ATOM   4083  C  CD  . GLU B 2  380  ? -9.764  -49.485  -13.229 1.00 121.17 ?  380  GLU B CD  1 
ATOM   4084  O  OE1 . GLU B 2  380  ? -10.668 -50.347  -13.199 1.00 113.13 ?  380  GLU B OE1 1 
ATOM   4085  O  OE2 . GLU B 2  380  ? -8.858  -49.475  -14.089 1.00 134.71 -1 380  GLU B OE2 1 
ATOM   4086  N  N   . LEU B 2  381  ? -9.653  -48.553  -7.939  1.00 73.00  ?  381  LEU B N   1 
ATOM   4087  C  CA  . LEU B 2  381  ? -8.909  -47.860  -6.894  1.00 70.97  ?  381  LEU B CA  1 
ATOM   4088  C  C   . LEU B 2  381  ? -7.979  -48.780  -6.113  1.00 77.53  ?  381  LEU B C   1 
ATOM   4089  O  O   . LEU B 2  381  ? -7.134  -48.279  -5.364  1.00 78.13  ?  381  LEU B O   1 
ATOM   4090  C  CB  . LEU B 2  381  ? -9.884  -47.178  -5.930  1.00 56.81  ?  381  LEU B CB  1 
ATOM   4091  C  CG  . LEU B 2  381  ? -10.592 -45.931  -6.462  1.00 64.96  ?  381  LEU B CG  1 
ATOM   4092  C  CD1 . LEU B 2  381  ? -11.617 -45.421  -5.460  1.00 64.75  ?  381  LEU B CD1 1 
ATOM   4093  C  CD2 . LEU B 2  381  ? -9.583  -44.843  -6.813  1.00 79.06  ?  381  LEU B CD2 1 
ATOM   4094  N  N   . GLY B 2  382  ? -8.110  -50.097  -6.259  1.00 59.81  ?  382  GLY B N   1 
ATOM   4095  C  CA  . GLY B 2  382  ? -7.318  -51.031  -5.487  1.00 49.87  ?  382  GLY B CA  1 
ATOM   4096  C  C   . GLY B 2  382  ? -7.869  -51.367  -4.119  1.00 53.16  ?  382  GLY B C   1 
ATOM   4097  O  O   . GLY B 2  382  ? -7.160  -51.993  -3.321  1.00 59.34  ?  382  GLY B O   1 
ATOM   4098  N  N   . ASN B 2  383  ? -9.111  -50.979  -3.823  1.00 67.11  ?  383  ASN B N   1 
ATOM   4099  C  CA  . ASN B 2  383  ? -9.668  -51.220  -2.497  1.00 64.07  ?  383  ASN B CA  1 
ATOM   4100  C  C   . ASN B 2  383  ? -9.973  -52.694  -2.270  1.00 65.48  ?  383  ASN B C   1 
ATOM   4101  O  O   . ASN B 2  383  ? -9.969  -53.154  -1.122  1.00 65.10  ?  383  ASN B O   1 
ATOM   4102  C  CB  . ASN B 2  383  ? -10.932 -50.386  -2.302  1.00 60.86  ?  383  ASN B CB  1 
ATOM   4103  C  CG  . ASN B 2  383  ? -10.726 -48.928  -2.652  1.00 64.16  ?  383  ASN B CG  1 
ATOM   4104  O  OD1 . ASN B 2  383  ? -9.620  -48.401  -2.539  1.00 66.89  ?  383  ASN B OD1 1 
ATOM   4105  N  ND2 . ASN B 2  383  ? -11.795 -48.267  -3.082  1.00 68.85  ?  383  ASN B ND2 1 
ATOM   4106  N  N   . VAL B 2  384  ? -10.245 -53.443  -3.343  1.00 90.00  ?  384  VAL B N   1 
ATOM   4107  C  CA  . VAL B 2  384  ? -10.581 -54.854  -3.201  1.00 95.33  ?  384  VAL B CA  1 
ATOM   4108  C  C   . VAL B 2  384  ? -9.438  -55.589  -2.517  1.00 91.62  ?  384  VAL B C   1 
ATOM   4109  O  O   . VAL B 2  384  ? -8.260  -55.396  -2.846  1.00 96.66  ?  384  VAL B O   1 
ATOM   4110  C  CB  . VAL B 2  384  ? -10.898 -55.468  -4.575  1.00 94.75  ?  384  VAL B CB  1 
ATOM   4111  C  CG1 . VAL B 2  384  ? -11.041 -56.978  -4.465  1.00 89.41  ?  384  VAL B CG1 1 
ATOM   4112  C  CG2 . VAL B 2  384  ? -12.163 -54.849  -5.150  1.00 95.37  ?  384  VAL B CG2 1 
ATOM   4113  N  N   . GLY B 2  385  ? -9.785  -56.434  -1.547  1.00 75.87  ?  385  GLY B N   1 
ATOM   4114  C  CA  . GLY B 2  385  ? -8.798  -57.129  -0.753  1.00 84.07  ?  385  GLY B CA  1 
ATOM   4115  C  C   . GLY B 2  385  ? -8.259  -56.346  0.421   1.00 82.55  ?  385  GLY B C   1 
ATOM   4116  O  O   . GLY B 2  385  ? -7.597  -56.935  1.287   1.00 77.44  ?  385  GLY B O   1 
ATOM   4117  N  N   . GLN B 2  386  ? -8.513  -55.040  0.484   1.00 85.97  ?  386  GLN B N   1 
ATOM   4118  C  CA  . GLN B 2  386  ? -8.091  -54.201  1.597   1.00 80.57  ?  386  GLN B CA  1 
ATOM   4119  C  C   . GLN B 2  386  ? -9.266  -53.661  2.396   1.00 77.48  ?  386  GLN B C   1 
ATOM   4120  O  O   . GLN B 2  386  ? -9.294  -53.792  3.624   1.00 78.26  ?  386  GLN B O   1 
ATOM   4121  C  CB  . GLN B 2  386  ? -7.233  -53.036  1.083   1.00 79.61  ?  386  GLN B CB  1 
ATOM   4122  C  CG  . GLN B 2  386  ? -5.983  -53.473  0.338   1.00 85.28  ?  386  GLN B CG  1 
ATOM   4123  C  CD  . GLN B 2  386  ? -5.043  -54.283  1.208   1.00 85.10  ?  386  GLN B CD  1 
ATOM   4124  O  OE1 . GLN B 2  386  ? -4.919  -55.498  1.047   1.00 88.54  ?  386  GLN B OE1 1 
ATOM   4125  N  NE2 . GLN B 2  386  ? -4.371  -53.612  2.136   1.00 83.03  ?  386  GLN B NE2 1 
ATOM   4126  N  N   . THR B 2  387  ? -10.246 -53.054  1.725   1.00 74.14  ?  387  THR B N   1 
ATOM   4127  C  CA  . THR B 2  387  ? -11.447 -52.559  2.380   1.00 75.17  ?  387  THR B CA  1 
ATOM   4128  C  C   . THR B 2  387  ? -12.729 -53.205  1.881   1.00 72.77  ?  387  THR B C   1 
ATOM   4129  O  O   . THR B 2  387  ? -13.745 -53.134  2.582   1.00 70.18  ?  387  THR B O   1 
ATOM   4130  C  CB  . THR B 2  387  ? -11.571 -51.035  2.209   1.00 72.94  ?  387  THR B CB  1 
ATOM   4131  O  OG1 . THR B 2  387  ? -11.653 -50.713  0.816   1.00 71.19  ?  387  THR B OG1 1 
ATOM   4132  C  CG2 . THR B 2  387  ? -10.368 -50.330  2.817   1.00 72.43  ?  387  THR B CG2 1 
ATOM   4133  N  N   . VAL B 2  388  ? -12.719 -53.824  0.704   1.00 71.17  ?  388  VAL B N   1 
ATOM   4134  C  CA  . VAL B 2  388  ? -13.884 -54.500  0.147   1.00 69.59  ?  388  VAL B CA  1 
ATOM   4135  C  C   . VAL B 2  388  ? -13.517 -55.961  -0.056  1.00 72.18  ?  388  VAL B C   1 
ATOM   4136  O  O   . VAL B 2  388  ? -12.560 -56.272  -0.776  1.00 80.58  ?  388  VAL B O   1 
ATOM   4137  C  CB  . VAL B 2  388  ? -14.341 -53.866  -1.176  1.00 76.47  ?  388  VAL B CB  1 
ATOM   4138  C  CG1 . VAL B 2  388  ? -15.505 -54.649  -1.763  1.00 81.06  ?  388  VAL B CG1 1 
ATOM   4139  C  CG2 . VAL B 2  388  ? -14.721 -52.414  -0.963  1.00 80.77  ?  388  VAL B CG2 1 
ATOM   4140  N  N   . PHE B 2  389  ? -14.273 -56.854  0.574   1.00 72.91  ?  389  PHE B N   1 
ATOM   4141  C  CA  . PHE B 2  389  ? -14.034 -58.284  0.485   1.00 79.07  ?  389  PHE B CA  1 
ATOM   4142  C  C   . PHE B 2  389  ? -15.256 -58.976  -0.101  1.00 85.37  ?  389  PHE B C   1 
ATOM   4143  O  O   . PHE B 2  389  ? -16.397 -58.573  0.142   1.00 83.17  ?  389  PHE B O   1 
ATOM   4144  C  CB  . PHE B 2  389  ? -13.701 -58.875  1.859   1.00 75.62  ?  389  PHE B CB  1 
ATOM   4145  C  CG  . PHE B 2  389  ? -12.412 -58.367  2.437   1.00 74.04  ?  389  PHE B CG  1 
ATOM   4146  C  CD1 . PHE B 2  389  ? -11.203 -58.931  2.067   1.00 71.81  ?  389  PHE B CD1 1 
ATOM   4147  C  CD2 . PHE B 2  389  ? -12.409 -57.319  3.342   1.00 78.23  ?  389  PHE B CD2 1 
ATOM   4148  C  CE1 . PHE B 2  389  ? -10.015 -58.464  2.595   1.00 75.03  ?  389  PHE B CE1 1 
ATOM   4149  C  CE2 . PHE B 2  389  ? -11.224 -56.847  3.872   1.00 67.97  ?  389  PHE B CE2 1 
ATOM   4150  C  CZ  . PHE B 2  389  ? -10.025 -57.420  3.498   1.00 70.96  ?  389  PHE B CZ  1 
ATOM   4151  N  N   . TYR B 2  390  ? -15.004 -60.022  -0.884  1.00 89.79  ?  390  TYR B N   1 
ATOM   4152  C  CA  . TYR B 2  390  ? -16.053 -60.782  -1.546  1.00 89.30  ?  390  TYR B CA  1 
ATOM   4153  C  C   . TYR B 2  390  ? -16.056 -62.206  -1.012  1.00 93.66  ?  390  TYR B C   1 
ATOM   4154  O  O   . TYR B 2  390  ? -15.016 -62.873  -1.002  1.00 98.18  ?  390  TYR B O   1 
ATOM   4155  C  CB  . TYR B 2  390  ? -15.859 -60.779  -3.065  1.00 90.93  ?  390  TYR B CB  1 
ATOM   4156  C  CG  . TYR B 2  390  ? -15.874 -59.397  -3.679  1.00 87.84  ?  390  TYR B CG  1 
ATOM   4157  C  CD1 . TYR B 2  390  ? -17.005 -58.594  -3.600  1.00 86.31  ?  390  TYR B CD1 1 
ATOM   4158  C  CD2 . TYR B 2  390  ? -14.760 -58.895  -4.339  1.00 88.79  ?  390  TYR B CD2 1 
ATOM   4159  C  CE1 . TYR B 2  390  ? -17.025 -57.330  -4.160  1.00 82.48  ?  390  TYR B CE1 1 
ATOM   4160  C  CE2 . TYR B 2  390  ? -14.771 -57.633  -4.903  1.00 92.53  ?  390  TYR B CE2 1 
ATOM   4161  C  CZ  . TYR B 2  390  ? -15.906 -56.855  -4.810  1.00 90.10  ?  390  TYR B CZ  1 
ATOM   4162  O  OH  . TYR B 2  390  ? -15.923 -55.598  -5.370  1.00 98.02  ?  390  TYR B OH  1 
ATOM   4163  N  N   . HIS B 2  391  ? -17.222 -62.663  -0.568  1.00 83.04  ?  391  HIS B N   1 
ATOM   4164  C  CA  . HIS B 2  391  ? -17.404 -64.003  -0.035  1.00 78.80  ?  391  HIS B CA  1 
ATOM   4165  C  C   . HIS B 2  391  ? -18.466 -64.740  -0.842  1.00 72.99  ?  391  HIS B C   1 
ATOM   4166  O  O   . HIS B 2  391  ? -19.162 -64.160  -1.679  1.00 74.84  ?  391  HIS B O   1 
ATOM   4167  C  CB  . HIS B 2  391  ? -17.805 -63.960  1.445   1.00 76.96  ?  391  HIS B CB  1 
ATOM   4168  C  CG  . HIS B 2  391  ? -16.806 -63.278  2.327   1.00 81.56  ?  391  HIS B CG  1 
ATOM   4169  N  ND1 . HIS B 2  391  ? -15.681 -63.912  2.807   1.00 84.51  ?  391  HIS B ND1 1 
ATOM   4170  C  CD2 . HIS B 2  391  ? -16.766 -62.017  2.819   1.00 85.19  ?  391  HIS B CD2 1 
ATOM   4171  C  CE1 . HIS B 2  391  ? -14.989 -63.071  3.555   1.00 81.89  ?  391  HIS B CE1 1 
ATOM   4172  N  NE2 . HIS B 2  391  ? -15.625 -61.914  3.578   1.00 84.25  ?  391  HIS B NE2 1 
ATOM   4173  N  N   . GLU B 2  392  ? -18.579 -66.038  -0.580  1.00 75.79  ?  392  GLU B N   1 
ATOM   4174  C  CA  . GLU B 2  392  ? -19.667 -66.813  -1.146  1.00 76.21  ?  392  GLU B CA  1 
ATOM   4175  C  C   . GLU B 2  392  ? -20.994 -66.346  -0.548  1.00 78.51  ?  392  GLU B C   1 
ATOM   4176  O  O   . GLU B 2  392  ? -21.027 -65.818  0.566   1.00 89.98  ?  392  GLU B O   1 
ATOM   4177  C  CB  . GLU B 2  392  ? -19.458 -68.302  -0.875  1.00 75.70  ?  392  GLU B CB  1 
ATOM   4178  C  CG  . GLU B 2  392  ? -18.333 -68.926  -1.690  1.00 80.06  ?  392  GLU B CG  1 
ATOM   4179  C  CD  . GLU B 2  392  ? -18.805 -69.473  -3.025  1.00 89.06  ?  392  GLU B CD  1 
ATOM   4180  O  OE1 . GLU B 2  392  ? -20.033 -69.532  -3.246  1.00 88.67  ?  392  GLU B OE1 1 
ATOM   4181  O  OE2 . GLU B 2  392  ? -17.947 -69.843  -3.855  1.00 99.44  -1 392  GLU B OE2 1 
ATOM   4182  N  N   . PRO B 2  393  ? -22.100 -66.511  -1.275  1.00 61.75  ?  393  PRO B N   1 
ATOM   4183  C  CA  . PRO B 2  393  ? -23.390 -66.027  -0.765  1.00 65.23  ?  393  PRO B CA  1 
ATOM   4184  C  C   . PRO B 2  393  ? -23.781 -66.713  0.538   1.00 68.02  ?  393  PRO B C   1 
ATOM   4185  O  O   . PRO B 2  393  ? -23.602 -67.921  0.710   1.00 54.26  ?  393  PRO B O   1 
ATOM   4186  C  CB  . PRO B 2  393  ? -24.370 -66.361  -1.897  1.00 57.40  ?  393  PRO B CB  1 
ATOM   4187  C  CG  . PRO B 2  393  ? -23.685 -67.411  -2.710  1.00 57.99  ?  393  PRO B CG  1 
ATOM   4188  C  CD  . PRO B 2  393  ? -22.225 -67.100  -2.619  1.00 59.17  ?  393  PRO B CD  1 
ATOM   4189  N  N   . VAL B 2  394  ? -24.318 -65.918  1.463   1.00 96.61  ?  394  VAL B N   1 
ATOM   4190  C  CA  . VAL B 2  394  ? -24.726 -66.389  2.781   1.00 90.49  ?  394  VAL B CA  1 
ATOM   4191  C  C   . VAL B 2  394  ? -26.236 -66.331  2.956   1.00 83.57  ?  394  VAL B C   1 
ATOM   4192  O  O   . VAL B 2  394  ? -26.733 -66.474  4.079   1.00 84.38  ?  394  VAL B O   1 
ATOM   4193  C  CB  . VAL B 2  394  ? -24.021 -65.601  3.896   1.00 87.22  ?  394  VAL B CB  1 
ATOM   4194  C  CG1 . VAL B 2  394  ? -22.515 -65.745  3.775   1.00 97.74  ?  394  VAL B CG1 1 
ATOM   4195  C  CG2 . VAL B 2  394  ? -24.425 -64.134  3.843   1.00 81.57  ?  394  VAL B CG2 1 
ATOM   4196  N  N   . GLU B 2  395  ? -26.983 -66.128  1.872   1.00 101.65 ?  395  GLU B N   1 
ATOM   4197  C  CA  . GLU B 2  395  ? -28.431 -65.966  1.924   1.00 106.01 ?  395  GLU B CA  1 
ATOM   4198  C  C   . GLU B 2  395  ? -29.170 -67.218  1.466   1.00 106.76 ?  395  GLU B C   1 
ATOM   4199  O  O   . GLU B 2  395  ? -30.313 -67.122  1.004   1.00 104.17 ?  395  GLU B O   1 
ATOM   4200  C  CB  . GLU B 2  395  ? -28.855 -64.769  1.074   1.00 102.45 ?  395  GLU B CB  1 
ATOM   4201  C  CG  . GLU B 2  395  ? -27.792 -63.694  0.941   1.00 107.64 ?  395  GLU B CG  1 
ATOM   4202  C  CD  . GLU B 2  395  ? -28.193 -62.601  -0.028  1.00 114.49 ?  395  GLU B CD  1 
ATOM   4203  O  OE1 . GLU B 2  395  ? -29.294 -62.699  -0.612  1.00 113.53 ?  395  GLU B OE1 1 
ATOM   4204  O  OE2 . GLU B 2  395  ? -27.406 -61.649  -0.213  1.00 123.36 -1 395  GLU B OE2 1 
ATOM   4205  N  N   . ALA B 2  396  ? -28.542 -68.389  1.592   1.00 71.22  ?  396  ALA B N   1 
ATOM   4206  C  CA  . ALA B 2  396  ? -29.072 -69.631  1.039   1.00 74.84  ?  396  ALA B CA  1 
ATOM   4207  C  C   . ALA B 2  396  ? -29.331 -69.472  -0.454  1.00 90.31  ?  396  ALA B C   1 
ATOM   4208  O  O   . ALA B 2  396  ? -28.408 -69.600  -1.265  1.00 98.84  ?  396  ALA B O   1 
ATOM   4209  C  CB  . ALA B 2  396  ? -30.344 -70.064  1.773   1.00 68.46  ?  396  ALA B CB  1 
ATOM   4210  N  N   . ARG B 2  397  ? -30.580 -69.187  -0.830  1.00 95.58  ?  397  ARG B N   1 
ATOM   4211  C  CA  . ARG B 2  397  ? -30.908 -68.925  -2.223  1.00 99.55  ?  397  ARG B CA  1 
ATOM   4212  C  C   . ARG B 2  397  ? -30.984 -67.422  -2.442  1.00 100.22 ?  397  ARG B C   1 
ATOM   4213  O  O   . ARG B 2  397  ? -31.938 -66.787  -1.969  1.00 100.13 ?  397  ARG B O   1 
ATOM   4214  C  CB  . ARG B 2  397  ? -32.231 -69.583  -2.609  1.00 99.95  ?  397  ARG B CB  1 
ATOM   4215  C  CG  . ARG B 2  397  ? -32.470 -69.619  -4.114  1.00 111.77 ?  397  ARG B CG  1 
ATOM   4216  C  CD  . ARG B 2  397  ? -33.825 -70.205  -4.478  1.00 105.14 ?  397  ARG B CD  1 
ATOM   4217  N  NE  . ARG B 2  397  ? -34.922 -69.344  -4.054  1.00 108.05 ?  397  ARG B NE  1 
ATOM   4218  C  CZ  . ARG B 2  397  ? -36.190 -69.520  -4.401  1.00 108.26 ?  397  ARG B CZ  1 
ATOM   4219  N  NH1 . ARG B 2  397  ? -36.561 -70.516  -5.189  1.00 104.57 ?  397  ARG B NH1 1 
ATOM   4220  N  NH2 . ARG B 2  397  ? -37.110 -68.672  -3.948  1.00 107.33 ?  397  ARG B NH2 1 
ATOM   4221  N  N   . PRO B 2  398  ? -30.023 -66.810  -3.129  1.00 89.15  ?  398  PRO B N   1 
ATOM   4222  C  CA  . PRO B 2  398  ? -30.143 -65.382  -3.447  1.00 87.62  ?  398  PRO B CA  1 
ATOM   4223  C  C   . PRO B 2  398  ? -30.968 -65.161  -4.705  1.00 92.19  ?  398  PRO B C   1 
ATOM   4224  O  O   . PRO B 2  398  ? -30.696 -65.768  -5.747  1.00 93.69  ?  398  PRO B O   1 
ATOM   4225  C  CB  . PRO B 2  398  ? -28.683 -64.939  -3.636  1.00 87.32  ?  398  PRO B CB  1 
ATOM   4226  C  CG  . PRO B 2  398  ? -27.830 -66.197  -3.386  1.00 85.98  ?  398  PRO B CG  1 
ATOM   4227  C  CD  . PRO B 2  398  ? -28.744 -67.352  -3.608  1.00 92.33  ?  398  PRO B CD  1 
ATOM   4228  N  N   . THR B 2  399  ? -31.976 -64.297  -4.625  1.00 106.47 ?  399  THR B N   1 
ATOM   4229  C  CA  . THR B 2  399  ? -32.884 -64.113  -5.748  1.00 111.16 ?  399  THR B CA  1 
ATOM   4230  C  C   . THR B 2  399  ? -33.562 -62.755  -5.644  1.00 106.05 ?  399  THR B C   1 
ATOM   4231  O  O   . THR B 2  399  ? -33.571 -62.119  -4.586  1.00 109.78 ?  399  THR B O   1 
ATOM   4232  C  CB  . THR B 2  399  ? -33.938 -65.224  -5.802  1.00 115.45 ?  399  THR B CB  1 
ATOM   4233  O  OG1 . THR B 2  399  ? -34.861 -64.960  -6.865  1.00 122.31 ?  399  THR B OG1 1 
ATOM   4234  C  CG2 . THR B 2  399  ? -34.697 -65.298  -4.484  1.00 107.04 ?  399  THR B CG2 1 
ATOM   4235  N  N   . ASN B 2  400  ? -34.126 -62.321  -6.769  1.00 87.83  ?  400  ASN B N   1 
ATOM   4236  C  CA  . ASN B 2  400  ? -34.952 -61.119  -6.819  1.00 89.48  ?  400  ASN B CA  1 
ATOM   4237  C  C   . ASN B 2  400  ? -36.304 -61.462  -6.210  1.00 90.69  ?  400  ASN B C   1 
ATOM   4238  O  O   . ASN B 2  400  ? -37.122 -62.143  -6.830  1.00 87.12  ?  400  ASN B O   1 
ATOM   4239  C  CB  . ASN B 2  400  ? -35.093 -60.627  -8.255  1.00 92.78  ?  400  ASN B CB  1 
ATOM   4240  C  CG  . ASN B 2  400  ? -35.474 -59.159  -8.339  1.00 97.40  ?  400  ASN B CG  1 
ATOM   4241  O  OD1 . ASN B 2  400  ? -35.962 -58.576  -7.372  1.00 94.14  ?  400  ASN B OD1 1 
ATOM   4242  N  ND2 . ASN B 2  400  ? -35.251 -58.554  -9.503  1.00 104.81 ?  400  ASN B ND2 1 
ATOM   4243  N  N   . GLN B 2  401  ? -36.539 -60.994  -4.981  1.00 87.91  ?  401  GLN B N   1 
ATOM   4244  C  CA  . GLN B 2  401  ? -37.728 -61.415  -4.247  1.00 77.64  ?  401  GLN B CA  1 
ATOM   4245  C  C   . GLN B 2  401  ? -38.995 -60.805  -4.834  1.00 77.94  ?  401  GLN B C   1 
ATOM   4246  O  O   . GLN B 2  401  ? -40.034 -61.472  -4.902  1.00 72.04  ?  401  GLN B O   1 
ATOM   4247  C  CB  . GLN B 2  401  ? -37.584 -61.054  -2.770  1.00 75.16  ?  401  GLN B CB  1 
ATOM   4248  C  CG  . GLN B 2  401  ? -36.458 -61.797  -2.065  1.00 76.28  ?  401  GLN B CG  1 
ATOM   4249  C  CD  . GLN B 2  401  ? -36.410 -61.516  -0.577  1.00 72.72  ?  401  GLN B CD  1 
ATOM   4250  O  OE1 . GLN B 2  401  ? -37.231 -60.769  -0.049  1.00 73.98  ?  401  GLN B OE1 1 
ATOM   4251  N  NE2 . GLN B 2  401  ? -35.445 -62.119  0.108   1.00 74.79  ?  401  GLN B NE2 1 
ATOM   4252  N  N   . THR B 2  402  ? -38.931 -59.545  -5.273  1.00 95.76  ?  402  THR B N   1 
ATOM   4253  C  CA  . THR B 2  402  ? -40.126 -58.908  -5.818  1.00 95.53  ?  402  THR B CA  1 
ATOM   4254  C  C   . THR B 2  402  ? -40.558 -59.551  -7.131  1.00 98.29  ?  402  THR B C   1 
ATOM   4255  O  O   . THR B 2  402  ? -41.758 -59.615  -7.419  1.00 98.50  ?  402  THR B O   1 
ATOM   4256  C  CB  . THR B 2  402  ? -39.900 -57.403  -6.001  1.00 97.55  ?  402  THR B CB  1 
ATOM   4257  O  OG1 . THR B 2  402  ? -41.102 -56.792  -6.491  1.00 99.19  ?  402  THR B OG1 1 
ATOM   4258  C  CG2 . THR B 2  402  ? -38.761 -57.128  -6.971  1.00 98.13  ?  402  THR B CG2 1 
ATOM   4259  N  N   . GLU B 2  403  ? -39.608 -60.043  -7.930  1.00 105.84 ?  403  GLU B N   1 
ATOM   4260  C  CA  . GLU B 2  403  ? -39.972 -60.738  -9.160  1.00 107.59 ?  403  GLU B CA  1 
ATOM   4261  C  C   . GLU B 2  403  ? -40.631 -62.077  -8.857  1.00 109.58 ?  403  GLU B C   1 
ATOM   4262  O  O   . GLU B 2  403  ? -41.580 -62.478  -9.540  1.00 116.04 ?  403  GLU B O   1 
ATOM   4263  C  CB  . GLU B 2  403  ? -38.739 -60.931  -10.041 1.00 114.04 ?  403  GLU B CB  1 
ATOM   4264  C  CG  . GLU B 2  403  ? -38.213 -59.646  -10.663 1.00 124.63 ?  403  GLU B CG  1 
ATOM   4265  C  CD  . GLU B 2  403  ? -39.274 -58.903  -11.453 1.00 139.45 ?  403  GLU B CD  1 
ATOM   4266  O  OE1 . GLU B 2  403  ? -39.962 -59.542  -12.277 1.00 138.02 ?  403  GLU B OE1 1 
ATOM   4267  O  OE2 . GLU B 2  403  ? -39.421 -57.679  -11.250 1.00 147.13 -1 403  GLU B OE2 1 
ATOM   4268  N  N   . GLU B 2  404  ? -40.143 -62.782  -7.833  1.00 74.40  ?  404  GLU B N   1 
ATOM   4269  C  CA  . GLU B 2  404  ? -40.773 -64.037  -7.438  1.00 67.59  ?  404  GLU B CA  1 
ATOM   4270  C  C   . GLU B 2  404  ? -42.145 -63.804  -6.823  1.00 65.46  ?  404  GLU B C   1 
ATOM   4271  O  O   . GLU B 2  404  ? -43.023 -64.668  -6.924  1.00 69.56  ?  404  GLU B O   1 
ATOM   4272  C  CB  . GLU B 2  404  ? -39.874 -64.794  -6.463  1.00 63.22  ?  404  GLU B CB  1 
ATOM   4273  C  CG  . GLU B 2  404  ? -38.592 -65.315  -7.086  1.00 77.87  ?  404  GLU B CG  1 
ATOM   4274  C  CD  . GLU B 2  404  ? -37.735 -66.078  -6.098  1.00 74.20  ?  404  GLU B CD  1 
ATOM   4275  O  OE1 . GLU B 2  404  ? -38.076 -66.084  -4.896  1.00 69.28  ?  404  GLU B OE1 1 
ATOM   4276  O  OE2 . GLU B 2  404  ? -36.721 -66.671  -6.523  1.00 78.37  -1 404  GLU B OE2 1 
ATOM   4277  N  N   . LEU B 2  405  ? -42.348 -62.651  -6.181  1.00 54.86  ?  405  LEU B N   1 
ATOM   4278  C  CA  . LEU B 2  405  ? -43.671 -62.327  -5.662  1.00 58.40  ?  405  LEU B CA  1 
ATOM   4279  C  C   . LEU B 2  405  ? -44.642 -62.027  -6.796  1.00 62.79  ?  405  LEU B C   1 
ATOM   4280  O  O   . LEU B 2  405  ? -45.818 -62.402  -6.731  1.00 65.72  ?  405  LEU B O   1 
ATOM   4281  C  CB  . LEU B 2  405  ? -43.586 -61.144  -4.698  1.00 57.46  ?  405  LEU B CB  1 
ATOM   4282  C  CG  . LEU B 2  405  ? -44.826 -60.881  -3.840  1.00 61.00  ?  405  LEU B CG  1 
ATOM   4283  C  CD1 . LEU B 2  405  ? -44.995 -61.963  -2.783  1.00 60.18  ?  405  LEU B CD1 1 
ATOM   4284  C  CD2 . LEU B 2  405  ? -44.759 -59.505  -3.197  1.00 54.30  ?  405  LEU B CD2 1 
ATOM   4285  N  N   . VAL B 2  406  ? -44.165 -61.353  -7.846  1.00 78.38  ?  406  VAL B N   1 
ATOM   4286  C  CA  . VAL B 2  406  ? -45.003 -61.108  -9.016  1.00 81.75  ?  406  VAL B CA  1 
ATOM   4287  C  C   . VAL B 2  406  ? -45.350 -62.420  -9.706  1.00 86.14  ?  406  VAL B C   1 
ATOM   4288  O  O   . VAL B 2  406  ? -46.479 -62.614  -10.173 1.00 89.89  ?  406  VAL B O   1 
ATOM   4289  C  CB  . VAL B 2  406  ? -44.307 -60.125  -9.975  1.00 65.45  ?  406  VAL B CB  1 
ATOM   4290  C  CG1 . VAL B 2  406  ? -45.083 -60.008  -11.276 1.00 64.39  ?  406  VAL B CG1 1 
ATOM   4291  C  CG2 . VAL B 2  406  ? -44.166 -58.760  -9.320  1.00 80.88  ?  406  VAL B CG2 1 
ATOM   4292  N  N   . ALA B 2  407  ? -44.392 -63.347  -9.775  1.00 89.25  ?  407  ALA B N   1 
ATOM   4293  C  CA  . ALA B 2  407  ? -44.670 -64.643  -10.381 1.00 88.84  ?  407  ALA B CA  1 
ATOM   4294  C  C   . ALA B 2  407  ? -45.675 -65.434  -9.553  1.00 93.92  ?  407  ALA B C   1 
ATOM   4295  O  O   . ALA B 2  407  ? -46.499 -66.171  -10.105 1.00 103.61 ?  407  ALA B O   1 
ATOM   4296  C  CB  . ALA B 2  407  ? -43.374 -65.434  -10.555 1.00 82.29  ?  407  ALA B CB  1 
ATOM   4297  N  N   . LEU B 2  408  ? -45.628 -65.287  -8.227  1.00 92.23  ?  408  LEU B N   1 
ATOM   4298  C  CA  . LEU B 2  408  ? -46.549 -66.028  -7.371  1.00 99.97  ?  408  LEU B CA  1 
ATOM   4299  C  C   . LEU B 2  408  ? -47.966 -65.476  -7.475  1.00 102.65 ?  408  LEU B C   1 
ATOM   4300  O  O   . LEU B 2  408  ? -48.932 -66.245  -7.547  1.00 107.72 ?  408  LEU B O   1 
ATOM   4301  C  CB  . LEU B 2  408  ? -46.061 -65.997  -5.922  1.00 99.63  ?  408  LEU B CB  1 
ATOM   4302  C  CG  . LEU B 2  408  ? -46.968 -66.651  -4.876  1.00 98.86  ?  408  LEU B CG  1 
ATOM   4303  C  CD1 . LEU B 2  408  ? -47.224 -68.112  -5.216  1.00 92.36  ?  408  LEU B CD1 1 
ATOM   4304  C  CD2 . LEU B 2  408  ? -46.367 -66.519  -3.486  1.00 90.16  ?  408  LEU B CD2 1 
ATOM   4305  N  N   . VAL B 2  409  ? -48.114 -64.149  -7.488  1.00 96.61  ?  409  VAL B N   1 
ATOM   4306  C  CA  . VAL B 2  409  ? -49.448 -63.569  -7.609  1.00 100.12 ?  409  VAL B CA  1 
ATOM   4307  C  C   . VAL B 2  409  ? -49.997 -63.777  -9.014  1.00 101.99 ?  409  VAL B C   1 
ATOM   4308  O  O   . VAL B 2  409  ? -51.218 -63.789  -9.214  1.00 107.63 ?  409  VAL B O   1 
ATOM   4309  C  CB  . VAL B 2  409  ? -49.435 -62.078  -7.220  1.00 96.99  ?  409  VAL B CB  1 
ATOM   4310  C  CG1 . VAL B 2  409  ? -48.916 -61.903  -5.800  1.00 94.07  ?  409  VAL B CG1 1 
ATOM   4311  C  CG2 . VAL B 2  409  ? -48.608 -61.269  -8.204  1.00 99.18  ?  409  VAL B CG2 1 
ATOM   4312  N  N   . SER B 2  410  ? -49.120 -63.946  -10.006 1.00 91.49  ?  410  SER B N   1 
ATOM   4313  C  CA  . SER B 2  410  ? -49.584 -64.283  -11.346 1.00 88.52  ?  410  SER B CA  1 
ATOM   4314  C  C   . SER B 2  410  ? -50.105 -65.713  -11.400 1.00 93.73  ?  410  SER B C   1 
ATOM   4315  O  O   . SER B 2  410  ? -51.134 -65.982  -12.031 1.00 94.56  ?  410  SER B O   1 
ATOM   4316  C  CB  . SER B 2  410  ? -48.459 -64.085  -12.360 1.00 83.76  ?  410  SER B CB  1 
ATOM   4317  O  OG  . SER B 2  410  ? -48.853 -64.536  -13.643 1.00 93.51  ?  410  SER B OG  1 
ATOM   4318  N  N   . GLU B 2  411  ? -49.405 -66.644  -10.745 1.00 99.56  ?  411  GLU B N   1 
ATOM   4319  C  CA  . GLU B 2  411  ? -49.891 -68.016  -10.661 1.00 94.55  ?  411  GLU B CA  1 
ATOM   4320  C  C   . GLU B 2  411  ? -51.181 -68.101  -9.857  1.00 96.91  ?  411  GLU B C   1 
ATOM   4321  O  O   . GLU B 2  411  ? -52.033 -68.953  -10.137 1.00 100.24 ?  411  GLU B O   1 
ATOM   4322  C  CB  . GLU B 2  411  ? -48.821 -68.915  -10.040 1.00 98.99  ?  411  GLU B CB  1 
ATOM   4323  C  CG  . GLU B 2  411  ? -47.584 -69.103  -10.903 1.00 111.37 ?  411  GLU B CG  1 
ATOM   4324  C  CD  . GLU B 2  411  ? -46.457 -69.792  -10.158 1.00 112.71 ?  411  GLU B CD  1 
ATOM   4325  O  OE1 . GLU B 2  411  ? -46.586 -69.991  -8.932  1.00 103.63 ?  411  GLU B OE1 1 
ATOM   4326  O  OE2 . GLU B 2  411  ? -45.441 -70.137  -10.799 1.00 111.64 -1 411  GLU B OE2 1 
ATOM   4327  N  N   . MET B 2  412  ? -51.343 -67.233  -8.856  1.00 88.99  ?  412  MET B N   1 
ATOM   4328  C  CA  . MET B 2  412  ? -52.577 -67.226  -8.077  1.00 88.15  ?  412  MET B CA  1 
ATOM   4329  C  C   . MET B 2  412  ? -53.738 -66.667  -8.889  1.00 82.38  ?  412  MET B C   1 
ATOM   4330  O  O   . MET B 2  412  ? -54.861 -67.178  -8.810  1.00 85.48  ?  412  MET B O   1 
ATOM   4331  C  CB  . MET B 2  412  ? -52.384 -66.420  -6.792  1.00 88.43  ?  412  MET B CB  1 
ATOM   4332  C  CG  . MET B 2  412  ? -51.566 -67.130  -5.728  1.00 92.24  ?  412  MET B CG  1 
ATOM   4333  S  SD  . MET B 2  412  ? -51.669 -66.326  -4.118  1.00 80.55  ?  412  MET B SD  1 
ATOM   4334  C  CE  . MET B 2  412  ? -50.816 -64.788  -4.451  1.00 76.67  ?  412  MET B CE  1 
ATOM   4335  N  N   . ALA B 2  413  ? -53.487 -65.617  -9.676  1.00 78.81  ?  413  ALA B N   1 
ATOM   4336  C  CA  . ALA B 2  413  ? -54.546 -65.040  -10.497 1.00 82.52  ?  413  ALA B CA  1 
ATOM   4337  C  C   . ALA B 2  413  ? -54.986 -66.005  -11.591 1.00 89.56  ?  413  ALA B C   1 
ATOM   4338  O  O   . ALA B 2  413  ? -56.170 -66.056  -11.943 1.00 87.19  ?  413  ALA B O   1 
ATOM   4339  C  CB  . ALA B 2  413  ? -54.080 -63.715  -11.102 1.00 83.69  ?  413  ALA B CB  1 
ATOM   4340  N  N   . ALA B 2  414  ? -54.047 -66.780  -12.138 1.00 126.12 ?  414  ALA B N   1 
ATOM   4341  C  CA  . ALA B 2  414  ? -54.389 -67.783  -13.137 1.00 121.77 ?  414  ALA B CA  1 
ATOM   4342  C  C   . ALA B 2  414  ? -55.101 -68.989  -12.540 1.00 126.80 ?  414  ALA B C   1 
ATOM   4343  O  O   . ALA B 2  414  ? -55.654 -69.795  -13.296 1.00 135.38 ?  414  ALA B O   1 
ATOM   4344  C  CB  . ALA B 2  414  ? -53.128 -68.239  -13.875 1.00 122.55 ?  414  ALA B CB  1 
ATOM   4345  N  N   . GLY B 2  415  ? -55.102 -69.132  -11.216 1.00 79.83  ?  415  GLY B N   1 
ATOM   4346  C  CA  . GLY B 2  415  ? -55.775 -70.244  -10.575 1.00 70.21  ?  415  GLY B CA  1 
ATOM   4347  C  C   . GLY B 2  415  ? -55.014 -71.548  -10.584 1.00 76.67  ?  415  GLY B C   1 
ATOM   4348  O  O   . GLY B 2  415  ? -55.613 -72.603  -10.357 1.00 79.98  ?  415  GLY B O   1 
ATOM   4349  N  N   . ARG B 2  416  ? -53.704 -71.511  -10.835 1.00 117.58 ?  416  ARG B N   1 
ATOM   4350  C  CA  . ARG B 2  416  ? -52.925 -72.741  -10.908 1.00 126.02 ?  416  ARG B CA  1 
ATOM   4351  C  C   . ARG B 2  416  ? -52.600 -73.300  -9.529  1.00 125.62 ?  416  ARG B C   1 
ATOM   4352  O  O   . ARG B 2  416  ? -52.480 -74.521  -9.374  1.00 129.57 ?  416  ARG B O   1 
ATOM   4353  C  CB  . ARG B 2  416  ? -51.631 -72.499  -11.686 1.00 123.58 ?  416  ARG B CB  1 
ATOM   4354  C  CG  . ARG B 2  416  ? -51.848 -72.101  -13.133 1.00 114.33 ?  416  ARG B CG  1 
ATOM   4355  C  CD  . ARG B 2  416  ? -52.411 -73.252  -13.945 1.00 125.05 ?  416  ARG B CD  1 
ATOM   4356  N  NE  . ARG B 2  416  ? -52.552 -72.904  -15.353 1.00 143.38 ?  416  ARG B NE  1 
ATOM   4357  C  CZ  . ARG B 2  416  ? -53.644 -72.374  -15.887 1.00 144.75 ?  416  ARG B CZ  1 
ATOM   4358  N  NH1 . ARG B 2  416  ? -54.716 -72.117  -15.156 1.00 135.08 ?  416  ARG B NH1 1 
ATOM   4359  N  NH2 . ARG B 2  416  ? -53.662 -72.097  -17.188 1.00 142.09 ?  416  ARG B NH2 1 
ATOM   4360  N  N   . VAL B 2  417  ? -52.459 -72.440  -8.528  1.00 153.20 ?  417  VAL B N   1 
ATOM   4361  C  CA  . VAL B 2  417  ? -52.066 -72.879  -7.195  1.00 156.59 ?  417  VAL B CA  1 
ATOM   4362  C  C   . VAL B 2  417  ? -53.267 -73.478  -6.476  1.00 150.58 ?  417  VAL B C   1 
ATOM   4363  O  O   . VAL B 2  417  ? -54.400 -72.997  -6.602  1.00 151.31 ?  417  VAL B O   1 
ATOM   4364  C  CB  . VAL B 2  417  ? -51.457 -71.709  -6.400  1.00 154.84 ?  417  VAL B CB  1 
ATOM   4365  C  CG1 . VAL B 2  417  ? -50.192 -71.214  -7.083  1.00 157.30 ?  417  VAL B CG1 1 
ATOM   4366  C  CG2 . VAL B 2  417  ? -52.458 -70.577  -6.265  1.00 147.78 ?  417  VAL B CG2 1 
ATOM   4367  N  N   . GLU B 2  418  ? -53.020 -74.553  -5.723  1.00 94.84  ?  418  GLU B N   1 
ATOM   4368  C  CA  . GLU B 2  418  ? -54.045 -75.199  -4.919  1.00 96.67  ?  418  GLU B CA  1 
ATOM   4369  C  C   . GLU B 2  418  ? -53.763 -75.162  -3.426  1.00 90.54  ?  418  GLU B C   1 
ATOM   4370  O  O   . GLU B 2  418  ? -54.709 -75.262  -2.638  1.00 87.39  ?  418  GLU B O   1 
ATOM   4371  C  CB  . GLU B 2  418  ? -54.228 -76.664  -5.349  1.00 105.06 ?  418  GLU B CB  1 
ATOM   4372  C  CG  . GLU B 2  418  ? -54.519 -76.848  -6.831  1.00 118.68 ?  418  GLU B CG  1 
ATOM   4373  C  CD  . GLU B 2  418  ? -54.594 -78.309  -7.235  1.00 127.29 ?  418  GLU B CD  1 
ATOM   4374  O  OE1 . GLU B 2  418  ? -54.439 -79.180  -6.354  1.00 125.89 ?  418  GLU B OE1 1 
ATOM   4375  O  OE2 . GLU B 2  418  ? -54.804 -78.585  -8.435  1.00 126.90 -1 418  GLU B OE2 1 
ATOM   4376  N  N   . THR B 2  419  ? -52.503 -75.021  -3.017  1.00 120.22 ?  419  THR B N   1 
ATOM   4377  C  CA  . THR B 2  419  ? -52.133 -74.929  -1.611  1.00 113.58 ?  419  THR B CA  1 
ATOM   4378  C  C   . THR B 2  419  ? -50.986 -73.941  -1.473  1.00 111.51 ?  419  THR B C   1 
ATOM   4379  O  O   . THR B 2  419  ? -49.991 -74.039  -2.198  1.00 120.02 ?  419  THR B O   1 
ATOM   4380  C  CB  . THR B 2  419  ? -51.726 -76.296  -1.046  1.00 104.14 ?  419  THR B CB  1 
ATOM   4381  O  OG1 . THR B 2  419  ? -52.750 -77.257  -1.328  1.00 108.21 ?  419  THR B OG1 1 
ATOM   4382  C  CG2 . THR B 2  419  ? -51.517 -76.209  0.458   1.00 95.47  ?  419  THR B CG2 1 
ATOM   4383  N  N   . LEU B 2  420  ? -51.127 -72.993  -0.549  1.00 73.01  ?  420  LEU B N   1 
ATOM   4384  C  CA  . LEU B 2  420  ? -50.131 -71.947  -0.334  1.00 69.21  ?  420  LEU B CA  1 
ATOM   4385  C  C   . LEU B 2  420  ? -49.744 -71.927  1.138   1.00 71.85  ?  420  LEU B C   1 
ATOM   4386  O  O   . LEU B 2  420  ? -50.570 -71.600  1.996   1.00 69.88  ?  420  LEU B O   1 
ATOM   4387  C  CB  . LEU B 2  420  ? -50.663 -70.584  -0.779  1.00 64.22  ?  420  LEU B CB  1 
ATOM   4388  C  CG  . LEU B 2  420  ? -49.680 -69.417  -0.691  1.00 63.19  ?  420  LEU B CG  1 
ATOM   4389  C  CD1 . LEU B 2  420  ? -48.417 -69.725  -1.471  1.00 74.94  ?  420  LEU B CD1 1 
ATOM   4390  C  CD2 . LEU B 2  420  ? -50.328 -68.148  -1.213  1.00 69.44  ?  420  LEU B CD2 1 
ATOM   4391  N  N   . ILE B 2  421  ? -48.493 -72.275  1.428   1.00 82.51  ?  421  ILE B N   1 
ATOM   4392  C  CA  . ILE B 2  421  ? -47.955 -72.272  2.783   1.00 72.71  ?  421  ILE B CA  1 
ATOM   4393  C  C   . ILE B 2  421  ? -47.039 -71.065  2.928   1.00 79.46  ?  421  ILE B C   1 
ATOM   4394  O  O   . ILE B 2  421  ? -46.119 -70.877  2.123   1.00 78.88  ?  421  ILE B O   1 
ATOM   4395  C  CB  . ILE B 2  421  ? -47.198 -73.576  3.096   1.00 73.34  ?  421  ILE B CB  1 
ATOM   4396  C  CG1 . ILE B 2  421  ? -48.135 -74.782  2.998   1.00 71.83  ?  421  ILE B CG1 1 
ATOM   4397  C  CG2 . ILE B 2  421  ? -46.559 -73.505  4.472   1.00 72.65  ?  421  ILE B CG2 1 
ATOM   4398  C  CD1 . ILE B 2  421  ? -47.967 -75.585  1.729   1.00 78.81  ?  421  ILE B CD1 1 
ATOM   4399  N  N   . MET B 2  422  ? -47.288 -70.250  3.949   1.00 87.58  ?  422  MET B N   1 
ATOM   4400  C  CA  . MET B 2  422  ? -46.502 -69.051  4.204   1.00 80.53  ?  422  MET B CA  1 
ATOM   4401  C  C   . MET B 2  422  ? -45.893 -69.142  5.594   1.00 79.43  ?  422  MET B C   1 
ATOM   4402  O  O   . MET B 2  422  ? -46.578 -69.516  6.550   1.00 77.85  ?  422  MET B O   1 
ATOM   4403  C  CB  . MET B 2  422  ? -47.362 -67.793  4.089   1.00 70.38  ?  422  MET B CB  1 
ATOM   4404  C  CG  . MET B 2  422  ? -48.187 -67.706  2.822   1.00 75.90  ?  422  MET B CG  1 
ATOM   4405  S  SD  . MET B 2  422  ? -49.576 -66.574  3.016   1.00 85.76  ?  422  MET B SD  1 
ATOM   4406  C  CE  . MET B 2  422  ? -50.890 -67.514  2.247   1.00 97.38  ?  422  MET B CE  1 
ATOM   4407  N  N   . ILE B 2  423  ? -44.610 -68.798  5.703   1.00 79.61  ?  423  ILE B N   1 
ATOM   4408  C  CA  . ILE B 2  423  ? -43.911 -68.827  6.984   1.00 76.56  ?  423  ILE B CA  1 
ATOM   4409  C  C   . ILE B 2  423  ? -43.509 -67.408  7.368   1.00 78.79  ?  423  ILE B C   1 
ATOM   4410  O  O   . ILE B 2  423  ? -42.384 -66.972  7.094   1.00 80.92  ?  423  ILE B O   1 
ATOM   4411  C  CB  . ILE B 2  423  ? -42.685 -69.757  6.930   1.00 71.03  ?  423  ILE B CB  1 
ATOM   4412  C  CG1 . ILE B 2  423  ? -43.091 -71.141  6.421   1.00 76.88  ?  423  ILE B CG1 1 
ATOM   4413  C  CG2 . ILE B 2  423  ? -42.041 -69.874  8.301   1.00 74.43  ?  423  ILE B CG2 1 
ATOM   4414  C  CD1 . ILE B 2  423  ? -41.969 -72.154  6.450   1.00 81.34  ?  423  ILE B CD1 1 
ATOM   4415  N  N   . GLY B 2  424  ? -44.425 -66.680  8.000   1.00 78.90  ?  424  GLY B N   1 
ATOM   4416  C  CA  . GLY B 2  424  ? -44.163 -65.311  8.402   1.00 79.87  ?  424  GLY B CA  1 
ATOM   4417  C  C   . GLY B 2  424  ? -44.114 -64.361  7.217   1.00 81.79  ?  424  GLY B C   1 
ATOM   4418  O  O   . GLY B 2  424  ? -44.348 -64.725  6.065   1.00 94.42  ?  424  GLY B O   1 
ATOM   4419  N  N   . GLY B 2  425  ? -43.803 -63.104  7.525   1.00 91.35  ?  425  GLY B N   1 
ATOM   4420  C  CA  . GLY B 2  425  ? -43.630 -62.078  6.526   1.00 113.47 ?  425  GLY B CA  1 
ATOM   4421  C  C   . GLY B 2  425  ? -44.836 -61.188  6.305   1.00 118.06 ?  425  GLY B C   1 
ATOM   4422  O  O   . GLY B 2  425  ? -44.674 -60.074  5.792   1.00 118.87 ?  425  GLY B O   1 
ATOM   4423  N  N   . ASN B 2  426  ? -46.035 -61.649  6.674   1.00 96.86  ?  426  ASN B N   1 
ATOM   4424  C  CA  . ASN B 2  426  ? -47.273 -60.892  6.512   1.00 97.44  ?  426  ASN B CA  1 
ATOM   4425  C  C   . ASN B 2  426  ? -47.434 -60.425  5.068   1.00 93.63  ?  426  ASN B C   1 
ATOM   4426  O  O   . ASN B 2  426  ? -47.297 -59.228  4.785   1.00 92.98  ?  426  ASN B O   1 
ATOM   4427  C  CB  . ASN B 2  426  ? -47.300 -59.697  7.467   1.00 93.19  ?  426  ASN B CB  1 
ATOM   4428  C  CG  . ASN B 2  426  ? -48.704 -59.209  7.752   1.00 89.78  ?  426  ASN B CG  1 
ATOM   4429  O  OD1 . ASN B 2  426  ? -49.679 -59.734  7.214   1.00 92.99  ?  426  ASN B OD1 1 
ATOM   4430  N  ND2 . ASN B 2  426  ? -48.816 -58.195  8.602   1.00 89.33  ?  426  ASN B ND2 1 
ATOM   4431  N  N   . PRO B 2  427  ? -47.722 -61.333  4.131   1.00 96.77  ?  427  PRO B N   1 
ATOM   4432  C  CA  . PRO B 2  427  ? -47.764 -60.928  2.718   1.00 94.34  ?  427  PRO B CA  1 
ATOM   4433  C  C   . PRO B 2  427  ? -48.914 -59.996  2.384   1.00 98.84  ?  427  PRO B C   1 
ATOM   4434  O  O   . PRO B 2  427  ? -48.767 -59.151  1.493   1.00 101.59 ?  427  PRO B O   1 
ATOM   4435  C  CB  . PRO B 2  427  ? -47.891 -62.265  1.971   1.00 97.86  ?  427  PRO B CB  1 
ATOM   4436  C  CG  . PRO B 2  427  ? -47.489 -63.316  2.970   1.00 98.79  ?  427  PRO B CG  1 
ATOM   4437  C  CD  . PRO B 2  427  ? -47.932 -62.780  4.291   1.00 103.07 ?  427  PRO B CD  1 
ATOM   4438  N  N   . VAL B 2  428  ? -50.054 -60.123  3.068   1.00 66.53  ?  428  VAL B N   1 
ATOM   4439  C  CA  . VAL B 2  428  ? -51.215 -59.298  2.741   1.00 65.42  ?  428  VAL B CA  1 
ATOM   4440  C  C   . VAL B 2  428  ? -50.912 -57.826  2.997   1.00 61.54  ?  428  VAL B C   1 
ATOM   4441  O  O   . VAL B 2  428  ? -51.342 -56.945  2.241   1.00 59.14  ?  428  VAL B O   1 
ATOM   4442  C  CB  . VAL B 2  428  ? -52.446 -59.777  3.534   1.00 64.87  ?  428  VAL B CB  1 
ATOM   4443  C  CG1 . VAL B 2  428  ? -53.522 -58.700  3.580   1.00 65.82  ?  428  VAL B CG1 1 
ATOM   4444  C  CG2 . VAL B 2  428  ? -52.996 -61.060  2.931   1.00 76.91  ?  428  VAL B CG2 1 
ATOM   4445  N  N   . TYR B 2  429  ? -50.151 -57.538  4.049   1.00 71.07  ?  429  TYR B N   1 
ATOM   4446  C  CA  . TYR B 2  429  ? -49.836 -56.162  4.408   1.00 71.25  ?  429  TYR B CA  1 
ATOM   4447  C  C   . TYR B 2  429  ? -48.550 -55.661  3.765   1.00 72.51  ?  429  TYR B C   1 
ATOM   4448  O  O   . TYR B 2  429  ? -48.428 -54.460  3.496   1.00 69.51  ?  429  TYR B O   1 
ATOM   4449  C  CB  . TYR B 2  429  ? -49.735 -56.035  5.931   1.00 79.43  ?  429  TYR B CB  1 
ATOM   4450  C  CG  . TYR B 2  429  ? -49.278 -54.678  6.413   1.00 83.70  ?  429  TYR B CG  1 
ATOM   4451  C  CD1 . TYR B 2  429  ? -50.127 -53.580  6.366   1.00 81.41  ?  429  TYR B CD1 1 
ATOM   4452  C  CD2 . TYR B 2  429  ? -47.994 -54.494  6.907   1.00 79.69  ?  429  TYR B CD2 1 
ATOM   4453  C  CE1 . TYR B 2  429  ? -49.711 -52.337  6.804   1.00 78.09  ?  429  TYR B CE1 1 
ATOM   4454  C  CE2 . TYR B 2  429  ? -47.569 -53.256  7.346   1.00 71.99  ?  429  TYR B CE2 1 
ATOM   4455  C  CZ  . TYR B 2  429  ? -48.431 -52.182  7.292   1.00 72.75  ?  429  TYR B CZ  1 
ATOM   4456  O  OH  . TYR B 2  429  ? -48.005 -50.950  7.730   1.00 75.85  ?  429  TYR B OH  1 
ATOM   4457  N  N   . ASN B 2  430  ? -47.593 -56.551  3.497   1.00 110.09 ?  430  ASN B N   1 
ATOM   4458  C  CA  . ASN B 2  430  ? -46.278 -56.140  3.024   1.00 108.26 ?  430  ASN B CA  1 
ATOM   4459  C  C   . ASN B 2  430  ? -46.167 -56.074  1.508   1.00 111.08 ?  430  ASN B C   1 
ATOM   4460  O  O   . ASN B 2  430  ? -45.308 -55.345  0.998   1.00 106.72 ?  430  ASN B O   1 
ATOM   4461  C  CB  . ASN B 2  430  ? -45.206 -57.091  3.562   1.00 107.53 ?  430  ASN B CB  1 
ATOM   4462  C  CG  . ASN B 2  430  ? -44.847 -56.804  5.003   1.00 110.72 ?  430  ASN B CG  1 
ATOM   4463  O  OD1 . ASN B 2  430  ? -45.009 -55.682  5.482   1.00 115.11 ?  430  ASN B OD1 1 
ATOM   4464  N  ND2 . ASN B 2  430  ? -44.352 -57.816  5.703   1.00 111.57 ?  430  ASN B ND2 1 
ATOM   4465  N  N   . ALA B 2  431  ? -46.998 -56.816  0.781   1.00 93.54  ?  431  ALA B N   1 
ATOM   4466  C  CA  . ALA B 2  431  ? -46.913 -56.817  -0.669  1.00 92.68  ?  431  ALA B CA  1 
ATOM   4467  C  C   . ALA B 2  431  ? -47.297 -55.448  -1.229  1.00 90.38  ?  431  ALA B C   1 
ATOM   4468  O  O   . ALA B 2  431  ? -48.094 -54.723  -0.626  1.00 85.60  ?  431  ALA B O   1 
ATOM   4469  C  CB  . ALA B 2  431  ? -47.822 -57.892  -1.260  1.00 97.05  ?  431  ALA B CB  1 
ATOM   4470  N  N   . PRO B 2  432  ? -46.730 -55.065  -2.373  1.00 84.75  ?  432  PRO B N   1 
ATOM   4471  C  CA  . PRO B 2  432  ? -47.097 -53.785  -2.987  1.00 89.22  ?  432  PRO B CA  1 
ATOM   4472  C  C   . PRO B 2  432  ? -48.577 -53.736  -3.342  1.00 89.20  ?  432  PRO B C   1 
ATOM   4473  O  O   . PRO B 2  432  ? -49.242 -54.760  -3.512  1.00 84.31  ?  432  PRO B O   1 
ATOM   4474  C  CB  . PRO B 2  432  ? -46.219 -53.727  -4.243  1.00 90.86  ?  432  PRO B CB  1 
ATOM   4475  C  CG  . PRO B 2  432  ? -45.063 -54.617  -3.934  1.00 84.52  ?  432  PRO B CG  1 
ATOM   4476  C  CD  . PRO B 2  432  ? -45.625 -55.725  -3.091  1.00 77.14  ?  432  PRO B CD  1 
ATOM   4477  N  N   . GLY B 2  433  ? -49.090 -52.509  -3.459  1.00 106.27 ?  433  GLY B N   1 
ATOM   4478  C  CA  . GLY B 2  433  ? -50.514 -52.327  -3.679  1.00 114.94 ?  433  GLY B CA  1 
ATOM   4479  C  C   . GLY B 2  433  ? -50.986 -52.759  -5.052  1.00 115.17 ?  433  GLY B C   1 
ATOM   4480  O  O   . GLY B 2  433  ? -52.135 -53.182  -5.209  1.00 110.60 ?  433  GLY B O   1 
ATOM   4481  N  N   . ASP B 2  434  ? -50.121 -52.662  -6.061  1.00 157.68 ?  434  ASP B N   1 
ATOM   4482  C  CA  . ASP B 2  434  ? -50.506 -53.004  -7.425  1.00 162.49 ?  434  ASP B CA  1 
ATOM   4483  C  C   . ASP B 2  434  ? -50.557 -54.505  -7.675  1.00 157.18 ?  434  ASP B C   1 
ATOM   4484  O  O   . ASP B 2  434  ? -50.899 -54.917  -8.789  1.00 162.57 ?  434  ASP B O   1 
ATOM   4485  C  CB  . ASP B 2  434  ? -49.545 -52.351  -8.424  1.00 168.57 ?  434  ASP B CB  1 
ATOM   4486  C  CG  . ASP B 2  434  ? -48.092 -52.657  -8.122  1.00 161.37 ?  434  ASP B CG  1 
ATOM   4487  O  OD1 . ASP B 2  434  ? -47.816 -53.235  -7.051  1.00 166.35 ?  434  ASP B OD1 1 
ATOM   4488  O  OD2 . ASP B 2  434  ? -47.226 -52.318  -8.957  1.00 154.93 -1 434  ASP B OD2 1 
ATOM   4489  N  N   . LEU B 2  435  ? -50.230 -55.329  -6.680  1.00 104.53 ?  435  LEU B N   1 
ATOM   4490  C  CA  . LEU B 2  435  ? -50.245 -56.775  -6.853  1.00 100.65 ?  435  LEU B CA  1 
ATOM   4491  C  C   . LEU B 2  435  ? -51.556 -57.417  -6.418  1.00 101.81 ?  435  LEU B C   1 
ATOM   4492  O  O   . LEU B 2  435  ? -51.882 -58.507  -6.903  1.00 104.24 ?  435  LEU B O   1 
ATOM   4493  C  CB  . LEU B 2  435  ? -49.085 -57.412  -6.080  1.00 95.57  ?  435  LEU B CB  1 
ATOM   4494  C  CG  . LEU B 2  435  ? -47.693 -57.192  -6.676  1.00 93.79  ?  435  LEU B CG  1 
ATOM   4495  C  CD1 . LEU B 2  435  ? -46.653 -58.037  -5.956  1.00 85.46  ?  435  LEU B CD1 1 
ATOM   4496  C  CD2 . LEU B 2  435  ? -47.688 -57.486  -8.169  1.00 106.08 ?  435  LEU B CD2 1 
ATOM   4497  N  N   . ARG B 2  436  ? -52.306 -56.771  -5.523  1.00 114.71 ?  436  ARG B N   1 
ATOM   4498  C  CA  . ARG B 2  436  ? -53.602 -57.264  -5.051  1.00 116.18 ?  436  ARG B CA  1 
ATOM   4499  C  C   . ARG B 2  436  ? -53.473 -58.673  -4.465  1.00 116.56 ?  436  ARG B C   1 
ATOM   4500  O  O   . ARG B 2  436  ? -54.095 -59.631  -4.927  1.00 122.54 ?  436  ARG B O   1 
ATOM   4501  C  CB  . ARG B 2  436  ? -54.646 -57.227  -6.174  1.00 126.10 ?  436  ARG B CB  1 
ATOM   4502  C  CG  . ARG B 2  436  ? -54.861 -55.854  -6.802  1.00 123.95 ?  436  ARG B CG  1 
ATOM   4503  C  CD  . ARG B 2  436  ? -54.871 -54.746  -5.759  1.00 125.85 ?  436  ARG B CD  1 
ATOM   4504  N  NE  . ARG B 2  436  ? -56.205 -54.502  -5.224  1.00 130.04 ?  436  ARG B NE  1 
ATOM   4505  C  CZ  . ARG B 2  436  ? -56.451 -53.860  -4.091  1.00 130.16 ?  436  ARG B CZ  1 
ATOM   4506  N  NH1 . ARG B 2  436  ? -55.472 -53.380  -3.341  1.00 130.69 ?  436  ARG B NH1 1 
ATOM   4507  N  NH2 . ARG B 2  436  ? -57.711 -53.694  -3.699  1.00 128.04 ?  436  ARG B NH2 1 
ATOM   4508  N  N   . PHE B 2  437  ? -52.643 -58.779  -3.423  1.00 82.37  ?  437  PHE B N   1 
ATOM   4509  C  CA  . PHE B 2  437  ? -52.390 -60.081  -2.812  1.00 80.44  ?  437  PHE B CA  1 
ATOM   4510  C  C   . PHE B 2  437  ? -53.631 -60.617  -2.107  1.00 89.82  ?  437  PHE B C   1 
ATOM   4511  O  O   . PHE B 2  437  ? -53.912 -61.819  -2.168  1.00 90.27  ?  437  PHE B O   1 
ATOM   4512  C  CB  . PHE B 2  437  ? -51.219 -59.987  -1.833  1.00 69.76  ?  437  PHE B CB  1 
ATOM   4513  C  CG  . PHE B 2  437  ? -50.578 -61.314  -1.525  1.00 69.58  ?  437  PHE B CG  1 
ATOM   4514  C  CD1 . PHE B 2  437  ? -51.111 -62.150  -0.557  1.00 71.40  ?  437  PHE B CD1 1 
ATOM   4515  C  CD2 . PHE B 2  437  ? -49.440 -61.723  -2.202  1.00 70.36  ?  437  PHE B CD2 1 
ATOM   4516  C  CE1 . PHE B 2  437  ? -50.524 -63.371  -0.273  1.00 65.76  ?  437  PHE B CE1 1 
ATOM   4517  C  CE2 . PHE B 2  437  ? -48.848 -62.941  -1.921  1.00 68.74  ?  437  PHE B CE2 1 
ATOM   4518  C  CZ  . PHE B 2  437  ? -49.391 -63.766  -0.955  1.00 62.94  ?  437  PHE B CZ  1 
ATOM   4519  N  N   . ALA B 2  438  ? -54.383 -59.743  -1.435  1.00 89.88  ?  438  ALA B N   1 
ATOM   4520  C  CA  . ALA B 2  438  ? -55.553 -60.194  -0.688  1.00 88.75  ?  438  ALA B CA  1 
ATOM   4521  C  C   . ALA B 2  438  ? -56.639 -60.723  -1.617  1.00 97.62  ?  438  ALA B C   1 
ATOM   4522  O  O   . ALA B 2  438  ? -57.310 -61.712  -1.297  1.00 101.17 ?  438  ALA B O   1 
ATOM   4523  C  CB  . ALA B 2  438  ? -56.094 -59.056  0.177   1.00 95.28  ?  438  ALA B CB  1 
ATOM   4524  N  N   . ASP B 2  439  ? -56.828 -60.081  -2.772  1.00 123.58 ?  439  ASP B N   1 
ATOM   4525  C  CA  . ASP B 2  439  ? -57.861 -60.527  -3.701  1.00 127.25 ?  439  ASP B CA  1 
ATOM   4526  C  C   . ASP B 2  439  ? -57.483 -61.850  -4.355  1.00 127.99 ?  439  ASP B C   1 
ATOM   4527  O  O   . ASP B 2  439  ? -58.321 -62.751  -4.476  1.00 126.46 ?  439  ASP B O   1 
ATOM   4528  C  CB  . ASP B 2  439  ? -58.113 -59.454  -4.760  1.00 131.42 ?  439  ASP B CB  1 
ATOM   4529  C  CG  . ASP B 2  439  ? -58.580 -58.141  -4.158  1.00 128.84 ?  439  ASP B CG  1 
ATOM   4530  O  OD1 . ASP B 2  439  ? -58.629 -58.040  -2.915  1.00 122.30 ?  439  ASP B OD1 1 
ATOM   4531  O  OD2 . ASP B 2  439  ? -58.896 -57.210  -4.929  1.00 131.37 -1 439  ASP B OD2 1 
ATOM   4532  N  N   . ARG B 2  440  ? -56.225 -61.988  -4.780  1.00 133.54 ?  440  ARG B N   1 
ATOM   4533  C  CA  . ARG B 2  440  ? -55.775 -63.233  -5.390  1.00 131.85 ?  440  ARG B CA  1 
ATOM   4534  C  C   . ARG B 2  440  ? -55.602 -64.347  -4.368  1.00 125.20 ?  440  ARG B C   1 
ATOM   4535  O  O   . ARG B 2  440  ? -55.578 -65.522  -4.747  1.00 129.70 ?  440  ARG B O   1 
ATOM   4536  C  CB  . ARG B 2  440  ? -54.459 -63.011  -6.138  1.00 125.21 ?  440  ARG B CB  1 
ATOM   4537  C  CG  . ARG B 2  440  ? -54.626 -62.639  -7.603  1.00 123.74 ?  440  ARG B CG  1 
ATOM   4538  C  CD  . ARG B 2  440  ? -54.915 -61.157  -7.768  1.00 125.17 ?  440  ARG B CD  1 
ATOM   4539  N  NE  . ARG B 2  440  ? -54.934 -60.757  -9.169  1.00 128.34 ?  440  ARG B NE  1 
ATOM   4540  C  CZ  . ARG B 2  440  ? -54.004 -60.008  -9.746  1.00 130.34 ?  440  ARG B CZ  1 
ATOM   4541  N  NH1 . ARG B 2  440  ? -52.958 -59.564  -9.069  1.00 126.38 ?  440  ARG B NH1 1 
ATOM   4542  N  NH2 . ARG B 2  440  ? -54.126 -59.700  -11.034 1.00 141.05 ?  440  ARG B NH2 1 
ATOM   4543  N  N   . MET B 2  441  ? -55.478 -64.002  -3.084  1.00 100.60 ?  441  MET B N   1 
ATOM   4544  C  CA  . MET B 2  441  ? -55.331 -65.019  -2.048  1.00 99.52  ?  441  MET B CA  1 
ATOM   4545  C  C   . MET B 2  441  ? -56.565 -65.906  -1.951  1.00 98.39  ?  441  MET B C   1 
ATOM   4546  O  O   . MET B 2  441  ? -56.471 -67.053  -1.500  1.00 93.56  ?  441  MET B O   1 
ATOM   4547  C  CB  . MET B 2  441  ? -55.049 -64.350  -0.704  1.00 95.00  ?  441  MET B CB  1 
ATOM   4548  C  CG  . MET B 2  441  ? -54.553 -65.284  0.377   1.00 98.21  ?  441  MET B CG  1 
ATOM   4549  S  SD  . MET B 2  441  ? -54.158 -64.377  1.881   1.00 103.90 ?  441  MET B SD  1 
ATOM   4550  C  CE  . MET B 2  441  ? -53.907 -65.727  3.020   1.00 71.46  ?  441  MET B CE  1 
ATOM   4551  N  N   . ALA B 2  442  ? -57.728 -65.400  -2.369  1.00 131.79 ?  442  ALA B N   1 
ATOM   4552  C  CA  . ALA B 2  442  ? -58.942 -66.208  -2.333  1.00 137.00 ?  442  ALA B CA  1 
ATOM   4553  C  C   . ALA B 2  442  ? -58.904 -67.333  -3.359  1.00 143.22 ?  442  ALA B C   1 
ATOM   4554  O  O   . ALA B 2  442  ? -59.575 -68.357  -3.179  1.00 145.84 ?  442  ALA B O   1 
ATOM   4555  C  CB  . ALA B 2  442  ? -60.167 -65.324  -2.561  1.00 139.24 ?  442  ALA B CB  1 
ATOM   4556  N  N   . SER B 2  443  ? -58.128 -67.164  -4.434  1.00 164.09 ?  443  SER B N   1 
ATOM   4557  C  CA  . SER B 2  443  ? -58.123 -68.151  -5.511  1.00 162.94 ?  443  SER B CA  1 
ATOM   4558  C  C   . SER B 2  443  ? -57.566 -69.489  -5.039  1.00 163.66 ?  443  SER B C   1 
ATOM   4559  O  O   . SER B 2  443  ? -58.077 -70.549  -5.417  1.00 165.82 ?  443  SER B O   1 
ATOM   4560  C  CB  . SER B 2  443  ? -57.323 -67.624  -6.702  1.00 157.72 ?  443  SER B CB  1 
ATOM   4561  O  OG  . SER B 2  443  ? -55.929 -67.682  -6.453  1.00 163.12 ?  443  SER B OG  1 
ATOM   4562  N  N   . VAL B 2  444  ? -56.525 -69.464  -4.220  1.00 126.63 ?  444  VAL B N   1 
ATOM   4563  C  CA  . VAL B 2  444  ? -55.975 -70.703  -3.667  1.00 117.05 ?  444  VAL B CA  1 
ATOM   4564  C  C   . VAL B 2  444  ? -56.870 -71.176  -2.523  1.00 107.16 ?  444  VAL B C   1 
ATOM   4565  O  O   . VAL B 2  444  ? -57.171 -70.390  -1.610  1.00 113.96 ?  444  VAL B O   1 
ATOM   4566  C  CB  . VAL B 2  444  ? -54.526 -70.503  -3.220  1.00 113.73 ?  444  VAL B CB  1 
ATOM   4567  C  CG1 . VAL B 2  444  ? -54.390 -69.333  -2.264  1.00 118.04 ?  444  VAL B CG1 1 
ATOM   4568  C  CG2 . VAL B 2  444  ? -53.992 -71.772  -2.580  1.00 109.67 ?  444  VAL B CG2 1 
ATOM   4569  N  N   . PRO B 2  445  ? -57.353 -72.420  -2.564  1.00 105.15 ?  445  PRO B N   1 
ATOM   4570  C  CA  . PRO B 2  445  ? -58.312 -72.855  -1.536  1.00 108.15 ?  445  PRO B CA  1 
ATOM   4571  C  C   . PRO B 2  445  ? -57.705 -72.971  -0.152  1.00 108.44 ?  445  PRO B C   1 
ATOM   4572  O  O   . PRO B 2  445  ? -58.331 -72.547  0.827   1.00 113.52 ?  445  PRO B O   1 
ATOM   4573  C  CB  . PRO B 2  445  ? -58.789 -74.215  -2.064  1.00 111.53 ?  445  PRO B CB  1 
ATOM   4574  C  CG  . PRO B 2  445  ? -58.530 -74.155  -3.544  1.00 123.00 ?  445  PRO B CG  1 
ATOM   4575  C  CD  . PRO B 2  445  ? -57.250 -73.390  -3.666  1.00 120.03 ?  445  PRO B CD  1 
ATOM   4576  N  N   . LEU B 2  446  ? -56.511 -73.541  -0.034  1.00 97.18  ?  446  LEU B N   1 
ATOM   4577  C  CA  . LEU B 2  446  ? -55.891 -73.804  1.258   1.00 90.38  ?  446  LEU B CA  1 
ATOM   4578  C  C   . LEU B 2  446  ? -54.753 -72.819  1.481   1.00 88.31  ?  446  LEU B C   1 
ATOM   4579  O  O   . LEU B 2  446  ? -53.757 -72.839  0.750   1.00 87.25  ?  446  LEU B O   1 
ATOM   4580  C  CB  . LEU B 2  446  ? -55.384 -75.245  1.340   1.00 90.07  ?  446  LEU B CB  1 
ATOM   4581  C  CG  . LEU B 2  446  ? -54.950 -75.718  2.729   1.00 87.16  ?  446  LEU B CG  1 
ATOM   4582  C  CD1 . LEU B 2  446  ? -56.096 -75.600  3.721   1.00 96.00  ?  446  LEU B CD1 1 
ATOM   4583  C  CD2 . LEU B 2  446  ? -54.432 -77.153  2.676   1.00 85.55  ?  446  LEU B CD2 1 
ATOM   4584  N  N   . THR B 2  447  ? -54.908 -71.959  2.485   1.00 97.29  ?  447  THR B N   1 
ATOM   4585  C  CA  . THR B 2  447  ? -53.880 -71.012  2.894   1.00 96.22  ?  447  THR B CA  1 
ATOM   4586  C  C   . THR B 2  447  ? -53.498 -71.316  4.334   1.00 95.68  ?  447  THR B C   1 
ATOM   4587  O  O   . THR B 2  447  ? -54.376 -71.527  5.174   1.00 96.02  ?  447  THR B O   1 
ATOM   4588  C  CB  . THR B 2  447  ? -54.373 -69.570  2.763   1.00 99.56  ?  447  THR B CB  1 
ATOM   4589  O  OG1 . THR B 2  447  ? -55.762 -69.506  3.113   1.00 102.37 ?  447  THR B OG1 1 
ATOM   4590  C  CG2 . THR B 2  447  ? -54.193 -69.080  1.342   1.00 95.55  ?  447  THR B CG2 1 
ATOM   4591  N  N   . ILE B 2  448  ? -52.196 -71.362  4.609   1.00 77.56  ?  448  ILE B N   1 
ATOM   4592  C  CA  . ILE B 2  448  ? -51.668 -71.709  5.923   1.00 66.30  ?  448  ILE B CA  1 
ATOM   4593  C  C   . ILE B 2  448  ? -50.583 -70.704  6.278   1.00 61.73  ?  448  ILE B C   1 
ATOM   4594  O  O   . ILE B 2  448  ? -49.756 -70.352  5.431   1.00 65.61  ?  448  ILE B O   1 
ATOM   4595  C  CB  . ILE B 2  448  ? -51.108 -73.148  5.949   1.00 64.36  ?  448  ILE B CB  1 
ATOM   4596  C  CG1 . ILE B 2  448  ? -52.199 -74.161  5.595   1.00 65.72  ?  448  ILE B CG1 1 
ATOM   4597  C  CG2 . ILE B 2  448  ? -50.515 -73.469  7.307   1.00 70.60  ?  448  ILE B CG2 1 
ATOM   4598  C  CD1 . ILE B 2  448  ? -51.670 -75.546  5.274   1.00 59.04  ?  448  ILE B CD1 1 
ATOM   4599  N  N   . HIS B 2  449  ? -50.581 -70.239  7.527   1.00 61.06  ?  449  HIS B N   1 
ATOM   4600  C  CA  . HIS B 2  449  ? -49.662 -69.185  7.930   1.00 64.26  ?  449  HIS B CA  1 
ATOM   4601  C  C   . HIS B 2  449  ? -49.185 -69.385  9.359   1.00 62.21  ?  449  HIS B C   1 
ATOM   4602  O  O   . HIS B 2  449  ? -49.953 -69.803  10.229  1.00 63.64  ?  449  HIS B O   1 
ATOM   4603  C  CB  . HIS B 2  449  ? -50.316 -67.802  7.799   1.00 65.29  ?  449  HIS B CB  1 
ATOM   4604  C  CG  . HIS B 2  449  ? -49.332 -66.677  7.730   1.00 67.41  ?  449  HIS B CG  1 
ATOM   4605  N  ND1 . HIS B 2  449  ? -48.984 -65.920  8.827   1.00 66.68  ?  449  HIS B ND1 1 
ATOM   4606  C  CD2 . HIS B 2  449  ? -48.618 -66.183  6.691   1.00 75.07  ?  449  HIS B CD2 1 
ATOM   4607  C  CE1 . HIS B 2  449  ? -48.100 -65.006  8.466   1.00 75.02  ?  449  HIS B CE1 1 
ATOM   4608  N  NE2 . HIS B 2  449  ? -47.860 -65.144  7.175   1.00 79.10  ?  449  HIS B NE2 1 
ATOM   4609  N  N   . LEU B 2  450  ? -47.904 -69.088  9.581   1.00 89.17  ?  450  LEU B N   1 
ATOM   4610  C  CA  . LEU B 2  450  ? -47.311 -68.966  10.909  1.00 95.13  ?  450  LEU B CA  1 
ATOM   4611  C  C   . LEU B 2  450  ? -46.848 -67.530  11.072  1.00 97.76  ?  450  LEU B C   1 
ATOM   4612  O  O   . LEU B 2  450  ? -45.941 -67.090  10.359  1.00 96.81  ?  450  LEU B O   1 
ATOM   4613  C  CB  . LEU B 2  450  ? -46.118 -69.906  11.094  1.00 79.04  ?  450  LEU B CB  1 
ATOM   4614  C  CG  . LEU B 2  450  ? -46.342 -71.389  10.889  1.00 92.45  ?  450  LEU B CG  1 
ATOM   4615  C  CD1 . LEU B 2  450  ? -45.930 -71.721  9.484   1.00 105.58 ?  450  LEU B CD1 1 
ATOM   4616  C  CD2 . LEU B 2  450  ? -45.534 -72.182  11.900  1.00 85.16  ?  450  LEU B CD2 1 
ATOM   4617  N  N   . SER B 2  451  ? -47.456 -66.804  12.006  1.00 91.31  ?  451  SER B N   1 
ATOM   4618  C  CA  . SER B 2  451  ? -47.197 -65.379  12.107  1.00 93.46  ?  451  SER B CA  1 
ATOM   4619  C  C   . SER B 2  451  ? -46.743 -64.894  13.475  1.00 105.86 ?  451  SER B C   1 
ATOM   4620  O  O   . SER B 2  451  ? -46.373 -63.719  13.584  1.00 116.34 ?  451  SER B O   1 
ATOM   4621  C  CB  . SER B 2  451  ? -48.443 -64.578  11.709  1.00 101.67 ?  451  SER B CB  1 
ATOM   4622  O  OG  . SER B 2  451  ? -48.084 -63.284  11.261  1.00 108.47 ?  451  SER B OG  1 
ATOM   4623  N  N   . GLN B 2  452  ? -46.784 -65.729  14.517  1.00 97.98  ?  452  GLN B N   1 
ATOM   4624  C  CA  . GLN B 2  452  ? -46.431 -65.325  15.879  1.00 103.33 ?  452  GLN B CA  1 
ATOM   4625  C  C   . GLN B 2  452  ? -47.446 -64.314  16.410  1.00 100.02 ?  452  GLN B C   1 
ATOM   4626  O  O   . GLN B 2  452  ? -47.450 -64.004  17.605  1.00 100.86 ?  452  GLN B O   1 
ATOM   4627  C  CB  . GLN B 2  452  ? -44.995 -64.773  15.930  1.00 98.69  ?  452  GLN B CB  1 
ATOM   4628  C  CG  . GLN B 2  452  ? -44.450 -64.307  17.271  1.00 102.86 ?  452  GLN B CG  1 
ATOM   4629  C  CD  . GLN B 2  452  ? -43.128 -63.593  17.089  1.00 93.31  ?  452  GLN B CD  1 
ATOM   4630  O  OE1 . GLN B 2  452  ? -42.287 -64.018  16.297  1.00 73.29  ?  452  GLN B OE1 1 
ATOM   4631  N  NE2 . GLN B 2  452  ? -42.935 -62.506  17.817  1.00 98.77  ?  452  GLN B NE2 1 
ATOM   4632  N  N   . PHE B 2  453  ? -48.328 -63.826  15.537  1.00 83.11  ?  453  PHE B N   1 
ATOM   4633  C  CA  . PHE B 2  453  ? -49.447 -62.960  15.882  1.00 82.24  ?  453  PHE B CA  1 
ATOM   4634  C  C   . PHE B 2  453  ? -50.619 -63.390  15.013  1.00 86.13  ?  453  PHE B C   1 
ATOM   4635  O  O   . PHE B 2  453  ? -50.456 -64.176  14.077  1.00 87.29  ?  453  PHE B O   1 
ATOM   4636  C  CB  . PHE B 2  453  ? -49.121 -61.480  15.641  1.00 85.09  ?  453  PHE B CB  1 
ATOM   4637  C  CG  . PHE B 2  453  ? -48.167 -60.897  16.636  1.00 85.09  ?  453  PHE B CG  1 
ATOM   4638  C  CD1 . PHE B 2  453  ? -48.624 -60.358  17.828  1.00 82.40  ?  453  PHE B CD1 1 
ATOM   4639  C  CD2 . PHE B 2  453  ? -46.810 -60.876  16.372  1.00 85.13  ?  453  PHE B CD2 1 
ATOM   4640  C  CE1 . PHE B 2  453  ? -47.734 -59.816  18.743  1.00 81.84  ?  453  PHE B CE1 1 
ATOM   4641  C  CE2 . PHE B 2  453  ? -45.918 -60.337  17.279  1.00 76.24  ?  453  PHE B CE2 1 
ATOM   4642  C  CZ  . PHE B 2  453  ? -46.378 -59.806  18.466  1.00 81.11  ?  453  PHE B CZ  1 
ATOM   4643  N  N   . VAL B 2  454  ? -51.813 -62.893  15.328  1.00 84.72  ?  454  VAL B N   1 
ATOM   4644  C  CA  . VAL B 2  454  ? -52.931 -63.062  14.405  1.00 76.35  ?  454  VAL B CA  1 
ATOM   4645  C  C   . VAL B 2  454  ? -52.876 -61.911  13.410  1.00 78.22  ?  454  VAL B C   1 
ATOM   4646  O  O   . VAL B 2  454  ? -53.638 -60.943  13.514  1.00 78.02  ?  454  VAL B O   1 
ATOM   4647  C  CB  . VAL B 2  454  ? -54.286 -63.122  15.134  1.00 74.24  ?  454  VAL B CB  1 
ATOM   4648  C  CG1 . VAL B 2  454  ? -55.382 -63.590  14.178  1.00 69.68  ?  454  VAL B CG1 1 
ATOM   4649  C  CG2 . VAL B 2  454  ? -54.195 -64.062  16.324  1.00 84.99  ?  454  VAL B CG2 1 
ATOM   4650  N  N   . ASP B 2  455  ? -51.961 -62.007  12.448  1.00 79.95  ?  455  ASP B N   1 
ATOM   4651  C  CA  . ASP B 2  455  ? -51.723 -60.914  11.520  1.00 79.22  ?  455  ASP B CA  1 
ATOM   4652  C  C   . ASP B 2  455  ? -52.858 -60.812  10.503  1.00 84.30  ?  455  ASP B C   1 
ATOM   4653  O  O   . ASP B 2  455  ? -53.782 -61.630  10.470  1.00 84.70  ?  455  ASP B O   1 
ATOM   4654  C  CB  . ASP B 2  455  ? -50.387 -61.101  10.803  1.00 75.72  ?  455  ASP B CB  1 
ATOM   4655  C  CG  . ASP B 2  455  ? -49.219 -60.546  11.594  1.00 94.65  ?  455  ASP B CG  1 
ATOM   4656  O  OD1 . ASP B 2  455  ? -49.443 -60.029  12.709  1.00 104.47 ?  455  ASP B OD1 1 
ATOM   4657  O  OD2 . ASP B 2  455  ? -48.074 -60.635  11.106  1.00 99.76  -1 455  ASP B OD2 1 
ATOM   4658  N  N   . GLU B 2  456  ? -52.772 -59.777  9.662   1.00 95.53  ?  456  GLU B N   1 
ATOM   4659  C  CA  . GLU B 2  456  ? -53.804 -59.543  8.657   1.00 97.23  ?  456  GLU B CA  1 
ATOM   4660  C  C   . GLU B 2  456  ? -53.941 -60.734  7.718   1.00 96.58  ?  456  GLU B C   1 
ATOM   4661  O  O   . GLU B 2  456  ? -55.058 -61.128  7.359   1.00 101.59 ?  456  GLU B O   1 
ATOM   4662  C  CB  . GLU B 2  456  ? -53.485 -58.276  7.862   1.00 96.91  ?  456  GLU B CB  1 
ATOM   4663  C  CG  . GLU B 2  456  ? -53.767 -56.979  8.604   1.00 103.49 ?  456  GLU B CG  1 
ATOM   4664  C  CD  . GLU B 2  456  ? -52.569 -56.500  9.403   1.00 106.01 ?  456  GLU B CD  1 
ATOM   4665  O  OE1 . GLU B 2  456  ? -51.470 -57.063  9.218   1.00 114.47 ?  456  GLU B OE1 1 
ATOM   4666  O  OE2 . GLU B 2  456  ? -52.723 -55.563  10.215  1.00 107.98 -1 456  GLU B OE2 1 
ATOM   4667  N  N   . THR B 2  457  ? -52.815 -61.326  7.316   1.00 78.51  ?  457  THR B N   1 
ATOM   4668  C  CA  . THR B 2  457  ? -52.858 -62.456  6.395   1.00 84.55  ?  457  THR B CA  1 
ATOM   4669  C  C   . THR B 2  457  ? -53.486 -63.685  7.044   1.00 84.10  ?  457  THR B C   1 
ATOM   4670  O  O   . THR B 2  457  ? -54.213 -64.436  6.384   1.00 88.28  ?  457  THR B O   1 
ATOM   4671  C  CB  . THR B 2  457  ? -51.450 -62.770  5.886   1.00 83.63  ?  457  THR B CB  1 
ATOM   4672  O  OG1 . THR B 2  457  ? -51.473 -63.971  5.103   1.00 87.90  ?  457  THR B OG1 1 
ATOM   4673  C  CG2 . THR B 2  457  ? -50.478 -62.927  7.050   1.00 82.90  ?  457  THR B CG2 1 
ATOM   4674  N  N   . SER B 2  458  ? -53.232 -63.902  8.337   1.00 107.60 ?  458  SER B N   1 
ATOM   4675  C  CA  . SER B 2  458  ? -53.775 -65.082  9.002   1.00 106.53 ?  458  SER B CA  1 
ATOM   4676  C  C   . SER B 2  458  ? -55.285 -64.988  9.173   1.00 106.03 ?  458  SER B C   1 
ATOM   4677  O  O   . SER B 2  458  ? -55.977 -66.013  9.154   1.00 106.33 ?  458  SER B O   1 
ATOM   4678  C  CB  . SER B 2  458  ? -53.096 -65.278  10.356  1.00 99.20  ?  458  SER B CB  1 
ATOM   4679  O  OG  . SER B 2  458  ? -51.688 -65.327  10.211  1.00 98.16  ?  458  SER B OG  1 
ATOM   4680  N  N   . ALA B 2  459  ? -55.814 -63.772  9.338   1.00 70.04  ?  459  ALA B N   1 
ATOM   4681  C  CA  . ALA B 2  459  ? -57.256 -63.609  9.475   1.00 62.36  ?  459  ALA B CA  1 
ATOM   4682  C  C   . ALA B 2  459  ? -57.983 -63.984  8.192   1.00 67.35  ?  459  ALA B C   1 
ATOM   4683  O  O   . ALA B 2  459  ? -59.101 -64.509  8.242   1.00 71.11  ?  459  ALA B O   1 
ATOM   4684  C  CB  . ALA B 2  459  ? -57.585 -62.171  9.878   1.00 56.67  ?  459  ALA B CB  1 
ATOM   4685  N  N   . ARG B 2  460  ? -57.368 -63.729  7.039   1.00 92.09  ?  460  ARG B N   1 
ATOM   4686  C  CA  . ARG B 2  460  ? -57.948 -64.063  5.747   1.00 95.00  ?  460  ARG B CA  1 
ATOM   4687  C  C   . ARG B 2  460  ? -57.480 -65.415  5.232   1.00 97.12  ?  460  ARG B C   1 
ATOM   4688  O  O   . ARG B 2  460  ? -57.673 -65.717  4.049   1.00 92.56  ?  460  ARG B O   1 
ATOM   4689  C  CB  . ARG B 2  460  ? -57.616 -62.972  4.725   1.00 95.29  ?  460  ARG B CB  1 
ATOM   4690  C  CG  . ARG B 2  460  ? -57.726 -61.561  5.288   1.00 97.90  ?  460  ARG B CG  1 
ATOM   4691  C  CD  . ARG B 2  460  ? -57.923 -60.524  4.202   1.00 103.70 ?  460  ARG B CD  1 
ATOM   4692  N  NE  . ARG B 2  460  ? -59.058 -60.843  3.349   1.00 113.14 ?  460  ARG B NE  1 
ATOM   4693  C  CZ  . ARG B 2  460  ? -59.608 -59.997  2.490   1.00 125.59 ?  460  ARG B CZ  1 
ATOM   4694  N  NH1 . ARG B 2  460  ? -59.149 -58.765  2.344   1.00 121.80 ?  460  ARG B NH1 1 
ATOM   4695  N  NH2 . ARG B 2  460  ? -60.648 -60.395  1.764   1.00 139.65 ?  460  ARG B NH2 1 
ATOM   4696  N  N   . ALA B 2  461  ? -56.871 -66.229  6.090   1.00 81.08  ?  461  ALA B N   1 
ATOM   4697  C  CA  . ALA B 2  461  ? -56.359 -67.536  5.719   1.00 73.23  ?  461  ALA B CA  1 
ATOM   4698  C  C   . ALA B 2  461  ? -56.969 -68.609  6.606   1.00 75.24  ?  461  ALA B C   1 
ATOM   4699  O  O   . ALA B 2  461  ? -57.496 -68.332  7.687   1.00 82.21  ?  461  ALA B O   1 
ATOM   4700  C  CB  . ALA B 2  461  ? -54.833 -67.596  5.839   1.00 78.08  ?  461  ALA B CB  1 
ATOM   4701  N  N   . THR B 2  462  ? -56.881 -69.846  6.136   1.00 89.24  ?  462  THR B N   1 
ATOM   4702  C  CA  . THR B 2  462  ? -57.248 -70.990  6.946   1.00 92.71  ?  462  THR B CA  1 
ATOM   4703  C  C   . THR B 2  462  ? -56.051 -71.437  7.780   1.00 89.26  ?  462  THR B C   1 
ATOM   4704  O  O   . THR B 2  462  ? -54.935 -70.936  7.624   1.00 89.32  ?  462  THR B O   1 
ATOM   4705  C  CB  . THR B 2  462  ? -57.756 -72.133  6.068   1.00 92.61  ?  462  THR B CB  1 
ATOM   4706  O  OG1 . THR B 2  462  ? -56.675 -72.647  5.282   1.00 97.07  ?  462  THR B OG1 1 
ATOM   4707  C  CG2 . THR B 2  462  ? -58.853 -71.643  5.144   1.00 88.79  ?  462  THR B CG2 1 
ATOM   4708  N  N   . TRP B 2  463  ? -56.314 -72.355  8.707   1.00 95.20  ?  463  TRP B N   1 
ATOM   4709  C  CA  . TRP B 2  463  ? -55.290 -73.085  9.462   1.00 98.83  ?  463  TRP B CA  1 
ATOM   4710  C  C   . TRP B 2  463  ? -54.130 -72.191  9.898   1.00 100.66 ?  463  TRP B C   1 
ATOM   4711  O  O   . TRP B 2  463  ? -52.978 -72.385  9.509   1.00 102.68 ?  463  TRP B O   1 
ATOM   4712  C  CB  . TRP B 2  463  ? -54.771 -74.271  8.652   1.00 97.25  ?  463  TRP B CB  1 
ATOM   4713  C  CG  . TRP B 2  463  ? -55.721 -75.420  8.563   1.00 102.85 ?  463  TRP B CG  1 
ATOM   4714  C  CD1 . TRP B 2  463  ? -56.236 -75.973  7.427   1.00 106.16 ?  463  TRP B CD1 1 
ATOM   4715  C  CD2 . TRP B 2  463  ? -56.249 -76.181  9.656   1.00 107.94 ?  463  TRP B CD2 1 
ATOM   4716  N  NE1 . TRP B 2  463  ? -57.063 -77.023  7.745   1.00 123.19 ?  463  TRP B NE1 1 
ATOM   4717  C  CE2 . TRP B 2  463  ? -57.087 -77.172  9.108   1.00 119.49 ?  463  TRP B CE2 1 
ATOM   4718  C  CE3 . TRP B 2  463  ? -56.101 -76.117  11.045  1.00 107.25 ?  463  TRP B CE3 1 
ATOM   4719  C  CZ2 . TRP B 2  463  ? -57.774 -78.090  9.899   1.00 120.19 ?  463  TRP B CZ2 1 
ATOM   4720  C  CZ3 . TRP B 2  463  ? -56.784 -77.031  11.829  1.00 112.23 ?  463  TRP B CZ3 1 
ATOM   4721  C  CH2 . TRP B 2  463  ? -57.610 -78.003  11.254  1.00 115.11 ?  463  TRP B CH2 1 
ATOM   4722  N  N   . HIS B 2  464  ? -54.449 -71.189  10.714  1.00 89.56  ?  464  HIS B N   1 
ATOM   4723  C  CA  . HIS B 2  464  ? -53.398 -70.360  11.287  1.00 79.92  ?  464  HIS B CA  1 
ATOM   4724  C  C   . HIS B 2  464  ? -52.700 -71.116  12.406  1.00 74.99  ?  464  HIS B C   1 
ATOM   4725  O  O   . HIS B 2  464  ? -53.353 -71.664  13.300  1.00 76.38  ?  464  HIS B O   1 
ATOM   4726  C  CB  . HIS B 2  464  ? -53.959 -69.046  11.819  1.00 75.67  ?  464  HIS B CB  1 
ATOM   4727  C  CG  . HIS B 2  464  ? -52.972 -68.265  12.631  1.00 73.52  ?  464  HIS B CG  1 
ATOM   4728  N  ND1 . HIS B 2  464  ? -51.734 -67.900  12.147  1.00 74.65  ?  464  HIS B ND1 1 
ATOM   4729  C  CD2 . HIS B 2  464  ? -53.035 -67.790  13.897  1.00 73.39  ?  464  HIS B CD2 1 
ATOM   4730  C  CE1 . HIS B 2  464  ? -51.079 -67.230  13.078  1.00 69.60  ?  464  HIS B CE1 1 
ATOM   4731  N  NE2 . HIS B 2  464  ? -51.846 -67.148  14.149  1.00 66.43  ?  464  HIS B NE2 1 
ATOM   4732  N  N   . ILE B 2  465  ? -51.377 -71.155  12.352  1.00 54.46  ?  465  ILE B N   1 
ATOM   4733  C  CA  . ILE B 2  465  ? -50.552 -71.866  13.321  1.00 52.27  ?  465  ILE B CA  1 
ATOM   4734  C  C   . ILE B 2  465  ? -49.745 -70.827  14.088  1.00 56.30  ?  465  ILE B C   1 
ATOM   4735  O  O   . ILE B 2  465  ? -49.019 -70.042  13.467  1.00 52.03  ?  465  ILE B O   1 
ATOM   4736  C  CB  . ILE B 2  465  ? -49.624 -72.886  12.646  1.00 49.04  ?  465  ILE B CB  1 
ATOM   4737  C  CG1 . ILE B 2  465  ? -50.412 -73.775  11.682  1.00 60.75  ?  465  ILE B CG1 1 
ATOM   4738  C  CG2 . ILE B 2  465  ? -48.906 -73.719  13.691  1.00 48.08  ?  465  ILE B CG2 1 
ATOM   4739  C  CD1 . ILE B 2  465  ? -51.471 -74.634  12.359  1.00 69.27  ?  465  ILE B CD1 1 
ATOM   4740  N  N   . PRO B 2  466  ? -49.856 -70.767  15.413  1.00 67.71  ?  466  PRO B N   1 
ATOM   4741  C  CA  . PRO B 2  466  ? -49.020 -69.839  16.181  1.00 57.93  ?  466  PRO B CA  1 
ATOM   4742  C  C   . PRO B 2  466  ? -47.553 -70.224  16.087  1.00 59.53  ?  466  PRO B C   1 
ATOM   4743  O  O   . PRO B 2  466  ? -47.193 -71.400  16.183  1.00 56.17  ?  466  PRO B O   1 
ATOM   4744  C  CB  . PRO B 2  466  ? -49.550 -69.988  17.612  1.00 58.55  ?  466  PRO B CB  1 
ATOM   4745  C  CG  . PRO B 2  466  ? -50.207 -71.331  17.634  1.00 62.05  ?  466  PRO B CG  1 
ATOM   4746  C  CD  . PRO B 2  466  ? -50.810 -71.488  16.269  1.00 67.42  ?  466  PRO B CD  1 
ATOM   4747  N  N   . GLN B 2  467  ? -46.702 -69.220  15.894  1.00 75.83  ?  467  GLN B N   1 
ATOM   4748  C  CA  . GLN B 2  467  ? -45.267 -69.435  15.771  1.00 75.87  ?  467  GLN B CA  1 
ATOM   4749  C  C   . GLN B 2  467  ? -44.571 -69.115  17.086  1.00 77.53  ?  467  GLN B C   1 
ATOM   4750  O  O   . GLN B 2  467  ? -44.923 -68.149  17.769  1.00 76.51  ?  467  GLN B O   1 
ATOM   4751  C  CB  . GLN B 2  467  ? -44.671 -68.579  14.652  1.00 77.56  ?  467  GLN B CB  1 
ATOM   4752  C  CG  . GLN B 2  467  ? -43.311 -69.068  14.178  1.00 77.33  ?  467  GLN B CG  1 
ATOM   4753  C  CD  . GLN B 2  467  ? -42.665 -68.129  13.181  1.00 77.87  ?  467  GLN B CD  1 
ATOM   4754  O  OE1 . GLN B 2  467  ? -43.088 -66.983  13.026  1.00 75.41  ?  467  GLN B OE1 1 
ATOM   4755  N  NE2 . GLN B 2  467  ? -41.631 -68.610  12.500  1.00 77.38  ?  467  GLN B NE2 1 
ATOM   4756  N  N   . ALA B 2  468  ? -43.576 -69.927  17.428  1.00 83.64  ?  468  ALA B N   1 
ATOM   4757  C  CA  . ALA B 2  468  ? -42.822 -69.731  18.656  1.00 71.07  ?  468  ALA B CA  1 
ATOM   4758  C  C   . ALA B 2  468  ? -41.867 -68.553  18.518  1.00 64.62  ?  468  ALA B C   1 
ATOM   4759  O  O   . ALA B 2  468  ? -41.214 -68.380  17.485  1.00 59.75  ?  468  ALA B O   1 
ATOM   4760  C  CB  . ALA B 2  468  ? -42.046 -71.000  19.010  1.00 70.51  ?  468  ALA B CB  1 
ATOM   4761  N  N   . HIS B 2  469  ? -41.793 -67.742  19.569  1.00 76.96  ?  469  HIS B N   1 
ATOM   4762  C  CA  . HIS B 2  469  ? -40.895 -66.600  19.575  1.00 73.55  ?  469  HIS B CA  1 
ATOM   4763  C  C   . HIS B 2  469  ? -39.439 -67.068  19.542  1.00 76.34  ?  469  HIS B C   1 
ATOM   4764  O  O   . HIS B 2  469  ? -39.119 -68.155  20.031  1.00 78.80  ?  469  HIS B O   1 
ATOM   4765  C  CB  . HIS B 2  469  ? -41.140 -65.744  20.816  1.00 71.36  ?  469  HIS B CB  1 
ATOM   4766  C  CG  . HIS B 2  469  ? -40.560 -64.368  20.725  1.00 76.98  ?  469  HIS B CG  1 
ATOM   4767  N  ND1 . HIS B 2  469  ? -39.303 -64.057  21.198  1.00 73.30  ?  469  HIS B ND1 1 
ATOM   4768  C  CD2 . HIS B 2  469  ? -41.061 -63.221  20.207  1.00 81.01  ?  469  HIS B CD2 1 
ATOM   4769  C  CE1 . HIS B 2  469  ? -39.057 -62.778  20.978  1.00 77.03  ?  469  HIS B CE1 1 
ATOM   4770  N  NE2 . HIS B 2  469  ? -40.108 -62.248  20.379  1.00 77.89  ?  469  HIS B NE2 1 
ATOM   4771  N  N   . PRO B 2  470  ? -38.540 -66.272  18.954  1.00 66.26  ?  470  PRO B N   1 
ATOM   4772  C  CA  . PRO B 2  470  ? -37.115 -66.653  18.946  1.00 62.93  ?  470  PRO B CA  1 
ATOM   4773  C  C   . PRO B 2  470  ? -36.514 -66.847  20.329  1.00 60.18  ?  470  PRO B C   1 
ATOM   4774  O  O   . PRO B 2  470  ? -35.470 -67.500  20.447  1.00 56.97  ?  470  PRO B O   1 
ATOM   4775  C  CB  . PRO B 2  470  ? -36.449 -65.486  18.209  1.00 55.96  ?  470  PRO B CB  1 
ATOM   4776  C  CG  . PRO B 2  470  ? -37.516 -64.967  17.311  1.00 68.12  ?  470  PRO B CG  1 
ATOM   4777  C  CD  . PRO B 2  470  ? -38.802 -65.118  18.075  1.00 68.03  ?  470  PRO B CD  1 
ATOM   4778  N  N   . LEU B 2  471  ? -37.128 -66.299  21.373  1.00 82.19  ?  471  LEU B N   1 
ATOM   4779  C  CA  . LEU B 2  471  ? -36.650 -66.475  22.737  1.00 84.23  ?  471  LEU B CA  1 
ATOM   4780  C  C   . LEU B 2  471  ? -37.241 -67.704  23.413  1.00 96.89  ?  471  LEU B C   1 
ATOM   4781  O  O   . LEU B 2  471  ? -36.960 -67.942  24.592  1.00 94.90  ?  471  LEU B O   1 
ATOM   4782  C  CB  . LEU B 2  471  ? -36.966 -65.226  23.564  1.00 78.84  ?  471  LEU B CB  1 
ATOM   4783  C  CG  . LEU B 2  471  ? -36.044 -64.031  23.320  1.00 82.02  ?  471  LEU B CG  1 
ATOM   4784  C  CD1 . LEU B 2  471  ? -36.520 -62.821  24.108  1.00 79.15  ?  471  LEU B CD1 1 
ATOM   4785  C  CD2 . LEU B 2  471  ? -34.602 -64.374  23.664  1.00 88.90  ?  471  LEU B CD2 1 
ATOM   4786  N  N   . GLU B 2  472  ? -38.052 -68.492  22.696  1.00 69.93  ?  472  GLU B N   1 
ATOM   4787  C  CA  . GLU B 2  472  ? -38.652 -69.691  23.267  1.00 63.44  ?  472  GLU B CA  1 
ATOM   4788  C  C   . GLU B 2  472  ? -38.606 -70.878  22.310  1.00 64.40  ?  472  GLU B C   1 
ATOM   4789  O  O   . GLU B 2  472  ? -39.434 -71.789  22.432  1.00 63.62  ?  472  GLU B O   1 
ATOM   4790  C  CB  . GLU B 2  472  ? -40.104 -69.425  23.679  1.00 67.26  ?  472  GLU B CB  1 
ATOM   4791  C  CG  . GLU B 2  472  ? -41.015 -69.061  22.519  1.00 61.96  ?  472  GLU B CG  1 
ATOM   4792  C  CD  . GLU B 2  472  ? -42.312 -68.425  22.972  1.00 64.85  ?  472  GLU B CD  1 
ATOM   4793  O  OE1 . GLU B 2  472  ? -42.281 -67.646  23.946  1.00 72.80  ?  472  GLU B OE1 1 
ATOM   4794  O  OE2 . GLU B 2  472  ? -43.364 -68.710  22.362  1.00 59.32  -1 472  GLU B OE2 1 
ATOM   4795  N  N   . SER B 2  473  ? -37.659 -70.901  21.372  1.00 70.52  ?  473  SER B N   1 
ATOM   4796  C  CA  . SER B 2  473  ? -37.637 -71.910  20.324  1.00 74.16  ?  473  SER B CA  1 
ATOM   4797  C  C   . SER B 2  473  ? -36.205 -72.317  20.008  1.00 72.28  ?  473  SER B C   1 
ATOM   4798  O  O   . SER B 2  473  ? -35.262 -71.550  20.217  1.00 63.96  ?  473  SER B O   1 
ATOM   4799  C  CB  . SER B 2  473  ? -38.317 -71.398  19.047  1.00 83.93  ?  473  SER B CB  1 
ATOM   4800  O  OG  . SER B 2  473  ? -37.547 -70.382  18.427  1.00 80.01  ?  473  SER B OG  1 
ATOM   4801  N  N   . TRP B 2  474  ? -36.055 -73.537  19.494  1.00 67.88  ?  474  TRP B N   1 
ATOM   4802  C  CA  . TRP B 2  474  ? -34.773 -74.020  18.996  1.00 62.84  ?  474  TRP B CA  1 
ATOM   4803  C  C   . TRP B 2  474  ? -34.623 -73.625  17.533  1.00 63.38  ?  474  TRP B C   1 
ATOM   4804  O  O   . TRP B 2  474  ? -35.606 -73.582  16.789  1.00 67.59  ?  474  TRP B O   1 
ATOM   4805  C  CB  . TRP B 2  474  ? -34.672 -75.540  19.138  1.00 60.08  ?  474  TRP B CB  1 
ATOM   4806  C  CG  . TRP B 2  474  ? -34.291 -76.010  20.510  1.00 57.04  ?  474  TRP B CG  1 
ATOM   4807  C  CD1 . TRP B 2  474  ? -35.113 -76.589  21.432  1.00 56.44  ?  474  TRP B CD1 1 
ATOM   4808  C  CD2 . TRP B 2  474  ? -32.990 -75.961  21.107  1.00 60.15  ?  474  TRP B CD2 1 
ATOM   4809  N  NE1 . TRP B 2  474  ? -34.407 -76.892  22.571  1.00 61.46  ?  474  TRP B NE1 1 
ATOM   4810  C  CE2 . TRP B 2  474  ? -33.101 -76.517  22.397  1.00 58.83  ?  474  TRP B CE2 1 
ATOM   4811  C  CE3 . TRP B 2  474  ? -31.743 -75.495  20.680  1.00 61.44  ?  474  TRP B CE3 1 
ATOM   4812  C  CZ2 . TRP B 2  474  ? -32.015 -76.622  23.261  1.00 59.30  ?  474  TRP B CZ2 1 
ATOM   4813  C  CZ3 . TRP B 2  474  ? -30.666 -75.599  21.539  1.00 58.85  ?  474  TRP B CZ3 1 
ATOM   4814  C  CH2 . TRP B 2  474  ? -30.809 -76.158  22.814  1.00 58.23  ?  474  TRP B CH2 1 
ATOM   4815  N  N   . GLY B 2  475  ? -33.394 -73.332  17.124  1.00 56.79  ?  475  GLY B N   1 
ATOM   4816  C  CA  . GLY B 2  475  ? -33.153 -72.979  15.741  1.00 51.63  ?  475  GLY B CA  1 
ATOM   4817  C  C   . GLY B 2  475  ? -31.725 -72.515  15.533  1.00 53.15  ?  475  GLY B C   1 
ATOM   4818  O  O   . GLY B 2  475  ? -30.870 -72.652  16.410  1.00 52.48  ?  475  GLY B O   1 
ATOM   4819  N  N   . ASP B 2  476  ? -31.491 -71.964  14.343  1.00 61.93  ?  476  ASP B N   1 
ATOM   4820  C  CA  . ASP B 2  476  ? -30.181 -71.454  13.968  1.00 62.26  ?  476  ASP B CA  1 
ATOM   4821  C  C   . ASP B 2  476  ? -30.368 -70.342  12.945  1.00 57.59  ?  476  ASP B C   1 
ATOM   4822  O  O   . ASP B 2  476  ? -31.459 -70.141  12.406  1.00 51.69  ?  476  ASP B O   1 
ATOM   4823  C  CB  . ASP B 2  476  ? -29.287 -72.566  13.413  1.00 59.04  ?  476  ASP B CB  1 
ATOM   4824  C  CG  . ASP B 2  476  ? -29.975 -73.382  12.337  1.00 66.26  ?  476  ASP B CG  1 
ATOM   4825  O  OD1 . ASP B 2  476  ? -31.164 -73.119  12.057  1.00 62.39  ?  476  ASP B OD1 1 
ATOM   4826  O  OD2 . ASP B 2  476  ? -29.326 -74.286  11.770  1.00 79.60  -1 476  ASP B OD2 1 
ATOM   4827  N  N   . ALA B 2  477  ? -29.283 -69.620  12.680  1.00 49.76  ?  477  ALA B N   1 
ATOM   4828  C  CA  . ALA B 2  477  ? -29.307 -68.509  11.739  1.00 47.41  ?  477  ALA B CA  1 
ATOM   4829  C  C   . ALA B 2  477  ? -27.876 -68.186  11.336  1.00 51.00  ?  477  ALA B C   1 
ATOM   4830  O  O   . ALA B 2  477  ? -26.917 -68.625  11.974  1.00 54.78  ?  477  ALA B O   1 
ATOM   4831  C  CB  . ALA B 2  477  ? -29.998 -67.279  12.337  1.00 54.85  ?  477  ALA B CB  1 
ATOM   4832  N  N   . ARG B 2  478  ? -27.745 -67.403  10.268  1.00 60.45  ?  478  ARG B N   1 
ATOM   4833  C  CA  . ARG B 2  478  ? -26.451 -66.987  9.747   1.00 62.58  ?  478  ARG B CA  1 
ATOM   4834  C  C   . ARG B 2  478  ? -26.392 -65.468  9.710   1.00 70.51  ?  478  ARG B C   1 
ATOM   4835  O  O   . ARG B 2  478  ? -27.332 -64.818  9.241   1.00 69.31  ?  478  ARG B O   1 
ATOM   4836  C  CB  . ARG B 2  478  ? -26.210 -67.564  8.349   1.00 65.66  ?  478  ARG B CB  1 
ATOM   4837  C  CG  . ARG B 2  478  ? -26.008 -69.070  8.323   1.00 78.77  ?  478  ARG B CG  1 
ATOM   4838  C  CD  . ARG B 2  478  ? -25.408 -69.527  7.001   1.00 81.84  ?  478  ARG B CD  1 
ATOM   4839  N  NE  . ARG B 2  478  ? -24.021 -69.103  6.841   1.00 92.79  ?  478  ARG B NE  1 
ATOM   4840  C  CZ  . ARG B 2  478  ? -23.296 -69.323  5.753   1.00 95.69  ?  478  ARG B CZ  1 
ATOM   4841  N  NH1 . ARG B 2  478  ? -23.799 -69.948  4.702   1.00 85.99  ?  478  ARG B NH1 1 
ATOM   4842  N  NH2 . ARG B 2  478  ? -22.034 -68.905  5.718   1.00 95.43  ?  478  ARG B NH2 1 
ATOM   4843  N  N   . ALA B 2  479  ? -25.295 -64.906  10.210  1.00 77.45  ?  479  ALA B N   1 
ATOM   4844  C  CA  . ALA B 2  479  ? -25.081 -63.470  10.164  1.00 72.95  ?  479  ALA B CA  1 
ATOM   4845  C  C   . ALA B 2  479  ? -24.402 -63.093  8.850   1.00 76.18  ?  479  ALA B C   1 
ATOM   4846  O  O   . ALA B 2  479  ? -24.101 -63.945  8.011   1.00 86.43  ?  479  ALA B O   1 
ATOM   4847  C  CB  . ALA B 2  479  ? -24.255 -63.014  11.365  1.00 77.11  ?  479  ALA B CB  1 
ATOM   4848  N  N   . PHE B 2  480  ? -24.167 -61.796  8.658   1.00 86.62  ?  480  PHE B N   1 
ATOM   4849  C  CA  . PHE B 2  480  ? -23.373 -61.361  7.518   1.00 81.89  ?  480  PHE B CA  1 
ATOM   4850  C  C   . PHE B 2  480  ? -21.959 -61.912  7.652   1.00 89.74  ?  480  PHE B C   1 
ATOM   4851  O  O   . PHE B 2  480  ? -21.447 -62.100  8.761   1.00 97.30  ?  480  PHE B O   1 
ATOM   4852  C  CB  . PHE B 2  480  ? -23.360 -59.833  7.416   1.00 79.56  ?  480  PHE B CB  1 
ATOM   4853  C  CG  . PHE B 2  480  ? -22.173 -59.182  8.071   1.00 84.29  ?  480  PHE B CG  1 
ATOM   4854  C  CD1 . PHE B 2  480  ? -22.080 -59.094  9.450   1.00 88.59  ?  480  PHE B CD1 1 
ATOM   4855  C  CD2 . PHE B 2  480  ? -21.156 -58.639  7.303   1.00 82.05  ?  480  PHE B CD2 1 
ATOM   4856  C  CE1 . PHE B 2  480  ? -20.986 -58.491  10.048  1.00 79.14  ?  480  PHE B CE1 1 
ATOM   4857  C  CE2 . PHE B 2  480  ? -20.064 -58.034  7.896   1.00 82.45  ?  480  PHE B CE2 1 
ATOM   4858  C  CZ  . PHE B 2  480  ? -19.980 -57.960  9.270   1.00 77.57  ?  480  PHE B CZ  1 
ATOM   4859  N  N   . ASP B 2  481  ? -21.343 -62.203  6.505   1.00 121.52 ?  481  ASP B N   1 
ATOM   4860  C  CA  . ASP B 2  481  ? -20.079 -62.925  6.373   1.00 134.66 ?  481  ASP B CA  1 
ATOM   4861  C  C   . ASP B 2  481  ? -20.232 -64.392  6.760   1.00 133.60 ?  481  ASP B C   1 
ATOM   4862  O  O   . ASP B 2  481  ? -19.264 -65.152  6.662   1.00 137.85 ?  481  ASP B O   1 
ATOM   4863  C  CB  . ASP B 2  481  ? -18.946 -62.289  7.200   1.00 138.51 ?  481  ASP B CB  1 
ATOM   4864  C  CG  . ASP B 2  481  ? -17.561 -62.727  6.750   1.00 154.52 ?  481  ASP B CG  1 
ATOM   4865  O  OD1 . ASP B 2  481  ? -17.454 -63.449  5.736   1.00 158.85 ?  481  ASP B OD1 1 
ATOM   4866  O  OD2 . ASP B 2  481  ? -16.574 -62.357  7.426   1.00 156.83 -1 481  ASP B OD2 1 
ATOM   4867  N  N   . GLY B 2  482  ? -21.415 -64.816  7.197   1.00 130.51 ?  482  GLY B N   1 
ATOM   4868  C  CA  . GLY B 2  482  ? -21.652 -66.206  7.525   1.00 132.51 ?  482  GLY B CA  1 
ATOM   4869  C  C   . GLY B 2  482  ? -20.990 -66.663  8.808   1.00 143.46 ?  482  GLY B C   1 
ATOM   4870  O  O   . GLY B 2  482  ? -19.760 -66.679  8.911   1.00 153.02 ?  482  GLY B O   1 
ATOM   4871  N  N   . THR B 2  483  ? -21.797 -67.040  9.796   1.00 92.56  ?  483  THR B N   1 
ATOM   4872  C  CA  . THR B 2  483  ? -21.269 -67.554  11.056  1.00 83.43  ?  483  THR B CA  1 
ATOM   4873  C  C   . THR B 2  483  ? -22.045 -68.739  11.613  1.00 95.34  ?  483  THR B C   1 
ATOM   4874  O  O   . THR B 2  483  ? -21.443 -69.565  12.307  1.00 100.15 ?  483  THR B O   1 
ATOM   4875  C  CB  . THR B 2  483  ? -21.229 -66.441  12.112  1.00 92.40  ?  483  THR B CB  1 
ATOM   4876  O  OG1 . THR B 2  483  ? -20.756 -65.232  11.508  1.00 85.83  ?  483  THR B OG1 1 
ATOM   4877  C  CG2 . THR B 2  483  ? -20.288 -66.813  13.249  1.00 96.72  ?  483  THR B CG2 1 
ATOM   4878  N  N   . ALA B 2  484  ? -23.343 -68.864  11.331  1.00 123.89 ?  484  ALA B N   1 
ATOM   4879  C  CA  . ALA B 2  484  ? -24.162 -70.007  11.735  1.00 122.15 ?  484  ALA B CA  1 
ATOM   4880  C  C   . ALA B 2  484  ? -24.169 -70.169  13.259  1.00 124.68 ?  484  ALA B C   1 
ATOM   4881  O  O   . ALA B 2  484  ? -23.596 -71.099  13.825  1.00 134.72 ?  484  ALA B O   1 
ATOM   4882  C  CB  . ALA B 2  484  ? -23.695 -71.292  11.043  1.00 128.68 ?  484  ALA B CB  1 
ATOM   4883  N  N   . SER B 2  485  ? -24.848 -69.230  13.906  1.00 66.38  ?  485  SER B N   1 
ATOM   4884  C  CA  . SER B 2  485  ? -25.048 -69.281  15.345  1.00 58.65  ?  485  SER B CA  1 
ATOM   4885  C  C   . SER B 2  485  ? -26.355 -70.001  15.670  1.00 51.95  ?  485  SER B C   1 
ATOM   4886  O  O   . SER B 2  485  ? -27.249 -70.128  14.832  1.00 56.07  ?  485  SER B O   1 
ATOM   4887  C  CB  . SER B 2  485  ? -25.048 -67.872  15.937  1.00 66.83  ?  485  SER B CB  1 
ATOM   4888  O  OG  . SER B 2  485  ? -26.080 -67.080  15.374  1.00 57.88  ?  485  SER B OG  1 
ATOM   4889  N  N   . ILE B 2  486  ? -26.454 -70.477  16.909  1.00 54.82  ?  486  ILE B N   1 
ATOM   4890  C  CA  . ILE B 2  486  ? -27.582 -71.290  17.351  1.00 49.70  ?  486  ILE B CA  1 
ATOM   4891  C  C   . ILE B 2  486  ? -28.563 -70.410  18.111  1.00 46.90  ?  486  ILE B C   1 
ATOM   4892  O  O   . ILE B 2  486  ? -28.163 -69.627  18.981  1.00 51.04  ?  486  ILE B O   1 
ATOM   4893  C  CB  . ILE B 2  486  ? -27.111 -72.464  18.227  1.00 45.08  ?  486  ILE B CB  1 
ATOM   4894  C  CG1 . ILE B 2  486  ? -26.103 -73.325  17.464  1.00 55.76  ?  486  ILE B CG1 1 
ATOM   4895  C  CG2 . ILE B 2  486  ? -28.296 -73.302  18.677  1.00 44.30  ?  486  ILE B CG2 1 
ATOM   4896  C  CD1 . ILE B 2  486  ? -26.677 -73.993  16.233  1.00 55.45  ?  486  ILE B CD1 1 
ATOM   4897  N  N   . VAL B 2  487  ? -29.848 -70.540  17.785  1.00 66.62  ?  487  VAL B N   1 
ATOM   4898  C  CA  . VAL B 2  487  ? -30.912 -69.848  18.505  1.00 70.61  ?  487  VAL B CA  1 
ATOM   4899  C  C   . VAL B 2  487  ? -31.324 -70.752  19.663  1.00 73.03  ?  487  VAL B C   1 
ATOM   4900  O  O   . VAL B 2  487  ? -32.066 -71.719  19.483  1.00 76.06  ?  487  VAL B O   1 
ATOM   4901  C  CB  . VAL B 2  487  ? -32.093 -69.513  17.594  1.00 62.72  ?  487  VAL B CB  1 
ATOM   4902  C  CG1 . VAL B 2  487  ? -33.176 -68.785  18.378  1.00 62.81  ?  487  VAL B CG1 1 
ATOM   4903  C  CG2 . VAL B 2  487  ? -31.629 -68.674  16.414  1.00 69.43  ?  487  VAL B CG2 1 
ATOM   4904  N  N   . GLN B 2  488  ? -30.835 -70.434  20.859  1.00 63.88  ?  488  GLN B N   1 
ATOM   4905  C  CA  . GLN B 2  488  ? -31.083 -71.248  22.044  1.00 65.56  ?  488  GLN B CA  1 
ATOM   4906  C  C   . GLN B 2  488  ? -32.301 -70.727  22.796  1.00 65.22  ?  488  GLN B C   1 
ATOM   4907  O  O   . GLN B 2  488  ? -32.379 -69.525  23.077  1.00 61.75  ?  488  GLN B O   1 
ATOM   4908  C  CB  . GLN B 2  488  ? -29.870 -71.242  22.961  1.00 65.04  ?  488  GLN B CB  1 
ATOM   4909  C  CG  . GLN B 2  488  ? -29.874 -72.335  24.011  1.00 70.34  ?  488  GLN B CG  1 
ATOM   4910  C  CD  . GLN B 2  488  ? -28.589 -72.370  24.809  1.00 70.57  ?  488  GLN B CD  1 
ATOM   4911  O  OE1 . GLN B 2  488  ? -28.188 -73.418  25.316  1.00 72.27  ?  488  GLN B OE1 1 
ATOM   4912  N  NE2 . GLN B 2  488  ? -27.929 -71.223  24.919  1.00 70.66  ?  488  GLN B NE2 1 
ATOM   4913  N  N   . PRO B 2  489  ? -33.258 -71.584  23.135  1.00 62.38  ?  489  PRO B N   1 
ATOM   4914  C  CA  . PRO B 2  489  ? -34.432 -71.127  23.882  1.00 61.97  ?  489  PRO B CA  1 
ATOM   4915  C  C   . PRO B 2  489  ? -34.106 -70.887  25.349  1.00 62.00  ?  489  PRO B C   1 
ATOM   4916  O  O   . PRO B 2  489  ? -33.126 -71.397  25.895  1.00 63.92  ?  489  PRO B O   1 
ATOM   4917  C  CB  . PRO B 2  489  ? -35.422 -72.285  23.721  1.00 66.51  ?  489  PRO B CB  1 
ATOM   4918  C  CG  . PRO B 2  489  ? -34.549 -73.484  23.575  1.00 62.65  ?  489  PRO B CG  1 
ATOM   4919  C  CD  . PRO B 2  489  ? -33.329 -73.020  22.817  1.00 59.17  ?  489  PRO B CD  1 
ATOM   4920  N  N   . LEU B 2  490  ? -34.958 -70.084  25.985  1.00 71.07  ?  490  LEU B N   1 
ATOM   4921  C  CA  . LEU B 2  490  ? -34.837 -69.791  27.404  1.00 78.53  ?  490  LEU B CA  1 
ATOM   4922  C  C   . LEU B 2  490  ? -36.043 -70.229  28.215  1.00 80.58  ?  490  LEU B C   1 
ATOM   4923  O  O   . LEU B 2  490  ? -35.989 -70.178  29.450  1.00 82.13  ?  490  LEU B O   1 
ATOM   4924  C  CB  . LEU B 2  490  ? -34.614 -68.288  27.629  1.00 76.23  ?  490  LEU B CB  1 
ATOM   4925  C  CG  . LEU B 2  490  ? -33.186 -67.787  27.437  1.00 71.99  ?  490  LEU B CG  1 
ATOM   4926  C  CD1 . LEU B 2  490  ? -32.872 -67.635  25.958  1.00 67.42  ?  490  LEU B CD1 1 
ATOM   4927  C  CD2 . LEU B 2  490  ? -32.995 -66.476  28.179  1.00 70.89  ?  490  LEU B CD2 1 
ATOM   4928  N  N   . ILE B 2  491  ? -37.122 -70.654  27.561  1.00 56.21  ?  491  ILE B N   1 
ATOM   4929  C  CA  . ILE B 2  491  ? -38.346 -71.055  28.239  1.00 60.30  ?  491  ILE B CA  1 
ATOM   4930  C  C   . ILE B 2  491  ? -39.141 -71.908  27.266  1.00 69.84  ?  491  ILE B C   1 
ATOM   4931  O  O   . ILE B 2  491  ? -39.041 -71.740  26.048  1.00 71.85  ?  491  ILE B O   1 
ATOM   4932  C  CB  . ILE B 2  491  ? -39.149 -69.819  28.722  1.00 50.00  ?  491  ILE B CB  1 
ATOM   4933  C  CG1 . ILE B 2  491  ? -40.246 -70.227  29.708  1.00 56.13  ?  491  ILE B CG1 1 
ATOM   4934  C  CG2 . ILE B 2  491  ? -39.720 -69.045  27.542  1.00 48.06  ?  491  ILE B CG2 1 
ATOM   4935  C  CD1 . ILE B 2  491  ? -40.836 -69.063  30.467  1.00 56.15  ?  491  ILE B CD1 1 
ATOM   4936  N  N   . GLU B 2  492  ? -39.910 -72.849  27.804  1.00 88.05  ?  492  GLU B N   1 
ATOM   4937  C  CA  . GLU B 2  492  ? -40.849 -73.570  26.967  1.00 83.08  ?  492  GLU B CA  1 
ATOM   4938  C  C   . GLU B 2  492  ? -41.870 -72.584  26.400  1.00 89.45  ?  492  GLU B C   1 
ATOM   4939  O  O   . GLU B 2  492  ? -42.222 -71.600  27.059  1.00 86.68  ?  492  GLU B O   1 
ATOM   4940  C  CB  . GLU B 2  492  ? -41.550 -74.671  27.762  1.00 92.27  ?  492  GLU B CB  1 
ATOM   4941  C  CG  . GLU B 2  492  ? -40.620 -75.770  28.273  1.00 103.61 ?  492  GLU B CG  1 
ATOM   4942  C  CD  . GLU B 2  492  ? -40.215 -76.759  27.192  1.00 106.40 ?  492  GLU B CD  1 
ATOM   4943  O  OE1 . GLU B 2  492  ? -40.706 -76.638  26.049  1.00 104.96 ?  492  GLU B OE1 1 
ATOM   4944  O  OE2 . GLU B 2  492  ? -39.404 -77.662  27.487  1.00 107.10 -1 492  GLU B OE2 1 
ATOM   4945  N  N   . PRO B 2  493  ? -42.334 -72.805  25.172  1.00 91.98  ?  493  PRO B N   1 
ATOM   4946  C  CA  . PRO B 2  493  ? -43.285 -71.869  24.558  1.00 84.35  ?  493  PRO B CA  1 
ATOM   4947  C  C   . PRO B 2  493  ? -44.494 -71.627  25.450  1.00 83.46  ?  493  PRO B C   1 
ATOM   4948  O  O   . PRO B 2  493  ? -45.162 -72.565  25.892  1.00 94.80  ?  493  PRO B O   1 
ATOM   4949  C  CB  . PRO B 2  493  ? -43.669 -72.570  23.253  1.00 85.84  ?  493  PRO B CB  1 
ATOM   4950  C  CG  . PRO B 2  493  ? -42.480 -73.407  22.924  1.00 82.56  ?  493  PRO B CG  1 
ATOM   4951  C  CD  . PRO B 2  493  ? -41.952 -73.887  24.248  1.00 90.51  ?  493  PRO B CD  1 
ATOM   4952  N  N   . LEU B 2  494  ? -44.760 -70.348  25.721  1.00 73.07  ?  494  LEU B N   1 
ATOM   4953  C  CA  . LEU B 2  494  ? -45.813 -69.975  26.662  1.00 80.05  ?  494  LEU B CA  1 
ATOM   4954  C  C   . LEU B 2  494  ? -47.169 -70.502  26.208  1.00 81.57  ?  494  LEU B C   1 
ATOM   4955  O  O   . LEU B 2  494  ? -47.834 -71.254  26.929  1.00 85.17  ?  494  LEU B O   1 
ATOM   4956  C  CB  . LEU B 2  494  ? -45.851 -68.454  26.820  1.00 73.75  ?  494  LEU B CB  1 
ATOM   4957  C  CG  . LEU B 2  494  ? -44.571 -67.777  27.316  1.00 61.02  ?  494  LEU B CG  1 
ATOM   4958  C  CD1 . LEU B 2  494  ? -44.731 -66.264  27.315  1.00 60.97  ?  494  LEU B CD1 1 
ATOM   4959  C  CD2 . LEU B 2  494  ? -44.199 -68.281  28.701  1.00 68.90  ?  494  LEU B CD2 1 
ATOM   4960  N  N   . TYR B 2  495  ? -47.595 -70.111  25.009  1.00 70.88  ?  495  TYR B N   1 
ATOM   4961  C  CA  . TYR B 2  495  ? -48.876 -70.521  24.456  1.00 72.74  ?  495  TYR B CA  1 
ATOM   4962  C  C   . TYR B 2  495  ? -48.736 -71.679  23.478  1.00 77.54  ?  495  TYR B C   1 
ATOM   4963  O  O   . TYR B 2  495  ? -49.612 -71.877  22.630  1.00 82.10  ?  495  TYR B O   1 
ATOM   4964  C  CB  . TYR B 2  495  ? -49.548 -69.335  23.766  1.00 71.39  ?  495  TYR B CB  1 
ATOM   4965  C  CG  . TYR B 2  495  ? -49.311 -68.011  24.451  1.00 64.34  ?  495  TYR B CG  1 
ATOM   4966  C  CD1 . TYR B 2  495  ? -49.925 -67.710  25.658  1.00 58.92  ?  495  TYR B CD1 1 
ATOM   4967  C  CD2 . TYR B 2  495  ? -48.463 -67.064  23.892  1.00 66.45  ?  495  TYR B CD2 1 
ATOM   4968  C  CE1 . TYR B 2  495  ? -49.707 -66.499  26.286  1.00 56.41  ?  495  TYR B CE1 1 
ATOM   4969  C  CE2 . TYR B 2  495  ? -48.239 -65.853  24.512  1.00 61.38  ?  495  TYR B CE2 1 
ATOM   4970  C  CZ  . TYR B 2  495  ? -48.863 -65.576  25.709  1.00 57.60  ?  495  TYR B CZ  1 
ATOM   4971  O  OH  . TYR B 2  495  ? -48.641 -64.369  26.328  1.00 62.66  ?  495  TYR B OH  1 
ATOM   4972  N  N   . GLY B 2  496  ? -47.656 -72.449  23.581  1.00 89.40  ?  496  GLY B N   1 
ATOM   4973  C  CA  . GLY B 2  496  ? -47.344 -73.412  22.546  1.00 92.13  ?  496  GLY B CA  1 
ATOM   4974  C  C   . GLY B 2  496  ? -46.758 -72.717  21.328  1.00 97.27  ?  496  GLY B C   1 
ATOM   4975  O  O   . GLY B 2  496  ? -46.087 -71.689  21.430  1.00 103.27 ?  496  GLY B O   1 
ATOM   4976  N  N   . GLY B 2  497  ? -47.031 -73.282  20.158  1.00 85.59  ?  497  GLY B N   1 
ATOM   4977  C  CA  . GLY B 2  497  ? -46.545 -72.689  18.929  1.00 83.17  ?  497  GLY B CA  1 
ATOM   4978  C  C   . GLY B 2  497  ? -45.304 -73.369  18.391  1.00 83.14  ?  497  GLY B C   1 
ATOM   4979  O  O   . GLY B 2  497  ? -44.333 -73.580  19.124  1.00 73.68  ?  497  GLY B O   1 
ATOM   4980  N  N   . LYS B 2  498  ? -45.326 -73.710  17.109  1.00 71.06  ?  498  LYS B N   1 
ATOM   4981  C  CA  . LYS B 2  498  ? -44.250 -74.460  16.483  1.00 71.65  ?  498  LYS B CA  1 
ATOM   4982  C  C   . LYS B 2  498  ? -43.317 -73.523  15.723  1.00 68.90  ?  498  LYS B C   1 
ATOM   4983  O  O   . LYS B 2  498  ? -43.625 -72.355  15.477  1.00 63.25  ?  498  LYS B O   1 
ATOM   4984  C  CB  . LYS B 2  498  ? -44.821 -75.530  15.546  1.00 64.74  ?  498  LYS B CB  1 
ATOM   4985  C  CG  . LYS B 2  498  ? -46.127 -76.141  16.035  1.00 67.26  ?  498  LYS B CG  1 
ATOM   4986  C  CD  . LYS B 2  498  ? -45.908 -77.008  17.265  1.00 71.11  ?  498  LYS B CD  1 
ATOM   4987  C  CE  . LYS B 2  498  ? -45.168 -78.288  16.922  1.00 71.91  ?  498  LYS B CE  1 
ATOM   4988  N  NZ  . LYS B 2  498  ? -45.020 -79.169  18.113  1.00 49.76  ?  498  LYS B NZ  1 
ATOM   4989  N  N   . THR B 2  499  ? -42.156 -74.057  15.356  1.00 95.24  ?  499  THR B N   1 
ATOM   4990  C  CA  . THR B 2  499  ? -41.165 -73.328  14.584  1.00 94.64  ?  499  THR B CA  1 
ATOM   4991  C  C   . THR B 2  499  ? -41.308 -73.669  13.102  1.00 98.40  ?  499  THR B C   1 
ATOM   4992  O  O   . THR B 2  499  ? -42.162 -74.460  12.695  1.00 106.82 ?  499  THR B O   1 
ATOM   4993  C  CB  . THR B 2  499  ? -39.755 -73.641  15.090  1.00 95.47  ?  499  THR B CB  1 
ATOM   4994  O  OG1 . THR B 2  499  ? -39.349 -74.927  14.609  1.00 91.42  ?  499  THR B OG1 1 
ATOM   4995  C  CG2 . THR B 2  499  ? -39.727 -73.647  16.608  1.00 100.51 ?  499  THR B CG2 1 
ATOM   4996  N  N   . ALA B 2  500  ? -40.448 -73.060  12.282  1.00 94.09  ?  500  ALA B N   1 
ATOM   4997  C  CA  . ALA B 2  500  ? -40.526 -73.275  10.841  1.00 98.78  ?  500  ALA B CA  1 
ATOM   4998  C  C   . ALA B 2  500  ? -40.083 -74.683  10.461  1.00 106.29 ?  500  ALA B C   1 
ATOM   4999  O  O   . ALA B 2  500  ? -40.733 -75.342  9.640   1.00 105.23 ?  500  ALA B O   1 
ATOM   5000  C  CB  . ALA B 2  500  ? -39.683 -72.231  10.109  1.00 89.63  ?  500  ALA B CB  1 
ATOM   5001  N  N   . ASN B 2  501  ? -38.980 -75.161  11.043  1.00 110.92 ?  501  ASN B N   1 
ATOM   5002  C  CA  . ASN B 2  501  ? -38.487 -76.491  10.704  1.00 107.47 ?  501  ASN B CA  1 
ATOM   5003  C  C   . ASN B 2  501  ? -39.413 -77.586  11.220  1.00 107.60 ?  501  ASN B C   1 
ATOM   5004  O  O   . ASN B 2  501  ? -39.434 -78.689  10.662  1.00 118.14 ?  501  ASN B O   1 
ATOM   5005  C  CB  . ASN B 2  501  ? -37.072 -76.683  11.249  1.00 98.36  ?  501  ASN B CB  1 
ATOM   5006  C  CG  . ASN B 2  501  ? -36.957 -76.315  12.713  1.00 116.94 ?  501  ASN B CG  1 
ATOM   5007  O  OD1 . ASN B 2  501  ? -37.952 -76.012  13.369  1.00 118.88 ?  501  ASN B OD1 1 
ATOM   5008  N  ND2 . ASN B 2  501  ? -35.737 -76.337  13.233  1.00 119.52 ?  501  ASN B ND2 1 
ATOM   5009  N  N   . GLU B 2  502  ? -40.180 -77.308  12.279  1.00 74.16  ?  502  GLU B N   1 
ATOM   5010  C  CA  . GLU B 2  502  ? -41.177 -78.274  12.731  1.00 81.81  ?  502  GLU B CA  1 
ATOM   5011  C  C   . GLU B 2  502  ? -42.281 -78.445  11.695  1.00 88.93  ?  502  GLU B C   1 
ATOM   5012  O  O   . GLU B 2  502  ? -42.754 -79.564  11.461  1.00 88.92  ?  502  GLU B O   1 
ATOM   5013  C  CB  . GLU B 2  502  ? -41.764 -77.846  14.077  1.00 78.25  ?  502  GLU B CB  1 
ATOM   5014  C  CG  . GLU B 2  502  ? -40.951 -78.293  15.286  1.00 81.18  ?  502  GLU B CG  1 
ATOM   5015  C  CD  . GLU B 2  502  ? -41.419 -77.650  16.581  1.00 81.59  ?  502  GLU B CD  1 
ATOM   5016  O  OE1 . GLU B 2  502  ? -41.651 -76.423  16.589  1.00 79.33  ?  502  GLU B OE1 1 
ATOM   5017  O  OE2 . GLU B 2  502  ? -41.555 -78.371  17.592  1.00 82.91  -1 502  GLU B OE2 1 
ATOM   5018  N  N   . LEU B 2  503  ? -42.705 -77.348  11.064  1.00 103.08 ?  503  LEU B N   1 
ATOM   5019  C  CA  . LEU B 2  503  ? -43.674 -77.456  9.980   1.00 106.58 ?  503  LEU B CA  1 
ATOM   5020  C  C   . LEU B 2  503  ? -43.071 -78.170  8.776   1.00 109.38 ?  503  LEU B C   1 
ATOM   5021  O  O   . LEU B 2  503  ? -43.714 -79.042  8.180   1.00 114.50 ?  503  LEU B O   1 
ATOM   5022  C  CB  . LEU B 2  503  ? -44.176 -76.074  9.570   1.00 93.03  ?  503  LEU B CB  1 
ATOM   5023  C  CG  . LEU B 2  503  ? -45.133 -76.136  8.376   1.00 99.14  ?  503  LEU B CG  1 
ATOM   5024  C  CD1 . LEU B 2  503  ? -46.356 -76.984  8.709   1.00 108.18 ?  503  LEU B CD1 1 
ATOM   5025  C  CD2 . LEU B 2  503  ? -45.533 -74.761  7.885   1.00 95.17  ?  503  LEU B CD2 1 
ATOM   5026  N  N   . LEU B 2  504  ? -41.838 -77.809  8.402   1.00 90.99  ?  504  LEU B N   1 
ATOM   5027  C  CA  . LEU B 2  504  ? -41.184 -78.462  7.272   1.00 89.67  ?  504  LEU B CA  1 
ATOM   5028  C  C   . LEU B 2  504  ? -41.027 -79.959  7.502   1.00 94.20  ?  504  LEU B C   1 
ATOM   5029  O  O   . LEU B 2  504  ? -41.115 -80.742  6.550   1.00 101.33 ?  504  LEU B O   1 
ATOM   5030  C  CB  . LEU B 2  504  ? -39.821 -77.819  7.004   1.00 88.04  ?  504  LEU B CB  1 
ATOM   5031  C  CG  . LEU B 2  504  ? -39.774 -76.745  5.915   1.00 85.30  ?  504  LEU B CG  1 
ATOM   5032  C  CD1 . LEU B 2  504  ? -40.003 -77.366  4.544   1.00 95.12  ?  504  LEU B CD1 1 
ATOM   5033  C  CD2 . LEU B 2  504  ? -40.788 -75.645  6.184   1.00 89.22  ?  504  LEU B CD2 1 
ATOM   5034  N  N   . ALA B 2  505  ? -40.793 -80.375  8.748   1.00 107.52 ?  505  ALA B N   1 
ATOM   5035  C  CA  . ALA B 2  505  ? -40.788 -81.800  9.055   1.00 110.23 ?  505  ALA B CA  1 
ATOM   5036  C  C   . ALA B 2  505  ? -42.187 -82.394  8.958   1.00 112.79 ?  505  ALA B C   1 
ATOM   5037  O  O   . ALA B 2  505  ? -42.338 -83.564  8.588   1.00 122.60 ?  505  ALA B O   1 
ATOM   5038  C  CB  . ALA B 2  505  ? -40.208 -82.040  10.449  1.00 106.23 ?  505  ALA B CB  1 
ATOM   5039  N  N   . ALA B 2  506  ? -43.216 -81.610  9.288   1.00 81.76  ?  506  ALA B N   1 
ATOM   5040  C  CA  . ALA B 2  506  ? -44.585 -82.099  9.165   1.00 79.86  ?  506  ALA B CA  1 
ATOM   5041  C  C   . ALA B 2  506  ? -44.964 -82.313  7.704   1.00 85.38  ?  506  ALA B C   1 
ATOM   5042  O  O   . ALA B 2  506  ? -45.627 -83.301  7.368   1.00 91.05  ?  506  ALA B O   1 
ATOM   5043  C  CB  . ALA B 2  506  ? -45.554 -81.128  9.838   1.00 83.62  ?  506  ALA B CB  1 
ATOM   5044  N  N   . MET B 2  507  ? -44.553 -81.398  6.821   1.00 86.00  ?  507  MET B N   1 
ATOM   5045  C  CA  . MET B 2  507  ? -44.778 -81.592  5.394   1.00 83.01  ?  507  MET B CA  1 
ATOM   5046  C  C   . MET B 2  507  ? -43.888 -82.685  4.815   1.00 76.66  ?  507  MET B C   1 
ATOM   5047  O  O   . MET B 2  507  ? -44.160 -83.170  3.713   1.00 75.35  ?  507  MET B O   1 
ATOM   5048  C  CB  . MET B 2  507  ? -44.554 -80.282  4.637   1.00 79.12  ?  507  MET B CB  1 
ATOM   5049  C  CG  . MET B 2  507  ? -45.121 -79.058  5.334   1.00 69.41  ?  507  MET B CG  1 
ATOM   5050  S  SD  . MET B 2  507  ? -45.345 -77.654  4.225   1.00 103.15 ?  507  MET B SD  1 
ATOM   5051  C  CE  . MET B 2  507  ? -43.643 -77.176  3.940   1.00 87.07  ?  507  MET B CE  1 
ATOM   5052  N  N   . LEU B 2  508  ? -42.832 -83.077  5.530   1.00 76.37  ?  508  LEU B N   1 
ATOM   5053  C  CA  . LEU B 2  508  ? -41.980 -84.190  5.130   1.00 75.54  ?  508  LEU B CA  1 
ATOM   5054  C  C   . LEU B 2  508  ? -42.402 -85.507  5.770   1.00 80.21  ?  508  LEU B C   1 
ATOM   5055  O  O   . LEU B 2  508  ? -41.554 -86.380  6.003   1.00 77.64  ?  508  LEU B O   1 
ATOM   5056  C  CB  . LEU B 2  508  ? -40.519 -83.880  5.461   1.00 73.69  ?  508  LEU B CB  1 
ATOM   5057  C  CG  . LEU B 2  508  ? -39.780 -82.983  4.468   1.00 80.24  ?  508  LEU B CG  1 
ATOM   5058  C  CD1 . LEU B 2  508  ? -38.547 -82.369  5.114   1.00 84.00  ?  508  LEU B CD1 1 
ATOM   5059  C  CD2 . LEU B 2  508  ? -39.406 -83.764  3.219   1.00 86.97  ?  508  LEU B CD2 1 
ATOM   5060  N  N   . GLY B 2  509  ? -43.689 -85.669  6.068   1.00 65.00  ?  509  GLY B N   1 
ATOM   5061  C  CA  . GLY B 2  509  ? -44.180 -86.912  6.636   1.00 72.33  ?  509  GLY B CA  1 
ATOM   5062  C  C   . GLY B 2  509  ? -43.582 -87.257  7.980   1.00 75.25  ?  509  GLY B C   1 
ATOM   5063  O  O   . GLY B 2  509  ? -43.395 -88.440  8.283   1.00 89.95  ?  509  GLY B O   1 
ATOM   5064  N  N   . GLN B 2  510  ? -43.273 -86.254  8.797   1.00 104.83 ?  510  GLN B N   1 
ATOM   5065  C  CA  . GLN B 2  510  ? -42.675 -86.461  10.117  1.00 104.74 ?  510  GLN B CA  1 
ATOM   5066  C  C   . GLN B 2  510  ? -43.369 -85.551  11.119  1.00 103.54 ?  510  GLN B C   1 
ATOM   5067  O  O   . GLN B 2  510  ? -42.802 -84.551  11.576  1.00 103.62 ?  510  GLN B O   1 
ATOM   5068  C  CB  . GLN B 2  510  ? -41.169 -86.196  10.078  1.00 99.96  ?  510  GLN B CB  1 
ATOM   5069  C  CG  . GLN B 2  510  ? -40.349 -87.094  10.985  1.00 102.32 ?  510  GLN B CG  1 
ATOM   5070  C  CD  . GLN B 2  510  ? -38.859 -86.856  10.836  1.00 113.12 ?  510  GLN B CD  1 
ATOM   5071  O  OE1 . GLN B 2  510  ? -38.400 -86.340  9.817   1.00 114.35 ?  510  GLN B OE1 1 
ATOM   5072  N  NE2 . GLN B 2  510  ? -38.095 -87.232  11.854  1.00 106.52 ?  510  GLN B NE2 1 
ATOM   5073  N  N   . PRO B 2  511  ? -44.612 -85.871  11.488  1.00 110.99 ?  511  PRO B N   1 
ATOM   5074  C  CA  . PRO B 2  511  ? -45.318 -85.040  12.471  1.00 114.91 ?  511  PRO B CA  1 
ATOM   5075  C  C   . PRO B 2  511  ? -44.758 -85.219  13.872  1.00 121.69 ?  511  PRO B C   1 
ATOM   5076  O  O   . PRO B 2  511  ? -43.831 -86.010  14.073  1.00 122.32 ?  511  PRO B O   1 
ATOM   5077  C  CB  . PRO B 2  511  ? -46.766 -85.533  12.373  1.00 113.21 ?  511  PRO B CB  1 
ATOM   5078  C  CG  . PRO B 2  511  ? -46.644 -86.946  11.927  1.00 123.04 ?  511  PRO B CG  1 
ATOM   5079  C  CD  . PRO B 2  511  ? -45.426 -87.016  11.042  1.00 119.31 ?  511  PRO B CD  1 
ATOM   5080  N  N   . GLU B 2  512  ? -45.332 -84.497  14.841  1.00 125.72 ?  512  GLU B N   1 
ATOM   5081  C  CA  . GLU B 2  512  ? -44.894 -84.460  16.237  1.00 125.54 ?  512  GLU B CA  1 
ATOM   5082  C  C   . GLU B 2  512  ? -43.377 -84.532  16.385  1.00 117.32 ?  512  GLU B C   1 
ATOM   5083  O  O   . GLU B 2  512  ? -42.861 -85.236  17.259  1.00 111.76 ?  512  GLU B O   1 
ATOM   5084  C  CB  . GLU B 2  512  ? -45.569 -85.576  17.052  1.00 138.12 ?  512  GLU B CB  1 
ATOM   5085  C  CG  . GLU B 2  512  ? -45.319 -87.010  16.590  1.00 143.77 ?  512  GLU B CG  1 
ATOM   5086  C  CD  . GLU B 2  512  ? -46.470 -87.569  15.775  1.00 145.13 ?  512  GLU B CD  1 
ATOM   5087  O  OE1 . GLU B 2  512  ? -47.478 -86.853  15.597  1.00 143.06 ?  512  GLU B OE1 1 
ATOM   5088  O  OE2 . GLU B 2  512  ? -46.367 -88.724  15.310  1.00 140.19 -1 512  GLU B OE2 1 
ATOM   5089  N  N   . ALA B 2  513  ? -42.658 -83.794  15.542  1.00 113.90 ?  513  ALA B N   1 
ATOM   5090  C  CA  . ALA B 2  513  ? -41.204 -83.758  15.585  1.00 107.82 ?  513  ALA B CA  1 
ATOM   5091  C  C   . ALA B 2  513  ? -40.748 -82.616  16.484  1.00 97.64  ?  513  ALA B C   1 
ATOM   5092  O  O   . ALA B 2  513  ? -41.218 -81.483  16.346  1.00 93.49  ?  513  ALA B O   1 
ATOM   5093  C  CB  . ALA B 2  513  ? -40.622 -83.597  14.180  1.00 104.65 ?  513  ALA B CB  1 
ATOM   5094  N  N   . GLU B 2  514  ? -39.836 -82.921  17.402  1.00 113.43 ?  514  GLU B N   1 
ATOM   5095  C  CA  . GLU B 2  514  ? -39.343 -81.927  18.344  1.00 118.97 ?  514  GLU B CA  1 
ATOM   5096  C  C   . GLU B 2  514  ? -38.355 -80.984  17.668  1.00 107.21 ?  514  GLU B C   1 
ATOM   5097  O  O   . GLU B 2  514  ? -37.487 -81.414  16.903  1.00 100.41 ?  514  GLU B O   1 
ATOM   5098  C  CB  . GLU B 2  514  ? -38.682 -82.610  19.544  1.00 123.21 ?  514  GLU B CB  1 
ATOM   5099  C  CG  . GLU B 2  514  ? -39.516 -83.710  20.206  1.00 126.96 ?  514  GLU B CG  1 
ATOM   5100  C  CD  . GLU B 2  514  ? -40.702 -83.191  21.016  1.00 135.49 ?  514  GLU B CD  1 
ATOM   5101  O  OE1 . GLU B 2  514  ? -41.269 -82.128  20.682  1.00 130.38 ?  514  GLU B OE1 1 
ATOM   5102  O  OE2 . GLU B 2  514  ? -41.074 -83.866  21.998  1.00 141.97 -1 514  GLU B OE2 1 
ATOM   5103  N  N   . SER B 2  515  ? -38.490 -79.687  17.962  1.00 80.51  ?  515  SER B N   1 
ATOM   5104  C  CA  . SER B 2  515  ? -37.587 -78.700  17.378  1.00 78.86  ?  515  SER B CA  1 
ATOM   5105  C  C   . SER B 2  515  ? -36.157 -78.883  17.872  1.00 78.34  ?  515  SER B C   1 
ATOM   5106  O  O   . SER B 2  515  ? -35.209 -78.526  17.163  1.00 78.03  ?  515  SER B O   1 
ATOM   5107  C  CB  . SER B 2  515  ? -38.077 -77.285  17.686  1.00 69.93  ?  515  SER B CB  1 
ATOM   5108  O  OG  . SER B 2  515  ? -38.226 -77.087  19.080  1.00 84.22  ?  515  SER B OG  1 
ATOM   5109  N  N   . TYR B 2  516  ? -35.983 -79.431  19.077  1.00 65.70  ?  516  TYR B N   1 
ATOM   5110  C  CA  . TYR B 2  516  ? -34.643 -79.722  19.575  1.00 58.44  ?  516  TYR B CA  1 
ATOM   5111  C  C   . TYR B 2  516  ? -33.970 -80.795  18.730  1.00 71.56  ?  516  TYR B C   1 
ATOM   5112  O  O   . TYR B 2  516  ? -32.826 -80.632  18.292  1.00 67.85  ?  516  TYR B O   1 
ATOM   5113  C  CB  . TYR B 2  516  ? -34.709 -80.161  21.038  1.00 58.16  ?  516  TYR B CB  1 
ATOM   5114  C  CG  . TYR B 2  516  ? -33.359 -80.465  21.652  1.00 63.09  ?  516  TYR B CG  1 
ATOM   5115  C  CD1 . TYR B 2  516  ? -32.271 -79.626  21.444  1.00 63.55  ?  516  TYR B CD1 1 
ATOM   5116  C  CD2 . TYR B 2  516  ? -33.168 -81.599  22.432  1.00 59.50  ?  516  TYR B CD2 1 
ATOM   5117  C  CE1 . TYR B 2  516  ? -31.036 -79.901  22.004  1.00 62.55  ?  516  TYR B CE1 1 
ATOM   5118  C  CE2 . TYR B 2  516  ? -31.937 -81.884  22.993  1.00 55.18  ?  516  TYR B CE2 1 
ATOM   5119  C  CZ  . TYR B 2  516  ? -30.874 -81.031  22.776  1.00 59.46  ?  516  TYR B CZ  1 
ATOM   5120  O  OH  . TYR B 2  516  ? -29.646 -81.308  23.332  1.00 55.41  ?  516  TYR B OH  1 
ATOM   5121  N  N   . ASP B 2  517  ? -34.674 -81.904  18.488  1.00 94.07  ?  517  ASP B N   1 
ATOM   5122  C  CA  . ASP B 2  517  ? -34.079 -83.021  17.764  1.00 93.18  ?  517  ASP B CA  1 
ATOM   5123  C  C   . ASP B 2  517  ? -33.815 -82.679  16.304  1.00 93.75  ?  517  ASP B C   1 
ATOM   5124  O  O   . ASP B 2  517  ? -32.907 -83.252  15.693  1.00 88.14  ?  517  ASP B O   1 
ATOM   5125  C  CB  . ASP B 2  517  ? -34.983 -84.250  17.865  1.00 94.51  ?  517  ASP B CB  1 
ATOM   5126  C  CG  . ASP B 2  517  ? -34.979 -84.862  19.250  1.00 104.07 ?  517  ASP B CG  1 
ATOM   5127  O  OD1 . ASP B 2  517  ? -33.954 -84.740  19.952  1.00 103.25 ?  517  ASP B OD1 1 
ATOM   5128  O  OD2 . ASP B 2  517  ? -36.002 -85.466  19.637  1.00 111.19 -1 517  ASP B OD2 1 
ATOM   5129  N  N   . LEU B 2  518  ? -34.588 -81.757  15.727  1.00 76.02  ?  518  LEU B N   1 
ATOM   5130  C  CA  . LEU B 2  518  ? -34.407 -81.415  14.319  1.00 70.68  ?  518  LEU B CA  1 
ATOM   5131  C  C   . LEU B 2  518  ? -33.101 -80.661  14.100  1.00 71.49  ?  518  LEU B C   1 
ATOM   5132  O  O   . LEU B 2  518  ? -32.272 -81.059  13.273  1.00 74.54  ?  518  LEU B O   1 
ATOM   5133  C  CB  . LEU B 2  518  ? -35.598 -80.595  13.818  1.00 76.75  ?  518  LEU B CB  1 
ATOM   5134  C  CG  . LEU B 2  518  ? -36.922 -81.346  13.662  1.00 76.47  ?  518  LEU B CG  1 
ATOM   5135  C  CD1 . LEU B 2  518  ? -38.046 -80.387  13.303  1.00 81.27  ?  518  LEU B CD1 1 
ATOM   5136  C  CD2 . LEU B 2  518  ? -36.797 -82.450  12.623  1.00 80.37  ?  518  LEU B CD2 1 
ATOM   5137  N  N   . VAL B 2  519  ? -32.901 -79.561  14.831  1.00 61.04  ?  519  VAL B N   1 
ATOM   5138  C  CA  . VAL B 2  519  ? -31.665 -78.798  14.683  1.00 61.76  ?  519  VAL B CA  1 
ATOM   5139  C  C   . VAL B 2  519  ? -30.475 -79.590  15.207  1.00 60.69  ?  519  VAL B C   1 
ATOM   5140  O  O   . VAL B 2  519  ? -29.350 -79.428  14.720  1.00 59.12  ?  519  VAL B O   1 
ATOM   5141  C  CB  . VAL B 2  519  ? -31.782 -77.429  15.381  1.00 55.18  ?  519  VAL B CB  1 
ATOM   5142  C  CG1 . VAL B 2  519  ? -32.843 -76.576  14.710  1.00 48.58  ?  519  VAL B CG1 1 
ATOM   5143  C  CG2 . VAL B 2  519  ? -32.093 -77.604  16.858  1.00 68.12  ?  519  VAL B CG2 1 
ATOM   5144  N  N   . ARG B 2  520  ? -30.693 -80.457  16.199  1.00 78.56  ?  520  ARG B N   1 
ATOM   5145  C  CA  . ARG B 2  520  ? -29.596 -81.265  16.719  1.00 83.68  ?  520  ARG B CA  1 
ATOM   5146  C  C   . ARG B 2  520  ? -29.212 -82.377  15.752  1.00 86.79  ?  520  ARG B C   1 
ATOM   5147  O  O   . ARG B 2  520  ? -28.040 -82.760  15.687  1.00 83.49  ?  520  ARG B O   1 
ATOM   5148  C  CB  . ARG B 2  520  ? -29.972 -81.844  18.083  1.00 78.15  ?  520  ARG B CB  1 
ATOM   5149  C  CG  . ARG B 2  520  ? -28.814 -82.436  18.865  1.00 81.77  ?  520  ARG B CG  1 
ATOM   5150  C  CD  . ARG B 2  520  ? -29.308 -83.098  20.140  1.00 77.36  ?  520  ARG B CD  1 
ATOM   5151  N  NE  . ARG B 2  520  ? -28.314 -83.047  21.205  1.00 79.42  ?  520  ARG B NE  1 
ATOM   5152  C  CZ  . ARG B 2  520  ? -27.454 -84.019  21.476  1.00 85.27  ?  520  ARG B CZ  1 
ATOM   5153  N  NH1 . ARG B 2  520  ? -27.432 -85.140  20.773  1.00 88.93  ?  520  ARG B NH1 1 
ATOM   5154  N  NH2 . ARG B 2  520  ? -26.597 -83.865  22.481  1.00 88.20  ?  520  ARG B NH2 1 
ATOM   5155  N  N   . SER B 2  521  ? -30.177 -82.902  14.991  1.00 100.86 ?  521  SER B N   1 
ATOM   5156  C  CA  . SER B 2  521  ? -29.858 -83.938  14.013  1.00 107.03 ?  521  SER B CA  1 
ATOM   5157  C  C   . SER B 2  521  ? -29.116 -83.358  12.816  1.00 104.53 ?  521  SER B C   1 
ATOM   5158  O  O   . SER B 2  521  ? -28.204 -83.995  12.276  1.00 110.00 ?  521  SER B O   1 
ATOM   5159  C  CB  . SER B 2  521  ? -31.132 -84.648  13.554  1.00 107.56 ?  521  SER B CB  1 
ATOM   5160  O  OG  . SER B 2  521  ? -31.675 -85.448  14.589  1.00 114.14 ?  521  SER B OG  1 
ATOM   5161  N  N   . PHE B 2  522  ? -29.492 -82.151  12.385  1.00 80.39  ?  522  PHE B N   1 
ATOM   5162  C  CA  . PHE B 2  522  ? -28.817 -81.538  11.246  1.00 83.37  ?  522  PHE B CA  1 
ATOM   5163  C  C   . PHE B 2  522  ? -27.420 -81.063  11.621  1.00 85.68  ?  522  PHE B C   1 
ATOM   5164  O  O   . PHE B 2  522  ? -26.466 -81.264  10.861  1.00 85.03  ?  522  PHE B O   1 
ATOM   5165  C  CB  . PHE B 2  522  ? -29.644 -80.375  10.701  1.00 83.94  ?  522  PHE B CB  1 
ATOM   5166  C  CG  . PHE B 2  522  ? -28.939 -79.580  9.636   1.00 83.29  ?  522  PHE B CG  1 
ATOM   5167  C  CD1 . PHE B 2  522  ? -28.911 -80.026  8.325   1.00 84.59  ?  522  PHE B CD1 1 
ATOM   5168  C  CD2 . PHE B 2  522  ? -28.299 -78.391  9.946   1.00 79.54  ?  522  PHE B CD2 1 
ATOM   5169  C  CE1 . PHE B 2  522  ? -28.261 -79.300  7.345   1.00 77.92  ?  522  PHE B CE1 1 
ATOM   5170  C  CE2 . PHE B 2  522  ? -27.647 -77.662  8.970   1.00 71.69  ?  522  PHE B CE2 1 
ATOM   5171  C  CZ  . PHE B 2  522  ? -27.629 -78.116  7.668   1.00 74.75  ?  522  PHE B CZ  1 
ATOM   5172  N  N   . TRP B 2  523  ? -27.279 -80.424  12.784  1.00 75.38  ?  523  TRP B N   1 
ATOM   5173  C  CA  . TRP B 2  523  ? -25.978 -79.896  13.175  1.00 70.81  ?  523  TRP B CA  1 
ATOM   5174  C  C   . TRP B 2  523  ? -25.023 -80.988  13.634  1.00 69.02  ?  523  TRP B C   1 
ATOM   5175  O  O   . TRP B 2  523  ? -23.805 -80.790  13.576  1.00 68.68  ?  523  TRP B O   1 
ATOM   5176  C  CB  . TRP B 2  523  ? -26.148 -78.833  14.259  1.00 68.24  ?  523  TRP B CB  1 
ATOM   5177  C  CG  . TRP B 2  523  ? -26.519 -77.498  13.688  1.00 71.21  ?  523  TRP B CG  1 
ATOM   5178  C  CD1 . TRP B 2  523  ? -27.673 -76.804  13.907  1.00 74.43  ?  523  TRP B CD1 1 
ATOM   5179  C  CD2 . TRP B 2  523  ? -25.739 -76.702  12.785  1.00 72.40  ?  523  TRP B CD2 1 
ATOM   5180  N  NE1 . TRP B 2  523  ? -27.657 -75.623  13.205  1.00 73.36  ?  523  TRP B NE1 1 
ATOM   5181  C  CE2 . TRP B 2  523  ? -26.481 -75.537  12.508  1.00 76.20  ?  523  TRP B CE2 1 
ATOM   5182  C  CE3 . TRP B 2  523  ? -24.483 -76.860  12.189  1.00 70.48  ?  523  TRP B CE3 1 
ATOM   5183  C  CZ2 . TRP B 2  523  ? -26.010 -74.536  11.661  1.00 70.56  ?  523  TRP B CZ2 1 
ATOM   5184  C  CZ3 . TRP B 2  523  ? -24.019 -75.866  11.350  1.00 70.68  ?  523  TRP B CZ3 1 
ATOM   5185  C  CH2 . TRP B 2  523  ? -24.780 -74.719  11.094  1.00 68.35  ?  523  TRP B CH2 1 
ATOM   5186  N  N   . LEU B 2  524  ? -25.538 -82.131  14.081  1.00 102.01 ?  524  LEU B N   1 
ATOM   5187  C  CA  . LEU B 2  524  ? -24.692 -83.301  14.250  1.00 108.92 ?  524  LEU B CA  1 
ATOM   5188  C  C   . LEU B 2  524  ? -24.278 -83.825  12.875  1.00 123.76 ?  524  LEU B C   1 
ATOM   5189  O  O   . LEU B 2  524  ? -24.685 -83.303  11.833  1.00 129.56 ?  524  LEU B O   1 
ATOM   5190  C  CB  . LEU B 2  524  ? -25.414 -84.371  15.065  1.00 109.10 ?  524  LEU B CB  1 
ATOM   5191  C  CG  . LEU B 2  524  ? -25.072 -84.457  16.557  1.00 112.30 ?  524  LEU B CG  1 
ATOM   5192  C  CD1 . LEU B 2  524  ? -25.224 -83.105  17.244  1.00 105.92 ?  524  LEU B CD1 1 
ATOM   5193  C  CD2 . LEU B 2  524  ? -25.933 -85.503  17.241  1.00 114.40 ?  524  LEU B CD2 1 
ATOM   5194  N  N   . GLU B 2  525  ? -23.426 -84.854  12.881  1.00 161.59 ?  525  GLU B N   1 
ATOM   5195  C  CA  . GLU B 2  525  ? -22.857 -85.468  11.680  1.00 167.12 ?  525  GLU B CA  1 
ATOM   5196  C  C   . GLU B 2  525  ? -22.189 -84.441  10.765  1.00 164.42 ?  525  GLU B C   1 
ATOM   5197  O  O   . GLU B 2  525  ? -21.795 -84.765  9.640   1.00 156.67 ?  525  GLU B O   1 
ATOM   5198  C  CB  . GLU B 2  525  ? -23.926 -86.274  10.923  1.00 166.39 ?  525  GLU B CB  1 
ATOM   5199  C  CG  . GLU B 2  525  ? -24.758 -85.511  9.893   1.00 164.49 ?  525  GLU B CG  1 
ATOM   5200  C  CD  . GLU B 2  525  ? -25.864 -86.353  9.290   1.00 184.52 ?  525  GLU B CD  1 
ATOM   5201  O  OE1 . GLU B 2  525  ? -25.997 -87.532  9.682   1.00 193.96 ?  525  GLU B OE1 1 
ATOM   5202  O  OE2 . GLU B 2  525  ? -26.602 -85.836  8.425   1.00 190.69 -1 525  GLU B OE2 1 
ATOM   5203  N  N   . GLN B 2  526  ? -22.035 -83.213  11.249  1.00 124.43 ?  526  GLN B N   1 
ATOM   5204  C  CA  . GLN B 2  526  ? -21.355 -82.127  10.552  1.00 118.49 ?  526  GLN B CA  1 
ATOM   5205  C  C   . GLN B 2  526  ? -20.286 -81.467  11.408  1.00 115.09 ?  526  GLN B C   1 
ATOM   5206  O  O   . GLN B 2  526  ? -19.180 -81.224  10.920  1.00 120.52 ?  526  GLN B O   1 
ATOM   5207  C  CB  . GLN B 2  526  ? -22.374 -81.071  10.084  1.00 114.37 ?  526  GLN B CB  1 
ATOM   5208  C  CG  . GLN B 2  526  ? -21.761 -79.925  9.293   1.00 109.62 ?  526  GLN B CG  1 
ATOM   5209  C  CD  . GLN B 2  526  ? -22.781 -79.183  8.448   1.00 116.57 ?  526  GLN B CD  1 
ATOM   5210  O  OE1 . GLN B 2  526  ? -23.895 -79.661  8.234   1.00 121.74 ?  526  GLN B OE1 1 
ATOM   5211  N  NE2 . GLN B 2  526  ? -22.402 -78.005  7.965   1.00 112.06 ?  526  GLN B NE2 1 
ATOM   5212  N  N   . ILE B 2  527  ? -20.586 -81.171  12.671  1.00 91.68  ?  527  ILE B N   1 
ATOM   5213  C  CA  . ILE B 2  527  ? -19.602 -80.619  13.595  1.00 94.50  ?  527  ILE B CA  1 
ATOM   5214  C  C   . ILE B 2  527  ? -19.352 -81.515  14.798  1.00 86.64  ?  527  ILE B C   1 
ATOM   5215  O  O   . ILE B 2  527  ? -18.377 -81.283  15.529  1.00 77.37  ?  527  ILE B O   1 
ATOM   5216  C  CB  . ILE B 2  527  ? -19.998 -79.203  14.069  1.00 95.54  ?  527  ILE B CB  1 
ATOM   5217  C  CG1 . ILE B 2  527  ? -21.245 -79.260  14.955  1.00 93.25  ?  527  ILE B CG1 1 
ATOM   5218  C  CG2 . ILE B 2  527  ? -20.221 -78.282  12.879  1.00 92.27  ?  527  ILE B CG2 1 
ATOM   5219  C  CD1 . ILE B 2  527  ? -21.734 -77.899  15.405  1.00 80.65  ?  527  ILE B CD1 1 
ATOM   5220  N  N   . GLY B 2  528  ? -20.189 -82.522  15.034  1.00 118.89 ?  528  GLY B N   1 
ATOM   5221  C  CA  . GLY B 2  528  ? -19.988 -83.447  16.129  1.00 121.62 ?  528  GLY B CA  1 
ATOM   5222  C  C   . GLY B 2  528  ? -20.744 -83.053  17.386  1.00 110.87 ?  528  GLY B C   1 
ATOM   5223  O  O   . GLY B 2  528  ? -21.291 -81.956  17.516  1.00 118.33 ?  528  GLY B O   1 
ATOM   5224  N  N   . GLU B 2  529  ? -20.771 -83.990  18.337  1.00 76.46  ?  529  GLU B N   1 
ATOM   5225  C  CA  . GLU B 2  529  ? -21.433 -83.726  19.610  1.00 81.09  ?  529  GLU B CA  1 
ATOM   5226  C  C   . GLU B 2  529  ? -20.636 -82.737  20.450  1.00 74.20  ?  529  GLU B C   1 
ATOM   5227  O  O   . GLU B 2  529  ? -21.213 -81.840  21.076  1.00 68.33  ?  529  GLU B O   1 
ATOM   5228  C  CB  . GLU B 2  529  ? -21.645 -85.031  20.375  1.00 84.00  ?  529  GLU B CB  1 
ATOM   5229  C  CG  . GLU B 2  529  ? -22.188 -84.834  21.779  1.00 90.83  ?  529  GLU B CG  1 
ATOM   5230  C  CD  . GLU B 2  529  ? -23.583 -84.243  21.782  1.00 88.61  ?  529  GLU B CD  1 
ATOM   5231  O  OE1 . GLU B 2  529  ? -24.407 -84.656  20.937  1.00 81.98  ?  529  GLU B OE1 1 
ATOM   5232  O  OE2 . GLU B 2  529  ? -23.857 -83.361  22.624  1.00 83.11  -1 529  GLU B OE2 1 
ATOM   5233  N  N   . THR B 2  530  ? -19.310 -82.886  20.480  1.00 87.72  ?  530  THR B N   1 
ATOM   5234  C  CA  . THR B 2  530  ? -18.481 -81.921  21.192  1.00 87.77  ?  530  THR B CA  1 
ATOM   5235  C  C   . THR B 2  530  ? -18.529 -80.549  20.531  1.00 89.18  ?  530  THR B C   1 
ATOM   5236  O  O   . THR B 2  530  ? -18.398 -79.528  21.216  1.00 91.41  ?  530  THR B O   1 
ATOM   5237  C  CB  . THR B 2  530  ? -17.040 -82.424  21.284  1.00 83.03  ?  530  THR B CB  1 
ATOM   5238  O  OG1 . THR B 2  530  ? -16.233 -81.452  21.963  1.00 87.35  ?  530  THR B OG1 1 
ATOM   5239  C  CG2 . THR B 2  530  ? -16.464 -82.687  19.898  1.00 86.84  ?  530  THR B CG2 1 
ATOM   5240  N  N   . GLY B 2  531  ? -18.720 -80.500  19.211  1.00 105.53 ?  531  GLY B N   1 
ATOM   5241  C  CA  . GLY B 2  531  ? -18.885 -79.218  18.548  1.00 99.84  ?  531  GLY B CA  1 
ATOM   5242  C  C   . GLY B 2  531  ? -20.215 -78.569  18.878  1.00 102.01 ?  531  GLY B C   1 
ATOM   5243  O  O   . GLY B 2  531  ? -20.304 -77.345  19.009  1.00 105.70 ?  531  GLY B O   1 
ATOM   5244  N  N   . TRP B 2  532  ? -21.267 -79.380  19.019  1.00 76.73  ?  532  TRP B N   1 
ATOM   5245  C  CA  . TRP B 2  532  ? -22.564 -78.850  19.426  1.00 74.36  ?  532  TRP B CA  1 
ATOM   5246  C  C   . TRP B 2  532  ? -22.515 -78.309  20.850  1.00 77.94  ?  532  TRP B C   1 
ATOM   5247  O  O   . TRP B 2  532  ? -23.143 -77.287  21.154  1.00 80.97  ?  532  TRP B O   1 
ATOM   5248  C  CB  . TRP B 2  532  ? -23.633 -79.937  19.293  1.00 72.19  ?  532  TRP B CB  1 
ATOM   5249  C  CG  . TRP B 2  532  ? -24.933 -79.607  19.964  1.00 69.35  ?  532  TRP B CG  1 
ATOM   5250  C  CD1 . TRP B 2  532  ? -25.313 -79.950  21.229  1.00 79.84  ?  532  TRP B CD1 1 
ATOM   5251  C  CD2 . TRP B 2  532  ? -26.028 -78.873  19.403  1.00 73.44  ?  532  TRP B CD2 1 
ATOM   5252  N  NE1 . TRP B 2  532  ? -26.573 -79.473  21.492  1.00 77.03  ?  532  TRP B NE1 1 
ATOM   5253  C  CE2 . TRP B 2  532  ? -27.035 -78.808  20.387  1.00 75.07  ?  532  TRP B CE2 1 
ATOM   5254  C  CE3 . TRP B 2  532  ? -26.254 -78.262  18.165  1.00 79.05  ?  532  TRP B CE3 1 
ATOM   5255  C  CZ2 . TRP B 2  532  ? -28.248 -78.159  20.172  1.00 80.44  ?  532  TRP B CZ2 1 
ATOM   5256  C  CZ3 . TRP B 2  532  ? -27.460 -77.617  17.954  1.00 75.00  ?  532  TRP B CZ3 1 
ATOM   5257  C  CH2 . TRP B 2  532  ? -28.441 -77.571  18.952  1.00 81.34  ?  532  TRP B CH2 1 
ATOM   5258  N  N   . GLN B 2  533  ? -21.773 -78.978  21.737  1.00 80.59  ?  533  GLN B N   1 
ATOM   5259  C  CA  . GLN B 2  533  ? -21.650 -78.502  23.111  1.00 76.89  ?  533  GLN B CA  1 
ATOM   5260  C  C   . GLN B 2  533  ? -20.849 -77.207  23.181  1.00 73.48  ?  533  GLN B C   1 
ATOM   5261  O  O   . GLN B 2  533  ? -21.189 -76.302  23.952  1.00 73.06  ?  533  GLN B O   1 
ATOM   5262  C  CB  . GLN B 2  533  ? -21.004 -79.577  23.985  1.00 81.06  ?  533  GLN B CB  1 
ATOM   5263  C  CG  . GLN B 2  533  ? -21.877 -80.801  24.218  1.00 86.13  ?  533  GLN B CG  1 
ATOM   5264  C  CD  . GLN B 2  533  ? -23.196 -80.456  24.884  1.00 86.49  ?  533  GLN B CD  1 
ATOM   5265  O  OE1 . GLN B 2  533  ? -23.265 -79.561  25.727  1.00 89.08  ?  533  GLN B OE1 1 
ATOM   5266  N  NE2 . GLN B 2  533  ? -24.253 -81.166  24.506  1.00 81.38  ?  533  GLN B NE2 1 
ATOM   5267  N  N   . VAL B 2  534  ? -19.778 -77.105  22.392  1.00 55.07  ?  534  VAL B N   1 
ATOM   5268  C  CA  . VAL B 2  534  ? -18.996 -75.874  22.359  1.00 50.69  ?  534  VAL B CA  1 
ATOM   5269  C  C   . VAL B 2  534  ? -19.805 -74.747  21.727  1.00 50.96  ?  534  VAL B C   1 
ATOM   5270  O  O   . VAL B 2  534  ? -19.727 -73.590  22.158  1.00 52.12  ?  534  VAL B O   1 
ATOM   5271  C  CB  . VAL B 2  534  ? -17.665 -76.111  21.619  1.00 43.06  ?  534  VAL B CB  1 
ATOM   5272  C  CG1 . VAL B 2  534  ? -16.960 -74.794  21.330  1.00 38.75  ?  534  VAL B CG1 1 
ATOM   5273  C  CG2 . VAL B 2  534  ? -16.765 -77.032  22.431  1.00 43.27  ?  534  VAL B CG2 1 
ATOM   5274  N  N   . ALA B 2  535  ? -20.609 -75.068  20.710  1.00 88.07  ?  535  ALA B N   1 
ATOM   5275  C  CA  . ALA B 2  535  ? -21.426 -74.048  20.060  1.00 94.87  ?  535  ALA B CA  1 
ATOM   5276  C  C   . ALA B 2  535  ? -22.490 -73.500  21.004  1.00 93.82  ?  535  ALA B C   1 
ATOM   5277  O  O   . ALA B 2  535  ? -22.774 -72.297  20.997  1.00 95.69  ?  535  ALA B O   1 
ATOM   5278  C  CB  . ALA B 2  535  ? -22.073 -74.617  18.799  1.00 97.28  ?  535  ALA B CB  1 
ATOM   5279  N  N   . LEU B 2  536  ? -23.094 -74.369  21.818  1.00 65.81  ?  536  LEU B N   1 
ATOM   5280  C  CA  . LEU B 2  536  ? -24.073 -73.904  22.796  1.00 61.26  ?  536  LEU B CA  1 
ATOM   5281  C  C   . LEU B 2  536  ? -23.405 -73.098  23.903  1.00 71.55  ?  536  LEU B C   1 
ATOM   5282  O  O   . LEU B 2  536  ? -23.980 -72.123  24.402  1.00 70.52  ?  536  LEU B O   1 
ATOM   5283  C  CB  . LEU B 2  536  ? -24.835 -75.091  23.384  1.00 68.73  ?  536  LEU B CB  1 
ATOM   5284  C  CG  . LEU B 2  536  ? -25.983 -75.665  22.554  1.00 74.23  ?  536  LEU B CG  1 
ATOM   5285  C  CD1 . LEU B 2  536  ? -26.832 -76.597  23.403  1.00 79.52  ?  536  LEU B CD1 1 
ATOM   5286  C  CD2 . LEU B 2  536  ? -26.830 -74.548  21.970  1.00 60.67  ?  536  LEU B CD2 1 
ATOM   5287  N  N   . ALA B 2  537  ? -22.193 -73.493  24.302  1.00 95.95  ?  537  ALA B N   1 
ATOM   5288  C  CA  . ALA B 2  537  ? -21.474 -72.771  25.347  1.00 84.64  ?  537  ALA B CA  1 
ATOM   5289  C  C   . ALA B 2  537  ? -21.179 -71.340  24.914  1.00 82.56  ?  537  ALA B C   1 
ATOM   5290  O  O   . ALA B 2  537  ? -21.593 -70.378  25.570  1.00 88.40  ?  537  ALA B O   1 
ATOM   5291  C  CB  . ALA B 2  537  ? -20.183 -73.511  25.700  1.00 89.72  ?  537  ALA B CB  1 
ATOM   5292  N  N   . ASN B 2  538  ? -20.461 -71.182  23.803  1.00 89.40  ?  538  ASN B N   1 
ATOM   5293  C  CA  . ASN B 2  538  ? -20.232 -69.863  23.228  1.00 88.92  ?  538  ASN B CA  1 
ATOM   5294  C  C   . ASN B 2  538  ? -21.470 -69.411  22.465  1.00 91.46  ?  538  ASN B C   1 
ATOM   5295  O  O   . ASN B 2  538  ? -22.558 -69.964  22.652  1.00 100.16 ?  538  ASN B O   1 
ATOM   5296  C  CB  . ASN B 2  538  ? -19.010 -69.877  22.309  1.00 85.89  ?  538  ASN B CB  1 
ATOM   5297  C  CG  . ASN B 2  538  ? -17.809 -70.547  22.947  1.00 94.87  ?  538  ASN B CG  1 
ATOM   5298  O  OD1 . ASN B 2  538  ? -17.754 -70.720  24.164  1.00 96.45  ?  538  ASN B OD1 1 
ATOM   5299  N  ND2 . ASN B 2  538  ? -16.837 -70.929  22.125  1.00 98.20  ?  538  ASN B ND2 1 
ATOM   5300  N  N   . GLY B 2  539  ? -21.317 -68.411  21.603  1.00 68.13  ?  539  GLY B N   1 
ATOM   5301  C  CA  . GLY B 2  539  ? -22.440 -67.934  20.821  1.00 76.49  ?  539  GLY B CA  1 
ATOM   5302  C  C   . GLY B 2  539  ? -22.261 -68.137  19.332  1.00 82.50  ?  539  GLY B C   1 
ATOM   5303  O  O   . GLY B 2  539  ? -23.118 -67.737  18.539  1.00 82.02  ?  539  GLY B O   1 
ATOM   5304  N  N   . VAL B 2  540  ? -21.153 -68.765  18.938  1.00 58.61  ?  540  VAL B N   1 
ATOM   5305  C  CA  . VAL B 2  540  ? -20.782 -68.911  17.538  1.00 47.29  ?  540  VAL B CA  1 
ATOM   5306  C  C   . VAL B 2  540  ? -20.444 -70.369  17.259  1.00 53.60  ?  540  VAL B C   1 
ATOM   5307  O  O   . VAL B 2  540  ? -20.267 -71.179  18.169  1.00 53.68  ?  540  VAL B O   1 
ATOM   5308  C  CB  . VAL B 2  540  ? -19.590 -68.010  17.155  1.00 41.57  ?  540  VAL B CB  1 
ATOM   5309  C  CG1 . VAL B 2  540  ? -19.943 -66.550  17.339  1.00 44.03  ?  540  VAL B CG1 1 
ATOM   5310  C  CG2 . VAL B 2  540  ? -18.365 -68.374  17.980  1.00 33.65  ?  540  VAL B CG2 1 
ATOM   5311  N  N   . ILE B 2  541  ? -20.356 -70.690  15.970  1.00 56.58  ?  541  ILE B N   1 
ATOM   5312  C  CA  . ILE B 2  541  ? -19.846 -71.971  15.490  1.00 56.68  ?  541  ILE B CA  1 
ATOM   5313  C  C   . ILE B 2  541  ? -18.575 -71.687  14.703  1.00 68.18  ?  541  ILE B C   1 
ATOM   5314  O  O   . ILE B 2  541  ? -18.611 -70.978  13.689  1.00 78.46  ?  541  ILE B O   1 
ATOM   5315  C  CB  . ILE B 2  541  ? -20.877 -72.716  14.628  1.00 60.58  ?  541  ILE B CB  1 
ATOM   5316  C  CG1 . ILE B 2  541  ? -22.034 -73.219  15.494  1.00 54.09  ?  541  ILE B CG1 1 
ATOM   5317  C  CG2 . ILE B 2  541  ? -20.214 -73.867  13.883  1.00 74.33  ?  541  ILE B CG2 1 
ATOM   5318  C  CD1 . ILE B 2  541  ? -22.983 -74.157  14.774  1.00 60.76  ?  541  ILE B CD1 1 
ATOM   5319  N  N   . ALA B 2  542  ? -17.453 -72.243  15.167  1.00 84.03  ?  542  ALA B N   1 
ATOM   5320  C  CA  . ALA B 2  542  ? -16.152 -71.879  14.616  1.00 92.14  ?  542  ALA B CA  1 
ATOM   5321  C  C   . ALA B 2  542  ? -15.908 -72.454  13.225  1.00 95.73  ?  542  ALA B C   1 
ATOM   5322  O  O   . ALA B 2  542  ? -15.021 -71.966  12.517  1.00 95.32  ?  542  ALA B O   1 
ATOM   5323  C  CB  . ALA B 2  542  ? -15.038 -72.331  15.562  1.00 81.82  ?  542  ALA B CB  1 
ATOM   5324  N  N   . GLU B 2  543  ? -16.668 -73.470  12.814  1.00 139.35 ?  543  GLU B N   1 
ATOM   5325  C  CA  . GLU B 2  543  ? -16.384 -74.122  11.540  1.00 147.31 ?  543  GLU B CA  1 
ATOM   5326  C  C   . GLU B 2  543  ? -17.013 -73.398  10.357  1.00 145.42 ?  543  GLU B C   1 
ATOM   5327  O  O   . GLU B 2  543  ? -16.483 -73.473  9.243   1.00 145.41 ?  543  GLU B O   1 
ATOM   5328  C  CB  . GLU B 2  543  ? -16.862 -75.576  11.572  1.00 156.56 ?  543  GLU B CB  1 
ATOM   5329  C  CG  . GLU B 2  543  ? -16.005 -76.495  12.429  1.00 154.29 ?  543  GLU B CG  1 
ATOM   5330  C  CD  . GLU B 2  543  ? -16.433 -76.505  13.883  1.00 155.66 ?  543  GLU B CD  1 
ATOM   5331  O  OE1 . GLU B 2  543  ? -17.459 -75.869  14.207  1.00 147.92 ?  543  GLU B OE1 1 
ATOM   5332  O  OE2 . GLU B 2  543  ? -15.743 -77.147  14.703  1.00 164.76 -1 543  GLU B OE2 1 
ATOM   5333  N  N   . THR B 2  544  ? -18.122 -72.694  10.565  1.00 122.18 ?  544  THR B N   1 
ATOM   5334  C  CA  . THR B 2  544  ? -18.882 -72.098  9.474   1.00 124.24 ?  544  THR B CA  1 
ATOM   5335  C  C   . THR B 2  544  ? -18.477 -70.641  9.289   1.00 116.78 ?  544  THR B C   1 
ATOM   5336  O  O   . THR B 2  544  ? -18.641 -69.823  10.201  1.00 113.03 ?  544  THR B O   1 
ATOM   5337  C  CB  . THR B 2  544  ? -20.384 -72.200  9.731   1.00 128.71 ?  544  THR B CB  1 
ATOM   5338  O  OG1 . THR B 2  544  ? -20.731 -73.561  10.014  1.00 132.81 ?  544  THR B OG1 1 
ATOM   5339  C  CG2 . THR B 2  544  ? -21.159 -71.728  8.508   1.00 119.69 ?  544  THR B CG2 1 
ATOM   5340  N  N   . VAL B 2  545  ? -17.954 -70.326  8.107   1.00 97.61  ?  545  VAL B N   1 
ATOM   5341  C  CA  . VAL B 2  545  ? -17.653 -68.953  7.717   1.00 96.16  ?  545  VAL B CA  1 
ATOM   5342  C  C   . VAL B 2  545  ? -17.585 -68.918  6.197   1.00 103.48 ?  545  VAL B C   1 
ATOM   5343  O  O   . VAL B 2  545  ? -17.113 -69.865  5.561   1.00 109.05 ?  545  VAL B O   1 
ATOM   5344  C  CB  . VAL B 2  545  ? -16.346 -68.447  8.376   1.00 94.37  ?  545  VAL B CB  1 
ATOM   5345  C  CG1 . VAL B 2  545  ? -15.143 -69.249  7.897   1.00 90.88  ?  545  VAL B CG1 1 
ATOM   5346  C  CG2 . VAL B 2  545  ? -16.150 -66.959  8.114   1.00 87.84  ?  545  VAL B CG2 1 
ATOM   5347  N  N   . ALA B 2  546  ? -18.085 -67.834  5.618   1.00 96.19  ?  546  ALA B N   1 
ATOM   5348  C  CA  . ALA B 2  546  ? -18.130 -67.712  4.164   1.00 91.59  ?  546  ALA B CA  1 
ATOM   5349  C  C   . ALA B 2  546  ? -16.718 -67.645  3.599   1.00 96.77  ?  546  ALA B C   1 
ATOM   5350  O  O   . ALA B 2  546  ? -15.947 -66.757  3.987   1.00 93.70  ?  546  ALA B O   1 
ATOM   5351  C  CB  . ALA B 2  546  ? -18.925 -66.478  3.758   1.00 86.06  ?  546  ALA B CB  1 
ATOM   5352  N  N   . PRO B 2  547  ? -16.335 -68.549  2.699   1.00 92.44  ?  547  PRO B N   1 
ATOM   5353  C  CA  . PRO B 2  547  ? -14.968 -68.527  2.169   1.00 99.02  ?  547  PRO B CA  1 
ATOM   5354  C  C   . PRO B 2  547  ? -14.714 -67.294  1.317   1.00 91.17  ?  547  PRO B C   1 
ATOM   5355  O  O   . PRO B 2  547  ? -15.628 -66.719  0.721   1.00 83.22  ?  547  PRO B O   1 
ATOM   5356  C  CB  . PRO B 2  547  ? -14.889 -69.809  1.327   1.00 98.00  ?  547  PRO B CB  1 
ATOM   5357  C  CG  . PRO B 2  547  ? -16.054 -70.649  1.772   1.00 87.50  ?  547  PRO B CG  1 
ATOM   5358  C  CD  . PRO B 2  547  ? -17.115 -69.681  2.176   1.00 80.40  ?  547  PRO B CD  1 
ATOM   5359  N  N   . VAL B 2  548  ? -13.448 -66.892  1.268   1.00 125.53 ?  548  VAL B N   1 
ATOM   5360  C  CA  . VAL B 2  548  ? -13.041 -65.728  0.489   1.00 126.20 ?  548  VAL B CA  1 
ATOM   5361  C  C   . VAL B 2  548  ? -12.816 -66.159  -0.955  1.00 120.59 ?  548  VAL B C   1 
ATOM   5362  O  O   . VAL B 2  548  ? -12.004 -67.049  -1.230  1.00 119.87 ?  548  VAL B O   1 
ATOM   5363  C  CB  . VAL B 2  548  ? -11.778 -65.082  1.076   1.00 136.80 ?  548  VAL B CB  1 
ATOM   5364  C  CG1 . VAL B 2  548  ? -11.514 -63.736  0.414   1.00 127.11 ?  548  VAL B CG1 1 
ATOM   5365  C  CG2 . VAL B 2  548  ? -11.915 -64.925  2.583   1.00 142.85 ?  548  VAL B CG2 1 
ATOM   5366  N  N   . ILE B 2  549  ? -13.537 -65.528  -1.880  1.00 98.38  ?  549  ILE B N   1 
ATOM   5367  C  CA  . ILE B 2  549  ? -13.430 -65.828  -3.299  1.00 100.10 ?  549  ILE B CA  1 
ATOM   5368  C  C   . ILE B 2  549  ? -13.010 -64.565  -4.039  1.00 98.11  ?  549  ILE B C   1 
ATOM   5369  O  O   . ILE B 2  549  ? -13.129 -63.446  -3.532  1.00 99.44  ?  549  ILE B O   1 
ATOM   5370  C  CB  . ILE B 2  549  ? -14.746 -66.384  -3.878  1.00 98.24  ?  549  ILE B CB  1 
ATOM   5371  C  CG1 . ILE B 2  549  ? -15.866 -65.350  -3.733  1.00 92.72  ?  549  ILE B CG1 1 
ATOM   5372  C  CG2 . ILE B 2  549  ? -15.117 -67.694  -3.200  1.00 95.55  ?  549  ILE B CG2 1 
ATOM   5373  C  CD1 . ILE B 2  549  ? -17.101 -65.670  -4.542  1.00 102.62 ?  549  ILE B CD1 1 
ATOM   5374  N  N   . GLU B 2  550  ? -12.512 -64.760  -5.260  1.00 89.78  ?  550  GLU B N   1 
ATOM   5375  C  CA  . GLU B 2  550  ? -12.054 -63.670  -6.121  1.00 92.90  ?  550  GLU B CA  1 
ATOM   5376  C  C   . GLU B 2  550  ? -12.805 -63.742  -7.444  1.00 90.92  ?  550  GLU B C   1 
ATOM   5377  O  O   . GLU B 2  550  ? -12.371 -64.433  -8.379  1.00 90.76  ?  550  GLU B O   1 
ATOM   5378  C  CB  . GLU B 2  550  ? -10.545 -63.738  -6.340  1.00 103.38 ?  550  GLU B CB  1 
ATOM   5379  C  CG  . GLU B 2  550  ? -9.725  -63.347  -5.121  1.00 110.77 ?  550  GLU B CG  1 
ATOM   5380  C  CD  . GLU B 2  550  ? -8.271  -63.083  -5.456  1.00 119.22 ?  550  GLU B CD  1 
ATOM   5381  O  OE1 . GLU B 2  550  ? -7.915  -63.138  -6.653  1.00 123.35 ?  550  GLU B OE1 1 
ATOM   5382  O  OE2 . GLU B 2  550  ? -7.483  -62.817  -4.524  1.00 118.57 -1 550  GLU B OE2 1 
ATOM   5383  N  N   . PRO B 2  551  ? -13.931 -63.051  -7.567  1.00 112.35 ?  551  PRO B N   1 
ATOM   5384  C  CA  . PRO B 2  551  ? -14.671 -63.049  -8.831  1.00 113.65 ?  551  PRO B CA  1 
ATOM   5385  C  C   . PRO B 2  551  ? -14.026 -62.115  -9.847  1.00 121.94 ?  551  PRO B C   1 
ATOM   5386  O  O   . PRO B 2  551  ? -13.170 -61.291  -9.528  1.00 120.39 ?  551  PRO B O   1 
ATOM   5387  C  CB  . PRO B 2  551  ? -16.059 -62.551  -8.423  1.00 113.61 ?  551  PRO B CB  1 
ATOM   5388  C  CG  . PRO B 2  551  ? -15.797 -61.671  -7.246  1.00 112.28 ?  551  PRO B CG  1 
ATOM   5389  C  CD  . PRO B 2  551  ? -14.602 -62.249  -6.528  1.00 116.43 ?  551  PRO B CD  1 
ATOM   5390  N  N   . THR B 2  552  ? -14.462 -62.260  -11.093 1.00 104.49 ?  552  THR B N   1 
ATOM   5391  C  CA  . THR B 2  552  ? -13.982 -61.430  -12.185 1.00 96.31  ?  552  THR B CA  1 
ATOM   5392  C  C   . THR B 2  552  ? -15.032 -60.391  -12.558 1.00 95.51  ?  552  THR B C   1 
ATOM   5393  O  O   . THR B 2  552  ? -16.237 -60.640  -12.472 1.00 95.05  ?  552  THR B O   1 
ATOM   5394  C  CB  . THR B 2  552  ? -13.626 -62.283  -13.405 1.00 93.33  ?  552  THR B CB  1 
ATOM   5395  O  OG1 . THR B 2  552  ? -13.123 -61.439  -14.450 1.00 114.63 ?  552  THR B OG1 1 
ATOM   5396  C  CG2 . THR B 2  552  ? -14.841 -63.052  -13.902 1.00 88.39  ?  552  THR B CG2 1 
ATOM   5397  N  N   . LEU B 2  553  ? -14.560 -59.216  -12.966 1.00 75.90  ?  553  LEU B N   1 
ATOM   5398  C  CA  . LEU B 2  553  ? -15.427 -58.093  -13.292 1.00 69.29  ?  553  LEU B CA  1 
ATOM   5399  C  C   . LEU B 2  553  ? -15.679 -58.033  -14.793 1.00 68.47  ?  553  LEU B C   1 
ATOM   5400  O  O   . LEU B 2  553  ? -14.753 -58.181  -15.596 1.00 70.23  ?  553  LEU B O   1 
ATOM   5401  C  CB  . LEU B 2  553  ? -14.815 -56.776  -12.811 1.00 70.06  ?  553  LEU B CB  1 
ATOM   5402  C  CG  . LEU B 2  553  ? -15.779 -55.597  -12.660 1.00 68.70  ?  553  LEU B CG  1 
ATOM   5403  C  CD1 . LEU B 2  553  ? -16.928 -55.959  -11.734 1.00 59.50  ?  553  LEU B CD1 1 
ATOM   5404  C  CD2 . LEU B 2  553  ? -15.045 -54.370  -12.148 1.00 63.36  ?  553  LEU B CD2 1 
ATOM   5405  N  N   . ASN B 2  554  ? -16.939 -57.811  -15.164 1.00 70.40  ?  554  ASN B N   1 
ATOM   5406  C  CA  . ASN B 2  554  ? -17.355 -57.734  -16.560 1.00 75.55  ?  554  ASN B CA  1 
ATOM   5407  C  C   . ASN B 2  554  ? -17.550 -56.269  -16.930 1.00 80.98  ?  554  ASN B C   1 
ATOM   5408  O  O   . ASN B 2  554  ? -18.537 -55.646  -16.529 1.00 86.81  ?  554  ASN B O   1 
ATOM   5409  C  CB  . ASN B 2  554  ? -18.637 -58.531  -16.792 1.00 82.64  ?  554  ASN B CB  1 
ATOM   5410  C  CG  . ASN B 2  554  ? -18.907 -58.781  -18.261 1.00 99.80  ?  554  ASN B CG  1 
ATOM   5411  O  OD1 . ASN B 2  554  ? -18.068 -58.498  -19.117 1.00 106.33 ?  554  ASN B OD1 1 
ATOM   5412  N  ND2 . ASN B 2  554  ? -20.084 -59.316  -18.562 1.00 108.13 ?  554  ASN B ND2 1 
ATOM   5413  N  N   . GLU B 2  555  ? -16.612 -55.724  -17.706 1.00 101.57 ?  555  GLU B N   1 
ATOM   5414  C  CA  . GLU B 2  555  ? -16.672 -54.306  -18.045 1.00 102.26 ?  555  GLU B CA  1 
ATOM   5415  C  C   . GLU B 2  555  ? -17.777 -54.017  -19.053 1.00 115.30 ?  555  GLU B C   1 
ATOM   5416  O  O   . GLU B 2  555  ? -18.456 -52.990  -18.955 1.00 117.16 ?  555  GLU B O   1 
ATOM   5417  C  CB  . GLU B 2  555  ? -15.322 -53.840  -18.591 1.00 111.77 ?  555  GLU B CB  1 
ATOM   5418  C  CG  . GLU B 2  555  ? -14.104 -54.434  -17.889 1.00 112.49 ?  555  GLU B CG  1 
ATOM   5419  C  CD  . GLU B 2  555  ? -14.183 -54.345  -16.372 1.00 114.03 ?  555  GLU B CD  1 
ATOM   5420  O  OE1 . GLU B 2  555  ? -14.608 -53.290  -15.849 1.00 113.39 ?  555  GLU B OE1 1 
ATOM   5421  O  OE2 . GLU B 2  555  ? -13.820 -55.334  -15.699 1.00 119.21 -1 555  GLU B OE2 1 
ATOM   5422  N  N   . GLY B 2  556  ? -17.964 -54.902  -20.035 1.00 142.10 ?  556  GLY B N   1 
ATOM   5423  C  CA  . GLY B 2  556  ? -18.892 -54.608  -21.116 1.00 144.33 ?  556  GLY B CA  1 
ATOM   5424  C  C   . GLY B 2  556  ? -20.333 -54.549  -20.650 1.00 140.05 ?  556  GLY B C   1 
ATOM   5425  O  O   . GLY B 2  556  ? -21.130 -53.758  -21.160 1.00 139.36 ?  556  GLY B O   1 
ATOM   5426  N  N   . ALA B 2  557  ? -20.686 -55.384  -19.671 1.00 88.04  ?  557  ALA B N   1 
ATOM   5427  C  CA  . ALA B 2  557  ? -22.061 -55.423  -19.190 1.00 84.42  ?  557  ALA B CA  1 
ATOM   5428  C  C   . ALA B 2  557  ? -22.396 -54.185  -18.367 1.00 83.42  ?  557  ALA B C   1 
ATOM   5429  O  O   . ALA B 2  557  ? -23.460 -53.581  -18.547 1.00 77.67  ?  557  ALA B O   1 
ATOM   5430  C  CB  . ALA B 2  557  ? -22.286 -56.698  -18.379 1.00 73.68  ?  557  ALA B CB  1 
ATOM   5431  N  N   . ILE B 2  558  ? -21.496 -53.785  -17.466 1.00 134.96 ?  558  ILE B N   1 
ATOM   5432  C  CA  . ILE B 2  558  ? -21.746 -52.615  -16.633 1.00 134.65 ?  558  ILE B CA  1 
ATOM   5433  C  C   . ILE B 2  558  ? -21.576 -51.315  -17.408 1.00 133.62 ?  558  ILE B C   1 
ATOM   5434  O  O   . ILE B 2  558  ? -22.082 -50.272  -16.977 1.00 130.00 ?  558  ILE B O   1 
ATOM   5435  C  CB  . ILE B 2  558  ? -20.828 -52.639  -15.398 1.00 127.81 ?  558  ILE B CB  1 
ATOM   5436  C  CG1 . ILE B 2  558  ? -19.361 -52.532  -15.819 1.00 126.94 ?  558  ILE B CG1 1 
ATOM   5437  C  CG2 . ILE B 2  558  ? -21.053 -53.910  -14.597 1.00 117.87 ?  558  ILE B CG2 1 
ATOM   5438  C  CD1 . ILE B 2  558  ? -18.388 -52.703  -14.674 1.00 126.23 ?  558  ILE B CD1 1 
ATOM   5439  N  N   . ARG B 2  559  ? -20.881 -51.347  -18.547 1.00 111.55 ?  559  ARG B N   1 
ATOM   5440  C  CA  . ARG B 2  559  ? -20.721 -50.144  -19.356 1.00 111.85 ?  559  ARG B CA  1 
ATOM   5441  C  C   . ARG B 2  559  ? -21.928 -49.914  -20.257 1.00 108.66 ?  559  ARG B C   1 
ATOM   5442  O  O   . ARG B 2  559  ? -22.312 -48.765  -20.504 1.00 110.87 ?  559  ARG B O   1 
ATOM   5443  C  CB  . ARG B 2  559  ? -19.443 -50.238  -20.191 1.00 116.77 ?  559  ARG B CB  1 
ATOM   5444  C  CG  . ARG B 2  559  ? -19.079 -48.962  -20.930 1.00 118.18 ?  559  ARG B CG  1 
ATOM   5445  C  CD  . ARG B 2  559  ? -17.710 -49.078  -21.581 1.00 128.57 ?  559  ARG B CD  1 
ATOM   5446  N  NE  . ARG B 2  559  ? -17.498 -50.398  -22.165 1.00 140.46 ?  559  ARG B NE  1 
ATOM   5447  C  CZ  . ARG B 2  559  ? -16.309 -50.955  -22.350 1.00 140.62 ?  559  ARG B CZ  1 
ATOM   5448  N  NH1 . ARG B 2  559  ? -15.193 -50.335  -22.004 1.00 157.79 ?  559  ARG B NH1 1 
ATOM   5449  N  NH2 . ARG B 2  559  ? -16.239 -52.166  -22.897 1.00 118.69 ?  559  ARG B NH2 1 
ATOM   5450  N  N   . ALA B 2  560  ? -22.538 -50.991  -20.753 1.00 93.94  ?  560  ALA B N   1 
ATOM   5451  C  CA  . ALA B 2  560  ? -23.710 -50.898  -21.622 1.00 100.31 ?  560  ALA B CA  1 
ATOM   5452  C  C   . ALA B 2  560  ? -24.961 -51.050  -20.760 1.00 106.70 ?  560  ALA B C   1 
ATOM   5453  O  O   . ALA B 2  560  ? -25.604 -52.099  -20.718 1.00 112.33 ?  560  ALA B O   1 
ATOM   5454  C  CB  . ALA B 2  560  ? -23.647 -51.947  -22.727 1.00 107.61 ?  560  ALA B CB  1 
ATOM   5455  N  N   . THR B 2  561  ? -25.304 -49.968  -20.061 1.00 138.05 ?  561  THR B N   1 
ATOM   5456  C  CA  . THR B 2  561  ? -26.462 -49.916  -19.183 1.00 128.76 ?  561  THR B CA  1 
ATOM   5457  C  C   . THR B 2  561  ? -27.131 -48.560  -19.360 1.00 127.80 ?  561  THR B C   1 
ATOM   5458  O  O   . THR B 2  561  ? -26.437 -47.535  -19.436 1.00 128.86 ?  561  THR B O   1 
ATOM   5459  C  CB  . THR B 2  561  ? -26.073 -50.121  -17.712 1.00 115.64 ?  561  THR B CB  1 
ATOM   5460  O  OG1 . THR B 2  561  ? -25.119 -51.186  -17.615 1.00 109.00 ?  561  THR B OG1 1 
ATOM   5461  C  CG2 . THR B 2  561  ? -27.291 -50.472  -16.874 1.00 113.01 ?  561  THR B CG2 1 
ATOM   5462  N  N   . PRO B 2  562  ? -28.466 -48.524  -19.448 1.00 128.84 ?  562  PRO B N   1 
ATOM   5463  C  CA  . PRO B 2  562  ? -29.153 -47.238  -19.673 1.00 133.19 ?  562  PRO B CA  1 
ATOM   5464  C  C   . PRO B 2  562  ? -28.803 -46.150  -18.670 1.00 129.28 ?  562  PRO B C   1 
ATOM   5465  O  O   . PRO B 2  562  ? -28.663 -44.986  -19.067 1.00 130.32 ?  562  PRO B O   1 
ATOM   5466  C  CB  . PRO B 2  562  ? -30.633 -47.628  -19.590 1.00 135.97 ?  562  PRO B CB  1 
ATOM   5467  C  CG  . PRO B 2  562  ? -30.667 -49.038  -20.063 1.00 134.32 ?  562  PRO B CG  1 
ATOM   5468  C  CD  . PRO B 2  562  ? -29.380 -49.671  -19.592 1.00 119.80 ?  562  PRO B CD  1 
ATOM   5469  N  N   . ILE B 2  563  ? -28.653 -46.495  -17.393 1.00 99.56  ?  563  ILE B N   1 
ATOM   5470  C  CA  . ILE B 2  563  ? -28.392 -45.536  -16.318 1.00 91.15  ?  563  ILE B CA  1 
ATOM   5471  C  C   . ILE B 2  563  ? -29.508 -44.497  -16.302 1.00 90.33  ?  563  ILE B C   1 
ATOM   5472  O  O   . ILE B 2  563  ? -29.387 -43.447  -16.949 1.00 91.05  ?  563  ILE B O   1 
ATOM   5473  C  CB  . ILE B 2  563  ? -27.011 -44.875  -16.469 1.00 92.26  ?  563  ILE B CB  1 
ATOM   5474  C  CG1 . ILE B 2  563  ? -25.928 -45.937  -16.670 1.00 96.90  ?  563  ILE B CG1 1 
ATOM   5475  C  CG2 . ILE B 2  563  ? -26.690 -44.019  -15.254 1.00 83.67  ?  563  ILE B CG2 1 
ATOM   5476  C  CD1 . ILE B 2  563  ? -24.590 -45.371  -17.093 1.00 103.11 ?  563  ILE B CD1 1 
ATOM   5477  N  N   . PRO B 2  564  ? -30.599 -44.736  -15.576 1.00 93.28  ?  564  PRO B N   1 
ATOM   5478  C  CA  . PRO B 2  564  ? -31.751 -43.832  -15.658 1.00 93.82  ?  564  PRO B CA  1 
ATOM   5479  C  C   . PRO B 2  564  ? -31.457 -42.468  -15.054 1.00 91.75  ?  564  PRO B C   1 
ATOM   5480  O  O   . PRO B 2  564  ? -30.668 -42.329  -14.117 1.00 90.52  ?  564  PRO B O   1 
ATOM   5481  C  CB  . PRO B 2  564  ? -32.835 -44.569  -14.862 1.00 92.04  ?  564  PRO B CB  1 
ATOM   5482  C  CG  . PRO B 2  564  ? -32.074 -45.430  -13.908 1.00 85.55  ?  564  PRO B CG  1 
ATOM   5483  C  CD  . PRO B 2  564  ? -30.821 -45.842  -14.629 1.00 85.11  ?  564  PRO B CD  1 
ATOM   5484  N  N   . GLN B 2  565  ? -32.123 -41.440  -15.617 1.00 97.87  ?  565  GLN B N   1 
ATOM   5485  C  CA  . GLN B 2  565  ? -32.025 -40.038  -15.244 1.00 103.95 ?  565  GLN B CA  1 
ATOM   5486  C  C   . GLN B 2  565  ? -33.254 -39.600  -14.453 1.00 101.95 ?  565  GLN B C   1 
ATOM   5487  O  O   . GLN B 2  565  ? -34.340 -40.166  -14.613 1.00 104.78 ?  565  GLN B O   1 
ATOM   5488  C  CB  . GLN B 2  565  ? -31.883 -39.157  -16.490 1.00 100.47 ?  565  GLN B CB  1 
ATOM   5489  C  CG  . GLN B 2  565  ? -31.137 -39.815  -17.639 1.00 92.65  ?  565  GLN B CG  1 
ATOM   5490  C  CD  . GLN B 2  565  ? -29.653 -39.963  -17.358 1.00 91.20  ?  565  GLN B CD  1 
ATOM   5491  O  OE1 . GLN B 2  565  ? -28.951 -38.977  -17.133 1.00 83.41  ?  565  GLN B OE1 1 
ATOM   5492  N  NE2 . GLN B 2  565  ? -29.168 -41.199  -17.370 1.00 100.84 ?  565  GLN B NE2 1 
ATOM   5493  N  N   . PRO B 2  566  ? -33.113 -38.596  -13.590 1.00 82.75  ?  566  PRO B N   1 
ATOM   5494  C  CA  . PRO B 2  566  ? -34.264 -38.114  -12.819 1.00 86.80  ?  566  PRO B CA  1 
ATOM   5495  C  C   . PRO B 2  566  ? -35.236 -37.342  -13.698 1.00 94.35  ?  566  PRO B C   1 
ATOM   5496  O  O   . PRO B 2  566  ? -34.966 -37.025  -14.857 1.00 110.30 ?  566  PRO B O   1 
ATOM   5497  C  CB  . PRO B 2  566  ? -33.630 -37.206  -11.763 1.00 84.08  ?  566  PRO B CB  1 
ATOM   5498  C  CG  . PRO B 2  566  ? -32.362 -36.738  -12.396 1.00 78.50  ?  566  PRO B CG  1 
ATOM   5499  C  CD  . PRO B 2  566  ? -31.871 -37.892  -13.225 1.00 72.84  ?  566  PRO B CD  1 
ATOM   5500  N  N   . GLY B 2  567  ? -36.386 -37.035  -13.120 1.00 147.52 ?  567  GLY B N   1 
ATOM   5501  C  CA  . GLY B 2  567  ? -37.403 -36.269  -13.807 1.00 156.37 ?  567  GLY B CA  1 
ATOM   5502  C  C   . GLY B 2  567  ? -38.782 -36.635  -13.295 1.00 163.58 ?  567  GLY B C   1 
ATOM   5503  O  O   . GLY B 2  567  ? -38.926 -37.195  -12.212 1.00 170.80 ?  567  GLY B O   1 
ATOM   5504  N  N   . ASP B 2  568  ? -39.785 -36.290  -14.103 1.00 161.39 ?  568  ASP B N   1 
ATOM   5505  C  CA  . ASP B 2  568  ? -41.206 -36.549  -13.881 1.00 158.84 ?  568  ASP B CA  1 
ATOM   5506  C  C   . ASP B 2  568  ? -41.792 -35.760  -12.715 1.00 155.99 ?  568  ASP B C   1 
ATOM   5507  O  O   . ASP B 2  568  ? -42.984 -35.916  -12.422 1.00 158.21 ?  568  ASP B O   1 
ATOM   5508  C  CB  . ASP B 2  568  ? -41.504 -38.042  -13.671 1.00 158.84 ?  568  ASP B CB  1 
ATOM   5509  C  CG  . ASP B 2  568  ? -41.197 -38.876  -14.900 1.00 162.77 ?  568  ASP B CG  1 
ATOM   5510  O  OD1 . ASP B 2  568  ? -41.076 -38.294  -15.999 1.00 168.24 ?  568  ASP B OD1 1 
ATOM   5511  O  OD2 . ASP B 2  568  ? -41.080 -40.113  -14.769 1.00 150.20 -1 568  ASP B OD2 1 
ATOM   5512  N  N   . GLY B 2  569  ? -41.009 -34.920  -12.040 1.00 110.78 ?  569  GLY B N   1 
ATOM   5513  C  CA  . GLY B 2  569  ? -41.550 -34.060  -11.005 1.00 108.63 ?  569  GLY B CA  1 
ATOM   5514  C  C   . GLY B 2  569  ? -41.281 -34.511  -9.584  1.00 109.66 ?  569  GLY B C   1 
ATOM   5515  O  O   . GLY B 2  569  ? -40.211 -35.052  -9.285  1.00 110.00 ?  569  GLY B O   1 
ATOM   5516  N  N   . VAL B 2  570  ? -42.252 -34.289  -8.697  1.00 99.07  ?  570  VAL B N   1 
ATOM   5517  C  CA  . VAL B 2  570  ? -42.081 -34.606  -7.283  1.00 95.19  ?  570  VAL B CA  1 
ATOM   5518  C  C   . VAL B 2  570  ? -42.016 -36.115  -7.100  1.00 91.55  ?  570  VAL B C   1 
ATOM   5519  O  O   . VAL B 2  570  ? -42.872 -36.857  -7.598  1.00 89.92  ?  570  VAL B O   1 
ATOM   5520  C  CB  . VAL B 2  570  ? -43.221 -33.996  -6.454  1.00 95.09  ?  570  VAL B CB  1 
ATOM   5521  C  CG1 . VAL B 2  570  ? -42.910 -34.098  -4.971  1.00 83.10  ?  570  VAL B CG1 1 
ATOM   5522  C  CG2 . VAL B 2  570  ? -43.455 -32.548  -6.859  1.00 103.75 ?  570  VAL B CG2 1 
ATOM   5523  N  N   . GLU B 2  571  ? -41.005 -36.575  -6.371  1.00 111.55 ?  571  GLU B N   1 
ATOM   5524  C  CA  . GLU B 2  571  ? -40.763 -37.994  -6.166  1.00 103.06 ?  571  GLU B CA  1 
ATOM   5525  C  C   . GLU B 2  571  ? -41.155 -38.408  -4.753  1.00 101.79 ?  571  GLU B C   1 
ATOM   5526  O  O   . GLU B 2  571  ? -41.218 -37.591  -3.831  1.00 99.85  ?  571  GLU B O   1 
ATOM   5527  C  CB  . GLU B 2  571  ? -39.291 -38.339  -6.417  1.00 102.11 ?  571  GLU B CB  1 
ATOM   5528  C  CG  . GLU B 2  571  ? -38.339 -37.761  -5.384  1.00 95.50  ?  571  GLU B CG  1 
ATOM   5529  C  CD  . GLU B 2  571  ? -36.891 -38.114  -5.661  1.00 108.02 ?  571  GLU B CD  1 
ATOM   5530  O  OE1 . GLU B 2  571  ? -36.627 -38.781  -6.682  1.00 115.38 ?  571  GLU B OE1 1 
ATOM   5531  O  OE2 . GLU B 2  571  ? -36.018 -37.726  -4.857  1.00 102.87 -1 571  GLU B OE2 1 
ATOM   5532  N  N   . ILE B 2  572  ? -41.421 -39.703  -4.601  1.00 71.92  ?  572  ILE B N   1 
ATOM   5533  C  CA  . ILE B 2  572  ? -41.732 -40.313  -3.315  1.00 60.35  ?  572  ILE B CA  1 
ATOM   5534  C  C   . ILE B 2  572  ? -40.634 -41.314  -2.986  1.00 60.94  ?  572  ILE B C   1 
ATOM   5535  O  O   . ILE B 2  572  ? -40.304 -42.173  -3.811  1.00 68.52  ?  572  ILE B O   1 
ATOM   5536  C  CB  . ILE B 2  572  ? -43.113 -40.997  -3.327  1.00 60.69  ?  572  ILE B CB  1 
ATOM   5537  C  CG1 . ILE B 2  572  ? -44.192 -40.017  -3.794  1.00 59.96  ?  572  ILE B CG1 1 
ATOM   5538  C  CG2 . ILE B 2  572  ? -43.442 -41.564  -1.954  1.00 63.81  ?  572  ILE B CG2 1 
ATOM   5539  C  CD1 . ILE B 2  572  ? -44.528 -38.948  -2.776  1.00 53.37  ?  572  ILE B CD1 1 
ATOM   5540  N  N   . VAL B 2  573  ? -40.070 -41.200  -1.788  1.00 68.44  ?  573  VAL B N   1 
ATOM   5541  C  CA  . VAL B 2  573  ? -39.005 -42.082  -1.328  1.00 68.81  ?  573  VAL B CA  1 
ATOM   5542  C  C   . VAL B 2  573  ? -39.554 -42.934  -0.193  1.00 67.40  ?  573  VAL B C   1 
ATOM   5543  O  O   . VAL B 2  573  ? -39.909 -42.412  0.871   1.00 67.93  ?  573  VAL B O   1 
ATOM   5544  C  CB  . VAL B 2  573  ? -37.767 -41.293  -0.880  1.00 62.69  ?  573  VAL B CB  1 
ATOM   5545  C  CG1 . VAL B 2  573  ? -36.614 -42.242  -0.595  1.00 65.03  ?  573  VAL B CG1 1 
ATOM   5546  C  CG2 . VAL B 2  573  ? -37.376 -40.285  -1.947  1.00 52.96  ?  573  VAL B CG2 1 
ATOM   5547  N  N   . PHE B 2  574  ? -39.627 -44.242  -0.420  1.00 76.36  ?  574  PHE B N   1 
ATOM   5548  C  CA  . PHE B 2  574  ? -40.126 -45.177  0.581   1.00 77.26  ?  574  PHE B CA  1 
ATOM   5549  C  C   . PHE B 2  574  ? -38.968 -45.646  1.454   1.00 79.46  ?  574  PHE B C   1 
ATOM   5550  O  O   . PHE B 2  574  ? -38.048 -46.310  0.967   1.00 79.06  ?  574  PHE B O   1 
ATOM   5551  C  CB  . PHE B 2  574  ? -40.815 -46.366  -0.087  1.00 76.24  ?  574  PHE B CB  1 
ATOM   5552  C  CG  . PHE B 2  574  ? -41.989 -45.983  -0.938  1.00 82.28  ?  574  PHE B CG  1 
ATOM   5553  C  CD1 . PHE B 2  574  ? -41.811 -45.608  -2.260  1.00 82.04  ?  574  PHE B CD1 1 
ATOM   5554  C  CD2 . PHE B 2  574  ? -43.271 -45.998  -0.418  1.00 76.13  ?  574  PHE B CD2 1 
ATOM   5555  C  CE1 . PHE B 2  574  ? -42.891 -45.254  -3.046  1.00 81.12  ?  574  PHE B CE1 1 
ATOM   5556  C  CE2 . PHE B 2  574  ? -44.356 -45.646  -1.201  1.00 79.04  ?  574  PHE B CE2 1 
ATOM   5557  C  CZ  . PHE B 2  574  ? -44.165 -45.273  -2.516  1.00 85.52  ?  574  PHE B CZ  1 
ATOM   5558  N  N   . ARG B 2  575  ? -39.015 -45.303  2.741   1.00 81.36  ?  575  ARG B N   1 
ATOM   5559  C  CA  . ARG B 2  575  ? -37.950 -45.662  3.657   1.00 76.50  ?  575  ARG B CA  1 
ATOM   5560  C  C   . ARG B 2  575  ? -38.511 -46.456  4.827   1.00 73.01  ?  575  ARG B C   1 
ATOM   5561  O  O   . ARG B 2  575  ? -39.641 -46.204  5.256   1.00 74.24  ?  575  ARG B O   1 
ATOM   5562  C  CB  . ARG B 2  575  ? -37.232 -44.413  4.197   1.00 68.87  ?  575  ARG B CB  1 
ATOM   5563  C  CG  . ARG B 2  575  ? -36.447 -43.648  3.150   1.00 72.91  ?  575  ARG B CG  1 
ATOM   5564  C  CD  . ARG B 2  575  ? -35.413 -44.516  2.456   1.00 85.66  ?  575  ARG B CD  1 
ATOM   5565  N  NE  . ARG B 2  575  ? -34.367 -44.969  3.365   1.00 75.43  ?  575  ARG B NE  1 
ATOM   5566  C  CZ  . ARG B 2  575  ? -33.803 -46.168  3.316   1.00 79.37  ?  575  ARG B CZ  1 
ATOM   5567  N  NH1 . ARG B 2  575  ? -34.172 -47.069  2.420   1.00 77.09  ?  575  ARG B NH1 1 
ATOM   5568  N  NH2 . ARG B 2  575  ? -32.847 -46.472  4.189   1.00 84.89  ?  575  ARG B NH2 1 
ATOM   5569  N  N   . PRO B 2  576  ? -37.764 -47.424  5.353   1.00 57.96  ?  576  PRO B N   1 
ATOM   5570  C  CA  . PRO B 2  576  ? -38.226 -48.131  6.553   1.00 61.91  ?  576  PRO B CA  1 
ATOM   5571  C  C   . PRO B 2  576  ? -38.259 -47.198  7.755   1.00 66.04  ?  576  PRO B C   1 
ATOM   5572  O  O   . PRO B 2  576  ? -37.386 -46.343  7.924   1.00 63.40  ?  576  PRO B O   1 
ATOM   5573  C  CB  . PRO B 2  576  ? -37.187 -49.246  6.735   1.00 56.08  ?  576  PRO B CB  1 
ATOM   5574  C  CG  . PRO B 2  576  ? -35.989 -48.785  5.977   1.00 61.25  ?  576  PRO B CG  1 
ATOM   5575  C  CD  . PRO B 2  576  ? -36.517 -47.996  4.818   1.00 53.69  ?  576  PRO B CD  1 
ATOM   5576  N  N   . ASP B 2  577  ? -39.284 -47.361  8.584   1.00 75.82  ?  577  ASP B N   1 
ATOM   5577  C  CA  . ASP B 2  577  ? -39.393 -46.549  9.787   1.00 69.58  ?  577  ASP B CA  1 
ATOM   5578  C  C   . ASP B 2  577  ? -38.247 -46.882  10.740  1.00 69.46  ?  577  ASP B C   1 
ATOM   5579  O  O   . ASP B 2  577  ? -37.898 -48.058  10.903  1.00 71.03  ?  577  ASP B O   1 
ATOM   5580  C  CB  . ASP B 2  577  ? -40.738 -46.782  10.475  1.00 65.07  ?  577  ASP B CB  1 
ATOM   5581  C  CG  . ASP B 2  577  ? -41.048 -45.731  11.520  1.00 67.43  ?  577  ASP B CG  1 
ATOM   5582  O  OD1 . ASP B 2  577  ? -41.069 -44.533  11.173  1.00 64.89  ?  577  ASP B OD1 1 
ATOM   5583  O  OD2 . ASP B 2  577  ? -41.282 -46.104  12.687  1.00 73.75  -1 577  ASP B OD2 1 
ATOM   5584  N  N   . PRO B 2  578  ? -37.630 -45.877  11.369  1.00 59.04  ?  578  PRO B N   1 
ATOM   5585  C  CA  . PRO B 2  578  ? -36.475 -46.159  12.236  1.00 60.30  ?  578  PRO B CA  1 
ATOM   5586  C  C   . PRO B 2  578  ? -36.791 -47.086  13.395  1.00 59.42  ?  578  PRO B C   1 
ATOM   5587  O  O   . PRO B 2  578  ? -35.912 -47.847  13.822  1.00 60.34  ?  578  PRO B O   1 
ATOM   5588  C  CB  . PRO B 2  578  ? -36.068 -44.763  12.727  1.00 57.22  ?  578  PRO B CB  1 
ATOM   5589  C  CG  . PRO B 2  578  ? -36.509 -43.853  11.632  1.00 62.16  ?  578  PRO B CG  1 
ATOM   5590  C  CD  . PRO B 2  578  ? -37.828 -44.429  11.181  1.00 65.32  ?  578  PRO B CD  1 
ATOM   5591  N  N   . SER B 2  579  ? -38.021 -47.056  13.914  1.00 64.44  ?  579  SER B N   1 
ATOM   5592  C  CA  . SER B 2  579  ? -38.386 -47.845  15.081  1.00 64.51  ?  579  SER B CA  1 
ATOM   5593  C  C   . SER B 2  579  ? -39.306 -49.019  14.776  1.00 70.90  ?  579  SER B C   1 
ATOM   5594  O  O   . SER B 2  579  ? -39.359 -49.958  15.576  1.00 72.50  ?  579  SER B O   1 
ATOM   5595  C  CB  . SER B 2  579  ? -39.056 -46.953  16.138  1.00 58.26  ?  579  SER B CB  1 
ATOM   5596  O  OG  . SER B 2  579  ? -40.171 -46.259  15.603  1.00 64.72  ?  579  SER B OG  1 
ATOM   5597  N  N   . LEU B 2  580  ? -40.020 -49.001  13.649  1.00 60.89  ?  580  LEU B N   1 
ATOM   5598  C  CA  . LEU B 2  580  ? -40.995 -50.041  13.345  1.00 56.78  ?  580  LEU B CA  1 
ATOM   5599  C  C   . LEU B 2  580  ? -40.558 -51.001  12.246  1.00 63.60  ?  580  LEU B C   1 
ATOM   5600  O  O   . LEU B 2  580  ? -41.182 -52.057  12.093  1.00 69.63  ?  580  LEU B O   1 
ATOM   5601  C  CB  . LEU B 2  580  ? -42.342 -49.408  12.961  1.00 54.46  ?  580  LEU B CB  1 
ATOM   5602  C  CG  . LEU B 2  580  ? -43.427 -49.454  14.040  1.00 58.65  ?  580  LEU B CG  1 
ATOM   5603  C  CD1 . LEU B 2  580  ? -42.903 -48.895  15.354  1.00 59.61  ?  580  LEU B CD1 1 
ATOM   5604  C  CD2 . LEU B 2  580  ? -44.660 -48.690  13.589  1.00 65.30  ?  580  LEU B CD2 1 
ATOM   5605  N  N   . PHE B 2  581  ? -39.509 -50.673  11.489  1.00 62.65  ?  581  PHE B N   1 
ATOM   5606  C  CA  . PHE B 2  581  ? -38.985 -51.522  10.413  1.00 61.83  ?  581  PHE B CA  1 
ATOM   5607  C  C   . PHE B 2  581  ? -40.103 -51.794  9.412   1.00 67.58  ?  581  PHE B C   1 
ATOM   5608  O  O   . PHE B 2  581  ? -40.684 -50.828  8.885   1.00 69.57  ?  581  PHE B O   1 
ATOM   5609  C  CB  . PHE B 2  581  ? -38.333 -52.765  11.025  1.00 61.06  ?  581  PHE B CB  1 
ATOM   5610  C  CG  . PHE B 2  581  ? -37.299 -53.401  10.137  1.00 66.29  ?  581  PHE B CG  1 
ATOM   5611  C  CD1 . PHE B 2  581  ? -36.210 -52.675  9.678   1.00 61.31  ?  581  PHE B CD1 1 
ATOM   5612  C  CD2 . PHE B 2  581  ? -37.430 -54.722  9.744   1.00 65.39  ?  581  PHE B CD2 1 
ATOM   5613  C  CE1 . PHE B 2  581  ? -35.263 -53.268  8.852   1.00 58.64  ?  581  PHE B CE1 1 
ATOM   5614  C  CE2 . PHE B 2  581  ? -36.493 -55.316  8.922   1.00 59.69  ?  581  PHE B CE2 1 
ATOM   5615  C  CZ  . PHE B 2  581  ? -35.409 -54.591  8.475   1.00 55.12  ?  581  PHE B CZ  1 
ATOM   5616  N  N   . ASP B 2  582  ? -40.424 -53.049  9.105   1.00 83.13  ?  582  ASP B N   1 
ATOM   5617  C  CA  . ASP B 2  582  ? -41.448 -53.401  8.131   1.00 77.63  ?  582  ASP B CA  1 
ATOM   5618  C  C   . ASP B 2  582  ? -42.855 -53.380  8.712   1.00 80.45  ?  582  ASP B C   1 
ATOM   5619  O  O   . ASP B 2  582  ? -43.798 -53.769  8.017   1.00 82.29  ?  582  ASP B O   1 
ATOM   5620  C  CB  . ASP B 2  582  ? -41.156 -54.788  7.552   1.00 77.30  ?  582  ASP B CB  1 
ATOM   5621  C  CG  . ASP B 2  582  ? -41.124 -55.868  8.620   1.00 92.96  ?  582  ASP B CG  1 
ATOM   5622  O  OD1 . ASP B 2  582  ? -40.618 -55.593  9.729   1.00 98.56  ?  582  ASP B OD1 1 
ATOM   5623  O  OD2 . ASP B 2  582  ? -41.608 -56.989  8.355   1.00 97.45  -1 582  ASP B OD2 1 
ATOM   5624  N  N   . GLY B 2  583  ? -43.019 -52.944  9.960   1.00 70.30  ?  583  GLY B N   1 
ATOM   5625  C  CA  . GLY B 2  583  ? -44.307 -52.973  10.620  1.00 69.86  ?  583  GLY B CA  1 
ATOM   5626  C  C   . GLY B 2  583  ? -44.531 -54.153  11.540  1.00 72.83  ?  583  GLY B C   1 
ATOM   5627  O  O   . GLY B 2  583  ? -45.611 -54.253  12.134  1.00 78.29  ?  583  GLY B O   1 
ATOM   5628  N  N   . PHE B 2  584  ? -43.553 -55.053  11.669  1.00 73.85  ?  584  PHE B N   1 
ATOM   5629  C  CA  . PHE B 2  584  ? -43.698 -56.171  12.596  1.00 72.28  ?  584  PHE B CA  1 
ATOM   5630  C  C   . PHE B 2  584  ? -43.799 -55.683  14.034  1.00 72.56  ?  584  PHE B C   1 
ATOM   5631  O  O   . PHE B 2  584  ? -44.616 -56.187  14.813  1.00 72.85  ?  584  PHE B O   1 
ATOM   5632  C  CB  . PHE B 2  584  ? -42.524 -57.139  12.445  1.00 66.60  ?  584  PHE B CB  1 
ATOM   5633  C  CG  . PHE B 2  584  ? -42.624 -58.351  13.326  1.00 70.83  ?  584  PHE B CG  1 
ATOM   5634  C  CD1 . PHE B 2  584  ? -43.469 -59.397  12.996  1.00 74.40  ?  584  PHE B CD1 1 
ATOM   5635  C  CD2 . PHE B 2  584  ? -41.884 -58.438  14.495  1.00 79.82  ?  584  PHE B CD2 1 
ATOM   5636  C  CE1 . PHE B 2  584  ? -43.567 -60.512  13.809  1.00 86.73  ?  584  PHE B CE1 1 
ATOM   5637  C  CE2 . PHE B 2  584  ? -41.978 -59.550  15.314  1.00 83.81  ?  584  PHE B CE2 1 
ATOM   5638  C  CZ  . PHE B 2  584  ? -42.820 -60.589  14.970  1.00 88.44  ?  584  PHE B CZ  1 
ATOM   5639  N  N   . TYR B 2  585  ? -42.980 -54.695  14.400  1.00 71.70  ?  585  TYR B N   1 
ATOM   5640  C  CA  . TYR B 2  585  ? -42.929 -54.173  15.760  1.00 64.59  ?  585  TYR B CA  1 
ATOM   5641  C  C   . TYR B 2  585  ? -43.931 -53.050  16.002  1.00 57.82  ?  585  TYR B C   1 
ATOM   5642  O  O   . TYR B 2  585  ? -43.706 -52.204  16.878  1.00 60.55  ?  585  TYR B O   1 
ATOM   5643  C  CB  . TYR B 2  585  ? -41.513 -53.696  16.086  1.00 65.07  ?  585  TYR B CB  1 
ATOM   5644  C  CG  . TYR B 2  585  ? -40.433 -54.732  15.861  1.00 66.19  ?  585  TYR B CG  1 
ATOM   5645  C  CD1 . TYR B 2  585  ? -40.150 -55.690  16.826  1.00 62.44  ?  585  TYR B CD1 1 
ATOM   5646  C  CD2 . TYR B 2  585  ? -39.685 -54.742  14.690  1.00 70.72  ?  585  TYR B CD2 1 
ATOM   5647  C  CE1 . TYR B 2  585  ? -39.162 -56.636  16.627  1.00 63.18  ?  585  TYR B CE1 1 
ATOM   5648  C  CE2 . TYR B 2  585  ? -38.694 -55.684  14.482  1.00 66.35  ?  585  TYR B CE2 1 
ATOM   5649  C  CZ  . TYR B 2  585  ? -38.437 -56.628  15.454  1.00 64.93  ?  585  TYR B CZ  1 
ATOM   5650  O  OH  . TYR B 2  585  ? -37.451 -57.568  15.253  1.00 65.45  ?  585  TYR B OH  1 
ATOM   5651  N  N   . ALA B 2  586  ? -45.034 -53.014  15.251  1.00 54.56  ?  586  ALA B N   1 
ATOM   5652  C  CA  . ALA B 2  586  ? -46.033 -51.973  15.462  1.00 56.82  ?  586  ALA B CA  1 
ATOM   5653  C  C   . ALA B 2  586  ? -46.823 -52.183  16.746  1.00 53.52  ?  586  ALA B C   1 
ATOM   5654  O  O   . ALA B 2  586  ? -47.449 -51.238  17.235  1.00 55.41  ?  586  ALA B O   1 
ATOM   5655  C  CB  . ALA B 2  586  ? -46.986 -51.903  14.269  1.00 60.77  ?  586  ALA B CB  1 
ATOM   5656  N  N   . ASN B 2  587  ? -46.813 -53.395  17.297  1.00 75.00  ?  587  ASN B N   1 
ATOM   5657  C  CA  . ASN B 2  587  ? -47.457 -53.671  18.573  1.00 82.10  ?  587  ASN B CA  1 
ATOM   5658  C  C   . ASN B 2  587  ? -46.538 -53.426  19.763  1.00 86.50  ?  587  ASN B C   1 
ATOM   5659  O  O   . ASN B 2  587  ? -47.023 -53.358  20.897  1.00 92.27  ?  587  ASN B O   1 
ATOM   5660  C  CB  . ASN B 2  587  ? -47.964 -55.118  18.606  1.00 94.75  ?  587  ASN B CB  1 
ATOM   5661  C  CG  . ASN B 2  587  ? -48.923 -55.374  19.753  1.00 95.60  ?  587  ASN B CG  1 
ATOM   5662  O  OD1 . ASN B 2  587  ? -49.622 -54.468  20.205  1.00 91.45  ?  587  ASN B OD1 1 
ATOM   5663  N  ND2 . ASN B 2  587  ? -48.954 -56.612  20.234  1.00 90.19  ?  587  ASN B ND2 1 
ATOM   5664  N  N   . ASN B 2  588  ? -45.235 -53.287  19.534  1.00 83.32  ?  588  ASN B N   1 
ATOM   5665  C  CA  . ASN B 2  588  ? -44.290 -53.071  20.622  1.00 77.61  ?  588  ASN B CA  1 
ATOM   5666  C  C   . ASN B 2  588  ? -44.410 -51.642  21.141  1.00 80.77  ?  588  ASN B C   1 
ATOM   5667  O  O   . ASN B 2  588  ? -44.196 -50.680  20.393  1.00 73.83  ?  588  ASN B O   1 
ATOM   5668  C  CB  . ASN B 2  588  ? -42.868 -53.357  20.148  1.00 73.46  ?  588  ASN B CB  1 
ATOM   5669  C  CG  . ASN B 2  588  ? -41.919 -53.649  21.293  1.00 76.03  ?  588  ASN B CG  1 
ATOM   5670  O  OD1 . ASN B 2  588  ? -41.503 -52.745  22.016  1.00 83.08  ?  588  ASN B OD1 1 
ATOM   5671  N  ND2 . ASN B 2  588  ? -41.572 -54.918  21.464  1.00 74.96  ?  588  ASN B ND2 1 
ATOM   5672  N  N   . GLY B 2  589  ? -44.750 -51.503  22.423  1.00 79.40  ?  589  GLY B N   1 
ATOM   5673  C  CA  . GLY B 2  589  ? -44.925 -50.176  22.991  1.00 74.47  ?  589  GLY B CA  1 
ATOM   5674  C  C   . GLY B 2  589  ? -43.621 -49.413  23.120  1.00 74.89  ?  589  GLY B C   1 
ATOM   5675  O  O   . GLY B 2  589  ? -43.590 -48.190  22.959  1.00 72.90  ?  589  GLY B O   1 
ATOM   5676  N  N   . TRP B 2  590  ? -42.527 -50.121  23.415  1.00 70.65  ?  590  TRP B N   1 
ATOM   5677  C  CA  . TRP B 2  590  ? -41.232 -49.463  23.557  1.00 69.89  ?  590  TRP B CA  1 
ATOM   5678  C  C   . TRP B 2  590  ? -40.799 -48.803  22.255  1.00 75.81  ?  590  TRP B C   1 
ATOM   5679  O  O   . TRP B 2  590  ? -40.288 -47.677  22.260  1.00 76.08  ?  590  TRP B O   1 
ATOM   5680  C  CB  . TRP B 2  590  ? -40.179 -50.471  24.015  1.00 68.04  ?  590  TRP B CB  1 
ATOM   5681  C  CG  . TRP B 2  590  ? -40.307 -50.884  25.445  1.00 68.96  ?  590  TRP B CG  1 
ATOM   5682  C  CD1 . TRP B 2  590  ? -41.034 -50.263  26.418  1.00 76.86  ?  590  TRP B CD1 1 
ATOM   5683  C  CD2 . TRP B 2  590  ? -39.686 -52.014  26.067  1.00 68.60  ?  590  TRP B CD2 1 
ATOM   5684  N  NE1 . TRP B 2  590  ? -40.903 -50.936  27.609  1.00 74.05  ?  590  TRP B NE1 1 
ATOM   5685  C  CE2 . TRP B 2  590  ? -40.081 -52.016  27.419  1.00 71.11  ?  590  TRP B CE2 1 
ATOM   5686  C  CE3 . TRP B 2  590  ? -38.834 -53.024  25.611  1.00 67.91  ?  590  TRP B CE3 1 
ATOM   5687  C  CZ2 . TRP B 2  590  ? -39.653 -52.990  28.320  1.00 72.19  ?  590  TRP B CZ2 1 
ATOM   5688  C  CZ3 . TRP B 2  590  ? -38.412 -53.990  26.506  1.00 70.27  ?  590  TRP B CZ3 1 
ATOM   5689  C  CH2 . TRP B 2  590  ? -38.822 -53.966  27.844  1.00 67.01  ?  590  TRP B CH2 1 
ATOM   5690  N  N   . LEU B 2  591  ? -40.995 -49.487  21.127  1.00 58.64  ?  591  LEU B N   1 
ATOM   5691  C  CA  . LEU B 2  591  ? -40.567 -48.940  19.845  1.00 52.92  ?  591  LEU B CA  1 
ATOM   5692  C  C   . LEU B 2  591  ? -41.550 -47.914  19.305  1.00 51.70  ?  591  LEU B C   1 
ATOM   5693  O  O   . LEU B 2  591  ? -41.135 -46.946  18.659  1.00 50.53  ?  591  LEU B O   1 
ATOM   5694  C  CB  . LEU B 2  591  ? -40.376 -50.067  18.831  1.00 56.62  ?  591  LEU B CB  1 
ATOM   5695  C  CG  . LEU B 2  591  ? -39.226 -51.021  19.149  1.00 54.01  ?  591  LEU B CG  1 
ATOM   5696  C  CD1 . LEU B 2  591  ? -39.065 -52.072  18.063  1.00 55.47  ?  591  LEU B CD1 1 
ATOM   5697  C  CD2 . LEU B 2  591  ? -37.926 -50.257  19.362  1.00 51.92  ?  591  LEU B CD2 1 
ATOM   5698  N  N   . GLN B 2  592  ? -42.848 -48.104  19.554  1.00 52.81  ?  592  GLN B N   1 
ATOM   5699  C  CA  . GLN B 2  592  ? -43.831 -47.138  19.080  1.00 58.40  ?  592  GLN B CA  1 
ATOM   5700  C  C   . GLN B 2  592  ? -43.715 -45.812  19.820  1.00 60.23  ?  592  GLN B C   1 
ATOM   5701  O  O   . GLN B 2  592  ? -43.994 -44.755  19.244  1.00 53.38  ?  592  GLN B O   1 
ATOM   5702  C  CB  . GLN B 2  592  ? -45.242 -47.709  19.226  1.00 57.31  ?  592  GLN B CB  1 
ATOM   5703  C  CG  . GLN B 2  592  ? -46.293 -46.961  18.426  1.00 64.18  ?  592  GLN B CG  1 
ATOM   5704  C  CD  . GLN B 2  592  ? -46.412 -47.474  17.004  1.00 68.10  ?  592  GLN B CD  1 
ATOM   5705  O  OE1 . GLN B 2  592  ? -46.178 -48.653  16.734  1.00 64.06  ?  592  GLN B OE1 1 
ATOM   5706  N  NE2 . GLN B 2  592  ? -46.764 -46.585  16.082  1.00 70.64  ?  592  GLN B NE2 1 
ATOM   5707  N  N   . GLU B 2  593  ? -43.303 -45.846  21.088  1.00 86.73  ?  593  GLU B N   1 
ATOM   5708  C  CA  . GLU B 2  593  ? -43.129 -44.632  21.874  1.00 85.09  ?  593  GLU B CA  1 
ATOM   5709  C  C   . GLU B 2  593  ? -41.753 -44.005  21.691  1.00 79.56  ?  593  GLU B C   1 
ATOM   5710  O  O   . GLU B 2  593  ? -41.592 -42.809  21.958  1.00 74.72  ?  593  GLU B O   1 
ATOM   5711  C  CB  . GLU B 2  593  ? -43.367 -44.930  23.361  1.00 79.41  ?  593  GLU B CB  1 
ATOM   5712  C  CG  . GLU B 2  593  ? -43.247 -43.719  24.280  1.00 88.57  ?  593  GLU B CG  1 
ATOM   5713  C  CD  . GLU B 2  593  ? -44.187 -43.786  25.465  1.00 95.09  ?  593  GLU B CD  1 
ATOM   5714  O  OE1 . GLU B 2  593  ? -44.095 -44.761  26.238  1.00 91.77  ?  593  GLU B OE1 1 
ATOM   5715  O  OE2 . GLU B 2  593  ? -45.022 -42.870  25.622  1.00 104.27 -1 593  GLU B OE2 1 
ATOM   5716  N  N   . LEU B 2  594  ? -40.771 -44.774  21.239  1.00 75.86  ?  594  LEU B N   1 
ATOM   5717  C  CA  . LEU B 2  594  ? -39.424 -44.260  21.027  1.00 71.50  ?  594  LEU B CA  1 
ATOM   5718  C  C   . LEU B 2  594  ? -39.437 -43.095  20.042  1.00 73.10  ?  594  LEU B C   1 
ATOM   5719  O  O   . LEU B 2  594  ? -39.876 -43.269  18.894  1.00 74.16  ?  594  LEU B O   1 
ATOM   5720  C  CB  . LEU B 2  594  ? -38.513 -45.370  20.513  1.00 76.30  ?  594  LEU B CB  1 
ATOM   5721  C  CG  . LEU B 2  594  ? -37.038 -45.007  20.336  1.00 70.57  ?  594  LEU B CG  1 
ATOM   5722  C  CD1 . LEU B 2  594  ? -36.351 -44.853  21.684  1.00 67.85  ?  594  LEU B CD1 1 
ATOM   5723  C  CD2 . LEU B 2  594  ? -36.340 -46.061  19.498  1.00 65.38  ?  594  LEU B CD2 1 
ATOM   5724  N  N   . PRO B 2  595  ? -38.981 -41.907  20.438  1.00 55.57  ?  595  PRO B N   1 
ATOM   5725  C  CA  . PRO B 2  595  ? -38.937 -40.781  19.496  1.00 52.70  ?  595  PRO B CA  1 
ATOM   5726  C  C   . PRO B 2  595  ? -37.997 -41.073  18.337  1.00 57.48  ?  595  PRO B C   1 
ATOM   5727  O  O   . PRO B 2  595  ? -36.832 -41.427  18.533  1.00 57.65  ?  595  PRO B O   1 
ATOM   5728  C  CB  . PRO B 2  595  ? -38.434 -39.617  20.359  1.00 51.35  ?  595  PRO B CB  1 
ATOM   5729  C  CG  . PRO B 2  595  ? -38.750 -40.017  21.762  1.00 57.97  ?  595  PRO B CG  1 
ATOM   5730  C  CD  . PRO B 2  595  ? -38.572 -41.505  21.793  1.00 59.21  ?  595  PRO B CD  1 
ATOM   5731  N  N   . ARG B 2  596  ? -38.518 -40.923  17.122  1.00 72.50  ?  596  ARG B N   1 
ATOM   5732  C  CA  . ARG B 2  596  ? -37.741 -41.222  15.932  1.00 72.07  ?  596  ARG B CA  1 
ATOM   5733  C  C   . ARG B 2  596  ? -36.585 -40.233  15.789  1.00 68.76  ?  596  ARG B C   1 
ATOM   5734  O  O   . ARG B 2  596  ? -36.709 -39.061  16.156  1.00 69.17  ?  596  ARG B O   1 
ATOM   5735  C  CB  . ARG B 2  596  ? -38.624 -41.176  14.686  1.00 69.61  ?  596  ARG B CB  1 
ATOM   5736  C  CG  . ARG B 2  596  ? -39.419 -42.454  14.418  1.00 66.30  ?  596  ARG B CG  1 
ATOM   5737  C  CD  . ARG B 2  596  ? -40.596 -42.589  15.371  1.00 71.36  ?  596  ARG B CD  1 
ATOM   5738  N  NE  . ARG B 2  596  ? -41.505 -43.665  14.998  1.00 67.03  ?  596  ARG B NE  1 
ATOM   5739  C  CZ  . ARG B 2  596  ? -42.436 -44.167  15.799  1.00 75.56  ?  596  ARG B CZ  1 
ATOM   5740  N  NH1 . ARG B 2  596  ? -42.597 -43.723  17.035  1.00 71.29  ?  596  ARG B NH1 1 
ATOM   5741  N  NH2 . ARG B 2  596  ? -43.224 -45.139  15.349  1.00 85.85  ?  596  ARG B NH2 1 
ATOM   5742  N  N   . PRO B 2  597  ? -35.444 -40.684  15.273  1.00 65.48  ?  597  PRO B N   1 
ATOM   5743  C  CA  . PRO B 2  597  ? -34.308 -39.775  15.094  1.00 63.32  ?  597  PRO B CA  1 
ATOM   5744  C  C   . PRO B 2  597  ? -34.612 -38.708  14.056  1.00 76.11  ?  597  PRO B C   1 
ATOM   5745  O  O   . PRO B 2  597  ? -35.355 -38.933  13.097  1.00 77.44  ?  597  PRO B O   1 
ATOM   5746  C  CB  . PRO B 2  597  ? -33.178 -40.699  14.622  1.00 66.98  ?  597  PRO B CB  1 
ATOM   5747  C  CG  . PRO B 2  597  ? -33.620 -42.082  14.991  1.00 64.10  ?  597  PRO B CG  1 
ATOM   5748  C  CD  . PRO B 2  597  ? -35.110 -42.066  14.892  1.00 65.17  ?  597  PRO B CD  1 
ATOM   5749  N  N   . LEU B 2  598  ? -34.047 -37.520  14.287  1.00 69.93  ?  598  LEU B N   1 
ATOM   5750  C  CA  . LEU B 2  598  ? -34.123 -36.388  13.365  1.00 73.86  ?  598  LEU B CA  1 
ATOM   5751  C  C   . LEU B 2  598  ? -35.537 -35.825  13.246  1.00 65.44  ?  598  LEU B C   1 
ATOM   5752  O  O   . LEU B 2  598  ? -35.723 -34.713  12.741  1.00 67.79  ?  598  LEU B O   1 
ATOM   5753  C  CB  . LEU B 2  598  ? -33.594 -36.786  11.982  1.00 58.84  ?  598  LEU B CB  1 
ATOM   5754  C  CG  . LEU B 2  598  ? -32.073 -36.839  11.818  1.00 66.29  ?  598  LEU B CG  1 
ATOM   5755  C  CD1 . LEU B 2  598  ? -31.504 -38.149  12.346  1.00 62.01  ?  598  LEU B CD1 1 
ATOM   5756  C  CD2 . LEU B 2  598  ? -31.690 -36.637  10.364  1.00 69.77  ?  598  LEU B CD2 1 
ATOM   5757  N  N   . THR B 2  599  ? -36.536 -36.570  13.710  1.00 47.37  ?  599  THR B N   1 
ATOM   5758  C  CA  . THR B 2  599  ? -37.929 -36.160  13.616  1.00 44.57  ?  599  THR B CA  1 
ATOM   5759  C  C   . THR B 2  599  ? -38.612 -36.019  14.966  1.00 45.84  ?  599  THR B C   1 
ATOM   5760  O  O   . THR B 2  599  ? -39.460 -35.137  15.120  1.00 47.13  ?  599  THR B O   1 
ATOM   5761  C  CB  . THR B 2  599  ? -38.721 -37.161  12.757  1.00 47.39  ?  599  THR B CB  1 
ATOM   5762  O  OG1 . THR B 2  599  ? -38.017 -37.391  11.532  1.00 60.41  ?  599  THR B OG1 1 
ATOM   5763  C  CG2 . THR B 2  599  ? -40.091 -36.609  12.421  1.00 43.74  ?  599  THR B CG2 1 
ATOM   5764  N  N   . LYS B 2  600  ? -38.264 -36.861  15.941  1.00 69.31  ?  600  LYS B N   1 
ATOM   5765  C  CA  . LYS B 2  600  ? -38.773 -36.793  17.310  1.00 72.40  ?  600  LYS B CA  1 
ATOM   5766  C  C   . LYS B 2  600  ? -40.278 -37.037  17.390  1.00 73.08  ?  600  LYS B C   1 
ATOM   5767  O  O   . LYS B 2  600  ? -40.906 -36.714  18.403  1.00 69.19  ?  600  LYS B O   1 
ATOM   5768  C  CB  . LYS B 2  600  ? -38.416 -35.456  17.971  1.00 73.72  ?  600  LYS B CB  1 
ATOM   5769  C  CG  . LYS B 2  600  ? -36.924 -35.245  18.172  1.00 65.00  ?  600  LYS B CG  1 
ATOM   5770  C  CD  . LYS B 2  600  ? -36.262 -36.478  18.767  1.00 65.90  ?  600  LYS B CD  1 
ATOM   5771  C  CE  . LYS B 2  600  ? -34.775 -36.508  18.452  1.00 68.59  ?  600  LYS B CE  1 
ATOM   5772  N  NZ  . LYS B 2  600  ? -34.145 -37.799  18.842  1.00 77.13  ?  600  LYS B NZ  1 
ATOM   5773  N  N   . LEU B 2  601  ? -40.872 -37.605  16.344  1.00 75.94  ?  601  LEU B N   1 
ATOM   5774  C  CA  . LEU B 2  601  ? -42.282 -37.967  16.372  1.00 78.19  ?  601  LEU B CA  1 
ATOM   5775  C  C   . LEU B 2  601  ? -42.464 -39.304  17.084  1.00 76.13  ?  601  LEU B C   1 
ATOM   5776  O  O   . LEU B 2  601  ? -41.565 -40.147  17.097  1.00 78.26  ?  601  LEU B O   1 
ATOM   5777  C  CB  . LEU B 2  601  ? -42.841 -38.062  14.951  1.00 81.07  ?  601  LEU B CB  1 
ATOM   5778  C  CG  . LEU B 2  601  ? -43.162 -36.775  14.185  1.00 81.01  ?  601  LEU B CG  1 
ATOM   5779  C  CD1 . LEU B 2  601  ? -43.772 -37.105  12.832  1.00 79.22  ?  601  LEU B CD1 1 
ATOM   5780  C  CD2 . LEU B 2  601  ? -44.074 -35.851  14.968  1.00 89.70  ?  601  LEU B CD2 1 
ATOM   5781  N  N   . VAL B 2  602  ? -43.636 -39.498  17.690  1.00 66.97  ?  602  VAL B N   1 
ATOM   5782  C  CA  . VAL B 2  602  ? -43.963 -40.772  18.321  1.00 75.47  ?  602  VAL B CA  1 
ATOM   5783  C  C   . VAL B 2  602  ? -45.395 -41.140  17.965  1.00 78.86  ?  602  VAL B C   1 
ATOM   5784  O  O   . VAL B 2  602  ? -46.222 -40.272  17.672  1.00 83.57  ?  602  VAL B O   1 
ATOM   5785  C  CB  . VAL B 2  602  ? -43.782 -40.757  19.863  1.00 73.76  ?  602  VAL B CB  1 
ATOM   5786  C  CG1 . VAL B 2  602  ? -42.372 -40.335  20.249  1.00 70.04  ?  602  VAL B CG1 1 
ATOM   5787  C  CG2 . VAL B 2  602  ? -44.834 -39.874  20.549  1.00 74.77  ?  602  VAL B CG2 1 
ATOM   5788  N  N   . TRP B 2  603  ? -45.676 -42.444  17.967  1.00 73.17  ?  603  TRP B N   1 
ATOM   5789  C  CA  . TRP B 2  603  ? -47.012 -43.015  17.802  1.00 73.34  ?  603  TRP B CA  1 
ATOM   5790  C  C   . TRP B 2  603  ? -47.681 -42.637  16.482  1.00 80.21  ?  603  TRP B C   1 
ATOM   5791  O  O   . TRP B 2  603  ? -48.888 -42.865  16.320  1.00 85.58  ?  603  TRP B O   1 
ATOM   5792  C  CB  . TRP B 2  603  ? -47.934 -42.622  18.964  1.00 72.77  ?  603  TRP B CB  1 
ATOM   5793  C  CG  . TRP B 2  603  ? -47.576 -43.255  20.274  1.00 72.58  ?  603  TRP B CG  1 
ATOM   5794  C  CD1 . TRP B 2  603  ? -46.732 -42.755  21.223  1.00 75.26  ?  603  TRP B CD1 1 
ATOM   5795  C  CD2 . TRP B 2  603  ? -48.054 -44.505  20.783  1.00 73.19  ?  603  TRP B CD2 1 
ATOM   5796  N  NE1 . TRP B 2  603  ? -46.655 -43.616  22.291  1.00 82.52  ?  603  TRP B NE1 1 
ATOM   5797  C  CE2 . TRP B 2  603  ? -47.457 -44.699  22.045  1.00 78.31  ?  603  TRP B CE2 1 
ATOM   5798  C  CE3 . TRP B 2  603  ? -48.929 -45.480  20.294  1.00 66.67  ?  603  TRP B CE3 1 
ATOM   5799  C  CZ2 . TRP B 2  603  ? -47.706 -45.825  22.822  1.00 77.12  ?  603  TRP B CZ2 1 
ATOM   5800  C  CZ3 . TRP B 2  603  ? -49.174 -46.597  21.066  1.00 67.89  ?  603  TRP B CZ3 1 
ATOM   5801  C  CH2 . TRP B 2  603  ? -48.566 -46.761  22.317  1.00 79.86  ?  603  TRP B CH2 1 
ATOM   5802  N  N   . ASP B 2  604  ? -46.943 -42.073  15.528  1.00 81.01  ?  604  ASP B N   1 
ATOM   5803  C  CA  . ASP B 2  604  ? -47.561 -41.573  14.309  1.00 79.01  ?  604  ASP B CA  1 
ATOM   5804  C  C   . ASP B 2  604  ? -46.604 -41.730  13.137  1.00 85.53  ?  604  ASP B C   1 
ATOM   5805  O  O   . ASP B 2  604  ? -45.445 -42.124  13.292  1.00 80.05  ?  604  ASP B O   1 
ATOM   5806  C  CB  . ASP B 2  604  ? -47.984 -40.107  14.458  1.00 81.39  ?  604  ASP B CB  1 
ATOM   5807  C  CG  . ASP B 2  604  ? -49.380 -39.957  15.032  1.00 97.55  ?  604  ASP B CG  1 
ATOM   5808  O  OD1 . ASP B 2  604  ? -50.250 -40.796  14.713  1.00 91.09  ?  604  ASP B OD1 1 
ATOM   5809  O  OD2 . ASP B 2  604  ? -49.610 -38.999  15.800  1.00 101.37 -1 604  ASP B OD2 1 
ATOM   5810  N  N   . ASN B 2  605  ? -47.119 -41.414  11.951  1.00 90.42  ?  605  ASN B N   1 
ATOM   5811  C  CA  . ASN B 2  605  ? -46.362 -41.417  10.709  1.00 71.30  ?  605  ASN B CA  1 
ATOM   5812  C  C   . ASN B 2  605  ? -46.656 -40.124  9.965   1.00 79.10  ?  605  ASN B C   1 
ATOM   5813  O  O   . ASN B 2  605  ? -47.768 -39.594  10.032  1.00 86.36  ?  605  ASN B O   1 
ATOM   5814  C  CB  . ASN B 2  605  ? -46.725 -42.626  9.833   1.00 71.59  ?  605  ASN B CB  1 
ATOM   5815  C  CG  . ASN B 2  605  ? -45.885 -42.710  8.570   1.00 85.74  ?  605  ASN B CG  1 
ATOM   5816  O  OD1 . ASN B 2  605  ? -44.834 -42.078  8.463   1.00 83.93  ?  605  ASN B OD1 1 
ATOM   5817  N  ND2 . ASN B 2  605  ? -46.352 -43.492  7.603   1.00 84.97  ?  605  ASN B ND2 1 
ATOM   5818  N  N   . ALA B 2  606  ? -45.652 -39.614  9.254   1.00 80.50  ?  606  ALA B N   1 
ATOM   5819  C  CA  . ALA B 2  606  ? -45.801 -38.338  8.570   1.00 78.32  ?  606  ALA B CA  1 
ATOM   5820  C  C   . ALA B 2  606  ? -45.019 -38.352  7.267   1.00 71.58  ?  606  ALA B C   1 
ATOM   5821  O  O   . ALA B 2  606  ? -44.086 -39.139  7.082   1.00 69.38  ?  606  ALA B O   1 
ATOM   5822  C  CB  . ALA B 2  606  ? -45.340 -37.172  9.452   1.00 76.26  ?  606  ALA B CB  1 
ATOM   5823  N  N   . ALA B 2  607  ? -45.418 -37.462  6.360   1.00 61.59  ?  607  ALA B N   1 
ATOM   5824  C  CA  . ALA B 2  607  ? -44.711 -37.247  5.103   1.00 62.60  ?  607  ALA B CA  1 
ATOM   5825  C  C   . ALA B 2  607  ? -43.639 -36.190  5.337   1.00 63.10  ?  607  ALA B C   1 
ATOM   5826  O  O   . ALA B 2  607  ? -43.951 -35.008  5.518   1.00 64.02  ?  607  ALA B O   1 
ATOM   5827  C  CB  . ALA B 2  607  ? -45.679 -36.822  4.003   1.00 62.13  ?  607  ALA B CB  1 
ATOM   5828  N  N   . LEU B 2  608  ? -42.378 -36.613  5.338   1.00 67.23  ?  608  LEU B N   1 
ATOM   5829  C  CA  . LEU B 2  608  ? -41.265 -35.728  5.650   1.00 67.10  ?  608  LEU B CA  1 
ATOM   5830  C  C   . LEU B 2  608  ? -40.818 -34.988  4.397   1.00 66.65  ?  608  LEU B C   1 
ATOM   5831  O  O   . LEU B 2  608  ? -40.562 -35.607  3.359   1.00 63.28  ?  608  LEU B O   1 
ATOM   5832  C  CB  . LEU B 2  608  ? -40.101 -36.523  6.243   1.00 65.40  ?  608  LEU B CB  1 
ATOM   5833  C  CG  . LEU B 2  608  ? -40.496 -37.609  7.247   1.00 55.49  ?  608  LEU B CG  1 
ATOM   5834  C  CD1 . LEU B 2  608  ? -39.293 -38.458  7.627   1.00 52.21  ?  608  LEU B CD1 1 
ATOM   5835  C  CD2 . LEU B 2  608  ? -41.141 -36.995  8.481   1.00 60.82  ?  608  LEU B CD2 1 
ATOM   5836  N  N   . MET B 2  609  ? -40.723 -33.663  4.499   1.00 75.70  ?  609  MET B N   1 
ATOM   5837  C  CA  . MET B 2  609  ? -40.313 -32.834  3.377   1.00 77.82  ?  609  MET B CA  1 
ATOM   5838  C  C   . MET B 2  609  ? -39.546 -31.630  3.902   1.00 75.29  ?  609  MET B C   1 
ATOM   5839  O  O   . MET B 2  609  ? -39.732 -31.209  5.047   1.00 72.25  ?  609  MET B O   1 
ATOM   5840  C  CB  . MET B 2  609  ? -41.517 -32.375  2.544   1.00 76.16  ?  609  MET B CB  1 
ATOM   5841  C  CG  . MET B 2  609  ? -42.496 -31.489  3.299   1.00 73.20  ?  609  MET B CG  1 
ATOM   5842  S  SD  . MET B 2  609  ? -44.050 -31.257  2.415   1.00 77.70  ?  609  MET B SD  1 
ATOM   5843  C  CE  . MET B 2  609  ? -44.636 -32.946  2.312   1.00 71.80  ?  609  MET B CE  1 
ATOM   5844  N  N   . SER B 2  610  ? -38.680 -31.085  3.052   1.00 86.54  ?  610  SER B N   1 
ATOM   5845  C  CA  . SER B 2  610  ? -37.923 -29.900  3.408   1.00 88.19  ?  610  SER B CA  1 
ATOM   5846  C  C   . SER B 2  610  ? -38.852 -28.691  3.497   1.00 93.04  ?  610  SER B C   1 
ATOM   5847  O  O   . SER B 2  610  ? -39.943 -28.693  2.923   1.00 96.20  ?  610  SER B O   1 
ATOM   5848  C  CB  . SER B 2  610  ? -36.822 -29.646  2.382   1.00 83.96  ?  610  SER B CB  1 
ATOM   5849  O  OG  . SER B 2  610  ? -37.367 -29.197  1.154   1.00 101.17 ?  610  SER B OG  1 
ATOM   5850  N  N   . PRO B 2  611  ? -38.445 -27.648  4.229   1.00 88.80  ?  611  PRO B N   1 
ATOM   5851  C  CA  . PRO B 2  611  ? -39.296 -26.448  4.309   1.00 89.71  ?  611  PRO B CA  1 
ATOM   5852  C  C   . PRO B 2  611  ? -39.587 -25.821  2.957   1.00 83.72  ?  611  PRO B C   1 
ATOM   5853  O  O   . PRO B 2  611  ? -40.730 -25.427  2.699   1.00 81.82  ?  611  PRO B O   1 
ATOM   5854  C  CB  . PRO B 2  611  ? -38.484 -25.510  5.213   1.00 88.04  ?  611  PRO B CB  1 
ATOM   5855  C  CG  . PRO B 2  611  ? -37.653 -26.428  6.045   1.00 83.89  ?  611  PRO B CG  1 
ATOM   5856  C  CD  . PRO B 2  611  ? -37.283 -27.557  5.130   1.00 84.53  ?  611  PRO B CD  1 
ATOM   5857  N  N   . ARG B 2  612  ? -38.584 -25.724  2.080   1.00 86.94  ?  612  ARG B N   1 
ATOM   5858  C  CA  . ARG B 2  612  ? -38.814 -25.149  0.758   1.00 93.30  ?  612  ARG B CA  1 
ATOM   5859  C  C   . ARG B 2  612  ? -39.828 -25.965  -0.033  1.00 87.91  ?  612  ARG B C   1 
ATOM   5860  O  O   . ARG B 2  612  ? -40.671 -25.404  -0.742  1.00 89.78  ?  612  ARG B O   1 
ATOM   5861  C  CB  . ARG B 2  612  ? -37.495 -25.050  -0.008  1.00 100.83 ?  612  ARG B CB  1 
ATOM   5862  C  CG  . ARG B 2  612  ? -37.449 -23.921  -1.022  1.00 96.19  ?  612  ARG B CG  1 
ATOM   5863  C  CD  . ARG B 2  612  ? -36.150 -23.950  -1.808  1.00 96.49  ?  612  ARG B CD  1 
ATOM   5864  N  NE  . ARG B 2  612  ? -35.004 -23.611  -0.973  1.00 98.67  ?  612  ARG B NE  1 
ATOM   5865  C  CZ  . ARG B 2  612  ? -34.650 -22.374  -0.652  1.00 100.64 ?  612  ARG B CZ  1 
ATOM   5866  N  NH1 . ARG B 2  612  ? -35.324 -21.325  -1.093  1.00 108.23 ?  612  ARG B NH1 1 
ATOM   5867  N  NH2 . ARG B 2  612  ? -33.591 -22.185  0.131   1.00 101.87 ?  612  ARG B NH2 1 
ATOM   5868  N  N   . THR B 2  613  ? -39.762 -27.295  0.077   1.00 70.71  ?  613  THR B N   1 
ATOM   5869  C  CA  . THR B 2  613  ? -40.707 -28.146  -0.638  1.00 72.66  ?  613  THR B CA  1 
ATOM   5870  C  C   . THR B 2  613  ? -42.130 -27.932  -0.138  1.00 70.92  ?  613  THR B C   1 
ATOM   5871  O  O   . THR B 2  613  ? -43.074 -27.866  -0.935  1.00 74.36  ?  613  THR B O   1 
ATOM   5872  C  CB  . THR B 2  613  ? -40.299 -29.615  -0.496  1.00 76.27  ?  613  THR B CB  1 
ATOM   5873  O  OG1 . THR B 2  613  ? -39.060 -29.836  -1.181  1.00 72.23  ?  613  THR B OG1 1 
ATOM   5874  C  CG2 . THR B 2  613  ? -41.364 -30.531  -1.081  1.00 74.06  ?  613  THR B CG2 1 
ATOM   5875  N  N   . ALA B 2  614  ? -42.306 -27.814  1.180   1.00 82.16  ?  614  ALA B N   1 
ATOM   5876  C  CA  . ALA B 2  614  ? -43.638 -27.583  1.727   1.00 83.33  ?  614  ALA B CA  1 
ATOM   5877  C  C   . ALA B 2  614  ? -44.169 -26.210  1.332   1.00 87.68  ?  614  ALA B C   1 
ATOM   5878  O  O   . ALA B 2  614  ? -45.367 -26.054  1.072   1.00 90.94  ?  614  ALA B O   1 
ATOM   5879  C  CB  . ALA B 2  614  ? -43.616 -27.732  3.246   1.00 84.85  ?  614  ALA B CB  1 
ATOM   5880  N  N   . ILE B 2  615  ? -43.292 -25.205  1.284   1.00 96.27  ?  615  ILE B N   1 
ATOM   5881  C  CA  . ILE B 2  615  ? -43.713 -23.862  0.889   1.00 99.33  ?  615  ILE B CA  1 
ATOM   5882  C  C   . ILE B 2  615  ? -44.193 -23.862  -0.557  1.00 94.79  ?  615  ILE B C   1 
ATOM   5883  O  O   . ILE B 2  615  ? -45.250 -23.308  -0.883  1.00 96.66  ?  615  ILE B O   1 
ATOM   5884  C  CB  . ILE B 2  615  ? -42.568 -22.854  1.099   1.00 96.22  ?  615  ILE B CB  1 
ATOM   5885  C  CG1 . ILE B 2  615  ? -42.242 -22.692  2.586   1.00 88.14  ?  615  ILE B CG1 1 
ATOM   5886  C  CG2 . ILE B 2  615  ? -42.916 -21.514  0.475   1.00 98.27  ?  615  ILE B CG2 1 
ATOM   5887  C  CD1 . ILE B 2  615  ? -43.452 -22.646  3.484   1.00 91.25  ?  615  ILE B CD1 1 
ATOM   5888  N  N   . LYS B 2  616  ? -43.423 -24.495  -1.445  1.00 95.92  ?  616  LYS B N   1 
ATOM   5889  C  CA  . LYS B 2  616  ? -43.734 -24.450  -2.869  1.00 102.57 ?  616  LYS B CA  1 
ATOM   5890  C  C   . LYS B 2  616  ? -44.937 -25.316  -3.222  1.00 102.55 ?  616  LYS B C   1 
ATOM   5891  O  O   . LYS B 2  616  ? -45.720 -24.952  -4.106  1.00 113.24 ?  616  LYS B O   1 
ATOM   5892  C  CB  . LYS B 2  616  ? -42.513 -24.885  -3.680  1.00 99.64  ?  616  LYS B CB  1 
ATOM   5893  C  CG  . LYS B 2  616  ? -42.721 -24.873  -5.184  1.00 104.46 ?  616  LYS B CG  1 
ATOM   5894  C  CD  . LYS B 2  616  ? -42.087 -26.089  -5.837  1.00 111.01 ?  616  LYS B CD  1 
ATOM   5895  C  CE  . LYS B 2  616  ? -42.235 -26.037  -7.349  1.00 116.25 ?  616  LYS B CE  1 
ATOM   5896  N  NZ  . LYS B 2  616  ? -42.129 -27.388  -7.963  1.00 119.62 ?  616  LYS B NZ  1 
ATOM   5897  N  N   . LEU B 2  617  ? -45.109 -26.450  -2.545  1.00 92.69  ?  617  LEU B N   1 
ATOM   5898  C  CA  . LEU B 2  617  ? -46.117 -27.421  -2.953  1.00 88.42  ?  617  LEU B CA  1 
ATOM   5899  C  C   . LEU B 2  617  ? -47.455 -27.231  -2.246  1.00 92.80  ?  617  LEU B C   1 
ATOM   5900  O  O   . LEU B 2  617  ? -48.508 -27.377  -2.877  1.00 105.67 ?  617  LEU B O   1 
ATOM   5901  C  CB  . LEU B 2  617  ? -45.594 -28.840  -2.720  1.00 89.66  ?  617  LEU B CB  1 
ATOM   5902  C  CG  . LEU B 2  617  ? -44.611 -29.323  -3.790  1.00 94.08  ?  617  LEU B CG  1 
ATOM   5903  C  CD1 . LEU B 2  617  ? -44.118 -30.728  -3.494  1.00 91.49  ?  617  LEU B CD1 1 
ATOM   5904  C  CD2 . LEU B 2  617  ? -45.248 -29.255  -5.169  1.00 100.76 ?  617  LEU B CD2 1 
ATOM   5905  N  N   . LEU B 2  618  ? -47.448 -26.913  -0.954  1.00 89.90  ?  618  LEU B N   1 
ATOM   5906  C  CA  . LEU B 2  618  ? -48.685 -26.738  -0.203  1.00 90.79  ?  618  LEU B CA  1 
ATOM   5907  C  C   . LEU B 2  618  ? -49.200 -25.304  -0.217  1.00 95.25  ?  618  LEU B C   1 
ATOM   5908  O  O   . LEU B 2  618  ? -50.257 -25.038  0.364   1.00 90.30  ?  618  LEU B O   1 
ATOM   5909  C  CB  . LEU B 2  618  ? -48.499 -27.199  1.246   1.00 94.66  ?  618  LEU B CB  1 
ATOM   5910  C  CG  . LEU B 2  618  ? -48.704 -28.692  1.514   1.00 93.00  ?  618  LEU B CG  1 
ATOM   5911  C  CD1 . LEU B 2  618  ? -47.486 -29.506  1.095   1.00 96.57  ?  618  LEU B CD1 1 
ATOM   5912  C  CD2 . LEU B 2  618  ? -49.042 -28.933  2.977   1.00 91.48  ?  618  LEU B CD2 1 
ATOM   5913  N  N   . GLY B 2  619  ? -48.486 -24.382  -0.856  1.00 70.98  ?  619  GLY B N   1 
ATOM   5914  C  CA  . GLY B 2  619  ? -48.906 -22.992  -0.899  1.00 70.37  ?  619  GLY B CA  1 
ATOM   5915  C  C   . GLY B 2  619  ? -48.948 -22.309  0.451   1.00 72.89  ?  619  GLY B C   1 
ATOM   5916  O  O   . GLY B 2  619  ? -49.921 -21.609  0.758   1.00 72.29  ?  619  GLY B O   1 
ATOM   5917  N  N   . LEU B 2  620  ? -47.915 -22.497  1.269   1.00 108.41 ?  620  LEU B N   1 
ATOM   5918  C  CA  . LEU B 2  620  ? -47.829 -21.913  2.601   1.00 104.08 ?  620  LEU B CA  1 
ATOM   5919  C  C   . LEU B 2  620  ? -47.211 -20.519  2.529   1.00 104.38 ?  620  LEU B C   1 
ATOM   5920  O  O   . LEU B 2  620  ? -46.283 -20.291  1.747   1.00 103.61 ?  620  LEU B O   1 
ATOM   5921  C  CB  . LEU B 2  620  ? -46.996 -22.800  3.521   1.00 98.18  ?  620  LEU B CB  1 
ATOM   5922  C  CG  . LEU B 2  620  ? -47.497 -24.238  3.674   1.00 99.31  ?  620  LEU B CG  1 
ATOM   5923  C  CD1 . LEU B 2  620  ? -46.520 -25.067  4.488   1.00 98.68  ?  620  LEU B CD1 1 
ATOM   5924  C  CD2 . LEU B 2  620  ? -48.884 -24.272  4.301   1.00 103.20 ?  620  LEU B CD2 1 
ATOM   5925  N  N   . PRO B 2  621  ? -47.703 -19.573  3.329   1.00 96.14  ?  621  PRO B N   1 
ATOM   5926  C  CA  . PRO B 2  621  ? -47.239 -18.172  3.227   1.00 92.99  ?  621  PRO B CA  1 
ATOM   5927  C  C   . PRO B 2  621  ? -45.939 -17.918  3.983   1.00 95.31  ?  621  PRO B C   1 
ATOM   5928  O  O   . PRO B 2  621  ? -45.890 -17.269  5.034   1.00 100.35 ?  621  PRO B O   1 
ATOM   5929  C  CB  . PRO B 2  621  ? -48.425 -17.397  3.808   1.00 101.51 ?  621  PRO B CB  1 
ATOM   5930  C  CG  . PRO B 2  621  ? -49.011 -18.329  4.827   1.00 98.52  ?  621  PRO B CG  1 
ATOM   5931  C  CD  . PRO B 2  621  ? -48.736 -19.742  4.366   1.00 94.30  ?  621  PRO B CD  1 
ATOM   5932  N  N   . PHE B 2  622  ? -44.843 -18.444  3.439   1.00 97.31  ?  622  PHE B N   1 
ATOM   5933  C  CA  . PHE B 2  622  ? -43.513 -18.209  3.981   1.00 97.51  ?  622  PHE B CA  1 
ATOM   5934  C  C   . PHE B 2  622  ? -42.533 -18.032  2.832   1.00 92.82  ?  622  PHE B C   1 
ATOM   5935  O  O   . PHE B 2  622  ? -42.721 -18.585  1.745   1.00 94.86  ?  622  PHE B O   1 
ATOM   5936  C  CB  . PHE B 2  622  ? -43.048 -19.353  4.894   1.00 95.97  ?  622  PHE B CB  1 
ATOM   5937  C  CG  . PHE B 2  622  ? -43.867 -19.505  6.148   1.00 94.63  ?  622  PHE B CG  1 
ATOM   5938  C  CD1 . PHE B 2  622  ? -45.054 -20.220  6.138   1.00 87.73  ?  622  PHE B CD1 1 
ATOM   5939  C  CD2 . PHE B 2  622  ? -43.444 -18.938  7.338   1.00 98.00  ?  622  PHE B CD2 1 
ATOM   5940  C  CE1 . PHE B 2  622  ? -45.805 -20.361  7.290   1.00 85.97  ?  622  PHE B CE1 1 
ATOM   5941  C  CE2 . PHE B 2  622  ? -44.191 -19.076  8.493   1.00 91.97  ?  622  PHE B CE2 1 
ATOM   5942  C  CZ  . PHE B 2  622  ? -45.372 -19.789  8.469   1.00 83.98  ?  622  PHE B CZ  1 
ATOM   5943  N  N   . ASN B 2  623  ? -41.481 -17.252  3.081   1.00 116.30 ?  623  ASN B N   1 
ATOM   5944  C  CA  . ASN B 2  623  ? -40.511 -16.965  2.031   1.00 124.80 ?  623  ASN B CA  1 
ATOM   5945  C  C   . ASN B 2  623  ? -39.530 -18.110  1.824   1.00 120.39 ?  623  ASN B C   1 
ATOM   5946  O  O   . ASN B 2  623  ? -39.080 -18.333  0.693   1.00 122.56 ?  623  ASN B O   1 
ATOM   5947  C  CB  . ASN B 2  623  ? -39.754 -15.675  2.355   1.00 123.66 ?  623  ASN B CB  1 
ATOM   5948  C  CG  . ASN B 2  623  ? -39.235 -14.973  1.113   1.00 129.44 ?  623  ASN B CG  1 
ATOM   5949  O  OD1 . ASN B 2  623  ? -38.816 -15.614  0.150   1.00 124.92 ?  623  ASN B OD1 1 
ATOM   5950  N  ND2 . ASN B 2  623  ? -39.264 -13.646  1.131   1.00 142.15 ?  623  ASN B ND2 1 
ATOM   5951  N  N   . ALA B 2  624  ? -39.174 -18.823  2.897   1.00 81.48  ?  624  ALA B N   1 
ATOM   5952  C  CA  . ALA B 2  624  ? -38.232 -19.942  2.870   1.00 80.02  ?  624  ALA B CA  1 
ATOM   5953  C  C   . ALA B 2  624  ? -36.817 -19.499  2.506   1.00 79.63  ?  624  ALA B C   1 
ATOM   5954  O  O   . ALA B 2  624  ? -35.863 -20.269  2.663   1.00 69.35  ?  624  ALA B O   1 
ATOM   5955  C  CB  . ALA B 2  624  ? -38.708 -21.038  1.911   1.00 74.13  ?  624  ALA B CB  1 
ATOM   5956  N  N   . ASP B 2  625  ? -36.668 -18.267  2.022   1.00 91.94  ?  625  ASP B N   1 
ATOM   5957  C  CA  . ASP B 2  625  ? -35.361 -17.680  1.770   1.00 91.03  ?  625  ASP B CA  1 
ATOM   5958  C  C   . ASP B 2  625  ? -34.829 -16.901  2.964   1.00 86.13  ?  625  ASP B C   1 
ATOM   5959  O  O   . ASP B 2  625  ? -33.634 -16.590  2.999   1.00 81.86  ?  625  ASP B O   1 
ATOM   5960  C  CB  . ASP B 2  625  ? -35.419 -16.761  0.545   1.00 98.66  ?  625  ASP B CB  1 
ATOM   5961  C  CG  . ASP B 2  625  ? -35.308 -17.523  -0.762  1.00 105.34 ?  625  ASP B CG  1 
ATOM   5962  O  OD1 . ASP B 2  625  ? -34.970 -18.725  -0.724  1.00 104.82 ?  625  ASP B OD1 1 
ATOM   5963  O  OD2 . ASP B 2  625  ? -35.558 -16.921  -1.827  1.00 108.18 -1 625  ASP B OD2 1 
ATOM   5964  N  N   . ARG B 2  626  ? -35.688 -16.578  3.935   1.00 106.58 ?  626  ARG B N   1 
ATOM   5965  C  CA  . ARG B 2  626  ? -35.238 -15.903  5.146   1.00 114.27 ?  626  ARG B CA  1 
ATOM   5966  C  C   . ARG B 2  626  ? -34.450 -16.830  6.060   1.00 107.69 ?  626  ARG B C   1 
ATOM   5967  O  O   . ARG B 2  626  ? -33.758 -16.350  6.964   1.00 100.17 ?  626  ARG B O   1 
ATOM   5968  C  CB  . ARG B 2  626  ? -36.436 -15.323  5.898   1.00 113.59 ?  626  ARG B CB  1 
ATOM   5969  C  CG  . ARG B 2  626  ? -37.113 -14.167  5.184   1.00 116.20 ?  626  ARG B CG  1 
ATOM   5970  C  CD  . ARG B 2  626  ? -38.088 -13.453  6.103   1.00 108.22 ?  626  ARG B CD  1 
ATOM   5971  N  NE  . ARG B 2  626  ? -37.444 -12.997  7.330   1.00 116.72 ?  626  ARG B NE  1 
ATOM   5972  C  CZ  . ARG B 2  626  ? -38.076 -12.393  8.327   1.00 122.88 ?  626  ARG B CZ  1 
ATOM   5973  N  NH1 . ARG B 2  626  ? -39.376 -12.152  8.276   1.00 118.68 ?  626  ARG B NH1 1 
ATOM   5974  N  NH2 . ARG B 2  626  ? -37.387 -12.023  9.402   1.00 123.79 ?  626  ARG B NH2 1 
ATOM   5975  N  N   . LEU B 2  627  ? -34.544 -18.144  5.848   1.00 100.89 ?  627  LEU B N   1 
ATOM   5976  C  CA  . LEU B 2  627  ? -33.715 -19.083  6.591   1.00 96.21  ?  627  LEU B CA  1 
ATOM   5977  C  C   . LEU B 2  627  ? -32.251 -19.006  6.174   1.00 100.87 ?  627  LEU B C   1 
ATOM   5978  O  O   . LEU B 2  627  ? -31.385 -19.501  6.903   1.00 98.97  ?  627  LEU B O   1 
ATOM   5979  C  CB  . LEU B 2  627  ? -34.246 -20.505  6.404   1.00 90.74  ?  627  LEU B CB  1 
ATOM   5980  C  CG  . LEU B 2  627  ? -35.672 -20.779  6.886   1.00 92.86  ?  627  LEU B CG  1 
ATOM   5981  C  CD1 . LEU B 2  627  ? -36.009 -22.254  6.748   1.00 91.14  ?  627  LEU B CD1 1 
ATOM   5982  C  CD2 . LEU B 2  627  ? -35.843 -20.321  8.325   1.00 91.92  ?  627  LEU B CD2 1 
ATOM   5983  N  N   . ILE B 2  628  ? -31.960 -18.396  5.026   1.00 98.16  ?  628  ILE B N   1 
ATOM   5984  C  CA  . ILE B 2  628  ? -30.587 -18.203  4.574   1.00 90.89  ?  628  ILE B CA  1 
ATOM   5985  C  C   . ILE B 2  628  ? -30.029 -16.937  5.207   1.00 96.54  ?  628  ILE B C   1 
ATOM   5986  O  O   . ILE B 2  628  ? -30.709 -15.905  5.276   1.00 97.40  ?  628  ILE B O   1 
ATOM   5987  C  CB  . ILE B 2  628  ? -30.530 -18.125  3.038   1.00 84.46  ?  628  ILE B CB  1 
ATOM   5988  C  CG1 . ILE B 2  628  ? -31.155 -19.372  2.415   1.00 90.58  ?  628  ILE B CG1 1 
ATOM   5989  C  CG2 . ILE B 2  628  ? -29.095 -17.962  2.564   1.00 81.11  ?  628  ILE B CG2 1 
ATOM   5990  C  CD1 . ILE B 2  628  ? -31.346 -19.279  0.918   1.00 101.66 ?  628  ILE B CD1 1 
ATOM   5991  N  N   . GLY B 2  629  ? -28.788 -17.008  5.673   1.00 78.19  ?  629  GLY B N   1 
ATOM   5992  C  CA  . GLY B 2  629  ? -28.163 -15.844  6.271   1.00 80.15  ?  629  GLY B CA  1 
ATOM   5993  C  C   . GLY B 2  629  ? -26.799 -16.193  6.820   1.00 77.48  ?  629  GLY B C   1 
ATOM   5994  O  O   . GLY B 2  629  ? -26.320 -17.325  6.698   1.00 72.30  ?  629  GLY B O   1 
ATOM   5995  N  N   . THR B 2  630  ? -26.178 -15.192  7.433   1.00 113.62 ?  630  THR B N   1 
ATOM   5996  C  CA  . THR B 2  630  ? -24.853 -15.310  8.013   1.00 124.22 ?  630  THR B CA  1 
ATOM   5997  C  C   . THR B 2  630  ? -24.958 -15.398  9.535   1.00 122.47 ?  630  THR B C   1 
ATOM   5998  O  O   . THR B 2  630  ? -26.045 -15.577  10.099  1.00 119.94 ?  630  THR B O   1 
ATOM   5999  C  CB  . THR B 2  630  ? -23.982 -14.131  7.570   1.00 129.38 ?  630  THR B CB  1 
ATOM   6000  O  OG1 . THR B 2  630  ? -22.646 -14.309  8.055   1.00 131.43 ?  630  THR B OG1 1 
ATOM   6001  C  CG2 . THR B 2  630  ? -24.547 -12.818  8.103   1.00 121.44 ?  630  THR B CG2 1 
ATOM   6002  N  N   . GLU B 2  631  ? -23.811 -15.276  10.205  1.00 118.92 ?  631  GLU B N   1 
ATOM   6003  C  CA  . GLU B 2  631  ? -23.780 -15.324  11.662  1.00 117.89 ?  631  GLU B CA  1 
ATOM   6004  C  C   . GLU B 2  631  ? -24.439 -14.104  12.295  1.00 124.60 ?  631  GLU B C   1 
ATOM   6005  O  O   . GLU B 2  631  ? -24.902 -14.187  13.438  1.00 125.49 ?  631  GLU B O   1 
ATOM   6006  C  CB  . GLU B 2  631  ? -22.331 -15.451  12.140  1.00 118.71 ?  631  GLU B CB  1 
ATOM   6007  C  CG  . GLU B 2  631  ? -22.159 -15.594  13.645  1.00 132.35 ?  631  GLU B CG  1 
ATOM   6008  C  CD  . GLU B 2  631  ? -21.979 -17.035  14.078  1.00 147.38 ?  631  GLU B CD  1 
ATOM   6009  O  OE1 . GLU B 2  631  ? -21.814 -17.906  13.198  1.00 143.63 ?  631  GLU B OE1 1 
ATOM   6010  O  OE2 . GLU B 2  631  ? -22.001 -17.298  15.299  1.00 162.04 -1 631  GLU B OE2 1 
ATOM   6011  N  N   . ALA B 2  632  ? -24.510 -12.982  11.573  1.00 102.58 ?  632  ALA B N   1 
ATOM   6012  C  CA  . ALA B 2  632  ? -25.032 -11.752  12.158  1.00 97.79  ?  632  ALA B CA  1 
ATOM   6013  C  C   . ALA B 2  632  ? -26.521 -11.849  12.471  1.00 97.23  ?  632  ALA B C   1 
ATOM   6014  O  O   . ALA B 2  632  ? -26.999 -11.184  13.397  1.00 97.99  ?  632  ALA B O   1 
ATOM   6015  C  CB  . ALA B 2  632  ? -24.766 -10.573  11.221  1.00 101.18 ?  632  ALA B CB  1 
ATOM   6016  N  N   . ASP B 2  633  ? -27.266 -12.662  11.723  1.00 131.40 ?  633  ASP B N   1 
ATOM   6017  C  CA  . ASP B 2  633  ? -28.709 -12.782  11.897  1.00 129.58 ?  633  ASP B CA  1 
ATOM   6018  C  C   . ASP B 2  633  ? -29.130 -14.222  12.179  1.00 126.50 ?  633  ASP B C   1 
ATOM   6019  O  O   . ASP B 2  633  ? -30.219 -14.647  11.788  1.00 125.65 ?  633  ASP B O   1 
ATOM   6020  C  CB  . ASP B 2  633  ? -29.444 -12.233  10.673  1.00 138.69 ?  633  ASP B CB  1 
ATOM   6021  C  CG  . ASP B 2  633  ? -29.223 -13.075  9.429   1.00 140.88 ?  633  ASP B CG  1 
ATOM   6022  O  OD1 . ASP B 2  633  ? -28.195 -13.781  9.358   1.00 139.18 ?  633  ASP B OD1 1 
ATOM   6023  O  OD2 . ASP B 2  633  ? -30.081 -13.034  8.523   1.00 146.08 -1 633  ASP B OD2 1 
ATOM   6024  N  N   . ASP B 2  634  ? -28.279 -14.980  12.876  1.00 117.04 ?  634  ASP B N   1 
ATOM   6025  C  CA  . ASP B 2  634  ? -28.582 -16.384  13.137  1.00 112.91 ?  634  ASP B CA  1 
ATOM   6026  C  C   . ASP B 2  634  ? -29.803 -16.535  14.036  1.00 108.54 ?  634  ASP B C   1 
ATOM   6027  O  O   . ASP B 2  634  ? -30.670 -17.378  13.777  1.00 102.21 ?  634  ASP B O   1 
ATOM   6028  C  CB  . ASP B 2  634  ? -27.368 -17.073  13.760  1.00 113.69 ?  634  ASP B CB  1 
ATOM   6029  C  CG  . ASP B 2  634  ? -27.627 -18.532  14.084  1.00 120.57 ?  634  ASP B CG  1 
ATOM   6030  O  OD1 . ASP B 2  634  ? -28.414 -19.174  13.357  1.00 118.57 ?  634  ASP B OD1 1 
ATOM   6031  O  OD2 . ASP B 2  634  ? -27.049 -19.035  15.071  1.00 112.01 -1 634  ASP B OD2 1 
ATOM   6032  N  N   . ARG B 2  635  ? -29.890 -15.726  15.096  1.00 102.31 ?  635  ARG B N   1 
ATOM   6033  C  CA  . ARG B 2  635  ? -31.016 -15.833  16.019  1.00 100.82 ?  635  ARG B CA  1 
ATOM   6034  C  C   . ARG B 2  635  ? -32.329 -15.460  15.341  1.00 99.93  ?  635  ARG B C   1 
ATOM   6035  O  O   . ARG B 2  635  ? -33.374 -16.053  15.633  1.00 92.46  ?  635  ARG B O   1 
ATOM   6036  C  CB  . ARG B 2  635  ? -30.776 -14.952  17.245  1.00 101.91 ?  635  ARG B CB  1 
ATOM   6037  C  CG  . ARG B 2  635  ? -29.491 -15.271  17.993  1.00 94.57  ?  635  ARG B CG  1 
ATOM   6038  C  CD  . ARG B 2  635  ? -29.555 -16.650  18.629  1.00 85.77  ?  635  ARG B CD  1 
ATOM   6039  N  NE  . ARG B 2  635  ? -30.697 -16.780  19.526  1.00 87.73  ?  635  ARG B NE  1 
ATOM   6040  C  CZ  . ARG B 2  635  ? -30.679 -16.449  20.810  1.00 85.28  ?  635  ARG B CZ  1 
ATOM   6041  N  NH1 . ARG B 2  635  ? -29.588 -15.973  21.385  1.00 82.54  ?  635  ARG B NH1 1 
ATOM   6042  N  NH2 . ARG B 2  635  ? -31.784 -16.600  21.534  1.00 81.18  ?  635  ARG B NH2 1 
ATOM   6043  N  N   . GLU B 2  636  ? -32.295 -14.481  14.435  1.00 95.45  ?  636  GLU B N   1 
ATOM   6044  C  CA  . GLU B 2  636  ? -33.503 -14.110  13.707  1.00 98.36  ?  636  GLU B CA  1 
ATOM   6045  C  C   . GLU B 2  636  ? -33.952 -15.235  12.782  1.00 97.76  ?  636  GLU B C   1 
ATOM   6046  O  O   . GLU B 2  636  ? -35.155 -15.476  12.625  1.00 96.76  ?  636  GLU B O   1 
ATOM   6047  C  CB  . GLU B 2  636  ? -33.261 -12.819  12.924  1.00 103.23 ?  636  GLU B CB  1 
ATOM   6048  C  CG  . GLU B 2  636  ? -34.357 -12.460  11.933  1.00 110.08 ?  636  GLU B CG  1 
ATOM   6049  C  CD  . GLU B 2  636  ? -33.984 -11.279  11.056  1.00 116.12 ?  636  GLU B CD  1 
ATOM   6050  O  OE1 . GLU B 2  636  ? -32.948 -10.637  11.331  1.00 117.54 ?  636  GLU B OE1 1 
ATOM   6051  O  OE2 . GLU B 2  636  ? -34.727 -10.992  10.093  1.00 114.21 -1 636  GLU B OE2 1 
ATOM   6052  N  N   . ARG B 2  637  ? -32.998 -15.941  12.171  1.00 95.60  ?  637  ARG B N   1 
ATOM   6053  C  CA  . ARG B 2  637  ? -33.343 -17.078  11.324  1.00 91.20  ?  637  ARG B CA  1 
ATOM   6054  C  C   . ARG B 2  637  ? -33.912 -18.226  12.149  1.00 82.42  ?  637  ARG B C   1 
ATOM   6055  O  O   . ARG B 2  637  ? -34.820 -18.933  11.697  1.00 78.66  ?  637  ARG B O   1 
ATOM   6056  C  CB  . ARG B 2  637  ? -32.116 -17.538  10.538  1.00 88.63  ?  637  ARG B CB  1 
ATOM   6057  C  CG  . ARG B 2  637  ? -31.578 -16.503  9.565   1.00 86.29  ?  637  ARG B CG  1 
ATOM   6058  C  CD  . ARG B 2  637  ? -30.457 -17.076  8.722   1.00 85.64  ?  637  ARG B CD  1 
ATOM   6059  N  NE  . ARG B 2  637  ? -29.253 -17.326  9.505   1.00 93.11  ?  637  ARG B NE  1 
ATOM   6060  C  CZ  . ARG B 2  637  ? -28.816 -18.531  9.845   1.00 94.78  ?  637  ARG B CZ  1 
ATOM   6061  N  NH1 . ARG B 2  637  ? -29.467 -19.627  9.491   1.00 93.26  ?  637  ARG B NH1 1 
ATOM   6062  N  NH2 . ARG B 2  637  ? -27.701 -18.639  10.562  1.00 92.17  ?  637  ARG B NH2 1 
ATOM   6063  N  N   . GLN B 2  638  ? -33.388 -18.428  13.361  1.00 77.86  ?  638  GLN B N   1 
ATOM   6064  C  CA  . GLN B 2  638  ? -33.928 -19.465  14.234  1.00 82.19  ?  638  GLN B CA  1 
ATOM   6065  C  C   . GLN B 2  638  ? -35.347 -19.129  14.673  1.00 83.84  ?  638  GLN B C   1 
ATOM   6066  O  O   . GLN B 2  638  ? -36.182 -20.026  14.836  1.00 81.44  ?  638  GLN B O   1 
ATOM   6067  C  CB  . GLN B 2  638  ? -33.024 -19.657  15.452  1.00 84.15  ?  638  GLN B CB  1 
ATOM   6068  C  CG  . GLN B 2  638  ? -31.639 -20.196  15.133  1.00 82.75  ?  638  GLN B CG  1 
ATOM   6069  C  CD  . GLN B 2  638  ? -30.782 -20.364  16.375  1.00 74.03  ?  638  GLN B CD  1 
ATOM   6070  O  OE1 . GLN B 2  638  ? -31.223 -20.085  17.490  1.00 74.98  ?  638  GLN B OE1 1 
ATOM   6071  N  NE2 . GLN B 2  638  ? -29.546 -20.810  16.186  1.00 75.94  ?  638  GLN B NE2 1 
ATOM   6072  N  N   . GLN B 2  639  ? -35.635 -17.840  14.877  1.00 78.38  ?  639  GLN B N   1 
ATOM   6073  C  CA  . GLN B 2  639  ? -36.997 -17.433  15.204  1.00 79.27  ?  639  GLN B CA  1 
ATOM   6074  C  C   . GLN B 2  639  ? -37.936 -17.665  14.027  1.00 82.00  ?  639  GLN B C   1 
ATOM   6075  O  O   . GLN B 2  639  ? -39.090 -18.067  14.216  1.00 79.14  ?  639  GLN B O   1 
ATOM   6076  C  CB  . GLN B 2  639  ? -37.022 -15.964  15.628  1.00 82.55  ?  639  GLN B CB  1 
ATOM   6077  C  CG  . GLN B 2  639  ? -36.344 -15.681  16.958  1.00 89.03  ?  639  GLN B CG  1 
ATOM   6078  C  CD  . GLN B 2  639  ? -36.284 -14.199  17.275  1.00 94.87  ?  639  GLN B CD  1 
ATOM   6079  O  OE1 . GLN B 2  639  ? -36.899 -13.380  16.591  1.00 86.90  ?  639  GLN B OE1 1 
ATOM   6080  N  NE2 . GLN B 2  639  ? -35.538 -13.845  18.316  1.00 98.31  ?  639  GLN B NE2 1 
ATOM   6081  N  N   . TYR B 2  640  ? -37.459 -17.417  12.805  1.00 96.36  ?  640  TYR B N   1 
ATOM   6082  C  CA  . TYR B 2  640  ? -38.286 -17.666  11.629  1.00 93.93  ?  640  TYR B CA  1 
ATOM   6083  C  C   . TYR B 2  640  ? -38.523 -19.156  11.429  1.00 86.99  ?  640  TYR B C   1 
ATOM   6084  O  O   . TYR B 2  640  ? -39.602 -19.563  10.981  1.00 91.05  ?  640  TYR B O   1 
ATOM   6085  C  CB  . TYR B 2  640  ? -37.637 -17.054  10.388  1.00 94.97  ?  640  TYR B CB  1 
ATOM   6086  C  CG  . TYR B 2  640  ? -38.571 -16.952  9.203   1.00 95.94  ?  640  TYR B CG  1 
ATOM   6087  C  CD1 . TYR B 2  640  ? -39.468 -15.898  9.090   1.00 102.99 ?  640  TYR B CD1 1 
ATOM   6088  C  CD2 . TYR B 2  640  ? -38.557 -17.910  8.198   1.00 94.47  ?  640  TYR B CD2 1 
ATOM   6089  C  CE1 . TYR B 2  640  ? -40.324 -15.801  8.009   1.00 109.53 ?  640  TYR B CE1 1 
ATOM   6090  C  CE2 . TYR B 2  640  ? -39.409 -17.822  7.113   1.00 97.55  ?  640  TYR B CE2 1 
ATOM   6091  C  CZ  . TYR B 2  640  ? -40.290 -16.765  7.024   1.00 104.79 ?  640  TYR B CZ  1 
ATOM   6092  O  OH  . TYR B 2  640  ? -41.140 -16.673  5.946   1.00 105.35 ?  640  TYR B OH  1 
ATOM   6093  N  N   . LEU B 2  641  ? -37.527 -19.986  11.750  1.00 74.42  ?  641  LEU B N   1 
ATOM   6094  C  CA  . LEU B 2  641  ? -37.724 -21.429  11.677  1.00 77.99  ?  641  LEU B CA  1 
ATOM   6095  C  C   . LEU B 2  641  ? -38.749 -21.892  12.704  1.00 67.02  ?  641  LEU B C   1 
ATOM   6096  O  O   . LEU B 2  641  ? -39.518 -22.826  12.446  1.00 61.13  ?  641  LEU B O   1 
ATOM   6097  C  CB  . LEU B 2  641  ? -36.393 -22.155  11.878  1.00 78.02  ?  641  LEU B CB  1 
ATOM   6098  C  CG  . LEU B 2  641  ? -36.430 -23.679  11.732  1.00 74.13  ?  641  LEU B CG  1 
ATOM   6099  C  CD1 . LEU B 2  641  ? -36.987 -24.076  10.372  1.00 72.16  ?  641  LEU B CD1 1 
ATOM   6100  C  CD2 . LEU B 2  641  ? -35.050 -24.282  11.948  1.00 75.36  ?  641  LEU B CD2 1 
ATOM   6101  N  N   . GLU B 2  642  ? -38.774 -21.251  13.876  1.00 82.53  ?  642  GLU B N   1 
ATOM   6102  C  CA  . GLU B 2  642  ? -39.807 -21.555  14.860  1.00 80.68  ?  642  GLU B CA  1 
ATOM   6103  C  C   . GLU B 2  642  ? -41.188 -21.197  14.329  1.00 83.59  ?  642  GLU B C   1 
ATOM   6104  O  O   . GLU B 2  642  ? -42.143 -21.966  14.489  1.00 76.79  ?  642  GLU B O   1 
ATOM   6105  C  CB  . GLU B 2  642  ? -39.526 -20.810  16.165  1.00 76.27  ?  642  GLU B CB  1 
ATOM   6106  C  CG  . GLU B 2  642  ? -40.574 -21.038  17.244  1.00 87.43  ?  642  GLU B CG  1 
ATOM   6107  C  CD  . GLU B 2  642  ? -40.259 -20.303  18.531  1.00 94.57  ?  642  GLU B CD  1 
ATOM   6108  O  OE1 . GLU B 2  642  ? -39.156 -19.725  18.635  1.00 98.87  ?  642  GLU B OE1 1 
ATOM   6109  O  OE2 . GLU B 2  642  ? -41.117 -20.299  19.439  1.00 91.22  -1 642  GLU B OE2 1 
ATOM   6110  N  N   . GLN B 2  643  ? -41.311 -20.034  13.686  1.00 87.45  ?  643  GLN B N   1 
ATOM   6111  C  CA  . GLN B 2  643  ? -42.588 -19.642  13.100  1.00 86.05  ?  643  GLN B CA  1 
ATOM   6112  C  C   . GLN B 2  643  ? -42.984 -20.565  11.956  1.00 90.04  ?  643  GLN B C   1 
ATOM   6113  O  O   . GLN B 2  643  ? -44.175 -20.828  11.755  1.00 89.62  ?  643  GLN B O   1 
ATOM   6114  C  CB  . GLN B 2  643  ? -42.517 -18.196  12.611  1.00 94.52  ?  643  GLN B CB  1 
ATOM   6115  C  CG  . GLN B 2  643  ? -42.221 -17.178  13.699  1.00 101.31 ?  643  GLN B CG  1 
ATOM   6116  C  CD  . GLN B 2  643  ? -43.179 -17.278  14.868  1.00 103.94 ?  643  GLN B CD  1 
ATOM   6117  O  OE1 . GLN B 2  643  ? -42.783 -17.626  15.979  1.00 106.30 ?  643  GLN B OE1 1 
ATOM   6118  N  NE2 . GLN B 2  643  ? -44.450 -16.972  14.622  1.00 101.74 ?  643  GLN B NE2 1 
ATOM   6119  N  N   . LEU B 2  644  ? -42.002 -21.064  11.200  1.00 84.03  ?  644  LEU B N   1 
ATOM   6120  C  CA  . LEU B 2  644  ? -42.300 -21.948  10.079  1.00 79.54  ?  644  LEU B CA  1 
ATOM   6121  C  C   . LEU B 2  644  ? -42.706 -23.340  10.549  1.00 72.53  ?  644  LEU B C   1 
ATOM   6122  O  O   . LEU B 2  644  ? -43.479 -24.019  9.865   1.00 62.42  ?  644  LEU B O   1 
ATOM   6123  C  CB  . LEU B 2  644  ? -41.094 -22.030  9.142   1.00 72.67  ?  644  LEU B CB  1 
ATOM   6124  C  CG  . LEU B 2  644  ? -41.232 -22.870  7.871   1.00 68.92  ?  644  LEU B CG  1 
ATOM   6125  C  CD1 . LEU B 2  644  ? -42.473 -22.478  7.092   1.00 65.94  ?  644  LEU B CD1 1 
ATOM   6126  C  CD2 . LEU B 2  644  ? -39.993 -22.717  7.003   1.00 67.74  ?  644  LEU B CD2 1 
ATOM   6127  N  N   . SER B 2  645  ? -42.208 -23.778  11.708  1.00 91.13  ?  645  SER B N   1 
ATOM   6128  C  CA  . SER B 2  645  ? -42.565 -25.093  12.231  1.00 84.74  ?  645  SER B CA  1 
ATOM   6129  C  C   . SER B 2  645  ? -44.027 -25.189  12.645  1.00 84.38  ?  645  SER B C   1 
ATOM   6130  O  O   . SER B 2  645  ? -44.478 -26.278  13.014  1.00 73.11  ?  645  SER B O   1 
ATOM   6131  C  CB  . SER B 2  645  ? -41.669 -25.446  13.418  1.00 73.09  ?  645  SER B CB  1 
ATOM   6132  O  OG  . SER B 2  645  ? -42.151 -24.861  14.616  1.00 83.31  ?  645  SER B OG  1 
ATOM   6133  N  N   . LYS B 2  646  ? -44.775 -24.084  12.598  1.00 88.71  ?  646  LYS B N   1 
ATOM   6134  C  CA  . LYS B 2  646  ? -46.189 -24.107  12.945  1.00 82.43  ?  646  LYS B CA  1 
ATOM   6135  C  C   . LYS B 2  646  ? -47.053 -24.738  11.861  1.00 80.58  ?  646  LYS B C   1 
ATOM   6136  O  O   . LYS B 2  646  ? -48.247 -24.949  12.094  1.00 70.69  ?  646  LYS B O   1 
ATOM   6137  C  CB  . LYS B 2  646  ? -46.679 -22.686  13.234  1.00 71.06  ?  646  LYS B CB  1 
ATOM   6138  C  CG  . LYS B 2  646  ? -46.741 -22.338  14.713  1.00 80.37  ?  646  LYS B CG  1 
ATOM   6139  C  CD  . LYS B 2  646  ? -45.350 -22.179  15.309  1.00 94.61  ?  646  LYS B CD  1 
ATOM   6140  C  CE  . LYS B 2  646  ? -45.365 -21.221  16.491  1.00 104.10 ?  646  LYS B CE  1 
ATOM   6141  N  NZ  . LYS B 2  646  ? -44.153 -21.371  17.343  1.00 99.29  ?  646  LYS B NZ  1 
ATOM   6142  N  N   . VAL B 2  647  ? -46.486 -25.043  10.688  1.00 81.61  ?  647  VAL B N   1 
ATOM   6143  C  CA  . VAL B 2  647  ? -47.255 -25.665  9.614   1.00 85.39  ?  647  VAL B CA  1 
ATOM   6144  C  C   . VAL B 2  647  ? -47.248 -27.184  9.697   1.00 75.13  ?  647  VAL B C   1 
ATOM   6145  O  O   . VAL B 2  647  ? -47.840 -27.844  8.832   1.00 72.09  ?  647  VAL B O   1 
ATOM   6146  C  CB  . VAL B 2  647  ? -46.735 -25.228  8.228   1.00 84.57  ?  647  VAL B CB  1 
ATOM   6147  C  CG1 . VAL B 2  647  ? -46.779 -23.713  8.097   1.00 73.14  ?  647  VAL B CG1 1 
ATOM   6148  C  CG2 . VAL B 2  647  ? -45.331 -25.759  7.989   1.00 74.15  ?  647  VAL B CG2 1 
ATOM   6149  N  N   . ASN B 2  648  ? -46.596 -27.760  10.706  1.00 63.10  ?  648  ASN B N   1 
ATOM   6150  C  CA  . ASN B 2  648  ? -46.589 -29.207  10.873  1.00 59.50  ?  648  ASN B CA  1 
ATOM   6151  C  C   . ASN B 2  648  ? -47.989 -29.709  11.203  1.00 62.21  ?  648  ASN B C   1 
ATOM   6152  O  O   . ASN B 2  648  ? -48.668 -29.161  12.078  1.00 65.67  ?  648  ASN B O   1 
ATOM   6153  C  CB  . ASN B 2  648  ? -45.614 -29.611  11.977  1.00 57.79  ?  648  ASN B CB  1 
ATOM   6154  C  CG  . ASN B 2  648  ? -44.167 -29.556  11.531  1.00 62.69  ?  648  ASN B CG  1 
ATOM   6155  O  OD1 . ASN B 2  648  ? -43.875 -29.505  10.336  1.00 64.38  ?  648  ASN B OD1 1 
ATOM   6156  N  ND2 . ASN B 2  648  ? -43.252 -29.562  12.492  1.00 61.34  ?  648  ASN B ND2 1 
ATOM   6157  N  N   . GLY B 2  649  ? -48.418 -30.756  10.505  1.00 60.48  ?  649  GLY B N   1 
ATOM   6158  C  CA  . GLY B 2  649  ? -49.711 -31.366  10.734  1.00 66.90  ?  649  GLY B CA  1 
ATOM   6159  C  C   . GLY B 2  649  ? -50.707 -31.185  9.612   1.00 72.32  ?  649  GLY B C   1 
ATOM   6160  O  O   . GLY B 2  649  ? -51.755 -31.841  9.630   1.00 79.28  ?  649  GLY B O   1 
ATOM   6161  N  N   . THR B 2  650  ? -50.425 -30.323  8.640   1.00 103.13 ?  650  THR B N   1 
ATOM   6162  C  CA  . THR B 2  650  ? -51.348 -30.123  7.531   1.00 112.51 ?  650  THR B CA  1 
ATOM   6163  C  C   . THR B 2  650  ? -51.433 -31.386  6.684   1.00 111.16 ?  650  THR B C   1 
ATOM   6164  O  O   . THR B 2  650  ? -50.414 -31.919  6.236   1.00 103.92 ?  650  THR B O   1 
ATOM   6165  C  CB  . THR B 2  650  ? -50.904 -28.940  6.675   1.00 110.63 ?  650  THR B CB  1 
ATOM   6166  O  OG1 . THR B 2  650  ? -49.476 -28.942  6.559   1.00 109.43 ?  650  THR B OG1 1 
ATOM   6167  C  CG2 . THR B 2  650  ? -51.350 -27.637  7.308   1.00 115.83 ?  650  THR B CG2 1 
ATOM   6168  N  N   . ILE B 2  651  ? -52.658 -31.869  6.472   1.00 115.60 ?  651  ILE B N   1 
ATOM   6169  C  CA  . ILE B 2  651  ? -52.869 -33.099  5.721   1.00 115.50 ?  651  ILE B CA  1 
ATOM   6170  C  C   . ILE B 2  651  ? -52.651 -32.842  4.236   1.00 115.45 ?  651  ILE B C   1 
ATOM   6171  O  O   . ILE B 2  651  ? -53.086 -31.817  3.692   1.00 117.48 ?  651  ILE B O   1 
ATOM   6172  C  CB  . ILE B 2  651  ? -54.278 -33.651  5.999   1.00 118.85 ?  651  ILE B CB  1 
ATOM   6173  C  CG1 . ILE B 2  651  ? -54.343 -34.267  7.399   1.00 123.94 ?  651  ILE B CG1 1 
ATOM   6174  C  CG2 . ILE B 2  651  ? -54.682 -34.668  4.947   1.00 119.36 ?  651  ILE B CG2 1 
ATOM   6175  C  CD1 . ILE B 2  651  ? -55.557 -35.142  7.633   1.00 129.51 ?  651  ILE B CD1 1 
ATOM   6176  N  N   . ALA B 2  652  ? -51.968 -33.775  3.573   1.00 102.17 ?  652  ALA B N   1 
ATOM   6177  C  CA  . ALA B 2  652  ? -51.667 -33.674  2.151   1.00 105.23 ?  652  ALA B CA  1 
ATOM   6178  C  C   . ALA B 2  652  ? -52.160 -34.920  1.430   1.00 106.57 ?  652  ALA B C   1 
ATOM   6179  O  O   . ALA B 2  652  ? -51.858 -36.043  1.846   1.00 108.42 ?  652  ALA B O   1 
ATOM   6180  C  CB  . ALA B 2  652  ? -50.165 -33.488  1.919   1.00 100.06 ?  652  ALA B CB  1 
ATOM   6181  N  N   . ARG B 2  653  ? -52.904 -34.715  0.342   1.00 90.30  ?  653  ARG B N   1 
ATOM   6182  C  CA  . ARG B 2  653  ? -53.455 -35.798  -0.475  1.00 92.43  ?  653  ARG B CA  1 
ATOM   6183  C  C   . ARG B 2  653  ? -52.454 -36.148  -1.568  1.00 87.11  ?  653  ARG B C   1 
ATOM   6184  O  O   . ARG B 2  653  ? -52.518 -35.633  -2.685  1.00 87.45  ?  653  ARG B O   1 
ATOM   6185  C  CB  . ARG B 2  653  ? -54.791 -35.380  -1.074  1.00 97.59  ?  653  ARG B CB  1 
ATOM   6186  C  CG  . ARG B 2  653  ? -55.491 -36.466  -1.868  1.00 95.74  ?  653  ARG B CG  1 
ATOM   6187  C  CD  . ARG B 2  653  ? -56.383 -35.852  -2.940  1.00 101.46 ?  653  ARG B CD  1 
ATOM   6188  N  NE  . ARG B 2  653  ? -57.542 -36.679  -3.257  1.00 107.46 ?  653  ARG B NE  1 
ATOM   6189  C  CZ  . ARG B 2  653  ? -58.735 -36.549  -2.694  1.00 110.21 ?  653  ARG B CZ  1 
ATOM   6190  N  NH1 . ARG B 2  653  ? -58.963 -35.641  -1.760  1.00 111.40 ?  653  ARG B NH1 1 
ATOM   6191  N  NH2 . ARG B 2  653  ? -59.724 -37.353  -3.075  1.00 108.09 ?  653  ARG B NH2 1 
ATOM   6192  N  N   . ILE B 2  654  ? -51.522 -37.042  -1.249  1.00 79.26  ?  654  ILE B N   1 
ATOM   6193  C  CA  . ILE B 2  654  ? -50.482 -37.430  -2.197  1.00 80.42  ?  654  ILE B CA  1 
ATOM   6194  C  C   . ILE B 2  654  ? -51.058 -38.436  -3.185  1.00 85.09  ?  654  ILE B C   1 
ATOM   6195  O  O   . ILE B 2  654  ? -51.517 -39.514  -2.791  1.00 77.39  ?  654  ILE B O   1 
ATOM   6196  C  CB  . ILE B 2  654  ? -49.257 -38.011  -1.476  1.00 75.97  ?  654  ILE B CB  1 
ATOM   6197  C  CG1 . ILE B 2  654  ? -48.664 -36.984  -0.510  1.00 78.11  ?  654  ILE B CG1 1 
ATOM   6198  C  CG2 . ILE B 2  654  ? -48.217 -38.472  -2.481  1.00 73.34  ?  654  ILE B CG2 1 
ATOM   6199  C  CD1 . ILE B 2  654  ? -47.423 -37.463  0.206   1.00 67.72  ?  654  ILE B CD1 1 
ATOM   6200  N  N   . GLU B 2  655  ? -51.035 -38.086  -4.468  1.00 78.69  ?  655  GLU B N   1 
ATOM   6201  C  CA  . GLU B 2  655  ? -51.462 -38.973  -5.543  1.00 75.45  ?  655  GLU B CA  1 
ATOM   6202  C  C   . GLU B 2  655  ? -50.229 -39.459  -6.291  1.00 74.27  ?  655  GLU B C   1 
ATOM   6203  O  O   . GLU B 2  655  ? -49.535 -38.664  -6.934  1.00 72.84  ?  655  GLU B O   1 
ATOM   6204  C  CB  . GLU B 2  655  ? -52.430 -38.267  -6.492  1.00 84.22  ?  655  GLU B CB  1 
ATOM   6205  C  CG  . GLU B 2  655  ? -53.199 -39.215  -7.396  1.00 97.59  ?  655  GLU B CG  1 
ATOM   6206  C  CD  . GLU B 2  655  ? -54.359 -38.542  -8.101  1.00 106.70 ?  655  GLU B CD  1 
ATOM   6207  O  OE1 . GLU B 2  655  ? -54.585 -37.337  -7.860  1.00 112.19 ?  655  GLU B OE1 1 
ATOM   6208  O  OE2 . GLU B 2  655  ? -55.048 -39.220  -8.892  1.00 111.67 ?  655  GLU B OE2 1 
ATOM   6209  N  N   . TYR B 2  656  ? -49.963 -40.763  -6.211  1.00 100.17 ?  656  TYR B N   1 
ATOM   6210  C  CA  . TYR B 2  656  ? -48.741 -41.332  -6.766  1.00 108.03 ?  656  TYR B CA  1 
ATOM   6211  C  C   . TYR B 2  656  ? -49.029 -42.045  -8.081  1.00 116.43 ?  656  TYR B C   1 
ATOM   6212  O  O   . TYR B 2  656  ? -48.714 -41.524  -9.156  1.00 116.62 ?  656  TYR B O   1 
ATOM   6213  C  CB  . TYR B 2  656  ? -48.103 -42.284  -5.751  1.00 99.92  ?  656  TYR B CB  1 
ATOM   6214  C  CG  . TYR B 2  656  ? -46.815 -42.935  -6.200  1.00 95.64  ?  656  TYR B CG  1 
ATOM   6215  C  CD1 . TYR B 2  656  ? -45.797 -42.189  -6.778  1.00 95.00  ?  656  TYR B CD1 1 
ATOM   6216  C  CD2 . TYR B 2  656  ? -46.608 -44.294  -6.022  1.00 94.18  ?  656  TYR B CD2 1 
ATOM   6217  C  CE1 . TYR B 2  656  ? -44.615 -42.787  -7.179  1.00 91.97  ?  656  TYR B CE1 1 
ATOM   6218  C  CE2 . TYR B 2  656  ? -45.433 -44.900  -6.417  1.00 98.66  ?  656  TYR B CE2 1 
ATOM   6219  C  CZ  . TYR B 2  656  ? -44.439 -44.143  -6.995  1.00 95.18  ?  656  TYR B CZ  1 
ATOM   6220  O  OH  . TYR B 2  656  ? -43.268 -44.749  -7.388  1.00 95.98  ?  656  TYR B OH  1 
ATOM   6221  N  N   . ARG B 2  657  ? -49.638 -43.237  -8.008  1.00 106.12 ?  657  ARG B N   1 
ATOM   6222  C  CA  . ARG B 2  657  ? -50.013 -44.007  -9.192  1.00 106.71 ?  657  ARG B CA  1 
ATOM   6223  C  C   . ARG B 2  657  ? -51.408 -44.595  -8.961  1.00 113.59 ?  657  ARG B C   1 
ATOM   6224  O  O   . ARG B 2  657  ? -51.587 -45.789  -8.720  1.00 114.27 ?  657  ARG B O   1 
ATOM   6225  C  CB  . ARG B 2  657  ? -48.979 -45.090  -9.508  1.00 97.80  ?  657  ARG B CB  1 
ATOM   6226  C  CG  . ARG B 2  657  ? -47.738 -44.547  -10.200 1.00 92.69  ?  657  ARG B CG  1 
ATOM   6227  C  CD  . ARG B 2  657  ? -46.532 -45.457  -10.040 1.00 94.25  ?  657  ARG B CD  1 
ATOM   6228  N  NE  . ARG B 2  657  ? -45.368 -44.905  -10.724 1.00 99.88  ?  657  ARG B NE  1 
ATOM   6229  C  CZ  . ARG B 2  657  ? -44.141 -45.401  -10.646 1.00 96.99  ?  657  ARG B CZ  1 
ATOM   6230  N  NH1 . ARG B 2  657  ? -43.875 -46.476  -9.923  1.00 95.84  ?  657  ARG B NH1 1 
ATOM   6231  N  NH2 . ARG B 2  657  ? -43.156 -44.801  -11.308 1.00 91.41  ?  657  ARG B NH2 1 
ATOM   6232  N  N   . GLY B 2  658  ? -52.417 -43.730  -9.044  1.00 130.74 ?  658  GLY B N   1 
ATOM   6233  C  CA  . GLY B 2  658  ? -53.794 -44.129  -8.846  1.00 126.47 ?  658  GLY B CA  1 
ATOM   6234  C  C   . GLY B 2  658  ? -54.227 -44.215  -7.403  1.00 129.11 ?  658  GLY B C   1 
ATOM   6235  O  O   . GLY B 2  658  ? -55.333 -44.698  -7.134  1.00 129.01 ?  658  GLY B O   1 
ATOM   6236  N  N   . GLY B 2  659  ? -53.400 -43.764  -6.474  1.00 86.17  ?  659  GLY B N   1 
ATOM   6237  C  CA  . GLY B 2  659  ? -53.709 -43.871  -5.057  1.00 79.21  ?  659  GLY B CA  1 
ATOM   6238  C  C   . GLY B 2  659  ? -53.625 -42.524  -4.376  1.00 74.30  ?  659  GLY B C   1 
ATOM   6239  O  O   . GLY B 2  659  ? -52.769 -41.707  -4.703  1.00 75.71  ?  659  GLY B O   1 
ATOM   6240  N  N   . ILE B 2  660  ? -54.537 -42.296  -3.434  1.00 100.98 ?  660  ILE B N   1 
ATOM   6241  C  CA  . ILE B 2  660  ? -54.508 -41.126  -2.562  1.00 108.58 ?  660  ILE B CA  1 
ATOM   6242  C  C   . ILE B 2  660  ? -54.234 -41.591  -1.135  1.00 111.21 ?  660  ILE B C   1 
ATOM   6243  O  O   . ILE B 2  660  ? -54.916 -42.483  -0.624  1.00 116.42 ?  660  ILE B O   1 
ATOM   6244  C  CB  . ILE B 2  660  ? -55.817 -40.324  -2.649  1.00 110.87 ?  660  ILE B CB  1 
ATOM   6245  C  CG1 . ILE B 2  660  ? -57.025 -41.244  -2.444  1.00 113.57 ?  660  ILE B CG1 1 
ATOM   6246  C  CG2 . ILE B 2  660  ? -55.913 -39.626  -3.997  1.00 111.29 ?  660  ILE B CG2 1 
ATOM   6247  C  CD1 . ILE B 2  660  ? -58.338 -40.512  -2.348  1.00 104.55 ?  660  ILE B CD1 1 
ATOM   6248  N  N   . ILE B 2  661  ? -53.236 -40.991  -0.489  1.00 105.06 ?  661  ILE B N   1 
ATOM   6249  C  CA  . ILE B 2  661  ? -52.792 -41.432  0.829   1.00 106.85 ?  661  ILE B CA  1 
ATOM   6250  C  C   . ILE B 2  661  ? -53.264 -40.520  1.961   1.00 114.37 ?  661  ILE B C   1 
ATOM   6251  O  O   . ILE B 2  661  ? -53.524 -41.014  3.064   1.00 112.83 ?  661  ILE B O   1 
ATOM   6252  C  CB  . ILE B 2  661  ? -51.253 -41.601  0.873   1.00 97.43  ?  661  ILE B CB  1 
ATOM   6253  C  CG1 . ILE B 2  661  ? -50.824 -42.471  2.059   1.00 95.34  ?  661  ILE B CG1 1 
ATOM   6254  C  CG2 . ILE B 2  661  ? -50.542 -40.282  0.918   1.00 100.39 ?  661  ILE B CG2 1 
ATOM   6255  C  CD1 . ILE B 2  661  ? -49.327 -42.515  2.268   1.00 95.58  ?  661  ILE B CD1 1 
ATOM   6256  N  N   . GLU B 2  662  ? -53.371 -39.214  1.734   1.00 115.46 ?  662  GLU B N   1 
ATOM   6257  C  CA  . GLU B 2  662  ? -53.887 -38.269  2.725   1.00 117.64 ?  662  GLU B CA  1 
ATOM   6258  C  C   . GLU B 2  662  ? -53.189 -38.424  4.079   1.00 108.96 ?  662  GLU B C   1 
ATOM   6259  O  O   . GLU B 2  662  ? -53.807 -38.734  5.102   1.00 108.49 ?  662  GLU B O   1 
ATOM   6260  C  CB  . GLU B 2  662  ? -55.401 -38.412  2.872   1.00 127.55 ?  662  GLU B CB  1 
ATOM   6261  C  CG  . GLU B 2  662  ? -56.177 -37.926  1.652   1.00 133.23 ?  662  GLU B CG  1 
ATOM   6262  C  CD  . GLU B 2  662  ? -57.629 -37.578  1.958   1.00 131.81 ?  662  GLU B CD  1 
ATOM   6263  O  OE1 . GLU B 2  662  ? -58.036 -37.653  3.143   1.00 119.17 ?  662  GLU B OE1 1 
ATOM   6264  O  OE2 . GLU B 2  662  ? -58.372 -37.253  1.007   1.00 133.24 -1 662  GLU B OE2 1 
ATOM   6265  N  N   . ILE B 2  663  ? -51.889 -38.143  4.081   1.00 81.40  ?  663  ILE B N   1 
ATOM   6266  C  CA  . ILE B 2  663  ? -51.044 -38.299  5.264   1.00 77.19  ?  663  ILE B CA  1 
ATOM   6267  C  C   . ILE B 2  663  ? -50.593 -36.913  5.710   1.00 78.95  ?  663  ILE B C   1 
ATOM   6268  O  O   . ILE B 2  663  ? -50.322 -36.048  4.864   1.00 81.32  ?  663  ILE B O   1 
ATOM   6269  C  CB  . ILE B 2  663  ? -49.855 -39.232  4.970   1.00 71.66  ?  663  ILE B CB  1 
ATOM   6270  C  CG1 . ILE B 2  663  ? -49.084 -39.555  6.252   1.00 66.89  ?  663  ILE B CG1 1 
ATOM   6271  C  CG2 . ILE B 2  663  ? -48.944 -38.638  3.905   1.00 66.84  ?  663  ILE B CG2 1 
ATOM   6272  C  CD1 . ILE B 2  663  ? -48.026 -40.616  6.080   1.00 66.91  ?  663  ILE B CD1 1 
ATOM   6273  N  N   . PRO B 2  664  ? -50.546 -36.640  7.010   1.00 68.54  ?  664  PRO B N   1 
ATOM   6274  C  CA  . PRO B 2  664  ? -50.050 -35.341  7.473   1.00 61.10  ?  664  PRO B CA  1 
ATOM   6275  C  C   . PRO B 2  664  ? -48.574 -35.157  7.152   1.00 56.06  ?  664  PRO B C   1 
ATOM   6276  O  O   . PRO B 2  664  ? -47.813 -36.115  6.999   1.00 54.81  ?  664  PRO B O   1 
ATOM   6277  C  CB  . PRO B 2  664  ? -50.292 -35.389  8.986   1.00 64.42  ?  664  PRO B CB  1 
ATOM   6278  C  CG  . PRO B 2  664  ? -50.401 -36.854  9.307   1.00 64.53  ?  664  PRO B CG  1 
ATOM   6279  C  CD  . PRO B 2  664  ? -51.086 -37.444  8.117   1.00 68.86  ?  664  PRO B CD  1 
ATOM   6280  N  N   . ILE B 2  665  ? -48.172 -33.893  7.058   1.00 61.20  ?  665  ILE B N   1 
ATOM   6281  C  CA  . ILE B 2  665  ? -46.817 -33.544  6.668   1.00 60.60  ?  665  ILE B CA  1 
ATOM   6282  C  C   . ILE B 2  665  ? -46.004 -33.198  7.906   1.00 53.63  ?  665  ILE B C   1 
ATOM   6283  O  O   . ILE B 2  665  ? -46.537 -32.858  8.967   1.00 50.20  ?  665  ILE B O   1 
ATOM   6284  C  CB  . ILE B 2  665  ? -46.779 -32.375  5.655   1.00 63.14  ?  665  ILE B CB  1 
ATOM   6285  C  CG1 . ILE B 2  665  ? -46.986 -31.041  6.377   1.00 66.49  ?  665  ILE B CG1 1 
ATOM   6286  C  CG2 . ILE B 2  665  ? -47.805 -32.580  4.553   1.00 61.48  ?  665  ILE B CG2 1 
ATOM   6287  C  CD1 . ILE B 2  665  ? -46.585 -29.829  5.559   1.00 73.86  ?  665  ILE B CD1 1 
ATOM   6288  N  N   . TRP B 2  666  ? -44.683 -33.278  7.758   1.00 65.97  ?  666  TRP B N   1 
ATOM   6289  C  CA  . TRP B 2  666  ? -43.732 -32.867  8.779   1.00 68.16  ?  666  TRP B CA  1 
ATOM   6290  C  C   . TRP B 2  666  ? -42.524 -32.245  8.097   1.00 64.24  ?  666  TRP B C   1 
ATOM   6291  O  O   . TRP B 2  666  ? -42.157 -32.631  6.984   1.00 69.28  ?  666  TRP B O   1 
ATOM   6292  C  CB  . TRP B 2  666  ? -43.291 -34.043  9.658   1.00 66.68  ?  666  TRP B CB  1 
ATOM   6293  C  CG  . TRP B 2  666  ? -42.483 -33.627  10.852  1.00 68.09  ?  666  TRP B CG  1 
ATOM   6294  C  CD1 . TRP B 2  666  ? -41.123 -33.604  10.954  1.00 68.90  ?  666  TRP B CD1 1 
ATOM   6295  C  CD2 . TRP B 2  666  ? -42.986 -33.171  12.113  1.00 61.67  ?  666  TRP B CD2 1 
ATOM   6296  N  NE1 . TRP B 2  666  ? -40.747 -33.166  12.201  1.00 56.53  ?  666  TRP B NE1 1 
ATOM   6297  C  CE2 . TRP B 2  666  ? -41.874 -32.893  12.932  1.00 61.79  ?  666  TRP B CE2 1 
ATOM   6298  C  CE3 . TRP B 2  666  ? -44.270 -32.972  12.629  1.00 61.08  ?  666  TRP B CE3 1 
ATOM   6299  C  CZ2 . TRP B 2  666  ? -42.007 -32.427  14.239  1.00 67.15  ?  666  TRP B CZ2 1 
ATOM   6300  C  CZ3 . TRP B 2  666  ? -44.400 -32.510  13.923  1.00 67.70  ?  666  TRP B CZ3 1 
ATOM   6301  C  CH2 . TRP B 2  666  ? -43.275 -32.243  14.714  1.00 68.85  ?  666  TRP B CH2 1 
ATOM   6302  N  N   . LEU B 2  667  ? -41.908 -31.279  8.773   1.00 53.26  ?  667  LEU B N   1 
ATOM   6303  C  CA  . LEU B 2  667  ? -40.797 -30.521  8.212   1.00 59.57  ?  667  LEU B CA  1 
ATOM   6304  C  C   . LEU B 2  667  ? -39.472 -31.118  8.672   1.00 59.07  ?  667  LEU B C   1 
ATOM   6305  O  O   . LEU B 2  667  ? -39.164 -31.119  9.869   1.00 60.48  ?  667  LEU B O   1 
ATOM   6306  C  CB  . LEU B 2  667  ? -40.888 -29.045  8.600   1.00 53.14  ?  667  LEU B CB  1 
ATOM   6307  C  CG  . LEU B 2  667  ? -41.915 -28.231  7.810   1.00 58.17  ?  667  LEU B CG  1 
ATOM   6308  C  CD1 . LEU B 2  667  ? -41.732 -26.740  8.048   1.00 67.41  ?  667  LEU B CD1 1 
ATOM   6309  C  CD2 . LEU B 2  667  ? -41.821 -28.556  6.329   1.00 63.51  ?  667  LEU B CD2 1 
ATOM   6310  N  N   . LEU B 2  668  ? -38.698 -31.619  7.717   1.00 58.22  ?  668  LEU B N   1 
ATOM   6311  C  CA  . LEU B 2  668  ? -37.350 -32.127  7.963   1.00 51.63  ?  668  LEU B CA  1 
ATOM   6312  C  C   . LEU B 2  668  ? -36.372 -31.293  7.154   1.00 55.26  ?  668  LEU B C   1 
ATOM   6313  O  O   . LEU B 2  668  ? -36.331 -31.426  5.916   1.00 60.03  ?  668  LEU B O   1 
ATOM   6314  C  CB  . LEU B 2  668  ? -37.250 -33.603  7.583   1.00 56.78  ?  668  LEU B CB  1 
ATOM   6315  C  CG  . LEU B 2  668  ? -35.938 -34.325  7.892   1.00 48.91  ?  668  LEU B CG  1 
ATOM   6316  C  CD1 . LEU B 2  668  ? -35.479 -34.039  9.311   1.00 58.42  ?  668  LEU B CD1 1 
ATOM   6317  C  CD2 . LEU B 2  668  ? -36.106 -35.823  7.677   1.00 51.28  ?  668  LEU B CD2 1 
ATOM   6318  N  N   . PRO B 2  669  ? -35.578 -30.426  7.790   1.00 68.77  ?  669  PRO B N   1 
ATOM   6319  C  CA  . PRO B 2  669  ? -34.794 -29.447  7.016   1.00 77.22  ?  669  PRO B CA  1 
ATOM   6320  C  C   . PRO B 2  669  ? -33.832 -30.065  6.018   1.00 83.04  ?  669  PRO B C   1 
ATOM   6321  O  O   . PRO B 2  669  ? -33.719 -29.566  4.892   1.00 86.20  ?  669  PRO B O   1 
ATOM   6322  C  CB  . PRO B 2  669  ? -34.057 -28.670  8.112   1.00 61.07  ?  669  PRO B CB  1 
ATOM   6323  C  CG  . PRO B 2  669  ? -34.997 -28.728  9.272   1.00 63.80  ?  669  PRO B CG  1 
ATOM   6324  C  CD  . PRO B 2  669  ? -35.529 -30.140  9.234   1.00 70.33  ?  669  PRO B CD  1 
ATOM   6325  N  N   . GLY B 2  670  ? -33.146 -31.146  6.386   1.00 69.48  ?  670  GLY B N   1 
ATOM   6326  C  CA  . GLY B 2  670  ? -32.121 -31.704  5.521   1.00 75.75  ?  670  GLY B CA  1 
ATOM   6327  C  C   . GLY B 2  670  ? -32.635 -32.378  4.265   1.00 64.88  ?  670  GLY B C   1 
ATOM   6328  O  O   . GLY B 2  670  ? -31.818 -32.801  3.439   1.00 57.94  ?  670  GLY B O   1 
ATOM   6329  N  N   . HIS B 2  671  ? -33.952 -32.489  4.102   1.00 80.14  ?  671  HIS B N   1 
ATOM   6330  C  CA  . HIS B 2  671  ? -34.511 -33.216  2.970   1.00 74.82  ?  671  HIS B CA  1 
ATOM   6331  C  C   . HIS B 2  671  ? -34.183 -32.520  1.655   1.00 84.42  ?  671  HIS B C   1 
ATOM   6332  O  O   . HIS B 2  671  ? -34.105 -31.291  1.579   1.00 87.38  ?  671  HIS B O   1 
ATOM   6333  C  CB  . HIS B 2  671  ? -36.026 -33.348  3.122   1.00 72.89  ?  671  HIS B CB  1 
ATOM   6334  C  CG  . HIS B 2  671  ? -36.574 -34.638  2.600   1.00 84.20  ?  671  HIS B CG  1 
ATOM   6335  N  ND1 . HIS B 2  671  ? -36.335 -35.080  1.317   1.00 88.40  ?  671  HIS B ND1 1 
ATOM   6336  C  CD2 . HIS B 2  671  ? -37.353 -35.579  3.184   1.00 84.55  ?  671  HIS B CD2 1 
ATOM   6337  C  CE1 . HIS B 2  671  ? -36.943 -36.237  1.132   1.00 84.29  ?  671  HIS B CE1 1 
ATOM   6338  N  NE2 . HIS B 2  671  ? -37.567 -36.562  2.249   1.00 79.90  ?  671  HIS B NE2 1 
ATOM   6339  N  N   . ALA B 2  672  ? -33.990 -33.324  0.613   1.00 77.13  ?  672  ALA B N   1 
ATOM   6340  C  CA  . ALA B 2  672  ? -33.786 -32.781  -0.721  1.00 78.46  ?  672  ALA B CA  1 
ATOM   6341  C  C   . ALA B 2  672  ? -35.086 -32.196  -1.260  1.00 84.58  ?  672  ALA B C   1 
ATOM   6342  O  O   . ALA B 2  672  ? -36.179 -32.700  -0.987  1.00 82.49  ?  672  ALA B O   1 
ATOM   6343  C  CB  . ALA B 2  672  ? -33.265 -33.863  -1.665  1.00 73.22  ?  672  ALA B CB  1 
ATOM   6344  N  N   . GLU B 2  673  ? -34.957 -31.122  -2.035  1.00 83.98  ?  673  GLU B N   1 
ATOM   6345  C  CA  . GLU B 2  673  ? -36.129 -30.435  -2.556  1.00 84.22  ?  673  GLU B CA  1 
ATOM   6346  C  C   . GLU B 2  673  ? -36.837 -31.296  -3.596  1.00 91.59  ?  673  GLU B C   1 
ATOM   6347  O  O   . GLU B 2  673  ? -36.219 -32.113  -4.285  1.00 85.83  ?  673  GLU B O   1 
ATOM   6348  C  CB  . GLU B 2  673  ? -35.732 -29.087  -3.158  1.00 88.64  ?  673  GLU B CB  1 
ATOM   6349  C  CG  . GLU B 2  673  ? -36.907 -28.165  -3.436  1.00 100.25 ?  673  GLU B CG  1 
ATOM   6350  C  CD  . GLU B 2  673  ? -36.486 -26.853  -4.070  1.00 106.58 ?  673  GLU B CD  1 
ATOM   6351  O  OE1 . GLU B 2  673  ? -35.269 -26.585  -4.139  1.00 100.25 ?  673  GLU B OE1 1 
ATOM   6352  O  OE2 . GLU B 2  673  ? -37.374 -26.083  -4.491  1.00 111.50 -1 673  GLU B OE2 1 
ATOM   6353  N  N   . ASP B 2  674  ? -38.157 -31.112  -3.684  1.00 107.39 ?  674  ASP B N   1 
ATOM   6354  C  CA  . ASP B 2  674  ? -39.021 -31.855  -4.602  1.00 104.69 ?  674  ASP B CA  1 
ATOM   6355  C  C   . ASP B 2  674  ? -39.015 -33.351  -4.307  1.00 106.19 ?  674  ASP B C   1 
ATOM   6356  O  O   . ASP B 2  674  ? -39.227 -34.170  -5.203  1.00 112.89 ?  674  ASP B O   1 
ATOM   6357  C  CB  . ASP B 2  674  ? -38.639 -31.597  -6.063  1.00 107.35 ?  674  ASP B CB  1 
ATOM   6358  C  CG  . ASP B 2  674  ? -38.984 -30.193  -6.515  1.00 117.36 ?  674  ASP B CG  1 
ATOM   6359  O  OD1 . ASP B 2  674  ? -39.671 -29.476  -5.759  1.00 115.80 ?  674  ASP B OD1 1 
ATOM   6360  O  OD2 . ASP B 2  674  ? -38.555 -29.799  -7.619  1.00 129.47 -1 674  ASP B OD2 1 
ATOM   6361  N  N   . SER B 2  675  ? -38.776 -33.718  -3.049  1.00 91.10  ?  675  SER B N   1 
ATOM   6362  C  CA  . SER B 2  675  ? -38.798 -35.109  -2.624  1.00 84.31  ?  675  SER B CA  1 
ATOM   6363  C  C   . SER B 2  675  ? -39.528 -35.213  -1.294  1.00 81.92  ?  675  SER B C   1 
ATOM   6364  O  O   . SER B 2  675  ? -39.327 -34.386  -0.398  1.00 79.53  ?  675  SER B O   1 
ATOM   6365  C  CB  . SER B 2  675  ? -37.380 -35.679  -2.495  1.00 87.28  ?  675  SER B CB  1 
ATOM   6366  O  OG  . SER B 2  675  ? -37.407 -37.006  -2.000  1.00 86.83  ?  675  SER B OG  1 
ATOM   6367  N  N   . ILE B 2  676  ? -40.381 -36.226  -1.177  1.00 71.48  ?  676  ILE B N   1 
ATOM   6368  C  CA  . ILE B 2  676  ? -41.166 -36.477  0.025   1.00 65.36  ?  676  ILE B CA  1 
ATOM   6369  C  C   . ILE B 2  676  ? -40.870 -37.893  0.493   1.00 65.54  ?  676  ILE B C   1 
ATOM   6370  O  O   . ILE B 2  676  ? -40.964 -38.843  -0.292  1.00 67.79  ?  676  ILE B O   1 
ATOM   6371  C  CB  . ILE B 2  676  ? -42.673 -36.290  -0.228  1.00 60.33  ?  676  ILE B CB  1 
ATOM   6372  C  CG1 . ILE B 2  676  ? -42.961 -34.864  -0.694  1.00 55.74  ?  676  ILE B CG1 1 
ATOM   6373  C  CG2 . ILE B 2  676  ? -43.469 -36.613  1.018   1.00 62.41  ?  676  ILE B CG2 1 
ATOM   6374  C  CD1 . ILE B 2  676  ? -44.393 -34.640  -1.112  1.00 67.31  ?  676  ILE B CD1 1 
ATOM   6375  N  N   . THR B 2  677  ? -40.510 -38.030  1.766   1.00 74.07  ?  677  THR B N   1 
ATOM   6376  C  CA  . THR B 2  677  ? -40.191 -39.324  2.354   1.00 72.15  ?  677  THR B CA  1 
ATOM   6377  C  C   . THR B 2  677  ? -41.387 -39.846  3.133   1.00 66.90  ?  677  THR B C   1 
ATOM   6378  O  O   . THR B 2  677  ? -41.920 -39.152  4.005   1.00 64.36  ?  677  THR B O   1 
ATOM   6379  C  CB  . THR B 2  677  ? -38.974 -39.234  3.272   1.00 71.12  ?  677  THR B CB  1 
ATOM   6380  O  OG1 . THR B 2  677  ? -37.818 -38.914  2.491   1.00 80.22  ?  677  THR B OG1 1 
ATOM   6381  C  CG2 . THR B 2  677  ? -38.746 -40.557  3.982   1.00 66.79  ?  677  THR B CG2 1 
ATOM   6382  N  N   . LEU B 2  678  ? -41.804 -41.065  2.809   1.00 78.58  ?  678  LEU B N   1 
ATOM   6383  C  CA  . LEU B 2  678  ? -42.912 -41.735  3.470   1.00 78.84  ?  678  LEU B CA  1 
ATOM   6384  C  C   . LEU B 2  678  ? -42.371 -42.970  4.172   1.00 78.40  ?  678  LEU B C   1 
ATOM   6385  O  O   . LEU B 2  678  ? -41.673 -43.781  3.552   1.00 77.05  ?  678  LEU B O   1 
ATOM   6386  C  CB  . LEU B 2  678  ? -44.004 -42.114  2.463   1.00 80.51  ?  678  LEU B CB  1 
ATOM   6387  C  CG  . LEU B 2  678  ? -44.901 -40.967  1.986   1.00 75.09  ?  678  LEU B CG  1 
ATOM   6388  C  CD1 . LEU B 2  678  ? -45.846 -41.423  0.889   1.00 81.86  ?  678  LEU B CD1 1 
ATOM   6389  C  CD2 . LEU B 2  678  ? -45.681 -40.380  3.150   1.00 80.05  ?  678  LEU B CD2 1 
ATOM   6390  N  N   . ASN B 2  679  ? -42.682 -43.108  5.460   1.00 71.50  ?  679  ASN B N   1 
ATOM   6391  C  CA  . ASN B 2  679  ? -42.124 -44.168  6.289   1.00 67.84  ?  679  ASN B CA  1 
ATOM   6392  C  C   . ASN B 2  679  ? -43.075 -45.358  6.335   1.00 61.86  ?  679  ASN B C   1 
ATOM   6393  O  O   . ASN B 2  679  ? -44.280 -45.194  6.563   1.00 66.86  ?  679  ASN B O   1 
ATOM   6394  C  CB  . ASN B 2  679  ? -41.831 -43.659  7.700   1.00 61.00  ?  679  ASN B CB  1 
ATOM   6395  C  CG  . ASN B 2  679  ? -40.623 -42.746  7.745   1.00 57.72  ?  679  ASN B CG  1 
ATOM   6396  O  OD1 . ASN B 2  679  ? -39.777 -42.772  6.850   1.00 55.66  ?  679  ASN B OD1 1 
ATOM   6397  N  ND2 . ASN B 2  679  ? -40.541 -41.922  8.782   1.00 62.07  ?  679  ASN B ND2 1 
ATOM   6398  N  N   . LEU B 2  680  ? -42.525 -46.549  6.118   1.00 70.55  ?  680  LEU B N   1 
ATOM   6399  C  CA  . LEU B 2  680  ? -43.301 -47.775  6.051   1.00 80.72  ?  680  LEU B CA  1 
ATOM   6400  C  C   . LEU B 2  680  ? -43.596 -48.313  7.449   1.00 76.33  ?  680  LEU B C   1 
ATOM   6401  O  O   . LEU B 2  680  ? -42.977 -47.920  8.442   1.00 81.21  ?  680  LEU B O   1 
ATOM   6402  C  CB  . LEU B 2  680  ? -42.554 -48.832  5.234   1.00 86.32  ?  680  LEU B CB  1 
ATOM   6403  C  CG  . LEU B 2  680  ? -42.131 -48.449  3.813   1.00 84.43  ?  680  LEU B CG  1 
ATOM   6404  C  CD1 . LEU B 2  680  ? -41.096 -49.422  3.278   1.00 80.32  ?  680  LEU B CD1 1 
ATOM   6405  C  CD2 . LEU B 2  680  ? -43.336 -48.391  2.890   1.00 91.09  ?  680  LEU B CD2 1 
ATOM   6406  N  N   . GLY B 2  681  ? -44.560 -49.225  7.514   1.00 54.56  ?  681  GLY B N   1 
ATOM   6407  C  CA  . GLY B 2  681  ? -44.861 -49.940  8.735   1.00 58.55  ?  681  GLY B CA  1 
ATOM   6408  C  C   . GLY B 2  681  ? -45.992 -49.381  9.570   1.00 61.59  ?  681  GLY B C   1 
ATOM   6409  O  O   . GLY B 2  681  ? -45.997 -49.595  10.788  1.00 64.74  ?  681  GLY B O   1 
ATOM   6410  N  N   . TYR B 2  682  ? -46.944 -48.677  8.966   1.00 81.03  ?  682  TYR B N   1 
ATOM   6411  C  CA  . TYR B 2  682  ? -48.050 -48.075  9.693   1.00 82.61  ?  682  TYR B CA  1 
ATOM   6412  C  C   . TYR B 2  682  ? -49.369 -48.463  9.038   1.00 89.72  ?  682  TYR B C   1 
ATOM   6413  O  O   . TYR B 2  682  ? -49.406 -49.019  7.938   1.00 91.22  ?  682  TYR B O   1 
ATOM   6414  C  CB  . TYR B 2  682  ? -47.915 -46.548  9.747   1.00 85.03  ?  682  TYR B CB  1 
ATOM   6415  C  CG  . TYR B 2  682  ? -46.789 -46.060  10.629  1.00 85.86  ?  682  TYR B CG  1 
ATOM   6416  C  CD1 . TYR B 2  682  ? -45.512 -45.877  10.119  1.00 79.33  ?  682  TYR B CD1 1 
ATOM   6417  C  CD2 . TYR B 2  682  ? -47.007 -45.768  11.970  1.00 88.73  ?  682  TYR B CD2 1 
ATOM   6418  C  CE1 . TYR B 2  682  ? -44.480 -45.427  10.920  1.00 79.41  ?  682  TYR B CE1 1 
ATOM   6419  C  CE2 . TYR B 2  682  ? -45.981 -45.316  12.781  1.00 83.83  ?  682  TYR B CE2 1 
ATOM   6420  C  CZ  . TYR B 2  682  ? -44.720 -45.147  12.249  1.00 78.65  ?  682  TYR B CZ  1 
ATOM   6421  O  OH  . TYR B 2  682  ? -43.693 -44.698  13.046  1.00 68.64  ?  682  TYR B OH  1 
ATOM   6422  N  N   . GLY B 2  683  ? -50.464 -48.153  9.729   1.00 101.52 ?  683  GLY B N   1 
ATOM   6423  C  CA  . GLY B 2  683  ? -51.787 -48.393  9.191   1.00 105.58 ?  683  GLY B CA  1 
ATOM   6424  C  C   . GLY B 2  683  ? -52.301 -49.804  9.349   1.00 104.28 ?  683  GLY B C   1 
ATOM   6425  O  O   . GLY B 2  683  ? -53.293 -50.158  8.701   1.00 109.29 ?  683  GLY B O   1 
ATOM   6426  N  N   . ARG B 2  684  ? -51.654 -50.625  10.175  1.00 74.97  ?  684  ARG B N   1 
ATOM   6427  C  CA  . ARG B 2  684  ? -52.113 -51.993  10.385  1.00 81.86  ?  684  ARG B CA  1 
ATOM   6428  C  C   . ARG B 2  684  ? -53.512 -51.997  10.989  1.00 84.17  ?  684  ARG B C   1 
ATOM   6429  O  O   . ARG B 2  684  ? -53.907 -51.063  11.688  1.00 83.01  ?  684  ARG B O   1 
ATOM   6430  C  CB  . ARG B 2  684  ? -51.137 -52.741  11.295  1.00 75.78  ?  684  ARG B CB  1 
ATOM   6431  C  CG  . ARG B 2  684  ? -49.770 -52.921  10.674  1.00 72.57  ?  684  ARG B CG  1 
ATOM   6432  C  CD  . ARG B 2  684  ? -48.781 -53.580  11.620  1.00 72.16  ?  684  ARG B CD  1 
ATOM   6433  N  NE  . ARG B 2  684  ? -49.236 -54.869  12.123  1.00 73.86  ?  684  ARG B NE  1 
ATOM   6434  C  CZ  . ARG B 2  684  ? -48.761 -56.037  11.715  1.00 75.35  ?  684  ARG B CZ  1 
ATOM   6435  N  NH1 . ARG B 2  684  ? -47.816 -56.114  10.792  1.00 80.19  ?  684  ARG B NH1 1 
ATOM   6436  N  NH2 . ARG B 2  684  ? -49.250 -57.157  12.241  1.00 71.40  ?  684  ARG B NH2 1 
ATOM   6437  N  N   . THR B 2  685  ? -54.277 -53.054  10.697  1.00 99.99  ?  685  THR B N   1 
ATOM   6438  C  CA  . THR B 2  685  ? -55.626 -53.203  11.227  1.00 103.03 ?  685  THR B CA  1 
ATOM   6439  C  C   . THR B 2  685  ? -55.800 -54.396  12.156  1.00 96.89  ?  685  THR B C   1 
ATOM   6440  O  O   . THR B 2  685  ? -56.734 -54.392  12.966  1.00 96.34  ?  685  THR B O   1 
ATOM   6441  C  CB  . THR B 2  685  ? -56.649 -53.328  10.086  1.00 107.12 ?  685  THR B CB  1 
ATOM   6442  O  OG1 . THR B 2  685  ? -56.422 -54.548  9.369   1.00 106.15 ?  685  THR B OG1 1 
ATOM   6443  C  CG2 . THR B 2  685  ? -56.534 -52.153  9.131   1.00 103.03 ?  685  THR B CG2 1 
ATOM   6444  N  N   . HIS B 2  686  ? -54.941 -55.409  12.062  1.00 88.26  ?  686  HIS B N   1 
ATOM   6445  C  CA  . HIS B 2  686  ? -55.018 -56.590  12.910  1.00 89.23  ?  686  HIS B CA  1 
ATOM   6446  C  C   . HIS B 2  686  ? -53.802 -56.706  13.821  1.00 87.38  ?  686  HIS B C   1 
ATOM   6447  O  O   . HIS B 2  686  ? -53.420 -57.808  14.224  1.00 88.03  ?  686  HIS B O   1 
ATOM   6448  C  CB  . HIS B 2  686  ? -55.180 -57.851  12.064  1.00 91.30  ?  686  HIS B CB  1 
ATOM   6449  C  CG  . HIS B 2  686  ? -56.599 -58.148  11.696  1.00 88.68  ?  686  HIS B CG  1 
ATOM   6450  N  ND1 . HIS B 2  686  ? -57.154 -57.747  10.500  1.00 87.89  ?  686  HIS B ND1 1 
ATOM   6451  C  CD2 . HIS B 2  686  ? -57.577 -58.808  12.361  1.00 80.45  ?  686  HIS B CD2 1 
ATOM   6452  C  CE1 . HIS B 2  686  ? -58.414 -58.138  10.448  1.00 92.21  ?  686  HIS B CE1 1 
ATOM   6453  N  NE2 . HIS B 2  686  ? -58.696 -58.787  11.563  1.00 83.78  ?  686  HIS B NE2 1 
ATOM   6454  N  N   . ALA B 2  687  ? -53.184 -55.572  14.144  1.00 114.32 ?  687  ALA B N   1 
ATOM   6455  C  CA  . ALA B 2  687  ? -52.118 -55.537  15.127  1.00 107.61 ?  687  ALA B CA  1 
ATOM   6456  C  C   . ALA B 2  687  ? -52.717 -55.546  16.530  1.00 122.42 ?  687  ALA B C   1 
ATOM   6457  O  O   . ALA B 2  687  ? -53.938 -55.520  16.716  1.00 127.35 ?  687  ALA B O   1 
ATOM   6458  C  CB  . ALA B 2  687  ? -51.232 -54.315  14.902  1.00 106.61 ?  687  ALA B CB  1 
ATOM   6459  N  N   . GLY B 2  688  ? -51.847 -55.574  17.532  1.00 122.08 ?  688  GLY B N   1 
ATOM   6460  C  CA  . GLY B 2  688  ? -52.279 -55.659  18.908  1.00 115.18 ?  688  GLY B CA  1 
ATOM   6461  C  C   . GLY B 2  688  ? -52.930 -54.377  19.391  1.00 115.42 ?  688  GLY B C   1 
ATOM   6462  O  O   . GLY B 2  688  ? -53.158 -53.423  18.647  1.00 118.65 ?  688  GLY B O   1 
ATOM   6463  N  N   . ARG B 2  689  ? -53.243 -54.376  20.692  1.00 78.12  ?  689  ARG B N   1 
ATOM   6464  C  CA  . ARG B 2  689  ? -53.884 -53.220  21.311  1.00 71.76  ?  689  ARG B CA  1 
ATOM   6465  C  C   . ARG B 2  689  ? -53.038 -51.966  21.159  1.00 73.18  ?  689  ARG B C   1 
ATOM   6466  O  O   . ARG B 2  689  ? -53.579 -50.861  21.034  1.00 71.74  ?  689  ARG B O   1 
ATOM   6467  C  CB  . ARG B 2  689  ? -54.154 -53.502  22.789  1.00 66.02  ?  689  ARG B CB  1 
ATOM   6468  C  CG  . ARG B 2  689  ? -52.953 -54.063  23.534  1.00 69.70  ?  689  ARG B CG  1 
ATOM   6469  C  CD  . ARG B 2  689  ? -53.373 -54.798  24.797  1.00 81.67  ?  689  ARG B CD  1 
ATOM   6470  N  NE  . ARG B 2  689  ? -54.162 -55.990  24.511  1.00 81.59  ?  689  ARG B NE  1 
ATOM   6471  C  CZ  . ARG B 2  689  ? -54.599 -56.835  25.435  1.00 82.69  ?  689  ARG B CZ  1 
ATOM   6472  N  NH1 . ARG B 2  689  ? -54.334 -56.653  26.719  1.00 77.10  ?  689  ARG B NH1 1 
ATOM   6473  N  NH2 . ARG B 2  689  ? -55.315 -57.892  25.062  1.00 82.04  ?  689  ARG B NH2 1 
ATOM   6474  N  N   . VAL B 2  690  ? -51.720 -52.113  21.164  1.00 96.82  ?  690  VAL B N   1 
ATOM   6475  C  CA  . VAL B 2  690  ? -50.814 -51.009  20.881  1.00 92.52  ?  690  VAL B CA  1 
ATOM   6476  C  C   . VAL B 2  690  ? -50.602 -50.935  19.377  1.00 99.08  ?  690  VAL B C   1 
ATOM   6477  O  O   . VAL B 2  690  ? -50.227 -51.929  18.742  1.00 99.15  ?  690  VAL B O   1 
ATOM   6478  C  CB  . VAL B 2  690  ? -49.477 -51.188  21.618  1.00 89.37  ?  690  VAL B CB  1 
ATOM   6479  C  CG1 . VAL B 2  690  ? -48.461 -50.164  21.123  1.00 87.36  ?  690  VAL B CG1 1 
ATOM   6480  C  CG2 . VAL B 2  690  ? -49.678 -51.060  23.120  1.00 102.60 ?  690  VAL B CG2 1 
ATOM   6481  N  N   . GLY B 2  691  ? -50.848 -49.760  18.803  1.00 90.50  ?  691  GLY B N   1 
ATOM   6482  C  CA  . GLY B 2  691  ? -50.652 -49.567  17.381  1.00 98.56  ?  691  GLY B CA  1 
ATOM   6483  C  C   . GLY B 2  691  ? -51.710 -50.169  16.487  1.00 100.55 ?  691  GLY B C   1 
ATOM   6484  O  O   . GLY B 2  691  ? -51.428 -50.447  15.316  1.00 96.84  ?  691  GLY B O   1 
ATOM   6485  N  N   . ASN B 2  692  ? -52.929 -50.372  16.997  1.00 91.78  ?  692  ASN B N   1 
ATOM   6486  C  CA  . ASN B 2  692  ? -53.956 -51.042  16.206  1.00 85.47  ?  692  ASN B CA  1 
ATOM   6487  C  C   . ASN B 2  692  ? -54.459 -50.163  15.072  1.00 88.94  ?  692  ASN B C   1 
ATOM   6488  O  O   . ASN B 2  692  ? -54.944 -50.684  14.062  1.00 106.09 ?  692  ASN B O   1 
ATOM   6489  C  CB  . ASN B 2  692  ? -55.121 -51.469  17.097  1.00 92.67  ?  692  ASN B CB  1 
ATOM   6490  C  CG  . ASN B 2  692  ? -55.908 -52.624  16.510  1.00 95.71  ?  692  ASN B CG  1 
ATOM   6491  O  OD1 . ASN B 2  692  ? -55.460 -53.289  15.575  1.00 92.43  ?  692  ASN B OD1 1 
ATOM   6492  N  ND2 . ASN B 2  692  ? -57.090 -52.871  17.061  1.00 105.20 ?  692  ASN B ND2 1 
ATOM   6493  N  N   . ASN B 2  693  ? -54.359 -48.846  15.216  1.00 75.02  ?  693  ASN B N   1 
ATOM   6494  C  CA  . ASN B 2  693  ? -54.750 -47.909  14.167  1.00 83.16  ?  693  ASN B CA  1 
ATOM   6495  C  C   . ASN B 2  693  ? -53.875 -46.658  14.254  1.00 82.20  ?  693  ASN B C   1 
ATOM   6496  O  O   . ASN B 2  693  ? -54.338 -45.544  14.500  1.00 74.40  ?  693  ASN B O   1 
ATOM   6497  C  CB  . ASN B 2  693  ? -56.237 -47.567  14.265  1.00 81.46  ?  693  ASN B CB  1 
ATOM   6498  C  CG  . ASN B 2  693  ? -57.143 -48.694  13.776  1.00 88.19  ?  693  ASN B CG  1 
ATOM   6499  O  OD1 . ASN B 2  693  ? -57.418 -49.652  14.501  1.00 98.60  ?  693  ASN B OD1 1 
ATOM   6500  N  ND2 . ASN B 2  693  ? -57.609 -48.581  12.537  1.00 87.73  ?  693  ASN B ND2 1 
ATOM   6501  N  N   . VAL B 2  694  ? -52.571 -46.818  14.040  1.00 77.79  ?  694  VAL B N   1 
ATOM   6502  C  CA  . VAL B 2  694  ? -51.631 -45.705  14.091  1.00 72.82  ?  694  VAL B CA  1 
ATOM   6503  C  C   . VAL B 2  694  ? -50.996 -45.536  12.718  1.00 77.40  ?  694  VAL B C   1 
ATOM   6504  O  O   . VAL B 2  694  ? -50.667 -46.520  12.045  1.00 73.06  ?  694  VAL B O   1 
ATOM   6505  C  CB  . VAL B 2  694  ? -50.551 -45.908  15.174  1.00 66.12  ?  694  VAL B CB  1 
ATOM   6506  C  CG1 . VAL B 2  694  ? -51.172 -45.842  16.564  1.00 61.44  ?  694  VAL B CG1 1 
ATOM   6507  C  CG2 . VAL B 2  694  ? -49.817 -47.217  14.962  1.00 74.89  ?  694  VAL B CG2 1 
ATOM   6508  N  N   . GLY B 2  695  ? -50.839 -44.282  12.302  1.00 110.52 ?  695  GLY B N   1 
ATOM   6509  C  CA  . GLY B 2  695  ? -50.211 -43.978  11.033  1.00 105.09 ?  695  GLY B CA  1 
ATOM   6510  C  C   . GLY B 2  695  ? -51.116 -44.233  9.842   1.00 106.79 ?  695  GLY B C   1 
ATOM   6511  O  O   . GLY B 2  695  ? -52.243 -44.721  9.955   1.00 104.31 ?  695  GLY B O   1 
ATOM   6512  N  N   . ILE B 2  696  ? -50.598 -43.880  8.668   1.00 68.93  ?  696  ILE B N   1 
ATOM   6513  C  CA  . ILE B 2  696  ? -51.292 -44.068  7.399   1.00 67.03  ?  696  ILE B CA  1 
ATOM   6514  C  C   . ILE B 2  696  ? -50.494 -45.063  6.571   1.00 65.86  ?  696  ILE B C   1 
ATOM   6515  O  O   . ILE B 2  696  ? -49.279 -44.902  6.403   1.00 65.61  ?  696  ILE B O   1 
ATOM   6516  C  CB  . ILE B 2  696  ? -51.466 -42.739  6.642   1.00 72.70  ?  696  ILE B CB  1 
ATOM   6517  C  CG1 . ILE B 2  696  ? -52.048 -41.666  7.566   1.00 64.79  ?  696  ILE B CG1 1 
ATOM   6518  C  CG2 . ILE B 2  696  ? -52.343 -42.936  5.418   1.00 80.33  ?  696  ILE B CG2 1 
ATOM   6519  C  CD1 . ILE B 2  696  ? -53.546 -41.784  7.787   1.00 61.39  ?  696  ILE B CD1 1 
ATOM   6520  N  N   . ASP B 2  697  ? -51.172 -46.090  6.063   1.00 92.52  ?  697  ASP B N   1 
ATOM   6521  C  CA  . ASP B 2  697  ? -50.491 -47.142  5.320   1.00 94.08  ?  697  ASP B CA  1 
ATOM   6522  C  C   . ASP B 2  697  ? -49.955 -46.611  3.998   1.00 88.35  ?  697  ASP B C   1 
ATOM   6523  O  O   . ASP B 2  697  ? -50.698 -46.041  3.193   1.00 90.17  ?  697  ASP B O   1 
ATOM   6524  C  CB  . ASP B 2  697  ? -51.433 -48.318  5.070   1.00 90.97  ?  697  ASP B CB  1 
ATOM   6525  C  CG  . ASP B 2  697  ? -50.690 -49.596  4.720   1.00 92.03  ?  697  ASP B CG  1 
ATOM   6526  O  OD1 . ASP B 2  697  ? -49.443 -49.607  4.811   1.00 96.24  ?  697  ASP B OD1 1 
ATOM   6527  O  OD2 . ASP B 2  697  ? -51.350 -50.589  4.352   1.00 97.90  -1 697  ASP B OD2 1 
ATOM   6528  N  N   . VAL B 2  698  ? -48.654 -46.806  3.778   1.00 55.31  ?  698  VAL B N   1 
ATOM   6529  C  CA  . VAL B 2  698  ? -48.004 -46.397  2.538   1.00 56.90  ?  698  VAL B CA  1 
ATOM   6530  C  C   . VAL B 2  698  ? -47.827 -47.561  1.574   1.00 62.88  ?  698  VAL B C   1 
ATOM   6531  O  O   . VAL B 2  698  ? -47.517 -47.335  0.393   1.00 63.28  ?  698  VAL B O   1 
ATOM   6532  C  CB  . VAL B 2  698  ? -46.643 -45.728  2.829   1.00 56.81  ?  698  VAL B CB  1 
ATOM   6533  C  CG1 . VAL B 2  698  ? -46.183 -44.908  1.637   1.00 69.88  ?  698  VAL B CG1 1 
ATOM   6534  C  CG2 . VAL B 2  698  ? -46.743 -44.850  4.069   1.00 58.32  ?  698  VAL B CG2 1 
ATOM   6535  N  N   . TYR B 2  699  ? -48.030 -48.793  2.034   1.00 83.62  ?  699  TYR B N   1 
ATOM   6536  C  CA  . TYR B 2  699  ? -47.883 -49.950  1.156   1.00 85.39  ?  699  TYR B CA  1 
ATOM   6537  C  C   . TYR B 2  699  ? -48.865 -49.967  -0.013  1.00 84.38  ?  699  TYR B C   1 
ATOM   6538  O  O   . TYR B 2  699  ? -48.470 -50.435  -1.096  1.00 88.44  ?  699  TYR B O   1 
ATOM   6539  C  CB  . TYR B 2  699  ? -48.000 -51.232  1.989   1.00 75.30  ?  699  TYR B CB  1 
ATOM   6540  C  CG  . TYR B 2  699  ? -46.731 -51.582  2.733   1.00 69.70  ?  699  TYR B CG  1 
ATOM   6541  C  CD1 . TYR B 2  699  ? -45.594 -51.995  2.052   1.00 74.62  ?  699  TYR B CD1 1 
ATOM   6542  C  CD2 . TYR B 2  699  ? -46.666 -51.486  4.117   1.00 77.80  ?  699  TYR B CD2 1 
ATOM   6543  C  CE1 . TYR B 2  699  ? -44.433 -52.309  2.729   1.00 81.36  ?  699  TYR B CE1 1 
ATOM   6544  C  CE2 . TYR B 2  699  ? -45.509 -51.798  4.803   1.00 74.59  ?  699  TYR B CE2 1 
ATOM   6545  C  CZ  . TYR B 2  699  ? -44.395 -52.209  4.104   1.00 74.22  ?  699  TYR B CZ  1 
ATOM   6546  O  OH  . TYR B 2  699  ? -43.234 -52.523  4.775   1.00 73.05  ?  699  TYR B OH  1 
ATOM   6547  N  N   . PRO B 2  700  ? -50.122 -49.510  0.116   1.00 83.41  ?  700  PRO B N   1 
ATOM   6548  C  CA  . PRO B 2  700  ? -50.998 -49.489  -1.069  1.00 89.81  ?  700  PRO B CA  1 
ATOM   6549  C  C   . PRO B 2  700  ? -50.452 -48.655  -2.212  1.00 84.37  ?  700  PRO B C   1 
ATOM   6550  O  O   . PRO B 2  700  ? -50.530 -49.082  -3.369  1.00 88.13  ?  700  PRO B O   1 
ATOM   6551  C  CB  . PRO B 2  700  ? -52.306 -48.908  -0.516  1.00 85.62  ?  700  PRO B CB  1 
ATOM   6552  C  CG  . PRO B 2  700  ? -52.322 -49.359  0.887   1.00 85.58  ?  700  PRO B CG  1 
ATOM   6553  C  CD  . PRO B 2  700  ? -50.893 -49.220  1.340   1.00 87.37  ?  700  PRO B CD  1 
ATOM   6554  N  N   . ILE B 2  701  ? -49.897 -47.476  -1.928  1.00 63.11  ?  701  ILE B N   1 
ATOM   6555  C  CA  . ILE B 2  701  ? -49.330 -46.663  -2.998  1.00 61.69  ?  701  ILE B CA  1 
ATOM   6556  C  C   . ILE B 2  701  ? -47.983 -47.198  -3.465  1.00 62.10  ?  701  ILE B C   1 
ATOM   6557  O  O   . ILE B 2  701  ? -47.495 -46.786  -4.524  1.00 63.95  ?  701  ILE B O   1 
ATOM   6558  C  CB  . ILE B 2  701  ? -49.195 -45.192  -2.565  1.00 48.89  ?  701  ILE B CB  1 
ATOM   6559  C  CG1 . ILE B 2  701  ? -47.842 -44.945  -1.893  1.00 60.92  ?  701  ILE B CG1 1 
ATOM   6560  C  CG2 . ILE B 2  701  ? -50.338 -44.796  -1.644  1.00 52.04  ?  701  ILE B CG2 1 
ATOM   6561  C  CD1 . ILE B 2  701  ? -47.535 -43.488  -1.670  1.00 77.52  ?  701  ILE B CD1 1 
ATOM   6562  N  N   . ARG B 2  702  ? -47.366 -48.102  -2.710  1.00 75.04  ?  702  ARG B N   1 
ATOM   6563  C  CA  . ARG B 2  702  ? -46.098 -48.682  -3.132  1.00 79.73  ?  702  ARG B CA  1 
ATOM   6564  C  C   . ARG B 2  702  ? -46.304 -49.581  -4.347  1.00 88.83  ?  702  ARG B C   1 
ATOM   6565  O  O   . ARG B 2  702  ? -47.296 -50.309  -4.438  1.00 92.94  ?  702  ARG B O   1 
ATOM   6566  C  CB  . ARG B 2  702  ? -45.469 -49.473  -1.984  1.00 78.88  ?  702  ARG B CB  1 
ATOM   6567  C  CG  . ARG B 2  702  ? -43.950 -49.531  -2.014  1.00 75.70  ?  702  ARG B CG  1 
ATOM   6568  C  CD  . ARG B 2  702  ? -43.428 -50.580  -1.050  1.00 73.19  ?  702  ARG B CD  1 
ATOM   6569  N  NE  . ARG B 2  702  ? -41.973 -50.564  -0.969  1.00 75.12  ?  702  ARG B NE  1 
ATOM   6570  C  CZ  . ARG B 2  702  ? -41.247 -51.492  -0.361  1.00 79.27  ?  702  ARG B CZ  1 
ATOM   6571  N  NH1 . ARG B 2  702  ? -41.812 -52.529  0.236   1.00 77.75  ?  702  ARG B NH1 1 
ATOM   6572  N  NH2 . ARG B 2  702  ? -39.923 -51.369  -0.340  1.00 72.17  ?  702  ARG B NH2 1 
ATOM   6573  N  N   . THR B 2  703  ? -45.356 -49.532  -5.284  1.00 92.01  ?  703  THR B N   1 
ATOM   6574  C  CA  . THR B 2  703  ? -45.479 -50.217  -6.563  1.00 83.77  ?  703  THR B CA  1 
ATOM   6575  C  C   . THR B 2  703  ? -44.336 -51.206  -6.753  1.00 80.21  ?  703  THR B C   1 
ATOM   6576  O  O   . THR B 2  703  ? -43.252 -51.044  -6.186  1.00 80.62  ?  703  THR B O   1 
ATOM   6577  C  CB  . THR B 2  703  ? -45.494 -49.220  -7.731  1.00 93.44  ?  703  THR B CB  1 
ATOM   6578  O  OG1 . THR B 2  703  ? -44.415 -48.289  -7.580  1.00 92.00  ?  703  THR B OG1 1 
ATOM   6579  C  CG2 . THR B 2  703  ? -46.810 -48.464  -7.765  1.00 94.25  ?  703  THR B CG2 1 
ATOM   6580  N  N   . SER B 2  704  ? -44.591 -52.236  -7.566  1.00 80.15  ?  704  SER B N   1 
ATOM   6581  C  CA  . SER B 2  704  ? -43.586 -53.272  -7.786  1.00 77.76  ?  704  SER B CA  1 
ATOM   6582  C  C   . SER B 2  704  ? -42.467 -52.793  -8.702  1.00 76.48  ?  704  SER B C   1 
ATOM   6583  O  O   . SER B 2  704  ? -41.316 -53.220  -8.547  1.00 72.71  ?  704  SER B O   1 
ATOM   6584  C  CB  . SER B 2  704  ? -44.239 -54.525  -8.369  1.00 79.69  ?  704  SER B CB  1 
ATOM   6585  O  OG  . SER B 2  704  ? -45.417 -54.872  -7.661  1.00 82.83  ?  704  SER B OG  1 
ATOM   6586  N  N   . ASP B 2  705  ? -42.779 -51.920  -9.662  1.00 119.81 ?  705  ASP B N   1 
ATOM   6587  C  CA  . ASP B 2  705  ? -41.765 -51.482  -10.616 1.00 121.63 ?  705  ASP B CA  1 
ATOM   6588  C  C   . ASP B 2  705  ? -40.651 -50.704  -9.925  1.00 120.71 ?  705  ASP B C   1 
ATOM   6589  O  O   . ASP B 2  705  ? -39.470 -50.875  -10.248 1.00 119.60 ?  705  ASP B O   1 
ATOM   6590  C  CB  . ASP B 2  705  ? -42.410 -50.646  -11.724 1.00 118.30 ?  705  ASP B CB  1 
ATOM   6591  C  CG  . ASP B 2  705  ? -43.414 -49.637  -11.191 1.00 122.49 ?  705  ASP B CG  1 
ATOM   6592  O  OD1 . ASP B 2  705  ? -43.243 -49.164  -10.050 1.00 126.88 ?  705  ASP B OD1 1 
ATOM   6593  O  OD2 . ASP B 2  705  ? -44.379 -49.317  -11.917 1.00 127.34 -1 705  ASP B OD2 1 
ATOM   6594  N  N   . SER B 2  706  ? -41.007 -49.849  -8.970  1.00 113.57 ?  706  SER B N   1 
ATOM   6595  C  CA  . SER B 2  706  ? -40.026 -49.122  -8.174  1.00 109.90 ?  706  SER B CA  1 
ATOM   6596  C  C   . SER B 2  706  ? -40.460 -49.136  -6.713  1.00 102.62 ?  706  SER B C   1 
ATOM   6597  O  O   . SER B 2  706  ? -41.403 -48.426  -6.337  1.00 102.59 ?  706  SER B O   1 
ATOM   6598  C  CB  . SER B 2  706  ? -39.861 -47.689  -8.682  1.00 114.50 ?  706  SER B CB  1 
ATOM   6599  O  OG  . SER B 2  706  ? -39.504 -47.676  -10.053 1.00 109.38 ?  706  SER B OG  1 
ATOM   6600  N  N   . PRO B 2  707  ? -39.802 -49.933  -5.865  1.00 79.27  ?  707  PRO B N   1 
ATOM   6601  C  CA  . PRO B 2  707  ? -40.232 -50.063  -4.469  1.00 77.09  ?  707  PRO B CA  1 
ATOM   6602  C  C   . PRO B 2  707  ? -39.615 -49.062  -3.504  1.00 71.53  ?  707  PRO B C   1 
ATOM   6603  O  O   . PRO B 2  707  ? -40.082 -48.973  -2.360  1.00 70.57  ?  707  PRO B O   1 
ATOM   6604  C  CB  . PRO B 2  707  ? -39.791 -51.493  -4.120  1.00 69.92  ?  707  PRO B CB  1 
ATOM   6605  C  CG  . PRO B 2  707  ? -38.582 -51.743  -4.989  1.00 72.80  ?  707  PRO B CG  1 
ATOM   6606  C  CD  . PRO B 2  707  ? -38.638 -50.784  -6.167  1.00 73.29  ?  707  PRO B CD  1 
ATOM   6607  N  N   . TRP B 2  708  ? -38.591 -48.313  -3.918  1.00 86.68  ?  708  TRP B N   1 
ATOM   6608  C  CA  . TRP B 2  708  ? -37.933 -47.353  -3.045  1.00 84.26  ?  708  TRP B CA  1 
ATOM   6609  C  C   . TRP B 2  708  ? -37.986 -45.919  -3.554  1.00 82.01  ?  708  TRP B C   1 
ATOM   6610  O  O   . TRP B 2  708  ? -37.867 -44.995  -2.741  1.00 76.82  ?  708  TRP B O   1 
ATOM   6611  C  CB  . TRP B 2  708  ? -36.461 -47.745  -2.827  1.00 88.86  ?  708  TRP B CB  1 
ATOM   6612  C  CG  . TRP B 2  708  ? -36.250 -49.199  -2.518  1.00 84.39  ?  708  TRP B CG  1 
ATOM   6613  C  CD1 . TRP B 2  708  ? -35.856 -50.169  -3.393  1.00 81.16  ?  708  TRP B CD1 1 
ATOM   6614  C  CD2 . TRP B 2  708  ? -36.406 -49.844  -1.247  1.00 78.71  ?  708  TRP B CD2 1 
ATOM   6615  N  NE1 . TRP B 2  708  ? -35.765 -51.378  -2.750  1.00 78.55  ?  708  TRP B NE1 1 
ATOM   6616  C  CE2 . TRP B 2  708  ? -36.097 -51.207  -1.432  1.00 84.21  ?  708  TRP B CE2 1 
ATOM   6617  C  CE3 . TRP B 2  708  ? -36.781 -49.403  0.027   1.00 75.80  ?  708  TRP B CE3 1 
ATOM   6618  C  CZ2 . TRP B 2  708  ? -36.151 -52.133  -0.391  1.00 88.46  ?  708  TRP B CZ2 1 
ATOM   6619  C  CZ3 . TRP B 2  708  ? -36.834 -50.326  1.060   1.00 78.55  ?  708  TRP B CZ3 1 
ATOM   6620  C  CH2 . TRP B 2  708  ? -36.520 -51.674  0.843   1.00 89.61  ?  708  TRP B CH2 1 
ATOM   6621  N  N   . PHE B 2  709  ? -38.171 -45.705  -4.856  1.00 99.49  ?  709  PHE B N   1 
ATOM   6622  C  CA  . PHE B 2  709  ? -38.196 -44.373  -5.442  1.00 93.42  ?  709  PHE B CA  1 
ATOM   6623  C  C   . PHE B 2  709  ? -39.550 -44.112  -6.088  1.00 98.68  ?  709  PHE B C   1 
ATOM   6624  O  O   . PHE B 2  709  ? -40.342 -45.030  -6.316  1.00 101.98 ?  709  PHE B O   1 
ATOM   6625  C  CB  . PHE B 2  709  ? -37.085 -44.192  -6.487  1.00 94.70  ?  709  PHE B CB  1 
ATOM   6626  C  CG  . PHE B 2  709  ? -35.706 -44.446  -5.959  1.00 95.52  ?  709  PHE B CG  1 
ATOM   6627  C  CD1 . PHE B 2  709  ? -35.366 -44.077  -4.669  1.00 98.39  ?  709  PHE B CD1 1 
ATOM   6628  C  CD2 . PHE B 2  709  ? -34.749 -45.054  -6.753  1.00 98.79  ?  709  PHE B CD2 1 
ATOM   6629  C  CE1 . PHE B 2  709  ? -34.096 -44.309  -4.178  1.00 103.67 ?  709  PHE B CE1 1 
ATOM   6630  C  CE2 . PHE B 2  709  ? -33.478 -45.292  -6.269  1.00 96.47  ?  709  PHE B CE2 1 
ATOM   6631  C  CZ  . PHE B 2  709  ? -33.152 -44.919  -4.979  1.00 98.25  ?  709  PHE B CZ  1 
ATOM   6632  N  N   . GLY B 2  710  ? -39.807 -42.832  -6.383  1.00 76.97  ?  710  GLY B N   1 
ATOM   6633  C  CA  . GLY B 2  710  ? -41.041 -42.428  -7.017  1.00 70.36  ?  710  GLY B CA  1 
ATOM   6634  C  C   . GLY B 2  710  ? -40.775 -41.534  -8.216  1.00 82.64  ?  710  GLY B C   1 
ATOM   6635  O  O   . GLY B 2  710  ? -39.661 -41.043  -8.419  1.00 86.42  ?  710  GLY B O   1 
ATOM   6636  N  N   . ALA B 2  711  ? -41.826 -41.327  -9.009  1.00 99.03  ?  711  ALA B N   1 
ATOM   6637  C  CA  . ALA B 2  711  ? -41.708 -40.548  -10.236 1.00 104.77 ?  711  ALA B CA  1 
ATOM   6638  C  C   . ALA B 2  711  ? -42.370 -39.183  -10.097 1.00 100.09 ?  711  ALA B C   1 
ATOM   6639  O  O   . ALA B 2  711  ? -41.690 -38.179  -9.860  1.00 100.25 ?  711  ALA B O   1 
ATOM   6640  C  CB  . ALA B 2  711  ? -42.315 -41.314  -11.415 1.00 113.09 ?  711  ALA B CB  1 
ATOM   6641  N  N   . GLY B 2  712  ? -43.683 -39.136  -10.245 1.00 80.05  ?  712  GLY B N   1 
ATOM   6642  C  CA  . GLY B 2  712  ? -44.420 -37.885  -10.151 1.00 78.52  ?  712  GLY B CA  1 
ATOM   6643  C  C   . GLY B 2  712  ? -45.587 -38.009  -9.198  1.00 85.07  ?  712  GLY B C   1 
ATOM   6644  O  O   . GLY B 2  712  ? -46.239 -39.051  -9.129  1.00 92.31  ?  712  GLY B O   1 
ATOM   6645  N  N   . ALA B 2  713  ? -45.850 -36.929  -8.465  1.00 87.11  ?  713  ALA B N   1 
ATOM   6646  C  CA  . ALA B 2  713  ? -46.867 -36.947  -7.425  1.00 88.68  ?  713  ALA B CA  1 
ATOM   6647  C  C   . ALA B 2  713  ? -47.607 -35.618  -7.384  1.00 86.57  ?  713  ALA B C   1 
ATOM   6648  O  O   . ALA B 2  713  ? -47.096 -34.582  -7.814  1.00 93.05  ?  713  ALA B O   1 
ATOM   6649  C  CB  . ALA B 2  713  ? -46.253 -37.241  -6.050  1.00 87.56  ?  713  ALA B CB  1 
ATOM   6650  N  N   . ARG B 2  714  ? -48.823 -35.667  -6.842  1.00 97.12  ?  714  ARG B N   1 
ATOM   6651  C  CA  . ARG B 2  714  ? -49.675 -34.499  -6.643  1.00 107.80 ?  714  ARG B CA  1 
ATOM   6652  C  C   . ARG B 2  714  ? -49.918 -34.346  -5.149  1.00 106.42 ?  714  ARG B C   1 
ATOM   6653  O  O   . ARG B 2  714  ? -50.528 -35.221  -4.529  1.00 110.52 ?  714  ARG B O   1 
ATOM   6654  C  CB  . ARG B 2  714  ? -50.998 -34.652  -7.398  1.00 116.41 ?  714  ARG B CB  1 
ATOM   6655  C  CG  . ARG B 2  714  ? -51.723 -33.346  -7.670  1.00 129.08 ?  714  ARG B CG  1 
ATOM   6656  C  CD  . ARG B 2  714  ? -52.067 -33.211  -9.145  1.00 129.51 ?  714  ARG B CD  1 
ATOM   6657  N  NE  . ARG B 2  714  ? -52.987 -34.250  -9.591  1.00 130.70 ?  714  ARG B NE  1 
ATOM   6658  C  CZ  . ARG B 2  714  ? -54.303 -34.107  -9.671  1.00 133.25 ?  714  ARG B CZ  1 
ATOM   6659  N  NH1 . ARG B 2  714  ? -54.896 -32.974  -9.337  1.00 135.81 ?  714  ARG B NH1 1 
ATOM   6660  N  NH2 . ARG B 2  714  ? -55.041 -35.131  -10.090 1.00 135.91 ?  714  ARG B NH2 1 
ATOM   6661  N  N   . VAL B 2  715  ? -49.438 -33.241  -4.575  1.00 105.38 ?  715  VAL B N   1 
ATOM   6662  C  CA  . VAL B 2  715  ? -49.459 -33.079  -3.123  1.00 114.26 ?  715  VAL B CA  1 
ATOM   6663  C  C   . VAL B 2  715  ? -50.866 -32.766  -2.618  1.00 118.52 ?  715  VAL B C   1 
ATOM   6664  O  O   . VAL B 2  715  ? -51.339 -33.385  -1.658  1.00 114.57 ?  715  VAL B O   1 
ATOM   6665  C  CB  . VAL B 2  715  ? -48.447 -32.000  -2.694  1.00 124.74 ?  715  VAL B CB  1 
ATOM   6666  C  CG1 . VAL B 2  715  ? -47.057 -32.591  -2.635  1.00 115.58 ?  715  VAL B CG1 1 
ATOM   6667  C  CG2 . VAL B 2  715  ? -48.479 -30.823  -3.655  1.00 123.10 ?  715  VAL B CG2 1 
ATOM   6668  N  N   . THR B 2  716  ? -51.538 -31.788  -3.231  1.00 102.32 ?  716  THR B N   1 
ATOM   6669  C  CA  . THR B 2  716  ? -52.926 -31.443  -2.923  1.00 104.18 ?  716  THR B CA  1 
ATOM   6670  C  C   . THR B 2  716  ? -53.134 -31.188  -1.432  1.00 102.63 ?  716  THR B C   1 
ATOM   6671  O  O   . THR B 2  716  ? -53.599 -32.068  -0.696  1.00 100.09 ?  716  THR B O   1 
ATOM   6672  C  CB  . THR B 2  716  ? -53.874 -32.541  -3.419  1.00 109.05 ?  716  THR B CB  1 
ATOM   6673  O  OG1 . THR B 2  716  ? -53.544 -32.873  -4.774  1.00 110.11 ?  716  THR B OG1 1 
ATOM   6674  C  CG2 . THR B 2  716  ? -55.325 -32.058  -3.368  1.00 106.53 ?  716  THR B CG2 1 
ATOM   6675  N  N   . ASN B 2  717  ? -52.785 -29.988  -0.977  1.00 88.96  ?  717  ASN B N   1 
ATOM   6676  C  CA  . ASN B 2  717  ? -53.053 -29.622  0.407   1.00 82.26  ?  717  ASN B CA  1 
ATOM   6677  C  C   . ASN B 2  717  ? -54.557 -29.512  0.636   1.00 79.82  ?  717  ASN B C   1 
ATOM   6678  O  O   . ASN B 2  717  ? -55.284 -28.947  -0.185  1.00 88.83  ?  717  ASN B O   1 
ATOM   6679  C  CB  . ASN B 2  717  ? -52.362 -28.304  0.758   1.00 76.19  ?  717  ASN B CB  1 
ATOM   6680  C  CG  . ASN B 2  717  ? -52.714 -27.818  2.154   1.00 82.57  ?  717  ASN B CG  1 
ATOM   6681  O  OD1 . ASN B 2  717  ? -52.931 -28.615  3.067   1.00 92.71  ?  717  ASN B OD1 1 
ATOM   6682  N  ND2 . ASN B 2  717  ? -52.768 -26.503  2.326   1.00 77.94  ?  717  ASN B ND2 1 
ATOM   6683  N  N   . THR B 2  718  ? -55.024 -30.059  1.760   1.00 58.11  ?  718  THR B N   1 
ATOM   6684  C  CA  . THR B 2  718  ? -56.452 -30.166  2.038   1.00 61.79  ?  718  THR B CA  1 
ATOM   6685  C  C   . THR B 2  718  ? -56.896 -29.343  3.239   1.00 72.93  ?  718  THR B C   1 
ATOM   6686  O  O   . THR B 2  718  ? -58.083 -29.369  3.590   1.00 83.99  ?  718  THR B O   1 
ATOM   6687  C  CB  . THR B 2  718  ? -56.837 -31.635  2.267   1.00 68.74  ?  718  THR B CB  1 
ATOM   6688  O  OG1 . THR B 2  718  ? -56.207 -32.116  3.460   1.00 65.60  ?  718  THR B OG1 1 
ATOM   6689  C  CG2 . THR B 2  718  ? -56.393 -32.498  1.092   1.00 73.58  ?  718  THR B CG2 1 
ATOM   6690  N  N   . GLY B 2  719  ? -55.994 -28.600  3.866   1.00 117.01 ?  719  GLY B N   1 
ATOM   6691  C  CA  . GLY B 2  719  ? -56.328 -28.046  5.167   1.00 121.14 ?  719  GLY B CA  1 
ATOM   6692  C  C   . GLY B 2  719  ? -56.464 -29.193  6.147   1.00 118.73 ?  719  GLY B C   1 
ATOM   6693  O  O   . GLY B 2  719  ? -55.641 -30.114  6.157   1.00 123.19 ?  719  GLY B O   1 
ATOM   6694  N  N   . ARG B 2  720  ? -57.511 -29.151  6.971   1.00 114.97 ?  720  ARG B N   1 
ATOM   6695  C  CA  . ARG B 2  720  ? -57.904 -30.269  7.831   1.00 127.41 ?  720  ARG B CA  1 
ATOM   6696  C  C   . ARG B 2  720  ? -56.704 -30.823  8.607   1.00 127.20 ?  720  ARG B C   1 
ATOM   6697  O  O   . ARG B 2  720  ? -56.217 -31.928  8.365   1.00 125.42 ?  720  ARG B O   1 
ATOM   6698  C  CB  . ARG B 2  720  ? -58.573 -31.372  7.003   1.00 127.15 ?  720  ARG B CB  1 
ATOM   6699  C  CG  . ARG B 2  720  ? -59.717 -30.893  6.125   1.00 123.27 ?  720  ARG B CG  1 
ATOM   6700  C  CD  . ARG B 2  720  ? -60.662 -32.035  5.764   1.00 130.85 ?  720  ARG B CD  1 
ATOM   6701  N  NE  . ARG B 2  720  ? -60.014 -33.337  5.866   1.00 136.68 ?  720  ARG B NE  1 
ATOM   6702  C  CZ  . ARG B 2  720  ? -59.479 -33.992  4.844   1.00 133.37 ?  720  ARG B CZ  1 
ATOM   6703  N  NH1 . ARG B 2  720  ? -59.487 -33.489  3.621   1.00 132.15 ?  720  ARG B NH1 1 
ATOM   6704  N  NH2 . ARG B 2  720  ? -58.906 -35.173  5.059   1.00 129.43 ?  720  ARG B NH2 1 
ATOM   6705  N  N   . THR B 2  721  ? -56.236 -30.013  9.551   1.00 121.95 ?  721  THR B N   1 
ATOM   6706  C  CA  . THR B 2  721  ? -55.010 -30.337  10.265  1.00 118.14 ?  721  THR B CA  1 
ATOM   6707  C  C   . THR B 2  721  ? -55.195 -31.568  11.146  1.00 113.58 ?  721  THR B C   1 
ATOM   6708  O  O   . THR B 2  721  ? -56.301 -31.885  11.590  1.00 110.96 ?  721  THR B O   1 
ATOM   6709  C  CB  . THR B 2  721  ? -54.560 -29.153  11.119  1.00 120.10 ?  721  THR B CB  1 
ATOM   6710  O  OG1 . THR B 2  721  ? -53.476 -29.563  11.961  1.00 114.00 ?  721  THR B OG1 1 
ATOM   6711  C  CG2 . THR B 2  721  ? -55.706 -28.653  11.975  1.00 112.10 ?  721  THR B CG2 1 
ATOM   6712  N  N   . TYR B 2  722  ? -54.089 -32.270  11.382  1.00 92.21  ?  722  TYR B N   1 
ATOM   6713  C  CA  . TYR B 2  722  ? -54.049 -33.443  12.243  1.00 81.24  ?  722  TYR B CA  1 
ATOM   6714  C  C   . TYR B 2  722  ? -52.951 -33.243  13.276  1.00 85.35  ?  722  TYR B C   1 
ATOM   6715  O  O   . TYR B 2  722  ? -51.910 -32.650  12.977  1.00 85.94  ?  722  TYR B O   1 
ATOM   6716  C  CB  . TYR B 2  722  ? -53.798 -34.724  11.433  1.00 82.92  ?  722  TYR B CB  1 
ATOM   6717  C  CG  . TYR B 2  722  ? -53.628 -35.973  12.269  1.00 86.15  ?  722  TYR B CG  1 
ATOM   6718  C  CD1 . TYR B 2  722  ? -54.712 -36.553  12.911  1.00 85.18  ?  722  TYR B CD1 1 
ATOM   6719  C  CD2 . TYR B 2  722  ? -52.383 -36.575  12.412  1.00 88.73  ?  722  TYR B CD2 1 
ATOM   6720  C  CE1 . TYR B 2  722  ? -54.563 -37.696  13.674  1.00 82.48  ?  722  TYR B CE1 1 
ATOM   6721  C  CE2 . TYR B 2  722  ? -52.223 -37.720  13.175  1.00 88.13  ?  722  TYR B CE2 1 
ATOM   6722  C  CZ  . TYR B 2  722  ? -53.317 -38.276  13.803  1.00 89.12  ?  722  TYR B CZ  1 
ATOM   6723  O  OH  . TYR B 2  722  ? -53.170 -39.415  14.564  1.00 92.50  ?  722  TYR B OH  1 
ATOM   6724  N  N   . LEU B 2  723  ? -53.187 -33.732  14.490  1.00 95.63  ?  723  LEU B N   1 
ATOM   6725  C  CA  . LEU B 2  723  ? -52.282 -33.482  15.608  1.00 92.77  ?  723  LEU B CA  1 
ATOM   6726  C  C   . LEU B 2  723  ? -51.097 -34.436  15.529  1.00 89.28  ?  723  LEU B C   1 
ATOM   6727  O  O   . LEU B 2  723  ? -51.258 -35.651  15.678  1.00 94.54  ?  723  LEU B O   1 
ATOM   6728  C  CB  . LEU B 2  723  ? -53.022 -33.630  16.934  1.00 89.20  ?  723  LEU B CB  1 
ATOM   6729  C  CG  . LEU B 2  723  ? -52.177 -33.409  18.190  1.00 91.61  ?  723  LEU B CG  1 
ATOM   6730  C  CD1 . LEU B 2  723  ? -51.582 -32.012  18.190  1.00 90.59  ?  723  LEU B CD1 1 
ATOM   6731  C  CD2 . LEU B 2  723  ? -53.002 -33.645  19.451  1.00 93.40  ?  723  LEU B CD2 1 
ATOM   6732  N  N   . LEU B 2  724  ? -49.910 -33.885  15.288  1.00 88.15  ?  724  LEU B N   1 
ATOM   6733  C  CA  . LEU B 2  724  ? -48.663 -34.635  15.327  1.00 91.77  ?  724  LEU B CA  1 
ATOM   6734  C  C   . LEU B 2  724  ? -47.924 -34.298  16.614  1.00 90.74  ?  724  LEU B C   1 
ATOM   6735  O  O   . LEU B 2  724  ? -47.914 -33.144  17.053  1.00 92.58  ?  724  LEU B O   1 
ATOM   6736  C  CB  . LEU B 2  724  ? -47.791 -34.316  14.110  1.00 80.46  ?  724  LEU B CB  1 
ATOM   6737  C  CG  . LEU B 2  724  ? -48.205 -35.000  12.805  1.00 82.17  ?  724  LEU B CG  1 
ATOM   6738  C  CD1 . LEU B 2  724  ? -47.205 -34.724  11.689  1.00 78.89  ?  724  LEU B CD1 1 
ATOM   6739  C  CD2 . LEU B 2  724  ? -48.383 -36.499  13.012  1.00 88.83  ?  724  LEU B CD2 1 
ATOM   6740  N  N   . VAL B 2  725  ? -47.310 -35.309  17.222  1.00 81.24  ?  725  VAL B N   1 
ATOM   6741  C  CA  . VAL B 2  725  ? -46.751 -35.194  18.564  1.00 78.60  ?  725  VAL B CA  1 
ATOM   6742  C  C   . VAL B 2  725  ? -45.235 -35.378  18.510  1.00 75.06  ?  725  VAL B C   1 
ATOM   6743  O  O   . VAL B 2  725  ? -44.735 -36.339  17.912  1.00 78.73  ?  725  VAL B O   1 
ATOM   6744  C  CB  . VAL B 2  725  ? -47.434 -36.182  19.531  1.00 79.24  ?  725  VAL B CB  1 
ATOM   6745  C  CG1 . VAL B 2  725  ? -48.937 -36.124  19.340  1.00 83.05  ?  725  VAL B CG1 1 
ATOM   6746  C  CG2 . VAL B 2  725  ? -47.020 -37.610  19.243  1.00 82.06  ?  725  VAL B CG2 1 
ATOM   6747  N  N   . SER B 2  726  ? -44.509 -34.449  19.136  1.00 87.21  ?  726  SER B N   1 
ATOM   6748  C  CA  . SER B 2  726  ? -43.054 -34.416  19.117  1.00 88.01  ?  726  SER B CA  1 
ATOM   6749  C  C   . SER B 2  726  ? -42.536 -34.250  20.536  1.00 92.94  ?  726  SER B C   1 
ATOM   6750  O  O   . SER B 2  726  ? -43.167 -33.580  21.360  1.00 92.03  ?  726  SER B O   1 
ATOM   6751  C  CB  . SER B 2  726  ? -42.538 -33.276  18.234  1.00 88.45  ?  726  SER B CB  1 
ATOM   6752  O  OG  . SER B 2  726  ? -41.127 -33.182  18.288  1.00 87.19  ?  726  SER B OG  1 
ATOM   6753  N  N   . THR B 2  727  ? -41.391 -34.866  20.816  1.00 74.21  ?  727  THR B N   1 
ATOM   6754  C  CA  . THR B 2  727  ? -40.816 -34.866  22.153  1.00 63.40  ?  727  THR B CA  1 
ATOM   6755  C  C   . THR B 2  727  ? -39.873 -33.697  22.398  1.00 55.31  ?  727  THR B C   1 
ATOM   6756  O  O   . THR B 2  727  ? -39.373 -33.555  23.518  1.00 66.07  ?  727  THR B O   1 
ATOM   6757  C  CB  . THR B 2  727  ? -40.075 -36.182  22.414  1.00 60.96  ?  727  THR B CB  1 
ATOM   6758  O  OG1 . THR B 2  727  ? -39.211 -36.483  21.308  1.00 54.68  ?  727  THR B OG1 1 
ATOM   6759  C  CG2 . THR B 2  727  ? -41.064 -37.319  22.606  1.00 55.69  ?  727  THR B CG2 1 
ATOM   6760  N  N   . GLN B 2  728  ? -39.625 -32.852  21.397  1.00 49.40  ?  728  GLN B N   1 
ATOM   6761  C  CA  . GLN B 2  728  ? -38.698 -31.735  21.552  1.00 53.58  ?  728  GLN B CA  1 
ATOM   6762  C  C   . GLN B 2  728  ? -39.346 -30.382  21.293  1.00 71.49  ?  728  GLN B C   1 
ATOM   6763  O  O   . GLN B 2  728  ? -39.200 -29.466  22.112  1.00 80.94  ?  728  GLN B O   1 
ATOM   6764  C  CB  . GLN B 2  728  ? -37.486 -31.924  20.631  1.00 50.25  ?  728  GLN B CB  1 
ATOM   6765  C  CG  . GLN B 2  728  ? -36.318 -31.020  20.974  1.00 49.41  ?  728  GLN B CG  1 
ATOM   6766  C  CD  . GLN B 2  728  ? -34.986 -31.579  20.520  1.00 53.38  ?  728  GLN B CD  1 
ATOM   6767  O  OE1 . GLN B 2  728  ? -34.745 -32.785  20.594  1.00 56.88  ?  728  GLN B OE1 1 
ATOM   6768  N  NE2 . GLN B 2  728  ? -34.114 -30.704  20.041  1.00 62.15  ?  728  GLN B NE2 1 
ATOM   6769  N  N   . ASP B 2  729  ? -40.028 -30.222  20.160  1.00 80.35  ?  729  ASP B N   1 
ATOM   6770  C  CA  . ASP B 2  729  ? -40.801 -29.030  19.818  1.00 90.50  ?  729  ASP B CA  1 
ATOM   6771  C  C   . ASP B 2  729  ? -39.931 -27.801  19.576  1.00 92.77  ?  729  ASP B C   1 
ATOM   6772  O  O   . ASP B 2  729  ? -40.454 -26.763  19.168  1.00 99.40  ?  729  ASP B O   1 
ATOM   6773  C  CB  . ASP B 2  729  ? -41.852 -28.709  20.892  1.00 95.50  ?  729  ASP B CB  1 
ATOM   6774  C  CG  . ASP B 2  729  ? -43.027 -29.663  20.860  1.00 109.64 ?  729  ASP B CG  1 
ATOM   6775  O  OD1 . ASP B 2  729  ? -43.262 -30.284  19.798  1.00 111.67 ?  729  ASP B OD1 1 
ATOM   6776  O  OD2 . ASP B 2  729  ? -43.693 -29.811  21.907  1.00 107.59 -1 729  ASP B OD2 1 
ATOM   6777  N  N   . HIS B 2  730  ? -38.619 -27.889  19.796  1.00 77.24  ?  730  HIS B N   1 
ATOM   6778  C  CA  . HIS B 2  730  ? -37.693 -26.815  19.450  1.00 74.71  ?  730  HIS B CA  1 
ATOM   6779  C  C   . HIS B 2  730  ? -36.473 -27.434  18.793  1.00 73.61  ?  730  HIS B C   1 
ATOM   6780  O  O   . HIS B 2  730  ? -35.817 -28.293  19.388  1.00 73.46  ?  730  HIS B O   1 
ATOM   6781  C  CB  . HIS B 2  730  ? -37.288 -25.999  20.677  1.00 71.83  ?  730  HIS B CB  1 
ATOM   6782  C  CG  . HIS B 2  730  ? -36.880 -24.599  20.350  1.00 72.98  ?  730  HIS B CG  1 
ATOM   6783  N  ND1 . HIS B 2  730  ? -37.768 -23.658  19.877  1.00 67.47  ?  730  HIS B ND1 1 
ATOM   6784  C  CD2 . HIS B 2  730  ? -35.678 -23.982  20.418  1.00 73.72  ?  730  HIS B CD2 1 
ATOM   6785  C  CE1 . HIS B 2  730  ? -37.131 -22.519  19.671  1.00 62.99  ?  730  HIS B CE1 1 
ATOM   6786  N  NE2 . HIS B 2  730  ? -35.861 -22.689  19.993  1.00 67.63  ?  730  HIS B NE2 1 
ATOM   6787  N  N   . TRP B 2  731  ? -36.172 -27.000  17.569  1.00 79.52  ?  731  TRP B N   1 
ATOM   6788  C  CA  . TRP B 2  731  ? -35.173 -27.647  16.731  1.00 71.53  ?  731  TRP B CA  1 
ATOM   6789  C  C   . TRP B 2  731  ? -33.873 -26.862  16.638  1.00 70.52  ?  731  TRP B C   1 
ATOM   6790  O  O   . TRP B 2  731  ? -33.025 -27.200  15.808  1.00 71.91  ?  731  TRP B O   1 
ATOM   6791  C  CB  . TRP B 2  731  ? -35.723 -27.863  15.320  1.00 78.62  ?  731  TRP B CB  1 
ATOM   6792  C  CG  . TRP B 2  731  ? -37.077 -28.500  15.240  1.00 82.57  ?  731  TRP B CG  1 
ATOM   6793  C  CD1 . TRP B 2  731  ? -37.762 -29.128  16.241  1.00 73.82  ?  731  TRP B CD1 1 
ATOM   6794  C  CD2 . TRP B 2  731  ? -37.908 -28.578  14.077  1.00 81.71  ?  731  TRP B CD2 1 
ATOM   6795  N  NE1 . TRP B 2  731  ? -38.968 -29.591  15.772  1.00 74.64  ?  731  TRP B NE1 1 
ATOM   6796  C  CE2 . TRP B 2  731  ? -39.081 -29.265  14.445  1.00 80.54  ?  731  TRP B CE2 1 
ATOM   6797  C  CE3 . TRP B 2  731  ? -37.772 -28.131  12.759  1.00 71.64  ?  731  TRP B CE3 1 
ATOM   6798  C  CZ2 . TRP B 2  731  ? -40.112 -29.515  13.543  1.00 76.17  ?  731  TRP B CZ2 1 
ATOM   6799  C  CZ3 . TRP B 2  731  ? -38.794 -28.380  11.866  1.00 79.74  ?  731  TRP B CZ3 1 
ATOM   6800  C  CH2 . TRP B 2  731  ? -39.950 -29.065  12.261  1.00 79.60  ?  731  TRP B CH2 1 
ATOM   6801  N  N   . THR B 2  732  ? -33.702 -25.809  17.434  1.00 77.14  ?  732  THR B N   1 
ATOM   6802  C  CA  . THR B 2  732  ? -32.516 -24.967  17.326  1.00 76.38  ?  732  THR B CA  1 
ATOM   6803  C  C   . THR B 2  732  ? -32.032 -24.561  18.709  1.00 75.99  ?  732  THR B C   1 
ATOM   6804  O  O   . THR B 2  732  ? -32.830 -24.133  19.547  1.00 80.60  ?  732  THR B O   1 
ATOM   6805  C  CB  . THR B 2  732  ? -32.796 -23.708  16.493  1.00 78.61  ?  732  THR B CB  1 
ATOM   6806  O  OG1 . THR B 2  732  ? -34.084 -23.181  16.832  1.00 89.65  ?  732  THR B OG1 1 
ATOM   6807  C  CG2 . THR B 2  732  ? -32.751 -24.026  15.004  1.00 84.82  ?  732  THR B CG2 1 
ATOM   6808  N  N   . LEU B 2  733  ? -30.726 -24.686  18.940  1.00 84.55  ?  733  LEU B N   1 
ATOM   6809  C  CA  . LEU B 2  733  ? -30.125 -24.184  20.169  1.00 84.78  ?  733  LEU B CA  1 
ATOM   6810  C  C   . LEU B 2  733  ? -29.899 -22.680  20.040  1.00 92.27  ?  733  LEU B C   1 
ATOM   6811  O  O   . LEU B 2  733  ? -29.265 -22.217  19.087  1.00 99.10  ?  733  LEU B O   1 
ATOM   6812  C  CB  . LEU B 2  733  ? -28.817 -24.919  20.478  1.00 86.97  ?  733  LEU B CB  1 
ATOM   6813  C  CG  . LEU B 2  733  ? -27.553 -24.736  19.632  1.00 90.47  ?  733  LEU B CG  1 
ATOM   6814  C  CD1 . LEU B 2  733  ? -26.345 -25.245  20.396  1.00 82.89  ?  733  LEU B CD1 1 
ATOM   6815  C  CD2 . LEU B 2  733  ? -27.666 -25.448  18.290  1.00 83.33  ?  733  LEU B CD2 1 
ATOM   6816  N  N   . GLU B 2  734  ? -30.442 -21.918  20.991  1.00 70.10  ?  734  GLU B N   1 
ATOM   6817  C  CA  . GLU B 2  734  ? -30.497 -20.458  20.889  1.00 70.79  ?  734  GLU B CA  1 
ATOM   6818  C  C   . GLU B 2  734  ? -29.164 -19.846  21.326  1.00 73.72  ?  734  GLU B C   1 
ATOM   6819  O  O   . GLU B 2  734  ? -29.047 -19.179  22.357  1.00 72.52  ?  734  GLU B O   1 
ATOM   6820  C  CB  . GLU B 2  734  ? -31.658 -19.916  21.713  1.00 75.75  ?  734  GLU B CB  1 
ATOM   6821  C  CG  . GLU B 2  734  ? -33.025 -20.413  21.262  1.00 75.75  ?  734  GLU B CG  1 
ATOM   6822  C  CD  . GLU B 2  734  ? -33.441 -19.848  19.916  1.00 73.78  ?  734  GLU B CD  1 
ATOM   6823  O  OE1 . GLU B 2  734  ? -33.442 -18.609  19.763  1.00 73.46  ?  734  GLU B OE1 1 
ATOM   6824  O  OE2 . GLU B 2  734  ? -33.775 -20.644  19.013  1.00 75.67  -1 734  GLU B OE2 1 
ATOM   6825  N  N   . GLY B 2  735  ? -28.146 -20.079  20.497  1.00 98.00  ?  735  GLY B N   1 
ATOM   6826  C  CA  . GLY B 2  735  ? -26.831 -19.496  20.692  1.00 97.41  ?  735  GLY B CA  1 
ATOM   6827  C  C   . GLY B 2  735  ? -26.242 -19.737  22.065  1.00 95.55  ?  735  GLY B C   1 
ATOM   6828  O  O   . GLY B 2  735  ? -25.825 -18.794  22.745  1.00 87.90  ?  735  GLY B O   1 
ATOM   6829  N  N   . ARG B 2  736  ? -26.203 -20.996  22.485  1.00 86.90  ?  736  ARG B N   1 
ATOM   6830  C  CA  . ARG B 2  736  ? -25.695 -21.364  23.795  1.00 77.56  ?  736  ARG B CA  1 
ATOM   6831  C  C   . ARG B 2  736  ? -24.602 -22.414  23.641  1.00 71.79  ?  736  ARG B C   1 
ATOM   6832  O  O   . ARG B 2  736  ? -24.389 -22.975  22.562  1.00 75.08  ?  736  ARG B O   1 
ATOM   6833  C  CB  . ARG B 2  736  ? -26.826 -21.877  24.696  1.00 76.72  ?  736  ARG B CB  1 
ATOM   6834  C  CG  . ARG B 2  736  ? -27.790 -20.786  25.138  1.00 77.62  ?  736  ARG B CG  1 
ATOM   6835  C  CD  . ARG B 2  736  ? -29.140 -21.351  25.560  1.00 77.43  ?  736  ARG B CD  1 
ATOM   6836  N  NE  . ARG B 2  736  ? -30.133 -20.294  25.721  1.00 86.67  ?  736  ARG B NE  1 
ATOM   6837  C  CZ  . ARG B 2  736  ? -31.320 -20.455  26.290  1.00 78.21  ?  736  ARG B CZ  1 
ATOM   6838  N  NH1 . ARG B 2  736  ? -31.706 -21.626  26.768  1.00 78.70  ?  736  ARG B NH1 1 
ATOM   6839  N  NH2 . ARG B 2  736  ? -32.140 -19.412  26.384  1.00 66.47  ?  736  ARG B NH2 1 
ATOM   6840  N  N   . ASP B 2  737  ? -23.902 -22.679  24.740  1.00 65.97  ?  737  ASP B N   1 
ATOM   6841  C  CA  . ASP B 2  737  ? -22.787 -23.625  24.737  1.00 68.30  ?  737  ASP B CA  1 
ATOM   6842  C  C   . ASP B 2  737  ? -23.269 -25.036  25.082  1.00 70.28  ?  737  ASP B C   1 
ATOM   6843  O  O   . ASP B 2  737  ? -22.814 -25.665  26.035  1.00 71.58  ?  737  ASP B O   1 
ATOM   6844  C  CB  . ASP B 2  737  ? -21.703 -23.161  25.701  1.00 68.97  ?  737  ASP B CB  1 
ATOM   6845  C  CG  . ASP B 2  737  ? -20.362 -23.806  25.422  1.00 63.81  ?  737  ASP B CG  1 
ATOM   6846  O  OD1 . ASP B 2  737  ? -20.153 -24.280  24.287  1.00 71.27  ?  737  ASP B OD1 1 
ATOM   6847  O  OD2 . ASP B 2  737  ? -19.516 -23.839  26.339  1.00 66.86  -1 737  ASP B OD2 1 
ATOM   6848  N  N   . ILE B 2  738  ? -24.209 -25.527  24.279  1.00 75.81  ?  738  ILE B N   1 
ATOM   6849  C  CA  . ILE B 2  738  ? -24.747 -26.874  24.458  1.00 70.28  ?  738  ILE B CA  1 
ATOM   6850  C  C   . ILE B 2  738  ? -23.929 -27.902  23.689  1.00 70.28  ?  738  ILE B C   1 
ATOM   6851  O  O   . ILE B 2  738  ? -23.576 -28.959  24.218  1.00 65.72  ?  738  ILE B O   1 
ATOM   6852  C  CB  . ILE B 2  738  ? -26.233 -26.913  24.036  1.00 65.80  ?  738  ILE B CB  1 
ATOM   6853  C  CG1 . ILE B 2  738  ? -26.954 -25.632  24.467  1.00 67.52  ?  738  ILE B CG1 1 
ATOM   6854  C  CG2 . ILE B 2  738  ? -26.918 -28.145  24.607  1.00 58.19  ?  738  ILE B CG2 1 
ATOM   6855  C  CD1 . ILE B 2  738  ? -26.958 -25.402  25.964  1.00 62.50  ?  738  ILE B CD1 1 
ATOM   6856  N  N   . TYR B 2  739  ? -23.608 -27.599  22.434  1.00 72.75  ?  739  TYR B N   1 
ATOM   6857  C  CA  . TYR B 2  739  ? -22.901 -28.510  21.546  1.00 60.30  ?  739  TYR B CA  1 
ATOM   6858  C  C   . TYR B 2  739  ? -21.630 -27.832  21.055  1.00 60.36  ?  739  TYR B C   1 
ATOM   6859  O  O   . TYR B 2  739  ? -21.676 -26.690  20.586  1.00 66.85  ?  739  TYR B O   1 
ATOM   6860  C  CB  . TYR B 2  739  ? -23.792 -28.908  20.365  1.00 63.31  ?  739  TYR B CB  1 
ATOM   6861  C  CG  . TYR B 2  739  ? -23.426 -30.217  19.707  1.00 64.45  ?  739  TYR B CG  1 
ATOM   6862  C  CD1 . TYR B 2  739  ? -22.431 -30.278  18.741  1.00 69.47  ?  739  TYR B CD1 1 
ATOM   6863  C  CD2 . TYR B 2  739  ? -24.086 -31.392  20.042  1.00 66.95  ?  739  TYR B CD2 1 
ATOM   6864  C  CE1 . TYR B 2  739  ? -22.098 -31.473  18.133  1.00 69.17  ?  739  TYR B CE1 1 
ATOM   6865  C  CE2 . TYR B 2  739  ? -23.760 -32.592  19.440  1.00 73.12  ?  739  TYR B CE2 1 
ATOM   6866  C  CZ  . TYR B 2  739  ? -22.765 -32.626  18.486  1.00 71.52  ?  739  TYR B CZ  1 
ATOM   6867  O  OH  . TYR B 2  739  ? -22.436 -33.818  17.883  1.00 66.39  ?  739  TYR B OH  1 
ATOM   6868  N  N   . ARG B 2  740  ? -20.502 -28.530  21.165  1.00 42.24  ?  740  ARG B N   1 
ATOM   6869  C  CA  . ARG B 2  740  ? -19.200 -27.992  20.794  1.00 44.19  ?  740  ARG B CA  1 
ATOM   6870  C  C   . ARG B 2  740  ? -18.640 -28.766  19.608  1.00 46.01  ?  740  ARG B C   1 
ATOM   6871  O  O   . ARG B 2  740  ? -18.605 -30.001  19.628  1.00 44.30  ?  740  ARG B O   1 
ATOM   6872  C  CB  . ARG B 2  740  ? -18.227 -28.052  21.975  1.00 46.79  ?  740  ARG B CB  1 
ATOM   6873  C  CG  . ARG B 2  740  ? -18.587 -27.118  23.120  1.00 46.02  ?  740  ARG B CG  1 
ATOM   6874  C  CD  . ARG B 2  740  ? -17.437 -26.977  24.105  1.00 48.57  ?  740  ARG B CD  1 
ATOM   6875  N  NE  . ARG B 2  740  ? -17.820 -26.219  25.291  1.00 46.85  ?  740  ARG B NE  1 
ATOM   6876  C  CZ  . ARG B 2  740  ? -17.027 -26.010  26.333  1.00 52.09  ?  740  ARG B CZ  1 
ATOM   6877  N  NH1 . ARG B 2  740  ? -15.795 -26.490  26.372  1.00 61.09  ?  740  ARG B NH1 1 
ATOM   6878  N  NH2 . ARG B 2  740  ? -17.481 -25.296  27.360  1.00 49.34  ?  740  ARG B NH2 1 
ATOM   6879  N  N   . VAL B 2  741  ? -18.205 -28.039  18.580  1.00 71.55  ?  741  VAL B N   1 
ATOM   6880  C  CA  . VAL B 2  741  ? -17.685 -28.627  17.351  1.00 62.04  ?  741  VAL B CA  1 
ATOM   6881  C  C   . VAL B 2  741  ? -16.350 -27.974  17.021  1.00 69.15  ?  741  VAL B C   1 
ATOM   6882  O  O   . VAL B 2  741  ? -16.170 -26.769  17.227  1.00 67.48  ?  741  VAL B O   1 
ATOM   6883  C  CB  . VAL B 2  741  ? -18.672 -28.463  16.174  1.00 60.19  ?  741  VAL B CB  1 
ATOM   6884  C  CG1 . VAL B 2  741  ? -18.147 -29.164  14.932  1.00 67.04  ?  741  VAL B CG1 1 
ATOM   6885  C  CG2 . VAL B 2  741  ? -20.042 -28.998  16.544  1.00 68.04  ?  741  VAL B CG2 1 
ATOM   6886  N  N   . GLY B 2  742  ? -15.413 -28.773  16.502  1.00 61.52  ?  742  GLY B N   1 
ATOM   6887  C  CA  . GLY B 2  742  ? -14.119 -28.273  16.091  1.00 62.71  ?  742  GLY B CA  1 
ATOM   6888  C  C   . GLY B 2  742  ? -13.639 -28.959  14.825  1.00 59.25  ?  742  GLY B C   1 
ATOM   6889  O  O   . GLY B 2  742  ? -14.337 -29.793  14.247  1.00 56.92  ?  742  GLY B O   1 
ATOM   6890  N  N   . GLU B 2  743  ? -12.433 -28.585  14.405  1.00 82.46  ?  743  GLU B N   1 
ATOM   6891  C  CA  . GLU B 2  743  ? -11.779 -29.169  13.243  1.00 73.88  ?  743  GLU B CA  1 
ATOM   6892  C  C   . GLU B 2  743  ? -10.583 -30.005  13.683  1.00 78.40  ?  743  GLU B C   1 
ATOM   6893  O  O   . GLU B 2  743  ? -9.929  -29.702  14.685  1.00 85.92  ?  743  GLU B O   1 
ATOM   6894  C  CB  . GLU B 2  743  ? -11.317 -28.088  12.260  1.00 84.40  ?  743  GLU B CB  1 
ATOM   6895  C  CG  . GLU B 2  743  ? -12.354 -27.699  11.217  1.00 93.29  ?  743  GLU B CG  1 
ATOM   6896  C  CD  . GLU B 2  743  ? -13.141 -26.464  11.609  1.00 106.29 ?  743  GLU B CD  1 
ATOM   6897  O  OE1 . GLU B 2  743  ? -12.766 -25.809  12.604  1.00 109.55 ?  743  GLU B OE1 1 
ATOM   6898  O  OE2 . GLU B 2  743  ? -14.134 -26.147  10.919  1.00 108.21 -1 743  GLU B OE2 1 
ATOM   6899  N  N   . PHE B 2  744  ? -10.297 -31.059  12.914  1.00 53.93  ?  744  PHE B N   1 
ATOM   6900  C  CA  . PHE B 2  744  ? -9.207  -31.959  13.275  1.00 60.48  ?  744  PHE B CA  1 
ATOM   6901  C  C   . PHE B 2  744  ? -7.841  -31.326  13.046  1.00 70.40  ?  744  PHE B C   1 
ATOM   6902  O  O   . PHE B 2  744  ? -6.897  -31.616  13.790  1.00 72.62  ?  744  PHE B O   1 
ATOM   6903  C  CB  . PHE B 2  744  ? -9.319  -33.267  12.491  1.00 66.52  ?  744  PHE B CB  1 
ATOM   6904  C  CG  . PHE B 2  744  ? -8.312  -34.304  12.900  1.00 70.50  ?  744  PHE B CG  1 
ATOM   6905  C  CD1 . PHE B 2  744  ? -8.168  -34.662  14.230  1.00 63.44  ?  744  PHE B CD1 1 
ATOM   6906  C  CD2 . PHE B 2  744  ? -7.509  -34.919  11.954  1.00 73.19  ?  744  PHE B CD2 1 
ATOM   6907  C  CE1 . PHE B 2  744  ? -7.240  -35.614  14.609  1.00 63.22  ?  744  PHE B CE1 1 
ATOM   6908  C  CE2 . PHE B 2  744  ? -6.580  -35.873  12.327  1.00 69.53  ?  744  PHE B CE2 1 
ATOM   6909  C  CZ  . PHE B 2  744  ? -6.446  -36.220  13.656  1.00 64.39  ?  744  PHE B CZ  1 
ATOM   6910  N  N   . LYS B 2  745  ? -7.712  -30.471  12.029  1.00 94.93  ?  745  LYS B N   1 
ATOM   6911  C  CA  . LYS B 2  745  ? -6.425  -29.839  11.762  1.00 96.29  ?  745  LYS B CA  1 
ATOM   6912  C  C   . LYS B 2  745  ? -6.020  -28.910  12.901  1.00 95.71  ?  745  LYS B C   1 
ATOM   6913  O  O   . LYS B 2  745  ? -4.841  -28.850  13.270  1.00 96.16  ?  745  LYS B O   1 
ATOM   6914  C  CB  . LYS B 2  745  ? -6.475  -29.081  10.435  1.00 101.59 ?  745  LYS B CB  1 
ATOM   6915  C  CG  . LYS B 2  745  ? -5.976  -29.888  9.245   1.00 105.20 ?  745  LYS B CG  1 
ATOM   6916  C  CD  . LYS B 2  745  ? -5.783  -29.010  8.019   1.00 118.61 ?  745  LYS B CD  1 
ATOM   6917  C  CE  . LYS B 2  745  ? -7.076  -28.315  7.622   1.00 128.44 ?  745  LYS B CE  1 
ATOM   6918  N  NZ  . LYS B 2  745  ? -8.008  -29.236  6.914   1.00 121.10 ?  745  LYS B NZ  1 
ATOM   6919  N  N   . LYS B 2  746  ? -6.981  -28.182  13.472  1.00 77.07  ?  746  LYS B N   1 
ATOM   6920  C  CA  . LYS B 2  746  ? -6.689  -27.338  14.625  1.00 78.16  ?  746  LYS B CA  1 
ATOM   6921  C  C   . LYS B 2  746  ? -6.638  -28.143  15.917  1.00 73.38  ?  746  LYS B C   1 
ATOM   6922  O  O   . LYS B 2  746  ? -5.934  -27.756  16.856  1.00 72.52  ?  746  LYS B O   1 
ATOM   6923  C  CB  . LYS B 2  746  ? -7.731  -26.224  14.743  1.00 73.88  ?  746  LYS B CB  1 
ATOM   6924  C  CG  . LYS B 2  746  ? -7.747  -25.259  13.570  1.00 71.12  ?  746  LYS B CG  1 
ATOM   6925  C  CD  . LYS B 2  746  ? -8.772  -24.158  13.780  1.00 69.98  ?  746  LYS B CD  1 
ATOM   6926  C  CE  . LYS B 2  746  ? -8.760  -23.165  12.630  1.00 91.89  ?  746  LYS B CE  1 
ATOM   6927  N  NZ  . LYS B 2  746  ? -9.723  -22.051  12.847  1.00 94.36  ?  746  LYS B NZ  1 
ATOM   6928  N  N   . PHE B 2  747  ? -7.373  -29.256  15.981  1.00 59.58  ?  747  PHE B N   1 
ATOM   6929  C  CA  . PHE B 2  747  ? -7.353  -30.096  17.173  1.00 59.55  ?  747  PHE B CA  1 
ATOM   6930  C  C   . PHE B 2  747  ? -5.999  -30.767  17.364  1.00 64.99  ?  747  PHE B C   1 
ATOM   6931  O  O   . PHE B 2  747  ? -5.574  -30.986  18.504  1.00 65.20  ?  747  PHE B O   1 
ATOM   6932  C  CB  . PHE B 2  747  ? -8.467  -31.142  17.085  1.00 58.11  ?  747  PHE B CB  1 
ATOM   6933  C  CG  . PHE B 2  747  ? -8.445  -32.161  18.190  1.00 61.55  ?  747  PHE B CG  1 
ATOM   6934  C  CD1 . PHE B 2  747  ? -9.059  -31.898  19.404  1.00 56.07  ?  747  PHE B CD1 1 
ATOM   6935  C  CD2 . PHE B 2  747  ? -7.831  -33.391  18.009  1.00 65.15  ?  747  PHE B CD2 1 
ATOM   6936  C  CE1 . PHE B 2  747  ? -9.049  -32.836  20.420  1.00 53.15  ?  747  PHE B CE1 1 
ATOM   6937  C  CE2 . PHE B 2  747  ? -7.817  -34.331  19.022  1.00 56.74  ?  747  PHE B CE2 1 
ATOM   6938  C  CZ  . PHE B 2  747  ? -8.426  -34.053  20.229  1.00 50.25  ?  747  PHE B CZ  1 
ATOM   6939  N  N   . LYS B 2  748  ? -5.309  -31.094  16.267  1.00 98.85  ?  748  LYS B N   1 
ATOM   6940  C  CA  . LYS B 2  748  ? -4.009  -31.749  16.373  1.00 102.02 ?  748  LYS B CA  1 
ATOM   6941  C  C   . LYS B 2  748  ? -2.989  -30.856  17.069  1.00 107.53 ?  748  LYS B C   1 
ATOM   6942  O  O   . LYS B 2  748  ? -2.236  -31.318  17.934  1.00 106.46 ?  748  LYS B O   1 
ATOM   6943  C  CB  . LYS B 2  748  ? -3.508  -32.145  14.984  1.00 105.79 ?  748  LYS B CB  1 
ATOM   6944  C  CG  . LYS B 2  748  ? -4.139  -33.410  14.428  1.00 103.00 ?  748  LYS B CG  1 
ATOM   6945  C  CD  . LYS B 2  748  ? -3.868  -33.553  12.936  1.00 109.26 ?  748  LYS B CD  1 
ATOM   6946  C  CE  . LYS B 2  748  ? -2.397  -33.344  12.609  1.00 101.91 ?  748  LYS B CE  1 
ATOM   6947  N  NZ  . LYS B 2  748  ? -1.518  -34.297  13.340  1.00 96.37  ?  748  LYS B NZ  1 
ATOM   6948  N  N   . GLU B 2  749  ? -2.949  -29.572  16.704  1.00 114.08 ?  749  GLU B N   1 
ATOM   6949  C  CA  . GLU B 2  749  ? -1.976  -28.664  17.304  1.00 112.17 ?  749  GLU B CA  1 
ATOM   6950  C  C   . GLU B 2  749  ? -2.307  -28.385  18.765  1.00 109.99 ?  749  GLU B C   1 
ATOM   6951  O  O   . GLU B 2  749  ? -1.402  -28.259  19.599  1.00 117.93 ?  749  GLU B O   1 
ATOM   6952  C  CB  . GLU B 2  749  ? -1.912  -27.361  16.507  1.00 112.11 ?  749  GLU B CB  1 
ATOM   6953  C  CG  . GLU B 2  749  ? -2.066  -27.539  15.001  1.00 132.68 ?  749  GLU B CG  1 
ATOM   6954  C  CD  . GLU B 2  749  ? -1.046  -28.501  14.413  1.00 141.72 ?  749  GLU B CD  1 
ATOM   6955  O  OE1 . GLU B 2  749  ? 0.141   -28.419  14.795  1.00 139.14 ?  749  GLU B OE1 1 
ATOM   6956  O  OE2 . GLU B 2  749  ? -1.432  -29.338  13.569  1.00 127.35 -1 749  GLU B OE2 1 
ATOM   6957  N  N   . ASP B 2  750  ? -3.592  -28.284  19.094  1.00 96.71  ?  750  ASP B N   1 
ATOM   6958  C  CA  . ASP B 2  750  ? -4.015  -28.048  20.469  1.00 100.97 ?  750  ASP B CA  1 
ATOM   6959  C  C   . ASP B 2  750  ? -5.391  -28.657  20.708  1.00 95.53  ?  750  ASP B C   1 
ATOM   6960  O  O   . ASP B 2  750  ? -6.391  -28.163  20.171  1.00 97.25  ?  750  ASP B O   1 
ATOM   6961  C  CB  . ASP B 2  750  ? -4.037  -26.552  20.783  1.00 100.34 ?  750  ASP B CB  1 
ATOM   6962  C  CG  . ASP B 2  750  ? -4.118  -26.270  22.272  1.00 105.63 ?  750  ASP B CG  1 
ATOM   6963  O  OD1 . ASP B 2  750  ? -4.115  -27.236  23.065  1.00 106.99 ?  750  ASP B OD1 1 
ATOM   6964  O  OD2 . ASP B 2  750  ? -4.189  -25.083  22.650  1.00 112.49 -1 750  ASP B OD2 1 
ATOM   6965  N  N   . PRO B 2  751  ? -5.488  -29.721  21.511  1.00 71.53  ?  751  PRO B N   1 
ATOM   6966  C  CA  . PRO B 2  751  ? -6.799  -30.339  21.762  1.00 65.89  ?  751  PRO B CA  1 
ATOM   6967  C  C   . PRO B 2  751  ? -7.729  -29.489  22.611  1.00 61.28  ?  751  PRO B C   1 
ATOM   6968  O  O   . PRO B 2  751  ? -8.909  -29.839  22.740  1.00 52.35  ?  751  PRO B O   1 
ATOM   6969  C  CB  . PRO B 2  751  ? -6.436  -31.643  22.484  1.00 56.06  ?  751  PRO B CB  1 
ATOM   6970  C  CG  . PRO B 2  751  ? -5.126  -31.350  23.136  1.00 60.96  ?  751  PRO B CG  1 
ATOM   6971  C  CD  . PRO B 2  751  ? -4.396  -30.440  22.190  1.00 70.30  ?  751  PRO B CD  1 
ATOM   6972  N  N   . LYS B 2  752  ? -7.245  -28.390  23.185  1.00 80.10  ?  752  LYS B N   1 
ATOM   6973  C  CA  . LYS B 2  752  ? -8.028  -27.564  24.092  1.00 80.94  ?  752  LYS B CA  1 
ATOM   6974  C  C   . LYS B 2  752  ? -8.548  -26.291  23.434  1.00 81.38  ?  752  LYS B C   1 
ATOM   6975  O  O   . LYS B 2  752  ? -9.040  -25.401  24.136  1.00 75.54  ?  752  LYS B O   1 
ATOM   6976  C  CB  . LYS B 2  752  ? -7.189  -27.206  25.322  1.00 82.40  ?  752  LYS B CB  1 
ATOM   6977  C  CG  . LYS B 2  752  ? -7.952  -27.205  26.636  1.00 80.22  ?  752  LYS B CG  1 
ATOM   6978  C  CD  . LYS B 2  752  ? -7.011  -26.966  27.807  1.00 70.17  ?  752  LYS B CD  1 
ATOM   6979  C  CE  . LYS B 2  752  ? -5.869  -27.966  27.811  1.00 79.95  ?  752  LYS B CE  1 
ATOM   6980  N  NZ  . LYS B 2  752  ? -4.945  -27.759  28.958  1.00 65.24  ?  752  LYS B NZ  1 
ATOM   6981  N  N   . TYR B 2  753  ? -8.473  -26.190  22.105  1.00 85.81  ?  753  TYR B N   1 
ATOM   6982  C  CA  . TYR B 2  753  ? -8.768  -24.920  21.445  1.00 88.01  ?  753  TYR B CA  1 
ATOM   6983  C  C   . TYR B 2  753  ? -10.258 -24.602  21.441  1.00 88.81  ?  753  TYR B C   1 
ATOM   6984  O  O   . TYR B 2  753  ? -10.635 -23.424  21.468  1.00 85.88  ?  753  TYR B O   1 
ATOM   6985  C  CB  . TYR B 2  753  ? -8.198  -24.933  20.023  1.00 78.67  ?  753  TYR B CB  1 
ATOM   6986  C  CG  . TYR B 2  753  ? -9.182  -25.263  18.921  1.00 77.48  ?  753  TYR B CG  1 
ATOM   6987  C  CD1 . TYR B 2  753  ? -9.402  -26.577  18.532  1.00 76.64  ?  753  TYR B CD1 1 
ATOM   6988  C  CD2 . TYR B 2  753  ? -9.863  -24.257  18.246  1.00 82.05  ?  753  TYR B CD2 1 
ATOM   6989  C  CE1 . TYR B 2  753  ? -10.288 -26.881  17.517  1.00 73.80  ?  753  TYR B CE1 1 
ATOM   6990  C  CE2 . TYR B 2  753  ? -10.753 -24.553  17.231  1.00 81.52  ?  753  TYR B CE2 1 
ATOM   6991  C  CZ  . TYR B 2  753  ? -10.961 -25.865  16.870  1.00 76.99  ?  753  TYR B CZ  1 
ATOM   6992  O  OH  . TYR B 2  753  ? -11.845 -26.156  15.857  1.00 76.21  ?  753  TYR B OH  1 
ATOM   6993  N  N   . ILE B 2  754  ? -11.117 -25.623  21.415  1.00 75.13  ?  754  ILE B N   1 
ATOM   6994  C  CA  . ILE B 2  754  ? -12.557 -25.372  21.436  1.00 66.60  ?  754  ILE B CA  1 
ATOM   6995  C  C   . ILE B 2  754  ? -12.967 -24.734  22.755  1.00 69.55  ?  754  ILE B C   1 
ATOM   6996  O  O   . ILE B 2  754  ? -13.781 -23.802  22.785  1.00 72.14  ?  754  ILE B O   1 
ATOM   6997  C  CB  . ILE B 2  754  ? -13.338 -26.673  21.177  1.00 59.92  ?  754  ILE B CB  1 
ATOM   6998  C  CG1 . ILE B 2  754  ? -12.612 -27.539  20.147  1.00 64.24  ?  754  ILE B CG1 1 
ATOM   6999  C  CG2 . ILE B 2  754  ? -14.764 -26.361  20.729  1.00 58.77  ?  754  ILE B CG2 1 
ATOM   7000  C  CD1 . ILE B 2  754  ? -13.369 -28.789  19.771  1.00 63.78  ?  754  ILE B CD1 1 
ATOM   7001  N  N   . ALA B 2  755  ? -12.417 -25.228  23.867  1.00 68.29  ?  755  ALA B N   1 
ATOM   7002  C  CA  . ALA B 2  755  ? -12.755 -24.664  25.169  1.00 58.75  ?  755  ALA B CA  1 
ATOM   7003  C  C   . ALA B 2  755  ? -12.187 -23.262  25.342  1.00 68.91  ?  755  ALA B C   1 
ATOM   7004  O  O   . ALA B 2  755  ? -12.797 -22.429  26.017  1.00 71.93  ?  755  ALA B O   1 
ATOM   7005  C  CB  . ALA B 2  755  ? -12.258 -25.585  26.284  1.00 62.80  ?  755  ALA B CB  1 
ATOM   7006  N  N   . LYS B 2  756  ? -11.029 -22.976  24.743  1.00 75.12  ?  756  LYS B N   1 
ATOM   7007  C  CA  . LYS B 2  756  ? -10.471 -21.632  24.846  1.00 80.53  ?  756  LYS B CA  1 
ATOM   7008  C  C   . LYS B 2  756  ? -11.340 -20.627  24.106  1.00 84.08  ?  756  LYS B C   1 
ATOM   7009  O  O   . LYS B 2  756  ? -11.510 -19.490  24.561  1.00 86.69  ?  756  LYS B O   1 
ATOM   7010  C  CB  . LYS B 2  756  ? -9.036  -21.618  24.323  1.00 83.23  ?  756  LYS B CB  1 
ATOM   7011  C  CG  . LYS B 2  756  ? -8.090  -22.417  25.199  1.00 76.07  ?  756  LYS B CG  1 
ATOM   7012  C  CD  . LYS B 2  756  ? -6.649  -22.286  24.758  1.00 80.38  ?  756  LYS B CD  1 
ATOM   7013  C  CE  . LYS B 2  756  ? -5.738  -23.082  25.678  1.00 88.77  ?  756  LYS B CE  1 
ATOM   7014  N  NZ  . LYS B 2  756  ? -4.303  -22.927  25.317  1.00 101.87 ?  756  LYS B NZ  1 
ATOM   7015  N  N   . GLU B 2  757  ? -11.909 -21.034  22.974  1.00 119.80 ?  757  GLU B N   1 
ATOM   7016  C  CA  . GLU B 2  757  ? -12.989 -20.277  22.371  1.00 117.53 ?  757  GLU B CA  1 
ATOM   7017  C  C   . GLU B 2  757  ? -14.218 -20.336  23.277  1.00 119.76 ?  757  GLU B C   1 
ATOM   7018  O  O   . GLU B 2  757  ? -14.231 -21.019  24.306  1.00 117.71 ?  757  GLU B O   1 
ATOM   7019  C  CB  . GLU B 2  757  ? -13.302 -20.813  20.974  1.00 116.34 ?  757  GLU B CB  1 
ATOM   7020  C  CG  . GLU B 2  757  ? -12.143 -20.671  19.997  1.00 127.06 ?  757  GLU B CG  1 
ATOM   7021  C  CD  . GLU B 2  757  ? -12.453 -21.243  18.626  1.00 132.78 ?  757  GLU B CD  1 
ATOM   7022  O  OE1 . GLU B 2  757  ? -13.492 -21.920  18.480  1.00 124.14 ?  757  GLU B OE1 1 
ATOM   7023  O  OE2 . GLU B 2  757  ? -11.650 -21.023  17.694  1.00 135.27 -1 757  GLU B OE2 1 
ATOM   7024  N  N   . VAL B 2  758  ? -15.254 -19.588  22.896  1.00 101.12 ?  758  VAL B N   1 
ATOM   7025  C  CA  . VAL B 2  758  ? -16.460 -19.417  23.705  1.00 103.29 ?  758  VAL B CA  1 
ATOM   7026  C  C   . VAL B 2  758  ? -16.125 -18.638  24.973  1.00 95.64  ?  758  VAL B C   1 
ATOM   7027  O  O   . VAL B 2  758  ? -16.679 -17.558  25.207  1.00 96.69  ?  758  VAL B O   1 
ATOM   7028  C  CB  . VAL B 2  758  ? -17.130 -20.764  24.044  1.00 97.26  ?  758  VAL B CB  1 
ATOM   7029  C  CG1 . VAL B 2  758  ? -18.237 -20.567  25.072  1.00 86.94  ?  758  VAL B CG1 1 
ATOM   7030  C  CG2 . VAL B 2  758  ? -17.672 -21.420  22.785  1.00 102.48 ?  758  VAL B CG2 1 
ATOM   7031  N  N   . TYR B 2  759  ? -15.219 -19.172  25.800  1.00 72.61  ?  759  TYR B N   1 
ATOM   7032  C  CA  . TYR B 2  759  ? -14.863 -18.490  27.042  1.00 77.82  ?  759  TYR B CA  1 
ATOM   7033  C  C   . TYR B 2  759  ? -14.241 -17.124  26.775  1.00 78.57  ?  759  TYR B C   1 
ATOM   7034  O  O   . TYR B 2  759  ? -14.380 -16.210  27.597  1.00 86.58  ?  759  TYR B O   1 
ATOM   7035  C  CB  . TYR B 2  759  ? -13.916 -19.356  27.876  1.00 74.40  ?  759  TYR B CB  1 
ATOM   7036  C  CG  . TYR B 2  759  ? -14.555 -20.617  28.417  1.00 70.13  ?  759  TYR B CG  1 
ATOM   7037  C  CD1 . TYR B 2  759  ? -15.905 -20.656  28.733  1.00 72.22  ?  759  TYR B CD1 1 
ATOM   7038  C  CD2 . TYR B 2  759  ? -13.802 -21.763  28.631  1.00 71.00  ?  759  TYR B CD2 1 
ATOM   7039  C  CE1 . TYR B 2  759  ? -16.492 -21.807  29.229  1.00 72.65  ?  759  TYR B CE1 1 
ATOM   7040  C  CE2 . TYR B 2  759  ? -14.378 -22.919  29.124  1.00 69.13  ?  759  TYR B CE2 1 
ATOM   7041  C  CZ  . TYR B 2  759  ? -15.723 -22.936  29.425  1.00 72.61  ?  759  TYR B CZ  1 
ATOM   7042  O  OH  . TYR B 2  759  ? -16.300 -24.084  29.921  1.00 58.81  ?  759  TYR B OH  1 
ATOM   7043  N  N   . GLN B 2  760  ? -13.554 -16.963  25.640  1.00 66.69  ?  760  GLN B N   1 
ATOM   7044  C  CA  . GLN B 2  760  ? -13.087 -15.637  25.250  1.00 68.90  ?  760  GLN B CA  1 
ATOM   7045  C  C   . GLN B 2  760  ? -14.248 -14.744  24.835  1.00 71.25  ?  760  GLN B C   1 
ATOM   7046  O  O   . GLN B 2  760  ? -14.304 -13.570  25.218  1.00 78.73  ?  760  GLN B O   1 
ATOM   7047  C  CB  . GLN B 2  760  ? -12.062 -15.737  24.119  1.00 61.25  ?  760  GLN B CB  1 
ATOM   7048  C  CG  . GLN B 2  760  ? -11.124 -14.540  24.031  1.00 58.36  ?  760  GLN B CG  1 
ATOM   7049  C  CD  . GLN B 2  760  ? -9.818  -14.757  24.761  1.00 69.59  ?  760  GLN B CD  1 
ATOM   7050  O  OE1 . GLN B 2  760  ? -9.504  -15.869  25.185  1.00 77.71  ?  760  GLN B OE1 1 
ATOM   7051  N  NE2 . GLN B 2  760  ? -9.044  -13.690  24.912  1.00 83.00  ?  760  GLN B NE2 1 
ATOM   7052  N  N   . GLU B 2  761  ? -15.188 -15.280  24.055  1.00 85.82  ?  761  GLU B N   1 
ATOM   7053  C  CA  . GLU B 2  761  ? -16.332 -14.486  23.626  1.00 91.02  ?  761  GLU B CA  1 
ATOM   7054  C  C   . GLU B 2  761  ? -17.325 -14.244  24.754  1.00 93.72  ?  761  GLU B C   1 
ATOM   7055  O  O   . GLU B 2  761  ? -18.127 -13.309  24.663  1.00 102.25 ?  761  GLU B O   1 
ATOM   7056  C  CB  . GLU B 2  761  ? -17.028 -15.168  22.449  1.00 96.79  ?  761  GLU B CB  1 
ATOM   7057  C  CG  . GLU B 2  761  ? -16.194 -15.196  21.179  1.00 108.20 ?  761  GLU B CG  1 
ATOM   7058  C  CD  . GLU B 2  761  ? -16.980 -15.664  19.971  1.00 117.21 ?  761  GLU B CD  1 
ATOM   7059  O  OE1 . GLU B 2  761  ? -18.153 -16.056  20.139  1.00 118.41 ?  761  GLU B OE1 1 
ATOM   7060  O  OE2 . GLU B 2  761  ? -16.422 -15.639  18.853  1.00 113.60 -1 761  GLU B OE2 1 
ATOM   7061  N  N   . GLU B 2  762  ? -17.290 -15.058  25.810  1.00 99.11  ?  762  GLU B N   1 
ATOM   7062  C  CA  . GLU B 2  762  ? -18.188 -14.876  26.945  1.00 101.30 ?  762  GLU B CA  1 
ATOM   7063  C  C   . GLU B 2  762  ? -17.560 -14.046  28.059  1.00 101.54 ?  762  GLU B C   1 
ATOM   7064  O  O   . GLU B 2  762  ? -18.254 -13.249  28.700  1.00 106.31 ?  762  GLU B O   1 
ATOM   7065  C  CB  . GLU B 2  762  ? -18.624 -16.234  27.505  1.00 101.66 ?  762  GLU B CB  1 
ATOM   7066  C  CG  . GLU B 2  762  ? -19.452 -17.083  26.550  1.00 110.55 ?  762  GLU B CG  1 
ATOM   7067  C  CD  . GLU B 2  762  ? -20.788 -16.456  26.212  1.00 114.70 ?  762  GLU B CD  1 
ATOM   7068  O  OE1 . GLU B 2  762  ? -21.369 -15.777  27.085  1.00 117.13 ?  762  GLU B OE1 1 
ATOM   7069  O  OE2 . GLU B 2  762  ? -21.259 -16.644  25.070  1.00 108.87 -1 762  GLU B OE2 1 
ATOM   7070  N  N   . TYR B 2  763  ? -16.260 -14.213  28.303  1.00 77.09  ?  763  TYR B N   1 
ATOM   7071  C  CA  . TYR B 2  763  ? -15.598 -13.556  29.424  1.00 81.04  ?  763  TYR B CA  1 
ATOM   7072  C  C   . TYR B 2  763  ? -14.379 -12.727  29.045  1.00 79.03  ?  763  TYR B C   1 
ATOM   7073  O  O   . TYR B 2  763  ? -13.950 -11.903  29.862  1.00 87.57  ?  763  TYR B O   1 
ATOM   7074  C  CB  . TYR B 2  763  ? -15.170 -14.591  30.476  1.00 79.35  ?  763  TYR B CB  1 
ATOM   7075  C  CG  . TYR B 2  763  ? -16.289 -15.500  30.934  1.00 74.84  ?  763  TYR B CG  1 
ATOM   7076  C  CD1 . TYR B 2  763  ? -17.356 -15.003  31.671  1.00 74.95  ?  763  TYR B CD1 1 
ATOM   7077  C  CD2 . TYR B 2  763  ? -16.275 -16.856  30.634  1.00 68.71  ?  763  TYR B CD2 1 
ATOM   7078  C  CE1 . TYR B 2  763  ? -18.381 -15.829  32.092  1.00 76.13  ?  763  TYR B CE1 1 
ATOM   7079  C  CE2 . TYR B 2  763  ? -17.296 -17.690  31.051  1.00 67.85  ?  763  TYR B CE2 1 
ATOM   7080  C  CZ  . TYR B 2  763  ? -18.346 -17.172  31.780  1.00 64.44  ?  763  TYR B CZ  1 
ATOM   7081  O  OH  . TYR B 2  763  ? -19.365 -17.996  32.199  1.00 55.33  ?  763  TYR B OH  1 
ATOM   7082  N  N   . GLY B 2  764  ? -13.809 -12.904  27.854  1.00 69.62  ?  764  GLY B N   1 
ATOM   7083  C  CA  . GLY B 2  764  ? -12.601 -12.205  27.474  1.00 73.80  ?  764  GLY B CA  1 
ATOM   7084  C  C   . GLY B 2  764  ? -11.315 -12.916  27.834  1.00 75.26  ?  764  GLY B C   1 
ATOM   7085  O  O   . GLY B 2  764  ? -10.243 -12.487  27.390  1.00 79.67  ?  764  GLY B O   1 
ATOM   7086  N  N   . ARG B 2  765  ? -11.387 -13.983  28.622  1.00 88.58  ?  765  ARG B N   1 
ATOM   7087  C  CA  . ARG B 2  765  ? -10.230 -14.773  29.009  1.00 91.26  ?  765  ARG B CA  1 
ATOM   7088  C  C   . ARG B 2  765  ? -10.404 -16.204  28.514  1.00 88.56  ?  765  ARG B C   1 
ATOM   7089  O  O   . ARG B 2  765  ? -11.489 -16.616  28.097  1.00 90.18  ?  765  ARG B O   1 
ATOM   7090  C  CB  . ARG B 2  765  ? -10.032 -14.748  30.530  1.00 98.35  ?  765  ARG B CB  1 
ATOM   7091  C  CG  . ARG B 2  765  ? -11.310 -14.979  31.318  1.00 96.62  ?  765  ARG B CG  1 
ATOM   7092  C  CD  . ARG B 2  765  ? -11.111 -14.711  32.800  1.00 87.31  ?  765  ARG B CD  1 
ATOM   7093  N  NE  . ARG B 2  765  ? -12.129 -15.370  33.608  1.00 79.30  ?  765  ARG B NE  1 
ATOM   7094  C  CZ  . ARG B 2  765  ? -13.272 -14.808  33.977  1.00 81.28  ?  765  ARG B CZ  1 
ATOM   7095  N  NH1 . ARG B 2  765  ? -13.579 -13.571  33.623  1.00 85.71  ?  765  ARG B NH1 1 
ATOM   7096  N  NH2 . ARG B 2  765  ? -14.129 -15.506  34.717  1.00 75.71  ?  765  ARG B NH2 1 
ATOM   7097  N  N   . GLU B 2  766  ? -9.314  -16.964  28.564  1.00 116.62 ?  766  GLU B N   1 
ATOM   7098  C  CA  . GLU B 2  766  ? -9.303  -18.336  28.077  1.00 118.79 ?  766  GLU B CA  1 
ATOM   7099  C  C   . GLU B 2  766  ? -9.726  -19.351  29.132  1.00 115.70 ?  766  GLU B C   1 
ATOM   7100  O  O   . GLU B 2  766  ? -9.793  -20.546  28.825  1.00 115.34 ?  766  GLU B O   1 
ATOM   7101  C  CB  . GLU B 2  766  ? -7.909  -18.693  27.550  1.00 120.71 ?  766  GLU B CB  1 
ATOM   7102  C  CG  . GLU B 2  766  ? -6.835  -18.749  28.625  1.00 135.69 ?  766  GLU B CG  1 
ATOM   7103  C  CD  . GLU B 2  766  ? -5.492  -19.199  28.087  1.00 143.59 ?  766  GLU B CD  1 
ATOM   7104  O  OE1 . GLU B 2  766  ? -5.341  -19.278  26.849  1.00 144.89 ?  766  GLU B OE1 1 
ATOM   7105  O  OE2 . GLU B 2  766  ? -4.585  -19.473  28.901  1.00 147.50 -1 766  GLU B OE2 1 
ATOM   7106  N  N   . THR B 2  767  ? -10.019 -18.912  30.358  1.00 98.25  ?  767  THR B N   1 
ATOM   7107  C  CA  . THR B 2  767  ? -10.382 -19.819  31.439  1.00 98.87  ?  767  THR B CA  1 
ATOM   7108  C  C   . THR B 2  767  ? -11.502 -19.202  32.270  1.00 105.06 ?  767  THR B C   1 
ATOM   7109  O  O   . THR B 2  767  ? -11.358 -18.063  32.751  1.00 111.86 ?  767  THR B O   1 
ATOM   7110  C  CB  . THR B 2  767  ? -9.177  -20.136  32.329  1.00 95.61  ?  767  THR B CB  1 
ATOM   7111  O  OG1 . THR B 2  767  ? -8.203  -20.869  31.577  1.00 88.63  ?  767  THR B OG1 1 
ATOM   7112  C  CG2 . THR B 2  767  ? -9.607  -20.958  33.535  1.00 94.30  ?  767  THR B CG2 1 
ATOM   7113  N  N   . PRO B 2  768  ? -12.615 -19.913  32.464  1.00 83.37  ?  768  PRO B N   1 
ATOM   7114  C  CA  . PRO B 2  768  ? -13.707 -19.394  33.299  1.00 79.77  ?  768  PRO B CA  1 
ATOM   7115  C  C   . PRO B 2  768  ? -13.442 -19.679  34.769  1.00 76.95  ?  768  PRO B C   1 
ATOM   7116  O  O   . PRO B 2  768  ? -13.548 -20.820  35.230  1.00 83.63  ?  768  PRO B O   1 
ATOM   7117  C  CB  . PRO B 2  768  ? -14.931 -20.158  32.775  1.00 75.98  ?  768  PRO B CB  1 
ATOM   7118  C  CG  . PRO B 2  768  ? -14.371 -21.469  32.315  1.00 71.67  ?  768  PRO B CG  1 
ATOM   7119  C  CD  . PRO B 2  768  ? -12.935 -21.233  31.893  1.00 72.38  ?  768  PRO B CD  1 
ATOM   7120  N  N   . ASN B 2  769  ? -13.092 -18.631  35.514  1.00 101.25 ?  769  ASN B N   1 
ATOM   7121  C  CA  . ASN B 2  769  ? -12.729 -18.771  36.924  1.00 100.87 ?  769  ASN B CA  1 
ATOM   7122  C  C   . ASN B 2  769  ? -13.998 -18.871  37.770  1.00 106.14 ?  769  ASN B C   1 
ATOM   7123  O  O   . ASN B 2  769  ? -14.329 -17.998  38.575  1.00 117.74 ?  769  ASN B O   1 
ATOM   7124  C  CB  . ASN B 2  769  ? -11.850 -17.608  37.361  1.00 115.70 ?  769  ASN B CB  1 
ATOM   7125  C  CG  . ASN B 2  769  ? -10.654 -17.414  36.452  1.00 122.68 ?  769  ASN B CG  1 
ATOM   7126  O  OD1 . ASN B 2  769  ? -10.177 -18.360  35.826  1.00 116.13 ?  769  ASN B OD1 1 
ATOM   7127  N  ND2 . ASN B 2  769  ? -10.163 -16.182  36.373  1.00 129.88 ?  769  ASN B ND2 1 
ATOM   7128  N  N   . TYR B 2  770  ? -14.718 -19.974  37.571  1.00 107.15 ?  770  TYR B N   1 
ATOM   7129  C  CA  . TYR B 2  770  ? -15.928 -20.224  38.342  1.00 101.17 ?  770  TYR B CA  1 
ATOM   7130  C  C   . TYR B 2  770  ? -15.590 -20.413  39.814  1.00 95.93  ?  770  TYR B C   1 
ATOM   7131  O  O   . TYR B 2  770  ? -14.677 -21.166  40.165  1.00 101.48 ?  770  TYR B O   1 
ATOM   7132  C  CB  . TYR B 2  770  ? -16.659 -21.457  37.807  1.00 102.72 ?  770  TYR B CB  1 
ATOM   7133  C  CG  . TYR B 2  770  ? -17.209 -21.301  36.407  1.00 110.37 ?  770  TYR B CG  1 
ATOM   7134  C  CD1 . TYR B 2  770  ? -17.700 -20.080  35.962  1.00 111.88 ?  770  TYR B CD1 1 
ATOM   7135  C  CD2 . TYR B 2  770  ? -17.249 -22.381  35.533  1.00 110.25 ?  770  TYR B CD2 1 
ATOM   7136  C  CE1 . TYR B 2  770  ? -18.208 -19.937  34.683  1.00 116.90 ?  770  TYR B CE1 1 
ATOM   7137  C  CE2 . TYR B 2  770  ? -17.756 -22.248  34.254  1.00 108.64 ?  770  TYR B CE2 1 
ATOM   7138  C  CZ  . TYR B 2  770  ? -18.234 -21.024  33.834  1.00 112.58 ?  770  TYR B CZ  1 
ATOM   7139  O  OH  . TYR B 2  770  ? -18.738 -20.889  32.561  1.00 104.96 ?  770  TYR B OH  1 
ATOM   7140  N  N   . GLN B 2  771  ? -16.329 -19.721  40.675  1.00 62.73  ?  771  GLN B N   1 
ATOM   7141  C  CA  . GLN B 2  771  ? -16.132 -19.787  42.114  1.00 68.04  ?  771  GLN B CA  1 
ATOM   7142  C  C   . GLN B 2  771  ? -17.438 -20.182  42.787  1.00 67.91  ?  771  GLN B C   1 
ATOM   7143  O  O   . GLN B 2  771  ? -18.513 -19.713  42.401  1.00 68.52  ?  771  GLN B O   1 
ATOM   7144  C  CB  . GLN B 2  771  ? -15.627 -18.449  42.660  1.00 73.24  ?  771  GLN B CB  1 
ATOM   7145  C  CG  . GLN B 2  771  ? -14.334 -17.983  42.013  1.00 70.55  ?  771  GLN B CG  1 
ATOM   7146  C  CD  . GLN B 2  771  ? -13.894 -16.619  42.497  1.00 70.41  ?  771  GLN B CD  1 
ATOM   7147  O  OE1 . GLN B 2  771  ? -14.513 -16.033  43.384  1.00 71.68  ?  771  GLN B OE1 1 
ATOM   7148  N  NE2 . GLN B 2  771  ? -12.818 -16.103  41.912  1.00 84.28  ?  771  GLN B NE2 1 
ATOM   7149  N  N   . SER B 2  772  ? -17.337 -21.051  43.789  1.00 72.65  ?  772  SER B N   1 
ATOM   7150  C  CA  . SER B 2  772  ? -18.494 -21.601  44.474  1.00 69.90  ?  772  SER B CA  1 
ATOM   7151  C  C   . SER B 2  772  ? -18.462 -21.229  45.950  1.00 72.12  ?  772  SER B C   1 
ATOM   7152  O  O   . SER B 2  772  ? -17.406 -20.940  46.521  1.00 76.09  ?  772  SER B O   1 
ATOM   7153  C  CB  . SER B 2  772  ? -18.552 -23.128  44.323  1.00 65.25  ?  772  SER B CB  1 
ATOM   7154  O  OG  . SER B 2  772  ? -19.610 -23.678  45.088  1.00 59.50  ?  772  SER B OG  1 
ATOM   7155  N  N   . LEU B 2  773  ? -19.644 -21.241  46.564  1.00 64.35  ?  773  LEU B N   1 
ATOM   7156  C  CA  . LEU B 2  773  ? -19.796 -20.976  47.988  1.00 61.61  ?  773  LEU B CA  1 
ATOM   7157  C  C   . LEU B 2  773  ? -20.046 -22.239  48.801  1.00 58.44  ?  773  LEU B C   1 
ATOM   7158  O  O   . LEU B 2  773  ? -20.139 -22.160  50.030  1.00 63.45  ?  773  LEU B O   1 
ATOM   7159  C  CB  . LEU B 2  773  ? -20.937 -19.981  48.223  1.00 61.06  ?  773  LEU B CB  1 
ATOM   7160  C  CG  . LEU B 2  773  ? -20.639 -18.509  47.929  1.00 59.54  ?  773  LEU B CG  1 
ATOM   7161  C  CD1 . LEU B 2  773  ? -21.900 -17.667  48.053  1.00 62.67  ?  773  LEU B CD1 1 
ATOM   7162  C  CD2 . LEU B 2  773  ? -19.550 -17.989  48.853  1.00 65.33  ?  773  LEU B CD2 1 
ATOM   7163  N  N   . GLN B 2  774  ? -20.158 -23.400  48.149  1.00 59.68  ?  774  GLN B N   1 
ATOM   7164  C  CA  . GLN B 2  774  ? -20.433 -24.654  48.827  1.00 55.07  ?  774  GLN B CA  1 
ATOM   7165  C  C   . GLN B 2  774  ? -19.198 -25.547  48.839  1.00 53.09  ?  774  GLN B C   1 
ATOM   7166  O  O   . GLN B 2  774  ? -18.458 -25.595  47.849  1.00 52.67  ?  774  GLN B O   1 
ATOM   7167  C  CB  . GLN B 2  774  ? -21.592 -25.401  48.155  1.00 52.23  ?  774  GLN B CB  1 
ATOM   7168  C  CG  . GLN B 2  774  ? -22.848 -24.563  47.962  1.00 53.43  ?  774  GLN B CG  1 
ATOM   7169  C  CD  . GLN B 2  774  ? -23.418 -24.033  49.269  1.00 51.18  ?  774  GLN B CD  1 
ATOM   7170  O  OE1 . GLN B 2  774  ? -23.208 -24.612  50.335  1.00 48.99  ?  774  GLN B OE1 1 
ATOM   7171  N  NE2 . GLN B 2  774  ? -24.148 -22.926  49.188  1.00 56.87  ?  774  GLN B NE2 1 
ATOM   7172  N  N   . PRO B 2  775  ? -18.949 -26.260  49.936  1.00 61.05  ?  775  PRO B N   1 
ATOM   7173  C  CA  . PRO B 2  775  ? -17.737 -27.087  50.015  1.00 63.85  ?  775  PRO B CA  1 
ATOM   7174  C  C   . PRO B 2  775  ? -17.841 -28.379  49.219  1.00 65.90  ?  775  PRO B C   1 
ATOM   7175  O  O   . PRO B 2  775  ? -16.874 -28.801  48.575  1.00 62.57  ?  775  PRO B O   1 
ATOM   7176  C  CB  . PRO B 2  775  ? -17.606 -27.365  51.518  1.00 62.04  ?  775  PRO B CB  1 
ATOM   7177  C  CG  . PRO B 2  775  ? -19.004 -27.290  52.036  1.00 57.57  ?  775  PRO B CG  1 
ATOM   7178  C  CD  . PRO B 2  775  ? -19.712 -26.260  51.196  1.00 61.32  ?  775  PRO B CD  1 
ATOM   7179  N  N   . GLY B 2  776  ? -19.009 -29.014  49.254  1.00 49.92  ?  776  GLY B N   1 
ATOM   7180  C  CA  . GLY B 2  776  ? -19.169 -30.311  48.629  1.00 45.48  ?  776  GLY B CA  1 
ATOM   7181  C  C   . GLY B 2  776  ? -18.555 -31.420  49.468  1.00 52.09  ?  776  GLY B C   1 
ATOM   7182  O  O   . GLY B 2  776  ? -18.407 -31.314  50.690  1.00 56.18  ?  776  GLY B O   1 
ATOM   7183  N  N   . ASP B 2  777  ? -18.196 -32.505  48.791  1.00 60.56  ?  777  ASP B N   1 
ATOM   7184  C  CA  . ASP B 2  777  ? -17.557 -33.650  49.420  1.00 65.84  ?  777  ASP B CA  1 
ATOM   7185  C  C   . ASP B 2  777  ? -16.208 -33.901  48.761  1.00 74.63  ?  777  ASP B C   1 
ATOM   7186  O  O   . ASP B 2  777  ? -15.885 -33.332  47.715  1.00 69.85  ?  777  ASP B O   1 
ATOM   7187  C  CB  . ASP B 2  777  ? -18.448 -34.896  49.337  1.00 66.02  ?  777  ASP B CB  1 
ATOM   7188  C  CG  . ASP B 2  777  ? -18.247 -35.835  50.507  1.00 71.89  ?  777  ASP B CG  1 
ATOM   7189  O  OD1 . ASP B 2  777  ? -17.502 -35.468  51.438  1.00 77.25  ?  777  ASP B OD1 1 
ATOM   7190  O  OD2 . ASP B 2  777  ? -18.837 -36.936  50.497  1.00 71.68  -1 777  ASP B OD2 1 
ATOM   7191  N  N   . ASP B 2  778  ? -15.416 -34.772  49.387  1.00 103.43 ?  778  ASP B N   1 
ATOM   7192  C  CA  . ASP B 2  778  ? -14.021 -34.931  48.988  1.00 109.07 ?  778  ASP B CA  1 
ATOM   7193  C  C   . ASP B 2  778  ? -13.874 -35.896  47.815  1.00 112.97 ?  778  ASP B C   1 
ATOM   7194  O  O   . ASP B 2  778  ? -13.433 -35.504  46.729  1.00 114.25 ?  778  ASP B O   1 
ATOM   7195  C  CB  . ASP B 2  778  ? -13.190 -35.402  50.184  1.00 108.14 ?  778  ASP B CB  1 
ATOM   7196  C  CG  . ASP B 2  778  ? -11.745 -34.957  50.097  1.00 124.86 ?  778  ASP B CG  1 
ATOM   7197  O  OD1 . ASP B 2  778  ? -11.404 -34.224  49.145  1.00 121.13 ?  778  ASP B OD1 1 
ATOM   7198  O  OD2 . ASP B 2  778  ? -10.947 -35.346  50.976  1.00 134.25 -1 778  ASP B OD2 1 
ATOM   7199  N  N   . TYR B 2  779  ? -14.237 -37.164  48.023  1.00 71.38  ?  779  TYR B N   1 
ATOM   7200  C  CA  . TYR B 2  779  ? -14.086 -38.224  47.022  1.00 67.17  ?  779  TYR B CA  1 
ATOM   7201  C  C   . TYR B 2  779  ? -12.623 -38.380  46.598  1.00 73.68  ?  779  TYR B C   1 
ATOM   7202  O  O   . TYR B 2  779  ? -12.270 -38.230  45.426  1.00 85.26  ?  779  TYR B O   1 
ATOM   7203  C  CB  . TYR B 2  779  ? -14.970 -37.977  45.790  1.00 70.06  ?  779  TYR B CB  1 
ATOM   7204  C  CG  . TYR B 2  779  ? -16.387 -37.528  46.063  1.00 60.38  ?  779  TYR B CG  1 
ATOM   7205  C  CD1 . TYR B 2  779  ? -17.298 -38.364  46.694  1.00 55.99  ?  779  TYR B CD1 1 
ATOM   7206  C  CD2 . TYR B 2  779  ? -16.818 -36.269  45.667  1.00 63.84  ?  779  TYR B CD2 1 
ATOM   7207  C  CE1 . TYR B 2  779  ? -18.597 -37.952  46.932  1.00 63.54  ?  779  TYR B CE1 1 
ATOM   7208  C  CE2 . TYR B 2  779  ? -18.110 -35.849  45.900  1.00 54.65  ?  779  TYR B CE2 1 
ATOM   7209  C  CZ  . TYR B 2  779  ? -18.996 -36.692  46.531  1.00 56.56  ?  779  TYR B CZ  1 
ATOM   7210  O  OH  . TYR B 2  779  ? -20.284 -36.266  46.764  1.00 58.54  ?  779  TYR B OH  1 
ATOM   7211  N  N   . THR B 2  780  ? -11.768 -38.693  47.571  1.00 60.61  ?  780  THR B N   1 
ATOM   7212  C  CA  . THR B 2  780  ? -10.349 -38.911  47.297  1.00 68.40  ?  780  THR B CA  1 
ATOM   7213  C  C   . THR B 2  780  ? -9.990  -40.393  47.281  1.00 70.84  ?  780  THR B C   1 
ATOM   7214  O  O   . THR B 2  780  ? -9.608  -40.933  46.238  1.00 63.14  ?  780  THR B O   1 
ATOM   7215  C  CB  . THR B 2  780  ? -9.480  -38.164  48.318  1.00 59.28  ?  780  THR B CB  1 
ATOM   7216  O  OG1 . THR B 2  780  ? -9.929  -38.464  49.646  1.00 64.26  ?  780  THR B OG1 1 
ATOM   7217  C  CG2 . THR B 2  780  ? -9.531  -36.661  48.074  1.00 59.28  ?  780  THR B CG2 1 
ATOM   7218  N  N   . GLY B 2  781  ? -10.099 -41.061  48.423  1.00 76.74  ?  781  GLY B N   1 
ATOM   7219  C  CA  . GLY B 2  781  ? -9.760  -42.463  48.522  1.00 75.12  ?  781  GLY B CA  1 
ATOM   7220  C  C   . GLY B 2  781  ? -10.891 -43.424  48.236  1.00 67.51  ?  781  GLY B C   1 
ATOM   7221  O  O   . GLY B 2  781  ? -10.716 -44.635  48.406  1.00 62.57  ?  781  GLY B O   1 
ATOM   7222  N  N   . ARG B 2  782  ? -12.045 -42.929  47.803  1.00 60.17  ?  782  ARG B N   1 
ATOM   7223  C  CA  . ARG B 2  782  ? -13.215 -43.758  47.563  1.00 60.33  ?  782  ARG B CA  1 
ATOM   7224  C  C   . ARG B 2  782  ? -13.509 -43.843  46.071  1.00 56.18  ?  782  ARG B C   1 
ATOM   7225  O  O   . ARG B 2  782  ? -12.975 -43.083  45.259  1.00 60.80  ?  782  ARG B O   1 
ATOM   7226  C  CB  . ARG B 2  782  ? -14.432 -43.204  48.314  1.00 57.69  ?  782  ARG B CB  1 
ATOM   7227  C  CG  . ARG B 2  782  ? -14.775 -41.769  47.951  1.00 57.55  ?  782  ARG B CG  1 
ATOM   7228  C  CD  . ARG B 2  782  ? -15.773 -41.170  48.925  1.00 57.65  ?  782  ARG B CD  1 
ATOM   7229  N  NE  . ARG B 2  782  ? -15.139 -40.673  50.139  1.00 54.06  ?  782  ARG B NE  1 
ATOM   7230  C  CZ  . ARG B 2  782  ? -15.720 -39.847  50.998  1.00 57.73  ?  782  ARG B CZ  1 
ATOM   7231  N  NH1 . ARG B 2  782  ? -16.955 -39.412  50.811  1.00 49.42  ?  782  ARG B NH1 1 
ATOM   7232  N  NH2 . ARG B 2  782  ? -15.044 -39.446  52.071  1.00 69.23  ?  782  ARG B NH2 1 
ATOM   7233  N  N   . ASN B 2  783  ? -14.373 -44.790  45.718  1.00 54.90  ?  783  ASN B N   1 
ATOM   7234  C  CA  . ASN B 2  783  ? -14.808 -44.927  44.336  1.00 51.45  ?  783  ASN B CA  1 
ATOM   7235  C  C   . ASN B 2  783  ? -15.678 -43.742  43.940  1.00 46.37  ?  783  ASN B C   1 
ATOM   7236  O  O   . ASN B 2  783  ? -16.504 -43.268  44.724  1.00 52.94  ?  783  ASN B O   1 
ATOM   7237  C  CB  . ASN B 2  783  ? -15.582 -46.231  44.145  1.00 59.81  ?  783  ASN B CB  1 
ATOM   7238  C  CG  . ASN B 2  783  ? -14.694 -47.457  44.239  1.00 69.56  ?  783  ASN B CG  1 
ATOM   7239  O  OD1 . ASN B 2  783  ? -13.498 -47.397  43.955  1.00 70.27  ?  783  ASN B OD1 1 
ATOM   7240  N  ND2 . ASN B 2  783  ? -15.279 -48.580  44.639  1.00 70.20  ?  783  ASN B ND2 1 
ATOM   7241  N  N   . ALA B 2  784  ? -15.483 -43.258  42.717  1.00 62.11  ?  784  ALA B N   1 
ATOM   7242  C  CA  . ALA B 2  784  ? -16.264 -42.151  42.173  1.00 67.69  ?  784  ALA B CA  1 
ATOM   7243  C  C   . ALA B 2  784  ? -16.757 -42.560  40.793  1.00 73.18  ?  784  ALA B C   1 
ATOM   7244  O  O   . ALA B 2  784  ? -15.969 -42.624  39.844  1.00 77.01  ?  784  ALA B O   1 
ATOM   7245  C  CB  . ALA B 2  784  ? -15.436 -40.868  42.104  1.00 65.70  ?  784  ALA B CB  1 
ATOM   7246  N  N   . TRP B 2  785  ? -18.052 -42.841  40.679  1.00 48.29  ?  785  TRP B N   1 
ATOM   7247  C  CA  . TRP B 2  785  ? -18.613 -43.302  39.417  1.00 47.01  ?  785  TRP B CA  1 
ATOM   7248  C  C   . TRP B 2  785  ? -18.853 -42.122  38.483  1.00 52.21  ?  785  TRP B C   1 
ATOM   7249  O  O   . TRP B 2  785  ? -19.452 -41.117  38.876  1.00 51.84  ?  785  TRP B O   1 
ATOM   7250  C  CB  . TRP B 2  785  ? -19.913 -44.068  39.654  1.00 43.33  ?  785  TRP B CB  1 
ATOM   7251  C  CG  . TRP B 2  785  ? -19.802 -45.129  40.711  1.00 46.48  ?  785  TRP B CG  1 
ATOM   7252  C  CD1 . TRP B 2  785  ? -20.533 -45.221  41.860  1.00 49.67  ?  785  TRP B CD1 1 
ATOM   7253  C  CD2 . TRP B 2  785  ? -18.895 -46.238  40.723  1.00 46.35  ?  785  TRP B CD2 1 
ATOM   7254  N  NE1 . TRP B 2  785  ? -20.144 -46.325  42.581  1.00 48.66  ?  785  TRP B NE1 1 
ATOM   7255  C  CE2 . TRP B 2  785  ? -19.139 -46.965  41.905  1.00 47.20  ?  785  TRP B CE2 1 
ATOM   7256  C  CE3 . TRP B 2  785  ? -17.904 -46.690  39.846  1.00 49.87  ?  785  TRP B CE3 1 
ATOM   7257  C  CZ2 . TRP B 2  785  ? -18.428 -48.116  42.232  1.00 58.51  ?  785  TRP B CZ2 1 
ATOM   7258  C  CZ3 . TRP B 2  785  ? -17.200 -47.832  40.173  1.00 53.15  ?  785  TRP B CZ3 1 
ATOM   7259  C  CH2 . TRP B 2  785  ? -17.465 -48.532  41.355  1.00 59.81  ?  785  TRP B CH2 1 
ATOM   7260  N  N   . GLY B 2  786  ? -18.378 -42.248  37.240  1.00 84.49  ?  786  GLY B N   1 
ATOM   7261  C  CA  . GLY B 2  786  ? -18.551 -41.207  36.251  1.00 75.85  ?  786  GLY B CA  1 
ATOM   7262  C  C   . GLY B 2  786  ? -18.812 -41.799  34.880  1.00 74.63  ?  786  GLY B C   1 
ATOM   7263  O  O   . GLY B 2  786  ? -18.597 -42.989  34.641  1.00 78.65  ?  786  GLY B O   1 
ATOM   7264  N  N   . MET B 2  787  ? -19.277 -40.937  33.977  1.00 40.45  ?  787  MET B N   1 
ATOM   7265  C  CA  . MET B 2  787  ? -19.654 -41.343  32.632  1.00 37.04  ?  787  MET B CA  1 
ATOM   7266  C  C   . MET B 2  787  ? -19.188 -40.294  31.631  1.00 36.04  ?  787  MET B C   1 
ATOM   7267  O  O   . MET B 2  787  ? -19.187 -39.095  31.927  1.00 33.87  ?  787  MET B O   1 
ATOM   7268  C  CB  . MET B 2  787  ? -21.174 -41.551  32.527  1.00 40.75  ?  787  MET B CB  1 
ATOM   7269  C  CG  . MET B 2  787  ? -21.667 -42.016  31.166  1.00 38.05  ?  787  MET B CG  1 
ATOM   7270  S  SD  . MET B 2  787  ? -23.419 -42.445  31.180  1.00 49.78  ?  787  MET B SD  1 
ATOM   7271  C  CE  . MET B 2  787  ? -23.451 -43.679  32.478  1.00 41.83  ?  787  MET B CE  1 
ATOM   7272  N  N   . THR B 2  788  ? -18.783 -40.755  30.450  1.00 61.42  ?  788  THR B N   1 
ATOM   7273  C  CA  . THR B 2  788  ? -18.315 -39.882  29.383  1.00 60.04  ?  788  THR B CA  1 
ATOM   7274  C  C   . THR B 2  788  ? -19.033 -40.248  28.093  1.00 59.45  ?  788  THR B C   1 
ATOM   7275  O  O   . THR B 2  788  ? -19.131 -41.430  27.748  1.00 60.53  ?  788  THR B O   1 
ATOM   7276  C  CB  . THR B 2  788  ? -16.799 -39.993  29.196  1.00 61.29  ?  788  THR B CB  1 
ATOM   7277  O  OG1 . THR B 2  788  ? -16.154 -39.948  30.475  1.00 76.66  ?  788  THR B OG1 1 
ATOM   7278  C  CG2 . THR B 2  788  ? -16.285 -38.848  28.340  1.00 69.21  ?  788  THR B CG2 1 
ATOM   7279  N  N   . ILE B 2  789  ? -19.535 -39.237  27.389  1.00 44.09  ?  789  ILE B N   1 
ATOM   7280  C  CA  . ILE B 2  789  ? -20.247 -39.420  26.128  1.00 48.71  ?  789  ILE B CA  1 
ATOM   7281  C  C   . ILE B 2  789  ? -19.430 -38.764  25.024  1.00 52.05  ?  789  ILE B C   1 
ATOM   7282  O  O   . ILE B 2  789  ? -19.193 -37.550  25.056  1.00 58.01  ?  789  ILE B O   1 
ATOM   7283  C  CB  . ILE B 2  789  ? -21.667 -38.835  26.179  1.00 43.97  ?  789  ILE B CB  1 
ATOM   7284  C  CG1 . ILE B 2  789  ? -22.386 -39.291  27.452  1.00 45.26  ?  789  ILE B CG1 1 
ATOM   7285  C  CG2 . ILE B 2  789  ? -22.449 -39.228  24.936  1.00 33.29  ?  789  ILE B CG2 1 
ATOM   7286  C  CD1 . ILE B 2  789  ? -23.841 -38.876  27.514  1.00 40.38  ?  789  ILE B CD1 1 
ATOM   7287  N  N   . ASN B 2  790  ? -19.006 -39.564  24.048  1.00 52.77  ?  790  ASN B N   1 
ATOM   7288  C  CA  . ASN B 2  790  ? -18.208 -39.076  22.928  1.00 50.72  ?  790  ASN B CA  1 
ATOM   7289  C  C   . ASN B 2  790  ? -19.147 -38.687  21.793  1.00 57.03  ?  790  ASN B C   1 
ATOM   7290  O  O   . ASN B 2  790  ? -19.820 -39.543  21.211  1.00 55.25  ?  790  ASN B O   1 
ATOM   7291  C  CB  . ASN B 2  790  ? -17.206 -40.135  22.478  1.00 52.92  ?  790  ASN B CB  1 
ATOM   7292  C  CG  . ASN B 2  790  ? -16.092 -39.558  21.629  1.00 54.85  ?  790  ASN B CG  1 
ATOM   7293  O  OD1 . ASN B 2  790  ? -15.965 -38.342  21.491  1.00 51.06  ?  790  ASN B OD1 1 
ATOM   7294  N  ND2 . ASN B 2  790  ? -15.274 -40.432  21.055  1.00 68.58  ?  790  ASN B ND2 1 
ATOM   7295  N  N   . LEU B 2  791  ? -19.189 -37.390  21.478  1.00 68.39  ?  791  LEU B N   1 
ATOM   7296  C  CA  . LEU B 2  791  ? -20.070 -36.903  20.424  1.00 60.46  ?  791  LEU B CA  1 
ATOM   7297  C  C   . LEU B 2  791  ? -19.616 -37.337  19.036  1.00 57.57  ?  791  LEU B C   1 
ATOM   7298  O  O   . LEU B 2  791  ? -20.442 -37.393  18.118  1.00 54.80  ?  791  LEU B O   1 
ATOM   7299  C  CB  . LEU B 2  791  ? -20.166 -35.379  20.491  1.00 53.80  ?  791  LEU B CB  1 
ATOM   7300  C  CG  . LEU B 2  791  ? -20.827 -34.824  21.753  1.00 55.02  ?  791  LEU B CG  1 
ATOM   7301  C  CD1 . LEU B 2  791  ? -20.763 -33.306  21.772  1.00 66.06  ?  791  LEU B CD1 1 
ATOM   7302  C  CD2 . LEU B 2  791  ? -22.266 -35.304  21.856  1.00 53.93  ?  791  LEU B CD2 1 
ATOM   7303  N  N   . ASN B 2  792  ? -18.328 -37.641  18.860  1.00 70.57  ?  792  ASN B N   1 
ATOM   7304  C  CA  . ASN B 2  792  ? -17.833 -38.115  17.574  1.00 74.79  ?  792  ASN B CA  1 
ATOM   7305  C  C   . ASN B 2  792  ? -18.299 -39.526  17.242  1.00 83.89  ?  792  ASN B C   1 
ATOM   7306  O  O   . ASN B 2  792  ? -18.148 -39.953  16.092  1.00 81.64  ?  792  ASN B O   1 
ATOM   7307  C  CB  . ASN B 2  792  ? -16.304 -38.062  17.544  1.00 87.98  ?  792  ASN B CB  1 
ATOM   7308  C  CG  . ASN B 2  792  ? -15.778 -36.766  16.963  1.00 88.61  ?  792  ASN B CG  1 
ATOM   7309  O  OD1 . ASN B 2  792  ? -14.912 -36.115  17.548  1.00 93.09  ?  792  ASN B OD1 1 
ATOM   7310  N  ND2 . ASN B 2  792  ? -16.292 -36.390  15.798  1.00 88.36  ?  792  ASN B ND2 1 
ATOM   7311  N  N   . ALA B 2  793  ? -18.856 -40.256  18.211  1.00 62.29  ?  793  ALA B N   1 
ATOM   7312  C  CA  . ALA B 2  793  ? -19.308 -41.620  17.984  1.00 55.73  ?  793  ALA B CA  1 
ATOM   7313  C  C   . ALA B 2  793  ? -20.819 -41.785  18.026  1.00 54.36  ?  793  ALA B C   1 
ATOM   7314  O  O   . ALA B 2  793  ? -21.321 -42.814  17.566  1.00 56.21  ?  793  ALA B O   1 
ATOM   7315  C  CB  . ALA B 2  793  ? -18.680 -42.570  19.015  1.00 52.65  ?  793  ALA B CB  1 
ATOM   7316  N  N   . CYS B 2  794  ? -21.552 -40.810  18.557  1.00 56.64  ?  794  CYS B N   1 
ATOM   7317  C  CA  . CYS B 2  794  ? -22.999 -40.942  18.639  1.00 61.82  ?  794  CYS B CA  1 
ATOM   7318  C  C   . CYS B 2  794  ? -23.626 -40.750  17.264  1.00 62.91  ?  794  CYS B C   1 
ATOM   7319  O  O   . CYS B 2  794  ? -23.312 -39.792  16.551  1.00 66.42  ?  794  CYS B O   1 
ATOM   7320  C  CB  . CYS B 2  794  ? -23.577 -39.936  19.630  1.00 60.53  ?  794  CYS B CB  1 
ATOM   7321  S  SG  . CYS B 2  794  ? -25.339 -40.182  19.949  1.00 63.91  ?  794  CYS B SG  1 
ATOM   7322  N  N   . ILE B 2  795  ? -24.514 -41.671  16.893  1.00 47.92  ?  795  ILE B N   1 
ATOM   7323  C  CA  . ILE B 2  795  ? -25.201 -41.639  15.609  1.00 44.26  ?  795  ILE B CA  1 
ATOM   7324  C  C   . ILE B 2  795  ? -26.712 -41.576  15.756  1.00 46.17  ?  795  ILE B C   1 
ATOM   7325  O  O   . ILE B 2  795  ? -27.419 -41.558  14.745  1.00 52.12  ?  795  ILE B O   1 
ATOM   7326  C  CB  . ILE B 2  795  ? -24.802 -42.842  14.731  1.00 41.62  ?  795  ILE B CB  1 
ATOM   7327  C  CG1 . ILE B 2  795  ? -25.174 -44.153  15.426  1.00 47.50  ?  795  ILE B CG1 1 
ATOM   7328  C  CG2 . ILE B 2  795  ? -23.315 -42.802  14.416  1.00 41.14  ?  795  ILE B CG2 1 
ATOM   7329  C  CD1 . ILE B 2  795  ? -24.853 -45.389  14.616  1.00 45.64  ?  795  ILE B CD1 1 
ATOM   7330  N  N   . GLY B 2  796  ? -27.231 -41.545  16.981  1.00 70.30  ?  796  GLY B N   1 
ATOM   7331  C  CA  . GLY B 2  796  ? -28.664 -41.435  17.182  1.00 62.62  ?  796  GLY B CA  1 
ATOM   7332  C  C   . GLY B 2  796  ? -29.445 -42.700  16.907  1.00 60.15  ?  796  GLY B C   1 
ATOM   7333  O  O   . GLY B 2  796  ? -30.620 -42.623  16.538  1.00 61.40  ?  796  GLY B O   1 
ATOM   7334  N  N   . CYS B 2  797  ? -28.826 -43.869  17.083  1.00 66.36  ?  797  CYS B N   1 
ATOM   7335  C  CA  . CYS B 2  797  ? -29.512 -45.129  16.823  1.00 68.40  ?  797  CYS B CA  1 
ATOM   7336  C  C   . CYS B 2  797  ? -30.602 -45.433  17.843  1.00 73.01  ?  797  CYS B C   1 
ATOM   7337  O  O   . CYS B 2  797  ? -31.389 -46.360  17.619  1.00 76.69  ?  797  CYS B O   1 
ATOM   7338  C  CB  . CYS B 2  797  ? -28.503 -46.277  16.792  1.00 67.48  ?  797  CYS B CB  1 
ATOM   7339  S  SG  . CYS B 2  797  ? -27.482 -46.400  18.268  1.00 79.87  ?  797  CYS B SG  1 
ATOM   7340  N  N   . ASN B 2  798  ? -30.659 -44.687  18.949  1.00 78.28  ?  798  ASN B N   1 
ATOM   7341  C  CA  . ASN B 2  798  ? -31.695 -44.838  19.972  1.00 72.63  ?  798  ASN B CA  1 
ATOM   7342  C  C   . ASN B 2  798  ? -31.687 -46.231  20.598  1.00 61.23  ?  798  ASN B C   1 
ATOM   7343  O  O   . ASN B 2  798  ? -32.715 -46.712  21.079  1.00 59.98  ?  798  ASN B O   1 
ATOM   7344  C  CB  . ASN B 2  798  ? -33.083 -44.513  19.413  1.00 76.24  ?  798  ASN B CB  1 
ATOM   7345  C  CG  . ASN B 2  798  ? -33.346 -43.022  19.337  1.00 72.02  ?  798  ASN B CG  1 
ATOM   7346  O  OD1 . ASN B 2  798  ? -32.944 -42.263  20.218  1.00 67.98  ?  798  ASN B OD1 1 
ATOM   7347  N  ND2 . ASN B 2  798  ? -34.028 -42.596  18.281  1.00 73.66  ?  798  ASN B ND2 1 
ATOM   7348  N  N   . ALA B 2  799  ? -30.527 -46.890  20.601  1.00 71.46  ?  799  ALA B N   1 
ATOM   7349  C  CA  . ALA B 2  799  ? -30.417 -48.185  21.261  1.00 72.55  ?  799  ALA B CA  1 
ATOM   7350  C  C   . ALA B 2  799  ? -30.269 -48.038  22.769  1.00 71.53  ?  799  ALA B C   1 
ATOM   7351  O  O   . ALA B 2  799  ? -30.720 -48.910  23.521  1.00 76.42  ?  799  ALA B O   1 
ATOM   7352  C  CB  . ALA B 2  799  ? -29.236 -48.970  20.691  1.00 72.83  ?  799  ALA B CB  1 
ATOM   7353  N  N   . CYS B 2  800  ? -29.649 -46.947  23.226  1.00 54.28  ?  800  CYS B N   1 
ATOM   7354  C  CA  . CYS B 2  800  ? -29.488 -46.728  24.659  1.00 55.75  ?  800  CYS B CA  1 
ATOM   7355  C  C   . CYS B 2  800  ? -30.820 -46.440  25.341  1.00 50.21  ?  800  CYS B C   1 
ATOM   7356  O  O   . CYS B 2  800  ? -30.993 -46.768  26.520  1.00 47.95  ?  800  CYS B O   1 
ATOM   7357  C  CB  . CYS B 2  800  ? -28.504 -45.585  24.904  1.00 65.48  ?  800  CYS B CB  1 
ATOM   7358  S  SG  . CYS B 2  800  ? -28.788 -44.127  23.878  1.00 53.95  ?  800  CYS B SG  1 
ATOM   7359  N  N   . VAL B 2  801  ? -31.769 -45.836  24.622  1.00 40.40  ?  801  VAL B N   1 
ATOM   7360  C  CA  . VAL B 2  801  ? -33.066 -45.527  25.217  1.00 43.95  ?  801  VAL B CA  1 
ATOM   7361  C  C   . VAL B 2  801  ? -33.866 -46.800  25.454  1.00 45.96  ?  801  VAL B C   1 
ATOM   7362  O  O   . VAL B 2  801  ? -34.483 -46.975  26.513  1.00 48.63  ?  801  VAL B O   1 
ATOM   7363  C  CB  . VAL B 2  801  ? -33.837 -44.531  24.333  1.00 42.66  ?  801  VAL B CB  1 
ATOM   7364  C  CG1 . VAL B 2  801  ? -35.071 -44.022  25.060  1.00 44.96  ?  801  VAL B CG1 1 
ATOM   7365  C  CG2 . VAL B 2  801  ? -32.940 -43.375  23.949  1.00 48.35  ?  801  VAL B CG2 1 
ATOM   7366  N  N   . VAL B 2  802  ? -33.872 -47.710  24.478  1.00 64.01  ?  802  VAL B N   1 
ATOM   7367  C  CA  . VAL B 2  802  ? -34.621 -48.950  24.645  1.00 69.67  ?  802  VAL B CA  1 
ATOM   7368  C  C   . VAL B 2  802  ? -33.946 -49.849  25.674  1.00 73.16  ?  802  VAL B C   1 
ATOM   7369  O  O   . VAL B 2  802  ? -34.620 -50.601  26.390  1.00 72.21  ?  802  VAL B O   1 
ATOM   7370  C  CB  . VAL B 2  802  ? -34.788 -49.656  23.286  1.00 64.67  ?  802  VAL B CB  1 
ATOM   7371  C  CG1 . VAL B 2  802  ? -35.624 -50.920  23.435  1.00 74.81  ?  802  VAL B CG1 1 
ATOM   7372  C  CG2 . VAL B 2  802  ? -35.418 -48.710  22.275  1.00 65.36  ?  802  VAL B CG2 1 
ATOM   7373  N  N   . ALA B 2  803  ? -32.616 -49.788  25.773  1.00 77.78  ?  803  ALA B N   1 
ATOM   7374  C  CA  . ALA B 2  803  ? -31.920 -50.549  26.804  1.00 76.79  ?  803  ALA B CA  1 
ATOM   7375  C  C   . ALA B 2  803  ? -32.248 -50.021  28.195  1.00 76.20  ?  803  ALA B C   1 
ATOM   7376  O  O   . ALA B 2  803  ? -32.448 -50.803  29.131  1.00 85.94  ?  803  ALA B O   1 
ATOM   7377  C  CB  . ALA B 2  803  ? -30.412 -50.511  26.562  1.00 73.20  ?  803  ALA B CB  1 
ATOM   7378  N  N   . CYS B 2  804  ? -32.306 -48.695  28.349  1.00 39.01  ?  804  CYS B N   1 
ATOM   7379  C  CA  . CYS B 2  804  ? -32.675 -48.116  29.636  1.00 43.96  ?  804  CYS B CA  1 
ATOM   7380  C  C   . CYS B 2  804  ? -34.113 -48.461  30.000  1.00 45.03  ?  804  CYS B C   1 
ATOM   7381  O  O   . CYS B 2  804  ? -34.419 -48.727  31.169  1.00 47.10  ?  804  CYS B O   1 
ATOM   7382  C  CB  . CYS B 2  804  ? -32.476 -46.601  29.606  1.00 52.91  ?  804  CYS B CB  1 
ATOM   7383  S  SG  . CYS B 2  804  ? -32.662 -45.797  31.213  1.00 38.34  ?  804  CYS B SG  1 
ATOM   7384  N  N   . GLN B 2  805  ? -35.009 -48.467  29.011  1.00 41.74  ?  805  GLN B N   1 
ATOM   7385  C  CA  . GLN B 2  805  ? -36.398 -48.832  29.271  1.00 44.96  ?  805  GLN B CA  1 
ATOM   7386  C  C   . GLN B 2  805  ? -36.522 -50.301  29.662  1.00 52.91  ?  805  GLN B C   1 
ATOM   7387  O  O   . GLN B 2  805  ? -37.291 -50.645  30.568  1.00 48.99  ?  805  GLN B O   1 
ATOM   7388  C  CB  . GLN B 2  805  ? -37.258 -48.526  28.044  1.00 51.40  ?  805  GLN B CB  1 
ATOM   7389  C  CG  . GLN B 2  805  ? -38.739 -48.354  28.347  1.00 54.05  ?  805  GLN B CG  1 
ATOM   7390  C  CD  . GLN B 2  805  ? -39.449 -47.492  27.322  1.00 54.92  ?  805  GLN B CD  1 
ATOM   7391  O  OE1 . GLN B 2  805  ? -38.893 -47.169  26.274  1.00 67.42  ?  805  GLN B OE1 1 
ATOM   7392  N  NE2 . GLN B 2  805  ? -40.690 -47.123  27.618  1.00 51.87  ?  805  GLN B NE2 1 
ATOM   7393  N  N   . ALA B 2  806  ? -35.768 -51.181  28.997  1.00 56.65  ?  806  ALA B N   1 
ATOM   7394  C  CA  . ALA B 2  806  ? -35.867 -52.608  29.289  1.00 55.97  ?  806  ALA B CA  1 
ATOM   7395  C  C   . ALA B 2  806  ? -35.189 -52.967  30.606  1.00 57.03  ?  806  ALA B C   1 
ATOM   7396  O  O   . ALA B 2  806  ? -35.560 -53.962  31.241  1.00 50.19  ?  806  ALA B O   1 
ATOM   7397  C  CB  . ALA B 2  806  ? -35.263 -53.419  28.144  1.00 55.16  ?  806  ALA B CB  1 
ATOM   7398  N  N   . GLU B 2  807  ? -34.204 -52.178  31.030  1.00 42.94  ?  807  GLU B N   1 
ATOM   7399  C  CA  . GLU B 2  807  ? -33.457 -52.475  32.245  1.00 39.86  ?  807  GLU B CA  1 
ATOM   7400  C  C   . GLU B 2  807  ? -34.091 -51.873  33.492  1.00 41.40  ?  807  GLU B C   1 
ATOM   7401  O  O   . GLU B 2  807  ? -34.011 -52.475  34.569  1.00 40.00  ?  807  GLU B O   1 
ATOM   7402  C  CB  . GLU B 2  807  ? -32.015 -51.970  32.104  1.00 39.78  ?  807  GLU B CB  1 
ATOM   7403  C  CG  . GLU B 2  807  ? -31.178 -52.037  33.378  1.00 47.04  ?  807  GLU B CG  1 
ATOM   7404  C  CD  . GLU B 2  807  ? -30.550 -53.402  33.602  1.00 45.22  ?  807  GLU B CD  1 
ATOM   7405  O  OE1 . GLU B 2  807  ? -30.496 -54.202  32.645  1.00 42.95  ?  807  GLU B OE1 1 
ATOM   7406  O  OE2 . GLU B 2  807  ? -30.110 -53.675  34.739  1.00 48.84  -1 807  GLU B OE2 1 
ATOM   7407  N  N   . ASN B 2  808  ? -34.735 -50.711  33.374  1.00 48.41  ?  808  ASN B N   1 
ATOM   7408  C  CA  . ASN B 2  808  ? -35.188 -49.955  34.535  1.00 46.97  ?  808  ASN B CA  1 
ATOM   7409  C  C   . ASN B 2  808  ? -36.708 -49.880  34.648  1.00 48.43  ?  808  ASN B C   1 
ATOM   7410  O  O   . ASN B 2  808  ? -37.228 -48.991  35.329  1.00 50.40  ?  808  ASN B O   1 
ATOM   7411  C  CB  . ASN B 2  808  ? -34.585 -48.551  34.510  1.00 44.69  ?  808  ASN B CB  1 
ATOM   7412  C  CG  . ASN B 2  808  ? -33.073 -48.569  34.608  1.00 42.09  ?  808  ASN B CG  1 
ATOM   7413  O  OD1 . ASN B 2  808  ? -32.372 -48.528  33.596  1.00 45.89  ?  808  ASN B OD1 1 
ATOM   7414  N  ND2 . ASN B 2  808  ? -32.560 -48.648  35.831  1.00 45.15  ?  808  ASN B ND2 1 
ATOM   7415  N  N   . ASN B 2  809  ? -37.429 -50.796  33.996  1.00 39.57  ?  809  ASN B N   1 
ATOM   7416  C  CA  . ASN B 2  809  ? -38.880 -50.934  34.162  1.00 38.21  ?  809  ASN B CA  1 
ATOM   7417  C  C   . ASN B 2  809  ? -39.611 -49.617  33.910  1.00 34.73  ?  809  ASN B C   1 
ATOM   7418  O  O   . ASN B 2  809  ? -40.582 -49.280  34.591  1.00 36.80  ?  809  ASN B O   1 
ATOM   7419  C  CB  . ASN B 2  809  ? -39.223 -51.481  35.550  1.00 41.22  ?  809  ASN B CB  1 
ATOM   7420  C  CG  . ASN B 2  809  ? -38.620 -52.850  35.806  1.00 40.90  ?  809  ASN B CG  1 
ATOM   7421  O  OD1 . ASN B 2  809  ? -38.203 -53.543  34.879  1.00 41.56  ?  809  ASN B OD1 1 
ATOM   7422  N  ND2 . ASN B 2  809  ? -38.570 -53.244  37.072  1.00 51.50  ?  809  ASN B ND2 1 
ATOM   7423  N  N   . ILE B 2  810  ? -39.138 -48.863  32.918  1.00 37.09  ?  810  ILE B N   1 
ATOM   7424  C  CA  . ILE B 2  810  ? -39.738 -47.572  32.604  1.00 37.82  ?  810  ILE B CA  1 
ATOM   7425  C  C   . ILE B 2  810  ? -41.095 -47.790  31.948  1.00 42.68  ?  810  ILE B C   1 
ATOM   7426  O  O   . ILE B 2  810  ? -41.230 -48.590  31.013  1.00 49.20  ?  810  ILE B O   1 
ATOM   7427  C  CB  . ILE B 2  810  ? -38.803 -46.752  31.705  1.00 40.69  ?  810  ILE B CB  1 
ATOM   7428  C  CG1 . ILE B 2  810  ? -37.482 -46.480  32.427  1.00 36.98  ?  810  ILE B CG1 1 
ATOM   7429  C  CG2 . ILE B 2  810  ? -39.461 -45.447  31.309  1.00 50.37  ?  810  ILE B CG2 1 
ATOM   7430  C  CD1 . ILE B 2  810  ? -36.418 -45.859  31.549  1.00 41.69  ?  810  ILE B CD1 1 
ATOM   7431  N  N   . ALA B 2  811  ? -42.107 -47.074  32.435  1.00 58.80  ?  811  ALA B N   1 
ATOM   7432  C  CA  . ALA B 2  811  ? -43.470 -47.276  31.972  1.00 63.53  ?  811  ALA B CA  1 
ATOM   7433  C  C   . ALA B 2  811  ? -43.665 -46.695  30.571  1.00 59.95  ?  811  ALA B C   1 
ATOM   7434  O  O   . ALA B 2  811  ? -42.836 -45.942  30.050  1.00 61.60  ?  811  ALA B O   1 
ATOM   7435  C  CB  . ALA B 2  811  ? -44.464 -46.650  32.949  1.00 71.93  ?  811  ALA B CB  1 
ATOM   7436  N  N   . VAL B 2  812  ? -44.789 -47.062  29.960  1.00 52.18  ?  812  VAL B N   1 
ATOM   7437  C  CA  . VAL B 2  812  ? -45.155 -46.628  28.616  1.00 60.71  ?  812  VAL B CA  1 
ATOM   7438  C  C   . VAL B 2  812  ? -46.466 -45.861  28.717  1.00 61.95  ?  812  VAL B C   1 
ATOM   7439  O  O   . VAL B 2  812  ? -47.506 -46.435  29.068  1.00 64.19  ?  812  VAL B O   1 
ATOM   7440  C  CB  . VAL B 2  812  ? -45.281 -47.809  27.644  1.00 55.85  ?  812  VAL B CB  1 
ATOM   7441  C  CG1 . VAL B 2  812  ? -45.901 -47.358  26.331  1.00 57.01  ?  812  VAL B CG1 1 
ATOM   7442  C  CG2 . VAL B 2  812  ? -43.918 -48.436  27.400  1.00 51.53  ?  812  VAL B CG2 1 
ATOM   7443  N  N   . VAL B 2  813  ? -46.420 -44.569  28.412  1.00 56.89  ?  813  VAL B N   1 
ATOM   7444  C  CA  . VAL B 2  813  ? -47.600 -43.723  28.442  1.00 60.76  ?  813  VAL B CA  1 
ATOM   7445  C  C   . VAL B 2  813  ? -48.176 -43.642  27.035  1.00 66.59  ?  813  VAL B C   1 
ATOM   7446  O  O   . VAL B 2  813  ? -47.513 -43.952  26.040  1.00 73.73  ?  813  VAL B O   1 
ATOM   7447  C  CB  . VAL B 2  813  ? -47.284 -42.316  28.999  1.00 59.85  ?  813  VAL B CB  1 
ATOM   7448  C  CG1 . VAL B 2  813  ? -46.551 -42.424  30.323  1.00 54.08  ?  813  VAL B CG1 1 
ATOM   7449  C  CG2 . VAL B 2  813  ? -46.468 -41.518  28.000  1.00 58.87  ?  813  VAL B CG2 1 
ATOM   7450  N  N   . GLY B 2  814  ? -49.437 -43.223  26.947  1.00 72.22  ?  814  GLY B N   1 
ATOM   7451  C  CA  . GLY B 2  814  ? -50.100 -43.138  25.665  1.00 87.99  ?  814  GLY B CA  1 
ATOM   7452  C  C   . GLY B 2  814  ? -49.666 -41.932  24.854  1.00 90.32  ?  814  GLY B C   1 
ATOM   7453  O  O   . GLY B 2  814  ? -48.903 -41.079  25.306  1.00 88.60  ?  814  GLY B O   1 
ATOM   7454  N  N   . LYS B 2  815  ? -50.169 -41.875  23.618  1.00 79.21  ?  815  LYS B N   1 
ATOM   7455  C  CA  . LYS B 2  815  ? -49.911 -40.715  22.769  1.00 77.76  ?  815  LYS B CA  1 
ATOM   7456  C  C   . LYS B 2  815  ? -50.490 -39.448  23.386  1.00 75.73  ?  815  LYS B C   1 
ATOM   7457  O  O   . LYS B 2  815  ? -49.898 -38.367  23.277  1.00 70.00  ?  815  LYS B O   1 
ATOM   7458  C  CB  . LYS B 2  815  ? -50.491 -40.949  21.373  1.00 83.27  ?  815  LYS B CB  1 
ATOM   7459  C  CG  . LYS B 2  815  ? -50.377 -39.757  20.433  1.00 78.98  ?  815  LYS B CG  1 
ATOM   7460  C  CD  . LYS B 2  815  ? -51.290 -39.916  19.227  1.00 74.39  ?  815  LYS B CD  1 
ATOM   7461  C  CE  . LYS B 2  815  ? -51.408 -38.617  18.445  1.00 77.16  ?  815  LYS B CE  1 
ATOM   7462  N  NZ  . LYS B 2  815  ? -52.441 -38.687  17.375  1.00 72.70  ?  815  LYS B NZ  1 
ATOM   7463  N  N   . ASP B 2  816  ? -51.644 -39.566  24.048  1.00 131.77 ?  816  ASP B N   1 
ATOM   7464  C  CA  . ASP B 2  816  ? -52.259 -38.405  24.684  1.00 135.64 ?  816  ASP B CA  1 
ATOM   7465  C  C   . ASP B 2  816  ? -51.372 -37.843  25.787  1.00 128.24 ?  816  ASP B C   1 
ATOM   7466  O  O   . ASP B 2  816  ? -51.273 -36.621  25.952  1.00 129.50 ?  816  ASP B O   1 
ATOM   7467  C  CB  . ASP B 2  816  ? -53.633 -38.782  25.240  1.00 146.92 ?  816  ASP B CB  1 
ATOM   7468  C  CG  . ASP B 2  816  ? -54.382 -37.591  25.803  1.00 146.63 ?  816  ASP B CG  1 
ATOM   7469  O  OD1 . ASP B 2  816  ? -54.195 -36.471  25.282  1.00 141.39 ?  816  ASP B OD1 1 
ATOM   7470  O  OD2 . ASP B 2  816  ? -55.155 -37.775  26.767  1.00 155.85 -1 816  ASP B OD2 1 
ATOM   7471  N  N   . GLN B 2  817  ? -50.716 -38.719  26.553  1.00 70.02  ?  817  GLN B N   1 
ATOM   7472  C  CA  . GLN B 2  817  ? -49.852 -38.250  27.631  1.00 64.61  ?  817  GLN B CA  1 
ATOM   7473  C  C   . GLN B 2  817  ? -48.547 -37.671  27.099  1.00 64.67  ?  817  GLN B C   1 
ATOM   7474  O  O   . GLN B 2  817  ? -47.942 -36.813  27.751  1.00 57.35  ?  817  GLN B O   1 
ATOM   7475  C  CB  . GLN B 2  817  ? -49.574 -39.387  28.614  1.00 63.39  ?  817  GLN B CB  1 
ATOM   7476  C  CG  . GLN B 2  817  ? -50.804 -39.865  29.369  1.00 70.61  ?  817  GLN B CG  1 
ATOM   7477  C  CD  . GLN B 2  817  ? -51.389 -38.791  30.265  1.00 64.19  ?  817  GLN B CD  1 
ATOM   7478  O  OE1 . GLN B 2  817  ? -50.688 -38.207  31.092  1.00 57.94  ?  817  GLN B OE1 1 
ATOM   7479  N  NE2 . GLN B 2  817  ? -52.680 -38.527  30.107  1.00 74.60  ?  817  GLN B NE2 1 
ATOM   7480  N  N   . VAL B 2  818  ? -48.097 -38.123  25.928  1.00 66.75  ?  818  VAL B N   1 
ATOM   7481  C  CA  . VAL B 2  818  ? -46.915 -37.520  25.322  1.00 60.46  ?  818  VAL B CA  1 
ATOM   7482  C  C   . VAL B 2  818  ? -47.250 -36.158  24.726  1.00 58.97  ?  818  VAL B C   1 
ATOM   7483  O  O   . VAL B 2  818  ? -46.411 -35.248  24.738  1.00 56.19  ?  818  VAL B O   1 
ATOM   7484  C  CB  . VAL B 2  818  ? -46.311 -38.461  24.265  1.00 59.94  ?  818  VAL B CB  1 
ATOM   7485  C  CG1 . VAL B 2  818  ? -45.087 -37.825  23.620  1.00 41.45  ?  818  VAL B CG1 1 
ATOM   7486  C  CG2 . VAL B 2  818  ? -45.952 -39.802  24.884  1.00 63.03  ?  818  VAL B CG2 1 
ATOM   7487  N  N   . SER B 2  819  ? -48.469 -35.993  24.207  1.00 65.51  ?  819  SER B N   1 
ATOM   7488  C  CA  . SER B 2  819  ? -48.887 -34.696  23.684  1.00 70.55  ?  819  SER B CA  1 
ATOM   7489  C  C   . SER B 2  819  ? -48.830 -33.622  24.762  1.00 73.09  ?  819  SER B C   1 
ATOM   7490  O  O   . SER B 2  819  ? -48.496 -32.465  24.480  1.00 73.61  ?  819  SER B O   1 
ATOM   7491  C  CB  . SER B 2  819  ? -50.296 -34.798  23.100  1.00 70.98  ?  819  SER B CB  1 
ATOM   7492  O  OG  . SER B 2  819  ? -51.267 -34.905  24.128  1.00 79.10  ?  819  SER B OG  1 
ATOM   7493  N  N   . ARG B 2  820  ? -49.151 -33.984  26.002  1.00 74.45  ?  820  ARG B N   1 
ATOM   7494  C  CA  . ARG B 2  820  ? -49.062 -33.069  27.130  1.00 78.59  ?  820  ARG B CA  1 
ATOM   7495  C  C   . ARG B 2  820  ? -47.663 -33.013  27.732  1.00 78.59  ?  820  ARG B C   1 
ATOM   7496  O  O   . ARG B 2  820  ? -47.488 -32.436  28.810  1.00 73.79  ?  820  ARG B O   1 
ATOM   7497  C  CB  . ARG B 2  820  ? -50.080 -33.455  28.206  1.00 78.28  ?  820  ARG B CB  1 
ATOM   7498  C  CG  . ARG B 2  820  ? -51.447 -33.828  27.655  1.00 74.60  ?  820  ARG B CG  1 
ATOM   7499  C  CD  . ARG B 2  820  ? -52.339 -34.427  28.729  1.00 83.96  ?  820  ARG B CD  1 
ATOM   7500  N  NE  . ARG B 2  820  ? -53.566 -34.979  28.166  1.00 79.46  ?  820  ARG B NE  1 
ATOM   7501  C  CZ  . ARG B 2  820  ? -54.695 -34.299  28.022  1.00 79.64  ?  820  ARG B CZ  1 
ATOM   7502  N  NH1 . ARG B 2  820  ? -54.789 -33.030  28.384  1.00 85.52  ?  820  ARG B NH1 1 
ATOM   7503  N  NH2 . ARG B 2  820  ? -55.757 -34.906  27.501  1.00 80.23  ?  820  ARG B NH2 1 
ATOM   7504  N  N   . GLY B 2  821  ? -46.670 -33.600  27.066  1.00 81.11  ?  821  GLY B N   1 
ATOM   7505  C  CA  . GLY B 2  821  ? -45.297 -33.543  27.526  1.00 77.50  ?  821  GLY B CA  1 
ATOM   7506  C  C   . GLY B 2  821  ? -45.037 -34.319  28.801  1.00 76.60  ?  821  GLY B C   1 
ATOM   7507  O  O   . GLY B 2  821  ? -44.408 -33.803  29.729  1.00 66.83  ?  821  GLY B O   1 
ATOM   7508  N  N   . ARG B 2  822  ? -45.510 -35.562  28.859  1.00 72.99  ?  822  ARG B N   1 
ATOM   7509  C  CA  . ARG B 2  822  ? -45.347 -36.407  30.036  1.00 68.49  ?  822  ARG B CA  1 
ATOM   7510  C  C   . ARG B 2  822  ? -44.699 -37.734  29.667  1.00 73.94  ?  822  ARG B C   1 
ATOM   7511  O  O   . ARG B 2  822  ? -45.022 -38.781  30.234  1.00 79.83  ?  822  ARG B O   1 
ATOM   7512  C  CB  . ARG B 2  822  ? -46.684 -36.643  30.734  1.00 72.17  ?  822  ARG B CB  1 
ATOM   7513  C  CG  . ARG B 2  822  ? -47.314 -35.392  31.320  1.00 74.36  ?  822  ARG B CG  1 
ATOM   7514  C  CD  . ARG B 2  822  ? -48.721 -35.673  31.820  1.00 73.32  ?  822  ARG B CD  1 
ATOM   7515  N  NE  . ARG B 2  822  ? -49.294 -34.526  32.515  1.00 74.43  ?  822  ARG B NE  1 
ATOM   7516  C  CZ  . ARG B 2  822  ? -50.538 -34.472  32.970  1.00 77.68  ?  822  ARG B CZ  1 
ATOM   7517  N  NH1 . ARG B 2  822  ? -51.375 -35.485  32.817  1.00 83.50  ?  822  ARG B NH1 1 
ATOM   7518  N  NH2 . ARG B 2  822  ? -50.952 -33.374  33.596  1.00 75.68  ?  822  ARG B NH2 1 
ATOM   7519  N  N   . GLU B 2  823  ? -43.775 -37.715  28.711  1.00 85.43  ?  823  GLU B N   1 
ATOM   7520  C  CA  . GLU B 2  823  ? -43.042 -38.928  28.378  1.00 85.12  ?  823  GLU B CA  1 
ATOM   7521  C  C   . GLU B 2  823  ? -42.064 -39.262  29.497  1.00 83.33  ?  823  GLU B C   1 
ATOM   7522  O  O   . GLU B 2  823  ? -41.480 -38.372  30.120  1.00 92.35  ?  823  GLU B O   1 
ATOM   7523  C  CB  . GLU B 2  823  ? -42.302 -38.767  27.049  1.00 84.23  ?  823  GLU B CB  1 
ATOM   7524  C  CG  . GLU B 2  823  ? -41.098 -37.835  27.090  1.00 83.98  ?  823  GLU B CG  1 
ATOM   7525  C  CD  . GLU B 2  823  ? -41.448 -36.405  26.728  1.00 95.94  ?  823  GLU B CD  1 
ATOM   7526  O  OE1 . GLU B 2  823  ? -42.653 -36.094  26.622  1.00 100.35 ?  823  GLU B OE1 1 
ATOM   7527  O  OE2 . GLU B 2  823  ? -40.516 -35.592  26.546  1.00 98.58  -1 823  GLU B OE2 1 
ATOM   7528  N  N   . MET B 2  824  ? -41.902 -40.555  29.765  1.00 69.77  ?  824  MET B N   1 
ATOM   7529  C  CA  . MET B 2  824  ? -41.012 -41.038  30.815  1.00 76.23  ?  824  MET B CA  1 
ATOM   7530  C  C   . MET B 2  824  ? -39.814 -41.709  30.158  1.00 77.95  ?  824  MET B C   1 
ATOM   7531  O  O   . MET B 2  824  ? -39.933 -42.813  29.617  1.00 92.28  ?  824  MET B O   1 
ATOM   7532  C  CB  . MET B 2  824  ? -41.740 -41.998  31.754  1.00 81.02  ?  824  MET B CB  1 
ATOM   7533  C  CG  . MET B 2  824  ? -43.154 -41.563  32.101  1.00 80.85  ?  824  MET B CG  1 
ATOM   7534  S  SD  . MET B 2  824  ? -43.196 -40.385  33.466  1.00 70.40  ?  824  MET B SD  1 
ATOM   7535  C  CE  . MET B 2  824  ? -42.256 -41.266  34.708  1.00 68.08  ?  824  MET B CE  1 
ATOM   7536  N  N   . HIS B 2  825  ? -38.667 -41.037  30.199  1.00 66.11  ?  825  HIS B N   1 
ATOM   7537  C  CA  . HIS B 2  825  ? -37.439 -41.560  29.617  1.00 63.58  ?  825  HIS B CA  1 
ATOM   7538  C  C   . HIS B 2  825  ? -36.267 -41.010  30.412  1.00 54.91  ?  825  HIS B C   1 
ATOM   7539  O  O   . HIS B 2  825  ? -36.158 -39.793  30.594  1.00 59.68  ?  825  HIS B O   1 
ATOM   7540  C  CB  . HIS B 2  825  ? -37.312 -41.174  28.138  1.00 71.74  ?  825  HIS B CB  1 
ATOM   7541  C  CG  . HIS B 2  825  ? -38.024 -42.104  27.205  1.00 74.99  ?  825  HIS B CG  1 
ATOM   7542  N  ND1 . HIS B 2  825  ? -39.000 -41.678  26.330  1.00 67.67  ?  825  HIS B ND1 1 
ATOM   7543  C  CD2 . HIS B 2  825  ? -37.904 -43.439  27.012  1.00 71.51  ?  825  HIS B CD2 1 
ATOM   7544  C  CE1 . HIS B 2  825  ? -39.447 -42.709  25.636  1.00 66.94  ?  825  HIS B CE1 1 
ATOM   7545  N  NE2 . HIS B 2  825  ? -38.799 -43.790  26.031  1.00 67.25  ?  825  HIS B NE2 1 
ATOM   7546  N  N   . TRP B 2  826  ? -35.399 -41.902  30.886  1.00 46.63  ?  826  TRP B N   1 
ATOM   7547  C  CA  . TRP B 2  826  ? -34.255 -41.470  31.678  1.00 56.76  ?  826  TRP B CA  1 
ATOM   7548  C  C   . TRP B 2  826  ? -33.113 -40.946  30.818  1.00 54.77  ?  826  TRP B C   1 
ATOM   7549  O  O   . TRP B 2  826  ? -32.237 -40.246  31.336  1.00 69.92  ?  826  TRP B O   1 
ATOM   7550  C  CB  . TRP B 2  826  ? -33.759 -42.616  32.563  1.00 53.36  ?  826  TRP B CB  1 
ATOM   7551  C  CG  . TRP B 2  826  ? -34.760 -43.073  33.588  1.00 53.56  ?  826  TRP B CG  1 
ATOM   7552  C  CD1 . TRP B 2  826  ? -36.064 -42.683  33.697  1.00 56.75  ?  826  TRP B CD1 1 
ATOM   7553  C  CD2 . TRP B 2  826  ? -34.533 -44.008  34.651  1.00 52.82  ?  826  TRP B CD2 1 
ATOM   7554  N  NE1 . TRP B 2  826  ? -36.662 -43.317  34.757  1.00 57.05  ?  826  TRP B NE1 1 
ATOM   7555  C  CE2 . TRP B 2  826  ? -35.744 -44.135  35.361  1.00 57.68  ?  826  TRP B CE2 1 
ATOM   7556  C  CE3 . TRP B 2  826  ? -33.425 -44.749  35.069  1.00 52.32  ?  826  TRP B CE3 1 
ATOM   7557  C  CZ2 . TRP B 2  826  ? -35.877 -44.974  36.466  1.00 56.80  ?  826  TRP B CZ2 1 
ATOM   7558  C  CZ3 . TRP B 2  826  ? -33.558 -45.580  36.168  1.00 56.65  ?  826  TRP B CZ3 1 
ATOM   7559  C  CH2 . TRP B 2  826  ? -34.775 -45.687  36.853  1.00 57.54  ?  826  TRP B CH2 1 
ATOM   7560  N  N   . ILE B 2  827  ? -33.107 -41.262  29.525  1.00 27.22  ?  827  ILE B N   1 
ATOM   7561  C  CA  . ILE B 2  827  ? -32.097 -40.774  28.593  1.00 27.22  ?  827  ILE B CA  1 
ATOM   7562  C  C   . ILE B 2  827  ? -32.801 -40.321  27.321  1.00 41.20  ?  827  ILE B C   1 
ATOM   7563  O  O   . ILE B 2  827  ? -33.787 -40.931  26.893  1.00 49.80  ?  827  ILE B O   1 
ATOM   7564  C  CB  . ILE B 2  827  ? -31.030 -41.851  28.294  1.00 27.93  ?  827  ILE B CB  1 
ATOM   7565  C  CG1 . ILE B 2  827  ? -29.937 -41.296  27.375  1.00 29.62  ?  827  ILE B CG1 1 
ATOM   7566  C  CG2 . ILE B 2  827  ? -31.667 -43.093  27.689  1.00 31.85  ?  827  ILE B CG2 1 
ATOM   7567  C  CD1 . ILE B 2  827  ? -28.710 -42.177  27.279  1.00 30.17  ?  827  ILE B CD1 1 
ATOM   7568  N  N   . ARG B 2  828  ? -32.305 -39.236  26.725  1.00 61.52  ?  828  ARG B N   1 
ATOM   7569  C  CA  . ARG B 2  828  ? -32.898 -38.669  25.522  1.00 63.77  ?  828  ARG B CA  1 
ATOM   7570  C  C   . ARG B 2  828  ? -31.802 -38.151  24.603  1.00 68.59  ?  828  ARG B C   1 
ATOM   7571  O  O   . ARG B 2  828  ? -30.772 -37.656  25.069  1.00 66.33  ?  828  ARG B O   1 
ATOM   7572  C  CB  . ARG B 2  828  ? -33.882 -37.539  25.867  1.00 66.81  ?  828  ARG B CB  1 
ATOM   7573  C  CG  . ARG B 2  828  ? -33.260 -36.365  26.614  1.00 72.23  ?  828  ARG B CG  1 
ATOM   7574  C  CD  . ARG B 2  828  ? -34.157 -35.134  26.564  1.00 77.01  ?  828  ARG B CD  1 
ATOM   7575  N  NE  . ARG B 2  828  ? -33.432 -33.909  26.883  1.00 80.62  ?  828  ARG B NE  1 
ATOM   7576  C  CZ  . ARG B 2  828  ? -33.417 -33.336  28.079  1.00 83.76  ?  828  ARG B CZ  1 
ATOM   7577  N  NH1 . ARG B 2  828  ? -34.077 -33.854  29.102  1.00 80.64  ?  828  ARG B NH1 1 
ATOM   7578  N  NH2 . ARG B 2  828  ? -32.725 -32.213  28.252  1.00 70.88  ?  828  ARG B NH2 1 
ATOM   7579  N  N   . ILE B 2  829  ? -32.029 -38.272  23.296  1.00 60.92  ?  829  ILE B N   1 
ATOM   7580  C  CA  . ILE B 2  829  ? -31.121 -37.763  22.274  1.00 61.38  ?  829  ILE B CA  1 
ATOM   7581  C  C   . ILE B 2  829  ? -31.757 -36.537  21.636  1.00 62.42  ?  829  ILE B C   1 
ATOM   7582  O  O   . ILE B 2  829  ? -32.925 -36.575  21.230  1.00 68.70  ?  829  ILE B O   1 
ATOM   7583  C  CB  . ILE B 2  829  ? -30.798 -38.831  21.213  1.00 62.68  ?  829  ILE B CB  1 
ATOM   7584  C  CG1 . ILE B 2  829  ? -29.916 -39.931  21.806  1.00 59.22  ?  829  ILE B CG1 1 
ATOM   7585  C  CG2 . ILE B 2  829  ? -30.125 -38.200  20.003  1.00 73.21  ?  829  ILE B CG2 1 
ATOM   7586  C  CD1 . ILE B 2  829  ? -30.683 -41.091  22.372  1.00 63.95  ?  829  ILE B CD1 1 
ATOM   7587  N  N   . ASP B 2  830  ? -30.987 -35.457  21.540  1.00 62.27  ?  830  ASP B N   1 
ATOM   7588  C  CA  . ASP B 2  830  ? -31.475 -34.179  21.043  1.00 71.57  ?  830  ASP B CA  1 
ATOM   7589  C  C   . ASP B 2  830  ? -30.750 -33.824  19.755  1.00 81.72  ?  830  ASP B C   1 
ATOM   7590  O  O   . ASP B 2  830  ? -29.516 -33.844  19.712  1.00 90.26  ?  830  ASP B O   1 
ATOM   7591  C  CB  . ASP B 2  830  ? -31.258 -33.074  22.080  1.00 67.24  ?  830  ASP B CB  1 
ATOM   7592  C  CG  . ASP B 2  830  ? -32.083 -33.277  23.332  1.00 75.26  ?  830  ASP B CG  1 
ATOM   7593  O  OD1 . ASP B 2  830  ? -33.181 -33.863  23.237  1.00 81.11  ?  830  ASP B OD1 1 
ATOM   7594  O  OD2 . ASP B 2  830  ? -31.632 -32.844  24.414  1.00 68.41  -1 830  ASP B OD2 1 
ATOM   7595  N  N   . ARG B 2  831  ? -31.511 -33.501  18.711  1.00 88.17  ?  831  ARG B N   1 
ATOM   7596  C  CA  . ARG B 2  831  ? -30.952 -32.933  17.493  1.00 95.31  ?  831  ARG B CA  1 
ATOM   7597  C  C   . ARG B 2  831  ? -31.274 -31.445  17.444  1.00 88.86  ?  831  ARG B C   1 
ATOM   7598  O  O   . ARG B 2  831  ? -32.310 -31.000  17.948  1.00 81.00  ?  831  ARG B O   1 
ATOM   7599  C  CB  . ARG B 2  831  ? -31.468 -33.649  16.236  1.00 100.19 ?  831  ARG B CB  1 
ATOM   7600  C  CG  . ARG B 2  831  ? -32.748 -33.099  15.627  1.00 85.68  ?  831  ARG B CG  1 
ATOM   7601  C  CD  . ARG B 2  831  ? -33.973 -33.572  16.383  1.00 92.50  ?  831  ARG B CD  1 
ATOM   7602  N  NE  . ARG B 2  831  ? -35.202 -33.275  15.660  1.00 84.41  ?  831  ARG B NE  1 
ATOM   7603  C  CZ  . ARG B 2  831  ? -35.853 -32.122  15.732  1.00 86.91  ?  831  ARG B CZ  1 
ATOM   7604  N  NH1 . ARG B 2  831  ? -35.413 -31.126  16.483  1.00 91.85  ?  831  ARG B NH1 1 
ATOM   7605  N  NH2 . ARG B 2  831  ? -36.971 -31.964  15.029  1.00 89.59  ?  831  ARG B NH2 1 
ATOM   7606  N  N   . TYR B 2  832  ? -30.367 -30.668  16.847  1.00 89.24  ?  832  TYR B N   1 
ATOM   7607  C  CA  . TYR B 2  832  ? -30.409 -29.222  16.996  1.00 92.97  ?  832  TYR B CA  1 
ATOM   7608  C  C   . TYR B 2  832  ? -30.363 -28.423  15.700  1.00 87.30  ?  832  TYR B C   1 
ATOM   7609  O  O   . TYR B 2  832  ? -30.335 -27.190  15.773  1.00 94.15  ?  832  TYR B O   1 
ATOM   7610  C  CB  . TYR B 2  832  ? -29.262 -28.752  17.905  1.00 94.00  ?  832  TYR B CB  1 
ATOM   7611  C  CG  . TYR B 2  832  ? -29.583 -28.836  19.380  1.00 83.95  ?  832  TYR B CG  1 
ATOM   7612  C  CD1 . TYR B 2  832  ? -30.601 -28.069  19.931  1.00 80.82  ?  832  TYR B CD1 1 
ATOM   7613  C  CD2 . TYR B 2  832  ? -28.868 -29.678  20.221  1.00 81.67  ?  832  TYR B CD2 1 
ATOM   7614  C  CE1 . TYR B 2  832  ? -30.900 -28.140  21.277  1.00 76.16  ?  832  TYR B CE1 1 
ATOM   7615  C  CE2 . TYR B 2  832  ? -29.159 -29.755  21.572  1.00 87.79  ?  832  TYR B CE2 1 
ATOM   7616  C  CZ  . TYR B 2  832  ? -30.176 -28.983  22.093  1.00 77.44  ?  832  TYR B CZ  1 
ATOM   7617  O  OH  . TYR B 2  832  ? -30.472 -29.054  23.435  1.00 78.03  ?  832  TYR B OH  1 
ATOM   7618  N  N   . PHE B 2  833  ? -30.357 -29.078  14.532  1.00 65.38  ?  833  PHE B N   1 
ATOM   7619  C  CA  . PHE B 2  833  ? -30.441 -28.438  13.215  1.00 67.99  ?  833  PHE B CA  1 
ATOM   7620  C  C   . PHE B 2  833  ? -29.831 -27.040  13.168  1.00 60.68  ?  833  PHE B C   1 
ATOM   7621  O  O   . PHE B 2  833  ? -30.567 -26.048  13.155  1.00 62.79  ?  833  PHE B O   1 
ATOM   7622  C  CB  . PHE B 2  833  ? -31.899 -28.351  12.754  1.00 56.70  ?  833  PHE B CB  1 
ATOM   7623  C  CG  . PHE B 2  833  ? -32.509 -29.677  12.411  1.00 56.44  ?  833  PHE B CG  1 
ATOM   7624  C  CD1 . PHE B 2  833  ? -31.856 -30.557  11.565  1.00 57.61  ?  833  PHE B CD1 1 
ATOM   7625  C  CD2 . PHE B 2  833  ? -33.747 -30.033  12.916  1.00 60.05  ?  833  PHE B CD2 1 
ATOM   7626  C  CE1 . PHE B 2  833  ? -32.421 -31.780  11.245  1.00 64.11  ?  833  PHE B CE1 1 
ATOM   7627  C  CE2 . PHE B 2  833  ? -34.319 -31.251  12.598  1.00 67.46  ?  833  PHE B CE2 1 
ATOM   7628  C  CZ  . PHE B 2  833  ? -33.656 -32.125  11.763  1.00 65.16  ?  833  PHE B CZ  1 
ATOM   7629  N  N   . ALA B 2  834  ? -28.505 -26.938  13.151  1.00 47.32  ?  834  ALA B N   1 
ATOM   7630  C  CA  . ALA B 2  834  ? -27.840 -25.649  13.260  1.00 53.26  ?  834  ALA B CA  1 
ATOM   7631  C  C   . ALA B 2  834  ? -26.955 -25.397  12.049  1.00 56.83  ?  834  ALA B C   1 
ATOM   7632  O  O   . ALA B 2  834  ? -26.541 -26.324  11.345  1.00 61.32  ?  834  ALA B O   1 
ATOM   7633  C  CB  . ALA B 2  834  ? -26.998 -25.551  14.538  1.00 58.21  ?  834  ALA B CB  1 
ATOM   7634  N  N   . GLY B 2  835  ? -26.677 -24.116  11.817  1.00 79.00  ?  835  GLY B N   1 
ATOM   7635  C  CA  . GLY B 2  835  ? -25.835 -23.675  10.724  1.00 89.12  ?  835  GLY B CA  1 
ATOM   7636  C  C   . GLY B 2  835  ? -26.511 -22.635  9.856   1.00 92.76  ?  835  GLY B C   1 
ATOM   7637  O  O   . GLY B 2  835  ? -27.619 -22.176  10.125  1.00 93.79  ?  835  GLY B O   1 
ATOM   7638  N  N   . GLU B 2  836  ? -25.807 -22.248  8.795   1.00 91.91  ?  836  GLU B N   1 
ATOM   7639  C  CA  . GLU B 2  836  ? -26.389 -21.347  7.813   1.00 90.47  ?  836  GLU B CA  1 
ATOM   7640  C  C   . GLU B 2  836  ? -27.436 -22.079  6.976   1.00 94.74  ?  836  GLU B C   1 
ATOM   7641  O  O   . GLU B 2  836  ? -27.544 -23.309  7.008   1.00 102.24 ?  836  GLU B O   1 
ATOM   7642  C  CB  . GLU B 2  836  ? -25.301 -20.759  6.916   1.00 85.77  ?  836  GLU B CB  1 
ATOM   7643  C  CG  . GLU B 2  836  ? -24.310 -19.879  7.663   1.00 104.28 ?  836  GLU B CG  1 
ATOM   7644  C  CD  . GLU B 2  836  ? -23.177 -19.384  6.781   1.00 113.11 ?  836  GLU B CD  1 
ATOM   7645  O  OE1 . GLU B 2  836  ? -22.994 -19.940  5.679   1.00 106.37 ?  836  GLU B OE1 1 
ATOM   7646  O  OE2 . GLU B 2  836  ? -22.469 -18.437  7.189   1.00 116.31 -1 836  GLU B OE2 1 
ATOM   7647  N  N   . ASP B 2  837  ? -28.222 -21.296  6.231   1.00 121.16 ?  837  ASP B N   1 
ATOM   7648  C  CA  . ASP B 2  837  ? -29.292 -21.794  5.365   1.00 130.12 ?  837  ASP B CA  1 
ATOM   7649  C  C   . ASP B 2  837  ? -30.484 -22.348  6.141   1.00 128.63 ?  837  ASP B C   1 
ATOM   7650  O  O   . ASP B 2  837  ? -31.631 -22.030  5.813   1.00 138.14 ?  837  ASP B O   1 
ATOM   7651  C  CB  . ASP B 2  837  ? -28.762 -22.862  4.402   1.00 141.07 ?  837  ASP B CB  1 
ATOM   7652  C  CG  . ASP B 2  837  ? -29.695 -23.108  3.234   1.00 142.20 ?  837  ASP B CG  1 
ATOM   7653  O  OD1 . ASP B 2  837  ? -30.681 -22.357  3.086   1.00 139.58 ?  837  ASP B OD1 1 
ATOM   7654  O  OD2 . ASP B 2  837  ? -29.435 -24.053  2.461   1.00 144.56 -1 837  ASP B OD2 1 
ATOM   7655  N  N   . LEU B 2  838  ? -30.240 -23.193  7.142   1.00 78.83  ?  838  LEU B N   1 
ATOM   7656  C  CA  . LEU B 2  838  ? -31.280 -23.897  7.893   1.00 74.73  ?  838  LEU B CA  1 
ATOM   7657  C  C   . LEU B 2  838  ? -32.211 -24.704  6.993   1.00 79.23  ?  838  LEU B C   1 
ATOM   7658  O  O   . LEU B 2  838  ? -33.216 -25.245  7.470   1.00 73.68  ?  838  LEU B O   1 
ATOM   7659  C  CB  . LEU B 2  838  ? -32.097 -22.941  8.775   1.00 70.95  ?  838  LEU B CB  1 
ATOM   7660  C  CG  . LEU B 2  838  ? -31.385 -22.445  10.036  1.00 65.98  ?  838  LEU B CG  1 
ATOM   7661  C  CD1 . LEU B 2  838  ? -32.311 -21.586  10.879  1.00 70.32  ?  838  LEU B CD1 1 
ATOM   7662  C  CD2 . LEU B 2  838  ? -30.856 -23.621  10.843  1.00 62.67  ?  838  LEU B CD2 1 
ATOM   7663  N  N   . ASP B 2  839  ? -31.908 -24.776  5.697   1.00 140.36 ?  839  ASP B N   1 
ATOM   7664  C  CA  . ASP B 2  839  ? -32.534 -25.709  4.777   1.00 142.43 ?  839  ASP B CA  1 
ATOM   7665  C  C   . ASP B 2  839  ? -31.578 -26.809  4.350   1.00 146.02 ?  839  ASP B C   1 
ATOM   7666  O  O   . ASP B 2  839  ? -32.022 -27.806  3.773   1.00 146.47 ?  839  ASP B O   1 
ATOM   7667  C  CB  . ASP B 2  839  ? -33.053 -24.973  3.533   1.00 146.58 ?  839  ASP B CB  1 
ATOM   7668  C  CG  . ASP B 2  839  ? -34.564 -24.865  3.508   1.00 147.94 ?  839  ASP B CG  1 
ATOM   7669  O  OD1 . ASP B 2  839  ? -35.182 -24.970  4.589   1.00 145.52 ?  839  ASP B OD1 1 
ATOM   7670  O  OD2 . ASP B 2  839  ? -35.131 -24.667  2.409   1.00 151.86 -1 839  ASP B OD2 1 
ATOM   7671  N  N   . ASN B 2  840  ? -30.282 -26.639  4.610   1.00 138.99 ?  840  ASN B N   1 
ATOM   7672  C  CA  . ASN B 2  840  ? -29.273 -27.687  4.471   1.00 136.95 ?  840  ASN B CA  1 
ATOM   7673  C  C   . ASN B 2  840  ? -28.437 -27.687  5.744   1.00 131.65 ?  840  ASN B C   1 
ATOM   7674  O  O   . ASN B 2  840  ? -27.255 -27.321  5.731   1.00 140.01 ?  840  ASN B O   1 
ATOM   7675  C  CB  . ASN B 2  840  ? -28.397 -27.458  3.238   1.00 134.50 ?  840  ASN B CB  1 
ATOM   7676  C  CG  . ASN B 2  840  ? -29.011 -28.013  1.966   1.00 132.89 ?  840  ASN B CG  1 
ATOM   7677  O  OD1 . ASN B 2  840  ? -30.081 -28.620  1.991   1.00 133.53 ?  840  ASN B OD1 1 
ATOM   7678  N  ND2 . ASN B 2  840  ? -28.337 -27.796  0.842   1.00 137.98 ?  840  ASN B ND2 1 
ATOM   7679  N  N   . PRO B 2  841  ? -29.026 -28.088  6.874   1.00 85.56  ?  841  PRO B N   1 
ATOM   7680  C  CA  . PRO B 2  841  ? -28.348 -27.890  8.158   1.00 81.07  ?  841  PRO B CA  1 
ATOM   7681  C  C   . PRO B 2  841  ? -27.575 -29.106  8.641   1.00 78.93  ?  841  PRO B C   1 
ATOM   7682  O  O   . PRO B 2  841  ? -27.988 -30.253  8.435   1.00 85.19  ?  841  PRO B O   1 
ATOM   7683  C  CB  . PRO B 2  841  ? -29.516 -27.565  9.090   1.00 79.53  ?  841  PRO B CB  1 
ATOM   7684  C  CG  . PRO B 2  841  ? -30.608 -28.481  8.578   1.00 75.72  ?  841  PRO B CG  1 
ATOM   7685  C  CD  . PRO B 2  841  ? -30.364 -28.676  7.073   1.00 81.04  ?  841  PRO B CD  1 
ATOM   7686  N  N   . SER B 2  842  ? -26.441 -28.857  9.288   1.00 78.95  ?  842  SER B N   1 
ATOM   7687  C  CA  . SER B 2  842  ? -25.757 -29.915  10.014  1.00 82.32  ?  842  SER B CA  1 
ATOM   7688  C  C   . SER B 2  842  ? -26.594 -30.333  11.216  1.00 78.93  ?  842  SER B C   1 
ATOM   7689  O  O   . SER B 2  842  ? -27.159 -29.495  11.924  1.00 80.27  ?  842  SER B O   1 
ATOM   7690  C  CB  . SER B 2  842  ? -24.374 -29.446  10.461  1.00 84.52  ?  842  SER B CB  1 
ATOM   7691  O  OG  . SER B 2  842  ? -24.431 -28.151  11.034  1.00 79.26  ?  842  SER B OG  1 
ATOM   7692  N  N   . ILE B 2  843  ? -26.682 -31.641  11.441  1.00 73.28  ?  843  ILE B N   1 
ATOM   7693  C  CA  . ILE B 2  843  ? -27.510 -32.208  12.498  1.00 69.70  ?  843  ILE B CA  1 
ATOM   7694  C  C   . ILE B 2  843  ? -26.605 -32.658  13.635  1.00 73.44  ?  843  ILE B C   1 
ATOM   7695  O  O   . ILE B 2  843  ? -25.614 -33.363  13.409  1.00 74.20  ?  843  ILE B O   1 
ATOM   7696  C  CB  . ILE B 2  843  ? -28.366 -33.373  11.975  1.00 61.53  ?  843  ILE B CB  1 
ATOM   7697  C  CG1 . ILE B 2  843  ? -29.023 -32.983  10.651  1.00 67.30  ?  843  ILE B CG1 1 
ATOM   7698  C  CG2 . ILE B 2  843  ? -29.425 -33.747  12.996  1.00 68.37  ?  843  ILE B CG2 1 
ATOM   7699  C  CD1 . ILE B 2  843  ? -29.129 -34.118  9.659   1.00 75.27  ?  843  ILE B CD1 1 
ATOM   7700  N  N   . TYR B 2  844  ? -26.953 -32.259  14.857  1.00 85.37  ?  844  TYR B N   1 
ATOM   7701  C  CA  . TYR B 2  844  ? -26.136 -32.507  16.041  1.00 87.42  ?  844  TYR B CA  1 
ATOM   7702  C  C   . TYR B 2  844  ? -26.945 -33.338  17.027  1.00 86.96  ?  844  TYR B C   1 
ATOM   7703  O  O   . TYR B 2  844  ? -27.850 -32.815  17.683  1.00 90.56  ?  844  TYR B O   1 
ATOM   7704  C  CB  . TYR B 2  844  ? -25.702 -31.191  16.684  1.00 88.13  ?  844  TYR B CB  1 
ATOM   7705  C  CG  . TYR B 2  844  ? -24.771 -30.359  15.835  1.00 91.74  ?  844  TYR B CG  1 
ATOM   7706  C  CD1 . TYR B 2  844  ? -23.763 -30.952  15.087  1.00 91.71  ?  844  TYR B CD1 1 
ATOM   7707  C  CD2 . TYR B 2  844  ? -24.903 -28.979  15.784  1.00 88.88  ?  844  TYR B CD2 1 
ATOM   7708  C  CE1 . TYR B 2  844  ? -22.912 -30.191  14.313  1.00 96.38  ?  844  TYR B CE1 1 
ATOM   7709  C  CE2 . TYR B 2  844  ? -24.058 -28.211  15.013  1.00 85.54  ?  844  TYR B CE2 1 
ATOM   7710  C  CZ  . TYR B 2  844  ? -23.064 -28.821  14.279  1.00 92.34  ?  844  TYR B CZ  1 
ATOM   7711  O  OH  . TYR B 2  844  ? -22.218 -28.057  13.507  1.00 93.19  ?  844  TYR B OH  1 
ATOM   7712  N  N   . MET B 2  845  ? -26.615 -34.621  17.140  1.00 69.53  ?  845  MET B N   1 
ATOM   7713  C  CA  . MET B 2  845  ? -27.271 -35.504  18.096  1.00 72.37  ?  845  MET B CA  1 
ATOM   7714  C  C   . MET B 2  845  ? -26.467 -35.564  19.389  1.00 71.33  ?  845  MET B C   1 
ATOM   7715  O  O   . MET B 2  845  ? -25.245 -35.741  19.361  1.00 73.08  ?  845  MET B O   1 
ATOM   7716  C  CB  . MET B 2  845  ? -27.444 -36.906  17.513  1.00 74.92  ?  845  MET B CB  1 
ATOM   7717  C  CG  . MET B 2  845  ? -27.865 -36.921  16.057  1.00 70.76  ?  845  MET B CG  1 
ATOM   7718  S  SD  . MET B 2  845  ? -29.639 -36.675  15.855  1.00 76.53  ?  845  MET B SD  1 
ATOM   7719  C  CE  . MET B 2  845  ? -30.264 -38.325  16.167  1.00 76.28  ?  845  MET B CE  1 
ATOM   7720  N  N   . MET B 2  846  ? -27.161 -35.425  20.519  1.00 66.74  ?  846  MET B N   1 
ATOM   7721  C  CA  . MET B 2  846  ? -26.535 -35.391  21.835  1.00 64.33  ?  846  MET B CA  1 
ATOM   7722  C  C   . MET B 2  846  ? -27.370 -36.155  22.855  1.00 57.97  ?  846  MET B C   1 
ATOM   7723  O  O   . MET B 2  846  ? -28.536 -35.810  23.090  1.00 53.47  ?  846  MET B O   1 
ATOM   7724  C  CB  . MET B 2  846  ? -26.342 -33.946  22.297  1.00 55.15  ?  846  MET B CB  1 
ATOM   7725  C  CG  . MET B 2  846  ? -25.305 -33.778  23.388  1.00 47.28  ?  846  MET B CG  1 
ATOM   7726  S  SD  . MET B 2  846  ? -25.298 -32.108  24.063  1.00 65.39  ?  846  MET B SD  1 
ATOM   7727  C  CE  . MET B 2  846  ? -27.047 -31.860  24.360  1.00 50.22  ?  846  MET B CE  1 
ATOM   7728  N  N   . PRO B 2  847  ? -26.816 -37.193  23.478  1.00 40.47  ?  847  PRO B N   1 
ATOM   7729  C  CA  . PRO B 2  847  ? -27.553 -37.907  24.525  1.00 40.52  ?  847  PRO B CA  1 
ATOM   7730  C  C   . PRO B 2  847  ? -27.472 -37.170  25.853  1.00 49.11  ?  847  PRO B C   1 
ATOM   7731  O  O   . PRO B 2  847  ? -26.429 -36.626  26.222  1.00 47.21  ?  847  PRO B O   1 
ATOM   7732  C  CB  . PRO B 2  847  ? -26.838 -39.265  24.603  1.00 37.13  ?  847  PRO B CB  1 
ATOM   7733  C  CG  . PRO B 2  847  ? -25.844 -39.277  23.456  1.00 39.89  ?  847  PRO B CG  1 
ATOM   7734  C  CD  . PRO B 2  847  ? -25.536 -37.847  23.174  1.00 39.82  ?  847  PRO B CD  1 
ATOM   7735  N  N   . VAL B 2  848  ? -28.591 -37.155  26.575  1.00 56.89  ?  848  VAL B N   1 
ATOM   7736  C  CA  . VAL B 2  848  ? -28.690 -36.468  27.858  1.00 52.13  ?  848  VAL B CA  1 
ATOM   7737  C  C   . VAL B 2  848  ? -29.366 -37.390  28.864  1.00 59.86  ?  848  VAL B C   1 
ATOM   7738  O  O   . VAL B 2  848  ? -30.455 -37.911  28.602  1.00 59.70  ?  848  VAL B O   1 
ATOM   7739  C  CB  . VAL B 2  848  ? -29.466 -35.141  27.744  1.00 46.49  ?  848  VAL B CB  1 
ATOM   7740  C  CG1 . VAL B 2  848  ? -29.612 -34.497  29.111  1.00 50.30  ?  848  VAL B CG1 1 
ATOM   7741  C  CG2 . VAL B 2  848  ? -28.764 -34.191  26.791  1.00 49.76  ?  848  VAL B CG2 1 
ATOM   7742  N  N   . ASN B 2  849  ? -28.719 -37.588  30.007  1.00 61.34  ?  849  ASN B N   1 
ATOM   7743  C  CA  . ASN B 2  849  ? -29.316 -38.299  31.131  1.00 53.09  ?  849  ASN B CA  1 
ATOM   7744  C  C   . ASN B 2  849  ? -29.017 -37.482  32.385  1.00 58.09  ?  849  ASN B C   1 
ATOM   7745  O  O   . ASN B 2  849  ? -28.728 -36.280  32.328  1.00 54.63  ?  849  ASN B O   1 
ATOM   7746  C  CB  . ASN B 2  849  ? -28.792 -39.738  31.216  1.00 48.94  ?  849  ASN B CB  1 
ATOM   7747  C  CG  . ASN B 2  849  ? -27.279 -39.808  31.275  1.00 51.81  ?  849  ASN B CG  1 
ATOM   7748  O  OD1 . ASN B 2  849  ? -26.583 -39.006  30.654  1.00 50.44  ?  849  ASN B OD1 1 
ATOM   7749  N  ND2 . ASN B 2  849  ? -26.762 -40.773  32.025  1.00 72.30  ?  849  ASN B ND2 1 
ATOM   7750  N  N   . CYS B 2  850  ? -29.080 -38.129  33.545  1.00 73.77  ?  850  CYS B N   1 
ATOM   7751  C  CA  . CYS B 2  850  ? -28.729 -37.455  34.789  1.00 73.29  ?  850  CYS B CA  1 
ATOM   7752  C  C   . CYS B 2  850  ? -27.227 -37.209  34.829  1.00 69.64  ?  850  CYS B C   1 
ATOM   7753  O  O   . CYS B 2  850  ? -26.433 -38.152  34.749  1.00 68.38  ?  850  CYS B O   1 
ATOM   7754  C  CB  . CYS B 2  850  ? -29.168 -38.283  35.993  1.00 68.91  ?  850  CYS B CB  1 
ATOM   7755  S  SG  . CYS B 2  850  ? -28.917 -37.453  37.575  1.00 72.09  ?  850  CYS B SG  1 
ATOM   7756  N  N   . MET B 2  851  ? -26.836 -35.940  34.948  1.00 61.29  ?  851  MET B N   1 
ATOM   7757  C  CA  . MET B 2  851  ? -25.421 -35.598  34.994  1.00 61.19  ?  851  MET B CA  1 
ATOM   7758  C  C   . MET B 2  851  ? -24.760 -35.997  36.306  1.00 62.88  ?  851  MET B C   1 
ATOM   7759  O  O   . MET B 2  851  ? -23.525 -36.012  36.372  1.00 63.96  ?  851  MET B O   1 
ATOM   7760  C  CB  . MET B 2  851  ? -25.237 -34.098  34.757  1.00 51.64  ?  851  MET B CB  1 
ATOM   7761  C  CG  . MET B 2  851  ? -25.958 -33.573  33.528  1.00 54.79  ?  851  MET B CG  1 
ATOM   7762  S  SD  . MET B 2  851  ? -24.994 -33.782  32.017  1.00 60.51  ?  851  MET B SD  1 
ATOM   7763  C  CE  . MET B 2  851  ? -25.913 -35.081  31.199  1.00 53.61  ?  851  MET B CE  1 
ATOM   7764  N  N   . GLN B 2  852  ? -25.543 -36.324  37.337  1.00 53.18  ?  852  GLN B N   1 
ATOM   7765  C  CA  . GLN B 2  852  ? -25.026 -36.702  38.652  1.00 54.97  ?  852  GLN B CA  1 
ATOM   7766  C  C   . GLN B 2  852  ? -24.117 -35.606  39.211  1.00 52.01  ?  852  GLN B C   1 
ATOM   7767  O  O   . GLN B 2  852  ? -22.926 -35.804  39.463  1.00 48.82  ?  852  GLN B O   1 
ATOM   7768  C  CB  . GLN B 2  852  ? -24.308 -38.054  38.589  1.00 51.72  ?  852  GLN B CB  1 
ATOM   7769  C  CG  . GLN B 2  852  ? -25.093 -39.119  37.843  1.00 45.79  ?  852  GLN B CG  1 
ATOM   7770  C  CD  . GLN B 2  852  ? -26.173 -39.748  38.698  1.00 53.91  ?  852  GLN B CD  1 
ATOM   7771  O  OE1 . GLN B 2  852  ? -26.117 -39.695  39.925  1.00 58.35  ?  852  GLN B OE1 1 
ATOM   7772  N  NE2 . GLN B 2  852  ? -27.172 -40.338  38.052  1.00 54.51  ?  852  GLN B NE2 1 
ATOM   7773  N  N   . CYS B 2  853  ? -24.714 -34.433  39.399  1.00 48.51  ?  853  CYS B N   1 
ATOM   7774  C  CA  . CYS B 2  853  ? -23.969 -33.262  39.837  1.00 48.21  ?  853  CYS B CA  1 
ATOM   7775  C  C   . CYS B 2  853  ? -23.485 -33.443  41.270  1.00 52.36  ?  853  CYS B C   1 
ATOM   7776  O  O   . CYS B 2  853  ? -24.272 -33.774  42.162  1.00 53.82  ?  853  CYS B O   1 
ATOM   7777  C  CB  . CYS B 2  853  ? -24.848 -32.018  39.728  1.00 51.23  ?  853  CYS B CB  1 
ATOM   7778  S  SG  . CYS B 2  853  ? -25.968 -32.016  38.306  1.00 42.25  ?  853  CYS B SG  1 
ATOM   7779  N  N   . GLU B 2  854  ? -22.185 -33.223  41.489  1.00 66.49  ?  854  GLU B N   1 
ATOM   7780  C  CA  . GLU B 2  854  ? -21.636 -33.327  42.838  1.00 61.06  ?  854  GLU B CA  1 
ATOM   7781  C  C   . GLU B 2  854  ? -22.327 -32.358  43.789  1.00 59.74  ?  854  GLU B C   1 
ATOM   7782  O  O   . GLU B 2  854  ? -22.587 -32.695  44.950  1.00 66.37  ?  854  GLU B O   1 
ATOM   7783  C  CB  . GLU B 2  854  ? -20.128 -33.076  42.816  1.00 65.70  ?  854  GLU B CB  1 
ATOM   7784  C  CG  . GLU B 2  854  ? -19.328 -34.141  42.081  1.00 69.14  ?  854  GLU B CG  1 
ATOM   7785  C  CD  . GLU B 2  854  ? -17.833 -33.885  42.128  1.00 70.80  ?  854  GLU B CD  1 
ATOM   7786  O  OE1 . GLU B 2  854  ? -17.411 -32.940  42.829  1.00 66.04  ?  854  GLU B OE1 1 
ATOM   7787  O  OE2 . GLU B 2  854  ? -17.079 -34.629  41.466  1.00 72.88  -1 854  GLU B OE2 1 
ATOM   7788  N  N   . LYS B 2  855  ? -22.632 -31.155  43.316  1.00 59.71  ?  855  LYS B N   1 
ATOM   7789  C  CA  . LYS B 2  855  ? -23.437 -30.191  44.058  1.00 59.42  ?  855  LYS B CA  1 
ATOM   7790  C  C   . LYS B 2  855  ? -24.810 -30.100  43.398  1.00 57.30  ?  855  LYS B C   1 
ATOM   7791  O  O   . LYS B 2  855  ? -25.176 -29.090  42.793  1.00 59.64  ?  855  LYS B O   1 
ATOM   7792  C  CB  . LYS B 2  855  ? -22.733 -28.828  44.107  1.00 60.33  ?  855  LYS B CB  1 
ATOM   7793  C  CG  . LYS B 2  855  ? -21.848 -28.628  45.329  1.00 58.16  ?  855  LYS B CG  1 
ATOM   7794  C  CD  . LYS B 2  855  ? -20.795 -27.556  45.085  1.00 61.53  ?  855  LYS B CD  1 
ATOM   7795  C  CE  . LYS B 2  855  ? -19.598 -28.112  44.331  1.00 62.70  ?  855  LYS B CE  1 
ATOM   7796  N  NZ  . LYS B 2  855  ? -18.457 -27.153  44.310  1.00 66.79  ?  855  LYS B NZ  1 
ATOM   7797  N  N   . ALA B 2  856  ? -25.573 -31.179  43.525  1.00 47.38  ?  856  ALA B N   1 
ATOM   7798  C  CA  . ALA B 2  856  ? -26.830 -31.321  42.798  1.00 44.51  ?  856  ALA B CA  1 
ATOM   7799  C  C   . ALA B 2  856  ? -27.882 -30.349  43.317  1.00 49.57  ?  856  ALA B C   1 
ATOM   7800  O  O   . ALA B 2  856  ? -28.267 -30.435  44.490  1.00 50.58  ?  856  ALA B O   1 
ATOM   7801  C  CB  . ALA B 2  856  ? -27.340 -32.754  42.909  1.00 47.91  ?  856  ALA B CB  1 
ATOM   7802  N  N   . PRO B 2  857  ? -28.380 -29.426  42.488  1.00 57.02  ?  857  PRO B N   1 
ATOM   7803  C  CA  . PRO B 2  857  ? -29.424 -28.500  42.954  1.00 55.18  ?  857  PRO B CA  1 
ATOM   7804  C  C   . PRO B 2  857  ? -30.770 -29.164  43.196  1.00 55.80  ?  857  PRO B C   1 
ATOM   7805  O  O   . PRO B 2  857  ? -31.627 -28.556  43.851  1.00 61.12  ?  857  PRO B O   1 
ATOM   7806  C  CB  . PRO B 2  857  ? -29.511 -27.472  41.819  1.00 51.37  ?  857  PRO B CB  1 
ATOM   7807  C  CG  . PRO B 2  857  ? -29.044 -28.212  40.611  1.00 49.11  ?  857  PRO B CG  1 
ATOM   7808  C  CD  . PRO B 2  857  ? -27.989 -29.167  41.092  1.00 55.51  ?  857  PRO B CD  1 
ATOM   7809  N  N   . CYS B 2  858  ? -30.989 -30.378  42.692  1.00 54.03  ?  858  CYS B N   1 
ATOM   7810  C  CA  . CYS B 2  858  ? -32.244 -31.081  42.923  1.00 50.28  ?  858  CYS B CA  1 
ATOM   7811  C  C   . CYS B 2  858  ? -32.344 -31.666  44.325  1.00 61.31  ?  858  CYS B C   1 
ATOM   7812  O  O   . CYS B 2  858  ? -33.428 -32.118  44.713  1.00 61.40  ?  858  CYS B O   1 
ATOM   7813  C  CB  . CYS B 2  858  ? -32.417 -32.201  41.894  1.00 53.15  ?  858  CYS B CB  1 
ATOM   7814  S  SG  . CYS B 2  858  ? -31.153 -33.489  41.985  1.00 62.36  ?  858  CYS B SG  1 
ATOM   7815  N  N   . GLU B 2  859  ? -31.249 -31.675  45.085  1.00 84.20  ?  859  GLU B N   1 
ATOM   7816  C  CA  . GLU B 2  859  ? -31.239 -32.246  46.423  1.00 88.20  ?  859  GLU B CA  1 
ATOM   7817  C  C   . GLU B 2  859  ? -31.494 -31.213  47.508  1.00 82.38  ?  859  GLU B C   1 
ATOM   7818  O  O   . GLU B 2  859  ? -31.930 -31.582  48.604  1.00 82.77  ?  859  GLU B O   1 
ATOM   7819  C  CB  . GLU B 2  859  ? -29.898 -32.936  46.694  1.00 82.09  ?  859  GLU B CB  1 
ATOM   7820  C  CG  . GLU B 2  859  ? -29.605 -34.102  45.771  1.00 75.29  ?  859  GLU B CG  1 
ATOM   7821  C  CD  . GLU B 2  859  ? -28.145 -34.509  45.791  1.00 83.89  ?  859  GLU B CD  1 
ATOM   7822  O  OE1 . GLU B 2  859  ? -27.335 -33.800  46.424  1.00 85.64  ?  859  GLU B OE1 1 
ATOM   7823  O  OE2 . GLU B 2  859  ? -27.806 -35.537  45.169  1.00 85.72  -1 859  GLU B OE2 1 
ATOM   7824  N  N   . VAL B 2  860  ? -31.249 -29.936  47.225  1.00 61.16  ?  860  VAL B N   1 
ATOM   7825  C  CA  . VAL B 2  860  ? -31.374 -28.886  48.229  1.00 59.82  ?  860  VAL B CA  1 
ATOM   7826  C  C   . VAL B 2  860  ? -32.771 -28.289  48.184  1.00 62.35  ?  860  VAL B C   1 
ATOM   7827  O  O   . VAL B 2  860  ? -33.033 -27.242  48.787  1.00 72.86  ?  860  VAL B O   1 
ATOM   7828  C  CB  . VAL B 2  860  ? -30.308 -27.795  48.028  1.00 67.29  ?  860  VAL B CB  1 
ATOM   7829  C  CG1 . VAL B 2  860  ? -28.923 -28.392  48.143  1.00 70.77  ?  860  VAL B CG1 1 
ATOM   7830  C  CG2 . VAL B 2  860  ? -30.500 -27.123  46.677  1.00 58.30  ?  860  VAL B CG2 1 
ATOM   7831  N  N   . VAL B 2  861  ? -33.686 -28.953  47.484  1.00 48.37  ?  861  VAL B N   1 
ATOM   7832  C  CA  . VAL B 2  861  ? -35.042 -28.431  47.371  1.00 53.22  ?  861  VAL B CA  1 
ATOM   7833  C  C   . VAL B 2  861  ? -36.108 -29.434  47.785  1.00 50.59  ?  861  VAL B C   1 
ATOM   7834  O  O   . VAL B 2  861  ? -37.272 -29.041  47.961  1.00 58.18  ?  861  VAL B O   1 
ATOM   7835  C  CB  . VAL B 2  861  ? -35.292 -27.942  45.930  1.00 53.84  ?  861  VAL B CB  1 
ATOM   7836  C  CG1 . VAL B 2  861  ? -34.538 -26.671  45.656  1.00 49.58  ?  861  VAL B CG1 1 
ATOM   7837  C  CG2 . VAL B 2  861  ? -34.884 -29.016  44.910  1.00 61.11  ?  861  VAL B CG2 1 
ATOM   7838  N  N   . CYS B 2  862  ? -35.816 -30.729  47.901  1.00 49.24  ?  862  CYS B N   1 
ATOM   7839  C  CA  . CYS B 2  862  ? -36.839 -31.707  48.228  1.00 57.46  ?  862  CYS B CA  1 
ATOM   7840  C  C   . CYS B 2  862  ? -37.017 -31.752  49.745  1.00 53.58  ?  862  CYS B C   1 
ATOM   7841  O  O   . CYS B 2  862  ? -36.081 -32.160  50.460  1.00 65.42  ?  862  CYS B O   1 
ATOM   7842  C  CB  . CYS B 2  862  ? -36.431 -33.055  47.700  1.00 55.91  ?  862  CYS B CB  1 
ATOM   7843  S  SG  . CYS B 2  862  ? -37.602 -34.331  47.939  1.00 53.72  ?  862  CYS B SG  1 
ATOM   7844  N  N   . PRO B 2  863  ? -38.178 -31.370  50.274  1.00 50.10  ?  863  PRO B N   1 
ATOM   7845  C  CA  . PRO B 2  863  ? -38.306 -31.200  51.720  1.00 61.44  ?  863  PRO B CA  1 
ATOM   7846  C  C   . PRO B 2  863  ? -38.250 -32.486  52.495  1.00 53.97  ?  863  PRO B C   1 
ATOM   7847  O  O   . PRO B 2  863  ? -37.994 -32.418  53.699  1.00 57.26  ?  863  PRO B O   1 
ATOM   7848  C  CB  . PRO B 2  863  ? -39.662 -30.507  51.884  1.00 62.29  ?  863  PRO B CB  1 
ATOM   7849  C  CG  . PRO B 2  863  ? -40.435 -30.842  50.651  1.00 56.18  ?  863  PRO B CG  1 
ATOM   7850  C  CD  . PRO B 2  863  ? -39.391 -30.899  49.565  1.00 54.49  ?  863  PRO B CD  1 
ATOM   7851  N  N   . VAL B 2  864  ? -38.485 -33.642  51.873  1.00 32.76  ?  864  VAL B N   1 
ATOM   7852  C  CA  . VAL B 2  864  ? -38.506 -34.909  52.595  1.00 39.36  ?  864  VAL B CA  1 
ATOM   7853  C  C   . VAL B 2  864  ? -37.207 -35.688  52.423  1.00 39.40  ?  864  VAL B C   1 
ATOM   7854  O  O   . VAL B 2  864  ? -37.152 -36.874  52.766  1.00 33.32  ?  864  VAL B O   1 
ATOM   7855  C  CB  . VAL B 2  864  ? -39.713 -35.765  52.183  1.00 35.33  ?  864  VAL B CB  1 
ATOM   7856  C  CG1 . VAL B 2  864  ? -41.003 -35.142  52.698  1.00 42.35  ?  864  VAL B CG1 1 
ATOM   7857  C  CG2 . VAL B 2  864  ? -39.756 -35.922  50.667  1.00 37.30  ?  864  VAL B CG2 1 
ATOM   7858  N  N   . ALA B 2  865  ? -36.162 -35.050  51.893  1.00 65.08  ?  865  ALA B N   1 
ATOM   7859  C  CA  . ALA B 2  865  ? -34.844 -35.667  51.739  1.00 56.93  ?  865  ALA B CA  1 
ATOM   7860  C  C   . ALA B 2  865  ? -34.902 -36.943  50.907  1.00 55.87  ?  865  ALA B C   1 
ATOM   7861  O  O   . ALA B 2  865  ? -34.124 -37.874  51.126  1.00 55.14  ?  865  ALA B O   1 
ATOM   7862  C  CB  . ALA B 2  865  ? -34.199 -35.949  53.098  1.00 59.65  ?  865  ALA B CB  1 
ATOM   7863  N  N   . ALA B 2  866  ? -35.828 -37.000  49.949  1.00 55.49  ?  866  ALA B N   1 
ATOM   7864  C  CA  . ALA B 2  866  ? -35.944 -38.172  49.091  1.00 47.08  ?  866  ALA B CA  1 
ATOM   7865  C  C   . ALA B 2  866  ? -34.848 -38.237  48.038  1.00 52.98  ?  866  ALA B C   1 
ATOM   7866  O  O   . ALA B 2  866  ? -34.597 -39.315  47.490  1.00 49.06  ?  866  ALA B O   1 
ATOM   7867  C  CB  . ALA B 2  866  ? -37.313 -38.193  48.411  1.00 45.86  ?  866  ALA B CB  1 
ATOM   7868  N  N   . THR B 2  867  ? -34.197 -37.114  47.742  1.00 74.14  ?  867  THR B N   1 
ATOM   7869  C  CA  . THR B 2  867  ? -33.092 -37.059  46.791  1.00 60.03  ?  867  THR B CA  1 
ATOM   7870  C  C   . THR B 2  867  ? -31.859 -36.549  47.525  1.00 64.10  ?  867  THR B C   1 
ATOM   7871  O  O   . THR B 2  867  ? -31.774 -35.361  47.853  1.00 67.69  ?  867  THR B O   1 
ATOM   7872  C  CB  . THR B 2  867  ? -33.430 -36.165  45.599  1.00 69.97  ?  867  THR B CB  1 
ATOM   7873  O  OG1 . THR B 2  867  ? -34.757 -36.455  45.143  1.00 73.10  ?  867  THR B OG1 1 
ATOM   7874  C  CG2 . THR B 2  867  ? -32.447 -36.400  44.463  1.00 66.25  ?  867  THR B CG2 1 
ATOM   7875  N  N   . VAL B 2  868  ? -30.912 -37.447  47.787  1.00 53.68  ?  868  VAL B N   1 
ATOM   7876  C  CA  . VAL B 2  868  ? -29.683 -37.092  48.486  1.00 54.34  ?  868  VAL B CA  1 
ATOM   7877  C  C   . VAL B 2  868  ? -28.496 -37.539  47.647  1.00 48.39  ?  868  VAL B C   1 
ATOM   7878  O  O   . VAL B 2  868  ? -28.662 -37.969  46.501  1.00 56.17  ?  868  VAL B O   1 
ATOM   7879  C  CB  . VAL B 2  868  ? -29.633 -37.723  49.888  1.00 55.81  ?  868  VAL B CB  1 
ATOM   7880  C  CG1 . VAL B 2  868  ? -30.757 -37.176  50.756  1.00 55.12  ?  868  VAL B CG1 1 
ATOM   7881  C  CG2 . VAL B 2  868  ? -29.711 -39.235  49.785  1.00 45.31  ?  868  VAL B CG2 1 
ATOM   7882  N  N   . HIS B 2  869  ? -27.296 -37.450  48.209  1.00 52.39  ?  869  HIS B N   1 
ATOM   7883  C  CA  . HIS B 2  869  ? -26.085 -37.838  47.505  1.00 55.25  ?  869  HIS B CA  1 
ATOM   7884  C  C   . HIS B 2  869  ? -25.464 -39.064  48.163  1.00 58.94  ?  869  HIS B C   1 
ATOM   7885  O  O   . HIS B 2  869  ? -25.681 -39.333  49.348  1.00 64.51  ?  869  HIS B O   1 
ATOM   7886  C  CB  . HIS B 2  869  ? -25.074 -36.688  47.467  1.00 61.65  ?  869  HIS B CB  1 
ATOM   7887  C  CG  . HIS B 2  869  ? -24.351 -36.569  46.162  1.00 55.40  ?  869  HIS B CG  1 
ATOM   7888  N  ND1 . HIS B 2  869  ? -24.933 -36.022  45.039  1.00 49.91  ?  869  HIS B ND1 1 
ATOM   7889  C  CD2 . HIS B 2  869  ? -23.098 -36.930  45.800  1.00 58.78  ?  869  HIS B CD2 1 
ATOM   7890  C  CE1 . HIS B 2  869  ? -24.068 -36.051  44.041  1.00 56.83  ?  869  HIS B CE1 1 
ATOM   7891  N  NE2 . HIS B 2  869  ? -22.946 -36.595  44.476  1.00 58.40  ?  869  HIS B NE2 1 
ATOM   7892  N  N   . ASP B 2  870  ? -24.690 -39.802  47.378  1.00 70.27  ?  870  ASP B N   1 
ATOM   7893  C  CA  . ASP B 2  870  ? -24.136 -41.085  47.780  1.00 73.37  ?  870  ASP B CA  1 
ATOM   7894  C  C   . ASP B 2  870  ? -22.673 -40.930  48.187  1.00 72.01  ?  870  ASP B C   1 
ATOM   7895  O  O   . ASP B 2  870  ? -22.015 -39.938  47.864  1.00 74.60  ?  870  ASP B O   1 
ATOM   7896  C  CB  . ASP B 2  870  ? -24.274 -42.096  46.634  1.00 74.13  ?  870  ASP B CB  1 
ATOM   7897  C  CG  . ASP B 2  870  ? -23.849 -43.498  47.025  1.00 79.55  ?  870  ASP B CG  1 
ATOM   7898  O  OD1 . ASP B 2  870  ? -24.415 -44.040  47.996  1.00 89.92  ?  870  ASP B OD1 1 
ATOM   7899  O  OD2 . ASP B 2  870  ? -22.954 -44.059  46.357  1.00 85.27  -1 870  ASP B OD2 1 
ATOM   7900  N  N   . TYR B 2  871  ? -22.174 -41.927  48.925  1.00 52.50  ?  871  TYR B N   1 
ATOM   7901  C  CA  . TYR B 2  871  ? -20.762 -41.951  49.296  1.00 54.40  ?  871  TYR B CA  1 
ATOM   7902  C  C   . TYR B 2  871  ? -19.866 -41.950  48.063  1.00 52.83  ?  871  TYR B C   1 
ATOM   7903  O  O   . TYR B 2  871  ? -18.809 -41.309  48.054  1.00 50.15  ?  871  TYR B O   1 
ATOM   7904  C  CB  . TYR B 2  871  ? -20.478 -43.176  50.169  1.00 57.02  ?  871  TYR B CB  1 
ATOM   7905  C  CG  . TYR B 2  871  ? -19.067 -43.272  50.711  1.00 54.04  ?  871  TYR B CG  1 
ATOM   7906  C  CD1 . TYR B 2  871  ? -18.645 -42.462  51.756  1.00 54.21  ?  871  TYR B CD1 1 
ATOM   7907  C  CD2 . TYR B 2  871  ? -18.164 -44.188  50.187  1.00 57.62  ?  871  TYR B CD2 1 
ATOM   7908  C  CE1 . TYR B 2  871  ? -17.358 -42.555  52.258  1.00 51.33  ?  871  TYR B CE1 1 
ATOM   7909  C  CE2 . TYR B 2  871  ? -16.876 -44.288  50.682  1.00 52.30  ?  871  TYR B CE2 1 
ATOM   7910  C  CZ  . TYR B 2  871  ? -16.479 -43.469  51.716  1.00 48.06  ?  871  TYR B CZ  1 
ATOM   7911  O  OH  . TYR B 2  871  ? -15.198 -43.566  52.209  1.00 47.59  ?  871  TYR B OH  1 
ATOM   7912  N  N   . GLU B 2  872  ? -20.278 -42.652  47.009  1.00 71.16  ?  872  GLU B N   1 
ATOM   7913  C  CA  . GLU B 2  872  ? -19.513 -42.742  45.774  1.00 70.50  ?  872  GLU B CA  1 
ATOM   7914  C  C   . GLU B 2  872  ? -19.795 -41.592  44.812  1.00 77.33  ?  872  GLU B C   1 
ATOM   7915  O  O   . GLU B 2  872  ? -19.381 -41.660  43.649  1.00 75.97  ?  872  GLU B O   1 
ATOM   7916  C  CB  . GLU B 2  872  ? -19.793 -44.076  45.076  1.00 69.38  ?  872  GLU B CB  1 
ATOM   7917  C  CG  . GLU B 2  872  ? -18.900 -45.221  45.526  1.00 75.30  ?  872  GLU B CG  1 
ATOM   7918  C  CD  . GLU B 2  872  ? -19.497 -46.014  46.671  1.00 84.47  ?  872  GLU B CD  1 
ATOM   7919  O  OE1 . GLU B 2  872  ? -20.719 -45.897  46.904  1.00 83.56  ?  872  GLU B OE1 1 
ATOM   7920  O  OE2 . GLU B 2  872  ? -18.744 -46.754  47.338  1.00 88.04  -1 872  GLU B OE2 1 
ATOM   7921  N  N   . GLY B 2  873  ? -20.481 -40.543  45.263  1.00 69.49  ?  873  GLY B N   1 
ATOM   7922  C  CA  . GLY B 2  873  ? -20.796 -39.414  44.414  1.00 68.87  ?  873  GLY B CA  1 
ATOM   7923  C  C   . GLY B 2  873  ? -22.052 -39.561  43.583  1.00 61.98  ?  873  GLY B C   1 
ATOM   7924  O  O   . GLY B 2  873  ? -22.376 -38.648  42.813  1.00 61.06  ?  873  GLY B O   1 
ATOM   7925  N  N   . LEU B 2  874  ? -22.763 -40.677  43.707  1.00 41.73  ?  874  LEU B N   1 
ATOM   7926  C  CA  . LEU B 2  874  ? -23.999 -40.902  42.978  1.00 34.12  ?  874  LEU B CA  1 
ATOM   7927  C  C   . LEU B 2  874  ? -25.133 -40.074  43.582  1.00 44.40  ?  874  LEU B C   1 
ATOM   7928  O  O   . LEU B 2  874  ? -25.082 -39.654  44.740  1.00 51.43  ?  874  LEU B O   1 
ATOM   7929  C  CB  . LEU B 2  874  ? -24.350 -42.392  42.995  1.00 47.50  ?  874  LEU B CB  1 
ATOM   7930  C  CG  . LEU B 2  874  ? -25.508 -42.915  42.145  1.00 48.97  ?  874  LEU B CG  1 
ATOM   7931  C  CD1 . LEU B 2  874  ? -25.205 -42.723  40.674  1.00 49.02  ?  874  LEU B CD1 1 
ATOM   7932  C  CD2 . LEU B 2  874  ? -25.783 -44.381  42.453  1.00 44.43  ?  874  LEU B CD2 1 
ATOM   7933  N  N   . ASN B 2  875  ? -26.166 -39.835  42.774  1.00 40.61  ?  875  ASN B N   1 
ATOM   7934  C  CA  . ASN B 2  875  ? -27.341 -39.075  43.193  1.00 43.84  ?  875  ASN B CA  1 
ATOM   7935  C  C   . ASN B 2  875  ? -28.468 -40.060  43.484  1.00 38.99  ?  875  ASN B C   1 
ATOM   7936  O  O   . ASN B 2  875  ? -29.063 -40.623  42.561  1.00 42.20  ?  875  ASN B O   1 
ATOM   7937  C  CB  . ASN B 2  875  ? -27.749 -38.072  42.115  1.00 42.54  ?  875  ASN B CB  1 
ATOM   7938  C  CG  . ASN B 2  875  ? -28.927 -37.206  42.529  1.00 42.51  ?  875  ASN B CG  1 
ATOM   7939  O  OD1 . ASN B 2  875  ? -29.387 -37.257  43.670  1.00 43.65  ?  875  ASN B OD1 1 
ATOM   7940  N  ND2 . ASN B 2  875  ? -29.436 -36.418  41.589  1.00 57.99  ?  875  ASN B ND2 1 
ATOM   7941  N  N   . ASN B 2  876  ? -28.763 -40.260  44.766  1.00 74.16  ?  876  ASN B N   1 
ATOM   7942  C  CA  . ASN B 2  876  ? -29.775 -41.225  45.175  1.00 69.35  ?  876  ASN B CA  1 
ATOM   7943  C  C   . ASN B 2  876  ? -31.163 -40.604  45.052  1.00 70.23  ?  876  ASN B C   1 
ATOM   7944  O  O   . ASN B 2  876  ? -31.447 -39.577  45.677  1.00 78.01  ?  876  ASN B O   1 
ATOM   7945  C  CB  . ASN B 2  876  ? -29.521 -41.688  46.608  1.00 72.36  ?  876  ASN B CB  1 
ATOM   7946  C  CG  . ASN B 2  876  ? -28.164 -42.346  46.778  1.00 79.02  ?  876  ASN B CG  1 
ATOM   7947  O  OD1 . ASN B 2  876  ? -27.499 -42.688  45.800  1.00 85.68  ?  876  ASN B OD1 1 
ATOM   7948  N  ND2 . ASN B 2  876  ? -27.747 -42.530  48.026  1.00 81.37  ?  876  ASN B ND2 1 
ATOM   7949  N  N   . MET B 2  877  ? -32.023 -41.225  44.244  1.00 35.35  ?  877  MET B N   1 
ATOM   7950  C  CA  . MET B 2  877  ? -33.429 -40.847  44.123  1.00 38.16  ?  877  MET B CA  1 
ATOM   7951  C  C   . MET B 2  877  ? -34.273 -42.000  44.656  1.00 43.31  ?  877  MET B C   1 
ATOM   7952  O  O   . MET B 2  877  ? -34.358 -43.060  44.025  1.00 40.41  ?  877  MET B O   1 
ATOM   7953  C  CB  . MET B 2  877  ? -33.789 -40.522  42.676  1.00 43.81  ?  877  MET B CB  1 
ATOM   7954  C  CG  . MET B 2  877  ? -35.285 -40.434  42.407  1.00 43.77  ?  877  MET B CG  1 
ATOM   7955  S  SD  . MET B 2  877  ? -36.063 -38.977  43.130  1.00 49.44  ?  877  MET B SD  1 
ATOM   7956  C  CE  . MET B 2  877  ? -37.474 -39.717  43.943  1.00 48.21  ?  877  MET B CE  1 
ATOM   7957  N  N   . VAL B 2  878  ? -34.898 -41.791  45.810  1.00 57.79  ?  878  VAL B N   1 
ATOM   7958  C  CA  . VAL B 2  878  ? -35.599 -42.845  46.534  1.00 56.71  ?  878  VAL B CA  1 
ATOM   7959  C  C   . VAL B 2  878  ? -37.092 -42.668  46.304  1.00 62.09  ?  878  VAL B C   1 
ATOM   7960  O  O   . VAL B 2  878  ? -37.670 -41.642  46.683  1.00 65.57  ?  878  VAL B O   1 
ATOM   7961  C  CB  . VAL B 2  878  ? -35.259 -42.810  48.031  1.00 42.44  ?  878  VAL B CB  1 
ATOM   7962  C  CG1 . VAL B 2  878  ? -35.710 -44.086  48.703  1.00 50.15  ?  878  VAL B CG1 1 
ATOM   7963  C  CG2 . VAL B 2  878  ? -33.772 -42.591  48.222  1.00 48.72  ?  878  VAL B CG2 1 
ATOM   7964  N  N   . TYR B 2  879  ? -37.721 -43.679  45.699  1.00 61.74  ?  879  TYR B N   1 
ATOM   7965  C  CA  . TYR B 2  879  ? -39.112 -43.546  45.279  1.00 60.60  ?  879  TYR B CA  1 
ATOM   7966  C  C   . TYR B 2  879  ? -40.064 -43.537  46.468  1.00 58.01  ?  879  TYR B C   1 
ATOM   7967  O  O   . TYR B 2  879  ? -41.011 -42.742  46.503  1.00 59.44  ?  879  TYR B O   1 
ATOM   7968  C  CB  . TYR B 2  879  ? -39.478 -44.676  44.316  1.00 48.04  ?  879  TYR B CB  1 
ATOM   7969  C  CG  . TYR B 2  879  ? -38.450 -44.920  43.235  1.00 51.25  ?  879  TYR B CG  1 
ATOM   7970  C  CD1 . TYR B 2  879  ? -38.172 -43.952  42.280  1.00 60.53  ?  879  TYR B CD1 1 
ATOM   7971  C  CD2 . TYR B 2  879  ? -37.754 -46.120  43.174  1.00 56.80  ?  879  TYR B CD2 1 
ATOM   7972  C  CE1 . TYR B 2  879  ? -37.229 -44.175  41.289  1.00 58.93  ?  879  TYR B CE1 1 
ATOM   7973  C  CE2 . TYR B 2  879  ? -36.810 -46.352  42.188  1.00 59.13  ?  879  TYR B CE2 1 
ATOM   7974  C  CZ  . TYR B 2  879  ? -36.551 -45.377  41.249  1.00 50.02  ?  879  TYR B CZ  1 
ATOM   7975  O  OH  . TYR B 2  879  ? -35.611 -45.604  40.268  1.00 45.79  ?  879  TYR B OH  1 
ATOM   7976  N  N   . ASN B 2  880  ? -39.838 -44.413  47.449  1.00 69.24  ?  880  ASN B N   1 
ATOM   7977  C  CA  . ASN B 2  880  ? -40.792 -44.556  48.542  1.00 72.21  ?  880  ASN B CA  1 
ATOM   7978  C  C   . ASN B 2  880  ? -40.821 -43.335  49.453  1.00 80.80  ?  880  ASN B C   1 
ATOM   7979  O  O   . ASN B 2  880  ? -41.794 -43.155  50.195  1.00 81.53  ?  880  ASN B O   1 
ATOM   7980  C  CB  . ASN B 2  880  ? -40.477 -45.819  49.348  1.00 68.48  ?  880  ASN B CB  1 
ATOM   7981  C  CG  . ASN B 2  880  ? -39.055 -45.834  49.893  1.00 76.39  ?  880  ASN B CG  1 
ATOM   7982  O  OD1 . ASN B 2  880  ? -38.405 -44.796  50.008  1.00 84.29  ?  880  ASN B OD1 1 
ATOM   7983  N  ND2 . ASN B 2  880  ? -38.562 -47.022  50.217  1.00 68.50  ?  880  ASN B ND2 1 
ATOM   7984  N  N   . ARG B 2  881  ? -39.855 -42.425  49.312  1.00 72.25  ?  881  ARG B N   1 
ATOM   7985  C  CA  . ARG B 2  881  ? -39.869 -41.183  50.135  1.00 70.57  ?  881  ARG B CA  1 
ATOM   7986  C  C   . ARG B 2  881  ? -40.482 -40.012  49.355  1.00 67.52  ?  881  ARG B C   1 
ATOM   7987  O  O   . ARG B 2  881  ? -40.983 -39.093  50.010  1.00 67.88  ?  881  ARG B O   1 
ATOM   7988  C  CB  . ARG B 2  881  ? -38.459 -40.844  50.618  1.00 72.24  ?  881  ARG B CB  1 
ATOM   7989  C  CG  . ARG B 2  881  ? -38.375 -39.666  51.577  1.00 63.52  ?  881  ARG B CG  1 
ATOM   7990  C  CD  . ARG B 2  881  ? -39.079 -39.903  52.896  1.00 59.84  ?  881  ARG B CD  1 
ATOM   7991  N  NE  . ARG B 2  881  ? -38.831 -38.806  53.817  1.00 70.68  ?  881  ARG B NE  1 
ATOM   7992  C  CZ  . ARG B 2  881  ? -39.329 -38.726  55.044  1.00 79.05  ?  881  ARG B CZ  1 
ATOM   7993  N  NH1 . ARG B 2  881  ? -40.168 -39.648  55.479  1.00 79.36  ?  881  ARG B NH1 1 
ATOM   7994  N  NH2 . ARG B 2  881  ? -38.989 -37.721  55.831  1.00 80.24  ?  881  ARG B NH2 1 
ATOM   7995  N  N   . CYS B 2  882  ? -40.461 -40.027  48.020  1.00 45.66  ?  882  CYS B N   1 
ATOM   7996  C  CA  . CYS B 2  882  ? -40.971 -38.834  47.289  1.00 56.42  ?  882  CYS B CA  1 
ATOM   7997  C  C   . CYS B 2  882  ? -42.447 -38.628  47.617  1.00 54.87  ?  882  CYS B C   1 
ATOM   7998  O  O   . CYS B 2  882  ? -43.216 -39.596  47.537  1.00 47.88  ?  882  CYS B O   1 
ATOM   7999  C  CB  . CYS B 2  882  ? -40.838 -38.929  45.773  1.00 52.41  ?  882  CYS B CB  1 
ATOM   8000  S  SG  . CYS B 2  882  ? -41.377 -37.435  44.906  1.00 40.94  ?  882  CYS B SG  1 
ATOM   8001  N  N   . VAL B 2  883  ? -42.802 -37.408  48.003  1.00 59.89  ?  883  VAL B N   1 
ATOM   8002  C  CA  . VAL B 2  883  ? -44.220 -37.080  48.274  1.00 57.49  ?  883  VAL B CA  1 
ATOM   8003  C  C   . VAL B 2  883  ? -44.741 -36.505  46.966  1.00 58.49  ?  883  VAL B C   1 
ATOM   8004  O  O   . VAL B 2  883  ? -45.959 -36.495  46.781  1.00 61.49  ?  883  VAL B O   1 
ATOM   8005  C  CB  . VAL B 2  883  ? -44.368 -36.094  49.441  1.00 59.24  ?  883  VAL B CB  1 
ATOM   8006  C  CG1 . VAL B 2  883  ? -44.172 -36.782  50.781  1.00 53.77  ?  883  VAL B CG1 1 
ATOM   8007  C  CG2 . VAL B 2  883  ? -43.421 -34.916  49.305  1.00 46.70  ?  883  VAL B CG2 1 
ATOM   8008  N  N   . GLY B 2  884  ? -43.830 -36.080  46.090  1.00 78.17  ?  884  GLY B N   1 
ATOM   8009  C  CA  . GLY B 2  884  ? -44.234 -35.578  44.797  1.00 71.78  ?  884  GLY B CA  1 
ATOM   8010  C  C   . GLY B 2  884  ? -44.392 -34.078  44.689  1.00 70.15  ?  884  GLY B C   1 
ATOM   8011  O  O   . GLY B 2  884  ? -45.281 -33.621  43.962  1.00 71.83  ?  884  GLY B O   1 
ATOM   8012  N  N   . THR B 2  885  ? -43.567 -33.295  45.390  1.00 83.54  ?  885  THR B N   1 
ATOM   8013  C  CA  . THR B 2  885  ? -43.687 -31.843  45.331  1.00 78.93  ?  885  THR B CA  1 
ATOM   8014  C  C   . THR B 2  885  ? -43.372 -31.281  43.951  1.00 78.66  ?  885  THR B C   1 
ATOM   8015  O  O   . THR B 2  885  ? -43.693 -30.117  43.690  1.00 78.14  ?  885  THR B O   1 
ATOM   8016  C  CB  . THR B 2  885  ? -42.764 -31.189  46.361  1.00 72.35  ?  885  THR B CB  1 
ATOM   8017  O  OG1 . THR B 2  885  ? -41.422 -31.176  45.858  1.00 78.76  ?  885  THR B OG1 1 
ATOM   8018  C  CG2 . THR B 2  885  ? -42.804 -31.950  47.670  1.00 76.47  ?  885  THR B CG2 1 
ATOM   8019  N  N   . LYS B 2  886  ? -42.744 -32.066  43.076  1.00 66.71  ?  886  LYS B N   1 
ATOM   8020  C  CA  . LYS B 2  886  ? -42.350 -31.653  41.731  1.00 61.13  ?  886  LYS B CA  1 
ATOM   8021  C  C   . LYS B 2  886  ? -41.419 -30.442  41.735  1.00 59.35  ?  886  LYS B C   1 
ATOM   8022  O  O   . LYS B 2  886  ? -41.190 -29.832  40.684  1.00 56.55  ?  886  LYS B O   1 
ATOM   8023  C  CB  . LYS B 2  886  ? -43.580 -31.385  40.851  1.00 59.71  ?  886  LYS B CB  1 
ATOM   8024  C  CG  . LYS B 2  886  ? -44.459 -32.611  40.665  1.00 55.68  ?  886  LYS B CG  1 
ATOM   8025  C  CD  . LYS B 2  886  ? -45.834 -32.250  40.143  1.00 63.22  ?  886  LYS B CD  1 
ATOM   8026  C  CE  . LYS B 2  886  ? -46.604 -31.463  41.193  1.00 70.61  ?  886  LYS B CE  1 
ATOM   8027  N  NZ  . LYS B 2  886  ? -46.895 -32.266  42.415  1.00 61.52  ?  886  LYS B NZ  1 
ATOM   8028  N  N   . TYR B 2  887  ? -40.813 -30.145  42.881  1.00 66.07  ?  887  TYR B N   1 
ATOM   8029  C  CA  . TYR B 2  887  ? -39.839 -29.027  42.990  1.00 71.95  ?  887  TYR B CA  1 
ATOM   8030  C  C   . TYR B 2  887  ? -38.458 -29.551  42.584  1.00 67.13  ?  887  TYR B C   1 
ATOM   8031  O  O   . TYR B 2  887  ? -37.616 -28.764  42.139  1.00 66.05  ?  887  TYR B O   1 
ATOM   8032  C  CB  . TYR B 2  887  ? -39.868 -28.525  44.434  1.00 69.40  ?  887  TYR B CB  1 
ATOM   8033  C  CG  . TYR B 2  887  ? -39.135 -27.254  44.777  1.00 63.28  ?  887  TYR B CG  1 
ATOM   8034  C  CD1 . TYR B 2  887  ? -38.523 -26.471  43.816  1.00 72.58  ?  887  TYR B CD1 1 
ATOM   8035  C  CD2 . TYR B 2  887  ? -39.053 -26.842  46.096  1.00 68.92  ?  887  TYR B CD2 1 
ATOM   8036  C  CE1 . TYR B 2  887  ? -37.850 -25.310  44.157  1.00 78.86  ?  887  TYR B CE1 1 
ATOM   8037  C  CE2 . TYR B 2  887  ? -38.386 -25.686  46.456  1.00 72.21  ?  887  TYR B CE2 1 
ATOM   8038  C  CZ  . TYR B 2  887  ? -37.782 -24.916  45.481  1.00 81.15  ?  887  TYR B CZ  1 
ATOM   8039  O  OH  . TYR B 2  887  ? -37.118 -23.773  45.842  1.00 86.30  ?  887  TYR B OH  1 
ATOM   8040  N  N   . CYS B 2  888  ? -38.235 -30.854  42.732  1.00 67.68  ?  888  CYS B N   1 
ATOM   8041  C  CA  . CYS B 2  888  ? -36.914 -31.454  42.412  1.00 66.51  ?  888  CYS B CA  1 
ATOM   8042  C  C   . CYS B 2  888  ? -36.641 -31.362  40.912  1.00 64.48  ?  888  CYS B C   1 
ATOM   8043  O  O   . CYS B 2  888  ? -35.478 -31.522  40.522  1.00 60.29  ?  888  CYS B O   1 
ATOM   8044  C  CB  . CYS B 2  888  ? -36.872 -32.912  42.857  1.00 73.40  ?  888  CYS B CB  1 
ATOM   8045  S  SG  . CYS B 2  888  ? -38.188 -33.964  42.200  1.00 92.68  ?  888  CYS B SG  1 
ATOM   8046  N  N   . SER B 2  889  ? -37.654 -31.052  40.114  1.00 68.44  ?  889  SER B N   1 
ATOM   8047  C  CA  . SER B 2  889  ? -37.540 -31.062  38.655  1.00 62.32  ?  889  SER B CA  1 
ATOM   8048  C  C   . SER B 2  889  ? -37.340 -29.620  38.201  1.00 64.70  ?  889  SER B C   1 
ATOM   8049  O  O   . SER B 2  889  ? -36.546 -29.353  37.290  1.00 62.11  ?  889  SER B O   1 
ATOM   8050  C  CB  . SER B 2  889  ? -38.748 -31.677  37.938  1.00 68.82  ?  889  SER B CB  1 
ATOM   8051  O  OG  . SER B 2  889  ? -38.598 -31.635  36.527  1.00 64.03  ?  889  SER B OG  1 
ATOM   8052  N  N   . ASN B 2  890  ? -38.039 -28.678  38.841  1.00 58.34  ?  890  ASN B N   1 
ATOM   8053  C  CA  . ASN B 2  890  ? -37.925 -27.274  38.461  1.00 49.60  ?  890  ASN B CA  1 
ATOM   8054  C  C   . ASN B 2  890  ? -36.527 -26.730  38.728  1.00 46.20  ?  890  ASN B C   1 
ATOM   8055  O  O   . ASN B 2  890  ? -36.075 -25.822  38.022  1.00 47.45  ?  890  ASN B O   1 
ATOM   8056  C  CB  . ASN B 2  890  ? -38.974 -26.446  39.204  1.00 45.67  ?  890  ASN B CB  1 
ATOM   8057  C  CG  . ASN B 2  890  ? -40.380 -26.984  39.012  1.00 58.19  ?  890  ASN B CG  1 
ATOM   8058  O  OD1 . ASN B 2  890  ? -40.657 -27.681  38.034  1.00 64.93  ?  890  ASN B OD1 1 
ATOM   8059  N  ND2 . ASN B 2  890  ? -41.272 -26.672  39.948  1.00 53.84  ?  890  ASN B ND2 1 
ATOM   8060  N  N   . ASN B 2  891  ? -35.830 -27.267  39.726  1.00 35.40  ?  891  ASN B N   1 
ATOM   8061  C  CA  . ASN B 2  891  ? -34.464 -26.857  40.015  1.00 37.91  ?  891  ASN B CA  1 
ATOM   8062  C  C   . ASN B 2  891  ? -33.426 -27.650  39.233  1.00 43.83  ?  891  ASN B C   1 
ATOM   8063  O  O   . ASN B 2  891  ? -32.232 -27.351  39.340  1.00 44.79  ?  891  ASN B O   1 
ATOM   8064  C  CB  . ASN B 2  891  ? -34.174 -26.978  41.514  1.00 41.64  ?  891  ASN B CB  1 
ATOM   8065  C  CG  . ASN B 2  891  ? -33.162 -25.954  41.990  1.00 49.05  ?  891  ASN B CG  1 
ATOM   8066  O  OD1 . ASN B 2  891  ? -32.955 -24.926  41.344  1.00 44.74  ?  891  ASN B OD1 1 
ATOM   8067  N  ND2 . ASN B 2  891  ? -32.515 -26.236  43.114  1.00 48.41  ?  891  ASN B ND2 1 
ATOM   8068  N  N   . CYS B 2  892  ? -33.840 -28.647  38.458  1.00 52.76  ?  892  CYS B N   1 
ATOM   8069  C  CA  . CYS B 2  892  ? -32.895 -29.408  37.649  1.00 47.68  ?  892  CYS B CA  1 
ATOM   8070  C  C   . CYS B 2  892  ? -32.587 -28.636  36.372  1.00 47.30  ?  892  CYS B C   1 
ATOM   8071  O  O   . CYS B 2  892  ? -33.492 -28.423  35.557  1.00 48.94  ?  892  CYS B O   1 
ATOM   8072  C  CB  . CYS B 2  892  ? -33.453 -30.785  37.313  1.00 51.62  ?  892  CYS B CB  1 
ATOM   8073  S  SG  . CYS B 2  892  ? -32.343 -31.820  36.313  1.00 50.19  ?  892  CYS B SG  1 
ATOM   8074  N  N   . PRO B 2  893  ? -31.343 -28.199  36.160  1.00 58.41  ?  893  PRO B N   1 
ATOM   8075  C  CA  . PRO B 2  893  ? -31.056 -27.365  34.982  1.00 61.56  ?  893  PRO B CA  1 
ATOM   8076  C  C   . PRO B 2  893  ? -31.226 -28.098  33.667  1.00 77.75  ?  893  PRO B C   1 
ATOM   8077  O  O   . PRO B 2  893  ? -31.544 -27.462  32.654  1.00 87.40  ?  893  PRO B O   1 
ATOM   8078  C  CB  . PRO B 2  893  ? -29.597 -26.938  35.199  1.00 74.11  ?  893  PRO B CB  1 
ATOM   8079  C  CG  . PRO B 2  893  ? -29.326 -27.184  36.656  1.00 73.52  ?  893  PRO B CG  1 
ATOM   8080  C  CD  . PRO B 2  893  ? -30.159 -28.370  37.016  1.00 68.30  ?  893  PRO B CD  1 
ATOM   8081  N  N   . TYR B 2  894  ? -31.026 -29.414  33.650  1.00 55.64  ?  894  TYR B N   1 
ATOM   8082  C  CA  . TYR B 2  894  ? -31.090 -30.198  32.426  1.00 50.29  ?  894  TYR B CA  1 
ATOM   8083  C  C   . TYR B 2  894  ? -32.449 -30.844  32.200  1.00 46.70  ?  894  TYR B C   1 
ATOM   8084  O  O   . TYR B 2  894  ? -32.678 -31.398  31.119  1.00 57.57  ?  894  TYR B O   1 
ATOM   8085  C  CB  . TYR B 2  894  ? -30.001 -31.281  32.439  1.00 44.98  ?  894  TYR B CB  1 
ATOM   8086  C  CG  . TYR B 2  894  ? -28.658 -30.780  32.930  1.00 51.96  ?  894  TYR B CG  1 
ATOM   8087  C  CD1 . TYR B 2  894  ? -27.735 -30.231  32.050  1.00 49.57  ?  894  TYR B CD1 1 
ATOM   8088  C  CD2 . TYR B 2  894  ? -28.316 -30.852  34.276  1.00 46.15  ?  894  TYR B CD2 1 
ATOM   8089  C  CE1 . TYR B 2  894  ? -26.509 -29.770  32.494  1.00 43.30  ?  894  TYR B CE1 1 
ATOM   8090  C  CE2 . TYR B 2  894  ? -27.093 -30.391  34.729  1.00 46.41  ?  894  TYR B CE2 1 
ATOM   8091  C  CZ  . TYR B 2  894  ? -26.194 -29.852  33.834  1.00 44.45  ?  894  TYR B CZ  1 
ATOM   8092  O  OH  . TYR B 2  894  ? -24.975 -29.395  34.278  1.00 46.38  ?  894  TYR B OH  1 
ATOM   8093  N  N   . LYS B 2  895  ? -33.347 -30.781  33.182  1.00 49.21  ?  895  LYS B N   1 
ATOM   8094  C  CA  . LYS B 2  895  ? -34.697 -31.335  33.079  1.00 55.68  ?  895  LYS B CA  1 
ATOM   8095  C  C   . LYS B 2  895  ? -34.654 -32.811  32.684  1.00 58.16  ?  895  LYS B C   1 
ATOM   8096  O  O   . LYS B 2  895  ? -35.182 -33.229  31.653  1.00 59.49  ?  895  LYS B O   1 
ATOM   8097  C  CB  . LYS B 2  895  ? -35.545 -30.521  32.099  1.00 56.37  ?  895  LYS B CB  1 
ATOM   8098  C  CG  . LYS B 2  895  ? -35.842 -29.107  32.569  1.00 57.82  ?  895  LYS B CG  1 
ATOM   8099  C  CD  . LYS B 2  895  ? -36.649 -29.122  33.858  1.00 66.15  ?  895  LYS B CD  1 
ATOM   8100  C  CE  . LYS B 2  895  ? -36.993 -27.714  34.313  1.00 65.55  ?  895  LYS B CE  1 
ATOM   8101  N  NZ  . LYS B 2  895  ? -35.772 -26.890  34.531  1.00 61.23  ?  895  LYS B NZ  1 
ATOM   8102  N  N   . VAL B 2  896  ? -34.005 -33.599  33.535  1.00 53.36  ?  896  VAL B N   1 
ATOM   8103  C  CA  . VAL B 2  896  ? -33.815 -35.021  33.292  1.00 50.21  ?  896  VAL B CA  1 
ATOM   8104  C  C   . VAL B 2  896  ? -34.631 -35.863  34.271  1.00 48.22  ?  896  VAL B C   1 
ATOM   8105  O  O   . VAL B 2  896  ? -34.370 -37.054  34.428  1.00 56.52  ?  896  VAL B O   1 
ATOM   8106  C  CB  . VAL B 2  896  ? -32.327 -35.398  33.343  1.00 50.08  ?  896  VAL B CB  1 
ATOM   8107  C  CG1 . VAL B 2  896  ? -31.570 -34.709  32.219  1.00 55.76  ?  896  VAL B CG1 1 
ATOM   8108  C  CG2 . VAL B 2  896  ? -31.735 -35.040  34.698  1.00 64.05  ?  896  VAL B CG2 1 
ATOM   8109  N  N   . ARG B 2  897  ? -35.614 -35.260  34.931  1.00 52.54  ?  897  ARG B N   1 
ATOM   8110  C  CA  . ARG B 2  897  ? -36.437 -35.939  35.922  1.00 49.99  ?  897  ARG B CA  1 
ATOM   8111  C  C   . ARG B 2  897  ? -37.858 -36.062  35.395  1.00 51.68  ?  897  ARG B C   1 
ATOM   8112  O  O   . ARG B 2  897  ? -38.438 -35.077  34.925  1.00 63.52  ?  897  ARG B O   1 
ATOM   8113  C  CB  . ARG B 2  897  ? -36.424 -35.185  37.253  1.00 50.55  ?  897  ARG B CB  1 
ATOM   8114  C  CG  . ARG B 2  897  ? -35.028 -34.965  37.812  1.00 55.04  ?  897  ARG B CG  1 
ATOM   8115  C  CD  . ARG B 2  897  ? -35.057 -34.255  39.153  1.00 55.54  ?  897  ARG B CD  1 
ATOM   8116  N  NE  . ARG B 2  897  ? -35.336 -35.179  40.244  1.00 54.16  ?  897  ARG B NE  1 
ATOM   8117  C  CZ  . ARG B 2  897  ? -34.413 -35.678  41.053  1.00 55.83  ?  897  ARG B CZ  1 
ATOM   8118  N  NH1 . ARG B 2  897  ? -33.134 -35.364  40.920  1.00 65.10  ?  897  ARG B NH1 1 
ATOM   8119  N  NH2 . ARG B 2  897  ? -34.780 -36.516  42.017  1.00 57.90  ?  897  ARG B NH2 1 
ATOM   8120  N  N   . ARG B 2  898  ? -38.412 -37.267  35.472  1.00 66.24  ?  898  ARG B N   1 
ATOM   8121  C  CA  . ARG B 2  898  ? -39.747 -37.553  34.970  1.00 72.51  ?  898  ARG B CA  1 
ATOM   8122  C  C   . ARG B 2  898  ? -40.663 -37.928  36.127  1.00 68.76  ?  898  ARG B C   1 
ATOM   8123  O  O   . ARG B 2  898  ? -40.244 -38.618  37.062  1.00 69.94  ?  898  ARG B O   1 
ATOM   8124  C  CB  . ARG B 2  898  ? -39.710 -38.679  33.933  1.00 68.29  ?  898  ARG B CB  1 
ATOM   8125  C  CG  . ARG B 2  898  ? -38.777 -38.400  32.764  1.00 67.45  ?  898  ARG B CG  1 
ATOM   8126  C  CD  . ARG B 2  898  ? -39.231 -37.172  31.989  1.00 77.95  ?  898  ARG B CD  1 
ATOM   8127  N  NE  . ARG B 2  898  ? -38.687 -37.134  30.637  1.00 72.24  ?  898  ARG B NE  1 
ATOM   8128  C  CZ  . ARG B 2  898  ? -37.774 -36.268  30.219  1.00 76.61  ?  898  ARG B CZ  1 
ATOM   8129  N  NH1 . ARG B 2  898  ? -37.273 -35.348  31.026  1.00 83.68  ?  898  ARG B NH1 1 
ATOM   8130  N  NH2 . ARG B 2  898  ? -37.357 -36.324  28.957  1.00 73.14  ?  898  ARG B NH2 1 
ATOM   8131  N  N   . PHE B 2  899  ? -41.911 -37.471  36.060  1.00 52.07  ?  899  PHE B N   1 
ATOM   8132  C  CA  . PHE B 2  899  ? -42.872 -37.635  37.142  1.00 44.76  ?  899  PHE B CA  1 
ATOM   8133  C  C   . PHE B 2  899  ? -44.042 -38.497  36.693  1.00 44.06  ?  899  PHE B C   1 
ATOM   8134  O  O   . PHE B 2  899  ? -44.514 -38.382  35.557  1.00 45.82  ?  899  PHE B O   1 
ATOM   8135  C  CB  . PHE B 2  899  ? -43.394 -36.280  37.631  1.00 42.94  ?  899  PHE B CB  1 
ATOM   8136  C  CG  . PHE B 2  899  ? -44.242 -36.369  38.866  1.00 46.14  ?  899  PHE B CG  1 
ATOM   8137  C  CD1 . PHE B 2  899  ? -43.663 -36.607  40.101  1.00 51.45  ?  899  PHE B CD1 1 
ATOM   8138  C  CD2 . PHE B 2  899  ? -45.616 -36.208  38.795  1.00 47.31  ?  899  PHE B CD2 1 
ATOM   8139  C  CE1 . PHE B 2  899  ? -44.438 -36.689  41.241  1.00 56.27  ?  899  PHE B CE1 1 
ATOM   8140  C  CE2 . PHE B 2  899  ? -46.397 -36.287  39.933  1.00 53.41  ?  899  PHE B CE2 1 
ATOM   8141  C  CZ  . PHE B 2  899  ? -45.807 -36.528  41.157  1.00 59.40  ?  899  PHE B CZ  1 
ATOM   8142  N  N   . ASN B 2  900  ? -44.514 -39.354  37.602  1.00 50.63  ?  900  ASN B N   1 
ATOM   8143  C  CA  . ASN B 2  900  ? -45.688 -40.190  37.355  1.00 51.70  ?  900  ASN B CA  1 
ATOM   8144  C  C   . ASN B 2  900  ? -46.933 -39.387  37.724  1.00 54.23  ?  900  ASN B C   1 
ATOM   8145  O  O   . ASN B 2  900  ? -47.510 -39.523  38.805  1.00 55.23  ?  900  ASN B O   1 
ATOM   8146  C  CB  . ASN B 2  900  ? -45.597 -41.493  38.140  1.00 42.54  ?  900  ASN B CB  1 
ATOM   8147  C  CG  . ASN B 2  900  ? -44.544 -42.437  37.587  1.00 50.12  ?  900  ASN B CG  1 
ATOM   8148  O  OD1 . ASN B 2  900  ? -44.858 -43.379  36.859  1.00 58.64  ?  900  ASN B OD1 1 
ATOM   8149  N  ND2 . ASN B 2  900  ? -43.286 -42.188  37.931  1.00 48.17  ?  900  ASN B ND2 1 
ATOM   8150  N  N   . PHE B 2  901  ? -47.343 -38.521  36.791  1.00 48.18  ?  901  PHE B N   1 
ATOM   8151  C  CA  . PHE B 2  901  ? -48.524 -37.691  37.007  1.00 42.52  ?  901  PHE B CA  1 
ATOM   8152  C  C   . PHE B 2  901  ? -49.773 -38.536  37.216  1.00 46.81  ?  901  PHE B C   1 
ATOM   8153  O  O   . PHE B 2  901  ? -50.659 -38.156  37.991  1.00 51.60  ?  901  PHE B O   1 
ATOM   8154  C  CB  . PHE B 2  901  ? -48.714 -36.743  35.824  1.00 47.50  ?  901  PHE B CB  1 
ATOM   8155  C  CG  . PHE B 2  901  ? -47.604 -35.746  35.668  1.00 47.31  ?  901  PHE B CG  1 
ATOM   8156  C  CD1 . PHE B 2  901  ? -47.599 -34.573  36.403  1.00 51.44  ?  901  PHE B CD1 1 
ATOM   8157  C  CD2 . PHE B 2  901  ? -46.557 -35.990  34.796  1.00 47.53  ?  901  PHE B CD2 1 
ATOM   8158  C  CE1 . PHE B 2  901  ? -46.574 -33.656  36.262  1.00 52.94  ?  901  PHE B CE1 1 
ATOM   8159  C  CE2 . PHE B 2  901  ? -45.531 -35.078  34.652  1.00 44.53  ?  901  PHE B CE2 1 
ATOM   8160  C  CZ  . PHE B 2  901  ? -45.539 -33.911  35.385  1.00 46.71  ?  901  PHE B CZ  1 
ATOM   8161  N  N   . LEU B 2  902  ? -49.861 -39.677  36.536  1.00 47.81  ?  902  LEU B N   1 
ATOM   8162  C  CA  . LEU B 2  902  ? -50.946 -40.628  36.741  1.00 47.06  ?  902  LEU B CA  1 
ATOM   8163  C  C   . LEU B 2  902  ? -50.366 -42.012  36.992  1.00 40.51  ?  902  LEU B C   1 
ATOM   8164  O  O   . LEU B 2  902  ? -49.155 -42.152  37.196  1.00 43.53  ?  902  LEU B O   1 
ATOM   8165  C  CB  . LEU B 2  902  ? -51.885 -40.645  35.534  1.00 48.53  ?  902  LEU B CB  1 
ATOM   8166  C  CG  . LEU B 2  902  ? -52.586 -39.322  35.224  1.00 48.91  ?  902  LEU B CG  1 
ATOM   8167  C  CD1 . LEU B 2  902  ? -53.229 -39.353  33.847  1.00 56.34  ?  902  LEU B CD1 1 
ATOM   8168  C  CD2 . LEU B 2  902  ? -53.618 -39.024  36.297  1.00 59.42  ?  902  LEU B CD2 1 
ATOM   8169  N  N   . GLN B 2  903  ? -51.212 -43.038  36.983  1.00 43.39  ?  903  GLN B N   1 
ATOM   8170  C  CA  . GLN B 2  903  ? -50.740 -44.414  37.122  1.00 45.85  ?  903  GLN B CA  1 
ATOM   8171  C  C   . GLN B 2  903  ? -50.328 -44.916  35.744  1.00 53.55  ?  903  GLN B C   1 
ATOM   8172  O  O   . GLN B 2  903  ? -51.172 -45.262  34.915  1.00 53.37  ?  903  GLN B O   1 
ATOM   8173  C  CB  . GLN B 2  903  ? -51.814 -45.298  37.744  1.00 38.95  ?  903  GLN B CB  1 
ATOM   8174  C  CG  . GLN B 2  903  ? -51.413 -46.760  37.853  1.00 37.44  ?  903  GLN B CG  1 
ATOM   8175  C  CD  . GLN B 2  903  ? -50.216 -46.974  38.761  1.00 52.36  ?  903  GLN B CD  1 
ATOM   8176  O  OE1 . GLN B 2  903  ? -49.980 -46.205  39.694  1.00 55.05  ?  903  GLN B OE1 1 
ATOM   8177  N  NE2 . GLN B 2  903  ? -49.446 -48.020  38.484  1.00 59.79  ?  903  GLN B NE2 1 
ATOM   8178  N  N   . TYR B 2  904  ? -49.019 -44.954  35.496  1.00 54.22  ?  904  TYR B N   1 
ATOM   8179  C  CA  . TYR B 2  904  ? -48.491 -45.323  34.190  1.00 49.87  ?  904  TYR B CA  1 
ATOM   8180  C  C   . TYR B 2  904  ? -48.059 -46.778  34.100  1.00 57.34  ?  904  TYR B C   1 
ATOM   8181  O  O   . TYR B 2  904  ? -48.150 -47.372  33.020  1.00 60.00  ?  904  TYR B O   1 
ATOM   8182  C  CB  . TYR B 2  904  ? -47.300 -44.430  33.828  1.00 45.27  ?  904  TYR B CB  1 
ATOM   8183  C  CG  . TYR B 2  904  ? -47.668 -42.985  33.590  1.00 53.70  ?  904  TYR B CG  1 
ATOM   8184  C  CD1 . TYR B 2  904  ? -48.869 -42.646  32.982  1.00 59.53  ?  904  TYR B CD1 1 
ATOM   8185  C  CD2 . TYR B 2  904  ? -46.805 -41.959  33.955  1.00 54.72  ?  904  TYR B CD2 1 
ATOM   8186  C  CE1 . TYR B 2  904  ? -49.208 -41.325  32.756  1.00 59.03  ?  904  TYR B CE1 1 
ATOM   8187  C  CE2 . TYR B 2  904  ? -47.135 -40.635  33.732  1.00 53.41  ?  904  TYR B CE2 1 
ATOM   8188  C  CZ  . TYR B 2  904  ? -48.337 -40.324  33.132  1.00 60.93  ?  904  TYR B CZ  1 
ATOM   8189  O  OH  . TYR B 2  904  ? -48.669 -39.007  32.908  1.00 65.93  ?  904  TYR B OH  1 
ATOM   8190  N  N   . SER B 2  905  ? -47.592 -47.365  35.197  1.00 60.26  ?  905  SER B N   1 
ATOM   8191  C  CA  . SER B 2  905  ? -47.116 -48.739  35.165  1.00 61.34  ?  905  SER B CA  1 
ATOM   8192  C  C   . SER B 2  905  ? -48.283 -49.712  35.040  1.00 66.48  ?  905  SER B C   1 
ATOM   8193  O  O   . SER B 2  905  ? -49.322 -49.550  35.687  1.00 66.86  ?  905  SER B O   1 
ATOM   8194  C  CB  . SER B 2  905  ? -46.305 -49.046  36.421  1.00 63.78  ?  905  SER B CB  1 
ATOM   8195  O  OG  . SER B 2  905  ? -45.195 -48.172  36.532  1.00 64.71  ?  905  SER B OG  1 
ATOM   8196  N  N   . ASP B 2  906  ? -48.103 -50.728  34.201  1.00 82.91  ?  906  ASP B N   1 
ATOM   8197  C  CA  . ASP B 2  906  ? -49.153 -51.711  33.976  1.00 83.02  ?  906  ASP B CA  1 
ATOM   8198  C  C   . ASP B 2  906  ? -49.291 -52.630  35.184  1.00 87.88  ?  906  ASP B C   1 
ATOM   8199  O  O   . ASP B 2  906  ? -48.300 -52.998  35.821  1.00 88.33  ?  906  ASP B O   1 
ATOM   8200  C  CB  . ASP B 2  906  ? -48.852 -52.525  32.718  1.00 87.54  ?  906  ASP B CB  1 
ATOM   8201  C  CG  . ASP B 2  906  ? -49.821 -53.672  32.518  1.00 100.74 ?  906  ASP B CG  1 
ATOM   8202  O  OD1 . ASP B 2  906  ? -50.922 -53.433  31.981  1.00 100.60 ?  906  ASP B OD1 1 
ATOM   8203  O  OD2 . ASP B 2  906  ? -49.480 -54.813  32.898  1.00 110.33 -1 906  ASP B OD2 1 
ATOM   8204  N  N   . THR B 2  907  ? -50.533 -52.997  35.501  1.00 77.12  ?  907  THR B N   1 
ATOM   8205  C  CA  . THR B 2  907  ? -50.811 -53.810  36.679  1.00 83.61  ?  907  THR B CA  1 
ATOM   8206  C  C   . THR B 2  907  ? -51.630 -55.049  36.334  1.00 93.63  ?  907  THR B C   1 
ATOM   8207  O  O   . THR B 2  907  ? -51.478 -56.096  36.972  1.00 90.73  ?  907  THR B O   1 
ATOM   8208  C  CB  . THR B 2  907  ? -51.546 -52.984  37.739  1.00 83.47  ?  907  THR B CB  1 
ATOM   8209  O  OG1 . THR B 2  907  ? -52.795 -52.524  37.207  1.00 86.83  ?  907  THR B OG1 1 
ATOM   8210  C  CG2 . THR B 2  907  ? -50.709 -51.786  38.167  1.00 80.76  ?  907  THR B CG2 1 
ATOM   8211  N  N   . THR B 2  908  ? -52.499 -54.944  35.329  1.00 97.43  ?  908  THR B N   1 
ATOM   8212  C  CA  . THR B 2  908  ? -53.435 -56.018  35.016  1.00 95.17  ?  908  THR B CA  1 
ATOM   8213  C  C   . THR B 2  908  ? -52.840 -57.074  34.092  1.00 96.76  ?  908  THR B C   1 
ATOM   8214  O  O   . THR B 2  908  ? -53.035 -58.274  34.318  1.00 93.78  ?  908  THR B O   1 
ATOM   8215  C  CB  . THR B 2  908  ? -54.706 -55.439  34.387  1.00 100.02 ?  908  THR B CB  1 
ATOM   8216  O  OG1 . THR B 2  908  ? -54.411 -54.951  33.072  1.00 99.26  ?  908  THR B OG1 1 
ATOM   8217  C  CG2 . THR B 2  908  ? -55.249 -54.301  35.235  1.00 107.72 ?  908  THR B CG2 1 
ATOM   8218  N  N   . THR B 2  909  ? -52.124 -56.657  33.051  1.00 95.60  ?  909  THR B N   1 
ATOM   8219  C  CA  . THR B 2  909  ? -51.572 -57.600  32.085  1.00 88.11  ?  909  THR B CA  1 
ATOM   8220  C  C   . THR B 2  909  ? -50.503 -58.465  32.741  1.00 86.26  ?  909  THR B C   1 
ATOM   8221  O  O   . THR B 2  909  ? -49.529 -57.948  33.297  1.00 94.15  ?  909  THR B O   1 
ATOM   8222  C  CB  . THR B 2  909  ? -50.991 -56.853  30.887  1.00 87.94  ?  909  THR B CB  1 
ATOM   8223  O  OG1 . THR B 2  909  ? -51.903 -55.829  30.469  1.00 88.18  ?  909  THR B OG1 1 
ATOM   8224  C  CG2 . THR B 2  909  ? -50.748 -57.809  29.729  1.00 92.76  ?  909  THR B CG2 1 
ATOM   8225  N  N   . GLU B 2  910  ? -50.678 -59.786  32.662  1.00 69.28  ?  910  GLU B N   1 
ATOM   8226  C  CA  . GLU B 2  910  ? -49.748 -60.693  33.327  1.00 79.69  ?  910  GLU B CA  1 
ATOM   8227  C  C   . GLU B 2  910  ? -48.417 -60.770  32.590  1.00 73.16  ?  910  GLU B C   1 
ATOM   8228  O  O   . GLU B 2  910  ? -47.358 -60.855  33.222  1.00 81.08  ?  910  GLU B O   1 
ATOM   8229  C  CB  . GLU B 2  910  ? -50.372 -62.083  33.456  1.00 84.14  ?  910  GLU B CB  1 
ATOM   8230  C  CG  . GLU B 2  910  ? -51.586 -62.136  34.370  1.00 91.73  ?  910  GLU B CG  1 
ATOM   8231  C  CD  . GLU B 2  910  ? -51.236 -61.849  35.820  1.00 85.18  ?  910  GLU B CD  1 
ATOM   8232  O  OE1 . GLU B 2  910  ? -50.178 -62.323  36.286  1.00 84.38  ?  910  GLU B OE1 1 
ATOM   8233  O  OE2 . GLU B 2  910  ? -52.019 -61.147  36.494  1.00 96.45  -1 910  GLU B OE2 1 
ATOM   8234  N  N   . THR B 2  911  ? -48.448 -60.745  31.257  1.00 85.33  ?  911  THR B N   1 
ATOM   8235  C  CA  . THR B 2  911  ? -47.213 -60.874  30.490  1.00 83.15  ?  911  THR B CA  1 
ATOM   8236  C  C   . THR B 2  911  ? -46.301 -59.671  30.698  1.00 84.58  ?  911  THR B C   1 
ATOM   8237  O  O   . THR B 2  911  ? -45.077 -59.821  30.782  1.00 81.96  ?  911  THR B O   1 
ATOM   8238  C  CB  . THR B 2  911  ? -47.532 -61.053  29.008  1.00 86.06  ?  911  THR B CB  1 
ATOM   8239  O  OG1 . THR B 2  911  ? -48.205 -59.887  28.519  1.00 89.82  ?  911  THR B OG1 1 
ATOM   8240  C  CG2 . THR B 2  911  ? -48.420 -62.265  28.803  1.00 87.97  ?  911  THR B CG2 1 
ATOM   8241  N  N   . PHE B 2  912  ? -46.877 -58.468  30.779  1.00 59.89  ?  912  PHE B N   1 
ATOM   8242  C  CA  . PHE B 2  912  ? -46.070 -57.289  31.071  1.00 49.19  ?  912  PHE B CA  1 
ATOM   8243  C  C   . PHE B 2  912  ? -45.484 -57.350  32.474  1.00 61.19  ?  912  PHE B C   1 
ATOM   8244  O  O   . PHE B 2  912  ? -44.377 -56.850  32.704  1.00 55.72  ?  912  PHE B O   1 
ATOM   8245  C  CB  . PHE B 2  912  ? -46.905 -56.022  30.893  1.00 61.91  ?  912  PHE B CB  1 
ATOM   8246  C  CG  . PHE B 2  912  ? -47.156 -55.658  29.458  1.00 71.68  ?  912  PHE B CG  1 
ATOM   8247  C  CD1 . PHE B 2  912  ? -46.445 -56.273  28.440  1.00 74.77  ?  912  PHE B CD1 1 
ATOM   8248  C  CD2 . PHE B 2  912  ? -48.102 -54.704  29.125  1.00 59.09  ?  912  PHE B CD2 1 
ATOM   8249  C  CE1 . PHE B 2  912  ? -46.672 -55.942  27.117  1.00 68.24  ?  912  PHE B CE1 1 
ATOM   8250  C  CE2 . PHE B 2  912  ? -48.334 -54.369  27.804  1.00 60.07  ?  912  PHE B CE2 1 
ATOM   8251  C  CZ  . PHE B 2  912  ? -47.618 -54.989  26.799  1.00 63.55  ?  912  PHE B CZ  1 
ATOM   8252  N  N   . LYS B 2  913  ? -46.207 -57.958  33.420  1.00 73.11  ?  913  LYS B N   1 
ATOM   8253  C  CA  . LYS B 2  913  ? -45.660 -58.166  34.756  1.00 58.17  ?  913  LYS B CA  1 
ATOM   8254  C  C   . LYS B 2  913  ? -44.497 -59.149  34.735  1.00 60.94  ?  913  LYS B C   1 
ATOM   8255  O  O   . LYS B 2  913  ? -43.586 -59.049  35.565  1.00 63.45  ?  913  LYS B O   1 
ATOM   8256  C  CB  . LYS B 2  913  ? -46.754 -58.660  35.702  1.00 56.82  ?  913  LYS B CB  1 
ATOM   8257  C  CG  . LYS B 2  913  ? -47.785 -57.605  36.070  1.00 70.28  ?  913  LYS B CG  1 
ATOM   8258  C  CD  . LYS B 2  913  ? -49.018 -58.238  36.699  1.00 73.59  ?  913  LYS B CD  1 
ATOM   8259  C  CE  . LYS B 2  913  ? -48.670 -59.002  37.967  1.00 74.50  ?  913  LYS B CE  1 
ATOM   8260  N  NZ  . LYS B 2  913  ? -49.890 -59.436  38.702  1.00 69.43  ?  913  LYS B NZ  1 
ATOM   8261  N  N   . LEU B 2  914  ? -44.512 -60.101  33.799  1.00 51.59  ?  914  LEU B N   1 
ATOM   8262  C  CA  . LEU B 2  914  ? -43.408 -61.039  33.648  1.00 48.39  ?  914  LEU B CA  1 
ATOM   8263  C  C   . LEU B 2  914  ? -42.184 -60.404  33.002  1.00 48.32  ?  914  LEU B C   1 
ATOM   8264  O  O   . LEU B 2  914  ? -41.083 -60.950  33.124  1.00 49.96  ?  914  LEU B O   1 
ATOM   8265  C  CB  . LEU B 2  914  ? -43.849 -62.245  32.815  1.00 46.94  ?  914  LEU B CB  1 
ATOM   8266  C  CG  . LEU B 2  914  ? -44.723 -63.286  33.517  1.00 51.79  ?  914  LEU B CG  1 
ATOM   8267  C  CD1 . LEU B 2  914  ? -45.264 -64.297  32.519  1.00 51.94  ?  914  LEU B CD1 1 
ATOM   8268  C  CD2 . LEU B 2  914  ? -43.960 -63.982  34.635  1.00 63.28  ?  914  LEU B CD2 1 
ATOM   8269  N  N   . ALA B 2  915  ? -42.351 -59.274  32.315  1.00 52.01  ?  915  ALA B N   1 
ATOM   8270  C  CA  . ALA B 2  915  ? -41.227 -58.629  31.651  1.00 43.31  ?  915  ALA B CA  1 
ATOM   8271  C  C   . ALA B 2  915  ? -40.446 -57.703  32.572  1.00 44.50  ?  915  ALA B C   1 
ATOM   8272  O  O   . ALA B 2  915  ? -39.320 -57.322  32.233  1.00 39.99  ?  915  ALA B O   1 
ATOM   8273  C  CB  . ALA B 2  915  ? -41.713 -57.845  30.429  1.00 37.54  ?  915  ALA B CB  1 
ATOM   8274  N  N   . PHE B 2  916  ? -41.013 -57.340  33.722  1.00 66.72  ?  916  PHE B N   1 
ATOM   8275  C  CA  . PHE B 2  916  ? -40.354 -56.410  34.628  1.00 61.44  ?  916  PHE B CA  1 
ATOM   8276  C  C   . PHE B 2  916  ? -39.055 -56.998  35.165  1.00 60.18  ?  916  PHE B C   1 
ATOM   8277  O  O   . PHE B 2  916  ? -38.951 -58.202  35.415  1.00 66.17  ?  916  PHE B O   1 
ATOM   8278  C  CB  . PHE B 2  916  ? -41.285 -56.057  35.789  1.00 61.87  ?  916  PHE B CB  1 
ATOM   8279  C  CG  . PHE B 2  916  ? -42.318 -55.023  35.450  1.00 54.87  ?  916  PHE B CG  1 
ATOM   8280  C  CD1 . PHE B 2  916  ? -41.953 -53.827  34.855  1.00 48.18  ?  916  PHE B CD1 1 
ATOM   8281  C  CD2 . PHE B 2  916  ? -43.656 -55.242  35.734  1.00 56.85  ?  916  PHE B CD2 1 
ATOM   8282  C  CE1 . PHE B 2  916  ? -42.904 -52.870  34.546  1.00 48.20  ?  916  PHE B CE1 1 
ATOM   8283  C  CE2 . PHE B 2  916  ? -44.612 -54.290  35.427  1.00 55.35  ?  916  PHE B CE2 1 
ATOM   8284  C  CZ  . PHE B 2  916  ? -44.235 -53.103  34.832  1.00 47.09  ?  916  PHE B CZ  1 
ATOM   8285  N  N   . ASN B 2  917  ? -38.061 -56.135  35.335  1.00 62.44  ?  917  ASN B N   1 
ATOM   8286  C  CA  . ASN B 2  917  ? -36.787 -56.546  35.909  1.00 60.81  ?  917  ASN B CA  1 
ATOM   8287  C  C   . ASN B 2  917  ? -36.899 -56.562  37.428  1.00 60.92  ?  917  ASN B C   1 
ATOM   8288  O  O   . ASN B 2  917  ? -37.143 -55.511  38.030  1.00 67.11  ?  917  ASN B O   1 
ATOM   8289  C  CB  . ASN B 2  917  ? -35.674 -55.604  35.466  1.00 59.55  ?  917  ASN B CB  1 
ATOM   8290  C  CG  . ASN B 2  917  ? -34.350 -55.905  36.141  1.00 58.39  ?  917  ASN B CG  1 
ATOM   8291  O  OD1 . ASN B 2  917  ? -34.025 -57.061  36.409  1.00 68.10  ?  917  ASN B OD1 1 
ATOM   8292  N  ND2 . ASN B 2  917  ? -33.575 -54.862  36.415  1.00 58.13  ?  917  ASN B ND2 1 
ATOM   8293  N  N   . PRO B 2  918  ? -36.730 -57.716  38.082  1.00 46.55  ?  918  PRO B N   1 
ATOM   8294  C  CA  . PRO B 2  918  ? -36.999 -57.793  39.528  1.00 50.27  ?  918  PRO B CA  1 
ATOM   8295  C  C   . PRO B 2  918  ? -36.030 -57.002  40.395  1.00 55.93  ?  918  PRO B C   1 
ATOM   8296  O  O   . PRO B 2  918  ? -36.303 -56.842  41.593  1.00 51.60  ?  918  PRO B O   1 
ATOM   8297  C  CB  . PRO B 2  918  ? -36.901 -59.296  39.822  1.00 52.15  ?  918  PRO B CB  1 
ATOM   8298  C  CG  . PRO B 2  918  ? -36.048 -59.846  38.728  1.00 44.53  ?  918  PRO B CG  1 
ATOM   8299  C  CD  . PRO B 2  918  ? -36.335 -59.016  37.515  1.00 43.30  ?  918  PRO B CD  1 
ATOM   8300  N  N   . ASP B 2  919  ? -34.920 -56.505  39.849  1.00 71.75  ?  919  ASP B N   1 
ATOM   8301  C  CA  . ASP B 2  919  ? -33.955 -55.738  40.629  1.00 68.98  ?  919  ASP B CA  1 
ATOM   8302  C  C   . ASP B 2  919  ? -34.275 -54.249  40.687  1.00 72.18  ?  919  ASP B C   1 
ATOM   8303  O  O   . ASP B 2  919  ? -33.542 -53.501  41.341  1.00 76.04  ?  919  ASP B O   1 
ATOM   8304  C  CB  . ASP B 2  919  ? -32.543 -55.931  40.068  1.00 64.56  ?  919  ASP B CB  1 
ATOM   8305  C  CG  . ASP B 2  919  ? -31.854 -57.155  40.636  1.00 84.42  ?  919  ASP B CG  1 
ATOM   8306  O  OD1 . ASP B 2  919  ? -32.042 -57.441  41.837  1.00 87.33  ?  919  ASP B OD1 1 
ATOM   8307  O  OD2 . ASP B 2  919  ? -31.126 -57.833  39.881  1.00 103.17 -1 919  ASP B OD2 1 
ATOM   8308  N  N   . VAL B 2  920  ? -35.342 -53.802  40.027  1.00 62.85  ?  920  VAL B N   1 
ATOM   8309  C  CA  . VAL B 2  920  ? -35.732 -52.396  40.009  1.00 65.10  ?  920  VAL B CA  1 
ATOM   8310  C  C   . VAL B 2  920  ? -37.196 -52.297  40.411  1.00 64.72  ?  920  VAL B C   1 
ATOM   8311  O  O   . VAL B 2  920  ? -38.042 -53.017  39.869  1.00 60.16  ?  920  VAL B O   1 
ATOM   8312  C  CB  . VAL B 2  920  ? -35.506 -51.758  38.624  1.00 62.90  ?  920  VAL B CB  1 
ATOM   8313  C  CG1 . VAL B 2  920  ? -36.029 -50.331  38.604  1.00 65.43  ?  920  VAL B CG1 1 
ATOM   8314  C  CG2 . VAL B 2  920  ? -34.032 -51.792  38.261  1.00 53.98  ?  920  VAL B CG2 1 
ATOM   8315  N  N   . THR B 2  921  ? -37.492 -51.417  41.365  1.00 58.60  ?  921  THR B N   1 
ATOM   8316  C  CA  . THR B 2  921  ? -38.872 -51.216  41.782  1.00 57.62  ?  921  THR B CA  1 
ATOM   8317  C  C   . THR B 2  921  ? -39.672 -50.570  40.660  1.00 54.03  ?  921  THR B C   1 
ATOM   8318  O  O   . THR B 2  921  ? -39.167 -49.720  39.921  1.00 46.02  ?  921  THR B O   1 
ATOM   8319  C  CB  . THR B 2  921  ? -38.946 -50.343  43.036  1.00 60.25  ?  921  THR B CB  1 
ATOM   8320  O  OG1 . THR B 2  921  ? -38.873 -48.962  42.665  1.00 70.36  ?  921  THR B OG1 1 
ATOM   8321  C  CG2 . THR B 2  921  ? -37.811 -50.665  43.989  1.00 53.64  ?  921  THR B CG2 1 
ATOM   8322  N  N   . VAL B 2  922  ? -40.926 -50.982  40.531  1.00 62.38  ?  922  VAL B N   1 
ATOM   8323  C  CA  . VAL B 2  922  ? -41.831 -50.415  39.540  1.00 57.76  ?  922  VAL B CA  1 
ATOM   8324  C  C   . VAL B 2  922  ? -42.563 -49.247  40.187  1.00 60.63  ?  922  VAL B C   1 
ATOM   8325  O  O   . VAL B 2  922  ? -43.263 -49.423  41.189  1.00 68.17  ?  922  VAL B O   1 
ATOM   8326  C  CB  . VAL B 2  922  ? -42.815 -51.470  39.017  1.00 52.71  ?  922  VAL B CB  1 
ATOM   8327  C  CG1 . VAL B 2  922  ? -43.665 -50.885  37.910  1.00 58.78  ?  922  VAL B CG1 1 
ATOM   8328  C  CG2 . VAL B 2  922  ? -42.060 -52.699  38.530  1.00 60.93  ?  922  VAL B CG2 1 
ATOM   8329  N  N   . ARG B 2  923  ? -42.405 -48.058  39.613  1.00 60.79  ?  923  ARG B N   1 
ATOM   8330  C  CA  . ARG B 2  923  ? -42.887 -46.842  40.252  1.00 66.64  ?  923  ARG B CA  1 
ATOM   8331  C  C   . ARG B 2  923  ? -44.408 -46.742  40.187  1.00 70.25  ?  923  ARG B C   1 
ATOM   8332  O  O   . ARG B 2  923  ? -45.045 -47.164  39.217  1.00 76.74  ?  923  ARG B O   1 
ATOM   8333  C  CB  . ARG B 2  923  ? -42.252 -45.613  39.599  1.00 66.41  ?  923  ARG B CB  1 
ATOM   8334  C  CG  . ARG B 2  923  ? -40.870 -45.264  40.139  1.00 61.30  ?  923  ARG B CG  1 
ATOM   8335  C  CD  . ARG B 2  923  ? -39.795 -46.168  39.557  1.00 60.92  ?  923  ARG B CD  1 
ATOM   8336  N  NE  . ARG B 2  923  ? -39.723 -46.059  38.106  1.00 66.77  ?  923  ARG B NE  1 
ATOM   8337  C  CZ  . ARG B 2  923  ? -39.019 -46.868  37.326  1.00 57.07  ?  923  ARG B CZ  1 
ATOM   8338  N  NH1 . ARG B 2  923  ? -38.317 -47.871  37.827  1.00 61.67  ?  923  ARG B NH1 1 
ATOM   8339  N  NH2 . ARG B 2  923  ? -39.021 -46.666  36.012  1.00 53.94  ?  923  ARG B NH2 1 
ATOM   8340  N  N   . ILE B 2  924  ? -44.987 -46.169  41.242  1.00 46.06  ?  924  ILE B N   1 
ATOM   8341  C  CA  . ILE B 2  924  ? -46.427 -45.959  41.337  1.00 46.15  ?  924  ILE B CA  1 
ATOM   8342  C  C   . ILE B 2  924  ? -46.720 -44.494  41.035  1.00 54.53  ?  924  ILE B C   1 
ATOM   8343  O  O   . ILE B 2  924  ? -45.800 -43.708  40.782  1.00 53.29  ?  924  ILE B O   1 
ATOM   8344  C  CB  . ILE B 2  924  ? -46.954 -46.374  42.726  1.00 49.33  ?  924  ILE B CB  1 
ATOM   8345  C  CG1 . ILE B 2  924  ? -48.440 -46.746  42.663  1.00 51.71  ?  924  ILE B CG1 1 
ATOM   8346  C  CG2 . ILE B 2  924  ? -46.700 -45.276  43.753  1.00 51.07  ?  924  ILE B CG2 1 
ATOM   8347  C  CD1 . ILE B 2  924  ? -48.976 -47.353  43.942  1.00 55.30  ?  924  ILE B CD1 1 
ATOM   8348  N  N   . ARG B 2  925  ? -47.997 -44.119  41.044  1.00 73.99  ?  925  ARG B N   1 
ATOM   8349  C  CA  . ARG B 2  925  ? -48.381 -42.740  40.773  1.00 67.34  ?  925  ARG B CA  1 
ATOM   8350  C  C   . ARG B 2  925  ? -47.877 -41.814  41.874  1.00 68.21  ?  925  ARG B C   1 
ATOM   8351  O  O   . ARG B 2  925  ? -48.002 -42.121  43.063  1.00 71.35  ?  925  ARG B O   1 
ATOM   8352  C  CB  . ARG B 2  925  ? -49.901 -42.630  40.651  1.00 68.05  ?  925  ARG B CB  1 
ATOM   8353  C  CG  . ARG B 2  925  ? -50.451 -41.241  40.949  1.00 72.89  ?  925  ARG B CG  1 
ATOM   8354  C  CD  . ARG B 2  925  ? -51.875 -41.079  40.444  1.00 78.19  ?  925  ARG B CD  1 
ATOM   8355  N  NE  . ARG B 2  925  ? -52.812 -41.938  41.158  1.00 91.47  ?  925  ARG B NE  1 
ATOM   8356  C  CZ  . ARG B 2  925  ? -53.479 -41.577  42.247  1.00 95.18  ?  925  ARG B CZ  1 
ATOM   8357  N  NH1 . ARG B 2  925  ? -53.327 -40.378  42.784  1.00 78.69  ?  925  ARG B NH1 1 
ATOM   8358  N  NH2 . ARG B 2  925  ? -54.317 -42.442  42.811  1.00 101.14 ?  925  ARG B NH2 1 
ATOM   8359  N  N   . GLY B 2  926  ? -47.300 -40.684  41.475  1.00 69.75  ?  926  GLY B N   1 
ATOM   8360  C  CA  . GLY B 2  926  ? -46.934 -39.638  42.407  1.00 76.76  ?  926  GLY B CA  1 
ATOM   8361  C  C   . GLY B 2  926  ? -45.477 -39.566  42.801  1.00 76.58  ?  926  GLY B C   1 
ATOM   8362  O  O   . GLY B 2  926  ? -45.152 -38.858  43.761  1.00 81.47  ?  926  GLY B O   1 
ATOM   8363  N  N   . VAL B 2  927  ? -44.588 -40.264  42.097  1.00 55.46  ?  927  VAL B N   1 
ATOM   8364  C  CA  . VAL B 2  927  ? -43.169 -40.274  42.424  1.00 51.05  ?  927  VAL B CA  1 
ATOM   8365  C  C   . VAL B 2  927  ? -42.370 -39.817  41.205  1.00 51.35  ?  927  VAL B C   1 
ATOM   8366  O  O   . VAL B 2  927  ? -42.891 -39.701  40.096  1.00 49.18  ?  927  VAL B O   1 
ATOM   8367  C  CB  . VAL B 2  927  ? -42.690 -41.656  42.909  1.00 36.62  ?  927  VAL B CB  1 
ATOM   8368  C  CG1 . VAL B 2  927  ? -43.477 -42.090  44.136  1.00 46.36  ?  927  VAL B CG1 1 
ATOM   8369  C  CG2 . VAL B 2  927  ? -42.825 -42.681  41.799  1.00 45.37  ?  927  VAL B CG2 1 
ATOM   8370  N  N   . MET B 2  928  ? -41.085 -39.561  41.435  1.00 55.10  ?  928  MET B N   1 
ATOM   8371  C  CA  . MET B 2  928  ? -40.173 -39.056  40.421  1.00 46.27  ?  928  MET B CA  1 
ATOM   8372  C  C   . MET B 2  928  ? -39.172 -40.131  40.014  1.00 51.75  ?  928  MET B C   1 
ATOM   8373  O  O   . MET B 2  928  ? -38.854 -41.037  40.791  1.00 57.09  ?  928  MET B O   1 
ATOM   8374  C  CB  . MET B 2  928  ? -39.432 -37.815  40.929  1.00 45.64  ?  928  MET B CB  1 
ATOM   8375  C  CG  . MET B 2  928  ? -38.901 -36.906  39.834  1.00 51.53  ?  928  MET B CG  1 
ATOM   8376  S  SD  . MET B 2  928  ? -40.217 -36.023  38.979  1.00 51.95  ?  928  MET B SD  1 
ATOM   8377  C  CE  . MET B 2  928  ? -40.110 -34.400  39.719  1.00 53.57  ?  928  MET B CE  1 
ATOM   8378  N  N   . GLU B 2  929  ? -38.685 -40.026  38.779  1.00 58.67  ?  929  GLU B N   1 
ATOM   8379  C  CA  . GLU B 2  929  ? -37.691 -40.944  38.245  1.00 55.80  ?  929  GLU B CA  1 
ATOM   8380  C  C   . GLU B 2  929  ? -36.599 -40.151  37.543  1.00 51.41  ?  929  GLU B C   1 
ATOM   8381  O  O   . GLU B 2  929  ? -36.814 -39.022  37.096  1.00 54.41  ?  929  GLU B O   1 
ATOM   8382  C  CB  . GLU B 2  929  ? -38.306 -41.948  37.259  1.00 53.17  ?  929  GLU B CB  1 
ATOM   8383  C  CG  . GLU B 2  929  ? -39.648 -42.515  37.677  1.00 52.62  ?  929  GLU B CG  1 
ATOM   8384  C  CD  . GLU B 2  929  ? -40.274 -43.365  36.591  1.00 48.01  ?  929  GLU B CD  1 
ATOM   8385  O  OE1 . GLU B 2  929  ? -39.590 -43.632  35.581  1.00 40.94  ?  929  GLU B OE1 1 
ATOM   8386  O  OE2 . GLU B 2  929  ? -41.456 -43.746  36.735  1.00 53.94  -1 929  GLU B OE2 1 
ATOM   8387  N  N   . LYS B 2  930  ? -35.424 -40.767  37.444  1.00 55.70  ?  930  LYS B N   1 
ATOM   8388  C  CA  . LYS B 2  930  ? -34.291 -40.188  36.731  1.00 58.55  ?  930  LYS B CA  1 
ATOM   8389  C  C   . LYS B 2  930  ? -33.208 -41.256  36.619  1.00 55.07  ?  930  LYS B C   1 
ATOM   8390  O  O   . LYS B 2  930  ? -33.310 -42.335  37.210  1.00 51.17  ?  930  LYS B O   1 
ATOM   8391  C  CB  . LYS B 2  930  ? -33.777 -38.917  37.421  1.00 59.65  ?  930  LYS B CB  1 
ATOM   8392  C  CG  . LYS B 2  930  ? -33.252 -39.114  38.833  1.00 56.14  ?  930  LYS B CG  1 
ATOM   8393  C  CD  . LYS B 2  930  ? -31.749 -39.287  38.832  1.00 53.74  ?  930  LYS B CD  1 
ATOM   8394  C  CE  . LYS B 2  930  ? -31.190 -39.416  40.232  1.00 59.46  ?  930  LYS B CE  1 
ATOM   8395  N  NZ  . LYS B 2  930  ? -29.729 -39.682  40.180  1.00 61.24  ?  930  LYS B NZ  1 
ATOM   8396  N  N   . CYS B 2  931  ? -32.166 -40.938  35.852  1.00 36.61  ?  931  CYS B N   1 
ATOM   8397  C  CA  . CYS B 2  931  ? -31.090 -41.886  35.587  1.00 31.74  ?  931  CYS B CA  1 
ATOM   8398  C  C   . CYS B 2  931  ? -30.285 -42.175  36.850  1.00 31.20  ?  931  CYS B C   1 
ATOM   8399  O  O   . CYS B 2  931  ? -29.814 -41.255  37.526  1.00 34.62  ?  931  CYS B O   1 
ATOM   8400  C  CB  . CYS B 2  931  ? -30.172 -41.343  34.494  1.00 41.02  ?  931  CYS B CB  1 
ATOM   8401  S  SG  . CYS B 2  931  ? -28.561 -42.148  34.402  1.00 35.18  ?  931  CYS B SG  1 
ATOM   8402  N  N   . THR B 2  932  ? -30.099 -43.463  37.149  1.00 37.96  ?  932  THR B N   1 
ATOM   8403  C  CA  . THR B 2  932  ? -29.464 -43.906  38.385  1.00 36.32  ?  932  THR B CA  1 
ATOM   8404  C  C   . THR B 2  932  ? -28.130 -44.608  38.145  1.00 33.75  ?  932  THR B C   1 
ATOM   8405  O  O   . THR B 2  932  ? -27.667 -45.354  39.014  1.00 31.01  ?  932  THR B O   1 
ATOM   8406  C  CB  . THR B 2  932  ? -30.406 -44.833  39.155  1.00 34.17  ?  932  THR B CB  1 
ATOM   8407  O  OG1 . THR B 2  932  ? -30.709 -45.982  38.354  1.00 30.43  ?  932  THR B OG1 1 
ATOM   8408  C  CG2 . THR B 2  932  ? -31.700 -44.113  39.498  1.00 36.54  ?  932  THR B CG2 1 
ATOM   8409  N  N   . TYR B 2  933  ? -27.502 -44.384  36.987  1.00 56.24  ?  933  TYR B N   1 
ATOM   8410  C  CA  . TYR B 2  933  ? -26.283 -45.100  36.598  1.00 65.27  ?  933  TYR B CA  1 
ATOM   8411  C  C   . TYR B 2  933  ? -26.450 -46.613  36.705  1.00 60.60  ?  933  TYR B C   1 
ATOM   8412  O  O   . TYR B 2  933  ? -25.478 -47.342  36.927  1.00 56.80  ?  933  TYR B O   1 
ATOM   8413  C  CB  . TYR B 2  933  ? -25.068 -44.650  37.416  1.00 56.90  ?  933  TYR B CB  1 
ATOM   8414  C  CG  . TYR B 2  933  ? -24.394 -43.392  36.920  1.00 60.74  ?  933  TYR B CG  1 
ATOM   8415  C  CD1 . TYR B 2  933  ? -24.743 -42.826  35.703  1.00 63.80  ?  933  TYR B CD1 1 
ATOM   8416  C  CD2 . TYR B 2  933  ? -23.368 -42.801  37.647  1.00 62.85  ?  933  TYR B CD2 1 
ATOM   8417  C  CE1 . TYR B 2  933  ? -24.116 -41.685  35.242  1.00 70.01  ?  933  TYR B CE1 1 
ATOM   8418  C  CE2 . TYR B 2  933  ? -22.731 -41.662  37.192  1.00 64.70  ?  933  TYR B CE2 1 
ATOM   8419  C  CZ  . TYR B 2  933  ? -23.108 -41.110  35.987  1.00 67.05  ?  933  TYR B CZ  1 
ATOM   8420  O  OH  . TYR B 2  933  ? -22.483 -39.976  35.524  1.00 65.89  ?  933  TYR B OH  1 
ATOM   8421  N  N   . CYS B 2  934  ? -27.681 -47.094  36.536  1.00 57.54  ?  934  CYS B N   1 
ATOM   8422  C  CA  . CYS B 2  934  ? -28.013 -48.507  36.699  1.00 58.97  ?  934  CYS B CA  1 
ATOM   8423  C  C   . CYS B 2  934  ? -27.491 -49.024  38.038  1.00 59.47  ?  934  CYS B C   1 
ATOM   8424  O  O   . CYS B 2  934  ? -26.610 -49.884  38.112  1.00 57.93  ?  934  CYS B O   1 
ATOM   8425  C  CB  . CYS B 2  934  ? -27.470 -49.335  35.531  1.00 59.72  ?  934  CYS B CB  1 
ATOM   8426  S  SG  . CYS B 2  934  ? -28.277 -48.991  33.954  1.00 45.22  ?  934  CYS B SG  1 
ATOM   8427  N  N   . VAL B 2  935  ? -28.054 -48.464  39.112  1.00 40.23  ?  935  VAL B N   1 
ATOM   8428  C  CA  . VAL B 2  935  ? -27.534 -48.715  40.451  1.00 34.40  ?  935  VAL B CA  1 
ATOM   8429  C  C   . VAL B 2  935  ? -27.603 -50.189  40.826  1.00 26.38  ?  935  VAL B C   1 
ATOM   8430  O  O   . VAL B 2  935  ? -26.804 -50.653  41.647  1.00 26.58  ?  935  VAL B O   1 
ATOM   8431  C  CB  . VAL B 2  935  ? -28.281 -47.838  41.480  1.00 26.20  ?  935  VAL B CB  1 
ATOM   8432  C  CG1 . VAL B 2  935  ? -29.698 -48.348  41.704  1.00 26.36  ?  935  VAL B CG1 1 
ATOM   8433  C  CG2 . VAL B 2  935  ? -27.508 -47.781  42.788  1.00 26.14  ?  935  VAL B CG2 1 
ATOM   8434  N  N   . GLN B 2  936  ? -28.527 -50.947  40.230  1.00 34.36  ?  936  GLN B N   1 
ATOM   8435  C  CA  . GLN B 2  936  ? -28.622 -52.370  40.536  1.00 40.44  ?  936  GLN B CA  1 
ATOM   8436  C  C   . GLN B 2  936  ? -27.338 -53.098  40.158  1.00 51.44  ?  936  GLN B C   1 
ATOM   8437  O  O   . GLN B 2  936  ? -26.913 -54.029  40.855  1.00 50.31  ?  936  GLN B O   1 
ATOM   8438  C  CB  . GLN B 2  936  ? -29.824 -52.983  39.815  1.00 48.70  ?  936  GLN B CB  1 
ATOM   8439  C  CG  . GLN B 2  936  ? -29.828 -52.773  38.307  1.00 48.93  ?  936  GLN B CG  1 
ATOM   8440  C  CD  . GLN B 2  936  ? -30.525 -51.494  37.894  1.00 44.98  ?  936  GLN B CD  1 
ATOM   8441  O  OE1 . GLN B 2  936  ? -30.995 -50.729  38.737  1.00 46.07  ?  936  GLN B OE1 1 
ATOM   8442  N  NE2 . GLN B 2  936  ? -30.594 -51.253  36.591  1.00 39.50  ?  936  GLN B NE2 1 
ATOM   8443  N  N   . ARG B 2  937  ? -26.698 -52.677  39.064  1.00 47.45  ?  937  ARG B N   1 
ATOM   8444  C  CA  . ARG B 2  937  ? -25.436 -53.273  38.643  1.00 42.51  ?  937  ARG B CA  1 
ATOM   8445  C  C   . ARG B 2  937  ? -24.266 -52.782  39.485  1.00 45.65  ?  937  ARG B C   1 
ATOM   8446  O  O   . ARG B 2  937  ? -23.299 -53.526  39.690  1.00 52.31  ?  937  ARG B O   1 
ATOM   8447  C  CB  . ARG B 2  937  ? -25.181 -52.964  37.167  1.00 42.51  ?  937  ARG B CB  1 
ATOM   8448  C  CG  . ARG B 2  937  ? -26.382 -53.213  36.266  1.00 42.80  ?  937  ARG B CG  1 
ATOM   8449  C  CD  . ARG B 2  937  ? -25.985 -53.231  34.801  1.00 39.99  ?  937  ARG B CD  1 
ATOM   8450  N  NE  . ARG B 2  937  ? -27.051 -53.762  33.961  1.00 36.96  ?  937  ARG B NE  1 
ATOM   8451  C  CZ  . ARG B 2  937  ? -26.933 -54.001  32.662  1.00 38.72  ?  937  ARG B CZ  1 
ATOM   8452  N  NH1 . ARG B 2  937  ? -25.796 -53.788  32.020  1.00 35.63  ?  937  ARG B NH1 1 
ATOM   8453  N  NH2 . ARG B 2  937  ? -27.985 -54.461  31.990  1.00 40.72  ?  937  ARG B NH2 1 
ATOM   8454  N  N   . ILE B 2  938  ? -24.331 -51.541  39.968  1.00 56.98  ?  938  ILE B N   1 
ATOM   8455  C  CA  . ILE B 2  938  ? -23.290 -51.036  40.855  1.00 55.69  ?  938  ILE B CA  1 
ATOM   8456  C  C   . ILE B 2  938  ? -23.356 -51.743  42.203  1.00 57.39  ?  938  ILE B C   1 
ATOM   8457  O  O   . ILE B 2  938  ? -22.325 -52.111  42.778  1.00 58.49  ?  938  ILE B O   1 
ATOM   8458  C  CB  . ILE B 2  938  ? -23.416 -49.508  41.006  1.00 58.51  ?  938  ILE B CB  1 
ATOM   8459  C  CG1 . ILE B 2  938  ? -23.189 -48.820  39.659  1.00 63.06  ?  938  ILE B CG1 1 
ATOM   8460  C  CG2 . ILE B 2  938  ? -22.430 -48.984  42.041  1.00 63.49  ?  938  ILE B CG2 1 
ATOM   8461  C  CD1 . ILE B 2  938  ? -23.310 -47.313  39.717  1.00 55.52  ?  938  ILE B CD1 1 
ATOM   8462  N  N   . SER B 2  939  ? -24.568 -51.951  42.724  1.00 64.31  ?  939  SER B N   1 
ATOM   8463  C  CA  . SER B 2  939  ? -24.719 -52.643  44.000  1.00 68.03  ?  939  SER B CA  1 
ATOM   8464  C  C   . SER B 2  939  ? -24.290 -54.101  43.894  1.00 62.37  ?  939  SER B C   1 
ATOM   8465  O  O   . SER B 2  939  ? -23.671 -54.639  44.819  1.00 65.53  ?  939  SER B O   1 
ATOM   8466  C  CB  . SER B 2  939  ? -26.165 -52.547  44.485  1.00 69.99  ?  939  SER B CB  1 
ATOM   8467  O  OG  . SER B 2  939  ? -26.576 -51.197  44.610  1.00 82.48  ?  939  SER B OG  1 
ATOM   8468  N  N   . GLY B 2  940  ? -24.611 -54.756  42.778  1.00 59.13  ?  940  GLY B N   1 
ATOM   8469  C  CA  . GLY B 2  940  ? -24.204 -56.141  42.607  1.00 68.29  ?  940  GLY B CA  1 
ATOM   8470  C  C   . GLY B 2  940  ? -22.698 -56.303  42.530  1.00 64.60  ?  940  GLY B C   1 
ATOM   8471  O  O   . GLY B 2  940  ? -22.134 -57.237  43.106  1.00 66.60  ?  940  GLY B O   1 
ATOM   8472  N  N   . ALA B 2  941  ? -22.026 -55.393  41.821  1.00 57.53  ?  941  ALA B N   1 
ATOM   8473  C  CA  . ALA B 2  941  ? -20.574 -55.477  41.703  1.00 60.29  ?  941  ALA B CA  1 
ATOM   8474  C  C   . ALA B 2  941  ? -19.889 -55.130  43.018  1.00 64.20  ?  941  ALA B C   1 
ATOM   8475  O  O   . ALA B 2  941  ? -18.863 -55.726  43.366  1.00 67.54  ?  941  ALA B O   1 
ATOM   8476  C  CB  . ALA B 2  941  ? -20.084 -54.560  40.584  1.00 52.79  ?  941  ALA B CB  1 
ATOM   8477  N  N   . ARG B 2  942  ? -20.436 -54.164  43.760  1.00 54.07  ?  942  ARG B N   1 
ATOM   8478  C  CA  . ARG B 2  942  ? -19.862 -53.818  45.056  1.00 57.67  ?  942  ARG B CA  1 
ATOM   8479  C  C   . ARG B 2  942  ? -20.022 -54.962  46.051  1.00 56.10  ?  942  ARG B C   1 
ATOM   8480  O  O   . ARG B 2  942  ? -19.085 -55.282  46.792  1.00 56.38  ?  942  ARG B O   1 
ATOM   8481  C  CB  . ARG B 2  942  ? -20.509 -52.541  45.593  1.00 54.76  ?  942  ARG B CB  1 
ATOM   8482  C  CG  . ARG B 2  942  ? -20.032 -52.137  46.978  1.00 52.08  ?  942  ARG B CG  1 
ATOM   8483  C  CD  . ARG B 2  942  ? -20.459 -50.720  47.315  1.00 51.55  ?  942  ARG B CD  1 
ATOM   8484  N  NE  . ARG B 2  942  ? -21.895 -50.628  47.546  1.00 55.81  ?  942  ARG B NE  1 
ATOM   8485  C  CZ  . ARG B 2  942  ? -22.710 -49.829  46.872  1.00 62.74  ?  942  ARG B CZ  1 
ATOM   8486  N  NH1 . ARG B 2  942  ? -22.260 -49.022  45.925  1.00 56.33  ?  942  ARG B NH1 1 
ATOM   8487  N  NH2 . ARG B 2  942  ? -24.010 -49.841  47.154  1.00 65.61  ?  942  ARG B NH2 1 
ATOM   8488  N  N   . ILE B 2  943  ? -21.199 -55.590  46.081  1.00 34.95  ?  943  ILE B N   1 
ATOM   8489  C  CA  . ILE B 2  943  ? -21.415 -56.724  46.974  1.00 31.31  ?  943  ILE B CA  1 
ATOM   8490  C  C   . ILE B 2  943  ? -20.501 -57.880  46.593  1.00 36.67  ?  943  ILE B C   1 
ATOM   8491  O  O   . ILE B 2  943  ? -19.901 -58.529  47.459  1.00 38.85  ?  943  ILE B O   1 
ATOM   8492  C  CB  . ILE B 2  943  ? -22.899 -57.141  46.959  1.00 35.77  ?  943  ILE B CB  1 
ATOM   8493  C  CG1 . ILE B 2  943  ? -23.749 -56.117  47.716  1.00 40.07  ?  943  ILE B CG1 1 
ATOM   8494  C  CG2 . ILE B 2  943  ? -23.078 -58.531  47.555  1.00 36.90  ?  943  ILE B CG2 1 
ATOM   8495  C  CD1 . ILE B 2  943  ? -25.237 -56.391  47.661  1.00 43.56  ?  943  ILE B CD1 1 
ATOM   8496  N  N   . ALA B 2  944  ? -20.368 -58.147  45.291  1.00 63.32  ?  944  ALA B N   1 
ATOM   8497  C  CA  . ALA B 2  944  ? -19.487 -59.221  44.845  1.00 64.17  ?  944  ALA B CA  1 
ATOM   8498  C  C   . ALA B 2  944  ? -18.033 -58.917  45.178  1.00 65.92  ?  944  ALA B C   1 
ATOM   8499  O  O   . ALA B 2  944  ? -17.261 -59.825  45.510  1.00 64.97  ?  944  ALA B O   1 
ATOM   8500  C  CB  . ALA B 2  944  ? -19.658 -59.451  43.344  1.00 59.86  ?  944  ALA B CB  1 
ATOM   8501  N  N   . ALA B 2  945  ? -17.639 -57.644  45.100  1.00 64.82  ?  945  ALA B N   1 
ATOM   8502  C  CA  . ALA B 2  945  ? -16.268 -57.275  45.435  1.00 67.53  ?  945  ALA B CA  1 
ATOM   8503  C  C   . ALA B 2  945  ? -16.008 -57.414  46.930  1.00 67.17  ?  945  ALA B C   1 
ATOM   8504  O  O   . ALA B 2  945  ? -14.941 -57.887  47.339  1.00 69.61  ?  945  ALA B O   1 
ATOM   8505  C  CB  . ALA B 2  945  ? -15.978 -55.849  44.969  1.00 73.36  ?  945  ALA B CB  1 
ATOM   8506  N  N   . LYS B 2  946  ? -16.971 -57.006  47.759  1.00 59.63  ?  946  LYS B N   1 
ATOM   8507  C  CA  . LYS B 2  946  ? -16.815 -57.153  49.203  1.00 56.63  ?  946  LYS B CA  1 
ATOM   8508  C  C   . LYS B 2  946  ? -16.795 -58.621  49.607  1.00 49.05  ?  946  LYS B C   1 
ATOM   8509  O  O   . LYS B 2  946  ? -16.006 -59.022  50.471  1.00 48.82  ?  946  LYS B O   1 
ATOM   8510  C  CB  . LYS B 2  946  ? -17.940 -56.413  49.926  1.00 39.51  ?  946  LYS B CB  1 
ATOM   8511  C  CG  . LYS B 2  946  ? -17.846 -54.900  49.826  1.00 45.87  ?  946  LYS B CG  1 
ATOM   8512  C  CD  . LYS B 2  946  ? -18.948 -54.227  50.623  1.00 45.30  ?  946  LYS B CD  1 
ATOM   8513  C  CE  . LYS B 2  946  ? -18.736 -52.725  50.697  1.00 42.05  ?  946  LYS B CE  1 
ATOM   8514  N  NZ  . LYS B 2  946  ? -19.769 -52.074  51.547  1.00 46.88  ?  946  LYS B NZ  1 
ATOM   8515  N  N   . ARG B 2  947  ? -17.653 -59.438  48.991  1.00 53.45  ?  947  ARG B N   1 
ATOM   8516  C  CA  . ARG B 2  947  ? -17.694 -60.858  49.325  1.00 59.94  ?  947  ARG B CA  1 
ATOM   8517  C  C   . ARG B 2  947  ? -16.414 -61.564  48.898  1.00 60.30  ?  947  ARG B C   1 
ATOM   8518  O  O   . ARG B 2  947  ? -15.917 -62.443  49.611  1.00 60.16  ?  947  ARG B O   1 
ATOM   8519  C  CB  . ARG B 2  947  ? -18.912 -61.514  48.676  1.00 53.33  ?  947  ARG B CB  1 
ATOM   8520  C  CG  . ARG B 2  947  ? -19.043 -63.002  48.954  1.00 45.35  ?  947  ARG B CG  1 
ATOM   8521  C  CD  . ARG B 2  947  ? -19.866 -63.677  47.873  1.00 52.29  ?  947  ARG B CD  1 
ATOM   8522  N  NE  . ARG B 2  947  ? -21.028 -62.880  47.501  1.00 45.55  ?  947  ARG B NE  1 
ATOM   8523  C  CZ  . ARG B 2  947  ? -21.655 -62.970  46.337  1.00 50.55  ?  947  ARG B CZ  1 
ATOM   8524  N  NH1 . ARG B 2  947  ? -21.253 -63.812  45.399  1.00 56.16  ?  947  ARG B NH1 1 
ATOM   8525  N  NH2 . ARG B 2  947  ? -22.711 -62.195  46.107  1.00 52.21  ?  947  ARG B NH2 1 
ATOM   8526  N  N   . ALA B 2  948  ? -15.867 -61.199  47.736  1.00 71.85  ?  948  ALA B N   1 
ATOM   8527  C  CA  . ALA B 2  948  ? -14.610 -61.797  47.302  1.00 66.76  ?  948  ALA B CA  1 
ATOM   8528  C  C   . ALA B 2  948  ? -13.444 -61.327  48.160  1.00 69.03  ?  948  ALA B C   1 
ATOM   8529  O  O   . ALA B 2  948  ? -12.448 -62.047  48.298  1.00 76.11  ?  948  ALA B O   1 
ATOM   8530  C  CB  . ALA B 2  948  ? -14.352 -61.474  45.831  1.00 70.16  ?  948  ALA B CB  1 
ATOM   8531  N  N   . ALA B 2  949  ? -13.549 -60.134  48.746  1.00 53.61  ?  949  ALA B N   1 
ATOM   8532  C  CA  . ALA B 2  949  ? -12.474 -59.618  49.584  1.00 61.44  ?  949  ALA B CA  1 
ATOM   8533  C  C   . ALA B 2  949  ? -12.471 -60.273  50.960  1.00 68.51  ?  949  ALA B C   1 
ATOM   8534  O  O   . ALA B 2  949  ? -11.402 -60.539  51.521  1.00 73.45  ?  949  ALA B O   1 
ATOM   8535  C  CB  . ALA B 2  949  ? -12.593 -58.099  49.715  1.00 69.91  ?  949  ALA B CB  1 
ATOM   8536  N  N   . VAL B 2  950  ? -13.652 -60.543  51.519  1.00 66.65  ?  950  VAL B N   1 
ATOM   8537  C  CA  . VAL B 2  950  ? -13.712 -61.155  52.842  1.00 67.12  ?  950  VAL B CA  1 
ATOM   8538  C  C   . VAL B 2  950  ? -13.480 -62.661  52.758  1.00 64.43  ?  950  VAL B C   1 
ATOM   8539  O  O   . VAL B 2  950  ? -12.904 -63.254  53.679  1.00 67.73  ?  950  VAL B O   1 
ATOM   8540  C  CB  . VAL B 2  950  ? -15.052 -60.820  53.526  1.00 63.61  ?  950  VAL B CB  1 
ATOM   8541  C  CG1 . VAL B 2  950  ? -16.229 -61.335  52.708  1.00 59.72  ?  950  VAL B CG1 1 
ATOM   8542  C  CG2 . VAL B 2  950  ? -15.090 -61.374  54.943  1.00 62.42  ?  950  VAL B CG2 1 
ATOM   8543  N  N   . GLN B 2  951  ? -13.900 -63.301  51.662  1.00 67.21  ?  951  GLN B N   1 
ATOM   8544  C  CA  . GLN B 2  951  ? -13.697 -64.739  51.522  1.00 67.92  ?  951  GLN B CA  1 
ATOM   8545  C  C   . GLN B 2  951  ? -12.222 -65.084  51.371  1.00 68.03  ?  951  GLN B C   1 
ATOM   8546  O  O   . GLN B 2  951  ? -11.809 -66.197  51.716  1.00 67.01  ?  951  GLN B O   1 
ATOM   8547  C  CB  . GLN B 2  951  ? -14.493 -65.273  50.330  1.00 64.36  ?  951  GLN B CB  1 
ATOM   8548  C  CG  . GLN B 2  951  ? -15.963 -65.530  50.633  1.00 68.87  ?  951  GLN B CG  1 
ATOM   8549  C  CD  . GLN B 2  951  ? -16.716 -66.101  49.445  1.00 68.10  ?  951  GLN B CD  1 
ATOM   8550  O  OE1 . GLN B 2  951  ? -16.259 -66.015  48.306  1.00 81.27  ?  951  GLN B OE1 1 
ATOM   8551  N  NE2 . GLN B 2  951  ? -17.883 -66.678  49.707  1.00 67.67  ?  951  GLN B NE2 1 
ATOM   8552  N  N   . ALA B 2  952  ? -11.420 -64.152  50.863  1.00 69.23  ?  952  ALA B N   1 
ATOM   8553  C  CA  . ALA B 2  952  ? -9.977  -64.329  50.790  1.00 74.08  ?  952  ALA B CA  1 
ATOM   8554  C  C   . ALA B 2  952  ? -9.252  -63.785  52.013  1.00 84.00  ?  952  ALA B C   1 
ATOM   8555  O  O   . ALA B 2  952  ? -8.061  -64.066  52.184  1.00 84.58  ?  952  ALA B O   1 
ATOM   8556  C  CB  . ALA B 2  952  ? -9.424  -63.660  49.527  1.00 68.83  ?  952  ALA B CB  1 
ATOM   8557  N  N   . GLY B 2  953  ? -9.936  -63.022  52.863  1.00 102.67 ?  953  GLY B N   1 
ATOM   8558  C  CA  . GLY B 2  953  ? -9.306  -62.470  54.045  1.00 104.03 ?  953  GLY B CA  1 
ATOM   8559  C  C   . GLY B 2  953  ? -8.437  -61.262  53.790  1.00 110.11 ?  953  GLY B C   1 
ATOM   8560  O  O   . GLY B 2  953  ? -7.441  -61.065  54.492  1.00 118.05 ?  953  GLY B O   1 
ATOM   8561  N  N   . GLN B 2  954  ? -8.787  -60.440  52.802  1.00 76.60  ?  954  GLN B N   1 
ATOM   8562  C  CA  . GLN B 2  954  ? -7.985  -59.278  52.442  1.00 78.44  ?  954  GLN B CA  1 
ATOM   8563  C  C   . GLN B 2  954  ? -8.533  -57.970  52.991  1.00 85.73  ?  954  GLN B C   1 
ATOM   8564  O  O   . GLN B 2  954  ? -7.749  -57.053  53.261  1.00 92.30  ?  954  GLN B O   1 
ATOM   8565  C  CB  . GLN B 2  954  ? -7.873  -59.158  50.918  1.00 82.41  ?  954  GLN B CB  1 
ATOM   8566  C  CG  . GLN B 2  954  ? -6.753  -59.976  50.299  1.00 86.24  ?  954  GLN B CG  1 
ATOM   8567  C  CD  . GLN B 2  954  ? -7.122  -60.517  48.931  1.00 83.24  ?  954  GLN B CD  1 
ATOM   8568  O  OE1 . GLN B 2  954  ? -8.026  -60.004  48.271  1.00 75.50  ?  954  GLN B OE1 1 
ATOM   8569  N  NE2 . GLN B 2  954  ? -6.423  -61.561  48.498  1.00 90.60  ?  954  GLN B NE2 1 
ATOM   8570  N  N   . SER B 2  955  ? -9.854  -57.862  53.158  1.00 94.19  ?  955  SER B N   1 
ATOM   8571  C  CA  . SER B 2  955  ? -10.512 -56.605  53.524  1.00 94.80  ?  955  SER B CA  1 
ATOM   8572  C  C   . SER B 2  955  ? -10.171 -55.490  52.540  1.00 103.02 ?  955  SER B C   1 
ATOM   8573  O  O   . SER B 2  955  ? -10.111 -54.315  52.910  1.00 103.41 ?  955  SER B O   1 
ATOM   8574  C  CB  . SER B 2  955  ? -10.162 -56.180  54.953  1.00 96.29  ?  955  SER B CB  1 
ATOM   8575  O  OG  . SER B 2  955  ? -8.835  -55.689  55.032  1.00 91.96  ?  955  SER B OG  1 
ATOM   8576  N  N   . SER B 2  956  ? -9.946  -55.854  51.277  1.00 137.41 ?  956  SER B N   1 
ATOM   8577  C  CA  . SER B 2  956  ? -9.517  -54.883  50.277  1.00 137.82 ?  956  SER B CA  1 
ATOM   8578  C  C   . SER B 2  956  ? -10.705 -54.140  49.677  1.00 136.13 ?  956  SER B C   1 
ATOM   8579  O  O   . SER B 2  956  ? -10.752 -52.905  49.701  1.00 140.15 ?  956  SER B O   1 
ATOM   8580  C  CB  . SER B 2  956  ? -8.711  -55.584  49.179  1.00 141.21 ?  956  SER B CB  1 
ATOM   8581  O  OG  . SER B 2  956  ? -9.504  -56.543  48.500  1.00 144.59 ?  956  SER B OG  1 
ATOM   8582  N  N   . TYR B 2  957  ? -11.674 -54.885  49.137  1.00 89.58  ?  957  TYR B N   1 
ATOM   8583  C  CA  . TYR B 2  957  ? -12.814 -54.314  48.428  1.00 84.12  ?  957  TYR B CA  1 
ATOM   8584  C  C   . TYR B 2  957  ? -12.309 -53.449  47.277  1.00 85.94  ?  957  TYR B C   1 
ATOM   8585  O  O   . TYR B 2  957  ? -12.193 -52.226  47.405  1.00 92.80  ?  957  TYR B O   1 
ATOM   8586  C  CB  . TYR B 2  957  ? -13.710 -53.525  49.396  1.00 77.36  ?  957  TYR B CB  1 
ATOM   8587  C  CG  . TYR B 2  957  ? -14.697 -52.568  48.756  1.00 77.01  ?  957  TYR B CG  1 
ATOM   8588  C  CD1 . TYR B 2  957  ? -15.417 -52.922  47.620  1.00 73.14  ?  957  TYR B CD1 1 
ATOM   8589  C  CD2 . TYR B 2  957  ? -14.898 -51.300  49.288  1.00 78.66  ?  957  TYR B CD2 1 
ATOM   8590  C  CE1 . TYR B 2  957  ? -16.309 -52.042  47.039  1.00 74.81  ?  957  TYR B CE1 1 
ATOM   8591  C  CE2 . TYR B 2  957  ? -15.787 -50.416  48.715  1.00 76.37  ?  957  TYR B CE2 1 
ATOM   8592  C  CZ  . TYR B 2  957  ? -16.490 -50.790  47.591  1.00 75.92  ?  957  TYR B CZ  1 
ATOM   8593  O  OH  . TYR B 2  957  ? -17.377 -49.907  47.020  1.00 82.06  ?  957  TYR B OH  1 
ATOM   8594  N  N   . VAL B 2  958  ? -11.982 -54.087  46.155  1.00 63.49  ?  958  VAL B N   1 
ATOM   8595  C  CA  . VAL B 2  958  ? -11.504 -53.402  44.961  1.00 63.90  ?  958  VAL B CA  1 
ATOM   8596  C  C   . VAL B 2  958  ? -12.334 -53.877  43.776  1.00 63.94  ?  958  VAL B C   1 
ATOM   8597  O  O   . VAL B 2  958  ? -12.567 -55.081  43.615  1.00 72.60  ?  958  VAL B O   1 
ATOM   8598  C  CB  . VAL B 2  958  ? -10.000 -53.645  44.721  1.00 62.52  ?  958  VAL B CB  1 
ATOM   8599  C  CG1 . VAL B 2  958  ? -9.686  -55.137  44.670  1.00 76.45  ?  958  VAL B CG1 1 
ATOM   8600  C  CG2 . VAL B 2  958  ? -9.543  -52.953  43.447  1.00 64.08  ?  958  VAL B CG2 1 
ATOM   8601  N  N   . ILE B 2  959  ? -12.796 -52.934  42.961  1.00 76.85  ?  959  ILE B N   1 
ATOM   8602  C  CA  . ILE B 2  959  ? -13.662 -53.220  41.825  1.00 79.29  ?  959  ILE B CA  1 
ATOM   8603  C  C   . ILE B 2  959  ? -12.850 -53.072  40.547  1.00 84.28  ?  959  ILE B C   1 
ATOM   8604  O  O   . ILE B 2  959  ? -12.111 -52.093  40.383  1.00 87.21  ?  959  ILE B O   1 
ATOM   8605  C  CB  . ILE B 2  959  ? -14.893 -52.297  41.807  1.00 74.03  ?  959  ILE B CB  1 
ATOM   8606  C  CG1 . ILE B 2  959  ? -15.520 -52.224  43.201  1.00 81.83  ?  959  ILE B CG1 1 
ATOM   8607  C  CG2 . ILE B 2  959  ? -15.909 -52.782  40.786  1.00 69.92  ?  959  ILE B CG2 1 
ATOM   8608  C  CD1 . ILE B 2  959  ? -16.829 -51.472  43.243  1.00 70.81  ?  959  ILE B CD1 1 
ATOM   8609  N  N   . SER B 2  960  ? -12.988 -54.042  39.647  1.00 105.32 ?  960  SER B N   1 
ATOM   8610  C  CA  . SER B 2  960  ? -12.301 -53.986  38.368  1.00 103.70 ?  960  SER B CA  1 
ATOM   8611  C  C   . SER B 2  960  ? -12.867 -52.858  37.507  1.00 110.58 ?  960  SER B C   1 
ATOM   8612  O  O   . SER B 2  960  ? -13.910 -52.267  37.805  1.00 114.85 ?  960  SER B O   1 
ATOM   8613  C  CB  . SER B 2  960  ? -12.421 -55.324  37.640  1.00 108.10 ?  960  SER B CB  1 
ATOM   8614  O  OG  . SER B 2  960  ? -11.967 -55.217  36.303  1.00 114.47 ?  960  SER B OG  1 
ATOM   8615  N  N   . ASP B 2  961  ? -12.159 -52.560  36.416  1.00 76.06  ?  961  ASP B N   1 
ATOM   8616  C  CA  . ASP B 2  961  ? -12.587 -51.486  35.526  1.00 67.48  ?  961  ASP B CA  1 
ATOM   8617  C  C   . ASP B 2  961  ? -13.838 -51.881  34.750  1.00 66.93  ?  961  ASP B C   1 
ATOM   8618  O  O   . ASP B 2  961  ? -14.858 -51.183  34.792  1.00 73.56  ?  961  ASP B O   1 
ATOM   8619  C  CB  . ASP B 2  961  ? -11.452 -51.111  34.572  1.00 77.06  ?  961  ASP B CB  1 
ATOM   8620  C  CG  . ASP B 2  961  ? -11.711 -49.805  33.844  1.00 82.09  ?  961  ASP B CG  1 
ATOM   8621  O  OD1 . ASP B 2  961  ? -12.601 -49.044  34.281  1.00 78.82  ?  961  ASP B OD1 1 
ATOM   8622  O  OD2 . ASP B 2  961  ? -11.022 -49.536  32.836  1.00 74.03  -1 961  ASP B OD2 1 
ATOM   8623  N  N   . GLY B 2  962  ? -13.780 -53.001  34.033  1.00 70.48  ?  962  GLY B N   1 
ATOM   8624  C  CA  . GLY B 2  962  ? -14.910 -53.459  33.255  1.00 79.29  ?  962  GLY B CA  1 
ATOM   8625  C  C   . GLY B 2  962  ? -15.950 -54.251  34.012  1.00 73.43  ?  962  GLY B C   1 
ATOM   8626  O  O   . GLY B 2  962  ? -16.800 -54.890  33.387  1.00 71.27  ?  962  GLY B O   1 
ATOM   8627  N  N   . ALA B 2  963  ? -15.915 -54.227  35.347  1.00 58.36  ?  963  ALA B N   1 
ATOM   8628  C  CA  . ALA B 2  963  ? -16.862 -55.017  36.128  1.00 58.22  ?  963  ALA B CA  1 
ATOM   8629  C  C   . ALA B 2  963  ? -18.281 -54.477  35.999  1.00 56.67  ?  963  ALA B C   1 
ATOM   8630  O  O   . ALA B 2  963  ? -19.241 -55.253  35.916  1.00 52.27  ?  963  ALA B O   1 
ATOM   8631  C  CB  . ALA B 2  963  ? -16.433 -55.052  37.595  1.00 54.04  ?  963  ALA B CB  1 
ATOM   8632  N  N   . ILE B 2  964  ? -18.437 -53.157  35.982  1.00 69.29  ?  964  ILE B N   1 
ATOM   8633  C  CA  . ILE B 2  964  ? -19.744 -52.521  35.867  1.00 65.42  ?  964  ILE B CA  1 
ATOM   8634  C  C   . ILE B 2  964  ? -19.900 -51.988  34.450  1.00 63.11  ?  964  ILE B C   1 
ATOM   8635  O  O   . ILE B 2  964  ? -18.985 -51.352  33.911  1.00 67.22  ?  964  ILE B O   1 
ATOM   8636  C  CB  . ILE B 2  964  ? -19.913 -51.394  36.900  1.00 58.76  ?  964  ILE B CB  1 
ATOM   8637  C  CG1 . ILE B 2  964  ? -19.449 -51.859  38.280  1.00 61.15  ?  964  ILE B CG1 1 
ATOM   8638  C  CG2 . ILE B 2  964  ? -21.364 -50.947  36.967  1.00 53.28  ?  964  ILE B CG2 1 
ATOM   8639  C  CD1 . ILE B 2  964  ? -19.463 -50.766  39.324  1.00 57.67  ?  964  ILE B CD1 1 
ATOM   8640  N  N   . GLN B 2  965  ? -21.055 -52.258  33.844  1.00 60.23  ?  965  GLN B N   1 
ATOM   8641  C  CA  . GLN B 2  965  ? -21.392 -51.742  32.519  1.00 63.85  ?  965  GLN B CA  1 
ATOM   8642  C  C   . GLN B 2  965  ? -22.875 -51.406  32.517  1.00 61.01  ?  965  GLN B C   1 
ATOM   8643  O  O   . GLN B 2  965  ? -23.716 -52.307  32.596  1.00 62.81  ?  965  GLN B O   1 
ATOM   8644  C  CB  . GLN B 2  965  ? -21.061 -52.752  31.420  1.00 66.56  ?  965  GLN B CB  1 
ATOM   8645  C  CG  . GLN B 2  965  ? -19.581 -52.896  31.107  1.00 71.43  ?  965  GLN B CG  1 
ATOM   8646  C  CD  . GLN B 2  965  ? -19.325 -53.846  29.952  1.00 69.27  ?  965  GLN B CD  1 
ATOM   8647  O  OE1 . GLN B 2  965  ? -20.259 -54.403  29.373  1.00 59.02  ?  965  GLN B OE1 1 
ATOM   8648  N  NE2 . GLN B 2  965  ? -18.056 -54.034  29.610  1.00 80.44  ?  965  GLN B NE2 1 
ATOM   8649  N  N   . THR B 2  966  ? -23.195 -50.119  32.430  1.00 53.95  ?  966  THR B N   1 
ATOM   8650  C  CA  . THR B 2  966  ? -24.586 -49.697  32.380  1.00 53.23  ?  966  THR B CA  1 
ATOM   8651  C  C   . THR B 2  966  ? -25.245 -50.183  31.090  1.00 59.05  ?  966  THR B C   1 
ATOM   8652  O  O   . THR B 2  966  ? -24.580 -50.517  30.105  1.00 59.39  ?  966  THR B O   1 
ATOM   8653  C  CB  . THR B 2  966  ? -24.690 -48.176  32.486  1.00 59.03  ?  966  THR B CB  1 
ATOM   8654  O  OG1 . THR B 2  966  ? -23.949 -47.567  31.423  1.00 58.91  ?  966  THR B OG1 1 
ATOM   8655  C  CG2 . THR B 2  966  ? -24.135 -47.699  33.820  1.00 68.08  ?  966  THR B CG2 1 
ATOM   8656  N  N   . ALA B 2  967  ? -26.581 -50.221  31.109  1.00 43.56  ?  967  ALA B N   1 
ATOM   8657  C  CA  . ALA B 2  967  ? -27.322 -50.754  29.970  1.00 44.19  ?  967  ALA B CA  1 
ATOM   8658  C  C   . ALA B 2  967  ? -27.105 -49.911  28.720  1.00 45.00  ?  967  ALA B C   1 
ATOM   8659  O  O   . ALA B 2  967  ? -26.990 -50.449  27.612  1.00 47.59  ?  967  ALA B O   1 
ATOM   8660  C  CB  . ALA B 2  967  ? -28.810 -50.843  30.306  1.00 45.58  ?  967  ALA B CB  1 
ATOM   8661  N  N   . CYS B 2  968  ? -27.045 -48.587  28.876  1.00 56.52  ?  968  CYS B N   1 
ATOM   8662  C  CA  . CYS B 2  968  ? -26.790 -47.721  27.730  1.00 58.02  ?  968  CYS B CA  1 
ATOM   8663  C  C   . CYS B 2  968  ? -25.368 -47.884  27.209  1.00 57.17  ?  968  CYS B C   1 
ATOM   8664  O  O   . CYS B 2  968  ? -25.111 -47.636  26.026  1.00 55.04  ?  968  CYS B O   1 
ATOM   8665  C  CB  . CYS B 2  968  ? -27.061 -46.264  28.104  1.00 61.91  ?  968  CYS B CB  1 
ATOM   8666  S  SG  . CYS B 2  968  ? -26.155 -45.680  29.550  1.00 67.21  ?  968  CYS B SG  1 
ATOM   8667  N  N   . GLU B 2  969  ? -24.436 -48.299  28.070  1.00 59.13  ?  969  GLU B N   1 
ATOM   8668  C  CA  . GLU B 2  969  ? -23.070 -48.543  27.620  1.00 53.36  ?  969  GLU B CA  1 
ATOM   8669  C  C   . GLU B 2  969  ? -22.980 -49.824  26.800  1.00 60.65  ?  969  GLU B C   1 
ATOM   8670  O  O   . GLU B 2  969  ? -22.282 -49.868  25.781  1.00 70.76  ?  969  GLU B O   1 
ATOM   8671  C  CB  . GLU B 2  969  ? -22.126 -48.608  28.820  1.00 56.47  ?  969  GLU B CB  1 
ATOM   8672  C  CG  . GLU B 2  969  ? -20.672 -48.861  28.456  1.00 57.82  ?  969  GLU B CG  1 
ATOM   8673  C  CD  . GLU B 2  969  ? -19.765 -48.914  29.671  1.00 69.15  ?  969  GLU B CD  1 
ATOM   8674  O  OE1 . GLU B 2  969  ? -20.288 -48.934  30.805  1.00 70.17  ?  969  GLU B OE1 1 
ATOM   8675  O  OE2 . GLU B 2  969  ? -18.528 -48.936  29.492  1.00 71.16  -1 969  GLU B OE2 1 
ATOM   8676  N  N   . GLN B 2  970  ? -23.683 -50.875  27.229  1.00 53.85  ?  970  GLN B N   1 
ATOM   8677  C  CA  . GLN B 2  970  ? -23.623 -52.146  26.516  1.00 54.11  ?  970  GLN B CA  1 
ATOM   8678  C  C   . GLN B 2  970  ? -24.399 -52.100  25.208  1.00 56.06  ?  970  GLN B C   1 
ATOM   8679  O  O   . GLN B 2  970  ? -24.020 -52.768  24.241  1.00 70.26  ?  970  GLN B O   1 
ATOM   8680  C  CB  . GLN B 2  970  ? -24.161 -53.271  27.400  1.00 58.11  ?  970  GLN B CB  1 
ATOM   8681  C  CG  . GLN B 2  970  ? -23.333 -53.540  28.642  1.00 58.22  ?  970  GLN B CG  1 
ATOM   8682  C  CD  . GLN B 2  970  ? -23.480 -54.964  29.134  1.00 50.66  ?  970  GLN B CD  1 
ATOM   8683  O  OE1 . GLN B 2  970  ? -23.968 -55.833  28.413  1.00 62.08  ?  970  GLN B OE1 1 
ATOM   8684  N  NE2 . GLN B 2  970  ? -23.065 -55.210  30.371  1.00 55.45  ?  970  GLN B NE2 1 
ATOM   8685  N  N   . ALA B 2  971  ? -25.484 -51.326  25.155  1.00 40.77  ?  971  ALA B N   1 
ATOM   8686  C  CA  . ALA B 2  971  ? -26.314 -51.311  23.956  1.00 42.60  ?  971  ALA B CA  1 
ATOM   8687  C  C   . ALA B 2  971  ? -25.622 -50.591  22.804  1.00 46.94  ?  971  ALA B C   1 
ATOM   8688  O  O   . ALA B 2  971  ? -25.700 -51.038  21.654  1.00 45.39  ?  971  ALA B O   1 
ATOM   8689  C  CB  . ALA B 2  971  ? -27.663 -50.664  24.259  1.00 51.10  ?  971  ALA B CB  1 
ATOM   8690  N  N   . CYS B 2  972  ? -24.940 -49.479  23.093  1.00 53.76  ?  972  CYS B N   1 
ATOM   8691  C  CA  . CYS B 2  972  ? -24.331 -48.626  22.078  1.00 54.86  ?  972  CYS B CA  1 
ATOM   8692  C  C   . CYS B 2  972  ? -23.382 -49.409  21.181  1.00 55.66  ?  972  CYS B C   1 
ATOM   8693  O  O   . CYS B 2  972  ? -22.328 -49.868  21.640  1.00 59.62  ?  972  CYS B O   1 
ATOM   8694  C  CB  . CYS B 2  972  ? -23.584 -47.464  22.733  1.00 55.59  ?  972  CYS B CB  1 
ATOM   8695  S  SG  . CYS B 2  972  ? -23.044 -46.189  21.572  1.00 60.33  ?  972  CYS B SG  1 
ATOM   8696  N  N   . PRO B 2  973  ? -23.717 -49.579  19.899  1.00 69.88  ?  973  PRO B N   1 
ATOM   8697  C  CA  . PRO B 2  973  ? -22.807 -50.301  18.997  1.00 73.07  ?  973  PRO B CA  1 
ATOM   8698  C  C   . PRO B 2  973  ? -21.561 -49.513  18.640  1.00 71.13  ?  973  PRO B C   1 
ATOM   8699  O  O   . PRO B 2  973  ? -20.574 -50.115  18.202  1.00 72.24  ?  973  PRO B O   1 
ATOM   8700  C  CB  . PRO B 2  973  ? -23.675 -50.562  17.761  1.00 69.49  ?  973  PRO B CB  1 
ATOM   8701  C  CG  . PRO B 2  973  ? -24.664 -49.446  17.768  1.00 66.64  ?  973  PRO B CG  1 
ATOM   8702  C  CD  . PRO B 2  973  ? -24.944 -49.135  19.215  1.00 67.79  ?  973  PRO B CD  1 
ATOM   8703  N  N   . THR B 2  974  ? -21.574 -48.191  18.809  1.00 47.68  ?  974  THR B N   1 
ATOM   8704  C  CA  . THR B 2  974  ? -20.408 -47.372  18.516  1.00 45.13  ?  974  THR B CA  1 
ATOM   8705  C  C   . THR B 2  974  ? -19.470 -47.225  19.705  1.00 50.69  ?  974  THR B C   1 
ATOM   8706  O  O   . THR B 2  974  ? -18.309 -46.844  19.516  1.00 50.12  ?  974  THR B O   1 
ATOM   8707  C  CB  . THR B 2  974  ? -20.841 -45.979  18.050  1.00 45.65  ?  974  THR B CB  1 
ATOM   8708  O  OG1 . THR B 2  974  ? -21.525 -45.309  19.115  1.00 52.81  ?  974  THR B OG1 1 
ATOM   8709  C  CG2 . THR B 2  974  ? -21.766 -46.081  16.849  1.00 55.66  ?  974  THR B CG2 1 
ATOM   8710  N  N   . GLY B 2  975  ? -19.937 -47.517  20.914  1.00 58.78  ?  975  GLY B N   1 
ATOM   8711  C  CA  . GLY B 2  975  ? -19.108 -47.349  22.095  1.00 58.81  ?  975  GLY B CA  1 
ATOM   8712  C  C   . GLY B 2  975  ? -18.919 -45.905  22.502  1.00 49.90  ?  975  GLY B C   1 
ATOM   8713  O  O   . GLY B 2  975  ? -17.829 -45.529  22.954  1.00 46.00  ?  975  GLY B O   1 
ATOM   8714  N  N   . ALA B 2  976  ? -19.955 -45.080  22.350  1.00 54.27  ?  976  ALA B N   1 
ATOM   8715  C  CA  . ALA B 2  976  ? -19.859 -43.672  22.708  1.00 57.04  ?  976  ALA B CA  1 
ATOM   8716  C  C   . ALA B 2  976  ? -19.987 -43.436  24.206  1.00 57.38  ?  976  ALA B C   1 
ATOM   8717  O  O   . ALA B 2  976  ? -19.564 -42.382  24.691  1.00 58.53  ?  976  ALA B O   1 
ATOM   8718  C  CB  . ALA B 2  976  ? -20.929 -42.865  21.969  1.00 56.17  ?  976  ALA B CB  1 
ATOM   8719  N  N   . ILE B 2  977  ? -20.553 -44.386  24.947  1.00 53.09  ?  977  ILE B N   1 
ATOM   8720  C  CA  . ILE B 2  977  ? -20.775 -44.245  26.382  1.00 54.64  ?  977  ILE B CA  1 
ATOM   8721  C  C   . ILE B 2  977  ? -19.733 -45.070  27.122  1.00 53.96  ?  977  ILE B C   1 
ATOM   8722  O  O   . ILE B 2  977  ? -19.574 -46.268  26.857  1.00 52.63  ?  977  ILE B O   1 
ATOM   8723  C  CB  . ILE B 2  977  ? -22.200 -44.676  26.770  1.00 53.39  ?  977  ILE B CB  1 
ATOM   8724  C  CG1 . ILE B 2  977  ? -23.226 -43.869  25.973  1.00 49.10  ?  977  ILE B CG1 1 
ATOM   8725  C  CG2 . ILE B 2  977  ? -22.418 -44.520  28.264  1.00 53.42  ?  977  ILE B CG2 1 
ATOM   8726  C  CD1 . ILE B 2  977  ? -24.657 -44.177  26.327  1.00 52.35  ?  977  ILE B CD1 1 
ATOM   8727  N  N   . VAL B 2  978  ? -19.014 -44.426  28.041  1.00 41.91  ?  978  VAL B N   1 
ATOM   8728  C  CA  . VAL B 2  978  ? -17.983 -45.075  28.845  1.00 40.38  ?  978  VAL B CA  1 
ATOM   8729  C  C   . VAL B 2  978  ? -18.261 -44.762  30.310  1.00 40.36  ?  978  VAL B C   1 
ATOM   8730  O  O   . VAL B 2  978  ? -18.362 -43.589  30.689  1.00 40.21  ?  978  VAL B O   1 
ATOM   8731  C  CB  . VAL B 2  978  ? -16.567 -44.617  28.453  1.00 39.31  ?  978  VAL B CB  1 
ATOM   8732  C  CG1 . VAL B 2  978  ? -15.517 -45.469  29.154  1.00 37.96  ?  978  VAL B CG1 1 
ATOM   8733  C  CG2 . VAL B 2  978  ? -16.381 -44.670  26.943  1.00 45.00  ?  978  VAL B CG2 1 
ATOM   8734  N  N   . PHE B 2  979  ? -18.378 -45.806  31.129  1.00 43.67  ?  979  PHE B N   1 
ATOM   8735  C  CA  . PHE B 2  979  ? -18.664 -45.676  32.551  1.00 44.30  ?  979  PHE B CA  1 
ATOM   8736  C  C   . PHE B 2  979  ? -17.562 -46.356  33.352  1.00 45.37  ?  979  PHE B C   1 
ATOM   8737  O  O   . PHE B 2  979  ? -17.029 -47.389  32.936  1.00 41.35  ?  979  PHE B O   1 
ATOM   8738  C  CB  . PHE B 2  979  ? -20.028 -46.292  32.897  1.00 42.86  ?  979  PHE B CB  1 
ATOM   8739  C  CG  . PHE B 2  979  ? -20.308 -46.366  34.372  1.00 50.00  ?  979  PHE B CG  1 
ATOM   8740  C  CD1 . PHE B 2  979  ? -20.859 -45.285  35.039  1.00 55.18  ?  979  PHE B CD1 1 
ATOM   8741  C  CD2 . PHE B 2  979  ? -20.022 -47.516  35.092  1.00 54.14  ?  979  PHE B CD2 1 
ATOM   8742  C  CE1 . PHE B 2  979  ? -21.118 -45.347  36.396  1.00 60.86  ?  979  PHE B CE1 1 
ATOM   8743  C  CE2 . PHE B 2  979  ? -20.276 -47.582  36.449  1.00 49.45  ?  979  PHE B CE2 1 
ATOM   8744  C  CZ  . PHE B 2  979  ? -20.826 -46.497  37.101  1.00 54.90  ?  979  PHE B CZ  1 
ATOM   8745  N  N   . GLY B 2  980  ? -17.222 -45.777  34.497  1.00 79.63  ?  980  GLY B N   1 
ATOM   8746  C  CA  . GLY B 2  980  ? -16.173 -46.340  35.321  1.00 88.99  ?  980  GLY B CA  1 
ATOM   8747  C  C   . GLY B 2  980  ? -15.833 -45.426  36.481  1.00 80.50  ?  980  GLY B C   1 
ATOM   8748  O  O   . GLY B 2  980  ? -16.528 -44.445  36.753  1.00 75.12  ?  980  GLY B O   1 
ATOM   8749  N  N   . ASP B 2  981  ? -14.739 -45.775  37.156  1.00 75.32  ?  981  ASP B N   1 
ATOM   8750  C  CA  . ASP B 2  981  ? -14.301 -45.054  38.344  1.00 74.79  ?  981  ASP B CA  1 
ATOM   8751  C  C   . ASP B 2  981  ? -13.528 -43.801  37.950  1.00 71.94  ?  981  ASP B C   1 
ATOM   8752  O  O   . ASP B 2  981  ? -12.630 -43.855  37.105  1.00 84.93  ?  981  ASP B O   1 
ATOM   8753  C  CB  . ASP B 2  981  ? -13.433 -45.961  39.217  1.00 75.79  ?  981  ASP B CB  1 
ATOM   8754  C  CG  . ASP B 2  981  ? -13.110 -45.345  40.564  1.00 73.23  ?  981  ASP B CG  1 
ATOM   8755  O  OD1 . ASP B 2  981  ? -13.786 -44.370  40.955  1.00 78.75  ?  981  ASP B OD1 1 
ATOM   8756  O  OD2 . ASP B 2  981  ? -12.175 -45.835  41.231  1.00 69.96  -1 981  ASP B OD2 1 
ATOM   8757  N  N   . ILE B 2  982  ? -13.878 -42.672  38.569  1.00 48.29  ?  982  ILE B N   1 
ATOM   8758  C  CA  . ILE B 2  982  ? -13.187 -41.419  38.282  1.00 55.50  ?  982  ILE B CA  1 
ATOM   8759  C  C   . ILE B 2  982  ? -11.834 -41.373  38.983  1.00 55.75  ?  982  ILE B C   1 
ATOM   8760  O  O   . ILE B 2  982  ? -10.843 -40.901  38.415  1.00 54.98  ?  982  ILE B O   1 
ATOM   8761  C  CB  . ILE B 2  982  ? -14.072 -40.222  38.680  1.00 58.37  ?  982  ILE B CB  1 
ATOM   8762  C  CG1 . ILE B 2  982  ? -15.349 -40.201  37.840  1.00 55.49  ?  982  ILE B CG1 1 
ATOM   8763  C  CG2 . ILE B 2  982  ? -13.319 -38.911  38.516  1.00 60.23  ?  982  ILE B CG2 1 
ATOM   8764  C  CD1 . ILE B 2  982  ? -15.093 -40.087  36.360  1.00 50.11  ?  982  ILE B CD1 1 
ATOM   8765  N  N   . ASN B 2  983  ? -11.767 -41.875  40.218  1.00 67.34  ?  983  ASN B N   1 
ATOM   8766  C  CA  . ASN B 2  983  ? -10.544 -41.749  41.004  1.00 65.84  ?  983  ASN B CA  1 
ATOM   8767  C  C   . ASN B 2  983  ? -9.441  -42.669  40.495  1.00 68.86  ?  983  ASN B C   1 
ATOM   8768  O  O   . ASN B 2  983  ? -8.261  -42.306  40.556  1.00 65.28  ?  983  ASN B O   1 
ATOM   8769  C  CB  . ASN B 2  983  ? -10.839 -42.033  42.475  1.00 62.87  ?  983  ASN B CB  1 
ATOM   8770  C  CG  . ASN B 2  983  ? -11.562 -40.886  43.153  1.00 65.94  ?  983  ASN B CG  1 
ATOM   8771  O  OD1 . ASN B 2  983  ? -11.663 -39.789  42.603  1.00 69.47  ?  983  ASN B OD1 1 
ATOM   8772  N  ND2 . ASN B 2  983  ? -12.071 -41.134  44.355  1.00 69.16  ?  983  ASN B ND2 1 
ATOM   8773  N  N   . ASP B 2  984  ? -9.795  -43.852  40.000  1.00 84.00  ?  984  ASP B N   1 
ATOM   8774  C  CA  . ASP B 2  984  ? -8.805  -44.773  39.448  1.00 88.04  ?  984  ASP B CA  1 
ATOM   8775  C  C   . ASP B 2  984  ? -8.265  -44.198  38.144  1.00 88.04  ?  984  ASP B C   1 
ATOM   8776  O  O   . ASP B 2  984  ? -8.973  -44.169  37.132  1.00 83.39  ?  984  ASP B O   1 
ATOM   8777  C  CB  . ASP B 2  984  ? -9.426  -46.150  39.233  1.00 94.64  ?  984  ASP B CB  1 
ATOM   8778  C  CG  . ASP B 2  984  ? -8.477  -47.120  38.554  1.00 96.98  ?  984  ASP B CG  1 
ATOM   8779  O  OD1 . ASP B 2  984  ? -7.250  -46.993  38.751  1.00 100.94 ?  984  ASP B OD1 1 
ATOM   8780  O  OD2 . ASP B 2  984  ? -8.959  -48.014  37.828  1.00 92.74  -1 984  ASP B OD2 1 
ATOM   8781  N  N   . SER B 2  985  ? -7.007  -43.748  38.164  1.00 77.16  ?  985  SER B N   1 
ATOM   8782  C  CA  . SER B 2  985  ? -6.459  -43.008  37.031  1.00 71.40  ?  985  SER B CA  1 
ATOM   8783  C  C   . SER B 2  985  ? -6.277  -43.886  35.799  1.00 76.54  ?  985  SER B C   1 
ATOM   8784  O  O   . SER B 2  985  ? -6.280  -43.373  34.674  1.00 84.42  ?  985  SER B O   1 
ATOM   8785  C  CB  . SER B 2  985  ? -5.125  -42.370  37.416  1.00 81.17  ?  985  SER B CB  1 
ATOM   8786  O  OG  . SER B 2  985  ? -4.165  -43.359  37.744  1.00 84.51  ?  985  SER B OG  1 
ATOM   8787  N  N   . ASN B 2  986  ? -6.110  -45.195  35.982  1.00 76.38  ?  986  ASN B N   1 
ATOM   8788  C  CA  . ASN B 2  986  ? -5.902  -46.099  34.859  1.00 75.59  ?  986  ASN B CA  1 
ATOM   8789  C  C   . ASN B 2  986  ? -7.202  -46.544  34.201  1.00 72.21  ?  986  ASN B C   1 
ATOM   8790  O  O   . ASN B 2  986  ? -7.152  -47.238  33.180  1.00 79.11  ?  986  ASN B O   1 
ATOM   8791  C  CB  . ASN B 2  986  ? -5.103  -47.324  35.309  1.00 84.89  ?  986  ASN B CB  1 
ATOM   8792  C  CG  . ASN B 2  986  ? -3.657  -46.992  35.620  1.00 88.02  ?  986  ASN B CG  1 
ATOM   8793  O  OD1 . ASN B 2  986  ? -3.204  -45.870  35.393  1.00 83.72  ?  986  ASN B OD1 1 
ATOM   8794  N  ND2 . ASN B 2  986  ? -2.924  -47.968  36.144  1.00 93.65  ?  986  ASN B ND2 1 
ATOM   8795  N  N   . SER B 2  987  ? -8.353  -46.163  34.748  1.00 67.13  ?  987  SER B N   1 
ATOM   8796  C  CA  . SER B 2  987  ? -9.624  -46.513  34.133  1.00 67.06  ?  987  SER B CA  1 
ATOM   8797  C  C   . SER B 2  987  ? -9.800  -45.773  32.808  1.00 63.78  ?  987  SER B C   1 
ATOM   8798  O  O   . SER B 2  987  ? -9.182  -44.735  32.555  1.00 63.15  ?  987  SER B O   1 
ATOM   8799  C  CB  . SER B 2  987  ? -10.785 -46.186  35.072  1.00 68.90  ?  987  SER B CB  1 
ATOM   8800  O  OG  . SER B 2  987  ? -11.071 -44.797  35.069  1.00 64.59  ?  987  SER B OG  1 
ATOM   8801  N  N   . ARG B 2  988  ? -10.665 -46.325  31.952  1.00 72.79  ?  988  ARG B N   1 
ATOM   8802  C  CA  . ARG B 2  988  ? -10.910 -45.705  30.653  1.00 68.02  ?  988  ARG B CA  1 
ATOM   8803  C  C   . ARG B 2  988  ? -11.576 -44.343  30.792  1.00 64.52  ?  988  ARG B C   1 
ATOM   8804  O  O   . ARG B 2  988  ? -11.313 -43.441  29.988  1.00 69.62  ?  988  ARG B O   1 
ATOM   8805  C  CB  . ARG B 2  988  ? -11.771 -46.621  29.784  1.00 65.31  ?  988  ARG B CB  1 
ATOM   8806  C  CG  . ARG B 2  988  ? -11.125 -47.951  29.443  1.00 68.23  ?  988  ARG B CG  1 
ATOM   8807  C  CD  . ARG B 2  988  ? -12.172 -49.006  29.150  1.00 61.14  ?  988  ARG B CD  1 
ATOM   8808  N  NE  . ARG B 2  988  ? -13.086 -49.194  30.269  1.00 77.64  ?  988  ARG B NE  1 
ATOM   8809  C  CZ  . ARG B 2  988  ? -14.151 -49.982  30.235  1.00 88.44  ?  988  ARG B CZ  1 
ATOM   8810  N  NH1 . ARG B 2  988  ? -14.464 -50.673  29.152  1.00 91.93  ?  988  ARG B NH1 1 
ATOM   8811  N  NH2 . ARG B 2  988  ? -14.922 -50.077  31.315  1.00 91.44  ?  988  ARG B NH2 1 
ATOM   8812  N  N   . VAL B 2  989  ? -12.431 -44.172  31.801  1.00 44.58  ?  989  VAL B N   1 
ATOM   8813  C  CA  . VAL B 2  989  ? -13.100 -42.889  31.994  1.00 38.06  ?  989  VAL B CA  1 
ATOM   8814  C  C   . VAL B 2  989  ? -12.108 -41.834  32.465  1.00 45.13  ?  989  VAL B C   1 
ATOM   8815  O  O   . VAL B 2  989  ? -12.150 -40.681  32.020  1.00 49.08  ?  989  VAL B O   1 
ATOM   8816  C  CB  . VAL B 2  989  ? -14.274 -43.042  32.977  1.00 34.67  ?  989  VAL B CB  1 
ATOM   8817  C  CG1 . VAL B 2  989  ? -15.024 -41.724  33.135  1.00 44.70  ?  989  VAL B CG1 1 
ATOM   8818  C  CG2 . VAL B 2  989  ? -15.207 -44.130  32.505  1.00 41.75  ?  989  VAL B CG2 1 
ATOM   8819  N  N   . ALA B 2  990  ? -11.208 -42.205  33.380  1.00 64.77  ?  990  ALA B N   1 
ATOM   8820  C  CA  . ALA B 2  990  ? -10.209 -41.256  33.859  1.00 65.68  ?  990  ALA B CA  1 
ATOM   8821  C  C   . ALA B 2  990  ? -9.289  -40.798  32.735  1.00 69.39  ?  990  ALA B C   1 
ATOM   8822  O  O   . ALA B 2  990  ? -8.866  -39.636  32.711  1.00 74.49  ?  990  ALA B O   1 
ATOM   8823  C  CB  . ALA B 2  990  ? -9.396  -41.880  34.992  1.00 63.71  ?  990  ALA B CB  1 
ATOM   8824  N  N   . LYS B 2  991  ? -8.970  -41.691  31.798  1.00 64.37  ?  991  LYS B N   1 
ATOM   8825  C  CA  . LYS B 2  991  ? -8.153  -41.298  30.657  1.00 61.39  ?  991  LYS B CA  1 
ATOM   8826  C  C   . LYS B 2  991  ? -8.940  -40.438  29.677  1.00 62.37  ?  991  LYS B C   1 
ATOM   8827  O  O   . LYS B 2  991  ? -8.373  -39.533  29.055  1.00 67.67  ?  991  LYS B O   1 
ATOM   8828  C  CB  . LYS B 2  991  ? -7.602  -42.539  29.955  1.00 67.02  ?  991  LYS B CB  1 
ATOM   8829  C  CG  . LYS B 2  991  ? -6.533  -43.277  30.743  1.00 66.33  ?  991  LYS B CG  1 
ATOM   8830  C  CD  . LYS B 2  991  ? -5.989  -44.462  29.960  1.00 76.68  ?  991  LYS B CD  1 
ATOM   8831  C  CE  . LYS B 2  991  ? -4.870  -45.160  30.718  1.00 80.55  ?  991  LYS B CE  1 
ATOM   8832  N  NZ  . LYS B 2  991  ? -4.355  -46.347  29.980  1.00 88.30  ?  991  LYS B NZ  1 
ATOM   8833  N  N   . TRP B 2  992  ? -10.241 -40.700  29.529  1.00 56.09  ?  992  TRP B N   1 
ATOM   8834  C  CA  . TRP B 2  992  ? -11.050 -39.920  28.599  1.00 54.29  ?  992  TRP B CA  1 
ATOM   8835  C  C   . TRP B 2  992  ? -11.350 -38.534  29.155  1.00 54.71  ?  992  TRP B C   1 
ATOM   8836  O  O   . TRP B 2  992  ? -11.359 -37.548  28.409  1.00 58.92  ?  992  TRP B O   1 
ATOM   8837  C  CB  . TRP B 2  992  ? -12.349 -40.661  28.279  1.00 57.72  ?  992  TRP B CB  1 
ATOM   8838  C  CG  . TRP B 2  992  ? -12.265 -41.562  27.078  1.00 58.34  ?  992  TRP B CG  1 
ATOM   8839  C  CD1 . TRP B 2  992  ? -12.503 -42.905  27.045  1.00 58.01  ?  992  TRP B CD1 1 
ATOM   8840  C  CD2 . TRP B 2  992  ? -11.927 -41.182  25.737  1.00 60.85  ?  992  TRP B CD2 1 
ATOM   8841  N  NE1 . TRP B 2  992  ? -12.331 -43.386  25.770  1.00 52.99  ?  992  TRP B NE1 1 
ATOM   8842  C  CE2 . TRP B 2  992  ? -11.978 -42.349  24.947  1.00 54.30  ?  992  TRP B CE2 1 
ATOM   8843  C  CE3 . TRP B 2  992  ? -11.584 -39.971  25.127  1.00 60.63  ?  992  TRP B CE3 1 
ATOM   8844  C  CZ2 . TRP B 2  992  ? -11.698 -42.340  23.583  1.00 55.46  ?  992  TRP B CZ2 1 
ATOM   8845  C  CZ3 . TRP B 2  992  ? -11.308 -39.964  23.772  1.00 59.49  ?  992  TRP B CZ3 1 
ATOM   8846  C  CH2 . TRP B 2  992  ? -11.366 -41.141  23.015  1.00 61.91  ?  992  TRP B CH2 1 
ATOM   8847  N  N   . LYS B 2  993  ? -11.599 -38.437  30.463  1.00 59.18  ?  993  LYS B N   1 
ATOM   8848  C  CA  . LYS B 2  993  ? -11.894 -37.144  31.069  1.00 62.90  ?  993  LYS B CA  1 
ATOM   8849  C  C   . LYS B 2  993  ? -10.675 -36.233  31.108  1.00 58.10  ?  993  LYS B C   1 
ATOM   8850  O  O   . LYS B 2  993  ? -10.828 -35.021  31.294  1.00 56.56  ?  993  LYS B O   1 
ATOM   8851  C  CB  . LYS B 2  993  ? -12.446 -37.343  32.481  1.00 61.29  ?  993  LYS B CB  1 
ATOM   8852  C  CG  . LYS B 2  993  ? -13.822 -37.995  32.523  1.00 52.43  ?  993  LYS B CG  1 
ATOM   8853  C  CD  . LYS B 2  993  ? -14.635 -37.514  33.713  1.00 54.13  ?  993  LYS B CD  1 
ATOM   8854  C  CE  . LYS B 2  993  ? -16.095 -37.924  33.585  1.00 46.30  ?  993  LYS B CE  1 
ATOM   8855  N  NZ  . LYS B 2  993  ? -16.975 -37.127  34.485  1.00 54.78  ?  993  LYS B NZ  1 
ATOM   8856  N  N   . ALA B 2  994  ? -9.475  -36.784  30.936  1.00 59.32  ?  994  ALA B N   1 
ATOM   8857  C  CA  . ALA B 2  994  ? -8.252  -35.992  30.928  1.00 60.29  ?  994  ALA B CA  1 
ATOM   8858  C  C   . ALA B 2  994  ? -7.965  -35.353  29.576  1.00 65.22  ?  994  ALA B C   1 
ATOM   8859  O  O   . ALA B 2  994  ? -6.978  -34.620  29.457  1.00 69.53  ?  994  ALA B O   1 
ATOM   8860  C  CB  . ALA B 2  994  ? -7.063  -36.859  31.348  1.00 58.76  ?  994  ALA B CB  1 
ATOM   8861  N  N   . GLU B 2  995  ? -8.791  -35.609  28.565  1.00 67.09  ?  995  GLU B N   1 
ATOM   8862  C  CA  . GLU B 2  995  ? -8.564  -35.041  27.246  1.00 63.04  ?  995  GLU B CA  1 
ATOM   8863  C  C   . GLU B 2  995  ? -8.844  -33.540  27.251  1.00 61.42  ?  995  GLU B C   1 
ATOM   8864  O  O   . GLU B 2  995  ? -9.535  -33.008  28.124  1.00 66.52  ?  995  GLU B O   1 
ATOM   8865  C  CB  . GLU B 2  995  ? -9.441  -35.736  26.204  1.00 63.19  ?  995  GLU B CB  1 
ATOM   8866  C  CG  . GLU B 2  995  ? -9.008  -37.159  25.872  1.00 69.39  ?  995  GLU B CG  1 
ATOM   8867  C  CD  . GLU B 2  995  ? -7.576  -37.240  25.375  1.00 71.67  ?  995  GLU B CD  1 
ATOM   8868  O  OE1 . GLU B 2  995  ? -7.159  -36.350  24.604  1.00 71.97  ?  995  GLU B OE1 1 
ATOM   8869  O  OE2 . GLU B 2  995  ? -6.868  -38.196  25.756  1.00 77.51  -1 995  GLU B OE2 1 
ATOM   8870  N  N   . GLY B 2  996  ? -8.291  -32.854  26.248  1.00 55.96  ?  996  GLY B N   1 
ATOM   8871  C  CA  . GLY B 2  996  ? -8.450  -31.413  26.176  1.00 64.40  ?  996  GLY B CA  1 
ATOM   8872  C  C   . GLY B 2  996  ? -9.856  -30.973  25.819  1.00 65.47  ?  996  GLY B C   1 
ATOM   8873  O  O   . GLY B 2  996  ? -10.265 -29.861  26.166  1.00 62.82  ?  996  GLY B O   1 
ATOM   8874  N  N   . HIS B 2  997  ? -10.614 -31.827  25.134  1.00 56.64  ?  997  HIS B N   1 
ATOM   8875  C  CA  . HIS B 2  997  ? -11.948 -31.477  24.666  1.00 56.97  ?  997  HIS B CA  1 
ATOM   8876  C  C   . HIS B 2  997  ? -13.053 -32.033  25.555  1.00 59.18  ?  997  HIS B C   1 
ATOM   8877  O  O   . HIS B 2  997  ? -14.215 -32.059  25.137  1.00 63.83  ?  997  HIS B O   1 
ATOM   8878  C  CB  . HIS B 2  997  ? -12.153 -31.953  23.224  1.00 57.46  ?  997  HIS B CB  1 
ATOM   8879  C  CG  . HIS B 2  997  ? -11.836 -33.401  23.009  1.00 59.17  ?  997  HIS B CG  1 
ATOM   8880  N  ND1 . HIS B 2  997  ? -10.561 -33.913  23.118  1.00 62.80  ?  997  HIS B ND1 1 
ATOM   8881  C  CD2 . HIS B 2  997  ? -12.633 -34.446  22.683  1.00 56.40  ?  997  HIS B CD2 1 
ATOM   8882  C  CE1 . HIS B 2  997  ? -10.587 -35.210  22.872  1.00 58.54  ?  997  HIS B CE1 1 
ATOM   8883  N  NE2 . HIS B 2  997  ? -11.832 -35.559  22.605  1.00 52.35  ?  997  HIS B NE2 1 
ATOM   8884  N  N   . ASN B 2  998  ? -12.722 -32.477  26.764  1.00 55.56  ?  998  ASN B N   1 
ATOM   8885  C  CA  . ASN B 2  998  ? -13.732 -32.959  27.696  1.00 56.52  ?  998  ASN B CA  1 
ATOM   8886  C  C   . ASN B 2  998  ? -14.359 -31.780  28.429  1.00 53.47  ?  998  ASN B C   1 
ATOM   8887  O  O   . ASN B 2  998  ? -13.652 -30.969  29.038  1.00 57.76  ?  998  ASN B O   1 
ATOM   8888  C  CB  . ASN B 2  998  ? -13.114 -33.946  28.688  1.00 62.88  ?  998  ASN B CB  1 
ATOM   8889  C  CG  . ASN B 2  998  ? -14.058 -34.312  29.821  1.00 65.97  ?  998  ASN B CG  1 
ATOM   8890  O  OD1 . ASN B 2  998  ? -14.742 -35.332  29.766  1.00 61.12  ?  998  ASN B OD1 1 
ATOM   8891  N  ND2 . ASN B 2  998  ? -14.076 -33.493  30.868  1.00 74.30  ?  998  ASN B ND2 1 
ATOM   8892  N  N   . TYR B 2  999  ? -15.685 -31.687  28.373  1.00 46.18  ?  999  TYR B N   1 
ATOM   8893  C  CA  . TYR B 2  999  ? -16.402 -30.577  28.981  1.00 52.75  ?  999  TYR B CA  1 
ATOM   8894  C  C   . TYR B 2  999  ? -17.719 -31.071  29.563  1.00 50.78  ?  999  TYR B C   1 
ATOM   8895  O  O   . TYR B 2  999  ? -18.204 -32.154  29.231  1.00 50.64  ?  999  TYR B O   1 
ATOM   8896  C  CB  . TYR B 2  999  ? -16.642 -29.443  27.970  1.00 52.36  ?  999  TYR B CB  1 
ATOM   8897  C  CG  . TYR B 2  999  ? -17.721 -29.716  26.940  1.00 48.56  ?  999  TYR B CG  1 
ATOM   8898  C  CD1 . TYR B 2  999  ? -17.439 -30.438  25.789  1.00 51.01  ?  999  TYR B CD1 1 
ATOM   8899  C  CD2 . TYR B 2  999  ? -19.013 -29.233  27.108  1.00 48.67  ?  999  TYR B CD2 1 
ATOM   8900  C  CE1 . TYR B 2  999  ? -18.416 -30.684  24.840  1.00 54.46  ?  999  TYR B CE1 1 
ATOM   8901  C  CE2 . TYR B 2  999  ? -19.998 -29.474  26.164  1.00 52.49  ?  999  TYR B CE2 1 
ATOM   8902  C  CZ  . TYR B 2  999  ? -19.693 -30.199  25.032  1.00 58.06  ?  999  TYR B CZ  1 
ATOM   8903  O  OH  . TYR B 2  999  ? -20.667 -30.442  24.090  1.00 58.62  ?  999  TYR B OH  1 
ATOM   8904  N  N   . GLY B 2  1000 ? -18.286 -30.256  30.442  1.00 55.04  ?  1000 GLY B N   1 
ATOM   8905  C  CA  . GLY B 2  1000 ? -19.548 -30.571  31.098  1.00 54.36  ?  1000 GLY B CA  1 
ATOM   8906  C  C   . GLY B 2  1000 ? -20.589 -29.508  30.807  1.00 55.09  ?  1000 GLY B C   1 
ATOM   8907  O  O   . GLY B 2  1000 ? -20.273 -28.317  30.759  1.00 61.59  ?  1000 GLY B O   1 
ATOM   8908  N  N   . LEU B 2  1001 ? -21.830 -29.946  30.618  1.00 68.66  ?  1001 LEU B N   1 
ATOM   8909  C  CA  . LEU B 2  1001 ? -22.898 -29.043  30.210  1.00 77.88  ?  1001 LEU B CA  1 
ATOM   8910  C  C   . LEU B 2  1001 ? -23.260 -28.069  31.325  1.00 75.55  ?  1001 LEU B C   1 
ATOM   8911  O  O   . LEU B 2  1001 ? -23.291 -28.431  32.505  1.00 79.72  ?  1001 LEU B O   1 
ATOM   8912  C  CB  . LEU B 2  1001 ? -24.132 -29.843  29.797  1.00 75.58  ?  1001 LEU B CB  1 
ATOM   8913  C  CG  . LEU B 2  1001 ? -24.456 -29.878  28.303  1.00 78.72  ?  1001 LEU B CG  1 
ATOM   8914  C  CD1 . LEU B 2  1001 ? -25.709 -30.702  28.045  1.00 67.42  ?  1001 LEU B CD1 1 
ATOM   8915  C  CD2 . LEU B 2  1001 ? -24.617 -28.468  27.758  1.00 77.68  ?  1001 LEU B CD2 1 
ATOM   8916  N  N   . LEU B 2  1002 ? -23.541 -26.824  30.931  1.00 53.21  ?  1002 LEU B N   1 
ATOM   8917  C  CA  . LEU B 2  1002 ? -24.017 -25.777  31.837  1.00 47.85  ?  1002 LEU B CA  1 
ATOM   8918  C  C   . LEU B 2  1002 ? -23.088 -25.615  33.038  1.00 57.30  ?  1002 LEU B C   1 
ATOM   8919  O  O   . LEU B 2  1002 ? -23.506 -25.664  34.198  1.00 57.73  ?  1002 LEU B O   1 
ATOM   8920  C  CB  . LEU B 2  1002 ? -25.453 -26.054  32.282  1.00 46.50  ?  1002 LEU B CB  1 
ATOM   8921  C  CG  . LEU B 2  1002 ? -26.477 -26.255  31.164  1.00 45.40  ?  1002 LEU B CG  1 
ATOM   8922  C  CD1 . LEU B 2  1002 ? -27.863 -26.471  31.744  1.00 53.27  ?  1002 LEU B CD1 1 
ATOM   8923  C  CD2 . LEU B 2  1002 ? -26.473 -25.061  30.223  1.00 45.40  ?  1002 LEU B CD2 1 
ATOM   8924  N  N   . GLY B 2  1003 ? -21.802 -25.411  32.745  1.00 64.24  ?  1003 GLY B N   1 
ATOM   8925  C  CA  . GLY B 2  1003 ? -20.815 -25.261  33.799  1.00 74.42  ?  1003 GLY B CA  1 
ATOM   8926  C  C   . GLY B 2  1003 ? -20.928 -23.970  34.583  1.00 76.02  ?  1003 GLY B C   1 
ATOM   8927  O  O   . GLY B 2  1003 ? -20.373 -23.880  35.684  1.00 72.16  ?  1003 GLY B O   1 
ATOM   8928  N  N   . PHE B 2  1004 ? -21.622 -22.965  34.040  1.00 80.77  ?  1004 PHE B N   1 
ATOM   8929  C  CA  . PHE B 2  1004 ? -21.758 -21.698  34.753  1.00 76.16  ?  1004 PHE B CA  1 
ATOM   8930  C  C   . PHE B 2  1004 ? -22.528 -21.887  36.053  1.00 75.61  ?  1004 PHE B C   1 
ATOM   8931  O  O   . PHE B 2  1004 ? -22.244 -21.220  37.055  1.00 85.65  ?  1004 PHE B O   1 
ATOM   8932  C  CB  . PHE B 2  1004 ? -22.432 -20.650  33.863  1.00 73.10  ?  1004 PHE B CB  1 
ATOM   8933  C  CG  . PHE B 2  1004 ? -23.863 -20.960  33.517  1.00 72.04  ?  1004 PHE B CG  1 
ATOM   8934  C  CD1 . PHE B 2  1004 ? -24.173 -21.911  32.558  1.00 70.06  ?  1004 PHE B CD1 1 
ATOM   8935  C  CD2 . PHE B 2  1004 ? -24.898 -20.286  34.144  1.00 77.99  ?  1004 PHE B CD2 1 
ATOM   8936  C  CE1 . PHE B 2  1004 ? -25.490 -22.188  32.237  1.00 73.85  ?  1004 PHE B CE1 1 
ATOM   8937  C  CE2 . PHE B 2  1004 ? -26.215 -20.558  33.828  1.00 77.87  ?  1004 PHE B CE2 1 
ATOM   8938  C  CZ  . PHE B 2  1004 ? -26.512 -21.511  32.874  1.00 75.50  ?  1004 PHE B CZ  1 
ATOM   8939  N  N   . LEU B 2  1005 ? -23.504 -22.791  36.056  1.00 72.67  ?  1005 LEU B N   1 
ATOM   8940  C  CA  . LEU B 2  1005 ? -24.071 -23.276  37.306  1.00 73.46  ?  1005 LEU B CA  1 
ATOM   8941  C  C   . LEU B 2  1005 ? -23.089 -24.248  37.944  1.00 73.44  ?  1005 LEU B C   1 
ATOM   8942  O  O   . LEU B 2  1005 ? -22.741 -25.270  37.342  1.00 84.26  ?  1005 LEU B O   1 
ATOM   8943  C  CB  . LEU B 2  1005 ? -25.415 -23.957  37.061  1.00 66.11  ?  1005 LEU B CB  1 
ATOM   8944  C  CG  . LEU B 2  1005 ? -26.497 -23.127  36.371  1.00 68.26  ?  1005 LEU B CG  1 
ATOM   8945  C  CD1 . LEU B 2  1005 ? -27.563 -24.027  35.788  1.00 69.04  ?  1005 LEU B CD1 1 
ATOM   8946  C  CD2 . LEU B 2  1005 ? -27.115 -22.132  37.345  1.00 83.82  ?  1005 LEU B CD2 1 
ATOM   8947  N  N   . ASN B 2  1006 ? -22.634 -23.933  39.158  1.00 66.13  ?  1006 ASN B N   1 
ATOM   8948  C  CA  . ASN B 2  1006 ? -21.620 -24.746  39.833  1.00 74.07  ?  1006 ASN B CA  1 
ATOM   8949  C  C   . ASN B 2  1006 ? -22.261 -26.045  40.314  1.00 79.30  ?  1006 ASN B C   1 
ATOM   8950  O  O   . ASN B 2  1006 ? -22.528 -26.254  41.502  1.00 80.30  ?  1006 ASN B O   1 
ATOM   8951  C  CB  . ASN B 2  1006 ? -20.974 -23.970  40.973  1.00 67.72  ?  1006 ASN B CB  1 
ATOM   8952  C  CG  . ASN B 2  1006 ? -20.201 -22.762  40.484  1.00 74.70  ?  1006 ASN B CG  1 
ATOM   8953  O  OD1 . ASN B 2  1006 ? -19.493 -22.835  39.480  1.00 88.02  ?  1006 ASN B OD1 1 
ATOM   8954  N  ND2 . ASN B 2  1006 ? -20.325 -21.645  41.195  1.00 72.88  ?  1006 ASN B ND2 1 
ATOM   8955  N  N   . THR B 2  1007 ? -22.509 -26.940  39.356  1.00 53.34  ?  1007 THR B N   1 
ATOM   8956  C  CA  . THR B 2  1007 ? -23.060 -28.256  39.648  1.00 49.32  ?  1007 THR B CA  1 
ATOM   8957  C  C   . THR B 2  1007 ? -22.005 -29.351  39.684  1.00 52.61  ?  1007 THR B C   1 
ATOM   8958  O  O   . THR B 2  1007 ? -22.208 -30.354  40.375  1.00 50.70  ?  1007 THR B O   1 
ATOM   8959  C  CB  . THR B 2  1007 ? -24.129 -28.636  38.616  1.00 44.73  ?  1007 THR B CB  1 
ATOM   8960  O  OG1 . THR B 2  1007 ? -23.623 -28.418  37.292  1.00 52.81  ?  1007 THR B OG1 1 
ATOM   8961  C  CG2 . THR B 2  1007 ? -25.389 -27.812  38.821  1.00 42.15  ?  1007 THR B CG2 1 
ATOM   8962  N  N   . VAL B 2  1008 ? -20.887 -29.167  38.984  1.00 66.26  ?  1008 VAL B N   1 
ATOM   8963  C  CA  . VAL B 2  1008 ? -19.814 -30.156  38.881  1.00 67.25  ?  1008 VAL B CA  1 
ATOM   8964  C  C   . VAL B 2  1008 ? -20.388 -31.496  38.434  1.00 67.85  ?  1008 VAL B C   1 
ATOM   8965  O  O   . VAL B 2  1008 ? -20.439 -32.445  39.231  1.00 67.96  ?  1008 VAL B O   1 
ATOM   8966  C  CB  . VAL B 2  1008 ? -19.048 -30.295  40.206  1.00 64.43  ?  1008 VAL B CB  1 
ATOM   8967  C  CG1 . VAL B 2  1008 ? -17.690 -30.930  39.962  1.00 65.75  ?  1008 VAL B CG1 1 
ATOM   8968  C  CG2 . VAL B 2  1008 ? -18.881 -28.935  40.862  1.00 70.15  ?  1008 VAL B CG2 1 
ATOM   8969  N  N   . PRO B 2  1009 ? -20.833 -31.623  37.185  1.00 59.87  ?  1009 PRO B N   1 
ATOM   8970  C  CA  . PRO B 2  1009 ? -21.429 -32.887  36.746  1.00 52.35  ?  1009 PRO B CA  1 
ATOM   8971  C  C   . PRO B 2  1009 ? -20.384 -33.980  36.615  1.00 54.03  ?  1009 PRO B C   1 
ATOM   8972  O  O   . PRO B 2  1009 ? -19.225 -33.730  36.275  1.00 54.95  ?  1009 PRO B O   1 
ATOM   8973  C  CB  . PRO B 2  1009 ? -22.039 -32.535  35.384  1.00 55.94  ?  1009 PRO B CB  1 
ATOM   8974  C  CG  . PRO B 2  1009 ? -21.216 -31.391  34.902  1.00 63.26  ?  1009 PRO B CG  1 
ATOM   8975  C  CD  . PRO B 2  1009 ? -20.906 -30.591  36.135  1.00 67.05  ?  1009 PRO B CD  1 
ATOM   8976  N  N   . ARG B 2  1010 ? -20.810 -35.211  36.896  1.00 72.39  ?  1010 ARG B N   1 
ATOM   8977  C  CA  . ARG B 2  1010 ? -19.960 -36.377  36.697  1.00 69.94  ?  1010 ARG B CA  1 
ATOM   8978  C  C   . ARG B 2  1010 ? -20.116 -36.985  35.310  1.00 66.75  ?  1010 ARG B C   1 
ATOM   8979  O  O   . ARG B 2  1010 ? -19.244 -37.750  34.882  1.00 66.52  ?  1010 ARG B O   1 
ATOM   8980  C  CB  . ARG B 2  1010 ? -20.255 -37.440  37.761  1.00 63.63  ?  1010 ARG B CB  1 
ATOM   8981  C  CG  . ARG B 2  1010 ? -19.845 -37.027  39.167  1.00 74.17  ?  1010 ARG B CG  1 
ATOM   8982  C  CD  . ARG B 2  1010 ? -19.890 -38.201  40.130  1.00 80.22  ?  1010 ARG B CD  1 
ATOM   8983  N  NE  . ARG B 2  1010 ? -19.188 -37.919  41.377  1.00 77.17  ?  1010 ARG B NE  1 
ATOM   8984  C  CZ  . ARG B 2  1010 ? -17.874 -37.995  41.533  1.00 78.43  ?  1010 ARG B CZ  1 
ATOM   8985  N  NH1 . ARG B 2  1010 ? -17.078 -38.344  40.535  1.00 84.10  ?  1010 ARG B NH1 1 
ATOM   8986  N  NH2 . ARG B 2  1010 ? -17.344 -37.718  42.721  1.00 76.46  ?  1010 ARG B NH2 1 
ATOM   8987  N  N   . THR B 2  1011 ? -21.198 -36.663  34.605  1.00 70.24  ?  1011 THR B N   1 
ATOM   8988  C  CA  . THR B 2  1011 ? -21.389 -37.079  33.220  1.00 68.07  ?  1011 THR B CA  1 
ATOM   8989  C  C   . THR B 2  1011 ? -20.917 -35.947  32.314  1.00 68.32  ?  1011 THR B C   1 
ATOM   8990  O  O   . THR B 2  1011 ? -21.547 -34.886  32.256  1.00 76.63  ?  1011 THR B O   1 
ATOM   8991  C  CB  . THR B 2  1011 ? -22.853 -37.422  32.950  1.00 66.42  ?  1011 THR B CB  1 
ATOM   8992  O  OG1 . THR B 2  1011 ? -23.251 -38.524  33.774  1.00 73.59  ?  1011 THR B OG1 1 
ATOM   8993  C  CG2 . THR B 2  1011 ? -23.058 -37.790  31.488  1.00 69.38  ?  1011 THR B CG2 1 
ATOM   8994  N  N   . THR B 2  1012 ? -19.814 -36.168  31.609  1.00 37.48  ?  1012 THR B N   1 
ATOM   8995  C  CA  . THR B 2  1012 ? -19.216 -35.154  30.755  1.00 34.96  ?  1012 THR B CA  1 
ATOM   8996  C  C   . THR B 2  1012 ? -19.334 -35.559  29.291  1.00 38.87  ?  1012 THR B C   1 
ATOM   8997  O  O   . THR B 2  1012 ? -19.689 -36.692  28.955  1.00 31.98  ?  1012 THR B O   1 
ATOM   8998  C  CB  . THR B 2  1012 ? -17.745 -34.922  31.123  1.00 35.21  ?  1012 THR B CB  1 
ATOM   8999  O  OG1 . THR B 2  1012 ? -17.016 -36.148  30.994  1.00 43.93  ?  1012 THR B OG1 1 
ATOM   9000  C  CG2 . THR B 2  1012 ? -17.628 -34.420  32.551  1.00 45.93  ?  1012 THR B CG2 1 
ATOM   9001  N  N   . TYR B 2  1013 ? -19.030 -34.603  28.418  1.00 67.66  ?  1013 TYR B N   1 
ATOM   9002  C  CA  . TYR B 2  1013 ? -19.081 -34.799  26.979  1.00 60.31  ?  1013 TYR B CA  1 
ATOM   9003  C  C   . TYR B 2  1013 ? -17.716 -34.516  26.370  1.00 60.19  ?  1013 TYR B C   1 
ATOM   9004  O  O   . TYR B 2  1013 ? -16.957 -33.676  26.863  1.00 65.22  ?  1013 TYR B O   1 
ATOM   9005  C  CB  . TYR B 2  1013 ? -20.128 -33.890  26.328  1.00 52.08  ?  1013 TYR B CB  1 
ATOM   9006  C  CG  . TYR B 2  1013 ? -21.550 -34.226  26.704  1.00 55.33  ?  1013 TYR B CG  1 
ATOM   9007  C  CD1 . TYR B 2  1013 ? -22.142 -33.658  27.824  1.00 67.54  ?  1013 TYR B CD1 1 
ATOM   9008  C  CD2 . TYR B 2  1013 ? -22.302 -35.104  25.938  1.00 50.36  ?  1013 TYR B CD2 1 
ATOM   9009  C  CE1 . TYR B 2  1013 ? -23.443 -33.960  28.173  1.00 68.02  ?  1013 TYR B CE1 1 
ATOM   9010  C  CE2 . TYR B 2  1013 ? -23.603 -35.411  26.278  1.00 55.42  ?  1013 TYR B CE2 1 
ATOM   9011  C  CZ  . TYR B 2  1013 ? -24.170 -34.837  27.397  1.00 62.40  ?  1013 TYR B CZ  1 
ATOM   9012  O  OH  . TYR B 2  1013 ? -25.467 -35.139  27.741  1.00 64.10  ?  1013 TYR B OH  1 
ATOM   9013  N  N   . LEU B 2  1014 ? -17.412 -35.229  25.292  1.00 40.87  ?  1014 LEU B N   1 
ATOM   9014  C  CA  . LEU B 2  1014 ? -16.216 -34.983  24.500  1.00 39.76  ?  1014 LEU B CA  1 
ATOM   9015  C  C   . LEU B 2  1014 ? -16.634 -34.237  23.240  1.00 51.34  ?  1014 LEU B C   1 
ATOM   9016  O  O   . LEU B 2  1014 ? -17.457 -34.737  22.465  1.00 46.31  ?  1014 LEU B O   1 
ATOM   9017  C  CB  . LEU B 2  1014 ? -15.513 -36.293  24.153  1.00 45.30  ?  1014 LEU B CB  1 
ATOM   9018  C  CG  . LEU B 2  1014 ? -14.900 -37.036  25.342  1.00 37.73  ?  1014 LEU B CG  1 
ATOM   9019  C  CD1 . LEU B 2  1014 ? -14.797 -38.524  25.044  1.00 43.88  ?  1014 LEU B CD1 1 
ATOM   9020  C  CD2 . LEU B 2  1014 ? -13.538 -36.458  25.704  1.00 39.73  ?  1014 LEU B CD2 1 
ATOM   9021  N  N   . ALA B 2  1015 ? -16.077 -33.041  23.049  1.00 61.48  ?  1015 ALA B N   1 
ATOM   9022  C  CA  . ALA B 2  1015 ? -16.502 -32.177  21.954  1.00 53.25  ?  1015 ALA B CA  1 
ATOM   9023  C  C   . ALA B 2  1015 ? -16.319 -32.869  20.610  1.00 56.52  ?  1015 ALA B C   1 
ATOM   9024  O  O   . ALA B 2  1015 ? -15.371 -33.633  20.406  1.00 60.83  ?  1015 ALA B O   1 
ATOM   9025  C  CB  . ALA B 2  1015 ? -15.719 -30.865  21.981  1.00 54.74  ?  1015 ALA B CB  1 
ATOM   9026  N  N   . ARG B 2  1016 ? -17.244 -32.604  19.690  1.00 55.43  ?  1016 ARG B N   1 
ATOM   9027  C  CA  . ARG B 2  1016 ? -17.162 -33.193  18.362  1.00 53.47  ?  1016 ARG B CA  1 
ATOM   9028  C  C   . ARG B 2  1016 ? -16.041 -32.545  17.561  1.00 59.28  ?  1016 ARG B C   1 
ATOM   9029  O  O   . ARG B 2  1016 ? -15.920 -31.317  17.516  1.00 66.78  ?  1016 ARG B O   1 
ATOM   9030  C  CB  . ARG B 2  1016 ? -18.489 -33.039  17.621  1.00 45.97  ?  1016 ARG B CB  1 
ATOM   9031  C  CG  . ARG B 2  1016 ? -18.453 -33.606  16.211  1.00 42.56  ?  1016 ARG B CG  1 
ATOM   9032  C  CD  . ARG B 2  1016 ? -19.842 -33.814  15.641  1.00 49.15  ?  1016 ARG B CD  1 
ATOM   9033  N  NE  . ARG B 2  1016 ? -19.789 -34.457  14.334  1.00 51.24  ?  1016 ARG B NE  1 
ATOM   9034  C  CZ  . ARG B 2  1016 ? -20.853 -34.785  13.615  1.00 56.96  ?  1016 ARG B CZ  1 
ATOM   9035  N  NH1 . ARG B 2  1016 ? -22.081 -34.539  14.045  1.00 59.19  ?  1016 ARG B NH1 1 
ATOM   9036  N  NH2 . ARG B 2  1016 ? -20.682 -35.374  12.434  1.00 58.99  ?  1016 ARG B NH2 1 
ATOM   9037  N  N   . VAL B 2  1017 ? -15.222 -33.377  16.927  1.00 57.86  ?  1017 VAL B N   1 
ATOM   9038  C  CA  . VAL B 2  1017 ? -14.157 -32.929  16.040  1.00 50.22  ?  1017 VAL B CA  1 
ATOM   9039  C  C   . VAL B 2  1017 ? -14.510 -33.376  14.629  1.00 60.08  ?  1017 VAL B C   1 
ATOM   9040  O  O   . VAL B 2  1017 ? -14.934 -34.519  14.423  1.00 71.25  ?  1017 VAL B O   1 
ATOM   9041  C  CB  . VAL B 2  1017 ? -12.791 -33.485  16.477  1.00 52.62  ?  1017 VAL B CB  1 
ATOM   9042  C  CG1 . VAL B 2  1017 ? -11.703 -33.015  15.539  1.00 60.09  ?  1017 VAL B CG1 1 
ATOM   9043  C  CG2 . VAL B 2  1017 ? -12.480 -33.066  17.905  1.00 57.60  ?  1017 VAL B CG2 1 
ATOM   9044  N  N   . ARG B 2  1018 ? -14.357 -32.473  13.666  1.00 70.99  ?  1018 ARG B N   1 
ATOM   9045  C  CA  . ARG B 2  1018 ? -14.641 -32.752  12.268  1.00 67.20  ?  1018 ARG B CA  1 
ATOM   9046  C  C   . ARG B 2  1018 ? -13.347 -32.792  11.465  1.00 64.00  ?  1018 ARG B C   1 
ATOM   9047  O  O   . ARG B 2  1018 ? -12.320 -32.240  11.868  1.00 56.93  ?  1018 ARG B O   1 
ATOM   9048  C  CB  . ARG B 2  1018 ? -15.592 -31.703  11.681  1.00 67.11  ?  1018 ARG B CB  1 
ATOM   9049  C  CG  . ARG B 2  1018 ? -16.971 -31.686  12.319  1.00 63.81  ?  1018 ARG B CG  1 
ATOM   9050  C  CD  . ARG B 2  1018 ? -17.886 -30.674  11.642  1.00 69.15  ?  1018 ARG B CD  1 
ATOM   9051  N  NE  . ARG B 2  1018 ? -18.049 -30.936  10.217  1.00 72.91  ?  1018 ARG B NE  1 
ATOM   9052  C  CZ  . ARG B 2  1018 ? -17.621 -30.130  9.255   1.00 75.09  ?  1018 ARG B CZ  1 
ATOM   9053  N  NH1 . ARG B 2  1018 ? -17.002 -28.993  9.531   1.00 75.05  ?  1018 ARG B NH1 1 
ATOM   9054  N  NH2 . ARG B 2  1018 ? -17.818 -30.472  7.985   1.00 81.88  ?  1018 ARG B NH2 1 
ATOM   9055  N  N   . ASN B 2  1019 ? -13.410 -33.462  10.315  1.00 79.54  ?  1019 ASN B N   1 
ATOM   9056  C  CA  . ASN B 2  1019 ? -12.277 -33.590  9.398   1.00 83.54  ?  1019 ASN B CA  1 
ATOM   9057  C  C   . ASN B 2  1019 ? -12.741 -33.221  7.997   1.00 86.24  ?  1019 ASN B C   1 
ATOM   9058  O  O   . ASN B 2  1019 ? -12.954 -34.097  7.148   1.00 95.22  ?  1019 ASN B O   1 
ATOM   9059  C  CB  . ASN B 2  1019 ? -11.696 -35.004  9.428   1.00 88.12  ?  1019 ASN B CB  1 
ATOM   9060  C  CG  . ASN B 2  1019 ? -10.314 -35.078  8.814   1.00 92.05  ?  1019 ASN B CG  1 
ATOM   9061  O  OD1 . ASN B 2  1019 ? -9.687  -34.055  8.540   1.00 93.26  ?  1019 ASN B OD1 1 
ATOM   9062  N  ND2 . ASN B 2  1019 ? -9.831  -36.294  8.592   1.00 96.17  ?  1019 ASN B ND2 1 
ATOM   9063  N  N   . PRO B 2  1020 ? -12.906 -31.932  7.717   1.00 54.13  ?  1020 PRO B N   1 
ATOM   9064  C  CA  . PRO B 2  1020 ? -13.394 -31.514  6.402   1.00 58.05  ?  1020 PRO B CA  1 
ATOM   9065  C  C   . PRO B 2  1020 ? -12.269 -31.332  5.397   1.00 65.69  ?  1020 PRO B C   1 
ATOM   9066  O  O   . PRO B 2  1020 ? -11.114 -31.077  5.745   1.00 68.04  ?  1020 PRO B O   1 
ATOM   9067  C  CB  . PRO B 2  1020 ? -14.079 -30.177  6.712   1.00 57.86  ?  1020 PRO B CB  1 
ATOM   9068  C  CG  . PRO B 2  1020 ? -13.257 -29.610  7.827   1.00 56.13  ?  1020 PRO B CG  1 
ATOM   9069  C  CD  . PRO B 2  1020 ? -12.702 -30.781  8.616   1.00 57.60  ?  1020 PRO B CD  1 
ATOM   9070  N  N   . SER B 2  1021 ? -12.630 -31.473  4.125   1.00 94.43  ?  1021 SER B N   1 
ATOM   9071  C  CA  . SER B 2  1021 ? -11.671 -31.314  3.044   1.00 102.83 ?  1021 SER B CA  1 
ATOM   9072  C  C   . SER B 2  1021 ? -11.412 -29.839  2.767   1.00 110.09 ?  1021 SER B C   1 
ATOM   9073  O  O   . SER B 2  1021 ? -12.286 -28.986  2.951   1.00 113.23 ?  1021 SER B O   1 
ATOM   9074  C  CB  . SER B 2  1021 ? -12.171 -32.002  1.774   1.00 105.73 ?  1021 SER B CB  1 
ATOM   9075  O  OG  . SER B 2  1021 ? -12.431 -33.374  2.007   1.00 112.80 ?  1021 SER B OG  1 
ATOM   9076  N  N   . GLU B 2  1022 ? -10.191 -29.543  2.317   1.00 129.98 ?  1022 GLU B N   1 
ATOM   9077  C  CA  . GLU B 2  1022 ? -9.824  -28.159  2.041   1.00 137.91 ?  1022 GLU B CA  1 
ATOM   9078  C  C   . GLU B 2  1022 ? -10.471 -27.646  0.762   1.00 137.00 ?  1022 GLU B C   1 
ATOM   9079  O  O   . GLU B 2  1022 ? -10.722 -26.442  0.637   1.00 138.96 ?  1022 GLU B O   1 
ATOM   9080  C  CB  . GLU B 2  1022 ? -8.303  -28.024  1.958   1.00 145.22 ?  1022 GLU B CB  1 
ATOM   9081  C  CG  . GLU B 2  1022 ? -7.574  -28.365  3.248   1.00 149.14 ?  1022 GLU B CG  1 
ATOM   9082  C  CD  . GLU B 2  1022 ? -7.249  -29.842  3.361   1.00 148.09 ?  1022 GLU B CD  1 
ATOM   9083  O  OE1 . GLU B 2  1022 ? -7.553  -30.592  2.410   1.00 145.12 ?  1022 GLU B OE1 1 
ATOM   9084  O  OE2 . GLU B 2  1022 ? -6.688  -30.250  4.400   1.00 144.12 -1 1022 GLU B OE2 1 
ATOM   9085  N  N   . GLU B 2  1023 ? -10.749 -28.534  -0.195  1.00 102.97 ?  1023 GLU B N   1 
ATOM   9086  C  CA  . GLU B 2  1023 ? -11.351 -28.095  -1.450  1.00 96.48  ?  1023 GLU B CA  1 
ATOM   9087  C  C   . GLU B 2  1023 ? -12.801 -27.670  -1.261  1.00 95.17  ?  1023 GLU B C   1 
ATOM   9088  O  O   . GLU B 2  1023 ? -13.279 -26.774  -1.966  1.00 100.91 ?  1023 GLU B O   1 
ATOM   9089  C  CB  . GLU B 2  1023 ? -11.252 -29.205  -2.497  1.00 99.71  ?  1023 GLU B CB  1 
ATOM   9090  C  CG  . GLU B 2  1023 ? -11.476 -28.732  -3.924  1.00 113.71 ?  1023 GLU B CG  1 
ATOM   9091  C  CD  . GLU B 2  1023 ? -10.748 -29.586  -4.943  1.00 107.31 ?  1023 GLU B CD  1 
ATOM   9092  O  OE1 . GLU B 2  1023 ? -9.727  -30.206  -4.578  1.00 96.87  ?  1023 GLU B OE1 1 
ATOM   9093  O  OE2 . GLU B 2  1023 ? -11.193 -29.635  -6.109  1.00 97.34  -1 1023 GLU B OE2 1 
ATOM   9094  N  N   . LEU B 2  1024 ? -13.511 -28.291  -0.319  1.00 93.99  ?  1024 LEU B N   1 
ATOM   9095  C  CA  . LEU B 2  1024 ? -14.896 -27.912  -0.064  1.00 96.17  ?  1024 LEU B CA  1 
ATOM   9096  C  C   . LEU B 2  1024 ? -14.989 -26.734  0.900   1.00 101.89 ?  1024 LEU B C   1 
ATOM   9097  O  O   . LEU B 2  1024 ? -15.826 -25.844  0.717   1.00 99.26  ?  1024 LEU B O   1 
ATOM   9098  C  CB  . LEU B 2  1024 ? -15.674 -29.109  0.482   1.00 93.35  ?  1024 LEU B CB  1 
ATOM   9099  C  CG  . LEU B 2  1024 ? -16.386 -29.985  -0.549  1.00 89.77  ?  1024 LEU B CG  1 
ATOM   9100  C  CD1 . LEU B 2  1024 ? -16.925 -31.248  0.104   1.00 82.38  ?  1024 LEU B CD1 1 
ATOM   9101  C  CD2 . LEU B 2  1024 ? -17.505 -29.209  -1.227  1.00 94.35  ?  1024 LEU B CD2 1 
ATOM   9102  N  N   . GLU B 2  1025 ? -14.138 -26.712  1.930   1.00 131.83 ?  1025 GLU B N   1 
ATOM   9103  C  CA  . GLU B 2  1025 ? -14.190 -25.631  2.910   1.00 131.76 ?  1025 GLU B CA  1 
ATOM   9104  C  C   . GLU B 2  1025 ? -13.667 -24.325  2.326   1.00 143.47 ?  1025 GLU B C   1 
ATOM   9105  O  O   . GLU B 2  1025 ? -14.237 -23.256  2.574   1.00 145.59 ?  1025 GLU B O   1 
ATOM   9106  C  CB  . GLU B 2  1025 ? -13.392 -26.012  4.156   1.00 128.26 ?  1025 GLU B CB  1 
ATOM   9107  C  CG  . GLU B 2  1025 ? -14.055 -27.069  5.022   1.00 125.99 ?  1025 GLU B CG  1 
ATOM   9108  C  CD  . GLU B 2  1025 ? -15.378 -26.609  5.602   1.00 137.86 ?  1025 GLU B CD  1 
ATOM   9109  O  OE1 . GLU B 2  1025 ? -15.460 -25.448  6.054   1.00 164.46 ?  1025 GLU B OE1 1 
ATOM   9110  O  OE2 . GLU B 2  1025 ? -16.337 -27.411  5.609   1.00 119.61 -1 1025 GLU B OE2 1 
ATOM   9111  N  N   . LYS B 2  1026 ? -12.586 -24.388  1.555   1.00 166.60 ?  1026 LYS B N   1 
ATOM   9112  C  CA  . LYS B 2  1026 ? -11.987 -23.191  0.978   1.00 168.52 ?  1026 LYS B CA  1 
ATOM   9113  C  C   . LYS B 2  1026 ? -12.424 -23.005  -0.472  1.00 152.78 ?  1026 LYS B C   1 
ATOM   9114  O  O   . LYS B 2  1026 ? -11.614 -23.113  -1.393  1.00 139.53 ?  1026 LYS B O   1 
ATOM   9115  C  CB  . LYS B 2  1026 ? -10.461 -23.260  1.065   1.00 168.60 ?  1026 LYS B CB  1 
ATOM   9116  C  CG  . LYS B 2  1026 ? -9.932  -23.519  2.467   1.00 164.38 ?  1026 LYS B CG  1 
ATOM   9117  C  CD  . LYS B 2  1026 ? -10.165 -22.327  3.381   1.00 161.17 ?  1026 LYS B CD  1 
ATOM   9118  C  CE  . LYS B 2  1026 ? -9.481  -22.522  4.724   1.00 150.62 ?  1026 LYS B CE  1 
ATOM   9119  N  NZ  . LYS B 2  1026 ? -9.506  -21.280  5.545   1.00 149.97 ?  1026 LYS B NZ  1 
ATOM   9120  N  N   . GLU C 3  16   ? -61.932 15.513   56.843  1.00 151.74 ?  16   GLU C N   1 
ATOM   9121  C  CA  . GLU C 3  16   ? -62.778 14.351   57.082  1.00 146.54 ?  16   GLU C CA  1 
ATOM   9122  C  C   . GLU C 3  16   ? -62.480 13.730   58.442  1.00 141.92 ?  16   GLU C C   1 
ATOM   9123  O  O   . GLU C 3  16   ? -61.424 13.972   59.026  1.00 141.51 ?  16   GLU C O   1 
ATOM   9124  C  CB  . GLU C 3  16   ? -62.590 13.313   55.973  1.00 145.04 ?  16   GLU C CB  1 
ATOM   9125  C  CG  . GLU C 3  16   ? -63.271 13.675   54.663  1.00 154.00 ?  16   GLU C CG  1 
ATOM   9126  C  CD  . GLU C 3  16   ? -64.754 13.360   54.670  1.00 154.97 ?  16   GLU C CD  1 
ATOM   9127  O  OE1 . GLU C 3  16   ? -65.198 12.597   55.554  1.00 154.00 ?  16   GLU C OE1 1 
ATOM   9128  O  OE2 . GLU C 3  16   ? -65.478 13.877   53.793  1.00 149.41 -1 16   GLU C OE2 1 
ATOM   9129  N  N   . ALA C 3  17   ? -63.418 12.929   58.941  1.00 133.11 ?  17   ALA C N   1 
ATOM   9130  C  CA  . ALA C 3  17   ? -63.283 12.277   60.234  1.00 127.48 ?  17   ALA C CA  1 
ATOM   9131  C  C   . ALA C 3  17   ? -63.547 10.787   60.087  1.00 127.30 ?  17   ALA C C   1 
ATOM   9132  O  O   . ALA C 3  17   ? -64.284 10.353   59.198  1.00 128.55 ?  17   ALA C O   1 
ATOM   9133  C  CB  . ALA C 3  17   ? -64.243 12.877   61.271  1.00 132.57 ?  17   ALA C CB  1 
ATOM   9134  N  N   . TYR C 3  18   ? -62.931 10.004   60.974  1.00 99.98  ?  18   TYR C N   1 
ATOM   9135  C  CA  . TYR C 3  18   ? -63.108 8.558    60.968  1.00 92.51  ?  18   TYR C CA  1 
ATOM   9136  C  C   . TYR C 3  18   ? -64.352 8.112    61.726  1.00 95.30  ?  18   TYR C C   1 
ATOM   9137  O  O   . TYR C 3  18   ? -64.700 6.928    61.671  1.00 89.37  ?  18   TYR C O   1 
ATOM   9138  C  CB  . TYR C 3  18   ? -61.872 7.876    61.562  1.00 90.83  ?  18   TYR C CB  1 
ATOM   9139  C  CG  . TYR C 3  18   ? -60.639 7.969    60.688  1.00 88.91  ?  18   TYR C CG  1 
ATOM   9140  C  CD1 . TYR C 3  18   ? -60.619 7.412    59.416  1.00 85.29  ?  18   TYR C CD1 1 
ATOM   9141  C  CD2 . TYR C 3  18   ? -59.492 8.610    61.140  1.00 90.71  ?  18   TYR C CD2 1 
ATOM   9142  C  CE1 . TYR C 3  18   ? -59.493 7.496    58.616  1.00 81.21  ?  18   TYR C CE1 1 
ATOM   9143  C  CE2 . TYR C 3  18   ? -58.361 8.697    60.348  1.00 81.05  ?  18   TYR C CE2 1 
ATOM   9144  C  CZ  . TYR C 3  18   ? -58.367 8.138    59.088  1.00 75.34  ?  18   TYR C CZ  1 
ATOM   9145  O  OH  . TYR C 3  18   ? -57.243 8.223    58.297  1.00 68.37  ?  18   TYR C OH  1 
ATOM   9146  N  N   . LEU C 3  19   ? -65.021 9.024    62.429  1.00 125.52 ?  19   LEU C N   1 
ATOM   9147  C  CA  . LEU C 3  19   ? -66.264 8.712    63.131  1.00 129.11 ?  19   LEU C CA  1 
ATOM   9148  C  C   . LEU C 3  19   ? -67.128 9.963    63.075  1.00 132.40 ?  19   LEU C C   1 
ATOM   9149  O  O   . LEU C 3  19   ? -66.826 10.954   63.746  1.00 137.90 ?  19   LEU C O   1 
ATOM   9150  C  CB  . LEU C 3  19   ? -65.994 8.281    64.570  1.00 129.83 ?  19   LEU C CB  1 
ATOM   9151  C  CG  . LEU C 3  19   ? -67.190 7.788    65.386  1.00 132.09 ?  19   LEU C CG  1 
ATOM   9152  C  CD1 . LEU C 3  19   ? -67.776 6.531    64.764  1.00 130.78 ?  19   LEU C CD1 1 
ATOM   9153  C  CD2 . LEU C 3  19   ? -66.786 7.537    66.831  1.00 127.39 ?  19   LEU C CD2 1 
ATOM   9154  N  N   . LEU C 3  20   ? -68.196 9.918    62.282  1.00 143.27 ?  20   LEU C N   1 
ATOM   9155  C  CA  . LEU C 3  20   ? -68.929 11.129   61.931  1.00 153.23 ?  20   LEU C CA  1 
ATOM   9156  C  C   . LEU C 3  20   ? -69.950 11.549   62.989  1.00 158.77 ?  20   LEU C C   1 
ATOM   9157  O  O   . LEU C 3  20   ? -69.781 12.611   63.603  1.00 153.05 ?  20   LEU C O   1 
ATOM   9158  C  CB  . LEU C 3  20   ? -69.614 10.955   60.570  1.00 149.96 ?  20   LEU C CB  1 
ATOM   9159  C  CG  . LEU C 3  20   ? -68.755 10.373   59.446  1.00 152.23 ?  20   LEU C CG  1 
ATOM   9160  C  CD1 . LEU C 3  20   ? -69.629 9.865    58.309  1.00 152.16 ?  20   LEU C CD1 1 
ATOM   9161  C  CD2 . LEU C 3  20   ? -67.757 11.403   58.942  1.00 152.24 ?  20   LEU C CD2 1 
ATOM   9162  N  N   . PRO C 3  21   ? -71.005 10.778   63.245  1.00 169.32 ?  21   PRO C N   1 
ATOM   9163  C  CA  . PRO C 3  21   ? -72.136 11.307   64.011  1.00 161.74 ?  21   PRO C CA  1 
ATOM   9164  C  C   . PRO C 3  21   ? -71.867 11.250   65.511  1.00 163.77 ?  21   PRO C C   1 
ATOM   9165  O  O   . PRO C 3  21   ? -70.796 10.854   65.967  1.00 168.22 ?  21   PRO C O   1 
ATOM   9166  C  CB  . PRO C 3  21   ? -73.278 10.375   63.610  1.00 159.08 ?  21   PRO C CB  1 
ATOM   9167  C  CG  . PRO C 3  21   ? -72.604 9.056    63.408  1.00 160.13 ?  21   PRO C CG  1 
ATOM   9168  C  CD  . PRO C 3  21   ? -71.149 9.321    63.052  1.00 160.67 ?  21   PRO C CD  1 
ATOM   9169  N  N   . GLY C 3  22   ? -72.872 11.662   66.277  1.00 165.71 ?  22   GLY C N   1 
ATOM   9170  C  CA  . GLY C 3  22   ? -72.797 11.598   67.722  1.00 168.17 ?  22   GLY C CA  1 
ATOM   9171  C  C   . GLY C 3  22   ? -73.200 10.239   68.250  1.00 166.29 ?  22   GLY C C   1 
ATOM   9172  O  O   . GLY C 3  22   ? -74.245 10.097   68.892  1.00 175.25 ?  22   GLY C O   1 
ATOM   9173  N  N   . GLU C 3  23   ? -72.379 9.228    67.979  1.00 139.35 ?  23   GLU C N   1 
ATOM   9174  C  CA  . GLU C 3  23   ? -72.678 7.878    68.430  1.00 135.83 ?  23   GLU C CA  1 
ATOM   9175  C  C   . GLU C 3  23   ? -72.541 7.767    69.944  1.00 140.53 ?  23   GLU C C   1 
ATOM   9176  O  O   . GLU C 3  23   ? -71.796 8.514    70.584  1.00 145.93 ?  23   GLU C O   1 
ATOM   9177  C  CB  . GLU C 3  23   ? -71.750 6.869    67.753  1.00 135.71 ?  23   GLU C CB  1 
ATOM   9178  C  CG  . GLU C 3  23   ? -71.846 6.845    66.236  1.00 139.94 ?  23   GLU C CG  1 
ATOM   9179  C  CD  . GLU C 3  23   ? -72.889 5.865    65.734  1.00 136.58 ?  23   GLU C CD  1 
ATOM   9180  O  OE1 . GLU C 3  23   ? -73.040 4.789    66.349  1.00 131.94 ?  23   GLU C OE1 1 
ATOM   9181  O  OE2 . GLU C 3  23   ? -73.557 6.168    64.722  1.00 136.85 -1 23   GLU C OE2 1 
ATOM   9182  N  N   . THR C 3  24   ? -73.276 6.820    70.514  1.00 140.42 ?  24   THR C N   1 
ATOM   9183  C  CA  . THR C 3  24   ? -73.204 6.494    71.929  1.00 141.71 ?  24   THR C CA  1 
ATOM   9184  C  C   . THR C 3  24   ? -72.670 5.076    72.081  1.00 139.77 ?  24   THR C C   1 
ATOM   9185  O  O   . THR C 3  24   ? -72.693 4.281    71.137  1.00 135.85 ?  24   THR C O   1 
ATOM   9186  C  CB  . THR C 3  24   ? -74.583 6.623    72.592  1.00 147.30 ?  24   THR C CB  1 
ATOM   9187  O  OG1 . THR C 3  24   ? -75.243 7.793    72.093  1.00 150.34 ?  24   THR C OG1 1 
ATOM   9188  C  CG2 . THR C 3  24   ? -74.452 6.755    74.103  1.00 146.14 ?  24   THR C CG2 1 
ATOM   9189  N  N   . TYR C 3  25   ? -72.163 4.770    73.278  1.00 114.85 ?  25   TYR C N   1 
ATOM   9190  C  CA  . TYR C 3  25   ? -71.694 3.414    73.551  1.00 109.84 ?  25   TYR C CA  1 
ATOM   9191  C  C   . TYR C 3  25   ? -72.800 2.392    73.322  1.00 110.31 ?  25   TYR C C   1 
ATOM   9192  O  O   . TYR C 3  25   ? -72.552 1.307    72.783  1.00 113.79 ?  25   TYR C O   1 
ATOM   9193  C  CB  . TYR C 3  25   ? -71.162 3.317    74.980  1.00 109.13 ?  25   TYR C CB  1 
ATOM   9194  C  CG  . TYR C 3  25   ? -70.201 4.420    75.358  1.00 104.87 ?  25   TYR C CG  1 
ATOM   9195  C  CD1 . TYR C 3  25   ? -68.864 4.358    74.987  1.00 102.16 ?  25   TYR C CD1 1 
ATOM   9196  C  CD2 . TYR C 3  25   ? -70.629 5.523    76.085  1.00 108.94 ?  25   TYR C CD2 1 
ATOM   9197  C  CE1 . TYR C 3  25   ? -67.980 5.362    75.330  1.00 103.54 ?  25   TYR C CE1 1 
ATOM   9198  C  CE2 . TYR C 3  25   ? -69.752 6.532    76.433  1.00 113.58 ?  25   TYR C CE2 1 
ATOM   9199  C  CZ  . TYR C 3  25   ? -68.429 6.446    76.053  1.00 104.98 ?  25   TYR C CZ  1 
ATOM   9200  O  OH  . TYR C 3  25   ? -67.551 7.448    76.396  1.00 93.15  ?  25   TYR C OH  1 
ATOM   9201  N  N   . THR C 3  26   ? -74.031 2.721    73.722  1.00 97.47  ?  26   THR C N   1 
ATOM   9202  C  CA  . THR C 3  26   ? -75.150 1.822    73.459  1.00 101.00 ?  26   THR C CA  1 
ATOM   9203  C  C   . THR C 3  26   ? -75.541 1.837    71.987  1.00 100.11 ?  26   THR C C   1 
ATOM   9204  O  O   . THR C 3  26   ? -76.099 0.855    71.486  1.00 95.48  ?  26   THR C O   1 
ATOM   9205  C  CB  . THR C 3  26   ? -76.349 2.197    74.331  1.00 100.39 ?  26   THR C CB  1 
ATOM   9206  O  OG1 . THR C 3  26   ? -75.895 2.560    75.641  1.00 103.19 ?  26   THR C OG1 1 
ATOM   9207  C  CG2 . THR C 3  26   ? -77.307 1.019    74.452  1.00 97.41  ?  26   THR C CG2 1 
ATOM   9208  N  N   . SER C 3  27   ? -75.263 2.937    71.283  1.00 151.03 ?  27   SER C N   1 
ATOM   9209  C  CA  . SER C 3  27   ? -75.521 2.984    69.846  1.00 154.28 ?  27   SER C CA  1 
ATOM   9210  C  C   . SER C 3  27   ? -74.618 2.013    69.099  1.00 149.36 ?  27   SER C C   1 
ATOM   9211  O  O   . SER C 3  27   ? -75.070 1.286    68.207  1.00 146.06 ?  27   SER C O   1 
ATOM   9212  C  CB  . SER C 3  27   ? -75.335 4.410    69.326  1.00 155.70 ?  27   SER C CB  1 
ATOM   9213  O  OG  . SER C 3  27   ? -76.264 5.304    69.917  1.00 149.95 ?  27   SER C OG  1 
ATOM   9214  N  N   . ILE C 3  28   ? -73.333 1.988    69.455  1.00 113.68 ?  28   ILE C N   1 
ATOM   9215  C  CA  . ILE C 3  28   ? -72.406 1.042    68.844  1.00 107.16 ?  28   ILE C CA  1 
ATOM   9216  C  C   . ILE C 3  28   ? -72.774 -0.385   69.230  1.00 101.32 ?  28   ILE C C   1 
ATOM   9217  O  O   . ILE C 3  28   ? -72.741 -1.299   68.397  1.00 93.03  ?  28   ILE C O   1 
ATOM   9218  C  CB  . ILE C 3  28   ? -70.960 1.387    69.248  1.00 105.25 ?  28   ILE C CB  1 
ATOM   9219  C  CG1 . ILE C 3  28   ? -70.502 2.671    68.552  1.00 104.37 ?  28   ILE C CG1 1 
ATOM   9220  C  CG2 . ILE C 3  28   ? -70.018 0.237    68.932  1.00 106.01 ?  28   ILE C CG2 1 
ATOM   9221  C  CD1 . ILE C 3  28   ? -69.221 3.249    69.117  1.00 103.26 ?  28   ILE C CD1 1 
ATOM   9222  N  N   . SER C 3  29   ? -73.148 -0.594   70.495  1.00 100.28 ?  29   SER C N   1 
ATOM   9223  C  CA  . SER C 3  29   ? -73.447 -1.940   70.975  1.00 98.37  ?  29   SER C CA  1 
ATOM   9224  C  C   . SER C 3  29   ? -74.671 -2.520   70.276  1.00 98.79  ?  29   SER C C   1 
ATOM   9225  O  O   . SER C 3  29   ? -74.659 -3.673   69.832  1.00 98.24  ?  29   SER C O   1 
ATOM   9226  C  CB  . SER C 3  29   ? -73.654 -1.916   72.490  1.00 99.78  ?  29   SER C CB  1 
ATOM   9227  O  OG  . SER C 3  29   ? -72.501 -1.426   73.153  1.00 97.61  ?  29   SER C OG  1 
ATOM   9228  N  N   . ALA C 3  30   ? -75.741 -1.730   70.169  1.00 116.85 ?  30   ALA C N   1 
ATOM   9229  C  CA  . ALA C 3  30   ? -76.973 -2.239   69.575  1.00 118.96 ?  30   ALA C CA  1 
ATOM   9230  C  C   . ALA C 3  30   ? -76.842 -2.398   68.066  1.00 115.11 ?  30   ALA C C   1 
ATOM   9231  O  O   . ALA C 3  30   ? -77.353 -3.366   67.493  1.00 118.40 ?  30   ALA C O   1 
ATOM   9232  C  CB  . ALA C 3  30   ? -78.143 -1.318   69.918  1.00 119.46 ?  30   ALA C CB  1 
ATOM   9233  N  N   . LYS C 3  31   ? -76.157 -1.461   67.405  1.00 110.46 ?  31   LYS C N   1 
ATOM   9234  C  CA  . LYS C 3  31   ? -76.075 -1.499   65.948  1.00 111.64 ?  31   LYS C CA  1 
ATOM   9235  C  C   . LYS C 3  31   ? -75.210 -2.660   65.466  1.00 113.92 ?  31   LYS C C   1 
ATOM   9236  O  O   . LYS C 3  31   ? -75.515 -3.283   64.442  1.00 112.31 ?  31   LYS C O   1 
ATOM   9237  C  CB  . LYS C 3  31   ? -75.536 -0.170   65.420  1.00 105.26 ?  31   LYS C CB  1 
ATOM   9238  C  CG  . LYS C 3  31   ? -75.819 0.086    63.948  1.00 105.58 ?  31   LYS C CG  1 
ATOM   9239  C  CD  . LYS C 3  31   ? -75.326 1.463    63.517  1.00 113.06 ?  31   LYS C CD  1 
ATOM   9240  C  CE  . LYS C 3  31   ? -75.737 2.547    64.505  1.00 112.33 ?  31   LYS C CE  1 
ATOM   9241  N  NZ  . LYS C 3  31   ? -75.056 3.843    64.221  1.00 106.80 ?  31   LYS C NZ  1 
ATOM   9242  N  N   . ILE C 3  32   ? -74.129 -2.965   66.185  1.00 113.74 ?  32   ILE C N   1 
ATOM   9243  C  CA  . ILE C 3  32   ? -73.275 -4.075   65.775  1.00 102.48 ?  32   ILE C CA  1 
ATOM   9244  C  C   . ILE C 3  32   ? -73.812 -5.395   66.313  1.00 105.49 ?  32   ILE C C   1 
ATOM   9245  O  O   . ILE C 3  32   ? -73.575 -6.454   65.721  1.00 109.80 ?  32   ILE C O   1 
ATOM   9246  C  CB  . ILE C 3  32   ? -71.824 -3.827   66.218  1.00 95.57  ?  32   ILE C CB  1 
ATOM   9247  C  CG1 . ILE C 3  32   ? -71.374 -2.431   65.778  1.00 95.87  ?  32   ILE C CG1 1 
ATOM   9248  C  CG2 . ILE C 3  32   ? -70.891 -4.889   65.642  1.00 86.65  ?  32   ILE C CG2 1 
ATOM   9249  C  CD1 . ILE C 3  32   ? -69.926 -2.118   66.110  1.00 93.96  ?  32   ILE C CD1 1 
ATOM   9250  N  N   . GLY C 3  33   ? -74.543 -5.360   67.431  1.00 137.67 ?  33   GLY C N   1 
ATOM   9251  C  CA  . GLY C 3  33   ? -75.115 -6.574   67.986  1.00 138.05 ?  33   GLY C CA  1 
ATOM   9252  C  C   . GLY C 3  33   ? -76.389 -7.031   67.312  1.00 147.65 ?  33   GLY C C   1 
ATOM   9253  O  O   . GLY C 3  33   ? -76.778 -8.191   67.472  1.00 144.79 ?  33   GLY C O   1 
ATOM   9254  N  N   . ASP C 3  34   ? -77.045 -6.145   66.559  1.00 193.01 ?  34   ASP C N   1 
ATOM   9255  C  CA  . ASP C 3  34   ? -78.283 -6.500   65.877  1.00 196.74 ?  34   ASP C CA  1 
ATOM   9256  C  C   . ASP C 3  34   ? -78.049 -7.326   64.620  1.00 195.57 ?  34   ASP C C   1 
ATOM   9257  O  O   . ASP C 3  34   ? -78.972 -8.013   64.168  1.00 197.06 ?  34   ASP C O   1 
ATOM   9258  C  CB  . ASP C 3  34   ? -79.070 -5.237   65.519  1.00 197.87 ?  34   ASP C CB  1 
ATOM   9259  C  CG  . ASP C 3  34   ? -79.981 -4.781   66.641  1.00 201.34 ?  34   ASP C CG  1 
ATOM   9260  O  OD1 . ASP C 3  34   ? -80.031 -5.466   67.684  1.00 197.00 ?  34   ASP C OD1 1 
ATOM   9261  O  OD2 . ASP C 3  34   ? -80.647 -3.736   66.480  1.00 204.37 -1 34   ASP C OD2 1 
ATOM   9262  N  N   . VAL C 3  35   ? -76.852 -7.273   64.044  1.00 152.28 ?  35   VAL C N   1 
ATOM   9263  C  CA  . VAL C 3  35   ? -76.537 -8.062   62.854  1.00 149.98 ?  35   VAL C CA  1 
ATOM   9264  C  C   . VAL C 3  35   ? -76.506 -9.541   63.235  1.00 145.05 ?  35   VAL C C   1 
ATOM   9265  O  O   . VAL C 3  35   ? -77.124 -10.357  62.535  1.00 141.96 ?  35   VAL C O   1 
ATOM   9266  C  CB  . VAL C 3  35   ? -75.222 -7.600   62.202  1.00 145.19 ?  35   VAL C CB  1 
ATOM   9267  C  CG1 . VAL C 3  35   ? -74.780 -8.592   61.137  1.00 135.51 ?  35   VAL C CG1 1 
ATOM   9268  C  CG2 . VAL C 3  35   ? -75.382 -6.206   61.614  1.00 141.44 ?  35   VAL C CG2 1 
ATOM   9269  N  N   . PRO C 3  36   ? -75.817 -9.953   64.325  1.00 142.78 ?  36   PRO C N   1 
ATOM   9270  C  CA  . PRO C 3  36   ? -76.039 -11.312  64.832  1.00 140.53 ?  36   PRO C CA  1 
ATOM   9271  C  C   . PRO C 3  36   ? -77.238 -11.348  65.764  1.00 151.90 ?  36   PRO C C   1 
ATOM   9272  O  O   . PRO C 3  36   ? -77.964 -10.355  65.876  1.00 157.47 ?  36   PRO C O   1 
ATOM   9273  C  CB  . PRO C 3  36   ? -74.734 -11.630  65.567  1.00 134.70 ?  36   PRO C CB  1 
ATOM   9274  C  CG  . PRO C 3  36   ? -74.296 -10.317  66.082  1.00 142.03 ?  36   PRO C CG  1 
ATOM   9275  C  CD  . PRO C 3  36   ? -74.722 -9.289   65.061  1.00 139.24 ?  36   PRO C CD  1 
ATOM   9276  N  N   . LEU C 3  37   ? -77.460 -12.480  66.430  1.00 110.77 ?  37   LEU C N   1 
ATOM   9277  C  CA  . LEU C 3  37   ? -78.569 -12.688  67.359  1.00 113.30 ?  37   LEU C CA  1 
ATOM   9278  C  C   . LEU C 3  37   ? -79.935 -12.537  66.697  1.00 120.71 ?  37   LEU C C   1 
ATOM   9279  O  O   . LEU C 3  37   ? -80.960 -12.571  67.389  1.00 116.77 ?  37   LEU C O   1 
ATOM   9280  C  CB  . LEU C 3  37   ? -78.472 -11.750  68.570  1.00 105.25 ?  37   LEU C CB  1 
ATOM   9281  C  CG  . LEU C 3  37   ? -77.174 -11.827  69.375  1.00 104.93 ?  37   LEU C CG  1 
ATOM   9282  C  CD1 . LEU C 3  37   ? -77.153 -10.764  70.460  1.00 111.30 ?  37   LEU C CD1 1 
ATOM   9283  C  CD2 . LEU C 3  37   ? -76.996 -13.214  69.974  1.00 110.25 ?  37   LEU C CD2 1 
ATOM   9284  N  N   . THR C 3  38   ? -79.978 -12.365  65.379  1.00 157.33 ?  38   THR C N   1 
ATOM   9285  C  CA  . THR C 3  38   ? -81.248 -12.309  64.674  1.00 148.14 ?  38   THR C CA  1 
ATOM   9286  C  C   . THR C 3  38   ? -81.854 -13.710  64.605  1.00 148.63 ?  38   THR C C   1 
ATOM   9287  O  O   . THR C 3  38   ? -81.133 -14.683  64.364  1.00 146.88 ?  38   THR C O   1 
ATOM   9288  C  CB  . THR C 3  38   ? -81.051 -11.748  63.263  1.00 142.40 ?  38   THR C CB  1 
ATOM   9289  O  OG1 . THR C 3  38   ? -80.189 -10.604  63.317  1.00 147.37 ?  38   THR C OG1 1 
ATOM   9290  C  CG2 . THR C 3  38   ? -82.380 -11.335  62.647  1.00 145.49 ?  38   THR C CG2 1 
ATOM   9291  N  N   . PRO C 3  39   ? -83.159 -13.848  64.837  1.00 135.96 ?  39   PRO C N   1 
ATOM   9292  C  CA  . PRO C 3  39   ? -83.774 -15.169  64.759  1.00 137.63 ?  39   PRO C CA  1 
ATOM   9293  C  C   . PRO C 3  39   ? -83.548 -15.787  63.393  1.00 139.31 ?  39   PRO C C   1 
ATOM   9294  O  O   . PRO C 3  39   ? -83.495 -15.076  62.371  1.00 136.34 ?  39   PRO C O   1 
ATOM   9295  C  CB  . PRO C 3  39   ? -85.260 -14.882  65.010  1.00 138.29 ?  39   PRO C CB  1 
ATOM   9296  C  CG  . PRO C 3  39   ? -85.264 -13.633  65.814  1.00 138.44 ?  39   PRO C CG  1 
ATOM   9297  C  CD  . PRO C 3  39   ? -84.105 -12.823  65.315  1.00 137.93 ?  39   PRO C CD  1 
ATOM   9298  N  N   . PRO C 3  40   ? -83.390 -17.112  63.329  1.00 129.80 ?  40   PRO C N   1 
ATOM   9299  C  CA  . PRO C 3  40   ? -83.111 -17.757  62.035  1.00 127.65 ?  40   PRO C CA  1 
ATOM   9300  C  C   . PRO C 3  40   ? -84.178 -17.504  60.988  1.00 130.34 ?  40   PRO C C   1 
ATOM   9301  O  O   . PRO C 3  40   ? -83.857 -17.431  59.795  1.00 130.37 ?  40   PRO C O   1 
ATOM   9302  C  CB  . PRO C 3  40   ? -83.022 -19.245  62.401  1.00 130.31 ?  40   PRO C CB  1 
ATOM   9303  C  CG  . PRO C 3  40   ? -82.639 -19.253  63.845  1.00 133.07 ?  40   PRO C CG  1 
ATOM   9304  C  CD  . PRO C 3  40   ? -83.338 -18.068  64.448  1.00 129.06 ?  40   PRO C CD  1 
ATOM   9305  N  N   . LEU C 3  41   ? -85.440 -17.363  61.396  1.00 132.18 ?  41   LEU C N   1 
ATOM   9306  C  CA  . LEU C 3  41   ? -86.510 -17.081  60.448  1.00 128.80 ?  41   LEU C CA  1 
ATOM   9307  C  C   . LEU C 3  41   ? -86.491 -15.642  59.952  1.00 131.64 ?  41   LEU C C   1 
ATOM   9308  O  O   . LEU C 3  41   ? -87.208 -15.326  58.996  1.00 130.19 ?  41   LEU C O   1 
ATOM   9309  C  CB  . LEU C 3  41   ? -87.869 -17.394  61.081  1.00 129.63 ?  41   LEU C CB  1 
ATOM   9310  C  CG  . LEU C 3  41   ? -88.367 -18.842  61.004  1.00 130.42 ?  41   LEU C CG  1 
ATOM   9311  C  CD1 . LEU C 3  41   ? -87.583 -19.751  61.943  1.00 133.63 ?  41   LEU C CD1 1 
ATOM   9312  C  CD2 . LEU C 3  41   ? -89.857 -18.913  61.306  1.00 117.29 ?  41   LEU C CD2 1 
ATOM   9313  N  N   . LYS C 3  42   ? -85.693 -14.768  60.569  1.00 145.71 ?  42   LYS C N   1 
ATOM   9314  C  CA  . LYS C 3  42   ? -85.604 -13.366  60.181  1.00 142.86 ?  42   LYS C CA  1 
ATOM   9315  C  C   . LYS C 3  42   ? -84.314 -13.061  59.425  1.00 132.91 ?  42   LYS C C   1 
ATOM   9316  O  O   . LYS C 3  42   ? -83.899 -11.900  59.353  1.00 129.86 ?  42   LYS C O   1 
ATOM   9317  C  CB  . LYS C 3  42   ? -85.724 -12.471  61.416  1.00 144.12 ?  42   LYS C CB  1 
ATOM   9318  C  CG  . LYS C 3  42   ? -86.336 -11.103  61.151  1.00 144.13 ?  42   LYS C CG  1 
ATOM   9319  C  CD  . LYS C 3  42   ? -87.854 -11.168  61.139  1.00 149.38 ?  42   LYS C CD  1 
ATOM   9320  C  CE  . LYS C 3  42   ? -88.397 -11.640  62.478  1.00 141.22 ?  42   LYS C CE  1 
ATOM   9321  N  NZ  . LYS C 3  42   ? -89.836 -12.012  62.395  1.00 146.96 ?  42   LYS C NZ  1 
ATOM   9322  N  N   . THR C 3  43   ? -83.671 -14.080  58.866  1.00 86.10  ?  43   THR C N   1 
ATOM   9323  C  CA  . THR C 3  43   ? -82.436 -13.869  58.120  1.00 72.18  ?  43   THR C CA  1 
ATOM   9324  C  C   . THR C 3  43   ? -82.738 -13.133  56.819  1.00 72.25  ?  43   THR C C   1 
ATOM   9325  O  O   . THR C 3  43   ? -83.689 -13.496  56.116  1.00 85.83  ?  43   THR C O   1 
ATOM   9326  C  CB  . THR C 3  43   ? -81.757 -15.207  57.826  1.00 70.83  ?  43   THR C CB  1 
ATOM   9327  O  OG1 . THR C 3  43   ? -81.438 -15.864  59.059  1.00 71.73  ?  43   THR C OG1 1 
ATOM   9328  C  CG2 . THR C 3  43   ? -80.479 -15.004  57.024  1.00 75.53  ?  43   THR C CG2 1 
ATOM   9329  N  N   . PRO C 3  44   ? -81.974 -12.097  56.470  1.00 103.09 ?  44   PRO C N   1 
ATOM   9330  C  CA  . PRO C 3  44   ? -82.223 -11.394  55.207  1.00 115.77 ?  44   PRO C CA  1 
ATOM   9331  C  C   . PRO C 3  44   ? -82.024 -12.311  54.008  1.00 115.88 ?  44   PRO C C   1 
ATOM   9332  O  O   . PRO C 3  44   ? -81.216 -13.242  54.034  1.00 116.86 ?  44   PRO C O   1 
ATOM   9333  C  CB  . PRO C 3  44   ? -81.195 -10.255  55.221  1.00 115.86 ?  44   PRO C CB  1 
ATOM   9334  C  CG  . PRO C 3  44   ? -80.156 -10.680  56.211  1.00 108.87 ?  44   PRO C CG  1 
ATOM   9335  C  CD  . PRO C 3  44   ? -80.890 -11.472  57.247  1.00 106.45 ?  44   PRO C CD  1 
ATOM   9336  N  N   . LYS C 3  45   ? -82.784 -12.033  52.946  1.00 100.58 ?  45   LYS C N   1 
ATOM   9337  C  CA  . LYS C 3  45   ? -82.746 -12.887  51.763  1.00 97.88  ?  45   LYS C CA  1 
ATOM   9338  C  C   . LYS C 3  45   ? -81.427 -12.762  51.013  1.00 102.67 ?  45   LYS C C   1 
ATOM   9339  O  O   . LYS C 3  45   ? -81.019 -13.702  50.322  1.00 101.84 ?  45   LYS C O   1 
ATOM   9340  C  CB  . LYS C 3  45   ? -83.917 -12.551  50.839  1.00 98.08  ?  45   LYS C CB  1 
ATOM   9341  C  CG  . LYS C 3  45   ? -85.282 -12.893  51.417  1.00 96.37  ?  45   LYS C CG  1 
ATOM   9342  C  CD  . LYS C 3  45   ? -86.382 -12.728  50.378  1.00 109.95 ?  45   LYS C CD  1 
ATOM   9343  C  CE  . LYS C 3  45   ? -86.106 -13.565  49.137  1.00 108.00 ?  45   LYS C CE  1 
ATOM   9344  N  NZ  . LYS C 3  45   ? -87.145 -13.374  48.086  1.00 66.53  ?  45   LYS C NZ  1 
ATOM   9345  N  N   . GLY C 3  46   ? -80.751 -11.616  51.130  1.00 138.97 ?  46   GLY C N   1 
ATOM   9346  C  CA  . GLY C 3  46   ? -79.472 -11.454  50.459  1.00 135.65 ?  46   GLY C CA  1 
ATOM   9347  C  C   . GLY C 3  46   ? -78.409 -12.392  50.997  1.00 128.17 ?  46   GLY C C   1 
ATOM   9348  O  O   . GLY C 3  46   ? -77.589 -12.916  50.239  1.00 124.39 ?  46   GLY C O   1 
ATOM   9349  N  N   . TRP C 3  47   ? -78.407 -12.614  52.314  1.00 102.90 ?  47   TRP C N   1 
ATOM   9350  C  CA  . TRP C 3  47   ? -77.483 -13.580  52.899  1.00 103.08 ?  47   TRP C CA  1 
ATOM   9351  C  C   . TRP C 3  47   ? -77.765 -14.986  52.387  1.00 106.51 ?  47   TRP C C   1 
ATOM   9352  O  O   . TRP C 3  47   ? -76.836 -15.764  52.138  1.00 106.75 ?  47   TRP C O   1 
ATOM   9353  C  CB  . TRP C 3  47   ? -77.574 -13.536  54.426  1.00 103.78 ?  47   TRP C CB  1 
ATOM   9354  C  CG  . TRP C 3  47   ? -76.530 -14.362  55.120  1.00 99.92  ?  47   TRP C CG  1 
ATOM   9355  C  CD1 . TRP C 3  47   ? -75.342 -13.922  55.628  1.00 96.88  ?  47   TRP C CD1 1 
ATOM   9356  C  CD2 . TRP C 3  47   ? -76.582 -15.770  55.386  1.00 98.13  ?  47   TRP C CD2 1 
ATOM   9357  N  NE1 . TRP C 3  47   ? -74.651 -14.968  56.191  1.00 95.43  ?  47   TRP C NE1 1 
ATOM   9358  C  CE2 . TRP C 3  47   ? -75.391 -16.114  56.055  1.00 96.90  ?  47   TRP C CE2 1 
ATOM   9359  C  CE3 . TRP C 3  47   ? -77.521 -16.773  55.123  1.00 96.25  ?  47   TRP C CE3 1 
ATOM   9360  C  CZ2 . TRP C 3  47   ? -75.113 -17.418  56.463  1.00 94.85  ?  47   TRP C CZ2 1 
ATOM   9361  C  CZ3 . TRP C 3  47   ? -77.243 -18.067  55.528  1.00 98.44  ?  47   TRP C CZ3 1 
ATOM   9362  C  CH2 . TRP C 3  47   ? -76.049 -18.377  56.191  1.00 94.91  ?  47   TRP C CH2 1 
ATOM   9363  N  N   . LEU C 3  48   ? -79.046 -15.330  52.223  1.00 103.31 ?  48   LEU C N   1 
ATOM   9364  C  CA  . LEU C 3  48   ? -79.403 -16.663  51.750  1.00 106.23 ?  48   LEU C CA  1 
ATOM   9365  C  C   . LEU C 3  48   ? -78.959 -16.878  50.308  1.00 105.85 ?  48   LEU C C   1 
ATOM   9366  O  O   . LEU C 3  48   ? -78.493 -17.966  49.951  1.00 106.15 ?  48   LEU C O   1 
ATOM   9367  C  CB  . LEU C 3  48   ? -80.910 -16.878  51.884  1.00 109.07 ?  48   LEU C CB  1 
ATOM   9368  C  CG  . LEU C 3  48   ? -81.496 -16.742  53.290  1.00 97.27  ?  48   LEU C CG  1 
ATOM   9369  C  CD1 . LEU C 3  48   ? -83.014 -16.679  53.232  1.00 114.17 ?  48   LEU C CD1 1 
ATOM   9370  C  CD2 . LEU C 3  48   ? -81.035 -17.885  54.181  1.00 86.70  ?  48   LEU C CD2 1 
ATOM   9371  N  N   . ALA C 3  49   ? -79.098 -15.852  49.465  1.00 94.03  ?  49   ALA C N   1 
ATOM   9372  C  CA  . ALA C 3  49   ? -78.665 -15.976  48.077  1.00 91.23  ?  49   ALA C CA  1 
ATOM   9373  C  C   . ALA C 3  49   ? -77.150 -16.097  47.981  1.00 92.75  ?  49   ALA C C   1 
ATOM   9374  O  O   . ALA C 3  49   ? -76.635 -16.911  47.205  1.00 91.58  ?  49   ALA C O   1 
ATOM   9375  C  CB  . ALA C 3  49   ? -79.162 -14.782  47.262  1.00 83.55  ?  49   ALA C CB  1 
ATOM   9376  N  N   . GLY C 3  50   ? -76.419 -15.300  48.762  1.00 119.70 ?  50   GLY C N   1 
ATOM   9377  C  CA  . GLY C 3  50   ? -74.969 -15.390  48.739  1.00 117.14 ?  50   GLY C CA  1 
ATOM   9378  C  C   . GLY C 3  50   ? -74.456 -16.708  49.287  1.00 117.92 ?  50   GLY C C   1 
ATOM   9379  O  O   . GLY C 3  50   ? -73.519 -17.295  48.740  1.00 114.97 ?  50   GLY C O   1 
ATOM   9380  N  N   . PHE C 3  51   ? -75.062 -17.192  50.375  1.00 141.88 ?  51   PHE C N   1 
ATOM   9381  C  CA  . PHE C 3  51   ? -74.658 -18.479  50.930  1.00 139.93 ?  51   PHE C CA  1 
ATOM   9382  C  C   . PHE C 3  51   ? -75.004 -19.628  49.992  1.00 138.57 ?  51   PHE C C   1 
ATOM   9383  O  O   . PHE C 3  51   ? -74.283 -20.632  49.953  1.00 144.62 ?  51   PHE C O   1 
ATOM   9384  C  CB  . PHE C 3  51   ? -75.311 -18.698  52.294  1.00 138.11 ?  51   PHE C CB  1 
ATOM   9385  C  CG  . PHE C 3  51   ? -74.913 -19.986  52.953  1.00 133.98 ?  51   PHE C CG  1 
ATOM   9386  C  CD1 . PHE C 3  51   ? -73.607 -20.192  53.366  1.00 129.81 ?  51   PHE C CD1 1 
ATOM   9387  C  CD2 . PHE C 3  51   ? -75.841 -20.994  53.152  1.00 138.15 ?  51   PHE C CD2 1 
ATOM   9388  C  CE1 . PHE C 3  51   ? -73.235 -21.378  53.970  1.00 131.46 ?  51   PHE C CE1 1 
ATOM   9389  C  CE2 . PHE C 3  51   ? -75.476 -22.182  53.755  1.00 143.20 ?  51   PHE C CE2 1 
ATOM   9390  C  CZ  . PHE C 3  51   ? -74.171 -22.374  54.165  1.00 133.87 ?  51   PHE C CZ  1 
ATOM   9391  N  N   . SER C 3  52   ? -76.097 -19.504  49.235  1.00 114.56 ?  52   SER C N   1 
ATOM   9392  C  CA  . SER C 3  52   ? -76.440 -20.535  48.262  1.00 117.41 ?  52   SER C CA  1 
ATOM   9393  C  C   . SER C 3  52   ? -75.418 -20.587  47.134  1.00 118.88 ?  52   SER C C   1 
ATOM   9394  O  O   . SER C 3  52   ? -75.024 -21.674  46.694  1.00 118.57 ?  52   SER C O   1 
ATOM   9395  C  CB  . SER C 3  52   ? -77.842 -20.287  47.706  1.00 114.38 ?  52   SER C CB  1 
ATOM   9396  O  OG  . SER C 3  52   ? -77.845 -19.199  46.798  1.00 121.69 ?  52   SER C OG  1 
ATOM   9397  N  N   . VAL C 3  53   ? -74.977 -19.422  46.653  1.00 108.59 ?  53   VAL C N   1 
ATOM   9398  C  CA  . VAL C 3  53   ? -73.939 -19.383  45.626  1.00 106.39 ?  53   VAL C CA  1 
ATOM   9399  C  C   . VAL C 3  53   ? -72.636 -19.954  46.170  1.00 108.68 ?  53   VAL C C   1 
ATOM   9400  O  O   . VAL C 3  53   ? -71.952 -20.735  45.496  1.00 103.98 ?  53   VAL C O   1 
ATOM   9401  C  CB  . VAL C 3  53   ? -73.757 -17.943  45.109  1.00 104.26 ?  53   VAL C CB  1 
ATOM   9402  C  CG1 . VAL C 3  53   ? -72.454 -17.810  44.333  1.00 101.03 ?  53   VAL C CG1 1 
ATOM   9403  C  CG2 . VAL C 3  53   ? -74.940 -17.536  44.247  1.00 101.75 ?  53   VAL C CG2 1 
ATOM   9404  N  N   . ALA C 3  54   ? -72.281 -19.587  47.403  1.00 118.22 ?  54   ALA C N   1 
ATOM   9405  C  CA  . ALA C 3  54   ? -71.041 -20.078  47.996  1.00 113.65 ?  54   ALA C CA  1 
ATOM   9406  C  C   . ALA C 3  54   ? -71.098 -21.581  48.244  1.00 114.28 ?  54   ALA C C   1 
ATOM   9407  O  O   . ALA C 3  54   ? -70.084 -22.276  48.108  1.00 112.28 ?  54   ALA C O   1 
ATOM   9408  C  CB  . ALA C 3  54   ? -70.750 -19.327  49.294  1.00 106.17 ?  54   ALA C CB  1 
ATOM   9409  N  N   . PHE C 3  55   ? -72.272 -22.103  48.608  1.00 110.55 ?  55   PHE C N   1 
ATOM   9410  C  CA  . PHE C 3  55   ? -72.394 -23.540  48.830  1.00 109.54 ?  55   PHE C CA  1 
ATOM   9411  C  C   . PHE C 3  55   ? -72.340 -24.308  47.515  1.00 107.67 ?  55   PHE C C   1 
ATOM   9412  O  O   . PHE C 3  55   ? -71.795 -25.416  47.461  1.00 103.08 ?  55   PHE C O   1 
ATOM   9413  C  CB  . PHE C 3  55   ? -73.686 -23.855  49.581  1.00 109.24 ?  55   PHE C CB  1 
ATOM   9414  C  CG  . PHE C 3  55   ? -73.736 -25.249  50.138  1.00 114.41 ?  55   PHE C CG  1 
ATOM   9415  C  CD1 . PHE C 3  55   ? -72.878 -25.634  51.156  1.00 107.68 ?  55   PHE C CD1 1 
ATOM   9416  C  CD2 . PHE C 3  55   ? -74.633 -26.177  49.637  1.00 111.37 ?  55   PHE C CD2 1 
ATOM   9417  C  CE1 . PHE C 3  55   ? -72.919 -26.917  51.669  1.00 108.36 ?  55   PHE C CE1 1 
ATOM   9418  C  CE2 . PHE C 3  55   ? -74.679 -27.462  50.146  1.00 117.15 ?  55   PHE C CE2 1 
ATOM   9419  C  CZ  . PHE C 3  55   ? -73.821 -27.832  51.163  1.00 114.60 ?  55   PHE C CZ  1 
ATOM   9420  N  N   . PHE C 3  56   ? -72.906 -23.739  46.447  1.00 100.14 ?  56   PHE C N   1 
ATOM   9421  C  CA  . PHE C 3  56   ? -72.817 -24.372  45.135  1.00 100.25 ?  56   PHE C CA  1 
ATOM   9422  C  C   . PHE C 3  56   ? -71.368 -24.481  44.680  1.00 101.19 ?  56   PHE C C   1 
ATOM   9423  O  O   . PHE C 3  56   ? -70.935 -25.529  44.185  1.00 97.46  ?  56   PHE C O   1 
ATOM   9424  C  CB  . PHE C 3  56   ? -73.642 -23.586  44.115  1.00 94.64  ?  56   PHE C CB  1 
ATOM   9425  C  CG  . PHE C 3  56   ? -73.459 -24.055  42.700  1.00 95.03  ?  56   PHE C CG  1 
ATOM   9426  C  CD1 . PHE C 3  56   ? -73.898 -25.309  42.308  1.00 99.94  ?  56   PHE C CD1 1 
ATOM   9427  C  CD2 . PHE C 3  56   ? -72.842 -23.242  41.763  1.00 95.18  ?  56   PHE C CD2 1 
ATOM   9428  C  CE1 . PHE C 3  56   ? -73.726 -25.742  41.006  1.00 100.78 ?  56   PHE C CE1 1 
ATOM   9429  C  CE2 . PHE C 3  56   ? -72.669 -23.669  40.461  1.00 98.39  ?  56   PHE C CE2 1 
ATOM   9430  C  CZ  . PHE C 3  56   ? -73.111 -24.920  40.082  1.00 101.00 ?  56   PHE C CZ  1 
ATOM   9431  N  N   . MET C 3  57   ? -70.599 -23.403  44.843  1.00 101.32 ?  57   MET C N   1 
ATOM   9432  C  CA  . MET C 3  57   ? -69.181 -23.448  44.505  1.00 93.96  ?  57   MET C CA  1 
ATOM   9433  C  C   . MET C 3  57   ? -68.414 -24.369  45.445  1.00 93.44  ?  57   MET C C   1 
ATOM   9434  O  O   . MET C 3  57   ? -67.373 -24.915  45.063  1.00 95.34  ?  57   MET C O   1 
ATOM   9435  C  CB  . MET C 3  57   ? -68.592 -22.040  44.538  1.00 95.70  ?  57   MET C CB  1 
ATOM   9436  C  CG  . MET C 3  57   ? -69.338 -21.026  43.686  1.00 96.74  ?  57   MET C CG  1 
ATOM   9437  S  SD  . MET C 3  57   ? -68.285 -19.668  43.145  1.00 105.73 ?  57   MET C SD  1 
ATOM   9438  C  CE  . MET C 3  57   ? -68.515 -18.505  44.487  1.00 107.42 ?  57   MET C CE  1 
ATOM   9439  N  N   . LEU C 3  58   ? -68.907 -24.548  46.674  1.00 81.15  ?  58   LEU C N   1 
ATOM   9440  C  CA  . LEU C 3  58   ? -68.278 -25.495  47.590  1.00 77.81  ?  58   LEU C CA  1 
ATOM   9441  C  C   . LEU C 3  58   ? -68.484 -26.929  47.120  1.00 79.20  ?  58   LEU C C   1 
ATOM   9442  O  O   . LEU C 3  58   ? -67.581 -27.764  47.245  1.00 79.39  ?  58   LEU C O   1 
ATOM   9443  C  CB  . LEU C 3  58   ? -68.826 -25.306  49.006  1.00 82.13  ?  58   LEU C CB  1 
ATOM   9444  C  CG  . LEU C 3  58   ? -68.270 -26.239  50.086  1.00 73.04  ?  58   LEU C CG  1 
ATOM   9445  C  CD1 . LEU C 3  58   ? -66.766 -26.062  50.238  1.00 65.89  ?  58   LEU C CD1 1 
ATOM   9446  C  CD2 . LEU C 3  58   ? -68.977 -26.017  51.414  1.00 63.80  ?  58   LEU C CD2 1 
ATOM   9447  N  N   . MET C 3  59   ? -69.667 -27.235  46.578  1.00 103.43 ?  59   MET C N   1 
ATOM   9448  C  CA  . MET C 3  59   ? -69.881 -28.550  45.982  1.00 104.45 ?  59   MET C CA  1 
ATOM   9449  C  C   . MET C 3  59   ? -69.003 -28.750  44.754  1.00 99.77  ?  59   MET C C   1 
ATOM   9450  O  O   . MET C 3  59   ? -68.561 -29.873  44.485  1.00 96.63  ?  59   MET C O   1 
ATOM   9451  C  CB  . MET C 3  59   ? -71.355 -28.737  45.620  1.00 98.23  ?  59   MET C CB  1 
ATOM   9452  C  CG  . MET C 3  59   ? -72.319 -28.448  46.758  1.00 106.71 ?  59   MET C CG  1 
ATOM   9453  S  SD  . MET C 3  59   ? -71.779 -29.150  48.329  1.00 132.49 ?  59   MET C SD  1 
ATOM   9454  C  CE  . MET C 3  59   ? -72.849 -30.581  48.448  1.00 120.77 ?  59   MET C CE  1 
ATOM   9455  N  N   . ILE C 3  60   ? -68.744 -27.678  44.001  1.00 73.24  ?  60   ILE C N   1 
ATOM   9456  C  CA  . ILE C 3  60   ? -67.786 -27.751  42.901  1.00 65.12  ?  60   ILE C CA  1 
ATOM   9457  C  C   . ILE C 3  60   ? -66.398 -28.077  43.437  1.00 63.98  ?  60   ILE C C   1 
ATOM   9458  O  O   . ILE C 3  60   ? -65.647 -28.855  42.835  1.00 62.55  ?  60   ILE C O   1 
ATOM   9459  C  CB  . ILE C 3  60   ? -67.796 -26.434  42.103  1.00 71.09  ?  60   ILE C CB  1 
ATOM   9460  C  CG1 . ILE C 3  60   ? -69.121 -26.275  41.354  1.00 75.29  ?  60   ILE C CG1 1 
ATOM   9461  C  CG2 . ILE C 3  60   ? -66.623 -26.378  41.133  1.00 60.49  ?  60   ILE C CG2 1 
ATOM   9462  C  CD1 . ILE C 3  60   ? -69.188 -25.038  40.487  1.00 77.34  ?  60   ILE C CD1 1 
ATOM   9463  N  N   . PHE C 3  61   ? -66.041 -27.492  44.584  1.00 82.89  ?  61   PHE C N   1 
ATOM   9464  C  CA  . PHE C 3  61   ? -64.762 -27.799  45.217  1.00 79.88  ?  61   PHE C CA  1 
ATOM   9465  C  C   . PHE C 3  61   ? -64.689 -29.264  45.625  1.00 82.44  ?  61   PHE C C   1 
ATOM   9466  O  O   . PHE C 3  61   ? -63.658 -29.920  45.434  1.00 78.71  ?  61   PHE C O   1 
ATOM   9467  C  CB  . PHE C 3  61   ? -64.555 -26.898  46.434  1.00 82.36  ?  61   PHE C CB  1 
ATOM   9468  C  CG  . PHE C 3  61   ? -63.323 -27.220  47.229  1.00 84.27  ?  61   PHE C CG  1 
ATOM   9469  C  CD1 . PHE C 3  61   ? -62.064 -26.929  46.730  1.00 77.29  ?  61   PHE C CD1 1 
ATOM   9470  C  CD2 . PHE C 3  61   ? -63.425 -27.813  48.477  1.00 83.44  ?  61   PHE C CD2 1 
ATOM   9471  C  CE1 . PHE C 3  61   ? -60.929 -27.222  47.462  1.00 80.21  ?  61   PHE C CE1 1 
ATOM   9472  C  CE2 . PHE C 3  61   ? -62.294 -28.111  49.212  1.00 76.57  ?  61   PHE C CE2 1 
ATOM   9473  C  CZ  . PHE C 3  61   ? -61.045 -27.815  48.704  1.00 78.96  ?  61   PHE C CZ  1 
ATOM   9474  N  N   . PHE C 3  62   ? -65.777 -29.794  46.189  1.00 95.07  ?  62   PHE C N   1 
ATOM   9475  C  CA  . PHE C 3  62   ? -65.778 -31.180  46.643  1.00 92.65  ?  62   PHE C CA  1 
ATOM   9476  C  C   . PHE C 3  62   ? -65.643 -32.143  45.471  1.00 88.55  ?  62   PHE C C   1 
ATOM   9477  O  O   . PHE C 3  62   ? -64.930 -33.149  45.566  1.00 87.75  ?  62   PHE C O   1 
ATOM   9478  C  CB  . PHE C 3  62   ? -67.053 -31.467  47.436  1.00 100.87 ?  62   PHE C CB  1 
ATOM   9479  C  CG  . PHE C 3  62   ? -67.002 -30.989  48.861  1.00 101.65 ?  62   PHE C CG  1 
ATOM   9480  C  CD1 . PHE C 3  62   ? -65.794 -30.892  49.533  1.00 100.29 ?  62   PHE C CD1 1 
ATOM   9481  C  CD2 . PHE C 3  62   ? -68.163 -30.629  49.526  1.00 102.12 ?  62   PHE C CD2 1 
ATOM   9482  C  CE1 . PHE C 3  62   ? -65.746 -30.450  50.842  1.00 97.43  ?  62   PHE C CE1 1 
ATOM   9483  C  CE2 . PHE C 3  62   ? -68.121 -30.186  50.834  1.00 101.17 ?  62   PHE C CE2 1 
ATOM   9484  C  CZ  . PHE C 3  62   ? -66.911 -30.096  51.493  1.00 94.89  ?  62   PHE C CZ  1 
ATOM   9485  N  N   . VAL C 3  63   ? -66.313 -31.847  44.354  1.00 67.14  ?  63   VAL C N   1 
ATOM   9486  C  CA  . VAL C 3  63   ? -66.208 -32.696  43.171  1.00 71.53  ?  63   VAL C CA  1 
ATOM   9487  C  C   . VAL C 3  63   ? -64.797 -32.642  42.597  1.00 65.97  ?  63   VAL C C   1 
ATOM   9488  O  O   . VAL C 3  63   ? -64.247 -33.663  42.166  1.00 68.64  ?  63   VAL C O   1 
ATOM   9489  C  CB  . VAL C 3  63   ? -67.263 -32.285  42.126  1.00 67.68  ?  63   VAL C CB  1 
ATOM   9490  C  CG1 . VAL C 3  63   ? -67.040 -33.023  40.812  1.00 46.33  ?  63   VAL C CG1 1 
ATOM   9491  C  CG2 . VAL C 3  63   ? -68.666 -32.549  42.656  1.00 75.44  ?  63   VAL C CG2 1 
ATOM   9492  N  N   . SER C 3  64   ? -64.187 -31.456  42.591  1.00 72.03  ?  64   SER C N   1 
ATOM   9493  C  CA  . SER C 3  64   ? -62.844 -31.314  42.036  1.00 73.69  ?  64   SER C CA  1 
ATOM   9494  C  C   . SER C 3  64   ? -61.819 -32.068  42.873  1.00 75.10  ?  64   SER C C   1 
ATOM   9495  O  O   . SER C 3  64   ? -60.963 -32.778  42.333  1.00 71.25  ?  64   SER C O   1 
ATOM   9496  C  CB  . SER C 3  64   ? -62.473 -29.835  41.938  1.00 77.26  ?  64   SER C CB  1 
ATOM   9497  O  OG  . SER C 3  64   ? -63.483 -29.107  41.267  1.00 82.35  ?  64   SER C OG  1 
ATOM   9498  N  N   . VAL C 3  65   ? -61.891 -31.923  44.198  1.00 79.07  ?  65   VAL C N   1 
ATOM   9499  C  CA  . VAL C 3  65   ? -60.938 -32.597  45.075  1.00 71.59  ?  65   VAL C CA  1 
ATOM   9500  C  C   . VAL C 3  65   ? -61.133 -34.106  45.019  1.00 69.23  ?  65   VAL C C   1 
ATOM   9501  O  O   . VAL C 3  65   ? -60.160 -34.871  45.002  1.00 68.42  ?  65   VAL C O   1 
ATOM   9502  C  CB  . VAL C 3  65   ? -61.066 -32.059  46.511  1.00 67.69  ?  65   VAL C CB  1 
ATOM   9503  C  CG1 . VAL C 3  65   ? -60.312 -32.949  47.488  1.00 62.07  ?  65   VAL C CG1 1 
ATOM   9504  C  CG2 . VAL C 3  65   ? -60.554 -30.633  46.586  1.00 64.44  ?  65   VAL C CG2 1 
ATOM   9505  N  N   . THR C 3  66   ? -62.388 -34.558  44.982  1.00 76.19  ?  66   THR C N   1 
ATOM   9506  C  CA  . THR C 3  66   ? -62.659 -35.991  44.920  1.00 81.00  ?  66   THR C CA  1 
ATOM   9507  C  C   . THR C 3  66   ? -62.072 -36.605  43.655  1.00 81.73  ?  66   THR C C   1 
ATOM   9508  O  O   . THR C 3  66   ? -61.421 -37.655  43.704  1.00 80.83  ?  66   THR C O   1 
ATOM   9509  C  CB  . THR C 3  66   ? -64.166 -36.247  44.992  1.00 84.76  ?  66   THR C CB  1 
ATOM   9510  O  OG1 . THR C 3  66   ? -64.682 -35.727  46.224  1.00 89.68  ?  66   THR C OG1 1 
ATOM   9511  C  CG2 . THR C 3  66   ? -64.457 -37.740  44.920  1.00 74.38  ?  66   THR C CG2 1 
ATOM   9512  N  N   . TRP C 3  67   ? -62.282 -35.954  42.507  1.00 79.37  ?  67   TRP C N   1 
ATOM   9513  C  CA  . TRP C 3  67   ? -61.728 -36.472  41.261  1.00 75.19  ?  67   TRP C CA  1 
ATOM   9514  C  C   . TRP C 3  67   ? -60.209 -36.367  41.232  1.00 76.45  ?  67   TRP C C   1 
ATOM   9515  O  O   . TRP C 3  67   ? -59.542 -37.226  40.644  1.00 81.99  ?  67   TRP C O   1 
ATOM   9516  C  CB  . TRP C 3  67   ? -62.327 -35.729  40.068  1.00 83.09  ?  67   TRP C CB  1 
ATOM   9517  C  CG  . TRP C 3  67   ? -61.893 -36.291  38.749  1.00 83.18  ?  67   TRP C CG  1 
ATOM   9518  C  CD1 . TRP C 3  67   ? -61.219 -35.635  37.762  1.00 80.32  ?  67   TRP C CD1 1 
ATOM   9519  C  CD2 . TRP C 3  67   ? -62.107 -37.625  38.271  1.00 88.72  ?  67   TRP C CD2 1 
ATOM   9520  N  NE1 . TRP C 3  67   ? -60.996 -36.477  36.700  1.00 84.47  ?  67   TRP C NE1 1 
ATOM   9521  C  CE2 . TRP C 3  67   ? -61.532 -37.705  36.987  1.00 90.82  ?  67   TRP C CE2 1 
ATOM   9522  C  CE3 . TRP C 3  67   ? -62.728 -38.760  38.803  1.00 78.36  ?  67   TRP C CE3 1 
ATOM   9523  C  CZ2 . TRP C 3  67   ? -61.559 -38.872  36.227  1.00 80.81  ?  67   TRP C CZ2 1 
ATOM   9524  C  CZ3 . TRP C 3  67   ? -62.753 -39.918  38.047  1.00 79.96  ?  67   TRP C CZ3 1 
ATOM   9525  C  CH2 . TRP C 3  67   ? -62.172 -39.965  36.773  1.00 74.08  ?  67   TRP C CH2 1 
ATOM   9526  N  N   . LEU C 3  68   ? -59.647 -35.325  41.847  1.00 61.67  ?  68   LEU C N   1 
ATOM   9527  C  CA  . LEU C 3  68   ? -58.195 -35.207  41.911  1.00 58.89  ?  68   LEU C CA  1 
ATOM   9528  C  C   . LEU C 3  68   ? -57.589 -36.323  42.752  1.00 58.98  ?  68   LEU C C   1 
ATOM   9529  O  O   . LEU C 3  68   ? -56.511 -36.835  42.431  1.00 57.80  ?  68   LEU C O   1 
ATOM   9530  C  CB  . LEU C 3  68   ? -57.800 -33.840  42.467  1.00 60.35  ?  68   LEU C CB  1 
ATOM   9531  C  CG  . LEU C 3  68   ? -56.356 -33.677  42.945  1.00 57.95  ?  68   LEU C CG  1 
ATOM   9532  C  CD1 . LEU C 3  68   ? -55.408 -33.577  41.763  1.00 53.62  ?  68   LEU C CD1 1 
ATOM   9533  C  CD2 . LEU C 3  68   ? -56.217 -32.459  43.852  1.00 60.68  ?  68   LEU C CD2 1 
ATOM   9534  N  N   . PHE C 3  69   ? -58.270 -36.712  43.832  1.00 81.72  ?  69   PHE C N   1 
ATOM   9535  C  CA  . PHE C 3  69   ? -57.775 -37.804  44.663  1.00 82.77  ?  69   PHE C CA  1 
ATOM   9536  C  C   . PHE C 3  69   ? -57.921 -39.147  43.957  1.00 75.37  ?  69   PHE C C   1 
ATOM   9537  O  O   . PHE C 3  69   ? -57.051 -40.017  44.079  1.00 70.79  ?  69   PHE C O   1 
ATOM   9538  C  CB  . PHE C 3  69   ? -58.515 -37.821  46.002  1.00 83.26  ?  69   PHE C CB  1 
ATOM   9539  C  CG  . PHE C 3  69   ? -58.015 -36.803  46.989  1.00 84.60  ?  69   PHE C CG  1 
ATOM   9540  C  CD1 . PHE C 3  69   ? -56.832 -36.119  46.764  1.00 88.46  ?  69   PHE C CD1 1 
ATOM   9541  C  CD2 . PHE C 3  69   ? -58.732 -36.527  48.142  1.00 88.81  ?  69   PHE C CD2 1 
ATOM   9542  C  CE1 . PHE C 3  69   ? -56.373 -35.182  47.670  1.00 85.42  ?  69   PHE C CE1 1 
ATOM   9543  C  CE2 . PHE C 3  69   ? -58.279 -35.590  49.052  1.00 89.74  ?  69   PHE C CE2 1 
ATOM   9544  C  CZ  . PHE C 3  69   ? -57.097 -34.917  48.816  1.00 83.95  ?  69   PHE C CZ  1 
ATOM   9545  N  N   . ILE C 3  70   ? -59.013 -39.331  43.212  1.00 55.89  ?  70   ILE C N   1 
ATOM   9546  C  CA  . ILE C 3  70   ? -59.267 -40.614  42.562  1.00 56.84  ?  70   ILE C CA  1 
ATOM   9547  C  C   . ILE C 3  70   ? -58.283 -40.842  41.421  1.00 62.92  ?  70   ILE C C   1 
ATOM   9548  O  O   . ILE C 3  70   ? -57.651 -41.901  41.326  1.00 60.20  ?  70   ILE C O   1 
ATOM   9549  C  CB  . ILE C 3  70   ? -60.725 -40.689  42.072  1.00 54.71  ?  70   ILE C CB  1 
ATOM   9550  C  CG1 . ILE C 3  70   ? -61.683 -40.813  43.257  1.00 51.49  ?  70   ILE C CG1 1 
ATOM   9551  C  CG2 . ILE C 3  70   ? -60.912 -41.852  41.113  1.00 51.25  ?  70   ILE C CG2 1 
ATOM   9552  C  CD1 . ILE C 3  70   ? -63.145 -40.774  42.866  1.00 53.15  ?  70   ILE C CD1 1 
ATOM   9553  N  N   . ARG C 3  71   ? -58.137 -39.854  40.539  1.00 69.69  ?  71   ARG C N   1 
ATOM   9554  C  CA  . ARG C 3  71   ? -57.306 -40.011  39.349  1.00 64.26  ?  71   ARG C CA  1 
ATOM   9555  C  C   . ARG C 3  71   ? -55.851 -39.624  39.610  1.00 64.19  ?  71   ARG C C   1 
ATOM   9556  O  O   . ARG C 3  71   ? -54.940 -40.423  39.374  1.00 61.94  ?  71   ARG C O   1 
ATOM   9557  C  CB  . ARG C 3  71   ? -57.882 -39.185  38.194  1.00 66.66  ?  71   ARG C CB  1 
ATOM   9558  C  CG  . ARG C 3  71   ? -57.172 -39.407  36.871  1.00 75.41  ?  71   ARG C CG  1 
ATOM   9559  C  CD  . ARG C 3  71   ? -57.530 -40.755  36.269  1.00 80.92  ?  71   ARG C CD  1 
ATOM   9560  N  NE  . ARG C 3  71   ? -56.740 -41.038  35.077  1.00 86.85  ?  71   ARG C NE  1 
ATOM   9561  C  CZ  . ARG C 3  71   ? -57.028 -40.588  33.863  1.00 94.86  ?  71   ARG C CZ  1 
ATOM   9562  N  NH1 . ARG C 3  71   ? -58.089 -39.831  33.640  1.00 97.84  ?  71   ARG C NH1 1 
ATOM   9563  N  NH2 . ARG C 3  71   ? -56.229 -40.905  32.848  1.00 102.04 ?  71   ARG C NH2 1 
ATOM   9564  N  N   . GLY C 3  72   ? -55.620 -38.403  40.086  1.00 58.73  ?  72   GLY C N   1 
ATOM   9565  C  CA  . GLY C 3  72   ? -54.270 -37.944  40.353  1.00 58.95  ?  72   GLY C CA  1 
ATOM   9566  C  C   . GLY C 3  72   ? -54.014 -36.536  39.859  1.00 53.31  ?  72   GLY C C   1 
ATOM   9567  O  O   . GLY C 3  72   ? -54.881 -35.930  39.222  1.00 62.40  ?  72   GLY C O   1 
ATOM   9568  N  N   . VAL C 3  73   ? -52.821 -36.010  40.133  1.00 54.28  ?  73   VAL C N   1 
ATOM   9569  C  CA  . VAL C 3  73   ? -52.474 -34.643  39.757  1.00 59.53  ?  73   VAL C CA  1 
ATOM   9570  C  C   . VAL C 3  73   ? -52.240 -34.552  38.255  1.00 67.24  ?  73   VAL C C   1 
ATOM   9571  O  O   . VAL C 3  73   ? -51.995 -33.464  37.721  1.00 72.83  ?  73   VAL C O   1 
ATOM   9572  C  CB  . VAL C 3  73   ? -51.244 -34.141  40.536  1.00 58.97  ?  73   VAL C CB  1 
ATOM   9573  C  CG1 . VAL C 3  73   ? -51.566 -34.032  42.015  1.00 62.16  ?  73   VAL C CG1 1 
ATOM   9574  C  CG2 . VAL C 3  73   ? -50.054 -35.060  40.306  1.00 59.13  ?  73   VAL C CG2 1 
ATOM   9575  N  N   . GLY C 3  74   ? -52.313 -35.689  37.563  1.00 94.84  ?  74   GLY C N   1 
ATOM   9576  C  CA  . GLY C 3  74   ? -52.215 -35.687  36.115  1.00 99.39  ?  74   GLY C CA  1 
ATOM   9577  C  C   . GLY C 3  74   ? -53.416 -35.099  35.405  1.00 94.37  ?  74   GLY C C   1 
ATOM   9578  O  O   . GLY C 3  74   ? -53.351 -34.891  34.189  1.00 84.95  ?  74   GLY C O   1 
ATOM   9579  N  N   . ILE C 3  75   ? -54.506 -34.830  36.130  1.00 83.47  ?  75   ILE C N   1 
ATOM   9580  C  CA  . ILE C 3  75   ? -55.670 -34.201  35.518  1.00 85.86  ?  75   ILE C CA  1 
ATOM   9581  C  C   . ILE C 3  75   ? -55.415 -32.733  35.215  1.00 85.34  ?  75   ILE C C   1 
ATOM   9582  O  O   . ILE C 3  75   ? -56.145 -32.133  34.417  1.00 89.82  ?  75   ILE C O   1 
ATOM   9583  C  CB  . ILE C 3  75   ? -56.911 -34.354  36.418  1.00 90.69  ?  75   ILE C CB  1 
ATOM   9584  C  CG1 . ILE C 3  75   ? -56.718 -33.597  37.732  1.00 77.80  ?  75   ILE C CG1 1 
ATOM   9585  C  CG2 . ILE C 3  75   ? -57.194 -35.820  36.688  1.00 86.56  ?  75   ILE C CG2 1 
ATOM   9586  C  CD1 . ILE C 3  75   ? -57.943 -33.599  38.619  1.00 73.35  ?  75   ILE C CD1 1 
ATOM   9587  N  N   . TRP C 3  76   ? -54.398 -32.137  35.831  1.00 83.79  ?  76   TRP C N   1 
ATOM   9588  C  CA  . TRP C 3  76   ? -54.035 -30.753  35.560  1.00 97.94  ?  76   TRP C CA  1 
ATOM   9589  C  C   . TRP C 3  76   ? -53.222 -30.687  34.268  1.00 93.22  ?  76   TRP C C   1 
ATOM   9590  O  O   . TRP C 3  76   ? -53.099 -31.668  33.529  1.00 95.12  ?  76   TRP C O   1 
ATOM   9591  C  CB  . TRP C 3  76   ? -53.280 -30.163  36.748  1.00 98.17  ?  76   TRP C CB  1 
ATOM   9592  C  CG  . TRP C 3  76   ? -54.078 -30.135  38.016  1.00 96.17  ?  76   TRP C CG  1 
ATOM   9593  C  CD1 . TRP C 3  76   ? -55.438 -30.128  38.131  1.00 90.91  ?  76   TRP C CD1 1 
ATOM   9594  C  CD2 . TRP C 3  76   ? -53.563 -30.113  39.352  1.00 86.99  ?  76   TRP C CD2 1 
ATOM   9595  N  NE1 . TRP C 3  76   ? -55.801 -30.102  39.456  1.00 87.52  ?  76   TRP C NE1 1 
ATOM   9596  C  CE2 . TRP C 3  76   ? -54.668 -30.092  40.226  1.00 86.97  ?  76   TRP C CE2 1 
ATOM   9597  C  CE3 . TRP C 3  76   ? -52.274 -30.109  39.894  1.00 83.58  ?  76   TRP C CE3 1 
ATOM   9598  C  CZ2 . TRP C 3  76   ? -54.523 -30.068  41.610  1.00 85.30  ?  76   TRP C CZ2 1 
ATOM   9599  C  CZ3 . TRP C 3  76   ? -52.133 -30.086  41.269  1.00 80.24  ?  76   TRP C CZ3 1 
ATOM   9600  C  CH2 . TRP C 3  76   ? -53.251 -30.064  42.111  1.00 78.78  ?  76   TRP C CH2 1 
ATOM   9601  N  N   . GLY C 3  77   ? -52.654 -29.519  33.978  1.00 67.39  ?  77   GLY C N   1 
ATOM   9602  C  CA  . GLY C 3  77   ? -51.885 -29.344  32.762  1.00 65.99  ?  77   GLY C CA  1 
ATOM   9603  C  C   . GLY C 3  77   ? -50.388 -29.330  32.992  1.00 69.18  ?  77   GLY C C   1 
ATOM   9604  O  O   . GLY C 3  77   ? -49.623 -28.919  32.115  1.00 70.84  ?  77   GLY C O   1 
ATOM   9605  N  N   . ILE C 3  78   ? -49.957 -29.780  34.171  1.00 81.48  ?  78   ILE C N   1 
ATOM   9606  C  CA  . ILE C 3  78   ? -48.539 -29.770  34.504  1.00 79.68  ?  78   ILE C CA  1 
ATOM   9607  C  C   . ILE C 3  78   ? -47.811 -30.851  33.717  1.00 76.36  ?  78   ILE C C   1 
ATOM   9608  O  O   . ILE C 3  78   ? -48.344 -31.944  33.480  1.00 73.44  ?  78   ILE C O   1 
ATOM   9609  C  CB  . ILE C 3  78   ? -48.347 -29.949  36.020  1.00 71.95  ?  78   ILE C CB  1 
ATOM   9610  C  CG1 . ILE C 3  78   ? -49.081 -31.199  36.510  1.00 77.11  ?  78   ILE C CG1 1 
ATOM   9611  C  CG2 . ILE C 3  78   ? -48.836 -28.717  36.764  1.00 75.24  ?  78   ILE C CG2 1 
ATOM   9612  C  CD1 . ILE C 3  78   ? -49.008 -31.404  38.008  1.00 75.62  ?  78   ILE C CD1 1 
ATOM   9613  N  N   . ASN C 3  79   ? -46.587 -30.547  33.301  1.00 84.49  ?  79   ASN C N   1 
ATOM   9614  C  CA  . ASN C 3  79   ? -45.780 -31.476  32.518  1.00 80.81  ?  79   ASN C CA  1 
ATOM   9615  C  C   . ASN C 3  79   ? -44.391 -31.553  33.148  1.00 77.13  ?  79   ASN C C   1 
ATOM   9616  O  O   . ASN C 3  79   ? -44.191 -31.265  34.334  1.00 71.94  ?  79   ASN C O   1 
ATOM   9617  C  CB  . ASN C 3  79   ? -45.732 -31.047  31.046  1.00 77.93  ?  79   ASN C CB  1 
ATOM   9618  C  CG  . ASN C 3  79   ? -45.442 -29.569  30.880  1.00 78.10  ?  79   ASN C CG  1 
ATOM   9619  O  OD1 . ASN C 3  79   ? -45.183 -28.862  31.852  1.00 83.96  ?  79   ASN C OD1 1 
ATOM   9620  N  ND2 . ASN C 3  79   ? -45.485 -29.095  29.641  1.00 82.94  ?  79   ASN C ND2 1 
ATOM   9621  N  N   . ILE C 3  80   ? -43.404 -31.936  32.346  1.00 90.55  ?  80   ILE C N   1 
ATOM   9622  C  CA  . ILE C 3  80   ? -42.041 -32.125  32.835  1.00 90.10  ?  80   ILE C CA  1 
ATOM   9623  C  C   . ILE C 3  80   ? -41.340 -30.778  33.007  1.00 103.19 ?  80   ILE C C   1 
ATOM   9624  O  O   . ILE C 3  80   ? -40.780 -30.527  34.085  1.00 111.30 ?  80   ILE C O   1 
ATOM   9625  C  CB  . ILE C 3  80   ? -41.245 -33.062  31.911  1.00 91.46  ?  80   ILE C CB  1 
ATOM   9626  C  CG1 . ILE C 3  80   ? -41.767 -34.493  32.032  1.00 98.34  ?  80   ILE C CG1 1 
ATOM   9627  C  CG2 . ILE C 3  80   ? -39.761 -33.011  32.242  1.00 87.83  ?  80   ILE C CG2 1 
ATOM   9628  C  CD1 . ILE C 3  80   ? -41.880 -34.983  33.461  1.00 83.59  ?  80   ILE C CD1 1 
ATOM   9629  N  N   . PRO C 3  81   ? -41.329 -29.867  31.995  1.00 73.48  ?  81   PRO C N   1 
ATOM   9630  C  CA  . PRO C 3  81   ? -40.664 -28.572  32.210  1.00 66.24  ?  81   PRO C CA  1 
ATOM   9631  C  C   . PRO C 3  81   ? -41.401 -27.704  33.218  1.00 72.26  ?  81   PRO C C   1 
ATOM   9632  O  O   . PRO C 3  81   ? -40.807 -27.205  34.179  1.00 80.82  ?  81   PRO C O   1 
ATOM   9633  C  CB  . PRO C 3  81   ? -40.658 -27.937  30.812  1.00 57.41  ?  81   PRO C CB  1 
ATOM   9634  C  CG  . PRO C 3  81   ? -41.768 -28.595  30.089  1.00 67.33  ?  81   PRO C CG  1 
ATOM   9635  C  CD  . PRO C 3  81   ? -41.832 -29.992  30.612  1.00 61.70  ?  81   PRO C CD  1 
ATOM   9636  N  N   . VAL C 3  82   ? -42.705 -27.521  33.009  1.00 60.62  ?  82   VAL C N   1 
ATOM   9637  C  CA  . VAL C 3  82   ? -43.543 -26.772  33.944  1.00 65.30  ?  82   VAL C CA  1 
ATOM   9638  C  C   . VAL C 3  82   ? -44.154 -27.711  34.984  1.00 59.58  ?  82   VAL C C   1 
ATOM   9639  O  O   . VAL C 3  82   ? -45.322 -28.098  34.875  1.00 50.56  ?  82   VAL C O   1 
ATOM   9640  C  CB  . VAL C 3  82   ? -44.651 -25.992  33.208  1.00 70.28  ?  82   VAL C CB  1 
ATOM   9641  C  CG1 . VAL C 3  82   ? -45.351 -25.063  34.179  1.00 65.27  ?  82   VAL C CG1 1 
ATOM   9642  C  CG2 . VAL C 3  82   ? -44.082 -25.239  32.023  1.00 66.83  ?  82   VAL C CG2 1 
ATOM   9643  N  N   . GLY C 3  83   ? -43.383 -28.061  36.012  1.00 81.26  ?  83   GLY C N   1 
ATOM   9644  C  CA  . GLY C 3  83   ? -43.899 -28.905  37.070  1.00 81.46  ?  83   GLY C CA  1 
ATOM   9645  C  C   . GLY C 3  83   ? -44.781 -28.208  38.088  1.00 77.90  ?  83   GLY C C   1 
ATOM   9646  O  O   . GLY C 3  83   ? -45.409 -28.871  38.924  1.00 79.84  ?  83   GLY C O   1 
ATOM   9647  N  N   . TRP C 3  84   ? -44.840 -26.882  38.036  1.00 67.85  ?  84   TRP C N   1 
ATOM   9648  C  CA  . TRP C 3  84   ? -45.658 -26.079  38.936  1.00 68.41  ?  84   TRP C CA  1 
ATOM   9649  C  C   . TRP C 3  84   ? -46.577 -25.212  38.086  1.00 71.32  ?  84   TRP C C   1 
ATOM   9650  O  O   . TRP C 3  84   ? -46.107 -24.321  37.370  1.00 74.52  ?  84   TRP C O   1 
ATOM   9651  C  CB  . TRP C 3  84   ? -44.782 -25.225  39.851  1.00 68.62  ?  84   TRP C CB  1 
ATOM   9652  C  CG  . TRP C 3  84   ? -44.329 -25.946  41.077  1.00 66.06  ?  84   TRP C CG  1 
ATOM   9653  C  CD1 . TRP C 3  84   ? -44.539 -27.258  41.382  1.00 66.96  ?  84   TRP C CD1 1 
ATOM   9654  C  CD2 . TRP C 3  84   ? -43.609 -25.388  42.181  1.00 66.25  ?  84   TRP C CD2 1 
ATOM   9655  N  NE1 . TRP C 3  84   ? -43.979 -27.557  42.599  1.00 71.53  ?  84   TRP C NE1 1 
ATOM   9656  C  CE2 . TRP C 3  84   ? -43.405 -26.424  43.112  1.00 66.90  ?  84   TRP C CE2 1 
ATOM   9657  C  CE3 . TRP C 3  84   ? -43.114 -24.114  42.470  1.00 67.27  ?  84   TRP C CE3 1 
ATOM   9658  C  CZ2 . TRP C 3  84   ? -42.728 -26.225  44.310  1.00 66.37  ?  84   TRP C CZ2 1 
ATOM   9659  C  CZ3 . TRP C 3  84   ? -42.441 -23.919  43.658  1.00 60.80  ?  84   TRP C CZ3 1 
ATOM   9660  C  CH2 . TRP C 3  84   ? -42.254 -24.969  44.564  1.00 67.25  ?  84   TRP C CH2 1 
ATOM   9661  N  N   . GLY C 3  85   ? -47.879 -25.477  38.159  1.00 83.90  ?  85   GLY C N   1 
ATOM   9662  C  CA  . GLY C 3  85   ? -48.855 -24.716  37.404  1.00 88.23  ?  85   GLY C CA  1 
ATOM   9663  C  C   . GLY C 3  85   ? -49.702 -23.815  38.278  1.00 87.25  ?  85   GLY C C   1 
ATOM   9664  O  O   . GLY C 3  85   ? -49.180 -23.170  39.192  1.00 88.54  ?  85   GLY C O   1 
ATOM   9665  N  N   . MET C 3  86   ? -51.012 -23.760  38.014  1.00 77.85  ?  86   MET C N   1 
ATOM   9666  C  CA  . MET C 3  86   ? -51.899 -22.935  38.829  1.00 79.40  ?  86   MET C CA  1 
ATOM   9667  C  C   . MET C 3  86   ? -52.039 -23.467  40.247  1.00 77.91  ?  86   MET C C   1 
ATOM   9668  O  O   . MET C 3  86   ? -52.499 -22.733  41.128  1.00 84.25  ?  86   MET C O   1 
ATOM   9669  C  CB  . MET C 3  86   ? -53.284 -22.837  38.188  1.00 83.64  ?  86   MET C CB  1 
ATOM   9670  C  CG  . MET C 3  86   ? -53.336 -22.040  36.896  1.00 84.98  ?  86   MET C CG  1 
ATOM   9671  S  SD  . MET C 3  86   ? -54.873 -22.307  35.987  1.00 93.65  ?  86   MET C SD  1 
ATOM   9672  C  CE  . MET C 3  86   ? -55.992 -22.741  37.316  1.00 74.51  ?  86   MET C CE  1 
ATOM   9673  N  N   . ASP C 3  87   ? -51.661 -24.728  40.481  1.00 91.86  ?  87   ASP C N   1 
ATOM   9674  C  CA  . ASP C 3  87   ? -51.694 -25.282  41.828  1.00 90.19  ?  87   ASP C CA  1 
ATOM   9675  C  C   . ASP C 3  87   ? -50.768 -24.515  42.766  1.00 87.03  ?  87   ASP C C   1 
ATOM   9676  O  O   . ASP C 3  87   ? -50.960 -24.550  43.980  1.00 88.19  ?  87   ASP C O   1 
ATOM   9677  C  CB  . ASP C 3  87   ? -51.318 -26.767  41.796  1.00 88.74  ?  87   ASP C CB  1 
ATOM   9678  C  CG  . ASP C 3  87   ? -49.962 -27.016  41.167  1.00 93.93  ?  87   ASP C CG  1 
ATOM   9679  O  OD1 . ASP C 3  87   ? -49.349 -26.049  40.673  1.00 90.41  ?  87   ASP C OD1 1 
ATOM   9680  O  OD2 . ASP C 3  87   ? -49.510 -28.182  41.169  1.00 89.83  -1 87   ASP C OD2 1 
ATOM   9681  N  N   . ILE C 3  88   ? -49.774 -23.822  42.222  1.00 65.91  ?  88   ILE C N   1 
ATOM   9682  C  CA  . ILE C 3  88   ? -48.913 -22.958  43.005  1.00 67.08  ?  88   ILE C CA  1 
ATOM   9683  C  C   . ILE C 3  88   ? -49.290 -21.485  42.853  1.00 69.75  ?  88   ILE C C   1 
ATOM   9684  O  O   . ILE C 3  88   ? -49.179 -20.724  43.824  1.00 69.76  ?  88   ILE C O   1 
ATOM   9685  C  CB  . ILE C 3  88   ? -47.421 -23.189  42.666  1.00 66.70  ?  88   ILE C CB  1 
ATOM   9686  C  CG1 . ILE C 3  88   ? -47.026 -24.653  42.904  1.00 65.43  ?  88   ILE C CG1 1 
ATOM   9687  C  CG2 . ILE C 3  88   ? -46.555 -22.283  43.494  1.00 57.94  ?  88   ILE C CG2 1 
ATOM   9688  C  CD1 . ILE C 3  88   ? -47.023 -25.029  44.401  1.00 62.54  ?  88   ILE C CD1 1 
ATOM   9689  N  N   . ILE C 3  89   ? -49.817 -21.083  41.691  1.00 68.32  ?  89   ILE C N   1 
ATOM   9690  C  CA  . ILE C 3  89   ? -50.216 -19.691  41.469  1.00 71.91  ?  89   ILE C CA  1 
ATOM   9691  C  C   . ILE C 3  89   ? -51.340 -19.301  42.418  1.00 73.23  ?  89   ILE C C   1 
ATOM   9692  O  O   . ILE C 3  89   ? -51.268 -18.278  43.111  1.00 84.02  ?  89   ILE C O   1 
ATOM   9693  C  CB  . ILE C 3  89   ? -50.629 -19.484  39.997  1.00 69.21  ?  89   ILE C CB  1 
ATOM   9694  C  CG1 . ILE C 3  89   ? -49.441 -19.765  39.085  1.00 68.06  ?  89   ILE C CG1 1 
ATOM   9695  C  CG2 . ILE C 3  89   ? -51.203 -18.063  39.729  1.00 61.71  ?  89   ILE C CG2 1 
ATOM   9696  C  CD1 . ILE C 3  89   ? -49.795 -19.877  37.624  1.00 64.10  ?  89   ILE C CD1 1 
ATOM   9697  N  N   . ASN C 3  90   ? -52.418 -20.092  42.425  1.00 84.37  ?  90   ASN C N   1 
ATOM   9698  C  CA  . ASN C 3  90   ? -53.538 -19.839  43.326  1.00 84.71  ?  90   ASN C CA  1 
ATOM   9699  C  C   . ASN C 3  90   ? -53.110 -19.915  44.785  1.00 90.75  ?  90   ASN C C   1 
ATOM   9700  O  O   . ASN C 3  90   ? -53.689 -19.232  45.637  1.00 93.20  ?  90   ASN C O   1 
ATOM   9701  C  CB  . ASN C 3  90   ? -54.668 -20.835  43.052  1.00 98.24  ?  90   ASN C CB  1 
ATOM   9702  C  CG  . ASN C 3  90   ? -55.031 -20.918  41.578  1.00 98.31  ?  90   ASN C CG  1 
ATOM   9703  O  OD1 . ASN C 3  90   ? -54.628 -20.074  40.777  1.00 83.49  ?  90   ASN C OD1 1 
ATOM   9704  N  ND2 . ASN C 3  90   ? -55.827 -21.922  41.221  1.00 95.31  ?  90   ASN C ND2 1 
ATOM   9705  N  N   . PHE C 3  91   ? -52.106 -20.738  45.092  1.00 79.91  ?  91   PHE C N   1 
ATOM   9706  C  CA  . PHE C 3  91   ? -51.600 -20.816  46.458  1.00 75.62  ?  91   PHE C CA  1 
ATOM   9707  C  C   . PHE C 3  91   ? -50.946 -19.503  46.875  1.00 73.91  ?  91   PHE C C   1 
ATOM   9708  O  O   . PHE C 3  91   ? -51.237 -18.966  47.950  1.00 85.63  ?  91   PHE C O   1 
ATOM   9709  C  CB  . PHE C 3  91   ? -50.615 -21.978  46.585  1.00 73.45  ?  91   PHE C CB  1 
ATOM   9710  C  CG  . PHE C 3  91   ? -49.749 -21.908  47.809  1.00 73.52  ?  91   PHE C CG  1 
ATOM   9711  C  CD1 . PHE C 3  91   ? -50.286 -22.121  49.068  1.00 75.13  ?  91   PHE C CD1 1 
ATOM   9712  C  CD2 . PHE C 3  91   ? -48.396 -21.631  47.701  1.00 70.15  ?  91   PHE C CD2 1 
ATOM   9713  C  CE1 . PHE C 3  91   ? -49.490 -22.057  50.197  1.00 78.18  ?  91   PHE C CE1 1 
ATOM   9714  C  CE2 . PHE C 3  91   ? -47.594 -21.565  48.825  1.00 72.89  ?  91   PHE C CE2 1 
ATOM   9715  C  CZ  . PHE C 3  91   ? -48.142 -21.779  50.075  1.00 75.27  ?  91   PHE C CZ  1 
ATOM   9716  N  N   . VAL C 3  92   ? -50.056 -18.972  46.033  1.00 58.01  ?  92   VAL C N   1 
ATOM   9717  C  CA  . VAL C 3  92   ? -49.399 -17.706  46.347  1.00 60.28  ?  92   VAL C CA  1 
ATOM   9718  C  C   . VAL C 3  92   ? -50.411 -16.567  46.351  1.00 66.44  ?  92   VAL C C   1 
ATOM   9719  O  O   . VAL C 3  92   ? -50.314 -15.633  47.156  1.00 66.32  ?  92   VAL C O   1 
ATOM   9720  C  CB  . VAL C 3  92   ? -48.248 -17.443  45.357  1.00 59.55  ?  92   VAL C CB  1 
ATOM   9721  C  CG1 . VAL C 3  92   ? -47.575 -16.109  45.653  1.00 61.54  ?  92   VAL C CG1 1 
ATOM   9722  C  CG2 . VAL C 3  92   ? -47.234 -18.575  45.410  1.00 70.26  ?  92   VAL C CG2 1 
ATOM   9723  N  N   . TRP C 3  93   ? -51.401 -16.630  45.458  1.00 82.57  ?  93   TRP C N   1 
ATOM   9724  C  CA  . TRP C 3  93   ? -52.435 -15.601  45.419  1.00 84.65  ?  93   TRP C CA  1 
ATOM   9725  C  C   . TRP C 3  93   ? -53.246 -15.586  46.709  1.00 86.09  ?  93   TRP C C   1 
ATOM   9726  O  O   . TRP C 3  93   ? -53.464 -14.525  47.307  1.00 90.16  ?  93   TRP C O   1 
ATOM   9727  C  CB  . TRP C 3  93   ? -53.345 -15.826  44.211  1.00 84.23  ?  93   TRP C CB  1 
ATOM   9728  C  CG  . TRP C 3  93   ? -54.223 -14.657  43.892  1.00 92.94  ?  93   TRP C CG  1 
ATOM   9729  C  CD1 . TRP C 3  93   ? -53.844 -13.479  43.318  1.00 92.91  ?  93   TRP C CD1 1 
ATOM   9730  C  CD2 . TRP C 3  93   ? -55.632 -14.556  44.125  1.00 90.67  ?  93   TRP C CD2 1 
ATOM   9731  N  NE1 . TRP C 3  93   ? -54.931 -12.649  43.181  1.00 94.16  ?  93   TRP C NE1 1 
ATOM   9732  C  CE2 . TRP C 3  93   ? -56.041 -13.287  43.669  1.00 85.21  ?  93   TRP C CE2 1 
ATOM   9733  C  CE3 . TRP C 3  93   ? -56.588 -15.415  44.677  1.00 86.10  ?  93   TRP C CE3 1 
ATOM   9734  C  CZ2 . TRP C 3  93   ? -57.364 -12.857  43.748  1.00 87.18  ?  93   TRP C CZ2 1 
ATOM   9735  C  CZ3 . TRP C 3  93   ? -57.899 -14.986  44.754  1.00 85.54  ?  93   TRP C CZ3 1 
ATOM   9736  C  CH2 . TRP C 3  93   ? -58.275 -13.719  44.292  1.00 88.77  ?  93   TRP C CH2 1 
ATOM   9737  N  N   . TRP C 3  94   ? -53.700 -16.759  47.157  1.00 60.61  ?  94   TRP C N   1 
ATOM   9738  C  CA  . TRP C 3  94   ? -54.492 -16.831  48.382  1.00 61.23  ?  94   TRP C CA  1 
ATOM   9739  C  C   . TRP C 3  94   ? -53.665 -16.439  49.601  1.00 64.99  ?  94   TRP C C   1 
ATOM   9740  O  O   . TRP C 3  94   ? -54.111 -15.644  50.436  1.00 61.35  ?  94   TRP C O   1 
ATOM   9741  C  CB  . TRP C 3  94   ? -55.067 -18.237  48.552  1.00 58.40  ?  94   TRP C CB  1 
ATOM   9742  C  CG  . TRP C 3  94   ? -56.342 -18.472  47.801  1.00 65.59  ?  94   TRP C CG  1 
ATOM   9743  C  CD1 . TRP C 3  94   ? -56.555 -19.395  46.818  1.00 73.49  ?  94   TRP C CD1 1 
ATOM   9744  C  CD2 . TRP C 3  94   ? -57.588 -17.788  47.985  1.00 71.70  ?  94   TRP C CD2 1 
ATOM   9745  N  NE1 . TRP C 3  94   ? -57.852 -19.321  46.372  1.00 75.81  ?  94   TRP C NE1 1 
ATOM   9746  C  CE2 . TRP C 3  94   ? -58.508 -18.344  47.073  1.00 70.48  ?  94   TRP C CE2 1 
ATOM   9747  C  CE3 . TRP C 3  94   ? -58.014 -16.758  48.829  1.00 74.61  ?  94   TRP C CE3 1 
ATOM   9748  C  CZ2 . TRP C 3  94   ? -59.827 -17.903  46.981  1.00 64.08  ?  94   TRP C CZ2 1 
ATOM   9749  C  CZ3 . TRP C 3  94   ? -59.324 -16.323  48.737  1.00 74.03  ?  94   TRP C CZ3 1 
ATOM   9750  C  CH2 . TRP C 3  94   ? -60.215 -16.895  47.819  1.00 66.31  ?  94   TRP C CH2 1 
ATOM   9751  N  N   . ILE C 3  95   ? -52.452 -16.987  49.720  1.00 79.32  ?  95   ILE C N   1 
ATOM   9752  C  CA  . ILE C 3  95   ? -51.613 -16.694  50.878  1.00 76.41  ?  95   ILE C CA  1 
ATOM   9753  C  C   . ILE C 3  95   ? -51.200 -15.229  50.917  1.00 76.43  ?  95   ILE C C   1 
ATOM   9754  O  O   . ILE C 3  95   ? -50.792 -14.732  51.973  1.00 82.59  ?  95   ILE C O   1 
ATOM   9755  C  CB  . ILE C 3  95   ? -50.375 -17.612  50.896  1.00 77.14  ?  95   ILE C CB  1 
ATOM   9756  C  CG1 . ILE C 3  95   ? -49.892 -17.832  52.330  1.00 76.09  ?  95   ILE C CG1 1 
ATOM   9757  C  CG2 . ILE C 3  95   ? -49.256 -17.032  50.040  1.00 81.67  ?  95   ILE C CG2 1 
ATOM   9758  C  CD1 . ILE C 3  95   ? -50.882 -18.575  53.200  1.00 85.74  ?  95   ILE C CD1 1 
ATOM   9759  N  N   . GLY C 3  96   ? -51.298 -14.522  49.794  1.00 56.62  ?  96   GLY C N   1 
ATOM   9760  C  CA  . GLY C 3  96   ? -50.971 -13.112  49.761  1.00 67.37  ?  96   GLY C CA  1 
ATOM   9761  C  C   . GLY C 3  96   ? -52.163 -12.240  50.092  1.00 69.52  ?  96   GLY C C   1 
ATOM   9762  O  O   . GLY C 3  96   ? -52.005 -11.077  50.474  1.00 64.40  ?  96   GLY C O   1 
ATOM   9763  N  N   . ILE C 3  97   ? -53.366 -12.802  49.954  1.00 96.84  ?  97   ILE C N   1 
ATOM   9764  C  CA  . ILE C 3  97   ? -54.583 -12.041  50.223  1.00 101.11 ?  97   ILE C CA  1 
ATOM   9765  C  C   . ILE C 3  97   ? -54.628 -11.607  51.683  1.00 106.40 ?  97   ILE C C   1 
ATOM   9766  O  O   . ILE C 3  97   ? -55.039 -10.484  52.003  1.00 109.62 ?  97   ILE C O   1 
ATOM   9767  C  CB  . ILE C 3  97   ? -55.823 -12.869  49.834  1.00 100.49 ?  97   ILE C CB  1 
ATOM   9768  C  CG1 . ILE C 3  97   ? -56.038 -12.832  48.320  1.00 101.34 ?  97   ILE C CG1 1 
ATOM   9769  C  CG2 . ILE C 3  97   ? -57.063 -12.367  50.558  1.00 99.25  ?  97   ILE C CG2 1 
ATOM   9770  C  CD1 . ILE C 3  97   ? -56.345 -11.455  47.777  1.00 99.04  ?  97   ILE C CD1 1 
ATOM   9771  N  N   . GLY C 3  98   ? -54.188 -12.477  52.588  1.00 113.35 ?  98   GLY C N   1 
ATOM   9772  C  CA  . GLY C 3  98   ? -54.259 -12.212  54.009  1.00 107.37 ?  98   GLY C CA  1 
ATOM   9773  C  C   . GLY C 3  98   ? -53.181 -11.323  54.584  1.00 110.24 ?  98   GLY C C   1 
ATOM   9774  O  O   . GLY C 3  98   ? -53.225 -11.025  55.781  1.00 110.02 ?  98   GLY C O   1 
ATOM   9775  N  N   . HIS C 3  99   ? -52.209 -10.883  53.783  1.00 113.81 ?  99   HIS C N   1 
ATOM   9776  C  CA  . HIS C 3  99   ? -51.156 -10.027  54.323  1.00 113.79 ?  99   HIS C CA  1 
ATOM   9777  C  C   . HIS C 3  99   ? -51.700 -8.661   54.721  1.00 115.40 ?  99   HIS C C   1 
ATOM   9778  O  O   . HIS C 3  99   ? -51.281 -8.093   55.736  1.00 106.65 ?  99   HIS C O   1 
ATOM   9779  C  CB  . HIS C 3  99   ? -50.019 -9.878   53.313  1.00 114.50 ?  99   HIS C CB  1 
ATOM   9780  C  CG  . HIS C 3  99   ? -48.798 -9.214   53.874  1.00 119.72 ?  99   HIS C CG  1 
ATOM   9781  N  ND1 . HIS C 3  99   ? -47.585 -9.859   53.983  1.00 116.85 ?  99   HIS C ND1 1 
ATOM   9782  C  CD2 . HIS C 3  99   ? -48.601 -7.961   54.348  1.00 115.80 ?  99   HIS C CD2 1 
ATOM   9783  C  CE1 . HIS C 3  99   ? -46.696 -9.035   54.509  1.00 111.62 ?  99   HIS C CE1 1 
ATOM   9784  N  NE2 . HIS C 3  99   ? -47.286 -7.876   54.738  1.00 110.84 ?  99   HIS C NE2 1 
ATOM   9785  N  N   . ALA C 3  100  ? -52.632 -8.116   53.935  1.00 123.35 ?  100  ALA C N   1 
ATOM   9786  C  CA  . ALA C 3  100  ? -53.179 -6.800   54.249  1.00 121.44 ?  100  ALA C CA  1 
ATOM   9787  C  C   . ALA C 3  100  ? -53.995 -6.830   55.534  1.00 115.74 ?  100  ALA C C   1 
ATOM   9788  O  O   . ALA C 3  100  ? -53.901 -5.912   56.356  1.00 117.74 ?  100  ALA C O   1 
ATOM   9789  C  CB  . ALA C 3  100  ? -54.028 -6.293   53.087  1.00 122.68 ?  100  ALA C CB  1 
ATOM   9790  N  N   . GLY C 3  101  ? -54.803 -7.874   55.724  1.00 107.22 ?  101  GLY C N   1 
ATOM   9791  C  CA  . GLY C 3  101  ? -55.569 -7.984   56.953  1.00 118.28 ?  101  GLY C CA  1 
ATOM   9792  C  C   . GLY C 3  101  ? -54.687 -8.161   58.174  1.00 121.14 ?  101  GLY C C   1 
ATOM   9793  O  O   . GLY C 3  101  ? -54.968 -7.606   59.240  1.00 117.85 ?  101  GLY C O   1 
ATOM   9794  N  N   . THR C 3  102  ? -53.609 -8.939   58.038  1.00 106.69 ?  102  THR C N   1 
ATOM   9795  C  CA  . THR C 3  102  ? -52.641 -9.053   59.124  1.00 96.03  ?  102  THR C CA  1 
ATOM   9796  C  C   . THR C 3  102  ? -51.941 -7.726   59.386  1.00 91.31  ?  102  THR C C   1 
ATOM   9797  O  O   . THR C 3  102  ? -51.593 -7.426   60.533  1.00 91.88  ?  102  THR C O   1 
ATOM   9798  C  CB  . THR C 3  102  ? -51.613 -10.140  58.805  1.00 88.23  ?  102  THR C CB  1 
ATOM   9799  O  OG1 . THR C 3  102  ? -52.283 -11.300  58.295  1.00 94.15  ?  102  THR C OG1 1 
ATOM   9800  C  CG2 . THR C 3  102  ? -50.834 -10.521  60.053  1.00 73.48  ?  102  THR C CG2 1 
ATOM   9801  N  N   . LEU C 3  103  ? -51.729 -6.923   58.341  1.00 72.83  ?  103  LEU C N   1 
ATOM   9802  C  CA  . LEU C 3  103  ? -51.161 -5.593   58.532  1.00 72.58  ?  103  LEU C CA  1 
ATOM   9803  C  C   . LEU C 3  103  ? -52.133 -4.681   59.268  1.00 78.30  ?  103  LEU C C   1 
ATOM   9804  O  O   . LEU C 3  103  ? -51.731 -3.924   60.159  1.00 76.15  ?  103  LEU C O   1 
ATOM   9805  C  CB  . LEU C 3  103  ? -50.777 -4.990   57.179  1.00 67.18  ?  103  LEU C CB  1 
ATOM   9806  C  CG  . LEU C 3  103  ? -50.133 -3.600   57.159  1.00 56.78  ?  103  LEU C CG  1 
ATOM   9807  C  CD1 . LEU C 3  103  ? -48.948 -3.571   56.206  1.00 48.60  ?  103  LEU C CD1 1 
ATOM   9808  C  CD2 . LEU C 3  103  ? -51.151 -2.534   56.776  1.00 55.15  ?  103  LEU C CD2 1 
ATOM   9809  N  N   . ILE C 3  104  ? -53.417 -4.738   58.908  1.00 134.80 ?  104  ILE C N   1 
ATOM   9810  C  CA  . ILE C 3  104  ? -54.409 -3.880   59.549  1.00 139.61 ?  104  ILE C CA  1 
ATOM   9811  C  C   . ILE C 3  104  ? -54.590 -4.267   61.011  1.00 142.72 ?  104  ILE C C   1 
ATOM   9812  O  O   . ILE C 3  104  ? -54.695 -3.402   61.889  1.00 145.02 ?  104  ILE C O   1 
ATOM   9813  C  CB  . ILE C 3  104  ? -55.740 -3.941   58.776  1.00 145.14 ?  104  ILE C CB  1 
ATOM   9814  C  CG1 . ILE C 3  104  ? -55.566 -3.378   57.364  1.00 144.76 ?  104  ILE C CG1 1 
ATOM   9815  C  CG2 . ILE C 3  104  ? -56.831 -3.186   59.521  1.00 143.23 ?  104  ILE C CG2 1 
ATOM   9816  C  CD1 . ILE C 3  104  ? -56.847 -3.339   56.560  1.00 150.50 ?  104  ILE C CD1 1 
ATOM   9817  N  N   . SER C 3  105  ? -54.614 -5.567   61.301  1.00 90.77  ?  105  SER C N   1 
ATOM   9818  C  CA  . SER C 3  105  ? -54.902 -6.041   62.649  1.00 90.39  ?  105  SER C CA  1 
ATOM   9819  C  C   . SER C 3  105  ? -53.688 -6.024   63.571  1.00 88.70  ?  105  SER C C   1 
ATOM   9820  O  O   . SER C 3  105  ? -53.858 -6.175   64.785  1.00 83.98  ?  105  SER C O   1 
ATOM   9821  C  CB  . SER C 3  105  ? -55.478 -7.459   62.590  1.00 91.42  ?  105  SER C CB  1 
ATOM   9822  O  OG  . SER C 3  105  ? -55.784 -7.942   63.885  1.00 90.35  ?  105  SER C OG  1 
ATOM   9823  N  N   . ALA C 3  106  ? -52.479 -5.841   63.040  1.00 101.77 ?  106  ALA C N   1 
ATOM   9824  C  CA  . ALA C 3  106  ? -51.283 -5.913   63.871  1.00 96.60  ?  106  ALA C CA  1 
ATOM   9825  C  C   . ALA C 3  106  ? -50.374 -4.704   63.685  1.00 97.78  ?  106  ALA C C   1 
ATOM   9826  O  O   . ALA C 3  106  ? -50.012 -4.041   64.662  1.00 99.12  ?  106  ALA C O   1 
ATOM   9827  C  CB  . ALA C 3  106  ? -50.507 -7.198   63.575  1.00 90.17  ?  106  ALA C CB  1 
ATOM   9828  N  N   . ILE C 3  107  ? -49.992 -4.416   62.438  1.00 86.93  ?  107  ILE C N   1 
ATOM   9829  C  CA  . ILE C 3  107  ? -49.048 -3.332   62.183  1.00 81.54  ?  107  ILE C CA  1 
ATOM   9830  C  C   . ILE C 3  107  ? -49.658 -1.986   62.560  1.00 85.26  ?  107  ILE C C   1 
ATOM   9831  O  O   . ILE C 3  107  ? -48.998 -1.142   63.178  1.00 83.63  ?  107  ILE C O   1 
ATOM   9832  C  CB  . ILE C 3  107  ? -48.589 -3.357   60.713  1.00 76.11  ?  107  ILE C CB  1 
ATOM   9833  C  CG1 . ILE C 3  107  ? -47.853 -4.665   60.412  1.00 71.19  ?  107  ILE C CG1 1 
ATOM   9834  C  CG2 . ILE C 3  107  ? -47.699 -2.158   60.411  1.00 75.85  ?  107  ILE C CG2 1 
ATOM   9835  C  CD1 . ILE C 3  107  ? -47.065 -4.648   59.122  1.00 71.66  ?  107  ILE C CD1 1 
ATOM   9836  N  N   . LEU C 3  108  ? -50.926 -1.765   62.205  1.00 100.10 ?  108  LEU C N   1 
ATOM   9837  C  CA  . LEU C 3  108  ? -51.582 -0.508   62.544  1.00 98.03  ?  108  LEU C CA  1 
ATOM   9838  C  C   . LEU C 3  108  ? -51.775 -0.349   64.047  1.00 98.29  ?  108  LEU C C   1 
ATOM   9839  O  O   . LEU C 3  108  ? -51.881 0.783    64.532  1.00 104.14 ?  108  LEU C O   1 
ATOM   9840  C  CB  . LEU C 3  108  ? -52.927 -0.407   61.825  1.00 97.47  ?  108  LEU C CB  1 
ATOM   9841  C  CG  . LEU C 3  108  ? -52.875 -0.238   60.305  1.00 87.36  ?  108  LEU C CG  1 
ATOM   9842  C  CD1 . LEU C 3  108  ? -54.277 -0.133   59.732  1.00 94.24  ?  108  LEU C CD1 1 
ATOM   9843  C  CD2 . LEU C 3  108  ? -52.051 0.983    59.928  1.00 85.06  ?  108  LEU C CD2 1 
ATOM   9844  N  N   . LEU C 3  109  ? -51.823 -1.456   64.792  1.00 91.18  ?  109  LEU C N   1 
ATOM   9845  C  CA  . LEU C 3  109  ? -51.896 -1.363   66.246  1.00 91.89  ?  109  LEU C CA  1 
ATOM   9846  C  C   . LEU C 3  109  ? -50.621 -0.756   66.820  1.00 90.34  ?  109  LEU C C   1 
ATOM   9847  O  O   . LEU C 3  109  ? -50.676 0.028    67.774  1.00 89.06  ?  109  LEU C O   1 
ATOM   9848  C  CB  . LEU C 3  109  ? -52.156 -2.743   66.850  1.00 92.99  ?  109  LEU C CB  1 
ATOM   9849  C  CG  . LEU C 3  109  ? -52.355 -2.806   68.367  1.00 83.32  ?  109  LEU C CG  1 
ATOM   9850  C  CD1 . LEU C 3  109  ? -53.327 -1.734   68.842  1.00 90.87  ?  109  LEU C CD1 1 
ATOM   9851  C  CD2 . LEU C 3  109  ? -52.820 -4.191   68.794  1.00 77.32  ?  109  LEU C CD2 1 
ATOM   9852  N  N   . LEU C 3  110  ? -49.464 -1.104   66.250  1.00 91.53  ?  110  LEU C N   1 
ATOM   9853  C  CA  . LEU C 3  110  ? -48.203 -0.508   66.678  1.00 92.27  ?  110  LEU C CA  1 
ATOM   9854  C  C   . LEU C 3  110  ? -48.034 0.913    66.155  1.00 96.30  ?  110  LEU C C   1 
ATOM   9855  O  O   . LEU C 3  110  ? -47.448 1.756    66.843  1.00 102.58 ?  110  LEU C O   1 
ATOM   9856  C  CB  . LEU C 3  110  ? -47.031 -1.376   66.213  1.00 91.33  ?  110  LEU C CB  1 
ATOM   9857  C  CG  . LEU C 3  110  ? -47.121 -2.866   66.534  1.00 84.18  ?  110  LEU C CG  1 
ATOM   9858  C  CD1 . LEU C 3  110  ? -45.980 -3.619   65.875  1.00 84.43  ?  110  LEU C CD1 1 
ATOM   9859  C  CD2 . LEU C 3  110  ? -47.128 -3.093   68.038  1.00 73.86  ?  110  LEU C CD2 1 
ATOM   9860  N  N   . LEU C 3  111  ? -48.533 1.194    64.950  1.00 85.33  ?  111  LEU C N   1 
ATOM   9861  C  CA  . LEU C 3  111  ? -48.424 2.524    64.363  1.00 85.35  ?  111  LEU C CA  1 
ATOM   9862  C  C   . LEU C 3  111  ? -49.363 3.533    65.010  1.00 88.14  ?  111  LEU C C   1 
ATOM   9863  O  O   . LEU C 3  111  ? -49.275 4.725    64.689  1.00 86.16  ?  111  LEU C O   1 
ATOM   9864  C  CB  . LEU C 3  111  ? -48.700 2.454    62.858  1.00 87.16  ?  111  LEU C CB  1 
ATOM   9865  C  CG  . LEU C 3  111  ? -47.498 2.338    61.916  1.00 83.32  ?  111  LEU C CG  1 
ATOM   9866  C  CD1 . LEU C 3  111  ? -46.747 1.038    62.145  1.00 79.89  ?  111  LEU C CD1 1 
ATOM   9867  C  CD2 . LEU C 3  111  ? -47.944 2.447    60.464  1.00 85.42  ?  111  LEU C CD2 1 
ATOM   9868  N  N   . ASN C 3  112  ? -50.252 3.085    65.901  1.00 106.69 ?  112  ASN C N   1 
ATOM   9869  C  CA  . ASN C 3  112  ? -51.206 3.955    66.592  1.00 105.30 ?  112  ASN C CA  1 
ATOM   9870  C  C   . ASN C 3  112  ? -52.109 4.686    65.600  1.00 112.01 ?  112  ASN C C   1 
ATOM   9871  O  O   . ASN C 3  112  ? -52.426 5.865    65.771  1.00 118.97 ?  112  ASN C O   1 
ATOM   9872  C  CB  . ASN C 3  112  ? -50.488 4.945    67.513  1.00 110.15 ?  112  ASN C CB  1 
ATOM   9873  C  CG  . ASN C 3  112  ? -51.393 5.493    68.601  1.00 112.18 ?  112  ASN C CG  1 
ATOM   9874  O  OD1 . ASN C 3  112  ? -52.498 4.995    68.816  1.00 108.86 ?  112  ASN C OD1 1 
ATOM   9875  N  ND2 . ASN C 3  112  ? -50.926 6.525    69.294  1.00 110.76 ?  112  ASN C ND2 1 
ATOM   9876  N  N   . GLN C 3  113  ? -52.526 3.979    64.553  1.00 122.93 ?  113  GLN C N   1 
ATOM   9877  C  CA  . GLN C 3  113  ? -53.439 4.531    63.563  1.00 121.69 ?  113  GLN C CA  1 
ATOM   9878  C  C   . GLN C 3  113  ? -54.874 4.240    63.982  1.00 127.29 ?  113  GLN C C   1 
ATOM   9879  O  O   . GLN C 3  113  ? -55.202 3.108    64.353  1.00 122.12 ?  113  GLN C O   1 
ATOM   9880  C  CB  . GLN C 3  113  ? -53.156 3.948    62.177  1.00 119.54 ?  113  GLN C CB  1 
ATOM   9881  C  CG  . GLN C 3  113  ? -51.829 4.392    61.578  1.00 123.00 ?  113  GLN C CG  1 
ATOM   9882  C  CD  . GLN C 3  113  ? -51.639 5.897    61.621  1.00 128.77 ?  113  GLN C CD  1 
ATOM   9883  O  OE1 . GLN C 3  113  ? -52.549 6.660    61.292  1.00 135.10 ?  113  GLN C OE1 1 
ATOM   9884  N  NE2 . GLN C 3  113  ? -50.453 6.332    62.030  1.00 128.72 ?  113  GLN C NE2 1 
ATOM   9885  N  N   . GLY C 3  114  ? -55.724 5.261    63.921  1.00 107.62 ?  114  GLY C N   1 
ATOM   9886  C  CA  . GLY C 3  114  ? -57.085 5.168    64.402  1.00 106.77 ?  114  GLY C CA  1 
ATOM   9887  C  C   . GLY C 3  114  ? -58.106 4.612    63.438  1.00 108.35 ?  114  GLY C C   1 
ATOM   9888  O  O   . GLY C 3  114  ? -59.271 4.459    63.816  1.00 113.16 ?  114  GLY C O   1 
ATOM   9889  N  N   . TRP C 3  115  ? -57.718 4.301    62.202  1.00 100.78 ?  115  TRP C N   1 
ATOM   9890  C  CA  . TRP C 3  115  ? -58.649 3.785    61.208  1.00 96.83  ?  115  TRP C CA  1 
ATOM   9891  C  C   . TRP C 3  115  ? -58.641 2.264    61.125  1.00 93.90  ?  115  TRP C C   1 
ATOM   9892  O  O   . TRP C 3  115  ? -59.193 1.703    60.174  1.00 94.61  ?  115  TRP C O   1 
ATOM   9893  C  CB  . TRP C 3  115  ? -58.346 4.389    59.833  1.00 97.42  ?  115  TRP C CB  1 
ATOM   9894  C  CG  . TRP C 3  115  ? -56.922 4.242    59.388  1.00 97.07  ?  115  TRP C CG  1 
ATOM   9895  C  CD1 . TRP C 3  115  ? -55.856 5.000    59.778  1.00 96.96  ?  115  TRP C CD1 1 
ATOM   9896  C  CD2 . TRP C 3  115  ? -56.412 3.290    58.445  1.00 99.37  ?  115  TRP C CD2 1 
ATOM   9897  N  NE1 . TRP C 3  115  ? -54.713 4.572    59.147  1.00 96.30  ?  115  TRP C NE1 1 
ATOM   9898  C  CE2 . TRP C 3  115  ? -55.028 3.523    58.323  1.00 95.52  ?  115  TRP C CE2 1 
ATOM   9899  C  CE3 . TRP C 3  115  ? -56.992 2.260    57.698  1.00 96.37  ?  115  TRP C CE3 1 
ATOM   9900  C  CZ2 . TRP C 3  115  ? -54.215 2.765    57.484  1.00 88.98  ?  115  TRP C CZ2 1 
ATOM   9901  C  CZ3 . TRP C 3  115  ? -56.183 1.508    56.867  1.00 88.59  ?  115  TRP C CZ3 1 
ATOM   9902  C  CH2 . TRP C 3  115  ? -54.810 1.765    56.766  1.00 88.20  ?  115  TRP C CH2 1 
ATOM   9903  N  N   . ARG C 3  116  ? -58.033 1.586    62.097  1.00 122.60 ?  116  ARG C N   1 
ATOM   9904  C  CA  . ARG C 3  116  ? -58.032 0.131    62.154  1.00 124.00 ?  116  ARG C CA  1 
ATOM   9905  C  C   . ARG C 3  116  ? -59.119 -0.424   63.061  1.00 119.37 ?  116  ARG C C   1 
ATOM   9906  O  O   . ARG C 3  116  ? -59.258 -1.646   63.163  1.00 116.42 ?  116  ARG C O   1 
ATOM   9907  C  CB  . ARG C 3  116  ? -56.670 -0.382   62.634  1.00 124.40 ?  116  ARG C CB  1 
ATOM   9908  C  CG  . ARG C 3  116  ? -56.321 0.045    64.052  1.00 123.38 ?  116  ARG C CG  1 
ATOM   9909  C  CD  . ARG C 3  116  ? -55.188 -0.788   64.626  1.00 125.00 ?  116  ARG C CD  1 
ATOM   9910  N  NE  . ARG C 3  116  ? -55.557 -2.191   64.770  1.00 123.13 ?  116  ARG C NE  1 
ATOM   9911  C  CZ  . ARG C 3  116  ? -56.095 -2.716   65.864  1.00 123.22 ?  116  ARG C CZ  1 
ATOM   9912  N  NH1 . ARG C 3  116  ? -56.336 -1.981   66.937  1.00 119.57 ?  116  ARG C NH1 1 
ATOM   9913  N  NH2 . ARG C 3  116  ? -56.397 -4.011   65.881  1.00 120.81 ?  116  ARG C NH2 1 
ATOM   9914  N  N   . ASN C 3  117  ? -59.890 0.440    63.721  1.00 96.57  ?  117  ASN C N   1 
ATOM   9915  C  CA  . ASN C 3  117  ? -60.830 -0.023   64.733  1.00 96.62  ?  117  ASN C CA  1 
ATOM   9916  C  C   . ASN C 3  117  ? -62.089 -0.628   64.126  1.00 99.60  ?  117  ASN C C   1 
ATOM   9917  O  O   . ASN C 3  117  ? -62.722 -1.485   64.754  1.00 101.64 ?  117  ASN C O   1 
ATOM   9918  C  CB  . ASN C 3  117  ? -61.200 1.134    65.662  1.00 96.99  ?  117  ASN C CB  1 
ATOM   9919  C  CG  . ASN C 3  117  ? -60.018 1.629    66.474  1.00 94.49  ?  117  ASN C CG  1 
ATOM   9920  O  OD1 . ASN C 3  117  ? -59.571 0.967    67.411  1.00 94.25  ?  117  ASN C OD1 1 
ATOM   9921  N  ND2 . ASN C 3  117  ? -59.504 2.800    66.116  1.00 88.22  ?  117  ASN C ND2 1 
ATOM   9922  N  N   . SER C 3  118  ? -62.465 -0.209   62.919  1.00 106.32 ?  118  SER C N   1 
ATOM   9923  C  CA  . SER C 3  118  ? -63.715 -0.642   62.312  1.00 106.90 ?  118  SER C CA  1 
ATOM   9924  C  C   . SER C 3  118  ? -63.540 -1.729   61.260  1.00 104.04 ?  118  SER C C   1 
ATOM   9925  O  O   . SER C 3  118  ? -64.544 -2.266   60.781  1.00 101.06 ?  118  SER C O   1 
ATOM   9926  C  CB  . SER C 3  118  ? -64.437 0.557    61.681  1.00 113.57 ?  118  SER C CB  1 
ATOM   9927  O  OG  . SER C 3  118  ? -63.781 0.983    60.499  1.00 104.96 ?  118  SER C OG  1 
ATOM   9928  N  N   . ILE C 3  119  ? -62.303 -2.070   60.891  1.00 86.95  ?  119  ILE C N   1 
ATOM   9929  C  CA  . ILE C 3  119  ? -62.051 -3.030   59.824  1.00 90.79  ?  119  ILE C CA  1 
ATOM   9930  C  C   . ILE C 3  119  ? -61.092 -4.137   60.231  1.00 89.45  ?  119  ILE C C   1 
ATOM   9931  O  O   . ILE C 3  119  ? -60.792 -5.006   59.412  1.00 77.56  ?  119  ILE C O   1 
ATOM   9932  C  CB  . ILE C 3  119  ? -61.536 -2.329   58.549  1.00 86.54  ?  119  ILE C CB  1 
ATOM   9933  C  CG1 . ILE C 3  119  ? -60.290 -1.497   58.862  1.00 87.64  ?  119  ILE C CG1 1 
ATOM   9934  C  CG2 . ILE C 3  119  ? -62.631 -1.472   57.928  1.00 88.82  ?  119  ILE C CG2 1 
ATOM   9935  C  CD1 . ILE C 3  119  ? -59.793 -0.674   57.693  1.00 91.13  ?  119  ILE C CD1 1 
ATOM   9936  N  N   . ASN C 3  120  ? -60.597 -4.143   61.471  1.00 111.97 ?  120  ASN C N   1 
ATOM   9937  C  CA  . ASN C 3  120  ? -59.638 -5.171   61.868  1.00 102.88 ?  120  ASN C CA  1 
ATOM   9938  C  C   . ASN C 3  120  ? -60.298 -6.535   62.024  1.00 95.30  ?  120  ASN C C   1 
ATOM   9939  O  O   . ASN C 3  120  ? -59.658 -7.562   61.774  1.00 96.39  ?  120  ASN C O   1 
ATOM   9940  C  CB  . ASN C 3  120  ? -58.937 -4.771   63.167  1.00 93.34  ?  120  ASN C CB  1 
ATOM   9941  C  CG  . ASN C 3  120  ? -59.809 -4.979   64.390  1.00 92.51  ?  120  ASN C CG  1 
ATOM   9942  O  OD1 . ASN C 3  120  ? -61.021 -4.764   64.347  1.00 96.69  ?  120  ASN C OD1 1 
ATOM   9943  N  ND2 . ASN C 3  120  ? -59.196 -5.407   65.487  1.00 104.39 ?  120  ASN C ND2 1 
ATOM   9944  N  N   . ARG C 3  121  ? -61.567 -6.569   62.436  1.00 89.80  ?  121  ARG C N   1 
ATOM   9945  C  CA  . ARG C 3  121  ? -62.249 -7.846   62.625  1.00 91.18  ?  121  ARG C CA  1 
ATOM   9946  C  C   . ARG C 3  121  ? -62.532 -8.520   61.289  1.00 94.98  ?  121  ARG C C   1 
ATOM   9947  O  O   . ARG C 3  121  ? -62.220 -9.701   61.099  1.00 88.84  ?  121  ARG C O   1 
ATOM   9948  C  CB  . ARG C 3  121  ? -63.544 -7.636   63.407  1.00 93.97  ?  121  ARG C CB  1 
ATOM   9949  C  CG  . ARG C 3  121  ? -64.492 -8.820   63.360  1.00 92.90  ?  121  ARG C CG  1 
ATOM   9950  C  CD  . ARG C 3  121  ? -64.029 -9.929   64.287  1.00 97.04  ?  121  ARG C CD  1 
ATOM   9951  N  NE  . ARG C 3  121  ? -63.543 -9.408   65.559  1.00 100.10 ?  121  ARG C NE  1 
ATOM   9952  C  CZ  . ARG C 3  121  ? -64.321 -8.987   66.547  1.00 101.00 ?  121  ARG C CZ  1 
ATOM   9953  N  NH1 . ARG C 3  121  ? -65.640 -9.003   66.442  1.00 100.09 ?  121  ARG C NH1 1 
ATOM   9954  N  NH2 . ARG C 3  121  ? -63.762 -8.548   67.670  1.00 102.72 ?  121  ARG C NH2 1 
ATOM   9955  N  N   . PHE C 3  122  ? -63.131 -7.783   60.351  1.00 101.15 ?  122  PHE C N   1 
ATOM   9956  C  CA  . PHE C 3  122  ? -63.417 -8.347   59.036  1.00 92.34  ?  122  PHE C CA  1 
ATOM   9957  C  C   . PHE C 3  122  ? -62.135 -8.709   58.298  1.00 86.85  ?  122  PHE C C   1 
ATOM   9958  O  O   . PHE C 3  122  ? -62.065 -9.752   57.638  1.00 87.22  ?  122  PHE C O   1 
ATOM   9959  C  CB  . PHE C 3  122  ? -64.249 -7.364   58.214  1.00 84.55  ?  122  PHE C CB  1 
ATOM   9960  C  CG  . PHE C 3  122  ? -65.128 -8.021   57.189  1.00 91.72  ?  122  PHE C CG  1 
ATOM   9961  C  CD1 . PHE C 3  122  ? -64.637 -8.317   55.927  1.00 99.42  ?  122  PHE C CD1 1 
ATOM   9962  C  CD2 . PHE C 3  122  ? -66.441 -8.343   57.484  1.00 96.90  ?  122  PHE C CD2 1 
ATOM   9963  C  CE1 . PHE C 3  122  ? -65.440 -8.921   54.978  1.00 95.43  ?  122  PHE C CE1 1 
ATOM   9964  C  CE2 . PHE C 3  122  ? -67.250 -8.948   56.538  1.00 104.29 ?  122  PHE C CE2 1 
ATOM   9965  C  CZ  . PHE C 3  122  ? -66.748 -9.238   55.284  1.00 99.42  ?  122  PHE C CZ  1 
ATOM   9966  N  N   . ALA C 3  123  ? -61.110 -7.860   58.398  1.00 99.27  ?  123  ALA C N   1 
ATOM   9967  C  CA  . ALA C 3  123  ? -59.856 -8.131   57.703  1.00 99.18  ?  123  ALA C CA  1 
ATOM   9968  C  C   . ALA C 3  123  ? -59.188 -9.387   58.248  1.00 99.53  ?  123  ALA C C   1 
ATOM   9969  O  O   . ALA C 3  123  ? -58.752 -10.252  57.480  1.00 105.93 ?  123  ALA C O   1 
ATOM   9970  C  CB  . ALA C 3  123  ? -58.918 -6.929   57.814  1.00 109.61 ?  123  ALA C CB  1 
ATOM   9971  N  N   . GLU C 3  124  ? -59.104 -9.507   59.576  1.00 103.49 ?  124  GLU C N   1 
ATOM   9972  C  CA  . GLU C 3  124  ? -58.483 -10.687  60.170  1.00 102.50 ?  124  GLU C CA  1 
ATOM   9973  C  C   . GLU C 3  124  ? -59.274 -11.948  59.848  1.00 99.11  ?  124  GLU C C   1 
ATOM   9974  O  O   . GLU C 3  124  ? -58.692 -13.022  59.657  1.00 102.98 ?  124  GLU C O   1 
ATOM   9975  C  CB  . GLU C 3  124  ? -58.346 -10.510  61.683  1.00 113.84 ?  124  GLU C CB  1 
ATOM   9976  C  CG  . GLU C 3  124  ? -57.640 -11.661  62.397  1.00 117.39 ?  124  GLU C CG  1 
ATOM   9977  C  CD  . GLU C 3  124  ? -56.123 -11.617  62.270  1.00 120.48 ?  124  GLU C CD  1 
ATOM   9978  O  OE1 . GLU C 3  124  ? -55.608 -11.122  61.245  1.00 112.89 ?  124  GLU C OE1 1 
ATOM   9979  O  OE2 . GLU C 3  124  ? -55.443 -12.087  63.207  1.00 121.53 -1 124  GLU C OE2 1 
ATOM   9980  N  N   . ALA C 3  125  ? -60.603 -11.839  59.785  1.00 71.58  ?  125  ALA C N   1 
ATOM   9981  C  CA  . ALA C 3  125  ? -61.411 -12.977  59.359  1.00 74.24  ?  125  ALA C CA  1 
ATOM   9982  C  C   . ALA C 3  125  ? -61.063 -13.389  57.936  1.00 67.05  ?  125  ALA C C   1 
ATOM   9983  O  O   . ALA C 3  125  ? -61.026 -14.583  57.618  1.00 66.98  ?  125  ALA C O   1 
ATOM   9984  C  CB  . ALA C 3  125  ? -62.898 -12.642  59.476  1.00 78.70  ?  125  ALA C CB  1 
ATOM   9985  N  N   . MET C 3  126  ? -60.795 -12.412  57.066  1.00 84.23  ?  126  MET C N   1 
ATOM   9986  C  CA  . MET C 3  126  ? -60.363 -12.723  55.708  1.00 79.23  ?  126  MET C CA  1 
ATOM   9987  C  C   . MET C 3  126  ? -59.000 -13.406  55.703  1.00 82.32  ?  126  MET C C   1 
ATOM   9988  O  O   . MET C 3  126  ? -58.743 -14.279  54.868  1.00 80.77  ?  126  MET C O   1 
ATOM   9989  C  CB  . MET C 3  126  ? -60.329 -11.449  54.866  1.00 73.44  ?  126  MET C CB  1 
ATOM   9990  C  CG  . MET C 3  126  ? -61.698 -10.865  54.570  1.00 75.19  ?  126  MET C CG  1 
ATOM   9991  S  SD  . MET C 3  126  ? -61.587 -9.290   53.701  1.00 95.86  ?  126  MET C SD  1 
ATOM   9992  C  CE  . MET C 3  126  ? -60.945 -9.820   52.114  1.00 85.63  ?  126  MET C CE  1 
ATOM   9993  N  N   . THR C 3  127  ? -58.113 -13.021  56.625  1.00 107.39 ?  127  THR C N   1 
ATOM   9994  C  CA  . THR C 3  127  ? -56.807 -13.671  56.712  1.00 104.08 ?  127  THR C CA  1 
ATOM   9995  C  C   . THR C 3  127  ? -56.951 -15.137  57.095  1.00 99.53  ?  127  THR C C   1 
ATOM   9996  O  O   . THR C 3  127  ? -56.345 -16.016  56.473  1.00 106.21 ?  127  THR C O   1 
ATOM   9997  C  CB  . THR C 3  127  ? -55.915 -12.947  57.721  1.00 108.65 ?  127  THR C CB  1 
ATOM   9998  O  OG1 . THR C 3  127  ? -56.416 -13.164  59.046  1.00 119.06 ?  127  THR C OG1 1 
ATOM   9999  C  CG2 . THR C 3  127  ? -55.882 -11.463  57.435  1.00 102.06 ?  127  THR C CG2 1 
ATOM   10000 N  N   . LEU C 3  128  ? -57.752 -15.420  58.127  1.00 96.53  ?  128  LEU C N   1 
ATOM   10001 C  CA  . LEU C 3  128  ? -57.937 -16.799  58.567  1.00 100.73 ?  128  LEU C CA  1 
ATOM   10002 C  C   . LEU C 3  128  ? -58.563 -17.653  57.472  1.00 102.51 ?  128  LEU C C   1 
ATOM   10003 O  O   . LEU C 3  128  ? -58.175 -18.812  57.282  1.00 105.28 ?  128  LEU C O   1 
ATOM   10004 C  CB  . LEU C 3  128  ? -58.796 -16.838  59.833  1.00 94.02  ?  128  LEU C CB  1 
ATOM   10005 C  CG  . LEU C 3  128  ? -58.074 -16.773  61.182  1.00 97.00  ?  128  LEU C CG  1 
ATOM   10006 C  CD1 . LEU C 3  128  ? -57.480 -15.395  61.438  1.00 104.20 ?  128  LEU C CD1 1 
ATOM   10007 C  CD2 . LEU C 3  128  ? -59.023 -17.161  62.302  1.00 105.27 ?  128  LEU C CD2 1 
ATOM   10008 N  N   . PHE C 3  129  ? -59.530 -17.099  56.737  1.00 89.84  ?  129  PHE C N   1 
ATOM   10009 C  CA  . PHE C 3  129  ? -60.182 -17.875  55.687  1.00 94.33  ?  129  PHE C CA  1 
ATOM   10010 C  C   . PHE C 3  129  ? -59.278 -18.028  54.469  1.00 94.22  ?  129  PHE C C   1 
ATOM   10011 O  O   . PHE C 3  129  ? -59.297 -19.071  53.804  1.00 90.62  ?  129  PHE C O   1 
ATOM   10012 C  CB  . PHE C 3  129  ? -61.510 -17.225  55.296  1.00 92.06  ?  129  PHE C CB  1 
ATOM   10013 C  CG  . PHE C 3  129  ? -62.479 -17.087  56.436  1.00 88.30  ?  129  PHE C CG  1 
ATOM   10014 C  CD1 . PHE C 3  129  ? -62.460 -17.980  57.494  1.00 88.65  ?  129  PHE C CD1 1 
ATOM   10015 C  CD2 . PHE C 3  129  ? -63.420 -16.069  56.441  1.00 88.52  ?  129  PHE C CD2 1 
ATOM   10016 C  CE1 . PHE C 3  129  ? -63.352 -17.856  58.541  1.00 92.71  ?  129  PHE C CE1 1 
ATOM   10017 C  CE2 . PHE C 3  129  ? -64.314 -15.939  57.486  1.00 98.68  ?  129  PHE C CE2 1 
ATOM   10018 C  CZ  . PHE C 3  129  ? -64.281 -16.834  58.536  1.00 97.45  ?  129  PHE C CZ  1 
ATOM   10019 N  N   . ALA C 3  130  ? -58.479 -17.003  54.159  1.00 84.29  ?  130  ALA C N   1 
ATOM   10020 C  CA  . ALA C 3  130  ? -57.557 -17.106  53.031  1.00 77.36  ?  130  ALA C CA  1 
ATOM   10021 C  C   . ALA C 3  130  ? -56.428 -18.082  53.331  1.00 77.95  ?  130  ALA C C   1 
ATOM   10022 O  O   . ALA C 3  130  ? -55.978 -18.811  52.440  1.00 80.24  ?  130  ALA C O   1 
ATOM   10023 C  CB  . ALA C 3  130  ? -56.995 -15.730  52.676  1.00 81.58  ?  130  ALA C CB  1 
ATOM   10024 N  N   . VAL C 3  131  ? -55.956 -18.108  54.579  1.00 93.27  ?  131  VAL C N   1 
ATOM   10025 C  CA  . VAL C 3  131  ? -54.942 -19.083  54.967  1.00 89.73  ?  131  VAL C CA  1 
ATOM   10026 C  C   . VAL C 3  131  ? -55.525 -20.491  54.949  1.00 94.11  ?  131  VAL C C   1 
ATOM   10027 O  O   . VAL C 3  131  ? -54.852 -21.452  54.558  1.00 102.22 ?  131  VAL C O   1 
ATOM   10028 C  CB  . VAL C 3  131  ? -54.357 -18.721  56.345  1.00 88.07  ?  131  VAL C CB  1 
ATOM   10029 C  CG1 . VAL C 3  131  ? -53.522 -19.866  56.895  1.00 96.99  ?  131  VAL C CG1 1 
ATOM   10030 C  CG2 . VAL C 3  131  ? -53.519 -17.459  56.242  1.00 90.93  ?  131  VAL C CG2 1 
ATOM   10031 N  N   . ALA C 3  132  ? -56.790 -20.634  55.353  1.00 83.40  ?  132  ALA C N   1 
ATOM   10032 C  CA  . ALA C 3  132  ? -57.435 -21.943  55.310  1.00 88.20  ?  132  ALA C CA  1 
ATOM   10033 C  C   . ALA C 3  132  ? -57.593 -22.435  53.876  1.00 93.03  ?  132  ALA C C   1 
ATOM   10034 O  O   . ALA C 3  132  ? -57.470 -23.636  53.609  1.00 92.65  ?  132  ALA C O   1 
ATOM   10035 C  CB  . ALA C 3  132  ? -58.791 -21.885  56.012  1.00 88.40  ?  132  ALA C CB  1 
ATOM   10036 N  N   . CYS C 3  133  ? -57.863 -21.522  52.939  1.00 105.76 ?  133  CYS C N   1 
ATOM   10037 C  CA  . CYS C 3  133  ? -57.972 -21.917  51.538  1.00 103.85 ?  133  CYS C CA  1 
ATOM   10038 C  C   . CYS C 3  133  ? -56.600 -22.192  50.937  1.00 101.69 ?  133  CYS C C   1 
ATOM   10039 O  O   . CYS C 3  133  ? -56.434 -23.142  50.162  1.00 104.26 ?  133  CYS C O   1 
ATOM   10040 C  CB  . CYS C 3  133  ? -58.698 -20.837  50.738  1.00 98.52  ?  133  CYS C CB  1 
ATOM   10041 S  SG  . CYS C 3  133  ? -60.442 -20.649  51.159  1.00 103.56 ?  133  CYS C SG  1 
ATOM   10042 N  N   . ALA C 3  134  ? -55.604 -21.371  51.277  1.00 90.66  ?  134  ALA C N   1 
ATOM   10043 C  CA  . ALA C 3  134  ? -54.256 -21.595  50.770  1.00 86.27  ?  134  ALA C CA  1 
ATOM   10044 C  C   . ALA C 3  134  ? -53.595 -22.814  51.391  1.00 86.74  ?  134  ALA C C   1 
ATOM   10045 O  O   . ALA C 3  134  ? -52.610 -23.313  50.843  1.00 87.45  ?  134  ALA C O   1 
ATOM   10046 C  CB  . ALA C 3  134  ? -53.388 -20.362  51.010  1.00 75.37  ?  134  ALA C CB  1 
ATOM   10047 N  N   . GLY C 3  135  ? -54.103 -23.300  52.520  1.00 102.71 ?  135  GLY C N   1 
ATOM   10048 C  CA  . GLY C 3  135  ? -53.477 -24.442  53.167  1.00 101.38 ?  135  GLY C CA  1 
ATOM   10049 C  C   . GLY C 3  135  ? -53.807 -25.777  52.540  1.00 105.24 ?  135  GLY C C   1 
ATOM   10050 O  O   . GLY C 3  135  ? -53.296 -26.801  53.004  1.00 105.91 ?  135  GLY C O   1 
ATOM   10051 N  N   . LEU C 3  136  ? -54.647 -25.794  51.509  1.00 93.45  ?  136  LEU C N   1 
ATOM   10052 C  CA  . LEU C 3  136  ? -55.002 -27.038  50.834  1.00 87.79  ?  136  LEU C CA  1 
ATOM   10053 C  C   . LEU C 3  136  ? -54.105 -27.336  49.642  1.00 82.81  ?  136  LEU C C   1 
ATOM   10054 O  O   . LEU C 3  136  ? -53.857 -28.510  49.346  1.00 87.90  ?  136  LEU C O   1 
ATOM   10055 C  CB  . LEU C 3  136  ? -56.461 -26.995  50.374  1.00 86.69  ?  136  LEU C CB  1 
ATOM   10056 C  CG  . LEU C 3  136  ? -57.485 -26.567  51.424  1.00 88.00  ?  136  LEU C CG  1 
ATOM   10057 C  CD1 . LEU C 3  136  ? -58.768 -26.093  50.758  1.00 91.99  ?  136  LEU C CD1 1 
ATOM   10058 C  CD2 . LEU C 3  136  ? -57.762 -27.716  52.380  1.00 81.89  ?  136  LEU C CD2 1 
ATOM   10059 N  N   . TYR C 3  137  ? -53.611 -26.306  48.953  1.00 85.45  ?  137  TYR C N   1 
ATOM   10060 C  CA  . TYR C 3  137  ? -52.778 -26.542  47.776  1.00 87.02  ?  137  TYR C CA  1 
ATOM   10061 C  C   . TYR C 3  137  ? -51.477 -27.281  48.081  1.00 86.06  ?  137  TYR C C   1 
ATOM   10062 O  O   . TYR C 3  137  ? -51.100 -28.152  47.277  1.00 82.51  ?  137  TYR C O   1 
ATOM   10063 C  CB  . TYR C 3  137  ? -52.497 -25.213  47.063  1.00 85.85  ?  137  TYR C CB  1 
ATOM   10064 C  CG  . TYR C 3  137  ? -53.615 -24.766  46.147  1.00 92.35  ?  137  TYR C CG  1 
ATOM   10065 C  CD1 . TYR C 3  137  ? -53.846 -25.411  44.938  1.00 90.33  ?  137  TYR C CD1 1 
ATOM   10066 C  CD2 . TYR C 3  137  ? -54.437 -23.700  46.487  1.00 93.86  ?  137  TYR C CD2 1 
ATOM   10067 C  CE1 . TYR C 3  137  ? -54.863 -25.009  44.095  1.00 86.29  ?  137  TYR C CE1 1 
ATOM   10068 C  CE2 . TYR C 3  137  ? -55.459 -23.290  45.648  1.00 89.81  ?  137  TYR C CE2 1 
ATOM   10069 C  CZ  . TYR C 3  137  ? -55.666 -23.950  44.454  1.00 78.08  ?  137  TYR C CZ  1 
ATOM   10070 O  OH  . TYR C 3  137  ? -56.679 -23.551  43.612  1.00 76.36  ?  137  TYR C OH  1 
ATOM   10071 N  N   . PRO C 3  138  ? -50.746 -27.000  49.168  1.00 100.00 ?  138  PRO C N   1 
ATOM   10072 C  CA  . PRO C 3  138  ? -49.569 -27.830  49.479  1.00 99.97  ?  138  PRO C CA  1 
ATOM   10073 C  C   . PRO C 3  138  ? -49.895 -29.297  49.704  1.00 95.68  ?  138  PRO C C   1 
ATOM   10074 O  O   . PRO C 3  138  ? -48.995 -30.139  49.593  1.00 89.24  ?  138  PRO C O   1 
ATOM   10075 C  CB  . PRO C 3  138  ? -49.006 -27.179  50.749  1.00 94.97  ?  138  PRO C CB  1 
ATOM   10076 C  CG  . PRO C 3  138  ? -49.445 -25.768  50.661  1.00 95.80  ?  138  PRO C CG  1 
ATOM   10077 C  CD  . PRO C 3  138  ? -50.813 -25.817  50.046  1.00 98.62  ?  138  PRO C CD  1 
ATOM   10078 N  N   . ILE C 3  139  ? -51.144 -29.631  50.021  1.00 78.02  ?  139  ILE C N   1 
ATOM   10079 C  CA  . ILE C 3  139  ? -51.547 -31.029  50.141  1.00 76.18  ?  139  ILE C CA  1 
ATOM   10080 C  C   . ILE C 3  139  ? -52.137 -31.548  48.834  1.00 79.23  ?  139  ILE C C   1 
ATOM   10081 O  O   . ILE C 3  139  ? -51.895 -32.694  48.450  1.00 80.46  ?  139  ILE C O   1 
ATOM   10082 C  CB  . ILE C 3  139  ? -52.538 -31.196  51.312  1.00 74.27  ?  139  ILE C CB  1 
ATOM   10083 C  CG1 . ILE C 3  139  ? -51.988 -30.543  52.581  1.00 77.81  ?  139  ILE C CG1 1 
ATOM   10084 C  CG2 . ILE C 3  139  ? -52.829 -32.669  51.560  1.00 66.26  ?  139  ILE C CG2 1 
ATOM   10085 C  CD1 . ILE C 3  139  ? -52.917 -30.650  53.772  1.00 80.29  ?  139  ILE C CD1 1 
ATOM   10086 N  N   . LEU C 3  140  ? -52.899 -30.713  48.125  1.00 72.35  ?  140  LEU C N   1 
ATOM   10087 C  CA  . LEU C 3  140  ? -53.593 -31.179  46.928  1.00 71.04  ?  140  LEU C CA  1 
ATOM   10088 C  C   . LEU C 3  140  ? -52.627 -31.404  45.770  1.00 69.79  ?  140  LEU C C   1 
ATOM   10089 O  O   . LEU C 3  140  ? -52.777 -32.367  45.009  1.00 72.36  ?  140  LEU C O   1 
ATOM   10090 C  CB  . LEU C 3  140  ? -54.681 -30.180  46.534  1.00 73.10  ?  140  LEU C CB  1 
ATOM   10091 C  CG  . LEU C 3  140  ? -55.913 -30.134  47.442  1.00 72.75  ?  140  LEU C CG  1 
ATOM   10092 C  CD1 . LEU C 3  140  ? -56.953 -29.166  46.897  1.00 76.99  ?  140  LEU C CD1 1 
ATOM   10093 C  CD2 . LEU C 3  140  ? -56.505 -31.523  47.631  1.00 65.44  ?  140  LEU C CD2 1 
ATOM   10094 N  N   . HIS C 3  141  ? -51.632 -30.531  45.619  1.00 60.69  ?  141  HIS C N   1 
ATOM   10095 C  CA  . HIS C 3  141  ? -50.686 -30.635  44.514  1.00 68.35  ?  141  HIS C CA  1 
ATOM   10096 C  C   . HIS C 3  141  ? -49.608 -31.684  44.750  1.00 66.42  ?  141  HIS C C   1 
ATOM   10097 O  O   . HIS C 3  141  ? -48.712 -31.829  43.911  1.00 64.92  ?  141  HIS C O   1 
ATOM   10098 C  CB  . HIS C 3  141  ? -50.027 -29.275  44.258  1.00 65.41  ?  141  HIS C CB  1 
ATOM   10099 C  CG  . HIS C 3  141  ? -48.729 -29.083  44.980  1.00 62.33  ?  141  HIS C CG  1 
ATOM   10100 N  ND1 . HIS C 3  141  ? -48.655 -28.866  46.339  1.00 67.73  ?  141  HIS C ND1 1 
ATOM   10101 C  CD2 . HIS C 3  141  ? -47.453 -29.066  44.528  1.00 57.38  ?  141  HIS C CD2 1 
ATOM   10102 C  CE1 . HIS C 3  141  ? -47.389 -28.732  46.694  1.00 68.75  ?  141  HIS C CE1 1 
ATOM   10103 N  NE2 . HIS C 3  141  ? -46.639 -28.848  45.613  1.00 60.80  ?  141  HIS C NE2 1 
ATOM   10104 N  N   . LEU C 3  142  ? -49.679 -32.425  45.857  1.00 73.10  ?  142  LEU C N   1 
ATOM   10105 C  CA  . LEU C 3  142  ? -48.569 -33.288  46.239  1.00 76.29  ?  142  LEU C CA  1 
ATOM   10106 C  C   . LEU C 3  142  ? -48.426 -34.491  45.312  1.00 80.79  ?  142  LEU C C   1 
ATOM   10107 O  O   . LEU C 3  142  ? -47.312 -34.991  45.125  1.00 81.20  ?  142  LEU C O   1 
ATOM   10108 C  CB  . LEU C 3  142  ? -48.748 -33.744  47.687  1.00 72.69  ?  142  LEU C CB  1 
ATOM   10109 C  CG  . LEU C 3  142  ? -47.456 -33.953  48.476  1.00 73.15  ?  142  LEU C CG  1 
ATOM   10110 C  CD1 . LEU C 3  142  ? -46.669 -32.657  48.557  1.00 72.58  ?  142  LEU C CD1 1 
ATOM   10111 C  CD2 . LEU C 3  142  ? -47.767 -34.465  49.869  1.00 72.19  ?  142  LEU C CD2 1 
ATOM   10112 N  N   . GLY C 3  143  ? -49.521 -34.961  44.720  1.00 131.16 ?  143  GLY C N   1 
ATOM   10113 C  CA  . GLY C 3  143  ? -49.545 -36.217  43.970  1.00 128.78 ?  143  GLY C CA  1 
ATOM   10114 C  C   . GLY C 3  143  ? -49.644 -37.467  44.834  1.00 139.19 ?  143  GLY C C   1 
ATOM   10115 O  O   . GLY C 3  143  ? -50.224 -38.476  44.423  1.00 153.77 ?  143  GLY C O   1 
ATOM   10116 N  N   . ARG C 3  144  ? -49.048 -37.416  46.022  1.00 72.67  ?  144  ARG C N   1 
ATOM   10117 C  CA  . ARG C 3  144  ? -49.263 -38.402  47.078  1.00 69.12  ?  144  ARG C CA  1 
ATOM   10118 C  C   . ARG C 3  144  ? -49.669 -37.613  48.313  1.00 69.76  ?  144  ARG C C   1 
ATOM   10119 O  O   . ARG C 3  144  ? -48.872 -37.438  49.245  1.00 70.50  ?  144  ARG C O   1 
ATOM   10120 C  CB  . ARG C 3  144  ? -48.021 -39.262  47.315  1.00 64.22  ?  144  ARG C CB  1 
ATOM   10121 C  CG  . ARG C 3  144  ? -47.806 -40.318  46.242  1.00 59.82  ?  144  ARG C CG  1 
ATOM   10122 C  CD  . ARG C 3  144  ? -47.210 -41.591  46.821  1.00 59.39  ?  144  ARG C CD  1 
ATOM   10123 N  NE  . ARG C 3  144  ? -45.833 -41.406  47.261  1.00 62.79  ?  144  ARG C NE  1 
ATOM   10124 C  CZ  . ARG C 3  144  ? -45.070 -42.371  47.754  1.00 61.29  ?  144  ARG C CZ  1 
ATOM   10125 N  NH1 . ARG C 3  144  ? -45.514 -43.613  47.870  1.00 54.09  ?  144  ARG C NH1 1 
ATOM   10126 N  NH2 . ARG C 3  144  ? -43.831 -42.083  48.141  1.00 57.05  ?  144  ARG C NH2 1 
ATOM   10127 N  N   . PRO C 3  145  ? -50.912 -37.123  48.353  1.00 54.17  ?  145  PRO C N   1 
ATOM   10128 C  CA  . PRO C 3  145  ? -51.271 -36.132  49.383  1.00 52.25  ?  145  PRO C CA  1 
ATOM   10129 C  C   . PRO C 3  145  ? -51.248 -36.670  50.802  1.00 44.88  ?  145  PRO C C   1 
ATOM   10130 O  O   . PRO C 3  145  ? -50.870 -35.935  51.723  1.00 44.72  ?  145  PRO C O   1 
ATOM   10131 C  CB  . PRO C 3  145  ? -52.684 -35.699  48.967  1.00 51.19  ?  145  PRO C CB  1 
ATOM   10132 C  CG  . PRO C 3  145  ? -53.200 -36.819  48.132  1.00 50.00  ?  145  PRO C CG  1 
ATOM   10133 C  CD  . PRO C 3  145  ? -52.013 -37.363  47.405  1.00 48.29  ?  145  PRO C CD  1 
ATOM   10134 N  N   . TRP C 3  146  ? -51.641 -37.928  51.013  1.00 63.45  ?  146  TRP C N   1 
ATOM   10135 C  CA  . TRP C 3  146  ? -51.773 -38.462  52.364  1.00 65.16  ?  146  TRP C CA  1 
ATOM   10136 C  C   . TRP C 3  146  ? -50.445 -38.570  53.104  1.00 61.03  ?  146  TRP C C   1 
ATOM   10137 O  O   . TRP C 3  146  ? -50.449 -38.888  54.298  1.00 61.67  ?  146  TRP C O   1 
ATOM   10138 C  CB  . TRP C 3  146  ? -52.447 -39.833  52.321  1.00 65.44  ?  146  TRP C CB  1 
ATOM   10139 C  CG  . TRP C 3  146  ? -51.677 -40.846  51.541  1.00 67.14  ?  146  TRP C CG  1 
ATOM   10140 C  CD1 . TRP C 3  146  ? -50.772 -41.742  52.029  1.00 72.20  ?  146  TRP C CD1 1 
ATOM   10141 C  CD2 . TRP C 3  146  ? -51.744 -41.070  50.129  1.00 66.12  ?  146  TRP C CD2 1 
ATOM   10142 N  NE1 . TRP C 3  146  ? -50.269 -42.510  51.007  1.00 73.21  ?  146  TRP C NE1 1 
ATOM   10143 C  CE2 . TRP C 3  146  ? -50.851 -42.117  49.830  1.00 71.30  ?  146  TRP C CE2 1 
ATOM   10144 C  CE3 . TRP C 3  146  ? -52.473 -40.487  49.088  1.00 71.03  ?  146  TRP C CE3 1 
ATOM   10145 C  CZ2 . TRP C 3  146  ? -50.667 -42.594  48.533  1.00 73.70  ?  146  TRP C CZ2 1 
ATOM   10146 C  CZ3 . TRP C 3  146  ? -52.289 -40.961  47.802  1.00 76.14  ?  146  TRP C CZ3 1 
ATOM   10147 C  CH2 . TRP C 3  146  ? -51.394 -42.004  47.535  1.00 82.42  ?  146  TRP C CH2 1 
ATOM   10148 N  N   . LEU C 3  147  ? -49.319 -38.319  52.438  1.00 54.18  ?  147  LEU C N   1 
ATOM   10149 C  CA  . LEU C 3  147  ? -48.009 -38.351  53.072  1.00 54.50  ?  147  LEU C CA  1 
ATOM   10150 C  C   . LEU C 3  147  ? -47.478 -36.956  53.383  1.00 50.69  ?  147  LEU C C   1 
ATOM   10151 O  O   . LEU C 3  147  ? -46.261 -36.778  53.508  1.00 49.55  ?  147  LEU C O   1 
ATOM   10152 C  CB  . LEU C 3  147  ? -47.013 -39.106  52.191  1.00 62.11  ?  147  LEU C CB  1 
ATOM   10153 C  CG  . LEU C 3  147  ? -47.279 -40.589  51.930  1.00 60.85  ?  147  LEU C CG  1 
ATOM   10154 C  CD1 . LEU C 3  147  ? -46.294 -41.116  50.901  1.00 59.52  ?  147  LEU C CD1 1 
ATOM   10155 C  CD2 . LEU C 3  147  ? -47.191 -41.390  53.220  1.00 53.05  ?  147  LEU C CD2 1 
ATOM   10156 N  N   . PHE C 3  148  ? -48.364 -35.964  53.510  1.00 61.27  ?  148  PHE C N   1 
ATOM   10157 C  CA  . PHE C 3  148  ? -47.913 -34.602  53.777  1.00 69.23  ?  148  PHE C CA  1 
ATOM   10158 C  C   . PHE C 3  148  ? -47.224 -34.493  55.130  1.00 73.32  ?  148  PHE C C   1 
ATOM   10159 O  O   . PHE C 3  148  ? -46.342 -33.646  55.310  1.00 67.39  ?  148  PHE C O   1 
ATOM   10160 C  CB  . PHE C 3  148  ? -49.093 -33.631  53.709  1.00 67.79  ?  148  PHE C CB  1 
ATOM   10161 C  CG  . PHE C 3  148  ? -50.079 -33.795  54.831  1.00 71.85  ?  148  PHE C CG  1 
ATOM   10162 C  CD1 . PHE C 3  148  ? -51.084 -34.745  54.756  1.00 80.94  ?  148  PHE C CD1 1 
ATOM   10163 C  CD2 . PHE C 3  148  ? -50.002 -32.996  55.961  1.00 63.91  ?  148  PHE C CD2 1 
ATOM   10164 C  CE1 . PHE C 3  148  ? -51.991 -34.898  55.789  1.00 78.85  ?  148  PHE C CE1 1 
ATOM   10165 C  CE2 . PHE C 3  148  ? -50.905 -33.145  56.995  1.00 61.45  ?  148  PHE C CE2 1 
ATOM   10166 C  CZ  . PHE C 3  148  ? -51.901 -34.096  56.909  1.00 68.36  ?  148  PHE C CZ  1 
ATOM   10167 N  N   . TYR C 3  149  ? -47.610 -35.335  56.091  1.00 72.74  ?  149  TYR C N   1 
ATOM   10168 C  CA  . TYR C 3  149  ? -47.012 -35.289  57.418  1.00 66.66  ?  149  TYR C CA  1 
ATOM   10169 C  C   . TYR C 3  149  ? -45.547 -35.706  57.422  1.00 71.54  ?  149  TYR C C   1 
ATOM   10170 O  O   . TYR C 3  149  ? -44.878 -35.534  58.446  1.00 77.31  ?  149  TYR C O   1 
ATOM   10171 C  CB  . TYR C 3  149  ? -47.811 -36.166  58.387  1.00 68.87  ?  149  TYR C CB  1 
ATOM   10172 C  CG  . TYR C 3  149  ? -47.778 -37.644  58.068  1.00 65.66  ?  149  TYR C CG  1 
ATOM   10173 C  CD1 . TYR C 3  149  ? -48.710 -38.208  57.207  1.00 65.99  ?  149  TYR C CD1 1 
ATOM   10174 C  CD2 . TYR C 3  149  ? -46.822 -38.478  58.637  1.00 63.55  ?  149  TYR C CD2 1 
ATOM   10175 C  CE1 . TYR C 3  149  ? -48.687 -39.558  56.915  1.00 65.24  ?  149  TYR C CE1 1 
ATOM   10176 C  CE2 . TYR C 3  149  ? -46.791 -39.830  58.349  1.00 71.60  ?  149  TYR C CE2 1 
ATOM   10177 C  CZ  . TYR C 3  149  ? -47.726 -40.364  57.488  1.00 70.00  ?  149  TYR C CZ  1 
ATOM   10178 O  OH  . TYR C 3  149  ? -47.698 -41.710  57.200  1.00 67.34  ?  149  TYR C OH  1 
ATOM   10179 N  N   . TRP C 3  150  ? -45.035 -36.248  56.314  1.00 71.45  ?  150  TRP C N   1 
ATOM   10180 C  CA  . TRP C 3  150  ? -43.615 -36.568  56.233  1.00 71.28  ?  150  TRP C CA  1 
ATOM   10181 C  C   . TRP C 3  150  ? -42.747 -35.317  56.219  1.00 68.84  ?  150  TRP C C   1 
ATOM   10182 O  O   . TRP C 3  150  ? -41.556 -35.399  56.536  1.00 68.17  ?  150  TRP C O   1 
ATOM   10183 C  CB  . TRP C 3  150  ? -43.337 -37.421  54.994  1.00 68.27  ?  150  TRP C CB  1 
ATOM   10184 C  CG  . TRP C 3  150  ? -43.489 -38.889  55.248  1.00 69.61  ?  150  TRP C CG  1 
ATOM   10185 C  CD1 . TRP C 3  150  ? -43.814 -39.485  56.432  1.00 72.35  ?  150  TRP C CD1 1 
ATOM   10186 C  CD2 . TRP C 3  150  ? -43.328 -39.949  54.297  1.00 68.26  ?  150  TRP C CD2 1 
ATOM   10187 N  NE1 . TRP C 3  150  ? -43.864 -40.849  56.278  1.00 76.08  ?  150  TRP C NE1 1 
ATOM   10188 C  CE2 . TRP C 3  150  ? -43.569 -41.160  54.976  1.00 71.85  ?  150  TRP C CE2 1 
ATOM   10189 C  CE3 . TRP C 3  150  ? -43.002 -39.992  52.938  1.00 74.03  ?  150  TRP C CE3 1 
ATOM   10190 C  CZ2 . TRP C 3  150  ? -43.495 -42.399  54.343  1.00 68.98  ?  150  TRP C CZ2 1 
ATOM   10191 C  CZ3 . TRP C 3  150  ? -42.930 -41.223  52.312  1.00 69.89  ?  150  TRP C CZ3 1 
ATOM   10192 C  CH2 . TRP C 3  150  ? -43.174 -42.409  53.014  1.00 69.81  ?  150  TRP C CH2 1 
ATOM   10193 N  N   . LEU C 3  151  ? -43.316 -34.166  55.863  1.00 68.23  ?  151  LEU C N   1 
ATOM   10194 C  CA  . LEU C 3  151  ? -42.607 -32.897  55.956  1.00 69.48  ?  151  LEU C CA  1 
ATOM   10195 C  C   . LEU C 3  151  ? -42.521 -32.376  57.383  1.00 72.51  ?  151  LEU C C   1 
ATOM   10196 O  O   . LEU C 3  151  ? -41.793 -31.409  57.630  1.00 84.91  ?  151  LEU C O   1 
ATOM   10197 C  CB  . LEU C 3  151  ? -43.287 -31.849  55.071  1.00 75.16  ?  151  LEU C CB  1 
ATOM   10198 C  CG  . LEU C 3  151  ? -42.986 -31.872  53.571  1.00 60.98  ?  151  LEU C CG  1 
ATOM   10199 C  CD1 . LEU C 3  151  ? -43.876 -32.875  52.856  1.00 62.27  ?  151  LEU C CD1 1 
ATOM   10200 C  CD2 . LEU C 3  151  ? -43.166 -30.485  52.979  1.00 63.46  ?  151  LEU C CD2 1 
ATOM   10201 N  N   . ILE C 3  152  ? -43.240 -32.985  58.315  1.00 68.85  ?  152  ILE C N   1 
ATOM   10202 C  CA  . ILE C 3  152  ? -43.267 -32.558  59.712  1.00 67.61  ?  152  ILE C CA  1 
ATOM   10203 C  C   . ILE C 3  152  ? -42.334 -33.465  60.506  1.00 68.74  ?  152  ILE C C   1 
ATOM   10204 O  O   . ILE C 3  152  ? -42.385 -34.690  60.326  1.00 77.76  ?  152  ILE C O   1 
ATOM   10205 C  CB  . ILE C 3  152  ? -44.694 -32.610  60.289  1.00 57.13  ?  152  ILE C CB  1 
ATOM   10206 C  CG1 . ILE C 3  152  ? -45.659 -31.816  59.409  1.00 62.94  ?  152  ILE C CG1 1 
ATOM   10207 C  CG2 . ILE C 3  152  ? -44.720 -32.081  61.714  1.00 59.70  ?  152  ILE C CG2 1 
ATOM   10208 C  CD1 . ILE C 3  152  ? -47.106 -31.936  59.837  1.00 57.49  ?  152  ILE C CD1 1 
ATOM   10209 N  N   . PRO C 3  153  ? -41.477 -32.921  61.375  1.00 82.92  ?  153  PRO C N   1 
ATOM   10210 C  CA  . PRO C 3  153  ? -40.619 -33.783  62.200  1.00 88.31  ?  153  PRO C CA  1 
ATOM   10211 C  C   . PRO C 3  153  ? -41.411 -34.561  63.240  1.00 84.61  ?  153  PRO C C   1 
ATOM   10212 O  O   . PRO C 3  153  ? -41.678 -34.059  64.336  1.00 84.37  ?  153  PRO C O   1 
ATOM   10213 C  CB  . PRO C 3  153  ? -39.647 -32.794  62.854  1.00 84.74  ?  153  PRO C CB  1 
ATOM   10214 C  CG  . PRO C 3  153  ? -40.355 -31.481  62.821  1.00 83.74  ?  153  PRO C CG  1 
ATOM   10215 C  CD  . PRO C 3  153  ? -41.192 -31.490  61.578  1.00 84.40  ?  153  PRO C CD  1 
ATOM   10216 N  N   . TYR C 3  154  ? -41.790 -35.792  62.904  1.00 70.05  ?  154  TYR C N   1 
ATOM   10217 C  CA  . TYR C 3  154  ? -42.550 -36.650  63.794  1.00 68.15  ?  154  TYR C CA  1 
ATOM   10218 C  C   . TYR C 3  154  ? -41.778 -37.934  64.073  1.00 75.04  ?  154  TYR C C   1 
ATOM   10219 O  O   . TYR C 3  154  ? -41.038 -38.417  63.211  1.00 79.08  ?  154  TYR C O   1 
ATOM   10220 C  CB  . TYR C 3  154  ? -43.921 -36.996  63.195  1.00 64.70  ?  154  TYR C CB  1 
ATOM   10221 C  CG  . TYR C 3  154  ? -43.877 -38.059  62.116  1.00 69.75  ?  154  TYR C CG  1 
ATOM   10222 C  CD1 . TYR C 3  154  ? -43.445 -37.758  60.830  1.00 68.44  ?  154  TYR C CD1 1 
ATOM   10223 C  CD2 . TYR C 3  154  ? -44.274 -39.364  62.383  1.00 79.40  ?  154  TYR C CD2 1 
ATOM   10224 C  CE1 . TYR C 3  154  ? -43.404 -38.729  59.843  1.00 69.24  ?  154  TYR C CE1 1 
ATOM   10225 C  CE2 . TYR C 3  154  ? -44.237 -40.339  61.404  1.00 80.94  ?  154  TYR C CE2 1 
ATOM   10226 C  CZ  . TYR C 3  154  ? -43.802 -40.017  60.137  1.00 75.22  ?  154  TYR C CZ  1 
ATOM   10227 O  OH  . TYR C 3  154  ? -43.767 -40.989  59.164  1.00 78.63  ?  154  TYR C OH  1 
ATOM   10228 N  N   . PRO C 3  155  ? -41.924 -38.507  65.269  1.00 59.50  ?  155  PRO C N   1 
ATOM   10229 C  CA  . PRO C 3  155  ? -41.243 -39.776  65.576  1.00 54.92  ?  155  PRO C CA  1 
ATOM   10230 C  C   . PRO C 3  155  ? -41.780 -40.896  64.697  1.00 52.31  ?  155  PRO C C   1 
ATOM   10231 O  O   . PRO C 3  155  ? -42.980 -41.181  64.695  1.00 58.45  ?  155  PRO C O   1 
ATOM   10232 C  CB  . PRO C 3  155  ? -41.568 -40.008  67.058  1.00 54.23  ?  155  PRO C CB  1 
ATOM   10233 C  CG  . PRO C 3  155  ? -42.030 -38.671  67.574  1.00 52.68  ?  155  PRO C CG  1 
ATOM   10234 C  CD  . PRO C 3  155  ? -42.698 -38.006  66.416  1.00 55.61  ?  155  PRO C CD  1 
ATOM   10235 N  N   . ASN C 3  156  ? -40.884 -41.532  63.949  1.00 65.29  ?  156  ASN C N   1 
ATOM   10236 C  CA  . ASN C 3  156  ? -41.260 -42.559  62.991  1.00 73.41  ?  156  ASN C CA  1 
ATOM   10237 C  C   . ASN C 3  156  ? -40.452 -43.823  63.244  1.00 72.11  ?  156  ASN C C   1 
ATOM   10238 O  O   . ASN C 3  156  ? -39.438 -43.816  63.947  1.00 68.71  ?  156  ASN C O   1 
ATOM   10239 C  CB  . ASN C 3  156  ? -41.055 -42.075  61.549  1.00 77.51  ?  156  ASN C CB  1 
ATOM   10240 C  CG  . ASN C 3  156  ? -39.688 -41.459  61.330  1.00 74.24  ?  156  ASN C CG  1 
ATOM   10241 O  OD1 . ASN C 3  156  ? -38.817 -41.526  62.197  1.00 73.62  ?  156  ASN C OD1 1 
ATOM   10242 N  ND2 . ASN C 3  156  ? -39.493 -40.851  60.166  1.00 78.00  ?  156  ASN C ND2 1 
ATOM   10243 N  N   . THR C 3  157  ? -40.917 -44.920  62.649  1.00 73.73  ?  157  THR C N   1 
ATOM   10244 C  CA  . THR C 3  157  ? -40.240 -46.206  62.735  1.00 65.34  ?  157  THR C CA  1 
ATOM   10245 C  C   . THR C 3  157  ? -39.008 -46.287  61.843  1.00 69.50  ?  157  THR C C   1 
ATOM   10246 O  O   . THR C 3  157  ? -38.350 -47.334  61.817  1.00 66.31  ?  157  THR C O   1 
ATOM   10247 C  CB  . THR C 3  157  ? -41.212 -47.333  62.368  1.00 73.12  ?  157  THR C CB  1 
ATOM   10248 O  OG1 . THR C 3  157  ? -41.336 -47.418  60.942  1.00 85.14  ?  157  THR C OG1 1 
ATOM   10249 C  CG2 . THR C 3  157  ? -42.584 -47.069  62.968  1.00 64.43  ?  157  THR C CG2 1 
ATOM   10250 N  N   . HIS C 3  158  ? -38.678 -45.217  61.121  1.00 75.92  ?  158  HIS C N   1 
ATOM   10251 C  CA  . HIS C 3  158  ? -37.583 -45.207  60.160  1.00 71.21  ?  158  HIS C CA  1 
ATOM   10252 C  C   . HIS C 3  158  ? -36.359 -44.459  60.663  1.00 66.21  ?  158  HIS C C   1 
ATOM   10253 O  O   . HIS C 3  158  ? -35.236 -44.962  60.558  1.00 63.95  ?  158  HIS C O   1 
ATOM   10254 C  CB  . HIS C 3  158  ? -38.052 -44.580  58.839  1.00 55.66  ?  158  HIS C CB  1 
ATOM   10255 C  CG  . HIS C 3  158  ? -39.413 -45.026  58.407  1.00 52.24  ?  158  HIS C CG  1 
ATOM   10256 N  ND1 . HIS C 3  158  ? -40.447 -44.144  58.185  1.00 52.47  ?  158  HIS C ND1 1 
ATOM   10257 C  CD2 . HIS C 3  158  ? -39.910 -46.260  58.157  1.00 54.41  ?  158  HIS C CD2 1 
ATOM   10258 C  CE1 . HIS C 3  158  ? -41.524 -44.815  57.815  1.00 62.09  ?  158  HIS C CE1 1 
ATOM   10259 N  NE2 . HIS C 3  158  ? -41.225 -46.101  57.791  1.00 60.87  ?  158  HIS C NE2 1 
ATOM   10260 N  N   . GLY C 3  159  ? -36.548 -43.263  61.205  1.00 76.94  ?  159  GLY C N   1 
ATOM   10261 C  CA  . GLY C 3  159  ? -35.449 -42.402  61.563  1.00 79.25  ?  159  GLY C CA  1 
ATOM   10262 C  C   . GLY C 3  159  ? -35.132 -41.335  60.541  1.00 79.68  ?  159  GLY C C   1 
ATOM   10263 O  O   . GLY C 3  159  ? -33.985 -40.879  60.483  1.00 75.91  ?  159  GLY C O   1 
ATOM   10264 N  N   . MET C 3  160  ? -36.108 -40.927  59.735  1.00 94.75  ?  160  MET C N   1 
ATOM   10265 C  CA  . MET C 3  160  ? -35.912 -39.945  58.680  1.00 97.04  ?  160  MET C CA  1 
ATOM   10266 C  C   . MET C 3  160  ? -36.370 -38.570  59.146  1.00 95.95  ?  160  MET C C   1 
ATOM   10267 O  O   . MET C 3  160  ? -37.375 -38.443  59.851  1.00 101.94 ?  160  MET C O   1 
ATOM   10268 C  CB  . MET C 3  160  ? -36.677 -40.345  57.417  1.00 92.06  ?  160  MET C CB  1 
ATOM   10269 C  CG  . MET C 3  160  ? -35.944 -41.334  56.525  1.00 86.50  ?  160  MET C CG  1 
ATOM   10270 S  SD  . MET C 3  160  ? -34.297 -40.767  56.058  1.00 97.52  ?  160  MET C SD  1 
ATOM   10271 C  CE  . MET C 3  160  ? -34.688 -39.266  55.161  1.00 92.04  ?  160  MET C CE  1 
ATOM   10272 N  N   . TRP C 3  161  ? -35.625 -37.543  58.744  1.00 71.84  ?  161  TRP C N   1 
ATOM   10273 C  CA  . TRP C 3  161  ? -35.933 -36.161  59.063  1.00 75.25  ?  161  TRP C CA  1 
ATOM   10274 C  C   . TRP C 3  161  ? -36.238 -35.386  57.788  1.00 75.39  ?  161  TRP C C   1 
ATOM   10275 O  O   . TRP C 3  161  ? -35.767 -35.754  56.707  1.00 84.67  ?  161  TRP C O   1 
ATOM   10276 C  CB  . TRP C 3  161  ? -34.767 -35.475  59.788  1.00 88.15  ?  161  TRP C CB  1 
ATOM   10277 C  CG  . TRP C 3  161  ? -34.356 -36.118  61.076  1.00 81.90  ?  161  TRP C CG  1 
ATOM   10278 C  CD1 . TRP C 3  161  ? -33.684 -37.295  61.227  1.00 82.67  ?  161  TRP C CD1 1 
ATOM   10279 C  CD2 . TRP C 3  161  ? -34.573 -35.607  62.397  1.00 82.30  ?  161  TRP C CD2 1 
ATOM   10280 N  NE1 . TRP C 3  161  ? -33.476 -37.554  62.560  1.00 92.51  ?  161  TRP C NE1 1 
ATOM   10281 C  CE2 . TRP C 3  161  ? -34.012 -36.533  63.300  1.00 84.66  ?  161  TRP C CE2 1 
ATOM   10282 C  CE3 . TRP C 3  161  ? -35.189 -34.460  62.905  1.00 78.72  ?  161  TRP C CE3 1 
ATOM   10283 C  CZ2 . TRP C 3  161  ? -34.050 -36.347  64.679  1.00 78.94  ?  161  TRP C CZ2 1 
ATOM   10284 C  CZ3 . TRP C 3  161  ? -35.226 -34.277  64.274  1.00 84.89  ?  161  TRP C CZ3 1 
ATOM   10285 C  CH2 . TRP C 3  161  ? -34.661 -35.216  65.146  1.00 83.25  ?  161  TRP C CH2 1 
ATOM   10286 N  N   . PRO C 3  162  ? -37.026 -34.317  57.877  1.00 56.70  ?  162  PRO C N   1 
ATOM   10287 C  CA  . PRO C 3  162  ? -37.099 -33.372  56.759  1.00 54.35  ?  162  PRO C CA  1 
ATOM   10288 C  C   . PRO C 3  162  ? -35.748 -32.705  56.543  1.00 61.52  ?  162  PRO C C   1 
ATOM   10289 O  O   . PRO C 3  162  ? -34.891 -32.678  57.429  1.00 65.71  ?  162  PRO C O   1 
ATOM   10290 C  CB  . PRO C 3  162  ? -38.163 -32.363  57.209  1.00 56.66  ?  162  PRO C CB  1 
ATOM   10291 C  CG  . PRO C 3  162  ? -38.947 -33.075  58.269  1.00 55.99  ?  162  PRO C CG  1 
ATOM   10292 C  CD  . PRO C 3  162  ? -37.974 -33.982  58.952  1.00 61.12  ?  162  PRO C CD  1 
ATOM   10293 N  N   . GLN C 3  163  ? -35.559 -32.159  55.339  1.00 95.60  ?  163  GLN C N   1 
ATOM   10294 C  CA  . GLN C 3  163  ? -34.253 -31.606  54.991  1.00 98.96  ?  163  GLN C CA  1 
ATOM   10295 C  C   . GLN C 3  163  ? -33.970 -30.308  55.739  1.00 99.63  ?  163  GLN C C   1 
ATOM   10296 O  O   . GLN C 3  163  ? -32.823 -30.050  56.123  1.00 109.65 ?  163  GLN C O   1 
ATOM   10297 C  CB  . GLN C 3  163  ? -34.152 -31.373  53.487  1.00 89.87  ?  163  GLN C CB  1 
ATOM   10298 C  CG  . GLN C 3  163  ? -32.768 -30.922  53.062  1.00 91.16  ?  163  GLN C CG  1 
ATOM   10299 C  CD  . GLN C 3  163  ? -32.685 -30.579  51.596  1.00 100.87 ?  163  GLN C CD  1 
ATOM   10300 O  OE1 . GLN C 3  163  ? -31.620 -30.229  51.092  1.00 104.37 ?  163  GLN C OE1 1 
ATOM   10301 N  NE2 . GLN C 3  163  ? -33.810 -30.677  50.899  1.00 106.03 ?  163  GLN C NE2 1 
ATOM   10302 N  N   . PHE C 3  164  ? -34.990 -29.465  55.916  1.00 73.38  ?  164  PHE C N   1 
ATOM   10303 C  CA  . PHE C 3  164  ? -34.874 -28.177  56.599  1.00 76.87  ?  164  PHE C CA  1 
ATOM   10304 C  C   . PHE C 3  164  ? -33.976 -27.194  55.849  1.00 67.22  ?  164  PHE C C   1 
ATOM   10305 O  O   . PHE C 3  164  ? -33.923 -26.011  56.199  1.00 65.22  ?  164  PHE C O   1 
ATOM   10306 C  CB  . PHE C 3  164  ? -34.368 -28.367  58.034  1.00 76.71  ?  164  PHE C CB  1 
ATOM   10307 C  CG  . PHE C 3  164  ? -35.352 -29.054  58.938  1.00 76.78  ?  164  PHE C CG  1 
ATOM   10308 C  CD1 . PHE C 3  164  ? -36.700 -28.740  58.882  1.00 83.00  ?  164  PHE C CD1 1 
ATOM   10309 C  CD2 . PHE C 3  164  ? -34.930 -30.016  59.840  1.00 68.40  ?  164  PHE C CD2 1 
ATOM   10310 C  CE1 . PHE C 3  164  ? -37.609 -29.371  59.712  1.00 86.91  ?  164  PHE C CE1 1 
ATOM   10311 C  CE2 . PHE C 3  164  ? -35.833 -30.651  60.672  1.00 78.41  ?  164  PHE C CE2 1 
ATOM   10312 C  CZ  . PHE C 3  164  ? -37.174 -30.328  60.608  1.00 83.65  ?  164  PHE C CZ  1 
ATOM   10313 N  N   . ARG C 3  165  ? -33.268 -27.666  54.822  1.00 61.30  ?  165  ARG C N   1 
ATOM   10314 C  CA  . ARG C 3  165  ? -32.499 -26.796  53.943  1.00 56.95  ?  165  ARG C CA  1 
ATOM   10315 C  C   . ARG C 3  165  ? -33.263 -26.409  52.685  1.00 57.82  ?  165  ARG C C   1 
ATOM   10316 O  O   . ARG C 3  165  ? -32.779 -25.571  51.917  1.00 50.21  ?  165  ARG C O   1 
ATOM   10317 C  CB  . ARG C 3  165  ? -31.172 -27.461  53.555  1.00 55.70  ?  165  ARG C CB  1 
ATOM   10318 C  CG  . ARG C 3  165  ? -30.491 -28.183  54.704  1.00 69.23  ?  165  ARG C CG  1 
ATOM   10319 C  CD  . ARG C 3  165  ? -29.083 -28.620  54.341  1.00 61.78  ?  165  ARG C CD  1 
ATOM   10320 N  NE  . ARG C 3  165  ? -28.762 -29.921  54.915  1.00 57.18  ?  165  ARG C NE  1 
ATOM   10321 C  CZ  . ARG C 3  165  ? -27.532 -30.354  55.155  1.00 60.38  ?  165  ARG C CZ  1 
ATOM   10322 N  NH1 . ARG C 3  165  ? -26.472 -29.609  54.887  1.00 52.03  ?  165  ARG C NH1 1 
ATOM   10323 N  NH2 . ARG C 3  165  ? -27.362 -31.566  55.678  1.00 62.90  ?  165  ARG C NH2 1 
ATOM   10324 N  N   . SER C 3  166  ? -34.431 -26.998  52.456  1.00 68.14  ?  166  SER C N   1 
ATOM   10325 C  CA  . SER C 3  166  ? -35.317 -26.570  51.388  1.00 65.76  ?  166  SER C CA  1 
ATOM   10326 C  C   . SER C 3  166  ? -36.281 -25.513  51.910  1.00 72.56  ?  166  SER C C   1 
ATOM   10327 O  O   . SER C 3  166  ? -36.473 -25.351  53.117  1.00 79.90  ?  166  SER C O   1 
ATOM   10328 C  CB  . SER C 3  166  ? -36.096 -27.756  50.816  1.00 71.15  ?  166  SER C CB  1 
ATOM   10329 O  OG  . SER C 3  166  ? -37.284 -27.991  51.552  1.00 70.05  ?  166  SER C OG  1 
ATOM   10330 N  N   . ALA C 3  167  ? -36.892 -24.786  50.978  1.00 65.84  ?  167  ALA C N   1 
ATOM   10331 C  CA  . ALA C 3  167  ? -37.828 -23.736  51.351  1.00 57.05  ?  167  ALA C CA  1 
ATOM   10332 C  C   . ALA C 3  167  ? -39.228 -24.259  51.637  1.00 61.81  ?  167  ALA C C   1 
ATOM   10333 O  O   . ALA C 3  167  ? -40.037 -23.524  52.213  1.00 73.45  ?  167  ALA C O   1 
ATOM   10334 C  CB  . ALA C 3  167  ? -37.888 -22.672  50.257  1.00 58.67  ?  167  ALA C CB  1 
ATOM   10335 N  N   . LEU C 3  168  ? -39.538 -25.498  51.252  1.00 89.56  ?  168  LEU C N   1 
ATOM   10336 C  CA  . LEU C 3  168  ? -40.844 -26.058  51.576  1.00 99.25  ?  168  LEU C CA  1 
ATOM   10337 C  C   . LEU C 3  168  ? -40.930 -26.484  53.036  1.00 99.46  ?  168  LEU C C   1 
ATOM   10338 O  O   . LEU C 3  168  ? -42.026 -26.498  53.609  1.00 107.72 ?  168  LEU C O   1 
ATOM   10339 C  CB  . LEU C 3  168  ? -41.157 -27.239  50.656  1.00 99.08  ?  168  LEU C CB  1 
ATOM   10340 C  CG  . LEU C 3  168  ? -41.239 -26.923  49.159  1.00 92.41  ?  168  LEU C CG  1 
ATOM   10341 C  CD1 . LEU C 3  168  ? -41.916 -28.058  48.409  1.00 79.75  ?  168  LEU C CD1 1 
ATOM   10342 C  CD2 . LEU C 3  168  ? -41.966 -25.607  48.915  1.00 86.61  ?  168  LEU C CD2 1 
ATOM   10343 N  N   . ALA C 3  169  ? -39.797 -26.830  53.651  1.00 74.47  ?  169  ALA C N   1 
ATOM   10344 C  CA  . ALA C 3  169  ? -39.790 -27.098  55.085  1.00 76.86  ?  169  ALA C CA  1 
ATOM   10345 C  C   . ALA C 3  169  ? -39.987 -25.813  55.879  1.00 85.28  ?  169  ALA C C   1 
ATOM   10346 O  O   . ALA C 3  169  ? -40.742 -25.791  56.859  1.00 85.75  ?  169  ALA C O   1 
ATOM   10347 C  CB  . ALA C 3  169  ? -38.487 -27.789  55.485  1.00 79.66  ?  169  ALA C CB  1 
ATOM   10348 N  N   . TRP C 3  170  ? -39.310 -24.733  55.474  1.00 62.26  ?  170  TRP C N   1 
ATOM   10349 C  CA  . TRP C 3  170  ? -39.605 -23.423  56.045  1.00 59.58  ?  170  TRP C CA  1 
ATOM   10350 C  C   . TRP C 3  170  ? -41.065 -23.063  55.824  1.00 63.29  ?  170  TRP C C   1 
ATOM   10351 O  O   . TRP C 3  170  ? -41.709 -22.462  56.691  1.00 71.36  ?  170  TRP C O   1 
ATOM   10352 C  CB  . TRP C 3  170  ? -38.715 -22.347  55.420  1.00 53.44  ?  170  TRP C CB  1 
ATOM   10353 C  CG  . TRP C 3  170  ? -37.260 -22.676  55.338  1.00 52.11  ?  170  TRP C CG  1 
ATOM   10354 C  CD1 . TRP C 3  170  ? -36.562 -23.551  56.119  1.00 50.31  ?  170  TRP C CD1 1 
ATOM   10355 C  CD2 . TRP C 3  170  ? -36.320 -22.134  54.404  1.00 55.88  ?  170  TRP C CD2 1 
ATOM   10356 N  NE1 . TRP C 3  170  ? -35.243 -23.581  55.731  1.00 45.84  ?  170  TRP C NE1 1 
ATOM   10357 C  CE2 . TRP C 3  170  ? -35.070 -22.720  54.679  1.00 53.86  ?  170  TRP C CE2 1 
ATOM   10358 C  CE3 . TRP C 3  170  ? -36.414 -21.205  53.362  1.00 48.57  ?  170  TRP C CE3 1 
ATOM   10359 C  CZ2 . TRP C 3  170  ? -33.926 -22.411  53.948  1.00 52.56  ?  170  TRP C CZ2 1 
ATOM   10360 C  CZ3 . TRP C 3  170  ? -35.277 -20.899  52.639  1.00 42.28  ?  170  TRP C CZ3 1 
ATOM   10361 C  CH2 . TRP C 3  170  ? -34.049 -21.499  52.936  1.00 48.04  ?  170  TRP C CH2 1 
ATOM   10362 N  N   . ASP C 3  171  ? -41.603 -23.432  54.661  1.00 108.54 ?  171  ASP C N   1 
ATOM   10363 C  CA  . ASP C 3  171  ? -42.972 -23.069  54.316  1.00 116.45 ?  171  ASP C CA  1 
ATOM   10364 C  C   . ASP C 3  171  ? -43.970 -23.772  55.227  1.00 112.32 ?  171  ASP C C   1 
ATOM   10365 O  O   . ASP C 3  171  ? -44.989 -23.185  55.612  1.00 115.70 ?  171  ASP C O   1 
ATOM   10366 C  CB  . ASP C 3  171  ? -43.232 -23.407  52.847  1.00 130.60 ?  171  ASP C CB  1 
ATOM   10367 C  CG  . ASP C 3  171  ? -44.536 -22.833  52.337  1.00 144.27 ?  171  ASP C CG  1 
ATOM   10368 O  OD1 . ASP C 3  171  ? -45.167 -22.054  53.077  1.00 151.17 ?  171  ASP C OD1 1 
ATOM   10369 O  OD2 . ASP C 3  171  ? -44.932 -23.169  51.198  1.00 140.13 -1 171  ASP C OD2 1 
ATOM   10370 N  N   . VAL C 3  172  ? -43.686 -25.024  55.589  1.00 83.75  ?  172  VAL C N   1 
ATOM   10371 C  CA  . VAL C 3  172  ? -44.571 -25.763  56.486  1.00 87.18  ?  172  VAL C CA  1 
ATOM   10372 C  C   . VAL C 3  172  ? -44.592 -25.111  57.862  1.00 89.60  ?  172  VAL C C   1 
ATOM   10373 O  O   . VAL C 3  172  ? -45.657 -24.884  58.447  1.00 88.33  ?  172  VAL C O   1 
ATOM   10374 C  CB  . VAL C 3  172  ? -44.145 -27.240  56.567  1.00 85.99  ?  172  VAL C CB  1 
ATOM   10375 C  CG1 . VAL C 3  172  ? -44.764 -27.914  57.788  1.00 89.43  ?  172  VAL C CG1 1 
ATOM   10376 C  CG2 . VAL C 3  172  ? -44.538 -27.974  55.296  1.00 85.76  ?  172  VAL C CG2 1 
ATOM   10377 N  N   . PHE C 3  173  ? -43.409 -24.794  58.396  1.00 85.18  ?  173  PHE C N   1 
ATOM   10378 C  CA  . PHE C 3  173  ? -43.332 -24.134  59.694  1.00 75.30  ?  173  PHE C CA  1 
ATOM   10379 C  C   . PHE C 3  173  ? -43.945 -22.740  59.652  1.00 81.99  ?  173  PHE C C   1 
ATOM   10380 O  O   . PHE C 3  173  ? -44.515 -22.280  60.648  1.00 84.68  ?  173  PHE C O   1 
ATOM   10381 C  CB  . PHE C 3  173  ? -41.875 -24.055  60.151  1.00 72.07  ?  173  PHE C CB  1 
ATOM   10382 C  CG  . PHE C 3  173  ? -41.433 -25.223  60.984  1.00 76.16  ?  173  PHE C CG  1 
ATOM   10383 C  CD1 . PHE C 3  173  ? -41.211 -26.462  60.405  1.00 85.35  ?  173  PHE C CD1 1 
ATOM   10384 C  CD2 . PHE C 3  173  ? -41.220 -25.078  62.345  1.00 78.65  ?  173  PHE C CD2 1 
ATOM   10385 C  CE1 . PHE C 3  173  ? -40.799 -27.536  61.171  1.00 84.45  ?  173  PHE C CE1 1 
ATOM   10386 C  CE2 . PHE C 3  173  ? -40.807 -26.147  63.115  1.00 72.71  ?  173  PHE C CE2 1 
ATOM   10387 C  CZ  . PHE C 3  173  ? -40.597 -27.377  62.528  1.00 78.60  ?  173  PHE C CZ  1 
ATOM   10388 N  N   . ALA C 3  174  ? -43.841 -22.055  58.511  1.00 65.65  ?  174  ALA C N   1 
ATOM   10389 C  CA  . ALA C 3  174  ? -44.338 -20.685  58.422  1.00 62.16  ?  174  ALA C CA  1 
ATOM   10390 C  C   . ALA C 3  174  ? -45.861 -20.646  58.411  1.00 61.97  ?  174  ALA C C   1 
ATOM   10391 O  O   . ALA C 3  174  ? -46.474 -19.877  59.160  1.00 64.24  ?  174  ALA C O   1 
ATOM   10392 C  CB  . ALA C 3  174  ? -43.772 -20.000  57.178  1.00 62.02  ?  174  ALA C CB  1 
ATOM   10393 N  N   . ILE C 3  175  ? -46.493 -21.462  57.560  1.00 76.38  ?  175  ILE C N   1 
ATOM   10394 C  CA  . ILE C 3  175  ? -47.954 -21.473  57.493  1.00 75.12  ?  175  ILE C CA  1 
ATOM   10395 C  C   . ILE C 3  175  ? -48.549 -21.941  58.817  1.00 80.24  ?  175  ILE C C   1 
ATOM   10396 O  O   . ILE C 3  175  ? -49.547 -21.388  59.294  1.00 82.92  ?  175  ILE C O   1 
ATOM   10397 C  CB  . ILE C 3  175  ? -48.440 -22.346  56.320  1.00 71.48  ?  175  ILE C CB  1 
ATOM   10398 C  CG1 . ILE C 3  175  ? -47.939 -21.799  54.985  1.00 77.95  ?  175  ILE C CG1 1 
ATOM   10399 C  CG2 . ILE C 3  175  ? -49.959 -22.434  56.311  1.00 58.48  ?  175  ILE C CG2 1 
ATOM   10400 C  CD1 . ILE C 3  175  ? -48.053 -22.800  53.857  1.00 90.98  ?  175  ILE C CD1 1 
ATOM   10401 N  N   . SER C 3  176  ? -47.950 -22.966  59.429  1.00 71.95  ?  176  SER C N   1 
ATOM   10402 C  CA  . SER C 3  176  ? -48.454 -23.465  60.705  1.00 65.55  ?  176  SER C CA  1 
ATOM   10403 C  C   . SER C 3  176  ? -48.395 -22.383  61.776  1.00 71.31  ?  176  SER C C   1 
ATOM   10404 O  O   . SER C 3  176  ? -49.360 -22.176  62.522  1.00 66.76  ?  176  SER C O   1 
ATOM   10405 C  CB  . SER C 3  176  ? -47.660 -24.698  61.138  1.00 65.71  ?  176  SER C CB  1 
ATOM   10406 O  OG  . SER C 3  176  ? -47.792 -25.747  60.196  1.00 72.45  ?  176  SER C OG  1 
ATOM   10407 N  N   . THR C 3  177  ? -47.267 -21.675  61.862  1.00 76.02  ?  177  THR C N   1 
ATOM   10408 C  CA  . THR C 3  177  ? -47.153 -20.591  62.832  1.00 74.88  ?  177  THR C CA  1 
ATOM   10409 C  C   . THR C 3  177  ? -48.087 -19.440  62.481  1.00 76.99  ?  177  THR C C   1 
ATOM   10410 O  O   . THR C 3  177  ? -48.725 -18.860  63.366  1.00 84.63  ?  177  THR C O   1 
ATOM   10411 C  CB  . THR C 3  177  ? -45.707 -20.102  62.907  1.00 76.46  ?  177  THR C CB  1 
ATOM   10412 O  OG1 . THR C 3  177  ? -44.843 -21.207  63.196  1.00 71.07  ?  177  THR C OG1 1 
ATOM   10413 C  CG2 . THR C 3  177  ? -45.555 -19.058  64.002  1.00 79.31  ?  177  THR C CG2 1 
ATOM   10414 N  N   . TYR C 3  178  ? -48.184 -19.102  61.193  1.00 65.71  ?  178  TYR C N   1 
ATOM   10415 C  CA  . TYR C 3  178  ? -49.060 -18.013  60.770  1.00 67.37  ?  178  TYR C CA  1 
ATOM   10416 C  C   . TYR C 3  178  ? -50.516 -18.319  61.101  1.00 73.69  ?  178  TYR C C   1 
ATOM   10417 O  O   . TYR C 3  178  ? -51.244 -17.458  61.608  1.00 80.91  ?  178  TYR C O   1 
ATOM   10418 C  CB  . TYR C 3  178  ? -48.886 -17.760  59.271  1.00 70.35  ?  178  TYR C CB  1 
ATOM   10419 C  CG  . TYR C 3  178  ? -49.613 -16.542  58.743  1.00 73.37  ?  178  TYR C CG  1 
ATOM   10420 C  CD1 . TYR C 3  178  ? -49.863 -15.443  59.557  1.00 69.74  ?  178  TYR C CD1 1 
ATOM   10421 C  CD2 . TYR C 3  178  ? -50.046 -16.491  57.424  1.00 75.39  ?  178  TYR C CD2 1 
ATOM   10422 C  CE1 . TYR C 3  178  ? -50.527 -14.330  59.071  1.00 69.45  ?  178  TYR C CE1 1 
ATOM   10423 C  CE2 . TYR C 3  178  ? -50.709 -15.383  56.930  1.00 77.36  ?  178  TYR C CE2 1 
ATOM   10424 C  CZ  . TYR C 3  178  ? -50.947 -14.307  57.757  1.00 78.37  ?  178  TYR C CZ  1 
ATOM   10425 O  OH  . TYR C 3  178  ? -51.608 -13.205  57.264  1.00 88.97  ?  178  TYR C OH  1 
ATOM   10426 N  N   . ALA C 3  179  ? -50.957 -19.550  60.829  1.00 65.04  ?  179  ALA C N   1 
ATOM   10427 C  CA  . ALA C 3  179  ? -52.353 -19.902  61.067  1.00 65.76  ?  179  ALA C CA  1 
ATOM   10428 C  C   . ALA C 3  179  ? -52.671 -19.955  62.556  1.00 71.48  ?  179  ALA C C   1 
ATOM   10429 O  O   . ALA C 3  179  ? -53.726 -19.476  62.988  1.00 78.28  ?  179  ALA C O   1 
ATOM   10430 C  CB  . ALA C 3  179  ? -52.680 -21.237  60.400  1.00 62.39  ?  179  ALA C CB  1 
ATOM   10431 N  N   . THR C 3  180  ? -51.774 -20.532  63.358  1.00 91.86  ?  180  THR C N   1 
ATOM   10432 C  CA  . THR C 3  180  ? -52.043 -20.665  64.786  1.00 97.47  ?  180  THR C CA  1 
ATOM   10433 C  C   . THR C 3  180  ? -52.015 -19.314  65.491  1.00 93.65  ?  180  THR C C   1 
ATOM   10434 O  O   . THR C 3  180  ? -52.871 -19.033  66.338  1.00 91.85  ?  180  THR C O   1 
ATOM   10435 C  CB  . THR C 3  180  ? -51.039 -21.623  65.426  1.00 94.74  ?  180  THR C CB  1 
ATOM   10436 O  OG1 . THR C 3  180  ? -49.712 -21.273  65.013  1.00 99.18  ?  180  THR C OG1 1 
ATOM   10437 C  CG2 . THR C 3  180  ? -51.336 -23.059  65.016  1.00 96.84  ?  180  THR C CG2 1 
ATOM   10438 N  N   . VAL C 3  181  ? -51.039 -18.465  65.160  1.00 79.75  ?  181  VAL C N   1 
ATOM   10439 C  CA  . VAL C 3  181  ? -50.940 -17.164  65.816  1.00 82.90  ?  181  VAL C CA  1 
ATOM   10440 C  C   . VAL C 3  181  ? -52.095 -16.261  65.398  1.00 80.65  ?  181  VAL C C   1 
ATOM   10441 O  O   . VAL C 3  181  ? -52.648 -15.521  66.220  1.00 86.32  ?  181  VAL C O   1 
ATOM   10442 C  CB  . VAL C 3  181  ? -49.573 -16.518  65.522  1.00 84.30  ?  181  VAL C CB  1 
ATOM   10443 C  CG1 . VAL C 3  181  ? -49.523 -15.101  66.068  1.00 72.45  ?  181  VAL C CG1 1 
ATOM   10444 C  CG2 . VAL C 3  181  ? -48.457 -17.353  66.128  1.00 81.23  ?  181  VAL C CG2 1 
ATOM   10445 N  N   . SER C 3  182  ? -52.484 -16.308  64.122  1.00 81.51  ?  182  SER C N   1 
ATOM   10446 C  CA  . SER C 3  182  ? -53.618 -15.503  63.676  1.00 83.56  ?  182  SER C CA  1 
ATOM   10447 C  C   . SER C 3  182  ? -54.922 -15.975  64.305  1.00 83.75  ?  182  SER C C   1 
ATOM   10448 O  O   . SER C 3  182  ? -55.829 -15.166  64.530  1.00 88.27  ?  182  SER C O   1 
ATOM   10449 C  CB  . SER C 3  182  ? -53.726 -15.537  62.153  1.00 85.98  ?  182  SER C CB  1 
ATOM   10450 O  OG  . SER C 3  182  ? -54.242 -16.779  61.707  1.00 84.07  ?  182  SER C OG  1 
ATOM   10451 N  N   . LEU C 3  183  ? -55.034 -17.273  64.596  1.00 66.40  ?  183  LEU C N   1 
ATOM   10452 C  CA  . LEU C 3  183  ? -56.253 -17.792  65.207  1.00 63.83  ?  183  LEU C CA  1 
ATOM   10453 C  C   . LEU C 3  183  ? -56.348 -17.387  66.672  1.00 69.34  ?  183  LEU C C   1 
ATOM   10454 O  O   . LEU C 3  183  ? -57.409 -16.955  67.139  1.00 71.70  ?  183  LEU C O   1 
ATOM   10455 C  CB  . LEU C 3  183  ? -56.309 -19.313  65.061  1.00 58.98  ?  183  LEU C CB  1 
ATOM   10456 C  CG  . LEU C 3  183  ? -57.504 -20.017  65.709  1.00 59.02  ?  183  LEU C CG  1 
ATOM   10457 C  CD1 . LEU C 3  183  ? -58.793 -19.689  64.972  1.00 57.09  ?  183  LEU C CD1 1 
ATOM   10458 C  CD2 . LEU C 3  183  ? -57.279 -21.521  65.756  1.00 56.98  ?  183  LEU C CD2 1 
ATOM   10459 N  N   . VAL C 3  184  ? -55.248 -17.517  67.417  1.00 80.72  ?  184  VAL C N   1 
ATOM   10460 C  CA  . VAL C 3  184  ? -55.284 -17.160  68.832  1.00 78.59  ?  184  VAL C CA  1 
ATOM   10461 C  C   . VAL C 3  184  ? -55.402 -15.650  69.004  1.00 88.26  ?  184  VAL C C   1 
ATOM   10462 O  O   . VAL C 3  184  ? -56.024 -15.178  69.963  1.00 103.69 ?  184  VAL C O   1 
ATOM   10463 C  CB  . VAL C 3  184  ? -54.053 -17.725  69.567  1.00 66.92  ?  184  VAL C CB  1 
ATOM   10464 C  CG1 . VAL C 3  184  ? -54.007 -19.241  69.435  1.00 64.21  ?  184  VAL C CG1 1 
ATOM   10465 C  CG2 . VAL C 3  184  ? -52.768 -17.100  69.047  1.00 77.46  ?  184  VAL C CG2 1 
ATOM   10466 N  N   . PHE C 3  185  ? -54.827 -14.869  68.087  1.00 80.93  ?  185  PHE C N   1 
ATOM   10467 C  CA  . PHE C 3  185  ? -54.987 -13.420  68.155  1.00 85.11  ?  185  PHE C CA  1 
ATOM   10468 C  C   . PHE C 3  185  ? -56.420 -13.012  67.840  1.00 88.94  ?  185  PHE C C   1 
ATOM   10469 O  O   . PHE C 3  185  ? -56.960 -12.087  68.459  1.00 100.47 ?  185  PHE C O   1 
ATOM   10470 C  CB  . PHE C 3  185  ? -54.013 -12.734  67.197  1.00 92.14  ?  185  PHE C CB  1 
ATOM   10471 C  CG  . PHE C 3  185  ? -53.958 -11.242  67.357  1.00 93.98  ?  185  PHE C CG  1 
ATOM   10472 C  CD1 . PHE C 3  185  ? -53.438 -10.674  68.507  1.00 90.13  ?  185  PHE C CD1 1 
ATOM   10473 C  CD2 . PHE C 3  185  ? -54.435 -10.407  66.361  1.00 94.47  ?  185  PHE C CD2 1 
ATOM   10474 C  CE1 . PHE C 3  185  ? -53.387 -9.301   68.659  1.00 88.08  ?  185  PHE C CE1 1 
ATOM   10475 C  CE2 . PHE C 3  185  ? -54.388 -9.033   66.508  1.00 101.99 ?  185  PHE C CE2 1 
ATOM   10476 C  CZ  . PHE C 3  185  ? -53.863 -8.480   67.658  1.00 92.95  ?  185  PHE C CZ  1 
ATOM   10477 N  N   . TRP C 3  186  ? -57.050 -13.689  66.878  1.00 83.42  ?  186  TRP C N   1 
ATOM   10478 C  CA  . TRP C 3  186  ? -58.444 -13.403  66.557  1.00 87.14  ?  186  TRP C CA  1 
ATOM   10479 C  C   . TRP C 3  186  ? -59.359 -13.752  67.723  1.00 90.34  ?  186  TRP C C   1 
ATOM   10480 O  O   . TRP C 3  186  ? -60.298 -13.007  68.029  1.00 96.36  ?  186  TRP C O   1 
ATOM   10481 C  CB  . TRP C 3  186  ? -58.853 -14.170  65.299  1.00 85.48  ?  186  TRP C CB  1 
ATOM   10482 C  CG  . TRP C 3  186  ? -60.106 -13.668  64.655  1.00 77.78  ?  186  TRP C CG  1 
ATOM   10483 C  CD1 . TRP C 3  186  ? -60.380 -12.385  64.281  1.00 81.63  ?  186  TRP C CD1 1 
ATOM   10484 C  CD2 . TRP C 3  186  ? -61.254 -14.444  64.296  1.00 76.55  ?  186  TRP C CD2 1 
ATOM   10485 N  NE1 . TRP C 3  186  ? -61.629 -12.314  63.716  1.00 87.74  ?  186  TRP C NE1 1 
ATOM   10486 C  CE2 . TRP C 3  186  ? -62.187 -13.565  63.714  1.00 85.93  ?  186  TRP C CE2 1 
ATOM   10487 C  CE3 . TRP C 3  186  ? -61.585 -15.798  64.414  1.00 77.25  ?  186  TRP C CE3 1 
ATOM   10488 C  CZ2 . TRP C 3  186  ? -63.429 -13.994  63.250  1.00 88.15  ?  186  TRP C CZ2 1 
ATOM   10489 C  CZ3 . TRP C 3  186  ? -62.817 -16.222  63.953  1.00 78.61  ?  186  TRP C CZ3 1 
ATOM   10490 C  CH2 . TRP C 3  186  ? -63.724 -15.323  63.378  1.00 85.10  ?  186  TRP C CH2 1 
ATOM   10491 N  N   . LEU C 3  187  ? -59.097 -14.877  68.393  1.00 86.09  ?  187  LEU C N   1 
ATOM   10492 C  CA  . LEU C 3  187  ? -59.934 -15.280  69.519  1.00 83.59  ?  187  LEU C CA  1 
ATOM   10493 C  C   . LEU C 3  187  ? -59.737 -14.357  70.716  1.00 99.00  ?  187  LEU C C   1 
ATOM   10494 O  O   . LEU C 3  187  ? -60.694 -14.064  71.442  1.00 104.25 ?  187  LEU C O   1 
ATOM   10495 C  CB  . LEU C 3  187  ? -59.641 -16.731  69.897  1.00 85.78  ?  187  LEU C CB  1 
ATOM   10496 C  CG  . LEU C 3  187  ? -60.016 -17.778  68.845  1.00 85.08  ?  187  LEU C CG  1 
ATOM   10497 C  CD1 . LEU C 3  187  ? -59.789 -19.187  69.373  1.00 73.83  ?  187  LEU C CD1 1 
ATOM   10498 C  CD2 . LEU C 3  187  ? -61.458 -17.593  68.396  1.00 83.90  ?  187  LEU C CD2 1 
ATOM   10499 N  N   . VAL C 3  188  ? -58.505 -13.893  70.941  1.00 102.47 ?  188  VAL C N   1 
ATOM   10500 C  CA  . VAL C 3  188  ? -58.263 -12.923  72.007  1.00 100.98 ?  188  VAL C CA  1 
ATOM   10501 C  C   . VAL C 3  188  ? -59.036 -11.638  71.737  1.00 101.97 ?  188  VAL C C   1 
ATOM   10502 O  O   . VAL C 3  188  ? -59.618 -11.041  72.652  1.00 114.67 ?  188  VAL C O   1 
ATOM   10503 C  CB  . VAL C 3  188  ? -56.752 -12.661  72.162  1.00 98.61  ?  188  VAL C CB  1 
ATOM   10504 C  CG1 . VAL C 3  188  ? -56.504 -11.390  72.958  1.00 95.95  ?  188  VAL C CG1 1 
ATOM   10505 C  CG2 . VAL C 3  188  ? -56.082 -13.841  72.845  1.00 101.92 ?  188  VAL C CG2 1 
ATOM   10506 N  N   . GLY C 3  189  ? -59.076 -11.204  70.475  1.00 91.70  ?  189  GLY C N   1 
ATOM   10507 C  CA  . GLY C 3  189  ? -59.846 -10.021  70.131  1.00 95.99  ?  189  GLY C CA  1 
ATOM   10508 C  C   . GLY C 3  189  ? -61.344 -10.241  70.186  1.00 102.46 ?  189  GLY C C   1 
ATOM   10509 O  O   . GLY C 3  189  ? -62.107 -9.290   70.377  1.00 103.18 ?  189  GLY C O   1 
ATOM   10510 N  N   . LEU C 3  190  ? -61.787 -11.490  70.024  1.00 104.51 ?  190  LEU C N   1 
ATOM   10511 C  CA  . LEU C 3  190  ? -63.210 -11.804  70.053  1.00 104.21 ?  190  LEU C CA  1 
ATOM   10512 C  C   . LEU C 3  190  ? -63.757 -11.985  71.464  1.00 106.36 ?  190  LEU C C   1 
ATOM   10513 O  O   . LEU C 3  190  ? -64.979 -11.965  71.641  1.00 109.58 ?  190  LEU C O   1 
ATOM   10514 C  CB  . LEU C 3  190  ? -63.489 -13.072  69.245  1.00 105.84 ?  190  LEU C CB  1 
ATOM   10515 C  CG  . LEU C 3  190  ? -63.510 -12.994  67.719  1.00 101.25 ?  190  LEU C CG  1 
ATOM   10516 C  CD1 . LEU C 3  190  ? -63.490 -14.391  67.132  1.00 96.37  ?  190  LEU C CD1 1 
ATOM   10517 C  CD2 . LEU C 3  190  ? -64.747 -12.254  67.259  1.00 94.19  ?  190  LEU C CD2 1 
ATOM   10518 N  N   . ILE C 3  191  ? -62.889 -12.163  72.464  1.00 109.93 ?  191  ILE C N   1 
ATOM   10519 C  CA  . ILE C 3  191  ? -63.367 -12.448  73.820  1.00 111.77 ?  191  ILE C CA  1 
ATOM   10520 C  C   . ILE C 3  191  ? -64.268 -11.344  74.365  1.00 109.17 ?  191  ILE C C   1 
ATOM   10521 O  O   . ILE C 3  191  ? -65.353 -11.662  74.878  1.00 108.43 ?  191  ILE C O   1 
ATOM   10522 C  CB  . ILE C 3  191  ? -62.177 -12.756  74.747  1.00 111.69 ?  191  ILE C CB  1 
ATOM   10523 C  CG1 . ILE C 3  191  ? -61.659 -14.173  74.497  1.00 118.72 ?  191  ILE C CG1 1 
ATOM   10524 C  CG2 . ILE C 3  191  ? -62.575 -12.581  76.204  1.00 113.21 ?  191  ILE C CG2 1 
ATOM   10525 C  CD1 . ILE C 3  191  ? -60.511 -14.573  75.399  1.00 118.44 ?  191  ILE C CD1 1 
ATOM   10526 N  N   . PRO C 3  192  ? -63.903 -10.055  74.298  1.00 99.49  ?  192  PRO C N   1 
ATOM   10527 C  CA  . PRO C 3  192  ? -64.845 -9.031   74.782  1.00 98.46  ?  192  PRO C CA  1 
ATOM   10528 C  C   . PRO C 3  192  ? -66.143 -8.992   73.993  1.00 103.75 ?  192  PRO C C   1 
ATOM   10529 O  O   . PRO C 3  192  ? -67.212 -8.795   74.584  1.00 108.82 ?  192  PRO C O   1 
ATOM   10530 C  CB  . PRO C 3  192  ? -64.048 -7.726   74.641  1.00 92.27  ?  192  PRO C CB  1 
ATOM   10531 C  CG  . PRO C 3  192  ? -62.621 -8.155   74.620  1.00 97.69  ?  192  PRO C CG  1 
ATOM   10532 C  CD  . PRO C 3  192  ? -62.629 -9.447   73.875  1.00 100.25 ?  192  PRO C CD  1 
ATOM   10533 N  N   . ASP C 3  193  ? -66.082 -9.178   72.671  1.00 118.12 ?  193  ASP C N   1 
ATOM   10534 C  CA  . ASP C 3  193  ? -67.308 -9.241   71.881  1.00 110.49 ?  193  ASP C CA  1 
ATOM   10535 C  C   . ASP C 3  193  ? -68.152 -10.454  72.249  1.00 109.32 ?  193  ASP C C   1 
ATOM   10536 O  O   . ASP C 3  193  ? -69.385 -10.388  72.191  1.00 114.97 ?  193  ASP C O   1 
ATOM   10537 C  CB  . ASP C 3  193  ? -66.981 -9.255   70.388  1.00 106.28 ?  193  ASP C CB  1 
ATOM   10538 C  CG  . ASP C 3  193  ? -66.311 -7.978   69.925  1.00 107.02 ?  193  ASP C CG  1 
ATOM   10539 O  OD1 . ASP C 3  193  ? -65.933 -7.158   70.787  1.00 108.37 ?  193  ASP C OD1 1 
ATOM   10540 O  OD2 . ASP C 3  193  ? -66.164 -7.794   68.698  1.00 111.84 -1 193  ASP C OD2 1 
ATOM   10541 N  N   . PHE C 3  194  ? -67.515 -11.568  72.621  1.00 83.64  ?  194  PHE C N   1 
ATOM   10542 C  CA  . PHE C 3  194  ? -68.270 -12.703  73.140  1.00 91.38  ?  194  PHE C CA  1 
ATOM   10543 C  C   . PHE C 3  194  ? -69.007 -12.325  74.418  1.00 94.89  ?  194  PHE C C   1 
ATOM   10544 O  O   . PHE C 3  194  ? -70.152 -12.743  74.632  1.00 101.73 ?  194  PHE C O   1 
ATOM   10545 C  CB  . PHE C 3  194  ? -67.340 -13.889  73.393  1.00 91.05  ?  194  PHE C CB  1 
ATOM   10546 C  CG  . PHE C 3  194  ? -66.796 -14.517  72.144  1.00 85.30  ?  194  PHE C CG  1 
ATOM   10547 C  CD1 . PHE C 3  194  ? -67.563 -14.584  70.995  1.00 82.46  ?  194  PHE C CD1 1 
ATOM   10548 C  CD2 . PHE C 3  194  ? -65.521 -15.059  72.127  1.00 86.27  ?  194  PHE C CD2 1 
ATOM   10549 C  CE1 . PHE C 3  194  ? -67.065 -15.167  69.847  1.00 86.35  ?  194  PHE C CE1 1 
ATOM   10550 C  CE2 . PHE C 3  194  ? -65.018 -15.646  70.983  1.00 89.89  ?  194  PHE C CE2 1 
ATOM   10551 C  CZ  . PHE C 3  194  ? -65.792 -15.699  69.840  1.00 90.15  ?  194  PHE C CZ  1 
ATOM   10552 N  N   . ALA C 3  195  ? -68.368 -11.529  75.278  1.00 99.79  ?  195  ALA C N   1 
ATOM   10553 C  CA  . ALA C 3  195  ? -69.013 -11.101  76.515  1.00 108.61 ?  195  ALA C CA  1 
ATOM   10554 C  C   . ALA C 3  195  ? -70.203 -10.193  76.233  1.00 109.19 ?  195  ALA C C   1 
ATOM   10555 O  O   . ALA C 3  195  ? -71.250 -10.315  76.880  1.00 116.65 ?  195  ALA C O   1 
ATOM   10556 C  CB  . ALA C 3  195  ? -68.002 -10.397  77.418  1.00 113.39 ?  195  ALA C CB  1 
ATOM   10557 N  N   . THR C 3  196  ? -70.063 -9.277   75.271  1.00 85.97  ?  196  THR C N   1 
ATOM   10558 C  CA  . THR C 3  196  ? -71.179 -8.405   74.920  1.00 84.24  ?  196  THR C CA  1 
ATOM   10559 C  C   . THR C 3  196  ? -72.312 -9.180   74.261  1.00 82.72  ?  196  THR C C   1 
ATOM   10560 O  O   . THR C 3  196  ? -73.474 -8.766   74.348  1.00 82.40  ?  196  THR C O   1 
ATOM   10561 C  CB  . THR C 3  196  ? -70.709 -7.277   73.998  1.00 83.73  ?  196  THR C CB  1 
ATOM   10562 O  OG1 . THR C 3  196  ? -70.375 -7.815   72.712  1.00 95.59  ?  196  THR C OG1 1 
ATOM   10563 C  CG2 . THR C 3  196  ? -69.491 -6.571   74.582  1.00 83.83  ?  196  THR C CG2 1 
ATOM   10564 N  N   . LEU C 3  197  ? -72.002 -10.299  73.603  1.00 101.65 ?  197  LEU C N   1 
ATOM   10565 C  CA  . LEU C 3  197  ? -73.048 -11.098  72.973  1.00 107.03 ?  197  LEU C CA  1 
ATOM   10566 C  C   . LEU C 3  197  ? -73.806 -11.938  73.994  1.00 108.30 ?  197  LEU C C   1 
ATOM   10567 O  O   . LEU C 3  197  ? -75.039 -12.006  73.948  1.00 111.55 ?  197  LEU C O   1 
ATOM   10568 C  CB  . LEU C 3  197  ? -72.453 -11.990  71.883  1.00 103.87 ?  197  LEU C CB  1 
ATOM   10569 C  CG  . LEU C 3  197  ? -72.095 -11.315  70.557  1.00 98.07  ?  197  LEU C CG  1 
ATOM   10570 C  CD1 . LEU C 3  197  ? -71.933 -12.353  69.459  1.00 102.54 ?  197  LEU C CD1 1 
ATOM   10571 C  CD2 . LEU C 3  197  ? -73.147 -10.286  70.170  1.00 94.69  ?  197  LEU C CD2 1 
ATOM   10572 N  N   . ARG C 3  198  ? -73.094 -12.585  74.921  1.00 125.67 ?  198  ARG C N   1 
ATOM   10573 C  CA  . ARG C 3  198  ? -73.769 -13.351  75.963  1.00 133.24 ?  198  ARG C CA  1 
ATOM   10574 C  C   . ARG C 3  198  ? -74.492 -12.460  76.964  1.00 135.88 ?  198  ARG C C   1 
ATOM   10575 O  O   . ARG C 3  198  ? -75.295 -12.969  77.753  1.00 135.29 ?  198  ARG C O   1 
ATOM   10576 C  CB  . ARG C 3  198  ? -72.771 -14.267  76.682  1.00 133.13 ?  198  ARG C CB  1 
ATOM   10577 C  CG  . ARG C 3  198  ? -71.574 -13.574  77.327  1.00 128.85 ?  198  ARG C CG  1 
ATOM   10578 C  CD  . ARG C 3  198  ? -71.821 -13.194  78.780  1.00 128.19 ?  198  ARG C CD  1 
ATOM   10579 N  NE  . ARG C 3  198  ? -70.611 -12.684  79.413  1.00 127.09 ?  198  ARG C NE  1 
ATOM   10580 C  CZ  . ARG C 3  198  ? -70.565 -12.152  80.627  1.00 140.06 ?  198  ARG C CZ  1 
ATOM   10581 N  NH1 . ARG C 3  198  ? -71.651 -12.040  81.375  1.00 148.95 ?  198  ARG C NH1 1 
ATOM   10582 N  NH2 . ARG C 3  198  ? -69.398 -11.730  81.106  1.00 141.72 ?  198  ARG C NH2 1 
ATOM   10583 N  N   . ASP C 3  199  ? -74.225 -11.154  76.953  1.00 133.15 ?  199  ASP C N   1 
ATOM   10584 C  CA  . ASP C 3  199  ? -74.992 -10.214  77.758  1.00 131.75 ?  199  ASP C CA  1 
ATOM   10585 C  C   . ASP C 3  199  ? -76.263 -9.756   77.057  1.00 133.55 ?  199  ASP C C   1 
ATOM   10586 O  O   . ASP C 3  199  ? -77.189 -9.285   77.726  1.00 139.83 ?  199  ASP C O   1 
ATOM   10587 C  CB  . ASP C 3  199  ? -74.127 -9.002   78.109  1.00 134.73 ?  199  ASP C CB  1 
ATOM   10588 C  CG  . ASP C 3  199  ? -73.298 -9.218   79.361  1.00 136.65 ?  199  ASP C CG  1 
ATOM   10589 O  OD1 . ASP C 3  199  ? -73.573 -10.187  80.100  1.00 133.31 ?  199  ASP C OD1 1 
ATOM   10590 O  OD2 . ASP C 3  199  ? -72.374 -8.415   79.610  1.00 133.16 -1 199  ASP C OD2 1 
ATOM   10591 N  N   . ARG C 3  200  ? -76.327 -9.888   75.733  1.00 129.62 ?  200  ARG C N   1 
ATOM   10592 C  CA  . ARG C 3  200  ? -77.488 -9.501   74.943  1.00 128.40 ?  200  ARG C CA  1 
ATOM   10593 C  C   . ARG C 3  200  ? -78.164 -10.693  74.278  1.00 128.42 ?  200  ARG C C   1 
ATOM   10594 O  O   . ARG C 3  200  ? -79.066 -10.503  73.455  1.00 123.83 ?  200  ARG C O   1 
ATOM   10595 C  CB  . ARG C 3  200  ? -77.080 -8.479   73.879  1.00 121.66 ?  200  ARG C CB  1 
ATOM   10596 C  CG  . ARG C 3  200  ? -76.349 -7.262   74.417  1.00 132.45 ?  200  ARG C CG  1 
ATOM   10597 C  CD  . ARG C 3  200  ? -75.860 -6.371   73.279  1.00 137.79 ?  200  ARG C CD  1 
ATOM   10598 N  NE  . ARG C 3  200  ? -76.900 -6.088   72.296  1.00 141.11 ?  200  ARG C NE  1 
ATOM   10599 C  CZ  . ARG C 3  200  ? -77.922 -5.265   72.493  1.00 135.78 ?  200  ARG C CZ  1 
ATOM   10600 N  NH1 . ARG C 3  200  ? -78.069 -4.605   73.629  1.00 139.34 ?  200  ARG C NH1 1 
ATOM   10601 N  NH2 . ARG C 3  200  ? -78.816 -5.098   71.522  1.00 126.40 ?  200  ARG C NH2 1 
ATOM   10602 N  N   . ALA C 3  201  ? -77.754 -11.918  74.616  1.00 160.57 ?  201  ALA C N   1 
ATOM   10603 C  CA  . ALA C 3  201  ? -78.235 -13.094  73.899  1.00 166.95 ?  201  ALA C CA  1 
ATOM   10604 C  C   . ALA C 3  201  ? -79.688 -13.426  74.212  1.00 166.28 ?  201  ALA C C   1 
ATOM   10605 O  O   . ALA C 3  201  ? -80.299 -14.204  73.471  1.00 168.19 ?  201  ALA C O   1 
ATOM   10606 C  CB  . ALA C 3  201  ? -77.349 -14.300  74.212  1.00 169.76 ?  201  ALA C CB  1 
ATOM   10607 N  N   . LYS C 3  202  ? -80.246 -12.871  75.290  1.00 140.32 ?  202  LYS C N   1 
ATOM   10608 C  CA  . LYS C 3  202  ? -81.647 -13.070  75.654  1.00 146.98 ?  202  LYS C CA  1 
ATOM   10609 C  C   . LYS C 3  202  ? -81.975 -14.540  75.901  1.00 152.13 ?  202  LYS C C   1 
ATOM   10610 O  O   . LYS C 3  202  ? -82.269 -14.930  77.036  1.00 151.15 ?  202  LYS C O   1 
ATOM   10611 C  CB  . LYS C 3  202  ? -82.566 -12.492  74.573  1.00 148.56 ?  202  LYS C CB  1 
ATOM   10612 C  CG  . LYS C 3  202  ? -84.030 -12.418  74.971  1.00 150.12 ?  202  LYS C CG  1 
ATOM   10613 C  CD  . LYS C 3  202  ? -84.931 -12.401  73.747  1.00 146.84 ?  202  LYS C CD  1 
ATOM   10614 C  CE  . LYS C 3  202  ? -84.892 -13.732  73.016  1.00 157.53 ?  202  LYS C CE  1 
ATOM   10615 N  NZ  . LYS C 3  202  ? -85.332 -14.857  73.884  1.00 163.88 ?  202  LYS C NZ  1 
ATOM   10616 N  N   . ASN C 3  203  ? -81.936 -15.358  74.851  1.00 162.22 ?  203  ASN C N   1 
ATOM   10617 C  CA  . ASN C 3  203  ? -82.255 -16.774  74.986  1.00 159.51 ?  203  ASN C CA  1 
ATOM   10618 C  C   . ASN C 3  203  ? -81.235 -17.473  75.880  1.00 155.67 ?  203  ASN C C   1 
ATOM   10619 O  O   . ASN C 3  203  ? -80.053 -17.118  75.911  1.00 152.98 ?  203  ASN C O   1 
ATOM   10620 C  CB  . ASN C 3  203  ? -82.302 -17.441  73.610  1.00 158.21 ?  203  ASN C CB  1 
ATOM   10621 C  CG  . ASN C 3  203  ? -82.666 -18.911  73.685  1.00 159.48 ?  203  ASN C CG  1 
ATOM   10622 O  OD1 . ASN C 3  203  ? -81.935 -19.769  73.191  1.00 158.34 ?  203  ASN C OD1 1 
ATOM   10623 N  ND2 . ASN C 3  203  ? -83.803 -19.210  74.304  1.00 168.25 ?  203  ASN C ND2 1 
ATOM   10624 N  N   . ILE C 3  204  ? -81.707 -18.487  76.611  1.00 211.14 ?  204  ILE C N   1 
ATOM   10625 C  CA  . ILE C 3  204  ? -80.864 -19.133  77.613  1.00 214.99 ?  204  ILE C CA  1 
ATOM   10626 C  C   . ILE C 3  204  ? -79.834 -20.050  76.961  1.00 210.69 ?  204  ILE C C   1 
ATOM   10627 O  O   . ILE C 3  204  ? -78.712 -20.188  77.465  1.00 209.85 ?  204  ILE C O   1 
ATOM   10628 C  CB  . ILE C 3  204  ? -81.736 -19.888  78.637  1.00 221.69 ?  204  ILE C CB  1 
ATOM   10629 C  CG1 . ILE C 3  204  ? -80.882 -20.403  79.800  1.00 214.48 ?  204  ILE C CG1 1 
ATOM   10630 C  CG2 . ILE C 3  204  ? -82.516 -21.023  77.976  1.00 215.83 ?  204  ILE C CG2 1 
ATOM   10631 C  CD1 . ILE C 3  204  ? -80.027 -19.336  80.451  1.00 209.38 ?  204  ILE C CD1 1 
ATOM   10632 N  N   . TRP C 3  205  ? -80.177 -20.684  75.841  1.00 150.75 ?  205  TRP C N   1 
ATOM   10633 C  CA  . TRP C 3  205  ? -79.242 -21.595  75.196  1.00 145.94 ?  205  TRP C CA  1 
ATOM   10634 C  C   . TRP C 3  205  ? -78.336 -20.905  74.185  1.00 142.29 ?  205  TRP C C   1 
ATOM   10635 O  O   . TRP C 3  205  ? -77.277 -21.449  73.854  1.00 133.02 ?  205  TRP C O   1 
ATOM   10636 C  CB  . TRP C 3  205  ? -79.995 -22.747  74.526  1.00 147.18 ?  205  TRP C CB  1 
ATOM   10637 C  CG  . TRP C 3  205  ? -80.448 -23.800  75.499  1.00 145.26 ?  205  TRP C CG  1 
ATOM   10638 C  CD1 . TRP C 3  205  ? -81.721 -24.258  75.676  1.00 148.84 ?  205  TRP C CD1 1 
ATOM   10639 C  CD2 . TRP C 3  205  ? -79.632 -24.515  76.439  1.00 146.25 ?  205  TRP C CD2 1 
ATOM   10640 N  NE1 . TRP C 3  205  ? -81.748 -25.219  76.658  1.00 153.25 ?  205  TRP C NE1 1 
ATOM   10641 C  CE2 . TRP C 3  205  ? -80.479 -25.394  77.144  1.00 155.26 ?  205  TRP C CE2 1 
ATOM   10642 C  CE3 . TRP C 3  205  ? -78.267 -24.501  76.751  1.00 144.18 ?  205  TRP C CE3 1 
ATOM   10643 C  CZ2 . TRP C 3  205  ? -80.007 -26.249  78.139  1.00 157.95 ?  205  TRP C CZ2 1 
ATOM   10644 C  CZ3 . TRP C 3  205  ? -77.802 -25.349  77.740  1.00 150.27 ?  205  TRP C CZ3 1 
ATOM   10645 C  CH2 . TRP C 3  205  ? -78.669 -26.211  78.421  1.00 154.14 ?  205  TRP C CH2 1 
ATOM   10646 N  N   . VAL C 3  206  ? -78.722 -19.729  73.686  1.00 153.14 ?  206  VAL C N   1 
ATOM   10647 C  CA  . VAL C 3  206  ? -77.751 -18.878  73.006  1.00 150.26 ?  206  VAL C CA  1 
ATOM   10648 C  C   . VAL C 3  206  ? -76.706 -18.395  74.002  1.00 149.69 ?  206  VAL C C   1 
ATOM   10649 O  O   . VAL C 3  206  ? -75.516 -18.288  73.678  1.00 147.94 ?  206  VAL C O   1 
ATOM   10650 C  CB  . VAL C 3  206  ? -78.457 -17.707  72.301  1.00 150.17 ?  206  VAL C CB  1 
ATOM   10651 C  CG1 . VAL C 3  206  ? -77.459 -16.896  71.490  1.00 143.93 ?  206  VAL C CG1 1 
ATOM   10652 C  CG2 . VAL C 3  206  ? -79.565 -18.230  71.403  1.00 153.80 ?  206  VAL C CG2 1 
ATOM   10653 N  N   . LYS C 3  207  ? -77.131 -18.105  75.230  1.00 123.23 ?  207  LYS C N   1 
ATOM   10654 C  CA  . LYS C 3  207  ? -76.203 -17.958  76.336  1.00 114.50 ?  207  LYS C CA  1 
ATOM   10655 C  C   . LYS C 3  207  ? -75.566 -19.309  76.657  1.00 110.77 ?  207  LYS C C   1 
ATOM   10656 O  O   . LYS C 3  207  ? -75.956 -20.352  76.123  1.00 113.22 ?  207  LYS C O   1 
ATOM   10657 C  CB  . LYS C 3  207  ? -76.917 -17.391  77.563  1.00 126.12 ?  207  LYS C CB  1 
ATOM   10658 C  CG  . LYS C 3  207  ? -77.436 -15.974  77.381  1.00 127.93 ?  207  LYS C CG  1 
ATOM   10659 C  CD  . LYS C 3  207  ? -78.429 -15.601  78.471  1.00 121.23 ?  207  LYS C CD  1 
ATOM   10660 C  CE  . LYS C 3  207  ? -78.950 -14.185  78.286  1.00 116.18 ?  207  LYS C CE  1 
ATOM   10661 N  NZ  . LYS C 3  207  ? -77.848 -13.183  78.304  1.00 112.30 ?  207  LYS C NZ  1 
ATOM   10662 N  N   . ARG C 3  208  ? -74.553 -19.274  77.527  1.00 133.53 ?  208  ARG C N   1 
ATOM   10663 C  CA  . ARG C 3  208  ? -73.757 -20.445  77.891  1.00 134.47 ?  208  ARG C CA  1 
ATOM   10664 C  C   . ARG C 3  208  ? -72.938 -20.956  76.708  1.00 132.81 ?  208  ARG C C   1 
ATOM   10665 O  O   . ARG C 3  208  ? -72.026 -21.769  76.884  1.00 134.10 ?  208  ARG C O   1 
ATOM   10666 C  CB  . ARG C 3  208  ? -74.643 -21.567  78.448  1.00 137.39 ?  208  ARG C CB  1 
ATOM   10667 C  CG  . ARG C 3  208  ? -75.485 -21.166  79.648  1.00 139.52 ?  208  ARG C CG  1 
ATOM   10668 C  CD  . ARG C 3  208  ? -76.574 -22.194  79.920  1.00 141.52 ?  208  ARG C CD  1 
ATOM   10669 N  NE  . ARG C 3  208  ? -77.175 -22.021  81.236  1.00 158.47 ?  208  ARG C NE  1 
ATOM   10670 C  CZ  . ARG C 3  208  ? -78.129 -22.797  81.733  1.00 154.05 ?  208  ARG C CZ  1 
ATOM   10671 N  NH1 . ARG C 3  208  ? -78.623 -23.812  81.043  1.00 153.70 ?  208  ARG C NH1 1 
ATOM   10672 N  NH2 . ARG C 3  208  ? -78.599 -22.548  82.952  1.00 146.52 ?  208  ARG C NH2 1 
ATOM   10673 N  N   . LEU C 3  209  ? -73.258 -20.492  75.501  1.00 108.67 ?  209  LEU C N   1 
ATOM   10674 C  CA  . LEU C 3  209  ? -72.464 -20.785  74.315  1.00 99.32  ?  209  LEU C CA  1 
ATOM   10675 C  C   . LEU C 3  209  ? -71.434 -19.689  74.069  1.00 103.68 ?  209  LEU C C   1 
ATOM   10676 O  O   . LEU C 3  209  ? -70.237 -19.971  73.956  1.00 109.78 ?  209  LEU C O   1 
ATOM   10677 C  CB  . LEU C 3  209  ? -73.377 -20.954  73.097  1.00 93.43  ?  209  LEU C CB  1 
ATOM   10678 C  CG  . LEU C 3  209  ? -72.798 -21.739  71.920  1.00 85.87  ?  209  LEU C CG  1 
ATOM   10679 C  CD1 . LEU C 3  209  ? -72.433 -23.151  72.350  1.00 74.50  ?  209  LEU C CD1 1 
ATOM   10680 C  CD2 . LEU C 3  209  ? -73.776 -21.765  70.757  1.00 83.69  ?  209  LEU C CD2 1 
ATOM   10681 N  N   . TYR C 3  210  ? -71.884 -18.434  73.989  1.00 110.79 ?  210  TYR C N   1 
ATOM   10682 C  CA  . TYR C 3  210  ? -70.955 -17.313  74.038  1.00 108.14 ?  210  TYR C CA  1 
ATOM   10683 C  C   . TYR C 3  210  ? -70.340 -17.148  75.420  1.00 114.48 ?  210  TYR C C   1 
ATOM   10684 O  O   . TYR C 3  210  ? -69.270 -16.543  75.540  1.00 115.07 ?  210  TYR C O   1 
ATOM   10685 C  CB  . TYR C 3  210  ? -71.654 -16.012  73.635  1.00 109.57 ?  210  TYR C CB  1 
ATOM   10686 C  CG  . TYR C 3  210  ? -72.227 -16.003  72.237  1.00 112.53 ?  210  TYR C CG  1 
ATOM   10687 C  CD1 . TYR C 3  210  ? -71.411 -16.199  71.130  1.00 115.49 ?  210  TYR C CD1 1 
ATOM   10688 C  CD2 . TYR C 3  210  ? -73.580 -15.781  72.021  1.00 114.93 ?  210  TYR C CD2 1 
ATOM   10689 C  CE1 . TYR C 3  210  ? -71.929 -16.184  69.848  1.00 113.56 ?  210  TYR C CE1 1 
ATOM   10690 C  CE2 . TYR C 3  210  ? -74.108 -15.765  70.744  1.00 113.51 ?  210  TYR C CE2 1 
ATOM   10691 C  CZ  . TYR C 3  210  ? -73.277 -15.966  69.661  1.00 113.78 ?  210  TYR C CZ  1 
ATOM   10692 O  OH  . TYR C 3  210  ? -73.797 -15.951  68.387  1.00 115.86 ?  210  TYR C OH  1 
ATOM   10693 N  N   . GLY C 3  211  ? -70.996 -17.669  76.460  1.00 137.27 ?  211  GLY C N   1 
ATOM   10694 C  CA  . GLY C 3  211  ? -70.458 -17.537  77.805  1.00 142.64 ?  211  GLY C CA  1 
ATOM   10695 C  C   . GLY C 3  211  ? -69.145 -18.274  77.979  1.00 138.39 ?  211  GLY C C   1 
ATOM   10696 O  O   . GLY C 3  211  ? -68.167 -17.718  78.484  1.00 142.03 ?  211  GLY C O   1 
ATOM   10697 N  N   . ILE C 3  212  ? -69.105 -19.543  77.562  1.00 101.91 ?  212  ILE C N   1 
ATOM   10698 C  CA  . ILE C 3  212  ? -67.854 -20.287  77.609  1.00 105.21 ?  212  ILE C CA  1 
ATOM   10699 C  C   . ILE C 3  212  ? -66.875 -19.792  76.554  1.00 98.12  ?  212  ILE C C   1 
ATOM   10700 O  O   . ILE C 3  212  ? -65.666 -20.011  76.685  1.00 98.16  ?  212  ILE C O   1 
ATOM   10701 C  CB  . ILE C 3  212  ? -68.107 -21.800  77.460  1.00 110.53 ?  212  ILE C CB  1 
ATOM   10702 C  CG1 . ILE C 3  212  ? -68.422 -22.158  76.006  1.00 111.49 ?  212  ILE C CG1 1 
ATOM   10703 C  CG2 . ILE C 3  212  ? -69.222 -22.250  78.391  1.00 119.59 ?  212  ILE C CG2 1 
ATOM   10704 C  CD1 . ILE C 3  212  ? -68.358 -23.642  75.718  1.00 112.54 ?  212  ILE C CD1 1 
ATOM   10705 N  N   . ALA C 3  213  ? -67.365 -19.125  75.506  1.00 87.29  ?  213  ALA C N   1 
ATOM   10706 C  CA  . ALA C 3  213  ? -66.463 -18.507  74.541  1.00 88.34  ?  213  ALA C CA  1 
ATOM   10707 C  C   . ALA C 3  213  ? -65.825 -17.252  75.119  1.00 96.56  ?  213  ALA C C   1 
ATOM   10708 O  O   . ALA C 3  213  ? -64.629 -17.006  74.921  1.00 97.34  ?  213  ALA C O   1 
ATOM   10709 C  CB  . ALA C 3  213  ? -67.212 -18.188  73.248  1.00 79.40  ?  213  ALA C CB  1 
ATOM   10710 N  N   . ALA C 3  214  ? -66.608 -16.444  75.837  1.00 127.27 ?  214  ALA C N   1 
ATOM   10711 C  CA  . ALA C 3  214  ? -66.063 -15.294  76.544  1.00 122.90 ?  214  ALA C CA  1 
ATOM   10712 C  C   . ALA C 3  214  ? -65.268 -15.691  77.778  1.00 123.86 ?  214  ALA C C   1 
ATOM   10713 O  O   . ALA C 3  214  ? -64.584 -14.836  78.351  1.00 117.60 ?  214  ALA C O   1 
ATOM   10714 C  CB  . ALA C 3  214  ? -67.188 -14.339  76.946  1.00 118.18 ?  214  ALA C CB  1 
ATOM   10715 N  N   . LEU C 3  215  ? -65.348 -16.957  78.196  1.00 120.92 ?  215  LEU C N   1 
ATOM   10716 C  CA  . LEU C 3  215  ? -64.655 -17.454  79.383  1.00 120.56 ?  215  LEU C CA  1 
ATOM   10717 C  C   . LEU C 3  215  ? -65.048 -16.675  80.635  1.00 122.91 ?  215  LEU C C   1 
ATOM   10718 O  O   . LEU C 3  215  ? -64.275 -16.589  81.589  1.00 123.84 ?  215  LEU C O   1 
ATOM   10719 C  CB  . LEU C 3  215  ? -63.134 -17.426  79.193  1.00 120.78 ?  215  LEU C CB  1 
ATOM   10720 C  CG  . LEU C 3  215  ? -62.572 -18.116  77.948  1.00 119.45 ?  215  LEU C CG  1 
ATOM   10721 C  CD1 . LEU C 3  215  ? -61.098 -17.791  77.773  1.00 112.53 ?  215  LEU C CD1 1 
ATOM   10722 C  CD2 . LEU C 3  215  ? -62.775 -19.618  78.037  1.00 115.78 ?  215  LEU C CD2 1 
ATOM   10723 N  N   . GLY C 3  216  ? -66.255 -16.114  80.652  1.00 143.43 ?  216  GLY C N   1 
ATOM   10724 C  CA  . GLY C 3  216  ? -66.647 -15.231  81.732  1.00 144.72 ?  216  GLY C CA  1 
ATOM   10725 C  C   . GLY C 3  216  ? -65.711 -14.045  81.823  1.00 140.15 ?  216  GLY C C   1 
ATOM   10726 O  O   . GLY C 3  216  ? -64.959 -13.909  82.793  1.00 142.13 ?  216  GLY C O   1 
ATOM   10727 N  N   . TRP C 3  217  ? -65.748 -13.185  80.802  1.00 119.12 ?  217  TRP C N   1 
ATOM   10728 C  CA  . TRP C 3  217  ? -64.759 -12.117  80.681  1.00 113.51 ?  217  TRP C CA  1 
ATOM   10729 C  C   . TRP C 3  217  ? -64.808 -11.175  81.877  1.00 118.88 ?  217  TRP C C   1 
ATOM   10730 O  O   . TRP C 3  217  ? -63.784 -10.925  82.524  1.00 123.69 ?  217  TRP C O   1 
ATOM   10731 C  CB  . TRP C 3  217  ? -64.977 -11.352  79.375  1.00 109.01 ?  217  TRP C CB  1 
ATOM   10732 C  CG  . TRP C 3  217  ? -64.174 -10.088  79.255  1.00 101.32 ?  217  TRP C CG  1 
ATOM   10733 C  CD1 . TRP C 3  217  ? -64.653 -8.840   78.986  1.00 105.02 ?  217  TRP C CD1 1 
ATOM   10734 C  CD2 . TRP C 3  217  ? -62.753 -9.950   79.393  1.00 97.09  ?  217  TRP C CD2 1 
ATOM   10735 N  NE1 . TRP C 3  217  ? -63.622 -7.933   78.949  1.00 102.76 ?  217  TRP C NE1 1 
ATOM   10736 C  CE2 . TRP C 3  217  ? -62.445 -8.589   79.197  1.00 96.69  ?  217  TRP C CE2 1 
ATOM   10737 C  CE3 . TRP C 3  217  ? -61.712 -10.843  79.664  1.00 97.78  ?  217  TRP C CE3 1 
ATOM   10738 C  CZ2 . TRP C 3  217  ? -61.142 -8.100   79.264  1.00 98.06  ?  217  TRP C CZ2 1 
ATOM   10739 C  CZ3 . TRP C 3  217  ? -60.419 -10.356  79.731  1.00 98.74  ?  217  TRP C CZ3 1 
ATOM   10740 C  CH2 . TRP C 3  217  ? -60.146 -8.997   79.532  1.00 100.79 ?  217  TRP C CH2 1 
ATOM   10741 N  N   . ARG C 3  218  ? -65.992 -10.649  82.189  1.00 133.69 ?  218  ARG C N   1 
ATOM   10742 C  CA  . ARG C 3  218  ? -66.179 -9.706   83.291  1.00 131.53 ?  218  ARG C CA  1 
ATOM   10743 C  C   . ARG C 3  218  ? -65.220 -8.521   83.143  1.00 127.39 ?  218  ARG C C   1 
ATOM   10744 O  O   . ARG C 3  218  ? -64.268 -8.341   83.905  1.00 128.17 ?  218  ARG C O   1 
ATOM   10745 C  CB  . ARG C 3  218  ? -66.006 -10.419  84.638  1.00 129.07 ?  218  ARG C CB  1 
ATOM   10746 C  CG  . ARG C 3  218  ? -66.359 -9.585   85.860  1.00 130.02 ?  218  ARG C CG  1 
ATOM   10747 C  CD  . ARG C 3  218  ? -65.930 -10.285  87.145  1.00 132.84 ?  218  ARG C CD  1 
ATOM   10748 N  NE  . ARG C 3  218  ? -64.563 -9.952   87.528  1.00 130.25 ?  218  ARG C NE  1 
ATOM   10749 C  CZ  . ARG C 3  218  ? -63.570 -10.829  87.603  1.00 125.87 ?  218  ARG C CZ  1 
ATOM   10750 N  NH1 . ARG C 3  218  ? -63.756 -12.108  87.321  1.00 125.67 ?  218  ARG C NH1 1 
ATOM   10751 N  NH2 . ARG C 3  218  ? -62.362 -10.412  87.970  1.00 129.44 ?  218  ARG C NH2 1 
ATOM   10752 N  N   . GLY C 3  219  ? -65.496 -7.729   82.108  1.00 112.17 ?  219  GLY C N   1 
ATOM   10753 C  CA  . GLY C 3  219  ? -64.644 -6.617   81.728  1.00 113.65 ?  219  GLY C CA  1 
ATOM   10754 C  C   . GLY C 3  219  ? -64.331 -5.664   82.859  1.00 116.96 ?  219  GLY C C   1 
ATOM   10755 O  O   . GLY C 3  219  ? -65.164 -4.830   83.222  1.00 125.22 ?  219  GLY C O   1 
ATOM   10756 N  N   . SER C 3  220  ? -63.128 -5.775   83.420  1.00 95.41  ?  220  SER C N   1 
ATOM   10757 C  CA  . SER C 3  220  ? -62.738 -4.997   84.585  1.00 96.29  ?  220  SER C CA  1 
ATOM   10758 C  C   . SER C 3  220  ? -61.273 -4.606   84.477  1.00 92.97  ?  220  SER C C   1 
ATOM   10759 O  O   . SER C 3  220  ? -60.527 -5.118   83.638  1.00 95.95  ?  220  SER C O   1 
ATOM   10760 C  CB  . SER C 3  220  ? -62.972 -5.778   85.883  1.00 102.71 ?  220  SER C CB  1 
ATOM   10761 O  OG  . SER C 3  220  ? -62.009 -6.807   86.041  1.00 97.23  ?  220  SER C OG  1 
ATOM   10762 N  N   . ALA C 3  221  ? -60.863 -3.687   85.349  1.00 96.01  ?  221  ALA C N   1 
ATOM   10763 C  CA  . ALA C 3  221  ? -59.453 -3.368   85.484  1.00 98.34  ?  221  ALA C CA  1 
ATOM   10764 C  C   . ALA C 3  221  ? -58.702 -4.573   86.046  1.00 104.26 ?  221  ALA C C   1 
ATOM   10765 O  O   . ALA C 3  221  ? -59.297 -5.568   86.471  1.00 106.46 ?  221  ALA C O   1 
ATOM   10766 C  CB  . ALA C 3  221  ? -59.261 -2.143   86.376  1.00 112.74 ?  221  ALA C CB  1 
ATOM   10767 N  N   . ARG C 3  222  ? -57.369 -4.479   86.021  1.00 148.98 ?  222  ARG C N   1 
ATOM   10768 C  CA  . ARG C 3  222  ? -56.471 -5.590   86.333  1.00 152.27 ?  222  ARG C CA  1 
ATOM   10769 C  C   . ARG C 3  222  ? -56.613 -6.704   85.298  1.00 148.81 ?  222  ARG C C   1 
ATOM   10770 O  O   . ARG C 3  222  ? -55.843 -7.670   85.305  1.00 157.94 ?  222  ARG C O   1 
ATOM   10771 C  CB  . ARG C 3  222  ? -56.720 -6.131   87.747  1.00 154.56 ?  222  ARG C CB  1 
ATOM   10772 C  CG  . ARG C 3  222  ? -56.500 -5.108   88.850  1.00 162.49 ?  222  ARG C CG  1 
ATOM   10773 C  CD  . ARG C 3  222  ? -56.182 -5.771   90.181  1.00 155.95 ?  222  ARG C CD  1 
ATOM   10774 N  NE  . ARG C 3  222  ? -57.067 -6.893   90.465  1.00 155.10 ?  222  ARG C NE  1 
ATOM   10775 C  CZ  . ARG C 3  222  ? -58.058 -6.859   91.345  1.00 159.00 ?  222  ARG C CZ  1 
ATOM   10776 N  NH1 . ARG C 3  222  ? -58.322 -5.768   92.046  1.00 157.03 ?  222  ARG C NH1 1 
ATOM   10777 N  NH2 . ARG C 3  222  ? -58.804 -7.945   91.526  1.00 155.20 ?  222  ARG C NH2 1 
ATOM   10778 N  N   . HIS C 3  223  ? -57.593 -6.573   84.408  1.00 117.48 ?  223  HIS C N   1 
ATOM   10779 C  CA  . HIS C 3  223  ? -57.792 -7.461   83.270  1.00 119.68 ?  223  HIS C CA  1 
ATOM   10780 C  C   . HIS C 3  223  ? -57.578 -6.761   81.939  1.00 110.90 ?  223  HIS C C   1 
ATOM   10781 O  O   . HIS C 3  223  ? -57.019 -7.357   81.017  1.00 107.29 ?  223  HIS C O   1 
ATOM   10782 C  CB  . HIS C 3  223  ? -59.205 -8.057   83.301  1.00 115.27 ?  223  HIS C CB  1 
ATOM   10783 C  CG  . HIS C 3  223  ? -59.381 -9.148   84.311  1.00 109.93 ?  223  HIS C CG  1 
ATOM   10784 N  ND1 . HIS C 3  223  ? -60.178 -10.249  84.085  1.00 102.95 ?  223  HIS C ND1 1 
ATOM   10785 C  CD2 . HIS C 3  223  ? -58.865 -9.306   85.553  1.00 111.54 ?  223  HIS C CD2 1 
ATOM   10786 C  CE1 . HIS C 3  223  ? -60.145 -11.039  85.143  1.00 102.14 ?  223  HIS C CE1 1 
ATOM   10787 N  NE2 . HIS C 3  223  ? -59.355 -10.490  86.048  1.00 108.89 ?  223  HIS C NE2 1 
ATOM   10788 N  N   . TRP C 3  224  ? -58.015 -5.504   81.821  1.00 108.34 ?  224  TRP C N   1 
ATOM   10789 C  CA  . TRP C 3  224  ? -57.754 -4.735   80.610  1.00 103.07 ?  224  TRP C CA  1 
ATOM   10790 C  C   . TRP C 3  224  ? -56.273 -4.408   80.467  1.00 103.95 ?  224  TRP C C   1 
ATOM   10791 O  O   . TRP C 3  224  ? -55.766 -4.317   79.344  1.00 107.38 ?  224  TRP C O   1 
ATOM   10792 C  CB  . TRP C 3  224  ? -58.577 -3.446   80.613  1.00 106.51 ?  224  TRP C CB  1 
ATOM   10793 C  CG  . TRP C 3  224  ? -60.042 -3.643   80.345  1.00 105.84 ?  224  TRP C CG  1 
ATOM   10794 C  CD1 . TRP C 3  224  ? -61.073 -3.354   81.191  1.00 113.12 ?  224  TRP C CD1 1 
ATOM   10795 C  CD2 . TRP C 3  224  ? -60.640 -4.155   79.147  1.00 105.86 ?  224  TRP C CD2 1 
ATOM   10796 N  NE1 . TRP C 3  224  ? -62.273 -3.662   80.599  1.00 111.12 ?  224  TRP C NE1 1 
ATOM   10797 C  CE2 . TRP C 3  224  ? -62.035 -4.155   79.344  1.00 105.86 ?  224  TRP C CE2 1 
ATOM   10798 C  CE3 . TRP C 3  224  ? -60.131 -4.617   77.929  1.00 107.91 ?  224  TRP C CE3 1 
ATOM   10799 C  CZ2 . TRP C 3  224  ? -62.927 -4.598   78.370  1.00 108.81 ?  224  TRP C CZ2 1 
ATOM   10800 C  CZ3 . TRP C 3  224  ? -61.019 -5.057   76.963  1.00 108.76 ?  224  TRP C CZ3 1 
ATOM   10801 C  CH2 . TRP C 3  224  ? -62.401 -5.044   77.190  1.00 111.47 ?  224  TRP C CH2 1 
ATOM   10802 N  N   . HIS C 3  225  ? -55.570 -4.226   81.588  1.00 98.11  ?  225  HIS C N   1 
ATOM   10803 C  CA  . HIS C 3  225  ? -54.141 -3.935   81.535  1.00 97.65  ?  225  HIS C CA  1 
ATOM   10804 C  C   . HIS C 3  225  ? -53.369 -5.087   80.904  1.00 95.89  ?  225  HIS C C   1 
ATOM   10805 O  O   . HIS C 3  225  ? -52.577 -4.887   79.976  1.00 98.48  ?  225  HIS C O   1 
ATOM   10806 C  CB  . HIS C 3  225  ? -53.613 -3.640   82.939  1.00 99.63  ?  225  HIS C CB  1 
ATOM   10807 C  CG  . HIS C 3  225  ? -52.347 -2.842   82.953  1.00 98.96  ?  225  HIS C CG  1 
ATOM   10808 N  ND1 . HIS C 3  225  ? -51.983 -2.004   81.921  1.00 105.00 ?  225  HIS C ND1 1 
ATOM   10809 C  CD2 . HIS C 3  225  ? -51.355 -2.760   83.872  1.00 99.11  ?  225  HIS C CD2 1 
ATOM   10810 C  CE1 . HIS C 3  225  ? -50.824 -1.438   82.205  1.00 112.22 ?  225  HIS C CE1 1 
ATOM   10811 N  NE2 . HIS C 3  225  ? -50.421 -1.879   83.383  1.00 108.11 ?  225  HIS C NE2 1 
ATOM   10812 N  N   . ARG C 3  226  ? -53.587 -6.306   81.401  1.00 100.25 ?  226  ARG C N   1 
ATOM   10813 C  CA  . ARG C 3  226  ? -52.925 -7.470   80.824  1.00 98.61  ?  226  ARG C CA  1 
ATOM   10814 C  C   . ARG C 3  226  ? -53.426 -7.753   79.414  1.00 96.65  ?  226  ARG C C   1 
ATOM   10815 O  O   . ARG C 3  226  ? -52.683 -8.297   78.589  1.00 95.27  ?  226  ARG C O   1 
ATOM   10816 C  CB  . ARG C 3  226  ? -53.138 -8.687   81.723  1.00 91.53  ?  226  ARG C CB  1 
ATOM   10817 C  CG  . ARG C 3  226  ? -52.529 -8.533   83.104  1.00 95.46  ?  226  ARG C CG  1 
ATOM   10818 C  CD  . ARG C 3  226  ? -52.334 -9.873   83.792  1.00 98.36  ?  226  ARG C CD  1 
ATOM   10819 N  NE  . ARG C 3  226  ? -51.835 -9.707   85.152  1.00 98.47  ?  226  ARG C NE  1 
ATOM   10820 C  CZ  . ARG C 3  226  ? -52.605 -9.506   86.213  1.00 103.12 ?  226  ARG C CZ  1 
ATOM   10821 N  NH1 . ARG C 3  226  ? -53.922 -9.450   86.110  1.00 106.55 ?  226  ARG C NH1 1 
ATOM   10822 N  NH2 . ARG C 3  226  ? -52.038 -9.356   87.406  1.00 112.39 ?  226  ARG C NH2 1 
ATOM   10823 N  N   . TYR C 3  227  ? -54.676 -7.392   79.122  1.00 111.64 ?  227  TYR C N   1 
ATOM   10824 C  CA  . TYR C 3  227  ? -55.215 -7.570   77.778  1.00 105.38 ?  227  TYR C CA  1 
ATOM   10825 C  C   . TYR C 3  227  ? -54.523 -6.647   76.782  1.00 103.85 ?  227  TYR C C   1 
ATOM   10826 O  O   . TYR C 3  227  ? -54.160 -7.069   75.677  1.00 103.70 ?  227  TYR C O   1 
ATOM   10827 C  CB  . TYR C 3  227  ? -56.723 -7.319   77.791  1.00 106.23 ?  227  TYR C CB  1 
ATOM   10828 C  CG  . TYR C 3  227  ? -57.438 -7.712   76.520  1.00 103.13 ?  227  TYR C CG  1 
ATOM   10829 C  CD1 . TYR C 3  227  ? -57.940 -8.996   76.349  1.00 98.80  ?  227  TYR C CD1 1 
ATOM   10830 C  CD2 . TYR C 3  227  ? -57.626 -6.793   75.496  1.00 109.06 ?  227  TYR C CD2 1 
ATOM   10831 C  CE1 . TYR C 3  227  ? -58.600 -9.355   75.190  1.00 100.64 ?  227  TYR C CE1 1 
ATOM   10832 C  CE2 . TYR C 3  227  ? -58.283 -7.143   74.335  1.00 112.24 ?  227  TYR C CE2 1 
ATOM   10833 C  CZ  . TYR C 3  227  ? -58.768 -8.423   74.188  1.00 110.38 ?  227  TYR C CZ  1 
ATOM   10834 O  OH  . TYR C 3  227  ? -59.423 -8.771   73.031  1.00 121.27 ?  227  TYR C OH  1 
ATOM   10835 N  N   . GLU C 3  228  ? -54.334 -5.380   77.157  1.00 110.30 ?  228  GLU C N   1 
ATOM   10836 C  CA  . GLU C 3  228  ? -53.691 -4.430   76.254  1.00 112.51 ?  228  GLU C CA  1 
ATOM   10837 C  C   . GLU C 3  228  ? -52.223 -4.774   76.036  1.00 107.58 ?  228  GLU C C   1 
ATOM   10838 O  O   . GLU C 3  228  ? -51.713 -4.654   74.916  1.00 114.27 ?  228  GLU C O   1 
ATOM   10839 C  CB  . GLU C 3  228  ? -53.833 -3.008   76.796  1.00 115.39 ?  228  GLU C CB  1 
ATOM   10840 C  CG  . GLU C 3  228  ? -55.253 -2.465   76.758  1.00 125.79 ?  228  GLU C CG  1 
ATOM   10841 C  CD  . GLU C 3  228  ? -55.551 -1.718   75.471  1.00 144.07 ?  228  GLU C CD  1 
ATOM   10842 O  OE1 . GLU C 3  228  ? -55.193 -0.526   75.379  1.00 149.68 ?  228  GLU C OE1 1 
ATOM   10843 O  OE2 . GLU C 3  228  ? -56.139 -2.324   74.548  1.00 135.84 -1 228  GLU C OE2 1 
ATOM   10844 N  N   . MET C 3  229  ? -51.524 -5.199   77.091  1.00 102.36 ?  229  MET C N   1 
ATOM   10845 C  CA  . MET C 3  229  ? -50.106 -5.515   76.948  1.00 103.59 ?  229  MET C CA  1 
ATOM   10846 C  C   . MET C 3  229  ? -49.901 -6.786   76.133  1.00 105.05 ?  229  MET C C   1 
ATOM   10847 O  O   . MET C 3  229  ? -48.971 -6.865   75.321  1.00 104.23 ?  229  MET C O   1 
ATOM   10848 C  CB  . MET C 3  229  ? -49.451 -5.645   78.322  1.00 103.95 ?  229  MET C CB  1 
ATOM   10849 C  CG  . MET C 3  229  ? -47.951 -5.868   78.253  1.00 100.51 ?  229  MET C CG  1 
ATOM   10850 S  SD  . MET C 3  229  ? -47.110 -4.486   77.456  1.00 110.47 ?  229  MET C SD  1 
ATOM   10851 C  CE  . MET C 3  229  ? -45.409 -4.796   77.916  1.00 104.06 ?  229  MET C CE  1 
ATOM   10852 N  N   . ALA C 3  230  ? -50.755 -7.792   76.335  1.00 92.87  ?  230  ALA C N   1 
ATOM   10853 C  CA  . ALA C 3  230  ? -50.655 -9.007   75.535  1.00 89.88  ?  230  ALA C CA  1 
ATOM   10854 C  C   . ALA C 3  230  ? -50.995 -8.733   74.075  1.00 83.28  ?  230  ALA C C   1 
ATOM   10855 O  O   . ALA C 3  230  ? -50.381 -9.310   73.170  1.00 79.66  ?  230  ALA C O   1 
ATOM   10856 C  CB  . ALA C 3  230  ? -51.566 -10.092  76.108  1.00 78.82  ?  230  ALA C CB  1 
ATOM   10857 N  N   . SER C 3  231  ? -51.965 -7.851   73.827  1.00 83.89  ?  231  SER C N   1 
ATOM   10858 C  CA  . SER C 3  231  ? -52.315 -7.505   72.454  1.00 79.31  ?  231  SER C CA  1 
ATOM   10859 C  C   . SER C 3  231  ? -51.198 -6.715   71.782  1.00 83.15  ?  231  SER C C   1 
ATOM   10860 O  O   . SER C 3  231  ? -50.947 -6.885   70.583  1.00 92.93  ?  231  SER C O   1 
ATOM   10861 C  CB  . SER C 3  231  ? -53.624 -6.717   72.428  1.00 81.53  ?  231  SER C CB  1 
ATOM   10862 O  OG  . SER C 3  231  ? -53.395 -5.341   72.679  1.00 96.36  ?  231  SER C OG  1 
ATOM   10863 N  N   . ILE C 3  232  ? -50.520 -5.846   72.535  1.00 77.08  ?  232  ILE C N   1 
ATOM   10864 C  CA  . ILE C 3  232  ? -49.388 -5.105   71.981  1.00 78.39  ?  232  ILE C CA  1 
ATOM   10865 C  C   . ILE C 3  232  ? -48.253 -6.060   71.635  1.00 81.41  ?  232  ILE C C   1 
ATOM   10866 O  O   . ILE C 3  232  ? -47.642 -5.969   70.563  1.00 82.23  ?  232  ILE C O   1 
ATOM   10867 C  CB  . ILE C 3  232  ? -48.927 -4.012   72.962  1.00 74.34  ?  232  ILE C CB  1 
ATOM   10868 C  CG1 . ILE C 3  232  ? -49.857 -2.799   72.889  1.00 82.50  ?  232  ILE C CG1 1 
ATOM   10869 C  CG2 . ILE C 3  232  ? -47.492 -3.599   72.671  1.00 64.10  ?  232  ILE C CG2 1 
ATOM   10870 C  CD1 . ILE C 3  232  ? -49.835 -2.095   71.549  1.00 91.82  ?  232  ILE C CD1 1 
ATOM   10871 N  N   . LEU C 3  233  ? -47.956 -6.995   72.541  1.00 86.57  ?  233  LEU C N   1 
ATOM   10872 C  CA  . LEU C 3  233  ? -46.906 -7.973   72.277  1.00 82.03  ?  233  LEU C CA  1 
ATOM   10873 C  C   . LEU C 3  233  ? -47.278 -8.877   71.109  1.00 80.09  ?  233  LEU C C   1 
ATOM   10874 O  O   . LEU C 3  233  ? -46.422 -9.224   70.285  1.00 76.59  ?  233  LEU C O   1 
ATOM   10875 C  CB  . LEU C 3  233  ? -46.636 -8.803   73.532  1.00 81.50  ?  233  LEU C CB  1 
ATOM   10876 C  CG  . LEU C 3  233  ? -45.918 -8.090   74.679  1.00 88.24  ?  233  LEU C CG  1 
ATOM   10877 C  CD1 . LEU C 3  233  ? -45.912 -8.957   75.930  1.00 95.90  ?  233  LEU C CD1 1 
ATOM   10878 C  CD2 . LEU C 3  233  ? -44.502 -7.712   74.275  1.00 77.24  ?  233  LEU C CD2 1 
ATOM   10879 N  N   . LEU C 3  234  ? -48.552 -9.267   71.019  1.00 78.37  ?  234  LEU C N   1 
ATOM   10880 C  CA  . LEU C 3  234  ? -48.981 -10.151  69.942  1.00 76.89  ?  234  LEU C CA  1 
ATOM   10881 C  C   . LEU C 3  234  ? -48.858 -9.468   68.587  1.00 77.05  ?  234  LEU C C   1 
ATOM   10882 O  O   . LEU C 3  234  ? -48.421 -10.089  67.612  1.00 79.69  ?  234  LEU C O   1 
ATOM   10883 C  CB  . LEU C 3  234  ? -50.416 -10.614  70.181  1.00 76.30  ?  234  LEU C CB  1 
ATOM   10884 C  CG  . LEU C 3  234  ? -50.583 -11.912  70.972  1.00 81.53  ?  234  LEU C CG  1 
ATOM   10885 C  CD1 . LEU C 3  234  ? -51.981 -12.005  71.562  1.00 83.41  ?  234  LEU C CD1 1 
ATOM   10886 C  CD2 . LEU C 3  234  ? -50.283 -13.117  70.097  1.00 85.09  ?  234  LEU C CD2 1 
ATOM   10887 N  N   . ALA C 3  235  ? -49.233 -8.191   68.506  1.00 73.61  ?  235  ALA C N   1 
ATOM   10888 C  CA  . ALA C 3  235  ? -49.070 -7.457   67.256  1.00 69.96  ?  235  ALA C CA  1 
ATOM   10889 C  C   . ALA C 3  235  ? -47.598 -7.245   66.924  1.00 68.25  ?  235  ALA C C   1 
ATOM   10890 O  O   . ALA C 3  235  ? -47.209 -7.303   65.753  1.00 73.23  ?  235  ALA C O   1 
ATOM   10891 C  CB  . ALA C 3  235  ? -49.795 -6.116   67.330  1.00 77.23  ?  235  ALA C CB  1 
ATOM   10892 N  N   . GLY C 3  236  ? -46.769 -6.969   67.933  1.00 58.57  ?  236  GLY C N   1 
ATOM   10893 C  CA  . GLY C 3  236  ? -45.350 -6.784   67.677  1.00 60.83  ?  236  GLY C CA  1 
ATOM   10894 C  C   . GLY C 3  236  ? -44.672 -8.066   67.248  1.00 64.96  ?  236  GLY C C   1 
ATOM   10895 O  O   . GLY C 3  236  ? -43.626 -8.038   66.592  1.00 66.25  ?  236  GLY C O   1 
ATOM   10896 N  N   . LEU C 3  237  ? -45.258 -9.204   67.607  1.00 94.50  ?  237  LEU C N   1 
ATOM   10897 C  CA  . LEU C 3  237  ? -44.713 -10.485  67.197  1.00 91.56  ?  237  LEU C CA  1 
ATOM   10898 C  C   . LEU C 3  237  ? -45.255 -10.926  65.845  1.00 98.59  ?  237  LEU C C   1 
ATOM   10899 O  O   . LEU C 3  237  ? -44.525 -11.527  65.050  1.00 105.22 ?  237  LEU C O   1 
ATOM   10900 C  CB  . LEU C 3  237  ? -45.015 -11.551  68.250  1.00 87.41  ?  237  LEU C CB  1 
ATOM   10901 C  CG  . LEU C 3  237  ? -44.215 -11.534  69.549  1.00 95.59  ?  237  LEU C CG  1 
ATOM   10902 C  CD1 . LEU C 3  237  ? -45.001 -12.218  70.659  1.00 101.50 ?  237  LEU C CD1 1 
ATOM   10903 C  CD2 . LEU C 3  237  ? -42.883 -12.220  69.334  1.00 104.74 ?  237  LEU C CD2 1 
ATOM   10904 N  N   . SER C 3  238  ? -46.523 -10.629  65.561  1.00 57.32  ?  238  SER C N   1 
ATOM   10905 C  CA  . SER C 3  238  ? -47.125 -11.073  64.311  1.00 49.50  ?  238  SER C CA  1 
ATOM   10906 C  C   . SER C 3  238  ? -46.682 -10.246  63.113  1.00 42.64  ?  238  SER C C   1 
ATOM   10907 O  O   . SER C 3  238  ? -46.842 -10.698  61.974  1.00 54.56  ?  238  SER C O   1 
ATOM   10908 C  CB  . SER C 3  238  ? -48.652 -11.047  64.418  1.00 44.59  ?  238  SER C CB  1 
ATOM   10909 O  OG  . SER C 3  238  ? -49.108 -9.795   64.892  1.00 59.88  ?  238  SER C OG  1 
ATOM   10910 N  N   . THR C 3  239  ? -46.133 -9.048   63.338  1.00 59.60  ?  239  THR C N   1 
ATOM   10911 C  CA  . THR C 3  239  ? -45.651 -8.251   62.211  1.00 66.74  ?  239  THR C CA  1 
ATOM   10912 C  C   . THR C 3  239  ? -44.457 -8.904   61.525  1.00 69.03  ?  239  THR C C   1 
ATOM   10913 O  O   . THR C 3  239  ? -44.509 -9.093   60.297  1.00 72.42  ?  239  THR C O   1 
ATOM   10914 C  CB  . THR C 3  239  ? -45.344 -6.821   62.670  1.00 67.28  ?  239  THR C CB  1 
ATOM   10915 O  OG1 . THR C 3  239  ? -46.564 -6.150   63.010  1.00 73.91  ?  239  THR C OG1 1 
ATOM   10916 C  CG2 . THR C 3  239  ? -44.633 -6.050   61.567  1.00 67.76  ?  239  THR C CG2 1 
ATOM   10917 N  N   . PRO C 3  240  ? -43.374 -9.282   62.219  1.00 81.10  ?  240  PRO C N   1 
ATOM   10918 C  CA  . PRO C 3  240  ? -42.316 -10.037  61.531  1.00 81.75  ?  240  PRO C CA  1 
ATOM   10919 C  C   . PRO C 3  240  ? -42.750 -11.432  61.127  1.00 86.68  ?  240  PRO C C   1 
ATOM   10920 O  O   . PRO C 3  240  ? -42.125 -12.023  60.238  1.00 93.50  ?  240  PRO C O   1 
ATOM   10921 C  CB  . PRO C 3  240  ? -41.179 -10.085  62.563  1.00 86.17  ?  240  PRO C CB  1 
ATOM   10922 C  CG  . PRO C 3  240  ? -41.524 -9.044   63.580  1.00 87.09  ?  240  PRO C CG  1 
ATOM   10923 C  CD  . PRO C 3  240  ? -43.013 -9.045   63.627  1.00 88.62  ?  240  PRO C CD  1 
ATOM   10924 N  N   . LEU C 3  241  ? -43.796 -11.975  61.752  1.00 54.15  ?  241  LEU C N   1 
ATOM   10925 C  CA  . LEU C 3  241  ? -44.287 -13.297  61.377  1.00 54.08  ?  241  LEU C CA  1 
ATOM   10926 C  C   . LEU C 3  241  ? -44.823 -13.292  59.951  1.00 62.13  ?  241  LEU C C   1 
ATOM   10927 O  O   . LEU C 3  241  ? -44.377 -14.073  59.103  1.00 67.39  ?  241  LEU C O   1 
ATOM   10928 C  CB  . LEU C 3  241  ? -45.366 -13.752  62.362  1.00 48.58  ?  241  LEU C CB  1 
ATOM   10929 C  CG  . LEU C 3  241  ? -46.246 -14.924  61.918  1.00 48.27  ?  241  LEU C CG  1 
ATOM   10930 C  CD1 . LEU C 3  241  ? -45.423 -16.192  61.776  1.00 53.65  ?  241  LEU C CD1 1 
ATOM   10931 C  CD2 . LEU C 3  241  ? -47.397 -15.135  62.887  1.00 48.15  ?  241  LEU C CD2 1 
ATOM   10932 N  N   . VAL C 3  242  ? -45.781 -12.405  59.666  1.00 60.72  ?  242  VAL C N   1 
ATOM   10933 C  CA  . VAL C 3  242  ? -46.367 -12.349  58.331  1.00 61.06  ?  242  VAL C CA  1 
ATOM   10934 C  C   . VAL C 3  242  ? -45.337 -11.889  57.304  1.00 58.00  ?  242  VAL C C   1 
ATOM   10935 O  O   . VAL C 3  242  ? -45.365 -12.329  56.148  1.00 56.20  ?  242  VAL C O   1 
ATOM   10936 C  CB  . VAL C 3  242  ? -47.618 -11.448  58.335  1.00 63.00  ?  242  VAL C CB  1 
ATOM   10937 C  CG1 . VAL C 3  242  ? -47.265 -10.031  58.764  1.00 53.56  ?  242  VAL C CG1 1 
ATOM   10938 C  CG2 . VAL C 3  242  ? -48.292 -11.453  56.970  1.00 68.34  ?  242  VAL C CG2 1 
ATOM   10939 N  N   . VAL C 3  243  ? -44.408 -11.016  57.702  1.00 64.90  ?  243  VAL C N   1 
ATOM   10940 C  CA  . VAL C 3  243  ? -43.340 -10.608  56.794  1.00 65.26  ?  243  VAL C CA  1 
ATOM   10941 C  C   . VAL C 3  243  ? -42.459 -11.800  56.443  1.00 71.51  ?  243  VAL C C   1 
ATOM   10942 O  O   . VAL C 3  243  ? -42.115 -12.014  55.275  1.00 67.82  ?  243  VAL C O   1 
ATOM   10943 C  CB  . VAL C 3  243  ? -42.521 -9.459   57.411  1.00 59.83  ?  243  VAL C CB  1 
ATOM   10944 C  CG1 . VAL C 3  243  ? -41.244 -9.232   56.618  1.00 57.30  ?  243  VAL C CG1 1 
ATOM   10945 C  CG2 . VAL C 3  243  ? -43.351 -8.188   57.451  1.00 61.55  ?  243  VAL C CG2 1 
ATOM   10946 N  N   . SER C 3  244  ? -42.093 -12.603  57.445  1.00 100.08 ?  244  SER C N   1 
ATOM   10947 C  CA  . SER C 3  244  ? -41.252 -13.767  57.185  1.00 98.35  ?  244  SER C CA  1 
ATOM   10948 C  C   . SER C 3  244  ? -42.003 -14.847  56.417  1.00 94.73  ?  244  SER C C   1 
ATOM   10949 O  O   . SER C 3  244  ? -41.390 -15.586  55.639  1.00 95.40  ?  244  SER C O   1 
ATOM   10950 C  CB  . SER C 3  244  ? -40.711 -14.331  58.499  1.00 92.16  ?  244  SER C CB  1 
ATOM   10951 O  OG  . SER C 3  244  ? -41.750 -14.899  59.277  1.00 92.65  ?  244  SER C OG  1 
ATOM   10952 N  N   . VAL C 3  245  ? -43.317 -14.959  56.623  1.00 64.98  ?  245  VAL C N   1 
ATOM   10953 C  CA  . VAL C 3  245  ? -44.106 -15.950  55.893  1.00 65.62  ?  245  VAL C CA  1 
ATOM   10954 C  C   . VAL C 3  245  ? -44.043 -15.674  54.396  1.00 61.17  ?  245  VAL C C   1 
ATOM   10955 O  O   . VAL C 3  245  ? -43.646 -16.533  53.603  1.00 61.12  ?  245  VAL C O   1 
ATOM   10956 C  CB  . VAL C 3  245  ? -45.560 -15.970  56.398  1.00 62.01  ?  245  VAL C CB  1 
ATOM   10957 C  CG1 . VAL C 3  245  ? -46.447 -16.724  55.422  1.00 61.09  ?  245  VAL C CG1 1 
ATOM   10958 C  CG2 . VAL C 3  245  ? -45.632 -16.620  57.765  1.00 61.87  ?  245  VAL C CG2 1 
ATOM   10959 N  N   . HIS C 3  246  ? -44.425 -14.461  53.990  1.00 94.50  ?  246  HIS C N   1 
ATOM   10960 C  CA  . HIS C 3  246  ? -44.410 -14.125  52.570  1.00 98.51  ?  246  HIS C CA  1 
ATOM   10961 C  C   . HIS C 3  246  ? -42.990 -14.024  52.029  1.00 96.64  ?  246  HIS C C   1 
ATOM   10962 O  O   . HIS C 3  246  ? -42.772 -14.214  50.827  1.00 89.15  ?  246  HIS C O   1 
ATOM   10963 C  CB  . HIS C 3  246  ? -45.172 -12.825  52.333  1.00 97.26  ?  246  HIS C CB  1 
ATOM   10964 C  CG  . HIS C 3  246  ? -46.641 -12.938  52.593  1.00 102.77 ?  246  HIS C CG  1 
ATOM   10965 N  ND1 . HIS C 3  246  ? -47.184 -12.836  53.856  1.00 102.25 ?  246  HIS C ND1 1 
ATOM   10966 C  CD2 . HIS C 3  246  ? -47.679 -13.166  51.755  1.00 105.21 ?  246  HIS C CD2 1 
ATOM   10967 C  CE1 . HIS C 3  246  ? -48.495 -12.982  53.782  1.00 100.85 ?  246  HIS C CE1 1 
ATOM   10968 N  NE2 . HIS C 3  246  ? -48.821 -13.183  52.518  1.00 106.33 ?  246  HIS C NE2 1 
ATOM   10969 N  N   . SER C 3  247  ? -42.015 -13.727  52.891  1.00 84.02  ?  247  SER C N   1 
ATOM   10970 C  CA  . SER C 3  247  ? -40.625 -13.771  52.456  1.00 79.14  ?  247  SER C CA  1 
ATOM   10971 C  C   . SER C 3  247  ? -40.182 -15.199  52.171  1.00 75.21  ?  247  SER C C   1 
ATOM   10972 O  O   . SER C 3  247  ? -39.345 -15.423  51.289  1.00 79.84  ?  247  SER C O   1 
ATOM   10973 C  CB  . SER C 3  247  ? -39.716 -13.132  53.506  1.00 74.85  ?  247  SER C CB  1 
ATOM   10974 O  OG  . SER C 3  247  ? -40.118 -11.802  53.786  1.00 72.04  ?  247  SER C OG  1 
ATOM   10975 N  N   . ILE C 3  248  ? -40.733 -16.172  52.898  1.00 59.18  ?  248  ILE C N   1 
ATOM   10976 C  CA  . ILE C 3  248  ? -40.417 -17.572  52.636  1.00 64.00  ?  248  ILE C CA  1 
ATOM   10977 C  C   . ILE C 3  248  ? -41.146 -18.062  51.389  1.00 70.52  ?  248  ILE C C   1 
ATOM   10978 O  O   . ILE C 3  248  ? -40.581 -18.811  50.583  1.00 73.64  ?  248  ILE C O   1 
ATOM   10979 C  CB  . ILE C 3  248  ? -40.745 -18.426  53.875  1.00 61.44  ?  248  ILE C CB  1 
ATOM   10980 C  CG1 . ILE C 3  248  ? -39.642 -18.273  54.926  1.00 60.80  ?  248  ILE C CG1 1 
ATOM   10981 C  CG2 . ILE C 3  248  ? -40.920 -19.890  53.500  1.00 56.28  ?  248  ILE C CG2 1 
ATOM   10982 C  CD1 . ILE C 3  248  ? -40.034 -18.753  56.304  1.00 58.23  ?  248  ILE C CD1 1 
ATOM   10983 N  N   . ILE C 3  249  ? -42.400 -17.639  51.199  1.00 82.34  ?  249  ILE C N   1 
ATOM   10984 C  CA  . ILE C 3  249  ? -43.104 -17.921  49.952  1.00 78.27  ?  249  ILE C CA  1 
ATOM   10985 C  C   . ILE C 3  249  ? -42.400 -17.268  48.771  1.00 75.99  ?  249  ILE C C   1 
ATOM   10986 O  O   . ILE C 3  249  ? -42.593 -17.684  47.625  1.00 82.75  ?  249  ILE C O   1 
ATOM   10987 C  CB  . ILE C 3  249  ? -44.578 -17.467  50.043  1.00 81.57  ?  249  ILE C CB  1 
ATOM   10988 C  CG1 . ILE C 3  249  ? -45.214 -17.971  51.337  1.00 87.19  ?  249  ILE C CG1 1 
ATOM   10989 C  CG2 . ILE C 3  249  ? -45.380 -17.977  48.853  1.00 83.85  ?  249  ILE C CG2 1 
ATOM   10990 C  CD1 . ILE C 3  249  ? -45.509 -19.450  51.327  1.00 93.72  ?  249  ILE C CD1 1 
ATOM   10991 N  N   . SER C 3  250  ? -41.586 -16.243  49.022  1.00 81.26  ?  250  SER C N   1 
ATOM   10992 C  CA  . SER C 3  250  ? -40.716 -15.720  47.978  1.00 86.57  ?  250  SER C CA  1 
ATOM   10993 C  C   . SER C 3  250  ? -39.425 -16.517  47.875  1.00 90.27  ?  250  SER C C   1 
ATOM   10994 O  O   . SER C 3  250  ? -38.857 -16.635  46.783  1.00 96.16  ?  250  SER C O   1 
ATOM   10995 C  CB  . SER C 3  250  ? -40.391 -14.253  48.246  1.00 86.16  ?  250  SER C CB  1 
ATOM   10996 O  OG  . SER C 3  250  ? -39.258 -14.145  49.089  1.00 82.96  ?  250  SER C OG  1 
ATOM   10997 N  N   . LEU C 3  251  ? -38.952 -17.068  48.996  1.00 77.17  ?  251  LEU C N   1 
ATOM   10998 C  CA  . LEU C 3  251  ? -37.694 -17.805  48.988  1.00 75.07  ?  251  LEU C CA  1 
ATOM   10999 C  C   . LEU C 3  251  ? -37.803 -19.110  48.209  1.00 75.83  ?  251  LEU C C   1 
ATOM   11000 O  O   . LEU C 3  251  ? -36.807 -19.572  47.646  1.00 72.09  ?  251  LEU C O   1 
ATOM   11001 C  CB  . LEU C 3  251  ? -37.236 -18.075  50.422  1.00 68.95  ?  251  LEU C CB  1 
ATOM   11002 C  CG  . LEU C 3  251  ? -36.498 -16.938  51.135  1.00 77.66  ?  251  LEU C CG  1 
ATOM   11003 C  CD1 . LEU C 3  251  ? -35.839 -17.431  52.415  1.00 77.51  ?  251  LEU C CD1 1 
ATOM   11004 C  CD2 . LEU C 3  251  ? -35.473 -16.289  50.218  1.00 73.22  ?  251  LEU C CD2 1 
ATOM   11005 N  N   . ASP C 3  252  ? -38.996 -19.709  48.148  1.00 115.74 ?  252  ASP C N   1 
ATOM   11006 C  CA  . ASP C 3  252  ? -39.141 -20.982  47.448  1.00 117.75 ?  252  ASP C CA  1 
ATOM   11007 C  C   . ASP C 3  252  ? -38.787 -20.860  45.967  1.00 118.86 ?  252  ASP C C   1 
ATOM   11008 O  O   . ASP C 3  252  ? -38.256 -21.808  45.376  1.00 120.01 ?  252  ASP C O   1 
ATOM   11009 C  CB  . ASP C 3  252  ? -40.559 -21.527  47.647  1.00 123.75 ?  252  ASP C CB  1 
ATOM   11010 C  CG  . ASP C 3  252  ? -41.628 -20.634  47.046  1.00 133.36 ?  252  ASP C CG  1 
ATOM   11011 O  OD1 . ASP C 3  252  ? -41.282 -19.647  46.367  1.00 136.39 ?  252  ASP C OD1 1 
ATOM   11012 O  OD2 . ASP C 3  252  ? -42.825 -20.929  47.254  1.00 134.33 -1 252  ASP C OD2 1 
ATOM   11013 N  N   . PHE C 3  253  ? -39.060 -19.706  45.354  1.00 73.71  ?  253  PHE C N   1 
ATOM   11014 C  CA  . PHE C 3  253  ? -38.597 -19.462  43.993  1.00 65.91  ?  253  PHE C CA  1 
ATOM   11015 C  C   . PHE C 3  253  ? -37.183 -18.894  43.965  1.00 69.12  ?  253  PHE C C   1 
ATOM   11016 O  O   . PHE C 3  253  ? -36.397 -19.231  43.072  1.00 68.56  ?  253  PHE C O   1 
ATOM   11017 C  CB  . PHE C 3  253  ? -39.543 -18.506  43.254  1.00 64.24  ?  253  PHE C CB  1 
ATOM   11018 C  CG  . PHE C 3  253  ? -40.998 -18.851  43.393  1.00 66.20  ?  253  PHE C CG  1 
ATOM   11019 C  CD1 . PHE C 3  253  ? -41.491 -20.044  42.893  1.00 65.06  ?  253  PHE C CD1 1 
ATOM   11020 C  CD2 . PHE C 3  253  ? -41.881 -17.961  43.984  1.00 75.58  ?  253  PHE C CD2 1 
ATOM   11021 C  CE1 . PHE C 3  253  ? -42.830 -20.361  43.010  1.00 67.99  ?  253  PHE C CE1 1 
ATOM   11022 C  CE2 . PHE C 3  253  ? -43.223 -18.272  44.104  1.00 79.17  ?  253  PHE C CE2 1 
ATOM   11023 C  CZ  . PHE C 3  253  ? -43.698 -19.473  43.615  1.00 74.82  ?  253  PHE C CZ  1 
ATOM   11024 N  N   . ALA C 3  254  ? -36.839 -18.046  44.936  1.00 54.96  ?  254  ALA C N   1 
ATOM   11025 C  CA  . ALA C 3  254  ? -35.540 -17.383  44.928  1.00 54.56  ?  254  ALA C CA  1 
ATOM   11026 C  C   . ALA C 3  254  ? -34.393 -18.329  45.262  1.00 61.74  ?  254  ALA C C   1 
ATOM   11027 O  O   . ALA C 3  254  ? -33.250 -18.050  44.883  1.00 59.16  ?  254  ALA C O   1 
ATOM   11028 C  CB  . ALA C 3  254  ? -35.547 -16.208  45.905  1.00 64.74  ?  254  ALA C CB  1 
ATOM   11029 N  N   . ILE C 3  255  ? -34.664 -19.433  45.962  1.00 75.83  ?  255  ILE C N   1 
ATOM   11030 C  CA  . ILE C 3  255  ? -33.601 -20.380  46.284  1.00 71.88  ?  255  ILE C CA  1 
ATOM   11031 C  C   . ILE C 3  255  ? -33.159 -21.137  45.037  1.00 74.30  ?  255  ILE C C   1 
ATOM   11032 O  O   . ILE C 3  255  ? -31.980 -21.487  44.897  1.00 72.81  ?  255  ILE C O   1 
ATOM   11033 C  CB  . ILE C 3  255  ? -34.069 -21.334  47.403  1.00 66.93  ?  255  ILE C CB  1 
ATOM   11034 C  CG1 . ILE C 3  255  ? -34.182 -20.584  48.733  1.00 73.91  ?  255  ILE C CG1 1 
ATOM   11035 C  CG2 . ILE C 3  255  ? -33.142 -22.538  47.533  1.00 66.98  ?  255  ILE C CG2 1 
ATOM   11036 C  CD1 . ILE C 3  255  ? -32.945 -19.815  49.125  1.00 75.11  ?  255  ILE C CD1 1 
ATOM   11037 N  N   . SER C 3  256  ? -34.078 -21.373  44.103  1.00 69.10  ?  256  SER C N   1 
ATOM   11038 C  CA  . SER C 3  256  ? -33.781 -22.130  42.898  1.00 60.09  ?  256  SER C CA  1 
ATOM   11039 C  C   . SER C 3  256  ? -32.817 -21.363  41.991  1.00 60.31  ?  256  SER C C   1 
ATOM   11040 O  O   . SER C 3  256  ? -32.471 -20.204  42.233  1.00 57.13  ?  256  SER C O   1 
ATOM   11041 C  CB  . SER C 3  256  ? -35.069 -22.452  42.144  1.00 64.10  ?  256  SER C CB  1 
ATOM   11042 O  OG  . SER C 3  256  ? -35.407 -21.404  41.251  1.00 66.91  ?  256  SER C OG  1 
ATOM   11043 N  N   . GLN C 3  257  ? -32.387 -22.035  40.922  1.00 87.54  ?  257  GLN C N   1 
ATOM   11044 C  CA  . GLN C 3  257  ? -31.459 -21.470  39.952  1.00 77.84  ?  257  GLN C CA  1 
ATOM   11045 C  C   . GLN C 3  257  ? -32.137 -21.012  38.669  1.00 66.86  ?  257  GLN C C   1 
ATOM   11046 O  O   . GLN C 3  257  ? -31.442 -20.602  37.735  1.00 72.88  ?  257  GLN C O   1 
ATOM   11047 C  CB  . GLN C 3  257  ? -30.371 -22.490  39.600  1.00 75.60  ?  257  GLN C CB  1 
ATOM   11048 C  CG  . GLN C 3  257  ? -29.509 -22.936  40.763  1.00 82.17  ?  257  GLN C CG  1 
ATOM   11049 C  CD  . GLN C 3  257  ? -28.401 -23.871  40.324  1.00 77.74  ?  257  GLN C CD  1 
ATOM   11050 O  OE1 . GLN C 3  257  ? -28.617 -24.762  39.501  1.00 70.17  ?  257  GLN C OE1 1 
ATOM   11051 N  NE2 . GLN C 3  257  ? -27.206 -23.671  40.866  1.00 81.25  ?  257  GLN C NE2 1 
ATOM   11052 N  N   . VAL C 3  258  ? -33.463 -21.084  38.596  1.00 48.39  ?  258  VAL C N   1 
ATOM   11053 C  CA  . VAL C 3  258  ? -34.175 -20.697  37.371  1.00 56.59  ?  258  VAL C CA  1 
ATOM   11054 C  C   . VAL C 3  258  ? -33.888 -19.231  37.067  1.00 59.78  ?  258  VAL C C   1 
ATOM   11055 O  O   . VAL C 3  258  ? -33.922 -18.392  37.989  1.00 70.77  ?  258  VAL C O   1 
ATOM   11056 C  CB  . VAL C 3  258  ? -35.686 -20.946  37.529  1.00 54.02  ?  258  VAL C CB  1 
ATOM   11057 C  CG1 . VAL C 3  258  ? -36.397 -20.835  36.190  1.00 57.02  ?  258  VAL C CG1 1 
ATOM   11058 C  CG2 . VAL C 3  258  ? -35.932 -22.312  38.151  1.00 43.28  ?  258  VAL C CG2 1 
ATOM   11059 N  N   . PRO C 3  259  ? -33.578 -18.869  35.815  1.00 61.48  ?  259  PRO C N   1 
ATOM   11060 C  CA  . PRO C 3  259  ? -33.195 -17.475  35.523  1.00 78.75  ?  259  PRO C CA  1 
ATOM   11061 C  C   . PRO C 3  259  ? -34.213 -16.441  35.975  1.00 86.35  ?  259  PRO C C   1 
ATOM   11062 O  O   . PRO C 3  259  ? -33.831 -15.424  36.569  1.00 84.39  ?  259  PRO C O   1 
ATOM   11063 C  CB  . PRO C 3  259  ? -33.031 -17.480  33.997  1.00 86.49  ?  259  PRO C CB  1 
ATOM   11064 C  CG  . PRO C 3  259  ? -32.655 -18.880  33.671  1.00 78.87  ?  259  PRO C CG  1 
ATOM   11065 C  CD  . PRO C 3  259  ? -33.414 -19.744  34.640  1.00 74.84  ?  259  PRO C CD  1 
ATOM   11066 N  N   . GLY C 3  260  ? -35.498 -16.669  35.716  1.00 59.99  ?  260  GLY C N   1 
ATOM   11067 C  CA  . GLY C 3  260  ? -36.510 -15.735  36.169  1.00 59.85  ?  260  GLY C CA  1 
ATOM   11068 C  C   . GLY C 3  260  ? -36.860 -15.830  37.636  1.00 67.91  ?  260  GLY C C   1 
ATOM   11069 O  O   . GLY C 3  260  ? -37.580 -14.965  38.143  1.00 70.82  ?  260  GLY C O   1 
ATOM   11070 N  N   . TRP C 3  261  ? -36.364 -16.853  38.330  1.00 79.83  ?  261  TRP C N   1 
ATOM   11071 C  CA  . TRP C 3  261  ? -36.691 -17.080  39.732  1.00 71.02  ?  261  TRP C CA  1 
ATOM   11072 C  C   . TRP C 3  261  ? -35.619 -16.580  40.690  1.00 79.84  ?  261  TRP C C   1 
ATOM   11073 O  O   . TRP C 3  261  ? -35.952 -16.051  41.754  1.00 81.47  ?  261  TRP C O   1 
ATOM   11074 C  CB  . TRP C 3  261  ? -36.941 -18.570  39.981  1.00 63.08  ?  261  TRP C CB  1 
ATOM   11075 C  CG  . TRP C 3  261  ? -38.280 -19.028  39.504  1.00 59.53  ?  261  TRP C CG  1 
ATOM   11076 C  CD1 . TRP C 3  261  ? -39.164 -18.319  38.745  1.00 66.87  ?  261  TRP C CD1 1 
ATOM   11077 C  CD2 . TRP C 3  261  ? -38.896 -20.296  39.758  1.00 58.27  ?  261  TRP C CD2 1 
ATOM   11078 N  NE1 . TRP C 3  261  ? -40.291 -19.067  38.507  1.00 71.64  ?  261  TRP C NE1 1 
ATOM   11079 C  CE2 . TRP C 3  261  ? -40.151 -20.285  39.119  1.00 67.09  ?  261  TRP C CE2 1 
ATOM   11080 C  CE3 . TRP C 3  261  ? -38.507 -21.439  40.463  1.00 58.51  ?  261  TRP C CE3 1 
ATOM   11081 C  CZ2 . TRP C 3  261  ? -41.020 -21.373  39.163  1.00 72.80  ?  261  TRP C CZ2 1 
ATOM   11082 C  CZ3 . TRP C 3  261  ? -39.371 -22.517  40.505  1.00 62.45  ?  261  TRP C CZ3 1 
ATOM   11083 C  CH2 . TRP C 3  261  ? -40.612 -22.477  39.860  1.00 69.98  ?  261  TRP C CH2 1 
ATOM   11084 N  N   . GLN C 3  262  ? -34.339 -16.736  40.350  1.00 87.89  ?  262  GLN C N   1 
ATOM   11085 C  CA  . GLN C 3  262  ? -33.264 -16.232  41.206  1.00 84.73  ?  262  GLN C CA  1 
ATOM   11086 C  C   . GLN C 3  262  ? -33.179 -14.720  41.021  1.00 90.74  ?  262  GLN C C   1 
ATOM   11087 O  O   . GLN C 3  262  ? -32.352 -14.185  40.278  1.00 98.37  ?  262  GLN C O   1 
ATOM   11088 C  CB  . GLN C 3  262  ? -31.941 -16.920  40.897  1.00 85.18  ?  262  GLN C CB  1 
ATOM   11089 C  CG  . GLN C 3  262  ? -30.783 -16.406  41.745  1.00 80.79  ?  262  GLN C CG  1 
ATOM   11090 C  CD  . GLN C 3  262  ? -29.929 -17.517  42.317  1.00 88.67  ?  262  GLN C CD  1 
ATOM   11091 O  OE1 . GLN C 3  262  ? -30.090 -18.684  41.962  1.00 96.28  ?  262  GLN C OE1 1 
ATOM   11092 N  NE2 . GLN C 3  262  ? -29.015 -17.159  43.211  1.00 89.51  ?  262  GLN C NE2 1 
ATOM   11093 N  N   . VAL C 3  263  ? -34.078 -14.023  41.708  1.00 72.57  ?  263  VAL C N   1 
ATOM   11094 C  CA  . VAL C 3  263  ? -34.084 -12.568  41.767  1.00 75.95  ?  263  VAL C CA  1 
ATOM   11095 C  C   . VAL C 3  263  ? -34.005 -12.186  43.238  1.00 74.57  ?  263  VAL C C   1 
ATOM   11096 O  O   . VAL C 3  263  ? -34.833 -12.629  44.045  1.00 75.31  ?  263  VAL C O   1 
ATOM   11097 C  CB  . VAL C 3  263  ? -35.332 -11.969  41.100  1.00 77.73  ?  263  VAL C CB  1 
ATOM   11098 C  CG1 . VAL C 3  263  ? -35.373 -10.462  41.299  1.00 75.21  ?  263  VAL C CG1 1 
ATOM   11099 C  CG2 . VAL C 3  263  ? -35.369 -12.325  39.619  1.00 78.79  ?  263  VAL C CG2 1 
ATOM   11100 N  N   . THR C 3  264  ? -33.011 -11.368  43.585  1.00 62.37  ?  264  THR C N   1 
ATOM   11101 C  CA  . THR C 3  264  ? -32.701 -11.122  44.987  1.00 55.90  ?  264  THR C CA  1 
ATOM   11102 C  C   . THR C 3  264  ? -33.738 -10.237  45.672  1.00 60.83  ?  264  THR C C   1 
ATOM   11103 O  O   . THR C 3  264  ? -33.850 -10.273  46.901  1.00 66.10  ?  264  THR C O   1 
ATOM   11104 C  CB  . THR C 3  264  ? -31.306 -10.498  45.097  1.00 56.01  ?  264  THR C CB  1 
ATOM   11105 O  OG1 . THR C 3  264  ? -30.386 -11.256  44.304  1.00 66.67  ?  264  THR C OG1 1 
ATOM   11106 C  CG2 . THR C 3  264  ? -30.816 -10.532  46.524  1.00 61.12  ?  264  THR C CG2 1 
ATOM   11107 N  N   . VAL C 3  265  ? -34.515 -9.469   44.910  1.00 81.44  ?  265  VAL C N   1 
ATOM   11108 C  CA  . VAL C 3  265  ? -35.455 -8.512   45.487  1.00 80.77  ?  265  VAL C CA  1 
ATOM   11109 C  C   . VAL C 3  265  ? -36.814 -9.172   45.694  1.00 80.37  ?  265  VAL C C   1 
ATOM   11110 O  O   . VAL C 3  265  ? -37.803 -8.500   46.008  1.00 84.87  ?  265  VAL C O   1 
ATOM   11111 C  CB  . VAL C 3  265  ? -35.570 -7.254   44.602  1.00 79.98  ?  265  VAL C CB  1 
ATOM   11112 C  CG1 . VAL C 3  265  ? -36.466 -7.517   43.391  1.00 82.18  ?  265  VAL C CG1 1 
ATOM   11113 C  CG2 . VAL C 3  265  ? -36.052 -6.050   45.411  1.00 78.37  ?  265  VAL C CG2 1 
ATOM   11114 N  N   . PHE C 3  266  ? -36.871 -10.493  45.540  1.00 84.65  ?  266  PHE C N   1 
ATOM   11115 C  CA  . PHE C 3  266  ? -38.147 -11.194  45.675  1.00 87.24  ?  266  PHE C CA  1 
ATOM   11116 C  C   . PHE C 3  266  ? -38.795 -11.085  47.056  1.00 88.49  ?  266  PHE C C   1 
ATOM   11117 O  O   . PHE C 3  266  ? -40.031 -10.956  47.105  1.00 90.70  ?  266  PHE C O   1 
ATOM   11118 C  CB  . PHE C 3  266  ? -37.973 -12.665  45.272  1.00 88.53  ?  266  PHE C CB  1 
ATOM   11119 C  CG  . PHE C 3  266  ? -38.281 -12.933  43.826  1.00 86.11  ?  266  PHE C CG  1 
ATOM   11120 C  CD1 . PHE C 3  266  ? -38.520 -11.886  42.951  1.00 90.63  ?  266  PHE C CD1 1 
ATOM   11121 C  CD2 . PHE C 3  266  ? -38.342 -14.229  43.343  1.00 90.82  ?  266  PHE C CD2 1 
ATOM   11122 C  CE1 . PHE C 3  266  ? -38.809 -12.126  41.621  1.00 92.91  ?  266  PHE C CE1 1 
ATOM   11123 C  CE2 . PHE C 3  266  ? -38.630 -14.475  42.013  1.00 97.95  ?  266  PHE C CE2 1 
ATOM   11124 C  CZ  . PHE C 3  266  ? -38.862 -13.422  41.151  1.00 94.04  ?  266  PHE C CZ  1 
ATOM   11125 N  N   . PRO C 3  267  ? -38.079 -11.143  48.181  1.00 76.05  ?  267  PRO C N   1 
ATOM   11126 C  CA  . PRO C 3  267  ? -38.761 -11.081  49.489  1.00 76.72  ?  267  PRO C CA  1 
ATOM   11127 C  C   . PRO C 3  267  ? -39.561 -9.799   49.672  1.00 82.42  ?  267  PRO C C   1 
ATOM   11128 O  O   . PRO C 3  267  ? -40.760 -9.872   49.978  1.00 85.12  ?  267  PRO C O   1 
ATOM   11129 C  CB  . PRO C 3  267  ? -37.610 -11.196  50.501  1.00 74.14  ?  267  PRO C CB  1 
ATOM   11130 C  CG  . PRO C 3  267  ? -36.574 -11.960  49.779  1.00 73.67  ?  267  PRO C CG  1 
ATOM   11131 C  CD  . PRO C 3  267  ? -36.664 -11.537  48.339  1.00 75.76  ?  267  PRO C CD  1 
ATOM   11132 N  N   . PRO C 3  268  ? -38.972 -8.605   49.496  1.00 66.74  ?  268  PRO C N   1 
ATOM   11133 C  CA  . PRO C 3  268  ? -39.796 -7.396   49.664  1.00 57.87  ?  268  PRO C CA  1 
ATOM   11134 C  C   . PRO C 3  268  ? -40.793 -7.201   48.538  1.00 63.02  ?  268  PRO C C   1 
ATOM   11135 O  O   . PRO C 3  268  ? -41.890 -6.679   48.777  1.00 68.54  ?  268  PRO C O   1 
ATOM   11136 C  CB  . PRO C 3  268  ? -38.762 -6.258   49.707  1.00 54.59  ?  268  PRO C CB  1 
ATOM   11137 C  CG  . PRO C 3  268  ? -37.432 -6.931   49.846  1.00 52.02  ?  268  PRO C CG  1 
ATOM   11138 C  CD  . PRO C 3  268  ? -37.593 -8.228   49.140  1.00 62.75  ?  268  PRO C CD  1 
ATOM   11139 N  N   . TYR C 3  269  ? -40.440 -7.604   47.317  1.00 97.51  ?  269  TYR C N   1 
ATOM   11140 C  CA  . TYR C 3  269  ? -41.372 -7.521   46.198  1.00 102.53 ?  269  TYR C CA  1 
ATOM   11141 C  C   . TYR C 3  269  ? -42.596 -8.399   46.430  1.00 101.80 ?  269  TYR C C   1 
ATOM   11142 O  O   . TYR C 3  269  ? -43.719 -8.019   46.076  1.00 102.51 ?  269  TYR C O   1 
ATOM   11143 C  CB  . TYR C 3  269  ? -40.651 -7.914   44.909  1.00 101.30 ?  269  TYR C CB  1 
ATOM   11144 C  CG  . TYR C 3  269  ? -41.535 -8.096   43.702  1.00 104.93 ?  269  TYR C CG  1 
ATOM   11145 C  CD1 . TYR C 3  269  ? -42.133 -7.009   43.079  1.00 110.72 ?  269  TYR C CD1 1 
ATOM   11146 C  CD2 . TYR C 3  269  ? -41.753 -9.359   43.171  1.00 99.99  ?  269  TYR C CD2 1 
ATOM   11147 C  CE1 . TYR C 3  269  ? -42.936 -7.179   41.967  1.00 110.68 ?  269  TYR C CE1 1 
ATOM   11148 C  CE2 . TYR C 3  269  ? -42.549 -9.538   42.065  1.00 109.38 ?  269  TYR C CE2 1 
ATOM   11149 C  CZ  . TYR C 3  269  ? -43.138 -8.447   41.466  1.00 115.92 ?  269  TYR C CZ  1 
ATOM   11150 O  OH  . TYR C 3  269  ? -43.933 -8.632   40.361  1.00 119.52 ?  269  TYR C OH  1 
ATOM   11151 N  N   . PHE C 3  270  ? -42.402 -9.575   47.031  1.00 85.19  ?  270  PHE C N   1 
ATOM   11152 C  CA  . PHE C 3  270  ? -43.532 -10.453  47.314  1.00 85.81  ?  270  PHE C CA  1 
ATOM   11153 C  C   . PHE C 3  270  ? -44.379 -9.908   48.457  1.00 91.53  ?  270  PHE C C   1 
ATOM   11154 O  O   . PHE C 3  270  ? -45.610 -10.030  48.438  1.00 101.89 ?  270  PHE C O   1 
ATOM   11155 C  CB  . PHE C 3  270  ? -43.035 -11.860  47.641  1.00 77.10  ?  270  PHE C CB  1 
ATOM   11156 C  CG  . PHE C 3  270  ? -43.056 -12.799  46.470  1.00 77.51  ?  270  PHE C CG  1 
ATOM   11157 C  CD1 . PHE C 3  270  ? -42.271 -12.554  45.356  1.00 81.55  ?  270  PHE C CD1 1 
ATOM   11158 C  CD2 . PHE C 3  270  ? -43.857 -13.929  46.485  1.00 80.34  ?  270  PHE C CD2 1 
ATOM   11159 C  CE1 . PHE C 3  270  ? -42.284 -13.417  44.277  1.00 81.44  ?  270  PHE C CE1 1 
ATOM   11160 C  CE2 . PHE C 3  270  ? -43.875 -14.796  45.410  1.00 81.05  ?  270  PHE C CE2 1 
ATOM   11161 C  CZ  . PHE C 3  270  ? -43.088 -14.539  44.304  1.00 82.81  ?  270  PHE C CZ  1 
ATOM   11162 N  N   . VAL C 3  271  ? -43.736 -9.311   49.463  1.00 72.78  ?  271  VAL C N   1 
ATOM   11163 C  CA  . VAL C 3  271  ? -44.474 -8.726   50.580  1.00 69.38  ?  271  VAL C CA  1 
ATOM   11164 C  C   . VAL C 3  271  ? -45.331 -7.564   50.096  1.00 71.91  ?  271  VAL C C   1 
ATOM   11165 O  O   . VAL C 3  271  ? -46.514 -7.454   50.441  1.00 78.04  ?  271  VAL C O   1 
ATOM   11166 C  CB  . VAL C 3  271  ? -43.506 -8.288   51.693  1.00 70.98  ?  271  VAL C CB  1 
ATOM   11167 C  CG1 . VAL C 3  271  ? -44.223 -7.417   52.712  1.00 73.84  ?  271  VAL C CG1 1 
ATOM   11168 C  CG2 . VAL C 3  271  ? -42.894 -9.502   52.372  1.00 67.05  ?  271  VAL C CG2 1 
ATOM   11169 N  N   . ALA C 3  272  ? -44.746 -6.683   49.281  1.00 62.09  ?  272  ALA C N   1 
ATOM   11170 C  CA  . ALA C 3  272  ? -45.501 -5.550   48.754  1.00 62.19  ?  272  ALA C CA  1 
ATOM   11171 C  C   . ALA C 3  272  ? -46.633 -6.016   47.850  1.00 69.70  ?  272  ALA C C   1 
ATOM   11172 O  O   . ALA C 3  272  ? -47.728 -5.442   47.868  1.00 75.17  ?  272  ALA C O   1 
ATOM   11173 C  CB  . ALA C 3  272  ? -44.568 -4.602   48.003  1.00 50.71  ?  272  ALA C CB  1 
ATOM   11174 N  N   . GLY C 3  273  ? -46.391 -7.056   47.051  1.00 89.62  ?  273  GLY C N   1 
ATOM   11175 C  CA  . GLY C 3  273  ? -47.443 -7.572   46.192  1.00 93.11  ?  273  GLY C CA  1 
ATOM   11176 C  C   . GLY C 3  273  ? -48.559 -8.237   46.973  1.00 92.46  ?  273  GLY C C   1 
ATOM   11177 O  O   . GLY C 3  273  ? -49.733 -8.137   46.604  1.00 97.12  ?  273  GLY C O   1 
ATOM   11178 N  N   . ALA C 3  274  ? -48.212 -8.922   48.063  1.00 89.39  ?  274  ALA C N   1 
ATOM   11179 C  CA  . ALA C 3  274  ? -49.228 -9.567   48.888  1.00 95.95  ?  274  ALA C CA  1 
ATOM   11180 C  C   . ALA C 3  274  ? -50.167 -8.536   49.503  1.00 99.36  ?  274  ALA C C   1 
ATOM   11181 O  O   . ALA C 3  274  ? -51.393 -8.643   49.383  1.00 102.48 ?  274  ALA C O   1 
ATOM   11182 C  CB  . ALA C 3  274  ? -48.560 -10.407  49.974  1.00 92.80  ?  274  ALA C CB  1 
ATOM   11183 N  N   . VAL C 3  275  ? -49.604 -7.520   50.160  1.00 115.29 ?  275  VAL C N   1 
ATOM   11184 C  CA  . VAL C 3  275  ? -50.429 -6.483   50.770  1.00 113.77 ?  275  VAL C CA  1 
ATOM   11185 C  C   . VAL C 3  275  ? -51.131 -5.651   49.699  1.00 114.66 ?  275  VAL C C   1 
ATOM   11186 O  O   . VAL C 3  275  ? -52.185 -5.057   49.956  1.00 120.69 ?  275  VAL C O   1 
ATOM   11187 C  CB  . VAL C 3  275  ? -49.566 -5.622   51.713  1.00 105.77 ?  275  VAL C CB  1 
ATOM   11188 C  CG1 . VAL C 3  275  ? -48.471 -4.910   50.939  1.00 113.10 ?  275  VAL C CG1 1 
ATOM   11189 C  CG2 . VAL C 3  275  ? -50.418 -4.635   52.492  1.00 104.91 ?  275  VAL C CG2 1 
ATOM   11190 N  N   . PHE C 3  276  ? -50.576 -5.607   48.485  1.00 106.99 ?  276  PHE C N   1 
ATOM   11191 C  CA  . PHE C 3  276  ? -51.254 -4.953   47.369  1.00 109.26 ?  276  PHE C CA  1 
ATOM   11192 C  C   . PHE C 3  276  ? -52.565 -5.658   47.036  1.00 111.22 ?  276  PHE C C   1 
ATOM   11193 O  O   . PHE C 3  276  ? -53.637 -5.043   47.038  1.00 106.51 ?  276  PHE C O   1 
ATOM   11194 C  CB  . PHE C 3  276  ? -50.330 -4.921   46.149  1.00 111.27 ?  276  PHE C CB  1 
ATOM   11195 C  CG  . PHE C 3  276  ? -50.849 -4.092   45.008  1.00 109.82 ?  276  PHE C CG  1 
ATOM   11196 C  CD1 . PHE C 3  276  ? -51.511 -2.898   45.236  1.00 113.30 ?  276  PHE C CD1 1 
ATOM   11197 C  CD2 . PHE C 3  276  ? -50.665 -4.509   43.700  1.00 111.28 ?  276  PHE C CD2 1 
ATOM   11198 C  CE1 . PHE C 3  276  ? -51.983 -2.139   44.178  1.00 116.84 ?  276  PHE C CE1 1 
ATOM   11199 C  CE2 . PHE C 3  276  ? -51.134 -3.755   42.641  1.00 110.85 ?  276  PHE C CE2 1 
ATOM   11200 C  CZ  . PHE C 3  276  ? -51.793 -2.570   42.880  1.00 118.00 ?  276  PHE C CZ  1 
ATOM   11201 N  N   . ALA C 3  277  ? -52.492 -6.960   46.741  1.00 99.48  ?  277  ALA C N   1 
ATOM   11202 C  CA  . ALA C 3  277  ? -53.697 -7.717   46.417  1.00 93.28  ?  277  ALA C CA  1 
ATOM   11203 C  C   . ALA C 3  277  ? -54.635 -7.821   47.611  1.00 93.38  ?  277  ALA C C   1 
ATOM   11204 O  O   . ALA C 3  277  ? -55.855 -7.922   47.436  1.00 93.42  ?  277  ALA C O   1 
ATOM   11205 C  CB  . ALA C 3  277  ? -53.322 -9.112   45.920  1.00 88.44  ?  277  ALA C CB  1 
ATOM   11206 N  N   . GLY C 3  278  ? -54.089 -7.803   48.828  1.00 80.89  ?  278  GLY C N   1 
ATOM   11207 C  CA  . GLY C 3  278  ? -54.937 -7.891   50.006  1.00 81.58  ?  278  GLY C CA  1 
ATOM   11208 C  C   . GLY C 3  278  ? -55.820 -6.669   50.176  1.00 81.01  ?  278  GLY C C   1 
ATOM   11209 O  O   . GLY C 3  278  ? -57.024 -6.789   50.417  1.00 84.12  ?  278  GLY C O   1 
ATOM   11210 N  N   . PHE C 3  279  ? -55.231 -5.475   50.056  1.00 92.65  ?  279  PHE C N   1 
ATOM   11211 C  CA  . PHE C 3  279  ? -56.022 -4.251   50.151  1.00 87.24  ?  279  PHE C CA  1 
ATOM   11212 C  C   . PHE C 3  279  ? -57.059 -4.167   49.039  1.00 91.41  ?  279  PHE C C   1 
ATOM   11213 O  O   . PHE C 3  279  ? -58.140 -3.605   49.242  1.00 90.18  ?  279  PHE C O   1 
ATOM   11214 C  CB  . PHE C 3  279  ? -55.109 -3.024   50.117  1.00 87.31  ?  279  PHE C CB  1 
ATOM   11215 C  CG  . PHE C 3  279  ? -54.683 -2.543   51.477  1.00 91.30  ?  279  PHE C CG  1 
ATOM   11216 C  CD1 . PHE C 3  279  ? -55.467 -1.648   52.186  1.00 93.92  ?  279  PHE C CD1 1 
ATOM   11217 C  CD2 . PHE C 3  279  ? -53.495 -2.973   52.039  1.00 93.61  ?  279  PHE C CD2 1 
ATOM   11218 C  CE1 . PHE C 3  279  ? -55.078 -1.202   53.435  1.00 91.95  ?  279  PHE C CE1 1 
ATOM   11219 C  CE2 . PHE C 3  279  ? -53.101 -2.530   53.288  1.00 96.93  ?  279  PHE C CE2 1 
ATOM   11220 C  CZ  . PHE C 3  279  ? -53.894 -1.643   53.985  1.00 94.52  ?  279  PHE C CZ  1 
ATOM   11221 N  N   . ALA C 3  280  ? -56.751 -4.715   47.862  1.00 115.96 ?  280  ALA C N   1 
ATOM   11222 C  CA  . ALA C 3  280  ? -57.727 -4.732   46.778  1.00 109.60 ?  280  ALA C CA  1 
ATOM   11223 C  C   . ALA C 3  280  ? -58.909 -5.631   47.119  1.00 112.83 ?  280  ALA C C   1 
ATOM   11224 O  O   . ALA C 3  280  ? -60.069 -5.260   46.903  1.00 109.99 ?  280  ALA C O   1 
ATOM   11225 C  CB  . ALA C 3  280  ? -57.059 -5.186   45.480  1.00 112.93 ?  280  ALA C CB  1 
ATOM   11226 N  N   . MET C 3  281  ? -58.632 -6.821   47.657  1.00 101.08 ?  281  MET C N   1 
ATOM   11227 C  CA  . MET C 3  281  ? -59.709 -7.727   48.044  1.00 90.80  ?  281  MET C CA  1 
ATOM   11228 C  C   . MET C 3  281  ? -60.497 -7.179   49.227  1.00 99.45  ?  281  MET C C   1 
ATOM   11229 O  O   . MET C 3  281  ? -61.717 -7.363   49.304  1.00 100.04 ?  281  MET C O   1 
ATOM   11230 C  CB  . MET C 3  281  ? -59.142 -9.107   48.375  1.00 99.38  ?  281  MET C CB  1 
ATOM   11231 C  CG  . MET C 3  281  ? -60.166 -10.230  48.315  1.00 104.21 ?  281  MET C CG  1 
ATOM   11232 S  SD  . MET C 3  281  ? -60.598 -10.704  46.630  1.00 119.19 ?  281  MET C SD  1 
ATOM   11233 C  CE  . MET C 3  281  ? -62.145 -11.563  46.910  1.00 106.34 ?  281  MET C CE  1 
ATOM   11234 N  N   . VAL C 3  282  ? -59.819 -6.507   50.159  1.00 105.47 ?  282  VAL C N   1 
ATOM   11235 C  CA  . VAL C 3  282  ? -60.507 -5.992   51.339  1.00 108.71 ?  282  VAL C CA  1 
ATOM   11236 C  C   . VAL C 3  282  ? -61.440 -4.848   50.956  1.00 102.94 ?  282  VAL C C   1 
ATOM   11237 O  O   . VAL C 3  282  ? -62.580 -4.778   51.430  1.00 102.58 ?  282  VAL C O   1 
ATOM   11238 C  CB  . VAL C 3  282  ? -59.485 -5.572   52.412  1.00 114.22 ?  282  VAL C CB  1 
ATOM   11239 C  CG1 . VAL C 3  282  ? -60.149 -4.722   53.476  1.00 104.12 ?  282  VAL C CG1 1 
ATOM   11240 C  CG2 . VAL C 3  282  ? -58.843 -6.800   53.042  1.00 117.01 ?  282  VAL C CG2 1 
ATOM   11241 N  N   . LEU C 3  283  ? -60.981 -3.940   50.089  1.00 75.57  ?  283  LEU C N   1 
ATOM   11242 C  CA  . LEU C 3  283  ? -61.864 -2.893   49.581  1.00 75.04  ?  283  LEU C CA  1 
ATOM   11243 C  C   . LEU C 3  283  ? -63.035 -3.486   48.806  1.00 77.43  ?  283  LEU C C   1 
ATOM   11244 O  O   . LEU C 3  283  ? -64.176 -3.028   48.942  1.00 77.85  ?  283  LEU C O   1 
ATOM   11245 C  CB  . LEU C 3  283  ? -61.088 -1.921   48.691  1.00 72.29  ?  283  LEU C CB  1 
ATOM   11246 C  CG  . LEU C 3  283  ? -60.077 -0.967   49.326  1.00 70.44  ?  283  LEU C CG  1 
ATOM   11247 C  CD1 . LEU C 3  283  ? -59.301 -0.233   48.245  1.00 69.20  ?  283  LEU C CD1 1 
ATOM   11248 C  CD2 . LEU C 3  283  ? -60.784 0.020    50.236  1.00 80.12  ?  283  LEU C CD2 1 
ATOM   11249 N  N   . LEU C 3  284  ? -62.768 -4.506   47.986  1.00 111.10 ?  284  LEU C N   1 
ATOM   11250 C  CA  . LEU C 3  284  ? -63.821 -5.115   47.181  1.00 107.34 ?  284  LEU C CA  1 
ATOM   11251 C  C   . LEU C 3  284  ? -64.888 -5.773   48.045  1.00 107.39 ?  284  LEU C C   1 
ATOM   11252 O  O   . LEU C 3  284  ? -66.058 -5.825   47.651  1.00 106.93 ?  284  LEU C O   1 
ATOM   11253 C  CB  . LEU C 3  284  ? -63.213 -6.138   46.222  1.00 108.21 ?  284  LEU C CB  1 
ATOM   11254 C  CG  . LEU C 3  284  ? -63.881 -6.294   44.856  1.00 109.44 ?  284  LEU C CG  1 
ATOM   11255 C  CD1 . LEU C 3  284  ? -63.899 -4.972   44.113  1.00 107.88 ?  284  LEU C CD1 1 
ATOM   11256 C  CD2 . LEU C 3  284  ? -63.169 -7.360   44.039  1.00 110.60 ?  284  LEU C CD2 1 
ATOM   11257 N  N   . LEU C 3  285  ? -64.511 -6.276   49.221  1.00 99.22  ?  285  LEU C N   1 
ATOM   11258 C  CA  . LEU C 3  285  ? -65.442 -6.988   50.085  1.00 96.15  ?  285  LEU C CA  1 
ATOM   11259 C  C   . LEU C 3  285  ? -66.002 -6.135   51.215  1.00 95.99  ?  285  LEU C C   1 
ATOM   11260 O  O   . LEU C 3  285  ? -67.012 -6.522   51.813  1.00 96.21  ?  285  LEU C O   1 
ATOM   11261 C  CB  . LEU C 3  285  ? -64.769 -8.229   50.684  1.00 96.99  ?  285  LEU C CB  1 
ATOM   11262 C  CG  . LEU C 3  285  ? -64.716 -9.460   49.779  1.00 88.97  ?  285  LEU C CG  1 
ATOM   11263 C  CD1 . LEU C 3  285  ? -64.119 -10.643  50.521  1.00 80.57  ?  285  LEU C CD1 1 
ATOM   11264 C  CD2 . LEU C 3  285  ? -66.103 -9.796   49.254  1.00 86.74  ?  285  LEU C CD2 1 
ATOM   11265 N  N   . MET C 3  286  ? -65.382 -4.997   51.524  1.00 88.08  ?  286  MET C N   1 
ATOM   11266 C  CA  . MET C 3  286  ? -65.867 -4.146   52.604  1.00 84.33  ?  286  MET C CA  1 
ATOM   11267 C  C   . MET C 3  286  ? -66.805 -3.049   52.123  1.00 84.15  ?  286  MET C C   1 
ATOM   11268 O  O   . MET C 3  286  ? -67.651 -2.590   52.900  1.00 84.09  ?  286  MET C O   1 
ATOM   11269 C  CB  . MET C 3  286  ? -64.692 -3.515   53.357  1.00 85.01  ?  286  MET C CB  1 
ATOM   11270 C  CG  . MET C 3  286  ? -64.988 -3.203   54.815  1.00 92.26  ?  286  MET C CG  1 
ATOM   11271 S  SD  . MET C 3  286  ? -64.808 -4.645   55.881  1.00 99.71  ?  286  MET C SD  1 
ATOM   11272 C  CE  . MET C 3  286  ? -63.113 -5.110   55.541  1.00 91.75  ?  286  MET C CE  1 
ATOM   11273 N  N   . ILE C 3  287  ? -66.673 -2.610   50.869  1.00 81.80  ?  287  ILE C N   1 
ATOM   11274 C  CA  . ILE C 3  287  ? -67.601 -1.612   50.333  1.00 84.20  ?  287  ILE C CA  1 
ATOM   11275 C  C   . ILE C 3  287  ? -69.039 -2.121   50.324  1.00 87.08  ?  287  ILE C C   1 
ATOM   11276 O  O   . ILE C 3  287  ? -69.934 -1.381   50.766  1.00 86.20  ?  287  ILE C O   1 
ATOM   11277 C  CB  . ILE C 3  287  ? -67.126 -1.137   48.948  1.00 85.73  ?  287  ILE C CB  1 
ATOM   11278 C  CG1 . ILE C 3  287  ? -65.910 -0.218   49.084  1.00 81.80  ?  287  ILE C CG1 1 
ATOM   11279 C  CG2 . ILE C 3  287  ? -68.251 -0.433   48.207  1.00 81.88  ?  287  ILE C CG2 1 
ATOM   11280 C  CD1 . ILE C 3  287  ? -65.294 0.177    47.760  1.00 79.94  ?  287  ILE C CD1 1 
ATOM   11281 N  N   . PRO C 3  288  ? -69.338 -3.340   49.855  1.00 78.77  ?  288  PRO C N   1 
ATOM   11282 C  CA  . PRO C 3  288  ? -70.724 -3.822   49.982  1.00 84.23  ?  288  PRO C CA  1 
ATOM   11283 C  C   . PRO C 3  288  ? -71.146 -4.041   51.424  1.00 80.70  ?  288  PRO C C   1 
ATOM   11284 O  O   . PRO C 3  288  ? -72.306 -3.784   51.768  1.00 83.18  ?  288  PRO C O   1 
ATOM   11285 C  CB  . PRO C 3  288  ? -70.717 -5.133   49.182  1.00 84.91  ?  288  PRO C CB  1 
ATOM   11286 C  CG  . PRO C 3  288  ? -69.542 -5.018   48.271  1.00 72.03  ?  288  PRO C CG  1 
ATOM   11287 C  CD  . PRO C 3  288  ? -68.519 -4.280   49.069  1.00 72.30  ?  288  PRO C CD  1 
ATOM   11288 N  N   . VAL C 3  289  ? -70.235 -4.513   52.279  1.00 77.94  ?  289  VAL C N   1 
ATOM   11289 C  CA  . VAL C 3  289  ? -70.559 -4.695   53.692  1.00 80.37  ?  289  VAL C CA  1 
ATOM   11290 C  C   . VAL C 3  289  ? -70.896 -3.356   54.337  1.00 81.76  ?  289  VAL C C   1 
ATOM   11291 O  O   . VAL C 3  289  ? -71.816 -3.257   55.158  1.00 75.65  ?  289  VAL C O   1 
ATOM   11292 C  CB  . VAL C 3  289  ? -69.398 -5.404   54.416  1.00 81.47  ?  289  VAL C CB  1 
ATOM   11293 C  CG1 . VAL C 3  289  ? -69.527 -5.253   55.922  1.00 78.13  ?  289  VAL C CG1 1 
ATOM   11294 C  CG2 . VAL C 3  289  ? -69.355 -6.873   54.030  1.00 81.34  ?  289  VAL C CG2 1 
ATOM   11295 N  N   . ARG C 3  290  ? -70.168 -2.301   53.963  1.00 121.52 ?  290  ARG C N   1 
ATOM   11296 C  CA  . ARG C 3  290  ? -70.448 -0.977   54.507  1.00 116.08 ?  290  ARG C CA  1 
ATOM   11297 C  C   . ARG C 3  290  ? -71.785 -0.441   54.008  1.00 127.29 ?  290  ARG C C   1 
ATOM   11298 O  O   . ARG C 3  290  ? -72.568 0.113    54.788  1.00 133.39 ?  290  ARG C O   1 
ATOM   11299 C  CB  . ARG C 3  290  ? -69.319 -0.014   54.143  1.00 118.43 ?  290  ARG C CB  1 
ATOM   11300 C  CG  . ARG C 3  290  ? -69.706 1.453    54.219  1.00 126.41 ?  290  ARG C CG  1 
ATOM   11301 C  CD  . ARG C 3  290  ? -68.694 2.330    53.505  1.00 131.34 ?  290  ARG C CD  1 
ATOM   11302 N  NE  . ARG C 3  290  ? -69.040 3.743    53.597  1.00 132.67 ?  290  ARG C NE  1 
ATOM   11303 C  CZ  . ARG C 3  290  ? -69.686 4.417    52.655  1.00 134.56 ?  290  ARG C CZ  1 
ATOM   11304 N  NH1 . ARG C 3  290  ? -70.074 3.835    51.532  1.00 140.03 ?  290  ARG C NH1 1 
ATOM   11305 N  NH2 . ARG C 3  290  ? -69.948 5.707    52.844  1.00 130.11 ?  290  ARG C NH2 1 
ATOM   11306 N  N   . THR C 3  291  ? -72.065 -0.598   52.713  1.00 128.57 ?  291  THR C N   1 
ATOM   11307 C  CA  . THR C 3  291  ? -73.257 0.001    52.123  1.00 132.88 ?  291  THR C CA  1 
ATOM   11308 C  C   . THR C 3  291  ? -74.523 -0.808   52.376  1.00 130.58 ?  291  THR C C   1 
ATOM   11309 O  O   . THR C 3  291  ? -75.623 -0.281   52.181  1.00 137.57 ?  291  THR C O   1 
ATOM   11310 C  CB  . THR C 3  291  ? -73.062 0.190    50.615  1.00 137.18 ?  291  THR C CB  1 
ATOM   11311 O  OG1 . THR C 3  291  ? -74.001 1.158    50.127  1.00 137.90 ?  291  THR C OG1 1 
ATOM   11312 C  CG2 . THR C 3  291  ? -73.268 -1.124   49.874  1.00 138.55 ?  291  THR C CG2 1 
ATOM   11313 N  N   . PHE C 3  292  ? -74.402 -2.064   52.807  1.00 91.00  ?  292  PHE C N   1 
ATOM   11314 C  CA  . PHE C 3  292  ? -75.577 -2.896   53.050  1.00 94.54  ?  292  PHE C CA  1 
ATOM   11315 C  C   . PHE C 3  292  ? -76.105 -2.710   54.470  1.00 98.14  ?  292  PHE C C   1 
ATOM   11316 O  O   . PHE C 3  292  ? -77.266 -2.336   54.664  1.00 113.52 ?  292  PHE C O   1 
ATOM   11317 C  CB  . PHE C 3  292  ? -75.248 -4.367   52.777  1.00 107.60 ?  292  PHE C CB  1 
ATOM   11318 C  CG  . PHE C 3  292  ? -75.256 -4.726   51.317  1.00 108.21 ?  292  PHE C CG  1 
ATOM   11319 C  CD1 . PHE C 3  292  ? -75.847 -3.886   50.387  1.00 98.60  ?  292  PHE C CD1 1 
ATOM   11320 C  CD2 . PHE C 3  292  ? -74.671 -5.902   50.874  1.00 106.28 ?  292  PHE C CD2 1 
ATOM   11321 C  CE1 . PHE C 3  292  ? -75.856 -4.210   49.044  1.00 94.27  ?  292  PHE C CE1 1 
ATOM   11322 C  CE2 . PHE C 3  292  ? -74.677 -6.232   49.532  1.00 100.58 ?  292  PHE C CE2 1 
ATOM   11323 C  CZ  . PHE C 3  292  ? -75.271 -5.385   48.616  1.00 97.63  ?  292  PHE C CZ  1 
ATOM   11324 N  N   . TYR C 3  293  ? -75.268 -2.971   55.468  1.00 122.13 ?  293  TYR C N   1 
ATOM   11325 C  CA  . TYR C 3  293  ? -75.649 -2.699   56.843  1.00 134.00 ?  293  TYR C CA  1 
ATOM   11326 C  C   . TYR C 3  293  ? -75.488 -1.212   57.147  1.00 133.18 ?  293  TYR C C   1 
ATOM   11327 O  O   . TYR C 3  293  ? -74.757 -0.487   56.466  1.00 132.94 ?  293  TYR C O   1 
ATOM   11328 C  CB  . TYR C 3  293  ? -74.808 -3.530   57.812  1.00 128.97 ?  293  TYR C CB  1 
ATOM   11329 C  CG  . TYR C 3  293  ? -74.852 -5.018   57.545  1.00 129.73 ?  293  TYR C CG  1 
ATOM   11330 C  CD1 . TYR C 3  293  ? -75.873 -5.806   58.061  1.00 131.88 ?  293  TYR C CD1 1 
ATOM   11331 C  CD2 . TYR C 3  293  ? -73.872 -5.634   56.778  1.00 128.32 ?  293  TYR C CD2 1 
ATOM   11332 C  CE1 . TYR C 3  293  ? -75.915 -7.167   57.820  1.00 133.21 ?  293  TYR C CE1 1 
ATOM   11333 C  CE2 . TYR C 3  293  ? -73.907 -6.993   56.531  1.00 127.30 ?  293  TYR C CE2 1 
ATOM   11334 C  CZ  . TYR C 3  293  ? -74.930 -7.755   57.055  1.00 128.69 ?  293  TYR C CZ  1 
ATOM   11335 O  OH  . TYR C 3  293  ? -74.968 -9.108   56.812  1.00 120.73 ?  293  TYR C OH  1 
ATOM   11336 N  N   . GLY C 3  294  ? -76.181 -0.760   58.188  1.00 146.61 ?  294  GLY C N   1 
ATOM   11337 C  CA  . GLY C 3  294  ? -76.103 0.633    58.587  1.00 144.14 ?  294  GLY C CA  1 
ATOM   11338 C  C   . GLY C 3  294  ? -74.773 0.996    59.216  1.00 146.83 ?  294  GLY C C   1 
ATOM   11339 O  O   . GLY C 3  294  ? -74.729 1.520    60.333  1.00 153.49 ?  294  GLY C O   1 
ATOM   11340 N  N   . PHE C 3  295  ? -73.679 0.730    58.501  1.00 104.64 ?  295  PHE C N   1 
ATOM   11341 C  CA  . PHE C 3  295  ? -72.331 0.928    59.016  1.00 107.37 ?  295  PHE C CA  1 
ATOM   11342 C  C   . PHE C 3  295  ? -71.636 2.124    58.375  1.00 105.43 ?  295  PHE C C   1 
ATOM   11343 O  O   . PHE C 3  295  ? -70.410 2.243    58.462  1.00 104.34 ?  295  PHE C O   1 
ATOM   11344 C  CB  . PHE C 3  295  ? -71.499 -0.339   58.813  1.00 104.75 ?  295  PHE C CB  1 
ATOM   11345 C  CG  . PHE C 3  295  ? -71.954 -1.504   59.648  1.00 106.78 ?  295  PHE C CG  1 
ATOM   11346 C  CD1 . PHE C 3  295  ? -72.725 -1.303   60.781  1.00 110.11 ?  295  PHE C CD1 1 
ATOM   11347 C  CD2 . PHE C 3  295  ? -71.616 -2.799   59.295  1.00 100.64 ?  295  PHE C CD2 1 
ATOM   11348 C  CE1 . PHE C 3  295  ? -73.147 -2.372   61.549  1.00 108.53 ?  295  PHE C CE1 1 
ATOM   11349 C  CE2 . PHE C 3  295  ? -72.034 -3.873   60.060  1.00 105.49 ?  295  PHE C CE2 1 
ATOM   11350 C  CZ  . PHE C 3  295  ? -72.801 -3.658   61.187  1.00 110.71 ?  295  PHE C CZ  1 
ATOM   11351 N  N   . GLU C 3  296  ? -72.396 3.013    57.731  1.00 117.85 ?  296  GLU C N   1 
ATOM   11352 C  CA  . GLU C 3  296  ? -71.802 4.203    57.133  1.00 119.66 ?  296  GLU C CA  1 
ATOM   11353 C  C   . GLU C 3  296  ? -71.243 5.156    58.180  1.00 129.88 ?  296  GLU C C   1 
ATOM   11354 O  O   . GLU C 3  296  ? -70.410 6.005    57.847  1.00 137.13 ?  296  GLU C O   1 
ATOM   11355 C  CB  . GLU C 3  296  ? -72.834 4.925    56.267  1.00 122.18 ?  296  GLU C CB  1 
ATOM   11356 C  CG  . GLU C 3  296  ? -72.944 4.377    54.855  1.00 133.18 ?  296  GLU C CG  1 
ATOM   11357 C  CD  . GLU C 3  296  ? -74.141 3.464    54.676  1.00 138.71 ?  296  GLU C CD  1 
ATOM   11358 O  OE1 . GLU C 3  296  ? -74.675 2.976    55.694  1.00 134.72 ?  296  GLU C OE1 1 
ATOM   11359 O  OE2 . GLU C 3  296  ? -74.547 3.235    53.516  1.00 139.20 -1 296  GLU C OE2 1 
ATOM   11360 N  N   . ASN C 3  297  ? -71.682 5.035    59.434  1.00 120.43 ?  297  ASN C N   1 
ATOM   11361 C  CA  . ASN C 3  297  ? -71.157 5.867    60.508  1.00 120.17 ?  297  ASN C CA  1 
ATOM   11362 C  C   . ASN C 3  297  ? -69.816 5.372    61.031  1.00 121.23 ?  297  ASN C C   1 
ATOM   11363 O  O   . ASN C 3  297  ? -69.074 6.155    61.634  1.00 116.42 ?  297  ASN C O   1 
ATOM   11364 C  CB  . ASN C 3  297  ? -72.163 5.929    61.660  1.00 127.91 ?  297  ASN C CB  1 
ATOM   11365 C  CG  . ASN C 3  297  ? -73.489 6.533    61.244  1.00 130.04 ?  297  ASN C CG  1 
ATOM   11366 O  OD1 . ASN C 3  297  ? -73.589 7.183    60.203  1.00 128.19 ?  297  ASN C OD1 1 
ATOM   11367 N  ND2 . ASN C 3  297  ? -74.517 6.321    62.057  1.00 125.65 ?  297  ASN C ND2 1 
ATOM   11368 N  N   . TYR C 3  298  ? -69.491 4.097    60.817  1.00 108.88 ?  298  TYR C N   1 
ATOM   11369 C  CA  . TYR C 3  298  ? -68.250 3.503    61.302  1.00 101.81 ?  298  TYR C CA  1 
ATOM   11370 C  C   . TYR C 3  298  ? -67.190 3.396    60.213  1.00 103.70 ?  298  TYR C C   1 
ATOM   11371 O  O   . TYR C 3  298  ? -66.026 3.737    60.446  1.00 104.58 ?  298  TYR C O   1 
ATOM   11372 C  CB  . TYR C 3  298  ? -68.531 2.119    61.899  1.00 87.55  ?  298  TYR C CB  1 
ATOM   11373 C  CG  . TYR C 3  298  ? -69.643 2.113    62.924  1.00 93.37  ?  298  TYR C CG  1 
ATOM   11374 C  CD1 . TYR C 3  298  ? -69.757 3.134    63.860  1.00 98.67  ?  298  TYR C CD1 1 
ATOM   11375 C  CD2 . TYR C 3  298  ? -70.581 1.090    62.954  1.00 100.01 ?  298  TYR C CD2 1 
ATOM   11376 C  CE1 . TYR C 3  298  ? -70.771 3.135    64.798  1.00 100.34 ?  298  TYR C CE1 1 
ATOM   11377 C  CE2 . TYR C 3  298  ? -71.600 1.082    63.889  1.00 106.20 ?  298  TYR C CE2 1 
ATOM   11378 C  CZ  . TYR C 3  298  ? -71.690 2.108    64.808  1.00 100.28 ?  298  TYR C CZ  1 
ATOM   11379 O  OH  . TYR C 3  298  ? -72.702 2.106    65.741  1.00 99.26  ?  298  TYR C OH  1 
ATOM   11380 N  N   . ILE C 3  299  ? -67.566 2.924    59.030  1.00 103.44 ?  299  ILE C N   1 
ATOM   11381 C  CA  . ILE C 3  299  ? -66.655 2.841    57.890  1.00 99.29  ?  299  ILE C CA  1 
ATOM   11382 C  C   . ILE C 3  299  ? -66.990 4.033    56.998  1.00 102.83 ?  299  ILE C C   1 
ATOM   11383 O  O   . ILE C 3  299  ? -67.892 3.981    56.161  1.00 105.59 ?  299  ILE C O   1 
ATOM   11384 C  CB  . ILE C 3  299  ? -66.778 1.509    57.153  1.00 95.68  ?  299  ILE C CB  1 
ATOM   11385 C  CG1 . ILE C 3  299  ? -66.939 0.358    58.149  1.00 93.13  ?  299  ILE C CG1 1 
ATOM   11386 C  CG2 . ILE C 3  299  ? -65.565 1.279    56.264  1.00 96.70  ?  299  ILE C CG2 1 
ATOM   11387 C  CD1 . ILE C 3  299  ? -67.226 -0.981   57.499  1.00 74.73  ?  299  ILE C CD1 1 
ATOM   11388 N  N   . THR C 3  300  ? -66.252 5.123    57.183  1.00 112.64 ?  300  THR C N   1 
ATOM   11389 C  CA  . THR C 3  300  ? -66.520 6.367    56.478  1.00 119.67 ?  300  THR C CA  1 
ATOM   11390 C  C   . THR C 3  300  ? -65.771 6.386    55.146  1.00 112.15 ?  300  THR C C   1 
ATOM   11391 O  O   . THR C 3  300  ? -65.137 5.406    54.746  1.00 115.36 ?  300  THR C O   1 
ATOM   11392 C  CB  . THR C 3  300  ? -66.141 7.561    57.350  1.00 117.95 ?  300  THR C CB  1 
ATOM   11393 O  OG1 . THR C 3  300  ? -64.715 7.699    57.381  1.00 114.70 ?  300  THR C OG1 1 
ATOM   11394 C  CG2 . THR C 3  300  ? -66.655 7.365    58.767  1.00 119.01 ?  300  THR C CG2 1 
ATOM   11395 N  N   . LEU C 3  301  ? -65.841 7.517    54.440  1.00 101.79 ?  301  LEU C N   1 
ATOM   11396 C  CA  . LEU C 3  301  ? -65.131 7.655    53.175  1.00 105.28 ?  301  LEU C CA  1 
ATOM   11397 C  C   . LEU C 3  301  ? -63.637 7.868    53.381  1.00 106.35 ?  301  LEU C C   1 
ATOM   11398 O  O   . LEU C 3  301  ? -62.842 7.530    52.497  1.00 103.26 ?  301  LEU C O   1 
ATOM   11399 C  CB  . LEU C 3  301  ? -65.720 8.810    52.363  1.00 109.39 ?  301  LEU C CB  1 
ATOM   11400 C  CG  . LEU C 3  301  ? -67.102 8.571    51.752  1.00 106.15 ?  301  LEU C CG  1 
ATOM   11401 C  CD1 . LEU C 3  301  ? -67.581 9.804    51.003  1.00 97.60  ?  301  LEU C CD1 1 
ATOM   11402 C  CD2 . LEU C 3  301  ? -67.078 7.359    50.833  1.00 103.87 ?  301  LEU C CD2 1 
ATOM   11403 N  N   . HIS C 3  302  ? -63.238 8.426    54.527  1.00 133.02 ?  302  HIS C N   1 
ATOM   11404 C  CA  . HIS C 3  302  ? -61.816 8.588    54.808  1.00 129.32 ?  302  HIS C CA  1 
ATOM   11405 C  C   . HIS C 3  302  ? -61.129 7.242    54.995  1.00 128.77 ?  302  HIS C C   1 
ATOM   11406 O  O   . HIS C 3  302  ? -59.924 7.123    54.743  1.00 129.03 ?  302  HIS C O   1 
ATOM   11407 C  CB  . HIS C 3  302  ? -61.615 9.466    56.044  1.00 127.45 ?  302  HIS C CB  1 
ATOM   11408 C  CG  . HIS C 3  302  ? -60.224 10.003   56.184  1.00 123.92 ?  302  HIS C CG  1 
ATOM   11409 N  ND1 . HIS C 3  302  ? -59.765 10.587   57.345  1.00 128.07 ?  302  HIS C ND1 1 
ATOM   11410 C  CD2 . HIS C 3  302  ? -59.192 10.047   55.307  1.00 115.33 ?  302  HIS C CD2 1 
ATOM   11411 C  CE1 . HIS C 3  302  ? -58.510 10.966   57.179  1.00 118.94 ?  302  HIS C CE1 1 
ATOM   11412 N  NE2 . HIS C 3  302  ? -58.139 10.649   55.951  1.00 109.18 ?  302  HIS C NE2 1 
ATOM   11413 N  N   . HIS C 3  303  ? -61.871 6.225    55.439  1.00 116.86 ?  303  HIS C N   1 
ATOM   11414 C  CA  . HIS C 3  303  ? -61.323 4.873    55.482  1.00 116.83 ?  303  HIS C CA  1 
ATOM   11415 C  C   . HIS C 3  303  ? -60.933 4.404    54.086  1.00 112.39 ?  303  HIS C C   1 
ATOM   11416 O  O   . HIS C 3  303  ? -59.799 3.969    53.859  1.00 112.16 ?  303  HIS C O   1 
ATOM   11417 C  CB  . HIS C 3  303  ? -62.335 3.913    56.108  1.00 118.96 ?  303  HIS C CB  1 
ATOM   11418 C  CG  . HIS C 3  303  ? -62.406 3.998    57.601  1.00 113.74 ?  303  HIS C CG  1 
ATOM   11419 N  ND1 . HIS C 3  303  ? -63.076 5.008    58.258  1.00 119.43 ?  303  HIS C ND1 1 
ATOM   11420 C  CD2 . HIS C 3  303  ? -61.896 3.195    58.564  1.00 107.19 ?  303  HIS C CD2 1 
ATOM   11421 C  CE1 . HIS C 3  303  ? -62.972 4.825    59.563  1.00 123.25 ?  303  HIS C CE1 1 
ATOM   11422 N  NE2 . HIS C 3  303  ? -62.261 3.732    59.775  1.00 115.64 ?  303  HIS C NE2 1 
ATOM   11423 N  N   . LEU C 3  304  ? -61.863 4.500    53.133  1.00 89.42  ?  304  LEU C N   1 
ATOM   11424 C  CA  . LEU C 3  304  ? -61.567 4.102    51.761  1.00 84.12  ?  304  LEU C CA  1 
ATOM   11425 C  C   . LEU C 3  304  ? -60.449 4.946    51.161  1.00 85.87  ?  304  LEU C C   1 
ATOM   11426 O  O   . LEU C 3  304  ? -59.673 4.451    50.336  1.00 91.26  ?  304  LEU C O   1 
ATOM   11427 C  CB  . LEU C 3  304  ? -62.828 4.209    50.904  1.00 81.50  ?  304  LEU C CB  1 
ATOM   11428 C  CG  . LEU C 3  304  ? -64.117 3.664    51.522  1.00 78.83  ?  304  LEU C CG  1 
ATOM   11429 C  CD1 . LEU C 3  304  ? -65.301 3.912    50.599  1.00 78.20  ?  304  LEU C CD1 1 
ATOM   11430 C  CD2 . LEU C 3  304  ? -63.981 2.183    51.841  1.00 80.98  ?  304  LEU C CD2 1 
ATOM   11431 N  N   . ASP C 3  305  ? -60.350 6.214    51.564  1.00 117.29 ?  305  ASP C N   1 
ATOM   11432 C  CA  . ASP C 3  305  ? -59.308 7.087    51.032  1.00 121.62 ?  305  ASP C CA  1 
ATOM   11433 C  C   . ASP C 3  305  ? -57.922 6.621    51.461  1.00 120.37 ?  305  ASP C C   1 
ATOM   11434 O  O   . ASP C 3  305  ? -57.024 6.461    50.626  1.00 118.50 ?  305  ASP C O   1 
ATOM   11435 C  CB  . ASP C 3  305  ? -59.555 8.528    51.479  1.00 123.41 ?  305  ASP C CB  1 
ATOM   11436 C  CG  . ASP C 3  305  ? -58.528 9.495    50.926  1.00 123.12 ?  305  ASP C CG  1 
ATOM   11437 O  OD1 . ASP C 3  305  ? -58.661 9.900    49.752  1.00 130.97 ?  305  ASP C OD1 1 
ATOM   11438 O  OD2 . ASP C 3  305  ? -57.590 9.854    51.669  1.00 119.49 -1 305  ASP C OD2 1 
ATOM   11439 N  N   . VAL C 3  306  ? -57.727 6.398    52.764  1.00 146.52 ?  306  VAL C N   1 
ATOM   11440 C  CA  . VAL C 3  306  ? -56.410 6.001    53.254  1.00 143.30 ?  306  VAL C CA  1 
ATOM   11441 C  C   . VAL C 3  306  ? -56.069 4.582    52.813  1.00 141.98 ?  306  VAL C C   1 
ATOM   11442 O  O   . VAL C 3  306  ? -54.896 4.264    52.580  1.00 143.84 ?  306  VAL C O   1 
ATOM   11443 C  CB  . VAL C 3  306  ? -56.337 6.163    54.786  1.00 139.98 ?  306  VAL C CB  1 
ATOM   11444 C  CG1 . VAL C 3  306  ? -57.304 5.217    55.485  1.00 132.76 ?  306  VAL C CG1 1 
ATOM   11445 C  CG2 . VAL C 3  306  ? -54.913 5.948    55.284  1.00 133.96 ?  306  VAL C CG2 1 
ATOM   11446 N  N   . MET C 3  307  ? -57.072 3.711    52.677  1.00 114.75 ?  307  MET C N   1 
ATOM   11447 C  CA  . MET C 3  307  ? -56.810 2.354    52.205  1.00 106.78 ?  307  MET C CA  1 
ATOM   11448 C  C   . MET C 3  307  ? -56.359 2.354    50.751  1.00 101.27 ?  307  MET C C   1 
ATOM   11449 O  O   . MET C 3  307  ? -55.450 1.603    50.377  1.00 101.73 ?  307  MET C O   1 
ATOM   11450 C  CB  . MET C 3  307  ? -58.055 1.487    52.384  1.00 110.75 ?  307  MET C CB  1 
ATOM   11451 C  CG  . MET C 3  307  ? -58.422 1.230    53.835  1.00 117.64 ?  307  MET C CG  1 
ATOM   11452 S  SD  . MET C 3  307  ? -59.992 0.364    53.999  1.00 118.83 ?  307  MET C SD  1 
ATOM   11453 C  CE  . MET C 3  307  ? -59.527 -1.258   53.409  1.00 119.08 ?  307  MET C CE  1 
ATOM   11454 N  N   . ALA C 3  308  ? -56.980 3.189    49.915  1.00 82.81  ?  308  ALA C N   1 
ATOM   11455 C  CA  . ALA C 3  308  ? -56.538 3.303    48.530  1.00 83.74  ?  308  ALA C CA  1 
ATOM   11456 C  C   . ALA C 3  308  ? -55.157 3.938    48.436  1.00 82.80  ?  308  ALA C C   1 
ATOM   11457 O  O   . ALA C 3  308  ? -54.395 3.625    47.514  1.00 80.70  ?  308  ALA C O   1 
ATOM   11458 C  CB  . ALA C 3  308  ? -57.553 4.108    47.718  1.00 86.72  ?  308  ALA C CB  1 
ATOM   11459 N  N   . LYS C 3  309  ? -54.818 4.826    49.374  1.00 99.42  ?  309  LYS C N   1 
ATOM   11460 C  CA  . LYS C 3  309  ? -53.479 5.408    49.387  1.00 99.45  ?  309  LYS C CA  1 
ATOM   11461 C  C   . LYS C 3  309  ? -52.427 4.356    49.717  1.00 94.48  ?  309  LYS C C   1 
ATOM   11462 O  O   . LYS C 3  309  ? -51.361 4.321    49.092  1.00 98.50  ?  309  LYS C O   1 
ATOM   11463 C  CB  . LYS C 3  309  ? -53.415 6.564    50.385  1.00 95.36  ?  309  LYS C CB  1 
ATOM   11464 C  CG  . LYS C 3  309  ? -53.644 7.933    49.764  1.00 101.32 ?  309  LYS C CG  1 
ATOM   11465 C  CD  . LYS C 3  309  ? -53.252 9.048    50.721  1.00 104.19 ?  309  LYS C CD  1 
ATOM   11466 C  CE  . LYS C 3  309  ? -54.233 9.159    51.875  1.00 104.25 ?  309  LYS C CE  1 
ATOM   11467 N  NZ  . LYS C 3  309  ? -54.013 10.400   52.667  1.00 103.08 ?  309  LYS C NZ  1 
ATOM   11468 N  N   . VAL C 3  310  ? -52.708 3.494    50.697  1.00 72.02  ?  310  VAL C N   1 
ATOM   11469 C  CA  . VAL C 3  310  ? -51.788 2.406    51.015  1.00 71.51  ?  310  VAL C CA  1 
ATOM   11470 C  C   . VAL C 3  310  ? -51.688 1.440    49.842  1.00 73.49  ?  310  VAL C C   1 
ATOM   11471 O  O   . VAL C 3  310  ? -50.601 0.954    49.507  1.00 69.95  ?  310  VAL C O   1 
ATOM   11472 C  CB  . VAL C 3  310  ? -52.230 1.689    52.306  1.00 72.75  ?  310  VAL C CB  1 
ATOM   11473 C  CG1 . VAL C 3  310  ? -51.319 0.510    52.603  1.00 64.68  ?  310  VAL C CG1 1 
ATOM   11474 C  CG2 . VAL C 3  310  ? -52.239 2.660    53.475  1.00 75.44  ?  310  VAL C CG2 1 
ATOM   11475 N  N   . MET C 3  311  ? -52.819 1.158    49.189  1.00 96.70  ?  311  MET C N   1 
ATOM   11476 C  CA  . MET C 3  311  ? -52.805 0.257    48.042  1.00 85.47  ?  311  MET C CA  1 
ATOM   11477 C  C   . MET C 3  311  ? -52.003 0.848    46.889  1.00 82.79  ?  311  MET C C   1 
ATOM   11478 O  O   . MET C 3  311  ? -51.293 0.124    46.182  1.00 87.81  ?  311  MET C O   1 
ATOM   11479 C  CB  . MET C 3  311  ? -54.238 -0.057   47.608  1.00 85.33  ?  311  MET C CB  1 
ATOM   11480 C  CG  . MET C 3  311  ? -54.342 -1.069   46.479  1.00 99.73  ?  311  MET C CG  1 
ATOM   11481 S  SD  . MET C 3  311  ? -56.034 -1.594   46.133  1.00 109.66 ?  311  MET C SD  1 
ATOM   11482 C  CE  . MET C 3  311  ? -56.645 -0.202   45.187  1.00 96.04  ?  311  MET C CE  1 
ATOM   11483 N  N   . LEU C 3  312  ? -52.093 2.166    46.691  1.00 76.57  ?  312  LEU C N   1 
ATOM   11484 C  CA  . LEU C 3  312  ? -51.312 2.807    45.637  1.00 80.97  ?  312  LEU C CA  1 
ATOM   11485 C  C   . LEU C 3  312  ? -49.821 2.758    45.948  1.00 83.27  ?  312  LEU C C   1 
ATOM   11486 O  O   . LEU C 3  312  ? -48.999 2.548    45.047  1.00 77.15  ?  312  LEU C O   1 
ATOM   11487 C  CB  . LEU C 3  312  ? -51.776 4.251    45.442  1.00 82.06  ?  312  LEU C CB  1 
ATOM   11488 C  CG  . LEU C 3  312  ? -50.805 5.194    44.728  1.00 88.14  ?  312  LEU C CG  1 
ATOM   11489 C  CD1 . LEU C 3  312  ? -50.774 4.902    43.235  1.00 82.99  ?  312  LEU C CD1 1 
ATOM   11490 C  CD2 . LEU C 3  312  ? -51.170 6.647    44.985  1.00 87.75  ?  312  LEU C CD2 1 
ATOM   11491 N  N   . THR C 3  313  ? -49.453 2.949    47.218  1.00 72.97  ?  313  THR C N   1 
ATOM   11492 C  CA  . THR C 3  313  ? -48.046 2.890    47.600  1.00 70.08  ?  313  THR C CA  1 
ATOM   11493 C  C   . THR C 3  313  ? -47.470 1.498    47.373  1.00 75.86  ?  313  THR C C   1 
ATOM   11494 O  O   . THR C 3  313  ? -46.366 1.354    46.834  1.00 78.21  ?  313  THR C O   1 
ATOM   11495 C  CB  . THR C 3  313  ? -47.882 3.307    49.062  1.00 60.57  ?  313  THR C CB  1 
ATOM   11496 O  OG1 . THR C 3  313  ? -48.214 4.693    49.204  1.00 64.66  ?  313  THR C OG1 1 
ATOM   11497 C  CG2 . THR C 3  313  ? -46.452 3.081    49.530  1.00 51.00  ?  313  THR C CG2 1 
ATOM   11498 N  N   . THR C 3  314  ? -48.207 0.459    47.771  1.00 103.01 ?  314  THR C N   1 
ATOM   11499 C  CA  . THR C 3  314  ? -47.728 -0.904   47.565  1.00 104.25 ?  314  THR C CA  1 
ATOM   11500 C  C   . THR C 3  314  ? -47.667 -1.250   46.082  1.00 105.41 ?  314  THR C C   1 
ATOM   11501 O  O   . THR C 3  314  ? -46.758 -1.964   45.643  1.00 99.84  ?  314  THR C O   1 
ATOM   11502 C  CB  . THR C 3  314  ? -48.619 -1.892   48.316  1.00 95.53  ?  314  THR C CB  1 
ATOM   11503 O  OG1 . THR C 3  314  ? -49.953 -1.827   47.798  1.00 106.68 ?  314  THR C OG1 1 
ATOM   11504 C  CG2 . THR C 3  314  ? -48.643 -1.552   49.795  1.00 87.07  ?  314  THR C CG2 1 
ATOM   11505 N  N   . GLY C 3  315  ? -48.623 -0.751   45.293  1.00 82.69  ?  315  GLY C N   1 
ATOM   11506 C  CA  . GLY C 3  315  ? -48.560 -0.951   43.856  1.00 82.88  ?  315  GLY C CA  1 
ATOM   11507 C  C   . GLY C 3  315  ? -47.371 -0.262   43.218  1.00 79.42  ?  315  GLY C C   1 
ATOM   11508 O  O   . GLY C 3  315  ? -46.795 -0.774   42.254  1.00 77.90  ?  315  GLY C O   1 
ATOM   11509 N  N   . MET C 3  316  ? -46.987 0.905    43.743  1.00 81.24  ?  316  MET C N   1 
ATOM   11510 C  CA  . MET C 3  316  ? -45.796 1.585    43.248  1.00 84.66  ?  316  MET C CA  1 
ATOM   11511 C  C   . MET C 3  316  ? -44.527 0.825    43.612  1.00 80.23  ?  316  MET C C   1 
ATOM   11512 O  O   . MET C 3  316  ? -43.563 0.826    42.839  1.00 77.36  ?  316  MET C O   1 
ATOM   11513 C  CB  . MET C 3  316  ? -45.738 3.012    43.794  1.00 92.49  ?  316  MET C CB  1 
ATOM   11514 C  CG  . MET C 3  316  ? -46.606 4.003    43.037  1.00 86.27  ?  316  MET C CG  1 
ATOM   11515 S  SD  . MET C 3  316  ? -46.661 3.665    41.267  1.00 93.19  ?  316  MET C SD  1 
ATOM   11516 C  CE  . MET C 3  316  ? -45.145 4.453    40.728  1.00 76.18  ?  316  MET C CE  1 
ATOM   11517 N  N   . ILE C 3  317  ? -44.505 0.175    44.779  1.00 75.93  ?  317  ILE C N   1 
ATOM   11518 C  CA  . ILE C 3  317  ? -43.367 -0.667   45.131  1.00 77.34  ?  317  ILE C CA  1 
ATOM   11519 C  C   . ILE C 3  317  ? -43.300 -1.875   44.206  1.00 77.25  ?  317  ILE C C   1 
ATOM   11520 O  O   . ILE C 3  317  ? -42.207 -2.345   43.860  1.00 71.15  ?  317  ILE C O   1 
ATOM   11521 C  CB  . ILE C 3  317  ? -43.450 -1.088   46.610  1.00 74.80  ?  317  ILE C CB  1 
ATOM   11522 C  CG1 . ILE C 3  317  ? -43.464 0.142    47.516  1.00 76.07  ?  317  ILE C CG1 1 
ATOM   11523 C  CG2 . ILE C 3  317  ? -42.275 -1.974   46.979  1.00 74.23  ?  317  ILE C CG2 1 
ATOM   11524 C  CD1 . ILE C 3  317  ? -43.546 -0.188   48.987  1.00 75.72  ?  317  ILE C CD1 1 
ATOM   11525 N  N   . VAL C 3  318  ? -44.456 -2.391   43.783  1.00 77.92  ?  318  VAL C N   1 
ATOM   11526 C  CA  . VAL C 3  318  ? -44.476 -3.503   42.839  1.00 78.77  ?  318  VAL C CA  1 
ATOM   11527 C  C   . VAL C 3  318  ? -43.948 -3.059   41.481  1.00 82.80  ?  318  VAL C C   1 
ATOM   11528 O  O   . VAL C 3  318  ? -43.172 -3.775   40.837  1.00 87.54  ?  318  VAL C O   1 
ATOM   11529 C  CB  . VAL C 3  318  ? -45.897 -4.088   42.733  1.00 80.02  ?  318  VAL C CB  1 
ATOM   11530 C  CG1 . VAL C 3  318  ? -45.980 -5.102   41.602  1.00 89.21  ?  318  VAL C CG1 1 
ATOM   11531 C  CG2 . VAL C 3  318  ? -46.304 -4.730   44.049  1.00 78.45  ?  318  VAL C CG2 1 
ATOM   11532 N  N   . VAL C 3  319  ? -44.361 -1.874   41.022  1.00 83.82  ?  319  VAL C N   1 
ATOM   11533 C  CA  . VAL C 3  319  ? -43.828 -1.329   39.776  1.00 81.49  ?  319  VAL C CA  1 
ATOM   11534 C  C   . VAL C 3  319  ? -42.324 -1.117   39.893  1.00 83.37  ?  319  VAL C C   1 
ATOM   11535 O  O   . VAL C 3  319  ? -41.572 -1.342   38.936  1.00 82.07  ?  319  VAL C O   1 
ATOM   11536 C  CB  . VAL C 3  319  ? -44.563 -0.026   39.407  1.00 81.47  ?  319  VAL C CB  1 
ATOM   11537 C  CG1 . VAL C 3  319  ? -43.843 0.703    38.284  1.00 75.91  ?  319  VAL C CG1 1 
ATOM   11538 C  CG2 . VAL C 3  319  ? -46.000 -0.327   39.012  1.00 77.62  ?  319  VAL C CG2 1 
ATOM   11539 N  N   . TYR C 3  320  ? -41.861 -0.693   41.072  1.00 77.72  ?  320  TYR C N   1 
ATOM   11540 C  CA  . TYR C 3  320  ? -40.425 -0.600   41.314  1.00 78.35  ?  320  TYR C CA  1 
ATOM   11541 C  C   . TYR C 3  320  ? -39.761 -1.965   41.179  1.00 75.54  ?  320  TYR C C   1 
ATOM   11542 O  O   . TYR C 3  320  ? -38.620 -2.067   40.714  1.00 71.53  ?  320  TYR C O   1 
ATOM   11543 C  CB  . TYR C 3  320  ? -40.169 -0.002   42.699  1.00 73.44  ?  320  TYR C CB  1 
ATOM   11544 C  CG  . TYR C 3  320  ? -38.782 -0.256   43.249  1.00 70.49  ?  320  TYR C CG  1 
ATOM   11545 C  CD1 . TYR C 3  320  ? -37.689 0.470    42.794  1.00 77.33  ?  320  TYR C CD1 1 
ATOM   11546 C  CD2 . TYR C 3  320  ? -38.567 -1.218   44.228  1.00 61.34  ?  320  TYR C CD2 1 
ATOM   11547 C  CE1 . TYR C 3  320  ? -36.420 0.243    43.297  1.00 70.88  ?  320  TYR C CE1 1 
ATOM   11548 C  CE2 . TYR C 3  320  ? -37.303 -1.453   44.736  1.00 63.07  ?  320  TYR C CE2 1 
ATOM   11549 C  CZ  . TYR C 3  320  ? -36.234 -0.719   44.267  1.00 67.08  ?  320  TYR C CZ  1 
ATOM   11550 O  OH  . TYR C 3  320  ? -34.974 -0.950   44.770  1.00 72.87  ?  320  TYR C OH  1 
ATOM   11551 N  N   . GLY C 3  321  ? -40.466 -3.028   41.574  1.00 74.96  ?  321  GLY C N   1 
ATOM   11552 C  CA  . GLY C 3  321  ? -39.937 -4.367   41.381  1.00 75.87  ?  321  GLY C CA  1 
ATOM   11553 C  C   . GLY C 3  321  ? -39.907 -4.776   39.921  1.00 82.36  ?  321  GLY C C   1 
ATOM   11554 O  O   . GLY C 3  321  ? -38.985 -5.468   39.481  1.00 80.03  ?  321  GLY C O   1 
ATOM   11555 N  N   . TYR C 3  322  ? -40.919 -4.361   39.152  1.00 86.52  ?  322  TYR C N   1 
ATOM   11556 C  CA  . TYR C 3  322  ? -40.909 -4.604   37.713  1.00 76.29  ?  322  TYR C CA  1 
ATOM   11557 C  C   . TYR C 3  322  ? -39.700 -3.946   37.063  1.00 76.31  ?  322  TYR C C   1 
ATOM   11558 O  O   . TYR C 3  322  ? -39.015 -4.554   36.232  1.00 73.55  ?  322  TYR C O   1 
ATOM   11559 C  CB  . TYR C 3  322  ? -42.197 -4.079   37.076  1.00 73.09  ?  322  TYR C CB  1 
ATOM   11560 C  CG  . TYR C 3  322  ? -43.463 -4.788   37.500  1.00 73.71  ?  322  TYR C CG  1 
ATOM   11561 C  CD1 . TYR C 3  322  ? -43.488 -6.162   37.696  1.00 72.11  ?  322  TYR C CD1 1 
ATOM   11562 C  CD2 . TYR C 3  322  ? -44.642 -4.079   37.689  1.00 82.72  ?  322  TYR C CD2 1 
ATOM   11563 C  CE1 . TYR C 3  322  ? -44.652 -6.807   38.077  1.00 81.77  ?  322  TYR C CE1 1 
ATOM   11564 C  CE2 . TYR C 3  322  ? -45.807 -4.713   38.070  1.00 87.76  ?  322  TYR C CE2 1 
ATOM   11565 C  CZ  . TYR C 3  322  ? -45.808 -6.077   38.264  1.00 85.82  ?  322  TYR C CZ  1 
ATOM   11566 O  OH  . TYR C 3  322  ? -46.969 -6.710   38.645  1.00 79.30  ?  322  TYR C OH  1 
ATOM   11567 N  N   . PHE C 3  323  ? -39.424 -2.694   37.436  1.00 94.24  ?  323  PHE C N   1 
ATOM   11568 C  CA  . PHE C 3  323  ? -38.302 -1.969   36.851  1.00 94.97  ?  323  PHE C CA  1 
ATOM   11569 C  C   . PHE C 3  323  ? -36.976 -2.609   37.234  1.00 97.42  ?  323  PHE C C   1 
ATOM   11570 O  O   . PHE C 3  323  ? -36.048 -2.669   36.418  1.00 97.52  ?  323  PHE C O   1 
ATOM   11571 C  CB  . PHE C 3  323  ? -38.337 -0.507   37.296  1.00 96.09  ?  323  PHE C CB  1 
ATOM   11572 C  CG  . PHE C 3  323  ? -39.378 0.318    36.594  1.00 105.36 ?  323  PHE C CG  1 
ATOM   11573 C  CD1 . PHE C 3  323  ? -39.975 -0.136   35.429  1.00 110.03 ?  323  PHE C CD1 1 
ATOM   11574 C  CD2 . PHE C 3  323  ? -39.768 1.543    37.109  1.00 106.16 ?  323  PHE C CD2 1 
ATOM   11575 C  CE1 . PHE C 3  323  ? -40.936 0.622    34.786  1.00 108.02 ?  323  PHE C CE1 1 
ATOM   11576 C  CE2 . PHE C 3  323  ? -40.728 2.305    36.472  1.00 111.69 ?  323  PHE C CE2 1 
ATOM   11577 C  CZ  . PHE C 3  323  ? -41.313 1.844    35.309  1.00 120.33 ?  323  PHE C CZ  1 
ATOM   11578 N  N   . MET C 3  324  ? -36.867 -3.093   38.474  1.00 99.23  ?  324  MET C N   1 
ATOM   11579 C  CA  . MET C 3  324  ? -35.632 -3.736   38.910  1.00 98.09  ?  324  MET C CA  1 
ATOM   11580 C  C   . MET C 3  324  ? -35.391 -5.034   38.152  1.00 98.24  ?  324  MET C C   1 
ATOM   11581 O  O   . MET C 3  324  ? -34.244 -5.373   37.840  1.00 97.24  ?  324  MET C O   1 
ATOM   11582 C  CB  . MET C 3  324  ? -35.676 -3.990   40.416  1.00 94.50  ?  324  MET C CB  1 
ATOM   11583 C  CG  . MET C 3  324  ? -35.453 -2.746   41.260  1.00 96.80  ?  324  MET C CG  1 
ATOM   11584 S  SD  . MET C 3  324  ? -34.005 -1.802   40.748  1.00 115.53 ?  324  MET C SD  1 
ATOM   11585 C  CE  . MET C 3  324  ? -34.775 -0.348   40.036  1.00 110.74 ?  324  MET C CE  1 
ATOM   11586 N  N   . GLU C 3  325  ? -36.461 -5.773   37.845  1.00 107.63 ?  325  GLU C N   1 
ATOM   11587 C  CA  . GLU C 3  325  ? -36.317 -6.978   37.037  1.00 108.61 ?  325  GLU C CA  1 
ATOM   11588 C  C   . GLU C 3  325  ? -35.894 -6.636   35.615  1.00 104.77 ?  325  GLU C C   1 
ATOM   11589 O  O   . GLU C 3  325  ? -35.041 -7.317   35.033  1.00 97.70  ?  325  GLU C O   1 
ATOM   11590 C  CB  . GLU C 3  325  ? -37.628 -7.764   37.027  1.00 107.59 ?  325  GLU C CB  1 
ATOM   11591 C  CG  . GLU C 3  325  ? -37.971 -8.433   38.347  1.00 107.47 ?  325  GLU C CG  1 
ATOM   11592 C  CD  . GLU C 3  325  ? -39.371 -9.014   38.352  1.00 124.36 ?  325  GLU C CD  1 
ATOM   11593 O  OE1 . GLU C 3  325  ? -40.006 -9.044   37.276  1.00 114.37 ?  325  GLU C OE1 1 
ATOM   11594 O  OE2 . GLU C 3  325  ? -39.839 -9.437   39.431  1.00 131.62 -1 325  GLU C OE2 1 
ATOM   11595 N  N   . VAL C 3  326  ? -36.480 -5.583   35.040  1.00 82.96  ?  326  VAL C N   1 
ATOM   11596 C  CA  . VAL C 3  326  ? -36.112 -5.166   33.690  1.00 77.85  ?  326  VAL C CA  1 
ATOM   11597 C  C   . VAL C 3  326  ? -34.679 -4.654   33.662  1.00 75.87  ?  326  VAL C C   1 
ATOM   11598 O  O   . VAL C 3  326  ? -33.913 -4.962   32.740  1.00 77.59  ?  326  VAL C O   1 
ATOM   11599 C  CB  . VAL C 3  326  ? -37.102 -4.108   33.171  1.00 68.94  ?  326  VAL C CB  1 
ATOM   11600 C  CG1 . VAL C 3  326  ? -36.609 -3.512   31.860  1.00 46.73  ?  326  VAL C CG1 1 
ATOM   11601 C  CG2 . VAL C 3  326  ? -38.486 -4.715   32.999  1.00 70.54  ?  326  VAL C CG2 1 
ATOM   11602 N  N   . PHE C 3  327  ? -34.291 -3.864   34.667  1.00 92.39  ?  327  PHE C N   1 
ATOM   11603 C  CA  . PHE C 3  327  ? -32.918 -3.376   34.727  1.00 94.87  ?  327  PHE C CA  1 
ATOM   11604 C  C   . PHE C 3  327  ? -31.937 -4.529   34.889  1.00 89.66  ?  327  PHE C C   1 
ATOM   11605 O  O   . PHE C 3  327  ? -30.841 -4.505   34.320  1.00 91.07  ?  327  PHE C O   1 
ATOM   11606 C  CB  . PHE C 3  327  ? -32.763 -2.371   35.870  1.00 93.98  ?  327  PHE C CB  1 
ATOM   11607 C  CG  . PHE C 3  327  ? -31.339 -1.962   36.135  1.00 91.57  ?  327  PHE C CG  1 
ATOM   11608 C  CD1 . PHE C 3  327  ? -30.750 -0.949   35.397  1.00 93.57  ?  327  PHE C CD1 1 
ATOM   11609 C  CD2 . PHE C 3  327  ? -30.592 -2.586   37.123  1.00 92.39  ?  327  PHE C CD2 1 
ATOM   11610 C  CE1 . PHE C 3  327  ? -29.444 -0.567   35.635  1.00 96.44  ?  327  PHE C CE1 1 
ATOM   11611 C  CE2 . PHE C 3  327  ? -29.282 -2.209   37.362  1.00 96.02  ?  327  PHE C CE2 1 
ATOM   11612 C  CZ  . PHE C 3  327  ? -28.710 -1.196   36.619  1.00 96.55  ?  327  PHE C CZ  1 
ATOM   11613 N  N   . ALA C 3  328  ? -32.319 -5.554   35.656  1.00 81.43  ?  328  ALA C N   1 
ATOM   11614 C  CA  . ALA C 3  328  ? -31.443 -6.706   35.841  1.00 86.51  ?  328  ALA C CA  1 
ATOM   11615 C  C   . ALA C 3  328  ? -31.279 -7.492   34.547  1.00 91.10  ?  328  ALA C C   1 
ATOM   11616 O  O   . ALA C 3  328  ? -30.183 -7.977   34.243  1.00 91.66  ?  328  ALA C O   1 
ATOM   11617 C  CB  . ALA C 3  328  ? -31.986 -7.608   36.949  1.00 79.18  ?  328  ALA C CB  1 
ATOM   11618 N  N   . SER C 3  329  ? -32.358 -7.632   33.772  1.00 108.89 ?  329  SER C N   1 
ATOM   11619 C  CA  . SER C 3  329  ? -32.267 -8.352   32.506  1.00 103.45 ?  329  SER C CA  1 
ATOM   11620 C  C   . SER C 3  329  ? -31.429 -7.590   31.487  1.00 100.97 ?  329  SER C C   1 
ATOM   11621 O  O   . SER C 3  329  ? -30.730 -8.206   30.676  1.00 101.11 ?  329  SER C O   1 
ATOM   11622 C  CB  . SER C 3  329  ? -33.667 -8.617   31.951  1.00 102.53 ?  329  SER C CB  1 
ATOM   11623 O  OG  . SER C 3  329  ? -34.375 -9.531   32.770  1.00 104.62 ?  329  SER C OG  1 
ATOM   11624 N  N   . LEU C 3  330  ? -31.481 -6.258   31.517  1.00 76.70  ?  330  LEU C N   1 
ATOM   11625 C  CA  . LEU C 3  330  ? -30.710 -5.448   30.583  1.00 72.01  ?  330  LEU C CA  1 
ATOM   11626 C  C   . LEU C 3  330  ? -29.275 -5.227   31.042  1.00 71.67  ?  330  LEU C C   1 
ATOM   11627 O  O   . LEU C 3  330  ? -28.399 -4.990   30.204  1.00 78.31  ?  330  LEU C O   1 
ATOM   11628 C  CB  . LEU C 3  330  ? -31.394 -4.094   30.376  1.00 70.83  ?  330  LEU C CB  1 
ATOM   11629 C  CG  . LEU C 3  330  ? -32.726 -4.094   29.622  1.00 63.80  ?  330  LEU C CG  1 
ATOM   11630 C  CD1 . LEU C 3  330  ? -33.315 -2.692   29.582  1.00 59.12  ?  330  LEU C CD1 1 
ATOM   11631 C  CD2 . LEU C 3  330  ? -32.555 -4.650   28.217  1.00 67.25  ?  330  LEU C CD2 1 
ATOM   11632 N  N   . TYR C 3  331  ? -29.018 -5.305   32.349  1.00 75.32  ?  331  TYR C N   1 
ATOM   11633 C  CA  . TYR C 3  331  ? -27.692 -5.006   32.879  1.00 73.38  ?  331  TYR C CA  1 
ATOM   11634 C  C   . TYR C 3  331  ? -26.736 -6.179   32.697  1.00 79.78  ?  331  TYR C C   1 
ATOM   11635 O  O   . TYR C 3  331  ? -25.554 -5.978   32.396  1.00 76.92  ?  331  TYR C O   1 
ATOM   11636 C  CB  . TYR C 3  331  ? -27.803 -4.632   34.357  1.00 76.36  ?  331  TYR C CB  1 
ATOM   11637 C  CG  . TYR C 3  331  ? -26.586 -3.963   34.949  1.00 77.36  ?  331  TYR C CG  1 
ATOM   11638 C  CD1 . TYR C 3  331  ? -26.319 -2.623   34.704  1.00 80.12  ?  331  TYR C CD1 1 
ATOM   11639 C  CD2 . TYR C 3  331  ? -25.714 -4.667   35.769  1.00 80.41  ?  331  TYR C CD2 1 
ATOM   11640 C  CE1 . TYR C 3  331  ? -25.214 -2.005   35.255  1.00 88.41  ?  331  TYR C CE1 1 
ATOM   11641 C  CE2 . TYR C 3  331  ? -24.605 -4.059   36.321  1.00 77.43  ?  331  TYR C CE2 1 
ATOM   11642 C  CZ  . TYR C 3  331  ? -24.359 -2.730   36.060  1.00 87.23  ?  331  TYR C CZ  1 
ATOM   11643 O  OH  . TYR C 3  331  ? -23.254 -2.123   36.609  1.00 89.86  ?  331  TYR C OH  1 
ATOM   11644 N  N   . SER C 3  332  ? -27.223 -7.403   32.874  1.00 96.92  ?  332  SER C N   1 
ATOM   11645 C  CA  . SER C 3  332  ? -26.374 -8.578   32.766  1.00 99.76  ?  332  SER C CA  1 
ATOM   11646 C  C   . SER C 3  332  ? -26.202 -8.993   31.310  1.00 107.56 ?  332  SER C C   1 
ATOM   11647 O  O   . SER C 3  332  ? -27.089 -8.800   30.474  1.00 105.32 ?  332  SER C O   1 
ATOM   11648 C  CB  . SER C 3  332  ? -26.958 -9.741   33.568  1.00 105.60 ?  332  SER C CB  1 
ATOM   11649 O  OG  . SER C 3  332  ? -28.249 -10.084  33.097  1.00 109.48 ?  332  SER C OG  1 
ATOM   11650 N  N   . GLY C 3  333  ? -25.042 -9.574   31.014  1.00 105.37 ?  333  GLY C N   1 
ATOM   11651 C  CA  . GLY C 3  333  ? -24.764 -10.063  29.679  1.00 105.93 ?  333  GLY C CA  1 
ATOM   11652 C  C   . GLY C 3  333  ? -25.101 -11.531  29.518  1.00 113.77 ?  333  GLY C C   1 
ATOM   11653 O  O   . GLY C 3  333  ? -24.617 -12.189  28.593  1.00 116.19 ?  333  GLY C O   1 
ATOM   11654 N  N   . ASN C 3  334  ? -25.933 -12.054  30.416  1.00 116.64 ?  334  ASN C N   1 
ATOM   11655 C  CA  . ASN C 3  334  ? -26.309 -13.460  30.376  1.00 113.08 ?  334  ASN C CA  1 
ATOM   11656 C  C   . ASN C 3  334  ? -27.363 -13.694  29.302  1.00 110.52 ?  334  ASN C C   1 
ATOM   11657 O  O   . ASN C 3  334  ? -28.338 -12.944  29.201  1.00 114.92 ?  334  ASN C O   1 
ATOM   11658 C  CB  . ASN C 3  334  ? -26.835 -13.913  31.738  1.00 109.12 ?  334  ASN C CB  1 
ATOM   11659 C  CG  . ASN C 3  334  ? -25.745 -13.982  32.789  1.00 129.86 ?  334  ASN C CG  1 
ATOM   11660 O  OD1 . ASN C 3  334  ? -24.630 -14.427  32.516  1.00 133.96 ?  334  ASN C OD1 1 
ATOM   11661 N  ND2 . ASN C 3  334  ? -26.065 -13.545  34.002  1.00 131.26 ?  334  ASN C ND2 1 
ATOM   11662 N  N   . GLU C 3  335  ? -27.161 -14.744  28.502  1.00 106.72 ?  335  GLU C N   1 
ATOM   11663 C  CA  . GLU C 3  335  ? -28.120 -15.086  27.456  1.00 99.18  ?  335  GLU C CA  1 
ATOM   11664 C  C   . GLU C 3  335  ? -29.481 -15.448  28.037  1.00 93.00  ?  335  GLU C C   1 
ATOM   11665 O  O   . GLU C 3  335  ? -30.511 -15.253  27.380  1.00 87.72  ?  335  GLU C O   1 
ATOM   11666 C  CB  . GLU C 3  335  ? -27.572 -16.243  26.615  1.00 86.46  ?  335  GLU C CB  1 
ATOM   11667 C  CG  . GLU C 3  335  ? -28.492 -16.733  25.504  1.00 91.04  ?  335  GLU C CG  1 
ATOM   11668 C  CD  . GLU C 3  335  ? -28.882 -15.636  24.535  1.00 105.72 ?  335  GLU C CD  1 
ATOM   11669 O  OE1 . GLU C 3  335  ? -27.983 -14.906  24.066  1.00 110.22 ?  335  GLU C OE1 1 
ATOM   11670 O  OE2 . GLU C 3  335  ? -30.090 -15.506  24.242  1.00 103.43 -1 335  GLU C OE2 1 
ATOM   11671 N  N   . PHE C 3  336  ? -29.510 -15.954  29.271  1.00 69.01  ?  336  PHE C N   1 
ATOM   11672 C  CA  . PHE C 3  336  ? -30.746 -16.486  29.833  1.00 62.80  ?  336  PHE C CA  1 
ATOM   11673 C  C   . PHE C 3  336  ? -31.622 -15.386  30.421  1.00 65.98  ?  336  PHE C C   1 
ATOM   11674 O  O   . PHE C 3  336  ? -32.854 -15.474  30.358  1.00 61.49  ?  336  PHE C O   1 
ATOM   11675 C  CB  . PHE C 3  336  ? -30.415 -17.542  30.886  1.00 51.32  ?  336  PHE C CB  1 
ATOM   11676 C  CG  . PHE C 3  336  ? -29.438 -18.577  30.407  1.00 46.49  ?  336  PHE C CG  1 
ATOM   11677 C  CD1 . PHE C 3  336  ? -29.869 -19.681  29.693  1.00 46.30  ?  336  PHE C CD1 1 
ATOM   11678 C  CD2 . PHE C 3  336  ? -28.083 -18.436  30.661  1.00 44.83  ?  336  PHE C CD2 1 
ATOM   11679 C  CE1 . PHE C 3  336  ? -28.967 -20.630  29.246  1.00 50.10  ?  336  PHE C CE1 1 
ATOM   11680 C  CE2 . PHE C 3  336  ? -27.178 -19.379  30.219  1.00 46.86  ?  336  PHE C CE2 1 
ATOM   11681 C  CZ  . PHE C 3  336  ? -27.620 -20.478  29.511  1.00 49.47  ?  336  PHE C CZ  1 
ATOM   11682 N  N   . GLU C 3  337  ? -31.013 -14.350  31.001  1.00 119.68 ?  337  GLU C N   1 
ATOM   11683 C  CA  . GLU C 3  337  ? -31.792 -13.193  31.432  1.00 120.14 ?  337  GLU C CA  1 
ATOM   11684 C  C   . GLU C 3  337  ? -32.359 -12.438  30.236  1.00 122.92 ?  337  GLU C C   1 
ATOM   11685 O  O   . GLU C 3  337  ? -33.495 -11.951  30.283  1.00 124.06 ?  337  GLU C O   1 
ATOM   11686 C  CB  . GLU C 3  337  ? -30.934 -12.265  32.293  1.00 122.16 ?  337  GLU C CB  1 
ATOM   11687 C  CG  . GLU C 3  337  ? -30.451 -12.878  33.598  1.00 129.18 ?  337  GLU C CG  1 
ATOM   11688 C  CD  . GLU C 3  337  ? -31.536 -12.911  34.659  1.00 125.37 ?  337  GLU C CD  1 
ATOM   11689 O  OE1 . GLU C 3  337  ? -32.514 -12.144  34.536  1.00 124.78 ?  337  GLU C OE1 1 
ATOM   11690 O  OE2 . GLU C 3  337  ? -31.408 -13.697  35.621  1.00 120.29 -1 337  GLU C OE2 1 
ATOM   11691 N  N   . GLU C 3  338  ? -31.581 -12.330  29.154  1.00 66.47  ?  338  GLU C N   1 
ATOM   11692 C  CA  . GLU C 3  338  ? -32.066 -11.657  27.954  1.00 57.24  ?  338  GLU C CA  1 
ATOM   11693 C  C   . GLU C 3  338  ? -33.219 -12.423  27.317  1.00 47.35  ?  338  GLU C C   1 
ATOM   11694 O  O   . GLU C 3  338  ? -34.222 -11.824  26.914  1.00 48.05  ?  338  GLU C O   1 
ATOM   11695 C  CB  . GLU C 3  338  ? -30.923 -11.477  26.955  1.00 63.31  ?  338  GLU C CB  1 
ATOM   11696 C  CG  . GLU C 3  338  ? -29.763 -10.648  27.479  1.00 65.64  ?  338  GLU C CG  1 
ATOM   11697 C  CD  . GLU C 3  338  ? -28.572 -10.652  26.541  1.00 79.24  ?  338  GLU C CD  1 
ATOM   11698 O  OE1 . GLU C 3  338  ? -28.775 -10.808  25.318  1.00 88.98  ?  338  GLU C OE1 1 
ATOM   11699 O  OE2 . GLU C 3  338  ? -27.433 -10.491  27.028  1.00 84.23  -1 338  GLU C OE2 1 
ATOM   11700 N  N   . TYR C 3  339  ? -33.098 -13.749  27.216  1.00 57.55  ?  339  TYR C N   1 
ATOM   11701 C  CA  . TYR C 3  339  ? -34.183 -14.527  26.630  1.00 55.71  ?  339  TYR C CA  1 
ATOM   11702 C  C   . TYR C 3  339  ? -35.407 -14.552  27.534  1.00 55.20  ?  339  TYR C C   1 
ATOM   11703 O  O   . TYR C 3  339  ? -36.536 -14.666  27.041  1.00 53.20  ?  339  TYR C O   1 
ATOM   11704 C  CB  . TYR C 3  339  ? -33.721 -15.951  26.325  1.00 52.99  ?  339  TYR C CB  1 
ATOM   11705 C  CG  . TYR C 3  339  ? -34.569 -16.622  25.273  1.00 49.85  ?  339  TYR C CG  1 
ATOM   11706 C  CD1 . TYR C 3  339  ? -34.354 -16.380  23.924  1.00 60.67  ?  339  TYR C CD1 1 
ATOM   11707 C  CD2 . TYR C 3  339  ? -35.603 -17.478  25.628  1.00 41.60  ?  339  TYR C CD2 1 
ATOM   11708 C  CE1 . TYR C 3  339  ? -35.132 -16.984  22.956  1.00 67.54  ?  339  TYR C CE1 1 
ATOM   11709 C  CE2 . TYR C 3  339  ? -36.388 -18.085  24.668  1.00 56.51  ?  339  TYR C CE2 1 
ATOM   11710 C  CZ  . TYR C 3  339  ? -36.148 -17.836  23.333  1.00 65.85  ?  339  TYR C CZ  1 
ATOM   11711 O  OH  . TYR C 3  339  ? -36.926 -18.439  22.371  1.00 63.22  ?  339  TYR C OH  1 
ATOM   11712 N  N   . LEU C 3  340  ? -35.209 -14.457  28.850  1.00 69.42  ?  340  LEU C N   1 
ATOM   11713 C  CA  . LEU C 3  340  ? -36.343 -14.338  29.761  1.00 73.81  ?  340  LEU C CA  1 
ATOM   11714 C  C   . LEU C 3  340  ? -37.148 -13.080  29.460  1.00 74.58  ?  340  LEU C C   1 
ATOM   11715 O  O   . LEU C 3  340  ? -38.382 -13.119  29.392  1.00 75.64  ?  340  LEU C O   1 
ATOM   11716 C  CB  . LEU C 3  340  ? -35.856 -14.332  31.209  1.00 68.16  ?  340  LEU C CB  1 
ATOM   11717 C  CG  . LEU C 3  340  ? -36.894 -13.876  32.235  1.00 60.29  ?  340  LEU C CG  1 
ATOM   11718 C  CD1 . LEU C 3  340  ? -37.876 -14.997  32.554  1.00 57.63  ?  340  LEU C CD1 1 
ATOM   11719 C  CD2 . LEU C 3  340  ? -36.216 -13.368  33.497  1.00 71.79  ?  340  LEU C CD2 1 
ATOM   11720 N  N   . LEU C 3  341  ? -36.461 -11.952  29.269  1.00 84.83  ?  341  LEU C N   1 
ATOM   11721 C  CA  . LEU C 3  341  ? -37.150 -10.714  28.921  1.00 80.55  ?  341  LEU C CA  1 
ATOM   11722 C  C   . LEU C 3  341  ? -37.810 -10.818  27.553  1.00 85.21  ?  341  LEU C C   1 
ATOM   11723 O  O   . LEU C 3  341  ? -38.920 -10.311  27.350  1.00 87.32  ?  341  LEU C O   1 
ATOM   11724 C  CB  . LEU C 3  341  ? -36.171 -9.541   28.956  1.00 85.55  ?  341  LEU C CB  1 
ATOM   11725 C  CG  . LEU C 3  341  ? -36.774 -8.141   28.827  1.00 88.68  ?  341  LEU C CG  1 
ATOM   11726 C  CD1 . LEU C 3  341  ? -37.895 -7.940   29.835  1.00 89.55  ?  341  LEU C CD1 1 
ATOM   11727 C  CD2 . LEU C 3  341  ? -35.699 -7.080   29.000  1.00 88.84  ?  341  LEU C CD2 1 
ATOM   11728 N  N   . TYR C 3  342  ? -37.142 -11.470  26.599  1.00 72.72  ?  342  TYR C N   1 
ATOM   11729 C  CA  . TYR C 3  342  ? -37.723 -11.622  25.269  1.00 70.68  ?  342  TYR C CA  1 
ATOM   11730 C  C   . TYR C 3  342  ? -38.923 -12.559  25.297  1.00 77.87  ?  342  TYR C C   1 
ATOM   11731 O  O   . TYR C 3  342  ? -39.925 -12.314  24.616  1.00 79.47  ?  342  TYR C O   1 
ATOM   11732 C  CB  . TYR C 3  342  ? -36.667 -12.126  24.286  1.00 75.25  ?  342  TYR C CB  1 
ATOM   11733 C  CG  . TYR C 3  342  ? -37.215 -12.438  22.911  1.00 78.15  ?  342  TYR C CG  1 
ATOM   11734 C  CD1 . TYR C 3  342  ? -37.490 -11.421  22.005  1.00 77.56  ?  342  TYR C CD1 1 
ATOM   11735 C  CD2 . TYR C 3  342  ? -37.454 -13.748  22.517  1.00 81.77  ?  342  TYR C CD2 1 
ATOM   11736 C  CE1 . TYR C 3  342  ? -37.993 -11.701  20.748  1.00 93.22  ?  342  TYR C CE1 1 
ATOM   11737 C  CE2 . TYR C 3  342  ? -37.955 -14.038  21.262  1.00 86.50  ?  342  TYR C CE2 1 
ATOM   11738 C  CZ  . TYR C 3  342  ? -38.223 -13.011  20.381  1.00 99.00  ?  342  TYR C CZ  1 
ATOM   11739 O  OH  . TYR C 3  342  ? -38.722 -13.294  19.130  1.00 109.23 ?  342  TYR C OH  1 
ATOM   11740 N  N   . ASN C 3  343  ? -38.842 -13.637  26.080  1.00 78.60  ?  343  ASN C N   1 
ATOM   11741 C  CA  . ASN C 3  343  ? -39.961 -14.567  26.161  1.00 79.64  ?  343  ASN C CA  1 
ATOM   11742 C  C   . ASN C 3  343  ? -41.140 -13.949  26.902  1.00 80.38  ?  343  ASN C C   1 
ATOM   11743 O  O   . ASN C 3  343  ? -42.288 -14.353  26.690  1.00 79.87  ?  343  ASN C O   1 
ATOM   11744 C  CB  . ASN C 3  343  ? -39.511 -15.866  26.833  1.00 72.13  ?  343  ASN C CB  1 
ATOM   11745 C  CG  . ASN C 3  343  ? -40.574 -16.949  26.792  1.00 73.99  ?  343  ASN C CG  1 
ATOM   11746 O  OD1 . ASN C 3  343  ? -41.440 -16.952  25.918  1.00 83.28  ?  343  ASN C OD1 1 
ATOM   11747 N  ND2 . ASN C 3  343  ? -40.508 -17.881  27.737  1.00 80.13  ?  343  ASN C ND2 1 
ATOM   11748 N  N   . ARG C 3  344  ? -40.878 -12.969  27.766  1.00 77.49  ?  344  ARG C N   1 
ATOM   11749 C  CA  . ARG C 3  344  ? -41.965 -12.277  28.443  1.00 76.98  ?  344  ARG C CA  1 
ATOM   11750 C  C   . ARG C 3  344  ? -42.611 -11.250  27.523  1.00 78.50  ?  344  ARG C C   1 
ATOM   11751 O  O   . ARG C 3  344  ? -43.829 -11.044  27.572  1.00 80.12  ?  344  ARG C O   1 
ATOM   11752 C  CB  . ARG C 3  344  ? -41.451 -11.602  29.716  1.00 70.49  ?  344  ARG C CB  1 
ATOM   11753 C  CG  . ARG C 3  344  ? -41.184 -12.555  30.873  1.00 67.58  ?  344  ARG C CG  1 
ATOM   11754 C  CD  . ARG C 3  344  ? -40.715 -11.803  32.117  1.00 75.32  ?  344  ARG C CD  1 
ATOM   11755 N  NE  . ARG C 3  344  ? -40.574 -12.679  33.276  1.00 71.81  ?  344  ARG C NE  1 
ATOM   11756 C  CZ  . ARG C 3  344  ? -40.138 -12.286  34.465  1.00 64.50  ?  344  ARG C CZ  1 
ATOM   11757 N  NH1 . ARG C 3  344  ? -39.781 -11.032  34.692  1.00 81.74  ?  344  ARG C NH1 1 
ATOM   11758 N  NH2 . ARG C 3  344  ? -40.060 -13.173  35.453  1.00 64.49  ?  344  ARG C NH2 1 
ATOM   11759 N  N   . LEU C 3  345  ? -41.816 -10.605  26.669  1.00 81.94  ?  345  LEU C N   1 
ATOM   11760 C  CA  . LEU C 3  345  ? -42.311 -9.499   25.859  1.00 88.94  ?  345  LEU C CA  1 
ATOM   11761 C  C   . LEU C 3  345  ? -42.960 -9.966   24.562  1.00 90.56  ?  345  LEU C C   1 
ATOM   11762 O  O   . LEU C 3  345  ? -44.021 -9.458   24.185  1.00 91.76  ?  345  LEU C O   1 
ATOM   11763 C  CB  . LEU C 3  345  ? -41.173 -8.523   25.554  1.00 92.01  ?  345  LEU C CB  1 
ATOM   11764 C  CG  . LEU C 3  345  ? -40.852 -7.492   26.636  1.00 87.18  ?  345  LEU C CG  1 
ATOM   11765 C  CD1 . LEU C 3  345  ? -39.545 -6.782   26.322  1.00 82.68  ?  345  LEU C CD1 1 
ATOM   11766 C  CD2 . LEU C 3  345  ? -41.991 -6.495   26.756  1.00 81.84  ?  345  LEU C CD2 1 
ATOM   11767 N  N   . PHE C 3  346  ? -42.346 -10.928  23.868  1.00 87.24  ?  346  PHE C N   1 
ATOM   11768 C  CA  . PHE C 3  346  ? -42.854 -11.384  22.579  1.00 84.45  ?  346  PHE C CA  1 
ATOM   11769 C  C   . PHE C 3  346  ? -42.971 -12.902  22.507  1.00 77.68  ?  346  PHE C C   1 
ATOM   11770 O  O   . PHE C 3  346  ? -43.082 -13.456  21.409  1.00 82.16  ?  346  PHE C O   1 
ATOM   11771 C  CB  . PHE C 3  346  ? -41.972 -10.877  21.433  1.00 87.77  ?  346  PHE C CB  1 
ATOM   11772 C  CG  . PHE C 3  346  ? -41.536 -9.448   21.588  1.00 91.51  ?  346  PHE C CG  1 
ATOM   11773 C  CD1 . PHE C 3  346  ? -42.430 -8.411   21.380  1.00 95.38  ?  346  PHE C CD1 1 
ATOM   11774 C  CD2 . PHE C 3  346  ? -40.231 -9.143   21.938  1.00 94.02  ?  346  PHE C CD2 1 
ATOM   11775 C  CE1 . PHE C 3  346  ? -42.030 -7.094   21.520  1.00 86.37  ?  346  PHE C CE1 1 
ATOM   11776 C  CE2 . PHE C 3  346  ? -39.826 -7.829   22.081  1.00 89.88  ?  346  PHE C CE2 1 
ATOM   11777 C  CZ  . PHE C 3  346  ? -40.726 -6.803   21.872  1.00 91.06  ?  346  PHE C CZ  1 
ATOM   11778 N  N   . GLY C 3  347  ? -42.953 -13.587  23.647  1.00 94.73  ?  347  GLY C N   1 
ATOM   11779 C  CA  . GLY C 3  347  ? -43.048 -15.026  23.653  1.00 103.89 ?  347  GLY C CA  1 
ATOM   11780 C  C   . GLY C 3  347  ? -44.464 -15.506  23.423  1.00 101.79 ?  347  GLY C C   1 
ATOM   11781 O  O   . GLY C 3  347  ? -45.406 -14.725  23.230  1.00 99.96  ?  347  GLY C O   1 
ATOM   11782 N  N   . PRO C 3  348  ? -44.629 -16.831  23.437  1.00 66.87  ?  348  PRO C N   1 
ATOM   11783 C  CA  . PRO C 3  348  ? -45.976 -17.401  23.279  1.00 61.15  ?  348  PRO C CA  1 
ATOM   11784 C  C   . PRO C 3  348  ? -46.908 -17.084  24.433  1.00 71.41  ?  348  PRO C C   1 
ATOM   11785 O  O   . PRO C 3  348  ? -48.125 -17.242  24.282  1.00 73.26  ?  348  PRO C O   1 
ATOM   11786 C  CB  . PRO C 3  348  ? -45.711 -18.909  23.175  1.00 54.64  ?  348  PRO C CB  1 
ATOM   11787 C  CG  . PRO C 3  348  ? -44.386 -19.107  23.839  1.00 67.49  ?  348  PRO C CG  1 
ATOM   11788 C  CD  . PRO C 3  348  ? -43.592 -17.871  23.545  1.00 59.66  ?  348  PRO C CD  1 
ATOM   11789 N  N   . SER C 3  349  ? -46.381 -16.646  25.577  1.00 93.37  ?  349  SER C N   1 
ATOM   11790 C  CA  . SER C 3  349  ? -47.190 -16.293  26.737  1.00 89.25  ?  349  SER C CA  1 
ATOM   11791 C  C   . SER C 3  349  ? -47.040 -14.817  27.091  1.00 85.38  ?  349  SER C C   1 
ATOM   11792 O  O   . SER C 3  349  ? -47.217 -14.427  28.246  1.00 86.10  ?  349  SER C O   1 
ATOM   11793 C  CB  . SER C 3  349  ? -46.828 -17.171  27.934  1.00 96.10  ?  349  SER C CB  1 
ATOM   11794 O  OG  . SER C 3  349  ? -47.131 -18.532  27.679  1.00 93.70  ?  349  SER C OG  1 
ATOM   11795 N  N   . SER C 3  350  ? -46.720 -13.981  26.100  1.00 106.23 ?  350  SER C N   1 
ATOM   11796 C  CA  . SER C 3  350  ? -46.537 -12.557  26.354  1.00 107.35 ?  350  SER C CA  1 
ATOM   11797 C  C   . SER C 3  350  ? -47.831 -11.867  26.765  1.00 106.10 ?  350  SER C C   1 
ATOM   11798 O  O   . SER C 3  350  ? -47.779 -10.755  27.301  1.00 110.76 ?  350  SER C O   1 
ATOM   11799 C  CB  . SER C 3  350  ? -45.960 -11.871  25.116  1.00 106.71 ?  350  SER C CB  1 
ATOM   11800 O  OG  . SER C 3  350  ? -46.831 -12.009  24.006  1.00 107.56 ?  350  SER C OG  1 
ATOM   11801 N  N   . TRP C 3  351  ? -48.982 -12.501  26.527  1.00 62.40  ?  351  TRP C N   1 
ATOM   11802 C  CA  . TRP C 3  351  ? -50.261 -11.887  26.873  1.00 62.06  ?  351  TRP C CA  1 
ATOM   11803 C  C   . TRP C 3  351  ? -50.366 -11.624  28.370  1.00 70.75  ?  351  TRP C C   1 
ATOM   11804 O  O   . TRP C 3  351  ? -50.959 -10.624  28.792  1.00 76.02  ?  351  TRP C O   1 
ATOM   11805 C  CB  . TRP C 3  351  ? -51.407 -12.783  26.404  1.00 63.65  ?  351  TRP C CB  1 
ATOM   11806 C  CG  . TRP C 3  351  ? -51.307 -14.179  26.932  1.00 64.16  ?  351  TRP C CG  1 
ATOM   11807 C  CD1 . TRP C 3  351  ? -50.677 -15.234  26.340  1.00 66.12  ?  351  TRP C CD1 1 
ATOM   11808 C  CD2 . TRP C 3  351  ? -51.851 -14.674  28.161  1.00 65.64  ?  351  TRP C CD2 1 
ATOM   11809 N  NE1 . TRP C 3  351  ? -50.794 -16.355  27.123  1.00 65.67  ?  351  TRP C NE1 1 
ATOM   11810 C  CE2 . TRP C 3  351  ? -51.511 -16.039  28.247  1.00 66.90  ?  351  TRP C CE2 1 
ATOM   11811 C  CE3 . TRP C 3  351  ? -52.594 -14.098  29.197  1.00 65.93  ?  351  TRP C CE3 1 
ATOM   11812 C  CZ2 . TRP C 3  351  ? -51.886 -16.836  29.326  1.00 63.94  ?  351  TRP C CZ2 1 
ATOM   11813 C  CZ3 . TRP C 3  351  ? -52.965 -14.891  30.268  1.00 64.74  ?  351  TRP C CZ3 1 
ATOM   11814 C  CH2 . TRP C 3  351  ? -52.611 -16.245  30.324  1.00 64.53  ?  351  TRP C CH2 1 
ATOM   11815 N  N   . ALA C 3  352  ? -49.795 -12.509  29.190  1.00 70.17  ?  352  ALA C N   1 
ATOM   11816 C  CA  . ALA C 3  352  ? -49.857 -12.315  30.635  1.00 63.69  ?  352  ALA C CA  1 
ATOM   11817 C  C   . ALA C 3  352  ? -48.959 -11.166  31.077  1.00 61.58  ?  352  ALA C C   1 
ATOM   11818 O  O   . ALA C 3  352  ? -49.293 -10.436  32.017  1.00 66.67  ?  352  ALA C O   1 
ATOM   11819 C  CB  . ALA C 3  352  ? -49.477 -13.609  31.354  1.00 60.13  ?  352  ALA C CB  1 
ATOM   11820 N  N   . TYR C 3  353  ? -47.816 -10.988  30.410  1.00 78.31  ?  353  TYR C N   1 
ATOM   11821 C  CA  . TYR C 3  353  ? -46.947 -9.859   30.726  1.00 88.49  ?  353  TYR C CA  1 
ATOM   11822 C  C   . TYR C 3  353  ? -47.597 -8.538   30.336  1.00 94.29  ?  353  TYR C C   1 
ATOM   11823 O  O   . TYR C 3  353  ? -47.472 -7.541   31.057  1.00 96.34  ?  353  TYR C O   1 
ATOM   11824 C  CB  . TYR C 3  353  ? -45.600 -10.020  30.022  1.00 88.98  ?  353  TYR C CB  1 
ATOM   11825 C  CG  . TYR C 3  353  ? -44.475 -9.226   30.647  1.00 86.43  ?  353  TYR C CG  1 
ATOM   11826 C  CD1 . TYR C 3  353  ? -44.038 -9.498   31.937  1.00 87.39  ?  353  TYR C CD1 1 
ATOM   11827 C  CD2 . TYR C 3  353  ? -43.853 -8.200   29.947  1.00 85.87  ?  353  TYR C CD2 1 
ATOM   11828 C  CE1 . TYR C 3  353  ? -43.009 -8.774   32.510  1.00 93.45  ?  353  TYR C CE1 1 
ATOM   11829 C  CE2 . TYR C 3  353  ? -42.825 -7.470   30.512  1.00 82.67  ?  353  TYR C CE2 1 
ATOM   11830 C  CZ  . TYR C 3  353  ? -42.407 -7.761   31.793  1.00 89.43  ?  353  TYR C CZ  1 
ATOM   11831 O  OH  . TYR C 3  353  ? -41.383 -7.037   32.360  1.00 88.11  ?  353  TYR C OH  1 
ATOM   11832 N  N   . TRP C 3  354  ? -48.292 -8.508   29.196  1.00 94.61  ?  354  TRP C N   1 
ATOM   11833 C  CA  . TRP C 3  354  ? -48.974 -7.285   28.785  1.00 97.25  ?  354  TRP C CA  1 
ATOM   11834 C  C   . TRP C 3  354  ? -50.155 -6.981   29.699  1.00 103.25 ?  354  TRP C C   1 
ATOM   11835 O  O   . TRP C 3  354  ? -50.405 -5.816   30.031  1.00 113.90 ?  354  TRP C O   1 
ATOM   11836 C  CB  . TRP C 3  354  ? -49.431 -7.395   27.330  1.00 101.86 ?  354  TRP C CB  1 
ATOM   11837 C  CG  . TRP C 3  354  ? -48.304 -7.377   26.337  1.00 108.80 ?  354  TRP C CG  1 
ATOM   11838 C  CD1 . TRP C 3  354  ? -47.963 -8.369   25.464  1.00 100.59 ?  354  TRP C CD1 1 
ATOM   11839 C  CD2 . TRP C 3  354  ? -47.366 -6.314   26.119  1.00 113.83 ?  354  TRP C CD2 1 
ATOM   11840 N  NE1 . TRP C 3  354  ? -46.875 -7.990   24.716  1.00 99.80  ?  354  TRP C NE1 1 
ATOM   11841 C  CE2 . TRP C 3  354  ? -46.489 -6.732   25.099  1.00 108.23 ?  354  TRP C CE2 1 
ATOM   11842 C  CE3 . TRP C 3  354  ? -47.185 -5.048   26.687  1.00 114.31 ?  354  TRP C CE3 1 
ATOM   11843 C  CZ2 . TRP C 3  354  ? -45.447 -5.932   24.635  1.00 106.12 ?  354  TRP C CZ2 1 
ATOM   11844 C  CZ3 . TRP C 3  354  ? -46.149 -4.256   26.225  1.00 113.66 ?  354  TRP C CZ3 1 
ATOM   11845 C  CH2 . TRP C 3  354  ? -45.294 -4.700   25.209  1.00 103.97 ?  354  TRP C CH2 1 
ATOM   11846 N  N   . GLY C 3  355  ? -50.895 -8.012   30.112  1.00 91.81  ?  355  GLY C N   1 
ATOM   11847 C  CA  . GLY C 3  355  ? -51.952 -7.801   31.087  1.00 93.48  ?  355  GLY C CA  1 
ATOM   11848 C  C   . GLY C 3  355  ? -51.410 -7.350   32.429  1.00 103.27 ?  355  GLY C C   1 
ATOM   11849 O  O   . GLY C 3  355  ? -52.032 -6.539   33.121  1.00 107.97 ?  355  GLY C O   1 
ATOM   11850 N  N   . LEU C 3  356  ? -50.243 -7.872   32.814  1.00 110.57 ?  356  LEU C N   1 
ATOM   11851 C  CA  . LEU C 3  356  ? -49.560 -7.394   34.012  1.00 109.48 ?  356  LEU C CA  1 
ATOM   11852 C  C   . LEU C 3  356  ? -49.287 -5.898   33.923  1.00 103.01 ?  356  LEU C C   1 
ATOM   11853 O  O   . LEU C 3  356  ? -49.646 -5.133   34.825  1.00 111.67 ?  356  LEU C O   1 
ATOM   11854 C  CB  . LEU C 3  356  ? -48.255 -8.173   34.203  1.00 105.72 ?  356  LEU C CB  1 
ATOM   11855 C  CG  . LEU C 3  356  ? -47.273 -7.808   35.320  1.00 93.15  ?  356  LEU C CG  1 
ATOM   11856 C  CD1 . LEU C 3  356  ? -46.523 -9.048   35.755  1.00 88.39  ?  356  LEU C CD1 1 
ATOM   11857 C  CD2 . LEU C 3  356  ? -46.281 -6.744   34.873  1.00 90.11  ?  356  LEU C CD2 1 
ATOM   11858 N  N   . LEU C 3  357  ? -48.647 -5.466   32.833  1.00 84.96  ?  357  LEU C N   1 
ATOM   11859 C  CA  . LEU C 3  357  ? -48.275 -4.063   32.691  1.00 89.12  ?  357  LEU C CA  1 
ATOM   11860 C  C   . LEU C 3  357  ? -49.497 -3.158   32.622  1.00 94.98  ?  357  LEU C C   1 
ATOM   11861 O  O   . LEU C 3  357  ? -49.447 -2.013   33.084  1.00 95.95  ?  357  LEU C O   1 
ATOM   11862 C  CB  . LEU C 3  357  ? -47.407 -3.883   31.445  1.00 89.10  ?  357  LEU C CB  1 
ATOM   11863 C  CG  . LEU C 3  357  ? -46.005 -4.492   31.512  1.00 81.29  ?  357  LEU C CG  1 
ATOM   11864 C  CD1 . LEU C 3  357  ? -45.262 -4.280   30.203  1.00 96.22  ?  357  LEU C CD1 1 
ATOM   11865 C  CD2 . LEU C 3  357  ? -45.225 -3.902   32.675  1.00 66.36  ?  357  LEU C CD2 1 
ATOM   11866 N  N   . PHE C 3  358  ? -50.601 -3.649   32.057  1.00 109.84 ?  358  PHE C N   1 
ATOM   11867 C  CA  . PHE C 3  358  ? -51.807 -2.834   31.968  1.00 121.87 ?  358  PHE C CA  1 
ATOM   11868 C  C   . PHE C 3  358  ? -52.518 -2.729   33.312  1.00 121.52 ?  358  PHE C C   1 
ATOM   11869 O  O   . PHE C 3  358  ? -53.020 -1.658   33.670  1.00 120.43 ?  358  PHE C O   1 
ATOM   11870 C  CB  . PHE C 3  358  ? -52.754 -3.410   30.914  1.00 123.90 ?  358  PHE C CB  1 
ATOM   11871 C  CG  . PHE C 3  358  ? -54.114 -2.770   30.910  1.00 129.27 ?  358  PHE C CG  1 
ATOM   11872 C  CD1 . PHE C 3  358  ? -54.304 -1.524   30.339  1.00 120.68 ?  358  PHE C CD1 1 
ATOM   11873 C  CD2 . PHE C 3  358  ? -55.203 -3.416   31.475  1.00 123.89 ?  358  PHE C CD2 1 
ATOM   11874 C  CE1 . PHE C 3  358  ? -55.552 -0.929   30.337  1.00 122.12 ?  358  PHE C CE1 1 
ATOM   11875 C  CE2 . PHE C 3  358  ? -56.454 -2.829   31.475  1.00 116.22 ?  358  PHE C CE2 1 
ATOM   11876 C  CZ  . PHE C 3  358  ? -56.630 -1.584   30.905  1.00 114.15 ?  358  PHE C CZ  1 
ATOM   11877 N  N   . CYS C 3  359  ? -52.566 -3.826   34.067  1.00 108.93 ?  359  CYS C N   1 
ATOM   11878 C  CA  . CYS C 3  359  ? -53.383 -3.869   35.274  1.00 113.75 ?  359  CYS C CA  1 
ATOM   11879 C  C   . CYS C 3  359  ? -52.697 -3.177   36.449  1.00 113.43 ?  359  CYS C C   1 
ATOM   11880 O  O   . CYS C 3  359  ? -53.189 -2.166   36.960  1.00 109.73 ?  359  CYS C O   1 
ATOM   11881 C  CB  . CYS C 3  359  ? -53.715 -5.322   35.626  1.00 106.84 ?  359  CYS C CB  1 
ATOM   11882 S  SG  . CYS C 3  359  ? -54.960 -6.085   34.560  1.00 112.04 ?  359  CYS C SG  1 
ATOM   11883 N  N   . ASN C 3  360  ? -51.563 -3.713   36.892  1.00 125.15 ?  360  ASN C N   1 
ATOM   11884 C  CA  . ASN C 3  360  ? -50.910 -3.260   38.113  1.00 116.47 ?  360  ASN C CA  1 
ATOM   11885 C  C   . ASN C 3  360  ? -49.960 -2.089   37.892  1.00 111.89 ?  360  ASN C C   1 
ATOM   11886 O  O   . ASN C 3  360  ? -49.207 -1.741   38.808  1.00 114.34 ?  360  ASN C O   1 
ATOM   11887 C  CB  . ASN C 3  360  ? -50.153 -4.420   38.763  1.00 108.04 ?  360  ASN C CB  1 
ATOM   11888 C  CG  . ASN C 3  360  ? -51.055 -5.592   39.088  1.00 104.58 ?  360  ASN C CG  1 
ATOM   11889 O  OD1 . ASN C 3  360  ? -52.280 -5.490   39.008  1.00 108.16 ?  360  ASN C OD1 1 
ATOM   11890 N  ND2 . ASN C 3  360  ? -50.453 -6.714   39.461  1.00 102.67 ?  360  ASN C ND2 1 
ATOM   11891 N  N   . ALA C 3  361  ? -49.973 -1.478   36.721  1.00 106.90 ?  361  ALA C N   1 
ATOM   11892 C  CA  . ALA C 3  361  ? -49.106 -0.330   36.481  1.00 110.71 ?  361  ALA C CA  1 
ATOM   11893 C  C   . ALA C 3  361  ? -49.847 0.859    35.889  1.00 115.03 ?  361  ALA C C   1 
ATOM   11894 O  O   . ALA C 3  361  ? -49.587 1.996    36.288  1.00 115.77 ?  361  ALA C O   1 
ATOM   11895 C  CB  . ALA C 3  361  ? -47.940 -0.727   35.561  1.00 104.94 ?  361  ALA C CB  1 
ATOM   11896 N  N   . VAL C 3  362  ? -50.762 0.627    34.953  1.00 92.55  ?  362  VAL C N   1 
ATOM   11897 C  CA  . VAL C 3  362  ? -51.518 1.718    34.346  1.00 81.38  ?  362  VAL C CA  1 
ATOM   11898 C  C   . VAL C 3  362  ? -52.802 1.999    35.116  1.00 80.92  ?  362  VAL C C   1 
ATOM   11899 O  O   . VAL C 3  362  ? -53.145 3.159    35.358  1.00 82.48  ?  362  VAL C O   1 
ATOM   11900 C  CB  . VAL C 3  362  ? -51.806 1.396    32.866  1.00 84.51  ?  362  VAL C CB  1 
ATOM   11901 C  CG1 . VAL C 3  362  ? -52.704 2.458    32.252  1.00 85.26  ?  362  VAL C CG1 1 
ATOM   11902 C  CG2 . VAL C 3  362  ? -50.506 1.278    32.087  1.00 87.96  ?  362  VAL C CG2 1 
ATOM   11903 N  N   . ALA C 3  363  ? -53.521 0.951    35.525  1.00 104.60 ?  363  ALA C N   1 
ATOM   11904 C  CA  . ALA C 3  363  ? -54.804 1.141    36.191  1.00 102.48 ?  363  ALA C CA  1 
ATOM   11905 C  C   . ALA C 3  363  ? -54.658 1.649    37.619  1.00 105.62 ?  363  ALA C C   1 
ATOM   11906 O  O   . ALA C 3  363  ? -55.642 2.129    38.193  1.00 112.60 ?  363  ALA C O   1 
ATOM   11907 C  CB  . ALA C 3  363  ? -55.600 -0.165   36.185  1.00 106.51 ?  363  ALA C CB  1 
ATOM   11908 N  N   . ILE C 3  364  ? -53.462 1.557    38.208  1.00 92.81  ?  364  ILE C N   1 
ATOM   11909 C  CA  . ILE C 3  364  ? -53.257 2.043    39.571  1.00 91.77  ?  364  ILE C CA  1 
ATOM   11910 C  C   . ILE C 3  364  ? -52.894 3.519    39.621  1.00 87.21  ?  364  ILE C C   1 
ATOM   11911 O  O   . ILE C 3  364  ? -52.889 4.108    40.713  1.00 93.27  ?  364  ILE C O   1 
ATOM   11912 C  CB  . ILE C 3  364  ? -52.164 1.232    40.296  1.00 87.77  ?  364  ILE C CB  1 
ATOM   11913 C  CG1 . ILE C 3  364  ? -50.774 1.651    39.814  1.00 85.99  ?  364  ILE C CG1 1 
ATOM   11914 C  CG2 . ILE C 3  364  ? -52.377 -0.257   40.081  1.00 89.04  ?  364  ILE C CG2 1 
ATOM   11915 C  CD1 . ILE C 3  364  ? -49.647 1.152    40.694  1.00 80.96  ?  364  ILE C CD1 1 
ATOM   11916 N  N   . GLN C 3  365  ? -52.591 4.136    38.482  1.00 86.83  ?  365  GLN C N   1 
ATOM   11917 C  CA  . GLN C 3  365  ? -52.235 5.550    38.416  1.00 93.11  ?  365  GLN C CA  1 
ATOM   11918 C  C   . GLN C 3  365  ? -53.395 6.481    38.773  1.00 96.48  ?  365  GLN C C   1 
ATOM   11919 O  O   . GLN C 3  365  ? -53.163 7.501    39.436  1.00 92.82  ?  365  GLN C O   1 
ATOM   11920 C  CB  . GLN C 3  365  ? -51.692 5.895    37.026  1.00 91.75  ?  365  GLN C CB  1 
ATOM   11921 C  CG  . GLN C 3  365  ? -50.403 5.172    36.670  1.00 91.07  ?  365  GLN C CG  1 
ATOM   11922 C  CD  . GLN C 3  365  ? -49.374 5.228    37.784  1.00 89.06  ?  365  GLN C CD  1 
ATOM   11923 O  OE1 . GLN C 3  365  ? -49.068 6.298    38.310  1.00 81.94  ?  365  GLN C OE1 1 
ATOM   11924 N  NE2 . GLN C 3  365  ? -48.838 4.070    38.153  1.00 100.91 ?  365  GLN C NE2 1 
ATOM   11925 N  N   . PRO C 3  366  ? -54.640 6.204    38.359  1.00 98.72  ?  366  PRO C N   1 
ATOM   11926 C  CA  . PRO C 3  366  ? -55.749 7.082    38.775  1.00 99.20  ?  366  PRO C CA  1 
ATOM   11927 C  C   . PRO C 3  366  ? -55.921 7.203    40.282  1.00 98.01  ?  366  PRO C C   1 
ATOM   11928 O  O   . PRO C 3  366  ? -56.608 8.126    40.735  1.00 100.63 ?  366  PRO C O   1 
ATOM   11929 C  CB  . PRO C 3  366  ? -56.976 6.430    38.125  1.00 96.65  ?  366  PRO C CB  1 
ATOM   11930 C  CG  . PRO C 3  366  ? -56.436 5.756    36.931  1.00 94.95  ?  366  PRO C CG  1 
ATOM   11931 C  CD  . PRO C 3  366  ? -55.085 5.242    37.330  1.00 94.59  ?  366  PRO C CD  1 
ATOM   11932 N  N   . LEU C 3  367  ? -55.325 6.309    41.073  1.00 105.87 ?  367  LEU C N   1 
ATOM   11933 C  CA  . LEU C 3  367  ? -55.403 6.423    42.524  1.00 97.66  ?  367  LEU C CA  1 
ATOM   11934 C  C   . LEU C 3  367  ? -54.628 7.617    43.067  1.00 94.78  ?  367  LEU C C   1 
ATOM   11935 O  O   . LEU C 3  367  ? -54.824 7.980    44.231  1.00 99.27  ?  367  LEU C O   1 
ATOM   11936 C  CB  . LEU C 3  367  ? -54.891 5.140    43.179  1.00 88.37  ?  367  LEU C CB  1 
ATOM   11937 C  CG  . LEU C 3  367  ? -55.818 3.928    43.102  1.00 85.67  ?  367  LEU C CG  1 
ATOM   11938 C  CD1 . LEU C 3  367  ? -55.117 2.700    43.652  1.00 89.05  ?  367  LEU C CD1 1 
ATOM   11939 C  CD2 . LEU C 3  367  ? -57.114 4.192    43.852  1.00 80.04  ?  367  LEU C CD2 1 
ATOM   11940 N  N   . TRP C 3  368  ? -53.757 8.229    42.260  1.00 101.87 ?  368  TRP C N   1 
ATOM   11941 C  CA  . TRP C 3  368  ? -52.999 9.387    42.724  1.00 107.41 ?  368  TRP C CA  1 
ATOM   11942 C  C   . TRP C 3  368  ? -53.909 10.567   43.035  1.00 115.07 ?  368  TRP C C   1 
ATOM   11943 O  O   . TRP C 3  368  ? -53.630 11.340   43.959  1.00 126.11 ?  368  TRP C O   1 
ATOM   11944 C  CB  . TRP C 3  368  ? -51.962 9.790    41.675  1.00 111.51 ?  368  TRP C CB  1 
ATOM   11945 C  CG  . TRP C 3  368  ? -50.718 8.955    41.689  1.00 106.21 ?  368  TRP C CG  1 
ATOM   11946 C  CD1 . TRP C 3  368  ? -50.400 7.946    40.828  1.00 100.08 ?  368  TRP C CD1 1 
ATOM   11947 C  CD2 . TRP C 3  368  ? -49.619 9.065    42.601  1.00 103.59 ?  368  TRP C CD2 1 
ATOM   11948 N  NE1 . TRP C 3  368  ? -49.174 7.416    41.151  1.00 95.13  ?  368  TRP C NE1 1 
ATOM   11949 C  CE2 . TRP C 3  368  ? -48.674 8.086    42.236  1.00 94.62  ?  368  TRP C CE2 1 
ATOM   11950 C  CE3 . TRP C 3  368  ? -49.344 9.894    43.693  1.00 113.57 ?  368  TRP C CE3 1 
ATOM   11951 C  CZ2 . TRP C 3  368  ? -47.474 7.913    42.923  1.00 93.15  ?  368  TRP C CZ2 1 
ATOM   11952 C  CZ3 . TRP C 3  368  ? -48.152 9.721    44.374  1.00 109.21 ?  368  TRP C CZ3 1 
ATOM   11953 C  CH2 . TRP C 3  368  ? -47.232 8.738    43.986  1.00 100.46 ?  368  TRP C CH2 1 
ATOM   11954 N  N   . PHE C 3  369  ? -54.995 10.722   42.283  1.00 112.01 ?  369  PHE C N   1 
ATOM   11955 C  CA  . PHE C 3  369  ? -55.872 11.871   42.433  1.00 117.07 ?  369  PHE C CA  1 
ATOM   11956 C  C   . PHE C 3  369  ? -56.859 11.652   43.578  1.00 124.74 ?  369  PHE C C   1 
ATOM   11957 O  O   . PHE C 3  369  ? -57.034 10.541   44.086  1.00 124.55 ?  369  PHE C O   1 
ATOM   11958 C  CB  . PHE C 3  369  ? -56.614 12.151   41.126  1.00 111.28 ?  369  PHE C CB  1 
ATOM   11959 C  CG  . PHE C 3  369  ? -55.710 12.514   39.981  1.00 107.80 ?  369  PHE C CG  1 
ATOM   11960 C  CD1 . PHE C 3  369  ? -54.988 11.540   39.310  1.00 103.56 ?  369  PHE C CD1 1 
ATOM   11961 C  CD2 . PHE C 3  369  ? -55.575 13.833   39.582  1.00 115.46 ?  369  PHE C CD2 1 
ATOM   11962 C  CE1 . PHE C 3  369  ? -54.153 11.873   38.260  1.00 106.75 ?  369  PHE C CE1 1 
ATOM   11963 C  CE2 . PHE C 3  369  ? -54.742 14.173   38.532  1.00 130.40 ?  369  PHE C CE2 1 
ATOM   11964 C  CZ  . PHE C 3  369  ? -54.031 13.192   37.870  1.00 120.64 ?  369  PHE C CZ  1 
ATOM   11965 N  N   . LYS C 3  370  ? -57.514 12.741   43.982  1.00 148.21 ?  370  LYS C N   1 
ATOM   11966 C  CA  . LYS C 3  370  ? -58.415 12.720   45.129  1.00 140.58 ?  370  LYS C CA  1 
ATOM   11967 C  C   . LYS C 3  370  ? -59.847 12.372   44.742  1.00 143.12 ?  370  LYS C C   1 
ATOM   11968 O  O   . LYS C 3  370  ? -60.514 11.620   45.461  1.00 140.48 ?  370  LYS C O   1 
ATOM   11969 C  CB  . LYS C 3  370  ? -58.389 14.075   45.844  1.00 147.06 ?  370  LYS C CB  1 
ATOM   11970 C  CG  . LYS C 3  370  ? -57.312 14.209   46.916  1.00 153.48 ?  370  LYS C CG  1 
ATOM   11971 C  CD  . LYS C 3  370  ? -55.916 14.243   46.313  1.00 161.04 ?  370  LYS C CD  1 
ATOM   11972 C  CE  . LYS C 3  370  ? -55.751 15.429   45.375  1.00 164.74 ?  370  LYS C CE  1 
ATOM   11973 N  NZ  . LYS C 3  370  ? -54.439 15.402   44.673  1.00 149.81 ?  370  LYS C NZ  1 
ATOM   11974 N  N   . LYS C 3  371  ? -60.335 12.911   43.621  1.00 121.29 ?  371  LYS C N   1 
ATOM   11975 C  CA  . LYS C 3  371  ? -61.699 12.616   43.190  1.00 117.88 ?  371  LYS C CA  1 
ATOM   11976 C  C   . LYS C 3  371  ? -61.868 11.134   42.880  1.00 118.32 ?  371  LYS C C   1 
ATOM   11977 O  O   . LYS C 3  371  ? -62.896 10.534   43.216  1.00 111.64 ?  371  LYS C O   1 
ATOM   11978 C  CB  . LYS C 3  371  ? -62.059 13.471   41.974  1.00 117.65 ?  371  LYS C CB  1 
ATOM   11979 C  CG  . LYS C 3  371  ? -63.462 13.237   41.425  1.00 120.90 ?  371  LYS C CG  1 
ATOM   11980 C  CD  . LYS C 3  371  ? -63.429 12.419   40.142  1.00 114.74 ?  371  LYS C CD  1 
ATOM   11981 C  CE  . LYS C 3  371  ? -64.754 11.716   39.899  1.00 114.08 ?  371  LYS C CE  1 
ATOM   11982 N  NZ  . LYS C 3  371  ? -64.673 10.774   38.750  1.00 108.18 ?  371  LYS C NZ  1 
ATOM   11983 N  N   . VAL C 3  372  ? -60.866 10.525   42.242  1.00 107.14 ?  372  VAL C N   1 
ATOM   11984 C  CA  . VAL C 3  372  ? -60.921 9.092    41.972  1.00 108.91 ?  372  VAL C CA  1 
ATOM   11985 C  C   . VAL C 3  372  ? -60.818 8.302    43.271  1.00 104.34 ?  372  VAL C C   1 
ATOM   11986 O  O   . VAL C 3  372  ? -61.463 7.259    43.434  1.00 99.12  ?  372  VAL C O   1 
ATOM   11987 C  CB  . VAL C 3  372  ? -59.816 8.697    40.975  1.00 98.72  ?  372  VAL C CB  1 
ATOM   11988 C  CG1 . VAL C 3  372  ? -59.903 7.215    40.636  1.00 94.76  ?  372  VAL C CG1 1 
ATOM   11989 C  CG2 . VAL C 3  372  ? -59.907 9.546    39.717  1.00 100.65 ?  372  VAL C CG2 1 
ATOM   11990 N  N   . ARG C 3  373  ? -60.013 8.789    44.218  1.00 93.50  ?  373  ARG C N   1 
ATOM   11991 C  CA  . ARG C 3  373  ? -59.858 8.106    45.497  1.00 94.27  ?  373  ARG C CA  1 
ATOM   11992 C  C   . ARG C 3  373  ? -61.116 8.183    46.353  1.00 100.31 ?  373  ARG C C   1 
ATOM   11993 O  O   . ARG C 3  373  ? -61.275 7.372    47.272  1.00 92.37  ?  373  ARG C O   1 
ATOM   11994 C  CB  . ARG C 3  373  ? -58.667 8.689    46.260  1.00 91.08  ?  373  ARG C CB  1 
ATOM   11995 C  CG  . ARG C 3  373  ? -57.848 7.652    47.009  1.00 80.51  ?  373  ARG C CG  1 
ATOM   11996 C  CD  . ARG C 3  373  ? -56.389 8.066    47.135  1.00 77.93  ?  373  ARG C CD  1 
ATOM   11997 N  NE  . ARG C 3  373  ? -56.221 9.293    47.904  1.00 76.40  ?  373  ARG C NE  1 
ATOM   11998 C  CZ  . ARG C 3  373  ? -55.615 10.383   47.453  1.00 77.81  ?  373  ARG C CZ  1 
ATOM   11999 N  NH1 . ARG C 3  373  ? -55.090 10.429   46.239  1.00 78.20  ?  373  ARG C NH1 1 
ATOM   12000 N  NH2 . ARG C 3  373  ? -55.530 11.452   48.239  1.00 86.00  ?  373  ARG C NH2 1 
ATOM   12001 N  N   . GLN C 3  374  ? -62.010 9.131    46.076  1.00 122.93 ?  374  GLN C N   1 
ATOM   12002 C  CA  . GLN C 3  374  ? -63.264 9.260    46.804  1.00 117.94 ?  374  GLN C CA  1 
ATOM   12003 C  C   . GLN C 3  374  ? -64.447 8.658    46.058  1.00 117.00 ?  374  GLN C C   1 
ATOM   12004 O  O   . GLN C 3  374  ? -65.572 8.706    46.565  1.00 113.50 ?  374  GLN C O   1 
ATOM   12005 C  CB  . GLN C 3  374  ? -63.544 10.734   47.115  1.00 125.14 ?  374  GLN C CB  1 
ATOM   12006 C  CG  . GLN C 3  374  ? -62.592 11.346   48.132  1.00 130.02 ?  374  GLN C CG  1 
ATOM   12007 C  CD  . GLN C 3  374  ? -63.154 11.338   49.542  1.00 135.31 ?  374  GLN C CD  1 
ATOM   12008 O  OE1 . GLN C 3  374  ? -64.289 11.754   49.772  1.00 143.94 ?  374  GLN C OE1 1 
ATOM   12009 N  NE2 . GLN C 3  374  ? -62.358 10.864   50.494  1.00 125.69 ?  374  GLN C NE2 1 
ATOM   12010 N  N   . ASN C 3  375  ? -64.224 8.097    44.872  1.00 128.81 ?  375  ASN C N   1 
ATOM   12011 C  CA  . ASN C 3  375  ? -65.286 7.472    44.095  1.00 128.04 ?  375  ASN C CA  1 
ATOM   12012 C  C   . ASN C 3  375  ? -65.345 5.982    44.411  1.00 120.11 ?  375  ASN C C   1 
ATOM   12013 O  O   . ASN C 3  375  ? -64.321 5.292    44.373  1.00 125.53 ?  375  ASN C O   1 
ATOM   12014 C  CB  . ASN C 3  375  ? -65.060 7.691    42.599  1.00 123.78 ?  375  ASN C CB  1 
ATOM   12015 C  CG  . ASN C 3  375  ? -66.331 7.535    41.789  1.00 125.27 ?  375  ASN C CG  1 
ATOM   12016 O  OD1 . ASN C 3  375  ? -67.430 7.793    42.281  1.00 130.00 ?  375  ASN C OD1 1 
ATOM   12017 N  ND2 . ASN C 3  375  ? -66.187 7.113    40.539  1.00 128.42 ?  375  ASN C ND2 1 
ATOM   12018 N  N   . ILE C 3  376  ? -66.542 5.493    44.716  1.00 91.28  ?  376  ILE C N   1 
ATOM   12019 C  CA  . ILE C 3  376  ? -66.736 4.100    45.115  1.00 98.60  ?  376  ILE C CA  1 
ATOM   12020 C  C   . ILE C 3  376  ? -66.700 3.167    43.906  1.00 103.09 ?  376  ILE C C   1 
ATOM   12021 O  O   . ILE C 3  376  ? -65.972 2.163    43.946  1.00 97.42  ?  376  ILE C O   1 
ATOM   12022 C  CB  . ILE C 3  376  ? -68.039 3.931    45.915  1.00 97.72  ?  376  ILE C CB  1 
ATOM   12023 C  CG1 . ILE C 3  376  ? -67.884 4.528    47.315  1.00 96.17  ?  376  ILE C CG1 1 
ATOM   12024 C  CG2 . ILE C 3  376  ? -68.436 2.465    45.992  1.00 94.84  ?  376  ILE C CG2 1 
ATOM   12025 C  CD1 . ILE C 3  376  ? -69.087 4.315    48.207  1.00 81.30  ?  376  ILE C CD1 1 
ATOM   12026 N  N   . PRO C 3  377  ? -67.450 3.423    42.821  1.00 122.91 ?  377  PRO C N   1 
ATOM   12027 C  CA  . PRO C 3  377  ? -67.374 2.493    41.678  1.00 121.10 ?  377  PRO C CA  1 
ATOM   12028 C  C   . PRO C 3  377  ? -65.988 2.409    41.065  1.00 117.52 ?  377  PRO C C   1 
ATOM   12029 O  O   . PRO C 3  377  ? -65.580 1.333    40.609  1.00 112.32 ?  377  PRO C O   1 
ATOM   12030 C  CB  . PRO C 3  377  ? -68.401 3.065    40.691  1.00 123.74 ?  377  PRO C CB  1 
ATOM   12031 C  CG  . PRO C 3  377  ? -69.329 3.863    41.528  1.00 118.34 ?  377  PRO C CG  1 
ATOM   12032 C  CD  . PRO C 3  377  ? -68.463 4.469    42.584  1.00 121.55 ?  377  PRO C CD  1 
ATOM   12033 N  N   . ALA C 3  378  ? -65.248 3.521    41.041  1.00 98.67  ?  378  ALA C N   1 
ATOM   12034 C  CA  . ALA C 3  378  ? -63.882 3.485    40.530  1.00 91.89  ?  378  ALA C CA  1 
ATOM   12035 C  C   . ALA C 3  378  ? -62.989 2.625    41.413  1.00 90.61  ?  378  ALA C C   1 
ATOM   12036 O  O   . ALA C 3  378  ? -62.089 1.937    40.917  1.00 85.95  ?  378  ALA C O   1 
ATOM   12037 C  CB  . ALA C 3  378  ? -63.324 4.904    40.420  1.00 95.50  ?  378  ALA C CB  1 
ATOM   12038 N  N   . LEU C 3  379  ? -63.224 2.646    42.727  1.00 91.42  ?  379  LEU C N   1 
ATOM   12039 C  CA  . LEU C 3  379  ? -62.441 1.811    43.631  1.00 86.49  ?  379  LEU C CA  1 
ATOM   12040 C  C   . LEU C 3  379  ? -62.754 0.334    43.428  1.00 86.21  ?  379  LEU C C   1 
ATOM   12041 O  O   . LEU C 3  379  ? -61.856 -0.513   43.509  1.00 91.65  ?  379  LEU C O   1 
ATOM   12042 C  CB  . LEU C 3  379  ? -62.697 2.223    45.080  1.00 83.80  ?  379  LEU C CB  1 
ATOM   12043 C  CG  . LEU C 3  379  ? -61.935 3.455    45.573  1.00 92.87  ?  379  LEU C CG  1 
ATOM   12044 C  CD1 . LEU C 3  379  ? -62.360 3.822    46.986  1.00 104.00 ?  379  LEU C CD1 1 
ATOM   12045 C  CD2 . LEU C 3  379  ? -60.434 3.223    45.504  1.00 94.66  ?  379  LEU C CD2 1 
ATOM   12046 N  N   . LEU C 3  380  ? -64.021 0.005    43.163  1.00 93.27  ?  380  LEU C N   1 
ATOM   12047 C  CA  . LEU C 3  380  ? -64.386 -1.387   42.917  1.00 92.73  ?  380  LEU C CA  1 
ATOM   12048 C  C   . LEU C 3  380  ? -63.762 -1.901   41.626  1.00 94.23  ?  380  LEU C C   1 
ATOM   12049 O  O   . LEU C 3  380  ? -63.272 -3.035   41.575  1.00 96.96  ?  380  LEU C O   1 
ATOM   12050 C  CB  . LEU C 3  380  ? -65.907 -1.533   42.870  1.00 93.82  ?  380  LEU C CB  1 
ATOM   12051 C  CG  . LEU C 3  380  ? -66.674 -1.370   44.184  1.00 94.55  ?  380  LEU C CG  1 
ATOM   12052 C  CD1 . LEU C 3  380  ? -68.167 -1.516   43.945  1.00 95.80  ?  380  LEU C CD1 1 
ATOM   12053 C  CD2 . LEU C 3  380  ? -66.198 -2.374   45.220  1.00 96.85  ?  380  LEU C CD2 1 
ATOM   12054 N  N   . ILE C 3  381  ? -63.770 -1.081   40.574  1.00 100.56 ?  381  ILE C N   1 
ATOM   12055 C  CA  . ILE C 3  381  ? -63.188 -1.501   39.303  1.00 99.65  ?  381  ILE C CA  1 
ATOM   12056 C  C   . ILE C 3  381  ? -61.675 -1.640   39.425  1.00 101.97 ?  381  ILE C C   1 
ATOM   12057 O  O   . ILE C 3  381  ? -61.083 -2.594   38.907  1.00 110.94 ?  381  ILE C O   1 
ATOM   12058 C  CB  . ILE C 3  381  ? -63.582 -0.518   38.186  1.00 95.96  ?  381  ILE C CB  1 
ATOM   12059 C  CG1 . ILE C 3  381  ? -65.098 -0.521   37.986  1.00 99.69  ?  381  ILE C CG1 1 
ATOM   12060 C  CG2 . ILE C 3  381  ? -62.870 -0.865   36.888  1.00 83.62  ?  381  ILE C CG2 1 
ATOM   12061 C  CD1 . ILE C 3  381  ? -65.582 0.511    36.994  1.00 96.23  ?  381  ILE C CD1 1 
ATOM   12062 N  N   . ILE C 3  382  ? -61.026 -0.698   40.113  1.00 86.38  ?  382  ILE C N   1 
ATOM   12063 C  CA  . ILE C 3  382  ? -59.575 -0.761   40.266  1.00 88.20  ?  382  ILE C CA  1 
ATOM   12064 C  C   . ILE C 3  382  ? -59.174 -1.976   41.093  1.00 87.33  ?  382  ILE C C   1 
ATOM   12065 O  O   . ILE C 3  382  ? -58.184 -2.652   40.787  1.00 92.63  ?  382  ILE C O   1 
ATOM   12066 C  CB  . ILE C 3  382  ? -59.045 0.550    40.878  1.00 85.71  ?  382  ILE C CB  1 
ATOM   12067 C  CG1 . ILE C 3  382  ? -59.132 1.687    39.858  1.00 85.99  ?  382  ILE C CG1 1 
ATOM   12068 C  CG2 . ILE C 3  382  ? -57.611 0.384    41.363  1.00 78.56  ?  382  ILE C CG2 1 
ATOM   12069 C  CD1 . ILE C 3  382  ? -58.617 3.014    40.374  1.00 89.03  ?  382  ILE C CD1 1 
ATOM   12070 N  N   . SER C 3  383  ? -59.939 -2.284   42.144  1.00 86.05  ?  383  SER C N   1 
ATOM   12071 C  CA  . SER C 3  383  ? -59.628 -3.451   42.965  1.00 95.49  ?  383  SER C CA  1 
ATOM   12072 C  C   . SER C 3  383  ? -59.763 -4.742   42.166  1.00 91.58  ?  383  SER C C   1 
ATOM   12073 O  O   . SER C 3  383  ? -58.941 -5.656   42.307  1.00 90.90  ?  383  SER C O   1 
ATOM   12074 C  CB  . SER C 3  383  ? -60.531 -3.484   44.197  1.00 94.01  ?  383  SER C CB  1 
ATOM   12075 O  OG  . SER C 3  383  ? -60.416 -2.288   44.947  1.00 93.91  ?  383  SER C OG  1 
ATOM   12076 N  N   . LEU C 3  384  ? -60.795 -4.836   41.323  1.00 79.90  ?  384  LEU C N   1 
ATOM   12077 C  CA  . LEU C 3  384  ? -60.954 -6.018   40.481  1.00 76.57  ?  384  LEU C CA  1 
ATOM   12078 C  C   . LEU C 3  384  ? -59.806 -6.144   39.487  1.00 79.87  ?  384  LEU C C   1 
ATOM   12079 O  O   . LEU C 3  384  ? -59.272 -7.240   39.279  1.00 75.11  ?  384  LEU C O   1 
ATOM   12080 C  CB  . LEU C 3  384  ? -62.294 -5.964   39.749  1.00 76.40  ?  384  LEU C CB  1 
ATOM   12081 C  CG  . LEU C 3  384  ? -62.761 -7.265   39.094  1.00 78.94  ?  384  LEU C CG  1 
ATOM   12082 C  CD1 . LEU C 3  384  ? -62.794 -8.400   40.107  1.00 84.01  ?  384  LEU C CD1 1 
ATOM   12083 C  CD2 . LEU C 3  384  ? -64.124 -7.077   38.446  1.00 71.30  ?  384  LEU C CD2 1 
ATOM   12084 N  N   . ILE C 3  385  ? -59.411 -5.030   38.867  1.00 94.59  ?  385  ILE C N   1 
ATOM   12085 C  CA  . ILE C 3  385  ? -58.312 -5.057   37.907  1.00 91.66  ?  385  ILE C CA  1 
ATOM   12086 C  C   . ILE C 3  385  ? -57.002 -5.406   38.602  1.00 91.70  ?  385  ILE C C   1 
ATOM   12087 O  O   . ILE C 3  385  ? -56.161 -6.125   38.049  1.00 89.03  ?  385  ILE C O   1 
ATOM   12088 C  CB  . ILE C 3  385  ? -58.227 -3.708   37.168  1.00 91.19  ?  385  ILE C CB  1 
ATOM   12089 C  CG1 . ILE C 3  385  ? -59.461 -3.506   36.287  1.00 86.10  ?  385  ILE C CG1 1 
ATOM   12090 C  CG2 . ILE C 3  385  ? -56.963 -3.625   36.331  1.00 97.95  ?  385  ILE C CG2 1 
ATOM   12091 C  CD1 . ILE C 3  385  ? -59.457 -2.202   35.521  1.00 96.27  ?  385  ILE C CD1 1 
ATOM   12092 N  N   . VAL C 3  386  ? -56.813 -4.916   39.829  1.00 94.68  ?  386  VAL C N   1 
ATOM   12093 C  CA  . VAL C 3  386  ? -55.587 -5.208   40.565  1.00 93.43  ?  386  VAL C CA  1 
ATOM   12094 C  C   . VAL C 3  386  ? -55.509 -6.692   40.906  1.00 86.75  ?  386  VAL C C   1 
ATOM   12095 O  O   . VAL C 3  386  ? -54.442 -7.309   40.802  1.00 88.15  ?  386  VAL C O   1 
ATOM   12096 C  CB  . VAL C 3  386  ? -55.499 -4.326   41.824  1.00 88.68  ?  386  VAL C CB  1 
ATOM   12097 C  CG1 . VAL C 3  386  ? -54.563 -4.943   42.853  1.00 98.75  ?  386  VAL C CG1 1 
ATOM   12098 C  CG2 . VAL C 3  386  ? -55.039 -2.923   41.456  1.00 94.95  ?  386  VAL C CG2 1 
ATOM   12099 N  N   . SER C 3  387  ? -56.634 -7.290   41.306  1.00 95.32  ?  387  SER C N   1 
ATOM   12100 C  CA  . SER C 3  387  ? -56.644 -8.716   41.615  1.00 91.22  ?  387  SER C CA  1 
ATOM   12101 C  C   . SER C 3  387  ? -56.320 -9.552   40.382  1.00 100.12 ?  387  SER C C   1 
ATOM   12102 O  O   . SER C 3  387  ? -55.573 -10.534  40.467  1.00 94.77  ?  387  SER C O   1 
ATOM   12103 C  CB  . SER C 3  387  ? -58.001 -9.119   42.192  1.00 90.01  ?  387  SER C CB  1 
ATOM   12104 O  OG  . SER C 3  387  ? -58.271 -8.419   43.394  1.00 99.07  ?  387  SER C OG  1 
ATOM   12105 N  N   . VAL C 3  388  ? -56.874 -9.177   39.226  1.00 79.05  ?  388  VAL C N   1 
ATOM   12106 C  CA  . VAL C 3  388  ? -56.569 -9.891   37.990  1.00 62.49  ?  388  VAL C CA  1 
ATOM   12107 C  C   . VAL C 3  388  ? -55.098 -9.729   37.632  1.00 65.04  ?  388  VAL C C   1 
ATOM   12108 O  O   . VAL C 3  388  ? -54.437 -10.685  37.207  1.00 73.41  ?  388  VAL C O   1 
ATOM   12109 C  CB  . VAL C 3  388  ? -57.487 -9.408   36.852  1.00 59.41  ?  388  VAL C CB  1 
ATOM   12110 C  CG1 . VAL C 3  388  ? -57.125 -10.097  35.547  1.00 62.51  ?  388  VAL C CG1 1 
ATOM   12111 C  CG2 . VAL C 3  388  ? -58.943 -9.663   37.202  1.00 67.95  ?  388  VAL C CG2 1 
ATOM   12112 N  N   . GLY C 3  389  ? -54.559 -8.520   37.802  1.00 90.96  ?  389  GLY C N   1 
ATOM   12113 C  CA  . GLY C 3  389  ? -53.153 -8.301   37.515  1.00 92.68  ?  389  GLY C CA  1 
ATOM   12114 C  C   . GLY C 3  389  ? -52.227 -9.055   38.446  1.00 88.64  ?  389  GLY C C   1 
ATOM   12115 O  O   . GLY C 3  389  ? -51.145 -9.484   38.034  1.00 89.26  ?  389  GLY C O   1 
ATOM   12116 N  N   . MET C 3  390  ? -52.630 -9.228   39.708  1.00 93.99  ?  390  MET C N   1 
ATOM   12117 C  CA  . MET C 3  390  ? -51.813 -9.994   40.644  1.00 92.12  ?  390  MET C CA  1 
ATOM   12118 C  C   . MET C 3  390  ? -51.770 -11.467  40.261  1.00 93.34  ?  390  MET C C   1 
ATOM   12119 O  O   . MET C 3  390  ? -50.714 -12.104  40.344  1.00 98.62  ?  390  MET C O   1 
ATOM   12120 C  CB  . MET C 3  390  ? -52.338 -9.821   42.068  1.00 87.45  ?  390  MET C CB  1 
ATOM   12121 C  CG  . MET C 3  390  ? -52.062 -8.452   42.651  1.00 98.81  ?  390  MET C CG  1 
ATOM   12122 S  SD  . MET C 3  390  ? -50.408 -7.894   42.219  1.00 88.57  ?  390  MET C SD  1 
ATOM   12123 C  CE  . MET C 3  390  ? -49.458 -8.684   43.509  1.00 82.44  ?  390  MET C CE  1 
ATOM   12124 N  N   . TRP C 3  391  ? -52.908 -12.028  39.847  1.00 78.32  ?  391  TRP C N   1 
ATOM   12125 C  CA  . TRP C 3  391  ? -52.908 -13.398  39.345  1.00 71.91  ?  391  TRP C CA  1 
ATOM   12126 C  C   . TRP C 3  391  ? -52.048 -13.520  38.094  1.00 71.50  ?  391  TRP C C   1 
ATOM   12127 O  O   . TRP C 3  391  ? -51.338 -14.516  37.913  1.00 68.27  ?  391  TRP C O   1 
ATOM   12128 C  CB  . TRP C 3  391  ? -54.337 -13.856  39.059  1.00 71.90  ?  391  TRP C CB  1 
ATOM   12129 C  CG  . TRP C 3  391  ? -54.454 -15.333  38.884  1.00 76.57  ?  391  TRP C CG  1 
ATOM   12130 C  CD1 . TRP C 3  391  ? -54.746 -16.254  39.846  1.00 74.33  ?  391  TRP C CD1 1 
ATOM   12131 C  CD2 . TRP C 3  391  ? -54.265 -16.067  37.669  1.00 75.48  ?  391  TRP C CD2 1 
ATOM   12132 N  NE1 . TRP C 3  391  ? -54.759 -17.517  39.305  1.00 72.96  ?  391  TRP C NE1 1 
ATOM   12133 C  CE2 . TRP C 3  391  ? -54.465 -17.429  37.969  1.00 76.05  ?  391  TRP C CE2 1 
ATOM   12134 C  CE3 . TRP C 3  391  ? -53.948 -15.704  36.356  1.00 69.87  ?  391  TRP C CE3 1 
ATOM   12135 C  CZ2 . TRP C 3  391  ? -54.361 -18.429  37.003  1.00 74.63  ?  391  TRP C CZ2 1 
ATOM   12136 C  CZ3 . TRP C 3  391  ? -53.844 -16.697  35.400  1.00 72.27  ?  391  TRP C CZ3 1 
ATOM   12137 C  CH2 . TRP C 3  391  ? -54.049 -18.043  35.728  1.00 72.86  ?  391  TRP C CH2 1 
ATOM   12138 N  N   . LEU C 3  392  ? -52.098 -12.514  37.218  1.00 74.01  ?  392  LEU C N   1 
ATOM   12139 C  CA  . LEU C 3  392  ? -51.264 -12.531  36.021  1.00 71.65  ?  392  LEU C CA  1 
ATOM   12140 C  C   . LEU C 3  392  ? -49.786 -12.404  36.365  1.00 69.02  ?  392  LEU C C   1 
ATOM   12141 O  O   . LEU C 3  392  ? -48.939 -12.971  35.665  1.00 69.68  ?  392  LEU C O   1 
ATOM   12142 C  CB  . LEU C 3  392  ? -51.683 -11.410  35.070  1.00 65.96  ?  392  LEU C CB  1 
ATOM   12143 C  CG  . LEU C 3  392  ? -53.015 -11.591  34.343  1.00 63.25  ?  392  LEU C CG  1 
ATOM   12144 C  CD1 . LEU C 3  392  ? -53.294 -10.401  33.439  1.00 61.66  ?  392  LEU C CD1 1 
ATOM   12145 C  CD2 . LEU C 3  392  ? -53.018 -12.886  33.549  1.00 69.27  ?  392  LEU C CD2 1 
ATOM   12146 N  N   . GLU C 3  393  ? -49.456 -11.670  37.429  1.00 93.24  ?  393  GLU C N   1 
ATOM   12147 C  CA  . GLU C 3  393  ? -48.055 -11.519  37.807  1.00 90.58  ?  393  GLU C CA  1 
ATOM   12148 C  C   . GLU C 3  393  ? -47.488 -12.822  38.358  1.00 87.46  ?  393  GLU C C   1 
ATOM   12149 O  O   . GLU C 3  393  ? -46.356 -13.198  38.034  1.00 89.18  ?  393  GLU C O   1 
ATOM   12150 C  CB  . GLU C 3  393  ? -47.900 -10.388  38.823  1.00 94.87  ?  393  GLU C CB  1 
ATOM   12151 C  CG  . GLU C 3  393  ? -46.595 -10.432  39.601  1.00 98.37  ?  393  GLU C CG  1 
ATOM   12152 C  CD  . GLU C 3  393  ? -46.676 -9.683   40.913  1.00 108.56 ?  393  GLU C CD  1 
ATOM   12153 O  OE1 . GLU C 3  393  ? -47.547 -8.798   41.032  1.00 111.54 ?  393  GLU C OE1 1 
ATOM   12154 O  OE2 . GLU C 3  393  ? -45.876 -9.981   41.826  1.00 110.02 -1 393  GLU C OE2 1 
ATOM   12155 N  N   . ARG C 3  394  ? -48.258 -13.526  39.190  1.00 79.52  ?  394  ARG C N   1 
ATOM   12156 C  CA  . ARG C 3  394  ? -47.814 -14.830  39.671  1.00 77.35  ?  394  ARG C CA  1 
ATOM   12157 C  C   . ARG C 3  394  ? -47.662 -15.813  38.516  1.00 85.18  ?  394  ARG C C   1 
ATOM   12158 O  O   . ARG C 3  394  ? -46.772 -16.671  38.532  1.00 86.54  ?  394  ARG C O   1 
ATOM   12159 C  CB  . ARG C 3  394  ? -48.795 -15.369  40.710  1.00 77.86  ?  394  ARG C CB  1 
ATOM   12160 C  CG  . ARG C 3  394  ? -48.398 -15.095  42.150  1.00 87.54  ?  394  ARG C CG  1 
ATOM   12161 C  CD  . ARG C 3  394  ? -48.977 -13.778  42.644  1.00 85.15  ?  394  ARG C CD  1 
ATOM   12162 N  NE  . ARG C 3  394  ? -48.374 -13.357  43.902  1.00 88.35  ?  394  ARG C NE  1 
ATOM   12163 C  CZ  . ARG C 3  394  ? -48.901 -12.457  44.720  1.00 100.95 ?  394  ARG C CZ  1 
ATOM   12164 N  NH1 . ARG C 3  394  ? -50.053 -11.867  44.448  1.00 105.72 ?  394  ARG C NH1 1 
ATOM   12165 N  NH2 . ARG C 3  394  ? -48.260 -12.147  45.844  1.00 100.24 ?  394  ARG C NH2 1 
ATOM   12166 N  N   . TYR C 3  395  ? -48.522 -15.699  37.502  1.00 78.84  ?  395  TYR C N   1 
ATOM   12167 C  CA  . TYR C 3  395  ? -48.404 -16.554  36.325  1.00 68.07  ?  395  TYR C CA  1 
ATOM   12168 C  C   . TYR C 3  395  ? -47.136 -16.239  35.541  1.00 69.55  ?  395  TYR C C   1 
ATOM   12169 O  O   . TYR C 3  395  ? -46.426 -17.153  35.105  1.00 71.23  ?  395  TYR C O   1 
ATOM   12170 C  CB  . TYR C 3  395  ? -49.641 -16.389  35.441  1.00 72.79  ?  395  TYR C CB  1 
ATOM   12171 C  CG  . TYR C 3  395  ? -49.722 -17.355  34.279  1.00 67.22  ?  395  TYR C CG  1 
ATOM   12172 C  CD1 . TYR C 3  395  ? -49.090 -17.078  33.073  1.00 71.68  ?  395  TYR C CD1 1 
ATOM   12173 C  CD2 . TYR C 3  395  ? -50.441 -18.537  34.384  1.00 69.62  ?  395  TYR C CD2 1 
ATOM   12174 C  CE1 . TYR C 3  395  ? -49.164 -17.957  32.008  1.00 79.01  ?  395  TYR C CE1 1 
ATOM   12175 C  CE2 . TYR C 3  395  ? -50.521 -19.422  33.325  1.00 76.38  ?  395  TYR C CE2 1 
ATOM   12176 C  CZ  . TYR C 3  395  ? -49.881 -19.127  32.140  1.00 77.94  ?  395  TYR C CZ  1 
ATOM   12177 O  OH  . TYR C 3  395  ? -49.962 -20.008  31.086  1.00 76.19  ?  395  TYR C OH  1 
ATOM   12178 N  N   . VAL C 3  396  ? -46.841 -14.951  35.348  1.00 63.27  ?  396  VAL C N   1 
ATOM   12179 C  CA  . VAL C 3  396  ? -45.650 -14.554  34.599  1.00 62.78  ?  396  VAL C CA  1 
ATOM   12180 C  C   . VAL C 3  396  ? -44.388 -15.015  35.316  1.00 67.16  ?  396  VAL C C   1 
ATOM   12181 O  O   . VAL C 3  396  ? -43.429 -15.477  34.686  1.00 69.18  ?  396  VAL C O   1 
ATOM   12182 C  CB  . VAL C 3  396  ? -45.649 -13.029  34.374  1.00 67.59  ?  396  VAL C CB  1 
ATOM   12183 C  CG1 . VAL C 3  396  ? -44.239 -12.515  34.104  1.00 61.61  ?  396  VAL C CG1 1 
ATOM   12184 C  CG2 . VAL C 3  396  ? -46.576 -12.658  33.230  1.00 68.29  ?  396  VAL C CG2 1 
ATOM   12185 N  N   . ILE C 3  397  ? -44.371 -14.902  36.645  1.00 84.38  ?  397  ILE C N   1 
ATOM   12186 C  CA  . ILE C 3  397  ? -43.182 -15.259  37.411  1.00 84.49  ?  397  ILE C CA  1 
ATOM   12187 C  C   . ILE C 3  397  ? -42.913 -16.758  37.325  1.00 87.82  ?  397  ILE C C   1 
ATOM   12188 O  O   . ILE C 3  397  ? -41.770 -17.187  37.129  1.00 86.23  ?  397  ILE C O   1 
ATOM   12189 C  CB  . ILE C 3  397  ? -43.335 -14.791  38.870  1.00 83.86  ?  397  ILE C CB  1 
ATOM   12190 C  CG1 . ILE C 3  397  ? -43.168 -13.274  38.964  1.00 97.93  ?  397  ILE C CG1 1 
ATOM   12191 C  CG2 . ILE C 3  397  ? -42.335 -15.499  39.772  1.00 80.85  ?  397  ILE C CG2 1 
ATOM   12192 C  CD1 . ILE C 3  397  ? -43.220 -12.740  40.379  1.00 105.68 ?  397  ILE C CD1 1 
ATOM   12193 N  N   . ILE C 3  398  ? -43.958 -17.575  37.452  1.00 63.88  ?  398  ILE C N   1 
ATOM   12194 C  CA  . ILE C 3  398  ? -43.800 -19.021  37.569  1.00 63.17  ?  398  ILE C CA  1 
ATOM   12195 C  C   . ILE C 3  398  ? -43.779 -19.689  36.199  1.00 69.43  ?  398  ILE C C   1 
ATOM   12196 O  O   . ILE C 3  398  ? -42.772 -20.290  35.807  1.00 69.87  ?  398  ILE C O   1 
ATOM   12197 C  CB  . ILE C 3  398  ? -44.912 -19.625  38.446  1.00 67.10  ?  398  ILE C CB  1 
ATOM   12198 C  CG1 . ILE C 3  398  ? -44.921 -18.970  39.830  1.00 60.57  ?  398  ILE C CG1 1 
ATOM   12199 C  CG2 . ILE C 3  398  ? -44.744 -21.134  38.557  1.00 65.00  ?  398  ILE C CG2 1 
ATOM   12200 C  CD1 . ILE C 3  398  ? -46.018 -19.478  40.742  1.00 60.85  ?  398  ILE C CD1 1 
ATOM   12201 N  N   . VAL C 3  399  ? -44.889 -19.593  35.465  1.00 66.65  ?  399  VAL C N   1 
ATOM   12202 C  CA  . VAL C 3  399  ? -45.072 -20.419  34.273  1.00 55.34  ?  399  VAL C CA  1 
ATOM   12203 C  C   . VAL C 3  399  ? -44.117 -19.993  33.163  1.00 52.10  ?  399  VAL C C   1 
ATOM   12204 O  O   . VAL C 3  399  ? -43.435 -20.829  32.558  1.00 56.35  ?  399  VAL C O   1 
ATOM   12205 C  CB  . VAL C 3  399  ? -46.538 -20.368  33.806  1.00 55.59  ?  399  VAL C CB  1 
ATOM   12206 C  CG1 . VAL C 3  399  ? -46.687 -21.026  32.441  1.00 56.27  ?  399  VAL C CG1 1 
ATOM   12207 C  CG2 . VAL C 3  399  ? -47.443 -21.039  34.830  1.00 66.02  ?  399  VAL C CG2 1 
ATOM   12208 N  N   . ILE C 3  400  ? -44.057 -18.690  32.874  1.00 71.66  ?  400  ILE C N   1 
ATOM   12209 C  CA  . ILE C 3  400  ? -43.230 -18.212  31.768  1.00 76.78  ?  400  ILE C CA  1 
ATOM   12210 C  C   . ILE C 3  400  ? -41.763 -18.540  32.014  1.00 78.89  ?  400  ILE C C   1 
ATOM   12211 O  O   . ILE C 3  400  ? -41.046 -18.975  31.104  1.00 78.98  ?  400  ILE C O   1 
ATOM   12212 C  CB  . ILE C 3  400  ? -43.444 -16.703  31.553  1.00 76.10  ?  400  ILE C CB  1 
ATOM   12213 C  CG1 . ILE C 3  400  ? -44.858 -16.434  31.036  1.00 72.77  ?  400  ILE C CG1 1 
ATOM   12214 C  CG2 . ILE C 3  400  ? -42.412 -16.148  30.581  1.00 70.63  ?  400  ILE C CG2 1 
ATOM   12215 C  CD1 . ILE C 3  400  ? -45.094 -14.998  30.630  1.00 80.78  ?  400  ILE C CD1 1 
ATOM   12216 N  N   . SER C 3  401  ? -41.296 -18.348  33.250  1.00 70.11  ?  401  SER C N   1 
ATOM   12217 C  CA  . SER C 3  401  ? -39.905 -18.647  33.566  1.00 66.85  ?  401  SER C CA  1 
ATOM   12218 C  C   . SER C 3  401  ? -39.614 -20.141  33.484  1.00 57.33  ?  401  SER C C   1 
ATOM   12219 O  O   . SER C 3  401  ? -38.495 -20.534  33.133  1.00 50.58  ?  401  SER C O   1 
ATOM   12220 C  CB  . SER C 3  401  ? -39.559 -18.111  34.956  1.00 66.93  ?  401  SER C CB  1 
ATOM   12221 O  OG  . SER C 3  401  ? -38.177 -18.253  35.229  1.00 74.98  ?  401  SER C OG  1 
ATOM   12222 N  N   . LEU C 3  402  ? -40.599 -20.983  33.797  1.00 72.63  ?  402  LEU C N   1 
ATOM   12223 C  CA  . LEU C 3  402  ? -40.397 -22.426  33.780  1.00 78.03  ?  402  LEU C CA  1 
ATOM   12224 C  C   . LEU C 3  402  ? -40.538 -23.029  32.389  1.00 73.30  ?  402  LEU C C   1 
ATOM   12225 O  O   . LEU C 3  402  ? -40.092 -24.161  32.173  1.00 75.62  ?  402  LEU C O   1 
ATOM   12226 C  CB  . LEU C 3  402  ? -41.388 -23.109  34.726  1.00 78.17  ?  402  LEU C CB  1 
ATOM   12227 C  CG  . LEU C 3  402  ? -40.919 -23.380  36.156  1.00 69.88  ?  402  LEU C CG  1 
ATOM   12228 C  CD1 . LEU C 3  402  ? -41.998 -24.118  36.933  1.00 80.92  ?  402  LEU C CD1 1 
ATOM   12229 C  CD2 . LEU C 3  402  ? -39.620 -24.167  36.155  1.00 66.29  ?  402  LEU C CD2 1 
ATOM   12230 N  N   . GLU C 3  403  ? -41.143 -22.304  31.447  1.00 80.10  ?  403  GLU C N   1 
ATOM   12231 C  CA  . GLU C 3  403  ? -41.391 -22.874  30.126  1.00 75.93  ?  403  GLU C CA  1 
ATOM   12232 C  C   . GLU C 3  403  ? -40.100 -23.020  29.328  1.00 79.50  ?  403  GLU C C   1 
ATOM   12233 O  O   . GLU C 3  403  ? -39.876 -24.051  28.684  1.00 82.69  ?  403  GLU C O   1 
ATOM   12234 C  CB  . GLU C 3  403  ? -42.396 -22.012  29.363  1.00 77.56  ?  403  GLU C CB  1 
ATOM   12235 C  CG  . GLU C 3  403  ? -43.851 -22.352  29.644  1.00 83.50  ?  403  GLU C CG  1 
ATOM   12236 C  CD  . GLU C 3  403  ? -44.812 -21.527  28.810  1.00 97.07  ?  403  GLU C CD  1 
ATOM   12237 O  OE1 . GLU C 3  403  ? -44.344 -20.642  28.063  1.00 108.89 ?  403  GLU C OE1 1 
ATOM   12238 O  OE2 . GLU C 3  403  ? -46.036 -21.763  28.900  1.00 96.99  -1 403  GLU C OE2 1 
ATOM   12239 N  N   . ARG C 3  404  ? -39.241 -22.004  29.357  1.00 66.69  ?  404  ARG C N   1 
ATOM   12240 C  CA  . ARG C 3  404  ? -38.026 -21.974  28.550  1.00 67.02  ?  404  ARG C CA  1 
ATOM   12241 C  C   . ARG C 3  404  ? -36.831 -21.836  29.485  1.00 62.27  ?  404  ARG C C   1 
ATOM   12242 O  O   . ARG C 3  404  ? -36.607 -20.766  30.060  1.00 68.93  ?  404  ARG C O   1 
ATOM   12243 C  CB  . ARG C 3  404  ? -38.083 -20.833  27.536  1.00 67.41  ?  404  ARG C CB  1 
ATOM   12244 C  CG  . ARG C 3  404  ? -39.341 -20.870  26.681  1.00 69.95  ?  404  ARG C CG  1 
ATOM   12245 C  CD  . ARG C 3  404  ? -39.167 -20.159  25.352  1.00 70.97  ?  404  ARG C CD  1 
ATOM   12246 N  NE  . ARG C 3  404  ? -40.112 -20.664  24.363  1.00 73.02  ?  404  ARG C NE  1 
ATOM   12247 C  CZ  . ARG C 3  404  ? -40.201 -20.228  23.114  1.00 66.41  ?  404  ARG C CZ  1 
ATOM   12248 N  NH1 . ARG C 3  404  ? -39.402 -19.278  22.655  1.00 64.39  ?  404  ARG C NH1 1 
ATOM   12249 N  NH2 . ARG C 3  404  ? -41.113 -20.759  22.305  1.00 63.08  ?  404  ARG C NH2 1 
ATOM   12250 N  N   . ASP C 3  405  ? -36.065 -22.917  29.631  1.00 63.91  ?  405  ASP C N   1 
ATOM   12251 C  CA  . ASP C 3  405  ? -34.964 -23.013  30.572  1.00 64.62  ?  405  ASP C CA  1 
ATOM   12252 C  C   . ASP C 3  405  ? -33.632 -22.941  29.819  1.00 72.30  ?  405  ASP C C   1 
ATOM   12253 O  O   . ASP C 3  405  ? -33.554 -22.310  28.750  1.00 76.04  ?  405  ASP C O   1 
ATOM   12254 C  CB  . ASP C 3  405  ? -35.130 -24.286  31.396  1.00 71.01  ?  405  ASP C CB  1 
ATOM   12255 C  CG  . ASP C 3  405  ? -35.854 -24.042  32.701  1.00 95.02  ?  405  ASP C CG  1 
ATOM   12256 O  OD1 . ASP C 3  405  ? -35.756 -22.916  33.233  1.00 103.17 ?  405  ASP C OD1 1 
ATOM   12257 O  OD2 . ASP C 3  405  ? -36.520 -24.975  33.195  1.00 98.23  -1 405  ASP C OD2 1 
ATOM   12258 N  N   . PHE C 3  406  ? -32.598 -23.583  30.368  1.00 71.45  ?  406  PHE C N   1 
ATOM   12259 C  CA  . PHE C 3  406  ? -31.263 -23.490  29.786  1.00 75.49  ?  406  PHE C CA  1 
ATOM   12260 C  C   . PHE C 3  406  ? -31.153 -24.330  28.520  1.00 68.94  ?  406  PHE C C   1 
ATOM   12261 O  O   . PHE C 3  406  ? -30.700 -23.843  27.478  1.00 72.57  ?  406  PHE C O   1 
ATOM   12262 C  CB  . PHE C 3  406  ? -30.218 -23.927  30.813  1.00 79.27  ?  406  PHE C CB  1 
ATOM   12263 C  CG  . PHE C 3  406  ? -30.350 -23.241  32.143  1.00 76.55  ?  406  PHE C CG  1 
ATOM   12264 C  CD1 . PHE C 3  406  ? -29.876 -21.953  32.324  1.00 74.72  ?  406  PHE C CD1 1 
ATOM   12265 C  CD2 . PHE C 3  406  ? -30.946 -23.887  33.214  1.00 72.58  ?  406  PHE C CD2 1 
ATOM   12266 C  CE1 . PHE C 3  406  ? -29.996 -21.319  33.546  1.00 73.11  ?  406  PHE C CE1 1 
ATOM   12267 C  CE2 . PHE C 3  406  ? -31.069 -23.260  34.439  1.00 68.27  ?  406  PHE C CE2 1 
ATOM   12268 C  CZ  . PHE C 3  406  ? -30.593 -21.975  34.606  1.00 71.00  ?  406  PHE C CZ  1 
ATOM   12269 N  N   . LEU C 3  407  ? -31.556 -25.592  28.593  1.00 58.52  ?  407  LEU C N   1 
ATOM   12270 C  CA  . LEU C 3  407  ? -31.482 -26.477  27.439  1.00 61.27  ?  407  LEU C CA  1 
ATOM   12271 C  C   . LEU C 3  407  ? -32.673 -26.225  26.523  1.00 67.72  ?  407  LEU C C   1 
ATOM   12272 O  O   . LEU C 3  407  ? -33.818 -26.426  26.945  1.00 70.36  ?  407  LEU C O   1 
ATOM   12273 C  CB  . LEU C 3  407  ? -31.458 -27.934  27.885  1.00 70.37  ?  407  LEU C CB  1 
ATOM   12274 C  CG  . LEU C 3  407  ? -30.166 -28.438  28.536  1.00 69.92  ?  407  LEU C CG  1 
ATOM   12275 C  CD1 . LEU C 3  407  ? -30.091 -29.957  28.476  1.00 61.90  ?  407  LEU C CD1 1 
ATOM   12276 C  CD2 . LEU C 3  407  ? -28.944 -27.813  27.880  1.00 46.12  ?  407  LEU C CD2 1 
ATOM   12277 N  N   . PRO C 3  408  ? -32.458 -25.785  25.280  1.00 61.81  ?  408  PRO C N   1 
ATOM   12278 C  CA  . PRO C 3  408  ? -33.603 -25.506  24.398  1.00 54.90  ?  408  PRO C CA  1 
ATOM   12279 C  C   . PRO C 3  408  ? -34.447 -26.729  24.096  1.00 53.93  ?  408  PRO C C   1 
ATOM   12280 O  O   . PRO C 3  408  ? -35.643 -26.592  23.812  1.00 59.66  ?  408  PRO C O   1 
ATOM   12281 C  CB  . PRO C 3  408  ? -32.939 -24.950  23.129  1.00 55.42  ?  408  PRO C CB  1 
ATOM   12282 C  CG  . PRO C 3  408  ? -31.601 -24.457  23.584  1.00 60.45  ?  408  PRO C CG  1 
ATOM   12283 C  CD  . PRO C 3  408  ? -31.178 -25.415  24.655  1.00 62.21  ?  408  PRO C CD  1 
ATOM   12284 N  N   . SER C 3  409  ? -33.862 -27.926  24.151  1.00 69.87  ?  409  SER C N   1 
ATOM   12285 C  CA  . SER C 3  409  ? -34.623 -29.138  23.881  1.00 74.39  ?  409  SER C CA  1 
ATOM   12286 C  C   . SER C 3  409  ? -35.666 -29.418  24.954  1.00 78.70  ?  409  SER C C   1 
ATOM   12287 O  O   . SER C 3  409  ? -36.650 -30.112  24.678  1.00 86.60  ?  409  SER C O   1 
ATOM   12288 C  CB  . SER C 3  409  ? -33.676 -30.329  23.749  1.00 75.36  ?  409  SER C CB  1 
ATOM   12289 O  OG  . SER C 3  409  ? -32.804 -30.412  24.863  1.00 79.96  ?  409  SER C OG  1 
ATOM   12290 N  N   . SER C 3  410  ? -35.477 -28.899  26.165  1.00 99.08  ?  410  SER C N   1 
ATOM   12291 C  CA  . SER C 3  410  ? -36.435 -29.081  27.255  1.00 103.84 ?  410  SER C CA  1 
ATOM   12292 C  C   . SER C 3  410  ? -37.474 -27.972  27.300  1.00 108.29 ?  410  SER C C   1 
ATOM   12293 O  O   . SER C 3  410  ? -37.886 -27.540  28.381  1.00 115.37 ?  410  SER C O   1 
ATOM   12294 C  CB  . SER C 3  410  ? -35.688 -29.179  28.581  1.00 109.19 ?  410  SER C CB  1 
ATOM   12295 O  OG  . SER C 3  410  ? -34.696 -30.190  28.528  1.00 106.71 ?  410  SER C OG  1 
ATOM   12296 N  N   . TRP C 3  411  ? -37.917 -27.489  26.144  1.00 73.06  ?  411  TRP C N   1 
ATOM   12297 C  CA  . TRP C 3  411  ? -38.894 -26.413  26.064  1.00 62.32  ?  411  TRP C CA  1 
ATOM   12298 C  C   . TRP C 3  411  ? -40.254 -26.973  25.675  1.00 57.43  ?  411  TRP C C   1 
ATOM   12299 O  O   . TRP C 3  411  ? -40.358 -27.818  24.780  1.00 70.55  ?  411  TRP C O   1 
ATOM   12300 C  CB  . TRP C 3  411  ? -38.460 -25.353  25.051  1.00 70.49  ?  411  TRP C CB  1 
ATOM   12301 C  CG  . TRP C 3  411  ? -37.280 -24.533  25.487  1.00 71.27  ?  411  TRP C CG  1 
ATOM   12302 C  CD1 . TRP C 3  411  ? -36.509 -24.729  26.596  1.00 72.66  ?  411  TRP C CD1 1 
ATOM   12303 C  CD2 . TRP C 3  411  ? -36.727 -23.399  24.809  1.00 70.91  ?  411  TRP C CD2 1 
ATOM   12304 N  NE1 . TRP C 3  411  ? -35.517 -23.779  26.656  1.00 76.09  ?  411  TRP C NE1 1 
ATOM   12305 C  CE2 . TRP C 3  411  ? -35.629 -22.951  25.570  1.00 70.32  ?  411  TRP C CE2 1 
ATOM   12306 C  CE3 . TRP C 3  411  ? -37.057 -22.716  23.636  1.00 67.50  ?  411  TRP C CE3 1 
ATOM   12307 C  CZ2 . TRP C 3  411  ? -34.859 -21.854  25.194  1.00 66.19  ?  411  TRP C CZ2 1 
ATOM   12308 C  CZ3 . TRP C 3  411  ? -36.292 -21.628  23.265  1.00 68.30  ?  411  TRP C CZ3 1 
ATOM   12309 C  CH2 . TRP C 3  411  ? -35.206 -21.208  24.041  1.00 70.17  ?  411  TRP C CH2 1 
ATOM   12310 N  N   . ASP C 3  412  ? -41.294 -26.498  26.353  1.00 41.90  ?  412  ASP C N   1 
ATOM   12311 C  CA  . ASP C 3  412  ? -42.659 -26.908  26.055  1.00 48.19  ?  412  ASP C CA  1 
ATOM   12312 C  C   . ASP C 3  412  ? -43.590 -25.811  26.554  1.00 55.04  ?  412  ASP C C   1 
ATOM   12313 O  O   . ASP C 3  412  ? -43.156 -24.846  27.187  1.00 63.54  ?  412  ASP C O   1 
ATOM   12314 C  CB  . ASP C 3  412  ? -42.983 -28.267  26.690  1.00 55.24  ?  412  ASP C CB  1 
ATOM   12315 C  CG  . ASP C 3  412  ? -44.249 -28.890  26.128  1.00 60.62  ?  412  ASP C CG  1 
ATOM   12316 O  OD1 . ASP C 3  412  ? -44.204 -29.403  24.990  1.00 60.36  ?  412  ASP C OD1 1 
ATOM   12317 O  OD2 . ASP C 3  412  ? -45.287 -28.865  26.821  1.00 67.66  -1 412  ASP C OD2 1 
ATOM   12318 N  N   . ILE C 3  413  ? -44.877 -25.964  26.255  1.00 60.99  ?  413  ILE C N   1 
ATOM   12319 C  CA  . ILE C 3  413  ? -45.884 -24.974  26.616  1.00 63.94  ?  413  ILE C CA  1 
ATOM   12320 C  C   . ILE C 3  413  ? -46.794 -25.559  27.689  1.00 72.40  ?  413  ILE C C   1 
ATOM   12321 O  O   . ILE C 3  413  ? -47.039 -26.771  27.735  1.00 66.02  ?  413  ILE C O   1 
ATOM   12322 C  CB  . ILE C 3  413  ? -46.693 -24.514  25.383  1.00 65.27  ?  413  ILE C CB  1 
ATOM   12323 C  CG1 . ILE C 3  413  ? -47.528 -23.275  25.712  1.00 77.05  ?  413  ILE C CG1 1 
ATOM   12324 C  CG2 . ILE C 3  413  ? -47.578 -25.639  24.864  1.00 58.52  ?  413  ILE C CG2 1 
ATOM   12325 C  CD1 . ILE C 3  413  ? -48.247 -22.688  24.518  1.00 90.02  ?  413  ILE C CD1 1 
ATOM   12326 N  N   . TYR C 3  414  ? -47.281 -24.687  28.570  1.00 92.17  ?  414  TYR C N   1 
ATOM   12327 C  CA  . TYR C 3  414  ? -48.180 -25.063  29.655  1.00 89.74  ?  414  TYR C CA  1 
ATOM   12328 C  C   . TYR C 3  414  ? -49.588 -24.587  29.321  1.00 91.71  ?  414  TYR C C   1 
ATOM   12329 O  O   . TYR C 3  414  ? -49.820 -23.382  29.174  1.00 94.53  ?  414  TYR C O   1 
ATOM   12330 C  CB  . TYR C 3  414  ? -47.718 -24.466  30.985  1.00 85.86  ?  414  TYR C CB  1 
ATOM   12331 C  CG  . TYR C 3  414  ? -48.702 -24.667  32.117  1.00 85.76  ?  414  TYR C CG  1 
ATOM   12332 C  CD1 . TYR C 3  414  ? -48.813 -25.893  32.759  1.00 88.86  ?  414  TYR C CD1 1 
ATOM   12333 C  CD2 . TYR C 3  414  ? -49.527 -23.631  32.538  1.00 88.22  ?  414  TYR C CD2 1 
ATOM   12334 C  CE1 . TYR C 3  414  ? -49.713 -26.081  33.793  1.00 84.79  ?  414  TYR C CE1 1 
ATOM   12335 C  CE2 . TYR C 3  414  ? -50.431 -23.810  33.569  1.00 90.62  ?  414  TYR C CE2 1 
ATOM   12336 C  CZ  . TYR C 3  414  ? -50.519 -25.037  34.193  1.00 87.81  ?  414  TYR C CZ  1 
ATOM   12337 O  OH  . TYR C 3  414  ? -51.416 -25.221  35.220  1.00 92.01  ?  414  TYR C OH  1 
ATOM   12338 N  N   . ILE C 3  415  ? -50.519 -25.528  29.207  1.00 91.57  ?  415  ILE C N   1 
ATOM   12339 C  CA  . ILE C 3  415  ? -51.922 -25.207  28.954  1.00 90.40  ?  415  ILE C CA  1 
ATOM   12340 C  C   . ILE C 3  415  ? -52.766 -25.770  30.091  1.00 93.09  ?  415  ILE C C   1 
ATOM   12341 O  O   . ILE C 3  415  ? -52.889 -26.997  30.221  1.00 93.90  ?  415  ILE C O   1 
ATOM   12342 C  CB  . ILE C 3  415  ? -52.386 -25.754  27.594  1.00 94.48  ?  415  ILE C CB  1 
ATOM   12343 C  CG1 . ILE C 3  415  ? -51.376 -25.399  26.499  1.00 93.93  ?  415  ILE C CG1 1 
ATOM   12344 C  CG2 . ILE C 3  415  ? -53.767 -25.216  27.250  1.00 92.15  ?  415  ILE C CG2 1 
ATOM   12345 C  CD1 . ILE C 3  415  ? -51.654 -26.071  25.172  1.00 97.73  ?  415  ILE C CD1 1 
ATOM   12346 N  N   . PRO C 3  416  ? -53.359 -24.925  30.933  1.00 89.49  ?  416  PRO C N   1 
ATOM   12347 C  CA  . PRO C 3  416  ? -54.156 -25.438  32.053  1.00 84.93  ?  416  PRO C CA  1 
ATOM   12348 C  C   . PRO C 3  416  ? -55.406 -26.159  31.571  1.00 86.23  ?  416  PRO C C   1 
ATOM   12349 O  O   . PRO C 3  416  ? -55.937 -25.881  30.493  1.00 91.56  ?  416  PRO C O   1 
ATOM   12350 C  CB  . PRO C 3  416  ? -54.511 -24.173  32.845  1.00 81.25  ?  416  PRO C CB  1 
ATOM   12351 C  CG  . PRO C 3  416  ? -54.416 -23.065  31.845  1.00 90.11  ?  416  PRO C CG  1 
ATOM   12352 C  CD  . PRO C 3  416  ? -53.310 -23.454  30.911  1.00 91.08  ?  416  PRO C CD  1 
ATOM   12353 N  N   . THR C 3  417  ? -55.869 -27.103  32.386  1.00 64.94  ?  417  THR C N   1 
ATOM   12354 C  CA  . THR C 3  417  ? -57.037 -27.901  32.043  1.00 76.69  ?  417  THR C CA  1 
ATOM   12355 C  C   . THR C 3  417  ? -58.277 -27.277  32.688  1.00 80.02  ?  417  THR C C   1 
ATOM   12356 O  O   . THR C 3  417  ? -58.267 -26.113  33.096  1.00 78.78  ?  417  THR C O   1 
ATOM   12357 C  CB  . THR C 3  417  ? -56.823 -29.358  32.474  1.00 76.59  ?  417  THR C CB  1 
ATOM   12358 O  OG1 . THR C 3  417  ? -56.613 -29.418  33.890  1.00 73.21  ?  417  THR C OG1 1 
ATOM   12359 C  CG2 . THR C 3  417  ? -55.604 -29.948  31.770  1.00 80.16  ?  417  THR C CG2 1 
ATOM   12360 N  N   . ILE C 3  418  ? -59.360 -28.048  32.790  1.00 70.12  ?  418  ILE C N   1 
ATOM   12361 C  CA  . ILE C 3  418  ? -60.576 -27.558  33.427  1.00 65.91  ?  418  ILE C CA  1 
ATOM   12362 C  C   . ILE C 3  418  ? -60.605 -27.856  34.923  1.00 65.81  ?  418  ILE C C   1 
ATOM   12363 O  O   . ILE C 3  418  ? -61.312 -27.163  35.669  1.00 71.58  ?  418  ILE C O   1 
ATOM   12364 C  CB  . ILE C 3  418  ? -61.816 -28.159  32.738  1.00 65.66  ?  418  ILE C CB  1 
ATOM   12365 C  CG1 . ILE C 3  418  ? -63.099 -27.464  33.202  1.00 54.43  ?  418  ILE C CG1 1 
ATOM   12366 C  CG2 . ILE C 3  418  ? -61.894 -29.657  32.980  1.00 73.77  ?  418  ILE C CG2 1 
ATOM   12367 C  CD1 . ILE C 3  418  ? -64.328 -27.892  32.429  1.00 62.25  ?  418  ILE C CD1 1 
ATOM   12368 N  N   . TRP C 3  419  ? -59.833 -28.839  35.387  1.00 79.02  ?  419  TRP C N   1 
ATOM   12369 C  CA  . TRP C 3  419  ? -59.946 -29.278  36.773  1.00 88.01  ?  419  TRP C CA  1 
ATOM   12370 C  C   . TRP C 3  419  ? -59.264 -28.313  37.736  1.00 92.47  ?  419  TRP C C   1 
ATOM   12371 O  O   . TRP C 3  419  ? -59.766 -28.085  38.843  1.00 96.86  ?  419  TRP C O   1 
ATOM   12372 C  CB  . TRP C 3  419  ? -59.373 -30.686  36.917  1.00 83.98  ?  419  TRP C CB  1 
ATOM   12373 C  CG  . TRP C 3  419  ? -60.202 -31.710  36.213  1.00 82.02  ?  419  TRP C CG  1 
ATOM   12374 C  CD1 . TRP C 3  419  ? -59.908 -32.340  35.039  1.00 85.07  ?  419  TRP C CD1 1 
ATOM   12375 C  CD2 . TRP C 3  419  ? -61.479 -32.209  36.627  1.00 83.99  ?  419  TRP C CD2 1 
ATOM   12376 N  NE1 . TRP C 3  419  ? -60.917 -33.210  34.702  1.00 88.55  ?  419  TRP C NE1 1 
ATOM   12377 C  CE2 . TRP C 3  419  ? -61.894 -33.147  35.661  1.00 89.12  ?  419  TRP C CE2 1 
ATOM   12378 C  CE3 . TRP C 3  419  ? -62.309 -31.957  37.724  1.00 80.14  ?  419  TRP C CE3 1 
ATOM   12379 C  CZ2 . TRP C 3  419  ? -63.103 -33.834  35.758  1.00 85.95  ?  419  TRP C CZ2 1 
ATOM   12380 C  CZ3 . TRP C 3  419  ? -63.508 -32.640  37.819  1.00 84.66  ?  419  TRP C CZ3 1 
ATOM   12381 C  CH2 . TRP C 3  419  ? -63.893 -33.568  36.843  1.00 89.52  ?  419  TRP C CH2 1 
ATOM   12382 N  N   . ASP C 3  420  ? -58.124 -27.739  37.342  1.00 114.32 ?  420  ASP C N   1 
ATOM   12383 C  CA  . ASP C 3  420  ? -57.486 -26.742  38.197  1.00 123.10 ?  420  ASP C CA  1 
ATOM   12384 C  C   . ASP C 3  420  ? -58.302 -25.457  38.253  1.00 121.51 ?  420  ASP C C   1 
ATOM   12385 O  O   . ASP C 3  420  ? -58.304 -24.771  39.282  1.00 123.76 ?  420  ASP C O   1 
ATOM   12386 C  CB  . ASP C 3  420  ? -56.063 -26.457  37.717  1.00 119.11 ?  420  ASP C CB  1 
ATOM   12387 C  CG  . ASP C 3  420  ? -55.985 -26.219  36.225  1.00 116.51 ?  420  ASP C CG  1 
ATOM   12388 O  OD1 . ASP C 3  420  ? -57.046 -26.218  35.568  1.00 119.00 ?  420  ASP C OD1 1 
ATOM   12389 O  OD2 . ASP C 3  420  ? -54.862 -26.034  35.712  1.00 119.42 -1 420  ASP C OD2 1 
ATOM   12390 N  N   . TRP C 3  421  ? -58.992 -25.114  37.163  1.00 77.10  ?  421  TRP C N   1 
ATOM   12391 C  CA  . TRP C 3  421  ? -59.967 -24.029  37.219  1.00 77.44  ?  421  TRP C CA  1 
ATOM   12392 C  C   . TRP C 3  421  ? -61.099 -24.370  38.179  1.00 78.48  ?  421  TRP C C   1 
ATOM   12393 O  O   . TRP C 3  421  ? -61.482 -23.552  39.022  1.00 82.30  ?  421  TRP C O   1 
ATOM   12394 C  CB  . TRP C 3  421  ? -60.518 -23.738  35.822  1.00 76.11  ?  421  TRP C CB  1 
ATOM   12395 C  CG  . TRP C 3  421  ? -59.632 -22.875  34.976  1.00 74.11  ?  421  TRP C CG  1 
ATOM   12396 C  CD1 . TRP C 3  421  ? -59.065 -23.207  33.781  1.00 72.40  ?  421  TRP C CD1 1 
ATOM   12397 C  CD2 . TRP C 3  421  ? -59.231 -21.526  35.250  1.00 76.35  ?  421  TRP C CD2 1 
ATOM   12398 N  NE1 . TRP C 3  421  ? -58.325 -22.154  33.299  1.00 76.47  ?  421  TRP C NE1 1 
ATOM   12399 C  CE2 . TRP C 3  421  ? -58.412 -21.109  34.182  1.00 74.63  ?  421  TRP C CE2 1 
ATOM   12400 C  CE3 . TRP C 3  421  ? -59.481 -20.632  36.297  1.00 75.70  ?  421  TRP C CE3 1 
ATOM   12401 C  CZ2 . TRP C 3  421  ? -57.840 -19.839  34.131  1.00 70.84  ?  421  TRP C CZ2 1 
ATOM   12402 C  CZ3 . TRP C 3  421  ? -58.912 -19.372  36.244  1.00 76.19  ?  421  TRP C CZ3 1 
ATOM   12403 C  CH2 . TRP C 3  421  ? -58.102 -18.987  35.169  1.00 70.36  ?  421  TRP C CH2 1 
ATOM   12404 N  N   . SER C 3  422  ? -61.641 -25.587  38.068  1.00 76.33  ?  422  SER C N   1 
ATOM   12405 C  CA  . SER C 3  422  ? -62.697 -26.020  38.978  1.00 76.08  ?  422  SER C CA  1 
ATOM   12406 C  C   . SER C 3  422  ? -62.247 -25.922  40.430  1.00 84.61  ?  422  SER C C   1 
ATOM   12407 O  O   . SER C 3  422  ? -63.037 -25.560  41.310  1.00 85.33  ?  422  SER C O   1 
ATOM   12408 C  CB  . SER C 3  422  ? -63.120 -27.449  38.640  1.00 70.16  ?  422  SER C CB  1 
ATOM   12409 O  OG  . SER C 3  422  ? -63.612 -27.534  37.315  1.00 86.15  ?  422  SER C OG  1 
ATOM   12410 N  N   . LEU C 3  423  ? -60.976 -26.233  40.699  1.00 83.42  ?  423  LEU C N   1 
ATOM   12411 C  CA  . LEU C 3  423  ? -60.437 -26.051  42.042  1.00 74.40  ?  423  LEU C CA  1 
ATOM   12412 C  C   . LEU C 3  423  ? -60.378 -24.581  42.431  1.00 74.03  ?  423  LEU C C   1 
ATOM   12413 O  O   . LEU C 3  423  ? -60.544 -24.247  43.609  1.00 77.57  ?  423  LEU C O   1 
ATOM   12414 C  CB  . LEU C 3  423  ? -59.046 -26.674  42.143  1.00 70.98  ?  423  LEU C CB  1 
ATOM   12415 C  CG  . LEU C 3  423  ? -58.969 -28.090  42.710  1.00 74.80  ?  423  LEU C CG  1 
ATOM   12416 C  CD1 . LEU C 3  423  ? -57.539 -28.597  42.671  1.00 80.92  ?  423  LEU C CD1 1 
ATOM   12417 C  CD2 . LEU C 3  423  ? -59.512 -28.125  44.128  1.00 70.88  ?  423  LEU C CD2 1 
ATOM   12418 N  N   . TYR C 3  424  ? -60.144 -23.693  41.463  1.00 98.86  ?  424  TYR C N   1 
ATOM   12419 C  CA  . TYR C 3  424  ? -60.058 -22.267  41.764  1.00 100.12 ?  424  TYR C CA  1 
ATOM   12420 C  C   . TYR C 3  424  ? -61.414 -21.711  42.184  1.00 99.03  ?  424  TYR C C   1 
ATOM   12421 O  O   . TYR C 3  424  ? -61.549 -21.120  43.261  1.00 105.21 ?  424  TYR C O   1 
ATOM   12422 C  CB  . TYR C 3  424  ? -59.510 -21.509  40.554  1.00 105.14 ?  424  TYR C CB  1 
ATOM   12423 C  CG  . TYR C 3  424  ? -58.918 -20.160  40.891  1.00 99.59  ?  424  TYR C CG  1 
ATOM   12424 C  CD1 . TYR C 3  424  ? -58.291 -19.940  42.110  1.00 89.05  ?  424  TYR C CD1 1 
ATOM   12425 C  CD2 . TYR C 3  424  ? -58.983 -19.107  39.988  1.00 100.72 ?  424  TYR C CD2 1 
ATOM   12426 C  CE1 . TYR C 3  424  ? -57.746 -18.709  42.421  1.00 96.49  ?  424  TYR C CE1 1 
ATOM   12427 C  CE2 . TYR C 3  424  ? -58.442 -17.873  40.290  1.00 99.62  ?  424  TYR C CE2 1 
ATOM   12428 C  CZ  . TYR C 3  424  ? -57.825 -17.680  41.507  1.00 99.10  ?  424  TYR C CZ  1 
ATOM   12429 O  OH  . TYR C 3  424  ? -57.286 -16.451  41.808  1.00 102.86 ?  424  TYR C OH  1 
ATOM   12430 N  N   . ILE C 3  425  ? -62.432 -21.883  41.334  1.00 50.70  ?  425  ILE C N   1 
ATOM   12431 C  CA  . ILE C 3  425  ? -63.790 -21.487  41.706  1.00 52.19  ?  425  ILE C CA  1 
ATOM   12432 C  C   . ILE C 3  425  ? -64.217 -22.180  42.996  1.00 55.81  ?  425  ILE C C   1 
ATOM   12433 O  O   . ILE C 3  425  ? -64.897 -21.588  43.844  1.00 55.45  ?  425  ILE C O   1 
ATOM   12434 C  CB  . ILE C 3  425  ? -64.775 -21.770  40.551  1.00 41.25  ?  425  ILE C CB  1 
ATOM   12435 C  CG1 . ILE C 3  425  ? -64.519 -20.845  39.351  1.00 50.36  ?  425  ILE C CG1 1 
ATOM   12436 C  CG2 . ILE C 3  425  ? -66.220 -21.658  41.026  1.00 45.31  ?  425  ILE C CG2 1 
ATOM   12437 C  CD1 . ILE C 3  425  ? -63.489 -21.324  38.368  1.00 57.29  ?  425  ILE C CD1 1 
ATOM   12438 N  N   . GLY C 3  426  ? -63.811 -23.438  43.175  1.00 73.55  ?  426  GLY C N   1 
ATOM   12439 C  CA  . GLY C 3  426  ? -64.145 -24.139  44.403  1.00 71.73  ?  426  GLY C CA  1 
ATOM   12440 C  C   . GLY C 3  426  ? -63.536 -23.495  45.634  1.00 80.86  ?  426  GLY C C   1 
ATOM   12441 O  O   . GLY C 3  426  ? -64.172 -23.424  46.689  1.00 87.56  ?  426  GLY C O   1 
ATOM   12442 N  N   . THR C 3  427  ? -62.294 -23.015  45.519  1.00 92.26  ?  427  THR C N   1 
ATOM   12443 C  CA  . THR C 3  427  ? -61.665 -22.332  46.645  1.00 90.63  ?  427  THR C CA  1 
ATOM   12444 C  C   . THR C 3  427  ? -62.337 -20.994  46.923  1.00 93.68  ?  427  THR C C   1 
ATOM   12445 O  O   . THR C 3  427  ? -62.440 -20.574  48.081  1.00 99.53  ?  427  THR C O   1 
ATOM   12446 C  CB  . THR C 3  427  ? -60.172 -22.135  46.383  1.00 87.08  ?  427  THR C CB  1 
ATOM   12447 O  OG1 . THR C 3  427  ? -59.977 -21.647  45.049  1.00 91.59  ?  427  THR C OG1 1 
ATOM   12448 C  CG2 . THR C 3  427  ? -59.421 -23.449  46.563  1.00 90.44  ?  427  THR C CG2 1 
ATOM   12449 N  N   . PHE C 3  428  ? -62.794 -20.305  45.873  1.00 85.66  ?  428  PHE C N   1 
ATOM   12450 C  CA  . PHE C 3  428  ? -63.575 -19.090  46.076  1.00 87.25  ?  428  PHE C CA  1 
ATOM   12451 C  C   . PHE C 3  428  ? -64.853 -19.386  46.850  1.00 94.23  ?  428  PHE C C   1 
ATOM   12452 O  O   . PHE C 3  428  ? -65.250 -18.613  47.730  1.00 95.72  ?  428  PHE C O   1 
ATOM   12453 C  CB  . PHE C 3  428  ? -63.906 -18.442  44.731  1.00 77.61  ?  428  PHE C CB  1 
ATOM   12454 C  CG  . PHE C 3  428  ? -62.801 -17.587  44.176  1.00 78.08  ?  428  PHE C CG  1 
ATOM   12455 C  CD1 . PHE C 3  428  ? -62.581 -16.311  44.667  1.00 77.83  ?  428  PHE C CD1 1 
ATOM   12456 C  CD2 . PHE C 3  428  ? -61.991 -18.055  43.154  1.00 85.88  ?  428  PHE C CD2 1 
ATOM   12457 C  CE1 . PHE C 3  428  ? -61.568 -15.521  44.155  1.00 81.84  ?  428  PHE C CE1 1 
ATOM   12458 C  CE2 . PHE C 3  428  ? -60.977 -17.269  42.639  1.00 82.87  ?  428  PHE C CE2 1 
ATOM   12459 C  CZ  . PHE C 3  428  ? -60.766 -16.000  43.140  1.00 82.57  ?  428  PHE C CZ  1 
ATOM   12460 N  N   . GLY C 3  429  ? -65.505 -20.509  46.544  1.00 84.77  ?  429  GLY C N   1 
ATOM   12461 C  CA  . GLY C 3  429  ? -66.747 -20.840  47.223  1.00 85.93  ?  429  GLY C CA  1 
ATOM   12462 C  C   . GLY C 3  429  ? -66.547 -21.199  48.682  1.00 81.66  ?  429  GLY C C   1 
ATOM   12463 O  O   . GLY C 3  429  ? -67.342 -20.807  49.539  1.00 85.89  ?  429  GLY C O   1 
ATOM   12464 N  N   . LEU C 3  430  ? -65.490 -21.956  48.985  1.00 80.68  ?  430  LEU C N   1 
ATOM   12465 C  CA  . LEU C 3  430  ? -65.184 -22.262  50.378  1.00 86.43  ?  430  LEU C CA  1 
ATOM   12466 C  C   . LEU C 3  430  ? -64.820 -20.998  51.146  1.00 83.75  ?  430  LEU C C   1 
ATOM   12467 O  O   . LEU C 3  430  ? -65.210 -20.833  52.308  1.00 84.67  ?  430  LEU C O   1 
ATOM   12468 C  CB  . LEU C 3  430  ? -64.050 -23.285  50.454  1.00 77.88  ?  430  LEU C CB  1 
ATOM   12469 C  CG  . LEU C 3  430  ? -63.365 -23.428  51.814  1.00 64.45  ?  430  LEU C CG  1 
ATOM   12470 C  CD1 . LEU C 3  430  ? -64.185 -24.324  52.729  1.00 72.90  ?  430  LEU C CD1 1 
ATOM   12471 C  CD2 . LEU C 3  430  ? -61.951 -23.961  51.657  1.00 69.09  ?  430  LEU C CD2 1 
ATOM   12472 N  N   . PHE C 3  431  ? -64.073 -20.094  50.507  1.00 76.05  ?  431  PHE C N   1 
ATOM   12473 C  CA  . PHE C 3  431  ? -63.735 -18.818  51.131  1.00 74.14  ?  431  PHE C CA  1 
ATOM   12474 C  C   . PHE C 3  431  ? -64.988 -18.020  51.464  1.00 78.07  ?  431  PHE C C   1 
ATOM   12475 O  O   . PHE C 3  431  ? -65.125 -17.487  52.572  1.00 79.43  ?  431  PHE C O   1 
ATOM   12476 C  CB  . PHE C 3  431  ? -62.816 -18.017  50.206  1.00 77.31  ?  431  PHE C CB  1 
ATOM   12477 C  CG  . PHE C 3  431  ? -62.488 -16.643  50.716  1.00 69.75  ?  431  PHE C CG  1 
ATOM   12478 C  CD1 . PHE C 3  431  ? -61.759 -16.473  51.880  1.00 73.21  ?  431  PHE C CD1 1 
ATOM   12479 C  CD2 . PHE C 3  431  ? -62.912 -15.519  50.027  1.00 72.75  ?  431  PHE C CD2 1 
ATOM   12480 C  CE1 . PHE C 3  431  ? -61.459 -15.206  52.348  1.00 78.76  ?  431  PHE C CE1 1 
ATOM   12481 C  CE2 . PHE C 3  431  ? -62.616 -14.252  50.489  1.00 74.73  ?  431  PHE C CE2 1 
ATOM   12482 C  CZ  . PHE C 3  431  ? -61.889 -14.095  51.651  1.00 78.07  ?  431  PHE C CZ  1 
ATOM   12483 N  N   . PHE C 3  432  ? -65.921 -17.930  50.513  1.00 89.82  ?  432  PHE C N   1 
ATOM   12484 C  CA  . PHE C 3  432  ? -67.122 -17.132  50.725  1.00 91.72  ?  432  PHE C CA  1 
ATOM   12485 C  C   . PHE C 3  432  ? -68.118 -17.827  51.644  1.00 95.07  ?  432  PHE C C   1 
ATOM   12486 O  O   . PHE C 3  432  ? -68.876 -17.152  52.349  1.00 98.33  ?  432  PHE C O   1 
ATOM   12487 C  CB  . PHE C 3  432  ? -67.774 -16.806  49.380  1.00 87.14  ?  432  PHE C CB  1 
ATOM   12488 C  CG  . PHE C 3  432  ? -67.126 -15.657  48.661  1.00 85.50  ?  432  PHE C CG  1 
ATOM   12489 C  CD1 . PHE C 3  432  ? -67.085 -14.400  49.237  1.00 80.18  ?  432  PHE C CD1 1 
ATOM   12490 C  CD2 . PHE C 3  432  ? -66.549 -15.838  47.415  1.00 90.15  ?  432  PHE C CD2 1 
ATOM   12491 C  CE1 . PHE C 3  432  ? -66.488 -13.344  48.582  1.00 79.84  ?  432  PHE C CE1 1 
ATOM   12492 C  CE2 . PHE C 3  432  ? -65.949 -14.786  46.755  1.00 90.63  ?  432  PHE C CE2 1 
ATOM   12493 C  CZ  . PHE C 3  432  ? -65.918 -13.536  47.340  1.00 86.34  ?  432  PHE C CZ  1 
ATOM   12494 N  N   . THR C 3  433  ? -68.133 -19.161  51.653  1.00 90.14  ?  433  THR C N   1 
ATOM   12495 C  CA  . THR C 3  433  ? -68.963 -19.884  52.612  1.00 84.89  ?  433  THR C CA  1 
ATOM   12496 C  C   . THR C 3  433  ? -68.528 -19.577  54.039  1.00 85.22  ?  433  THR C C   1 
ATOM   12497 O  O   . THR C 3  433  ? -69.361 -19.308  54.913  1.00 94.21  ?  433  THR C O   1 
ATOM   12498 C  CB  . THR C 3  433  ? -68.897 -21.390  52.345  1.00 83.00  ?  433  THR C CB  1 
ATOM   12499 O  OG1 . THR C 3  433  ? -69.465 -21.683  51.063  1.00 86.67  ?  433  THR C OG1 1 
ATOM   12500 C  CG2 . THR C 3  433  ? -69.653 -22.163  53.418  1.00 82.50  ?  433  THR C CG2 1 
ATOM   12501 N  N   . LEU C 3  434  ? -67.218 -19.609  54.291  1.00 75.75  ?  434  LEU C N   1 
ATOM   12502 C  CA  . LEU C 3  434  ? -66.710 -19.314  55.626  1.00 76.46  ?  434  LEU C CA  1 
ATOM   12503 C  C   . LEU C 3  434  ? -66.955 -17.858  56.003  1.00 74.75  ?  434  LEU C C   1 
ATOM   12504 O  O   . LEU C 3  434  ? -67.215 -17.550  57.172  1.00 82.24  ?  434  LEU C O   1 
ATOM   12505 C  CB  . LEU C 3  434  ? -65.221 -19.651  55.701  1.00 74.49  ?  434  LEU C CB  1 
ATOM   12506 C  CG  . LEU C 3  434  ? -64.849 -20.984  56.354  1.00 62.59  ?  434  LEU C CG  1 
ATOM   12507 C  CD1 . LEU C 3  434  ? -65.566 -22.142  55.681  1.00 61.13  ?  434  LEU C CD1 1 
ATOM   12508 C  CD2 . LEU C 3  434  ? -63.345 -21.194  56.308  1.00 62.48  ?  434  LEU C CD2 1 
ATOM   12509 N  N   . LEU C 3  435  ? -66.880 -16.947  55.029  1.00 69.40  ?  435  LEU C N   1 
ATOM   12510 C  CA  . LEU C 3  435  ? -67.140 -15.539  55.316  1.00 79.23  ?  435  LEU C CA  1 
ATOM   12511 C  C   . LEU C 3  435  ? -68.611 -15.299  55.633  1.00 83.79  ?  435  LEU C C   1 
ATOM   12512 O  O   . LEU C 3  435  ? -68.936 -14.529  56.543  1.00 88.37  ?  435  LEU C O   1 
ATOM   12513 C  CB  . LEU C 3  435  ? -66.699 -14.669  54.140  1.00 80.18  ?  435  LEU C CB  1 
ATOM   12514 C  CG  . LEU C 3  435  ? -65.382 -13.912  54.309  1.00 77.69  ?  435  LEU C CG  1 
ATOM   12515 C  CD1 . LEU C 3  435  ? -65.039 -13.152  53.040  1.00 70.69  ?  435  LEU C CD1 1 
ATOM   12516 C  CD2 . LEU C 3  435  ? -65.453 -12.969  55.500  1.00 71.55  ?  435  LEU C CD2 1 
ATOM   12517 N  N   . PHE C 3  436  ? -69.513 -15.945  54.890  1.00 71.34  ?  436  PHE C N   1 
ATOM   12518 C  CA  . PHE C 3  436  ? -70.941 -15.780  55.148  1.00 75.04  ?  436  PHE C CA  1 
ATOM   12519 C  C   . PHE C 3  436  ? -71.333 -16.366  56.499  1.00 76.87  ?  436  PHE C C   1 
ATOM   12520 O  O   . PHE C 3  436  ? -72.202 -15.820  57.188  1.00 77.85  ?  436  PHE C O   1 
ATOM   12521 C  CB  . PHE C 3  436  ? -71.754 -16.421  54.024  1.00 77.97  ?  436  PHE C CB  1 
ATOM   12522 C  CG  . PHE C 3  436  ? -72.104 -15.473  52.914  1.00 75.80  ?  436  PHE C CG  1 
ATOM   12523 C  CD1 . PHE C 3  436  ? -73.268 -14.728  52.963  1.00 83.26  ?  436  PHE C CD1 1 
ATOM   12524 C  CD2 . PHE C 3  436  ? -71.262 -15.320  51.825  1.00 64.57  ?  436  PHE C CD2 1 
ATOM   12525 C  CE1 . PHE C 3  436  ? -73.592 -13.855  51.944  1.00 78.82  ?  436  PHE C CE1 1 
ATOM   12526 C  CE2 . PHE C 3  436  ? -71.579 -14.447  50.804  1.00 61.75  ?  436  PHE C CE2 1 
ATOM   12527 C  CZ  . PHE C 3  436  ? -72.745 -13.712  50.864  1.00 62.37  ?  436  PHE C CZ  1 
ATOM   12528 N  N   . LEU C 3  437  ? -70.708 -17.480  56.895  1.00 99.88  ?  437  LEU C N   1 
ATOM   12529 C  CA  . LEU C 3  437  ? -70.956 -18.027  58.225  1.00 102.07 ?  437  LEU C CA  1 
ATOM   12530 C  C   . LEU C 3  437  ? -70.406 -17.117  59.316  1.00 101.15 ?  437  LEU C C   1 
ATOM   12531 O  O   . LEU C 3  437  ? -70.988 -17.032  60.403  1.00 106.69 ?  437  LEU C O   1 
ATOM   12532 C  CB  . LEU C 3  437  ? -70.346 -19.425  58.347  1.00 101.98 ?  437  LEU C CB  1 
ATOM   12533 C  CG  . LEU C 3  437  ? -70.930 -20.515  57.450  1.00 98.41  ?  437  LEU C CG  1 
ATOM   12534 C  CD1 . LEU C 3  437  ? -70.303 -21.860  57.778  1.00 102.53 ?  437  LEU C CD1 1 
ATOM   12535 C  CD2 . LEU C 3  437  ? -72.444 -20.567  57.583  1.00 97.95  ?  437  LEU C CD2 1 
ATOM   12536 N  N   . PHE C 3  438  ? -69.294 -16.433  59.047  1.00 95.80  ?  438  PHE C N   1 
ATOM   12537 C  CA  . PHE C 3  438  ? -68.714 -15.537  60.043  1.00 97.99  ?  438  PHE C CA  1 
ATOM   12538 C  C   . PHE C 3  438  ? -69.592 -14.311  60.258  1.00 95.09  ?  438  PHE C C   1 
ATOM   12539 O  O   . PHE C 3  438  ? -69.856 -13.916  61.399  1.00 99.00  ?  438  PHE C O   1 
ATOM   12540 C  CB  . PHE C 3  438  ? -67.303 -15.128  59.616  1.00 100.82 ?  438  PHE C CB  1 
ATOM   12541 C  CG  . PHE C 3  438  ? -66.877 -13.776  60.124  1.00 102.39 ?  438  PHE C CG  1 
ATOM   12542 C  CD1 . PHE C 3  438  ? -66.574 -13.583  61.462  1.00 102.23 ?  438  PHE C CD1 1 
ATOM   12543 C  CD2 . PHE C 3  438  ? -66.776 -12.700  59.257  1.00 104.34 ?  438  PHE C CD2 1 
ATOM   12544 C  CE1 . PHE C 3  438  ? -66.183 -12.339  61.925  1.00 96.12  ?  438  PHE C CE1 1 
ATOM   12545 C  CE2 . PHE C 3  438  ? -66.387 -11.456  59.715  1.00 99.67  ?  438  PHE C CE2 1 
ATOM   12546 C  CZ  . PHE C 3  438  ? -66.089 -11.276  61.050  1.00 97.48  ?  438  PHE C CZ  1 
ATOM   12547 N  N   . ILE C 3  439  ? -70.055 -13.691  59.169  1.00 118.95 ?  439  ILE C N   1 
ATOM   12548 C  CA  . ILE C 3  439  ? -70.902 -12.510  59.285  1.00 123.33 ?  439  ILE C CA  1 
ATOM   12549 C  C   . ILE C 3  439  ? -72.298 -12.837  59.790  1.00 123.78 ?  439  ILE C C   1 
ATOM   12550 O  O   . ILE C 3  439  ? -73.040 -11.922  60.162  1.00 132.29 ?  439  ILE C O   1 
ATOM   12551 C  CB  . ILE C 3  439  ? -71.002 -11.771  57.936  1.00 120.11 ?  439  ILE C CB  1 
ATOM   12552 C  CG1 . ILE C 3  439  ? -71.845 -12.576  56.944  1.00 126.55 ?  439  ILE C CG1 1 
ATOM   12553 C  CG2 . ILE C 3  439  ? -69.616 -11.482  57.383  1.00 116.68 ?  439  ILE C CG2 1 
ATOM   12554 C  CD1 . ILE C 3  439  ? -72.065 -11.878  55.620  1.00 124.17 ?  439  ILE C CD1 1 
ATOM   12555 N  N   . ARG C 3  440  ? -72.678 -14.114  59.809  1.00 102.36 ?  440  ARG C N   1 
ATOM   12556 C  CA  . ARG C 3  440  ? -73.981 -14.506  60.330  1.00 105.70 ?  440  ARG C CA  1 
ATOM   12557 C  C   . ARG C 3  440  ? -73.946 -14.799  61.824  1.00 108.34 ?  440  ARG C C   1 
ATOM   12558 O  O   . ARG C 3  440  ? -74.899 -14.472  62.540  1.00 116.44 ?  440  ARG C O   1 
ATOM   12559 C  CB  . ARG C 3  440  ? -74.508 -15.732  59.578  1.00 109.38 ?  440  ARG C CB  1 
ATOM   12560 C  CG  . ARG C 3  440  ? -75.938 -16.100  59.941  1.00 110.59 ?  440  ARG C CG  1 
ATOM   12561 C  CD  . ARG C 3  440  ? -76.868 -14.911  59.762  1.00 124.88 ?  440  ARG C CD  1 
ATOM   12562 N  NE  . ARG C 3  440  ? -78.209 -15.178  60.268  1.00 130.58 ?  440  ARG C NE  1 
ATOM   12563 C  CZ  . ARG C 3  440  ? -78.594 -14.948  61.516  1.00 125.42 ?  440  ARG C CZ  1 
ATOM   12564 N  NH1 . ARG C 3  440  ? -77.763 -14.444  62.413  1.00 123.77 ?  440  ARG C NH1 1 
ATOM   12565 N  NH2 . ARG C 3  440  ? -79.844 -15.230  61.872  1.00 129.11 ?  440  ARG C NH2 1 
ATOM   12566 N  N   . VAL C 3  441  ? -72.867 -15.403  62.311  1.00 87.94  ?  441  VAL C N   1 
ATOM   12567 C  CA  . VAL C 3  441  ? -72.782 -15.806  63.712  1.00 82.09  ?  441  VAL C CA  1 
ATOM   12568 C  C   . VAL C 3  441  ? -72.124 -14.730  64.565  1.00 82.69  ?  441  VAL C C   1 
ATOM   12569 O  O   . VAL C 3  441  ? -72.678 -14.303  65.582  1.00 90.34  ?  441  VAL C O   1 
ATOM   12570 C  CB  . VAL C 3  441  ? -72.033 -17.150  63.827  1.00 77.79  ?  441  VAL C CB  1 
ATOM   12571 C  CG1 . VAL C 3  441  ? -71.972 -17.600  65.276  1.00 79.80  ?  441  VAL C CG1 1 
ATOM   12572 C  CG2 . VAL C 3  441  ? -72.704 -18.205  62.961  1.00 79.18  ?  441  VAL C CG2 1 
ATOM   12573 N  N   . LEU C 3  442  ? -70.941 -14.274  64.171  1.00 108.84 ?  442  LEU C N   1 
ATOM   12574 C  CA  . LEU C 3  442  ? -70.146 -13.363  64.978  1.00 102.88 ?  442  LEU C CA  1 
ATOM   12575 C  C   . LEU C 3  442  ? -70.281 -11.931  64.481  1.00 108.63 ?  442  LEU C C   1 
ATOM   12576 O  O   . LEU C 3  442  ? -70.612 -11.692  63.316  1.00 120.56 ?  442  LEU C O   1 
ATOM   12577 C  CB  . LEU C 3  442  ? -68.673 -13.784  64.949  1.00 101.62 ?  442  LEU C CB  1 
ATOM   12578 C  CG  . LEU C 3  442  ? -68.397 -15.198  65.458  1.00 108.58 ?  442  LEU C CG  1 
ATOM   12579 C  CD1 . LEU C 3  442  ? -66.920 -15.547  65.325  1.00 111.34 ?  442  LEU C CD1 1 
ATOM   12580 C  CD2 . LEU C 3  442  ? -68.876 -15.356  66.892  1.00 108.45 ?  442  LEU C CD2 1 
ATOM   12581 N  N   . PRO C 3  443  ? -70.038 -10.945  65.347  1.00 90.78  ?  443  PRO C N   1 
ATOM   12582 C  CA  . PRO C 3  443  ? -70.073 -9.547   64.895  1.00 94.06  ?  443  PRO C CA  1 
ATOM   12583 C  C   . PRO C 3  443  ? -68.891 -9.243   63.986  1.00 93.77  ?  443  PRO C C   1 
ATOM   12584 O  O   . PRO C 3  443  ? -67.749 -9.596   64.289  1.00 95.53  ?  443  PRO C O   1 
ATOM   12585 C  CB  . PRO C 3  443  ? -70.004 -8.748   66.202  1.00 103.36 ?  443  PRO C CB  1 
ATOM   12586 C  CG  . PRO C 3  443  ? -69.344 -9.669   67.171  1.00 93.60  ?  443  PRO C CG  1 
ATOM   12587 C  CD  . PRO C 3  443  ? -69.778 -11.055  66.793  1.00 92.94  ?  443  PRO C CD  1 
ATOM   12588 N  N   . MET C 3  444  ? -69.176 -8.581   62.865  1.00 109.29 ?  444  MET C N   1 
ATOM   12589 C  CA  . MET C 3  444  ? -68.158 -8.299   61.861  1.00 107.54 ?  444  MET C CA  1 
ATOM   12590 C  C   . MET C 3  444  ? -67.330 -7.060   62.174  1.00 110.45 ?  444  MET C C   1 
ATOM   12591 O  O   . MET C 3  444  ? -66.318 -6.828   61.502  1.00 106.19 ?  444  MET C O   1 
ATOM   12592 C  CB  . MET C 3  444  ? -68.811 -8.147   60.487  1.00 102.96 ?  444  MET C CB  1 
ATOM   12593 C  CG  . MET C 3  444  ? -69.776 -6.981   60.388  1.00 110.43 ?  444  MET C CG  1 
ATOM   12594 S  SD  . MET C 3  444  ? -70.649 -6.960   58.814  1.00 131.47 ?  444  MET C SD  1 
ATOM   12595 C  CE  . MET C 3  444  ? -71.770 -8.337   59.037  1.00 124.26 ?  444  MET C CE  1 
ATOM   12596 N  N   . ILE C 3  445  ? -67.727 -6.261   63.161  1.00 94.40  ?  445  ILE C N   1 
ATOM   12597 C  CA  . ILE C 3  445  ? -66.968 -5.093   63.591  1.00 85.39  ?  445  ILE C CA  1 
ATOM   12598 C  C   . ILE C 3  445  ? -66.667 -5.248   65.073  1.00 90.82  ?  445  ILE C C   1 
ATOM   12599 O  O   . ILE C 3  445  ? -67.566 -5.561   65.863  1.00 99.33  ?  445  ILE C O   1 
ATOM   12600 C  CB  . ILE C 3  445  ? -67.728 -3.782   63.319  1.00 93.20  ?  445  ILE C CB  1 
ATOM   12601 C  CG1 . ILE C 3  445  ? -67.923 -3.577   61.817  1.00 94.46  ?  445  ILE C CG1 1 
ATOM   12602 C  CG2 . ILE C 3  445  ? -66.981 -2.599   63.913  1.00 95.53  ?  445  ILE C CG2 1 
ATOM   12603 C  CD1 . ILE C 3  445  ? -68.847 -2.426   61.477  1.00 94.69  ?  445  ILE C CD1 1 
ATOM   12604 N  N   . ASN C 3  446  ? -65.406 -5.042   65.446  1.00 101.11 ?  446  ASN C N   1 
ATOM   12605 C  CA  . ASN C 3  446  ? -65.005 -5.155   66.842  1.00 104.34 ?  446  ASN C CA  1 
ATOM   12606 C  C   . ASN C 3  446  ? -65.684 -4.060   67.656  1.00 108.79 ?  446  ASN C C   1 
ATOM   12607 O  O   . ASN C 3  446  ? -65.493 -2.870   67.389  1.00 111.79 ?  446  ASN C O   1 
ATOM   12608 C  CB  . ASN C 3  446  ? -63.486 -5.068   66.962  1.00 104.63 ?  446  ASN C CB  1 
ATOM   12609 C  CG  . ASN C 3  446  ? -62.977 -5.600   68.284  1.00 105.55 ?  446  ASN C CG  1 
ATOM   12610 O  OD1 . ASN C 3  446  ? -63.759 -5.957   69.164  1.00 113.02 ?  446  ASN C OD1 1 
ATOM   12611 N  ND2 . ASN C 3  446  ? -61.659 -5.679   68.422  1.00 97.95  ?  446  ASN C ND2 1 
ATOM   12612 N  N   . ILE C 3  447  ? -66.477 -4.464   68.649  1.00 90.49  ?  447  ILE C N   1 
ATOM   12613 C  CA  . ILE C 3  447  ? -67.370 -3.525   69.322  1.00 94.28  ?  447  ILE C CA  1 
ATOM   12614 C  C   . ILE C 3  447  ? -66.621 -2.710   70.369  1.00 99.38  ?  447  ILE C C   1 
ATOM   12615 O  O   . ILE C 3  447  ? -66.699 -1.475   70.382  1.00 100.14 ?  447  ILE C O   1 
ATOM   12616 C  CB  . ILE C 3  447  ? -68.564 -4.277   69.937  1.00 89.18  ?  447  ILE C CB  1 
ATOM   12617 C  CG1 . ILE C 3  447  ? -69.199 -5.202   68.897  1.00 80.39  ?  447  ILE C CG1 1 
ATOM   12618 C  CG2 . ILE C 3  447  ? -69.597 -3.295   70.460  1.00 106.21 ?  447  ILE C CG2 1 
ATOM   12619 C  CD1 . ILE C 3  447  ? -70.204 -6.172   69.474  1.00 81.92  ?  447  ILE C CD1 1 
ATOM   12620 N  N   . PHE C 3  448  ? -65.892 -3.379   71.268  1.00 103.71 ?  448  PHE C N   1 
ATOM   12621 C  CA  . PHE C 3  448  ? -65.241 -2.656   72.357  1.00 113.38 ?  448  PHE C CA  1 
ATOM   12622 C  C   . PHE C 3  448  ? -64.161 -1.714   71.842  1.00 111.28 ?  448  PHE C C   1 
ATOM   12623 O  O   . PHE C 3  448  ? -63.895 -0.680   72.466  1.00 117.22 ?  448  PHE C O   1 
ATOM   12624 C  CB  . PHE C 3  448  ? -64.658 -3.638   73.377  1.00 117.71 ?  448  PHE C CB  1 
ATOM   12625 C  CG  . PHE C 3  448  ? -63.332 -4.223   72.978  1.00 113.48 ?  448  PHE C CG  1 
ATOM   12626 C  CD1 . PHE C 3  448  ? -63.270 -5.352   72.182  1.00 106.14 ?  448  PHE C CD1 1 
ATOM   12627 C  CD2 . PHE C 3  448  ? -62.147 -3.661   73.428  1.00 111.26 ?  448  PHE C CD2 1 
ATOM   12628 C  CE1 . PHE C 3  448  ? -62.052 -5.895   71.821  1.00 102.35 ?  448  PHE C CE1 1 
ATOM   12629 C  CE2 . PHE C 3  448  ? -60.926 -4.200   73.070  1.00 101.07 ?  448  PHE C CE2 1 
ATOM   12630 C  CZ  . PHE C 3  448  ? -60.879 -5.319   72.267  1.00 99.87  ?  448  PHE C CZ  1 
ATOM   12631 N  N   . GLU C 3  449  ? -63.530 -2.048   70.714  1.00 100.19 ?  449  GLU C N   1 
ATOM   12632 C  CA  . GLU C 3  449  ? -62.565 -1.133   70.116  1.00 111.23 ?  449  GLU C CA  1 
ATOM   12633 C  C   . GLU C 3  449  ? -63.250 0.097    69.534  1.00 119.19 ?  449  GLU C C   1 
ATOM   12634 O  O   . GLU C 3  449  ? -62.671 1.189    69.538  1.00 119.13 ?  449  GLU C O   1 
ATOM   12635 C  CB  . GLU C 3  449  ? -61.757 -1.851   69.035  1.00 108.74 ?  449  GLU C CB  1 
ATOM   12636 C  CG  . GLU C 3  449  ? -60.724 -2.823   69.577  1.00 112.48 ?  449  GLU C CG  1 
ATOM   12637 C  CD  . GLU C 3  449  ? -59.452 -2.830   68.753  1.00 119.60 ?  449  GLU C CD  1 
ATOM   12638 O  OE1 . GLU C 3  449  ? -59.549 -2.728   67.512  1.00 115.02 ?  449  GLU C OE1 1 
ATOM   12639 O  OE2 . GLU C 3  449  ? -58.355 -2.937   69.342  1.00 125.70 -1 449  GLU C OE2 1 
ATOM   12640 N  N   . MET C 3  450  ? -64.478 -0.058   69.035  1.00 106.63 ?  450  MET C N   1 
ATOM   12641 C  CA  . MET C 3  450  ? -65.187 1.079    68.458  1.00 107.49 ?  450  MET C CA  1 
ATOM   12642 C  C   . MET C 3  450  ? -65.668 2.040    69.538  1.00 106.31 ?  450  MET C C   1 
ATOM   12643 O  O   . MET C 3  450  ? -65.558 3.262    69.381  1.00 105.90 ?  450  MET C O   1 
ATOM   12644 C  CB  . MET C 3  450  ? -66.359 0.589    67.607  1.00 101.74 ?  450  MET C CB  1 
ATOM   12645 C  CG  . MET C 3  450  ? -65.962 0.138    66.208  1.00 92.56  ?  450  MET C CG  1 
ATOM   12646 S  SD  . MET C 3  450  ? -65.519 1.496    65.104  1.00 105.78 ?  450  MET C SD  1 
ATOM   12647 C  CE  . MET C 3  450  ? -66.662 2.771    65.632  1.00 112.30 ?  450  MET C CE  1 
ATOM   12648 N  N   . ARG C 3  451  ? -66.205 1.512    70.642  1.00 122.35 ?  451  ARG C N   1 
ATOM   12649 C  CA  . ARG C 3  451  ? -66.634 2.385    71.729  1.00 128.31 ?  451  ARG C CA  1 
ATOM   12650 C  C   . ARG C 3  451  ? -65.446 3.034    72.429  1.00 125.25 ?  451  ARG C C   1 
ATOM   12651 O  O   . ARG C 3  451  ? -65.574 4.142    72.962  1.00 123.79 ?  451  ARG C O   1 
ATOM   12652 C  CB  . ARG C 3  451  ? -67.493 1.610    72.732  1.00 128.42 ?  451  ARG C CB  1 
ATOM   12653 C  CG  . ARG C 3  451  ? -66.775 0.480    73.451  1.00 119.71 ?  451  ARG C CG  1 
ATOM   12654 C  CD  . ARG C 3  451  ? -67.613 -0.061   74.604  1.00 123.94 ?  451  ARG C CD  1 
ATOM   12655 N  NE  . ARG C 3  451  ? -68.870 -0.647   74.153  1.00 123.90 ?  451  ARG C NE  1 
ATOM   12656 C  CZ  . ARG C 3  451  ? -69.101 -1.950   74.059  1.00 122.51 ?  451  ARG C CZ  1 
ATOM   12657 N  NH1 . ARG C 3  451  ? -68.176 -2.841   74.374  1.00 120.34 ?  451  ARG C NH1 1 
ATOM   12658 N  NH2 . ARG C 3  451  ? -70.292 -2.369   73.640  1.00 122.37 ?  451  ARG C NH2 1 
ATOM   12659 N  N   . LEU C 3  452  ? -64.289 2.367    72.440  1.00 105.62 ?  452  LEU C N   1 
ATOM   12660 C  CA  . LEU C 3  452  ? -63.079 3.004    72.948  1.00 107.62 ?  452  LEU C CA  1 
ATOM   12661 C  C   . LEU C 3  452  ? -62.630 4.130    72.027  1.00 104.35 ?  452  LEU C C   1 
ATOM   12662 O  O   . LEU C 3  452  ? -62.173 5.181    72.494  1.00 105.90 ?  452  LEU C O   1 
ATOM   12663 C  CB  . LEU C 3  452  ? -61.966 1.967    73.113  1.00 111.00 ?  452  LEU C CB  1 
ATOM   12664 C  CG  . LEU C 3  452  ? -60.558 2.508    73.371  1.00 109.06 ?  452  LEU C CG  1 
ATOM   12665 C  CD1 . LEU C 3  452  ? -60.488 3.211    74.719  1.00 110.59 ?  452  LEU C CD1 1 
ATOM   12666 C  CD2 . LEU C 3  452  ? -59.525 1.395    73.288  1.00 106.15 ?  452  LEU C CD2 1 
ATOM   12667 N  N   . PHE C 3  453  ? -62.757 3.928    70.713  1.00 102.82 ?  453  PHE C N   1 
ATOM   12668 C  CA  . PHE C 3  453  ? -62.451 4.991    69.762  1.00 106.85 ?  453  PHE C CA  1 
ATOM   12669 C  C   . PHE C 3  453  ? -63.390 6.176    69.947  1.00 110.81 ?  453  PHE C C   1 
ATOM   12670 O  O   . PHE C 3  453  ? -62.970 7.335    69.843  1.00 105.57 ?  453  PHE C O   1 
ATOM   12671 C  CB  . PHE C 3  453  ? -62.536 4.448    68.335  1.00 95.04  ?  453  PHE C CB  1 
ATOM   12672 C  CG  . PHE C 3  453  ? -62.041 5.404    67.289  1.00 94.66  ?  453  PHE C CG  1 
ATOM   12673 C  CD1 . PHE C 3  453  ? -60.845 6.081    67.459  1.00 97.49  ?  453  PHE C CD1 1 
ATOM   12674 C  CD2 . PHE C 3  453  ? -62.771 5.623    66.133  1.00 100.87 ?  453  PHE C CD2 1 
ATOM   12675 C  CE1 . PHE C 3  453  ? -60.387 6.961    66.496  1.00 95.08  ?  453  PHE C CE1 1 
ATOM   12676 C  CE2 . PHE C 3  453  ? -62.319 6.502    65.166  1.00 99.14  ?  453  PHE C CE2 1 
ATOM   12677 C  CZ  . PHE C 3  453  ? -61.126 7.172    65.348  1.00 95.10  ?  453  PHE C CZ  1 
ATOM   12678 N  N   . LEU C 3  454  ? -64.668 5.904    70.229  1.00 117.88 ?  454  LEU C N   1 
ATOM   12679 C  CA  . LEU C 3  454  ? -65.616 6.980    70.498  1.00 112.48 ?  454  LEU C CA  1 
ATOM   12680 C  C   . LEU C 3  454  ? -65.239 7.740    71.763  1.00 110.01 ?  454  LEU C C   1 
ATOM   12681 O  O   . LEU C 3  454  ? -65.329 8.973    71.807  1.00 112.20 ?  454  LEU C O   1 
ATOM   12682 C  CB  . LEU C 3  454  ? -67.031 6.412    70.615  1.00 108.47 ?  454  LEU C CB  1 
ATOM   12683 C  CG  . LEU C 3  454  ? -68.106 7.344    71.177  1.00 108.07 ?  454  LEU C CG  1 
ATOM   12684 C  CD1 . LEU C 3  454  ? -68.391 8.488    70.214  1.00 111.10 ?  454  LEU C CD1 1 
ATOM   12685 C  CD2 . LEU C 3  454  ? -69.375 6.568    71.491  1.00 115.09 ?  454  LEU C CD2 1 
ATOM   12686 N  N   . TYR C 3  455  ? -64.815 7.020    72.804  1.00 119.48 ?  455  TYR C N   1 
ATOM   12687 C  CA  . TYR C 3  455  ? -64.382 7.675    74.033  1.00 125.50 ?  455  TYR C CA  1 
ATOM   12688 C  C   . TYR C 3  455  ? -63.129 8.508    73.799  1.00 128.16 ?  455  TYR C C   1 
ATOM   12689 O  O   . TYR C 3  455  ? -62.973 9.588    74.380  1.00 130.06 ?  455  TYR C O   1 
ATOM   12690 C  CB  . TYR C 3  455  ? -64.140 6.630    75.122  1.00 118.63 ?  455  TYR C CB  1 
ATOM   12691 C  CG  . TYR C 3  455  ? -63.495 7.176    76.376  1.00 125.71 ?  455  TYR C CG  1 
ATOM   12692 C  CD1 . TYR C 3  455  ? -64.183 8.042    77.216  1.00 127.05 ?  455  TYR C CD1 1 
ATOM   12693 C  CD2 . TYR C 3  455  ? -62.197 6.823    76.721  1.00 133.08 ?  455  TYR C CD2 1 
ATOM   12694 C  CE1 . TYR C 3  455  ? -63.596 8.541    78.365  1.00 127.36 ?  455  TYR C CE1 1 
ATOM   12695 C  CE2 . TYR C 3  455  ? -61.601 7.317    77.866  1.00 129.41 ?  455  TYR C CE2 1 
ATOM   12696 C  CZ  . TYR C 3  455  ? -62.305 8.175    78.684  1.00 126.31 ?  455  TYR C CZ  1 
ATOM   12697 O  OH  . TYR C 3  455  ? -61.714 8.668    79.825  1.00 128.13 ?  455  TYR C OH  1 
ATOM   12698 N  N   . GLN C 3  456  ? -62.224 8.023    72.944  1.00 105.99 ?  456  GLN C N   1 
ATOM   12699 C  CA  . GLN C 3  456  ? -61.009 8.774    72.651  1.00 102.54 ?  456  GLN C CA  1 
ATOM   12700 C  C   . GLN C 3  456  ? -61.319 10.038   71.859  1.00 104.97 ?  456  GLN C C   1 
ATOM   12701 O  O   . GLN C 3  456  ? -60.720 11.092   72.103  1.00 105.70 ?  456  GLN C O   1 
ATOM   12702 C  CB  . GLN C 3  456  ? -60.017 7.895    71.892  1.00 103.28 ?  456  GLN C CB  1 
ATOM   12703 C  CG  . GLN C 3  456  ? -59.340 6.845    72.750  1.00 104.77 ?  456  GLN C CG  1 
ATOM   12704 C  CD  . GLN C 3  456  ? -58.457 5.919    71.941  1.00 102.44 ?  456  GLN C CD  1 
ATOM   12705 O  OE1 . GLN C 3  456  ? -58.479 5.938    70.709  1.00 93.83  ?  456  GLN C OE1 1 
ATOM   12706 N  NE2 . GLN C 3  456  ? -57.672 5.101    72.630  1.00 98.14  ?  456  GLN C NE2 1 
ATOM   12707 N  N   . GLU C 3  457  ? -62.250 9.953    70.905  1.00 129.86 ?  457  GLU C N   1 
ATOM   12708 C  CA  . GLU C 3  457  ? -62.637 11.139   70.148  1.00 133.28 ?  457  GLU C CA  1 
ATOM   12709 C  C   . GLU C 3  457  ? -63.363 12.150   71.025  1.00 130.34 ?  457  GLU C C   1 
ATOM   12710 O  O   . GLU C 3  457  ? -63.219 13.362   70.823  1.00 129.85 ?  457  GLU C O   1 
ATOM   12711 C  CB  . GLU C 3  457  ? -63.512 10.741   68.958  1.00 138.61 ?  457  GLU C CB  1 
ATOM   12712 C  CG  . GLU C 3  457  ? -62.788 9.927    67.899  1.00 131.97 ?  457  GLU C CG  1 
ATOM   12713 C  CD  . GLU C 3  457  ? -62.205 10.789   66.795  1.00 137.37 ?  457  GLU C CD  1 
ATOM   12714 O  OE1 . GLU C 3  457  ? -61.659 11.871   67.101  1.00 133.88 ?  457  GLU C OE1 1 
ATOM   12715 O  OE2 . GLU C 3  457  ? -62.288 10.381   65.619  1.00 151.78 -1 457  GLU C OE2 1 
ATOM   12716 N  N   . THR C 3  458  ? -64.142 11.673   71.998  1.00 129.01 ?  458  THR C N   1 
ATOM   12717 C  CA  . THR C 3  458  ? -64.793 12.581   72.936  1.00 129.90 ?  458  THR C CA  1 
ATOM   12718 C  C   . THR C 3  458  ? -63.764 13.313   73.788  1.00 131.64 ?  458  THR C C   1 
ATOM   12719 O  O   . THR C 3  458  ? -63.893 14.518   74.035  1.00 138.70 ?  458  THR C O   1 
ATOM   12720 C  CB  . THR C 3  458  ? -65.775 11.809   73.823  1.00 124.07 ?  458  THR C CB  1 
ATOM   12721 O  OG1 . THR C 3  458  ? -66.808 11.236   73.012  1.00 119.45 ?  458  THR C OG1 1 
ATOM   12722 C  CG2 . THR C 3  458  ? -66.407 12.725   74.863  1.00 124.16 ?  458  THR C CG2 1 
ATOM   12723 N  N   . GLU C 3  459  ? -62.730 12.600   74.244  1.00 140.52 ?  459  GLU C N   1 
ATOM   12724 C  CA  . GLU C 3  459  ? -61.678 13.240   75.026  1.00 142.69 ?  459  GLU C CA  1 
ATOM   12725 C  C   . GLU C 3  459  ? -60.887 14.232   74.182  1.00 142.20 ?  459  GLU C C   1 
ATOM   12726 O  O   . GLU C 3  459  ? -60.482 15.291   74.676  1.00 142.20 ?  459  GLU C O   1 
ATOM   12727 C  CB  . GLU C 3  459  ? -60.748 12.182   75.620  1.00 142.12 ?  459  GLU C CB  1 
ATOM   12728 C  CG  . GLU C 3  459  ? -61.401 11.306   76.675  1.00 145.25 ?  459  GLU C CG  1 
ATOM   12729 C  CD  . GLU C 3  459  ? -61.975 12.111   77.824  1.00 160.19 ?  459  GLU C CD  1 
ATOM   12730 O  OE1 . GLU C 3  459  ? -61.257 12.983   78.358  1.00 157.55 ?  459  GLU C OE1 1 
ATOM   12731 O  OE2 . GLU C 3  459  ? -63.143 11.870   78.195  1.00 170.13 -1 459  GLU C OE2 1 
ATOM   12732 N  N   . LYS C 3  460  ? -60.657 13.907   72.907  1.00 129.15 ?  460  LYS C N   1 
ATOM   12733 C  CA  . LYS C 3  460  ? -59.940 14.827   72.030  1.00 127.48 ?  460  LYS C CA  1 
ATOM   12734 C  C   . LYS C 3  460  ? -60.754 16.090   71.773  1.00 131.50 ?  460  LYS C C   1 
ATOM   12735 O  O   . LYS C 3  460  ? -60.202 17.196   71.749  1.00 132.21 ?  460  LYS C O   1 
ATOM   12736 C  CB  . LYS C 3  460  ? -59.591 14.135   70.713  1.00 128.69 ?  460  LYS C CB  1 
ATOM   12737 C  CG  . LYS C 3  460  ? -58.447 13.140   70.816  1.00 128.20 ?  460  LYS C CG  1 
ATOM   12738 C  CD  . LYS C 3  460  ? -58.125 12.531   69.460  1.00 122.85 ?  460  LYS C CD  1 
ATOM   12739 C  CE  . LYS C 3  460  ? -57.020 11.494   69.568  1.00 122.78 ?  460  LYS C CE  1 
ATOM   12740 N  NZ  . LYS C 3  460  ? -56.755 10.826   68.263  1.00 126.65 ?  460  LYS C NZ  1 
ATOM   12741 N  N   . ALA C 3  461  ? -62.067 15.944   71.576  1.00 104.78 ?  461  ALA C N   1 
ATOM   12742 C  CA  . ALA C 3  461  ? -62.921 17.115   71.404  1.00 102.85 ?  461  ALA C CA  1 
ATOM   12743 C  C   . ALA C 3  461  ? -63.000 17.941   72.681  1.00 98.31  ?  461  ALA C C   1 
ATOM   12744 O  O   . ALA C 3  461  ? -63.177 19.163   72.618  1.00 94.53  ?  461  ALA C O   1 
ATOM   12745 C  CB  . ALA C 3  461  ? -64.318 16.687   70.959  1.00 92.64  ?  461  ALA C CB  1 
ATOM   12746 N  N   . LYS C 3  462  ? -62.873 17.295   73.843  1.00 120.03 ?  462  LYS C N   1 
ATOM   12747 C  CA  . LYS C 3  462  ? -62.857 18.029   75.103  1.00 120.56 ?  462  LYS C CA  1 
ATOM   12748 C  C   . LYS C 3  462  ? -61.611 18.898   75.216  1.00 124.31 ?  462  LYS C C   1 
ATOM   12749 O  O   . LYS C 3  462  ? -61.687 20.050   75.660  1.00 124.70 ?  462  LYS C O   1 
ATOM   12750 C  CB  . LYS C 3  462  ? -62.942 17.053   76.276  1.00 119.02 ?  462  LYS C CB  1 
ATOM   12751 C  CG  . LYS C 3  462  ? -64.355 16.785   76.767  1.00 123.92 ?  462  LYS C CG  1 
ATOM   12752 C  CD  . LYS C 3  462  ? -64.348 16.265   78.195  1.00 128.05 ?  462  LYS C CD  1 
ATOM   12753 C  CE  . LYS C 3  462  ? -65.362 15.149   78.383  1.00 117.85 ?  462  LYS C CE  1 
ATOM   12754 N  NZ  . LYS C 3  462  ? -65.341 14.609   79.770  1.00 121.37 ?  462  LYS C NZ  1 
ATOM   12755 N  N   . GLN C 3  463  ? -60.457 18.364   74.819  1.00 124.35 ?  463  GLN C N   1 
ATOM   12756 C  CA  . GLN C 3  463  ? -59.214 19.122   74.816  1.00 119.96 ?  463  GLN C CA  1 
ATOM   12757 C  C   . GLN C 3  463  ? -59.081 20.035   73.604  1.00 116.80 ?  463  GLN C C   1 
ATOM   12758 O  O   . GLN C 3  463  ? -58.074 20.743   73.495  1.00 118.76 ?  463  GLN C O   1 
ATOM   12759 C  CB  . GLN C 3  463  ? -58.017 18.169   74.875  1.00 124.39 ?  463  GLN C CB  1 
ATOM   12760 C  CG  . GLN C 3  463  ? -57.439 17.979   76.270  1.00 135.91 ?  463  GLN C CG  1 
ATOM   12761 C  CD  . GLN C 3  463  ? -56.544 16.759   76.367  1.00 144.59 ?  463  GLN C CD  1 
ATOM   12762 O  OE1 . GLN C 3  463  ? -55.887 16.379   75.398  1.00 147.17 ?  463  GLN C OE1 1 
ATOM   12763 N  NE2 . GLN C 3  463  ? -56.511 16.140   77.542  1.00 141.05 ?  463  GLN C NE2 1 
ATOM   12764 N  N   . ARG C 3  464  ? -60.064 20.029   72.705  1.00 123.43 ?  464  ARG C N   1 
ATOM   12765 C  CA  . ARG C 3  464  ? -60.058 20.862   71.502  1.00 128.96 ?  464  ARG C CA  1 
ATOM   12766 C  C   . ARG C 3  464  ? -58.792 20.667   70.673  1.00 135.34 ?  464  ARG C C   1 
ATOM   12767 O  O   . ARG C 3  464  ? -58.850 20.582   69.446  1.00 132.59 ?  464  ARG C O   1 
ATOM   12768 C  CB  . ARG C 3  464  ? -60.222 22.339   71.872  1.00 122.65 ?  464  ARG C CB  1 
ATOM   12769 C  CG  . ARG C 3  464  ? -61.498 22.648   72.638  1.00 124.19 ?  464  ARG C CG  1 
ATOM   12770 C  CD  . ARG C 3  464  ? -61.273 23.751   73.657  1.00 125.64 ?  464  ARG C CD  1 
ATOM   12771 N  NE  . ARG C 3  464  ? -60.448 23.299   74.771  1.00 134.81 ?  464  ARG C NE  1 
ATOM   12772 C  CZ  . ARG C 3  464  ? -59.316 23.878   75.147  1.00 136.20 ?  464  ARG C CZ  1 
ATOM   12773 N  NH1 . ARG C 3  464  ? -58.841 24.940   74.518  1.00 132.50 ?  464  ARG C NH1 1 
ATOM   12774 N  NH2 . ARG C 3  464  ? -58.645 23.379   76.181  1.00 133.05 ?  464  ARG C NH2 1 
ATOM   12775 N  N   . VAL D 4  5    ? -72.317 -10.596  100.544 1.00 124.11 ?  5    VAL D N   1 
ATOM   12776 C  CA  . VAL D 4  5    ? -71.189 -10.692  101.460 1.00 117.63 ?  5    VAL D CA  1 
ATOM   12777 C  C   . VAL D 4  5    ? -69.883 -10.538  100.687 1.00 130.13 ?  5    VAL D C   1 
ATOM   12778 O  O   . VAL D 4  5    ? -68.836 -10.262  101.269 1.00 129.86 ?  5    VAL D O   1 
ATOM   12779 C  CB  . VAL D 4  5    ? -71.221 -12.018  102.245 1.00 125.40 ?  5    VAL D CB  1 
ATOM   12780 C  CG1 . VAL D 4  5    ? -70.280 -11.961  103.442 1.00 128.44 ?  5    VAL D CG1 1 
ATOM   12781 C  CG2 . VAL D 4  5    ? -72.641 -12.333  102.691 1.00 119.87 ?  5    VAL D CG2 1 
ATOM   12782 N  N   . TYR D 4  6    ? -69.949 -10.711  99.364  1.00 125.04 ?  6    TYR D N   1 
ATOM   12783 C  CA  . TYR D 4  6    ? -68.748 -10.560  98.547  1.00 124.99 ?  6    TYR D CA  1 
ATOM   12784 C  C   . TYR D 4  6    ? -68.322 -9.100   98.455  1.00 130.39 ?  6    TYR D C   1 
ATOM   12785 O  O   . TYR D 4  6    ? -67.125 -8.795   98.486  1.00 134.29 ?  6    TYR D O   1 
ATOM   12786 C  CB  . TYR D 4  6    ? -68.980 -11.143  97.152  1.00 126.81 ?  6    TYR D CB  1 
ATOM   12787 C  CG  . TYR D 4  6    ? -67.822 -10.946  96.195  1.00 131.24 ?  6    TYR D CG  1 
ATOM   12788 C  CD1 . TYR D 4  6    ? -66.564 -11.462  96.481  1.00 132.15 ?  6    TYR D CD1 1 
ATOM   12789 C  CD2 . TYR D 4  6    ? -67.988 -10.248  95.005  1.00 127.89 ?  6    TYR D CD2 1 
ATOM   12790 C  CE1 . TYR D 4  6    ? -65.505 -11.287  95.609  1.00 130.81 ?  6    TYR D CE1 1 
ATOM   12791 C  CE2 . TYR D 4  6    ? -66.933 -10.068  94.127  1.00 128.48 ?  6    TYR D CE2 1 
ATOM   12792 C  CZ  . TYR D 4  6    ? -65.695 -10.590  94.435  1.00 132.18 ?  6    TYR D CZ  1 
ATOM   12793 O  OH  . TYR D 4  6    ? -64.643 -10.413  93.565  1.00 131.59 ?  6    TYR D OH  1 
ATOM   12794 N  N   . GLY D 4  7    ? -69.277 -8.187   98.346  1.00 93.84  ?  7    GLY D N   1 
ATOM   12795 C  CA  . GLY D 4  7    ? -68.939 -6.781   98.268  1.00 87.63  ?  7    GLY D CA  1 
ATOM   12796 C  C   . GLY D 4  7    ? -70.159 -5.920   98.044  1.00 88.11  ?  7    GLY D C   1 
ATOM   12797 O  O   . GLY D 4  7    ? -71.289 -6.338   98.301  1.00 92.01  ?  7    GLY D O   1 
ATOM   12798 N  N   . VAL D 4  8    ? -69.914 -4.702   97.562  1.00 80.29  ?  8    VAL D N   1 
ATOM   12799 C  CA  . VAL D 4  8    ? -70.962 -3.725   97.293  1.00 79.32  ?  8    VAL D CA  1 
ATOM   12800 C  C   . VAL D 4  8    ? -70.747 -3.170   95.891  1.00 74.97  ?  8    VAL D C   1 
ATOM   12801 O  O   . VAL D 4  8    ? -69.623 -3.154   95.382  1.00 69.08  ?  8    VAL D O   1 
ATOM   12802 C  CB  . VAL D 4  8    ? -70.972 -2.589   98.342  1.00 83.17  ?  8    VAL D CB  1 
ATOM   12803 C  CG1 . VAL D 4  8    ? -72.246 -1.774   98.235  1.00 85.87  ?  8    VAL D CG1 1 
ATOM   12804 C  CG2 . VAL D 4  8    ? -70.812 -3.148   99.749  1.00 81.37  ?  8    VAL D CG2 1 
ATOM   12805 N  N   . MET D 4  9    ? -71.829 -2.714   95.262  1.00 120.50 ?  9    MET D N   1 
ATOM   12806 C  CA  . MET D 4  9    ? -71.785 -2.250   93.883  1.00 114.84 ?  9    MET D CA  1 
ATOM   12807 C  C   . MET D 4  9    ? -72.215 -0.791   93.788  1.00 116.19 ?  9    MET D C   1 
ATOM   12808 O  O   . MET D 4  9    ? -72.889 -0.262   94.676  1.00 124.16 ?  9    MET D O   1 
ATOM   12809 C  CB  . MET D 4  9    ? -72.671 -3.113   92.984  1.00 124.21 ?  9    MET D CB  1 
ATOM   12810 C  CG  . MET D 4  9    ? -71.996 -4.387   92.543  1.00 127.52 ?  9    MET D CG  1 
ATOM   12811 S  SD  . MET D 4  9    ? -70.764 -4.098   91.263  1.00 131.73 ?  9    MET D SD  1 
ATOM   12812 C  CE  . MET D 4  9    ? -70.701 -5.721   90.524  1.00 123.08 ?  9    MET D CE  1 
ATOM   12813 N  N   . ALA D 4  10   ? -71.826 -0.149   92.684  1.00 149.33 ?  10   ALA D N   1 
ATOM   12814 C  CA  . ALA D 4  10   ? -72.014 1.288    92.497  1.00 151.53 ?  10   ALA D CA  1 
ATOM   12815 C  C   . ALA D 4  10   ? -72.866 1.652    91.290  1.00 158.55 ?  10   ALA D C   1 
ATOM   12816 O  O   . ALA D 4  10   ? -73.721 2.535    91.401  1.00 166.88 ?  10   ALA D O   1 
ATOM   12817 C  CB  . ALA D 4  10   ? -70.652 1.988    92.382  1.00 143.45 ?  10   ALA D CB  1 
ATOM   12818 N  N   . GLU D 4  11   ? -72.641 1.018    90.133  1.00 142.93 ?  11   GLU D N   1 
ATOM   12819 C  CA  . GLU D 4  11   ? -73.460 1.222    88.931  1.00 142.84 ?  11   GLU D CA  1 
ATOM   12820 C  C   . GLU D 4  11   ? -73.428 2.679    88.465  1.00 142.14 ?  11   GLU D C   1 
ATOM   12821 O  O   . GLU D 4  11   ? -74.465 3.323    88.297  1.00 145.61 ?  11   GLU D O   1 
ATOM   12822 C  CB  . GLU D 4  11   ? -74.902 0.759    89.166  1.00 144.32 ?  11   GLU D CB  1 
ATOM   12823 C  CG  . GLU D 4  11   ? -75.540 0.068    87.974  1.00 143.96 ?  11   GLU D CG  1 
ATOM   12824 C  CD  . GLU D 4  11   ? -76.043 1.041    86.925  1.00 151.78 ?  11   GLU D CD  1 
ATOM   12825 O  OE1 . GLU D 4  11   ? -77.113 1.645    87.140  1.00 155.89 ?  11   GLU D OE1 1 
ATOM   12826 O  OE2 . GLU D 4  11   ? -75.370 1.205    85.886  1.00 148.97 -1 11   GLU D OE2 1 
ATOM   12827 N  N   . PHE D 4  12   ? -72.222 3.204    88.261  1.00 111.61 ?  12   PHE D N   1 
ATOM   12828 C  CA  . PHE D 4  12   ? -72.092 4.597    87.844  1.00 114.66 ?  12   PHE D CA  1 
ATOM   12829 C  C   . PHE D 4  12   ? -72.478 4.754    86.375  1.00 113.58 ?  12   PHE D C   1 
ATOM   12830 O  O   . PHE D 4  12   ? -72.152 3.892    85.551  1.00 116.07 ?  12   PHE D O   1 
ATOM   12831 C  CB  . PHE D 4  12   ? -70.673 5.107    88.083  1.00 107.55 ?  12   PHE D CB  1 
ATOM   12832 C  CG  . PHE D 4  12   ? -70.468 5.694    89.448  1.00 111.34 ?  12   PHE D CG  1 
ATOM   12833 C  CD1 . PHE D 4  12   ? -70.143 4.897    90.529  1.00 113.36 ?  12   PHE D CD1 1 
ATOM   12834 C  CD2 . PHE D 4  12   ? -70.593 7.058    89.642  1.00 117.41 ?  12   PHE D CD2 1 
ATOM   12835 C  CE1 . PHE D 4  12   ? -69.957 5.455    91.783  1.00 124.25 ?  12   PHE D CE1 1 
ATOM   12836 C  CE2 . PHE D 4  12   ? -70.400 7.624    90.886  1.00 125.85 ?  12   PHE D CE2 1 
ATOM   12837 C  CZ  . PHE D 4  12   ? -70.090 6.822    91.961  1.00 131.09 ?  12   PHE D CZ  1 
ATOM   12838 N  N   . PRO D 4  13   ? -73.187 5.832    86.017  1.00 132.90 ?  13   PRO D N   1 
ATOM   12839 C  CA  . PRO D 4  13   ? -73.777 5.874    84.668  1.00 137.34 ?  13   PRO D CA  1 
ATOM   12840 C  C   . PRO D 4  13   ? -72.761 6.184    83.585  1.00 129.13 ?  13   PRO D C   1 
ATOM   12841 O  O   . PRO D 4  13   ? -72.741 5.498    82.555  1.00 122.55 ?  13   PRO D O   1 
ATOM   12842 C  CB  . PRO D 4  13   ? -74.863 6.960    84.792  1.00 140.88 ?  13   PRO D CB  1 
ATOM   12843 C  CG  . PRO D 4  13   ? -74.426 7.812    85.919  1.00 143.64 ?  13   PRO D CG  1 
ATOM   12844 C  CD  . PRO D 4  13   ? -73.718 6.898    86.886  1.00 138.39 ?  13   PRO D CD  1 
ATOM   12845 N  N   . THR D 4  14   ? -71.886 7.169    83.801  1.00 118.76 ?  14   THR D N   1 
ATOM   12846 C  CA  . THR D 4  14   ? -70.945 7.615    82.787  1.00 114.79 ?  14   THR D CA  1 
ATOM   12847 C  C   . THR D 4  14   ? -69.519 7.183    83.133  1.00 119.80 ?  14   THR D C   1 
ATOM   12848 O  O   . THR D 4  14   ? -69.175 7.039    84.313  1.00 122.09 ?  14   THR D O   1 
ATOM   12849 C  CB  . THR D 4  14   ? -71.011 9.142    82.641  1.00 120.90 ?  14   THR D CB  1 
ATOM   12850 O  OG1 . THR D 4  14   ? -69.882 9.621    81.898  1.00 119.36 ?  14   THR D OG1 1 
ATOM   12851 C  CG2 . THR D 4  14   ? -71.048 9.810    84.001  1.00 123.61 ?  14   THR D CG2 1 
ATOM   12852 N  N   . PRO D 4  15   ? -68.671 6.943    82.123  1.00 129.90 ?  15   PRO D N   1 
ATOM   12853 C  CA  . PRO D 4  15   ? -67.301 6.490    82.424  1.00 130.44 ?  15   PRO D CA  1 
ATOM   12854 C  C   . PRO D 4  15   ? -66.510 7.486    83.253  1.00 133.53 ?  15   PRO D C   1 
ATOM   12855 O  O   . PRO D 4  15   ? -65.736 7.076    84.126  1.00 130.41 ?  15   PRO D O   1 
ATOM   12856 C  CB  . PRO D 4  15   ? -66.682 6.282    81.032  1.00 118.13 ?  15   PRO D CB  1 
ATOM   12857 C  CG  . PRO D 4  15   ? -67.559 7.043    80.087  1.00 123.81 ?  15   PRO D CG  1 
ATOM   12858 C  CD  . PRO D 4  15   ? -68.931 7.004    80.675  1.00 128.10 ?  15   PRO D CD  1 
ATOM   12859 N  N   . GLU D 4  16   ? -66.696 8.789    83.021  1.00 123.24 ?  16   GLU D N   1 
ATOM   12860 C  CA  . GLU D 4  16   ? -65.969 9.790    83.799  1.00 114.87 ?  16   GLU D CA  1 
ATOM   12861 C  C   . GLU D 4  16   ? -66.342 9.726    85.276  1.00 117.97 ?  16   GLU D C   1 
ATOM   12862 O  O   . GLU D 4  16   ? -65.497 9.970    86.145  1.00 125.11 ?  16   GLU D O   1 
ATOM   12863 C  CB  . GLU D 4  16   ? -66.229 11.188   83.236  1.00 116.97 ?  16   GLU D CB  1 
ATOM   12864 C  CG  . GLU D 4  16   ? -65.536 11.466   81.908  1.00 121.70 ?  16   GLU D CG  1 
ATOM   12865 C  CD  . GLU D 4  16   ? -66.262 10.858   80.726  1.00 122.76 ?  16   GLU D CD  1 
ATOM   12866 O  OE1 . GLU D 4  16   ? -67.473 10.578   80.853  1.00 121.47 ?  16   GLU D OE1 1 
ATOM   12867 O  OE2 . GLU D 4  16   ? -65.622 10.664   79.670  1.00 121.06 -1 16   GLU D OE2 1 
ATOM   12868 N  N   . ALA D 4  17   ? -67.602 9.401    85.581  1.00 98.34  ?  17   ALA D N   1 
ATOM   12869 C  CA  . ALA D 4  17   ? -68.008 9.270    86.978  1.00 103.24 ?  17   ALA D CA  1 
ATOM   12870 C  C   . ALA D 4  17   ? -67.290 8.111    87.654  1.00 105.30 ?  17   ALA D C   1 
ATOM   12871 O  O   . ALA D 4  17   ? -66.936 8.194    88.836  1.00 104.40 ?  17   ALA D O   1 
ATOM   12872 C  CB  . ALA D 4  17   ? -69.522 9.090    87.076  1.00 101.12 ?  17   ALA D CB  1 
ATOM   12873 N  N   . LEU D 4  18   ? -67.069 7.018    86.920  1.00 123.47 ?  18   LEU D N   1 
ATOM   12874 C  CA  . LEU D 4  18   ? -66.326 5.890    87.473  1.00 120.39 ?  18   LEU D CA  1 
ATOM   12875 C  C   . LEU D 4  18   ? -64.901 6.294    87.826  1.00 116.97 ?  18   LEU D C   1 
ATOM   12876 O  O   . LEU D 4  18   ? -64.377 5.903    88.876  1.00 112.92 ?  18   LEU D O   1 
ATOM   12877 C  CB  . LEU D 4  18   ? -66.324 4.730    86.479  1.00 113.47 ?  18   LEU D CB  1 
ATOM   12878 C  CG  . LEU D 4  18   ? -65.982 3.364    87.066  1.00 104.91 ?  18   LEU D CG  1 
ATOM   12879 C  CD1 . LEU D 4  18   ? -66.981 3.021    88.146  1.00 108.11 ?  18   LEU D CD1 1 
ATOM   12880 C  CD2 . LEU D 4  18   ? -65.958 2.295    85.987  1.00 104.76 ?  18   LEU D CD2 1 
ATOM   12881 N  N   . ILE D 4  19   ? -64.260 7.078    86.955  1.00 136.43 ?  19   ILE D N   1 
ATOM   12882 C  CA  . ILE D 4  19   ? -62.912 7.565    87.231  1.00 137.38 ?  19   ILE D CA  1 
ATOM   12883 C  C   . ILE D 4  19   ? -62.903 8.397    88.504  1.00 140.15 ?  19   ILE D C   1 
ATOM   12884 O  O   . ILE D 4  19   ? -62.071 8.193    89.396  1.00 144.14 ?  19   ILE D O   1 
ATOM   12885 C  CB  . ILE D 4  19   ? -62.377 8.373    86.035  1.00 139.31 ?  19   ILE D CB  1 
ATOM   12886 C  CG1 . ILE D 4  19   ? -62.602 7.613    84.729  1.00 134.17 ?  19   ILE D CG1 1 
ATOM   12887 C  CG2 . ILE D 4  19   ? -60.907 8.692    86.225  1.00 144.09 ?  19   ILE D CG2 1 
ATOM   12888 C  CD1 . ILE D 4  19   ? -62.350 8.445    83.496  1.00 131.86 ?  19   ILE D CD1 1 
ATOM   12889 N  N   . GLU D 4  20   ? -63.839 9.343    88.610  1.00 174.20 ?  20   GLU D N   1 
ATOM   12890 C  CA  . GLU D 4  20   ? -63.882 10.216   89.777  1.00 175.46 ?  20   GLU D CA  1 
ATOM   12891 C  C   . GLU D 4  20   ? -64.192 9.427    91.040  1.00 173.29 ?  20   GLU D C   1 
ATOM   12892 O  O   . GLU D 4  20   ? -63.598 9.674    92.096  1.00 175.97 ?  20   GLU D O   1 
ATOM   12893 C  CB  . GLU D 4  20   ? -64.918 11.320   89.565  1.00 181.17 ?  20   GLU D CB  1 
ATOM   12894 C  CG  . GLU D 4  20   ? -64.654 12.208   88.355  1.00 184.06 ?  20   GLU D CG  1 
ATOM   12895 C  CD  . GLU D 4  20   ? -63.503 13.175   88.553  1.00 195.64 ?  20   GLU D CD  1 
ATOM   12896 O  OE1 . GLU D 4  20   ? -63.000 13.281   89.692  1.00 196.54 ?  20   GLU D OE1 1 
ATOM   12897 O  OE2 . GLU D 4  20   ? -63.105 13.830   87.564  1.00 197.26 -1 20   GLU D OE2 1 
ATOM   12898 N  N   . ALA D 4  21   ? -65.110 8.461    90.945  1.00 111.54 ?  21   ALA D N   1 
ATOM   12899 C  CA  . ALA D 4  21   ? -65.493 7.676    92.115  1.00 111.19 ?  21   ALA D CA  1 
ATOM   12900 C  C   . ALA D 4  21   ? -64.340 6.812    92.605  1.00 112.45 ?  21   ALA D C   1 
ATOM   12901 O  O   . ALA D 4  21   ? -64.105 6.708    93.815  1.00 111.25 ?  21   ALA D O   1 
ATOM   12902 C  CB  . ALA D 4  21   ? -66.704 6.808    91.789  1.00 105.99 ?  21   ALA D CB  1 
ATOM   12903 N  N   . THR D 4  22   ? -63.621 6.170    91.681  1.00 110.17 ?  22   THR D N   1 
ATOM   12904 C  CA  . THR D 4  22   ? -62.446 5.397    92.068  1.00 103.32 ?  22   THR D CA  1 
ATOM   12905 C  C   . THR D 4  22   ? -61.400 6.288    92.724  1.00 106.81 ?  22   THR D C   1 
ATOM   12906 O  O   . THR D 4  22   ? -60.719 5.870    93.668  1.00 110.87 ?  22   THR D O   1 
ATOM   12907 C  CB  . THR D 4  22   ? -61.859 4.687    90.848  1.00 100.13 ?  22   THR D CB  1 
ATOM   12908 O  OG1 . THR D 4  22   ? -62.883 3.919    90.205  1.00 96.95  ?  22   THR D OG1 1 
ATOM   12909 C  CG2 . THR D 4  22   ? -60.731 3.763    91.261  1.00 100.36 ?  22   THR D CG2 1 
ATOM   12910 N  N   . ARG D 4  23   ? -61.272 7.529    92.247  1.00 120.38 ?  23   ARG D N   1 
ATOM   12911 C  CA  . ARG D 4  23   ? -60.326 8.461    92.848  1.00 119.71 ?  23   ARG D CA  1 
ATOM   12912 C  C   . ARG D 4  23   ? -60.829 8.976    94.191  1.00 117.75 ?  23   ARG D C   1 
ATOM   12913 O  O   . ARG D 4  23   ? -60.020 9.335    95.055  1.00 117.23 ?  23   ARG D O   1 
ATOM   12914 C  CB  . ARG D 4  23   ? -60.055 9.620    91.889  1.00 123.44 ?  23   ARG D CB  1 
ATOM   12915 C  CG  . ARG D 4  23   ? -59.305 9.202    90.634  1.00 125.43 ?  23   ARG D CG  1 
ATOM   12916 C  CD  . ARG D 4  23   ? -59.006 10.382   89.731  1.00 127.65 ?  23   ARG D CD  1 
ATOM   12917 N  NE  . ARG D 4  23   ? -58.401 9.949    88.478  1.00 127.01 ?  23   ARG D NE  1 
ATOM   12918 C  CZ  . ARG D 4  23   ? -57.102 9.751    88.304  1.00 135.02 ?  23   ARG D CZ  1 
ATOM   12919 N  NH1 . ARG D 4  23   ? -56.235 9.948    89.284  1.00 142.16 ?  23   ARG D NH1 1 
ATOM   12920 N  NH2 . ARG D 4  23   ? -56.661 9.340    87.119  1.00 136.17 ?  23   ARG D NH2 1 
ATOM   12921 N  N   . LYS D 4  24   ? -62.151 9.028    94.384  1.00 122.05 ?  24   LYS D N   1 
ATOM   12922 C  CA  . LYS D 4  24   ? -62.692 9.360    95.699  1.00 118.99 ?  24   LYS D CA  1 
ATOM   12923 C  C   . LYS D 4  24   ? -62.356 8.272    96.709  1.00 123.52 ?  24   LYS D C   1 
ATOM   12924 O  O   . LYS D 4  24   ? -61.924 8.565    97.830  1.00 131.25 ?  24   LYS D O   1 
ATOM   12925 C  CB  . LYS D 4  24   ? -64.203 9.581    95.618  1.00 117.44 ?  24   LYS D CB  1 
ATOM   12926 C  CG  . LYS D 4  24   ? -64.601 10.841   94.871  1.00 121.19 ?  24   LYS D CG  1 
ATOM   12927 C  CD  . LYS D 4  24   ? -66.105 11.045   94.885  1.00 115.62 ?  24   LYS D CD  1 
ATOM   12928 C  CE  . LYS D 4  24   ? -66.533 12.111   93.886  1.00 116.17 ?  24   LYS D CE  1 
ATOM   12929 N  NZ  . LYS D 4  24   ? -65.792 13.393   94.082  1.00 125.71 ?  24   LYS D NZ  1 
ATOM   12930 N  N   . ALA D 4  25   ? -62.534 7.010    96.324  1.00 113.77 ?  25   ALA D N   1 
ATOM   12931 C  CA  . ALA D 4  25   ? -61.975 5.906    97.086  1.00 106.37 ?  25   ALA D CA  1 
ATOM   12932 C  C   . ALA D 4  25   ? -60.453 5.932    96.961  1.00 113.61 ?  25   ALA D C   1 
ATOM   12933 O  O   . ALA D 4  25   ? -59.874 6.824    96.335  1.00 115.76 ?  25   ALA D O   1 
ATOM   12934 C  CB  . ALA D 4  25   ? -62.554 4.577    96.609  1.00 108.86 ?  25   ALA D CB  1 
ATOM   12935 N  N   . LYS D 4  26   ? -59.794 4.941    97.569  1.00 141.82 ?  26   LYS D N   1 
ATOM   12936 C  CA  . LYS D 4  26   ? -58.334 4.903    97.673  1.00 145.43 ?  26   LYS D CA  1 
ATOM   12937 C  C   . LYS D 4  26   ? -57.828 6.061    98.530  1.00 150.94 ?  26   LYS D C   1 
ATOM   12938 O  O   . LYS D 4  26   ? -57.065 5.850    99.479  1.00 155.31 ?  26   LYS D O   1 
ATOM   12939 C  CB  . LYS D 4  26   ? -57.681 4.920    96.286  1.00 140.34 ?  26   LYS D CB  1 
ATOM   12940 C  CG  . LYS D 4  26   ? -56.168 4.802    96.287  1.00 140.27 ?  26   LYS D CG  1 
ATOM   12941 C  CD  . LYS D 4  26   ? -55.647 4.573    94.875  1.00 139.32 ?  26   LYS D CD  1 
ATOM   12942 C  CE  . LYS D 4  26   ? -54.130 4.514    94.842  1.00 134.95 ?  26   LYS D CE  1 
ATOM   12943 N  NZ  . LYS D 4  26   ? -53.598 3.493    95.788  1.00 130.29 ?  26   LYS D NZ  1 
ATOM   12944 N  N   . ALA D 4  27   ? -58.232 7.290    98.198  1.00 126.98 ?  27   ALA D N   1 
ATOM   12945 C  CA  . ALA D 4  27   ? -58.036 8.401    99.122  1.00 120.95 ?  27   ALA D CA  1 
ATOM   12946 C  C   . ALA D 4  27   ? -58.734 8.132    100.449 1.00 118.02 ?  27   ALA D C   1 
ATOM   12947 O  O   . ALA D 4  27   ? -58.179 8.410    101.519 1.00 109.90 ?  27   ALA D O   1 
ATOM   12948 C  CB  . ALA D 4  27   ? -58.543 9.701    98.500  1.00 118.57 ?  27   ALA D CB  1 
ATOM   12949 N  N   . ALA D 4  28   ? -59.950 7.581    100.399 1.00 101.70 ?  28   ALA D N   1 
ATOM   12950 C  CA  . ALA D 4  28   ? -60.615 7.151    101.624 1.00 98.19  ?  28   ALA D CA  1 
ATOM   12951 C  C   . ALA D 4  28   ? -59.851 6.022    102.303 1.00 100.06 ?  28   ALA D C   1 
ATOM   12952 O  O   . ALA D 4  28   ? -59.930 5.866    103.527 1.00 95.04  ?  28   ALA D O   1 
ATOM   12953 C  CB  . ALA D 4  28   ? -62.049 6.712    101.324 1.00 96.74  ?  28   ALA D CB  1 
ATOM   12954 N  N   . GLY D 4  29   ? -59.105 5.232    101.531 1.00 129.52 ?  29   GLY D N   1 
ATOM   12955 C  CA  . GLY D 4  29   ? -58.369 4.102    102.060 1.00 128.91 ?  29   GLY D CA  1 
ATOM   12956 C  C   . GLY D 4  29   ? -58.941 2.752    101.694 1.00 130.51 ?  29   GLY D C   1 
ATOM   12957 O  O   . GLY D 4  29   ? -58.335 1.730    102.038 1.00 131.96 ?  29   GLY D O   1 
ATOM   12958 N  N   . TYR D 4  30   ? -60.089 2.710    101.018 1.00 126.97 ?  30   TYR D N   1 
ATOM   12959 C  CA  . TYR D 4  30   ? -60.644 1.441    100.567 1.00 125.27 ?  30   TYR D CA  1 
ATOM   12960 C  C   . TYR D 4  30   ? -59.702 0.790    99.563  1.00 130.18 ?  30   TYR D C   1 
ATOM   12961 O  O   . TYR D 4  30   ? -59.275 1.422    98.592  1.00 131.19 ?  30   TYR D O   1 
ATOM   12962 C  CB  . TYR D 4  30   ? -62.022 1.655    99.939  1.00 123.61 ?  30   TYR D CB  1 
ATOM   12963 C  CG  . TYR D 4  30   ? -63.147 1.817    100.938 1.00 121.68 ?  30   TYR D CG  1 
ATOM   12964 C  CD1 . TYR D 4  30   ? -63.750 0.710    101.520 1.00 125.28 ?  30   TYR D CD1 1 
ATOM   12965 C  CD2 . TYR D 4  30   ? -63.615 3.076    101.288 1.00 125.23 ?  30   TYR D CD2 1 
ATOM   12966 C  CE1 . TYR D 4  30   ? -64.781 0.853    102.431 1.00 126.19 ?  30   TYR D CE1 1 
ATOM   12967 C  CE2 . TYR D 4  30   ? -64.647 3.228    102.197 1.00 125.42 ?  30   TYR D CE2 1 
ATOM   12968 C  CZ  . TYR D 4  30   ? -65.226 2.113    102.765 1.00 123.99 ?  30   TYR D CZ  1 
ATOM   12969 O  OH  . TYR D 4  30   ? -66.253 2.256    103.670 1.00 130.05 ?  30   TYR D OH  1 
ATOM   12970 N  N   . THR D 4  31   ? -59.368 -0.473   99.806  1.00 158.63 ?  31   THR D N   1 
ATOM   12971 C  CA  . THR D 4  31   ? -58.472 -1.221   98.940  1.00 158.38 ?  31   THR D CA  1 
ATOM   12972 C  C   . THR D 4  31   ? -59.117 -2.552   98.576  1.00 153.74 ?  31   THR D C   1 
ATOM   12973 O  O   . THR D 4  31   ? -60.189 -2.907   99.074  1.00 153.80 ?  31   THR D O   1 
ATOM   12974 C  CB  . THR D 4  31   ? -57.104 -1.438   99.602  1.00 151.11 ?  31   THR D CB  1 
ATOM   12975 O  OG1 . THR D 4  31   ? -56.243 -2.165   98.715  1.00 154.46 ?  31   THR D OG1 1 
ATOM   12976 C  CG2 . THR D 4  31   ? -57.258 -2.198   100.907 1.00 146.78 ?  31   THR D CG2 1 
ATOM   12977 N  N   . LYS D 4  32   ? -58.443 -3.289   97.693  1.00 115.39 ?  32   LYS D N   1 
ATOM   12978 C  CA  . LYS D 4  32   ? -58.986 -4.512   97.099  1.00 119.18 ?  32   LYS D CA  1 
ATOM   12979 C  C   . LYS D 4  32   ? -60.344 -4.244   96.452  1.00 122.10 ?  32   LYS D C   1 
ATOM   12980 O  O   . LYS D 4  32   ? -61.316 -4.974   96.653  1.00 121.94 ?  32   LYS D O   1 
ATOM   12981 C  CB  . LYS D 4  32   ? -59.076 -5.639   98.130  1.00 113.19 ?  32   LYS D CB  1 
ATOM   12982 C  CG  . LYS D 4  32   ? -57.724 -6.104   98.646  1.00 110.78 ?  32   LYS D CG  1 
ATOM   12983 C  CD  . LYS D 4  32   ? -57.865 -7.287   99.585  1.00 103.52 ?  32   LYS D CD  1 
ATOM   12984 C  CE  . LYS D 4  32   ? -56.511 -7.840   99.986  1.00 91.79  ?  32   LYS D CE  1 
ATOM   12985 N  NZ  . LYS D 4  32   ? -55.703 -6.847   100.727 1.00 99.39  ?  32   LYS D NZ  1 
ATOM   12986 N  N   . MET D 4  33   ? -60.401 -3.167   95.674  1.00 161.51 ?  33   MET D N   1 
ATOM   12987 C  CA  . MET D 4  33   ? -61.588 -2.778   94.927  1.00 160.92 ?  33   MET D CA  1 
ATOM   12988 C  C   . MET D 4  33   ? -61.306 -2.907   93.438  1.00 165.62 ?  33   MET D C   1 
ATOM   12989 O  O   . MET D 4  33   ? -60.190 -2.637   92.985  1.00 168.12 ?  33   MET D O   1 
ATOM   12990 C  CB  . MET D 4  33   ? -61.998 -1.339   95.252  1.00 157.41 ?  33   MET D CB  1 
ATOM   12991 C  CG  . MET D 4  33   ? -60.821 -0.381   95.348  1.00 158.39 ?  33   MET D CG  1 
ATOM   12992 S  SD  . MET D 4  33   ? -61.300 1.354    95.268  1.00 172.90 ?  33   MET D SD  1 
ATOM   12993 C  CE  . MET D 4  33   ? -59.694 2.140    95.181  1.00 159.62 ?  33   MET D CE  1 
ATOM   12994 N  N   . ASP D 4  34   ? -62.316 -3.319   92.680  1.00 138.24 ?  34   ASP D N   1 
ATOM   12995 C  CA  . ASP D 4  34   ? -62.183 -3.489   91.242  1.00 127.26 ?  34   ASP D CA  1 
ATOM   12996 C  C   . ASP D 4  34   ? -63.338 -2.789   90.542  1.00 114.18 ?  34   ASP D C   1 
ATOM   12997 O  O   . ASP D 4  34   ? -64.456 -2.732   91.062  1.00 120.19 ?  34   ASP D O   1 
ATOM   12998 C  CB  . ASP D 4  34   ? -62.147 -4.975   90.856  1.00 133.01 ?  34   ASP D CB  1 
ATOM   12999 C  CG  . ASP D 4  34   ? -61.456 -5.216   89.528  1.00 131.07 ?  34   ASP D CG  1 
ATOM   13000 O  OD1 . ASP D 4  34   ? -60.867 -4.260   88.981  1.00 128.90 ?  34   ASP D OD1 1 
ATOM   13001 O  OD2 . ASP D 4  34   ? -61.496 -6.362   89.032  1.00 123.24 -1 34   ASP D OD2 1 
ATOM   13002 N  N   . ALA D 4  35   ? -63.056 -2.256   89.355  1.00 96.43  ?  35   ALA D N   1 
ATOM   13003 C  CA  . ALA D 4  35   ? -64.032 -1.518   88.565  1.00 101.89 ?  35   ALA D CA  1 
ATOM   13004 C  C   . ALA D 4  35   ? -64.257 -2.228   87.239  1.00 100.95 ?  35   ALA D C   1 
ATOM   13005 O  O   . ALA D 4  35   ? -63.295 -2.630   86.576  1.00 99.79  ?  35   ALA D O   1 
ATOM   13006 C  CB  . ALA D 4  35   ? -63.571 -0.079   88.326  1.00 104.14 ?  35   ALA D CB  1 
ATOM   13007 N  N   . PHE D 4  36   ? -65.523 -2.365   86.854  1.00 95.93  ?  36   PHE D N   1 
ATOM   13008 C  CA  . PHE D 4  36   ? -65.927 -3.104   85.664  1.00 88.44  ?  36   PHE D CA  1 
ATOM   13009 C  C   . PHE D 4  36   ? -66.426 -2.118   84.615  1.00 94.19  ?  36   PHE D C   1 
ATOM   13010 O  O   . PHE D 4  36   ? -67.333 -1.324   84.888  1.00 102.14 ?  36   PHE D O   1 
ATOM   13011 C  CB  . PHE D 4  36   ? -67.010 -4.127   86.007  1.00 89.95  ?  36   PHE D CB  1 
ATOM   13012 C  CG  . PHE D 4  36   ? -66.748 -4.883   87.281  1.00 92.59  ?  36   PHE D CG  1 
ATOM   13013 C  CD1 . PHE D 4  36   ? -66.035 -6.069   87.264  1.00 93.16  ?  36   PHE D CD1 1 
ATOM   13014 C  CD2 . PHE D 4  36   ? -67.214 -4.407   88.496  1.00 96.98  ?  36   PHE D CD2 1 
ATOM   13015 C  CE1 . PHE D 4  36   ? -65.788 -6.766   88.429  1.00 93.01  ?  36   PHE D CE1 1 
ATOM   13016 C  CE2 . PHE D 4  36   ? -66.970 -5.100   89.665  1.00 104.30 ?  36   PHE D CE2 1 
ATOM   13017 C  CZ  . PHE D 4  36   ? -66.256 -6.282   89.631  1.00 99.96  ?  36   PHE D CZ  1 
ATOM   13018 N  N   . SER D 4  37   ? -65.840 -2.173   83.424  1.00 91.24  ?  37   SER D N   1 
ATOM   13019 C  CA  . SER D 4  37   ? -66.156 -1.247   82.349  1.00 89.35  ?  37   SER D CA  1 
ATOM   13020 C  C   . SER D 4  37   ? -66.209 -1.988   81.022  1.00 95.47  ?  37   SER D C   1 
ATOM   13021 O  O   . SER D 4  37   ? -65.455 -2.946   80.810  1.00 94.97  ?  37   SER D O   1 
ATOM   13022 C  CB  . SER D 4  37   ? -65.119 -0.117   82.267  1.00 82.61  ?  37   SER D CB  1 
ATOM   13023 O  OG  . SER D 4  37   ? -65.277 0.638    81.080  1.00 97.55  ?  37   SER D OG  1 
ATOM   13024 N  N   . PRO D 4  38   ? -67.094 -1.570   80.113  1.00 112.28 ?  38   PRO D N   1 
ATOM   13025 C  CA  . PRO D 4  38   ? -67.156 -2.235   78.800  1.00 107.01 ?  38   PRO D CA  1 
ATOM   13026 C  C   . PRO D 4  38   ? -65.883 -2.086   77.988  1.00 105.28 ?  38   PRO D C   1 
ATOM   13027 O  O   . PRO D 4  38   ? -65.489 -3.030   77.295  1.00 110.36 ?  38   PRO D O   1 
ATOM   13028 C  CB  . PRO D 4  38   ? -68.351 -1.552   78.115  1.00 108.12 ?  38   PRO D CB  1 
ATOM   13029 C  CG  . PRO D 4  38   ? -68.618 -0.308   78.922  1.00 112.69 ?  38   PRO D CG  1 
ATOM   13030 C  CD  . PRO D 4  38   ? -68.213 -0.638   80.316  1.00 118.73 ?  38   PRO D CD  1 
ATOM   13031 N  N   . PHE D 4  39   ? -65.233 -0.931   78.050  1.00 91.37  ?  39   PHE D N   1 
ATOM   13032 C  CA  . PHE D 4  39   ? -63.980 -0.677   77.362  1.00 96.23  ?  39   PHE D CA  1 
ATOM   13033 C  C   . PHE D 4  39   ? -62.906 -0.294   78.372  1.00 101.65 ?  39   PHE D C   1 
ATOM   13034 O  O   . PHE D 4  39   ? -63.216 0.177    79.473  1.00 103.49 ?  39   PHE D O   1 
ATOM   13035 C  CB  . PHE D 4  39   ? -64.144 0.436    76.314  1.00 95.73  ?  39   PHE D CB  1 
ATOM   13036 C  CG  . PHE D 4  39   ? -64.469 1.788    76.893  1.00 95.57  ?  39   PHE D CG  1 
ATOM   13037 C  CD1 . PHE D 4  39   ? -63.462 2.652    77.297  1.00 96.24  ?  39   PHE D CD1 1 
ATOM   13038 C  CD2 . PHE D 4  39   ? -65.785 2.197    77.024  1.00 95.05  ?  39   PHE D CD2 1 
ATOM   13039 C  CE1 . PHE D 4  39   ? -63.764 3.895    77.826  1.00 96.91  ?  39   PHE D CE1 1 
ATOM   13040 C  CE2 . PHE D 4  39   ? -66.092 3.438    77.550  1.00 97.23  ?  39   PHE D CE2 1 
ATOM   13041 C  CZ  . PHE D 4  39   ? -65.082 4.288    77.951  1.00 98.58  ?  39   PHE D CZ  1 
ATOM   13042 N  N   . PRO D 4  40   ? -61.631 -0.502   78.041  1.00 142.24 ?  40   PRO D N   1 
ATOM   13043 C  CA  . PRO D 4  40   ? -60.556 -0.074   78.951  1.00 139.62 ?  40   PRO D CA  1 
ATOM   13044 C  C   . PRO D 4  40   ? -60.561 1.437    79.131  1.00 148.13 ?  40   PRO D C   1 
ATOM   13045 O  O   . PRO D 4  40   ? -60.355 2.197    78.182  1.00 156.41 ?  40   PRO D O   1 
ATOM   13046 C  CB  . PRO D 4  40   ? -59.281 -0.572   78.257  1.00 133.91 ?  40   PRO D CB  1 
ATOM   13047 C  CG  . PRO D 4  40   ? -59.668 -0.828   76.842  1.00 138.78 ?  40   PRO D CG  1 
ATOM   13048 C  CD  . PRO D 4  40   ? -61.111 -1.215   76.862  1.00 144.60 ?  40   PRO D CD  1 
ATOM   13049 N  N   . ILE D 4  41   ? -60.819 1.869    80.368  1.00 142.10 ?  41   ILE D N   1 
ATOM   13050 C  CA  . ILE D 4  41   ? -60.908 3.297    80.660  1.00 143.46 ?  41   ILE D CA  1 
ATOM   13051 C  C   . ILE D 4  41   ? -59.561 3.977    80.450  1.00 144.70 ?  41   ILE D C   1 
ATOM   13052 O  O   . ILE D 4  41   ? -59.497 5.132    80.008  1.00 153.77 ?  41   ILE D O   1 
ATOM   13053 C  CB  . ILE D 4  41   ? -61.434 3.518    82.090  1.00 143.06 ?  41   ILE D CB  1 
ATOM   13054 C  CG1 . ILE D 4  41   ? -62.779 2.812    82.281  1.00 134.20 ?  41   ILE D CG1 1 
ATOM   13055 C  CG2 . ILE D 4  41   ? -61.554 5.002    82.396  1.00 146.95 ?  41   ILE D CG2 1 
ATOM   13056 C  CD1 . ILE D 4  41   ? -63.968 3.580    81.729  1.00 134.27 ?  41   ILE D CD1 1 
ATOM   13057 N  N   . GLU D 4  42   ? -58.470 3.275    80.761  1.00 115.51 ?  42   GLU D N   1 
ATOM   13058 C  CA  . GLU D 4  42   ? -57.091 3.758    80.743  1.00 118.99 ?  42   GLU D CA  1 
ATOM   13059 C  C   . GLU D 4  42   ? -56.850 4.798    81.829  1.00 122.04 ?  42   GLU D C   1 
ATOM   13060 O  O   . GLU D 4  42   ? -55.715 5.259    81.984  1.00 123.67 ?  42   GLU D O   1 
ATOM   13061 C  CB  . GLU D 4  42   ? -56.674 4.332    79.379  1.00 125.27 ?  42   GLU D CB  1 
ATOM   13062 C  CG  . GLU D 4  42   ? -56.713 3.319    78.243  1.00 137.57 ?  42   GLU D CG  1 
ATOM   13063 C  CD  . GLU D 4  42   ? -55.636 2.258    78.354  1.00 137.22 ?  42   GLU D CD  1 
ATOM   13064 O  OE1 . GLU D 4  42   ? -54.549 2.559    78.892  1.00 139.54 ?  42   GLU D OE1 1 
ATOM   13065 O  OE2 . GLU D 4  42   ? -55.883 1.121    77.898  1.00 127.38 -1 42   GLU D OE2 1 
ATOM   13066 N  N   . GLU D 4  43   ? -57.879 5.178    82.586  1.00 168.23 ?  43   GLU D N   1 
ATOM   13067 C  CA  . GLU D 4  43   ? -57.763 6.074    83.729  1.00 174.52 ?  43   GLU D CA  1 
ATOM   13068 C  C   . GLU D 4  43   ? -58.017 5.349    85.038  1.00 165.58 ?  43   GLU D C   1 
ATOM   13069 O  O   . GLU D 4  43   ? -57.296 5.556    86.017  1.00 169.19 ?  43   GLU D O   1 
ATOM   13070 C  CB  . GLU D 4  43   ? -58.744 7.248    83.590  1.00 174.98 ?  43   GLU D CB  1 
ATOM   13071 C  CG  . GLU D 4  43   ? -58.610 8.028    82.293  1.00 174.66 ?  43   GLU D CG  1 
ATOM   13072 C  CD  . GLU D 4  43   ? -57.421 8.969    82.283  1.00 177.28 ?  43   GLU D CD  1 
ATOM   13073 O  OE1 . GLU D 4  43   ? -56.917 9.300    83.378  1.00 171.49 ?  43   GLU D OE1 1 
ATOM   13074 O  OE2 . GLU D 4  43   ? -57.001 9.377    81.177  1.00 175.90 -1 43   GLU D OE2 1 
ATOM   13075 N  N   . VAL D 4  44   ? -59.043 4.495    85.074  1.00 104.66 ?  44   VAL D N   1 
ATOM   13076 C  CA  . VAL D 4  44   ? -59.242 3.608    86.213  1.00 101.44 ?  44   VAL D CA  1 
ATOM   13077 C  C   . VAL D 4  44   ? -58.134 2.566    86.269  1.00 111.32 ?  44   VAL D C   1 
ATOM   13078 O  O   . VAL D 4  44   ? -57.714 2.139    87.352  1.00 114.47 ?  44   VAL D O   1 
ATOM   13079 C  CB  . VAL D 4  44   ? -60.634 2.956    86.131  1.00 104.35 ?  44   VAL D CB  1 
ATOM   13080 C  CG1 . VAL D 4  44   ? -60.784 1.863    87.175  1.00 100.11 ?  44   VAL D CG1 1 
ATOM   13081 C  CG2 . VAL D 4  44   ? -61.722 4.010    86.292  1.00 107.28 ?  44   VAL D CG2 1 
ATOM   13082 N  N   . ILE D 4  45   ? -57.629 2.159    85.101  1.00 155.31 ?  45   ILE D N   1 
ATOM   13083 C  CA  . ILE D 4  45   ? -56.623 1.103    85.037  1.00 156.78 ?  45   ILE D CA  1 
ATOM   13084 C  C   . ILE D 4  45   ? -55.365 1.514    85.791  1.00 162.15 ?  45   ILE D C   1 
ATOM   13085 O  O   . ILE D 4  45   ? -54.798 0.728    86.560  1.00 166.74 ?  45   ILE D O   1 
ATOM   13086 C  CB  . ILE D 4  45   ? -56.311 0.751    83.572  1.00 148.04 ?  45   ILE D CB  1 
ATOM   13087 C  CG1 . ILE D 4  45   ? -57.605 0.639    82.765  1.00 145.56 ?  45   ILE D CG1 1 
ATOM   13088 C  CG2 . ILE D 4  45   ? -55.514 -0.540   83.491  1.00 148.50 ?  45   ILE D CG2 1 
ATOM   13089 C  CD1 . ILE D 4  45   ? -58.453 -0.559   83.125  1.00 142.04 ?  45   ILE D CD1 1 
ATOM   13090 N  N   . GLU D 4  46   ? -54.909 2.752    85.583  1.00 182.96 ?  46   GLU D N   1 
ATOM   13091 C  CA  . GLU D 4  46   ? -53.696 3.212    86.252  1.00 186.50 ?  46   GLU D CA  1 
ATOM   13092 C  C   . GLU D 4  46   ? -53.915 3.428    87.745  1.00 182.17 ?  46   GLU D C   1 
ATOM   13093 O  O   . GLU D 4  46   ? -52.958 3.356    88.526  1.00 179.89 ?  46   GLU D O   1 
ATOM   13094 C  CB  . GLU D 4  46   ? -53.189 4.497    85.597  1.00 188.01 ?  46   GLU D CB  1 
ATOM   13095 C  CG  . GLU D 4  46   ? -54.213 5.614    85.553  1.00 192.08 ?  46   GLU D CG  1 
ATOM   13096 C  CD  . GLU D 4  46   ? -53.829 6.808    86.406  1.00 200.97 ?  46   GLU D CD  1 
ATOM   13097 O  OE1 . GLU D 4  46   ? -52.660 6.884    86.839  1.00 201.60 ?  46   GLU D OE1 1 
ATOM   13098 O  OE2 . GLU D 4  46   ? -54.696 7.677    86.637  1.00 201.65 -1 46   GLU D OE2 1 
ATOM   13099 N  N   . GLU D 4  47   ? -55.159 3.679    88.165  1.00 147.34 ?  47   GLU D N   1 
ATOM   13100 C  CA  . GLU D 4  47   ? -55.413 3.962    89.574  1.00 148.17 ?  47   GLU D CA  1 
ATOM   13101 C  C   . GLU D 4  47   ? -55.265 2.715    90.442  1.00 142.20 ?  47   GLU D C   1 
ATOM   13102 O  O   . GLU D 4  47   ? -54.653 2.772    91.514  1.00 139.77 ?  47   GLU D O   1 
ATOM   13103 C  CB  . GLU D 4  47   ? -56.803 4.574    89.749  1.00 149.79 ?  47   GLU D CB  1 
ATOM   13104 C  CG  . GLU D 4  47   ? -56.957 5.391    91.026  1.00 154.02 ?  47   GLU D CG  1 
ATOM   13105 C  CD  . GLU D 4  47   ? -56.297 6.757    90.955  1.00 159.19 ?  47   GLU D CD  1 
ATOM   13106 O  OE1 . GLU D 4  47   ? -55.816 7.139    89.867  1.00 161.42 ?  47   GLU D OE1 1 
ATOM   13107 O  OE2 . GLU D 4  47   ? -56.262 7.446    91.997  1.00 154.94 -1 47   GLU D OE2 1 
ATOM   13108 N  N   . ILE D 4  48   ? -55.806 1.582    90.000  1.00 124.07 ?  48   ILE D N   1 
ATOM   13109 C  CA  . ILE D 4  48   ? -55.838 0.377    90.826  1.00 118.05 ?  48   ILE D CA  1 
ATOM   13110 C  C   . ILE D 4  48   ? -54.897 -0.715   90.342  1.00 118.37 ?  48   ILE D C   1 
ATOM   13111 O  O   . ILE D 4  48   ? -54.664 -1.679   91.090  1.00 116.44 ?  48   ILE D O   1 
ATOM   13112 C  CB  . ILE D 4  48   ? -57.270 -0.189   90.950  1.00 112.82 ?  48   ILE D CB  1 
ATOM   13113 C  CG1 . ILE D 4  48   ? -57.948 -0.273   89.581  1.00 114.36 ?  48   ILE D CG1 1 
ATOM   13114 C  CG2 . ILE D 4  48   ? -58.099 0.653    91.910  1.00 122.97 ?  48   ILE D CG2 1 
ATOM   13115 C  CD1 . ILE D 4  48   ? -59.396 -0.731   89.660  1.00 106.35 ?  48   ILE D CD1 1 
ATOM   13116 N  N   . ALA D 4  49   ? -54.353 -0.615   89.121  1.00 155.62 ?  49   ALA D N   1 
ATOM   13117 C  CA  . ALA D 4  49   ? -53.495 -1.669   88.564  1.00 149.84 ?  49   ALA D CA  1 
ATOM   13118 C  C   . ALA D 4  49   ? -52.337 -1.023   87.800  1.00 155.59 ?  49   ALA D C   1 
ATOM   13119 O  O   . ALA D 4  49   ? -52.346 -0.942   86.570  1.00 159.67 ?  49   ALA D O   1 
ATOM   13120 C  CB  . ALA D 4  49   ? -54.294 -2.615   87.669  1.00 151.19 ?  49   ALA D CB  1 
ATOM   13121 N  N   . HIS D 4  50   ? -51.325 -0.575   88.535  1.00 163.45 ?  50   HIS D N   1 
ATOM   13122 C  CA  . HIS D 4  50   ? -50.108 -0.028   87.947  1.00 171.15 ?  50   HIS D CA  1 
ATOM   13123 C  C   . HIS D 4  50   ? -48.949 -0.957   88.277  1.00 167.74 ?  50   HIS D C   1 
ATOM   13124 O  O   . HIS D 4  50   ? -48.635 -1.169   89.453  1.00 166.27 ?  50   HIS D O   1 
ATOM   13125 C  CB  . HIS D 4  50   ? -49.826 1.387    88.453  1.00 178.66 ?  50   HIS D CB  1 
ATOM   13126 C  CG  . HIS D 4  50   ? -49.090 2.241    87.468  1.00 189.66 ?  50   HIS D CG  1 
ATOM   13127 N  ND1 . HIS D 4  50   ? -49.689 2.762    86.342  1.00 187.07 ?  50   HIS D ND1 1 
ATOM   13128 C  CD2 . HIS D 4  50   ? -47.802 2.658    87.437  1.00 192.83 ?  50   HIS D CD2 1 
ATOM   13129 C  CE1 . HIS D 4  50   ? -48.803 3.468    85.662  1.00 182.78 ?  50   HIS D CE1 1 
ATOM   13130 N  NE2 . HIS D 4  50   ? -47.651 3.421    86.305  1.00 189.05 ?  50   HIS D NE2 1 
ATOM   13131 N  N   . GLY D 4  51   ? -48.330 -1.507   87.248  1.00 136.09 ?  51   GLY D N   1 
ATOM   13132 C  CA  . GLY D 4  51   ? -47.224 -2.426   87.423  1.00 130.30 ?  51   GLY D CA  1 
ATOM   13133 C  C   . GLY D 4  51   ? -47.122 -3.360   86.235  1.00 124.03 ?  51   GLY D C   1 
ATOM   13134 O  O   . GLY D 4  51   ? -47.874 -3.259   85.268  1.00 119.47 ?  51   GLY D O   1 
ATOM   13135 N  N   . ASP D 4  52   ? -46.162 -4.278   86.330  1.00 158.26 ?  52   ASP D N   1 
ATOM   13136 C  CA  . ASP D 4  52   ? -45.945 -5.248   85.264  1.00 156.24 ?  52   ASP D CA  1 
ATOM   13137 C  C   . ASP D 4  52   ? -47.119 -6.213   85.176  1.00 149.71 ?  52   ASP D C   1 
ATOM   13138 O  O   . ASP D 4  52   ? -47.583 -6.741   86.191  1.00 147.75 ?  52   ASP D O   1 
ATOM   13139 C  CB  . ASP D 4  52   ? -44.650 -6.022   85.499  1.00 155.38 ?  52   ASP D CB  1 
ATOM   13140 C  CG  . ASP D 4  52   ? -44.288 -6.919   84.329  1.00 154.67 ?  52   ASP D CG  1 
ATOM   13141 O  OD1 . ASP D 4  52   ? -44.763 -6.653   83.204  1.00 146.89 ?  52   ASP D OD1 1 
ATOM   13142 O  OD2 . ASP D 4  52   ? -43.532 -7.892   84.535  1.00 152.74 -1 52   ASP D OD2 1 
ATOM   13143 N  N   . THR D 4  53   ? -47.604 -6.440   83.953  1.00 110.65 ?  53   THR D N   1 
ATOM   13144 C  CA  . THR D 4  53   ? -48.657 -7.429   83.755  1.00 102.09 ?  53   THR D CA  1 
ATOM   13145 C  C   . THR D 4  53   ? -48.158 -8.838   84.041  1.00 102.90 ?  53   THR D C   1 
ATOM   13146 O  O   . THR D 4  53   ? -48.950 -9.716   84.403  1.00 101.93 ?  53   THR D O   1 
ATOM   13147 C  CB  . THR D 4  53   ? -49.198 -7.346   82.327  1.00 103.59 ?  53   THR D CB  1 
ATOM   13148 O  OG1 . THR D 4  53   ? -48.161 -7.698   81.402  1.00 112.30 ?  53   THR D OG1 1 
ATOM   13149 C  CG2 . THR D 4  53   ? -49.684 -5.939   82.020  1.00 109.72 ?  53   THR D CG2 1 
ATOM   13150 N  N   . GLY D 4  54   ? -46.852 -9.070   83.905  1.00 113.75 ?  54   GLY D N   1 
ATOM   13151 C  CA  . GLY D 4  54   ? -46.292 -10.401  83.987  1.00 118.75 ?  54   GLY D CA  1 
ATOM   13152 C  C   . GLY D 4  54   ? -46.295 -11.158  82.679  1.00 114.45 ?  54   GLY D C   1 
ATOM   13153 O  O   . GLY D 4  54   ? -45.591 -12.170  82.562  1.00 109.00 ?  54   GLY D O   1 
ATOM   13154 N  N   . VAL D 4  55   ? -47.069 -10.699  81.693  1.00 113.61 ?  55   VAL D N   1 
ATOM   13155 C  CA  . VAL D 4  55   ? -47.043 -11.331  80.371  1.00 103.45 ?  55   VAL D CA  1 
ATOM   13156 C  C   . VAL D 4  55   ? -45.676 -11.226  79.707  1.00 102.26 ?  55   VAL D C   1 
ATOM   13157 O  O   . VAL D 4  55   ? -45.231 -12.217  79.109  1.00 101.62 ?  55   VAL D O   1 
ATOM   13158 C  CB  . VAL D 4  55   ? -48.179 -10.777  79.500  1.00 109.45 ?  55   VAL D CB  1 
ATOM   13159 C  CG1 . VAL D 4  55   ? -48.120 -11.363  78.096  1.00 110.31 ?  55   VAL D CG1 1 
ATOM   13160 C  CG2 . VAL D 4  55   ? -49.530 -11.061  80.147  1.00 106.76 ?  55   VAL D CG2 1 
ATOM   13161 N  N   . PRO D 4  56   ? -44.958 -10.089  79.754  1.00 74.59  ?  56   PRO D N   1 
ATOM   13162 C  CA  . PRO D 4  56   ? -43.693 -10.005  78.999  1.00 67.04  ?  56   PRO D CA  1 
ATOM   13163 C  C   . PRO D 4  56   ? -42.663 -11.059  79.363  1.00 70.56  ?  56   PRO D C   1 
ATOM   13164 O  O   . PRO D 4  56   ? -42.016 -11.602  78.460  1.00 71.12  ?  56   PRO D O   1 
ATOM   13165 C  CB  . PRO D 4  56   ? -43.190 -8.594   79.328  1.00 61.28  ?  56   PRO D CB  1 
ATOM   13166 C  CG  . PRO D 4  56   ? -44.424 -7.825   79.553  1.00 76.26  ?  56   PRO D CG  1 
ATOM   13167 C  CD  . PRO D 4  56   ? -45.334 -8.766   80.289  1.00 78.98  ?  56   PRO D CD  1 
ATOM   13168 N  N   . ARG D 4  57   ? -42.477 -11.365  80.651  1.00 91.49  ?  57   ARG D N   1 
ATOM   13169 C  CA  . ARG D 4  57   ? -41.435 -12.319  81.027  1.00 95.28  ?  57   ARG D CA  1 
ATOM   13170 C  C   . ARG D 4  57   ? -41.737 -13.710  80.482  1.00 88.27  ?  57   ARG D C   1 
ATOM   13171 O  O   . ARG D 4  57   ? -40.819 -14.451  80.108  1.00 84.20  ?  57   ARG D O   1 
ATOM   13172 C  CB  . ARG D 4  57   ? -41.266 -12.361  82.548  1.00 103.07 ?  57   ARG D CB  1 
ATOM   13173 C  CG  . ARG D 4  57   ? -42.447 -12.943  83.312  1.00 105.52 ?  57   ARG D CG  1 
ATOM   13174 C  CD  . ARG D 4  57   ? -42.860 -12.053  84.470  1.00 118.58 ?  57   ARG D CD  1 
ATOM   13175 N  NE  . ARG D 4  57   ? -41.706 -11.566  85.217  1.00 122.85 ?  57   ARG D NE  1 
ATOM   13176 C  CZ  . ARG D 4  57   ? -41.769 -10.689  86.209  1.00 133.71 ?  57   ARG D CZ  1 
ATOM   13177 N  NH1 . ARG D 4  57   ? -42.924 -10.180  86.609  1.00 120.97 ?  57   ARG D NH1 1 
ATOM   13178 N  NH2 . ARG D 4  57   ? -40.647 -10.316  86.818  1.00 145.92 ?  57   ARG D NH2 1 
ATOM   13179 N  N   . LEU D 4  58   ? -43.018 -14.079  80.422  1.00 86.35  ?  58   LEU D N   1 
ATOM   13180 C  CA  . LEU D 4  58   ? -43.390 -15.371  79.857  1.00 84.19  ?  58   LEU D CA  1 
ATOM   13181 C  C   . LEU D 4  58   ? -43.081 -15.423  78.367  1.00 83.77  ?  58   LEU D C   1 
ATOM   13182 O  O   . LEU D 4  58   ? -42.629 -16.453  77.852  1.00 80.07  ?  58   LEU D O   1 
ATOM   13183 C  CB  . LEU D 4  58   ? -44.874 -15.641  80.104  1.00 87.14  ?  58   LEU D CB  1 
ATOM   13184 C  CG  . LEU D 4  58   ? -45.373 -15.516  81.545  1.00 89.01  ?  58   LEU D CG  1 
ATOM   13185 C  CD1 . LEU D 4  58   ? -46.892 -15.570  81.592  1.00 91.36  ?  58   LEU D CD1 1 
ATOM   13186 C  CD2 . LEU D 4  58   ? -44.773 -16.609  82.416  1.00 94.63  ?  58   LEU D CD2 1 
ATOM   13187 N  N   . VAL D 4  59   ? -43.313 -14.315  77.661  1.00 108.32 ?  59   VAL D N   1 
ATOM   13188 C  CA  . VAL D 4  59   ? -43.086 -14.276  76.218  1.00 107.24 ?  59   VAL D CA  1 
ATOM   13189 C  C   . VAL D 4  59   ? -41.603 -14.437  75.907  1.00 106.42 ?  59   VAL D C   1 
ATOM   13190 O  O   . VAL D 4  59   ? -41.215 -15.214  75.026  1.00 112.34 ?  59   VAL D O   1 
ATOM   13191 C  CB  . VAL D 4  59   ? -43.650 -12.972  75.627  1.00 110.08 ?  59   VAL D CB  1 
ATOM   13192 C  CG1 . VAL D 4  59   ? -43.198 -12.796  74.188  1.00 110.26 ?  59   VAL D CG1 1 
ATOM   13193 C  CG2 . VAL D 4  59   ? -45.167 -12.966  75.719  1.00 109.25 ?  59   VAL D CG2 1 
ATOM   13194 N  N   . LEU D 4  60   ? -40.750 -13.705  76.628  1.00 65.60  ?  60   LEU D N   1 
ATOM   13195 C  CA  . LEU D 4  60   ? -39.313 -13.779  76.379  1.00 65.28  ?  60   LEU D CA  1 
ATOM   13196 C  C   . LEU D 4  60   ? -38.752 -15.154  76.722  1.00 64.18  ?  60   LEU D C   1 
ATOM   13197 O  O   . LEU D 4  60   ? -37.931 -15.698  75.973  1.00 59.59  ?  60   LEU D O   1 
ATOM   13198 C  CB  . LEU D 4  60   ? -38.586 -12.693  77.171  1.00 61.80  ?  60   LEU D CB  1 
ATOM   13199 C  CG  . LEU D 4  60   ? -37.105 -12.511  76.833  1.00 49.71  ?  60   LEU D CG  1 
ATOM   13200 C  CD1 . LEU D 4  60   ? -36.906 -12.300  75.340  1.00 55.47  ?  60   LEU D CD1 1 
ATOM   13201 C  CD2 . LEU D 4  60   ? -36.497 -11.366  77.626  1.00 55.63  ?  60   LEU D CD2 1 
ATOM   13202 N  N   . LEU D 4  61   ? -39.178 -15.729  77.849  1.00 87.99  ?  61   LEU D N   1 
ATOM   13203 C  CA  . LEU D 4  61   ? -38.674 -17.039  78.252  1.00 89.03  ?  61   LEU D CA  1 
ATOM   13204 C  C   . LEU D 4  61   ? -39.024 -18.105  77.222  1.00 88.91  ?  61   LEU D C   1 
ATOM   13205 O  O   . LEU D 4  61   ? -38.153 -18.852  76.763  1.00 92.06  ?  61   LEU D O   1 
ATOM   13206 C  CB  . LEU D 4  61   ? -39.232 -17.419  79.624  1.00 79.69  ?  61   LEU D CB  1 
ATOM   13207 C  CG  . LEU D 4  61   ? -38.812 -18.789  80.160  1.00 77.95  ?  61   LEU D CG  1 
ATOM   13208 C  CD1 . LEU D 4  61   ? -37.311 -18.838  80.382  1.00 79.45  ?  61   LEU D CD1 1 
ATOM   13209 C  CD2 . LEU D 4  61   ? -39.559 -19.123  81.444  1.00 90.26  ?  61   LEU D CD2 1 
ATOM   13210 N  N   . PHE D 4  62   ? -40.301 -18.187  76.844  1.00 102.62 ?  62   PHE D N   1 
ATOM   13211 C  CA  . PHE D 4  62   ? -40.722 -19.209  75.893  1.00 106.88 ?  62   PHE D CA  1 
ATOM   13212 C  C   . PHE D 4  62   ? -40.204 -18.919  74.490  1.00 107.96 ?  62   PHE D C   1 
ATOM   13213 O  O   . PHE D 4  62   ? -39.928 -19.852  73.727  1.00 102.40 ?  62   PHE D O   1 
ATOM   13214 C  CB  . PHE D 4  62   ? -42.245 -19.321  75.891  1.00 111.66 ?  62   PHE D CB  1 
ATOM   13215 C  CG  . PHE D 4  62   ? -42.793 -20.092  77.056  1.00 118.23 ?  62   PHE D CG  1 
ATOM   13216 C  CD1 . PHE D 4  62   ? -42.631 -21.464  77.134  1.00 121.84 ?  62   PHE D CD1 1 
ATOM   13217 C  CD2 . PHE D 4  62   ? -43.470 -19.443  78.076  1.00 118.83 ?  62   PHE D CD2 1 
ATOM   13218 C  CE1 . PHE D 4  62   ? -43.134 -22.174  78.208  1.00 125.04 ?  62   PHE D CE1 1 
ATOM   13219 C  CE2 . PHE D 4  62   ? -43.976 -20.146  79.150  1.00 118.39 ?  62   PHE D CE2 1 
ATOM   13220 C  CZ  . PHE D 4  62   ? -43.808 -21.512  79.217  1.00 117.16 ?  62   PHE D CZ  1 
ATOM   13221 N  N   . GLY D 4  63   ? -40.063 -17.640  74.136  1.00 95.72  ?  63   GLY D N   1 
ATOM   13222 C  CA  . GLY D 4  63   ? -39.547 -17.299  72.821  1.00 88.79  ?  63   GLY D CA  1 
ATOM   13223 C  C   . GLY D 4  63   ? -38.104 -17.725  72.631  1.00 85.62  ?  63   GLY D C   1 
ATOM   13224 O  O   . GLY D 4  63   ? -37.743 -18.275  71.587  1.00 89.58  ?  63   GLY D O   1 
ATOM   13225 N  N   . LEU D 4  64   ? -37.260 -17.480  73.635  1.00 71.32  ?  64   LEU D N   1 
ATOM   13226 C  CA  . LEU D 4  64   ? -35.872 -17.925  73.557  1.00 72.98  ?  64   LEU D CA  1 
ATOM   13227 C  C   . LEU D 4  64   ? -35.783 -19.445  73.566  1.00 72.81  ?  64   LEU D C   1 
ATOM   13228 O  O   . LEU D 4  64   ? -34.943 -20.027  72.868  1.00 76.36  ?  64   LEU D O   1 
ATOM   13229 C  CB  . LEU D 4  64   ? -35.064 -17.327  74.708  1.00 77.36  ?  64   LEU D CB  1 
ATOM   13230 C  CG  . LEU D 4  64   ? -34.841 -15.815  74.645  1.00 81.17  ?  64   LEU D CG  1 
ATOM   13231 C  CD1 . LEU D 4  64   ? -33.982 -15.350  75.809  1.00 87.62  ?  64   LEU D CD1 1 
ATOM   13232 C  CD2 . LEU D 4  64   ? -34.210 -15.417  73.315  1.00 74.60  ?  64   LEU D CD2 1 
ATOM   13233 N  N   . ILE D 4  65   ? -36.638 -20.105  74.351  1.00 77.46  ?  65   ILE D N   1 
ATOM   13234 C  CA  . ILE D 4  65   ? -36.712 -21.563  74.306  1.00 79.29  ?  65   ILE D CA  1 
ATOM   13235 C  C   . ILE D 4  65   ? -37.138 -22.026  72.920  1.00 81.38  ?  65   ILE D C   1 
ATOM   13236 O  O   . ILE D 4  65   ? -36.592 -22.993  72.376  1.00 84.64  ?  65   ILE D O   1 
ATOM   13237 C  CB  . ILE D 4  65   ? -37.667 -22.086  75.396  1.00 87.66  ?  65   ILE D CB  1 
ATOM   13238 C  CG1 . ILE D 4  65   ? -37.098 -21.819  76.790  1.00 88.96  ?  65   ILE D CG1 1 
ATOM   13239 C  CG2 . ILE D 4  65   ? -37.935 -23.574  75.213  1.00 71.08  ?  65   ILE D CG2 1 
ATOM   13240 C  CD1 . ILE D 4  65   ? -38.029 -22.226  77.912  1.00 74.48  ?  65   ILE D CD1 1 
ATOM   13241 N  N   . GLY D 4  66   ? -38.111 -21.335  72.321  1.00 85.93  ?  66   GLY D N   1 
ATOM   13242 C  CA  . GLY D 4  66   ? -38.582 -21.727  71.003  1.00 88.55  ?  66   GLY D CA  1 
ATOM   13243 C  C   . GLY D 4  66   ? -37.515 -21.591  69.935  1.00 91.40  ?  66   GLY D C   1 
ATOM   13244 O  O   . GLY D 4  66   ? -37.342 -22.478  69.095  1.00 95.99  ?  66   GLY D O   1 
ATOM   13245 N  N   . ALA D 4  67   ? -36.783 -20.475  69.953  1.00 69.12  ?  67   ALA D N   1 
ATOM   13246 C  CA  . ALA D 4  67   ? -35.707 -20.284  68.987  1.00 67.20  ?  67   ALA D CA  1 
ATOM   13247 C  C   . ALA D 4  67   ? -34.607 -21.320  69.182  1.00 69.58  ?  67   ALA D C   1 
ATOM   13248 O  O   . ALA D 4  67   ? -34.139 -21.936  68.218  1.00 75.39  ?  67   ALA D O   1 
ATOM   13249 C  CB  . ALA D 4  67   ? -35.144 -18.866  69.099  1.00 70.04  ?  67   ALA D CB  1 
ATOM   13250 N  N   . ALA D 4  68   ? -34.189 -21.532  70.433  1.00 52.36  ?  68   ALA D N   1 
ATOM   13251 C  CA  . ALA D 4  68   ? -33.158 -22.528  70.708  1.00 49.43  ?  68   ALA D CA  1 
ATOM   13252 C  C   . ALA D 4  68   ? -33.613 -23.922  70.298  1.00 55.53  ?  68   ALA D C   1 
ATOM   13253 O  O   . ALA D 4  68   ? -32.825 -24.704  69.753  1.00 59.14  ?  68   ALA D O   1 
ATOM   13254 C  CB  . ALA D 4  68   ? -32.782 -22.499  72.189  1.00 50.05  ?  68   ALA D CB  1 
ATOM   13255 N  N   . SER D 4  69   ? -34.884 -24.248  70.544  1.00 58.37  ?  69   SER D N   1 
ATOM   13256 C  CA  . SER D 4  69   ? -35.399 -25.565  70.180  1.00 59.12  ?  69   SER D CA  1 
ATOM   13257 C  C   . SER D 4  69   ? -35.337 -25.791  68.674  1.00 65.94  ?  69   SER D C   1 
ATOM   13258 O  O   . SER D 4  69   ? -34.996 -26.890  68.219  1.00 61.38  ?  69   SER D O   1 
ATOM   13259 C  CB  . SER D 4  69   ? -36.833 -25.724  70.686  1.00 60.38  ?  69   SER D CB  1 
ATOM   13260 O  OG  . SER D 4  69   ? -36.889 -25.630  72.099  1.00 70.97  ?  69   SER D OG  1 
ATOM   13261 N  N   . GLY D 4  70   ? -35.659 -24.762  67.887  1.00 71.19  ?  70   GLY D N   1 
ATOM   13262 C  CA  . GLY D 4  70   ? -35.631 -24.910  66.440  1.00 68.82  ?  70   GLY D CA  1 
ATOM   13263 C  C   . GLY D 4  70   ? -34.230 -25.110  65.896  1.00 63.55  ?  70   GLY D C   1 
ATOM   13264 O  O   . GLY D 4  70   ? -34.012 -25.941  65.009  1.00 58.91  ?  70   GLY D O   1 
ATOM   13265 N  N   . PHE D 4  71   ? -33.261 -24.353  66.417  1.00 56.87  ?  71   PHE D N   1 
ATOM   13266 C  CA  . PHE D 4  71   ? -31.878 -24.526  65.984  1.00 62.48  ?  71   PHE D CA  1 
ATOM   13267 C  C   . PHE D 4  71   ? -31.339 -25.888  66.398  1.00 69.52  ?  71   PHE D C   1 
ATOM   13268 O  O   . PHE D 4  71   ? -30.648 -26.553  65.616  1.00 68.43  ?  71   PHE D O   1 
ATOM   13269 C  CB  . PHE D 4  71   ? -31.001 -23.412  66.553  1.00 59.81  ?  71   PHE D CB  1 
ATOM   13270 C  CG  . PHE D 4  71   ? -29.738 -23.175  65.771  1.00 58.29  ?  71   PHE D CG  1 
ATOM   13271 C  CD1 . PHE D 4  71   ? -29.718 -22.284  64.710  1.00 58.98  ?  71   PHE D CD1 1 
ATOM   13272 C  CD2 . PHE D 4  71   ? -28.572 -23.850  66.095  1.00 61.32  ?  71   PHE D CD2 1 
ATOM   13273 C  CE1 . PHE D 4  71   ? -28.554 -22.065  63.990  1.00 60.89  ?  71   PHE D CE1 1 
ATOM   13274 C  CE2 . PHE D 4  71   ? -27.407 -23.637  65.378  1.00 60.35  ?  71   PHE D CE2 1 
ATOM   13275 C  CZ  . PHE D 4  71   ? -27.398 -22.744  64.325  1.00 52.96  ?  71   PHE D CZ  1 
ATOM   13276 N  N   . ILE D 4  72   ? -31.647 -26.322  67.624  1.00 71.61  ?  72   ILE D N   1 
ATOM   13277 C  CA  . ILE D 4  72   ? -31.181 -27.624  68.095  1.00 67.59  ?  72   ILE D CA  1 
ATOM   13278 C  C   . ILE D 4  72   ? -31.784 -28.745  67.259  1.00 70.48  ?  72   ILE D C   1 
ATOM   13279 O  O   . ILE D 4  72   ? -31.095 -29.705  66.893  1.00 76.32  ?  72   ILE D O   1 
ATOM   13280 C  CB  . ILE D 4  72   ? -31.501 -27.800  69.592  1.00 65.55  ?  72   ILE D CB  1 
ATOM   13281 C  CG1 . ILE D 4  72   ? -30.684 -26.820  70.435  1.00 63.74  ?  72   ILE D CG1 1 
ATOM   13282 C  CG2 . ILE D 4  72   ? -31.243 -29.227  70.032  1.00 57.47  ?  72   ILE D CG2 1 
ATOM   13283 C  CD1 . ILE D 4  72   ? -29.209 -26.812  70.112  1.00 63.96  ?  72   ILE D CD1 1 
ATOM   13284 N  N   . LEU D 4  73   ? -33.076 -28.641  66.939  1.00 64.24  ?  73   LEU D N   1 
ATOM   13285 C  CA  . LEU D 4  73   ? -33.738 -29.681  66.157  1.00 63.73  ?  73   LEU D CA  1 
ATOM   13286 C  C   . LEU D 4  73   ? -33.093 -29.837  64.785  1.00 58.47  ?  73   LEU D C   1 
ATOM   13287 O  O   . LEU D 4  73   ? -32.833 -30.958  64.332  1.00 66.17  ?  73   LEU D O   1 
ATOM   13288 C  CB  . LEU D 4  73   ? -35.226 -29.359  66.018  1.00 63.16  ?  73   LEU D CB  1 
ATOM   13289 C  CG  . LEU D 4  73   ? -36.074 -30.412  65.304  1.00 66.97  ?  73   LEU D CG  1 
ATOM   13290 C  CD1 . LEU D 4  73   ? -36.427 -31.548  66.249  1.00 70.19  ?  73   LEU D CD1 1 
ATOM   13291 C  CD2 . LEU D 4  73   ? -37.328 -29.787  64.708  1.00 73.92  ?  73   LEU D CD2 1 
ATOM   13292 N  N   . GLN D 4  74   ? -32.825 -28.717  64.109  1.00 67.29  ?  74   GLN D N   1 
ATOM   13293 C  CA  . GLN D 4  74   ? -32.228 -28.775  62.779  1.00 63.27  ?  74   GLN D CA  1 
ATOM   13294 C  C   . GLN D 4  74   ? -30.815 -29.342  62.835  1.00 68.01  ?  74   GLN D C   1 
ATOM   13295 O  O   . GLN D 4  74   ? -30.445 -30.200  62.025  1.00 69.29  ?  74   GLN D O   1 
ATOM   13296 C  CB  . GLN D 4  74   ? -32.221 -27.381  62.149  1.00 67.08  ?  74   GLN D CB  1 
ATOM   13297 C  CG  . GLN D 4  74   ? -33.597 -26.842  61.807  1.00 69.85  ?  74   GLN D CG  1 
ATOM   13298 C  CD  . GLN D 4  74   ? -33.540 -25.463  61.181  1.00 68.39  ?  74   GLN D CD  1 
ATOM   13299 O  OE1 . GLN D 4  74   ? -33.593 -25.319  59.960  1.00 60.94  ?  74   GLN D OE1 1 
ATOM   13300 N  NE2 . GLN D 4  74   ? -33.423 -24.439  62.018  1.00 76.58  ?  74   GLN D NE2 1 
ATOM   13301 N  N   . TYR D 4  75   ? -30.012 -28.872  63.793  1.00 65.36  ?  75   TYR D N   1 
ATOM   13302 C  CA  . TYR D 4  75   ? -28.617 -29.295  63.876  1.00 62.94  ?  75   TYR D CA  1 
ATOM   13303 C  C   . TYR D 4  75   ? -28.512 -30.781  64.192  1.00 65.00  ?  75   TYR D C   1 
ATOM   13304 O  O   . TYR D 4  75   ? -27.721 -31.505  63.577  1.00 66.39  ?  75   TYR D O   1 
ATOM   13305 C  CB  . TYR D 4  75   ? -27.882 -28.462  64.928  1.00 54.21  ?  75   TYR D CB  1 
ATOM   13306 C  CG  . TYR D 4  75   ? -26.376 -28.455  64.780  1.00 57.26  ?  75   TYR D CG  1 
ATOM   13307 C  CD1 . TYR D 4  75   ? -25.608 -29.534  65.199  1.00 60.07  ?  75   TYR D CD1 1 
ATOM   13308 C  CD2 . TYR D 4  75   ? -25.722 -27.363  64.227  1.00 62.39  ?  75   TYR D CD2 1 
ATOM   13309 C  CE1 . TYR D 4  75   ? -24.229 -29.527  65.067  1.00 66.98  ?  75   TYR D CE1 1 
ATOM   13310 C  CE2 . TYR D 4  75   ? -24.345 -27.347  64.091  1.00 69.69  ?  75   TYR D CE2 1 
ATOM   13311 C  CZ  . TYR D 4  75   ? -23.603 -28.430  64.512  1.00 72.84  ?  75   TYR D CZ  1 
ATOM   13312 O  OH  . TYR D 4  75   ? -22.232 -28.413  64.377  1.00 73.28  ?  75   TYR D OH  1 
ATOM   13313 N  N   . ILE D 4  76   ? -29.311 -31.258  65.147  1.00 71.23  ?  76   ILE D N   1 
ATOM   13314 C  CA  . ILE D 4  76   ? -29.266 -32.671  65.508  1.00 72.31  ?  76   ILE D CA  1 
ATOM   13315 C  C   . ILE D 4  76   ? -29.823 -33.533  64.382  1.00 78.60  ?  76   ILE D C   1 
ATOM   13316 O  O   . ILE D 4  76   ? -29.283 -34.602  64.076  1.00 79.82  ?  76   ILE D O   1 
ATOM   13317 C  CB  . ILE D 4  76   ? -30.021 -32.913  66.829  1.00 72.02  ?  76   ILE D CB  1 
ATOM   13318 C  CG1 . ILE D 4  76   ? -29.372 -32.133  67.973  1.00 73.88  ?  76   ILE D CG1 1 
ATOM   13319 C  CG2 . ILE D 4  76   ? -30.072 -34.394  67.158  1.00 63.04  ?  76   ILE D CG2 1 
ATOM   13320 C  CD1 . ILE D 4  76   ? -27.898 -32.424  68.161  1.00 72.82  ?  76   ILE D CD1 1 
ATOM   13321 N  N   . GLY D 4  77   ? -30.901 -33.079  63.742  1.00 85.74  ?  77   GLY D N   1 
ATOM   13322 C  CA  . GLY D 4  77   ? -31.583 -33.926  62.776  1.00 84.31  ?  77   GLY D CA  1 
ATOM   13323 C  C   . GLY D 4  77   ? -30.788 -34.135  61.501  1.00 84.66  ?  77   GLY D C   1 
ATOM   13324 O  O   . GLY D 4  77   ? -30.669 -35.260  61.008  1.00 84.69  ?  77   GLY D O   1 
ATOM   13325 N  N   . ASN D 4  78   ? -30.235 -33.054  60.947  1.00 60.08  ?  78   ASN D N   1 
ATOM   13326 C  CA  . ASN D 4  78   ? -29.568 -33.113  59.656  1.00 59.26  ?  78   ASN D CA  1 
ATOM   13327 C  C   . ASN D 4  78   ? -28.050 -33.058  59.732  1.00 63.84  ?  78   ASN D C   1 
ATOM   13328 O  O   . ASN D 4  78   ? -27.392 -33.418  58.751  1.00 69.60  ?  78   ASN D O   1 
ATOM   13329 C  CB  . ASN D 4  78   ? -30.063 -31.972  58.757  1.00 63.08  ?  78   ASN D CB  1 
ATOM   13330 C  CG  . ASN D 4  78   ? -31.507 -32.145  58.351  1.00 65.18  ?  78   ASN D CG  1 
ATOM   13331 O  OD1 . ASN D 4  78   ? -32.331 -31.254  58.549  1.00 64.11  ?  78   ASN D OD1 1 
ATOM   13332 N  ND2 . ASN D 4  78   ? -31.826 -33.303  57.786  1.00 70.99  ?  78   ASN D ND2 1 
ATOM   13333 N  N   . LEU D 4  79   ? -27.476 -32.631  60.857  1.00 60.02  ?  79   LEU D N   1 
ATOM   13334 C  CA  . LEU D 4  79   ? -26.029 -32.541  60.987  1.00 62.51  ?  79   LEU D CA  1 
ATOM   13335 C  C   . LEU D 4  79   ? -25.456 -33.474  62.045  1.00 59.77  ?  79   LEU D C   1 
ATOM   13336 O  O   . LEU D 4  79   ? -24.242 -33.441  62.282  1.00 63.89  ?  79   LEU D O   1 
ATOM   13337 C  CB  . LEU D 4  79   ? -25.610 -31.095  61.298  1.00 66.22  ?  79   LEU D CB  1 
ATOM   13338 C  CG  . LEU D 4  79   ? -26.298 -30.005  60.473  1.00 63.41  ?  79   LEU D CG  1 
ATOM   13339 C  CD1 . LEU D 4  79   ? -25.814 -28.626  60.889  1.00 58.35  ?  79   LEU D CD1 1 
ATOM   13340 C  CD2 . LEU D 4  79   ? -26.075 -30.227  58.985  1.00 61.22  ?  79   LEU D CD2 1 
ATOM   13341 N  N   . VAL D 4  80   ? -26.282 -34.302  62.686  1.00 64.69  ?  80   VAL D N   1 
ATOM   13342 C  CA  . VAL D 4  80   ? -25.804 -35.220  63.716  1.00 60.65  ?  80   VAL D CA  1 
ATOM   13343 C  C   . VAL D 4  80   ? -26.428 -36.599  63.530  1.00 60.52  ?  80   VAL D C   1 
ATOM   13344 O  O   . VAL D 4  80   ? -25.728 -37.566  63.207  1.00 67.01  ?  80   VAL D O   1 
ATOM   13345 C  CB  . VAL D 4  80   ? -26.095 -34.683  65.131  1.00 59.22  ?  80   VAL D CB  1 
ATOM   13346 C  CG1 . VAL D 4  80   ? -25.742 -35.728  66.181  1.00 54.92  ?  80   VAL D CG1 1 
ATOM   13347 C  CG2 . VAL D 4  80   ? -25.319 -33.403  65.390  1.00 66.25  ?  80   VAL D CG2 1 
ATOM   13348 N  N   . ASP D 4  81   ? -27.748 -36.698  63.737  1.00 63.14  ?  81   ASP D N   1 
ATOM   13349 C  CA  . ASP D 4  81   ? -28.407 -38.004  63.758  1.00 74.35  ?  81   ASP D CA  1 
ATOM   13350 C  C   . ASP D 4  81   ? -28.265 -38.719  62.420  1.00 71.93  ?  81   ASP D C   1 
ATOM   13351 O  O   . ASP D 4  81   ? -27.880 -39.892  62.369  1.00 73.71  ?  81   ASP D O   1 
ATOM   13352 C  CB  . ASP D 4  81   ? -29.883 -37.848  64.127  1.00 75.06  ?  81   ASP D CB  1 
ATOM   13353 C  CG  . ASP D 4  81   ? -30.532 -39.169  64.498  1.00 83.94  ?  81   ASP D CG  1 
ATOM   13354 O  OD1 . ASP D 4  81   ? -29.806 -40.088  64.939  1.00 89.32  ?  81   ASP D OD1 1 
ATOM   13355 O  OD2 . ASP D 4  81   ? -31.764 -39.289  64.351  1.00 82.29  -1 81   ASP D OD2 1 
ATOM   13356 N  N   . TYR D 4  82   ? -28.571 -38.031  61.324  1.00 76.24  ?  82   TYR D N   1 
ATOM   13357 C  CA  . TYR D 4  82   ? -28.448 -38.603  59.985  1.00 66.67  ?  82   TYR D CA  1 
ATOM   13358 C  C   . TYR D 4  82   ? -27.755 -37.577  59.097  1.00 67.18  ?  82   TYR D C   1 
ATOM   13359 O  O   . TYR D 4  82   ? -28.417 -36.683  58.540  1.00 65.23  ?  82   TYR D O   1 
ATOM   13360 C  CB  . TYR D 4  82   ? -29.811 -38.998  59.425  1.00 71.91  ?  82   TYR D CB  1 
ATOM   13361 C  CG  . TYR D 4  82   ? -29.774 -40.231  58.550  1.00 64.38  ?  82   TYR D CG  1 
ATOM   13362 C  CD1 . TYR D 4  82   ? -29.745 -41.505  59.107  1.00 68.46  ?  82   TYR D CD1 1 
ATOM   13363 C  CD2 . TYR D 4  82   ? -29.765 -40.118  57.168  1.00 68.04  ?  82   TYR D CD2 1 
ATOM   13364 C  CE1 . TYR D 4  82   ? -29.707 -42.633  58.304  1.00 69.54  ?  82   TYR D CE1 1 
ATOM   13365 C  CE2 . TYR D 4  82   ? -29.725 -41.233  56.358  1.00 72.62  ?  82   TYR D CE2 1 
ATOM   13366 C  CZ  . TYR D 4  82   ? -29.698 -42.489  56.927  1.00 67.22  ?  82   TYR D CZ  1 
ATOM   13367 O  OH  . TYR D 4  82   ? -29.660 -43.599  56.109  1.00 63.62  ?  82   TYR D OH  1 
ATOM   13368 N  N   . PRO D 4  83   ? -26.426 -37.654  58.959  1.00 54.82  ?  83   PRO D N   1 
ATOM   13369 C  CA  . PRO D 4  83   ? -25.651 -36.624  58.232  1.00 58.50  ?  83   PRO D CA  1 
ATOM   13370 C  C   . PRO D 4  83   ? -25.732 -36.786  56.719  1.00 60.16  ?  83   PRO D C   1 
ATOM   13371 O  O   . PRO D 4  83   ? -24.776 -37.168  56.035  1.00 60.92  ?  83   PRO D O   1 
ATOM   13372 C  CB  . PRO D 4  83   ? -24.230 -36.840  58.775  1.00 65.33  ?  83   PRO D CB  1 
ATOM   13373 C  CG  . PRO D 4  83   ? -24.372 -37.807  59.947  1.00 58.06  ?  83   PRO D CG  1 
ATOM   13374 C  CD  . PRO D 4  83   ? -25.541 -38.644  59.587  1.00 51.43  ?  83   PRO D CD  1 
ATOM   13375 N  N   . LEU D 4  84   ? -26.902 -36.486  56.161  1.00 65.98  ?  84   LEU D N   1 
ATOM   13376 C  CA  . LEU D 4  84   ? -27.073 -36.545  54.715  1.00 69.57  ?  84   LEU D CA  1 
ATOM   13377 C  C   . LEU D 4  84   ? -26.405 -35.358  54.036  1.00 77.85  ?  84   LEU D C   1 
ATOM   13378 O  O   . LEU D 4  84   ? -26.583 -34.207  54.448  1.00 60.96  ?  84   LEU D O   1 
ATOM   13379 C  CB  . LEU D 4  84   ? -28.556 -36.591  54.347  1.00 59.14  ?  84   LEU D CB  1 
ATOM   13380 C  CG  . LEU D 4  84   ? -29.276 -37.894  54.676  1.00 59.32  ?  84   LEU D CG  1 
ATOM   13381 C  CD1 . LEU D 4  84   ? -30.755 -37.813  54.342  1.00 63.90  ?  84   LEU D CD1 1 
ATOM   13382 C  CD2 . LEU D 4  84   ? -28.617 -39.021  53.902  1.00 55.38  ?  84   LEU D CD2 1 
ATOM   13383 N  N   . ASN D 4  85   ? -25.628 -35.646  52.996  1.00 111.28 ?  85   ASN D N   1 
ATOM   13384 C  CA  . ASN D 4  85   ? -25.079 -34.615  52.129  1.00 109.06 ?  85   ASN D CA  1 
ATOM   13385 C  C   . ASN D 4  85   ? -26.095 -34.296  51.041  1.00 101.18 ?  85   ASN D C   1 
ATOM   13386 O  O   . ASN D 4  85   ? -26.411 -35.155  50.209  1.00 102.18 ?  85   ASN D O   1 
ATOM   13387 C  CB  . ASN D 4  85   ? -23.755 -35.064  51.517  1.00 111.93 ?  85   ASN D CB  1 
ATOM   13388 C  CG  . ASN D 4  85   ? -23.179 -34.033  50.575  1.00 112.89 ?  85   ASN D CG  1 
ATOM   13389 O  OD1 . ASN D 4  85   ? -23.230 -32.832  50.847  1.00 106.17 ?  85   ASN D OD1 1 
ATOM   13390 N  ND2 . ASN D 4  85   ? -22.639 -34.491  49.452  1.00 105.57 ?  85   ASN D ND2 1 
ATOM   13391 N  N   . VAL D 4  86   ? -26.617 -33.071  51.059  1.00 49.42  ?  86   VAL D N   1 
ATOM   13392 C  CA  . VAL D 4  86   ? -27.607 -32.617  50.088  1.00 48.46  ?  86   VAL D CA  1 
ATOM   13393 C  C   . VAL D 4  86   ? -27.030 -31.424  49.328  1.00 48.64  ?  86   VAL D C   1 
ATOM   13394 O  O   . VAL D 4  86   ? -26.788 -30.356  49.906  1.00 59.56  ?  86   VAL D O   1 
ATOM   13395 C  CB  . VAL D 4  86   ? -28.953 -32.281  50.750  1.00 46.53  ?  86   VAL D CB  1 
ATOM   13396 C  CG1 . VAL D 4  86   ? -29.612 -33.558  51.243  1.00 48.86  ?  86   VAL D CG1 1 
ATOM   13397 C  CG2 . VAL D 4  86   ? -28.766 -31.338  51.923  1.00 54.68  ?  86   VAL D CG2 1 
ATOM   13398 N  N   . GLY D 4  87   ? -26.796 -31.617  48.030  1.00 37.77  ?  87   GLY D N   1 
ATOM   13399 C  CA  . GLY D 4  87   ? -26.288 -30.572  47.161  1.00 36.23  ?  87   GLY D CA  1 
ATOM   13400 C  C   . GLY D 4  87   ? -24.940 -30.007  47.538  1.00 39.68  ?  87   GLY D C   1 
ATOM   13401 O  O   . GLY D 4  87   ? -24.634 -28.870  47.170  1.00 47.45  ?  87   GLY D O   1 
ATOM   13402 N  N   . GLY D 4  88   ? -24.117 -30.764  48.259  1.00 41.57  ?  88   GLY D N   1 
ATOM   13403 C  CA  . GLY D 4  88   ? -22.851 -30.231  48.717  1.00 47.67  ?  88   GLY D CA  1 
ATOM   13404 C  C   . GLY D 4  88   ? -22.958 -29.165  49.783  1.00 51.00  ?  88   GLY D C   1 
ATOM   13405 O  O   . GLY D 4  88   ? -21.948 -28.535  50.113  1.00 45.18  ?  88   GLY D O   1 
ATOM   13406 N  N   . ARG D 4  89   ? -24.156 -28.931  50.317  1.00 60.42  ?  89   ARG D N   1 
ATOM   13407 C  CA  . ARG D 4  89   ? -24.319 -27.958  51.380  1.00 62.95  ?  89   ARG D CA  1 
ATOM   13408 C  C   . ARG D 4  89   ? -23.567 -28.428  52.623  1.00 72.82  ?  89   ARG D C   1 
ATOM   13409 O  O   . ARG D 4  89   ? -23.465 -29.632  52.875  1.00 68.22  ?  89   ARG D O   1 
ATOM   13410 C  CB  . ARG D 4  89   ? -25.795 -27.761  51.711  1.00 66.89  ?  89   ARG D CB  1 
ATOM   13411 C  CG  . ARG D 4  89   ? -26.627 -27.233  50.564  1.00 62.40  ?  89   ARG D CG  1 
ATOM   13412 C  CD  . ARG D 4  89   ? -26.203 -25.846  50.104  1.00 66.19  ?  89   ARG D CD  1 
ATOM   13413 N  NE  . ARG D 4  89   ? -26.938 -25.448  48.908  1.00 65.19  ?  89   ARG D NE  1 
ATOM   13414 C  CZ  . ARG D 4  89   ? -26.564 -25.737  47.669  1.00 61.16  ?  89   ARG D CZ  1 
ATOM   13415 N  NH1 . ARG D 4  89   ? -25.469 -26.435  47.423  1.00 58.27  ?  89   ARG D NH1 1 
ATOM   13416 N  NH2 . ARG D 4  89   ? -27.307 -25.310  46.651  1.00 69.30  ?  89   ARG D NH2 1 
ATOM   13417 N  N   . PRO D 4  90   ? -23.019 -27.503  53.404  1.00 78.68  ?  90   PRO D N   1 
ATOM   13418 C  CA  . PRO D 4  90   ? -22.163 -27.905  54.524  1.00 76.85  ?  90   PRO D CA  1 
ATOM   13419 C  C   . PRO D 4  90   ? -22.931 -28.656  55.601  1.00 77.40  ?  90   PRO D C   1 
ATOM   13420 O  O   . PRO D 4  90   ? -24.126 -28.440  55.818  1.00 76.79  ?  90   PRO D O   1 
ATOM   13421 C  CB  . PRO D 4  90   ? -21.630 -26.572  55.058  1.00 80.66  ?  90   PRO D CB  1 
ATOM   13422 C  CG  . PRO D 4  90   ? -22.615 -25.551  54.590  1.00 79.47  ?  90   PRO D CG  1 
ATOM   13423 C  CD  . PRO D 4  90   ? -23.087 -26.038  53.259  1.00 68.51  ?  90   PRO D CD  1 
ATOM   13424 N  N   . LEU D 4  91   ? -22.216 -29.549  56.284  1.00 77.51  ?  91   LEU D N   1 
ATOM   13425 C  CA  . LEU D 4  91   ? -22.744 -30.280  57.427  1.00 77.51  ?  91   LEU D CA  1 
ATOM   13426 C  C   . LEU D 4  91   ? -22.240 -29.720  58.751  1.00 82.49  ?  91   LEU D C   1 
ATOM   13427 O  O   . LEU D 4  91   ? -22.450 -30.341  59.798  1.00 79.47  ?  91   LEU D O   1 
ATOM   13428 C  CB  . LEU D 4  91   ? -22.390 -31.766  57.314  1.00 72.67  ?  91   LEU D CB  1 
ATOM   13429 C  CG  . LEU D 4  91   ? -23.192 -32.578  56.295  1.00 78.01  ?  91   LEU D CG  1 
ATOM   13430 C  CD1 . LEU D 4  91   ? -22.408 -33.798  55.835  1.00 73.46  ?  91   LEU D CD1 1 
ATOM   13431 C  CD2 . LEU D 4  91   ? -24.535 -32.992  56.881  1.00 82.32  ?  91   LEU D CD2 1 
ATOM   13432 N  N   . ASP D 4  92   ? -21.583 -28.565  58.727  1.00 81.62  ?  92   ASP D N   1 
ATOM   13433 C  CA  . ASP D 4  92   ? -21.007 -27.942  59.905  1.00 76.06  ?  92   ASP D CA  1 
ATOM   13434 C  C   . ASP D 4  92   ? -21.921 -26.817  60.395  1.00 77.02  ?  92   ASP D C   1 
ATOM   13435 O  O   . ASP D 4  92   ? -23.097 -26.744  60.020  1.00 78.94  ?  92   ASP D O   1 
ATOM   13436 C  CB  . ASP D 4  92   ? -19.600 -27.425  59.577  1.00 77.88  ?  92   ASP D CB  1 
ATOM   13437 C  CG  . ASP D 4  92   ? -18.792 -28.402  58.752  1.00 93.18  ?  92   ASP D CG  1 
ATOM   13438 O  OD1 . ASP D 4  92   ? -18.875 -29.619  59.014  1.00 99.38  ?  92   ASP D OD1 1 
ATOM   13439 O  OD2 . ASP D 4  92   ? -18.073 -27.950  57.837  1.00 95.57  -1 92   ASP D OD2 1 
ATOM   13440 N  N   . ILE D 4  93   ? -21.381 -25.927  61.232  1.00 48.51  ?  93   ILE D N   1 
ATOM   13441 C  CA  . ILE D 4  93   ? -22.092 -24.702  61.565  1.00 41.95  ?  93   ILE D CA  1 
ATOM   13442 C  C   . ILE D 4  93   ? -22.125 -23.760  60.369  1.00 39.33  ?  93   ILE D C   1 
ATOM   13443 O  O   . ILE D 4  93   ? -22.950 -22.838  60.327  1.00 33.92  ?  93   ILE D O   1 
ATOM   13444 C  CB  . ILE D 4  93   ? -21.453 -24.030  62.797  1.00 39.37  ?  93   ILE D CB  1 
ATOM   13445 C  CG1 . ILE D 4  93   ? -22.406 -23.004  63.423  1.00 37.87  ?  93   ILE D CG1 1 
ATOM   13446 C  CG2 . ILE D 4  93   ? -20.131 -23.379  62.428  1.00 38.65  ?  93   ILE D CG2 1 
ATOM   13447 C  CD1 . ILE D 4  93   ? -23.729 -23.586  63.886  1.00 34.48  ?  93   ILE D CD1 1 
ATOM   13448 N  N   . THR D 4  94   ? -21.253 -23.978  59.379  1.00 65.21  ?  94   THR D N   1 
ATOM   13449 C  CA  . THR D 4  94   ? -21.305 -23.204  58.144  1.00 67.80  ?  94   THR D CA  1 
ATOM   13450 C  C   . THR D 4  94   ? -22.619 -23.382  57.398  1.00 69.32  ?  94   THR D C   1 
ATOM   13451 O  O   . THR D 4  94   ? -22.883 -22.627  56.458  1.00 76.52  ?  94   THR D O   1 
ATOM   13452 C  CB  . THR D 4  94   ? -20.128 -23.574  57.247  1.00 70.12  ?  94   THR D CB  1 
ATOM   13453 O  OG1 . THR D 4  94   ? -20.061 -24.998  57.110  1.00 81.34  ?  94   THR D OG1 1 
ATOM   13454 C  CG2 . THR D 4  94   ? -18.829 -23.063  57.853  1.00 67.22  ?  94   THR D CG2 1 
ATOM   13455 N  N   . ASN D 4  95   ? -23.449 -24.346  57.798  1.00 52.51  ?  95   ASN D N   1 
ATOM   13456 C  CA  . ASN D 4  95   ? -24.843 -24.404  57.379  1.00 50.28  ?  95   ASN D CA  1 
ATOM   13457 C  C   . ASN D 4  95   ? -25.734 -23.470  58.195  1.00 55.20  ?  95   ASN D C   1 
ATOM   13458 O  O   . ASN D 4  95   ? -26.937 -23.726  58.318  1.00 57.76  ?  95   ASN D O   1 
ATOM   13459 C  CB  . ASN D 4  95   ? -25.357 -25.843  57.472  1.00 52.59  ?  95   ASN D CB  1 
ATOM   13460 C  CG  . ASN D 4  95   ? -26.590 -26.084  56.617  1.00 63.86  ?  95   ASN D CG  1 
ATOM   13461 O  OD1 . ASN D 4  95   ? -26.803 -25.413  55.606  1.00 67.66  ?  95   ASN D OD1 1 
ATOM   13462 N  ND2 . ASN D 4  95   ? -27.417 -27.039  57.029  1.00 65.45  ?  95   ASN D ND2 1 
ATOM   13463 N  N   . TRP D 4  96   ? -25.171 -22.405  58.769  1.00 65.07  ?  96   TRP D N   1 
ATOM   13464 C  CA  . TRP D 4  96   ? -25.993 -21.451  59.509  1.00 65.23  ?  96   TRP D CA  1 
ATOM   13465 C  C   . TRP D 4  96   ? -27.003 -20.718  58.628  1.00 61.38  ?  96   TRP D C   1 
ATOM   13466 O  O   . TRP D 4  96   ? -28.090 -20.393  59.136  1.00 58.47  ?  96   TRP D O   1 
ATOM   13467 C  CB  . TRP D 4  96   ? -25.094 -20.477  60.296  1.00 57.09  ?  96   TRP D CB  1 
ATOM   13468 C  CG  . TRP D 4  96   ? -24.591 -19.275  59.544  1.00 59.97  ?  96   TRP D CG  1 
ATOM   13469 C  CD1 . TRP D 4  96   ? -23.348 -19.111  59.001  1.00 61.79  ?  96   TRP D CD1 1 
ATOM   13470 C  CD2 . TRP D 4  96   ? -25.310 -18.066  59.267  1.00 66.36  ?  96   TRP D CD2 1 
ATOM   13471 N  NE1 . TRP D 4  96   ? -23.255 -17.882  58.393  1.00 69.93  ?  96   TRP D NE1 1 
ATOM   13472 C  CE2 . TRP D 4  96   ? -24.446 -17.221  58.543  1.00 74.02  ?  96   TRP D CE2 1 
ATOM   13473 C  CE3 . TRP D 4  96   ? -26.604 -17.620  59.555  1.00 66.16  ?  96   TRP D CE3 1 
ATOM   13474 C  CZ2 . TRP D 4  96   ? -24.833 -15.955  58.107  1.00 73.86  ?  96   TRP D CZ2 1 
ATOM   13475 C  CZ3 . TRP D 4  96   ? -26.986 -16.366  59.118  1.00 71.07  ?  96   TRP D CZ3 1 
ATOM   13476 C  CH2 . TRP D 4  96   ? -26.104 -15.548  58.403  1.00 70.77  ?  96   TRP D CH2 1 
ATOM   13477 N  N   . PRO D 4  97   ? -26.740 -20.426  57.350  1.00 59.52  ?  97   PRO D N   1 
ATOM   13478 C  CA  . PRO D 4  97   ? -27.849 -20.071  56.461  1.00 65.26  ?  97   PRO D CA  1 
ATOM   13479 C  C   . PRO D 4  97   ? -28.723 -21.289  56.238  1.00 66.98  ?  97   PRO D C   1 
ATOM   13480 O  O   . PRO D 4  97   ? -28.244 -22.425  56.242  1.00 69.71  ?  97   PRO D O   1 
ATOM   13481 C  CB  . PRO D 4  97   ? -27.155 -19.639  55.164  1.00 67.09  ?  97   PRO D CB  1 
ATOM   13482 C  CG  . PRO D 4  97   ? -25.768 -19.335  55.560  1.00 69.25  ?  97   PRO D CG  1 
ATOM   13483 C  CD  . PRO D 4  97   ? -25.454 -20.307  56.641  1.00 61.24  ?  97   PRO D CD  1 
ATOM   13484 N  N   . ALA D 4  98   ? -30.018 -21.036  56.061  1.00 76.81  ?  98   ALA D N   1 
ATOM   13485 C  CA  . ALA D 4  98   ? -31.079 -22.034  55.918  1.00 83.23  ?  98   ALA D CA  1 
ATOM   13486 C  C   . ALA D 4  98   ? -31.425 -22.678  57.254  1.00 84.23  ?  98   ALA D C   1 
ATOM   13487 O  O   . ALA D 4  98   ? -32.137 -23.685  57.269  1.00 82.83  ?  98   ALA D O   1 
ATOM   13488 C  CB  . ALA D 4  98   ? -30.745 -23.131  54.896  1.00 79.17  ?  98   ALA D CB  1 
ATOM   13489 N  N   . MET D 4  99   ? -30.937 -22.142  58.375  1.00 79.88  ?  99   MET D N   1 
ATOM   13490 C  CA  . MET D 4  99   ? -31.394 -22.544  59.699  1.00 85.24  ?  99   MET D CA  1 
ATOM   13491 C  C   . MET D 4  99   ? -32.089 -21.416  60.447  1.00 79.41  ?  99   MET D C   1 
ATOM   13492 O  O   . MET D 4  99   ? -32.678 -21.663  61.507  1.00 80.74  ?  99   MET D O   1 
ATOM   13493 C  CB  . MET D 4  99   ? -30.222 -23.061  60.546  1.00 78.28  ?  99   MET D CB  1 
ATOM   13494 C  CG  . MET D 4  99   ? -29.586 -24.326  60.006  1.00 66.14  ?  99   MET D CG  1 
ATOM   13495 S  SD  . MET D 4  99   ? -28.166 -24.855  60.980  1.00 68.07  ?  99   MET D SD  1 
ATOM   13496 C  CE  . MET D 4  99   ? -28.973 -25.440  62.469  1.00 82.93  ?  99   MET D CE  1 
ATOM   13497 N  N   . ILE D 4  100  ? -32.032 -20.198  59.921  1.00 53.37  ?  100  ILE D N   1 
ATOM   13498 C  CA  . ILE D 4  100  ? -32.689 -19.030  60.497  1.00 61.89  ?  100  ILE D CA  1 
ATOM   13499 C  C   . ILE D 4  100  ? -34.210 -19.143  60.412  1.00 61.02  ?  100  ILE D C   1 
ATOM   13500 O  O   . ILE D 4  100  ? -34.882 -18.828  61.405  1.00 59.24  ?  100  ILE D O   1 
ATOM   13501 C  CB  . ILE D 4  100  ? -32.196 -17.740  59.818  1.00 51.68  ?  100  ILE D CB  1 
ATOM   13502 C  CG1 . ILE D 4  100  ? -30.678 -17.614  59.950  1.00 56.86  ?  100  ILE D CG1 1 
ATOM   13503 C  CG2 . ILE D 4  100  ? -32.881 -16.519  60.410  1.00 53.30  ?  100  ILE D CG2 1 
ATOM   13504 C  CD1 . ILE D 4  100  ? -30.201 -17.316  61.356  1.00 67.51  ?  100  ILE D CD1 1 
ATOM   13505 N  N   . PRO D 4  101  ? -34.808 -19.555  59.277  1.00 69.95  ?  101  PRO D N   1 
ATOM   13506 C  CA  . PRO D 4  101  ? -36.281 -19.490  59.190  1.00 67.67  ?  101  PRO D CA  1 
ATOM   13507 C  C   . PRO D 4  101  ? -36.981 -20.405  60.180  1.00 67.54  ?  101  PRO D C   1 
ATOM   13508 O  O   . PRO D 4  101  ? -37.841 -19.933  60.934  1.00 68.25  ?  101  PRO D O   1 
ATOM   13509 C  CB  . PRO D 4  101  ? -36.561 -19.867  57.720  1.00 71.40  ?  101  PRO D CB  1 
ATOM   13510 C  CG  . PRO D 4  101  ? -35.295 -19.513  57.002  1.00 70.11  ?  101  PRO D CG  1 
ATOM   13511 C  CD  . PRO D 4  101  ? -34.227 -19.922  57.970  1.00 74.61  ?  101  PRO D CD  1 
ATOM   13512 N  N   . ILE D 4  102  ? -36.610 -21.688  60.234  1.00 76.71  ?  102  ILE D N   1 
ATOM   13513 C  CA  . ILE D 4  102  ? -37.265 -22.619  61.153  1.00 79.92  ?  102  ILE D CA  1 
ATOM   13514 C  C   . ILE D 4  102  ? -37.095 -22.153  62.594  1.00 77.67  ?  102  ILE D C   1 
ATOM   13515 O  O   . ILE D 4  102  ? -38.025 -22.236  63.407  1.00 84.22  ?  102  ILE D O   1 
ATOM   13516 C  CB  . ILE D 4  102  ? -36.712 -24.041  60.953  1.00 77.55  ?  102  ILE D CB  1 
ATOM   13517 C  CG1 . ILE D 4  102  ? -36.837 -24.458  59.486  1.00 82.00  ?  102  ILE D CG1 1 
ATOM   13518 C  CG2 . ILE D 4  102  ? -37.426 -25.029  61.864  1.00 70.09  ?  102  ILE D CG2 1 
ATOM   13519 C  CD1 . ILE D 4  102  ? -38.167 -25.070  59.119  1.00 82.53  ?  102  ILE D CD1 1 
ATOM   13520 N  N   . THR D 4  103  ? -35.905 -21.651  62.929  1.00 53.38  ?  103  THR D N   1 
ATOM   13521 C  CA  . THR D 4  103  ? -35.656 -21.144  64.274  1.00 64.90  ?  103  THR D CA  1 
ATOM   13522 C  C   . THR D 4  103  ? -36.541 -19.943  64.590  1.00 71.81  ?  103  THR D C   1 
ATOM   13523 O  O   . THR D 4  103  ? -37.121 -19.857  65.679  1.00 70.37  ?  103  THR D O   1 
ATOM   13524 C  CB  . THR D 4  103  ? -34.178 -20.777  64.418  1.00 66.99  ?  103  THR D CB  1 
ATOM   13525 O  OG1 . THR D 4  103  ? -33.381 -21.969  64.403  1.00 54.63  ?  103  THR D OG1 1 
ATOM   13526 C  CG2 . THR D 4  103  ? -33.936 -20.019  65.707  1.00 71.21  ?  103  THR D CG2 1 
ATOM   13527 N  N   . PHE D 4  104  ? -36.662 -19.007  63.645  1.00 69.20  ?  104  PHE D N   1 
ATOM   13528 C  CA  . PHE D 4  104  ? -37.475 -17.816  63.876  1.00 65.35  ?  104  PHE D CA  1 
ATOM   13529 C  C   . PHE D 4  104  ? -38.946 -18.176  64.045  1.00 68.44  ?  104  PHE D C   1 
ATOM   13530 O  O   . PHE D 4  104  ? -39.621 -17.667  64.947  1.00 76.63  ?  104  PHE D O   1 
ATOM   13531 C  CB  . PHE D 4  104  ? -37.289 -16.826  62.725  1.00 55.07  ?  104  PHE D CB  1 
ATOM   13532 C  CG  . PHE D 4  104  ? -38.167 -15.608  62.821  1.00 67.45  ?  104  PHE D CG  1 
ATOM   13533 C  CD1 . PHE D 4  104  ? -37.789 -14.524  63.596  1.00 76.29  ?  104  PHE D CD1 1 
ATOM   13534 C  CD2 . PHE D 4  104  ? -39.365 -15.544  62.128  1.00 71.02  ?  104  PHE D CD2 1 
ATOM   13535 C  CE1 . PHE D 4  104  ? -38.594 -13.401  63.683  1.00 82.09  ?  104  PHE D CE1 1 
ATOM   13536 C  CE2 . PHE D 4  104  ? -40.175 -14.425  62.211  1.00 74.09  ?  104  PHE D CE2 1 
ATOM   13537 C  CZ  . PHE D 4  104  ? -39.788 -13.353  62.989  1.00 80.76  ?  104  PHE D CZ  1 
ATOM   13538 N  N   . GLU D 4  105  ? -39.460 -19.057  63.182  1.00 80.58  ?  105  GLU D N   1 
ATOM   13539 C  CA  . GLU D 4  105  ? -40.875 -19.413  63.241  1.00 83.36  ?  105  GLU D CA  1 
ATOM   13540 C  C   . GLU D 4  105  ? -41.210 -20.135  64.538  1.00 89.84  ?  105  GLU D C   1 
ATOM   13541 O  O   . GLU D 4  105  ? -42.290 -19.935  65.107  1.00 91.41  ?  105  GLU D O   1 
ATOM   13542 C  CB  . GLU D 4  105  ? -41.250 -20.275  62.034  1.00 91.51  ?  105  GLU D CB  1 
ATOM   13543 C  CG  . GLU D 4  105  ? -41.046 -19.595  60.687  1.00 94.26  ?  105  GLU D CG  1 
ATOM   13544 C  CD  . GLU D 4  105  ? -41.980 -18.419  60.461  1.00 98.38  ?  105  GLU D CD  1 
ATOM   13545 O  OE1 . GLU D 4  105  ? -42.998 -18.316  61.177  1.00 99.51  ?  105  GLU D OE1 1 
ATOM   13546 O  OE2 . GLU D 4  105  ? -41.690 -17.596  59.566  1.00 96.44  -1 105  GLU D OE2 1 
ATOM   13547 N  N   . SER D 4  106  ? -40.292 -20.975  65.025  1.00 92.65  ?  106  SER D N   1 
ATOM   13548 C  CA  . SER D 4  106  ? -40.536 -21.699  66.270  1.00 96.97  ?  106  SER D CA  1 
ATOM   13549 C  C   . SER D 4  106  ? -40.585 -20.751  67.461  1.00 97.76  ?  106  SER D C   1 
ATOM   13550 O  O   . SER D 4  106  ? -41.434 -20.902  68.348  1.00 96.24  ?  106  SER D O   1 
ATOM   13551 C  CB  . SER D 4  106  ? -39.461 -22.767  66.478  1.00 89.36  ?  106  SER D CB  1 
ATOM   13552 O  OG  . SER D 4  106  ? -39.410 -23.663  65.382  1.00 92.59  ?  106  SER D OG  1 
ATOM   13553 N  N   . GLY D 4  107  ? -39.683 -19.766  67.495  1.00 73.77  ?  107  GLY D N   1 
ATOM   13554 C  CA  . GLY D 4  107  ? -39.685 -18.811  68.591  1.00 72.45  ?  107  GLY D CA  1 
ATOM   13555 C  C   . GLY D 4  107  ? -40.941 -17.961  68.632  1.00 78.46  ?  107  GLY D C   1 
ATOM   13556 O  O   . GLY D 4  107  ? -41.499 -17.714  69.705  1.00 86.33  ?  107  GLY D O   1 
ATOM   13557 N  N   . ILE D 4  108  ? -41.406 -17.506  67.464  1.00 54.27  ?  108  ILE D N   1 
ATOM   13558 C  CA  . ILE D 4  108  ? -42.615 -16.686  67.412  1.00 53.69  ?  108  ILE D CA  1 
ATOM   13559 C  C   . ILE D 4  108  ? -43.821 -17.478  67.895  1.00 57.11  ?  108  ILE D C   1 
ATOM   13560 O  O   . ILE D 4  108  ? -44.685 -16.950  68.606  1.00 63.39  ?  108  ILE D O   1 
ATOM   13561 C  CB  . ILE D 4  108  ? -42.832 -16.136  65.988  1.00 56.11  ?  108  ILE D CB  1 
ATOM   13562 C  CG1 . ILE D 4  108  ? -41.648 -15.269  65.563  1.00 49.93  ?  108  ILE D CG1 1 
ATOM   13563 C  CG2 . ILE D 4  108  ? -44.129 -15.346  65.903  1.00 59.83  ?  108  ILE D CG2 1 
ATOM   13564 C  CD1 . ILE D 4  108  ? -41.472 -14.027  66.401  1.00 52.36  ?  108  ILE D CD1 1 
ATOM   13565 N  N   . LEU D 4  109  ? -43.894 -18.760  67.529  1.00 62.74  ?  109  LEU D N   1 
ATOM   13566 C  CA  . LEU D 4  109  ? -45.031 -19.586  67.924  1.00 69.77  ?  109  LEU D CA  1 
ATOM   13567 C  C   . LEU D 4  109  ? -45.120 -19.721  69.440  1.00 72.37  ?  109  LEU D C   1 
ATOM   13568 O  O   . LEU D 4  109  ? -46.189 -19.523  70.030  1.00 73.45  ?  109  LEU D O   1 
ATOM   13569 C  CB  . LEU D 4  109  ? -44.931 -20.963  67.265  1.00 66.00  ?  109  LEU D CB  1 
ATOM   13570 C  CG  . LEU D 4  109  ? -46.046 -21.942  67.637  1.00 65.07  ?  109  LEU D CG  1 
ATOM   13571 C  CD1 . LEU D 4  109  ? -47.413 -21.351  67.329  1.00 74.36  ?  109  LEU D CD1 1 
ATOM   13572 C  CD2 . LEU D 4  109  ? -45.861 -23.270  66.921  1.00 60.22  ?  109  LEU D CD2 1 
ATOM   13573 N  N   . LEU D 4  110  ? -44.003 -20.058  70.090  1.00 82.04  ?  110  LEU D N   1 
ATOM   13574 C  CA  . LEU D 4  110  ? -44.018 -20.234  71.539  1.00 84.37  ?  110  LEU D CA  1 
ATOM   13575 C  C   . LEU D 4  110  ? -44.289 -18.919  72.259  1.00 86.56  ?  110  LEU D C   1 
ATOM   13576 O  O   . LEU D 4  110  ? -45.029 -18.889  73.250  1.00 92.59  ?  110  LEU D O   1 
ATOM   13577 C  CB  . LEU D 4  110  ? -42.696 -20.839  72.010  1.00 83.01  ?  110  LEU D CB  1 
ATOM   13578 C  CG  . LEU D 4  110  ? -42.582 -22.362  71.917  1.00 81.08  ?  110  LEU D CG  1 
ATOM   13579 C  CD1 . LEU D 4  110  ? -41.439 -22.873  72.780  1.00 83.17  ?  110  LEU D CD1 1 
ATOM   13580 C  CD2 . LEU D 4  110  ? -43.895 -23.035  72.296  1.00 64.86  ?  110  LEU D CD2 1 
ATOM   13581 N  N   . ALA D 4  111  ? -43.697 -17.823  71.778  1.00 69.62  ?  111  ALA D N   1 
ATOM   13582 C  CA  . ALA D 4  111  ? -43.926 -16.524  72.403  1.00 69.35  ?  111  ALA D CA  1 
ATOM   13583 C  C   . ALA D 4  111  ? -45.386 -16.098  72.283  1.00 70.70  ?  111  ALA D C   1 
ATOM   13584 O  O   . ALA D 4  111  ? -45.976 -15.603  73.252  1.00 71.94  ?  111  ALA D O   1 
ATOM   13585 C  CB  . ALA D 4  111  ? -43.006 -15.473  71.784  1.00 63.34  ?  111  ALA D CB  1 
ATOM   13586 N  N   . SER D 4  112  ? -45.989 -16.288  71.105  1.00 83.47  ?  112  SER D N   1 
ATOM   13587 C  CA  . SER D 4  112  ? -47.386 -15.901  70.919  1.00 84.72  ?  112  SER D CA  1 
ATOM   13588 C  C   . SER D 4  112  ? -48.317 -16.754  71.770  1.00 86.11  ?  112  SER D C   1 
ATOM   13589 O  O   . SER D 4  112  ? -49.260 -16.232  72.378  1.00 90.21  ?  112  SER D O   1 
ATOM   13590 C  CB  . SER D 4  112  ? -47.771 -15.999  69.442  1.00 96.66  ?  112  SER D CB  1 
ATOM   13591 O  OG  . SER D 4  112  ? -47.004 -15.109  68.648  1.00 103.66 ?  112  SER D OG  1 
ATOM   13592 N  N   . PHE D 4  113  ? -48.070 -18.065  71.824  1.00 79.74  ?  113  PHE D N   1 
ATOM   13593 C  CA  . PHE D 4  113  ? -48.890 -18.939  72.657  1.00 75.58  ?  113  PHE D CA  1 
ATOM   13594 C  C   . PHE D 4  113  ? -48.813 -18.534  74.120  1.00 76.20  ?  113  PHE D C   1 
ATOM   13595 O  O   . PHE D 4  113  ? -49.820 -18.574  74.837  1.00 82.84  ?  113  PHE D O   1 
ATOM   13596 C  CB  . PHE D 4  113  ? -48.450 -20.393  72.488  1.00 74.42  ?  113  PHE D CB  1 
ATOM   13597 C  CG  . PHE D 4  113  ? -49.141 -21.116  71.367  1.00 72.72  ?  113  PHE D CG  1 
ATOM   13598 C  CD1 . PHE D 4  113  ? -50.052 -20.460  70.556  1.00 77.55  ?  113  PHE D CD1 1 
ATOM   13599 C  CD2 . PHE D 4  113  ? -48.873 -22.452  71.122  1.00 67.21  ?  113  PHE D CD2 1 
ATOM   13600 C  CE1 . PHE D 4  113  ? -50.688 -21.127  69.528  1.00 92.76  ?  113  PHE D CE1 1 
ATOM   13601 C  CE2 . PHE D 4  113  ? -49.503 -23.123  70.093  1.00 76.90  ?  113  PHE D CE2 1 
ATOM   13602 C  CZ  . PHE D 4  113  ? -50.412 -22.458  69.294  1.00 92.78  ?  113  PHE D CZ  1 
ATOM   13603 N  N   . ALA D 4  114  ? -47.624 -18.137  74.579  1.00 60.71  ?  114  ALA D N   1 
ATOM   13604 C  CA  . ALA D 4  114  ? -47.453 -17.759  75.978  1.00 67.64  ?  114  ALA D CA  1 
ATOM   13605 C  C   . ALA D 4  114  ? -48.234 -16.495  76.314  1.00 70.73  ?  114  ALA D C   1 
ATOM   13606 O  O   . ALA D 4  114  ? -48.791 -16.380  77.412  1.00 68.29  ?  114  ALA D O   1 
ATOM   13607 C  CB  . ALA D 4  114  ? -45.969 -17.574  76.295  1.00 63.68  ?  114  ALA D CB  1 
ATOM   13608 N  N   . ALA D 4  115  ? -48.289 -15.538  75.385  1.00 77.31  ?  115  ALA D N   1 
ATOM   13609 C  CA  . ALA D 4  115  ? -48.994 -14.287  75.649  1.00 69.73  ?  115  ALA D CA  1 
ATOM   13610 C  C   . ALA D 4  115  ? -50.495 -14.515  75.789  1.00 70.39  ?  115  ALA D C   1 
ATOM   13611 O  O   . ALA D 4  115  ? -51.125 -14.014  76.728  1.00 79.99  ?  115  ALA D O   1 
ATOM   13612 C  CB  . ALA D 4  115  ? -48.704 -13.275  74.540  1.00 64.65  ?  115  ALA D CB  1 
ATOM   13613 N  N   . ALA D 4  116  ? -51.085 -15.270  74.860  1.00 91.60  ?  116  ALA D N   1 
ATOM   13614 C  CA  . ALA D 4  116  ? -52.523 -15.516  74.910  1.00 93.77  ?  116  ALA D CA  1 
ATOM   13615 C  C   . ALA D 4  116  ? -52.891 -16.389  76.104  1.00 98.65  ?  116  ALA D C   1 
ATOM   13616 O  O   . ALA D 4  116  ? -53.787 -16.045  76.885  1.00 103.01 ?  116  ALA D O   1 
ATOM   13617 C  CB  . ALA D 4  116  ? -52.990 -16.159  73.605  1.00 93.17  ?  116  ALA D CB  1 
ATOM   13618 N  N   . ILE D 4  117  ? -52.212 -17.528  76.259  1.00 68.78  ?  117  ILE D N   1 
ATOM   13619 C  CA  . ILE D 4  117  ? -52.485 -18.408  77.392  1.00 66.43  ?  117  ILE D CA  1 
ATOM   13620 C  C   . ILE D 4  117  ? -52.139 -17.714  78.703  1.00 74.24  ?  117  ILE D C   1 
ATOM   13621 O  O   . ILE D 4  117  ? -52.847 -17.864  79.708  1.00 86.24  ?  117  ILE D O   1 
ATOM   13622 C  CB  . ILE D 4  117  ? -51.721 -19.736  77.233  1.00 68.91  ?  117  ILE D CB  1 
ATOM   13623 C  CG1 . ILE D 4  117  ? -52.184 -20.472  75.976  1.00 64.49  ?  117  ILE D CG1 1 
ATOM   13624 C  CG2 . ILE D 4  117  ? -51.913 -20.620  78.458  1.00 70.06  ?  117  ILE D CG2 1 
ATOM   13625 C  CD1 . ILE D 4  117  ? -51.454 -21.775  75.732  1.00 61.29  ?  117  ILE D CD1 1 
ATOM   13626 N  N   . GLY D 4  118  ? -51.054 -16.935  78.714  1.00 80.09  ?  118  GLY D N   1 
ATOM   13627 C  CA  . GLY D 4  118  ? -50.647 -16.263  79.938  1.00 85.96  ?  118  GLY D CA  1 
ATOM   13628 C  C   . GLY D 4  118  ? -51.660 -15.242  80.417  1.00 93.23  ?  118  GLY D C   1 
ATOM   13629 O  O   . GLY D 4  118  ? -51.963 -15.168  81.609  1.00 94.32  ?  118  GLY D O   1 
ATOM   13630 N  N   . MET D 4  119  ? -52.200 -14.442  79.494  1.00 95.32  ?  119  MET D N   1 
ATOM   13631 C  CA  . MET D 4  119  ? -53.229 -13.476  79.867  1.00 89.55  ?  119  MET D CA  1 
ATOM   13632 C  C   . MET D 4  119  ? -54.438 -14.171  80.477  1.00 94.29  ?  119  MET D C   1 
ATOM   13633 O  O   . MET D 4  119  ? -55.028 -13.676  81.444  1.00 102.19 ?  119  MET D O   1 
ATOM   13634 C  CB  . MET D 4  119  ? -53.649 -12.658  78.647  1.00 83.56  ?  119  MET D CB  1 
ATOM   13635 C  CG  . MET D 4  119  ? -54.592 -11.513  78.968  1.00 93.13  ?  119  MET D CG  1 
ATOM   13636 S  SD  . MET D 4  119  ? -56.300 -11.880  78.522  1.00 112.84 ?  119  MET D SD  1 
ATOM   13637 C  CE  . MET D 4  119  ? -56.101 -12.505  76.854  1.00 113.75 ?  119  MET D CE  1 
ATOM   13638 N  N   . ILE D 4  120  ? -54.817 -15.323  79.923  1.00 87.20  ?  120  ILE D N   1 
ATOM   13639 C  CA  . ILE D 4  120  ? -55.956 -16.071  80.444  1.00 90.59  ?  120  ILE D CA  1 
ATOM   13640 C  C   . ILE D 4  120  ? -55.645 -16.620  81.832  1.00 93.20  ?  120  ILE D C   1 
ATOM   13641 O  O   . ILE D 4  120  ? -56.452 -16.501  82.762  1.00 100.51 ?  120  ILE D O   1 
ATOM   13642 C  CB  . ILE D 4  120  ? -56.347 -17.193  79.464  1.00 88.48  ?  120  ILE D CB  1 
ATOM   13643 C  CG1 . ILE D 4  120  ? -56.769 -16.602  78.117  1.00 89.61  ?  120  ILE D CG1 1 
ATOM   13644 C  CG2 . ILE D 4  120  ? -57.451 -18.057  80.039  1.00 91.11  ?  120  ILE D CG2 1 
ATOM   13645 C  CD1 . ILE D 4  120  ? -56.971 -17.636  77.030  1.00 93.20  ?  120  ILE D CD1 1 
ATOM   13646 N  N   . VAL D 4  121  ? -54.466 -17.221  81.997  1.00 77.79  ?  121  VAL D N   1 
ATOM   13647 C  CA  . VAL D 4  121  ? -54.133 -17.874  83.260  1.00 75.68  ?  121  VAL D CA  1 
ATOM   13648 C  C   . VAL D 4  121  ? -53.853 -16.840  84.345  1.00 85.20  ?  121  VAL D C   1 
ATOM   13649 O  O   . VAL D 4  121  ? -54.326 -16.968  85.480  1.00 89.97  ?  121  VAL D O   1 
ATOM   13650 C  CB  . VAL D 4  121  ? -52.943 -18.831  83.070  1.00 72.28  ?  121  VAL D CB  1 
ATOM   13651 C  CG1 . VAL D 4  121  ? -52.483 -19.380  84.411  1.00 72.07  ?  121  VAL D CG1 1 
ATOM   13652 C  CG2 . VAL D 4  121  ? -53.321 -19.964  82.133  1.00 81.23  ?  121  VAL D CG2 1 
ATOM   13653 N  N   . LEU D 4  122  ? -53.075 -15.802  84.015  1.00 89.05  ?  122  LEU D N   1 
ATOM   13654 C  CA  . LEU D 4  122  ? -52.728 -14.789  85.008  1.00 86.78  ?  122  LEU D CA  1 
ATOM   13655 C  C   . LEU D 4  122  ? -53.969 -14.078  85.534  1.00 87.05  ?  122  LEU D C   1 
ATOM   13656 O  O   . LEU D 4  122  ? -54.079 -13.811  86.736  1.00 92.83  ?  122  LEU D O   1 
ATOM   13657 C  CB  . LEU D 4  122  ? -51.750 -13.776  84.411  1.00 78.82  ?  122  LEU D CB  1 
ATOM   13658 C  CG  . LEU D 4  122  ? -50.284 -14.199  84.317  1.00 74.50  ?  122  LEU D CG  1 
ATOM   13659 C  CD1 . LEU D 4  122  ? -49.454 -13.104  83.670  1.00 80.25  ?  122  LEU D CD1 1 
ATOM   13660 C  CD2 . LEU D 4  122  ? -49.741 -14.542  85.693  1.00 70.42  ?  122  LEU D CD2 1 
ATOM   13661 N  N   . ASN D 4  123  ? -54.914 -13.765  84.648  1.00 89.81  ?  123  ASN D N   1 
ATOM   13662 C  CA  . ASN D 4  123  ? -56.160 -13.135  85.067  1.00 94.41  ?  123  ASN D CA  1 
ATOM   13663 C  C   . ASN D 4  123  ? -57.114 -14.100  85.756  1.00 90.34  ?  123  ASN D C   1 
ATOM   13664 O  O   . ASN D 4  123  ? -58.174 -13.659  86.217  1.00 94.67  ?  123  ASN D O   1 
ATOM   13665 C  CB  . ASN D 4  123  ? -56.866 -12.503  83.863  1.00 98.55  ?  123  ASN D CB  1 
ATOM   13666 C  CG  . ASN D 4  123  ? -56.275 -11.163  83.474  1.00 99.86  ?  123  ASN D CG  1 
ATOM   13667 O  OD1 . ASN D 4  123  ? -55.535 -10.552  84.244  1.00 99.20  ?  123  ASN D OD1 1 
ATOM   13668 N  ND2 . ASN D 4  123  ? -56.607 -10.695  82.277  1.00 96.85  ?  123  ASN D ND2 1 
ATOM   13669 N  N   . GLY D 4  124  ? -56.769 -15.380  85.856  1.00 81.92  ?  124  GLY D N   1 
ATOM   13670 C  CA  . GLY D 4  124  ? -57.763 -16.368  86.254  1.00 89.11  ?  124  GLY D CA  1 
ATOM   13671 C  C   . GLY D 4  124  ? -58.977 -16.334  85.357  1.00 91.23  ?  124  GLY D C   1 
ATOM   13672 O  O   . GLY D 4  124  ? -60.112 -16.478  85.829  1.00 95.93  ?  124  GLY D O   1 
ATOM   13673 N  N   . LEU D 4  125  ? -58.758 -16.132  84.058  1.00 184.98 ?  125  LEU D N   1 
ATOM   13674 C  CA  . LEU D 4  125  ? -59.866 -15.838  83.155  1.00 191.21 ?  125  LEU D CA  1 
ATOM   13675 C  C   . LEU D 4  125  ? -60.907 -16.950  83.058  1.00 200.52 ?  125  LEU D C   1 
ATOM   13676 O  O   . LEU D 4  125  ? -62.105 -16.620  83.056  1.00 203.69 ?  125  LEU D O   1 
ATOM   13677 C  CB  . LEU D 4  125  ? -59.322 -15.482  81.766  1.00 192.94 ?  125  LEU D CB  1 
ATOM   13678 C  CG  . LEU D 4  125  ? -60.226 -14.570  80.939  1.00 200.85 ?  125  LEU D CG  1 
ATOM   13679 C  CD1 . LEU D 4  125  ? -60.686 -13.404  81.794  1.00 196.98 ?  125  LEU D CD1 1 
ATOM   13680 C  CD2 . LEU D 4  125  ? -59.497 -14.078  79.705  1.00 197.48 ?  125  LEU D CD2 1 
ATOM   13681 N  N   . PRO D 4  126  ? -60.556 -18.255  82.983  1.00 117.74 ?  126  PRO D N   1 
ATOM   13682 C  CA  . PRO D 4  126  ? -61.615 -19.271  82.873  1.00 119.91 ?  126  PRO D CA  1 
ATOM   13683 C  C   . PRO D 4  126  ? -62.531 -19.288  84.088  1.00 124.30 ?  126  PRO D C   1 
ATOM   13684 O  O   . PRO D 4  126  ? -62.484 -20.214  84.905  1.00 128.66 ?  126  PRO D O   1 
ATOM   13685 C  CB  . PRO D 4  126  ? -60.838 -20.589  82.736  1.00 113.67 ?  126  PRO D CB  1 
ATOM   13686 C  CG  . PRO D 4  126  ? -59.443 -20.195  82.395  1.00 106.62 ?  126  PRO D CG  1 
ATOM   13687 C  CD  . PRO D 4  126  ? -59.225 -18.883  83.054  1.00 100.94 ?  126  PRO D CD  1 
ATOM   13688 N  N   . SER D 4  127  ? -63.372 -18.260  84.213  1.00 100.57 ?  127  SER D N   1 
ATOM   13689 C  CA  . SER D 4  127  ? -64.302 -18.116  85.333  1.00 98.52  ?  127  SER D CA  1 
ATOM   13690 C  C   . SER D 4  127  ? -65.683 -17.799  84.780  1.00 94.69  ?  127  SER D C   1 
ATOM   13691 O  O   . SER D 4  127  ? -66.109 -16.635  84.769  1.00 87.56  ?  127  SER D O   1 
ATOM   13692 C  CB  . SER D 4  127  ? -63.835 -17.031  86.305  1.00 95.12  ?  127  SER D CB  1 
ATOM   13693 O  OG  . SER D 4  127  ? -63.447 -15.854  85.618  1.00 97.90  ?  127  SER D OG  1 
ATOM   13694 N  N   . PRO D 4  128  ? -66.409 -18.814  84.298  1.00 104.00 ?  128  PRO D N   1 
ATOM   13695 C  CA  . PRO D 4  128  ? -67.773 -18.557  83.806  1.00 109.16 ?  128  PRO D CA  1 
ATOM   13696 C  C   . PRO D 4  128  ? -68.681 -17.977  84.870  1.00 114.47 ?  128  PRO D C   1 
ATOM   13697 O  O   . PRO D 4  128  ? -69.531 -17.132  84.565  1.00 114.32 ?  128  PRO D O   1 
ATOM   13698 C  CB  . PRO D 4  128  ? -68.240 -19.946  83.349  1.00 115.45 ?  128  PRO D CB  1 
ATOM   13699 C  CG  . PRO D 4  128  ? -66.970 -20.663  83.007  1.00 110.11 ?  128  PRO D CG  1 
ATOM   13700 C  CD  . PRO D 4  128  ? -65.986 -20.201  84.045  1.00 106.33 ?  128  PRO D CD  1 
ATOM   13701 N  N   . TYR D 4  129  ? -68.510 -18.403  86.116  1.00 149.91 ?  129  TYR D N   1 
ATOM   13702 C  CA  . TYR D 4  129  ? -69.325 -17.962  87.236  1.00 146.90 ?  129  TYR D CA  1 
ATOM   13703 C  C   . TYR D 4  129  ? -68.494 -17.035  88.108  1.00 148.37 ?  129  TYR D C   1 
ATOM   13704 O  O   . TYR D 4  129  ? -67.316 -17.304  88.367  1.00 147.98 ?  129  TYR D O   1 
ATOM   13705 C  CB  . TYR D 4  129  ? -69.821 -19.167  88.049  1.00 150.96 ?  129  TYR D CB  1 
ATOM   13706 C  CG  . TYR D 4  129  ? -70.437 -18.852  89.401  1.00 150.38 ?  129  TYR D CG  1 
ATOM   13707 C  CD1 . TYR D 4  129  ? -69.644 -18.642  90.524  1.00 148.22 ?  129  TYR D CD1 1 
ATOM   13708 C  CD2 . TYR D 4  129  ? -71.814 -18.803  89.559  1.00 148.41 ?  129  TYR D CD2 1 
ATOM   13709 C  CE1 . TYR D 4  129  ? -70.204 -18.366  91.754  1.00 151.87 ?  129  TYR D CE1 1 
ATOM   13710 C  CE2 . TYR D 4  129  ? -72.383 -18.530  90.786  1.00 149.45 ?  129  TYR D CE2 1 
ATOM   13711 C  CZ  . TYR D 4  129  ? -71.574 -18.313  91.878  1.00 153.60 ?  129  TYR D CZ  1 
ATOM   13712 O  OH  . TYR D 4  129  ? -72.144 -18.042  93.100  1.00 160.16 ?  129  TYR D OH  1 
ATOM   13713 N  N   . HIS D 4  130  ? -69.110 -15.941  88.555  1.00 109.60 ?  130  HIS D N   1 
ATOM   13714 C  CA  . HIS D 4  130  ? -68.472 -15.004  89.455  1.00 101.47 ?  130  HIS D CA  1 
ATOM   13715 C  C   . HIS D 4  130  ? -69.591 -14.419  90.298  1.00 103.51 ?  130  HIS D C   1 
ATOM   13716 O  O   . HIS D 4  130  ? -70.696 -14.202  89.779  1.00 106.76 ?  130  HIS D O   1 
ATOM   13717 C  CB  . HIS D 4  130  ? -67.721 -13.883  88.731  1.00 100.55 ?  130  HIS D CB  1 
ATOM   13718 C  CG  . HIS D 4  130  ? -66.618 -13.278  89.541  1.00 96.38  ?  130  HIS D CG  1 
ATOM   13719 N  ND1 . HIS D 4  130  ? -66.698 -12.017  90.092  1.00 95.79  ?  130  HIS D ND1 1 
ATOM   13720 C  CD2 . HIS D 4  130  ? -65.406 -13.767  89.896  1.00 92.42  ?  130  HIS D CD2 1 
ATOM   13721 C  CE1 . HIS D 4  130  ? -65.584 -11.757  90.755  1.00 97.83  ?  130  HIS D CE1 1 
ATOM   13722 N  NE2 . HIS D 4  130  ? -64.783 -12.802  90.650  1.00 89.56  ?  130  HIS D NE2 1 
ATOM   13723 N  N   . PRO D 4  131  ? -69.350 -14.165  91.583  1.00 81.26  ?  131  PRO D N   1 
ATOM   13724 C  CA  . PRO D 4  131  ? -70.386 -13.523  92.406  1.00 86.90  ?  131  PRO D CA  1 
ATOM   13725 C  C   . PRO D 4  131  ? -70.882 -12.223  91.813  1.00 88.64  ?  131  PRO D C   1 
ATOM   13726 O  O   . PRO D 4  131  ? -72.064 -11.891  91.960  1.00 90.78  ?  131  PRO D O   1 
ATOM   13727 C  CB  . PRO D 4  131  ? -69.670 -13.295  93.740  1.00 89.00  ?  131  PRO D CB  1 
ATOM   13728 C  CG  . PRO D 4  131  ? -68.625 -14.372  93.778  1.00 88.40  ?  131  PRO D CG  1 
ATOM   13729 C  CD  . PRO D 4  131  ? -68.147 -14.496  92.363  1.00 80.55  ?  131  PRO D CD  1 
ATOM   13730 N  N   . VAL D 4  132  ? -70.001 -11.491  91.126  1.00 118.57 ?  132  VAL D N   1 
ATOM   13731 C  CA  . VAL D 4  132  ? -70.330 -10.186  90.554  1.00 118.05 ?  132  VAL D CA  1 
ATOM   13732 C  C   . VAL D 4  132  ? -71.569 -10.257  89.669  1.00 120.35 ?  132  VAL D C   1 
ATOM   13733 O  O   . VAL D 4  132  ? -72.419 -9.358   89.694  1.00 122.33 ?  132  VAL D O   1 
ATOM   13734 C  CB  . VAL D 4  132  ? -69.111 -9.640   89.786  1.00 117.42 ?  132  VAL D CB  1 
ATOM   13735 C  CG1 . VAL D 4  132  ? -69.514 -8.520   88.869  1.00 117.70 ?  132  VAL D CG1 1 
ATOM   13736 C  CG2 . VAL D 4  132  ? -68.070 -9.150   90.774  1.00 118.93 ?  132  VAL D CG2 1 
ATOM   13737 N  N   . PHE D 4  133  ? -71.705 -11.331  88.887  1.00 131.73 ?  133  PHE D N   1 
ATOM   13738 C  CA  . PHE D 4  133  ? -72.822 -11.426  87.949  1.00 132.86 ?  133  PHE D CA  1 
ATOM   13739 C  C   . PHE D 4  133  ? -74.180 -11.447  88.644  1.00 133.19 ?  133  PHE D C   1 
ATOM   13740 O  O   . PHE D 4  133  ? -75.192 -11.156  87.998  1.00 133.51 ?  133  PHE D O   1 
ATOM   13741 C  CB  . PHE D 4  133  ? -72.678 -12.672  87.075  1.00 133.85 ?  133  PHE D CB  1 
ATOM   13742 C  CG  . PHE D 4  133  ? -71.471 -12.655  86.180  1.00 130.26 ?  133  PHE D CG  1 
ATOM   13743 C  CD1 . PHE D 4  133  ? -71.315 -11.666  85.222  1.00 128.44 ?  133  PHE D CD1 1 
ATOM   13744 C  CD2 . PHE D 4  133  ? -70.502 -13.640  86.282  1.00 128.22 ?  133  PHE D CD2 1 
ATOM   13745 C  CE1 . PHE D 4  133  ? -70.208 -11.652  84.392  1.00 127.33 ?  133  PHE D CE1 1 
ATOM   13746 C  CE2 . PHE D 4  133  ? -69.393 -13.633  85.453  1.00 127.90 ?  133  PHE D CE2 1 
ATOM   13747 C  CZ  . PHE D 4  133  ? -69.246 -12.637  84.508  1.00 125.80 ?  133  PHE D CZ  1 
ATOM   13748 N  N   . ASN D 4  134  ? -74.228 -11.777  89.939  1.00 137.04 ?  134  ASN D N   1 
ATOM   13749 C  CA  . ASN D 4  134  ? -75.511 -11.872  90.633  1.00 136.60 ?  134  ASN D CA  1 
ATOM   13750 C  C   . ASN D 4  134  ? -76.262 -10.546  90.626  1.00 138.65 ?  134  ASN D C   1 
ATOM   13751 O  O   . ASN D 4  134  ? -77.499 -10.535  90.646  1.00 137.28 ?  134  ASN D O   1 
ATOM   13752 C  CB  . ASN D 4  134  ? -75.301 -12.352  92.070  1.00 130.29 ?  134  ASN D CB  1 
ATOM   13753 C  CG  . ASN D 4  134  ? -75.429 -13.856  92.206  1.00 132.35 ?  134  ASN D CG  1 
ATOM   13754 O  OD1 . ASN D 4  134  ? -76.273 -14.478  91.561  1.00 137.21 ?  134  ASN D OD1 1 
ATOM   13755 N  ND2 . ASN D 4  134  ? -74.581 -14.450  93.037  1.00 140.19 ?  134  ASN D ND2 1 
ATOM   13756 N  N   . VAL D 4  135  ? -75.540 -9.429   90.607  1.00 107.02 ?  135  VAL D N   1 
ATOM   13757 C  CA  . VAL D 4  135  ? -76.188 -8.116   90.520  1.00 105.41 ?  135  VAL D CA  1 
ATOM   13758 C  C   . VAL D 4  135  ? -77.021 -8.057   89.244  1.00 113.25 ?  135  VAL D C   1 
ATOM   13759 O  O   . VAL D 4  135  ? -76.525 -8.436   88.164  1.00 116.55 ?  135  VAL D O   1 
ATOM   13760 C  CB  . VAL D 4  135  ? -75.134 -6.997   90.545  1.00 103.60 ?  135  VAL D CB  1 
ATOM   13761 C  CG1 . VAL D 4  135  ? -75.773 -5.645   90.261  1.00 94.83  ?  135  VAL D CG1 1 
ATOM   13762 C  CG2 . VAL D 4  135  ? -74.412 -6.988   91.882  1.00 107.90 ?  135  VAL D CG2 1 
ATOM   13763 N  N   . PRO D 4  136  ? -78.281 -7.610   89.303  1.00 133.07 ?  136  PRO D N   1 
ATOM   13764 C  CA  . PRO D 4  136  ? -79.153 -7.745   88.123  1.00 132.38 ?  136  PRO D CA  1 
ATOM   13765 C  C   . PRO D 4  136  ? -78.687 -6.950   86.916  1.00 128.27 ?  136  PRO D C   1 
ATOM   13766 O  O   . PRO D 4  136  ? -78.716 -7.473   85.795  1.00 124.86 ?  136  PRO D O   1 
ATOM   13767 C  CB  . PRO D 4  136  ? -80.515 -7.252   88.637  1.00 130.45 ?  136  PRO D CB  1 
ATOM   13768 C  CG  . PRO D 4  136  ? -80.189 -6.403   89.827  1.00 128.85 ?  136  PRO D CG  1 
ATOM   13769 C  CD  . PRO D 4  136  ? -79.006 -7.064   90.462  1.00 132.28 ?  136  PRO D CD  1 
ATOM   13770 N  N   . ARG D 4  137  ? -78.257 -5.705   87.102  1.00 149.83 ?  137  ARG D N   1 
ATOM   13771 C  CA  . ARG D 4  137  ? -77.918 -4.846   85.975  1.00 157.98 ?  137  ARG D CA  1 
ATOM   13772 C  C   . ARG D 4  137  ? -76.499 -5.054   85.465  1.00 159.78 ?  137  ARG D C   1 
ATOM   13773 O  O   . ARG D 4  137  ? -76.059 -4.306   84.586  1.00 162.32 ?  137  ARG D O   1 
ATOM   13774 C  CB  . ARG D 4  137  ? -78.120 -3.374   86.342  1.00 151.52 ?  137  ARG D CB  1 
ATOM   13775 C  CG  . ARG D 4  137  ? -79.579 -2.947   86.378  1.00 144.61 ?  137  ARG D CG  1 
ATOM   13776 C  CD  . ARG D 4  137  ? -79.724 -1.447   86.543  1.00 147.55 ?  137  ARG D CD  1 
ATOM   13777 N  NE  . ARG D 4  137  ? -78.740 -0.727   85.747  1.00 150.44 ?  137  ARG D NE  1 
ATOM   13778 C  CZ  . ARG D 4  137  ? -78.935 -0.334   84.496  1.00 149.00 ?  137  ARG D CZ  1 
ATOM   13779 N  NH1 . ARG D 4  137  ? -80.072 -0.576   83.865  1.00 149.06 ?  137  ARG D NH1 1 
ATOM   13780 N  NH2 . ARG D 4  137  ? -77.964 0.318    83.862  1.00 146.02 ?  137  ARG D NH2 1 
ATOM   13781 N  N   . PHE D 4  138  ? -75.767 -6.041   85.990  1.00 110.33 ?  138  PHE D N   1 
ATOM   13782 C  CA  . PHE D 4  138  ? -74.457 -6.340   85.426  1.00 103.34 ?  138  PHE D CA  1 
ATOM   13783 C  C   . PHE D 4  138  ? -74.557 -6.990   84.054  1.00 107.73 ?  138  PHE D C   1 
ATOM   13784 O  O   . PHE D 4  138  ? -73.550 -7.063   83.345  1.00 108.29 ?  138  PHE D O   1 
ATOM   13785 C  CB  . PHE D 4  138  ? -73.648 -7.235   86.364  1.00 104.40 ?  138  PHE D CB  1 
ATOM   13786 C  CG  . PHE D 4  138  ? -72.161 -7.104   86.183  1.00 105.70 ?  138  PHE D CG  1 
ATOM   13787 C  CD1 . PHE D 4  138  ? -71.478 -6.021   86.708  1.00 98.89  ?  138  PHE D CD1 1 
ATOM   13788 C  CD2 . PHE D 4  138  ? -71.451 -8.059   85.474  1.00 113.18 ?  138  PHE D CD2 1 
ATOM   13789 C  CE1 . PHE D 4  138  ? -70.111 -5.896   86.537  1.00 97.04  ?  138  PHE D CE1 1 
ATOM   13790 C  CE2 . PHE D 4  138  ? -70.084 -7.940   85.299  1.00 105.73 ?  138  PHE D CE2 1 
ATOM   13791 C  CZ  . PHE D 4  138  ? -69.413 -6.857   85.830  1.00 99.00  ?  138  PHE D CZ  1 
ATOM   13792 N  N   . GLN D 4  139  ? -75.742 -7.470   83.665  1.00 151.58 ?  139  GLN D N   1 
ATOM   13793 C  CA  . GLN D 4  139  ? -75.919 -7.937   82.294  1.00 150.29 ?  139  GLN D CA  1 
ATOM   13794 C  C   . GLN D 4  139  ? -75.729 -6.798   81.305  1.00 150.11 ?  139  GLN D C   1 
ATOM   13795 O  O   . GLN D 4  139  ? -75.234 -7.012   80.194  1.00 156.59 ?  139  GLN D O   1 
ATOM   13796 C  CB  . GLN D 4  139  ? -77.301 -8.566   82.114  1.00 152.08 ?  139  GLN D CB  1 
ATOM   13797 C  CG  . GLN D 4  139  ? -78.452 -7.679   82.559  1.00 155.28 ?  139  GLN D CG  1 
ATOM   13798 C  CD  . GLN D 4  139  ? -79.801 -8.333   82.355  1.00 162.72 ?  139  GLN D CD  1 
ATOM   13799 O  OE1 . GLN D 4  139  ? -79.969 -9.170   81.469  1.00 157.85 ?  139  GLN D OE1 1 
ATOM   13800 N  NE2 . GLN D 4  139  ? -80.775 -7.951   83.174  1.00 166.55 ?  139  GLN D NE2 1 
ATOM   13801 N  N   . TYR D 4  140  ? -76.106 -5.583   81.692  1.00 130.16 ?  140  TYR D N   1 
ATOM   13802 C  CA  . TYR D 4  140  ? -75.913 -4.419   80.843  1.00 129.68 ?  140  TYR D CA  1 
ATOM   13803 C  C   . TYR D 4  140  ? -74.513 -3.831   80.954  1.00 130.78 ?  140  TYR D C   1 
ATOM   13804 O  O   . TYR D 4  140  ? -74.243 -2.813   80.313  1.00 133.32 ?  140  TYR D O   1 
ATOM   13805 C  CB  . TYR D 4  140  ? -76.949 -3.344   81.181  1.00 129.10 ?  140  TYR D CB  1 
ATOM   13806 C  CG  . TYR D 4  140  ? -78.360 -3.869   81.310  1.00 132.80 ?  140  TYR D CG  1 
ATOM   13807 C  CD1 . TYR D 4  140  ? -79.063 -4.308   80.197  1.00 124.98 ?  140  TYR D CD1 1 
ATOM   13808 C  CD2 . TYR D 4  140  ? -78.988 -3.925   82.547  1.00 138.96 ?  140  TYR D CD2 1 
ATOM   13809 C  CE1 . TYR D 4  140  ? -80.354 -4.789   80.313  1.00 131.75 ?  140  TYR D CE1 1 
ATOM   13810 C  CE2 . TYR D 4  140  ? -80.277 -4.403   82.673  1.00 142.38 ?  140  TYR D CE2 1 
ATOM   13811 C  CZ  . TYR D 4  140  ? -80.956 -4.834   81.553  1.00 145.19 ?  140  TYR D CZ  1 
ATOM   13812 O  OH  . TYR D 4  140  ? -82.242 -5.312   81.677  1.00 143.62 ?  140  TYR D OH  1 
ATOM   13813 N  N   . ALA D 4  141  ? -73.619 -4.444   81.736  1.00 113.89 ?  141  ALA D N   1 
ATOM   13814 C  CA  . ALA D 4  141  ? -72.284 -3.881   81.918  1.00 114.36 ?  141  ALA D CA  1 
ATOM   13815 C  C   . ALA D 4  141  ? -71.521 -3.795   80.603  1.00 117.94 ?  141  ALA D C   1 
ATOM   13816 O  O   . ALA D 4  141  ? -70.664 -2.918   80.438  1.00 116.19 ?  141  ALA D O   1 
ATOM   13817 C  CB  . ALA D 4  141  ? -71.493 -4.706   82.933  1.00 107.59 ?  141  ALA D CB  1 
ATOM   13818 N  N   . SER D 4  142  ? -71.812 -4.690   79.657  1.00 125.50 ?  142  SER D N   1 
ATOM   13819 C  CA  . SER D 4  142  ? -71.130 -4.629   78.370  1.00 118.16 ?  142  SER D CA  1 
ATOM   13820 C  C   . SER D 4  142  ? -71.676 -3.500   77.502  1.00 123.23 ?  142  SER D C   1 
ATOM   13821 O  O   . SER D 4  142  ? -70.954 -2.975   76.646  1.00 122.92 ?  142  SER D O   1 
ATOM   13822 C  CB  . SER D 4  142  ? -71.246 -5.970   77.648  1.00 118.08 ?  142  SER D CB  1 
ATOM   13823 O  OG  . SER D 4  142  ? -70.416 -6.953   78.244  1.00 114.55 ?  142  SER D OG  1 
ATOM   13824 N  N   . GLN D 4  143  ? -72.937 -3.106   77.708  1.00 121.21 ?  143  GLN D N   1 
ATOM   13825 C  CA  . GLN D 4  143  ? -73.549 -1.992   76.982  1.00 122.60 ?  143  GLN D CA  1 
ATOM   13826 C  C   . GLN D 4  143  ? -73.723 -0.836   77.962  1.00 121.91 ?  143  GLN D C   1 
ATOM   13827 O  O   . GLN D 4  143  ? -74.731 -0.765   78.672  1.00 119.02 ?  143  GLN D O   1 
ATOM   13828 C  CB  . GLN D 4  143  ? -74.897 -2.362   76.355  1.00 125.10 ?  143  GLN D CB  1 
ATOM   13829 C  CG  . GLN D 4  143  ? -74.995 -3.675   75.571  1.00 118.76 ?  143  GLN D CG  1 
ATOM   13830 C  CD  . GLN D 4  143  ? -75.245 -4.890   76.443  1.00 117.89 ?  143  GLN D CD  1 
ATOM   13831 O  OE1 . GLN D 4  143  ? -74.447 -5.210   77.320  1.00 118.56 ?  143  GLN D OE1 1 
ATOM   13832 N  NE2 . GLN D 4  143  ? -76.351 -5.579   76.195  1.00 120.35 ?  143  GLN D NE2 1 
ATOM   13833 N  N   . ASP D 4  144  ? -72.759 0.078    77.976  1.00 162.63 ?  144  ASP D N   1 
ATOM   13834 C  CA  . ASP D 4  144  ? -72.730 1.192    78.942  1.00 161.18 ?  144  ASP D CA  1 
ATOM   13835 C  C   . ASP D 4  144  ? -72.705 0.564    80.340  1.00 166.75 ?  144  ASP D C   1 
ATOM   13836 O  O   . ASP D 4  144  ? -72.012 -0.446   80.539  1.00 169.43 ?  144  ASP D O   1 
ATOM   13837 C  CB  . ASP D 4  144  ? -73.887 2.144    78.686  1.00 164.39 ?  144  ASP D CB  1 
ATOM   13838 C  CG  . ASP D 4  144  ? -73.449 3.432    78.019  1.00 174.69 ?  144  ASP D CG  1 
ATOM   13839 O  OD1 . ASP D 4  144  ? -72.275 3.819    78.193  1.00 174.53 ?  144  ASP D OD1 1 
ATOM   13840 O  OD2 . ASP D 4  144  ? -74.275 4.056    77.320  1.00 179.29 -1 144  ASP D OD2 1 
ATOM   13841 N  N   . ALA D 4  145  ? -73.437 1.127    81.301  1.00 151.43 ?  145  ALA D N   1 
ATOM   13842 C  CA  . ALA D 4  145  ? -73.604 0.562    82.640  1.00 149.98 ?  145  ALA D CA  1 
ATOM   13843 C  C   . ALA D 4  145  ? -72.258 0.199    83.266  1.00 150.37 ?  145  ALA D C   1 
ATOM   13844 O  O   . ALA D 4  145  ? -71.922 -0.969   83.472  1.00 148.78 ?  145  ALA D O   1 
ATOM   13845 C  CB  . ALA D 4  145  ? -74.545 -0.646   82.608  1.00 149.21 ?  145  ALA D CB  1 
ATOM   13846 N  N   . PHE D 4  146  ? -71.479 1.236    83.551  1.00 121.51 ?  146  PHE D N   1 
ATOM   13847 C  CA  . PHE D 4  146  ? -70.207 1.056    84.233  1.00 118.20 ?  146  PHE D CA  1 
ATOM   13848 C  C   . PHE D 4  146  ? -70.441 0.772    85.714  1.00 121.96 ?  146  PHE D C   1 
ATOM   13849 O  O   . PHE D 4  146  ? -71.407 1.248    86.317  1.00 133.53 ?  146  PHE D O   1 
ATOM   13850 C  CB  . PHE D 4  146  ? -69.324 2.293    84.054  1.00 114.72 ?  146  PHE D CB  1 
ATOM   13851 C  CG  . PHE D 4  146  ? -69.130 2.707    82.615  1.00 118.35 ?  146  PHE D CG  1 
ATOM   13852 C  CD1 . PHE D 4  146  ? -70.141 3.347    81.913  1.00 120.57 ?  146  PHE D CD1 1 
ATOM   13853 C  CD2 . PHE D 4  146  ? -67.926 2.472    81.971  1.00 119.33 ?  146  PHE D CD2 1 
ATOM   13854 C  CE1 . PHE D 4  146  ? -69.960 3.727    80.594  1.00 122.99 ?  146  PHE D CE1 1 
ATOM   13855 C  CE2 . PHE D 4  146  ? -67.738 2.856    80.651  1.00 121.04 ?  146  PHE D CE2 1 
ATOM   13856 C  CZ  . PHE D 4  146  ? -68.756 3.485    79.963  1.00 119.71 ?  146  PHE D CZ  1 
ATOM   13857 N  N   . PHE D 4  147  ? -69.549 -0.023   86.298  1.00 99.09  ?  147  PHE D N   1 
ATOM   13858 C  CA  . PHE D 4  147  ? -69.726 -0.513   87.657  1.00 99.55  ?  147  PHE D CA  1 
ATOM   13859 C  C   . PHE D 4  147  ? -68.456 -0.284   88.464  1.00 100.66 ?  147  PHE D C   1 
ATOM   13860 O  O   . PHE D 4  147  ? -67.363 -0.131   87.914  1.00 97.37  ?  147  PHE D O   1 
ATOM   13861 C  CB  . PHE D 4  147  ? -70.073 -2.009   87.678  1.00 99.44  ?  147  PHE D CB  1 
ATOM   13862 C  CG  . PHE D 4  147  ? -71.536 -2.307   87.489  1.00 105.67 ?  147  PHE D CG  1 
ATOM   13863 C  CD1 . PHE D 4  147  ? -72.124 -2.190   86.243  1.00 105.57 ?  147  PHE D CD1 1 
ATOM   13864 C  CD2 . PHE D 4  147  ? -72.318 -2.722   88.554  1.00 112.17 ?  147  PHE D CD2 1 
ATOM   13865 C  CE1 . PHE D 4  147  ? -73.468 -2.473   86.059  1.00 108.05 ?  147  PHE D CE1 1 
ATOM   13866 C  CE2 . PHE D 4  147  ? -73.663 -3.008   88.376  1.00 116.64 ?  147  PHE D CE2 1 
ATOM   13867 C  CZ  . PHE D 4  147  ? -74.235 -2.887   87.126  1.00 110.81 ?  147  PHE D CZ  1 
ATOM   13868 N  N   . LEU D 4  148  ? -68.618 -0.278   89.787  1.00 116.24 ?  148  LEU D N   1 
ATOM   13869 C  CA  . LEU D 4  148  ? -67.509 -0.233   90.731  1.00 115.85 ?  148  LEU D CA  1 
ATOM   13870 C  C   . LEU D 4  148  ? -67.880 -1.054   91.955  1.00 115.73 ?  148  LEU D C   1 
ATOM   13871 O  O   . LEU D 4  148  ? -69.020 -0.995   92.425  1.00 119.73 ?  148  LEU D O   1 
ATOM   13872 C  CB  . LEU D 4  148  ? -67.164 1.204    91.149  1.00 119.16 ?  148  LEU D CB  1 
ATOM   13873 C  CG  . LEU D 4  148  ? -66.128 1.358    92.268  1.00 112.14 ?  148  LEU D CG  1 
ATOM   13874 C  CD1 . LEU D 4  148  ? -64.774 0.840    91.820  1.00 115.15 ?  148  LEU D CD1 1 
ATOM   13875 C  CD2 . LEU D 4  148  ? -66.024 2.809    92.723  1.00 104.64 ?  148  LEU D CD2 1 
ATOM   13876 N  N   . CYS D 4  149  ? -66.917 -1.818   92.471  1.00 112.03 ?  149  CYS D N   1 
ATOM   13877 C  CA  . CYS D 4  149  ? -67.177 -2.741   93.566  1.00 116.07 ?  149  CYS D CA  1 
ATOM   13878 C  C   . CYS D 4  149  ? -66.026 -2.737   94.560  1.00 123.20 ?  149  CYS D C   1 
ATOM   13879 O  O   . CYS D 4  149  ? -64.857 -2.635   94.175  1.00 121.86 ?  149  CYS D O   1 
ATOM   13880 C  CB  . CYS D 4  149  ? -67.410 -4.166   93.045  1.00 105.22 ?  149  CYS D CB  1 
ATOM   13881 S  SG  . CYS D 4  149  ? -67.494 -5.439   94.325  1.00 115.59 ?  149  CYS D SG  1 
ATOM   13882 N  N   . ILE D 4  150  ? -66.373 -2.846   95.841  1.00 115.03 ?  150  ILE D N   1 
ATOM   13883 C  CA  . ILE D 4  150  ? -65.412 -2.963   96.931  1.00 110.19 ?  150  ILE D CA  1 
ATOM   13884 C  C   . ILE D 4  150  ? -65.646 -4.305   97.605  1.00 107.84 ?  150  ILE D C   1 
ATOM   13885 O  O   . ILE D 4  150  ? -66.733 -4.556   98.140  1.00 100.80 ?  150  ILE D O   1 
ATOM   13886 C  CB  . ILE D 4  150  ? -65.541 -1.814   97.942  1.00 106.34 ?  150  ILE D CB  1 
ATOM   13887 C  CG1 . ILE D 4  150  ? -65.574 -0.466   97.221  1.00 108.76 ?  150  ILE D CG1 1 
ATOM   13888 C  CG2 . ILE D 4  150  ? -64.394 -1.853   98.939  1.00 109.36 ?  150  ILE D CG2 1 
ATOM   13889 C  CD1 . ILE D 4  150  ? -65.593 0.729    98.153  1.00 111.43 ?  150  ILE D CD1 1 
ATOM   13890 N  N   . GLU D 4  151  ? -64.631 -5.162   97.586  1.00 144.08 ?  151  GLU D N   1 
ATOM   13891 C  CA  . GLU D 4  151  ? -64.781 -6.516   98.093  1.00 145.16 ?  151  GLU D CA  1 
ATOM   13892 C  C   . GLU D 4  151  ? -64.736 -6.543   99.619  1.00 144.95 ?  151  GLU D C   1 
ATOM   13893 O  O   . GLU D 4  151  ? -64.223 -5.629   100.272 1.00 147.43 ?  151  GLU D O   1 
ATOM   13894 C  CB  . GLU D 4  151  ? -63.684 -7.419   97.532  1.00 145.00 ?  151  GLU D CB  1 
ATOM   13895 C  CG  . GLU D 4  151  ? -63.636 -7.476   96.015  1.00 144.05 ?  151  GLU D CG  1 
ATOM   13896 C  CD  . GLU D 4  151  ? -62.310 -7.994   95.492  1.00 144.93 ?  151  GLU D CD  1 
ATOM   13897 O  OE1 . GLU D 4  151  ? -61.427 -8.311   96.317  1.00 146.46 ?  151  GLU D OE1 1 
ATOM   13898 O  OE2 . GLU D 4  151  ? -62.148 -8.078   94.256  1.00 147.14 -1 151  GLU D OE2 1 
ATOM   13899 N  N   . ALA D 4  152  ? -65.281 -7.625   100.185 1.00 107.92 ?  152  ALA D N   1 
ATOM   13900 C  CA  . ALA D 4  152  ? -65.179 -7.860   101.622 1.00 106.69 ?  152  ALA D CA  1 
ATOM   13901 C  C   . ALA D 4  152  ? -63.745 -8.122   102.070 1.00 107.00 ?  152  ALA D C   1 
ATOM   13902 O  O   . ALA D 4  152  ? -63.426 -7.911   103.245 1.00 112.74 ?  152  ALA D O   1 
ATOM   13903 C  CB  . ALA D 4  152  ? -66.067 -9.040   102.019 1.00 107.12 ?  152  ALA D CB  1 
ATOM   13904 N  N   . THR D 4  153  ? -62.878 -8.576   101.163 1.00 124.06 ?  153  THR D N   1 
ATOM   13905 C  CA  . THR D 4  153  ? -61.477 -8.798   101.501 1.00 127.12 ?  153  THR D CA  1 
ATOM   13906 C  C   . THR D 4  153  ? -60.770 -7.510   101.892 1.00 131.62 ?  153  THR D C   1 
ATOM   13907 O  O   . THR D 4  153  ? -59.671 -7.567   102.455 1.00 135.94 ?  153  THR D O   1 
ATOM   13908 C  CB  . THR D 4  153  ? -60.759 -9.454   100.321 1.00 132.95 ?  153  THR D CB  1 
ATOM   13909 O  OG1 . THR D 4  153  ? -60.784 -8.566   99.196  1.00 136.19 ?  153  THR D OG1 1 
ATOM   13910 C  CG2 . THR D 4  153  ? -61.440 -10.755  99.946  1.00 133.71 ?  153  THR D CG2 1 
ATOM   13911 N  N   . ASP D 4  154  ? -61.365 -6.362   101.588 1.00 192.44 ?  154  ASP D N   1 
ATOM   13912 C  CA  . ASP D 4  154  ? -60.839 -5.087   102.044 1.00 197.50 ?  154  ASP D CA  1 
ATOM   13913 C  C   . ASP D 4  154  ? -60.683 -5.121   103.563 1.00 202.71 ?  154  ASP D C   1 
ATOM   13914 O  O   . ASP D 4  154  ? -61.634 -5.487   104.268 1.00 206.84 ?  154  ASP D O   1 
ATOM   13915 C  CB  . ASP D 4  154  ? -61.785 -3.960   101.611 1.00 200.10 ?  154  ASP D CB  1 
ATOM   13916 C  CG  . ASP D 4  154  ? -61.276 -2.562   101.963 1.00 201.61 ?  154  ASP D CG  1 
ATOM   13917 O  OD1 . ASP D 4  154  ? -60.559 -2.381   102.970 1.00 203.10 ?  154  ASP D OD1 1 
ATOM   13918 O  OD2 . ASP D 4  154  ? -61.616 -1.623   101.212 1.00 198.92 -1 154  ASP D OD2 1 
ATOM   13919 N  N   . PRO D 4  155  ? -59.506 -4.786   104.097 1.00 135.23 ?  155  PRO D N   1 
ATOM   13920 C  CA  . PRO D 4  155  ? -59.308 -4.846   105.556 1.00 133.68 ?  155  PRO D CA  1 
ATOM   13921 C  C   . PRO D 4  155  ? -60.359 -4.104   106.360 1.00 132.16 ?  155  PRO D C   1 
ATOM   13922 O  O   . PRO D 4  155  ? -60.666 -4.516   107.488 1.00 131.54 ?  155  PRO D O   1 
ATOM   13923 C  CB  . PRO D 4  155  ? -57.917 -4.216   105.745 1.00 127.61 ?  155  PRO D CB  1 
ATOM   13924 C  CG  . PRO D 4  155  ? -57.552 -3.606   104.403 1.00 133.74 ?  155  PRO D CG  1 
ATOM   13925 C  CD  . PRO D 4  155  ? -58.259 -4.446   103.396 1.00 130.64 ?  155  PRO D CD  1 
ATOM   13926 N  N   . LEU D 4  156  ? -60.919 -3.020   105.820 1.00 126.58 ?  156  LEU D N   1 
ATOM   13927 C  CA  . LEU D 4  156  ? -61.928 -2.264   106.554 1.00 129.17 ?  156  LEU D CA  1 
ATOM   13928 C  C   . LEU D 4  156  ? -63.131 -3.135   106.894 1.00 137.66 ?  156  LEU D C   1 
ATOM   13929 O  O   . LEU D 4  156  ? -63.602 -3.137   108.038 1.00 146.21 ?  156  LEU D O   1 
ATOM   13930 C  CB  . LEU D 4  156  ? -62.354 -1.035   105.749 1.00 124.82 ?  156  LEU D CB  1 
ATOM   13931 C  CG  . LEU D 4  156  ? -61.210 -0.078   105.416 1.00 123.01 ?  156  LEU D CG  1 
ATOM   13932 C  CD1 . LEU D 4  156  ? -61.721 1.162    104.697 1.00 117.72 ?  156  LEU D CD1 1 
ATOM   13933 C  CD2 . LEU D 4  156  ? -60.454 0.295    106.683 1.00 119.48 ?  156  LEU D CD2 1 
ATOM   13934 N  N   . PHE D 4  157  ? -63.633 -3.891   105.913 1.00 181.16 ?  157  PHE D N   1 
ATOM   13935 C  CA  . PHE D 4  157  ? -64.747 -4.821   106.121 1.00 186.09 ?  157  PHE D CA  1 
ATOM   13936 C  C   . PHE D 4  157  ? -65.956 -4.098   106.709 1.00 183.78 ?  157  PHE D C   1 
ATOM   13937 O  O   . PHE D 4  157  ? -66.668 -4.624   107.568 1.00 182.54 ?  157  PHE D O   1 
ATOM   13938 C  CB  . PHE D 4  157  ? -64.319 -5.991   107.013 1.00 185.02 ?  157  PHE D CB  1 
ATOM   13939 C  CG  . PHE D 4  157  ? -64.771 -7.334   106.516 1.00 181.91 ?  157  PHE D CG  1 
ATOM   13940 C  CD1 . PHE D 4  157  ? -66.040 -7.504   105.991 1.00 184.30 ?  157  PHE D CD1 1 
ATOM   13941 C  CD2 . PHE D 4  157  ? -63.923 -8.430   106.578 1.00 178.45 ?  157  PHE D CD2 1 
ATOM   13942 C  CE1 . PHE D 4  157  ? -66.457 -8.740   105.534 1.00 189.45 ?  157  PHE D CE1 1 
ATOM   13943 C  CE2 . PHE D 4  157  ? -64.334 -9.669   106.122 1.00 178.09 ?  157  PHE D CE2 1 
ATOM   13944 C  CZ  . PHE D 4  157  ? -65.603 -9.824   105.599 1.00 186.29 ?  157  PHE D CZ  1 
ATOM   13945 N  N   . ASP D 4  158  ? -66.186 -2.870   106.236 1.00 211.26 ?  158  ASP D N   1 
ATOM   13946 C  CA  . ASP D 4  158  ? -67.144 -1.979   106.882 1.00 216.10 ?  158  ASP D CA  1 
ATOM   13947 C  C   . ASP D 4  158  ? -68.585 -2.429   106.672 1.00 208.67 ?  158  ASP D C   1 
ATOM   13948 O  O   . ASP D 4  158  ? -69.449 -2.136   107.508 1.00 210.18 ?  158  ASP D O   1 
ATOM   13949 C  CB  . ASP D 4  158  ? -66.957 -0.556   106.361 1.00 222.63 ?  158  ASP D CB  1 
ATOM   13950 C  CG  . ASP D 4  158  ? -65.639 0.056    106.791 1.00 224.83 ?  158  ASP D CG  1 
ATOM   13951 O  OD1 . ASP D 4  158  ? -65.028 -0.459   107.752 1.00 223.66 ?  158  ASP D OD1 1 
ATOM   13952 O  OD2 . ASP D 4  158  ? -65.219 1.055    106.169 1.00 226.96 -1 158  ASP D OD2 1 
ATOM   13953 N  N   . ARG D 4  159  ? -68.860 -3.134   105.573 1.00 119.38 ?  159  ARG D N   1 
ATOM   13954 C  CA  . ARG D 4  159  ? -70.213 -3.539   105.200 1.00 121.04 ?  159  ARG D CA  1 
ATOM   13955 C  C   . ARG D 4  159  ? -71.135 -2.338   105.012 1.00 121.22 ?  159  ARG D C   1 
ATOM   13956 O  O   . ARG D 4  159  ? -71.135 -1.710   103.947 1.00 118.84 ?  159  ARG D O   1 
ATOM   13957 C  CB  . ARG D 4  159  ? -70.805 -4.501   106.238 1.00 122.56 ?  159  ARG D CB  1 
ATOM   13958 C  CG  . ARG D 4  159  ? -72.044 -5.237   105.751 1.00 124.78 ?  159  ARG D CG  1 
ATOM   13959 C  CD  . ARG D 4  159  ? -72.430 -6.387   106.663 1.00 131.27 ?  159  ARG D CD  1 
ATOM   13960 N  NE  . ARG D 4  159  ? -73.691 -6.989   106.242 1.00 139.66 ?  159  ARG D NE  1 
ATOM   13961 C  CZ  . ARG D 4  159  ? -73.795 -7.988   105.376 1.00 135.00 ?  159  ARG D CZ  1 
ATOM   13962 N  NH1 . ARG D 4  159  ? -72.728 -8.531   104.813 1.00 133.58 ?  159  ARG D NH1 1 
ATOM   13963 N  NH2 . ARG D 4  159  ? -75.001 -8.457   105.069 1.00 128.90 ?  159  ARG D NH2 1 
ATOM   13964 N  N   . SER D 4  160  ? -71.933 -2.017   106.036 1.00 142.52 ?  160  SER D N   1 
ATOM   13965 C  CA  . SER D 4  160  ? -72.931 -0.960   105.892 1.00 140.25 ?  160  SER D CA  1 
ATOM   13966 C  C   . SER D 4  160  ? -72.275 0.400    105.690 1.00 136.20 ?  160  SER D C   1 
ATOM   13967 O  O   . SER D 4  160  ? -72.799 1.248    104.958 1.00 136.39 ?  160  SER D O   1 
ATOM   13968 C  CB  . SER D 4  160  ? -73.855 -0.939   107.110 1.00 135.79 ?  160  SER D CB  1 
ATOM   13969 O  OG  . SER D 4  160  ? -73.119 -0.768   108.307 1.00 146.30 ?  160  SER D OG  1 
ATOM   13970 N  N   . ARG D 4  161  ? -71.128 0.630    106.336 1.00 145.17 ?  161  ARG D N   1 
ATOM   13971 C  CA  . ARG D 4  161  ? -70.385 1.864    106.105 1.00 143.13 ?  161  ARG D CA  1 
ATOM   13972 C  C   . ARG D 4  161  ? -69.880 1.934    104.670 1.00 148.69 ?  161  ARG D C   1 
ATOM   13973 O  O   . ARG D 4  161  ? -69.900 3.003    104.047 1.00 147.87 ?  161  ARG D O   1 
ATOM   13974 C  CB  . ARG D 4  161  ? -69.222 1.969    107.091 1.00 144.82 ?  161  ARG D CB  1 
ATOM   13975 C  CG  . ARG D 4  161  ? -69.635 2.110    108.545 1.00 154.46 ?  161  ARG D CG  1 
ATOM   13976 C  CD  . ARG D 4  161  ? -68.458 2.558    109.403 1.00 157.03 ?  161  ARG D CD  1 
ATOM   13977 N  NE  . ARG D 4  161  ? -68.059 3.934    109.133 1.00 162.34 ?  161  ARG D NE  1 
ATOM   13978 C  CZ  . ARG D 4  161  ? -66.974 4.278    108.451 1.00 158.24 ?  161  ARG D CZ  1 
ATOM   13979 N  NH1 . ARG D 4  161  ? -66.156 3.367    107.948 1.00 152.96 ?  161  ARG D NH1 1 
ATOM   13980 N  NH2 . ARG D 4  161  ? -66.705 5.567    108.265 1.00 146.17 ?  161  ARG D NH2 1 
ATOM   13981 N  N   . THR D 4  162  ? -69.425 0.800    104.128 1.00 133.62 ?  162  THR D N   1 
ATOM   13982 C  CA  . THR D 4  162  ? -69.013 0.755    102.729 1.00 128.46 ?  162  THR D CA  1 
ATOM   13983 C  C   . THR D 4  162  ? -70.179 1.083    101.807 1.00 127.38 ?  162  THR D C   1 
ATOM   13984 O  O   . THR D 4  162  ? -70.033 1.857    100.854 1.00 128.31 ?  162  THR D O   1 
ATOM   13985 C  CB  . THR D 4  162  ? -68.430 -0.617   102.390 1.00 130.79 ?  162  THR D CB  1 
ATOM   13986 O  OG1 . THR D 4  162  ? -67.316 -0.890   103.246 1.00 130.82 ?  162  THR D OG1 1 
ATOM   13987 C  CG2 . THR D 4  162  ? -67.970 -0.655   100.945 1.00 125.55 ?  162  THR D CG2 1 
ATOM   13988 N  N   . SER D 4  163  ? -71.348 0.496    102.077 1.00 124.07 ?  163  SER D N   1 
ATOM   13989 C  CA  . SER D 4  163  ? -72.546 0.845    101.321 1.00 123.58 ?  163  SER D CA  1 
ATOM   13990 C  C   . SER D 4  163  ? -72.879 2.323    101.481 1.00 127.12 ?  163  SER D C   1 
ATOM   13991 O  O   . SER D 4  163  ? -73.259 2.991    100.512 1.00 126.09 ?  163  SER D O   1 
ATOM   13992 C  CB  . SER D 4  163  ? -73.720 -0.025   101.771 1.00 119.11 ?  163  SER D CB  1 
ATOM   13993 O  OG  . SER D 4  163  ? -74.950 0.480    101.277 1.00 124.47 ?  163  SER D OG  1 
ATOM   13994 N  N   . GLN D 4  164  ? -72.729 2.854    102.697 1.00 146.74 ?  164  GLN D N   1 
ATOM   13995 C  CA  . GLN D 4  164  ? -72.985 4.273    102.918 1.00 140.75 ?  164  GLN D CA  1 
ATOM   13996 C  C   . GLN D 4  164  ? -71.941 5.138    102.224 1.00 145.63 ?  164  GLN D C   1 
ATOM   13997 O  O   . GLN D 4  164  ? -72.273 6.190    101.666 1.00 148.12 ?  164  GLN D O   1 
ATOM   13998 C  CB  . GLN D 4  164  ? -73.030 4.573    104.415 1.00 140.17 ?  164  GLN D CB  1 
ATOM   13999 C  CG  . GLN D 4  164  ? -74.384 4.314    105.053 1.00 153.16 ?  164  GLN D CG  1 
ATOM   14000 C  CD  . GLN D 4  164  ? -75.427 5.332    104.634 1.00 152.72 ?  164  GLN D CD  1 
ATOM   14001 O  OE1 . GLN D 4  164  ? -75.097 6.449    104.238 1.00 155.10 ?  164  GLN D OE1 1 
ATOM   14002 N  NE2 . GLN D 4  164  ? -76.695 4.950    104.723 1.00 145.72 ?  164  GLN D NE2 1 
ATOM   14003 N  N   . PHE D 4  165  ? -70.673 4.716    102.250 1.00 145.09 ?  165  PHE D N   1 
ATOM   14004 C  CA  . PHE D 4  165  ? -69.648 5.429    101.493 1.00 144.67 ?  165  PHE D CA  1 
ATOM   14005 C  C   . PHE D 4  165  ? -69.966 5.414    100.005 1.00 144.18 ?  165  PHE D C   1 
ATOM   14006 O  O   . PHE D 4  165  ? -69.810 6.430    99.316  1.00 143.58 ?  165  PHE D O   1 
ATOM   14007 C  CB  . PHE D 4  165  ? -68.272 4.816    101.750 1.00 141.06 ?  165  PHE D CB  1 
ATOM   14008 C  CG  . PHE D 4  165  ? -67.216 5.282    100.785 1.00 141.87 ?  165  PHE D CG  1 
ATOM   14009 C  CD1 . PHE D 4  165  ? -66.646 6.537    100.915 1.00 136.51 ?  165  PHE D CD1 1 
ATOM   14010 C  CD2 . PHE D 4  165  ? -66.801 4.469    99.741  1.00 150.12 ?  165  PHE D CD2 1 
ATOM   14011 C  CE1 . PHE D 4  165  ? -65.678 6.973    100.027 1.00 147.02 ?  165  PHE D CE1 1 
ATOM   14012 C  CE2 . PHE D 4  165  ? -65.833 4.900    98.849  1.00 151.01 ?  165  PHE D CE2 1 
ATOM   14013 C  CZ  . PHE D 4  165  ? -65.271 6.153    98.993  1.00 152.77 ?  165  PHE D CZ  1 
ATOM   14014 N  N   . LEU D 4  166  ? -70.414 4.266    99.492  1.00 100.20 ?  166  LEU D N   1 
ATOM   14015 C  CA  . LEU D 4  166  ? -70.835 4.193    98.098  1.00 101.34 ?  166  LEU D CA  1 
ATOM   14016 C  C   . LEU D 4  166  ? -72.088 5.027    97.862  1.00 109.59 ?  166  LEU D C   1 
ATOM   14017 O  O   . LEU D 4  166  ? -72.267 5.595    96.778  1.00 108.58 ?  166  LEU D O   1 
ATOM   14018 C  CB  . LEU D 4  166  ? -71.069 2.736    97.698  1.00 93.24  ?  166  LEU D CB  1 
ATOM   14019 C  CG  . LEU D 4  166  ? -69.819 1.897    97.419  1.00 89.99  ?  166  LEU D CG  1 
ATOM   14020 C  CD1 . LEU D 4  166  ? -70.156 0.700    96.545  1.00 96.27  ?  166  LEU D CD1 1 
ATOM   14021 C  CD2 . LEU D 4  166  ? -68.721 2.736    96.780  1.00 93.71  ?  166  LEU D CD2 1 
ATOM   14022 N  N   . ARG D 4  167  ? -72.963 5.114    98.867  1.00 136.42 ?  167  ARG D N   1 
ATOM   14023 C  CA  . ARG D 4  167  ? -74.141 5.969    98.757  1.00 131.25 ?  167  ARG D CA  1 
ATOM   14024 C  C   . ARG D 4  167  ? -73.766 7.445    98.795  1.00 132.84 ?  167  ARG D C   1 
ATOM   14025 O  O   . ARG D 4  167  ? -74.465 8.276    98.203  1.00 131.81 ?  167  ARG D O   1 
ATOM   14026 C  CB  . ARG D 4  167  ? -75.131 5.646    99.875  1.00 127.49 ?  167  ARG D CB  1 
ATOM   14027 C  CG  . ARG D 4  167  ? -76.014 4.430    99.615  1.00 118.70 ?  167  ARG D CG  1 
ATOM   14028 C  CD  . ARG D 4  167  ? -76.921 4.650    98.415  1.00 120.91 ?  167  ARG D CD  1 
ATOM   14029 N  NE  . ARG D 4  167  ? -77.878 3.562    98.248  1.00 126.02 ?  167  ARG D NE  1 
ATOM   14030 C  CZ  . ARG D 4  167  ? -78.747 3.474    97.250  1.00 123.80 ?  167  ARG D CZ  1 
ATOM   14031 N  NH1 . ARG D 4  167  ? -78.806 4.395    96.302  1.00 126.41 ?  167  ARG D NH1 1 
ATOM   14032 N  NH2 . ARG D 4  167  ? -79.578 2.437    97.203  1.00 111.71 ?  167  ARG D NH2 1 
ATOM   14033 N  N   . SER D 4  168  ? -72.686 7.789    99.500  1.00 143.75 ?  168  SER D N   1 
ATOM   14034 C  CA  . SER D 4  168  ? -72.206 9.167    99.491  1.00 148.34 ?  168  SER D CA  1 
ATOM   14035 C  C   . SER D 4  168  ? -71.760 9.567    98.092  1.00 155.38 ?  168  SER D C   1 
ATOM   14036 O  O   . SER D 4  168  ? -72.118 10.640   97.591  1.00 156.73 ?  168  SER D O   1 
ATOM   14037 C  CB  . SER D 4  168  ? -71.064 9.330    100.495 1.00 144.94 ?  168  SER D CB  1 
ATOM   14038 O  OG  . SER D 4  168  ? -70.359 10.540   100.282 1.00 139.73 ?  168  SER D OG  1 
ATOM   14039 N  N   . LEU D 4  169  ? -70.964 8.714    97.450  1.00 162.34 ?  169  LEU D N   1 
ATOM   14040 C  CA  . LEU D 4  169  ? -70.747 8.827    96.018  1.00 159.48 ?  169  LEU D CA  1 
ATOM   14041 C  C   . LEU D 4  169  ? -72.093 8.689    95.318  1.00 159.47 ?  169  LEU D C   1 
ATOM   14042 O  O   . LEU D 4  169  ? -73.035 8.129    95.873  1.00 163.77 ?  169  LEU D O   1 
ATOM   14043 C  CB  . LEU D 4  169  ? -69.771 7.747    95.549  1.00 154.55 ?  169  LEU D CB  1 
ATOM   14044 C  CG  . LEU D 4  169  ? -68.266 8.029    95.627  1.00 151.77 ?  169  LEU D CG  1 
ATOM   14045 C  CD1 . LEU D 4  169  ? -67.854 8.639    96.956  1.00 142.88 ?  169  LEU D CD1 1 
ATOM   14046 C  CD2 . LEU D 4  169  ? -67.480 6.744    95.374  1.00 150.21 ?  169  LEU D CD2 1 
ATOM   14047 N  N   . ASN D 4  170  ? -72.197 9.224    94.098  1.00 122.91 ?  170  ASN D N   1 
ATOM   14048 C  CA  . ASN D 4  170  ? -73.512 9.274    93.457  1.00 130.66 ?  170  ASN D CA  1 
ATOM   14049 C  C   . ASN D 4  170  ? -73.799 8.033    92.617  1.00 123.98 ?  170  ASN D C   1 
ATOM   14050 O  O   . ASN D 4  170  ? -73.282 7.904    91.501  1.00 120.80 ?  170  ASN D O   1 
ATOM   14051 C  CB  . ASN D 4  170  ? -73.645 10.521   92.583  1.00 132.93 ?  170  ASN D CB  1 
ATOM   14052 C  CG  . ASN D 4  170  ? -75.048 10.697   92.039  1.00 134.64 ?  170  ASN D CG  1 
ATOM   14053 O  OD1 . ASN D 4  170  ? -76.032 10.460   92.740  1.00 137.33 ?  170  ASN D OD1 1 
ATOM   14054 N  ND2 . ASN D 4  170  ? -75.148 11.107   90.780  1.00 130.58 ?  170  ASN D ND2 1 
ATOM   14055 N  N   . PRO D 4  171  ? -74.643 7.116    93.097  1.00 165.87 ?  171  PRO D N   1 
ATOM   14056 C  CA  . PRO D 4  171  ? -74.858 5.865    92.368  1.00 164.51 ?  171  PRO D CA  1 
ATOM   14057 C  C   . PRO D 4  171  ? -76.250 5.760    91.769  1.00 165.53 ?  171  PRO D C   1 
ATOM   14058 O  O   . PRO D 4  171  ? -77.240 6.116    92.417  1.00 170.34 ?  171  PRO D O   1 
ATOM   14059 C  CB  . PRO D 4  171  ? -74.646 4.815    93.463  1.00 156.87 ?  171  PRO D CB  1 
ATOM   14060 C  CG  . PRO D 4  171  ? -75.052 5.568    94.782  1.00 167.49 ?  171  PRO D CG  1 
ATOM   14061 C  CD  . PRO D 4  171  ? -75.260 7.034    94.428  1.00 173.97 ?  171  PRO D CD  1 
ATOM   14062 N  N   . MET D 4  172  ? -76.353 5.269    90.534  1.00 148.63 ?  172  MET D N   1 
ATOM   14063 C  CA  . MET D 4  172  ? -77.674 4.936    90.014  1.00 145.34 ?  172  MET D CA  1 
ATOM   14064 C  C   . MET D 4  172  ? -78.334 3.867    90.873  1.00 147.26 ?  172  MET D C   1 
ATOM   14065 O  O   . MET D 4  172  ? -79.554 3.885    91.072  1.00 153.08 ?  172  MET D O   1 
ATOM   14066 C  CB  . MET D 4  172  ? -77.585 4.475    88.560  1.00 146.97 ?  172  MET D CB  1 
ATOM   14067 C  CG  . MET D 4  172  ? -77.387 5.597    87.558  1.00 154.18 ?  172  MET D CG  1 
ATOM   14068 S  SD  . MET D 4  172  ? -77.509 5.012    85.857  1.00 153.15 ?  172  MET D SD  1 
ATOM   14069 C  CE  . MET D 4  172  ? -79.157 4.320    85.861  1.00 135.01 ?  172  MET D CE  1 
ATOM   14070 N  N   . GLN D 4  173  ? -77.538 2.942    91.409  1.00 140.96 ?  173  GLN D N   1 
ATOM   14071 C  CA  . GLN D 4  173  ? -78.048 1.888    92.275  1.00 145.94 ?  173  GLN D CA  1 
ATOM   14072 C  C   . GLN D 4  173  ? -76.880 1.254    93.014  1.00 146.42 ?  173  GLN D C   1 
ATOM   14073 O  O   . GLN D 4  173  ? -75.855 0.936    92.402  1.00 145.72 ?  173  GLN D O   1 
ATOM   14074 C  CB  . GLN D 4  173  ? -78.810 0.826    91.474  1.00 145.69 ?  173  GLN D CB  1 
ATOM   14075 C  CG  . GLN D 4  173  ? -79.245 -0.381   92.288  1.00 141.13 ?  173  GLN D CG  1 
ATOM   14076 C  CD  . GLN D 4  173  ? -79.879 -1.454   91.431  1.00 141.81 ?  173  GLN D CD  1 
ATOM   14077 O  OE1 . GLN D 4  173  ? -80.209 -1.224   90.267  1.00 129.50 ?  173  GLN D OE1 1 
ATOM   14078 N  NE2 . GLN D 4  173  ? -80.059 -2.636   92.005  1.00 156.72 ?  173  GLN D NE2 1 
ATOM   14079 N  N   . VAL D 4  174  ? -77.041 1.078    94.323  1.00 119.37 ?  174  VAL D N   1 
ATOM   14080 C  CA  . VAL D 4  174  ? -76.072 0.387    95.167  1.00 112.44 ?  174  VAL D CA  1 
ATOM   14081 C  C   . VAL D 4  174  ? -76.624 -0.991   95.498  1.00 115.04 ?  174  VAL D C   1 
ATOM   14082 O  O   . VAL D 4  174  ? -77.776 -1.119   95.932  1.00 110.16 ?  174  VAL D O   1 
ATOM   14083 C  CB  . VAL D 4  174  ? -75.769 1.180    96.449  1.00 108.85 ?  174  VAL D CB  1 
ATOM   14084 C  CG1 . VAL D 4  174  ? -75.087 0.292    97.470  1.00 108.57 ?  174  VAL D CG1 1 
ATOM   14085 C  CG2 . VAL D 4  174  ? -74.884 2.360    96.134  1.00 109.32 ?  174  VAL D CG2 1 
ATOM   14086 N  N   . SER D 4  175  ? -75.803 -2.018   95.295  1.00 131.32 ?  175  SER D N   1 
ATOM   14087 C  CA  . SER D 4  175  ? -76.208 -3.399   95.505  1.00 133.35 ?  175  SER D CA  1 
ATOM   14088 C  C   . SER D 4  175  ? -75.181 -4.115   96.369  1.00 131.97 ?  175  SER D C   1 
ATOM   14089 O  O   . SER D 4  175  ? -74.005 -3.744   96.397  1.00 125.56 ?  175  SER D O   1 
ATOM   14090 C  CB  . SER D 4  175  ? -76.371 -4.143   94.173  1.00 136.13 ?  175  SER D CB  1 
ATOM   14091 O  OG  . SER D 4  175  ? -77.200 -3.420   93.282  1.00 140.86 ?  175  SER D OG  1 
ATOM   14092 N  N   . GLU D 4  176  ? -75.638 -5.146   97.073  1.00 157.77 ?  176  GLU D N   1 
ATOM   14093 C  CA  . GLU D 4  176  ? -74.784 -5.981   97.916  1.00 160.76 ?  176  GLU D CA  1 
ATOM   14094 C  C   . GLU D 4  176  ? -74.580 -7.306   97.190  1.00 158.36 ?  176  GLU D C   1 
ATOM   14095 O  O   . GLU D 4  176  ? -75.434 -8.196   97.250  1.00 160.83 ?  176  GLU D O   1 
ATOM   14096 C  CB  . GLU D 4  176  ? -75.405 -6.185   99.294  1.00 161.25 ?  176  GLU D CB  1 
ATOM   14097 C  CG  . GLU D 4  176  ? -75.692 -4.894   100.044 1.00 166.00 ?  176  GLU D CG  1 
ATOM   14098 C  CD  . GLU D 4  176  ? -76.126 -5.135   101.477 1.00 177.99 ?  176  GLU D CD  1 
ATOM   14099 O  OE1 . GLU D 4  176  ? -76.156 -6.309   101.901 1.00 180.53 ?  176  GLU D OE1 1 
ATOM   14100 O  OE2 . GLU D 4  176  ? -76.441 -4.149   102.178 1.00 171.54 -1 176  GLU D OE2 1 
ATOM   14101 N  N   . VAL D 4  177  ? -73.450 -7.433   96.502  1.00 145.12 ?  177  VAL D N   1 
ATOM   14102 C  CA  . VAL D 4  177  ? -73.158 -8.633   95.727  1.00 141.14 ?  177  VAL D CA  1 
ATOM   14103 C  C   . VAL D 4  177  ? -72.766 -9.763   96.673  1.00 141.59 ?  177  VAL D C   1 
ATOM   14104 O  O   . VAL D 4  177  ? -71.918 -9.589   97.557  1.00 144.31 ?  177  VAL D O   1 
ATOM   14105 C  CB  . VAL D 4  177  ? -72.062 -8.355   94.685  1.00 143.13 ?  177  VAL D CB  1 
ATOM   14106 C  CG1 . VAL D 4  177  ? -70.848 -7.715   95.324  1.00 133.50 ?  177  VAL D CG1 1 
ATOM   14107 C  CG2 . VAL D 4  177  ? -71.660 -9.635   93.999  1.00 149.90 ?  177  VAL D CG2 1 
ATOM   14108 N  N   . ALA D 4  178  ? -73.397 -10.920  96.498  1.00 125.56 ?  178  ALA D N   1 
ATOM   14109 C  CA  . ALA D 4  178  ? -73.164 -12.087  97.333  1.00 135.61 ?  178  ALA D CA  1 
ATOM   14110 C  C   . ALA D 4  178  ? -72.708 -13.259  96.474  1.00 140.18 ?  178  ALA D C   1 
ATOM   14111 O  O   . ALA D 4  178  ? -72.808 -13.240  95.244  1.00 142.17 ?  178  ALA D O   1 
ATOM   14112 C  CB  . ALA D 4  178  ? -74.426 -12.463  98.122  1.00 146.18 ?  178  ALA D CB  1 
ATOM   14113 N  N   . TYR D 4  179  ? -72.203 -14.290  97.144  1.00 158.13 ?  179  TYR D N   1 
ATOM   14114 C  CA  . TYR D 4  179  ? -71.706 -15.482  96.466  1.00 153.25 ?  179  TYR D CA  1 
ATOM   14115 C  C   . TYR D 4  179  ? -72.846 -16.261  95.817  1.00 157.94 ?  179  TYR D C   1 
ATOM   14116 O  O   . TYR D 4  179  ? -72.699 -17.440  95.494  1.00 162.48 ?  179  TYR D O   1 
ATOM   14117 C  CB  . TYR D 4  179  ? -70.949 -16.379  97.447  1.00 154.79 ?  179  TYR D CB  1 
ATOM   14118 C  CG  . TYR D 4  179  ? -69.860 -15.664  98.214  1.00 154.95 ?  179  TYR D CG  1 
ATOM   14119 C  CD1 . TYR D 4  179  ? -68.626 -15.409  97.631  1.00 154.96 ?  179  TYR D CD1 1 
ATOM   14120 C  CD2 . TYR D 4  179  ? -70.066 -15.245  99.522  1.00 153.16 ?  179  TYR D CD2 1 
ATOM   14121 C  CE1 . TYR D 4  179  ? -67.627 -14.756  98.329  1.00 156.43 ?  179  TYR D CE1 1 
ATOM   14122 C  CE2 . TYR D 4  179  ? -69.074 -14.592  100.228 1.00 148.16 ?  179  TYR D CE2 1 
ATOM   14123 C  CZ  . TYR D 4  179  ? -67.857 -14.350  99.627  1.00 153.19 ?  179  TYR D CZ  1 
ATOM   14124 O  OH  . TYR D 4  179  ? -66.866 -13.699  100.327 1.00 154.60 ?  179  TYR D OH  1 
ATOM   14125 N  N   . CYS E 5  26   ? -52.136 -48.829  55.863  1.00 113.66 ?  26   CYS E N   1 
ATOM   14126 C  CA  . CYS E 5  26   ? -52.321 -47.383  55.889  1.00 105.15 ?  26   CYS E CA  1 
ATOM   14127 C  C   . CYS E 5  26   ? -51.452 -46.705  54.835  1.00 99.69  ?  26   CYS E C   1 
ATOM   14128 O  O   . CYS E 5  26   ? -51.388 -45.478  54.761  1.00 103.26 ?  26   CYS E O   1 
ATOM   14129 C  CB  . CYS E 5  26   ? -52.009 -46.825  57.280  1.00 102.25 ?  26   CYS E CB  1 
ATOM   14130 S  SG  . CYS E 5  26   ? -53.071 -47.473  58.596  1.00 103.79 ?  26   CYS E SG  1 
ATOM   14131 N  N   . HIS E 5  27   ? -50.778 -47.515  54.019  1.00 90.48  ?  27   HIS E N   1 
ATOM   14132 C  CA  . HIS E 5  27   ? -50.003 -46.989  52.904  1.00 86.02  ?  27   HIS E CA  1 
ATOM   14133 C  C   . HIS E 5  27   ? -50.077 -47.955  51.730  1.00 95.10  ?  27   HIS E C   1 
ATOM   14134 O  O   . HIS E 5  27   ? -50.832 -47.722  50.780  1.00 99.79  ?  27   HIS E O   1 
ATOM   14135 C  CB  . HIS E 5  27   ? -48.553 -46.747  53.315  1.00 89.46  ?  27   HIS E CB  1 
ATOM   14136 C  CG  . HIS E 5  27   ? -47.770 -45.964  52.312  1.00 88.26  ?  27   HIS E CG  1 
ATOM   14137 N  ND1 . HIS E 5  27   ? -48.273 -44.842  51.689  1.00 80.34  ?  27   HIS E ND1 1 
ATOM   14138 C  CD2 . HIS E 5  27   ? -46.524 -46.142  51.817  1.00 87.14  ?  27   HIS E CD2 1 
ATOM   14139 C  CE1 . HIS E 5  27   ? -47.367 -44.359  50.859  1.00 87.24  ?  27   HIS E CE1 1 
ATOM   14140 N  NE2 . HIS E 5  27   ? -46.295 -45.129  50.918  1.00 94.52  ?  27   HIS E NE2 1 
ATOM   14141 N  N   . GLN E 5  28   ? -49.303 -49.041  51.796  1.00 99.78  ?  28   GLN E N   1 
ATOM   14142 C  CA  . GLN E 5  28   ? -49.372 -50.134  50.822  1.00 91.62  ?  28   GLN E CA  1 
ATOM   14143 C  C   . GLN E 5  28   ? -49.218 -49.622  49.393  1.00 87.29  ?  28   GLN E C   1 
ATOM   14144 O  O   . GLN E 5  28   ? -50.028 -49.912  48.511  1.00 91.98  ?  28   GLN E O   1 
ATOM   14145 C  CB  . GLN E 5  28   ? -50.682 -50.913  50.979  1.00 88.55  ?  28   GLN E CB  1 
ATOM   14146 C  CG  . GLN E 5  28   ? -50.695 -51.872  52.152  1.00 89.80  ?  28   GLN E CG  1 
ATOM   14147 C  CD  . GLN E 5  28   ? -50.585 -53.319  51.718  1.00 89.37  ?  28   GLN E CD  1 
ATOM   14148 O  OE1 . GLN E 5  28   ? -50.316 -53.616  50.552  1.00 86.31  ?  28   GLN E OE1 1 
ATOM   14149 N  NE2 . GLN E 5  28   ? -50.806 -54.231  52.656  1.00 85.43  ?  28   GLN E NE2 1 
ATOM   14150 N  N   . ASP E 5  29   ? -48.168 -48.841  49.167  1.00 75.69  ?  29   ASP E N   1 
ATOM   14151 C  CA  . ASP E 5  29   ? -47.984 -48.256  47.846  1.00 79.18  ?  29   ASP E CA  1 
ATOM   14152 C  C   . ASP E 5  29   ? -47.093 -49.136  46.982  1.00 85.91  ?  29   ASP E C   1 
ATOM   14153 O  O   . ASP E 5  29   ? -47.577 -49.821  46.076  1.00 96.42  ?  29   ASP E O   1 
ATOM   14154 C  CB  . ASP E 5  29   ? -47.404 -46.849  47.966  1.00 80.28  ?  29   ASP E CB  1 
ATOM   14155 C  CG  . ASP E 5  29   ? -48.448 -45.778  47.767  1.00 87.53  ?  29   ASP E CG  1 
ATOM   14156 O  OD1 . ASP E 5  29   ? -49.657 -46.101  47.851  1.00 86.25  ?  29   ASP E OD1 1 
ATOM   14157 O  OD2 . ASP E 5  29   ? -48.066 -44.622  47.508  1.00 79.61  -1 29   ASP E OD2 1 
ATOM   14158 N  N   . MET E 5  30   ? -45.791 -49.125  47.254  1.00 61.89  ?  30   MET E N   1 
ATOM   14159 C  CA  . MET E 5  30   ? -44.860 -50.027  46.594  1.00 59.79  ?  30   MET E CA  1 
ATOM   14160 C  C   . MET E 5  30   ? -44.491 -51.209  47.478  1.00 62.20  ?  30   MET E C   1 
ATOM   14161 O  O   . MET E 5  30   ? -43.481 -51.874  47.225  1.00 56.63  ?  30   MET E O   1 
ATOM   14162 C  CB  . MET E 5  30   ? -43.608 -49.272  46.146  1.00 52.48  ?  30   MET E CB  1 
ATOM   14163 C  CG  . MET E 5  30   ? -43.736 -48.660  44.756  1.00 52.22  ?  30   MET E CG  1 
ATOM   14164 S  SD  . MET E 5  30   ? -42.554 -47.342  44.424  1.00 64.04  ?  30   MET E SD  1 
ATOM   14165 C  CE  . MET E 5  30   ? -43.243 -46.011  45.398  1.00 52.51  ?  30   MET E CE  1 
ATOM   14166 N  N   . TYR E 5  31   ? -45.306 -51.489  48.500  1.00 76.26  ?  31   TYR E N   1 
ATOM   14167 C  CA  . TYR E 5  31   ? -45.044 -52.612  49.395  1.00 65.77  ?  31   TYR E CA  1 
ATOM   14168 C  C   . TYR E 5  31   ? -45.130 -53.934  48.643  1.00 62.79  ?  31   TYR E C   1 
ATOM   14169 O  O   . TYR E 5  31   ? -44.259 -54.801  48.777  1.00 61.78  ?  31   TYR E O   1 
ATOM   14170 C  CB  . TYR E 5  31   ? -46.035 -52.592  50.563  1.00 62.56  ?  31   TYR E CB  1 
ATOM   14171 C  CG  . TYR E 5  31   ? -45.849 -51.465  51.564  1.00 60.51  ?  31   TYR E CG  1 
ATOM   14172 C  CD1 . TYR E 5  31   ? -45.203 -50.287  51.213  1.00 69.62  ?  31   TYR E CD1 1 
ATOM   14173 C  CD2 . TYR E 5  31   ? -46.353 -51.570  52.853  1.00 67.99  ?  31   TYR E CD2 1 
ATOM   14174 C  CE1 . TYR E 5  31   ? -45.043 -49.256  52.122  1.00 79.19  ?  31   TYR E CE1 1 
ATOM   14175 C  CE2 . TYR E 5  31   ? -46.201 -50.543  53.770  1.00 70.39  ?  31   TYR E CE2 1 
ATOM   14176 C  CZ  . TYR E 5  31   ? -45.544 -49.388  53.398  1.00 70.85  ?  31   TYR E CZ  1 
ATOM   14177 O  OH  . TYR E 5  31   ? -45.387 -48.361  54.302  1.00 68.61  ?  31   TYR E OH  1 
ATOM   14178 N  N   . ASP E 5  32   ? -46.186 -54.107  47.853  1.00 86.15  ?  32   ASP E N   1 
ATOM   14179 C  CA  . ASP E 5  32   ? -46.344 -55.247  46.959  1.00 92.52  ?  32   ASP E CA  1 
ATOM   14180 C  C   . ASP E 5  32   ? -46.376 -54.711  45.537  1.00 102.78 ?  32   ASP E C   1 
ATOM   14181 O  O   . ASP E 5  32   ? -47.230 -53.881  45.207  1.00 111.11 ?  32   ASP E O   1 
ATOM   14182 C  CB  . ASP E 5  32   ? -47.624 -56.024  47.273  1.00 95.73  ?  32   ASP E CB  1 
ATOM   14183 C  CG  . ASP E 5  32   ? -47.561 -56.739  48.606  1.00 100.80 ?  32   ASP E CG  1 
ATOM   14184 O  OD1 . ASP E 5  32   ? -46.590 -56.510  49.355  1.00 104.16 ?  32   ASP E OD1 1 
ATOM   14185 O  OD2 . ASP E 5  32   ? -48.479 -57.533  48.903  1.00 95.59  -1 32   ASP E OD2 1 
ATOM   14186 N  N   . GLN E 5  33   ? -45.450 -55.173  44.701  1.00 83.09  ?  33   GLN E N   1 
ATOM   14187 C  CA  . GLN E 5  33   ? -45.280 -54.613  43.370  1.00 75.91  ?  33   GLN E CA  1 
ATOM   14188 C  C   . GLN E 5  33   ? -45.640 -55.630  42.297  1.00 76.52  ?  33   GLN E C   1 
ATOM   14189 O  O   . GLN E 5  33   ? -45.672 -56.842  42.535  1.00 76.53  ?  33   GLN E O   1 
ATOM   14190 C  CB  . GLN E 5  33   ? -43.847 -54.109  43.154  1.00 78.33  ?  33   GLN E CB  1 
ATOM   14191 C  CG  . GLN E 5  33   ? -43.494 -52.899  44.001  1.00 84.04  ?  33   GLN E CG  1 
ATOM   14192 C  CD  . GLN E 5  33   ? -42.042 -52.497  43.865  1.00 78.33  ?  33   GLN E CD  1 
ATOM   14193 O  OE1 . GLN E 5  33   ? -41.388 -52.828  42.877  1.00 73.67  ?  33   GLN E OE1 1 
ATOM   14194 N  NE2 . GLN E 5  33   ? -41.531 -51.772  44.854  1.00 81.09  ?  33   GLN E NE2 1 
ATOM   14195 N  N   . GLN E 5  34   ? -45.903 -55.101  41.098  1.00 68.92  ?  34   GLN E N   1 
ATOM   14196 C  CA  . GLN E 5  34   ? -46.357 -55.930  39.988  1.00 68.22  ?  34   GLN E CA  1 
ATOM   14197 C  C   . GLN E 5  34   ? -45.269 -56.879  39.505  1.00 75.37  ?  34   GLN E C   1 
ATOM   14198 O  O   . GLN E 5  34   ? -45.579 -57.930  38.932  1.00 70.73  ?  34   GLN E O   1 
ATOM   14199 C  CB  . GLN E 5  34   ? -46.830 -55.039  38.841  1.00 58.27  ?  34   GLN E CB  1 
ATOM   14200 C  CG  . GLN E 5  34   ? -47.890 -54.040  39.252  1.00 66.98  ?  34   GLN E CG  1 
ATOM   14201 C  CD  . GLN E 5  34   ? -47.334 -52.648  39.458  1.00 66.01  ?  34   GLN E CD  1 
ATOM   14202 O  OE1 . GLN E 5  34   ? -46.417 -52.223  38.758  1.00 67.98  ?  34   GLN E OE1 1 
ATOM   14203 N  NE2 . GLN E 5  34   ? -47.898 -51.923  40.414  1.00 68.87  ?  34   GLN E NE2 1 
ATOM   14204 N  N   . LYS E 5  35   ? -44.000 -56.533  39.718  1.00 80.86  ?  35   LYS E N   1 
ATOM   14205 C  CA  . LYS E 5  35   ? -42.923 -57.407  39.281  1.00 66.02  ?  35   LYS E CA  1 
ATOM   14206 C  C   . LYS E 5  35   ? -42.991 -58.738  40.021  1.00 72.44  ?  35   LYS E C   1 
ATOM   14207 O  O   . LYS E 5  35   ? -43.544 -58.844  41.119  1.00 75.05  ?  35   LYS E O   1 
ATOM   14208 C  CB  . LYS E 5  35   ? -41.559 -56.756  39.511  1.00 63.23  ?  35   LYS E CB  1 
ATOM   14209 C  CG  . LYS E 5  35   ? -41.217 -56.506  40.971  1.00 66.91  ?  35   LYS E CG  1 
ATOM   14210 C  CD  . LYS E 5  35   ? -39.879 -55.795  41.107  1.00 66.98  ?  35   LYS E CD  1 
ATOM   14211 C  CE  . LYS E 5  35   ? -39.451 -55.702  42.561  1.00 63.00  ?  35   LYS E CE  1 
ATOM   14212 N  NZ  . LYS E 5  35   ? -38.316 -54.760  42.754  1.00 61.00  ?  35   LYS E NZ  1 
ATOM   14213 N  N   . TYR E 5  36   ? -42.420 -59.764  39.401  1.00 71.62  ?  36   TYR E N   1 
ATOM   14214 C  CA  . TYR E 5  36   ? -42.434 -61.112  39.949  1.00 65.66  ?  36   TYR E CA  1 
ATOM   14215 C  C   . TYR E 5  36   ? -41.088 -61.396  40.604  1.00 68.94  ?  36   TYR E C   1 
ATOM   14216 O  O   . TYR E 5  36   ? -40.059 -61.439  39.922  1.00 70.80  ?  36   TYR E O   1 
ATOM   14217 C  CB  . TYR E 5  36   ? -42.733 -62.139  38.858  1.00 69.41  ?  36   TYR E CB  1 
ATOM   14218 C  CG  . TYR E 5  36   ? -44.207 -62.301  38.575  1.00 68.40  ?  36   TYR E CG  1 
ATOM   14219 C  CD1 . TYR E 5  36   ? -45.030 -62.994  39.452  1.00 74.86  ?  36   TYR E CD1 1 
ATOM   14220 C  CD2 . TYR E 5  36   ? -44.778 -61.756  37.433  1.00 63.94  ?  36   TYR E CD2 1 
ATOM   14221 C  CE1 . TYR E 5  36   ? -46.380 -63.141  39.200  1.00 79.13  ?  36   TYR E CE1 1 
ATOM   14222 C  CE2 . TYR E 5  36   ? -46.126 -61.898  37.171  1.00 67.43  ?  36   TYR E CE2 1 
ATOM   14223 C  CZ  . TYR E 5  36   ? -46.923 -62.591  38.058  1.00 77.80  ?  36   TYR E CZ  1 
ATOM   14224 O  OH  . TYR E 5  36   ? -48.267 -62.736  37.802  1.00 81.35  ?  36   TYR E OH  1 
ATOM   14225 N  N   . THR E 5  37   ? -41.099 -61.588  41.923  1.00 84.77  ?  37   THR E N   1 
ATOM   14226 C  CA  . THR E 5  37   ? -39.874 -61.886  42.654  1.00 82.75  ?  37   THR E CA  1 
ATOM   14227 C  C   . THR E 5  37   ? -39.438 -63.327  42.410  1.00 84.41  ?  37   THR E C   1 
ATOM   14228 O  O   . THR E 5  37   ? -39.893 -63.964  41.455  1.00 85.20  ?  37   THR E O   1 
ATOM   14229 C  CB  . THR E 5  37   ? -40.061 -61.623  44.151  1.00 90.06  ?  37   THR E CB  1 
ATOM   14230 O  OG1 . THR E 5  37   ? -40.818 -62.689  44.739  1.00 97.75  ?  37   THR E OG1 1 
ATOM   14231 C  CG2 . THR E 5  37   ? -40.784 -60.299  44.372  1.00 80.27  ?  37   THR E CG2 1 
ATOM   14232 N  N   . THR E 5  38   ? -38.561 -63.849  43.269  1.00 83.49  ?  38   THR E N   1 
ATOM   14233 C  CA  . THR E 5  38   ? -37.949 -65.151  43.015  1.00 90.20  ?  38   THR E CA  1 
ATOM   14234 C  C   . THR E 5  38   ? -38.987 -66.270  43.028  1.00 93.67  ?  38   THR E C   1 
ATOM   14235 O  O   . THR E 5  38   ? -39.133 -67.011  42.049  1.00 101.11 ?  38   THR E O   1 
ATOM   14236 C  CB  . THR E 5  38   ? -36.846 -65.419  44.040  1.00 85.19  ?  38   THR E CB  1 
ATOM   14237 O  OG1 . THR E 5  38   ? -35.896 -64.347  44.010  1.00 73.96  ?  38   THR E OG1 1 
ATOM   14238 C  CG2 . THR E 5  38   ? -36.135 -66.728  43.726  1.00 85.45  ?  38   THR E CG2 1 
ATOM   14239 N  N   . TYR E 5  39   ? -39.719 -66.410  44.134  1.00 48.47  ?  39   TYR E N   1 
ATOM   14240 C  CA  . TYR E 5  39   ? -40.689 -67.488  44.288  1.00 44.91  ?  39   TYR E CA  1 
ATOM   14241 C  C   . TYR E 5  39   ? -42.125 -66.979  44.361  1.00 47.47  ?  39   TYR E C   1 
ATOM   14242 O  O   . TYR E 5  39   ? -43.005 -67.691  44.855  1.00 50.30  ?  39   TYR E O   1 
ATOM   14243 C  CB  . TYR E 5  39   ? -40.361 -68.320  45.529  1.00 57.29  ?  39   TYR E CB  1 
ATOM   14244 C  CG  . TYR E 5  39   ? -39.299 -69.374  45.309  1.00 55.26  ?  39   TYR E CG  1 
ATOM   14245 C  CD1 . TYR E 5  39   ? -38.857 -69.686  44.030  1.00 58.42  ?  39   TYR E CD1 1 
ATOM   14246 C  CD2 . TYR E 5  39   ? -38.745 -70.063  46.380  1.00 59.98  ?  39   TYR E CD2 1 
ATOM   14247 C  CE1 . TYR E 5  39   ? -37.887 -70.652  43.825  1.00 66.76  ?  39   TYR E CE1 1 
ATOM   14248 C  CE2 . TYR E 5  39   ? -37.775 -71.030  46.185  1.00 60.36  ?  39   TYR E CE2 1 
ATOM   14249 C  CZ  . TYR E 5  39   ? -37.350 -71.321  44.905  1.00 61.22  ?  39   TYR E CZ  1 
ATOM   14250 O  OH  . TYR E 5  39   ? -36.386 -72.284  44.704  1.00 50.41  ?  39   TYR E OH  1 
ATOM   14251 N  N   . GLU E 5  40   ? -42.378 -65.768  43.876  1.00 65.16  ?  40   GLU E N   1 
ATOM   14252 C  CA  . GLU E 5  40   ? -43.719 -65.204  43.931  1.00 66.56  ?  40   GLU E CA  1 
ATOM   14253 C  C   . GLU E 5  40   ? -44.673 -66.056  43.099  1.00 70.02  ?  40   GLU E C   1 
ATOM   14254 O  O   . GLU E 5  40   ? -44.391 -66.324  41.924  1.00 83.57  ?  40   GLU E O   1 
ATOM   14255 C  CB  . GLU E 5  40   ? -43.708 -63.761  43.422  1.00 64.51  ?  40   GLU E CB  1 
ATOM   14256 C  CG  . GLU E 5  40   ? -45.054 -63.049  43.487  1.00 70.63  ?  40   GLU E CG  1 
ATOM   14257 C  CD  . GLU E 5  40   ? -44.931 -61.544  43.298  1.00 84.60  ?  40   GLU E CD  1 
ATOM   14258 O  OE1 . GLU E 5  40   ? -43.888 -60.975  43.683  1.00 79.61  ?  40   GLU E OE1 1 
ATOM   14259 O  OE2 . GLU E 5  40   ? -45.879 -60.927  42.764  1.00 89.61  -1 40   GLU E OE2 1 
ATOM   14260 N  N   . PRO E 5  41   ? -45.790 -66.511  43.663  1.00 55.70  ?  41   PRO E N   1 
ATOM   14261 C  CA  . PRO E 5  41   ? -46.731 -67.321  42.883  1.00 57.35  ?  41   PRO E CA  1 
ATOM   14262 C  C   . PRO E 5  41   ? -47.358 -66.517  41.755  1.00 62.64  ?  41   PRO E C   1 
ATOM   14263 O  O   . PRO E 5  41   ? -47.603 -65.315  41.876  1.00 63.92  ?  41   PRO E O   1 
ATOM   14264 C  CB  . PRO E 5  41   ? -47.781 -67.743  43.917  1.00 54.50  ?  41   PRO E CB  1 
ATOM   14265 C  CG  . PRO E 5  41   ? -47.682 -66.719  44.998  1.00 57.71  ?  41   PRO E CG  1 
ATOM   14266 C  CD  . PRO E 5  41   ? -46.239 -66.319  45.052  1.00 61.37  ?  41   PRO E CD  1 
ATOM   14267 N  N   . SER E 5  42   ? -47.616 -67.204  40.644  1.00 70.74  ?  42   SER E N   1 
ATOM   14268 C  CA  . SER E 5  42   ? -48.126 -66.579  39.433  1.00 80.84  ?  42   SER E CA  1 
ATOM   14269 C  C   . SER E 5  42   ? -49.366 -67.313  38.950  1.00 79.57  ?  42   SER E C   1 
ATOM   14270 O  O   . SER E 5  42   ? -49.420 -68.545  38.977  1.00 67.35  ?  42   SER E O   1 
ATOM   14271 C  CB  . SER E 5  42   ? -47.065 -66.571  38.325  1.00 82.17  ?  42   SER E CB  1 
ATOM   14272 O  OG  . SER E 5  42   ? -47.600 -66.079  37.109  1.00 79.94  ?  42   SER E OG  1 
ATOM   14273 N  N   . SER E 5  43   ? -50.360 -66.549  38.504  1.00 117.13 ?  43   SER E N   1 
ATOM   14274 C  CA  . SER E 5  43   ? -51.587 -67.106  37.952  1.00 121.04 ?  43   SER E CA  1 
ATOM   14275 C  C   . SER E 5  43   ? -51.568 -67.181  36.432  1.00 119.90 ?  43   SER E C   1 
ATOM   14276 O  O   . SER E 5  43   ? -52.535 -67.667  35.837  1.00 117.49 ?  43   SER E O   1 
ATOM   14277 C  CB  . SER E 5  43   ? -52.795 -66.285  38.415  1.00 127.71 ?  43   SER E CB  1 
ATOM   14278 O  OG  . SER E 5  43   ? -52.745 -64.969  37.892  1.00 134.12 ?  43   SER E OG  1 
ATOM   14279 N  N   . PHE E 5  44   ? -50.496 -66.712  35.791  1.00 99.27  ?  44   PHE E N   1 
ATOM   14280 C  CA  . PHE E 5  44   ? -50.400 -66.786  34.338  1.00 94.79  ?  44   PHE E CA  1 
ATOM   14281 C  C   . PHE E 5  44   ? -49.953 -68.164  33.866  1.00 85.32  ?  44   PHE E C   1 
ATOM   14282 O  O   . PHE E 5  44   ? -50.344 -68.597  32.777  1.00 84.66  ?  44   PHE E O   1 
ATOM   14283 C  CB  . PHE E 5  44   ? -49.436 -65.717  33.819  1.00 89.15  ?  44   PHE E CB  1 
ATOM   14284 C  CG  . PHE E 5  44   ? -49.269 -65.725  32.327  1.00 78.66  ?  44   PHE E CG  1 
ATOM   14285 C  CD1 . PHE E 5  44   ? -50.276 -65.255  31.500  1.00 78.12  ?  44   PHE E CD1 1 
ATOM   14286 C  CD2 . PHE E 5  44   ? -48.107 -66.208  31.750  1.00 76.32  ?  44   PHE E CD2 1 
ATOM   14287 C  CE1 . PHE E 5  44   ? -50.124 -65.262  30.127  1.00 75.52  ?  44   PHE E CE1 1 
ATOM   14288 C  CE2 . PHE E 5  44   ? -47.949 -66.218  30.378  1.00 75.70  ?  44   PHE E CE2 1 
ATOM   14289 C  CZ  . PHE E 5  44   ? -48.959 -65.744  29.566  1.00 75.33  ?  44   PHE E CZ  1 
ATOM   14290 N  N   . PHE E 5  45   ? -49.143 -68.857  34.659  1.00 70.85  ?  45   PHE E N   1 
ATOM   14291 C  CA  . PHE E 5  45   ? -48.693 -70.199  34.326  1.00 72.83  ?  45   PHE E CA  1 
ATOM   14292 C  C   . PHE E 5  45   ? -49.637 -71.243  34.916  1.00 79.01  ?  45   PHE E C   1 
ATOM   14293 O  O   . PHE E 5  45   ? -50.438 -70.962  35.810  1.00 83.90  ?  45   PHE E O   1 
ATOM   14294 C  CB  . PHE E 5  45   ? -47.265 -70.428  34.823  1.00 70.15  ?  45   PHE E CB  1 
ATOM   14295 C  CG  . PHE E 5  45   ? -46.244 -69.550  34.157  1.00 72.04  ?  45   PHE E CG  1 
ATOM   14296 C  CD1 . PHE E 5  45   ? -45.791 -69.839  32.881  1.00 70.29  ?  45   PHE E CD1 1 
ATOM   14297 C  CD2 . PHE E 5  45   ? -45.742 -68.432  34.803  1.00 79.05  ?  45   PHE E CD2 1 
ATOM   14298 C  CE1 . PHE E 5  45   ? -44.854 -69.034  32.262  1.00 67.30  ?  45   PHE E CE1 1 
ATOM   14299 C  CE2 . PHE E 5  45   ? -44.804 -67.622  34.190  1.00 74.29  ?  45   PHE E CE2 1 
ATOM   14300 C  CZ  . PHE E 5  45   ? -44.360 -67.924  32.918  1.00 67.27  ?  45   PHE E CZ  1 
ATOM   14301 N  N   . ALA E 5  46   ? -49.525 -72.468  34.399  1.00 65.12  ?  46   ALA E N   1 
ATOM   14302 C  CA  . ALA E 5  46   ? -50.466 -73.519  34.775  1.00 63.42  ?  46   ALA E CA  1 
ATOM   14303 C  C   . ALA E 5  46   ? -50.204 -74.022  36.190  1.00 65.61  ?  46   ALA E C   1 
ATOM   14304 O  O   . ALA E 5  46   ? -51.137 -74.169  36.989  1.00 66.46  ?  46   ALA E O   1 
ATOM   14305 C  CB  . ALA E 5  46   ? -50.392 -74.669  33.772  1.00 54.34  ?  46   ALA E CB  1 
ATOM   14306 N  N   . ASP E 5  47   ? -48.943 -74.293  36.520  1.00 97.55  ?  47   ASP E N   1 
ATOM   14307 C  CA  . ASP E 5  47   ? -48.586 -74.863  37.813  1.00 99.87  ?  47   ASP E CA  1 
ATOM   14308 C  C   . ASP E 5  47   ? -48.492 -73.824  38.930  1.00 99.59  ?  47   ASP E C   1 
ATOM   14309 O  O   . ASP E 5  47   ? -48.076 -74.171  40.041  1.00 91.25  ?  47   ASP E O   1 
ATOM   14310 C  CB  . ASP E 5  47   ? -47.266 -75.633  37.698  1.00 102.79 ?  47   ASP E CB  1 
ATOM   14311 C  CG  . ASP E 5  47   ? -46.117 -74.762  37.226  1.00 105.68 ?  47   ASP E CG  1 
ATOM   14312 O  OD1 . ASP E 5  47   ? -46.347 -73.575  36.915  1.00 106.93 ?  47   ASP E OD1 1 
ATOM   14313 O  OD2 . ASP E 5  47   ? -44.977 -75.269  37.167  1.00 105.82 -1 47   ASP E OD2 1 
ATOM   14314 N  N   . GLY E 5  48   ? -48.862 -72.574  38.669  1.00 92.60  ?  48   GLY E N   1 
ATOM   14315 C  CA  . GLY E 5  48   ? -48.869 -71.555  39.707  1.00 81.26  ?  48   GLY E CA  1 
ATOM   14316 C  C   . GLY E 5  48   ? -47.504 -71.170  40.235  1.00 73.75  ?  48   GLY E C   1 
ATOM   14317 O  O   . GLY E 5  48   ? -47.331 -71.033  41.452  1.00 81.97  ?  48   GLY E O   1 
ATOM   14318 N  N   . ARG E 5  49   ? -46.529 -70.984  39.348  1.00 77.90  ?  49   ARG E N   1 
ATOM   14319 C  CA  . ARG E 5  49   ? -45.170 -70.638  39.742  1.00 73.29  ?  49   ARG E CA  1 
ATOM   14320 C  C   . ARG E 5  49   ? -44.587 -69.663  38.732  1.00 77.37  ?  49   ARG E C   1 
ATOM   14321 O  O   . ARG E 5  49   ? -44.600 -69.935  37.528  1.00 85.06  ?  49   ARG E O   1 
ATOM   14322 C  CB  . ARG E 5  49   ? -44.285 -71.886  39.831  1.00 66.43  ?  49   ARG E CB  1 
ATOM   14323 C  CG  . ARG E 5  49   ? -44.044 -72.391  41.239  1.00 66.58  ?  49   ARG E CG  1 
ATOM   14324 C  CD  . ARG E 5  49   ? -42.867 -73.352  41.273  1.00 79.88  ?  49   ARG E CD  1 
ATOM   14325 N  NE  . ARG E 5  49   ? -43.017 -74.440  40.314  1.00 86.02  ?  49   ARG E NE  1 
ATOM   14326 C  CZ  . ARG E 5  49   ? -43.493 -75.642  40.609  1.00 80.17  ?  49   ARG E CZ  1 
ATOM   14327 N  NH1 . ARG E 5  49   ? -43.876 -75.951  41.837  1.00 83.32  ?  49   ARG E NH1 1 
ATOM   14328 N  NH2 . ARG E 5  49   ? -43.587 -76.557  39.649  1.00 83.93  ?  49   ARG E NH2 1 
ATOM   14329 N  N   . SER E 5  50   ? -44.075 -68.531  39.220  1.00 67.71  ?  50   SER E N   1 
ATOM   14330 C  CA  . SER E 5  50   ? -43.408 -67.591  38.327  1.00 72.20  ?  50   SER E CA  1 
ATOM   14331 C  C   . SER E 5  50   ? -42.023 -68.081  37.926  1.00 81.50  ?  50   SER E C   1 
ATOM   14332 O  O   . SER E 5  50   ? -41.572 -67.804  36.809  1.00 80.76  ?  50   SER E O   1 
ATOM   14333 C  CB  . SER E 5  50   ? -43.312 -66.211  38.979  1.00 64.24  ?  50   SER E CB  1 
ATOM   14334 O  OG  . SER E 5  50   ? -42.395 -66.216  40.058  1.00 63.99  ?  50   SER E OG  1 
ATOM   14335 N  N   . SER E 5  51   ? -41.340 -68.801  38.813  1.00 65.61  ?  51   SER E N   1 
ATOM   14336 C  CA  . SER E 5  51   ? -40.071 -69.415  38.454  1.00 58.22  ?  51   SER E CA  1 
ATOM   14337 C  C   . SER E 5  51   ? -40.306 -70.598  37.522  1.00 62.46  ?  51   SER E C   1 
ATOM   14338 O  O   . SER E 5  51   ? -41.306 -71.314  37.627  1.00 71.82  ?  51   SER E O   1 
ATOM   14339 C  CB  . SER E 5  51   ? -39.319 -69.864  39.706  1.00 55.19  ?  51   SER E CB  1 
ATOM   14340 O  OG  . SER E 5  51   ? -38.889 -68.746  40.463  1.00 52.58  ?  51   SER E OG  1 
ATOM   14341 N  N   . ARG E 5  52   ? -39.369 -70.801  36.601  1.00 64.81  ?  52   ARG E N   1 
ATOM   14342 C  CA  . ARG E 5  52   ? -39.585 -71.766  35.541  1.00 69.28  ?  52   ARG E CA  1 
ATOM   14343 C  C   . ARG E 5  52   ? -38.530 -72.865  35.577  1.00 63.72  ?  52   ARG E C   1 
ATOM   14344 O  O   . ARG E 5  52   ? -37.377 -72.615  35.943  1.00 58.01  ?  52   ARG E O   1 
ATOM   14345 C  CB  . ARG E 5  52   ? -39.563 -71.074  34.172  1.00 69.14  ?  52   ARG E CB  1 
ATOM   14346 C  CG  . ARG E 5  52   ? -40.713 -70.100  33.962  1.00 61.98  ?  52   ARG E CG  1 
ATOM   14347 C  CD  . ARG E 5  52   ? -41.978 -70.825  33.537  1.00 64.53  ?  52   ARG E CD  1 
ATOM   14348 N  NE  . ARG E 5  52   ? -42.765 -71.267  34.681  1.00 61.99  ?  52   ARG E NE  1 
ATOM   14349 C  CZ  . ARG E 5  52   ? -43.639 -72.263  34.646  1.00 78.78  ?  52   ARG E CZ  1 
ATOM   14350 N  NH1 . ARG E 5  52   ? -43.859 -72.951  33.537  1.00 79.29  ?  52   ARG E NH1 1 
ATOM   14351 N  NH2 . ARG E 5  52   ? -44.307 -72.579  35.751  1.00 89.30  ?  52   ARG E NH2 1 
ATOM   14352 N  N   . PRO E 5  53   ? -38.895 -74.092  35.212  1.00 64.85  ?  53   PRO E N   1 
ATOM   14353 C  CA  . PRO E 5  53   ? -37.909 -75.177  35.165  1.00 70.81  ?  53   PRO E CA  1 
ATOM   14354 C  C   . PRO E 5  53   ? -36.947 -75.001  33.999  1.00 67.33  ?  53   PRO E C   1 
ATOM   14355 O  O   . PRO E 5  53   ? -37.138 -74.174  33.106  1.00 68.00  ?  53   PRO E O   1 
ATOM   14356 C  CB  . PRO E 5  53   ? -38.769 -76.434  34.999  1.00 69.08  ?  53   PRO E CB  1 
ATOM   14357 C  CG  . PRO E 5  53   ? -40.023 -75.943  34.354  1.00 68.41  ?  53   PRO E CG  1 
ATOM   14358 C  CD  . PRO E 5  53   ? -40.256 -74.564  34.903  1.00 62.91  ?  53   PRO E CD  1 
ATOM   14359 N  N   . ASN E 5  54   ? -35.892 -75.810  34.019  1.00 83.62  ?  54   ASN E N   1 
ATOM   14360 C  CA  . ASN E 5  54   ? -34.850 -75.704  33.007  1.00 83.36  ?  54   ASN E CA  1 
ATOM   14361 C  C   . ASN E 5  54   ? -35.321 -76.278  31.677  1.00 82.81  ?  54   ASN E C   1 
ATOM   14362 O  O   . ASN E 5  54   ? -36.018 -77.295  31.630  1.00 86.06  ?  54   ASN E O   1 
ATOM   14363 C  CB  . ASN E 5  54   ? -33.587 -76.431  33.468  1.00 75.12  ?  54   ASN E CB  1 
ATOM   14364 C  CG  . ASN E 5  54   ? -32.655 -75.537  34.261  1.00 84.73  ?  54   ASN E CG  1 
ATOM   14365 O  OD1 . ASN E 5  54   ? -32.782 -74.313  34.241  1.00 92.95  ?  54   ASN E OD1 1 
ATOM   14366 N  ND2 . ASN E 5  54   ? -31.709 -76.147  34.965  1.00 89.48  ?  54   ASN E ND2 1 
ATOM   14367 N  N   . VAL E 5  55   ? -34.942 -75.612  30.594  1.00 80.53  ?  55   VAL E N   1 
ATOM   14368 C  CA  . VAL E 5  55   ? -35.172 -76.162  29.253  1.00 79.47  ?  55   VAL E CA  1 
ATOM   14369 C  C   . VAL E 5  55   ? -34.263 -77.373  29.062  1.00 79.99  ?  55   VAL E C   1 
ATOM   14370 O  O   . VAL E 5  55   ? -33.072 -77.304  29.411  1.00 82.19  ?  55   VAL E O   1 
ATOM   14371 C  CB  . VAL E 5  55   ? -34.910 -75.092  28.190  1.00 81.41  ?  55   VAL E CB  1 
ATOM   14372 C  CG1 . VAL E 5  55   ? -35.289 -75.590  26.802  1.00 85.57  ?  55   VAL E CG1 1 
ATOM   14373 C  CG2 . VAL E 5  55   ? -35.672 -73.819  28.527  1.00 86.20  ?  55   VAL E CG2 1 
ATOM   14374 N  N   . PRO E 5  56   ? -34.773 -78.503  28.533  1.00 71.77  ?  56   PRO E N   1 
ATOM   14375 C  CA  . PRO E 5  56   ? -33.995 -79.753  28.531  1.00 77.98  ?  56   PRO E CA  1 
ATOM   14376 C  C   . PRO E 5  56   ? -32.566 -79.641  28.013  1.00 80.74  ?  56   PRO E C   1 
ATOM   14377 O  O   . PRO E 5  56   ? -31.618 -79.899  28.761  1.00 77.16  ?  56   PRO E O   1 
ATOM   14378 C  CB  . PRO E 5  56   ? -34.835 -80.669  27.632  1.00 81.87  ?  56   PRO E CB  1 
ATOM   14379 C  CG  . PRO E 5  56   ? -36.229 -80.204  27.858  1.00 78.50  ?  56   PRO E CG  1 
ATOM   14380 C  CD  . PRO E 5  56   ? -36.141 -78.709  28.021  1.00 72.51  ?  56   PRO E CD  1 
ATOM   14381 N  N   . GLY E 5  57   ? -32.392 -79.260  26.750  1.00 71.40  ?  57   GLY E N   1 
ATOM   14382 C  CA  . GLY E 5  57   ? -31.068 -79.260  26.157  1.00 68.69  ?  57   GLY E CA  1 
ATOM   14383 C  C   . GLY E 5  57   ? -30.356 -77.923  26.173  1.00 73.49  ?  57   GLY E C   1 
ATOM   14384 O  O   . GLY E 5  57   ? -29.473 -77.679  25.344  1.00 78.88  ?  57   GLY E O   1 
ATOM   14385 N  N   . THR E 5  58   ? -30.712 -77.053  27.113  1.00 94.17  ?  58   THR E N   1 
ATOM   14386 C  CA  . THR E 5  58   ? -30.170 -75.702  27.176  1.00 84.17  ?  58   THR E CA  1 
ATOM   14387 C  C   . THR E 5  58   ? -29.090 -75.615  28.246  1.00 88.57  ?  58   THR E C   1 
ATOM   14388 O  O   . THR E 5  58   ? -29.292 -76.061  29.380  1.00 97.04  ?  58   THR E O   1 
ATOM   14389 C  CB  . THR E 5  58   ? -31.279 -74.687  27.460  1.00 87.60  ?  58   THR E CB  1 
ATOM   14390 O  OG1 . THR E 5  58   ? -32.241 -74.729  26.400  1.00 93.97  ?  58   THR E OG1 1 
ATOM   14391 C  CG2 . THR E 5  58   ? -30.707 -73.283  27.558  1.00 101.36 ?  58   THR E CG2 1 
ATOM   14392 N  N   . THR E 5  59   ? -27.945 -75.040  27.880  1.00 81.50  ?  59   THR E N   1 
ATOM   14393 C  CA  . THR E 5  59   ? -26.820 -74.832  28.775  1.00 80.52  ?  59   THR E CA  1 
ATOM   14394 C  C   . THR E 5  59   ? -26.482 -73.347  28.857  1.00 84.31  ?  59   THR E C   1 
ATOM   14395 O  O   . THR E 5  59   ? -26.695 -72.605  27.893  1.00 88.31  ?  59   THR E O   1 
ATOM   14396 C  CB  . THR E 5  59   ? -25.582 -75.608  28.306  1.00 97.55  ?  59   THR E CB  1 
ATOM   14397 O  OG1 . THR E 5  59   ? -25.183 -75.139  27.013  1.00 100.18 ?  59   THR E OG1 1 
ATOM   14398 C  CG2 . THR E 5  59   ? -25.885 -77.099  28.230  1.00 100.24 ?  59   THR E CG2 1 
ATOM   14399 N  N   . PRO E 5  60   ? -25.955 -72.882  29.995  1.00 67.78  ?  60   PRO E N   1 
ATOM   14400 C  CA  . PRO E 5  60   ? -25.650 -71.450  30.138  1.00 63.51  ?  60   PRO E CA  1 
ATOM   14401 C  C   . PRO E 5  60   ? -24.517 -70.976  29.240  1.00 59.72  ?  60   PRO E C   1 
ATOM   14402 O  O   . PRO E 5  60   ? -23.985 -71.740  28.428  1.00 57.41  ?  60   PRO E O   1 
ATOM   14403 C  CB  . PRO E 5  60   ? -25.275 -71.317  31.621  1.00 53.99  ?  60   PRO E CB  1 
ATOM   14404 C  CG  . PRO E 5  60   ? -25.864 -72.523  32.280  1.00 58.44  ?  60   PRO E CG  1 
ATOM   14405 C  CD  . PRO E 5  60   ? -25.777 -73.611  31.261  1.00 68.30  ?  60   PRO E CD  1 
ATOM   14406 N  N   . PHE E 5  61   ? -24.141 -69.708  29.391  1.00 58.90  ?  61   PHE E N   1 
ATOM   14407 C  CA  . PHE E 5  61   ? -23.097 -69.111  28.570  1.00 55.07  ?  61   PHE E CA  1 
ATOM   14408 C  C   . PHE E 5  61   ? -21.713 -69.486  29.083  1.00 52.57  ?  61   PHE E C   1 
ATOM   14409 O  O   . PHE E 5  61   ? -21.445 -69.435  30.287  1.00 56.50  ?  61   PHE E O   1 
ATOM   14410 C  CB  . PHE E 5  61   ? -23.248 -67.589  28.549  1.00 53.08  ?  61   PHE E CB  1 
ATOM   14411 C  CG  . PHE E 5  61   ? -22.234 -66.892  27.688  1.00 59.31  ?  61   PHE E CG  1 
ATOM   14412 C  CD1 . PHE E 5  61   ? -22.084 -67.232  26.354  1.00 60.62  ?  61   PHE E CD1 1 
ATOM   14413 C  CD2 . PHE E 5  61   ? -21.432 -65.891  28.214  1.00 47.74  ?  61   PHE E CD2 1 
ATOM   14414 C  CE1 . PHE E 5  61   ? -21.151 -66.590  25.561  1.00 61.69  ?  61   PHE E CE1 1 
ATOM   14415 C  CE2 . PHE E 5  61   ? -20.499 -65.246  27.427  1.00 48.17  ?  61   PHE E CE2 1 
ATOM   14416 C  CZ  . PHE E 5  61   ? -20.358 -65.595  26.100  1.00 57.56  ?  61   PHE E CZ  1 
ATOM   14417 N  N   . GLU E 5  62   ? -20.834 -69.861  28.151  1.00 67.68  ?  62   GLU E N   1 
ATOM   14418 C  CA  . GLU E 5  62   ? -19.445 -70.220  28.450  1.00 67.86  ?  62   GLU E CA  1 
ATOM   14419 C  C   . GLU E 5  62   ? -19.353 -71.376  29.443  1.00 71.63  ?  62   GLU E C   1 
ATOM   14420 O  O   . GLU E 5  62   ? -18.393 -71.473  30.211  1.00 73.69  ?  62   GLU E O   1 
ATOM   14421 C  CB  . GLU E 5  62   ? -18.655 -69.009  28.956  1.00 69.66  ?  62   GLU E CB  1 
ATOM   14422 C  CG  . GLU E 5  62   ? -18.054 -68.165  27.840  1.00 89.98  ?  62   GLU E CG  1 
ATOM   14423 C  CD  . GLU E 5  62   ? -17.291 -66.960  28.357  1.00 95.20  ?  62   GLU E CD  1 
ATOM   14424 O  OE1 . GLU E 5  62   ? -17.337 -66.702  29.578  1.00 104.31 ?  62   GLU E OE1 1 
ATOM   14425 O  OE2 . GLU E 5  62   ? -16.644 -66.272  27.539  1.00 92.21  -1 62   GLU E OE2 1 
ATOM   14426 N  N   . VAL E 5  63   ? -20.347 -72.259  29.430  1.00 70.00  ?  63   VAL E N   1 
ATOM   14427 C  CA  . VAL E 5  63   ? -20.365 -73.457  30.264  1.00 70.28  ?  63   VAL E CA  1 
ATOM   14428 C  C   . VAL E 5  63   ? -20.476 -74.639  29.311  1.00 72.48  ?  63   VAL E C   1 
ATOM   14429 O  O   . VAL E 5  63   ? -21.566 -74.948  28.813  1.00 79.93  ?  63   VAL E O   1 
ATOM   14430 C  CB  . VAL E 5  63   ? -21.512 -73.445  31.280  1.00 68.67  ?  63   VAL E CB  1 
ATOM   14431 C  CG1 . VAL E 5  63   ? -21.560 -74.760  32.046  1.00 71.60  ?  63   VAL E CG1 1 
ATOM   14432 C  CG2 . VAL E 5  63   ? -21.363 -72.272  32.235  1.00 65.46  ?  63   VAL E CG2 1 
ATOM   14433 N  N   . VAL E 5  64   ? -19.354 -75.303  29.051  1.00 48.67  ?  64   VAL E N   1 
ATOM   14434 C  CA  . VAL E 5  64   ? -19.282 -76.386  28.077  1.00 56.68  ?  64   VAL E CA  1 
ATOM   14435 C  C   . VAL E 5  64   ? -19.429 -77.720  28.800  1.00 63.89  ?  64   VAL E C   1 
ATOM   14436 O  O   . VAL E 5  64   ? -18.820 -77.938  29.856  1.00 66.72  ?  64   VAL E O   1 
ATOM   14437 C  CB  . VAL E 5  64   ? -17.972 -76.316  27.270  1.00 55.76  ?  64   VAL E CB  1 
ATOM   14438 C  CG1 . VAL E 5  64   ? -16.754 -76.412  28.186  1.00 55.13  ?  64   VAL E CG1 1 
ATOM   14439 C  CG2 . VAL E 5  64   ? -17.941 -77.398  26.202  1.00 68.77  ?  64   VAL E CG2 1 
ATOM   14440 N  N   . LYS E 5  65   ? -20.256 -78.608  28.244  1.00 86.41  ?  65   LYS E N   1 
ATOM   14441 C  CA  . LYS E 5  65   ? -20.507 -79.928  28.810  1.00 95.14  ?  65   LYS E CA  1 
ATOM   14442 C  C   . LYS E 5  65   ? -19.731 -81.025  28.088  1.00 99.45  ?  65   LYS E C   1 
ATOM   14443 O  O   . LYS E 5  65   ? -20.229 -82.148  27.948  1.00 101.62 ?  65   LYS E O   1 
ATOM   14444 C  CB  . LYS E 5  65   ? -22.004 -80.241  28.781  1.00 108.27 ?  65   LYS E CB  1 
ATOM   14445 C  CG  . LYS E 5  65   ? -22.696 -80.192  30.136  1.00 103.12 ?  65   LYS E CG  1 
ATOM   14446 C  CD  . LYS E 5  65   ? -22.703 -78.788  30.712  1.00 99.47  ?  65   LYS E CD  1 
ATOM   14447 C  CE  . LYS E 5  65   ? -23.775 -78.644  31.778  1.00 105.83 ?  65   LYS E CE  1 
ATOM   14448 N  NZ  . LYS E 5  65   ? -24.029 -77.220  32.124  1.00 111.39 ?  65   LYS E NZ  1 
ATOM   14449 N  N   . THR E 5  66   ? -18.514 -80.726  27.629  1.00 87.37  ?  66   THR E N   1 
ATOM   14450 C  CA  . THR E 5  66   ? -17.766 -81.692  26.829  1.00 96.34  ?  66   THR E CA  1 
ATOM   14451 C  C   . THR E 5  66   ? -17.226 -82.828  27.689  1.00 104.62 ?  66   THR E C   1 
ATOM   14452 O  O   . THR E 5  66   ? -17.415 -84.007  27.367  1.00 113.23 ?  66   THR E O   1 
ATOM   14453 C  CB  . THR E 5  66   ? -16.629 -80.990  26.084  1.00 99.74  ?  66   THR E CB  1 
ATOM   14454 O  OG1 . THR E 5  66   ? -17.163 -80.265  24.969  1.00 94.64  ?  66   THR E OG1 1 
ATOM   14455 C  CG2 . THR E 5  66   ? -15.613 -82.006  25.576  1.00 106.09 ?  66   THR E CG2 1 
ATOM   14456 N  N   . ASP E 5  67   ? -16.549 -82.494  28.787  1.00 119.36 ?  67   ASP E N   1 
ATOM   14457 C  CA  . ASP E 5  67   ? -15.952 -83.517  29.636  1.00 121.15 ?  67   ASP E CA  1 
ATOM   14458 C  C   . ASP E 5  67   ? -17.031 -84.385  30.270  1.00 120.28 ?  67   ASP E C   1 
ATOM   14459 O  O   . ASP E 5  67   ? -17.984 -83.877  30.869  1.00 119.59 ?  67   ASP E O   1 
ATOM   14460 C  CB  . ASP E 5  67   ? -15.089 -82.869  30.719  1.00 125.62 ?  67   ASP E CB  1 
ATOM   14461 C  CG  . ASP E 5  67   ? -14.323 -83.888  31.541  1.00 125.26 ?  67   ASP E CG  1 
ATOM   14462 O  OD1 . ASP E 5  67   ? -14.027 -84.980  31.011  1.00 116.57 ?  67   ASP E OD1 1 
ATOM   14463 O  OD2 . ASP E 5  67   ? -14.016 -83.596  32.716  1.00 123.57 -1 67   ASP E OD2 1 
ATOM   14464 N  N   . GLU E 5  68   ? -16.877 -85.704  30.134  1.00 106.86 ?  68   GLU E N   1 
ATOM   14465 C  CA  . GLU E 5  68   ? -17.871 -86.628  30.666  1.00 112.19 ?  68   GLU E CA  1 
ATOM   14466 C  C   . GLU E 5  68   ? -17.634 -86.925  32.142  1.00 117.52 ?  68   GLU E C   1 
ATOM   14467 O  O   . GLU E 5  68   ? -18.589 -86.968  32.926  1.00 115.56 ?  68   GLU E O   1 
ATOM   14468 C  CB  . GLU E 5  68   ? -17.872 -87.923  29.853  1.00 114.60 ?  68   GLU E CB  1 
ATOM   14469 C  CG  . GLU E 5  68   ? -18.428 -87.764  28.447  1.00 116.35 ?  68   GLU E CG  1 
ATOM   14470 C  CD  . GLU E 5  68   ? -19.832 -87.193  28.440  1.00 113.88 ?  68   GLU E CD  1 
ATOM   14471 O  OE1 . GLU E 5  68   ? -20.664 -87.650  29.251  1.00 123.43 ?  68   GLU E OE1 1 
ATOM   14472 O  OE2 . GLU E 5  68   ? -20.103 -86.282  27.628  1.00 112.60 -1 68   GLU E OE2 1 
ATOM   14473 N  N   . PHE E 5  69   ? -16.375 -87.133  32.538  1.00 149.12 ?  69   PHE E N   1 
ATOM   14474 C  CA  . PHE E 5  69   ? -16.075 -87.392  33.943  1.00 146.83 ?  69   PHE E CA  1 
ATOM   14475 C  C   . PHE E 5  69   ? -16.522 -86.243  34.835  1.00 137.99 ?  69   PHE E C   1 
ATOM   14476 O  O   . PHE E 5  69   ? -16.905 -86.465  35.989  1.00 138.19 ?  69   PHE E O   1 
ATOM   14477 C  CB  . PHE E 5  69   ? -14.582 -87.653  34.128  1.00 155.10 ?  69   PHE E CB  1 
ATOM   14478 C  CG  . PHE E 5  69   ? -14.168 -89.050  33.787  1.00 162.55 ?  69   PHE E CG  1 
ATOM   14479 C  CD1 . PHE E 5  69   ? -14.337 -90.074  34.702  1.00 151.96 ?  69   PHE E CD1 1 
ATOM   14480 C  CD2 . PHE E 5  69   ? -13.609 -89.342  32.555  1.00 178.23 ?  69   PHE E CD2 1 
ATOM   14481 C  CE1 . PHE E 5  69   ? -13.961 -91.363  34.395  1.00 171.26 ?  69   PHE E CE1 1 
ATOM   14482 C  CE2 . PHE E 5  69   ? -13.227 -90.632  32.242  1.00 184.01 ?  69   PHE E CE2 1 
ATOM   14483 C  CZ  . PHE E 5  69   ? -13.404 -91.644  33.164  1.00 184.12 ?  69   PHE E CZ  1 
ATOM   14484 N  N   . LEU E 5  70   ? -16.483 -85.014  34.321  1.00 117.51 ?  70   LEU E N   1 
ATOM   14485 C  CA  . LEU E 5  70   ? -16.973 -83.875  35.085  1.00 117.38 ?  70   LEU E CA  1 
ATOM   14486 C  C   . LEU E 5  70   ? -18.484 -83.911  35.270  1.00 122.32 ?  70   LEU E C   1 
ATOM   14487 O  O   . LEU E 5  70   ? -19.006 -83.197  36.131  1.00 127.65 ?  70   LEU E O   1 
ATOM   14488 C  CB  . LEU E 5  70   ? -16.565 -82.570  34.398  1.00 117.98 ?  70   LEU E CB  1 
ATOM   14489 C  CG  . LEU E 5  70   ? -16.476 -81.325  35.282  1.00 112.23 ?  70   LEU E CG  1 
ATOM   14490 C  CD1 . LEU E 5  70   ? -15.605 -81.596  36.499  1.00 105.00 ?  70   LEU E CD1 1 
ATOM   14491 C  CD2 . LEU E 5  70   ? -15.952 -80.134  34.492  1.00 115.34 ?  70   LEU E CD2 1 
ATOM   14492 N  N   . TYR E 5  71   ? -19.197 -84.726  34.489  1.00 92.87  ?  71   TYR E N   1 
ATOM   14493 C  CA  . TYR E 5  71   ? -20.651 -84.765  34.545  1.00 90.43  ?  71   TYR E CA  1 
ATOM   14494 C  C   . TYR E 5  71   ? -21.237 -86.168  34.628  1.00 91.05  ?  71   TYR E C   1 
ATOM   14495 O  O   . TYR E 5  71   ? -22.447 -86.291  34.849  1.00 96.49  ?  71   TYR E O   1 
ATOM   14496 C  CB  . TYR E 5  71   ? -21.251 -84.044  33.328  1.00 79.43  ?  71   TYR E CB  1 
ATOM   14497 C  CG  . TYR E 5  71   ? -20.979 -82.556  33.324  1.00 80.56  ?  71   TYR E CG  1 
ATOM   14498 C  CD1 . TYR E 5  71   ? -21.752 -81.688  34.083  1.00 84.14  ?  71   TYR E CD1 1 
ATOM   14499 C  CD2 . TYR E 5  71   ? -19.939 -82.023  32.574  1.00 82.15  ?  71   TYR E CD2 1 
ATOM   14500 C  CE1 . TYR E 5  71   ? -21.504 -80.327  34.087  1.00 88.81  ?  71   TYR E CE1 1 
ATOM   14501 C  CE2 . TYR E 5  71   ? -19.683 -80.664  32.572  1.00 89.90  ?  71   TYR E CE2 1 
ATOM   14502 C  CZ  . TYR E 5  71   ? -20.468 -79.821  33.330  1.00 89.87  ?  71   TYR E CZ  1 
ATOM   14503 O  OH  . TYR E 5  71   ? -20.216 -78.468  33.331  1.00 74.61  ?  71   TYR E OH  1 
ATOM   14504 N  N   . THR E 5  72   ? -20.437 -87.217  34.458  1.00 116.97 ?  72   THR E N   1 
ATOM   14505 C  CA  . THR E 5  72   ? -20.922 -88.580  34.629  1.00 125.03 ?  72   THR E CA  1 
ATOM   14506 C  C   . THR E 5  72   ? -19.739 -89.484  34.945  1.00 132.13 ?  72   THR E C   1 
ATOM   14507 O  O   . THR E 5  72   ? -18.615 -89.241  34.498  1.00 134.49 ?  72   THR E O   1 
ATOM   14508 C  CB  . THR E 5  72   ? -21.675 -89.082  33.388  1.00 130.34 ?  72   THR E CB  1 
ATOM   14509 O  OG1 . THR E 5  72   ? -22.310 -90.332  33.685  1.00 139.36 ?  72   THR E OG1 1 
ATOM   14510 C  CG2 . THR E 5  72   ? -20.730 -89.264  32.207  1.00 129.17 ?  72   THR E CG2 1 
ATOM   14511 N  N   . GLY E 5  73   ? -20.003 -90.521  35.733  1.00 107.69 ?  73   GLY E N   1 
ATOM   14512 C  CA  . GLY E 5  73   ? -18.965 -91.444  36.131  1.00 111.63 ?  73   GLY E CA  1 
ATOM   14513 C  C   . GLY E 5  73   ? -18.660 -92.544  35.145  1.00 124.00 ?  73   GLY E C   1 
ATOM   14514 O  O   . GLY E 5  73   ? -17.868 -93.437  35.452  1.00 130.92 ?  73   GLY E O   1 
ATOM   14515 N  N   . LEU E 5  74   ? -19.258 -92.511  33.959  1.00 85.74  ?  74   LEU E N   1 
ATOM   14516 C  CA  . LEU E 5  74   ? -19.104 -93.578  32.981  1.00 91.38  ?  74   LEU E CA  1 
ATOM   14517 C  C   . LEU E 5  74   ? -18.171 -93.124  31.867  1.00 93.34  ?  74   LEU E C   1 
ATOM   14518 O  O   . LEU E 5  74   ? -18.326 -92.021  31.333  1.00 101.63 ?  74   LEU E O   1 
ATOM   14519 C  CB  . LEU E 5  74   ? -20.464 -93.987  32.409  1.00 99.36  ?  74   LEU E CB  1 
ATOM   14520 C  CG  . LEU E 5  74   ? -21.463 -94.531  33.435  1.00 88.57  ?  74   LEU E CG  1 
ATOM   14521 C  CD1 . LEU E 5  74   ? -22.819 -94.800  32.796  1.00 88.89  ?  74   LEU E CD1 1 
ATOM   14522 C  CD2 . LEU E 5  74   ? -20.923 -95.781  34.120  1.00 87.23  ?  74   LEU E CD2 1 
ATOM   14523 N  N   . ILE E 5  75   ? -17.200 -93.971  31.526  1.00 122.24 ?  75   ILE E N   1 
ATOM   14524 C  CA  . ILE E 5  75   ? -16.277 -93.686  30.433  1.00 129.89 ?  75   ILE E CA  1 
ATOM   14525 C  C   . ILE E 5  75   ? -16.719 -94.470  29.204  1.00 136.52 ?  75   ILE E C   1 
ATOM   14526 O  O   . ILE E 5  75   ? -16.454 -94.066  28.067  1.00 143.39 ?  75   ILE E O   1 
ATOM   14527 C  CB  . ILE E 5  75   ? -14.820 -94.014  30.822  1.00 126.81 ?  75   ILE E CB  1 
ATOM   14528 C  CG1 . ILE E 5  75   ? -13.835 -93.276  29.912  1.00 132.83 ?  75   ILE E CG1 1 
ATOM   14529 C  CG2 . ILE E 5  75   ? -14.562 -95.514  30.775  1.00 127.66 ?  75   ILE E CG2 1 
ATOM   14530 C  CD1 . ILE E 5  75   ? -12.379 -93.542  30.247  1.00 131.47 ?  75   ILE E CD1 1 
ATOM   14531 N  N   . ASP E 5  76   ? -17.413 -95.595  29.432  1.00 147.35 ?  76   ASP E N   1 
ATOM   14532 C  CA  . ASP E 5  76   ? -17.927 -96.419  28.342  1.00 150.58 ?  76   ASP E CA  1 
ATOM   14533 C  C   . ASP E 5  76   ? -19.169 -97.192  28.770  1.00 146.28 ?  76   ASP E C   1 
ATOM   14534 O  O   . ASP E 5  76   ? -19.471 -98.235  28.178  1.00 152.73 ?  76   ASP E O   1 
ATOM   14535 C  CB  . ASP E 5  76   ? -16.863 -97.409  27.843  1.00 154.15 ?  76   ASP E CB  1 
ATOM   14536 C  CG  . ASP E 5  76   ? -15.942 -96.805  26.802  1.00 163.91 ?  76   ASP E CG  1 
ATOM   14537 O  OD1 . ASP E 5  76   ? -16.404 -95.945  26.023  1.00 165.51 ?  76   ASP E OD1 1 
ATOM   14538 O  OD2 . ASP E 5  76   ? -14.756 -97.194  26.760  1.00 167.46 -1 76   ASP E OD2 1 
ATOM   14539 N  N   . GLY E 5  77   ? -19.892 -96.709  29.776  1.00 100.92 ?  77   GLY E N   1 
ATOM   14540 C  CA  . GLY E 5  77   ? -20.977 -97.447  30.379  1.00 103.93 ?  77   GLY E CA  1 
ATOM   14541 C  C   . GLY E 5  77   ? -20.596 -98.216  31.624  1.00 106.98 ?  77   GLY E C   1 
ATOM   14542 O  O   . GLY E 5  77   ? -21.455 -98.897  32.196  1.00 103.91 ?  77   GLY E O   1 
ATOM   14543 N  N   . GLN E 5  78   ? -19.340 -98.131  32.057  1.00 159.54 ?  78   GLN E N   1 
ATOM   14544 C  CA  . GLN E 5  78   ? -18.843 -98.841  33.226  1.00 160.60 ?  78   GLN E CA  1 
ATOM   14545 C  C   . GLN E 5  78   ? -18.065 -97.877  34.111  1.00 153.95 ?  78   GLN E C   1 
ATOM   14546 O  O   . GLN E 5  78   ? -17.714 -96.766  33.703  1.00 151.93 ?  78   GLN E O   1 
ATOM   14547 C  CB  . GLN E 5  78   ? -17.955 -100.028 32.824  1.00 162.43 ?  78   GLN E CB  1 
ATOM   14548 C  CG  . GLN E 5  78   ? -18.589 -100.971 31.814  1.00 170.50 ?  78   GLN E CG  1 
ATOM   14549 C  CD  . GLN E 5  78   ? -17.695 -102.146 31.471  1.00 177.72 ?  78   GLN E CD  1 
ATOM   14550 O  OE1 . GLN E 5  78   ? -16.856 -102.556 32.272  1.00 180.61 ?  78   GLN E OE1 1 
ATOM   14551 N  NE2 . GLN E 5  78   ? -17.872 -102.695 30.274  1.00 172.71 ?  78   GLN E NE2 1 
ATOM   14552 N  N   . GLU E 5  79   ? -17.797 -98.317  35.336  1.00 128.18 ?  79   GLU E N   1 
ATOM   14553 C  CA  . GLU E 5  79   ? -17.041 -97.522  36.289  1.00 122.17 ?  79   GLU E CA  1 
ATOM   14554 C  C   . GLU E 5  79   ? -15.545 -97.614  35.991  1.00 121.11 ?  79   GLU E C   1 
ATOM   14555 O  O   . GLU E 5  79   ? -15.084 -98.492  35.256  1.00 129.37 ?  79   GLU E O   1 
ATOM   14556 C  CB  . GLU E 5  79   ? -17.333 -97.984  37.716  1.00 122.06 ?  79   GLU E CB  1 
ATOM   14557 C  CG  . GLU E 5  79   ? -18.543 -97.317  38.359  1.00 119.19 ?  79   GLU E CG  1 
ATOM   14558 C  CD  . GLU E 5  79   ? -19.851 -98.020  38.036  1.00 117.53 ?  79   GLU E CD  1 
ATOM   14559 O  OE1 . GLU E 5  79   ? -19.966 -98.603  36.938  1.00 124.12 ?  79   GLU E OE1 1 
ATOM   14560 O  OE2 . GLU E 5  79   ? -20.767 -97.989  38.886  1.00 110.47 -1 79   GLU E OE2 1 
ATOM   14561 N  N   . VAL E 5  80   ? -14.784 -96.691  36.576  1.00 98.73  ?  80   VAL E N   1 
ATOM   14562 C  CA  . VAL E 5  80   ? -13.373 -96.543  36.241  1.00 99.42  ?  80   VAL E CA  1 
ATOM   14563 C  C   . VAL E 5  80   ? -12.447 -96.647  37.446  1.00 100.40 ?  80   VAL E C   1 
ATOM   14564 O  O   . VAL E 5  80   ? -11.262 -96.974  37.261  1.00 106.50 ?  80   VAL E O   1 
ATOM   14565 C  CB  . VAL E 5  80   ? -13.118 -95.214  35.499  1.00 102.15 ?  80   VAL E CB  1 
ATOM   14566 C  CG1 . VAL E 5  80   ? -14.077 -95.058  34.334  1.00 114.83 ?  80   VAL E CG1 1 
ATOM   14567 C  CG2 . VAL E 5  80   ? -13.240 -94.040  36.458  1.00 104.69 ?  80   VAL E CG2 1 
ATOM   14568 N  N   . ASP E 5  81   ? -12.922 -96.384  38.663  1.00 112.99 ?  81   ASP E N   1 
ATOM   14569 C  CA  . ASP E 5  81   ? -12.066 -96.280  39.845  1.00 114.77 ?  81   ASP E CA  1 
ATOM   14570 C  C   . ASP E 5  81   ? -10.960 -95.250  39.621  1.00 115.73 ?  81   ASP E C   1 
ATOM   14571 O  O   . ASP E 5  81   ? -9.768  -95.530  39.767  1.00 108.41 ?  81   ASP E O   1 
ATOM   14572 C  CB  . ASP E 5  81   ? -11.484 -97.641  40.234  1.00 120.35 ?  81   ASP E CB  1 
ATOM   14573 C  CG  . ASP E 5  81   ? -11.220 -97.757  41.724  1.00 121.76 ?  81   ASP E CG  1 
ATOM   14574 O  OD1 . ASP E 5  81   ? -10.507 -96.888  42.270  1.00 111.86 ?  81   ASP E OD1 1 
ATOM   14575 O  OD2 . ASP E 5  81   ? -11.727 -98.714  42.348  1.00 122.11 -1 81   ASP E OD2 1 
ATOM   14576 N  N   . ALA E 5  82   ? -11.375 -94.041  39.250  1.00 100.48 ?  82   ALA E N   1 
ATOM   14577 C  CA  . ALA E 5  82   ? -10.458 -92.931  39.036  1.00 94.59  ?  82   ALA E CA  1 
ATOM   14578 C  C   . ALA E 5  82   ? -11.207 -91.630  39.288  1.00 88.91  ?  82   ALA E C   1 
ATOM   14579 O  O   . ALA E 5  82   ? -12.418 -91.621  39.512  1.00 86.64  ?  82   ALA E O   1 
ATOM   14580 C  CB  . ALA E 5  82   ? -9.859  -92.958  37.626  1.00 95.47  ?  82   ALA E CB  1 
ATOM   14581 N  N   . MET E 5  83   ? -10.471 -90.523  39.241  1.00 123.19 ?  83   MET E N   1 
ATOM   14582 C  CA  . MET E 5  83   ? -11.037 -89.221  39.549  1.00 129.02 ?  83   MET E CA  1 
ATOM   14583 C  C   . MET E 5  83   ? -10.594 -88.219  38.492  1.00 137.81 ?  83   MET E C   1 
ATOM   14584 O  O   . MET E 5  83   ? -9.416  -88.199  38.118  1.00 146.02 ?  83   MET E O   1 
ATOM   14585 C  CB  . MET E 5  83   ? -10.598 -88.762  40.948  1.00 122.08 ?  83   MET E CB  1 
ATOM   14586 C  CG  . MET E 5  83   ? -11.321 -87.538  41.472  1.00 121.66 ?  83   MET E CG  1 
ATOM   14587 S  SD  . MET E 5  83   ? -10.876 -87.179  43.178  1.00 140.00 ?  83   MET E SD  1 
ATOM   14588 C  CE  . MET E 5  83   ? -11.835 -85.698  43.466  1.00 116.52 ?  83   MET E CE  1 
ATOM   14589 N  N   . PRO E 5  84   ? -11.509 -87.387  37.981  1.00 104.10 ?  84   PRO E N   1 
ATOM   14590 C  CA  . PRO E 5  84   ? -11.155 -86.510  36.848  1.00 93.70  ?  84   PRO E CA  1 
ATOM   14591 C  C   . PRO E 5  84   ? -10.019 -85.541  37.135  1.00 95.23  ?  84   PRO E C   1 
ATOM   14592 O  O   . PRO E 5  84   ? -9.224  -85.253  36.232  1.00 100.01 ?  84   PRO E O   1 
ATOM   14593 C  CB  . PRO E 5  84   ? -12.469 -85.767  36.560  1.00 90.40  ?  84   PRO E CB  1 
ATOM   14594 C  CG  . PRO E 5  84   ? -13.274 -85.903  37.814  1.00 96.13  ?  84   PRO E CG  1 
ATOM   14595 C  CD  . PRO E 5  84   ? -12.922 -87.245  38.366  1.00 96.78  ?  84   PRO E CD  1 
ATOM   14596 N  N   . PHE E 5  85   ? -9.915  -85.025  38.355  1.00 86.14  ?  85   PHE E N   1 
ATOM   14597 C  CA  . PHE E 5  85   ? -8.852  -84.098  38.704  1.00 87.10  ?  85   PHE E CA  1 
ATOM   14598 C  C   . PHE E 5  85   ? -8.125  -84.584  39.949  1.00 95.53  ?  85   PHE E C   1 
ATOM   14599 O  O   . PHE E 5  85   ? -8.696  -85.325  40.756  1.00 100.84 ?  85   PHE E O   1 
ATOM   14600 C  CB  . PHE E 5  85   ? -9.403  -82.681  38.936  1.00 80.45  ?  85   PHE E CB  1 
ATOM   14601 C  CG  . PHE E 5  85   ? -10.760 -82.653  39.575  1.00 80.24  ?  85   PHE E CG  1 
ATOM   14602 C  CD1 . PHE E 5  85   ? -10.898 -82.767  40.947  1.00 84.86  ?  85   PHE E CD1 1 
ATOM   14603 C  CD2 . PHE E 5  85   ? -11.899 -82.511  38.801  1.00 81.75  ?  85   PHE E CD2 1 
ATOM   14604 C  CE1 . PHE E 5  85   ? -12.148 -82.739  41.536  1.00 82.82  ?  85   PHE E CE1 1 
ATOM   14605 C  CE2 . PHE E 5  85   ? -13.151 -82.484  39.383  1.00 83.66  ?  85   PHE E CE2 1 
ATOM   14606 C  CZ  . PHE E 5  85   ? -13.276 -82.598  40.752  1.00 80.72  ?  85   PHE E CZ  1 
ATOM   14607 N  N   . PRO E 5  86   ? -6.859  -84.199  40.120  1.00 94.87  ?  86   PRO E N   1 
ATOM   14608 C  CA  . PRO E 5  86   ? -6.100  -84.659  41.289  1.00 94.38  ?  86   PRO E CA  1 
ATOM   14609 C  C   . PRO E 5  86   ? -6.709  -84.172  42.596  1.00 99.06  ?  86   PRO E C   1 
ATOM   14610 O  O   . PRO E 5  86   ? -7.425  -83.170  42.652  1.00 95.52  ?  86   PRO E O   1 
ATOM   14611 C  CB  . PRO E 5  86   ? -4.705  -84.059  41.068  1.00 84.80  ?  86   PRO E CB  1 
ATOM   14612 C  CG  . PRO E 5  86   ? -4.630  -83.808  39.599  1.00 92.42  ?  86   PRO E CG  1 
ATOM   14613 C  CD  . PRO E 5  86   ? -6.018  -83.427  39.189  1.00 90.94  ?  86   PRO E CD  1 
ATOM   14614 N  N   . VAL E 5  87   ? -6.405  -84.907  43.662  1.00 108.92 ?  87   VAL E N   1 
ATOM   14615 C  CA  . VAL E 5  87   ? -6.938  -84.610  44.986  1.00 102.87 ?  87   VAL E CA  1 
ATOM   14616 C  C   . VAL E 5  87   ? -6.114  -83.503  45.628  1.00 96.81  ?  87   VAL E C   1 
ATOM   14617 O  O   . VAL E 5  87   ? -4.878  -83.512  45.572  1.00 103.95 ?  87   VAL E O   1 
ATOM   14618 C  CB  . VAL E 5  87   ? -6.945  -85.881  45.855  1.00 92.05  ?  87   VAL E CB  1 
ATOM   14619 C  CG1 . VAL E 5  87   ? -7.402  -85.562  47.271  1.00 93.39  ?  87   VAL E CG1 1 
ATOM   14620 C  CG2 . VAL E 5  87   ? -7.831  -86.947  45.229  1.00 87.55  ?  87   VAL E CG2 1 
ATOM   14621 N  N   . THR E 5  88   ? -6.799  -82.541  46.242  1.00 101.35 ?  88   THR E N   1 
ATOM   14622 C  CA  . THR E 5  88   ? -6.157  -81.440  46.943  1.00 107.23 ?  88   THR E CA  1 
ATOM   14623 C  C   . THR E 5  88   ? -6.679  -81.392  48.372  1.00 109.57 ?  88   THR E C   1 
ATOM   14624 O  O   . THR E 5  88   ? -7.773  -81.878  48.670  1.00 111.53 ?  88   THR E O   1 
ATOM   14625 C  CB  . THR E 5  88   ? -6.415  -80.097  46.240  1.00 112.63 ?  88   THR E CB  1 
ATOM   14626 O  OG1 . THR E 5  88   ? -6.368  -80.283  44.821  1.00 120.34 ?  88   THR E OG1 1 
ATOM   14627 C  CG2 . THR E 5  88   ? -5.360  -79.072  46.632  1.00 111.32 ?  88   THR E CG2 1 
ATOM   14628 N  N   . LYS E 5  89   ? -5.875  -80.808  49.265  1.00 119.25 ?  89   LYS E N   1 
ATOM   14629 C  CA  . LYS E 5  89   ? -6.304  -80.663  50.652  1.00 115.76 ?  89   LYS E CA  1 
ATOM   14630 C  C   . LYS E 5  89   ? -7.534  -79.770  50.759  1.00 118.54 ?  89   LYS E C   1 
ATOM   14631 O  O   . LYS E 5  89   ? -8.459  -80.067  51.524  1.00 123.30 ?  89   LYS E O   1 
ATOM   14632 C  CB  . LYS E 5  89   ? -5.163  -80.110  51.505  1.00 125.27 ?  89   LYS E CB  1 
ATOM   14633 C  CG  . LYS E 5  89   ? -5.414  -80.212  53.000  1.00 133.92 ?  89   LYS E CG  1 
ATOM   14634 C  CD  . LYS E 5  89   ? -5.760  -81.636  53.407  1.00 128.41 ?  89   LYS E CD  1 
ATOM   14635 C  CE  . LYS E 5  89   ? -6.193  -81.704  54.863  1.00 130.07 ?  89   LYS E CE  1 
ATOM   14636 N  NZ  . LYS E 5  89   ? -5.121  -81.240  55.787  1.00 140.35 ?  89   LYS E NZ  1 
ATOM   14637 N  N   . ASP E 5  90   ? -7.562  -78.669  50.004  1.00 106.26 ?  90   ASP E N   1 
ATOM   14638 C  CA  . ASP E 5  90   ? -8.760  -77.835  49.966  1.00 107.33 ?  90   ASP E CA  1 
ATOM   14639 C  C   . ASP E 5  90   ? -9.932  -78.595  49.359  1.00 95.40  ?  90   ASP E C   1 
ATOM   14640 O  O   . ASP E 5  90   ? -11.084 -78.411  49.771  1.00 86.04  ?  90   ASP E O   1 
ATOM   14641 C  CB  . ASP E 5  90   ? -8.487  -76.553  49.179  1.00 104.20 ?  90   ASP E CB  1 
ATOM   14642 C  CG  . ASP E 5  90   ? -7.485  -75.649  49.866  1.00 110.37 ?  90   ASP E CG  1 
ATOM   14643 O  OD1 . ASP E 5  90   ? -7.177  -75.891  51.052  1.00 110.18 ?  90   ASP E OD1 1 
ATOM   14644 O  OD2 . ASP E 5  90   ? -7.007  -74.693  49.220  1.00 124.59 -1 90   ASP E OD2 1 
ATOM   14645 N  N   . LEU E 5  91   ? -9.654  -79.455  48.378  1.00 82.34  ?  91   LEU E N   1 
ATOM   14646 C  CA  . LEU E 5  91   ? -10.708 -80.269  47.783  1.00 86.60  ?  91   LEU E CA  1 
ATOM   14647 C  C   . LEU E 5  91   ? -11.266 -81.269  48.789  1.00 85.19  ?  91   LEU E C   1 
ATOM   14648 O  O   . LEU E 5  91   ? -12.478 -81.508  48.829  1.00 83.96  ?  91   LEU E O   1 
ATOM   14649 C  CB  . LEU E 5  91   ? -10.171 -80.986  46.545  1.00 89.27  ?  91   LEU E CB  1 
ATOM   14650 C  CG  . LEU E 5  91   ? -11.147 -81.825  45.720  1.00 85.80  ?  91   LEU E CG  1 
ATOM   14651 C  CD1 . LEU E 5  91   ? -12.161 -80.939  45.015  1.00 78.34  ?  91   LEU E CD1 1 
ATOM   14652 C  CD2 . LEU E 5  91   ? -10.382 -82.669  44.719  1.00 92.26  ?  91   LEU E CD2 1 
ATOM   14653 N  N   . LEU E 5  92   ? -10.396 -81.860  49.611  1.00 70.78  ?  92   LEU E N   1 
ATOM   14654 C  CA  . LEU E 5  92   ? -10.864 -82.779  50.643  1.00 70.60  ?  92   LEU E CA  1 
ATOM   14655 C  C   . LEU E 5  92   ? -11.629 -82.038  51.733  1.00 72.03  ?  92   LEU E C   1 
ATOM   14656 O  O   . LEU E 5  92   ? -12.605 -82.563  52.281  1.00 71.09  ?  92   LEU E O   1 
ATOM   14657 C  CB  . LEU E 5  92   ? -9.682  -83.548  51.234  1.00 77.98  ?  92   LEU E CB  1 
ATOM   14658 C  CG  . LEU E 5  92   ? -9.213  -84.773  50.444  1.00 74.63  ?  92   LEU E CG  1 
ATOM   14659 C  CD1 . LEU E 5  92   ? -7.981  -85.397  51.080  1.00 75.29  ?  92   LEU E CD1 1 
ATOM   14660 C  CD2 . LEU E 5  92   ? -10.331 -85.796  50.333  1.00 59.09  ?  92   LEU E CD2 1 
ATOM   14661 N  N   . LEU E 5  93   ? -11.202 -80.815  52.058  1.00 85.79  ?  93   LEU E N   1 
ATOM   14662 C  CA  . LEU E 5  93   ? -11.935 -80.013  53.032  1.00 81.02  ?  93   LEU E CA  1 
ATOM   14663 C  C   . LEU E 5  93   ? -13.321 -79.650  52.514  1.00 79.07  ?  93   LEU E C   1 
ATOM   14664 O  O   . LEU E 5  93   ? -14.305 -79.711  53.261  1.00 85.99  ?  93   LEU E O   1 
ATOM   14665 C  CB  . LEU E 5  93   ? -11.143 -78.753  53.377  1.00 85.57  ?  93   LEU E CB  1 
ATOM   14666 C  CG  . LEU E 5  93   ? -9.931  -78.935  54.291  1.00 83.96  ?  93   LEU E CG  1 
ATOM   14667 C  CD1 . LEU E 5  93   ? -9.139  -77.642  54.386  1.00 94.36  ?  93   LEU E CD1 1 
ATOM   14668 C  CD2 . LEU E 5  93   ? -10.372 -79.393  55.670  1.00 98.94  ?  93   LEU E CD2 1 
ATOM   14669 N  N   . ARG E 5  94   ? -13.418 -79.267  51.238  1.00 67.12  ?  94   ARG E N   1 
ATOM   14670 C  CA  . ARG E 5  94   ? -14.722 -78.978  50.651  1.00 65.83  ?  94   ARG E CA  1 
ATOM   14671 C  C   . ARG E 5  94   ? -15.597 -80.224  50.618  1.00 75.70  ?  94   ARG E C   1 
ATOM   14672 O  O   . ARG E 5  94   ? -16.810 -80.147  50.846  1.00 79.39  ?  94   ARG E O   1 
ATOM   14673 C  CB  . ARG E 5  94   ? -14.548 -78.404  49.244  1.00 72.34  ?  94   ARG E CB  1 
ATOM   14674 C  CG  . ARG E 5  94   ? -15.849 -78.240  48.477  1.00 81.50  ?  94   ARG E CG  1 
ATOM   14675 C  CD  . ARG E 5  94   ? -16.694 -77.115  49.049  1.00 84.24  ?  94   ARG E CD  1 
ATOM   14676 N  NE  . ARG E 5  94   ? -17.371 -76.355  48.006  1.00 81.26  ?  94   ARG E NE  1 
ATOM   14677 C  CZ  . ARG E 5  94   ? -17.989 -75.199  48.205  1.00 94.64  ?  94   ARG E CZ  1 
ATOM   14678 N  NH1 . ARG E 5  94   ? -18.029 -74.634  49.402  1.00 95.72  ?  94   ARG E NH1 1 
ATOM   14679 N  NH2 . ARG E 5  94   ? -18.584 -74.596  47.180  1.00 90.92  ?  94   ARG E NH2 1 
ATOM   14680 N  N   . GLY E 5  95   ? -14.998 -81.384  50.341  1.00 102.65 ?  95   GLY E N   1 
ATOM   14681 C  CA  . GLY E 5  95   ? -15.761 -82.621  50.365  1.00 98.07  ?  95   GLY E CA  1 
ATOM   14682 C  C   . GLY E 5  95   ? -16.248 -82.976  51.755  1.00 96.25  ?  95   GLY E C   1 
ATOM   14683 O  O   . GLY E 5  95   ? -17.363 -83.478  51.922  1.00 98.16  ?  95   GLY E O   1 
ATOM   14684 N  N   . GLN E 5  96   ? -15.421 -82.721  52.771  1.00 80.51  ?  96   GLN E N   1 
ATOM   14685 C  CA  . GLN E 5  96   ? -15.849 -82.947  54.147  1.00 83.91  ?  96   GLN E CA  1 
ATOM   14686 C  C   . GLN E 5  96   ? -17.007 -82.031  54.518  1.00 88.44  ?  96   GLN E C   1 
ATOM   14687 O  O   . GLN E 5  96   ? -17.947 -82.450  55.204  1.00 90.60  ?  96   GLN E O   1 
ATOM   14688 C  CB  . GLN E 5  96   ? -14.674 -82.739  55.102  1.00 85.03  ?  96   GLN E CB  1 
ATOM   14689 C  CG  . GLN E 5  96   ? -15.029 -82.909  56.569  1.00 85.48  ?  96   GLN E CG  1 
ATOM   14690 C  CD  . GLN E 5  96   ? -13.854 -82.647  57.485  1.00 86.33  ?  96   GLN E CD  1 
ATOM   14691 O  OE1 . GLN E 5  96   ? -12.923 -81.927  57.128  1.00 86.57  ?  96   GLN E OE1 1 
ATOM   14692 N  NE2 . GLN E 5  96   ? -13.887 -83.239  58.673  1.00 92.56  ?  96   GLN E NE2 1 
ATOM   14693 N  N   . LEU E 5  97   ? -16.955 -80.774  54.069  1.00 70.84  ?  97   LEU E N   1 
ATOM   14694 C  CA  . LEU E 5  97   ? -18.034 -79.835  54.354  1.00 66.94  ?  97   LEU E CA  1 
ATOM   14695 C  C   . LEU E 5  97   ? -19.333 -80.274  53.692  1.00 61.52  ?  97   LEU E C   1 
ATOM   14696 O  O   . LEU E 5  97   ? -20.389 -80.316  54.334  1.00 60.13  ?  97   LEU E O   1 
ATOM   14697 C  CB  . LEU E 5  97   ? -17.642 -78.432  53.891  1.00 68.93  ?  97   LEU E CB  1 
ATOM   14698 C  CG  . LEU E 5  97   ? -18.687 -77.341  54.128  1.00 65.45  ?  97   LEU E CG  1 
ATOM   14699 C  CD1 . LEU E 5  97   ? -18.868 -77.084  55.617  1.00 68.47  ?  97   LEU E CD1 1 
ATOM   14700 C  CD2 . LEU E 5  97   ? -18.310 -76.060  53.399  1.00 63.67  ?  97   LEU E CD2 1 
ATOM   14701 N  N   . LYS E 5  98   ? -19.275 -80.605  52.400  1.00 51.01  ?  98   LYS E N   1 
ATOM   14702 C  CA  . LYS E 5  98   ? -20.476 -81.038  51.694  1.00 55.43  ?  98   LYS E CA  1 
ATOM   14703 C  C   . LYS E 5  98   ? -20.983 -82.376  52.218  1.00 63.39  ?  98   LYS E C   1 
ATOM   14704 O  O   . LYS E 5  98   ? -22.193 -82.631  52.190  1.00 61.33  ?  98   LYS E O   1 
ATOM   14705 C  CB  . LYS E 5  98   ? -20.199 -81.122  50.194  1.00 57.76  ?  98   LYS E CB  1 
ATOM   14706 C  CG  . LYS E 5  98   ? -20.029 -79.774  49.513  1.00 62.96  ?  98   LYS E CG  1 
ATOM   14707 C  CD  . LYS E 5  98   ? -21.108 -78.791  49.938  1.00 56.14  ?  98   LYS E CD  1 
ATOM   14708 C  CE  . LYS E 5  98   ? -20.833 -77.405  49.378  1.00 56.16  ?  98   LYS E CE  1 
ATOM   14709 N  NZ  . LYS E 5  98   ? -21.715 -76.371  49.985  1.00 67.35  ?  98   LYS E NZ  1 
ATOM   14710 N  N   . TYR E 5  99   ? -20.082 -83.238  52.694  1.00 69.06  ?  99   TYR E N   1 
ATOM   14711 C  CA  . TYR E 5  99   ? -20.510 -84.492  53.304  1.00 63.33  ?  99   TYR E CA  1 
ATOM   14712 C  C   . TYR E 5  99   ? -21.225 -84.238  54.624  1.00 64.66  ?  99   TYR E C   1 
ATOM   14713 O  O   . TYR E 5  99   ? -22.268 -84.841  54.899  1.00 69.86  ?  99   TYR E O   1 
ATOM   14714 C  CB  . TYR E 5  99   ? -19.304 -85.414  53.510  1.00 65.71  ?  99   TYR E CB  1 
ATOM   14715 C  CG  . TYR E 5  99   ? -19.617 -86.748  54.165  1.00 75.39  ?  99   TYR E CG  1 
ATOM   14716 C  CD1 . TYR E 5  99   ? -19.668 -86.877  55.550  1.00 74.51  ?  99   TYR E CD1 1 
ATOM   14717 C  CD2 . TYR E 5  99   ? -19.843 -87.881  53.396  1.00 69.02  ?  99   TYR E CD2 1 
ATOM   14718 C  CE1 . TYR E 5  99   ? -19.951 -88.093  56.146  1.00 69.38  ?  99   TYR E CE1 1 
ATOM   14719 C  CE2 . TYR E 5  99   ? -20.126 -89.100  53.983  1.00 69.56  ?  99   TYR E CE2 1 
ATOM   14720 C  CZ  . TYR E 5  99   ? -20.177 -89.201  55.357  1.00 73.79  ?  99   TYR E CZ  1 
ATOM   14721 O  OH  . TYR E 5  99   ? -20.457 -90.415  55.942  1.00 79.08  ?  99   TYR E OH  1 
ATOM   14722 N  N   . ASN E 5  100  ? -20.680 -83.345  55.453  1.00 51.45  ?  100  ASN E N   1 
ATOM   14723 C  CA  . ASN E 5  100  ? -21.295 -83.063  56.744  1.00 47.76  ?  100  ASN E CA  1 
ATOM   14724 C  C   . ASN E 5  100  ? -22.645 -82.373  56.592  1.00 53.70  ?  100  ASN E C   1 
ATOM   14725 O  O   . ASN E 5  100  ? -23.522 -82.536  57.449  1.00 60.43  ?  100  ASN E O   1 
ATOM   14726 C  CB  . ASN E 5  100  ? -20.351 -82.216  57.597  1.00 49.78  ?  100  ASN E CB  1 
ATOM   14727 C  CG  . ASN E 5  100  ? -19.289 -83.048  58.292  1.00 54.36  ?  100  ASN E CG  1 
ATOM   14728 O  OD1 . ASN E 5  100  ? -19.067 -84.209  57.947  1.00 53.14  ?  100  ASN E OD1 1 
ATOM   14729 N  ND2 . ASN E 5  100  ? -18.618 -82.451  59.270  1.00 61.34  ?  100  ASN E ND2 1 
ATOM   14730 N  N   . ILE E 5  101  ? -22.839 -81.613  55.516  1.00 85.27  ?  101  ILE E N   1 
ATOM   14731 C  CA  . ILE E 5  101  ? -24.103 -80.909  55.316  1.00 80.77  ?  101  ILE E CA  1 
ATOM   14732 C  C   . ILE E 5  101  ? -25.166 -81.853  54.764  1.00 88.21  ?  101  ILE E C   1 
ATOM   14733 O  O   . ILE E 5  101  ? -26.238 -82.024  55.356  1.00 91.39  ?  101  ILE E O   1 
ATOM   14734 C  CB  . ILE E 5  101  ? -23.903 -79.691  54.397  1.00 72.33  ?  101  ILE E CB  1 
ATOM   14735 C  CG1 . ILE E 5  101  ? -22.974 -78.669  55.056  1.00 69.94  ?  101  ILE E CG1 1 
ATOM   14736 C  CG2 . ILE E 5  101  ? -25.242 -79.056  54.054  1.00 77.65  ?  101  ILE E CG2 1 
ATOM   14737 C  CD1 . ILE E 5  101  ? -22.497 -77.585  54.116  1.00 82.45  ?  101  ILE E CD1 1 
ATOM   14738 N  N   . TYR E 5  102  ? -24.881 -82.483  53.626  1.00 81.25  ?  102  TYR E N   1 
ATOM   14739 C  CA  . TYR E 5  102  ? -25.869 -83.278  52.905  1.00 77.40  ?  102  TYR E CA  1 
ATOM   14740 C  C   . TYR E 5  102  ? -25.801 -84.766  53.215  1.00 78.74  ?  102  TYR E C   1 
ATOM   14741 O  O   . TYR E 5  102  ? -26.839 -85.434  53.241  1.00 85.11  ?  102  TYR E O   1 
ATOM   14742 C  CB  . TYR E 5  102  ? -25.703 -83.082  51.394  1.00 80.70  ?  102  TYR E CB  1 
ATOM   14743 C  CG  . TYR E 5  102  ? -25.907 -81.660  50.925  1.00 81.07  ?  102  TYR E CG  1 
ATOM   14744 C  CD1 . TYR E 5  102  ? -27.174 -81.191  50.606  1.00 77.87  ?  102  TYR E CD1 1 
ATOM   14745 C  CD2 . TYR E 5  102  ? -24.833 -80.791  50.788  1.00 78.23  ?  102  TYR E CD2 1 
ATOM   14746 C  CE1 . TYR E 5  102  ? -27.368 -79.893  50.173  1.00 76.15  ?  102  TYR E CE1 1 
ATOM   14747 C  CE2 . TYR E 5  102  ? -25.016 -79.492  50.354  1.00 80.10  ?  102  TYR E CE2 1 
ATOM   14748 C  CZ  . TYR E 5  102  ? -26.286 -79.049  50.048  1.00 81.82  ?  102  TYR E CZ  1 
ATOM   14749 O  OH  . TYR E 5  102  ? -26.476 -77.756  49.615  1.00 86.48  ?  102  TYR E OH  1 
ATOM   14750 N  N   . CYS E 5  103  ? -24.607 -85.303  53.450  1.00 81.33  ?  103  CYS E N   1 
ATOM   14751 C  CA  . CYS E 5  103  ? -24.415 -86.745  53.505  1.00 83.29  ?  103  CYS E CA  1 
ATOM   14752 C  C   . CYS E 5  103  ? -24.344 -87.300  54.919  1.00 88.74  ?  103  CYS E C   1 
ATOM   14753 O  O   . CYS E 5  103  ? -24.757 -88.443  55.142  1.00 82.47  ?  103  CYS E O   1 
ATOM   14754 C  CB  . CYS E 5  103  ? -23.133 -87.125  52.757  1.00 84.99  ?  103  CYS E CB  1 
ATOM   14755 S  SG  . CYS E 5  103  ? -23.099 -86.588  51.032  1.00 88.26  ?  103  CYS E SG  1 
ATOM   14756 N  N   . ALA E 5  104  ? -23.829 -86.524  55.876  1.00 97.80  ?  104  ALA E N   1 
ATOM   14757 C  CA  . ALA E 5  104  ? -23.633 -87.042  57.226  1.00 93.37  ?  104  ALA E CA  1 
ATOM   14758 C  C   . ALA E 5  104  ? -24.963 -87.380  57.883  1.00 97.61  ?  104  ALA E C   1 
ATOM   14759 O  O   . ALA E 5  104  ? -25.114 -88.445  58.494  1.00 101.43 ?  104  ALA E O   1 
ATOM   14760 C  CB  . ALA E 5  104  ? -22.860 -86.031  58.071  1.00 93.66  ?  104  ALA E CB  1 
ATOM   14761 N  N   . VAL E 5  105  ? -25.943 -86.479  57.777  1.00 79.03  ?  105  VAL E N   1 
ATOM   14762 C  CA  . VAL E 5  105  ? -27.266 -86.783  58.303  1.00 83.90  ?  105  VAL E CA  1 
ATOM   14763 C  C   . VAL E 5  105  ? -27.857 -87.952  57.524  1.00 83.70  ?  105  VAL E C   1 
ATOM   14764 O  O   . VAL E 5  105  ? -27.537 -88.173  56.349  1.00 84.37  ?  105  VAL E O   1 
ATOM   14765 C  CB  . VAL E 5  105  ? -28.185 -85.551  58.242  1.00 76.38  ?  105  VAL E CB  1 
ATOM   14766 C  CG1 . VAL E 5  105  ? -27.549 -84.388  58.974  1.00 71.87  ?  105  VAL E CG1 1 
ATOM   14767 C  CG2 . VAL E 5  105  ? -28.486 -85.179  56.801  1.00 81.05  ?  105  VAL E CG2 1 
ATOM   14768 N  N   . CYS E 5  106  ? -28.692 -88.740  58.200  1.00 103.13 ?  106  CYS E N   1 
ATOM   14769 C  CA  . CYS E 5  106  ? -29.471 -89.823  57.606  1.00 115.25 ?  106  CYS E CA  1 
ATOM   14770 C  C   . CYS E 5  106  ? -28.594 -90.971  57.108  1.00 111.20 ?  106  CYS E C   1 
ATOM   14771 O  O   . CYS E 5  106  ? -29.121 -91.947  56.553  1.00 121.70 ?  106  CYS E O   1 
ATOM   14772 C  CB  . CYS E 5  106  ? -30.368 -89.301  56.469  1.00 112.99 ?  106  CYS E CB  1 
ATOM   14773 S  SG  . CYS E 5  106  ? -31.444 -90.485  55.589  1.00 107.56 ?  106  CYS E SG  1 
ATOM   14774 N  N   . HIS E 5  107  ? -27.279 -90.922  57.323  1.00 110.87 ?  107  HIS E N   1 
ATOM   14775 C  CA  . HIS E 5  107  ? -26.444 -91.864  56.595  1.00 116.28 ?  107  HIS E CA  1 
ATOM   14776 C  C   . HIS E 5  107  ? -25.119 -92.060  57.323  1.00 111.99 ?  107  HIS E C   1 
ATOM   14777 O  O   . HIS E 5  107  ? -24.318 -92.922  56.953  1.00 117.18 ?  107  HIS E O   1 
ATOM   14778 C  CB  . HIS E 5  107  ? -26.281 -91.332  55.162  1.00 114.50 ?  107  HIS E CB  1 
ATOM   14779 C  CG  . HIS E 5  107  ? -25.932 -92.366  54.139  1.00 111.54 ?  107  HIS E CG  1 
ATOM   14780 N  ND1 . HIS E 5  107  ? -26.905 -93.124  53.527  1.00 122.69 ?  107  HIS E ND1 1 
ATOM   14781 C  CD2 . HIS E 5  107  ? -24.770 -92.669  53.509  1.00 110.48 ?  107  HIS E CD2 1 
ATOM   14782 C  CE1 . HIS E 5  107  ? -26.348 -93.914  52.631  1.00 123.40 ?  107  HIS E CE1 1 
ATOM   14783 N  NE2 . HIS E 5  107  ? -25.057 -93.645  52.583  1.00 122.00 ?  107  HIS E NE2 1 
ATOM   14784 N  N   . GLY E 5  108  ? -24.891 -91.271  58.369  1.00 97.39  ?  108  GLY E N   1 
ATOM   14785 C  CA  . GLY E 5  108  ? -23.750 -91.468  59.276  1.00 97.81  ?  108  GLY E CA  1 
ATOM   14786 C  C   . GLY E 5  108  ? -22.774 -90.307  59.291  1.00 98.17  ?  108  GLY E C   1 
ATOM   14787 O  O   . GLY E 5  108  ? -22.345 -89.801  58.254  1.00 101.95 ?  108  GLY E O   1 
ATOM   14788 N  N   . GLU E 5  109  ? -22.404 -89.886  60.504  1.00 86.85  ?  109  GLU E N   1 
ATOM   14789 C  CA  . GLU E 5  109  ? -21.422 -88.817  60.661  1.00 75.69  ?  109  GLU E CA  1 
ATOM   14790 C  C   . GLU E 5  109  ? -20.009 -89.303  60.362  1.00 76.12  ?  109  GLU E C   1 
ATOM   14791 O  O   . GLU E 5  109  ? -19.237 -88.601  59.700  1.00 69.94  ?  109  GLU E O   1 
ATOM   14792 C  CB  . GLU E 5  109  ? -21.492 -88.240  62.077  1.00 87.39  ?  109  GLU E CB  1 
ATOM   14793 C  CG  . GLU E 5  109  ? -20.510 -87.101  62.356  1.00 92.38  ?  109  GLU E CG  1 
ATOM   14794 C  CD  . GLU E 5  109  ? -20.821 -85.839  61.571  1.00 95.93  ?  109  GLU E CD  1 
ATOM   14795 O  OE1 . GLU E 5  109  ? -22.001 -85.630  61.216  1.00 100.45 ?  109  GLU E OE1 1 
ATOM   14796 O  OE2 . GLU E 5  109  ? -19.883 -85.055  61.310  1.00 89.31  -1 109  GLU E OE2 1 
ATOM   14797 N  N   . ALA E 5  110  ? -19.649 -90.488  60.850  1.00 114.67 ?  110  ALA E N   1 
ATOM   14798 C  CA  . ALA E 5  110  ? -18.341 -91.074  60.594  1.00 107.02 ?  110  ALA E CA  1 
ATOM   14799 C  C   . ALA E 5  110  ? -18.367 -92.101  59.471  1.00 100.53 ?  110  ALA E C   1 
ATOM   14800 O  O   . ALA E 5  110  ? -17.319 -92.664  59.140  1.00 99.08  ?  110  ALA E O   1 
ATOM   14801 C  CB  . ALA E 5  110  ? -17.789 -91.718  61.869  1.00 98.25  ?  110  ALA E CB  1 
ATOM   14802 N  N   . GLY E 5  111  ? -19.532 -92.360  58.885  1.00 65.45  ?  111  GLY E N   1 
ATOM   14803 C  CA  . GLY E 5  111  ? -19.656 -93.310  57.801  1.00 64.30  ?  111  GLY E CA  1 
ATOM   14804 C  C   . GLY E 5  111  ? -20.121 -94.696  58.187  1.00 69.41  ?  111  GLY E C   1 
ATOM   14805 O  O   . GLY E 5  111  ? -20.090 -95.596  57.340  1.00 74.83  ?  111  GLY E O   1 
ATOM   14806 N  N   . TYR E 5  112  ? -20.551 -94.901  59.431  1.00 79.81  ?  112  TYR E N   1 
ATOM   14807 C  CA  . TYR E 5  112  ? -20.991 -96.213  59.885  1.00 79.60  ?  112  TYR E CA  1 
ATOM   14808 C  C   . TYR E 5  112  ? -22.483 -96.447  59.683  1.00 82.79  ?  112  TYR E C   1 
ATOM   14809 O  O   . TYR E 5  112  ? -22.950 -97.573  59.893  1.00 82.93  ?  112  TYR E O   1 
ATOM   14810 C  CB  . TYR E 5  112  ? -20.639 -96.403  61.365  1.00 82.65  ?  112  TYR E CB  1 
ATOM   14811 C  CG  . TYR E 5  112  ? -19.199 -96.801  61.602  1.00 75.62  ?  112  TYR E CG  1 
ATOM   14812 C  CD1 . TYR E 5  112  ? -18.793 -98.123  61.474  1.00 70.01  ?  112  TYR E CD1 1 
ATOM   14813 C  CD2 . TYR E 5  112  ? -18.243 -95.855  61.948  1.00 77.87  ?  112  TYR E CD2 1 
ATOM   14814 C  CE1 . TYR E 5  112  ? -17.478 -98.493  61.688  1.00 71.34  ?  112  TYR E CE1 1 
ATOM   14815 C  CE2 . TYR E 5  112  ? -16.925 -96.215  62.163  1.00 67.76  ?  112  TYR E CE2 1 
ATOM   14816 C  CZ  . TYR E 5  112  ? -16.549 -97.535  62.032  1.00 64.44  ?  112  TYR E CZ  1 
ATOM   14817 O  OH  . TYR E 5  112  ? -15.239 -97.897  62.246  1.00 59.47  ?  112  TYR E OH  1 
ATOM   14818 N  N   . GLY E 5  113  ? -23.233 -95.426  59.281  1.00 81.06  ?  113  GLY E N   1 
ATOM   14819 C  CA  . GLY E 5  113  ? -24.660 -95.556  59.081  1.00 80.42  ?  113  GLY E CA  1 
ATOM   14820 C  C   . GLY E 5  113  ? -25.509 -95.379  60.319  1.00 83.21  ?  113  GLY E C   1 
ATOM   14821 O  O   . GLY E 5  113  ? -26.723 -95.603  60.251  1.00 82.79  ?  113  GLY E O   1 
ATOM   14822 N  N   . ALA E 5  114  ? -24.916 -94.990  61.445  1.00 88.72  ?  114  ALA E N   1 
ATOM   14823 C  CA  . ALA E 5  114  ? -25.658 -94.773  62.684  1.00 85.02  ?  114  ALA E CA  1 
ATOM   14824 C  C   . ALA E 5  114  ? -26.087 -93.311  62.744  1.00 83.02  ?  114  ALA E C   1 
ATOM   14825 O  O   . ALA E 5  114  ? -25.244 -92.412  62.824  1.00 82.05  ?  114  ALA E O   1 
ATOM   14826 C  CB  . ALA E 5  114  ? -24.810 -95.149  63.896  1.00 85.14  ?  114  ALA E CB  1 
ATOM   14827 N  N   . SER E 5  115  ? -27.396 -93.075  62.708  1.00 88.60  ?  115  SER E N   1 
ATOM   14828 C  CA  . SER E 5  115  ? -27.927 -91.721  62.718  1.00 89.89  ?  115  SER E CA  1 
ATOM   14829 C  C   . SER E 5  115  ? -29.283 -91.716  63.407  1.00 98.09  ?  115  SER E C   1 
ATOM   14830 O  O   . SER E 5  115  ? -29.927 -92.757  63.566  1.00 105.15 ?  115  SER E O   1 
ATOM   14831 C  CB  . SER E 5  115  ? -28.046 -91.153  61.298  1.00 89.04  ?  115  SER E CB  1 
ATOM   14832 O  OG  . SER E 5  115  ? -29.014 -91.863  60.546  1.00 85.04  ?  115  SER E OG  1 
ATOM   14833 N  N   . MET E 5  116  ? -29.707 -90.519  63.822  1.00 91.78  ?  116  MET E N   1 
ATOM   14834 C  CA  . MET E 5  116  ? -31.030 -90.363  64.417  1.00 93.34  ?  116  MET E CA  1 
ATOM   14835 C  C   . MET E 5  116  ? -32.129 -90.656  63.406  1.00 85.55  ?  116  MET E C   1 
ATOM   14836 O  O   . MET E 5  116  ? -33.243 -91.036  63.786  1.00 85.83  ?  116  MET E O   1 
ATOM   14837 C  CB  . MET E 5  116  ? -31.185 -88.948  64.977  1.00 90.19  ?  116  MET E CB  1 
ATOM   14838 C  CG  . MET E 5  116  ? -32.441 -88.714  65.803  1.00 83.29  ?  116  MET E CG  1 
ATOM   14839 S  SD  . MET E 5  116  ? -32.438 -89.631  67.353  1.00 83.18  ?  116  MET E SD  1 
ATOM   14840 C  CE  . MET E 5  116  ? -34.191 -89.706  67.708  1.00 99.45  ?  116  MET E CE  1 
ATOM   14841 N  N   . VAL E 5  117  ? -31.831 -90.492  62.116  1.00 74.44  ?  117  VAL E N   1 
ATOM   14842 C  CA  . VAL E 5  117  ? -32.826 -90.722  61.075  1.00 78.11  ?  117  VAL E CA  1 
ATOM   14843 C  C   . VAL E 5  117  ? -33.152 -92.205  60.955  1.00 83.32  ?  117  VAL E C   1 
ATOM   14844 O  O   . VAL E 5  117  ? -34.322 -92.589  60.842  1.00 83.34  ?  117  VAL E O   1 
ATOM   14845 C  CB  . VAL E 5  117  ? -32.329 -90.139  59.742  1.00 65.18  ?  117  VAL E CB  1 
ATOM   14846 C  CG1 . VAL E 5  117  ? -33.325 -90.408  58.641  1.00 64.43  ?  117  VAL E CG1 1 
ATOM   14847 C  CG2 . VAL E 5  117  ? -32.077 -88.649  59.883  1.00 63.47  ?  117  VAL E CG2 1 
ATOM   14848 N  N   . ALA E 5  118  ? -32.129 -93.063  60.980  1.00 98.41  ?  118  ALA E N   1 
ATOM   14849 C  CA  . ALA E 5  118  ? -32.360 -94.499  60.866  1.00 103.19 ?  118  ALA E CA  1 
ATOM   14850 C  C   . ALA E 5  118  ? -33.147 -95.054  62.044  1.00 104.25 ?  118  ALA E C   1 
ATOM   14851 O  O   . ALA E 5  118  ? -33.780 -96.108  61.912  1.00 107.79 ?  118  ALA E O   1 
ATOM   14852 C  CB  . ALA E 5  118  ? -31.028 -95.238  60.736  1.00 106.65 ?  118  ALA E CB  1 
ATOM   14853 N  N   . GLU E 5  119  ? -33.123 -94.371  63.191  1.00 99.05  ?  119  GLU E N   1 
ATOM   14854 C  CA  . GLU E 5  119  ? -33.868 -94.847  64.351  1.00 107.61 ?  119  GLU E CA  1 
ATOM   14855 C  C   . GLU E 5  119  ? -35.371 -94.729  64.130  1.00 113.65 ?  119  GLU E C   1 
ATOM   14856 O  O   . GLU E 5  119  ? -36.129 -95.644  64.473  1.00 113.79 ?  119  GLU E O   1 
ATOM   14857 C  CB  . GLU E 5  119  ? -33.440 -94.072  65.598  1.00 104.43 ?  119  GLU E CB  1 
ATOM   14858 C  CG  . GLU E 5  119  ? -34.429 -94.132  66.752  1.00 119.47 ?  119  GLU E CG  1 
ATOM   14859 C  CD  . GLU E 5  119  ? -33.827 -93.656  68.061  1.00 114.94 ?  119  GLU E CD  1 
ATOM   14860 O  OE1 . GLU E 5  119  ? -32.620 -93.890  68.284  1.00 103.53 ?  119  GLU E OE1 1 
ATOM   14861 O  OE2 . GLU E 5  119  ? -34.562 -93.046  68.867  1.00 122.33 -1 119  GLU E OE2 1 
ATOM   14862 N  N   . ARG E 5  120  ? -35.819 -93.619  63.549  1.00 112.09 ?  120  ARG E N   1 
ATOM   14863 C  CA  . ARG E 5  120  ? -37.236 -93.363  63.300  1.00 107.08 ?  120  ARG E CA  1 
ATOM   14864 C  C   . ARG E 5  120  ? -37.487 -93.487  61.800  1.00 111.33 ?  120  ARG E C   1 
ATOM   14865 O  O   . ARG E 5  120  ? -37.215 -92.556  61.037  1.00 106.28 ?  120  ARG E O   1 
ATOM   14866 C  CB  . ARG E 5  120  ? -37.637 -91.985  63.819  1.00 102.22 ?  120  ARG E CB  1 
ATOM   14867 C  CG  . ARG E 5  120  ? -37.027 -91.625  65.163  1.00 105.89 ?  120  ARG E CG  1 
ATOM   14868 C  CD  . ARG E 5  120  ? -36.897 -90.120  65.322  1.00 106.15 ?  120  ARG E CD  1 
ATOM   14869 N  NE  . ARG E 5  120  ? -38.180 -89.475  65.574  1.00 112.79 ?  120  ARG E NE  1 
ATOM   14870 C  CZ  . ARG E 5  120  ? -38.525 -88.918  66.727  1.00 109.00 ?  120  ARG E CZ  1 
ATOM   14871 N  NH1 . ARG E 5  120  ? -37.700 -88.903  67.761  1.00 101.87 ?  120  ARG E NH1 1 
ATOM   14872 N  NH2 . ARG E 5  120  ? -39.725 -88.357  66.843  1.00 105.73 ?  120  ARG E NH2 1 
ATOM   14873 N  N   . GLY E 5  121  ? -38.008 -94.638  61.381  1.00 107.00 ?  121  GLY E N   1 
ATOM   14874 C  CA  . GLY E 5  121  ? -38.332 -94.849  59.984  1.00 90.33  ?  121  GLY E CA  1 
ATOM   14875 C  C   . GLY E 5  121  ? -37.797 -96.148  59.418  1.00 97.02  ?  121  GLY E C   1 
ATOM   14876 O  O   . GLY E 5  121  ? -38.311 -96.652  58.414  1.00 104.87 ?  121  GLY E O   1 
ATOM   14877 N  N   . GLY E 5  122  ? -36.767 -96.703  60.052  1.00 87.15  ?  122  GLY E N   1 
ATOM   14878 C  CA  . GLY E 5  122  ? -36.157 -97.926  59.567  1.00 94.49  ?  122  GLY E CA  1 
ATOM   14879 C  C   . GLY E 5  122  ? -35.448 -97.727  58.245  1.00 97.99  ?  122  GLY E C   1 
ATOM   14880 O  O   . GLY E 5  122  ? -35.612 -98.520  57.313  1.00 95.08  ?  122  GLY E O   1 
ATOM   14881 N  N   . ILE E 5  123  ? -34.651 -96.659  58.156  1.00 123.51 ?  123  ILE E N   1 
ATOM   14882 C  CA  . ILE E 5  123  ? -33.980 -96.325  56.905  1.00 121.10 ?  123  ILE E CA  1 
ATOM   14883 C  C   . ILE E 5  123  ? -32.868 -97.319  56.595  1.00 121.56 ?  123  ILE E C   1 
ATOM   14884 O  O   . ILE E 5  123  ? -32.639 -97.651  55.424  1.00 116.02 ?  123  ILE E O   1 
ATOM   14885 C  CB  . ILE E 5  123  ? -33.448 -94.881  56.965  1.00 110.47 ?  123  ILE E CB  1 
ATOM   14886 C  CG1 . ILE E 5  123  ? -34.598 -93.908  57.221  1.00 108.15 ?  123  ILE E CG1 1 
ATOM   14887 C  CG2 . ILE E 5  123  ? -32.728 -94.514  55.679  1.00 109.17 ?  123  ILE E CG2 1 
ATOM   14888 C  CD1 . ILE E 5  123  ? -35.640 -93.918  56.127  1.00 99.02  ?  123  ILE E CD1 1 
ATOM   14889 N  N   . VAL E 5  124  ? -32.197 -97.830  57.626  1.00 95.22  ?  124  VAL E N   1 
ATOM   14890 C  CA  . VAL E 5  124  ? -30.990 -98.661  57.547  1.00 93.63  ?  124  VAL E CA  1 
ATOM   14891 C  C   . VAL E 5  124  ? -30.119 -98.232  56.367  1.00 87.43  ?  124  VAL E C   1 
ATOM   14892 O  O   . VAL E 5  124  ? -30.097 -98.893  55.317  1.00 79.68  ?  124  VAL E O   1 
ATOM   14893 C  CB  . VAL E 5  124  ? -31.342 -100.167 57.527  1.00 88.12  ?  124  VAL E CB  1 
ATOM   14894 C  CG1 . VAL E 5  124  ? -32.304 -100.555 56.392  1.00 87.81  ?  124  VAL E CG1 1 
ATOM   14895 C  CG2 . VAL E 5  124  ? -30.075 -101.027 57.507  1.00 75.29  ?  124  VAL E CG2 1 
ATOM   14896 N  N   . PRO E 5  125  ? -29.397 -97.120  56.487  1.00 85.15  ?  125  PRO E N   1 
ATOM   14897 C  CA  . PRO E 5  125  ? -28.516 -96.687  55.398  1.00 84.83  ?  125  PRO E CA  1 
ATOM   14898 C  C   . PRO E 5  125  ? -27.299 -97.592  55.285  1.00 83.50  ?  125  PRO E C   1 
ATOM   14899 O  O   . PRO E 5  125  ? -27.015 -98.425  56.147  1.00 94.33  ?  125  PRO E O   1 
ATOM   14900 C  CB  . PRO E 5  125  ? -28.122 -95.264  55.802  1.00 78.18  ?  125  PRO E CB  1 
ATOM   14901 C  CG  . PRO E 5  125  ? -28.253 -95.252  57.285  1.00 81.63  ?  125  PRO E CG  1 
ATOM   14902 C  CD  . PRO E 5  125  ? -29.408 -96.160  57.604  1.00 81.00  ?  125  PRO E CD  1 
ATOM   14903 N  N   . ALA E 5  126  ? -26.566 -97.406  54.191  1.00 70.48  ?  126  ALA E N   1 
ATOM   14904 C  CA  . ALA E 5  126  ? -25.417 -98.247  53.898  1.00 74.90  ?  126  ALA E CA  1 
ATOM   14905 C  C   . ALA E 5  126  ? -24.222 -97.865  54.764  1.00 76.26  ?  126  ALA E C   1 
ATOM   14906 O  O   . ALA E 5  126  ? -24.079 -96.719  55.198  1.00 68.62  ?  126  ALA E O   1 
ATOM   14907 C  CB  . ALA E 5  126  ? -25.042 -98.146  52.420  1.00 80.72  ?  126  ALA E CB  1 
ATOM   14908 N  N   . ASN E 5  127  ? -23.358 -98.847  55.009  1.00 91.22  ?  127  ASN E N   1 
ATOM   14909 C  CA  . ASN E 5  127  ? -22.146 -98.663  55.795  1.00 89.49  ?  127  ASN E CA  1 
ATOM   14910 C  C   . ASN E 5  127  ? -20.952 -98.608  54.850  1.00 90.82  ?  127  ASN E C   1 
ATOM   14911 O  O   . ASN E 5  127  ? -20.689 -99.572  54.122  1.00 88.90  ?  127  ASN E O   1 
ATOM   14912 C  CB  . ASN E 5  127  ? -21.983 -99.792  56.813  1.00 87.60  ?  127  ASN E CB  1 
ATOM   14913 C  CG  . ASN E 5  127  ? -20.856 -99.538  57.797  1.00 89.57  ?  127  ASN E CG  1 
ATOM   14914 O  OD1 . ASN E 5  127  ? -20.167 -98.520  57.724  1.00 93.64  ?  127  ASN E OD1 1 
ATOM   14915 N  ND2 . ASN E 5  127  ? -20.663 -100.467 58.726  1.00 85.18  ?  127  ASN E ND2 1 
ATOM   14916 N  N   . PHE E 5  128  ? -20.228 -97.486  54.869  1.00 86.01  ?  128  PHE E N   1 
ATOM   14917 C  CA  . PHE E 5  128  ? -19.119 -97.288  53.942  1.00 83.09  ?  128  PHE E CA  1 
ATOM   14918 C  C   . PHE E 5  128  ? -17.957 -98.237  54.201  1.00 93.98  ?  128  PHE E C   1 
ATOM   14919 O  O   . PHE E 5  128  ? -17.163 -98.485  53.287  1.00 101.82 ?  128  PHE E O   1 
ATOM   14920 C  CB  . PHE E 5  128  ? -18.614 -95.847  54.019  1.00 79.17  ?  128  PHE E CB  1 
ATOM   14921 C  CG  . PHE E 5  128  ? -19.600 -94.830  53.528  1.00 81.26  ?  128  PHE E CG  1 
ATOM   14922 C  CD1 . PHE E 5  128  ? -20.459 -95.127  52.484  1.00 78.68  ?  128  PHE E CD1 1 
ATOM   14923 C  CD2 . PHE E 5  128  ? -19.666 -93.575  54.108  1.00 83.19  ?  128  PHE E CD2 1 
ATOM   14924 C  CE1 . PHE E 5  128  ? -21.366 -94.193  52.032  1.00 70.91  ?  128  PHE E CE1 1 
ATOM   14925 C  CE2 . PHE E 5  128  ? -20.572 -92.637  53.659  1.00 72.86  ?  128  PHE E CE2 1 
ATOM   14926 C  CZ  . PHE E 5  128  ? -21.423 -92.946  52.620  1.00 70.23  ?  128  PHE E CZ  1 
ATOM   14927 N  N   . HIS E 5  129  ? -17.834 -98.770  55.416  1.00 104.13 ?  129  HIS E N   1 
ATOM   14928 C  CA  . HIS E 5  129  ? -16.681 -99.571  55.799  1.00 107.24 ?  129  HIS E CA  1 
ATOM   14929 C  C   . HIS E 5  129  ? -16.897 -101.065 55.585  1.00 108.92 ?  129  HIS E C   1 
ATOM   14930 O  O   . HIS E 5  129  ? -16.141 -101.876 56.133  1.00 115.56 ?  129  HIS E O   1 
ATOM   14931 C  CB  . HIS E 5  129  ? -16.310 -99.282  57.253  1.00 104.11 ?  129  HIS E CB  1 
ATOM   14932 C  CG  . HIS E 5  129  ? -16.235 -97.821  57.569  1.00 99.50  ?  129  HIS E CG  1 
ATOM   14933 N  ND1 . HIS E 5  129  ? -16.993 -97.231  58.557  1.00 102.00 ?  129  HIS E ND1 1 
ATOM   14934 C  CD2 . HIS E 5  129  ? -15.506 -96.826  57.010  1.00 95.87  ?  129  HIS E CD2 1 
ATOM   14935 C  CE1 . HIS E 5  129  ? -16.726 -95.938  58.602  1.00 95.34  ?  129  HIS E CE1 1 
ATOM   14936 N  NE2 . HIS E 5  129  ? -15.829 -95.666  57.671  1.00 93.89  ?  129  HIS E NE2 1 
ATOM   14937 N  N   . GLN E 5  130  ? -17.905 -101.446 54.806  1.00 106.35 ?  130  GLN E N   1 
ATOM   14938 C  CA  . GLN E 5  130  ? -18.038 -102.831 54.392  1.00 115.19 ?  130  GLN E CA  1 
ATOM   14939 C  C   . GLN E 5  130  ? -17.173 -103.089 53.161  1.00 118.80 ?  130  GLN E C   1 
ATOM   14940 O  O   . GLN E 5  130  ? -16.827 -102.174 52.409  1.00 118.59 ?  130  GLN E O   1 
ATOM   14941 C  CB  . GLN E 5  130  ? -19.502 -103.177 54.113  1.00 118.15 ?  130  GLN E CB  1 
ATOM   14942 C  CG  . GLN E 5  130  ? -20.081 -102.540 52.860  1.00 115.74 ?  130  GLN E CG  1 
ATOM   14943 C  CD  . GLN E 5  130  ? -21.538 -102.907 52.646  1.00 114.06 ?  130  GLN E CD  1 
ATOM   14944 O  OE1 . GLN E 5  130  ? -22.130 -103.635 53.443  1.00 118.61 ?  130  GLN E OE1 1 
ATOM   14945 N  NE2 . GLN E 5  130  ? -22.124 -102.404 51.565  1.00 116.93 ?  130  GLN E NE2 1 
ATOM   14946 N  N   . GLN E 5  131  ? -16.814 -104.359 52.965  1.00 144.29 ?  131  GLN E N   1 
ATOM   14947 C  CA  . GLN E 5  131  ? -15.845 -104.702 51.931  1.00 151.98 ?  131  GLN E CA  1 
ATOM   14948 C  C   . GLN E 5  131  ? -16.376 -104.474 50.522  1.00 153.69 ?  131  GLN E C   1 
ATOM   14949 O  O   . GLN E 5  131  ? -15.577 -104.290 49.597  1.00 147.91 ?  131  GLN E O   1 
ATOM   14950 C  CB  . GLN E 5  131  ? -15.400 -106.158 52.091  1.00 155.84 ?  131  GLN E CB  1 
ATOM   14951 C  CG  . GLN E 5  131  ? -14.112 -106.336 52.890  1.00 160.01 ?  131  GLN E CG  1 
ATOM   14952 C  CD  . GLN E 5  131  ? -12.930 -105.573 52.309  1.00 161.01 ?  131  GLN E CD  1 
ATOM   14953 O  OE1 . GLN E 5  131  ? -12.905 -105.239 51.123  1.00 162.45 ?  131  GLN E OE1 1 
ATOM   14954 N  NE2 . GLN E 5  131  ? -11.943 -105.289 53.152  1.00 150.80 ?  131  GLN E NE2 1 
ATOM   14955 N  N   . ARG E 5  132  ? -17.698 -104.478 50.332  1.00 137.48 ?  132  ARG E N   1 
ATOM   14956 C  CA  . ARG E 5  132  ? -18.241 -104.282 48.992  1.00 129.50 ?  132  ARG E CA  1 
ATOM   14957 C  C   . ARG E 5  132  ? -18.032 -102.850 48.514  1.00 121.19 ?  132  ARG E C   1 
ATOM   14958 O  O   . ARG E 5  132  ? -17.641 -102.625 47.363  1.00 125.53 ?  132  ARG E O   1 
ATOM   14959 C  CB  . ARG E 5  132  ? -19.724 -104.650 48.962  1.00 125.96 ?  132  ARG E CB  1 
ATOM   14960 C  CG  . ARG E 5  132  ? -20.321 -104.667 47.563  1.00 128.60 ?  132  ARG E CG  1 
ATOM   14961 C  CD  . ARG E 5  132  ? -21.834 -104.802 47.602  1.00 128.61 ?  132  ARG E CD  1 
ATOM   14962 N  NE  . ARG E 5  132  ? -22.482 -103.594 48.097  1.00 127.25 ?  132  ARG E NE  1 
ATOM   14963 C  CZ  . ARG E 5  132  ? -23.790 -103.382 48.071  1.00 131.00 ?  132  ARG E CZ  1 
ATOM   14964 N  NH1 . ARG E 5  132  ? -24.626 -104.283 47.580  1.00 137.43 ?  132  ARG E NH1 1 
ATOM   14965 N  NH2 . ARG E 5  132  ? -24.273 -102.239 48.551  1.00 125.15 ?  132  ARG E NH2 1 
ATOM   14966 N  N   . LEU E 5  133  ? -18.285 -101.869 49.380  1.00 83.26  ?  133  LEU E N   1 
ATOM   14967 C  CA  . LEU E 5  133  ? -18.055 -100.473 49.031  1.00 84.56  ?  133  LEU E CA  1 
ATOM   14968 C  C   . LEU E 5  133  ? -16.610 -100.039 49.242  1.00 84.10  ?  133  LEU E C   1 
ATOM   14969 O  O   . LEU E 5  133  ? -16.271 -98.896  48.915  1.00 82.81  ?  133  LEU E O   1 
ATOM   14970 C  CB  . LEU E 5  133  ? -18.991 -99.562  49.831  1.00 79.60  ?  133  LEU E CB  1 
ATOM   14971 C  CG  . LEU E 5  133  ? -20.478 -99.916  49.784  1.00 81.85  ?  133  LEU E CG  1 
ATOM   14972 C  CD1 . LEU E 5  133  ? -21.232 -99.236  50.916  1.00 80.58  ?  133  LEU E CD1 1 
ATOM   14973 C  CD2 . LEU E 5  133  ? -21.074 -99.537  48.436  1.00 74.47  ?  133  LEU E CD2 1 
ATOM   14974 N  N   . ARG E 5  134  ? -15.756 -100.910 49.778  1.00 107.66 ?  134  ARG E N   1 
ATOM   14975 C  CA  . ARG E 5  134  ? -14.335 -100.590 49.854  1.00 112.42 ?  134  ARG E CA  1 
ATOM   14976 C  C   . ARG E 5  134  ? -13.641 -100.849 48.522  1.00 117.06 ?  134  ARG E C   1 
ATOM   14977 O  O   . ARG E 5  134  ? -12.743 -100.095 48.129  1.00 105.60 ?  134  ARG E O   1 
ATOM   14978 C  CB  . ARG E 5  134  ? -13.673 -101.394 50.973  1.00 115.55 ?  134  ARG E CB  1 
ATOM   14979 C  CG  . ARG E 5  134  ? -13.710 -100.705 52.327  1.00 113.31 ?  134  ARG E CG  1 
ATOM   14980 C  CD  . ARG E 5  134  ? -12.541 -101.132 53.199  1.00 120.36 ?  134  ARG E CD  1 
ATOM   14981 N  NE  . ARG E 5  134  ? -12.895 -102.224 54.097  1.00 115.78 ?  134  ARG E NE  1 
ATOM   14982 C  CZ  . ARG E 5  134  ? -12.991 -102.109 55.414  1.00 117.26 ?  134  ARG E CZ  1 
ATOM   14983 N  NH1 . ARG E 5  134  ? -12.770 -100.956 56.024  1.00 109.93 ?  134  ARG E NH1 1 
ATOM   14984 N  NH2 . ARG E 5  134  ? -13.316 -103.176 56.137  1.00 126.49 ?  134  ARG E NH2 1 
ATOM   14985 N  N   . GLU E 5  135  ? -14.045 -101.904 47.819  1.00 136.45 ?  135  GLU E N   1 
ATOM   14986 C  CA  . GLU E 5  135  ? -13.534 -102.211 46.491  1.00 134.60 ?  135  GLU E CA  1 
ATOM   14987 C  C   . GLU E 5  135  ? -14.314 -101.514 45.383  1.00 131.95 ?  135  GLU E C   1 
ATOM   14988 O  O   . GLU E 5  135  ? -13.980 -101.686 44.206  1.00 136.65 ?  135  GLU E O   1 
ATOM   14989 C  CB  . GLU E 5  135  ? -13.549 -103.729 46.255  1.00 131.60 ?  135  GLU E CB  1 
ATOM   14990 C  CG  . GLU E 5  135  ? -13.099 -104.579 47.446  1.00 138.78 ?  135  GLU E CG  1 
ATOM   14991 C  CD  . GLU E 5  135  ? -11.643 -104.364 47.848  1.00 149.39 ?  135  GLU E CD  1 
ATOM   14992 O  OE1 . GLU E 5  135  ? -10.917 -103.603 47.170  1.00 150.38 ?  135  GLU E OE1 1 
ATOM   14993 O  OE2 . GLU E 5  135  ? -11.222 -104.966 48.857  1.00 151.89 -1 135  GLU E OE2 1 
ATOM   14994 N  N   . ALA E 5  136  ? -15.339 -100.736 45.729  1.00 127.64 ?  136  ALA E N   1 
ATOM   14995 C  CA  . ALA E 5  136  ? -16.152 -100.054 44.741  1.00 125.11 ?  136  ALA E CA  1 
ATOM   14996 C  C   . ALA E 5  136  ? -15.393 -98.871  44.147  1.00 131.24 ?  136  ALA E C   1 
ATOM   14997 O  O   . ALA E 5  136  ? -14.628 -98.202  44.845  1.00 135.52 ?  136  ALA E O   1 
ATOM   14998 C  CB  . ALA E 5  136  ? -17.452 -99.564  45.366  1.00 127.28 ?  136  ALA E CB  1 
ATOM   14999 N  N   . PRO E 5  137  ? -15.593 -98.598  42.862  1.00 90.07  ?  137  PRO E N   1 
ATOM   15000 C  CA  . PRO E 5  137  ? -14.886 -97.489  42.213  1.00 86.89  ?  137  PRO E CA  1 
ATOM   15001 C  C   . PRO E 5  137  ? -15.378 -96.133  42.699  1.00 84.10  ?  137  PRO E C   1 
ATOM   15002 O  O   . PRO E 5  137  ? -16.456 -95.998  43.282  1.00 85.80  ?  137  PRO E O   1 
ATOM   15003 C  CB  . PRO E 5  137  ? -15.206 -97.690  40.726  1.00 88.07  ?  137  PRO E CB  1 
ATOM   15004 C  CG  . PRO E 5  137  ? -15.643 -99.127  40.619  1.00 81.55  ?  137  PRO E CG  1 
ATOM   15005 C  CD  . PRO E 5  137  ? -16.353 -99.406  41.896  1.00 84.46  ?  137  PRO E CD  1 
ATOM   15006 N  N   . LEU E 5  138  ? -14.551 -95.114  42.446  1.00 87.91  ?  138  LEU E N   1 
ATOM   15007 C  CA  . LEU E 5  138  ? -14.920 -93.748  42.807  1.00 86.42  ?  138  LEU E CA  1 
ATOM   15008 C  C   . LEU E 5  138  ? -16.125 -93.272  42.008  1.00 92.81  ?  138  LEU E C   1 
ATOM   15009 O  O   . LEU E 5  138  ? -17.029 -92.631  42.558  1.00 93.07  ?  138  LEU E O   1 
ATOM   15010 C  CB  . LEU E 5  138  ? -13.736 -92.806  42.591  1.00 82.15  ?  138  LEU E CB  1 
ATOM   15011 C  CG  . LEU E 5  138  ? -12.768 -92.576  43.753  1.00 83.12  ?  138  LEU E CG  1 
ATOM   15012 C  CD1 . LEU E 5  138  ? -13.484 -91.902  44.916  1.00 88.73  ?  138  LEU E CD1 1 
ATOM   15013 C  CD2 . LEU E 5  138  ? -12.108 -93.873  44.196  1.00 90.05  ?  138  LEU E CD2 1 
ATOM   15014 N  N   . SER E 5  139  ? -16.153 -93.572  40.709  1.00 97.18  ?  139  SER E N   1 
ATOM   15015 C  CA  . SER E 5  139  ? -17.280 -93.177  39.874  1.00 91.34  ?  139  SER E CA  1 
ATOM   15016 C  C   . SER E 5  139  ? -18.575 -93.860  40.293  1.00 90.20  ?  139  SER E C   1 
ATOM   15017 O  O   . SER E 5  139  ? -19.659 -93.350  39.986  1.00 87.00  ?  139  SER E O   1 
ATOM   15018 C  CB  . SER E 5  139  ? -16.968 -93.479  38.410  1.00 100.11 ?  139  SER E CB  1 
ATOM   15019 O  OG  . SER E 5  139  ? -16.534 -94.817  38.247  1.00 107.16 ?  139  SER E OG  1 
ATOM   15020 N  N   . HIS E 5  140  ? -18.490 -95.002  40.980  1.00 94.37  ?  140  HIS E N   1 
ATOM   15021 C  CA  . HIS E 5  140  ? -19.689 -95.606  41.550  1.00 96.63  ?  140  HIS E CA  1 
ATOM   15022 C  C   . HIS E 5  140  ? -20.270 -94.728  42.650  1.00 90.21  ?  140  HIS E C   1 
ATOM   15023 O  O   . HIS E 5  140  ? -21.493 -94.597  42.768  1.00 87.54  ?  140  HIS E O   1 
ATOM   15024 C  CB  . HIS E 5  140  ? -19.375 -97.003  42.084  1.00 97.66  ?  140  HIS E CB  1 
ATOM   15025 C  CG  . HIS E 5  140  ? -20.479 -97.598  42.902  1.00 92.99  ?  140  HIS E CG  1 
ATOM   15026 N  ND1 . HIS E 5  140  ? -21.661 -98.040  42.347  1.00 92.30  ?  140  HIS E ND1 1 
ATOM   15027 C  CD2 . HIS E 5  140  ? -20.582 -97.821  44.233  1.00 90.77  ?  140  HIS E CD2 1 
ATOM   15028 C  CE1 . HIS E 5  140  ? -22.444 -98.511  43.302  1.00 91.85  ?  140  HIS E CE1 1 
ATOM   15029 N  NE2 . HIS E 5  140  ? -21.812 -98.389  44.456  1.00 95.58  ?  140  HIS E NE2 1 
ATOM   15030 N  N   . PHE E 5  141  ? -19.406 -94.121  43.467  1.00 89.73  ?  141  PHE E N   1 
ATOM   15031 C  CA  . PHE E 5  141  ? -19.877 -93.151  44.448  1.00 86.34  ?  141  PHE E CA  1 
ATOM   15032 C  C   . PHE E 5  141  ? -20.492 -91.939  43.762  1.00 83.03  ?  141  PHE E C   1 
ATOM   15033 O  O   . PHE E 5  141  ? -21.530 -91.429  44.198  1.00 78.89  ?  141  PHE E O   1 
ATOM   15034 C  CB  . PHE E 5  141  ? -18.725 -92.721  45.357  1.00 92.28  ?  141  PHE E CB  1 
ATOM   15035 C  CG  . PHE E 5  141  ? -18.201 -93.821  46.236  1.00 95.87  ?  141  PHE E CG  1 
ATOM   15036 C  CD1 . PHE E 5  141  ? -19.054 -94.533  47.059  1.00 94.45  ?  141  PHE E CD1 1 
ATOM   15037 C  CD2 . PHE E 5  141  ? -16.853 -94.140  46.239  1.00 98.54  ?  141  PHE E CD2 1 
ATOM   15038 C  CE1 . PHE E 5  141  ? -18.575 -95.545  47.869  1.00 93.16  ?  141  PHE E CE1 1 
ATOM   15039 C  CE2 . PHE E 5  141  ? -16.367 -95.150  47.047  1.00 100.65 ?  141  PHE E CE2 1 
ATOM   15040 C  CZ  . PHE E 5  141  ? -17.229 -95.854  47.864  1.00 101.21 ?  141  PHE E CZ  1 
ATOM   15041 N  N   . PHE E 5  142  ? -19.870 -91.473  42.677  1.00 82.86  ?  142  PHE E N   1 
ATOM   15042 C  CA  . PHE E 5  142  ? -20.382 -90.307  41.965  1.00 77.46  ?  142  PHE E CA  1 
ATOM   15043 C  C   . PHE E 5  142  ? -21.771 -90.573  41.398  1.00 74.89  ?  142  PHE E C   1 
ATOM   15044 O  O   . PHE E 5  142  ? -22.685 -89.755  41.551  1.00 78.02  ?  142  PHE E O   1 
ATOM   15045 C  CB  . PHE E 5  142  ? -19.410 -89.911  40.851  1.00 77.68  ?  142  PHE E CB  1 
ATOM   15046 C  CG  . PHE E 5  142  ? -19.814 -88.673  40.104  1.00 74.80  ?  142  PHE E CG  1 
ATOM   15047 C  CD1 . PHE E 5  142  ? -19.508 -87.418  40.601  1.00 72.94  ?  142  PHE E CD1 1 
ATOM   15048 C  CD2 . PHE E 5  142  ? -20.503 -88.765  38.906  1.00 83.00  ?  142  PHE E CD2 1 
ATOM   15049 C  CE1 . PHE E 5  142  ? -19.879 -86.277  39.915  1.00 77.44  ?  142  PHE E CE1 1 
ATOM   15050 C  CE2 . PHE E 5  142  ? -20.878 -87.629  38.217  1.00 82.23  ?  142  PHE E CE2 1 
ATOM   15051 C  CZ  . PHE E 5  142  ? -20.566 -86.383  38.722  1.00 80.32  ?  142  PHE E CZ  1 
ATOM   15052 N  N   . VAL E 5  143  ? -21.951 -91.722  40.740  1.00 60.35  ?  143  VAL E N   1 
ATOM   15053 C  CA  . VAL E 5  143  ? -23.238 -92.033  40.131  1.00 61.97  ?  143  VAL E CA  1 
ATOM   15054 C  C   . VAL E 5  143  ? -24.299 -92.340  41.182  1.00 66.93  ?  143  VAL E C   1 
ATOM   15055 O  O   . VAL E 5  143  ? -25.497 -92.211  40.904  1.00 66.36  ?  143  VAL E O   1 
ATOM   15056 C  CB  . VAL E 5  143  ? -23.086 -93.195  39.129  1.00 64.06  ?  143  VAL E CB  1 
ATOM   15057 C  CG1 . VAL E 5  143  ? -22.924 -94.523  39.855  1.00 69.61  ?  143  VAL E CG1 1 
ATOM   15058 C  CG2 . VAL E 5  143  ? -24.268 -93.237  38.170  1.00 75.62  ?  143  VAL E CG2 1 
ATOM   15059 N  N   . VAL E 5  144  ? -23.894 -92.731  42.392  1.00 71.30  ?  144  VAL E N   1 
ATOM   15060 C  CA  . VAL E 5  144  ? -24.864 -92.959  43.457  1.00 68.41  ?  144  VAL E CA  1 
ATOM   15061 C  C   . VAL E 5  144  ? -25.359 -91.633  44.025  1.00 67.97  ?  144  VAL E C   1 
ATOM   15062 O  O   . VAL E 5  144  ? -26.555 -91.467  44.290  1.00 68.91  ?  144  VAL E O   1 
ATOM   15063 C  CB  . VAL E 5  144  ? -24.257 -93.863  44.546  1.00 66.18  ?  144  VAL E CB  1 
ATOM   15064 C  CG1 . VAL E 5  144  ? -25.011 -93.713  45.859  1.00 75.34  ?  144  VAL E CG1 1 
ATOM   15065 C  CG2 . VAL E 5  144  ? -24.274 -95.315  44.092  1.00 70.63  ?  144  VAL E CG2 1 
ATOM   15066 N  N   . ILE E 5  145  ? -24.455 -90.666  44.211  1.00 70.52  ?  145  ILE E N   1 
ATOM   15067 C  CA  . ILE E 5  145  ? -24.871 -89.333  44.644  1.00 69.20  ?  145  ILE E CA  1 
ATOM   15068 C  C   . ILE E 5  145  ? -25.770 -88.694  43.595  1.00 79.98  ?  145  ILE E C   1 
ATOM   15069 O  O   . ILE E 5  145  ? -26.719 -87.970  43.922  1.00 73.83  ?  145  ILE E O   1 
ATOM   15070 C  CB  . ILE E 5  145  ? -23.642 -88.452  44.936  1.00 61.90  ?  145  ILE E CB  1 
ATOM   15071 C  CG1 . ILE E 5  145  ? -22.694 -89.146  45.911  1.00 63.87  ?  145  ILE E CG1 1 
ATOM   15072 C  CG2 . ILE E 5  145  ? -24.071 -87.105  45.496  1.00 58.63  ?  145  ILE E CG2 1 
ATOM   15073 C  CD1 . ILE E 5  145  ? -21.317 -88.515  45.975  1.00 60.47  ?  145  ILE E CD1 1 
ATOM   15074 N  N   . THR E 5  146  ? -25.492 -88.960  42.318  1.00 87.50  ?  146  THR E N   1 
ATOM   15075 C  CA  . THR E 5  146  ? -26.240 -88.322  41.242  1.00 80.21  ?  146  THR E CA  1 
ATOM   15076 C  C   . THR E 5  146  ? -27.633 -88.925  41.097  1.00 83.37  ?  146  THR E C   1 
ATOM   15077 O  O   . THR E 5  146  ? -28.637 -88.203  41.106  1.00 83.54  ?  146  THR E O   1 
ATOM   15078 C  CB  . THR E 5  146  ? -25.465 -88.440  39.929  1.00 79.76  ?  146  THR E CB  1 
ATOM   15079 O  OG1 . THR E 5  146  ? -24.149 -87.899  40.097  1.00 73.66  ?  146  THR E OG1 1 
ATOM   15080 C  CG2 . THR E 5  146  ? -26.185 -87.696  38.813  1.00 81.01  ?  146  THR E CG2 1 
ATOM   15081 N  N   . ASN E 5  147  ? -27.716 -90.248  40.964  1.00 92.54  ?  147  ASN E N   1 
ATOM   15082 C  CA  . ASN E 5  147  ? -28.975 -90.920  40.658  1.00 95.59  ?  147  ASN E CA  1 
ATOM   15083 C  C   . ASN E 5  147  ? -29.635 -91.510  41.900  1.00 96.40  ?  147  ASN E C   1 
ATOM   15084 O  O   . ASN E 5  147  ? -30.790 -91.197  42.203  1.00 103.06 ?  147  ASN E O   1 
ATOM   15085 C  CB  . ASN E 5  147  ? -28.734 -92.012  39.608  1.00 91.80  ?  147  ASN E CB  1 
ATOM   15086 C  CG  . ASN E 5  147  ? -28.220 -91.452  38.299  1.00 87.46  ?  147  ASN E CG  1 
ATOM   15087 O  OD1 . ASN E 5  147  ? -28.521 -90.315  37.936  1.00 93.35  ?  147  ASN E OD1 1 
ATOM   15088 N  ND2 . ASN E 5  147  ? -27.437 -92.248  37.581  1.00 92.31  ?  147  ASN E ND2 1 
ATOM   15089 N  N   . GLY E 5  148  ? -28.924 -92.362  42.622  1.00 102.89 ?  148  GLY E N   1 
ATOM   15090 C  CA  . GLY E 5  148  ? -29.460 -93.038  43.779  1.00 104.88 ?  148  GLY E CA  1 
ATOM   15091 C  C   . GLY E 5  148  ? -28.915 -94.445  43.852  1.00 117.73 ?  148  GLY E C   1 
ATOM   15092 O  O   . GLY E 5  148  ? -27.868 -94.749  43.283  1.00 126.64 ?  148  GLY E O   1 
ATOM   15093 N  N   . VAL E 5  149  ? -29.635 -95.312  44.558  1.00 75.53  ?  149  VAL E N   1 
ATOM   15094 C  CA  . VAL E 5  149  ? -29.215 -96.704  44.688  1.00 82.52  ?  149  VAL E CA  1 
ATOM   15095 C  C   . VAL E 5  149  ? -29.826 -97.576  43.593  1.00 91.15  ?  149  VAL E C   1 
ATOM   15096 O  O   . VAL E 5  149  ? -29.105 -98.276  42.875  1.00 87.38  ?  149  VAL E O   1 
ATOM   15097 C  CB  . VAL E 5  149  ? -29.538 -97.229  46.107  1.00 71.19  ?  149  VAL E CB  1 
ATOM   15098 C  CG1 . VAL E 5  149  ? -31.021 -97.110  46.430  1.00 78.24  ?  149  VAL E CG1 1 
ATOM   15099 C  CG2 . VAL E 5  149  ? -29.067 -98.666  46.261  1.00 82.68  ?  149  VAL E CG2 1 
ATOM   15100 N  N   . TYR E 5  150  ? -31.147 -97.528  43.423  1.00 101.35 ?  150  TYR E N   1 
ATOM   15101 C  CA  . TYR E 5  150  ? -31.847 -98.275  42.386  1.00 103.22 ?  150  TYR E CA  1 
ATOM   15102 C  C   . TYR E 5  150  ? -33.299 -97.824  42.364  1.00 104.51 ?  150  TYR E C   1 
ATOM   15103 O  O   . TYR E 5  150  ? -33.913 -97.647  43.419  1.00 105.68 ?  150  TYR E O   1 
ATOM   15104 C  CB  . TYR E 5  150  ? -31.755 -99.794  42.616  1.00 101.48 ?  150  TYR E CB  1 
ATOM   15105 C  CG  . TYR E 5  150  ? -32.709 -100.347 43.653  1.00 102.09 ?  150  TYR E CG  1 
ATOM   15106 C  CD1 . TYR E 5  150  ? -32.429 -100.239 45.009  1.00 99.40  ?  150  TYR E CD1 1 
ATOM   15107 C  CD2 . TYR E 5  150  ? -33.878 -100.995 43.276  1.00 106.98 ?  150  TYR E CD2 1 
ATOM   15108 C  CE1 . TYR E 5  150  ? -33.294 -100.747 45.960  1.00 92.52  ?  150  TYR E CE1 1 
ATOM   15109 C  CE2 . TYR E 5  150  ? -34.750 -101.506 44.219  1.00 104.08 ?  150  TYR E CE2 1 
ATOM   15110 C  CZ  . TYR E 5  150  ? -34.452 -101.380 45.560  1.00 92.80  ?  150  TYR E CZ  1 
ATOM   15111 O  OH  . TYR E 5  150  ? -35.315 -101.888 46.503  1.00 109.30 ?  150  TYR E OH  1 
ATOM   15112 N  N   . ARG E 5  151  ? -33.833 -97.627  41.162  1.00 159.63 ?  151  ARG E N   1 
ATOM   15113 C  CA  . ARG E 5  151  ? -35.207 -97.182  41.005  1.00 167.10 ?  151  ARG E CA  1 
ATOM   15114 C  C   . ARG E 5  151  ? -36.164 -98.359  41.178  1.00 172.38 ?  151  ARG E C   1 
ATOM   15115 O  O   . ARG E 5  151  ? -35.758 -99.501  41.408  1.00 172.11 ?  151  ARG E O   1 
ATOM   15116 C  CB  . ARG E 5  151  ? -35.396 -96.511  39.645  1.00 167.02 ?  151  ARG E CB  1 
ATOM   15117 N  N   . GLY E 5  152  ? -37.459 -98.075  41.065  1.00 220.87 ?  152  GLY E N   1 
ATOM   15118 C  CA  . GLY E 5  152  ? -38.456 -99.123  41.206  1.00 228.35 ?  152  GLY E CA  1 
ATOM   15119 C  C   . GLY E 5  152  ? -38.387 -100.100 40.047  1.00 238.06 ?  152  GLY E C   1 
ATOM   15120 O  O   . GLY E 5  152  ? -38.357 -99.699  38.877  1.00 234.02 ?  152  GLY E O   1 
ATOM   15121 N  N   . ASP E 5  153  ? -38.350 -101.391 40.368  1.00 195.00 ?  153  ASP E N   1 
ATOM   15122 C  CA  . ASP E 5  153  ? -38.338 -102.413 39.337  1.00 194.52 ?  153  ASP E CA  1 
ATOM   15123 C  C   . ASP E 5  153  ? -39.647 -102.386 38.551  1.00 198.50 ?  153  ASP E C   1 
ATOM   15124 O  O   . ASP E 5  153  ? -40.707 -102.084 39.106  1.00 196.41 ?  153  ASP E O   1 
ATOM   15125 C  CB  . ASP E 5  153  ? -38.134 -103.794 39.953  1.00 191.65 ?  153  ASP E CB  1 
ATOM   15126 C  CG  . ASP E 5  153  ? -36.840 -103.901 40.730  1.00 183.11 ?  153  ASP E CG  1 
ATOM   15127 O  OD1 . ASP E 5  153  ? -35.988 -102.997 40.596  1.00 178.85 ?  153  ASP E OD1 1 
ATOM   15128 O  OD2 . ASP E 5  153  ? -36.675 -104.888 41.477  1.00 181.32 -1 153  ASP E OD2 1 
ATOM   15129 N  N   . PRO E 5  154  ? -39.599 -102.689 37.252  1.00 197.28 ?  154  PRO E N   1 
ATOM   15130 C  CA  . PRO E 5  154  ? -40.839 -102.671 36.459  1.00 199.87 ?  154  PRO E CA  1 
ATOM   15131 C  C   . PRO E 5  154  ? -41.850 -103.711 36.905  1.00 202.11 ?  154  PRO E C   1 
ATOM   15132 O  O   . PRO E 5  154  ? -43.054 -103.527 36.688  1.00 198.17 ?  154  PRO E O   1 
ATOM   15133 C  CB  . PRO E 5  154  ? -40.344 -102.934 35.029  1.00 200.63 ?  154  PRO E CB  1 
ATOM   15134 C  CG  . PRO E 5  154  ? -39.041 -103.642 35.204  1.00 199.64 ?  154  PRO E CG  1 
ATOM   15135 C  CD  . PRO E 5  154  ? -38.426 -103.065 36.444  1.00 197.60 ?  154  PRO E CD  1 
ATOM   15136 N  N   . GLU E 5  155  ? -41.399 -104.796 37.528  1.00 229.14 ?  155  GLU E N   1 
ATOM   15137 C  CA  . GLU E 5  155  ? -42.277 -105.837 38.036  1.00 230.75 ?  155  GLU E CA  1 
ATOM   15138 C  C   . GLU E 5  155  ? -42.045 -106.024 39.529  1.00 230.03 ?  155  GLU E C   1 
ATOM   15139 O  O   . GLU E 5  155  ? -40.980 -105.694 40.060  1.00 225.68 ?  155  GLU E O   1 
ATOM   15140 C  CB  . GLU E 5  155  ? -42.052 -107.163 37.298  1.00 234.09 ?  155  GLU E CB  1 
ATOM   15141 C  CG  . GLU E 5  155  ? -42.678 -107.217 35.913  1.00 237.10 ?  155  GLU E CG  1 
ATOM   15142 C  CD  . GLU E 5  155  ? -41.731 -106.746 34.826  1.00 234.32 ?  155  GLU E CD  1 
ATOM   15143 O  OE1 . GLU E 5  155  ? -40.501 -106.840 35.025  1.00 231.12 ?  155  GLU E OE1 1 
ATOM   15144 O  OE2 . GLU E 5  155  ? -42.216 -106.282 33.773  1.00 231.28 -1 155  GLU E OE2 1 
ATOM   15145 N  N   . ASN E 5  156  ? -43.068 -106.555 40.201  1.00 221.19 ?  156  ASN E N   1 
ATOM   15146 C  CA  . ASN E 5  156  ? -43.023 -106.841 41.637  1.00 225.74 ?  156  ASN E CA  1 
ATOM   15147 C  C   . ASN E 5  156  ? -42.744 -105.587 42.462  1.00 218.29 ?  156  ASN E C   1 
ATOM   15148 O  O   . ASN E 5  156  ? -42.124 -105.657 43.527  1.00 212.83 ?  156  ASN E O   1 
ATOM   15149 C  CB  . ASN E 5  156  ? -41.994 -107.931 41.955  1.00 223.54 ?  156  ASN E CB  1 
ATOM   15150 C  CG  . ASN E 5  156  ? -42.298 -109.240 41.256  1.00 223.68 ?  156  ASN E CG  1 
ATOM   15151 O  OD1 . ASN E 5  156  ? -43.454 -109.652 41.158  1.00 223.42 ?  156  ASN E OD1 1 
ATOM   15152 N  ND2 . ASN E 5  156  ? -41.258 -109.903 40.764  1.00 223.82 ?  156  ASN E ND2 1 
ATOM   15153 N  N   . GLY E 5  157  ? -43.202 -104.432 41.983  1.00 171.10 ?  157  GLY E N   1 
ATOM   15154 C  CA  . GLY E 5  157  ? -42.994 -103.202 42.720  1.00 161.45 ?  157  GLY E CA  1 
ATOM   15155 C  C   . GLY E 5  157  ? -41.537 -102.763 42.706  1.00 161.41 ?  157  GLY E C   1 
ATOM   15156 O  O   . GLY E 5  157  ? -40.714 -103.231 41.915  1.00 164.77 ?  157  GLY E O   1 
ATOM   15157 N  N   . GLY E 5  158  ? -41.231 -101.847 43.606  1.00 179.60 ?  158  GLY E N   1 
ATOM   15158 C  CA  . GLY E 5  158  ? -39.893 -101.305 43.759  1.00 169.52 ?  158  GLY E CA  1 
ATOM   15159 C  C   . GLY E 5  158  ? -39.962 -99.865  44.233  1.00 154.60 ?  158  GLY E C   1 
ATOM   15160 O  O   . GLY E 5  158  ? -40.940 -99.150  44.030  1.00 151.37 ?  158  GLY E O   1 
ATOM   15161 N  N   . TYR E 5  159  ? -38.884 -99.425  44.880  1.00 148.46 ?  159  TYR E N   1 
ATOM   15162 C  CA  . TYR E 5  159  ? -38.817 -98.080  45.434  1.00 141.67 ?  159  TYR E CA  1 
ATOM   15163 C  C   . TYR E 5  159  ? -37.365 -97.623  45.464  1.00 136.88 ?  159  TYR E C   1 
ATOM   15164 O  O   . TYR E 5  159  ? -36.436 -98.436  45.480  1.00 135.79 ?  159  TYR E O   1 
ATOM   15165 C  CB  . TYR E 5  159  ? -39.430 -98.017  46.842  1.00 140.61 ?  159  TYR E CB  1 
ATOM   15166 C  CG  . TYR E 5  159  ? -38.741 -98.906  47.857  1.00 135.00 ?  159  TYR E CG  1 
ATOM   15167 C  CD1 . TYR E 5  159  ? -38.995 -100.272 47.904  1.00 134.94 ?  159  TYR E CD1 1 
ATOM   15168 C  CD2 . TYR E 5  159  ? -37.835 -98.378  48.767  1.00 130.01 ?  159  TYR E CD2 1 
ATOM   15169 C  CE1 . TYR E 5  159  ? -38.365 -101.086 48.827  1.00 139.56 ?  159  TYR E CE1 1 
ATOM   15170 C  CE2 . TYR E 5  159  ? -37.199 -99.185  49.696  1.00 127.11 ?  159  TYR E CE2 1 
ATOM   15171 C  CZ  . TYR E 5  159  ? -37.469 -100.537 49.721  1.00 139.73 ?  159  TYR E CZ  1 
ATOM   15172 O  OH  . TYR E 5  159  ? -36.839 -101.343 50.643  1.00 147.14 ?  159  TYR E OH  1 
ATOM   15173 N  N   . GLN E 5  160  ? -37.183 -96.304  45.468  1.00 136.24 ?  160  GLN E N   1 
ATOM   15174 C  CA  . GLN E 5  160  ? -35.860 -95.703  45.551  1.00 130.43 ?  160  GLN E CA  1 
ATOM   15175 C  C   . GLN E 5  160  ? -35.528 -95.418  47.010  1.00 121.40 ?  160  GLN E C   1 
ATOM   15176 O  O   . GLN E 5  160  ? -36.368 -94.907  47.758  1.00 122.08 ?  160  GLN E O   1 
ATOM   15177 C  CB  . GLN E 5  160  ? -35.791 -94.415  44.729  1.00 124.38 ?  160  GLN E CB  1 
ATOM   15178 C  CG  . GLN E 5  160  ? -34.409 -94.100  44.167  1.00 125.40 ?  160  GLN E CG  1 
ATOM   15179 C  CD  . GLN E 5  160  ? -34.452 -93.065  43.057  1.00 127.16 ?  160  GLN E CD  1 
ATOM   15180 O  OE1 . GLN E 5  160  ? -35.514 -92.537  42.723  1.00 127.27 ?  160  GLN E OE1 1 
ATOM   15181 N  NE2 . GLN E 5  160  ? -33.294 -92.773  42.475  1.00 124.96 ?  160  GLN E NE2 1 
ATOM   15182 N  N   . SER E 5  161  ? -34.305 -95.753  47.412  1.00 108.94 ?  161  SER E N   1 
ATOM   15183 C  CA  . SER E 5  161  ? -33.881 -95.616  48.797  1.00 113.34 ?  161  SER E CA  1 
ATOM   15184 C  C   . SER E 5  161  ? -32.936 -94.436  48.978  1.00 110.48 ?  161  SER E C   1 
ATOM   15185 O  O   . SER E 5  161  ? -33.204 -93.530  49.776  1.00 115.32 ?  161  SER E O   1 
ATOM   15186 C  CB  . SER E 5  161  ? -33.223 -96.917  49.269  1.00 116.74 ?  161  SER E CB  1 
ATOM   15187 O  OG  . SER E 5  161  ? -34.140 -98.002  49.218  1.00 121.19 ?  161  SER E OG  1 
ATOM   15188 N  N   . MET E 5  162  ? -31.825 -94.421  48.240  1.00 95.98  ?  162  MET E N   1 
ATOM   15189 C  CA  . MET E 5  162  ? -30.850 -93.343  48.364  1.00 92.05  ?  162  MET E CA  1 
ATOM   15190 C  C   . MET E 5  162  ? -31.354 -92.053  47.729  1.00 84.83  ?  162  MET E C   1 
ATOM   15191 O  O   . MET E 5  162  ? -30.914 -90.962  48.113  1.00 83.00  ?  162  MET E O   1 
ATOM   15192 C  CB  . MET E 5  162  ? -29.528 -93.807  47.755  1.00 96.13  ?  162  MET E CB  1 
ATOM   15193 C  CG  . MET E 5  162  ? -28.402 -92.800  47.718  1.00 89.02  ?  162  MET E CG  1 
ATOM   15194 S  SD  . MET E 5  162  ? -27.714 -92.253  49.295  1.00 82.51  ?  162  MET E SD  1 
ATOM   15195 C  CE  . MET E 5  162  ? -27.190 -90.656  48.675  1.00 96.30  ?  162  MET E CE  1 
ATOM   15196 N  N   . TYR E 5  163  ? -32.252 -92.167  46.748  1.00 85.25  ?  163  TYR E N   1 
ATOM   15197 C  CA  . TYR E 5  163  ? -33.069 -91.079  46.214  1.00 83.99  ?  163  TYR E CA  1 
ATOM   15198 C  C   . TYR E 5  163  ? -32.279 -90.031  45.432  1.00 87.29  ?  163  TYR E C   1 
ATOM   15199 O  O   . TYR E 5  163  ? -32.878 -89.179  44.766  1.00 87.40  ?  163  TYR E O   1 
ATOM   15200 C  CB  . TYR E 5  163  ? -33.854 -90.405  47.344  1.00 78.03  ?  163  TYR E CB  1 
ATOM   15201 C  CG  . TYR E 5  163  ? -35.292 -90.089  46.984  1.00 83.76  ?  163  TYR E CG  1 
ATOM   15202 C  CD1 . TYR E 5  163  ? -36.265 -91.079  47.017  1.00 89.50  ?  163  TYR E CD1 1 
ATOM   15203 C  CD2 . TYR E 5  163  ? -35.677 -88.805  46.615  1.00 78.39  ?  163  TYR E CD2 1 
ATOM   15204 C  CE1 . TYR E 5  163  ? -37.579 -90.802  46.690  1.00 87.44  ?  163  TYR E CE1 1 
ATOM   15205 C  CE2 . TYR E 5  163  ? -36.994 -88.518  46.286  1.00 81.76  ?  163  TYR E CE2 1 
ATOM   15206 C  CZ  . TYR E 5  163  ? -37.938 -89.522  46.327  1.00 85.39  ?  163  TYR E CZ  1 
ATOM   15207 O  OH  . TYR E 5  163  ? -39.247 -89.253  46.004  1.00 90.52  ?  163  TYR E OH  1 
ATOM   15208 N  N   . GLY E 5  164  ? -30.955 -90.067  45.506  1.00 112.40 ?  164  GLY E N   1 
ATOM   15209 C  CA  . GLY E 5  164  ? -30.122 -89.203  44.696  1.00 111.16 ?  164  GLY E CA  1 
ATOM   15210 C  C   . GLY E 5  164  ? -30.051 -87.776  45.215  1.00 109.43 ?  164  GLY E C   1 
ATOM   15211 O  O   . GLY E 5  164  ? -30.908 -87.300  45.957  1.00 111.71 ?  164  GLY E O   1 
ATOM   15212 N  N   . TYR E 5  165  ? -28.994 -87.084  44.797  1.00 95.88  ?  165  TYR E N   1 
ATOM   15213 C  CA  . TYR E 5  165  ? -28.723 -85.707  45.205  1.00 97.43  ?  165  TYR E CA  1 
ATOM   15214 C  C   . TYR E 5  165  ? -28.130 -84.929  44.035  1.00 98.15  ?  165  TYR E C   1 
ATOM   15215 O  O   . TYR E 5  165  ? -27.102 -84.263  44.156  1.00 97.81  ?  165  TYR E O   1 
ATOM   15216 C  CB  . TYR E 5  165  ? -27.787 -85.669  46.411  1.00 89.99  ?  165  TYR E CB  1 
ATOM   15217 C  CG  . TYR E 5  165  ? -28.483 -85.882  47.733  1.00 95.05  ?  165  TYR E CG  1 
ATOM   15218 C  CD1 . TYR E 5  165  ? -28.701 -87.160  48.230  1.00 99.80  ?  165  TYR E CD1 1 
ATOM   15219 C  CD2 . TYR E 5  165  ? -28.919 -84.802  48.488  1.00 99.32  ?  165  TYR E CD2 1 
ATOM   15220 C  CE1 . TYR E 5  165  ? -29.340 -87.356  49.439  1.00 103.76 ?  165  TYR E CE1 1 
ATOM   15221 C  CE2 . TYR E 5  165  ? -29.556 -84.987  49.697  1.00 101.36 ?  165  TYR E CE2 1 
ATOM   15222 C  CZ  . TYR E 5  165  ? -29.764 -86.266  50.168  1.00 102.81 ?  165  TYR E CZ  1 
ATOM   15223 O  OH  . TYR E 5  165  ? -30.400 -86.451  51.372  1.00 91.30  ?  165  TYR E OH  1 
ATOM   15224 N  N   . ALA E 5  166  ? -28.788 -85.004  42.877  1.00 91.04  ?  166  ALA E N   1 
ATOM   15225 C  CA  . ALA E 5  166  ? -28.225 -84.406  41.671  1.00 86.27  ?  166  ALA E CA  1 
ATOM   15226 C  C   . ALA E 5  166  ? -28.383 -82.889  41.677  1.00 81.04  ?  166  ALA E C   1 
ATOM   15227 O  O   . ALA E 5  166  ? -27.431 -82.154  41.390  1.00 74.00  ?  166  ALA E O   1 
ATOM   15228 C  CB  . ALA E 5  166  ? -28.878 -85.017  40.430  1.00 83.57  ?  166  ALA E CB  1 
ATOM   15229 N  N   . SER E 5  167  ? -29.580 -82.401  42.013  1.00 78.63  ?  167  SER E N   1 
ATOM   15230 C  CA  . SER E 5  167  ? -29.875 -80.977  41.890  1.00 73.71  ?  167  SER E CA  1 
ATOM   15231 C  C   . SER E 5  167  ? -29.199 -80.142  42.970  1.00 73.99  ?  167  SER E C   1 
ATOM   15232 O  O   . SER E 5  167  ? -28.851 -78.983  42.722  1.00 78.98  ?  167  SER E O   1 
ATOM   15233 C  CB  . SER E 5  167  ? -31.386 -80.750  41.941  1.00 70.34  ?  167  SER E CB  1 
ATOM   15234 O  OG  . SER E 5  167  ? -31.949 -81.331  43.105  1.00 76.20  ?  167  SER E OG  1 
ATOM   15235 N  N   . ARG E 5  168  ? -28.999 -80.702  44.161  1.00 79.26  ?  168  ARG E N   1 
ATOM   15236 C  CA  . ARG E 5  168  ? -28.506 -79.919  45.284  1.00 71.84  ?  168  ARG E CA  1 
ATOM   15237 C  C   . ARG E 5  168  ? -26.987 -79.802  45.331  1.00 67.76  ?  168  ARG E C   1 
ATOM   15238 O  O   . ARG E 5  168  ? -26.472 -78.921  46.028  1.00 64.88  ?  168  ARG E O   1 
ATOM   15239 C  CB  . ARG E 5  168  ? -29.003 -80.519  46.605  1.00 76.33  ?  168  ARG E CB  1 
ATOM   15240 C  CG  . ARG E 5  168  ? -30.330 -79.954  47.096  1.00 75.32  ?  168  ARG E CG  1 
ATOM   15241 C  CD  . ARG E 5  168  ? -30.983 -80.895  48.097  1.00 72.31  ?  168  ARG E CD  1 
ATOM   15242 N  NE  . ARG E 5  168  ? -31.511 -82.093  47.453  1.00 86.72  ?  168  ARG E NE  1 
ATOM   15243 C  CZ  . ARG E 5  168  ? -32.136 -83.073  48.091  1.00 87.55  ?  168  ARG E CZ  1 
ATOM   15244 N  NH1 . ARG E 5  168  ? -32.335 -83.030  49.398  1.00 85.30  ?  168  ARG E NH1 1 
ATOM   15245 N  NH2 . ARG E 5  168  ? -32.570 -84.124  47.400  1.00 87.66  ?  168  ARG E NH2 1 
ATOM   15246 N  N   . ILE E 5  169  ? -26.252 -80.654  44.620  1.00 55.99  ?  169  ILE E N   1 
ATOM   15247 C  CA  . ILE E 5  169  ? -24.801 -80.720  44.746  1.00 53.45  ?  169  ILE E CA  1 
ATOM   15248 C  C   . ILE E 5  169  ? -24.156 -80.489  43.388  1.00 54.62  ?  169  ILE E C   1 
ATOM   15249 O  O   . ILE E 5  169  ? -24.600 -81.037  42.374  1.00 44.50  ?  169  ILE E O   1 
ATOM   15250 C  CB  . ILE E 5  169  ? -24.340 -82.066  45.342  1.00 45.58  ?  169  ILE E CB  1 
ATOM   15251 C  CG1 . ILE E 5  169  ? -25.122 -82.380  46.618  1.00 41.67  ?  169  ILE E CG1 1 
ATOM   15252 C  CG2 . ILE E 5  169  ? -22.850 -82.042  45.624  1.00 42.67  ?  169  ILE E CG2 1 
ATOM   15253 C  CD1 . ILE E 5  169  ? -24.544 -83.517  47.433  1.00 48.26  ?  169  ILE E CD1 1 
ATOM   15254 N  N   . THR E 5  170  ? -23.099 -79.683  43.382  1.00 74.43  ?  170  THR E N   1 
ATOM   15255 C  CA  . THR E 5  170  ? -22.339 -79.440  42.169  1.00 62.32  ?  170  THR E CA  1 
ATOM   15256 C  C   . THR E 5  170  ? -21.469 -80.654  41.849  1.00 68.85  ?  170  THR E C   1 
ATOM   15257 O  O   . THR E 5  170  ? -20.993 -81.328  42.766  1.00 74.95  ?  170  THR E O   1 
ATOM   15258 C  CB  . THR E 5  170  ? -21.484 -78.181  42.343  1.00 66.19  ?  170  THR E CB  1 
ATOM   15259 O  OG1 . THR E 5  170  ? -22.348 -77.080  42.661  1.00 85.10  ?  170  THR E OG1 1 
ATOM   15260 C  CG2 . THR E 5  170  ? -20.716 -77.867  41.075  1.00 69.94  ?  170  THR E CG2 1 
ATOM   15261 N  N   . PRO E 5  171  ? -21.310 -81.000  40.564  1.00 84.55  ?  171  PRO E N   1 
ATOM   15262 C  CA  . PRO E 5  171  ? -20.472 -82.159  40.215  1.00 79.24  ?  171  PRO E CA  1 
ATOM   15263 C  C   . PRO E 5  171  ? -19.077 -82.147  40.824  1.00 79.10  ?  171  PRO E C   1 
ATOM   15264 O  O   . PRO E 5  171  ? -18.591 -83.207  41.239  1.00 85.49  ?  171  PRO E O   1 
ATOM   15265 C  CB  . PRO E 5  171  ? -20.415 -82.083  38.687  1.00 74.27  ?  171  PRO E CB  1 
ATOM   15266 C  CG  . PRO E 5  171  ? -21.713 -81.491  38.305  1.00 70.45  ?  171  PRO E CG  1 
ATOM   15267 C  CD  . PRO E 5  171  ? -22.060 -80.500  39.393  1.00 73.01  ?  171  PRO E CD  1 
ATOM   15268 N  N   . GLU E 5  172  ? -18.407 -80.992  40.874  1.00 91.88  ?  172  GLU E N   1 
ATOM   15269 C  CA  . GLU E 5  172  ? -17.094 -80.941  41.512  1.00 92.34  ?  172  GLU E CA  1 
ATOM   15270 C  C   . GLU E 5  172  ? -17.196 -81.218  43.007  1.00 95.20  ?  172  GLU E C   1 
ATOM   15271 O  O   . GLU E 5  172  ? -16.324 -81.878  43.584  1.00 92.94  ?  172  GLU E O   1 
ATOM   15272 C  CB  . GLU E 5  172  ? -16.427 -79.589  41.257  1.00 100.68 ?  172  GLU E CB  1 
ATOM   15273 C  CG  . GLU E 5  172  ? -16.007 -79.369  39.815  1.00 111.93 ?  172  GLU E CG  1 
ATOM   15274 C  CD  . GLU E 5  172  ? -17.043 -78.613  39.011  1.00 121.36 ?  172  GLU E CD  1 
ATOM   15275 O  OE1 . GLU E 5  172  ? -17.862 -77.895  39.621  1.00 123.09 ?  172  GLU E OE1 1 
ATOM   15276 O  OE2 . GLU E 5  172  ? -17.035 -78.734  37.768  1.00 122.98 -1 172  GLU E OE2 1 
ATOM   15277 N  N   . ASP E 5  173  ? -18.255 -80.722  43.652  1.00 97.53  ?  173  ASP E N   1 
ATOM   15278 C  CA  . ASP E 5  173  ? -18.484 -81.060  45.052  1.00 91.04  ?  173  ASP E CA  1 
ATOM   15279 C  C   . ASP E 5  173  ? -18.826 -82.535  45.220  1.00 84.43  ?  173  ASP E C   1 
ATOM   15280 O  O   . ASP E 5  173  ? -18.499 -83.130  46.253  1.00 93.92  ?  173  ASP E O   1 
ATOM   15281 C  CB  . ASP E 5  173  ? -19.594 -80.185  45.634  1.00 92.11  ?  173  ASP E CB  1 
ATOM   15282 C  CG  . ASP E 5  173  ? -19.330 -78.703  45.444  1.00 96.62  ?  173  ASP E CG  1 
ATOM   15283 O  OD1 . ASP E 5  173  ? -18.149 -78.321  45.304  1.00 94.69  ?  173  ASP E OD1 1 
ATOM   15284 O  OD2 . ASP E 5  173  ? -20.303 -77.920  45.438  1.00 99.79  -1 173  ASP E OD2 1 
ATOM   15285 N  N   . ARG E 5  174  ? -19.481 -83.139  44.224  1.00 63.91  ?  174  ARG E N   1 
ATOM   15286 C  CA  . ARG E 5  174  ? -19.754 -84.572  44.280  1.00 68.13  ?  174  ARG E CA  1 
ATOM   15287 C  C   . ARG E 5  174  ? -18.461 -85.377  44.253  1.00 70.12  ?  174  ARG E C   1 
ATOM   15288 O  O   . ARG E 5  174  ? -18.321 -86.369  44.980  1.00 68.66  ?  174  ARG E O   1 
ATOM   15289 C  CB  . ARG E 5  174  ? -20.660 -84.985  43.121  1.00 66.70  ?  174  ARG E CB  1 
ATOM   15290 C  CG  . ARG E 5  174  ? -22.142 -84.807  43.388  1.00 73.94  ?  174  ARG E CG  1 
ATOM   15291 C  CD  . ARG E 5  174  ? -22.968 -85.121  42.149  1.00 77.64  ?  174  ARG E CD  1 
ATOM   15292 N  NE  . ARG E 5  174  ? -23.307 -83.922  41.391  1.00 80.39  ?  174  ARG E NE  1 
ATOM   15293 C  CZ  . ARG E 5  174  ? -24.199 -83.885  40.410  1.00 81.01  ?  174  ARG E CZ  1 
ATOM   15294 N  NH1 . ARG E 5  174  ? -24.856 -84.969  40.034  1.00 85.68  ?  174  ARG E NH1 1 
ATOM   15295 N  NH2 . ARG E 5  174  ? -24.441 -82.732  39.794  1.00 79.70  ?  174  ARG E NH2 1 
ATOM   15296 N  N   . TRP E 5  175  ? -17.506 -84.967  43.414  1.00 56.75  ?  175  TRP E N   1 
ATOM   15297 C  CA  . TRP E 5  175  ? -16.208 -85.632  43.394  1.00 61.14  ?  175  TRP E CA  1 
ATOM   15298 C  C   . TRP E 5  175  ? -15.437 -85.388  44.684  1.00 57.99  ?  175  TRP E C   1 
ATOM   15299 O  O   . TRP E 5  175  ? -14.719 -86.277  45.154  1.00 59.73  ?  175  TRP E O   1 
ATOM   15300 C  CB  . TRP E 5  175  ? -15.398 -85.156  42.187  1.00 63.58  ?  175  TRP E CB  1 
ATOM   15301 C  CG  . TRP E 5  175  ? -15.879 -85.719  40.891  1.00 61.74  ?  175  TRP E CG  1 
ATOM   15302 C  CD1 . TRP E 5  175  ? -16.451 -85.030  39.862  1.00 66.61  ?  175  TRP E CD1 1 
ATOM   15303 C  CD2 . TRP E 5  175  ? -15.834 -87.091  40.480  1.00 63.29  ?  175  TRP E CD2 1 
ATOM   15304 N  NE1 . TRP E 5  175  ? -16.765 -85.887  38.836  1.00 69.50  ?  175  TRP E NE1 1 
ATOM   15305 C  CE2 . TRP E 5  175  ? -16.396 -87.159  39.191  1.00 67.16  ?  175  TRP E CE2 1 
ATOM   15306 C  CE3 . TRP E 5  175  ? -15.373 -88.269  41.077  1.00 63.40  ?  175  TRP E CE3 1 
ATOM   15307 C  CZ2 . TRP E 5  175  ? -16.510 -88.356  38.488  1.00 69.88  ?  175  TRP E CZ2 1 
ATOM   15308 C  CZ3 . TRP E 5  175  ? -15.487 -89.459  40.376  1.00 65.34  ?  175  TRP E CZ3 1 
ATOM   15309 C  CH2 . TRP E 5  175  ? -16.050 -89.492  39.096  1.00 69.25  ?  175  TRP E CH2 1 
ATOM   15310 N  N   . ALA E 5  176  ? -15.578 -84.199  45.271  1.00 72.52  ?  176  ALA E N   1 
ATOM   15311 C  CA  . ALA E 5  176  ? -14.950 -83.937  46.560  1.00 73.66  ?  176  ALA E CA  1 
ATOM   15312 C  C   . ALA E 5  176  ? -15.569 -84.795  47.656  1.00 75.10  ?  176  ALA E C   1 
ATOM   15313 O  O   . ALA E 5  176  ? -14.868 -85.245  48.570  1.00 75.49  ?  176  ALA E O   1 
ATOM   15314 C  CB  . ALA E 5  176  ? -15.062 -82.454  46.908  1.00 70.48  ?  176  ALA E CB  1 
ATOM   15315 N  N   . ILE E 5  177  ? -16.881 -85.030  47.582  1.00 66.64  ?  177  ILE E N   1 
ATOM   15316 C  CA  . ILE E 5  177  ? -17.533 -85.917  48.541  1.00 66.54  ?  177  ILE E CA  1 
ATOM   15317 C  C   . ILE E 5  177  ? -17.025 -87.344  48.373  1.00 67.20  ?  177  ILE E C   1 
ATOM   15318 O  O   . ILE E 5  177  ? -16.784 -88.053  49.357  1.00 68.93  ?  177  ILE E O   1 
ATOM   15319 C  CB  . ILE E 5  177  ? -19.063 -85.836  48.388  1.00 59.92  ?  177  ILE E CB  1 
ATOM   15320 C  CG1 . ILE E 5  177  ? -19.589 -84.512  48.944  1.00 55.82  ?  177  ILE E CG1 1 
ATOM   15321 C  CG2 . ILE E 5  177  ? -19.742 -87.005  49.088  1.00 62.36  ?  177  ILE E CG2 1 
ATOM   15322 C  CD1 . ILE E 5  177  ? -21.091 -84.362  48.831  1.00 57.15  ?  177  ILE E CD1 1 
ATOM   15323 N  N   . ALA E 5  178  ? -16.847 -87.785  47.125  1.00 74.04  ?  178  ALA E N   1 
ATOM   15324 C  CA  . ALA E 5  178  ? -16.319 -89.124  46.884  1.00 77.04  ?  178  ALA E CA  1 
ATOM   15325 C  C   . ALA E 5  178  ? -14.892 -89.253  47.401  1.00 81.01  ?  178  ALA E C   1 
ATOM   15326 O  O   . ALA E 5  178  ? -14.504 -90.308  47.916  1.00 89.85  ?  178  ALA E O   1 
ATOM   15327 C  CB  . ALA E 5  178  ? -16.383 -89.454  45.393  1.00 77.57  ?  178  ALA E CB  1 
ATOM   15328 N  N   . ALA E 5  179  ? -14.097 -88.189  47.275  1.00 79.01  ?  179  ALA E N   1 
ATOM   15329 C  CA  . ALA E 5  179  ? -12.738 -88.219  47.805  1.00 80.62  ?  179  ALA E CA  1 
ATOM   15330 C  C   . ALA E 5  179  ? -12.743 -88.263  49.328  1.00 84.62  ?  179  ALA E C   1 
ATOM   15331 O  O   . ALA E 5  179  ? -11.898 -88.930  49.938  1.00 79.69  ?  179  ALA E O   1 
ATOM   15332 C  CB  . ALA E 5  179  ? -11.952 -87.009  47.302  1.00 80.42  ?  179  ALA E CB  1 
ATOM   15333 N  N   . TYR E 5  180  ? -13.689 -87.563  49.960  1.00 85.67  ?  180  TYR E N   1 
ATOM   15334 C  CA  . TYR E 5  180  ? -13.788 -87.605  51.415  1.00 84.14  ?  180  TYR E CA  1 
ATOM   15335 C  C   . TYR E 5  180  ? -14.281 -88.959  51.907  1.00 80.38  ?  180  TYR E C   1 
ATOM   15336 O  O   . TYR E 5  180  ? -13.893 -89.398  52.996  1.00 87.86  ?  180  TYR E O   1 
ATOM   15337 C  CB  . TYR E 5  180  ? -14.707 -86.492  51.916  1.00 85.32  ?  180  TYR E CB  1 
ATOM   15338 C  CG  . TYR E 5  180  ? -14.816 -86.427  53.422  1.00 80.31  ?  180  TYR E CG  1 
ATOM   15339 C  CD1 . TYR E 5  180  ? -13.698 -86.184  54.209  1.00 79.24  ?  180  TYR E CD1 1 
ATOM   15340 C  CD2 . TYR E 5  180  ? -16.037 -86.610  54.057  1.00 74.50  ?  180  TYR E CD2 1 
ATOM   15341 C  CE1 . TYR E 5  180  ? -13.793 -86.127  55.586  1.00 88.74  ?  180  TYR E CE1 1 
ATOM   15342 C  CE2 . TYR E 5  180  ? -16.142 -86.551  55.432  1.00 84.07  ?  180  TYR E CE2 1 
ATOM   15343 C  CZ  . TYR E 5  180  ? -15.018 -86.311  56.192  1.00 93.88  ?  180  TYR E CZ  1 
ATOM   15344 O  OH  . TYR E 5  180  ? -15.119 -86.252  57.564  1.00 98.62  ?  180  TYR E OH  1 
ATOM   15345 N  N   . ILE E 5  181  ? -15.139 -89.627  51.132  1.00 52.22  ?  181  ILE E N   1 
ATOM   15346 C  CA  . ILE E 5  181  ? -15.564 -90.978  51.488  1.00 52.36  ?  181  ILE E CA  1 
ATOM   15347 C  C   . ILE E 5  181  ? -14.371 -91.923  51.474  1.00 61.39  ?  181  ILE E C   1 
ATOM   15348 O  O   . ILE E 5  181  ? -14.234 -92.793  52.344  1.00 61.18  ?  181  ILE E O   1 
ATOM   15349 C  CB  . ILE E 5  181  ? -16.679 -91.456  50.538  1.00 56.46  ?  181  ILE E CB  1 
ATOM   15350 C  CG1 . ILE E 5  181  ? -17.982 -90.711  50.824  1.00 55.07  ?  181  ILE E CG1 1 
ATOM   15351 C  CG2 . ILE E 5  181  ? -16.894 -92.957  50.667  1.00 59.94  ?  181  ILE E CG2 1 
ATOM   15352 C  CD1 . ILE E 5  181  ? -19.132 -91.167  49.959  1.00 62.95  ?  181  ILE E CD1 1 
ATOM   15353 N  N   . ARG E 5  182  ? -13.484 -91.761  50.489  1.00 93.86  ?  182  ARG E N   1 
ATOM   15354 C  CA  . ARG E 5  182  ? -12.258 -92.551  50.455  1.00 97.59  ?  182  ARG E CA  1 
ATOM   15355 C  C   . ARG E 5  182  ? -11.371 -92.239  51.654  1.00 97.98  ?  182  ARG E C   1 
ATOM   15356 O  O   . ARG E 5  182  ? -10.735 -93.137  52.217  1.00 92.63  ?  182  ARG E O   1 
ATOM   15357 C  CB  . ARG E 5  182  ? -11.504 -92.289  49.152  1.00 96.21  ?  182  ARG E CB  1 
ATOM   15358 C  CG  . ARG E 5  182  ? -11.901 -93.196  48.003  1.00 96.76  ?  182  ARG E CG  1 
ATOM   15359 C  CD  . ARG E 5  182  ? -11.440 -94.620  48.241  1.00 106.88 ?  182  ARG E CD  1 
ATOM   15360 N  NE  . ARG E 5  182  ? -11.762 -95.487  47.114  1.00 120.21 ?  182  ARG E NE  1 
ATOM   15361 C  CZ  . ARG E 5  182  ? -12.756 -96.363  47.101  1.00 116.07 ?  182  ARG E CZ  1 
ATOM   15362 N  NH1 . ARG E 5  182  ? -13.555 -96.519  48.144  1.00 117.48 ?  182  ARG E NH1 1 
ATOM   15363 N  NH2 . ARG E 5  182  ? -12.955 -97.102  46.013  1.00 108.74 ?  182  ARG E NH2 1 
ATOM   15364 N  N   . ALA E 5  183  ? -11.314 -90.966  52.057  1.00 80.39  ?  183  ALA E N   1 
ATOM   15365 C  CA  . ALA E 5  183  ? -10.518 -90.594  53.222  1.00 75.17  ?  183  ALA E CA  1 
ATOM   15366 C  C   . ALA E 5  183  ? -11.109 -91.175  54.501  1.00 76.47  ?  183  ALA E C   1 
ATOM   15367 O  O   . ALA E 5  183  ? -10.368 -91.590  55.400  1.00 77.78  ?  183  ALA E O   1 
ATOM   15368 C  CB  . ALA E 5  183  ? -10.408 -89.073  53.320  1.00 79.02  ?  183  ALA E CB  1 
ATOM   15369 N  N   . LEU E 5  184  ? -12.440 -91.212  54.601  1.00 67.96  ?  184  LEU E N   1 
ATOM   15370 C  CA  . LEU E 5  184  ? -13.076 -91.835  55.757  1.00 68.54  ?  184  LEU E CA  1 
ATOM   15371 C  C   . LEU E 5  184  ? -12.815 -93.335  55.785  1.00 68.86  ?  184  LEU E C   1 
ATOM   15372 O  O   . LEU E 5  184  ? -12.584 -93.911  56.855  1.00 72.22  ?  184  LEU E O   1 
ATOM   15373 C  CB  . LEU E 5  184  ? -14.578 -91.558  55.747  1.00 61.46  ?  184  LEU E CB  1 
ATOM   15374 C  CG  . LEU E 5  184  ? -15.027 -90.160  56.170  1.00 58.12  ?  184  LEU E CG  1 
ATOM   15375 C  CD1 . LEU E 5  184  ? -16.525 -90.001  55.964  1.00 53.25  ?  184  LEU E CD1 1 
ATOM   15376 C  CD2 . LEU E 5  184  ? -14.649 -89.899  57.617  1.00 66.41  ?  184  LEU E CD2 1 
ATOM   15377 N  N   . GLN E 5  185  ? -12.850 -93.984  54.619  1.00 88.17  ?  185  GLN E N   1 
ATOM   15378 C  CA  . GLN E 5  185  ? -12.582 -95.417  54.560  1.00 90.12  ?  185  GLN E CA  1 
ATOM   15379 C  C   . GLN E 5  185  ? -11.151 -95.724  54.984  1.00 92.23  ?  185  GLN E C   1 
ATOM   15380 O  O   . GLN E 5  185  ? -10.889 -96.756  55.613  1.00 92.60  ?  185  GLN E O   1 
ATOM   15381 C  CB  . GLN E 5  185  ? -12.855 -95.941  53.150  1.00 88.56  ?  185  GLN E CB  1 
ATOM   15382 C  CG  . GLN E 5  185  ? -14.305 -96.334  52.907  1.00 91.70  ?  185  GLN E CG  1 
ATOM   15383 C  CD  . GLN E 5  185  ? -14.553 -96.821  51.491  1.00 88.94  ?  185  GLN E CD  1 
ATOM   15384 O  OE1 . GLN E 5  185  ? -13.709 -96.661  50.610  1.00 91.60  ?  185  GLN E OE1 1 
ATOM   15385 N  NE2 . GLN E 5  185  ? -15.720 -97.413  51.266  1.00 91.63  ?  185  GLN E NE2 1 
ATOM   15386 N  N   . LEU E 5  186  ? -10.211 -94.835  54.652  1.00 81.76  ?  186  LEU E N   1 
ATOM   15387 C  CA  . LEU E 5  186  ? -8.831  -95.019  55.088  1.00 73.04  ?  186  LEU E CA  1 
ATOM   15388 C  C   . LEU E 5  186  ? -8.684  -94.738  56.577  1.00 75.83  ?  186  LEU E C   1 
ATOM   15389 O  O   . LEU E 5  186  ? -7.949  -95.443  57.278  1.00 81.97  ?  186  LEU E O   1 
ATOM   15390 C  CB  . LEU E 5  186  ? -7.898  -94.116  54.280  1.00 73.79  ?  186  LEU E CB  1 
ATOM   15391 C  CG  . LEU E 5  186  ? -6.508  -93.870  54.877  1.00 69.20  ?  186  LEU E CG  1 
ATOM   15392 C  CD1 . LEU E 5  186  ? -5.678  -95.146  54.868  1.00 68.76  ?  186  LEU E CD1 1 
ATOM   15393 C  CD2 . LEU E 5  186  ? -5.785  -92.746  54.147  1.00 82.83  ?  186  LEU E CD2 1 
ATOM   15394 N  N   . SER E 5  187  ? -9.381  -93.716  57.080  1.00 123.69 ?  187  SER E N   1 
ATOM   15395 C  CA  . SER E 5  187  ? -9.270  -93.357  58.488  1.00 128.07 ?  187  SER E CA  1 
ATOM   15396 C  C   . SER E 5  187  ? -9.781  -94.456  59.409  1.00 122.41 ?  187  SER E C   1 
ATOM   15397 O  O   . SER E 5  187  ? -9.473  -94.439  60.606  1.00 127.49 ?  187  SER E O   1 
ATOM   15398 C  CB  . SER E 5  187  ? -10.026 -92.056  58.760  1.00 128.05 ?  187  SER E CB  1 
ATOM   15399 O  OG  . SER E 5  187  ? -11.426 -92.252  58.668  1.00 123.30 ?  187  SER E OG  1 
ATOM   15400 N  N   . GLN E 5  188  ? -10.552 -95.408  58.884  1.00 69.74  ?  188  GLN E N   1 
ATOM   15401 C  CA  . GLN E 5  188  ? -11.054 -96.532  59.661  1.00 71.06  ?  188  GLN E CA  1 
ATOM   15402 C  C   . GLN E 5  188  ? -10.298 -97.824  59.367  1.00 76.08  ?  188  GLN E C   1 
ATOM   15403 O  O   . GLN E 5  188  ? -10.815 -98.913  59.639  1.00 80.44  ?  188  GLN E O   1 
ATOM   15404 C  CB  . GLN E 5  188  ? -12.549 -96.720  59.406  1.00 66.19  ?  188  GLN E CB  1 
ATOM   15405 C  CG  . GLN E 5  188  ? -13.399 -95.515  59.779  1.00 58.54  ?  188  GLN E CG  1 
ATOM   15406 C  CD  . GLN E 5  188  ? -13.180 -95.059  61.208  1.00 60.71  ?  188  GLN E CD  1 
ATOM   15407 O  OE1 . GLN E 5  188  ? -13.784 -95.591  62.138  1.00 60.84  ?  188  GLN E OE1 1 
ATOM   15408 N  NE2 . GLN E 5  188  ? -12.324 -94.060  61.389  1.00 62.07  ?  188  GLN E NE2 1 
ATOM   15409 N  N   . ASN E 5  189  ? -9.091  -97.723  58.820  1.00 91.05  ?  189  ASN E N   1 
ATOM   15410 C  CA  . ASN E 5  189  ? -8.271  -98.895  58.530  1.00 90.87  ?  189  ASN E CA  1 
ATOM   15411 C  C   . ASN E 5  189  ? -6.859  -98.721  59.083  1.00 83.14  ?  189  ASN E C   1 
ATOM   15412 O  O   . ASN E 5  189  ? -5.951  -98.286  58.375  1.00 77.47  ?  189  ASN E O   1 
ATOM   15413 C  CB  . ASN E 5  189  ? -8.221  -99.158  57.022  1.00 76.01  ?  189  ASN E CB  1 
ATOM   15414 C  CG  . ASN E 5  189  ? -9.277  -100.148 56.568  1.00 83.34  ?  189  ASN E CG  1 
ATOM   15415 O  OD1 . ASN E 5  189  ? -9.899  -100.828 57.383  1.00 91.96  ?  189  ASN E OD1 1 
ATOM   15416 N  ND2 . ASN E 5  189  ? -9.484  -100.233 55.259  1.00 98.96  ?  189  ASN E ND2 1 
ATOM   15417 N  N   . ILE F 6  11   ? -29.333 25.619   71.986  1.00 168.02 ?  11   ILE F N   1 
ATOM   15418 C  CA  . ILE F 6  11   ? -28.587 26.376   70.985  1.00 169.97 ?  11   ILE F CA  1 
ATOM   15419 C  C   . ILE F 6  11   ? -27.071 26.366   71.255  1.00 171.40 ?  11   ILE F C   1 
ATOM   15420 O  O   . ILE F 6  11   ? -26.295 26.157   70.322  1.00 171.71 ?  11   ILE F O   1 
ATOM   15421 C  CB  . ILE F 6  11   ? -29.124 27.821   70.872  1.00 162.16 ?  11   ILE F CB  1 
ATOM   15422 C  CG1 . ILE F 6  11   ? -30.628 27.809   70.596  1.00 162.43 ?  11   ILE F CG1 1 
ATOM   15423 C  CG2 . ILE F 6  11   ? -28.389 28.582   69.779  1.00 155.85 ?  11   ILE F CG2 1 
ATOM   15424 C  CD1 . ILE F 6  11   ? -31.013 27.063   69.338  1.00 161.80 ?  11   ILE F CD1 1 
ATOM   15425 N  N   . PRO F 6  12   ? -26.633 26.592   72.505  1.00 197.64 ?  12   PRO F N   1 
ATOM   15426 C  CA  . PRO F 6  12   ? -25.190 26.454   72.776  1.00 197.39 ?  12   PRO F CA  1 
ATOM   15427 C  C   . PRO F 6  12   ? -24.678 25.042   72.560  1.00 198.69 ?  12   PRO F C   1 
ATOM   15428 O  O   . PRO F 6  12   ? -23.539 24.863   72.109  1.00 198.75 ?  12   PRO F O   1 
ATOM   15429 C  CB  . PRO F 6  12   ? -25.058 26.891   74.244  1.00 201.73 ?  12   PRO F CB  1 
ATOM   15430 C  CG  . PRO F 6  12   ? -26.426 26.798   74.807  1.00 201.13 ?  12   PRO F CG  1 
ATOM   15431 C  CD  . PRO F 6  12   ? -27.342 27.131   73.681  1.00 202.90 ?  12   PRO F CD  1 
ATOM   15432 N  N   . GLN F 6  13   ? -25.489 24.030   72.877  1.00 215.88 ?  13   GLN F N   1 
ATOM   15433 C  CA  . GLN F 6  13   ? -25.083 22.653   72.614  1.00 212.39 ?  13   GLN F CA  1 
ATOM   15434 C  C   . GLN F 6  13   ? -24.943 22.402   71.119  1.00 213.55 ?  13   GLN F C   1 
ATOM   15435 O  O   . GLN F 6  13   ? -24.073 21.636   70.689  1.00 214.89 ?  13   GLN F O   1 
ATOM   15436 C  CB  . GLN F 6  13   ? -26.088 21.678   73.230  1.00 203.93 ?  13   GLN F CB  1 
ATOM   15437 C  CG  . GLN F 6  13   ? -26.398 21.940   74.694  1.00 215.77 ?  13   GLN F CG  1 
ATOM   15438 C  CD  . GLN F 6  13   ? -27.612 22.827   74.882  1.00 221.32 ?  13   GLN F CD  1 
ATOM   15439 O  OE1 . GLN F 6  13   ? -28.460 22.935   73.996  1.00 215.55 ?  13   GLN F OE1 1 
ATOM   15440 N  NE2 . GLN F 6  13   ? -27.702 23.469   76.041  1.00 217.86 ?  13   GLN F NE2 1 
ATOM   15441 N  N   . LEU F 6  14   ? -25.793 23.041   70.311  1.00 122.36 ?  14   LEU F N   1 
ATOM   15442 C  CA  . LEU F 6  14   ? -25.672 22.916   68.863  1.00 112.42 ?  14   LEU F CA  1 
ATOM   15443 C  C   . LEU F 6  14   ? -24.387 23.563   68.362  1.00 118.69 ?  14   LEU F C   1 
ATOM   15444 O  O   . LEU F 6  14   ? -23.765 23.069   67.413  1.00 115.33 ?  14   LEU F O   1 
ATOM   15445 C  CB  . LEU F 6  14   ? -26.890 23.539   68.181  1.00 109.17 ?  14   LEU F CB  1 
ATOM   15446 C  CG  . LEU F 6  14   ? -28.209 22.778   68.320  1.00 104.13 ?  14   LEU F CG  1 
ATOM   15447 C  CD1 . LEU F 6  14   ? -29.373 23.627   67.831  1.00 109.66 ?  14   LEU F CD1 1 
ATOM   15448 C  CD2 . LEU F 6  14   ? -28.149 21.458   67.569  1.00 107.74 ?  14   LEU F CD2 1 
ATOM   15449 N  N   . GLY F 6  15   ? -23.975 24.668   68.985  1.00 209.66 ?  15   GLY F N   1 
ATOM   15450 C  CA  . GLY F 6  15   ? -22.722 25.297   68.602  1.00 208.63 ?  15   GLY F CA  1 
ATOM   15451 C  C   . GLY F 6  15   ? -21.514 24.463   68.985  1.00 204.97 ?  15   GLY F C   1 
ATOM   15452 O  O   . GLY F 6  15   ? -20.522 24.419   68.252  1.00 207.46 ?  15   GLY F O   1 
ATOM   15453 N  N   . GLN F 6  16   ? -21.579 23.793   70.138  1.00 170.58 ?  16   GLN F N   1 
ATOM   15454 C  CA  . GLN F 6  16   ? -20.507 22.881   70.525  1.00 171.04 ?  16   GLN F CA  1 
ATOM   15455 C  C   . GLN F 6  16   ? -20.424 21.697   69.570  1.00 172.16 ?  16   GLN F C   1 
ATOM   15456 O  O   . GLN F 6  16   ? -19.325 21.268   69.198  1.00 169.76 ?  16   GLN F O   1 
ATOM   15457 C  CB  . GLN F 6  16   ? -20.720 22.403   71.962  1.00 177.92 ?  16   GLN F CB  1 
ATOM   15458 C  CG  . GLN F 6  16   ? -19.862 21.212   72.361  1.00 179.34 ?  16   GLN F CG  1 
ATOM   15459 C  CD  . GLN F 6  16   ? -20.558 20.297   73.349  1.00 180.03 ?  16   GLN F CD  1 
ATOM   15460 O  OE1 . GLN F 6  16   ? -21.749 20.449   73.621  1.00 179.24 ?  16   GLN F OE1 1 
ATOM   15461 N  NE2 . GLN F 6  16   ? -19.817 19.338   73.891  1.00 183.74 ?  16   GLN F NE2 1 
ATOM   15462 N  N   . VAL F 6  17   ? -21.576 21.160   69.162  1.00 133.81 ?  17   VAL F N   1 
ATOM   15463 C  CA  . VAL F 6  17   ? -21.592 20.079   68.179  1.00 127.27 ?  17   VAL F CA  1 
ATOM   15464 C  C   . VAL F 6  17   ? -21.032 20.565   66.849  1.00 122.69 ?  17   VAL F C   1 
ATOM   15465 O  O   . VAL F 6  17   ? -20.304 19.838   66.160  1.00 118.88 ?  17   VAL F O   1 
ATOM   15466 C  CB  . VAL F 6  17   ? -23.020 19.519   68.028  1.00 124.22 ?  17   VAL F CB  1 
ATOM   15467 C  CG1 . VAL F 6  17   ? -23.123 18.612   66.811  1.00 116.23 ?  17   VAL F CG1 1 
ATOM   15468 C  CG2 . VAL F 6  17   ? -23.434 18.770   69.288  1.00 124.32 ?  17   VAL F CG2 1 
ATOM   15469 N  N   . GLN F 6  18   ? -21.352 21.805   66.472  1.00 173.98 ?  18   GLN F N   1 
ATOM   15470 C  CA  . GLN F 6  18   ? -20.826 22.364   65.231  1.00 172.40 ?  18   GLN F CA  1 
ATOM   15471 C  C   . GLN F 6  18   ? -19.309 22.498   65.285  1.00 172.03 ?  18   GLN F C   1 
ATOM   15472 O  O   . GLN F 6  18   ? -18.617 22.206   64.302  1.00 167.82 ?  18   GLN F O   1 
ATOM   15473 C  CB  . GLN F 6  18   ? -21.474 23.720   64.952  1.00 169.29 ?  18   GLN F CB  1 
ATOM   15474 C  CG  . GLN F 6  18   ? -21.297 24.213   63.526  1.00 165.23 ?  18   GLN F CG  1 
ATOM   15475 C  CD  . GLN F 6  18   ? -20.150 25.195   63.387  1.00 169.97 ?  18   GLN F CD  1 
ATOM   15476 O  OE1 . GLN F 6  18   ? -19.459 25.501   64.359  1.00 166.77 ?  18   GLN F OE1 1 
ATOM   15477 N  NE2 . GLN F 6  18   ? -19.942 25.695   62.174  1.00 174.00 ?  18   GLN F NE2 1 
ATOM   15478 N  N   . MET F 6  19   ? -18.774 22.939   66.426  1.00 187.25 ?  19   MET F N   1 
ATOM   15479 C  CA  . MET F 6  19   ? -17.327 23.068   66.562  1.00 186.06 ?  19   MET F CA  1 
ATOM   15480 C  C   . MET F 6  19   ? -16.647 21.704   66.543  1.00 185.57 ?  19   MET F C   1 
ATOM   15481 O  O   . MET F 6  19   ? -15.568 21.550   65.959  1.00 186.64 ?  19   MET F O   1 
ATOM   15482 C  CB  . MET F 6  19   ? -16.985 23.822   67.847  1.00 186.67 ?  19   MET F CB  1 
ATOM   15483 C  CG  . MET F 6  19   ? -17.096 25.335   67.731  1.00 193.68 ?  19   MET F CG  1 
ATOM   15484 S  SD  . MET F 6  19   ? -15.618 26.095   67.031  1.00 205.45 ?  19   MET F SD  1 
ATOM   15485 C  CE  . MET F 6  19   ? -16.328 27.052   65.695  1.00 192.73 ?  19   MET F CE  1 
ATOM   15486 N  N   . LEU F 6  20   ? -17.262 20.703   67.179  1.00 146.17 ?  20   LEU F N   1 
ATOM   15487 C  CA  . LEU F 6  20   ? -16.697 19.357   67.158  1.00 140.78 ?  20   LEU F CA  1 
ATOM   15488 C  C   . LEU F 6  20   ? -16.720 18.772   65.752  1.00 135.72 ?  20   LEU F C   1 
ATOM   15489 O  O   . LEU F 6  20   ? -15.760 18.116   65.331  1.00 137.55 ?  20   LEU F O   1 
ATOM   15490 C  CB  . LEU F 6  20   ? -17.457 18.452   68.128  1.00 143.03 ?  20   LEU F CB  1 
ATOM   15491 C  CG  . LEU F 6  20   ? -17.255 18.713   69.622  1.00 148.00 ?  20   LEU F CG  1 
ATOM   15492 C  CD1 . LEU F 6  20   ? -18.084 17.747   70.456  1.00 142.64 ?  20   LEU F CD1 1 
ATOM   15493 C  CD2 . LEU F 6  20   ? -15.783 18.615   69.990  1.00 146.31 ?  20   LEU F CD2 1 
ATOM   15494 N  N   . GLY F 6  21   ? -17.806 19.000   65.012  1.00 136.23 ?  21   GLY F N   1 
ATOM   15495 C  CA  . GLY F 6  21   ? -17.870 18.512   63.644  1.00 131.09 ?  21   GLY F CA  1 
ATOM   15496 C  C   . GLY F 6  21   ? -16.867 19.196   62.735  1.00 134.33 ?  21   GLY F C   1 
ATOM   15497 O  O   . GLY F 6  21   ? -16.304 18.568   61.834  1.00 132.01 ?  21   GLY F O   1 
ATOM   15498 N  N   . LEU F 6  22   ? -16.629 20.491   62.957  1.00 131.34 ?  22   LEU F N   1 
ATOM   15499 C  CA  . LEU F 6  22   ? -15.622 21.200   62.175  1.00 128.82 ?  22   LEU F CA  1 
ATOM   15500 C  C   . LEU F 6  22   ? -14.223 20.679   62.477  1.00 129.90 ?  22   LEU F C   1 
ATOM   15501 O  O   . LEU F 6  22   ? -13.395 20.545   61.568  1.00 126.43 ?  22   LEU F O   1 
ATOM   15502 C  CB  . LEU F 6  22   ? -15.704 22.701   62.449  1.00 128.10 ?  22   LEU F CB  1 
ATOM   15503 C  CG  . LEU F 6  22   ? -16.724 23.498   61.635  1.00 133.81 ?  22   LEU F CG  1 
ATOM   15504 C  CD1 . LEU F 6  22   ? -16.614 24.982   61.948  1.00 138.07 ?  22   LEU F CD1 1 
ATOM   15505 C  CD2 . LEU F 6  22   ? -16.538 23.245   60.146  1.00 133.59 ?  22   LEU F CD2 1 
ATOM   15506 N  N   . ALA F 6  23   ? -13.941 20.382   63.748  1.00 149.50 ?  23   ALA F N   1 
ATOM   15507 C  CA  . ALA F 6  23   ? -12.629 19.858   64.111  1.00 147.17 ?  23   ALA F CA  1 
ATOM   15508 C  C   . ALA F 6  23   ? -12.413 18.464   63.538  1.00 146.39 ?  23   ALA F C   1 
ATOM   15509 O  O   . ALA F 6  23   ? -11.313 18.141   63.075  1.00 147.47 ?  23   ALA F O   1 
ATOM   15510 C  CB  . ALA F 6  23   ? -12.470 19.847   65.631  1.00 141.24 ?  23   ALA F CB  1 
ATOM   15511 N  N   . ALA F 6  24   ? -13.449 17.623   63.562  1.00 149.12 ?  24   ALA F N   1 
ATOM   15512 C  CA  . ALA F 6  24   ? -13.326 16.290   62.982  1.00 146.60 ?  24   ALA F CA  1 
ATOM   15513 C  C   . ALA F 6  24   ? -13.188 16.361   61.467  1.00 145.52 ?  24   ALA F C   1 
ATOM   15514 O  O   . ALA F 6  24   ? -12.484 15.543   60.863  1.00 147.87 ?  24   ALA F O   1 
ATOM   15515 C  CB  . ALA F 6  24   ? -14.529 15.432   63.374  1.00 141.40 ?  24   ALA F CB  1 
ATOM   15516 N  N   . ALA F 6  25   ? -13.845 17.337   60.836  1.00 106.06 ?  25   ALA F N   1 
ATOM   15517 C  CA  . ALA F 6  25   ? -13.767 17.462   59.385  1.00 97.61  ?  25   ALA F CA  1 
ATOM   15518 C  C   . ALA F 6  25   ? -12.392 17.947   58.942  1.00 105.54 ?  25   ALA F C   1 
ATOM   15519 O  O   . ALA F 6  25   ? -11.830 17.427   57.971  1.00 102.15 ?  25   ALA F O   1 
ATOM   15520 C  CB  . ALA F 6  25   ? -14.858 18.406   58.880  1.00 91.10  ?  25   ALA F CB  1 
ATOM   15521 N  N   . VAL F 6  26   ? -11.831 18.937   59.640  1.00 118.60 ?  26   VAL F N   1 
ATOM   15522 C  CA  . VAL F 6  26   ? -10.532 19.469   59.241  1.00 118.45 ?  26   VAL F CA  1 
ATOM   15523 C  C   . VAL F 6  26   ? -9.420  18.466   59.532  1.00 120.10 ?  26   VAL F C   1 
ATOM   15524 O  O   . VAL F 6  26   ? -8.422  18.409   58.803  1.00 118.06 ?  26   VAL F O   1 
ATOM   15525 C  CB  . VAL F 6  26   ? -10.274 20.829   59.921  1.00 113.69 ?  26   VAL F CB  1 
ATOM   15526 C  CG1 . VAL F 6  26   ? -10.123 20.669   61.426  1.00 115.11 ?  26   VAL F CG1 1 
ATOM   15527 C  CG2 . VAL F 6  26   ? -9.046  21.503   59.322  1.00 104.93 ?  26   VAL F CG2 1 
ATOM   15528 N  N   . ILE F 6  27   ? -9.569  17.654   60.582  1.00 139.77 ?  27   ILE F N   1 
ATOM   15529 C  CA  . ILE F 6  27   ? -8.579  16.616   60.855  1.00 142.91 ?  27   ILE F CA  1 
ATOM   15530 C  C   . ILE F 6  27   ? -8.639  15.534   59.785  1.00 145.96 ?  27   ILE F C   1 
ATOM   15531 O  O   . ILE F 6  27   ? -7.605  15.093   59.269  1.00 149.81 ?  27   ILE F O   1 
ATOM   15532 C  CB  . ILE F 6  27   ? -8.782  16.034   62.266  1.00 139.67 ?  27   ILE F CB  1 
ATOM   15533 C  CG1 . ILE F 6  27   ? -8.298  17.022   63.330  1.00 133.22 ?  27   ILE F CG1 1 
ATOM   15534 C  CG2 . ILE F 6  27   ? -8.064  14.697   62.407  1.00 130.60 ?  27   ILE F CG2 1 
ATOM   15535 C  CD1 . ILE F 6  27   ? -8.593  16.587   64.746  1.00 123.80 ?  27   ILE F CD1 1 
ATOM   15536 N  N   . GLY F 6  28   ? -9.848  15.102   59.425  1.00 170.55 ?  28   GLY F N   1 
ATOM   15537 C  CA  . GLY F 6  28   ? -9.984  14.074   58.406  1.00 159.40 ?  28   GLY F CA  1 
ATOM   15538 C  C   . GLY F 6  28   ? -9.502  14.527   57.042  1.00 166.20 ?  28   GLY F C   1 
ATOM   15539 O  O   . GLY F 6  28   ? -8.854  13.765   56.321  1.00 170.41 ?  28   GLY F O   1 
ATOM   15540 N  N   . ILE F 6  29   ? -9.812  15.771   56.667  1.00 145.12 ?  29   ILE F N   1 
ATOM   15541 C  CA  . ILE F 6  29   ? -9.355  16.295   55.383  1.00 145.94 ?  29   ILE F CA  1 
ATOM   15542 C  C   . ILE F 6  29   ? -7.837  16.428   55.369  1.00 150.50 ?  29   ILE F C   1 
ATOM   15543 O  O   . ILE F 6  29   ? -7.186  16.174   54.348  1.00 149.92 ?  29   ILE F O   1 
ATOM   15544 C  CB  . ILE F 6  29   ? -10.052 17.635   55.078  1.00 150.46 ?  29   ILE F CB  1 
ATOM   15545 C  CG1 . ILE F 6  29   ? -11.544 17.417   54.814  1.00 146.44 ?  29   ILE F CG1 1 
ATOM   15546 C  CG2 . ILE F 6  29   ? -9.403  18.332   53.889  1.00 148.84 ?  29   ILE F CG2 1 
ATOM   15547 C  CD1 . ILE F 6  29   ? -11.832 16.377   53.753  1.00 133.39 ?  29   ILE F CD1 1 
ATOM   15548 N  N   . GLY F 6  30   ? -7.247  16.810   56.503  1.00 182.43 ?  30   GLY F N   1 
ATOM   15549 C  CA  . GLY F 6  30   ? -5.801  16.965   56.557  1.00 184.48 ?  30   GLY F CA  1 
ATOM   15550 C  C   . GLY F 6  30   ? -5.064  15.653   56.365  1.00 186.31 ?  30   GLY F C   1 
ATOM   15551 O  O   . GLY F 6  30   ? -4.133  15.562   55.560  1.00 196.08 ?  30   GLY F O   1 
ATOM   15552 N  N   . VAL F 6  31   ? -5.468  14.617   57.105  1.00 141.47 ?  31   VAL F N   1 
ATOM   15553 C  CA  . VAL F 6  31   ? -4.823  13.316   56.960  1.00 142.50 ?  31   VAL F CA  1 
ATOM   15554 C  C   . VAL F 6  31   ? -5.195  12.677   55.625  1.00 146.88 ?  31   VAL F C   1 
ATOM   15555 O  O   . VAL F 6  31   ? -4.421  11.887   55.070  1.00 145.65 ?  31   VAL F O   1 
ATOM   15556 C  CB  . VAL F 6  31   ? -5.176  12.414   58.160  1.00 135.63 ?  31   VAL F CB  1 
ATOM   15557 C  CG1 . VAL F 6  31   ? -6.676  12.246   58.283  1.00 135.86 ?  31   VAL F CG1 1 
ATOM   15558 C  CG2 . VAL F 6  31   ? -4.485  11.060   58.052  1.00 136.76 ?  31   VAL F CG2 1 
ATOM   15559 N  N   . LEU F 6  32   ? -6.366  13.016   55.077  1.00 189.64 ?  32   LEU F N   1 
ATOM   15560 C  CA  . LEU F 6  32   ? -6.713  12.548   53.738  1.00 187.95 ?  32   LEU F CA  1 
ATOM   15561 C  C   . LEU F 6  32   ? -5.797  13.164   52.689  1.00 186.66 ?  32   LEU F C   1 
ATOM   15562 O  O   . LEU F 6  32   ? -5.364  12.478   51.755  1.00 183.30 ?  32   LEU F O   1 
ATOM   15563 C  CB  . LEU F 6  32   ? -8.175  12.871   53.427  1.00 181.37 ?  32   LEU F CB  1 
ATOM   15564 C  CG  . LEU F 6  32   ? -8.859  12.029   52.348  1.00 173.98 ?  32   LEU F CG  1 
ATOM   15565 C  CD1 . LEU F 6  32   ? -8.617  10.547   52.584  1.00 169.37 ?  32   LEU F CD1 1 
ATOM   15566 C  CD2 . LEU F 6  32   ? -10.349 12.331   52.292  1.00 166.61 ?  32   LEU F CD2 1 
ATOM   15567 N  N   . ALA F 6  33   ? -5.494  14.457   52.824  1.00 151.98 ?  33   ALA F N   1 
ATOM   15568 C  CA  . ALA F 6  33   ? -4.561  15.097   51.903  1.00 155.44 ?  33   ALA F CA  1 
ATOM   15569 C  C   . ALA F 6  33   ? -3.151  14.545   52.063  1.00 161.40 ?  33   ALA F C   1 
ATOM   15570 O  O   . ALA F 6  33   ? -2.408  14.453   51.080  1.00 166.95 ?  33   ALA F O   1 
ATOM   15571 C  CB  . ALA F 6  33   ? -4.568  16.611   52.112  1.00 151.58 ?  33   ALA F CB  1 
ATOM   15572 N  N   . ALA F 6  34   ? -2.766  14.177   53.288  1.00 140.24 ?  34   ALA F N   1 
ATOM   15573 C  CA  . ALA F 6  34   ? -1.469  13.540   53.493  1.00 139.37 ?  34   ALA F CA  1 
ATOM   15574 C  C   . ALA F 6  34   ? -1.415  12.182   52.808  1.00 147.05 ?  34   ALA F C   1 
ATOM   15575 O  O   . ALA F 6  34   ? -0.404  11.830   52.189  1.00 154.18 ?  34   ALA F O   1 
ATOM   15576 C  CB  . ALA F 6  34   ? -1.179  13.402   54.987  1.00 140.32 ?  34   ALA F CB  1 
ATOM   15577 N  N   . GLY F 6  35   ? -2.496  11.405   52.906  1.00 177.79 ?  35   GLY F N   1 
ATOM   15578 C  CA  . GLY F 6  35   ? -2.548  10.133   52.208  1.00 180.94 ?  35   GLY F CA  1 
ATOM   15579 C  C   . GLY F 6  35   ? -2.577  10.283   50.701  1.00 180.90 ?  35   GLY F C   1 
ATOM   15580 O  O   . GLY F 6  35   ? -2.074  9.417    49.979  1.00 180.24 ?  35   GLY F O   1 
ATOM   15581 N  N   . TYR F 6  36   ? -3.162  11.376   50.205  1.00 151.33 ?  36   TYR F N   1 
ATOM   15582 C  CA  . TYR F 6  36   ? -3.156  11.628   48.767  1.00 148.06 ?  36   TYR F CA  1 
ATOM   15583 C  C   . TYR F 6  36   ? -1.749  11.922   48.266  1.00 147.04 ?  36   TYR F C   1 
ATOM   15584 O  O   . TYR F 6  36   ? -1.339  11.417   47.214  1.00 143.27 ?  36   TYR F O   1 
ATOM   15585 C  CB  . TYR F 6  36   ? -4.098  12.785   48.428  1.00 146.37 ?  36   TYR F CB  1 
ATOM   15586 C  CG  . TYR F 6  36   ? -3.906  13.340   47.033  1.00 141.02 ?  36   TYR F CG  1 
ATOM   15587 C  CD1 . TYR F 6  36   ? -4.509  12.737   45.938  1.00 139.48 ?  36   TYR F CD1 1 
ATOM   15588 C  CD2 . TYR F 6  36   ? -3.132  14.473   46.812  1.00 146.24 ?  36   TYR F CD2 1 
ATOM   15589 C  CE1 . TYR F 6  36   ? -4.338  13.238   44.661  1.00 141.40 ?  36   TYR F CE1 1 
ATOM   15590 C  CE2 . TYR F 6  36   ? -2.956  14.981   45.540  1.00 143.07 ?  36   TYR F CE2 1 
ATOM   15591 C  CZ  . TYR F 6  36   ? -3.562  14.360   44.468  1.00 140.17 ?  36   TYR F CZ  1 
ATOM   15592 O  OH  . TYR F 6  36   ? -3.391  14.862   43.198  1.00 139.65 ?  36   TYR F OH  1 
ATOM   15593 N  N   . PHE F 6  37   ? -0.999  12.745   49.002  1.00 169.45 ?  37   PHE F N   1 
ATOM   15594 C  CA  . PHE F 6  37   ? 0.373   13.045   48.609  1.00 174.94 ?  37   PHE F CA  1 
ATOM   15595 C  C   . PHE F 6  37   ? 1.251   11.802   48.664  1.00 176.77 ?  37   PHE F C   1 
ATOM   15596 O  O   . PHE F 6  37   ? 2.179   11.660   47.859  1.00 173.45 ?  37   PHE F O   1 
ATOM   15597 C  CB  . PHE F 6  37   ? 0.941   14.146   49.505  1.00 180.75 ?  37   PHE F CB  1 
ATOM   15598 C  CG  . PHE F 6  37   ? 2.333   14.570   49.138  1.00 191.86 ?  37   PHE F CG  1 
ATOM   15599 C  CD1 . PHE F 6  37   ? 2.557   15.369   48.030  1.00 193.31 ?  37   PHE F CD1 1 
ATOM   15600 C  CD2 . PHE F 6  37   ? 3.417   14.175   49.904  1.00 195.39 ?  37   PHE F CD2 1 
ATOM   15601 C  CE1 . PHE F 6  37   ? 3.836   15.764   47.689  1.00 201.65 ?  37   PHE F CE1 1 
ATOM   15602 C  CE2 . PHE F 6  37   ? 4.699   14.566   49.569  1.00 200.04 ?  37   PHE F CE2 1 
ATOM   15603 C  CZ  . PHE F 6  37   ? 4.908   15.362   48.460  1.00 205.15 ?  37   PHE F CZ  1 
ATOM   15604 N  N   . LEU F 6  38   ? 0.974   10.892   49.601  1.00 190.61 ?  38   LEU F N   1 
ATOM   15605 C  CA  . LEU F 6  38   ? 1.722   9.640    49.660  1.00 191.90 ?  38   LEU F CA  1 
ATOM   15606 C  C   . LEU F 6  38   ? 1.305   8.697    48.538  1.00 187.01 ?  38   LEU F C   1 
ATOM   15607 O  O   . LEU F 6  38   ? 2.152   8.031    47.931  1.00 181.75 ?  38   LEU F O   1 
ATOM   15608 C  CB  . LEU F 6  38   ? 1.526   8.973    51.022  1.00 188.17 ?  38   LEU F CB  1 
ATOM   15609 C  CG  . LEU F 6  38   ? 2.034   9.733    52.250  1.00 184.46 ?  38   LEU F CG  1 
ATOM   15610 C  CD1 . LEU F 6  38   ? 1.766   8.941    53.521  1.00 189.27 ?  38   LEU F CD1 1 
ATOM   15611 C  CD2 . LEU F 6  38   ? 3.514   10.052   52.115  1.00 182.73 ?  38   LEU F CD2 1 
ATOM   15612 N  N   . SER F 6  39   ? 0.006   8.626    48.248  1.00 187.57 ?  39   SER F N   1 
ATOM   15613 C  CA  . SER F 6  39   ? -0.508  7.780    47.179  1.00 184.25 ?  39   SER F CA  1 
ATOM   15614 C  C   . SER F 6  39   ? -1.779  8.392    46.601  1.00 179.79 ?  39   SER F C   1 
ATOM   15615 O  O   . SER F 6  39   ? -2.784  8.523    47.310  1.00 177.77 ?  39   SER F O   1 
ATOM   15616 C  CB  . SER F 6  39   ? -0.779  6.365    47.692  1.00 181.18 ?  39   SER F CB  1 
ATOM   15617 O  OG  . SER F 6  39   ? -1.409  5.575    46.698  1.00 167.69 ?  39   SER F OG  1 
ATOM   15618 N  N   . PRO F 6  40   ? -1.773  8.780    45.323  1.00 145.84 ?  40   PRO F N   1 
ATOM   15619 C  CA  . PRO F 6  40   ? -2.961  9.441    44.761  1.00 143.03 ?  40   PRO F CA  1 
ATOM   15620 C  C   . PRO F 6  40   ? -4.138  8.506    44.552  1.00 139.21 ?  40   PRO F C   1 
ATOM   15621 O  O   . PRO F 6  40   ? -5.288  8.957    44.630  1.00 134.55 ?  40   PRO F O   1 
ATOM   15622 C  CB  . PRO F 6  40   ? -2.449  10.005   43.428  1.00 141.31 ?  40   PRO F CB  1 
ATOM   15623 C  CG  . PRO F 6  40   ? -1.279  9.147    43.081  1.00 143.78 ?  40   PRO F CG  1 
ATOM   15624 C  CD  . PRO F 6  40   ? -0.643  8.761    44.380  1.00 143.08 ?  40   PRO F CD  1 
ATOM   15625 N  N   . THR F 6  41   ? -3.893  7.222    44.286  1.00 173.62 ?  41   THR F N   1 
ATOM   15626 C  CA  . THR F 6  41   ? -4.994  6.299    44.028  1.00 167.39 ?  41   THR F CA  1 
ATOM   15627 C  C   . THR F 6  41   ? -5.785  6.014    45.299  1.00 159.80 ?  41   THR F C   1 
ATOM   15628 O  O   . THR F 6  41   ? -7.018  6.102    45.305  1.00 155.10 ?  41   THR F O   1 
ATOM   15629 C  CB  . THR F 6  41   ? -4.466  4.998    43.421  1.00 160.83 ?  41   THR F CB  1 
ATOM   15630 O  OG1 . THR F 6  41   ? -3.729  5.289    42.227  1.00 170.39 ?  41   THR F OG1 1 
ATOM   15631 C  CG2 . THR F 6  41   ? -5.618  4.061    43.085  1.00 148.00 ?  41   THR F CG2 1 
ATOM   15632 N  N   . SER F 6  42   ? -5.088  5.681    46.392  1.00 133.27 ?  42   SER F N   1 
ATOM   15633 C  CA  . SER F 6  42   ? -5.768  5.335    47.638  1.00 128.45 ?  42   SER F CA  1 
ATOM   15634 C  C   . SER F 6  42   ? -6.624  6.482    48.158  1.00 122.97 ?  42   SER F C   1 
ATOM   15635 O  O   . SER F 6  42   ? -7.585  6.252    48.901  1.00 114.86 ?  42   SER F O   1 
ATOM   15636 C  CB  . SER F 6  42   ? -4.745  4.919    48.696  1.00 130.62 ?  42   SER F CB  1 
ATOM   15637 O  OG  . SER F 6  42   ? -4.029  6.042    49.181  1.00 128.83 ?  42   SER F OG  1 
ATOM   15638 N  N   . PHE F 6  43   ? -6.291  7.720    47.785  1.00 160.78 ?  43   PHE F N   1 
ATOM   15639 C  CA  . PHE F 6  43   ? -7.111  8.862    48.178  1.00 158.69 ?  43   PHE F CA  1 
ATOM   15640 C  C   . PHE F 6  43   ? -8.511  8.757    47.587  1.00 150.57 ?  43   PHE F C   1 
ATOM   15641 O  O   . PHE F 6  43   ? -9.512  8.899    48.299  1.00 150.48 ?  43   PHE F O   1 
ATOM   15642 C  CB  . PHE F 6  43   ? -6.433  10.161   47.742  1.00 165.31 ?  43   PHE F CB  1 
ATOM   15643 C  CG  . PHE F 6  43   ? -7.349  11.353   47.733  1.00 166.55 ?  43   PHE F CG  1 
ATOM   15644 C  CD1 . PHE F 6  43   ? -7.684  11.996   48.913  1.00 165.88 ?  43   PHE F CD1 1 
ATOM   15645 C  CD2 . PHE F 6  43   ? -7.867  11.837   46.541  1.00 161.98 ?  43   PHE F CD2 1 
ATOM   15646 C  CE1 . PHE F 6  43   ? -8.525  13.094   48.907  1.00 155.47 ?  43   PHE F CE1 1 
ATOM   15647 C  CE2 . PHE F 6  43   ? -8.707  12.933   46.528  1.00 162.85 ?  43   PHE F CE2 1 
ATOM   15648 C  CZ  . PHE F 6  43   ? -9.036  13.563   47.712  1.00 158.79 ?  43   PHE F CZ  1 
ATOM   15649 N  N   . PHE F 6  44   ? -8.601  8.505    46.279  1.00 129.36 ?  44   PHE F N   1 
ATOM   15650 C  CA  . PHE F 6  44   ? -9.905  8.379    45.638  1.00 127.56 ?  44   PHE F CA  1 
ATOM   15651 C  C   . PHE F 6  44   ? -10.622 7.106    46.066  1.00 121.89 ?  44   PHE F C   1 
ATOM   15652 O  O   . PHE F 6  44   ? -11.855 7.092    46.151  1.00 118.25 ?  44   PHE F O   1 
ATOM   15653 C  CB  . PHE F 6  44   ? -9.754  8.414    44.118  1.00 133.56 ?  44   PHE F CB  1 
ATOM   15654 C  CG  . PHE F 6  44   ? -9.444  9.777    43.572  1.00 139.42 ?  44   PHE F CG  1 
ATOM   15655 C  CD1 . PHE F 6  44   ? -10.464 10.656   43.248  1.00 134.95 ?  44   PHE F CD1 1 
ATOM   15656 C  CD2 . PHE F 6  44   ? -8.133  10.179   43.377  1.00 140.56 ?  44   PHE F CD2 1 
ATOM   15657 C  CE1 . PHE F 6  44   ? -10.184 11.911   42.743  1.00 131.18 ?  44   PHE F CE1 1 
ATOM   15658 C  CE2 . PHE F 6  44   ? -7.845  11.432   42.873  1.00 140.23 ?  44   PHE F CE2 1 
ATOM   15659 C  CZ  . PHE F 6  44   ? -8.872  12.299   42.555  1.00 136.97 ?  44   PHE F CZ  1 
ATOM   15660 N  N   . GLU F 6  45   ? -9.876  6.031    46.335  1.00 136.37 ?  45   GLU F N   1 
ATOM   15661 C  CA  . GLU F 6  45   ? -10.507 4.798    46.792  1.00 130.26 ?  45   GLU F CA  1 
ATOM   15662 C  C   . GLU F 6  45   ? -11.194 5.004    48.134  1.00 123.87 ?  45   GLU F C   1 
ATOM   15663 O  O   . GLU F 6  45   ? -12.293 4.488    48.366  1.00 117.08 ?  45   GLU F O   1 
ATOM   15664 C  CB  . GLU F 6  45   ? -9.471  3.677    46.889  1.00 131.95 ?  45   GLU F CB  1 
ATOM   15665 C  CG  . GLU F 6  45   ? -8.625  3.478    45.639  1.00 134.89 ?  45   GLU F CG  1 
ATOM   15666 C  CD  . GLU F 6  45   ? -9.237  2.506    44.652  1.00 133.35 ?  45   GLU F CD  1 
ATOM   15667 O  OE1 . GLU F 6  45   ? -10.480 2.458    44.556  1.00 130.61 ?  45   GLU F OE1 1 
ATOM   15668 O  OE2 . GLU F 6  45   ? -8.472  1.789    43.971  1.00 141.23 -1 45   GLU F OE2 1 
ATOM   15669 N  N   . SER F 6  46   ? -10.562 5.764    49.030  1.00 121.65 ?  46   SER F N   1 
ATOM   15670 C  CA  . SER F 6  46   ? -11.167 6.055    50.323  1.00 115.96 ?  46   SER F CA  1 
ATOM   15671 C  C   . SER F 6  46   ? -12.231 7.139    50.224  1.00 111.93 ?  46   SER F C   1 
ATOM   15672 O  O   . SER F 6  46   ? -13.207 7.112    50.982  1.00 108.82 ?  46   SER F O   1 
ATOM   15673 C  CB  . SER F 6  46   ? -10.089 6.467    51.325  1.00 118.87 ?  46   SER F CB  1 
ATOM   15674 O  OG  . SER F 6  46   ? -9.094  5.465    51.442  1.00 116.71 ?  46   SER F OG  1 
ATOM   15675 N  N   . TYR F 6  47   ? -12.065 8.092    49.303  1.00 101.12 ?  47   TYR F N   1 
ATOM   15676 C  CA  . TYR F 6  47   ? -13.049 9.159    49.155  1.00 100.40 ?  47   TYR F CA  1 
ATOM   15677 C  C   . TYR F 6  47   ? -14.387 8.627    48.658  1.00 99.70  ?  47   TYR F C   1 
ATOM   15678 O  O   . TYR F 6  47   ? -15.438 9.176    49.010  1.00 91.32  ?  47   TYR F O   1 
ATOM   15679 C  CB  . TYR F 6  47   ? -12.520 10.234   48.206  1.00 103.79 ?  47   TYR F CB  1 
ATOM   15680 C  CG  . TYR F 6  47   ? -13.351 11.498   48.187  1.00 99.26  ?  47   TYR F CG  1 
ATOM   15681 C  CD1 . TYR F 6  47   ? -13.126 12.512   49.108  1.00 100.31 ?  47   TYR F CD1 1 
ATOM   15682 C  CD2 . TYR F 6  47   ? -14.359 11.677   47.247  1.00 102.87 ?  47   TYR F CD2 1 
ATOM   15683 C  CE1 . TYR F 6  47   ? -13.883 13.669   49.096  1.00 102.38 ?  47   TYR F CE1 1 
ATOM   15684 C  CE2 . TYR F 6  47   ? -15.121 12.831   47.228  1.00 103.66 ?  47   TYR F CE2 1 
ATOM   15685 C  CZ  . TYR F 6  47   ? -14.878 13.824   48.154  1.00 105.73 ?  47   TYR F CZ  1 
ATOM   15686 O  OH  . TYR F 6  47   ? -15.633 14.975   48.140  1.00 104.18 ?  47   TYR F OH  1 
ATOM   15687 N  N   . ILE F 6  48   ? -14.371 7.572    47.839  1.00 107.72 ?  48   ILE F N   1 
ATOM   15688 C  CA  . ILE F 6  48   ? -15.618 6.950    47.399  1.00 99.74  ?  48   ILE F CA  1 
ATOM   15689 C  C   . ILE F 6  48   ? -16.370 6.377    48.592  1.00 94.15  ?  48   ILE F C   1 
ATOM   15690 O  O   . ILE F 6  48   ? -17.579 6.588    48.751  1.00 91.20  ?  48   ILE F O   1 
ATOM   15691 C  CB  . ILE F 6  48   ? -15.339 5.865    46.344  1.00 98.78  ?  48   ILE F CB  1 
ATOM   15692 C  CG1 . ILE F 6  48   ? -14.836 6.487    45.041  1.00 99.88  ?  48   ILE F CG1 1 
ATOM   15693 C  CG2 . ILE F 6  48   ? -16.588 5.033    46.090  1.00 97.37  ?  48   ILE F CG2 1 
ATOM   15694 C  CD1 . ILE F 6  48   ? -14.592 5.468    43.951  1.00 101.62 ?  48   ILE F CD1 1 
ATOM   15695 N  N   . TYR F 6  49   ? -15.662 5.640    49.450  1.00 105.90 ?  49   TYR F N   1 
ATOM   15696 C  CA  . TYR F 6  49   ? -16.293 5.062    50.630  1.00 102.73 ?  49   TYR F CA  1 
ATOM   15697 C  C   . TYR F 6  49   ? -16.749 6.148    51.597  1.00 105.44 ?  49   TYR F C   1 
ATOM   15698 O  O   . TYR F 6  49   ? -17.826 6.041    52.195  1.00 108.55 ?  49   TYR F O   1 
ATOM   15699 C  CB  . TYR F 6  49   ? -15.328 4.092    51.313  1.00 104.11 ?  49   TYR F CB  1 
ATOM   15700 C  CG  . TYR F 6  49   ? -15.656 3.792    52.759  1.00 97.51  ?  49   TYR F CG  1 
ATOM   15701 C  CD1 . TYR F 6  49   ? -16.847 3.168    53.106  1.00 97.87  ?  49   TYR F CD1 1 
ATOM   15702 C  CD2 . TYR F 6  49   ? -14.772 4.128    53.775  1.00 93.22  ?  49   TYR F CD2 1 
ATOM   15703 C  CE1 . TYR F 6  49   ? -17.150 2.891    54.425  1.00 96.71  ?  49   TYR F CE1 1 
ATOM   15704 C  CE2 . TYR F 6  49   ? -15.067 3.855    55.098  1.00 101.51 ?  49   TYR F CE2 1 
ATOM   15705 C  CZ  . TYR F 6  49   ? -16.257 3.236    55.417  1.00 100.15 ?  49   TYR F CZ  1 
ATOM   15706 O  OH  . TYR F 6  49   ? -16.554 2.961    56.732  1.00 100.03 ?  49   TYR F OH  1 
ATOM   15707 N  N   . GLY F 6  50   ? -15.949 7.205    51.753  1.00 82.53  ?  50   GLY F N   1 
ATOM   15708 C  CA  . GLY F 6  50   ? -16.347 8.297    52.627  1.00 86.34  ?  50   GLY F CA  1 
ATOM   15709 C  C   . GLY F 6  50   ? -17.568 9.039    52.118  1.00 85.47  ?  50   GLY F C   1 
ATOM   15710 O  O   . GLY F 6  50   ? -18.439 9.430    52.900  1.00 85.66  ?  50   GLY F O   1 
ATOM   15711 N  N   . TYR F 6  51   ? -17.648 9.247    50.802  1.00 87.09  ?  51   TYR F N   1 
ATOM   15712 C  CA  . TYR F 6  51   ? -18.826 9.886    50.223  1.00 84.62  ?  51   TYR F CA  1 
ATOM   15713 C  C   . TYR F 6  51   ? -20.059 9.004    50.367  1.00 84.39  ?  51   TYR F C   1 
ATOM   15714 O  O   . TYR F 6  51   ? -21.168 9.505    50.591  1.00 82.83  ?  51   TYR F O   1 
ATOM   15715 C  CB  . TYR F 6  51   ? -18.572 10.211   48.752  1.00 77.56  ?  51   TYR F CB  1 
ATOM   15716 C  CG  . TYR F 6  51   ? -19.644 11.066   48.120  1.00 86.61  ?  51   TYR F CG  1 
ATOM   15717 C  CD1 . TYR F 6  51   ? -19.714 12.428   48.374  1.00 99.44  ?  51   TYR F CD1 1 
ATOM   15718 C  CD2 . TYR F 6  51   ? -20.589 10.508   47.270  1.00 92.82  ?  51   TYR F CD2 1 
ATOM   15719 C  CE1 . TYR F 6  51   ? -20.694 13.213   47.798  1.00 102.16 ?  51   TYR F CE1 1 
ATOM   15720 C  CE2 . TYR F 6  51   ? -21.573 11.283   46.689  1.00 94.89  ?  51   TYR F CE2 1 
ATOM   15721 C  CZ  . TYR F 6  51   ? -21.620 12.634   46.957  1.00 98.30  ?  51   TYR F CZ  1 
ATOM   15722 O  OH  . TYR F 6  51   ? -22.597 13.409   46.381  1.00 98.42  ?  51   TYR F OH  1 
ATOM   15723 N  N   . TYR F 6  52   ? -19.884 7.688    50.240  1.00 95.49  ?  52   TYR F N   1 
ATOM   15724 C  CA  . TYR F 6  52   ? -21.015 6.771    50.330  1.00 91.12  ?  52   TYR F CA  1 
ATOM   15725 C  C   . TYR F 6  52   ? -21.563 6.699    51.750  1.00 89.78  ?  52   TYR F C   1 
ATOM   15726 O  O   . TYR F 6  52   ? -22.776 6.563    51.946  1.00 86.87  ?  52   TYR F O   1 
ATOM   15727 C  CB  . TYR F 6  52   ? -20.592 5.387    49.838  1.00 84.76  ?  52   TYR F CB  1 
ATOM   15728 C  CG  . TYR F 6  52   ? -21.736 4.429    49.592  1.00 84.84  ?  52   TYR F CG  1 
ATOM   15729 C  CD1 . TYR F 6  52   ? -22.599 4.606    48.518  1.00 86.71  ?  52   TYR F CD1 1 
ATOM   15730 C  CD2 . TYR F 6  52   ? -21.940 3.335    50.423  1.00 83.59  ?  52   TYR F CD2 1 
ATOM   15731 C  CE1 . TYR F 6  52   ? -23.642 3.728    48.287  1.00 87.44  ?  52   TYR F CE1 1 
ATOM   15732 C  CE2 . TYR F 6  52   ? -22.980 2.451    50.200  1.00 83.90  ?  52   TYR F CE2 1 
ATOM   15733 C  CZ  . TYR F 6  52   ? -23.827 2.652    49.131  1.00 85.96  ?  52   TYR F CZ  1 
ATOM   15734 O  OH  . TYR F 6  52   ? -24.863 1.774    48.905  1.00 85.27  ?  52   TYR F OH  1 
ATOM   15735 N  N   . VAL F 6  53   ? -20.689 6.793    52.754  1.00 71.90  ?  53   VAL F N   1 
ATOM   15736 C  CA  . VAL F 6  53   ? -21.144 6.680    54.136  1.00 69.59  ?  53   VAL F CA  1 
ATOM   15737 C  C   . VAL F 6  53   ? -21.676 8.015    54.653  1.00 71.63  ?  53   VAL F C   1 
ATOM   15738 O  O   . VAL F 6  53   ? -22.588 8.041    55.488  1.00 71.24  ?  53   VAL F O   1 
ATOM   15739 C  CB  . VAL F 6  53   ? -20.014 6.131    55.028  1.00 71.60  ?  53   VAL F CB  1 
ATOM   15740 C  CG1 . VAL F 6  53   ? -18.839 7.092    55.067  1.00 74.50  ?  53   VAL F CG1 1 
ATOM   15741 C  CG2 . VAL F 6  53   ? -20.522 5.840    56.434  1.00 73.30  ?  53   VAL F CG2 1 
ATOM   15742 N  N   . ALA F 6  54   ? -21.142 9.137    54.163  1.00 111.72 ?  54   ALA F N   1 
ATOM   15743 C  CA  . ALA F 6  54   ? -21.604 10.446   54.609  1.00 116.91 ?  54   ALA F CA  1 
ATOM   15744 C  C   . ALA F 6  54   ? -22.914 10.862   53.955  1.00 121.35 ?  54   ALA F C   1 
ATOM   15745 O  O   . ALA F 6  54   ? -23.613 11.726   54.494  1.00 122.95 ?  54   ALA F O   1 
ATOM   15746 C  CB  . ALA F 6  54   ? -20.534 11.505   54.334  1.00 108.84 ?  54   ALA F CB  1 
ATOM   15747 N  N   . MET F 6  55   ? -23.262 10.267   52.813  1.00 121.00 ?  55   MET F N   1 
ATOM   15748 C  CA  . MET F 6  55   ? -24.497 10.594   52.111  1.00 116.28 ?  55   MET F CA  1 
ATOM   15749 C  C   . MET F 6  55   ? -25.742 10.072   52.820  1.00 115.86 ?  55   MET F C   1 
ATOM   15750 O  O   . MET F 6  55   ? -26.856 10.446   52.437  1.00 111.46 ?  55   MET F O   1 
ATOM   15751 C  CB  . MET F 6  55   ? -24.435 10.035   50.688  1.00 113.65 ?  55   MET F CB  1 
ATOM   15752 C  CG  . MET F 6  55   ? -25.449 10.635   49.739  1.00 115.03 ?  55   MET F CG  1 
ATOM   15753 S  SD  . MET F 6  55   ? -25.104 12.348   49.318  1.00 133.07 ?  55   MET F SD  1 
ATOM   15754 C  CE  . MET F 6  55   ? -26.101 12.501   47.843  1.00 120.81 ?  55   MET F CE  1 
ATOM   15755 N  N   . THR F 6  56   ? -25.584 9.240    53.851  1.00 106.59 ?  56   THR F N   1 
ATOM   15756 C  CA  . THR F 6  56   ? -26.739 8.578    54.448  1.00 106.57 ?  56   THR F CA  1 
ATOM   15757 C  C   . THR F 6  56   ? -27.566 9.523    55.310  1.00 108.52 ?  56   THR F C   1 
ATOM   15758 O  O   . THR F 6  56   ? -28.790 9.366    55.395  1.00 105.88 ?  56   THR F O   1 
ATOM   15759 C  CB  . THR F 6  56   ? -26.277 7.378    55.268  1.00 95.11  ?  56   THR F CB  1 
ATOM   15760 O  OG1 . THR F 6  56   ? -25.390 7.819    56.304  1.00 92.12  ?  56   THR F OG1 1 
ATOM   15761 C  CG2 . THR F 6  56   ? -25.548 6.400    54.374  1.00 93.41  ?  56   THR F CG2 1 
ATOM   15762 N  N   . ILE F 6  57   ? -26.930 10.495   55.955  1.00 125.39 ?  57   ILE F N   1 
ATOM   15763 C  CA  . ILE F 6  57   ? -27.640 11.420   56.837  1.00 131.32 ?  57   ILE F CA  1 
ATOM   15764 C  C   . ILE F 6  57   ? -28.577 12.318   56.030  1.00 128.68 ?  57   ILE F C   1 
ATOM   15765 O  O   . ILE F 6  57   ? -29.766 12.400   56.368  1.00 126.86 ?  57   ILE F O   1 
ATOM   15766 C  CB  . ILE F 6  57   ? -26.665 12.248   57.692  1.00 136.35 ?  57   ILE F CB  1 
ATOM   15767 C  CG1 . ILE F 6  57   ? -25.876 11.345   58.645  1.00 136.46 ?  57   ILE F CG1 1 
ATOM   15768 C  CG2 . ILE F 6  57   ? -27.418 13.317   58.470  1.00 136.68 ?  57   ILE F CG2 1 
ATOM   15769 C  CD1 . ILE F 6  57   ? -24.558 10.849   58.086  1.00 138.66 ?  57   ILE F CD1 1 
ATOM   15770 N  N   . PRO F 6  58   ? -28.122 13.006   54.972  1.00 116.07 ?  58   PRO F N   1 
ATOM   15771 C  CA  . PRO F 6  58   ? -29.066 13.878   54.249  1.00 117.70 ?  58   PRO F CA  1 
ATOM   15772 C  C   . PRO F 6  58   ? -30.152 13.114   53.513  1.00 114.15 ?  58   PRO F C   1 
ATOM   15773 O  O   . PRO F 6  58   ? -31.314 13.538   53.531  1.00 113.95 ?  58   PRO F O   1 
ATOM   15774 C  CB  . PRO F 6  58   ? -28.159 14.653   53.283  1.00 124.98 ?  58   PRO F CB  1 
ATOM   15775 C  CG  . PRO F 6  58   ? -26.987 13.774   53.086  1.00 122.14 ?  58   PRO F CG  1 
ATOM   15776 C  CD  . PRO F 6  58   ? -26.763 13.108   54.407  1.00 120.91 ?  58   PRO F CD  1 
ATOM   15777 N  N   . LEU F 6  59   ? -29.811 11.999   52.862  1.00 80.48  ?  59   LEU F N   1 
ATOM   15778 C  CA  . LEU F 6  59   ? -30.816 11.238   52.126  1.00 76.58  ?  59   LEU F CA  1 
ATOM   15779 C  C   . LEU F 6  59   ? -31.847 10.631   53.068  1.00 74.02  ?  59   LEU F C   1 
ATOM   15780 O  O   . LEU F 6  59   ? -33.055 10.694   52.806  1.00 73.00  ?  59   LEU F O   1 
ATOM   15781 C  CB  . LEU F 6  59   ? -30.147 10.148   51.288  1.00 72.23  ?  59   LEU F CB  1 
ATOM   15782 C  CG  . LEU F 6  59   ? -29.475 10.602   49.993  1.00 71.83  ?  59   LEU F CG  1 
ATOM   15783 C  CD1 . LEU F 6  59   ? -28.878 9.414    49.258  1.00 72.53  ?  59   LEU F CD1 1 
ATOM   15784 C  CD2 . LEU F 6  59   ? -30.469 11.335   49.109  1.00 80.22  ?  59   LEU F CD2 1 
ATOM   15785 N  N   . GLY F 6  60   ? -31.390 10.032   54.169  1.00 80.93  ?  60   GLY F N   1 
ATOM   15786 C  CA  . GLY F 6  60   ? -32.321 9.492    55.144  1.00 82.53  ?  60   GLY F CA  1 
ATOM   15787 C  C   . GLY F 6  60   ? -33.174 10.559   55.799  1.00 82.52  ?  60   GLY F C   1 
ATOM   15788 O  O   . GLY F 6  60   ? -34.343 10.320   56.112  1.00 70.51  ?  60   GLY F O   1 
ATOM   15789 N  N   . CYS F 6  61   ? -32.607 11.749   56.011  1.00 125.85 ?  61   CYS F N   1 
ATOM   15790 C  CA  . CYS F 6  61   ? -33.381 12.846   56.582  1.00 127.76 ?  61   CYS F CA  1 
ATOM   15791 C  C   . CYS F 6  61   ? -34.478 13.301   55.628  1.00 125.10 ?  61   CYS F C   1 
ATOM   15792 O  O   . CYS F 6  61   ? -35.609 13.565   56.053  1.00 126.67 ?  61   CYS F O   1 
ATOM   15793 C  CB  . CYS F 6  61   ? -32.459 14.012   56.936  1.00 120.47 ?  61   CYS F CB  1 
ATOM   15794 S  SG  . CYS F 6  61   ? -31.611 13.847   58.527  1.00 132.18 ?  61   CYS F SG  1 
ATOM   15795 N  N   . LEU F 6  62   ? -34.162 13.397   54.334  1.00 109.11 ?  62   LEU F N   1 
ATOM   15796 C  CA  . LEU F 6  62   ? -35.168 13.789   53.352  1.00 112.62 ?  62   LEU F CA  1 
ATOM   15797 C  C   . LEU F 6  62   ? -36.268 12.742   53.242  1.00 115.62 ?  62   LEU F C   1 
ATOM   15798 O  O   . LEU F 6  62   ? -37.455 13.083   53.168  1.00 112.96 ?  62   LEU F O   1 
ATOM   15799 C  CB  . LEU F 6  62   ? -34.509 14.019   51.992  1.00 111.35 ?  62   LEU F CB  1 
ATOM   15800 C  CG  . LEU F 6  62   ? -35.450 14.360   50.835  1.00 110.92 ?  62   LEU F CG  1 
ATOM   15801 C  CD1 . LEU F 6  62   ? -36.114 15.709   51.064  1.00 114.21 ?  62   LEU F CD1 1 
ATOM   15802 C  CD2 . LEU F 6  62   ? -34.705 14.338   49.510  1.00 114.96 ?  62   LEU F CD2 1 
ATOM   15803 N  N   . GLY F 6  63   ? -35.893 11.462   53.231  1.00 130.09 ?  63   GLY F N   1 
ATOM   15804 C  CA  . GLY F 6  63   ? -36.891 10.410   53.126  1.00 129.67 ?  63   GLY F CA  1 
ATOM   15805 C  C   . GLY F 6  63   ? -37.810 10.348   54.331  1.00 125.64 ?  63   GLY F C   1 
ATOM   15806 O  O   . GLY F 6  63   ? -39.028 10.208   54.186  1.00 124.36 ?  63   GLY F O   1 
ATOM   15807 N  N   . PHE F 6  64   ? -37.245 10.451   55.536  1.00 93.18  ?  64   PHE F N   1 
ATOM   15808 C  CA  . PHE F 6  64   ? -38.071 10.417   56.737  1.00 94.40  ?  64   PHE F CA  1 
ATOM   15809 C  C   . PHE F 6  64   ? -38.926 11.670   56.866  1.00 103.43 ?  64   PHE F C   1 
ATOM   15810 O  O   . PHE F 6  64   ? -40.035 11.607   57.408  1.00 109.01 ?  64   PHE F O   1 
ATOM   15811 C  CB  . PHE F 6  64   ? -37.194 10.239   57.976  1.00 92.01  ?  64   PHE F CB  1 
ATOM   15812 C  CG  . PHE F 6  64   ? -36.974 8.804    58.359  1.00 92.64  ?  64   PHE F CG  1 
ATOM   15813 C  CD1 . PHE F 6  64   ? -37.994 8.060    58.929  1.00 93.59  ?  64   PHE F CD1 1 
ATOM   15814 C  CD2 . PHE F 6  64   ? -35.748 8.199    58.144  1.00 92.83  ?  64   PHE F CD2 1 
ATOM   15815 C  CE1 . PHE F 6  64   ? -37.792 6.739    59.280  1.00 89.46  ?  64   PHE F CE1 1 
ATOM   15816 C  CE2 . PHE F 6  64   ? -35.541 6.881    58.493  1.00 83.39  ?  64   PHE F CE2 1 
ATOM   15817 C  CZ  . PHE F 6  64   ? -36.563 6.149    59.062  1.00 87.05  ?  64   PHE F CZ  1 
ATOM   15818 N  N   . LEU F 6  65   ? -38.429 12.809   56.380  1.00 89.46  ?  65   LEU F N   1 
ATOM   15819 C  CA  . LEU F 6  65   ? -39.234 14.026   56.364  1.00 92.41  ?  65   LEU F CA  1 
ATOM   15820 C  C   . LEU F 6  65   ? -40.473 13.849   55.495  1.00 95.20  ?  65   LEU F C   1 
ATOM   15821 O  O   . LEU F 6  65   ? -41.582 14.231   55.884  1.00 96.32  ?  65   LEU F O   1 
ATOM   15822 C  CB  . LEU F 6  65   ? -38.394 15.200   55.862  1.00 93.86  ?  65   LEU F CB  1 
ATOM   15823 C  CG  . LEU F 6  65   ? -39.104 16.551   55.767  1.00 94.04  ?  65   LEU F CG  1 
ATOM   15824 C  CD1 . LEU F 6  65   ? -39.458 17.075   57.152  1.00 105.45 ?  65   LEU F CD1 1 
ATOM   15825 C  CD2 . LEU F 6  65   ? -38.255 17.552   54.999  1.00 91.46  ?  65   LEU F CD2 1 
ATOM   15826 N  N   . MET F 6  66   ? -40.296 13.273   54.306  1.00 105.38 ?  66   MET F N   1 
ATOM   15827 C  CA  . MET F 6  66   ? -41.423 13.064   53.405  1.00 106.12 ?  66   MET F CA  1 
ATOM   15828 C  C   . MET F 6  66   ? -42.334 11.944   53.891  1.00 96.44  ?  66   MET F C   1 
ATOM   15829 O  O   . MET F 6  66   ? -43.544 11.978   53.639  1.00 88.86  ?  66   MET F O   1 
ATOM   15830 C  CB  . MET F 6  66   ? -40.901 12.774   51.999  1.00 97.01  ?  66   MET F CB  1 
ATOM   15831 C  CG  . MET F 6  66   ? -40.734 14.014   51.139  1.00 101.34 ?  66   MET F CG  1 
ATOM   15832 S  SD  . MET F 6  66   ? -39.211 13.990   50.173  1.00 122.73 ?  66   MET F SD  1 
ATOM   15833 C  CE  . MET F 6  66   ? -39.428 12.493   49.222  1.00 101.51 ?  66   MET F CE  1 
ATOM   15834 N  N   . VAL F 6  67   ? -41.779 10.950   54.588  1.00 93.40  ?  67   VAL F N   1 
ATOM   15835 C  CA  . VAL F 6  67   ? -42.603 9.866    55.116  1.00 96.27  ?  67   VAL F CA  1 
ATOM   15836 C  C   . VAL F 6  67   ? -43.473 10.366   56.263  1.00 102.81 ?  67   VAL F C   1 
ATOM   15837 O  O   . VAL F 6  67   ? -44.674 10.070   56.322  1.00 108.40 ?  67   VAL F O   1 
ATOM   15838 C  CB  . VAL F 6  67   ? -41.716 8.681    55.539  1.00 91.17  ?  67   VAL F CB  1 
ATOM   15839 C  CG1 . VAL F 6  67   ? -42.446 7.794    56.534  1.00 83.87  ?  67   VAL F CG1 1 
ATOM   15840 C  CG2 . VAL F 6  67   ? -41.295 7.877    54.320  1.00 82.21  ?  67   VAL F CG2 1 
ATOM   15841 N  N   . GLN F 6  68   ? -42.893 11.142   57.184  1.00 98.33  ?  68   GLN F N   1 
ATOM   15842 C  CA  . GLN F 6  68   ? -43.676 11.681   58.290  1.00 99.51  ?  68   GLN F CA  1 
ATOM   15843 C  C   . GLN F 6  68   ? -44.687 12.723   57.827  1.00 102.27 ?  68   GLN F C   1 
ATOM   15844 O  O   . GLN F 6  68   ? -45.695 12.937   58.509  1.00 109.66 ?  68   GLN F O   1 
ATOM   15845 C  CB  . GLN F 6  68   ? -42.748 12.268   59.363  1.00 100.83 ?  68   GLN F CB  1 
ATOM   15846 C  CG  . GLN F 6  68   ? -42.051 13.570   58.984  1.00 100.95 ?  68   GLN F CG  1 
ATOM   15847 C  CD  . GLN F 6  68   ? -42.827 14.801   59.422  1.00 108.09 ?  68   GLN F CD  1 
ATOM   15848 O  OE1 . GLN F 6  68   ? -43.833 14.698   60.125  1.00 114.98 ?  68   GLN F OE1 1 
ATOM   15849 N  NE2 . GLN F 6  68   ? -42.357 15.973   59.012  1.00 105.36 ?  68   GLN F NE2 1 
ATOM   15850 N  N   . HIS F 6  69   ? -44.447 13.370   56.683  1.00 91.96  ?  69   HIS F N   1 
ATOM   15851 C  CA  . HIS F 6  69   ? -45.461 14.255   56.118  1.00 94.93  ?  69   HIS F CA  1 
ATOM   15852 C  C   . HIS F 6  69   ? -46.643 13.460   55.584  1.00 96.83  ?  69   HIS F C   1 
ATOM   15853 O  O   . HIS F 6  69   ? -47.795 13.892   55.705  1.00 91.79  ?  69   HIS F O   1 
ATOM   15854 C  CB  . HIS F 6  69   ? -44.861 15.125   55.012  1.00 99.03  ?  69   HIS F CB  1 
ATOM   15855 C  CG  . HIS F 6  69   ? -44.279 16.415   55.504  1.00 105.24 ?  69   HIS F CG  1 
ATOM   15856 N  ND1 . HIS F 6  69   ? -42.942 16.566   55.800  1.00 111.95 ?  69   HIS F ND1 1 
ATOM   15857 C  CD2 . HIS F 6  69   ? -44.856 17.615   55.751  1.00 98.59  ?  69   HIS F CD2 1 
ATOM   15858 C  CE1 . HIS F 6  69   ? -42.720 17.802   56.210  1.00 104.68 ?  69   HIS F CE1 1 
ATOM   15859 N  NE2 . HIS F 6  69   ? -43.865 18.458   56.192  1.00 99.69  ?  69   HIS F NE2 1 
ATOM   15860 N  N   . LEU F 6  70   ? -46.377 12.298   54.983  1.00 109.11 ?  70   LEU F N   1 
ATOM   15861 C  CA  . LEU F 6  70   ? -47.458 11.451   54.493  1.00 106.83 ?  70   LEU F CA  1 
ATOM   15862 C  C   . LEU F 6  70   ? -48.254 10.859   55.650  1.00 102.90 ?  70   LEU F C   1 
ATOM   15863 O  O   . LEU F 6  70   ? -49.490 10.891   55.648  1.00 103.68 ?  70   LEU F O   1 
ATOM   15864 C  CB  . LEU F 6  70   ? -46.891 10.345   53.602  1.00 101.80 ?  70   LEU F CB  1 
ATOM   15865 C  CG  . LEU F 6  70   ? -46.705 10.697   52.125  1.00 90.82  ?  70   LEU F CG  1 
ATOM   15866 C  CD1 . LEU F 6  70   ? -46.184 9.500    51.345  1.00 94.76  ?  70   LEU F CD1 1 
ATOM   15867 C  CD2 . LEU F 6  70   ? -48.010 11.202   51.530  1.00 87.31  ?  70   LEU F CD2 1 
ATOM   15868 N  N   . THR F 6  71   ? -47.562 10.316   56.647  1.00 117.37 ?  71   THR F N   1 
ATOM   15869 C  CA  . THR F 6  71   ? -48.187 9.757    57.842  1.00 120.12 ?  71   THR F CA  1 
ATOM   15870 C  C   . THR F 6  71   ? -47.760 10.614   59.029  1.00 119.75 ?  71   THR F C   1 
ATOM   15871 O  O   . THR F 6  71   ? -46.666 10.439   59.572  1.00 119.56 ?  71   THR F O   1 
ATOM   15872 C  CB  . THR F 6  71   ? -47.792 8.295    58.039  1.00 119.49 ?  71   THR F CB  1 
ATOM   15873 O  OG1 . THR F 6  71   ? -46.421 8.220    58.452  1.00 117.03 ?  71   THR F OG1 1 
ATOM   15874 C  CG2 . THR F 6  71   ? -47.972 7.515    56.745  1.00 118.29 ?  71   THR F CG2 1 
ATOM   15875 N  N   . GLY F 6  72   ? -48.627 11.542   59.426  1.00 163.15 ?  72   GLY F N   1 
ATOM   15876 C  CA  . GLY F 6  72   ? -48.298 12.430   60.526  1.00 173.10 ?  72   GLY F CA  1 
ATOM   15877 C  C   . GLY F 6  72   ? -48.329 11.706   61.861  1.00 172.43 ?  72   GLY F C   1 
ATOM   15878 O  O   . GLY F 6  72   ? -49.222 10.906   62.141  1.00 178.41 ?  72   GLY F O   1 
ATOM   15879 N  N   . GLY F 6  73   ? -47.332 11.998   62.694  1.00 128.58 ?  73   GLY F N   1 
ATOM   15880 C  CA  . GLY F 6  73   ? -47.231 11.401   64.008  1.00 133.83 ?  73   GLY F CA  1 
ATOM   15881 C  C   . GLY F 6  73   ? -46.532 12.343   64.964  1.00 130.78 ?  73   GLY F C   1 
ATOM   15882 O  O   . GLY F 6  73   ? -46.075 13.422   64.583  1.00 130.07 ?  73   GLY F O   1 
ATOM   15883 N  N   . ALA F 6  74   ? -46.456 11.921   66.228  1.00 129.93 ?  74   ALA F N   1 
ATOM   15884 C  CA  . ALA F 6  74   ? -45.787 12.738   67.235  1.00 134.97 ?  74   ALA F CA  1 
ATOM   15885 C  C   . ALA F 6  74   ? -44.283 12.784   66.998  1.00 130.42 ?  74   ALA F C   1 
ATOM   15886 O  O   . ALA F 6  74   ? -43.657 13.840   67.144  1.00 136.05 ?  74   ALA F O   1 
ATOM   15887 C  CB  . ALA F 6  74   ? -46.098 12.208   68.634  1.00 133.64 ?  74   ALA F CB  1 
ATOM   15888 N  N   . TRP F 6  75   ? -43.686 11.647   66.629  1.00 92.75  ?  75   TRP F N   1 
ATOM   15889 C  CA  . TRP F 6  75   ? -42.255 11.618   66.347  1.00 96.66  ?  75   TRP F CA  1 
ATOM   15890 C  C   . TRP F 6  75   ? -41.905 12.448   65.119  1.00 99.03  ?  75   TRP F C   1 
ATOM   15891 O  O   . TRP F 6  75   ? -40.781 12.951   65.013  1.00 102.00 ?  75   TRP F O   1 
ATOM   15892 C  CB  . TRP F 6  75   ? -41.789 10.174   66.164  1.00 102.68 ?  75   TRP F CB  1 
ATOM   15893 C  CG  . TRP F 6  75   ? -42.414 9.495    64.986  1.00 102.66 ?  75   TRP F CG  1 
ATOM   15894 C  CD1 . TRP F 6  75   ? -43.559 8.753    64.981  1.00 99.24  ?  75   TRP F CD1 1 
ATOM   15895 C  CD2 . TRP F 6  75   ? -41.933 9.500    63.635  1.00 98.68  ?  75   TRP F CD2 1 
ATOM   15896 N  NE1 . TRP F 6  75   ? -43.820 8.293    63.713  1.00 96.03  ?  75   TRP F NE1 1 
ATOM   15897 C  CE2 . TRP F 6  75   ? -42.838 8.738    62.869  1.00 93.13  ?  75   TRP F CE2 1 
ATOM   15898 C  CE3 . TRP F 6  75   ? -40.826 10.073   63.000  1.00 96.95  ?  75   TRP F CE3 1 
ATOM   15899 C  CZ2 . TRP F 6  75   ? -42.669 8.534    61.501  1.00 93.69  ?  75   TRP F CZ2 1 
ATOM   15900 C  CZ3 . TRP F 6  75   ? -40.662 9.869    61.641  1.00 86.51  ?  75   TRP F CZ3 1 
ATOM   15901 C  CH2 . TRP F 6  75   ? -41.578 9.106    60.907  1.00 93.23  ?  75   TRP F CH2 1 
ATOM   15902 N  N   . GLY F 6  76   ? -42.845 12.602   64.185  1.00 110.38 ?  76   GLY F N   1 
ATOM   15903 C  CA  . GLY F 6  76   ? -42.569 13.398   63.001  1.00 118.31 ?  76   GLY F CA  1 
ATOM   15904 C  C   . GLY F 6  76   ? -42.535 14.886   63.292  1.00 120.13 ?  76   GLY F C   1 
ATOM   15905 O  O   . GLY F 6  76   ? -41.668 15.606   62.789  1.00 113.47 ?  76   GLY F O   1 
ATOM   15906 N  N   . VAL F 6  77   ? -43.477 15.368   64.105  1.00 104.13 ?  77   VAL F N   1 
ATOM   15907 C  CA  . VAL F 6  77   ? -43.487 16.780   64.471  1.00 98.67  ?  77   VAL F CA  1 
ATOM   15908 C  C   . VAL F 6  77   ? -42.321 17.101   65.398  1.00 97.41  ?  77   VAL F C   1 
ATOM   15909 O  O   . VAL F 6  77   ? -41.838 18.240   65.431  1.00 99.49  ?  77   VAL F O   1 
ATOM   15910 C  CB  . VAL F 6  77   ? -44.840 17.151   65.107  1.00 100.98 ?  77   VAL F CB  1 
ATOM   15911 C  CG1 . VAL F 6  77   ? -44.922 18.647   65.381  1.00 109.55 ?  77   VAL F CG1 1 
ATOM   15912 C  CG2 . VAL F 6  77   ? -45.985 16.702   64.214  1.00 105.52 ?  77   VAL F CG2 1 
ATOM   15913 N  N   . THR F 6  78   ? -41.843 16.109   66.152  1.00 86.24  ?  78   THR F N   1 
ATOM   15914 C  CA  . THR F 6  78   ? -40.756 16.348   67.097  1.00 86.31  ?  78   THR F CA  1 
ATOM   15915 C  C   . THR F 6  78   ? -39.454 16.683   66.378  1.00 92.29  ?  78   THR F C   1 
ATOM   15916 O  O   . THR F 6  78   ? -38.708 17.569   66.812  1.00 87.57  ?  78   THR F O   1 
ATOM   15917 C  CB  . THR F 6  78   ? -40.571 15.127   68.001  1.00 78.80  ?  78   THR F CB  1 
ATOM   15918 O  OG1 . THR F 6  78   ? -41.800 14.845   68.682  1.00 84.41  ?  78   THR F OG1 1 
ATOM   15919 C  CG2 . THR F 6  78   ? -39.477 15.378   69.028  1.00 86.79  ?  78   THR F CG2 1 
ATOM   15920 N  N   . VAL F 6  79   ? -39.165 15.994   65.275  1.00 119.64 ?  79   VAL F N   1 
ATOM   15921 C  CA  . VAL F 6  79   ? -37.908 16.165   64.560  1.00 119.82 ?  79   VAL F CA  1 
ATOM   15922 C  C   . VAL F 6  79   ? -38.132 16.672   63.135  1.00 119.34 ?  79   VAL F C   1 
ATOM   15923 O  O   . VAL F 6  79   ? -37.291 16.467   62.267  1.00 121.63 ?  79   VAL F O   1 
ATOM   15924 C  CB  . VAL F 6  79   ? -37.089 14.860   64.563  1.00 113.74 ?  79   VAL F CB  1 
ATOM   15925 C  CG1 . VAL F 6  79   ? -36.749 14.450   65.988  1.00 119.46 ?  79   VAL F CG1 1 
ATOM   15926 C  CG2 . VAL F 6  79   ? -37.851 13.749   63.855  1.00 104.70 ?  79   VAL F CG2 1 
ATOM   15927 N  N   . ARG F 6  80   ? -39.259 17.345   62.884  1.00 105.63 ?  80   ARG F N   1 
ATOM   15928 C  CA  . ARG F 6  80   ? -39.537 17.845   61.540  1.00 105.86 ?  80   ARG F CA  1 
ATOM   15929 C  C   . ARG F 6  80   ? -38.508 18.887   61.117  1.00 109.30 ?  80   ARG F C   1 
ATOM   15930 O  O   . ARG F 6  80   ? -37.935 18.802   60.024  1.00 107.74 ?  80   ARG F O   1 
ATOM   15931 C  CB  . ARG F 6  80   ? -40.950 18.426   61.472  1.00 111.04 ?  80   ARG F CB  1 
ATOM   15932 C  CG  . ARG F 6  80   ? -41.270 19.108   60.148  1.00 110.35 ?  80   ARG F CG  1 
ATOM   15933 C  CD  . ARG F 6  80   ? -42.737 19.500   60.055  1.00 112.19 ?  80   ARG F CD  1 
ATOM   15934 N  NE  . ARG F 6  80   ? -43.622 18.372   60.315  1.00 113.51 ?  80   ARG F NE  1 
ATOM   15935 C  CZ  . ARG F 6  80   ? -44.920 18.358   60.042  1.00 114.65 ?  80   ARG F CZ  1 
ATOM   15936 N  NH1 . ARG F 6  80   ? -45.522 19.402   59.494  1.00 117.54 ?  80   ARG F NH1 1 
ATOM   15937 N  NH2 . ARG F 6  80   ? -45.631 17.271   60.323  1.00 111.59 ?  80   ARG F NH2 1 
ATOM   15938 N  N   . ARG F 6  81   ? -38.260 19.881   61.974  1.00 112.65 ?  81   ARG F N   1 
ATOM   15939 C  CA  . ARG F 6  81   ? -37.282 20.914   61.646  1.00 110.82 ?  81   ARG F CA  1 
ATOM   15940 C  C   . ARG F 6  81   ? -35.876 20.342   61.545  1.00 108.01 ?  81   ARG F C   1 
ATOM   15941 O  O   . ARG F 6  81   ? -35.068 20.817   60.738  1.00 105.83 ?  81   ARG F O   1 
ATOM   15942 C  CB  . ARG F 6  81   ? -37.326 22.029   62.691  1.00 109.81 ?  81   ARG F CB  1 
ATOM   15943 C  CG  . ARG F 6  81   ? -38.507 22.974   62.545  1.00 119.19 ?  81   ARG F CG  1 
ATOM   15944 C  CD  . ARG F 6  81   ? -38.334 23.912   61.362  1.00 113.47 ?  81   ARG F CD  1 
ATOM   15945 N  NE  . ARG F 6  81   ? -39.616 24.269   60.766  1.00 118.53 ?  81   ARG F NE  1 
ATOM   15946 C  CZ  . ARG F 6  81   ? -40.299 25.366   61.061  1.00 129.24 ?  81   ARG F CZ  1 
ATOM   15947 N  NH1 . ARG F 6  81   ? -39.852 26.240   61.948  1.00 128.73 ?  81   ARG F NH1 1 
ATOM   15948 N  NH2 . ARG F 6  81   ? -41.460 25.591   60.453  1.00 137.15 ?  81   ARG F NH2 1 
ATOM   15949 N  N   . MET F 6  82   ? -35.564 19.328   62.354  1.00 122.84 ?  82   MET F N   1 
ATOM   15950 C  CA  . MET F 6  82   ? -34.256 18.689   62.271  1.00 126.92 ?  82   MET F CA  1 
ATOM   15951 C  C   . MET F 6  82   ? -34.108 17.908   60.972  1.00 122.19 ?  82   MET F C   1 
ATOM   15952 O  O   . MET F 6  82   ? -33.019 17.864   60.387  1.00 115.93 ?  82   MET F O   1 
ATOM   15953 C  CB  . MET F 6  82   ? -34.048 17.777   63.478  1.00 124.89 ?  82   MET F CB  1 
ATOM   15954 C  CG  . MET F 6  82   ? -33.999 18.517   64.803  1.00 130.97 ?  82   MET F CG  1 
ATOM   15955 S  SD  . MET F 6  82   ? -33.902 17.399   66.211  1.00 146.31 ?  82   MET F SD  1 
ATOM   15956 C  CE  . MET F 6  82   ? -32.239 16.768   66.020  1.00 129.58 ?  82   MET F CE  1 
ATOM   15957 N  N   . LEU F 6  83   ? -35.193 17.286   60.505  1.00 116.73 ?  83   LEU F N   1 
ATOM   15958 C  CA  . LEU F 6  83   ? -35.149 16.574   59.232  1.00 114.92 ?  83   LEU F CA  1 
ATOM   15959 C  C   . LEU F 6  83   ? -35.003 17.544   58.066  1.00 116.37 ?  83   LEU F C   1 
ATOM   15960 O  O   . LEU F 6  83   ? -34.310 17.246   57.086  1.00 112.16 ?  83   LEU F O   1 
ATOM   15961 C  CB  . LEU F 6  83   ? -36.405 15.718   59.065  1.00 111.22 ?  83   LEU F CB  1 
ATOM   15962 C  CG  . LEU F 6  83   ? -36.509 14.447   59.913  1.00 101.32 ?  83   LEU F CG  1 
ATOM   15963 C  CD1 . LEU F 6  83   ? -37.934 13.915   59.907  1.00 101.42 ?  83   LEU F CD1 1 
ATOM   15964 C  CD2 . LEU F 6  83   ? -35.538 13.385   59.430  1.00 98.53  ?  83   LEU F CD2 1 
ATOM   15965 N  N   . GLU F 6  84   ? -35.652 18.708   58.153  1.00 114.85 ?  84   GLU F N   1 
ATOM   15966 C  CA  . GLU F 6  84   ? -35.510 19.714   57.105  1.00 113.45 ?  84   GLU F CA  1 
ATOM   15967 C  C   . GLU F 6  84   ? -34.094 20.272   57.067  1.00 113.02 ?  84   GLU F C   1 
ATOM   15968 O  O   . GLU F 6  84   ? -33.545 20.517   55.986  1.00 109.52 ?  84   GLU F O   1 
ATOM   15969 C  CB  . GLU F 6  84   ? -36.523 20.839   57.317  1.00 107.87 ?  84   GLU F CB  1 
ATOM   15970 C  CG  . GLU F 6  84   ? -37.971 20.412   57.159  1.00 108.77 ?  84   GLU F CG  1 
ATOM   15971 C  CD  . GLU F 6  84   ? -38.943 21.419   57.736  1.00 113.60 ?  84   GLU F CD  1 
ATOM   15972 O  OE1 . GLU F 6  84   ? -38.494 22.506   58.156  1.00 114.57 ?  84   GLU F OE1 1 
ATOM   15973 O  OE2 . GLU F 6  84   ? -40.157 21.125   57.768  1.00 117.27 -1 84   GLU F OE2 1 
ATOM   15974 N  N   . ALA F 6  85   ? -33.486 20.478   58.238  1.00 124.04 ?  85   ALA F N   1 
ATOM   15975 C  CA  . ALA F 6  85   ? -32.120 20.987   58.287  1.00 125.74 ?  85   ALA F CA  1 
ATOM   15976 C  C   . ALA F 6  85   ? -31.130 19.963   57.745  1.00 124.61 ?  85   ALA F C   1 
ATOM   15977 O  O   . ALA F 6  85   ? -30.163 20.326   57.066  1.00 125.24 ?  85   ALA F O   1 
ATOM   15978 C  CB  . ALA F 6  85   ? -31.759 21.381   59.719  1.00 130.30 ?  85   ALA F CB  1 
ATOM   15979 N  N   . GLY F 6  86   ? -31.354 18.681   58.035  1.00 96.01  ?  86   GLY F N   1 
ATOM   15980 C  CA  . GLY F 6  86   ? -30.473 17.653   57.507  1.00 93.60  ?  86   GLY F CA  1 
ATOM   15981 C  C   . GLY F 6  86   ? -30.627 17.464   56.011  1.00 91.53  ?  86   GLY F C   1 
ATOM   15982 O  O   . GLY F 6  86   ? -29.651 17.189   55.307  1.00 90.49  ?  86   GLY F O   1 
ATOM   15983 N  N   . ALA F 6  87   ? -31.851 17.610   55.501  1.00 128.24 ?  87   ALA F N   1 
ATOM   15984 C  CA  . ALA F 6  87   ? -32.098 17.454   54.074  1.00 128.62 ?  87   ALA F CA  1 
ATOM   15985 C  C   . ALA F 6  87   ? -31.648 18.661   53.263  1.00 130.07 ?  87   ALA F C   1 
ATOM   15986 O  O   . ALA F 6  87   ? -31.411 18.527   52.058  1.00 127.24 ?  87   ALA F O   1 
ATOM   15987 C  CB  . ALA F 6  87   ? -33.583 17.191   53.820  1.00 119.80 ?  87   ALA F CB  1 
ATOM   15988 N  N   . ALA F 6  88   ? -31.524 19.831   53.892  1.00 108.95 ?  88   ALA F N   1 
ATOM   15989 C  CA  . ALA F 6  88   ? -31.107 21.032   53.180  1.00 106.68 ?  88   ALA F CA  1 
ATOM   15990 C  C   . ALA F 6  88   ? -29.624 21.032   52.834  1.00 116.82 ?  88   ALA F C   1 
ATOM   15991 O  O   . ALA F 6  88   ? -29.172 21.943   52.133  1.00 120.58 ?  88   ALA F O   1 
ATOM   15992 C  CB  . ALA F 6  88   ? -31.443 22.275   54.005  1.00 109.61 ?  88   ALA F CB  1 
ATOM   15993 N  N   . THR F 6  89   ? -28.864 20.046   53.304  1.00 117.87 ?  89   THR F N   1 
ATOM   15994 C  CA  . THR F 6  89   ? -27.443 19.943   53.002  1.00 115.67 ?  89   THR F CA  1 
ATOM   15995 C  C   . THR F 6  89   ? -27.168 19.194   51.705  1.00 110.61 ?  89   THR F C   1 
ATOM   15996 O  O   . THR F 6  89   ? -26.001 19.034   51.335  1.00 104.05 ?  89   THR F O   1 
ATOM   15997 C  CB  . THR F 6  89   ? -26.706 19.250   54.152  1.00 112.97 ?  89   THR F CB  1 
ATOM   15998 O  OG1 . THR F 6  89   ? -27.056 17.861   54.175  1.00 109.47 ?  89   THR F OG1 1 
ATOM   15999 C  CG2 . THR F 6  89   ? -27.082 19.880   55.483  1.00 114.20 ?  89   THR F CG2 1 
ATOM   16000 N  N   . LEU F 6  90   ? -28.210 18.735   51.014  1.00 106.30 ?  90   LEU F N   1 
ATOM   16001 C  CA  . LEU F 6  90   ? -28.008 17.948   49.801  1.00 102.46 ?  90   LEU F CA  1 
ATOM   16002 C  C   . LEU F 6  90   ? -27.305 18.705   48.676  1.00 104.55 ?  90   LEU F C   1 
ATOM   16003 O  O   . LEU F 6  90   ? -26.456 18.093   48.005  1.00 108.18 ?  90   LEU F O   1 
ATOM   16004 C  CB  . LEU F 6  90   ? -29.355 17.392   49.319  1.00 101.83 ?  90   LEU F CB  1 
ATOM   16005 C  CG  . LEU F 6  90   ? -29.838 16.108   49.999  1.00 96.69  ?  90   LEU F CG  1 
ATOM   16006 C  CD1 . LEU F 6  90   ? -31.316 15.877   49.726  1.00 93.80  ?  90   LEU F CD1 1 
ATOM   16007 C  CD2 . LEU F 6  90   ? -29.013 14.909   49.551  1.00 79.43  ?  90   LEU F CD2 1 
ATOM   16008 N  N   . PRO F 6  91   ? -27.599 19.985   48.398  1.00 127.77 ?  91   PRO F N   1 
ATOM   16009 C  CA  . PRO F 6  91   ? -26.869 20.661   47.308  1.00 129.90 ?  91   PRO F CA  1 
ATOM   16010 C  C   . PRO F 6  91   ? -25.366 20.721   47.525  1.00 134.19 ?  91   PRO F C   1 
ATOM   16011 O  O   . PRO F 6  91   ? -24.604 20.596   46.557  1.00 130.35 ?  91   PRO F O   1 
ATOM   16012 C  CB  . PRO F 6  91   ? -27.498 22.063   47.278  1.00 121.96 ?  91   PRO F CB  1 
ATOM   16013 C  CG  . PRO F 6  91   ? -28.198 22.210   48.588  1.00 126.06 ?  91   PRO F CG  1 
ATOM   16014 C  CD  . PRO F 6  91   ? -28.679 20.840   48.920  1.00 129.03 ?  91   PRO F CD  1 
ATOM   16015 N  N   . ILE F 6  92   ? -24.914 20.910   48.768  1.00 116.03 ?  92   ILE F N   1 
ATOM   16016 C  CA  . ILE F 6  92   ? -23.479 20.909   49.039  1.00 115.60 ?  92   ILE F CA  1 
ATOM   16017 C  C   . ILE F 6  92   ? -22.884 19.535   48.769  1.00 114.06 ?  92   ILE F C   1 
ATOM   16018 O  O   . ILE F 6  92   ? -21.731 19.422   48.332  1.00 115.01 ?  92   ILE F O   1 
ATOM   16019 C  CB  . ILE F 6  92   ? -23.202 21.369   50.484  1.00 114.54 ?  92   ILE F CB  1 
ATOM   16020 C  CG1 . ILE F 6  92   ? -23.993 22.638   50.804  1.00 108.77 ?  92   ILE F CG1 1 
ATOM   16021 C  CG2 . ILE F 6  92   ? -21.714 21.605   50.694  1.00 113.32 ?  92   ILE F CG2 1 
ATOM   16022 C  CD1 . ILE F 6  92   ? -23.531 23.854   50.031  1.00 99.48  ?  92   ILE F CD1 1 
ATOM   16023 N  N   . MET F 6  93   ? -23.654 18.472   49.015  1.00 135.47 ?  93   MET F N   1 
ATOM   16024 C  CA  . MET F 6  93   ? -23.170 17.125   48.732  1.00 135.28 ?  93   MET F CA  1 
ATOM   16025 C  C   . MET F 6  93   ? -22.957 16.910   47.240  1.00 131.97 ?  93   MET F C   1 
ATOM   16026 O  O   . MET F 6  93   ? -22.050 16.170   46.844  1.00 123.01 ?  93   MET F O   1 
ATOM   16027 C  CB  . MET F 6  93   ? -24.151 16.089   49.281  1.00 128.31 ?  93   MET F CB  1 
ATOM   16028 C  CG  . MET F 6  93   ? -24.333 16.140   50.789  1.00 125.70 ?  93   MET F CG  1 
ATOM   16029 S  SD  . MET F 6  93   ? -22.789 15.925   51.694  1.00 131.21 ?  93   MET F SD  1 
ATOM   16030 C  CE  . MET F 6  93   ? -22.676 17.503   52.534  1.00 137.22 ?  93   MET F CE  1 
ATOM   16031 N  N   . GLY F 6  94   ? -23.780 17.545   46.403  1.00 136.53 ?  94   GLY F N   1 
ATOM   16032 C  CA  . GLY F 6  94   ? -23.609 17.409   44.966  1.00 130.47 ?  94   GLY F CA  1 
ATOM   16033 C  C   . GLY F 6  94   ? -22.290 17.975   44.479  1.00 133.32 ?  94   GLY F C   1 
ATOM   16034 O  O   . GLY F 6  94   ? -21.634 17.390   43.612  1.00 132.59 ?  94   GLY F O   1 
ATOM   16035 N  N   . LEU F 6  95   ? -21.883 19.123   45.026  1.00 126.83 ?  95   LEU F N   1 
ATOM   16036 C  CA  . LEU F 6  95   ? -20.561 19.657   44.721  1.00 128.10 ?  95   LEU F CA  1 
ATOM   16037 C  C   . LEU F 6  95   ? -19.459 18.718   45.194  1.00 127.06 ?  95   LEU F C   1 
ATOM   16038 O  O   . LEU F 6  95   ? -18.411 18.610   44.545  1.00 130.76 ?  95   LEU F O   1 
ATOM   16039 C  CB  . LEU F 6  95   ? -20.399 21.040   45.354  1.00 127.35 ?  95   LEU F CB  1 
ATOM   16040 C  CG  . LEU F 6  95   ? -19.022 21.695   45.230  1.00 127.07 ?  95   LEU F CG  1 
ATOM   16041 C  CD1 . LEU F 6  95   ? -18.699 22.001   43.773  1.00 127.05 ?  95   LEU F CD1 1 
ATOM   16042 C  CD2 . LEU F 6  95   ? -18.942 22.956   46.076  1.00 125.90 ?  95   LEU F CD2 1 
ATOM   16043 N  N   . LEU F 6  96   ? -19.683 18.018   46.309  1.00 113.18 ?  96   LEU F N   1 
ATOM   16044 C  CA  . LEU F 6  96   ? -18.695 17.075   46.814  1.00 109.81 ?  96   LEU F CA  1 
ATOM   16045 C  C   . LEU F 6  96   ? -18.542 15.857   45.914  1.00 113.92 ?  96   LEU F C   1 
ATOM   16046 O  O   . LEU F 6  96   ? -17.561 15.120   46.055  1.00 113.43 ?  96   LEU F O   1 
ATOM   16047 C  CB  . LEU F 6  96   ? -19.064 16.627   48.230  1.00 106.94 ?  96   LEU F CB  1 
ATOM   16048 C  CG  . LEU F 6  96   ? -18.997 17.707   49.310  1.00 106.26 ?  96   LEU F CG  1 
ATOM   16049 C  CD1 . LEU F 6  96   ? -19.198 17.101   50.690  1.00 102.51 ?  96   LEU F CD1 1 
ATOM   16050 C  CD2 . LEU F 6  96   ? -17.674 18.457   49.235  1.00 106.49 ?  96   LEU F CD2 1 
ATOM   16051 N  N   . PHE F 6  97   ? -19.486 15.628   45.000  1.00 129.10 ?  97   PHE F N   1 
ATOM   16052 C  CA  . PHE F 6  97   ? -19.373 14.549   44.026  1.00 127.50 ?  97   PHE F CA  1 
ATOM   16053 C  C   . PHE F 6  97   ? -18.435 14.892   42.873  1.00 124.97 ?  97   PHE F C   1 
ATOM   16054 O  O   . PHE F 6  97   ? -18.035 13.982   42.136  1.00 122.46 ?  97   PHE F O   1 
ATOM   16055 C  CB  . PHE F 6  97   ? -20.762 14.188   43.483  1.00 122.26 ?  97   PHE F CB  1 
ATOM   16056 C  CG  . PHE F 6  97   ? -20.756 13.039   42.508  1.00 122.03 ?  97   PHE F CG  1 
ATOM   16057 C  CD1 . PHE F 6  97   ? -20.664 11.734   42.958  1.00 122.50 ?  97   PHE F CD1 1 
ATOM   16058 C  CD2 . PHE F 6  97   ? -20.841 13.266   41.142  1.00 118.20 ?  97   PHE F CD2 1 
ATOM   16059 C  CE1 . PHE F 6  97   ? -20.653 10.676   42.070  1.00 117.90 ?  97   PHE F CE1 1 
ATOM   16060 C  CE2 . PHE F 6  97   ? -20.828 12.210   40.248  1.00 113.23 ?  97   PHE F CE2 1 
ATOM   16061 C  CZ  . PHE F 6  97   ? -20.735 10.914   40.714  1.00 109.08 ?  97   PHE F CZ  1 
ATOM   16062 N  N   . ILE F 6  98   ? -18.071 16.172   42.717  1.00 90.77  ?  98   ILE F N   1 
ATOM   16063 C  CA  . ILE F 6  98   ? -17.206 16.584   41.607  1.00 93.36  ?  98   ILE F CA  1 
ATOM   16064 C  C   . ILE F 6  98   ? -15.890 15.809   41.592  1.00 95.10  ?  98   ILE F C   1 
ATOM   16065 O  O   . ILE F 6  98   ? -15.466 15.380   40.508  1.00 95.47  ?  98   ILE F O   1 
ATOM   16066 C  CB  . ILE F 6  98   ? -17.007 18.098   41.616  1.00 92.45  ?  98   ILE F CB  1 
ATOM   16067 C  CG1 . ILE F 6  98   ? -18.311 18.809   41.249  1.00 98.73  ?  98   ILE F CG1 1 
ATOM   16068 C  CG2 . ILE F 6  98   ? -15.882 18.501   40.674  1.00 92.47  ?  98   ILE F CG2 1 
ATOM   16069 C  CD1 . ILE F 6  98   ? -18.929 18.300   39.957  1.00 101.66 ?  98   ILE F CD1 1 
ATOM   16070 N  N   . PRO F 6  99   ? -15.198 15.598   42.722  1.00 114.05 ?  99   PRO F N   1 
ATOM   16071 C  CA  . PRO F 6  99   ? -13.964 14.792   42.657  1.00 117.64 ?  99   PRO F CA  1 
ATOM   16072 C  C   . PRO F 6  99   ? -14.168 13.395   42.095  1.00 116.55 ?  99   PRO F C   1 
ATOM   16073 O  O   . PRO F 6  99   ? -13.326 12.919   41.323  1.00 114.74 ?  99   PRO F O   1 
ATOM   16074 C  CB  . PRO F 6  99   ? -13.504 14.751   44.119  1.00 116.22 ?  99   PRO F CB  1 
ATOM   16075 C  CG  . PRO F 6  99   ? -13.996 16.019   44.691  1.00 107.65 ?  99   PRO F CG  1 
ATOM   16076 C  CD  . PRO F 6  99   ? -15.336 16.255   44.036  1.00 109.80 ?  99   PRO F CD  1 
ATOM   16077 N  N   . ILE F 6  100  ? -15.259 12.719   42.463  1.00 113.74 ?  100  ILE F N   1 
ATOM   16078 C  CA  . ILE F 6  100  ? -15.496 11.369   41.958  1.00 106.41 ?  100  ILE F CA  1 
ATOM   16079 C  C   . ILE F 6  100  ? -15.725 11.398   40.454  1.00 107.40 ?  100  ILE F C   1 
ATOM   16080 O  O   . ILE F 6  100  ? -15.231 10.534   39.718  1.00 110.72 ?  100  ILE F O   1 
ATOM   16081 C  CB  . ILE F 6  100  ? -16.678 10.718   42.696  1.00 104.38 ?  100  ILE F CB  1 
ATOM   16082 C  CG1 . ILE F 6  100  ? -16.429 10.717   44.205  1.00 106.82 ?  100  ILE F CG1 1 
ATOM   16083 C  CG2 . ILE F 6  100  ? -16.909 9.304    42.185  1.00 102.84 ?  100  ILE F CG2 1 
ATOM   16084 C  CD1 . ILE F 6  100  ? -17.531 10.053   44.999  1.00 100.34 ?  100  ILE F CD1 1 
ATOM   16085 N  N   . ALA F 6  101  ? -16.474 12.394   39.972  1.00 121.13 ?  101  ALA F N   1 
ATOM   16086 C  CA  . ALA F 6  101  ? -16.710 12.515   38.538  1.00 118.77 ?  101  ALA F CA  1 
ATOM   16087 C  C   . ALA F 6  101  ? -15.416 12.806   37.789  1.00 118.38 ?  101  ALA F C   1 
ATOM   16088 O  O   . ALA F 6  101  ? -15.205 12.303   36.680  1.00 114.55 ?  101  ALA F O   1 
ATOM   16089 C  CB  . ALA F 6  101  ? -17.748 13.603   38.265  1.00 118.65 ?  101  ALA F CB  1 
ATOM   16090 N  N   . LEU F 6  102  ? -14.536 13.616   38.384  1.00 98.72  ?  102  LEU F N   1 
ATOM   16091 C  CA  . LEU F 6  102  ? -13.234 13.869   37.777  1.00 99.67  ?  102  LEU F CA  1 
ATOM   16092 C  C   . LEU F 6  102  ? -12.421 12.588   37.652  1.00 97.10  ?  102  LEU F C   1 
ATOM   16093 O  O   . LEU F 6  102  ? -11.563 12.480   36.769  1.00 103.17 ?  102  LEU F O   1 
ATOM   16094 C  CB  . LEU F 6  102  ? -12.465 14.905   38.599  1.00 95.65  ?  102  LEU F CB  1 
ATOM   16095 C  CG  . LEU F 6  102  ? -13.002 16.337   38.599  1.00 92.49  ?  102  LEU F CG  1 
ATOM   16096 C  CD1 . LEU F 6  102  ? -12.171 17.222   39.515  1.00 86.18  ?  102  LEU F CD1 1 
ATOM   16097 C  CD2 . LEU F 6  102  ? -13.030 16.900   37.188  1.00 103.63 ?  102  LEU F CD2 1 
ATOM   16098 N  N   . GLY F 6  103  ? -12.681 11.608   38.519  1.00 128.32 ?  103  GLY F N   1 
ATOM   16099 C  CA  . GLY F 6  103  ? -11.919 10.371   38.472  1.00 133.35 ?  103  GLY F CA  1 
ATOM   16100 C  C   . GLY F 6  103  ? -12.230 9.535    37.245  1.00 130.44 ?  103  GLY F C   1 
ATOM   16101 O  O   . GLY F 6  103  ? -11.321 9.027    36.582  1.00 133.94 ?  103  GLY F O   1 
ATOM   16102 N  N   . TYR F 6  104  ? -13.513 9.377    36.924  1.00 106.56 ?  104  TYR F N   1 
ATOM   16103 C  CA  . TYR F 6  104  ? -13.918 8.527    35.812  1.00 101.67 ?  104  TYR F CA  1 
ATOM   16104 C  C   . TYR F 6  104  ? -14.043 9.282    34.493  1.00 105.17 ?  104  TYR F C   1 
ATOM   16105 O  O   . TYR F 6  104  ? -14.519 8.706    33.510  1.00 99.76  ?  104  TYR F O   1 
ATOM   16106 C  CB  . TYR F 6  104  ? -15.231 7.797    36.140  1.00 103.08 ?  104  TYR F CB  1 
ATOM   16107 C  CG  . TYR F 6  104  ? -16.453 8.660    36.422  1.00 98.73  ?  104  TYR F CG  1 
ATOM   16108 C  CD1 . TYR F 6  104  ? -17.025 9.453    35.432  1.00 96.73  ?  104  TYR F CD1 1 
ATOM   16109 C  CD2 . TYR F 6  104  ? -17.056 8.647    37.674  1.00 105.60 ?  104  TYR F CD2 1 
ATOM   16110 C  CE1 . TYR F 6  104  ? -18.145 10.223   35.688  1.00 104.15 ?  104  TYR F CE1 1 
ATOM   16111 C  CE2 . TYR F 6  104  ? -18.178 9.413    37.938  1.00 106.12 ?  104  TYR F CE2 1 
ATOM   16112 C  CZ  . TYR F 6  104  ? -18.717 10.199   36.942  1.00 106.03 ?  104  TYR F CZ  1 
ATOM   16113 O  OH  . TYR F 6  104  ? -19.832 10.964   37.202  1.00 105.39 ?  104  TYR F OH  1 
ATOM   16114 N  N   . PHE F 6  105  ? -13.635 10.545   34.446  1.00 115.68 ?  105  PHE F N   1 
ATOM   16115 C  CA  . PHE F 6  105  ? -13.584 11.293   33.202  1.00 115.29 ?  105  PHE F CA  1 
ATOM   16116 C  C   . PHE F 6  105  ? -12.161 11.263   32.649  1.00 119.17 ?  105  PHE F C   1 
ATOM   16117 O  O   . PHE F 6  105  ? -11.279 10.574   33.172  1.00 126.01 ?  105  PHE F O   1 
ATOM   16118 C  CB  . PHE F 6  105  ? -14.080 12.725   33.417  1.00 112.68 ?  105  PHE F CB  1 
ATOM   16119 C  CG  . PHE F 6  105  ? -15.527 12.923   33.066  1.00 104.68 ?  105  PHE F CG  1 
ATOM   16120 C  CD1 . PHE F 6  105  ? -15.965 12.745   31.764  1.00 99.70  ?  105  PHE F CD1 1 
ATOM   16121 C  CD2 . PHE F 6  105  ? -16.445 13.297   34.033  1.00 98.97  ?  105  PHE F CD2 1 
ATOM   16122 C  CE1 . PHE F 6  105  ? -17.294 12.926   31.434  1.00 91.71  ?  105  PHE F CE1 1 
ATOM   16123 C  CE2 . PHE F 6  105  ? -17.775 13.481   33.709  1.00 99.71  ?  105  PHE F CE2 1 
ATOM   16124 C  CZ  . PHE F 6  105  ? -18.200 13.296   32.407  1.00 98.80  ?  105  PHE F CZ  1 
ATOM   16125 N  N   . ASP F 6  106  ? -11.925 12.024   31.579  1.00 96.45  ?  106  ASP F N   1 
ATOM   16126 C  CA  . ASP F 6  106  ? -10.595 12.088   30.984  1.00 106.38 ?  106  ASP F CA  1 
ATOM   16127 C  C   . ASP F 6  106  ? -9.589  12.824   31.859  1.00 112.01 ?  106  ASP F C   1 
ATOM   16128 O  O   . ASP F 6  106  ? -8.423  12.935   31.464  1.00 111.00 ?  106  ASP F O   1 
ATOM   16129 C  CB  . ASP F 6  106  ? -10.665 12.751   29.607  1.00 113.66 ?  106  ASP F CB  1 
ATOM   16130 C  CG  . ASP F 6  106  ? -9.735  12.101   28.600  1.00 117.75 ?  106  ASP F CG  1 
ATOM   16131 O  OD1 . ASP F 6  106  ? -9.082  11.096   28.954  1.00 119.14 ?  106  ASP F OD1 1 
ATOM   16132 O  OD2 . ASP F 6  106  ? -9.656  12.595   27.455  1.00 118.38 -1 106  ASP F OD2 1 
ATOM   16133 N  N   . THR F 6  107  ? -10.002 13.321   33.028  1.00 132.31 ?  107  THR F N   1 
ATOM   16134 C  CA  . THR F 6  107  ? -9.071  13.974   33.941  1.00 132.37 ?  107  THR F CA  1 
ATOM   16135 C  C   . THR F 6  107  ? -8.033  13.002   34.490  1.00 137.99 ?  107  THR F C   1 
ATOM   16136 O  O   . THR F 6  107  ? -7.008  13.443   35.019  1.00 144.32 ?  107  THR F O   1 
ATOM   16137 C  CB  . THR F 6  107  ? -9.837  14.634   35.090  1.00 129.75 ?  107  THR F CB  1 
ATOM   16138 O  OG1 . THR F 6  107  ? -11.064 15.184   34.593  1.00 122.37 ?  107  THR F OG1 1 
ATOM   16139 C  CG2 . THR F 6  107  ? -9.016  15.755   35.712  1.00 133.76 ?  107  THR F CG2 1 
ATOM   16140 N  N   . TYR F 6  108  ? -8.271  11.697   34.371  1.00 188.33 ?  108  TYR F N   1 
ATOM   16141 C  CA  . TYR F 6  108  ? -7.262  10.717   34.741  1.00 190.18 ?  108  TYR F CA  1 
ATOM   16142 C  C   . TYR F 6  108  ? -6.040  10.866   33.831  1.00 200.25 ?  108  TYR F C   1 
ATOM   16143 O  O   . TYR F 6  108  ? -6.073  11.561   32.811  1.00 199.66 ?  108  TYR F O   1 
ATOM   16144 C  CB  . TYR F 6  108  ? -7.862  9.307    34.708  1.00 186.60 ?  108  TYR F CB  1 
ATOM   16145 C  CG  . TYR F 6  108  ? -7.759  8.550    33.396  1.00 195.15 ?  108  TYR F CG  1 
ATOM   16146 C  CD1 . TYR F 6  108  ? -6.600  7.865    33.042  1.00 190.17 ?  108  TYR F CD1 1 
ATOM   16147 C  CD2 . TYR F 6  108  ? -8.832  8.514    32.515  1.00 191.40 ?  108  TYR F CD2 1 
ATOM   16148 C  CE1 . TYR F 6  108  ? -6.514  7.173    31.849  1.00 183.27 ?  108  TYR F CE1 1 
ATOM   16149 C  CE2 . TYR F 6  108  ? -8.754  7.826    31.320  1.00 181.23 ?  108  TYR F CE2 1 
ATOM   16150 C  CZ  . TYR F 6  108  ? -7.594  7.158    30.992  1.00 185.28 ?  108  TYR F CZ  1 
ATOM   16151 O  OH  . TYR F 6  108  ? -7.513  6.471    29.803  1.00 194.69 ?  108  TYR F OH  1 
ATOM   16152 N  N   . LYS F 6  109  ? -4.947  10.207   34.236  1.00 178.15 ?  109  LYS F N   1 
ATOM   16153 C  CA  . LYS F 6  109  ? -3.585  10.420   33.740  1.00 179.05 ?  109  LYS F CA  1 
ATOM   16154 C  C   . LYS F 6  109  ? -3.022  11.705   34.340  1.00 178.52 ?  109  LYS F C   1 
ATOM   16155 O  O   . LYS F 6  109  ? -1.802  11.891   34.402  1.00 180.53 ?  109  LYS F O   1 
ATOM   16156 C  CB  . LYS F 6  109  ? -3.520  10.448   32.208  1.00 171.24 ?  109  LYS F CB  1 
ATOM   16157 C  CG  . LYS F 6  109  ? -3.539  9.071    31.565  1.00 166.86 ?  109  LYS F CG  1 
ATOM   16158 C  CD  . LYS F 6  109  ? -3.781  9.155    30.067  1.00 164.13 ?  109  LYS F CD  1 
ATOM   16159 C  CE  . LYS F 6  109  ? -2.697  9.962    29.370  1.00 165.97 ?  109  LYS F CE  1 
ATOM   16160 N  NZ  . LYS F 6  109  ? -2.961  10.091   27.909  1.00 168.75 ?  109  LYS F NZ  1 
ATOM   16161 N  N   . ALA F 6  110  ? -3.906  12.594   34.779  1.00 127.40 ?  110  ALA F N   1 
ATOM   16162 C  CA  . ALA F 6  110  ? -3.580  13.678   35.691  1.00 124.58 ?  110  ALA F CA  1 
ATOM   16163 C  C   . ALA F 6  110  ? -4.110  13.326   37.074  1.00 123.57 ?  110  ALA F C   1 
ATOM   16164 O  O   . ALA F 6  110  ? -4.786  12.311   37.263  1.00 122.03 ?  110  ALA F O   1 
ATOM   16165 C  CB  . ALA F 6  110  ? -4.164  15.009   35.203  1.00 122.53 ?  110  ALA F CB  1 
ATOM   16166 N  N   . LEU F 6  111  ? -3.785  14.173   38.049  1.00 124.68 ?  111  LEU F N   1 
ATOM   16167 C  CA  . LEU F 6  111  ? -4.149  13.989   39.452  1.00 128.05 ?  111  LEU F CA  1 
ATOM   16168 C  C   . LEU F 6  111  ? -3.524  12.740   40.068  1.00 132.56 ?  111  LEU F C   1 
ATOM   16169 O  O   . LEU F 6  111  ? -3.833  12.401   41.216  1.00 134.85 ?  111  LEU F O   1 
ATOM   16170 C  CB  . LEU F 6  111  ? -5.674  13.952   39.645  1.00 122.13 ?  111  LEU F CB  1 
ATOM   16171 C  CG  . LEU F 6  111  ? -6.436  15.274   39.785  1.00 116.64 ?  111  LEU F CG  1 
ATOM   16172 C  CD1 . LEU F 6  111  ? -6.343  16.114   38.519  1.00 117.44 ?  111  LEU F CD1 1 
ATOM   16173 C  CD2 . LEU F 6  111  ? -7.891  15.012   40.148  1.00 107.77 ?  111  LEU F CD2 1 
ATOM   16174 N  N   . GLY F 6  112  ? -2.654  12.043   39.336  1.00 157.26 ?  112  GLY F N   1 
ATOM   16175 C  CA  . GLY F 6  112  ? -1.953  10.888   39.856  1.00 153.76 ?  112  GLY F CA  1 
ATOM   16176 C  C   . GLY F 6  112  ? -2.593  9.545    39.575  1.00 151.59 ?  112  GLY F C   1 
ATOM   16177 O  O   . GLY F 6  112  ? -2.073  8.523    40.041  1.00 151.58 ?  112  GLY F O   1 
ATOM   16178 N  N   . LEU F 6  113  ? -3.694  9.505    38.829  1.00 156.04 ?  113  LEU F N   1 
ATOM   16179 C  CA  . LEU F 6  113  ? -4.406  8.259    38.562  1.00 152.57 ?  113  LEU F CA  1 
ATOM   16180 C  C   . LEU F 6  113  ? -3.798  7.586    37.335  1.00 149.25 ?  113  LEU F C   1 
ATOM   16181 O  O   . LEU F 6  113  ? -3.952  8.073    36.210  1.00 149.17 ?  113  LEU F O   1 
ATOM   16182 C  CB  . LEU F 6  113  ? -5.896  8.522    38.363  1.00 149.08 ?  113  LEU F CB  1 
ATOM   16183 C  CG  . LEU F 6  113  ? -6.669  8.986    39.599  1.00 144.94 ?  113  LEU F CG  1 
ATOM   16184 C  CD1 . LEU F 6  113  ? -8.158  9.080    39.302  1.00 136.44 ?  113  LEU F CD1 1 
ATOM   16185 C  CD2 . LEU F 6  113  ? -6.411  8.058    40.777  1.00 141.44 ?  113  LEU F CD2 1 
ATOM   16186 N  N   . GLU F 6  114  ? -3.106  6.466    37.553  1.00 145.25 ?  114  GLU F N   1 
ATOM   16187 C  CA  . GLU F 6  114  ? -2.556  5.703    36.437  1.00 147.88 ?  114  GLU F CA  1 
ATOM   16188 C  C   . GLU F 6  114  ? -3.667  5.086    35.597  1.00 138.28 ?  114  GLU F C   1 
ATOM   16189 O  O   . GLU F 6  114  ? -3.714  5.269    34.375  1.00 134.68 ?  114  GLU F O   1 
ATOM   16190 C  CB  . GLU F 6  114  ? -1.609  4.621    36.958  1.00 155.53 ?  114  GLU F CB  1 
ATOM   16191 C  CG  . GLU F 6  114  ? -0.946  3.797    35.865  1.00 152.17 ?  114  GLU F CG  1 
ATOM   16192 C  CD  . GLU F 6  114  ? -0.083  2.680    36.420  1.00 142.96 ?  114  GLU F CD  1 
ATOM   16193 O  OE1 . GLU F 6  114  ? -0.093  2.476    37.652  1.00 144.16 ?  114  GLU F OE1 1 
ATOM   16194 O  OE2 . GLU F 6  114  ? 0.602   2.004    35.623  1.00 130.31 -1 114  GLU F OE2 1 
ATOM   16195 N  N   . HIS F 6  115  ? -4.568  4.347    36.237  1.00 160.87 ?  115  HIS F N   1 
ATOM   16196 C  CA  . HIS F 6  115  ? -5.731  3.766    35.594  1.00 156.90 ?  115  HIS F CA  1 
ATOM   16197 C  C   . HIS F 6  115  ? -7.003  4.443    36.096  1.00 154.49 ?  115  HIS F C   1 
ATOM   16198 O  O   . HIS F 6  115  ? -7.042  4.937    37.227  1.00 155.90 ?  115  HIS F O   1 
ATOM   16199 C  CB  . HIS F 6  115  ? -5.811  2.256    35.855  1.00 152.02 ?  115  HIS F CB  1 
ATOM   16200 C  CG  . HIS F 6  115  ? -5.977  1.900    37.299  1.00 158.36 ?  115  HIS F CG  1 
ATOM   16201 N  ND1 . HIS F 6  115  ? -4.930  1.920    38.196  1.00 165.96 ?  115  HIS F ND1 1 
ATOM   16202 C  CD2 . HIS F 6  115  ? -7.066  1.505    38.002  1.00 161.99 ?  115  HIS F CD2 1 
ATOM   16203 C  CE1 . HIS F 6  115  ? -5.367  1.558    39.389  1.00 171.10 ?  115  HIS F CE1 1 
ATOM   16204 N  NE2 . HIS F 6  115  ? -6.660  1.301    39.298  1.00 171.80 ?  115  HIS F NE2 1 
ATOM   16205 N  N   . PRO F 6  116  ? -8.052  4.500    35.273  1.00 118.70 ?  116  PRO F N   1 
ATOM   16206 C  CA  . PRO F 6  116  ? -9.279  5.192    35.683  1.00 113.99 ?  116  PRO F CA  1 
ATOM   16207 C  C   . PRO F 6  116  ? -9.863  4.621    36.967  1.00 116.81 ?  116  PRO F C   1 
ATOM   16208 O  O   . PRO F 6  116  ? -9.624  3.471    37.342  1.00 113.05 ?  116  PRO F O   1 
ATOM   16209 C  CB  . PRO F 6  116  ? -10.224 4.971    34.496  1.00 106.43 ?  116  PRO F CB  1 
ATOM   16210 C  CG  . PRO F 6  116  ? -9.313  4.794    33.333  1.00 111.17 ?  116  PRO F CG  1 
ATOM   16211 C  CD  . PRO F 6  116  ? -8.105  4.072    33.864  1.00 118.34 ?  116  PRO F CD  1 
ATOM   16212 N  N   . LEU F 6  117  ? -10.649 5.461    37.644  1.00 117.81 ?  117  LEU F N   1 
ATOM   16213 C  CA  . LEU F 6  117  ? -11.190 5.097    38.949  1.00 111.84 ?  117  LEU F CA  1 
ATOM   16214 C  C   . LEU F 6  117  ? -12.207 3.966    38.850  1.00 106.08 ?  117  LEU F C   1 
ATOM   16215 O  O   . LEU F 6  117  ? -12.332 3.166    39.784  1.00 101.32 ?  117  LEU F O   1 
ATOM   16216 C  CB  . LEU F 6  117  ? -11.814 6.328    39.606  1.00 111.50 ?  117  LEU F CB  1 
ATOM   16217 C  CG  . LEU F 6  117  ? -12.366 6.191    41.023  1.00 115.26 ?  117  LEU F CG  1 
ATOM   16218 C  CD1 . LEU F 6  117  ? -11.259 5.814    41.992  1.00 115.56 ?  117  LEU F CD1 1 
ATOM   16219 C  CD2 . LEU F 6  117  ? -13.027 7.494    41.441  1.00 119.14 ?  117  LEU F CD2 1 
ATOM   16220 N  N   . TYR F 6  118  ? -12.932 3.877    37.739  1.00 114.40 ?  118  TYR F N   1 
ATOM   16221 C  CA  . TYR F 6  118  ? -13.922 2.833    37.529  1.00 115.08 ?  118  TYR F CA  1 
ATOM   16222 C  C   . TYR F 6  118  ? -13.515 1.958    36.351  1.00 113.50 ?  118  TYR F C   1 
ATOM   16223 O  O   . TYR F 6  118  ? -12.851 2.415    35.416  1.00 108.82 ?  118  TYR F O   1 
ATOM   16224 C  CB  . TYR F 6  118  ? -15.315 3.427    37.285  1.00 106.96 ?  118  TYR F CB  1 
ATOM   16225 C  CG  . TYR F 6  118  ? -16.007 3.904    38.543  1.00 108.74 ?  118  TYR F CG  1 
ATOM   16226 C  CD1 . TYR F 6  118  ? -16.818 3.050    39.279  1.00 107.16 ?  118  TYR F CD1 1 
ATOM   16227 C  CD2 . TYR F 6  118  ? -15.850 5.208    38.994  1.00 108.09 ?  118  TYR F CD2 1 
ATOM   16228 C  CE1 . TYR F 6  118  ? -17.453 3.481    40.429  1.00 102.79 ?  118  TYR F CE1 1 
ATOM   16229 C  CE2 . TYR F 6  118  ? -16.481 5.648    40.143  1.00 104.85 ?  118  TYR F CE2 1 
ATOM   16230 C  CZ  . TYR F 6  118  ? -17.281 4.781    40.856  1.00 106.48 ?  118  TYR F CZ  1 
ATOM   16231 O  OH  . TYR F 6  118  ? -17.910 5.215    42.000  1.00 108.73 ?  118  TYR F OH  1 
ATOM   16232 N  N   . GLU F 6  119  ? -13.922 0.687    36.408  1.00 140.61 ?  119  GLU F N   1 
ATOM   16233 C  CA  . GLU F 6  119  ? -13.557 -0.255   35.355  1.00 139.10 ?  119  GLU F CA  1 
ATOM   16234 C  C   . GLU F 6  119  ? -14.249 0.083    34.040  1.00 134.91 ?  119  GLU F C   1 
ATOM   16235 O  O   . GLU F 6  119  ? -13.657 -0.071   32.965  1.00 136.66 ?  119  GLU F O   1 
ATOM   16236 C  CB  . GLU F 6  119  ? -13.896 -1.682   35.786  1.00 135.89 ?  119  GLU F CB  1 
ATOM   16237 C  CG  . GLU F 6  119  ? -13.380 -2.060   37.164  1.00 144.10 ?  119  GLU F CG  1 
ATOM   16238 C  CD  . GLU F 6  119  ? -13.110 -3.547   37.293  1.00 153.52 ?  119  GLU F CD  1 
ATOM   16239 O  OE1 . GLU F 6  119  ? -13.312 -4.277   36.300  1.00 145.05 ?  119  GLU F OE1 1 
ATOM   16240 O  OE2 . GLU F 6  119  ? -12.697 -3.986   38.387  1.00 164.10 -1 119  GLU F OE2 1 
ATOM   16241 N  N   . TRP F 6  120  ? -15.497 0.544    34.102  1.00 96.43  ?  120  TRP F N   1 
ATOM   16242 C  CA  . TRP F 6  120  ? -16.257 0.860    32.898  1.00 91.89  ?  120  TRP F CA  1 
ATOM   16243 C  C   . TRP F 6  120  ? -15.829 2.168    32.247  1.00 99.89  ?  120  TRP F C   1 
ATOM   16244 O  O   . TRP F 6  120  ? -16.366 2.518    31.190  1.00 96.12  ?  120  TRP F O   1 
ATOM   16245 C  CB  . TRP F 6  120  ? -17.755 0.905    33.217  1.00 87.78  ?  120  TRP F CB  1 
ATOM   16246 C  CG  . TRP F 6  120  ? -18.087 1.624    34.489  1.00 93.60  ?  120  TRP F CG  1 
ATOM   16247 C  CD1 . TRP F 6  120  ? -18.366 1.060    35.700  1.00 96.53  ?  120  TRP F CD1 1 
ATOM   16248 C  CD2 . TRP F 6  120  ? -18.189 3.041    34.674  1.00 97.41  ?  120  TRP F CD2 1 
ATOM   16249 N  NE1 . TRP F 6  120  ? -18.627 2.037    36.629  1.00 92.32  ?  120  TRP F NE1 1 
ATOM   16250 C  CE2 . TRP F 6  120  ? -18.526 3.262    36.024  1.00 96.92  ?  120  TRP F CE2 1 
ATOM   16251 C  CE3 . TRP F 6  120  ? -18.025 4.145    33.831  1.00 95.32  ?  120  TRP F CE3 1 
ATOM   16252 C  CZ2 . TRP F 6  120  ? -18.702 4.540    36.550  1.00 98.55  ?  120  TRP F CZ2 1 
ATOM   16253 C  CZ3 . TRP F 6  120  ? -18.200 5.412    34.355  1.00 96.82  ?  120  TRP F CZ3 1 
ATOM   16254 C  CH2 . TRP F 6  120  ? -18.535 5.600    35.702  1.00 99.76  ?  120  TRP F CH2 1 
ATOM   16255 N  N   . ALA F 6  121  ? -14.885 2.894    32.842  1.00 113.21 ?  121  ALA F N   1 
ATOM   16256 C  CA  . ALA F 6  121  ? -14.365 4.126    32.267  1.00 114.81 ?  121  ALA F CA  1 
ATOM   16257 C  C   . ALA F 6  121  ? -12.985 3.952    31.647  1.00 116.69 ?  121  ALA F C   1 
ATOM   16258 O  O   . ALA F 6  121  ? -12.434 4.919    31.112  1.00 108.47 ?  121  ALA F O   1 
ATOM   16259 C  CB  . ALA F 6  121  ? -14.319 5.228    33.331  1.00 114.93 ?  121  ALA F CB  1 
ATOM   16260 N  N   . ASN F 6  122  ? -12.416 2.750    31.707  1.00 134.31 ?  122  ASN F N   1 
ATOM   16261 C  CA  . ASN F 6  122  ? -11.102 2.493    31.133  1.00 133.46 ?  122  ASN F CA  1 
ATOM   16262 C  C   . ASN F 6  122  ? -11.250 2.157    29.655  1.00 131.52 ?  122  ASN F C   1 
ATOM   16263 O  O   . ASN F 6  122  ? -11.947 1.189    29.321  1.00 125.37 ?  122  ASN F O   1 
ATOM   16264 C  CB  . ASN F 6  122  ? -10.413 1.350    31.862  1.00 130.23 ?  122  ASN F CB  1 
ATOM   16265 C  CG  . ASN F 6  122  ? -8.925  1.283    31.572  1.00 133.02 ?  122  ASN F CG  1 
ATOM   16266 O  OD1 . ASN F 6  122  ? -8.335  2.236    31.063  1.00 136.53 ?  122  ASN F OD1 1 
ATOM   16267 N  ND2 . ASN F 6  122  ? -8.309  0.153    31.901  1.00 135.52 ?  122  ASN F ND2 1 
ATOM   16268 N  N   . PRO F 6  123  ? -10.633 2.916    28.747  1.00 121.36 ?  123  PRO F N   1 
ATOM   16269 C  CA  . PRO F 6  123  ? -10.775 2.608    27.313  1.00 115.47 ?  123  PRO F CA  1 
ATOM   16270 C  C   . PRO F 6  123  ? -10.212 1.254    26.919  1.00 114.84 ?  123  PRO F C   1 
ATOM   16271 O  O   . PRO F 6  123  ? -10.583 0.733    25.860  1.00 113.04 ?  123  PRO F O   1 
ATOM   16272 C  CB  . PRO F 6  123  ? -10.009 3.751    26.630  1.00 113.31 ?  123  PRO F CB  1 
ATOM   16273 C  CG  . PRO F 6  123  ? -9.966  4.847    27.648  1.00 118.73 ?  123  PRO F CG  1 
ATOM   16274 C  CD  . PRO F 6  123  ? -9.871  4.156    28.973  1.00 120.81 ?  123  PRO F CD  1 
ATOM   16275 N  N   . GLU F 6  124  ? -9.333  0.667    27.730  1.00 153.32 ?  124  GLU F N   1 
ATOM   16276 C  CA  . GLU F 6  124  ? -8.756  -0.634   27.418  1.00 157.77 ?  124  GLU F CA  1 
ATOM   16277 C  C   . GLU F 6  124  ? -9.717  -1.790   27.664  1.00 155.71 ?  124  GLU F C   1 
ATOM   16278 O  O   . GLU F 6  124  ? -9.396  -2.925   27.295  1.00 154.31 ?  124  GLU F O   1 
ATOM   16279 C  CB  . GLU F 6  124  ? -7.482  -0.855   28.240  1.00 161.31 ?  124  GLU F CB  1 
ATOM   16280 C  CG  . GLU F 6  124  ? -6.608  0.381    28.395  1.00 156.31 ?  124  GLU F CG  1 
ATOM   16281 C  CD  . GLU F 6  124  ? -5.976  0.819    27.088  1.00 161.98 ?  124  GLU F CD  1 
ATOM   16282 O  OE1 . GLU F 6  124  ? -5.702  -0.054   26.236  1.00 152.70 ?  124  GLU F OE1 1 
ATOM   16283 O  OE2 . GLU F 6  124  ? -5.751  2.035    26.913  1.00 175.14 -1 124  GLU F OE2 1 
ATOM   16284 N  N   . VAL F 6  125  ? -10.876 -1.536   28.264  1.00 94.54  ?  125  VAL F N   1 
ATOM   16285 C  CA  . VAL F 6  125  ? -11.802 -2.583   28.679  1.00 80.12  ?  125  VAL F CA  1 
ATOM   16286 C  C   . VAL F 6  125  ? -13.093 -2.544   27.867  1.00 79.82  ?  125  VAL F C   1 
ATOM   16287 O  O   . VAL F 6  125  ? -13.520 -3.560   27.316  1.00 84.69  ?  125  VAL F O   1 
ATOM   16288 C  CB  . VAL F 6  125  ? -12.099 -2.486   30.192  1.00 77.65  ?  125  VAL F CB  1 
ATOM   16289 C  CG1 . VAL F 6  125  ? -13.222 -3.436   30.577  1.00 74.00  ?  125  VAL F CG1 1 
ATOM   16290 C  CG2 . VAL F 6  125  ? -10.841 -2.775   30.999  1.00 84.61  ?  125  VAL F CG2 1 
ATOM   16291 N  N   . VAL F 6  126  ? -13.731 -1.373   27.785  1.00 108.59 ?  126  VAL F N   1 
ATOM   16292 C  CA  . VAL F 6  126  ? -15.045 -1.273   27.150  1.00 112.50 ?  126  VAL F CA  1 
ATOM   16293 C  C   . VAL F 6  126  ? -14.986 -1.262   25.631  1.00 112.62 ?  126  VAL F C   1 
ATOM   16294 O  O   . VAL F 6  126  ? -16.030 -1.414   24.984  1.00 113.04 ?  126  VAL F O   1 
ATOM   16295 C  CB  . VAL F 6  126  ? -15.790 -0.011   27.622  1.00 117.11 ?  126  VAL F CB  1 
ATOM   16296 C  CG1 . VAL F 6  126  ? -16.322 -0.206   29.034  1.00 116.62 ?  126  VAL F CG1 1 
ATOM   16297 C  CG2 . VAL F 6  126  ? -14.875 1.202    27.551  1.00 122.44 ?  126  VAL F CG2 1 
ATOM   16298 N  N   . THR F 6  127  ? -13.803 -1.086   25.040  1.00 113.83 ?  127  THR F N   1 
ATOM   16299 C  CA  . THR F 6  127  ? -13.719 -1.031   23.584  1.00 112.62 ?  127  THR F CA  1 
ATOM   16300 C  C   . THR F 6  127  ? -13.334 -2.392   23.027  1.00 109.34 ?  127  THR F C   1 
ATOM   16301 O  O   . THR F 6  127  ? -12.346 -2.984   23.488  1.00 109.64 ?  127  THR F O   1 
ATOM   16302 C  CB  . THR F 6  127  ? -12.699 0.015    23.141  1.00 115.32 ?  127  THR F CB  1 
ATOM   16303 O  OG1 . THR F 6  127  ? -11.392 -0.365   23.591  1.00 120.24 ?  127  THR F OG1 1 
ATOM   16304 C  CG2 . THR F 6  127  ? -13.051 1.381    23.715  1.00 113.99 ?  127  THR F CG2 1 
ATOM   16305 N  N   . PRO F 6  128  ? -14.080 -2.921   22.057  1.00 105.87 ?  128  PRO F N   1 
ATOM   16306 C  CA  . PRO F 6  128  ? -13.696 -4.201   21.450  1.00 100.51 ?  128  PRO F CA  1 
ATOM   16307 C  C   . PRO F 6  128  ? -12.361 -4.082   20.731  1.00 101.80 ?  128  PRO F C   1 
ATOM   16308 O  O   . PRO F 6  128  ? -12.068 -3.073   20.088  1.00 108.25 ?  128  PRO F O   1 
ATOM   16309 C  CB  . PRO F 6  128  ? -14.840 -4.494   20.470  1.00 95.83  ?  128  PRO F CB  1 
ATOM   16310 C  CG  . PRO F 6  128  ? -15.513 -3.179   20.247  1.00 101.65 ?  128  PRO F CG  1 
ATOM   16311 C  CD  . PRO F 6  128  ? -15.341 -2.397   21.509  1.00 112.15 ?  128  PRO F CD  1 
ATOM   16312 N  N   . GLY F 6  129  ? -11.550 -5.130   20.844  1.00 95.80  ?  129  GLY F N   1 
ATOM   16313 C  CA  . GLY F 6  129  ? -10.197 -5.093   20.336  1.00 98.31  ?  129  GLY F CA  1 
ATOM   16314 C  C   . GLY F 6  129  ? -9.181  -4.502   21.287  1.00 99.94  ?  129  GLY F C   1 
ATOM   16315 O  O   . GLY F 6  129  ? -8.003  -4.400   20.922  1.00 102.29 ?  129  GLY F O   1 
ATOM   16316 N  N   . GLY F 6  130  ? -9.596  -4.103   22.491  1.00 101.02 ?  130  GLY F N   1 
ATOM   16317 C  CA  . GLY F 6  130  ? -8.668  -3.586   23.471  1.00 106.88 ?  130  GLY F CA  1 
ATOM   16318 C  C   . GLY F 6  130  ? -7.865  -4.682   24.146  1.00 110.61 ?  130  GLY F C   1 
ATOM   16319 O  O   . GLY F 6  130  ? -8.157  -5.873   24.034  1.00 111.76 ?  130  GLY F O   1 
ATOM   16320 N  N   . ALA F 6  131  ? -6.826  -4.257   24.868  1.00 114.56 ?  131  ALA F N   1 
ATOM   16321 C  CA  . ALA F 6  131  ? -5.943  -5.216   25.522  1.00 118.93 ?  131  ALA F CA  1 
ATOM   16322 C  C   . ALA F 6  131  ? -6.629  -5.919   26.687  1.00 123.75 ?  131  ALA F C   1 
ATOM   16323 O  O   . ALA F 6  131  ? -6.326  -7.084   26.970  1.00 128.45 ?  131  ALA F O   1 
ATOM   16324 C  CB  . ALA F 6  131  ? -4.670  -4.517   26.000  1.00 116.44 ?  131  ALA F CB  1 
ATOM   16325 N  N   . GLU F 6  132  ? -7.548  -5.240   27.367  1.00 140.85 ?  132  GLU F N   1 
ATOM   16326 C  CA  . GLU F 6  132  ? -8.238  -5.775   28.534  1.00 132.70 ?  132  GLU F CA  1 
ATOM   16327 C  C   . GLU F 6  132  ? -9.741  -5.849   28.291  1.00 126.14 ?  132  GLU F C   1 
ATOM   16328 O  O   . GLU F 6  132  ? -10.548 -5.541   29.170  1.00 122.12 ?  132  GLU F O   1 
ATOM   16329 C  CB  . GLU F 6  132  ? -7.937  -4.934   29.772  1.00 131.68 ?  132  GLU F CB  1 
ATOM   16330 C  CG  . GLU F 6  132  ? -6.460  -4.641   29.976  1.00 138.72 ?  132  GLU F CG  1 
ATOM   16331 C  CD  . GLU F 6  132  ? -6.219  -3.559   31.010  1.00 144.99 ?  132  GLU F CD  1 
ATOM   16332 O  OE1 . GLU F 6  132  ? -7.207  -3.041   31.572  1.00 141.41 ?  132  GLU F OE1 1 
ATOM   16333 O  OE2 . GLU F 6  132  ? -5.042  -3.223   31.259  1.00 147.27 -1 132  GLU F OE2 1 
ATOM   16334 N  N   . PHE F 6  133  ? -10.131 -6.264   27.088  1.00 111.16 ?  133  PHE F N   1 
ATOM   16335 C  CA  . PHE F 6  133  ? -11.539 -6.288   26.710  1.00 104.86 ?  133  PHE F CA  1 
ATOM   16336 C  C   . PHE F 6  133  ? -12.301 -7.308   27.549  1.00 96.66  ?  133  PHE F C   1 
ATOM   16337 O  O   . PHE F 6  133  ? -11.936 -8.487   27.594  1.00 98.56  ?  133  PHE F O   1 
ATOM   16338 C  CB  . PHE F 6  133  ? -11.680 -6.612   25.226  1.00 102.23 ?  133  PHE F CB  1 
ATOM   16339 C  CG  . PHE F 6  133  ? -13.105 -6.706   24.760  1.00 100.32 ?  133  PHE F CG  1 
ATOM   16340 C  CD1 . PHE F 6  133  ? -13.945 -5.607   24.826  1.00 103.30 ?  133  PHE F CD1 1 
ATOM   16341 C  CD2 . PHE F 6  133  ? -13.609 -7.898   24.265  1.00 102.85 ?  133  PHE F CD2 1 
ATOM   16342 C  CE1 . PHE F 6  133  ? -15.255 -5.692   24.398  1.00 99.69  ?  133  PHE F CE1 1 
ATOM   16343 C  CE2 . PHE F 6  133  ? -14.921 -7.988   23.837  1.00 104.20 ?  133  PHE F CE2 1 
ATOM   16344 C  CZ  . PHE F 6  133  ? -15.745 -6.883   23.905  1.00 93.51  ?  133  PHE F CZ  1 
ATOM   16345 N  N   . ASP F 6  134  ? -13.359 -6.853   28.207  1.00 103.20 ?  134  ASP F N   1 
ATOM   16346 C  CA  . ASP F 6  134  ? -14.255 -7.730   28.958  1.00 93.71  ?  134  ASP F CA  1 
ATOM   16347 C  C   . ASP F 6  134  ? -15.656 -7.588   28.382  1.00 96.11  ?  134  ASP F C   1 
ATOM   16348 O  O   . ASP F 6  134  ? -16.263 -6.507   28.505  1.00 100.04 ?  134  ASP F O   1 
ATOM   16349 C  CB  . ASP F 6  134  ? -14.241 -7.383   30.446  1.00 87.99  ?  134  ASP F CB  1 
ATOM   16350 C  CG  . ASP F 6  134  ? -14.947 -8.423   31.296  1.00 93.84  ?  134  ASP F CG  1 
ATOM   16351 O  OD1 . ASP F 6  134  ? -16.184 -8.556   31.179  1.00 93.60  ?  134  ASP F OD1 1 
ATOM   16352 O  OD2 . ASP F 6  134  ? -14.262 -9.110   32.083  1.00 94.97  -1 134  ASP F OD2 1 
ATOM   16353 N  N   . PRO F 6  135  ? -16.205 -8.625   27.743  1.00 93.18  ?  135  PRO F N   1 
ATOM   16354 C  CA  . PRO F 6  135  ? -17.510 -8.467   27.077  1.00 89.28  ?  135  PRO F CA  1 
ATOM   16355 C  C   . PRO F 6  135  ? -18.652 -8.141   28.023  1.00 89.49  ?  135  PRO F C   1 
ATOM   16356 O  O   . PRO F 6  135  ? -19.606 -7.467   27.614  1.00 93.06  ?  135  PRO F O   1 
ATOM   16357 C  CB  . PRO F 6  135  ? -17.718 -9.828   26.396  1.00 90.20  ?  135  PRO F CB  1 
ATOM   16358 C  CG  . PRO F 6  135  ? -16.340 -10.390  26.243  1.00 92.05  ?  135  PRO F CG  1 
ATOM   16359 C  CD  . PRO F 6  135  ? -15.601 -9.938   27.466  1.00 95.19  ?  135  PRO F CD  1 
ATOM   16360 N  N   . ILE F 6  136  ? -18.590 -8.598   29.275  1.00 77.98  ?  136  ILE F N   1 
ATOM   16361 C  CA  . ILE F 6  136  ? -19.668 -8.315   30.217  1.00 75.14  ?  136  ILE F CA  1 
ATOM   16362 C  C   . ILE F 6  136  ? -19.664 -6.842   30.607  1.00 76.29  ?  136  ILE F C   1 
ATOM   16363 O  O   . ILE F 6  136  ? -20.721 -6.206   30.693  1.00 79.03  ?  136  ILE F O   1 
ATOM   16364 C  CB  . ILE F 6  136  ? -19.557 -9.231   31.448  1.00 70.75  ?  136  ILE F CB  1 
ATOM   16365 C  CG1 . ILE F 6  136  ? -19.252 -10.667  31.015  1.00 70.18  ?  136  ILE F CG1 1 
ATOM   16366 C  CG2 . ILE F 6  136  ? -20.837 -9.174   32.270  1.00 70.15  ?  136  ILE F CG2 1 
ATOM   16367 C  CD1 . ILE F 6  136  ? -18.957 -11.610  32.162  1.00 54.52  ?  136  ILE F CD1 1 
ATOM   16368 N  N   . ILE F 6  137  ? -18.479 -6.275   30.846  1.00 71.75  ?  137  ILE F N   1 
ATOM   16369 C  CA  . ILE F 6  137  ? -18.391 -4.860   31.191  1.00 71.46  ?  137  ILE F CA  1 
ATOM   16370 C  C   . ILE F 6  137  ? -18.708 -3.993   29.977  1.00 77.28  ?  137  ILE F C   1 
ATOM   16371 O  O   . ILE F 6  137  ? -19.387 -2.965   30.091  1.00 78.58  ?  137  ILE F O   1 
ATOM   16372 C  CB  . ILE F 6  137  ? -17.001 -4.536   31.770  1.00 73.18  ?  137  ILE F CB  1 
ATOM   16373 C  CG1 . ILE F 6  137  ? -16.696 -5.439   32.968  1.00 76.62  ?  137  ILE F CG1 1 
ATOM   16374 C  CG2 . ILE F 6  137  ? -16.915 -3.070   32.169  1.00 75.89  ?  137  ILE F CG2 1 
ATOM   16375 C  CD1 . ILE F 6  137  ? -15.400 -5.099   33.679  1.00 68.57  ?  137  ILE F CD1 1 
ATOM   16376 N  N   . ALA F 6  138  ? -18.231 -4.396   28.797  1.00 93.13  ?  138  ALA F N   1 
ATOM   16377 C  CA  . ALA F 6  138  ? -18.444 -3.601   27.593  1.00 97.84  ?  138  ALA F CA  1 
ATOM   16378 C  C   . ALA F 6  138  ? -19.877 -3.678   27.084  1.00 102.38 ?  138  ALA F C   1 
ATOM   16379 O  O   . ALA F 6  138  ? -20.294 -2.802   26.318  1.00 112.95 ?  138  ALA F O   1 
ATOM   16380 C  CB  . ALA F 6  138  ? -17.480 -4.043   26.493  1.00 100.61 ?  138  ALA F CB  1 
ATOM   16381 N  N   . HIS F 6  139  ? -20.638 -4.700   27.485  1.00 100.24 ?  139  HIS F N   1 
ATOM   16382 C  CA  . HIS F 6  139  ? -22.039 -4.784   27.091  1.00 99.88  ?  139  HIS F CA  1 
ATOM   16383 C  C   . HIS F 6  139  ? -22.848 -3.604   27.615  1.00 101.35 ?  139  HIS F C   1 
ATOM   16384 O  O   . HIS F 6  139  ? -23.907 -3.290   27.059  1.00 104.07 ?  139  HIS F O   1 
ATOM   16385 C  CB  . HIS F 6  139  ? -22.637 -6.108   27.581  1.00 96.05  ?  139  HIS F CB  1 
ATOM   16386 C  CG  . HIS F 6  139  ? -24.134 -6.144   27.571  1.00 97.25  ?  139  HIS F CG  1 
ATOM   16387 N  ND1 . HIS F 6  139  ? -24.866 -6.366   26.424  1.00 102.29 ?  139  HIS F ND1 1 
ATOM   16388 C  CD2 . HIS F 6  139  ? -25.036 -5.987   28.568  1.00 97.25  ?  139  HIS F CD2 1 
ATOM   16389 C  CE1 . HIS F 6  139  ? -26.154 -6.343   26.715  1.00 96.90  ?  139  HIS F CE1 1 
ATOM   16390 N  NE2 . HIS F 6  139  ? -26.285 -6.115   28.009  1.00 92.21  ?  139  HIS F NE2 1 
ATOM   16391 N  N   . LYS F 6  140  ? -22.358 -2.931   28.656  1.00 96.23  ?  140  LYS F N   1 
ATOM   16392 C  CA  . LYS F 6  140  ? -23.034 -1.795   29.267  1.00 93.48  ?  140  LYS F CA  1 
ATOM   16393 C  C   . LYS F 6  140  ? -22.361 -0.473   28.907  1.00 105.35 ?  140  LYS F C   1 
ATOM   16394 O  O   . LYS F 6  140  ? -22.369 0.469    29.702  1.00 103.25 ?  140  LYS F O   1 
ATOM   16395 C  CB  . LYS F 6  140  ? -23.075 -1.970   30.784  1.00 90.67  ?  140  LYS F CB  1 
ATOM   16396 C  CG  . LYS F 6  140  ? -23.735 -3.260   31.242  1.00 95.65  ?  140  LYS F CG  1 
ATOM   16397 C  CD  . LYS F 6  140  ? -23.499 -3.501   32.723  1.00 81.81  ?  140  LYS F CD  1 
ATOM   16398 C  CE  . LYS F 6  140  ? -22.212 -4.270   32.972  1.00 75.78  ?  140  LYS F CE  1 
ATOM   16399 N  NZ  . LYS F 6  140  ? -22.356 -5.718   32.654  1.00 82.22  ?  140  LYS F NZ  1 
ATOM   16400 N  N   . VAL F 6  141  ? -21.781 -0.386   27.714  1.00 151.54 ?  141  VAL F N   1 
ATOM   16401 C  CA  . VAL F 6  141  ? -20.977 0.774    27.332  1.00 144.77 ?  141  VAL F CA  1 
ATOM   16402 C  C   . VAL F 6  141  ? -21.814 2.038    27.112  1.00 145.00 ?  141  VAL F C   1 
ATOM   16403 O  O   . VAL F 6  141  ? -21.302 3.135    27.383  1.00 148.13 ?  141  VAL F O   1 
ATOM   16404 C  CB  . VAL F 6  141  ? -20.094 0.455    26.107  1.00 156.82 ?  141  VAL F CB  1 
ATOM   16405 C  CG1 . VAL F 6  141  ? -20.914 0.184    24.853  1.00 150.24 ?  141  VAL F CG1 1 
ATOM   16406 C  CG2 . VAL F 6  141  ? -19.078 1.568    25.863  1.00 160.29 ?  141  VAL F CG2 1 
ATOM   16407 N  N   . PRO F 6  142  ? -23.096 1.985    26.650  1.00 105.07 ?  142  PRO F N   1 
ATOM   16408 C  CA  . PRO F 6  142  ? -23.841 3.248    26.556  1.00 98.10  ?  142  PRO F CA  1 
ATOM   16409 C  C   . PRO F 6  142  ? -24.423 3.669    27.897  1.00 99.83  ?  142  PRO F C   1 
ATOM   16410 O  O   . PRO F 6  142  ? -24.449 4.858    28.227  1.00 97.37  ?  142  PRO F O   1 
ATOM   16411 C  CB  . PRO F 6  142  ? -24.937 2.933    25.533  1.00 96.26  ?  142  PRO F CB  1 
ATOM   16412 C  CG  . PRO F 6  142  ? -25.220 1.506    25.743  1.00 99.04  ?  142  PRO F CG  1 
ATOM   16413 C  CD  . PRO F 6  142  ? -23.917 0.860    26.151  1.00 102.55 ?  142  PRO F CD  1 
ATOM   16414 N  N   . TRP F 6  143  ? -24.878 2.691    28.683  1.00 115.32 ?  143  TRP F N   1 
ATOM   16415 C  CA  . TRP F 6  143  ? -25.473 2.988    29.982  1.00 108.18 ?  143  TRP F CA  1 
ATOM   16416 C  C   . TRP F 6  143  ? -24.408 3.399    30.992  1.00 109.21 ?  143  TRP F C   1 
ATOM   16417 O  O   . TRP F 6  143  ? -24.518 4.451    31.632  1.00 110.89 ?  143  TRP F O   1 
ATOM   16418 C  CB  . TRP F 6  143  ? -26.258 1.771    30.476  1.00 106.62 ?  143  TRP F CB  1 
ATOM   16419 C  CG  . TRP F 6  143  ? -26.957 1.968    31.786  1.00 104.62 ?  143  TRP F CG  1 
ATOM   16420 C  CD1 . TRP F 6  143  ? -26.659 1.362    32.972  1.00 103.58 ?  143  TRP F CD1 1 
ATOM   16421 C  CD2 . TRP F 6  143  ? -28.082 2.817    32.042  1.00 107.32 ?  143  TRP F CD2 1 
ATOM   16422 N  NE1 . TRP F 6  143  ? -27.524 1.786    33.951  1.00 105.60 ?  143  TRP F NE1 1 
ATOM   16423 C  CE2 . TRP F 6  143  ? -28.408 2.679    33.406  1.00 109.13 ?  143  TRP F CE2 1 
ATOM   16424 C  CE3 . TRP F 6  143  ? -28.843 3.684    31.252  1.00 111.19 ?  143  TRP F CE3 1 
ATOM   16425 C  CZ2 . TRP F 6  143  ? -29.462 3.374    33.996  1.00 106.77 ?  143  TRP F CZ2 1 
ATOM   16426 C  CZ3 . TRP F 6  143  ? -29.888 4.373    31.840  1.00 109.20 ?  143  TRP F CZ3 1 
ATOM   16427 C  CH2 . TRP F 6  143  ? -30.187 4.215    33.199  1.00 103.99 ?  143  TRP F CH2 1 
ATOM   16428 N  N   . LEU F 6  144  ? -23.365 2.581    31.146  1.00 80.40  ?  144  LEU F N   1 
ATOM   16429 C  CA  . LEU F 6  144  ? -22.271 2.881    32.070  1.00 79.25  ?  144  LEU F CA  1 
ATOM   16430 C  C   . LEU F 6  144  ? -21.202 3.674    31.323  1.00 74.24  ?  144  LEU F C   1 
ATOM   16431 O  O   . LEU F 6  144  ? -20.139 3.169    30.955  1.00 73.26  ?  144  LEU F O   1 
ATOM   16432 C  CB  . LEU F 6  144  ? -21.707 1.601    32.674  1.00 76.17  ?  144  LEU F CB  1 
ATOM   16433 C  CG  . LEU F 6  144  ? -22.534 0.943    33.780  1.00 63.04  ?  144  LEU F CG  1 
ATOM   16434 C  CD1 . LEU F 6  144  ? -21.858 -0.327   34.268  1.00 61.26  ?  144  LEU F CD1 1 
ATOM   16435 C  CD2 . LEU F 6  144  ? -22.752 1.910    34.930  1.00 67.08  ?  144  LEU F CD2 1 
ATOM   16436 N  N   . SER F 6  145  ? -21.503 4.949    31.096  1.00 109.95 ?  145  SER F N   1 
ATOM   16437 C  CA  . SER F 6  145  ? -20.581 5.886    30.483  1.00 116.93 ?  145  SER F CA  1 
ATOM   16438 C  C   . SER F 6  145  ? -20.388 7.093    31.393  1.00 113.11 ?  145  SER F C   1 
ATOM   16439 O  O   . SER F 6  145  ? -21.303 7.464    32.136  1.00 108.47 ?  145  SER F O   1 
ATOM   16440 C  CB  . SER F 6  145  ? -21.088 6.355    29.113  1.00 121.73 ?  145  SER F CB  1 
ATOM   16441 O  OG  . SER F 6  145  ? -21.271 5.258    28.234  1.00 121.66 ?  145  SER F OG  1 
ATOM   16442 N  N   . PRO F 6  146  ? -19.207 7.717    31.369  1.00 86.69  ?  146  PRO F N   1 
ATOM   16443 C  CA  . PRO F 6  146  ? -18.990 8.890    32.234  1.00 93.92  ?  146  PRO F CA  1 
ATOM   16444 C  C   . PRO F 6  146  ? -19.983 10.013   31.986  1.00 100.95 ?  146  PRO F C   1 
ATOM   16445 O  O   . PRO F 6  146  ? -20.400 10.686   32.937  1.00 103.30 ?  146  PRO F O   1 
ATOM   16446 C  CB  . PRO F 6  146  ? -17.553 9.310    31.895  1.00 94.14  ?  146  PRO F CB  1 
ATOM   16447 C  CG  . PRO F 6  146  ? -16.910 8.071    31.364  1.00 88.36  ?  146  PRO F CG  1 
ATOM   16448 C  CD  . PRO F 6  146  ? -17.990 7.337    30.631  1.00 84.87  ?  146  PRO F CD  1 
ATOM   16449 N  N   . LEU F 6  147  ? -20.381 10.231   30.731  1.00 118.84 ?  147  LEU F N   1 
ATOM   16450 C  CA  . LEU F 6  147  ? -21.379 11.256   30.442  1.00 121.47 ?  147  LEU F CA  1 
ATOM   16451 C  C   . LEU F 6  147  ? -22.755 10.849   30.955  1.00 119.80 ?  147  LEU F C   1 
ATOM   16452 O  O   . LEU F 6  147  ? -23.472 11.667   31.542  1.00 123.76 ?  147  LEU F O   1 
ATOM   16453 C  CB  . LEU F 6  147  ? -21.426 11.532   28.939  1.00 129.04 ?  147  LEU F CB  1 
ATOM   16454 C  CG  . LEU F 6  147  ? -22.145 12.812   28.508  1.00 131.99 ?  147  LEU F CG  1 
ATOM   16455 C  CD1 . LEU F 6  147  ? -21.376 14.045   28.959  1.00 130.45 ?  147  LEU F CD1 1 
ATOM   16456 C  CD2 . LEU F 6  147  ? -22.357 12.827   27.002  1.00 128.94 ?  147  LEU F CD2 1 
ATOM   16457 N  N   . TRP F 6  148  ? -23.139 9.587    30.746  1.00 109.77 ?  148  TRP F N   1 
ATOM   16458 C  CA  . TRP F 6  148  ? -24.451 9.133    31.194  1.00 111.78 ?  148  TRP F CA  1 
ATOM   16459 C  C   . TRP F 6  148  ? -24.531 9.073    32.714  1.00 117.44 ?  148  TRP F C   1 
ATOM   16460 O  O   . TRP F 6  148  ? -25.556 9.440    33.301  1.00 116.35 ?  148  TRP F O   1 
ATOM   16461 C  CB  . TRP F 6  148  ? -24.769 7.766    30.590  1.00 110.44 ?  148  TRP F CB  1 
ATOM   16462 C  CG  . TRP F 6  148  ? -25.104 7.802    29.130  1.00 111.11 ?  148  TRP F CG  1 
ATOM   16463 C  CD1 . TRP F 6  148  ? -24.377 8.386    28.134  1.00 111.91 ?  148  TRP F CD1 1 
ATOM   16464 C  CD2 . TRP F 6  148  ? -26.256 7.228    28.502  1.00 114.11 ?  148  TRP F CD2 1 
ATOM   16465 N  NE1 . TRP F 6  148  ? -25.004 8.208    26.924  1.00 109.44 ?  148  TRP F NE1 1 
ATOM   16466 C  CE2 . TRP F 6  148  ? -26.159 7.500    27.123  1.00 113.70 ?  148  TRP F CE2 1 
ATOM   16467 C  CE3 . TRP F 6  148  ? -27.357 6.506    28.972  1.00 111.51 ?  148  TRP F CE3 1 
ATOM   16468 C  CZ2 . TRP F 6  148  ? -27.124 7.079    26.211  1.00 112.99 ?  148  TRP F CZ2 1 
ATOM   16469 C  CZ3 . TRP F 6  148  ? -28.313 6.089    28.065  1.00 111.69 ?  148  TRP F CZ3 1 
ATOM   16470 C  CH2 . TRP F 6  148  ? -28.190 6.376    26.700  1.00 119.94 ?  148  TRP F CH2 1 
ATOM   16471 N  N   . VAL F 6  149  ? -23.464 8.609    33.369  1.00 90.58  ?  149  VAL F N   1 
ATOM   16472 C  CA  . VAL F 6  149  ? -23.466 8.525    34.826  1.00 90.45  ?  149  VAL F CA  1 
ATOM   16473 C  C   . VAL F 6  149  ? -23.532 9.916    35.443  1.00 94.42  ?  149  VAL F C   1 
ATOM   16474 O  O   . VAL F 6  149  ? -24.293 10.155   36.389  1.00 100.63 ?  149  VAL F O   1 
ATOM   16475 C  CB  . VAL F 6  149  ? -22.235 7.741    35.318  1.00 92.73  ?  149  VAL F CB  1 
ATOM   16476 C  CG1 . VAL F 6  149  ? -22.076 7.886    36.823  1.00 98.07  ?  149  VAL F CG1 1 
ATOM   16477 C  CG2 . VAL F 6  149  ? -22.358 6.274    34.939  1.00 91.00  ?  149  VAL F CG2 1 
ATOM   16478 N  N   . THR F 6  150  ? -22.751 10.860   34.912  1.00 98.22  ?  150  THR F N   1 
ATOM   16479 C  CA  . THR F 6  150  ? -22.778 12.221   35.439  1.00 103.13 ?  150  THR F CA  1 
ATOM   16480 C  C   . THR F 6  150  ? -24.133 12.878   35.206  1.00 99.22  ?  150  THR F C   1 
ATOM   16481 O  O   . THR F 6  150  ? -24.612 13.643   36.052  1.00 99.06  ?  150  THR F O   1 
ATOM   16482 C  CB  . THR F 6  150  ? -21.662 13.051   34.806  1.00 109.39 ?  150  THR F CB  1 
ATOM   16483 O  OG1 . THR F 6  150  ? -20.417 12.353   34.933  1.00 107.74 ?  150  THR F OG1 1 
ATOM   16484 C  CG2 . THR F 6  150  ? -21.546 14.404   35.492  1.00 109.14 ?  150  THR F CG2 1 
ATOM   16485 N  N   . ALA F 6  151  ? -24.769 12.589   34.069  1.00 74.61  ?  151  ALA F N   1 
ATOM   16486 C  CA  . ALA F 6  151  ? -26.089 13.150   33.800  1.00 71.38  ?  151  ALA F CA  1 
ATOM   16487 C  C   . ALA F 6  151  ? -27.132 12.587   34.756  1.00 75.81  ?  151  ALA F C   1 
ATOM   16488 O  O   . ALA F 6  151  ? -27.982 13.329   35.262  1.00 77.80  ?  151  ALA F O   1 
ATOM   16489 C  CB  . ALA F 6  151  ? -26.490 12.884   32.350  1.00 73.65  ?  151  ALA F CB  1 
ATOM   16490 N  N   . ARG F 6  152  ? -27.085 11.278   35.013  1.00 110.34 ?  152  ARG F N   1 
ATOM   16491 C  CA  . ARG F 6  152  ? -28.016 10.675   35.961  1.00 113.45 ?  152  ARG F CA  1 
ATOM   16492 C  C   . ARG F 6  152  ? -27.797 11.216   37.368  1.00 114.84 ?  152  ARG F C   1 
ATOM   16493 O  O   . ARG F 6  152  ? -28.760 11.485   38.095  1.00 111.26 ?  152  ARG F O   1 
ATOM   16494 C  CB  . ARG F 6  152  ? -27.867 9.154    35.947  1.00 114.30 ?  152  ARG F CB  1 
ATOM   16495 C  CG  . ARG F 6  152  ? -28.805 8.438    34.994  1.00 114.36 ?  152  ARG F CG  1 
ATOM   16496 C  CD  . ARG F 6  152  ? -28.558 6.940    35.025  1.00 113.00 ?  152  ARG F CD  1 
ATOM   16497 N  NE  . ARG F 6  152  ? -27.297 6.591    34.382  1.00 116.79 ?  152  ARG F NE  1 
ATOM   16498 C  CZ  . ARG F 6  152  ? -26.600 5.494    34.643  1.00 113.97 ?  152  ARG F CZ  1 
ATOM   16499 N  NH1 . ARG F 6  152  ? -27.011 4.610    35.537  1.00 118.34 ?  152  ARG F NH1 1 
ATOM   16500 N  NH2 . ARG F 6  152  ? -25.461 5.278    33.991  1.00 110.36 ?  152  ARG F NH2 1 
ATOM   16501 N  N   . ILE F 6  153  ? -26.535 11.381   37.767  1.00 104.29 ?  153  ILE F N   1 
ATOM   16502 C  CA  . ILE F 6  153  ? -26.236 11.897   39.099  1.00 106.56 ?  153  ILE F CA  1 
ATOM   16503 C  C   . ILE F 6  153  ? -26.706 13.341   39.231  1.00 111.16 ?  153  ILE F C   1 
ATOM   16504 O  O   . ILE F 6  153  ? -27.277 13.731   40.257  1.00 110.29 ?  153  ILE F O   1 
ATOM   16505 C  CB  . ILE F 6  153  ? -24.731 11.756   39.395  1.00 108.27 ?  153  ILE F CB  1 
ATOM   16506 C  CG1 . ILE F 6  153  ? -24.358 10.284   39.578  1.00 102.47 ?  153  ILE F CG1 1 
ATOM   16507 C  CG2 . ILE F 6  153  ? -24.348 12.553   40.627  1.00 108.54 ?  153  ILE F CG2 1 
ATOM   16508 C  CD1 . ILE F 6  153  ? -25.082 9.606    40.716  1.00 102.74 ?  153  ILE F CD1 1 
ATOM   16509 N  N   . ALA F 6  154  ? -26.488 14.154   38.194  1.00 108.39 ?  154  ALA F N   1 
ATOM   16510 C  CA  . ALA F 6  154  ? -26.917 15.548   38.244  1.00 106.60 ?  154  ALA F CA  1 
ATOM   16511 C  C   . ALA F 6  154  ? -28.437 15.660   38.269  1.00 100.62 ?  154  ALA F C   1 
ATOM   16512 O  O   . ALA F 6  154  ? -28.989 16.518   38.969  1.00 100.21 ?  154  ALA F O   1 
ATOM   16513 C  CB  . ALA F 6  154  ? -26.341 16.318   37.057  1.00 101.89 ?  154  ALA F CB  1 
ATOM   16514 N  N   . ILE F 6  155  ? -29.129 14.807   37.511  1.00 85.73  ?  155  ILE F N   1 
ATOM   16515 C  CA  . ILE F 6  155  ? -30.589 14.834   37.510  1.00 85.11  ?  155  ILE F CA  1 
ATOM   16516 C  C   . ILE F 6  155  ? -31.131 14.433   38.876  1.00 79.39  ?  155  ILE F C   1 
ATOM   16517 O  O   . ILE F 6  155  ? -32.098 15.023   39.374  1.00 85.22  ?  155  ILE F O   1 
ATOM   16518 C  CB  . ILE F 6  155  ? -31.139 13.932   36.390  1.00 89.29  ?  155  ILE F CB  1 
ATOM   16519 C  CG1 . ILE F 6  155  ? -30.897 14.574   35.023  1.00 86.79  ?  155  ILE F CG1 1 
ATOM   16520 C  CG2 . ILE F 6  155  ? -32.621 13.654   36.595  1.00 87.68  ?  155  ILE F CG2 1 
ATOM   16521 C  CD1 . ILE F 6  155  ? -31.251 13.679   33.856  1.00 86.35  ?  155  ILE F CD1 1 
ATOM   16522 N  N   . PHE F 6  156  ? -30.516 13.431   39.509  1.00 97.64  ?  156  PHE F N   1 
ATOM   16523 C  CA  . PHE F 6  156  ? -30.945 13.032   40.845  1.00 106.52 ?  156  PHE F CA  1 
ATOM   16524 C  C   . PHE F 6  156  ? -30.714 14.152   41.853  1.00 100.27 ?  156  PHE F C   1 
ATOM   16525 O  O   . PHE F 6  156  ? -31.532 14.365   42.756  1.00 92.51  ?  156  PHE F O   1 
ATOM   16526 C  CB  . PHE F 6  156  ? -30.214 11.759   41.277  1.00 102.29 ?  156  PHE F CB  1 
ATOM   16527 C  CG  . PHE F 6  156  ? -30.530 10.554   40.431  1.00 104.04 ?  156  PHE F CG  1 
ATOM   16528 C  CD1 . PHE F 6  156  ? -31.676 10.514   39.652  1.00 103.09 ?  156  PHE F CD1 1 
ATOM   16529 C  CD2 . PHE F 6  156  ? -29.681 9.460    40.419  1.00 103.17 ?  156  PHE F CD2 1 
ATOM   16530 C  CE1 . PHE F 6  156  ? -31.967 9.407    38.876  1.00 99.54  ?  156  PHE F CE1 1 
ATOM   16531 C  CE2 . PHE F 6  156  ? -29.966 8.349    39.645  1.00 96.13  ?  156  PHE F CE2 1 
ATOM   16532 C  CZ  . PHE F 6  156  ? -31.110 8.323    38.873  1.00 99.38  ?  156  PHE F CZ  1 
ATOM   16533 N  N   . PHE F 6  157  ? -29.608 14.886   41.708  1.00 108.37 ?  157  PHE F N   1 
ATOM   16534 C  CA  . PHE F 6  157  ? -29.310 15.971   42.638  1.00 109.66 ?  157  PHE F CA  1 
ATOM   16535 C  C   . PHE F 6  157  ? -30.260 17.146   42.446  1.00 105.42 ?  157  PHE F C   1 
ATOM   16536 O  O   . PHE F 6  157  ? -30.641 17.809   43.418  1.00 100.81 ?  157  PHE F O   1 
ATOM   16537 C  CB  . PHE F 6  157  ? -27.859 16.417   42.471  1.00 113.01 ?  157  PHE F CB  1 
ATOM   16538 C  CG  . PHE F 6  157  ? -26.898 15.674   43.348  1.00 120.10 ?  157  PHE F CG  1 
ATOM   16539 C  CD1 . PHE F 6  157  ? -27.053 15.683   44.723  1.00 112.60 ?  157  PHE F CD1 1 
ATOM   16540 C  CD2 . PHE F 6  157  ? -25.850 14.953   42.801  1.00 129.28 ?  157  PHE F CD2 1 
ATOM   16541 C  CE1 . PHE F 6  157  ? -26.177 14.999   45.534  1.00 117.77 ?  157  PHE F CE1 1 
ATOM   16542 C  CE2 . PHE F 6  157  ? -24.970 14.263   43.611  1.00 123.85 ?  157  PHE F CE2 1 
ATOM   16543 C  CZ  . PHE F 6  157  ? -25.136 14.285   44.978  1.00 120.97 ?  157  PHE F CZ  1 
ATOM   16544 N  N   . ILE F 6  158  ? -30.646 17.427   41.199  1.00 91.65  ?  158  ILE F N   1 
ATOM   16545 C  CA  . ILE F 6  158  ? -31.623 18.482   40.945  1.00 88.90  ?  158  ILE F CA  1 
ATOM   16546 C  C   . ILE F 6  158  ? -32.963 18.119   41.571  1.00 88.49  ?  158  ILE F C   1 
ATOM   16547 O  O   . ILE F 6  158  ? -33.644 18.969   42.158  1.00 94.73  ?  158  ILE F O   1 
ATOM   16548 C  CB  . ILE F 6  158  ? -31.751 18.737   39.431  1.00 86.00  ?  158  ILE F CB  1 
ATOM   16549 C  CG1 . ILE F 6  158  ? -30.505 19.451   38.902  1.00 91.13  ?  158  ILE F CG1 1 
ATOM   16550 C  CG2 . ILE F 6  158  ? -32.998 19.552   39.124  1.00 82.59  ?  158  ILE F CG2 1 
ATOM   16551 C  CD1 . ILE F 6  158  ? -30.230 20.777   39.575  1.00 100.28 ?  158  ILE F CD1 1 
ATOM   16552 N  N   . ILE F 6  159  ? -33.352 16.847   41.471  1.00 86.39  ?  159  ILE F N   1 
ATOM   16553 C  CA  . ILE F 6  159  ? -34.612 16.399   42.057  1.00 82.68  ?  159  ILE F CA  1 
ATOM   16554 C  C   . ILE F 6  159  ? -34.556 16.498   43.576  1.00 92.30  ?  159  ILE F C   1 
ATOM   16555 O  O   . ILE F 6  159  ? -35.490 16.993   44.218  1.00 93.98  ?  159  ILE F O   1 
ATOM   16556 C  CB  . ILE F 6  159  ? -34.935 14.966   41.595  1.00 83.61  ?  159  ILE F CB  1 
ATOM   16557 C  CG1 . ILE F 6  159  ? -35.314 14.956   40.114  1.00 90.17  ?  159  ILE F CG1 1 
ATOM   16558 C  CG2 . ILE F 6  159  ? -36.055 14.372   42.431  1.00 72.03  ?  159  ILE F CG2 1 
ATOM   16559 C  CD1 . ILE F 6  159  ? -35.662 13.585   39.584  1.00 87.58  ?  159  ILE F CD1 1 
ATOM   16560 N  N   . TRP F 6  160  ? -33.453 16.037   44.172  1.00 104.00 ?  160  TRP F N   1 
ATOM   16561 C  CA  . TRP F 6  160  ? -33.339 16.030   45.628  1.00 102.31 ?  160  TRP F CA  1 
ATOM   16562 C  C   . TRP F 6  160  ? -33.292 17.447   46.186  1.00 97.51  ?  160  TRP F C   1 
ATOM   16563 O  O   . TRP F 6  160  ? -33.965 17.757   47.176  1.00 102.87 ?  160  TRP F O   1 
ATOM   16564 C  CB  . TRP F 6  160  ? -32.099 15.243   46.057  1.00 104.33 ?  160  TRP F CB  1 
ATOM   16565 C  CG  . TRP F 6  160  ? -32.153 13.786   45.703  1.00 101.13 ?  160  TRP F CG  1 
ATOM   16566 C  CD1 . TRP F 6  160  ? -33.272 13.030   45.511  1.00 95.30  ?  160  TRP F CD1 1 
ATOM   16567 C  CD2 . TRP F 6  160  ? -31.036 12.912   45.494  1.00 98.15  ?  160  TRP F CD2 1 
ATOM   16568 N  NE1 . TRP F 6  160  ? -32.922 11.738   45.197  1.00 95.04  ?  160  TRP F NE1 1 
ATOM   16569 C  CE2 . TRP F 6  160  ? -31.556 11.640   45.180  1.00 94.11  ?  160  TRP F CE2 1 
ATOM   16570 C  CE3 . TRP F 6  160  ? -29.649 13.081   45.543  1.00 97.44  ?  160  TRP F CE3 1 
ATOM   16571 C  CZ2 . TRP F 6  160  ? -30.737 10.544   44.916  1.00 93.05  ?  160  TRP F CZ2 1 
ATOM   16572 C  CZ3 . TRP F 6  160  ? -28.838 11.991   45.280  1.00 91.25  ?  160  TRP F CZ3 1 
ATOM   16573 C  CH2 . TRP F 6  160  ? -29.384 10.739   44.971  1.00 90.89  ?  160  TRP F CH2 1 
ATOM   16574 N  N   . SER F 6  161  ? -32.496 18.321   45.566  1.00 95.34  ?  161  SER F N   1 
ATOM   16575 C  CA  . SER F 6  161  ? -32.390 19.693   46.053  1.00 94.91  ?  161  SER F CA  1 
ATOM   16576 C  C   . SER F 6  161  ? -33.705 20.445   45.884  1.00 96.43  ?  161  SER F C   1 
ATOM   16577 O  O   . SER F 6  161  ? -34.102 21.215   46.765  1.00 102.85 ?  161  SER F O   1 
ATOM   16578 C  CB  . SER F 6  161  ? -31.256 20.420   45.331  1.00 94.80  ?  161  SER F CB  1 
ATOM   16579 O  OG  . SER F 6  161  ? -30.011 19.788   45.572  1.00 94.27  ?  161  SER F OG  1 
ATOM   16580 N  N   . ALA F 6  162  ? -34.394 20.233   44.760  1.00 78.99  ?  162  ALA F N   1 
ATOM   16581 C  CA  . ALA F 6  162  ? -35.675 20.898   44.545  1.00 80.11  ?  162  ALA F CA  1 
ATOM   16582 C  C   . ALA F 6  162  ? -36.707 20.457   45.576  1.00 79.73  ?  162  ALA F C   1 
ATOM   16583 O  O   . ALA F 6  162  ? -37.459 21.282   46.105  1.00 85.60  ?  162  ALA F O   1 
ATOM   16584 C  CB  . ALA F 6  162  ? -36.179 20.625   43.128  1.00 72.06  ?  162  ALA F CB  1 
ATOM   16585 N  N   . LEU F 6  163  ? -36.752 19.158   45.879  1.00 95.69  ?  163  LEU F N   1 
ATOM   16586 C  CA  . LEU F 6  163  ? -37.715 18.654   46.854  1.00 98.11  ?  163  LEU F CA  1 
ATOM   16587 C  C   . LEU F 6  163  ? -37.410 19.174   48.253  1.00 98.49  ?  163  LEU F C   1 
ATOM   16588 O  O   . LEU F 6  163  ? -38.315 19.605   48.978  1.00 98.59  ?  163  LEU F O   1 
ATOM   16589 C  CB  . LEU F 6  163  ? -37.723 17.125   46.844  1.00 100.50 ?  163  LEU F CB  1 
ATOM   16590 C  CG  . LEU F 6  163  ? -38.506 16.421   45.735  1.00 89.89  ?  163  LEU F CG  1 
ATOM   16591 C  CD1 . LEU F 6  163  ? -38.178 14.938   45.719  1.00 102.63 ?  163  LEU F CD1 1 
ATOM   16592 C  CD2 . LEU F 6  163  ? -40.001 16.639   45.915  1.00 95.32  ?  163  LEU F CD2 1 
ATOM   16593 N  N   . ALA F 6  164  ? -36.137 19.138   48.653  1.00 94.01  ?  164  ALA F N   1 
ATOM   16594 C  CA  . ALA F 6  164  ? -35.775 19.531   50.011  1.00 99.01  ?  164  ALA F CA  1 
ATOM   16595 C  C   . ALA F 6  164  ? -35.966 21.027   50.224  1.00 101.22 ?  164  ALA F C   1 
ATOM   16596 O  O   . ALA F 6  164  ? -36.515 21.454   51.247  1.00 100.57 ?  164  ALA F O   1 
ATOM   16597 C  CB  . ALA F 6  164  ? -34.332 19.124   50.308  1.00 103.30 ?  164  ALA F CB  1 
ATOM   16598 N  N   . LEU F 6  165  ? -35.518 21.842   49.265  1.00 99.85  ?  165  LEU F N   1 
ATOM   16599 C  CA  . LEU F 6  165  ? -35.613 23.289   49.424  1.00 86.84  ?  165  LEU F CA  1 
ATOM   16600 C  C   . LEU F 6  165  ? -37.060 23.763   49.361  1.00 94.09  ?  165  LEU F C   1 
ATOM   16601 O  O   . LEU F 6  165  ? -37.441 24.702   50.071  1.00 105.01 ?  165  LEU F O   1 
ATOM   16602 C  CB  . LEU F 6  165  ? -34.769 23.988   48.360  1.00 78.61  ?  165  LEU F CB  1 
ATOM   16603 C  CG  . LEU F 6  165  ? -33.256 23.794   48.492  1.00 76.62  ?  165  LEU F CG  1 
ATOM   16604 C  CD1 . LEU F 6  165  ? -32.515 24.577   47.420  1.00 87.07  ?  165  LEU F CD1 1 
ATOM   16605 C  CD2 . LEU F 6  165  ? -32.781 24.192   49.881  1.00 87.22  ?  165  LEU F CD2 1 
ATOM   16606 N  N   . THR F 6  166  ? -37.882 23.129   48.521  1.00 80.20  ?  166  THR F N   1 
ATOM   16607 C  CA  . THR F 6  166  ? -39.288 23.511   48.440  1.00 85.87  ?  166  THR F CA  1 
ATOM   16608 C  C   . THR F 6  166  ? -40.032 23.149   49.719  1.00 89.73  ?  166  THR F C   1 
ATOM   16609 O  O   . THR F 6  166  ? -40.843 23.940   50.217  1.00 98.20  ?  166  THR F O   1 
ATOM   16610 C  CB  . THR F 6  166  ? -39.949 22.848   47.230  1.00 82.90  ?  166  THR F CB  1 
ATOM   16611 O  OG1 . THR F 6  166  ? -39.313 23.302   46.028  1.00 74.57  ?  166  THR F OG1 1 
ATOM   16612 C  CG2 . THR F 6  166  ? -41.431 23.189   47.172  1.00 95.23  ?  166  THR F CG2 1 
ATOM   16613 N  N   . LEU F 6  167  ? -39.769 21.961   50.268  1.00 105.07 ?  167  LEU F N   1 
ATOM   16614 C  CA  . LEU F 6  167  ? -40.414 21.568   51.516  1.00 117.07 ?  167  LEU F CA  1 
ATOM   16615 C  C   . LEU F 6  167  ? -39.977 22.461   52.670  1.00 120.09 ?  167  LEU F C   1 
ATOM   16616 O  O   . LEU F 6  167  ? -40.799 22.847   53.508  1.00 120.77 ?  167  LEU F O   1 
ATOM   16617 C  CB  . LEU F 6  167  ? -40.113 20.103   51.827  1.00 114.93 ?  167  LEU F CB  1 
ATOM   16618 C  CG  . LEU F 6  167  ? -40.937 19.066   51.063  1.00 116.21 ?  167  LEU F CG  1 
ATOM   16619 C  CD1 . LEU F 6  167  ? -40.588 17.663   51.530  1.00 118.29 ?  167  LEU F CD1 1 
ATOM   16620 C  CD2 . LEU F 6  167  ? -42.424 19.337   51.228  1.00 112.74 ?  167  LEU F CD2 1 
ATOM   16621 N  N   . ARG F 6  168  ? -38.688 22.802   52.731  1.00 110.39 ?  168  ARG F N   1 
ATOM   16622 C  CA  . ARG F 6  168  ? -38.217 23.682   53.795  1.00 100.84 ?  168  ARG F CA  1 
ATOM   16623 C  C   . ARG F 6  168  ? -38.799 25.082   53.646  1.00 110.80 ?  168  ARG F C   1 
ATOM   16624 O  O   . ARG F 6  168  ? -39.180 25.708   54.641  1.00 123.23 ?  168  ARG F O   1 
ATOM   16625 C  CB  . ARG F 6  168  ? -36.690 23.730   53.808  1.00 89.68  ?  168  ARG F CB  1 
ATOM   16626 C  CG  . ARG F 6  168  ? -36.107 24.249   55.114  1.00 91.82  ?  168  ARG F CG  1 
ATOM   16627 C  CD  . ARG F 6  168  ? -34.591 24.341   55.062  1.00 92.44  ?  168  ARG F CD  1 
ATOM   16628 N  NE  . ARG F 6  168  ? -34.130 25.344   54.109  1.00 107.05 ?  168  ARG F NE  1 
ATOM   16629 C  CZ  . ARG F 6  168  ? -32.933 25.913   54.144  1.00 114.98 ?  168  ARG F CZ  1 
ATOM   16630 N  NH1 . ARG F 6  168  ? -32.047 25.604   55.077  1.00 111.40 ?  168  ARG F NH1 1 
ATOM   16631 N  NH2 . ARG F 6  168  ? -32.616 26.815   53.219  1.00 109.93 ?  168  ARG F NH2 1 
ATOM   16632 N  N   . ALA F 6  169  ? -38.884 25.583   52.411  1.00 97.84  ?  169  ALA F N   1 
ATOM   16633 C  CA  . ALA F 6  169  ? -39.460 26.906   52.187  1.00 98.10  ?  169  ALA F CA  1 
ATOM   16634 C  C   . ALA F 6  169  ? -40.933 26.939   52.576  1.00 104.52 ?  169  ALA F C   1 
ATOM   16635 O  O   . ALA F 6  169  ? -41.408 27.925   53.153  1.00 111.38 ?  169  ALA F O   1 
ATOM   16636 C  CB  . ALA F 6  169  ? -39.280 27.319   50.727  1.00 89.89  ?  169  ALA F CB  1 
ATOM   16637 N  N   . TRP F 6  170  ? -41.672 25.871   52.268  1.00 122.91 ?  170  TRP F N   1 
ATOM   16638 C  CA  . TRP F 6  170  ? -43.071 25.801   52.678  1.00 131.54 ?  170  TRP F CA  1 
ATOM   16639 C  C   . TRP F 6  170  ? -43.205 25.679   54.190  1.00 139.47 ?  170  TRP F C   1 
ATOM   16640 O  O   . TRP F 6  170  ? -44.168 26.195   54.769  1.00 144.11 ?  170  TRP F O   1 
ATOM   16641 C  CB  . TRP F 6  170  ? -43.764 24.627   51.988  1.00 133.15 ?  170  TRP F CB  1 
ATOM   16642 C  CG  . TRP F 6  170  ? -44.087 24.878   50.547  1.00 135.97 ?  170  TRP F CG  1 
ATOM   16643 C  CD1 . TRP F 6  170  ? -44.000 26.066   49.881  1.00 131.30 ?  170  TRP F CD1 1 
ATOM   16644 C  CD2 . TRP F 6  170  ? -44.552 23.916   49.592  1.00 141.32 ?  170  TRP F CD2 1 
ATOM   16645 N  NE1 . TRP F 6  170  ? -44.381 25.902   48.571  1.00 128.88 ?  170  TRP F NE1 1 
ATOM   16646 C  CE2 . TRP F 6  170  ? -44.724 24.592   48.368  1.00 133.74 ?  170  TRP F CE2 1 
ATOM   16647 C  CE3 . TRP F 6  170  ? -44.838 22.548   49.654  1.00 132.41 ?  170  TRP F CE3 1 
ATOM   16648 C  CZ2 . TRP F 6  170  ? -45.170 23.947   47.217  1.00 131.50 ?  170  TRP F CZ2 1 
ATOM   16649 C  CZ3 . TRP F 6  170  ? -45.280 21.910   48.510  1.00 124.52 ?  170  TRP F CZ3 1 
ATOM   16650 C  CH2 . TRP F 6  170  ? -45.442 22.609   47.308  1.00 125.96 ?  170  TRP F CH2 1 
ATOM   16651 N  N   . SER F 6  171  ? -42.257 25.004   54.845  1.00 142.58 ?  171  SER F N   1 
ATOM   16652 C  CA  . SER F 6  171  ? -42.302 24.897   56.300  1.00 141.48 ?  171  SER F CA  1 
ATOM   16653 C  C   . SER F 6  171  ? -41.996 26.235   56.961  1.00 143.07 ?  171  SER F C   1 
ATOM   16654 O  O   . SER F 6  171  ? -42.578 26.568   58.000  1.00 144.00 ?  171  SER F O   1 
ATOM   16655 C  CB  . SER F 6  171  ? -41.325 23.823   56.777  1.00 140.14 ?  171  SER F CB  1 
ATOM   16656 O  OG  . SER F 6  171  ? -41.383 23.670   58.185  1.00 151.20 ?  171  SER F OG  1 
ATOM   16657 N  N   . ARG F 6  172  ? -41.081 27.014   56.376  1.00 120.21 ?  172  ARG F N   1 
ATOM   16658 C  CA  . ARG F 6  172  ? -40.821 28.356   56.887  1.00 116.18 ?  172  ARG F CA  1 
ATOM   16659 C  C   . ARG F 6  172  ? -42.038 29.254   56.710  1.00 124.99 ?  172  ARG F C   1 
ATOM   16660 O  O   . ARG F 6  172  ? -42.392 30.016   57.617  1.00 127.67 ?  172  ARG F O   1 
ATOM   16661 C  CB  . ARG F 6  172  ? -39.607 28.964   56.184  1.00 116.53 ?  172  ARG F CB  1 
ATOM   16662 C  CG  . ARG F 6  172  ? -38.326 28.164   56.329  1.00 109.61 ?  172  ARG F CG  1 
ATOM   16663 C  CD  . ARG F 6  172  ? -37.691 28.352   57.693  1.00 113.86 ?  172  ARG F CD  1 
ATOM   16664 N  NE  . ARG F 6  172  ? -36.400 27.678   57.779  1.00 118.91 ?  172  ARG F NE  1 
ATOM   16665 C  CZ  . ARG F 6  172  ? -35.270 28.156   57.276  1.00 121.89 ?  172  ARG F CZ  1 
ATOM   16666 N  NH1 . ARG F 6  172  ? -35.230 29.319   56.646  1.00 117.89 ?  172  ARG F NH1 1 
ATOM   16667 N  NH2 . ARG F 6  172  ? -34.151 27.448   57.408  1.00 120.67 ?  172  ARG F NH2 1 
ATOM   16668 N  N   . GLN F 6  173  ? -42.692 29.175   55.548  1.00 117.93 ?  173  GLN F N   1 
ATOM   16669 C  CA  . GLN F 6  173  ? -43.892 29.966   55.305  1.00 119.77 ?  173  GLN F CA  1 
ATOM   16670 C  C   . GLN F 6  173  ? -45.050 29.545   56.199  1.00 121.16 ?  173  GLN F C   1 
ATOM   16671 O  O   . GLN F 6  173  ? -45.964 30.345   56.426  1.00 128.34 ?  173  GLN F O   1 
ATOM   16672 C  CB  . GLN F 6  173  ? -44.303 29.859   53.836  1.00 117.55 ?  173  GLN F CB  1 
ATOM   16673 C  CG  . GLN F 6  173  ? -43.409 30.631   52.878  1.00 115.46 ?  173  GLN F CG  1 
ATOM   16674 C  CD  . GLN F 6  173  ? -43.767 30.385   51.426  1.00 117.31 ?  173  GLN F CD  1 
ATOM   16675 O  OE1 . GLN F 6  173  ? -44.790 29.771   51.123  1.00 117.26 ?  173  GLN F OE1 1 
ATOM   16676 N  NE2 . GLN F 6  173  ? -42.923 30.862   50.519  1.00 125.98 ?  173  GLN F NE2 1 
ATOM   16677 N  N   . GLN F 6  174  ? -45.033 28.310   56.706  1.00 144.13 ?  174  GLN F N   1 
ATOM   16678 C  CA  . GLN F 6  174  ? -46.078 27.873   57.624  1.00 148.64 ?  174  GLN F CA  1 
ATOM   16679 C  C   . GLN F 6  174  ? -46.050 28.670   58.921  1.00 152.99 ?  174  GLN F C   1 
ATOM   16680 O  O   . GLN F 6  174  ? -47.083 28.811   59.586  1.00 153.96 ?  174  GLN F O   1 
ATOM   16681 C  CB  . GLN F 6  174  ? -45.930 26.379   57.915  1.00 150.23 ?  174  GLN F CB  1 
ATOM   16682 C  CG  . GLN F 6  174  ? -47.212 25.707   58.371  1.00 151.35 ?  174  GLN F CG  1 
ATOM   16683 C  CD  . GLN F 6  174  ? -46.986 24.287   58.847  1.00 151.31 ?  174  GLN F CD  1 
ATOM   16684 O  OE1 . GLN F 6  174  ? -45.855 23.885   59.121  1.00 149.67 ?  174  GLN F OE1 1 
ATOM   16685 N  NE2 . GLN F 6  174  ? -48.064 23.518   58.951  1.00 148.45 ?  174  GLN F NE2 1 
ATOM   16686 N  N   . ASP F 6  175  ? -44.886 29.200   59.292  1.00 138.01 ?  175  ASP F N   1 
ATOM   16687 C  CA  . ASP F 6  175  ? -44.751 30.023   60.486  1.00 133.03 ?  175  ASP F CA  1 
ATOM   16688 C  C   . ASP F 6  175  ? -45.278 31.438   60.293  1.00 129.37 ?  175  ASP F C   1 
ATOM   16689 O  O   . ASP F 6  175  ? -45.209 32.240   61.231  1.00 122.08 ?  175  ASP F O   1 
ATOM   16690 C  CB  . ASP F 6  175  ? -43.283 30.074   60.919  1.00 130.24 ?  175  ASP F CB  1 
ATOM   16691 C  CG  . ASP F 6  175  ? -42.708 28.697   61.192  1.00 133.26 ?  175  ASP F CG  1 
ATOM   16692 O  OD1 . ASP F 6  175  ? -43.459 27.704   61.086  1.00 132.40 ?  175  ASP F OD1 1 
ATOM   16693 O  OD2 . ASP F 6  175  ? -41.503 28.606   61.509  1.00 136.64 -1 175  ASP F OD2 1 
ATOM   16694 N  N   . ALA F 6  176  ? -45.797 31.765   59.108  1.00 126.28 ?  176  ALA F N   1 
ATOM   16695 C  CA  . ALA F 6  176  ? -46.329 33.093   58.823  1.00 126.09 ?  176  ALA F CA  1 
ATOM   16696 C  C   . ALA F 6  176  ? -47.853 33.119   58.883  1.00 129.16 ?  176  ALA F C   1 
ATOM   16697 O  O   . ALA F 6  176  ? -48.434 33.886   59.657  1.00 129.82 ?  176  ALA F O   1 
ATOM   16698 C  CB  . ALA F 6  176  ? -45.837 33.574   57.452  1.00 120.36 ?  176  ALA F CB  1 
ATOM   16699 N  N   . GLY F 6  177  ? -48.512 32.295   58.079  1.00 112.90 ?  177  GLY F N   1 
ATOM   16700 C  CA  . GLY F 6  177  ? -49.962 32.261   58.075  1.00 114.86 ?  177  GLY F CA  1 
ATOM   16701 C  C   . GLY F 6  177  ? -50.469 31.203   57.119  1.00 113.59 ?  177  GLY F C   1 
ATOM   16702 O  O   . GLY F 6  177  ? -49.753 30.747   56.221  1.00 109.41 ?  177  GLY F O   1 
ATOM   16703 N  N   . GLY F 6  178  ? -51.728 30.823   57.331  1.00 149.95 ?  178  GLY F N   1 
ATOM   16704 C  CA  . GLY F 6  178  ? -52.380 29.834   56.493  1.00 153.30 ?  178  GLY F CA  1 
ATOM   16705 C  C   . GLY F 6  178  ? -51.796 28.444   56.637  1.00 163.58 ?  178  GLY F C   1 
ATOM   16706 O  O   . GLY F 6  178  ? -51.394 27.827   55.646  1.00 171.89 ?  178  GLY F O   1 
ATOM   16707 N  N   . ASP F 6  179  ? -51.752 27.936   57.867  1.00 215.93 ?  179  ASP F N   1 
ATOM   16708 C  CA  . ASP F 6  179  ? -51.149 26.638   58.139  1.00 219.23 ?  179  ASP F CA  1 
ATOM   16709 C  C   . ASP F 6  179  ? -52.131 25.477   58.023  1.00 221.21 ?  179  ASP F C   1 
ATOM   16710 O  O   . ASP F 6  179  ? -51.710 24.343   57.764  1.00 214.07 ?  179  ASP F O   1 
ATOM   16711 C  CB  . ASP F 6  179  ? -50.508 26.644   59.532  1.00 220.88 ?  179  ASP F CB  1 
ATOM   16712 C  CG  . ASP F 6  179  ? -51.532 26.713   60.657  1.00 228.88 ?  179  ASP F CG  1 
ATOM   16713 O  OD1 . ASP F 6  179  ? -52.727 26.957   60.385  1.00 232.57 ?  179  ASP F OD1 1 
ATOM   16714 O  OD2 . ASP F 6  179  ? -51.136 26.510   61.825  1.00 229.32 -1 179  ASP F OD2 1 
ATOM   16715 N  N   . ALA F 6  180  ? -53.427 25.727   58.211  1.00 157.18 ?  180  ALA F N   1 
ATOM   16716 C  CA  . ALA F 6  180  ? -54.424 24.663   58.184  1.00 156.12 ?  180  ALA F CA  1 
ATOM   16717 C  C   . ALA F 6  180  ? -54.924 24.379   56.771  1.00 157.72 ?  180  ALA F C   1 
ATOM   16718 O  O   . ALA F 6  180  ? -54.897 23.230   56.318  1.00 151.88 ?  180  ALA F O   1 
ATOM   16719 C  CB  . ALA F 6  180  ? -55.597 25.022   59.100  1.00 159.38 ?  180  ALA F CB  1 
ATOM   16720 N  N   . LYS F 6  181  ? -55.380 25.415   56.063  1.00 218.84 ?  181  LYS F N   1 
ATOM   16721 C  CA  . LYS F 6  181  ? -55.913 25.218   54.719  1.00 224.80 ?  181  LYS F CA  1 
ATOM   16722 C  C   . LYS F 6  181  ? -54.824 24.759   53.756  1.00 213.79 ?  181  LYS F C   1 
ATOM   16723 O  O   . LYS F 6  181  ? -54.993 23.764   53.042  1.00 204.30 ?  181  LYS F O   1 
ATOM   16724 C  CB  . LYS F 6  181  ? -56.569 26.508   54.222  1.00 230.87 ?  181  LYS F CB  1 
ATOM   16725 C  CG  . LYS F 6  181  ? -57.780 26.944   55.033  1.00 225.47 ?  181  LYS F CG  1 
ATOM   16726 C  CD  . LYS F 6  181  ? -58.992 26.074   54.746  1.00 227.11 ?  181  LYS F CD  1 
ATOM   16727 C  CE  . LYS F 6  181  ? -59.490 26.273   53.324  1.00 234.04 ?  181  LYS F CE  1 
ATOM   16728 N  NZ  . LYS F 6  181  ? -60.713 25.471   53.045  1.00 232.96 ?  181  LYS F NZ  1 
ATOM   16729 N  N   . LYS F 6  182  ? -53.700 25.466   53.727  1.00 152.26 ?  182  LYS F N   1 
ATOM   16730 C  CA  . LYS F 6  182  ? -52.568 25.140   52.868  1.00 142.34 ?  182  LYS F CA  1 
ATOM   16731 C  C   . LYS F 6  182  ? -51.331 24.897   53.735  1.00 134.67 ?  182  LYS F C   1 
ATOM   16732 O  O   . LYS F 6  182  ? -51.409 24.850   54.967  1.00 138.91 ?  182  LYS F O   1 
ATOM   16733 C  CB  . LYS F 6  182  ? -52.337 26.257   51.846  1.00 156.02 ?  182  LYS F CB  1 
ATOM   16734 C  CG  . LYS F 6  182  ? -53.521 26.513   50.919  1.00 162.63 ?  182  LYS F CG  1 
ATOM   16735 C  CD  . LYS F 6  182  ? -53.145 27.469   49.798  1.00 164.95 ?  182  LYS F CD  1 
ATOM   16736 C  CE  . LYS F 6  182  ? -52.840 28.858   50.334  1.00 164.52 ?  182  LYS F CE  1 
ATOM   16737 N  NZ  . LYS F 6  182  ? -54.044 29.515   50.911  1.00 160.61 ?  182  LYS F NZ  1 
ATOM   16738 N  N   . LEU F 6  183  ? -50.184 24.741   53.074  1.00 131.23 ?  183  LEU F N   1 
ATOM   16739 C  CA  . LEU F 6  183  ? -48.877 24.535   53.694  1.00 132.38 ?  183  LEU F CA  1 
ATOM   16740 C  C   . LEU F 6  183  ? -48.826 23.292   54.575  1.00 132.05 ?  183  LEU F C   1 
ATOM   16741 O  O   . LEU F 6  183  ? -47.828 23.077   55.269  1.00 129.17 ?  183  LEU F O   1 
ATOM   16742 C  CB  . LEU F 6  183  ? -48.431 25.769   54.494  1.00 126.94 ?  183  LEU F CB  1 
ATOM   16743 C  CG  . LEU F 6  183  ? -48.493 27.088   53.729  1.00 125.96 ?  183  LEU F CG  1 
ATOM   16744 C  CD1 . LEU F 6  183  ? -48.294 28.244   54.686  1.00 129.93 ?  183  LEU F CD1 1 
ATOM   16745 C  CD2 . LEU F 6  183  ? -47.449 27.099   52.627  1.00 122.86 ?  183  LEU F CD2 1 
ATOM   16746 N  N   . ALA F 6  184  ? -49.878 22.471   54.565  1.00 208.56 ?  184  ALA F N   1 
ATOM   16747 C  CA  . ALA F 6  184  ? -49.923 21.173   55.235  1.00 208.95 ?  184  ALA F CA  1 
ATOM   16748 C  C   . ALA F 6  184  ? -50.421 20.067   54.314  1.00 203.95 ?  184  ALA F C   1 
ATOM   16749 O  O   . ALA F 6  184  ? -49.967 18.922   54.425  1.00 201.96 ?  184  ALA F O   1 
ATOM   16750 C  CB  . ALA F 6  184  ? -50.800 21.245   56.494  1.00 211.07 ?  184  ALA F CB  1 
ATOM   16751 N  N   . THR F 6  185  ? -51.340 20.381   53.399  1.00 199.24 ?  185  THR F N   1 
ATOM   16752 C  CA  . THR F 6  185  ? -51.790 19.441   52.380  1.00 199.82 ?  185  THR F CA  1 
ATOM   16753 C  C   . THR F 6  185  ? -50.893 19.480   51.156  1.00 195.48 ?  185  THR F C   1 
ATOM   16754 O  O   . THR F 6  185  ? -50.655 18.438   50.538  1.00 200.98 ?  185  THR F O   1 
ATOM   16755 C  CB  . THR F 6  185  ? -53.247 19.732   51.975  1.00 204.35 ?  185  THR F CB  1 
ATOM   16756 O  OG1 . THR F 6  185  ? -54.060 19.865   53.148  1.00 209.65 ?  185  THR F OG1 1 
ATOM   16757 C  CG2 . THR F 6  185  ? -53.828 18.620   51.097  1.00 205.10 ?  185  THR F CG2 1 
ATOM   16758 N  N   . ARG F 6  186  ? -50.396 20.668   50.801  1.00 149.24 ?  186  ARG F N   1 
ATOM   16759 C  CA  . ARG F 6  186  ? -49.461 20.793   49.689  1.00 153.75 ?  186  ARG F CA  1 
ATOM   16760 C  C   . ARG F 6  186  ? -48.191 19.997   49.955  1.00 143.88 ?  186  ARG F C   1 
ATOM   16761 O  O   . ARG F 6  186  ? -47.689 19.291   49.073  1.00 139.35 ?  186  ARG F O   1 
ATOM   16762 C  CB  . ARG F 6  186  ? -49.131 22.266   49.452  1.00 162.37 ?  186  ARG F CB  1 
ATOM   16763 C  CG  . ARG F 6  186  ? -50.329 23.144   49.128  1.00 165.47 ?  186  ARG F CG  1 
ATOM   16764 C  CD  . ARG F 6  186  ? -49.910 24.310   48.242  1.00 157.98 ?  186  ARG F CD  1 
ATOM   16765 N  NE  . ARG F 6  186  ? -49.032 25.241   48.942  1.00 160.36 ?  186  ARG F NE  1 
ATOM   16766 C  CZ  . ARG F 6  186  ? -48.615 26.398   48.446  1.00 163.33 ?  186  ARG F CZ  1 
ATOM   16767 N  NH1 . ARG F 6  186  ? -48.989 26.810   47.245  1.00 169.56 ?  186  ARG F NH1 1 
ATOM   16768 N  NH2 . ARG F 6  186  ? -47.806 27.162   49.174  1.00 161.41 ?  186  ARG F NH2 1 
ATOM   16769 N  N   . MET F 6  187  ? -47.647 20.111   51.169  1.00 136.07 ?  187  MET F N   1 
ATOM   16770 C  CA  . MET F 6  187  ? -46.454 19.350   51.518  1.00 135.41 ?  187  MET F CA  1 
ATOM   16771 C  C   . MET F 6  187  ? -46.742 17.856   51.568  1.00 129.33 ?  187  MET F C   1 
ATOM   16772 O  O   . MET F 6  187  ? -45.847 17.043   51.311  1.00 127.30 ?  187  MET F O   1 
ATOM   16773 C  CB  . MET F 6  187  ? -45.901 19.831   52.859  1.00 143.40 ?  187  MET F CB  1 
ATOM   16774 C  CG  . MET F 6  187  ? -45.501 21.298   52.869  1.00 143.59 ?  187  MET F CG  1 
ATOM   16775 S  SD  . MET F 6  187  ? -44.926 21.876   54.477  1.00 145.42 ?  187  MET F SD  1 
ATOM   16776 C  CE  . MET F 6  187  ? -43.291 21.155   54.526  1.00 133.57 ?  187  MET F CE  1 
ATOM   16777 N  N   . ARG F 6  188  ? -47.981 17.479   51.894  1.00 128.69 ?  188  ARG F N   1 
ATOM   16778 C  CA  . ARG F 6  188  ? -48.346 16.067   51.924  1.00 124.74 ?  188  ARG F CA  1 
ATOM   16779 C  C   . ARG F 6  188  ? -48.389 15.479   50.520  1.00 124.03 ?  188  ARG F C   1 
ATOM   16780 O  O   . ARG F 6  188  ? -47.891 14.371   50.289  1.00 131.36 ?  188  ARG F O   1 
ATOM   16781 C  CB  . ARG F 6  188  ? -49.694 15.888   52.622  1.00 128.26 ?  188  ARG F CB  1 
ATOM   16782 C  CG  . ARG F 6  188  ? -50.088 14.436   52.854  1.00 124.72 ?  188  ARG F CG  1 
ATOM   16783 C  CD  . ARG F 6  188  ? -51.103 14.308   53.980  1.00 134.15 ?  188  ARG F CD  1 
ATOM   16784 N  NE  . ARG F 6  188  ? -52.317 15.071   53.710  1.00 144.84 ?  188  ARG F NE  1 
ATOM   16785 C  CZ  . ARG F 6  188  ? -52.676 16.166   54.365  1.00 142.21 ?  188  ARG F CZ  1 
ATOM   16786 N  NH1 . ARG F 6  188  ? -51.932 16.664   55.340  1.00 145.84 ?  188  ARG F NH1 1 
ATOM   16787 N  NH2 . ARG F 6  188  ? -53.809 16.779   54.033  1.00 138.94 ?  188  ARG F NH2 1 
ATOM   16788 N  N   . ARG F 6  189  ? -48.981 16.205   49.569  1.00 106.27 ?  189  ARG F N   1 
ATOM   16789 C  CA  . ARG F 6  189  ? -49.040 15.712   48.197  1.00 105.68 ?  189  ARG F CA  1 
ATOM   16790 C  C   . ARG F 6  189  ? -47.659 15.705   47.553  1.00 99.81  ?  189  ARG F C   1 
ATOM   16791 O  O   . ARG F 6  189  ? -47.330 14.787   46.792  1.00 99.84  ?  189  ARG F O   1 
ATOM   16792 C  CB  . ARG F 6  189  ? -50.013 16.557   47.376  1.00 116.78 ?  189  ARG F CB  1 
ATOM   16793 C  CG  . ARG F 6  189  ? -51.405 16.664   47.980  1.00 120.58 ?  189  ARG F CG  1 
ATOM   16794 C  CD  . ARG F 6  189  ? -52.278 17.620   47.185  1.00 119.62 ?  189  ARG F CD  1 
ATOM   16795 N  NE  . ARG F 6  189  ? -51.654 18.929   47.039  1.00 114.84 ?  189  ARG F NE  1 
ATOM   16796 C  CZ  . ARG F 6  189  ? -52.236 19.977   46.473  1.00 112.80 ?  189  ARG F CZ  1 
ATOM   16797 N  NH1 . ARG F 6  189  ? -53.466 19.909   45.991  1.00 104.37 ?  189  ARG F NH1 1 
ATOM   16798 N  NH2 . ARG F 6  189  ? -51.566 21.123   46.388  1.00 123.32 ?  189  ARG F NH2 1 
ATOM   16799 N  N   . LEU F 6  190  ? -46.839 16.720   47.839  1.00 92.74  ?  190  LEU F N   1 
ATOM   16800 C  CA  . LEU F 6  190  ? -45.476 16.734   47.319  1.00 97.27  ?  190  LEU F CA  1 
ATOM   16801 C  C   . LEU F 6  190  ? -44.667 15.568   47.870  1.00 101.12 ?  190  LEU F C   1 
ATOM   16802 O  O   . LEU F 6  190  ? -43.858 14.968   47.153  1.00 99.54  ?  190  LEU F O   1 
ATOM   16803 C  CB  . LEU F 6  190  ? -44.795 18.062   47.653  1.00 108.10 ?  190  LEU F CB  1 
ATOM   16804 C  CG  . LEU F 6  190  ? -43.520 18.369   46.862  1.00 101.56 ?  190  LEU F CG  1 
ATOM   16805 C  CD1 . LEU F 6  190  ? -43.840 18.616   45.395  1.00 92.01  ?  190  LEU F CD1 1 
ATOM   16806 C  CD2 . LEU F 6  190  ? -42.775 19.554   47.461  1.00 102.76 ?  190  LEU F CD2 1 
ATOM   16807 N  N   . SER F 6  191  ? -44.872 15.232   49.146  1.00 177.77 ?  191  SER F N   1 
ATOM   16808 C  CA  . SER F 6  191  ? -44.199 14.073   49.719  1.00 172.61 ?  191  SER F CA  1 
ATOM   16809 C  C   . SER F 6  191  ? -44.730 12.772   49.131  1.00 174.20 ?  191  SER F C   1 
ATOM   16810 O  O   . SER F 6  191  ? -43.981 11.795   49.020  1.00 174.72 ?  191  SER F O   1 
ATOM   16811 C  CB  . SER F 6  191  ? -44.355 14.074   51.239  1.00 168.51 ?  191  SER F CB  1 
ATOM   16812 O  OG  . SER F 6  191  ? -43.897 15.294   51.796  1.00 177.16 ?  191  SER F OG  1 
ATOM   16813 N  N   . GLY F 6  192  ? -46.008 12.741   48.746  1.00 123.72 ?  192  GLY F N   1 
ATOM   16814 C  CA  . GLY F 6  192  ? -46.566 11.528   48.169  1.00 118.62 ?  192  GLY F CA  1 
ATOM   16815 C  C   . GLY F 6  192  ? -45.904 11.151   46.857  1.00 110.46 ?  192  GLY F C   1 
ATOM   16816 O  O   . GLY F 6  192  ? -45.496 10.004   46.659  1.00 106.26 ?  192  GLY F O   1 
ATOM   16817 N  N   . ILE F 6  193  ? -45.789 12.116   45.942  1.00 93.38  ?  193  ILE F N   1 
ATOM   16818 C  CA  . ILE F 6  193  ? -45.100 11.858   44.683  1.00 88.06  ?  193  ILE F CA  1 
ATOM   16819 C  C   . ILE F 6  193  ? -43.594 11.791   44.901  1.00 88.60  ?  193  ILE F C   1 
ATOM   16820 O  O   . ILE F 6  193  ? -42.882 11.091   44.169  1.00 81.52  ?  193  ILE F O   1 
ATOM   16821 C  CB  . ILE F 6  193  ? -45.478 12.925   43.638  1.00 90.12  ?  193  ILE F CB  1 
ATOM   16822 C  CG1 . ILE F 6  193  ? -44.871 12.584   42.275  1.00 89.52  ?  193  ILE F CG1 1 
ATOM   16823 C  CG2 . ILE F 6  193  ? -45.036 14.312   44.092  1.00 95.53  ?  193  ILE F CG2 1 
ATOM   16824 C  CD1 . ILE F 6  193  ? -45.456 11.341   41.643  1.00 95.96  ?  193  ILE F CD1 1 
ATOM   16825 N  N   . GLY F 6  194  ? -43.084 12.499   45.912  1.00 96.40  ?  194  GLY F N   1 
ATOM   16826 C  CA  . GLY F 6  194  ? -41.655 12.488   46.166  1.00 95.22  ?  194  GLY F CA  1 
ATOM   16827 C  C   . GLY F 6  194  ? -41.145 11.155   46.672  1.00 90.88  ?  194  GLY F C   1 
ATOM   16828 O  O   . GLY F 6  194  ? -39.988 10.801   46.429  1.00 86.46  ?  194  GLY F O   1 
ATOM   16829 N  N   . VAL F 6  195  ? -41.989 10.403   47.386  1.00 130.08 ?  195  VAL F N   1 
ATOM   16830 C  CA  . VAL F 6  195  ? -41.572 9.105    47.914  1.00 134.30 ?  195  VAL F CA  1 
ATOM   16831 C  C   . VAL F 6  195  ? -41.201 8.163    46.775  1.00 137.24 ?  195  VAL F C   1 
ATOM   16832 O  O   . VAL F 6  195  ? -40.147 7.517    46.799  1.00 135.46 ?  195  VAL F O   1 
ATOM   16833 C  CB  . VAL F 6  195  ? -42.676 8.508    48.807  1.00 134.83 ?  195  VAL F CB  1 
ATOM   16834 C  CG1 . VAL F 6  195  ? -42.511 7.000    48.926  1.00 125.39 ?  195  VAL F CG1 1 
ATOM   16835 C  CG2 . VAL F 6  195  ? -42.646 9.151    50.183  1.00 129.51 ?  195  VAL F CG2 1 
ATOM   16836 N  N   . ALA F 6  196  ? -42.060 8.076    45.757  1.00 109.06 ?  196  ALA F N   1 
ATOM   16837 C  CA  . ALA F 6  196  ? -41.739 7.258    44.592  1.00 97.35  ?  196  ALA F CA  1 
ATOM   16838 C  C   . ALA F 6  196  ? -40.527 7.810    43.854  1.00 98.62  ?  196  ALA F C   1 
ATOM   16839 O  O   . ALA F 6  196  ? -39.661 7.047    43.408  1.00 108.30 ?  196  ALA F O   1 
ATOM   16840 C  CB  . ALA F 6  196  ? -42.946 7.172    43.660  1.00 83.62  ?  196  ALA F CB  1 
ATOM   16841 N  N   . LEU F 6  197  ? -40.446 9.136    43.721  1.00 80.92  ?  197  LEU F N   1 
ATOM   16842 C  CA  . LEU F 6  197  ? -39.278 9.749    43.097  1.00 83.99  ?  197  LEU F CA  1 
ATOM   16843 C  C   . LEU F 6  197  ? -38.013 9.463    43.896  1.00 82.72  ?  197  LEU F C   1 
ATOM   16844 O  O   . LEU F 6  197  ? -36.968 9.135    43.323  1.00 77.82  ?  197  LEU F O   1 
ATOM   16845 C  CB  . LEU F 6  197  ? -39.492 11.257   42.958  1.00 89.94  ?  197  LEU F CB  1 
ATOM   16846 C  CG  . LEU F 6  197  ? -40.228 11.762   41.716  1.00 81.89  ?  197  LEU F CG  1 
ATOM   16847 C  CD1 . LEU F 6  197  ? -40.615 13.222   41.890  1.00 86.39  ?  197  LEU F CD1 1 
ATOM   16848 C  CD2 . LEU F 6  197  ? -39.371 11.577   40.475  1.00 72.66  ?  197  LEU F CD2 1 
ATOM   16849 N  N   . PHE F 6  198  ? -38.092 9.570    45.225  1.00 89.52  ?  198  PHE F N   1 
ATOM   16850 C  CA  . PHE F 6  198  ? -36.913 9.374    46.062  1.00 93.21  ?  198  PHE F CA  1 
ATOM   16851 C  C   . PHE F 6  198  ? -36.458 7.919    46.046  1.00 91.44  ?  198  PHE F C   1 
ATOM   16852 O  O   . PHE F 6  198  ? -35.254 7.639    46.096  1.00 92.30  ?  198  PHE F O   1 
ATOM   16853 C  CB  . PHE F 6  198  ? -37.211 9.848    47.488  1.00 92.45  ?  198  PHE F CB  1 
ATOM   16854 C  CG  . PHE F 6  198  ? -36.213 9.391    48.517  1.00 89.82  ?  198  PHE F CG  1 
ATOM   16855 C  CD1 . PHE F 6  198  ? -35.088 10.152   48.790  1.00 99.54  ?  198  PHE F CD1 1 
ATOM   16856 C  CD2 . PHE F 6  198  ? -36.418 8.225    49.239  1.00 89.04  ?  198  PHE F CD2 1 
ATOM   16857 C  CE1 . PHE F 6  198  ? -34.174 9.747    49.745  1.00 92.77  ?  198  PHE F CE1 1 
ATOM   16858 C  CE2 . PHE F 6  198  ? -35.505 7.813    50.192  1.00 89.00  ?  198  PHE F CE2 1 
ATOM   16859 C  CZ  . PHE F 6  198  ? -34.382 8.576    50.445  1.00 86.15  ?  198  PHE F CZ  1 
ATOM   16860 N  N   . VAL F 6  199  ? -37.403 6.980    45.972  1.00 92.17  ?  199  VAL F N   1 
ATOM   16861 C  CA  . VAL F 6  199  ? -37.045 5.564    45.941  1.00 89.41  ?  199  VAL F CA  1 
ATOM   16862 C  C   . VAL F 6  199  ? -36.313 5.226    44.647  1.00 94.24  ?  199  VAL F C   1 
ATOM   16863 O  O   . VAL F 6  199  ? -35.278 4.548    44.660  1.00 95.04  ?  199  VAL F O   1 
ATOM   16864 C  CB  . VAL F 6  199  ? -38.299 4.690    46.127  1.00 84.21  ?  199  VAL F CB  1 
ATOM   16865 C  CG1 . VAL F 6  199  ? -38.024 3.261    45.687  1.00 79.42  ?  199  VAL F CG1 1 
ATOM   16866 C  CG2 . VAL F 6  199  ? -38.751 4.721    47.576  1.00 82.87  ?  199  VAL F CG2 1 
ATOM   16867 N  N   . ILE F 6  200  ? -36.830 5.703    43.513  1.00 92.15  ?  200  ILE F N   1 
ATOM   16868 C  CA  . ILE F 6  200  ? -36.209 5.403    42.227  1.00 91.60  ?  200  ILE F CA  1 
ATOM   16869 C  C   . ILE F 6  200  ? -34.829 6.043    42.135  1.00 93.24  ?  200  ILE F C   1 
ATOM   16870 O  O   . ILE F 6  200  ? -33.856 5.403    41.719  1.00 99.18  ?  200  ILE F O   1 
ATOM   16871 C  CB  . ILE F 6  200  ? -37.119 5.858    41.071  1.00 91.38  ?  200  ILE F CB  1 
ATOM   16872 C  CG1 . ILE F 6  200  ? -38.465 5.133    41.126  1.00 89.23  ?  200  ILE F CG1 1 
ATOM   16873 C  CG2 . ILE F 6  200  ? -36.442 5.618    39.730  1.00 85.31  ?  200  ILE F CG2 1 
ATOM   16874 C  CD1 . ILE F 6  200  ? -38.360 3.633    40.951  1.00 90.86  ?  200  ILE F CD1 1 
ATOM   16875 N  N   . THR F 6  201  ? -34.721 7.312    42.536  1.00 78.59  ?  201  THR F N   1 
ATOM   16876 C  CA  . THR F 6  201  ? -33.460 8.033    42.386  1.00 82.99  ?  201  THR F CA  1 
ATOM   16877 C  C   . THR F 6  201  ? -32.370 7.453    43.282  1.00 82.40  ?  201  THR F C   1 
ATOM   16878 O  O   . THR F 6  201  ? -31.222 7.302    42.850  1.00 82.60  ?  201  THR F O   1 
ATOM   16879 C  CB  . THR F 6  201  ? -33.662 9.519    42.685  1.00 84.43  ?  201  THR F CB  1 
ATOM   16880 O  OG1 . THR F 6  201  ? -34.300 9.670    43.959  1.00 82.64  ?  201  THR F OG1 1 
ATOM   16881 C  CG2 . THR F 6  201  ? -34.525 10.166   41.612  1.00 82.26  ?  201  THR F CG2 1 
ATOM   16882 N  N   . VAL F 6  202  ? -32.706 7.125    44.532  1.00 88.92  ?  202  VAL F N   1 
ATOM   16883 C  CA  . VAL F 6  202  ? -31.701 6.599    45.451  1.00 91.55  ?  202  VAL F CA  1 
ATOM   16884 C  C   . VAL F 6  202  ? -31.273 5.197    45.033  1.00 89.14  ?  202  VAL F C   1 
ATOM   16885 O  O   . VAL F 6  202  ? -30.096 4.832    45.150  1.00 86.39  ?  202  VAL F O   1 
ATOM   16886 C  CB  . VAL F 6  202  ? -32.233 6.631    46.896  1.00 89.42  ?  202  VAL F CB  1 
ATOM   16887 C  CG1 . VAL F 6  202  ? -31.369 5.780    47.813  1.00 83.63  ?  202  VAL F CG1 1 
ATOM   16888 C  CG2 . VAL F 6  202  ? -32.284 8.061    47.399  1.00 88.53  ?  202  VAL F CG2 1 
ATOM   16889 N  N   . THR F 6  203  ? -32.213 4.395    44.529  1.00 80.52  ?  203  THR F N   1 
ATOM   16890 C  CA  . THR F 6  203  ? -31.874 3.051    44.069  1.00 77.80  ?  203  THR F CA  1 
ATOM   16891 C  C   . THR F 6  203  ? -30.871 3.104    42.924  1.00 78.49  ?  203  THR F C   1 
ATOM   16892 O  O   . THR F 6  203  ? -29.877 2.367    42.917  1.00 75.41  ?  203  THR F O   1 
ATOM   16893 C  CB  . THR F 6  203  ? -33.139 2.306    43.641  1.00 79.70  ?  203  THR F CB  1 
ATOM   16894 O  OG1 . THR F 6  203  ? -34.012 2.153    44.768  1.00 78.56  ?  203  THR F OG1 1 
ATOM   16895 C  CG2 . THR F 6  203  ? -32.790 0.934    43.086  1.00 80.39  ?  203  THR F CG2 1 
ATOM   16896 N  N   . PHE F 6  204  ? -31.110 3.982    41.948  1.00 110.10 ?  204  PHE F N   1 
ATOM   16897 C  CA  . PHE F 6  204  ? -30.189 4.103    40.824  1.00 110.48 ?  204  PHE F CA  1 
ATOM   16898 C  C   . PHE F 6  204  ? -28.907 4.820    41.226  1.00 111.18 ?  204  PHE F C   1 
ATOM   16899 O  O   . PHE F 6  204  ? -27.852 4.581    40.626  1.00 105.97 ?  204  PHE F O   1 
ATOM   16900 C  CB  . PHE F 6  204  ? -30.871 4.828    39.666  1.00 93.60  ?  204  PHE F CB  1 
ATOM   16901 C  CG  . PHE F 6  204  ? -31.721 3.933    38.812  1.00 93.13  ?  204  PHE F CG  1 
ATOM   16902 C  CD1 . PHE F 6  204  ? -31.157 2.872    38.124  1.00 90.52  ?  204  PHE F CD1 1 
ATOM   16903 C  CD2 . PHE F 6  204  ? -33.085 4.147    38.706  1.00 100.10 ?  204  PHE F CD2 1 
ATOM   16904 C  CE1 . PHE F 6  204  ? -31.938 2.044    37.341  1.00 93.85  ?  204  PHE F CE1 1 
ATOM   16905 C  CE2 . PHE F 6  204  ? -33.871 3.323    37.924  1.00 109.29 ?  204  PHE F CE2 1 
ATOM   16906 C  CZ  . PHE F 6  204  ? -33.297 2.270    37.241  1.00 98.36  ?  204  PHE F CZ  1 
ATOM   16907 N  N   . PHE F 6  205  ? -28.976 5.702    42.227  1.00 89.44  ?  205  PHE F N   1 
ATOM   16908 C  CA  . PHE F 6  205  ? -27.761 6.304    42.765  1.00 86.80  ?  205  PHE F CA  1 
ATOM   16909 C  C   . PHE F 6  205  ? -26.877 5.249    43.415  1.00 84.63  ?  205  PHE F C   1 
ATOM   16910 O  O   . PHE F 6  205  ? -25.654 5.253    43.233  1.00 84.14  ?  205  PHE F O   1 
ATOM   16911 C  CB  . PHE F 6  205  ? -28.117 7.404    43.768  1.00 88.99  ?  205  PHE F CB  1 
ATOM   16912 C  CG  . PHE F 6  205  ? -26.944 7.911    44.565  1.00 88.22  ?  205  PHE F CG  1 
ATOM   16913 C  CD1 . PHE F 6  205  ? -26.120 8.902    44.055  1.00 82.21  ?  205  PHE F CD1 1 
ATOM   16914 C  CD2 . PHE F 6  205  ? -26.678 7.412    45.831  1.00 88.15  ?  205  PHE F CD2 1 
ATOM   16915 C  CE1 . PHE F 6  205  ? -25.046 9.374    44.787  1.00 82.68  ?  205  PHE F CE1 1 
ATOM   16916 C  CE2 . PHE F 6  205  ? -25.605 7.880    46.566  1.00 83.42  ?  205  PHE F CE2 1 
ATOM   16917 C  CZ  . PHE F 6  205  ? -24.788 8.862    46.043  1.00 82.44  ?  205  PHE F CZ  1 
ATOM   16918 N  N   . SER F 6  206  ? -27.481 4.338    44.181  1.00 99.93  ?  206  SER F N   1 
ATOM   16919 C  CA  . SER F 6  206  ? -26.719 3.247    44.776  1.00 98.97  ?  206  SER F CA  1 
ATOM   16920 C  C   . SER F 6  206  ? -26.186 2.294    43.714  1.00 99.37  ?  206  SER F C   1 
ATOM   16921 O  O   . SER F 6  206  ? -25.099 1.729    43.878  1.00 101.45 ?  206  SER F O   1 
ATOM   16922 C  CB  . SER F 6  206  ? -27.588 2.495    45.784  1.00 91.81  ?  206  SER F CB  1 
ATOM   16923 O  OG  . SER F 6  206  ? -26.885 1.409    46.357  1.00 88.62  ?  206  SER F OG  1 
ATOM   16924 N  N   . PHE F 6  207  ? -26.932 2.107    42.622  1.00 85.58  ?  207  PHE F N   1 
ATOM   16925 C  CA  . PHE F 6  207  ? -26.452 1.271    41.526  1.00 82.97  ?  207  PHE F CA  1 
ATOM   16926 C  C   . PHE F 6  207  ? -25.244 1.897    40.840  1.00 88.41  ?  207  PHE F C   1 
ATOM   16927 O  O   . PHE F 6  207  ? -24.295 1.194    40.473  1.00 82.11  ?  207  PHE F O   1 
ATOM   16928 C  CB  . PHE F 6  207  ? -27.572 1.041    40.511  1.00 78.39  ?  207  PHE F CB  1 
ATOM   16929 C  CG  . PHE F 6  207  ? -28.548 -0.031   40.907  1.00 77.45  ?  207  PHE F CG  1 
ATOM   16930 C  CD1 . PHE F 6  207  ? -28.346 -0.792   42.046  1.00 79.29  ?  207  PHE F CD1 1 
ATOM   16931 C  CD2 . PHE F 6  207  ? -29.674 -0.272   40.138  1.00 78.72  ?  207  PHE F CD2 1 
ATOM   16932 C  CE1 . PHE F 6  207  ? -29.246 -1.779   42.406  1.00 75.67  ?  207  PHE F CE1 1 
ATOM   16933 C  CE2 . PHE F 6  207  ? -30.577 -1.255   40.493  1.00 73.16  ?  207  PHE F CE2 1 
ATOM   16934 C  CZ  . PHE F 6  207  ? -30.364 -2.009   41.629  1.00 72.72  ?  207  PHE F CZ  1 
ATOM   16935 N  N   . ASP F 6  208  ? -25.259 3.220    40.666  1.00 110.81 ?  208  ASP F N   1 
ATOM   16936 C  CA  . ASP F 6  208  ? -24.224 3.887    39.886  1.00 104.07 ?  208  ASP F CA  1 
ATOM   16937 C  C   . ASP F 6  208  ? -22.933 4.057    40.675  1.00 104.51 ?  208  ASP F C   1 
ATOM   16938 O  O   . ASP F 6  208  ? -21.842 3.826    40.143  1.00 101.33 ?  208  ASP F O   1 
ATOM   16939 C  CB  . ASP F 6  208  ? -24.730 5.250    39.411  1.00 112.59 ?  208  ASP F CB  1 
ATOM   16940 C  CG  . ASP F 6  208  ? -25.714 5.139    38.265  1.00 123.77 ?  208  ASP F CG  1 
ATOM   16941 O  OD1 . ASP F 6  208  ? -25.778 4.064    37.633  1.00 118.90 ?  208  ASP F OD1 1 
ATOM   16942 O  OD2 . ASP F 6  208  ? -26.424 6.131    37.995  1.00 130.50 -1 208  ASP F OD2 1 
ATOM   16943 N  N   . VAL F 6  209  ? -23.034 4.459    41.941  1.00 100.01 ?  209  VAL F N   1 
ATOM   16944 C  CA  . VAL F 6  209  ? -21.846 4.841    42.697  1.00 98.04  ?  209  VAL F CA  1 
ATOM   16945 C  C   . VAL F 6  209  ? -21.131 3.614    43.249  1.00 95.03  ?  209  VAL F C   1 
ATOM   16946 O  O   . VAL F 6  209  ? -19.911 3.477    43.112  1.00 98.18  ?  209  VAL F O   1 
ATOM   16947 C  CB  . VAL F 6  209  ? -22.224 5.828    43.817  1.00 85.58  ?  209  VAL F CB  1 
ATOM   16948 C  CG1 . VAL F 6  209  ? -21.014 6.139    44.685  1.00 80.53  ?  209  VAL F CG1 1 
ATOM   16949 C  CG2 . VAL F 6  209  ? -22.802 7.103    43.225  1.00 88.73  ?  209  VAL F CG2 1 
ATOM   16950 N  N   . ALA F 6  210  ? -21.873 2.703    43.877  1.00 72.80  ?  210  ALA F N   1 
ATOM   16951 C  CA  . ALA F 6  210  ? -21.273 1.595    44.612  1.00 72.54  ?  210  ALA F CA  1 
ATOM   16952 C  C   . ALA F 6  210  ? -21.332 0.269    43.862  1.00 72.45  ?  210  ALA F C   1 
ATOM   16953 O  O   . ALA F 6  210  ? -20.327 -0.445   43.794  1.00 67.27  ?  210  ALA F O   1 
ATOM   16954 C  CB  . ALA F 6  210  ? -21.951 1.451    45.979  1.00 74.93  ?  210  ALA F CB  1 
ATOM   16955 N  N   . MET F 6  211  ? -22.492 -0.082   43.300  1.00 89.12  ?  211  MET F N   1 
ATOM   16956 C  CA  . MET F 6  211  ? -22.628 -1.384   42.652  1.00 84.36  ?  211  MET F CA  1 
ATOM   16957 C  C   . MET F 6  211  ? -21.816 -1.468   41.366  1.00 88.89  ?  211  MET F C   1 
ATOM   16958 O  O   . MET F 6  211  ? -21.383 -2.559   40.979  1.00 88.18  ?  211  MET F O   1 
ATOM   16959 C  CB  . MET F 6  211  ? -24.100 -1.683   42.368  1.00 86.99  ?  211  MET F CB  1 
ATOM   16960 C  CG  . MET F 6  211  ? -24.368 -3.125   41.961  1.00 87.94  ?  211  MET F CG  1 
ATOM   16961 S  SD  . MET F 6  211  ? -26.111 -3.578   42.029  1.00 99.75  ?  211  MET F SD  1 
ATOM   16962 C  CE  . MET F 6  211  ? -26.595 -3.315   40.324  1.00 78.10  ?  211  MET F CE  1 
ATOM   16963 N  N   . SER F 6  212  ? -21.592 -0.337   40.696  1.00 83.30  ?  212  SER F N   1 
ATOM   16964 C  CA  . SER F 6  212  ? -20.825 -0.329   39.457  1.00 81.57  ?  212  SER F CA  1 
ATOM   16965 C  C   . SER F 6  212  ? -19.331 -0.528   39.678  1.00 88.20  ?  212  SER F C   1 
ATOM   16966 O  O   . SER F 6  212  ? -18.576 -0.516   38.698  1.00 92.71  ?  212  SER F O   1 
ATOM   16967 C  CB  . SER F 6  212  ? -21.062 0.980    38.703  1.00 89.45  ?  212  SER F CB  1 
ATOM   16968 O  OG  . SER F 6  212  ? -20.149 1.979    39.121  1.00 94.84  ?  212  SER F OG  1 
ATOM   16969 N  N   . LEU F 6  213  ? -18.884 -0.699   40.925  1.00 73.41  ?  213  LEU F N   1 
ATOM   16970 C  CA  . LEU F 6  213  ? -17.471 -0.961   41.177  1.00 73.87  ?  213  LEU F CA  1 
ATOM   16971 C  C   . LEU F 6  213  ? -17.052 -2.323   40.639  1.00 75.22  ?  213  LEU F C   1 
ATOM   16972 O  O   . LEU F 6  213  ? -15.904 -2.495   40.213  1.00 78.43  ?  213  LEU F O   1 
ATOM   16973 C  CB  . LEU F 6  213  ? -17.182 -0.866   42.675  1.00 74.19  ?  213  LEU F CB  1 
ATOM   16974 C  CG  . LEU F 6  213  ? -16.901 0.536    43.221  1.00 66.41  ?  213  LEU F CG  1 
ATOM   16975 C  CD1 . LEU F 6  213  ? -16.778 0.507    44.735  1.00 58.14  ?  213  LEU F CD1 1 
ATOM   16976 C  CD2 . LEU F 6  213  ? -15.643 1.113    42.589  1.00 64.80  ?  213  LEU F CD2 1 
ATOM   16977 N  N   . ASP F 6  214  ? -17.963 -3.297   40.651  1.00 142.70 ?  214  ASP F N   1 
ATOM   16978 C  CA  . ASP F 6  214  ? -17.739 -4.622   40.076  1.00 143.81 ?  214  ASP F CA  1 
ATOM   16979 C  C   . ASP F 6  214  ? -18.825 -4.859   39.035  1.00 133.72 ?  214  ASP F C   1 
ATOM   16980 O  O   . ASP F 6  214  ? -19.913 -5.359   39.362  1.00 131.79 ?  214  ASP F O   1 
ATOM   16981 C  CB  . ASP F 6  214  ? -17.753 -5.706   41.152  1.00 139.79 ?  214  ASP F CB  1 
ATOM   16982 C  CG  . ASP F 6  214  ? -17.196 -7.026   40.656  1.00 142.79 ?  214  ASP F CG  1 
ATOM   16983 O  OD1 . ASP F 6  214  ? -16.251 -7.005   39.840  1.00 148.02 ?  214  ASP F OD1 1 
ATOM   16984 O  OD2 . ASP F 6  214  ? -17.704 -8.086   41.081  1.00 142.53 -1 214  ASP F OD2 1 
ATOM   16985 N  N   . PRO F 6  215  ? -18.578 -4.510   37.768  1.00 97.07  ?  215  PRO F N   1 
ATOM   16986 C  CA  . PRO F 6  215  ? -19.611 -4.677   36.733  1.00 98.39  ?  215  PRO F CA  1 
ATOM   16987 C  C   . PRO F 6  215  ? -19.975 -6.124   36.439  1.00 99.06  ?  215  PRO F C   1 
ATOM   16988 O  O   . PRO F 6  215  ? -20.890 -6.360   35.641  1.00 98.92  ?  215  PRO F O   1 
ATOM   16989 C  CB  . PRO F 6  215  ? -18.977 -4.012   35.498  1.00 105.88 ?  215  PRO F CB  1 
ATOM   16990 C  CG  . PRO F 6  215  ? -17.893 -3.129   36.043  1.00 109.94 ?  215  PRO F CG  1 
ATOM   16991 C  CD  . PRO F 6  215  ? -17.373 -3.847   37.246  1.00 101.26 ?  215  PRO F CD  1 
ATOM   16992 N  N   . HIS F 6  216  ? -19.293 -7.096   37.044  1.00 101.05 ?  216  HIS F N   1 
ATOM   16993 C  CA  . HIS F 6  216  ? -19.612 -8.501   36.835  1.00 95.77  ?  216  HIS F CA  1 
ATOM   16994 C  C   . HIS F 6  216  ? -20.740 -8.994   37.732  1.00 91.31  ?  216  HIS F C   1 
ATOM   16995 O  O   . HIS F 6  216  ? -21.237 -10.104  37.518  1.00 98.63  ?  216  HIS F O   1 
ATOM   16996 C  CB  . HIS F 6  216  ? -18.370 -9.363   37.074  1.00 93.19  ?  216  HIS F CB  1 
ATOM   16997 C  CG  . HIS F 6  216  ? -17.192 -8.971   36.238  1.00 90.05  ?  216  HIS F CG  1 
ATOM   16998 N  ND1 . HIS F 6  216  ? -16.062 -8.389   36.772  1.00 93.13  ?  216  HIS F ND1 1 
ATOM   16999 C  CD2 . HIS F 6  216  ? -16.965 -9.083   34.908  1.00 88.66  ?  216  HIS F CD2 1 
ATOM   17000 C  CE1 . HIS F 6  216  ? -15.192 -8.155   35.806  1.00 96.58  ?  216  HIS F CE1 1 
ATOM   17001 N  NE2 . HIS F 6  216  ? -15.714 -8.568   34.666  1.00 91.11  ?  216  HIS F NE2 1 
ATOM   17002 N  N   . TRP F 6  217  ? -21.153 -8.204   38.720  1.00 72.83  ?  217  TRP F N   1 
ATOM   17003 C  CA  . TRP F 6  217  ? -22.119 -8.634   39.718  1.00 73.39  ?  217  TRP F CA  1 
ATOM   17004 C  C   . TRP F 6  217  ? -23.224 -7.596   39.849  1.00 72.64  ?  217  TRP F C   1 
ATOM   17005 O  O   . TRP F 6  217  ? -22.987 -6.393   39.708  1.00 75.33  ?  217  TRP F O   1 
ATOM   17006 C  CB  . TRP F 6  217  ? -21.436 -8.860   41.076  1.00 74.13  ?  217  TRP F CB  1 
ATOM   17007 C  CG  . TRP F 6  217  ? -22.365 -9.255   42.183  1.00 71.87  ?  217  TRP F CG  1 
ATOM   17008 C  CD1 . TRP F 6  217  ? -22.822 -10.511  42.460  1.00 69.04  ?  217  TRP F CD1 1 
ATOM   17009 C  CD2 . TRP F 6  217  ? -22.938 -8.392   43.172  1.00 75.82  ?  217  TRP F CD2 1 
ATOM   17010 N  NE1 . TRP F 6  217  ? -23.650 -10.482  43.557  1.00 71.28  ?  217  TRP F NE1 1 
ATOM   17011 C  CE2 . TRP F 6  217  ? -23.737 -9.193   44.013  1.00 75.14  ?  217  TRP F CE2 1 
ATOM   17012 C  CE3 . TRP F 6  217  ? -22.857 -7.019   43.427  1.00 72.62  ?  217  TRP F CE3 1 
ATOM   17013 C  CZ2 . TRP F 6  217  ? -24.449 -8.668   45.089  1.00 70.66  ?  217  TRP F CZ2 1 
ATOM   17014 C  CZ3 . TRP F 6  217  ? -23.564 -6.500   44.496  1.00 79.91  ?  217  TRP F CZ3 1 
ATOM   17015 C  CH2 . TRP F 6  217  ? -24.350 -7.323   45.314  1.00 79.31  ?  217  TRP F CH2 1 
ATOM   17016 N  N   . PHE F 6  218  ? -24.437 -8.074   40.116  1.00 86.03  ?  218  PHE F N   1 
ATOM   17017 C  CA  . PHE F 6  218  ? -25.581 -7.200   40.324  1.00 87.33  ?  218  PHE F CA  1 
ATOM   17018 C  C   . PHE F 6  218  ? -26.545 -7.876   41.286  1.00 83.98  ?  218  PHE F C   1 
ATOM   17019 O  O   . PHE F 6  218  ? -26.614 -9.106   41.354  1.00 81.99  ?  218  PHE F O   1 
ATOM   17020 C  CB  . PHE F 6  218  ? -26.289 -6.866   39.003  1.00 84.84  ?  218  PHE F CB  1 
ATOM   17021 C  CG  . PHE F 6  218  ? -26.989 -8.038   38.374  1.00 83.77  ?  218  PHE F CG  1 
ATOM   17022 C  CD1 . PHE F 6  218  ? -26.287 -8.952   37.606  1.00 89.88  ?  218  PHE F CD1 1 
ATOM   17023 C  CD2 . PHE F 6  218  ? -28.354 -8.216   38.538  1.00 80.16  ?  218  PHE F CD2 1 
ATOM   17024 C  CE1 . PHE F 6  218  ? -26.930 -10.030  37.026  1.00 92.51  ?  218  PHE F CE1 1 
ATOM   17025 C  CE2 . PHE F 6  218  ? -29.002 -9.289   37.959  1.00 83.26  ?  218  PHE F CE2 1 
ATOM   17026 C  CZ  . PHE F 6  218  ? -28.290 -10.197  37.202  1.00 92.43  ?  218  PHE F CZ  1 
ATOM   17027 N  N   . SER F 6  219  ? -27.286 -7.060   42.033  1.00 72.18  ?  219  SER F N   1 
ATOM   17028 C  CA  . SER F 6  219  ? -28.293 -7.557   42.961  1.00 74.22  ?  219  SER F CA  1 
ATOM   17029 C  C   . SER F 6  219  ? -29.503 -6.639   42.910  1.00 67.38  ?  219  SER F C   1 
ATOM   17030 O  O   . SER F 6  219  ? -29.362 -5.417   43.010  1.00 70.55  ?  219  SER F O   1 
ATOM   17031 C  CB  . SER F 6  219  ? -27.746 -7.639   44.390  1.00 75.08  ?  219  SER F CB  1 
ATOM   17032 O  OG  . SER F 6  219  ? -28.750 -8.048   45.302  1.00 79.28  ?  219  SER F OG  1 
ATOM   17033 N  N   . THR F 6  220  ? -30.688 -7.232   42.757  1.00 72.87  ?  220  THR F N   1 
ATOM   17034 C  CA  . THR F 6  220  ? -31.902 -6.431   42.648  1.00 75.13  ?  220  THR F CA  1 
ATOM   17035 C  C   . THR F 6  220  ? -32.306 -5.846   43.996  1.00 81.71  ?  220  THR F C   1 
ATOM   17036 O  O   . THR F 6  220  ? -32.794 -4.712   44.064  1.00 87.74  ?  220  THR F O   1 
ATOM   17037 C  CB  . THR F 6  220  ? -33.034 -7.275   42.067  1.00 82.40  ?  220  THR F CB  1 
ATOM   17038 O  OG1 . THR F 6  220  ? -32.939 -8.613   42.571  1.00 85.52  ?  220  THR F OG1 1 
ATOM   17039 C  CG2 . THR F 6  220  ? -32.952 -7.304   40.550  1.00 88.57  ?  220  THR F CG2 1 
ATOM   17040 N  N   . ILE F 6  221  ? -32.108 -6.601   45.081  1.00 81.12  ?  221  ILE F N   1 
ATOM   17041 C  CA  . ILE F 6  221  ? -32.431 -6.088   46.407  1.00 81.14  ?  221  ILE F CA  1 
ATOM   17042 C  C   . ILE F 6  221  ? -31.507 -4.945   46.803  1.00 79.99  ?  221  ILE F C   1 
ATOM   17043 O  O   . ILE F 6  221  ? -31.845 -4.160   47.697  1.00 84.37  ?  221  ILE F O   1 
ATOM   17044 C  CB  . ILE F 6  221  ? -32.375 -7.215   47.457  1.00 72.09  ?  221  ILE F CB  1 
ATOM   17045 C  CG1 . ILE F 6  221  ? -33.403 -6.968   48.562  1.00 71.30  ?  221  ILE F CG1 1 
ATOM   17046 C  CG2 . ILE F 6  221  ? -30.983 -7.325   48.063  1.00 66.50  ?  221  ILE F CG2 1 
ATOM   17047 C  CD1 . ILE F 6  221  ? -33.435 -8.053   49.617  1.00 70.85  ?  221  ILE F CD1 1 
ATOM   17048 N  N   . TYR F 6  222  ? -30.350 -4.828   46.157  1.00 97.78  ?  222  TYR F N   1 
ATOM   17049 C  CA  . TYR F 6  222  ? -29.400 -3.785   46.507  1.00 102.36 ?  222  TYR F CA  1 
ATOM   17050 C  C   . TYR F 6  222  ? -29.974 -2.421   46.148  1.00 112.62 ?  222  TYR F C   1 
ATOM   17051 O  O   . TYR F 6  222  ? -30.689 -2.274   45.154  1.00 117.45 ?  222  TYR F O   1 
ATOM   17052 C  CB  . TYR F 6  222  ? -28.073 -4.024   45.790  1.00 105.87 ?  222  TYR F CB  1 
ATOM   17053 C  CG  . TYR F 6  222  ? -26.950 -3.122   46.239  1.00 112.32 ?  222  TYR F CG  1 
ATOM   17054 C  CD1 . TYR F 6  222  ? -26.329 -3.322   47.464  1.00 116.34 ?  222  TYR F CD1 1 
ATOM   17055 C  CD2 . TYR F 6  222  ? -26.493 -2.090   45.431  1.00 115.88 ?  222  TYR F CD2 1 
ATOM   17056 C  CE1 . TYR F 6  222  ? -25.298 -2.508   47.881  1.00 119.15 ?  222  TYR F CE1 1 
ATOM   17057 C  CE2 . TYR F 6  222  ? -25.458 -1.270   45.838  1.00 125.40 ?  222  TYR F CE2 1 
ATOM   17058 C  CZ  . TYR F 6  222  ? -24.865 -1.484   47.065  1.00 125.88 ?  222  TYR F CZ  1 
ATOM   17059 O  OH  . TYR F 6  222  ? -23.835 -0.673   47.480  1.00 125.36 ?  222  TYR F OH  1 
ATOM   17060 N  N   . GLY F 6  223  ? -29.667 -1.423   46.970  1.00 106.62 ?  223  GLY F N   1 
ATOM   17061 C  CA  . GLY F 6  223  ? -30.300 -0.126   46.838  1.00 109.17 ?  223  GLY F CA  1 
ATOM   17062 C  C   . GLY F 6  223  ? -31.392 0.043    47.873  1.00 109.46 ?  223  GLY F C   1 
ATOM   17063 O  O   . GLY F 6  223  ? -31.402 1.022    48.625  1.00 110.60 ?  223  GLY F O   1 
ATOM   17064 N  N   . ALA F 6  224  ? -32.324 -0.912   47.916  1.00 92.93  ?  224  ALA F N   1 
ATOM   17065 C  CA  . ALA F 6  224  ? -33.272 -0.960   49.023  1.00 86.18  ?  224  ALA F CA  1 
ATOM   17066 C  C   . ALA F 6  224  ? -32.555 -1.256   50.332  1.00 90.40  ?  224  ALA F C   1 
ATOM   17067 O  O   . ALA F 6  224  ? -32.920 -0.720   51.385  1.00 96.73  ?  224  ALA F O   1 
ATOM   17068 C  CB  . ALA F 6  224  ? -34.353 -2.006   48.750  1.00 78.17  ?  224  ALA F CB  1 
ATOM   17069 N  N   . HIS F 6  225  ? -31.531 -2.112   50.282  1.00 83.34  ?  225  HIS F N   1 
ATOM   17070 C  CA  . HIS F 6  225  ? -30.649 -2.292   51.429  1.00 82.12  ?  225  HIS F CA  1 
ATOM   17071 C  C   . HIS F 6  225  ? -29.975 -0.980   51.811  1.00 90.68  ?  225  HIS F C   1 
ATOM   17072 O  O   . HIS F 6  225  ? -29.760 -0.704   52.997  1.00 89.83  ?  225  HIS F O   1 
ATOM   17073 C  CB  . HIS F 6  225  ? -29.603 -3.362   51.112  1.00 77.78  ?  225  HIS F CB  1 
ATOM   17074 C  CG  . HIS F 6  225  ? -28.691 -3.680   52.254  1.00 85.56  ?  225  HIS F CG  1 
ATOM   17075 N  ND1 . HIS F 6  225  ? -27.407 -3.186   52.339  1.00 89.28  ?  225  HIS F ND1 1 
ATOM   17076 C  CD2 . HIS F 6  225  ? -28.871 -4.451   53.353  1.00 86.62  ?  225  HIS F CD2 1 
ATOM   17077 C  CE1 . HIS F 6  225  ? -26.837 -3.633   53.444  1.00 87.43  ?  225  HIS F CE1 1 
ATOM   17078 N  NE2 . HIS F 6  225  ? -27.704 -4.404   54.076  1.00 91.30  ?  225  HIS F NE2 1 
ATOM   17079 N  N   . TYR F 6  226  ? -29.640 -0.155   50.816  1.00 91.82  ?  226  TYR F N   1 
ATOM   17080 C  CA  . TYR F 6  226  ? -29.020 1.136    51.097  1.00 88.76  ?  226  TYR F CA  1 
ATOM   17081 C  C   . TYR F 6  226  ? -30.006 2.095    51.753  1.00 88.22  ?  226  TYR F C   1 
ATOM   17082 O  O   . TYR F 6  226  ? -29.622 2.890    52.618  1.00 88.94  ?  226  TYR F O   1 
ATOM   17083 C  CB  . TYR F 6  226  ? -28.462 1.739    49.808  1.00 84.37  ?  226  TYR F CB  1 
ATOM   17084 C  CG  . TYR F 6  226  ? -27.748 3.055    50.007  1.00 83.46  ?  226  TYR F CG  1 
ATOM   17085 C  CD1 . TYR F 6  226  ? -26.745 3.188    50.958  1.00 82.27  ?  226  TYR F CD1 1 
ATOM   17086 C  CD2 . TYR F 6  226  ? -28.081 4.167    49.246  1.00 90.27  ?  226  TYR F CD2 1 
ATOM   17087 C  CE1 . TYR F 6  226  ? -26.089 4.392    51.141  1.00 85.02  ?  226  TYR F CE1 1 
ATOM   17088 C  CE2 . TYR F 6  226  ? -27.433 5.374    49.422  1.00 85.83  ?  226  TYR F CE2 1 
ATOM   17089 C  CZ  . TYR F 6  226  ? -26.438 5.481    50.370  1.00 82.45  ?  226  TYR F CZ  1 
ATOM   17090 O  OH  . TYR F 6  226  ? -25.792 6.683    50.547  1.00 87.39  ?  226  TYR F OH  1 
ATOM   17091 N  N   . MET F 6  227  ? -31.279 2.043    51.353  1.00 112.95 ?  227  MET F N   1 
ATOM   17092 C  CA  . MET F 6  227  ? -32.271 2.924    51.961  1.00 110.70 ?  227  MET F CA  1 
ATOM   17093 C  C   . MET F 6  227  ? -32.524 2.549    53.416  1.00 113.64 ?  227  MET F C   1 
ATOM   17094 O  O   . MET F 6  227  ? -32.621 3.428    54.280  1.00 121.48 ?  227  MET F O   1 
ATOM   17095 C  CB  . MET F 6  227  ? -33.575 2.893    51.165  1.00 112.44 ?  227  MET F CB  1 
ATOM   17096 C  CG  . MET F 6  227  ? -33.484 3.554    49.804  1.00 111.73 ?  227  MET F CG  1 
ATOM   17097 S  SD  . MET F 6  227  ? -35.085 3.687    48.984  1.00 125.78 ?  227  MET F SD  1 
ATOM   17098 C  CE  . MET F 6  227  ? -35.356 1.991    48.473  1.00 122.16 ?  227  MET F CE  1 
ATOM   17099 N  N   . ALA F 6  228  ? -32.637 1.250    53.707  1.00 69.27  ?  228  ALA F N   1 
ATOM   17100 C  CA  . ALA F 6  228  ? -32.795 0.822    55.093  1.00 72.97  ?  228  ALA F CA  1 
ATOM   17101 C  C   . ALA F 6  228  ? -31.544 1.129    55.906  1.00 77.83  ?  228  ALA F C   1 
ATOM   17102 O  O   . ALA F 6  228  ? -31.635 1.468    57.092  1.00 80.45  ?  228  ALA F O   1 
ATOM   17103 C  CB  . ALA F 6  228  ? -33.126 -0.669   55.152  1.00 71.31  ?  228  ALA F CB  1 
ATOM   17104 N  N   . ASN F 6  229  ? -30.368 1.020    55.285  1.00 102.28 ?  229  ASN F N   1 
ATOM   17105 C  CA  . ASN F 6  229  ? -29.131 1.366    55.976  1.00 104.24 ?  229  ASN F CA  1 
ATOM   17106 C  C   . ASN F 6  229  ? -29.068 2.858    56.275  1.00 105.67 ?  229  ASN F C   1 
ATOM   17107 O  O   . ASN F 6  229  ? -28.702 3.260    57.385  1.00 107.53 ?  229  ASN F O   1 
ATOM   17108 C  CB  . ASN F 6  229  ? -27.927 0.932    55.140  1.00 108.06 ?  229  ASN F CB  1 
ATOM   17109 C  CG  . ASN F 6  229  ? -26.650 0.843    55.953  1.00 110.52 ?  229  ASN F CG  1 
ATOM   17110 O  OD1 . ASN F 6  229  ? -26.571 1.358    57.067  1.00 114.65 ?  229  ASN F OD1 1 
ATOM   17111 N  ND2 . ASN F 6  229  ? -25.642 0.180    55.399  1.00 115.23 ?  229  ASN F ND2 1 
ATOM   17112 N  N   . ALA F 6  230  ? -29.423 3.694    55.296  1.00 98.78  ?  230  ALA F N   1 
ATOM   17113 C  CA  . ALA F 6  230  ? -29.431 5.134    55.526  1.00 100.80 ?  230  ALA F CA  1 
ATOM   17114 C  C   . ALA F 6  230  ? -30.512 5.535    56.520  1.00 101.40 ?  230  ALA F C   1 
ATOM   17115 O  O   . ALA F 6  230  ? -30.335 6.504    57.267  1.00 108.00 ?  230  ALA F O   1 
ATOM   17116 C  CB  . ALA F 6  230  ? -29.621 5.878    54.205  1.00 91.89  ?  230  ALA F CB  1 
ATOM   17117 N  N   . GLY F 6  231  ? -31.630 4.808    56.546  1.00 93.45  ?  231  GLY F N   1 
ATOM   17118 C  CA  . GLY F 6  231  ? -32.674 5.111    57.510  1.00 99.81  ?  231  GLY F CA  1 
ATOM   17119 C  C   . GLY F 6  231  ? -32.259 4.806    58.936  1.00 102.65 ?  231  GLY F C   1 
ATOM   17120 O  O   . GLY F 6  231  ? -32.589 5.553    59.861  1.00 101.84 ?  231  GLY F O   1 
ATOM   17121 N  N   . LEU F 6  232  ? -31.533 3.704    59.135  1.00 104.48 ?  232  LEU F N   1 
ATOM   17122 C  CA  . LEU F 6  232  ? -31.037 3.377    60.468  1.00 102.38 ?  232  LEU F CA  1 
ATOM   17123 C  C   . LEU F 6  232  ? -29.972 4.370    60.919  1.00 101.36 ?  232  LEU F C   1 
ATOM   17124 O  O   . LEU F 6  232  ? -29.900 4.718    62.104  1.00 107.63 ?  232  LEU F O   1 
ATOM   17125 C  CB  . LEU F 6  232  ? -30.482 1.953    60.484  1.00 103.36 ?  232  LEU F CB  1 
ATOM   17126 C  CG  . LEU F 6  232  ? -30.003 1.396    61.828  1.00 102.98 ?  232  LEU F CG  1 
ATOM   17127 C  CD1 . LEU F 6  232  ? -30.966 1.760    62.953  1.00 99.41  ?  232  LEU F CD1 1 
ATOM   17128 C  CD2 . LEU F 6  232  ? -29.805 -0.110   61.748  1.00 99.50  ?  232  LEU F CD2 1 
ATOM   17129 N  N   . MET F 6  233  ? -29.136 4.836    59.988  1.00 79.01  ?  233  MET F N   1 
ATOM   17130 C  CA  . MET F 6  233  ? -28.085 5.786    60.340  1.00 81.60  ?  233  MET F CA  1 
ATOM   17131 C  C   . MET F 6  233  ? -28.672 7.133    60.744  1.00 88.54  ?  233  MET F C   1 
ATOM   17132 O  O   . MET F 6  233  ? -28.268 7.718    61.756  1.00 89.46  ?  233  MET F O   1 
ATOM   17133 C  CB  . MET F 6  233  ? -27.114 5.954    59.172  1.00 92.74  ?  233  MET F CB  1 
ATOM   17134 C  CG  . MET F 6  233  ? -26.115 7.083    59.369  1.00 94.70  ?  233  MET F CG  1 
ATOM   17135 S  SD  . MET F 6  233  ? -24.615 6.554    60.214  1.00 96.07  ?  233  MET F SD  1 
ATOM   17136 C  CE  . MET F 6  233  ? -23.773 5.698    58.884  1.00 93.96  ?  233  MET F CE  1 
ATOM   17137 N  N   . THR F 6  234  ? -29.628 7.645    59.965  1.00 87.30  ?  234  THR F N   1 
ATOM   17138 C  CA  . THR F 6  234  ? -30.238 8.930    60.292  1.00 86.62  ?  234  THR F CA  1 
ATOM   17139 C  C   . THR F 6  234  ? -31.152 8.859    61.509  1.00 87.40  ?  234  THR F C   1 
ATOM   17140 O  O   . THR F 6  234  ? -31.375 9.887    62.155  1.00 92.67  ?  234  THR F O   1 
ATOM   17141 C  CB  . THR F 6  234  ? -31.018 9.472    59.092  1.00 84.39  ?  234  THR F CB  1 
ATOM   17142 O  OG1 . THR F 6  234  ? -31.402 10.829   59.349  1.00 84.62  ?  234  THR F OG1 1 
ATOM   17143 C  CG2 . THR F 6  234  ? -32.259 8.634    58.822  1.00 88.94  ?  234  THR F CG2 1 
ATOM   17144 N  N   . LEU F 6  235  ? -31.683 7.679    61.837  1.00 88.75  ?  235  LEU F N   1 
ATOM   17145 C  CA  . LEU F 6  235  ? -32.478 7.551    63.055  1.00 83.15  ?  235  LEU F CA  1 
ATOM   17146 C  C   . LEU F 6  235  ? -31.595 7.590    64.295  1.00 88.59  ?  235  LEU F C   1 
ATOM   17147 O  O   . LEU F 6  235  ? -31.936 8.246    65.286  1.00 99.17  ?  235  LEU F O   1 
ATOM   17148 C  CB  . LEU F 6  235  ? -33.299 6.262    63.027  1.00 80.50  ?  235  LEU F CB  1 
ATOM   17149 C  CG  . LEU F 6  235  ? -34.682 6.337    62.378  1.00 80.28  ?  235  LEU F CG  1 
ATOM   17150 C  CD1 . LEU F 6  235  ? -35.412 5.010    62.510  1.00 72.12  ?  235  LEU F CD1 1 
ATOM   17151 C  CD2 . LEU F 6  235  ? -35.494 7.463    62.996  1.00 77.54  ?  235  LEU F CD2 1 
ATOM   17152 N  N   . ALA F 6  236  ? -30.462 6.884    64.264  1.00 81.35  ?  236  ALA F N   1 
ATOM   17153 C  CA  . ALA F 6  236  ? -29.509 6.962    65.365  1.00 80.64  ?  236  ALA F CA  1 
ATOM   17154 C  C   . ALA F 6  236  ? -28.887 8.348    65.468  1.00 87.71  ?  236  ALA F C   1 
ATOM   17155 O  O   . ALA F 6  236  ? -28.593 8.816    66.574  1.00 91.02  ?  236  ALA F O   1 
ATOM   17156 C  CB  . ALA F 6  236  ? -28.425 5.900    65.189  1.00 82.08  ?  236  ALA F CB  1 
ATOM   17157 N  N   . PHE F 6  237  ? -28.680 9.016    64.332  1.00 104.80 ?  237  PHE F N   1 
ATOM   17158 C  CA  . PHE F 6  237  ? -28.186 10.388   64.359  1.00 112.81 ?  237  PHE F CA  1 
ATOM   17159 C  C   . PHE F 6  237  ? -29.211 11.329   64.979  1.00 115.43 ?  237  PHE F C   1 
ATOM   17160 O  O   . PHE F 6  237  ? -28.848 12.243   65.728  1.00 117.67 ?  237  PHE F O   1 
ATOM   17161 C  CB  . PHE F 6  237  ? -27.820 10.837   62.944  1.00 120.83 ?  237  PHE F CB  1 
ATOM   17162 C  CG  . PHE F 6  237  ? -27.719 12.327   62.783  1.00 115.03 ?  237  PHE F CG  1 
ATOM   17163 C  CD1 . PHE F 6  237  ? -26.644 13.026   63.305  1.00 114.09 ?  237  PHE F CD1 1 
ATOM   17164 C  CD2 . PHE F 6  237  ? -28.699 13.028   62.097  1.00 115.69 ?  237  PHE F CD2 1 
ATOM   17165 C  CE1 . PHE F 6  237  ? -26.555 14.395   63.154  1.00 123.61 ?  237  PHE F CE1 1 
ATOM   17166 C  CE2 . PHE F 6  237  ? -28.612 14.396   61.944  1.00 120.86 ?  237  PHE F CE2 1 
ATOM   17167 C  CZ  . PHE F 6  237  ? -27.539 15.080   62.472  1.00 125.01 ?  237  PHE F CZ  1 
ATOM   17168 N  N   . LEU F 6  238  ? -30.495 11.121   64.677  1.00 100.94 ?  238  LEU F N   1 
ATOM   17169 C  CA  . LEU F 6  238  ? -31.539 11.954   65.267  1.00 98.26  ?  238  LEU F CA  1 
ATOM   17170 C  C   . LEU F 6  238  ? -31.650 11.721   66.768  1.00 96.36  ?  238  LEU F C   1 
ATOM   17171 O  O   . LEU F 6  238  ? -31.901 12.661   67.531  1.00 106.57 ?  238  LEU F O   1 
ATOM   17172 C  CB  . LEU F 6  238  ? -32.879 11.684   64.585  1.00 91.32  ?  238  LEU F CB  1 
ATOM   17173 C  CG  . LEU F 6  238  ? -33.121 12.369   63.240  1.00 93.96  ?  238  LEU F CG  1 
ATOM   17174 C  CD1 . LEU F 6  238  ? -34.374 11.814   62.582  1.00 99.56  ?  238  LEU F CD1 1 
ATOM   17175 C  CD2 . LEU F 6  238  ? -33.226 13.875   63.416  1.00 93.55  ?  238  LEU F CD2 1 
ATOM   17176 N  N   . ALA F 6  239  ? -31.475 10.474   67.210  1.00 75.49  ?  239  ALA F N   1 
ATOM   17177 C  CA  . ALA F 6  239  ? -31.529 10.187   68.639  1.00 83.83  ?  239  ALA F CA  1 
ATOM   17178 C  C   . ALA F 6  239  ? -30.356 10.823   69.374  1.00 88.18  ?  239  ALA F C   1 
ATOM   17179 O  O   . ALA F 6  239  ? -30.510 11.306   70.502  1.00 81.90  ?  239  ALA F O   1 
ATOM   17180 C  CB  . ALA F 6  239  ? -31.558 8.677    68.871  1.00 81.30  ?  239  ALA F CB  1 
ATOM   17181 N  N   . LEU F 6  240  ? -29.175 10.833   68.750  1.00 108.63 ?  240  LEU F N   1 
ATOM   17182 C  CA  . LEU F 6  240  ? -28.018 11.476   69.364  1.00 103.40 ?  240  LEU F CA  1 
ATOM   17183 C  C   . LEU F 6  240  ? -28.225 12.981   69.477  1.00 108.35 ?  240  LEU F C   1 
ATOM   17184 O  O   . LEU F 6  240  ? -27.974 13.578   70.531  1.00 114.39 ?  240  LEU F O   1 
ATOM   17185 C  CB  . LEU F 6  240  ? -26.756 11.168   68.558  1.00 104.67 ?  240  LEU F CB  1 
ATOM   17186 C  CG  . LEU F 6  240  ? -26.099 9.805    68.779  1.00 100.67 ?  240  LEU F CG  1 
ATOM   17187 C  CD1 . LEU F 6  240  ? -25.433 9.318    67.501  1.00 96.62  ?  240  LEU F CD1 1 
ATOM   17188 C  CD2 . LEU F 6  240  ? -25.094 9.877    69.917  1.00 85.82  ?  240  LEU F CD2 1 
ATOM   17189 N  N   . MET F 6  241  ? -28.688 13.612   68.397  1.00 114.46 ?  241  MET F N   1 
ATOM   17190 C  CA  . MET F 6  241  ? -28.874 15.058   68.414  1.00 118.13 ?  241  MET F CA  1 
ATOM   17191 C  C   . MET F 6  241  ? -30.050 15.467   69.290  1.00 123.25 ?  241  MET F C   1 
ATOM   17192 O  O   . MET F 6  241  ? -30.074 16.590   69.805  1.00 133.05 ?  241  MET F O   1 
ATOM   17193 C  CB  . MET F 6  241  ? -29.059 15.580   66.991  1.00 113.44 ?  241  MET F CB  1 
ATOM   17194 C  CG  . MET F 6  241  ? -27.794 15.538   66.158  1.00 112.30 ?  241  MET F CG  1 
ATOM   17195 S  SD  . MET F 6  241  ? -26.413 16.379   66.955  1.00 129.85 ?  241  MET F SD  1 
ATOM   17196 C  CE  . MET F 6  241  ? -25.162 15.097   66.916  1.00 127.40 ?  241  MET F CE  1 
ATOM   17197 N  N   . MET F 6  242  ? -31.031 14.580   69.472  1.00 115.45 ?  242  MET F N   1 
ATOM   17198 C  CA  . MET F 6  242  ? -32.109 14.873   70.410  1.00 113.71 ?  242  MET F CA  1 
ATOM   17199 C  C   . MET F 6  242  ? -31.601 14.857   71.844  1.00 109.45 ?  242  MET F C   1 
ATOM   17200 O  O   . MET F 6  242  ? -32.016 15.684   72.665  1.00 113.34 ?  242  MET F O   1 
ATOM   17201 C  CB  . MET F 6  242  ? -33.250 13.872   70.240  1.00 113.68 ?  242  MET F CB  1 
ATOM   17202 C  CG  . MET F 6  242  ? -34.580 14.366   70.782  1.00 116.49 ?  242  MET F CG  1 
ATOM   17203 S  SD  . MET F 6  242  ? -35.979 13.683   69.879  1.00 133.49 ?  242  MET F SD  1 
ATOM   17204 C  CE  . MET F 6  242  ? -35.536 11.949   69.871  1.00 119.11 ?  242  MET F CE  1 
ATOM   17205 N  N   . SER F 6  243  ? -30.705 13.920   72.164  1.00 110.25 ?  243  SER F N   1 
ATOM   17206 C  CA  . SER F 6  243  ? -30.108 13.886   73.493  1.00 111.81 ?  243  SER F CA  1 
ATOM   17207 C  C   . SER F 6  243  ? -29.194 15.081   73.727  1.00 119.17 ?  243  SER F C   1 
ATOM   17208 O  O   . SER F 6  243  ? -28.970 15.473   74.878  1.00 124.11 ?  243  SER F O   1 
ATOM   17209 C  CB  . SER F 6  243  ? -29.333 12.582   73.686  1.00 112.23 ?  243  SER F CB  1 
ATOM   17210 O  OG  . SER F 6  243  ? -28.584 12.602   74.889  1.00 115.70 ?  243  SER F OG  1 
ATOM   17211 N  N   . ARG F 6  244  ? -28.665 15.673   72.656  1.00 119.79 ?  244  ARG F N   1 
ATOM   17212 C  CA  . ARG F 6  244  ? -27.781 16.824   72.793  1.00 122.56 ?  244  ARG F CA  1 
ATOM   17213 C  C   . ARG F 6  244  ? -28.558 18.098   73.102  1.00 128.36 ?  244  ARG F C   1 
ATOM   17214 O  O   . ARG F 6  244  ? -28.112 18.920   73.909  1.00 138.48 ?  244  ARG F O   1 
ATOM   17215 C  CB  . ARG F 6  244  ? -26.960 17.003   71.516  1.00 130.08 ?  244  ARG F CB  1 
ATOM   17216 C  CG  . ARG F 6  244  ? -25.630 16.273   71.514  1.00 136.43 ?  244  ARG F CG  1 
ATOM   17217 C  CD  . ARG F 6  244  ? -24.776 16.696   72.693  1.00 139.04 ?  244  ARG F CD  1 
ATOM   17218 N  NE  . ARG F 6  244  ? -23.355 16.511   72.425  1.00 150.84 ?  244  ARG F NE  1 
ATOM   17219 C  CZ  . ARG F 6  244  ? -22.398 16.648   73.331  1.00 161.39 ?  244  ARG F CZ  1 
ATOM   17220 N  NH1 . ARG F 6  244  ? -22.673 16.970   74.585  1.00 167.22 ?  244  ARG F NH1 1 
ATOM   17221 N  NH2 . ARG F 6  244  ? -21.131 16.460   72.971  1.00 158.93 ?  244  ARG F NH2 1 
ATOM   17222 N  N   . VAL F 6  245  ? -29.720 18.275   72.475  1.00 103.58 ?  245  VAL F N   1 
ATOM   17223 C  CA  . VAL F 6  245  ? -30.462 19.528   72.556  1.00 108.09 ?  245  VAL F CA  1 
ATOM   17224 C  C   . VAL F 6  245  ? -31.757 19.306   73.337  1.00 105.05 ?  245  VAL F C   1 
ATOM   17225 O  O   . VAL F 6  245  ? -32.772 19.971   73.100  1.00 105.83 ?  245  VAL F O   1 
ATOM   17226 C  CB  . VAL F 6  245  ? -30.705 20.092   71.138  1.00 106.71 ?  245  VAL F CB  1 
ATOM   17227 C  CG1 . VAL F 6  245  ? -31.769 19.290   70.378  1.00 101.28 ?  245  VAL F CG1 1 
ATOM   17228 C  CG2 . VAL F 6  245  ? -31.028 21.585   71.179  1.00 111.12 ?  245  VAL F CG2 1 
ATOM   17229 N  N   . ARG F 6  246  ? -31.715 18.394   74.311  1.00 130.33 ?  246  ARG F N   1 
ATOM   17230 C  CA  . ARG F 6  246  ? -32.906 18.055   75.083  1.00 136.79 ?  246  ARG F CA  1 
ATOM   17231 C  C   . ARG F 6  246  ? -33.393 19.189   75.976  1.00 144.84 ?  246  ARG F C   1 
ATOM   17232 O  O   . ARG F 6  246  ? -34.486 19.075   76.542  1.00 143.35 ?  246  ARG F O   1 
ATOM   17233 C  CB  . ARG F 6  246  ? -32.644 16.820   75.947  1.00 129.49 ?  246  ARG F CB  1 
ATOM   17234 C  CG  . ARG F 6  246  ? -31.648 17.051   77.071  1.00 124.22 ?  246  ARG F CG  1 
ATOM   17235 C  CD  . ARG F 6  246  ? -31.592 15.856   78.009  1.00 118.06 ?  246  ARG F CD  1 
ATOM   17236 N  NE  . ARG F 6  246  ? -30.878 14.727   77.427  1.00 118.60 ?  246  ARG F NE  1 
ATOM   17237 C  CZ  . ARG F 6  246  ? -30.655 13.580   78.055  1.00 120.23 ?  246  ARG F CZ  1 
ATOM   17238 N  NH1 . ARG F 6  246  ? -31.082 13.375   79.290  1.00 117.41 ?  246  ARG F NH1 1 
ATOM   17239 N  NH2 . ARG F 6  246  ? -29.989 12.615   77.427  1.00 120.83 ?  246  ARG F NH2 1 
ATOM   17240 N  N   . ASP F 6  247  ? -32.625 20.269   76.123  1.00 177.28 ?  247  ASP F N   1 
ATOM   17241 C  CA  . ASP F 6  247  ? -32.974 21.367   77.022  1.00 176.60 ?  247  ASP F CA  1 
ATOM   17242 C  C   . ASP F 6  247  ? -32.811 22.705   76.297  1.00 181.57 ?  247  ASP F C   1 
ATOM   17243 O  O   . ASP F 6  247  ? -32.062 23.585   76.718  1.00 184.17 ?  247  ASP F O   1 
ATOM   17244 C  CB  . ASP F 6  247  ? -32.121 21.320   78.288  1.00 176.12 ?  247  ASP F CB  1 
ATOM   17245 C  CG  . ASP F 6  247  ? -30.642 21.173   77.987  1.00 186.07 ?  247  ASP F CG  1 
ATOM   17246 O  OD1 . ASP F 6  247  ? -30.286 21.019   76.799  1.00 184.16 ?  247  ASP F OD1 1 
ATOM   17247 O  OD2 . ASP F 6  247  ? -29.833 21.216   78.938  1.00 185.26 -1 247  ASP F OD2 1 
ATOM   17248 N  N   . ALA F 6  248  ? -33.536 22.861   75.191  1.00 162.12 ?  248  ALA F N   1 
ATOM   17249 C  CA  . ALA F 6  248  ? -33.467 24.066   74.376  1.00 167.31 ?  248  ALA F CA  1 
ATOM   17250 C  C   . ALA F 6  248  ? -34.633 25.014   74.622  1.00 174.25 ?  248  ALA F C   1 
ATOM   17251 O  O   . ALA F 6  248  ? -34.867 25.911   73.805  1.00 169.94 ?  248  ALA F O   1 
ATOM   17252 C  CB  . ALA F 6  248  ? -33.405 23.696   72.894  1.00 163.27 ?  248  ALA F CB  1 
ATOM   17253 N  N   . ALA F 6  249  ? -35.371 24.831   75.717  1.00 163.28 ?  249  ALA F N   1 
ATOM   17254 C  CA  . ALA F 6  249  ? -36.553 25.601   76.100  1.00 159.31 ?  249  ALA F CA  1 
ATOM   17255 C  C   . ALA F 6  249  ? -37.712 25.431   75.124  1.00 159.19 ?  249  ALA F C   1 
ATOM   17256 O  O   . ALA F 6  249  ? -38.804 25.951   75.388  1.00 161.78 ?  249  ALA F O   1 
ATOM   17257 C  CB  . ALA F 6  249  ? -36.254 27.099   76.266  1.00 150.47 ?  249  ALA F CB  1 
ATOM   17258 N  N   . LEU F 6  250  ? -37.517 24.732   74.007  1.00 135.33 ?  250  LEU F N   1 
ATOM   17259 C  CA  . LEU F 6  250  ? -38.597 24.361   73.101  1.00 126.93 ?  250  LEU F CA  1 
ATOM   17260 C  C   . LEU F 6  250  ? -39.030 22.914   73.284  1.00 118.48 ?  250  LEU F C   1 
ATOM   17261 O  O   . LEU F 6  250  ? -40.231 22.625   73.284  1.00 111.37 ?  250  LEU F O   1 
ATOM   17262 C  CB  . LEU F 6  250  ? -38.173 24.585   71.645  1.00 116.16 ?  250  LEU F CB  1 
ATOM   17263 C  CG  . LEU F 6  250  ? -37.817 26.015   71.234  1.00 109.62 ?  250  LEU F CG  1 
ATOM   17264 C  CD1 . LEU F 6  250  ? -37.248 26.041   69.823  1.00 103.17 ?  250  LEU F CD1 1 
ATOM   17265 C  CD2 . LEU F 6  250  ? -39.029 26.927   71.342  1.00 119.44 ?  250  LEU F CD2 1 
ATOM   17266 N  N   . PHE F 6  251  ? -38.069 22.000   73.438  1.00 172.11 ?  251  PHE F N   1 
ATOM   17267 C  CA  . PHE F 6  251  ? -38.398 20.619   73.773  1.00 168.41 ?  251  PHE F CA  1 
ATOM   17268 C  C   . PHE F 6  251  ? -39.033 20.529   75.153  1.00 165.71 ?  251  PHE F C   1 
ATOM   17269 O  O   . PHE F 6  251  ? -39.976 19.757   75.365  1.00 164.51 ?  251  PHE F O   1 
ATOM   17270 C  CB  . PHE F 6  251  ? -37.140 19.751   73.724  1.00 168.39 ?  251  PHE F CB  1 
ATOM   17271 C  CG  . PHE F 6  251  ? -36.686 19.402   72.337  1.00 166.70 ?  251  PHE F CG  1 
ATOM   17272 C  CD1 . PHE F 6  251  ? -36.089 20.353   71.527  1.00 174.71 ?  251  PHE F CD1 1 
ATOM   17273 C  CD2 . PHE F 6  251  ? -36.836 18.114   71.852  1.00 160.15 ?  251  PHE F CD2 1 
ATOM   17274 C  CE1 . PHE F 6  251  ? -35.664 20.029   70.254  1.00 161.91 ?  251  PHE F CE1 1 
ATOM   17275 C  CE2 . PHE F 6  251  ? -36.411 17.784   70.580  1.00 165.63 ?  251  PHE F CE2 1 
ATOM   17276 C  CZ  . PHE F 6  251  ? -35.824 18.744   69.779  1.00 163.05 ?  251  PHE F CZ  1 
ATOM   17277 N  N   . ARG F 6  252  ? -38.525 21.319   76.104  1.00 125.62 ?  252  ARG F N   1 
ATOM   17278 C  CA  . ARG F 6  252  ? -38.945 21.198   77.496  1.00 127.45 ?  252  ARG F CA  1 
ATOM   17279 C  C   . ARG F 6  252  ? -40.436 21.449   77.667  1.00 124.94 ?  252  ARG F C   1 
ATOM   17280 O  O   . ARG F 6  252  ? -41.054 20.906   78.590  1.00 127.19 ?  252  ARG F O   1 
ATOM   17281 C  CB  . ARG F 6  252  ? -38.144 22.173   78.361  1.00 137.97 ?  252  ARG F CB  1 
ATOM   17282 C  CG  . ARG F 6  252  ? -36.635 21.997   78.265  1.00 135.62 ?  252  ARG F CG  1 
ATOM   17283 C  CD  . ARG F 6  252  ? -36.162 20.764   79.015  1.00 135.67 ?  252  ARG F CD  1 
ATOM   17284 N  NE  . ARG F 6  252  ? -36.562 20.797   80.416  1.00 130.80 ?  252  ARG F NE  1 
ATOM   17285 C  CZ  . ARG F 6  252  ? -36.306 19.836   81.292  1.00 130.30 ?  252  ARG F CZ  1 
ATOM   17286 N  NH1 . ARG F 6  252  ? -35.644 18.744   80.946  1.00 125.47 ?  252  ARG F NH1 1 
ATOM   17287 N  NH2 . ARG F 6  252  ? -36.720 19.976   82.548  1.00 131.13 ?  252  ARG F NH2 1 
ATOM   17288 N  N   . GLU F 6  253  ? -41.033 22.257   76.792  1.00 144.41 ?  253  GLU F N   1 
ATOM   17289 C  CA  . GLU F 6  253  ? -42.425 22.656   76.937  1.00 142.40 ?  253  GLU F CA  1 
ATOM   17290 C  C   . GLU F 6  253  ? -43.369 21.927   75.990  1.00 141.87 ?  253  GLU F C   1 
ATOM   17291 O  O   . GLU F 6  253  ? -44.588 22.037   76.157  1.00 145.89 ?  253  GLU F O   1 
ATOM   17292 C  CB  . GLU F 6  253  ? -42.565 24.168   76.719  1.00 149.28 ?  253  GLU F CB  1 
ATOM   17293 C  CG  . GLU F 6  253  ? -41.563 25.006   77.497  1.00 154.50 ?  253  GLU F CG  1 
ATOM   17294 C  CD  . GLU F 6  253  ? -42.118 25.512   78.813  1.00 163.53 ?  253  GLU F CD  1 
ATOM   17295 O  OE1 . GLU F 6  253  ? -43.358 25.567   78.954  1.00 165.66 ?  253  GLU F OE1 1 
ATOM   17296 O  OE2 . GLU F 6  253  ? -41.314 25.860   79.704  1.00 167.63 -1 253  GLU F OE2 1 
ATOM   17297 N  N   . TYR F 6  254  ? -42.848 21.185   75.009  1.00 113.10 ?  254  TYR F N   1 
ATOM   17298 C  CA  . TYR F 6  254  ? -43.694 20.565   74.000  1.00 111.51 ?  254  TYR F CA  1 
ATOM   17299 C  C   . TYR F 6  254  ? -43.353 19.110   73.700  1.00 108.64 ?  254  TYR F C   1 
ATOM   17300 O  O   . TYR F 6  254  ? -44.063 18.483   72.906  1.00 108.91 ?  254  TYR F O   1 
ATOM   17301 C  CB  . TYR F 6  254  ? -43.633 21.365   72.688  1.00 116.89 ?  254  TYR F CB  1 
ATOM   17302 C  CG  . TYR F 6  254  ? -44.273 22.735   72.758  1.00 111.67 ?  254  TYR F CG  1 
ATOM   17303 C  CD1 . TYR F 6  254  ? -43.546 23.841   73.179  1.00 112.98 ?  254  TYR F CD1 1 
ATOM   17304 C  CD2 . TYR F 6  254  ? -45.600 22.923   72.395  1.00 107.06 ?  254  TYR F CD2 1 
ATOM   17305 C  CE1 . TYR F 6  254  ? -44.124 25.095   73.242  1.00 116.01 ?  254  TYR F CE1 1 
ATOM   17306 C  CE2 . TYR F 6  254  ? -46.187 24.174   72.455  1.00 108.43 ?  254  TYR F CE2 1 
ATOM   17307 C  CZ  . TYR F 6  254  ? -45.445 25.256   72.879  1.00 113.85 ?  254  TYR F CZ  1 
ATOM   17308 O  OH  . TYR F 6  254  ? -46.026 26.503   72.939  1.00 104.63 ?  254  TYR F OH  1 
ATOM   17309 N  N   . VAL F 6  255  ? -42.305 18.553   74.302  1.00 100.80 ?  255  VAL F N   1 
ATOM   17310 C  CA  . VAL F 6  255  ? -41.845 17.202   74.000  1.00 90.87  ?  255  VAL F CA  1 
ATOM   17311 C  C   . VAL F 6  255  ? -41.882 16.374   75.276  1.00 83.67  ?  255  VAL F C   1 
ATOM   17312 O  O   . VAL F 6  255  ? -41.328 16.783   76.304  1.00 83.43  ?  255  VAL F O   1 
ATOM   17313 C  CB  . VAL F 6  255  ? -40.430 17.207   73.391  1.00 87.28  ?  255  VAL F CB  1 
ATOM   17314 C  CG1 . VAL F 6  255  ? -39.840 15.805   73.392  1.00 92.89  ?  255  VAL F CG1 1 
ATOM   17315 C  CG2 . VAL F 6  255  ? -40.462 17.777   71.982  1.00 84.79  ?  255  VAL F CG2 1 
ATOM   17316 N  N   . SER F 6  256  ? -42.527 15.211   75.206  1.00 92.34  ?  256  SER F N   1 
ATOM   17317 C  CA  . SER F 6  256  ? -42.624 14.278   76.313  1.00 91.77  ?  256  SER F CA  1 
ATOM   17318 C  C   . SER F 6  256  ? -41.816 13.015   75.997  1.00 98.17  ?  256  SER F C   1 
ATOM   17319 O  O   . SER F 6  256  ? -40.961 13.017   75.100  1.00 103.51 ?  256  SER F O   1 
ATOM   17320 C  CB  . SER F 6  256  ? -44.100 13.982   76.595  1.00 94.22  ?  256  SER F CB  1 
ATOM   17321 O  OG  . SER F 6  256  ? -44.754 13.489   75.439  1.00 97.33  ?  256  SER F OG  1 
ATOM   17322 N  N   . VAL F 6  257  ? -42.087 11.937   76.739  1.00 111.96 ?  257  VAL F N   1 
ATOM   17323 C  CA  . VAL F 6  257  ? -41.385 10.673   76.521  1.00 110.10 ?  257  VAL F CA  1 
ATOM   17324 C  C   . VAL F 6  257  ? -41.981 9.856    75.388  1.00 110.56 ?  257  VAL F C   1 
ATOM   17325 O  O   . VAL F 6  257  ? -41.351 8.892    74.936  1.00 112.56 ?  257  VAL F O   1 
ATOM   17326 C  CB  . VAL F 6  257  ? -41.381 9.812    77.797  1.00 110.05 ?  257  VAL F CB  1 
ATOM   17327 C  CG1 . VAL F 6  257  ? -40.504 10.449   78.869  1.00 122.02 ?  257  VAL F CG1 1 
ATOM   17328 C  CG2 . VAL F 6  257  ? -42.802 9.603    78.303  1.00 102.61 ?  257  VAL F CG2 1 
ATOM   17329 N  N   . LYS F 6  258  ? -43.180 10.209   74.917  1.00 119.74 ?  258  LYS F N   1 
ATOM   17330 C  CA  . LYS F 6  258  ? -43.791 9.444    73.831  1.00 120.80 ?  258  LYS F CA  1 
ATOM   17331 C  C   . LYS F 6  258  ? -43.003 9.556    72.530  1.00 114.62 ?  258  LYS F C   1 
ATOM   17332 O  O   . LYS F 6  258  ? -42.775 8.518    71.884  1.00 112.13 ?  258  LYS F O   1 
ATOM   17333 C  CB  . LYS F 6  258  ? -45.254 9.867    73.657  1.00 122.75 ?  258  LYS F CB  1 
ATOM   17334 C  CG  . LYS F 6  258  ? -45.970 9.180    72.508  1.00 119.62 ?  258  LYS F CG  1 
ATOM   17335 C  CD  . LYS F 6  258  ? -47.373 9.738    72.327  1.00 121.65 ?  258  LYS F CD  1 
ATOM   17336 C  CE  . LYS F 6  258  ? -48.121 9.019    71.217  1.00 128.13 ?  258  LYS F CE  1 
ATOM   17337 N  NZ  . LYS F 6  258  ? -48.231 7.556    71.479  1.00 123.58 ?  258  LYS F NZ  1 
ATOM   17338 N  N   . PRO F 6  259  ? -42.569 10.742   72.077  1.00 115.09 ?  259  PRO F N   1 
ATOM   17339 C  CA  . PRO F 6  259  ? -41.758 10.777   70.846  1.00 123.40 ?  259  PRO F CA  1 
ATOM   17340 C  C   . PRO F 6  259  ? -40.446 10.019   70.968  1.00 121.92 ?  259  PRO F C   1 
ATOM   17341 O  O   . PRO F 6  259  ? -40.003 9.396    69.995  1.00 127.19 ?  259  PRO F O   1 
ATOM   17342 C  CB  . PRO F 6  259  ? -41.528 12.278   70.622  1.00 124.03 ?  259  PRO F CB  1 
ATOM   17343 C  CG  . PRO F 6  259  ? -42.651 12.943   71.327  1.00 119.21 ?  259  PRO F CG  1 
ATOM   17344 C  CD  . PRO F 6  259  ? -42.905 12.102   72.537  1.00 119.79 ?  259  PRO F CD  1 
ATOM   17345 N  N   . ILE F 6  260  ? -39.809 10.057   72.140  1.00 88.78  ?  260  ILE F N   1 
ATOM   17346 C  CA  . ILE F 6  260  ? -38.565 9.318    72.332  1.00 88.94  ?  260  ILE F CA  1 
ATOM   17347 C  C   . ILE F 6  260  ? -38.822 7.817    72.266  1.00 91.25  ?  260  ILE F C   1 
ATOM   17348 O  O   . ILE F 6  260  ? -38.017 7.059    71.711  1.00 92.49  ?  260  ILE F O   1 
ATOM   17349 C  CB  . ILE F 6  260  ? -37.904 9.723    73.662  1.00 91.70  ?  260  ILE F CB  1 
ATOM   17350 C  CG1 . ILE F 6  260  ? -37.769 11.244   73.747  1.00 98.27  ?  260  ILE F CG1 1 
ATOM   17351 C  CG2 . ILE F 6  260  ? -36.544 9.059    73.809  1.00 96.78  ?  260  ILE F CG2 1 
ATOM   17352 C  CD1 . ILE F 6  260  ? -37.368 11.746   75.117  1.00 102.11 ?  260  ILE F CD1 1 
ATOM   17353 N  N   . HIS F 6  261  ? -39.946 7.365    72.826  1.00 99.32  ?  261  HIS F N   1 
ATOM   17354 C  CA  . HIS F 6  261  ? -40.284 5.947    72.763  1.00 98.27  ?  261  HIS F CA  1 
ATOM   17355 C  C   . HIS F 6  261  ? -40.602 5.517    71.335  1.00 104.91 ?  261  HIS F C   1 
ATOM   17356 O  O   . HIS F 6  261  ? -40.233 4.413    70.918  1.00 102.39 ?  261  HIS F O   1 
ATOM   17357 C  CB  . HIS F 6  261  ? -41.462 5.648    73.690  1.00 96.39  ?  261  HIS F CB  1 
ATOM   17358 C  CG  . HIS F 6  261  ? -41.597 4.201    74.049  1.00 101.11 ?  261  HIS F CG  1 
ATOM   17359 N  ND1 . HIS F 6  261  ? -42.394 3.329    73.339  1.00 106.41 ?  261  HIS F ND1 1 
ATOM   17360 C  CD2 . HIS F 6  261  ? -41.037 3.472    75.043  1.00 106.11 ?  261  HIS F CD2 1 
ATOM   17361 C  CE1 . HIS F 6  261  ? -42.319 2.126    73.880  1.00 107.85 ?  261  HIS F CE1 1 
ATOM   17362 N  NE2 . HIS F 6  261  ? -41.502 2.185    74.916  1.00 105.28 ?  261  HIS F NE2 1 
ATOM   17363 N  N   . ASP F 6  262  ? -41.282 6.376    70.571  1.00 136.42 ?  262  ASP F N   1 
ATOM   17364 C  CA  . ASP F 6  262  ? -41.619 6.035    69.192  1.00 131.61 ?  262  ASP F CA  1 
ATOM   17365 C  C   . ASP F 6  262  ? -40.374 5.966    68.317  1.00 130.08 ?  262  ASP F C   1 
ATOM   17366 O  O   . ASP F 6  262  ? -40.264 5.089    67.453  1.00 132.93 ?  262  ASP F O   1 
ATOM   17367 C  CB  . ASP F 6  262  ? -42.614 7.048    68.626  1.00 128.86 ?  262  ASP F CB  1 
ATOM   17368 C  CG  . ASP F 6  262  ? -43.919 7.075    69.394  1.00 136.94 ?  262  ASP F CG  1 
ATOM   17369 O  OD1 . ASP F 6  262  ? -44.080 6.258    70.324  1.00 137.00 ?  262  ASP F OD1 1 
ATOM   17370 O  OD2 . ASP F 6  262  ? -44.786 7.913    69.066  1.00 143.79 -1 262  ASP F OD2 1 
ATOM   17371 N  N   . ILE F 6  263  ? -39.429 6.885    68.522  1.00 93.15  ?  263  ILE F N   1 
ATOM   17372 C  CA  . ILE F 6  263  ? -38.203 6.872    67.730  1.00 93.36  ?  263  ILE F CA  1 
ATOM   17373 C  C   . ILE F 6  263  ? -37.337 5.675    68.105  1.00 96.09  ?  263  ILE F C   1 
ATOM   17374 O  O   . ILE F 6  263  ? -36.695 5.061    67.244  1.00 97.48  ?  263  ILE F O   1 
ATOM   17375 C  CB  . ILE F 6  263  ? -37.457 8.209    67.891  1.00 90.25  ?  263  ILE F CB  1 
ATOM   17376 C  CG1 . ILE F 6  263  ? -38.114 9.275    67.012  1.00 95.56  ?  263  ILE F CG1 1 
ATOM   17377 C  CG2 . ILE F 6  263  ? -35.980 8.062    67.553  1.00 87.14  ?  263  ILE F CG2 1 
ATOM   17378 C  CD1 . ILE F 6  263  ? -37.586 10.668   67.229  1.00 109.25 ?  263  ILE F CD1 1 
ATOM   17379 N  N   . GLY F 6  264  ? -37.318 5.311    69.389  1.00 100.96 ?  264  GLY F N   1 
ATOM   17380 C  CA  . GLY F 6  264  ? -36.628 4.095    69.788  1.00 101.14 ?  264  GLY F CA  1 
ATOM   17381 C  C   . GLY F 6  264  ? -37.234 2.854    69.160  1.00 99.36  ?  264  GLY F C   1 
ATOM   17382 O  O   . GLY F 6  264  ? -36.517 1.933    68.762  1.00 94.47  ?  264  GLY F O   1 
ATOM   17383 N  N   . LYS F 6  265  ? -38.566 2.816    69.058  1.00 89.78  ?  265  LYS F N   1 
ATOM   17384 C  CA  . LYS F 6  265  ? -39.226 1.704    68.383  1.00 89.68  ?  265  LYS F CA  1 
ATOM   17385 C  C   . LYS F 6  265  ? -38.914 1.704    66.892  1.00 83.92  ?  265  LYS F C   1 
ATOM   17386 O  O   . LYS F 6  265  ? -38.790 0.638    66.277  1.00 75.85  ?  265  LYS F O   1 
ATOM   17387 C  CB  . LYS F 6  265  ? -40.736 1.770    68.612  1.00 94.18  ?  265  LYS F CB  1 
ATOM   17388 C  CG  . LYS F 6  265  ? -41.189 1.334    69.997  1.00 91.01  ?  265  LYS F CG  1 
ATOM   17389 C  CD  . LYS F 6  265  ? -42.707 1.351    70.104  1.00 88.60  ?  265  LYS F CD  1 
ATOM   17390 C  CE  . LYS F 6  265  ? -43.244 2.775    70.106  1.00 82.10  ?  265  LYS F CE  1 
ATOM   17391 N  NZ  . LYS F 6  265  ? -44.672 2.834    70.524  1.00 75.48  ?  265  LYS F NZ  1 
ATOM   17392 N  N   . LEU F 6  266  ? -38.790 2.891    66.293  1.00 97.26  ?  266  LEU F N   1 
ATOM   17393 C  CA  . LEU F 6  266  ? -38.442 2.973    64.879  1.00 96.92  ?  266  LEU F CA  1 
ATOM   17394 C  C   . LEU F 6  266  ? -37.015 2.501    64.636  1.00 90.67  ?  266  LEU F C   1 
ATOM   17395 O  O   . LEU F 6  266  ? -36.735 1.849    63.623  1.00 88.05  ?  266  LEU F O   1 
ATOM   17396 C  CB  . LEU F 6  266  ? -38.627 4.404    64.375  1.00 91.36  ?  266  LEU F CB  1 
ATOM   17397 C  CG  . LEU F 6  266  ? -40.043 4.797    63.952  1.00 87.53  ?  266  LEU F CG  1 
ATOM   17398 C  CD1 . LEU F 6  266  ? -40.127 6.293    63.699  1.00 99.79  ?  266  LEU F CD1 1 
ATOM   17399 C  CD2 . LEU F 6  266  ? -40.475 4.016    62.721  1.00 83.84  ?  266  LEU F CD2 1 
ATOM   17400 N  N   . ILE F 6  267  ? -36.099 2.826    65.551  1.00 67.07  ?  267  ILE F N   1 
ATOM   17401 C  CA  . ILE F 6  267  ? -34.725 2.344    65.437  1.00 63.92  ?  267  ILE F CA  1 
ATOM   17402 C  C   . ILE F 6  267  ? -34.688 0.824    65.537  1.00 64.12  ?  267  ILE F C   1 
ATOM   17403 O  O   . ILE F 6  267  ? -33.965 0.154    64.788  1.00 67.35  ?  267  ILE F O   1 
ATOM   17404 C  CB  . ILE F 6  267  ? -33.837 3.006    66.508  1.00 62.26  ?  267  ILE F CB  1 
ATOM   17405 C  CG1 . ILE F 6  267  ? -33.631 4.487    66.189  1.00 76.38  ?  267  ILE F CG1 1 
ATOM   17406 C  CG2 . ILE F 6  267  ? -32.498 2.299    66.612  1.00 60.57  ?  267  ILE F CG2 1 
ATOM   17407 C  CD1 . ILE F 6  267  ? -32.851 5.234    67.249  1.00 84.74  ?  267  ILE F CD1 1 
ATOM   17408 N  N   . PHE F 6  268  ? -35.470 0.258    66.459  1.00 82.02  ?  268  PHE F N   1 
ATOM   17409 C  CA  . PHE F 6  268  ? -35.542 -1.194   66.587  1.00 81.24  ?  268  PHE F CA  1 
ATOM   17410 C  C   . PHE F 6  268  ? -36.110 -1.833   65.326  1.00 79.06  ?  268  PHE F C   1 
ATOM   17411 O  O   . PHE F 6  268  ? -35.623 -2.878   64.878  1.00 76.77  ?  268  PHE F O   1 
ATOM   17412 C  CB  . PHE F 6  268  ? -36.390 -1.566   67.805  1.00 83.25  ?  268  PHE F CB  1 
ATOM   17413 C  CG  . PHE F 6  268  ? -36.647 -3.040   67.943  1.00 77.44  ?  268  PHE F CG  1 
ATOM   17414 C  CD1 . PHE F 6  268  ? -35.675 -3.881   68.457  1.00 75.35  ?  268  PHE F CD1 1 
ATOM   17415 C  CD2 . PHE F 6  268  ? -37.864 -3.583   67.563  1.00 76.29  ?  268  PHE F CD2 1 
ATOM   17416 C  CE1 . PHE F 6  268  ? -35.911 -5.236   68.588  1.00 71.55  ?  268  PHE F CE1 1 
ATOM   17417 C  CE2 . PHE F 6  268  ? -38.105 -4.938   67.689  1.00 76.65  ?  268  PHE F CE2 1 
ATOM   17418 C  CZ  . PHE F 6  268  ? -37.127 -5.765   68.203  1.00 72.50  ?  268  PHE F CZ  1 
ATOM   17419 N  N   . ALA F 6  269  ? -37.140 -1.219   64.740  1.00 81.49  ?  269  ALA F N   1 
ATOM   17420 C  CA  . ALA F 6  269  ? -37.768 -1.796   63.557  1.00 75.37  ?  269  ALA F CA  1 
ATOM   17421 C  C   . ALA F 6  269  ? -36.859 -1.696   62.339  1.00 66.27  ?  269  ALA F C   1 
ATOM   17422 O  O   . ALA F 6  269  ? -36.847 -2.596   61.492  1.00 69.42  ?  269  ALA F O   1 
ATOM   17423 C  CB  . ALA F 6  269  ? -39.108 -1.112   63.287  1.00 76.21  ?  269  ALA F CB  1 
ATOM   17424 N  N   . PHE F 6  270  ? -36.090 -0.612   62.231  1.00 67.08  ?  270  PHE F N   1 
ATOM   17425 C  CA  . PHE F 6  270  ? -35.182 -0.472   61.098  1.00 73.66  ?  270  PHE F CA  1 
ATOM   17426 C  C   . PHE F 6  270  ? -33.943 -1.346   61.250  1.00 75.86  ?  270  PHE F C   1 
ATOM   17427 O  O   . PHE F 6  270  ? -33.325 -1.715   60.245  1.00 82.39  ?  270  PHE F O   1 
ATOM   17428 C  CB  . PHE F 6  270  ? -34.785 0.994    60.918  1.00 80.66  ?  270  PHE F CB  1 
ATOM   17429 C  CG  . PHE F 6  270  ? -35.536 1.689    59.819  1.00 81.63  ?  270  PHE F CG  1 
ATOM   17430 C  CD1 . PHE F 6  270  ? -36.830 2.138    60.024  1.00 80.69  ?  270  PHE F CD1 1 
ATOM   17431 C  CD2 . PHE F 6  270  ? -34.952 1.888    58.579  1.00 82.11  ?  270  PHE F CD2 1 
ATOM   17432 C  CE1 . PHE F 6  270  ? -37.528 2.775    59.015  1.00 80.62  ?  270  PHE F CE1 1 
ATOM   17433 C  CE2 . PHE F 6  270  ? -35.644 2.525    57.565  1.00 82.26  ?  270  PHE F CE2 1 
ATOM   17434 C  CZ  . PHE F 6  270  ? -36.933 2.969    57.783  1.00 83.43  ?  270  PHE F CZ  1 
ATOM   17435 N  N   . THR F 6  271  ? -33.570 -1.690   62.484  1.00 74.33  ?  271  THR F N   1 
ATOM   17436 C  CA  . THR F 6  271  ? -32.450 -2.603   62.690  1.00 74.49  ?  271  THR F CA  1 
ATOM   17437 C  C   . THR F 6  271  ? -32.806 -4.014   62.238  1.00 79.67  ?  271  THR F C   1 
ATOM   17438 O  O   . THR F 6  271  ? -32.028 -4.667   61.533  1.00 85.56  ?  271  THR F O   1 
ATOM   17439 C  CB  . THR F 6  271  ? -32.026 -2.596   64.160  1.00 76.18  ?  271  THR F CB  1 
ATOM   17440 O  OG1 . THR F 6  271  ? -31.334 -1.376   64.453  1.00 77.03  ?  271  THR F OG1 1 
ATOM   17441 C  CG2 . THR F 6  271  ? -31.114 -3.777   64.461  1.00 73.36  ?  271  THR F CG2 1 
ATOM   17442 N  N   . VAL F 6  272  ? -33.986 -4.501   62.631  1.00 79.03  ?  272  VAL F N   1 
ATOM   17443 C  CA  . VAL F 6  272  ? -34.409 -5.827   62.195  1.00 74.84  ?  272  VAL F CA  1 
ATOM   17444 C  C   . VAL F 6  272  ? -34.769 -5.819   60.715  1.00 77.95  ?  272  VAL F C   1 
ATOM   17445 O  O   . VAL F 6  272  ? -34.703 -6.859   60.049  1.00 77.59  ?  272  VAL F O   1 
ATOM   17446 C  CB  . VAL F 6  272  ? -35.579 -6.338   63.060  1.00 64.62  ?  272  VAL F CB  1 
ATOM   17447 C  CG1 . VAL F 6  272  ? -35.179 -6.369   64.525  1.00 64.54  ?  272  VAL F CG1 1 
ATOM   17448 C  CG2 . VAL F 6  272  ? -36.819 -5.481   62.855  1.00 70.20  ?  272  VAL F CG2 1 
ATOM   17449 N  N   . LEU F 6  273  ? -35.148 -4.659   60.171  1.00 78.69  ?  273  LEU F N   1 
ATOM   17450 C  CA  . LEU F 6  273  ? -35.412 -4.571   58.739  1.00 78.44  ?  273  LEU F CA  1 
ATOM   17451 C  C   . LEU F 6  273  ? -34.122 -4.699   57.940  1.00 77.90  ?  273  LEU F C   1 
ATOM   17452 O  O   . LEU F 6  273  ? -34.066 -5.430   56.945  1.00 79.79  ?  273  LEU F O   1 
ATOM   17453 C  CB  . LEU F 6  273  ? -36.123 -3.259   58.409  1.00 69.90  ?  273  LEU F CB  1 
ATOM   17454 C  CG  . LEU F 6  273  ? -36.538 -3.084   56.947  1.00 73.81  ?  273  LEU F CG  1 
ATOM   17455 C  CD1 . LEU F 6  273  ? -37.580 -4.122   56.560  1.00 80.07  ?  273  LEU F CD1 1 
ATOM   17456 C  CD2 . LEU F 6  273  ? -37.059 -1.677   56.694  1.00 80.86  ?  273  LEU F CD2 1 
ATOM   17457 N  N   . TRP F 6  274  ? -33.070 -3.996   58.368  1.00 74.76  ?  274  TRP F N   1 
ATOM   17458 C  CA  . TRP F 6  274  ? -31.783 -4.102   57.688  1.00 79.12  ?  274  TRP F CA  1 
ATOM   17459 C  C   . TRP F 6  274  ? -31.231 -5.521   57.770  1.00 77.63  ?  274  TRP F C   1 
ATOM   17460 O  O   . TRP F 6  274  ? -30.698 -6.045   56.784  1.00 76.19  ?  274  TRP F O   1 
ATOM   17461 C  CB  . TRP F 6  274  ? -30.790 -3.103   58.283  1.00 72.96  ?  274  TRP F CB  1 
ATOM   17462 C  CG  . TRP F 6  274  ? -29.362 -3.424   57.962  1.00 78.31  ?  274  TRP F CG  1 
ATOM   17463 C  CD1 . TRP F 6  274  ? -28.664 -3.040   56.854  1.00 79.52  ?  274  TRP F CD1 1 
ATOM   17464 C  CD2 . TRP F 6  274  ? -28.458 -4.204   58.754  1.00 81.96  ?  274  TRP F CD2 1 
ATOM   17465 N  NE1 . TRP F 6  274  ? -27.381 -3.529   56.909  1.00 82.82  ?  274  TRP F NE1 1 
ATOM   17466 C  CE2 . TRP F 6  274  ? -27.230 -4.248   58.065  1.00 82.25  ?  274  TRP F CE2 1 
ATOM   17467 C  CE3 . TRP F 6  274  ? -28.568 -4.868   59.979  1.00 79.96  ?  274  TRP F CE3 1 
ATOM   17468 C  CZ2 . TRP F 6  274  ? -26.121 -4.931   58.560  1.00 89.46  ?  274  TRP F CZ2 1 
ATOM   17469 C  CZ3 . TRP F 6  274  ? -27.466 -5.545   60.469  1.00 80.61  ?  274  TRP F CZ3 1 
ATOM   17470 C  CH2 . TRP F 6  274  ? -26.258 -5.570   59.762  1.00 85.40  ?  274  TRP F CH2 1 
ATOM   17471 N  N   . THR F 6  275  ? -31.347 -6.157   58.939  1.00 67.07  ?  275  THR F N   1 
ATOM   17472 C  CA  . THR F 6  275  ? -30.889 -7.538   59.078  1.00 73.29  ?  275  THR F CA  1 
ATOM   17473 C  C   . THR F 6  275  ? -31.702 -8.474   58.193  1.00 66.69  ?  275  THR F C   1 
ATOM   17474 O  O   . THR F 6  275  ? -31.171 -9.451   57.654  1.00 52.95  ?  275  THR F O   1 
ATOM   17475 C  CB  . THR F 6  275  ? -30.976 -7.981   60.540  1.00 69.39  ?  275  THR F CB  1 
ATOM   17476 O  OG1 . THR F 6  275  ? -30.325 -7.018   61.377  1.00 68.78  ?  275  THR F OG1 1 
ATOM   17477 C  CG2 . THR F 6  275  ? -30.306 -9.335   60.729  1.00 55.88  ?  275  THR F CG2 1 
ATOM   17478 N  N   . TYR F 6  276  ? -32.994 -8.185   58.030  1.00 97.50  ?  276  TYR F N   1 
ATOM   17479 C  CA  . TYR F 6  276  ? -33.847 -9.025   57.197  1.00 87.73  ?  276  TYR F CA  1 
ATOM   17480 C  C   . TYR F 6  276  ? -33.476 -8.905   55.723  1.00 89.65  ?  276  TYR F C   1 
ATOM   17481 O  O   . TYR F 6  276  ? -33.458 -9.909   55.001  1.00 96.43  ?  276  TYR F O   1 
ATOM   17482 C  CB  . TYR F 6  276  ? -35.313 -8.657   57.425  1.00 87.36  ?  276  TYR F CB  1 
ATOM   17483 C  CG  . TYR F 6  276  ? -36.215 -8.896   56.237  1.00 88.08  ?  276  TYR F CG  1 
ATOM   17484 C  CD1 . TYR F 6  276  ? -36.613 -10.180  55.888  1.00 82.70  ?  276  TYR F CD1 1 
ATOM   17485 C  CD2 . TYR F 6  276  ? -36.679 -7.834   55.472  1.00 92.03  ?  276  TYR F CD2 1 
ATOM   17486 C  CE1 . TYR F 6  276  ? -37.442 -10.400  54.807  1.00 79.99  ?  276  TYR F CE1 1 
ATOM   17487 C  CE2 . TYR F 6  276  ? -37.508 -8.044   54.389  1.00 87.09  ?  276  TYR F CE2 1 
ATOM   17488 C  CZ  . TYR F 6  276  ? -37.886 -9.328   54.061  1.00 84.82  ?  276  TYR F CZ  1 
ATOM   17489 O  OH  . TYR F 6  276  ? -38.713 -9.539   52.983  1.00 90.78  ?  276  TYR F OH  1 
ATOM   17490 N  N   . MET F 6  277  ? -33.177 -7.689   55.259  1.00 88.48  ?  277  MET F N   1 
ATOM   17491 C  CA  . MET F 6  277  ? -32.753 -7.506   53.873  1.00 89.89  ?  277  MET F CA  1 
ATOM   17492 C  C   . MET F 6  277  ? -31.409 -8.177   53.614  1.00 83.98  ?  277  MET F C   1 
ATOM   17493 O  O   . MET F 6  277  ? -31.229 -8.860   52.600  1.00 75.69  ?  277  MET F O   1 
ATOM   17494 C  CB  . MET F 6  277  ? -32.677 -6.017   53.535  1.00 89.63  ?  277  MET F CB  1 
ATOM   17495 C  CG  . MET F 6  277  ? -33.950 -5.240   53.809  1.00 96.67  ?  277  MET F CG  1 
ATOM   17496 S  SD  . MET F 6  277  ? -34.161 -3.879   52.646  1.00 107.26 ?  277  MET F SD  1 
ATOM   17497 C  CE  . MET F 6  277  ? -35.083 -4.684   51.340  1.00 90.03  ?  277  MET F CE  1 
ATOM   17498 N  N   . SER F 6  278  ? -30.450 -7.989   54.524  1.00 75.81  ?  278  SER F N   1 
ATOM   17499 C  CA  . SER F 6  278  ? -29.118 -8.550   54.324  1.00 66.62  ?  278  SER F CA  1 
ATOM   17500 C  C   . SER F 6  278  ? -29.145 -10.074  54.347  1.00 73.12  ?  278  SER F C   1 
ATOM   17501 O  O   . SER F 6  278  ? -28.485 -10.723  53.527  1.00 68.50  ?  278  SER F O   1 
ATOM   17502 C  CB  . SER F 6  278  ? -28.158 -8.009   55.383  1.00 71.17  ?  278  SER F CB  1 
ATOM   17503 O  OG  . SER F 6  278  ? -28.588 -8.356   56.688  1.00 94.60  ?  278  SER F OG  1 
ATOM   17504 N  N   . TYR F 6  279  ? -29.900 -10.664  55.278  1.00 79.69  ?  279  TYR F N   1 
ATOM   17505 C  CA  . TYR F 6  279  ? -30.008 -12.118  55.308  1.00 70.58  ?  279  TYR F CA  1 
ATOM   17506 C  C   . TYR F 6  279  ? -30.739 -12.639  54.079  1.00 69.85  ?  279  TYR F C   1 
ATOM   17507 O  O   . TYR F 6  279  ? -30.402 -13.709  53.558  1.00 73.34  ?  279  TYR F O   1 
ATOM   17508 C  CB  . TYR F 6  279  ? -30.718 -12.581  56.581  1.00 70.16  ?  279  TYR F CB  1 
ATOM   17509 C  CG  . TYR F 6  279  ? -31.135 -14.033  56.520  1.00 73.10  ?  279  TYR F CG  1 
ATOM   17510 C  CD1 . TYR F 6  279  ? -30.189 -15.048  56.576  1.00 74.99  ?  279  TYR F CD1 1 
ATOM   17511 C  CD2 . TYR F 6  279  ? -32.472 -14.390  56.390  1.00 76.99  ?  279  TYR F CD2 1 
ATOM   17512 C  CE1 . TYR F 6  279  ? -30.560 -16.376  56.512  1.00 71.82  ?  279  TYR F CE1 1 
ATOM   17513 C  CE2 . TYR F 6  279  ? -32.853 -15.718  56.326  1.00 75.58  ?  279  TYR F CE2 1 
ATOM   17514 C  CZ  . TYR F 6  279  ? -31.893 -16.706  56.387  1.00 72.25  ?  279  TYR F CZ  1 
ATOM   17515 O  OH  . TYR F 6  279  ? -32.262 -18.029  56.323  1.00 77.40  ?  279  TYR F OH  1 
ATOM   17516 N  N   . GLY F 6  280  ? -31.745 -11.901  53.605  1.00 98.46  ?  280  GLY F N   1 
ATOM   17517 C  CA  . GLY F 6  280  ? -32.459 -12.322  52.410  1.00 106.26 ?  280  GLY F CA  1 
ATOM   17518 C  C   . GLY F 6  280  ? -31.559 -12.384  51.193  1.00 103.01 ?  280  GLY F C   1 
ATOM   17519 O  O   . GLY F 6  280  ? -31.584 -13.356  50.434  1.00 97.12  ?  280  GLY F O   1 
ATOM   17520 N  N   . GLN F 6  281  ? -30.744 -11.345  50.992  1.00 81.14  ?  281  GLN F N   1 
ATOM   17521 C  CA  . GLN F 6  281  ? -29.785 -11.360  49.892  1.00 77.94  ?  281  GLN F CA  1 
ATOM   17522 C  C   . GLN F 6  281  ? -28.774 -12.486  50.059  1.00 81.18  ?  281  GLN F C   1 
ATOM   17523 O  O   . GLN F 6  281  ? -28.389 -13.136  49.080  1.00 83.36  ?  281  GLN F O   1 
ATOM   17524 C  CB  . GLN F 6  281  ? -29.067 -10.014  49.795  1.00 85.63  ?  281  GLN F CB  1 
ATOM   17525 C  CG  . GLN F 6  281  ? -27.954 -9.988   48.755  1.00 78.02  ?  281  GLN F CG  1 
ATOM   17526 C  CD  . GLN F 6  281  ? -27.154 -8.701   48.778  1.00 88.22  ?  281  GLN F CD  1 
ATOM   17527 O  OE1 . GLN F 6  281  ? -27.676 -7.636   49.104  1.00 94.34  ?  281  GLN F OE1 1 
ATOM   17528 N  NE2 . GLN F 6  281  ? -25.874 -8.797   48.438  1.00 87.62  ?  281  GLN F NE2 1 
ATOM   17529 N  N   . LEU F 6  282  ? -28.338 -12.734  51.294  1.00 72.58  ?  282  LEU F N   1 
ATOM   17530 C  CA  . LEU F 6  282  ? -27.326 -13.758  51.529  1.00 70.82  ?  282  LEU F CA  1 
ATOM   17531 C  C   . LEU F 6  282  ? -27.867 -15.149  51.220  1.00 61.38  ?  282  LEU F C   1 
ATOM   17532 O  O   . LEU F 6  282  ? -27.229 -15.924  50.500  1.00 57.06  ?  282  LEU F O   1 
ATOM   17533 C  CB  . LEU F 6  282  ? -26.826 -13.673  52.971  1.00 69.28  ?  282  LEU F CB  1 
ATOM   17534 C  CG  . LEU F 6  282  ? -26.016 -14.859  53.494  1.00 58.58  ?  282  LEU F CG  1 
ATOM   17535 C  CD1 . LEU F 6  282  ? -24.728 -15.022  52.705  1.00 52.96  ?  282  LEU F CD1 1 
ATOM   17536 C  CD2 . LEU F 6  282  ? -25.723 -14.676  54.971  1.00 67.44  ?  282  LEU F CD2 1 
ATOM   17537 N  N   . VAL F 6  283  ? -29.052 -15.477  51.741  1.00 54.13  ?  283  VAL F N   1 
ATOM   17538 C  CA  . VAL F 6  283  ? -29.588 -16.822  51.555  1.00 51.54  ?  283  VAL F CA  1 
ATOM   17539 C  C   . VAL F 6  283  ? -29.975 -17.060  50.099  1.00 51.93  ?  283  VAL F C   1 
ATOM   17540 O  O   . VAL F 6  283  ? -29.883 -18.191  49.604  1.00 54.49  ?  283  VAL F O   1 
ATOM   17541 C  CB  . VAL F 6  283  ? -30.776 -17.064  52.509  1.00 56.63  ?  283  VAL F CB  1 
ATOM   17542 C  CG1 . VAL F 6  283  ? -31.949 -16.156  52.165  1.00 63.37  ?  283  VAL F CG1 1 
ATOM   17543 C  CG2 . VAL F 6  283  ? -31.197 -18.529  52.484  1.00 54.45  ?  283  VAL F CG2 1 
ATOM   17544 N  N   . ILE F 6  284  ? -30.400 -16.015  49.386  1.00 62.33  ?  284  ILE F N   1 
ATOM   17545 C  CA  . ILE F 6  284  ? -30.755 -16.176  47.980  1.00 68.24  ?  284  ILE F CA  1 
ATOM   17546 C  C   . ILE F 6  284  ? -29.517 -16.501  47.154  1.00 61.96  ?  284  ILE F C   1 
ATOM   17547 O  O   . ILE F 6  284  ? -29.541 -17.389  46.293  1.00 64.26  ?  284  ILE F O   1 
ATOM   17548 C  CB  . ILE F 6  284  ? -31.473 -14.915  47.463  1.00 68.42  ?  284  ILE F CB  1 
ATOM   17549 C  CG1 . ILE F 6  284  ? -32.908 -14.864  47.992  1.00 65.28  ?  284  ILE F CG1 1 
ATOM   17550 C  CG2 . ILE F 6  284  ? -31.469 -14.874  45.944  1.00 58.13  ?  284  ILE F CG2 1 
ATOM   17551 C  CD1 . ILE F 6  284  ? -33.648 -13.595  47.633  1.00 75.97  ?  284  ILE F CD1 1 
ATOM   17552 N  N   . ILE F 6  285  ? -28.413 -15.801  47.412  1.00 66.17  ?  285  ILE F N   1 
ATOM   17553 C  CA  . ILE F 6  285  ? -27.180 -16.059  46.679  1.00 64.90  ?  285  ILE F CA  1 
ATOM   17554 C  C   . ILE F 6  285  ? -26.512 -17.340  47.173  1.00 61.78  ?  285  ILE F C   1 
ATOM   17555 O  O   . ILE F 6  285  ? -25.881 -18.059  46.389  1.00 61.90  ?  285  ILE F O   1 
ATOM   17556 C  CB  . ILE F 6  285  ? -26.245 -14.841  46.799  1.00 66.28  ?  285  ILE F CB  1 
ATOM   17557 C  CG1 . ILE F 6  285  ? -26.810 -13.656  46.015  1.00 60.45  ?  285  ILE F CG1 1 
ATOM   17558 C  CG2 . ILE F 6  285  ? -24.846 -15.171  46.301  1.00 62.21  ?  285  ILE F CG2 1 
ATOM   17559 C  CD1 . ILE F 6  285  ? -25.880 -12.462  45.956  1.00 66.47  ?  285  ILE F CD1 1 
ATOM   17560 N  N   . TRP F 6  286  ? -26.661 -17.661  48.460  1.00 61.95  ?  286  TRP F N   1 
ATOM   17561 C  CA  . TRP F 6  286  ? -25.958 -18.804  49.035  1.00 66.08  ?  286  TRP F CA  1 
ATOM   17562 C  C   . TRP F 6  286  ? -26.563 -20.125  48.571  1.00 68.90  ?  286  TRP F C   1 
ATOM   17563 O  O   . TRP F 6  286  ? -25.846 -21.014  48.099  1.00 68.26  ?  286  TRP F O   1 
ATOM   17564 C  CB  . TRP F 6  286  ? -25.975 -18.707  50.560  1.00 66.14  ?  286  TRP F CB  1 
ATOM   17565 C  CG  . TRP F 6  286  ? -25.165 -19.745  51.262  1.00 58.62  ?  286  TRP F CG  1 
ATOM   17566 C  CD1 . TRP F 6  286  ? -23.821 -19.719  51.493  1.00 61.19  ?  286  TRP F CD1 1 
ATOM   17567 C  CD2 . TRP F 6  286  ? -25.652 -20.952  51.859  1.00 58.15  ?  286  TRP F CD2 1 
ATOM   17568 N  NE1 . TRP F 6  286  ? -23.438 -20.842  52.184  1.00 64.39  ?  286  TRP F NE1 1 
ATOM   17569 C  CE2 . TRP F 6  286  ? -24.544 -21.615  52.422  1.00 61.72  ?  286  TRP F CE2 1 
ATOM   17570 C  CE3 . TRP F 6  286  ? -26.916 -21.540  51.964  1.00 59.78  ?  286  TRP F CE3 1 
ATOM   17571 C  CZ2 . TRP F 6  286  ? -24.662 -22.836  53.080  1.00 63.85  ?  286  TRP F CZ2 1 
ATOM   17572 C  CZ3 . TRP F 6  286  ? -27.031 -22.751  52.618  1.00 61.05  ?  286  TRP F CZ3 1 
ATOM   17573 C  CH2 . TRP F 6  286  ? -25.910 -23.387  53.168  1.00 65.37  ?  286  TRP F CH2 1 
ATOM   17574 N  N   . SER F 6  287  ? -27.884 -20.274  48.699  1.00 67.01  ?  287  SER F N   1 
ATOM   17575 C  CA  . SER F 6  287  ? -28.516 -21.544  48.352  1.00 62.73  ?  287  SER F CA  1 
ATOM   17576 C  C   . SER F 6  287  ? -28.487 -21.788  46.848  1.00 62.79  ?  287  SER F C   1 
ATOM   17577 O  O   . SER F 6  287  ? -28.235 -22.913  46.401  1.00 76.02  ?  287  SER F O   1 
ATOM   17578 C  CB  . SER F 6  287  ? -29.950 -21.575  48.875  1.00 67.50  ?  287  SER F CB  1 
ATOM   17579 O  OG  . SER F 6  287  ? -30.000 -21.248  50.253  1.00 62.05  ?  287  SER F OG  1 
ATOM   17580 N  N   . GLY F 6  288  ? -28.749 -20.755  46.052  1.00 73.71  ?  288  GLY F N   1 
ATOM   17581 C  CA  . GLY F 6  288  ? -28.596 -20.861  44.614  1.00 73.17  ?  288  GLY F CA  1 
ATOM   17582 C  C   . GLY F 6  288  ? -27.174 -20.551  44.196  1.00 68.22  ?  288  GLY F C   1 
ATOM   17583 O  O   . GLY F 6  288  ? -26.830 -19.390  43.955  1.00 69.50  ?  288  GLY F O   1 
ATOM   17584 N  N   . ASP F 6  289  ? -26.334 -21.583  44.103  1.00 64.77  ?  289  ASP F N   1 
ATOM   17585 C  CA  . ASP F 6  289  ? -24.892 -21.403  43.934  1.00 65.07  ?  289  ASP F CA  1 
ATOM   17586 C  C   . ASP F 6  289  ? -24.536 -21.100  42.475  1.00 62.78  ?  289  ASP F C   1 
ATOM   17587 O  O   . ASP F 6  289  ? -23.777 -21.814  41.822  1.00 65.32  ?  289  ASP F O   1 
ATOM   17588 C  CB  . ASP F 6  289  ? -24.156 -22.636  44.443  1.00 68.36  ?  289  ASP F CB  1 
ATOM   17589 C  CG  . ASP F 6  289  ? -22.694 -22.363  44.736  1.00 67.07  ?  289  ASP F CG  1 
ATOM   17590 O  OD1 . ASP F 6  289  ? -22.408 -21.614  45.693  1.00 65.80  ?  289  ASP F OD1 1 
ATOM   17591 O  OD2 . ASP F 6  289  ? -21.830 -22.904  44.014  1.00 71.99  -1 289  ASP F OD2 1 
ATOM   17592 N  N   . VAL F 6  290  ? -25.098 -20.003  41.972  1.00 71.54  ?  290  VAL F N   1 
ATOM   17593 C  CA  . VAL F 6  290  ? -24.812 -19.550  40.615  1.00 73.76  ?  290  VAL F CA  1 
ATOM   17594 C  C   . VAL F 6  290  ? -23.503 -18.773  40.623  1.00 74.17  ?  290  VAL F C   1 
ATOM   17595 O  O   . VAL F 6  290  ? -23.277 -17.923  41.492  1.00 76.65  ?  290  VAL F O   1 
ATOM   17596 C  CB  . VAL F 6  290  ? -25.967 -18.697  40.068  1.00 69.11  ?  290  VAL F CB  1 
ATOM   17597 C  CG1 . VAL F 6  290  ? -25.685 -18.278  38.636  1.00 73.60  ?  290  VAL F CG1 1 
ATOM   17598 C  CG2 . VAL F 6  290  ? -27.273 -19.471  40.145  1.00 71.12  ?  290  VAL F CG2 1 
ATOM   17599 N  N   . ALA F 6  291  ? -22.636 -19.059  39.650  1.00 46.39  ?  291  ALA F N   1 
ATOM   17600 C  CA  . ALA F 6  291  ? -21.284 -18.515  39.687  1.00 52.63  ?  291  ALA F CA  1 
ATOM   17601 C  C   . ALA F 6  291  ? -21.233 -17.028  39.367  1.00 60.32  ?  291  ALA F C   1 
ATOM   17602 O  O   . ALA F 6  291  ? -20.208 -16.390  39.628  1.00 59.52  ?  291  ALA F O   1 
ATOM   17603 C  CB  . ALA F 6  291  ? -20.378 -19.280  38.723  1.00 49.97  ?  291  ALA F CB  1 
ATOM   17604 N  N   . GLU F 6  292  ? -22.302 -16.459  38.813  1.00 111.04 ?  292  GLU F N   1 
ATOM   17605 C  CA  . GLU F 6  292  ? -22.307 -15.034  38.512  1.00 113.43 ?  292  GLU F CA  1 
ATOM   17606 C  C   . GLU F 6  292  ? -22.591 -14.165  39.732  1.00 114.75 ?  292  GLU F C   1 
ATOM   17607 O  O   . GLU F 6  292  ? -22.409 -12.945  39.654  1.00 116.23 ?  292  GLU F O   1 
ATOM   17608 C  CB  . GLU F 6  292  ? -23.327 -14.724  37.414  1.00 118.72 ?  292  GLU F CB  1 
ATOM   17609 C  CG  . GLU F 6  292  ? -22.832 -15.027  36.006  1.00 136.02 ?  292  GLU F CG  1 
ATOM   17610 C  CD  . GLU F 6  292  ? -23.448 -16.282  35.419  1.00 144.67 ?  292  GLU F CD  1 
ATOM   17611 O  OE1 . GLU F 6  292  ? -23.959 -17.119  36.193  1.00 141.56 ?  292  GLU F OE1 1 
ATOM   17612 O  OE2 . GLU F 6  292  ? -23.428 -16.426  34.178  1.00 140.98 -1 292  GLU F OE2 1 
ATOM   17613 N  N   . PHE F 6  293  ? -23.023 -14.752  40.849  1.00 80.86  ?  293  PHE F N   1 
ATOM   17614 C  CA  . PHE F 6  293  ? -23.323 -13.993  42.056  1.00 70.85  ?  293  PHE F CA  1 
ATOM   17615 C  C   . PHE F 6  293  ? -22.487 -14.410  43.258  1.00 75.13  ?  293  PHE F C   1 
ATOM   17616 O  O   . PHE F 6  293  ? -22.595 -13.779  44.316  1.00 95.02  ?  293  PHE F O   1 
ATOM   17617 C  CB  . PHE F 6  293  ? -24.813 -14.114  42.406  1.00 76.69  ?  293  PHE F CB  1 
ATOM   17618 C  CG  . PHE F 6  293  ? -25.737 -13.815  41.257  1.00 79.44  ?  293  PHE F CG  1 
ATOM   17619 C  CD1 . PHE F 6  293  ? -25.908 -12.516  40.807  1.00 86.29  ?  293  PHE F CD1 1 
ATOM   17620 C  CD2 . PHE F 6  293  ? -26.437 -14.833  40.630  1.00 78.57  ?  293  PHE F CD2 1 
ATOM   17621 C  CE1 . PHE F 6  293  ? -26.759 -12.238  39.752  1.00 81.10  ?  293  PHE F CE1 1 
ATOM   17622 C  CE2 . PHE F 6  293  ? -27.289 -14.561  39.574  1.00 79.27  ?  293  PHE F CE2 1 
ATOM   17623 C  CZ  . PHE F 6  293  ? -27.449 -13.262  39.135  1.00 76.88  ?  293  PHE F CZ  1 
ATOM   17624 N  N   . THR F 6  294  ? -21.660 -15.446  43.131  1.00 66.25  ?  294  THR F N   1 
ATOM   17625 C  CA  . THR F 6  294  ? -20.835 -15.946  44.226  1.00 68.85  ?  294  THR F CA  1 
ATOM   17626 C  C   . THR F 6  294  ? -19.568 -15.131  44.506  1.00 72.35  ?  294  THR F C   1 
ATOM   17627 O  O   . THR F 6  294  ? -19.157 -15.059  45.671  1.00 60.37  ?  294  THR F O   1 
ATOM   17628 C  CB  . THR F 6  294  ? -20.448 -17.406  43.971  1.00 68.96  ?  294  THR F CB  1 
ATOM   17629 O  OG1 . THR F 6  294  ? -19.992 -17.563  42.620  1.00 67.55  ?  294  THR F OG1 1 
ATOM   17630 C  CG2 . THR F 6  294  ? -21.636 -18.326  44.221  1.00 67.44  ?  294  THR F CG2 1 
ATOM   17631 N  N   . PRO F 6  295  ? -18.901 -14.528  43.507  1.00 110.07 ?  295  PRO F N   1 
ATOM   17632 C  CA  . PRO F 6  295  ? -17.667 -13.786  43.826  1.00 107.48 ?  295  PRO F CA  1 
ATOM   17633 C  C   . PRO F 6  295  ? -17.858 -12.660  44.826  1.00 108.83 ?  295  PRO F C   1 
ATOM   17634 O  O   . PRO F 6  295  ? -16.899 -12.300  45.521  1.00 106.81 ?  295  PRO F O   1 
ATOM   17635 C  CB  . PRO F 6  295  ? -17.222 -13.247  42.460  1.00 96.77  ?  295  PRO F CB  1 
ATOM   17636 C  CG  . PRO F 6  295  ? -17.751 -14.221  41.497  1.00 106.55 ?  295  PRO F CG  1 
ATOM   17637 C  CD  . PRO F 6  295  ? -19.090 -14.617  42.046  1.00 103.87 ?  295  PRO F CD  1 
ATOM   17638 N  N   . TRP F 6  296  ? -19.060 -12.088  44.921  1.00 79.80  ?  296  TRP F N   1 
ATOM   17639 C  CA  . TRP F 6  296  ? -19.295 -11.032  45.901  1.00 75.78  ?  296  TRP F CA  1 
ATOM   17640 C  C   . TRP F 6  296  ? -19.112 -11.554  47.320  1.00 74.50  ?  296  TRP F C   1 
ATOM   17641 O  O   . TRP F 6  296  ? -18.321 -11.008  48.097  1.00 79.84  ?  296  TRP F O   1 
ATOM   17642 C  CB  . TRP F 6  296  ? -20.692 -10.438  45.721  1.00 79.06  ?  296  TRP F CB  1 
ATOM   17643 C  CG  . TRP F 6  296  ? -20.844 -9.092   46.366  1.00 85.75  ?  296  TRP F CG  1 
ATOM   17644 C  CD1 . TRP F 6  296  ? -20.447 -7.890   45.859  1.00 87.72  ?  296  TRP F CD1 1 
ATOM   17645 C  CD2 . TRP F 6  296  ? -21.434 -8.814   47.642  1.00 77.09  ?  296  TRP F CD2 1 
ATOM   17646 N  NE1 . TRP F 6  296  ? -20.753 -6.880   46.739  1.00 85.80  ?  296  TRP F NE1 1 
ATOM   17647 C  CE2 . TRP F 6  296  ? -21.360 -7.421   47.842  1.00 73.84  ?  296  TRP F CE2 1 
ATOM   17648 C  CE3 . TRP F 6  296  ? -22.018 -9.607   48.634  1.00 73.30  ?  296  TRP F CE3 1 
ATOM   17649 C  CZ2 . TRP F 6  296  ? -21.849 -6.805   48.991  1.00 77.25  ?  296  TRP F CZ2 1 
ATOM   17650 C  CZ3 . TRP F 6  296  ? -22.502 -8.994   49.773  1.00 72.18  ?  296  TRP F CZ3 1 
ATOM   17651 C  CH2 . TRP F 6  296  ? -22.415 -7.607   49.943  1.00 74.83  ?  296  TRP F CH2 1 
ATOM   17652 N  N   . TYR F 6  297  ? -19.832 -12.619  47.676  1.00 65.60  ?  297  TYR F N   1 
ATOM   17653 C  CA  . TYR F 6  297  ? -19.703 -13.184  49.013  1.00 63.89  ?  297  TYR F CA  1 
ATOM   17654 C  C   . TYR F 6  297  ? -18.407 -13.962  49.202  1.00 68.23  ?  297  TYR F C   1 
ATOM   17655 O  O   . TYR F 6  297  ? -18.088 -14.330  50.337  1.00 66.98  ?  297  TYR F O   1 
ATOM   17656 C  CB  . TYR F 6  297  ? -20.907 -14.076  49.319  1.00 59.05  ?  297  TYR F CB  1 
ATOM   17657 C  CG  . TYR F 6  297  ? -22.120 -13.296  49.770  1.00 60.59  ?  297  TYR F CG  1 
ATOM   17658 C  CD1 . TYR F 6  297  ? -22.164 -12.712  51.029  1.00 61.61  ?  297  TYR F CD1 1 
ATOM   17659 C  CD2 . TYR F 6  297  ? -23.214 -13.128  48.932  1.00 63.50  ?  297  TYR F CD2 1 
ATOM   17660 C  CE1 . TYR F 6  297  ? -23.269 -11.993  51.445  1.00 63.75  ?  297  TYR F CE1 1 
ATOM   17661 C  CE2 . TYR F 6  297  ? -24.326 -12.410  49.339  1.00 64.50  ?  297  TYR F CE2 1 
ATOM   17662 C  CZ  . TYR F 6  297  ? -24.347 -11.845  50.597  1.00 63.59  ?  297  TYR F CZ  1 
ATOM   17663 O  OH  . TYR F 6  297  ? -25.449 -11.128  51.007  1.00 67.07  ?  297  TYR F OH  1 
ATOM   17664 N  N   . VAL F 6  298  ? -17.653 -14.213  48.132  1.00 91.47  ?  298  VAL F N   1 
ATOM   17665 C  CA  . VAL F 6  298  ? -16.348 -14.847  48.281  1.00 87.79  ?  298  VAL F CA  1 
ATOM   17666 C  C   . VAL F 6  298  ? -15.338 -13.852  48.841  1.00 94.34  ?  298  VAL F C   1 
ATOM   17667 O  O   . VAL F 6  298  ? -14.602 -14.155  49.788  1.00 95.72  ?  298  VAL F O   1 
ATOM   17668 C  CB  . VAL F 6  298  ? -15.880 -15.433  46.936  1.00 85.62  ?  298  VAL F CB  1 
ATOM   17669 C  CG1 . VAL F 6  298  ? -14.369 -15.613  46.924  1.00 86.85  ?  298  VAL F CG1 1 
ATOM   17670 C  CG2 . VAL F 6  298  ? -16.578 -16.756  46.664  1.00 87.09  ?  298  VAL F CG2 1 
ATOM   17671 N  N   . HIS F 6  299  ? -15.297 -12.645  48.269  1.00 85.79  ?  299  HIS F N   1 
ATOM   17672 C  CA  . HIS F 6  299  ? -14.337 -11.641  48.718  1.00 83.43  ?  299  HIS F CA  1 
ATOM   17673 C  C   . HIS F 6  299  ? -14.637 -11.182  50.139  1.00 76.09  ?  299  HIS F C   1 
ATOM   17674 O  O   . HIS F 6  299  ? -13.716 -10.908  50.917  1.00 73.27  ?  299  HIS F O   1 
ATOM   17675 C  CB  . HIS F 6  299  ? -14.340 -10.445  47.765  1.00 86.58  ?  299  HIS F CB  1 
ATOM   17676 C  CG  . HIS F 6  299  ? -14.154 -10.813  46.325  1.00 88.35  ?  299  HIS F CG  1 
ATOM   17677 N  ND1 . HIS F 6  299  ? -13.481 -11.947  45.923  1.00 89.36  ?  299  HIS F ND1 1 
ATOM   17678 C  CD2 . HIS F 6  299  ? -14.554 -10.191  45.190  1.00 81.12  ?  299  HIS F CD2 1 
ATOM   17679 C  CE1 . HIS F 6  299  ? -13.475 -12.008  44.603  1.00 86.39  ?  299  HIS F CE1 1 
ATOM   17680 N  NE2 . HIS F 6  299  ? -14.119 -10.955  44.134  1.00 77.31  ?  299  HIS F NE2 1 
ATOM   17681 N  N   . ARG F 6  300  ? -15.918 -11.092  50.499  1.00 71.23  ?  300  ARG F N   1 
ATOM   17682 C  CA  . ARG F 6  300  ? -16.297 -10.635  51.829  1.00 72.35  ?  300  ARG F CA  1 
ATOM   17683 C  C   . ARG F 6  300  ? -16.109 -11.702  52.898  1.00 76.41  ?  300  ARG F C   1 
ATOM   17684 O  O   . ARG F 6  300  ? -16.257 -11.397  54.086  1.00 82.41  ?  300  ARG F O   1 
ATOM   17685 C  CB  . ARG F 6  300  ? -17.753 -10.154  51.831  1.00 75.32  ?  300  ARG F CB  1 
ATOM   17686 C  CG  . ARG F 6  300  ? -17.941 -8.700   51.397  1.00 79.69  ?  300  ARG F CG  1 
ATOM   17687 C  CD  . ARG F 6  300  ? -17.699 -8.538   49.907  1.00 79.05  ?  300  ARG F CD  1 
ATOM   17688 N  NE  . ARG F 6  300  ? -17.964 -7.188   49.427  1.00 83.89  ?  300  ARG F NE  1 
ATOM   17689 C  CZ  . ARG F 6  300  ? -17.773 -6.793   48.176  1.00 96.98  ?  300  ARG F CZ  1 
ATOM   17690 N  NH1 . ARG F 6  300  ? -17.318 -7.622   47.251  1.00 96.53  ?  300  ARG F NH1 1 
ATOM   17691 N  NH2 . ARG F 6  300  ? -18.044 -5.534   47.845  1.00 94.37  ?  300  ARG F NH2 1 
ATOM   17692 N  N   . THR F 6  301  ? -15.794 -12.938  52.508  1.00 73.60  ?  301  THR F N   1 
ATOM   17693 C  CA  . THR F 6  301  ? -15.515 -14.020  53.444  1.00 72.49  ?  301  THR F CA  1 
ATOM   17694 C  C   . THR F 6  301  ? -14.064 -14.482  53.370  1.00 80.05  ?  301  THR F C   1 
ATOM   17695 O  O   . THR F 6  301  ? -13.732 -15.558  53.875  1.00 92.54  ?  301  THR F O   1 
ATOM   17696 C  CB  . THR F 6  301  ? -16.453 -15.201  53.193  1.00 74.93  ?  301  THR F CB  1 
ATOM   17697 O  OG1 . THR F 6  301  ? -16.332 -15.629  51.830  1.00 78.78  ?  301  THR F OG1 1 
ATOM   17698 C  CG2 . THR F 6  301  ? -17.894 -14.811  53.481  1.00 66.81  ?  301  THR F CG2 1 
ATOM   17699 N  N   . GLN F 6  302  ? -13.192 -13.686  52.758  1.00 91.71  ?  302  GLN F N   1 
ATOM   17700 C  CA  . GLN F 6  302  ? -11.813 -14.073  52.515  1.00 92.96  ?  302  GLN F CA  1 
ATOM   17701 C  C   . GLN F 6  302  ? -10.854 -13.086  53.169  1.00 96.99  ?  302  GLN F C   1 
ATOM   17702 O  O   . GLN F 6  302  ? -11.183 -11.916  53.387  1.00 105.97 ?  302  GLN F O   1 
ATOM   17703 C  CB  . GLN F 6  302  ? -11.521 -14.159  51.010  1.00 95.07  ?  302  GLN F CB  1 
ATOM   17704 C  CG  . GLN F 6  302  ? -11.192 -12.820  50.361  1.00 97.48  ?  302  GLN F CG  1 
ATOM   17705 C  CD  . GLN F 6  302  ? -10.813 -12.951  48.899  1.00 99.99  ?  302  GLN F CD  1 
ATOM   17706 O  OE1 . GLN F 6  302  ? -10.676 -14.057  48.377  1.00 110.40 ?  302  GLN F OE1 1 
ATOM   17707 N  NE2 . GLN F 6  302  ? -10.645 -11.817  48.228  1.00 101.63 ?  302  GLN F NE2 1 
ATOM   17708 N  N   . HIS F 6  303  ? -9.656  -13.589  53.480  1.00 84.75  ?  303  HIS F N   1 
ATOM   17709 C  CA  . HIS F 6  303  ? -8.554  -12.778  54.006  1.00 94.16  ?  303  HIS F CA  1 
ATOM   17710 C  C   . HIS F 6  303  ? -8.982  -11.941  55.210  1.00 90.57  ?  303  HIS F C   1 
ATOM   17711 O  O   . HIS F 6  303  ? -8.667  -10.754  55.315  1.00 94.60  ?  303  HIS F O   1 
ATOM   17712 C  CB  . HIS F 6  303  ? -7.955  -11.894  52.910  1.00 101.25 ?  303  HIS F CB  1 
ATOM   17713 C  CG  . HIS F 6  303  ? -7.377  -12.663  51.762  1.00 106.36 ?  303  HIS F CG  1 
ATOM   17714 N  ND1 . HIS F 6  303  ? -6.406  -13.627  51.928  1.00 109.95 ?  303  HIS F ND1 1 
ATOM   17715 C  CD2 . HIS F 6  303  ? -7.631  -12.612  50.432  1.00 107.79 ?  303  HIS F CD2 1 
ATOM   17716 C  CE1 . HIS F 6  303  ? -6.085  -14.135  50.751  1.00 113.78 ?  303  HIS F CE1 1 
ATOM   17717 N  NE2 . HIS F 6  303  ? -6.815  -13.537  49.827  1.00 109.25 ?  303  HIS F NE2 1 
ATOM   17718 N  N   . GLY F 6  304  ? -9.709  -12.569  56.132  1.00 116.83 ?  304  GLY F N   1 
ATOM   17719 C  CA  . GLY F 6  304  ? -10.099 -11.927  57.367  1.00 122.23 ?  304  GLY F CA  1 
ATOM   17720 C  C   . GLY F 6  304  ? -11.375 -11.115  57.308  1.00 122.11 ?  304  GLY F C   1 
ATOM   17721 O  O   . GLY F 6  304  ? -11.870 -10.697  58.362  1.00 123.87 ?  304  GLY F O   1 
ATOM   17722 N  N   . TRP F 6  305  ? -11.928 -10.879  56.116  1.00 89.17  ?  305  TRP F N   1 
ATOM   17723 C  CA  . TRP F 6  305  ? -13.158 -10.104  56.011  1.00 86.14  ?  305  TRP F CA  1 
ATOM   17724 C  C   . TRP F 6  305  ? -14.346 -10.822  56.637  1.00 82.48  ?  305  TRP F C   1 
ATOM   17725 O  O   . TRP F 6  305  ? -15.371 -10.184  56.905  1.00 81.35  ?  305  TRP F O   1 
ATOM   17726 C  CB  . TRP F 6  305  ? -13.456 -9.781   54.546  1.00 86.43  ?  305  TRP F CB  1 
ATOM   17727 C  CG  . TRP F 6  305  ? -12.587 -8.696   53.979  1.00 88.73  ?  305  TRP F CG  1 
ATOM   17728 C  CD1 . TRP F 6  305  ? -11.503 -8.858   53.166  1.00 93.48  ?  305  TRP F CD1 1 
ATOM   17729 C  CD2 . TRP F 6  305  ? -12.720 -7.285   54.192  1.00 94.66  ?  305  TRP F CD2 1 
ATOM   17730 N  NE1 . TRP F 6  305  ? -10.957 -7.638   52.854  1.00 95.57  ?  305  TRP F NE1 1 
ATOM   17731 C  CE2 . TRP F 6  305  ? -11.684 -6.656   53.472  1.00 98.46  ?  305  TRP F CE2 1 
ATOM   17732 C  CE3 . TRP F 6  305  ? -13.614 -6.491   54.919  1.00 93.28  ?  305  TRP F CE3 1 
ATOM   17733 C  CZ2 . TRP F 6  305  ? -11.517 -5.274   53.457  1.00 105.92 ?  305  TRP F CZ2 1 
ATOM   17734 C  CZ3 . TRP F 6  305  ? -13.445 -5.117   54.902  1.00 96.93  ?  305  TRP F CZ3 1 
ATOM   17735 C  CH2 . TRP F 6  305  ? -12.406 -4.524   54.176  1.00 104.33 ?  305  TRP F CH2 1 
ATOM   17736 N  N   . VAL F 6  306  ? -14.230 -12.129  56.873  1.00 87.17  ?  306  VAL F N   1 
ATOM   17737 C  CA  . VAL F 6  306  ? -15.307 -12.874  57.513  1.00 92.29  ?  306  VAL F CA  1 
ATOM   17738 C  C   . VAL F 6  306  ? -15.505 -12.402  58.949  1.00 91.75  ?  306  VAL F C   1 
ATOM   17739 O  O   . VAL F 6  306  ? -16.640 -12.317  59.438  1.00 88.40  ?  306  VAL F O   1 
ATOM   17740 C  CB  . VAL F 6  306  ? -15.019 -14.385  57.435  1.00 98.49  ?  306  VAL F CB  1 
ATOM   17741 C  CG1 . VAL F 6  306  ? -13.586 -14.674  57.860  1.00 105.57 ?  306  VAL F CG1 1 
ATOM   17742 C  CG2 . VAL F 6  306  ? -16.006 -15.170  58.288  1.00 89.07  ?  306  VAL F CG2 1 
ATOM   17743 N  N   . PHE F 6  307  ? -14.411 -12.067  59.641  1.00 74.24  ?  307  PHE F N   1 
ATOM   17744 C  CA  . PHE F 6  307  ? -14.521 -11.594  61.018  1.00 67.02  ?  307  PHE F CA  1 
ATOM   17745 C  C   . PHE F 6  307  ? -15.334 -10.309  61.092  1.00 65.11  ?  307  PHE F C   1 
ATOM   17746 O  O   . PHE F 6  307  ? -16.063 -10.081  62.065  1.00 64.59  ?  307  PHE F O   1 
ATOM   17747 C  CB  . PHE F 6  307  ? -13.130 -11.379  61.615  1.00 68.91  ?  307  PHE F CB  1 
ATOM   17748 C  CG  . PHE F 6  307  ? -12.237 -12.579  61.515  1.00 80.36  ?  307  PHE F CG  1 
ATOM   17749 C  CD1 . PHE F 6  307  ? -12.656 -13.814  61.980  1.00 83.83  ?  307  PHE F CD1 1 
ATOM   17750 C  CD2 . PHE F 6  307  ? -10.975 -12.473  60.955  1.00 87.46  ?  307  PHE F CD2 1 
ATOM   17751 C  CE1 . PHE F 6  307  ? -11.831 -14.922  61.887  1.00 88.10  ?  307  PHE F CE1 1 
ATOM   17752 C  CE2 . PHE F 6  307  ? -10.146 -13.574  60.859  1.00 93.54  ?  307  PHE F CE2 1 
ATOM   17753 C  CZ  . PHE F 6  307  ? -10.574 -14.801  61.325  1.00 96.55  ?  307  PHE F CZ  1 
ATOM   17754 N  N   . VAL F 6  308  ? -15.223 -9.460   60.069  1.00 66.94  ?  308  VAL F N   1 
ATOM   17755 C  CA  . VAL F 6  308  ? -16.046 -8.257   60.006  1.00 61.45  ?  308  VAL F CA  1 
ATOM   17756 C  C   . VAL F 6  308  ? -17.520 -8.627   59.903  1.00 66.69  ?  308  VAL F C   1 
ATOM   17757 O  O   . VAL F 6  308  ? -18.373 -8.037   60.578  1.00 67.67  ?  308  VAL F O   1 
ATOM   17758 C  CB  . VAL F 6  308  ? -15.600 -7.369   58.830  1.00 64.75  ?  308  VAL F CB  1 
ATOM   17759 C  CG1 . VAL F 6  308  ? -16.518 -6.162   58.692  1.00 66.45  ?  308  VAL F CG1 1 
ATOM   17760 C  CG2 . VAL F 6  308  ? -14.151 -6.933   59.014  1.00 72.58  ?  308  VAL F CG2 1 
ATOM   17761 N  N   . ALA F 6  309  ? -17.840 -9.617   59.065  1.00 81.24  ?  309  ALA F N   1 
ATOM   17762 C  CA  . ALA F 6  309  ? -19.230 -10.030  58.906  1.00 81.15  ?  309  ALA F CA  1 
ATOM   17763 C  C   . ALA F 6  309  ? -19.784 -10.622  60.195  1.00 83.01  ?  309  ALA F C   1 
ATOM   17764 O  O   . ALA F 6  309  ? -20.940 -10.371  60.555  1.00 86.75  ?  309  ALA F O   1 
ATOM   17765 C  CB  . ALA F 6  309  ? -19.354 -11.033  57.759  1.00 77.61  ?  309  ALA F CB  1 
ATOM   17766 N  N   . LEU F 6  310  ? -18.974 -11.410  60.906  1.00 76.70  ?  310  LEU F N   1 
ATOM   17767 C  CA  . LEU F 6  310  ? -19.434 -12.003  62.157  1.00 77.71  ?  310  LEU F CA  1 
ATOM   17768 C  C   . LEU F 6  310  ? -19.681 -10.937  63.216  1.00 79.15  ?  310  LEU F C   1 
ATOM   17769 O  O   . LEU F 6  310  ? -20.643 -11.032  63.988  1.00 87.60  ?  310  LEU F O   1 
ATOM   17770 C  CB  . LEU F 6  310  ? -18.421 -13.033  62.655  1.00 83.65  ?  310  LEU F CB  1 
ATOM   17771 C  CG  . LEU F 6  310  ? -18.187 -14.235  61.738  1.00 83.17  ?  310  LEU F CG  1 
ATOM   17772 C  CD1 . LEU F 6  310  ? -17.013 -15.067  62.231  1.00 78.89  ?  310  LEU F CD1 1 
ATOM   17773 C  CD2 . LEU F 6  310  ? -19.447 -15.084  61.630  1.00 73.87  ?  310  LEU F CD2 1 
ATOM   17774 N  N   . ALA F 6  311  ? -18.824 -9.913   63.267  1.00 57.73  ?  311  ALA F N   1 
ATOM   17775 C  CA  . ALA F 6  311  ? -19.034 -8.822   64.213  1.00 59.25  ?  311  ALA F CA  1 
ATOM   17776 C  C   . ALA F 6  311  ? -20.327 -8.077   63.910  1.00 64.01  ?  311  ALA F C   1 
ATOM   17777 O  O   . ALA F 6  311  ? -21.064 -7.697   64.827  1.00 68.49  ?  311  ALA F O   1 
ATOM   17778 C  CB  . ALA F 6  311  ? -17.844 -7.863   64.188  1.00 55.00  ?  311  ALA F CB  1 
ATOM   17779 N  N   . LEU F 6  312  ? -20.616 -7.860   62.625  1.00 80.23  ?  312  LEU F N   1 
ATOM   17780 C  CA  . LEU F 6  312  ? -21.874 -7.225   62.248  1.00 80.07  ?  312  LEU F CA  1 
ATOM   17781 C  C   . LEU F 6  312  ? -23.065 -8.087   62.645  1.00 80.58  ?  312  LEU F C   1 
ATOM   17782 O  O   . LEU F 6  312  ? -24.111 -7.568   63.051  1.00 80.31  ?  312  LEU F O   1 
ATOM   17783 C  CB  . LEU F 6  312  ? -21.888 -6.952   60.744  1.00 75.62  ?  312  LEU F CB  1 
ATOM   17784 C  CG  . LEU F 6  312  ? -20.881 -5.929   60.213  1.00 83.21  ?  312  LEU F CG  1 
ATOM   17785 C  CD1 . LEU F 6  312  ? -20.911 -5.896   58.693  1.00 82.17  ?  312  LEU F CD1 1 
ATOM   17786 C  CD2 . LEU F 6  312  ? -21.147 -4.543   60.786  1.00 86.43  ?  312  LEU F CD2 1 
ATOM   17787 N  N   . MET F 6  313  ? -22.924 -9.410   62.538  1.00 103.62 ?  313  MET F N   1 
ATOM   17788 C  CA  . MET F 6  313  ? -24.031 -10.302  62.871  1.00 100.82 ?  313  MET F CA  1 
ATOM   17789 C  C   . MET F 6  313  ? -24.399 -10.206  64.346  1.00 104.81 ?  313  MET F C   1 
ATOM   17790 O  O   . MET F 6  313  ? -25.577 -10.310  64.707  1.00 105.27 ?  313  MET F O   1 
ATOM   17791 C  CB  . MET F 6  313  ? -23.672 -11.741  62.506  1.00 96.42  ?  313  MET F CB  1 
ATOM   17792 C  CG  . MET F 6  313  ? -23.799 -12.063  61.029  1.00 112.65 ?  313  MET F CG  1 
ATOM   17793 S  SD  . MET F 6  313  ? -23.197 -13.720  60.652  1.00 139.15 ?  313  MET F SD  1 
ATOM   17794 C  CE  . MET F 6  313  ? -24.040 -14.683  61.906  1.00 102.73 ?  313  MET F CE  1 
ATOM   17795 N  N   . LEU F 6  314  ? -23.409 -10.004  65.213  1.00 99.98  ?  314  LEU F N   1 
ATOM   17796 C  CA  . LEU F 6  314  ? -23.627 -9.985   66.654  1.00 103.44 ?  314  LEU F CA  1 
ATOM   17797 C  C   . LEU F 6  314  ? -23.738 -8.573   67.216  1.00 101.27 ?  314  LEU F C   1 
ATOM   17798 O  O   . LEU F 6  314  ? -24.708 -8.257   67.910  1.00 96.60  ?  314  LEU F O   1 
ATOM   17799 C  CB  . LEU F 6  314  ? -22.497 -10.743  67.361  1.00 106.99 ?  314  LEU F CB  1 
ATOM   17800 C  CG  . LEU F 6  314  ? -22.542 -10.772  68.889  1.00 101.07 ?  314  LEU F CG  1 
ATOM   17801 C  CD1 . LEU F 6  314  ? -23.671 -11.669  69.372  1.00 100.47 ?  314  LEU F CD1 1 
ATOM   17802 C  CD2 . LEU F 6  314  ? -21.208 -11.224  69.457  1.00 90.89  ?  314  LEU F CD2 1 
ATOM   17803 N  N   . PHE F 6  315  ? -22.761 -7.710   66.925  1.00 98.17  ?  315  PHE F N   1 
ATOM   17804 C  CA  . PHE F 6  315  ? -22.769 -6.369   67.500  1.00 90.08  ?  315  PHE F CA  1 
ATOM   17805 C  C   . PHE F 6  315  ? -23.820 -5.473   66.856  1.00 88.80  ?  315  PHE F C   1 
ATOM   17806 O  O   . PHE F 6  315  ? -24.299 -4.530   67.496  1.00 93.18  ?  315  PHE F O   1 
ATOM   17807 C  CB  . PHE F 6  315  ? -21.388 -5.727   67.373  1.00 84.34  ?  315  PHE F CB  1 
ATOM   17808 C  CG  . PHE F 6  315  ? -20.327 -6.395   68.198  1.00 93.64  ?  315  PHE F CG  1 
ATOM   17809 C  CD1 . PHE F 6  315  ? -20.629 -6.929   69.441  1.00 86.69  ?  315  PHE F CD1 1 
ATOM   17810 C  CD2 . PHE F 6  315  ? -19.024 -6.480   67.737  1.00 97.79  ?  315  PHE F CD2 1 
ATOM   17811 C  CE1 . PHE F 6  315  ? -19.652 -7.539   70.204  1.00 84.18  ?  315  PHE F CE1 1 
ATOM   17812 C  CE2 . PHE F 6  315  ? -18.043 -7.089   68.495  1.00 97.30  ?  315  PHE F CE2 1 
ATOM   17813 C  CZ  . PHE F 6  315  ? -18.358 -7.619   69.730  1.00 91.71  ?  315  PHE F CZ  1 
ATOM   17814 N  N   . ALA F 6  316  ? -24.188 -5.737   65.602  1.00 80.75  ?  316  ALA F N   1 
ATOM   17815 C  CA  . ALA F 6  316  ? -25.137 -4.884   64.900  1.00 76.50  ?  316  ALA F CA  1 
ATOM   17816 C  C   . ALA F 6  316  ? -26.532 -5.485   64.792  1.00 75.59  ?  316  ALA F C   1 
ATOM   17817 O  O   . ALA F 6  316  ? -27.448 -4.794   64.336  1.00 73.60  ?  316  ALA F O   1 
ATOM   17818 C  CB  . ALA F 6  316  ? -24.618 -4.545   63.496  1.00 71.63  ?  316  ALA F CB  1 
ATOM   17819 N  N   . PHE F 6  317  ? -26.723 -6.743   65.199  1.00 81.08  ?  317  PHE F N   1 
ATOM   17820 C  CA  . PHE F 6  317  ? -28.054 -7.346   65.207  1.00 79.54  ?  317  PHE F CA  1 
ATOM   17821 C  C   . PHE F 6  317  ? -28.444 -7.812   66.604  1.00 85.17  ?  317  PHE F C   1 
ATOM   17822 O  O   . PHE F 6  317  ? -29.329 -7.210   67.215  1.00 92.20  ?  317  PHE F O   1 
ATOM   17823 C  CB  . PHE F 6  317  ? -28.144 -8.502   64.211  1.00 73.12  ?  317  PHE F CB  1 
ATOM   17824 C  CG  . PHE F 6  317  ? -29.395 -9.321   64.363  1.00 77.51  ?  317  PHE F CG  1 
ATOM   17825 C  CD1 . PHE F 6  317  ? -30.642 -8.727   64.257  1.00 84.19  ?  317  PHE F CD1 1 
ATOM   17826 C  CD2 . PHE F 6  317  ? -29.325 -10.674  64.652  1.00 76.96  ?  317  PHE F CD2 1 
ATOM   17827 C  CE1 . PHE F 6  317  ? -31.796 -9.469   64.409  1.00 82.98  ?  317  PHE F CE1 1 
ATOM   17828 C  CE2 . PHE F 6  317  ? -30.478 -11.423  64.807  1.00 79.92  ?  317  PHE F CE2 1 
ATOM   17829 C  CZ  . PHE F 6  317  ? -31.715 -10.819  64.686  1.00 78.72  ?  317  PHE F CZ  1 
ATOM   17830 N  N   . ALA F 6  318  ? -27.817 -8.870   67.127  1.00 86.11  ?  318  ALA F N   1 
ATOM   17831 C  CA  . ALA F 6  318  ? -28.299 -9.492   68.357  1.00 83.27  ?  318  ALA F CA  1 
ATOM   17832 C  C   . ALA F 6  318  ? -28.233 -8.527   69.533  1.00 87.95  ?  318  ALA F C   1 
ATOM   17833 O  O   . ALA F 6  318  ? -29.207 -8.374   70.279  1.00 91.92  ?  318  ALA F O   1 
ATOM   17834 C  CB  . ALA F 6  318  ? -27.497 -10.759  68.656  1.00 87.45  ?  318  ALA F CB  1 
ATOM   17835 N  N   . LEU F 6  319  ? -27.091 -7.864   69.713  1.00 92.33  ?  319  LEU F N   1 
ATOM   17836 C  CA  . LEU F 6  319  ? -26.949 -6.936   70.833  1.00 88.38  ?  319  LEU F CA  1 
ATOM   17837 C  C   . LEU F 6  319  ? -27.936 -5.776   70.760  1.00 89.39  ?  319  LEU F C   1 
ATOM   17838 O  O   . LEU F 6  319  ? -28.569 -5.475   71.786  1.00 92.84  ?  319  LEU F O   1 
ATOM   17839 C  CB  . LEU F 6  319  ? -25.499 -6.447   70.918  1.00 89.42  ?  319  LEU F CB  1 
ATOM   17840 C  CG  . LEU F 6  319  ? -25.130 -5.607   72.141  1.00 100.96 ?  319  LEU F CG  1 
ATOM   17841 C  CD1 . LEU F 6  319  ? -25.186 -6.445   73.408  1.00 91.15  ?  319  LEU F CD1 1 
ATOM   17842 C  CD2 . LEU F 6  319  ? -23.755 -4.979   71.963  1.00 104.72 ?  319  LEU F CD2 1 
ATOM   17843 N  N   . PRO F 6  320  ? -28.126 -5.091   69.623  1.00 70.68  ?  320  PRO F N   1 
ATOM   17844 C  CA  . PRO F 6  320  ? -29.166 -4.048   69.596  1.00 68.65  ?  320  PRO F CA  1 
ATOM   17845 C  C   . PRO F 6  320  ? -30.571 -4.605   69.724  1.00 70.75  ?  320  PRO F C   1 
ATOM   17846 O  O   . PRO F 6  320  ? -31.436 -3.957   70.327  1.00 74.99  ?  320  PRO F O   1 
ATOM   17847 C  CB  . PRO F 6  320  ? -28.945 -3.371   68.235  1.00 59.60  ?  320  PRO F CB  1 
ATOM   17848 C  CG  . PRO F 6  320  ? -27.513 -3.632   67.922  1.00 57.27  ?  320  PRO F CG  1 
ATOM   17849 C  CD  . PRO F 6  320  ? -27.304 -5.042   68.401  1.00 67.04  ?  320  PRO F CD  1 
ATOM   17850 N  N   . PHE F 6  321  ? -30.820 -5.796   69.175  1.00 78.06  ?  321  PHE F N   1 
ATOM   17851 C  CA  . PHE F 6  321  ? -32.160 -6.374   69.212  1.00 79.03  ?  321  PHE F CA  1 
ATOM   17852 C  C   . PHE F 6  321  ? -32.595 -6.683   70.639  1.00 86.31  ?  321  PHE F C   1 
ATOM   17853 O  O   . PHE F 6  321  ? -33.750 -6.441   71.011  1.00 88.18  ?  321  PHE F O   1 
ATOM   17854 C  CB  . PHE F 6  321  ? -32.204 -7.630   68.338  1.00 72.48  ?  321  PHE F CB  1 
ATOM   17855 C  CG  . PHE F 6  321  ? -33.413 -8.496   68.558  1.00 73.19  ?  321  PHE F CG  1 
ATOM   17856 C  CD1 . PHE F 6  321  ? -34.578 -8.280   67.842  1.00 69.16  ?  321  PHE F CD1 1 
ATOM   17857 C  CD2 . PHE F 6  321  ? -33.370 -9.556   69.452  1.00 83.59  ?  321  PHE F CD2 1 
ATOM   17858 C  CE1 . PHE F 6  321  ? -35.690 -9.083   68.037  1.00 72.16  ?  321  PHE F CE1 1 
ATOM   17859 C  CE2 . PHE F 6  321  ? -34.477 -10.363  69.650  1.00 79.93  ?  321  PHE F CE2 1 
ATOM   17860 C  CZ  . PHE F 6  321  ? -35.637 -10.127  68.942  1.00 74.11  ?  321  PHE F CZ  1 
ATOM   17861 N  N   . PHE F 6  322  ? -31.684 -7.215   71.456  1.00 110.91 ?  322  PHE F N   1 
ATOM   17862 C  CA  . PHE F 6  322  ? -32.037 -7.577   72.824  1.00 113.39 ?  322  PHE F CA  1 
ATOM   17863 C  C   . PHE F 6  322  ? -32.116 -6.357   73.735  1.00 117.45 ?  322  PHE F C   1 
ATOM   17864 O  O   . PHE F 6  322  ? -32.974 -6.298   74.622  1.00 114.01 ?  322  PHE F O   1 
ATOM   17865 C  CB  . PHE F 6  322  ? -31.029 -8.586   73.374  1.00 110.96 ?  322  PHE F CB  1 
ATOM   17866 C  CG  . PHE F 6  322  ? -31.263 -9.994   72.906  1.00 120.68 ?  322  PHE F CG  1 
ATOM   17867 C  CD1 . PHE F 6  322  ? -32.452 -10.642  73.197  1.00 118.76 ?  322  PHE F CD1 1 
ATOM   17868 C  CD2 . PHE F 6  322  ? -30.296 -10.672  72.180  1.00 122.58 ?  322  PHE F CD2 1 
ATOM   17869 C  CE1 . PHE F 6  322  ? -32.675 -11.937  72.772  1.00 119.42 ?  322  PHE F CE1 1 
ATOM   17870 C  CE2 . PHE F 6  322  ? -30.514 -11.969  71.752  1.00 126.71 ?  322  PHE F CE2 1 
ATOM   17871 C  CZ  . PHE F 6  322  ? -31.706 -12.602  72.049  1.00 128.30 ?  322  PHE F CZ  1 
ATOM   17872 N  N   . VAL F 6  323  ? -31.229 -5.379   73.539  1.00 95.43  ?  323  VAL F N   1 
ATOM   17873 C  CA  . VAL F 6  323  ? -31.233 -4.191   74.388  1.00 87.77  ?  323  VAL F CA  1 
ATOM   17874 C  C   . VAL F 6  323  ? -32.490 -3.364   74.148  1.00 89.45  ?  323  VAL F C   1 
ATOM   17875 O  O   . VAL F 6  323  ? -33.174 -2.955   75.094  1.00 96.27  ?  323  VAL F O   1 
ATOM   17876 C  CB  . VAL F 6  323  ? -29.958 -3.360   74.159  1.00 83.92  ?  323  VAL F CB  1 
ATOM   17877 C  CG1 . VAL F 6  323  ? -30.060 -2.029   74.881  1.00 92.66  ?  323  VAL F CG1 1 
ATOM   17878 C  CG2 . VAL F 6  323  ? -28.740 -4.125   74.647  1.00 79.44  ?  323  VAL F CG2 1 
ATOM   17879 N  N   . LEU F 6  324  ? -32.815 -3.108   72.882  1.00 65.93  ?  324  LEU F N   1 
ATOM   17880 C  CA  . LEU F 6  324  ? -33.994 -2.322   72.540  1.00 68.66  ?  324  LEU F CA  1 
ATOM   17881 C  C   . LEU F 6  324  ? -35.290 -3.117   72.641  1.00 70.97  ?  324  LEU F C   1 
ATOM   17882 O  O   . LEU F 6  324  ? -36.364 -2.553   72.406  1.00 69.31  ?  324  LEU F O   1 
ATOM   17883 C  CB  . LEU F 6  324  ? -33.843 -1.742   71.132  1.00 68.27  ?  324  LEU F CB  1 
ATOM   17884 C  CG  . LEU F 6  324  ? -32.907 -0.533   71.048  1.00 72.75  ?  324  LEU F CG  1 
ATOM   17885 C  CD1 . LEU F 6  324  ? -32.727 -0.063   69.609  1.00 65.55  ?  324  LEU F CD1 1 
ATOM   17886 C  CD2 . LEU F 6  324  ? -33.412 0.601    71.934  1.00 71.74  ?  324  LEU F CD2 1 
ATOM   17887 N  N   . LEU F 6  325  ? -35.216 -4.407   72.981  1.00 86.54  ?  325  LEU F N   1 
ATOM   17888 C  CA  . LEU F 6  325  ? -36.427 -5.198   73.173  1.00 86.19  ?  325  LEU F CA  1 
ATOM   17889 C  C   . LEU F 6  325  ? -37.217 -4.725   74.386  1.00 90.61  ?  325  LEU F C   1 
ATOM   17890 O  O   . LEU F 6  325  ? -38.451 -4.802   74.395  1.00 98.77  ?  325  LEU F O   1 
ATOM   17891 C  CB  . LEU F 6  325  ? -36.064 -6.677   73.324  1.00 76.83  ?  325  LEU F CB  1 
ATOM   17892 C  CG  . LEU F 6  325  ? -37.084 -7.728   72.883  1.00 80.02  ?  325  LEU F CG  1 
ATOM   17893 C  CD1 . LEU F 6  325  ? -37.566 -7.454   71.470  1.00 77.08  ?  325  LEU F CD1 1 
ATOM   17894 C  CD2 . LEU F 6  325  ? -36.485 -9.124   72.985  1.00 94.82  ?  325  LEU F CD2 1 
ATOM   17895 N  N   . PHE F 6  326  ? -36.526 -4.232   75.410  1.00 93.08  ?  326  PHE F N   1 
ATOM   17896 C  CA  . PHE F 6  326  ? -37.166 -3.835   76.652  1.00 94.49  ?  326  PHE F CA  1 
ATOM   17897 C  C   . PHE F 6  326  ? -37.859 -2.484   76.495  1.00 94.99  ?  326  PHE F C   1 
ATOM   17898 O  O   . PHE F 6  326  ? -37.515 -1.674   75.628  1.00 92.70  ?  326  PHE F O   1 
ATOM   17899 C  CB  . PHE F 6  326  ? -36.140 -3.770   77.782  1.00 91.05  ?  326  PHE F CB  1 
ATOM   17900 C  CG  . PHE F 6  326  ? -35.461 -5.081   78.058  1.00 91.02  ?  326  PHE F CG  1 
ATOM   17901 C  CD1 . PHE F 6  326  ? -36.116 -6.081   78.758  1.00 86.96  ?  326  PHE F CD1 1 
ATOM   17902 C  CD2 . PHE F 6  326  ? -34.173 -5.319   77.609  1.00 87.35  ?  326  PHE F CD2 1 
ATOM   17903 C  CE1 . PHE F 6  326  ? -35.494 -7.293   79.013  1.00 81.28  ?  326  PHE F CE1 1 
ATOM   17904 C  CE2 . PHE F 6  326  ? -33.547 -6.528   77.859  1.00 89.70  ?  326  PHE F CE2 1 
ATOM   17905 C  CZ  . PHE F 6  326  ? -34.209 -7.516   78.562  1.00 85.90  ?  326  PHE F CZ  1 
ATOM   17906 N  N   . ARG F 6  327  ? -38.856 -2.249   77.356  1.00 95.44  ?  327  ARG F N   1 
ATOM   17907 C  CA  . ARG F 6  327  ? -39.523 -0.951   77.373  1.00 103.80 ?  327  ARG F CA  1 
ATOM   17908 C  C   . ARG F 6  327  ? -38.560 0.149    77.808  1.00 99.55  ?  327  ARG F C   1 
ATOM   17909 O  O   . ARG F 6  327  ? -38.611 1.269    77.284  1.00 99.78  ?  327  ARG F O   1 
ATOM   17910 C  CB  . ARG F 6  327  ? -40.747 -1.000   78.288  1.00 98.23  ?  327  ARG F CB  1 
ATOM   17911 C  CG  . ARG F 6  327  ? -41.674 0.188    78.115  1.00 95.40  ?  327  ARG F CG  1 
ATOM   17912 C  CD  . ARG F 6  327  ? -43.017 -0.057   78.779  1.00 108.11 ?  327  ARG F CD  1 
ATOM   17913 N  NE  . ARG F 6  327  ? -44.056 0.827    78.262  1.00 116.68 ?  327  ARG F NE  1 
ATOM   17914 C  CZ  . ARG F 6  327  ? -44.401 1.982    78.815  1.00 127.58 ?  327  ARG F CZ  1 
ATOM   17915 N  NH1 . ARG F 6  327  ? -43.802 2.431    79.904  1.00 129.71 ?  327  ARG F NH1 1 
ATOM   17916 N  NH2 . ARG F 6  327  ? -45.372 2.702    78.260  1.00 130.10 ?  327  ARG F NH2 1 
ATOM   17917 N  N   . GLY F 6  328  ? -37.678 -0.153   78.761  1.00 105.36 ?  328  GLY F N   1 
ATOM   17918 C  CA  . GLY F 6  328  ? -36.577 0.732    79.067  1.00 96.27  ?  328  GLY F CA  1 
ATOM   17919 C  C   . GLY F 6  328  ? -35.532 0.697    77.974  1.00 104.15 ?  328  GLY F C   1 
ATOM   17920 O  O   . GLY F 6  328  ? -35.582 -0.125   77.056  1.00 104.85 ?  328  GLY F O   1 
ATOM   17921 N  N   . THR F 6  329  ? -34.559 1.612    78.092  1.00 112.97 ?  329  THR F N   1 
ATOM   17922 C  CA  . THR F 6  329  ? -33.486 1.797    77.114  1.00 107.59 ?  329  THR F CA  1 
ATOM   17923 C  C   . THR F 6  329  ? -33.987 2.442    75.827  1.00 111.19 ?  329  THR F C   1 
ATOM   17924 O  O   . THR F 6  329  ? -33.180 2.908    75.016  1.00 107.49 ?  329  THR F O   1 
ATOM   17925 C  CB  . THR F 6  329  ? -32.774 0.475    76.813  1.00 107.76 ?  329  THR F CB  1 
ATOM   17926 O  OG1 . THR F 6  329  ? -33.588 -0.309   75.926  1.00 112.25 ?  329  THR F OG1 1 
ATOM   17927 C  CG2 . THR F 6  329  ? -32.450 -0.278   78.110  1.00 110.34 ?  329  THR F CG2 1 
ATOM   17928 N  N   . LYS F 6  330  ? -35.305 2.513    75.642  1.00 112.98 ?  330  LYS F N   1 
ATOM   17929 C  CA  . LYS F 6  330  ? -35.882 3.341    74.589  1.00 120.37 ?  330  LYS F CA  1 
ATOM   17930 C  C   . LYS F 6  330  ? -36.667 4.528    75.125  1.00 123.24 ?  330  LYS F C   1 
ATOM   17931 O  O   . LYS F 6  330  ? -36.720 5.570    74.464  1.00 120.25 ?  330  LYS F O   1 
ATOM   17932 C  CB  . LYS F 6  330  ? -36.797 2.512    73.678  1.00 120.44 ?  330  LYS F CB  1 
ATOM   17933 C  CG  . LYS F 6  330  ? -37.501 1.350    74.358  1.00 121.11 ?  330  LYS F CG  1 
ATOM   17934 C  CD  . LYS F 6  330  ? -38.431 0.630    73.387  1.00 121.00 ?  330  LYS F CD  1 
ATOM   17935 C  CE  . LYS F 6  330  ? -37.777 0.370    72.036  1.00 118.41 ?  330  LYS F CE  1 
ATOM   17936 N  NZ  . LYS F 6  330  ? -38.524 -0.659   71.255  1.00 117.20 ?  330  LYS F NZ  1 
ATOM   17937 N  N   . ARG F 6  331  ? -37.259 4.399    76.315  1.00 112.98 ?  331  ARG F N   1 
ATOM   17938 C  CA  . ARG F 6  331  ? -37.920 5.537    76.943  1.00 115.88 ?  331  ARG F CA  1 
ATOM   17939 C  C   . ARG F 6  331  ? -36.901 6.542    77.465  1.00 117.71 ?  331  ARG F C   1 
ATOM   17940 O  O   . ARG F 6  331  ? -37.131 7.755    77.405  1.00 119.24 ?  331  ARG F O   1 
ATOM   17941 C  CB  . ARG F 6  331  ? -38.831 5.053    78.071  1.00 111.55 ?  331  ARG F CB  1 
ATOM   17942 C  CG  . ARG F 6  331  ? -39.529 6.172    78.838  1.00 119.73 ?  331  ARG F CG  1 
ATOM   17943 C  CD  . ARG F 6  331  ? -40.963 5.816    79.183  1.00 122.40 ?  331  ARG F CD  1 
ATOM   17944 N  NE  . ARG F 6  331  ? -41.754 5.508    78.000  1.00 118.09 ?  331  ARG F NE  1 
ATOM   17945 C  CZ  . ARG F 6  331  ? -43.077 5.423    77.992  1.00 123.10 ?  331  ARG F CZ  1 
ATOM   17946 N  NH1 . ARG F 6  331  ? -43.786 5.606    79.093  1.00 117.41 ?  331  ARG F NH1 1 
ATOM   17947 N  NH2 . ARG F 6  331  ? -43.703 5.154    76.850  1.00 129.37 ?  331  ARG F NH2 1 
ATOM   17948 N  N   . ASN F 6  332  ? -35.769 6.059    77.972  1.00 105.08 ?  332  ASN F N   1 
ATOM   17949 C  CA  . ASN F 6  332  ? -34.729 6.939    78.486  1.00 107.34 ?  332  ASN F CA  1 
ATOM   17950 C  C   . ASN F 6  332  ? -33.885 7.455    77.328  1.00 111.83 ?  332  ASN F C   1 
ATOM   17951 O  O   . ASN F 6  332  ? -33.327 6.664    76.559  1.00 116.01 ?  332  ASN F O   1 
ATOM   17952 C  CB  . ASN F 6  332  ? -33.865 6.203    79.506  1.00 109.67 ?  332  ASN F CB  1 
ATOM   17953 C  CG  . ASN F 6  332  ? -32.904 7.125    80.227  1.00 111.57 ?  332  ASN F CG  1 
ATOM   17954 O  OD1 . ASN F 6  332  ? -32.968 8.345    80.080  1.00 120.46 ?  332  ASN F OD1 1 
ATOM   17955 N  ND2 . ASN F 6  332  ? -32.008 6.545    81.017  1.00 106.31 ?  332  ASN F ND2 1 
ATOM   17956 N  N   . LEU F 6  333  ? -33.796 8.781    77.202  1.00 105.12 ?  333  LEU F N   1 
ATOM   17957 C  CA  . LEU F 6  333  ? -33.049 9.377    76.099  1.00 107.07 ?  333  LEU F CA  1 
ATOM   17958 C  C   . LEU F 6  333  ? -31.557 9.089    76.216  1.00 109.74 ?  333  LEU F C   1 
ATOM   17959 O  O   . LEU F 6  333  ? -30.881 8.873    75.203  1.00 109.51 ?  333  LEU F O   1 
ATOM   17960 C  CB  . LEU F 6  333  ? -33.304 10.883   76.054  1.00 115.53 ?  333  LEU F CB  1 
ATOM   17961 C  CG  . LEU F 6  333  ? -32.874 11.631   74.791  1.00 123.48 ?  333  LEU F CG  1 
ATOM   17962 C  CD1 . LEU F 6  333  ? -33.217 10.838   73.539  1.00 117.36 ?  333  LEU F CD1 1 
ATOM   17963 C  CD2 . LEU F 6  333  ? -33.511 13.012   74.747  1.00 116.57 ?  333  LEU F CD2 1 
ATOM   17964 N  N   . ASN F 6  334  ? -31.028 9.084    77.442  1.00 117.20 ?  334  ASN F N   1 
ATOM   17965 C  CA  . ASN F 6  334  ? -29.603 8.833    77.639  1.00 122.32 ?  334  ASN F CA  1 
ATOM   17966 C  C   . ASN F 6  334  ? -29.215 7.447    77.141  1.00 126.25 ?  334  ASN F C   1 
ATOM   17967 O  O   . ASN F 6  334  ? -28.242 7.291    76.393  1.00 129.91 ?  334  ASN F O   1 
ATOM   17968 C  CB  . ASN F 6  334  ? -29.241 8.990    79.117  1.00 125.54 ?  334  ASN F CB  1 
ATOM   17969 C  CG  . ASN F 6  334  ? -28.889 10.419   79.483  1.00 133.94 ?  334  ASN F CG  1 
ATOM   17970 O  OD1 . ASN F 6  334  ? -28.084 11.062   78.810  1.00 138.81 ?  334  ASN F OD1 1 
ATOM   17971 N  ND2 . ASN F 6  334  ? -29.491 10.922   80.556  1.00 133.41 ?  334  ASN F ND2 1 
ATOM   17972 N  N   . THR F 6  335  ? -29.968 6.423    77.551  1.00 102.89 ?  335  THR F N   1 
ATOM   17973 C  CA  . THR F 6  335  ? -29.658 5.060    77.132  1.00 102.65 ?  335  THR F CA  1 
ATOM   17974 C  C   . THR F 6  335  ? -29.843 4.882    75.631  1.00 99.82  ?  335  THR F C   1 
ATOM   17975 O  O   . THR F 6  335  ? -29.041 4.203    74.980  1.00 96.22  ?  335  THR F O   1 
ATOM   17976 C  CB  . THR F 6  335  ? -30.525 4.063    77.899  1.00 98.75  ?  335  THR F CB  1 
ATOM   17977 O  OG1 . THR F 6  335  ? -30.671 4.503    79.253  1.00 103.88 ?  335  THR F OG1 1 
ATOM   17978 C  CG2 . THR F 6  335  ? -29.885 2.688    77.890  1.00 90.99  ?  335  THR F CG2 1 
ATOM   17979 N  N   . LEU F 6  336  ? -30.891 5.488    75.064  1.00 94.00  ?  336  LEU F N   1 
ATOM   17980 C  CA  . LEU F 6  336  ? -31.124 5.379    73.626  1.00 88.71  ?  336  LEU F CA  1 
ATOM   17981 C  C   . LEU F 6  336  ? -29.995 6.022    72.834  1.00 87.63  ?  336  LEU F C   1 
ATOM   17982 O  O   . LEU F 6  336  ? -29.596 5.511    71.780  1.00 83.28  ?  336  LEU F O   1 
ATOM   17983 C  CB  . LEU F 6  336  ? -32.465 6.018    73.262  1.00 83.01  ?  336  LEU F CB  1 
ATOM   17984 C  CG  . LEU F 6  336  ? -32.918 5.889    71.805  1.00 89.49  ?  336  LEU F CG  1 
ATOM   17985 C  CD1 . LEU F 6  336  ? -33.102 4.432    71.426  1.00 87.11  ?  336  LEU F CD1 1 
ATOM   17986 C  CD2 . LEU F 6  336  ? -34.197 6.676    71.564  1.00 94.33  ?  336  LEU F CD2 1 
ATOM   17987 N  N   . ALA F 6  337  ? -29.469 7.148    73.323  1.00 108.79 ?  337  ALA F N   1 
ATOM   17988 C  CA  . ALA F 6  337  ? -28.356 7.801    72.642  1.00 111.91 ?  337  ALA F CA  1 
ATOM   17989 C  C   . ALA F 6  337  ? -27.098 6.943    72.695  1.00 111.21 ?  337  ALA F C   1 
ATOM   17990 O  O   . ALA F 6  337  ? -26.336 6.889    71.723  1.00 108.75 ?  337  ALA F O   1 
ATOM   17991 C  CB  . ALA F 6  337  ? -28.096 9.176    73.256  1.00 107.08 ?  337  ALA F CB  1 
ATOM   17992 N  N   . THR F 6  338  ? -26.866 6.265    73.823  1.00 90.67  ?  338  THR F N   1 
ATOM   17993 C  CA  . THR F 6  338  ? -25.716 5.371    73.922  1.00 88.54  ?  338  THR F CA  1 
ATOM   17994 C  C   . THR F 6  338  ? -25.829 4.215    72.937  1.00 78.96  ?  338  THR F C   1 
ATOM   17995 O  O   . THR F 6  338  ? -24.845 3.848    72.285  1.00 78.35  ?  338  THR F O   1 
ATOM   17996 C  CB  . THR F 6  338  ? -25.577 4.842    75.349  1.00 88.41  ?  338  THR F CB  1 
ATOM   17997 O  OG1 . THR F 6  338  ? -25.703 5.928    76.277  1.00 86.92  ?  338  THR F OG1 1 
ATOM   17998 C  CG2 . THR F 6  338  ? -24.229 4.168    75.536  1.00 88.27  ?  338  THR F CG2 1 
ATOM   17999 N  N   . ILE F 6  339  ? -27.024 3.631    72.815  1.00 85.18  ?  339  ILE F N   1 
ATOM   18000 C  CA  . ILE F 6  339  ? -27.236 2.564    71.841  1.00 83.55  ?  339  ILE F CA  1 
ATOM   18001 C  C   . ILE F 6  339  ? -27.101 3.106    70.425  1.00 87.95  ?  339  ILE F C   1 
ATOM   18002 O  O   . ILE F 6  339  ? -26.535 2.448    69.543  1.00 94.57  ?  339  ILE F O   1 
ATOM   18003 C  CB  . ILE F 6  339  ? -28.606 1.898    72.068  1.00 81.04  ?  339  ILE F CB  1 
ATOM   18004 C  CG1 . ILE F 6  339  ? -28.680 1.283    73.466  1.00 75.82  ?  339  ILE F CG1 1 
ATOM   18005 C  CG2 . ILE F 6  339  ? -28.882 0.845    71.007  1.00 87.25  ?  339  ILE F CG2 1 
ATOM   18006 C  CD1 . ILE F 6  339  ? -27.477 0.435    73.828  1.00 74.42  ?  339  ILE F CD1 1 
ATOM   18007 N  N   . ALA F 6  340  ? -27.610 4.318    70.188  1.00 76.35  ?  340  ALA F N   1 
ATOM   18008 C  CA  . ALA F 6  340  ? -27.516 4.921    68.862  1.00 75.67  ?  340  ALA F CA  1 
ATOM   18009 C  C   . ALA F 6  340  ? -26.065 5.161    68.464  1.00 83.97  ?  340  ALA F C   1 
ATOM   18010 O  O   . ALA F 6  340  ? -25.708 5.035    67.286  1.00 82.88  ?  340  ALA F O   1 
ATOM   18011 C  CB  . ALA F 6  340  ? -28.308 6.228    68.823  1.00 77.94  ?  340  ALA F CB  1 
ATOM   18012 N  N   . GLY F 6  341  ? -25.213 5.511    69.431  1.00 106.46 ?  341  GLY F N   1 
ATOM   18013 C  CA  . GLY F 6  341  ? -23.800 5.678    69.133  1.00 101.48 ?  341  GLY F CA  1 
ATOM   18014 C  C   . GLY F 6  341  ? -23.135 4.375    68.732  1.00 102.55 ?  341  GLY F C   1 
ATOM   18015 O  O   . GLY F 6  341  ? -22.325 4.340    67.802  1.00 110.71 ?  341  GLY F O   1 
ATOM   18016 N  N   . TRP F 6  342  ? -23.471 3.284    69.428  1.00 96.28  ?  342  TRP F N   1 
ATOM   18017 C  CA  . TRP F 6  342  ? -22.976 1.970    69.030  1.00 102.58 ?  342  TRP F CA  1 
ATOM   18018 C  C   . TRP F 6  342  ? -23.502 1.582    67.656  1.00 104.88 ?  342  TRP F C   1 
ATOM   18019 O  O   . TRP F 6  342  ? -22.764 1.024    66.835  1.00 104.08 ?  342  TRP F O   1 
ATOM   18020 C  CB  . TRP F 6  342  ? -23.372 0.921    70.069  1.00 95.26  ?  342  TRP F CB  1 
ATOM   18021 C  CG  . TRP F 6  342  ? -22.799 -0.437   69.807  1.00 102.26 ?  342  TRP F CG  1 
ATOM   18022 C  CD1 . TRP F 6  342  ? -23.479 -1.546   69.397  1.00 102.69 ?  342  TRP F CD1 1 
ATOM   18023 C  CD2 . TRP F 6  342  ? -21.430 -0.836   69.949  1.00 113.29 ?  342  TRP F CD2 1 
ATOM   18024 N  NE1 . TRP F 6  342  ? -22.620 -2.609   69.271  1.00 108.08 ?  342  TRP F NE1 1 
ATOM   18025 C  CE2 . TRP F 6  342  ? -21.355 -2.199   69.604  1.00 114.99 ?  342  TRP F CE2 1 
ATOM   18026 C  CE3 . TRP F 6  342  ? -20.261 -0.172   70.333  1.00 113.42 ?  342  TRP F CE3 1 
ATOM   18027 C  CZ2 . TRP F 6  342  ? -20.158 -2.911   69.631  1.00 115.66 ?  342  TRP F CZ2 1 
ATOM   18028 C  CZ3 . TRP F 6  342  ? -19.074 -0.880   70.359  1.00 119.92 ?  342  TRP F CZ3 1 
ATOM   18029 C  CH2 . TRP F 6  342  ? -19.031 -2.235   70.010  1.00 116.72 ?  342  TRP F CH2 1 
ATOM   18030 N  N   . ILE F 6  343  ? -24.776 1.876    67.386  1.00 79.73  ?  343  ILE F N   1 
ATOM   18031 C  CA  . ILE F 6  343  ? -25.355 1.575    66.080  1.00 71.83  ?  343  ILE F CA  1 
ATOM   18032 C  C   . ILE F 6  343  ? -24.640 2.360    64.990  1.00 77.45  ?  343  ILE F C   1 
ATOM   18033 O  O   . ILE F 6  343  ? -24.302 1.814    63.932  1.00 76.88  ?  343  ILE F O   1 
ATOM   18034 C  CB  . ILE F 6  343  ? -26.867 1.861    66.090  1.00 63.54  ?  343  ILE F CB  1 
ATOM   18035 C  CG1 . ILE F 6  343  ? -27.592 0.839    66.966  1.00 72.28  ?  343  ILE F CG1 1 
ATOM   18036 C  CG2 . ILE F 6  343  ? -27.424 1.851    64.675  1.00 68.98  ?  343  ILE F CG2 1 
ATOM   18037 C  CD1 . ILE F 6  343  ? -29.091 1.009    66.990  1.00 74.56  ?  343  ILE F CD1 1 
ATOM   18038 N  N   . VAL F 6  344  ? -24.383 3.647    65.237  1.00 86.13  ?  344  VAL F N   1 
ATOM   18039 C  CA  . VAL F 6  344  ? -23.693 4.479    64.253  1.00 90.43  ?  344  VAL F CA  1 
ATOM   18040 C  C   . VAL F 6  344  ? -22.312 3.909    63.953  1.00 92.53  ?  344  VAL F C   1 
ATOM   18041 O  O   . VAL F 6  344  ? -21.897 3.821    62.791  1.00 91.92  ?  344  VAL F O   1 
ATOM   18042 C  CB  . VAL F 6  344  ? -23.612 5.935    64.745  1.00 90.33  ?  344  VAL F CB  1 
ATOM   18043 C  CG1 . VAL F 6  344  ? -22.449 6.662    64.083  1.00 91.72  ?  344  VAL F CG1 1 
ATOM   18044 C  CG2 . VAL F 6  344  ? -24.916 6.656    64.474  1.00 96.30  ?  344  VAL F CG2 1 
ATOM   18045 N  N   . VAL F 6  345  ? -21.586 3.502    64.997  1.00 81.49  ?  345  VAL F N   1 
ATOM   18046 C  CA  . VAL F 6  345  ? -20.267 2.904    64.801  1.00 82.50  ?  345  VAL F CA  1 
ATOM   18047 C  C   . VAL F 6  345  ? -20.376 1.639    63.959  1.00 84.71  ?  345  VAL F C   1 
ATOM   18048 O  O   . VAL F 6  345  ? -19.568 1.407    63.050  1.00 87.13  ?  345  VAL F O   1 
ATOM   18049 C  CB  . VAL F 6  345  ? -19.603 2.626    66.162  1.00 72.91  ?  345  VAL F CB  1 
ATOM   18050 C  CG1 . VAL F 6  345  ? -18.423 1.683    65.996  1.00 63.76  ?  345  VAL F CG1 1 
ATOM   18051 C  CG2 . VAL F 6  345  ? -19.166 3.928    66.813  1.00 70.60  ?  345  VAL F CG2 1 
ATOM   18052 N  N   . MET F 6  346  ? -21.383 0.808    64.240  1.00 116.07 ?  346  MET F N   1 
ATOM   18053 C  CA  . MET F 6  346  ? -21.560 -0.427   63.483  1.00 112.69 ?  346  MET F CA  1 
ATOM   18054 C  C   . MET F 6  346  ? -21.945 -0.142   62.038  1.00 114.06 ?  346  MET F C   1 
ATOM   18055 O  O   . MET F 6  346  ? -21.532 -0.871   61.128  1.00 119.58 ?  346  MET F O   1 
ATOM   18056 C  CB  . MET F 6  346  ? -22.611 -1.311   64.154  1.00 108.94 ?  346  MET F CB  1 
ATOM   18057 C  CG  . MET F 6  346  ? -22.077 -2.131   65.313  1.00 115.41 ?  346  MET F CG  1 
ATOM   18058 S  SD  . MET F 6  346  ? -20.675 -3.147   64.818  1.00 120.80 ?  346  MET F SD  1 
ATOM   18059 C  CE  . MET F 6  346  ? -19.430 -2.593   65.980  1.00 124.15 ?  346  MET F CE  1 
ATOM   18060 N  N   . ARG F 6  347  ? -22.732 0.912    61.803  1.00 81.81  ?  347  ARG F N   1 
ATOM   18061 C  CA  . ARG F 6  347  ? -23.116 1.239    60.433  1.00 82.99  ?  347  ARG F CA  1 
ATOM   18062 C  C   . ARG F 6  347  ? -21.892 1.581    59.597  1.00 81.17  ?  347  ARG F C   1 
ATOM   18063 O  O   . ARG F 6  347  ? -21.817 1.221    58.417  1.00 83.52  ?  347  ARG F O   1 
ATOM   18064 C  CB  . ARG F 6  347  ? -24.111 2.399    60.416  1.00 78.99  ?  347  ARG F CB  1 
ATOM   18065 C  CG  . ARG F 6  347  ? -25.453 2.135    61.099  1.00 80.43  ?  347  ARG F CG  1 
ATOM   18066 C  CD  . ARG F 6  347  ? -26.463 1.365    60.261  1.00 80.96  ?  347  ARG F CD  1 
ATOM   18067 N  NE  . ARG F 6  347  ? -25.937 0.113    59.737  1.00 82.96  ?  347  ARG F NE  1 
ATOM   18068 C  CZ  . ARG F 6  347  ? -25.921 -1.025   60.414  1.00 84.40  ?  347  ARG F CZ  1 
ATOM   18069 N  NH1 . ARG F 6  347  ? -26.403 -1.104   61.644  1.00 94.45  ?  347  ARG F NH1 1 
ATOM   18070 N  NH2 . ARG F 6  347  ? -25.414 -2.112   59.842  1.00 77.79  ?  347  ARG F NH2 1 
ATOM   18071 N  N   . PHE F 6  348  ? -20.915 2.264    60.200  1.00 89.33  ?  348  PHE F N   1 
ATOM   18072 C  CA  . PHE F 6  348  ? -19.672 2.573    59.498  1.00 94.46  ?  348  PHE F CA  1 
ATOM   18073 C  C   . PHE F 6  348  ? -18.945 1.301    59.081  1.00 91.95  ?  348  PHE F C   1 
ATOM   18074 O  O   . PHE F 6  348  ? -18.394 1.225    57.976  1.00 92.23  ?  348  PHE F O   1 
ATOM   18075 C  CB  . PHE F 6  348  ? -18.772 3.432    60.386  1.00 97.24  ?  348  PHE F CB  1 
ATOM   18076 C  CG  . PHE F 6  348  ? -19.048 4.906    60.292  1.00 100.02 ?  348  PHE F CG  1 
ATOM   18077 C  CD1 . PHE F 6  348  ? -20.276 5.420    60.676  1.00 98.74  ?  348  PHE F CD1 1 
ATOM   18078 C  CD2 . PHE F 6  348  ? -18.075 5.780    59.839  1.00 104.84 ?  348  PHE F CD2 1 
ATOM   18079 C  CE1 . PHE F 6  348  ? -20.534 6.775    60.598  1.00 97.72  ?  348  PHE F CE1 1 
ATOM   18080 C  CE2 . PHE F 6  348  ? -18.326 7.137    59.759  1.00 110.97 ?  348  PHE F CE2 1 
ATOM   18081 C  CZ  . PHE F 6  348  ? -19.558 7.634    60.140  1.00 107.11 ?  348  PHE F CZ  1 
ATOM   18082 N  N   . VAL F 6  349  ? -18.932 0.292    59.954  1.00 88.11  ?  349  VAL F N   1 
ATOM   18083 C  CA  . VAL F 6  349  ? -18.248 -0.958   59.641  1.00 92.77  ?  349  VAL F CA  1 
ATOM   18084 C  C   . VAL F 6  349  ? -18.982 -1.709   58.537  1.00 93.08  ?  349  VAL F C   1 
ATOM   18085 O  O   . VAL F 6  349  ? -18.356 -2.328   57.667  1.00 91.12  ?  349  VAL F O   1 
ATOM   18086 C  CB  . VAL F 6  349  ? -18.101 -1.816   60.911  1.00 81.65  ?  349  VAL F CB  1 
ATOM   18087 C  CG1 . VAL F 6  349  ? -17.325 -3.088   60.609  1.00 68.00  ?  349  VAL F CG1 1 
ATOM   18088 C  CG2 . VAL F 6  349  ? -17.420 -1.015   62.012  1.00 77.89  ?  349  VAL F CG2 1 
ATOM   18089 N  N   . ASP F 6  350  ? -20.317 -1.664   58.550  1.00 92.04  ?  350  ASP F N   1 
ATOM   18090 C  CA  . ASP F 6  350  ? -21.095 -2.348   57.521  1.00 88.94  ?  350  ASP F CA  1 
ATOM   18091 C  C   . ASP F 6  350  ? -20.771 -1.802   56.137  1.00 80.65  ?  350  ASP F C   1 
ATOM   18092 O  O   . ASP F 6  350  ? -20.573 -2.565   55.186  1.00 79.66  ?  350  ASP F O   1 
ATOM   18093 C  CB  . ASP F 6  350  ? -22.590 -2.216   57.817  1.00 95.55  ?  350  ASP F CB  1 
ATOM   18094 C  CG  . ASP F 6  350  ? -23.448 -2.993   56.837  1.00 103.49 ?  350  ASP F CG  1 
ATOM   18095 O  OD1 . ASP F 6  350  ? -23.030 -4.096   56.420  1.00 103.97 ?  350  ASP F OD1 1 
ATOM   18096 O  OD2 . ASP F 6  350  ? -24.537 -2.498   56.479  1.00 101.89 -1 350  ASP F OD2 1 
ATOM   18097 N  N   . MET F 6  351  ? -20.705 -0.477   56.009  1.00 96.01  ?  351  MET F N   1 
ATOM   18098 C  CA  . MET F 6  351  ? -20.366 0.121    54.723  1.00 96.88  ?  351  MET F CA  1 
ATOM   18099 C  C   . MET F 6  351  ? -18.939 -0.223   54.323  1.00 97.75  ?  351  MET F C   1 
ATOM   18100 O  O   . MET F 6  351  ? -18.646 -0.422   53.137  1.00 95.98  ?  351  MET F O   1 
ATOM   18101 C  CB  . MET F 6  351  ? -20.560 1.634    54.796  1.00 97.19  ?  351  MET F CB  1 
ATOM   18102 C  CG  . MET F 6  351  ? -21.887 2.025    55.417  1.00 99.18  ?  351  MET F CG  1 
ATOM   18103 S  SD  . MET F 6  351  ? -22.675 3.493    54.740  1.00 119.05 ?  351  MET F SD  1 
ATOM   18104 C  CE  . MET F 6  351  ? -24.170 3.491    55.723  1.00 105.67 ?  351  MET F CE  1 
ATOM   18105 N  N   . ALA F 6  352  ? -18.036 -0.291   55.304  1.00 107.50 ?  352  ALA F N   1 
ATOM   18106 C  CA  . ALA F 6  352  ? -16.677 -0.739   55.028  1.00 106.73 ?  352  ALA F CA  1 
ATOM   18107 C  C   . ALA F 6  352  ? -16.672 -2.165   54.500  1.00 107.21 ?  352  ALA F C   1 
ATOM   18108 O  O   . ALA F 6  352  ? -15.885 -2.501   53.611  1.00 109.77 ?  352  ALA F O   1 
ATOM   18109 C  CB  . ALA F 6  352  ? -15.818 -0.631   56.288  1.00 108.83 ?  352  ALA F CB  1 
ATOM   18110 N  N   . TRP F 6  353  ? -17.552 -3.017   55.031  1.00 89.97  ?  353  TRP F N   1 
ATOM   18111 C  CA  . TRP F 6  353  ? -17.628 -4.397   54.562  1.00 84.19  ?  353  TRP F CA  1 
ATOM   18112 C  C   . TRP F 6  353  ? -18.162 -4.485   53.137  1.00 86.49  ?  353  TRP F C   1 
ATOM   18113 O  O   . TRP F 6  353  ? -17.860 -5.448   52.420  1.00 89.64  ?  353  TRP F O   1 
ATOM   18114 C  CB  . TRP F 6  353  ? -18.499 -5.214   55.520  1.00 77.71  ?  353  TRP F CB  1 
ATOM   18115 C  CG  . TRP F 6  353  ? -18.545 -6.678   55.233  1.00 75.67  ?  353  TRP F CG  1 
ATOM   18116 C  CD1 . TRP F 6  353  ? -17.520 -7.571   55.340  1.00 77.89  ?  353  TRP F CD1 1 
ATOM   18117 C  CD2 . TRP F 6  353  ? -19.694 -7.431   54.831  1.00 68.42  ?  353  TRP F CD2 1 
ATOM   18118 N  NE1 . TRP F 6  353  ? -17.955 -8.831   55.007  1.00 72.87  ?  353  TRP F NE1 1 
ATOM   18119 C  CE2 . TRP F 6  353  ? -19.288 -8.772   54.693  1.00 66.13  ?  353  TRP F CE2 1 
ATOM   18120 C  CE3 . TRP F 6  353  ? -21.026 -7.098   54.565  1.00 65.59  ?  353  TRP F CE3 1 
ATOM   18121 C  CZ2 . TRP F 6  353  ? -20.167 -9.780   54.301  1.00 65.35  ?  353  TRP F CZ2 1 
ATOM   18122 C  CZ3 . TRP F 6  353  ? -21.896 -8.100   54.176  1.00 64.21  ?  353  TRP F CZ3 1 
ATOM   18123 C  CH2 . TRP F 6  353  ? -21.463 -9.424   54.047  1.00 65.32  ?  353  TRP F CH2 1 
ATOM   18124 N  N   . ILE F 6  354  ? -18.943 -3.495   52.703  1.00 81.94  ?  354  ILE F N   1 
ATOM   18125 C  CA  . ILE F 6  354  ? -19.525 -3.547   51.366  1.00 76.56  ?  354  ILE F CA  1 
ATOM   18126 C  C   . ILE F 6  354  ? -18.593 -2.921   50.339  1.00 77.92  ?  354  ILE F C   1 
ATOM   18127 O  O   . ILE F 6  354  ? -18.441 -3.438   49.227  1.00 84.60  ?  354  ILE F O   1 
ATOM   18128 C  CB  . ILE F 6  354  ? -20.908 -2.868   51.359  1.00 77.87  ?  354  ILE F CB  1 
ATOM   18129 C  CG1 . ILE F 6  354  ? -21.839 -3.528   52.380  1.00 81.53  ?  354  ILE F CG1 1 
ATOM   18130 C  CG2 . ILE F 6  354  ? -21.519 -2.907   49.968  1.00 79.43  ?  354  ILE F CG2 1 
ATOM   18131 C  CD1 . ILE F 6  354  ? -23.214 -2.891   52.464  1.00 92.76  ?  354  ILE F CD1 1 
ATOM   18132 N  N   . ILE F 6  355  ? -17.950 -1.812   50.688  1.00 69.89  ?  355  ILE F N   1 
ATOM   18133 C  CA  . ILE F 6  355  ? -17.191 -1.012   49.731  1.00 70.87  ?  355  ILE F CA  1 
ATOM   18134 C  C   . ILE F 6  355  ? -15.701 -1.329   49.773  1.00 73.07  ?  355  ILE F C   1 
ATOM   18135 O  O   . ILE F 6  355  ? -15.077 -1.523   48.731  1.00 75.72  ?  355  ILE F O   1 
ATOM   18136 C  CB  . ILE F 6  355  ? -17.448 0.494    49.968  1.00 64.48  ?  355  ILE F CB  1 
ATOM   18137 C  CG1 . ILE F 6  355  ? -18.933 0.748    50.232  1.00 68.13  ?  355  ILE F CG1 1 
ATOM   18138 C  CG2 . ILE F 6  355  ? -16.970 1.306    48.784  1.00 66.04  ?  355  ILE F CG2 1 
ATOM   18139 C  CD1 . ILE F 6  355  ? -19.804 0.661    48.997  1.00 70.79  ?  355  ILE F CD1 1 
ATOM   18140 N  N   . LEU F 6  356  ? -15.111 -1.380   50.968  1.00 114.50 ?  356  LEU F N   1 
ATOM   18141 C  CA  . LEU F 6  356  ? -13.657 -1.497   51.068  1.00 119.38 ?  356  LEU F CA  1 
ATOM   18142 C  C   . LEU F 6  356  ? -13.073 -2.774   50.467  1.00 124.41 ?  356  LEU F C   1 
ATOM   18143 O  O   . LEU F 6  356  ? -11.964 -2.695   49.910  1.00 129.62 ?  356  LEU F O   1 
ATOM   18144 C  CB  . LEU F 6  356  ? -13.221 -1.353   52.532  1.00 120.03 ?  356  LEU F CB  1 
ATOM   18145 C  CG  . LEU F 6  356  ? -13.391 0.028    53.171  1.00 120.76 ?  356  LEU F CG  1 
ATOM   18146 C  CD1 . LEU F 6  356  ? -12.736 0.067    54.543  1.00 112.80 ?  356  LEU F CD1 1 
ATOM   18147 C  CD2 . LEU F 6  356  ? -12.817 1.109    52.269  1.00 126.63 ?  356  LEU F CD2 1 
ATOM   18148 N  N   . PRO F 6  357  ? -13.708 -3.955   50.552  1.00 89.81  ?  357  PRO F N   1 
ATOM   18149 C  CA  . PRO F 6  357  ? -13.093 -5.146   49.941  1.00 90.60  ?  357  PRO F CA  1 
ATOM   18150 C  C   . PRO F 6  357  ? -12.778 -4.994   48.468  1.00 89.53  ?  357  PRO F C   1 
ATOM   18151 O  O   . PRO F 6  357  ? -11.842 -5.639   47.977  1.00 92.31  ?  357  PRO F O   1 
ATOM   18152 C  CB  . PRO F 6  357  ? -14.152 -6.230   50.179  1.00 77.64  ?  357  PRO F CB  1 
ATOM   18153 C  CG  . PRO F 6  357  ? -14.731 -5.840   51.484  1.00 79.41  ?  357  PRO F CG  1 
ATOM   18154 C  CD  . PRO F 6  357  ? -14.877 -4.340   51.366  1.00 82.69  ?  357  PRO F CD  1 
ATOM   18155 N  N   . GLU F 6  358  ? -13.527 -4.156   47.748  1.00 97.32  ?  358  GLU F N   1 
ATOM   18156 C  CA  . GLU F 6  358  ? -13.289 -3.988   46.319  1.00 103.20 ?  358  GLU F CA  1 
ATOM   18157 C  C   . GLU F 6  358  ? -11.915 -3.386   46.059  1.00 108.24 ?  358  GLU F C   1 
ATOM   18158 O  O   . GLU F 6  358  ? -11.252 -3.733   45.074  1.00 111.39 ?  358  GLU F O   1 
ATOM   18159 C  CB  . GLU F 6  358  ? -14.388 -3.117   45.707  1.00 101.44 ?  358  GLU F CB  1 
ATOM   18160 C  CG  . GLU F 6  358  ? -15.788 -3.701   45.842  1.00 101.42 ?  358  GLU F CG  1 
ATOM   18161 C  CD  . GLU F 6  358  ? -16.173 -4.589   44.676  1.00 109.61 ?  358  GLU F CD  1 
ATOM   18162 O  OE1 . GLU F 6  358  ? -15.403 -4.650   43.694  1.00 108.70 ?  358  GLU F OE1 1 
ATOM   18163 O  OE2 . GLU F 6  358  ? -17.252 -5.218   44.742  1.00 103.25 -1 358  GLU F OE2 1 
ATOM   18164 N  N   . PHE F 6  359  ? -11.465 -2.491   46.938  1.00 103.75 ?  359  PHE F N   1 
ATOM   18165 C  CA  . PHE F 6  359  ? -10.160 -1.857   46.787  1.00 105.97 ?  359  PHE F CA  1 
ATOM   18166 C  C   . PHE F 6  359  ? -9.088  -2.623   47.551  1.00 107.64 ?  359  PHE F C   1 
ATOM   18167 O  O   . PHE F 6  359  ? -8.136  -3.138   46.957  1.00 112.29 ?  359  PHE F O   1 
ATOM   18168 C  CB  . PHE F 6  359  ? -10.188 -0.408   47.292  1.00 105.47 ?  359  PHE F CB  1 
ATOM   18169 C  CG  . PHE F 6  359  ? -11.516 0.270    47.157  1.00 103.02 ?  359  PHE F CG  1 
ATOM   18170 C  CD1 . PHE F 6  359  ? -12.157 0.356    45.935  1.00 106.05 ?  359  PHE F CD1 1 
ATOM   18171 C  CD2 . PHE F 6  359  ? -12.120 0.833    48.269  1.00 100.48 ?  359  PHE F CD2 1 
ATOM   18172 C  CE1 . PHE F 6  359  ? -13.382 0.992    45.825  1.00 97.40  ?  359  PHE F CE1 1 
ATOM   18173 C  CE2 . PHE F 6  359  ? -13.341 1.466    48.166  1.00 102.25 ?  359  PHE F CE2 1 
ATOM   18174 C  CZ  . PHE F 6  359  ? -13.974 1.548    46.944  1.00 94.64  ?  359  PHE F CZ  1 
ATOM   18175 N  N   . ARG F 6  360  ? -9.250  -2.711   48.874  1.00 132.67 ?  360  ARG F N   1 
ATOM   18176 C  CA  . ARG F 6  360  ? -8.186  -3.206   49.738  1.00 137.50 ?  360  ARG F CA  1 
ATOM   18177 C  C   . ARG F 6  360  ? -7.933  -4.693   49.528  1.00 144.07 ?  360  ARG F C   1 
ATOM   18178 O  O   . ARG F 6  360  ? -6.776  -5.134   49.531  1.00 150.17 ?  360  ARG F O   1 
ATOM   18179 C  CB  . ARG F 6  360  ? -8.529  -2.909   51.200  1.00 136.85 ?  360  ARG F CB  1 
ATOM   18180 C  CG  . ARG F 6  360  ? -8.787  -1.428   51.486  1.00 139.22 ?  360  ARG F CG  1 
ATOM   18181 C  CD  . ARG F 6  360  ? -7.515  -0.596   51.291  1.00 143.56 ?  360  ARG F CD  1 
ATOM   18182 N  NE  . ARG F 6  360  ? -7.292  -0.152   49.918  1.00 142.83 ?  360  ARG F NE  1 
ATOM   18183 C  CZ  . ARG F 6  360  ? -7.597  1.054    49.455  1.00 143.15 ?  360  ARG F CZ  1 
ATOM   18184 N  NH1 . ARG F 6  360  ? -8.164  1.967    50.226  1.00 141.68 ?  360  ARG F NH1 1 
ATOM   18185 N  NH2 . ARG F 6  360  ? -7.327  1.350    48.186  1.00 145.73 ?  360  ARG F NH2 1 
ATOM   18186 N  N   . GLU F 6  361  ? -8.994  -5.485   49.366  1.00 137.03 ?  361  GLU F N   1 
ATOM   18187 C  CA  . GLU F 6  361  ? -8.928  -6.924   49.117  1.00 141.33 ?  361  GLU F CA  1 
ATOM   18188 C  C   . GLU F 6  361  ? -8.314  -7.679   50.299  1.00 136.13 ?  361  GLU F C   1 
ATOM   18189 O  O   . GLU F 6  361  ? -8.266  -8.915   50.278  1.00 135.08 ?  361  GLU F O   1 
ATOM   18190 C  CB  . GLU F 6  361  ? -8.164  -7.229   47.814  1.00 147.93 ?  361  GLU F CB  1 
ATOM   18191 C  CG  . GLU F 6  361  ? -8.273  -8.645   47.272  1.00 151.58 ?  361  GLU F CG  1 
ATOM   18192 C  CD  . GLU F 6  361  ? -6.918  -9.322   47.169  1.00 152.43 ?  361  GLU F CD  1 
ATOM   18193 O  OE1 . GLU F 6  361  ? -5.893  -8.626   47.329  1.00 151.27 ?  361  GLU F OE1 1 
ATOM   18194 O  OE2 . GLU F 6  361  ? -6.877  -10.545  46.920  1.00 155.14 -1 361  GLU F OE2 1 
ATOM   18195 N  N   . HIS F 6  362  ? -7.872  -6.976   51.340  1.00 130.52 ?  362  HIS F N   1 
ATOM   18196 C  CA  . HIS F 6  362  ? -7.366  -7.575   52.565  1.00 124.26 ?  362  HIS F CA  1 
ATOM   18197 C  C   . HIS F 6  362  ? -7.796  -6.700   53.730  1.00 124.38 ?  362  HIS F C   1 
ATOM   18198 O  O   . HIS F 6  362  ? -7.912  -5.480   53.590  1.00 130.10 ?  362  HIS F O   1 
ATOM   18199 C  CB  . HIS F 6  362  ? -5.835  -7.697   52.557  1.00 128.70 ?  362  HIS F CB  1 
ATOM   18200 C  CG  . HIS F 6  362  ? -5.312  -8.763   51.647  1.00 133.46 ?  362  HIS F CG  1 
ATOM   18201 N  ND1 . HIS F 6  362  ? -5.068  -10.051  52.072  1.00 124.72 ?  362  HIS F ND1 1 
ATOM   18202 C  CD2 . HIS F 6  362  ? -4.978  -8.729   50.335  1.00 138.97 ?  362  HIS F CD2 1 
ATOM   18203 C  CE1 . HIS F 6  362  ? -4.612  -10.766  51.059  1.00 131.55 ?  362  HIS F CE1 1 
ATOM   18204 N  NE2 . HIS F 6  362  ? -4.548  -9.988   49.994  1.00 135.16 ?  362  HIS F NE2 1 
ATOM   18205 N  N   . LEU F 6  363  ? -8.033  -7.324   54.886  1.00 83.87  ?  363  LEU F N   1 
ATOM   18206 C  CA  . LEU F 6  363  ? -8.348  -6.537   56.075  1.00 78.70  ?  363  LEU F CA  1 
ATOM   18207 C  C   . LEU F 6  363  ? -7.153  -5.693   56.504  1.00 83.77  ?  363  LEU F C   1 
ATOM   18208 O  O   . LEU F 6  363  ? -7.314  -4.537   56.912  1.00 88.62  ?  363  LEU F O   1 
ATOM   18209 C  CB  . LEU F 6  363  ? -8.801  -7.447   57.217  1.00 73.49  ?  363  LEU F CB  1 
ATOM   18210 C  CG  . LEU F 6  363  ? -9.706  -6.775   58.255  1.00 70.20  ?  363  LEU F CG  1 
ATOM   18211 C  CD1 . LEU F 6  363  ? -10.812 -5.971   57.582  1.00 67.26  ?  363  LEU F CD1 1 
ATOM   18212 C  CD2 . LEU F 6  363  ? -10.291 -7.797   59.213  1.00 72.53  ?  363  LEU F CD2 1 
ATOM   18213 N  N   . TRP F 6  364  ? -5.942  -6.250   56.407  1.00 128.03 ?  364  TRP F N   1 
ATOM   18214 C  CA  . TRP F 6  364  ? -4.754  -5.487   56.774  1.00 129.74 ?  364  TRP F CA  1 
ATOM   18215 C  C   . TRP F 6  364  ? -4.445  -4.399   55.754  1.00 132.72 ?  364  TRP F C   1 
ATOM   18216 O  O   . TRP F 6  364  ? -3.888  -3.355   56.116  1.00 138.70 ?  364  TRP F O   1 
ATOM   18217 C  CB  . TRP F 6  364  ? -3.551  -6.417   56.933  1.00 133.76 ?  364  TRP F CB  1 
ATOM   18218 C  CG  . TRP F 6  364  ? -3.590  -7.642   56.069  1.00 140.51 ?  364  TRP F CG  1 
ATOM   18219 C  CD1 . TRP F 6  364  ? -2.972  -7.814   54.865  1.00 144.27 ?  364  TRP F CD1 1 
ATOM   18220 C  CD2 . TRP F 6  364  ? -4.238  -8.884   56.370  1.00 137.85 ?  364  TRP F CD2 1 
ATOM   18221 N  NE1 . TRP F 6  364  ? -3.218  -9.078   54.383  1.00 144.69 ?  364  TRP F NE1 1 
ATOM   18222 C  CE2 . TRP F 6  364  ? -3.991  -9.756   55.290  1.00 140.67 ?  364  TRP F CE2 1 
ATOM   18223 C  CE3 . TRP F 6  364  ? -5.012  -9.339   57.441  1.00 133.92 ?  364  TRP F CE3 1 
ATOM   18224 C  CZ2 . TRP F 6  364  ? -4.490  -11.057  55.252  1.00 136.82 ?  364  TRP F CZ2 1 
ATOM   18225 C  CZ3 . TRP F 6  364  ? -5.506  -10.628  57.402  1.00 137.27 ?  364  TRP F CZ3 1 
ATOM   18226 C  CH2 . TRP F 6  364  ? -5.244  -11.473  56.316  1.00 141.89 ?  364  TRP F CH2 1 
ATOM   18227 N  N   . ASP F 6  365  ? -4.800  -4.614   54.484  1.00 133.66 ?  365  ASP F N   1 
ATOM   18228 C  CA  . ASP F 6  365  ? -4.543  -3.610   53.457  1.00 136.10 ?  365  ASP F CA  1 
ATOM   18229 C  C   . ASP F 6  365  ? -5.346  -2.330   53.654  1.00 133.93 ?  365  ASP F C   1 
ATOM   18230 O  O   . ASP F 6  365  ? -5.031  -1.326   53.007  1.00 130.46 ?  365  ASP F O   1 
ATOM   18231 C  CB  . ASP F 6  365  ? -4.821  -4.187   52.067  1.00 135.55 ?  365  ASP F CB  1 
ATOM   18232 C  CG  . ASP F 6  365  ? -3.632  -4.932   51.499  1.00 140.82 ?  365  ASP F CG  1 
ATOM   18233 O  OD1 . ASP F 6  365  ? -2.651  -5.145   52.244  1.00 141.39 ?  365  ASP F OD1 1 
ATOM   18234 O  OD2 . ASP F 6  365  ? -3.680  -5.293   50.303  1.00 150.22 -1 365  ASP F OD2 1 
ATOM   18235 N  N   . ILE F 6  366  ? -6.359  -2.337   54.526  1.00 95.54  ?  366  ILE F N   1 
ATOM   18236 C  CA  . ILE F 6  366  ? -7.080  -1.111   54.854  1.00 89.40  ?  366  ILE F CA  1 
ATOM   18237 C  C   . ILE F 6  366  ? -6.095  -0.067   55.351  1.00 85.51  ?  366  ILE F C   1 
ATOM   18238 O  O   . ILE F 6  366  ? -5.311  -0.324   56.270  1.00 84.45  ?  366  ILE F O   1 
ATOM   18239 C  CB  . ILE F 6  366  ? -8.170  -1.395   55.904  1.00 91.66  ?  366  ILE F CB  1 
ATOM   18240 C  CG1 . ILE F 6  366  ? -9.287  -2.255   55.312  1.00 88.50  ?  366  ILE F CG1 1 
ATOM   18241 C  CG2 . ILE F 6  366  ? -8.740  -0.102   56.459  1.00 88.93  ?  366  ILE F CG2 1 
ATOM   18242 C  CD1 . ILE F 6  366  ? -10.447 -2.482   56.262  1.00 71.77  ?  366  ILE F CD1 1 
ATOM   18243 N  N   . ALA F 6  367  ? -6.134  1.115    54.745  1.00 132.63 ?  367  ALA F N   1 
ATOM   18244 C  CA  . ALA F 6  367  ? -5.200  2.182    55.061  1.00 141.59 ?  367  ALA F CA  1 
ATOM   18245 C  C   . ALA F 6  367  ? -5.838  3.172    56.031  1.00 143.88 ?  367  ALA F C   1 
ATOM   18246 O  O   . ALA F 6  367  ? -6.982  3.012    56.471  1.00 138.99 ?  367  ALA F O   1 
ATOM   18247 C  CB  . ALA F 6  367  ? -4.733  2.878    53.780  1.00 144.89 ?  367  ALA F CB  1 
ATOM   18248 N  N   . ILE F 6  368  ? -5.073  4.211    56.372  1.00 120.75 ?  368  ILE F N   1 
ATOM   18249 C  CA  . ILE F 6  368  ? -5.569  5.216    57.301  1.00 114.39 ?  368  ILE F CA  1 
ATOM   18250 C  C   . ILE F 6  368  ? -6.578  6.123    56.607  1.00 110.49 ?  368  ILE F C   1 
ATOM   18251 O  O   . ILE F 6  368  ? -7.455  6.703    57.260  1.00 109.44 ?  368  ILE F O   1 
ATOM   18252 C  CB  . ILE F 6  368  ? -4.389  6.011    57.900  1.00 116.23 ?  368  ILE F CB  1 
ATOM   18253 C  CG1 . ILE F 6  368  ? -4.861  6.933    59.030  1.00 122.64 ?  368  ILE F CG1 1 
ATOM   18254 C  CG2 . ILE F 6  368  ? -3.651  6.785    56.821  1.00 115.15 ?  368  ILE F CG2 1 
ATOM   18255 C  CD1 . ILE F 6  368  ? -5.632  6.218    60.116  1.00 119.62 ?  368  ILE F CD1 1 
ATOM   18256 N  N   . THR F 6  369  ? -6.482  6.260    55.280  1.00 101.71 ?  369  THR F N   1 
ATOM   18257 C  CA  . THR F 6  369  ? -7.428  7.106    54.561  1.00 106.50 ?  369  THR F CA  1 
ATOM   18258 C  C   . THR F 6  369  ? -8.828  6.504    54.554  1.00 105.24 ?  369  THR F C   1 
ATOM   18259 O  O   . THR F 6  369  ? -9.817  7.242    54.477  1.00 102.40 ?  369  THR F O   1 
ATOM   18260 C  CB  . THR F 6  369  ? -6.941  7.344    53.133  1.00 109.89 ?  369  THR F CB  1 
ATOM   18261 O  OG1 . THR F 6  369  ? -6.872  6.096    52.432  1.00 116.12 ?  369  THR F OG1 1 
ATOM   18262 C  CG2 . THR F 6  369  ? -5.559  7.990    53.154  1.00 120.68 ?  369  THR F CG2 1 
ATOM   18263 N  N   . ASP F 6  370  ? -8.936  5.175    54.652  1.00 147.75 ?  370  ASP F N   1 
ATOM   18264 C  CA  . ASP F 6  370  ? -10.250 4.541    54.716  1.00 146.27 ?  370  ASP F CA  1 
ATOM   18265 C  C   . ASP F 6  370  ? -10.986 4.909    55.998  1.00 140.73 ?  370  ASP F C   1 
ATOM   18266 O  O   . ASP F 6  370  ? -12.219 4.850    56.042  1.00 141.88 ?  370  ASP F O   1 
ATOM   18267 C  CB  . ASP F 6  370  ? -10.109 3.024    54.602  1.00 149.07 ?  370  ASP F CB  1 
ATOM   18268 C  CG  . ASP F 6  370  ? -9.596  2.590    53.245  1.00 148.08 ?  370  ASP F CG  1 
ATOM   18269 O  OD1 . ASP F 6  370  ? -9.621  3.415    52.309  1.00 137.95 ?  370  ASP F OD1 1 
ATOM   18270 O  OD2 . ASP F 6  370  ? -9.165  1.425    53.115  1.00 153.70 -1 370  ASP F OD2 1 
ATOM   18271 N  N   . VAL F 6  371  ? -10.253 5.278    57.045  1.00 102.09 ?  371  VAL F N   1 
ATOM   18272 C  CA  . VAL F 6  371  ? -10.874 5.791    58.259  1.00 101.52 ?  371  VAL F CA  1 
ATOM   18273 C  C   . VAL F 6  371  ? -10.994 7.312    58.211  1.00 98.05  ?  371  VAL F C   1 
ATOM   18274 O  O   . VAL F 6  371  ? -11.895 7.884    58.835  1.00 98.93  ?  371  VAL F O   1 
ATOM   18275 C  CB  . VAL F 6  371  ? -10.073 5.330    59.491  1.00 96.27  ?  371  VAL F CB  1 
ATOM   18276 C  CG1 . VAL F 6  371  ? -10.727 5.806    60.781  1.00 93.29  ?  371  VAL F CG1 1 
ATOM   18277 C  CG2 . VAL F 6  371  ? -9.920  3.815    59.491  1.00 98.01  ?  371  VAL F CG2 1 
ATOM   18278 N  N   . ALA F 6  372  ? -10.116 7.977    57.460  1.00 86.93  ?  372  ALA F N   1 
ATOM   18279 C  CA  . ALA F 6  372  ? -10.110 9.435    57.423  1.00 91.53  ?  372  ALA F CA  1 
ATOM   18280 C  C   . ALA F 6  372  ? -11.314 9.980    56.664  1.00 91.25  ?  372  ALA F C   1 
ATOM   18281 O  O   . ALA F 6  372  ? -12.014 10.874   57.153  1.00 91.66  ?  372  ALA F O   1 
ATOM   18282 C  CB  . ALA F 6  372  ? -8.811  9.929    56.788  1.00 101.30 ?  372  ALA F CB  1 
ATOM   18283 N  N   . ALA F 6  373  ? -11.563 9.457    55.464  1.00 118.52 ?  373  ALA F N   1 
ATOM   18284 C  CA  . ALA F 6  373  ? -12.617 10.009   54.615  1.00 118.24 ?  373  ALA F CA  1 
ATOM   18285 C  C   . ALA F 6  373  ? -14.009 9.967    55.240  1.00 120.19 ?  373  ALA F C   1 
ATOM   18286 O  O   . ALA F 6  373  ? -14.731 10.972   55.120  1.00 119.32 ?  373  ALA F O   1 
ATOM   18287 C  CB  . ALA F 6  373  ? -12.611 9.293    53.258  1.00 116.79 ?  373  ALA F CB  1 
ATOM   18288 N  N   . PRO F 6  374  ? -14.457 8.880    55.885  1.00 122.28 ?  374  PRO F N   1 
ATOM   18289 C  CA  . PRO F 6  374  ? -15.796 8.923    56.501  1.00 117.60 ?  374  PRO F CA  1 
ATOM   18290 C  C   . PRO F 6  374  ? -15.932 10.000   57.563  1.00 124.94 ?  374  PRO F C   1 
ATOM   18291 O  O   . PRO F 6  374  ? -16.908 10.761   57.549  1.00 125.90 ?  374  PRO F O   1 
ATOM   18292 C  CB  . PRO F 6  374  ? -15.957 7.511    57.086  1.00 112.98 ?  374  PRO F CB  1 
ATOM   18293 C  CG  . PRO F 6  374  ? -14.577 6.972    57.193  1.00 114.48 ?  374  PRO F CG  1 
ATOM   18294 C  CD  . PRO F 6  374  ? -13.845 7.548    56.029  1.00 118.38 ?  374  PRO F CD  1 
ATOM   18295 N  N   . ILE F 6  375  ? -14.973 10.089   58.485  1.00 112.52 ?  375  ILE F N   1 
ATOM   18296 C  CA  . ILE F 6  375  ? -15.035 11.115   59.522  1.00 105.57 ?  375  ILE F CA  1 
ATOM   18297 C  C   . ILE F 6  375  ? -14.860 12.501   58.915  1.00 104.92 ?  375  ILE F C   1 
ATOM   18298 O  O   . ILE F 6  375  ? -15.495 13.468   59.351  1.00 105.73 ?  375  ILE F O   1 
ATOM   18299 C  CB  . ILE F 6  375  ? -13.984 10.836   60.611  1.00 108.96 ?  375  ILE F CB  1 
ATOM   18300 C  CG1 . ILE F 6  375  ? -14.172 9.431    61.187  1.00 106.47 ?  375  ILE F CG1 1 
ATOM   18301 C  CG2 . ILE F 6  375  ? -14.066 11.881   61.714  1.00 107.03 ?  375  ILE F CG2 1 
ATOM   18302 C  CD1 . ILE F 6  375  ? -15.560 9.175    61.733  1.00 101.24 ?  375  ILE F CD1 1 
ATOM   18303 N  N   . GLY F 6  376  ? -14.006 12.619   57.897  1.00 78.45  ?  376  GLY F N   1 
ATOM   18304 C  CA  . GLY F 6  376  ? -13.743 13.925   57.314  1.00 82.31  ?  376  GLY F CA  1 
ATOM   18305 C  C   . GLY F 6  376  ? -14.953 14.516   56.617  1.00 80.49  ?  376  GLY F C   1 
ATOM   18306 O  O   . GLY F 6  376  ? -15.173 15.729   56.656  1.00 85.55  ?  376  GLY F O   1 
ATOM   18307 N  N   . LEU F 6  377  ? -15.755 13.671   55.971  1.00 99.64  ?  377  LEU F N   1 
ATOM   18308 C  CA  . LEU F 6  377  ? -16.941 14.148   55.271  1.00 96.93  ?  377  LEU F CA  1 
ATOM   18309 C  C   . LEU F 6  377  ? -18.162 14.248   56.173  1.00 100.73 ?  377  LEU F C   1 
ATOM   18310 O  O   . LEU F 6  377  ? -18.992 15.144   55.977  1.00 102.27 ?  377  LEU F O   1 
ATOM   18311 C  CB  . LEU F 6  377  ? -17.253 13.239   54.079  1.00 97.85  ?  377  LEU F CB  1 
ATOM   18312 C  CG  . LEU F 6  377  ? -16.252 13.319   52.924  1.00 92.01  ?  377  LEU F CG  1 
ATOM   18313 C  CD1 . LEU F 6  377  ? -16.686 12.435   51.769  1.00 85.04  ?  377  LEU F CD1 1 
ATOM   18314 C  CD2 . LEU F 6  377  ? -16.082 14.760   52.467  1.00 98.61  ?  377  LEU F CD2 1 
ATOM   18315 N  N   . ILE F 6  378  ? -18.298 13.356   57.158  1.00 114.32 ?  378  ILE F N   1 
ATOM   18316 C  CA  . ILE F 6  378  ? -19.417 13.473   58.086  1.00 111.34 ?  378  ILE F CA  1 
ATOM   18317 C  C   . ILE F 6  378  ? -19.245 14.701   58.971  1.00 115.59 ?  378  ILE F C   1 
ATOM   18318 O  O   . ILE F 6  378  ? -20.230 15.263   59.464  1.00 117.14 ?  378  ILE F O   1 
ATOM   18319 C  CB  . ILE F 6  378  ? -19.577 12.186   58.919  1.00 101.35 ?  378  ILE F CB  1 
ATOM   18320 C  CG1 . ILE F 6  378  ? -20.965 12.131   59.558  1.00 103.66 ?  378  ILE F CG1 1 
ATOM   18321 C  CG2 . ILE F 6  378  ? -18.507 12.096   59.995  1.00 98.33  ?  378  ILE F CG2 1 
ATOM   18322 C  CD1 . ILE F 6  378  ? -21.325 10.773   60.118  1.00 94.87  ?  378  ILE F CD1 1 
ATOM   18323 N  N   . GLY F 6  379  ? -18.004 15.148   59.176  1.00 117.35 ?  379  GLY F N   1 
ATOM   18324 C  CA  . GLY F 6  379  ? -17.787 16.375   59.924  1.00 115.35 ?  379  GLY F CA  1 
ATOM   18325 C  C   . GLY F 6  379  ? -18.342 17.590   59.209  1.00 114.74 ?  379  GLY F C   1 
ATOM   18326 O  O   . GLY F 6  379  ? -18.928 18.478   59.834  1.00 127.19 ?  379  GLY F O   1 
ATOM   18327 N  N   . LEU F 6  380  ? -18.168 17.645   57.886  1.00 84.89  ?  380  LEU F N   1 
ATOM   18328 C  CA  . LEU F 6  380  ? -18.786 18.710   57.103  1.00 88.22  ?  380  LEU F CA  1 
ATOM   18329 C  C   . LEU F 6  380  ? -20.304 18.583   57.108  1.00 88.99  ?  380  LEU F C   1 
ATOM   18330 O  O   . LEU F 6  380  ? -21.017 19.593   57.095  1.00 98.15  ?  380  LEU F O   1 
ATOM   18331 C  CB  . LEU F 6  380  ? -18.255 18.689   55.669  1.00 77.54  ?  380  LEU F CB  1 
ATOM   18332 C  CG  . LEU F 6  380  ? -16.835 19.210   55.438  1.00 77.90  ?  380  LEU F CG  1 
ATOM   18333 C  CD1 . LEU F 6  380  ? -16.513 19.226   53.953  1.00 81.81  ?  380  LEU F CD1 1 
ATOM   18334 C  CD2 . LEU F 6  380  ? -16.664 20.593   56.044  1.00 100.63 ?  380  LEU F CD2 1 
ATOM   18335 N  N   . VAL F 6  381  ? -20.815 17.350   57.127  1.00 79.47  ?  381  VAL F N   1 
ATOM   18336 C  CA  . VAL F 6  381  ? -22.260 17.145   57.147  1.00 83.52  ?  381  VAL F CA  1 
ATOM   18337 C  C   . VAL F 6  381  ? -22.846 17.616   58.472  1.00 85.04  ?  381  VAL F C   1 
ATOM   18338 O  O   . VAL F 6  381  ? -23.907 18.251   58.508  1.00 94.44  ?  381  VAL F O   1 
ATOM   18339 C  CB  . VAL F 6  381  ? -22.593 15.667   56.871  1.00 80.72  ?  381  VAL F CB  1 
ATOM   18340 C  CG1 . VAL F 6  381  ? -24.073 15.394   57.106  1.00 77.58  ?  381  VAL F CG1 1 
ATOM   18341 C  CG2 . VAL F 6  381  ? -22.197 15.288   55.452  1.00 78.93  ?  381  VAL F CG2 1 
ATOM   18342 N  N   . ILE F 6  382  ? -22.163 17.322   59.580  1.00 97.84  ?  382  ILE F N   1 
ATOM   18343 C  CA  . ILE F 6  382  ? -22.662 17.735   60.886  1.00 103.41 ?  382  ILE F CA  1 
ATOM   18344 C  C   . ILE F 6  382  ? -22.590 19.250   61.029  1.00 105.51 ?  382  ILE F C   1 
ATOM   18345 O  O   . ILE F 6  382  ? -23.495 19.879   61.590  1.00 107.29 ?  382  ILE F O   1 
ATOM   18346 C  CB  . ILE F 6  382  ? -21.884 17.021   62.007  1.00 102.87 ?  382  ILE F CB  1 
ATOM   18347 C  CG1 . ILE F 6  382  ? -22.101 15.509   61.934  1.00 98.22  ?  382  ILE F CG1 1 
ATOM   18348 C  CG2 . ILE F 6  382  ? -22.303 17.545   63.374  1.00 93.37  ?  382  ILE F CG2 1 
ATOM   18349 C  CD1 . ILE F 6  382  ? -23.533 15.104   61.702  1.00 98.87  ?  382  ILE F CD1 1 
ATOM   18350 N  N   . ALA F 6  383  ? -21.518 19.860   60.517  1.00 84.76  ?  383  ALA F N   1 
ATOM   18351 C  CA  . ALA F 6  383  ? -21.369 21.308   60.612  1.00 85.66  ?  383  ALA F CA  1 
ATOM   18352 C  C   . ALA F 6  383  ? -22.468 22.024   59.837  1.00 88.24  ?  383  ALA F C   1 
ATOM   18353 O  O   . ALA F 6  383  ? -23.062 22.991   60.329  1.00 107.56 ?  383  ALA F O   1 
ATOM   18354 C  CB  . ALA F 6  383  ? -19.988 21.727   60.108  1.00 86.68  ?  383  ALA F CB  1 
ATOM   18355 N  N   . LEU F 6  384  ? -22.756 21.561   58.619  1.00 96.11  ?  384  LEU F N   1 
ATOM   18356 C  CA  . LEU F 6  384  ? -23.839 22.156   57.844  1.00 102.98 ?  384  LEU F CA  1 
ATOM   18357 C  C   . LEU F 6  384  ? -25.198 21.869   58.470  1.00 108.32 ?  384  LEU F C   1 
ATOM   18358 O  O   . LEU F 6  384  ? -26.106 22.703   58.385  1.00 108.86 ?  384  LEU F O   1 
ATOM   18359 C  CB  . LEU F 6  384  ? -23.798 21.645   56.404  1.00 100.94 ?  384  LEU F CB  1 
ATOM   18360 C  CG  . LEU F 6  384  ? -22.538 21.986   55.607  1.00 110.01 ?  384  LEU F CG  1 
ATOM   18361 C  CD1 . LEU F 6  384  ? -22.585 21.336   54.234  1.00 118.84 ?  384  LEU F CD1 1 
ATOM   18362 C  CD2 . LEU F 6  384  ? -22.359 23.492   55.490  1.00 102.69 ?  384  LEU F CD2 1 
ATOM   18363 N  N   . PHE F 6  385  ? -25.355 20.701   59.098  1.00 116.78 ?  385  PHE F N   1 
ATOM   18364 C  CA  . PHE F 6  385  ? -26.606 20.392   59.783  1.00 118.35 ?  385  PHE F CA  1 
ATOM   18365 C  C   . PHE F 6  385  ? -26.813 21.304   60.985  1.00 126.45 ?  385  PHE F C   1 
ATOM   18366 O  O   . PHE F 6  385  ? -27.938 21.745   61.252  1.00 131.18 ?  385  PHE F O   1 
ATOM   18367 C  CB  . PHE F 6  385  ? -26.619 18.922   60.208  1.00 112.25 ?  385  PHE F CB  1 
ATOM   18368 C  CG  . PHE F 6  385  ? -27.649 18.598   61.256  1.00 113.96 ?  385  PHE F CG  1 
ATOM   18369 C  CD1 . PHE F 6  385  ? -28.956 18.310   60.896  1.00 107.26 ?  385  PHE F CD1 1 
ATOM   18370 C  CD2 . PHE F 6  385  ? -27.308 18.564   62.600  1.00 116.50 ?  385  PHE F CD2 1 
ATOM   18371 C  CE1 . PHE F 6  385  ? -29.904 18.008   61.855  1.00 108.89 ?  385  PHE F CE1 1 
ATOM   18372 C  CE2 . PHE F 6  385  ? -28.253 18.265   63.563  1.00 113.21 ?  385  PHE F CE2 1 
ATOM   18373 C  CZ  . PHE F 6  385  ? -29.552 17.984   63.189  1.00 112.08 ?  385  PHE F CZ  1 
ATOM   18374 N  N   . ALA F 6  386  ? -25.740 21.598   61.723  1.00 142.49 ?  386  ALA F N   1 
ATOM   18375 C  CA  . ALA F 6  386  ? -25.861 22.467   62.889  1.00 141.58 ?  386  ALA F CA  1 
ATOM   18376 C  C   . ALA F 6  386  ? -26.142 23.907   62.480  1.00 145.50 ?  386  ALA F C   1 
ATOM   18377 O  O   . ALA F 6  386  ? -26.862 24.628   63.180  1.00 154.80 ?  386  ALA F O   1 
ATOM   18378 C  CB  . ALA F 6  386  ? -24.595 22.385   63.739  1.00 145.47 ?  386  ALA F CB  1 
ATOM   18379 N  N   . ALA F 6  387  ? -25.581 24.346   61.351  1.00 104.78 ?  387  ALA F N   1 
ATOM   18380 C  CA  . ALA F 6  387  ? -25.860 25.694   60.867  1.00 101.84 ?  387  ALA F CA  1 
ATOM   18381 C  C   . ALA F 6  387  ? -27.299 25.818   60.383  1.00 105.55 ?  387  ALA F C   1 
ATOM   18382 O  O   . ALA F 6  387  ? -27.951 26.845   60.608  1.00 106.27 ?  387  ALA F O   1 
ATOM   18383 C  CB  . ALA F 6  387  ? -24.884 26.065   59.751  1.00 99.57  ?  387  ALA F CB  1 
ATOM   18384 N  N   . ASN F 6  388  ? -27.814 24.780   59.720  1.00 144.86 ?  388  ASN F N   1 
ATOM   18385 C  CA  . ASN F 6  388  ? -29.182 24.830   59.215  1.00 145.60 ?  388  ASN F CA  1 
ATOM   18386 C  C   . ASN F 6  388  ? -30.206 24.713   60.337  1.00 143.68 ?  388  ASN F C   1 
ATOM   18387 O  O   . ASN F 6  388  ? -31.316 25.243   60.215  1.00 146.67 ?  388  ASN F O   1 
ATOM   18388 C  CB  . ASN F 6  388  ? -29.400 23.726   58.179  1.00 139.47 ?  388  ASN F CB  1 
ATOM   18389 C  CG  . ASN F 6  388  ? -28.678 23.999   56.873  1.00 146.93 ?  388  ASN F CG  1 
ATOM   18390 O  OD1 . ASN F 6  388  ? -28.099 25.068   56.682  1.00 154.56 ?  388  ASN F OD1 1 
ATOM   18391 N  ND2 . ASN F 6  388  ? -28.709 23.029   55.965  1.00 146.82 ?  388  ASN F ND2 1 
ATOM   18392 N  N   . VAL F 6  389  ? -29.860 24.032   61.431  1.00 155.57 ?  389  VAL F N   1 
ATOM   18393 C  CA  . VAL F 6  389  ? -30.811 23.895   62.529  1.00 155.45 ?  389  VAL F CA  1 
ATOM   18394 C  C   . VAL F 6  389  ? -30.793 25.132   63.425  1.00 158.99 ?  389  VAL F C   1 
ATOM   18395 O  O   . VAL F 6  389  ? -31.793 25.438   64.084  1.00 155.45 ?  389  VAL F O   1 
ATOM   18396 C  CB  . VAL F 6  389  ? -30.534 22.606   63.326  1.00 154.56 ?  389  VAL F CB  1 
ATOM   18397 C  CG1 . VAL F 6  389  ? -29.282 22.747   64.178  1.00 153.25 ?  389  VAL F CG1 1 
ATOM   18398 C  CG2 . VAL F 6  389  ? -31.739 22.233   64.182  1.00 155.83 ?  389  VAL F CG2 1 
ATOM   18399 N  N   . GLN F 6  390  ? -29.677 25.863   63.463  1.00 130.49 ?  390  GLN F N   1 
ATOM   18400 C  CA  . GLN F 6  390  ? -29.636 27.142   64.159  1.00 126.27 ?  390  GLN F CA  1 
ATOM   18401 C  C   . GLN F 6  390  ? -30.231 28.275   63.335  1.00 117.90 ?  390  GLN F C   1 
ATOM   18402 O  O   . GLN F 6  390  ? -30.477 29.355   63.882  1.00 108.26 ?  390  GLN F O   1 
ATOM   18403 C  CB  . GLN F 6  390  ? -28.198 27.499   64.546  1.00 127.77 ?  390  GLN F CB  1 
ATOM   18404 C  CG  . GLN F 6  390  ? -27.670 26.759   65.763  1.00 129.10 ?  390  GLN F CG  1 
ATOM   18405 C  CD  . GLN F 6  390  ? -26.169 26.906   65.924  1.00 138.12 ?  390  GLN F CD  1 
ATOM   18406 O  OE1 . GLN F 6  390  ? -25.479 27.377   65.020  1.00 141.28 ?  390  GLN F OE1 1 
ATOM   18407 N  NE2 . GLN F 6  390  ? -25.657 26.506   67.082  1.00 141.34 ?  390  GLN F NE2 1 
ATOM   18408 N  N   . GLN F 6  391  ? -30.462 28.053   62.038  1.00 165.62 ?  391  GLN F N   1 
ATOM   18409 C  CA  . GLN F 6  391  ? -31.044 29.089   61.191  1.00 166.37 ?  391  GLN F CA  1 
ATOM   18410 C  C   . GLN F 6  391  ? -32.477 29.403   61.603  1.00 165.81 ?  391  GLN F C   1 
ATOM   18411 O  O   . GLN F 6  391  ? -32.862 30.575   61.687  1.00 169.12 ?  391  GLN F O   1 
ATOM   18412 C  CB  . GLN F 6  391  ? -31.000 28.650   59.727  1.00 159.79 ?  391  GLN F CB  1 
ATOM   18413 C  CG  . GLN F 6  391  ? -29.878 29.264   58.910  1.00 155.92 ?  391  GLN F CG  1 
ATOM   18414 C  CD  . GLN F 6  391  ? -29.911 28.817   57.461  1.00 160.93 ?  391  GLN F CD  1 
ATOM   18415 O  OE1 . GLN F 6  391  ? -30.884 29.059   56.747  1.00 160.99 ?  391  GLN F OE1 1 
ATOM   18416 N  NE2 . GLN F 6  391  ? -28.846 28.158   57.021  1.00 167.56 ?  391  GLN F NE2 1 
ATOM   18417 N  N   . ALA F 6  392  ? -33.275 28.375   61.862  1.00 119.50 ?  392  ALA F N   1 
ATOM   18418 C  CA  . ALA F 6  392  ? -34.691 28.501   62.160  1.00 110.27 ?  392  ALA F CA  1 
ATOM   18419 C  C   . ALA F 6  392  ? -35.017 27.849   63.497  1.00 104.28 ?  392  ALA F C   1 
ATOM   18420 O  O   . ALA F 6  392  ? -34.291 26.961   63.959  1.00 98.84  ?  392  ALA F O   1 
ATOM   18421 C  CB  . ALA F 6  392  ? -35.535 27.856   61.050  1.00 111.06 ?  392  ALA F CB  1 
ATOM   18422 N  N   . PRO F 6  393  ? -36.097 28.271   64.151  1.00 129.91 ?  393  PRO F N   1 
ATOM   18423 C  CA  . PRO F 6  393  ? -36.496 27.624   65.404  1.00 127.01 ?  393  PRO F CA  1 
ATOM   18424 C  C   . PRO F 6  393  ? -37.025 26.219   65.164  1.00 123.23 ?  393  PRO F C   1 
ATOM   18425 O  O   . PRO F 6  393  ? -37.503 25.875   64.081  1.00 124.38 ?  393  PRO F O   1 
ATOM   18426 C  CB  . PRO F 6  393  ? -37.594 28.544   65.947  1.00 129.78 ?  393  PRO F CB  1 
ATOM   18427 C  CG  . PRO F 6  393  ? -38.137 29.227   64.737  1.00 131.30 ?  393  PRO F CG  1 
ATOM   18428 C  CD  . PRO F 6  393  ? -36.957 29.423   63.830  1.00 137.03 ?  393  PRO F CD  1 
ATOM   18429 N  N   . LEU F 6  394  ? -36.930 25.401   66.205  1.00 134.08 ?  394  LEU F N   1 
ATOM   18430 C  CA  . LEU F 6  394  ? -37.386 24.022   66.149  1.00 132.25 ?  394  LEU F CA  1 
ATOM   18431 C  C   . LEU F 6  394  ? -38.864 23.936   66.516  1.00 140.79 ?  394  LEU F C   1 
ATOM   18432 O  O   . LEU F 6  394  ? -39.425 24.834   67.148  1.00 150.88 ?  394  LEU F O   1 
ATOM   18433 C  CB  . LEU F 6  394  ? -36.564 23.136   67.089  1.00 128.92 ?  394  LEU F CB  1 
ATOM   18434 C  CG  . LEU F 6  394  ? -35.057 23.017   66.847  1.00 136.86 ?  394  LEU F CG  1 
ATOM   18435 C  CD1 . LEU F 6  394  ? -34.287 24.131   67.547  1.00 135.85 ?  394  LEU F CD1 1 
ATOM   18436 C  CD2 . LEU F 6  394  ? -34.551 21.653   67.292  1.00 137.46 ?  394  LEU F CD2 1 
ATOM   18437 N  N   . LEU F 6  395  ? -39.490 22.830   66.101  1.00 168.74 ?  395  LEU F N   1 
ATOM   18438 C  CA  . LEU F 6  395  ? -40.885 22.514   66.392  1.00 172.87 ?  395  LEU F CA  1 
ATOM   18439 C  C   . LEU F 6  395  ? -41.814 23.590   65.840  1.00 177.94 ?  395  LEU F C   1 
ATOM   18440 O  O   . LEU F 6  395  ? -42.068 24.597   66.513  1.00 186.95 ?  395  LEU F O   1 
ATOM   18441 C  CB  . LEU F 6  395  ? -41.105 22.348   67.899  1.00 169.25 ?  395  LEU F CB  1 
ATOM   18442 C  CG  . LEU F 6  395  ? -40.674 21.032   68.556  1.00 168.79 ?  395  LEU F CG  1 
ATOM   18443 C  CD1 . LEU F 6  395  ? -39.157 20.927   68.671  1.00 166.59 ?  395  LEU F CD1 1 
ATOM   18444 C  CD2 . LEU F 6  395  ? -41.324 20.883   69.922  1.00 172.83 ?  395  LEU F CD2 1 
ATOM   18445 N  N   . PRO F 6  396  ? -42.344 23.413   64.627  1.00 121.47 ?  396  PRO F N   1 
ATOM   18446 C  CA  . PRO F 6  396  ? -43.257 24.419   64.066  1.00 124.84 ?  396  PRO F CA  1 
ATOM   18447 C  C   . PRO F 6  396  ? -44.540 24.546   64.872  1.00 129.31 ?  396  PRO F C   1 
ATOM   18448 O  O   . PRO F 6  396  ? -45.396 23.656   64.836  1.00 125.55 ?  396  PRO F O   1 
ATOM   18449 C  CB  . PRO F 6  396  ? -43.530 23.894   62.650  1.00 128.62 ?  396  PRO F CB  1 
ATOM   18450 C  CG  . PRO F 6  396  ? -43.266 22.425   62.736  1.00 125.98 ?  396  PRO F CG  1 
ATOM   18451 C  CD  . PRO F 6  396  ? -42.140 22.276   63.715  1.00 115.53 ?  396  PRO F CD  1 
ATOM   18452 N  N   . LEU F 6  397  ? -44.677 25.653   65.607  1.00 114.53 ?  397  LEU F N   1 
ATOM   18453 C  CA  . LEU F 6  397  ? -45.841 25.830   66.470  1.00 109.32 ?  397  LEU F CA  1 
ATOM   18454 C  C   . LEU F 6  397  ? -47.128 25.890   65.658  1.00 106.44 ?  397  LEU F C   1 
ATOM   18455 O  O   . LEU F 6  397  ? -48.160 25.352   66.076  1.00 107.13 ?  397  LEU F O   1 
ATOM   18456 C  CB  . LEU F 6  397  ? -45.688 27.093   67.318  1.00 113.89 ?  397  LEU F CB  1 
ATOM   18457 C  CG  . LEU F 6  397  ? -44.782 27.032   68.552  1.00 106.66 ?  397  LEU F CG  1 
ATOM   18458 C  CD1 . LEU F 6  397  ? -43.306 27.063   68.170  1.00 94.56  ?  397  LEU F CD1 1 
ATOM   18459 C  CD2 . LEU F 6  397  ? -45.117 28.159   69.520  1.00 106.77 ?  397  LEU F CD2 1 
ATOM   18460 N  N   . ARG F 6  398  ? -47.089 26.541   64.498  1.00 113.23 ?  398  ARG F N   1 
ATOM   18461 C  CA  . ARG F 6  398  ? -48.260 26.641   63.628  1.00 124.39 ?  398  ARG F CA  1 
ATOM   18462 C  C   . ARG F 6  398  ? -48.294 25.401   62.745  1.00 130.33 ?  398  ARG F C   1 
ATOM   18463 O  O   . ARG F 6  398  ? -47.746 25.378   61.642  1.00 134.42 ?  398  ARG F O   1 
ATOM   18464 C  CB  . ARG F 6  398  ? -48.221 27.924   62.808  1.00 137.15 ?  398  ARG F CB  1 
ATOM   18465 C  CG  . ARG F 6  398  ? -48.429 29.189   63.627  1.00 129.50 ?  398  ARG F CG  1 
ATOM   18466 C  CD  . ARG F 6  398  ? -48.415 30.423   62.742  1.00 131.62 ?  398  ARG F CD  1 
ATOM   18467 N  NE  . ARG F 6  398  ? -49.294 30.266   61.589  1.00 131.87 ?  398  ARG F NE  1 
ATOM   18468 C  CZ  . ARG F 6  398  ? -50.578 30.596   61.576  1.00 133.05 ?  398  ARG F CZ  1 
ATOM   18469 N  NH1 . ARG F 6  398  ? -51.170 31.111   62.641  1.00 138.53 ?  398  ARG F NH1 1 
ATOM   18470 N  NH2 . ARG F 6  398  ? -51.286 30.402   60.467  1.00 131.06 ?  398  ARG F NH2 1 
ATOM   18471 N  N   . ASP F 6  399  ? -48.946 24.354   63.243  1.00 167.22 ?  399  ASP F N   1 
ATOM   18472 C  CA  . ASP F 6  399  ? -49.064 23.089   62.532  1.00 166.85 ?  399  ASP F CA  1 
ATOM   18473 C  C   . ASP F 6  399  ? -50.248 22.310   63.090  1.00 164.78 ?  399  ASP F C   1 
ATOM   18474 O  O   . ASP F 6  399  ? -50.319 22.080   64.304  1.00 163.19 ?  399  ASP F O   1 
ATOM   18475 C  CB  . ASP F 6  399  ? -47.772 22.278   62.656  1.00 163.34 ?  399  ASP F CB  1 
ATOM   18476 C  CG  . ASP F 6  399  ? -47.522 21.385   61.454  1.00 170.26 ?  399  ASP F CG  1 
ATOM   18477 O  OD1 . ASP F 6  399  ? -48.493 20.813   60.917  1.00 165.39 ?  399  ASP F OD1 1 
ATOM   18478 O  OD2 . ASP F 6  399  ? -46.349 21.257   61.042  1.00 176.55 -1 399  ASP F OD2 1 
ATOM   18479 N  N   . PRO F 6  400  ? -51.200 21.899   62.248  1.00 127.49 ?  400  PRO F N   1 
ATOM   18480 C  CA  . PRO F 6  400  ? -52.349 21.132   62.760  1.00 121.34 ?  400  PRO F CA  1 
ATOM   18481 C  C   . PRO F 6  400  ? -51.962 19.826   63.429  1.00 120.11 ?  400  PRO F C   1 
ATOM   18482 O  O   . PRO F 6  400  ? -52.761 19.285   64.204  1.00 116.22 ?  400  PRO F O   1 
ATOM   18483 C  CB  . PRO F 6  400  ? -53.200 20.889   61.504  1.00 125.89 ?  400  PRO F CB  1 
ATOM   18484 C  CG  . PRO F 6  400  ? -52.281 21.148   60.345  1.00 136.55 ?  400  PRO F CG  1 
ATOM   18485 C  CD  . PRO F 6  400  ? -51.330 22.199   60.814  1.00 133.87 ?  400  PRO F CD  1 
ATOM   18486 N  N   . ASN F 6  401  ? -50.767 19.301   63.158  1.00 157.37 ?  401  ASN F N   1 
ATOM   18487 C  CA  . ASN F 6  401  ? -50.303 18.084   63.809  1.00 155.53 ?  401  ASN F CA  1 
ATOM   18488 C  C   . ASN F 6  401  ? -49.673 18.344   65.170  1.00 158.13 ?  401  ASN F C   1 
ATOM   18489 O  O   . ASN F 6  401  ? -49.333 17.382   65.868  1.00 161.18 ?  401  ASN F O   1 
ATOM   18490 C  CB  . ASN F 6  401  ? -49.300 17.356   62.911  1.00 157.08 ?  401  ASN F CB  1 
ATOM   18491 C  CG  . ASN F 6  401  ? -49.948 16.759   61.677  1.00 156.05 ?  401  ASN F CG  1 
ATOM   18492 O  OD1 . ASN F 6  401  ? -51.005 16.133   61.758  1.00 154.75 ?  401  ASN F OD1 1 
ATOM   18493 N  ND2 . ASN F 6  401  ? -49.316 16.950   60.525  1.00 149.19 ?  401  ASN F ND2 1 
ATOM   18494 N  N   . MET F 6  402  ? -49.507 19.610   65.562  1.00 128.56 ?  402  MET F N   1 
ATOM   18495 C  CA  . MET F 6  402  ? -48.936 19.919   66.869  1.00 122.87 ?  402  MET F CA  1 
ATOM   18496 C  C   . MET F 6  402  ? -49.833 19.462   68.010  1.00 117.84 ?  402  MET F C   1 
ATOM   18497 O  O   . MET F 6  402  ? -49.339 19.234   69.120  1.00 115.24 ?  402  MET F O   1 
ATOM   18498 C  CB  . MET F 6  402  ? -48.669 21.421   66.983  1.00 123.68 ?  402  MET F CB  1 
ATOM   18499 C  CG  . MET F 6  402  ? -47.581 21.791   67.976  1.00 116.07 ?  402  MET F CG  1 
ATOM   18500 S  SD  . MET F 6  402  ? -45.928 21.637   67.272  1.00 119.12 ?  402  MET F SD  1 
ATOM   18501 C  CE  . MET F 6  402  ? -44.913 21.898   68.725  1.00 125.26 ?  402  MET F CE  1 
ATOM   18502 N  N   . GLU F 6  403  ? -51.139 19.323   67.765  1.00 135.91 ?  403  GLU F N   1 
ATOM   18503 C  CA  . GLU F 6  403  ? -52.042 18.810   68.788  1.00 133.57 ?  403  GLU F CA  1 
ATOM   18504 C  C   . GLU F 6  403  ? -51.699 17.382   69.191  1.00 139.01 ?  403  GLU F C   1 
ATOM   18505 O  O   . GLU F 6  403  ? -52.066 16.955   70.291  1.00 152.78 ?  403  GLU F O   1 
ATOM   18506 C  CB  . GLU F 6  403  ? -53.488 18.879   68.294  1.00 138.61 ?  403  GLU F CB  1 
ATOM   18507 C  CG  . GLU F 6  403  ? -54.019 20.293   68.123  1.00 148.27 ?  403  GLU F CG  1 
ATOM   18508 C  CD  . GLU F 6  403  ? -55.441 20.320   67.598  1.00 149.08 ?  403  GLU F CD  1 
ATOM   18509 O  OE1 . GLU F 6  403  ? -55.962 19.245   67.233  1.00 147.24 ?  403  GLU F OE1 1 
ATOM   18510 O  OE2 . GLU F 6  403  ? -56.038 21.416   67.551  1.00 147.96 -1 403  GLU F OE2 1 
ATOM   18511 N  N   . GLN F 6  404  ? -51.006 16.636   68.327  1.00 111.53 ?  404  GLN F N   1 
ATOM   18512 C  CA  . GLN F 6  404  ? -50.577 15.283   68.654  1.00 115.22 ?  404  GLN F CA  1 
ATOM   18513 C  C   . GLN F 6  404  ? -49.488 15.251   69.719  1.00 119.76 ?  404  GLN F C   1 
ATOM   18514 O  O   . GLN F 6  404  ? -49.226 14.180   70.278  1.00 124.19 ?  404  GLN F O   1 
ATOM   18515 C  CB  . GLN F 6  404  ? -50.090 14.571   67.390  1.00 110.69 ?  404  GLN F CB  1 
ATOM   18516 C  CG  . GLN F 6  404  ? -51.201 14.231   66.410  1.00 114.58 ?  404  GLN F CG  1 
ATOM   18517 C  CD  . GLN F 6  404  ? -50.684 13.590   65.138  1.00 108.92 ?  404  GLN F CD  1 
ATOM   18518 O  OE1 . GLN F 6  404  ? -49.478 13.553   64.894  1.00 104.72 ?  404  GLN F OE1 1 
ATOM   18519 N  NE2 . GLN F 6  404  ? -51.596 13.074   64.324  1.00 110.07 ?  404  GLN F NE2 1 
ATOM   18520 N  N   . LEU F 6  405  ? -48.851 16.388   70.007  1.00 112.87 ?  405  LEU F N   1 
ATOM   18521 C  CA  . LEU F 6  405  ? -47.861 16.469   71.073  1.00 107.91 ?  405  LEU F CA  1 
ATOM   18522 C  C   . LEU F 6  405  ? -48.482 16.700   72.443  1.00 115.24 ?  405  LEU F C   1 
ATOM   18523 O  O   . LEU F 6  405  ? -47.807 16.486   73.457  1.00 117.03 ?  405  LEU F O   1 
ATOM   18524 C  CB  . LEU F 6  405  ? -46.853 17.586   70.777  1.00 113.43 ?  405  LEU F CB  1 
ATOM   18525 C  CG  . LEU F 6  405  ? -45.776 17.243   69.746  1.00 110.23 ?  405  LEU F CG  1 
ATOM   18526 C  CD1 . LEU F 6  405  ? -44.745 18.356   69.638  1.00 101.91 ?  405  LEU F CD1 1 
ATOM   18527 C  CD2 . LEU F 6  405  ? -45.112 15.915   70.083  1.00 116.82 ?  405  LEU F CD2 1 
ATOM   18528 N  N   . GLN F 6  406  ? -49.741 17.138   72.498  1.00 126.54 ?  406  GLN F N   1 
ATOM   18529 C  CA  . GLN F 6  406  ? -50.448 17.290   73.763  1.00 126.58 ?  406  GLN F CA  1 
ATOM   18530 C  C   . GLN F 6  406  ? -50.997 15.974   74.297  1.00 132.11 ?  406  GLN F C   1 
ATOM   18531 O  O   . GLN F 6  406  ? -51.394 15.916   75.466  1.00 133.76 ?  406  GLN F O   1 
ATOM   18532 C  CB  . GLN F 6  406  ? -51.598 18.291   73.611  1.00 126.99 ?  406  GLN F CB  1 
ATOM   18533 C  CG  . GLN F 6  406  ? -51.188 19.745   73.773  1.00 131.02 ?  406  GLN F CG  1 
ATOM   18534 C  CD  . GLN F 6  406  ? -52.271 20.587   74.421  1.00 129.29 ?  406  GLN F CD  1 
ATOM   18535 O  OE1 . GLN F 6  406  ? -53.454 20.443   74.112  1.00 121.13 ?  406  GLN F OE1 1 
ATOM   18536 N  NE2 . GLN F 6  406  ? -51.869 21.473   75.324  1.00 128.94 ?  406  GLN F NE2 1 
ATOM   18537 N  N   . LEU G 7  32   ? -58.667 -27.348  91.399  1.00 115.43 ?  32   LEU G N   1 
ATOM   18538 C  CA  . LEU G 7  32   ? -58.292 -28.117  92.580  1.00 122.13 ?  32   LEU G CA  1 
ATOM   18539 C  C   . LEU G 7  32   ? -57.263 -29.182  92.214  1.00 118.17 ?  32   LEU G C   1 
ATOM   18540 O  O   . LEU G 7  32   ? -57.354 -29.805  91.157  1.00 114.91 ?  32   LEU G O   1 
ATOM   18541 C  CB  . LEU G 7  32   ? -59.524 -28.761  93.217  1.00 117.98 ?  32   LEU G CB  1 
ATOM   18542 C  CG  . LEU G 7  32   ? -59.301 -29.541  94.515  1.00 114.10 ?  32   LEU G CG  1 
ATOM   18543 C  CD1 . LEU G 7  32   ? -58.575 -28.684  95.541  1.00 109.34 ?  32   LEU G CD1 1 
ATOM   18544 C  CD2 . LEU G 7  32   ? -60.622 -30.048  95.070  1.00 94.55  ?  32   LEU G CD2 1 
ATOM   18545 N  N   . SER G 7  33   ? -56.275 -29.378  93.090  1.00 172.04 ?  33   SER G N   1 
ATOM   18546 C  CA  . SER G 7  33   ? -55.217 -30.340  92.802  1.00 168.28 ?  33   SER G CA  1 
ATOM   18547 C  C   . SER G 7  33   ? -55.704 -31.776  92.926  1.00 162.06 ?  33   SER G C   1 
ATOM   18548 O  O   . SER G 7  33   ? -55.186 -32.662  92.238  1.00 161.76 ?  33   SER G O   1 
ATOM   18549 C  CB  . SER G 7  33   ? -54.028 -30.112  93.731  1.00 167.90 ?  33   SER G CB  1 
ATOM   18550 O  OG  . SER G 7  33   ? -54.380 -30.363  95.081  1.00 164.86 ?  33   SER G OG  1 
ATOM   18551 N  N   . ARG G 7  34   ? -56.687 -32.026  93.794  1.00 139.52 ?  34   ARG G N   1 
ATOM   18552 C  CA  . ARG G 7  34   ? -57.160 -33.390  94.007  1.00 142.74 ?  34   ARG G CA  1 
ATOM   18553 C  C   . ARG G 7  34   ? -57.754 -33.973  92.731  1.00 141.63 ?  34   ARG G C   1 
ATOM   18554 O  O   . ARG G 7  34   ? -57.444 -35.107  92.348  1.00 141.93 ?  34   ARG G O   1 
ATOM   18555 C  CB  . ARG G 7  34   ? -58.186 -33.418  95.140  1.00 145.18 ?  34   ARG G CB  1 
ATOM   18556 C  CG  . ARG G 7  34   ? -57.593 -33.734  96.502  1.00 149.28 ?  34   ARG G CG  1 
ATOM   18557 C  CD  . ARG G 7  34   ? -58.390 -33.078  97.615  1.00 157.44 ?  34   ARG G CD  1 
ATOM   18558 N  NE  . ARG G 7  34   ? -58.121 -33.695  98.907  1.00 160.79 ?  34   ARG G NE  1 
ATOM   18559 C  CZ  . ARG G 7  34   ? -58.790 -34.731  99.392  1.00 158.55 ?  34   ARG G CZ  1 
ATOM   18560 N  NH1 . ARG G 7  34   ? -59.779 -35.293  98.716  1.00 153.36 ?  34   ARG G NH1 1 
ATOM   18561 N  NH2 . ARG G 7  34   ? -58.460 -35.216  100.586 1.00 159.12 ?  34   ARG G NH2 1 
ATOM   18562 N  N   . LEU G 7  35   ? -58.612 -33.207  92.054  1.00 124.17 ?  35   LEU G N   1 
ATOM   18563 C  CA  . LEU G 7  35   ? -59.224 -33.698  90.825  1.00 118.56 ?  35   LEU G CA  1 
ATOM   18564 C  C   . LEU G 7  35   ? -58.200 -33.801  89.702  1.00 118.27 ?  35   LEU G C   1 
ATOM   18565 O  O   . LEU G 7  35   ? -58.262 -34.721  88.878  1.00 116.98 ?  35   LEU G O   1 
ATOM   18566 C  CB  . LEU G 7  35   ? -60.379 -32.786  90.418  1.00 126.04 ?  35   LEU G CB  1 
ATOM   18567 C  CG  . LEU G 7  35   ? -61.348 -32.411  91.540  1.00 123.31 ?  35   LEU G CG  1 
ATOM   18568 C  CD1 . LEU G 7  35   ? -62.437 -31.491  91.019  1.00 125.25 ?  35   LEU G CD1 1 
ATOM   18569 C  CD2 . LEU G 7  35   ? -61.951 -33.656  92.176  1.00 109.13 ?  35   LEU G CD2 1 
ATOM   18570 N  N   . MET G 7  36   ? -57.248 -32.867  89.657  1.00 129.55 ?  36   MET G N   1 
ATOM   18571 C  CA  . MET G 7  36   ? -56.231 -32.895  88.612  1.00 127.49 ?  36   MET G CA  1 
ATOM   18572 C  C   . MET G 7  36   ? -55.280 -34.071  88.799  1.00 127.96 ?  36   MET G C   1 
ATOM   18573 O  O   . MET G 7  36   ? -54.867 -34.703  87.820  1.00 131.35 ?  36   MET G O   1 
ATOM   18574 C  CB  . MET G 7  36   ? -55.467 -31.572  88.600  1.00 126.51 ?  36   MET G CB  1 
ATOM   18575 C  CG  . MET G 7  36   ? -56.046 -30.539  87.650  1.00 126.99 ?  36   MET G CG  1 
ATOM   18576 S  SD  . MET G 7  36   ? -54.934 -29.147  87.404  1.00 142.13 ?  36   MET G SD  1 
ATOM   18577 C  CE  . MET G 7  36   ? -56.080 -27.883  86.861  1.00 144.09 ?  36   MET G CE  1 
ATOM   18578 N  N   . ILE G 7  37   ? -54.922 -34.379  90.048  1.00 121.99 ?  37   ILE G N   1 
ATOM   18579 C  CA  . ILE G 7  37   ? -54.098 -35.554  90.315  1.00 120.85 ?  37   ILE G CA  1 
ATOM   18580 C  C   . ILE G 7  37   ? -54.887 -36.828  90.037  1.00 117.55 ?  37   ILE G C   1 
ATOM   18581 O  O   . ILE G 7  37   ? -54.341 -37.815  89.528  1.00 124.56 ?  37   ILE G O   1 
ATOM   18582 C  CB  . ILE G 7  37   ? -53.563 -35.514  91.759  1.00 118.34 ?  37   ILE G CB  1 
ATOM   18583 C  CG1 . ILE G 7  37   ? -52.536 -34.390  91.917  1.00 118.95 ?  37   ILE G CG1 1 
ATOM   18584 C  CG2 . ILE G 7  37   ? -52.950 -36.852  92.150  1.00 113.55 ?  37   ILE G CG2 1 
ATOM   18585 C  CD1 . ILE G 7  37   ? -51.296 -34.569  91.066  1.00 119.06 ?  37   ILE G CD1 1 
ATOM   18586 N  N   . ALA G 7  38   ? -56.185 -36.824  90.353  1.00 78.53  ?  38   ALA G N   1 
ATOM   18587 C  CA  . ALA G 7  38   ? -57.025 -37.982  90.063  1.00 72.95  ?  38   ALA G CA  1 
ATOM   18588 C  C   . ALA G 7  38   ? -57.121 -38.226  88.562  1.00 76.17  ?  38   ALA G C   1 
ATOM   18589 O  O   . ALA G 7  38   ? -56.990 -39.364  88.096  1.00 73.10  ?  38   ALA G O   1 
ATOM   18590 C  CB  . ALA G 7  38   ? -58.415 -37.787  90.669  1.00 71.65  ?  38   ALA G CB  1 
ATOM   18591 N  N   . GLY G 7  39   ? -57.352 -37.164  87.786  1.00 145.94 ?  39   GLY G N   1 
ATOM   18592 C  CA  . GLY G 7  39   ? -57.366 -37.305  86.340  1.00 144.91 ?  39   GLY G CA  1 
ATOM   18593 C  C   . GLY G 7  39   ? -56.023 -37.720  85.777  1.00 139.75 ?  39   GLY G C   1 
ATOM   18594 O  O   . GLY G 7  39   ? -55.957 -38.369  84.729  1.00 134.94 ?  39   GLY G O   1 
ATOM   18595 N  N   . LEU G 7  40   ? -54.935 -37.357  86.461  1.00 116.38 ?  40   LEU G N   1 
ATOM   18596 C  CA  . LEU G 7  40   ? -53.610 -37.790  86.030  1.00 111.58 ?  40   LEU G CA  1 
ATOM   18597 C  C   . LEU G 7  40   ? -53.416 -39.283  86.262  1.00 107.67 ?  40   LEU G C   1 
ATOM   18598 O  O   . LEU G 7  40   ? -52.958 -40.005  85.368  1.00 106.95 ?  40   LEU G O   1 
ATOM   18599 C  CB  . LEU G 7  40   ? -52.529 -36.991  86.755  1.00 115.08 ?  40   LEU G CB  1 
ATOM   18600 C  CG  . LEU G 7  40   ? -51.132 -37.561  86.518  1.00 117.82 ?  40   LEU G CG  1 
ATOM   18601 C  CD1 . LEU G 7  40   ? -50.783 -37.485  85.042  1.00 126.47 ?  40   LEU G CD1 1 
ATOM   18602 C  CD2 . LEU G 7  40   ? -50.096 -36.837  87.359  1.00 119.13 ?  40   LEU G CD2 1 
ATOM   18603 N  N   . MET G 7  41   ? -53.749 -39.764  87.463  1.00 117.12 ?  41   MET G N   1 
ATOM   18604 C  CA  . MET G 7  41   ? -53.619 -41.190  87.748  1.00 113.50 ?  41   MET G CA  1 
ATOM   18605 C  C   . MET G 7  41   ? -54.467 -42.026  86.799  1.00 112.18 ?  41   MET G C   1 
ATOM   18606 O  O   . MET G 7  41   ? -54.075 -43.139  86.433  1.00 110.95 ?  41   MET G O   1 
ATOM   18607 C  CB  . MET G 7  41   ? -54.004 -41.469  89.200  1.00 115.20 ?  41   MET G CB  1 
ATOM   18608 C  CG  . MET G 7  41   ? -53.156 -40.727  90.221  1.00 125.40 ?  41   MET G CG  1 
ATOM   18609 S  SD  . MET G 7  41   ? -51.457 -40.470  89.673  1.00 144.21 ?  41   MET G SD  1 
ATOM   18610 C  CE  . MET G 7  41   ? -50.663 -40.050  91.224  1.00 135.55 ?  41   MET G CE  1 
ATOM   18611 N  N   . VAL G 7  42   ? -55.623 -41.503  86.385  1.00 96.16  ?  42   VAL G N   1 
ATOM   18612 C  CA  . VAL G 7  42   ? -56.445 -42.202  85.404  1.00 92.67  ?  42   VAL G CA  1 
ATOM   18613 C  C   . VAL G 7  42   ? -55.743 -42.240  84.052  1.00 96.34  ?  42   VAL G C   1 
ATOM   18614 O  O   . VAL G 7  42   ? -55.718 -43.277  83.378  1.00 93.56  ?  42   VAL G O   1 
ATOM   18615 C  CB  . VAL G 7  42   ? -57.833 -41.542  85.308  1.00 94.18  ?  42   VAL G CB  1 
ATOM   18616 C  CG1 . VAL G 7  42   ? -58.604 -42.083  84.110  1.00 93.26  ?  42   VAL G CG1 1 
ATOM   18617 C  CG2 . VAL G 7  42   ? -58.613 -41.763  86.594  1.00 85.89  ?  42   VAL G CG2 1 
ATOM   18618 N  N   . PHE G 7  43   ? -55.153 -41.115  83.638  1.00 105.94 ?  43   PHE G N   1 
ATOM   18619 C  CA  . PHE G 7  43   ? -54.428 -41.076  82.372  1.00 103.20 ?  43   PHE G CA  1 
ATOM   18620 C  C   . PHE G 7  43   ? -53.187 -41.963  82.416  1.00 99.20  ?  43   PHE G C   1 
ATOM   18621 O  O   . PHE G 7  43   ? -52.841 -42.604  81.417  1.00 94.77  ?  43   PHE G O   1 
ATOM   18622 C  CB  . PHE G 7  43   ? -54.052 -39.634  82.036  1.00 104.89 ?  43   PHE G CB  1 
ATOM   18623 C  CG  . PHE G 7  43   ? -52.900 -39.510  81.080  1.00 104.21 ?  43   PHE G CG  1 
ATOM   18624 C  CD1 . PHE G 7  43   ? -53.037 -39.894  79.757  1.00 103.24 ?  43   PHE G CD1 1 
ATOM   18625 C  CD2 . PHE G 7  43   ? -51.679 -39.011  81.504  1.00 107.42 ?  43   PHE G CD2 1 
ATOM   18626 C  CE1 . PHE G 7  43   ? -51.983 -39.777  78.872  1.00 104.20 ?  43   PHE G CE1 1 
ATOM   18627 C  CE2 . PHE G 7  43   ? -50.619 -38.894  80.624  1.00 108.36 ?  43   PHE G CE2 1 
ATOM   18628 C  CZ  . PHE G 7  43   ? -50.774 -39.276  79.305  1.00 105.54 ?  43   PHE G CZ  1 
ATOM   18629 N  N   . LEU G 7  44   ? -52.504 -42.008  83.565  1.00 97.08  ?  44   LEU G N   1 
ATOM   18630 C  CA  . LEU G 7  44   ? -51.360 -42.903  83.727  1.00 92.57  ?  44   LEU G CA  1 
ATOM   18631 C  C   . LEU G 7  44   ? -51.769 -44.369  83.628  1.00 88.66  ?  44   LEU G C   1 
ATOM   18632 O  O   . LEU G 7  44   ? -51.075 -45.171  82.994  1.00 95.36  ?  44   LEU G O   1 
ATOM   18633 C  CB  . LEU G 7  44   ? -50.664 -42.630  85.062  1.00 92.55  ?  44   LEU G CB  1 
ATOM   18634 C  CG  . LEU G 7  44   ? -49.292 -43.282  85.266  1.00 92.83  ?  44   LEU G CG  1 
ATOM   18635 C  CD1 . LEU G 7  44   ? -48.278 -42.849  84.209  1.00 95.17  ?  44   LEU G CD1 1 
ATOM   18636 C  CD2 . LEU G 7  44   ? -48.769 -42.941  86.648  1.00 95.30  ?  44   LEU G CD2 1 
ATOM   18637 N  N   . VAL G 7  45   ? -52.884 -44.746  84.257  1.00 102.92 ?  45   VAL G N   1 
ATOM   18638 C  CA  . VAL G 7  45   ? -53.334 -46.134  84.192  1.00 108.43 ?  45   VAL G CA  1 
ATOM   18639 C  C   . VAL G 7  45   ? -53.749 -46.498  82.771  1.00 107.50 ?  45   VAL G C   1 
ATOM   18640 O  O   . VAL G 7  45   ? -53.358 -47.547  82.245  1.00 102.10 ?  45   VAL G O   1 
ATOM   18641 C  CB  . VAL G 7  45   ? -54.477 -46.372  85.195  1.00 104.32 ?  45   VAL G CB  1 
ATOM   18642 C  CG1 . VAL G 7  45   ? -55.133 -47.714  84.935  1.00 91.26  ?  45   VAL G CG1 1 
ATOM   18643 C  CG2 . VAL G 7  45   ? -53.954 -46.299  86.621  1.00 96.40  ?  45   VAL G CG2 1 
ATOM   18644 N  N   . LEU G 7  46   ? -54.549 -45.640  82.130  1.00 93.54  ?  46   LEU G N   1 
ATOM   18645 C  CA  . LEU G 7  46   ? -54.995 -45.906  80.763  1.00 88.70  ?  46   LEU G CA  1 
ATOM   18646 C  C   . LEU G 7  46   ? -53.819 -46.089  79.813  1.00 89.88  ?  46   LEU G C   1 
ATOM   18647 O  O   . LEU G 7  46   ? -53.829 -46.988  78.964  1.00 88.48  ?  46   LEU G O   1 
ATOM   18648 C  CB  . LEU G 7  46   ? -55.892 -44.771  80.272  1.00 93.95  ?  46   LEU G CB  1 
ATOM   18649 C  CG  . LEU G 7  46   ? -56.515 -44.977  78.889  1.00 96.51  ?  46   LEU G CG  1 
ATOM   18650 C  CD1 . LEU G 7  46   ? -57.287 -46.287  78.827  1.00 96.05  ?  46   LEU G CD1 1 
ATOM   18651 C  CD2 . LEU G 7  46   ? -57.419 -43.808  78.531  1.00 94.84  ?  46   LEU G CD2 1 
ATOM   18652 N  N   . SER G 7  47   ? -52.801 -45.237  79.938  1.00 98.31  ?  47   SER G N   1 
ATOM   18653 C  CA  . SER G 7  47   ? -51.647 -45.298  79.048  1.00 91.23  ?  47   SER G CA  1 
ATOM   18654 C  C   . SER G 7  47   ? -50.823 -46.554  79.286  1.00 87.42  ?  47   SER G C   1 
ATOM   18655 O  O   . SER G 7  47   ? -50.357 -47.185  78.329  1.00 92.46  ?  47   SER G O   1 
ATOM   18656 C  CB  . SER G 7  47   ? -50.774 -44.075  79.261  1.00 89.83  ?  47   SER G CB  1 
ATOM   18657 O  OG  . SER G 7  47   ? -50.128 -44.199  80.515  1.00 100.33 ?  47   SER G OG  1 
ATOM   18658 N  N   . LEU G 7  48   ? -50.604 -46.915  80.556  1.00 71.39  ?  48   LEU G N   1 
ATOM   18659 C  CA  . LEU G 7  48   ? -49.872 -48.142  80.857  1.00 71.55  ?  48   LEU G CA  1 
ATOM   18660 C  C   . LEU G 7  48   ? -50.609 -49.368  80.335  1.00 71.24  ?  48   LEU G C   1 
ATOM   18661 O  O   . LEU G 7  48   ? -49.975 -50.347  79.924  1.00 61.32  ?  48   LEU G O   1 
ATOM   18662 C  CB  . LEU G 7  48   ? -49.632 -48.268  82.365  1.00 76.92  ?  48   LEU G CB  1 
ATOM   18663 C  CG  . LEU G 7  48   ? -48.292 -47.771  82.918  1.00 77.29  ?  48   LEU G CG  1 
ATOM   18664 C  CD1 . LEU G 7  48   ? -47.140 -48.613  82.380  1.00 62.00  ?  48   LEU G CD1 1 
ATOM   18665 C  CD2 . LEU G 7  48   ? -48.072 -46.302  82.603  1.00 90.56  ?  48   LEU G CD2 1 
ATOM   18666 N  N   . VAL G 7  49   ? -51.942 -49.330  80.342  1.00 93.72  ?  49   VAL G N   1 
ATOM   18667 C  CA  . VAL G 7  49   ? -52.720 -50.414  79.752  1.00 90.14  ?  49   VAL G CA  1 
ATOM   18668 C  C   . VAL G 7  49   ? -52.545 -50.433  78.239  1.00 88.39  ?  49   VAL G C   1 
ATOM   18669 O  O   . VAL G 7  49   ? -52.419 -51.502  77.629  1.00 88.44  ?  49   VAL G O   1 
ATOM   18670 C  CB  . VAL G 7  49   ? -54.202 -50.284  80.151  1.00 96.96  ?  49   VAL G CB  1 
ATOM   18671 C  CG1 . VAL G 7  49   ? -55.057 -51.278  79.379  1.00 90.38  ?  49   VAL G CG1 1 
ATOM   18672 C  CG2 . VAL G 7  49   ? -54.366 -50.501  81.647  1.00 98.02  ?  49   VAL G CG2 1 
ATOM   18673 N  N   . VAL G 7  50   ? -52.534 -49.256  77.609  1.00 72.95  ?  50   VAL G N   1 
ATOM   18674 C  CA  . VAL G 7  50   ? -52.345 -49.188  76.163  1.00 68.52  ?  50   VAL G CA  1 
ATOM   18675 C  C   . VAL G 7  50   ? -50.941 -49.645  75.786  1.00 66.54  ?  50   VAL G C   1 
ATOM   18676 O  O   . VAL G 7  50   ? -50.752 -50.364  74.797  1.00 62.03  ?  50   VAL G O   1 
ATOM   18677 C  CB  . VAL G 7  50   ? -52.639 -47.765  75.654  1.00 68.15  ?  50   VAL G CB  1 
ATOM   18678 C  CG1 . VAL G 7  50   ? -52.189 -47.607  74.209  1.00 64.26  ?  50   VAL G CG1 1 
ATOM   18679 C  CG2 . VAL G 7  50   ? -54.120 -47.449  75.789  1.00 71.55  ?  50   VAL G CG2 1 
ATOM   18680 N  N   . LEU G 7  51   ? -49.938 -49.245  76.571  1.00 65.48  ?  51   LEU G N   1 
ATOM   18681 C  CA  . LEU G 7  51   ? -48.571 -49.679  76.301  1.00 67.50  ?  51   LEU G CA  1 
ATOM   18682 C  C   . LEU G 7  51   ? -48.426 -51.187  76.468  1.00 66.63  ?  51   LEU G C   1 
ATOM   18683 O  O   . LEU G 7  51   ? -47.705 -51.837  75.702  1.00 65.76  ?  51   LEU G O   1 
ATOM   18684 C  CB  . LEU G 7  51   ? -47.597 -48.938  77.217  1.00 60.80  ?  51   LEU G CB  1 
ATOM   18685 C  CG  . LEU G 7  51   ? -47.345 -47.468  76.880  1.00 54.95  ?  51   LEU G CG  1 
ATOM   18686 C  CD1 . LEU G 7  51   ? -46.695 -46.757  78.052  1.00 71.57  ?  51   LEU G CD1 1 
ATOM   18687 C  CD2 . LEU G 7  51   ? -46.480 -47.348  75.636  1.00 71.33  ?  51   LEU G CD2 1 
ATOM   18688 N  N   . LEU G 7  52   ? -49.105 -51.764  77.464  1.00 76.20  ?  52   LEU G N   1 
ATOM   18689 C  CA  . LEU G 7  52   ? -49.067 -53.213  77.634  1.00 74.05  ?  52   LEU G CA  1 
ATOM   18690 C  C   . LEU G 7  52   ? -49.806 -53.919  76.505  1.00 78.09  ?  52   LEU G C   1 
ATOM   18691 O  O   . LEU G 7  52   ? -49.378 -54.984  76.045  1.00 79.11  ?  52   LEU G O   1 
ATOM   18692 C  CB  . LEU G 7  52   ? -49.663 -53.601  78.987  1.00 74.50  ?  52   LEU G CB  1 
ATOM   18693 C  CG  . LEU G 7  52   ? -49.645 -55.092  79.334  1.00 68.22  ?  52   LEU G CG  1 
ATOM   18694 C  CD1 . LEU G 7  52   ? -48.218 -55.619  79.375  1.00 64.28  ?  52   LEU G CD1 1 
ATOM   18695 C  CD2 . LEU G 7  52   ? -50.356 -55.348  80.653  1.00 73.63  ?  52   LEU G CD2 1 
ATOM   18696 N  N   . ALA G 7  53   ? -50.918 -53.342  76.043  1.00 102.70 ?  53   ALA G N   1 
ATOM   18697 C  CA  . ALA G 7  53   ? -51.668 -53.946  74.949  1.00 101.91 ?  53   ALA G CA  1 
ATOM   18698 C  C   . ALA G 7  53   ? -50.907 -53.893  73.632  1.00 105.42 ?  53   ALA G C   1 
ATOM   18699 O  O   . ALA G 7  53   ? -51.174 -54.705  72.740  1.00 101.33 ?  53   ALA G O   1 
ATOM   18700 C  CB  . ALA G 7  53   ? -53.025 -53.259  74.801  1.00 106.07 ?  53   ALA G CB  1 
ATOM   18701 N  N   . GLY G 7  54   ? -49.965 -52.960  73.493  1.00 111.41 ?  54   GLY G N   1 
ATOM   18702 C  CA  . GLY G 7  54   ? -49.179 -52.899  72.273  1.00 107.91 ?  54   GLY G CA  1 
ATOM   18703 C  C   . GLY G 7  54   ? -48.181 -54.037  72.166  1.00 104.11 ?  54   GLY G C   1 
ATOM   18704 O  O   . GLY G 7  54   ? -47.994 -54.611  71.089  1.00 103.32 ?  54   GLY G O   1 
ATOM   18705 N  N   . ARG G 7  55   ? -47.520 -54.373  73.275  1.00 83.56  ?  55   ARG G N   1 
ATOM   18706 C  CA  . ARG G 7  55   ? -46.587 -55.491  73.336  1.00 86.98  ?  55   ARG G CA  1 
ATOM   18707 C  C   . ARG G 7  55   ? -47.248 -56.752  73.870  1.00 90.93  ?  55   ARG G C   1 
ATOM   18708 O  O   . ARG G 7  55   ? -46.575 -57.600  74.467  1.00 83.01  ?  55   ARG G O   1 
ATOM   18709 C  CB  . ARG G 7  55   ? -45.376 -55.135  74.200  1.00 83.52  ?  55   ARG G CB  1 
ATOM   18710 C  CG  . ARG G 7  55   ? -44.528 -54.018  73.633  1.00 96.34  ?  55   ARG G CG  1 
ATOM   18711 C  CD  . ARG G 7  55   ? -43.049 -54.361  73.553  1.00 101.53 ?  55   ARG G CD  1 
ATOM   18712 N  NE  . ARG G 7  55   ? -42.786 -55.495  72.679  1.00 105.95 ?  55   ARG G NE  1 
ATOM   18713 C  CZ  . ARG G 7  55   ? -42.722 -55.413  71.357  1.00 105.94 ?  55   ARG G CZ  1 
ATOM   18714 N  NH1 . ARG G 7  55   ? -42.955 -54.275  70.724  1.00 91.83  ?  55   ARG G NH1 1 
ATOM   18715 N  NH2 . ARG G 7  55   ? -42.417 -56.499  70.653  1.00 114.83 ?  55   ARG G NH2 1 
ATOM   18716 N  N   . LEU G 7  56   ? -48.560 -56.879  73.677  1.00 206.72 ?  56   LEU G N   1 
ATOM   18717 C  CA  . LEU G 7  56   ? -49.304 -57.973  74.300  1.00 211.48 ?  56   LEU G CA  1 
ATOM   18718 C  C   . LEU G 7  56   ? -48.850 -59.353  73.838  1.00 218.90 ?  56   LEU G C   1 
ATOM   18719 O  O   . LEU G 7  56   ? -48.626 -60.220  74.703  1.00 220.64 ?  56   LEU G O   1 
ATOM   18720 C  CB  . LEU G 7  56   ? -50.804 -57.769  74.073  1.00 206.52 ?  56   LEU G CB  1 
ATOM   18721 C  CG  . LEU G 7  56   ? -51.722 -58.652  74.915  1.00 208.02 ?  56   LEU G CG  1 
ATOM   18722 C  CD1 . LEU G 7  56   ? -51.296 -58.605  76.371  1.00 210.04 ?  56   LEU G CD1 1 
ATOM   18723 C  CD2 . LEU G 7  56   ? -53.172 -58.225  74.754  1.00 213.85 ?  56   LEU G CD2 1 
ATOM   18724 N  N   . PRO G 7  57   ? -48.697 -59.643  72.526  1.00 119.14 ?  57   PRO G N   1 
ATOM   18725 C  CA  . PRO G 7  57   ? -48.206 -60.975  72.140  1.00 110.01 ?  57   PRO G CA  1 
ATOM   18726 C  C   . PRO G 7  57   ? -46.781 -61.220  72.609  1.00 107.50 ?  57   PRO G C   1 
ATOM   18727 O  O   . PRO G 7  57   ? -45.824 -60.947  71.878  1.00 111.56 ?  57   PRO G O   1 
ATOM   18728 C  CB  . PRO G 7  57   ? -48.301 -60.963  70.606  1.00 97.29  ?  57   PRO G CB  1 
ATOM   18729 C  CG  . PRO G 7  57   ? -49.241 -59.857  70.282  1.00 96.57  ?  57   PRO G CG  1 
ATOM   18730 C  CD  . PRO G 7  57   ? -49.026 -58.829  71.342  1.00 101.44 ?  57   PRO G CD  1 
ATOM   18731 N  N   . PHE G 7  58   ? -46.636 -61.728  73.832  1.00 86.99  ?  58   PHE G N   1 
ATOM   18732 C  CA  . PHE G 7  58   ? -45.320 -62.004  74.389  1.00 79.78  ?  58   PHE G CA  1 
ATOM   18733 C  C   . PHE G 7  58   ? -44.590 -63.047  73.548  1.00 79.05  ?  58   PHE G C   1 
ATOM   18734 O  O   . PHE G 7  58   ? -45.195 -63.812  72.791  1.00 83.45  ?  58   PHE G O   1 
ATOM   18735 C  CB  . PHE G 7  58   ? -45.441 -62.491  75.834  1.00 83.83  ?  58   PHE G CB  1 
ATOM   18736 C  CG  . PHE G 7  58   ? -46.029 -61.474  76.772  1.00 93.96  ?  58   PHE G CG  1 
ATOM   18737 C  CD1 . PHE G 7  58   ? -45.319 -60.336  77.119  1.00 85.86  ?  58   PHE G CD1 1 
ATOM   18738 C  CD2 . PHE G 7  58   ? -47.295 -61.656  77.305  1.00 96.51  ?  58   PHE G CD2 1 
ATOM   18739 C  CE1 . PHE G 7  58   ? -45.860 -59.400  77.982  1.00 74.74  ?  58   PHE G CE1 1 
ATOM   18740 C  CE2 . PHE G 7  58   ? -47.841 -60.724  78.167  1.00 86.20  ?  58   PHE G CE2 1 
ATOM   18741 C  CZ  . PHE G 7  58   ? -47.123 -59.595  78.506  1.00 78.08  ?  58   PHE G CZ  1 
ATOM   18742 N  N   . THR G 7  59   ? -43.269 -63.070  73.687  1.00 68.23  ?  59   THR G N   1 
ATOM   18743 C  CA  . THR G 7  59   ? -42.466 -64.027  72.941  1.00 71.03  ?  59   THR G CA  1 
ATOM   18744 C  C   . THR G 7  59   ? -42.807 -65.451  73.381  1.00 75.46  ?  59   THR G C   1 
ATOM   18745 O  O   . THR G 7  59   ? -42.867 -65.727  74.588  1.00 82.34  ?  59   THR G O   1 
ATOM   18746 C  CB  . THR G 7  59   ? -40.972 -63.742  73.125  1.00 66.34  ?  59   THR G CB  1 
ATOM   18747 O  OG1 . THR G 7  59   ? -40.201 -64.725  72.423  1.00 69.31  ?  59   THR G OG1 1 
ATOM   18748 C  CG2 . THR G 7  59   ? -40.578 -63.721  74.601  1.00 73.88  ?  59   THR G CG2 1 
ATOM   18749 N  N   . PRO G 7  60   ? -43.070 -66.363  72.448  1.00 90.30  ?  60   PRO G N   1 
ATOM   18750 C  CA  . PRO G 7  60   ? -43.454 -67.723  72.837  1.00 85.29  ?  60   PRO G CA  1 
ATOM   18751 C  C   . PRO G 7  60   ? -42.312 -68.459  73.519  1.00 89.71  ?  60   PRO G C   1 
ATOM   18752 O  O   . PRO G 7  60   ? -41.133 -68.174  73.298  1.00 87.77  ?  60   PRO G O   1 
ATOM   18753 C  CB  . PRO G 7  60   ? -43.822 -68.387  71.504  1.00 80.93  ?  60   PRO G CB  1 
ATOM   18754 C  CG  . PRO G 7  60   ? -44.111 -67.248  70.573  1.00 78.79  ?  60   PRO G CG  1 
ATOM   18755 C  CD  . PRO G 7  60   ? -43.184 -66.151  70.996  1.00 82.71  ?  60   PRO G CD  1 
ATOM   18756 N  N   . GLN G 7  61   ? -42.684 -69.417  74.366  1.00 118.92 ?  61   GLN G N   1 
ATOM   18757 C  CA  . GLN G 7  61   ? -41.737 -70.279  75.070  1.00 120.28 ?  61   GLN G CA  1 
ATOM   18758 C  C   . GLN G 7  61   ? -42.063 -71.721  74.707  1.00 116.30 ?  61   GLN G C   1 
ATOM   18759 O  O   . GLN G 7  61   ? -42.906 -72.360  75.357  1.00 114.23 ?  61   GLN G O   1 
ATOM   18760 C  CB  . GLN G 7  61   ? -41.802 -70.056  76.579  1.00 135.16 ?  61   GLN G CB  1 
ATOM   18761 C  CG  . GLN G 7  61   ? -41.048 -68.826  77.055  1.00 132.08 ?  61   GLN G CG  1 
ATOM   18762 C  CD  . GLN G 7  61   ? -41.833 -68.019  78.070  1.00 144.09 ?  61   GLN G CD  1 
ATOM   18763 O  OE1 . GLN G 7  61   ? -42.647 -68.562  78.816  1.00 150.88 ?  61   GLN G OE1 1 
ATOM   18764 N  NE2 . GLN G 7  61   ? -41.593 -66.713  78.101  1.00 149.31 ?  61   GLN G NE2 1 
ATOM   18765 N  N   . PRO G 7  62   ? -41.430 -72.271  73.671  1.00 93.36  ?  62   PRO G N   1 
ATOM   18766 C  CA  . PRO G 7  62   ? -41.731 -73.649  73.270  1.00 92.52  ?  62   PRO G CA  1 
ATOM   18767 C  C   . PRO G 7  62   ? -41.343 -74.642  74.353  1.00 95.05  ?  62   PRO G C   1 
ATOM   18768 O  O   . PRO G 7  62   ? -40.447 -74.396  75.164  1.00 98.77  ?  62   PRO G O   1 
ATOM   18769 C  CB  . PRO G 7  62   ? -40.881 -73.841  72.008  1.00 90.73  ?  62   PRO G CB  1 
ATOM   18770 C  CG  . PRO G 7  62   ? -40.673 -72.446  71.492  1.00 93.04  ?  62   PRO G CG  1 
ATOM   18771 C  CD  . PRO G 7  62   ? -40.488 -71.631  72.738  1.00 92.97  ?  62   PRO G CD  1 
ATOM   18772 N  N   . ALA G 7  63   ? -42.039 -75.774  74.361  1.00 106.24 ?  63   ALA G N   1 
ATOM   18773 C  CA  . ALA G 7  63   ? -41.743 -76.813  75.333  1.00 114.30 ?  63   ALA G CA  1 
ATOM   18774 C  C   . ALA G 7  63   ? -40.337 -77.359  75.095  1.00 121.53 ?  63   ALA G C   1 
ATOM   18775 O  O   . ALA G 7  63   ? -39.890 -77.441  73.944  1.00 127.59 ?  63   ALA G O   1 
ATOM   18776 C  CB  . ALA G 7  63   ? -42.770 -77.943  75.243  1.00 120.91 ?  63   ALA G CB  1 
ATOM   18777 N  N   . PRO G 7  64   ? -39.609 -77.722  76.150  1.00 102.77 ?  64   PRO G N   1 
ATOM   18778 C  CA  . PRO G 7  64   ? -38.271 -78.287  75.955  1.00 107.67 ?  64   PRO G CA  1 
ATOM   18779 C  C   . PRO G 7  64   ? -38.338 -79.595  75.183  1.00 117.77 ?  64   PRO G C   1 
ATOM   18780 O  O   . PRO G 7  64   ? -39.301 -80.359  75.292  1.00 123.54 ?  64   PRO G O   1 
ATOM   18781 C  CB  . PRO G 7  64   ? -37.760 -78.504  77.386  1.00 108.59 ?  64   PRO G CB  1 
ATOM   18782 C  CG  . PRO G 7  64   ? -38.617 -77.623  78.244  1.00 115.41 ?  64   PRO G CG  1 
ATOM   18783 C  CD  . PRO G 7  64   ? -39.954 -77.585  77.574  1.00 102.80 ?  64   PRO G CD  1 
ATOM   18784 N  N   . VAL G 7  65   ? -37.298 -79.842  74.384  1.00 111.39 ?  65   VAL G N   1 
ATOM   18785 C  CA  . VAL G 7  65   ? -37.277 -81.035  73.551  1.00 115.05 ?  65   VAL G CA  1 
ATOM   18786 C  C   . VAL G 7  65   ? -37.229 -82.283  74.428  1.00 123.57 ?  65   VAL G C   1 
ATOM   18787 O  O   . VAL G 7  65   ? -36.724 -82.262  75.559  1.00 115.88 ?  65   VAL G O   1 
ATOM   18788 C  CB  . VAL G 7  65   ? -36.086 -81.004  72.578  1.00 96.66  ?  65   VAL G CB  1 
ATOM   18789 C  CG1 . VAL G 7  65   ? -36.254 -79.880  71.573  1.00 82.30  ?  65   VAL G CG1 1 
ATOM   18790 C  CG2 . VAL G 7  65   ? -34.778 -80.849  73.340  1.00 103.62 ?  65   VAL G CG2 1 
ATOM   18791 N  N   . THR G 7  66   ? -37.769 -83.380  73.902  1.00 162.08 ?  66   THR G N   1 
ATOM   18792 C  CA  . THR G 7  66   ? -37.702 -84.651  74.602  1.00 160.83 ?  66   THR G CA  1 
ATOM   18793 C  C   . THR G 7  66   ? -36.253 -85.135  74.673  1.00 157.71 ?  66   THR G C   1 
ATOM   18794 O  O   . THR G 7  66   ? -35.352 -84.586  74.033  1.00 159.08 ?  66   THR G O   1 
ATOM   18795 C  CB  . THR G 7  66   ? -38.592 -85.690  73.918  1.00 150.53 ?  66   THR G CB  1 
ATOM   18796 O  OG1 . THR G 7  66   ? -38.576 -86.909  74.671  1.00 136.26 ?  66   THR G OG1 1 
ATOM   18797 C  CG2 . THR G 7  66   ? -38.105 -85.964  72.504  1.00 154.66 ?  66   THR G CG2 1 
ATOM   18798 N  N   . GLY G 7  67   ? -36.038 -86.187  75.465  1.00 186.22 ?  67   GLY G N   1 
ATOM   18799 C  CA  . GLY G 7  67   ? -34.679 -86.609  75.770  1.00 185.50 ?  67   GLY G CA  1 
ATOM   18800 C  C   . GLY G 7  67   ? -33.887 -87.032  74.547  1.00 186.40 ?  67   GLY G C   1 
ATOM   18801 O  O   . GLY G 7  67   ? -32.719 -86.665  74.397  1.00 179.12 ?  67   GLY G O   1 
ATOM   18802 N  N   . ASN G 7  68   ? -34.507 -87.804  73.658  1.00 134.33 ?  68   ASN G N   1 
ATOM   18803 C  CA  . ASN G 7  68   ? -33.793 -88.366  72.516  1.00 125.24 ?  68   ASN G CA  1 
ATOM   18804 C  C   . ASN G 7  68   ? -33.432 -87.270  71.520  1.00 127.63 ?  68   ASN G C   1 
ATOM   18805 O  O   . ASN G 7  68   ? -34.309 -86.545  71.037  1.00 125.73 ?  68   ASN G O   1 
ATOM   18806 C  CB  . ASN G 7  68   ? -34.642 -89.442  71.846  1.00 131.06 ?  68   ASN G CB  1 
ATOM   18807 C  CG  . ASN G 7  68   ? -33.845 -90.687  71.517  1.00 131.59 ?  68   ASN G CG  1 
ATOM   18808 O  OD1 . ASN G 7  68   ? -32.624 -90.714  71.668  1.00 125.45 ?  68   ASN G OD1 1 
ATOM   18809 N  ND2 . ASN G 7  68   ? -34.534 -91.728  71.064  1.00 140.32 ?  68   ASN G ND2 1 
ATOM   18810 N  N   . THR G 7  69   ? -32.142 -87.156  71.206  1.00 115.32 ?  69   THR G N   1 
ATOM   18811 C  CA  . THR G 7  69   ? -31.651 -86.163  70.261  1.00 103.48 ?  69   THR G CA  1 
ATOM   18812 C  C   . THR G 7  69   ? -30.527 -86.766  69.431  1.00 92.91  ?  69   THR G C   1 
ATOM   18813 O  O   . THR G 7  69   ? -30.014 -87.849  69.723  1.00 91.54  ?  69   THR G O   1 
ATOM   18814 C  CB  . THR G 7  69   ? -31.150 -84.896  70.969  1.00 108.91 ?  69   THR G CB  1 
ATOM   18815 O  OG1 . THR G 7  69   ? -30.521 -85.251  72.207  1.00 113.04 ?  69   THR G OG1 1 
ATOM   18816 C  CG2 . THR G 7  69   ? -32.300 -83.935  71.236  1.00 109.13 ?  69   THR G CG2 1 
ATOM   18817 N  N   . TYR G 7  70   ? -30.146 -86.038  68.381  1.00 83.12  ?  70   TYR G N   1 
ATOM   18818 C  CA  . TYR G 7  70   ? -29.028 -86.414  67.526  1.00 79.16  ?  70   TYR G CA  1 
ATOM   18819 C  C   . TYR G 7  70   ? -27.676 -86.098  68.147  1.00 75.96  ?  70   TYR G C   1 
ATOM   18820 O  O   . TYR G 7  70   ? -26.650 -86.524  67.606  1.00 72.82  ?  70   TYR G O   1 
ATOM   18821 C  CB  . TYR G 7  70   ? -29.121 -85.685  66.184  1.00 78.19  ?  70   TYR G CB  1 
ATOM   18822 C  CG  . TYR G 7  70   ? -28.761 -84.219  66.295  1.00 74.99  ?  70   TYR G CG  1 
ATOM   18823 C  CD1 . TYR G 7  70   ? -29.615 -83.319  66.919  1.00 79.78  ?  70   TYR G CD1 1 
ATOM   18824 C  CD2 . TYR G 7  70   ? -27.555 -83.738  65.798  1.00 69.65  ?  70   TYR G CD2 1 
ATOM   18825 C  CE1 . TYR G 7  70   ? -29.286 -81.982  67.035  1.00 73.93  ?  70   TYR G CE1 1 
ATOM   18826 C  CE2 . TYR G 7  70   ? -27.218 -82.402  65.910  1.00 66.44  ?  70   TYR G CE2 1 
ATOM   18827 C  CZ  . TYR G 7  70   ? -28.088 -81.530  66.530  1.00 65.72  ?  70   TYR G CZ  1 
ATOM   18828 O  OH  . TYR G 7  70   ? -27.763 -80.199  66.646  1.00 70.33  ?  70   TYR G OH  1 
ATOM   18829 N  N   . ARG G 7  71   ? -27.652 -85.351  69.253  1.00 105.25 ?  71   ARG G N   1 
ATOM   18830 C  CA  . ARG G 7  71   ? -26.393 -84.833  69.779  1.00 106.20 ?  71   ARG G CA  1 
ATOM   18831 C  C   . ARG G 7  71   ? -25.462 -85.957  70.213  1.00 103.68 ?  71   ARG G C   1 
ATOM   18832 O  O   . ARG G 7  71   ? -24.241 -85.861  70.044  1.00 102.04 ?  71   ARG G O   1 
ATOM   18833 C  CB  . ARG G 7  71   ? -26.672 -83.884  70.944  1.00 119.83 ?  71   ARG G CB  1 
ATOM   18834 C  CG  . ARG G 7  71   ? -27.016 -82.467  70.515  1.00 118.57 ?  71   ARG G CG  1 
ATOM   18835 C  CD  . ARG G 7  71   ? -27.556 -81.655  71.681  1.00 125.37 ?  71   ARG G CD  1 
ATOM   18836 N  NE  . ARG G 7  71   ? -27.759 -80.255  71.328  1.00 120.90 ?  71   ARG G NE  1 
ATOM   18837 C  CZ  . ARG G 7  71   ? -28.910 -79.750  70.905  1.00 118.75 ?  71   ARG G CZ  1 
ATOM   18838 N  NH1 . ARG G 7  71   ? -29.987 -80.505  70.771  1.00 119.56 ?  71   ARG G NH1 1 
ATOM   18839 N  NH2 . ARG G 7  71   ? -28.981 -78.455  70.611  1.00 116.35 ?  71   ARG G NH2 1 
ATOM   18840 N  N   . THR G 7  72   ? -26.020 -87.033  70.772  1.00 100.39 ?  72   THR G N   1 
ATOM   18841 C  CA  . THR G 7  72   ? -25.182 -88.134  71.234  1.00 100.13 ?  72   THR G CA  1 
ATOM   18842 C  C   . THR G 7  72   ? -24.543 -88.876  70.064  1.00 97.19  ?  72   THR G C   1 
ATOM   18843 O  O   . THR G 7  72   ? -23.396 -89.326  70.164  1.00 99.10  ?  72   THR G O   1 
ATOM   18844 C  CB  . THR G 7  72   ? -26.000 -89.088  72.109  1.00 93.80  ?  72   THR G CB  1 
ATOM   18845 O  OG1 . THR G 7  72   ? -25.226 -90.258  72.404  1.00 102.43 ?  72   THR G OG1 1 
ATOM   18846 C  CG2 . THR G 7  72   ? -27.296 -89.490  71.416  1.00 92.80  ?  72   THR G CG2 1 
ATOM   18847 N  N   . TYR G 7  73   ? -25.260 -89.004  68.944  1.00 81.33  ?  73   TYR G N   1 
ATOM   18848 C  CA  . TYR G 7  73   ? -24.680 -89.643  67.766  1.00 84.26  ?  73   TYR G CA  1 
ATOM   18849 C  C   . TYR G 7  73   ? -23.516 -88.827  67.217  1.00 84.42  ?  73   TYR G C   1 
ATOM   18850 O  O   . TYR G 7  73   ? -22.455 -89.373  66.895  1.00 83.55  ?  73   TYR G O   1 
ATOM   18851 C  CB  . TYR G 7  73   ? -25.748 -89.836  66.687  1.00 88.72  ?  73   TYR G CB  1 
ATOM   18852 C  CG  . TYR G 7  73   ? -26.796 -90.877  67.011  1.00 92.98  ?  73   TYR G CG  1 
ATOM   18853 C  CD1 . TYR G 7  73   ? -26.597 -92.213  66.690  1.00 90.33  ?  73   TYR G CD1 1 
ATOM   18854 C  CD2 . TYR G 7  73   ? -27.989 -90.522  67.627  1.00 99.43  ?  73   TYR G CD2 1 
ATOM   18855 C  CE1 . TYR G 7  73   ? -27.553 -93.169  66.979  1.00 96.91  ?  73   TYR G CE1 1 
ATOM   18856 C  CE2 . TYR G 7  73   ? -28.951 -91.471  67.921  1.00 102.51 ?  73   TYR G CE2 1 
ATOM   18857 C  CZ  . TYR G 7  73   ? -28.728 -92.792  67.595  1.00 100.12 ?  73   TYR G CZ  1 
ATOM   18858 O  OH  . TYR G 7  73   ? -29.684 -93.739  67.886  1.00 95.24  ?  73   TYR G OH  1 
ATOM   18859 N  N   . VAL G 7  74   ? -23.699 -87.510  67.108  1.00 105.13 ?  74   VAL G N   1 
ATOM   18860 C  CA  . VAL G 7  74   ? -22.677 -86.663  66.502  1.00 99.16  ?  74   VAL G CA  1 
ATOM   18861 C  C   . VAL G 7  74   ? -21.453 -86.567  67.405  1.00 98.53  ?  74   VAL G C   1 
ATOM   18862 O  O   . VAL G 7  74   ? -20.311 -86.607  66.929  1.00 100.45 ?  74   VAL G O   1 
ATOM   18863 C  CB  . VAL G 7  74   ? -23.263 -85.276  66.183  1.00 96.16  ?  74   VAL G CB  1 
ATOM   18864 C  CG1 . VAL G 7  74   ? -22.160 -84.301  65.793  1.00 101.61 ?  74   VAL G CG1 1 
ATOM   18865 C  CG2 . VAL G 7  74   ? -24.306 -85.383  65.081  1.00 100.85 ?  74   VAL G CG2 1 
ATOM   18866 N  N   . ASN G 7  75   ? -21.665 -86.443  68.718  1.00 83.43  ?  75   ASN G N   1 
ATOM   18867 C  CA  . ASN G 7  75   ? -20.538 -86.361  69.642  1.00 81.11  ?  75   ASN G CA  1 
ATOM   18868 C  C   . ASN G 7  75   ? -19.718 -87.645  69.631  1.00 76.36  ?  75   ASN G C   1 
ATOM   18869 O  O   . ASN G 7  75   ? -18.482 -87.601  69.637  1.00 73.65  ?  75   ASN G O   1 
ATOM   18870 C  CB  . ASN G 7  75   ? -21.034 -86.056  71.057  1.00 78.50  ?  75   ASN G CB  1 
ATOM   18871 C  CG  . ASN G 7  75   ? -21.601 -84.656  71.189  1.00 77.38  ?  75   ASN G CG  1 
ATOM   18872 O  OD1 . ASN G 7  75   ? -21.196 -83.739  70.474  1.00 82.03  ?  75   ASN G OD1 1 
ATOM   18873 N  ND2 . ASN G 7  75   ? -22.543 -84.484  72.109  1.00 79.00  ?  75   ASN G ND2 1 
ATOM   18874 N  N   . ASP G 7  76   ? -20.387 -88.801  69.612  1.00 118.26 ?  76   ASP G N   1 
ATOM   18875 C  CA  . ASP G 7  76   ? -19.668 -90.072  69.593  1.00 126.51 ?  76   ASP G CA  1 
ATOM   18876 C  C   . ASP G 7  76   ? -18.889 -90.254  68.296  1.00 126.21 ?  76   ASP G C   1 
ATOM   18877 O  O   . ASP G 7  76   ? -17.745 -90.722  68.313  1.00 127.03 ?  76   ASP G O   1 
ATOM   18878 C  CB  . ASP G 7  76   ? -20.643 -91.233  69.792  1.00 123.04 ?  76   ASP G CB  1 
ATOM   18879 C  CG  . ASP G 7  76   ? -21.277 -91.234  71.167  1.00 132.98 ?  76   ASP G CG  1 
ATOM   18880 O  OD1 . ASP G 7  76   ? -20.812 -90.468  72.038  1.00 140.53 ?  76   ASP G OD1 1 
ATOM   18881 O  OD2 . ASP G 7  76   ? -22.242 -92.001  71.376  1.00 137.66 -1 76   ASP G OD2 1 
ATOM   18882 N  N   . ALA G 7  77   ? -19.491 -89.888  67.162  1.00 110.64 ?  77   ALA G N   1 
ATOM   18883 C  CA  . ALA G 7  77   ? -18.837 -90.106  65.876  1.00 106.55 ?  77   ALA G CA  1 
ATOM   18884 C  C   . ALA G 7  77   ? -17.640 -89.181  65.694  1.00 96.20  ?  77   ALA G C   1 
ATOM   18885 O  O   . ALA G 7  77   ? -16.588 -89.610  65.206  1.00 96.16  ?  77   ALA G O   1 
ATOM   18886 C  CB  . ALA G 7  77   ? -19.840 -89.917  64.740  1.00 105.61 ?  77   ALA G CB  1 
ATOM   18887 N  N   . ARG G 7  78   ? -17.777 -87.909  66.075  1.00 73.88  ?  78   ARG G N   1 
ATOM   18888 C  CA  . ARG G 7  78   ? -16.653 -86.987  65.957  1.00 74.57  ?  78   ARG G CA  1 
ATOM   18889 C  C   . ARG G 7  78   ? -15.536 -87.336  66.933  1.00 87.63  ?  78   ARG G C   1 
ATOM   18890 O  O   . ARG G 7  78   ? -14.358 -87.134  66.620  1.00 86.72  ?  78   ARG G O   1 
ATOM   18891 C  CB  . ARG G 7  78   ? -17.123 -85.549  66.170  1.00 81.54  ?  78   ARG G CB  1 
ATOM   18892 C  CG  . ARG G 7  78   ? -18.039 -85.037  65.071  1.00 88.13  ?  78   ARG G CG  1 
ATOM   18893 C  CD  . ARG G 7  78   ? -17.569 -83.693  64.538  1.00 92.16  ?  78   ARG G CD  1 
ATOM   18894 N  NE  . ARG G 7  78   ? -17.869 -82.602  65.457  1.00 93.70  ?  78   ARG G NE  1 
ATOM   18895 C  CZ  . ARG G 7  78   ? -18.899 -81.776  65.327  1.00 103.35 ?  78   ARG G CZ  1 
ATOM   18896 N  NH1 . ARG G 7  78   ? -19.750 -81.886  64.320  1.00 101.66 ?  78   ARG G NH1 1 
ATOM   18897 N  NH2 . ARG G 7  78   ? -19.077 -80.815  66.229  1.00 110.15 ?  78   ARG G NH2 1 
ATOM   18898 N  N   . THR G 7  79   ? -15.882 -87.855  68.114  1.00 83.80  ?  79   THR G N   1 
ATOM   18899 C  CA  . THR G 7  79   ? -14.857 -88.373  69.014  1.00 79.39  ?  79   THR G CA  1 
ATOM   18900 C  C   . THR G 7  79   ? -14.170 -89.591  68.408  1.00 87.89  ?  79   THR G C   1 
ATOM   18901 O  O   . THR G 7  79   ? -12.960 -89.780  68.582  1.00 93.10  ?  79   THR G O   1 
ATOM   18902 C  CB  . THR G 7  79   ? -15.471 -88.724  70.371  1.00 83.46  ?  79   THR G CB  1 
ATOM   18903 O  OG1 . THR G 7  79   ? -16.209 -87.601  70.869  1.00 92.81  ?  79   THR G OG1 1 
ATOM   18904 C  CG2 . THR G 7  79   ? -14.385 -89.091  71.372  1.00 85.74  ?  79   THR G CG2 1 
ATOM   18905 N  N   . LEU G 7  80   ? -14.928 -90.423  67.690  1.00 83.85  ?  80   LEU G N   1 
ATOM   18906 C  CA  . LEU G 7  80   ? -14.333 -91.556  66.988  1.00 84.24  ?  80   LEU G CA  1 
ATOM   18907 C  C   . LEU G 7  80   ? -13.417 -91.089  65.865  1.00 79.84  ?  80   LEU G C   1 
ATOM   18908 O  O   . LEU G 7  80   ? -12.393 -91.724  65.587  1.00 81.08  ?  80   LEU G O   1 
ATOM   18909 C  CB  . LEU G 7  80   ? -15.429 -92.466  66.434  1.00 87.39  ?  80   LEU G CB  1 
ATOM   18910 C  CG  . LEU G 7  80   ? -15.005 -93.885  66.047  1.00 85.30  ?  80   LEU G CG  1 
ATOM   18911 C  CD1 . LEU G 7  80   ? -14.706 -94.714  67.287  1.00 97.52  ?  80   LEU G CD1 1 
ATOM   18912 C  CD2 . LEU G 7  80   ? -16.072 -94.553  65.194  1.00 78.83  ?  80   LEU G CD2 1 
ATOM   18913 N  N   . LEU G 7  81   ? -13.767 -89.982  65.212  1.00 82.91  ?  81   LEU G N   1 
ATOM   18914 C  CA  . LEU G 7  81   ? -12.964 -89.426  64.126  1.00 83.86  ?  81   LEU G CA  1 
ATOM   18915 C  C   . LEU G 7  81   ? -11.673 -88.772  64.617  1.00 86.07  ?  81   LEU G C   1 
ATOM   18916 O  O   . LEU G 7  81   ? -10.972 -88.151  63.808  1.00 90.39  ?  81   LEU G O   1 
ATOM   18917 C  CB  . LEU G 7  81   ? -13.795 -88.421  63.326  1.00 75.51  ?  81   LEU G CB  1 
ATOM   18918 C  CG  . LEU G 7  81   ? -14.822 -89.017  62.357  1.00 71.05  ?  81   LEU G CG  1 
ATOM   18919 C  CD1 . LEU G 7  81   ? -15.430 -87.939  61.469  1.00 69.29  ?  81   LEU G CD1 1 
ATOM   18920 C  CD2 . LEU G 7  81   ? -14.204 -90.125  61.516  1.00 67.73  ?  81   LEU G CD2 1 
ATOM   18921 N  N   . ASN G 7  82   ? -11.353 -88.889  65.906  1.00 85.98  ?  82   ASN G N   1 
ATOM   18922 C  CA  . ASN G 7  82   ? -10.096 -88.408  66.462  1.00 89.28  ?  82   ASN G CA  1 
ATOM   18923 C  C   . ASN G 7  82   ? -9.583  -89.437  67.463  1.00 90.47  ?  82   ASN G C   1 
ATOM   18924 O  O   . ASN G 7  82   ? -10.202 -90.483  67.683  1.00 85.13  ?  82   ASN G O   1 
ATOM   18925 C  CB  . ASN G 7  82   ? -10.260 -87.034  67.126  1.00 82.36  ?  82   ASN G CB  1 
ATOM   18926 C  CG  . ASN G 7  82   ? -10.779 -85.978  66.170  1.00 86.93  ?  82   ASN G CG  1 
ATOM   18927 O  OD1 . ASN G 7  82   ? -11.755 -85.287  66.462  1.00 86.39  ?  82   ASN G OD1 1 
ATOM   18928 N  ND2 . ASN G 7  82   ? -10.126 -85.846  65.022  1.00 94.93  ?  82   ASN G ND2 1 
ATOM   18929 N  N   . SER G 7  83   ? -8.429  -89.135  68.058  1.00 169.41 ?  83   SER G N   1 
ATOM   18930 C  CA  . SER G 7  83   ? -7.862  -89.887  69.178  1.00 181.82 ?  83   SER G CA  1 
ATOM   18931 C  C   . SER G 7  83   ? -7.498  -91.326  68.817  1.00 186.85 ?  83   SER G C   1 
ATOM   18932 O  O   . SER G 7  83   ? -7.355  -92.167  69.711  1.00 185.13 ?  83   SER G O   1 
ATOM   18933 C  CB  . SER G 7  83   ? -8.808  -89.876  70.385  1.00 185.85 ?  83   SER G CB  1 
ATOM   18934 O  OG  . SER G 7  83   ? -9.752  -90.931  70.300  1.00 187.19 ?  83   SER G OG  1 
ATOM   18935 N  N   . TYR G 7  84   ? -7.340  -91.626  67.525  1.00 119.44 ?  84   TYR G N   1 
ATOM   18936 C  CA  . TYR G 7  84   ? -6.910  -92.945  67.067  1.00 113.86 ?  84   TYR G CA  1 
ATOM   18937 C  C   . TYR G 7  84   ? -7.806  -94.053  67.611  1.00 115.22 ?  84   TYR G C   1 
ATOM   18938 O  O   . TYR G 7  84   ? -9.032  -93.906  67.646  1.00 116.43 ?  84   TYR G O   1 
ATOM   18939 C  CB  . TYR G 7  84   ? -5.451  -93.196  67.462  1.00 104.03 ?  84   TYR G CB  1 
ATOM   18940 C  CG  . TYR G 7  84   ? -4.470  -92.245  66.812  1.00 104.64 ?  84   TYR G CG  1 
ATOM   18941 C  CD1 . TYR G 7  84   ? -4.183  -91.012  67.386  1.00 108.75 ?  84   TYR G CD1 1 
ATOM   18942 C  CD2 . TYR G 7  84   ? -3.828  -92.580  65.627  1.00 97.37  ?  84   TYR G CD2 1 
ATOM   18943 C  CE1 . TYR G 7  84   ? -3.288  -90.139  66.797  1.00 110.26 ?  84   TYR G CE1 1 
ATOM   18944 C  CE2 . TYR G 7  84   ? -2.930  -91.713  65.029  1.00 88.35  ?  84   TYR G CE2 1 
ATOM   18945 C  CZ  . TYR G 7  84   ? -2.665  -90.494  65.619  1.00 101.52 ?  84   TYR G CZ  1 
ATOM   18946 O  OH  . TYR G 7  84   ? -1.774  -89.627  65.030  1.00 110.43 ?  84   TYR G OH  1 
ATOM   18947 N  N   . GLY G 7  85   ? -7.208  -95.163  68.028  1.00 75.16  ?  85   GLY G N   1 
ATOM   18948 C  CA  . GLY G 7  85   ? -7.937  -96.281  68.596  1.00 78.39  ?  85   GLY G CA  1 
ATOM   18949 C  C   . GLY G 7  85   ? -7.849  -97.521  67.720  1.00 81.15  ?  85   GLY G C   1 
ATOM   18950 O  O   . GLY G 7  85   ? -7.249  -97.524  66.644  1.00 83.62  ?  85   GLY G O   1 
ATOM   18951 N  N   . TYR G 7  86   ? -8.466  -98.591  68.219  1.00 132.07 ?  86   TYR G N   1 
ATOM   18952 C  CA  . TYR G 7  86   ? -8.539  -99.870  67.523  1.00 129.10 ?  86   TYR G CA  1 
ATOM   18953 C  C   . TYR G 7  86   ? -9.999  -100.220 67.274  1.00 125.09 ?  86   TYR G C   1 
ATOM   18954 O  O   . TYR G 7  86   ? -10.804 -100.240 68.211  1.00 118.07 ?  86   TYR G O   1 
ATOM   18955 C  CB  . TYR G 7  86   ? -7.866  -100.987 68.331  1.00 127.23 ?  86   TYR G CB  1 
ATOM   18956 C  CG  . TYR G 7  86   ? -6.411  -100.743 68.672  1.00 139.85 ?  86   TYR G CG  1 
ATOM   18957 C  CD1 . TYR G 7  86   ? -5.606  -99.952  67.862  1.00 146.94 ?  86   TYR G CD1 1 
ATOM   18958 C  CD2 . TYR G 7  86   ? -5.842  -101.307 69.806  1.00 142.40 ?  86   TYR G CD2 1 
ATOM   18959 C  CE1 . TYR G 7  86   ? -4.277  -99.729  68.173  1.00 146.88 ?  86   TYR G CE1 1 
ATOM   18960 C  CE2 . TYR G 7  86   ? -4.514  -101.090 70.125  1.00 144.61 ?  86   TYR G CE2 1 
ATOM   18961 C  CZ  . TYR G 7  86   ? -3.737  -100.300 69.305  1.00 142.84 ?  86   TYR G CZ  1 
ATOM   18962 O  OH  . TYR G 7  86   ? -2.415  -100.081 69.618  1.00 130.24 ?  86   TYR G OH  1 
ATOM   18963 N  N   . THR G 7  87   ? -10.337 -100.500 66.018  1.00 168.16 ?  87   THR G N   1 
ATOM   18964 C  CA  . THR G 7  87   ? -11.701 -100.873 65.676  1.00 171.78 ?  87   THR G CA  1 
ATOM   18965 C  C   . THR G 7  87   ? -11.948 -102.344 66.009  1.00 169.90 ?  87   THR G C   1 
ATOM   18966 O  O   . THR G 7  87   ? -11.050 -103.077 66.434  1.00 174.23 ?  87   THR G O   1 
ATOM   18967 C  CB  . THR G 7  87   ? -11.983 -100.582 64.203  1.00 173.40 ?  87   THR G CB  1 
ATOM   18968 O  OG1 . THR G 7  87   ? -13.366 -100.833 63.919  1.00 171.54 ?  87   THR G OG1 1 
ATOM   18969 C  CG2 . THR G 7  87   ? -11.116 -101.442 63.309  1.00 174.22 ?  87   THR G CG2 1 
ATOM   18970 N  N   . MET G 7  88   ? -13.192 -102.782 65.808  1.00 120.96 ?  88   MET G N   1 
ATOM   18971 C  CA  . MET G 7  88   ? -13.587 -104.120 66.236  1.00 126.07 ?  88   MET G CA  1 
ATOM   18972 C  C   . MET G 7  88   ? -12.979 -105.194 65.342  1.00 125.83 ?  88   MET G C   1 
ATOM   18973 O  O   . MET G 7  88   ? -12.303 -106.109 65.827  1.00 134.53 ?  88   MET G O   1 
ATOM   18974 C  CB  . MET G 7  88   ? -15.113 -104.230 66.257  1.00 129.37 ?  88   MET G CB  1 
ATOM   18975 C  CG  . MET G 7  88   ? -15.756 -103.666 67.518  1.00 134.51 ?  88   MET G CG  1 
ATOM   18976 S  SD  . MET G 7  88   ? -17.555 -103.577 67.419  1.00 141.42 ?  88   MET G SD  1 
ATOM   18977 C  CE  . MET G 7  88   ? -17.797 -101.821 67.162  1.00 130.09 ?  88   MET G CE  1 
ATOM   18978 N  N   . GLU G 7  89   ? -13.203 -105.100 64.035  1.00 135.88 ?  89   GLU G N   1 
ATOM   18979 C  CA  . GLU G 7  89   ? -12.772 -106.132 63.101  1.00 137.95 ?  89   GLU G CA  1 
ATOM   18980 C  C   . GLU G 7  89   ? -11.418 -105.846 62.465  1.00 140.36 ?  89   GLU G C   1 
ATOM   18981 O  O   . GLU G 7  89   ? -10.923 -106.680 61.700  1.00 145.45 ?  89   GLU G O   1 
ATOM   18982 C  CB  . GLU G 7  89   ? -13.824 -106.316 62.001  1.00 144.91 ?  89   GLU G CB  1 
ATOM   18983 C  CG  . GLU G 7  89   ? -14.255 -105.021 61.322  1.00 142.69 ?  89   GLU G CG  1 
ATOM   18984 C  CD  . GLU G 7  89   ? -13.446 -104.714 60.073  1.00 148.96 ?  89   GLU G CD  1 
ATOM   18985 O  OE1 . GLU G 7  89   ? -12.911 -105.662 59.459  1.00 152.47 ?  89   GLU G OE1 1 
ATOM   18986 O  OE2 . GLU G 7  89   ? -13.345 -103.525 59.704  1.00 139.96 -1 89   GLU G OE2 1 
ATOM   18987 N  N   . GLY G 7  90   ? -10.803 -104.703 62.761  1.00 129.69 ?  90   GLY G N   1 
ATOM   18988 C  CA  . GLY G 7  90   ? -9.570  -104.332 62.094  1.00 136.22 ?  90   GLY G CA  1 
ATOM   18989 C  C   . GLY G 7  90   ? -8.384  -104.135 63.015  1.00 128.89 ?  90   GLY G C   1 
ATOM   18990 O  O   . GLY G 7  90   ? -8.302  -104.754 64.080  1.00 115.31 ?  90   GLY G O   1 
ATOM   18991 N  N   . LYS G 7  91   ? -7.459  -103.264 62.612  1.00 234.16 ?  91   LYS G N   1 
ATOM   18992 C  CA  . LYS G 7  91   ? -6.198  -103.073 63.316  1.00 245.60 ?  91   LYS G CA  1 
ATOM   18993 C  C   . LYS G 7  91   ? -6.159  -101.769 64.103  1.00 238.36 ?  91   LYS G C   1 
ATOM   18994 O  O   . LYS G 7  91   ? -6.022  -101.794 65.330  1.00 241.06 ?  91   LYS G O   1 
ATOM   18995 C  CB  . LYS G 7  91   ? -5.032  -103.129 62.318  1.00 245.19 ?  91   LYS G CB  1 
ATOM   18996 N  N   . VAL G 7  92   ? -6.273  -100.622 63.433  1.00 88.76  ?  92   VAL G N   1 
ATOM   18997 C  CA  . VAL G 7  92   ? -6.056  -99.334  64.080  1.00 90.81  ?  92   VAL G CA  1 
ATOM   18998 C  C   . VAL G 7  92   ? -6.929  -98.281  63.409  1.00 85.35  ?  92   VAL G C   1 
ATOM   18999 O  O   . VAL G 7  92   ? -7.260  -98.383  62.224  1.00 75.80  ?  92   VAL G O   1 
ATOM   19000 C  CB  . VAL G 7  92   ? -4.557  -98.941  64.037  1.00 96.96  ?  92   VAL G CB  1 
ATOM   19001 C  CG1 . VAL G 7  92   ? -4.101  -98.695  62.602  1.00 91.83  ?  92   VAL G CG1 1 
ATOM   19002 C  CG2 . VAL G 7  92   ? -4.277  -97.731  64.924  1.00 98.83  ?  92   VAL G CG2 1 
ATOM   19003 N  N   . HIS G 7  93   ? -7.315  -97.274  64.187  1.00 136.26 ?  93   HIS G N   1 
ATOM   19004 C  CA  . HIS G 7  93   ? -8.024  -96.104  63.693  1.00 124.27 ?  93   HIS G CA  1 
ATOM   19005 C  C   . HIS G 7  93   ? -7.038  -95.044  63.215  1.00 120.90 ?  93   HIS G C   1 
ATOM   19006 O  O   . HIS G 7  93   ? -5.845  -95.080  63.526  1.00 123.94 ?  93   HIS G O   1 
ATOM   19007 C  CB  . HIS G 7  93   ? -8.912  -95.504  64.784  1.00 124.12 ?  93   HIS G CB  1 
ATOM   19008 C  CG  . HIS G 7  93   ? -10.229 -96.193  64.951  1.00 126.61 ?  93   HIS G CG  1 
ATOM   19009 N  ND1 . HIS G 7  93   ? -11.109 -95.872  65.961  1.00 116.40 ?  93   HIS G ND1 1 
ATOM   19010 C  CD2 . HIS G 7  93   ? -10.821 -97.177  64.234  1.00 132.05 ?  93   HIS G CD2 1 
ATOM   19011 C  CE1 . HIS G 7  93   ? -12.185 -96.632  65.863  1.00 123.84 ?  93   HIS G CE1 1 
ATOM   19012 N  NE2 . HIS G 7  93   ? -12.036 -97.431  64.822  1.00 132.69 ?  93   HIS G NE2 1 
ATOM   19013 N  N   . ILE G 7  94   ? -7.557  -94.091  62.449  1.00 106.95 ?  94   ILE G N   1 
ATOM   19014 C  CA  . ILE G 7  94   ? -6.804  -92.902  62.058  1.00 101.71 ?  94   ILE G CA  1 
ATOM   19015 C  C   . ILE G 7  94   ? -7.703  -91.690  62.273  1.00 100.07 ?  94   ILE G C   1 
ATOM   19016 O  O   . ILE G 7  94   ? -8.853  -91.684  61.810  1.00 101.19 ?  94   ILE G O   1 
ATOM   19017 C  CB  . ILE G 7  94   ? -6.315  -92.983  60.602  1.00 103.46 ?  94   ILE G CB  1 
ATOM   19018 C  CG1 . ILE G 7  94   ? -5.530  -94.276  60.357  1.00 97.24  ?  94   ILE G CG1 1 
ATOM   19019 C  CG2 . ILE G 7  94   ? -5.466  -91.765  60.256  1.00 99.52  ?  94   ILE G CG2 1 
ATOM   19020 C  CD1 . ILE G 7  94   ? -4.807  -94.314  59.026  1.00 107.28 ?  94   ILE G CD1 1 
ATOM   19021 N  N   . PRO G 7  95   ? -7.238  -90.657  62.971  1.00 72.08  ?  95   PRO G N   1 
ATOM   19022 C  CA  . PRO G 7  95   ? -8.079  -89.475  63.179  1.00 69.92  ?  95   PRO G CA  1 
ATOM   19023 C  C   . PRO G 7  95   ? -8.330  -88.734  61.877  1.00 79.64  ?  95   PRO G C   1 
ATOM   19024 O  O   . PRO G 7  95   ? -7.509  -88.747  60.956  1.00 84.53  ?  95   PRO G O   1 
ATOM   19025 C  CB  . PRO G 7  95   ? -7.258  -88.619  64.152  1.00 77.37  ?  95   PRO G CB  1 
ATOM   19026 C  CG  . PRO G 7  95   ? -6.271  -89.562  64.767  1.00 85.63  ?  95   PRO G CG  1 
ATOM   19027 C  CD  . PRO G 7  95   ? -5.961  -90.557  63.694  1.00 80.70  ?  95   PRO G CD  1 
ATOM   19028 N  N   . ILE G 7  96   ? -9.492  -88.082  61.807  1.00 150.36 ?  96   ILE G N   1 
ATOM   19029 C  CA  . ILE G 7  96   ? -9.779  -87.232  60.659  1.00 149.99 ?  96   ILE G CA  1 
ATOM   19030 C  C   . ILE G 7  96   ? -8.867  -86.008  60.687  1.00 156.32 ?  96   ILE G C   1 
ATOM   19031 O  O   . ILE G 7  96   ? -8.237  -85.685  61.703  1.00 156.83 ?  96   ILE G O   1 
ATOM   19032 C  CB  . ILE G 7  96   ? -11.263 -86.831  60.622  1.00 143.38 ?  96   ILE G CB  1 
ATOM   19033 C  CG1 . ILE G 7  96   ? -11.725 -86.637  59.176  1.00 137.41 ?  96   ILE G CG1 1 
ATOM   19034 C  CG2 . ILE G 7  96   ? -11.504 -85.571  61.441  1.00 154.82 ?  96   ILE G CG2 1 
ATOM   19035 C  CD1 . ILE G 7  96   ? -11.657 -87.898  58.343  1.00 129.33 ?  96   ILE G CD1 1 
ATOM   19036 N  N   . ASP G 7  97   ? -8.787  -85.329  59.543  1.00 142.65 ?  97   ASP G N   1 
ATOM   19037 C  CA  . ASP G 7  97   ? -7.828  -84.259  59.274  1.00 147.13 ?  97   ASP G CA  1 
ATOM   19038 C  C   . ASP G 7  97   ? -6.386  -84.753  59.310  1.00 144.95 ?  97   ASP G C   1 
ATOM   19039 O  O   . ASP G 7  97   ? -5.454  -83.942  59.267  1.00 143.57 ?  97   ASP G O   1 
ATOM   19040 C  CB  . ASP G 7  97   ? -8.007  -83.076  60.237  1.00 152.58 ?  97   ASP G CB  1 
ATOM   19041 C  CG  . ASP G 7  97   ? -7.597  -81.753  59.620  1.00 165.55 ?  97   ASP G CG  1 
ATOM   19042 O  OD1 . ASP G 7  97   ? -7.112  -81.757  58.469  1.00 157.29 ?  97   ASP G OD1 1 
ATOM   19043 O  OD2 . ASP G 7  97   ? -7.762  -80.709  60.286  1.00 181.19 -1 97   ASP G OD2 1 
ATOM   19044 N  N   . ARG G 7  98   ? -6.184  -86.063  59.398  1.00 81.78  ?  98   ARG G N   1 
ATOM   19045 C  CA  . ARG G 7  98   ? -4.883  -86.707  59.275  1.00 82.39  ?  98   ARG G CA  1 
ATOM   19046 C  C   . ARG G 7  98   ? -4.856  -87.746  58.169  1.00 79.02  ?  98   ARG G C   1 
ATOM   19047 O  O   . ARG G 7  98   ? -3.856  -87.858  57.456  1.00 77.94  ?  98   ARG G O   1 
ATOM   19048 C  CB  . ARG G 7  98   ? -4.483  -87.362  60.606  1.00 93.09  ?  98   ARG G CB  1 
ATOM   19049 C  CG  . ARG G 7  98   ? -3.251  -88.254  60.521  1.00 99.61  ?  98   ARG G CG  1 
ATOM   19050 C  CD  . ARG G 7  98   ? -1.992  -87.433  60.289  1.00 107.28 ?  98   ARG G CD  1 
ATOM   19051 N  NE  . ARG G 7  98   ? -0.965  -88.187  59.579  1.00 108.66 ?  98   ARG G NE  1 
ATOM   19052 C  CZ  . ARG G 7  98   ? -0.074  -88.976  60.164  1.00 99.24  ?  98   ARG G CZ  1 
ATOM   19053 N  NH1 . ARG G 7  98   ? -0.051  -89.138  61.477  1.00 110.17 ?  98   ARG G NH1 1 
ATOM   19054 N  NH2 . ARG G 7  98   ? 0.818   -89.615  59.414  1.00 91.37  ?  98   ARG G NH2 1 
ATOM   19055 N  N   . ALA G 7  99   ? -5.939  -88.508  58.003  1.00 96.03  ?  99   ALA G N   1 
ATOM   19056 C  CA  . ALA G 7  99   ? -6.046  -89.386  56.845  1.00 93.40  ?  99   ALA G CA  1 
ATOM   19057 C  C   . ALA G 7  99   ? -6.176  -88.588  55.556  1.00 91.97  ?  99   ALA G C   1 
ATOM   19058 O  O   . ALA G 7  99   ? -5.803  -89.079  54.486  1.00 97.93  ?  99   ALA G O   1 
ATOM   19059 C  CB  . ALA G 7  99   ? -7.235  -90.332  57.007  1.00 78.49  ?  99   ALA G CB  1 
ATOM   19060 N  N   . MET G 7  100  ? -6.701  -87.363  55.636  1.00 100.91 ?  100  MET G N   1 
ATOM   19061 C  CA  . MET G 7  100  ? -6.773  -86.516  54.451  1.00 101.14 ?  100  MET G CA  1 
ATOM   19062 C  C   . MET G 7  100  ? -5.377  -86.128  53.980  1.00 102.28 ?  100  MET G C   1 
ATOM   19063 O  O   . MET G 7  100  ? -5.130  -86.001  52.774  1.00 104.26 ?  100  MET G O   1 
ATOM   19064 C  CB  . MET G 7  100  ? -7.613  -85.271  54.742  1.00 107.55 ?  100  MET G CB  1 
ATOM   19065 C  CG  . MET G 7  100  ? -9.090  -85.555  54.977  1.00 103.69 ?  100  MET G CG  1 
ATOM   19066 S  SD  . MET G 7  100  ? -9.884  -84.284  55.982  1.00 111.32 ?  100  MET G SD  1 
ATOM   19067 C  CE  . MET G 7  100  ? -9.914  -82.908  54.836  1.00 96.40  ?  100  MET G CE  1 
ATOM   19068 N  N   . ASP G 7  101  ? -4.444  -85.937  54.919  1.00 114.69 ?  101  ASP G N   1 
ATOM   19069 C  CA  . ASP G 7  101  ? -3.058  -85.679  54.539  1.00 114.08 ?  101  ASP G CA  1 
ATOM   19070 C  C   . ASP G 7  101  ? -2.420  -86.908  53.905  1.00 115.12 ?  101  ASP G C   1 
ATOM   19071 O  O   . ASP G 7  101  ? -1.553  -86.778  53.034  1.00 121.10 ?  101  ASP G O   1 
ATOM   19072 C  CB  . ASP G 7  101  ? -2.251  -85.227  55.755  1.00 114.46 ?  101  ASP G CB  1 
ATOM   19073 C  CG  . ASP G 7  101  ? -2.870  -84.033  56.449  1.00 119.01 ?  101  ASP G CG  1 
ATOM   19074 O  OD1 . ASP G 7  101  ? -2.863  -82.935  55.856  1.00 128.15 ?  101  ASP G OD1 1 
ATOM   19075 O  OD2 . ASP G 7  101  ? -3.349  -84.190  57.594  1.00 121.91 -1 101  ASP G OD2 1 
ATOM   19076 N  N   . LEU G 7  102  ? -2.829  -88.106  54.327  1.00 76.96  ?  102  LEU G N   1 
ATOM   19077 C  CA  . LEU G 7  102  ? -2.338  -89.318  53.679  1.00 78.84  ?  102  LEU G CA  1 
ATOM   19078 C  C   . LEU G 7  102  ? -2.899  -89.452  52.268  1.00 80.80  ?  102  LEU G C   1 
ATOM   19079 O  O   . LEU G 7  102  ? -2.203  -89.923  51.362  1.00 81.92  ?  102  LEU G O   1 
ATOM   19080 C  CB  . LEU G 7  102  ? -2.694  -90.546  54.518  1.00 79.70  ?  102  LEU G CB  1 
ATOM   19081 C  CG  . LEU G 7  102  ? -1.674  -91.035  55.553  1.00 81.11  ?  102  LEU G CG  1 
ATOM   19082 C  CD1 . LEU G 7  102  ? -0.367  -91.428  54.884  1.00 86.73  ?  102  LEU G CD1 1 
ATOM   19083 C  CD2 . LEU G 7  102  ? -1.434  -89.989  56.633  1.00 85.99  ?  102  LEU G CD2 1 
ATOM   19084 N  N   . ILE G 7  103  ? -4.152  -89.037  52.065  1.00 94.15  ?  103  ILE G N   1 
ATOM   19085 C  CA  . ILE G 7  103  ? -4.770  -89.123  50.743  1.00 86.23  ?  103  ILE G CA  1 
ATOM   19086 C  C   . ILE G 7  103  ? -4.040  -88.228  49.747  1.00 85.12  ?  103  ILE G C   1 
ATOM   19087 O  O   . ILE G 7  103  ? -3.686  -88.663  48.645  1.00 85.20  ?  103  ILE G O   1 
ATOM   19088 C  CB  . ILE G 7  103  ? -6.267  -88.774  50.825  1.00 88.12  ?  103  ILE G CB  1 
ATOM   19089 C  CG1 . ILE G 7  103  ? -7.013  -89.826  51.648  1.00 83.45  ?  103  ILE G CG1 1 
ATOM   19090 C  CG2 . ILE G 7  103  ? -6.862  -88.656  49.433  1.00 89.75  ?  103  ILE G CG2 1 
ATOM   19091 C  CD1 . ILE G 7  103  ? -6.966  -91.205  51.038  1.00 69.78  ?  103  ILE G CD1 1 
ATOM   19092 N  N   . VAL G 7  104  ? -3.804  -86.963  50.113  1.00 96.39  ?  104  VAL G N   1 
ATOM   19093 C  CA  . VAL G 7  104  ? -3.082  -86.067  49.212  1.00 96.21  ?  104  VAL G CA  1 
ATOM   19094 C  C   . VAL G 7  104  ? -1.636  -86.503  49.018  1.00 104.52 ?  104  VAL G C   1 
ATOM   19095 O  O   . VAL G 7  104  ? -1.016  -86.148  48.009  1.00 108.64 ?  104  VAL G O   1 
ATOM   19096 C  CB  . VAL G 7  104  ? -3.134  -84.609  49.717  1.00 94.39  ?  104  VAL G CB  1 
ATOM   19097 C  CG1 . VAL G 7  104  ? -4.571  -84.148  49.896  1.00 96.94  ?  104  VAL G CG1 1 
ATOM   19098 C  CG2 . VAL G 7  104  ? -2.355  -84.455  51.019  1.00 102.14 ?  104  VAL G CG2 1 
ATOM   19099 N  N   . GLU G 7  105  ? -1.079  -87.268  49.959  1.00 111.91 ?  105  GLU G N   1 
ATOM   19100 C  CA  . GLU G 7  105  ? 0.286   -87.761  49.808  1.00 114.87 ?  105  GLU G CA  1 
ATOM   19101 C  C   . GLU G 7  105  ? 0.355   -88.927  48.828  1.00 111.18 ?  105  GLU G C   1 
ATOM   19102 O  O   . GLU G 7  105  ? 1.147   -88.902  47.881  1.00 113.03 ?  105  GLU G O   1 
ATOM   19103 C  CB  . GLU G 7  105  ? 0.852   -88.172  51.171  1.00 107.94 ?  105  GLU G CB  1 
ATOM   19104 C  CG  . GLU G 7  105  ? 2.279   -88.709  51.118  1.00 112.15 ?  105  GLU G CG  1 
ATOM   19105 C  CD  . GLU G 7  105  ? 2.796   -89.139  52.478  1.00 115.41 ?  105  GLU G CD  1 
ATOM   19106 O  OE1 . GLU G 7  105  ? 2.037   -89.038  53.465  1.00 114.20 ?  105  GLU G OE1 1 
ATOM   19107 O  OE2 . GLU G 7  105  ? 3.963   -89.579  52.557  1.00 108.81 ?  105  GLU G OE2 1 
ATOM   19108 N  N   . ARG G 7  106  ? -0.462  -89.962  49.043  1.00 90.62  ?  106  ARG G N   1 
ATOM   19109 C  CA  . ARG G 7  106  ? -0.436  -91.117  48.152  1.00 89.11  ?  106  ARG G CA  1 
ATOM   19110 C  C   . ARG G 7  106  ? -1.179  -90.851  46.849  1.00 88.55  ?  106  ARG G C   1 
ATOM   19111 O  O   . ARG G 7  106  ? -0.824  -91.422  45.812  1.00 97.11  ?  106  ARG G O   1 
ATOM   19112 C  CB  . ARG G 7  106  ? -1.015  -92.348  48.858  1.00 93.86  ?  106  ARG G CB  1 
ATOM   19113 C  CG  . ARG G 7  106  ? -2.473  -92.221  49.275  1.00 98.54  ?  106  ARG G CG  1 
ATOM   19114 C  CD  . ARG G 7  106  ? -2.857  -93.294  50.286  1.00 99.17  ?  106  ARG G CD  1 
ATOM   19115 N  NE  . ARG G 7  106  ? -1.833  -93.461  51.310  1.00 104.47 ?  106  ARG G NE  1 
ATOM   19116 C  CZ  . ARG G 7  106  ? -1.877  -94.366  52.279  1.00 98.61  ?  106  ARG G CZ  1 
ATOM   19117 N  NH1 . ARG G 7  106  ? -2.892  -95.207  52.395  1.00 92.58  ?  106  ARG G NH1 1 
ATOM   19118 N  NH2 . ARG G 7  106  ? -0.882  -94.420  53.161  1.00 84.68  ?  106  ARG G NH2 1 
ATOM   19119 N  N   . GLY G 7  107  ? -2.199  -89.997  46.877  1.00 94.76  ?  107  GLY G N   1 
ATOM   19120 C  CA  . GLY G 7  107  ? -2.886  -89.588  45.672  1.00 96.07  ?  107  GLY G CA  1 
ATOM   19121 C  C   . GLY G 7  107  ? -3.895  -90.608  45.175  1.00 87.55  ?  107  GLY G C   1 
ATOM   19122 O  O   . GLY G 7  107  ? -3.936  -91.766  45.596  1.00 79.98  ?  107  GLY G O   1 
ATOM   19123 N  N   . LEU G 7  108  ? -4.732  -90.150  44.244  1.00 84.88  ?  108  LEU G N   1 
ATOM   19124 C  CA  . LEU G 7  108  ? -5.763  -90.949  43.603  1.00 84.85  ?  108  LEU G CA  1 
ATOM   19125 C  C   . LEU G 7  108  ? -5.526  -91.008  42.097  1.00 91.62  ?  108  LEU G C   1 
ATOM   19126 O  O   . LEU G 7  108  ? -4.926  -90.094  41.523  1.00 100.22 ?  108  LEU G O   1 
ATOM   19127 C  CB  . LEU G 7  108  ? -7.160  -90.374  43.874  1.00 77.30  ?  108  LEU G CB  1 
ATOM   19128 C  CG  . LEU G 7  108  ? -7.937  -90.984  45.041  1.00 75.24  ?  108  LEU G CG  1 
ATOM   19129 C  CD1 . LEU G 7  108  ? -7.348  -90.536  46.366  1.00 82.80  ?  108  LEU G CD1 1 
ATOM   19130 C  CD2 . LEU G 7  108  ? -9.408  -90.611  44.953  1.00 72.89  ?  108  LEU G CD2 1 
ATOM   19131 N  N   . PRO G 7  109  ? -5.974  -92.075  41.434  1.00 77.24  ?  109  PRO G N   1 
ATOM   19132 C  CA  . PRO G 7  109  ? -5.812  -92.154  39.977  1.00 87.55  ?  109  PRO G CA  1 
ATOM   19133 C  C   . PRO G 7  109  ? -6.595  -91.055  39.272  1.00 80.11  ?  109  PRO G C   1 
ATOM   19134 O  O   . PRO G 7  109  ? -7.746  -90.771  39.609  1.00 74.26  ?  109  PRO G O   1 
ATOM   19135 C  CB  . PRO G 7  109  ? -6.357  -93.546  39.629  1.00 88.25  ?  109  PRO G CB  1 
ATOM   19136 C  CG  . PRO G 7  109  ? -7.155  -93.970  40.825  1.00 75.90  ?  109  PRO G CG  1 
ATOM   19137 C  CD  . PRO G 7  109  ? -6.510  -93.322  42.002  1.00 73.16  ?  109  PRO G CD  1 
ATOM   19138 N  N   . VAL G 7  110  ? -5.954  -90.435  38.284  1.00 113.06 ?  110  VAL G N   1 
ATOM   19139 C  CA  . VAL G 7  110  ? -6.524  -89.314  37.550  1.00 121.74 ?  110  VAL G CA  1 
ATOM   19140 C  C   . VAL G 7  110  ? -6.534  -89.653  36.066  1.00 126.39 ?  110  VAL G C   1 
ATOM   19141 O  O   . VAL G 7  110  ? -5.585  -90.254  35.552  1.00 135.38 ?  110  VAL G O   1 
ATOM   19142 C  CB  . VAL G 7  110  ? -5.740  -88.009  37.810  1.00 115.86 ?  110  VAL G CB  1 
ATOM   19143 C  CG1 . VAL G 7  110  ? -6.384  -86.837  37.081  1.00 119.13 ?  110  VAL G CG1 1 
ATOM   19144 C  CG2 . VAL G 7  110  ? -5.653  -87.732  39.301  1.00 105.93 ?  110  VAL G CG2 1 
ATOM   19145 N  N   . ARG G 7  111  ? -7.616  -89.271  35.387  1.00 140.00 ?  111  ARG G N   1 
ATOM   19146 C  CA  . ARG G 7  111  ? -7.756  -89.443  33.942  1.00 157.18 ?  111  ARG G CA  1 
ATOM   19147 C  C   . ARG G 7  111  ? -7.641  -90.909  33.532  1.00 154.59 ?  111  ARG G C   1 
ATOM   19148 O  O   . ARG G 7  111  ? -8.643  -91.563  33.244  1.00 143.16 ?  111  ARG G O   1 
ATOM   19149 C  CB  . ARG G 7  111  ? -6.710  -88.603  33.199  1.00 155.72 ?  111  ARG G CB  1 
ATOM   19150 C  CG  . ARG G 7  111  ? -6.748  -88.743  31.686  1.00 153.71 ?  111  ARG G CG  1 
ATOM   19151 C  CD  . ARG G 7  111  ? -7.853  -87.892  31.078  1.00 157.14 ?  111  ARG G CD  1 
ATOM   19152 N  NE  . ARG G 7  111  ? -9.083  -88.647  30.873  1.00 174.85 ?  111  ARG G NE  1 
ATOM   19153 C  CZ  . ARG G 7  111  ? -10.225 -88.119  30.453  1.00 175.26 ?  111  ARG G CZ  1 
ATOM   19154 N  NH1 . ARG G 7  111  ? -10.333 -86.827  30.189  1.00 170.91 ?  111  ARG G NH1 1 
ATOM   19155 N  NH2 . ARG G 7  111  ? -11.284 -88.906  30.292  1.00 169.57 ?  111  ARG G NH2 1 
ATOM   19156 N  N   . VAL H 8  11   ? -54.051 -23.218  94.560  1.00 108.14 ?  11   VAL I N   1 
ATOM   19157 C  CA  . VAL H 8  11   ? -53.346 -22.572  93.461  1.00 121.25 ?  11   VAL I CA  1 
ATOM   19158 C  C   . VAL H 8  11   ? -51.970 -23.208  93.297  1.00 118.96 ?  11   VAL I C   1 
ATOM   19159 O  O   . VAL H 8  11   ? -51.687 -23.832  92.277  1.00 122.57 ?  11   VAL I O   1 
ATOM   19160 C  CB  . VAL H 8  11   ? -53.234 -21.055  93.683  1.00 122.00 ?  11   VAL I CB  1 
ATOM   19161 C  CG1 . VAL H 8  11   ? -52.164 -20.456  92.778  1.00 114.08 ?  11   VAL I CG1 1 
ATOM   19162 C  CG2 . VAL H 8  11   ? -54.581 -20.385  93.451  1.00 121.94 ?  11   VAL I CG2 1 
ATOM   19163 N  N   . LYS H 8  12   ? -51.111 -23.039  94.298  1.00 167.77 ?  12   LYS I N   1 
ATOM   19164 C  CA  . LYS H 8  12   ? -49.840 -23.756  94.302  1.00 173.71 ?  12   LYS I CA  1 
ATOM   19165 C  C   . LYS H 8  12   ? -50.021 -25.267  94.218  1.00 174.88 ?  12   LYS I C   1 
ATOM   19166 O  O   . LYS H 8  12   ? -49.199 -25.920  93.552  1.00 168.43 ?  12   LYS I O   1 
ATOM   19167 C  CB  . LYS H 8  12   ? -49.026 -23.371  95.548  1.00 171.20 ?  12   LYS I CB  1 
ATOM   19168 C  CG  . LYS H 8  12   ? -48.523 -21.941  95.547  1.00 171.90 ?  12   LYS I CG  1 
ATOM   19169 C  CD  . LYS H 8  12   ? -47.730 -21.626  94.290  1.00 172.94 ?  12   LYS I CD  1 
ATOM   19170 C  CE  . LYS H 8  12   ? -47.399 -20.144  94.222  1.00 179.54 ?  12   LYS I CE  1 
ATOM   19171 N  NZ  . LYS H 8  12   ? -46.578 -19.709  95.388  1.00 176.97 ?  12   LYS I NZ  1 
ATOM   19172 N  N   . PRO H 8  13   ? -51.031 -25.880  94.853  1.00 139.93 ?  13   PRO I N   1 
ATOM   19173 C  CA  . PRO H 8  13   ? -51.284 -27.308  94.601  1.00 133.96 ?  13   PRO I CA  1 
ATOM   19174 C  C   . PRO H 8  13   ? -51.562 -27.650  93.144  1.00 133.74 ?  13   PRO I C   1 
ATOM   19175 O  O   . PRO H 8  13   ? -51.041 -28.660  92.655  1.00 124.51 ?  13   PRO I O   1 
ATOM   19176 C  CB  . PRO H 8  13   ? -52.496 -27.598  95.496  1.00 135.83 ?  13   PRO I CB  1 
ATOM   19177 C  CG  . PRO H 8  13   ? -52.329 -26.683  96.634  1.00 137.51 ?  13   PRO I CG  1 
ATOM   19178 C  CD  . PRO H 8  13   ? -51.756 -25.417  96.055  1.00 141.12 ?  13   PRO I CD  1 
ATOM   19179 N  N   . VAL H 8  14   ? -52.360 -26.850  92.432  1.00 169.73 ?  14   VAL I N   1 
ATOM   19180 C  CA  . VAL H 8  14   ? -52.694 -27.221  91.058  1.00 162.51 ?  14   VAL I CA  1 
ATOM   19181 C  C   . VAL H 8  14   ? -51.513 -26.979  90.132  1.00 161.69 ?  14   VAL I C   1 
ATOM   19182 O  O   . VAL H 8  14   ? -51.398 -27.634  89.090  1.00 159.47 ?  14   VAL I O   1 
ATOM   19183 C  CB  . VAL H 8  14   ? -53.951 -26.482  90.555  1.00 169.21 ?  14   VAL I CB  1 
ATOM   19184 C  CG1 . VAL H 8  14   ? -55.120 -26.681  91.513  1.00 167.05 ?  14   VAL I CG1 1 
ATOM   19185 C  CG2 . VAL H 8  14   ? -53.670 -25.002  90.298  1.00 172.20 ?  14   VAL I CG2 1 
ATOM   19186 N  N   . PHE H 8  15   ? -50.624 -26.046  90.484  1.00 151.28 ?  15   PHE I N   1 
ATOM   19187 C  CA  . PHE H 8  15   ? -49.394 -25.872  89.718  1.00 147.19 ?  15   PHE I CA  1 
ATOM   19188 C  C   . PHE H 8  15   ? -48.517 -27.111  89.814  1.00 146.80 ?  15   PHE I C   1 
ATOM   19189 O  O   . PHE H 8  15   ? -47.865 -27.500  88.838  1.00 145.74 ?  15   PHE I O   1 
ATOM   19190 C  CB  . PHE H 8  15   ? -48.633 -24.639  90.207  1.00 145.01 ?  15   PHE I CB  1 
ATOM   19191 C  CG  . PHE H 8  15   ? -47.829 -23.952  89.134  1.00 143.27 ?  15   PHE I CG  1 
ATOM   19192 C  CD1 . PHE H 8  15   ? -48.440 -23.452  87.996  1.00 142.25 ?  15   PHE I CD1 1 
ATOM   19193 C  CD2 . PHE H 8  15   ? -46.457 -23.812  89.269  1.00 142.03 ?  15   PHE I CD2 1 
ATOM   19194 C  CE1 . PHE H 8  15   ? -47.696 -22.821  87.014  1.00 141.39 ?  15   PHE I CE1 1 
ATOM   19195 C  CE2 . PHE H 8  15   ? -45.709 -23.183  88.291  1.00 139.94 ?  15   PHE I CE2 1 
ATOM   19196 C  CZ  . PHE H 8  15   ? -46.329 -22.687  87.163  1.00 136.05 ?  15   PHE I CZ  1 
ATOM   19197 N  N   . LEU H 8  16   ? -48.487 -27.743  90.990  1.00 145.07 ?  16   LEU I N   1 
ATOM   19198 C  CA  . LEU H 8  16   ? -47.774 -29.006  91.136  1.00 142.87 ?  16   LEU I CA  1 
ATOM   19199 C  C   . LEU H 8  16   ? -48.484 -30.126  90.387  1.00 143.51 ?  16   LEU I C   1 
ATOM   19200 O  O   . LEU H 8  16   ? -47.833 -31.019  89.831  1.00 137.60 ?  16   LEU I O   1 
ATOM   19201 C  CB  . LEU H 8  16   ? -47.635 -29.357  92.617  1.00 139.89 ?  16   LEU I CB  1 
ATOM   19202 C  CG  . LEU H 8  16   ? -46.649 -30.469  92.977  1.00 139.52 ?  16   LEU I CG  1 
ATOM   19203 C  CD1 . LEU H 8  16   ? -45.217 -30.010  92.762  1.00 117.18 ?  16   LEU I CD1 1 
ATOM   19204 C  CD2 . LEU H 8  16   ? -46.866 -30.929  94.411  1.00 148.65 ?  16   LEU I CD2 1 
ATOM   19205 N  N   . ALA H 8  17   ? -49.820 -30.092  90.359  1.00 161.28 ?  17   ALA I N   1 
ATOM   19206 C  CA  . ALA H 8  17   ? -50.579 -31.129  89.668  1.00 155.62 ?  17   ALA I CA  1 
ATOM   19207 C  C   . ALA H 8  17   ? -50.350 -31.068  88.162  1.00 152.20 ?  17   ALA I C   1 
ATOM   19208 O  O   . ALA H 8  17   ? -50.097 -32.096  87.522  1.00 147.29 ?  17   ALA I O   1 
ATOM   19209 C  CB  . ALA H 8  17   ? -52.067 -31.001  89.999  1.00 150.47 ?  17   ALA I CB  1 
ATOM   19210 N  N   . VAL H 8  18   ? -50.429 -29.870  87.574  1.00 114.72 ?  18   VAL I N   1 
ATOM   19211 C  CA  . VAL H 8  18   ? -50.130 -29.718  86.153  1.00 105.07 ?  18   VAL I CA  1 
ATOM   19212 C  C   . VAL H 8  18   ? -48.662 -29.945  85.838  1.00 107.85 ?  18   VAL I C   1 
ATOM   19213 O  O   . VAL H 8  18   ? -48.307 -30.094  84.662  1.00 111.48 ?  18   VAL I O   1 
ATOM   19214 C  CB  . VAL H 8  18   ? -50.545 -28.330  85.623  1.00 103.60 ?  18   VAL I CB  1 
ATOM   19215 C  CG1 . VAL H 8  18   ? -52.011 -28.072  85.894  1.00 110.53 ?  18   VAL I CG1 1 
ATOM   19216 C  CG2 . VAL H 8  18   ? -49.688 -27.244  86.251  1.00 107.95 ?  18   VAL I CG2 1 
ATOM   19217 N  N   . THR H 8  19   ? -47.800 -29.967  86.857  1.00 130.59 ?  19   THR I N   1 
ATOM   19218 C  CA  . THR H 8  19   ? -46.397 -30.309  86.652  1.00 130.43 ?  19   THR I CA  1 
ATOM   19219 C  C   . THR H 8  19   ? -46.204 -31.818  86.608  1.00 126.05 ?  19   THR I C   1 
ATOM   19220 O  O   . THR H 8  19   ? -45.569 -32.343  85.687  1.00 118.95 ?  19   THR I O   1 
ATOM   19221 C  CB  . THR H 8  19   ? -45.531 -29.700  87.754  1.00 130.76 ?  19   THR I CB  1 
ATOM   19222 O  OG1 . THR H 8  19   ? -45.633 -28.273  87.711  1.00 128.25 ?  19   THR I OG1 1 
ATOM   19223 C  CG2 . THR H 8  19   ? -44.078 -30.107  87.567  1.00 119.04 ?  19   THR I CG2 1 
ATOM   19224 N  N   . LEU H 8  20   ? -46.749 -32.528  87.600  1.00 143.22 ?  20   LEU I N   1 
ATOM   19225 C  CA  . LEU H 8  20   ? -46.665 -33.984  87.599  1.00 138.91 ?  20   LEU I CA  1 
ATOM   19226 C  C   . LEU H 8  20   ? -47.334 -34.566  86.362  1.00 131.58 ?  20   LEU I C   1 
ATOM   19227 O  O   . LEU H 8  20   ? -46.826 -35.520  85.764  1.00 122.91 ?  20   LEU I O   1 
ATOM   19228 C  CB  . LEU H 8  20   ? -47.297 -34.556  88.869  1.00 140.98 ?  20   LEU I CB  1 
ATOM   19229 C  CG  . LEU H 8  20   ? -46.414 -34.739  90.108  1.00 139.88 ?  20   LEU I CG  1 
ATOM   19230 C  CD1 . LEU H 8  20   ? -45.495 -33.548  90.341  1.00 137.26 ?  20   LEU I CD1 1 
ATOM   19231 C  CD2 . LEU H 8  20   ? -47.277 -34.997  91.332  1.00 140.29 ?  20   LEU I CD2 1 
ATOM   19232 N  N   . THR H 8  21   ? -48.469 -33.994  85.957  1.00 109.78 ?  21   THR I N   1 
ATOM   19233 C  CA  . THR H 8  21   ? -49.119 -34.423  84.723  1.00 110.33 ?  21   THR I CA  1 
ATOM   19234 C  C   . THR H 8  21   ? -48.183 -34.313  83.523  1.00 108.85 ?  21   THR I C   1 
ATOM   19235 O  O   . THR H 8  21   ? -48.157 -35.201  82.661  1.00 106.77 ?  21   THR I O   1 
ATOM   19236 C  CB  . THR H 8  21   ? -50.384 -33.600  84.488  1.00 110.61 ?  21   THR I CB  1 
ATOM   19237 O  OG1 . THR H 8  21   ? -51.299 -33.798  85.575  1.00 112.82 ?  21   THR I OG1 1 
ATOM   19238 C  CG2 . THR H 8  21   ? -51.034 -34.006  83.186  1.00 109.38 ?  21   THR I CG2 1 
ATOM   19239 N  N   . GLY H 8  22   ? -47.400 -33.235  83.458  1.00 116.28 ?  22   GLY I N   1 
ATOM   19240 C  CA  . GLY H 8  22   ? -46.512 -33.045  82.321  1.00 114.41 ?  22   GLY I CA  1 
ATOM   19241 C  C   . GLY H 8  22   ? -45.417 -34.092  82.251  1.00 116.59 ?  22   GLY I C   1 
ATOM   19242 O  O   . GLY H 8  22   ? -45.209 -34.722  81.211  1.00 115.88 ?  22   GLY I O   1 
ATOM   19243 N  N   . MET H 8  23   ? -44.703 -34.299  83.362  1.00 148.80 ?  23   MET I N   1 
ATOM   19244 C  CA  . MET H 8  23   ? -43.612 -35.269  83.357  1.00 145.52 ?  23   MET I CA  1 
ATOM   19245 C  C   . MET H 8  23   ? -44.137 -36.684  83.168  1.00 147.64 ?  23   MET I C   1 
ATOM   19246 O  O   . MET H 8  23   ? -43.507 -37.493  82.474  1.00 149.24 ?  23   MET I O   1 
ATOM   19247 C  CB  . MET H 8  23   ? -42.793 -35.172  84.644  1.00 147.32 ?  23   MET I CB  1 
ATOM   19248 C  CG  . MET H 8  23   ? -43.606 -35.059  85.921  1.00 151.97 ?  23   MET I CG  1 
ATOM   19249 S  SD  . MET H 8  23   ? -43.996 -36.674  86.612  1.00 162.00 ?  23   MET I SD  1 
ATOM   19250 C  CE  . MET H 8  23   ? -42.537 -36.983  87.594  1.00 149.64 ?  23   MET I CE  1 
ATOM   19251 N  N   . VAL H 8  24   ? -45.280 -37.001  83.788  1.00 115.45 ?  24   VAL I N   1 
ATOM   19252 C  CA  . VAL H 8  24   ? -45.942 -38.276  83.529  1.00 115.95 ?  24   VAL I CA  1 
ATOM   19253 C  C   . VAL H 8  24   ? -46.068 -38.509  82.030  1.00 116.74 ?  24   VAL I C   1 
ATOM   19254 O  O   . VAL H 8  24   ? -45.609 -39.528  81.508  1.00 117.13 ?  24   VAL I O   1 
ATOM   19255 C  CB  . VAL H 8  24   ? -47.309 -38.329  84.229  1.00 116.20 ?  24   VAL I CB  1 
ATOM   19256 C  CG1 . VAL H 8  24   ? -48.142 -39.443  83.629  1.00 116.22 ?  24   VAL I CG1 1 
ATOM   19257 C  CG2 . VAL H 8  24   ? -47.104 -38.613  85.703  1.00 115.60 ?  24   VAL I CG2 1 
ATOM   19258 N  N   . ALA H 8  25   ? -46.621 -37.530  81.306  1.00 114.66 ?  25   ALA I N   1 
ATOM   19259 C  CA  . ALA H 8  25   ? -46.794 -37.674  79.862  1.00 109.35 ?  25   ALA I CA  1 
ATOM   19260 C  C   . ALA H 8  25   ? -45.459 -37.881  79.156  1.00 112.64 ?  25   ALA I C   1 
ATOM   19261 O  O   . ALA H 8  25   ? -45.348 -38.714  78.250  1.00 113.75 ?  25   ALA I O   1 
ATOM   19262 C  CB  . ALA H 8  25   ? -47.516 -36.450  79.297  1.00 108.88 ?  25   ALA I CB  1 
ATOM   19263 N  N   . PHE H 8  26   ? -44.433 -37.125  79.557  1.00 104.85 ?  26   PHE I N   1 
ATOM   19264 C  CA  . PHE H 8  26   ? -43.128 -37.234  78.911  1.00 102.55 ?  26   PHE I CA  1 
ATOM   19265 C  C   . PHE H 8  26   ? -42.566 -38.646  79.031  1.00 102.24 ?  26   PHE I C   1 
ATOM   19266 O  O   . PHE H 8  26   ? -42.147 -39.244  78.034  1.00 105.59 ?  26   PHE I O   1 
ATOM   19267 C  CB  . PHE H 8  26   ? -42.161 -36.214  79.513  1.00 105.86 ?  26   PHE I CB  1 
ATOM   19268 C  CG  . PHE H 8  26   ? -40.951 -35.959  78.666  1.00 105.95 ?  26   PHE I CG  1 
ATOM   19269 C  CD1 . PHE H 8  26   ? -41.082 -35.486  77.371  1.00 104.28 ?  26   PHE I CD1 1 
ATOM   19270 C  CD2 . PHE H 8  26   ? -39.680 -36.191  79.165  1.00 107.01 ?  26   PHE I CD2 1 
ATOM   19271 C  CE1 . PHE H 8  26   ? -39.967 -35.253  76.587  1.00 105.45 ?  26   PHE I CE1 1 
ATOM   19272 C  CE2 . PHE H 8  26   ? -38.562 -35.958  78.389  1.00 104.32 ?  26   PHE I CE2 1 
ATOM   19273 C  CZ  . PHE H 8  26   ? -38.705 -35.488  77.097  1.00 106.36 ?  26   PHE I CZ  1 
ATOM   19274 N  N   . LEU H 8  27   ? -42.552 -39.194  80.251  1.00 115.68 ?  27   LEU I N   1 
ATOM   19275 C  CA  . LEU H 8  27   ? -42.084 -40.562  80.460  1.00 120.38 ?  27   LEU I CA  1 
ATOM   19276 C  C   . LEU H 8  27   ? -42.849 -41.528  79.569  1.00 118.79 ?  27   LEU I C   1 
ATOM   19277 O  O   . LEU H 8  27   ? -42.261 -42.357  78.866  1.00 121.90 ?  27   LEU I O   1 
ATOM   19278 C  CB  . LEU H 8  27   ? -42.256 -40.949  81.930  1.00 118.06 ?  27   LEU I CB  1 
ATOM   19279 C  CG  . LEU H 8  27   ? -41.659 -40.008  82.980  1.00 121.55 ?  27   LEU I CG  1 
ATOM   19280 C  CD1 . LEU H 8  27   ? -41.727 -40.629  84.369  1.00 121.94 ?  27   LEU I CD1 1 
ATOM   19281 C  CD2 . LEU H 8  27   ? -40.225 -39.612  82.633  1.00 121.32 ?  27   LEU I CD2 1 
ATOM   19282 N  N   . LEU H 8  28   ? -44.175 -41.426  79.604  1.00 108.85 ?  28   LEU I N   1 
ATOM   19283 C  CA  . LEU H 8  28   ? -45.068 -42.163  78.723  1.00 108.31 ?  28   LEU I CA  1 
ATOM   19284 C  C   . LEU H 8  28   ? -44.640 -42.056  77.263  1.00 109.06 ?  28   LEU I C   1 
ATOM   19285 O  O   . LEU H 8  28   ? -44.345 -43.063  76.608  1.00 110.69 ?  28   LEU I O   1 
ATOM   19286 C  CB  . LEU H 8  28   ? -46.466 -41.593  78.928  1.00 107.21 ?  28   LEU I CB  1 
ATOM   19287 C  CG  . LEU H 8  28   ? -47.054 -41.881  80.306  1.00 108.43 ?  28   LEU I CG  1 
ATOM   19288 C  CD1 . LEU H 8  28   ? -48.522 -41.726  80.200  1.00 109.19 ?  28   LEU I CD1 1 
ATOM   19289 C  CD2 . LEU H 8  28   ? -46.725 -43.292  80.776  1.00 108.65 ?  28   LEU I CD2 1 
ATOM   19290 N  N   . MET H 8  29   ? -44.605 -40.825  76.744  1.00 124.01 ?  29   MET I N   1 
ATOM   19291 C  CA  . MET H 8  29   ? -44.266 -40.594  75.343  1.00 122.81 ?  29   MET I CA  1 
ATOM   19292 C  C   . MET H 8  29   ? -42.853 -41.071  75.024  1.00 125.44 ?  29   MET I C   1 
ATOM   19293 O  O   . MET H 8  29   ? -42.633 -41.767  74.026  1.00 120.95 ?  29   MET I O   1 
ATOM   19294 C  CB  . MET H 8  29   ? -44.420 -39.108  75.013  1.00 125.47 ?  29   MET I CB  1 
ATOM   19295 C  CG  . MET H 8  29   ? -45.827 -38.553  75.208  1.00 122.59 ?  29   MET I CG  1 
ATOM   19296 S  SD  . MET H 8  29   ? -46.809 -38.584  73.698  1.00 134.01 ?  29   MET I SD  1 
ATOM   19297 C  CE  . MET H 8  29   ? -47.468 -40.248  73.758  1.00 124.74 ?  29   MET I CE  1 
ATOM   19298 N  N   . VAL H 8  30   ? -41.878 -40.699  75.860  1.00 71.47  ?  30   VAL I N   1 
ATOM   19299 C  CA  . VAL H 8  30   ? -40.488 -41.077  75.603  1.00 71.52  ?  30   VAL I CA  1 
ATOM   19300 C  C   . VAL H 8  30   ? -40.351 -42.593  75.535  1.00 72.25  ?  30   VAL I C   1 
ATOM   19301 O  O   . VAL H 8  30   ? -39.638 -43.129  74.677  1.00 75.24  ?  30   VAL I O   1 
ATOM   19302 C  CB  . VAL H 8  30   ? -39.562 -40.468  76.674  1.00 67.33  ?  30   VAL I CB  1 
ATOM   19303 C  CG1 . VAL H 8  30   ? -38.229 -41.198  76.714  1.00 66.01  ?  30   VAL I CG1 1 
ATOM   19304 C  CG2 . VAL H 8  30   ? -39.360 -38.984  76.414  1.00 70.69  ?  30   VAL I CG2 1 
ATOM   19305 N  N   . TRP H 8  31   ? -41.045 -43.307  76.423  1.00 123.38 ?  31   TRP I N   1 
ATOM   19306 C  CA  . TRP H 8  31   ? -41.022 -44.766  76.394  1.00 125.46 ?  31   TRP I CA  1 
ATOM   19307 C  C   . TRP H 8  31   ? -41.480 -45.292  75.039  1.00 126.31 ?  31   TRP I C   1 
ATOM   19308 O  O   . TRP H 8  31   ? -40.815 -46.140  74.433  1.00 131.92 ?  31   TRP I O   1 
ATOM   19309 C  CB  . TRP H 8  31   ? -41.901 -45.317  77.518  1.00 124.08 ?  31   TRP I CB  1 
ATOM   19310 C  CG  . TRP H 8  31   ? -41.878 -46.811  77.681  1.00 129.77 ?  31   TRP I CG  1 
ATOM   19311 C  CD1 . TRP H 8  31   ? -41.136 -47.714  76.971  1.00 129.24 ?  31   TRP I CD1 1 
ATOM   19312 C  CD2 . TRP H 8  31   ? -42.651 -47.574  78.614  1.00 132.61 ?  31   TRP I CD2 1 
ATOM   19313 N  NE1 . TRP H 8  31   ? -41.399 -48.990  77.409  1.00 131.45 ?  31   TRP I NE1 1 
ATOM   19314 C  CE2 . TRP H 8  31   ? -42.325 -48.930  78.418  1.00 132.49 ?  31   TRP I CE2 1 
ATOM   19315 C  CE3 . TRP H 8  31   ? -43.585 -47.239  79.601  1.00 130.73 ?  31   TRP I CE3 1 
ATOM   19316 C  CZ2 . TRP H 8  31   ? -42.901 -49.953  79.171  1.00 132.26 ?  31   TRP I CZ2 1 
ATOM   19317 C  CZ3 . TRP H 8  31   ? -44.157 -48.255  80.347  1.00 134.23 ?  31   TRP I CZ3 1 
ATOM   19318 C  CH2 . TRP H 8  31   ? -43.812 -49.595  80.129  1.00 133.65 ?  31   TRP I CH2 1 
ATOM   19319 N  N   . LEU H 8  32   ? -42.605 -44.776  74.535  1.00 86.01  ?  32   LEU I N   1 
ATOM   19320 C  CA  . LEU H 8  32   ? -43.174 -45.285  73.289  1.00 90.23  ?  32   LEU I CA  1 
ATOM   19321 C  C   . LEU H 8  32   ? -42.239 -45.057  72.107  1.00 90.33  ?  32   LEU I C   1 
ATOM   19322 O  O   . LEU H 8  32   ? -42.019 -45.961  71.293  1.00 92.00  ?  32   LEU I O   1 
ATOM   19323 C  CB  . LEU H 8  32   ? -44.532 -44.631  73.028  1.00 91.65  ?  32   LEU I CB  1 
ATOM   19324 C  CG  . LEU H 8  32   ? -45.192 -44.976  71.692  1.00 89.56  ?  32   LEU I CG  1 
ATOM   19325 C  CD1 . LEU H 8  32   ? -45.476 -46.465  71.605  1.00 88.77  ?  32   LEU I CD1 1 
ATOM   19326 C  CD2 . LEU H 8  32   ? -46.470 -44.176  71.508  1.00 89.85  ?  32   LEU I CD2 1 
ATOM   19327 N  N   . PHE H 8  33   ? -41.682 -43.853  71.992  1.00 94.13  ?  33   PHE I N   1 
ATOM   19328 C  CA  . PHE H 8  33   ? -40.880 -43.480  70.832  1.00 94.27  ?  33   PHE I CA  1 
ATOM   19329 C  C   . PHE H 8  33   ? -39.398 -43.804  70.987  1.00 101.44 ?  33   PHE I C   1 
ATOM   19330 O  O   . PHE H 8  33   ? -38.619 -43.506  70.076  1.00 101.09 ?  33   PHE I O   1 
ATOM   19331 C  CB  . PHE H 8  33   ? -41.053 -41.989  70.540  1.00 95.38  ?  33   PHE I CB  1 
ATOM   19332 C  CG  . PHE H 8  33   ? -42.486 -41.563  70.405  1.00 95.39  ?  33   PHE I CG  1 
ATOM   19333 C  CD1 . PHE H 8  33   ? -43.312 -42.160  69.468  1.00 93.77  ?  33   PHE I CD1 1 
ATOM   19334 C  CD2 . PHE H 8  33   ? -43.004 -40.562  71.210  1.00 94.69  ?  33   PHE I CD2 1 
ATOM   19335 C  CE1 . PHE H 8  33   ? -44.632 -41.772  69.339  1.00 96.22  ?  33   PHE I CE1 1 
ATOM   19336 C  CE2 . PHE H 8  33   ? -44.323 -40.168  71.086  1.00 98.35  ?  33   PHE I CE2 1 
ATOM   19337 C  CZ  . PHE H 8  33   ? -45.139 -40.773  70.148  1.00 100.59 ?  33   PHE I CZ  1 
ATOM   19338 N  N   . ALA H 8  34   ? -38.987 -44.404  72.103  1.00 113.17 ?  34   ALA I N   1 
ATOM   19339 C  CA  . ALA H 8  34   ? -37.583 -44.754  72.285  1.00 106.85 ?  34   ALA I CA  1 
ATOM   19340 C  C   . ALA H 8  34   ? -37.416 -46.217  72.672  1.00 110.89 ?  34   ALA I C   1 
ATOM   19341 O  O   . ALA H 8  34   ? -37.178 -47.068  71.810  1.00 119.07 ?  34   ALA I O   1 
ATOM   19342 C  CB  . ALA H 8  34   ? -36.931 -43.853  73.337  1.00 103.39 ?  34   ALA I CB  1 
ATOM   19343 N  N   . PHE H 8  35   ? -37.537 -46.521  73.961  1.00 165.73 ?  35   PHE I N   1 
ATOM   19344 C  CA  . PHE H 8  35   ? -37.258 -47.863  74.479  1.00 168.67 ?  35   PHE I CA  1 
ATOM   19345 C  C   . PHE H 8  35   ? -38.508 -48.742  74.484  1.00 169.72 ?  35   PHE I C   1 
ATOM   19346 O  O   . PHE H 8  35   ? -38.885 -49.324  75.501  1.00 170.13 ?  35   PHE I O   1 
ATOM   19347 C  CB  . PHE H 8  35   ? -36.652 -47.760  75.874  1.00 166.29 ?  35   PHE I CB  1 
ATOM   19348 C  CG  . PHE H 8  35   ? -35.848 -46.510  76.095  1.00 167.86 ?  35   PHE I CG  1 
ATOM   19349 C  CD1 . PHE H 8  35   ? -34.691 -46.276  75.368  1.00 166.92 ?  35   PHE I CD1 1 
ATOM   19350 C  CD2 . PHE H 8  35   ? -36.259 -45.563  77.018  1.00 171.26 ?  35   PHE I CD2 1 
ATOM   19351 C  CE1 . PHE H 8  35   ? -33.953 -45.125  75.565  1.00 167.27 ?  35   PHE I CE1 1 
ATOM   19352 C  CE2 . PHE H 8  35   ? -35.527 -44.410  77.220  1.00 168.08 ?  35   PHE I CE2 1 
ATOM   19353 C  CZ  . PHE H 8  35   ? -34.371 -44.190  76.492  1.00 167.37 ?  35   PHE I CZ  1 
ATOM   19354 N  N   . TYR H 8  36   ? -39.155 -48.847  73.321  1.00 117.16 ?  36   TYR I N   1 
ATOM   19355 C  CA  . TYR H 8  36   ? -40.365 -49.653  73.177  1.00 114.54 ?  36   TYR I CA  1 
ATOM   19356 C  C   . TYR H 8  36   ? -40.192 -50.673  72.060  1.00 117.28 ?  36   TYR I C   1 
ATOM   19357 O  O   . TYR H 8  36   ? -40.086 -51.870  72.341  1.00 117.97 ?  36   TYR I O   1 
ATOM   19358 C  CB  . TYR H 8  36   ? -41.574 -48.755  72.913  1.00 114.90 ?  36   TYR I CB  1 
ATOM   19359 C  CG  . TYR H 8  36   ? -42.904 -49.465  72.995  1.00 117.75 ?  36   TYR I CG  1 
ATOM   19360 C  CD1 . TYR H 8  36   ? -43.304 -50.087  74.168  1.00 114.32 ?  36   TYR I CD1 1 
ATOM   19361 C  CD2 . TYR H 8  36   ? -43.748 -49.533  71.893  1.00 115.34 ?  36   TYR I CD2 1 
ATOM   19362 C  CE1 . TYR H 8  36   ? -44.515 -50.731  74.256  1.00 110.51 ?  36   TYR I CE1 1 
ATOM   19363 C  CE2 . TYR H 8  36   ? -44.963 -50.186  71.969  1.00 115.22 ?  36   TYR I CE2 1 
ATOM   19364 C  CZ  . TYR H 8  36   ? -45.340 -50.784  73.153  1.00 112.40 ?  36   TYR I CZ  1 
ATOM   19365 O  OH  . TYR H 8  36   ? -46.545 -51.438  73.244  1.00 120.20 ?  36   TYR I OH  1 
ATOM   19366 N  N   . TRP H 8  37   ? -40.166 -50.234  70.803  1.00 188.67 ?  37   TRP I N   1 
ATOM   19367 C  CA  . TRP H 8  37   ? -39.992 -51.110  69.644  1.00 191.05 ?  37   TRP I CA  1 
ATOM   19368 C  C   . TRP H 8  37   ? -41.083 -52.174  69.560  1.00 191.71 ?  37   TRP I C   1 
ATOM   19369 O  O   . TRP H 8  37   ? -40.880 -53.320  69.961  1.00 195.01 ?  37   TRP I O   1 
ATOM   19370 C  CB  . TRP H 8  37   ? -38.616 -51.779  69.677  1.00 183.99 ?  37   TRP I CB  1 
ATOM   19371 C  CG  . TRP H 8  37   ? -37.515 -50.835  70.023  1.00 185.47 ?  37   TRP I CG  1 
ATOM   19372 C  CD1 . TRP H 8  37   ? -37.101 -49.758  69.299  1.00 183.45 ?  37   TRP I CD1 1 
ATOM   19373 C  CD2 . TRP H 8  37   ? -36.687 -50.878  71.191  1.00 189.07 ?  37   TRP I CD2 1 
ATOM   19374 N  NE1 . TRP H 8  37   ? -36.063 -49.127  69.942  1.00 183.87 ?  37   TRP I NE1 1 
ATOM   19375 C  CE2 . TRP H 8  37   ? -35.790 -49.796  71.106  1.00 191.21 ?  37   TRP I CE2 1 
ATOM   19376 C  CE3 . TRP H 8  37   ? -36.616 -51.729  72.300  1.00 188.66 ?  37   TRP I CE3 1 
ATOM   19377 C  CZ2 . TRP H 8  37   ? -34.833 -49.540  72.086  1.00 187.05 ?  37   TRP I CZ2 1 
ATOM   19378 C  CZ3 . TRP H 8  37   ? -35.665 -51.474  73.273  1.00 190.63 ?  37   TRP I CZ3 1 
ATOM   19379 C  CH2 . TRP H 8  37   ? -34.786 -50.388  73.159  1.00 188.56 ?  37   TRP I CH2 1 
HETATM 19380 FE FE  . HEC I 9  .    ? -35.193 -46.916  54.259  1.00 65.20  ?  301  HEC A FE  1 
HETATM 19381 C  CHA . HEC I 9  .    ? -38.325 -48.136  54.618  1.00 64.17  ?  301  HEC A CHA 1 
HETATM 19382 C  CHB . HEC I 9  .    ? -36.489 -44.018  52.822  1.00 61.82  ?  301  HEC A CHB 1 
HETATM 19383 C  CHC . HEC I 9  .    ? -32.042 -45.588  53.905  1.00 59.05  ?  301  HEC A CHC 1 
HETATM 19384 C  CHD . HEC I 9  .    ? -33.797 -50.015  54.866  1.00 63.38  ?  301  HEC A CHD 1 
HETATM 19385 N  NA  . HEC I 9  .    ? -37.050 -46.244  53.698  1.00 64.72  ?  301  HEC A NA  1 
HETATM 19386 C  C1A . HEC I 9  .    ? -38.205 -46.844  54.159  1.00 63.97  ?  301  HEC A C1A 1 
HETATM 19387 C  C2A . HEC I 9  .    ? -39.272 -45.868  54.078  1.00 62.95  ?  301  HEC A C2A 1 
HETATM 19388 C  C3A . HEC I 9  .    ? -38.773 -44.738  53.582  1.00 62.60  ?  301  HEC A C3A 1 
HETATM 19389 C  C4A . HEC I 9  .    ? -37.364 -44.947  53.332  1.00 63.45  ?  301  HEC A C4A 1 
HETATM 19390 C  CMA . HEC I 9  .    ? -39.563 -43.438  53.325  1.00 61.13  ?  301  HEC A CMA 1 
HETATM 19391 C  CAA . HEC I 9  .    ? -40.742 -46.092  54.478  1.00 61.98  ?  301  HEC A CAA 1 
HETATM 19392 C  CBA . HEC I 9  .    ? -41.489 -46.509  53.218  1.00 62.31  ?  301  HEC A CBA 1 
HETATM 19393 C  CGA . HEC I 9  .    ? -42.970 -46.352  53.414  1.00 64.21  ?  301  HEC A CGA 1 
HETATM 19394 O  O1A . HEC I 9  .    ? -43.416 -46.189  54.579  1.00 65.43  ?  301  HEC A O1A 1 
HETATM 19395 O  O2A . HEC I 9  .    ? -43.701 -46.394  52.396  1.00 65.17  ?  301  HEC A O2A 1 
HETATM 19396 N  NB  . HEC I 9  .    ? -34.419 -45.127  53.509  1.00 63.24  ?  301  HEC A NB  1 
HETATM 19397 C  C1B . HEC I 9  .    ? -35.123 -44.077  52.951  1.00 61.82  ?  301  HEC A C1B 1 
HETATM 19398 C  C2B . HEC I 9  .    ? -34.182 -43.059  52.534  1.00 58.65  ?  301  HEC A C2B 1 
HETATM 19399 C  C3B . HEC I 9  .    ? -32.953 -43.496  52.837  1.00 57.70  ?  301  HEC A C3B 1 
HETATM 19400 C  C4B . HEC I 9  .    ? -33.078 -44.802  53.453  1.00 59.90  ?  301  HEC A C4B 1 
HETATM 19401 C  CMB . HEC I 9  .    ? -34.572 -41.721  51.861  1.00 55.93  ?  301  HEC A CMB 1 
HETATM 19402 C  CAB . HEC I 9  .    ? -31.610 -42.774  52.594  1.00 53.54  ?  301  HEC A CAB 1 
HETATM 19403 C  CBB . HEC I 9  .    ? -31.511 -41.486  53.442  1.00 54.80  ?  301  HEC A CBB 1 
HETATM 19404 N  NC  . HEC I 9  .    ? -33.267 -47.699  54.263  1.00 63.83  ?  301  HEC A NC  1 
HETATM 19405 C  C1C . HEC I 9  .    ? -32.134 -46.906  54.302  1.00 61.28  ?  301  HEC A C1C 1 
HETATM 19406 C  C2C . HEC I 9  .    ? -31.096 -47.650  54.981  1.00 60.46  ?  301  HEC A C2C 1 
HETATM 19407 C  C3C . HEC I 9  .    ? -31.510 -48.913  55.098  1.00 61.29  ?  301  HEC A C3C 1 
HETATM 19408 C  C4C . HEC I 9  .    ? -32.925 -48.949  54.750  1.00 63.33  ?  301  HEC A C4C 1 
HETATM 19409 C  CMC . HEC I 9  .    ? -29.619 -47.207  55.054  1.00 56.37  ?  301  HEC A CMC 1 
HETATM 19410 C  CAC . HEC I 9  .    ? -30.652 -50.044  55.713  1.00 57.46  ?  301  HEC A CAC 1 
HETATM 19411 C  CBC . HEC I 9  .    ? -30.093 -51.020  54.662  1.00 56.19  ?  301  HEC A CBC 1 
HETATM 19412 N  ND  . HEC I 9  .    ? -35.946 -48.811  54.632  1.00 65.38  ?  301  HEC A ND  1 
HETATM 19413 C  C1D . HEC I 9  .    ? -35.175 -49.925  54.965  1.00 64.42  ?  301  HEC A C1D 1 
HETATM 19414 C  C2D . HEC I 9  .    ? -36.063 -50.964  55.443  1.00 63.36  ?  301  HEC A C2D 1 
HETATM 19415 C  C3D . HEC I 9  .    ? -37.477 -50.374  55.368  1.00 63.70  ?  301  HEC A C3D 1 
HETATM 19416 C  C4D . HEC I 9  .    ? -37.305 -49.034  54.850  1.00 64.90  ?  301  HEC A C4D 1 
HETATM 19417 C  CMD . HEC I 9  .    ? -35.685 -52.376  55.933  1.00 61.14  ?  301  HEC A CMD 1 
HETATM 19418 C  CAD . HEC I 9  .    ? -38.797 -51.073  55.763  1.00 62.48  ?  301  HEC A CAD 1 
HETATM 19419 C  CBD . HEC I 9  .    ? -39.382 -50.372  56.988  1.00 62.77  ?  301  HEC A CBD 1 
HETATM 19420 C  CGD . HEC I 9  .    ? -40.563 -51.136  57.526  1.00 63.02  ?  301  HEC A CGD 1 
HETATM 19421 O  O1D . HEC I 9  .    ? -40.926 -52.185  56.933  1.00 63.06  ?  301  HEC A O1D 1 
HETATM 19422 O  O2D . HEC I 9  .    ? -41.142 -50.694  58.552  1.00 64.23  ?  301  HEC A O2D 1 
HETATM 19423 FE FE  . HEC J 9  .    ? -27.093 -54.936  56.408  1.00 68.81  ?  302  HEC A FE  1 
HETATM 19424 C  CHA . HEC J 9  .    ? -24.261 -54.700  54.491  1.00 67.14  ?  302  HEC A CHA 1 
HETATM 19425 C  CHB . HEC J 9  .    ? -29.017 -54.452  53.591  1.00 69.37  ?  302  HEC A CHB 1 
HETATM 19426 C  CHC . HEC J 9  .    ? -29.968 -55.200  58.294  1.00 70.32  ?  302  HEC A CHC 1 
HETATM 19427 C  CHD . HEC J 9  .    ? -25.257 -56.046  59.100  1.00 69.35  ?  302  HEC A CHD 1 
HETATM 19428 N  NA  . HEC J 9  .    ? -26.706 -54.574  54.410  1.00 68.05  ?  302  HEC A NA  1 
HETATM 19429 C  C1A . HEC J 9  .    ? -25.459 -54.629  53.814  1.00 67.23  ?  302  HEC A C1A 1 
HETATM 19430 C  C2A . HEC J 9  .    ? -25.650 -54.606  52.375  1.00 66.98  ?  302  HEC A C2A 1 
HETATM 19431 C  C3A . HEC J 9  .    ? -26.960 -54.535  52.136  1.00 67.59  ?  302  HEC A C3A 1 
HETATM 19432 C  C4A . HEC J 9  .    ? -27.654 -54.513  53.406  1.00 68.57  ?  302  HEC A C4A 1 
HETATM 19433 C  CMA . HEC J 9  .    ? -27.616 -54.489  50.741  1.00 67.75  ?  302  HEC A CMA 1 
HETATM 19434 C  CAA . HEC J 9  .    ? -24.551 -54.639  51.290  1.00 65.45  ?  302  HEC A CAA 1 
HETATM 19435 C  CBA . HEC J 9  .    ? -23.624 -53.438  51.457  1.00 64.90  ?  302  HEC A CBA 1 
HETATM 19436 C  CGA . HEC J 9  .    ? -23.340 -52.823  50.114  1.00 63.79  ?  302  HEC A CGA 1 
HETATM 19437 O  O1A . HEC J 9  .    ? -22.457 -51.931  50.038  1.00 63.83  ?  302  HEC A O1A 1 
HETATM 19438 O  O2A . HEC J 9  .    ? -23.998 -53.223  49.121  1.00 63.92  ?  302  HEC A O2A 1 
HETATM 19439 N  NB  . HEC J 9  .    ? -29.115 -54.903  56.011  1.00 69.70  ?  302  HEC A NB  1 
HETATM 19440 C  C1B . HEC J 9  .    ? -29.679 -54.571  54.795  1.00 70.00  ?  302  HEC A C1B 1 
HETATM 19441 C  C2B . HEC J 9  .    ? -31.098 -54.371  55.001  1.00 70.81  ?  302  HEC A C2B 1 
HETATM 19442 C  C3B . HEC J 9  .    ? -31.368 -54.569  56.296  1.00 70.66  ?  302  HEC A C3B 1 
HETATM 19443 C  C4B . HEC J 9  .    ? -30.124 -54.914  56.956  1.00 70.32  ?  302  HEC A C4B 1 
HETATM 19444 C  CMB . HEC J 9  .    ? -32.092 -53.979  53.890  1.00 71.78  ?  302  HEC A CMB 1 
HETATM 19445 C  CAB . HEC J 9  .    ? -32.747 -54.469  56.991  1.00 71.03  ?  302  HEC A CAB 1 
HETATM 19446 C  CBB . HEC J 9  .    ? -33.668 -55.628  56.546  1.00 71.68  ?  302  HEC A CBB 1 
HETATM 19447 N  NC  . HEC J 9  .    ? -27.535 -55.557  58.319  1.00 69.45  ?  302  HEC A NC  1 
HETATM 19448 C  C1C . HEC J 9  .    ? -28.778 -55.499  58.922  1.00 70.17  ?  302  HEC A C1C 1 
HETATM 19449 C  C2C . HEC J 9  .    ? -28.634 -55.938  60.293  1.00 71.00  ?  302  HEC A C2C 1 
HETATM 19450 C  C3C . HEC J 9  .    ? -27.324 -56.037  60.548  1.00 70.14  ?  302  HEC A C3C 1 
HETATM 19451 C  C4C . HEC J 9  .    ? -26.612 -55.886  59.293  1.00 69.55  ?  302  HEC A C4C 1 
HETATM 19452 C  CMC . HEC J 9  .    ? -29.759 -55.841  61.346  1.00 72.03  ?  302  HEC A CMC 1 
HETATM 19453 C  CAC . HEC J 9  .    ? -26.671 -56.401  61.901  1.00 69.80  ?  302  HEC A CAC 1 
HETATM 19454 C  CBC . HEC J 9  .    ? -27.046 -57.842  62.314  1.00 70.75  ?  302  HEC A CBC 1 
HETATM 19455 N  ND  . HEC J 9  .    ? -25.068 -55.291  56.750  1.00 68.59  ?  302  HEC A ND  1 
HETATM 19456 C  C1D . HEC J 9  .    ? -24.552 -55.803  57.939  1.00 69.00  ?  302  HEC A C1D 1 
HETATM 19457 C  C2D . HEC J 9  .    ? -23.136 -56.044  57.763  1.00 69.22  ?  302  HEC A C2D 1 
HETATM 19458 C  C3D . HEC J 9  .    ? -22.823 -55.619  56.324  1.00 68.08  ?  302  HEC A C3D 1 
HETATM 19459 C  C4D . HEC J 9  .    ? -24.081 -55.171  55.773  1.00 67.67  ?  302  HEC A C4D 1 
HETATM 19460 C  CMD . HEC J 9  .    ? -22.144 -56.604  58.805  1.00 69.86  ?  302  HEC A CMD 1 
HETATM 19461 C  CAD . HEC J 9  .    ? -21.458 -55.667  55.608  1.00 66.70  ?  302  HEC A CAD 1 
HETATM 19462 C  CBD . HEC J 9  .    ? -20.979 -54.243  55.349  1.00 66.46  ?  302  HEC A CBD 1 
HETATM 19463 C  CGD . HEC J 9  .    ? -19.837 -54.270  54.370  1.00 65.16  ?  302  HEC A CGD 1 
HETATM 19464 O  O1D . HEC J 9  .    ? -19.255 -53.190  54.094  1.00 65.94  ?  302  HEC A O1D 1 
HETATM 19465 O  O2D . HEC J 9  .    ? -19.508 -55.374  53.865  1.00 64.68  ?  302  HEC A O2D 1 
HETATM 19466 FE FE  . HEC K 9  .    ? -32.623 -64.623  56.653  1.00 61.66  ?  303  HEC A FE  1 
HETATM 19467 C  CHA . HEC K 9  .    ? -35.652 -64.062  55.175  1.00 61.25  ?  303  HEC A CHA 1 
HETATM 19468 C  CHB . HEC K 9  .    ? -33.207 -67.989  56.618  1.00 63.69  ?  303  HEC A CHB 1 
HETATM 19469 C  CHC . HEC K 9  .    ? -29.414 -65.220  57.784  1.00 58.87  ?  303  HEC A CHC 1 
HETATM 19470 C  CHD . HEC K 9  .    ? -32.384 -61.389  57.663  1.00 57.75  ?  303  HEC A CHD 1 
HETATM 19471 N  NA  . HEC K 9  .    ? -34.206 -65.811  56.100  1.00 63.01  ?  303  HEC A NA  1 
HETATM 19472 C  C1A . HEC K 9  .    ? -35.260 -65.373  55.323  1.00 62.54  ?  303  HEC A C1A 1 
HETATM 19473 C  C2A . HEC K 9  .    ? -35.864 -66.531  54.693  1.00 63.53  ?  303  HEC A C2A 1 
HETATM 19474 C  C3A . HEC K 9  .    ? -35.191 -67.617  55.094  1.00 64.10  ?  303  HEC A C3A 1 
HETATM 19475 C  C4A . HEC K 9  .    ? -34.134 -67.187  55.988  1.00 63.66  ?  303  HEC A C4A 1 
HETATM 19476 C  CMA . HEC K 9  .    ? -35.478 -69.078  54.683  1.00 64.79  ?  303  HEC A CMA 1 
HETATM 19477 C  CAA . HEC K 9  .    ? -37.078 -66.505  53.737  1.00 62.62  ?  303  HEC A CAA 1 
HETATM 19478 C  CBA . HEC K 9  .    ? -36.617 -66.691  52.293  1.00 63.10  ?  303  HEC A CBA 1 
HETATM 19479 C  CGA . HEC K 9  .    ? -35.901 -65.458  51.806  1.00 62.20  ?  303  HEC A CGA 1 
HETATM 19480 O  O1A . HEC K 9  .    ? -36.303 -64.334  52.200  1.00 60.77  ?  303  HEC A O1A 1 
HETATM 19481 O  O2A . HEC K 9  .    ? -34.936 -65.594  51.010  1.00 61.38  ?  303  HEC A O2A 1 
HETATM 19482 N  NB  . HEC K 9  .    ? -31.526 -66.314  57.222  1.00 61.31  ?  303  HEC A NB  1 
HETATM 19483 C  C1B . HEC K 9  .    ? -31.917 -67.601  56.910  1.00 62.45  ?  303  HEC A C1B 1 
HETATM 19484 C  C2B . HEC K 9  .    ? -30.738 -68.446  56.936  1.00 61.61  ?  303  HEC A C2B 1 
HETATM 19485 C  C3B . HEC K 9  .    ? -29.685 -67.689  57.260  1.00 59.97  ?  303  HEC A C3B 1 
HETATM 19486 C  C4B . HEC K 9  .    ? -30.161 -66.326  57.444  1.00 59.97  ?  303  HEC A C4B 1 
HETATM 19487 C  CMB . HEC K 9  .    ? -30.708 -69.963  56.643  1.00 62.25  ?  303  HEC A CMB 1 
HETATM 19488 C  CAB . HEC K 9  .    ? -28.229 -68.203  57.386  1.00 59.14  ?  303  HEC A CAB 1 
HETATM 19489 C  CBB . HEC K 9  .    ? -27.638 -67.957  58.790  1.00 60.76  ?  303  HEC A CBB 1 
HETATM 19490 N  NC  . HEC K 9  .    ? -31.181 -63.514  57.619  1.00 59.11  ?  303  HEC A NC  1 
HETATM 19491 C  C1C . HEC K 9  .    ? -29.889 -63.929  57.878  1.00 58.20  ?  303  HEC A C1C 1 
HETATM 19492 C  C2C . HEC K 9  .    ? -29.159 -62.796  58.405  1.00 56.26  ?  303  HEC A C2C 1 
HETATM 19493 C  C3C . HEC K 9  .    ? -29.914 -61.706  58.236  1.00 55.51  ?  303  HEC A C3C 1 
HETATM 19494 C  C4C . HEC K 9  .    ? -31.242 -62.149  57.826  1.00 57.68  ?  303  HEC A C4C 1 
HETATM 19495 C  CMC . HEC K 9  .    ? -27.632 -62.784  58.626  1.00 53.20  ?  303  HEC A CMC 1 
HETATM 19496 C  CAC . HEC K 9  .    ? -29.437 -60.271  58.576  1.00 52.80  ?  303  HEC A CAC 1 
HETATM 19497 C  CBC . HEC K 9  .    ? -30.371 -59.547  59.567  1.00 52.82  ?  303  HEC A CBC 1 
HETATM 19498 N  ND  . HEC K 9  .    ? -33.870 -62.985  56.500  1.00 59.97  ?  303  HEC A ND  1 
HETATM 19499 C  C1D . HEC K 9  .    ? -33.475 -61.705  56.878  1.00 58.48  ?  303  HEC A C1D 1 
HETATM 19500 C  C2D . HEC K 9  .    ? -34.403 -60.753  56.308  1.00 57.24  ?  303  HEC A C2D 1 
HETATM 19501 C  C3D . HEC K 9  .    ? -35.426 -61.588  55.527  1.00 57.45  ?  303  HEC A C3D 1 
HETATM 19502 C  C4D . HEC K 9  .    ? -35.014 -62.962  55.706  1.00 59.70  ?  303  HEC A C4D 1 
HETATM 19503 C  CMD . HEC K 9  .    ? -34.369 -59.217  56.453  1.00 53.40  ?  303  HEC A CMD 1 
HETATM 19504 C  CAD . HEC K 9  .    ? -36.639 -61.069  54.722  1.00 55.31  ?  303  HEC A CAD 1 
HETATM 19505 C  CBD . HEC K 9  .    ? -36.327 -61.179  53.231  1.00 54.95  ?  303  HEC A CBD 1 
HETATM 19506 C  CGD . HEC K 9  .    ? -37.463 -60.631  52.405  1.00 52.88  ?  303  HEC A CGD 1 
HETATM 19507 O  O1D . HEC K 9  .    ? -37.317 -60.564  51.157  1.00 52.46  ?  303  HEC A O1D 1 
HETATM 19508 O  O2D . HEC K 9  .    ? -38.513 -60.259  52.992  1.00 52.37  ?  303  HEC A O2D 1 
HETATM 19509 FE FE  . HEC L 9  .    ? -35.924 -73.205  57.691  1.00 68.29  ?  304  HEC A FE  1 
HETATM 19510 C  CHA . HEC L 9  .    ? -38.639 -71.428  56.629  1.00 66.92  ?  304  HEC A CHA 1 
HETATM 19511 C  CHB . HEC L 9  .    ? -34.476 -70.326  58.859  1.00 64.94  ?  304  HEC A CHB 1 
HETATM 19512 C  CHC . HEC L 9  .    ? -33.364 -75.044  59.078  1.00 68.28  ?  304  HEC A CHC 1 
HETATM 19513 C  CHD . HEC L 9  .    ? -37.004 -76.005  56.018  1.00 70.18  ?  304  HEC A CHD 1 
HETATM 19514 N  NA  . HEC L 9  .    ? -36.430 -71.222  57.673  1.00 66.24  ?  304  HEC A NA  1 
HETATM 19515 C  C1A . HEC L 9  .    ? -37.669 -70.726  57.312  1.00 66.04  ?  304  HEC A C1A 1 
HETATM 19516 C  C2A . HEC L 9  .    ? -37.756 -69.356  57.789  1.00 63.97  ?  304  HEC A C2A 1 
HETATM 19517 C  C3A . HEC L 9  .    ? -36.607 -69.061  58.399  1.00 63.47  ?  304  HEC A C3A 1 
HETATM 19518 C  C4A . HEC L 9  .    ? -35.747 -70.224  58.341  1.00 65.39  ?  304  HEC A C4A 1 
HETATM 19519 C  CMA . HEC L 9  .    ? -36.257 -67.710  59.056  1.00 61.80  ?  304  HEC A CMA 1 
HETATM 19520 C  CAA . HEC L 9  .    ? -38.943 -68.378  57.630  1.00 61.05  ?  304  HEC A CAA 1 
HETATM 19521 C  CBA . HEC L 9  .    ? -39.290 -68.172  56.158  1.00 61.39  ?  304  HEC A CBA 1 
HETATM 19522 C  CGA . HEC L 9  .    ? -40.036 -66.875  55.987  1.00 58.35  ?  304  HEC A CGA 1 
HETATM 19523 O  O1A . HEC L 9  .    ? -40.638 -66.667  54.902  1.00 58.74  ?  304  HEC A O1A 1 
HETATM 19524 O  O2A . HEC L 9  .    ? -40.032 -66.050  56.935  1.00 56.43  ?  304  HEC A O2A 1 
HETATM 19525 N  NB  . HEC L 9  .    ? -34.210 -72.763  58.734  1.00 66.93  ?  304  HEC A NB  1 
HETATM 19526 C  C1B . HEC L 9  .    ? -33.848 -71.507  59.183  1.00 65.65  ?  304  HEC A C1B 1 
HETATM 19527 C  C2B . HEC L 9  .    ? -32.702 -71.653  60.055  1.00 65.43  ?  304  HEC A C2B 1 
HETATM 19528 C  C3B . HEC L 9  .    ? -32.390 -72.953  60.112  1.00 66.08  ?  304  HEC A C3B 1 
HETATM 19529 C  C4B . HEC L 9  .    ? -33.336 -73.680  59.286  1.00 67.27  ?  304  HEC A C4B 1 
HETATM 19530 C  CMB . HEC L 9  .    ? -31.977 -70.490  60.768  1.00 64.56  ?  304  HEC A CMB 1 
HETATM 19531 C  CAB . HEC L 9  .    ? -31.242 -73.589  60.925  1.00 65.50  ?  304  HEC A CAB 1 
HETATM 19532 C  CBB . HEC L 9  .    ? -31.565 -73.533  62.436  1.00 65.72  ?  304  HEC A CBB 1 
HETATM 19533 N  NC  . HEC L 9  .    ? -35.271 -75.164  57.525  1.00 69.47  ?  304  HEC A NC  1 
HETATM 19534 C  C1C . HEC L 9  .    ? -34.253 -75.725  58.271  1.00 69.53  ?  304  HEC A C1C 1 
HETATM 19535 C  C2C . HEC L 9  .    ? -34.222 -77.142  57.974  1.00 70.66  ?  304  HEC A C2C 1 
HETATM 19536 C  C3C . HEC L 9  .    ? -35.280 -77.438  57.213  1.00 70.77  ?  304  HEC A C3C 1 
HETATM 19537 C  C4C . HEC L 9  .    ? -35.928 -76.184  56.860  1.00 70.32  ?  304  HEC A C4C 1 
HETATM 19538 C  CMC . HEC L 9  .    ? -33.328 -78.172  58.696  1.00 71.12  ?  304  HEC A CMC 1 
HETATM 19539 C  CAC . HEC L 9  .    ? -35.651 -78.866  56.737  1.00 71.42  ?  304  HEC A CAC 1 
HETATM 19540 C  CBC . HEC L 9  .    ? -35.721 -78.979  55.198  1.00 70.71  ?  304  HEC A CBC 1 
HETATM 19541 N  ND  . HEC L 9  .    ? -37.536 -73.633  56.444  1.00 68.79  ?  304  HEC A ND  1 
HETATM 19542 C  C1D . HEC L 9  .    ? -37.849 -74.917  56.004  1.00 69.84  ?  304  HEC A C1D 1 
HETATM 19543 C  C2D . HEC L 9  .    ? -39.215 -74.928  55.531  1.00 69.83  ?  304  HEC A C2D 1 
HETATM 19544 C  C3D . HEC L 9  .    ? -39.721 -73.492  55.720  1.00 68.98  ?  304  HEC A C3D 1 
HETATM 19545 C  C4D . HEC L 9  .    ? -38.614 -72.764  56.294  1.00 68.21  ?  304  HEC A C4D 1 
HETATM 19546 C  CMD . HEC L 9  .    ? -39.996 -76.127  54.953  1.00 69.63  ?  304  HEC A CMD 1 
HETATM 19547 C  CAD . HEC L 9  .    ? -41.122 -72.940  55.387  1.00 67.82  ?  304  HEC A CAD 1 
HETATM 19548 C  CBD . HEC L 9  .    ? -42.097 -73.474  56.431  1.00 68.67  ?  304  HEC A CBD 1 
HETATM 19549 C  CGD . HEC L 9  .    ? -42.121 -72.548  57.619  1.00 67.83  ?  304  HEC A CGD 1 
HETATM 19550 O  O1D . HEC L 9  .    ? -41.650 -71.390  57.484  1.00 66.40  ?  304  HEC A O1D 1 
HETATM 19551 O  O2D . HEC L 9  .    ? -42.616 -72.966  58.698  1.00 68.30  ?  304  HEC A O2D 1 
HETATM 19552 FE FE  . HEC M 9  .    ? -39.411 -84.493  58.077  1.00 77.63  ?  305  HEC A FE  1 
HETATM 19553 C  CHA . HEC M 9  .    ? -41.021 -85.873  60.767  1.00 78.65  ?  305  HEC A CHA 1 
HETATM 19554 C  CHB . HEC M 9  .    ? -42.287 -82.769  57.250  1.00 77.12  ?  305  HEC A CHB 1 
HETATM 19555 C  CHC . HEC M 9  .    ? -37.754 -82.960  55.499  1.00 73.79  ?  305  HEC A CHC 1 
HETATM 19556 C  CHD . HEC M 9  .    ? -36.657 -86.512  58.632  1.00 76.67  ?  305  HEC A CHD 1 
HETATM 19557 N  NA  . HEC M 9  .    ? -41.298 -84.338  58.862  1.00 78.31  ?  305  HEC A NA  1 
HETATM 19558 C  C1A . HEC M 9  .    ? -41.757 -85.016  59.977  1.00 78.52  ?  305  HEC A C1A 1 
HETATM 19559 C  C2A . HEC M 9  .    ? -43.149 -84.660  60.168  1.00 78.69  ?  305  HEC A C2A 1 
HETATM 19560 C  C3A . HEC M 9  .    ? -43.498 -83.808  59.203  1.00 78.34  ?  305  HEC A C3A 1 
HETATM 19561 C  C4A . HEC M 9  .    ? -42.342 -83.585  58.358  1.00 77.87  ?  305  HEC A C4A 1 
HETATM 19562 C  CMA . HEC M 9  .    ? -44.892 -83.171  59.020  1.00 78.60  ?  305  HEC A CMA 1 
HETATM 19563 C  CAA . HEC M 9  .    ? -44.074 -85.177  61.292  1.00 79.26  ?  305  HEC A CAA 1 
HETATM 19564 C  CBA . HEC M 9  .    ? -44.423 -86.643  61.052  1.00 81.00  ?  305  HEC A CBA 1 
HETATM 19565 C  CGA . HEC M 9  .    ? -45.126 -87.194  62.265  1.00 82.43  ?  305  HEC A CGA 1 
HETATM 19566 O  O1A . HEC M 9  .    ? -45.198 -86.475  63.296  1.00 81.68  ?  305  HEC A O1A 1 
HETATM 19567 O  O2A . HEC M 9  .    ? -45.611 -88.354  62.205  1.00 84.26  ?  305  HEC A O2A 1 
HETATM 19568 N  NB  . HEC M 9  .    ? -39.921 -83.104  56.657  1.00 75.99  ?  305  HEC A NB  1 
HETATM 19569 C  C1B . HEC M 9  .    ? -41.174 -82.554  56.464  1.00 76.03  ?  305  HEC A C1B 1 
HETATM 19570 C  C2B . HEC M 9  .    ? -41.111 -81.708  55.290  1.00 74.28  ?  305  HEC A C2B 1 
HETATM 19571 C  C3B . HEC M 9  .    ? -39.866 -81.764  54.802  1.00 73.14  ?  305  HEC A C3B 1 
HETATM 19572 C  C4B . HEC M 9  .    ? -39.087 -82.640  55.656  1.00 74.35  ?  305  HEC A C4B 1 
HETATM 19573 C  CMB . HEC M 9  .    ? -42.298 -80.904  54.716  1.00 73.92  ?  305  HEC A CMB 1 
HETATM 19574 C  CAB . HEC M 9  .    ? -39.324 -81.021  53.559  1.00 70.65  ?  305  HEC A CAB 1 
HETATM 19575 C  CBB . HEC M 9  .    ? -39.186 -79.512  53.859  1.00 69.77  ?  305  HEC A CBB 1 
HETATM 19576 N  NC  . HEC M 9  .    ? -37.566 -84.748  57.185  1.00 76.40  ?  305  HEC A NC  1 
HETATM 19577 C  C1C . HEC M 9  .    ? -37.052 -83.910  56.213  1.00 74.99  ?  305  HEC A C1C 1 
HETATM 19578 C  C2C . HEC M 9  .    ? -35.635 -84.186  56.099  1.00 74.19  ?  305  HEC A C2C 1 
HETATM 19579 C  C3C . HEC M 9  .    ? -35.329 -85.184  56.933  1.00 74.98  ?  305  HEC A C3C 1 
HETATM 19580 C  C4C . HEC M 9  .    ? -36.537 -85.546  57.654  1.00 76.33  ?  305  HEC A C4C 1 
HETATM 19581 C  CMC . HEC M 9  .    ? -34.670 -83.508  55.106  1.00 72.01  ?  305  HEC A CMC 1 
HETATM 19582 C  CAC . HEC M 9  .    ? -33.918 -85.795  57.113  1.00 74.74  ?  305  HEC A CAC 1 
HETATM 19583 C  CBC . HEC M 9  .    ? -33.915 -87.297  56.758  1.00 75.88  ?  305  HEC A CBC 1 
HETATM 19584 N  ND  . HEC M 9  .    ? -38.918 -85.982  59.468  1.00 78.11  ?  305  HEC A ND  1 
HETATM 19585 C  C1D . HEC M 9  .    ? -37.694 -86.646  59.531  1.00 77.66  ?  305  HEC A C1D 1 
HETATM 19586 C  C2D . HEC M 9  .    ? -37.687 -87.506  60.696  1.00 78.46  ?  305  HEC A C2D 1 
HETATM 19587 C  C3D . HEC M 9  .    ? -39.055 -87.297  61.361  1.00 79.26  ?  305  HEC A C3D 1 
HETATM 19588 C  C4D . HEC M 9  .    ? -39.747 -86.341  60.528  1.00 78.40  ?  305  HEC A C4D 1 
HETATM 19589 C  CMD . HEC M 9  .    ? -36.543 -88.430  61.171  1.00 80.37  ?  305  HEC A CMD 1 
HETATM 19590 C  CAD . HEC M 9  .    ? -39.606 -87.960  62.641  1.00 82.03  ?  305  HEC A CAD 1 
HETATM 19591 C  CBD . HEC M 9  .    ? -39.847 -89.444  62.393  1.00 86.23  ?  305  HEC A CBD 1 
HETATM 19592 C  CGD . HEC M 9  .    ? -40.805 -89.968  63.430  1.00 88.28  ?  305  HEC A CGD 1 
HETATM 19593 O  O1D . HEC M 9  .    ? -41.388 -89.141  64.179  1.00 87.94  ?  305  HEC A O1D 1 
HETATM 19594 O  O2D . HEC M 9  .    ? -40.992 -91.211  63.505  1.00 90.62  ?  305  HEC A O2D 1 
HETATM 19595 FE FE1 . SF4 N 10 .    ? -26.906 -44.727  19.680  1.00 74.88  ?  1101 SF4 B FE1 1 
HETATM 19596 FE FE2 . SF4 N 10 .    ? -24.765 -44.732  21.372  1.00 70.33  ?  1101 SF4 B FE2 1 
HETATM 19597 FE FE3 . SF4 N 10 .    ? -27.207 -43.876  22.262  1.00 72.53  ?  1101 SF4 B FE3 1 
HETATM 19598 FE FE4 . SF4 N 10 .    ? -25.789 -42.355  20.472  1.00 71.73  ?  1101 SF4 B FE4 1 
HETATM 19599 S  S1  . SF4 N 10 .    ? -25.190 -42.864  22.615  1.00 68.97  ?  1101 SF4 B S1  1 
HETATM 19600 S  S2  . SF4 N 10 .    ? -28.012 -42.860  20.384  1.00 74.96  ?  1101 SF4 B S2  1 
HETATM 19601 S  S3  . SF4 N 10 .    ? -24.802 -43.984  19.220  1.00 71.28  ?  1101 SF4 B S3  1 
HETATM 19602 S  S4  . SF4 N 10 .    ? -26.664 -45.975  21.572  1.00 72.20  ?  1101 SF4 B S4  1 
HETATM 19603 FE FE1 . SF4 O 10 .    ? -28.553 -46.840  33.273  1.00 53.72  ?  1102 SF4 B FE1 1 
HETATM 19604 FE FE2 . SF4 O 10 .    ? -28.696 -44.106  33.268  1.00 53.35  ?  1102 SF4 B FE2 1 
HETATM 19605 FE FE3 . SF4 O 10 .    ? -30.483 -45.569  31.810  1.00 52.23  ?  1102 SF4 B FE3 1 
HETATM 19606 FE FE4 . SF4 O 10 .    ? -27.861 -45.432  31.032  1.00 56.36  ?  1102 SF4 B FE4 1 
HETATM 19607 S  S1  . SF4 O 10 .    ? -29.351 -43.712  31.123  1.00 54.05  ?  1102 SF4 B S1  1 
HETATM 19608 S  S2  . SF4 O 10 .    ? -29.166 -47.300  31.129  1.00 54.27  ?  1102 SF4 B S2  1 
HETATM 19609 S  S3  . SF4 O 10 .    ? -26.816 -45.374  33.055  1.00 55.67  ?  1102 SF4 B S3  1 
HETATM 19610 S  S4  . SF4 O 10 .    ? -30.258 -45.560  34.077  1.00 51.21  ?  1102 SF4 B S4  1 
HETATM 19611 FE FE1 . SF4 P 10 .    ? -29.316 -35.250  37.947  1.00 48.34  ?  1103 SF4 B FE1 1 
HETATM 19612 FE FE2 . SF4 P 10 .    ? -30.128 -33.600  39.967  1.00 48.67  ?  1103 SF4 B FE2 1 
HETATM 19613 FE FE3 . SF4 P 10 .    ? -30.661 -32.940  37.369  1.00 47.48  ?  1103 SF4 B FE3 1 
HETATM 19614 FE FE4 . SF4 P 10 .    ? -28.088 -32.833  38.314  1.00 45.35  ?  1103 SF4 B FE4 1 
HETATM 19615 S  S1  . SF4 P 10 .    ? -29.849 -31.556  38.994  1.00 46.50  ?  1103 SF4 B S1  1 
HETATM 19616 S  S2  . SF4 P 10 .    ? -28.788 -33.728  36.334  1.00 46.39  ?  1103 SF4 B S2  1 
HETATM 19617 S  S3  . SF4 P 10 .    ? -28.088 -34.598  39.753  1.00 46.74  ?  1103 SF4 B S3  1 
HETATM 19618 S  S4  . SF4 P 10 .    ? -31.463 -34.738  38.511  1.00 49.35  ?  1103 SF4 B S4  1 
HETATM 19619 FE FE1 . F3S Q 11 .    ? -38.694 -34.535  46.264  1.00 96.00  ?  1104 F3S B FE1 1 
HETATM 19620 FE FE3 . F3S Q 11 .    ? -38.752 -34.320  43.943  1.00 100.07 ?  1104 F3S B FE3 1 
HETATM 19621 FE FE4 . F3S Q 11 .    ? -40.040 -36.115  45.126  1.00 150.10 ?  1104 F3S B FE4 1 
HETATM 19622 S  S1  . F3S Q 11 .    ? -39.222 -32.607  45.248  1.00 86.20  ?  1104 F3S B S1  1 
HETATM 19623 S  S2  . F3S Q 11 .    ? -40.631 -35.237  47.089  1.00 74.14  ?  1104 F3S B S2  1 
HETATM 19624 S  S3  . F3S Q 11 .    ? -37.829 -36.079  44.929  1.00 97.44  ?  1104 F3S B S3  1 
HETATM 19625 S  S4  . F3S Q 11 .    ? -40.895 -34.755  43.579  1.00 109.06 ?  1104 F3S B S4  1 
HETATM 19626 FE FE  . HEC R 9  .    ? -26.642 -92.906  51.166  1.00 96.90  ?  301  HEC E FE  1 
HETATM 19627 C  CHA . HEC R 9  .    ? -26.827 -96.109  49.976  1.00 99.96  ?  301  HEC E CHA 1 
HETATM 19628 C  CHB . HEC R 9  .    ? -23.471 -92.583  49.925  1.00 92.22  ?  301  HEC E CHB 1 
HETATM 19629 C  CHC . HEC R 9  .    ? -26.659 -89.506  51.898  1.00 90.28  ?  301  HEC E CHC 1 
HETATM 19630 C  CHD . HEC R 9  .    ? -29.905 -93.094  52.333  1.00 98.93  ?  301  HEC E CHD 1 
HETATM 19631 N  NA  . HEC R 9  .    ? -25.396 -94.105  50.110  1.00 96.57  ?  301  HEC E NA  1 
HETATM 19632 C  C1A . HEC R 9  .    ? -25.643 -95.426  49.784  1.00 98.11  ?  301  HEC E C1A 1 
HETATM 19633 C  C2A . HEC R 9  .    ? -24.434 -95.969  49.203  1.00 97.84  ?  301  HEC E C2A 1 
HETATM 19634 C  C3A . HEC R 9  .    ? -23.510 -95.006  49.187  1.00 95.51  ?  301  HEC E C3A 1 
HETATM 19635 C  C4A . HEC R 9  .    ? -24.092 -93.806  49.758  1.00 94.74  ?  301  HEC E C4A 1 
HETATM 19636 C  CMA . HEC R 9  .    ? -22.072 -95.153  48.650  1.00 94.02  ?  301  HEC E CMA 1 
HETATM 19637 C  CAA . HEC R 9  .    ? -24.253 -97.415  48.694  1.00 99.34  ?  301  HEC E CAA 1 
HETATM 19638 C  CBA . HEC R 9  .    ? -24.655 -97.494  47.226  1.00 98.65  ?  301  HEC E CBA 1 
HETATM 19639 C  CGA . HEC R 9  .    ? -24.699 -98.936  46.796  1.00 101.22 ?  301  HEC E CGA 1 
HETATM 19640 O  O1A . HEC R 9  .    ? -24.897 -99.191  45.579  1.00 100.91 ?  301  HEC E O1A 1 
HETATM 19641 O  O2A . HEC R 9  .    ? -24.536 -99.829  47.668  1.00 104.00 ?  301  HEC E O2A 1 
HETATM 19642 N  NB  . HEC R 9  .    ? -25.283 -91.345  51.026  1.00 92.71  ?  301  HEC E NB  1 
HETATM 19643 C  C1B . HEC R 9  .    ? -24.089 -91.419  50.336  1.00 91.43  ?  301  HEC E C1B 1 
HETATM 19644 C  C2B . HEC R 9  .    ? -23.617 -90.064  50.120  1.00 87.18  ?  301  HEC E C2B 1 
HETATM 19645 C  C3B . HEC R 9  .    ? -24.497 -89.221  50.673  1.00 87.18  ?  301  HEC E C3B 1 
HETATM 19646 C  C4B . HEC R 9  .    ? -25.554 -90.009  51.257  1.00 90.52  ?  301  HEC E C4B 1 
HETATM 19647 C  CMB . HEC R 9  .    ? -22.313 -89.679  49.391  1.00 81.55  ?  301  HEC E CMB 1 
HETATM 19648 C  CAB . HEC R 9  .    ? -24.449 -87.678  50.703  1.00 83.30  ?  301  HEC E CAB 1 
HETATM 19649 C  CBB . HEC R 9  .    ? -24.759 -87.108  49.299  1.00 80.68  ?  301  HEC E CBB 1 
HETATM 19650 N  NC  . HEC R 9  .    ? -28.042 -91.547  51.903  1.00 95.95  ?  301  HEC E NC  1 
HETATM 19651 C  C1C . HEC R 9  .    ? -27.784 -90.226  52.224  1.00 93.39  ?  301  HEC E C1C 1 
HETATM 19652 C  C2C . HEC R 9  .    ? -28.973 -89.665  52.826  1.00 93.10  ?  301  HEC E C2C 1 
HETATM 19653 C  C3C . HEC R 9  .    ? -29.792 -90.685  53.110  1.00 94.76  ?  301  HEC E C3C 1 
HETATM 19654 C  C4C . HEC R 9  .    ? -29.283 -91.864  52.430  1.00 96.83  ?  301  HEC E C4C 1 
HETATM 19655 C  CMC . HEC R 9  .    ? -28.978 -88.282  53.514  1.00 89.79  ?  301  HEC E CMC 1 
HETATM 19656 C  CAC . HEC R 9  .    ? -31.148 -90.588  53.850  1.00 94.03  ?  301  HEC E CAC 1 
HETATM 19657 C  CBC . HEC R 9  .    ? -32.161 -89.832  52.964  1.00 91.13  ?  301  HEC E CBC 1 
HETATM 19658 N  ND  . HEC R 9  .    ? -28.177 -94.358  51.082  1.00 99.66  ?  301  HEC E ND  1 
HETATM 19659 C  C1D . HEC R 9  .    ? -29.362 -94.254  51.812  1.00 100.22 ?  301  HEC E C1D 1 
HETATM 19660 C  C2D . HEC R 9  .    ? -29.936 -95.575  51.945  1.00 102.11 ?  301  HEC E C2D 1 
HETATM 19661 C  C3D . HEC R 9  .    ? -28.977 -96.520  51.210  1.00 101.98 ?  301  HEC E C3D 1 
HETATM 19662 C  C4D . HEC R 9  .    ? -27.918 -95.676  50.702  1.00 100.52 ?  301  HEC E C4D 1 
HETATM 19663 C  CMD . HEC R 9  .    ? -31.242 -95.957  52.673  1.00 104.17 ?  301  HEC E CMD 1 
HETATM 19664 C  CAD . HEC R 9  .    ? -29.118 -98.048  51.044  1.00 103.58 ?  301  HEC E CAD 1 
HETATM 19665 C  CBD . HEC R 9  .    ? -29.944 -98.347  49.798  1.00 106.12 ?  301  HEC E CBD 1 
HETATM 19666 C  CGD . HEC R 9  .    ? -30.196 -99.829  49.710  1.00 107.71 ?  301  HEC E CGD 1 
HETATM 19667 O  O1D . HEC R 9  .    ? -30.865 -100.266 48.740  1.00 108.74 ?  301  HEC E O1D 1 
HETATM 19668 O  O2D . HEC R 9  .    ? -29.728 -100.572 50.610  1.00 107.56 ?  301  HEC E O2D 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   . ALA A 2    ? 1.2972 1.6623 1.3281 0.3182  0.0850  -0.1140 2    ALA A N   
2     C  CA  . ALA A 2    ? 1.3487 1.7260 1.3825 0.3202  0.0928  -0.1141 2    ALA A CA  
3     C  C   . ALA A 2    ? 1.3580 1.7523 1.4041 0.3214  0.0923  -0.1154 2    ALA A C   
4     O  O   . ALA A 2    ? 1.3905 1.7984 1.4425 0.3223  0.0987  -0.1156 2    ALA A O   
5     C  CB  . ALA A 2    ? 1.3687 1.7323 1.3853 0.3288  0.0933  -0.1143 2    ALA A CB  
6     N  N   . GLN A 3    ? 1.6041 1.9974 1.6536 0.3217  0.0846  -0.1162 3    GLN A N   
7     C  CA  . GLN A 3    ? 1.5914 2.0000 1.6517 0.3231  0.0831  -0.1175 3    GLN A CA  
8     C  C   . GLN A 3    ? 1.6564 2.0854 1.7357 0.3140  0.0876  -0.1175 3    GLN A C   
9     O  O   . GLN A 3    ? 1.7624 2.2086 1.8516 0.3138  0.0926  -0.1183 3    GLN A O   
10    C  CB  . GLN A 3    ? 1.5758 1.9751 1.6319 0.3267  0.0735  -0.1183 3    GLN A CB  
11    C  CG  . GLN A 3    ? 1.5494 1.9584 1.6092 0.3326  0.0710  -0.1198 3    GLN A CG  
12    C  CD  . GLN A 3    ? 1.5830 1.9799 1.6275 0.3432  0.0690  -0.1204 3    GLN A CD  
13    O  OE1 . GLN A 3    ? 1.5716 1.9487 1.6015 0.3465  0.0655  -0.1200 3    GLN A OE1 
14    N  NE2 . GLN A 3    ? 1.5787 1.9875 1.6264 0.3485  0.0711  -0.1214 3    GLN A NE2 
15    N  N   . ILE A 4    ? 1.2544 1.6817 1.3389 0.3064  0.0860  -0.1167 4    ILE A N   
16    C  CA  . ILE A 4    ? 1.1900 1.6353 1.2923 0.2974  0.0889  -0.1169 4    ILE A CA  
17    C  C   . ILE A 4    ? 1.1181 1.5608 1.2224 0.2890  0.0935  -0.1152 4    ILE A C   
18    O  O   . ILE A 4    ? 1.1054 1.5593 1.2230 0.2806  0.0951  -0.1152 4    ILE A O   
19    C  CB  . ILE A 4    ? 1.1729 1.6209 1.2816 0.2965  0.0809  -0.1178 4    ILE A CB  
20    C  CG1 . ILE A 4    ? 1.1984 1.6264 1.2964 0.2972  0.0739  -0.1169 4    ILE A CG1 
21    C  CG2 . ILE A 4    ? 1.2464 1.7002 1.3549 0.3044  0.0774  -0.1195 4    ILE A CG2 
22    C  CD1 . ILE A 4    ? 1.2574 1.6850 1.3589 0.2973  0.0659  -0.1177 4    ILE A CD1 
23    N  N   . PHE A 5    ? 1.3828 1.8106 1.4738 0.2912  0.0956  -0.1139 5    PHE A N   
24    C  CA  . PHE A 5    ? 1.3786 1.8015 1.4691 0.2841  0.0993  -0.1123 5    PHE A CA  
25    C  C   . PHE A 5    ? 1.3490 1.7681 1.4313 0.2854  0.1075  -0.1111 5    PHE A C   
26    O  O   . PHE A 5    ? 1.3638 1.7742 1.4339 0.2935  0.1072  -0.1113 5    PHE A O   
27    C  CB  . PHE A 5    ? 1.4320 1.8364 1.5129 0.2848  0.0917  -0.1117 5    PHE A CB  
28    C  CG  . PHE A 5    ? 1.5127 1.9210 1.6033 0.2801  0.0857  -0.1121 5    PHE A CG  
29    C  CD1 . PHE A 5    ? 1.4690 1.8869 1.5717 0.2706  0.0888  -0.1115 5    PHE A CD1 
30    C  CD2 . PHE A 5    ? 1.4766 1.8783 1.5638 0.2851  0.0772  -0.1132 5    PHE A CD2 
31    C  CE1 . PHE A 5    ? 1.3224 1.7435 1.4336 0.2663  0.0832  -0.1119 5    PHE A CE1 
32    C  CE2 . PHE A 5    ? 1.3296 1.7342 1.4249 0.2809  0.0718  -0.1134 5    PHE A CE2 
33    C  CZ  . PHE A 5    ? 1.2711 1.6855 1.3784 0.2716  0.0747  -0.1128 5    PHE A CZ  
34    N  N   . PRO A 6    ? 0.8888 1.3138 0.9769 0.2777  0.1151  -0.1097 6    PRO A N   
35    C  CA  . PRO A 6    ? 0.9107 1.3300 0.9893 0.2787  0.1231  -0.1083 6    PRO A CA  
36    C  C   . PRO A 6    ? 0.9913 1.3887 1.0522 0.2826  0.1193  -0.1072 6    PRO A C   
37    O  O   . PRO A 6    ? 0.9903 1.3775 1.0478 0.2831  0.1112  -0.1075 6    PRO A O   
38    C  CB  . PRO A 6    ? 0.9402 1.3715 1.0307 0.2684  0.1315  -0.1071 6    PRO A CB  
39    C  CG  . PRO A 6    ? 0.9849 1.4322 1.0931 0.2629  0.1285  -0.1086 6    PRO A CG  
40    C  CD  . PRO A 6    ? 0.9240 1.3619 1.0277 0.2677  0.1172  -0.1096 6    PRO A CD  
41    N  N   . ARG A 7    ? 1.4097 1.7997 1.4592 0.2855  0.1254  -0.1060 7    ARG A N   
42    C  CA  . ARG A 7    ? 1.4488 1.8178 1.4801 0.2903  0.1218  -0.1052 7    ARG A CA  
43    C  C   . ARG A 7    ? 1.4909 1.8527 1.5217 0.2840  0.1207  -0.1039 7    ARG A C   
44    O  O   . ARG A 7    ? 1.5736 1.9199 1.5943 0.2869  0.1135  -0.1041 7    ARG A O   
45    C  CB  . ARG A 7    ? 1.4401 1.8034 1.4591 0.2947  0.1290  -0.1042 7    ARG A CB  
46    C  CG  . ARG A 7    ? 1.5117 1.8532 1.5105 0.3016  0.1242  -0.1041 7    ARG A CG  
47    C  CD  . ARG A 7    ? 1.5987 1.9350 1.5850 0.3070  0.1307  -0.1034 7    ARG A CD  
48    N  NE  . ARG A 7    ? 1.5727 1.9168 1.5609 0.3127  0.1316  -0.1048 7    ARG A NE  
49    C  CZ  . ARG A 7    ? 1.4976 1.8575 1.4954 0.3108  0.1401  -0.1044 7    ARG A CZ  
50    N  NH1 . ARG A 7    ? 1.4426 1.8122 1.4490 0.3029  0.1488  -0.1028 7    ARG A NH1 
51    N  NH2 . ARG A 7    ? 1.3676 1.7335 1.3663 0.3168  0.1399  -0.1058 7    ARG A NH2 
52    N  N   . ASN A 8    ? 1.5714 1.9445 1.6131 0.2755  0.1277  -0.1025 8    ASN A N   
53    C  CA  . ASN A 8    ? 1.5714 1.9378 1.6118 0.2696  0.1278  -0.1009 8    ASN A CA  
54    C  C   . ASN A 8    ? 1.5654 1.9312 1.6131 0.2666  0.1190  -0.1019 8    ASN A C   
55    O  O   . ASN A 8    ? 1.5338 1.8913 1.5785 0.2633  0.1173  -0.1008 8    ASN A O   
56    C  CB  . ASN A 8    ? 1.5894 1.9678 1.6391 0.2611  0.1384  -0.0992 8    ASN A CB  
57    C  CG  . ASN A 8    ? 1.5736 1.9724 1.6436 0.2545  0.1399  -0.1005 8    ASN A CG  
58    O  OD1 . ASN A 8    ? 1.5417 1.9472 1.6181 0.2576  0.1343  -0.1025 8    ASN A OD1 
59    N  ND2 . ASN A 8    ? 1.5672 1.9755 1.6468 0.2455  0.1473  -0.0993 8    ASN A ND2 
60    N  N   . ALA A 9    ? 1.8698 2.2438 1.9265 0.2680  0.1136  -0.1037 9    ALA A N   
61    C  CA  . ALA A 9    ? 1.8112 2.1864 1.8764 0.2644  0.1062  -0.1044 9    ALA A CA  
62    C  C   . ALA A 9    ? 1.8721 2.2283 1.9253 0.2679  0.0981  -0.1044 9    ALA A C   
63    O  O   . ALA A 9    ? 1.9073 2.2615 1.9653 0.2632  0.0941  -0.1041 9    ALA A O   
64    C  CB  . ALA A 9    ? 1.8175 2.2034 1.8920 0.2666  0.1018  -0.1064 9    ALA A CB  
65    N  N   . ASN A 10   ? 1.9004 2.2425 1.9383 0.2758  0.0956  -0.1049 10   ASN A N   
66    C  CA  . ASN A 10   ? 1.8929 2.2166 1.9194 0.2790  0.0879  -0.1053 10   ASN A CA  
67    C  C   . ASN A 10   ? 1.8965 2.2140 1.9204 0.2740  0.0900  -0.1036 10   ASN A C   
68    O  O   . ASN A 10   ? 1.9219 2.2299 1.9452 0.2712  0.0833  -0.1033 10   ASN A O   
69    C  CB  . ASN A 10   ? 1.9492 2.2593 1.9593 0.2881  0.0859  -0.1063 10   ASN A CB  
70    C  CG  . ASN A 10   ? 1.9304 2.2449 1.9416 0.2937  0.0833  -0.1079 10   ASN A CG  
71    O  OD1 . ASN A 10   ? 1.9289 2.2544 1.9521 0.2915  0.0813  -0.1085 10   ASN A OD1 
72    N  ND2 . ASN A 10   ? 1.8536 2.1591 1.8516 0.3013  0.0833  -0.1087 10   ASN A ND2 
73    N  N   . LEU A 11   ? 1.4520 1.7731 1.4741 0.2716  0.0989  -0.1019 11   LEU A N   
74    C  CA  . LEU A 11   ? 1.4237 1.7360 1.4430 0.2634  0.1004  -0.0987 11   LEU A CA  
75    C  C   . LEU A 11   ? 1.4735 1.7962 1.5085 0.2532  0.1009  -0.0975 11   LEU A C   
76    O  O   . LEU A 11   ? 1.4692 1.7825 1.5039 0.2470  0.0965  -0.0958 11   LEU A O   
77    C  CB  . LEU A 11   ? 1.3465 1.6578 1.3578 0.2635  0.1099  -0.0968 11   LEU A CB  
78    C  CG  . LEU A 11   ? 1.3193 1.6203 1.3254 0.2559  0.1126  -0.0932 11   LEU A CG  
79    C  CD1 . LEU A 11   ? 1.3586 1.6403 1.3543 0.2564  0.1033  -0.0926 11   LEU A CD1 
80    C  CD2 . LEU A 11   ? 1.3013 1.6002 1.2974 0.2581  0.1221  -0.0915 11   LEU A CD2 
81    N  N   . LEU A 12   ? 1.4279 1.7705 1.4768 0.2513  0.1063  -0.0987 12   LEU A N   
82    C  CA  . LEU A 12   ? 1.4150 1.7688 1.4793 0.2415  0.1073  -0.0979 12   LEU A CA  
83    C  C   . LEU A 12   ? 1.3363 1.6857 1.4049 0.2401  0.0973  -0.0987 12   LEU A C   
84    O  O   . LEU A 12   ? 1.2774 1.6235 1.3506 0.2318  0.0954  -0.0969 12   LEU A O   
85    C  CB  . LEU A 12   ? 1.3712 1.7482 1.4498 0.2410  0.1139  -0.0999 12   LEU A CB  
86    C  CG  . LEU A 12   ? 1.3185 1.7046 1.4009 0.2353  0.1254  -0.0984 12   LEU A CG  
87    C  CD1 . LEU A 12   ? 1.4045 1.7838 1.4730 0.2421  0.1312  -0.0977 12   LEU A CD1 
88    C  CD2 . LEU A 12   ? 1.2621 1.6698 1.3619 0.2310  0.1292  -0.1000 12   LEU A CD2 
89    N  N   . SER A 13   ? 1.5491 1.8978 1.6159 0.2483  0.0910  -0.1013 13   SER A N   
90    C  CA  . SER A 13   ? 1.5720 1.9165 1.6426 0.2476  0.0819  -0.1021 13   SER A CA  
91    C  C   . SER A 13   ? 1.5835 1.9085 1.6453 0.2437  0.0766  -0.0999 13   SER A C   
92    O  O   . SER A 13   ? 1.5038 1.8275 1.5721 0.2368  0.0731  -0.0987 13   SER A O   
93    C  CB  . SER A 13   ? 1.5952 1.9386 1.6621 0.2575  0.0765  -0.1049 13   SER A CB  
94    O  OG  . SER A 13   ? 1.5648 1.8914 1.6158 0.2645  0.0737  -0.1052 13   SER A OG  
95    N  N   . ARG A 14   ? 1.6422 1.9521 1.6891 0.2482  0.0758  -0.0993 14   ARG A N   
96    C  CA  . ARG A 14   ? 1.6290 1.9212 1.6675 0.2447  0.0709  -0.0974 14   ARG A CA  
97    C  C   . ARG A 14   ? 1.4747 1.7677 1.5172 0.2349  0.0756  -0.0942 14   ARG A C   
98    O  O   . ARG A 14   ? 1.5220 1.8076 1.5660 0.2291  0.0713  -0.0927 14   ARG A O   
99    C  CB  . ARG A 14   ? 1.5768 1.8543 1.5986 0.2517  0.0698  -0.0978 14   ARG A CB  
100   C  CG  . ARG A 14   ? 1.6503 1.9224 1.6660 0.2610  0.0637  -0.1009 14   ARG A CG  
101   C  CD  . ARG A 14   ? 1.6879 1.9533 1.6896 0.2690  0.0663  -0.1019 14   ARG A CD  
102   N  NE  . ARG A 14   ? 1.8124 2.0746 1.8089 0.2784  0.0618  -0.1051 14   ARG A NE  
103   C  CZ  . ARG A 14   ? 1.8936 2.1505 1.8781 0.2868  0.0633  -0.1067 14   ARG A CZ  
104   N  NH1 . ARG A 14   ? 2.0160 2.2703 1.9923 0.2874  0.0691  -0.1054 14   ARG A NH1 
105   N  NH2 . ARG A 14   ? 1.8025 2.0562 1.7826 0.2950  0.0590  -0.1097 14   ARG A NH2 
106   N  N   . LEU A 15   ? 1.1382 1.4399 1.1822 0.2330  0.0848  -0.0932 15   LEU A N   
107   C  CA  . LEU A 15   ? 1.1528 1.4554 1.2005 0.2236  0.0901  -0.0901 15   LEU A CA  
108   C  C   . LEU A 15   ? 1.2009 1.5142 1.2640 0.2159  0.0889  -0.0902 15   LEU A C   
109   O  O   . LEU A 15   ? 1.1917 1.4999 1.2567 0.2082  0.0885  -0.0879 15   LEU A O   
110   C  CB  . LEU A 15   ? 1.1774 1.4876 1.2239 0.2232  0.1008  -0.0893 15   LEU A CB  
111   C  CG  . LEU A 15   ? 1.1109 1.4129 1.1512 0.2171  0.1067  -0.0857 15   LEU A CG  
112   C  CD1 . LEU A 15   ? 1.1073 1.3890 1.1316 0.2205  0.1016  -0.0843 15   LEU A CD1 
113   C  CD2 . LEU A 15   ? 1.0927 1.4029 1.1319 0.2175  0.1178  -0.0851 15   LEU A CD2 
114   N  N   . SER A 16   ? 1.3936 1.7219 1.4675 0.2181  0.0883  -0.0928 16   SER A N   
115   C  CA  . SER A 16   ? 1.2881 1.6275 1.3767 0.2114  0.0868  -0.0933 16   SER A CA  
116   C  C   . SER A 16   ? 1.2116 1.5393 1.2990 0.2094  0.0779  -0.0926 16   SER A C   
117   O  O   . SER A 16   ? 1.1357 1.4639 1.2296 0.2013  0.0774  -0.0911 16   SER A O   
118   C  CB  . SER A 16   ? 1.3170 1.6744 1.4161 0.2158  0.0871  -0.0966 16   SER A CB  
119   O  OG  . SER A 16   ? 1.3720 1.7243 1.4675 0.2235  0.0790  -0.0986 16   SER A OG  
120   N  N   . ILE A 17   ? 1.1867 1.5037 1.2657 0.2166  0.0709  -0.0938 17   ILE A N   
121   C  CA  . ILE A 17   ? 1.1031 1.4078 1.1800 0.2149  0.0627  -0.0931 17   ILE A CA  
122   C  C   . ILE A 17   ? 1.0318 1.3243 1.1032 0.2085  0.0633  -0.0900 17   ILE A C   
123   O  O   . ILE A 17   ? 1.0350 1.3246 1.1112 0.2022  0.0604  -0.0886 17   ILE A O   
124   C  CB  . ILE A 17   ? 1.0904 1.3844 1.1579 0.2238  0.0560  -0.0950 17   ILE A CB  
125   C  CG1 . ILE A 17   ? 1.1268 1.4326 1.1994 0.2307  0.0553  -0.0981 17   ILE A CG1 
126   C  CG2 . ILE A 17   ? 1.1852 1.4662 1.2507 0.2216  0.0480  -0.0943 17   ILE A CG2 
127   C  CD1 . ILE A 17   ? 1.0421 1.3603 1.1284 0.2270  0.0536  -0.0988 17   ILE A CD1 
128   N  N   . PHE A 18   ? 1.1583 1.4434 1.2191 0.2105  0.0672  -0.0888 18   PHE A N   
129   C  CA  . PHE A 18   ? 1.1521 1.4261 1.2068 0.2051  0.0685  -0.0857 18   PHE A CA  
130   C  C   . PHE A 18   ? 1.1000 1.3824 1.1645 0.1958  0.0741  -0.0837 18   PHE A C   
131   O  O   . PHE A 18   ? 1.1045 1.3802 1.1701 0.1898  0.0719  -0.0817 18   PHE A O   
132   C  CB  . PHE A 18   ? 1.1712 1.4378 1.2128 0.2096  0.0728  -0.0849 18   PHE A CB  
133   C  CG  . PHE A 18   ? 1.1741 1.4287 1.2079 0.2053  0.0740  -0.0818 18   PHE A CG  
134   C  CD1 . PHE A 18   ? 1.2374 1.4779 1.2647 0.2056  0.0667  -0.0813 18   PHE A CD1 
135   C  CD2 . PHE A 18   ? 1.2046 1.4620 1.2376 0.2010  0.0828  -0.0795 18   PHE A CD2 
136   C  CE1 . PHE A 18   ? 1.2735 1.5036 1.2937 0.2022  0.0677  -0.0785 18   PHE A CE1 
137   C  CE2 . PHE A 18   ? 1.2186 1.4645 1.2436 0.1976  0.0841  -0.0765 18   PHE A CE2 
138   C  CZ  . PHE A 18   ? 1.2721 1.5046 1.2908 0.1985  0.0763  -0.0760 18   PHE A CZ  
139   N  N   . ALA A 19   ? 0.8447 1.1417 0.9164 0.1943  0.0815  -0.0844 19   ALA A N   
140   C  CA  . ALA A 19   ? 0.7901 1.0955 0.8714 0.1850  0.0872  -0.0829 19   ALA A CA  
141   C  C   . ALA A 19   ? 0.7802 1.0904 0.8727 0.1802  0.0818  -0.0836 19   ALA A C   
142   O  O   . ALA A 19   ? 0.7356 1.0444 0.8321 0.1723  0.0831  -0.0817 19   ALA A O   
143   C  CB  . ALA A 19   ? 0.7317 1.0533 0.8199 0.1847  0.0958  -0.0842 19   ALA A CB  
144   N  N   . LEU A 20   ? 1.0687 1.3840 1.1656 0.1853  0.0759  -0.0863 20   LEU A N   
145   C  CA  . LEU A 20   ? 1.0295 1.3484 1.1358 0.1817  0.0704  -0.0869 20   LEU A CA  
146   C  C   . LEU A 20   ? 1.0495 1.3527 1.1505 0.1782  0.0652  -0.0846 20   LEU A C   
147   O  O   . LEU A 20   ? 0.9910 1.2953 1.0985 0.1711  0.0648  -0.0834 20   LEU A O   
148   C  CB  . LEU A 20   ? 1.0915 1.4159 1.2006 0.1892  0.0648  -0.0900 20   LEU A CB  
149   C  CG  . LEU A 20   ? 1.0141 1.3436 1.1328 0.1868  0.0594  -0.0910 20   LEU A CG  
150   C  CD1 . LEU A 20   ? 0.9338 1.2801 1.0657 0.1801  0.0642  -0.0918 20   LEU A CD1 
151   C  CD2 . LEU A 20   ? 0.8981 1.2295 1.0162 0.1955  0.0537  -0.0937 20   LEU A CD2 
152   N  N   . VAL A 21   ? 0.9066 1.1954 0.9959 0.1832  0.0613  -0.0840 21   VAL A N   
153   C  CA  . VAL A 21   ? 0.8095 1.0840 0.8940 0.1805  0.0561  -0.0820 21   VAL A CA  
154   C  C   . VAL A 21   ? 0.8539 1.1248 0.9375 0.1730  0.0610  -0.0789 21   VAL A C   
155   O  O   . VAL A 21   ? 0.8850 1.1516 0.9718 0.1674  0.0587  -0.0773 21   VAL A O   
156   C  CB  . VAL A 21   ? 0.7871 1.0479 0.8592 0.1874  0.0513  -0.0825 21   VAL A CB  
157   C  CG1 . VAL A 21   ? 0.6994 0.9461 0.7664 0.1842  0.0470  -0.0803 21   VAL A CG1 
158   C  CG2 . VAL A 21   ? 0.9002 1.1624 0.9733 0.1941  0.0456  -0.0854 21   VAL A CG2 
159   N  N   . LEU A 22   ? 0.9569 1.2289 1.0357 0.1730  0.0683  -0.0779 22   LEU A N   
160   C  CA  . LEU A 22   ? 0.8764 1.1446 0.9535 0.1661  0.0739  -0.0749 22   LEU A CA  
161   C  C   . LEU A 22   ? 0.9576 1.2362 1.0472 0.1579  0.0767  -0.0747 22   LEU A C   
162   O  O   . LEU A 22   ? 0.9359 1.2085 1.0260 0.1517  0.0766  -0.0725 22   LEU A O   
163   C  CB  . LEU A 22   ? 0.9691 1.2376 1.0389 0.1680  0.0819  -0.0741 22   LEU A CB  
164   C  CG  . LEU A 22   ? 1.0896 1.3447 1.1445 0.1749  0.0798  -0.0735 22   LEU A CG  
165   C  CD1 . LEU A 22   ? 1.1215 1.3746 1.1683 0.1749  0.0886  -0.0716 22   LEU A CD1 
166   C  CD2 . LEU A 22   ? 1.0789 1.3200 1.1284 0.1736  0.0733  -0.0718 22   LEU A CD2 
167   N  N   . LEU A 23   ? 0.9012 1.1955 1.0009 0.1579  0.0790  -0.0772 23   LEU A N   
168   C  CA  . LEU A 23   ? 0.8465 1.1519 0.9587 0.1502  0.0814  -0.0777 23   LEU A CA  
169   C  C   . LEU A 23   ? 0.8827 1.1839 0.9990 0.1477  0.0740  -0.0775 23   LEU A C   
170   O  O   . LEU A 23   ? 0.8448 1.1460 0.9658 0.1402  0.0753  -0.0762 23   LEU A O   
171   C  CB  . LEU A 23   ? 0.9413 1.2652 1.0637 0.1519  0.0841  -0.0809 23   LEU A CB  
172   C  CG  . LEU A 23   ? 0.9758 1.3070 1.0972 0.1524  0.0931  -0.0811 23   LEU A CG  
173   C  CD1 . LEU A 23   ? 0.9615 1.3120 1.0939 0.1549  0.0946  -0.0848 23   LEU A CD1 
174   C  CD2 . LEU A 23   ? 0.9017 1.2317 1.0238 0.1434  0.1009  -0.0788 23   LEU A CD2 
175   N  N   . VAL A 24   ? 1.2355 1.5327 1.3496 0.1540  0.0664  -0.0788 24   VAL A N   
176   C  CA  . VAL A 24   ? 1.1717 1.4638 1.2888 0.1521  0.0595  -0.0785 24   VAL A CA  
177   C  C   . VAL A 24   ? 1.1417 1.4197 1.2525 0.1477  0.0589  -0.0753 24   VAL A C   
178   O  O   . VAL A 24   ? 1.0904 1.3678 1.2061 0.1415  0.0583  -0.0741 24   VAL A O   
179   C  CB  . VAL A 24   ? 1.2704 1.5589 1.3847 0.1599  0.0521  -0.0804 24   VAL A CB  
180   C  CG1 . VAL A 24   ? 1.1901 1.4715 1.3063 0.1578  0.0454  -0.0797 24   VAL A CG1 
181   C  CG2 . VAL A 24   ? 1.3212 1.6243 1.4424 0.1643  0.0524  -0.0836 24   VAL A CG2 
182   N  N   . VAL A 25   ? 0.9580 1.2246 1.0576 0.1512  0.0589  -0.0739 25   VAL A N   
183   C  CA  . VAL A 25   ? 0.9223 1.1757 1.0153 0.1479  0.0583  -0.0709 25   VAL A CA  
184   C  C   . VAL A 25   ? 0.8674 1.1231 0.9631 0.1401  0.0653  -0.0688 25   VAL A C   
185   O  O   . VAL A 25   ? 0.8818 1.1314 0.9782 0.1350  0.0642  -0.0668 25   VAL A O   
186   C  CB  . VAL A 25   ? 1.0311 1.2733 1.1113 0.1537  0.0576  -0.0701 25   VAL A CB  
187   C  CG1 . VAL A 25   ? 1.0324 1.2631 1.1055 0.1503  0.0590  -0.0669 25   VAL A CG1 
188   C  CG2 . VAL A 25   ? 0.9825 1.2191 1.0597 0.1600  0.0495  -0.0720 25   VAL A CG2 
189   N  N   . GLU A 26   ? 1.1635 1.4278 1.2608 0.1390  0.0727  -0.0692 26   GLU A N   
190   C  CA  . GLU A 26   ? 1.2231 1.4896 1.3231 0.1311  0.0800  -0.0675 26   GLU A CA  
191   C  C   . GLU A 26   ? 1.1883 1.4624 1.2999 0.1246  0.0787  -0.0683 26   GLU A C   
192   O  O   . GLU A 26   ? 1.2276 1.4979 1.3400 0.1177  0.0816  -0.0664 26   GLU A O   
193   C  CB  . GLU A 26   ? 1.2869 1.5626 1.3876 0.1311  0.0883  -0.0683 26   GLU A CB  
194   C  CG  . GLU A 26   ? 1.2016 1.4788 1.3042 0.1229  0.0969  -0.0665 26   GLU A CG  
195   C  CD  . GLU A 26   ? 1.2954 1.5564 1.3858 0.1215  0.0993  -0.0627 26   GLU A CD  
196   O  OE1 . GLU A 26   ? 1.2927 1.5433 1.3722 0.1279  0.0965  -0.0617 26   GLU A OE1 
197   O  OE2 . GLU A 26   ? 1.3524 1.6108 1.4440 0.1141  0.1039  -0.0609 26   GLU A OE2 
198   N  N   . GLY A 27   ? 0.8759 1.1602 0.9960 0.1269  0.0742  -0.0712 27   GLY A N   
199   C  CA  . GLY A 27   ? 0.8000 1.0917 0.9307 0.1214  0.0723  -0.0723 27   GLY A CA  
200   C  C   . GLY A 27   ? 0.6991 0.9791 0.8274 0.1187  0.0675  -0.0702 27   GLY A C   
201   O  O   . GLY A 27   ? 0.6740 0.9537 0.8060 0.1117  0.0696  -0.0691 27   GLY A O   
202   N  N   . ILE A 28   ? 0.9142 1.1844 1.0364 0.1243  0.0610  -0.0696 28   ILE A N   
203   C  CA  . ILE A 28   ? 0.9051 1.1640 1.0248 0.1221  0.0565  -0.0675 28   ILE A CA  
204   C  C   . ILE A 28   ? 0.9899 1.2393 1.1032 0.1176  0.0611  -0.0643 28   ILE A C   
205   O  O   . ILE A 28   ? 1.1239 1.3685 1.2385 0.1125  0.0607  -0.0627 28   ILE A O   
206   C  CB  . ILE A 28   ? 0.9765 1.2266 1.0904 0.1289  0.0493  -0.0678 28   ILE A CB  
207   C  CG1 . ILE A 28   ? 1.2210 1.4783 1.3413 0.1325  0.0441  -0.0705 28   ILE A CG1 
208   C  CG2 . ILE A 28   ? 1.0083 1.2456 1.1180 0.1269  0.0459  -0.0652 28   ILE A CG2 
209   C  CD1 . ILE A 28   ? 1.2279 1.4921 1.3474 0.1391  0.0444  -0.0730 28   ILE A CD1 
210   N  N   . LEU A 29   ? 0.7657 1.0119 0.8714 0.1197  0.0658  -0.0634 29   LEU A N   
211   C  CA  . LEU A 29   ? 0.7872 1.0236 0.8854 0.1161  0.0706  -0.0602 29   LEU A CA  
212   C  C   . LEU A 29   ? 0.6952 0.9366 0.7995 0.1076  0.0765  -0.0596 29   LEU A C   
213   O  O   . LEU A 29   ? 0.6520 0.8854 0.7543 0.1032  0.0771  -0.0573 29   LEU A O   
214   C  CB  . LEU A 29   ? 0.8217 1.0547 0.9104 0.1203  0.0751  -0.0595 29   LEU A CB  
215   C  CG  . LEU A 29   ? 0.8007 1.0206 0.8782 0.1194  0.0787  -0.0560 29   LEU A CG  
216   C  CD1 . LEU A 29   ? 1.1411 1.3541 1.2075 0.1270  0.0776  -0.0558 29   LEU A CD1 
217   C  CD2 . LEU A 29   ? 0.7899 1.0119 0.8677 0.1130  0.0881  -0.0546 29   LEU A CD2 
218   N  N   . ILE A 30   ? 0.6683 0.9230 0.7803 0.1054  0.0810  -0.0618 30   ILE A N   
219   C  CA  . ILE A 30   ? 0.6520 0.9125 0.7706 0.0969  0.0867  -0.0619 30   ILE A CA  
220   C  C   . ILE A 30   ? 0.6447 0.9050 0.7697 0.0928  0.0819  -0.0621 30   ILE A C   
221   O  O   . ILE A 30   ? 0.7053 0.9613 0.8305 0.0861  0.0851  -0.0606 30   ILE A O   
222   C  CB  . ILE A 30   ? 0.6765 0.9535 0.8040 0.0958  0.0912  -0.0650 30   ILE A CB  
223   C  CG1 . ILE A 30   ? 0.7679 1.0440 0.8884 0.0981  0.0982  -0.0642 30   ILE A CG1 
224   C  CG2 . ILE A 30   ? 0.6607 0.9460 0.7978 0.0868  0.0952  -0.0661 30   ILE A CG2 
225   C  CD1 . ILE A 30   ? 0.7915 1.0840 0.9209 0.0961  0.1040  -0.0670 30   ILE A CD1 
226   N  N   . LEU A 31   ? 0.7733 1.0373 0.9028 0.0969  0.0745  -0.0640 31   LEU A N   
227   C  CA  . LEU A 31   ? 0.7388 1.0028 0.8740 0.0937  0.0698  -0.0643 31   LEU A CA  
228   C  C   . LEU A 31   ? 0.6829 0.9317 0.8109 0.0919  0.0684  -0.0609 31   LEU A C   
229   O  O   . LEU A 31   ? 0.6776 0.9243 0.8080 0.0858  0.0696  -0.0600 31   LEU A O   
230   C  CB  . LEU A 31   ? 0.6390 0.9079 0.7784 0.0995  0.0623  -0.0665 31   LEU A CB  
231   C  CG  . LEU A 31   ? 0.6586 0.9303 0.8051 0.0968  0.0576  -0.0675 31   LEU A CG  
232   C  CD1 . LEU A 31   ? 0.6224 0.9064 0.7781 0.0903  0.0616  -0.0696 31   LEU A CD1 
233   C  CD2 . LEU A 31   ? 0.5773 0.8520 0.7259 0.1035  0.0506  -0.0695 31   LEU A CD2 
234   N  N   . GLY A 32   ? 0.6785 0.9169 0.7976 0.0973  0.0657  -0.0591 32   GLY A N   
235   C  CA  . GLY A 32   ? 0.6549 0.8798 0.7675 0.0963  0.0640  -0.0560 32   GLY A CA  
236   C  C   . GLY A 32   ? 0.7488 0.9673 0.8560 0.0912  0.0710  -0.0534 32   GLY A C   
237   O  O   . GLY A 32   ? 0.8076 1.0182 0.9129 0.0876  0.0709  -0.0514 32   GLY A O   
238   N  N   . VAL A 33   ? 0.9517 1.1728 1.0558 0.0910  0.0775  -0.0535 33   VAL A N   
239   C  CA  . VAL A 33   ? 0.8978 1.1119 0.9958 0.0862  0.0850  -0.0509 33   VAL A CA  
240   C  C   . VAL A 33   ? 0.9362 1.1547 1.0417 0.0777  0.0883  -0.0515 33   VAL A C   
241   O  O   . VAL A 33   ? 0.9120 1.1212 1.0128 0.0733  0.0916  -0.0490 33   VAL A O   
242   C  CB  . VAL A 33   ? 0.9653 1.1819 1.0587 0.0878  0.0916  -0.0510 33   VAL A CB  
243   C  CG1 . VAL A 33   ? 0.9950 1.2047 1.0826 0.0821  0.1003  -0.0485 33   VAL A CG1 
244   C  CG2 . VAL A 33   ? 1.0246 1.2345 1.1087 0.0962  0.0884  -0.0502 33   VAL A CG2 
245   N  N   . TYR A 34   ? 0.8018 1.0342 0.9186 0.0756  0.0872  -0.0548 34   TYR A N   
246   C  CA  . TYR A 34   ? 0.7368 0.9744 0.8611 0.0675  0.0899  -0.0559 34   TYR A CA  
247   C  C   . TYR A 34   ? 0.8001 1.0300 0.9243 0.0656  0.0852  -0.0546 34   TYR A C   
248   O  O   . TYR A 34   ? 0.7779 1.0024 0.9010 0.0593  0.0888  -0.0534 34   TYR A O   
249   C  CB  . TYR A 34   ? 0.8024 1.0576 0.9389 0.0665  0.0890  -0.0601 34   TYR A CB  
250   C  CG  . TYR A 34   ? 0.8947 1.1565 1.0395 0.0580  0.0918  -0.0619 34   TYR A CG  
251   C  CD1 . TYR A 34   ? 0.8943 1.1560 1.0386 0.0510  0.1003  -0.0615 34   TYR A CD1 
252   C  CD2 . TYR A 34   ? 0.8334 1.1010 0.9860 0.0569  0.0860  -0.0639 34   TYR A CD2 
253   C  CE1 . TYR A 34   ? 0.7977 1.0653 0.9496 0.0428  0.1028  -0.0635 34   TYR A CE1 
254   C  CE2 . TYR A 34   ? 0.8644 1.1379 1.0241 0.0492  0.0881  -0.0659 34   TYR A CE2 
255   C  CZ  . TYR A 34   ? 0.8041 1.0778 0.9637 0.0420  0.0964  -0.0658 34   TYR A CZ  
256   O  OH  . TYR A 34   ? 0.9145 1.1941 1.0814 0.0339  0.0985  -0.0680 34   TYR A OH  
257   N  N   . PHE A 35   ? 0.9859 1.2146 1.1109 0.0710  0.0773  -0.0549 35   PHE A N   
258   C  CA  . PHE A 35   ? 0.9055 1.1278 1.0311 0.0696  0.0727  -0.0538 35   PHE A CA  
259   C  C   . PHE A 35   ? 0.9344 1.1411 1.0498 0.0703  0.0732  -0.0499 35   PHE A C   
260   O  O   . PHE A 35   ? 1.0014 1.2019 1.1165 0.0694  0.0698  -0.0487 35   PHE A O   
261   C  CB  . PHE A 35   ? 0.9012 1.1275 1.0312 0.0750  0.0646  -0.0554 35   PHE A CB  
262   C  CG  . PHE A 35   ? 0.9263 1.1660 1.0668 0.0732  0.0627  -0.0589 35   PHE A CG  
263   C  CD1 . PHE A 35   ? 0.9401 1.1925 1.0859 0.0736  0.0653  -0.0617 35   PHE A CD1 
264   C  CD2 . PHE A 35   ? 1.0324 1.2721 1.1772 0.0713  0.0585  -0.0594 35   PHE A CD2 
265   C  CE1 . PHE A 35   ? 1.0341 1.2997 1.1897 0.0724  0.0632  -0.0651 35   PHE A CE1 
266   C  CE2 . PHE A 35   ? 0.9571 1.2090 1.1108 0.0702  0.0565  -0.0627 35   PHE A CE2 
267   C  CZ  . PHE A 35   ? 0.9734 1.2385 1.1327 0.0708  0.0587  -0.0657 35   PHE A CZ  
268   N  N   . ARG A 36   ? 0.7313 0.9316 0.8381 0.0722  0.0774  -0.0480 36   ARG A N   
269   C  CA  . ARG A 36   ? 0.7105 0.8964 0.8070 0.0734  0.0782  -0.0444 36   ARG A CA  
270   C  C   . ARG A 36   ? 0.7235 0.9035 0.8132 0.0692  0.0869  -0.0424 36   ARG A C   
271   O  O   . ARG A 36   ? 0.7387 0.9063 0.8185 0.0706  0.0884  -0.0392 36   ARG A O   
272   C  CB  . ARG A 36   ? 0.7537 0.9347 0.8437 0.0814  0.0738  -0.0436 36   ARG A CB  
273   C  CG  . ARG A 36   ? 0.7600 0.9433 0.8549 0.0854  0.0654  -0.0449 36   ARG A CG  
274   C  CD  . ARG A 36   ? 0.7382 0.9214 0.8293 0.0928  0.0617  -0.0457 36   ARG A CD  
275   N  NE  . ARG A 36   ? 0.7031 0.8848 0.7967 0.0964  0.0539  -0.0463 36   ARG A NE  
276   C  CZ  . ARG A 36   ? 0.7513 0.9407 0.8528 0.0973  0.0497  -0.0488 36   ARG A CZ  
277   N  NH1 . ARG A 36   ? 0.6860 0.8862 0.7942 0.0951  0.0520  -0.0511 36   ARG A NH1 
278   N  NH2 . ARG A 36   ? 0.7080 0.8943 0.8106 0.1005  0.0432  -0.0490 36   ARG A NH2 
279   N  N   . SER A 37   ? 0.7028 0.8913 0.7975 0.0641  0.0926  -0.0442 37   SER A N   
280   C  CA  . SER A 37   ? 0.7635 0.9466 0.8520 0.0598  0.1016  -0.0425 37   SER A CA  
281   C  C   . SER A 37   ? 0.7716 0.9451 0.8571 0.0538  0.1044  -0.0405 37   SER A C   
282   O  O   . SER A 37   ? 0.8418 1.0154 0.9320 0.0520  0.0999  -0.0410 37   SER A O   
283   C  CB  . SER A 37   ? 0.7952 0.9916 0.8915 0.0556  0.1069  -0.0455 37   SER A CB  
284   O  OG  . SER A 37   ? 0.7376 0.9422 0.8443 0.0489  0.1067  -0.0480 37   SER A OG  
285   N  N   . ASN A 38   ? 1.0153 1.1798 1.0922 0.0508  0.1123  -0.0382 38   ASN A N   
286   C  CA  . ASN A 38   ? 1.0062 1.1607 1.0791 0.0448  0.1163  -0.0363 38   ASN A CA  
287   C  C   . ASN A 38   ? 1.0210 1.1840 1.1033 0.0356  0.1204  -0.0391 38   ASN A C   
288   O  O   . ASN A 38   ? 0.9434 1.0994 1.0243 0.0301  0.1226  -0.0383 38   ASN A O   
289   C  CB  . ASN A 38   ? 0.9793 1.1193 1.0380 0.0455  0.1233  -0.0325 38   ASN A CB  
290   C  CG  . ASN A 38   ? 1.0519 1.1811 1.1003 0.0539  0.1187  -0.0295 38   ASN A CG  
291   O  OD1 . ASN A 38   ? 1.1215 1.2540 1.1738 0.0587  0.1104  -0.0303 38   ASN A OD1 
292   N  ND2 . ASN A 38   ? 1.0835 1.1996 1.1185 0.0557  0.1241  -0.0261 38   ASN A ND2 
293   N  N   . TYR A 39   ? 0.8731 1.0511 0.9650 0.0340  0.1216  -0.0425 39   TYR A N   
294   C  CA  . TYR A 39   ? 0.8621 1.0505 0.9646 0.0255  0.1244  -0.0459 39   TYR A CA  
295   C  C   . TYR A 39   ? 0.8685 1.0660 0.9814 0.0257  0.1162  -0.0487 39   TYR A C   
296   O  O   . TYR A 39   ? 0.8525 1.0514 0.9703 0.0191  0.1166  -0.0502 39   TYR A O   
297   C  CB  . TYR A 39   ? 0.8678 1.0693 0.9765 0.0237  0.1296  -0.0485 39   TYR A CB  
298   C  CG  . TYR A 39   ? 0.8486 1.0662 0.9716 0.0170  0.1297  -0.0532 39   TYR A CG  
299   C  CD1 . TYR A 39   ? 0.8622 1.0789 0.9876 0.0073  0.1359  -0.0543 39   TYR A CD1 
300   C  CD2 . TYR A 39   ? 0.8740 1.1077 1.0079 0.0206  0.1236  -0.0568 39   TYR A CD2 
301   C  CE1 . TYR A 39   ? 0.9780 1.2103 1.1170 0.0012  0.1356  -0.0590 39   TYR A CE1 
302   C  CE2 . TYR A 39   ? 0.9663 1.2154 1.1133 0.0150  0.1233  -0.0613 39   TYR A CE2 
303   C  CZ  . TYR A 39   ? 1.0620 1.3108 1.2118 0.0053  0.1292  -0.0625 39   TYR A CZ  
304   O  OH  . TYR A 39   ? 1.0964 1.3613 1.2596 -0.0003 0.1285  -0.0673 39   TYR A OH  
305   N  N   . PHE A 40   ? 0.9834 1.1865 1.0992 0.0331  0.1088  -0.0494 40   PHE A N   
306   C  CA  . PHE A 40   ? 1.0006 1.2111 1.1250 0.0341  0.1010  -0.0518 40   PHE A CA  
307   C  C   . PHE A 40   ? 0.9695 1.1678 1.0891 0.0335  0.0978  -0.0494 40   PHE A C   
308   O  O   . PHE A 40   ? 0.9502 1.1517 1.0758 0.0297  0.0953  -0.0511 40   PHE A O   
309   C  CB  . PHE A 40   ? 0.9325 1.1499 1.0596 0.0424  0.0945  -0.0528 40   PHE A CB  
310   C  CG  . PHE A 40   ? 0.9793 1.2052 1.1151 0.0438  0.0870  -0.0554 40   PHE A CG  
311   C  CD1 . PHE A 40   ? 1.0087 1.2478 1.1551 0.0390  0.0872  -0.0592 40   PHE A CD1 
312   C  CD2 . PHE A 40   ? 0.9937 1.2143 1.1272 0.0498  0.0798  -0.0541 40   PHE A CD2 
313   C  CE1 . PHE A 40   ? 0.9985 1.2448 1.1520 0.0408  0.0803  -0.0615 40   PHE A CE1 
314   C  CE2 . PHE A 40   ? 0.9355 1.1629 1.0763 0.0513  0.0734  -0.0563 40   PHE A CE2 
315   C  CZ  . PHE A 40   ? 0.9467 1.1866 1.0970 0.0470  0.0735  -0.0599 40   PHE A CZ  
316   N  N   . ARG A 41   ? 0.7236 0.9080 0.8324 0.0376  0.0978  -0.0455 41   ARG A N   
317   C  CA  . ARG A 41   ? 0.6639 0.8365 0.7676 0.0378  0.0951  -0.0430 41   ARG A CA  
318   C  C   . ARG A 41   ? 0.7471 0.9087 0.8443 0.0315  0.1019  -0.0410 41   ARG A C   
319   O  O   . ARG A 41   ? 0.8419 0.9932 0.9344 0.0313  0.1004  -0.0389 41   ARG A O   
320   C  CB  . ARG A 41   ? 0.5845 0.7485 0.6805 0.0459  0.0910  -0.0401 41   ARG A CB  
321   C  CG  . ARG A 41   ? 0.6186 0.7914 0.7199 0.0523  0.0841  -0.0419 41   ARG A CG  
322   C  CD  . ARG A 41   ? 0.7652 0.9468 0.8766 0.0510  0.0786  -0.0446 41   ARG A CD  
323   N  NE  . ARG A 41   ? 0.7347 0.9080 0.8445 0.0500  0.0758  -0.0429 41   ARG A NE  
324   C  CZ  . ARG A 41   ? 0.6780 0.8510 0.7902 0.0539  0.0690  -0.0428 41   ARG A CZ  
325   N  NH1 . ARG A 41   ? 0.7229 0.9027 0.8389 0.0591  0.0641  -0.0444 41   ARG A NH1 
326   N  NH2 . ARG A 41   ? 0.7227 0.8880 0.8331 0.0525  0.0675  -0.0412 41   ARG A NH2 
327   N  N   . GLN A 42   ? 0.8860 1.0493 0.9824 0.0263  0.1097  -0.0417 42   GLN A N   
328   C  CA  . GLN A 42   ? 1.0127 1.1650 1.1025 0.0197  0.1171  -0.0400 42   GLN A CA  
329   C  C   . GLN A 42   ? 0.9373 1.0719 1.0131 0.0241  0.1181  -0.0352 42   GLN A C   
330   O  O   . GLN A 42   ? 0.9099 1.0336 0.9806 0.0217  0.1189  -0.0334 42   GLN A O   
331   C  CB  . GLN A 42   ? 0.9386 1.0929 1.0346 0.0128  0.1163  -0.0421 42   GLN A CB  
332   C  CG  . GLN A 42   ? 0.9418 1.1128 1.0506 0.0071  0.1169  -0.0470 42   GLN A CG  
333   C  CD  . GLN A 42   ? 1.0339 1.2080 1.1426 0.0019  0.1258  -0.0479 42   GLN A CD  
334   O  OE1 . GLN A 42   ? 0.9930 1.1816 1.1102 0.0018  0.1262  -0.0509 42   GLN A OE1 
335   N  NE2 . GLN A 42   ? 0.9952 1.1554 1.0942 -0.0024 0.1332  -0.0452 42   GLN A NE2 
336   N  N   . VAL A 43   ? 0.8594 0.9915 0.9289 0.0308  0.1179  -0.0333 43   VAL A N   
337   C  CA  . VAL A 43   ? 0.8806 0.9974 0.9369 0.0361  0.1183  -0.0291 43   VAL A CA  
338   C  C   . VAL A 43   ? 0.8710 0.9789 0.9171 0.0339  0.1278  -0.0270 43   VAL A C   
339   O  O   . VAL A 43   ? 0.9193 1.0347 0.9680 0.0322  0.1321  -0.0285 43   VAL A O   
340   C  CB  . VAL A 43   ? 0.9016 1.0206 0.9567 0.0455  0.1114  -0.0285 43   VAL A CB  
341   C  CG1 . VAL A 43   ? 0.8167 0.9209 0.8580 0.0513  0.1121  -0.0244 43   VAL A CG1 
342   C  CG2 . VAL A 43   ? 0.8518 0.9776 0.9160 0.0475  0.1026  -0.0302 43   VAL A CG2 
343   N  N   . ASN A 44   ? 0.8072 0.8990 0.8414 0.0340  0.1312  -0.0234 44   ASN A N   
344   C  CA  . ASN A 44   ? 0.8559 0.9360 0.8782 0.0320  0.1406  -0.0207 44   ASN A CA  
345   C  C   . ASN A 44   ? 0.8699 0.9542 0.8972 0.0219  0.1485  -0.0230 44   ASN A C   
346   O  O   . ASN A 44   ? 0.9016 0.9808 0.9221 0.0196  0.1568  -0.0218 44   ASN A O   
347   C  CB  . ASN A 44   ? 0.9020 0.9814 0.9172 0.0390  0.1416  -0.0193 44   ASN A CB  
348   C  CG  . ASN A 44   ? 0.9685 1.0403 0.9755 0.0486  0.1353  -0.0167 44   ASN A CG  
349   O  OD1 . ASN A 44   ? 0.8857 0.9494 0.8894 0.0499  0.1322  -0.0150 44   ASN A OD1 
350   N  ND2 . ASN A 44   ? 1.0147 1.0892 1.0185 0.0555  0.1334  -0.0166 44   ASN A ND2 
351   N  N   . VAL A 45   ? 1.1456 1.2391 1.1847 0.0158  0.1460  -0.0263 45   VAL A N   
352   C  CA  . VAL A 45   ? 1.1479 1.2463 1.1931 0.0056  0.1527  -0.0290 45   VAL A CA  
353   C  C   . VAL A 45   ? 1.1952 1.2806 1.2350 0.0001  0.1555  -0.0277 45   VAL A C   
354   O  O   . VAL A 45   ? 1.2647 1.3487 1.3068 0.0013  0.1493  -0.0278 45   VAL A O   
355   C  CB  . VAL A 45   ? 1.0848 1.2036 1.1473 0.0026  0.1479  -0.0341 45   VAL A CB  
356   C  CG1 . VAL A 45   ? 1.0976 1.2225 1.1670 -0.0081 0.1548  -0.0373 45   VAL A CG1 
357   C  CG2 . VAL A 45   ? 1.0154 1.1461 1.0824 0.0091  0.1446  -0.0352 45   VAL A CG2 
358   N  N   . ALA A 46   ? 0.8604 0.9354 0.8924 -0.0060 0.1652  -0.0264 46   ALA A N   
359   C  CA  . ALA A 46   ? 0.8883 0.9492 0.9136 -0.0116 0.1690  -0.0251 46   ALA A CA  
360   C  C   . ALA A 46   ? 0.9779 1.0496 1.0162 -0.0214 0.1691  -0.0300 46   ALA A C   
361   O  O   . ALA A 46   ? 1.0031 1.0793 1.0454 -0.0295 0.1761  -0.0323 46   ALA A O   
362   C  CB  . ALA A 46   ? 0.8735 0.9175 0.8840 -0.0140 0.1796  -0.0217 46   ALA A CB  
363   N  N   . ILE A 47   ? 0.8895 0.9657 0.9344 -0.0206 0.1612  -0.0316 47   ILE A N   
364   C  CA  . ILE A 47   ? 0.9720 1.0587 1.0290 -0.0290 0.1601  -0.0364 47   ILE A CA  
365   C  C   . ILE A 47   ? 1.0059 1.0789 1.0560 -0.0379 0.1678  -0.0361 47   ILE A C   
366   O  O   . ILE A 47   ? 0.8785 0.9340 0.9164 -0.0360 0.1691  -0.0325 47   ILE A O   
367   C  CB  . ILE A 47   ? 1.0502 1.1435 1.1143 -0.0252 0.1499  -0.0377 47   ILE A CB  
368   C  CG1 . ILE A 47   ? 0.8977 1.0057 0.9700 -0.0175 0.1426  -0.0387 47   ILE A CG1 
369   C  CG2 . ILE A 47   ? 1.1295 1.2307 1.2036 -0.0337 0.1490  -0.0424 47   ILE A CG2 
370   C  CD1 . ILE A 47   ? 0.8527 0.9523 0.9164 -0.0072 0.1381  -0.0345 47   ILE A CD1 
371   N  N   . GLU A 48   ? 1.2006 1.2818 1.2587 -0.0476 0.1731  -0.0401 48   GLU A N   
372   C  CA  . GLU A 48   ? 1.2669 1.3359 1.3193 -0.0572 0.1809  -0.0405 48   GLU A CA  
373   C  C   . GLU A 48   ? 1.2456 1.3124 1.3007 -0.0603 0.1759  -0.0424 48   GLU A C   
374   O  O   . GLU A 48   ? 1.1613 1.2439 1.2294 -0.0608 0.1688  -0.0465 48   GLU A O   
375   C  CB  . GLU A 48   ? 1.2866 1.3666 1.3480 -0.0671 0.1880  -0.0446 48   GLU A CB  
376   C  CG  . GLU A 48   ? 1.3894 1.4561 1.4447 -0.0779 0.1971  -0.0452 48   GLU A CG  
377   C  CD  . GLU A 48   ? 1.5018 1.5799 1.5665 -0.0878 0.2046  -0.0492 48   GLU A CD  
378   O  OE1 . GLU A 48   ? 1.5141 1.6110 1.5902 -0.0859 0.2025  -0.0516 48   GLU A OE1 
379   O  OE2 . GLU A 48   ? 1.5223 1.5903 1.5828 -0.0975 0.2128  -0.0501 48   GLU A OE2 
380   N  N   . GLN A 49   ? 1.0017 1.0483 1.0437 -0.0619 0.1797  -0.0395 49   GLN A N   
381   C  CA  . GLN A 49   ? 0.9033 0.9443 0.9450 -0.0645 0.1760  -0.0407 49   GLN A CA  
382   C  C   . GLN A 49   ? 0.9948 1.0328 1.0382 -0.0771 0.1826  -0.0444 49   GLN A C   
383   O  O   . GLN A 49   ? 1.1063 1.1390 1.1457 -0.0831 0.1918  -0.0443 49   GLN A O   
384   C  CB  . GLN A 49   ? 0.9645 0.9847 0.9903 -0.0577 0.1757  -0.0352 49   GLN A CB  
385   C  CG  . GLN A 49   ? 0.8552 0.8780 0.8794 -0.0455 0.1686  -0.0318 49   GLN A CG  
386   C  CD  . GLN A 49   ? 0.7679 0.8061 0.8047 -0.0421 0.1582  -0.0346 49   GLN A CD  
387   O  OE1 . GLN A 49   ? 0.8511 0.8934 0.8943 -0.0474 0.1557  -0.0380 49   GLN A OE1 
388   N  NE2 . GLN A 49   ? 0.8108 0.8570 0.8507 -0.0332 0.1523  -0.0332 49   GLN A NE2 
389   N  N   . PRO A 50   ? 1.0258 1.0669 1.0749 -0.0814 0.1782  -0.0480 50   PRO A N   
390   C  CA  . PRO A 50   ? 0.9979 1.0374 1.0497 -0.0939 0.1839  -0.0523 50   PRO A CA  
391   C  C   . PRO A 50   ? 1.0742 1.0889 1.1094 -0.0981 0.1929  -0.0490 50   PRO A C   
392   O  O   . PRO A 50   ? 1.1335 1.1452 1.1691 -0.1087 0.2007  -0.0517 50   PRO A O   
393   C  CB  . PRO A 50   ? 0.9317 0.9795 0.9920 -0.0952 0.1756  -0.0564 50   PRO A CB  
394   C  CG  . PRO A 50   ? 0.9857 1.0297 1.0413 -0.0836 0.1678  -0.0523 50   PRO A CG  
395   C  CD  . PRO A 50   ? 1.0037 1.0522 1.0586 -0.0755 0.1677  -0.0489 50   PRO A CD  
396   N  N   . VAL A 51   ? 1.2437 1.2407 1.2645 -0.0901 0.1923  -0.0434 51   VAL A N   
397   C  CA  . VAL A 51   ? 1.2483 1.2205 1.2520 -0.0929 0.2005  -0.0400 51   VAL A CA  
398   C  C   . VAL A 51   ? 1.3206 1.2801 1.3111 -0.0872 0.2068  -0.0343 51   VAL A C   
399   O  O   . VAL A 51   ? 1.3447 1.2826 1.3196 -0.0889 0.2144  -0.0310 51   VAL A O   
400   C  CB  . VAL A 51   ? 1.3098 1.2689 1.3052 -0.0888 0.1959  -0.0381 51   VAL A CB  
401   C  CG1 . VAL A 51   ? 1.4209 1.3905 1.4276 -0.0950 0.1905  -0.0439 51   VAL A CG1 
402   C  CG2 . VAL A 51   ? 1.3718 1.3318 1.3644 -0.0754 0.1885  -0.0338 51   VAL A CG2 
403   N  N   . ALA A 52   ? 0.8955 0.8670 0.8909 -0.0802 0.2039  -0.0330 52   ALA A N   
404   C  CA  . ALA A 52   ? 0.9130 0.8743 0.8964 -0.0741 0.2092  -0.0279 52   ALA A CA  
405   C  C   . ALA A 52   ? 0.8362 0.7758 0.8019 -0.0659 0.2092  -0.0221 52   ALA A C   
406   O  O   . ALA A 52   ? 0.7671 0.6864 0.7174 -0.0676 0.2176  -0.0188 52   ALA A O   
407   C  CB  . ALA A 52   ? 0.7982 0.7540 0.7781 -0.0832 0.2209  -0.0285 52   ALA A CB  
408   N  N   . PHE A 53   ? 1.2614 1.2059 1.2296 -0.0568 0.1996  -0.0209 53   PHE A N   
409   C  CA  . PHE A 53   ? 1.1802 1.1077 1.1339 -0.0479 0.1981  -0.0157 53   PHE A CA  
410   C  C   . PHE A 53   ? 1.1580 1.0832 1.1043 -0.0378 0.1979  -0.0113 53   PHE A C   
411   O  O   . PHE A 53   ? 1.0979 1.0396 1.0542 -0.0336 0.1926  -0.0124 53   PHE A O   
412   C  CB  . PHE A 53   ? 1.1445 1.0782 1.1048 -0.0435 0.1881  -0.0167 53   PHE A CB  
413   C  CG  . PHE A 53   ? 1.1202 1.0383 1.0672 -0.0341 0.1861  -0.0117 53   PHE A CG  
414   C  CD1 . PHE A 53   ? 1.0909 0.9883 1.0240 -0.0361 0.1914  -0.0095 53   PHE A CD1 
415   C  CD2 . PHE A 53   ? 1.1313 1.0555 1.0795 -0.0232 0.1789  -0.0092 53   PHE A CD2 
416   C  CE1 . PHE A 53   ? 1.1137 0.9975 1.0347 -0.0270 0.1895  -0.0050 53   PHE A CE1 
417   C  CE2 . PHE A 53   ? 1.1411 1.0523 1.0780 -0.0145 0.1770  -0.0049 53   PHE A CE2 
418   C  CZ  . PHE A 53   ? 1.1088 1.0000 1.0321 -0.0162 0.1823  -0.0027 53   PHE A CZ  
419   N  N   . SER A 54   ? 1.0712 0.9756 0.9995 -0.0336 0.2035  -0.0064 54   SER A N   
420   C  CA  . SER A 54   ? 1.1326 1.0321 1.0512 -0.0238 0.2040  -0.0020 54   SER A CA  
421   C  C   . SER A 54   ? 1.0701 0.9612 0.9805 -0.0130 0.1979  0.0017  54   SER A C   
422   O  O   . SER A 54   ? 1.0452 0.9179 0.9425 -0.0121 0.2013  0.0044  54   SER A O   
423   C  CB  . SER A 54   ? 1.2619 1.1442 1.1653 -0.0268 0.2157  0.0008  54   SER A CB  
424   O  OG  . SER A 54   ? 1.1924 1.0637 1.0815 -0.0159 0.2161  0.0059  54   SER A OG  
425   N  N   . HIS A 55   ? 0.8960 0.8007 0.8143 -0.0048 0.1890  0.0017  55   HIS A N   
426   C  CA  . HIS A 55   ? 0.9303 0.8286 0.8418 0.0059  0.1831  0.0051  55   HIS A CA  
427   C  C   . HIS A 55   ? 0.9184 0.7995 0.8113 0.0133  0.1881  0.0103  55   HIS A C   
428   O  O   . HIS A 55   ? 0.8723 0.7413 0.7548 0.0202  0.1865  0.0136  55   HIS A O   
429   C  CB  . HIS A 55   ? 0.9407 0.8579 0.8654 0.0123  0.1727  0.0036  55   HIS A CB  
430   C  CG  . HIS A 55   ? 0.8433 0.7722 0.7818 0.0094  0.1658  0.0003  55   HIS A CG  
431   N  ND1 . HIS A 55   ? 0.8486 0.7916 0.8012 0.0009  0.1650  -0.0045 55   HIS A ND1 
432   C  CD2 . HIS A 55   ? 0.9968 0.9253 0.9369 0.0141  0.1593  0.0010  55   HIS A CD2 
433   C  CE1 . HIS A 55   ? 1.0081 0.9583 0.9697 0.0008  0.1583  -0.0065 55   HIS A CE1 
434   N  NE2 . HIS A 55   ? 0.9859 0.9274 0.9402 0.0085  0.1550  -0.0031 55   HIS A NE2 
435   N  N   . GLN A 56   ? 1.1777 1.0576 1.0660 0.0122  0.1941  0.0109  56   GLN A N   
436   C  CA  . GLN A 56   ? 1.1867 1.0499 1.0564 0.0195  0.1991  0.0158  56   GLN A CA  
437   C  C   . GLN A 56   ? 1.1545 0.9944 1.0078 0.0169  0.2071  0.0187  56   GLN A C   
438   O  O   . GLN A 56   ? 1.0877 0.9122 0.9253 0.0254  0.2081  0.0230  56   GLN A O   
439   C  CB  . GLN A 56   ? 1.0551 0.9218 0.9236 0.0180  0.2046  0.0157  56   GLN A CB  
440   C  CG  . GLN A 56   ? 1.1397 0.9909 0.9892 0.0268  0.2088  0.0207  56   GLN A CG  
441   C  CD  . GLN A 56   ? 1.2767 1.1302 1.1241 0.0246  0.2154  0.0206  56   GLN A CD  
442   O  OE1 . GLN A 56   ? 1.2356 1.0882 1.0852 0.0143  0.2234  0.0189  56   GLN A OE1 
443   N  NE2 . GLN A 56   ? 1.3753 1.2321 1.2186 0.0342  0.2120  0.0223  56   GLN A NE2 
444   N  N   . LEU A 57   ? 0.9936 0.8307 0.8502 0.0053  0.2128  0.0161  57   LEU A N   
445   C  CA  . LEU A 57   ? 1.0034 0.8176 0.8443 0.0019  0.2209  0.0184  57   LEU A CA  
446   C  C   . LEU A 57   ? 1.0775 0.8854 0.9159 0.0062  0.2155  0.0194  57   LEU A C   
447   O  O   . LEU A 57   ? 1.1236 0.9112 0.9449 0.0105  0.2195  0.0233  57   LEU A O   
448   C  CB  . LEU A 57   ? 0.9574 0.7713 0.8035 -0.0124 0.2285  0.0148  57   LEU A CB  
449   C  CG  . LEU A 57   ? 0.9287 0.7186 0.7592 -0.0180 0.2378  0.0166  57   LEU A CG  
450   C  CD1 . LEU A 57   ? 1.0200 0.7883 0.8284 -0.0108 0.2449  0.0223  57   LEU A CD1 
451   C  CD2 . LEU A 57   ? 0.8944 0.6868 0.7321 -0.0327 0.2451  0.0124  57   LEU A CD2 
452   N  N   . HIS A 58   ? 0.9135 0.7383 0.7682 0.0055  0.2067  0.0161  58   HIS A N   
453   C  CA  . HIS A 58   ? 0.8494 0.6691 0.7031 0.0082  0.2021  0.0165  58   HIS A CA  
454   C  C   . HIS A 58   ? 0.8955 0.7161 0.7458 0.0214  0.1946  0.0198  58   HIS A C   
455   O  O   . HIS A 58   ? 0.9898 0.8014 0.8344 0.0255  0.1926  0.0214  58   HIS A O   
456   C  CB  . HIS A 58   ? 0.8803 0.7164 0.7522 0.0007  0.1966  0.0114  58   HIS A CB  
457   C  CG  . HIS A 58   ? 0.9298 0.7622 0.8037 -0.0124 0.2035  0.0081  58   HIS A CG  
458   N  ND1 . HIS A 58   ? 0.9252 0.7661 0.8060 -0.0206 0.2080  0.0052  58   HIS A ND1 
459   C  CD2 . HIS A 58   ? 1.0305 0.8517 0.9002 -0.0188 0.2065  0.0069  58   HIS A CD2 
460   C  CE1 . HIS A 58   ? 1.0062 0.8419 0.8878 -0.0317 0.2135  0.0023  58   HIS A CE1 
461   N  NE2 . HIS A 58   ? 0.9727 0.7961 0.8473 -0.0309 0.2126  0.0032  58   HIS A NE2 
462   N  N   . VAL A 59   ? 1.2739 1.1049 1.1276 0.0283  0.1905  0.0205  59   VAL A N   
463   C  CA  . VAL A 59   ? 1.2486 1.0822 1.1004 0.0406  0.1831  0.0230  59   VAL A CA  
464   C  C   . VAL A 59   ? 1.3752 1.1943 1.2090 0.0492  0.1871  0.0276  59   VAL A C   
465   O  O   . VAL A 59   ? 1.4557 1.2639 1.2785 0.0577  0.1857  0.0310  59   VAL A O   
466   C  CB  . VAL A 59   ? 1.2302 1.0871 1.0998 0.0429  0.1738  0.0201  59   VAL A CB  
467   C  CG1 . VAL A 59   ? 1.2723 1.1320 1.1406 0.0549  0.1661  0.0224  59   VAL A CG1 
468   C  CG2 . VAL A 59   ? 1.2331 1.1035 1.1194 0.0350  0.1698  0.0157  59   VAL A CG2 
469   N  N   . ASN A 60   ? 1.0878 0.9069 0.9182 0.0473  0.1922  0.0278  60   ASN A N   
470   C  CA  . ASN A 60   ? 1.0772 0.8833 0.8903 0.0561  0.1958  0.0321  60   ASN A CA  
471   C  C   . ASN A 60   ? 1.1532 0.9345 0.9466 0.0538  0.2065  0.0354  60   ASN A C   
472   O  O   . ASN A 60   ? 1.2860 1.0525 1.0622 0.0629  0.2088  0.0397  60   ASN A O   
473   C  CB  . ASN A 60   ? 1.1340 0.9501 0.9507 0.0561  0.1966  0.0312  60   ASN A CB  
474   C  CG  . ASN A 60   ? 1.0460 0.8817 0.8757 0.0628  0.1859  0.0294  60   ASN A CG  
475   O  OD1 . ASN A 60   ? 1.0768 0.9141 0.9065 0.0714  0.1787  0.0306  60   ASN A OD1 
476   N  ND2 . ASN A 60   ? 0.9296 0.7802 0.7705 0.0591  0.1851  0.0265  60   ASN A ND2 
477   N  N   . VAL A 61   ? 1.1198 0.8958 0.9149 0.0421  0.2131  0.0335  61   VAL A N   
478   C  CA  . VAL A 61   ? 1.1996 0.9514 0.9761 0.0388  0.2240  0.0363  61   VAL A CA  
479   C  C   . VAL A 61   ? 1.1567 0.8969 0.9284 0.0381  0.2238  0.0369  61   VAL A C   
480   O  O   . VAL A 61   ? 1.2273 0.9487 0.9813 0.0456  0.2263  0.0411  61   VAL A O   
481   C  CB  . VAL A 61   ? 1.1020 0.8537 0.8818 0.0258  0.2329  0.0338  61   VAL A CB  
482   C  CG1 . VAL A 61   ? 1.2376 0.9632 0.9982 0.0214  0.2444  0.0365  61   VAL A CG1 
483   C  CG2 . VAL A 61   ? 1.1846 0.9461 0.9670 0.0273  0.2340  0.0337  61   VAL A CG2 
484   N  N   . VAL A 62   ? 0.8982 0.6490 0.6849 0.0295  0.2207  0.0327  62   VAL A N   
485   C  CA  . VAL A 62   ? 0.9549 0.6951 0.7375 0.0283  0.2205  0.0329  62   VAL A CA  
486   C  C   . VAL A 62   ? 0.9834 0.7275 0.7667 0.0403  0.2114  0.0348  62   VAL A C   
487   O  O   . VAL A 62   ? 1.0346 0.7626 0.8047 0.0457  0.2128  0.0378  62   VAL A O   
488   C  CB  . VAL A 62   ? 0.8939 0.6446 0.6921 0.0158  0.2198  0.0276  62   VAL A CB  
489   C  CG1 . VAL A 62   ? 0.8816 0.6213 0.6752 0.0149  0.2193  0.0277  62   VAL A CG1 
490   C  CG2 . VAL A 62   ? 0.7839 0.5306 0.5814 0.0038  0.2292  0.0256  62   VAL A CG2 
491   N  N   . GLY A 63   ? 0.7668 0.5321 0.5652 0.0445  0.2022  0.0331  63   GLY A N   
492   C  CA  . GLY A 63   ? 0.8099 0.5805 0.6101 0.0558  0.1937  0.0347  63   GLY A CA  
493   C  C   . GLY A 63   ? 0.7110 0.4911 0.5240 0.0536  0.1872  0.0321  63   GLY A C   
494   O  O   . GLY A 63   ? 0.6304 0.4041 0.4381 0.0605  0.1845  0.0343  63   GLY A O   
495   N  N   . ILE A 64   ? 1.4838 1.2793 1.3134 0.0445  0.1849  0.0276  64   ILE A N   
496   C  CA  . ILE A 64   ? 1.4124 1.2178 1.2546 0.0419  0.1788  0.0249  64   ILE A CA  
497   C  C   . ILE A 64   ? 1.3539 1.1789 1.2101 0.0488  0.1687  0.0240  64   ILE A C   
498   O  O   . ILE A 64   ? 1.4463 1.2840 1.3101 0.0492  0.1663  0.0228  64   ILE A O   
499   C  CB  . ILE A 64   ? 1.3009 1.1129 1.1537 0.0288  0.1811  0.0202  64   ILE A CB  
500   C  CG1 . ILE A 64   ? 1.3528 1.1459 1.1923 0.0211  0.1918  0.0208  64   ILE A CG1 
501   C  CG2 . ILE A 64   ? 1.3822 1.2013 1.2453 0.0265  0.1755  0.0177  64   ILE A CG2 
502   C  CD1 . ILE A 64   ? 1.3773 1.1787 1.2274 0.0081  0.1948  0.0160  64   ILE A CD1 
503   N  N   . ASP A 65   ? 0.9971 0.8242 0.8563 0.0540  0.1630  0.0246  65   ASP A N   
504   C  CA  . ASP A 65   ? 1.0044 0.8498 0.8775 0.0596  0.1536  0.0235  65   ASP A CA  
505   C  C   . ASP A 65   ? 1.0057 0.8689 0.8968 0.0516  0.1498  0.0188  65   ASP A C   
506   O  O   . ASP A 65   ? 1.0522 0.9138 0.9460 0.0424  0.1530  0.0163  65   ASP A O   
507   C  CB  . ASP A 65   ? 1.0143 0.8568 0.8860 0.0668  0.1493  0.0253  65   ASP A CB  
508   C  CG  . ASP A 65   ? 0.9876 0.8476 0.8724 0.0733  0.1401  0.0246  65   ASP A CG  
509   O  OD1 . ASP A 65   ? 1.0306 0.8935 0.9130 0.0809  0.1376  0.0262  65   ASP A OD1 
510   O  OD2 . ASP A 65   ? 0.9695 0.8399 0.8666 0.0707  0.1353  0.0223  65   ASP A OD2 
511   N  N   . CYS A 66   ? 0.9680 0.8482 0.8712 0.0554  0.1427  0.0175  66   CYS A N   
512   C  CA  . CYS A 66   ? 0.9413 0.8389 0.8612 0.0490  0.1385  0.0132  66   CYS A CA  
513   C  C   . CYS A 66   ? 1.0017 0.9025 0.9290 0.0464  0.1351  0.0115  66   CYS A C   
514   O  O   . CYS A 66   ? 0.9501 0.8581 0.8864 0.0384  0.1348  0.0080  66   CYS A O   
515   C  CB  . CYS A 66   ? 0.9494 0.8628 0.8792 0.0544  0.1318  0.0124  66   CYS A CB  
516   S  SG  . CYS A 66   ? 0.9628 0.8725 0.8831 0.0593  0.1350  0.0146  66   CYS A SG  
517   N  N   . ARG A 67   ? 1.0563 0.9518 0.9797 0.0533  0.1323  0.0140  67   ARG A N   
518   C  CA  . ARG A 67   ? 0.9221 0.8197 0.8514 0.0516  0.1293  0.0127  67   ARG A CA  
519   C  C   . ARG A 67   ? 0.9745 0.8584 0.8958 0.0446  0.1355  0.0122  67   ARG A C   
520   O  O   . ARG A 67   ? 0.9739 0.8600 0.9005 0.0414  0.1335  0.0104  67   ARG A O   
521   C  CB  . ARG A 67   ? 0.8888 0.7851 0.8164 0.0612  0.1251  0.0155  67   ARG A CB  
522   C  CG  . ARG A 67   ? 0.8923 0.8046 0.8313 0.0669  0.1177  0.0150  67   ARG A CG  
523   C  CD  . ARG A 67   ? 1.1903 1.1001 1.1259 0.0768  0.1145  0.0181  67   ARG A CD  
524   N  NE  . ARG A 67   ? 1.1850 1.0826 1.1063 0.0826  0.1183  0.0214  67   ARG A NE  
525   C  CZ  . ARG A 67   ? 1.2037 1.0986 1.1201 0.0920  0.1161  0.0242  67   ARG A CZ  
526   N  NH1 . ARG A 67   ? 1.2880 1.1918 1.2134 0.0964  0.1102  0.0240  67   ARG A NH1 
527   N  NH2 . ARG A 67   ? 1.0805 0.9636 0.9828 0.0973  0.1198  0.0271  67   ARG A NH2 
528   N  N   . TYR A 68   ? 1.0078 0.8773 0.9162 0.0422  0.1430  0.0137  68   TYR A N   
529   C  CA  . TYR A 68   ? 0.9198 0.7766 0.8212 0.0341  0.1492  0.0125  68   TYR A CA  
530   C  C   . TYR A 68   ? 0.8687 0.7368 0.7819 0.0236  0.1489  0.0076  68   TYR A C   
531   O  O   . TYR A 68   ? 0.9922 0.8543 0.9041 0.0165  0.1516  0.0055  68   TYR A O   
532   C  CB  . TYR A 68   ? 0.9319 0.7706 0.8167 0.0337  0.1577  0.0153  68   TYR A CB  
533   C  CG  . TYR A 68   ? 0.9987 0.8210 0.8736 0.0262  0.1648  0.0146  68   TYR A CG  
534   C  CD1 . TYR A 68   ? 1.0532 0.8590 0.9157 0.0302  0.1670  0.0174  68   TYR A CD1 
535   C  CD2 . TYR A 68   ? 0.9701 0.7932 0.8480 0.0150  0.1693  0.0112  68   TYR A CD2 
536   C  CE1 . TYR A 68   ? 1.0544 0.8441 0.9072 0.0233  0.1735  0.0166  68   TYR A CE1 
537   C  CE2 . TYR A 68   ? 1.0407 0.8485 0.9097 0.0076  0.1757  0.0102  68   TYR A CE2 
538   C  CZ  . TYR A 68   ? 1.0519 0.8426 0.9080 0.0118  0.1778  0.0130  68   TYR A CZ  
539   O  OH  . TYR A 68   ? 1.0626 0.8373 0.9094 0.0043  0.1842  0.0119  68   TYR A OH  
540   N  N   . CYS A 69   ? 1.0093 0.8938 0.9342 0.0227  0.1455  0.0056  69   CYS A N   
541   C  CA  . CYS A 69   ? 1.0475 0.9441 0.9839 0.0134  0.1451  0.0008  69   CYS A CA  
542   C  C   . CYS A 69   ? 1.0263 0.9422 0.9788 0.0150  0.1366  -0.0017 69   CYS A C   
543   O  O   . CYS A 69   ? 0.9813 0.9039 0.9419 0.0092  0.1345  -0.0053 69   CYS A O   
544   C  CB  . CYS A 69   ? 1.1160 1.0143 1.0513 0.0099  0.1499  0.0004  69   CYS A CB  
545   S  SG  . CYS A 69   ? 1.1365 1.0127 1.0549 0.0039  0.1612  0.0019  69   CYS A SG  
546   N  N   . HIS A 70   ? 0.7703 0.6948 0.7271 0.0227  0.1316  -0.0001 70   HIS A N   
547   C  CA  . HIS A 70   ? 0.7798 0.7209 0.7505 0.0251  0.1236  -0.0021 70   HIS A CA  
548   C  C   . HIS A 70   ? 0.8519 0.7895 0.8210 0.0323  0.1196  0.0004  70   HIS A C   
549   O  O   . HIS A 70   ? 0.7793 0.7209 0.7499 0.0401  0.1156  0.0024  70   HIS A O   
550   C  CB  . HIS A 70   ? 0.8660 0.8194 0.8433 0.0285  0.1207  -0.0024 70   HIS A CB  
551   C  CG  . HIS A 70   ? 0.7953 0.7497 0.7715 0.0229  0.1259  -0.0039 70   HIS A CG  
552   N  ND1 . HIS A 70   ? 0.8213 0.7820 0.8042 0.0138  0.1278  -0.0078 70   HIS A ND1 
553   C  CD2 . HIS A 70   ? 0.8860 0.8363 0.8553 0.0252  0.1297  -0.0019 70   HIS A CD2 
554   C  CE1 . HIS A 70   ? 0.9062 0.8669 0.8869 0.0105  0.1328  -0.0083 70   HIS A CE1 
555   N  NE2 . HIS A 70   ? 0.9725 0.9265 0.9446 0.0173  0.1342  -0.0046 70   HIS A NE2 
556   N  N   . THR A 71   ? 0.9585 0.8885 0.9245 0.0293  0.1209  -0.0001 71   THR A N   
557   C  CA  . THR A 71   ? 0.8395 0.7629 0.8015 0.0355  0.1189  0.0026  71   THR A CA  
558   C  C   . THR A 71   ? 0.7228 0.6598 0.6969 0.0394  0.1114  0.0017  71   THR A C   
559   O  O   . THR A 71   ? 0.7425 0.6763 0.7146 0.0457  0.1092  0.0042  71   THR A O   
560   C  CB  . THR A 71   ? 0.9157 0.8262 0.8701 0.0308  0.1229  0.0021  71   THR A CB  
561   O  OG1 . THR A 71   ? 1.0511 0.9708 1.0154 0.0258  0.1194  -0.0016 71   THR A OG1 
562   C  CG2 . THR A 71   ? 0.9067 0.8056 0.8515 0.0242  0.1305  0.0017  71   THR A CG2 
563   N  N   . SER A 72   ? 0.8983 0.8500 0.8844 0.0360  0.1075  -0.0016 72   SER A N   
564   C  CA  . SER A 72   ? 0.9637 0.9273 0.9608 0.0388  0.1008  -0.0026 72   SER A CA  
565   C  C   . SER A 72   ? 0.9684 0.9439 0.9732 0.0438  0.0962  -0.0024 72   SER A C   
566   O  O   . SER A 72   ? 0.8946 0.8818 0.9099 0.0445  0.0909  -0.0041 72   SER A O   
567   C  CB  . SER A 72   ? 0.8849 0.8559 0.8898 0.0318  0.0992  -0.0068 72   SER A CB  
568   O  OG  . SER A 72   ? 0.9866 0.9671 1.0006 0.0348  0.0933  -0.0075 72   SER A OG  
569   N  N   . VAL A 73   ? 1.1937 1.1657 1.1928 0.0474  0.0982  -0.0003 73   VAL A N   
570   C  CA  . VAL A 73   ? 1.1680 1.1512 1.1739 0.0513  0.0941  -0.0006 73   VAL A CA  
571   C  C   . VAL A 73   ? 1.2030 1.1897 1.2123 0.0590  0.0890  0.0013  73   VAL A C   
572   O  O   . VAL A 73   ? 1.1818 1.1802 1.2006 0.0612  0.0838  0.0000  73   VAL A O   
573   C  CB  . VAL A 73   ? 1.0646 1.0431 1.0629 0.0520  0.0981  0.0006  73   VAL A CB  
574   C  CG1 . VAL A 73   ? 1.1622 1.1258 1.1471 0.0567  0.1019  0.0044  73   VAL A CG1 
575   C  CG2 . VAL A 73   ? 1.0364 1.0264 1.0412 0.0560  0.0938  0.0000  73   VAL A CG2 
576   N  N   . ASP A 74   ? 1.2312 1.2079 1.2331 0.0633  0.0903  0.0042  74   ASP A N   
577   C  CA  . ASP A 74   ? 1.2193 1.1996 1.2246 0.0706  0.0859  0.0060  74   ASP A CA  
578   C  C   . ASP A 74   ? 1.2036 1.1867 1.2152 0.0701  0.0832  0.0055  74   ASP A C   
579   O  O   . ASP A 74   ? 1.2036 1.1887 1.2180 0.0757  0.0803  0.0070  74   ASP A O   
580   C  CB  . ASP A 74   ? 1.3079 1.2769 1.3019 0.0767  0.0886  0.0096  74   ASP A CB  
581   C  CG  . ASP A 74   ? 1.3549 1.3098 1.3389 0.0748  0.0938  0.0111  74   ASP A CG  
582   O  OD1 . ASP A 74   ? 1.3736 1.3251 1.3562 0.0676  0.0970  0.0093  74   ASP A OD1 
583   O  OD2 . ASP A 74   ? 1.4822 1.4298 1.4598 0.0806  0.0945  0.0139  74   ASP A OD2 
584   N  N   . GLN A 75   ? 0.7550 0.7385 0.7690 0.0637  0.0843  0.0032  75   GLN A N   
585   C  CA  . GLN A 75   ? 0.7371 0.7219 0.7556 0.0631  0.0823  0.0028  75   GLN A CA  
586   C  C   . GLN A 75   ? 0.7264 0.7227 0.7556 0.0591  0.0786  -0.0006 75   GLN A C   
587   O  O   . GLN A 75   ? 0.6516 0.6521 0.6867 0.0605  0.0754  -0.0008 75   GLN A O   
588   C  CB  . GLN A 75   ? 0.8703 0.8423 0.8796 0.0600  0.0870  0.0034  75   GLN A CB  
589   C  CG  . GLN A 75   ? 0.8721 0.8416 0.8822 0.0623  0.0859  0.0044  75   GLN A CG  
590   C  CD  . GLN A 75   ? 0.8602 0.8145 0.8584 0.0621  0.0909  0.0062  75   GLN A CD  
591   O  OE1 . GLN A 75   ? 0.9959 0.9414 0.9857 0.0583  0.0955  0.0060  75   GLN A OE1 
592   N  NE2 . GLN A 75   ? 1.0642 1.0149 1.0613 0.0661  0.0905  0.0081  75   GLN A NE2 
593   N  N   . SER A 76   ? 0.6438 0.6453 0.6755 0.0544  0.0790  -0.0031 76   SER A N   
594   C  CA  . SER A 76   ? 0.6498 0.6622 0.6910 0.0508  0.0756  -0.0065 76   SER A CA  
595   C  C   . SER A 76   ? 0.6047 0.6266 0.6510 0.0508  0.0739  -0.0080 76   SER A C   
596   O  O   . SER A 76   ? 0.6151 0.6348 0.6573 0.0532  0.0755  -0.0066 76   SER A O   
597   C  CB  . SER A 76   ? 0.5416 0.5509 0.5807 0.0439  0.0782  -0.0089 76   SER A CB  
598   O  OG  . SER A 76   ? 0.5578 0.5675 0.5949 0.0391  0.0814  -0.0106 76   SER A OG  
599   N  N   . TYR A 77   ? 0.5857 0.6181 0.6406 0.0483  0.0705  -0.0110 77   TYR A N   
600   C  CA  . TYR A 77   ? 0.6066 0.6486 0.6667 0.0479  0.0690  -0.0129 77   TYR A CA  
601   C  C   . TYR A 77   ? 0.6593 0.6994 0.7154 0.0426  0.0737  -0.0143 77   TYR A C   
602   O  O   . TYR A 77   ? 0.6819 0.7278 0.7400 0.0427  0.0737  -0.0153 77   TYR A O   
603   C  CB  . TYR A 77   ? 0.5362 0.5894 0.6061 0.0471  0.0642  -0.0158 77   TYR A CB  
604   C  CG  . TYR A 77   ? 0.4934 0.5501 0.5653 0.0408  0.0654  -0.0191 77   TYR A CG  
605   C  CD1 . TYR A 77   ? 0.5183 0.5698 0.5877 0.0376  0.0665  -0.0197 77   TYR A CD1 
606   C  CD2 . TYR A 77   ? 0.4680 0.5337 0.5444 0.0381  0.0652  -0.0219 77   TYR A CD2 
607   C  CE1 . TYR A 77   ? 0.6158 0.6712 0.6874 0.0318  0.0671  -0.0231 77   TYR A CE1 
608   C  CE2 . TYR A 77   ? 0.4680 0.5382 0.5472 0.0323  0.0660  -0.0253 77   TYR A CE2 
609   C  CZ  . TYR A 77   ? 0.5943 0.6594 0.6710 0.0291  0.0668  -0.0260 77   TYR A CZ  
610   O  OH  . TYR A 77   ? 0.7856 0.8558 0.8653 0.0234  0.0672  -0.0298 77   TYR A OH  
611   N  N   . PHE A 78   ? 0.9035 0.9353 0.9537 0.0379  0.0778  -0.0145 78   PHE A N   
612   C  CA  . PHE A 78   ? 0.9150 0.9454 0.9624 0.0316  0.0825  -0.0164 78   PHE A CA  
613   C  C   . PHE A 78   ? 0.9170 0.9334 0.9527 0.0316  0.0884  -0.0136 78   PHE A C   
614   O  O   . PHE A 78   ? 0.8713 0.8771 0.9003 0.0328  0.0900  -0.0115 78   PHE A O   
615   C  CB  . PHE A 78   ? 0.8833 0.9155 0.9336 0.0253  0.0827  -0.0197 78   PHE A CB  
616   C  CG  . PHE A 78   ? 0.8803 0.9139 0.9302 0.0180  0.0869  -0.0225 78   PHE A CG  
617   C  CD1 . PHE A 78   ? 0.9120 0.9585 0.9700 0.0161  0.0854  -0.0254 78   PHE A CD1 
618   C  CD2 . PHE A 78   ? 0.8878 0.9099 0.9295 0.0130  0.0925  -0.0223 78   PHE A CD2 
619   C  CE1 . PHE A 78   ? 1.0523 1.1010 1.1109 0.0092  0.0896  -0.0281 78   PHE A CE1 
620   C  CE2 . PHE A 78   ? 0.9724 0.9959 1.0143 0.0057  0.0967  -0.0251 78   PHE A CE2 
621   C  CZ  . PHE A 78   ? 1.0334 1.0708 1.0842 0.0037  0.0953  -0.0280 78   PHE A CZ  
622   N  N   . ALA A 79   ? 1.3061 1.3220 1.3387 0.0305  0.0919  -0.0134 79   ALA A N   
623   C  CA  . ALA A 79   ? 1.3516 1.3537 1.3722 0.0296  0.0983  -0.0110 79   ALA A CA  
624   C  C   . ALA A 79   ? 1.4401 1.4373 1.4581 0.0210  0.1032  -0.0133 79   ALA A C   
625   O  O   . ALA A 79   ? 1.5292 1.5349 1.5531 0.0155  0.1041  -0.0166 79   ALA A O   
626   C  CB  . ALA A 79   ? 1.3168 1.3197 1.3345 0.0322  0.1003  -0.0098 79   ALA A CB  
627   N  N   . ASN A 80   ? 1.0592 1.0432 1.0686 0.0199  0.1064  -0.0118 80   ASN A N   
628   C  CA  . ASN A 80   ? 1.0620 1.0408 1.0690 0.0115  0.1105  -0.0143 80   ASN A CA  
629   C  C   . ASN A 80   ? 1.0916 1.0676 1.0949 0.0059  0.1168  -0.0152 80   ASN A C   
630   O  O   . ASN A 80   ? 1.0966 1.0650 1.0918 0.0091  0.1205  -0.0122 80   ASN A O   
631   C  CB  . ASN A 80   ? 0.9887 0.9515 0.9851 0.0123  0.1132  -0.0121 80   ASN A CB  
632   C  CG  . ASN A 80   ? 0.9433 0.9008 0.9377 0.0036  0.1165  -0.0151 80   ASN A CG  
633   O  OD1 . ASN A 80   ? 1.0363 1.0035 1.0383 -0.0029 0.1162  -0.0192 80   ASN A OD1 
634   N  ND2 . ASN A 80   ? 1.0179 0.9602 1.0018 0.0038  0.1197  -0.0133 80   ASN A ND2 
635   N  N   . ILE A 81   ? 0.8455 0.8280 0.8547 -0.0023 0.1180  -0.0195 81   ILE A N   
636   C  CA  . ILE A 81   ? 0.7529 0.7326 0.7591 -0.0092 0.1248  -0.0208 81   ILE A CA  
637   C  C   . ILE A 81   ? 0.8319 0.7956 0.8280 -0.0148 0.1305  -0.0207 81   ILE A C   
638   O  O   . ILE A 81   ? 0.9118 0.8753 0.9101 -0.0179 0.1283  -0.0230 81   ILE A O   
639   C  CB  . ILE A 81   ? 0.7249 0.7217 0.7440 -0.0150 0.1231  -0.0257 81   ILE A CB  
640   C  CG1 . ILE A 81   ? 0.7054 0.7156 0.7321 -0.0091 0.1188  -0.0253 81   ILE A CG1 
641   C  CG2 . ILE A 81   ? 0.6586 0.6518 0.6750 -0.0238 0.1306  -0.0277 81   ILE A CG2 
642   C  CD1 . ILE A 81   ? 0.8006 0.8061 0.8208 -0.0070 0.1236  -0.0226 81   ILE A CD1 
643   N  N   . PRO A 82   ? 0.8563 0.8056 0.8406 -0.0161 0.1378  -0.0182 82   PRO A N   
644   C  CA  . PRO A 82   ? 0.7883 0.7195 0.7607 -0.0199 0.1432  -0.0174 82   PRO A CA  
645   C  C   . PRO A 82   ? 0.7937 0.7275 0.7710 -0.0305 0.1448  -0.0225 82   PRO A C   
646   O  O   . PRO A 82   ? 0.7429 0.6866 0.7277 -0.0373 0.1466  -0.0260 82   PRO A O   
647   C  CB  . PRO A 82   ? 0.8575 0.7751 0.8175 -0.0196 0.1510  -0.0141 82   PRO A CB  
648   C  CG  . PRO A 82   ? 0.9251 0.8516 0.8885 -0.0122 0.1481  -0.0119 82   PRO A CG  
649   C  CD  . PRO A 82   ? 0.9033 0.8511 0.8833 -0.0133 0.1415  -0.0157 82   PRO A CD  
650   N  N   . ALA A 83   ? 0.7562 0.6814 0.7291 -0.0318 0.1441  -0.0230 83   ALA A N   
651   C  CA  . ALA A 83   ? 0.6794 0.6041 0.6546 -0.0418 0.1459  -0.0278 83   ALA A CA  
652   C  C   . ALA A 83   ? 0.7473 0.6569 0.7120 -0.0490 0.1554  -0.0277 83   ALA A C   
653   O  O   . ALA A 83   ? 0.7304 0.6268 0.6836 -0.0453 0.1605  -0.0233 83   ALA A O   
654   C  CB  . ALA A 83   ? 0.5959 0.5144 0.5681 -0.0404 0.1425  -0.0283 83   ALA A CB  
655   N  N   . THR A 84   ? 0.8747 0.7862 0.8432 -0.0596 0.1577  -0.0327 84   THR A N   
656   C  CA  . THR A 84   ? 0.8538 0.7511 0.8131 -0.0678 0.1670  -0.0332 84   THR A CA  
657   C  C   . THR A 84   ? 0.8547 0.7275 0.7963 -0.0656 0.1717  -0.0295 84   THR A C   
658   O  O   . THR A 84   ? 0.9497 0.8068 0.8799 -0.0694 0.1800  -0.0278 84   THR A O   
659   C  CB  . THR A 84   ? 0.8955 0.8010 0.8636 -0.0798 0.1678  -0.0400 84   THR A CB  
660   O  OG1 . THR A 84   ? 0.7953 0.7250 0.7806 -0.0801 0.1617  -0.0436 84   THR A OG1 
661   C  CG2 . THR A 84   ? 0.9759 0.8716 0.9382 -0.0891 0.1776  -0.0410 84   THR A CG2 
662   N  N   . GLU A 85   ? 1.2026 1.0715 1.1413 -0.0592 0.1666  -0.0279 85   GLU A N   
663   C  CA  . GLU A 85   ? 1.2665 1.1125 1.1883 -0.0559 0.1707  -0.0242 85   GLU A CA  
664   C  C   . GLU A 85   ? 1.3229 1.1577 1.2334 -0.0481 0.1748  -0.0181 85   GLU A C   
665   O  O   . GLU A 85   ? 1.3554 1.1696 1.2504 -0.0488 0.1820  -0.0154 85   GLU A O   
666   C  CB  . GLU A 85   ? 1.3085 1.1551 1.2309 -0.0498 0.1641  -0.0237 85   GLU A CB  
667   C  CG  . GLU A 85   ? 1.4220 1.2481 1.3307 -0.0513 0.1677  -0.0232 85   GLU A CG  
668   C  CD  . GLU A 85   ? 1.4468 1.2733 1.3555 -0.0438 0.1615  -0.0219 85   GLU A CD  
669   O  OE1 . GLU A 85   ? 1.2452 1.0876 1.1646 -0.0375 0.1546  -0.0212 85   GLU A OE1 
670   O  OE2 . GLU A 85   ? 1.6305 1.4411 1.5283 -0.0442 0.1637  -0.0215 85   GLU A OE2 
671   N  N   . THR A 86   ? 1.0434 0.8910 0.9608 -0.0404 0.1703  -0.0158 86   THR A N   
672   C  CA  . THR A 86   ? 1.0033 0.8415 0.9103 -0.0324 0.1734  -0.0103 86   THR A CA  
673   C  C   . THR A 86   ? 1.0253 0.8558 0.9259 -0.0384 0.1820  -0.0100 86   THR A C   
674   O  O   . THR A 86   ? 1.0944 0.9075 0.9799 -0.0346 0.1879  -0.0057 86   THR A O   
675   C  CB  . THR A 86   ? 0.9477 0.8026 0.8646 -0.0236 0.1663  -0.0087 86   THR A CB  
676   O  OG1 . THR A 86   ? 1.0372 0.9103 0.9679 -0.0287 0.1646  -0.0123 86   THR A OG1 
677   C  CG2 . THR A 86   ? 0.9713 0.8336 0.8947 -0.0180 0.1583  -0.0088 86   THR A CG2 
678   N  N   . CYS A 87   ? 1.0112 0.8545 0.9230 -0.0475 0.1830  -0.0146 87   CYS A N   
679   C  CA  . CYS A 87   ? 1.0717 0.9083 0.9782 -0.0542 0.1918  -0.0147 87   CYS A CA  
680   C  C   . CYS A 87   ? 1.0763 0.8916 0.9697 -0.0619 0.1999  -0.0152 87   CYS A C   
681   O  O   . CYS A 87   ? 1.1444 0.9431 1.0243 -0.0627 0.2082  -0.0122 87   CYS A O   
682   C  CB  . CYS A 87   ? 1.0847 0.9421 1.0079 -0.0619 0.1905  -0.0198 87   CYS A CB  
683   S  SG  . CYS A 87   ? 1.0113 0.8947 0.9514 -0.0539 0.1801  -0.0203 87   CYS A SG  
684   N  N   . MET A 88   ? 1.3629 1.1778 1.2594 -0.0674 0.1976  -0.0190 88   MET A N   
685   C  CA  . MET A 88   ? 1.4247 1.2192 1.3088 -0.0752 0.2050  -0.0200 88   MET A CA  
686   C  C   . MET A 88   ? 1.4855 1.2565 1.3504 -0.0671 0.2080  -0.0144 88   MET A C   
687   O  O   . MET A 88   ? 1.4825 1.2326 1.3334 -0.0721 0.2159  -0.0139 88   MET A O   
688   C  CB  . MET A 88   ? 1.3587 1.1600 1.2516 -0.0830 0.2010  -0.0260 88   MET A CB  
689   C  CG  . MET A 88   ? 1.4304 1.2495 1.3389 -0.0941 0.2010  -0.0324 88   MET A CG  
690   S  SD  . MET A 88   ? 1.4609 1.2759 1.3663 -0.1014 0.2115  -0.0319 88   MET A SD  
691   C  CE  . MET A 88   ? 1.6384 1.4242 1.5255 -0.1100 0.2218  -0.0320 88   MET A CE  
692   N  N   . THR A 89   ? 1.3649 1.1387 1.2289 -0.0548 0.2021  -0.0104 89   THR A N   
693   C  CA  . THR A 89   ? 1.2738 1.0267 1.1200 -0.0461 0.2047  -0.0049 89   THR A CA  
694   C  C   . THR A 89   ? 1.2624 0.9980 1.0934 -0.0454 0.2139  -0.0010 89   THR A C   
695   O  O   . THR A 89   ? 1.4427 1.1553 1.2559 -0.0433 0.2196  0.0021  89   THR A O   
696   C  CB  . THR A 89   ? 1.3211 1.0835 1.1713 -0.0332 0.1966  -0.0016 89   THR A CB  
697   O  OG1 . THR A 89   ? 1.4758 1.2540 1.3400 -0.0340 0.1885  -0.0052 89   THR A OG1 
698   C  CG2 . THR A 89   ? 1.2924 1.0345 1.1252 -0.0239 0.1988  0.0037  89   THR A CG2 
699   N  N   . CYS A 90   ? 1.2388 0.9844 1.0756 -0.0471 0.2156  -0.0011 90   CYS A N   
700   C  CA  . CYS A 90   ? 1.3232 1.0535 1.1460 -0.0467 0.2245  0.0025  90   CYS A CA  
701   C  C   . CYS A 90   ? 1.3371 1.0640 1.1608 -0.0605 0.2328  -0.0011 90   CYS A C   
702   O  O   . CYS A 90   ? 1.4398 1.1449 1.2473 -0.0636 0.2421  0.0010  90   CYS A O   
703   C  CB  . CYS A 90   ? 1.2421 0.9843 1.0691 -0.0380 0.2215  0.0055  90   CYS A CB  
704   S  SG  . CYS A 90   ? 1.2610 0.9980 1.0789 -0.0209 0.2159  0.0116  90   CYS A SG  
705   N  N   . HIS A 91   ? 1.1286 0.8766 0.9707 -0.0687 0.2296  -0.0066 91   HIS A N   
706   C  CA  . HIS A 91   ? 1.1610 0.9095 1.0065 -0.0817 0.2371  -0.0103 91   HIS A CA  
707   C  C   . HIS A 91   ? 1.3117 1.0499 1.1547 -0.0930 0.2407  -0.0146 91   HIS A C   
708   O  O   . HIS A 91   ? 1.3525 1.0927 1.2003 -0.1051 0.2464  -0.0187 91   HIS A O   
709   C  CB  . HIS A 91   ? 1.1040 0.8805 0.9705 -0.0852 0.2321  -0.0145 91   HIS A CB  
710   C  CG  . HIS A 91   ? 1.1376 0.9232 1.0059 -0.0758 0.2300  -0.0107 91   HIS A CG  
711   N  ND1 . HIS A 91   ? 1.1857 0.9597 1.0424 -0.0742 0.2380  -0.0069 91   HIS A ND1 
712   C  CD2 . HIS A 91   ? 1.2392 1.0434 1.1187 -0.0672 0.2208  -0.0102 91   HIS A CD2 
713   C  CE1 . HIS A 91   ? 1.1330 0.9185 0.9938 -0.0651 0.2336  -0.0044 91   HIS A CE1 
714   N  NE2 . HIS A 91   ? 1.1839 0.9878 1.0587 -0.0609 0.2232  -0.0064 91   HIS A NE2 
715   N  N   . SER A 92   ? 1.4573 1.1849 1.2933 -0.0895 0.2377  -0.0140 92   SER A N   
716   C  CA  . SER A 92   ? 1.4268 1.1386 1.2554 -0.0993 0.2427  -0.0172 92   SER A CA  
717   C  C   . SER A 92   ? 1.4666 1.1504 1.2743 -0.1015 0.2544  -0.0135 92   SER A C   
718   O  O   . SER A 92   ? 1.5924 1.2628 1.3942 -0.1122 0.2608  -0.0166 92   SER A O   
719   C  CB  . SER A 92   ? 1.4489 1.1564 1.2748 -0.0942 0.2363  -0.0173 92   SER A CB  
720   O  OG  . SER A 92   ? 1.4346 1.1662 1.2795 -0.0952 0.2266  -0.0219 92   SER A OG  
721   N  N   . GLN A 93   ? 1.5040 1.1785 1.3000 -0.0916 0.2573  -0.0072 93   GLN A N   
722   C  CA  . GLN A 93   ? 1.6218 1.2691 1.3966 -0.0922 0.2684  -0.0031 93   GLN A CA  
723   C  C   . GLN A 93   ? 1.6740 1.3244 1.4477 -0.0903 0.2733  -0.0002 93   GLN A C   
724   O  O   . GLN A 93   ? 1.7270 1.3601 1.4882 -0.0958 0.2839  0.0013  93   GLN A O   
725   C  CB  . GLN A 93   ? 1.6826 1.3093 1.4387 -0.0801 0.2681  0.0026  93   GLN A CB  
726   C  CG  . GLN A 93   ? 1.5751 1.1949 1.3291 -0.0815 0.2647  0.0003  93   GLN A CG  
727   C  CD  . GLN A 93   ? 1.6930 1.2898 1.4267 -0.0702 0.2662  0.0060  93   GLN A CD  
728   O  OE1 . GLN A 93   ? 1.8033 1.3907 1.5250 -0.0605 0.2689  0.0118  93   GLN A OE1 
729   N  NE2 . GLN A 93   ? 1.7652 1.3529 1.4944 -0.0710 0.2643  0.0044  93   GLN A NE2 
730   N  N   . ILE A 94   ? 1.5446 1.2165 1.3308 -0.0827 0.2657  0.0007  94   ILE A N   
731   C  CA  . ILE A 94   ? 1.4070 1.0835 1.1927 -0.0796 0.2692  0.0035  94   ILE A CA  
732   C  C   . ILE A 94   ? 1.4123 1.1080 1.2155 -0.0915 0.2707  -0.0020 94   ILE A C   
733   O  O   . ILE A 94   ? 1.4426 1.1616 1.2653 -0.0944 0.2626  -0.0068 94   ILE A O   
734   C  CB  . ILE A 94   ? 1.3045 0.9939 1.0941 -0.0651 0.2603  0.0071  94   ILE A CB  
735   C  CG1 . ILE A 94   ? 1.4064 1.0749 1.1762 -0.0527 0.2609  0.0133  94   ILE A CG1 
736   C  CG2 . ILE A 94   ? 1.1926 0.8939 0.9877 -0.0637 0.2619  0.0080  94   ILE A CG2 
737   C  CD1 . ILE A 94   ? 1.3377 1.0186 1.1114 -0.0387 0.2523  0.0166  94   ILE A CD1 
738   N  N   . LYS A 95   ? 1.3368 1.0228 1.1329 -0.0981 0.2812  -0.0013 95   LYS A N   
739   C  CA  . LYS A 95   ? 1.3163 1.0201 1.1282 -0.1089 0.2840  -0.0060 95   LYS A CA  
740   C  C   . LYS A 95   ? 1.3753 1.0924 1.2034 -0.1210 0.2807  -0.0135 95   LYS A C   
741   O  O   . LYS A 95   ? 1.2845 1.0259 1.1321 -0.1265 0.2770  -0.0183 95   LYS A O   
742   C  CB  . LYS A 95   ? 1.1952 0.9220 1.0198 -0.1013 0.2775  -0.0052 95   LYS A CB  
743   C  CG  . LYS A 95   ? 1.1816 0.8983 0.9930 -0.0944 0.2839  0.0005  95   LYS A CG  
744   C  CD  . LYS A 95   ? 1.2778 0.9815 1.0818 -0.1055 0.2972  0.0000  95   LYS A CD  
745   C  CE  . LYS A 95   ? 1.4145 1.1075 1.2043 -0.0982 0.3038  0.0059  95   LYS A CE  
746   N  NZ  . LYS A 95   ? 1.3845 1.0651 1.1673 -0.1092 0.3173  0.0055  95   LYS A NZ  
747   N  N   . THR A 96   ? 2.0644 1.7659 1.8843 -0.1248 0.2818  -0.0147 96   THR A N   
748   C  CA  . THR A 96   ? 2.1055 1.8174 1.9388 -0.1365 0.2791  -0.0220 96   THR A CA  
749   C  C   . THR A 96   ? 2.1739 1.8873 2.0126 -0.1516 0.2883  -0.0264 96   THR A C   
750   O  O   . THR A 96   ? 2.2432 1.9400 2.0691 -0.1542 0.2990  -0.0232 96   THR A O   
751   C  CB  . THR A 96   ? 2.0961 1.7884 1.9173 -0.1368 0.2788  -0.0220 96   THR A CB  
752   O  OG1 . THR A 96   ? 2.2443 1.9479 2.0790 -0.1478 0.2753  -0.0295 96   THR A OG1 
753   C  CG2 . THR A 96   ? 2.1366 1.7971 1.9350 -0.1401 0.2911  -0.0185 96   THR A CG2 
754   N  N   . TYR A 97   ? 1.8922 1.6264 1.7503 -0.1615 0.2840  -0.0337 97   TYR A N   
755   C  CA  . TYR A 97   ? 1.9436 1.6850 1.8113 -0.1763 0.2913  -0.0390 97   TYR A CA  
756   C  C   . TYR A 97   ? 1.8412 1.5927 1.7132 -0.1744 0.2956  -0.0366 97   TYR A C   
757   O  O   . TYR A 97   ? 1.8107 1.5512 1.6759 -0.1817 0.3069  -0.0359 97   TYR A O   
758   C  CB  . TYR A 97   ? 2.0186 1.7332 1.8710 -0.1869 0.3026  -0.0396 97   TYR A CB  
759   C  CG  . TYR A 97   ? 2.1662 1.8661 2.0100 -0.1871 0.2993  -0.0409 97   TYR A CG  
760   C  CD1 . TYR A 97   ? 2.2186 1.9363 2.0771 -0.1879 0.2885  -0.0462 97   TYR A CD1 
761   C  CD2 . TYR A 97   ? 2.2611 1.9287 2.0815 -0.1861 0.3070  -0.0367 97   TYR A CD2 
762   C  CE1 . TYR A 97   ? 2.1901 1.8942 2.0403 -0.1879 0.2856  -0.0473 97   TYR A CE1 
763   C  CE2 . TYR A 97   ? 2.3357 1.9895 2.1477 -0.1860 0.3041  -0.0379 97   TYR A CE2 
764   C  CZ  . TYR A 97   ? 2.2546 1.9269 2.0817 -0.1870 0.2934  -0.0432 97   TYR A CZ  
765   O  OH  . TYR A 97   ? 2.2031 1.8614 2.0215 -0.1867 0.2907  -0.0443 97   TYR A OH  
766   N  N   . SER A 98   ? 1.5458 1.3181 1.4290 -0.1644 0.2866  -0.0354 98   SER A N   
767   C  CA  . SER A 98   ? 1.4532 1.2381 1.3420 -0.1611 0.2887  -0.0335 98   SER A CA  
768   C  C   . SER A 98   ? 1.3793 1.1975 1.2931 -0.1630 0.2801  -0.0391 98   SER A C   
769   O  O   . SER A 98   ? 1.4203 1.2513 1.3440 -0.1600 0.2696  -0.0419 98   SER A O   
770   C  CB  . SER A 98   ? 1.3582 1.1345 1.2341 -0.1450 0.2862  -0.0258 98   SER A CB  
771   O  OG  . SER A 98   ? 1.2225 1.0128 1.1048 -0.1411 0.2868  -0.0242 98   SER A OG  
772   N  N   . PRO A 99   ? 1.2212 1.0537 1.1451 -0.1676 0.2845  -0.0408 99   PRO A N   
773   C  CA  . PRO A 99   ? 1.2337 1.0981 1.1814 -0.1696 0.2766  -0.0464 99   PRO A CA  
774   C  C   . PRO A 99   ? 1.1635 1.0424 1.1168 -0.1555 0.2653  -0.0439 99   PRO A C   
775   O  O   . PRO A 99   ? 1.2805 1.1813 1.2506 -0.1552 0.2558  -0.0484 99   PRO A O   
776   C  CB  . PRO A 99   ? 1.1978 1.0701 1.1514 -0.1770 0.2857  -0.0477 99   PRO A CB  
777   C  CG  . PRO A 99   ? 1.1194 0.9660 1.0513 -0.1729 0.2958  -0.0406 99   PRO A CG  
778   C  CD  . PRO A 99   ? 1.1806 1.0008 1.0948 -0.1722 0.2973  -0.0381 99   PRO A CD  
779   N  N   . LEU A 100  ? 1.1484 1.0155 1.0881 -0.1438 0.2659  -0.0369 100  LEU A N   
780   C  CA  . LEU A 100  ? 1.1864 1.0671 1.1315 -0.1307 0.2556  -0.0346 100  LEU A CA  
781   C  C   . LEU A 100  ? 1.1527 1.0351 1.1000 -0.1254 0.2451  -0.0354 100  LEU A C   
782   O  O   . LEU A 100  ? 1.0875 0.9866 1.0448 -0.1174 0.2354  -0.0356 100  LEU A O   
783   C  CB  . LEU A 100  ? 1.2201 1.0861 1.1488 -0.1197 0.2589  -0.0272 100  LEU A CB  
784   C  CG  . LEU A 100  ? 0.9941 0.8641 0.9230 -0.1210 0.2665  -0.0259 100  LEU A CG  
785   C  CD1 . LEU A 100  ? 0.9805 0.8326 0.8903 -0.1098 0.2699  -0.0185 100  LEU A CD1 
786   C  CD2 . LEU A 100  ? 0.8928 0.7923 0.8421 -0.1199 0.2598  -0.0297 100  LEU A CD2 
787   N  N   . LEU A 101  ? 1.1035 0.9685 1.0412 -0.1296 0.2472  -0.0357 101  LEU A N   
788   C  CA  . LEU A 101  ? 1.0436 0.9084 0.9820 -0.1250 0.2382  -0.0364 101  LEU A CA  
789   C  C   . LEU A 101  ? 1.0290 0.9046 0.9802 -0.1357 0.2352  -0.0437 101  LEU A C   
790   O  O   . LEU A 101  ? 0.9955 0.8662 0.9445 -0.1342 0.2299  -0.0445 101  LEU A O   
791   C  CB  . LEU A 101  ? 1.0427 0.8794 0.9598 -0.1200 0.2418  -0.0310 101  LEU A CB  
792   C  CG  . LEU A 101  ? 0.9664 0.7949 0.8720 -0.1056 0.2399  -0.0239 101  LEU A CG  
793   C  CD1 . LEU A 101  ? 1.0041 0.8025 0.8866 -0.1035 0.2484  -0.0187 101  LEU A CD1 
794   C  CD2 . LEU A 101  ? 1.0298 0.8680 0.9412 -0.0957 0.2282  -0.0233 101  LEU A CD2 
795   N  N   . GLU A 102  ? 1.5452 1.4355 1.5096 -0.1463 0.2385  -0.0490 102  GLU A N   
796   C  CA  . GLU A 102  ? 1.6137 1.5142 1.5900 -0.1571 0.2360  -0.0564 102  GLU A CA  
797   C  C   . GLU A 102  ? 1.5510 1.4702 1.5401 -0.1513 0.2232  -0.0592 102  GLU A C   
798   O  O   . GLU A 102  ? 1.5861 1.5031 1.5759 -0.1544 0.2190  -0.0625 102  GLU A O   
799   C  CB  . GLU A 102  ? 1.6480 1.5634 1.6375 -0.1686 0.2417  -0.0616 102  GLU A CB  
800   C  CG  . GLU A 102  ? 1.7813 1.7086 1.7841 -0.1810 0.2398  -0.0700 102  GLU A CG  
801   C  CD  . GLU A 102  ? 1.9745 1.8802 1.9653 -0.1874 0.2429  -0.0711 102  GLU A CD  
802   O  OE1 . GLU A 102  ? 1.9351 1.8341 1.9203 -0.1810 0.2361  -0.0699 102  GLU A OE1 
803   O  OE2 . GLU A 102  ? 2.1220 2.0172 2.1088 -0.1991 0.2525  -0.0734 102  GLU A OE2 
804   N  N   . LYS A 103  ? 1.1170 1.0540 1.1155 -0.1428 0.2170  -0.0579 103  LYS A N   
805   C  CA  . LYS A 103  ? 0.9911 0.9456 1.0013 -0.1368 0.2051  -0.0602 103  LYS A CA  
806   C  C   . LYS A 103  ? 0.9976 0.9373 0.9964 -0.1287 0.2003  -0.0565 103  LYS A C   
807   O  O   . LYS A 103  ? 1.0869 1.0327 1.0913 -0.1287 0.1931  -0.0598 103  LYS A O   
808   C  CB  . LYS A 103  ? 1.0783 1.0515 1.0984 -0.1285 0.2003  -0.0588 103  LYS A CB  
809   C  CG  . LYS A 103  ? 1.1274 1.1180 1.1604 -0.1355 0.2041  -0.0626 103  LYS A CG  
810   C  CD  . LYS A 103  ? 1.1696 1.1825 1.2208 -0.1420 0.1982  -0.0703 103  LYS A CD  
811   C  CE  . LYS A 103  ? 1.2607 1.2941 1.3262 -0.1468 0.2008  -0.0739 103  LYS A CE  
812   N  NZ  . LYS A 103  ? 1.3619 1.4029 1.4285 -0.1363 0.1986  -0.0697 103  LYS A NZ  
813   N  N   . VAL A 104  ? 0.7769 0.6973 0.7595 -0.1214 0.2042  -0.0498 104  VAL A N   
814   C  CA  . VAL A 104  ? 0.7652 0.6715 0.7367 -0.1132 0.2001  -0.0460 104  VAL A CA  
815   C  C   . VAL A 104  ? 0.8743 0.7659 0.8387 -0.1209 0.2027  -0.0487 104  VAL A C   
816   O  O   . VAL A 104  ? 0.8785 0.7678 0.8417 -0.1173 0.1966  -0.0491 104  VAL A O   
817   C  CB  . VAL A 104  ? 0.7124 0.6017 0.6682 -0.1037 0.2041  -0.0385 104  VAL A CB  
818   C  CG1 . VAL A 104  ? 0.6287 0.5021 0.5723 -0.0959 0.2010  -0.0347 104  VAL A CG1 
819   C  CG2 . VAL A 104  ? 0.6983 0.6030 0.6615 -0.0953 0.2000  -0.0362 104  VAL A CG2 
820   N  N   . ARG A 105  ? 1.3810 1.2620 1.3404 -0.1316 0.2120  -0.0506 105  ARG A N   
821   C  CA  . ARG A 105  ? 1.3745 1.2414 1.3273 -0.1401 0.2150  -0.0537 105  ARG A CA  
822   C  C   . ARG A 105  ? 1.3610 1.2462 1.3299 -0.1483 0.2092  -0.0616 105  ARG A C   
823   O  O   . ARG A 105  ? 1.4706 1.3471 1.4353 -0.1524 0.2080  -0.0644 105  ARG A O   
824   C  CB  . ARG A 105  ? 1.3880 1.2362 1.3294 -0.1492 0.2273  -0.0531 105  ARG A CB  
825   C  CG  . ARG A 105  ? 1.4144 1.2379 1.3352 -0.1415 0.2335  -0.0454 105  ARG A CG  
826   C  CD  . ARG A 105  ? 1.4759 1.2774 1.3834 -0.1511 0.2458  -0.0452 105  ARG A CD  
827   N  NE  . ARG A 105  ? 1.5107 1.3245 1.4298 -0.1630 0.2511  -0.0500 105  ARG A NE  
828   C  CZ  . ARG A 105  ? 1.5508 1.3674 1.4702 -0.1630 0.2571  -0.0476 105  ARG A CZ  
829   N  NH1 . ARG A 105  ? 1.5772 1.3851 1.4856 -0.1517 0.2584  -0.0406 105  ARG A NH1 
830   N  NH2 . ARG A 105  ? 1.4604 1.2890 1.3914 -0.1745 0.2620  -0.0525 105  ARG A NH2 
831   N  N   . GLU A 106  ? 1.0302 0.9404 1.0167 -0.1503 0.2054  -0.0654 106  GLU A N   
832   C  CA  . GLU A 106  ? 1.0730 1.0022 1.0751 -0.1565 0.1988  -0.0729 106  GLU A CA  
833   C  C   . GLU A 106  ? 1.1740 1.1090 1.1784 -0.1471 0.1880  -0.0724 106  GLU A C   
834   O  O   . GLU A 106  ? 1.2233 1.1599 1.2303 -0.1510 0.1836  -0.0769 106  GLU A O   
835   C  CB  . GLU A 106  ? 1.1008 1.0553 1.1209 -0.1605 0.1979  -0.0770 106  GLU A CB  
836   C  CG  . GLU A 106  ? 1.1889 1.1643 1.2256 -0.1669 0.1911  -0.0851 106  GLU A CG  
837   C  CD  . GLU A 106  ? 1.4097 1.4013 1.4600 -0.1778 0.1955  -0.0908 106  GLU A CD  
838   O  OE1 . GLU A 106  ? 1.4522 1.4409 1.5002 -0.1792 0.2033  -0.0880 106  GLU A OE1 
839   O  OE2 . GLU A 106  ? 1.4870 1.4944 1.5502 -0.1848 0.1912  -0.0981 106  GLU A OE2 
840   N  N   . SER A 107  ? 1.2671 1.2049 1.2700 -0.1349 0.1837  -0.0670 107  SER A N   
841   C  CA  . SER A 107  ? 1.2051 1.1426 1.2062 -0.1254 0.1753  -0.0651 107  SER A CA  
842   C  C   . SER A 107  ? 1.2588 1.1705 1.2421 -0.1239 0.1787  -0.0617 107  SER A C   
843   O  O   . SER A 107  ? 1.3759 1.2698 1.3480 -0.1301 0.1875  -0.0609 107  SER A O   
844   C  CB  . SER A 107  ? 1.0182 0.9645 1.0222 -0.1133 0.1706  -0.0602 107  SER A CB  
845   O  OG  . SER A 107  ? 1.0365 1.0062 1.0565 -0.1143 0.1674  -0.0634 107  SER A OG  
846   N  N   . TYR A 108  ? 1.2721 1.1814 1.2523 -0.1156 0.1720  -0.0597 108  TYR A N   
847   C  CA  . TYR A 108  ? 1.4309 1.3173 1.3950 -0.1129 0.1741  -0.0566 108  TYR A CA  
848   C  C   . TYR A 108  ? 1.4514 1.3291 1.4123 -0.1239 0.1768  -0.0620 108  TYR A C   
849   O  O   . TYR A 108  ? 1.3434 1.2108 1.2971 -0.1220 0.1743  -0.0622 108  TYR A O   
850   C  CB  . TYR A 108  ? 1.3838 1.2504 1.3324 -0.1085 0.1818  -0.0500 108  TYR A CB  
851   C  CG  . TYR A 108  ? 1.4023 1.2469 1.3344 -0.1024 0.1830  -0.0456 108  TYR A CG  
852   C  CD1 . TYR A 108  ? 1.3969 1.2426 1.3274 -0.0903 0.1769  -0.0413 108  TYR A CD1 
853   C  CD2 . TYR A 108  ? 1.3112 1.1338 1.2293 -0.1087 0.1903  -0.0459 108  TYR A CD2 
854   C  CE1 . TYR A 108  ? 1.3584 1.1849 1.2743 -0.0844 0.1781  -0.0374 108  TYR A CE1 
855   C  CE2 . TYR A 108  ? 1.4208 1.2231 1.3234 -0.1026 0.1914  -0.0419 108  TYR A CE2 
856   C  CZ  . TYR A 108  ? 1.4726 1.2775 1.3744 -0.0903 0.1853  -0.0377 108  TYR A CZ  
857   O  OH  . TYR A 108  ? 1.6306 1.4162 1.5175 -0.0839 0.1865  -0.0337 108  TYR A OH  
858   N  N   . ALA A 109  ? 1.5024 1.3841 1.4686 -0.1354 0.1821  -0.0666 109  ALA A N   
859   C  CA  . ALA A 109  ? 1.5455 1.4244 1.5127 -0.1468 0.1832  -0.0732 109  ALA A CA  
860   C  C   . ALA A 109  ? 1.5650 1.4671 1.5485 -0.1482 0.1737  -0.0795 109  ALA A C   
861   O  O   . ALA A 109  ? 1.6579 1.5567 1.6398 -0.1508 0.1701  -0.0832 109  ALA A O   
862   C  CB  . ALA A 109  ? 1.6208 1.4963 1.5885 -0.1591 0.1925  -0.0761 109  ALA A CB  
863   N  N   . THR A 110  ? 1.5266 1.4516 1.5253 -0.1462 0.1696  -0.0807 110  THR A N   
864   C  CA  . THR A 110  ? 1.5155 1.4631 1.5291 -0.1446 0.1598  -0.0854 110  THR A CA  
865   C  C   . THR A 110  ? 1.4978 1.4534 1.5139 -0.1311 0.1532  -0.0804 110  THR A C   
866   O  O   . THR A 110  ? 1.5337 1.4850 1.5455 -0.1249 0.1563  -0.0746 110  THR A O   
867   C  CB  . THR A 110  ? 1.5494 1.5190 1.5797 -0.1531 0.1598  -0.0917 110  THR A CB  
868   O  OG1 . THR A 110  ? 1.4647 1.4425 1.4997 -0.1492 0.1624  -0.0881 110  THR A OG1 
869   C  CG2 . THR A 110  ? 1.6182 1.5796 1.6464 -0.1671 0.1673  -0.0965 110  THR A CG2 
870   N  N   . GLY A 111  ? 1.5914 1.5584 1.6141 -0.1267 0.1443  -0.0827 111  GLY A N   
871   C  CA  . GLY A 111  ? 1.5997 1.5732 1.6243 -0.1143 0.1378  -0.0782 111  GLY A CA  
872   C  C   . GLY A 111  ? 1.5413 1.5333 1.5777 -0.1104 0.1358  -0.0773 111  GLY A C   
873   O  O   . GLY A 111  ? 1.4672 1.4650 1.5057 -0.1004 0.1304  -0.0738 111  GLY A O   
874   N  N   . LYS A 112  ? 1.5696 1.5710 1.6137 -0.1180 0.1400  -0.0804 112  LYS A N   
875   C  CA  . LYS A 112  ? 1.4897 1.5093 1.5452 -0.1145 0.1381  -0.0800 112  LYS A CA  
876   C  C   . LYS A 112  ? 1.5047 1.5149 1.5520 -0.1058 0.1410  -0.0725 112  LYS A C   
877   O  O   . LYS A 112  ? 1.6025 1.5934 1.6368 -0.1066 0.1481  -0.0686 112  LYS A O   
878   C  CB  . LYS A 112  ? 1.4921 1.5226 1.5568 -0.1249 0.1432  -0.0849 112  LYS A CB  
879   C  CG  . LYS A 112  ? 1.5014 1.5434 1.5756 -0.1340 0.1402  -0.0930 112  LYS A CG  
880   C  CD  . LYS A 112  ? 1.3962 1.4623 1.4852 -0.1296 0.1308  -0.0966 112  LYS A CD  
881   C  CE  . LYS A 112  ? 1.4971 1.5678 1.5893 -0.1329 0.1246  -0.1025 112  LYS A CE  
882   N  NZ  . LYS A 112  ? 1.3738 1.4512 1.4731 -0.1459 0.1278  -0.1098 112  LYS A NZ  
883   N  N   . PRO A 113  ? 1.0437 1.0669 1.0980 -0.0971 0.1357  -0.0704 113  PRO A N   
884   C  CA  . PRO A 113  ? 0.9651 0.9806 1.0123 -0.0887 0.1378  -0.0636 113  PRO A CA  
885   C  C   . PRO A 113  ? 0.9456 0.9656 0.9955 -0.0918 0.1440  -0.0631 113  PRO A C   
886   O  O   . PRO A 113  ? 0.9347 0.9645 0.9927 -0.1006 0.1468  -0.0680 113  PRO A O   
887   C  CB  . PRO A 113  ? 0.8821 0.9103 0.9364 -0.0789 0.1288  -0.0624 113  PRO A CB  
888   C  CG  . PRO A 113  ? 0.8385 0.8873 0.9074 -0.0832 0.1239  -0.0689 113  PRO A CG  
889   C  CD  . PRO A 113  ? 1.0141 1.0588 1.0823 -0.0940 0.1270  -0.0740 113  PRO A CD  
890   N  N   . ILE A 114  ? 1.1150 1.1281 1.1581 -0.0844 0.1461  -0.0574 114  ILE A N   
891   C  CA  . ILE A 114  ? 1.1612 1.1785 1.2059 -0.0853 0.1513  -0.0562 114  ILE A CA  
892   C  C   . ILE A 114  ? 1.1351 1.1705 1.1903 -0.0775 0.1446  -0.0559 114  ILE A C   
893   O  O   . ILE A 114  ? 1.1366 1.1698 1.1887 -0.0679 0.1397  -0.0521 114  ILE A O   
894   C  CB  . ILE A 114  ? 1.1331 1.1296 1.1619 -0.0823 0.1585  -0.0501 114  ILE A CB  
895   C  CG1 . ILE A 114  ? 1.0149 0.9923 1.0325 -0.0900 0.1653  -0.0505 114  ILE A CG1 
896   C  CG2 . ILE A 114  ? 1.1210 1.1222 1.1512 -0.0826 0.1638  -0.0488 114  ILE A CG2 
897   C  CD1 . ILE A 114  ? 0.9712 0.9267 0.9718 -0.0870 0.1728  -0.0446 114  ILE A CD1 
898   N  N   . GLU A 115  ? 1.4036 1.4569 1.4712 -0.0817 0.1446  -0.0600 115  GLU A N   
899   C  CA  . GLU A 115  ? 1.3794 1.4513 1.4580 -0.0750 0.1379  -0.0606 115  GLU A CA  
900   C  C   . GLU A 115  ? 1.3265 1.3966 1.4013 -0.0696 0.1414  -0.0563 115  GLU A C   
901   O  O   . GLU A 115  ? 1.3875 1.4677 1.4685 -0.0727 0.1449  -0.0581 115  GLU A O   
902   C  CB  . GLU A 115  ? 1.4893 1.5819 1.5832 -0.0813 0.1357  -0.0673 115  GLU A CB  
903   C  CG  . GLU A 115  ? 1.5849 1.6806 1.6830 -0.0863 0.1315  -0.0721 115  GLU A CG  
904   C  CD  . GLU A 115  ? 1.5696 1.6701 1.6700 -0.0779 0.1220  -0.0715 115  GLU A CD  
905   O  OE1 . GLU A 115  ? 1.4976 1.6076 1.6027 -0.0700 0.1175  -0.0698 115  GLU A OE1 
906   O  OE2 . GLU A 115  ? 1.5322 1.6265 1.6295 -0.0793 0.1192  -0.0728 115  GLU A OE2 
907   N  N   . TRP A 116  ? 0.9117 0.9691 0.9761 -0.0613 0.1404  -0.0508 116  TRP A N   
908   C  CA  . TRP A 116  ? 0.8805 0.9367 0.9410 -0.0547 0.1422  -0.0468 116  TRP A CA  
909   C  C   . TRP A 116  ? 0.8664 0.9418 0.9388 -0.0489 0.1353  -0.0483 116  TRP A C   
910   O  O   . TRP A 116  ? 0.8786 0.9651 0.9597 -0.0476 0.1281  -0.0511 116  TRP A O   
911   C  CB  . TRP A 116  ? 0.7696 0.8082 0.8164 -0.0470 0.1423  -0.0408 116  TRP A CB  
912   C  CG  . TRP A 116  ? 0.9843 1.0024 1.0170 -0.0509 0.1507  -0.0381 116  TRP A CG  
913   C  CD1 . TRP A 116  ? 0.9286 0.9383 0.9536 -0.0529 0.1588  -0.0359 116  TRP A CD1 
914   C  CD2 . TRP A 116  ? 0.9178 0.9203 0.9415 -0.0529 0.1519  -0.0371 116  TRP A CD2 
915   N  NE1 . TRP A 116  ? 0.8405 0.8300 0.8520 -0.0560 0.1651  -0.0336 116  TRP A NE1 
916   C  CE2 . TRP A 116  ? 0.9161 0.9009 0.9266 -0.0560 0.1610  -0.0344 116  TRP A CE2 
917   C  CE3 . TRP A 116  ? 0.8170 0.8182 0.8419 -0.0521 0.1465  -0.0382 116  TRP A CE3 
918   C  CZ2 . TRP A 116  ? 0.9802 0.9461 0.9788 -0.0583 0.1646  -0.0328 116  TRP A CZ2 
919   C  CZ3 . TRP A 116  ? 0.9686 0.9516 0.9819 -0.0544 0.1501  -0.0367 116  TRP A CZ3 
920   C  CH2 . TRP A 116  ? 1.0246 0.9901 1.0250 -0.0574 0.1590  -0.0341 116  TRP A CH2 
921   N  N   . VAL A 117  ? 0.9390 1.0175 1.0107 -0.0453 0.1376  -0.0463 117  VAL A N   
922   C  CA  . VAL A 117  ? 0.9054 1.0005 0.9869 -0.0394 0.1318  -0.0474 117  VAL A CA  
923   C  C   . VAL A 117  ? 0.8802 0.9686 0.9550 -0.0288 0.1276  -0.0427 117  VAL A C   
924   O  O   . VAL A 117  ? 0.8725 0.9465 0.9356 -0.0259 0.1317  -0.0383 117  VAL A O   
925   C  CB  . VAL A 117  ? 0.9094 1.0137 0.9953 -0.0423 0.1371  -0.0489 117  VAL A CB  
926   C  CG1 . VAL A 117  ? 0.8812 1.0033 0.9775 -0.0363 0.1308  -0.0506 117  VAL A CG1 
927   C  CG2 . VAL A 117  ? 0.9847 1.0943 1.0766 -0.0536 0.1424  -0.0535 117  VAL A CG2 
928   N  N   . LYS A 118  ? 0.8955 0.9943 0.9777 -0.0230 0.1193  -0.0436 118  LYS A N   
929   C  CA  . LYS A 118  ? 0.9217 1.0159 0.9994 -0.0134 0.1146  -0.0397 118  LYS A CA  
930   C  C   . LYS A 118  ? 0.8465 0.9447 0.9235 -0.0087 0.1159  -0.0382 118  LYS A C   
931   O  O   . LYS A 118  ? 0.7467 0.8594 0.8327 -0.0093 0.1149  -0.0412 118  LYS A O   
932   C  CB  . LYS A 118  ? 0.8846 0.9883 0.9705 -0.0093 0.1058  -0.0414 118  LYS A CB  
933   C  CG  . LYS A 118  ? 0.8817 0.9754 0.9614 -0.0025 0.1017  -0.0376 118  LYS A CG  
934   C  CD  . LYS A 118  ? 0.9655 1.0677 1.0530 0.0004  0.0940  -0.0394 118  LYS A CD  
935   C  CE  . LYS A 118  ? 0.9471 1.0414 1.0299 0.0077  0.0899  -0.0357 118  LYS A CE  
936   N  NZ  . LYS A 118  ? 0.8482 0.9256 0.9197 0.0072  0.0941  -0.0322 118  LYS A NZ  
937   N  N   . VAL A 119  ? 0.7060 0.7913 0.7718 -0.0038 0.1182  -0.0337 119  VAL A N   
938   C  CA  . VAL A 119  ? 0.7344 0.8220 0.7979 0.0018  0.1189  -0.0320 119  VAL A CA  
939   C  C   . VAL A 119  ? 0.7096 0.8035 0.7771 0.0103  0.1106  -0.0314 119  VAL A C   
940   O  O   . VAL A 119  ? 0.6956 0.8012 0.7695 0.0132  0.1079  -0.0331 119  VAL A O   
941   C  CB  . VAL A 119  ? 0.6898 0.7604 0.7388 0.0033  0.1253  -0.0277 119  VAL A CB  
942   C  CG1 . VAL A 119  ? 0.5484 0.6208 0.5940 0.0098  0.1255  -0.0259 119  VAL A CG1 
943   C  CG2 . VAL A 119  ? 0.6270 0.6909 0.6719 -0.0056 0.1342  -0.0284 119  VAL A CG2 
944   N  N   . TYR A 120  ? 0.8393 0.9255 0.9031 0.0145  0.1065  -0.0291 120  TYR A N   
945   C  CA  . TYR A 120  ? 0.7852 0.8765 0.8528 0.0220  0.0988  -0.0286 120  TYR A CA  
946   C  C   . TYR A 120  ? 0.7727 0.8740 0.8507 0.0202  0.0933  -0.0318 120  TYR A C   
947   O  O   . TYR A 120  ? 0.7483 0.8446 0.8256 0.0177  0.0926  -0.0317 120  TYR A O   
948   C  CB  . TYR A 120  ? 0.7846 0.8629 0.8431 0.0275  0.0975  -0.0245 120  TYR A CB  
949   C  CG  . TYR A 120  ? 0.7882 0.8581 0.8365 0.0316  0.1012  -0.0214 120  TYR A CG  
950   C  CD1 . TYR A 120  ? 0.8200 0.8785 0.8585 0.0280  0.1089  -0.0196 120  TYR A CD1 
951   C  CD2 . TYR A 120  ? 0.7548 0.8277 0.8029 0.0391  0.0969  -0.0203 120  TYR A CD2 
952   C  CE1 . TYR A 120  ? 0.9197 0.9700 0.9480 0.0323  0.1124  -0.0166 120  TYR A CE1 
953   C  CE2 . TYR A 120  ? 0.8352 0.9004 0.8733 0.0433  0.1000  -0.0176 120  TYR A CE2 
954   C  CZ  . TYR A 120  ? 0.9159 0.9698 0.9441 0.0400  0.1077  -0.0157 120  TYR A CZ  
955   O  OH  . TYR A 120  ? 0.9161 0.9617 0.9334 0.0446  0.1109  -0.0129 120  TYR A OH  
956   N  N   . ASP A 121  ? 0.8623 0.9776 0.9495 0.0217  0.0894  -0.0346 121  ASP A N   
957   C  CA  . ASP A 121  ? 0.8054 0.9315 0.9025 0.0201  0.0846  -0.0380 121  ASP A CA  
958   C  C   . ASP A 121  ? 0.8166 0.9478 0.9177 0.0274  0.0773  -0.0377 121  ASP A C   
959   O  O   . ASP A 121  ? 0.9817 1.1146 1.0818 0.0325  0.0761  -0.0367 121  ASP A O   
960   C  CB  . ASP A 121  ? 0.8749 1.0140 0.9799 0.0152  0.0866  -0.0421 121  ASP A CB  
961   C  CG  . ASP A 121  ? 0.7692 0.9178 0.8830 0.0120  0.0828  -0.0458 121  ASP A CG  
962   O  OD1 . ASP A 121  ? 0.7923 0.9361 0.9052 0.0132  0.0792  -0.0451 121  ASP A OD1 
963   O  OD2 . ASP A 121  ? 0.8150 0.9761 0.9366 0.0086  0.0834  -0.0496 121  ASP A OD2 
964   N  N   . LEU A 122  ? 0.5742 0.7074 0.6795 0.0277  0.0725  -0.0386 122  LEU A N   
965   C  CA  . LEU A 122  ? 0.5256 0.6630 0.6349 0.0339  0.0659  -0.0385 122  LEU A CA  
966   C  C   . LEU A 122  ? 0.5691 0.7177 0.6871 0.0325  0.0619  -0.0422 122  LEU A C   
967   O  O   . LEU A 122  ? 0.6707 0.8203 0.7904 0.0273  0.0632  -0.0441 122  LEU A O   
968   C  CB  . LEU A 122  ? 0.6227 0.7493 0.7270 0.0371  0.0637  -0.0353 122  LEU A CB  
969   C  CG  . LEU A 122  ? 0.5905 0.7089 0.6878 0.0418  0.0647  -0.0318 122  LEU A CG  
970   C  CD1 . LEU A 122  ? 0.5645 0.6733 0.6578 0.0445  0.0629  -0.0289 122  LEU A CD1 
971   C  CD2 . LEU A 122  ? 0.5965 0.7217 0.6968 0.0472  0.0612  -0.0323 122  LEU A CD2 
972   N  N   . PRO A 123  ? 1.0528 1.2094 1.1759 0.0374  0.0571  -0.0434 123  PRO A N   
973   C  CA  . PRO A 123  ? 1.1275 1.2953 1.2585 0.0369  0.0533  -0.0470 123  PRO A CA  
974   C  C   . PRO A 123  ? 1.1469 1.3115 1.2784 0.0375  0.0495  -0.0468 123  PRO A C   
975   O  O   . PRO A 123  ? 1.2769 1.4485 1.4133 0.0403  0.0448  -0.0486 123  PRO A O   
976   C  CB  . PRO A 123  ? 0.9806 1.1559 1.1151 0.0427  0.0498  -0.0477 123  PRO A CB  
977   C  CG  . PRO A 123  ? 0.9569 1.1272 1.0861 0.0445  0.0530  -0.0454 123  PRO A CG  
978   C  CD  . PRO A 123  ? 1.0468 1.2039 1.1686 0.0432  0.0555  -0.0420 123  PRO A CD  
979   N  N   . ASN A 124  ? 0.7871 0.9409 0.9131 0.0352  0.0515  -0.0445 124  ASN A N   
980   C  CA  . ASN A 124  ? 0.8122 0.9623 0.9380 0.0347  0.0490  -0.0445 124  ASN A CA  
981   C  C   . ASN A 124  ? 0.8226 0.9724 0.9499 0.0407  0.0436  -0.0433 124  ASN A C   
982   O  O   . ASN A 124  ? 0.7084 0.8537 0.8346 0.0409  0.0417  -0.0427 124  ASN A O   
983   C  CB  . ASN A 124  ? 0.7760 0.9344 0.9066 0.0300  0.0487  -0.0485 124  ASN A CB  
984   C  CG  . ASN A 124  ? 0.9182 1.0733 1.0462 0.0228  0.0542  -0.0494 124  ASN A CG  
985   O  OD1 . ASN A 124  ? 1.0005 1.1645 1.1332 0.0184  0.0558  -0.0529 124  ASN A OD1 
986   N  ND2 . ASN A 124  ? 0.7838 0.9258 0.9043 0.0216  0.0574  -0.0462 124  ASN A ND2 
987   N  N   . PHE A 125  ? 0.7685 0.9224 0.8980 0.0455  0.0411  -0.0431 125  PHE A N   
988   C  CA  . PHE A 125  ? 0.6858 0.8375 0.8159 0.0509  0.0366  -0.0416 125  PHE A CA  
989   C  C   . PHE A 125  ? 0.7636 0.9078 0.8897 0.0541  0.0372  -0.0383 125  PHE A C   
990   O  O   . PHE A 125  ? 0.7858 0.9302 0.9132 0.0588  0.0338  -0.0376 125  PHE A O   
991   C  CB  . PHE A 125  ? 0.5821 0.7437 0.7177 0.0544  0.0326  -0.0442 125  PHE A CB  
992   C  CG  . PHE A 125  ? 0.6846 0.8538 0.8223 0.0549  0.0338  -0.0458 125  PHE A CG  
993   C  CD1 . PHE A 125  ? 0.6269 0.7926 0.7617 0.0572  0.0351  -0.0439 125  PHE A CD1 
994   C  CD2 . PHE A 125  ? 0.6891 0.8695 0.8318 0.0534  0.0335  -0.0494 125  PHE A CD2 
995   C  CE1 . PHE A 125  ? 0.5157 0.6880 0.6518 0.0579  0.0364  -0.0454 125  PHE A CE1 
996   C  CE2 . PHE A 125  ? 0.6594 0.8472 0.8042 0.0541  0.0349  -0.0509 125  PHE A CE2 
997   C  CZ  . PHE A 125  ? 0.5325 0.7159 0.6738 0.0563  0.0365  -0.0488 125  PHE A CZ  
998   N  N   . VAL A 126  ? 0.9882 1.1256 1.1092 0.0518  0.0415  -0.0365 126  VAL A N   
999   C  CA  . VAL A 126  ? 1.0434 1.1743 1.1600 0.0549  0.0423  -0.0336 126  VAL A CA  
1000  C  C   . VAL A 126  ? 1.0166 1.1373 1.1288 0.0552  0.0431  -0.0305 126  VAL A C   
1001  O  O   . VAL A 126  ? 1.1251 1.2421 1.2365 0.0593  0.0410  -0.0285 126  VAL A O   
1002  C  CB  . VAL A 126  ? 1.0149 1.1457 1.1281 0.0530  0.0468  -0.0335 126  VAL A CB  
1003  C  CG1 . VAL A 126  ? 0.8966 1.0194 1.0038 0.0563  0.0478  -0.0304 126  VAL A CG1 
1004  C  CG2 . VAL A 126  ? 1.0571 1.1983 1.1748 0.0539  0.0458  -0.0363 126  VAL A CG2 
1005  N  N   . TYR A 127  ? 0.6407 0.7568 0.7501 0.0510  0.0460  -0.0304 127  TYR A N   
1006  C  CA  . TYR A 127  ? 0.6887 0.7950 0.7937 0.0512  0.0471  -0.0276 127  TYR A CA  
1007  C  C   . TYR A 127  ? 0.6291 0.7281 0.7285 0.0541  0.0489  -0.0245 127  TYR A C   
1008  O  O   . TYR A 127  ? 0.6548 0.7524 0.7551 0.0585  0.0461  -0.0229 127  TYR A O   
1009  C  CB  . TYR A 127  ? 0.6438 0.7505 0.7522 0.0539  0.0429  -0.0273 127  TYR A CB  
1010  C  CG  . TYR A 127  ? 0.6760 0.7881 0.7882 0.0514  0.0413  -0.0301 127  TYR A CG  
1011  C  CD1 . TYR A 127  ? 0.6934 0.8023 0.8030 0.0469  0.0437  -0.0308 127  TYR A CD1 
1012  C  CD2 . TYR A 127  ? 0.6746 0.7948 0.7924 0.0537  0.0372  -0.0321 127  TYR A CD2 
1013  C  CE1 . TYR A 127  ? 0.6144 0.7286 0.7272 0.0450  0.0418  -0.0336 127  TYR A CE1 
1014  C  CE2 . TYR A 127  ? 0.6749 0.8001 0.7956 0.0521  0.0354  -0.0346 127  TYR A CE2 
1015  C  CZ  . TYR A 127  ? 0.6700 0.7926 0.7884 0.0478  0.0376  -0.0355 127  TYR A CZ  
1016  O  OH  . TYR A 127  ? 0.7904 0.9184 0.9115 0.0464  0.0355  -0.0383 127  TYR A OH  
1017  N  N   . PHE A 128  ? 0.5329 0.6273 0.6267 0.0516  0.0536  -0.0239 128  PHE A N   
1018  C  CA  . PHE A 128  ? 0.6135 0.6999 0.7005 0.0545  0.0558  -0.0209 128  PHE A CA  
1019  C  C   . PHE A 128  ? 0.6694 0.7455 0.7507 0.0539  0.0580  -0.0184 128  PHE A C   
1020  O  O   . PHE A 128  ? 0.7216 0.7955 0.8025 0.0499  0.0596  -0.0192 128  PHE A O   
1021  C  CB  . PHE A 128  ? 0.6838 0.7693 0.7662 0.0525  0.0602  -0.0211 128  PHE A CB  
1022  C  CG  . PHE A 128  ? 0.6677 0.7447 0.7421 0.0561  0.0624  -0.0180 128  PHE A CG  
1023  C  CD1 . PHE A 128  ? 0.6292 0.7085 0.7042 0.0617  0.0591  -0.0172 128  PHE A CD1 
1024  C  CD2 . PHE A 128  ? 0.6181 0.6846 0.6840 0.0540  0.0675  -0.0160 128  PHE A CD2 
1025  C  CE1 . PHE A 128  ? 0.6089 0.6808 0.6762 0.0655  0.0607  -0.0146 128  PHE A CE1 
1026  C  CE2 . PHE A 128  ? 0.6538 0.7122 0.7116 0.0579  0.0694  -0.0131 128  PHE A CE2 
1027  C  CZ  . PHE A 128  ? 0.6559 0.7173 0.7145 0.0638  0.0659  -0.0124 128  PHE A CZ  
1028  N  N   . ASN A 129  ? 0.7612 0.8312 0.8382 0.0584  0.0581  -0.0155 129  ASN A N   
1029  C  CA  . ASN A 129  ? 0.6961 0.7564 0.7675 0.0592  0.0600  -0.0129 129  ASN A CA  
1030  C  C   . ASN A 129  ? 0.6854 0.7375 0.7480 0.0618  0.0633  -0.0103 129  ASN A C   
1031  O  O   . ASN A 129  ? 0.7323 0.7858 0.7949 0.0669  0.0610  -0.0092 129  ASN A O   
1032  C  CB  . ASN A 129  ? 0.7308 0.7926 0.8070 0.0630  0.0558  -0.0119 129  ASN A CB  
1033  C  CG  . ASN A 129  ? 0.7100 0.7633 0.7821 0.0628  0.0577  -0.0099 129  ASN A CG  
1034  O  OD1 . ASN A 129  ? 0.8044 0.8488 0.8684 0.0634  0.0614  -0.0078 129  ASN A OD1 
1035  N  ND2 . ASN A 129  ? 0.6253 0.6808 0.7022 0.0623  0.0554  -0.0105 129  ASN A ND2 
1036  N  N   . HIS A 130  ? 0.4870 0.5302 0.5417 0.0584  0.0687  -0.0094 130  HIS A N   
1037  C  CA  . HIS A 130  ? 0.4745 0.5084 0.5193 0.0611  0.0724  -0.0067 130  HIS A CA  
1038  C  C   . HIS A 130  ? 0.4408 0.4684 0.4820 0.0667  0.0713  -0.0037 130  HIS A C   
1039  O  O   . HIS A 130  ? 0.4881 0.5116 0.5235 0.0715  0.0718  -0.0017 130  HIS A O   
1040  C  CB  . HIS A 130  ? 0.5186 0.5437 0.5555 0.0556  0.0788  -0.0066 130  HIS A CB  
1041  C  CG  . HIS A 130  ? 0.5580 0.5876 0.5958 0.0513  0.0814  -0.0088 130  HIS A CG  
1042  N  ND1 . HIS A 130  ? 0.6138 0.6518 0.6590 0.0457  0.0808  -0.0122 130  HIS A ND1 
1043  C  CD2 . HIS A 130  ? 0.6195 0.6466 0.6515 0.0520  0.0847  -0.0080 130  HIS A CD2 
1044  C  CE1 . HIS A 130  ? 0.7524 0.7935 0.7971 0.0429  0.0837  -0.0135 130  HIS A CE1 
1045  N  NE2 . HIS A 130  ? 0.7136 0.7479 0.7502 0.0466  0.0863  -0.0110 130  HIS A NE2 
1046  N  N   . SER A 131  ? 0.6042 0.6310 0.6484 0.0663  0.0698  -0.0035 131  SER A N   
1047  C  CA  . SER A 131  ? 0.5907 0.6111 0.6311 0.0712  0.0697  -0.0006 131  SER A CA  
1048  C  C   . SER A 131  ? 0.6494 0.6760 0.6946 0.0775  0.0649  0.0000  131  SER A C   
1049  O  O   . SER A 131  ? 0.6293 0.6512 0.6691 0.0827  0.0653  0.0023  131  SER A O   
1050  C  CB  . SER A 131  ? 0.5709 0.5894 0.6138 0.0692  0.0694  -0.0007 131  SER A CB  
1051  O  OG  . SER A 131  ? 0.6068 0.6201 0.6469 0.0742  0.0692  0.0020  131  SER A OG  
1052  N  N   . ILE A 132  ? 0.8135 0.8507 0.8688 0.0773  0.0603  -0.0021 132  ILE A N   
1053  C  CA  . ILE A 132  ? 0.7838 0.8272 0.8444 0.0827  0.0556  -0.0019 132  ILE A CA  
1054  C  C   . ILE A 132  ? 0.7568 0.8006 0.8133 0.0859  0.0553  -0.0017 132  ILE A C   
1055  O  O   . ILE A 132  ? 0.8006 0.8449 0.8565 0.0914  0.0530  -0.0006 132  ILE A O   
1056  C  CB  . ILE A 132  ? 0.7242 0.7775 0.7958 0.0814  0.0510  -0.0042 132  ILE A CB  
1057  C  CG1 . ILE A 132  ? 0.7040 0.7635 0.7813 0.0863  0.0462  -0.0044 132  ILE A CG1 
1058  C  CG2 . ILE A 132  ? 0.7441 0.8024 0.8178 0.0771  0.0512  -0.0069 132  ILE A CG2 
1059  C  CD1 . ILE A 132  ? 0.6922 0.7495 0.7704 0.0901  0.0453  -0.0023 132  ILE A CD1 
1060  N  N   . HIS A 133  ? 0.3956 0.4392 0.4488 0.0827  0.0579  -0.0029 133  HIS A N   
1061  C  CA  . HIS A 133  ? 0.3590 0.4023 0.4073 0.0859  0.0581  -0.0026 133  HIS A CA  
1062  C  C   . HIS A 133  ? 0.4886 0.5212 0.5255 0.0894  0.0617  0.0004  133  HIS A C   
1063  O  O   . HIS A 133  ? 0.4416 0.4739 0.4753 0.0952  0.0599  0.0014  133  HIS A O   
1064  C  CB  . HIS A 133  ? 0.3553 0.4015 0.4034 0.0815  0.0604  -0.0046 133  HIS A CB  
1065  C  CG  . HIS A 133  ? 0.4051 0.4627 0.4632 0.0803  0.0560  -0.0076 133  HIS A CG  
1066  N  ND1 . HIS A 133  ? 0.4784 0.5413 0.5449 0.0780  0.0533  -0.0090 133  HIS A ND1 
1067  C  CD2 . HIS A 133  ? 0.5291 0.5931 0.5895 0.0817  0.0539  -0.0093 133  HIS A CD2 
1068  C  CE1 . HIS A 133  ? 0.4938 0.5656 0.5672 0.0780  0.0498  -0.0115 133  HIS A CE1 
1069  N  NE2 . HIS A 133  ? 0.4258 0.4986 0.4959 0.0802  0.0501  -0.0117 133  HIS A NE2 
1070  N  N   . VAL A 134  ? 0.6811 0.7044 0.7113 0.0863  0.0668  0.0018  134  VAL A N   
1071  C  CA  . VAL A 134  ? 0.5903 0.6018 0.6084 0.0897  0.0708  0.0048  134  VAL A CA  
1072  C  C   . VAL A 134  ? 0.6178 0.6285 0.6362 0.0962  0.0677  0.0067  134  VAL A C   
1073  O  O   . VAL A 134  ? 0.5523 0.5589 0.5638 0.1022  0.0677  0.0086  134  VAL A O   
1074  C  CB  . VAL A 134  ? 0.5825 0.5838 0.5934 0.0842  0.0770  0.0056  134  VAL A CB  
1075  C  CG1 . VAL A 134  ? 0.7650 0.7534 0.7643 0.0884  0.0805  0.0090  134  VAL A CG1 
1076  C  CG2 . VAL A 134  ? 0.5559 0.5559 0.5633 0.0791  0.0811  0.0043  134  VAL A CG2 
1077  N  N   . ASN A 135  ? 0.8040 0.8189 0.8304 0.0953  0.0652  0.0063  135  ASN A N   
1078  C  CA  . ASN A 135  ? 0.7836 0.7986 0.8115 0.1010  0.0627  0.0079  135  ASN A CA  
1079  C  C   . ASN A 135  ? 0.6675 0.6917 0.7017 0.1063  0.0570  0.0071  135  ASN A C   
1080  O  O   . ASN A 135  ? 0.6300 0.6546 0.6646 0.1118  0.0549  0.0084  135  ASN A O   
1081  C  CB  . ASN A 135  ? 0.7716 0.7886 0.8066 0.0983  0.0619  0.0076  135  ASN A CB  
1082  C  CG  . ASN A 135  ? 0.6546 0.6603 0.6814 0.0956  0.0673  0.0092  135  ASN A CG  
1083  O  OD1 . ASN A 135  ? 0.5181 0.5153 0.5367 0.0996  0.0698  0.0118  135  ASN A OD1 
1084  N  ND2 . ASN A 135  ? 0.7407 0.7462 0.7695 0.0890  0.0690  0.0076  135  ASN A ND2 
1085  N  N   . LYS A 136  ? 0.4521 0.4837 0.4910 0.1049  0.0543  0.0047  136  LYS A N   
1086  C  CA  . LYS A 136  ? 0.5060 0.5461 0.5505 0.1095  0.0488  0.0035  136  LYS A CA  
1087  C  C   . LYS A 136  ? 0.5789 0.6163 0.6149 0.1134  0.0492  0.0038  136  LYS A C   
1088  O  O   . LYS A 136  ? 0.6154 0.6599 0.6554 0.1160  0.0448  0.0021  136  LYS A O   
1089  C  CB  . LYS A 136  ? 0.6321 0.6824 0.6880 0.1059  0.0449  0.0005  136  LYS A CB  
1090  C  CG  . LYS A 136  ? 0.5121 0.5663 0.5773 0.1038  0.0432  0.0001  136  LYS A CG  
1091  C  CD  . LYS A 136  ? 0.4160 0.4757 0.4876 0.1086  0.0387  0.0001  136  LYS A CD  
1092  C  CE  . LYS A 136  ? 0.3973 0.4598 0.4772 0.1066  0.0379  0.0001  136  LYS A CE  
1093  N  NZ  . LYS A 136  ? 0.4262 0.4971 0.5159 0.1093  0.0328  -0.0011 136  LYS A NZ  
1094  N  N   . GLY A 137  ? 0.5514 0.5780 0.5752 0.1139  0.0545  0.0061  137  GLY A N   
1095  C  CA  . GLY A 137  ? 0.5538 0.5762 0.5679 0.1182  0.0555  0.0069  137  GLY A CA  
1096  C  C   . GLY A 137  ? 0.6155 0.6404 0.6289 0.1149  0.0566  0.0051  137  GLY A C   
1097  O  O   . GLY A 137  ? 0.6181 0.6474 0.6312 0.1187  0.0534  0.0040  137  GLY A O   
1098  N  N   . ILE A 138  ? 0.9746 0.9969 0.9876 0.1080  0.0610  0.0046  138  ILE A N   
1099  C  CA  . ILE A 138  ? 0.8758 0.9004 0.8881 0.1044  0.0630  0.0030  138  ILE A CA  
1100  C  C   . ILE A 138  ? 0.9399 0.9536 0.9420 0.1003  0.0707  0.0046  138  ILE A C   
1101  O  O   . ILE A 138  ? 1.0205 1.0303 1.0233 0.0956  0.0736  0.0050  138  ILE A O   
1102  C  CB  . ILE A 138  ? 0.8329 0.8684 0.8579 0.0992  0.0601  -0.0002 138  ILE A CB  
1103  C  CG1 . ILE A 138  ? 0.8212 0.8663 0.8559 0.1029  0.0529  -0.0018 138  ILE A CG1 
1104  C  CG2 . ILE A 138  ? 0.8412 0.8794 0.8653 0.0959  0.0625  -0.0019 138  ILE A CG2 
1105  C  CD1 . ILE A 138  ? 0.8165 0.8658 0.8500 0.1076  0.0496  -0.0029 138  ILE A CD1 
1106  N  N   . GLY A 139  ? 0.8500 0.8583 0.8424 0.1020  0.0741  0.0055  139  GLY A N   
1107  C  CA  . GLY A 139  ? 0.8680 0.8646 0.8496 0.0984  0.0819  0.0073  139  GLY A CA  
1108  C  C   . GLY A 139  ? 0.8773 0.8776 0.8621 0.0909  0.0855  0.0051  139  GLY A C   
1109  O  O   . GLY A 139  ? 0.8864 0.8978 0.8801 0.0897  0.0821  0.0025  139  GLY A O   
1110  N  N   . CYS A 140  ? 0.8425 0.8329 0.8198 0.0858  0.0926  0.0062  140  CYS A N   
1111  C  CA  . CYS A 140  ? 0.8644 0.8578 0.8442 0.0784  0.0969  0.0041  140  CYS A CA  
1112  C  C   . CYS A 140  ? 0.9865 0.9810 0.9616 0.0804  0.0988  0.0041  140  CYS A C   
1113  O  O   . CYS A 140  ? 0.9578 0.9594 0.9383 0.0754  0.1005  0.0017  140  CYS A O   
1114  C  CB  . CYS A 140  ? 0.8280 0.8098 0.8004 0.0722  0.1044  0.0053  140  CYS A CB  
1115  S  SG  . CYS A 140  ? 0.8643 0.8401 0.8372 0.0714  0.1034  0.0063  140  CYS A SG  
1116  N  N   . SER A 141  ? 1.2687 1.2565 1.2337 0.0880  0.0985  0.0065  141  SER A N   
1117  C  CA  . SER A 141  ? 1.1290 1.1170 1.0882 0.0907  0.1003  0.0066  141  SER A CA  
1118  C  C   . SER A 141  ? 1.2272 1.2302 1.1979 0.0918  0.0941  0.0034  141  SER A C   
1119  O  O   . SER A 141  ? 1.2407 1.2480 1.2121 0.0897  0.0964  0.0020  141  SER A O   
1120  C  CB  . SER A 141  ? 1.2817 1.2594 1.2273 0.0994  0.1004  0.0098  141  SER A CB  
1121  O  OG  . SER A 141  ? 1.5330 1.5102 1.4720 0.1026  0.1020  0.0099  141  SER A OG  
1122  N  N   . THR A 142  ? 0.8649 0.8759 0.8447 0.0950  0.0865  0.0023  142  THR A N   
1123  C  CA  . THR A 142  ? 0.8066 0.8309 0.7969 0.0962  0.0804  -0.0007 142  THR A CA  
1124  C  C   . THR A 142  ? 0.8026 0.8365 0.8044 0.0888  0.0806  -0.0037 142  THR A C   
1125  O  O   . THR A 142  ? 0.8844 0.9288 0.8942 0.0894  0.0765  -0.0063 142  THR A O   
1126  C  CB  . THR A 142  ? 0.6290 0.6582 0.6254 0.1015  0.0726  -0.0011 142  THR A CB  
1127  O  OG1 . THR A 142  ? 0.6825 0.7137 0.6869 0.0976  0.0713  -0.0015 142  THR A OG1 
1128  C  CG2 . THR A 142  ? 0.6935 0.7138 0.6791 0.1090  0.0721  0.0017  142  THR A CG2 
1129  N  N   . CYS A 143  ? 0.6682 0.6987 0.6708 0.0822  0.0851  -0.0036 143  CYS A N   
1130  C  CA  . CYS A 143  ? 0.7500 0.7899 0.7636 0.0754  0.0850  -0.0066 143  CYS A CA  
1131  C  C   . CYS A 143  ? 0.7015 0.7386 0.7116 0.0688  0.0926  -0.0070 143  CYS A C   
1132  O  O   . CYS A 143  ? 0.6889 0.7342 0.7035 0.0667  0.0934  -0.0092 143  CYS A O   
1133  C  CB  . CYS A 143  ? 0.8413 0.8817 0.8611 0.0730  0.0823  -0.0068 143  CYS A CB  
1134  S  SG  . CYS A 143  ? 0.6851 0.7349 0.7152 0.0780  0.0730  -0.0080 143  CYS A SG  
1135  N  N   . HIS A 144  ? 0.8271 0.8529 0.8294 0.0654  0.0984  -0.0051 144  HIS A N   
1136  C  CA  . HIS A 144  ? 0.9053 0.9276 0.9043 0.0583  0.1061  -0.0056 144  HIS A CA  
1137  C  C   . HIS A 144  ? 0.8884 0.9015 0.8747 0.0607  0.1121  -0.0033 144  HIS A C   
1138  O  O   . HIS A 144  ? 0.8797 0.8898 0.8630 0.0548  0.1192  -0.0036 144  HIS A O   
1139  C  CB  . HIS A 144  ? 0.8512 0.8649 0.8476 0.0528  0.1098  -0.0049 144  HIS A CB  
1140  C  CG  . HIS A 144  ? 0.7350 0.7568 0.7428 0.0499  0.1048  -0.0072 144  HIS A CG  
1141  N  ND1 . HIS A 144  ? 0.7614 0.7976 0.7818 0.0469  0.1014  -0.0108 144  HIS A ND1 
1142  C  CD2 . HIS A 144  ? 0.8865 0.9036 0.8945 0.0500  0.1028  -0.0063 144  HIS A CD2 
1143  C  CE1 . HIS A 144  ? 1.0171 1.0568 1.0444 0.0452  0.0975  -0.0120 144  HIS A CE1 
1144  N  NE2 . HIS A 144  ? 1.0099 1.0382 1.0300 0.0470  0.0984  -0.0094 144  HIS A NE2 
1145  N  N   . GLY A 145  ? 0.6389 0.6475 0.6178 0.0690  0.1095  -0.0010 145  GLY A N   
1146  C  CA  . GLY A 145  ? 0.7705 0.7698 0.7363 0.0722  0.1148  0.0014  145  GLY A CA  
1147  C  C   . GLY A 145  ? 0.6934 0.6754 0.6452 0.0721  0.1211  0.0049  145  GLY A C   
1148  O  O   . GLY A 145  ? 0.5699 0.5463 0.5207 0.0724  0.1197  0.0061  145  GLY A O   
1149  N  N   . GLN A 146  ? 0.9864 0.9592 0.9266 0.0718  0.1284  0.0067  146  GLN A N   
1150  C  CA  . GLN A 146  ? 0.9798 0.9344 0.9047 0.0719  0.1354  0.0102  146  GLN A CA  
1151  C  C   . GLN A 146  ? 1.0143 0.9653 0.9410 0.0612  0.1425  0.0092  146  GLN A C   
1152  O  O   . GLN A 146  ? 1.0317 0.9768 0.9523 0.0564  0.1506  0.0095  146  GLN A O   
1153  C  CB  . GLN A 146  ? 0.9288 0.8741 0.8392 0.0772  0.1400  0.0129  146  GLN A CB  
1154  C  CG  . GLN A 146  ? 1.0118 0.9591 0.9186 0.0882  0.1330  0.0140  146  GLN A CG  
1155  C  CD  . GLN A 146  ? 1.1429 1.0815 1.0433 0.0945  0.1297  0.0165  146  GLN A CD  
1156  O  OE1 . GLN A 146  ? 1.2070 1.1317 1.0975 0.0930  0.1351  0.0190  146  GLN A OE1 
1157  N  NE2 . GLN A 146  ? 1.1869 1.1336 1.0926 0.1016  0.1208  0.0158  146  GLN A NE2 
1158  N  N   . VAL A 147  ? 1.0853 1.0398 1.0206 0.0573  0.1393  0.0076  147  VAL A N   
1159  C  CA  . VAL A 147  ? 1.1147 1.0672 1.0532 0.0470  0.1448  0.0059  147  VAL A CA  
1160  C  C   . VAL A 147  ? 1.1373 1.0698 1.0597 0.0452  0.1535  0.0091  147  VAL A C   
1161  O  O   . VAL A 147  ? 1.1502 1.0785 1.0717 0.0363  0.1605  0.0080  147  VAL A O   
1162  C  CB  . VAL A 147  ? 1.1116 1.0718 1.0618 0.0443  0.1388  0.0037  147  VAL A CB  
1163  C  CG1 . VAL A 147  ? 1.0364 0.9982 0.9923 0.0334  0.1433  0.0008  147  VAL A CG1 
1164  C  CG2 . VAL A 147  ? 1.1583 1.1358 1.1220 0.0480  0.1299  0.0013  147  VAL A CG2 
1165  N  N   . ASN A 148  ? 0.9568 0.8767 0.8661 0.0534  0.1532  0.0130  148  ASN A N   
1166  C  CA  . ASN A 148  ? 0.9565 0.8559 0.8491 0.0528  0.1613  0.0164  148  ASN A CA  
1167  C  C   . ASN A 148  ? 1.1295 1.0212 1.0128 0.0490  0.1705  0.0173  148  ASN A C   
1168  O  O   . ASN A 148  ? 1.2452 1.1205 1.1164 0.0453  0.1788  0.0193  148  ASN A O   
1169  C  CB  . ASN A 148  ? 1.0184 0.9074 0.8990 0.0638  0.1584  0.0203  148  ASN A CB  
1170  C  CG  . ASN A 148  ? 1.0876 0.9838 0.9678 0.0729  0.1533  0.0209  148  ASN A CG  
1171  O  OD1 . ASN A 148  ? 1.0105 0.9226 0.9040 0.0750  0.1452  0.0185  148  ASN A OD1 
1172  N  ND2 . ASN A 148  ? 1.2017 1.0855 1.0661 0.0784  0.1579  0.0242  148  ASN A ND2 
1173  N  N   . ASN A 149  ? 0.9749 0.8776 0.8634 0.0499  0.1697  0.0159  149  ASN A N   
1174  C  CA  . ASN A 149  ? 1.0047 0.9009 0.8845 0.0471  0.1786  0.0169  149  ASN A CA  
1175  C  C   . ASN A 149  ? 0.9371 0.8477 0.8309 0.0375  0.1809  0.0127  149  ASN A C   
1176  O  O   . ASN A 149  ? 1.0205 0.9319 0.9113 0.0363  0.1862  0.0128  149  ASN A O   
1177  C  CB  . ASN A 149  ? 1.0339 0.9282 0.9045 0.0574  0.1770  0.0194  149  ASN A CB  
1178  C  CG  . ASN A 149  ? 1.0864 0.9631 0.9387 0.0579  0.1872  0.0228  149  ASN A CG  
1179  O  OD1 . ASN A 149  ? 1.0804 0.9393 0.9196 0.0570  0.1931  0.0257  149  ASN A OD1 
1180  N  ND2 . ASN A 149  ? 1.1072 0.9882 0.9578 0.0595  0.1896  0.0227  149  ASN A ND2 
1181  N  N   . MET A 150  ? 1.1226 1.0448 1.0313 0.0309  0.1771  0.0090  150  MET A N   
1182  C  CA  . MET A 150  ? 1.1793 1.1166 1.1021 0.0222  0.1785  0.0047  150  MET A CA  
1183  C  C   . MET A 150  ? 1.2447 1.1747 1.1666 0.0110  0.1866  0.0034  150  MET A C   
1184  O  O   . MET A 150  ? 1.1707 1.0988 1.0959 0.0074  0.1844  0.0023  150  MET A O   
1185  C  CB  . MET A 150  ? 1.1505 1.1070 1.0910 0.0226  0.1686  0.0010  150  MET A CB  
1186  C  CG  . MET A 150  ? 1.1431 1.1063 1.0853 0.0333  0.1598  0.0020  150  MET A CG  
1187  S  SD  . MET A 150  ? 1.0991 1.0831 1.0615 0.0329  0.1490  -0.0023 150  MET A SD  
1188  C  CE  . MET A 150  ? 1.1322 1.1269 1.0973 0.0421  0.1430  -0.0024 150  MET A CE  
1189  N  N   . PRO A 151  ? 1.3095 1.2352 1.2269 0.0050  0.1959  0.0034  151  PRO A N   
1190  C  CA  . PRO A 151  ? 1.1774 1.0997 1.0975 -0.0071 0.2030  0.0010  151  PRO A CA  
1191  C  C   . PRO A 151  ? 1.0632 1.0057 1.0033 -0.0141 0.1979  -0.0045 151  PRO A C   
1192  O  O   . PRO A 151  ? 1.1603 1.1011 1.1043 -0.0220 0.1991  -0.0068 151  PRO A O   
1193  C  CB  . PRO A 151  ? 1.2238 1.1401 1.1363 -0.0111 0.2136  0.0021  151  PRO A CB  
1194  C  CG  . PRO A 151  ? 1.2851 1.2094 1.1975 -0.0022 0.2103  0.0033  151  PRO A CG  
1195  C  CD  . PRO A 151  ? 1.2885 1.2113 1.1976 0.0089  0.2009  0.0055  151  PRO A CD  
1196  N  N   . VAL A 152  ? 0.7390 0.7003 0.6915 -0.0111 0.1921  -0.0069 152  VAL A N   
1197  C  CA  . VAL A 152  ? 0.7571 0.7384 0.7283 -0.0153 0.1855  -0.0119 152  VAL A CA  
1198  C  C   . VAL A 152  ? 0.8617 0.8535 0.8388 -0.0054 0.1749  -0.0117 152  VAL A C   
1199  O  O   . VAL A 152  ? 0.7349 0.7280 0.7081 0.0019  0.1737  -0.0098 152  VAL A O   
1200  C  CB  . VAL A 152  ? 0.5903 0.5861 0.5725 -0.0227 0.1898  -0.0158 152  VAL A CB  
1201  C  CG1 . VAL A 152  ? 0.7328 0.7477 0.7333 -0.0275 0.1834  -0.0211 152  VAL A CG1 
1202  C  CG2 . VAL A 152  ? 0.5627 0.5467 0.5374 -0.0319 0.2015  -0.0154 152  VAL A CG2 
1203  N  N   . VAL A 153  ? 0.9984 0.9972 0.9845 -0.0054 0.1673  -0.0137 153  VAL A N   
1204  C  CA  . VAL A 153  ? 0.8376 0.8444 0.8287 0.0035  0.1574  -0.0133 153  VAL A CA  
1205  C  C   . VAL A 153  ? 0.7293 0.7559 0.7339 0.0041  0.1533  -0.0167 153  VAL A C   
1206  O  O   . VAL A 153  ? 0.7838 0.8223 0.7996 -0.0032 0.1542  -0.0207 153  VAL A O   
1207  C  CB  . VAL A 153  ? 0.7253 0.7318 0.7207 0.0032  0.1515  -0.0141 153  VAL A CB  
1208  C  CG1 . VAL A 153  ? 0.6150 0.6290 0.6153 0.0122  0.1418  -0.0135 153  VAL A CG1 
1209  C  CG2 . VAL A 153  ? 0.7686 0.7551 0.7502 0.0024  0.1561  -0.0108 153  VAL A CG2 
1210  N  N   . TRP A 154  ? 0.7574 0.7876 0.7609 0.0130  0.1486  -0.0152 154  TRP A N   
1211  C  CA  . TRP A 154  ? 0.7573 0.8051 0.7723 0.0151  0.1438  -0.0181 154  TRP A CA  
1212  C  C   . TRP A 154  ? 0.7513 0.8038 0.7699 0.0235  0.1339  -0.0177 154  TRP A C   
1213  O  O   . TRP A 154  ? 0.7139 0.7556 0.7242 0.0289  0.1316  -0.0146 154  TRP A O   
1214  C  CB  . TRP A 154  ? 0.6960 0.7443 0.7060 0.0173  0.1489  -0.0172 154  TRP A CB  
1215  C  CG  . TRP A 154  ? 0.8181 0.8549 0.8148 0.0265  0.1483  -0.0130 154  TRP A CG  
1216  C  CD1 . TRP A 154  ? 0.8807 0.9218 0.8781 0.0354  0.1407  -0.0125 154  TRP A CD1 
1217  C  CD2 . TRP A 154  ? 0.8341 0.8531 0.8144 0.0277  0.1555  -0.0090 154  TRP A CD2 
1218  N  NE1 . TRP A 154  ? 0.8852 0.9131 0.8681 0.0422  0.1424  -0.0085 154  TRP A NE1 
1219  C  CE2 . TRP A 154  ? 0.8100 0.8240 0.7819 0.0380  0.1514  -0.0062 154  TRP A CE2 
1220  C  CE3 . TRP A 154  ? 0.7438 0.7500 0.7153 0.0212  0.1651  -0.0076 154  TRP A CE3 
1221  C  CZ2 . TRP A 154  ? 0.7572 0.7544 0.7120 0.0424  0.1563  -0.0020 154  TRP A CZ2 
1222  C  CZ3 . TRP A 154  ? 0.7812 0.7698 0.7353 0.0255  0.1703  -0.0031 154  TRP A CZ3 
1223  C  CH2 . TRP A 154  ? 0.8323 0.8167 0.7782 0.0363  0.1658  -0.0004 154  TRP A CH2 
1224  N  N   . GLN A 155  ? 0.9365 1.0052 0.9675 0.0245  0.1283  -0.0209 155  GLN A N   
1225  C  CA  . GLN A 155  ? 0.9522 1.0262 0.9875 0.0318  0.1191  -0.0210 155  GLN A CA  
1226  C  C   . GLN A 155  ? 0.9205 0.9916 0.9485 0.0400  0.1180  -0.0187 155  GLN A C   
1227  O  O   . GLN A 155  ? 0.9466 1.0243 0.9759 0.0408  0.1199  -0.0199 155  GLN A O   
1228  C  CB  . GLN A 155  ? 0.9984 1.0898 1.0487 0.0301  0.1138  -0.0252 155  GLN A CB  
1229  C  CG  . GLN A 155  ? 0.9737 1.0698 1.0291 0.0363  0.1046  -0.0254 155  GLN A CG  
1230  C  CD  . GLN A 155  ? 1.0330 1.1427 1.1016 0.0334  0.0999  -0.0293 155  GLN A CD  
1231  O  OE1 . GLN A 155  ? 1.0838 1.1994 1.1580 0.0265  0.1032  -0.0319 155  GLN A OE1 
1232  N  NE2 . GLN A 155  ? 0.9551 1.0699 1.0287 0.0387  0.0923  -0.0298 155  GLN A NE2 
1233  N  N   . GLN A 156  ? 0.7872 0.8487 0.8076 0.0463  0.1147  -0.0157 156  GLN A N   
1234  C  CA  . GLN A 156  ? 0.9241 0.9810 0.9357 0.0543  0.1138  -0.0135 156  GLN A CA  
1235  C  C   . GLN A 156  ? 0.8902 0.9601 0.9100 0.0589  0.1074  -0.0159 156  GLN A C   
1236  O  O   . GLN A 156  ? 0.8558 0.9263 0.8710 0.0630  0.1085  -0.0156 156  GLN A O   
1237  C  CB  . GLN A 156  ? 0.8649 0.9101 0.8678 0.0599  0.1111  -0.0102 156  GLN A CB  
1238  C  CG  . GLN A 156  ? 0.8611 0.8974 0.8512 0.0673  0.1124  -0.0073 156  GLN A CG  
1239  C  CD  . GLN A 156  ? 0.8753 0.9067 0.8616 0.0748  0.1061  -0.0054 156  GLN A CD  
1240  O  OE1 . GLN A 156  ? 0.8824 0.9197 0.8775 0.0753  0.0998  -0.0066 156  GLN A OE1 
1241  N  NE2 . GLN A 156  ? 0.9050 0.9254 0.8779 0.0807  0.1080  -0.0024 156  GLN A NE2 
1242  N  N   . GLN A 157  ? 0.9820 1.0617 1.0132 0.0585  0.1008  -0.0183 157  GLN A N   
1243  C  CA  . GLN A 157  ? 0.9295 1.0213 0.9688 0.0623  0.0948  -0.0209 157  GLN A CA  
1244  C  C   . GLN A 157  ? 0.8766 0.9788 0.9287 0.0587  0.0904  -0.0238 157  GLN A C   
1245  O  O   . GLN A 157  ? 1.0117 1.1105 1.0655 0.0552  0.0902  -0.0234 157  GLN A O   
1246  C  CB  . GLN A 157  ? 0.9476 1.0361 0.9826 0.0708  0.0888  -0.0194 157  GLN A CB  
1247  C  CG  . GLN A 157  ? 0.9012 0.9890 0.9406 0.0725  0.0824  -0.0191 157  GLN A CG  
1248  C  CD  . GLN A 157  ? 0.9385 1.0136 0.9697 0.0722  0.0849  -0.0159 157  GLN A CD  
1249  O  OE1 . GLN A 157  ? 0.9805 1.0475 1.0040 0.0690  0.0919  -0.0142 157  GLN A OE1 
1250  N  NE2 . GLN A 157  ? 0.8958 0.9689 0.9284 0.0757  0.0795  -0.0150 157  GLN A NE2 
1251  N  N   . ALA A 158  ? 0.5988 0.7131 0.6592 0.0600  0.0869  -0.0267 158  ALA A N   
1252  C  CA  . ALA A 158  ? 0.7342 0.8588 0.8062 0.0572  0.0827  -0.0296 158  ALA A CA  
1253  C  C   . ALA A 158  ? 0.6956 0.8180 0.7698 0.0608  0.0758  -0.0289 158  ALA A C   
1254  O  O   . ALA A 158  ? 0.6046 0.7233 0.6750 0.0669  0.0721  -0.0275 158  ALA A O   
1255  C  CB  . ALA A 158  ? 0.6940 0.8316 0.7734 0.0586  0.0809  -0.0328 158  ALA A CB  
1256  N  N   . LEU A 159  ? 0.9230 1.0478 1.0034 0.0570  0.0741  -0.0300 159  LEU A N   
1257  C  CA  . LEU A 159  ? 0.8424 0.9647 0.9249 0.0596  0.0683  -0.0292 159  LEU A CA  
1258  C  C   . LEU A 159  ? 0.7713 0.9037 0.8623 0.0628  0.0619  -0.0317 159  LEU A C   
1259  O  O   . LEU A 159  ? 0.7051 0.8432 0.8033 0.0607  0.0592  -0.0335 159  LEU A O   
1260  C  CB  . LEU A 159  ? 0.7773 0.8962 0.8612 0.0542  0.0699  -0.0289 159  LEU A CB  
1261  C  CG  . LEU A 159  ? 0.6882 0.7973 0.7640 0.0499  0.0769  -0.0270 159  LEU A CG  
1262  C  CD1 . LEU A 159  ? 0.8115 0.9198 0.8902 0.0436  0.0785  -0.0280 159  LEU A CD1 
1263  C  CD2 . LEU A 159  ? 0.6096 0.7065 0.6756 0.0544  0.0774  -0.0233 159  LEU A CD2 
1264  N  N   . TYR A 160  ? 0.7507 0.8844 0.8399 0.0682  0.0595  -0.0317 160  TYR A N   
1265  C  CA  . TYR A 160  ? 0.6950 0.8363 0.7906 0.0720  0.0535  -0.0338 160  TYR A CA  
1266  C  C   . TYR A 160  ? 0.6773 0.8148 0.7747 0.0745  0.0482  -0.0328 160  TYR A C   
1267  O  O   . TYR A 160  ? 0.7023 0.8316 0.7955 0.0742  0.0490  -0.0303 160  TYR A O   
1268  C  CB  . TYR A 160  ? 0.7689 0.9116 0.8612 0.0770  0.0527  -0.0342 160  TYR A CB  
1269  C  CG  . TYR A 160  ? 0.7841 0.9308 0.8745 0.0752  0.0582  -0.0352 160  TYR A CG  
1270  C  CD1 . TYR A 160  ? 0.7594 0.9161 0.8568 0.0716  0.0597  -0.0379 160  TYR A CD1 
1271  C  CD2 . TYR A 160  ? 0.8863 1.0269 0.9678 0.0774  0.0618  -0.0334 160  TYR A CD2 
1272  C  CE1 . TYR A 160  ? 0.8428 1.0038 0.9393 0.0698  0.0650  -0.0389 160  TYR A CE1 
1273  C  CE2 . TYR A 160  ? 0.8694 1.0133 0.9490 0.0757  0.0674  -0.0341 160  TYR A CE2 
1274  C  CZ  . TYR A 160  ? 0.8656 1.0200 0.9530 0.0717  0.0691  -0.0369 160  TYR A CZ  
1275  O  OH  . TYR A 160  ? 0.9318 1.0903 1.0181 0.0698  0.0749  -0.0377 160  TYR A OH  
1276  N  N   . MET A 161  ? 0.6417 0.7852 0.7452 0.0770  0.0429  -0.0347 161  MET A N   
1277  C  CA  . MET A 161  ? 0.6398 0.7799 0.7452 0.0795  0.0381  -0.0338 161  MET A CA  
1278  C  C   . MET A 161  ? 0.6377 0.7730 0.7385 0.0846  0.0356  -0.0326 161  MET A C   
1279  O  O   . MET A 161  ? 0.5903 0.7198 0.6898 0.0858  0.0339  -0.0307 161  MET A O   
1280  C  CB  . MET A 161  ? 0.7442 0.8911 0.8569 0.0803  0.0336  -0.0362 161  MET A CB  
1281  C  CG  . MET A 161  ? 0.7951 0.9383 0.9103 0.0817  0.0295  -0.0352 161  MET A CG  
1282  S  SD  . MET A 161  ? 1.0387 1.1880 1.1611 0.0828  0.0248  -0.0376 161  MET A SD  
1283  C  CE  . MET A 161  ? 0.8694 1.0197 0.9913 0.0885  0.0207  -0.0389 161  MET A CE  
1284  N  N   . GLY A 162  ? 0.5481 0.6861 0.6467 0.0877  0.0354  -0.0338 162  GLY A N   
1285  C  CA  . GLY A 162  ? 0.5793 0.7128 0.6726 0.0925  0.0333  -0.0329 162  GLY A CA  
1286  C  C   . GLY A 162  ? 0.5744 0.6997 0.6599 0.0926  0.0367  -0.0300 162  GLY A C   
1287  O  O   . GLY A 162  ? 0.5680 0.6888 0.6501 0.0964  0.0341  -0.0290 162  GLY A O   
1288  N  N   . TRP A 163  ? 0.7734 0.8965 0.8559 0.0884  0.0425  -0.0289 163  TRP A N   
1289  C  CA  . TRP A 163  ? 0.8514 0.9654 0.9255 0.0885  0.0462  -0.0259 163  TRP A CA  
1290  C  C   . TRP A 163  ? 0.8250 0.9342 0.9003 0.0885  0.0441  -0.0241 163  TRP A C   
1291  O  O   . TRP A 163  ? 0.8733 0.9759 0.9428 0.0918  0.0436  -0.0221 163  TRP A O   
1292  C  CB  . TRP A 163  ? 0.8069 0.9193 0.8777 0.0835  0.0533  -0.0253 163  TRP A CB  
1293  C  CG  . TRP A 163  ? 0.8292 0.9310 0.8914 0.0829  0.0574  -0.0222 163  TRP A CG  
1294  C  CD1 . TRP A 163  ? 0.8220 0.9164 0.8743 0.0868  0.0593  -0.0201 163  TRP A CD1 
1295  C  CD2 . TRP A 163  ? 0.8170 0.9139 0.8789 0.0784  0.0603  -0.0208 163  TRP A CD2 
1296  N  NE1 . TRP A 163  ? 0.8288 0.9138 0.8746 0.0852  0.0633  -0.0173 163  TRP A NE1 
1297  C  CE2 . TRP A 163  ? 0.8764 0.9625 0.9279 0.0800  0.0640  -0.0177 163  TRP A CE2 
1298  C  CE3 . TRP A 163  ? 0.6827 0.7827 0.7515 0.0736  0.0600  -0.0218 163  TRP A CE3 
1299  C  CZ2 . TRP A 163  ? 0.8433 0.9215 0.8911 0.0768  0.0675  -0.0157 163  TRP A CZ2 
1300  C  CZ3 . TRP A 163  ? 0.6817 0.7742 0.7469 0.0703  0.0633  -0.0200 163  TRP A CZ3 
1301  C  CH2 . TRP A 163  ? 0.8426 0.9242 0.8975 0.0718  0.0671  -0.0170 163  TRP A CH2 
1302  N  N   . CYS A 164  ? 0.6370 0.7492 0.7193 0.0851  0.0428  -0.0249 164  CYS A N   
1303  C  CA  . CYS A 164  ? 0.6320 0.7403 0.7161 0.0855  0.0405  -0.0234 164  CYS A CA  
1304  C  C   . CYS A 164  ? 0.6119 0.7218 0.6991 0.0903  0.0345  -0.0240 164  CYS A C   
1305  O  O   . CYS A 164  ? 0.6208 0.7262 0.7063 0.0927  0.0330  -0.0222 164  CYS A O   
1306  C  CB  . CYS A 164  ? 0.6230 0.7342 0.7135 0.0809  0.0405  -0.0242 164  CYS A CB  
1307  S  SG  . CYS A 164  ? 0.6425 0.7547 0.7319 0.0745  0.0467  -0.0249 164  CYS A SG  
1308  N  N   . LEU A 165  ? 0.5055 0.6220 0.5974 0.0917  0.0311  -0.0265 165  LEU A N   
1309  C  CA  . LEU A 165  ? 0.4773 0.5953 0.5725 0.0957  0.0254  -0.0275 165  LEU A CA  
1310  C  C   . LEU A 165  ? 0.6556 0.7698 0.7444 0.1002  0.0243  -0.0266 165  LEU A C   
1311  O  O   . LEU A 165  ? 0.6167 0.7304 0.7074 0.1032  0.0201  -0.0267 165  LEU A O   
1312  C  CB  . LEU A 165  ? 0.5340 0.6587 0.6340 0.0963  0.0225  -0.0304 165  LEU A CB  
1313  C  CG  . LEU A 165  ? 0.4926 0.6211 0.5997 0.0933  0.0215  -0.0315 165  LEU A CG  
1314  C  CD1 . LEU A 165  ? 0.6319 0.7665 0.7427 0.0948  0.0188  -0.0343 165  LEU A CD1 
1315  C  CD2 . LEU A 165  ? 0.5273 0.6530 0.6382 0.0935  0.0185  -0.0305 165  LEU A CD2 
1316  N  N   . ASN A 166  ? 0.7929 0.9047 0.8741 0.1009  0.0282  -0.0259 166  ASN A N   
1317  C  CA  . ASN A 166  ? 0.7510 0.8589 0.8250 0.1059  0.0272  -0.0252 166  ASN A CA  
1318  C  C   . ASN A 166  ? 0.7174 0.8194 0.7885 0.1073  0.0272  -0.0226 166  ASN A C   
1319  O  O   . ASN A 166  ? 0.7638 0.8651 0.8340 0.1117  0.0232  -0.0227 166  ASN A O   
1320  C  CB  . ASN A 166  ? 0.7613 0.8671 0.8271 0.1062  0.0321  -0.0247 166  ASN A CB  
1321  C  CG  . ASN A 166  ? 0.8017 0.9030 0.8587 0.1118  0.0312  -0.0239 166  ASN A CG  
1322  O  OD1 . ASN A 166  ? 1.0083 1.1039 1.0562 0.1124  0.0360  -0.0220 166  ASN A OD1 
1323  N  ND2 . ASN A 166  ? 0.7905 0.8939 0.8498 0.1160  0.0251  -0.0254 166  ASN A ND2 
1324  N  N   . CYS A 167  ? 0.5938 0.6916 0.6633 0.1038  0.0315  -0.0205 167  CYS A N   
1325  C  CA  . CYS A 167  ? 0.6279 0.7199 0.6945 0.1054  0.0317  -0.0180 167  CYS A CA  
1326  C  C   . CYS A 167  ? 0.5698 0.6650 0.6453 0.1053  0.0272  -0.0185 167  CYS A C   
1327  O  O   . CYS A 167  ? 0.5217 0.6155 0.5971 0.1088  0.0245  -0.0177 167  CYS A O   
1328  C  CB  . CYS A 167  ? 0.5410 0.6266 0.6025 0.1016  0.0380  -0.0156 167  CYS A CB  
1329  S  SG  . CYS A 167  ? 0.5202 0.5962 0.5734 0.1050  0.0398  -0.0121 167  CYS A SG  
1330  N  N   . HIS A 168  ? 0.8510 0.9508 0.9343 0.1015  0.0264  -0.0200 168  HIS A N   
1331  C  CA  . HIS A 168  ? 0.8332 0.9354 0.9245 0.1010  0.0228  -0.0203 168  HIS A CA  
1332  C  C   . HIS A 168  ? 0.8625 0.9684 0.9577 0.1049  0.0171  -0.0221 168  HIS A C   
1333  O  O   . HIS A 168  ? 0.8185 0.9246 0.9177 0.1063  0.0144  -0.0217 168  HIS A O   
1334  C  CB  . HIS A 168  ? 0.8429 0.9486 0.9403 0.0965  0.0234  -0.0215 168  HIS A CB  
1335  C  CG  . HIS A 168  ? 0.8178 0.9197 0.9134 0.0925  0.0279  -0.0198 168  HIS A CG  
1336  N  ND1 . HIS A 168  ? 0.8424 0.9404 0.9387 0.0921  0.0285  -0.0178 168  HIS A ND1 
1337  C  CD2 . HIS A 168  ? 0.8331 0.9344 0.9261 0.0888  0.0321  -0.0199 168  HIS A CD2 
1338  C  CE1 . HIS A 168  ? 0.8203 0.9148 0.9139 0.0883  0.0327  -0.0168 168  HIS A CE1 
1339  N  NE2 . HIS A 168  ? 0.7985 0.8951 0.8903 0.0860  0.0350  -0.0181 168  HIS A NE2 
1340  N  N   . ARG A 169  ? 0.6261 0.7351 0.7204 0.1066  0.0153  -0.0243 169  ARG A N   
1341  C  CA  . ARG A 169  ? 0.6950 0.8071 0.7924 0.1101  0.0097  -0.0264 169  ARG A CA  
1342  C  C   . ARG A 169  ? 0.7998 0.9092 0.8912 0.1149  0.0084  -0.0256 169  ARG A C   
1343  O  O   . ARG A 169  ? 0.7572 0.8687 0.8524 0.1174  0.0037  -0.0268 169  ARG A O   
1344  C  CB  . ARG A 169  ? 0.7110 0.8269 0.8088 0.1105  0.0081  -0.0291 169  ARG A CB  
1345  C  CG  . ARG A 169  ? 0.7181 0.8375 0.8226 0.1070  0.0080  -0.0304 169  ARG A CG  
1346  C  CD  . ARG A 169  ? 0.8125 0.9357 0.9198 0.1087  0.0041  -0.0335 169  ARG A CD  
1347  N  NE  . ARG A 169  ? 0.7389 0.8653 0.8487 0.1063  0.0055  -0.0347 169  ARG A NE  
1348  C  CZ  . ARG A 169  ? 0.8154 0.9438 0.9215 0.1063  0.0080  -0.0354 169  ARG A CZ  
1349  N  NH1 . ARG A 169  ? 0.9357 1.0624 1.0348 0.1086  0.0097  -0.0350 169  ARG A NH1 
1350  N  NH2 . ARG A 169  ? 0.6340 0.7662 0.7434 0.1043  0.0089  -0.0367 169  ARG A NH2 
1351  N  N   . ASN A 170  ? 0.8772 0.9821 0.9595 0.1161  0.0123  -0.0237 170  ASN A N   
1352  C  CA  . ASN A 170  ? 0.8448 0.9463 0.9196 0.1213  0.0114  -0.0228 170  ASN A CA  
1353  C  C   . ASN A 170  ? 0.8758 0.9704 0.9433 0.1211  0.0166  -0.0193 170  ASN A C   
1354  O  O   . ASN A 170  ? 0.8984 0.9882 0.9566 0.1219  0.0208  -0.0180 170  ASN A O   
1355  C  CB  . ASN A 170  ? 0.8019 0.9037 0.8703 0.1245  0.0107  -0.0244 170  ASN A CB  
1356  C  CG  . ASN A 170  ? 0.8497 0.9574 0.9243 0.1253  0.0054  -0.0279 170  ASN A CG  
1357  O  OD1 . ASN A 170  ? 0.8539 0.9633 0.9271 0.1249  0.0060  -0.0295 170  ASN A OD1 
1358  N  ND2 . ASN A 170  ? 0.8863 0.9970 0.9678 0.1264  0.0002  -0.0293 170  ASN A ND2 
1359  N  N   . PRO A 171  ? 0.8920 0.9853 0.9631 0.1201  0.0168  -0.0177 171  PRO A N   
1360  C  CA  . PRO A 171  ? 0.9359 1.0217 0.9996 0.1200  0.0219  -0.0144 171  PRO A CA  
1361  C  C   . PRO A 171  ? 0.8785 0.9600 0.9338 0.1262  0.0212  -0.0129 171  PRO A C   
1362  O  O   . PRO A 171  ? 0.8277 0.9016 0.8748 0.1269  0.0257  -0.0100 171  PRO A O   
1363  C  CB  . PRO A 171  ? 0.7896 0.8762 0.8608 0.1170  0.0218  -0.0136 171  PRO A CB  
1364  C  CG  . PRO A 171  ? 0.7722 0.8660 0.8531 0.1183  0.0157  -0.0159 171  PRO A CG  
1365  C  CD  . PRO A 171  ? 0.8916 0.9897 0.9735 0.1188  0.0130  -0.0188 171  PRO A CD  
1366  N  N   . GLU A 172  ? 0.8542 0.9400 0.9111 0.1309  0.0156  -0.0148 172  GLU A N   
1367  C  CA  . GLU A 172  ? 0.9329 1.0153 0.9817 0.1375  0.0143  -0.0137 172  GLU A CA  
1368  C  C   . GLU A 172  ? 0.9825 1.0574 1.0177 0.1397  0.0188  -0.0121 172  GLU A C   
1369  O  O   . GLU A 172  ? 0.9935 1.0622 1.0191 0.1446  0.0201  -0.0099 172  GLU A O   
1370  C  CB  . GLU A 172  ? 0.9707 1.0600 1.0245 0.1417  0.0070  -0.0168 172  GLU A CB  
1371  C  CG  . GLU A 172  ? 1.0512 1.1454 1.1087 0.1400  0.0044  -0.0200 172  GLU A CG  
1372  C  CD  . GLU A 172  ? 1.0601 1.1610 1.1309 0.1354  0.0015  -0.0222 172  GLU A CD  
1373  O  OE1 . GLU A 172  ? 1.0478 1.1485 1.1240 0.1317  0.0036  -0.0207 172  GLU A OE1 
1374  O  OE2 . GLU A 172  ? 0.9410 1.0468 1.0162 0.1356  -0.0027 -0.0254 172  GLU A OE2 
1375  N  N   . LEU A 173  ? 0.8613 0.9364 0.8952 0.1364  0.0214  -0.0131 173  LEU A N   
1376  C  CA  . LEU A 173  ? 0.9060 0.9745 0.9274 0.1383  0.0258  -0.0118 173  LEU A CA  
1377  C  C   . LEU A 173  ? 0.8614 0.9211 0.8755 0.1350  0.0335  -0.0085 173  LEU A C   
1378  O  O   . LEU A 173  ? 0.9387 0.9905 0.9404 0.1377  0.0377  -0.0065 173  LEU A O   
1379  C  CB  . LEU A 173  ? 0.9246 0.9976 0.9478 0.1362  0.0256  -0.0143 173  LEU A CB  
1380  C  CG  . LEU A 173  ? 0.8181 0.8999 0.8503 0.1376  0.0185  -0.0180 173  LEU A CG  
1381  C  CD1 . LEU A 173  ? 0.6817 0.7673 0.7158 0.1348  0.0194  -0.0202 173  LEU A CD1 
1382  C  CD2 . LEU A 173  ? 0.8131 0.8949 0.8403 0.1449  0.0134  -0.0190 173  LEU A CD2 
1383  N  N   . TYR A 174  ? 0.7058 0.7662 0.7267 0.1293  0.0356  -0.0079 174  TYR A N   
1384  C  CA  . TYR A 174  ? 0.6812 0.7337 0.6961 0.1251  0.0430  -0.0054 174  TYR A CA  
1385  C  C   . TYR A 174  ? 0.6974 0.7446 0.7116 0.1249  0.0445  -0.0030 174  TYR A C   
1386  O  O   . TYR A 174  ? 0.7999 0.8394 0.8083 0.1214  0.0506  -0.0009 174  TYR A O   
1387  C  CB  . TYR A 174  ? 0.6937 0.7508 0.7157 0.1177  0.0454  -0.0071 174  TYR A CB  
1388  C  CG  . TYR A 174  ? 0.6996 0.7634 0.7243 0.1177  0.0435  -0.0098 174  TYR A CG  
1389  C  CD1 . TYR A 174  ? 0.6070 0.6673 0.6232 0.1176  0.0481  -0.0094 174  TYR A CD1 
1390  C  CD2 . TYR A 174  ? 0.6467 0.7198 0.6819 0.1178  0.0374  -0.0127 174  TYR A CD2 
1391  C  CE1 . TYR A 174  ? 0.5325 0.5989 0.5509 0.1180  0.0466  -0.0119 174  TYR A CE1 
1392  C  CE2 . TYR A 174  ? 0.5933 0.6719 0.6303 0.1181  0.0358  -0.0152 174  TYR A CE2 
1393  C  CZ  . TYR A 174  ? 0.6441 0.7196 0.6728 0.1184  0.0403  -0.0148 174  TYR A CZ  
1394  O  OH  . TYR A 174  ? 0.9362 1.0172 0.9665 0.1191  0.0388  -0.0173 174  TYR A OH  
1395  N  N   . VAL A 175  ? 0.6685 0.7197 0.6885 0.1283  0.0393  -0.0033 175  VAL A N   
1396  C  CA  . VAL A 175  ? 0.6630 0.7096 0.6827 0.1285  0.0407  -0.0010 175  VAL A CA  
1397  C  C   . VAL A 175  ? 0.8275 0.8637 0.8333 0.1340  0.0439  0.0020  175  VAL A C   
1398  O  O   . VAL A 175  ? 0.8969 0.9319 0.8956 0.1397  0.0423  0.0020  175  VAL A O   
1399  C  CB  . VAL A 175  ? 0.6599 0.7149 0.6911 0.1303  0.0344  -0.0024 175  VAL A CB  
1400  C  CG1 . VAL A 175  ? 0.7393 0.7975 0.7689 0.1377  0.0292  -0.0033 175  VAL A CG1 
1401  C  CG2 . VAL A 175  ? 0.6507 0.7019 0.6831 0.1294  0.0364  -0.0002 175  VAL A CG2 
1402  N  N   . ARG A 176  ? 0.8193 0.8474 0.8204 0.1325  0.0485  0.0046  176  ARG A N   
1403  C  CA  . ARG A 176  ? 0.7967 0.8130 0.7836 0.1373  0.0525  0.0079  176  ARG A CA  
1404  C  C   . ARG A 176  ? 0.8765 0.8904 0.8646 0.1395  0.0521  0.0097  176  ARG A C   
1405  O  O   . ARG A 176  ? 0.8869 0.9054 0.8851 0.1353  0.0511  0.0089  176  ARG A O   
1406  C  CB  . ARG A 176  ? 0.8156 0.8214 0.7924 0.1325  0.0605  0.0095  176  ARG A CB  
1407  C  CG  . ARG A 176  ? 0.9693 0.9671 0.9438 0.1283  0.0656  0.0115  176  ARG A CG  
1408  C  CD  . ARG A 176  ? 0.9537 0.9404 0.9172 0.1239  0.0736  0.0130  176  ARG A CD  
1409  N  NE  . ARG A 176  ? 0.9764 0.9685 0.9428 0.1199  0.0744  0.0108  176  ARG A NE  
1410  C  CZ  . ARG A 176  ? 0.9940 0.9785 0.9506 0.1176  0.0805  0.0117  176  ARG A CZ  
1411  N  NH1 . ARG A 176  ? 1.0247 0.9949 0.9676 0.1185  0.0868  0.0148  176  ARG A NH1 
1412  N  NH2 . ARG A 176  ? 0.9604 0.9515 0.9210 0.1144  0.0807  0.0095  176  ARG A NH2 
1413  N  N   . PRO A 177  ? 1.0740 1.0804 1.0515 0.1467  0.0527  0.0121  177  PRO A N   
1414  C  CA  . PRO A 177  ? 1.1353 1.1407 1.1145 0.1501  0.0517  0.0137  177  PRO A CA  
1415  C  C   . PRO A 177  ? 1.2862 1.2798 1.2582 0.1469  0.0585  0.0165  177  PRO A C   
1416  O  O   . PRO A 177  ? 1.4756 1.4589 1.4360 0.1519  0.0615  0.0194  177  PRO A O   
1417  C  CB  . PRO A 177  ? 0.9232 0.9270 0.8942 0.1600  0.0488  0.0147  177  PRO A CB  
1418  C  CG  . PRO A 177  ? 1.1673 1.1628 1.1252 0.1611  0.0525  0.0156  177  PRO A CG  
1419  C  CD  . PRO A 177  ? 1.0821 1.0823 1.0464 0.1531  0.0536  0.0133  177  PRO A CD  
1420  N  N   . ARG A 178  ? 1.0168 1.0118 0.9956 0.1385  0.0608  0.0154  178  ARG A N   
1421  C  CA  . ARG A 178  ? 1.0760 1.0618 1.0509 0.1345  0.0662  0.0173  178  ARG A CA  
1422  C  C   . ARG A 178  ? 1.2754 1.2453 1.2331 0.1356  0.0732  0.0202  178  ARG A C   
1423  O  O   . ARG A 178  ? 1.2476 1.2074 1.1976 0.1372  0.0768  0.0227  178  ARG A O   
1424  C  CB  . ARG A 178  ? 1.0821 1.0701 1.0622 0.1378  0.0639  0.0182  178  ARG A CB  
1425  C  CG  . ARG A 178  ? 1.0803 1.0826 1.0772 0.1357  0.0580  0.0155  178  ARG A CG  
1426  C  CD  . ARG A 178  ? 0.9942 0.9986 0.9982 0.1267  0.0599  0.0140  178  ARG A CD  
1427  N  NE  . ARG A 178  ? 1.0553 1.0534 1.0582 0.1246  0.0632  0.0156  178  ARG A NE  
1428  C  CZ  . ARG A 178  ? 0.9304 0.9341 0.9421 0.1255  0.0605  0.0154  178  ARG A CZ  
1429  N  NH1 . ARG A 178  ? 0.8658 0.8814 0.8886 0.1281  0.0547  0.0138  178  ARG A NH1 
1430  N  NH2 . ARG A 178  ? 0.7275 0.7244 0.7367 0.1236  0.0641  0.0169  178  ARG A NH2 
1431  N  N   . GLU A 179  ? 1.2926 1.2597 1.2437 0.1348  0.0754  0.0199  179  GLU A N   
1432  C  CA  . GLU A 179  ? 1.2298 1.1814 1.1653 0.1338  0.0831  0.0224  179  GLU A CA  
1433  C  C   . GLU A 179  ? 1.2368 1.1889 1.1742 0.1249  0.0871  0.0207  179  GLU A C   
1434  O  O   . GLU A 179  ? 1.2746 1.2202 1.2023 0.1247  0.0912  0.0215  179  GLU A O   
1435  C  CB  . GLU A 179  ? 1.2883 1.2333 1.2106 0.1424  0.0834  0.0244  179  GLU A CB  
1436  C  CG  . GLU A 179  ? 1.1963 1.1531 1.1245 0.1462  0.0771  0.0222  179  GLU A CG  
1437  C  CD  . GLU A 179  ? 1.2429 1.1936 1.1582 0.1560  0.0763  0.0241  179  GLU A CD  
1438  O  OE1 . GLU A 179  ? 1.1337 1.0710 1.0353 0.1601  0.0807  0.0273  179  GLU A OE1 
1439  O  OE2 . GLU A 179  ? 1.3771 1.3361 1.2952 0.1597  0.0713  0.0223  179  GLU A OE2 
1440  N  N   . GLU A 180  ? 1.4641 1.4242 1.4138 0.1178  0.0858  0.0184  180  GLU A N   
1441  C  CA  . GLU A 180  ? 1.4440 1.4086 1.3991 0.1095  0.0880  0.0160  180  GLU A CA  
1442  C  C   . GLU A 180  ? 1.4977 1.4507 1.4450 0.1026  0.0959  0.0169  180  GLU A C   
1443  O  O   . GLU A 180  ? 1.4421 1.3940 1.3872 0.0977  0.0999  0.0159  180  GLU A O   
1444  C  CB  . GLU A 180  ? 1.3807 1.3594 1.3525 0.1055  0.0827  0.0129  180  GLU A CB  
1445  C  CG  . GLU A 180  ? 1.3382 1.3155 1.3143 0.1036  0.0823  0.0133  180  GLU A CG  
1446  C  CD  . GLU A 180  ? 1.4900 1.4734 1.4721 0.1102  0.0763  0.0138  180  GLU A CD  
1447  O  OE1 . GLU A 180  ? 1.4451 1.4357 1.4302 0.1152  0.0716  0.0130  180  GLU A OE1 
1448  O  OE2 . GLU A 180  ? 1.5913 1.5723 1.5751 0.1102  0.0764  0.0147  180  GLU A OE2 
1449  N  N   . VAL A 181  ? 1.3711 1.3155 1.3145 0.1019  0.0983  0.0185  181  VAL A N   
1450  C  CA  . VAL A 181  ? 1.3475 1.2811 1.2845 0.0946  0.1055  0.0188  181  VAL A CA  
1451  C  C   . VAL A 181  ? 1.4494 1.3698 1.3711 0.0952  0.1123  0.0209  181  VAL A C   
1452  O  O   . VAL A 181  ? 1.4979 1.4154 1.4177 0.0880  0.1176  0.0199  181  VAL A O   
1453  C  CB  . VAL A 181  ? 1.2057 1.1318 1.1403 0.0948  0.1065  0.0202  181  VAL A CB  
1454  C  CG1 . VAL A 181  ? 1.0513 0.9894 1.0009 0.0909  0.1017  0.0176  181  VAL A CG1 
1455  C  CG2 . VAL A 181  ? 1.2893 1.2100 1.2166 0.1048  0.1045  0.0232  181  VAL A CG2 
1456  N  N   . TYR A 182  ? 2.0065 1.9187 1.9169 0.1039  0.1125  0.0240  182  TYR A N   
1457  C  CA  . TYR A 182  ? 1.9937 1.8935 1.8888 0.1060  0.1184  0.0263  182  TYR A CA  
1458  C  C   . TYR A 182  ? 1.9361 1.8444 1.8326 0.1121  0.1141  0.0258  182  TYR A C   
1459  O  O   . TYR A 182  ? 1.8548 1.7788 1.7652 0.1115  0.1078  0.0230  182  TYR A O   
1460  C  CB  . TYR A 182  ? 2.1105 1.9930 1.9898 0.1117  0.1224  0.0301  182  TYR A CB  
1461  C  CG  . TYR A 182  ? 2.2176 2.1027 2.0958 0.1227  0.1164  0.0317  182  TYR A CG  
1462  C  CD1 . TYR A 182  ? 2.2132 2.1090 2.1039 0.1242  0.1101  0.0305  182  TYR A CD1 
1463  C  CD2 . TYR A 182  ? 2.1557 2.0325 2.0203 0.1317  0.1172  0.0345  182  TYR A CD2 
1464  C  CE1 . TYR A 182  ? 2.2142 2.1133 2.1049 0.1339  0.1048  0.0317  182  TYR A CE1 
1465  C  CE2 . TYR A 182  ? 2.1066 1.9867 1.9707 0.1418  0.1115  0.0356  182  TYR A CE2 
1466  C  CZ  . TYR A 182  ? 2.1652 2.0570 2.0430 0.1427  0.1053  0.0341  182  TYR A CZ  
1467  O  OH  . TYR A 182  ? 2.1816 2.0777 2.0600 0.1524  0.0997  0.0350  182  TYR A OH  
1468  N  N   . ASN A 183  ? 1.6701 1.5673 1.5514 0.1181  0.1175  0.0285  183  ASN A N   
1469  C  CA  . ASN A 183  ? 1.5745 1.4776 1.4544 0.1247  0.1137  0.0283  183  ASN A CA  
1470  C  C   . ASN A 183  ? 1.5924 1.5071 1.4822 0.1185  0.1131  0.0252  183  ASN A C   
1471  O  O   . ASN A 183  ? 1.6252 1.5534 1.5246 0.1213  0.1065  0.0230  183  ASN A O   
1472  C  CB  . ASN A 183  ? 1.5540 1.4671 1.4408 0.1331  0.1047  0.0279  183  ASN A CB  
1473  C  CG  . ASN A 183  ? 1.6189 1.5208 1.4912 0.1434  0.1050  0.0313  183  ASN A CG  
1474  O  OD1 . ASN A 183  ? 1.6839 1.5714 1.5398 0.1458  0.1111  0.0340  183  ASN A OD1 
1475  N  ND2 . ASN A 183  ? 1.5781 1.4866 1.4562 0.1496  0.0985  0.0312  183  ASN A ND2 
1476  N  N   . MET A 184  ? 1.4164 1.3259 1.3039 0.1100  0.1204  0.0248  184  MET A N   
1477  C  CA  . MET A 184  ? 1.3366 1.2552 1.2306 0.1050  0.1212  0.0222  184  MET A CA  
1478  C  C   . MET A 184  ? 1.3221 1.2381 1.2063 0.1119  0.1215  0.0235  184  MET A C   
1479  O  O   . MET A 184  ? 1.2320 1.1587 1.1229 0.1112  0.1192  0.0212  184  MET A O   
1480  C  CB  . MET A 184  ? 1.2299 1.1427 1.1225 0.0946  0.1294  0.0216  184  MET A CB  
1481  C  CG  . MET A 184  ? 1.2380 1.1536 1.1402 0.0873  0.1291  0.0199  184  MET A CG  
1482  S  SD  . MET A 184  ? 1.4452 1.3831 1.3696 0.0835  0.1208  0.0153  184  MET A SD  
1483  C  CE  . MET A 184  ? 1.1811 1.1257 1.1096 0.0760  0.1254  0.0128  184  MET A CE  
1484  N  N   . ASP A 185  ? 1.5467 1.4482 1.4143 0.1190  0.1244  0.0271  185  ASP A N   
1485  C  CA  . ASP A 185  ? 1.6279 1.5259 1.4846 0.1272  0.1240  0.0286  185  ASP A CA  
1486  C  C   . ASP A 185  ? 1.6471 1.5568 1.5105 0.1358  0.1138  0.0272  185  ASP A C   
1487  O  O   . ASP A 185  ? 1.7155 1.6267 1.5735 0.1419  0.1118  0.0273  185  ASP A O   
1488  C  CB  . ASP A 185  ? 1.7655 1.6433 1.6014 0.1324  0.1305  0.0330  185  ASP A CB  
1489  C  CG  . ASP A 185  ? 1.8095 1.6741 1.6381 0.1237  0.1408  0.0343  185  ASP A CG  
1490  O  OD1 . ASP A 185  ? 1.8099 1.6814 1.6482 0.1140  0.1435  0.0318  185  ASP A OD1 
1491  O  OD2 . ASP A 185  ? 1.7582 1.6053 1.5712 0.1265  0.1462  0.0378  185  ASP A OD2 
1492  N  N   . TYR A 186  ? 1.2354 1.1533 1.1102 0.1362  0.1077  0.0260  186  TYR A N   
1493  C  CA  . TYR A 186  ? 1.2127 1.1427 1.0956 0.1433  0.0981  0.0244  186  TYR A CA  
1494  C  C   . TYR A 186  ? 1.1713 1.1155 1.0654 0.1408  0.0940  0.0208  186  TYR A C   
1495  O  O   . TYR A 186  ? 1.1151 1.0651 1.0182 0.1323  0.0962  0.0188  186  TYR A O   
1496  C  CB  . TYR A 186  ? 1.1397 1.0761 1.0340 0.1427  0.0931  0.0236  186  TYR A CB  
1497  C  CG  . TYR A 186  ? 0.9986 0.9516 0.9075 0.1456  0.0835  0.0205  186  TYR A CG  
1498  C  CD1 . TYR A 186  ? 1.0980 1.0535 1.0044 0.1553  0.0775  0.0208  186  TYR A CD1 
1499  C  CD2 . TYR A 186  ? 0.9102 0.8762 0.8354 0.1388  0.0804  0.0172  186  TYR A CD2 
1500  C  CE1 . TYR A 186  ? 0.9152 0.8855 0.8351 0.1574  0.0690  0.0178  186  TYR A CE1 
1501  C  CE2 . TYR A 186  ? 0.8437 0.8236 0.7816 0.1412  0.0721  0.0145  186  TYR A CE2 
1502  C  CZ  . TYR A 186  ? 0.8336 0.8156 0.7690 0.1502  0.0665  0.0147  186  TYR A CZ  
1503  O  OH  . TYR A 186  ? 0.8405 0.8360 0.7887 0.1521  0.0584  0.0118  186  TYR A OH  
1504  N  N   . VAL A 187  ? 1.2620 1.2119 1.1554 0.1485  0.0879  0.0199  187  VAL A N   
1505  C  CA  . VAL A 187  ? 1.2062 1.1685 1.1086 0.1474  0.0837  0.0166  187  VAL A CA  
1506  C  C   . VAL A 187  ? 1.1470 1.1206 1.0583 0.1536  0.0737  0.0144  187  VAL A C   
1507  O  O   . VAL A 187  ? 1.1266 1.0970 1.0334 0.1605  0.0707  0.0158  187  VAL A O   
1508  C  CB  . VAL A 187  ? 1.3441 1.2999 1.2336 0.1501  0.0881  0.0175  187  VAL A CB  
1509  C  CG1 . VAL A 187  ? 1.4269 1.3760 1.3129 0.1416  0.0975  0.0184  187  VAL A CG1 
1510  C  CG2 . VAL A 187  ? 1.3981 1.3419 1.2704 0.1599  0.0888  0.0206  187  VAL A CG2 
1511  N  N   . PRO A 188  ? 1.1624 1.1493 1.0866 0.1511  0.0686  0.0108  188  PRO A N   
1512  C  CA  . PRO A 188  ? 1.1168 1.1147 1.0506 0.1560  0.0592  0.0083  188  PRO A CA  
1513  C  C   . PRO A 188  ? 1.2091 1.2034 1.1318 0.1662  0.0558  0.0091  188  PRO A C   
1514  O  O   . PRO A 188  ? 1.3317 1.3211 1.2435 0.1693  0.0581  0.0096  188  PRO A O   
1515  C  CB  . PRO A 188  ? 1.1720 1.1818 1.1173 0.1517  0.0561  0.0046  188  PRO A CB  
1516  C  CG  . PRO A 188  ? 1.2221 1.2264 1.1607 0.1471  0.0637  0.0054  188  PRO A CG  
1517  C  CD  . PRO A 188  ? 1.2078 1.2006 1.1389 0.1437  0.0712  0.0087  188  PRO A CD  
1518  N  N   . PRO A 189  ? 1.0931 1.0899 1.0181 0.1718  0.0504  0.0092  189  PRO A N   
1519  C  CA  . PRO A 189  ? 1.0980 1.0925 1.0131 0.1821  0.0463  0.0096  189  PRO A CA  
1520  C  C   . PRO A 189  ? 1.1715 1.1755 1.0908 0.1846  0.0401  0.0059  189  PRO A C   
1521  O  O   . PRO A 189  ? 1.1299 1.1433 1.0615 0.1789  0.0378  0.0029  189  PRO A O   
1522  C  CB  . PRO A 189  ? 1.1065 1.1048 1.0275 0.1859  0.0414  0.0097  189  PRO A CB  
1523  C  CG  . PRO A 189  ? 1.1759 1.1837 1.1144 0.1777  0.0399  0.0078  189  PRO A CG  
1524  C  CD  . PRO A 189  ? 1.1756 1.1782 1.1129 0.1691  0.0475  0.0088  189  PRO A CD  
1525  N  N   . SER A 190  ? 1.1889 1.1897 1.0970 0.1937  0.0372  0.0061  190  SER A N   
1526  C  CA  . SER A 190  ? 1.1837 1.1922 1.0938 0.1971  0.0311  0.0026  190  SER A CA  
1527  C  C   . SER A 190  ? 1.1351 1.1583 1.0629 0.1958  0.0223  -0.0015 190  SER A C   
1528  O  O   . SER A 190  ? 1.0601 1.0915 0.9958 0.1934  0.0186  -0.0050 190  SER A O   
1529  C  CB  . SER A 190  ? 1.1139 1.1156 1.0077 0.2077  0.0294  0.0035  190  SER A CB  
1530  O  OG  . SER A 190  ? 1.2745 1.2846 1.1711 0.2117  0.0220  -0.0004 190  SER A OG  
1531  N  N   . ASN A 191  ? 1.4672 1.4937 1.4013 0.1974  0.0191  -0.0011 191  ASN A N   
1532  C  CA  . ASN A 191  ? 1.4255 1.4655 1.3767 0.1959  0.0114  -0.0048 191  ASN A CA  
1533  C  C   . ASN A 191  ? 1.4851 1.5287 1.4495 0.1868  0.0140  -0.0045 191  ASN A C   
1534  O  O   . ASN A 191  ? 1.6388 1.6863 1.6116 0.1861  0.0122  -0.0042 191  ASN A O   
1535  C  CB  . ASN A 191  ? 1.4674 1.5103 1.4182 0.2038  0.0058  -0.0049 191  ASN A CB  
1536  C  CG  . ASN A 191  ? 1.5968 1.6296 1.5385 0.2064  0.0111  -0.0005 191  ASN A CG  
1537  O  OD1 . ASN A 191  ? 1.5725 1.5937 1.5036 0.2041  0.0191  0.0029  191  ASN A OD1 
1538  N  ND2 . ASN A 191  ? 1.6658 1.7030 1.6117 0.2111  0.0069  -0.0005 191  ASN A ND2 
1539  N  N   . GLN A 192  ? 1.1278 1.1704 1.0940 0.1798  0.0184  -0.0047 192  GLN A N   
1540  C  CA  . GLN A 192  ? 1.0097 1.0548 0.9868 0.1712  0.0213  -0.0044 192  GLN A CA  
1541  C  C   . GLN A 192  ? 0.9778 1.0354 0.9720 0.1685  0.0147  -0.0079 192  GLN A C   
1542  O  O   . GLN A 192  ? 0.9851 1.0453 0.9886 0.1640  0.0153  -0.0074 192  GLN A O   
1543  C  CB  . GLN A 192  ? 0.9982 1.0399 0.9727 0.1650  0.0275  -0.0041 192  GLN A CB  
1544  C  CG  . GLN A 192  ? 0.9146 0.9609 0.9015 0.1562  0.0293  -0.0048 192  GLN A CG  
1545  C  CD  . GLN A 192  ? 0.9388 0.9792 0.9251 0.1533  0.0339  -0.0018 192  GLN A CD  
1546  O  OE1 . GLN A 192  ? 1.0866 1.1163 1.0611 0.1537  0.0401  0.0013  192  GLN A OE1 
1547  N  NE2 . GLN A 192  ? 0.8576 0.9042 0.8561 0.1504  0.0309  -0.0027 192  GLN A NE2 
1548  N  N   . LEU A 193  ? 0.9942 1.0591 0.9923 0.1711  0.0084  -0.0115 193  LEU A N   
1549  C  CA  . LEU A 193  ? 0.9178 0.9937 0.9316 0.1680  0.0024  -0.0149 193  LEU A CA  
1550  C  C   . LEU A 193  ? 0.9424 1.0227 0.9632 0.1705  -0.0014 -0.0149 193  LEU A C   
1551  O  O   . LEU A 193  ? 1.0530 1.1386 1.0860 0.1657  -0.0023 -0.0155 193  LEU A O   
1552  C  CB  . LEU A 193  ? 0.8302 0.9117 0.8451 0.1707  -0.0034 -0.0188 193  LEU A CB  
1553  C  CG  . LEU A 193  ? 0.8749 0.9663 0.9051 0.1662  -0.0085 -0.0226 193  LEU A CG  
1554  C  CD1 . LEU A 193  ? 1.0005 1.0920 1.0372 0.1582  -0.0040 -0.0219 193  LEU A CD1 
1555  C  CD2 . LEU A 193  ? 0.9480 1.0433 0.9774 0.1691  -0.0139 -0.0265 193  LEU A CD2 
1556  N  N   . GLU A 194  ? 1.1382 1.2165 1.1513 0.1782  -0.0037 -0.0141 194  GLU A N   
1557  C  CA  . GLU A 194  ? 1.2209 1.3040 1.2405 0.1812  -0.0073 -0.0141 194  GLU A CA  
1558  C  C   . GLU A 194  ? 1.1904 1.2683 1.2104 0.1780  -0.0015 -0.0104 194  GLU A C   
1559  O  O   . GLU A 194  ? 1.1842 1.2681 1.2161 0.1752  -0.0030 -0.0109 194  GLU A O   
1560  C  CB  . GLU A 194  ? 1.3704 1.4523 1.3804 0.1909  -0.0108 -0.0141 194  GLU A CB  
1561  C  CG  . GLU A 194  ? 1.4655 1.5533 1.4822 0.1947  -0.0147 -0.0142 194  GLU A CG  
1562  C  CD  . GLU A 194  ? 1.6723 1.7598 1.6796 0.2049  -0.0188 -0.0146 194  GLU A CD  
1563  O  OE1 . GLU A 194  ? 1.5981 1.6789 1.5918 0.2090  -0.0180 -0.0142 194  GLU A OE1 
1564  O  OE2 . GLU A 194  ? 1.8765 1.9706 1.8898 0.2089  -0.0229 -0.0153 194  GLU A OE2 
1565  N  N   . ILE A 195  ? 0.8932 0.9596 0.9000 0.1785  0.0053  -0.0068 195  ILE A N   
1566  C  CA  . ILE A 195  ? 0.8502 0.9104 0.8562 0.1752  0.0112  -0.0034 195  ILE A CA  
1567  C  C   . ILE A 195  ? 0.8152 0.8791 0.8327 0.1661  0.0130  -0.0043 195  ILE A C   
1568  O  O   . ILE A 195  ? 0.8454 0.9102 0.8697 0.1632  0.0143  -0.0032 195  ILE A O   
1569  C  CB  . ILE A 195  ? 0.8462 0.8923 0.8349 0.1770  0.0184  0.0003  195  ILE A CB  
1570  C  CG1 . ILE A 195  ? 0.9367 0.9784 0.9130 0.1870  0.0165  0.0014  195  ILE A CG1 
1571  C  CG2 . ILE A 195  ? 0.9471 0.9861 0.9346 0.1730  0.0246  0.0035  195  ILE A CG2 
1572  C  CD1 . ILE A 195  ? 1.0784 1.1228 1.0575 0.1923  0.0136  0.0023  195  ILE A CD1 
1573  N  N   . GLY A 196  ? 0.9979 1.0641 1.0177 0.1618  0.0130  -0.0063 196  GLY A N   
1574  C  CA  . GLY A 196  ? 0.9608 1.0304 0.9907 0.1537  0.0147  -0.0072 196  GLY A CA  
1575  C  C   . GLY A 196  ? 0.9806 1.0603 1.0257 0.1518  0.0094  -0.0095 196  GLY A C   
1576  O  O   . GLY A 196  ? 0.9521 1.0326 1.0044 0.1469  0.0114  -0.0088 196  GLY A O   
1577  N  N   . ARG A 197  ? 1.0921 1.1792 1.1421 0.1555  0.0028  -0.0125 197  ARG A N   
1578  C  CA  . ARG A 197  ? 1.0793 1.1759 1.1438 0.1536  -0.0021 -0.0149 197  ARG A CA  
1579  C  C   . ARG A 197  ? 1.0417 1.1387 1.1097 0.1551  -0.0014 -0.0129 197  ARG A C   
1580  O  O   . ARG A 197  ? 1.0442 1.1455 1.1230 0.1510  -0.0017 -0.0132 197  ARG A O   
1581  C  CB  . ARG A 197  ? 1.1624 1.2664 1.2305 0.1574  -0.0092 -0.0187 197  ARG A CB  
1582  C  CG  . ARG A 197  ? 1.1644 1.2692 1.2312 0.1555  -0.0104 -0.0212 197  ARG A CG  
1583  C  CD  . ARG A 197  ? 1.2161 1.3299 1.2927 0.1559  -0.0176 -0.0256 197  ARG A CD  
1584  N  NE  . ARG A 197  ? 1.3501 1.4641 1.4252 0.1542  -0.0186 -0.0281 197  ARG A NE  
1585  C  CZ  . ARG A 197  ? 1.3710 1.4848 1.4390 0.1588  -0.0217 -0.0300 197  ARG A CZ  
1586  N  NH1 . ARG A 197  ? 1.2698 1.3832 1.3314 0.1655  -0.0244 -0.0300 197  ARG A NH1 
1587  N  NH2 . ARG A 197  ? 1.3806 1.4946 1.4477 0.1570  -0.0222 -0.0321 197  ARG A NH2 
1588  N  N   . GLN A 198  ? 1.1602 1.2525 1.2186 0.1614  -0.0005 -0.0107 198  GLN A N   
1589  C  CA  . GLN A 198  ? 1.1859 1.2778 1.2462 0.1636  0.0006  -0.0085 198  GLN A CA  
1590  C  C   . GLN A 198  ? 1.2460 1.3310 1.3052 0.1582  0.0072  -0.0056 198  GLN A C   
1591  O  O   . GLN A 198  ? 1.3022 1.3899 1.3694 0.1563  0.0077  -0.0049 198  GLN A O   
1592  C  CB  . GLN A 198  ? 1.3240 1.4111 1.3724 0.1721  0.0005  -0.0068 198  GLN A CB  
1593  C  CG  . GLN A 198  ? 1.4939 1.5802 1.5429 0.1755  0.0017  -0.0044 198  GLN A CG  
1594  C  CD  . GLN A 198  ? 1.6553 1.7349 1.6903 0.1843  0.0024  -0.0022 198  GLN A CD  
1595  O  OE1 . GLN A 198  ? 1.5780 1.6517 1.6013 0.1872  0.0031  -0.0019 198  GLN A OE1 
1596  N  NE2 . GLN A 198  ? 1.6921 1.7725 1.7278 0.1888  0.0023  -0.0006 198  GLN A NE2 
1597  N  N   . LEU A 199  ? 0.8309 0.9071 0.8804 0.1555  0.0124  -0.0039 199  LEU A N   
1598  C  CA  . LEU A 199  ? 0.7984 0.8680 0.8465 0.1501  0.0186  -0.0015 199  LEU A CA  
1599  C  C   . LEU A 199  ? 0.7758 0.8515 0.8365 0.1430  0.0178  -0.0033 199  LEU A C   
1600  O  O   . LEU A 199  ? 0.7458 0.8198 0.8101 0.1397  0.0206  -0.0019 199  LEU A O   
1601  C  CB  . LEU A 199  ? 0.6826 0.7419 0.7177 0.1486  0.0242  0.0003  199  LEU A CB  
1602  C  CG  . LEU A 199  ? 0.6656 0.7150 0.6858 0.1547  0.0274  0.0032  199  LEU A CG  
1603  C  CD1 . LEU A 199  ? 0.7370 0.7763 0.7455 0.1519  0.0336  0.0048  199  LEU A CD1 
1604  C  CD2 . LEU A 199  ? 0.7819 0.8270 0.8008 0.1568  0.0296  0.0058  199  LEU A CD2 
1605  N  N   . VAL A 200  ? 0.6342 0.7166 0.7011 0.1410  0.0141  -0.0064 200  VAL A N   
1606  C  CA  . VAL A 200  ? 0.5755 0.6634 0.6539 0.1350  0.0130  -0.0082 200  VAL A CA  
1607  C  C   . VAL A 200  ? 0.5358 0.6300 0.6250 0.1354  0.0101  -0.0086 200  VAL A C   
1608  O  O   . VAL A 200  ? 0.5375 0.6323 0.6332 0.1310  0.0118  -0.0081 200  VAL A O   
1609  C  CB  . VAL A 200  ? 0.4855 0.5786 0.5672 0.1336  0.0095  -0.0114 200  VAL A CB  
1610  C  CG1 . VAL A 200  ? 0.4063 0.5063 0.5009 0.1291  0.0068  -0.0137 200  VAL A CG1 
1611  C  CG2 . VAL A 200  ? 0.5280 0.6156 0.6014 0.1311  0.0136  -0.0109 200  VAL A CG2 
1612  N  N   . ALA A 201  ? 0.6426 0.7415 0.7337 0.1409  0.0058  -0.0096 201  ALA A N   
1613  C  CA  . ALA A 201  ? 0.6455 0.7512 0.7475 0.1414  0.0032  -0.0101 201  ALA A CA  
1614  C  C   . ALA A 201  ? 0.6144 0.7151 0.7136 0.1424  0.0075  -0.0067 201  ALA A C   
1615  O  O   . ALA A 201  ? 0.5084 0.6121 0.6163 0.1399  0.0080  -0.0064 201  ALA A O   
1616  C  CB  . ALA A 201  ? 0.6501 0.7631 0.7553 0.1470  -0.0028 -0.0125 201  ALA A CB  
1617  N  N   . GLU A 202  ? 0.9298 1.0222 1.0165 0.1461  0.0109  -0.0041 202  GLU A N   
1618  C  CA  . GLU A 202  ? 1.0756 1.1622 1.1583 0.1477  0.0150  -0.0008 202  GLU A CA  
1619  C  C   . GLU A 202  ? 0.9793 1.0597 1.0612 0.1412  0.0203  0.0008  202  GLU A C   
1620  O  O   . GLU A 202  ? 0.8431 0.9230 0.9289 0.1401  0.0223  0.0022  202  GLU A O   
1621  C  CB  . GLU A 202  ? 1.0215 1.1000 1.0899 0.1539  0.0171  0.0015  202  GLU A CB  
1622  C  CG  . GLU A 202  ? 1.1401 1.2114 1.2029 0.1563  0.0216  0.0049  202  GLU A CG  
1623  C  CD  . GLU A 202  ? 1.2798 1.3401 1.3262 0.1616  0.0248  0.0076  202  GLU A CD  
1624  O  OE1 . GLU A 202  ? 1.2931 1.3530 1.3334 0.1648  0.0228  0.0067  202  GLU A OE1 
1625  O  OE2 . GLU A 202  ? 1.3113 1.3629 1.3505 0.1626  0.0296  0.0106  202  GLU A OE2 
1626  N  N   . TYR A 203  ? 0.7793 0.8552 0.8561 0.1371  0.0226  0.0005  203  TYR A N   
1627  C  CA  . TYR A 203  ? 0.6709 0.7414 0.7468 0.1309  0.0273  0.0015  203  TYR A CA  
1628  C  C   . TYR A 203  ? 0.6876 0.7651 0.7755 0.1256  0.0253  -0.0005 203  TYR A C   
1629  O  O   . TYR A 203  ? 0.8181 0.8920 0.9063 0.1207  0.0286  0.0001  203  TYR A O   
1630  C  CB  . TYR A 203  ? 0.7268 0.7901 0.7925 0.1286  0.0309  0.0020  203  TYR A CB  
1631  C  CG  . TYR A 203  ? 0.7827 0.8369 0.8348 0.1333  0.0340  0.0044  203  TYR A CG  
1632  C  CD1 . TYR A 203  ? 0.7819 0.8320 0.8299 0.1380  0.0352  0.0068  203  TYR A CD1 
1633  C  CD2 . TYR A 203  ? 0.7949 0.8442 0.8378 0.1332  0.0360  0.0044  203  TYR A CD2 
1634  C  CE1 . TYR A 203  ? 0.8408 0.8815 0.8753 0.1428  0.0382  0.0092  203  TYR A CE1 
1635  C  CE2 . TYR A 203  ? 0.7819 0.8218 0.8114 0.1376  0.0393  0.0068  203  TYR A CE2 
1636  C  CZ  . TYR A 203  ? 0.8394 0.8747 0.8644 0.1425  0.0403  0.0092  203  TYR A CZ  
1637  O  OH  . TYR A 203  ? 0.9081 0.9330 0.9189 0.1474  0.0437  0.0118  203  TYR A OH  
1638  N  N   . GLY A 204  ? 0.7233 0.8099 0.8205 0.1264  0.0200  -0.0031 204  GLY A N   
1639  C  CA  . GLY A 204  ? 0.7311 0.8233 0.8390 0.1217  0.0183  -0.0050 204  GLY A CA  
1640  C  C   . GLY A 204  ? 0.7494 0.8404 0.8561 0.1169  0.0193  -0.0063 204  GLY A C   
1641  O  O   . GLY A 204  ? 0.8436 0.9354 0.9555 0.1125  0.0201  -0.0067 204  GLY A O   
1642  N  N   . ILE A 205  ? 0.6440 0.7331 0.7436 0.1179  0.0193  -0.0070 205  ILE A N   
1643  C  CA  . ILE A 205  ? 0.6778 0.7673 0.7771 0.1138  0.0199  -0.0086 205  ILE A CA  
1644  C  C   . ILE A 205  ? 0.7362 0.8334 0.8458 0.1124  0.0153  -0.0115 205  ILE A C   
1645  O  O   . ILE A 205  ? 0.6553 0.7574 0.7684 0.1155  0.0109  -0.0132 205  ILE A O   
1646  C  CB  . ILE A 205  ? 0.7144 0.8008 0.8044 0.1158  0.0208  -0.0087 205  ILE A CB  
1647  C  CG1 . ILE A 205  ? 0.6933 0.7708 0.7724 0.1171  0.0259  -0.0057 205  ILE A CG1 
1648  C  CG2 . ILE A 205  ? 0.7441 0.8321 0.8347 0.1117  0.0215  -0.0105 205  ILE A CG2 
1649  C  CD1 . ILE A 205  ? 0.6439 0.7168 0.7129 0.1180  0.0283  -0.0055 205  ILE A CD1 
1650  N  N   . MET A 206  ? 0.8684 0.9664 0.9826 0.1078  0.0162  -0.0121 206  MET A N   
1651  C  CA  . MET A 206  ? 0.7912 0.8950 0.9147 0.1064  0.0124  -0.0145 206  MET A CA  
1652  C  C   . MET A 206  ? 0.8367 0.9440 0.9600 0.1073  0.0092  -0.0172 206  MET A C   
1653  O  O   . MET A 206  ? 0.8723 0.9774 0.9885 0.1077  0.0108  -0.0172 206  MET A O   
1654  C  CB  . MET A 206  ? 0.6958 0.7987 0.8228 0.1018  0.0144  -0.0143 206  MET A CB  
1655  C  CG  . MET A 206  ? 0.7750 0.8761 0.9052 0.1011  0.0162  -0.0122 206  MET A CG  
1656  S  SD  . MET A 206  ? 0.8264 0.9333 0.9671 0.1027  0.0123  -0.0132 206  MET A SD  
1657  C  CE  . MET A 206  ? 0.8710 0.9804 1.0185 0.0990  0.0105  -0.0155 206  MET A CE  
1658  N  N   . PRO A 207  ? 0.6055 0.7178 0.7362 0.1075  0.0049  -0.0196 207  PRO A N   
1659  C  CA  . PRO A 207  ? 0.6021 0.7174 0.7323 0.1088  0.0015  -0.0224 207  PRO A CA  
1660  C  C   . PRO A 207  ? 0.6605 0.7750 0.7885 0.1060  0.0032  -0.0232 207  PRO A C   
1661  O  O   . PRO A 207  ? 0.6340 0.7465 0.7623 0.1028  0.0063  -0.0220 207  PRO A O   
1662  C  CB  . PRO A 207  ? 0.7013 0.8213 0.8409 0.1087  -0.0029 -0.0246 207  PRO A CB  
1663  C  CG  . PRO A 207  ? 0.7944 0.9135 0.9396 0.1056  -0.0008 -0.0231 207  PRO A CG  
1664  C  CD  . PRO A 207  ? 0.7060 0.8213 0.8460 0.1066  0.0031  -0.0199 207  PRO A CD  
1665  N  N   . PRO A 208  ? 0.7226 0.8389 0.8482 0.1074  0.0011  -0.0254 208  PRO A N   
1666  C  CA  . PRO A 208  ? 0.7100 0.8265 0.8338 0.1052  0.0027  -0.0264 208  PRO A CA  
1667  C  C   . PRO A 208  ? 0.6871 0.8053 0.8176 0.1022  0.0018  -0.0275 208  PRO A C   
1668  O  O   . PRO A 208  ? 0.5780 0.6965 0.7073 0.1002  0.0036  -0.0279 208  PRO A O   
1669  C  CB  . PRO A 208  ? 0.6421 0.7605 0.7627 0.1082  -0.0001 -0.0287 208  PRO A CB  
1670  C  CG  . PRO A 208  ? 0.8182 0.9356 0.9351 0.1120  -0.0013 -0.0280 208  PRO A CG  
1671  C  CD  . PRO A 208  ? 0.8464 0.9643 0.9695 0.1116  -0.0024 -0.0270 208  PRO A CD  
1672  N  N   . ASP A 209  ? 0.9528 1.0720 1.0900 0.1019  -0.0007 -0.0279 209  ASP A N   
1673  C  CA  . ASP A 209  ? 0.8333 0.9530 0.9759 0.0994  -0.0013 -0.0288 209  ASP A CA  
1674  C  C   . ASP A 209  ? 0.9163 1.0337 1.0580 0.0965  0.0026  -0.0268 209  ASP A C   
1675  O  O   . ASP A 209  ? 1.0401 1.1579 1.1824 0.0948  0.0030  -0.0276 209  ASP A O   
1676  C  CB  . ASP A 209  ? 0.8936 1.0143 1.0435 0.0993  -0.0040 -0.0294 209  ASP A CB  
1677  C  CG  . ASP A 209  ? 1.1521 1.2754 1.3033 0.1020  -0.0082 -0.0317 209  ASP A CG  
1678  O  OD1 . ASP A 209  ? 1.1682 1.2922 1.3141 0.1042  -0.0092 -0.0329 209  ASP A OD1 
1679  O  OD2 . ASP A 209  ? 1.2593 1.3841 1.4166 0.1019  -0.0105 -0.0324 209  ASP A OD2 
1680  N  N   . GLN A 210  ? 0.5981 0.7130 0.7382 0.0960  0.0054  -0.0243 210  GLN A N   
1681  C  CA  . GLN A 210  ? 0.4349 0.5471 0.5734 0.0933  0.0090  -0.0225 210  GLN A CA  
1682  C  C   . GLN A 210  ? 0.4362 0.5476 0.5682 0.0923  0.0120  -0.0223 210  GLN A C   
1683  O  O   . GLN A 210  ? 0.4453 0.5569 0.5769 0.0899  0.0135  -0.0227 210  GLN A O   
1684  C  CB  . GLN A 210  ? 0.4561 0.5654 0.5953 0.0932  0.0110  -0.0200 210  GLN A CB  
1685  C  CG  . GLN A 210  ? 0.5404 0.6461 0.6767 0.0905  0.0149  -0.0182 210  GLN A CG  
1686  C  CD  . GLN A 210  ? 0.5806 0.6823 0.7133 0.0912  0.0178  -0.0156 210  GLN A CD  
1687  O  OE1 . GLN A 210  ? 0.7215 0.8198 0.8482 0.0900  0.0210  -0.0145 210  GLN A OE1 
1688  N  NE2 . GLN A 210  ? 0.5954 0.6975 0.7319 0.0931  0.0167  -0.0146 210  GLN A NE2 
1689  N  N   . LEU A 211  ? 0.5106 0.6210 0.6374 0.0943  0.0128  -0.0218 211  LEU A N   
1690  C  CA  . LEU A 211  ? 0.5357 0.6445 0.6561 0.0930  0.0164  -0.0213 211  LEU A CA  
1691  C  C   . LEU A 211  ? 0.5007 0.6134 0.6212 0.0921  0.0159  -0.0236 211  LEU A C   
1692  O  O   . LEU A 211  ? 0.4226 0.5350 0.5395 0.0899  0.0191  -0.0235 211  LEU A O   
1693  C  CB  . LEU A 211  ? 0.4178 0.5240 0.5318 0.0958  0.0174  -0.0201 211  LEU A CB  
1694  C  CG  . LEU A 211  ? 0.3930 0.4950 0.5054 0.0972  0.0186  -0.0175 211  LEU A CG  
1695  C  CD1 . LEU A 211  ? 0.4510 0.5498 0.5557 0.1004  0.0199  -0.0164 211  LEU A CD1 
1696  C  CD2 . LEU A 211  ? 0.4686 0.5667 0.5800 0.0938  0.0225  -0.0158 211  LEU A CD2 
1697  N  N   . THR A 212  ? 0.9139 1.0301 1.0384 0.0936  0.0120  -0.0258 212  THR A N   
1698  C  CA  . THR A 212  ? 0.9208 1.0410 1.0458 0.0933  0.0113  -0.0281 212  THR A CA  
1699  C  C   . THR A 212  ? 0.9143 1.0360 1.0436 0.0911  0.0109  -0.0288 212  THR A C   
1700  O  O   . THR A 212  ? 0.8424 0.9678 0.9726 0.0912  0.0100  -0.0309 212  THR A O   
1701  C  CB  . THR A 212  ? 0.8236 0.9460 0.9494 0.0965  0.0074  -0.0302 212  THR A CB  
1702  O  OG1 . THR A 212  ? 0.8924 1.0142 1.0232 0.0975  0.0041  -0.0304 212  THR A OG1 
1703  C  CG2 . THR A 212  ? 0.8336 0.9550 0.9535 0.0990  0.0081  -0.0298 212  THR A CG2 
1704  N  N   . ASN A 213  ? 0.6543 0.7734 0.7860 0.0895  0.0116  -0.0273 213  ASN A N   
1705  C  CA  . ASN A 213  ? 0.5948 0.7146 0.7295 0.0878  0.0113  -0.0279 213  ASN A CA  
1706  C  C   . ASN A 213  ? 0.5411 0.6628 0.6734 0.0854  0.0140  -0.0284 213  ASN A C   
1707  O  O   . ASN A 213  ? 0.5437 0.6644 0.6722 0.0840  0.0171  -0.0275 213  ASN A O   
1708  C  CB  . ASN A 213  ? 0.5114 0.6273 0.6484 0.0869  0.0118  -0.0259 213  ASN A CB  
1709  C  CG  . ASN A 213  ? 0.5830 0.6982 0.7241 0.0887  0.0090  -0.0259 213  ASN A CG  
1710  O  OD1 . ASN A 213  ? 0.5060 0.6184 0.6486 0.0885  0.0097  -0.0241 213  ASN A OD1 
1711  N  ND2 . ASN A 213  ? 0.7111 0.8286 0.8538 0.0905  0.0059  -0.0280 213  ASN A ND2 
1712  N  N   . CYS A 214  ? 0.4292 0.5537 0.5639 0.0850  0.0128  -0.0299 214  CYS A N   
1713  C  CA  . CYS A 214  ? 0.3715 0.4994 0.5050 0.0828  0.0148  -0.0310 214  CYS A CA  
1714  C  C   . CYS A 214  ? 0.4171 0.5418 0.5488 0.0796  0.0178  -0.0294 214  CYS A C   
1715  O  O   . CYS A 214  ? 0.3780 0.5038 0.5073 0.0771  0.0207  -0.0297 214  CYS A O   
1716  C  CB  . CYS A 214  ? 0.4439 0.5757 0.5801 0.0839  0.0123  -0.0332 214  CYS A CB  
1717  S  SG  . CYS A 214  ? 0.4949 0.6297 0.6326 0.0878  0.0088  -0.0353 214  CYS A SG  
1718  N  N   . TYR A 215  ? 0.6966 0.8169 0.8294 0.0795  0.0174  -0.0279 215  TYR A N   
1719  C  CA  . TYR A 215  ? 0.6841 0.8010 0.8150 0.0768  0.0200  -0.0266 215  TYR A CA  
1720  C  C   . TYR A 215  ? 0.6724 0.7847 0.7996 0.0757  0.0231  -0.0244 215  TYR A C   
1721  O  O   . TYR A 215  ? 0.7764 0.8850 0.9010 0.0733  0.0256  -0.0234 215  TYR A O   
1722  C  CB  . TYR A 215  ? 0.6614 0.7750 0.7944 0.0775  0.0188  -0.0255 215  TYR A CB  
1723  C  CG  . TYR A 215  ? 0.6263 0.7426 0.7604 0.0775  0.0172  -0.0273 215  TYR A CG  
1724  C  CD1 . TYR A 215  ? 0.5754 0.6977 0.7095 0.0767  0.0170  -0.0298 215  TYR A CD1 
1725  C  CD2 . TYR A 215  ? 0.6263 0.7395 0.7615 0.0785  0.0161  -0.0266 215  TYR A CD2 
1726  C  CE1 . TYR A 215  ? 0.5842 0.7097 0.7193 0.0772  0.0152  -0.0315 215  TYR A CE1 
1727  C  CE2 . TYR A 215  ? 0.5796 0.6948 0.7150 0.0791  0.0146  -0.0281 215  TYR A CE2 
1728  C  CZ  . TYR A 215  ? 0.5820 0.7036 0.7173 0.0786  0.0139  -0.0307 215  TYR A CZ  
1729  O  OH  . TYR A 215  ? 0.6093 0.7334 0.7447 0.0798  0.0121  -0.0324 215  TYR A OH  
1730  N  N   . VAL A 216  ? 0.3974 0.5092 0.5234 0.0776  0.0230  -0.0238 216  VAL A N   
1731  C  CA  . VAL A 216  ? 0.4021 0.5093 0.5232 0.0769  0.0262  -0.0218 216  VAL A CA  
1732  C  C   . VAL A 216  ? 0.5769 0.6847 0.6943 0.0737  0.0295  -0.0227 216  VAL A C   
1733  O  O   . VAL A 216  ? 0.7088 0.8115 0.8217 0.0717  0.0330  -0.0212 216  VAL A O   
1734  C  CB  . VAL A 216  ? 0.3704 0.4774 0.4907 0.0803  0.0249  -0.0213 216  VAL A CB  
1735  C  CG1 . VAL A 216  ? 0.4123 0.5142 0.5264 0.0802  0.0283  -0.0192 216  VAL A CG1 
1736  C  CG2 . VAL A 216  ? 0.4333 0.5398 0.5579 0.0828  0.0218  -0.0206 216  VAL A CG2 
1737  N  N   . CYS A 217  ? 0.5515 0.6656 0.6708 0.0730  0.0287  -0.0252 217  CYS A N   
1738  C  CA  . CYS A 217  ? 0.5573 0.6734 0.6743 0.0696  0.0319  -0.0264 217  CYS A CA  
1739  C  C   . CYS A 217  ? 0.6511 0.7720 0.7715 0.0671  0.0311  -0.0286 217  CYS A C   
1740  O  O   . CYS A 217  ? 0.7947 0.9132 0.9136 0.0639  0.0332  -0.0285 217  CYS A O   
1741  C  CB  . CYS A 217  ? 0.6619 0.7822 0.7781 0.0708  0.0322  -0.0276 217  CYS A CB  
1742  S  SG  . CYS A 217  ? 0.7304 0.8455 0.8421 0.0746  0.0324  -0.0253 217  CYS A SG  
1743  N  N   . HIS A 218  ? 0.6044 0.7320 0.7291 0.0690  0.0279  -0.0308 218  HIS A N   
1744  C  CA  . HIS A 218  ? 0.6425 0.7755 0.7702 0.0674  0.0268  -0.0331 218  HIS A CA  
1745  C  C   . HIS A 218  ? 0.6113 0.7405 0.7397 0.0678  0.0252  -0.0322 218  HIS A C   
1746  O  O   . HIS A 218  ? 0.5208 0.6459 0.6496 0.0704  0.0235  -0.0305 218  HIS A O   
1747  C  CB  . HIS A 218  ? 0.5783 0.7190 0.7096 0.0701  0.0239  -0.0356 218  HIS A CB  
1748  C  CG  . HIS A 218  ? 0.6601 0.8040 0.7905 0.0707  0.0253  -0.0362 218  HIS A CG  
1749  N  ND1 . HIS A 218  ? 0.6798 0.8273 0.8093 0.0674  0.0288  -0.0374 218  HIS A ND1 
1750  C  CD2 . HIS A 218  ? 0.7663 0.9100 0.8962 0.0742  0.0238  -0.0359 218  HIS A CD2 
1751  C  CE1 . HIS A 218  ? 0.8266 0.9758 0.9547 0.0691  0.0296  -0.0375 218  HIS A CE1 
1752  N  NE2 . HIS A 218  ? 0.7625 0.9094 0.8907 0.0733  0.0264  -0.0367 218  HIS A NE2 
1753  N  N   . ARG A 219  ? 0.6835 0.8142 0.8119 0.0650  0.0258  -0.0335 219  ARG A N   
1754  C  CA  . ARG A 219  ? 0.5916 0.7187 0.7199 0.0654  0.0244  -0.0329 219  ARG A CA  
1755  C  C   . ARG A 219  ? 0.6132 0.7467 0.7436 0.0648  0.0226  -0.0358 219  ARG A C   
1756  O  O   . ARG A 219  ? 0.6895 0.8231 0.8185 0.0615  0.0239  -0.0368 219  ARG A O   
1757  C  CB  . ARG A 219  ? 0.5608 0.6802 0.6850 0.0627  0.0276  -0.0308 219  ARG A CB  
1758  C  CG  . ARG A 219  ? 0.5819 0.6947 0.7037 0.0640  0.0292  -0.0277 219  ARG A CG  
1759  C  CD  . ARG A 219  ? 0.6077 0.7124 0.7262 0.0633  0.0310  -0.0254 219  ARG A CD  
1760  N  NE  . ARG A 219  ? 0.6878 0.7900 0.8024 0.0591  0.0342  -0.0259 219  ARG A NE  
1761  C  CZ  . ARG A 219  ? 0.7328 0.8302 0.8431 0.0573  0.0378  -0.0246 219  ARG A CZ  
1762  N  NH1 . ARG A 219  ? 0.5944 0.6895 0.7035 0.0597  0.0384  -0.0227 219  ARG A NH1 
1763  N  NH2 . ARG A 219  ? 0.7794 0.8739 0.8860 0.0531  0.0408  -0.0254 219  ARG A NH2 
1764  N  N   . ALA B 75   ? 2.2496 2.5691 2.4593 0.0050  0.0870  -0.0857 75   ALA B N   
1765  C  CA  . ALA B 75   ? 2.2432 2.5678 2.4528 0.0138  0.0847  -0.0850 75   ALA B CA  
1766  C  C   . ALA B 75   ? 2.2531 2.5614 2.4506 0.0179  0.0870  -0.0797 75   ALA B C   
1767  O  O   . ALA B 75   ? 2.3372 2.6432 2.5312 0.0263  0.0827  -0.0781 75   ALA B O   
1768  C  CB  . ALA B 75   ? 2.2519 2.5943 2.4709 0.0123  0.0887  -0.0887 75   ALA B CB  
1769  N  N   . CYS B 76   ? 1.3734 1.6699 1.5642 0.0121  0.0938  -0.0771 76   CYS B N   
1770  C  CA  . CYS B 76   ? 1.2788 1.5596 1.4576 0.0154  0.0967  -0.0722 76   CYS B CA  
1771  C  C   . CYS B 76   ? 1.1929 1.4562 1.3629 0.0130  0.0965  -0.0688 76   CYS B C   
1772  O  O   . CYS B 76   ? 1.1663 1.4292 1.3391 0.0094  0.0936  -0.0701 76   CYS B O   
1773  C  CB  . CYS B 76   ? 1.1965 1.4781 1.3735 0.0118  0.1058  -0.0717 76   CYS B CB  
1774  S  SG  . CYS B 76   ? 1.1398 1.4439 1.3288 0.0128  0.1076  -0.0763 76   CYS B SG  
1775  N  N   . THR B 77   ? 1.4411 1.6897 1.5998 0.0155  0.0995  -0.0644 77   THR B N   
1776  C  CA  . THR B 77   ? 1.4470 1.6779 1.5958 0.0138  0.1006  -0.0606 77   THR B CA  
1777  C  C   . THR B 77   ? 1.4437 1.6695 1.5915 0.0179  0.0926  -0.0596 77   THR B C   
1778  O  O   . THR B 77   ? 1.4538 1.6670 1.5955 0.0157  0.0930  -0.0572 77   THR B O   
1779  C  CB  . THR B 77   ? 1.4869 1.7142 1.6357 0.0039  0.1070  -0.0614 77   THR B CB  
1780  O  OG1 . THR B 77   ? 1.5385 1.7735 1.6957 0.0000  0.1030  -0.0648 77   THR B OG1 
1781  C  CG2 . THR B 77   ? 1.4250 1.6597 1.5769 -0.0012 0.1151  -0.0631 77   THR B CG2 
1782  N  N   . TYR B 78   ? 1.0424 1.2774 1.1960 0.0238  0.0857  -0.0614 78   TYR B N   
1783  C  CA  . TYR B 78   ? 0.9205 1.1498 1.0722 0.0288  0.0784  -0.0600 78   TYR B CA  
1784  C  C   . TYR B 78   ? 0.8516 1.0788 1.0056 0.0242  0.0764  -0.0609 78   TYR B C   
1785  O  O   . TYR B 78   ? 0.8771 1.1089 1.0354 0.0270  0.0701  -0.0624 78   TYR B O   
1786  C  CB  . TYR B 78   ? 0.9595 1.1736 1.1004 0.0333  0.0784  -0.0554 78   TYR B CB  
1787  C  CG  . TYR B 78   ? 0.8538 1.0615 0.9926 0.0385  0.0715  -0.0537 78   TYR B CG  
1788  C  CD1 . TYR B 78   ? 0.8517 1.0632 0.9920 0.0457  0.0659  -0.0540 78   TYR B CD1 
1789  C  CD2 . TYR B 78   ? 0.8760 1.0733 1.0109 0.0362  0.0709  -0.0517 78   TYR B CD2 
1790  C  CE1 . TYR B 78   ? 0.8437 1.0491 0.9823 0.0500  0.0601  -0.0525 78   TYR B CE1 
1791  C  CE2 . TYR B 78   ? 0.8649 1.0566 0.9982 0.0408  0.0651  -0.0501 78   TYR B CE2 
1792  C  CZ  . TYR B 78   ? 0.7738 0.9697 0.9091 0.0475  0.0598  -0.0505 78   TYR B CZ  
1793  O  OH  . TYR B 78   ? 0.7070 0.8972 0.8410 0.0515  0.0544  -0.0490 78   TYR B OH  
1794  N  N   . GLN B 79   ? 0.9321 1.1516 1.0824 0.0173  0.0817  -0.0601 79   GLN B N   
1795  C  CA  . GLN B 79   ? 0.8858 1.1018 1.0370 0.0125  0.0805  -0.0609 79   GLN B CA  
1796  C  C   . GLN B 79   ? 0.9615 1.1781 1.1138 0.0032  0.0875  -0.0627 79   GLN B C   
1797  O  O   . GLN B 79   ? 0.9707 1.1843 1.1194 0.0008  0.0941  -0.0615 79   GLN B O   
1798  C  CB  . GLN B 79   ? 0.9452 1.1446 1.0870 0.0149  0.0790  -0.0567 79   GLN B CB  
1799  C  CG  . GLN B 79   ? 0.8809 1.0802 1.0250 0.0175  0.0721  -0.0571 79   GLN B CG  
1800  C  CD  . GLN B 79   ? 0.8065 0.9908 0.9421 0.0211  0.0705  -0.0528 79   GLN B CD  
1801  O  OE1 . GLN B 79   ? 0.8118 0.9878 0.9406 0.0241  0.0727  -0.0495 79   GLN B OE1 
1802  N  NE2 . GLN B 79   ? 0.7847 0.9656 0.9205 0.0209  0.0668  -0.0528 79   GLN B NE2 
1803  N  N   . PRO B 80   ? 0.9423 1.1626 1.0994 -0.0024 0.0863  -0.0657 80   PRO B N   
1804  C  CA  . PRO B 80   ? 0.9255 1.1459 1.0838 -0.0120 0.0930  -0.0677 80   PRO B CA  
1805  C  C   . PRO B 80   ? 1.0921 1.2935 1.2388 -0.0151 0.0984  -0.0637 80   PRO B C   
1806  O  O   . PRO B 80   ? 1.2503 1.4398 1.3882 -0.0096 0.0981  -0.0593 80   PRO B O   
1807  C  CB  . PRO B 80   ? 0.9510 1.1798 1.1169 -0.0157 0.0887  -0.0720 80   PRO B CB  
1808  C  CG  . PRO B 80   ? 0.9839 1.2089 1.1477 -0.0084 0.0810  -0.0703 80   PRO B CG  
1809  C  CD  . PRO B 80   ? 0.9218 1.1475 1.0839 -0.0001 0.0789  -0.0678 80   PRO B CD  
1810  N  N   . ARG B 81   ? 1.3130 1.5113 1.4596 -0.0240 0.1034  -0.0655 81   ARG B N   
1811  C  CA  . ARG B 81   ? 1.4669 1.6466 1.6018 -0.0272 0.1095  -0.0618 81   ARG B CA  
1812  C  C   . ARG B 81   ? 1.4505 1.6175 1.5786 -0.0245 0.1054  -0.0592 81   ARG B C   
1813  O  O   . ARG B 81   ? 1.6054 1.7571 1.7226 -0.0213 0.1073  -0.0546 81   ARG B O   
1814  C  CB  . ARG B 81   ? 1.4954 1.6752 1.6319 -0.0380 0.1167  -0.0646 81   ARG B CB  
1815  C  CG  . ARG B 81   ? 1.6062 1.7963 1.7481 -0.0412 0.1225  -0.0665 81   ARG B CG  
1816  C  CD  . ARG B 81   ? 1.6665 1.8525 1.8075 -0.0521 0.1311  -0.0682 81   ARG B CD  
1817  N  NE  . ARG B 81   ? 1.7442 1.9096 1.8708 -0.0528 0.1378  -0.0633 81   ARG B NE  
1818  C  CZ  . ARG B 81   ? 1.6453 1.8057 1.7658 -0.0511 0.1439  -0.0603 81   ARG B CZ  
1819  N  NH1 . ARG B 81   ? 1.5070 1.6812 1.6344 -0.0488 0.1444  -0.0617 81   ARG B NH1 
1820  N  NH2 . ARG B 81   ? 1.6403 1.7810 1.7468 -0.0514 0.1497  -0.0558 81   ARG B NH2 
1821  N  N   . GLN B 82   ? 0.8211 0.9942 0.9551 -0.0254 0.0998  -0.0622 82   GLN B N   
1822  C  CA  . GLN B 82   ? 0.8248 0.9868 0.9530 -0.0231 0.0960  -0.0602 82   GLN B CA  
1823  C  C   . GLN B 82   ? 0.8320 0.9765 0.9497 -0.0281 0.1021  -0.0578 82   GLN B C   
1824  O  O   . GLN B 82   ? 0.8885 1.0196 0.9963 -0.0243 0.1044  -0.0530 82   GLN B O   
1825  C  CB  . GLN B 82   ? 0.9250 1.0831 1.0497 -0.0133 0.0909  -0.0563 82   GLN B CB  
1826  C  CG  . GLN B 82   ? 1.0200 1.1923 1.1535 -0.0077 0.0836  -0.0585 82   GLN B CG  
1827  C  CD  . GLN B 82   ? 0.8605 1.0267 0.9900 0.0009  0.0784  -0.0549 82   GLN B CD  
1828  O  OE1 . GLN B 82   ? 0.5994 0.7736 0.7331 0.0067  0.0743  -0.0551 82   GLN B OE1 
1829  N  NE2 . GLN B 82   ? 0.9519 1.1038 1.0733 0.0016  0.0788  -0.0516 82   GLN B NE2 
1830  N  N   . TYR B 83   ? 0.8611 1.0056 0.9806 -0.0365 0.1046  -0.0611 83   TYR B N   
1831  C  CA  . TYR B 83   ? 0.7850 0.9121 0.8941 -0.0416 0.1106  -0.0591 83   TYR B CA  
1832  C  C   . TYR B 83   ? 0.6153 0.7300 0.7170 -0.0373 0.1068  -0.0562 83   TYR B C   
1833  O  O   . TYR B 83   ? 0.5595 0.6801 0.6654 -0.0321 0.0996  -0.0567 83   TYR B O   
1834  C  CB  . TYR B 83   ? 0.8280 0.9589 0.9415 -0.0523 0.1145  -0.0640 83   TYR B CB  
1835  C  CG  . TYR B 83   ? 0.9378 1.0809 1.0589 -0.0575 0.1192  -0.0670 83   TYR B CG  
1836  C  CD1 . TYR B 83   ? 0.9808 1.1445 1.1151 -0.0567 0.1148  -0.0712 83   TYR B CD1 
1837  C  CD2 . TYR B 83   ? 0.9707 1.1044 1.0855 -0.0631 0.1283  -0.0656 83   TYR B CD2 
1838  C  CE1 . TYR B 83   ? 1.0186 1.1943 1.1604 -0.0613 0.1193  -0.0740 83   TYR B CE1 
1839  C  CE2 . TYR B 83   ? 1.0494 1.1943 1.1713 -0.0680 0.1332  -0.0682 83   TYR B CE2 
1840  C  CZ  . TYR B 83   ? 1.0740 1.2403 1.2097 -0.0671 0.1286  -0.0725 83   TYR B CZ  
1841  O  OH  . TYR B 83   ? 1.1296 1.3078 1.2729 -0.0718 0.1336  -0.0752 83   TYR B OH  
1842  N  N   . ILE B 84   ? 0.7153 0.8122 0.8055 -0.0394 0.1120  -0.0532 84   ILE B N   
1843  C  CA  . ILE B 84   ? 0.6463 0.7301 0.7285 -0.0357 0.1096  -0.0503 84   ILE B CA  
1844  C  C   . ILE B 84   ? 0.7480 0.8186 0.8228 -0.0434 0.1150  -0.0510 84   ILE B C   
1845  O  O   . ILE B 84   ? 0.8574 0.9198 0.9264 -0.0483 0.1224  -0.0502 84   ILE B O   
1846  C  CB  . ILE B 84   ? 0.7023 0.7757 0.7759 -0.0273 0.1097  -0.0444 84   ILE B CB  
1847  C  CG1 . ILE B 84   ? 0.6602 0.7190 0.7249 -0.0243 0.1085  -0.0413 84   ILE B CG1 
1848  C  CG2 . ILE B 84   ? 0.8570 0.9229 0.9236 -0.0288 0.1172  -0.0420 84   ILE B CG2 
1849  C  CD1 . ILE B 84   ? 0.7764 0.8289 0.8356 -0.0150 0.1064  -0.0363 84   ILE B CD1 
1850  N  N   . ALA B 85   ? 0.6005 0.6687 0.6752 -0.0446 0.1114  -0.0527 85   ALA B N   
1851  C  CA  . ALA B 85   ? 0.6319 0.6883 0.7002 -0.0521 0.1157  -0.0542 85   ALA B CA  
1852  C  C   . ALA B 85   ? 0.5488 0.5892 0.6065 -0.0475 0.1146  -0.0504 85   ALA B C   
1853  O  O   . ALA B 85   ? 0.5197 0.5632 0.5801 -0.0446 0.1087  -0.0514 85   ALA B O   
1854  C  CB  . ALA B 85   ? 0.6075 0.6762 0.6854 -0.0589 0.1128  -0.0607 85   ALA B CB  
1855  N  N   . PRO B 86   ? 0.7929 0.8161 0.8383 -0.0462 0.1203  -0.0460 86   PRO B N   
1856  C  CA  . PRO B 86   ? 0.8342 0.8424 0.8695 -0.0415 0.1195  -0.0424 86   PRO B CA  
1857  C  C   . PRO B 86   ? 0.7887 0.7864 0.8184 -0.0484 0.1220  -0.0448 86   PRO B C   
1858  O  O   . PRO B 86   ? 0.7314 0.7358 0.7669 -0.0568 0.1229  -0.0499 86   PRO B O   
1859  C  CB  . PRO B 86   ? 0.8468 0.8417 0.8712 -0.0373 0.1247  -0.0370 86   PRO B CB  
1860  C  CG  . PRO B 86   ? 0.7880 0.7840 0.8128 -0.0442 0.1312  -0.0386 86   PRO B CG  
1861  C  CD  . PRO B 86   ? 0.7793 0.7960 0.8191 -0.0482 0.1276  -0.0438 86   PRO B CD  
1862  N  N   . PHE B 87   ? 1.0382 1.0197 1.0567 -0.0450 0.1231  -0.0414 87   PHE B N   
1863  C  CA  . PHE B 87   ? 1.0773 1.0470 1.0890 -0.0506 0.1254  -0.0433 87   PHE B CA  
1864  C  C   . PHE B 87   ? 1.1477 1.1038 1.1504 -0.0580 0.1343  -0.0433 87   PHE B C   
1865  O  O   . PHE B 87   ? 1.1802 1.1356 1.1814 -0.0582 0.1388  -0.0414 87   PHE B O   
1866  C  CB  . PHE B 87   ? 1.0453 1.0027 1.0482 -0.0436 0.1234  -0.0396 87   PHE B CB  
1867  C  CG  . PHE B 87   ? 1.0065 0.9742 1.0169 -0.0397 0.1156  -0.0411 87   PHE B CG  
1868  C  CD1 . PHE B 87   ? 1.0714 1.0421 1.0847 -0.0452 0.1132  -0.0460 87   PHE B CD1 
1869  C  CD2 . PHE B 87   ? 1.0150 0.9888 1.0289 -0.0305 0.1107  -0.0379 87   PHE B CD2 
1870  C  CE1 . PHE B 87   ? 0.9240 0.9034 0.9431 -0.0412 0.1063  -0.0472 87   PHE B CE1 
1871  C  CE2 . PHE B 87   ? 0.8447 0.8269 0.8648 -0.0269 0.1040  -0.0391 87   PHE B CE2 
1872  C  CZ  . PHE B 87   ? 0.8573 0.8420 0.8796 -0.0321 0.1019  -0.0437 87   PHE B CZ  
1873  N  N   . ASP B 88   ? 1.2406 1.1853 1.2367 -0.0641 0.1370  -0.0455 88   ASP B N   
1874  C  CA  . ASP B 88   ? 1.2891 1.2153 1.2729 -0.0698 0.1458  -0.0444 88   ASP B CA  
1875  C  C   . ASP B 88   ? 1.3225 1.2279 1.2912 -0.0645 0.1478  -0.0400 88   ASP B C   
1876  O  O   . ASP B 88   ? 1.2905 1.1791 1.2468 -0.0650 0.1549  -0.0367 88   ASP B O   
1877  C  CB  . ASP B 88   ? 1.3849 1.3121 1.3717 -0.0819 0.1484  -0.0507 88   ASP B CB  
1878  C  CG  . ASP B 88   ? 1.4205 1.3474 1.4080 -0.0833 0.1435  -0.0540 88   ASP B CG  
1879  O  OD1 . ASP B 88   ? 1.3736 1.3102 1.3668 -0.0763 0.1360  -0.0536 88   ASP B OD1 
1880  O  OD2 . ASP B 88   ? 1.4070 1.3233 1.3886 -0.0913 0.1472  -0.0571 88   ASP B OD2 
1881  N  N   . ARG B 89   ? 1.0518 0.9580 1.0210 -0.0594 0.1420  -0.0397 89   ARG B N   
1882  C  CA  . ARG B 89   ? 1.0407 0.9300 0.9971 -0.0525 0.1428  -0.0351 89   ARG B CA  
1883  C  C   . ARG B 89   ? 0.9647 0.8642 0.9275 -0.0430 0.1352  -0.0331 89   ARG B C   
1884  O  O   . ARG B 89   ? 0.8365 0.7490 0.8091 -0.0439 0.1292  -0.0366 89   ARG B O   
1885  C  CB  . ARG B 89   ? 1.1115 0.9869 1.0594 -0.0581 0.1451  -0.0377 89   ARG B CB  
1886  C  CG  . ARG B 89   ? 1.1417 1.0026 1.0805 -0.0672 0.1536  -0.0390 89   ARG B CG  
1887  C  CD  . ARG B 89   ? 1.1932 1.0442 1.1266 -0.0742 0.1546  -0.0431 89   ARG B CD  
1888  N  NE  . ARG B 89   ? 1.3348 1.1727 1.2605 -0.0841 0.1628  -0.0451 89   ARG B NE  
1889  C  CZ  . ARG B 89   ? 1.2590 1.1064 1.1934 -0.0946 0.1643  -0.0506 89   ARG B CZ  
1890  N  NH1 . ARG B 89   ? 1.1757 1.0460 1.1266 -0.0964 0.1581  -0.0547 89   ARG B NH1 
1891  N  NH2 . ARG B 89   ? 1.2542 1.0877 1.1805 -0.1035 0.1724  -0.0520 89   ARG B NH2 
1892  N  N   . GLN B 90   ? 1.0736 0.9675 1.0309 -0.0339 0.1354  -0.0275 90   GLN B N   
1893  C  CA  . GLN B 90   ? 1.0015 0.9057 0.9656 -0.0250 0.1286  -0.0254 90   GLN B CA  
1894  C  C   . GLN B 90   ? 1.0156 0.9141 0.9763 -0.0224 0.1256  -0.0255 90   GLN B C   
1895  O  O   . GLN B 90   ? 1.0675 0.9491 1.0162 -0.0234 0.1298  -0.0244 90   GLN B O   
1896  C  CB  . GLN B 90   ? 1.0859 0.9857 1.0451 -0.0162 0.1297  -0.0198 90   GLN B CB  
1897  C  CG  . GLN B 90   ? 1.1261 1.0374 1.0924 -0.0159 0.1296  -0.0196 90   GLN B CG  
1898  C  CD  . GLN B 90   ? 1.0654 0.9963 1.0459 -0.0123 0.1221  -0.0209 90   GLN B CD  
1899  O  OE1 . GLN B 90   ? 1.1421 1.0855 1.1309 -0.0140 0.1211  -0.0226 90   GLN B OE1 
1900  N  NE2 . GLN B 90   ? 0.9348 0.8680 0.9176 -0.0071 0.1171  -0.0201 90   GLN B NE2 
1901  N  N   . PRO B 91   ? 1.3170 1.2287 1.2874 -0.0190 0.1188  -0.0267 91   PRO B N   
1902  C  CA  . PRO B 91   ? 1.3413 1.2474 1.3080 -0.0148 0.1162  -0.0258 91   PRO B CA  
1903  C  C   . PRO B 91   ? 1.3602 1.2552 1.3183 -0.0060 0.1180  -0.0199 91   PRO B C   
1904  O  O   . PRO B 91   ? 1.4166 1.3153 1.3765 -0.0008 0.1178  -0.0167 91   PRO B O   
1905  C  CB  . PRO B 91   ? 1.2154 1.1395 1.1952 -0.0123 0.1088  -0.0277 91   PRO B CB  
1906  C  CG  . PRO B 91   ? 1.1441 1.0819 1.1336 -0.0185 0.1079  -0.0317 91   PRO B CG  
1907  C  CD  . PRO B 91   ? 1.1875 1.1194 1.1724 -0.0198 0.1135  -0.0296 91   PRO B CD  
1908  N  N   . GLU B 92   ? 1.4819 1.3635 1.4304 -0.0042 0.1195  -0.0187 92   GLU B N   
1909  C  CA  . GLU B 92   ? 1.5667 1.4357 1.5053 0.0035  0.1223  -0.0134 92   GLU B CA  
1910  C  C   . GLU B 92   ? 1.5235 1.4028 1.4694 0.0126  0.1174  -0.0102 92   GLU B C   
1911  O  O   . GLU B 92   ? 1.3876 1.2654 1.3314 0.0186  0.1185  -0.0064 92   GLU B O   
1912  C  CB  . GLU B 92   ? 1.5836 1.4364 1.5105 0.0034  0.1249  -0.0132 92   GLU B CB  
1913  C  CG  . GLU B 92   ? 1.5946 1.4293 1.5081 -0.0018 0.1321  -0.0133 92   GLU B CG  
1914  C  CD  . GLU B 92   ? 1.7981 1.6345 1.7139 -0.0131 0.1334  -0.0189 92   GLU B CD  
1915  O  OE1 . GLU B 92   ? 1.7391 1.5923 1.6677 -0.0166 0.1287  -0.0226 92   GLU B OE1 
1916  O  OE2 . GLU B 92   ? 1.8373 1.6582 1.7422 -0.0185 0.1393  -0.0197 92   GLU B OE2 
1917  N  N   . GLY B 93   ? 0.9524 0.8419 0.9067 0.0139  0.1121  -0.0118 93   GLY B N   
1918  C  CA  . GLY B 93   ? 0.8492 0.7470 0.8098 0.0221  0.1078  -0.0090 93   GLY B CA  
1919  C  C   . GLY B 93   ? 0.8908 0.8070 0.8653 0.0226  0.1026  -0.0103 93   GLY B C   
1920  O  O   . GLY B 93   ? 1.0202 0.9439 1.0010 0.0283  0.0987  -0.0087 93   GLY B O   
1921  N  N   . ARG B 94   ? 0.8852 0.8087 0.8646 0.0168  0.1027  -0.0132 94   ARG B N   
1922  C  CA  . ARG B 94   ? 0.8511 0.7917 0.8431 0.0171  0.0979  -0.0149 94   ARG B CA  
1923  C  C   . ARG B 94   ? 0.8626 0.8062 0.8559 0.0196  0.0992  -0.0127 94   ARG B C   
1924  O  O   . ARG B 94   ? 0.9834 0.9198 0.9704 0.0162  0.1039  -0.0125 94   ARG B O   
1925  C  CB  . ARG B 94   ? 0.8830 0.8320 0.8810 0.0093  0.0965  -0.0202 94   ARG B CB  
1926  C  CG  . ARG B 94   ? 0.7743 0.7249 0.7738 0.0076  0.0934  -0.0229 94   ARG B CG  
1927  C  CD  . ARG B 94   ? 0.8000 0.7673 0.8114 0.0056  0.0881  -0.0267 94   ARG B CD  
1928  N  NE  . ARG B 94   ? 0.7286 0.7032 0.7446 0.0000  0.0894  -0.0295 94   ARG B NE  
1929  C  CZ  . ARG B 94   ? 0.7122 0.6880 0.7286 -0.0079 0.0906  -0.0340 94   ARG B CZ  
1930  N  NH1 . ARG B 94   ? 0.8398 0.8097 0.8519 -0.0113 0.0905  -0.0365 94   ARG B NH1 
1931  N  NH2 . ARG B 94   ? 0.7534 0.7367 0.7748 -0.0126 0.0921  -0.0362 94   ARG B NH2 
1932  N  N   . VAL B 95   ? 0.7592 0.7128 0.7601 0.0254  0.0950  -0.0110 95   VAL B N   
1933  C  CA  . VAL B 95   ? 0.6770 0.6363 0.6808 0.0279  0.0949  -0.0097 95   VAL B CA  
1934  C  C   . VAL B 95   ? 0.7074 0.6817 0.7221 0.0242  0.0916  -0.0133 95   VAL B C   
1935  O  O   . VAL B 95   ? 0.7517 0.7358 0.7747 0.0256  0.0866  -0.0147 95   VAL B O   
1936  C  CB  . VAL B 95   ? 0.7408 0.7022 0.7466 0.0366  0.0922  -0.0060 95   VAL B CB  
1937  C  CG1 . VAL B 95   ? 0.6529 0.6185 0.6600 0.0393  0.0923  -0.0046 95   VAL B CG1 
1938  C  CG2 . VAL B 95   ? 0.7390 0.6869 0.7350 0.0407  0.0950  -0.0027 95   VAL B CG2 
1939  N  N   . PRO B 96   ? 0.6865 0.6627 0.7011 0.0196  0.0943  -0.0149 96   PRO B N   
1940  C  CA  . PRO B 96   ? 0.7544 0.7453 0.7795 0.0160  0.0913  -0.0187 96   PRO B CA  
1941  C  C   . PRO B 96   ? 0.7328 0.7356 0.7667 0.0219  0.0860  -0.0179 96   PRO B C   
1942  O  O   . PRO B 96   ? 0.7687 0.7702 0.8010 0.0273  0.0860  -0.0148 96   PRO B O   
1943  C  CB  . PRO B 96   ? 0.6194 0.6080 0.6412 0.0114  0.0963  -0.0194 96   PRO B CB  
1944  C  CG  . PRO B 96   ? 0.6005 0.5718 0.6096 0.0100  0.1022  -0.0172 96   PRO B CG  
1945  C  CD  . PRO B 96   ? 0.5841 0.5486 0.5888 0.0175  0.1006  -0.0134 96   PRO B CD  
1946  N  N   . GLY B 97   ? 0.8246 0.8389 0.8675 0.0209  0.0813  -0.0208 97   GLY B N   
1947  C  CA  . GLY B 97   ? 0.7872 0.8122 0.8383 0.0261  0.0762  -0.0204 97   GLY B CA  
1948  C  C   . GLY B 97   ? 0.7218 0.7447 0.7735 0.0316  0.0731  -0.0181 97   GLY B C   
1949  O  O   . GLY B 97   ? 0.6510 0.6817 0.7091 0.0359  0.0690  -0.0176 97   GLY B O   
1950  N  N   . ILE B 98   ? 0.5196 0.5319 0.5644 0.0315  0.0752  -0.0167 98   ILE B N   
1951  C  CA  . ILE B 98   ? 0.4080 0.4179 0.4530 0.0365  0.0729  -0.0145 98   ILE B CA  
1952  C  C   . ILE B 98   ? 0.5179 0.5272 0.5630 0.0336  0.0717  -0.0169 98   ILE B C   
1953  O  O   . ILE B 98   ? 0.5034 0.5040 0.5415 0.0297  0.0749  -0.0177 98   ILE B O   
1954  C  CB  . ILE B 98   ? 0.3861 0.3840 0.4227 0.0403  0.0763  -0.0106 98   ILE B CB  
1955  C  CG1 . ILE B 98   ? 0.6133 0.6130 0.6505 0.0446  0.0764  -0.0082 98   ILE B CG1 
1956  C  CG2 . ILE B 98   ? 0.4707 0.4658 0.5074 0.0444  0.0747  -0.0087 98   ILE B CG2 
1957  C  CD1 . ILE B 98   ? 0.5987 0.5890 0.6293 0.0499  0.0785  -0.0043 98   ILE B CD1 
1958  N  N   . PRO B 99   ? 0.6445 0.6620 0.6964 0.0355  0.0672  -0.0180 99   PRO B N   
1959  C  CA  . PRO B 99   ? 0.6311 0.6474 0.6820 0.0336  0.0659  -0.0200 99   PRO B CA  
1960  C  C   . PRO B 99   ? 0.6906 0.6954 0.7343 0.0363  0.0680  -0.0172 99   PRO B C   
1961  O  O   . PRO B 99   ? 0.7028 0.7040 0.7454 0.0412  0.0688  -0.0136 99   PRO B O   
1962  C  CB  . PRO B 99   ? 0.6506 0.6779 0.7100 0.0363  0.0607  -0.0211 99   PRO B CB  
1963  C  CG  . PRO B 99   ? 0.7089 0.7446 0.7744 0.0376  0.0594  -0.0210 99   PRO B CG  
1964  C  CD  . PRO B 99   ? 0.6599 0.6882 0.7204 0.0392  0.0631  -0.0178 99   PRO B CD  
1965  N  N   . GLN B 100  ? 0.7297 0.7290 0.7686 0.0331  0.0687  -0.0191 100  GLN B N   
1966  C  CA  . GLN B 100  ? 0.6928 0.6809 0.7242 0.0354  0.0708  -0.0169 100  GLN B CA  
1967  C  C   . GLN B 100  ? 0.6780 0.6684 0.7109 0.0363  0.0676  -0.0183 100  GLN B C   
1968  O  O   . GLN B 100  ? 0.6445 0.6440 0.6828 0.0342  0.0641  -0.0216 100  GLN B O   
1969  C  CB  . GLN B 100  ? 0.6883 0.6644 0.7099 0.0310  0.0754  -0.0176 100  GLN B CB  
1970  C  CG  . GLN B 100  ? 0.6243 0.5917 0.6400 0.0330  0.0797  -0.0141 100  GLN B CG  
1971  C  CD  . GLN B 100  ? 0.7338 0.6877 0.7386 0.0290  0.0845  -0.0146 100  GLN B CD  
1972  O  OE1 . GLN B 100  ? 0.7862 0.7399 0.7898 0.0225  0.0850  -0.0184 100  GLN B OE1 
1973  N  NE2 . GLN B 100  ? 0.7360 0.6785 0.7328 0.0328  0.0881  -0.0109 100  GLN B NE2 
1974  N  N   . TYR B 101  ? 0.6117 0.5938 0.6394 0.0399  0.0689  -0.0158 101  TYR B N   
1975  C  CA  . TYR B 101  ? 0.5615 0.5438 0.5890 0.0415  0.0665  -0.0166 101  TYR B CA  
1976  C  C   . TYR B 101  ? 0.6161 0.5863 0.6334 0.0398  0.0693  -0.0171 101  TYR B C   
1977  O  O   . TYR B 101  ? 0.5623 0.5222 0.5727 0.0407  0.0733  -0.0147 101  TYR B O   
1978  C  CB  . TYR B 101  ? 0.4301 0.4145 0.4616 0.0478  0.0655  -0.0130 101  TYR B CB  
1979  C  CG  . TYR B 101  ? 0.5862 0.5827 0.6277 0.0495  0.0620  -0.0131 101  TYR B CG  
1980  C  CD1 . TYR B 101  ? 0.6974 0.6976 0.7428 0.0500  0.0625  -0.0119 101  TYR B CD1 
1981  C  CD2 . TYR B 101  ? 0.6022 0.6056 0.6486 0.0508  0.0582  -0.0145 101  TYR B CD2 
1982  C  CE1 . TYR B 101  ? 0.7122 0.7229 0.7662 0.0516  0.0593  -0.0122 101  TYR B CE1 
1983  C  CE2 . TYR B 101  ? 0.5898 0.6032 0.6447 0.0524  0.0552  -0.0146 101  TYR B CE2 
1984  C  CZ  . TYR B 101  ? 0.6386 0.6558 0.6975 0.0527  0.0557  -0.0136 101  TYR B CZ  
1985  O  OH  . TYR B 101  ? 0.6855 0.7121 0.7522 0.0543  0.0526  -0.0139 101  TYR B OH  
1986  N  N   . PHE B 102  ? 0.8686 0.8397 0.8845 0.0377  0.0670  -0.0204 102  PHE B N   
1987  C  CA  . PHE B 102  ? 0.8151 0.7751 0.8212 0.0361  0.0689  -0.0214 102  PHE B CA  
1988  C  C   . PHE B 102  ? 0.7567 0.7168 0.7618 0.0398  0.0664  -0.0213 102  PHE B C   
1989  O  O   . PHE B 102  ? 0.7114 0.6813 0.7233 0.0412  0.0624  -0.0224 102  PHE B O   
1990  C  CB  . PHE B 102  ? 0.7658 0.7257 0.7694 0.0288  0.0687  -0.0264 102  PHE B CB  
1991  C  CG  . PHE B 102  ? 0.8477 0.8058 0.8509 0.0246  0.0720  -0.0265 102  PHE B CG  
1992  C  CD1 . PHE B 102  ? 0.8524 0.8218 0.8642 0.0227  0.0704  -0.0277 102  PHE B CD1 
1993  C  CD2 . PHE B 102  ? 0.8881 0.8325 0.8815 0.0229  0.0768  -0.0254 102  PHE B CD2 
1994  C  CE1 . PHE B 102  ? 0.9048 0.8720 0.9155 0.0191  0.0738  -0.0276 102  PHE B CE1 
1995  C  CE2 . PHE B 102  ? 0.8128 0.7545 0.8049 0.0193  0.0802  -0.0253 102  PHE B CE2 
1996  C  CZ  . PHE B 102  ? 0.8665 0.8196 0.8672 0.0173  0.0788  -0.0264 102  PHE B CZ  
1997  N  N   . ALA B 103  ? 0.9321 0.8805 0.9282 0.0416  0.0690  -0.0199 103  ALA B N   
1998  C  CA  . ALA B 103  ? 0.9698 0.9160 0.9631 0.0454  0.0676  -0.0193 103  ALA B CA  
1999  C  C   . ALA B 103  ? 0.9258 0.8693 0.9132 0.0415  0.0657  -0.0241 103  ALA B C   
2000  O  O   . ALA B 103  ? 0.9127 0.8461 0.8916 0.0384  0.0683  -0.0254 103  ALA B O   
2001  C  CB  . ALA B 103  ? 1.0544 0.9899 1.0414 0.0504  0.0717  -0.0149 103  ALA B CB  
2002  N  N   . SER B 104  ? 0.6963 0.6485 0.6879 0.0419  0.0611  -0.0267 104  SER B N   
2003  C  CA  . SER B 104  ? 0.7706 0.7216 0.7571 0.0389  0.0584  -0.0315 104  SER B CA  
2004  C  C   . SER B 104  ? 0.8230 0.7743 0.8074 0.0440  0.0558  -0.0309 104  SER B C   
2005  O  O   . SER B 104  ? 0.7386 0.6881 0.7239 0.0496  0.0572  -0.0265 104  SER B O   
2006  C  CB  . SER B 104  ? 0.7751 0.7376 0.7684 0.0333  0.0549  -0.0365 104  SER B CB  
2007  O  OG  . SER B 104  ? 0.7402 0.7013 0.7284 0.0297  0.0525  -0.0416 104  SER B OG  
2008  N  N   . THR B 105  ? 0.8106 0.7642 0.7922 0.0423  0.0520  -0.0355 105  THR B N   
2009  C  CA  . THR B 105  ? 0.7226 0.6756 0.7007 0.0473  0.0494  -0.0353 105  THR B CA  
2010  C  C   . THR B 105  ? 0.7670 0.7308 0.7488 0.0456  0.0435  -0.0405 105  THR B C   
2011  O  O   . THR B 105  ? 0.7841 0.7512 0.7661 0.0399  0.0417  -0.0454 105  THR B O   
2012  C  CB  . THR B 105  ? 0.7508 0.6899 0.7163 0.0487  0.0516  -0.0351 105  THR B CB  
2013  O  OG1 . THR B 105  ? 0.8556 0.7851 0.8179 0.0508  0.0572  -0.0302 105  THR B OG1 
2014  C  CG2 . THR B 105  ? 0.7506 0.6884 0.7117 0.0543  0.0493  -0.0347 105  THR B CG2 
2015  N  N   . LEU B 106  ? 0.8582 0.8277 0.8430 0.0507  0.0405  -0.0394 106  LEU B N   
2016  C  CA  . LEU B 106  ? 0.8547 0.8345 0.8425 0.0507  0.0347  -0.0439 106  LEU B CA  
2017  C  C   . LEU B 106  ? 0.9549 0.9292 0.9341 0.0561  0.0328  -0.0438 106  LEU B C   
2018  O  O   . LEU B 106  ? 0.9892 0.9577 0.9660 0.0615  0.0351  -0.0390 106  LEU B O   
2019  C  CB  . LEU B 106  ? 0.7773 0.7694 0.7762 0.0522  0.0326  -0.0429 106  LEU B CB  
2020  C  CG  . LEU B 106  ? 0.6929 0.6926 0.7004 0.0468  0.0335  -0.0441 106  LEU B CG  
2021  C  CD1 . LEU B 106  ? 0.7349 0.7463 0.7525 0.0489  0.0311  -0.0433 106  LEU B CD1 
2022  C  CD2 . LEU B 106  ? 0.7604 0.7640 0.7675 0.0403  0.0315  -0.0502 106  LEU B CD2 
2023  N  N   . THR B 107  ? 1.2076 1.1839 1.1824 0.0546  0.0287  -0.0491 107  THR B N   
2024  C  CA  . THR B 107  ? 1.1938 1.1643 1.1590 0.0596  0.0265  -0.0496 107  THR B CA  
2025  C  C   . THR B 107  ? 1.1100 1.0914 1.0790 0.0631  0.0208  -0.0520 107  THR B C   
2026  O  O   . THR B 107  ? 1.2121 1.2058 1.1888 0.0598  0.0170  -0.0562 107  THR B O   
2027  C  CB  . THR B 107  ? 1.2765 1.2402 1.2323 0.0562  0.0256  -0.0542 107  THR B CB  
2028  O  OG1 . THR B 107  ? 1.4247 1.3998 1.3855 0.0513  0.0206  -0.0608 107  THR B OG1 
2029  C  CG2 . THR B 107  ? 1.2591 1.2124 1.2114 0.0522  0.0312  -0.0524 107  THR B CG2 
2030  N  N   . LEU B 108  ? 0.9285 0.9052 0.8919 0.0701  0.0204  -0.0491 108  LEU B N   
2031  C  CA  . LEU B 108  ? 1.0004 0.9852 0.9652 0.0746  0.0152  -0.0508 108  LEU B CA  
2032  C  C   . LEU B 108  ? 1.0368 1.0190 0.9913 0.0767  0.0110  -0.0552 108  LEU B C   
2033  O  O   . LEU B 108  ? 1.0448 1.0367 1.0018 0.0742  0.0057  -0.0612 108  LEU B O   
2034  C  CB  . LEU B 108  ? 1.0035 0.9847 0.9684 0.0812  0.0175  -0.0450 108  LEU B CB  
2035  C  CG  . LEU B 108  ? 0.9793 0.9673 0.9448 0.0866  0.0128  -0.0460 108  LEU B CG  
2036  C  CD1 . LEU B 108  ? 0.9033 0.9068 0.8797 0.0834  0.0084  -0.0501 108  LEU B CD1 
2037  C  CD2 . LEU B 108  ? 0.9646 0.9476 0.9304 0.0921  0.0161  -0.0399 108  LEU B CD2 
2038  N  N   . GLY B 109  ? 0.5849 0.5543 0.5280 0.0815  0.0132  -0.0525 109  GLY B N   
2039  C  CA  . GLY B 109  ? 0.6898 0.6551 0.6216 0.0840  0.0094  -0.0564 109  GLY B CA  
2040  C  C   . GLY B 109  ? 0.7370 0.6900 0.6594 0.0811  0.0126  -0.0569 109  GLY B C   
2041  O  O   . GLY B 109  ? 0.5986 0.5410 0.5086 0.0855  0.0129  -0.0564 109  GLY B O   
2042  N  N   . GLY B 110  ? 0.9701 0.9237 0.8978 0.0740  0.0151  -0.0579 110  GLY B N   
2043  C  CA  . GLY B 110  ? 0.8833 0.8247 0.8027 0.0709  0.0189  -0.0580 110  GLY B CA  
2044  C  C   . GLY B 110  ? 0.8979 0.8292 0.8165 0.0723  0.0262  -0.0512 110  GLY B C   
2045  O  O   . GLY B 110  ? 1.0321 0.9544 0.9461 0.0688  0.0300  -0.0510 110  GLY B O   
2046  N  N   . TYR B 111  ? 0.8807 0.8131 0.8035 0.0771  0.0284  -0.0458 111  TYR B N   
2047  C  CA  . TYR B 111  ? 0.9482 0.8729 0.8718 0.0787  0.0351  -0.0394 111  TYR B CA  
2048  C  C   . TYR B 111  ? 0.9815 0.9145 0.9180 0.0744  0.0367  -0.0380 111  TYR B C   
2049  O  O   . TYR B 111  ? 0.9684 0.9134 0.9143 0.0737  0.0333  -0.0393 111  TYR B O   
2050  C  CB  . TYR B 111  ? 1.0115 0.9322 0.9323 0.0861  0.0370  -0.0343 111  TYR B CB  
2051  C  CG  . TYR B 111  ? 0.9551 0.8664 0.8620 0.0911  0.0360  -0.0351 111  TYR B CG  
2052  C  CD1 . TYR B 111  ? 1.0080 0.9055 0.9043 0.0927  0.0406  -0.0330 111  TYR B CD1 
2053  C  CD2 . TYR B 111  ? 0.8716 0.7874 0.7754 0.0945  0.0305  -0.0381 111  TYR B CD2 
2054  C  CE1 . TYR B 111  ? 1.0880 0.9764 0.9708 0.0974  0.0398  -0.0337 111  TYR B CE1 
2055  C  CE2 . TYR B 111  ? 1.0895 0.9963 0.9797 0.0995  0.0294  -0.0389 111  TYR B CE2 
2056  C  CZ  . TYR B 111  ? 1.2078 1.1008 1.0874 0.1008  0.0342  -0.0367 111  TYR B CZ  
2057  O  OH  . TYR B 111  ? 1.2880 1.1715 1.1534 0.1060  0.0333  -0.0374 111  TYR B OH  
2058  N  N   . GLY B 112  ? 0.9416 0.8680 0.8780 0.0721  0.0419  -0.0353 112  GLY B N   
2059  C  CA  . GLY B 112  ? 0.9740 0.9070 0.9210 0.0678  0.0434  -0.0343 112  GLY B CA  
2060  C  C   . GLY B 112  ? 0.9311 0.8679 0.8863 0.0714  0.0458  -0.0289 112  GLY B C   
2061  O  O   . GLY B 112  ? 0.9509 0.8829 0.9032 0.0768  0.0478  -0.0250 112  GLY B O   
2062  N  N   . THR B 113  ? 0.9117 0.8572 0.8774 0.0680  0.0457  -0.0289 113  THR B N   
2063  C  CA  . THR B 113  ? 0.8739 0.8237 0.8484 0.0704  0.0477  -0.0244 113  THR B CA  
2064  C  C   . THR B 113  ? 0.7983 0.7511 0.7793 0.0660  0.0498  -0.0239 113  THR B C   
2065  O  O   . THR B 113  ? 0.7646 0.7247 0.7500 0.0613  0.0472  -0.0276 113  THR B O   
2066  C  CB  . THR B 113  ? 0.8415 0.8020 0.8230 0.0724  0.0433  -0.0253 113  THR B CB  
2067  O  OG1 . THR B 113  ? 0.8725 0.8297 0.8465 0.0766  0.0411  -0.0262 113  THR B OG1 
2068  C  CG2 . THR B 113  ? 0.7348 0.6984 0.7243 0.0751  0.0456  -0.0206 113  THR B CG2 
2069  N  N   . GLY B 114  ? 0.7911 0.7381 0.7724 0.0677  0.0547  -0.0194 114  GLY B N   
2070  C  CA  . GLY B 114  ? 0.8172 0.7655 0.8030 0.0643  0.0570  -0.0186 114  GLY B CA  
2071  C  C   . GLY B 114  ? 0.7628 0.7232 0.7603 0.0634  0.0548  -0.0185 114  GLY B C   
2072  O  O   . GLY B 114  ? 0.7553 0.7199 0.7583 0.0671  0.0543  -0.0159 114  GLY B O   
2073  N  N   . VAL B 115  ? 0.7112 0.6768 0.7124 0.0584  0.0537  -0.0214 115  VAL B N   
2074  C  CA  . VAL B 115  ? 0.6938 0.6709 0.7054 0.0573  0.0515  -0.0218 115  VAL B CA  
2075  C  C   . VAL B 115  ? 0.8201 0.7966 0.8342 0.0543  0.0544  -0.0207 115  VAL B C   
2076  O  O   . VAL B 115  ? 0.9353 0.9047 0.9433 0.0510  0.0569  -0.0217 115  VAL B O   
2077  C  CB  . VAL B 115  ? 0.6734 0.6599 0.6881 0.0543  0.0465  -0.0269 115  VAL B CB  
2078  C  CG1 . VAL B 115  ? 0.6982 0.6871 0.7119 0.0586  0.0432  -0.0274 115  VAL B CG1 
2079  C  CG2 . VAL B 115  ? 0.8109 0.7940 0.8197 0.0491  0.0464  -0.0312 115  VAL B CG2 
2080  N  N   . LEU B 116  ? 0.9493 0.9326 0.9717 0.0556  0.0543  -0.0186 116  LEU B N   
2081  C  CA  . LEU B 116  ? 0.8983 0.8826 0.9237 0.0532  0.0565  -0.0178 116  LEU B CA  
2082  C  C   . LEU B 116  ? 0.9284 0.9237 0.9607 0.0496  0.0533  -0.0212 116  LEU B C   
2083  O  O   . LEU B 116  ? 1.0124 1.0165 1.0522 0.0516  0.0506  -0.0209 116  LEU B O   
2084  C  CB  . LEU B 116  ? 0.9277 0.9118 0.9573 0.0574  0.0585  -0.0131 116  LEU B CB  
2085  C  CG  . LEU B 116  ? 0.9578 0.9410 0.9886 0.0562  0.0612  -0.0116 116  LEU B CG  
2086  C  CD1 . LEU B 116  ? 1.0761 1.0478 1.0973 0.0544  0.0651  -0.0113 116  LEU B CD1 
2087  C  CD2 . LEU B 116  ? 1.0039 0.9893 1.0403 0.0607  0.0622  -0.0076 116  LEU B CD2 
2088  N  N   . VAL B 117  ? 0.6323 0.6270 0.6621 0.0443  0.0538  -0.0245 117  VAL B N   
2089  C  CA  . VAL B 117  ? 0.6424 0.6475 0.6781 0.0403  0.0510  -0.0284 117  VAL B CA  
2090  C  C   . VAL B 117  ? 0.6986 0.7047 0.7370 0.0377  0.0537  -0.0275 117  VAL B C   
2091  O  O   . VAL B 117  ? 0.7003 0.6969 0.7327 0.0364  0.0578  -0.0258 117  VAL B O   
2092  C  CB  . VAL B 117  ? 0.5836 0.5887 0.6154 0.0358  0.0494  -0.0333 117  VAL B CB  
2093  C  CG1 . VAL B 117  ? 0.6777 0.6706 0.7005 0.0326  0.0534  -0.0334 117  VAL B CG1 
2094  C  CG2 . VAL B 117  ? 0.5940 0.6109 0.6327 0.0314  0.0469  -0.0376 117  VAL B CG2 
2095  N  N   . ARG B 118  ? 0.9630 0.9799 1.0094 0.0371  0.0515  -0.0286 118  ARG B N   
2096  C  CA  . ARG B 118  ? 0.9309 0.9498 0.9803 0.0356  0.0538  -0.0275 118  ARG B CA  
2097  C  C   . ARG B 118  ? 0.9441 0.9667 0.9942 0.0291  0.0543  -0.0316 118  ARG B C   
2098  O  O   . ARG B 118  ? 0.9484 0.9805 1.0032 0.0271  0.0509  -0.0354 118  ARG B O   
2099  C  CB  . ARG B 118  ? 0.8951 0.9232 0.9528 0.0393  0.0513  -0.0260 118  ARG B CB  
2100  C  CG  . ARG B 118  ? 0.9015 0.9325 0.9623 0.0381  0.0531  -0.0252 118  ARG B CG  
2101  C  CD  . ARG B 118  ? 0.9481 0.9887 1.0170 0.0416  0.0500  -0.0245 118  ARG B CD  
2102  N  NE  . ARG B 118  ? 0.8829 0.9341 0.9572 0.0401  0.0463  -0.0283 118  ARG B NE  
2103  C  CZ  . ARG B 118  ? 0.9044 0.9634 0.9848 0.0435  0.0428  -0.0284 118  ARG B CZ  
2104  N  NH1 . ARG B 118  ? 0.9003 0.9581 0.9827 0.0480  0.0425  -0.0251 118  ARG B NH1 
2105  N  NH2 . ARG B 118  ? 0.8532 0.9215 0.9377 0.0424  0.0396  -0.0320 118  ARG B NH2 
2106  N  N   . SER B 119  ? 0.8565 0.8717 0.9018 0.0259  0.0587  -0.0308 119  SER B N   
2107  C  CA  . SER B 119  ? 0.9365 0.9542 0.9823 0.0193  0.0603  -0.0342 119  SER B CA  
2108  C  C   . SER B 119  ? 0.9510 0.9721 1.0004 0.0196  0.0621  -0.0324 119  SER B C   
2109  O  O   . SER B 119  ? 0.8707 0.8838 0.9158 0.0221  0.0653  -0.0285 119  SER B O   
2110  C  CB  . SER B 119  ? 0.9557 0.9609 0.9920 0.0149  0.0643  -0.0350 119  SER B CB  
2111  O  OG  . SER B 119  ? 0.9711 0.9668 1.0022 0.0156  0.0691  -0.0313 119  SER B OG  
2112  N  N   . ASN B 120  ? 1.0936 1.1267 1.1506 0.0175  0.0601  -0.0351 120  ASN B N   
2113  C  CA  . ASN B 120  ? 1.1023 1.1393 1.1627 0.0181  0.0616  -0.0336 120  ASN B CA  
2114  C  C   . ASN B 120  ? 1.2044 1.2340 1.2593 0.0130  0.0670  -0.0337 120  ASN B C   
2115  O  O   . ASN B 120  ? 1.2375 1.2590 1.2875 0.0151  0.0704  -0.0301 120  ASN B O   
2116  C  CB  . ASN B 120  ? 0.9882 1.0403 1.0582 0.0178  0.0578  -0.0366 120  ASN B CB  
2117  C  CG  . ASN B 120  ? 1.0664 1.1243 1.1415 0.0243  0.0537  -0.0347 120  ASN B CG  
2118  O  OD1 . ASN B 120  ? 1.0161 1.0787 1.0937 0.0261  0.0498  -0.0363 120  ASN B OD1 
2119  N  ND2 . ASN B 120  ? 1.1106 1.1677 1.1866 0.0280  0.0545  -0.0314 120  ASN B ND2 
2120  N  N   . GLU B 121  ? 1.0232 1.0555 1.0787 0.0062  0.0679  -0.0380 121  GLU B N   
2121  C  CA  . GLU B 121  ? 1.0252 1.0498 1.0751 0.0003  0.0735  -0.0386 121  GLU B CA  
2122  C  C   . GLU B 121  ? 1.1613 1.1812 1.2072 -0.0057 0.0742  -0.0423 121  GLU B C   
2123  O  O   . GLU B 121  ? 1.1795 1.2015 1.2264 -0.0128 0.0764  -0.0460 121  GLU B O   
2124  C  CB  . GLU B 121  ? 1.0654 1.0994 1.1213 -0.0030 0.0747  -0.0404 121  GLU B CB  
2125  C  CG  . GLU B 121  ? 1.0656 1.0996 1.1219 0.0019  0.0759  -0.0364 121  GLU B CG  
2126  C  CD  . GLU B 121  ? 1.1403 1.1595 1.1865 0.0020  0.0816  -0.0327 121  GLU B CD  
2127  O  OE1 . GLU B 121  ? 1.1388 1.1513 1.1799 -0.0042 0.0863  -0.0342 121  GLU B OE1 
2128  O  OE2 . GLU B 121  ? 1.0959 1.1100 1.1390 0.0083  0.0815  -0.0285 121  GLU B OE2 
2129  N  N   . GLY B 122  ? 1.2195 1.2330 1.2609 -0.0030 0.0725  -0.0416 122  GLY B N   
2130  C  CA  . GLY B 122  ? 1.1379 1.1474 1.1754 -0.0078 0.0723  -0.0453 122  GLY B CA  
2131  C  C   . GLY B 122  ? 1.1677 1.1896 1.2122 -0.0081 0.0664  -0.0496 122  GLY B C   
2132  O  O   . GLY B 122  ? 1.1079 1.1292 1.1507 -0.0130 0.0657  -0.0539 122  GLY B O   
2133  N  N   . ARG B 123  ? 1.3161 1.3492 1.3683 -0.0028 0.0621  -0.0488 123  ARG B N   
2134  C  CA  . ARG B 123  ? 1.2671 1.3122 1.3256 -0.0020 0.0564  -0.0526 123  ARG B CA  
2135  C  C   . ARG B 123  ? 1.1792 1.2239 1.2376 0.0059  0.0529  -0.0494 123  ARG B C   
2136  O  O   . ARG B 123  ? 1.1662 1.2105 1.2262 0.0108  0.0534  -0.0453 123  ARG B O   
2137  C  CB  . ARG B 123  ? 1.2004 1.2612 1.2692 -0.0038 0.0545  -0.0554 123  ARG B CB  
2138  C  CG  . ARG B 123  ? 1.3331 1.3949 1.4030 -0.0113 0.0589  -0.0577 123  ARG B CG  
2139  C  CD  . ARG B 123  ? 1.3577 1.4360 1.4381 -0.0125 0.0568  -0.0606 123  ARG B CD  
2140  N  NE  . ARG B 123  ? 1.3899 1.4708 1.4733 -0.0074 0.0572  -0.0567 123  ARG B NE  
2141  C  CZ  . ARG B 123  ? 1.2622 1.3511 1.3507 -0.0011 0.0527  -0.0557 123  ARG B CZ  
2142  N  NH1 . ARG B 123  ? 1.0564 1.1514 1.1474 0.0015  0.0476  -0.0579 123  ARG B NH1 
2143  N  NH2 . ARG B 123  ? 1.2297 1.3202 1.3204 0.0029  0.0535  -0.0524 123  ARG B NH2 
2144  N  N   . PRO B 124  ? 0.6114 0.6561 0.6678 0.0074  0.0494  -0.0513 124  PRO B N   
2145  C  CA  . PRO B 124  ? 0.6569 0.7015 0.7133 0.0148  0.0464  -0.0484 124  PRO B CA  
2146  C  C   . PRO B 124  ? 0.6134 0.6717 0.6791 0.0181  0.0424  -0.0490 124  PRO B C   
2147  O  O   . PRO B 124  ? 0.5119 0.5815 0.5834 0.0154  0.0398  -0.0533 124  PRO B O   
2148  C  CB  . PRO B 124  ? 0.7203 0.7617 0.7717 0.0148  0.0438  -0.0510 124  PRO B CB  
2149  C  CG  . PRO B 124  ? 0.7248 0.7613 0.7718 0.0074  0.0464  -0.0546 124  PRO B CG  
2150  C  CD  . PRO B 124  ? 0.5952 0.6390 0.6485 0.0024  0.0483  -0.0562 124  PRO B CD  
2151  N  N   . THR B 125  ? 0.8155 0.8728 0.8826 0.0240  0.0421  -0.0447 125  THR B N   
2152  C  CA  . THR B 125  ? 0.8074 0.8759 0.8823 0.0276  0.0386  -0.0448 125  THR B CA  
2153  C  C   . THR B 125  ? 0.7660 0.8328 0.8403 0.0343  0.0361  -0.0421 125  THR B C   
2154  O  O   . THR B 125  ? 0.7527 0.8279 0.8313 0.0371  0.0320  -0.0437 125  THR B O   
2155  C  CB  . THR B 125  ? 0.7798 0.8504 0.8586 0.0274  0.0411  -0.0426 125  THR B CB  
2156  O  OG1 . THR B 125  ? 0.8525 0.9243 0.9314 0.0211  0.0440  -0.0450 125  THR B OG1 
2157  C  CG2 . THR B 125  ? 0.7341 0.8162 0.8207 0.0309  0.0376  -0.0431 125  THR B CG2 
2158  N  N   . LYS B 126  ? 0.8877 0.9437 0.9568 0.0370  0.0385  -0.0380 126  LYS B N   
2159  C  CA  . LYS B 126  ? 0.9173 0.9709 0.9860 0.0430  0.0369  -0.0351 126  LYS B CA  
2160  C  C   . LYS B 126  ? 0.9462 0.9882 1.0067 0.0440  0.0389  -0.0333 126  LYS B C   
2161  O  O   . LYS B 126  ? 0.8975 0.9313 0.9528 0.0414  0.0425  -0.0325 126  LYS B O   
2162  C  CB  . LYS B 126  ? 0.9008 0.9547 0.9736 0.0462  0.0381  -0.0311 126  LYS B CB  
2163  C  CG  . LYS B 126  ? 0.8161 0.8693 0.8902 0.0519  0.0364  -0.0286 126  LYS B CG  
2164  C  CD  . LYS B 126  ? 0.8627 0.9254 0.9414 0.0537  0.0319  -0.0311 126  LYS B CD  
2165  C  CE  . LYS B 126  ? 0.9828 1.0441 1.0628 0.0591  0.0307  -0.0283 126  LYS B CE  
2166  N  NZ  . LYS B 126  ? 1.0401 1.0915 1.1138 0.0613  0.0325  -0.0258 126  LYS B NZ  
2167  N  N   . VAL B 127  ? 0.8254 0.8661 0.8840 0.0482  0.0367  -0.0327 127  VAL B N   
2168  C  CA  . VAL B 127  ? 0.8265 0.8565 0.8772 0.0502  0.0384  -0.0308 127  VAL B CA  
2169  C  C   . VAL B 127  ? 0.7799 0.8071 0.8318 0.0557  0.0390  -0.0264 127  VAL B C   
2170  O  O   . VAL B 127  ? 0.7390 0.7725 0.7956 0.0587  0.0362  -0.0264 127  VAL B O   
2171  C  CB  . VAL B 127  ? 0.7703 0.8005 0.8163 0.0499  0.0354  -0.0345 127  VAL B CB  
2172  C  CG1 . VAL B 127  ? 0.7471 0.7664 0.7849 0.0533  0.0369  -0.0320 127  VAL B CG1 
2173  C  CG2 . VAL B 127  ? 0.6973 0.7288 0.7416 0.0437  0.0354  -0.0388 127  VAL B CG2 
2174  N  N   . GLU B 128  ? 0.7855 0.8033 0.8334 0.0572  0.0429  -0.0228 128  GLU B N   
2175  C  CA  . GLU B 128  ? 0.8486 0.8634 0.8977 0.0620  0.0441  -0.0186 128  GLU B CA  
2176  C  C   . GLU B 128  ? 0.8618 0.8655 0.9028 0.0638  0.0471  -0.0165 128  GLU B C   
2177  O  O   . GLU B 128  ? 0.8253 0.8234 0.8594 0.0613  0.0481  -0.0182 128  GLU B O   
2178  C  CB  . GLU B 128  ? 0.9788 0.9959 1.0340 0.0625  0.0459  -0.0159 128  GLU B CB  
2179  C  CG  . GLU B 128  ? 1.0108 1.0384 1.0741 0.0618  0.0429  -0.0175 128  GLU B CG  
2180  C  CD  . GLU B 128  ? 1.0908 1.1206 1.1570 0.0593  0.0446  -0.0172 128  GLU B CD  
2181  O  OE1 . GLU B 128  ? 1.2194 1.2422 1.2812 0.0582  0.0480  -0.0157 128  GLU B OE1 
2182  O  OE2 . GLU B 128  ? 0.9859 1.0239 1.0583 0.0588  0.0425  -0.0184 128  GLU B OE2 
2183  N  N   . GLY B 129  ? 0.9570 0.9575 0.9987 0.0680  0.0488  -0.0128 129  GLY B N   
2184  C  CA  . GLY B 129  ? 0.9487 0.9391 0.9830 0.0703  0.0518  -0.0105 129  GLY B CA  
2185  C  C   . GLY B 129  ? 0.9923 0.9760 1.0235 0.0696  0.0561  -0.0083 129  GLY B C   
2186  O  O   . GLY B 129  ? 1.0194 1.0059 1.0554 0.0686  0.0572  -0.0073 129  GLY B O   
2187  N  N   . ASN B 130  ? 0.8849 0.8588 0.9072 0.0705  0.0586  -0.0077 130  ASN B N   
2188  C  CA  . ASN B 130  ? 0.8094 0.7753 0.8271 0.0707  0.0629  -0.0054 130  ASN B CA  
2189  C  C   . ASN B 130  ? 0.8187 0.7803 0.8364 0.0755  0.0662  -0.0011 130  ASN B C   
2190  O  O   . ASN B 130  ? 0.8868 0.8419 0.8981 0.0778  0.0674  -0.0004 130  ASN B O   
2191  C  CB  . ASN B 130  ? 0.7944 0.7517 0.8016 0.0682  0.0637  -0.0079 130  ASN B CB  
2192  C  CG  . ASN B 130  ? 0.8414 0.7901 0.8433 0.0677  0.0681  -0.0061 130  ASN B CG  
2193  O  OD1 . ASN B 130  ? 0.7953 0.7402 0.7972 0.0715  0.0714  -0.0023 130  ASN B OD1 
2194  N  ND2 . ASN B 130  ? 1.0126 0.9583 1.0100 0.0632  0.0681  -0.0091 130  ASN B ND2 
2195  N  N   . PRO B 131  ? 0.6371 0.6022 0.6619 0.0772  0.0678  0.0018  131  PRO B N   
2196  C  CA  . PRO B 131  ? 0.6611 0.6238 0.6875 0.0816  0.0709  0.0057  131  PRO B CA  
2197  C  C   . PRO B 131  ? 0.6200 0.5719 0.6373 0.0838  0.0751  0.0076  131  PRO B C   
2198  O  O   . PRO B 131  ? 0.5253 0.4744 0.5423 0.0873  0.0777  0.0104  131  PRO B O   
2199  C  CB  . PRO B 131  ? 0.6608 0.6300 0.6964 0.0823  0.0714  0.0077  131  PRO B CB  
2200  C  CG  . PRO B 131  ? 0.6885 0.6650 0.7284 0.0787  0.0676  0.0047  131  PRO B CG  
2201  C  CD  . PRO B 131  ? 0.6705 0.6425 0.7023 0.0754  0.0668  0.0015  131  PRO B CD  
2202  N  N   . ARG B 132  ? 0.9111 0.8566 0.9208 0.0816  0.0761  0.0061  132  ARG B N   
2203  C  CA  . ARG B 132  ? 0.8572 0.7916 0.8572 0.0837  0.0803  0.0077  132  ARG B CA  
2204  C  C   . ARG B 132  ? 0.8230 0.7505 0.8137 0.0837  0.0797  0.0059  132  ARG B C   
2205  O  O   . ARG B 132  ? 0.8218 0.7395 0.8038 0.0859  0.0831  0.0072  132  ARG B O   
2206  C  CB  . ARG B 132  ? 0.8185 0.7477 0.8137 0.0816  0.0820  0.0071  132  ARG B CB  
2207  C  CG  . ARG B 132  ? 0.8484 0.7844 0.8517 0.0813  0.0818  0.0083  132  ARG B CG  
2208  C  CD  . ARG B 132  ? 1.0707 0.9998 1.0675 0.0797  0.0841  0.0080  132  ARG B CD  
2209  N  NE  . ARG B 132  ? 1.0968 1.0154 1.0855 0.0834  0.0887  0.0106  132  ARG B NE  
2210  C  CZ  . ARG B 132  ? 1.1553 1.0733 1.1458 0.0873  0.0916  0.0139  132  ARG B CZ  
2211  N  NH1 . ARG B 132  ? 1.1686 1.0955 1.1684 0.0881  0.0904  0.0150  132  ARG B NH1 
2212  N  NH2 . ARG B 132  ? 1.1527 1.0611 1.1354 0.0909  0.0958  0.0161  132  ARG B NH2 
2213  N  N   . HIS B 133  ? 0.7713 0.7036 0.7632 0.0816  0.0754  0.0028  133  HIS B N   
2214  C  CA  . HIS B 133  ? 0.8478 0.7744 0.8305 0.0815  0.0741  0.0003  133  HIS B CA  
2215  C  C   . HIS B 133  ? 0.8907 0.8183 0.8742 0.0853  0.0736  0.0019  133  HIS B C   
2216  O  O   . HIS B 133  ? 0.8883 0.8245 0.8802 0.0855  0.0712  0.0020  133  HIS B O   
2217  C  CB  . HIS B 133  ? 0.8548 0.7861 0.8374 0.0766  0.0694  -0.0047 133  HIS B CB  
2218  C  CG  . HIS B 133  ? 0.9014 0.8263 0.8737 0.0759  0.0678  -0.0080 133  HIS B CG  
2219  N  ND1 . HIS B 133  ? 0.9188 0.8469 0.8901 0.0771  0.0641  -0.0099 133  HIS B ND1 
2220  C  CD2 . HIS B 133  ? 0.9030 0.8183 0.8651 0.0741  0.0692  -0.0098 133  HIS B CD2 
2221  C  CE1 . HIS B 133  ? 0.9972 0.9186 0.9585 0.0763  0.0631  -0.0129 133  HIS B CE1 
2222  N  NE2 . HIS B 133  ? 0.9188 0.8323 0.8744 0.0742  0.0661  -0.0130 133  HIS B NE2 
2223  N  N   . PRO B 134  ? 0.9257 0.8441 0.9001 0.0885  0.0761  0.0031  134  PRO B N   
2224  C  CA  . PRO B 134  ? 0.8955 0.8137 0.8687 0.0920  0.0756  0.0042  134  PRO B CA  
2225  C  C   . PRO B 134  ? 0.9507 0.8736 0.9230 0.0901  0.0699  0.0000  134  PRO B C   
2226  O  O   . PRO B 134  ? 0.9816 0.9050 0.9507 0.0864  0.0670  -0.0041 134  PRO B O   
2227  C  CB  . PRO B 134  ? 0.8109 0.7169 0.7724 0.0953  0.0795  0.0058  134  PRO B CB  
2228  C  CG  . PRO B 134  ? 1.0474 0.9485 1.0071 0.0946  0.0832  0.0071  134  PRO B CG  
2229  C  CD  . PRO B 134  ? 0.9090 0.8159 0.8731 0.0895  0.0800  0.0039  134  PRO B CD  
2230  N  N   . ALA B 135  ? 1.0604 0.9869 1.0358 0.0927  0.0684  0.0009  135  ALA B N   
2231  C  CA  . ALA B 135  ? 1.1498 1.0820 1.1254 0.0922  0.0630  -0.0026 135  ALA B CA  
2232  C  C   . ALA B 135  ? 1.0917 1.0353 1.0777 0.0884  0.0594  -0.0048 135  ALA B C   
2233  O  O   . ALA B 135  ? 1.1286 1.0781 1.1154 0.0874  0.0546  -0.0083 135  ALA B O   
2234  C  CB  . ALA B 135  ? 1.1846 1.1118 1.1492 0.0915  0.0602  -0.0066 135  ALA B CB  
2235  N  N   . SER B 136  ? 1.3753 1.3225 1.3691 0.0865  0.0614  -0.0031 136  SER B N   
2236  C  CA  . SER B 136  ? 1.3496 1.3074 1.3534 0.0834  0.0585  -0.0047 136  SER B CA  
2237  C  C   . SER B 136  ? 1.2282 1.1883 1.2399 0.0835  0.0616  -0.0013 136  SER B C   
2238  O  O   . SER B 136  ? 1.2896 1.2533 1.3053 0.0805  0.0614  -0.0021 136  SER B O   
2239  C  CB  . SER B 136  ? 1.4328 1.3930 1.4348 0.0786  0.0558  -0.0091 136  SER B CB  
2240  O  OG  . SER B 136  ? 1.4945 1.4649 1.5060 0.0758  0.0534  -0.0105 136  SER B OG  
2241  N  N   . LEU B 137  ? 0.8161 0.7741 0.8301 0.0871  0.0646  0.0025  137  LEU B N   
2242  C  CA  . LEU B 137  ? 0.7619 0.7226 0.7837 0.0876  0.0675  0.0057  137  LEU B CA  
2243  C  C   . LEU B 137  ? 0.8361 0.8073 0.8685 0.0857  0.0645  0.0047  137  LEU B C   
2244  O  O   . LEU B 137  ? 0.9836 0.9587 1.0227 0.0873  0.0645  0.0064  137  LEU B O   
2245  C  CB  . LEU B 137  ? 0.8563 0.8132 0.8787 0.0915  0.0714  0.0096  137  LEU B CB  
2246  C  CG  . LEU B 137  ? 0.8645 0.8108 0.8757 0.0940  0.0743  0.0106  137  LEU B CG  
2247  C  CD1 . LEU B 137  ? 0.8118 0.7549 0.8228 0.0977  0.0771  0.0137  137  LEU B CD1 
2248  C  CD2 . LEU B 137  ? 0.7448 0.6853 0.7520 0.0941  0.0781  0.0120  137  LEU B CD2 
2249  N  N   . GLY B 138  ? 0.8813 0.8567 0.9148 0.0822  0.0620  0.0018  138  GLY B N   
2250  C  CA  . GLY B 138  ? 0.8543 0.8394 0.8969 0.0805  0.0589  0.0006  138  GLY B CA  
2251  C  C   . GLY B 138  ? 0.9087 0.8991 0.9529 0.0805  0.0547  -0.0019 138  GLY B C   
2252  O  O   . GLY B 138  ? 0.9882 0.9860 1.0401 0.0803  0.0525  -0.0023 138  GLY B O   
2253  N  N   . GLY B 139  ? 1.1649 1.1515 1.2016 0.0810  0.0533  -0.0038 139  GLY B N   
2254  C  CA  . GLY B 139  ? 1.1629 1.1542 1.2002 0.0818  0.0491  -0.0062 139  GLY B CA  
2255  C  C   . GLY B 139  ? 1.1022 1.0931 1.1328 0.0801  0.0463  -0.0102 139  GLY B C   
2256  O  O   . GLY B 139  ? 1.1287 1.1128 1.1520 0.0791  0.0480  -0.0106 139  GLY B O   
2257  N  N   . THR B 140  ? 0.7348 0.7331 0.7679 0.0798  0.0418  -0.0133 140  THR B N   
2258  C  CA  . THR B 140  ? 0.7870 0.7873 0.8153 0.0781  0.0383  -0.0178 140  THR B CA  
2259  C  C   . THR B 140  ? 0.7913 0.7948 0.8183 0.0816  0.0345  -0.0193 140  THR B C   
2260  O  O   . THR B 140  ? 0.7533 0.7586 0.7844 0.0845  0.0343  -0.0173 140  THR B O   
2261  C  CB  . THR B 140  ? 0.7164 0.7249 0.7500 0.0732  0.0364  -0.0212 140  THR B CB  
2262  O  OG1 . THR B 140  ? 0.7110 0.7295 0.7520 0.0737  0.0330  -0.0226 140  THR B OG1 
2263  C  CG2 . THR B 140  ? 0.7763 0.7828 0.8128 0.0705  0.0402  -0.0191 140  THR B CG2 
2264  N  N   . ASP B 141  ? 0.9884 0.9923 1.0094 0.0815  0.0313  -0.0231 141  ASP B N   
2265  C  CA  . ASP B 141  ? 0.8842 0.8924 0.9036 0.0848  0.0269  -0.0253 141  ASP B CA  
2266  C  C   . ASP B 141  ? 0.9135 0.9341 0.9397 0.0819  0.0225  -0.0299 141  ASP B C   
2267  O  O   . ASP B 141  ? 0.9789 1.0038 1.0097 0.0769  0.0232  -0.0314 141  ASP B O   
2268  C  CB  . ASP B 141  ? 0.9919 0.9934 1.0003 0.0873  0.0257  -0.0269 141  ASP B CB  
2269  C  CG  . ASP B 141  ? 1.1082 1.1096 1.1131 0.0827  0.0248  -0.0307 141  ASP B CG  
2270  O  OD1 . ASP B 141  ? 1.3128 1.3135 1.3208 0.0783  0.0277  -0.0302 141  ASP B OD1 
2271  O  OD2 . ASP B 141  ? 1.0339 1.0359 1.0327 0.0837  0.0212  -0.0344 141  ASP B OD2 
2272  N  N   . LEU B 142  ? 0.7138 0.7400 0.7401 0.0853  0.0183  -0.0319 142  LEU B N   
2273  C  CA  . LEU B 142  ? 0.7356 0.7746 0.7689 0.0833  0.0142  -0.0360 142  LEU B CA  
2274  C  C   . LEU B 142  ? 0.7606 0.8042 0.7933 0.0784  0.0123  -0.0409 142  LEU B C   
2275  O  O   . LEU B 142  ? 0.8105 0.8640 0.8505 0.0745  0.0108  -0.0438 142  LEU B O   
2276  C  CB  . LEU B 142  ? 0.7915 0.8347 0.8237 0.0888  0.0099  -0.0374 142  LEU B CB  
2277  C  CG  . LEU B 142  ? 0.7958 0.8372 0.8189 0.0922  0.0064  -0.0402 142  LEU B CG  
2278  C  CD1 . LEU B 142  ? 0.8860 0.9355 0.9104 0.0968  0.0014  -0.0426 142  LEU B CD1 
2279  C  CD2 . LEU B 142  ? 0.8347 0.8624 0.8479 0.0960  0.0094  -0.0364 142  LEU B CD2 
2280  N  N   . PHE B 143  ? 0.8535 0.8899 0.8774 0.0784  0.0125  -0.0420 143  PHE B N   
2281  C  CA  . PHE B 143  ? 0.9510 0.9913 0.9740 0.0734  0.0107  -0.0470 143  PHE B CA  
2282  C  C   . PHE B 143  ? 0.9316 0.9696 0.9577 0.0671  0.0148  -0.0462 143  PHE B C   
2283  O  O   . PHE B 143  ? 0.8771 0.9222 0.9074 0.0617  0.0138  -0.0501 143  PHE B O   
2284  C  CB  . PHE B 143  ? 0.9073 0.9398 0.9192 0.0754  0.0094  -0.0485 143  PHE B CB  
2285  C  CG  . PHE B 143  ? 0.8715 0.9046 0.8786 0.0823  0.0056  -0.0489 143  PHE B CG  
2286  C  CD1 . PHE B 143  ? 0.8916 0.9368 0.9028 0.0836  0.0001  -0.0532 143  PHE B CD1 
2287  C  CD2 . PHE B 143  ? 0.9560 0.9774 0.9544 0.0877  0.0077  -0.0449 143  PHE B CD2 
2288  C  CE1 . PHE B 143  ? 0.9226 0.9677 0.9284 0.0905  -0.0035 -0.0535 143  PHE B CE1 
2289  C  CE2 . PHE B 143  ? 0.9358 0.9567 0.9287 0.0943  0.0045  -0.0451 143  PHE B CE2 
2290  C  CZ  . PHE B 143  ? 0.9325 0.9650 0.9289 0.0959  -0.0012 -0.0494 143  PHE B CZ  
2291  N  N   . ALA B 144  ? 0.5481 0.5764 0.5723 0.0678  0.0198  -0.0412 144  ALA B N   
2292  C  CA  . ALA B 144  ? 0.4679 0.4936 0.4945 0.0628  0.0238  -0.0400 144  ALA B CA  
2293  C  C   . ALA B 144  ? 0.6674 0.7030 0.7044 0.0604  0.0236  -0.0402 144  ALA B C   
2294  O  O   . ALA B 144  ? 0.8282 0.8655 0.8680 0.0551  0.0254  -0.0415 144  ALA B O   
2295  C  CB  . ALA B 144  ? 0.4619 0.4758 0.4843 0.0651  0.0288  -0.0345 144  ALA B CB  
2296  N  N   . GLN B 145  ? 0.8459 0.8875 0.8882 0.0641  0.0216  -0.0390 145  GLN B N   
2297  C  CA  . GLN B 145  ? 0.8789 0.9303 0.9306 0.0623  0.0210  -0.0396 145  GLN B CA  
2298  C  C   . GLN B 145  ? 0.8604 0.9233 0.9160 0.0591  0.0172  -0.0452 145  GLN B C   
2299  O  O   . GLN B 145  ? 0.9323 1.0017 0.9941 0.0549  0.0179  -0.0467 145  GLN B O   
2300  C  CB  . GLN B 145  ? 0.8219 0.8754 0.8775 0.0673  0.0201  -0.0368 145  GLN B CB  
2301  C  CG  . GLN B 145  ? 0.8432 0.8866 0.8961 0.0703  0.0238  -0.0314 145  GLN B CG  
2302  C  CD  . GLN B 145  ? 0.8728 0.9132 0.9285 0.0673  0.0280  -0.0289 145  GLN B CD  
2303  O  OE1 . GLN B 145  ? 0.9405 0.9720 0.9911 0.0666  0.0314  -0.0268 145  GLN B OE1 
2304  N  NE2 . GLN B 145  ? 0.8036 0.8513 0.8669 0.0658  0.0277  -0.0290 145  GLN B NE2 
2305  N  N   . ALA B 146  ? 0.5397 0.6054 0.5918 0.0612  0.0132  -0.0485 146  ALA B N   
2306  C  CA  . ALA B 146  ? 0.5156 0.5936 0.5721 0.0589  0.0091  -0.0541 146  ALA B CA  
2307  C  C   . ALA B 146  ? 0.5067 0.5848 0.5614 0.0524  0.0096  -0.0581 146  ALA B C   
2308  O  O   . ALA B 146  ? 0.5418 0.6308 0.6015 0.0491  0.0068  -0.0630 146  ALA B O   
2309  C  CB  . ALA B 146  ? 0.5315 0.6132 0.5851 0.0645  0.0040  -0.0562 146  ALA B CB  
2310  N  N   . GLU B 147  ? 0.7990 0.8650 0.8467 0.0504  0.0132  -0.0561 147  GLU B N   
2311  C  CA  . GLU B 147  ? 0.8644 0.9288 0.9098 0.0439  0.0143  -0.0598 147  GLU B CA  
2312  C  C   . GLU B 147  ? 0.8752 0.9460 0.9282 0.0377  0.0166  -0.0610 147  GLU B C   
2313  O  O   . GLU B 147  ? 0.9429 1.0162 0.9963 0.0315  0.0167  -0.0653 147  GLU B O   
2314  C  CB  . GLU B 147  ? 0.9036 0.9526 0.9395 0.0437  0.0182  -0.0568 147  GLU B CB  
2315  C  CG  . GLU B 147  ? 0.9043 0.9494 0.9333 0.0399  0.0172  -0.0612 147  GLU B CG  
2316  C  CD  . GLU B 147  ? 1.0006 1.0480 1.0251 0.0443  0.0120  -0.0641 147  GLU B CD  
2317  O  OE1 . GLU B 147  ? 0.9230 0.9668 0.9444 0.0511  0.0113  -0.0606 147  GLU B OE1 
2318  O  OE2 . GLU B 147  ? 1.2031 1.2556 1.2269 0.0410  0.0087  -0.0698 147  GLU B OE2 
2319  N  N   . ILE B 148  ? 0.6800 0.7531 0.7387 0.0391  0.0185  -0.0575 148  ILE B N   
2320  C  CA  . ILE B 148  ? 0.7326 0.8120 0.7981 0.0339  0.0206  -0.0586 148  ILE B CA  
2321  C  C   . ILE B 148  ? 0.7045 0.7989 0.7770 0.0314  0.0167  -0.0643 148  ILE B C   
2322  O  O   . ILE B 148  ? 0.6937 0.7920 0.7686 0.0249  0.0177  -0.0680 148  ILE B O   
2323  C  CB  . ILE B 148  ? 0.5275 0.6067 0.5973 0.0369  0.0228  -0.0538 148  ILE B CB  
2324  C  CG1 . ILE B 148  ? 0.5022 0.5677 0.5661 0.0376  0.0275  -0.0488 148  ILE B CG1 
2325  C  CG2 . ILE B 148  ? 0.5327 0.6213 0.6103 0.0329  0.0238  -0.0555 148  ILE B CG2 
2326  C  CD1 . ILE B 148  ? 0.6054 0.6645 0.6659 0.0315  0.0316  -0.0495 148  ILE B CD1 
2327  N  N   . LEU B 149  ? 0.6087 0.7116 0.6847 0.0367  0.0123  -0.0651 149  LEU B N   
2328  C  CA  . LEU B 149  ? 0.6453 0.7635 0.7283 0.0353  0.0082  -0.0705 149  LEU B CA  
2329  C  C   . LEU B 149  ? 0.6608 0.7812 0.7406 0.0328  0.0051  -0.0759 149  LEU B C   
2330  O  O   . LEU B 149  ? 0.6841 0.8165 0.7700 0.0285  0.0031  -0.0812 149  LEU B O   
2331  C  CB  . LEU B 149  ? 0.6282 0.7536 0.7146 0.0425  0.0043  -0.0697 149  LEU B CB  
2332  C  CG  . LEU B 149  ? 0.4270 0.5694 0.5226 0.0419  0.0010  -0.0742 149  LEU B CG  
2333  C  CD1 . LEU B 149  ? 0.4618 0.6086 0.5643 0.0371  0.0048  -0.0737 149  LEU B CD1 
2334  C  CD2 . LEU B 149  ? 0.4585 0.6058 0.5552 0.0499  -0.0030 -0.0734 149  LEU B CD2 
2335  N  N   . THR B 150  ? 0.9008 1.0105 0.9713 0.0353  0.0046  -0.0747 150  THR B N   
2336  C  CA  . THR B 150  ? 0.9767 1.0874 1.0431 0.0329  0.0016  -0.0799 150  THR B CA  
2337  C  C   . THR B 150  ? 0.9686 1.0783 1.0360 0.0238  0.0047  -0.0830 150  THR B C   
2338  O  O   . THR B 150  ? 1.0181 1.1359 1.0878 0.0195  0.0019  -0.0891 150  THR B O   
2339  C  CB  . THR B 150  ? 0.9610 1.0586 1.0162 0.0377  0.0011  -0.0775 150  THR B CB  
2340  O  OG1 . THR B 150  ? 1.0067 1.1055 1.0609 0.0460  -0.0017 -0.0750 150  THR B OG1 
2341  C  CG2 . THR B 150  ? 0.8782 0.9761 0.9282 0.0354  -0.0022 -0.0831 150  THR B CG2 
2342  N  N   . MET B 151  ? 0.9602 1.0597 1.0256 0.0207  0.0106  -0.0790 151  MET B N   
2343  C  CA  . MET B 151  ? 0.9728 1.0698 1.0384 0.0121  0.0143  -0.0814 151  MET B CA  
2344  C  C   . MET B 151  ? 1.0569 1.1684 1.1334 0.0070  0.0143  -0.0849 151  MET B C   
2345  O  O   . MET B 151  ? 1.0436 1.1591 1.1223 -0.0003 0.0148  -0.0898 151  MET B O   
2346  C  CB  . MET B 151  ? 0.8929 0.9749 0.9529 0.0112  0.0206  -0.0758 151  MET B CB  
2347  C  CG  . MET B 151  ? 0.8245 0.9013 0.8830 0.0026  0.0251  -0.0777 151  MET B CG  
2348  S  SD  . MET B 151  ? 0.8339 0.9006 0.8911 0.0019  0.0322  -0.0713 151  MET B SD  
2349  C  CE  . MET B 151  ? 0.8605 0.9269 0.9189 -0.0089 0.0363  -0.0754 151  MET B CE  
2350  N  N   . TYR B 152  ? 0.9700 1.0894 1.0533 0.0108  0.0138  -0.0827 152  TYR B N   
2351  C  CA  . TYR B 152  ? 0.8853 1.0185 0.9789 0.0069  0.0141  -0.0855 152  TYR B CA  
2352  C  C   . TYR B 152  ? 0.9432 1.0933 1.0437 0.0086  0.0080  -0.0910 152  TYR B C   
2353  O  O   . TYR B 152  ? 0.9328 1.0956 1.0423 0.0085  0.0074  -0.0923 152  TYR B O   
2354  C  CB  . TYR B 152  ? 0.7778 0.9107 0.8748 0.0102  0.0168  -0.0803 152  TYR B CB  
2355  C  CG  . TYR B 152  ? 0.7379 0.8575 0.8303 0.0072  0.0232  -0.0759 152  TYR B CG  
2356  C  CD1 . TYR B 152  ? 0.7631 0.8819 0.8567 -0.0007 0.0275  -0.0777 152  TYR B CD1 
2357  C  CD2 . TYR B 152  ? 0.6838 0.7917 0.7705 0.0124  0.0250  -0.0699 152  TYR B CD2 
2358  C  CE1 . TYR B 152  ? 0.7054 0.8115 0.7938 -0.0028 0.0333  -0.0736 152  TYR B CE1 
2359  C  CE2 . TYR B 152  ? 0.6185 0.7149 0.7009 0.0104  0.0305  -0.0660 152  TYR B CE2 
2360  C  CZ  . TYR B 152  ? 0.6613 0.7565 0.7441 0.0030  0.0346  -0.0677 152  TYR B CZ  
2361  O  OH  . TYR B 152  ? 0.6129 0.6959 0.6904 0.0016  0.0401  -0.0637 152  TYR B OH  
2362  N  N   . ASP B 153  ? 1.3879 1.5383 1.4842 0.0106  0.0034  -0.0942 153  ASP B N   
2363  C  CA  . ASP B 153  ? 1.4065 1.5734 1.5091 0.0124  -0.0027 -0.0998 153  ASP B CA  
2364  C  C   . ASP B 153  ? 1.4594 1.6380 1.5700 0.0036  -0.0022 -0.1061 153  ASP B C   
2365  O  O   . ASP B 153  ? 1.4272 1.5989 1.5343 -0.0035 0.0005  -0.1081 153  ASP B O   
2366  C  CB  . ASP B 153  ? 1.4493 1.6127 1.5442 0.0171  -0.0077 -0.1017 153  ASP B CB  
2367  C  CG  . ASP B 153  ? 1.5601 1.7155 1.6488 0.0266  -0.0090 -0.0962 153  ASP B CG  
2368  O  OD1 . ASP B 153  ? 1.4943 1.6532 1.5874 0.0307  -0.0084 -0.0929 153  ASP B OD1 
2369  O  OD2 . ASP B 153  ? 1.6432 1.7884 1.7223 0.0300  -0.0104 -0.0952 153  ASP B OD2 
2370  N  N   . PRO B 154  ? 0.8281 1.0241 0.9493 0.0036  -0.0045 -0.1095 154  PRO B N   
2371  C  CA  . PRO B 154  ? 0.8452 1.0538 0.9749 -0.0050 -0.0040 -0.1159 154  PRO B CA  
2372  C  C   . PRO B 154  ? 0.8684 1.0842 0.9981 -0.0069 -0.0094 -0.1228 154  PRO B C   
2373  O  O   . PRO B 154  ? 0.8880 1.1141 1.0248 -0.0148 -0.0092 -0.1288 154  PRO B O   
2374  C  CB  . PRO B 154  ? 0.7265 0.9517 0.8674 -0.0026 -0.0051 -0.1167 154  PRO B CB  
2375  C  CG  . PRO B 154  ? 0.6511 0.8760 0.7888 0.0083  -0.0095 -0.1136 154  PRO B CG  
2376  C  CD  . PRO B 154  ? 0.6718 0.8766 0.7976 0.0115  -0.0074 -0.1075 154  PRO B CD  
2377  N  N   . ASP B 155  ? 1.0513 1.2617 1.1730 -0.0001 -0.0142 -0.1224 155  ASP B N   
2378  C  CA  . ASP B 155  ? 0.9537 1.1703 1.0740 -0.0007 -0.0200 -0.1290 155  ASP B CA  
2379  C  C   . ASP B 155  ? 1.0635 1.2635 1.1725 -0.0041 -0.0185 -0.1289 155  ASP B C   
2380  O  O   . ASP B 155  ? 1.2503 1.4523 1.3555 -0.0034 -0.0236 -0.1336 155  ASP B O   
2381  C  CB  . ASP B 155  ? 1.0513 1.2744 1.1698 0.0100  -0.0270 -0.1292 155  ASP B CB  
2382  C  CG  . ASP B 155  ? 1.0553 1.2941 1.1840 0.0143  -0.0286 -0.1293 155  ASP B CG  
2383  O  OD1 . ASP B 155  ? 0.9996 1.2550 1.1394 0.0093  -0.0294 -0.1347 155  ASP B OD1 
2384  O  OD2 . ASP B 155  ? 1.1348 1.3691 1.2603 0.0226  -0.0290 -0.1240 155  ASP B OD2 
2385  N  N   . ARG B 156  ? 0.7651 0.9489 0.8683 -0.0073 -0.0119 -0.1237 156  ARG B N   
2386  C  CA  . ARG B 156  ? 0.8216 0.9892 0.9140 -0.0109 -0.0099 -0.1236 156  ARG B CA  
2387  C  C   . ARG B 156  ? 0.8123 0.9853 0.9085 -0.0214 -0.0096 -0.1309 156  ARG B C   
2388  O  O   . ARG B 156  ? 0.7565 0.9411 0.8633 -0.0280 -0.0076 -0.1338 156  ARG B O   
2389  C  CB  . ARG B 156  ? 0.7596 0.9092 0.8453 -0.0114 -0.0026 -0.1162 156  ARG B CB  
2390  C  CG  . ARG B 156  ? 0.6763 0.8152 0.7543 -0.0016 -0.0029 -0.1094 156  ARG B CG  
2391  C  CD  . ARG B 156  ? 0.6563 0.7794 0.7291 -0.0024 0.0041  -0.1025 156  ARG B CD  
2392  N  NE  . ARG B 156  ? 0.8185 0.9287 0.8841 -0.0092 0.0081  -0.1034 156  ARG B NE  
2393  C  CZ  . ARG B 156  ? 0.7343 0.8336 0.7974 -0.0132 0.0147  -0.0996 156  ARG B CZ  
2394  N  NH1 . ARG B 156  ? 0.6577 0.7577 0.7252 -0.0113 0.0181  -0.0948 156  ARG B NH1 
2395  N  NH2 . ARG B 156  ? 0.7743 0.8615 0.8300 -0.0190 0.0180  -0.1009 156  ARG B NH2 
2396  N  N   . SER B 157  ? 1.0879 1.2524 1.1754 -0.0231 -0.0115 -0.1338 157  SER B N   
2397  C  CA  . SER B 157  ? 1.1608 1.3299 1.2512 -0.0331 -0.0118 -0.1414 157  SER B CA  
2398  C  C   . SER B 157  ? 1.1197 1.2802 1.2110 -0.0427 -0.0036 -0.1398 157  SER B C   
2399  O  O   . SER B 157  ? 1.0311 1.1745 1.1143 -0.0416 0.0019  -0.1333 157  SER B O   
2400  C  CB  . SER B 157  ? 1.2313 1.3902 1.3102 -0.0324 -0.0153 -0.1443 157  SER B CB  
2401  O  OG  . SER B 157  ? 1.2928 1.4310 1.3587 -0.0277 -0.0118 -0.1373 157  SER B OG  
2402  N  N   . THR B 158  ? 1.0285 1.2013 1.1298 -0.0519 -0.0028 -0.1459 158  THR B N   
2403  C  CA  . THR B 158  ? 0.8869 1.0530 0.9899 -0.0615 0.0051  -0.1450 158  THR B CA  
2404  C  C   . THR B 158  ? 0.9137 1.0756 1.0146 -0.0723 0.0065  -0.1514 158  THR B C   
2405  O  O   . THR B 158  ? 0.9677 1.1176 1.0653 -0.0796 0.0138  -0.1497 158  THR B O   
2406  C  CB  . THR B 158  ? 0.7714 0.9544 0.8886 -0.0642 0.0071  -0.1457 158  THR B CB  
2407  O  OG1 . THR B 158  ? 0.9071 1.1090 1.0352 -0.0703 0.0032  -0.1546 158  THR B OG1 
2408  C  CG2 . THR B 158  ? 0.6913 0.8817 0.8118 -0.0534 0.0042  -0.1409 158  THR B CG2 
2409  N  N   . THR B 159  ? 0.9114 1.0822 1.0136 -0.0735 -0.0001 -0.1588 159  THR B N   
2410  C  CA  . THR B 159  ? 1.0423 1.2109 1.1437 -0.0844 0.0007  -0.1659 159  THR B CA  
2411  C  C   . THR B 159  ? 1.0674 1.2332 1.1606 -0.0813 -0.0063 -0.1703 159  THR B C   
2412  O  O   . THR B 159  ? 1.0280 1.1996 1.1196 -0.0713 -0.0128 -0.1696 159  THR B O   
2413  C  CB  . THR B 159  ? 1.0974 1.2873 1.2149 -0.0932 0.0002  -0.1732 159  THR B CB  
2414  O  OG1 . THR B 159  ? 1.2015 1.3886 1.3180 -0.1043 0.0010  -0.1804 159  THR B OG1 
2415  C  CG2 . THR B 159  ? 0.9889 1.2020 1.1165 -0.0867 -0.0085 -0.1775 159  THR B CG2 
2416  N  N   . VAL B 160  ? 1.0991 1.2552 1.1865 -0.0899 -0.0048 -0.1749 160  VAL B N   
2417  C  CA  . VAL B 160  ? 1.1010 1.2543 1.1805 -0.0885 -0.0113 -0.1803 160  VAL B CA  
2418  C  C   . VAL B 160  ? 1.2099 1.3878 1.3021 -0.0911 -0.0190 -0.1899 160  VAL B C   
2419  O  O   . VAL B 160  ? 1.2426 1.4341 1.3475 -0.1004 -0.0173 -0.1950 160  VAL B O   
2420  C  CB  . VAL B 160  ? 1.1640 1.2976 1.2325 -0.0972 -0.0067 -0.1821 160  VAL B CB  
2421  C  CG1 . VAL B 160  ? 1.2723 1.4049 1.3338 -0.0970 -0.0138 -0.1891 160  VAL B CG1 
2422  C  CG2 . VAL B 160  ? 1.1698 1.2792 1.2248 -0.0930 0.0002  -0.1726 160  VAL B CG2 
2423  N  N   . LEU B 161  ? 1.1639 1.3480 1.2527 -0.0826 -0.0275 -0.1923 161  LEU B N   
2424  C  CA  . LEU B 161  ? 1.2398 1.4477 1.3396 -0.0830 -0.0359 -0.2013 161  LEU B CA  
2425  C  C   . LEU B 161  ? 1.2540 1.4572 1.3446 -0.0840 -0.0420 -0.2080 161  LEU B C   
2426  O  O   . LEU B 161  ? 1.3600 1.5525 1.4378 -0.0745 -0.0456 -0.2051 161  LEU B O   
2427  C  CB  . LEU B 161  ? 1.1579 1.3800 1.2627 -0.0708 -0.0414 -0.1985 161  LEU B CB  
2428  C  CG  . LEU B 161  ? 0.9724 1.1977 1.0847 -0.0683 -0.0358 -0.1913 161  LEU B CG  
2429  C  CD1 . LEU B 161  ? 1.0120 1.2444 1.1242 -0.0547 -0.0408 -0.1871 161  LEU B CD1 
2430  C  CD2 . LEU B 161  ? 0.9892 1.2330 1.1185 -0.0779 -0.0334 -0.1962 161  LEU B CD2 
2431  N  N   . ARG B 162  ? 1.2525 1.4638 1.3497 -0.0954 -0.0430 -0.2171 162  ARG B N   
2432  C  CA  . ARG B 162  ? 1.3589 1.5673 1.4483 -0.0971 -0.0494 -0.2246 162  ARG B CA  
2433  C  C   . ARG B 162  ? 1.4408 1.6668 1.5328 -0.0872 -0.0602 -0.2289 162  ARG B C   
2434  O  O   . ARG B 162  ? 1.5004 1.7172 1.5792 -0.0797 -0.0653 -0.2290 162  ARG B O   
2435  C  CB  . ARG B 162  ? 1.3666 1.5807 1.4637 -0.1123 -0.0479 -0.2338 162  ARG B CB  
2436  C  CG  . ARG B 162  ? 1.4888 1.6951 1.5756 -0.1154 -0.0531 -0.2411 162  ARG B CG  
2437  C  CD  . ARG B 162  ? 1.5879 1.8025 1.6841 -0.1309 -0.0524 -0.2512 162  ARG B CD  
2438  N  NE  . ARG B 162  ? 1.7961 2.0404 1.9086 -0.1321 -0.0605 -0.2604 162  ARG B NE  
2439  C  CZ  . ARG B 162  ? 1.7408 1.9946 1.8521 -0.1307 -0.0701 -0.2691 162  ARG B CZ  
2440  N  NH1 . ARG B 162  ? 1.6321 1.8680 1.7265 -0.1281 -0.0729 -0.2700 162  ARG B NH1 
2441  N  NH2 . ARG B 162  ? 1.7428 2.0251 1.8703 -0.1316 -0.0772 -0.2772 162  ARG B NH2 
2442  N  N   . GLN B 163  ? 1.1903 1.4415 1.2988 -0.0868 -0.0638 -0.2326 163  GLN B N   
2443  C  CA  . GLN B 163  ? 1.2850 1.5544 1.3969 -0.0768 -0.0740 -0.2365 163  GLN B CA  
2444  C  C   . GLN B 163  ? 1.2115 1.4999 1.3378 -0.0723 -0.0738 -0.2338 163  GLN B C   
2445  O  O   . GLN B 163  ? 1.1663 1.4794 1.3064 -0.0727 -0.0796 -0.2408 163  GLN B O   
2446  C  CB  . GLN B 163  ? 1.4285 1.7133 1.5462 -0.0831 -0.0817 -0.2489 163  GLN B CB  
2447  C  CG  . GLN B 163  ? 1.3557 1.6248 1.4568 -0.0817 -0.0859 -0.2520 163  GLN B CG  
2448  C  CD  . GLN B 163  ? 1.3724 1.6605 1.4779 -0.0811 -0.0970 -0.2632 163  GLN B CD  
2449  O  OE1 . GLN B 163  ? 1.4258 1.7395 1.5466 -0.0802 -0.1020 -0.2683 163  GLN B OE1 
2450  N  NE2 . GLN B 163  ? 1.4836 1.7593 1.5755 -0.0815 -0.1009 -0.2673 163  GLN B NE2 
2451  N  N   . GLY B 164  ? 1.1613 1.4381 1.2842 -0.0675 -0.0672 -0.2237 164  GLY B N   
2452  C  CA  . GLY B 164  ? 1.0529 1.3440 1.1893 -0.0661 -0.0644 -0.2205 164  GLY B CA  
2453  C  C   . GLY B 164  ? 1.0633 1.3601 1.2120 -0.0796 -0.0572 -0.2227 164  GLY B C   
2454  O  O   . GLY B 164  ? 1.0067 1.3117 1.1651 -0.0792 -0.0531 -0.2190 164  GLY B O   
2455  N  N   . VAL B 165  ? 1.6870 1.9787 1.8349 -0.0913 -0.0553 -0.2286 165  VAL B N   
2456  C  CA  . VAL B 165  ? 1.6442 1.9397 1.8029 -0.1050 -0.0478 -0.2309 165  VAL B CA  
2457  C  C   . VAL B 165  ? 1.6175 1.8874 1.7658 -0.1078 -0.0375 -0.2219 165  VAL B C   
2458  O  O   . VAL B 165  ? 1.6468 1.8946 1.7791 -0.1056 -0.0364 -0.2185 165  VAL B O   
2459  C  CB  . VAL B 165  ? 1.8367 2.1383 1.9993 -0.1166 -0.0505 -0.2416 165  VAL B CB  
2460  C  CG1 . VAL B 165  ? 1.8876 2.1674 2.0325 -0.1162 -0.0520 -0.2418 165  VAL B CG1 
2461  C  CG2 . VAL B 165  ? 1.8572 2.1589 2.0288 -0.1310 -0.0416 -0.2433 165  VAL B CG2 
2462  N  N   . PRO B 166  ? 1.0467 1.3189 1.2032 -0.1120 -0.0300 -0.2179 166  PRO B N   
2463  C  CA  . PRO B 166  ? 0.9938 1.2420 1.1406 -0.1157 -0.0201 -0.2102 166  PRO B CA  
2464  C  C   . PRO B 166  ? 0.9835 1.2173 1.1235 -0.1274 -0.0164 -0.2145 166  PRO B C   
2465  O  O   . PRO B 166  ? 0.9499 1.1951 1.0998 -0.1386 -0.0163 -0.2227 166  PRO B O   
2466  C  CB  . PRO B 166  ? 0.9093 1.1678 1.0689 -0.1194 -0.0137 -0.2075 166  PRO B CB  
2467  C  CG  . PRO B 166  ? 0.8450 1.1286 1.0170 -0.1120 -0.0207 -0.2101 166  PRO B CG  
2468  C  CD  . PRO B 166  ? 0.9909 1.2866 1.1646 -0.1119 -0.0302 -0.2193 166  PRO B CD  
2469  N  N   . SER B 167  ? 1.2437 1.4520 1.3666 -0.1248 -0.0134 -0.2091 167  SER B N   
2470  C  CA  . SER B 167  ? 1.3301 1.5214 1.4441 -0.1350 -0.0096 -0.2124 167  SER B CA  
2471  C  C   . SER B 167  ? 1.2406 1.4063 1.3426 -0.1358 0.0002  -0.2035 167  SER B C   
2472  O  O   . SER B 167  ? 1.1776 1.3417 1.2812 -0.1307 0.0045  -0.1958 167  SER B O   
2473  C  CB  . SER B 167  ? 1.3859 1.5715 1.4891 -0.1313 -0.0172 -0.2169 167  SER B CB  
2474  O  OG  . SER B 167  ? 1.5713 1.7474 1.6700 -0.1430 -0.0152 -0.2233 167  SER B OG  
2475  N  N   . THR B 168  ? 1.5580 1.7034 1.6476 -0.1419 0.0035  -0.2046 168  THR B N   
2476  C  CA  . THR B 168  ? 1.5694 1.6897 1.6468 -0.1431 0.0128  -0.1969 168  THR B CA  
2477  C  C   . THR B 168  ? 1.5537 1.6527 1.6127 -0.1356 0.0113  -0.1931 168  THR B C   
2478  O  O   . THR B 168  ? 1.6248 1.7271 1.6798 -0.1312 0.0036  -0.1972 168  THR B O   
2479  C  CB  . THR B 168  ? 1.5847 1.6972 1.6629 -0.1579 0.0202  -0.2009 168  THR B CB  
2480  O  OG1 . THR B 168  ? 1.7110 1.8210 1.7851 -0.1647 0.0162  -0.2096 168  THR B OG1 
2481  C  CG2 . THR B 168  ? 1.6561 1.7894 1.7526 -0.1654 0.0226  -0.2043 168  THR B CG2 
2482  N  N   . TRP B 169  ? 1.1960 1.2729 1.2436 -0.1339 0.0190  -0.1850 169  TRP B N   
2483  C  CA  . TRP B 169  ? 1.1852 1.2406 1.2151 -0.1269 0.0189  -0.1806 169  TRP B CA  
2484  C  C   . TRP B 169  ? 1.2329 1.2724 1.2521 -0.1355 0.0205  -0.1860 169  TRP B C   
2485  O  O   . TRP B 169  ? 1.2913 1.3195 1.2979 -0.1306 0.0170  -0.1864 169  TRP B O   
2486  C  CB  . TRP B 169  ? 1.1465 1.1859 1.1690 -0.1208 0.0262  -0.1697 169  TRP B CB  
2487  C  CG  . TRP B 169  ? 1.1596 1.1744 1.1637 -0.1157 0.0286  -0.1649 169  TRP B CG  
2488  C  CD1 . TRP B 169  ? 1.1394 1.1318 1.1318 -0.1205 0.0362  -0.1624 169  TRP B CD1 
2489  C  CD2 . TRP B 169  ? 1.1711 1.1809 1.1662 -0.1044 0.0236  -0.1619 169  TRP B CD2 
2490  N  NE1 . TRP B 169  ? 1.0738 1.0483 1.0509 -0.1128 0.0361  -0.1581 169  TRP B NE1 
2491  C  CE2 . TRP B 169  ? 1.0366 1.0214 1.0152 -0.1030 0.0286  -0.1577 169  TRP B CE2 
2492  C  CE3 . TRP B 169  ? 1.1519 1.1755 1.1508 -0.0951 0.0156  -0.1623 169  TRP B CE3 
2493  C  CZ2 . TRP B 169  ? 0.9326 0.9065 0.8990 -0.0930 0.0260  -0.1540 169  TRP B CZ2 
2494  C  CZ3 . TRP B 169  ? 1.0481 1.0600 1.0344 -0.0853 0.0132  -0.1585 169  TRP B CZ3 
2495  C  CH2 . TRP B 169  ? 1.0121 0.9998 0.9827 -0.0844 0.0185  -0.1544 169  TRP B CH2 
2496  N  N   . ALA B 170  ? 0.9729 1.0108 0.9962 -0.1483 0.0260  -0.1902 170  ALA B N   
2497  C  CA  . ALA B 170  ? 0.9819 1.0044 0.9952 -0.1574 0.0277  -0.1959 170  ALA B CA  
2498  C  C   . ALA B 170  ? 1.1338 1.1702 1.1512 -0.1602 0.0183  -0.2063 170  ALA B C   
2499  O  O   . ALA B 170  ? 1.2667 1.2896 1.2718 -0.1615 0.0163  -0.2099 170  ALA B O   
2500  C  CB  . ALA B 170  ? 0.9298 0.9468 0.9467 -0.1707 0.0364  -0.1976 170  ALA B CB  
2501  N  N   . GLU B 171  ? 1.3768 1.4402 1.4113 -0.1608 0.0125  -0.2113 171  GLU B N   
2502  C  CA  . GLU B 171  ? 1.4867 1.5654 1.5258 -0.1622 0.0027  -0.2212 171  GLU B CA  
2503  C  C   . GLU B 171  ? 1.5225 1.5961 1.5500 -0.1492 -0.0044 -0.2190 171  GLU B C   
2504  O  O   . GLU B 171  ? 1.5692 1.6395 1.5895 -0.1502 -0.0100 -0.2254 171  GLU B O   
2505  C  CB  . GLU B 171  ? 1.5027 1.6122 1.5628 -0.1641 -0.0019 -0.2262 171  GLU B CB  
2506  C  CG  . GLU B 171  ? 1.6454 1.7731 1.7125 -0.1674 -0.0116 -0.2377 171  GLU B CG  
2507  C  CD  . GLU B 171  ? 1.7444 1.8978 1.8322 -0.1770 -0.0123 -0.2450 171  GLU B CD  
2508  O  OE1 . GLU B 171  ? 1.6104 1.7826 1.7107 -0.1715 -0.0140 -0.2426 171  GLU B OE1 
2509  O  OE2 . GLU B 171  ? 1.9317 2.0865 2.0235 -0.1901 -0.0111 -0.2533 171  GLU B OE2 
2510  N  N   . PHE B 172  ? 1.3167 1.3894 1.3422 -0.1370 -0.0043 -0.2100 172  PHE B N   
2511  C  CA  . PHE B 172  ? 1.3250 1.3913 1.3389 -0.1244 -0.0100 -0.2070 172  PHE B CA  
2512  C  C   . PHE B 172  ? 1.3764 1.4147 1.3706 -0.1239 -0.0061 -0.2043 172  PHE B C   
2513  O  O   . PHE B 172  ? 1.4518 1.4842 1.4353 -0.1187 -0.0117 -0.2067 172  PHE B O   
2514  C  CB  . PHE B 172  ? 1.1931 1.2638 1.2097 -0.1124 -0.0095 -0.1978 172  PHE B CB  
2515  C  CG  . PHE B 172  ? 1.2086 1.2665 1.2108 -0.0998 -0.0122 -0.1922 172  PHE B CG  
2516  C  CD1 . PHE B 172  ? 1.2405 1.3069 1.2402 -0.0929 -0.0214 -0.1965 172  PHE B CD1 
2517  C  CD2 . PHE B 172  ? 1.1885 1.2261 1.1796 -0.0946 -0.0054 -0.1827 172  PHE B CD2 
2518  C  CE1 . PHE B 172  ? 1.2151 1.2692 1.2012 -0.0814 -0.0233 -0.1912 172  PHE B CE1 
2519  C  CE2 . PHE B 172  ? 1.0931 1.1194 1.0716 -0.0833 -0.0074 -0.1775 172  PHE B CE2 
2520  C  CZ  . PHE B 172  ? 1.0878 1.1220 1.0636 -0.0768 -0.0161 -0.1817 172  PHE B CZ  
2521  N  N   . THR B 173  ? 1.1289 1.1494 1.1175 -0.1290 0.0034  -0.1993 173  THR B N   
2522  C  CA  . THR B 173  ? 1.1467 1.1400 1.1164 -0.1288 0.0077  -0.1967 173  THR B CA  
2523  C  C   . THR B 173  ? 1.2057 1.1945 1.1701 -0.1379 0.0046  -0.2067 173  THR B C   
2524  O  O   . THR B 173  ? 1.2118 1.1862 1.1613 -0.1338 0.0021  -0.2075 173  THR B O   
2525  C  CB  . THR B 173  ? 1.0741 1.0506 1.0399 -0.1328 0.0186  -0.1898 173  THR B CB  
2526  O  OG1 . THR B 173  ? 0.9281 0.9035 0.8939 -0.1221 0.0211  -0.1797 173  THR B OG1 
2527  C  CG2 . THR B 173  ? 1.1276 1.0767 1.0750 -0.1357 0.0235  -0.1893 173  THR B CG2 
2528  N  N   . THR B 174  ? 1.3182 1.3194 1.2946 -0.1504 0.0046  -0.2146 174  THR B N   
2529  C  CA  . THR B 174  ? 1.4124 1.4112 1.3853 -0.1599 0.0013  -0.2250 174  THR B CA  
2530  C  C   . THR B 174  ? 1.3373 1.3493 1.3102 -0.1535 -0.0102 -0.2313 174  THR B C   
2531  O  O   . THR B 174  ? 1.3951 1.3961 1.3560 -0.1547 -0.0136 -0.2364 174  THR B O   
2532  C  CB  . THR B 174  ? 1.3707 1.3824 1.3586 -0.1747 0.0039  -0.2322 174  THR B CB  
2533  O  OG1 . THR B 174  ? 1.1732 1.1769 1.1634 -0.1784 0.0141  -0.2252 174  THR B OG1 
2534  C  CG2 . THR B 174  ? 1.4345 1.4358 1.4156 -0.1864 0.0037  -0.2414 174  THR B CG2 
2535  N  N   . THR B 175  ? 1.2549 1.2900 1.2404 -0.1464 -0.0163 -0.2309 175  THR B N   
2536  C  CA  . THR B 175  ? 1.3646 1.4123 1.3495 -0.1391 -0.0273 -0.2363 175  THR B CA  
2537  C  C   . THR B 175  ? 1.3848 1.4140 1.3509 -0.1266 -0.0287 -0.2302 175  THR B C   
2538  O  O   . THR B 175  ? 1.4324 1.4593 1.3895 -0.1236 -0.0355 -0.2356 175  THR B O   
2539  C  CB  . THR B 175  ? 1.3177 1.3933 1.3198 -0.1337 -0.0328 -0.2367 175  THR B CB  
2540  O  OG1 . THR B 175  ? 1.3614 1.4538 1.3812 -0.1453 -0.0304 -0.2416 175  THR B OG1 
2541  C  CG2 . THR B 175  ? 1.2803 1.3704 1.2825 -0.1271 -0.0445 -0.2435 175  THR B CG2 
2542  N  N   . LEU B 176  ? 1.2308 1.2469 1.1908 -0.1192 -0.0221 -0.2192 176  LEU B N   
2543  C  CA  . LEU B 176  ? 1.1894 1.1874 1.1319 -0.1076 -0.0224 -0.2129 176  LEU B CA  
2544  C  C   . LEU B 176  ? 1.2843 1.2581 1.2097 -0.1123 -0.0194 -0.2152 176  LEU B C   
2545  O  O   . LEU B 176  ? 1.4100 1.3745 1.3218 -0.1056 -0.0238 -0.2162 176  LEU B O   
2546  C  CB  . LEU B 176  ? 1.1338 1.1242 1.0752 -0.0997 -0.0157 -0.2009 176  LEU B CB  
2547  C  CG  . LEU B 176  ? 1.1398 1.1130 1.0648 -0.0872 -0.0152 -0.1935 176  LEU B CG  
2548  C  CD1 . LEU B 176  ? 0.9999 0.9867 0.9261 -0.0763 -0.0240 -0.1943 176  LEU B CD1 
2549  C  CD2 . LEU B 176  ? 1.1775 1.1396 1.1008 -0.0827 -0.0067 -0.1824 176  LEU B CD2 
2550  N  N   . GLY B 177  ? 1.1396 1.1024 1.0647 -0.1235 -0.0119 -0.2159 177  GLY B N   
2551  C  CA  . GLY B 177  ? 1.1887 1.1278 1.0972 -0.1284 -0.0087 -0.2184 177  GLY B CA  
2552  C  C   . GLY B 177  ? 1.2160 1.1607 1.1228 -0.1342 -0.0166 -0.2302 177  GLY B C   
2553  O  O   . GLY B 177  ? 1.2421 1.1696 1.1324 -0.1324 -0.0180 -0.2322 177  GLY B O   
2554  N  N   . ASN B 178  ? 1.2603 1.2293 1.1842 -0.1412 -0.0220 -0.2384 178  ASN B N   
2555  C  CA  . ASN B 178  ? 1.3342 1.3116 1.2581 -0.1464 -0.0306 -0.2503 178  ASN B CA  
2556  C  C   . ASN B 178  ? 1.3477 1.3304 1.2646 -0.1333 -0.0400 -0.2509 178  ASN B C   
2557  O  O   . ASN B 178  ? 1.3781 1.3538 1.2837 -0.1334 -0.0454 -0.2573 178  ASN B O   
2558  C  CB  . ASN B 178  ? 1.3649 1.3687 1.3103 -0.1569 -0.0338 -0.2587 178  ASN B CB  
2559  C  CG  . ASN B 178  ? 1.3896 1.3859 1.3389 -0.1728 -0.0259 -0.2621 178  ASN B CG  
2560  O  OD1 . ASN B 178  ? 1.2768 1.2476 1.2115 -0.1765 -0.0191 -0.2598 178  ASN B OD1 
2561  N  ND2 . ASN B 178  ? 1.3391 1.3574 1.3079 -0.1821 -0.0264 -0.2677 178  ASN B ND2 
2562  N  N   . ALA B 179  ? 1.4696 1.4641 1.3923 -0.1220 -0.0421 -0.2442 179  ALA B N   
2563  C  CA  . ALA B 179  ? 1.4653 1.4635 1.3804 -0.1088 -0.0503 -0.2438 179  ALA B CA  
2564  C  C   . ALA B 179  ? 1.4083 1.3793 1.3011 -0.1008 -0.0471 -0.2377 179  ALA B C   
2565  O  O   . ALA B 179  ? 1.4813 1.4483 1.3624 -0.0945 -0.0536 -0.2411 179  ALA B O   
2566  C  CB  . ALA B 179  ? 1.3496 1.3656 1.2761 -0.0991 -0.0523 -0.2378 179  ALA B CB  
2567  N  N   . LEU B 180  ? 0.9281 0.8806 0.8148 -0.1007 -0.0372 -0.2287 180  LEU B N   
2568  C  CA  . LEU B 180  ? 1.0545 0.9813 0.9207 -0.0932 -0.0334 -0.2227 180  LEU B CA  
2569  C  C   . LEU B 180  ? 1.1884 1.0973 1.0409 -0.1010 -0.0329 -0.2295 180  LEU B C   
2570  O  O   . LEU B 180  ? 1.1952 1.0858 1.0295 -0.0942 -0.0329 -0.2275 180  LEU B O   
2571  C  CB  . LEU B 180  ? 1.0459 0.9595 0.9104 -0.0903 -0.0231 -0.2112 180  LEU B CB  
2572  C  CG  . LEU B 180  ? 0.9507 0.8649 0.8129 -0.0759 -0.0229 -0.2014 180  LEU B CG  
2573  C  CD1 . LEU B 180  ? 0.8666 0.8071 0.7437 -0.0714 -0.0304 -0.2032 180  LEU B CD1 
2574  C  CD2 . LEU B 180  ? 0.8798 0.7835 0.7428 -0.0748 -0.0130 -0.1911 180  LEU B CD2 
2575  N  N   . THR B 181  ? 1.7414 1.6550 1.6020 -0.1152 -0.0321 -0.2374 181  THR B N   
2576  C  CA  . THR B 181  ? 1.7402 1.6388 1.5887 -0.1233 -0.0328 -0.2453 181  THR B CA  
2577  C  C   . THR B 181  ? 1.6913 1.5974 1.5342 -0.1188 -0.0439 -0.2536 181  THR B C   
2578  O  O   . THR B 181  ? 1.7826 1.6701 1.6075 -0.1169 -0.0449 -0.2558 181  THR B O   
2579  C  CB  . THR B 181  ? 1.7276 1.6318 1.5878 -0.1399 -0.0298 -0.2525 181  THR B CB  
2580  O  OG1 . THR B 181  ? 1.8033 1.6980 1.6664 -0.1434 -0.0190 -0.2445 181  THR B OG1 
2581  C  CG2 . THR B 181  ? 1.7201 1.6085 1.5678 -0.1488 -0.0306 -0.2612 181  THR B CG2 
2582  N  N   . ALA B 182  ? 1.2726 1.2054 1.1301 -0.1166 -0.0523 -0.2581 182  ALA B N   
2583  C  CA  . ALA B 182  ? 1.3493 1.2903 1.2012 -0.1102 -0.0633 -0.2650 182  ALA B CA  
2584  C  C   . ALA B 182  ? 1.4236 1.3498 1.2578 -0.0947 -0.0637 -0.2572 182  ALA B C   
2585  O  O   . ALA B 182  ? 1.4948 1.4120 1.3141 -0.0903 -0.0690 -0.2615 182  ALA B O   
2586  C  CB  . ALA B 182  ? 1.3651 1.3380 1.2364 -0.1094 -0.0716 -0.2701 182  ALA B CB  
2587  N  N   . ALA B 183  ? 1.2913 1.2148 1.1270 -0.0863 -0.0579 -0.2457 183  ALA B N   
2588  C  CA  . ALA B 183  ? 1.2391 1.1477 1.0585 -0.0721 -0.0570 -0.2375 183  ALA B CA  
2589  C  C   . ALA B 183  ? 1.2194 1.0985 1.0187 -0.0729 -0.0509 -0.2354 183  ALA B C   
2590  O  O   . ALA B 183  ? 1.2467 1.1126 1.0292 -0.0631 -0.0525 -0.2331 183  ALA B O   
2591  C  CB  . ALA B 183  ? 1.1589 1.0714 0.9857 -0.0644 -0.0516 -0.2261 183  ALA B CB  
2592  N  N   . ARG B 184  ? 1.4882 1.3564 1.2885 -0.0843 -0.0436 -0.2360 184  ARG B N   
2593  C  CA  . ARG B 184  ? 1.5156 1.3551 1.2965 -0.0854 -0.0374 -0.2342 184  ARG B CA  
2594  C  C   . ARG B 184  ? 1.6175 1.4499 1.3849 -0.0870 -0.0443 -0.2440 184  ARG B C   
2595  O  O   . ARG B 184  ? 1.6246 1.4338 1.3724 -0.0828 -0.0415 -0.2419 184  ARG B O   
2596  C  CB  . ARG B 184  ? 1.5390 1.3689 1.3239 -0.0976 -0.0284 -0.2335 184  ARG B CB  
2597  C  CG  . ARG B 184  ? 1.4948 1.3083 1.2744 -0.0926 -0.0179 -0.2213 184  ARG B CG  
2598  C  CD  . ARG B 184  ? 1.5667 1.3720 1.3508 -0.1048 -0.0094 -0.2210 184  ARG B CD  
2599  N  NE  . ARG B 184  ? 1.6128 1.4411 1.4186 -0.1131 -0.0106 -0.2241 184  ARG B NE  
2600  C  CZ  . ARG B 184  ? 1.6443 1.4827 1.4627 -0.1108 -0.0065 -0.2167 184  ARG B CZ  
2601  N  NH1 . ARG B 184  ? 1.7127 1.5410 1.5252 -0.1006 -0.0011 -0.2058 184  ARG B NH1 
2602  N  NH2 . ARG B 184  ? 1.5214 1.3805 1.3589 -0.1189 -0.0078 -0.2205 184  ARG B NH2 
2603  N  N   . ALA B 185  ? 2.1525 2.0046 1.9301 -0.0930 -0.0534 -0.2548 185  ALA B N   
2604  C  CA  . ALA B 185  ? 2.1684 2.0160 1.9336 -0.0934 -0.0613 -0.2645 185  ALA B CA  
2605  C  C   . ALA B 185  ? 2.2050 2.0484 1.9562 -0.0776 -0.0662 -0.2607 185  ALA B C   
2606  O  O   . ALA B 185  ? 2.2234 2.0484 1.9552 -0.0740 -0.0674 -0.2628 185  ALA B O   
2607  C  CB  . ALA B 185  ? 2.1116 1.9842 1.8928 -0.1027 -0.0704 -0.2768 185  ALA B CB  
2608  N  N   . THR B 186  ? 1.5313 1.3907 1.2916 -0.0678 -0.0687 -0.2551 186  THR B N   
2609  C  CA  . THR B 186  ? 1.4536 1.3060 1.2005 -0.0521 -0.0704 -0.2485 186  THR B CA  
2610  C  C   . THR B 186  ? 1.4421 1.2747 1.1810 -0.0468 -0.0592 -0.2360 186  THR B C   
2611  O  O   . THR B 186  ? 1.4381 1.2575 1.1762 -0.0550 -0.0512 -0.2341 186  THR B O   
2612  C  CB  . THR B 186  ? 1.4890 1.3659 1.2483 -0.0440 -0.0774 -0.2478 186  THR B CB  
2613  O  OG1 . THR B 186  ? 1.5625 1.4476 1.3364 -0.0437 -0.0711 -0.2391 186  THR B OG1 
2614  C  CG2 . THR B 186  ? 1.4463 1.3464 1.2185 -0.0514 -0.0874 -0.2601 186  THR B CG2 
2615  N  N   . GLN B 187  ? 1.4359 1.2661 1.1689 -0.0332 -0.0584 -0.2275 187  GLN B N   
2616  C  CA  . GLN B 187  ? 1.4304 1.2456 1.1588 -0.0277 -0.0482 -0.2154 187  GLN B CA  
2617  C  C   . GLN B 187  ? 1.3602 1.1920 1.1047 -0.0228 -0.0467 -0.2079 187  GLN B C   
2618  O  O   . GLN B 187  ? 1.3867 1.2103 1.1268 -0.0137 -0.0411 -0.1977 187  GLN B O   
2619  C  CB  . GLN B 187  ? 1.5002 1.2948 1.2067 -0.0161 -0.0466 -0.2106 187  GLN B CB  
2620  C  CG  . GLN B 187  ? 1.5048 1.2816 1.1937 -0.0198 -0.0481 -0.2178 187  GLN B CG  
2621  C  CD  . GLN B 187  ? 1.5599 1.3184 1.2445 -0.0291 -0.0393 -0.2167 187  GLN B CD  
2622  O  OE1 . GLN B 187  ? 1.6049 1.3557 1.2918 -0.0278 -0.0304 -0.2075 187  GLN B OE1 
2623  N  NE2 . GLN B 187  ? 1.5471 1.2982 1.2251 -0.0384 -0.0419 -0.2262 187  GLN B NE2 
2624  N  N   . GLY B 188  ? 1.0201 0.8754 0.7832 -0.0286 -0.0517 -0.2129 188  GLY B N   
2625  C  CA  . GLY B 188  ? 1.0596 0.9321 0.8380 -0.0239 -0.0514 -0.2069 188  GLY B CA  
2626  C  C   . GLY B 188  ? 1.1142 0.9982 0.8912 -0.0120 -0.0590 -0.2065 188  GLY B C   
2627  O  O   . GLY B 188  ? 1.0889 0.9808 0.8733 -0.0050 -0.0573 -0.1991 188  GLY B O   
2628  N  N   . ALA B 189  ? 1.4444 1.3291 1.2115 -0.0094 -0.0673 -0.2143 189  ALA B N   
2629  C  CA  . ALA B 189  ? 1.3899 1.2835 1.1531 0.0028  -0.0745 -0.2139 189  ALA B CA  
2630  C  C   . ALA B 189  ? 1.3414 1.2618 1.1245 0.0029  -0.0795 -0.2154 189  ALA B C   
2631  O  O   . ALA B 189  ? 1.2963 1.2230 1.0802 0.0135  -0.0811 -0.2099 189  ALA B O   
2632  C  CB  . ALA B 189  ? 1.4574 1.3477 1.2068 0.0045  -0.0831 -0.2232 189  ALA B CB  
2633  N  N   . GLY B 190  ? 1.4025 1.3385 1.2014 -0.0089 -0.0818 -0.2228 190  GLY B N   
2634  C  CA  . GLY B 190  ? 1.4295 1.3911 1.2482 -0.0095 -0.0858 -0.2241 190  GLY B CA  
2635  C  C   . GLY B 190  ? 1.4648 1.4290 1.2954 -0.0098 -0.0778 -0.2146 190  GLY B C   
2636  O  O   . GLY B 190  ? 1.3797 1.3625 1.2237 -0.0065 -0.0805 -0.2133 190  GLY B O   
2637  N  N   . VAL B 191  ? 1.5220 1.4678 1.3476 -0.0132 -0.0680 -0.2081 191  VAL B N   
2638  C  CA  . VAL B 191  ? 1.2982 1.2452 1.1345 -0.0138 -0.0601 -0.1992 191  VAL B CA  
2639  C  C   . VAL B 191  ? 1.3359 1.2784 1.1664 -0.0002 -0.0584 -0.1896 191  VAL B C   
2640  O  O   . VAL B 191  ? 1.4136 1.3385 1.2271 0.0074  -0.0567 -0.1857 191  VAL B O   
2641  C  CB  . VAL B 191  ? 1.3702 1.2987 1.2023 -0.0219 -0.0505 -0.1959 191  VAL B CB  
2642  C  CG1 . VAL B 191  ? 1.2834 1.2125 1.1252 -0.0213 -0.0425 -0.1864 191  VAL B CG1 
2643  C  CG2 . VAL B 191  ? 1.4338 1.3668 1.2723 -0.0361 -0.0517 -0.2055 191  VAL B CG2 
2644  N  N   . ARG B 192  ? 1.1669 1.1251 1.0115 0.0028  -0.0586 -0.1857 192  ARG B N   
2645  C  CA  . ARG B 192  ? 1.1429 1.0985 0.9841 0.0149  -0.0568 -0.1766 192  ARG B CA  
2646  C  C   . ARG B 192  ? 1.1992 1.1608 1.0545 0.0130  -0.0504 -0.1695 192  ARG B C   
2647  O  O   . ARG B 192  ? 1.1919 1.1688 1.0630 0.0051  -0.0511 -0.1730 192  ARG B O   
2648  C  CB  . ARG B 192  ? 1.0236 0.9938 0.8653 0.0237  -0.0660 -0.1799 192  ARG B CB  
2649  C  CG  . ARG B 192  ? 1.2553 1.2167 1.0796 0.0295  -0.0718 -0.1845 192  ARG B CG  
2650  C  CD  . ARG B 192  ? 1.2638 1.2020 1.0702 0.0378  -0.0659 -0.1763 192  ARG B CD  
2651  N  NE  . ARG B 192  ? 1.3394 1.2698 1.1286 0.0453  -0.0717 -0.1800 192  ARG B NE  
2652  C  CZ  . ARG B 192  ? 1.3917 1.3109 1.1689 0.0414  -0.0733 -0.1860 192  ARG B CZ  
2653  N  NH1 . ARG B 192  ? 1.3642 1.2778 1.1443 0.0299  -0.0694 -0.1890 192  ARG B NH1 
2654  N  NH2 . ARG B 192  ? 1.3665 1.2793 1.1278 0.0493  -0.0789 -0.1890 192  ARG B NH2 
2655  N  N   . LEU B 193  ? 1.3865 1.3360 1.2361 0.0203  -0.0442 -0.1597 193  LEU B N   
2656  C  CA  . LEU B 193  ? 1.2274 1.1815 1.0889 0.0203  -0.0384 -0.1522 193  LEU B CA  
2657  C  C   . LEU B 193  ? 1.2232 1.1867 1.0878 0.0308  -0.0413 -0.1479 193  LEU B C   
2658  O  O   . LEU B 193  ? 1.4286 1.3913 1.2838 0.0391  -0.0466 -0.1492 193  LEU B O   
2659  C  CB  . LEU B 193  ? 1.2219 1.1562 1.0760 0.0202  -0.0287 -0.1443 193  LEU B CB  
2660  C  CG  . LEU B 193  ? 1.2907 1.2199 1.1494 0.0089  -0.0230 -0.1455 193  LEU B CG  
2661  C  CD1 . LEU B 193  ? 1.3786 1.2856 1.2254 0.0106  -0.0146 -0.1386 193  LEU B CD1 
2662  C  CD2 . LEU B 193  ? 1.2259 1.1704 1.1028 0.0040  -0.0212 -0.1440 193  LEU B CD2 
2663  N  N   . LEU B 194  ? 0.8281 0.7999 0.7056 0.0306  -0.0378 -0.1427 194  LEU B N   
2664  C  CA  . LEU B 194  ? 0.7378 0.7176 0.6189 0.0401  -0.0398 -0.1380 194  LEU B CA  
2665  C  C   . LEU B 194  ? 0.8248 0.8069 0.7172 0.0386  -0.0332 -0.1308 194  LEU B C   
2666  O  O   . LEU B 194  ? 0.8667 0.8643 0.7739 0.0338  -0.0344 -0.1328 194  LEU B O   
2667  C  CB  . LEU B 194  ? 0.7063 0.7063 0.5951 0.0415  -0.0489 -0.1449 194  LEU B CB  
2668  C  CG  . LEU B 194  ? 0.6346 0.6417 0.5245 0.0524  -0.0518 -0.1409 194  LEU B CG  
2669  C  CD1 . LEU B 194  ? 0.6208 0.6109 0.4935 0.0625  -0.0504 -0.1356 194  LEU B CD1 
2670  C  CD2 . LEU B 194  ? 0.7054 0.7323 0.6020 0.0538  -0.0613 -0.1487 194  LEU B CD2 
2671  N  N   . THR B 195  ? 1.0695 1.0361 0.9547 0.0430  -0.0264 -0.1226 195  THR B N   
2672  C  CA  . THR B 195  ? 0.9687 0.9357 0.8629 0.0427  -0.0201 -0.1152 195  THR B CA  
2673  C  C   . THR B 195  ? 0.9748 0.9416 0.8674 0.0532  -0.0199 -0.1088 195  THR B C   
2674  O  O   . THR B 195  ? 1.0431 1.0102 0.9281 0.0605  -0.0247 -0.1100 195  THR B O   
2675  C  CB  . THR B 195  ? 0.9311 0.8811 0.8195 0.0390  -0.0119 -0.1109 195  THR B CB  
2676  O  OG1 . THR B 195  ? 1.0075 0.9410 0.8809 0.0464  -0.0094 -0.1065 195  THR B OG1 
2677  C  CG2 . THR B 195  ? 0.9903 0.9378 0.8775 0.0290  -0.0121 -0.1176 195  THR B CG2 
2678  N  N   . THR B 196  ? 1.0964 1.0625 0.9960 0.0539  -0.0143 -0.1018 196  THR B N   
2679  C  CA  . THR B 196  ? 1.0881 1.0525 0.9867 0.0629  -0.0128 -0.0951 196  THR B CA  
2680  C  C   . THR B 196  ? 1.0530 0.9985 0.9403 0.0668  -0.0061 -0.0884 196  THR B C   
2681  O  O   . THR B 196  ? 1.0499 0.9833 0.9271 0.0646  -0.0043 -0.0900 196  THR B O   
2682  C  CB  . THR B 196  ? 1.0644 1.0409 0.9783 0.0614  -0.0114 -0.0921 196  THR B CB  
2683  O  OG1 . THR B 196  ? 1.0552 1.0262 0.9737 0.0555  -0.0047 -0.0887 196  THR B OG1 
2684  C  CG2 . THR B 196  ? 0.9792 0.9745 0.9043 0.0573  -0.0177 -0.0990 196  THR B CG2 
2685  N  N   . THR B 197  ? 0.7471 0.6898 0.6361 0.0726  -0.0022 -0.0812 197  THR B N   
2686  C  CA  . THR B 197  ? 0.6927 0.6192 0.5729 0.0763  0.0047  -0.0745 197  THR B CA  
2687  C  C   . THR B 197  ? 0.6152 0.5366 0.4994 0.0693  0.0105  -0.0729 197  THR B C   
2688  O  O   . THR B 197  ? 0.8042 0.7316 0.6997 0.0667  0.0133  -0.0698 197  THR B O   
2689  C  CB  . THR B 197  ? 0.6448 0.5713 0.5278 0.0834  0.0072  -0.0676 197  THR B CB  
2690  O  OG1 . THR B 197  ? 0.5931 0.5232 0.4711 0.0902  0.0020  -0.0691 197  THR B OG1 
2691  C  CG2 . THR B 197  ? 0.5518 0.4625 0.4265 0.0870  0.0146  -0.0609 197  THR B CG2 
2692  N  N   . ILE B 198  ? 0.7502 0.6599 0.6243 0.0664  0.0122  -0.0750 198  ILE B N   
2693  C  CA  . ILE B 198  ? 0.8007 0.7043 0.6765 0.0596  0.0174  -0.0743 198  ILE B CA  
2694  C  C   . ILE B 198  ? 0.8373 0.7271 0.7074 0.0640  0.0248  -0.0667 198  ILE B C   
2695  O  O   . ILE B 198  ? 1.0272 0.9053 0.8848 0.0696  0.0263  -0.0648 198  ILE B O   
2696  C  CB  . ILE B 198  ? 0.8021 0.7001 0.6701 0.0537  0.0154  -0.0811 198  ILE B CB  
2697  C  CG1 . ILE B 198  ? 0.7641 0.6778 0.6401 0.0485  0.0081  -0.0889 198  ILE B CG1 
2698  C  CG2 . ILE B 198  ? 0.8651 0.7538 0.7326 0.0476  0.0215  -0.0797 198  ILE B CG2 
2699  C  CD1 . ILE B 198  ? 0.8320 0.7594 0.7241 0.0428  0.0086  -0.0891 198  ILE B CD1 
2700  N  N   . THR B 199  ? 0.8867 0.7782 0.7657 0.0617  0.0296  -0.0623 199  THR B N   
2701  C  CA  . THR B 199  ? 0.9763 0.8559 0.8513 0.0650  0.0368  -0.0556 199  THR B CA  
2702  C  C   . THR B 199  ? 1.0365 0.9109 0.9132 0.0590  0.0415  -0.0550 199  THR B C   
2703  O  O   . THR B 199  ? 0.9999 0.8640 0.8725 0.0616  0.0475  -0.0498 199  THR B O   
2704  C  CB  . THR B 199  ? 0.9746 0.8601 0.8582 0.0702  0.0388  -0.0493 199  THR B CB  
2705  O  OG1 . THR B 199  ? 0.9687 0.8666 0.8664 0.0657  0.0381  -0.0495 199  THR B OG1 
2706  C  CG2 . THR B 199  ? 1.0146 0.9044 0.8959 0.0764  0.0346  -0.0496 199  THR B CG2 
2707  N  N   . SER B 200  ? 1.1650 1.0461 1.0473 0.0512  0.0391  -0.0602 200  SER B N   
2708  C  CA  . SER B 200  ? 1.1384 1.0139 1.0217 0.0453  0.0436  -0.0598 200  SER B CA  
2709  C  C   . SER B 200  ? 1.2411 1.0994 1.1096 0.0447  0.0467  -0.0608 200  SER B C   
2710  O  O   . SER B 200  ? 1.3246 1.1802 1.1857 0.0426  0.0429  -0.0665 200  SER B O   
2711  C  CB  . SER B 200  ? 1.1463 1.0333 1.0390 0.0369  0.0404  -0.0654 200  SER B CB  
2712  O  OG  . SER B 200  ? 1.2244 1.1033 1.1148 0.0306  0.0447  -0.0661 200  SER B OG  
2713  N  N   . PRO B 201  ? 1.1343 0.9808 0.9981 0.0467  0.0532  -0.0556 201  PRO B N   
2714  C  CA  . PRO B 201  ? 1.1429 0.9722 0.9918 0.0464  0.0564  -0.0565 201  PRO B CA  
2715  C  C   . PRO B 201  ? 1.1678 0.9938 1.0139 0.0375  0.0554  -0.0629 201  PRO B C   
2716  O  O   . PRO B 201  ? 1.3042 1.1193 1.1381 0.0363  0.0547  -0.0667 201  PRO B O   
2717  C  CB  . PRO B 201  ? 1.1299 0.9503 0.9776 0.0503  0.0637  -0.0494 201  PRO B CB  
2718  C  CG  . PRO B 201  ? 1.0974 0.9296 0.9569 0.0548  0.0636  -0.0445 201  PRO B CG  
2719  C  CD  . PRO B 201  ? 1.1071 0.9554 0.9782 0.0502  0.0579  -0.0486 201  PRO B CD  
2720  N  N   . SER B 202  ? 0.9778 0.8125 0.8346 0.0309  0.0554  -0.0642 202  SER B N   
2721  C  CA  . SER B 202  ? 1.0614 0.8930 0.9161 0.0217  0.0551  -0.0702 202  SER B CA  
2722  C  C   . SER B 202  ? 1.1374 0.9767 0.9921 0.0181  0.0479  -0.0781 202  SER B C   
2723  O  O   . SER B 202  ? 1.2916 1.1221 1.1369 0.0137  0.0471  -0.0833 202  SER B O   
2724  C  CB  . SER B 202  ? 1.1076 0.9474 0.9742 0.0160  0.0571  -0.0695 202  SER B CB  
2725  O  OG  . SER B 202  ? 1.2021 1.0354 1.0688 0.0198  0.0632  -0.0625 202  SER B OG  
2726  N  N   . LEU B 203  ? 1.1273 0.9831 0.9921 0.0201  0.0426  -0.0792 203  LEU B N   
2727  C  CA  . LEU B 203  ? 1.1671 1.0316 1.0323 0.0176  0.0353  -0.0866 203  LEU B CA  
2728  C  C   . LEU B 203  ? 1.2648 1.1186 1.1154 0.0230  0.0333  -0.0880 203  LEU B C   
2729  O  O   . LEU B 203  ? 1.3049 1.1574 1.1497 0.0192  0.0292  -0.0949 203  LEU B O   
2730  C  CB  . LEU B 203  ? 1.0362 0.9200 0.9147 0.0199  0.0303  -0.0868 203  LEU B CB  
2731  C  CG  . LEU B 203  ? 0.9643 0.8608 0.8463 0.0168  0.0225  -0.0949 203  LEU B CG  
2732  C  CD1 . LEU B 203  ? 0.9417 0.8401 0.8267 0.0059  0.0221  -0.1015 203  LEU B CD1 
2733  C  CD2 . LEU B 203  ? 0.9464 0.8612 0.8413 0.0199  0.0182  -0.0943 203  LEU B CD2 
2734  N  N   . ALA B 204  ? 1.0253 0.8715 0.8699 0.0318  0.0363  -0.0815 204  ALA B N   
2735  C  CA  . ALA B 204  ? 1.0324 0.8675 0.8623 0.0376  0.0351  -0.0821 204  ALA B CA  
2736  C  C   . ALA B 204  ? 1.1389 0.9567 0.9554 0.0340  0.0383  -0.0845 204  ALA B C   
2737  O  O   . ALA B 204  ? 1.2371 1.0484 1.0425 0.0344  0.0350  -0.0893 204  ALA B O   
2738  C  CB  . ALA B 204  ? 0.9904 0.8211 0.8177 0.0474  0.0386  -0.0742 204  ALA B CB  
2739  N  N   . ALA B 205  ? 1.0701 0.8797 0.8868 0.0307  0.0447  -0.0813 205  ALA B N   
2740  C  CA  . ALA B 205  ? 1.1124 0.9044 0.9159 0.0273  0.0482  -0.0834 205  ALA B CA  
2741  C  C   . ALA B 205  ? 1.1282 0.9230 0.9322 0.0173  0.0441  -0.0923 205  ALA B C   
2742  O  O   . ALA B 205  ? 1.3268 1.1095 1.1181 0.0151  0.0435  -0.0968 205  ALA B O   
2743  C  CB  . ALA B 205  ? 0.9988 0.7814 0.8023 0.0269  0.0561  -0.0775 205  ALA B CB  
2744  N  N   . GLN B 206  ? 1.2090 1.0197 1.0276 0.0110  0.0414  -0.0951 206  GLN B N   
2745  C  CA  . GLN B 206  ? 1.2872 1.1025 1.1081 0.0011  0.0376  -0.1038 206  GLN B CA  
2746  C  C   . GLN B 206  ? 1.2944 1.1172 1.1129 0.0022  0.0294  -0.1105 206  GLN B C   
2747  O  O   . GLN B 206  ? 1.3013 1.1207 1.1143 -0.0041 0.0265  -0.1180 206  GLN B O   
2748  C  CB  . GLN B 206  ? 1.3356 1.1663 1.1732 -0.0056 0.0376  -0.1046 206  GLN B CB  
2749  C  CG  . GLN B 206  ? 1.2644 1.0860 1.1026 -0.0097 0.0453  -0.1006 206  GLN B CG  
2750  C  CD  . GLN B 206  ? 1.2846 1.1202 1.1378 -0.0176 0.0451  -0.1027 206  GLN B CD  
2751  O  OE1 . GLN B 206  ? 1.2452 1.0987 1.1095 -0.0194 0.0393  -0.1066 206  GLN B OE1 
2752  N  NE2 . GLN B 206  ? 1.3446 1.1721 1.1977 -0.0220 0.0516  -0.1000 206  GLN B NE2 
2753  N  N   . ILE B 207  ? 0.8403 0.6732 0.6625 0.0102  0.0256  -0.1081 207  ILE B N   
2754  C  CA  . ILE B 207  ? 0.8108 0.6497 0.6289 0.0129  0.0178  -0.1138 207  ILE B CA  
2755  C  C   . ILE B 207  ? 0.7999 0.6204 0.5991 0.0168  0.0185  -0.1146 207  ILE B C   
2756  O  O   . ILE B 207  ? 0.8597 0.6794 0.6521 0.0144  0.0131  -0.1221 207  ILE B O   
2757  C  CB  . ILE B 207  ? 0.6911 0.5436 0.5168 0.0211  0.0143  -0.1103 207  ILE B CB  
2758  C  CG1 . ILE B 207  ? 0.6298 0.5025 0.4738 0.0162  0.0115  -0.1120 207  ILE B CG1 
2759  C  CG2 . ILE B 207  ? 0.7175 0.5715 0.5346 0.0267  0.0074  -0.1144 207  ILE B CG2 
2760  C  CD1 . ILE B 207  ? 0.5863 0.4714 0.4382 0.0240  0.0091  -0.1078 207  ILE B CD1 
2761  N  N   . GLU B 208  ? 1.4499 1.2555 1.2402 0.0231  0.0251  -0.1072 208  GLU B N   
2762  C  CA  . GLU B 208  ? 1.5822 1.3692 1.3539 0.0270  0.0266  -0.1076 208  GLU B CA  
2763  C  C   . GLU B 208  ? 1.6079 1.3834 1.3720 0.0181  0.0278  -0.1135 208  GLU B C   
2764  O  O   . GLU B 208  ? 1.7471 1.5135 1.4983 0.0180  0.0249  -0.1188 208  GLU B O   
2765  C  CB  . GLU B 208  ? 1.6679 1.4424 1.4332 0.0352  0.0341  -0.0983 208  GLU B CB  
2766  C  CG  . GLU B 208  ? 1.7624 1.5191 1.5086 0.0415  0.0355  -0.0978 208  GLU B CG  
2767  C  CD  . GLU B 208  ? 2.1060 1.8498 1.8463 0.0483  0.0438  -0.0889 208  GLU B CD  
2768  O  OE1 . GLU B 208  ? 2.1866 1.9334 1.9366 0.0469  0.0487  -0.0839 208  GLU B OE1 
2769  O  OE2 . GLU B 208  ? 2.2154 1.9462 1.9412 0.0552  0.0455  -0.0871 208  GLU B OE2 
2770  N  N   . GLN B 209  ? 1.2031 0.9783 0.9746 0.0106  0.0323  -0.1128 209  GLN B N   
2771  C  CA  . GLN B 209  ? 1.2625 1.0267 1.0274 0.0013  0.0338  -0.1186 209  GLN B CA  
2772  C  C   . GLN B 209  ? 1.2514 1.0270 1.0205 -0.0063 0.0259  -0.1289 209  GLN B C   
2773  O  O   . GLN B 209  ? 1.3056 1.0709 1.0639 -0.0109 0.0243  -0.1353 209  GLN B O   
2774  C  CB  . GLN B 209  ? 1.3353 1.0978 1.1078 -0.0049 0.0403  -0.1154 209  GLN B CB  
2775  C  CG  . GLN B 209  ? 1.4057 1.1539 1.1700 -0.0142 0.0434  -0.1202 209  GLN B CG  
2776  C  CD  . GLN B 209  ? 1.4761 1.2216 1.2468 -0.0196 0.0502  -0.1166 209  GLN B CD  
2777  O  OE1 . GLN B 209  ? 1.3193 1.0729 1.1000 -0.0158 0.0528  -0.1100 209  GLN B OE1 
2778  N  NE2 . GLN B 209  ? 1.6117 1.3453 1.3763 -0.0285 0.0532  -0.1208 209  GLN B NE2 
2779  N  N   . PHE B 210  ? 1.0081 0.8052 0.7928 -0.0076 0.0207  -0.1308 210  PHE B N   
2780  C  CA  . PHE B 210  ? 1.0371 0.8475 0.8270 -0.0137 0.0126  -0.1405 210  PHE B CA  
2781  C  C   . PHE B 210  ? 1.0927 0.8997 0.8703 -0.0074 0.0064  -0.1444 210  PHE B C   
2782  O  O   . PHE B 210  ? 1.1583 0.9665 0.9323 -0.0130 0.0009  -0.1533 210  PHE B O   
2783  C  CB  . PHE B 210  ? 0.9460 0.7803 0.7550 -0.0148 0.0086  -0.1409 210  PHE B CB  
2784  C  CG  . PHE B 210  ? 0.9392 0.7896 0.7552 -0.0204 0.0000  -0.1508 210  PHE B CG  
2785  C  CD1 . PHE B 210  ? 0.9959 0.8483 0.8160 -0.0325 -0.0005 -0.1584 210  PHE B CD1 
2786  C  CD2 . PHE B 210  ? 0.9418 0.8055 0.7601 -0.0134 -0.0076 -0.1527 210  PHE B CD2 
2787  C  CE1 . PHE B 210  ? 0.9738 0.8424 0.8013 -0.0377 -0.0085 -0.1678 210  PHE B CE1 
2788  C  CE2 . PHE B 210  ? 0.9387 0.8182 0.7637 -0.0179 -0.0158 -0.1620 210  PHE B CE2 
2789  C  CZ  . PHE B 210  ? 0.9735 0.8561 0.8036 -0.0302 -0.0164 -0.1697 210  PHE B CZ  
2790  N  N   . LEU B 211  ? 1.2353 1.0376 1.0059 0.0041  0.0072  -0.1380 211  LEU B N   
2791  C  CA  . LEU B 211  ? 1.2572 1.0544 1.0143 0.0110  0.0020  -0.1409 211  LEU B CA  
2792  C  C   . LEU B 211  ? 1.2970 1.0719 1.0356 0.0098  0.0049  -0.1430 211  LEU B C   
2793  O  O   . LEU B 211  ? 1.3422 1.1136 1.0703 0.0103  -0.0007 -0.1496 211  LEU B O   
2794  C  CB  . LEU B 211  ? 1.1907 0.9885 0.9455 0.0234  0.0029  -0.1330 211  LEU B CB  
2795  C  CG  . LEU B 211  ? 1.0490 0.8658 0.8123 0.0281  -0.0048 -0.1348 211  LEU B CG  
2796  C  CD1 . LEU B 211  ? 0.9473 0.7845 0.7305 0.0210  -0.0072 -0.1373 211  LEU B CD1 
2797  C  CD2 . LEU B 211  ? 1.0514 0.8661 0.8118 0.0399  -0.0022 -0.1261 211  LEU B CD2 
2798  N  N   . GLN B 212  ? 1.9785 1.7379 1.7122 0.0086  0.0135  -0.1376 212  GLN B N   
2799  C  CA  . GLN B 212  ? 2.0284 1.7661 1.7447 0.0066  0.0167  -0.1399 212  GLN B CA  
2800  C  C   . GLN B 212  ? 2.0160 1.7545 1.7333 -0.0057 0.0133  -0.1499 212  GLN B C   
2801  O  O   . GLN B 212  ? 2.0699 1.7956 1.7728 -0.0073 0.0114  -0.1556 212  GLN B O   
2802  C  CB  . GLN B 212  ? 2.0133 1.7351 1.7248 0.0084  0.0268  -0.1317 212  GLN B CB  
2803  C  CG  . GLN B 212  ? 2.0990 1.8188 1.8091 0.0202  0.0308  -0.1218 212  GLN B CG  
2804  C  CD  . GLN B 212  ? 2.1922 1.8949 1.8829 0.0288  0.0320  -0.1202 212  GLN B CD  
2805  O  OE1 . GLN B 212  ? 2.2682 1.9535 1.9447 0.0265  0.0343  -0.1231 212  GLN B OE1 
2806  N  NE2 . GLN B 212  ? 2.1669 1.8739 1.8565 0.0389  0.0308  -0.1156 212  GLN B NE2 
2807  N  N   . ALA B 213  ? 1.6871 1.4404 1.4212 -0.0145 0.0126  -0.1524 213  ALA B N   
2808  C  CA  . ALA B 213  ? 1.7668 1.5228 1.5037 -0.0269 0.0094  -0.1622 213  ALA B CA  
2809  C  C   . ALA B 213  ? 1.7297 1.4997 1.4683 -0.0275 -0.0010 -0.1713 213  ALA B C   
2810  O  O   . ALA B 213  ? 1.7624 1.5281 1.4952 -0.0347 -0.0046 -0.1801 213  ALA B O   
2811  C  CB  . ALA B 213  ? 1.6921 1.4602 1.4466 -0.0359 0.0124  -0.1618 213  ALA B CB  
2812  N  N   . TYR B 214  ? 1.4671 1.2535 1.2135 -0.0198 -0.0062 -0.1694 214  TYR B N   
2813  C  CA  . TYR B 214  ? 1.4934 1.2943 1.2416 -0.0186 -0.0165 -0.1773 214  TYR B CA  
2814  C  C   . TYR B 214  ? 1.5462 1.3424 1.2827 -0.0049 -0.0187 -0.1729 214  TYR B C   
2815  O  O   . TYR B 214  ? 1.4304 1.2378 1.1745 0.0027  -0.0195 -0.1673 214  TYR B O   
2816  C  CB  . TYR B 214  ? 1.3757 1.2028 1.1452 -0.0227 -0.0211 -0.1799 214  TYR B CB  
2817  C  CG  . TYR B 214  ? 1.4471 1.2811 1.2279 -0.0370 -0.0206 -0.1867 214  TYR B CG  
2818  C  CD1 . TYR B 214  ? 1.6600 1.5012 1.4418 -0.0447 -0.0277 -0.1980 214  TYR B CD1 
2819  C  CD2 . TYR B 214  ? 1.3678 1.2008 1.1578 -0.0427 -0.0129 -0.1818 214  TYR B CD2 
2820  C  CE1 . TYR B 214  ? 1.6901 1.5376 1.4826 -0.0583 -0.0267 -0.2042 214  TYR B CE1 
2821  C  CE2 . TYR B 214  ? 1.3606 1.1990 1.1604 -0.0558 -0.0118 -0.1876 214  TYR B CE2 
2822  C  CZ  . TYR B 214  ? 1.5295 1.3752 1.3307 -0.0638 -0.0185 -0.1988 214  TYR B CZ  
2823  O  OH  . TYR B 214  ? 1.5245 1.3757 1.3358 -0.0774 -0.0170 -0.2048 214  TYR B OH  
2824  N  N   . PRO B 215  ? 1.3716 1.1508 1.0891 -0.0012 -0.0196 -0.1752 215  PRO B N   
2825  C  CA  . PRO B 215  ? 1.3243 1.0960 1.0291 0.0123  -0.0200 -0.1697 215  PRO B CA  
2826  C  C   . PRO B 215  ? 1.2715 1.0612 0.9815 0.0190  -0.0286 -0.1719 215  PRO B C   
2827  O  O   . PRO B 215  ? 1.2978 1.0880 1.0061 0.0295  -0.0272 -0.1645 215  PRO B O   
2828  C  CB  . PRO B 215  ? 1.3885 1.1395 1.0723 0.0127  -0.0202 -0.1739 215  PRO B CB  
2829  C  CG  . PRO B 215  ? 1.3479 1.0899 1.0325 0.0007  -0.0157 -0.1774 215  PRO B CG  
2830  C  CD  . PRO B 215  ? 1.3241 1.0875 1.0299 -0.0091 -0.0187 -0.1816 215  PRO B CD  
2831  N  N   . GLN B 216  ? 1.7403 1.5447 1.4566 0.0134  -0.0374 -0.1818 216  GLN B N   
2832  C  CA  . GLN B 216  ? 1.8200 1.6410 1.5397 0.0204  -0.0462 -0.1846 216  GLN B CA  
2833  C  C   . GLN B 216  ? 1.7597 1.6019 1.4995 0.0206  -0.0469 -0.1813 216  GLN B C   
2834  O  O   . GLN B 216  ? 1.7452 1.6035 1.4902 0.0252  -0.0546 -0.1844 216  GLN B O   
2835  C  CB  . GLN B 216  ? 1.8907 1.7197 1.6086 0.0150  -0.0560 -0.1971 216  GLN B CB  
2836  C  CG  . GLN B 216  ? 1.8612 1.6699 1.5582 0.0154  -0.0566 -0.2015 216  GLN B CG  
2837  C  CD  . GLN B 216  ? 1.9894 1.7857 1.6683 0.0294  -0.0570 -0.1966 216  GLN B CD  
2838  O  OE1 . GLN B 216  ? 2.0794 1.8864 1.7606 0.0385  -0.0609 -0.1939 216  GLN B OE1 
2839  N  NE2 . GLN B 216  ? 1.9777 1.7509 1.6379 0.0313  -0.0526 -0.1953 216  GLN B NE2 
2840  N  N   . ALA B 217  ? 1.5365 1.3788 1.2872 0.0162  -0.0393 -0.1751 217  ALA B N   
2841  C  CA  . ALA B 217  ? 1.4311 1.2923 1.2000 0.0169  -0.0395 -0.1714 217  ALA B CA  
2842  C  C   . ALA B 217  ? 1.4017 1.2599 1.1670 0.0294  -0.0368 -0.1617 217  ALA B C   
2843  O  O   . ALA B 217  ? 1.5226 1.3625 1.2735 0.0359  -0.0317 -0.1559 217  ALA B O   
2844  C  CB  . ALA B 217  ? 1.4017 1.2644 1.1835 0.0071  -0.0327 -0.1690 217  ALA B CB  
2845  N  N   . ARG B 218  ? 1.2432 1.1195 1.0217 0.0327  -0.0400 -0.1601 218  ARG B N   
2846  C  CA  . ARG B 218  ? 1.3278 1.2032 1.1047 0.0440  -0.0378 -0.1514 218  ARG B CA  
2847  C  C   . ARG B 218  ? 1.1947 1.0819 0.9892 0.0419  -0.0338 -0.1459 218  ARG B C   
2848  O  O   . ARG B 218  ? 1.1418 1.0448 0.9513 0.0341  -0.0364 -0.1503 218  ARG B O   
2849  C  CB  . ARG B 218  ? 1.3321 1.2165 1.1044 0.0528  -0.0463 -0.1546 218  ARG B CB  
2850  C  CG  . ARG B 218  ? 1.2910 1.1649 1.0455 0.0555  -0.0512 -0.1606 218  ARG B CG  
2851  C  CD  . ARG B 218  ? 1.3330 1.1865 1.0692 0.0655  -0.0462 -0.1534 218  ARG B CD  
2852  N  NE  . ARG B 218  ? 1.6351 1.4775 1.3532 0.0684  -0.0506 -0.1591 218  ARG B NE  
2853  C  CZ  . ARG B 218  ? 1.5571 1.3794 1.2606 0.0676  -0.0459 -0.1584 218  ARG B CZ  
2854  N  NH1 . ARG B 218  ? 1.5064 1.3172 1.2109 0.0642  -0.0366 -0.1521 218  ARG B NH1 
2855  N  NH2 . ARG B 218  ? 1.4259 1.2394 1.1130 0.0706  -0.0508 -0.1642 218  ARG B NH2 
2856  N  N   . TRP B 219  ? 1.3385 1.2181 1.1311 0.0489  -0.0275 -0.1362 219  TRP B N   
2857  C  CA  . TRP B 219  ? 1.3242 1.2128 1.1321 0.0475  -0.0232 -0.1302 219  TRP B CA  
2858  C  C   . TRP B 219  ? 1.3414 1.2479 1.1592 0.0528  -0.0288 -0.1302 219  TRP B C   
2859  O  O   . TRP B 219  ? 1.3692 1.2926 1.2024 0.0474  -0.0315 -0.1333 219  TRP B O   
2860  C  CB  . TRP B 219  ? 1.3022 1.1755 1.1045 0.0524  -0.0142 -0.1203 219  TRP B CB  
2861  C  CG  . TRP B 219  ? 1.2178 1.0975 1.0347 0.0495  -0.0088 -0.1145 219  TRP B CG  
2862  C  CD1 . TRP B 219  ? 1.1602 1.0570 0.9938 0.0435  -0.0110 -0.1169 219  TRP B CD1 
2863  C  CD2 . TRP B 219  ? 1.1691 1.0383 0.9851 0.0527  -0.0004 -0.1055 219  TRP B CD2 
2864  N  NE1 . TRP B 219  ? 1.1884 1.0855 1.0309 0.0429  -0.0046 -0.1100 219  TRP B NE1 
2865  C  CE2 . TRP B 219  ? 1.1534 1.0341 0.9856 0.0484  0.0018  -0.1030 219  TRP B CE2 
2866  C  CE3 . TRP B 219  ? 1.1646 1.0164 0.9679 0.0588  0.0054  -0.0994 219  TRP B CE3 
2867  C  CZ2 . TRP B 219  ? 1.2043 1.0795 1.0401 0.0501  0.0092  -0.0949 219  TRP B CZ2 
2868  C  CZ3 . TRP B 219  ? 1.2170 1.0642 1.0247 0.0604  0.0129  -0.0914 219  TRP B CZ3 
2869  C  CH2 . TRP B 219  ? 1.2496 1.1086 1.0735 0.0561  0.0145  -0.0893 219  TRP B CH2 
2870  N  N   . TYR B 220  ? 1.0669 0.9693 0.8755 0.0637  -0.0302 -0.1265 220  TYR B N   
2871  C  CA  . TYR B 220  ? 1.0140 0.9309 0.8292 0.0701  -0.0353 -0.1261 220  TYR B CA  
2872  C  C   . TYR B 220  ? 0.9460 0.8740 0.7779 0.0682  -0.0320 -0.1212 220  TYR B C   
2873  O  O   . TYR B 220  ? 0.9201 0.8638 0.7662 0.0615  -0.0349 -0.1256 220  TYR B O   
2874  C  CB  . TYR B 220  ? 0.9744 0.9063 0.7925 0.0681  -0.0453 -0.1360 220  TYR B CB  
2875  C  CG  . TYR B 220  ? 1.0034 0.9264 0.8045 0.0719  -0.0502 -0.1412 220  TYR B CG  
2876  C  CD1 . TYR B 220  ? 1.0745 0.9799 0.8586 0.0808  -0.0471 -0.1360 220  TYR B CD1 
2877  C  CD2 . TYR B 220  ? 1.0875 1.0200 0.8898 0.0667  -0.0580 -0.1516 220  TYR B CD2 
2878  C  CE1 . TYR B 220  ? 1.2348 1.1315 1.0025 0.0847  -0.0517 -0.1408 220  TYR B CE1 
2879  C  CE2 . TYR B 220  ? 1.2052 1.1296 0.9917 0.0703  -0.0630 -0.1567 220  TYR B CE2 
2880  C  CZ  . TYR B 220  ? 1.2968 1.2030 1.0656 0.0795  -0.0598 -0.1512 220  TYR B CZ  
2881  O  OH  . TYR B 220  ? 1.3610 1.2586 1.1131 0.0835  -0.0647 -0.1563 220  TYR B OH  
2882  N  N   . GLN B 221  ? 1.0240 0.9443 0.8547 0.0740  -0.0258 -0.1122 221  GLN B N   
2883  C  CA  . GLN B 221  ? 0.9627 0.8925 0.8080 0.0733  -0.0227 -0.1072 221  GLN B CA  
2884  C  C   . GLN B 221  ? 0.8977 0.8347 0.7439 0.0825  -0.0261 -0.1046 221  GLN B C   
2885  O  O   . GLN B 221  ? 0.8991 0.8265 0.7323 0.0910  -0.0264 -0.1021 221  GLN B O   
2886  C  CB  . GLN B 221  ? 0.9412 0.8583 0.7860 0.0728  -0.0133 -0.0991 221  GLN B CB  
2887  C  CG  . GLN B 221  ? 1.0990 0.9975 0.9275 0.0797  -0.0092 -0.0944 221  GLN B CG  
2888  C  CD  . GLN B 221  ? 1.1375 1.0242 0.9659 0.0785  -0.0001 -0.0873 221  GLN B CD  
2889  O  OE1 . GLN B 221  ? 1.2224 1.0933 1.0381 0.0820  0.0042  -0.0842 221  GLN B OE1 
2890  N  NE2 . GLN B 221  ? 0.8453 0.7401 0.6880 0.0738  0.0029  -0.0847 221  GLN B NE2 
2891  N  N   . TYR B 222  ? 0.9415 0.8948 0.8025 0.0809  -0.0284 -0.1051 222  TYR B N   
2892  C  CA  . TYR B 222  ? 0.9146 0.8753 0.7773 0.0893  -0.0316 -0.1028 222  TYR B CA  
2893  C  C   . TYR B 222  ? 0.9630 0.9371 0.8427 0.0865  -0.0304 -0.1006 222  TYR B C   
2894  O  O   . TYR B 222  ? 1.0248 1.0085 0.9160 0.0779  -0.0306 -0.1041 222  TYR B O   
2895  C  CB  . TYR B 222  ? 0.9449 0.9148 0.8032 0.0930  -0.0410 -0.1102 222  TYR B CB  
2896  C  CG  . TYR B 222  ? 0.9246 0.9044 0.7864 0.1010  -0.0448 -0.1087 222  TYR B CG  
2897  C  CD1 . TYR B 222  ? 0.9889 0.9582 0.8386 0.1114  -0.0438 -0.1035 222  TYR B CD1 
2898  C  CD2 . TYR B 222  ? 0.9127 0.9116 0.7893 0.0983  -0.0492 -0.1123 222  TYR B CD2 
2899  C  CE1 . TYR B 222  ? 0.9726 0.9495 0.8244 0.1188  -0.0470 -0.1020 222  TYR B CE1 
2900  C  CE2 . TYR B 222  ? 0.8829 0.8900 0.7619 0.1060  -0.0526 -0.1108 222  TYR B CE2 
2901  C  CZ  . TYR B 222  ? 0.9322 0.9280 0.7985 0.1162  -0.0515 -0.1057 222  TYR B CZ  
2902  O  OH  . TYR B 222  ? 0.9653 0.9682 0.8332 0.1240  -0.0547 -0.1042 222  TYR B OH  
2903  N  N   . GLU B 223  ? 1.0298 1.0039 0.9104 0.0937  -0.0290 -0.0948 223  GLU B N   
2904  C  CA  . GLU B 223  ? 0.9611 0.9481 0.8562 0.0930  -0.0289 -0.0928 223  GLU B CA  
2905  C  C   . GLU B 223  ? 1.0410 1.0281 0.9318 0.1032  -0.0308 -0.0894 223  GLU B C   
2906  O  O   . GLU B 223  ? 1.0284 1.0019 0.9061 0.1100  -0.0287 -0.0856 223  GLU B O   
2907  C  CB  . GLU B 223  ? 1.0105 0.9930 0.9134 0.0883  -0.0210 -0.0868 223  GLU B CB  
2908  C  CG  . GLU B 223  ? 1.0584 1.0253 0.9532 0.0939  -0.0144 -0.0786 223  GLU B CG  
2909  C  CD  . GLU B 223  ? 1.1314 1.0970 1.0359 0.0900  -0.0076 -0.0730 223  GLU B CD  
2910  O  OE1 . GLU B 223  ? 1.0064 0.9825 0.9229 0.0832  -0.0080 -0.0753 223  GLU B OE1 
2911  O  OE2 . GLU B 223  ? 1.2798 1.2341 1.1797 0.0939  -0.0019 -0.0664 223  GLU B OE2 
2912  N  N   . PRO B 224  ? 0.9909 0.9927 0.8920 0.1047  -0.0346 -0.0907 224  PRO B N   
2913  C  CA  . PRO B 224  ? 0.8977 0.8992 0.7935 0.1148  -0.0370 -0.0881 224  PRO B CA  
2914  C  C   . PRO B 224  ? 0.9117 0.8999 0.8031 0.1197  -0.0300 -0.0792 224  PRO B C   
2915  O  O   . PRO B 224  ? 0.9086 0.8888 0.7889 0.1283  -0.0304 -0.0764 224  PRO B O   
2916  C  CB  . PRO B 224  ? 0.8327 0.8531 0.7424 0.1139  -0.0416 -0.0912 224  PRO B CB  
2917  C  CG  . PRO B 224  ? 0.8802 0.9076 0.8036 0.1036  -0.0385 -0.0922 224  PRO B CG  
2918  C  CD  . PRO B 224  ? 0.9782 0.9969 0.8954 0.0976  -0.0367 -0.0946 224  PRO B CD  
2919  N  N   . ILE B 225  ? 0.9650 0.9505 0.8645 0.1145  -0.0235 -0.0746 225  ILE B N   
2920  C  CA  . ILE B 225  ? 0.9435 0.9174 0.8404 0.1182  -0.0166 -0.0664 225  ILE B CA  
2921  C  C   . ILE B 225  ? 0.9906 0.9503 0.8800 0.1154  -0.0109 -0.0640 225  ILE B C   
2922  O  O   . ILE B 225  ? 1.0563 1.0159 0.9529 0.1085  -0.0069 -0.0630 225  ILE B O   
2923  C  CB  . ILE B 225  ? 0.8364 0.8181 0.7480 0.1152  -0.0137 -0.0631 225  ILE B CB  
2924  C  CG1 . ILE B 225  ? 0.8782 0.8746 0.7970 0.1178  -0.0197 -0.0663 225  ILE B CG1 
2925  C  CG2 . ILE B 225  ? 0.7609 0.7312 0.6703 0.1189  -0.0068 -0.0550 225  ILE B CG2 
2926  C  CD1 . ILE B 225  ? 0.9149 0.9072 0.8240 0.1278  -0.0222 -0.0646 225  ILE B CD1 
2927  N  N   . ASN B 226  ? 0.9748 0.9222 0.8491 0.1211  -0.0106 -0.0631 226  ASN B N   
2928  C  CA  . ASN B 226  ? 0.9931 0.9263 0.8582 0.1196  -0.0056 -0.0613 226  ASN B CA  
2929  C  C   . ASN B 226  ? 0.9850 0.9040 0.8408 0.1266  0.0003  -0.0540 226  ASN B C   
2930  O  O   . ASN B 226  ? 1.0087 0.9286 0.8658 0.1318  0.0008  -0.0504 226  ASN B O   
2931  C  CB  . ASN B 226  ? 0.9785 0.9095 0.8331 0.1191  -0.0107 -0.0678 226  ASN B CB  
2932  C  CG  . ASN B 226  ? 0.9955 0.9304 0.8424 0.1264  -0.0177 -0.0713 226  ASN B CG  
2933  O  OD1 . ASN B 226  ? 1.2145 1.1489 1.0599 0.1333  -0.0176 -0.0676 226  ASN B OD1 
2934  N  ND2 . ASN B 226  ? 0.9542 0.8926 0.7958 0.1251  -0.0239 -0.0786 226  ASN B ND2 
2935  N  N   . ARG B 227  ? 1.0934 0.9988 0.9395 0.1265  0.0050  -0.0520 227  ARG B N   
2936  C  CA  . ARG B 227  ? 1.2118 1.1029 1.0485 0.1327  0.0114  -0.0452 227  ARG B CA  
2937  C  C   . ARG B 227  ? 1.3160 1.1948 1.1346 0.1376  0.0105  -0.0467 227  ARG B C   
2938  O  O   . ARG B 227  ? 1.2647 1.1303 1.0752 0.1388  0.0166  -0.0430 227  ARG B O   
2939  C  CB  . ARG B 227  ? 1.1651 1.0509 1.0080 0.1286  0.0194  -0.0399 227  ARG B CB  
2940  C  CG  . ARG B 227  ? 1.0897 0.9876 0.9500 0.1222  0.0198  -0.0396 227  ARG B CG  
2941  C  CD  . ARG B 227  ? 1.0367 0.9288 0.9023 0.1210  0.0280  -0.0330 227  ARG B CD  
2942  N  NE  . ARG B 227  ? 1.0121 0.8993 0.8761 0.1271  0.0318  -0.0272 227  ARG B NE  
2943  C  CZ  . ARG B 227  ? 1.0306 0.9132 0.8990 0.1272  0.0387  -0.0212 227  ARG B CZ  
2944  N  NH1 . ARG B 227  ? 1.1359 1.0180 1.0102 0.1222  0.0427  -0.0199 227  ARG B NH1 
2945  N  NH2 . ARG B 227  ? 0.9412 0.8197 0.8082 0.1324  0.0419  -0.0164 227  ARG B NH2 
2946  N  N   . ASP B 228  ? 1.4583 1.3413 1.2702 0.1408  0.0030  -0.0523 228  ASP B N   
2947  C  CA  . ASP B 228  ? 1.4079 1.2796 1.2020 0.1456  0.0013  -0.0545 228  ASP B CA  
2948  C  C   . ASP B 228  ? 1.3080 1.1656 1.0896 0.1544  0.0065  -0.0480 228  ASP B C   
2949  O  O   . ASP B 228  ? 1.1747 1.0185 0.9425 0.1573  0.0097  -0.0466 228  ASP B O   
2950  C  CB  . ASP B 228  ? 1.4441 1.3251 1.2348 0.1473  -0.0085 -0.0622 228  ASP B CB  
2951  C  CG  . ASP B 228  ? 1.4598 1.3562 1.2641 0.1384  -0.0135 -0.0687 228  ASP B CG  
2952  O  OD1 . ASP B 228  ? 1.4214 1.3191 1.2356 0.1309  -0.0091 -0.0674 228  ASP B OD1 
2953  O  OD2 . ASP B 228  ? 1.4785 1.3858 1.2836 0.1391  -0.0216 -0.0752 228  ASP B OD2 
2954  N  N   . ASN B 229  ? 1.3877 1.2482 1.1736 0.1586  0.0076  -0.0439 229  ASN B N   
2955  C  CA  . ASN B 229  ? 1.3680 1.2149 1.1423 0.1667  0.0130  -0.0375 229  ASN B CA  
2956  C  C   . ASN B 229  ? 1.3295 1.1661 1.1049 0.1648  0.0228  -0.0310 229  ASN B C   
2957  O  O   . ASN B 229  ? 1.3716 1.1941 1.1342 0.1705  0.0280  -0.0268 229  ASN B O   
2958  C  CB  . ASN B 229  ? 1.3411 1.1934 1.1202 0.1711  0.0119  -0.0349 229  ASN B CB  
2959  C  CG  . ASN B 229  ? 1.3853 1.2452 1.1596 0.1756  0.0027  -0.0406 229  ASN B CG  
2960  O  OD1 . ASN B 229  ? 1.5585 1.4168 1.3222 0.1774  -0.0024 -0.0458 229  ASN B OD1 
2961  N  ND2 . ASN B 229  ? 1.4024 1.2709 1.1843 0.1777  0.0004  -0.0399 229  ASN B ND2 
2962  N  N   . VAL B 230  ? 0.8549 0.6984 0.6452 0.1572  0.0255  -0.0302 230  VAL B N   
2963  C  CA  . VAL B 230  ? 0.8648 0.7000 0.6574 0.1555  0.0345  -0.0242 230  VAL B CA  
2964  C  C   . VAL B 230  ? 0.9264 0.7500 0.7067 0.1554  0.0369  -0.0252 230  VAL B C   
2965  O  O   . VAL B 230  ? 0.9610 0.7719 0.7327 0.1594  0.0437  -0.0203 230  VAL B O   
2966  C  CB  . VAL B 230  ? 0.7551 0.6011 0.5663 0.1478  0.0362  -0.0234 230  VAL B CB  
2967  C  CG1 . VAL B 230  ? 0.7447 0.5830 0.5586 0.1467  0.0452  -0.0173 230  VAL B CG1 
2968  C  CG2 . VAL B 230  ? 0.7978 0.6550 0.6204 0.1481  0.0336  -0.0227 230  VAL B CG2 
2969  N  N   . VAL B 231  ? 1.0946 0.9223 0.8741 0.1509  0.0315  -0.0318 231  VAL B N   
2970  C  CA  . VAL B 231  ? 1.0629 0.8791 0.8303 0.1505  0.0333  -0.0333 231  VAL B CA  
2971  C  C   . VAL B 231  ? 1.1530 0.9579 0.9012 0.1586  0.0318  -0.0340 231  VAL B C   
2972  O  O   . VAL B 231  ? 1.2100 1.0012 0.9457 0.1613  0.0363  -0.0321 231  VAL B O   
2973  C  CB  . VAL B 231  ? 0.9759 0.7994 0.7481 0.1427  0.0281  -0.0404 231  VAL B CB  
2974  C  CG1 . VAL B 231  ? 1.0405 0.8741 0.8120 0.1429  0.0184  -0.0475 231  VAL B CG1 
2975  C  CG2 . VAL B 231  ? 1.1092 0.9198 0.8694 0.1417  0.0308  -0.0417 231  VAL B CG2 
2976  N  N   . ALA B 232  ? 1.1309 0.9410 0.8758 0.1631  0.0256  -0.0365 232  ALA B N   
2977  C  CA  . ALA B 232  ? 1.1239 0.9229 0.8497 0.1717  0.0241  -0.0368 232  ALA B CA  
2978  C  C   . ALA B 232  ? 1.0884 0.8746 0.8072 0.1782  0.0328  -0.0286 232  ALA B C   
2979  O  O   . ALA B 232  ? 1.1747 0.9466 0.8772 0.1834  0.0361  -0.0270 232  ALA B O   
2980  C  CB  . ALA B 232  ? 1.1288 0.9370 0.8533 0.1755  0.0153  -0.0414 232  ALA B CB  
2981  N  N   . GLY B 233  ? 1.0399 0.8309 0.7706 0.1777  0.0369  -0.0234 233  GLY B N   
2982  C  CA  . GLY B 233  ? 1.0792 0.8590 0.8053 0.1826  0.0458  -0.0155 233  GLY B CA  
2983  C  C   . GLY B 233  ? 1.0907 0.8618 0.8163 0.1801  0.0539  -0.0119 233  GLY B C   
2984  O  O   . GLY B 233  ? 1.1767 0.9348 0.8917 0.1854  0.0608  -0.0069 233  GLY B O   
2985  N  N   . ALA B 234  ? 0.8662 0.6443 0.6029 0.1724  0.0535  -0.0142 234  ALA B N   
2986  C  CA  . ALA B 234  ? 0.9358 0.7059 0.6717 0.1703  0.0607  -0.0112 234  ALA B CA  
2987  C  C   . ALA B 234  ? 1.0244 0.7814 0.7416 0.1737  0.0605  -0.0136 234  ALA B C   
2988  O  O   . ALA B 234  ? 0.9815 0.7264 0.6907 0.1767  0.0679  -0.0093 234  ALA B O   
2989  C  CB  . ALA B 234  ? 0.9185 0.6989 0.6701 0.1615  0.0599  -0.0132 234  ALA B CB  
2990  N  N   . ARG B 235  ? 1.2368 0.9961 0.9468 0.1734  0.0521  -0.0207 235  ARG B N   
2991  C  CA  . ARG B 235  ? 1.2312 0.9779 0.9225 0.1769  0.0511  -0.0237 235  ARG B CA  
2992  C  C   . ARG B 235  ? 1.2504 0.9848 0.9250 0.1867  0.0538  -0.0201 235  ARG B C   
2993  O  O   . ARG B 235  ? 1.2602 0.9806 0.9197 0.1908  0.0577  -0.0188 235  ARG B O   
2994  C  CB  . ARG B 235  ? 1.0912 0.8449 0.7802 0.1737  0.0408  -0.0327 235  ARG B CB  
2995  C  CG  . ARG B 235  ? 1.1219 0.8837 0.8229 0.1640  0.0389  -0.0368 235  ARG B CG  
2996  C  CD  . ARG B 235  ? 1.0946 0.8657 0.7958 0.1604  0.0287  -0.0457 235  ARG B CD  
2997  N  NE  . ARG B 235  ? 1.1606 0.9382 0.8725 0.1508  0.0274  -0.0497 235  ARG B NE  
2998  C  CZ  . ARG B 235  ? 1.1814 0.9691 0.8977 0.1453  0.0195  -0.0574 235  ARG B CZ  
2999  N  NH1 . ARG B 235  ? 1.0714 0.8652 0.7832 0.1485  0.0115  -0.0625 235  ARG B NH1 
3000  N  NH2 . ARG B 235  ? 1.1999 0.9920 0.9254 0.1365  0.0198  -0.0602 235  ARG B NH2 
3001  N  N   . LEU B 236  ? 1.1795 0.9185 0.8561 0.1907  0.0519  -0.0183 236  LEU B N   
3002  C  CA  . LEU B 236  ? 1.1112 0.8380 0.7716 0.2002  0.0547  -0.0147 236  LEU B CA  
3003  C  C   . LEU B 236  ? 1.1054 0.8218 0.7648 0.2027  0.0663  -0.0063 236  LEU B C   
3004  O  O   . LEU B 236  ? 1.1672 0.8691 0.8099 0.2095  0.0709  -0.0034 236  LEU B O   
3005  C  CB  . LEU B 236  ? 1.0258 0.7600 0.6887 0.2038  0.0498  -0.0150 236  LEU B CB  
3006  C  CG  . LEU B 236  ? 1.0183 0.7400 0.6639 0.2140  0.0521  -0.0113 236  LEU B CG  
3007  C  CD1 . LEU B 236  ? 1.2197 0.9314 0.8444 0.2195  0.0478  -0.0158 236  LEU B CD1 
3008  C  CD2 . LEU B 236  ? 1.0439 0.7735 0.6940 0.2169  0.0477  -0.0113 236  LEU B CD2 
3009  N  N   . ALA B 237  ? 1.3255 1.0494 1.0027 0.1972  0.0712  -0.0025 237  ALA B N   
3010  C  CA  . ALA B 237  ? 1.3533 1.0700 1.0325 0.1991  0.0820  0.0053  237  ALA B CA  
3011  C  C   . ALA B 237  ? 1.3435 1.0527 1.0199 0.1972  0.0879  0.0066  237  ALA B C   
3012  O  O   . ALA B 237  ? 1.3704 1.0663 1.0344 0.2026  0.0949  0.0107  237  ALA B O   
3013  C  CB  . ALA B 237  ? 1.2040 0.9326 0.9037 0.1944  0.0842  0.0087  237  ALA B CB  
3014  N  N   . PHE B 238  ? 1.2758 0.9930 0.9631 0.1899  0.0855  0.0033  238  PHE B N   
3015  C  CA  . PHE B 238  ? 1.2717 0.9827 0.9581 0.1878  0.0912  0.0047  238  PHE B CA  
3016  C  C   . PHE B 238  ? 1.2891 0.9923 0.9610 0.1879  0.0871  -0.0010 238  PHE B C   
3017  O  O   . PHE B 238  ? 1.2630 0.9580 0.9302 0.1877  0.0922  0.0003  238  PHE B O   
3018  C  CB  . PHE B 238  ? 1.3149 1.0379 1.0215 0.1800  0.0922  0.0052  238  PHE B CB  
3019  C  CG  . PHE B 238  ? 1.1788 0.9102 0.9007 0.1792  0.0961  0.0104  238  PHE B CG  
3020  C  CD1 . PHE B 238  ? 1.3160 1.0413 1.0385 0.1825  0.1056  0.0173  238  PHE B CD1 
3021  C  CD2 . PHE B 238  ? 1.0980 0.8432 0.8337 0.1750  0.0903  0.0082  238  PHE B CD2 
3022  C  CE1 . PHE B 238  ? 1.3135 1.0464 1.0502 0.1814  0.1090  0.0217  238  PHE B CE1 
3023  C  CE2 . PHE B 238  ? 1.1536 0.9059 0.9030 0.1742  0.0937  0.0127  238  PHE B CE2 
3024  C  CZ  . PHE B 238  ? 1.2160 0.9621 0.9659 0.1772  0.1030  0.0194  238  PHE B CZ  
3025  N  N   . GLY B 239  ? 1.2646 0.9701 0.9294 0.1884  0.0781  -0.0073 239  GLY B N   
3026  C  CA  . GLY B 239  ? 1.3194 1.0184 0.9714 0.1877  0.0735  -0.0134 239  GLY B CA  
3027  C  C   . GLY B 239  ? 1.3092 1.0154 0.9716 0.1789  0.0705  -0.0179 239  GLY B C   
3028  O  O   . GLY B 239  ? 1.2675 0.9671 0.9197 0.1774  0.0679  -0.0227 239  GLY B O   
3029  N  N   . ARG B 240  ? 1.7166 1.4356 1.3984 0.1729  0.0711  -0.0164 240  ARG B N   
3030  C  CA  . ARG B 240  ? 1.7159 1.4418 1.4082 0.1645  0.0689  -0.0201 240  ARG B CA  
3031  C  C   . ARG B 240  ? 1.7147 1.4575 1.4267 0.1592  0.0657  -0.0204 240  ARG B C   
3032  O  O   . ARG B 240  ? 1.6627 1.4111 1.3801 0.1622  0.0656  -0.0174 240  ARG B O   
3033  C  CB  . ARG B 240  ? 1.6596 1.3775 1.3524 0.1634  0.0774  -0.0159 240  ARG B CB  
3034  C  CG  . ARG B 240  ? 1.6994 1.4191 1.4022 0.1657  0.0855  -0.0079 240  ARG B CG  
3035  C  CD  . ARG B 240  ? 1.7715 1.4886 1.4801 0.1628  0.0923  -0.0048 240  ARG B CD  
3036  N  NE  . ARG B 240  ? 1.7829 1.5075 1.5008 0.1549  0.0882  -0.0092 240  ARG B NE  
3037  C  CZ  . ARG B 240  ? 1.8072 1.5299 1.5297 0.1517  0.0926  -0.0078 240  ARG B CZ  
3038  N  NH1 . ARG B 240  ? 1.7715 1.4862 1.4911 0.1557  0.1009  -0.0022 240  ARG B NH1 
3039  N  NH2 . ARG B 240  ? 1.8165 1.5455 1.5465 0.1444  0.0886  -0.0121 240  ARG B NH2 
3040  N  N   . ASP B 241  ? 1.5097 1.2601 1.2321 0.1514  0.0631  -0.0239 241  ASP B N   
3041  C  CA  . ASP B 241  ? 1.3687 1.1350 1.1098 0.1458  0.0603  -0.0245 241  ASP B CA  
3042  C  C   . ASP B 241  ? 1.3003 1.0685 1.0535 0.1445  0.0679  -0.0179 241  ASP B C   
3043  O  O   . ASP B 241  ? 1.3598 1.1216 1.1119 0.1426  0.0728  -0.0164 241  ASP B O   
3044  C  CB  . ASP B 241  ? 1.3804 1.1541 1.1265 0.1380  0.0539  -0.0316 241  ASP B CB  
3045  C  CG  . ASP B 241  ? 1.4516 1.2247 1.1867 0.1389  0.0459  -0.0388 241  ASP B CG  
3046  O  OD1 . ASP B 241  ? 1.3899 1.1624 1.1180 0.1451  0.0433  -0.0385 241  ASP B OD1 
3047  O  OD2 . ASP B 241  ? 1.4914 1.2645 1.2245 0.1333  0.0423  -0.0447 241  ASP B OD2 
3048  N  N   . VAL B 242  ? 1.2233 1.0000 0.9877 0.1456  0.0688  -0.0142 242  VAL B N   
3049  C  CA  . VAL B 242  ? 1.2123 0.9929 0.9898 0.1442  0.0753  -0.0084 242  VAL B CA  
3050  C  C   . VAL B 242  ? 1.0656 0.8618 0.8599 0.1401  0.0713  -0.0091 242  VAL B C   
3051  O  O   . VAL B 242  ? 1.0451 0.8479 0.8399 0.1403  0.0648  -0.0127 242  VAL B O   
3052  C  CB  . VAL B 242  ? 1.1850 0.9575 0.9580 0.1509  0.0828  -0.0015 242  VAL B CB  
3053  C  CG1 . VAL B 242  ? 1.2463 1.0034 1.0031 0.1550  0.0875  -0.0004 242  VAL B CG1 
3054  C  CG2 . VAL B 242  ? 1.2136 0.9877 0.9836 0.1556  0.0802  -0.0008 242  VAL B CG2 
3055  N  N   . THR B 243  ? 1.2409 1.0428 1.0487 0.1368  0.0753  -0.0057 243  THR B N   
3056  C  CA  . THR B 243  ? 1.2082 1.0243 1.0324 0.1330  0.0726  -0.0058 243  THR B CA  
3057  C  C   . THR B 243  ? 1.1546 0.9717 0.9862 0.1361  0.0785  0.0008  243  THR B C   
3058  O  O   . THR B 243  ? 1.1684 0.9809 1.0018 0.1368  0.0852  0.0051  243  THR B O   
3059  C  CB  . THR B 243  ? 1.2183 1.0411 1.0526 0.1260  0.0717  -0.0080 243  THR B CB  
3060  O  OG1 . THR B 243  ? 1.2039 1.0284 1.0338 0.1222  0.0653  -0.0147 243  THR B OG1 
3061  C  CG2 . THR B 243  ? 1.2154 1.0515 1.0669 0.1229  0.0708  -0.0065 243  THR B CG2 
3062  N  N   . THR B 244  ? 1.0457 0.8688 0.8817 0.1379  0.0760  0.0014  244  THR B N   
3063  C  CA  . THR B 244  ? 1.0574 0.8808 0.8995 0.1407  0.0812  0.0071  244  THR B CA  
3064  C  C   . THR B 244  ? 1.0426 0.8789 0.9028 0.1360  0.0805  0.0079  244  THR B C   
3065  O  O   . THR B 244  ? 0.9729 0.8188 0.8394 0.1332  0.0744  0.0043  244  THR B O   
3066  C  CB  . THR B 244  ? 1.1066 0.9269 0.9410 0.1461  0.0795  0.0077  244  THR B CB  
3067  O  OG1 . THR B 244  ? 0.9917 0.8000 0.8084 0.1508  0.0795  0.0065  244  THR B OG1 
3068  C  CG2 . THR B 244  ? 1.1031 0.9217 0.9426 0.1489  0.0859  0.0139  244  THR B CG2 
3069  N  N   . ARG B 245  ? 0.8956 0.7322 0.7639 0.1352  0.0868  0.0124  245  ARG B N   
3070  C  CA  . ARG B 245  ? 0.8158 0.6638 0.7009 0.1312  0.0868  0.0136  245  ARG B CA  
3071  C  C   . ARG B 245  ? 0.8499 0.6980 0.7408 0.1339  0.0918  0.0187  245  ARG B C   
3072  O  O   . ARG B 245  ? 0.9052 0.7443 0.7897 0.1378  0.0979  0.0226  245  ARG B O   
3073  C  CB  . ARG B 245  ? 0.9181 0.7677 0.8091 0.1276  0.0894  0.0140  245  ARG B CB  
3074  C  CG  . ARG B 245  ? 0.9133 0.7748 0.8209 0.1235  0.0888  0.0147  245  ARG B CG  
3075  C  CD  . ARG B 245  ? 0.9288 0.7911 0.8406 0.1205  0.0911  0.0149  245  ARG B CD  
3076  N  NE  . ARG B 245  ? 0.9873 0.8423 0.8963 0.1238  0.0984  0.0194  245  ARG B NE  
3077  C  CZ  . ARG B 245  ? 0.9451 0.8038 0.8638 0.1248  0.1030  0.0236  245  ARG B CZ  
3078  N  NH1 . ARG B 245  ? 0.9053 0.7742 0.8367 0.1227  0.1012  0.0241  245  ARG B NH1 
3079  N  NH2 . ARG B 245  ? 0.9615 0.8138 0.8772 0.1279  0.1096  0.0273  245  ARG B NH2 
3080  N  N   . TYR B 246  ? 0.9788 0.8367 0.8816 0.1317  0.0894  0.0187  246  TYR B N   
3081  C  CA  . TYR B 246  ? 0.9509 0.8095 0.8601 0.1335  0.0935  0.0230  246  TYR B CA  
3082  C  C   . TYR B 246  ? 0.9190 0.7870 0.8444 0.1295  0.0955  0.0247  246  TYR B C   
3083  O  O   . TYR B 246  ? 0.8838 0.7613 0.8179 0.1255  0.0908  0.0219  246  TYR B O   
3084  C  CB  . TYR B 246  ? 0.9046 0.7657 0.8128 0.1350  0.0891  0.0216  246  TYR B CB  
3085  C  CG  . TYR B 246  ? 0.9149 0.7678 0.8072 0.1393  0.0861  0.0195  246  TYR B CG  
3086  C  CD1 . TYR B 246  ? 0.9821 0.8226 0.8619 0.1444  0.0911  0.0226  246  TYR B CD1 
3087  C  CD2 . TYR B 246  ? 0.8825 0.7404 0.7721 0.1384  0.0783  0.0142  246  TYR B CD2 
3088  C  CE1 . TYR B 246  ? 1.0494 0.8822 0.9138 0.1489  0.0882  0.0205  246  TYR B CE1 
3089  C  CE2 . TYR B 246  ? 0.9798 0.8309 0.8548 0.1427  0.0751  0.0119  246  TYR B CE2 
3090  C  CZ  . TYR B 246  ? 1.0558 0.8942 0.9180 0.1480  0.0799  0.0151  246  TYR B CZ  
3091  O  OH  . TYR B 246  ? 1.0879 0.9191 0.9347 0.1527  0.0766  0.0127  246  TYR B OH  
3092  N  N   . ASP B 247  ? 1.0271 0.8926 0.9565 0.1308  0.1025  0.0293  247  ASP B N   
3093  C  CA  . ASP B 247  ? 0.9247 0.7991 0.8696 0.1277  0.1047  0.0312  247  ASP B CA  
3094  C  C   . ASP B 247  ? 1.0003 0.8775 0.9525 0.1281  0.1063  0.0335  247  ASP B C   
3095  O  O   . ASP B 247  ? 1.0597 0.9326 1.0125 0.1301  0.1126  0.0375  247  ASP B O   
3096  C  CB  . ASP B 247  ? 1.0897 0.9607 1.0352 0.1287  0.1112  0.0343  247  ASP B CB  
3097  C  CG  . ASP B 247  ? 1.1349 1.0160 1.0960 0.1256  0.1125  0.0354  247  ASP B CG  
3098  O  OD1 . ASP B 247  ? 1.1835 1.0739 1.1540 0.1222  0.1078  0.0333  247  ASP B OD1 
3099  O  OD2 . ASP B 247  ? 1.1212 1.0012 1.0851 0.1268  0.1182  0.0384  247  ASP B OD2 
3100  N  N   . LEU B 248  ? 0.8117 0.6959 0.7693 0.1260  0.1006  0.0310  248  LEU B N   
3101  C  CA  . LEU B 248  ? 0.7439 0.6299 0.7072 0.1263  0.1014  0.0327  248  LEU B CA  
3102  C  C   . LEU B 248  ? 0.8254 0.7179 0.8033 0.1238  0.1056  0.0354  248  LEU B C   
3103  O  O   . LEU B 248  ? 0.8900 0.7822 0.8723 0.1240  0.1079  0.0375  248  LEU B O   
3104  C  CB  . LEU B 248  ? 0.6952 0.5877 0.6607 0.1248  0.0940  0.0290  248  LEU B CB  
3105  C  CG  . LEU B 248  ? 0.6337 0.5222 0.5864 0.1270  0.0888  0.0255  248  LEU B CG  
3106  C  CD1 . LEU B 248  ? 0.7685 0.6647 0.7251 0.1258  0.0819  0.0220  248  LEU B CD1 
3107  C  CD2 . LEU B 248  ? 0.7555 0.6317 0.6942 0.1323  0.0921  0.0276  248  LEU B CD2 
3108  N  N   . SER B 249  ? 0.9264 0.8243 0.9114 0.1216  0.1066  0.0355  249  SER B N   
3109  C  CA  . SER B 249  ? 0.9596 0.8646 0.9588 0.1194  0.1100  0.0377  249  SER B CA  
3110  C  C   . SER B 249  ? 0.9705 0.8698 0.9696 0.1217  0.1179  0.0420  249  SER B C   
3111  O  O   . SER B 249  ? 0.9450 0.8501 0.9563 0.1199  0.1208  0.0438  249  SER B O   
3112  C  CB  . SER B 249  ? 0.9042 0.8153 0.9092 0.1175  0.1094  0.0368  249  SER B CB  
3113  O  OG  . SER B 249  ? 0.9058 0.8102 0.9042 0.1200  0.1145  0.0389  249  SER B OG  
3114  N  N   . ALA B 250  ? 1.1353 1.0236 1.1212 0.1254  0.1214  0.0436  250  ALA B N   
3115  C  CA  . ALA B 250  ? 1.1738 1.0558 1.1583 0.1278  0.1294  0.0478  250  ALA B CA  
3116  C  C   . ALA B 250  ? 1.2119 1.0834 1.1845 0.1310  0.1306  0.0489  250  ALA B C   
3117  O  O   . ALA B 250  ? 1.3148 1.1772 1.2797 0.1342  0.1370  0.0520  250  ALA B O   
3118  C  CB  . ALA B 250  ? 1.2546 1.1319 1.2336 0.1302  0.1341  0.0495  250  ALA B CB  
3119  N  N   . ALA B 251  ? 0.8292 0.7017 0.7997 0.1305  0.1247  0.0464  251  ALA B N   
3120  C  CA  . ALA B 251  ? 0.8094 0.6720 0.7678 0.1340  0.1248  0.0470  251  ALA B CA  
3121  C  C   . ALA B 251  ? 0.9035 0.7690 0.8704 0.1322  0.1253  0.0480  251  ALA B C   
3122  O  O   . ALA B 251  ? 0.8939 0.7670 0.8673 0.1298  0.1193  0.0452  251  ALA B O   
3123  C  CB  . ALA B 251  ? 0.7492 0.6102 0.6968 0.1356  0.1173  0.0430  251  ALA B CB  
3124  N  N   . GLN B 252  ? 1.1275 0.9865 1.0942 0.1333  0.1327  0.0520  252  GLN B N   
3125  C  CA  . GLN B 252  ? 1.0037 0.8632 0.9769 0.1316  0.1339  0.0531  252  GLN B CA  
3126  C  C   . GLN B 252  ? 0.9670 0.8178 0.9274 0.1352  0.1310  0.0524  252  GLN B C   
3127  O  O   . GLN B 252  ? 0.9836 0.8365 0.9486 0.1338  0.1285  0.0516  252  GLN B O   
3128  C  CB  . GLN B 252  ? 1.0334 0.8894 1.0117 0.1310  0.1434  0.0575  252  GLN B CB  
3129  C  CG  . GLN B 252  ? 1.2141 1.0790 1.2052 0.1282  0.1467  0.0583  252  GLN B CG  
3130  C  CD  . GLN B 252  ? 1.3435 1.2221 1.3522 0.1230  0.1431  0.0563  252  GLN B CD  
3131  O  OE1 . GLN B 252  ? 1.4306 1.3185 1.4487 0.1211  0.1422  0.0554  252  GLN B OE1 
3132  N  NE2 . GLN B 252  ? 1.1466 1.0261 1.1594 0.1211  0.1410  0.0555  252  GLN B NE2 
3133  N  N   . VAL B 253  ? 1.1013 0.9421 1.0452 0.1401  0.1310  0.0526  253  VAL B N   
3134  C  CA  . VAL B 253  ? 1.1356 0.9677 1.0656 0.1445  0.1279  0.0518  253  VAL B CA  
3135  C  C   . VAL B 253  ? 1.1235 0.9560 1.0433 0.1470  0.1211  0.0481  253  VAL B C   
3136  O  O   . VAL B 253  ? 1.1852 1.0137 1.0980 0.1488  0.1231  0.0485  253  VAL B O   
3137  C  CB  . VAL B 253  ? 1.1976 1.0148 1.1154 0.1489  0.1356  0.0562  253  VAL B CB  
3138  C  CG1 . VAL B 253  ? 1.2106 1.0183 1.1113 0.1546  0.1316  0.0551  253  VAL B CG1 
3139  C  CG2 . VAL B 253  ? 1.1848 1.0014 1.1126 0.1459  0.1419  0.0594  253  VAL B CG2 
3140  N  N   . VAL B 254  ? 0.9423 0.7799 0.8616 0.1471  0.1131  0.0443  254  VAL B N   
3141  C  CA  . VAL B 254  ? 1.0015 0.8407 0.9122 0.1490  0.1060  0.0401  254  VAL B CA  
3142  C  C   . VAL B 254  ? 0.9991 0.8320 0.8973 0.1541  0.1019  0.0388  254  VAL B C   
3143  O  O   . VAL B 254  ? 0.9568 0.7914 0.8589 0.1540  0.1004  0.0388  254  VAL B O   
3144  C  CB  . VAL B 254  ? 1.0131 0.8666 0.9363 0.1440  0.0996  0.0360  254  VAL B CB  
3145  C  CG1 . VAL B 254  ? 0.9183 0.7798 0.8531 0.1412  0.0969  0.0352  254  VAL B CG1 
3146  C  CG2 . VAL B 254  ? 1.0001 0.8555 0.9147 0.1455  0.0923  0.0314  254  VAL B CG2 
3147  N  N   . VAL B 255  ? 0.8504 0.6757 0.7330 0.1589  0.1003  0.0377  255  VAL B N   
3148  C  CA  . VAL B 255  ? 0.8643 0.6832 0.7331 0.1648  0.0962  0.0363  255  VAL B CA  
3149  C  C   . VAL B 255  ? 0.8889 0.7142 0.7534 0.1653  0.0875  0.0307  255  VAL B C   
3150  O  O   . VAL B 255  ? 0.9384 0.7631 0.7992 0.1647  0.0873  0.0294  255  VAL B O   
3151  C  CB  . VAL B 255  ? 0.8501 0.6526 0.7022 0.1709  0.1024  0.0402  255  VAL B CB  
3152  C  CG1 . VAL B 255  ? 0.9154 0.7112 0.7524 0.1777  0.0976  0.0387  255  VAL B CG1 
3153  C  CG2 . VAL B 255  ? 0.8455 0.6421 0.7028 0.1697  0.1116  0.0457  255  VAL B CG2 
3154  N  N   . SER B 256  ? 0.9126 0.7440 0.7777 0.1665  0.0804  0.0273  256  SER B N   
3155  C  CA  . SER B 256  ? 0.8576 0.6965 0.7199 0.1668  0.0718  0.0215  256  SER B CA  
3156  C  C   . SER B 256  ? 0.9876 0.8194 0.8337 0.1743  0.0678  0.0201  256  SER B C   
3157  O  O   . SER B 256  ? 1.0428 0.8715 0.8865 0.1778  0.0676  0.0215  256  SER B O   
3158  C  CB  . SER B 256  ? 0.8338 0.6879 0.7113 0.1618  0.0661  0.0180  256  SER B CB  
3159  O  OG  . SER B 256  ? 0.7609 0.6217 0.6345 0.1633  0.0576  0.0126  256  SER B OG  
3160  N  N   . LEU B 257  ? 0.8832 0.7120 0.7178 0.1771  0.0646  0.0173  257  LEU B N   
3161  C  CA  . LEU B 257  ? 0.8012 0.6241 0.6197 0.1846  0.0600  0.0152  257  LEU B CA  
3162  C  C   . LEU B 257  ? 0.8080 0.6443 0.6303 0.1831  0.0501  0.0083  257  LEU B C   
3163  O  O   . LEU B 257  ? 0.7892 0.6274 0.6069 0.1824  0.0464  0.0045  257  LEU B O   
3164  C  CB  . LEU B 257  ? 0.8078 0.6172 0.6097 0.1891  0.0636  0.0168  257  LEU B CB  
3165  C  CG  . LEU B 257  ? 0.8174 0.6138 0.6159 0.1902  0.0741  0.0237  257  LEU B CG  
3166  C  CD1 . LEU B 257  ? 0.7416 0.5274 0.5271 0.1929  0.0778  0.0247  257  LEU B CD1 
3167  C  CD2 . LEU B 257  ? 1.0320 0.8189 0.8224 0.1961  0.0768  0.0272  257  LEU B CD2 
3168  N  N   . ASP B 258  ? 1.1082 0.9539 0.9391 0.1825  0.0458  0.0067  258  ASP B N   
3169  C  CA  . ASP B 258  ? 1.1712 1.0316 1.0086 0.1804  0.0368  0.0003  258  ASP B CA  
3170  C  C   . ASP B 258  ? 1.2508 1.1207 1.0997 0.1723  0.0362  -0.0024 258  ASP B C   
3171  O  O   . ASP B 258  ? 1.2852 1.1625 1.1336 0.1708  0.0301  -0.0078 258  ASP B O   
3172  C  CB  . ASP B 258  ? 1.1860 1.0446 1.0088 0.1872  0.0302  -0.0038 258  ASP B CB  
3173  C  CG  . ASP B 258  ? 1.3318 1.2059 1.1614 0.1864  0.0210  -0.0101 258  ASP B CG  
3174  O  OD1 . ASP B 258  ? 1.3635 1.2492 1.2089 0.1806  0.0201  -0.0110 258  ASP B OD1 
3175  O  OD2 . ASP B 258  ? 1.3558 1.2309 1.1751 0.1918  0.0147  -0.0141 258  ASP B OD2 
3176  N  N   . ALA B 259  ? 1.0557 0.9250 0.9147 0.1672  0.0426  0.0014  259  ALA B N   
3177  C  CA  . ALA B 259  ? 1.0264 0.9029 0.8958 0.1598  0.0430  -0.0002 259  ALA B CA  
3178  C  C   . ALA B 259  ? 1.0438 0.9324 0.9304 0.1545  0.0420  -0.0005 259  ALA B C   
3179  O  O   . ALA B 259  ? 0.9641 0.8507 0.8576 0.1532  0.0472  0.0038  259  ALA B O   
3180  C  CB  . ALA B 259  ? 1.0855 0.9521 0.9524 0.1587  0.0511  0.0043  259  ALA B CB  
3181  N  N   . ASP B 260  ? 1.2567 1.1580 1.1503 0.1512  0.0354  -0.0058 260  ASP B N   
3182  C  CA  . ASP B 260  ? 1.1925 1.1059 1.1017 0.1462  0.0339  -0.0067 260  ASP B CA  
3183  C  C   . ASP B 260  ? 1.1780 1.0956 1.0970 0.1391  0.0367  -0.0065 260  ASP B C   
3184  O  O   . ASP B 260  ? 1.1297 1.0575 1.0559 0.1345  0.0328  -0.0106 260  ASP B O   
3185  C  CB  . ASP B 260  ? 1.1047 1.0298 1.0164 0.1467  0.0258  -0.0123 260  ASP B CB  
3186  C  CG  . ASP B 260  ? 1.2338 1.1694 1.1592 0.1439  0.0243  -0.0126 260  ASP B CG  
3187  O  OD1 . ASP B 260  ? 1.1992 1.1330 1.1322 0.1413  0.0294  -0.0086 260  ASP B OD1 
3188  O  OD2 . ASP B 260  ? 1.2626 1.2087 1.1913 0.1442  0.0181  -0.0170 260  ASP B OD2 
3189  N  N   . PHE B 261  ? 1.0784 0.9877 0.9974 0.1385  0.0438  -0.0017 261  PHE B N   
3190  C  CA  . PHE B 261  ? 0.9871 0.8984 0.9135 0.1329  0.0471  -0.0009 261  PHE B CA  
3191  C  C   . PHE B 261  ? 0.9654 0.8873 0.9076 0.1279  0.0469  -0.0008 261  PHE B C   
3192  O  O   . PHE B 261  ? 0.9896 0.9149 0.9385 0.1231  0.0485  -0.0010 261  PHE B O   
3193  C  CB  . PHE B 261  ? 0.9310 0.8306 0.8524 0.1345  0.0548  0.0042  261  PHE B CB  
3194  C  CG  . PHE B 261  ? 0.9514 0.8484 0.8786 0.1354  0.0599  0.0090  261  PHE B CG  
3195  C  CD1 . PHE B 261  ? 0.9705 0.8604 0.8903 0.1406  0.0611  0.0112  261  PHE B CD1 
3196  C  CD2 . PHE B 261  ? 0.8878 0.7892 0.8274 0.1310  0.0638  0.0114  261  PHE B CD2 
3197  C  CE1 . PHE B 261  ? 0.8803 0.7672 0.8054 0.1409  0.0661  0.0155  261  PHE B CE1 
3198  C  CE2 . PHE B 261  ? 0.9099 0.8094 0.8554 0.1314  0.0683  0.0155  261  PHE B CE2 
3199  C  CZ  . PHE B 261  ? 0.9241 0.8163 0.8625 0.1361  0.0697  0.0175  261  PHE B CZ  
3200  N  N   . LEU B 262  ? 0.9107 0.8372 0.8583 0.1291  0.0451  -0.0005 262  LEU B N   
3201  C  CA  . LEU B 262  ? 0.9486 0.8855 0.9103 0.1248  0.0440  -0.0011 262  LEU B CA  
3202  C  C   . LEU B 262  ? 0.9738 0.9223 0.9394 0.1230  0.0370  -0.0064 262  LEU B C   
3203  O  O   . LEU B 262  ? 0.9319 0.8889 0.9072 0.1212  0.0350  -0.0072 262  LEU B O   
3204  C  CB  . LEU B 262  ? 0.9362 0.8713 0.9021 0.1267  0.0465  0.0024  262  LEU B CB  
3205  C  CG  . LEU B 262  ? 0.8330 0.7593 0.7993 0.1269  0.0541  0.0077  262  LEU B CG  
3206  C  CD1 . LEU B 262  ? 0.8146 0.7404 0.7866 0.1277  0.0561  0.0103  262  LEU B CD1 
3207  C  CD2 . LEU B 262  ? 0.6475 0.5773 0.6219 0.1220  0.0570  0.0085  262  LEU B CD2 
3208  N  N   . ALA B 263  ? 0.9133 0.8625 0.8718 0.1234  0.0332  -0.0103 263  ALA B N   
3209  C  CA  . ALA B 263  ? 0.8518 0.8123 0.8139 0.1213  0.0268  -0.0158 263  ALA B CA  
3210  C  C   . ALA B 263  ? 0.9164 0.8793 0.8798 0.1160  0.0267  -0.0184 263  ALA B C   
3211  O  O   . ALA B 263  ? 0.9113 0.8654 0.8690 0.1156  0.0307  -0.0164 263  ALA B O   
3212  C  CB  . ALA B 263  ? 0.9012 0.8612 0.8534 0.1268  0.0217  -0.0188 263  ALA B CB  
3213  N  N   . PRO B 264  ? 1.0329 1.0073 1.0035 0.1117  0.0224  -0.0229 264  PRO B N   
3214  C  CA  . PRO B 264  ? 0.9764 0.9523 0.9479 0.1062  0.0226  -0.0255 264  PRO B CA  
3215  C  C   . PRO B 264  ? 1.0111 0.9791 0.9702 0.1077  0.0220  -0.0273 264  PRO B C   
3216  O  O   . PRO B 264  ? 1.0938 1.0649 1.0476 0.1097  0.0168  -0.0315 264  PRO B O   
3217  C  CB  . PRO B 264  ? 1.0708 1.0606 1.0506 0.1027  0.0173  -0.0305 264  PRO B CB  
3218  C  CG  . PRO B 264  ? 1.1215 1.1170 1.1087 0.1048  0.0167  -0.0288 264  PRO B CG  
3219  C  CD  . PRO B 264  ? 1.1180 1.1040 1.0971 0.1114  0.0182  -0.0252 264  PRO B CD  
3220  N  N   . GLY B 265  ? 0.7652 0.7231 0.7196 0.1070  0.0272  -0.0243 265  GLY B N   
3221  C  CA  . GLY B 265  ? 0.6535 0.6025 0.5956 0.1083  0.0273  -0.0257 265  GLY B CA  
3222  C  C   . GLY B 265  ? 0.7440 0.6848 0.6845 0.1055  0.0330  -0.0230 265  GLY B C   
3223  O  O   . GLY B 265  ? 0.8906 0.8347 0.8401 0.1014  0.0357  -0.0215 265  GLY B O   
3224  N  N   . PRO B 266  ? 0.7328 0.6624 0.6610 0.1081  0.0349  -0.0225 266  PRO B N   
3225  C  CA  . PRO B 266  ? 0.7765 0.6973 0.7020 0.1062  0.0406  -0.0198 266  PRO B CA  
3226  C  C   . PRO B 266  ? 0.8674 0.7850 0.7982 0.1080  0.0467  -0.0135 266  PRO B C   
3227  O  O   . PRO B 266  ? 0.8058 0.7178 0.7324 0.1130  0.0490  -0.0101 266  PRO B O   
3228  C  CB  . PRO B 266  ? 0.7287 0.6383 0.6388 0.1099  0.0408  -0.0207 266  PRO B CB  
3229  C  CG  . PRO B 266  ? 0.7191 0.6339 0.6251 0.1119  0.0338  -0.0256 266  PRO B CG  
3230  C  CD  . PRO B 266  ? 0.7760 0.7006 0.6919 0.1130  0.0317  -0.0247 266  PRO B CD  
3231  N  N   . GLY B 267  ? 1.4904 1.4115 1.4303 0.1038  0.0494  -0.0122 267  GLY B N   
3232  C  CA  . GLY B 267  ? 1.4615 1.3811 1.4077 0.1049  0.0548  -0.0067 267  GLY B CA  
3233  C  C   . GLY B 267  ? 1.3907 1.3170 1.3453 0.1065  0.0538  -0.0050 267  GLY B C   
3234  O  O   . GLY B 267  ? 1.4330 1.3555 1.3893 0.1092  0.0581  -0.0005 267  GLY B O   
3235  N  N   . PHE B 268  ? 1.1287 1.0648 1.0886 0.1049  0.0483  -0.0086 268  PHE B N   
3236  C  CA  . PHE B 268  ? 1.1310 1.0728 1.0977 0.1067  0.0470  -0.0073 268  PHE B CA  
3237  C  C   . PHE B 268  ? 1.1109 1.0569 1.0894 0.1045  0.0503  -0.0041 268  PHE B C   
3238  O  O   . PHE B 268  ? 1.0807 1.0253 1.0623 0.1069  0.0527  -0.0007 268  PHE B O   
3239  C  CB  . PHE B 268  ? 1.1029 1.0546 1.0725 0.1056  0.0402  -0.0122 268  PHE B CB  
3240  C  CG  . PHE B 268  ? 1.1093 1.0696 1.0895 0.1053  0.0388  -0.0115 268  PHE B CG  
3241  C  CD1 . PHE B 268  ? 1.1252 1.0826 1.1048 0.1097  0.0399  -0.0086 268  PHE B CD1 
3242  C  CD2 . PHE B 268  ? 1.1182 1.0890 1.1084 0.1007  0.0365  -0.0139 268  PHE B CD2 
3243  C  CE1 . PHE B 268  ? 1.1265 1.0911 1.1153 0.1094  0.0385  -0.0082 268  PHE B CE1 
3244  C  CE2 . PHE B 268  ? 1.0796 1.0578 1.0790 0.1007  0.0351  -0.0134 268  PHE B CE2 
3245  C  CZ  . PHE B 268  ? 1.0302 1.0053 1.0289 0.1050  0.0360  -0.0107 268  PHE B CZ  
3246  N  N   . VAL B 269  ? 0.9618 0.9125 0.9464 0.0998  0.0504  -0.0052 269  VAL B N   
3247  C  CA  . VAL B 269  ? 0.8585 0.8142 0.8543 0.0978  0.0527  -0.0027 269  VAL B CA  
3248  C  C   . VAL B 269  ? 0.8718 0.8203 0.8673 0.0999  0.0589  0.0022  269  VAL B C   
3249  O  O   . VAL B 269  ? 0.8160 0.7671 0.8192 0.1006  0.0609  0.0050  269  VAL B O   
3250  C  CB  . VAL B 269  ? 0.9280 0.8895 0.9290 0.0928  0.0516  -0.0051 269  VAL B CB  
3251  C  CG1 . VAL B 269  ? 0.8732 0.8391 0.8846 0.0913  0.0541  -0.0024 269  VAL B CG1 
3252  C  CG2 . VAL B 269  ? 0.9333 0.9035 0.9363 0.0905  0.0458  -0.0100 269  VAL B CG2 
3253  N  N   . ALA B 270  ? 0.7386 0.6782 0.7253 0.1011  0.0621  0.0032  270  ALA B N   
3254  C  CA  . ALA B 270  ? 0.6720 0.6051 0.6584 0.1032  0.0682  0.0078  270  ALA B CA  
3255  C  C   . ALA B 270  ? 0.7181 0.6470 0.7024 0.1073  0.0704  0.0107  270  ALA B C   
3256  O  O   . ALA B 270  ? 0.8099 0.7388 0.8004 0.1081  0.0745  0.0143  270  ALA B O   
3257  C  CB  . ALA B 270  ? 0.6443 0.5684 0.6208 0.1038  0.0711  0.0079  270  ALA B CB  
3258  N  N   . TYR B 271  ? 0.7457 0.6708 0.7211 0.1100  0.0678  0.0091  271  TYR B N   
3259  C  CA  . TYR B 271  ? 0.7644 0.6843 0.7365 0.1141  0.0699  0.0118  271  TYR B CA  
3260  C  C   . TYR B 271  ? 0.7677 0.6948 0.7502 0.1133  0.0686  0.0125  271  TYR B C   
3261  O  O   . TYR B 271  ? 0.6459 0.5703 0.6315 0.1148  0.0727  0.0161  271  TYR B O   
3262  C  CB  . TYR B 271  ? 0.7145 0.6287 0.6737 0.1176  0.0668  0.0096  271  TYR B CB  
3263  C  CG  . TYR B 271  ? 0.7942 0.6996 0.7415 0.1190  0.0683  0.0091  271  TYR B CG  
3264  C  CD1 . TYR B 271  ? 0.8587 0.7591 0.8057 0.1184  0.0738  0.0118  271  TYR B CD1 
3265  C  CD2 . TYR B 271  ? 0.7927 0.6948 0.7289 0.1211  0.0641  0.0056  271  TYR B CD2 
3266  C  CE1 . TYR B 271  ? 0.8730 0.7646 0.8084 0.1199  0.0752  0.0112  271  TYR B CE1 
3267  C  CE2 . TYR B 271  ? 0.8695 0.7632 0.7943 0.1223  0.0652  0.0048  271  TYR B CE2 
3268  C  CZ  . TYR B 271  ? 0.9387 0.8268 0.8630 0.1217  0.0709  0.0077  271  TYR B CZ  
3269  O  OH  . TYR B 271  ? 0.9861 0.8650 0.8984 0.1230  0.0722  0.0068  271  TYR B OH  
3270  N  N   . ALA B 272  ? 0.8031 0.7394 0.7911 0.1109  0.0630  0.0089  272  ALA B N   
3271  C  CA  . ALA B 272  ? 0.6954 0.6384 0.6928 0.1103  0.0614  0.0092  272  ALA B CA  
3272  C  C   . ALA B 272  ? 0.6853 0.6321 0.6940 0.1077  0.0650  0.0118  272  ALA B C   
3273  O  O   . ALA B 272  ? 0.7305 0.6783 0.7452 0.1082  0.0666  0.0139  272  ALA B O   
3274  C  CB  . ALA B 272  ? 0.6961 0.6486 0.6968 0.1083  0.0549  0.0046  272  ALA B CB  
3275  N  N   . ARG B 273  ? 1.0312 0.9800 1.0428 0.1051  0.0663  0.0117  273  ARG B N   
3276  C  CA  . ARG B 273  ? 1.0237 0.9765 1.0458 0.1031  0.0695  0.0141  273  ARG B CA  
3277  C  C   . ARG B 273  ? 1.0367 0.9830 1.0584 0.1055  0.0756  0.0184  273  ARG B C   
3278  O  O   . ARG B 273  ? 1.0259 0.9754 1.0564 0.1050  0.0775  0.0203  273  ARG B O   
3279  C  CB  . ARG B 273  ? 1.0009 0.9560 1.0243 0.1005  0.0697  0.0131  273  ARG B CB  
3280  C  CG  . ARG B 273  ? 1.0113 0.9708 1.0449 0.0991  0.0726  0.0154  273  ARG B CG  
3281  C  CD  . ARG B 273  ? 0.9581 0.9277 1.0015 0.0962  0.0687  0.0134  273  ARG B CD  
3282  N  NE  . ARG B 273  ? 1.0427 1.0153 1.0830 0.0940  0.0644  0.0096  273  ARG B NE  
3283  C  CZ  . ARG B 273  ? 1.0884 1.0690 1.1354 0.0913  0.0614  0.0076  273  ARG B CZ  
3284  N  NH1 . ARG B 273  ? 1.1638 1.1501 1.2205 0.0906  0.0618  0.0088  273  ARG B NH1 
3285  N  NH2 . ARG B 273  ? 1.1078 1.0906 1.1515 0.0891  0.0580  0.0041  273  ARG B NH2 
3286  N  N   . ALA B 274  ? 0.9099 0.8473 0.9218 0.1079  0.0789  0.0198  274  ALA B N   
3287  C  CA  . ALA B 274  ? 0.9333 0.8643 0.9443 0.1102  0.0853  0.0240  274  ALA B CA  
3288  C  C   . ALA B 274  ? 1.0405 0.9691 1.0518 0.1120  0.0862  0.0255  274  ALA B C   
3289  O  O   . ALA B 274  ? 1.0490 0.9778 1.0672 0.1118  0.0904  0.0284  274  ALA B O   
3290  C  CB  . ALA B 274  ? 1.0583 0.9794 1.0569 0.1130  0.0883  0.0249  274  ALA B CB  
3291  N  N   . PHE B 275  ? 1.0102 0.9364 1.0141 0.1137  0.0822  0.0234  275  PHE B N   
3292  C  CA  . PHE B 275  ? 0.9333 0.8562 0.9361 0.1158  0.0828  0.0247  275  PHE B CA  
3293  C  C   . PHE B 275  ? 0.8978 0.8288 0.9136 0.1130  0.0817  0.0246  275  PHE B C   
3294  O  O   . PHE B 275  ? 0.8974 0.8258 0.9168 0.1134  0.0854  0.0273  275  PHE B O   
3295  C  CB  . PHE B 275  ? 0.8324 0.7522 0.8246 0.1186  0.0779  0.0220  275  PHE B CB  
3296  C  CG  . PHE B 275  ? 0.8585 0.7712 0.8451 0.1222  0.0795  0.0239  275  PHE B CG  
3297  C  CD1 . PHE B 275  ? 0.8881 0.7899 0.8669 0.1252  0.0856  0.0276  275  PHE B CD1 
3298  C  CD2 . PHE B 275  ? 0.8492 0.7653 0.8376 0.1227  0.0752  0.0221  275  PHE B CD2 
3299  C  CE1 . PHE B 275  ? 0.9428 0.8368 0.9155 0.1286  0.0875  0.0295  275  PHE B CE1 
3300  C  CE2 . PHE B 275  ? 0.8075 0.7158 0.7897 0.1263  0.0768  0.0240  275  PHE B CE2 
3301  C  CZ  . PHE B 275  ? 0.9001 0.7972 0.8744 0.1291  0.0830  0.0277  275  PHE B CZ  
3302  N  N   . ALA B 276  ? 0.6456 0.5862 0.6684 0.1101  0.0767  0.0216  276  ALA B N   
3303  C  CA  . ALA B 276  ? 0.6103 0.5587 0.6448 0.1076  0.0751  0.0211  276  ALA B CA  
3304  C  C   . ALA B 276  ? 0.7158 0.6667 0.7604 0.1056  0.0799  0.0238  276  ALA B C   
3305  O  O   . ALA B 276  ? 0.6725 0.6242 0.7238 0.1048  0.0816  0.0252  276  ALA B O   
3306  C  CB  . ALA B 276  ? 0.7429 0.7008 0.7818 0.1052  0.0691  0.0172  276  ALA B CB  
3307  N  N   . GLU B 277  ? 1.2032 1.1552 1.2490 0.1047  0.0820  0.0245  277  GLU B N   
3308  C  CA  . GLU B 277  ? 1.2092 1.1643 1.2646 0.1034  0.0864  0.0270  277  GLU B CA  
3309  C  C   . GLU B 277  ? 1.0946 1.0427 1.1489 0.1050  0.0926  0.0305  277  GLU B C   
3310  O  O   . GLU B 277  ? 1.0963 1.0480 1.1605 0.1035  0.0960  0.0323  277  GLU B O   
3311  C  CB  . GLU B 277  ? 1.1789 1.1352 1.2338 0.1031  0.0877  0.0272  277  GLU B CB  
3312  C  CG  . GLU B 277  ? 1.1917 1.1538 1.2470 0.1012  0.0824  0.0238  277  GLU B CG  
3313  C  CD  . GLU B 277  ? 1.3863 1.3582 1.4538 0.0986  0.0811  0.0233  277  GLU B CD  
3314  O  OE1 . GLU B 277  ? 1.4545 1.4301 1.5309 0.0978  0.0822  0.0243  277  GLU B OE1 
3315  O  OE2 . GLU B 277  ? 1.5094 1.4847 1.5770 0.0974  0.0790  0.0217  277  GLU B OE2 
3316  N  N   . ARG B 278  ? 0.9322 0.8704 0.9745 0.1081  0.0942  0.0315  278  ARG B N   
3317  C  CA  . ARG B 278  ? 1.0577 0.9884 1.0980 0.1098  0.1003  0.0350  278  ARG B CA  
3318  C  C   . ARG B 278  ? 1.0940 1.0236 1.1366 0.1094  0.0994  0.0349  278  ARG B C   
3319  O  O   . ARG B 278  ? 1.0077 0.9325 1.0519 0.1095  0.1047  0.0377  278  ARG B O   
3320  C  CB  . ARG B 278  ? 1.1201 1.0395 1.1453 0.1138  0.1028  0.0363  278  ARG B CB  
3321  C  CG  . ARG B 278  ? 1.1387 1.0565 1.1606 0.1146  0.1056  0.0372  278  ARG B CG  
3322  C  CD  . ARG B 278  ? 1.1238 1.0446 1.1555 0.1134  0.1116  0.0402  278  ARG B CD  
3323  N  NE  . ARG B 278  ? 1.1545 1.0715 1.1891 0.1136  0.1168  0.0430  278  ARG B NE  
3324  C  CZ  . ARG B 278  ? 1.4191 1.3264 1.4458 0.1164  0.1229  0.0461  278  ARG B CZ  
3325  N  NH1 . ARG B 278  ? 1.3940 1.2940 1.4089 0.1197  0.1246  0.0468  278  ARG B NH1 
3326  N  NH2 . ARG B 278  ? 1.4580 1.3622 1.4883 0.1159  0.1277  0.0486  278  ARG B NH2 
3327  N  N   . ARG B 279  ? 0.9230 0.8568 0.9658 0.1088  0.0930  0.0318  279  ARG B N   
3328  C  CA  . ARG B 279  ? 0.7853 0.7179 0.8296 0.1088  0.0916  0.0314  279  ARG B CA  
3329  C  C   . ARG B 279  ? 0.7599 0.7021 0.8184 0.1048  0.0897  0.0301  279  ARG B C   
3330  O  O   . ARG B 279  ? 0.8406 0.7813 0.9017 0.1043  0.0896  0.0301  279  ARG B O   
3331  C  CB  . ARG B 279  ? 0.7449 0.6757 0.7796 0.1113  0.0857  0.0286  279  ARG B CB  
3332  C  CG  . ARG B 279  ? 0.8554 0.7756 0.8749 0.1158  0.0870  0.0296  279  ARG B CG  
3333  C  CD  . ARG B 279  ? 0.8673 0.7847 0.8784 0.1190  0.0822  0.0275  279  ARG B CD  
3334  N  NE  . ARG B 279  ? 0.9644 0.8736 0.9724 0.1209  0.0853  0.0298  279  ARG B NE  
3335  C  CZ  . ARG B 279  ? 0.9320 0.8292 0.9291 0.1245  0.0900  0.0327  279  ARG B CZ  
3336  N  NH1 . ARG B 279  ? 0.8716 0.7636 0.8599 0.1268  0.0921  0.0337  279  ARG B NH1 
3337  N  NH2 . ARG B 279  ? 1.0371 0.9267 1.0316 0.1259  0.0928  0.0347  279  ARG B NH2 
3338  N  N   . LYS B 280  ? 0.7663 0.7177 0.8334 0.1023  0.0882  0.0290  280  LYS B N   
3339  C  CA  . LYS B 280  ? 0.8355 0.7965 0.9158 0.0989  0.0860  0.0275  280  LYS B CA  
3340  C  C   . LYS B 280  ? 0.8488 0.8096 0.9378 0.0971  0.0917  0.0301  280  LYS B C   
3341  O  O   . LYS B 280  ? 0.9437 0.9065 1.0370 0.0966  0.0955  0.0318  280  LYS B O   
3342  C  CB  . LYS B 280  ? 0.7577 0.7278 0.8430 0.0974  0.0828  0.0257  280  LYS B CB  
3343  C  CG  . LYS B 280  ? 0.6192 0.5917 0.6988 0.0979  0.0767  0.0225  280  LYS B CG  
3344  C  CD  . LYS B 280  ? 0.7783 0.7569 0.8602 0.0967  0.0750  0.0212  280  LYS B CD  
3345  C  CE  . LYS B 280  ? 0.7813 0.7610 0.8563 0.0971  0.0699  0.0182  280  LYS B CE  
3346  N  NZ  . LYS B 280  ? 0.7148 0.6977 0.7895 0.0959  0.0693  0.0173  280  LYS B NZ  
3347  N  N   . VAL B 281  ? 0.6569 0.6151 0.7485 0.0962  0.0923  0.0303  281  VAL B N   
3348  C  CA  . VAL B 281  ? 0.6816 0.6388 0.7812 0.0940  0.0980  0.0325  281  VAL B CA  
3349  C  C   . VAL B 281  ? 0.7314 0.6993 0.8453 0.0902  0.0953  0.0304  281  VAL B C   
3350  O  O   . VAL B 281  ? 0.7831 0.7557 0.8987 0.0895  0.0895  0.0275  281  VAL B O   
3351  C  CB  . VAL B 281  ? 0.7655 0.7115 0.8582 0.0952  0.1012  0.0342  281  VAL B CB  
3352  C  CG1 . VAL B 281  ? 0.8379 0.7732 0.9178 0.0989  0.1057  0.0370  281  VAL B CG1 
3353  C  CG2 . VAL B 281  ? 0.8078 0.7524 0.8958 0.0962  0.0955  0.0316  281  VAL B CG2 
3354  N  N   . ARG B 282  ? 1.0140 0.9861 1.1384 0.0878  0.0996  0.0318  282  ARG B N   
3355  C  CA  . ARG B 282  ? 0.9856 0.9682 1.1241 0.0842  0.0974  0.0298  282  ARG B CA  
3356  C  C   . ARG B 282  ? 1.0742 1.0554 1.2211 0.0812  0.1027  0.0311  282  ARG B C   
3357  O  O   . ARG B 282  ? 1.0607 1.0317 1.2014 0.0819  0.1077  0.0335  282  ARG B O   
3358  C  CB  . ARG B 282  ? 0.8403 0.8328 0.9856 0.0841  0.0964  0.0293  282  ARG B CB  
3359  C  CG  . ARG B 282  ? 0.8425 0.8381 0.9822 0.0858  0.0906  0.0273  282  ARG B CG  
3360  C  CD  . ARG B 282  ? 1.0510 1.0546 1.1962 0.0860  0.0905  0.0273  282  ARG B CD  
3361  N  NE  . ARG B 282  ? 1.1550 1.1629 1.2973 0.0867  0.0848  0.0249  282  ARG B NE  
3362  C  CZ  . ARG B 282  ? 0.9570 0.9735 1.1068 0.0851  0.0802  0.0224  282  ARG B CZ  
3363  N  NH1 . ARG B 282  ? 0.8373 0.8594 0.9980 0.0827  0.0800  0.0216  282  ARG B NH1 
3364  N  NH2 . ARG B 282  ? 0.8418 0.8611 0.9878 0.0858  0.0757  0.0206  282  ARG B NH2 
3365  N  N   . LYS B 283  ? 1.2386 1.2300 1.3995 0.0779  0.1017  0.0295  283  LYS B N   
3366  C  CA  . LYS B 283  ? 1.2428 1.2346 1.4135 0.0744  0.1068  0.0304  283  LYS B CA  
3367  C  C   . LYS B 283  ? 1.3380 1.3287 1.5100 0.0751  0.1140  0.0337  283  LYS B C   
3368  O  O   . LYS B 283  ? 1.3586 1.3417 1.5293 0.0741  0.1204  0.0361  283  LYS B O   
3369  C  CB  . LYS B 283  ? 1.2352 1.2392 1.4207 0.0707  0.1032  0.0273  283  LYS B CB  
3370  C  CG  . LYS B 283  ? 1.2697 1.2752 1.4667 0.0662  0.1077  0.0274  283  LYS B CG  
3371  C  CD  . LYS B 283  ? 1.5090 1.5010 1.6986 0.0655  0.1126  0.0293  283  LYS B CD  
3372  C  CE  . LYS B 283  ? 1.5314 1.5249 1.7329 0.0602  0.1163  0.0287  283  LYS B CE  
3373  N  NZ  . LYS B 283  ? 1.4258 1.4064 1.6214 0.0595  0.1243  0.0319  283  LYS B NZ  
3374  N  N   . ASP B 284  ? 1.1990 1.1970 1.3733 0.0768  0.1133  0.0339  284  ASP B N   
3375  C  CA  . ASP B 284  ? 1.1634 1.1612 1.3389 0.0781  0.1199  0.0369  284  ASP B CA  
3376  C  C   . ASP B 284  ? 1.1309 1.1161 1.2908 0.0819  0.1236  0.0398  284  ASP B C   
3377  O  O   . ASP B 284  ? 1.1041 1.0870 1.2633 0.0832  0.1299  0.0426  284  ASP B O   
3378  C  CB  . ASP B 284  ? 1.2022 1.2112 1.3842 0.0793  0.1177  0.0361  284  ASP B CB  
3379  C  CG  . ASP B 284  ? 1.3917 1.4131 1.5871 0.0765  0.1126  0.0328  284  ASP B CG  
3380  O  OD1 . ASP B 284  ? 1.5422 1.5707 1.7506 0.0736  0.1153  0.0324  284  ASP B OD1 
3381  O  OD2 . ASP B 284  ? 1.5277 1.5521 1.7205 0.0772  0.1060  0.0303  284  ASP B OD2 
3382  N  N   . SER B 285  ? 0.7755 0.7529 0.9231 0.0839  0.1198  0.0391  285  SER B N   
3383  C  CA  . SER B 285  ? 0.6560 0.6217 0.7882 0.0878  0.1224  0.0414  285  SER B CA  
3384  C  C   . SER B 285  ? 0.7454 0.7013 0.8745 0.0876  0.1301  0.0446  285  SER B C   
3385  O  O   . SER B 285  ? 0.8769 0.8317 1.0121 0.0845  0.1321  0.0445  285  SER B O   
3386  C  CB  . SER B 285  ? 0.5315 0.4920 0.6524 0.0897  0.1163  0.0395  285  SER B CB  
3387  O  OG  . SER B 285  ? 0.6607 0.6104 0.7666 0.0937  0.1182  0.0413  285  SER B OG  
3388  N  N   . THR B 286  ? 0.8818 0.8298 1.0008 0.0911  0.1348  0.0474  286  THR B N   
3389  C  CA  . THR B 286  ? 0.9377 0.8753 1.0520 0.0915  0.1429  0.0509  286  THR B CA  
3390  C  C   . THR B 286  ? 0.9246 0.8482 1.0201 0.0963  0.1442  0.0527  286  THR B C   
3391  O  O   . THR B 286  ? 0.8361 0.7489 0.9253 0.0969  0.1498  0.0552  286  THR B O   
3392  C  CB  . THR B 286  ? 0.9169 0.8594 1.0400 0.0908  0.1499  0.0532  286  THR B CB  
3393  O  OG1 . THR B 286  ? 0.9854 0.9179 1.1048 0.0907  0.1584  0.0565  286  THR B OG1 
3394  C  CG2 . THR B 286  ? 0.8433 0.7866 0.9599 0.0948  0.1497  0.0539  286  THR B CG2 
3395  N  N   . THR B 287  ? 1.3041 1.2272 1.3904 0.0996  0.1394  0.0515  287  THR B N   
3396  C  CA  . THR B 287  ? 1.3537 1.2644 1.4221 0.1043  0.1399  0.0527  287  THR B CA  
3397  C  C   . THR B 287  ? 1.3060 1.2169 1.3673 0.1057  0.1313  0.0495  287  THR B C   
3398  O  O   . THR B 287  ? 1.2510 1.1721 1.3203 0.1035  0.1253  0.0464  287  THR B O   
3399  C  CB  . THR B 287  ? 1.3868 1.2955 1.4490 0.1075  0.1431  0.0545  287  THR B CB  
3400  O  OG1 . THR B 287  ? 1.3128 1.2317 1.3805 0.1068  0.1380  0.0520  287  THR B OG1 
3401  C  CG2 . THR B 287  ? 1.3449 1.2530 1.4134 0.1066  0.1521  0.0579  287  THR B CG2 
3402  N  N   . MET B 288  ? 0.9671 0.8667 1.0129 0.1097  0.1309  0.0501  288  MET B N   
3403  C  CA  . MET B 288  ? 0.9078 0.8074 0.9460 0.1116  0.1230  0.0470  288  MET B CA  
3404  C  C   . MET B 288  ? 0.9975 0.8852 1.0177 0.1168  0.1237  0.0480  288  MET B C   
3405  O  O   . MET B 288  ? 1.1446 1.0211 1.1569 0.1191  0.1292  0.0510  288  MET B O   
3406  C  CB  . MET B 288  ? 0.9050 0.8050 0.9467 0.1099  0.1199  0.0455  288  MET B CB  
3407  C  CG  . MET B 288  ? 0.9220 0.8203 0.9540 0.1129  0.1127  0.0427  288  MET B CG  
3408  S  SD  . MET B 288  ? 1.0233 0.9280 1.0639 0.1101  0.1071  0.0397  288  MET B SD  
3409  C  CE  . MET B 288  ? 0.9286 0.8245 0.9526 0.1156  0.1024  0.0384  288  MET B CE  
3410  N  N   . ASN B 289  ? 0.7884 0.6782 0.8021 0.1188  0.1183  0.0456  289  ASN B N   
3411  C  CA  . ASN B 289  ? 0.7813 0.6608 0.7780 0.1238  0.1183  0.0460  289  ASN B CA  
3412  C  C   . ASN B 289  ? 0.7936 0.6667 0.7809 0.1267  0.1147  0.0450  289  ASN B C   
3413  O  O   . ASN B 289  ? 0.8222 0.7006 0.8159 0.1249  0.1106  0.0430  289  ASN B O   
3414  C  CB  . ASN B 289  ? 0.7726 0.6564 0.7656 0.1245  0.1135  0.0433  289  ASN B CB  
3415  C  CG  . ASN B 289  ? 0.5987 0.4931 0.5979 0.1221  0.1053  0.0391  289  ASN B CG  
3416  O  OD1 . ASN B 289  ? 0.6420 0.5413 0.6494 0.1199  0.1031  0.0381  289  ASN B OD1 
3417  N  ND2 . ASN B 289  ? 0.5664 0.4639 0.5615 0.1225  0.1009  0.0364  289  ASN B ND2 
3418  N  N   . ARG B 290  ? 0.7706 0.6320 0.7421 0.1318  0.1164  0.0463  290  ARG B N   
3419  C  CA  . ARG B 290  ? 0.7945 0.6484 0.7547 0.1359  0.1135  0.0457  290  ARG B CA  
3420  C  C   . ARG B 290  ? 0.8205 0.6720 0.7673 0.1403  0.1081  0.0432  290  ARG B C   
3421  O  O   . ARG B 290  ? 0.8927 0.7412 0.8333 0.1417  0.1101  0.0438  290  ARG B O   
3422  C  CB  . ARG B 290  ? 0.8777 0.7178 0.8300 0.1385  0.1211  0.0500  290  ARG B CB  
3423  C  CG  . ARG B 290  ? 0.9496 0.7799 0.8881 0.1437  0.1188  0.0499  290  ARG B CG  
3424  C  CD  . ARG B 290  ? 1.0307 0.8460 0.9602 0.1463  0.1273  0.0545  290  ARG B CD  
3425  N  NE  . ARG B 290  ? 1.0202 0.8365 0.9624 0.1413  0.1330  0.0567  290  ARG B NE  
3426  C  CZ  . ARG B 290  ? 1.0189 0.8333 0.9668 0.1386  0.1413  0.0601  290  ARG B CZ  
3427  N  NH1 . ARG B 290  ? 1.0042 0.8149 0.9460 0.1407  0.1453  0.0620  290  ARG B NH1 
3428  N  NH2 . ARG B 290  ? 1.1198 0.9362 1.0800 0.1337  0.1456  0.0615  290  ARG B NH2 
3429  N  N   . LEU B 291  ? 0.6493 0.5026 0.5917 0.1424  0.1013  0.0401  291  LEU B N   
3430  C  CA  . LEU B 291  ? 0.6077 0.4612 0.5392 0.1461  0.0950  0.0368  291  LEU B CA  
3431  C  C   . LEU B 291  ? 0.7081 0.5509 0.6244 0.1526  0.0939  0.0372  291  LEU B C   
3432  O  O   . LEU B 291  ? 0.7937 0.6357 0.7112 0.1534  0.0925  0.0372  291  LEU B O   
3433  C  CB  . LEU B 291  ? 0.4802 0.3478 0.4209 0.1429  0.0869  0.0320  291  LEU B CB  
3434  C  CG  . LEU B 291  ? 0.4723 0.3423 0.4039 0.1462  0.0794  0.0277  291  LEU B CG  
3435  C  CD1 . LEU B 291  ? 0.5433 0.4076 0.4640 0.1484  0.0804  0.0276  291  LEU B CD1 
3436  C  CD2 . LEU B 291  ? 0.4719 0.3565 0.4148 0.1420  0.0727  0.0234  291  LEU B CD2 
3437  N  N   . TYR B 292  ? 1.0629 0.8971 0.9643 0.1574  0.0944  0.0376  292  TYR B N   
3438  C  CA  . TYR B 292  ? 1.0399 0.8646 0.9249 0.1645  0.0921  0.0373  292  TYR B CA  
3439  C  C   . TYR B 292  ? 1.0149 0.8459 0.8942 0.1666  0.0835  0.0322  292  TYR B C   
3440  O  O   . TYR B 292  ? 0.9206 0.7544 0.7994 0.1650  0.0827  0.0307  292  TYR B O   
3441  C  CB  . TYR B 292  ? 1.0683 0.8770 0.9389 0.1691  0.0994  0.0416  292  TYR B CB  
3442  C  CG  . TYR B 292  ? 1.1326 0.9330 1.0063 0.1679  0.1082  0.0467  292  TYR B CG  
3443  C  CD1 . TYR B 292  ? 1.2002 0.9928 1.0684 0.1710  0.1092  0.0483  292  TYR B CD1 
3444  C  CD2 . TYR B 292  ? 1.1515 0.9517 1.0332 0.1638  0.1158  0.0499  292  TYR B CD2 
3445  C  CE1 . TYR B 292  ? 1.2729 1.0574 1.1438 0.1694  0.1176  0.0528  292  TYR B CE1 
3446  C  CE2 . TYR B 292  ? 1.1527 0.9460 1.0380 0.1623  0.1240  0.0543  292  TYR B CE2 
3447  C  CZ  . TYR B 292  ? 1.2401 1.0254 1.1200 0.1648  0.1249  0.0557  292  TYR B CZ  
3448  O  OH  . TYR B 292  ? 1.3355 1.1135 1.2190 0.1627  0.1334  0.0599  292  TYR B OH  
3449  N  N   . VAL B 293  ? 0.9210 0.7543 0.7962 0.1701  0.0771  0.0293  293  VAL B N   
3450  C  CA  . VAL B 293  ? 0.9393 0.7796 0.8096 0.1722  0.0686  0.0241  293  VAL B CA  
3451  C  C   . VAL B 293  ? 0.9941 0.8258 0.8482 0.1805  0.0656  0.0236  293  VAL B C   
3452  O  O   . VAL B 293  ? 1.0599 0.8855 0.9113 0.1835  0.0675  0.0260  293  VAL B O   
3453  C  CB  . VAL B 293  ? 0.8732 0.7300 0.7583 0.1673  0.0620  0.0198  293  VAL B CB  
3454  C  CG1 . VAL B 293  ? 0.8696 0.7280 0.7585 0.1686  0.0604  0.0200  293  VAL B CG1 
3455  C  CG2 . VAL B 293  ? 0.9157 0.7805 0.7971 0.1683  0.0540  0.0141  293  VAL B CG2 
3456  N  N   . VAL B 294  ? 0.6793 0.5100 0.5219 0.1845  0.0611  0.0206  294  VAL B N   
3457  C  CA  . VAL B 294  ? 0.6705 0.4947 0.4971 0.1930  0.0569  0.0193  294  VAL B CA  
3458  C  C   . VAL B 294  ? 0.7752 0.6123 0.6031 0.1930  0.0472  0.0126  294  VAL B C   
3459  O  O   . VAL B 294  ? 0.9173 0.7565 0.7426 0.1916  0.0454  0.0101  294  VAL B O   
3460  C  CB  . VAL B 294  ? 0.8335 0.6414 0.6421 0.1989  0.0618  0.0225  294  VAL B CB  
3461  C  CG1 . VAL B 294  ? 0.9613 0.7634 0.7528 0.2081  0.0565  0.0205  294  VAL B CG1 
3462  C  CG2 . VAL B 294  ? 0.8241 0.6194 0.6320 0.1985  0.0720  0.0291  294  VAL B CG2 
3463  N  N   . GLU B 295  ? 1.0949 0.9408 0.9271 0.1945  0.0410  0.0096  295  GLU B N   
3464  C  CA  . GLU B 295  ? 1.1528 1.0133 0.9893 0.1935  0.0320  0.0030  295  GLU B CA  
3465  C  C   . GLU B 295  ? 1.2251 1.0869 1.0536 0.2011  0.0257  0.0005  295  GLU B C   
3466  O  O   . GLU B 295  ? 1.2641 1.1181 1.0882 0.2054  0.0281  0.0037  295  GLU B O   
3467  C  CB  . GLU B 295  ? 1.1268 1.0023 0.9831 0.1849  0.0305  0.0010  295  GLU B CB  
3468  C  CG  . GLU B 295  ? 1.2790 1.1557 1.1445 0.1836  0.0329  0.0036  295  GLU B CG  
3469  C  CD  . GLU B 295  ? 1.3634 1.2539 1.2476 0.1753  0.0321  0.0020  295  GLU B CD  
3470  O  OE1 . GLU B 295  ? 1.4209 1.3189 1.3108 0.1703  0.0305  -0.0006 295  GLU B OE1 
3471  O  OE2 . GLU B 295  ? 1.2812 1.1745 1.1738 0.1739  0.0329  0.0032  295  GLU B OE2 
3472  N  N   . ALA B 296  ? 0.9850 0.8569 0.8118 0.2026  0.0174  -0.0055 296  ALA B N   
3473  C  CA  . ALA B 296  ? 0.9548 0.8308 0.7754 0.2099  0.0104  -0.0087 296  ALA B CA  
3474  C  C   . ALA B 296  ? 0.9910 0.8814 0.8268 0.2066  0.0067  -0.0111 296  ALA B C   
3475  O  O   . ALA B 296  ? 1.0723 0.9603 0.9060 0.2113  0.0063  -0.0097 296  ALA B O   
3476  C  CB  . ALA B 296  ? 1.0578 0.9392 0.8701 0.2132  0.0030  -0.0144 296  ALA B CB  
3477  N  N   . SER B 297  ? 1.2848 1.1898 1.1353 0.1986  0.0042  -0.0147 297  SER B N   
3478  C  CA  . SER B 297  ? 1.2095 1.1281 1.0753 0.1946  0.0014  -0.0168 297  SER B CA  
3479  C  C   . SER B 297  ? 1.1963 1.1144 1.0749 0.1866  0.0080  -0.0130 297  SER B C   
3480  O  O   . SER B 297  ? 1.1149 1.0315 0.9964 0.1812  0.0115  -0.0121 297  SER B O   
3481  C  CB  . SER B 297  ? 1.1072 1.0435 0.9810 0.1914  -0.0062 -0.0237 297  SER B CB  
3482  O  OG  . SER B 297  ? 1.0454 0.9840 0.9235 0.1844  -0.0047 -0.0249 297  SER B OG  
3483  N  N   . PRO B 298  ? 1.2269 1.1462 1.1131 0.1859  0.0098  -0.0109 298  PRO B N   
3484  C  CA  . PRO B 298  ? 1.2204 1.1400 1.1191 0.1783  0.0156  -0.0077 298  PRO B CA  
3485  C  C   . PRO B 298  ? 1.1406 1.0747 1.0531 0.1704  0.0131  -0.0114 298  PRO B C   
3486  O  O   . PRO B 298  ? 0.9769 0.9233 0.8926 0.1702  0.0066  -0.0166 298  PRO B O   
3487  C  CB  . PRO B 298  ? 1.1508 1.0702 1.0538 0.1801  0.0161  -0.0061 298  PRO B CB  
3488  C  CG  . PRO B 298  ? 1.1271 1.0523 1.0244 0.1868  0.0088  -0.0101 298  PRO B CG  
3489  C  CD  . PRO B 298  ? 1.1030 1.0226 0.9857 0.1922  0.0065  -0.0115 298  PRO B CD  
3490  N  N   . SER B 299  ? 1.0928 1.0254 1.0134 0.1639  0.0186  -0.0085 299  SER B N   
3491  C  CA  . SER B 299  ? 0.9967 0.9406 0.9290 0.1564  0.0174  -0.0113 299  SER B CA  
3492  C  C   . SER B 299  ? 0.9041 0.8482 0.8481 0.1507  0.0228  -0.0078 299  SER B C   
3493  O  O   . SER B 299  ? 0.8766 0.8144 0.8213 0.1522  0.0264  -0.0042 299  SER B O   
3494  C  CB  . SER B 299  ? 1.1580 1.0987 1.0837 0.1552  0.0178  -0.0124 299  SER B CB  
3495  O  OG  . SER B 299  ? 1.1745 1.1016 1.0939 0.1559  0.0248  -0.0074 299  SER B OG  
3496  N  N   . THR B 300  ? 0.9998 0.9509 0.9530 0.1441  0.0233  -0.0090 300  THR B N   
3497  C  CA  . THR B 300  ? 0.9615 0.9137 0.9259 0.1387  0.0280  -0.0061 300  THR B CA  
3498  C  C   . THR B 300  ? 0.9852 0.9245 0.9451 0.1393  0.0353  -0.0008 300  THR B C   
3499  O  O   . THR B 300  ? 0.9697 0.9067 0.9362 0.1375  0.0395  0.0025  300  THR B O   
3500  C  CB  . THR B 300  ? 0.9450 0.9070 0.9186 0.1322  0.0269  -0.0087 300  THR B CB  
3501  O  OG1 . THR B 300  ? 1.1034 1.0606 1.0700 0.1315  0.0281  -0.0090 300  THR B OG1 
3502  C  CG2 . THR B 300  ? 0.8727 0.8480 0.8515 0.1312  0.0202  -0.0139 300  THR B CG2 
3503  N  N   . THR B 301  ? 0.8455 0.7764 0.7943 0.1418  0.0369  -0.0001 301  THR B N   
3504  C  CA  . THR B 301  ? 0.8076 0.7263 0.7515 0.1427  0.0442  0.0049  301  THR B CA  
3505  C  C   . THR B 301  ? 0.7206 0.6300 0.6593 0.1473  0.0471  0.0083  301  THR B C   
3506  O  O   . THR B 301  ? 0.6862 0.5899 0.6287 0.1458  0.0533  0.0125  301  THR B O   
3507  C  CB  . THR B 301  ? 0.9774 0.8888 0.9091 0.1451  0.0448  0.0046  301  THR B CB  
3508  O  OG1 . THR B 301  ? 0.8156 0.7345 0.7520 0.1404  0.0426  0.0014  301  THR B OG1 
3509  C  CG2 . THR B 301  ? 1.0374 0.9361 0.9639 0.1463  0.0528  0.0099  301  THR B CG2 
3510  N  N   . GLY B 302  ? 0.8166 0.7245 0.7468 0.1529  0.0428  0.0066  302  GLY B N   
3511  C  CA  . GLY B 302  ? 0.9722 0.8705 0.8963 0.1576  0.0454  0.0097  302  GLY B CA  
3512  C  C   . GLY B 302  ? 0.8867 0.7889 0.8226 0.1544  0.0467  0.0109  302  GLY B C   
3513  O  O   . GLY B 302  ? 0.9035 0.7962 0.8366 0.1564  0.0512  0.0145  302  GLY B O   
3514  N  N   . THR B 303  ? 0.9283 0.8439 0.8771 0.1495  0.0431  0.0079  303  THR B N   
3515  C  CA  . THR B 303  ? 0.9299 0.8497 0.8902 0.1463  0.0441  0.0087  303  THR B CA  
3516  C  C   . THR B 303  ? 0.9130 0.8277 0.8796 0.1421  0.0514  0.0130  303  THR B C   
3517  O  O   . THR B 303  ? 0.9161 0.8251 0.8846 0.1422  0.0551  0.0157  303  THR B O   
3518  C  CB  . THR B 303  ? 0.9735 0.9088 0.9455 0.1420  0.0387  0.0046  303  THR B CB  
3519  O  OG1 . THR B 303  ? 0.9748 0.9155 0.9425 0.1461  0.0322  0.0007  303  THR B OG1 
3520  C  CG2 . THR B 303  ? 1.0363 0.9759 1.0209 0.1378  0.0405  0.0056  303  THR B CG2 
3521  N  N   . ALA B 304  ? 0.7191 0.6359 0.6889 0.1385  0.0537  0.0134  304  ALA B N   
3522  C  CA  . ALA B 304  ? 0.7181 0.6317 0.6947 0.1347  0.0604  0.0171  304  ALA B CA  
3523  C  C   . ALA B 304  ? 0.8046 0.7041 0.7712 0.1379  0.0669  0.0214  304  ALA B C   
3524  O  O   . ALA B 304  ? 0.8561 0.7528 0.8271 0.1352  0.0728  0.0244  304  ALA B O   
3525  C  CB  . ALA B 304  ? 0.7721 0.6931 0.7553 0.1302  0.0603  0.0160  304  ALA B CB  
3526  N  N   . ALA B 305  ? 0.9651 0.8556 0.9182 0.1439  0.0660  0.0217  305  ALA B N   
3527  C  CA  . ALA B 305  ? 0.9457 0.8218 0.8875 0.1476  0.0723  0.0258  305  ALA B CA  
3528  C  C   . ALA B 305  ? 0.9940 0.8623 0.9368 0.1480  0.0770  0.0291  305  ALA B C   
3529  O  O   . ALA B 305  ? 1.0175 0.8870 0.9609 0.1495  0.0737  0.0278  305  ALA B O   
3530  C  CB  . ALA B 305  ? 0.9872 0.8567 0.9124 0.1544  0.0690  0.0245  305  ALA B CB  
3531  N  N   . ASP B 306  ? 1.2588 1.1188 1.2016 0.1467  0.0850  0.0334  306  ASP B N   
3532  C  CA  . ASP B 306  ? 1.3929 1.2438 1.3356 0.1469  0.0904  0.0367  306  ASP B CA  
3533  C  C   . ASP B 306  ? 1.3944 1.2315 1.3197 0.1541  0.0911  0.0381  306  ASP B C   
3534  O  O   . ASP B 306  ? 1.3571 1.1877 1.2804 0.1555  0.0925  0.0394  306  ASP B O   
3535  C  CB  . ASP B 306  ? 1.3297 1.1767 1.2783 0.1431  0.0991  0.0407  306  ASP B CB  
3536  C  CG  . ASP B 306  ? 1.4513 1.3112 1.4184 0.1361  0.0990  0.0396  306  ASP B CG  
3537  O  OD1 . ASP B 306  ? 1.3795 1.2491 1.3549 0.1339  0.0932  0.0365  306  ASP B OD1 
3538  O  OD2 . ASP B 306  ? 1.5609 1.4212 1.5338 0.1331  0.1046  0.0419  306  ASP B OD2 
3539  N  N   . HIS B 307  ? 0.9699 0.8018 0.8818 0.1591  0.0899  0.0379  307  HIS B N   
3540  C  CA  . HIS B 307  ? 1.0142 0.8336 0.9082 0.1669  0.0896  0.0389  307  HIS B CA  
3541  C  C   . HIS B 307  ? 1.0356 0.8598 0.9211 0.1711  0.0819  0.0348  307  HIS B C   
3542  O  O   . HIS B 307  ? 1.0071 0.8353 0.8929 0.1696  0.0813  0.0338  307  HIS B O   
3543  C  CB  . HIS B 307  ? 1.0686 0.8722 0.9519 0.1693  0.0985  0.0439  307  HIS B CB  
3544  C  CG  . HIS B 307  ? 1.1146 0.9130 1.0059 0.1650  0.1067  0.0478  307  HIS B CG  
3545  N  ND1 . HIS B 307  ? 1.0693 0.8610 0.9594 0.1659  0.1081  0.0491  307  HIS B ND1 
3546  C  CD2 . HIS B 307  ? 1.1251 0.9241 1.0259 0.1597  0.1138  0.0506  307  HIS B CD2 
3547  C  CE1 . HIS B 307  ? 1.1493 0.9378 1.0481 0.1608  0.1158  0.0523  307  HIS B CE1 
3548  N  NE2 . HIS B 307  ? 1.0721 0.8654 0.9778 0.1571  0.1193  0.0533  307  HIS B NE2 
3549  N  N   . ARG B 308  ? 1.0452 0.8693 0.9234 0.1764  0.0760  0.0324  308  ARG B N   
3550  C  CA  . ARG B 308  ? 0.9736 0.8038 0.8447 0.1804  0.0679  0.0280  308  ARG B CA  
3551  C  C   . ARG B 308  ? 0.9965 0.8141 0.8484 0.1897  0.0670  0.0288  308  ARG B C   
3552  O  O   . ARG B 308  ? 1.0459 0.8563 0.8936 0.1930  0.0683  0.0305  308  ARG B O   
3553  C  CB  . ARG B 308  ? 0.9977 0.8439 0.8804 0.1778  0.0601  0.0231  308  ARG B CB  
3554  C  CG  . ARG B 308  ? 1.0022 0.8579 0.8814 0.1800  0.0519  0.0179  308  ARG B CG  
3555  C  CD  . ARG B 308  ? 0.9300 0.8013 0.8212 0.1774  0.0450  0.0134  308  ARG B CD  
3556  N  NE  . ARG B 308  ? 0.9743 0.8430 0.8604 0.1829  0.0422  0.0130  308  ARG B NE  
3557  C  CZ  . ARG B 308  ? 1.0479 0.9168 0.9232 0.1900  0.0363  0.0102  308  ARG B CZ  
3558  N  NH1 . ARG B 308  ? 0.9629 0.8353 0.8317 0.1921  0.0322  0.0072  308  ARG B NH1 
3559  N  NH2 . ARG B 308  ? 1.1016 0.9670 0.9721 0.1953  0.0345  0.0104  308  ARG B NH2 
3560  N  N   . LEU B 309  ? 1.0532 0.8678 0.8930 0.1941  0.0648  0.0275  309  LEU B N   
3561  C  CA  . LEU B 309  ? 1.0943 0.8967 0.9143 0.2036  0.0636  0.0281  309  LEU B CA  
3562  C  C   . LEU B 309  ? 1.0518 0.8642 0.8675 0.2077  0.0534  0.0222  309  LEU B C   
3563  O  O   . LEU B 309  ? 1.0503 0.8685 0.8657 0.2062  0.0505  0.0194  309  LEU B O   
3564  C  CB  . LEU B 309  ? 1.1506 0.9385 0.9576 0.2064  0.0704  0.0320  309  LEU B CB  
3565  C  CG  . LEU B 309  ? 1.1994 0.9733 0.9841 0.2167  0.0696  0.0329  309  LEU B CG  
3566  C  CD1 . LEU B 309  ? 1.2232 0.9836 1.0006 0.2208  0.0744  0.0371  309  LEU B CD1 
3567  C  CD2 . LEU B 309  ? 1.1996 0.9633 0.9727 0.2187  0.0743  0.0352  309  LEU B CD2 
3568  N  N   . PRO B 310  ? 0.9530 0.7680 0.7655 0.2127  0.0478  0.0200  310  PRO B N   
3569  C  CA  . PRO B 310  ? 1.0193 0.8452 0.8284 0.2168  0.0379  0.0140  310  PRO B CA  
3570  C  C   . PRO B 310  ? 1.1813 0.9969 0.9699 0.2258  0.0361  0.0138  310  PRO B C   
3571  O  O   . PRO B 310  ? 1.2410 1.0504 1.0168 0.2344  0.0333  0.0136  310  PRO B O   
3572  C  CB  . PRO B 310  ? 1.0763 0.9075 0.8894 0.2193  0.0338  0.0125  310  PRO B CB  
3573  C  CG  . PRO B 310  ? 1.1880 1.0126 1.0090 0.2148  0.0413  0.0172  310  PRO B CG  
3574  C  CD  . PRO B 310  ? 1.0271 0.8367 0.8408 0.2141  0.0502  0.0225  310  PRO B CD  
3575  N  N   . LEU B 311  ? 1.0725 0.8857 0.8572 0.2242  0.0378  0.0137  311  LEU B N   
3576  C  CA  . LEU B 311  ? 1.1592 0.9633 0.9247 0.2321  0.0359  0.0130  311  LEU B CA  
3577  C  C   . LEU B 311  ? 1.1470 0.9657 0.9133 0.2334  0.0254  0.0058  311  LEU B C   
3578  O  O   . LEU B 311  ? 1.0699 0.9048 0.8520 0.2265  0.0212  0.0018  311  LEU B O   
3579  C  CB  . LEU B 311  ? 1.1741 0.9675 0.9341 0.2300  0.0432  0.0165  311  LEU B CB  
3580  C  CG  . LEU B 311  ? 1.1502 0.9274 0.8875 0.2390  0.0448  0.0184  311  LEU B CG  
3581  C  CD1 . LEU B 311  ? 1.1684 0.9311 0.8930 0.2468  0.0483  0.0226  311  LEU B CD1 
3582  C  CD2 . LEU B 311  ? 1.1123 0.8802 0.8466 0.2359  0.0527  0.0220  311  LEU B CD2 
3583  N  N   . ARG B 312  ? 1.2307 1.0433 0.9794 0.2423  0.0213  0.0040  312  ARG B N   
3584  C  CA  . ARG B 312  ? 1.1903 1.0163 0.9387 0.2438  0.0113  -0.0032 312  ARG B CA  
3585  C  C   . ARG B 312  ? 1.2483 1.0793 1.0018 0.2370  0.0114  -0.0055 312  ARG B C   
3586  O  O   . ARG B 312  ? 1.3235 1.1442 1.0749 0.2339  0.0190  -0.0013 312  ARG B O   
3587  C  CB  . ARG B 312  ? 1.2312 1.0490 0.9588 0.2556  0.0067  -0.0045 312  ARG B CB  
3588  C  CG  . ARG B 312  ? 1.4008 1.2275 1.1284 0.2617  -0.0010 -0.0081 312  ARG B CG  
3589  C  CD  . ARG B 312  ? 1.2381 1.0575 0.9447 0.2738  -0.0061 -0.0098 312  ARG B CD  
3590  N  NE  . ARG B 312  ? 1.2068 1.0325 0.9092 0.2739  -0.0120 -0.0152 312  ARG B NE  
3591  C  CZ  . ARG B 312  ? 1.2831 1.1086 0.9708 0.2831  -0.0192 -0.0191 312  ARG B CZ  
3592  N  NH1 . ARG B 312  ? 1.4718 1.2915 1.1472 0.2937  -0.0217 -0.0183 312  ARG B NH1 
3593  N  NH2 . ARG B 312  ? 1.2774 1.1088 0.9625 0.2818  -0.0242 -0.0242 312  ARG B NH2 
3594  N  N   . ALA B 313  ? 1.2020 1.0488 0.9621 0.2345  0.0030  -0.0124 313  ALA B N   
3595  C  CA  . ALA B 313  ? 1.1451 0.9975 0.9111 0.2272  0.0027  -0.0151 313  ALA B CA  
3596  C  C   . ALA B 313  ? 1.2215 1.0612 0.9697 0.2320  0.0039  -0.0148 313  ALA B C   
3597  O  O   . ALA B 313  ? 1.1824 1.0191 0.9322 0.2266  0.0077  -0.0141 313  ALA B O   
3598  C  CB  . ALA B 313  ? 1.0704 0.9430 0.8481 0.2231  -0.0064 -0.0228 313  ALA B CB  
3599  N  N   . ASP B 314  ? 1.4242 1.2559 1.1548 0.2423  0.0006  -0.0153 314  ASP B N   
3600  C  CA  . ASP B 314  ? 1.2716 1.0908 0.9838 0.2475  0.0012  -0.0152 314  ASP B CA  
3601  C  C   . ASP B 314  ? 1.3182 1.1171 1.0196 0.2501  0.0119  -0.0073 314  ASP B C   
3602  O  O   . ASP B 314  ? 1.4519 1.2411 1.1436 0.2505  0.0154  -0.0061 314  ASP B O   
3603  C  CB  . ASP B 314  ? 1.3235 1.1429 1.0205 0.2580  -0.0071 -0.0194 314  ASP B CB  
3604  C  CG  . ASP B 314  ? 1.5321 1.3723 1.2395 0.2557  -0.0179 -0.0277 314  ASP B CG  
3605  O  OD1 . ASP B 314  ? 1.4528 1.3058 1.1768 0.2458  -0.0188 -0.0307 314  ASP B OD1 
3606  O  OD2 . ASP B 314  ? 1.5853 1.4293 1.2843 0.2639  -0.0253 -0.0313 314  ASP B OD2 
3607  N  N   . ALA B 315  ? 1.5404 1.3326 1.2432 0.2518  0.0175  -0.0019 315  ALA B N   
3608  C  CA  . ALA B 315  ? 1.5515 1.3245 1.2443 0.2543  0.0280  0.0057  315  ALA B CA  
3609  C  C   . ALA B 315  ? 1.5500 1.3222 1.2554 0.2449  0.0363  0.0094  315  ALA B C   
3610  O  O   . ALA B 315  ? 1.6003 1.3579 1.2998 0.2459  0.0457  0.0157  315  ALA B O   
3611  C  CB  . ALA B 315  ? 1.4808 1.2466 1.1705 0.2593  0.0309  0.0099  315  ALA B CB  
3612  N  N   . ILE B 316  ? 1.3135 1.1008 1.0358 0.2360  0.0334  0.0057  316  ILE B N   
3613  C  CA  . ILE B 316  ? 1.2842 1.0715 1.0188 0.2275  0.0410  0.0090  316  ILE B CA  
3614  C  C   . ILE B 316  ? 1.2669 1.0439 0.9907 0.2281  0.0451  0.0102  316  ILE B C   
3615  O  O   . ILE B 316  ? 1.2119 0.9814 0.9384 0.2248  0.0540  0.0152  316  ILE B O   
3616  C  CB  . ILE B 316  ? 1.2259 1.0321 0.9815 0.2183  0.0365  0.0048  316  ILE B CB  
3617  C  CG1 . ILE B 316  ? 1.2164 1.0312 0.9823 0.2180  0.0337  0.0045  316  ILE B CG1 
3618  C  CG2 . ILE B 316  ? 1.1462 0.9527 0.9137 0.2100  0.0438  0.0079  316  ILE B CG2 
3619  C  CD1 . ILE B 316  ? 1.1697 1.0036 0.9542 0.2103  0.0281  -0.0003 316  ILE B CD1 
3620  N  N   . ALA B 317  ? 1.2693 1.0459 0.9808 0.2324  0.0388  0.0055  317  ALA B N   
3621  C  CA  . ALA B 317  ? 1.2576 1.0227 0.9562 0.2341  0.0426  0.0066  317  ALA B CA  
3622  C  C   . ALA B 317  ? 1.2797 1.0252 0.9620 0.2414  0.0508  0.0133  317  ALA B C   
3623  O  O   . ALA B 317  ? 1.2744 1.0098 0.9536 0.2400  0.0592  0.0176  317  ALA B O   
3624  C  CB  . ALA B 317  ? 1.1827 0.9514 0.8708 0.2376  0.0334  -0.0003 317  ALA B CB  
3625  N  N   . ALA B 318  ? 1.2072 0.9468 0.8785 0.2495  0.0488  0.0142  318  ALA B N   
3626  C  CA  . ALA B 318  ? 1.2310 0.9514 0.8870 0.2562  0.0572  0.0209  318  ALA B CA  
3627  C  C   . ALA B 318  ? 1.2150 0.9324 0.8834 0.2507  0.0672  0.0272  318  ALA B C   
3628  O  O   . ALA B 318  ? 1.2654 0.9679 0.9256 0.2526  0.0768  0.0331  318  ALA B O   
3629  C  CB  . ALA B 318  ? 1.2930 1.0081 0.9345 0.2662  0.0524  0.0202  318  ALA B CB  
3630  N  N   . PHE B 319  ? 1.3838 1.1153 1.0721 0.2437  0.0650  0.0259  319  PHE B N   
3631  C  CA  . PHE B 319  ? 1.4034 1.1339 1.1054 0.2376  0.0737  0.0312  319  PHE B CA  
3632  C  C   . PHE B 319  ? 1.3471 1.0765 1.0554 0.2315  0.0806  0.0334  319  PHE B C   
3633  O  O   . PHE B 319  ? 1.3258 1.0454 1.0344 0.2305  0.0906  0.0393  319  PHE B O   
3634  C  CB  . PHE B 319  ? 1.2578 1.0048 0.9794 0.2315  0.0689  0.0284  319  PHE B CB  
3635  C  CG  . PHE B 319  ? 1.1631 0.9098 0.8988 0.2256  0.0767  0.0333  319  PHE B CG  
3636  C  CD1 . PHE B 319  ? 1.1823 0.9363 0.9340 0.2169  0.0807  0.0341  319  PHE B CD1 
3637  C  CD2 . PHE B 319  ? 1.1737 0.9127 0.9064 0.2288  0.0800  0.0368  319  PHE B CD2 
3638  C  CE1 . PHE B 319  ? 1.1928 0.9474 0.9577 0.2115  0.0875  0.0381  319  PHE B CE1 
3639  C  CE2 . PHE B 319  ? 1.2838 1.0228 1.0298 0.2229  0.0870  0.0408  319  PHE B CE2 
3640  C  CZ  . PHE B 319  ? 1.2625 1.0097 1.0249 0.2143  0.0906  0.0414  319  PHE B CZ  
3641  N  N   . THR B 320  ? 1.2964 1.0354 1.0096 0.2276  0.0756  0.0288  320  THR B N   
3642  C  CA  . THR B 320  ? 1.3177 1.0551 1.0355 0.2226  0.0817  0.0306  320  THR B CA  
3643  C  C   . THR B 320  ? 1.3531 1.0727 1.0518 0.2289  0.0884  0.0344  320  THR B C   
3644  O  O   . THR B 320  ? 1.2514 0.9647 0.9525 0.2265  0.0976  0.0391  320  THR B O   
3645  C  CB  . THR B 320  ? 1.2445 0.9947 0.9695 0.2177  0.0745  0.0244  320  THR B CB  
3646  O  OG1 . THR B 320  ? 1.2235 0.9899 0.9642 0.2128  0.0677  0.0205  320  THR B OG1 
3647  C  CG2 . THR B 320  ? 1.1974 0.9476 0.9302 0.2117  0.0809  0.0264  320  THR B CG2 
3648  N  N   . GLY B 321  ? 1.6856 1.3971 1.3650 0.2373  0.0840  0.0325  321  GLY B N   
3649  C  CA  . GLY B 321  ? 1.6859 1.3794 1.3454 0.2442  0.0903  0.0362  321  GLY B CA  
3650  C  C   . GLY B 321  ? 1.7386 1.4190 1.3943 0.2466  0.1006  0.0436  321  GLY B C   
3651  O  O   . GLY B 321  ? 1.8160 1.4848 1.4654 0.2476  0.1099  0.0484  321  GLY B O   
3652  N  N   . ALA B 322  ? 1.4394 1.1215 1.0992 0.2476  0.0994  0.0446  322  ALA B N   
3653  C  CA  . ALA B 322  ? 1.4534 1.1233 1.1109 0.2490  0.1094  0.0514  322  ALA B CA  
3654  C  C   . ALA B 322  ? 1.4250 1.1000 1.1016 0.2399  0.1176  0.0550  322  ALA B C   
3655  O  O   . ALA B 322  ? 1.4673 1.1307 1.1408 0.2403  0.1282  0.0609  322  ALA B O   
3656  C  CB  . ALA B 322  ? 1.5089 1.1795 1.1661 0.2520  0.1055  0.0511  322  ALA B CB  
3657  N  N   . LEU B 323  ? 1.3998 1.0920 1.0961 0.2319  0.1130  0.0514  323  LEU B N   
3658  C  CA  . LEU B 323  ? 1.4107 1.1090 1.1255 0.2235  0.1199  0.0543  323  LEU B CA  
3659  C  C   . LEU B 323  ? 1.3460 1.0378 1.0562 0.2232  0.1268  0.0566  323  LEU B C   
3660  O  O   . LEU B 323  ? 1.3618 1.0486 1.0770 0.2208  0.1368  0.0617  323  LEU B O   
3661  C  CB  . LEU B 323  ? 1.3346 1.0523 1.0697 0.2158  0.1128  0.0496  323  LEU B CB  
3662  C  CG  . LEU B 323  ? 1.1367 0.8622 0.8919 0.2073  0.1190  0.0521  323  LEU B CG  
3663  C  CD1 . LEU B 323  ? 1.1427 0.8608 0.9012 0.2069  0.1275  0.0577  323  LEU B CD1 
3664  C  CD2 . LEU B 323  ? 1.2114 0.9553 0.9851 0.2005  0.1115  0.0475  323  LEU B CD2 
3665  N  N   . ALA B 324  ? 0.9477 0.6397 0.6485 0.2257  0.1216  0.0528  324  ALA B N   
3666  C  CA  . ALA B 324  ? 1.0390 0.7233 0.7330 0.2264  0.1279  0.0549  324  ALA B CA  
3667  C  C   . ALA B 324  ? 1.1649 0.8303 0.8412 0.2334  0.1369  0.0606  324  ALA B C   
3668  O  O   . ALA B 324  ? 1.1826 0.8416 0.8589 0.2324  0.1464  0.0648  324  ALA B O   
3669  C  CB  . ALA B 324  ? 1.0399 0.7270 0.7255 0.2280  0.1199  0.0492  324  ALA B CB  
3670  N  N   . ASN B 325  ? 1.6014 1.2575 1.2622 0.2406  0.1345  0.0608  325  ASN B N   
3671  C  CA  . ASN B 325  ? 1.5755 1.2123 1.2177 0.2478  0.1431  0.0663  325  ASN B CA  
3672  C  C   . ASN B 325  ? 1.6171 1.2496 1.2687 0.2443  0.1540  0.0726  325  ASN B C   
3673  O  O   . ASN B 325  ? 1.6934 1.3127 1.3364 0.2468  0.1643  0.0779  325  ASN B O   
3674  C  CB  . ASN B 325  ? 1.6317 1.2599 1.2547 0.2568  0.1369  0.0646  325  ASN B CB  
3675  C  CG  . ASN B 325  ? 1.6900 1.2968 1.2905 0.2654  0.1452  0.0699  325  ASN B CG  
3676  O  OD1 . ASN B 325  ? 1.7391 1.3369 1.3397 0.2654  0.1544  0.0757  325  ASN B OD1 
3677  N  ND2 . ASN B 325  ? 1.6448 1.2431 1.2255 0.2727  0.1420  0.0679  325  ASN B ND2 
3678  N  N   . GLU B 326  ? 1.5325 1.1759 1.2019 0.2384  0.1521  0.0720  326  GLU B N   
3679  C  CA  . GLU B 326  ? 1.5239 1.1635 1.2025 0.2348  0.1619  0.0775  326  GLU B CA  
3680  C  C   . GLU B 326  ? 1.5234 1.1682 1.2169 0.2280  0.1701  0.0802  326  GLU B C   
3681  O  O   . GLU B 326  ? 1.4875 1.1239 1.1819 0.2271  0.1810  0.0857  326  GLU B O   
3682  C  CB  . GLU B 326  ? 1.5138 1.1635 1.2066 0.2306  0.1570  0.0757  326  GLU B CB  
3683  C  CG  . GLU B 326  ? 1.6251 1.2704 1.3271 0.2267  0.1665  0.0809  326  GLU B CG  
3684  C  CD  . GLU B 326  ? 1.7031 1.3444 1.4015 0.2292  0.1637  0.0810  326  GLU B CD  
3685  O  OE1 . GLU B 326  ? 1.7417 1.3856 1.4323 0.2338  0.1537  0.0768  326  GLU B OE1 
3686  O  OE2 . GLU B 326  ? 1.6426 1.2779 1.3459 0.2266  0.1714  0.0851  326  GLU B OE2 
3687  N  N   . LEU B 327  ? 1.3827 1.0410 1.0876 0.2233  0.1651  0.0763  327  LEU B N   
3688  C  CA  . LEU B 327  ? 1.4014 1.0655 1.1203 0.2174  0.1721  0.0785  327  LEU B CA  
3689  C  C   . LEU B 327  ? 1.4283 1.0798 1.1329 0.2220  0.1798  0.0816  327  LEU B C   
3690  O  O   . LEU B 327  ? 1.4737 1.1294 1.1881 0.2182  0.1856  0.0833  327  LEU B O   
3691  C  CB  . LEU B 327  ? 1.4043 1.0859 1.1388 0.2114  0.1642  0.0733  327  LEU B CB  
3692  C  CG  . LEU B 327  ? 1.3070 1.0032 1.0588 0.2057  0.1571  0.0701  327  LEU B CG  
3693  C  CD1 . LEU B 327  ? 1.1151 0.8264 0.8778 0.2011  0.1489  0.0648  327  LEU B CD1 
3694  C  CD2 . LEU B 327  ? 1.2241 0.9243 0.9928 0.1999  0.1644  0.0739  327  LEU B CD2 
3695  N  N   . GLY B 328  ? 1.5784 1.2148 1.2599 0.2305  0.1799  0.0824  328  GLY B N   
3696  C  CA  . GLY B 328  ? 1.5934 1.2169 1.2594 0.2356  0.1868  0.0852  328  GLY B CA  
3697  C  C   . GLY B 328  ? 1.5825 1.2086 1.2414 0.2373  0.1803  0.0807  328  GLY B C   
3698  O  O   . GLY B 328  ? 1.5774 1.1948 1.2263 0.2404  0.1863  0.0828  328  GLY B O   
3699  N  N   . VAL B 329  ? 1.7253 1.3629 1.3891 0.2354  0.1686  0.0745  329  VAL B N   
3700  C  CA  . VAL B 329  ? 1.7795 1.4204 1.4379 0.2361  0.1618  0.0696  329  VAL B CA  
3701  C  C   . VAL B 329  ? 1.8019 1.4365 1.4410 0.2433  0.1530  0.0656  329  VAL B C   
3702  O  O   . VAL B 329  ? 1.8108 1.4436 1.4460 0.2461  0.1498  0.0656  329  VAL B O   
3703  C  CB  . VAL B 329  ? 1.6596 1.3194 1.3392 0.2276  0.1553  0.0652  329  VAL B CB  
3704  C  CG1 . VAL B 329  ? 1.6324 1.2940 1.3072 0.2274  0.1511  0.0611  329  VAL B CG1 
3705  C  CG2 . VAL B 329  ? 1.5233 1.1908 1.2236 0.2207  0.1631  0.0691  329  VAL B CG2 
3706  N  N   . GLY B 330  ? 2.0717 1.7026 1.6983 0.2464  0.1491  0.0622  330  GLY B N   
3707  C  CA  . GLY B 330  ? 2.1541 1.7793 1.7618 0.2534  0.1405  0.0579  330  GLY B CA  
3708  C  C   . GLY B 330  ? 1.8335 1.4713 1.4486 0.2517  0.1291  0.0526  330  GLY B C   
3709  O  O   . GLY B 330  ? 1.8238 1.4770 1.4553 0.2447  0.1231  0.0484  330  GLY B O   
3710  N  N   . GLY B 331  ? 1.3647 0.9958 0.9675 0.2583  0.1263  0.0528  331  GLY B N   
3711  C  CA  . GLY B 331  ? 1.3172 0.9594 0.9253 0.2579  0.1157  0.0479  331  GLY B CA  
3712  C  C   . GLY B 331  ? 1.4721 1.1028 1.0594 0.2680  0.1127  0.0480  331  GLY B C   
3713  O  O   . GLY B 331  ? 1.7289 1.3450 1.2953 0.2755  0.1150  0.0493  331  GLY B O   
3714  N  N   . ALA B 332  ? 1.3830 1.0199 0.9753 0.2686  0.1074  0.0468  332  ALA B N   
3715  C  CA  . ALA B 332  ? 1.4896 1.1165 1.0629 0.2785  0.1040  0.0467  332  ALA B CA  
3716  C  C   . ALA B 332  ? 1.4016 1.0304 0.9827 0.2781  0.1050  0.0493  332  ALA B C   
3717  O  O   . ALA B 332  ? 1.4367 1.0815 1.0363 0.2719  0.0995  0.0461  332  ALA B O   
3718  C  CB  . ALA B 332  ? 1.5118 1.1463 1.0776 0.2823  0.0908  0.0388  332  ALA B CB  
3719  N  N   . PRO B 333  ? 1.3224 0.9346 0.8898 0.2844  0.1123  0.0550  333  PRO B N   
3720  C  CA  . PRO B 333  ? 1.3399 0.9522 0.9129 0.2846  0.1132  0.0573  333  PRO B CA  
3721  C  C   . PRO B 333  ? 1.3335 0.9539 0.9028 0.2894  0.1009  0.0516  333  PRO B C   
3722  O  O   . PRO B 333  ? 1.3632 0.9818 0.9172 0.2964  0.0935  0.0475  333  PRO B O   
3723  C  CB  . PRO B 333  ? 1.4595 1.0495 1.0138 0.2916  0.1238  0.0645  333  PRO B CB  
3724  C  CG  . PRO B 333  ? 1.4418 1.0228 0.9881 0.2920  0.1310  0.0670  333  PRO B CG  
3725  C  CD  . PRO B 333  ? 1.4171 1.0091 0.9637 0.2913  0.1211  0.0601  333  PRO B CD  
3726  N  N   . ALA B 334  ? 1.3398 0.9694 0.9234 0.2857  0.0986  0.0512  334  ALA B N   
3727  C  CA  . ALA B 334  ? 1.4932 1.1325 1.0764 0.2895  0.0872  0.0459  334  ALA B CA  
3728  C  C   . ALA B 334  ? 1.4787 1.1114 1.0605 0.2925  0.0901  0.0495  334  ALA B C   
3729  O  O   . ALA B 334  ? 1.4137 1.0441 1.0070 0.2866  0.0984  0.0542  334  ALA B O   
3730  C  CB  . ALA B 334  ? 1.4288 1.0912 1.0345 0.2806  0.0789  0.0397  334  ALA B CB  
3731  N  N   . THR B 335  ? 1.8930 1.5226 1.4606 0.3019  0.0830  0.0472  335  THR B N   
3732  C  CA  . THR B 335  ? 1.9763 1.6001 1.5415 0.3056  0.0842  0.0499  335  THR B CA  
3733  C  C   . THR B 335  ? 1.8676 1.5112 1.4561 0.2980  0.0782  0.0461  335  THR B C   
3734  O  O   . THR B 335  ? 1.8309 1.4899 1.4243 0.2987  0.0671  0.0395  335  THR B O   
3735  C  CB  . THR B 335  ? 2.0017 1.6159 1.5432 0.3190  0.0782  0.0484  335  THR B CB  
3736  O  OG1 . THR B 335  ? 2.0586 1.6883 1.6010 0.3210  0.0655  0.0406  335  THR B OG1 
3737  C  CG2 . THR B 335  ? 1.9286 1.5203 1.4457 0.3269  0.0858  0.0533  335  THR B CG2 
3738  N  N   . LEU B 336  ? 1.7161 1.3596 1.3191 0.2907  0.0856  0.0501  336  LEU B N   
3739  C  CA  . LEU B 336  ? 1.6623 1.3239 1.2882 0.2827  0.0812  0.0470  336  LEU B CA  
3740  C  C   . LEU B 336  ? 1.6807 1.3348 1.3072 0.2839  0.0851  0.0506  336  LEU B C   
3741  O  O   . LEU B 336  ? 1.7403 1.3750 1.3521 0.2890  0.0931  0.0562  336  LEU B O   
3742  C  CB  . LEU B 336  ? 1.5471 1.2191 1.1939 0.2707  0.0855  0.0474  336  LEU B CB  
3743  C  CG  . LEU B 336  ? 1.4867 1.1688 1.1363 0.2679  0.0806  0.0430  336  LEU B CG  
3744  C  CD1 . LEU B 336  ? 1.4717 1.1633 1.1418 0.2566  0.0854  0.0438  336  LEU B CD1 
3745  C  CD2 . LEU B 336  ? 1.3721 1.0700 1.0243 0.2699  0.0676  0.0354  336  LEU B CD2 
3746  N  N   . SER B 337  ? 1.3588 1.0281 1.0023 0.2791  0.0796  0.0474  337  SER B N   
3747  C  CA  . SER B 337  ? 1.3646 1.0286 1.0105 0.2795  0.0825  0.0501  337  SER B CA  
3748  C  C   . SER B 337  ? 1.3779 1.0332 1.0324 0.2719  0.0947  0.0561  337  SER B C   
3749  O  O   . SER B 337  ? 1.4373 1.0971 1.1023 0.2645  0.0991  0.0570  337  SER B O   
3750  C  CB  . SER B 337  ? 1.4646 1.1484 1.1279 0.2755  0.0736  0.0448  337  SER B CB  
3751  O  OG  . SER B 337  ? 1.4043 1.1011 1.0907 0.2637  0.0758  0.0443  337  SER B OG  
3752  N  N   . PRO B 338  ? 1.5246 1.1670 1.1744 0.2738  0.1004  0.0602  338  PRO B N   
3753  C  CA  . PRO B 338  ? 1.5392 1.1745 1.1988 0.2658  0.1119  0.0655  338  PRO B CA  
3754  C  C   . PRO B 338  ? 1.5400 1.1940 1.2264 0.2539  0.1109  0.0632  338  PRO B C   
3755  O  O   . PRO B 338  ? 1.5247 1.1776 1.2211 0.2464  0.1191  0.0664  338  PRO B O   
3756  C  CB  . PRO B 338  ? 1.5707 1.1910 1.2207 0.2704  0.1156  0.0688  338  PRO B CB  
3757  C  CG  . PRO B 338  ? 1.5540 1.1661 1.1813 0.2832  0.1094  0.0674  338  PRO B CG  
3758  C  CD  . PRO B 338  ? 1.5566 1.1885 1.1900 0.2838  0.0975  0.0605  338  PRO B CD  
3759  N  N   . LYS B 339  ? 1.4863 1.1575 1.1846 0.2521  0.1012  0.0579  339  LYS B N   
3760  C  CA  . LYS B 339  ? 1.4330 1.1224 1.1559 0.2412  0.0997  0.0554  339  LYS B CA  
3761  C  C   . LYS B 339  ? 1.4206 1.1187 1.1497 0.2368  0.0995  0.0540  339  LYS B C   
3762  O  O   . LYS B 339  ? 1.4648 1.1685 1.2092 0.2281  0.1046  0.0554  339  LYS B O   
3763  C  CB  . LYS B 339  ? 1.6237 1.3292 1.3562 0.2410  0.0893  0.0499  339  LYS B CB  
3764  C  CG  . LYS B 339  ? 1.8059 1.5085 1.5436 0.2398  0.0908  0.0512  339  LYS B CG  
3765  C  CD  . LYS B 339  ? 1.6725 1.3950 1.4275 0.2354  0.0823  0.0459  339  LYS B CD  
3766  C  CE  . LYS B 339  ? 1.6934 1.4135 1.4559 0.2327  0.0847  0.0472  339  LYS B CE  
3767  N  NZ  . LYS B 339  ? 1.9392 1.6577 1.6921 0.2409  0.0782  0.0450  339  LYS B NZ  
3768  N  N   . ALA B 340  ? 1.1321 0.8313 0.8492 0.2428  0.0935  0.0511  340  ALA B N   
3769  C  CA  . ALA B 340  ? 1.0384 0.7438 0.7591 0.2392  0.0935  0.0497  340  ALA B CA  
3770  C  C   . ALA B 340  ? 1.1348 0.8254 0.8486 0.2387  0.1048  0.0555  340  ALA B C   
3771  O  O   . ALA B 340  ? 1.1053 0.8013 0.8283 0.2327  0.1079  0.0558  340  ALA B O   
3772  C  CB  . ALA B 340  ? 0.9898 0.6988 0.6980 0.2461  0.0845  0.0450  340  ALA B CB  
3773  N  N   . GLU B 341  ? 1.7230 1.3946 1.4205 0.2449  0.1113  0.0603  341  GLU B N   
3774  C  CA  . GLU B 341  ? 1.6899 1.3469 1.3811 0.2442  0.1229  0.0661  341  GLU B CA  
3775  C  C   . GLU B 341  ? 1.6693 1.3306 1.3803 0.2341  0.1306  0.0690  341  GLU B C   
3776  O  O   . GLU B 341  ? 1.6737 1.3351 1.3907 0.2294  0.1373  0.0713  341  GLU B O   
3777  C  CB  . GLU B 341  ? 1.8966 1.5318 1.5652 0.2534  0.1281  0.0705  341  GLU B CB  
3778  C  CG  . GLU B 341  ? 1.9359 1.5551 1.5909 0.2561  0.1380  0.0755  341  GLU B CG  
3779  C  CD  . GLU B 341  ? 1.9778 1.5941 1.6156 0.2638  0.1328  0.0731  341  GLU B CD  
3780  O  OE1 . GLU B 341  ? 1.9466 1.5715 1.5809 0.2680  0.1217  0.0678  341  GLU B OE1 
3781  O  OE2 . GLU B 341  ? 2.1173 1.7229 1.7453 0.2655  0.1399  0.0764  341  GLU B OE2 
3782  N  N   . GLU B 342  ? 1.5631 1.2281 1.2844 0.2308  0.1298  0.0688  342  GLU B N   
3783  C  CA  . GLU B 342  ? 1.5767 1.2474 1.3179 0.2210  0.1360  0.0707  342  GLU B CA  
3784  C  C   . GLU B 342  ? 1.4956 1.1863 1.2565 0.2132  0.1316  0.0670  342  GLU B C   
3785  O  O   . GLU B 342  ? 1.4443 1.1392 1.2195 0.2057  0.1378  0.0690  342  GLU B O   
3786  C  CB  . GLU B 342  ? 1.5351 1.2053 1.2819 0.2197  0.1350  0.0707  342  GLU B CB  
3787  C  CG  . GLU B 342  ? 1.6808 1.3294 1.4113 0.2250  0.1427  0.0756  342  GLU B CG  
3788  C  CD  . GLU B 342  ? 1.8298 1.4777 1.5675 0.2224  0.1427  0.0757  342  GLU B CD  
3789  O  OE1 . GLU B 342  ? 1.8599 1.5243 1.6141 0.2173  0.1360  0.0716  342  GLU B OE1 
3790  O  OE2 . GLU B 342  ? 1.8052 1.4352 1.5314 0.2254  0.1497  0.0799  342  GLU B OE2 
3791  N  N   . PHE B 343  ? 1.3941 1.0973 1.1562 0.2148  0.1210  0.0616  343  PHE B N   
3792  C  CA  . PHE B 343  ? 1.3157 1.0367 1.0948 0.2078  0.1168  0.0580  343  PHE B CA  
3793  C  C   . PHE B 343  ? 1.3454 1.0638 1.1208 0.2073  0.1211  0.0594  343  PHE B C   
3794  O  O   . PHE B 343  ? 1.3381 1.0651 1.1283 0.2002  0.1240  0.0596  343  PHE B O   
3795  C  CB  . PHE B 343  ? 1.3313 1.0655 1.1118 0.2097  0.1047  0.0518  343  PHE B CB  
3796  C  CG  . PHE B 343  ? 1.2240 0.9774 1.0252 0.2015  0.1001  0.0480  343  PHE B CG  
3797  C  CD1 . PHE B 343  ? 1.1825 0.9442 0.9993 0.1961  0.0995  0.0475  343  PHE B CD1 
3798  C  CD2 . PHE B 343  ? 1.3005 1.0629 1.1048 0.1994  0.0965  0.0450  343  PHE B CD2 
3799  C  CE1 . PHE B 343  ? 1.1395 0.9182 0.9744 0.1889  0.0953  0.0441  343  PHE B CE1 
3800  C  CE2 . PHE B 343  ? 1.3127 1.0917 1.1350 0.1920  0.0925  0.0417  343  PHE B CE2 
3801  C  CZ  . PHE B 343  ? 1.2068 0.9941 1.0444 0.1870  0.0920  0.0414  343  PHE B CZ  
3802  N  N   . LEU B 344  ? 1.0499 0.7563 0.8051 0.2152  0.1214  0.0602  344  LEU B N   
3803  C  CA  . LEU B 344  ? 0.9548 0.6558 0.7040 0.2155  0.1267  0.0622  344  LEU B CA  
3804  C  C   . LEU B 344  ? 1.0521 0.7453 0.8068 0.2115  0.1389  0.0680  344  LEU B C   
3805  O  O   . LEU B 344  ? 1.0005 0.6975 0.7627 0.2073  0.1432  0.0690  344  LEU B O   
3806  C  CB  . LEU B 344  ? 1.1211 0.8084 0.8459 0.2255  0.1254  0.0624  344  LEU B CB  
3807  C  CG  . LEU B 344  ? 1.1724 0.8672 0.8900 0.2299  0.1138  0.0563  344  LEU B CG  
3808  C  CD1 . LEU B 344  ? 1.2025 0.8816 0.8949 0.2405  0.1134  0.0572  344  LEU B CD1 
3809  C  CD2 . LEU B 344  ? 1.1355 0.8415 0.8616 0.2249  0.1110  0.0531  344  LEU B CD2 
3810  N  N   . ARG B 345  ? 1.5146 1.1968 1.2655 0.2128  0.1447  0.0718  345  ARG B N   
3811  C  CA  . ARG B 345  ? 1.5665 1.2417 1.3235 0.2084  0.1565  0.0772  345  ARG B CA  
3812  C  C   . ARG B 345  ? 1.5407 1.2322 1.3225 0.1984  0.1572  0.0761  345  ARG B C   
3813  O  O   . ARG B 345  ? 1.5176 1.2105 1.3062 0.1947  0.1639  0.0783  345  ARG B O   
3814  C  CB  . ARG B 345  ? 1.6157 1.2777 1.3663 0.2106  0.1615  0.0806  345  ARG B CB  
3815  C  CG  . ARG B 345  ? 1.7883 1.4355 1.5345 0.2098  0.1749  0.0869  345  ARG B CG  
3816  C  CD  . ARG B 345  ? 1.8261 1.4592 1.5515 0.2172  0.1791  0.0895  345  ARG B CD  
3817  N  NE  . ARG B 345  ? 1.8067 1.4313 1.5114 0.2269  0.1722  0.0877  345  ARG B NE  
3818  C  CZ  . ARG B 345  ? 1.7861 1.3941 1.4742 0.2333  0.1751  0.0906  345  ARG B CZ  
3819  N  NH1 . ARG B 345  ? 1.7728 1.3699 1.4622 0.2308  0.1852  0.0954  345  ARG B NH1 
3820  N  NH2 . ARG B 345  ? 1.7433 1.3454 1.4130 0.2426  0.1678  0.0884  345  ARG B NH2 
3821  N  N   . ALA B 346  ? 1.3323 1.0364 1.1275 0.1944  0.1503  0.0725  346  ALA B N   
3822  C  CA  . ALA B 346  ? 1.2821 1.0013 1.1005 0.1853  0.1508  0.0715  346  ALA B CA  
3823  C  C   . ALA B 346  ? 1.2489 0.9803 1.0748 0.1826  0.1473  0.0687  346  ALA B C   
3824  O  O   . ALA B 346  ? 1.2473 0.9852 1.0867 0.1768  0.1521  0.0700  346  ALA B O   
3825  C  CB  . ALA B 346  ? 1.2525 0.9813 1.0817 0.1824  0.1439  0.0682  346  ALA B CB  
3826  N  N   . ILE B 347  ? 1.2093 0.9440 1.0265 0.1867  0.1389  0.0648  347  ILE B N   
3827  C  CA  . ILE B 347  ? 1.1513 0.8956 0.9733 0.1844  0.1358  0.0622  347  ILE B CA  
3828  C  C   . ILE B 347  ? 1.1876 0.9234 1.0044 0.1852  0.1449  0.0662  347  ILE B C   
3829  O  O   . ILE B 347  ? 1.2737 1.0174 1.1026 0.1802  0.1476  0.0664  347  ILE B O   
3830  C  CB  . ILE B 347  ? 1.0560 0.8031 0.8672 0.1892  0.1259  0.0574  347  ILE B CB  
3831  C  CG1 . ILE B 347  ? 1.0355 0.7952 0.8561 0.1870  0.1167  0.0528  347  ILE B CG1 
3832  C  CG2 . ILE B 347  ? 0.9174 0.6697 0.7292 0.1878  0.1245  0.0554  347  ILE B CG2 
3833  C  CD1 . ILE B 347  ? 0.9787 0.7446 0.7925 0.1902  0.1068  0.0475  347  ILE B CD1 
3834  N  N   . ALA B 348  ? 1.1078 0.8271 0.9060 0.1918  0.1498  0.0694  348  ALA B N   
3835  C  CA  . ALA B 348  ? 1.1258 0.8359 0.9175 0.1932  0.1589  0.0734  348  ALA B CA  
3836  C  C   . ALA B 348  ? 1.1489 0.8602 0.9550 0.1873  0.1687  0.0776  348  ALA B C   
3837  O  O   . ALA B 348  ? 1.1856 0.8976 0.9956 0.1855  0.1748  0.0796  348  ALA B O   
3838  C  CB  . ALA B 348  ? 1.2707 0.9622 1.0385 0.2019  0.1621  0.0761  348  ALA B CB  
3839  N  N   . ARG B 349  ? 1.3745 1.0859 1.1886 0.1842  0.1705  0.0788  349  ARG B N   
3840  C  CA  . ARG B 349  ? 1.4470 1.1596 1.2751 0.1783  0.1799  0.0825  349  ARG B CA  
3841  C  C   . ARG B 349  ? 1.3947 1.1258 1.2453 0.1707  0.1774  0.0800  349  ARG B C   
3842  O  O   . ARG B 349  ? 1.4205 1.1548 1.2814 0.1668  0.1846  0.0825  349  ARG B O   
3843  C  CB  . ARG B 349  ? 1.4472 1.1527 1.2758 0.1775  0.1830  0.0845  349  ARG B CB  
3844  C  CG  . ARG B 349  ? 1.5292 1.2141 1.3359 0.1847  0.1884  0.0882  349  ARG B CG  
3845  C  CD  . ARG B 349  ? 1.6318 1.3067 1.4280 0.1879  0.1970  0.0921  349  ARG B CD  
3846  N  NE  . ARG B 349  ? 1.6541 1.3217 1.4303 0.1960  0.1923  0.0907  349  ARG B NE  
3847  C  CZ  . ARG B 349  ? 1.6240 1.2858 1.3906 0.1994  0.1966  0.0924  349  ARG B CZ  
3848  N  NH1 . ARG B 349  ? 1.6421 1.3046 1.4172 0.1957  0.2061  0.0958  349  ARG B NH1 
3849  N  NH2 . ARG B 349  ? 1.5868 1.2421 1.3350 0.2067  0.1914  0.0906  349  ARG B NH2 
3850  N  N   . ASP B 350  ? 1.7020 1.4454 1.5606 0.1685  0.1674  0.0753  350  ASP B N   
3851  C  CA  . ASP B 350  ? 1.6609 1.4214 1.5392 0.1619  0.1645  0.0728  350  ASP B CA  
3852  C  C   . ASP B 350  ? 1.7035 1.4673 1.5798 0.1628  0.1644  0.0721  350  ASP B C   
3853  O  O   . ASP B 350  ? 1.7999 1.5718 1.6893 0.1585  0.1679  0.0728  350  ASP B O   
3854  C  CB  . ASP B 350  ? 1.5959 1.3678 1.4818 0.1597  0.1541  0.0680  350  ASP B CB  
3855  C  CG  . ASP B 350  ? 1.6983 1.4705 1.5923 0.1567  0.1549  0.0686  350  ASP B CG  
3856  O  OD1 . ASP B 350  ? 1.7472 1.5100 1.6400 0.1562  0.1634  0.0726  350  ASP B OD1 
3857  O  OD2 . ASP B 350  ? 1.6479 1.4296 1.5492 0.1547  0.1472  0.0649  350  ASP B OD2 
3858  N  N   . LEU B 351  ? 1.1521 0.9092 1.0115 0.1687  0.1603  0.0706  351  LEU B N   
3859  C  CA  . LEU B 351  ? 1.0710 0.8263 0.9244 0.1706  0.1623  0.0709  351  LEU B CA  
3860  C  C   . LEU B 351  ? 1.2306 0.9747 1.0789 0.1724  0.1740  0.0764  351  LEU B C   
3861  O  O   . LEU B 351  ? 1.2610 0.9975 1.1083 0.1725  0.1800  0.0797  351  LEU B O   
3862  C  CB  . LEU B 351  ? 1.0311 0.7806 0.8665 0.1766  0.1554  0.0678  351  LEU B CB  
3863  C  CG  . LEU B 351  ? 0.8663 0.6277 0.7066 0.1749  0.1439  0.0621  351  LEU B CG  
3864  C  CD1 . LEU B 351  ? 0.7357 0.4913 0.5581 0.1809  0.1376  0.0590  351  LEU B CD1 
3865  C  CD2 . LEU B 351  ? 1.0475 0.8232 0.9042 0.1687  0.1419  0.0599  351  LEU B CD2 
3866  N  N   . GLU B 352  ? 1.7183 1.4614 1.5638 0.1735  0.1776  0.0773  352  GLU B N   
3867  C  CA  . GLU B 352  ? 1.8082 1.5419 1.6495 0.1752  0.1890  0.0824  352  GLU B CA  
3868  C  C   . GLU B 352  ? 1.7278 1.4697 1.5890 0.1689  0.1959  0.0849  352  GLU B C   
3869  O  O   . GLU B 352  ? 1.8305 1.5702 1.6942 0.1687  0.2048  0.0884  352  GLU B O   
3870  C  CB  . GLU B 352  ? 1.9048 1.6207 1.7269 0.1814  0.1935  0.0855  352  GLU B CB  
3871  C  CG  . GLU B 352  ? 1.9398 1.6455 1.7401 0.1887  0.1893  0.0840  352  GLU B CG  
3872  C  CD  . GLU B 352  ? 2.0297 1.7176 1.8106 0.1952  0.1936  0.0872  352  GLU B CD  
3873  O  OE1 . GLU B 352  ? 2.0113 1.6963 1.7954 0.1939  0.1959  0.0890  352  GLU B OE1 
3874  O  OE2 . GLU B 352  ? 2.0960 1.7724 1.8581 0.2018  0.1946  0.0878  352  GLU B OE2 
3875  N  N   . GLU B 353  ? 1.2757 1.0270 1.1510 0.1638  0.1919  0.0831  353  GLU B N   
3876  C  CA  . GLU B 353  ? 1.3770 1.1388 1.2731 0.1571  0.1964  0.0843  353  GLU B CA  
3877  C  C   . GLU B 353  ? 1.2032 0.9822 1.1154 0.1526  0.1902  0.0807  353  GLU B C   
3878  O  O   . GLU B 353  ? 1.0955 0.8847 1.0253 0.1475  0.1935  0.0813  353  GLU B O   
3879  C  CB  . GLU B 353  ? 1.4433 1.2037 1.3447 0.1543  0.1966  0.0847  353  GLU B CB  
3880  C  CG  . GLU B 353  ? 1.5100 1.2772 1.4300 0.1479  0.2036  0.0868  353  GLU B CG  
3881  C  CD  . GLU B 353  ? 1.6361 1.4021 1.5611 0.1448  0.2025  0.0865  353  GLU B CD  
3882  O  OE1 . GLU B 353  ? 1.6168 1.3794 1.5331 0.1473  0.1952  0.0842  353  GLU B OE1 
3883  O  OE2 . GLU B 353  ? 1.7537 1.5222 1.6914 0.1398  0.2091  0.0884  353  GLU B OE2 
3884  N  N   . HIS B 354  ? 1.5979 1.3800 1.5041 0.1545  0.1813  0.0768  354  HIS B N   
3885  C  CA  . HIS B 354  ? 1.7136 1.5103 1.6324 0.1508  0.1753  0.0733  354  HIS B CA  
3886  C  C   . HIS B 354  ? 1.6754 1.4686 1.5820 0.1548  0.1729  0.0720  354  HIS B C   
3887  O  O   . HIS B 354  ? 1.6375 1.4330 1.5388 0.1556  0.1645  0.0680  354  HIS B O   
3888  C  CB  . HIS B 354  ? 1.6431 1.4486 1.5688 0.1479  0.1659  0.0693  354  HIS B CB  
3889  C  CG  . HIS B 354  ? 1.6802 1.4901 1.6189 0.1435  0.1677  0.0701  354  HIS B CG  
3890  N  ND1 . HIS B 354  ? 1.6749 1.4765 1.6067 0.1450  0.1675  0.0708  354  HIS B ND1 
3891  C  CD2 . HIS B 354  ? 1.6805 1.5017 1.6382 0.1379  0.1695  0.0702  354  HIS B CD2 
3892  C  CE1 . HIS B 354  ? 1.6866 1.4938 1.6326 0.1401  0.1694  0.0713  354  HIS B CE1 
3893  N  NE2 . HIS B 354  ? 1.7231 1.5426 1.6851 0.1357  0.1704  0.0709  354  HIS B NE2 
3894  N  N   . ARG B 355  ? 1.5222 1.3097 1.4245 0.1571  0.1807  0.0751  355  ARG B N   
3895  C  CA  . ARG B 355  ? 1.4668 1.2489 1.3561 0.1612  0.1797  0.0742  355  ARG B CA  
3896  C  C   . ARG B 355  ? 1.5193 1.3134 1.4203 0.1579  0.1769  0.0720  355  ARG B C   
3897  O  O   . ARG B 355  ? 1.6358 1.4381 1.5516 0.1548  0.1816  0.0737  355  ARG B O   
3898  C  CB  . ARG B 355  ? 1.5172 1.2868 1.3954 0.1657  0.1896  0.0787  355  ARG B CB  
3899  C  CG  . ARG B 355  ? 1.6939 1.4488 1.5557 0.1703  0.1920  0.0807  355  ARG B CG  
3900  C  CD  . ARG B 355  ? 1.8049 1.5469 1.6543 0.1751  0.2018  0.0851  355  ARG B CD  
3901  N  NE  . ARG B 355  ? 1.8437 1.5704 1.6755 0.1802  0.2039  0.0871  355  ARG B NE  
3902  C  CZ  . ARG B 355  ? 1.8631 1.5788 1.6746 0.1863  0.2005  0.0858  355  ARG B CZ  
3903  N  NH1 . ARG B 355  ? 1.7699 1.4877 1.5759 0.1878  0.1948  0.0824  355  ARG B NH1 
3904  N  NH2 . ARG B 355  ? 1.8044 1.5064 1.6004 0.1911  0.2028  0.0879  355  ARG B NH2 
3905  N  N   . GLY B 356  ? 1.1872 0.9822 1.0813 0.1589  0.1694  0.0681  356  GLY B N   
3906  C  CA  . GLY B 356  ? 1.1181 0.9242 1.0226 0.1555  0.1654  0.0654  356  GLY B CA  
3907  C  C   . GLY B 356  ? 1.1601 0.9795 1.0805 0.1500  0.1594  0.0628  356  GLY B C   
3908  O  O   . GLY B 356  ? 1.1267 0.9554 1.0554 0.1472  0.1554  0.0604  356  GLY B O   
3909  N  N   . GLN B 357  ? 1.2492 1.0694 1.1737 0.1487  0.1589  0.0634  357  GLN B N   
3910  C  CA  . GLN B 357  ? 1.2389 1.0707 1.1772 0.1440  0.1529  0.0608  357  GLN B CA  
3911  C  C   . GLN B 357  ? 1.2100 1.0387 1.1397 0.1453  0.1458  0.0580  357  GLN B C   
3912  O  O   . GLN B 357  ? 1.2710 1.1057 1.2092 0.1425  0.1424  0.0568  357  GLN B O   
3913  C  CB  . GLN B 357  ? 1.2484 1.0849 1.2010 0.1407  0.1583  0.0636  357  GLN B CB  
3914  C  CG  . GLN B 357  ? 1.1785 1.0223 1.1436 0.1386  0.1639  0.0655  357  GLN B CG  
3915  C  CD  . GLN B 357  ? 1.3076 1.1563 1.2869 0.1353  0.1695  0.0680  357  GLN B CD  
3916  O  OE1 . GLN B 357  ? 1.4742 1.3187 1.4525 0.1347  0.1702  0.0687  357  GLN B OE1 
3917  N  NE2 . GLN B 357  ? 1.2369 1.0942 1.2293 0.1332  0.1735  0.0691  357  GLN B NE2 
3918  N  N   . SER B 358  ? 0.8316 0.6513 0.7445 0.1497  0.1433  0.0567  358  SER B N   
3919  C  CA  . SER B 358  ? 0.7878 0.6040 0.6909 0.1519  0.1368  0.0541  358  SER B CA  
3920  C  C   . SER B 358  ? 0.8611 0.6771 0.7545 0.1534  0.1302  0.0499  358  SER B C   
3921  O  O   . SER B 358  ? 0.9450 0.7600 0.8360 0.1536  0.1317  0.0497  358  SER B O   
3922  C  CB  . SER B 358  ? 0.8982 0.7004 0.7875 0.1570  0.1416  0.0572  358  SER B CB  
3923  O  OG  . SER B 358  ? 0.8042 0.5960 0.6815 0.1610  0.1474  0.0597  358  SER B OG  
3924  N  N   . VAL B 359  ? 1.1438 0.9608 1.0320 0.1545  0.1227  0.0465  359  VAL B N   
3925  C  CA  . VAL B 359  ? 1.1142 0.9315 0.9932 0.1558  0.1157  0.0420  359  VAL B CA  
3926  C  C   . VAL B 359  ? 1.1841 0.9981 1.0531 0.1594  0.1100  0.0397  359  VAL B C   
3927  O  O   . VAL B 359  ? 1.2656 1.0834 1.1405 0.1587  0.1082  0.0398  359  VAL B O   
3928  C  CB  . VAL B 359  ? 1.0290 0.8593 0.9204 0.1502  0.1105  0.0383  359  VAL B CB  
3929  C  CG1 . VAL B 359  ? 1.0946 0.9356 0.9983 0.1468  0.1056  0.0365  359  VAL B CG1 
3930  C  CG2 . VAL B 359  ? 1.0620 0.8914 0.9436 0.1510  0.1045  0.0338  359  VAL B CG2 
3931  N  N   . VAL B 360  ? 0.8533 0.6599 0.7065 0.1637  0.1072  0.0376  360  VAL B N   
3932  C  CA  . VAL B 360  ? 0.7399 0.5440 0.5823 0.1679  0.1008  0.0347  360  VAL B CA  
3933  C  C   . VAL B 360  ? 0.8267 0.6385 0.6685 0.1660  0.0923  0.0287  360  VAL B C   
3934  O  O   . VAL B 360  ? 0.9211 0.7297 0.7566 0.1660  0.0924  0.0273  360  VAL B O   
3935  C  CB  . VAL B 360  ? 0.9245 0.7131 0.7478 0.1752  0.1045  0.0372  360  VAL B CB  
3936  C  CG1 . VAL B 360  ? 0.9270 0.7137 0.7387 0.1800  0.0970  0.0338  360  VAL B CG1 
3937  C  CG2 . VAL B 360  ? 0.9092 0.6900 0.7335 0.1765  0.1136  0.0433  360  VAL B CG2 
3938  N  N   . ILE B 361  ? 0.8231 0.6449 0.6715 0.1642  0.0851  0.0250  361  ILE B N   
3939  C  CA  . ILE B 361  ? 0.8847 0.7161 0.7356 0.1613  0.0771  0.0191  361  ILE B CA  
3940  C  C   . ILE B 361  ? 0.8739 0.7040 0.7133 0.1662  0.0701  0.0154  361  ILE B C   
3941  O  O   . ILE B 361  ? 0.8366 0.6661 0.6749 0.1694  0.0690  0.0164  361  ILE B O   
3942  C  CB  . ILE B 361  ? 0.8627 0.7084 0.7320 0.1549  0.0743  0.0175  361  ILE B CB  
3943  C  CG1 . ILE B 361  ? 0.8639 0.7106 0.7445 0.1510  0.0815  0.0217  361  ILE B CG1 
3944  C  CG2 . ILE B 361  ? 0.8197 0.6745 0.6918 0.1511  0.0675  0.0117  361  ILE B CG2 
3945  C  CD1 . ILE B 361  ? 0.8049 0.6650 0.7028 0.1449  0.0791  0.0202  361  ILE B CD1 
3946  N  N   . ALA B 362  ? 1.0931 0.9228 0.9239 0.1669  0.0654  0.0111  362  ALA B N   
3947  C  CA  . ALA B 362  ? 1.1021 0.9322 0.9223 0.1715  0.0580  0.0067  362  ALA B CA  
3948  C  C   . ALA B 362  ? 1.1151 0.9598 0.9447 0.1665  0.0499  0.0004  362  ALA B C   
3949  O  O   . ALA B 362  ? 1.0395 0.8886 0.8748 0.1610  0.0496  -0.0017 362  ALA B O   
3950  C  CB  . ALA B 362  ? 1.0629 0.8809 0.8648 0.1765  0.0585  0.0061  362  ALA B CB  
3951  N  N   . GLY B 363  ? 1.0688 0.9207 0.8997 0.1686  0.0435  -0.0025 363  GLY B N   
3952  C  CA  . GLY B 363  ? 1.0565 0.9231 0.8968 0.1640  0.0360  -0.0085 363  GLY B CA  
3953  C  C   . GLY B 363  ? 1.0499 0.9171 0.8814 0.1643  0.0305  -0.0142 363  GLY B C   
3954  O  O   . GLY B 363  ? 1.0656 0.9227 0.8815 0.1700  0.0303  -0.0143 363  GLY B O   
3955  N  N   . ASP B 364  ? 0.9833 0.8624 0.8248 0.1578  0.0261  -0.0190 364  ASP B N   
3956  C  CA  . ASP B 364  ? 0.9670 0.8482 0.8018 0.1567  0.0205  -0.0252 364  ASP B CA  
3957  C  C   . ASP B 364  ? 1.0061 0.8896 0.8317 0.1630  0.0132  -0.0292 364  ASP B C   
3958  O  O   . ASP B 364  ? 1.0590 0.9394 0.8735 0.1651  0.0093  -0.0333 364  ASP B O   
3959  C  CB  . ASP B 364  ? 0.9490 0.8432 0.7976 0.1482  0.0175  -0.0295 364  ASP B CB  
3960  C  CG  . ASP B 364  ? 0.9825 0.8746 0.8399 0.1423  0.0243  -0.0257 364  ASP B CG  
3961  O  OD1 . ASP B 364  ? 0.9511 0.8327 0.8048 0.1449  0.0312  -0.0199 364  ASP B OD1 
3962  O  OD2 . ASP B 364  ? 1.0409 0.9420 0.9088 0.1354  0.0228  -0.0286 364  ASP B OD2 
3963  N  N   . GLN B 365  ? 1.2907 1.1795 1.1202 0.1665  0.0111  -0.0283 365  GLN B N   
3964  C  CA  . GLN B 365  ? 1.3189 1.2103 1.1396 0.1733  0.0041  -0.0320 365  GLN B CA  
3965  C  C   . GLN B 365  ? 1.3891 1.2645 1.1906 0.1820  0.0063  -0.0291 365  GLN B C   
3966  O  O   . GLN B 365  ? 1.4899 1.3648 1.2799 0.1875  0.0003  -0.0331 365  GLN B O   
3967  C  CB  . GLN B 365  ? 1.3301 1.2306 1.1599 0.1749  0.0017  -0.0314 365  GLN B CB  
3968  C  CG  . GLN B 365  ? 1.2936 1.1876 1.1285 0.1748  0.0094  -0.0243 365  GLN B CG  
3969  C  CD  . GLN B 365  ? 1.4394 1.3443 1.2930 0.1666  0.0110  -0.0239 365  GLN B CD  
3970  O  OE1 . GLN B 365  ? 1.5968 1.5097 1.4581 0.1600  0.0092  -0.0275 365  GLN B OE1 
3971  N  NE2 . GLN B 365  ? 1.3817 1.2863 1.2420 0.1671  0.0146  -0.0197 365  GLN B NE2 
3972  N  N   . GLN B 366  ? 1.1244 0.9869 0.9221 0.1834  0.0149  -0.0223 366  GLN B N   
3973  C  CA  . GLN B 366  ? 1.0873 0.9338 0.8668 0.1917  0.0180  -0.0188 366  GLN B CA  
3974  C  C   . GLN B 366  ? 1.1968 1.0362 0.9631 0.1930  0.0167  -0.0218 366  GLN B C   
3975  O  O   . GLN B 366  ? 1.2994 1.1425 1.0714 0.1863  0.0166  -0.0243 366  GLN B O   
3976  C  CB  . GLN B 366  ? 1.0870 0.9224 0.8673 0.1919  0.0282  -0.0108 366  GLN B CB  
3977  C  CG  . GLN B 366  ? 1.1110 0.9489 0.8987 0.1934  0.0298  -0.0074 366  GLN B CG  
3978  C  CD  . GLN B 366  ? 1.1548 0.9892 0.9302 0.2023  0.0253  -0.0084 366  GLN B CD  
3979  O  OE1 . GLN B 366  ? 1.1695 0.9913 0.9274 0.2094  0.0263  -0.0072 366  GLN B OE1 
3980  N  NE2 . GLN B 366  ? 1.2023 1.0476 0.9863 0.2024  0.0204  -0.0105 366  GLN B NE2 
3981  N  N   . PRO B 367  ? 1.0044 0.8328 0.7523 0.2015  0.0156  -0.0215 367  PRO B N   
3982  C  CA  . PRO B 367  ? 0.9289 0.7505 0.6630 0.2034  0.0133  -0.0250 367  PRO B CA  
3983  C  C   . PRO B 367  ? 0.9315 0.7425 0.6637 0.1999  0.0216  -0.0211 367  PRO B C   
3984  O  O   . PRO B 367  ? 0.9517 0.7585 0.6906 0.1979  0.0297  -0.0149 367  PRO B O   
3985  C  CB  . PRO B 367  ? 0.9456 0.7561 0.6601 0.2145  0.0118  -0.0239 367  PRO B CB  
3986  C  CG  . PRO B 367  ? 1.0252 0.8426 0.7457 0.2175  0.0093  -0.0230 367  PRO B CG  
3987  C  CD  . PRO B 367  ? 0.9812 0.8032 0.7194 0.2104  0.0155  -0.0186 367  PRO B CD  
3988  N  N   . PRO B 368  ? 0.9355 0.7421 0.6587 0.1992  0.0198  -0.0247 368  PRO B N   
3989  C  CA  . PRO B 368  ? 0.9523 0.7491 0.6737 0.1959  0.0276  -0.0214 368  PRO B CA  
3990  C  C   . PRO B 368  ? 0.9539 0.7347 0.6651 0.2017  0.0368  -0.0137 368  PRO B C   
3991  O  O   . PRO B 368  ? 0.9119 0.6879 0.6280 0.1983  0.0448  -0.0091 368  PRO B O   
3992  C  CB  . PRO B 368  ? 0.9325 0.7264 0.6424 0.1960  0.0225  -0.0275 368  PRO B CB  
3993  C  CG  . PRO B 368  ? 0.9858 0.7950 0.7020 0.1940  0.0120  -0.0350 368  PRO B CG  
3994  C  CD  . PRO B 368  ? 0.9711 0.7841 0.6885 0.1997  0.0102  -0.0329 368  PRO B CD  
3995  N  N   . ILE B 369  ? 1.0117 0.7842 0.7086 0.2106  0.0362  -0.0120 369  ILE B N   
3996  C  CA  . ILE B 369  ? 1.0398 0.7962 0.7260 0.2162  0.0455  -0.0047 369  ILE B CA  
3997  C  C   . ILE B 369  ? 1.1091 0.8681 0.8102 0.2127  0.0528  0.0014  369  ILE B C   
3998  O  O   . ILE B 369  ? 1.0553 0.8047 0.7554 0.2128  0.0621  0.0074  369  ILE B O   
3999  C  CB  . ILE B 369  ? 0.9939 0.7407 0.6611 0.2267  0.0430  -0.0044 369  ILE B CB  
4000  C  CG1 . ILE B 369  ? 1.0550 0.7848 0.7115 0.2324  0.0534  0.0036  369  ILE B CG1 
4001  C  CG2 . ILE B 369  ? 1.1022 0.8599 0.7754 0.2285  0.0359  -0.0069 369  ILE B CG2 
4002  C  CD1 . ILE B 369  ? 1.0765 0.7947 0.7252 0.2319  0.0606  0.0063  369  ILE B CD1 
4003  N  N   . VAL B 370  ? 0.9104 0.6828 0.6259 0.2094  0.0485  -0.0002 370  VAL B N   
4004  C  CA  . VAL B 370  ? 0.8770 0.6525 0.6070 0.2057  0.0545  0.0050  370  VAL B CA  
4005  C  C   . VAL B 370  ? 0.8976 0.6765 0.6407 0.1979  0.0599  0.0067  370  VAL B C   
4006  O  O   . VAL B 370  ? 0.8802 0.6546 0.6289 0.1965  0.0683  0.0126  370  VAL B O   
4007  C  CB  . VAL B 370  ? 0.8413 0.6308 0.5834 0.2040  0.0480  0.0022  370  VAL B CB  
4008  C  CG1 . VAL B 370  ? 0.7644 0.5574 0.5219 0.1997  0.0540  0.0071  370  VAL B CG1 
4009  C  CG2 . VAL B 370  ? 0.8838 0.6694 0.6124 0.2127  0.0430  0.0009  370  VAL B CG2 
4010  N  N   . HIS B 371  ? 1.0292 0.8160 0.7772 0.1926  0.0551  0.0015  371  HIS B N   
4011  C  CA  . HIS B 371  ? 1.0016 0.7904 0.7598 0.1858  0.0600  0.0029  371  HIS B CA  
4012  C  C   . HIS B 371  ? 1.0825 0.8562 0.8293 0.1890  0.0684  0.0075  371  HIS B C   
4013  O  O   . HIS B 371  ? 1.0416 0.8136 0.7964 0.1863  0.0761  0.0123  371  HIS B O   
4014  C  CB  . HIS B 371  ? 1.0676 0.8655 0.8301 0.1802  0.0533  -0.0038 371  HIS B CB  
4015  C  CG  . HIS B 371  ? 1.0497 0.8638 0.8266 0.1755  0.0464  -0.0079 371  HIS B CG  
4016  N  ND1 . HIS B 371  ? 1.1289 0.9495 0.9023 0.1782  0.0379  -0.0130 371  HIS B ND1 
4017  C  CD2 . HIS B 371  ? 0.9507 0.7763 0.7456 0.1685  0.0468  -0.0079 371  HIS B CD2 
4018  C  CE1 . HIS B 371  ? 1.0402 0.8755 0.8289 0.1729  0.0336  -0.0158 371  HIS B CE1 
4019  N  NE2 . HIS B 371  ? 1.0091 0.8473 0.8107 0.1670  0.0389  -0.0127 371  HIS B NE2 
4020  N  N   . ALA B 372  ? 1.2760 1.0389 1.0040 0.1951  0.0669  0.0060  372  ALA B N   
4021  C  CA  . ALA B 372  ? 1.2958 1.0440 1.0116 0.1986  0.0747  0.0099  372  ALA B CA  
4022  C  C   . ALA B 372  ? 1.2385 0.9781 0.9530 0.2024  0.0837  0.0174  372  ALA B C   
4023  O  O   . ALA B 372  ? 1.2308 0.9644 0.9468 0.2016  0.0923  0.0221  372  ALA B O   
4024  C  CB  . ALA B 372  ? 1.2884 1.0269 0.9834 0.2047  0.0705  0.0063  372  ALA B CB  
4025  N  N   . LEU B 373  ? 0.8386 0.5776 0.5502 0.2067  0.0820  0.0186  373  LEU B N   
4026  C  CA  . LEU B 373  ? 0.9586 0.6896 0.6697 0.2096  0.0907  0.0256  373  LEU B CA  
4027  C  C   . LEU B 373  ? 0.9047 0.6446 0.6366 0.2025  0.0957  0.0288  373  LEU B C   
4028  O  O   . LEU B 373  ? 0.7808 0.5143 0.5147 0.2028  0.1050  0.0347  373  LEU B O   
4029  C  CB  . LEU B 373  ? 0.9338 0.6624 0.6376 0.2155  0.0873  0.0257  373  LEU B CB  
4030  C  CG  . LEU B 373  ? 0.9675 0.6843 0.6482 0.2244  0.0841  0.0240  373  LEU B CG  
4031  C  CD1 . LEU B 373  ? 1.0272 0.7432 0.7023 0.2300  0.0800  0.0239  373  LEU B CD1 
4032  C  CD2 . LEU B 373  ? 0.9106 0.6103 0.5769 0.2291  0.0935  0.0293  373  LEU B CD2 
4033  N  N   . ALA B 374  ? 1.2373 0.9924 0.9850 0.1962  0.0897  0.0250  374  ALA B N   
4034  C  CA  . ALA B 374  ? 1.2788 1.0430 1.0462 0.1895  0.0937  0.0275  374  ALA B CA  
4035  C  C   . ALA B 374  ? 1.2768 1.0387 1.0476 0.1863  0.0999  0.0295  374  ALA B C   
4036  O  O   . ALA B 374  ? 1.3108 1.0727 1.0910 0.1842  0.1074  0.0343  374  ALA B O   
4037  C  CB  . ALA B 374  ? 1.2712 1.0514 1.0529 0.1839  0.0855  0.0226  374  ALA B CB  
4038  N  N   . HIS B 375  ? 1.0885 0.8487 0.8521 0.1859  0.0968  0.0258  375  HIS B N   
4039  C  CA  . HIS B 375  ? 1.1255 0.8817 0.8897 0.1840  0.1028  0.0277  375  HIS B CA  
4040  C  C   . HIS B 375  ? 1.1668 0.9094 0.9211 0.1894  0.1124  0.0337  375  HIS B C   
4041  O  O   . HIS B 375  ? 1.1739 0.9159 0.9355 0.1875  0.1201  0.0378  375  HIS B O   
4042  C  CB  . HIS B 375  ? 1.0463 0.8007 0.8014 0.1836  0.0977  0.0224  375  HIS B CB  
4043  C  CG  . HIS B 375  ? 1.0848 0.8528 0.8513 0.1771  0.0898  0.0168  375  HIS B CG  
4044  N  ND1 . HIS B 375  ? 1.1173 0.8877 0.8767 0.1772  0.0811  0.0104  375  HIS B ND1 
4045  C  CD2 . HIS B 375  ? 1.1089 0.8886 0.8931 0.1704  0.0895  0.0165  375  HIS B CD2 
4046  C  CE1 . HIS B 375  ? 1.0158 0.7988 0.7884 0.1706  0.0761  0.0066  375  HIS B CE1 
4047  N  NE2 . HIS B 375  ? 1.1448 0.9332 0.9321 0.1665  0.0810  0.0103  375  HIS B NE2 
4048  N  N   . LEU B 376  ? 1.2993 1.0310 1.0366 0.1963  0.1122  0.0343  376  LEU B N   
4049  C  CA  . LEU B 376  ? 1.3904 1.1081 1.1167 0.2018  0.1216  0.0401  376  LEU B CA  
4050  C  C   . LEU B 376  ? 1.4089 1.1286 1.1473 0.2001  0.1288  0.0457  376  LEU B C   
4051  O  O   . LEU B 376  ? 1.4575 1.1725 1.1982 0.2002  0.1381  0.0506  376  LEU B O   
4052  C  CB  . LEU B 376  ? 1.4250 1.1308 1.1300 0.2097  0.1190  0.0392  376  LEU B CB  
4053  C  CG  . LEU B 376  ? 1.3012 0.9916 0.9930 0.2163  0.1282  0.0453  376  LEU B CG  
4054  C  CD1 . LEU B 376  ? 1.3907 1.0730 1.0779 0.2171  0.1366  0.0484  376  LEU B CD1 
4055  C  CD2 . LEU B 376  ? 1.3031 0.9832 0.9742 0.2243  0.1239  0.0436  376  LEU B CD2 
4056  N  N   . ILE B 377  ? 0.9375 0.6645 0.6840 0.1986  0.1247  0.0449  377  ILE B N   
4057  C  CA  . ILE B 377  ? 0.9531 0.6824 0.7117 0.1964  0.1309  0.0496  377  ILE B CA  
4058  C  C   . ILE B 377  ? 1.0085 0.7478 0.7860 0.1896  0.1348  0.0510  377  ILE B C   
4059  O  O   . ILE B 377  ? 1.0340 0.7710 0.8177 0.1888  0.1436  0.0560  377  ILE B O   
4060  C  CB  . ILE B 377  ? 0.9322 0.6679 0.6957 0.1959  0.1246  0.0477  377  ILE B CB  
4061  C  CG1 . ILE B 377  ? 0.9329 0.6566 0.6771 0.2038  0.1230  0.0480  377  ILE B CG1 
4062  C  CG2 . ILE B 377  ? 1.0162 0.7573 0.7960 0.1917  0.1298  0.0515  377  ILE B CG2 
4063  C  CD1 . ILE B 377  ? 0.8568 0.5861 0.6042 0.2043  0.1166  0.0459  377  ILE B CD1 
4064  N  N   . ASN B 378  ? 1.1659 0.9166 0.9529 0.1847  0.1284  0.0466  378  ASN B N   
4065  C  CA  . ASN B 378  ? 1.1226 0.8830 0.9270 0.1787  0.1314  0.0476  378  ASN B CA  
4066  C  C   . ASN B 378  ? 1.1509 0.9042 0.9511 0.1802  0.1394  0.0508  378  ASN B C   
4067  O  O   . ASN B 378  ? 1.1889 0.9460 1.0012 0.1775  0.1460  0.0543  378  ASN B O   
4068  C  CB  . ASN B 378  ? 1.0874 0.8598 0.9005 0.1736  0.1229  0.0421  378  ASN B CB  
4069  C  CG  . ASN B 378  ? 1.1161 0.8991 0.9394 0.1707  0.1164  0.0396  378  ASN B CG  
4070  O  OD1 . ASN B 378  ? 1.1225 0.9075 0.9537 0.1700  0.1194  0.0426  378  ASN B OD1 
4071  N  ND2 . ASN B 378  ? 1.0424 0.8320 0.8654 0.1689  0.1076  0.0341  378  ASN B ND2 
4072  N  N   . ALA B 379  ? 0.9793 0.7223 0.7624 0.1846  0.1389  0.0494  379  ALA B N   
4073  C  CA  . ALA B 379  ? 0.9010 0.6363 0.6785 0.1867  0.1464  0.0523  379  ALA B CA  
4074  C  C   . ALA B 379  ? 1.0051 0.7322 0.7802 0.1901  0.1567  0.0586  379  ALA B C   
4075  O  O   . ALA B 379  ? 1.0014 0.7296 0.7843 0.1889  0.1644  0.0622  379  ALA B O   
4076  C  CB  . ALA B 379  ? 0.7915 0.5168 0.5498 0.1909  0.1431  0.0491  379  ALA B CB  
4077  N  N   . GLU B 380  ? 1.2390 0.9577 1.0032 0.1945  0.1571  0.0599  380  GLU B N   
4078  C  CA  . GLU B 380  ? 1.2781 0.9876 1.0387 0.1977  0.1672  0.0660  380  GLU B CA  
4079  C  C   . GLU B 380  ? 1.2833 1.0027 1.0645 0.1923  0.1720  0.0691  380  GLU B C   
4080  O  O   . GLU B 380  ? 1.3524 1.0694 1.1380 0.1923  0.1816  0.0737  380  GLU B O   
4081  C  CB  . GLU B 380  ? 1.4987 1.1972 1.2431 0.2035  0.1659  0.0665  380  GLU B CB  
4082  C  CG  . GLU B 380  ? 1.7041 1.3870 1.4344 0.2094  0.1760  0.0719  380  GLU B CG  
4083  C  CD  . GLU B 380  ? 1.7395 1.4120 1.4524 0.2145  0.1770  0.0711  380  GLU B CD  
4084  O  OE1 . GLU B 380  ? 1.6385 1.3136 1.3464 0.2144  0.1685  0.0658  380  GLU B OE1 
4085  O  OE2 . GLU B 380  ? 1.9177 1.5791 1.6217 0.2185  0.1865  0.0757  380  GLU B OE2 
4086  N  N   . LEU B 381  ? 1.0828 0.8138 0.8770 0.1876  0.1655  0.0664  381  LEU B N   
4087  C  CA  . LEU B 381  ? 1.0472 0.7882 0.8612 0.1822  0.1689  0.0687  381  LEU B CA  
4088  C  C   . LEU B 381  ? 1.1221 0.8728 0.9510 0.1779  0.1720  0.0692  381  LEU B C   
4089  O  O   . LEU B 381  ? 1.1218 0.8802 0.9667 0.1739  0.1763  0.0715  381  LEU B O   
4090  C  CB  . LEU B 381  ? 0.8616 0.6123 0.6845 0.1787  0.1603  0.0652  381  LEU B CB  
4091  C  CG  . LEU B 381  ? 0.9710 0.7138 0.7835 0.1824  0.1586  0.0656  381  LEU B CG  
4092  C  CD1 . LEU B 381  ? 0.9618 0.7153 0.7832 0.1791  0.1494  0.0616  381  LEU B CD1 
4093  C  CD2 . LEU B 381  ? 1.1516 0.8871 0.9652 0.1832  0.1684  0.0712  381  LEU B CD2 
4094  N  N   . GLY B 382  ? 0.8994 0.6498 0.7233 0.1787  0.1698  0.0669  382  GLY B N   
4095  C  CA  . GLY B 382  ? 0.7662 0.5256 0.6031 0.1751  0.1720  0.0671  382  GLY B CA  
4096  C  C   . GLY B 382  ? 0.7982 0.5719 0.6496 0.1693  0.1641  0.0631  382  GLY B C   
4097  O  O   . GLY B 382  ? 0.8694 0.6516 0.7335 0.1662  0.1660  0.0635  382  GLY B O   
4098  N  N   . ASN B 383  ? 0.9745 0.7511 0.8241 0.1682  0.1556  0.0592  383  ASN B N   
4099  C  CA  . ASN B 383  ? 0.9270 0.7171 0.7903 0.1627  0.1484  0.0555  383  ASN B CA  
4100  C  C   . ASN B 383  ? 0.9449 0.7370 0.8061 0.1615  0.1448  0.0522  383  ASN B C   
4101  O  O   . ASN B 383  ? 0.9321 0.7351 0.8063 0.1569  0.1418  0.0504  383  ASN B O   
4102  C  CB  . ASN B 383  ? 0.8862 0.6786 0.7476 0.1622  0.1406  0.0523  383  ASN B CB  
4103  C  CG  . ASN B 383  ? 0.9299 0.7177 0.7903 0.1641  0.1441  0.0555  383  ASN B CG  
4104  O  OD1 . ASN B 383  ? 0.9618 0.7497 0.8301 0.1632  0.1516  0.0596  383  ASN B OD1 
4105  N  ND2 . ASN B 383  ? 0.9939 0.7776 0.8445 0.1668  0.1389  0.0534  383  ASN B ND2 
4106  N  N   . VAL B 384  ? 1.2647 1.0459 1.1091 0.1657  0.1450  0.0514  384  VAL B N   
4107  C  CA  . VAL B 384  ? 1.3332 1.1148 1.1740 0.1645  0.1416  0.0480  384  VAL B CA  
4108  C  C   . VAL B 384  ? 1.2808 1.0675 1.1328 0.1624  0.1469  0.0503  384  VAL B C   
4109  O  O   . VAL B 384  ? 1.3449 1.1288 1.1990 0.1646  0.1551  0.0548  384  VAL B O   
4110  C  CB  . VAL B 384  ? 1.3375 1.1050 1.1575 0.1698  0.1421  0.0472  384  VAL B CB  
4111  C  CG1 . VAL B 384  ? 1.2716 1.0378 1.0876 0.1686  0.1402  0.0442  384  VAL B CG1 
4112  C  CG2 . VAL B 384  ? 1.3502 1.1141 1.1593 0.1719  0.1354  0.0440  384  VAL B CG2 
4113  N  N   . GLY B 385  ? 1.0762 0.8708 0.9357 0.1583  0.1422  0.0472  385  GLY B N   
4114  C  CA  . GLY B 385  ? 1.1743 0.9749 1.0450 0.1564  0.1461  0.0489  385  GLY B CA  
4115  C  C   . GLY B 385  ? 1.1444 0.9578 1.0343 0.1526  0.1468  0.0505  385  GLY B C   
4116  O  O   . GLY B 385  ? 1.0737 0.8943 0.9743 0.1506  0.1483  0.0512  385  GLY B O   
4117  N  N   . GLN B 386  ? 1.1853 1.0015 1.0796 0.1519  0.1457  0.0512  386  GLN B N   
4118  C  CA  . GLN B 386  ? 1.1070 0.9350 1.0192 0.1481  0.1457  0.0522  386  GLN B CA  
4119  C  C   . GLN B 386  ? 1.0637 0.8992 0.9810 0.1445  0.1374  0.0484  386  GLN B C   
4120  O  O   . GLN B 386  ? 1.0657 0.9121 0.9959 0.1404  0.1342  0.0470  386  GLN B O   
4121  C  CB  . GLN B 386  ? 1.0950 0.9201 1.0096 0.1499  0.1526  0.0566  386  GLN B CB  
4122  C  CG  . GLN B 386  ? 1.1699 0.9889 1.0813 0.1533  0.1617  0.0607  386  GLN B CG  
4123  C  CD  . GLN B 386  ? 1.1605 0.9884 1.0845 0.1515  0.1642  0.0614  386  GLN B CD  
4124  O  OE1 . GLN B 386  ? 1.2071 1.0319 1.1252 0.1532  0.1647  0.0608  386  GLN B OE1 
4125  N  NE2 . GLN B 386  ? 1.1249 0.9638 1.0660 0.1482  0.1657  0.0627  386  GLN B NE2 
4126  N  N   . THR B 387  ? 1.0268 0.8567 0.9337 0.1463  0.1336  0.0468  387  THR B N   
4127  C  CA  . THR B 387  ? 1.0364 0.8730 0.9468 0.1435  0.1255  0.0429  387  THR B CA  
4128  C  C   . THR B 387  ? 1.0116 0.8442 0.9092 0.1445  0.1190  0.0385  387  THR B C   
4129  O  O   . THR B 387  ? 0.9748 0.8150 0.8768 0.1415  0.1120  0.0347  387  THR B O   
4130  C  CB  . THR B 387  ? 1.0079 0.8439 0.9197 0.1445  0.1259  0.0445  387  THR B CB  
4131  O  OG1 . THR B 387  ? 0.9953 0.8184 0.8911 0.1498  0.1287  0.0461  387  THR B OG1 
4132  C  CG2 . THR B 387  ? 0.9950 0.8362 0.9209 0.1425  0.1317  0.0482  387  THR B CG2 
4133  N  N   . VAL B 388  ? 1.0001 0.8214 0.8825 0.1485  0.1212  0.0388  388  VAL B N   
4134  C  CA  . VAL B 388  ? 0.9858 0.8029 0.8556 0.1494  0.1152  0.0343  388  VAL B CA  
4135  C  C   . VAL B 388  ? 1.0219 0.8343 0.8863 0.1494  0.1173  0.0337  388  VAL B C   
4136  O  O   . VAL B 388  ? 1.1332 0.9372 0.9914 0.1528  0.1241  0.0371  388  VAL B O   
4137  C  CB  . VAL B 388  ? 1.0817 0.8882 0.9357 0.1549  0.1149  0.0345  388  VAL B CB  
4138  C  CG1 . VAL B 388  ? 1.1453 0.9480 0.9866 0.1558  0.1084  0.0294  388  VAL B CG1 
4139  C  CG2 . VAL B 388  ? 1.1334 0.9437 0.9920 0.1553  0.1129  0.0351  388  VAL B CG2 
4140  N  N   . PHE B 389  ? 1.0288 0.8462 0.8952 0.1455  0.1118  0.0294  389  PHE B N   
4141  C  CA  . PHE B 389  ? 1.1101 0.9228 0.9712 0.1450  0.1133  0.0283  389  PHE B CA  
4142  C  C   . PHE B 389  ? 1.1958 1.0037 1.0443 0.1447  0.1071  0.0230  389  PHE B C   
4143  O  O   . PHE B 389  ? 1.1655 0.9793 1.0154 0.1426  0.1002  0.0192  389  PHE B O   
4144  C  CB  . PHE B 389  ? 1.0586 0.8808 0.9338 0.1401  0.1131  0.0281  389  PHE B CB  
4145  C  CG  . PHE B 389  ? 1.0328 0.8599 0.9204 0.1404  0.1192  0.0330  389  PHE B CG  
4146  C  CD1 . PHE B 389  ? 1.0071 0.8286 0.8926 0.1433  0.1265  0.0367  389  PHE B CD1 
4147  C  CD2 . PHE B 389  ? 1.0778 0.9155 0.9793 0.1379  0.1176  0.0337  389  PHE B CD2 
4148  C  CE1 . PHE B 389  ? 1.0419 0.8691 0.9397 0.1434  0.1319  0.0408  389  PHE B CE1 
4149  C  CE2 . PHE B 389  ? 0.9421 0.7848 0.8555 0.1378  0.1229  0.0377  389  PHE B CE2 
4150  C  CZ  . PHE B 389  ? 0.9821 0.8200 0.8941 0.1405  0.1300  0.0412  389  PHE B CZ  
4151  N  N   . TYR B 390  ? 1.2595 1.0567 1.0955 0.1470  0.1097  0.0227  390  TYR B N   
4152  C  CA  . TYR B 390  ? 1.2595 1.0509 1.0824 0.1468  0.1044  0.0176  390  TYR B CA  
4153  C  C   . TYR B 390  ? 1.3150 1.1055 1.1382 0.1430  0.1042  0.0153  390  TYR B C   
4154  O  O   . TYR B 390  ? 1.3741 1.1596 1.1967 0.1444  0.1104  0.0185  390  TYR B O   
4155  C  CB  . TYR B 390  ? 1.2907 1.0683 1.0959 0.1531  0.1072  0.0187  390  TYR B CB  
4156  C  CG  . TYR B 390  ? 1.2528 1.0293 1.0554 0.1574  0.1078  0.0211  390  TYR B CG  
4157  C  CD1 . TYR B 390  ? 1.2310 1.0136 1.0347 0.1567  0.1007  0.0178  390  TYR B CD1 
4158  C  CD2 . TYR B 390  ? 1.2686 1.0376 1.0674 0.1623  0.1157  0.0267  390  TYR B CD2 
4159  C  CE1 . TYR B 390  ? 1.1844 0.9648 0.9847 0.1610  0.1014  0.0201  390  TYR B CE1 
4160  C  CE2 . TYR B 390  ? 1.3178 1.0845 1.1134 0.1662  0.1167  0.0290  390  TYR B CE2 
4161  C  CZ  . TYR B 390  ? 1.2852 1.0572 1.0812 0.1656  0.1095  0.0258  390  TYR B CZ  
4162  O  OH  . TYR B 390  ? 1.3879 1.1566 1.1797 0.1698  0.1106  0.0282  390  TYR B OH  
4163  N  N   . HIS B 391  ? 1.1785 0.9740 1.0028 0.1383  0.0973  0.0098  391  HIS B N   
4164  C  CA  . HIS B 391  ? 1.1253 0.9196 0.9493 0.1340  0.0966  0.0070  391  HIS B CA  
4165  C  C   . HIS B 391  ? 1.0585 0.8460 0.8688 0.1332  0.0916  0.0012  391  HIS B C   
4166  O  O   . HIS B 391  ? 1.0850 0.8710 0.8877 0.1357  0.0876  -0.0010 391  HIS B O   
4167  C  CB  . HIS B 391  ? 1.0923 0.8997 0.9322 0.1279  0.0934  0.0055  391  HIS B CB  
4168  C  CG  . HIS B 391  ? 1.1434 0.9583 0.9973 0.1282  0.0976  0.0106  391  HIS B CG  
4169  N  ND1 . HIS B 391  ? 1.1801 0.9931 1.0378 0.1287  0.1035  0.0141  391  HIS B ND1 
4170  C  CD2 . HIS B 391  ? 1.1826 1.0069 1.0475 0.1282  0.0966  0.0124  391  HIS B CD2 
4171  C  CE1 . HIS B 391  ? 1.1396 0.9611 1.0106 0.1288  0.1057  0.0177  391  HIS B CE1 
4172  N  NE2 . HIS B 391  ? 1.1659 0.9940 1.0413 0.1283  0.1018  0.0168  391  HIS B NE2 
4173  N  N   . GLU B 392  ? 1.0966 0.8797 0.9034 0.1297  0.0917  -0.0013 392  GLU B N   
4174  C  CA  . GLU B 392  ? 1.1072 0.8853 0.9031 0.1273  0.0864  -0.0076 392  GLU B CA  
4175  C  C   . GLU B 392  ? 1.1293 0.9201 0.9338 0.1223  0.0785  -0.0126 392  GLU B C   
4176  O  O   . GLU B 392  ? 1.2657 1.0682 1.0849 0.1192  0.0778  -0.0114 392  GLU B O   
4177  C  CB  . GLU B 392  ? 1.1048 0.8753 0.8961 0.1242  0.0888  -0.0090 392  GLU B CB  
4178  C  CG  . GLU B 392  ? 1.1688 0.9249 0.9481 0.1296  0.0958  -0.0053 392  GLU B CG  
4179  C  CD  . GLU B 392  ? 1.2932 1.0368 1.0540 0.1321  0.0939  -0.0090 392  GLU B CD  
4180  O  OE1 . GLU B 392  ? 1.2884 1.0346 1.0461 0.1287  0.0869  -0.0150 392  GLU B OE1 
4181  O  OE2 . GLU B 392  ? 1.4324 1.1638 1.1819 0.1374  0.0994  -0.0061 392  GLU B OE2 
4182  N  N   . PRO B 393  ? 0.9204 0.7097 0.7160 0.1215  0.0725  -0.0183 393  PRO B N   
4183  C  CA  . PRO B 393  ? 0.9574 0.7597 0.7614 0.1172  0.0649  -0.0233 393  PRO B CA  
4184  C  C   . PRO B 393  ? 0.9863 0.7964 0.8017 0.1094  0.0638  -0.0256 393  PRO B C   
4185  O  O   . PRO B 393  ? 0.8158 0.6189 0.6270 0.1062  0.0662  -0.0267 393  PRO B O   
4186  C  CB  . PRO B 393  ? 0.8645 0.6617 0.6548 0.1180  0.0593  -0.0293 393  PRO B CB  
4187  C  CG  . PRO B 393  ? 0.8822 0.6633 0.6580 0.1203  0.0639  -0.0284 393  PRO B CG  
4188  C  CD  . PRO B 393  ? 0.8982 0.6743 0.6757 0.1250  0.0721  -0.0207 393  PRO B CD  
4189  N  N   . VAL B 394  ? 1.3392 1.1634 1.1683 0.1066  0.0604  -0.0262 394  VAL B N   
4190  C  CA  . VAL B 394  ? 1.2548 1.0877 1.0958 0.0995  0.0594  -0.0280 394  VAL B CA  
4191  C  C   . VAL B 394  ? 1.1625 1.0055 1.0071 0.0946  0.0517  -0.0349 394  VAL B C   
4192  O  O   . VAL B 394  ? 1.1658 1.0184 1.0217 0.0888  0.0502  -0.0366 394  VAL B O   
4193  C  CB  . VAL B 394  ? 1.2057 1.0472 1.0610 0.0998  0.0624  -0.0229 394  VAL B CB  
4194  C  CG1 . VAL B 394  ? 1.3427 1.1754 1.1956 0.1042  0.0700  -0.0165 394  VAL B CG1 
4195  C  CG2 . VAL B 394  ? 1.1288 0.9800 0.9903 0.1026  0.0587  -0.0224 394  VAL B CG2 
4196  N  N   . GLU B 395  ? 1.3951 1.2365 1.2306 0.0969  0.0469  -0.0390 395  GLU B N   
4197  C  CA  . GLU B 395  ? 1.4456 1.2978 1.2846 0.0931  0.0392  -0.0457 395  GLU B CA  
4198  C  C   . GLU B 395  ? 1.4597 1.3065 1.2902 0.0882  0.0365  -0.0522 395  GLU B C   
4199  O  O   . GLU B 395  ? 1.4255 1.2782 1.2542 0.0869  0.0298  -0.0583 395  GLU B O   
4200  C  CB  . GLU B 395  ? 1.4005 1.2563 1.2358 0.0993  0.0347  -0.0463 395  GLU B CB  
4201  C  CG  . GLU B 395  ? 1.4670 1.3199 1.3029 0.1062  0.0392  -0.0391 395  GLU B CG  
4202  C  CD  . GLU B 395  ? 1.5557 1.4093 1.3850 0.1128  0.0354  -0.0396 395  GLU B CD  
4203  O  OE1 . GLU B 395  ? 1.5443 1.4010 1.3685 0.1125  0.0288  -0.0457 395  GLU B OE1 
4204  O  OE2 . GLU B 395  ? 1.6691 1.5199 1.4983 0.1184  0.0389  -0.0341 395  GLU B OE2 
4205  N  N   . ALA B 396  ? 1.0149 0.8508 0.8403 0.0857  0.0415  -0.0511 396  ALA B N   
4206  C  CA  . ALA B 396  ? 1.0671 0.8946 0.8821 0.0815  0.0400  -0.0567 396  ALA B CA  
4207  C  C   . ALA B 396  ? 1.2701 1.0906 1.0707 0.0869  0.0365  -0.0594 396  ALA B C   
4208  O  O   . ALA B 396  ? 1.3864 1.1938 1.1753 0.0927  0.0408  -0.0557 396  ALA B O   
4209  C  CB  . ALA B 396  ? 0.9796 0.8182 0.8035 0.0728  0.0350  -0.0633 396  ALA B CB  
4210  N  N   . ARG B 397  ? 1.3337 1.1630 1.1347 0.0852  0.0288  -0.0659 397  ARG B N   
4211  C  CA  . ARG B 397  ? 1.3903 1.2144 1.1779 0.0909  0.0247  -0.0688 397  ARG B CA  
4212  C  C   . ARG B 397  ? 1.3948 1.2272 1.1860 0.0976  0.0221  -0.0662 397  ARG B C   
4213  O  O   . ARG B 397  ? 1.3851 1.2325 1.1867 0.0955  0.0165  -0.0695 397  ARG B O   
4214  C  CB  . ARG B 397  ? 1.3949 1.2231 1.1795 0.0854  0.0175  -0.0781 397  ARG B CB  
4215  C  CG  . ARG B 397  ? 1.5532 1.3726 1.3209 0.0910  0.0137  -0.0815 397  ARG B CG  
4216  C  CD  . ARG B 397  ? 1.4679 1.2932 1.2339 0.0854  0.0058  -0.0913 397  ARG B CD  
4217  N  NE  . ARG B 397  ? 1.4942 1.3385 1.2726 0.0840  -0.0011 -0.0951 397  ARG B NE  
4218  C  CZ  . ARG B 397  ? 1.4936 1.3470 1.2726 0.0806  -0.0090 -0.1036 397  ARG B CZ  
4219  N  NH1 . ARG B 397  ? 1.4535 1.2986 1.2211 0.0779  -0.0115 -0.1096 397  ARG B NH1 
4220  N  NH2 . ARG B 397  ? 1.4718 1.3432 1.2630 0.0799  -0.0147 -0.1063 397  ARG B NH2 
4221  N  N   . PRO B 398  ? 1.2603 1.0837 1.0434 0.1058  0.0261  -0.0603 398  PRO B N   
4222  C  CA  . PRO B 398  ? 1.2383 1.0680 1.0229 0.1125  0.0236  -0.0581 398  PRO B CA  
4223  C  C   . PRO B 398  ? 1.3010 1.1289 1.0729 0.1170  0.0169  -0.0632 398  PRO B C   
4224  O  O   . PRO B 398  ? 1.3296 1.1442 1.0860 0.1200  0.0179  -0.0642 398  PRO B O   
4225  C  CB  . PRO B 398  ? 1.2393 1.0586 1.0201 0.1186  0.0317  -0.0495 398  PRO B CB  
4226  C  CG  . PRO B 398  ? 1.2268 1.0354 1.0047 0.1152  0.0381  -0.0475 398  PRO B CG  
4227  C  CD  . PRO B 398  ? 1.3095 1.1165 1.0820 0.1095  0.0337  -0.0551 398  PRO B CD  
4228  N  N   . THR B 399  ? 1.4755 1.3166 1.2534 0.1179  0.0100  -0.0667 399  THR B N   
4229  C  CA  . THR B 399  ? 1.5385 1.3799 1.3052 0.1220  0.0027  -0.0724 399  THR B CA  
4230  C  C   . THR B 399  ? 1.4674 1.3215 1.2404 0.1263  -0.0025 -0.0728 399  THR B C   
4231  O  O   . THR B 399  ? 1.5062 1.3710 1.2938 0.1241  -0.0016 -0.0703 399  THR B O   
4232  C  CB  . THR B 399  ? 1.5916 1.4372 1.3580 0.1147  -0.0030 -0.0813 399  THR B CB  
4233  O  OG1 . THR B 399  ? 1.6810 1.5287 1.4376 0.1190  -0.0109 -0.0873 399  THR B OG1 
4234  C  CG2 . THR B 399  ? 1.4733 1.3355 1.2583 0.1062  -0.0055 -0.0844 399  THR B CG2 
4235  N  N   . ASN B 400  ? 1.2413 1.0936 1.0023 0.1329  -0.0081 -0.0760 400  ASN B N   
4236  C  CA  . ASN B 400  ? 1.2571 1.1212 1.0217 0.1376  -0.0143 -0.0777 400  ASN B CA  
4237  C  C   . ASN B 400  ? 1.2627 1.1441 1.0391 0.1305  -0.0219 -0.0858 400  ASN B C   
4238  O  O   . ASN B 400  ? 1.2189 1.1019 0.9893 0.1287  -0.0279 -0.0932 400  ASN B O   
4239  C  CB  . ASN B 400  ? 1.3078 1.1633 1.0543 0.1474  -0.0177 -0.0785 400  ASN B CB  
4240  C  CG  . ASN B 400  ? 1.3634 1.2260 1.1112 0.1548  -0.0210 -0.0768 400  ASN B CG  
4241  O  OD1 . ASN B 400  ? 1.3124 1.1893 1.0752 0.1520  -0.0232 -0.0773 400  ASN B OD1 
4242  N  ND2 . ASN B 400  ? 1.4663 1.3183 1.1977 0.1646  -0.0213 -0.0748 400  ASN B ND2 
4243  N  N   . GLN B 401  ? 1.2173 1.1121 1.0109 0.1263  -0.0217 -0.0847 401  GLN B N   
4244  C  CA  . GLN B 401  ? 1.0773 0.9887 0.8839 0.1183  -0.0275 -0.0919 401  GLN B CA  
4245  C  C   . GLN B 401  ? 1.0777 1.0008 0.8826 0.1225  -0.0371 -0.0985 401  GLN B C   
4246  O  O   . GLN B 401  ? 0.9991 0.9313 0.8068 0.1172  -0.0432 -0.1066 401  GLN B O   
4247  C  CB  . GLN B 401  ? 1.0365 0.9583 0.8611 0.1133  -0.0242 -0.0886 401  GLN B CB  
4248  C  CG  . GLN B 401  ? 1.0527 0.9651 0.8806 0.1082  -0.0155 -0.0832 401  GLN B CG  
4249  C  CD  . GLN B 401  ? 0.9981 0.9215 0.8436 0.1030  -0.0129 -0.0807 401  GLN B CD  
4250  O  OE1 . GLN B 401  ? 1.0058 0.9438 0.8614 0.1028  -0.0174 -0.0830 401  GLN B OE1 
4251  N  NE2 . GLN B 401  ? 1.0256 0.9418 0.8744 0.0989  -0.0056 -0.0761 401  GLN B NE2 
4252  N  N   . THR B 402  ? 1.3052 1.2281 1.1052 0.1319  -0.0386 -0.0952 402  THR B N   
4253  C  CA  . THR B 402  ? 1.2991 1.2334 1.0972 0.1369  -0.0478 -0.1012 402  THR B CA  
4254  C  C   . THR B 402  ? 1.3414 1.2692 1.1238 0.1396  -0.0530 -0.1071 402  THR B C   
4255  O  O   . THR B 402  ? 1.3395 1.2796 1.1234 0.1392  -0.0617 -0.1151 402  THR B O   
4256  C  CB  . THR B 402  ? 1.3259 1.2595 1.1209 0.1469  -0.0477 -0.0959 402  THR B CB  
4257  O  OG1 . THR B 402  ? 1.3435 1.2887 1.1367 0.1522  -0.0570 -0.1019 402  THR B OG1 
4258  C  CG2 . THR B 402  ? 1.3457 1.2591 1.1235 0.1548  -0.0420 -0.0893 402  THR B CG2 
4259  N  N   . GLU B 403  ? 1.4483 1.3573 1.2158 0.1424  -0.0480 -0.1036 403  GLU B N   
4260  C  CA  . GLU B 403  ? 1.4782 1.3798 1.2300 0.1446  -0.0527 -0.1093 403  GLU B CA  
4261  C  C   . GLU B 403  ? 1.4993 1.4070 1.2573 0.1338  -0.0556 -0.1171 403  GLU B C   
4262  O  O   . GLU B 403  ? 1.5811 1.4939 1.3340 0.1335  -0.0634 -0.1253 403  GLU B O   
4263  C  CB  . GLU B 403  ? 1.5731 1.4526 1.3074 0.1503  -0.0458 -0.1032 403  GLU B CB  
4264  C  CG  . GLU B 403  ? 1.7132 1.5850 1.4373 0.1619  -0.0439 -0.0968 403  GLU B CG  
4265  C  CD  . GLU B 403  ? 1.9007 1.7800 1.6176 0.1697  -0.0533 -0.1020 403  GLU B CD  
4266  O  OE1 . GLU B 403  ? 1.8858 1.7650 1.5934 0.1701  -0.0598 -0.1093 403  GLU B OE1 
4267  O  OE2 . GLU B 403  ? 1.9951 1.8800 1.7152 0.1756  -0.0543 -0.0990 403  GLU B OE2 
4268  N  N   . GLU B 404  ? 1.0503 0.9574 0.8192 0.1248  -0.0493 -0.1147 404  GLU B N   
4269  C  CA  . GLU B 404  ? 0.9600 0.8725 0.7355 0.1138  -0.0514 -0.1217 404  GLU B CA  
4270  C  C   . GLU B 404  ? 0.9205 0.8554 0.7113 0.1091  -0.0590 -0.1289 404  GLU B C   
4271  O  O   . GLU B 404  ? 0.9694 0.9110 0.7626 0.1022  -0.0640 -0.1373 404  GLU B O   
4272  C  CB  . GLU B 404  ? 0.9047 0.8102 0.6873 0.1062  -0.0424 -0.1168 404  GLU B CB  
4273  C  CG  . GLU B 404  ? 1.1024 0.9863 0.8702 0.1095  -0.0351 -0.1111 404  GLU B CG  
4274  C  CD  . GLU B 404  ? 1.0555 0.9333 0.8304 0.1023  -0.0266 -0.1065 404  GLU B CD  
4275  O  OE1 . GLU B 404  ? 0.9836 0.8736 0.7749 0.0955  -0.0261 -0.1070 404  GLU B OE1 
4276  O  OE2 . GLU B 404  ? 1.1178 0.9785 0.8816 0.1039  -0.0204 -0.1025 404  GLU B OE2 
4277  N  N   . LEU B 405  ? 0.7787 0.7254 0.5801 0.1125  -0.0599 -0.1259 405  LEU B N   
4278  C  CA  . LEU B 405  ? 0.8116 0.7802 0.6270 0.1093  -0.0673 -0.1327 405  LEU B CA  
4279  C  C   . LEU B 405  ? 0.8682 0.8428 0.6746 0.1156  -0.0771 -0.1398 405  LEU B C   
4280  O  O   . LEU B 405  ? 0.8978 0.8875 0.7117 0.1105  -0.0841 -0.1486 405  LEU B O   
4281  C  CB  . LEU B 405  ? 0.7922 0.7707 0.6201 0.1120  -0.0654 -0.1273 405  LEU B CB  
4282  C  CG  . LEU B 405  ? 0.8236 0.8251 0.6691 0.1072  -0.0711 -0.1331 405  LEU B CG  
4283  C  CD1 . LEU B 405  ? 0.8070 0.8138 0.6658 0.0943  -0.0678 -0.1356 405  LEU B CD1 
4284  C  CD2 . LEU B 405  ? 0.7336 0.7428 0.5870 0.1131  -0.0704 -0.1279 405  LEU B CD2 
4285  N  N   . VAL B 406  ? 1.0751 1.0380 0.8651 0.1268  -0.0775 -0.1363 406  VAL B N   
4286  C  CA  . VAL B 406  ? 1.1202 1.0866 0.8991 0.1338  -0.0867 -0.1428 406  VAL B CA  
4287  C  C   . VAL B 406  ? 1.1801 1.1418 0.9512 0.1282  -0.0899 -0.1503 406  VAL B C   
4288  O  O   . VAL B 406  ? 1.2234 1.1971 0.9950 0.1275  -0.0990 -0.1595 406  VAL B O   
4289  C  CB  . VAL B 406  ? 0.9243 0.8767 0.6859 0.1472  -0.0853 -0.1365 406  VAL B CB  
4290  C  CG1 . VAL B 406  ? 0.9153 0.8686 0.6626 0.1548  -0.0945 -0.1432 406  VAL B CG1 
4291  C  CG2 . VAL B 406  ? 1.1149 1.0737 0.8844 0.1527  -0.0834 -0.1304 406  VAL B CG2 
4292  N  N   . ALA B 407  ? 1.2275 1.1720 0.9917 0.1239  -0.0827 -0.1469 407  ALA B N   
4293  C  CA  . ALA B 407  ? 1.2268 1.1654 0.9833 0.1180  -0.0851 -0.1540 407  ALA B CA  
4294  C  C   . ALA B 407  ? 1.2800 1.2351 1.0534 0.1055  -0.0885 -0.1619 407  ALA B C   
4295  O  O   . ALA B 407  ? 1.4022 1.3617 1.1728 0.1014  -0.0951 -0.1711 407  ALA B O   
4296  C  CB  . ALA B 407  ? 1.1549 1.0712 0.9006 0.1165  -0.0758 -0.1480 407  ALA B CB  
4297  N  N   . LEU B 408  ? 1.2496 1.2141 1.0406 0.0991  -0.0842 -0.1587 408  LEU B N   
4298  C  CA  . LEU B 408  ? 1.3371 1.3169 1.1445 0.0870  -0.0864 -0.1657 408  LEU B CA  
4299  C  C   . LEU B 408  ? 1.3606 1.3629 1.1769 0.0880  -0.0967 -0.1740 408  LEU B C   
4300  O  O   . LEU B 408  ? 1.4195 1.4320 1.2412 0.0803  -0.1021 -0.1834 408  LEU B O   
4301  C  CB  . LEU B 408  ? 1.3267 1.3094 1.1494 0.0806  -0.0785 -0.1596 408  LEU B CB  
4302  C  CG  . LEU B 408  ? 1.3055 1.3043 1.1463 0.0681  -0.0796 -0.1656 408  LEU B CG  
4303  C  CD1 . LEU B 408  ? 1.2271 1.2191 1.0631 0.0588  -0.0800 -0.1724 408  LEU B CD1 
4304  C  CD2 . LEU B 408  ? 1.1908 1.1905 1.0445 0.0636  -0.0715 -0.1585 408  LEU B CD2 
4305  N  N   . VAL B 409  ? 1.2807 1.2912 1.0988 0.0976  -0.0995 -0.1709 409  VAL B N   
4306  C  CA  . VAL B 409  ? 1.3153 1.3475 1.1415 0.0998  -0.1094 -0.1785 409  VAL B CA  
4307  C  C   . VAL B 409  ? 1.3445 1.3749 1.1559 0.1053  -0.1180 -0.1858 409  VAL B C   
4308  O  O   . VAL B 409  ? 1.4077 1.4560 1.2256 0.1039  -0.1270 -0.1950 409  VAL B O   
4309  C  CB  . VAL B 409  ? 1.2711 1.3115 1.1024 0.1091  -0.1098 -0.1729 409  VAL B CB  
4310  C  CG1 . VAL B 409  ? 1.2285 1.2712 1.0746 0.1033  -0.1017 -0.1662 409  VAL B CG1 
4311  C  CG2 . VAL B 409  ? 1.3108 1.3346 1.1231 0.1223  -0.1086 -0.1664 409  VAL B CG2 
4312  N  N   . SER B 410  ? 1.2253 1.2344 1.0167 0.1116  -0.1154 -0.1821 410  SER B N   
4313  C  CA  . SER B 410  ? 1.1939 1.1993 0.9700 0.1161  -0.1231 -0.1892 410  SER B CA  
4314  C  C   . SER B 410  ? 1.2585 1.2655 1.0373 0.1041  -0.1252 -0.1981 410  SER B C   
4315  O  O   . SER B 410  ? 1.2658 1.2836 1.0436 0.1034  -0.1346 -0.2080 410  SER B O   
4316  C  CB  . SER B 410  ? 1.1492 1.1305 0.9028 0.1262  -0.1189 -0.1823 410  SER B CB  
4317  O  OG  . SER B 410  ? 1.2798 1.2557 1.0173 0.1300  -0.1258 -0.1893 410  SER B OG  
4318  N  N   . GLU B 411  ? 1.3348 1.3310 1.1169 0.0945  -0.1167 -0.1948 411  GLU B N   
4319  C  CA  . GLU B 411  ? 1.2698 1.2670 1.0556 0.0820  -0.1178 -0.2029 411  GLU B CA  
4320  C  C   . GLU B 411  ? 1.2842 1.3068 1.0911 0.0730  -0.1232 -0.2109 411  GLU B C   
4321  O  O   . GLU B 411  ? 1.3232 1.3529 1.1325 0.0653  -0.1287 -0.2209 411  GLU B O   
4322  C  CB  . GLU B 411  ? 1.3323 1.3119 1.1170 0.0745  -0.1068 -0.1967 411  GLU B CB  
4323  C  CG  . GLU B 411  ? 1.5046 1.4586 1.2681 0.0817  -0.1013 -0.1902 411  GLU B CG  
4324  C  CD  . GLU B 411  ? 1.5266 1.4650 1.2908 0.0758  -0.0900 -0.1827 411  GLU B CD  
4325  O  OE1 . GLU B 411  ? 1.4031 1.3504 1.1840 0.0671  -0.0861 -0.1817 411  GLU B OE1 
4326  O  OE2 . GLU B 411  ? 1.5256 1.4430 1.2734 0.0801  -0.0849 -0.1780 411  GLU B OE2 
4327  N  N   . MET B 412  ? 1.1741 1.2106 0.9965 0.0737  -0.1215 -0.2068 412  MET B N   
4328  C  CA  . MET B 412  ? 1.1483 1.2099 0.9911 0.0660  -0.1264 -0.2141 412  MET B CA  
4329  C  C   . MET B 412  ? 1.0695 1.1484 0.9119 0.0723  -0.1384 -0.2228 412  MET B C   
4330  O  O   . MET B 412  ? 1.0995 1.1956 0.9528 0.0645  -0.1447 -0.2329 412  MET B O   
4331  C  CB  . MET B 412  ? 1.1436 1.2144 1.0020 0.0658  -0.1211 -0.2070 412  MET B CB  
4332  C  CG  . MET B 412  ? 1.1933 1.2536 1.0577 0.0564  -0.1103 -0.2010 412  MET B CG  
4333  S  SD  . MET B 412  ? 1.0330 1.1088 0.9187 0.0539  -0.1058 -0.1956 412  MET B SD  
4334  C  CE  . MET B 412  ? 0.9896 1.0578 0.8656 0.0699  -0.1046 -0.1856 412  MET B CE  
4335  N  N   . ALA B 413  ? 1.0299 1.1046 0.8598 0.0866  -0.1418 -0.2191 413  ALA B N   
4336  C  CA  . ALA B 413  ? 1.0725 1.1626 0.9002 0.0941  -0.1534 -0.2269 413  ALA B CA  
4337  C  C   . ALA B 413  ? 1.1667 1.2529 0.9833 0.0915  -0.1599 -0.2364 413  ALA B C   
4338  O  O   . ALA B 413  ? 1.1285 1.2333 0.9509 0.0905  -0.1698 -0.2467 413  ALA B O   
4339  C  CB  . ALA B 413  ? 1.0939 1.1774 0.9087 0.1104  -0.1545 -0.2200 413  ALA B CB  
4340  N  N   . ALA B 414  ? 1.6431 1.7054 1.4436 0.0904  -0.1546 -0.2333 414  ALA B N   
4341  C  CA  . ALA B 414  ? 1.5938 1.6501 1.3829 0.0871  -0.1601 -0.2421 414  ALA B CA  
4342  C  C   . ALA B 414  ? 1.6493 1.7156 1.4529 0.0707  -0.1605 -0.2507 414  ALA B C   
4343  O  O   . ALA B 414  ? 1.7598 1.8264 1.5575 0.0666  -0.1667 -0.2602 414  ALA B O   
4344  C  CB  . ALA B 414  ? 1.6208 1.6477 1.3879 0.0912  -0.1536 -0.2358 414  ALA B CB  
4345  N  N   . GLY B 415  ? 1.0457 1.1198 0.8677 0.0612  -0.1541 -0.2478 415  GLY B N   
4346  C  CA  . GLY B 415  ? 0.9161 0.9994 0.7523 0.0454  -0.1536 -0.2555 415  GLY B CA  
4347  C  C   . GLY B 415  ? 1.0082 1.0694 0.8355 0.0363  -0.1461 -0.2542 415  GLY B C   
4348  O  O   . GLY B 415  ? 1.0461 1.1120 0.8809 0.0235  -0.1468 -0.2622 415  GLY B O   
4349  N  N   . ARG B 416  ? 1.5396 1.5768 1.3512 0.0426  -0.1385 -0.2445 416  ARG B N   
4350  C  CA  . ARG B 416  ? 1.6573 1.6722 1.4588 0.0353  -0.1313 -0.2430 416  ARG B CA  
4351  C  C   . ARG B 416  ? 1.6479 1.6616 1.4634 0.0239  -0.1217 -0.2387 416  ARG B C   
4352  O  O   . ARG B 416  ? 1.7021 1.7053 1.5157 0.0133  -0.1176 -0.2416 416  ARG B O   
4353  C  CB  . ARG B 416  ? 1.6419 1.6320 1.4216 0.0465  -0.1265 -0.2342 416  ARG B CB  
4354  C  CG  . ARG B 416  ? 1.5316 1.5185 1.2939 0.0578  -0.1351 -0.2382 416  ARG B CG  
4355  C  CD  . ARG B 416  ? 1.6716 1.6544 1.4255 0.0511  -0.1407 -0.2490 416  ARG B CD  
4356  N  NE  . ARG B 416  ? 1.9114 1.8894 1.6470 0.0625  -0.1488 -0.2526 416  ARG B NE  
4357  C  CZ  . ARG B 416  ? 1.9214 1.9183 1.6600 0.0667  -0.1601 -0.2609 416  ARG B CZ  
4358  N  NH1 . ARG B 416  ? 1.7833 1.8059 1.5432 0.0607  -0.1649 -0.2666 416  ARG B NH1 
4359  N  NH2 . ARG B 416  ? 1.8964 1.8862 1.6161 0.0777  -0.1668 -0.2634 416  ARG B NH2 
4360  N  N   . VAL B 417  ? 1.9894 2.0132 1.8183 0.0259  -0.1180 -0.2320 417  VAL B N   
4361  C  CA  . VAL B 417  ? 2.0289 2.0508 1.8700 0.0164  -0.1086 -0.2270 417  VAL B CA  
4362  C  C   . VAL B 417  ? 1.9402 1.9813 1.7998 0.0030  -0.1113 -0.2361 417  VAL B C   
4363  O  O   . VAL B 417  ? 1.9386 2.0019 1.8086 0.0034  -0.1199 -0.2435 417  VAL B O   
4364  C  CB  . VAL B 417  ? 2.0032 2.0286 1.8513 0.0238  -0.1038 -0.2165 417  VAL B CB  
4365  C  CG1 . VAL B 417  ? 2.0473 2.0522 1.8773 0.0359  -0.0998 -0.2073 417  VAL B CG1 
4366  C  CG2 . VAL B 417  ? 1.9013 1.9515 1.7620 0.0288  -0.1116 -0.2199 417  VAL B CG2 
4367  N  N   . GLU B 418  ? 1.2358 1.2682 1.0994 -0.0088 -0.1038 -0.2356 418  GLU B N   
4368  C  CA  . GLU B 418  ? 1.2479 1.2962 1.1291 -0.0227 -0.1043 -0.2432 418  GLU B CA  
4369  C  C   . GLU B 418  ? 1.1644 1.2158 1.0600 -0.0287 -0.0955 -0.2366 418  GLU B C   
4370  O  O   . GLU B 418  ? 1.1124 1.1825 1.0257 -0.0375 -0.0966 -0.2418 418  GLU B O   
4371  C  CB  . GLU B 418  ? 1.3605 1.3968 1.2343 -0.0337 -0.1038 -0.2507 418  GLU B CB  
4372  C  CG  . GLU B 418  ? 1.5395 1.5714 1.3982 -0.0288 -0.1125 -0.2580 418  GLU B CG  
4373  C  CD  . GLU B 418  ? 1.6563 1.6739 1.5064 -0.0396 -0.1112 -0.2648 418  GLU B CD  
4374  O  OE1 . GLU B 418  ? 1.6388 1.6497 1.4947 -0.0509 -0.1033 -0.2638 418  GLU B OE1 
4375  O  OE2 . GLU B 418  ? 1.6576 1.6698 1.4944 -0.0366 -0.1179 -0.2712 418  GLU B OE2 
4376  N  N   . THR B 419  ? 1.5484 1.5825 1.4369 -0.0240 -0.0869 -0.2256 419  THR B N   
4377  C  CA  . THR B 419  ? 1.4597 1.4955 1.3604 -0.0284 -0.0786 -0.2187 419  THR B CA  
4378  C  C   . THR B 419  ? 1.4384 1.4654 1.3333 -0.0164 -0.0744 -0.2071 419  THR B C   
4379  O  O   . THR B 419  ? 1.5583 1.5656 1.4363 -0.0096 -0.0719 -0.2022 419  THR B O   
4380  C  CB  . THR B 419  ? 1.3462 1.3660 1.2445 -0.0399 -0.0702 -0.2182 419  THR B CB  
4381  O  OG1 . THR B 419  ? 1.3947 1.4203 1.2963 -0.0511 -0.0742 -0.2293 419  THR B OG1 
4382  C  CG2 . THR B 419  ? 1.2304 1.2546 1.1425 -0.0449 -0.0624 -0.2121 419  THR B CG2 
4383  N  N   . LEU B 420  ? 0.9413 0.9828 0.8501 -0.0139 -0.0734 -0.2030 420  LEU B N   
4384  C  CA  . LEU B 420  ? 0.8962 0.9319 0.8017 -0.0030 -0.0698 -0.1925 420  LEU B CA  
4385  C  C   . LEU B 420  ? 0.9250 0.9623 0.8427 -0.0079 -0.0617 -0.1861 420  LEU B C   
4386  O  O   . LEU B 420  ? 0.8882 0.9444 0.8224 -0.0124 -0.0631 -0.1888 420  LEU B O   
4387  C  CB  . LEU B 420  ? 0.8266 0.8782 0.7352 0.0074  -0.0777 -0.1934 420  LEU B CB  
4388  C  CG  . LEU B 420  ? 0.8171 0.8625 0.7213 0.0192  -0.0746 -0.1831 420  LEU B CG  
4389  C  CD1 . LEU B 420  ? 0.9805 1.0011 0.8656 0.0249  -0.0700 -0.1772 420  LEU B CD1 
4390  C  CD2 . LEU B 420  ? 0.8905 0.9512 0.7966 0.0291  -0.0829 -0.1851 420  LEU B CD2 
4391  N  N   . ILE B 421  ? 1.0693 1.0871 0.9787 -0.0068 -0.0533 -0.1779 421  ILE B N   
4392  C  CA  . ILE B 421  ? 0.9425 0.9592 0.8611 -0.0102 -0.0453 -0.1710 421  ILE B CA  
4393  C  C   . ILE B 421  ? 1.0294 1.0436 0.9463 0.0011  -0.0433 -0.1617 421  ILE B C   
4394  O  O   . ILE B 421  ? 1.0316 1.0309 0.9345 0.0092  -0.0421 -0.1570 421  ILE B O   
4395  C  CB  . ILE B 421  ? 0.9596 0.9564 0.8707 -0.0174 -0.0371 -0.1686 421  ILE B CB  
4396  C  CG1 . ILE B 421  ? 0.9392 0.9379 0.8522 -0.0294 -0.0387 -0.1781 421  ILE B CG1 
4397  C  CG2 . ILE B 421  ? 0.9486 0.9436 0.8680 -0.0195 -0.0290 -0.1609 421  ILE B CG2 
4398  C  CD1 . ILE B 421  ? 1.0383 1.0216 0.9345 -0.0292 -0.0409 -0.1822 421  ILE B CD1 
4399  N  N   . MET B 422  ? 1.1226 1.1512 1.0538 0.0016  -0.0426 -0.1590 422  MET B N   
4400  C  CA  . MET B 422  ? 1.0335 1.0613 0.9649 0.0115  -0.0408 -0.1506 422  MET B CA  
4401  C  C   . MET B 422  ? 1.0174 1.0431 0.9574 0.0076  -0.0329 -0.1441 422  MET B C   
4402  O  O   . MET B 422  ? 0.9898 1.0261 0.9421 -0.0009 -0.0317 -0.1472 422  MET B O   
4403  C  CB  . MET B 422  ? 0.8956 0.9430 0.8353 0.0175  -0.0482 -0.1532 422  MET B CB  
4404  C  CG  . MET B 422  ? 0.9659 1.0190 0.8992 0.0207  -0.0570 -0.1609 422  MET B CG  
4405  S  SD  . MET B 422  ? 1.0766 1.1575 1.0244 0.0237  -0.0658 -0.1666 422  MET B SD  
4406  C  CE  . MET B 422  ? 1.2201 1.3110 1.1688 0.0161  -0.0734 -0.1794 422  MET B CE  
4407  N  N   . ILE B 423  ? 1.0264 1.0387 0.9598 0.0139  -0.0274 -0.1352 423  ILE B N   
4408  C  CA  . ILE B 423  ? 0.9863 0.9958 0.9267 0.0115  -0.0201 -0.1286 423  ILE B CA  
4409  C  C   . ILE B 423  ? 1.0106 1.0268 0.9564 0.0201  -0.0203 -0.1226 423  ILE B C   
4410  O  O   . ILE B 423  ? 1.0440 1.0485 0.9821 0.0273  -0.0171 -0.1156 423  ILE B O   
4411  C  CB  . ILE B 423  ? 0.9273 0.9152 0.8564 0.0106  -0.0126 -0.1234 423  ILE B CB  
4412  C  CG1 . ILE B 423  ? 1.0065 0.9862 0.9285 0.0027  -0.0126 -0.1298 423  ILE B CG1 
4413  C  CG2 . ILE B 423  ? 0.9685 0.9544 0.9052 0.0077  -0.0054 -0.1173 423  ILE B CG2 
4414  C  CD1 . ILE B 423  ? 1.0736 1.0321 0.9847 0.0012  -0.0051 -0.1251 423  ILE B CD1 
4415  N  N   . GLY B 424  ? 1.0012 1.0362 0.9603 0.0192  -0.0241 -0.1252 424  GLY B N   
4416  C  CA  . GLY B 424  ? 1.0094 1.0515 0.9739 0.0270  -0.0247 -0.1202 424  GLY B CA  
4417  C  C   . GLY B 424  ? 1.0369 1.0781 0.9927 0.0372  -0.0300 -0.1199 424  GLY B C   
4418  O  O   . GLY B 424  ? 1.2018 1.2382 1.1476 0.0387  -0.0338 -0.1240 424  GLY B O   
4419  N  N   . GLY B 425  ? 1.1553 1.2010 1.1148 0.0445  -0.0302 -0.1150 425  GLY B N   
4420  C  CA  . GLY B 425  ? 1.4390 1.4824 1.3899 0.0549  -0.0341 -0.1134 425  GLY B CA  
4421  C  C   . GLY B 425  ? 1.4893 1.5503 1.4461 0.0586  -0.0420 -0.1187 425  GLY B C   
4422  O  O   . GLY B 425  ? 1.5012 1.5620 1.4533 0.0680  -0.0445 -0.1161 425  GLY B O   
4423  N  N   . ASN B 426  ? 1.2123 1.2886 1.1792 0.0516  -0.0458 -0.1261 426  ASN B N   
4424  C  CA  . ASN B 426  ? 1.2111 1.3061 1.1848 0.0545  -0.0536 -0.1319 426  ASN B CA  
4425  C  C   . ASN B 426  ? 1.1683 1.2599 1.1292 0.0634  -0.0598 -0.1341 426  ASN B C   
4426  O  O   . ASN B 426  ? 1.1608 1.2535 1.1187 0.0730  -0.0619 -0.1309 426  ASN B O   
4427  C  CB  . ASN B 426  ? 1.1507 1.2556 1.1346 0.0586  -0.0529 -0.1278 426  ASN B CB  
4428  C  CG  . ASN B 426  ? 1.0961 1.2233 1.0917 0.0582  -0.0595 -0.1345 426  ASN B CG  
4429  O  OD1 . ASN B 426  ? 1.1333 1.2697 1.1302 0.0549  -0.0649 -0.1423 426  ASN B OD1 
4430  N  ND2 . ASN B 426  ? 1.0844 1.2208 1.0890 0.0616  -0.0591 -0.1315 426  ASN B ND2 
4431  N  N   . PRO B 427  ? 1.2124 1.2993 1.1650 0.0606  -0.0626 -0.1396 427  PRO B N   
4432  C  CA  . PRO B 427  ? 1.1882 1.2697 1.1267 0.0696  -0.0681 -0.1412 427  PRO B CA  
4433  C  C   . PRO B 427  ? 1.2378 1.3372 1.1806 0.0756  -0.0768 -0.1465 427  PRO B C   
4434  O  O   . PRO B 427  ? 1.2776 1.3727 1.2098 0.0861  -0.0802 -0.1449 427  PRO B O   
4435  C  CB  . PRO B 427  ? 1.2380 1.3116 1.1685 0.0634  -0.0690 -0.1467 427  PRO B CB  
4436  C  CG  . PRO B 427  ? 1.2492 1.3180 1.1865 0.0526  -0.0617 -0.1451 427  PRO B CG  
4437  C  CD  . PRO B 427  ? 1.2925 1.3768 1.2468 0.0495  -0.0606 -0.1441 427  PRO B CD  
4438  N  N   . VAL B 428  ? 0.8169 0.9361 0.7747 0.0695  -0.0804 -0.1528 428  VAL B N   
4439  C  CA  . VAL B 428  ? 0.7951 0.9328 0.7576 0.0752  -0.0891 -0.1585 428  VAL B CA  
4440  C  C   . VAL B 428  ? 0.7456 0.8846 0.7081 0.0855  -0.0889 -0.1523 428  VAL B C   
4441  O  O   . VAL B 428  ? 0.7156 0.8591 0.6722 0.0953  -0.0951 -0.1539 428  VAL B O   
4442  C  CB  . VAL B 428  ? 0.7752 0.9343 0.7552 0.0657  -0.0919 -0.1662 428  VAL B CB  
4443  C  CG1 . VAL B 428  ? 0.7776 0.9575 0.7659 0.0722  -0.0992 -0.1702 428  VAL B CG1 
4444  C  CG2 . VAL B 428  ? 0.9280 1.0879 0.9062 0.0574  -0.0948 -0.1744 428  VAL B CG2 
4445  N  N   . TYR B 429  ? 0.8659 1.0001 0.8343 0.0838  -0.0817 -0.1451 429  TYR B N   
4446  C  CA  . TYR B 429  ? 0.8677 1.0027 0.8369 0.0926  -0.0809 -0.1392 429  TYR B CA  
4447  C  C   . TYR B 429  ? 0.8956 1.0096 0.8496 0.1005  -0.0768 -0.1311 429  TYR B C   
4448  O  O   . TYR B 429  ? 0.8597 0.9725 0.8089 0.1104  -0.0784 -0.1278 429  TYR B O   
4449  C  CB  . TYR B 429  ? 0.9640 1.1059 0.9481 0.0868  -0.0757 -0.1360 429  TYR B CB  
4450  C  CG  . TYR B 429  ? 1.0181 1.1589 1.0032 0.0948  -0.0739 -0.1293 429  TYR B CG  
4451  C  CD1 . TYR B 429  ? 0.9833 1.1379 0.9719 0.1022  -0.0798 -0.1317 429  TYR B CD1 
4452  C  CD2 . TYR B 429  ? 0.9731 1.0991 0.9554 0.0951  -0.0662 -0.1209 429  TYR B CD2 
4453  C  CE1 . TYR B 429  ? 0.9418 1.0943 0.9307 0.1094  -0.0780 -0.1258 429  TYR B CE1 
4454  C  CE2 . TYR B 429  ? 0.8759 1.0004 0.8590 0.1020  -0.0646 -0.1151 429  TYR B CE2 
4455  C  CZ  . TYR B 429  ? 0.8803 1.0176 0.8664 0.1090  -0.0704 -0.1176 429  TYR B CZ  
4456  O  OH  . TYR B 429  ? 0.9203 1.0551 0.9067 0.1157  -0.0685 -0.1120 429  TYR B OH  
4457  N  N   . ASN B 430  ? 1.3800 1.4772 1.3260 0.0966  -0.0713 -0.1280 430  ASN B N   
4458  C  CA  . ASN B 430  ? 1.3676 1.4451 1.3008 0.1031  -0.0660 -0.1199 430  ASN B CA  
4459  C  C   . ASN B 430  ? 1.4126 1.4796 1.3284 0.1108  -0.0696 -0.1210 430  ASN B C   
4460  O  O   . ASN B 430  ? 1.3654 1.4191 1.2704 0.1189  -0.0669 -0.1148 430  ASN B O   
4461  C  CB  . ASN B 430  ? 1.3626 1.4270 1.2961 0.0956  -0.0576 -0.1153 430  ASN B CB  
4462  C  CG  . ASN B 430  ? 1.3971 1.4660 1.3438 0.0916  -0.0524 -0.1107 430  ASN B CG  
4463  O  OD1 . ASN B 430  ? 1.4483 1.5247 1.4006 0.0964  -0.0534 -0.1085 430  ASN B OD1 
4464  N  ND2 . ASN B 430  ? 1.4081 1.4720 1.3591 0.0830  -0.0466 -0.1093 430  ASN B ND2 
4465  N  N   . ALA B 431  ? 1.1898 1.2620 1.1024 0.1084  -0.0755 -0.1289 431  ALA B N   
4466  C  CA  . ALA B 431  ? 1.1881 1.2499 1.0833 0.1157  -0.0792 -0.1304 431  ALA B CA  
4467  C  C   . ALA B 431  ? 1.1594 1.2255 1.0490 0.1277  -0.0845 -0.1298 431  ALA B C   
4468  O  O   . ALA B 431  ? 1.0898 1.1722 0.9904 0.1291  -0.0882 -0.1319 431  ALA B O   
4469  C  CB  . ALA B 431  ? 1.2416 1.3100 1.1358 0.1101  -0.0851 -0.1398 431  ALA B CB  
4470  N  N   . PRO B 432  ? 1.0990 1.1501 0.9710 0.1368  -0.0845 -0.1267 432  PRO B N   
4471  C  CA  . PRO B 432  ? 1.1574 1.2107 1.0219 0.1489  -0.0895 -0.1261 432  PRO B CA  
4472  C  C   . PRO B 432  ? 1.1496 1.2218 1.0178 0.1506  -0.0999 -0.1356 432  PRO B C   
4473  O  O   . PRO B 432  ? 1.0839 1.1639 0.9557 0.1437  -0.1039 -0.1431 432  PRO B O   
4474  C  CB  . PRO B 432  ? 1.1921 1.2243 1.0357 0.1566  -0.0872 -0.1219 432  PRO B CB  
4475  C  CG  . PRO B 432  ? 1.1168 1.1347 0.9598 0.1493  -0.0784 -0.1170 432  PRO B CG  
4476  C  CD  . PRO B 432  ? 1.0144 1.0444 0.8722 0.1369  -0.0790 -0.1226 432  PRO B CD  
4477  N  N   . GLY B 433  ? 1.3636 1.4433 1.2309 0.1602  -0.1044 -0.1354 433  GLY B N   
4478  C  CA  . GLY B 433  ? 1.4650 1.5647 1.3375 0.1626  -0.1144 -0.1441 433  GLY B CA  
4479  C  C   . GLY B 433  ? 1.4734 1.5708 1.3319 0.1672  -0.1215 -0.1504 433  GLY B C   
4480  O  O   . GLY B 433  ? 1.4076 1.5220 1.2726 0.1645  -0.1294 -0.1595 433  GLY B O   
4481  N  N   . ASP B 434  ? 2.0250 2.1017 1.8643 0.1740  -0.1189 -0.1457 434  ASP B N   
4482  C  CA  . ASP B 434  ? 2.0924 2.1651 1.9163 0.1796  -0.1256 -0.1512 434  ASP B CA  
4483  C  C   . ASP B 434  ? 2.0257 2.0966 1.8498 0.1693  -0.1258 -0.1568 434  ASP B C   
4484  O  O   . ASP B 434  ? 2.0991 2.1669 1.9108 0.1728  -0.1316 -0.1621 434  ASP B O   
4485  C  CB  . ASP B 434  ? 2.1841 2.2343 1.9864 0.1908  -0.1221 -0.1440 434  ASP B CB  
4486  C  CG  . ASP B 434  ? 2.1007 2.1312 1.8996 0.1866  -0.1108 -0.1351 434  ASP B CG  
4487  O  OD1 . ASP B 434  ? 2.1575 2.1920 1.9712 0.1759  -0.1057 -0.1338 434  ASP B OD1 
4488  O  OD2 . ASP B 434  ? 2.0313 2.0425 1.8129 0.1942  -0.1070 -0.1293 434  ASP B OD2 
4489  N  N   . LEU B 435  ? 1.3540 1.4262 1.1913 0.1570  -0.1198 -0.1558 435  LEU B N   
4490  C  CA  . LEU B 435  ? 1.3059 1.3751 1.1434 0.1468  -0.1194 -0.1608 435  LEU B CA  
4491  C  C   . LEU B 435  ? 1.3078 1.3996 1.1610 0.1380  -0.1261 -0.1711 435  LEU B C   
4492  O  O   . LEU B 435  ? 1.3396 1.4310 1.1901 0.1317  -0.1289 -0.1777 435  LEU B O   
4493  C  CB  . LEU B 435  ? 1.2448 1.3005 1.0859 0.1384  -0.1086 -0.1539 435  LEU B CB  
4494  C  CG  . LEU B 435  ? 1.2359 1.2673 1.0603 0.1448  -0.1013 -0.1449 435  LEU B CG  
4495  C  CD1 . LEU B 435  ? 1.1330 1.1528 0.9615 0.1356  -0.0916 -0.1396 435  LEU B CD1 
4496  C  CD2 . LEU B 435  ? 1.4022 1.4220 1.2065 0.1514  -0.1055 -0.1479 435  LEU B CD2 
4497  N  N   . ARG B 436  ? 1.4594 1.5705 1.3287 0.1372  -0.1285 -0.1726 436  ARG B N   
4498  C  CA  . ARG B 436  ? 1.4646 1.5993 1.3505 0.1292  -0.1347 -0.1823 436  ARG B CA  
4499  C  C   . ARG B 436  ? 1.4671 1.6002 1.3615 0.1143  -0.1300 -0.1848 436  ARG B C   
4500  O  O   . ARG B 436  ? 1.5412 1.6792 1.4357 0.1081  -0.1345 -0.1931 436  ARG B O   
4501  C  CB  . ARG B 436  ? 1.5890 1.7340 1.4681 0.1352  -0.1459 -0.1915 436  ARG B CB  
4502  C  CG  . ARG B 436  ? 1.5644 1.7111 1.4340 0.1506  -0.1512 -0.1895 436  ARG B CG  
4503  C  CD  . ARG B 436  ? 1.5818 1.7370 1.4629 0.1538  -0.1483 -0.1841 436  ARG B CD  
4504  N  NE  . ARG B 436  ? 1.6202 1.8024 1.5182 0.1521  -0.1553 -0.1916 436  ARG B NE  
4505  C  CZ  . ARG B 436  ? 1.6127 1.8070 1.5257 0.1509  -0.1530 -0.1892 436  ARG B CZ  
4506  N  NH1 . ARG B 436  ? 1.6231 1.8055 1.5368 0.1510  -0.1443 -0.1797 436  ARG B NH1 
4507  N  NH2 . ARG B 436  ? 1.5726 1.7920 1.5004 0.1495  -0.1598 -0.1968 436  ARG B NH2 
4508  N  N   . PHE B 437  ? 1.0342 1.1600 0.9355 0.1087  -0.1207 -0.1776 437  PHE B N   
4509  C  CA  . PHE B 437  ? 1.0089 1.1306 0.9169 0.0952  -0.1151 -0.1787 437  PHE B CA  
4510  C  C   . PHE B 437  ? 1.1141 1.2583 1.0405 0.0851  -0.1190 -0.1874 437  PHE B C   
4511  O  O   . PHE B 437  ? 1.1190 1.2632 1.0476 0.0750  -0.1190 -0.1932 437  PHE B O   
4512  C  CB  . PHE B 437  ? 0.8767 0.9861 0.7877 0.0926  -0.1045 -0.1687 437  PHE B CB  
4513  C  CG  . PHE B 437  ? 0.8789 0.9757 0.7892 0.0819  -0.0977 -0.1678 437  PHE B CG  
4514  C  CD1 . PHE B 437  ? 0.8934 1.0007 0.8187 0.0696  -0.0959 -0.1719 437  PHE B CD1 
4515  C  CD2 . PHE B 437  ? 0.9017 0.9758 0.7959 0.0845  -0.0928 -0.1627 437  PHE B CD2 
4516  C  CE1 . PHE B 437  ? 0.8267 0.9214 0.7504 0.0601  -0.0894 -0.1709 437  PHE B CE1 
4517  C  CE2 . PHE B 437  ? 0.8856 0.9477 0.7786 0.0752  -0.0865 -0.1617 437  PHE B CE2 
4518  C  CZ  . PHE B 437  ? 0.8041 0.8761 0.7115 0.0632  -0.0849 -0.1658 437  PHE B CZ  
4519  N  N   . ALA B 438  ? 1.1039 1.2674 1.0438 0.0875  -0.1221 -0.1886 438  ALA B N   
4520  C  CA  . ALA B 438  ? 1.0759 1.2618 1.0345 0.0778  -0.1252 -0.1965 438  ALA B CA  
4521  C  C   . ALA B 438  ? 1.1846 1.3823 1.1421 0.0764  -0.1346 -0.2077 438  ALA B C   
4522  O  O   . ALA B 438  ? 1.2227 1.4304 1.1908 0.0647  -0.1354 -0.2149 438  ALA B O   
4523  C  CB  . ALA B 438  ? 1.1482 1.3517 1.1202 0.0822  -0.1265 -0.1950 438  ALA B CB  
4524  N  N   . ASP B 439  ? 1.5180 1.7148 1.4628 0.0880  -0.1419 -0.2095 439  ASP B N   
4525  C  CA  . ASP B 439  ? 1.5611 1.7696 1.5043 0.0876  -0.1516 -0.2204 439  ASP B CA  
4526  C  C   . ASP B 439  ? 1.5789 1.7722 1.5119 0.0800  -0.1501 -0.2236 439  ASP B C   
4527  O  O   . ASP B 439  ? 1.5535 1.7578 1.4935 0.0709  -0.1544 -0.2331 439  ASP B O   
4528  C  CB  . ASP B 439  ? 1.6175 1.8276 1.5482 0.1031  -0.1597 -0.2210 439  ASP B CB  
4529  C  CG  . ASP B 439  ? 1.5765 1.8021 1.5167 0.1110  -0.1618 -0.2187 439  ASP B CG  
4530  O  OD1 . ASP B 439  ? 1.4856 1.7196 1.4416 0.1047  -0.1566 -0.2161 439  ASP B OD1 
4531  O  OD2 . ASP B 439  ? 1.6104 1.8393 1.5417 0.1238  -0.1685 -0.2195 439  ASP B OD2 
4532  N  N   . ARG B 440  ? 1.6632 1.8311 1.5797 0.0835  -0.1440 -0.2158 440  ARG B N   
4533  C  CA  . ARG B 440  ? 1.6508 1.8023 1.5564 0.0769  -0.1418 -0.2180 440  ARG B CA  
4534  C  C   . ARG B 440  ? 1.5635 1.7130 1.4805 0.0619  -0.1343 -0.2181 440  ARG B C   
4535  O  O   . ARG B 440  ? 1.6248 1.7661 1.5369 0.0538  -0.1338 -0.2227 440  ARG B O   
4536  C  CB  . ARG B 440  ? 1.5826 1.7077 1.4671 0.0858  -0.1371 -0.2094 440  ARG B CB  
4537  C  CG  . ARG B 440  ? 1.5716 1.6918 1.4383 0.0972  -0.1449 -0.2125 440  ARG B CG  
4538  C  CD  . ARG B 440  ? 1.5870 1.7163 1.4527 0.1105  -0.1495 -0.2099 440  ARG B CD  
4539  N  NE  . ARG B 440  ? 1.6361 1.7577 1.4825 0.1226  -0.1560 -0.2116 440  ARG B NE  
4540  C  CZ  . ARG B 440  ? 1.6730 1.7766 1.5028 0.1339  -0.1527 -0.2033 440  ARG B CZ  
4541  N  NH1 . ARG B 440  ? 1.6266 1.7183 1.4570 0.1348  -0.1433 -0.1928 440  ARG B NH1 
4542  N  NH2 . ARG B 440  ? 1.8167 1.9140 1.6287 0.1446  -0.1591 -0.2056 440  ARG B NH2 
4543  N  N   . MET B 441  ? 1.2449 1.4011 1.1763 0.0581  -0.1285 -0.2131 441  MET B N   
4544  C  CA  . MET B 441  ? 1.2282 1.3827 1.1704 0.0443  -0.1211 -0.2128 441  MET B CA  
4545  C  C   . MET B 441  ? 1.2041 1.3758 1.1584 0.0329  -0.1260 -0.2243 441  MET B C   
4546  O  O   . MET B 441  ? 1.1437 1.3096 1.1016 0.0208  -0.1209 -0.2261 441  MET B O   
4547  C  CB  . MET B 441  ? 1.1647 1.3248 1.1199 0.0438  -0.1148 -0.2056 441  MET B CB  
4548  C  CG  . MET B 441  ? 1.2055 1.3581 1.1679 0.0318  -0.1054 -0.2024 441  MET B CG  
4549  S  SD  . MET B 441  ? 1.2712 1.4295 1.2469 0.0331  -0.0987 -0.1936 441  MET B SD  
4550  C  CE  . MET B 441  ? 0.8595 1.0119 0.8438 0.0175  -0.0895 -0.1931 441  MET B CE  
4551  N  N   . ALA B 442  ? 1.6180 1.8108 1.5786 0.0365  -0.1357 -0.2322 442  ALA B N   
4552  C  CA  . ALA B 442  ? 1.6739 1.8847 1.6468 0.0258  -0.1409 -0.2438 442  ALA B CA  
4553  C  C   . ALA B 442  ? 1.7610 1.9596 1.7212 0.0210  -0.1434 -0.2500 442  ALA B C   
4554  O  O   . ALA B 442  ? 1.7888 1.9946 1.7576 0.0085  -0.1441 -0.2580 442  ALA B O   
4555  C  CB  . ALA B 442  ? 1.6902 1.9274 1.6729 0.0320  -0.1510 -0.2507 442  ALA B CB  
4556  N  N   . SER B 443  ? 2.0384 2.2181 1.9781 0.0307  -0.1446 -0.2464 443  SER B N   
4557  C  CA  . SER B 443  ? 2.0323 2.2004 1.9584 0.0276  -0.1479 -0.2526 443  SER B CA  
4558  C  C   . SER B 443  ? 2.0469 2.1991 1.9722 0.0146  -0.1392 -0.2516 443  SER B C   
4559  O  O   . SER B 443  ? 2.0743 2.2268 1.9992 0.0053  -0.1419 -0.2602 443  SER B O   
4560  C  CB  . SER B 443  ? 1.9797 2.1297 1.8833 0.0415  -0.1499 -0.2479 443  SER B CB  
4561  O  OG  . SER B 443  ? 2.0595 2.1856 1.9528 0.0435  -0.1398 -0.2368 443  SER B OG  
4562  N  N   . VAL B 444  ? 1.5829 1.7209 1.5076 0.0137  -0.1290 -0.2414 444  VAL B N   
4563  C  CA  . VAL B 444  ? 1.4667 1.5896 1.3910 0.0018  -0.1203 -0.2397 444  VAL B CA  
4564  C  C   . VAL B 444  ? 1.3284 1.4692 1.2739 -0.0114 -0.1186 -0.2448 444  VAL B C   
4565  O  O   . VAL B 444  ? 1.4046 1.5608 1.3645 -0.0102 -0.1176 -0.2420 444  VAL B O   
4566  C  CB  . VAL B 444  ? 1.4346 1.5363 1.3504 0.0063  -0.1102 -0.2271 444  VAL B CB  
4567  C  CG1 . VAL B 444  ? 1.4819 1.5941 1.4092 0.0117  -0.1076 -0.2199 444  VAL B CG1 
4568  C  CG2 . VAL B 444  ? 1.3881 1.4750 1.3038 -0.0056 -0.1012 -0.2254 444  VAL B CG2 
4569  N  N   . PRO B 445  ? 1.3025 1.4424 1.2503 -0.0241 -0.1183 -0.2526 445  PRO B N   
4570  C  CA  . PRO B 445  ? 1.3275 1.4859 1.2958 -0.0369 -0.1171 -0.2583 445  PRO B CA  
4571  C  C   . PRO B 445  ? 1.3303 1.4830 1.3068 -0.0423 -0.1062 -0.2499 445  PRO B C   
4572  O  O   . PRO B 445  ? 1.3826 1.5540 1.3767 -0.0456 -0.1054 -0.2503 445  PRO B O   
4573  C  CB  . PRO B 445  ? 1.3730 1.5266 1.3380 -0.0487 -0.1188 -0.2680 445  PRO B CB  
4574  C  CG  . PRO B 445  ? 1.5283 1.6710 1.4742 -0.0395 -0.1256 -0.2704 445  PRO B CG  
4575  C  CD  . PRO B 445  ? 1.5011 1.6262 1.4335 -0.0267 -0.1210 -0.2582 445  PRO B CD  
4576  N  N   . LEU B 446  ? 1.2003 1.3278 1.1643 -0.0429 -0.0978 -0.2423 446  LEU B N   
4577  C  CA  . LEU B 446  ? 1.1146 1.2347 1.0848 -0.0485 -0.0873 -0.2347 446  LEU B CA  
4578  C  C   . LEU B 446  ? 1.0939 1.2040 1.0576 -0.0365 -0.0832 -0.2229 446  LEU B C   
4579  O  O   . LEU B 446  ? 1.0927 1.1831 1.0394 -0.0293 -0.0816 -0.2178 446  LEU B O   
4580  C  CB  . LEU B 446  ? 1.1205 1.2197 1.0822 -0.0588 -0.0802 -0.2349 446  LEU B CB  
4581  C  CG  . LEU B 446  ? 1.0831 1.1762 1.0524 -0.0668 -0.0696 -0.2289 446  LEU B CG  
4582  C  CD1 . LEU B 446  ? 1.1799 1.2970 1.1706 -0.0753 -0.0702 -0.2339 446  LEU B CD1 
4583  C  CD2 . LEU B 446  ? 1.0739 1.1445 1.0323 -0.0759 -0.0630 -0.2293 446  LEU B CD2 
4584  N  N   . THR B 447  ? 1.1984 1.3223 1.1757 -0.0344 -0.0815 -0.2188 447  THR B N   
4585  C  CA  . THR B 447  ? 1.1887 1.3049 1.1625 -0.0245 -0.0770 -0.2077 447  THR B CA  
4586  C  C   . THR B 447  ? 1.1795 1.2932 1.1629 -0.0316 -0.0677 -0.2021 447  THR B C   
4587  O  O   . THR B 447  ? 1.1734 1.3029 1.1722 -0.0402 -0.0673 -0.2065 447  THR B O   
4588  C  CB  . THR B 447  ? 1.2228 1.3571 1.2030 -0.0140 -0.0838 -0.2075 447  THR B CB  
4589  O  OG1 . THR B 447  ? 1.2445 1.4037 1.2413 -0.0200 -0.0892 -0.2162 447  THR B OG1 
4590  C  CG2 . THR B 447  ? 1.1791 1.3074 1.1441 -0.0030 -0.0906 -0.2085 447  THR B CG2 
4591  N  N   . ILE B 448  ? 0.9595 1.0537 0.9336 -0.0279 -0.0603 -0.1926 448  ILE B N   
4592  C  CA  . ILE B 448  ? 0.8167 0.9053 0.7971 -0.0337 -0.0511 -0.1866 448  ILE B CA  
4593  C  C   . ILE B 448  ? 0.7621 0.8440 0.7394 -0.0233 -0.0475 -0.1760 448  ILE B C   
4594  O  O   . ILE B 448  ? 0.8200 0.8890 0.7838 -0.0143 -0.0482 -0.1718 448  ILE B O   
4595  C  CB  . ILE B 448  ? 0.8020 0.8703 0.7732 -0.0422 -0.0444 -0.1863 448  ILE B CB  
4596  C  CG1 . ILE B 448  ? 0.8161 0.8906 0.7904 -0.0533 -0.0479 -0.1972 448  ILE B CG1 
4597  C  CG2 . ILE B 448  ? 0.8813 0.9432 0.8578 -0.0470 -0.0350 -0.1796 448  ILE B CG2 
4598  C  CD1 . ILE B 448  ? 0.7431 0.7955 0.7046 -0.0602 -0.0428 -0.1979 448  ILE B CD1 
4599  N  N   . HIS B 449  ? 0.7467 0.8372 0.7363 -0.0246 -0.0436 -0.1719 449  HIS B N   
4600  C  CA  . HIS B 449  ? 0.7888 0.8755 0.7773 -0.0151 -0.0409 -0.1626 449  HIS B CA  
4601  C  C   . HIS B 449  ? 0.7611 0.8452 0.7572 -0.0198 -0.0327 -0.1568 449  HIS B C   
4602  O  O   . HIS B 449  ? 0.7717 0.8667 0.7797 -0.0286 -0.0312 -0.1605 449  HIS B O   
4603  C  CB  . HIS B 449  ? 0.7931 0.8984 0.7891 -0.0070 -0.0478 -0.1639 449  HIS B CB  
4604  C  CG  . HIS B 449  ? 0.8241 0.9226 0.8145 0.0046  -0.0466 -0.1553 449  HIS B CG  
4605  N  ND1 . HIS B 449  ? 0.8106 0.9135 0.8095 0.0069  -0.0428 -0.1491 449  HIS B ND1 
4606  C  CD2 . HIS B 449  ? 0.9295 1.0165 0.9063 0.0142  -0.0484 -0.1519 449  HIS B CD2 
4607  C  CE1 . HIS B 449  ? 0.9214 1.0162 0.9128 0.0171  -0.0424 -0.1425 449  HIS B CE1 
4608  N  NE2 . HIS B 449  ? 0.9809 1.0658 0.9587 0.0217  -0.0455 -0.1439 449  HIS B NE2 
4609  N  N   . LEU B 450  ? 1.1097 1.1794 1.0988 -0.0138 -0.0274 -0.1478 450  LEU B N   
4610  C  CA  . LEU B 450  ? 1.1836 1.2514 1.1793 -0.0152 -0.0205 -0.1411 450  LEU B CA  
4611  C  C   . LEU B 450  ? 1.2145 1.2873 1.2126 -0.0047 -0.0220 -0.1352 450  LEU B C   
4612  O  O   . LEU B 450  ? 1.2098 1.2712 1.1973 0.0036  -0.0219 -0.1304 450  LEU B O   
4613  C  CB  . LEU B 450  ? 0.9906 1.0366 0.9761 -0.0172 -0.0127 -0.1355 450  LEU B CB  
4614  C  CG  . LEU B 450  ? 1.1655 1.2016 1.1455 -0.0269 -0.0101 -0.1402 450  LEU B CG  
4615  C  CD1 . LEU B 450  ? 1.3414 1.3642 1.3061 -0.0228 -0.0126 -0.1415 450  LEU B CD1 
4616  C  CD2 . LEU B 450  ? 1.0782 1.1010 1.0566 -0.0315 -0.0011 -0.1347 450  LEU B CD2 
4617  N  N   . SER B 451  ? 1.1229 1.2121 1.1345 -0.0051 -0.0229 -0.1354 451  SER B N   
4618  C  CA  . SER B 451  ? 1.1470 1.2426 1.1613 0.0047  -0.0252 -0.1310 451  SER B CA  
4619  C  C   . SER B 451  ? 1.3005 1.3984 1.3232 0.0049  -0.0202 -0.1249 451  SER B C   
4620  O  O   . SER B 451  ? 1.4320 1.5326 1.4559 0.0131  -0.0213 -0.1205 451  SER B O   
4621  C  CB  . SER B 451  ? 1.2420 1.3574 1.2636 0.0075  -0.0335 -0.1374 451  SER B CB  
4622  O  OG  . SER B 451  ? 1.3291 1.4451 1.3471 0.0187  -0.0367 -0.1335 451  SER B OG  
4623  N  N   . GLN B 452  ? 1.1992 1.2961 1.2276 -0.0036 -0.0147 -0.1247 452  GLN B N   
4624  C  CA  . GLN B 452  ? 1.2633 1.3631 1.2998 -0.0038 -0.0100 -0.1195 452  GLN B CA  
4625  C  C   . GLN B 452  ? 1.2100 1.3307 1.2595 -0.0022 -0.0143 -0.1223 452  GLN B C   
4626  O  O   . GLN B 452  ? 1.2159 1.3424 1.2740 -0.0035 -0.0112 -0.1196 452  GLN B O   
4627  C  CB  . GLN B 452  ? 1.2114 1.2975 1.2407 0.0040  -0.0064 -0.1107 452  GLN B CB  
4628  C  CG  . GLN B 452  ? 1.2616 1.3489 1.2977 0.0049  -0.0018 -0.1048 452  GLN B CG  
4629  C  CD  . GLN B 452  ? 1.1466 1.2226 1.1760 0.0134  0.0001  -0.0973 452  GLN B CD  
4630  O  OE1 . GLN B 452  ? 0.9016 0.9630 0.9200 0.0156  0.0018  -0.0949 452  GLN B OE1 
4631  N  NE2 . GLN B 452  ? 1.2113 1.2941 1.2474 0.0181  0.0000  -0.0936 452  GLN B NE2 
4632  N  N   . PHE B 453  ? 0.9916 1.1238 1.0424 0.0008  -0.0216 -0.1280 453  PHE B N   
4633  C  CA  . PHE B 453  ? 0.9697 1.1229 1.0324 0.0023  -0.0265 -0.1320 453  PHE B CA  
4634  C  C   . PHE B 453  ? 1.0147 1.1786 1.0791 -0.0013 -0.0327 -0.1411 453  PHE B C   
4635  O  O   . PHE B 453  ? 1.0359 1.1898 1.0909 -0.0034 -0.0335 -0.1436 453  PHE B O   
4636  C  CB  . PHE B 453  ? 1.0054 1.1612 1.0666 0.0139  -0.0300 -0.1280 453  PHE B CB  
4637  C  CG  . PHE B 453  ? 1.0069 1.1566 1.0695 0.0171  -0.0248 -0.1200 453  PHE B CG  
4638  C  CD1 . PHE B 453  ? 0.9648 1.1270 1.0392 0.0161  -0.0238 -0.1196 453  PHE B CD1 
4639  C  CD2 . PHE B 453  ? 1.0169 1.1485 1.0691 0.0214  -0.0210 -0.1132 453  PHE B CD2 
4640  C  CE1 . PHE B 453  ? 0.9592 1.1156 1.0346 0.0192  -0.0193 -0.1125 453  PHE B CE1 
4641  C  CE2 . PHE B 453  ? 0.9055 1.0320 0.9594 0.0243  -0.0165 -0.1063 453  PHE B CE2 
4642  C  CZ  . PHE B 453  ? 0.9593 1.0980 1.0246 0.0232  -0.0158 -0.1060 453  PHE B CZ  
4643  N  N   . VAL B 454  ? 0.9859 1.1707 1.0625 -0.0021 -0.0370 -0.1464 454  VAL B N   
4644  C  CA  . VAL B 454  ? 0.8750 1.0723 0.9536 -0.0035 -0.0442 -0.1553 454  VAL B CA  
4645  C  C   . VAL B 454  ? 0.9003 1.0995 0.9723 0.0086  -0.0510 -0.1546 454  VAL B C   
4646  O  O   . VAL B 454  ? 0.8896 1.1053 0.9693 0.0136  -0.0559 -0.1569 454  VAL B O   
4647  C  CB  . VAL B 454  ? 0.8354 1.0551 0.9303 -0.0101 -0.0459 -0.1619 454  VAL B CB  
4648  C  CG1 . VAL B 454  ? 0.7732 1.0044 0.8701 -0.0137 -0.0527 -0.1717 454  VAL B CG1 
4649  C  CG2 . VAL B 454  ? 0.9706 1.1869 1.0717 -0.0208 -0.0379 -0.1606 454  VAL B CG2 
4650  N  N   . ASP B 455  ? 0.9330 1.1146 0.9903 0.0135  -0.0510 -0.1513 455  ASP B N   
4651  C  CA  . ASP B 455  ? 0.9270 1.1069 0.9760 0.0254  -0.0561 -0.1494 455  ASP B CA  
4652  C  C   . ASP B 455  ? 0.9869 1.1801 1.0361 0.0274  -0.0650 -0.1580 455  ASP B C   
4653  O  O   . ASP B 455  ? 0.9863 1.1898 1.0422 0.0191  -0.0671 -0.1655 455  ASP B O   
4654  C  CB  . ASP B 455  ? 0.8957 1.0525 0.9288 0.0297  -0.0528 -0.1432 455  ASP B CB  
4655  C  CG  . ASP B 455  ? 1.1393 1.2855 1.1713 0.0334  -0.0464 -0.1339 455  ASP B CG  
4656  O  OD1 . ASP B 455  ? 1.2568 1.4129 1.2999 0.0325  -0.0446 -0.1322 455  ASP B OD1 
4657  O  OD2 . ASP B 455  ? 1.2139 1.3421 1.2342 0.0370  -0.0430 -0.1284 455  ASP B OD2 
4658  N  N   . GLU B 456  ? 1.1318 1.3246 1.1734 0.0387  -0.0701 -0.1567 456  GLU B N   
4659  C  CA  . GLU B 456  ? 1.1494 1.3547 1.1900 0.0425  -0.0792 -0.1644 456  GLU B CA  
4660  C  C   . GLU B 456  ? 1.1459 1.3446 1.1790 0.0368  -0.0810 -0.1700 456  GLU B C   
4661  O  O   . GLU B 456  ? 1.2026 1.4160 1.2415 0.0328  -0.0868 -0.1789 456  GLU B O   
4662  C  CB  . GLU B 456  ? 1.1501 1.3514 1.1806 0.0563  -0.0833 -0.1609 456  GLU B CB  
4663  C  CG  . GLU B 456  ? 1.2268 1.4399 1.2656 0.0629  -0.0843 -0.1581 456  GLU B CG  
4664  C  CD  . GLU B 456  ? 1.2638 1.4634 1.3009 0.0650  -0.0767 -0.1484 456  GLU B CD  
4665  O  OE1 . GLU B 456  ? 1.3803 1.5610 1.4082 0.0631  -0.0713 -0.1435 456  GLU B OE1 
4666  O  OE2 . GLU B 456  ? 1.2832 1.4913 1.3281 0.0686  -0.0762 -0.1458 456  GLU B OE2 
4667  N  N   . THR B 457  ? 0.9287 1.1055 0.9489 0.0363  -0.0761 -0.1652 457  THR B N   
4668  C  CA  . THR B 457  ? 1.0110 1.1793 1.0224 0.0313  -0.0776 -0.1701 457  THR B CA  
4669  C  C   . THR B 457  ? 0.9997 1.1744 1.0213 0.0175  -0.0751 -0.1759 457  THR B C   
4670  O  O   . THR B 457  ? 1.0513 1.2307 1.0722 0.0123  -0.0795 -0.1839 457  THR B O   
4671  C  CB  . THR B 457  ? 1.0131 1.1560 1.0083 0.0344  -0.0721 -0.1630 457  THR B CB  
4672  O  OG1 . THR B 457  ? 1.0732 1.2068 1.0599 0.0287  -0.0727 -0.1678 457  THR B OG1 
4673  C  CG2 . THR B 457  ? 1.0059 1.1391 1.0047 0.0308  -0.0629 -0.1550 457  THR B CG2 
4674  N  N   . SER B 458  ? 1.2941 1.4691 1.3251 0.0112  -0.0681 -0.1720 458  SER B N   
4675  C  CA  . SER B 458  ? 1.2761 1.4555 1.3160 -0.0021 -0.0648 -0.1768 458  SER B CA  
4676  C  C   . SER B 458  ? 1.2565 1.4611 1.3112 -0.0064 -0.0707 -0.1859 458  SER B C   
4677  O  O   . SER B 458  ? 1.2569 1.4665 1.3165 -0.0168 -0.0710 -0.1930 458  SER B O   
4678  C  CB  . SER B 458  ? 1.1837 1.3565 1.2290 -0.0067 -0.0557 -0.1698 458  SER B CB  
4679  O  OG  . SER B 458  ? 1.1821 1.3330 1.2146 -0.0022 -0.0503 -0.1615 458  SER B OG  
4680  N  N   . ALA B 459  ? 0.7928 1.0135 0.8549 0.0013  -0.0754 -0.1860 459  ALA B N   
4681  C  CA  . ALA B 459  ? 0.6822 0.9283 0.7587 -0.0018 -0.0814 -0.1947 459  ALA B CA  
4682  C  C   . ALA B 459  ? 0.7451 0.9969 0.8170 -0.0017 -0.0896 -0.2036 459  ALA B C   
4683  O  O   . ALA B 459  ? 0.7834 1.0519 0.8664 -0.0096 -0.0930 -0.2124 459  ALA B O   
4684  C  CB  . ALA B 459  ? 0.6030 0.8635 0.6866 0.0079  -0.0846 -0.1923 459  ALA B CB  
4685  N  N   . ARG B 460  ? 1.0684 1.3065 1.1241 0.0070  -0.0929 -0.2016 460  ARG B N   
4686  C  CA  . ARG B 460  ? 1.1064 1.3476 1.1554 0.0082  -0.1009 -0.2095 460  ARG B CA  
4687  C  C   . ARG B 460  ? 1.1426 1.3662 1.1815 0.0000  -0.0978 -0.2113 460  ARG B C   
4688  O  O   . ARG B 460  ? 1.0892 1.3095 1.1183 0.0021  -0.1037 -0.2165 460  ARG B O   
4689  C  CB  . ARG B 460  ? 1.1159 1.3526 1.1521 0.0231  -0.1067 -0.2067 460  ARG B CB  
4690  C  CG  . ARG B 460  ? 1.1432 1.3906 1.1858 0.0325  -0.1078 -0.2022 460  ARG B CG  
4691  C  CD  . ARG B 460  ? 1.2189 1.4692 1.2519 0.0463  -0.1160 -0.2031 460  ARG B CD  
4692  N  NE  . ARG B 460  ? 1.3328 1.5981 1.3678 0.0453  -0.1251 -0.2138 460  ARG B NE  
4693  C  CZ  . ARG B 460  ? 1.4891 1.7635 1.5194 0.0562  -0.1339 -0.2172 460  ARG B CZ  
4694  N  NH1 . ARG B 460  ? 1.4452 1.7146 1.4681 0.0690  -0.1344 -0.2106 460  ARG B NH1 
4695  N  NH2 . ARG B 460  ? 1.6614 1.9502 1.6943 0.0544  -0.1422 -0.2275 460  ARG B NH2 
4696  N  N   . ALA B 461  ? 0.9428 1.1545 0.9832 -0.0089 -0.0888 -0.2072 461  ALA B N   
4697  C  CA  . ALA B 461  ? 0.8528 1.0461 0.8833 -0.0168 -0.0848 -0.2081 461  ALA B CA  
4698  C  C   . ALA B 461  ? 0.8721 1.0718 0.9150 -0.0316 -0.0804 -0.2128 461  ALA B C   
4699  O  O   . ALA B 461  ? 0.9503 1.1648 1.0084 -0.0355 -0.0781 -0.2128 461  ALA B O   
4700  C  CB  . ALA B 461  ? 0.9270 1.0952 0.9444 -0.0127 -0.0770 -0.1975 461  ALA B CB  
4701  N  N   . THR B 462  ? 1.0558 1.2434 1.0914 -0.0399 -0.0788 -0.2168 462  THR B N   
4702  C  CA  . THR B 462  ? 1.0968 1.2848 1.1409 -0.0543 -0.0730 -0.2201 462  THR B CA  
4703  C  C   . THR B 462  ? 1.0621 1.2291 1.1003 -0.0565 -0.0623 -0.2106 462  THR B C   
4704  O  O   . THR B 462  ? 1.0714 1.2237 1.0987 -0.0473 -0.0598 -0.2022 462  THR B O   
4705  C  CB  . THR B 462  ? 1.0985 1.2829 1.1375 -0.0626 -0.0763 -0.2293 462  THR B CB  
4706  O  OG1 . THR B 462  ? 1.1699 1.3288 1.1895 -0.0593 -0.0739 -0.2253 462  THR B OG1 
4707  C  CG2 . THR B 462  ? 1.0419 1.2463 1.0852 -0.0590 -0.0876 -0.2386 462  THR B CG2 
4708  N  N   . TRP B 463  ? 1.1348 1.3016 1.1809 -0.0687 -0.0559 -0.2121 463  TRP B N   
4709  C  CA  . TRP B 463  ? 1.1899 1.3358 1.2296 -0.0730 -0.0457 -0.2047 463  TRP B CA  
4710  C  C   . TRP B 463  ? 1.2178 1.3544 1.2525 -0.0623 -0.0419 -0.1936 463  TRP B C   
4711  O  O   . TRP B 463  ? 1.2551 1.3709 1.2753 -0.0575 -0.0386 -0.1875 463  TRP B O   
4712  C  CB  . TRP B 463  ? 1.1822 1.3066 1.2064 -0.0773 -0.0438 -0.2064 463  TRP B CB  
4713  C  CG  . TRP B 463  ? 1.2500 1.3787 1.2790 -0.0908 -0.0442 -0.2161 463  TRP B CG  
4714  C  CD1 . TRP B 463  ? 1.2940 1.4223 1.3172 -0.0937 -0.0503 -0.2246 463  TRP B CD1 
4715  C  CD2 . TRP B 463  ? 1.3093 1.4423 1.3495 -0.1035 -0.0379 -0.2183 463  TRP B CD2 
4716  N  NE1 . TRP B 463  ? 1.5058 1.6385 1.5365 -0.1078 -0.0483 -0.2322 463  TRP B NE1 
4717  C  CE2 . TRP B 463  ? 1.4546 1.5899 1.4957 -0.1141 -0.0405 -0.2284 463  TRP B CE2 
4718  C  CE3 . TRP B 463  ? 1.2970 1.4318 1.3461 -0.1069 -0.0303 -0.2128 463  TRP B CE3 
4719  C  CZ2 . TRP B 463  ? 1.4588 1.5981 1.5097 -0.1282 -0.0353 -0.2330 463  TRP B CZ2 
4720  C  CZ3 . TRP B 463  ? 1.3559 1.4943 1.4141 -0.1204 -0.0252 -0.2172 463  TRP B CZ3 
4721  C  CH2 . TRP B 463  ? 1.3913 1.5318 1.4504 -0.1311 -0.0275 -0.2271 463  TRP B CH2 
4722  N  N   . HIS B 464  ? 1.0677 1.2204 1.1148 -0.0586 -0.0424 -0.1912 464  HIS B N   
4723  C  CA  . HIS B 464  ? 0.9492 1.0940 0.9933 -0.0499 -0.0384 -0.1809 464  HIS B CA  
4724  C  C   . HIS B 464  ? 0.8914 1.0229 0.9351 -0.0564 -0.0284 -0.1752 464  HIS B C   
4725  O  O   . HIS B 464  ? 0.9029 1.0421 0.9571 -0.0661 -0.0249 -0.1782 464  HIS B O   
4726  C  CB  . HIS B 464  ? 0.8844 1.0498 0.9411 -0.0437 -0.0421 -0.1803 464  HIS B CB  
4727  C  CG  . HIS B 464  ? 0.8596 1.0183 0.9155 -0.0368 -0.0371 -0.1703 464  HIS B CG  
4728  N  ND1 . HIS B 464  ? 0.8841 1.0255 0.9268 -0.0280 -0.0356 -0.1630 464  HIS B ND1 
4729  C  CD2 . HIS B 464  ? 0.8515 1.0185 0.9183 -0.0375 -0.0333 -0.1666 464  HIS B CD2 
4730  C  CE1 . HIS B 464  ? 0.8196 0.9593 0.8656 -0.0239 -0.0313 -0.1555 464  HIS B CE1 
4731  N  NE2 . HIS B 464  ? 0.7697 0.9244 0.8298 -0.0293 -0.0299 -0.1575 464  HIS B NE2 
4732  N  N   . ILE B 465  ? 0.6420 0.7535 0.6736 -0.0510 -0.0237 -0.1671 465  ILE B N   
4733  C  CA  . ILE B 465  ? 0.6202 0.7167 0.6491 -0.0555 -0.0144 -0.1610 465  ILE B CA  
4734  C  C   . ILE B 465  ? 0.6705 0.7670 0.7018 -0.0470 -0.0117 -0.1522 465  ILE B C   
4735  O  O   . ILE B 465  ? 0.6206 0.7117 0.6446 -0.0369 -0.0141 -0.1478 465  ILE B O   
4736  C  CB  . ILE B 465  ? 0.5928 0.6653 0.6053 -0.0565 -0.0107 -0.1590 465  ILE B CB  
4737  C  CG1 . ILE B 465  ? 0.7423 0.8148 0.7510 -0.0634 -0.0148 -0.1682 465  ILE B CG1 
4738  C  CG2 . ILE B 465  ? 0.5862 0.6444 0.5964 -0.0619 -0.0012 -0.1536 465  ILE B CG2 
4739  C  CD1 . ILE B 465  ? 0.8437 0.9252 0.8630 -0.0766 -0.0127 -0.1749 465  ILE B CD1 
4740  N  N   . PRO B 466  ? 0.8097 0.9120 0.8509 -0.0508 -0.0069 -0.1496 466  PRO B N   
4741  C  CA  . PRO B 466  ? 0.6858 0.7867 0.7287 -0.0431 -0.0041 -0.1412 466  PRO B CA  
4742  C  C   . PRO B 466  ? 0.7180 0.7963 0.7475 -0.0394 0.0014  -0.1336 466  PRO B C   
4743  O  O   . PRO B 466  ? 0.6825 0.7464 0.7052 -0.0455 0.0066  -0.1333 466  PRO B O   
4744  C  CB  . PRO B 466  ? 0.6863 0.7969 0.7415 -0.0500 0.0004  -0.1412 466  PRO B CB  
4745  C  CG  . PRO B 466  ? 0.7314 0.8394 0.7870 -0.0620 0.0030  -0.1472 466  PRO B CG  
4746  C  CD  . PRO B 466  ? 0.7995 0.9110 0.8513 -0.0622 -0.0040 -0.1545 466  PRO B CD  
4747  N  N   . GLN B 467  ? 0.9267 1.0018 0.9526 -0.0291 0.0003  -0.1275 467  GLN B N   
4748  C  CA  . GLN B 467  ? 0.9377 0.9932 0.9520 -0.0243 0.0051  -0.1201 467  GLN B CA  
4749  C  C   . GLN B 467  ? 0.9575 1.0115 0.9768 -0.0229 0.0107  -0.1131 467  GLN B C   
4750  O  O   . GLN B 467  ? 0.9367 1.0044 0.9662 -0.0203 0.0090  -0.1122 467  GLN B O   
4751  C  CB  . GLN B 467  ? 0.9631 1.0145 0.9694 -0.0140 0.0009  -0.1176 467  GLN B CB  
4752  C  CG  . GLN B 467  ? 0.9718 1.0020 0.9643 -0.0103 0.0054  -0.1119 467  GLN B CG  
4753  C  CD  . GLN B 467  ? 0.9824 1.0086 0.9675 0.0002  0.0022  -0.1086 467  GLN B CD  
4754  O  OE1 . GLN B 467  ? 0.9453 0.9839 0.9359 0.0056  -0.0028 -0.1092 467  GLN B OE1 
4755  N  NE2 . GLN B 467  ? 0.9864 0.9950 0.9587 0.0033  0.0052  -0.1050 467  GLN B NE2 
4756  N  N   . ALA B 468  ? 1.0432 1.0802 1.0547 -0.0243 0.0173  -0.1083 468  ALA B N   
4757  C  CA  . ALA B 468  ? 0.8838 0.9178 0.8986 -0.0228 0.0227  -0.1017 468  ALA B CA  
4758  C  C   . ALA B 468  ? 0.8029 0.8358 0.8164 -0.0124 0.0215  -0.0954 468  ALA B C   
4759  O  O   . ALA B 468  ? 0.7472 0.7714 0.7517 -0.0066 0.0200  -0.0937 468  ALA B O   
4760  C  CB  . ALA B 468  ? 0.8857 0.9015 0.8917 -0.0270 0.0299  -0.0987 468  ALA B CB  
4761  N  N   . HIS B 469  ? 0.9533 0.9950 0.9758 -0.0101 0.0223  -0.0921 469  HIS B N   
4762  C  CA  . HIS B 469  ? 0.9103 0.9514 0.9327 -0.0009 0.0216  -0.0863 469  HIS B CA  
4763  C  C   . HIS B 469  ? 0.9549 0.9781 0.9677 0.0022  0.0269  -0.0799 469  HIS B C   
4764  O  O   . HIS B 469  ? 0.9905 1.0040 0.9995 -0.0027 0.0320  -0.0788 469  HIS B O   
4765  C  CB  . HIS B 469  ? 0.8747 0.9282 0.9085 0.0000  0.0217  -0.0845 469  HIS B CB  
4766  C  CG  . HIS B 469  ? 0.9442 1.0009 0.9797 0.0090  0.0193  -0.0802 469  HIS B CG  
4767  N  ND1 . HIS B 469  ? 0.9013 0.9494 0.9345 0.0136  0.0230  -0.0734 469  HIS B ND1 
4768  C  CD2 . HIS B 469  ? 0.9906 1.0578 1.0295 0.0142  0.0136  -0.0820 469  HIS B CD2 
4769  C  CE1 . HIS B 469  ? 0.9461 0.9991 0.9816 0.0208  0.0199  -0.0712 469  HIS B CE1 
4770  N  NE2 . HIS B 469  ? 0.9523 1.0164 0.9908 0.0215  0.0143  -0.0762 469  HIS B NE2 
4771  N  N   . PRO B 470  ? 0.8302 0.8488 0.8387 0.0104  0.0259  -0.0755 470  PRO B N   
4772  C  CA  . PRO B 470  ? 0.7959 0.7989 0.7964 0.0138  0.0310  -0.0693 470  PRO B CA  
4773  C  C   . PRO B 470  ? 0.7601 0.7614 0.7651 0.0125  0.0361  -0.0649 470  PRO B C   
4774  O  O   . PRO B 470  ? 0.7260 0.7143 0.7243 0.0136  0.0409  -0.0607 470  PRO B O   
4775  C  CB  . PRO B 470  ? 0.7084 0.7111 0.7069 0.0227  0.0285  -0.0659 470  PRO B CB  
4776  C  CG  . PRO B 470  ? 0.8590 0.8711 0.8583 0.0234  0.0221  -0.0714 470  PRO B CG  
4777  C  CD  . PRO B 470  ? 0.8500 0.8758 0.8590 0.0168  0.0201  -0.0766 470  PRO B CD  
4778  N  N   . LEU B 471  ? 1.0311 1.0450 1.0466 0.0107  0.0352  -0.0656 471  LEU B N   
4779  C  CA  . LEU B 471  ? 1.0560 1.0689 1.0755 0.0095  0.0397  -0.0618 471  LEU B CA  
4780  C  C   . LEU B 471  ? 1.2173 1.2277 1.2365 0.0011  0.0433  -0.0645 471  LEU B C   
4781  O  O   . LEU B 471  ? 1.1916 1.2009 1.2135 -0.0003 0.0472  -0.0618 471  LEU B O   
4782  C  CB  . LEU B 471  ? 0.9794 1.0064 1.0098 0.0123  0.0371  -0.0610 471  LEU B CB  
4783  C  CG  . LEU B 471  ? 1.0195 1.0464 1.0504 0.0207  0.0356  -0.0564 471  LEU B CG  
4784  C  CD1 . LEU B 471  ? 0.9750 1.0159 1.0163 0.0228  0.0327  -0.0565 471  LEU B CD1 
4785  C  CD2 . LEU B 471  ? 1.1123 1.1270 1.1384 0.0236  0.0405  -0.0503 471  LEU B CD2 
4786  N  N   . GLU B 472  ? 0.8775 0.8865 0.8932 -0.0045 0.0422  -0.0700 472  GLU B N   
4787  C  CA  . GLU B 472  ? 0.7966 0.8023 0.8115 -0.0131 0.0459  -0.0729 472  GLU B CA  
4788  C  C   . GLU B 472  ? 0.8168 0.8092 0.8208 -0.0169 0.0474  -0.0755 472  GLU B C   
4789  O  O   . GLU B 472  ? 0.8072 0.7990 0.8110 -0.0250 0.0488  -0.0801 472  GLU B O   
4790  C  CB  . GLU B 472  ? 0.8358 0.8582 0.8615 -0.0188 0.0430  -0.0787 472  GLU B CB  
4791  C  CG  . GLU B 472  ? 0.7651 0.7965 0.7924 -0.0191 0.0366  -0.0847 472  GLU B CG  
4792  C  CD  . GLU B 472  ? 0.7911 0.8419 0.8308 -0.0220 0.0328  -0.0895 472  GLU B CD  
4793  O  OE1 . GLU B 472  ? 0.8866 0.9457 0.9340 -0.0194 0.0332  -0.0868 472  GLU B OE1 
4794  O  OE2 . GLU B 472  ? 0.7180 0.7761 0.7599 -0.0268 0.0295  -0.0961 472  GLU B OE2 
4795  N  N   . SER B 473  ? 0.9012 0.8823 0.8959 -0.0113 0.0473  -0.0726 473  SER B N   
4796  C  CA  . SER B 473  ? 0.9551 0.9238 0.9387 -0.0139 0.0479  -0.0754 473  SER B CA  
4797  C  C   . SER B 473  ? 0.9406 0.8924 0.9133 -0.0084 0.0521  -0.0695 473  SER B C   
4798  O  O   . SER B 473  ? 0.8348 0.7867 0.8089 -0.0013 0.0526  -0.0640 473  SER B O   
4799  C  CB  . SER B 473  ? 1.0766 1.0523 1.0599 -0.0124 0.0414  -0.0803 473  SER B CB  
4800  O  OG  . SER B 473  ? 1.0276 1.0033 1.0091 -0.0033 0.0389  -0.0765 473  SER B OG  
4801  N  N   . TRP B 474  ? 0.8933 0.8306 0.8552 -0.0119 0.0551  -0.0710 474  TRP B N   
4802  C  CA  . TRP B 474  ? 0.8388 0.7595 0.7892 -0.0067 0.0587  -0.0662 474  TRP B CA  
4803  C  C   . TRP B 474  ? 0.8485 0.7670 0.7927 -0.0019 0.0547  -0.0676 474  TRP B C   
4804  O  O   . TRP B 474  ? 0.8997 0.8241 0.8444 -0.0051 0.0501  -0.0736 474  TRP B O   
4805  C  CB  . TRP B 474  ? 0.8126 0.7174 0.7530 -0.0124 0.0642  -0.0671 474  TRP B CB  
4806  C  CG  . TRP B 474  ? 0.7748 0.6757 0.7168 -0.0142 0.0698  -0.0632 474  TRP B CG  
4807  C  CD1 . TRP B 474  ? 0.7650 0.6684 0.7109 -0.0221 0.0721  -0.0659 474  TRP B CD1 
4808  C  CD2 . TRP B 474  ? 0.8175 0.7111 0.7569 -0.0077 0.0739  -0.0561 474  TRP B CD2 
4809  N  NE1 . TRP B 474  ? 0.8309 0.7283 0.7759 -0.0206 0.0774  -0.0608 474  TRP B NE1 
4810  C  CE2 . TRP B 474  ? 0.8007 0.6925 0.7420 -0.0118 0.0783  -0.0548 474  TRP B CE2 
4811  C  CE3 . TRP B 474  ? 0.8365 0.7254 0.7724 0.0011  0.0744  -0.0508 474  TRP B CE3 
4812  C  CZ2 . TRP B 474  ? 0.8094 0.6950 0.7488 -0.0069 0.0827  -0.0486 474  TRP B CZ2 
4813  C  CZ3 . TRP B 474  ? 0.8058 0.6893 0.7409 0.0055  0.0788  -0.0448 474  TRP B CZ3 
4814  C  CH2 . TRP B 474  ? 0.7979 0.6799 0.7345 0.0017  0.0826  -0.0438 474  TRP B CH2 
4815  N  N   . GLY B 475  ? 0.7695 0.6800 0.7081 0.0058  0.0565  -0.0621 475  GLY B N   
4816  C  CA  . GLY B 475  ? 0.7078 0.6146 0.6393 0.0109  0.0535  -0.0627 475  GLY B CA  
4817  C  C   . GLY B 475  ? 0.7305 0.6304 0.6584 0.0196  0.0563  -0.0557 475  GLY B C   
4818  O  O   . GLY B 475  ? 0.7227 0.6190 0.6522 0.0214  0.0608  -0.0507 475  GLY B O   
4819  N  N   . ASP B 476  ? 0.8440 0.7423 0.7668 0.0250  0.0536  -0.0557 476  ASP B N   
4820  C  CA  . ASP B 476  ? 0.8514 0.7437 0.7707 0.0333  0.0561  -0.0495 476  ASP B CA  
4821  C  C   . ASP B 476  ? 0.7902 0.6884 0.7094 0.0384  0.0513  -0.0503 476  ASP B C   
4822  O  O   . ASP B 476  ? 0.7132 0.6180 0.6329 0.0360  0.0461  -0.0558 476  ASP B O   
4823  C  CB  . ASP B 476  ? 0.8210 0.6953 0.7270 0.0348  0.0611  -0.0474 476  ASP B CB  
4824  C  CG  . ASP B 476  ? 0.9187 0.7850 0.8140 0.0314  0.0591  -0.0530 476  ASP B CG  
4825  O  OD1 . ASP B 476  ? 0.8653 0.7409 0.7641 0.0275  0.0538  -0.0588 476  ASP B OD1 
4826  O  OD2 . ASP B 476  ? 1.0967 0.9478 0.9800 0.0328  0.0628  -0.0519 476  ASP B OD2 
4827  N  N   . ALA B 477  ? 0.6922 0.5878 0.6107 0.0457  0.0532  -0.0448 477  ALA B N   
4828  C  CA  . ALA B 477  ? 0.6615 0.5610 0.5790 0.0514  0.0497  -0.0445 477  ALA B CA  
4829  C  C   . ALA B 477  ? 0.7112 0.6022 0.6244 0.0586  0.0541  -0.0381 477  ALA B C   
4830  O  O   . ALA B 477  ? 0.7606 0.6463 0.6745 0.0593  0.0592  -0.0338 477  ALA B O   
4831  C  CB  . ALA B 477  ? 0.7461 0.6619 0.6760 0.0515  0.0452  -0.0455 477  ALA B CB  
4832  N  N   . ARG B 478  ? 0.8328 0.7228 0.7413 0.0642  0.0521  -0.0375 478  ARG B N   
4833  C  CA  . ARG B 478  ? 0.8637 0.7461 0.7679 0.0711  0.0562  -0.0317 478  ARG B CA  
4834  C  C   . ARG B 478  ? 0.9586 0.8503 0.8700 0.0755  0.0540  -0.0295 478  ARG B C   
4835  O  O   . ARG B 478  ? 0.9413 0.8393 0.8528 0.0759  0.0486  -0.0331 478  ARG B O   
4836  C  CB  . ARG B 478  ? 0.9121 0.7813 0.8013 0.0741  0.0572  -0.0325 478  ARG B CB  
4837  C  CG  . ARG B 478  ? 1.0850 0.9424 0.9657 0.0708  0.0607  -0.0336 478  ARG B CG  
4838  C  CD  . ARG B 478  ? 1.1336 0.9766 0.9994 0.0755  0.0631  -0.0327 478  ARG B CD  
4839  N  NE  . ARG B 478  ? 1.2742 1.1122 1.1393 0.0821  0.0684  -0.0260 478  ARG B NE  
4840  C  CZ  . ARG B 478  ? 1.3188 1.1450 1.1721 0.0873  0.0715  -0.0239 478  ARG B CZ  
4841  N  NH1 . ARG B 478  ? 1.2031 1.0205 1.0436 0.0871  0.0697  -0.0279 478  ARG B NH1 
4842  N  NH2 . ARG B 478  ? 1.3160 1.1394 1.1706 0.0928  0.0767  -0.0177 478  ARG B NH2 
4843  N  N   . ALA B 479  ? 1.0445 0.9367 0.9615 0.0790  0.0579  -0.0238 479  ALA B N   
4844  C  CA  . ALA B 479  ? 0.9832 0.8822 0.9062 0.0833  0.0566  -0.0212 479  ALA B CA  
4845  C  C   . ALA B 479  ? 1.0307 0.9202 0.9437 0.0896  0.0587  -0.0186 479  ALA B C   
4846  O  O   . ALA B 479  ? 1.1680 1.0463 1.0697 0.0908  0.0610  -0.0188 479  ALA B O   
4847  C  CB  . ALA B 479  ? 1.0302 0.9348 0.9647 0.0834  0.0597  -0.0168 479  ALA B CB  
4848  N  N   . PHE B 480  ? 1.1603 1.0539 1.0769 0.0939  0.0582  -0.0160 480  PHE B N   
4849  C  CA  . PHE B 480  ? 1.1064 0.9908 1.0143 0.1001  0.0613  -0.0126 480  PHE B CA  
4850  C  C   . PHE B 480  ? 1.2086 1.0854 1.1158 0.1017  0.0683  -0.0076 480  PHE B C   
4851  O  O   . PHE B 480  ? 1.2996 1.1809 1.2163 0.0993  0.0706  -0.0056 480  PHE B O   
4852  C  CB  . PHE B 480  ? 1.0734 0.9634 0.9860 0.1039  0.0599  -0.0106 480  PHE B CB  
4853  C  CG  . PHE B 480  ? 1.1297 1.0215 1.0513 0.1055  0.0647  -0.0050 480  PHE B CG  
4854  C  CD1 . PHE B 480  ? 1.1769 1.0779 1.1113 0.1018  0.0645  -0.0045 480  PHE B CD1 
4855  C  CD2 . PHE B 480  ? 1.1054 0.9898 1.0225 0.1106  0.0694  -0.0005 480  PHE B CD2 
4856  C  CE1 . PHE B 480  ? 1.0536 0.9569 0.9966 0.1032  0.0686  0.0002  480  PHE B CE1 
4857  C  CE2 . PHE B 480  ? 1.1067 0.9934 1.0327 0.1117  0.0738  0.0043  480  PHE B CE2 
4858  C  CZ  . PHE B 480  ? 1.0372 0.9336 0.9764 0.1079  0.0731  0.0045  480  PHE B CZ  
4859  N  N   . ASP B 481  ? 1.6188 1.4839 1.5144 0.1060  0.0718  -0.0057 481  ASP B N   
4860  C  CA  . ASP B 481  ? 1.7894 1.6456 1.6814 0.1081  0.0785  -0.0016 481  ASP B CA  
4861  C  C   . ASP B 481  ? 1.7786 1.6304 1.6671 0.1040  0.0792  -0.0039 481  ASP B C   
4862  O  O   . ASP B 481  ? 1.8365 1.6803 1.7209 0.1058  0.0845  -0.0010 481  ASP B O   
4863  C  CB  . ASP B 481  ? 1.8325 1.6940 1.7363 0.1094  0.0828  0.0036  481  ASP B CB  
4864  C  CG  . ASP B 481  ? 2.0397 1.8922 1.9390 0.1134  0.0900  0.0083  481  ASP B CG  
4865  O  OD1 . ASP B 481  ? 2.1027 1.9440 1.9890 0.1157  0.0919  0.0079  481  ASP B OD1 
4866  O  OD2 . ASP B 481  ? 2.0643 1.9212 1.9734 0.1143  0.0937  0.0123  481  ASP B OD2 
4867  N  N   . GLY B 482  ? 1.7374 1.5941 1.6274 0.0987  0.0742  -0.0091 482  GLY B N   
4868  C  CA  . GLY B 482  ? 1.7658 1.6172 1.6516 0.0944  0.0748  -0.0116 482  GLY B CA  
4869  C  C   . GLY B 482  ? 1.9007 1.7550 1.7953 0.0922  0.0783  -0.0089 482  GLY B C   
4870  O  O   . GLY B 482  ? 2.0225 1.8733 1.9182 0.0959  0.0836  -0.0040 482  GLY B O   
4871  N  N   . THR B 483  ? 1.2518 1.1126 1.1525 0.0863  0.0755  -0.0121 483  THR B N   
4872  C  CA  . THR B 483  ? 1.1330 0.9960 1.0409 0.0842  0.0785  -0.0099 483  THR B CA  
4873  C  C   . THR B 483  ? 1.2856 1.1460 1.1908 0.0780  0.0777  -0.0138 483  THR B C   
4874  O  O   . THR B 483  ? 1.3481 1.2039 1.2530 0.0773  0.0816  -0.0117 483  THR B O   
4875  C  CB  . THR B 483  ? 1.2372 1.1138 1.1598 0.0838  0.0769  -0.0081 483  THR B CB  
4876  O  OG1 . THR B 483  ? 1.1524 1.0315 1.0771 0.0887  0.0769  -0.0054 483  THR B OG1 
4877  C  CG2 . THR B 483  ? 1.2895 1.1671 1.2185 0.0840  0.0809  -0.0044 483  THR B CG2 
4878  N  N   . ALA B 484  ? 1.6470 1.5101 1.5501 0.0736  0.0728  -0.0194 484  ALA B N   
4879  C  CA  . ALA B 484  ? 1.6270 1.4871 1.5270 0.0670  0.0721  -0.0237 484  ALA B CA  
4880  C  C   . ALA B 484  ? 1.6535 1.5203 1.5635 0.0634  0.0733  -0.0226 484  ALA B C   
4881  O  O   . ALA B 484  ? 1.7840 1.6435 1.6912 0.0626  0.0776  -0.0207 484  ALA B O   
4882  C  CB  . ALA B 484  ? 1.7198 1.5637 1.6058 0.0676  0.0760  -0.0237 484  ALA B CB  
4883  N  N   . SER B 485  ? 0.9068 0.7874 0.8280 0.0614  0.0693  -0.0240 485  SER B N   
4884  C  CA  . SER B 485  ? 0.8031 0.6913 0.7340 0.0577  0.0697  -0.0236 485  SER B CA  
4885  C  C   . SER B 485  ? 0.7177 0.6079 0.6483 0.0501  0.0673  -0.0293 485  SER B C   
4886  O  O   . SER B 485  ? 0.7715 0.6614 0.6974 0.0477  0.0639  -0.0341 485  SER B O   
4887  C  CB  . SER B 485  ? 0.8981 0.7999 0.8414 0.0598  0.0670  -0.0220 485  SER B CB  
4888  O  OG  . SER B 485  ? 0.7813 0.6910 0.7267 0.0590  0.0616  -0.0258 485  SER B OG  
4889  N  N   . ILE B 486  ? 0.7518 0.6440 0.6872 0.0463  0.0692  -0.0290 486  ILE B N   
4890  C  CA  . ILE B 486  ? 0.6868 0.5797 0.6218 0.0386  0.0683  -0.0339 486  ILE B CA  
4891  C  C   . ILE B 486  ? 0.6419 0.5509 0.5893 0.0355  0.0641  -0.0364 486  ILE B C   
4892  O  O   . ILE B 486  ? 0.6887 0.6056 0.6449 0.0380  0.0642  -0.0331 486  ILE B O   
4893  C  CB  . ILE B 486  ? 0.6327 0.5161 0.5638 0.0363  0.0736  -0.0319 486  ILE B CB  
4894  C  CG1 . ILE B 486  ? 0.7776 0.6448 0.6961 0.0401  0.0780  -0.0292 486  ILE B CG1 
4895  C  CG2 . ILE B 486  ? 0.6230 0.5065 0.5535 0.0279  0.0732  -0.0369 486  ILE B CG2 
4896  C  CD1 . ILE B 486  ? 0.7803 0.6387 0.6879 0.0377  0.0767  -0.0337 486  ILE B CD1 
4897  N  N   . VAL B 487  ? 0.8898 0.8039 0.8377 0.0302  0.0603  -0.0423 487  VAL B N   
4898  C  CA  . VAL B 487  ? 0.9313 0.8608 0.8906 0.0267  0.0564  -0.0454 487  VAL B CA  
4899  C  C   . VAL B 487  ? 0.9616 0.8903 0.9230 0.0201  0.0595  -0.0465 487  VAL B C   
4900  O  O   . VAL B 487  ? 1.0029 0.9272 0.9598 0.0138  0.0600  -0.0508 487  VAL B O   
4901  C  CB  . VAL B 487  ? 0.8290 0.7656 0.7885 0.0245  0.0507  -0.0514 487  VAL B CB  
4902  C  CG1 . VAL B 487  ? 0.8205 0.7738 0.7923 0.0213  0.0469  -0.0545 487  VAL B CG1 
4903  C  CG2 . VAL B 487  ? 0.9158 0.8511 0.8713 0.0316  0.0482  -0.0499 487  VAL B CG2 
4904  N  N   . GLN B 488  ? 0.8422 0.7748 0.8102 0.0215  0.0617  -0.0426 488  GLN B N   
4905  C  CA  . GLN B 488  ? 0.8636 0.7945 0.8330 0.0163  0.0653  -0.0427 488  GLN B CA  
4906  C  C   . GLN B 488  ? 0.8508 0.7965 0.8309 0.0115  0.0622  -0.0465 488  GLN B C   
4907  O  O   . GLN B 488  ? 0.7998 0.7575 0.7888 0.0148  0.0589  -0.0456 488  GLN B O   
4908  C  CB  . GLN B 488  ? 0.8583 0.7849 0.8282 0.0208  0.0693  -0.0366 488  GLN B CB  
4909  C  CG  . GLN B 488  ? 0.9288 0.8483 0.8956 0.0166  0.0742  -0.0359 488  GLN B CG  
4910  C  CD  . GLN B 488  ? 0.9336 0.8482 0.8997 0.0221  0.0779  -0.0298 488  GLN B CD  
4911  O  OE1 . GLN B 488  ? 0.9611 0.8646 0.9202 0.0211  0.0826  -0.0280 488  GLN B OE1 
4912  N  NE2 . GLN B 488  ? 0.9297 0.8523 0.9028 0.0280  0.0758  -0.0267 488  GLN B NE2 
4913  N  N   . PRO B 489  ? 0.8150 0.7604 0.7946 0.0038  0.0633  -0.0507 489  PRO B N   
4914  C  CA  . PRO B 489  ? 0.8014 0.7615 0.7916 -0.0009 0.0609  -0.0543 489  PRO B CA  
4915  C  C   . PRO B 489  ? 0.7986 0.7624 0.7948 -0.0001 0.0637  -0.0505 489  PRO B C   
4916  O  O   . PRO B 489  ? 0.8280 0.7816 0.8191 0.0022  0.0682  -0.0460 489  PRO B O   
4917  C  CB  . PRO B 489  ? 0.8615 0.8177 0.8480 -0.0098 0.0622  -0.0597 489  PRO B CB  
4918  C  CG  . PRO B 489  ? 0.8229 0.7603 0.7970 -0.0098 0.0676  -0.0570 489  PRO B CG  
4919  C  CD  . PRO B 489  ? 0.7827 0.7139 0.7517 -0.0012 0.0671  -0.0525 489  PRO B CD  
4920  N  N   . LEU B 490  ? 0.9049 0.8838 0.9118 -0.0017 0.0608  -0.0527 490  LEU B N   
4921  C  CA  . LEU B 490  ? 0.9956 0.9795 1.0087 -0.0013 0.0629  -0.0499 490  LEU B CA  
4922  C  C   . LEU B 490  ? 1.0177 1.0083 1.0357 -0.0091 0.0641  -0.0539 490  LEU B C   
4923  O  O   . LEU B 490  ? 1.0353 1.0283 1.0570 -0.0094 0.0667  -0.0517 490  LEU B O   
4924  C  CB  . LEU B 490  ? 0.9594 0.9554 0.9814 0.0048  0.0588  -0.0479 490  LEU B CB  
4925  C  CG  . LEU B 490  ? 0.9088 0.8987 0.9279 0.0127  0.0593  -0.0423 490  LEU B CG  
4926  C  CD1 . LEU B 490  ? 0.8543 0.8395 0.8679 0.0158  0.0570  -0.0428 490  LEU B CD1 
4927  C  CD2 . LEU B 490  ? 0.8880 0.8891 0.9165 0.0172  0.0569  -0.0401 490  LEU B CD2 
4928  N  N   . ILE B 491  ? 0.7079 0.7016 0.7262 -0.0152 0.0624  -0.0597 491  ILE B N   
4929  C  CA  . ILE B 491  ? 0.7553 0.7566 0.7793 -0.0232 0.0636  -0.0641 491  ILE B CA  
4930  C  C   . ILE B 491  ? 0.8785 0.8767 0.8984 -0.0299 0.0629  -0.0699 491  ILE B C   
4931  O  O   . ILE B 491  ? 0.9056 0.9023 0.9220 -0.0275 0.0592  -0.0716 491  ILE B O   
4932  C  CB  . ILE B 491  ? 0.6142 0.6348 0.6509 -0.0220 0.0593  -0.0660 491  ILE B CB  
4933  C  CG1 . ILE B 491  ? 0.6871 0.7152 0.7302 -0.0297 0.0619  -0.0693 491  ILE B CG1 
4934  C  CG2 . ILE B 491  ? 0.5851 0.6155 0.6254 -0.0201 0.0526  -0.0700 491  ILE B CG2 
4935  C  CD1 . ILE B 491  ? 0.6778 0.7230 0.7326 -0.0276 0.0589  -0.0698 491  ILE B CD1 
4936  N  N   . GLU B 492  ? 1.1096 1.1062 1.1296 -0.0384 0.0667  -0.0730 492  GLU B N   
4937  C  CA  . GLU B 492  ? 1.0472 1.0439 1.0657 -0.0458 0.0655  -0.0796 492  GLU B CA  
4938  C  C   . GLU B 492  ? 1.1180 1.1337 1.1470 -0.0457 0.0584  -0.0848 492  GLU B C   
4939  O  O   . GLU B 492  ? 1.0748 1.1047 1.1138 -0.0432 0.0562  -0.0843 492  GLU B O   
4940  C  CB  . GLU B 492  ? 1.1649 1.1577 1.1831 -0.0555 0.0712  -0.0821 492  GLU B CB  
4941  C  CG  . GLU B 492  ? 1.3193 1.2918 1.3256 -0.0560 0.0784  -0.0774 492  GLU B CG  
4942  C  CD  . GLU B 492  ? 1.3643 1.3204 1.3581 -0.0574 0.0795  -0.0786 492  GLU B CD  
4943  O  OE1 . GLU B 492  ? 1.3444 1.3049 1.3388 -0.0587 0.0747  -0.0833 492  GLU B OE1 
4944  O  OE2 . GLU B 492  ? 1.3826 1.3211 1.3656 -0.0570 0.0852  -0.0747 492  GLU B OE2 
4945  N  N   . PRO B 493  ? 1.1509 1.1669 1.1772 -0.0477 0.0545  -0.0898 493  PRO B N   
4946  C  CA  . PRO B 493  ? 1.0452 1.0790 1.0805 -0.0467 0.0474  -0.0948 493  PRO B CA  
4947  C  C   . PRO B 493  ? 1.0242 1.0749 1.0722 -0.0523 0.0472  -0.0987 493  PRO B C   
4948  O  O   . PRO B 493  ? 1.1677 1.2174 1.2170 -0.0613 0.0510  -0.1020 493  PRO B O   
4949  C  CB  . PRO B 493  ? 1.0680 1.0967 1.0968 -0.0504 0.0448  -0.1002 493  PRO B CB  
4950  C  CG  . PRO B 493  ? 1.0382 1.0455 1.0531 -0.0485 0.0492  -0.0958 493  PRO B CG  
4951  C  CD  . PRO B 493  ? 1.1419 1.1414 1.1559 -0.0501 0.0563  -0.0909 493  PRO B CD  
4952  N  N   . LEU B 494  ? 0.8843 0.9503 0.9417 -0.0469 0.0429  -0.0982 494  LEU B N   
4953  C  CA  . LEU B 494  ? 0.9631 1.0457 1.0328 -0.0509 0.0429  -0.1010 494  LEU B CA  
4954  C  C   . LEU B 494  ? 0.9770 1.0699 1.0525 -0.0595 0.0409  -0.1094 494  LEU B C   
4955  O  O   . LEU B 494  ? 1.0207 1.1155 1.1000 -0.0680 0.0453  -0.1120 494  LEU B O   
4956  C  CB  . LEU B 494  ? 0.8760 0.9726 0.9536 -0.0426 0.0379  -0.0994 494  LEU B CB  
4957  C  CG  . LEU B 494  ? 0.7185 0.8074 0.7924 -0.0342 0.0394  -0.0916 494  LEU B CG  
4958  C  CD1 . LEU B 494  ? 0.7109 0.8136 0.7923 -0.0266 0.0339  -0.0910 494  LEU B CD1 
4959  C  CD2 . LEU B 494  ? 0.8205 0.9033 0.8942 -0.0369 0.0462  -0.0876 494  LEU B CD2 
4960  N  N   . TYR B 495  ? 0.8392 0.9389 0.9151 -0.0573 0.0342  -0.1138 495  TYR B N   
4961  C  CA  . TYR B 495  ? 0.8570 0.9680 0.9387 -0.0647 0.0310  -0.1223 495  TYR B CA  
4962  C  C   . TYR B 495  ? 0.9259 1.0230 0.9972 -0.0698 0.0317  -0.1253 495  TYR B C   
4963  O  O   . TYR B 495  ? 0.9802 1.0853 1.0541 -0.0736 0.0271  -0.1325 495  TYR B O   
4964  C  CB  . TYR B 495  ? 0.8314 0.9604 0.9205 -0.0589 0.0226  -0.1260 495  TYR B CB  
4965  C  CG  . TYR B 495  ? 0.7370 0.8752 0.8323 -0.0506 0.0211  -0.1215 495  TYR B CG  
4966  C  CD1 . TYR B 495  ? 0.6608 0.8112 0.7669 -0.0533 0.0234  -0.1217 495  TYR B CD1 
4967  C  CD2 . TYR B 495  ? 0.7670 0.9009 0.8570 -0.0403 0.0175  -0.1170 495  TYR B CD2 
4968  C  CE1 . TYR B 495  ? 0.6247 0.7828 0.7359 -0.0456 0.0220  -0.1177 495  TYR B CE1 
4969  C  CE2 . TYR B 495  ? 0.6986 0.8400 0.7938 -0.0330 0.0162  -0.1131 495  TYR B CE2 
4970  C  CZ  . TYR B 495  ? 0.6431 0.7965 0.7488 -0.0357 0.0183  -0.1135 495  TYR B CZ  
4971  O  OH  . TYR B 495  ? 0.7033 0.8636 0.8137 -0.0284 0.0169  -0.1098 495  TYR B OH  
4972  N  N   . GLY B 496  ? 1.0870 1.1634 1.1466 -0.0696 0.0373  -0.1202 496  GLY B N   
4973  C  CA  . GLY B 496  ? 1.1303 1.1917 1.1783 -0.0722 0.0375  -0.1222 496  GLY B CA  
4974  C  C   . GLY B 496  ? 1.1986 1.2574 1.2400 -0.0629 0.0316  -0.1210 496  GLY B C   
4975  O  O   . GLY B 496  ? 1.2737 1.3345 1.3157 -0.0538 0.0299  -0.1158 496  GLY B O   
4976  N  N   . GLY B 497  ? 1.0542 1.1085 1.0893 -0.0655 0.0285  -0.1261 497  GLY B N   
4977  C  CA  . GLY B 497  ? 1.0269 1.0782 1.0548 -0.0570 0.0230  -0.1254 497  GLY B CA  
4978  C  C   . GLY B 497  ? 1.0392 1.0679 1.0517 -0.0540 0.0267  -0.1207 497  GLY B C   
4979  O  O   . GLY B 497  ? 0.9246 0.9418 0.9331 -0.0520 0.0327  -0.1141 497  GLY B O   
4980  N  N   . LYS B 498  ? 0.8913 0.9136 0.8951 -0.0533 0.0232  -0.1243 498  LYS B N   
4981  C  CA  . LYS B 498  ? 0.9110 0.9117 0.8995 -0.0510 0.0266  -0.1209 498  LYS B CA  
4982  C  C   . LYS B 498  ? 0.8795 0.8764 0.8619 -0.0394 0.0237  -0.1159 498  LYS B C   
4983  O  O   . LYS B 498  ? 0.8013 0.8118 0.7901 -0.0336 0.0182  -0.1163 498  LYS B O   
4984  C  CB  . LYS B 498  ? 0.8282 0.8222 0.8095 -0.0580 0.0251  -0.1280 498  LYS B CB  
4985  C  CG  . LYS B 498  ? 0.8534 0.8581 0.8441 -0.0696 0.0252  -0.1354 498  LYS B CG  
4986  C  CD  . LYS B 498  ? 0.9050 0.9007 0.8961 -0.0764 0.0337  -0.1324 498  LYS B CD  
4987  C  CE  . LYS B 498  ? 0.9282 0.9000 0.9040 -0.0792 0.0391  -0.1310 498  LYS B CE  
4988  N  NZ  . LYS B 498  ? 0.6510 0.6135 0.6262 -0.0859 0.0475  -0.1284 498  LYS B NZ  
4989  N  N   . THR B 499  ? 1.2237 1.2016 1.1934 -0.0359 0.0278  -0.1111 499  THR B N   
4990  C  CA  . THR B 499  ? 1.2205 1.1922 1.1830 -0.0255 0.0262  -0.1062 499  THR B CA  
4991  C  C   . THR B 499  ? 1.2741 1.2390 1.2258 -0.0243 0.0222  -0.1106 499  THR B C   
4992  O  O   . THR B 499  ? 1.3811 1.3463 1.3312 -0.0316 0.0204  -0.1175 499  THR B O   
4993  C  CB  . THR B 499  ? 1.2386 1.1946 1.1942 -0.0216 0.0332  -0.0980 499  THR B CB  
4994  O  OG1 . THR B 499  ? 1.1977 1.1355 1.1405 -0.0249 0.0370  -0.0987 499  THR B OG1 
4995  C  CG2 . THR B 499  ? 1.2979 1.2585 1.2626 -0.0249 0.0377  -0.0949 499  THR B CG2 
4996  N  N   . ALA B 500  ? 1.2243 1.1826 1.1681 -0.0149 0.0210  -0.1064 500  ALA B N   
4997  C  CA  . ALA B 500  ? 1.2897 1.2413 1.2224 -0.0125 0.0170  -0.1101 500  ALA B CA  
4998  C  C   . ALA B 500  ? 1.3954 1.3278 1.3153 -0.0167 0.0215  -0.1109 500  ALA B C   
4999  O  O   . ALA B 500  ? 1.3848 1.3145 1.2988 -0.0210 0.0185  -0.1175 500  ALA B O   
5000  C  CB  . ALA B 500  ? 1.1764 1.1254 1.1038 -0.0012 0.0153  -0.1050 500  ALA B CB  
5001  N  N   . ASN B 501  ? 1.4603 1.3790 1.3753 -0.0155 0.0287  -0.1043 501  ASN B N   
5002  C  CA  . ASN B 501  ? 1.4274 1.3266 1.3293 -0.0187 0.0334  -0.1045 501  ASN B CA  
5003  C  C   . ASN B 501  ? 1.4283 1.3273 1.3326 -0.0304 0.0349  -0.1104 501  ASN B C   
5004  O  O   . ASN B 501  ? 1.5700 1.4552 1.4635 -0.0347 0.0366  -0.1137 501  ASN B O   
5005  C  CB  . ASN B 501  ? 1.3182 1.2040 1.2149 -0.0138 0.0406  -0.0959 501  ASN B CB  
5006  C  CG  . ASN B 501  ? 1.5468 1.4410 1.4554 -0.0150 0.0438  -0.0917 501  ASN B CG  
5007  O  OD1 . ASN B 501  ? 1.5626 1.4716 1.4829 -0.0203 0.0414  -0.0953 501  ASN B OD1 
5008  N  ND2 . ASN B 501  ? 1.5835 1.4686 1.4892 -0.0100 0.0493  -0.0843 501  ASN B ND2 
5009  N  N   . GLU B 502  ? 0.9953 0.9090 0.9135 -0.0357 0.0347  -0.1120 502  GLU B N   
5010  C  CA  . GLU B 502  ? 1.0905 1.0057 1.0122 -0.0473 0.0360  -0.1183 502  GLU B CA  
5011  C  C   . GLU B 502  ? 1.1786 1.1005 1.0997 -0.0517 0.0293  -0.1275 502  GLU B C   
5012  O  O   . GLU B 502  ? 1.1829 1.0968 1.0987 -0.0601 0.0306  -0.1328 502  GLU B O   
5013  C  CB  . GLU B 502  ? 1.0352 0.9657 0.9722 -0.0514 0.0372  -0.1178 502  GLU B CB  
5014  C  CG  . GLU B 502  ? 1.0760 0.9965 1.0120 -0.0520 0.0453  -0.1110 502  GLU B CG  
5015  C  CD  . GLU B 502  ? 1.0710 1.0072 1.0218 -0.0539 0.0460  -0.1097 502  GLU B CD  
5016  O  OE1 . GLU B 502  ? 1.0341 0.9861 0.9941 -0.0487 0.0411  -0.1092 502  GLU B OE1 
5017  O  OE2 . GLU B 502  ? 1.0886 1.0208 1.0410 -0.0604 0.0516  -0.1091 502  GLU B OE2 
5018  N  N   . LEU B 503  ? 1.3513 1.2877 1.2775 -0.0462 0.0220  -0.1295 503  LEU B N   
5019  C  CA  . LEU B 503  ? 1.3941 1.3368 1.3188 -0.0489 0.0150  -0.1381 503  LEU B CA  
5020  C  C   . LEU B 503  ? 1.4416 1.3653 1.3488 -0.0463 0.0151  -0.1388 503  LEU B C   
5021  O  O   . LEU B 503  ? 1.5095 1.4292 1.4117 -0.0532 0.0132  -0.1460 503  LEU B O   
5022  C  CB  . LEU B 503  ? 1.2135 1.1750 1.1463 -0.0420 0.0073  -0.1395 503  LEU B CB  
5023  C  CG  . LEU B 503  ? 1.2895 1.2577 1.2198 -0.0434 -0.0007 -0.1484 503  LEU B CG  
5024  C  CD1 . LEU B 503  ? 1.3987 1.3750 1.3367 -0.0560 -0.0016 -0.1570 503  LEU B CD1 
5025  C  CD2 . LEU B 503  ? 1.2318 1.2164 1.1678 -0.0351 -0.0082 -0.1491 503  LEU B CD2 
5026  N  N   . LEU B 504  ? 1.2159 1.1278 1.1136 -0.0366 0.0175  -0.1315 504  LEU B N   
5027  C  CA  . LEU B 504  ? 1.2111 1.1043 1.0916 -0.0333 0.0182  -0.1315 504  LEU B CA  
5028  C  C   . LEU B 504  ? 1.2770 1.1530 1.1490 -0.0415 0.0242  -0.1329 504  LEU B C   
5029  O  O   . LEU B 504  ? 1.3754 1.2396 1.2353 -0.0434 0.0231  -0.1374 504  LEU B O   
5030  C  CB  . LEU B 504  ? 1.1959 1.0799 1.0692 -0.0218 0.0210  -0.1226 504  LEU B CB  
5031  C  CG  . LEU B 504  ? 1.1603 1.0501 1.0305 -0.0124 0.0148  -0.1226 504  LEU B CG  
5032  C  CD1 . LEU B 504  ? 1.2928 1.1725 1.1488 -0.0124 0.0112  -0.1283 504  LEU B CD1 
5033  C  CD2 . LEU B 504  ? 1.1976 1.1103 1.0823 -0.0123 0.0083  -0.1258 504  LEU B CD2 
5034  N  N   . ALA B 505  ? 1.4448 1.3182 1.3221 -0.0460 0.0307  -0.1293 505  ALA B N   
5035  C  CA  . ALA B 505  ? 1.4870 1.3446 1.3568 -0.0546 0.0365  -0.1312 505  ALA B CA  
5036  C  C   . ALA B 505  ? 1.5149 1.3805 1.3900 -0.0661 0.0331  -0.1411 505  ALA B C   
5037  O  O   . ALA B 505  ? 1.6472 1.4987 1.5124 -0.0727 0.0352  -0.1454 505  ALA B O   
5038  C  CB  . ALA B 505  ? 1.4362 1.2897 1.3103 -0.0560 0.0442  -0.1246 505  ALA B CB  
5039  N  N   . ALA B 506  ? 1.1093 0.9974 0.9999 -0.0688 0.0278  -0.1451 506  ALA B N   
5040  C  CA  . ALA B 506  ? 1.0796 0.9778 0.9768 -0.0796 0.0241  -0.1551 506  ALA B CA  
5041  C  C   . ALA B 506  ? 1.1535 1.0489 1.0415 -0.0790 0.0175  -0.1620 506  ALA B C   
5042  O  O   . ALA B 506  ? 1.2282 1.1186 1.1126 -0.0883 0.0170  -0.1694 506  ALA B O   
5043  C  CB  . ALA B 506  ? 1.1123 1.0364 1.0286 -0.0813 0.0199  -0.1574 506  ALA B CB  
5044  N  N   . MET B 507  ? 1.1619 1.0600 1.0455 -0.0681 0.0124  -0.1599 507  MET B N   
5045  C  CA  . MET B 507  ? 1.1294 1.0226 1.0019 -0.0661 0.0064  -0.1657 507  MET B CA  
5046  C  C   . MET B 507  ? 1.0640 0.9310 0.9176 -0.0656 0.0114  -0.1639 507  MET B C   
5047  O  O   . MET B 507  ? 1.0532 0.9133 0.8964 -0.0666 0.0074  -0.1699 507  MET B O   
5048  C  CB  . MET B 507  ? 1.0772 0.9797 0.9495 -0.0540 0.0001  -0.1633 507  MET B CB  
5049  C  CG  . MET B 507  ? 0.9405 0.8664 0.8302 -0.0517 -0.0034 -0.1624 507  MET B CG  
5050  S  SD  . MET B 507  ? 1.3637 1.3026 1.2529 -0.0400 -0.0129 -0.1634 507  MET B SD  
5051  C  CE  . MET B 507  ? 1.1703 1.0914 1.0466 -0.0274 -0.0077 -0.1520 507  MET B CE  
5052  N  N   . LEU B 508  ? 1.0669 0.9192 0.9157 -0.0639 0.0199  -0.1559 508  LEU B N   
5053  C  CA  . LEU B 508  ? 1.0708 0.8976 0.9019 -0.0639 0.0256  -0.1538 508  LEU B CA  
5054  C  C   . LEU B 508  ? 1.1336 0.9507 0.9635 -0.0762 0.0309  -0.1576 508  LEU B C   
5055  O  O   . LEU B 508  ? 1.1116 0.9081 0.9301 -0.0763 0.0382  -0.1533 508  LEU B O   
5056  C  CB  . LEU B 508  ? 1.0530 0.8686 0.8783 -0.0539 0.0317  -0.1429 508  LEU B CB  
5057  C  CG  . LEU B 508  ? 1.1387 0.9532 0.9570 -0.0414 0.0284  -0.1389 508  LEU B CG  
5058  C  CD1 . LEU B 508  ? 1.1867 0.9983 1.0065 -0.0327 0.0338  -0.1284 508  LEU B CD1 
5059  C  CD2 . LEU B 508  ? 1.2366 1.0320 1.0359 -0.0393 0.0282  -0.1414 508  LEU B CD2 
5060  N  N   . GLY B 509  ? 0.9323 0.7637 0.7738 -0.0866 0.0276  -0.1656 509  GLY B N   
5061  C  CA  . GLY B 509  ? 1.0283 0.8508 0.8689 -0.0992 0.0326  -0.1698 509  GLY B CA  
5062  C  C   . GLY B 509  ? 1.0672 0.8820 0.9101 -0.1009 0.0418  -0.1625 509  GLY B C   
5063  O  O   . GLY B 509  ? 1.2624 1.0590 1.0962 -0.1074 0.0483  -0.1628 509  GLY B O   
5064  N  N   . GLN B 510  ? 1.4338 1.2613 1.2878 -0.0950 0.0425  -0.1560 510  GLN B N   
5065  C  CA  . GLN B 510  ? 1.4338 1.2555 1.2903 -0.0955 0.0507  -0.1487 510  GLN B CA  
5066  C  C   . GLN B 510  ? 1.4043 1.2494 1.2803 -0.0975 0.0490  -0.1485 510  GLN B C   
5067  O  O   . GLN B 510  ? 1.4006 1.2539 1.2826 -0.0890 0.0488  -0.1418 510  GLN B O   
5068  C  CB  . GLN B 510  ? 1.3810 1.1894 1.2276 -0.0836 0.0546  -0.1389 510  GLN B CB  
5069  C  CG  . GLN B 510  ? 1.4196 1.2095 1.2585 -0.0848 0.0641  -0.1329 510  GLN B CG  
5070  C  CD  . GLN B 510  ? 1.5638 1.3412 1.3929 -0.0727 0.0675  -0.1238 510  GLN B CD  
5071  O  OE1 . GLN B 510  ? 1.5814 1.3583 1.4050 -0.0646 0.0635  -0.1229 510  GLN B OE1 
5072  N  NE2 . GLN B 510  ? 1.4843 1.2520 1.3112 -0.0713 0.0749  -0.1171 510  GLN B NE2 
5073  N  N   . PRO B 511  ? 1.4914 1.3479 1.3776 -0.1088 0.0477  -0.1559 511  PRO B N   
5074  C  CA  . PRO B 511  ? 1.5275 1.4064 1.4323 -0.1109 0.0464  -0.1558 511  PRO B CA  
5075  C  C   . PRO B 511  ? 1.6145 1.4876 1.5215 -0.1113 0.0548  -0.1485 511  PRO B C   
5076  O  O   . PRO B 511  ? 1.6340 1.4856 1.5281 -0.1100 0.0615  -0.1435 511  PRO B O   
5077  C  CB  . PRO B 511  ? 1.4994 1.3894 1.4126 -0.1236 0.0435  -0.1663 511  PRO B CB  
5078  C  CG  . PRO B 511  ? 1.6362 1.5039 1.5348 -0.1307 0.0477  -0.1697 511  PRO B CG  
5079  C  CD  . PRO B 511  ? 1.6008 1.4501 1.4823 -0.1204 0.0478  -0.1646 511  PRO B CD  
5080  N  N   . GLU B 512  ? 1.6541 1.5460 1.5769 -0.1130 0.0544  -0.1479 512  GLU B N   
5081  C  CA  . GLU B 512  ? 1.6510 1.5411 1.5779 -0.1126 0.0613  -0.1410 512  GLU B CA  
5082  C  C   . GLU B 512  ? 1.5570 1.4289 1.4716 -0.1030 0.0662  -0.1316 512  GLU B C   
5083  O  O   . GLU B 512  ? 1.4929 1.3512 1.4021 -0.1049 0.0739  -0.1271 512  GLU B O   
5084  C  CB  . GLU B 512  ? 1.8119 1.6961 1.7400 -0.1254 0.0678  -0.1445 512  GLU B CB  
5085  C  CG  . GLU B 512  ? 1.8969 1.7569 1.8090 -0.1314 0.0726  -0.1466 512  GLU B CG  
5086  C  CD  . GLU B 512  ? 1.9121 1.7765 1.8258 -0.1417 0.0685  -0.1573 512  GLU B CD  
5087  O  OE1 . GLU B 512  ? 1.8735 1.7606 1.8014 -0.1442 0.0620  -0.1631 512  GLU B OE1 
5088  O  OE2 . GLU B 512  ? 1.8603 1.7053 1.7609 -0.1472 0.0718  -0.1601 512  GLU B OE2 
5089  N  N   . ALA B 513  ? 1.5151 1.3872 1.4255 -0.0924 0.0618  -0.1286 513  ALA B N   
5090  C  CA  . ALA B 513  ? 1.4467 1.3036 1.3465 -0.0827 0.0657  -0.1199 513  ALA B CA  
5091  C  C   . ALA B 513  ? 1.3100 1.1794 1.2203 -0.0754 0.0658  -0.1133 513  ALA B C   
5092  O  O   . ALA B 513  ? 1.2474 1.1358 1.1690 -0.0723 0.0597  -0.1147 513  ALA B O   
5093  C  CB  . ALA B 513  ? 1.4125 1.2620 1.3016 -0.0752 0.0616  -0.1200 513  ALA B CB  
5094  N  N   . GLU B 514  ? 1.5150 1.3734 1.4212 -0.0726 0.0725  -0.1062 514  GLU B N   
5095  C  CA  . GLU B 514  ? 1.5786 1.4474 1.4941 -0.0661 0.0730  -0.0998 514  GLU B CA  
5096  C  C   . GLU B 514  ? 1.4303 1.3000 1.3434 -0.0544 0.0697  -0.0950 514  GLU B C   
5097  O  O   . GLU B 514  ? 1.3535 1.2078 1.2539 -0.0496 0.0712  -0.0926 514  GLU B O   
5098  C  CB  . GLU B 514  ? 1.6379 1.4943 1.5491 -0.0668 0.0812  -0.0942 514  GLU B CB  
5099  C  CG  . GLU B 514  ? 1.6875 1.5383 1.5980 -0.0784 0.0860  -0.0982 514  GLU B CG  
5100  C  CD  . GLU B 514  ? 1.7836 1.6544 1.7100 -0.0850 0.0843  -0.1020 514  GLU B CD  
5101  O  OE1 . GLU B 514  ? 1.7088 1.5987 1.6465 -0.0830 0.0776  -0.1047 514  GLU B OE1 
5102  O  OE2 . GLU B 514  ? 1.8668 1.7336 1.7940 -0.0920 0.0900  -0.1021 514  GLU B OE2 
5103  N  N   . SER B 515  ? 1.0821 0.9696 1.0074 -0.0497 0.0655  -0.0934 515  SER B N   
5104  C  CA  . SER B 515  ? 1.0610 0.9503 0.9851 -0.0388 0.0626  -0.0887 515  SER B CA  
5105  C  C   . SER B 515  ? 1.0611 0.9371 0.9784 -0.0322 0.0684  -0.0805 515  SER B C   
5106  O  O   . SER B 515  ? 1.0611 0.9313 0.9723 -0.0241 0.0678  -0.0767 515  SER B O   
5107  C  CB  . SER B 515  ? 0.9360 0.8466 0.8745 -0.0357 0.0573  -0.0888 515  SER B CB  
5108  O  OG  . SER B 515  ? 1.1114 1.0293 1.0593 -0.0380 0.0603  -0.0864 515  SER B OG  
5109  N  N   . TYR B 516  ? 0.9022 0.7737 0.8204 -0.0353 0.0740  -0.0777 516  TYR B N   
5110  C  CA  . TYR B 516  ? 0.8168 0.6754 0.7280 -0.0291 0.0796  -0.0703 516  TYR B CA  
5111  C  C   . TYR B 516  ? 0.9953 0.8333 0.8904 -0.0280 0.0829  -0.0698 516  TYR B C   
5112  O  O   . TYR B 516  ? 0.9530 0.7833 0.8417 -0.0197 0.0840  -0.0649 516  TYR B O   
5113  C  CB  . TYR B 516  ? 0.8127 0.6701 0.7272 -0.0330 0.0848  -0.0680 516  TYR B CB  
5114  C  CG  . TYR B 516  ? 0.8814 0.7265 0.7891 -0.0264 0.0902  -0.0605 516  TYR B CG  
5115  C  CD1 . TYR B 516  ? 0.8861 0.7335 0.7950 -0.0166 0.0889  -0.0552 516  TYR B CD1 
5116  C  CD2 . TYR B 516  ? 0.8432 0.6743 0.7432 -0.0299 0.0968  -0.0589 516  TYR B CD2 
5117  C  CE1 . TYR B 516  ? 0.8786 0.7161 0.7821 -0.0104 0.0936  -0.0487 516  TYR B CE1 
5118  C  CE2 . TYR B 516  ? 0.7942 0.6146 0.6878 -0.0233 0.1015  -0.0523 516  TYR B CE2 
5119  C  CZ  . TYR B 516  ? 0.8464 0.6706 0.7422 -0.0135 0.0997  -0.0473 516  TYR B CZ  
5120  O  OH  . TYR B 516  ? 0.8000 0.6148 0.6903 -0.0068 0.1041  -0.0410 516  TYR B OH  
5121  N  N   . ASP B 517  ? 1.2857 1.1144 1.1740 -0.0363 0.0846  -0.0750 517  ASP B N   
5122  C  CA  . ASP B 517  ? 1.2868 1.0945 1.1589 -0.0358 0.0882  -0.0747 517  ASP B CA  
5123  C  C   . ASP B 517  ? 1.2967 1.1026 1.1628 -0.0306 0.0838  -0.0762 517  ASP B C   
5124  O  O   . ASP B 517  ? 1.2353 1.0251 1.0886 -0.0259 0.0867  -0.0735 517  ASP B O   
5125  C  CB  . ASP B 517  ? 1.3085 1.1071 1.1752 -0.0468 0.0910  -0.0805 517  ASP B CB  
5126  C  CG  . ASP B 517  ? 1.4311 1.2245 1.2985 -0.0510 0.0974  -0.0779 517  ASP B CG  
5127  O  OD1 . ASP B 517  ? 1.4228 1.2117 1.2886 -0.0442 0.1011  -0.0709 517  ASP B OD1 
5128  O  OD2 . ASP B 517  ? 1.5204 1.3144 1.3900 -0.0611 0.0988  -0.0829 517  ASP B OD2 
5129  N  N   . LEU B 518  ? 1.0638 0.8858 0.9386 -0.0310 0.0769  -0.0804 518  LEU B N   
5130  C  CA  . LEU B 518  ? 0.9989 0.8191 0.8674 -0.0259 0.0725  -0.0820 518  LEU B CA  
5131  C  C   . LEU B 518  ? 1.0104 0.8288 0.8771 -0.0146 0.0734  -0.0747 518  LEU B C   
5132  O  O   . LEU B 518  ? 1.0578 0.8622 0.9123 -0.0095 0.0753  -0.0726 518  LEU B O   
5133  C  CB  . LEU B 518  ? 1.0664 0.9048 0.9448 -0.0288 0.0648  -0.0883 518  LEU B CB  
5134  C  CG  . LEU B 518  ? 1.0620 0.9025 0.9412 -0.0398 0.0629  -0.0969 518  LEU B CG  
5135  C  CD1 . LEU B 518  ? 1.1120 0.9732 1.0028 -0.0414 0.0550  -0.1026 518  LEU B CD1 
5136  C  CD2 . LEU B 518  ? 1.1227 0.9449 0.9861 -0.0419 0.0640  -0.1003 518  LEU B CD2 
5137  N  N   . VAL B 519  ? 0.8693 0.7019 0.7482 -0.0107 0.0721  -0.0709 519  VAL B N   
5138  C  CA  . VAL B 519  ? 0.8788 0.7106 0.7573 -0.0005 0.0731  -0.0641 519  VAL B CA  
5139  C  C   . VAL B 519  ? 0.8730 0.6896 0.7435 0.0028  0.0801  -0.0582 519  VAL B C   
5140  O  O   . VAL B 519  ? 0.8574 0.6669 0.7220 0.0107  0.0820  -0.0534 519  VAL B O   
5141  C  CB  . VAL B 519  ? 0.7842 0.6347 0.6778 0.0024  0.0699  -0.0618 519  VAL B CB  
5142  C  CG1 . VAL B 519  ? 0.6936 0.5585 0.5937 0.0010  0.0627  -0.0672 519  VAL B CG1 
5143  C  CG2 . VAL B 519  ? 0.9434 0.7994 0.8454 -0.0025 0.0726  -0.0609 519  VAL B CG2 
5144  N  N   . ARG B 520  ? 1.1014 0.9125 0.9711 -0.0030 0.0843  -0.0584 520  ARG B N   
5145  C  CA  . ARG B 520  ? 1.1741 0.9701 1.0353 0.0004  0.0910  -0.0529 520  ARG B CA  
5146  C  C   . ARG B 520  ? 1.2255 1.0019 1.0701 0.0009  0.0939  -0.0540 520  ARG B C   
5147  O  O   . ARG B 520  ? 1.1905 0.9549 1.0268 0.0074  0.0983  -0.0489 520  ARG B O   
5148  C  CB  . ARG B 520  ? 1.1031 0.8985 0.9677 -0.0055 0.0948  -0.0527 520  ARG B CB  
5149  C  CG  . ARG B 520  ? 1.1550 0.9384 1.0133 -0.0007 0.1012  -0.0463 520  ARG B CG  
5150  C  CD  . ARG B 520  ? 1.0994 0.8806 0.9592 -0.0072 0.1050  -0.0467 520  ARG B CD  
5151  N  NE  . ARG B 520  ? 1.1259 0.9051 0.9866 -0.0013 0.1090  -0.0401 520  ARG B NE  
5152  C  CZ  . ARG B 520  ? 1.2095 0.9718 1.0585 0.0019  0.1148  -0.0364 520  ARG B CZ  
5153  N  NH1 . ARG B 520  ? 1.2666 1.0112 1.1013 -0.0003 0.1177  -0.0383 520  ARG B NH1 
5154  N  NH2 . ARG B 520  ? 1.2457 1.0087 1.0969 0.0076  0.1175  -0.0307 520  ARG B NH2 
5155  N  N   . SER B 521  ? 1.4064 1.1795 1.2461 -0.0058 0.0914  -0.0608 521  SER B N   
5156  C  CA  . SER B 521  ? 1.4964 1.2504 1.3197 -0.0055 0.0938  -0.0623 521  SER B CA  
5157  C  C   . SER B 521  ? 1.4669 1.2194 1.2852 0.0032  0.0916  -0.0602 521  SER B C   
5158  O  O   . SER B 521  ? 1.5458 1.2824 1.3513 0.0082  0.0954  -0.0574 521  SER B O   
5159  C  CB  . SER B 521  ? 1.5051 1.2566 1.3250 -0.0156 0.0914  -0.0706 521  SER B CB  
5160  O  OG  . SER B 521  ? 1.5893 1.3371 1.4103 -0.0238 0.0952  -0.0721 521  SER B OG  
5161  N  N   . PHE B 522  ? 1.1528 0.9213 0.9805 0.0055  0.0856  -0.0615 522  PHE B N   
5162  C  CA  . PHE B 522  ? 1.1925 0.9597 1.0154 0.0138  0.0837  -0.0594 522  PHE B CA  
5163  C  C   . PHE B 522  ? 1.2216 0.9877 1.0461 0.0229  0.0877  -0.0512 522  PHE B C   
5164  O  O   . PHE B 522  ? 1.2203 0.9754 1.0349 0.0295  0.0903  -0.0481 522  PHE B O   
5165  C  CB  . PHE B 522  ? 1.1912 0.9751 1.0231 0.0137  0.0764  -0.0631 522  PHE B CB  
5166  C  CG  . PHE B 522  ? 1.1843 0.9681 1.0124 0.0227  0.0747  -0.0603 522  PHE B CG  
5167  C  CD1 . PHE B 522  ? 1.2090 0.9814 1.0236 0.0245  0.0737  -0.0630 522  PHE B CD1 
5168  C  CD2 . PHE B 522  ? 1.1301 0.9245 0.9675 0.0293  0.0743  -0.0550 522  PHE B CD2 
5169  C  CE1 . PHE B 522  ? 1.1262 0.8978 0.9365 0.0329  0.0726  -0.0603 522  PHE B CE1 
5170  C  CE2 . PHE B 522  ? 1.0323 0.8258 0.8658 0.0373  0.0734  -0.0523 522  PHE B CE2 
5171  C  CZ  . PHE B 522  ? 1.0794 0.8615 0.8993 0.0392  0.0726  -0.0548 522  PHE B CZ  
5172  N  N   . TRP B 523  ? 1.0831 0.8609 0.9202 0.0233  0.0882  -0.0479 523  TRP B N   
5173  C  CA  . TRP B 523  ? 1.0238 0.8026 0.8641 0.0317  0.0914  -0.0405 523  TRP B CA  
5174  C  C   . TRP B 523  ? 1.0095 0.7726 0.8404 0.0339  0.0982  -0.0365 523  TRP B C   
5175  O  O   . TRP B 523  ? 1.0068 0.7667 0.8362 0.0418  0.1013  -0.0309 523  TRP B O   
5176  C  CB  . TRP B 523  ? 0.9800 0.7765 0.8365 0.0315  0.0892  -0.0386 523  TRP B CB  
5177  C  CG  . TRP B 523  ? 1.0100 0.8208 0.8749 0.0339  0.0835  -0.0397 523  TRP B CG  
5178  C  CD1 . TRP B 523  ? 1.0426 0.8680 0.9175 0.0292  0.0782  -0.0440 523  TRP B CD1 
5179  C  CD2 . TRP B 523  ? 1.0255 0.8367 0.8887 0.0417  0.0828  -0.0366 523  TRP B CD2 
5180  N  NE1 . TRP B 523  ? 1.0246 0.8591 0.9037 0.0339  0.0741  -0.0436 523  TRP B NE1 
5181  C  CE2 . TRP B 523  ? 1.0658 0.8915 0.9378 0.0415  0.0770  -0.0391 523  TRP B CE2 
5182  C  CE3 . TRP B 523  ? 1.0073 0.8082 0.8625 0.0491  0.0868  -0.0319 523  TRP B CE3 
5183  C  CZ2 . TRP B 523  ? 0.9932 0.8222 0.8654 0.0481  0.0752  -0.0369 523  TRP B CZ2 
5184  C  CZ3 . TRP B 523  ? 1.0082 0.8130 0.8644 0.0554  0.0852  -0.0298 523  TRP B CZ3 
5185  C  CH2 . TRP B 523  ? 0.9714 0.7898 0.8357 0.0548  0.0795  -0.0322 523  TRP B CH2 
5186  N  N   . LEU B 524  ? 1.4326 1.1860 1.2573 0.0273  0.1007  -0.0393 524  LEU B N   
5187  C  CA  . LEU B 524  ? 1.5304 1.2655 1.3426 0.0298  0.1071  -0.0362 524  LEU B CA  
5188  C  C   . LEU B 524  ? 1.7279 1.4487 1.5256 0.0334  0.1081  -0.0371 524  LEU B C   
5189  O  O   . LEU B 524  ? 1.8001 1.5252 1.5974 0.0336  0.1037  -0.0402 524  LEU B O   
5190  C  CB  . LEU B 524  ? 1.5364 1.2638 1.3450 0.0214  0.1098  -0.0391 524  LEU B CB  
5191  C  CG  . LEU B 524  ? 1.5741 1.3041 1.3886 0.0217  0.1133  -0.0349 524  LEU B CG  
5192  C  CD1 . LEU B 524  ? 1.4805 1.2317 1.3123 0.0229  0.1094  -0.0334 524  LEU B CD1 
5193  C  CD2 . LEU B 524  ? 1.6049 1.3267 1.4150 0.0126  0.1160  -0.0385 524  LEU B CD2 
5194  N  N   . GLU B 525  ? 2.2169 1.9205 2.0021 0.0368  0.1139  -0.0341 525  GLU B N   
5195  C  CA  . GLU B 525  ? 2.2973 1.9851 2.0673 0.0413  0.1161  -0.0341 525  GLU B CA  
5196  C  C   . GLU B 525  ? 2.2599 1.9547 2.0326 0.0493  0.1140  -0.0314 525  GLU B C   
5197  O  O   . GLU B 525  ? 2.1693 1.8532 1.9303 0.0533  0.1150  -0.0317 525  GLU B O   
5198  C  CB  . GLU B 525  ? 2.2947 1.9728 2.0547 0.0335  0.1141  -0.0414 525  GLU B CB  
5199  C  CG  . GLU B 525  ? 2.2662 1.9541 2.0295 0.0314  0.1074  -0.0465 525  GLU B CG  
5200  C  CD  . GLU B 525  ? 2.5256 2.2050 2.2801 0.0229  0.1052  -0.0543 525  GLU B CD  
5201  O  OE1 . GLU B 525  ? 2.6528 2.3180 2.3986 0.0181  0.1093  -0.0557 525  GLU B OE1 
5202  O  OE2 . GLU B 525  ? 2.6009 2.2876 2.3570 0.0210  0.0994  -0.0591 525  GLU B OE2 
5203  N  N   . GLN B 526  ? 1.7426 1.4550 1.5303 0.0518  0.1114  -0.0286 526  GLN B N   
5204  C  CA  . GLN B 526  ? 1.6633 1.3836 1.4554 0.0592  0.1100  -0.0255 526  GLN B CA  
5205  C  C   . GLN B 526  ? 1.6138 1.3428 1.4163 0.0654  0.1125  -0.0189 526  GLN B C   
5206  O  O   . GLN B 526  ? 1.6844 1.4106 1.4844 0.0732  0.1153  -0.0144 526  GLN B O   
5207  C  CB  . GLN B 526  ? 1.6035 1.3381 1.4041 0.0559  0.1031  -0.0297 526  GLN B CB  
5208  C  CG  . GLN B 526  ? 1.5398 1.2814 1.3437 0.0633  0.1016  -0.0266 526  GLN B CG  
5209  C  CD  . GLN B 526  ? 1.6246 1.3742 1.4303 0.0609  0.0952  -0.0316 526  GLN B CD  
5210  O  OE1 . GLN B 526  ? 1.6918 1.4398 1.4941 0.0541  0.0919  -0.0377 526  GLN B OE1 
5211  N  NE2 . GLN B 526  ? 1.5629 1.3210 1.3739 0.0665  0.0934  -0.0290 526  GLN B NE2 
5212  N  N   . ILE B 527  ? 1.3100 1.0494 1.1240 0.0619  0.1116  -0.0182 527  ILE B N   
5213  C  CA  . ILE B 527  ? 1.3398 1.0874 1.1636 0.0673  0.1138  -0.0124 527  ILE B CA  
5214  C  C   . ILE B 527  ? 1.2428 0.9843 1.0648 0.0660  0.1178  -0.0106 527  ILE B C   
5215  O  O   . ILE B 527  ? 1.1223 0.8676 0.9497 0.0715  0.1203  -0.0056 527  ILE B O   
5216  C  CB  . ILE B 527  ? 1.3408 1.1082 1.1812 0.0662  0.1090  -0.0124 527  ILE B CB  
5217  C  CG1 . ILE B 527  ? 1.3072 1.0817 1.1540 0.0577  0.1060  -0.0166 527  ILE B CG1 
5218  C  CG2 . ILE B 527  ? 1.2972 1.0700 1.1385 0.0681  0.1053  -0.0140 527  ILE B CG2 
5219  C  CD1 . ILE B 527  ? 1.1361 0.9296 0.9984 0.0565  0.1011  -0.0171 527  ILE B CD1 
5220  N  N   . GLY B 528  ? 1.6569 1.3889 1.4714 0.0592  0.1185  -0.0144 528  GLY B N   
5221  C  CA  . GLY B 528  ? 1.6955 1.4195 1.5062 0.0580  0.1228  -0.0127 528  GLY B CA  
5222  C  C   . GLY B 528  ? 1.5513 1.2875 1.3739 0.0523  0.1206  -0.0138 528  GLY B C   
5223  O  O   . GLY B 528  ? 1.6361 1.3886 1.4714 0.0502  0.1159  -0.0152 528  GLY B O   
5224  N  N   . GLU B 529  ? 1.1202 0.8474 0.9376 0.0500  0.1245  -0.0131 529  GLU B N   
5225  C  CA  . GLU B 529  ? 1.1723 0.9094 0.9995 0.0449  0.1233  -0.0137 529  GLU B CA  
5226  C  C   . GLU B 529  ? 1.0761 0.8273 0.9158 0.0511  0.1225  -0.0089 529  GLU B C   
5227  O  O   . GLU B 529  ? 0.9924 0.7589 0.8449 0.0481  0.1188  -0.0099 529  GLU B O   
5228  C  CB  . GLU B 529  ? 1.2175 0.9397 1.0344 0.0411  0.1283  -0.0140 529  GLU B CB  
5229  C  CG  . GLU B 529  ? 1.2982 1.0291 1.1239 0.0369  0.1281  -0.0139 529  GLU B CG  
5230  C  CD  . GLU B 529  ? 1.2626 1.0063 1.0981 0.0281  0.1234  -0.0193 529  GLU B CD  
5231  O  OE1 . GLU B 529  ? 1.1820 0.9205 1.0123 0.0220  0.1221  -0.0244 529  GLU B OE1 
5232  O  OE2 . GLU B 529  ? 1.1834 0.9426 1.0320 0.0274  0.1208  -0.0187 529  GLU B OE2 
5233  N  N   . THR B 530  ? 1.2502 0.9964 1.0864 0.0597  0.1258  -0.0037 530  THR B N   
5234  C  CA  . THR B 530  ? 1.2421 1.0021 1.0905 0.0657  0.1247  0.0006  530  THR B CA  
5235  C  C   . THR B 530  ? 1.2511 1.0262 1.1110 0.0669  0.1200  0.0000  530  THR B C   
5236  O  O   . THR B 530  ? 1.2701 1.0600 1.1431 0.0682  0.1174  0.0016  530  THR B O   
5237  C  CB  . THR B 530  ? 1.1869 0.9386 1.0291 0.0748  0.1293  0.0059  530  THR B CB  
5238  O  OG1 . THR B 530  ? 1.2326 0.9986 1.0876 0.0803  0.1280  0.0096  530  THR B OG1 
5239  C  CG2 . THR B 530  ? 1.2413 0.9837 1.0745 0.0790  0.1309  0.0063  530  THR B CG2 
5240  N  N   . GLY B 531  ? 1.4613 1.2323 1.3159 0.0666  0.1188  -0.0022 531  GLY B N   
5241  C  CA  . GLY B 531  ? 1.3818 1.1660 1.2459 0.0674  0.1143  -0.0030 531  GLY B CA  
5242  C  C   . GLY B 531  ? 1.4022 1.1983 1.2754 0.0601  0.1093  -0.0074 531  GLY B C   
5243  O  O   . GLY B 531  ? 1.4400 1.2508 1.3252 0.0610  0.1056  -0.0070 531  GLY B O   
5244  N  N   . TRP B 532  ? 1.0860 0.8759 0.9536 0.0527  0.1092  -0.0117 532  TRP B N   
5245  C  CA  . TRP B 532  ? 1.0490 0.8508 0.9256 0.0455  0.1048  -0.0161 532  TRP B CA  
5246  C  C   . TRP B 532  ? 1.0868 0.8999 0.9748 0.0454  0.1045  -0.0138 532  TRP B C   
5247  O  O   . TRP B 532  ? 1.1163 0.9442 1.0159 0.0432  0.1002  -0.0154 532  TRP B O   
5248  C  CB  . TRP B 532  ? 1.0277 0.8197 0.8957 0.0373  0.1056  -0.0212 532  TRP B CB  
5249  C  CG  . TRP B 532  ? 0.9848 0.7882 0.8619 0.0294  0.1023  -0.0254 532  TRP B CG  
5250  C  CD1 . TRP B 532  ? 1.1160 0.9209 0.9965 0.0253  0.1042  -0.0253 532  TRP B CD1 
5251  C  CD2 . TRP B 532  ? 1.0304 0.8454 0.9144 0.0251  0.0966  -0.0304 532  TRP B CD2 
5252  N  NE1 . TRP B 532  ? 1.0734 0.8905 0.9628 0.0185  0.1003  -0.0299 532  TRP B NE1 
5253  C  CE2 . TRP B 532  ? 1.0455 0.8693 0.9374 0.0183  0.0955  -0.0331 532  TRP B CE2 
5254  C  CE3 . TRP B 532  ? 1.1004 0.9192 0.9841 0.0266  0.0925  -0.0328 532  TRP B CE3 
5255  C  CZ2 . TRP B 532  ? 1.1064 0.9433 1.0066 0.0131  0.0903  -0.0383 532  TRP B CZ2 
5256  C  CZ3 . TRP B 532  ? 1.0423 0.8736 0.9336 0.0217  0.0871  -0.0378 532  TRP B CZ3 
5257  C  CH2 . TRP B 532  ? 1.1167 0.9573 1.0165 0.0150  0.0860  -0.0406 532  TRP B CH2 
5258  N  N   . GLN B 533  ? 1.1239 0.9298 1.0082 0.0482  0.1089  -0.0101 533  GLN B N   
5259  C  CA  . GLN B 533  ? 1.0705 0.8863 0.9646 0.0488  0.1087  -0.0078 533  GLN B CA  
5260  C  C   . GLN B 533  ? 1.0191 0.8483 0.9246 0.0551  0.1062  -0.0045 533  GLN B C   
5261  O  O   . GLN B 533  ? 1.0053 0.8481 0.9224 0.0539  0.1031  -0.0047 533  GLN B O   
5262  C  CB  . GLN B 533  ? 1.1300 0.9339 1.0159 0.0510  0.1140  -0.0046 533  GLN B CB  
5263  C  CG  . GLN B 533  ? 1.2017 0.9932 1.0776 0.0439  0.1168  -0.0078 533  GLN B CG  
5264  C  CD  . GLN B 533  ? 1.2002 1.0018 1.0843 0.0358  0.1141  -0.0118 533  GLN B CD  
5265  O  OE1 . GLN B 533  ? 1.2246 1.0399 1.1202 0.0365  0.1118  -0.0107 533  GLN B OE1 
5266  N  NE2 . GLN B 533  ? 1.1396 0.9345 1.0179 0.0279  0.1146  -0.0166 533  GLN B NE2 
5267  N  N   . VAL B 534  ? 0.7883 0.6135 0.6906 0.0617  0.1076  -0.0015 534  VAL B N   
5268  C  CA  . VAL B 534  ? 0.7253 0.5625 0.6382 0.0672  0.1056  0.0015  534  VAL B CA  
5269  C  C   . VAL B 534  ? 0.7225 0.5709 0.6431 0.0644  0.1005  -0.0016 534  VAL B C   
5270  O  O   . VAL B 534  ? 0.7287 0.5905 0.6611 0.0657  0.0976  -0.0007 534  VAL B O   
5271  C  CB  . VAL B 534  ? 0.6330 0.4628 0.5402 0.0747  0.1090  0.0053  534  VAL B CB  
5272  C  CG1 . VAL B 534  ? 0.5708 0.4126 0.4889 0.0794  0.1070  0.0077  534  VAL B CG1 
5273  C  CG2 . VAL B 534  ? 0.6402 0.4619 0.5421 0.0788  0.1136  0.0089  534  VAL B CG2 
5274  N  N   . ALA B 535  ? 1.1965 1.0395 1.1103 0.0606  0.0993  -0.0055 535  ALA B N   
5275  C  CA  . ALA B 535  ? 1.2772 1.1302 1.1971 0.0584  0.0942  -0.0086 535  ALA B CA  
5276  C  C   . ALA B 535  ? 1.2566 1.1219 1.1864 0.0530  0.0906  -0.0114 535  ALA B C   
5277  O  O   . ALA B 535  ? 1.2728 1.1507 1.2124 0.0536  0.0867  -0.0120 535  ALA B O   
5278  C  CB  . ALA B 535  ? 1.3142 1.1582 1.2236 0.0556  0.0935  -0.0126 535  ALA B CB  
5279  N  N   . LEU B 536  ? 0.9039 0.7655 0.8312 0.0478  0.0922  -0.0132 536  LEU B N   
5280  C  CA  . LEU B 536  ? 0.8392 0.7124 0.7760 0.0428  0.0894  -0.0156 536  LEU B CA  
5281  C  C   . LEU B 536  ? 0.9629 0.8457 0.9098 0.0468  0.0893  -0.0118 536  LEU B C   
5282  O  O   . LEU B 536  ? 0.9420 0.8380 0.8992 0.0453  0.0856  -0.0131 536  LEU B O   
5283  C  CB  . LEU B 536  ? 0.9383 0.8039 0.8691 0.0362  0.0920  -0.0183 536  LEU B CB  
5284  C  CG  . LEU B 536  ? 1.0113 0.8727 0.9364 0.0295  0.0905  -0.0240 536  LEU B CG  
5285  C  CD1 . LEU B 536  ? 1.0803 0.9379 1.0032 0.0221  0.0929  -0.0267 536  LEU B CD1 
5286  C  CD2 . LEU B 536  ? 0.8321 0.7073 0.7657 0.0281  0.0846  -0.0275 536  LEU B CD2 
5287  N  N   . ALA B 537  ? 1.2751 1.1516 1.2189 0.0520  0.0930  -0.0073 537  ALA B N   
5288  C  CA  . ALA B 537  ? 1.1258 1.0112 1.0788 0.0561  0.0927  -0.0038 537  ALA B CA  
5289  C  C   . ALA B 537  ? 1.0924 0.9895 1.0552 0.0594  0.0891  -0.0029 537  ALA B C   
5290  O  O   . ALA B 537  ? 1.1589 1.0682 1.1319 0.0583  0.0858  -0.0037 537  ALA B O   
5291  C  CB  . ALA B 537  ? 1.1951 1.0714 1.1423 0.0617  0.0973  0.0007  537  ALA B CB  
5292  N  N   . ASN B 538  ? 1.1815 1.0743 1.1408 0.0636  0.0899  -0.0014 538  ASN B N   
5293  C  CA  . ASN B 538  ? 1.1699 1.0718 1.1368 0.0664  0.0869  -0.0007 538  ASN B CA  
5294  C  C   . ASN B 538  ? 1.2007 1.1064 1.1678 0.0623  0.0829  -0.0052 538  ASN B C   
5295  O  O   . ASN B 538  ? 1.3121 1.2170 1.2766 0.0567  0.0819  -0.0089 538  ASN B O   
5296  C  CB  . ASN B 538  ? 1.1350 1.0307 1.0978 0.0725  0.0898  0.0027  538  ASN B CB  
5297  C  CG  . ASN B 538  ? 1.2510 1.1416 1.2119 0.0768  0.0940  0.0067  538  ASN B CG  
5298  O  OD1 . ASN B 538  ? 1.2686 1.1626 1.2334 0.0762  0.0943  0.0075  538  ASN B OD1 
5299  N  ND2 . ASN B 538  ? 1.2979 1.1805 1.2526 0.0815  0.0974  0.0093  538  ASN B ND2 
5300  N  N   . GLY B 539  ? 0.9029 0.8130 0.8729 0.0651  0.0808  -0.0048 539  GLY B N   
5301  C  CA  . GLY B 539  ? 1.0076 0.9214 0.9771 0.0622  0.0767  -0.0090 539  GLY B CA  
5302  C  C   . GLY B 539  ? 1.0898 0.9948 1.0499 0.0645  0.0773  -0.0093 539  GLY B C   
5303  O  O   . GLY B 539  ? 1.0835 0.9909 1.0421 0.0630  0.0738  -0.0127 539  GLY B O   
5304  N  N   . VAL B 540  ? 0.7929 0.6878 0.7462 0.0684  0.0818  -0.0060 540  VAL B N   
5305  C  CA  . VAL B 540  ? 0.6555 0.5416 0.5997 0.0716  0.0831  -0.0056 540  VAL B CA  
5306  C  C   . VAL B 540  ? 0.7441 0.6160 0.6764 0.0714  0.0872  -0.0054 540  VAL B C   
5307  O  O   . VAL B 540  ? 0.7465 0.6151 0.6780 0.0699  0.0896  -0.0046 540  VAL B O   
5308  C  CB  . VAL B 540  ? 0.5811 0.4692 0.5291 0.0780  0.0849  -0.0010 540  VAL B CB  
5309  C  CG1 . VAL B 540  ? 0.6046 0.5052 0.5631 0.0782  0.0809  -0.0014 540  VAL B CG1 
5310  C  CG2 . VAL B 540  ? 0.4802 0.3671 0.4313 0.0811  0.0891  0.0033  540  VAL B CG2 
5311  N  N   . ILE B 541  ? 0.7884 0.6510 0.7104 0.0733  0.0880  -0.0061 541  ILE B N   
5312  C  CA  . ILE B 541  ? 0.7987 0.6464 0.7082 0.0746  0.0924  -0.0053 541  ILE B CA  
5313  C  C   . ILE B 541  ? 0.9470 0.7901 0.8535 0.0818  0.0959  -0.0009 541  ILE B C   
5314  O  O   . ILE B 541  ? 1.0774 0.9213 0.9823 0.0841  0.0944  -0.0012 541  ILE B O   
5315  C  CB  . ILE B 541  ? 0.8545 0.6940 0.7532 0.0702  0.0906  -0.0105 541  ILE B CB  
5316  C  CG1 . ILE B 541  ? 0.7704 0.6132 0.6717 0.0627  0.0884  -0.0147 541  ILE B CG1 
5317  C  CG2 . ILE B 541  ? 1.0388 0.8619 0.9234 0.0729  0.0951  -0.0094 541  ILE B CG2 
5318  C  CD1 . ILE B 541  ? 0.8612 0.6952 0.7520 0.0576  0.0872  -0.0199 541  ILE B CD1 
5319  N  N   . ALA B 542  ? 1.1496 0.9879 1.0551 0.0855  0.1006  0.0031  542  ALA B N   
5320  C  CA  . ALA B 542  ? 1.2529 1.0896 1.1585 0.0924  0.1042  0.0076  542  ALA B CA  
5321  C  C   . ALA B 542  ? 1.3072 1.1309 1.1991 0.0953  0.1067  0.0075  542  ALA B C   
5322  O  O   . ALA B 542  ? 1.3025 1.1253 1.1941 0.1007  0.1093  0.0106  542  ALA B O   
5323  C  CB  . ALA B 542  ? 1.1210 0.9576 1.0301 0.0958  0.1083  0.0117  542  ALA B CB  
5324  N  N   . GLU B 543  ? 1.8670 1.6802 1.7474 0.0918  0.1063  0.0038  543  GLU B N   
5325  C  CA  . GLU B 543  ? 1.9771 1.7766 1.8434 0.0948  0.1089  0.0035  543  GLU B CA  
5326  C  C   . GLU B 543  ? 1.9540 1.7545 1.8170 0.0948  0.1054  0.0010  543  GLU B C   
5327  O  O   . GLU B 543  ? 1.9596 1.7518 1.8136 0.0994  0.1078  0.0023  543  GLU B O   
5328  C  CB  . GLU B 543  ? 2.1027 1.8891 1.9569 0.0912  0.1102  0.0006  543  GLU B CB  
5329  C  CG  . GLU B 543  ? 2.0765 1.8569 1.9290 0.0933  0.1151  0.0039  543  GLU B CG  
5330  C  CD  . GLU B 543  ? 2.0879 1.8765 1.9498 0.0889  0.1135  0.0033  543  GLU B CD  
5331  O  OE1 . GLU B 543  ? 1.9841 1.7826 1.8536 0.0836  0.1087  0.0001  543  GLU B OE1 
5332  O  OE2 . GLU B 543  ? 2.2045 1.9896 2.0660 0.0910  0.1171  0.0062  543  GLU B OE2 
5333  N  N   . THR B 544  ? 1.6541 1.4645 1.5238 0.0902  0.0998  -0.0026 544  THR B N   
5334  C  CA  . THR B 544  ? 1.6814 1.4924 1.5469 0.0900  0.0958  -0.0058 544  THR B CA  
5335  C  C   . THR B 544  ? 1.5807 1.4016 1.4550 0.0940  0.0949  -0.0028 544  THR B C   
5336  O  O   . THR B 544  ? 1.5248 1.3581 1.4119 0.0923  0.0927  -0.0022 544  THR B O   
5337  C  CB  . THR B 544  ? 1.7357 1.5519 1.6027 0.0828  0.0901  -0.0119 544  THR B CB  
5338  O  OG1 . THR B 544  ? 1.7933 1.6002 1.6529 0.0784  0.0915  -0.0145 544  THR B OG1 
5339  C  CG2 . THR B 544  ? 1.6238 1.4394 1.4846 0.0832  0.0858  -0.0155 544  THR B CG2 
5340  N  N   . VAL B 545  ? 1.3423 1.1570 1.2093 0.0992  0.0968  -0.0010 545  VAL B N   
5341  C  CA  . VAL B 545  ? 1.3197 1.1414 1.1925 0.1030  0.0962  0.0014  545  VAL B CA  
5342  C  C   . VAL B 545  ? 1.4202 1.2319 1.2798 0.1072  0.0970  0.0011  545  VAL B C   
5343  O  O   . VAL B 545  ? 1.4987 1.2980 1.3468 0.1095  0.1006  0.0017  545  VAL B O   
5344  C  CB  . VAL B 545  ? 1.2919 1.1188 1.1749 0.1066  0.1008  0.0072  545  VAL B CB  
5345  C  CG1 . VAL B 545  ? 1.2540 1.0700 1.1291 0.1114  0.1073  0.0108  545  VAL B CG1 
5346  C  CG2 . VAL B 545  ? 1.2040 1.0389 1.0944 0.1093  0.0998  0.0093  545  VAL B CG2 
5347  N  N   . ALA B 546  ? 1.3259 1.1424 1.1865 0.1085  0.0935  0.0002  546  ALA B N   
5348  C  CA  . ALA B 546  ? 1.2751 1.0823 1.1226 0.1128  0.0937  -0.0004 546  ALA B CA  
5349  C  C   . ALA B 546  ? 1.3444 1.1443 1.1881 0.1191  0.1008  0.0053  546  ALA B C   
5350  O  O   . ALA B 546  ? 1.2999 1.1065 1.1536 0.1214  0.1035  0.0096  546  ALA B O   
5351  C  CB  . ALA B 546  ? 1.2019 1.0164 1.0518 0.1134  0.0886  -0.0021 546  ALA B CB  
5352  N  N   . PRO B 547  ? 1.2987 1.0851 1.1284 0.1220  0.1042  0.0055  547  PRO B N   
5353  C  CA  . PRO B 547  ? 1.3854 1.1652 1.2118 0.1282  0.1114  0.0109  547  PRO B CA  
5354  C  C   . PRO B 547  ? 1.2861 1.0667 1.1115 0.1329  0.1123  0.0134  547  PRO B C   
5355  O  O   . PRO B 547  ? 1.1866 0.9678 1.0075 0.1327  0.1075  0.0105  547  PRO B O   
5356  C  CB  . PRO B 547  ? 1.3831 1.1475 1.1927 0.1299  0.1137  0.0094  547  PRO B CB  
5357  C  CG  . PRO B 547  ? 1.2510 1.0151 1.0583 0.1235  0.1084  0.0035  547  PRO B CG  
5358  C  CD  . PRO B 547  ? 1.1538 0.9305 0.9705 0.1196  0.1017  0.0005  547  PRO B CD  
5359  N  N   . VAL B 548  ? 1.7197 1.5004 1.5494 0.1372  0.1187  0.0190  548  VAL B N   
5360  C  CA  . VAL B 548  ? 1.7285 1.5091 1.5576 0.1416  0.1210  0.0221  548  VAL B CA  
5361  C  C   . VAL B 548  ? 1.6683 1.4342 1.4795 0.1469  0.1242  0.0225  548  VAL B C   
5362  O  O   . VAL B 548  ? 1.6640 1.4216 1.4690 0.1496  0.1295  0.0245  548  VAL B O   
5363  C  CB  . VAL B 548  ? 1.8560 1.6436 1.6983 0.1434  0.1267  0.0277  548  VAL B CB  
5364  C  CG1 . VAL B 548  ? 1.7326 1.5212 1.5758 0.1468  0.1285  0.0305  548  VAL B CG1 
5365  C  CG2 . VAL B 548  ? 1.9228 1.7236 1.7814 0.1384  0.1238  0.0271  548  VAL B CG2 
5366  N  N   . ILE B 549  ? 1.3910 1.1536 1.1936 0.1486  0.1209  0.0206  549  ILE B N   
5367  C  CA  . ILE B 549  ? 1.4234 1.1719 1.2080 0.1539  0.1232  0.0206  549  ILE B CA  
5368  C  C   . ILE B 549  ? 1.3990 1.1466 1.1822 0.1588  0.1262  0.0244  549  ILE B C   
5369  O  O   . ILE B 549  ? 1.4088 1.1662 1.2033 0.1575  0.1247  0.0256  549  ILE B O   
5370  C  CB  . ILE B 549  ? 1.4059 1.1490 1.1779 0.1521  0.1162  0.0142  549  ILE B CB  
5371  C  CG1 . ILE B 549  ? 1.3311 1.0836 1.1082 0.1498  0.1089  0.0111  549  ILE B CG1 
5372  C  CG2 . ILE B 549  ? 1.3720 1.1143 1.1443 0.1470  0.1141  0.0105  549  ILE B CG2 
5373  C  CD1 . ILE B 549  ? 1.4626 1.2100 1.2266 0.1495  0.1022  0.0050  549  ILE B CD1 
5374  N  N   . GLU B 550  ? 1.3027 1.0375 1.0712 0.1647  0.1309  0.0264  550  GLU B N   
5375  C  CA  . GLU B 550  ? 1.3448 1.0758 1.1090 0.1700  0.1349  0.0303  550  GLU B CA  
5376  C  C   . GLU B 550  ? 1.3302 1.0496 1.0749 0.1739  0.1319  0.0273  550  GLU B C   
5377  O  O   . GLU B 550  ? 1.3371 1.0439 1.0674 0.1783  0.1359  0.0281  550  GLU B O   
5378  C  CB  . GLU B 550  ? 1.4784 1.2054 1.2442 0.1741  0.1449  0.0364  550  GLU B CB  
5379  C  CG  . GLU B 550  ? 1.5610 1.3007 1.3469 0.1710  0.1480  0.0398  550  GLU B CG  
5380  C  CD  . GLU B 550  ? 1.6680 1.4052 1.4565 0.1754  0.1578  0.0459  550  GLU B CD  
5381  O  OE1 . GLU B 550  ? 1.7290 1.4544 1.5033 0.1809  0.1625  0.0478  550  GLU B OE1 
5382  O  OE2 . GLU B 550  ? 1.6509 1.3984 1.4557 0.1733  0.1609  0.0487  550  GLU B OE2 
5383  N  N   . PRO B 551  ? 1.6008 1.3241 1.3441 0.1729  0.1246  0.0238  551  PRO B N   
5384  C  CA  . PRO B 551  ? 1.6268 1.3398 1.3515 0.1771  0.1212  0.0207  551  PRO B CA  
5385  C  C   . PRO B 551  ? 1.7375 1.4422 1.4534 0.1842  0.1270  0.0256  551  PRO B C   
5386  O  O   . PRO B 551  ? 1.7133 1.4219 1.4391 0.1850  0.1328  0.0309  551  PRO B O   
5387  C  CB  . PRO B 551  ? 1.6216 1.3442 1.3509 0.1734  0.1114  0.0154  551  PRO B CB  
5388  C  CG  . PRO B 551  ? 1.5938 1.3299 1.3426 0.1698  0.1121  0.0182  551  PRO B CG  
5389  C  CD  . PRO B 551  ? 1.6425 1.3802 1.4012 0.1680  0.1191  0.0221  551  PRO B CD  
5390  N  N   . THR B 552  ? 1.5268 1.2198 1.2237 0.1892  0.1254  0.0237  552  THR B N   
5391  C  CA  . THR B 552  ? 1.4303 1.1135 1.1156 0.1965  0.1305  0.0278  552  THR B CA  
5392  C  C   . THR B 552  ? 1.4211 1.1062 1.1018 0.1984  0.1238  0.0254  552  THR B C   
5393  O  O   . THR B 552  ? 1.4146 1.1039 1.0931 0.1959  0.1147  0.0192  552  THR B O   
5394  C  CB  . THR B 552  ? 1.4046 1.0716 1.0698 0.2021  0.1343  0.0280  552  THR B CB  
5395  O  OG1 . THR B 552  ? 1.6815 1.3386 1.3354 0.2093  0.1400  0.0324  552  THR B OG1 
5396  C  CG2 . THR B 552  ? 1.3479 1.0106 1.0000 0.2015  0.1256  0.0206  552  THR B CG2 
5397  N  N   . LEU B 553  ? 1.1741 0.8563 0.8534 0.2027  0.1286  0.0303  553  LEU B N   
5398  C  CA  . LEU B 553  ? 1.0914 0.7749 0.7665 0.2053  0.1233  0.0290  553  LEU B CA  
5399  C  C   . LEU B 553  ? 1.0938 0.7621 0.7454 0.2134  0.1233  0.0285  553  LEU B C   
5400  O  O   . LEU B 553  ? 1.1237 0.7800 0.7649 0.2183  0.1315  0.0328  553  LEU B O   
5401  C  CB  . LEU B 553  ? 1.0955 0.7841 0.7826 0.2052  0.1283  0.0344  553  LEU B CB  
5402  C  CG  . LEU B 553  ? 1.0756 0.7699 0.7646 0.2058  0.1218  0.0327  553  LEU B CG  
5403  C  CD1 . LEU B 553  ? 0.9512 0.6590 0.6504 0.1998  0.1117  0.0263  553  LEU B CD1 
5404  C  CD2 . LEU B 553  ? 1.0027 0.7009 0.7038 0.2052  0.1277  0.0383  553  LEU B CD2 
5405  N  N   . ASN B 554  ? 1.1208 0.7901 0.7641 0.2149  0.1141  0.0232  554  ASN B N   
5406  C  CA  . ASN B 554  ? 1.1981 0.8539 0.8184 0.2227  0.1124  0.0218  554  ASN B CA  
5407  C  C   . ASN B 554  ? 1.2688 0.9228 0.8853 0.2279  0.1127  0.0248  554  ASN B C   
5408  O  O   . ASN B 554  ? 1.3378 1.0010 0.9595 0.2266  0.1049  0.0214  554  ASN B O   
5409  C  CB  . ASN B 554  ? 1.2898 0.9476 0.9025 0.2214  0.1017  0.0135  554  ASN B CB  
5410  C  CG  . ASN B 554  ? 1.5204 1.1631 1.1084 0.2293  0.1005  0.0117  554  ASN B CG  
5411  O  OD1 . ASN B 554  ? 1.6116 1.2411 1.1873 0.2358  0.1085  0.0170  554  ASN B OD1 
5412  N  ND2 . ASN B 554  ? 1.6278 1.2723 1.2082 0.2288  0.0906  0.0041  554  ASN B ND2 
5413  N  N   . GLU B 555  ? 1.5369 1.1786 1.1437 0.2339  0.1219  0.0310  555  GLU B N   
5414  C  CA  . GLU B 555  ? 1.5481 1.1864 1.1508 0.2388  0.1235  0.0346  555  GLU B CA  
5415  C  C   . GLU B 555  ? 1.7221 1.3534 1.3052 0.2457  0.1159  0.0305  555  GLU B C   
5416  O  O   . GLU B 555  ? 1.7442 1.3794 1.3279 0.2476  0.1114  0.0299  555  GLU B O   
5417  C  CB  . GLU B 555  ? 1.6740 1.3008 1.2720 0.2428  0.1363  0.0425  555  GLU B CB  
5418  C  CG  . GLU B 555  ? 1.6767 1.3077 1.2897 0.2375  0.1445  0.0462  555  GLU B CG  
5419  C  CD  . GLU B 555  ? 1.6820 1.3308 1.3199 0.2287  0.1414  0.0450  555  GLU B CD  
5420  O  OE1 . GLU B 555  ? 1.6687 1.3246 1.3149 0.2274  0.1384  0.0453  555  GLU B OE1 
5421  O  OE2 . GLU B 555  ? 1.7420 1.3972 1.3903 0.2235  0.1420  0.0439  555  GLU B OE2 
5422  N  N   . GLY B 556  ? 2.0710 1.6920 1.6362 0.2499  0.1143  0.0276  556  GLY B N   
5423  C  CA  . GLY B 556  ? 2.1088 1.7216 1.6534 0.2576  0.1079  0.0242  556  GLY B CA  
5424  C  C   . GLY B 556  ? 2.0484 1.6743 1.5984 0.2549  0.0949  0.0167  556  GLY B C   
5425  O  O   . GLY B 556  ? 2.0435 1.6678 1.5836 0.2606  0.0894  0.0150  556  GLY B O   
5426  N  N   . ALA B 557  ? 1.3801 1.0192 0.9460 0.2462  0.0901  0.0122  557  ALA B N   
5427  C  CA  . ALA B 557  ? 1.3276 0.9802 0.8998 0.2429  0.0781  0.0047  557  ALA B CA  
5428  C  C   . ALA B 557  ? 1.3065 0.9704 0.8927 0.2415  0.0761  0.0063  557  ALA B C   
5429  O  O   . ALA B 557  ? 1.2334 0.9019 0.8156 0.2447  0.0679  0.0024  557  ALA B O   
5430  C  CB  . ALA B 557  ? 1.1842 0.8465 0.7688 0.2338  0.0745  -0.0002 557  ALA B CB  
5431  N  N   . ILE B 558  ? 1.9522 1.6207 1.5548 0.2369  0.0834  0.0118  558  ILE B N   
5432  C  CA  . ILE B 558  ? 1.9404 1.6190 1.5566 0.2352  0.0820  0.0135  558  ILE B CA  
5433  C  C   . ILE B 558  ? 1.9352 1.6030 1.5387 0.2437  0.0856  0.0182  558  ILE B C   
5434  O  O   . ILE B 558  ? 1.8853 1.5595 1.4947 0.2444  0.0824  0.0183  558  ILE B O   
5435  C  CB  . ILE B 558  ? 1.8438 1.5308 1.4816 0.2274  0.0884  0.0175  558  ILE B CB  
5436  C  CG1 . ILE B 558  ? 1.8381 1.5130 1.4721 0.2298  0.1008  0.0251  558  ILE B CG1 
5437  C  CG2 . ILE B 558  ? 1.7105 1.4077 1.3601 0.2193  0.0847  0.0128  558  ILE B CG2 
5438  C  CD1 . ILE B 558  ? 1.8195 1.5026 1.4741 0.2224  0.1071  0.0286  558  ILE B CD1 
5439  N  N   . ARG B 559  ? 1.6673 1.3182 1.2529 0.2505  0.0925  0.0221  559  ARG B N   
5440  C  CA  . ARG B 559  ? 1.6798 1.3187 1.2513 0.2590  0.0965  0.0267  559  ARG B CA  
5441  C  C   . ARG B 559  ? 1.6469 1.2818 1.2001 0.2667  0.0871  0.0218  559  ARG B C   
5442  O  O   . ARG B 559  ? 1.6778 1.3099 1.2248 0.2724  0.0858  0.0233  559  ARG B O   
5443  C  CB  . ARG B 559  ? 1.7515 1.3737 1.3114 0.2631  0.1084  0.0334  559  ARG B CB  
5444  C  CG  . ARG B 559  ? 1.7782 1.3871 1.3251 0.2709  0.1147  0.0393  559  ARG B CG  
5445  C  CD  . ARG B 559  ? 1.9171 1.5116 1.4564 0.2734  0.1278  0.0462  559  ARG B CD  
5446  N  NE  . ARG B 559  ? 2.0726 1.6616 1.6026 0.2741  0.1282  0.0439  559  ARG B NE  
5447  C  CZ  . ARG B 559  ? 2.0766 1.6590 1.6071 0.2730  0.1382  0.0483  559  ARG B CZ  
5448  N  NH1 . ARG B 559  ? 2.2912 1.8723 1.8317 0.2710  0.1488  0.0552  559  ARG B NH1 
5449  N  NH2 . ARG B 559  ? 1.8040 1.3811 1.3247 0.2740  0.1376  0.0456  559  ARG B NH2 
5450  N  N   . ALA B 560  ? 1.4634 1.0982 1.0076 0.2672  0.0806  0.0156  560  ALA B N   
5451  C  CA  . ALA B 560  ? 1.5506 1.1830 1.0778 0.2743  0.0709  0.0100  560  ALA B CA  
5452  C  C   . ALA B 560  ? 1.6204 1.2719 1.1617 0.2689  0.0591  0.0025  560  ALA B C   
5453  O  O   . ALA B 560  ? 1.6891 1.3472 1.2316 0.2651  0.0520  -0.0043 560  ALA B O   
5454  C  CB  . ALA B 560  ? 1.6534 1.2738 1.1615 0.2783  0.0705  0.0074  560  ALA B CB  
5455  N  N   . THR B 561  ? 2.0109 1.6711 1.5630 0.2684  0.0573  0.0037  561  THR B N   
5456  C  CA  . THR B 561  ? 1.8824 1.5612 1.4488 0.2637  0.0469  -0.0027 561  THR B CA  
5457  C  C   . THR B 561  ? 1.8719 1.5512 1.4328 0.2709  0.0430  -0.0021 561  THR B C   
5458  O  O   . THR B 561  ? 1.8891 1.5595 1.4474 0.2746  0.0506  0.0048  561  THR B O   
5459  C  CB  . THR B 561  ? 1.7031 1.3957 1.2952 0.2528  0.0495  -0.0016 561  THR B CB  
5460  O  OG1 . THR B 561  ? 1.6193 1.3075 1.2147 0.2476  0.0562  0.0004  561  THR B OG1 
5461  C  CG2 . THR B 561  ? 1.6587 1.3703 1.2647 0.2469  0.0387  -0.0093 561  THR B CG2 
5462  N  N   . PRO B 562  ? 1.8825 1.5717 1.4413 0.2732  0.0314  -0.0093 562  PRO B N   
5463  C  CA  . PRO B 562  ? 1.9398 1.6291 1.4918 0.2812  0.0272  -0.0090 562  PRO B CA  
5464  C  C   . PRO B 562  ? 1.8835 1.5778 1.4506 0.2784  0.0317  -0.0040 562  PRO B C   
5465  O  O   . PRO B 562  ? 1.9033 1.5879 1.4604 0.2859  0.0348  0.0006  562  PRO B O   
5466  C  CB  . PRO B 562  ? 1.9690 1.6737 1.5234 0.2809  0.0136  -0.0186 562  PRO B CB  
5467  C  CG  . PRO B 562  ? 1.9504 1.6535 1.4996 0.2777  0.0113  -0.0233 562  PRO B CG  
5468  C  CD  . PRO B 562  ? 1.7651 1.4631 1.3235 0.2702  0.0219  -0.0180 562  PRO B CD  
5469  N  N   . ILE B 563  ? 1.4949 1.2032 1.0849 0.2680  0.0322  -0.0046 563  ILE B N   
5470  C  CA  . ILE B 563  ? 1.3806 1.0957 0.9868 0.2644  0.0355  -0.0008 563  ILE B CA  
5471  C  C   . ILE B 563  ? 1.3692 1.0903 0.9724 0.2706  0.0275  -0.0036 563  ILE B C   
5472  O  O   . ILE B 563  ? 1.3872 1.0961 0.9763 0.2793  0.0303  0.0005  563  ILE B O   
5473  C  CB  . ILE B 563  ? 1.4007 1.1009 1.0039 0.2657  0.0482  0.0084  563  ILE B CB  
5474  C  CG1 . ILE B 563  ? 1.4617 1.1549 1.0651 0.2613  0.0559  0.0109  563  ILE B CG1 
5475  C  CG2 . ILE B 563  ? 1.2830 0.9912 0.9049 0.2604  0.0515  0.0117  563  ILE B CG2 
5476  C  CD1 . ILE B 563  ? 1.5479 1.2250 1.1448 0.2639  0.0685  0.0195  563  ILE B CD1 
5477  N  N   . PRO B 564  ? 1.3963 1.1358 1.0121 0.2666  0.0179  -0.0103 564  PRO B N   
5478  C  CA  . PRO B 564  ? 1.4024 1.1483 1.0141 0.2734  0.0095  -0.0138 564  PRO B CA  
5479  C  C   . PRO B 564  ? 1.3748 1.1190 0.9922 0.2751  0.0139  -0.0083 564  PRO B C   
5480  O  O   . PRO B 564  ? 1.3533 1.0998 0.9860 0.2678  0.0205  -0.0042 564  PRO B O   
5481  C  CB  . PRO B 564  ? 1.3673 1.1347 0.9949 0.2665  -0.0004 -0.0221 564  PRO B CB  
5482  C  CG  . PRO B 564  ? 1.2774 1.0503 0.9228 0.2548  0.0050  -0.0207 564  PRO B CG  
5483  C  CD  . PRO B 564  ? 1.2815 1.0366 0.9159 0.2557  0.0147  -0.0151 564  PRO B CD  
5484  N  N   . GLN B 565  ? 1.4582 1.1980 1.0623 0.2852  0.0098  -0.0085 565  GLN B N   
5485  C  CA  . GLN B 565  ? 1.5363 1.2723 1.1412 0.2891  0.0129  -0.0039 565  GLN B CA  
5486  C  C   . GLN B 565  ? 1.5010 1.2552 1.1173 0.2890  0.0031  -0.0094 565  GLN B C   
5487  O  O   . GLN B 565  ? 1.5328 1.2992 1.1490 0.2901  -0.0069 -0.0169 565  GLN B O   
5488  C  CB  . GLN B 565  ? 1.5072 1.2233 1.0870 0.3016  0.0158  0.0002  565  GLN B CB  
5489  C  CG  . GLN B 565  ? 1.4192 1.1189 0.9821 0.3046  0.0214  0.0028  565  GLN B CG  
5490  C  CD  . GLN B 565  ? 1.4019 1.0921 0.9713 0.2979  0.0341  0.0099  565  GLN B CD  
5491  O  OE1 . GLN B 565  ? 1.3059 0.9873 0.8761 0.2986  0.0420  0.0163  565  GLN B OE1 
5492  N  NE2 . GLN B 565  ? 1.5216 1.2138 1.0960 0.2914  0.0361  0.0087  565  GLN B NE2 
5493  N  N   . PRO B 566  ? 1.2537 1.0104 0.8800 0.2877  0.0059  -0.0062 566  PRO B N   
5494  C  CA  . PRO B 566  ? 1.2958 1.0695 0.9327 0.2881  -0.0029 -0.0111 566  PRO B CA  
5495  C  C   . PRO B 566  ? 1.3988 1.1686 1.0175 0.3010  -0.0098 -0.0134 566  PRO B C   
5496  O  O   . PRO B 566  ? 1.6137 1.3662 1.2111 0.3099  -0.0071 -0.0104 566  PRO B O   
5497  C  CB  . PRO B 566  ? 1.2572 1.0304 0.9072 0.2837  0.0037  -0.0058 566  PRO B CB  
5498  C  CG  . PRO B 566  ? 1.1978 0.9493 0.8357 0.2864  0.0150  0.0023  566  PRO B CG  
5499  C  CD  . PRO B 566  ? 1.1311 0.8759 0.7608 0.2850  0.0173  0.0020  566  PRO B CD  
5500  N  N   . GLY B 567  ? 2.0638 1.8502 1.6911 0.3021  -0.0188 -0.0188 567  GLY B N   
5501  C  CA  . GLY B 567  ? 2.1812 1.9668 1.7935 0.3144  -0.0263 -0.0216 567  GLY B CA  
5502  C  C   . GLY B 567  ? 2.2605 2.0699 1.8848 0.3130  -0.0383 -0.0305 567  GLY B C   
5503  O  O   . GLY B 567  ? 2.3395 2.1651 1.9849 0.3026  -0.0396 -0.0333 567  GLY B O   
5504  N  N   . ASP B 568  ? 2.2371 2.0480 1.8471 0.3240  -0.0467 -0.0347 568  ASP B N   
5505  C  CA  . ASP B 568  ? 2.1950 2.0276 1.8125 0.3254  -0.0590 -0.0436 568  ASP B CA  
5506  C  C   . ASP B 568  ? 2.1489 1.9958 1.7823 0.3240  -0.0616 -0.0446 568  ASP B C   
5507  O  O   . ASP B 568  ? 2.1677 2.0342 1.8093 0.3248  -0.0714 -0.0519 568  ASP B O   
5508  C  CB  . ASP B 568  ? 2.1858 2.0334 1.8161 0.3152  -0.0634 -0.0502 568  ASP B CB  
5509  C  CG  . ASP B 568  ? 2.2450 2.0808 1.8585 0.3178  -0.0632 -0.0511 568  ASP B CG  
5510  O  OD1 . ASP B 568  ? 2.3272 2.1468 1.9184 0.3292  -0.0624 -0.0484 568  ASP B OD1 
5511  O  OD2 . ASP B 568  ? 2.0809 1.9232 1.7029 0.3086  -0.0637 -0.0546 568  ASP B OD2 
5512  N  N   . GLY B 569  ? 1.5776 1.4158 1.2156 0.3219  -0.0533 -0.0377 569  GLY B N   
5513  C  CA  . GLY B 569  ? 1.5425 1.3921 1.1930 0.3220  -0.0557 -0.0383 569  GLY B CA  
5514  C  C   . GLY B 569  ? 1.5425 1.4059 1.2182 0.3085  -0.0530 -0.0387 569  GLY B C   
5515  O  O   . GLY B 569  ? 1.5468 1.4037 1.2290 0.2996  -0.0451 -0.0347 569  GLY B O   
5516  N  N   . VAL B 570  ? 1.3971 1.2799 1.0872 0.3072  -0.0596 -0.0435 570  VAL B N   
5517  C  CA  . VAL B 570  ? 1.3357 1.2319 1.0492 0.2953  -0.0574 -0.0439 570  VAL B CA  
5518  C  C   . VAL B 570  ? 1.2822 1.1888 1.0072 0.2844  -0.0585 -0.0480 570  VAL B C   
5519  O  O   . VAL B 570  ? 1.2586 1.1758 0.9820 0.2855  -0.0663 -0.0548 570  VAL B O   
5520  C  CB  . VAL B 570  ? 1.3246 1.2390 1.0492 0.2976  -0.0645 -0.0484 570  VAL B CB  
5521  C  CG1 . VAL B 570  ? 1.1621 1.0867 0.9087 0.2864  -0.0609 -0.0474 570  VAL B CG1 
5522  C  CG2 . VAL B 570  ? 1.4430 1.3465 1.1525 0.3105  -0.0649 -0.0453 570  VAL B CG2 
5523  N  N   . GLU B 571  ? 1.5328 1.4364 1.2694 0.2740  -0.0507 -0.0441 571  GLU B N   
5524  C  CA  . GLU B 571  ? 1.4196 1.3300 1.1661 0.2635  -0.0502 -0.0469 571  GLU B CA  
5525  C  C   . GLU B 571  ? 1.3893 1.3191 1.1590 0.2534  -0.0520 -0.0502 571  GLU B C   
5526  O  O   . GLU B 571  ? 1.3601 1.2946 1.1391 0.2529  -0.0509 -0.0485 571  GLU B O   
5527  C  CB  . GLU B 571  ? 1.4151 1.3076 1.1571 0.2592  -0.0399 -0.0401 571  GLU B CB  
5528  C  CG  . GLU B 571  ? 1.3290 1.2173 1.0821 0.2537  -0.0316 -0.0339 571  GLU B CG  
5529  C  CD  . GLU B 571  ? 1.4943 1.3663 1.2436 0.2497  -0.0216 -0.0275 571  GLU B CD  
5530  O  OE1 . GLU B 571  ? 1.5947 1.4577 1.3317 0.2517  -0.0208 -0.0276 571  GLU B OE1 
5531  O  OE2 . GLU B 571  ? 1.4272 1.2956 1.1858 0.2446  -0.0146 -0.0226 571  GLU B OE2 
5532  N  N   . ILE B 572  ? 1.0046 0.9451 0.7831 0.2452  -0.0547 -0.0552 572  ILE B N   
5533  C  CA  . ILE B 572  ? 0.8450 0.8030 0.6449 0.2346  -0.0558 -0.0584 572  ILE B CA  
5534  C  C   . ILE B 572  ? 0.8526 0.8043 0.6586 0.2246  -0.0484 -0.0553 572  ILE B C   
5535  O  O   . ILE B 572  ? 0.9541 0.8981 0.7513 0.2237  -0.0475 -0.0559 572  ILE B O   
5536  C  CB  . ILE B 572  ? 0.8407 0.8184 0.6469 0.2333  -0.0656 -0.0676 572  ILE B CB  
5537  C  CG1 . ILE B 572  ? 0.8320 0.8157 0.6305 0.2445  -0.0733 -0.0709 572  ILE B CG1 
5538  C  CG2 . ILE B 572  ? 0.8671 0.8623 0.6952 0.2224  -0.0660 -0.0706 572  ILE B CG2 
5539  C  CD1 . ILE B 572  ? 0.7426 0.7343 0.5510 0.2462  -0.0735 -0.0696 572  ILE B CD1 
5540  N  N   . VAL B 573  ? 0.9418 0.8965 0.7622 0.2175  -0.0433 -0.0521 573  VAL B N   
5541  C  CA  . VAL B 573  ? 0.9458 0.8954 0.7733 0.2081  -0.0362 -0.0489 573  VAL B CA  
5542  C  C   . VAL B 573  ? 0.9158 0.8834 0.7618 0.1982  -0.0389 -0.0536 573  VAL B C   
5543  O  O   . VAL B 573  ? 0.9147 0.8930 0.7733 0.1961  -0.0399 -0.0541 573  VAL B O   
5544  C  CB  . VAL B 573  ? 0.8720 0.8093 0.7007 0.2078  -0.0274 -0.0409 573  VAL B CB  
5545  C  CG1 . VAL B 573  ? 0.9019 0.8330 0.7358 0.1994  -0.0202 -0.0376 573  VAL B CG1 
5546  C  CG2 . VAL B 573  ? 0.7605 0.6808 0.5709 0.2181  -0.0249 -0.0364 573  VAL B CG2 
5547  N  N   . PHE B 574  ? 1.0279 0.9981 0.8752 0.1922  -0.0399 -0.0572 574  PHE B N   
5548  C  CA  . PHE B 574  ? 1.0288 1.0145 0.8924 0.1824  -0.0419 -0.0617 574  PHE B CA  
5549  C  C   . PHE B 574  ? 1.0554 1.0358 0.9279 0.1743  -0.0337 -0.0567 574  PHE B C   
5550  O  O   . PHE B 574  ? 1.0566 1.0247 0.9227 0.1724  -0.0287 -0.0538 574  PHE B O   
5551  C  CB  . PHE B 574  ? 1.0153 1.0060 0.8755 0.1797  -0.0470 -0.0683 574  PHE B CB  
5552  C  CG  . PHE B 574  ? 1.0923 1.0897 0.9443 0.1875  -0.0556 -0.0739 574  PHE B CG  
5553  C  CD1 . PHE B 574  ? 1.0999 1.0841 0.9332 0.1967  -0.0565 -0.0726 574  PHE B CD1 
5554  C  CD2 . PHE B 574  ? 1.0043 1.0214 0.8671 0.1858  -0.0629 -0.0807 574  PHE B CD2 
5555  C  CE1 . PHE B 574  ? 1.0888 1.0793 0.9140 0.2045  -0.0649 -0.0779 574  PHE B CE1 
5556  C  CE2 . PHE B 574  ? 1.0410 1.0653 0.8967 0.1933  -0.0712 -0.0861 574  PHE B CE2 
5557  C  CZ  . PHE B 574  ? 1.1339 1.1449 0.9706 0.2028  -0.0724 -0.0847 574  PHE B CZ  
5558  N  N   . ARG B 575  ? 1.0713 1.0612 0.9586 0.1699  -0.0326 -0.0559 575  ARG B N   
5559  C  CA  . ARG B 575  ? 1.0080 0.9942 0.9044 0.1627  -0.0254 -0.0514 575  ARG B CA  
5560  C  C   . ARG B 575  ? 0.9534 0.9549 0.8658 0.1537  -0.0271 -0.0555 575  ARG B C   
5561  O  O   . ARG B 575  ? 0.9618 0.9778 0.8811 0.1539  -0.0330 -0.0603 575  ARG B O   
5562  C  CB  . ARG B 575  ? 0.9125 0.8930 0.8111 0.1659  -0.0209 -0.0454 575  ARG B CB  
5563  C  CG  . ARG B 575  ? 0.9745 0.9377 0.8581 0.1736  -0.0171 -0.0402 575  ARG B CG  
5564  C  CD  . ARG B 575  ? 1.1429 1.0930 1.0189 0.1715  -0.0115 -0.0371 575  ARG B CD  
5565  N  NE  . ARG B 575  ? 1.0103 0.9588 0.8968 0.1642  -0.0049 -0.0334 575  ARG B NE  
5566  C  CZ  . ARG B 575  ? 1.0610 1.0062 0.9483 0.1586  -0.0017 -0.0332 575  ARG B CZ  
5567  N  NH1 . ARG B 575  ? 1.0359 0.9787 0.9143 0.1590  -0.0043 -0.0366 575  ARG B NH1 
5568  N  NH2 . ARG B 575  ? 1.1281 1.0723 1.0250 0.1528  0.0041  -0.0295 575  ARG B NH2 
5569  N  N   . PRO B 576  ? 0.7618 0.7604 0.6798 0.1461  -0.0221 -0.0537 576  PRO B N   
5570  C  CA  . PRO B 576  ? 0.8025 0.8145 0.7354 0.1375  -0.0230 -0.0569 576  PRO B CA  
5571  C  C   . PRO B 576  ? 0.8484 0.8680 0.7926 0.1372  -0.0222 -0.0550 576  PRO B C   
5572  O  O   . PRO B 576  ? 0.8182 0.8296 0.7612 0.1403  -0.0179 -0.0494 576  PRO B O   
5573  C  CB  . PRO B 576  ? 0.7314 0.7346 0.6649 0.1311  -0.0167 -0.0541 576  PRO B CB  
5574  C  CG  . PRO B 576  ? 0.8059 0.7926 0.7287 0.1363  -0.0114 -0.0479 576  PRO B CG  
5575  C  CD  . PRO B 576  ? 0.7155 0.6987 0.6259 0.1451  -0.0157 -0.0491 576  PRO B CD  
5576  N  N   . ASP B 577  ? 0.9633 0.9988 0.9186 0.1334  -0.0263 -0.0598 577  ASP B N   
5577  C  CA  . ASP B 577  ? 0.8779 0.9214 0.8443 0.1328  -0.0258 -0.0584 577  ASP B CA  
5578  C  C   . ASP B 577  ? 0.8759 0.9142 0.8492 0.1270  -0.0190 -0.0536 577  ASP B C   
5579  O  O   . ASP B 577  ? 0.8958 0.9321 0.8710 0.1206  -0.0164 -0.0539 577  ASP B O   
5580  C  CB  . ASP B 577  ? 0.8112 0.8732 0.7881 0.1294  -0.0313 -0.0648 577  ASP B CB  
5581  C  CG  . ASP B 577  ? 0.8352 0.9058 0.8212 0.1312  -0.0320 -0.0639 577  ASP B CG  
5582  O  OD1 . ASP B 577  ? 0.8059 0.8731 0.7864 0.1390  -0.0334 -0.0621 577  ASP B OD1 
5583  O  OD2 . ASP B 577  ? 0.9079 0.9881 0.9060 0.1249  -0.0311 -0.0652 577  ASP B OD2 
5584  N  N   . PRO B 578  ? 0.7437 0.7790 0.7204 0.1292  -0.0161 -0.0491 578  PRO B N   
5585  C  CA  . PRO B 578  ? 0.7594 0.7896 0.7424 0.1242  -0.0098 -0.0445 578  PRO B CA  
5586  C  C   . PRO B 578  ? 0.7408 0.7814 0.7356 0.1161  -0.0095 -0.0470 578  PRO B C   
5587  O  O   . PRO B 578  ? 0.7533 0.7887 0.7506 0.1112  -0.0047 -0.0444 578  PRO B O   
5588  C  CB  . PRO B 578  ? 0.7203 0.7484 0.7055 0.1285  -0.0083 -0.0407 578  PRO B CB  
5589  C  CG  . PRO B 578  ? 0.7879 0.8116 0.7621 0.1368  -0.0116 -0.0411 578  PRO B CG  
5590  C  CD  . PRO B 578  ? 0.8249 0.8590 0.7979 0.1369  -0.0179 -0.0476 578  PRO B CD  
5591  N  N   . SER B 579  ? 0.7973 0.8522 0.7990 0.1147  -0.0144 -0.0520 579  SER B N   
5592  C  CA  . SER B 579  ? 0.7911 0.8561 0.8041 0.1072  -0.0138 -0.0544 579  SER B CA  
5593  C  C   . SER B 579  ? 0.8694 0.9414 0.8829 0.1024  -0.0168 -0.0601 579  SER B C   
5594  O  O   . SER B 579  ? 0.8861 0.9622 0.9065 0.0952  -0.0148 -0.0613 579  SER B O   
5595  C  CB  . SER B 579  ? 0.7047 0.7816 0.7272 0.1081  -0.0162 -0.0556 579  SER B CB  
5596  O  OG  . SER B 579  ? 0.7847 0.8695 0.8050 0.1135  -0.0221 -0.0595 579  SER B OG  
5597  N  N   . LEU B 580  ? 0.7447 0.8179 0.7508 0.1061  -0.0214 -0.0638 580  LEU B N   
5598  C  CA  . LEU B 580  ? 0.6897 0.7708 0.6969 0.1015  -0.0249 -0.0700 580  LEU B CA  
5599  C  C   . LEU B 580  ? 0.7833 0.8532 0.7800 0.1005  -0.0237 -0.0703 580  LEU B C   
5600  O  O   . LEU B 580  ? 0.8578 0.9323 0.8556 0.0951  -0.0255 -0.0751 580  LEU B O   
5601  C  CB  . LEU B 580  ? 0.6557 0.7497 0.6638 0.1060  -0.0321 -0.0755 580  LEU B CB  
5602  C  CG  . LEU B 580  ? 0.6984 0.8102 0.7199 0.1016  -0.0347 -0.0800 580  LEU B CG  
5603  C  CD1 . LEU B 580  ? 0.7075 0.8202 0.7372 0.1004  -0.0307 -0.0757 580  LEU B CD1 
5604  C  CD2 . LEU B 580  ? 0.7784 0.9025 0.8001 0.1075  -0.0418 -0.0849 580  LEU B CD2 
5605  N  N   . PHE B 581  ? 0.7796 0.8346 0.7660 0.1053  -0.0206 -0.0653 581  PHE B N   
5606  C  CA  . PHE B 581  ? 0.7771 0.8199 0.7524 0.1052  -0.0190 -0.0649 581  PHE B CA  
5607  C  C   . PHE B 581  ? 0.8499 0.8982 0.8194 0.1069  -0.0255 -0.0714 581  PHE B C   
5608  O  O   . PHE B 581  ? 0.8751 0.9273 0.8410 0.1139  -0.0301 -0.0727 581  PHE B O   
5609  C  CB  . PHE B 581  ? 0.7676 0.8060 0.7465 0.0972  -0.0138 -0.0636 581  PHE B CB  
5610  C  CG  . PHE B 581  ? 0.8429 0.8652 0.8106 0.0981  -0.0096 -0.0604 581  PHE B CG  
5611  C  CD1 . PHE B 581  ? 0.7860 0.7966 0.7470 0.1039  -0.0059 -0.0544 581  PHE B CD1 
5612  C  CD2 . PHE B 581  ? 0.8341 0.8528 0.7977 0.0931  -0.0093 -0.0635 581  PHE B CD2 
5613  C  CE1 . PHE B 581  ? 0.7603 0.7566 0.7111 0.1050  -0.0018 -0.0515 581  PHE B CE1 
5614  C  CE2 . PHE B 581  ? 0.7704 0.7743 0.7233 0.0943  -0.0054 -0.0606 581  PHE B CE2 
5615  C  CZ  . PHE B 581  ? 0.7182 0.7111 0.6648 0.1004  -0.0017 -0.0546 581  PHE B CZ  
5616  N  N   . ASP B 582  ? 1.0474 1.0958 1.0153 0.1012  -0.0262 -0.0755 582  ASP B N   
5617  C  CA  . ASP B 582  ? 0.9780 1.0314 0.9404 0.1023  -0.0325 -0.0820 582  ASP B CA  
5618  C  C   . ASP B 582  ? 1.0034 1.0762 0.9771 0.0991  -0.0381 -0.0887 582  ASP B C   
5619  O  O   . ASP B 582  ? 1.0254 1.1048 0.9966 0.0988  -0.0437 -0.0950 582  ASP B O   
5620  C  CB  . ASP B 582  ? 0.9790 1.0235 0.9347 0.0972  -0.0306 -0.0838 582  ASP B CB  
5621  C  CG  . ASP B 582  ? 1.1730 1.2207 1.1384 0.0871  -0.0270 -0.0847 582  ASP B CG  
5622  O  OD1 . ASP B 582  ? 1.2407 1.2897 1.2145 0.0851  -0.0228 -0.0806 582  ASP B OD1 
5623  O  OD2 . ASP B 582  ? 1.2299 1.2785 1.1941 0.0813  -0.0282 -0.0896 582  ASP B OD2 
5624  N  N   . GLY B 583  ? 0.8676 0.9499 0.8536 0.0967  -0.0368 -0.0875 583  GLY B N   
5625  C  CA  . GLY B 583  ? 0.8519 0.9528 0.8496 0.0930  -0.0412 -0.0935 583  GLY B CA  
5626  C  C   . GLY B 583  ? 0.8846 0.9908 0.8918 0.0823  -0.0384 -0.0960 583  GLY B C   
5627  O  O   . GLY B 583  ? 0.9450 1.0671 0.9627 0.0784  -0.0414 -0.1011 583  GLY B O   
5628  N  N   . PHE B 584  ? 0.9031 0.9963 0.9067 0.0776  -0.0325 -0.0925 584  PHE B N   
5629  C  CA  . PHE B 584  ? 0.8794 0.9759 0.8911 0.0677  -0.0291 -0.0942 584  PHE B CA  
5630  C  C   . PHE B 584  ? 0.8757 0.9815 0.8999 0.0656  -0.0269 -0.0922 584  PHE B C   
5631  O  O   . PHE B 584  ? 0.8722 0.9896 0.9062 0.0589  -0.0273 -0.0963 584  PHE B O   
5632  C  CB  . PHE B 584  ? 0.8156 0.8950 0.8198 0.0644  -0.0230 -0.0901 584  PHE B CB  
5633  C  CG  . PHE B 584  ? 0.8667 0.9472 0.8772 0.0546  -0.0191 -0.0917 584  PHE B CG  
5634  C  CD1 . PHE B 584  ? 0.9106 0.9951 0.9212 0.0481  -0.0213 -0.0982 584  PHE B CD1 
5635  C  CD2 . PHE B 584  ? 0.9798 1.0571 0.9958 0.0519  -0.0134 -0.0867 584  PHE B CD2 
5636  C  CE1 . PHE B 584  ? 1.0651 1.1494 1.0807 0.0389  -0.0173 -0.0995 584  PHE B CE1 
5637  C  CE2 . PHE B 584  ? 1.0288 1.1061 1.0495 0.0433  -0.0096 -0.0879 584  PHE B CE2 
5638  C  CZ  . PHE B 584  ? 1.0865 1.1669 1.1069 0.0367  -0.0114 -0.0942 584  PHE B CZ  
5639  N  N   . TYR B 585  ? 0.8665 0.9673 0.8903 0.0711  -0.0245 -0.0862 585  TYR B N   
5640  C  CA  . TYR B 585  ? 0.7708 0.8784 0.8051 0.0698  -0.0222 -0.0837 585  TYR B CA  
5641  C  C   . TYR B 585  ? 0.6778 0.8003 0.7187 0.0743  -0.0274 -0.0865 585  TYR B C   
5642  O  O   . TYR B 585  ? 0.7096 0.8349 0.7560 0.0766  -0.0260 -0.0834 585  TYR B O   
5643  C  CB  . TYR B 585  ? 0.7821 0.8770 0.8134 0.0730  -0.0170 -0.0761 585  TYR B CB  
5644  C  CG  . TYR B 585  ? 0.8033 0.8835 0.8280 0.0696  -0.0117 -0.0728 585  TYR B CG  
5645  C  CD1 . TYR B 585  ? 0.7545 0.8336 0.7843 0.0624  -0.0072 -0.0720 585  TYR B CD1 
5646  C  CD2 . TYR B 585  ? 0.8690 0.9361 0.8820 0.0740  -0.0109 -0.0703 585  TYR B CD2 
5647  C  CE1 . TYR B 585  ? 0.7706 0.8361 0.7940 0.0599  -0.0023 -0.0690 585  TYR B CE1 
5648  C  CE2 . TYR B 585  ? 0.8201 0.8739 0.8271 0.0713  -0.0059 -0.0673 585  TYR B CE2 
5649  C  CZ  . TYR B 585  ? 0.8006 0.8537 0.8129 0.0644  -0.0017 -0.0667 585  TYR B CZ  
5650  O  OH  . TYR B 585  ? 0.8137 0.8535 0.8196 0.0623  0.0032  -0.0637 585  TYR B OH  
5651  N  N   . ALA B 586  ? 0.6335 0.7656 0.6737 0.0758  -0.0334 -0.0926 586  ALA B N   
5652  C  CA  . ALA B 586  ? 0.6552 0.8021 0.7015 0.0806  -0.0385 -0.0955 586  ALA B CA  
5653  C  C   . ALA B 586  ? 0.6038 0.7657 0.6640 0.0744  -0.0380 -0.0984 586  ALA B C   
5654  O  O   . ALA B 586  ? 0.6218 0.7951 0.6884 0.0783  -0.0407 -0.0994 586  ALA B O   
5655  C  CB  . ALA B 586  ? 0.7046 0.8582 0.7462 0.0844  -0.0454 -0.1014 586  ALA B CB  
5656  N  N   . ASN B 587  ? 0.8744 1.0361 0.9390 0.0652  -0.0343 -0.0997 587  ASN B N   
5657  C  CA  . ASN B 587  ? 0.9561 1.1302 1.0332 0.0589  -0.0326 -0.1018 587  ASN B CA  
5658  C  C   . ASN B 587  ? 1.0129 1.1806 1.0930 0.0581  -0.0268 -0.0956 587  ASN B C   
5659  O  O   . ASN B 587  ? 1.0793 1.2571 1.1693 0.0548  -0.0255 -0.0965 587  ASN B O   
5660  C  CB  . ASN B 587  ? 1.1145 1.2912 1.1945 0.0490  -0.0313 -0.1066 587  ASN B CB  
5661  C  CG  . ASN B 587  ? 1.1156 1.3079 1.2087 0.0426  -0.0305 -0.1102 587  ASN B CG  
5662  O  OD1 . ASN B 587  ? 1.0562 1.2618 1.1567 0.0463  -0.0333 -0.1117 587  ASN B OD1 
5663  N  ND2 . ASN B 587  ? 1.0469 1.2370 1.1427 0.0332  -0.0262 -0.1116 587  ASN B ND2 
5664  N  N   . ASN B 588  ? 0.9807 1.1324 1.0528 0.0611  -0.0234 -0.0895 588  ASN B N   
5665  C  CA  . ASN B 588  ? 0.9095 1.0550 0.9843 0.0605  -0.0181 -0.0837 588  ASN B CA  
5666  C  C   . ASN B 588  ? 0.9461 1.0978 1.0249 0.0671  -0.0201 -0.0819 588  ASN B C   
5667  O  O   . ASN B 588  ? 0.8614 1.0095 0.9344 0.0746  -0.0227 -0.0804 588  ASN B O   
5668  C  CB  . ASN B 588  ? 0.8661 0.9935 0.9315 0.0619  -0.0141 -0.0781 588  ASN B CB  
5669  C  CG  . ASN B 588  ? 0.8998 1.0209 0.9683 0.0586  -0.0082 -0.0733 588  ASN B CG  
5670  O  OD1 . ASN B 588  ? 0.9877 1.1095 1.0596 0.0620  -0.0072 -0.0698 588  ASN B OD1 
5671  N  ND2 . ASN B 588  ? 0.8889 1.0035 0.9558 0.0522  -0.0043 -0.0731 588  ASN B ND2 
5672  N  N   . GLY B 589  ? 0.9227 1.0833 1.0110 0.0643  -0.0185 -0.0821 589  GLY B N   
5673  C  CA  . GLY B 589  ? 0.8568 1.0236 0.9492 0.0702  -0.0203 -0.0808 589  GLY B CA  
5674  C  C   . GLY B 589  ? 0.8681 1.0220 0.9556 0.0750  -0.0176 -0.0742 589  GLY B C   
5675  O  O   . GLY B 589  ? 0.8434 0.9974 0.9292 0.0820  -0.0199 -0.0728 589  GLY B O   
5676  N  N   . TRP B 590  ? 0.8190 0.9614 0.9040 0.0712  -0.0125 -0.0702 590  TRP B N   
5677  C  CA  . TRP B 590  ? 0.8145 0.9452 0.8958 0.0751  -0.0096 -0.0642 590  TRP B CA  
5678  C  C   . TRP B 590  ? 0.8955 1.0175 0.9675 0.0817  -0.0115 -0.0625 590  TRP B C   
5679  O  O   . TRP B 590  ? 0.9009 1.0187 0.9711 0.0873  -0.0116 -0.0593 590  TRP B O   
5680  C  CB  . TRP B 590  ? 0.7946 0.9155 0.8749 0.0700  -0.0041 -0.0607 590  TRP B CB  
5681  C  CG  . TRP B 590  ? 0.8018 0.9284 0.8900 0.0650  -0.0014 -0.0607 590  TRP B CG  
5682  C  CD1 . TRP B 590  ? 0.8955 1.0334 0.9915 0.0654  -0.0028 -0.0624 590  TRP B CD1 
5683  C  CD2 . TRP B 590  ? 0.7991 0.9197 0.8876 0.0592  0.0034  -0.0589 590  TRP B CD2 
5684  N  NE1 . TRP B 590  ? 0.8578 0.9971 0.9587 0.0601  0.0008  -0.0617 590  TRP B NE1 
5685  C  CE2 . TRP B 590  ? 0.8257 0.9543 0.9219 0.0563  0.0047  -0.0595 590  TRP B CE2 
5686  C  CE3 . TRP B 590  ? 0.7963 0.9052 0.8786 0.0566  0.0069  -0.0567 590  TRP B CE3 
5687  C  CZ2 . TRP B 590  ? 0.8401 0.9650 0.9377 0.0511  0.0092  -0.0579 590  TRP B CZ2 
5688  C  CZ3 . TRP B 590  ? 0.8269 0.9323 0.9108 0.0514  0.0113  -0.0552 590  TRP B CZ3 
5689  C  CH2 . TRP B 590  ? 0.7805 0.8938 0.8718 0.0488  0.0124  -0.0558 590  TRP B CH2 
5690  N  N   . LEU B 591  ? 0.6813 0.8000 0.7469 0.0810  -0.0129 -0.0647 591  LEU B N   
5691  C  CA  . LEU B 591  ? 0.6153 0.7246 0.6708 0.0873  -0.0143 -0.0629 591  LEU B CA  
5692  C  C   . LEU B 591  ? 0.5975 0.7149 0.6518 0.0937  -0.0200 -0.0661 591  LEU B C   
5693  O  O   . LEU B 591  ? 0.5874 0.6976 0.6349 0.1006  -0.0208 -0.0634 591  LEU B O   
5694  C  CB  . LEU B 591  ? 0.6671 0.7689 0.7152 0.0846  -0.0136 -0.0641 591  LEU B CB  
5695  C  CG  . LEU B 591  ? 0.6383 0.7291 0.6849 0.0798  -0.0076 -0.0602 591  LEU B CG  
5696  C  CD1 . LEU B 591  ? 0.6623 0.7450 0.7003 0.0779  -0.0071 -0.0615 591  LEU B CD1 
5697  C  CD2 . LEU B 591  ? 0.6157 0.6966 0.6605 0.0836  -0.0040 -0.0539 591  LEU B CD2 
5698  N  N   . GLN B 592  ? 0.6046 0.7367 0.6652 0.0918  -0.0239 -0.0717 592  GLN B N   
5699  C  CA  . GLN B 592  ? 0.6726 0.8136 0.7326 0.0983  -0.0296 -0.0750 592  GLN B CA  
5700  C  C   . GLN B 592  ? 0.6942 0.8369 0.7572 0.1035  -0.0296 -0.0722 592  GLN B C   
5701  O  O   . GLN B 592  ? 0.6091 0.7517 0.6673 0.1112  -0.0330 -0.0723 592  GLN B O   
5702  C  CB  . GLN B 592  ? 0.6509 0.8086 0.7181 0.0945  -0.0336 -0.0819 592  GLN B CB  
5703  C  CG  . GLN B 592  ? 0.7357 0.9025 0.8006 0.1014  -0.0402 -0.0862 592  GLN B CG  
5704  C  CD  . GLN B 592  ? 0.7900 0.9519 0.8455 0.1029  -0.0431 -0.0886 592  GLN B CD  
5705  O  OE1 . GLN B 592  ? 0.7408 0.8984 0.7948 0.0966  -0.0411 -0.0896 592  GLN B OE1 
5706  N  NE2 . GLN B 592  ? 0.8247 0.9865 0.8729 0.1116  -0.0477 -0.0895 592  GLN B NE2 
5707  N  N   . GLU B 593  ? 1.0270 1.1708 1.0975 0.0996  -0.0259 -0.0699 593  GLU B N   
5708  C  CA  . GLU B 593  ? 1.0050 1.1497 1.0785 0.1039  -0.0257 -0.0674 593  GLU B CA  
5709  C  C   . GLU B 593  ? 0.9422 1.0712 1.0094 0.1071  -0.0221 -0.0612 593  GLU B C   
5710  O  O   . GLU B 593  ? 0.8818 1.0090 0.9483 0.1124  -0.0226 -0.0592 593  GLU B O   
5711  C  CB  . GLU B 593  ? 0.9264 1.0800 1.0107 0.0985  -0.0235 -0.0680 593  GLU B CB  
5712  C  CG  . GLU B 593  ? 1.0407 1.1960 1.1286 0.1025  -0.0234 -0.0659 593  GLU B CG  
5713  C  CD  . GLU B 593  ? 1.1150 1.2849 1.2130 0.0996  -0.0241 -0.0692 593  GLU B CD  
5714  O  OE1 . GLU B 593  ? 1.0704 1.2426 1.1738 0.0926  -0.0210 -0.0694 593  GLU B OE1 
5715  O  OE2 . GLU B 593  ? 1.2275 1.4064 1.3278 0.1047  -0.0276 -0.0714 593  GLU B OE2 
5716  N  N   . LEU B 594  ? 0.9007 1.0184 0.9631 0.1041  -0.0185 -0.0584 594  LEU B N   
5717  C  CA  . LEU B 594  ? 0.8521 0.9555 0.9092 0.1066  -0.0147 -0.0526 594  LEU B CA  
5718  C  C   . LEU B 594  ? 0.8772 0.9745 0.9256 0.1149  -0.0170 -0.0515 594  LEU B C   
5719  O  O   . LEU B 594  ? 0.8935 0.9896 0.9347 0.1177  -0.0197 -0.0535 594  LEU B O   
5720  C  CB  . LEU B 594  ? 0.9177 1.0110 0.9704 0.1026  -0.0109 -0.0504 594  LEU B CB  
5721  C  CG  . LEU B 594  ? 0.8513 0.9304 0.8997 0.1042  -0.0063 -0.0445 594  LEU B CG  
5722  C  CD1 . LEU B 594  ? 0.8139 0.8938 0.8703 0.1011  -0.0030 -0.0418 594  LEU B CD1 
5723  C  CD2 . LEU B 594  ? 0.7909 0.8604 0.8328 0.1018  -0.0034 -0.0431 594  LEU B CD2 
5724  N  N   . PRO B 595  ? 0.6566 0.7497 0.7050 0.1190  -0.0160 -0.0484 595  PRO B N   
5725  C  CA  . PRO B 595  ? 0.6259 0.7115 0.6650 0.1269  -0.0176 -0.0469 595  PRO B CA  
5726  C  C   . PRO B 595  ? 0.6944 0.7658 0.7238 0.1281  -0.0147 -0.0436 595  PRO B C   
5727  O  O   . PRO B 595  ? 0.6992 0.7621 0.7292 0.1246  -0.0098 -0.0398 595  PRO B O   
5728  C  CB  . PRO B 595  ? 0.6087 0.6913 0.6510 0.1291  -0.0158 -0.0439 595  PRO B CB  
5729  C  CG  . PRO B 595  ? 0.6850 0.7787 0.7388 0.1237  -0.0157 -0.0456 595  PRO B CG  
5730  C  CD  . PRO B 595  ? 0.6993 0.7947 0.7559 0.1167  -0.0138 -0.0465 595  PRO B CD  
5731  N  N   . ARG B 596  ? 0.8885 0.9576 0.9085 0.1332  -0.0178 -0.0453 596  ARG B N   
5732  C  CA  . ARG B 596  ? 0.8910 0.9468 0.9006 0.1349  -0.0153 -0.0426 596  ARG B CA  
5733  C  C   . ARG B 596  ? 0.8552 0.8973 0.8600 0.1383  -0.0108 -0.0368 596  ARG B C   
5734  O  O   . ARG B 596  ? 0.8604 0.9022 0.8656 0.1424  -0.0116 -0.0359 596  ARG B O   
5735  C  CB  . ARG B 596  ? 0.8628 0.9194 0.8628 0.1405  -0.0201 -0.0459 596  ARG B CB  
5736  C  CG  . ARG B 596  ? 0.8172 0.8828 0.8191 0.1361  -0.0232 -0.0510 596  ARG B CG  
5737  C  CD  . ARG B 596  ? 0.8717 0.9550 0.8848 0.1332  -0.0272 -0.0560 596  ARG B CD  
5738  N  NE  . ARG B 596  ? 0.8132 0.9058 0.8277 0.1297  -0.0308 -0.0615 596  ARG B NE  
5739  C  CZ  . ARG B 596  ? 0.9127 1.0204 0.9377 0.1249  -0.0331 -0.0661 596  ARG B CZ  
5740  N  NH1 . ARG B 596  ? 0.8529 0.9682 0.8876 0.1232  -0.0323 -0.0657 596  ARG B NH1 
5741  N  NH2 . ARG B 596  ? 1.0404 1.1556 1.0660 0.1215  -0.0362 -0.0713 596  ARG B NH2 
5742  N  N   . PRO B 597  ? 0.8191 0.8494 0.8194 0.1365  -0.0060 -0.0330 597  PRO B N   
5743  C  CA  . PRO B 597  ? 0.7974 0.8148 0.7936 0.1393  -0.0013 -0.0277 597  PRO B CA  
5744  C  C   . PRO B 597  ? 0.9659 0.9756 0.9503 0.1477  -0.0029 -0.0269 597  PRO B C   
5745  O  O   . PRO B 597  ? 0.9852 0.9955 0.9615 0.1515  -0.0066 -0.0296 597  PRO B O   
5746  C  CB  . PRO B 597  ? 0.8478 0.8559 0.8414 0.1357  0.0039  -0.0245 597  PRO B CB  
5747  C  CG  . PRO B 597  ? 0.8063 0.8236 0.8056 0.1297  0.0024  -0.0280 597  PRO B CG  
5748  C  CD  . PRO B 597  ? 0.8161 0.8446 0.8154 0.1317  -0.0041 -0.0335 597  PRO B CD  
5749  N  N   . LEU B 598  ? 0.8905 0.8928 0.8738 0.1506  -0.0004 -0.0235 598  LEU B N   
5750  C  CA  . LEU B 598  ? 0.9477 0.9396 0.9190 0.1586  -0.0006 -0.0217 598  LEU B CA  
5751  C  C   . LEU B 598  ? 0.8392 0.8396 0.8076 0.1646  -0.0073 -0.0259 598  LEU B C   
5752  O  O   . LEU B 598  ? 0.8743 0.8675 0.8338 0.1718  -0.0080 -0.0247 598  LEU B O   
5753  C  CB  . LEU B 598  ? 0.7655 0.7453 0.7246 0.1611  0.0020  -0.0195 598  LEU B CB  
5754  C  CG  . LEU B 598  ? 0.8644 0.8316 0.8227 0.1583  0.0096  -0.0140 598  LEU B CG  
5755  C  CD1 . LEU B 598  ? 0.8055 0.7777 0.7729 0.1504  0.0119  -0.0141 598  LEU B CD1 
5756  C  CD2 . LEU B 598  ? 0.9183 0.8711 0.8616 0.1638  0.0121  -0.0113 598  LEU B CD2 
5757  N  N   . THR B 599  ? 0.6029 0.6185 0.5786 0.1618  -0.0120 -0.0309 599  THR B N   
5758  C  CA  . THR B 599  ? 0.5644 0.5903 0.5388 0.1671  -0.0187 -0.0356 599  THR B CA  
5759  C  C   . THR B 599  ? 0.5714 0.6119 0.5585 0.1641  -0.0212 -0.0385 599  THR B C   
5760  O  O   . THR B 599  ? 0.5863 0.6320 0.5724 0.1698  -0.0251 -0.0405 599  THR B O   
5761  C  CB  . THR B 599  ? 0.5993 0.6315 0.5698 0.1673  -0.0229 -0.0399 599  THR B CB  
5762  O  OG1 . THR B 599  ? 0.7729 0.7910 0.7313 0.1696  -0.0201 -0.0370 599  THR B OG1 
5763  C  CG2 . THR B 599  ? 0.5512 0.5926 0.5182 0.1743  -0.0298 -0.0444 599  THR B CG2 
5764  N  N   . LYS B 600  ? 0.8628 0.9095 0.8612 0.1559  -0.0190 -0.0387 600  LYS B N   
5765  C  CA  . LYS B 600  ? 0.8937 0.9531 0.9043 0.1524  -0.0205 -0.0410 600  LYS B CA  
5766  C  C   . LYS B 600  ? 0.8957 0.9712 0.9099 0.1539  -0.0267 -0.0470 600  LYS B C   
5767  O  O   . LYS B 600  ? 0.8400 0.9264 0.8626 0.1533  -0.0286 -0.0491 600  LYS B O   
5768  C  CB  . LYS B 600  ? 0.9117 0.9662 0.9230 0.1557  -0.0190 -0.0382 600  LYS B CB  
5769  C  CG  . LYS B 600  ? 0.8057 0.8471 0.8169 0.1527  -0.0127 -0.0328 600  LYS B CG  
5770  C  CD  . LYS B 600  ? 0.8133 0.8577 0.8329 0.1441  -0.0096 -0.0323 600  LYS B CD  
5771  C  CE  . LYS B 600  ? 0.8530 0.8835 0.8698 0.1421  -0.0036 -0.0271 600  LYS B CE  
5772  N  NZ  . LYS B 600  ? 0.9582 0.9909 0.9814 0.1347  -0.0007 -0.0266 600  LYS B NZ  
5773  N  N   . LEU B 601  ? 0.9332 1.0109 0.9414 0.1558  -0.0300 -0.0499 601  LEU B N   
5774  C  CA  . LEU B 601  ? 0.9547 1.0487 0.9673 0.1564  -0.0359 -0.0560 601  LEU B CA  
5775  C  C   . LEU B 601  ? 0.9216 1.0260 0.9450 0.1469  -0.0351 -0.0587 601  LEU B C   
5776  O  O   . LEU B 601  ? 0.9508 1.0480 0.9746 0.1411  -0.0309 -0.0563 601  LEU B O   
5777  C  CB  . LEU B 601  ? 0.9954 1.0878 0.9971 0.1621  -0.0400 -0.0584 601  LEU B CB  
5778  C  CG  . LEU B 601  ? 1.0004 1.0867 0.9909 0.1729  -0.0428 -0.0577 601  LEU B CG  
5779  C  CD1 . LEU B 601  ? 0.9809 1.0675 0.9614 0.1777  -0.0472 -0.0608 601  LEU B CD1 
5780  C  CD2 . LEU B 601  ? 1.1049 1.2024 1.1010 0.1771  -0.0463 -0.0600 601  LEU B CD2 
5781  N  N   . VAL B 602  ? 0.7971 0.9182 0.8292 0.1455  -0.0390 -0.0638 602  VAL B N   
5782  C  CA  . VAL B 602  ? 0.8981 1.0295 0.9400 0.1366  -0.0385 -0.0669 602  VAL B CA  
5783  C  C   . VAL B 602  ? 0.9349 1.0819 0.9797 0.1373  -0.0444 -0.0736 602  VAL B C   
5784  O  O   . VAL B 602  ? 0.9931 1.1464 1.0358 0.1446  -0.0490 -0.0760 602  VAL B O   
5785  C  CB  . VAL B 602  ? 0.8708 1.0077 0.9240 0.1315  -0.0355 -0.0658 602  VAL B CB  
5786  C  CG1 . VAL B 602  ? 0.8291 0.9517 0.8802 0.1309  -0.0300 -0.0595 602  VAL B CG1 
5787  C  CG2 . VAL B 602  ? 0.8773 1.0272 0.9364 0.1355  -0.0391 -0.0687 602  VAL B CG2 
5788  N  N   . TRP B 603  ? 0.8592 1.0122 0.9086 0.1298  -0.0443 -0.0768 603  TRP B N   
5789  C  CA  . TRP B 603  ? 0.8541 1.0236 0.9090 0.1281  -0.0492 -0.0837 603  TRP B CA  
5790  C  C   . TRP B 603  ? 0.9435 1.1145 0.9895 0.1357  -0.0551 -0.0869 603  TRP B C   
5791  O  O   . TRP B 603  ? 1.0048 1.1911 1.0555 0.1359  -0.0602 -0.0930 603  TRP B O   
5792  C  CB  . TRP B 603  ? 0.8375 1.0233 0.9042 0.1273  -0.0508 -0.0866 603  TRP B CB  
5793  C  CG  . TRP B 603  ? 0.8310 1.0190 0.9076 0.1188  -0.0459 -0.0852 603  TRP B CG  
5794  C  CD1 . TRP B 603  ? 0.8667 1.0477 0.9452 0.1184  -0.0415 -0.0803 603  TRP B CD1 
5795  C  CD2 . TRP B 603  ? 0.8328 1.0303 0.9180 0.1097  -0.0447 -0.0888 603  TRP B CD2 
5796  N  NE1 . TRP B 603  ? 0.9541 1.1397 1.0415 0.1100  -0.0380 -0.0806 603  TRP B NE1 
5797  C  CE2 . TRP B 603  ? 0.8963 1.0915 0.9877 0.1045  -0.0396 -0.0856 603  TRP B CE2 
5798  C  CE3 . TRP B 603  ? 0.7459 0.9532 0.8339 0.1053  -0.0475 -0.0946 603  TRP B CE3 
5799  C  CZ2 . TRP B 603  ? 0.8762 1.0780 0.9759 0.0955  -0.0369 -0.0876 603  TRP B CZ2 
5800  C  CZ3 . TRP B 603  ? 0.7564 0.9702 0.8531 0.0957  -0.0447 -0.0968 603  TRP B CZ3 
5801  C  CH2 . TRP B 603  ? 0.9072 1.1178 1.0093 0.0910  -0.0392 -0.0931 603  TRP B CH2 
5802  N  N   . ASP B 604  ? 0.9630 1.1187 0.9963 0.1420  -0.0545 -0.0830 604  ASP B N   
5803  C  CA  . ASP B 604  ? 0.9407 1.0969 0.9642 0.1506  -0.0601 -0.0856 604  ASP B CA  
5804  C  C   . ASP B 604  ? 1.0341 1.1720 1.0436 0.1531  -0.0580 -0.0819 604  ASP B C   
5805  O  O   . ASP B 604  ? 0.9694 1.0947 0.9773 0.1486  -0.0521 -0.0771 604  ASP B O   
5806  C  CB  . ASP B 604  ? 0.9709 1.1294 0.9923 0.1601  -0.0628 -0.0848 604  ASP B CB  
5807  C  CG  . ASP B 604  ? 1.1649 1.3446 1.1967 0.1608  -0.0679 -0.0909 604  ASP B CG  
5808  O  OD1 . ASP B 604  ? 1.0775 1.2698 1.1137 0.1576  -0.0718 -0.0968 604  ASP B OD1 
5809  O  OD2 . ASP B 604  ? 1.2107 1.3944 1.2464 0.1647  -0.0680 -0.0898 604  ASP B OD2 
5810  N  N   . ASN B 605  ? 1.0997 1.2368 1.0991 0.1606  -0.0629 -0.0843 605  ASN B N   
5811  C  CA  . ASN B 605  ? 0.8683 0.9884 0.8526 0.1648  -0.0616 -0.0811 605  ASN B CA  
5812  C  C   . ASN B 605  ? 0.9723 1.0879 0.9455 0.1768  -0.0651 -0.0802 605  ASN B C   
5813  O  O   . ASN B 605  ? 1.0589 1.1877 1.0348 0.1818  -0.0709 -0.0845 605  ASN B O   
5814  C  CB  . ASN B 605  ? 0.8721 0.9947 0.8532 0.1613  -0.0645 -0.0858 605  ASN B CB  
5815  C  CG  . ASN B 605  ? 1.0627 1.1671 1.0280 0.1653  -0.0626 -0.0824 605  ASN B CG  
5816  O  OD1 . ASN B 605  ? 1.0473 1.1362 1.0055 0.1685  -0.0576 -0.0759 605  ASN B OD1 
5817  N  ND2 . ASN B 605  ? 1.0542 1.1604 1.0137 0.1652  -0.0665 -0.0869 605  ASN B ND2 
5818  N  N   . ALA B 606  ? 1.0006 1.0972 0.9609 0.1816  -0.0613 -0.0746 606  ALA B N   
5819  C  CA  . ALA B 606  ? 0.9795 1.0688 0.9277 0.1931  -0.0635 -0.0728 606  ALA B CA  
5820  C  C   . ALA B 606  ? 0.9058 0.9766 0.8374 0.1975  -0.0613 -0.0692 606  ALA B C   
5821  O  O   . ALA B 606  ? 0.8816 0.9427 0.8117 0.1917  -0.0564 -0.0665 606  ALA B O   
5822  C  CB  . ALA B 606  ? 0.9541 1.0384 0.9050 0.1954  -0.0598 -0.0681 606  ALA B CB  
5823  N  N   . ALA B 607  ? 0.7853 0.8511 0.7039 0.2084  -0.0649 -0.0693 607  ALA B N   
5824  C  CA  . ALA B 607  ? 0.8102 0.8572 0.7112 0.2144  -0.0627 -0.0655 607  ALA B CA  
5825  C  C   . ALA B 607  ? 0.8238 0.8541 0.7197 0.2172  -0.0558 -0.0580 607  ALA B C   
5826  O  O   . ALA B 607  ? 0.8368 0.8660 0.7295 0.2243  -0.0571 -0.0569 607  ALA B O   
5827  C  CB  . ALA B 607  ? 0.8076 0.8569 0.6962 0.2251  -0.0699 -0.0694 607  ALA B CB  
5828  N  N   . LEU B 608  ? 0.8807 0.8980 0.7757 0.2115  -0.0486 -0.0530 608  LEU B N   
5829  C  CA  . LEU B 608  ? 0.8849 0.8873 0.7773 0.2122  -0.0414 -0.0461 608  LEU B CA  
5830  C  C   . LEU B 608  ? 0.8918 0.8756 0.7650 0.2215  -0.0394 -0.0421 608  LEU B C   
5831  O  O   . LEU B 608  ? 0.8549 0.8312 0.7181 0.2226  -0.0390 -0.0420 608  LEU B O   
5832  C  CB  . LEU B 608  ? 0.8620 0.8600 0.7630 0.2021  -0.0345 -0.0426 608  LEU B CB  
5833  C  CG  . LEU B 608  ? 0.7255 0.7401 0.6429 0.1924  -0.0362 -0.0468 608  LEU B CG  
5834  C  CD1 . LEU B 608  ? 0.6843 0.6924 0.6072 0.1836  -0.0294 -0.0432 608  LEU B CD1 
5835  C  CD2 . LEU B 608  ? 0.7846 0.8122 0.7142 0.1915  -0.0386 -0.0487 608  LEU B CD2 
5836  N  N   . MET B 609  ? 1.0109 0.9868 0.8785 0.2281  -0.0380 -0.0389 609  MET B N   
5837  C  CA  . MET B 609  ? 1.0502 1.0074 0.8990 0.2372  -0.0356 -0.0347 609  MET B CA  
5838  C  C   . MET B 609  ? 1.0225 0.9676 0.8705 0.2385  -0.0295 -0.0290 609  MET B C   
5839  O  O   . MET B 609  ? 0.9773 0.9309 0.8372 0.2355  -0.0299 -0.0296 609  MET B O   
5840  C  CB  . MET B 609  ? 1.0318 0.9929 0.8690 0.2482  -0.0433 -0.0388 609  MET B CB  
5841  C  CG  . MET B 609  ? 0.9885 0.9612 0.8315 0.2527  -0.0483 -0.0416 609  MET B CG  
5842  S  SD  . MET B 609  ? 1.0455 1.0284 0.8785 0.2644  -0.0588 -0.0479 609  MET B SD  
5843  C  CE  . MET B 609  ? 0.9613 0.9623 0.8046 0.2563  -0.0639 -0.0548 609  MET B CE  
5844  N  N   . SER B 610  ? 1.1765 1.1015 1.0101 0.2429  -0.0238 -0.0235 610  SER B N   
5845  C  CA  . SER B 610  ? 1.2028 1.1143 1.0338 0.2444  -0.0177 -0.0181 610  SER B CA  
5846  C  C   . SER B 610  ? 1.2658 1.1784 1.0908 0.2538  -0.0222 -0.0195 610  SER B C   
5847  O  O   . SER B 610  ? 1.3059 1.2254 1.1239 0.2612  -0.0294 -0.0237 610  SER B O   
5848  C  CB  . SER B 610  ? 1.1613 1.0510 0.9776 0.2470  -0.0103 -0.0121 610  SER B CB  
5849  O  OG  . SER B 610  ? 1.3886 1.2694 1.1859 0.2580  -0.0132 -0.0123 610  SER B OG  
5850  N  N   . PRO B 611  ? 1.2135 1.1196 1.0410 0.2537  -0.0184 -0.0162 611  PRO B N   
5851  C  CA  . PRO B 611  ? 1.2275 1.1330 1.0481 0.2632  -0.0223 -0.0173 611  PRO B CA  
5852  C  C   . PRO B 611  ? 1.1636 1.0550 0.9623 0.2752  -0.0234 -0.0158 611  PRO B C   
5853  O  O   . PRO B 611  ? 1.1393 1.0375 0.9320 0.2841  -0.0304 -0.0196 611  PRO B O   
5854  C  CB  . PRO B 611  ? 1.2076 1.1041 1.0333 0.2597  -0.0159 -0.0130 611  PRO B CB  
5855  C  CG  . PRO B 611  ? 1.1473 1.0505 0.9897 0.2471  -0.0121 -0.0124 611  PRO B CG  
5856  C  CD  . PRO B 611  ? 1.1573 1.0587 0.9958 0.2446  -0.0110 -0.0122 611  PRO B CD  
5857  N  N   . ARG B 612  ? 1.2150 1.0870 1.0014 0.2761  -0.0166 -0.0106 612  ARG B N   
5858  C  CA  . ARG B 612  ? 1.3079 1.1650 1.0721 0.2878  -0.0171 -0.0089 612  ARG B CA  
5859  C  C   . ARG B 612  ? 1.2375 1.1061 0.9968 0.2927  -0.0255 -0.0144 612  ARG B C   
5860  O  O   . ARG B 612  ? 1.2665 1.1329 1.0118 0.3041  -0.0306 -0.0161 612  ARG B O   
5861  C  CB  . ARG B 612  ? 1.4142 1.2493 1.1675 0.2865  -0.0077 -0.0023 612  ARG B CB  
5862  C  CG  . ARG B 612  ? 1.3701 1.1840 1.1006 0.2981  -0.0050 0.0017  612  ARG B CG  
5863  C  CD  . ARG B 612  ? 1.3841 1.1774 1.1046 0.2962  0.0047  0.0080  612  ARG B CD  
5864  N  NE  . ARG B 612  ? 1.4102 1.1972 1.1416 0.2870  0.0131  0.0123  612  ARG B NE  
5865  C  CZ  . ARG B 612  ? 1.4409 1.2149 1.1681 0.2891  0.0179  0.0160  612  ARG B CZ  
5866  N  NH1 . ARG B 612  ? 1.5454 1.3101 1.2569 0.3004  0.0156  0.0164  612  ARG B NH1 
5867  N  NH2 . ARG B 612  ? 1.4539 1.2240 1.1928 0.2798  0.0252  0.0193  612  ARG B NH2 
5868  N  N   . THR B 613  ? 1.0119 0.8926 0.7822 0.2843  -0.0270 -0.0174 613  THR B N   
5869  C  CA  . THR B 613  ? 1.0339 0.9262 0.8007 0.2877  -0.0349 -0.0231 613  THR B CA  
5870  C  C   . THR B 613  ? 1.0031 0.9149 0.7766 0.2921  -0.0443 -0.0295 613  THR B C   
5871  O  O   . THR B 613  ? 1.0489 0.9646 0.8119 0.3013  -0.0512 -0.0332 613  THR B O   
5872  C  CB  . THR B 613  ? 1.0728 0.9738 0.8513 0.2768  -0.0340 -0.0249 613  THR B CB  
5873  O  OG1 . THR B 613  ? 1.0307 0.9133 0.8003 0.2747  -0.0258 -0.0194 613  THR B OG1 
5874  C  CG2 . THR B 613  ? 1.0405 0.9557 0.8178 0.2791  -0.0427 -0.0318 613  THR B CG2 
5875  N  N   . ALA B 614  ? 1.1355 1.0599 0.9263 0.2858  -0.0446 -0.0309 614  ALA B N   
5876  C  CA  . ALA B 614  ? 1.1415 1.0850 0.9396 0.2897  -0.0530 -0.0368 614  ALA B CA  
5877  C  C   . ALA B 614  ? 1.2044 1.1392 0.9877 0.3029  -0.0551 -0.0356 614  ALA B C   
5878  O  O   . ALA B 614  ? 1.2428 1.1894 1.0232 0.3109  -0.0633 -0.0407 614  ALA B O   
5879  C  CB  . ALA B 614  ? 1.1491 1.1063 0.9683 0.2800  -0.0519 -0.0379 614  ALA B CB  
5880  N  N   . ILE B 615  ? 1.3233 1.2374 1.0970 0.3055  -0.0478 -0.0291 615  ILE B N   
5881  C  CA  . ILE B 615  ? 1.3711 1.2740 1.1290 0.3182  -0.0490 -0.0274 615  ILE B CA  
5882  C  C   . ILE B 615  ? 1.3225 1.2185 1.0606 0.3295  -0.0531 -0.0284 615  ILE B C   
5883  O  O   . ILE B 615  ? 1.3471 1.2483 1.0771 0.3405  -0.0600 -0.0316 615  ILE B O   
5884  C  CB  . ILE B 615  ? 1.3412 1.2217 1.0928 0.3174  -0.0394 -0.0200 615  ILE B CB  
5885  C  CG1 . ILE B 615  ? 1.2301 1.1183 1.0005 0.3079  -0.0365 -0.0196 615  ILE B CG1 
5886  C  CG2 . ILE B 615  ? 1.3792 1.2441 1.1107 0.3312  -0.0397 -0.0176 615  ILE B CG2 
5887  C  CD1 . ILE B 615  ? 1.2581 1.1682 1.0408 0.3092  -0.0443 -0.0256 615  ILE B CD1 
5888  N  N   . LYS B 616  ? 1.3435 1.2278 1.0733 0.3272  -0.0491 -0.0257 616  LYS B N   
5889  C  CA  . LYS B 616  ? 1.4378 1.3125 1.1468 0.3381  -0.0520 -0.0260 616  LYS B CA  
5890  C  C   . LYS B 616  ? 1.4295 1.3251 1.1420 0.3406  -0.0626 -0.0339 616  LYS B C   
5891  O  O   . LYS B 616  ? 1.5703 1.4646 1.2677 0.3527  -0.0685 -0.0362 616  LYS B O   
5892  C  CB  . LYS B 616  ? 1.4103 1.2661 1.1096 0.3345  -0.0440 -0.0207 616  LYS B CB  
5893  C  CG  . LYS B 616  ? 1.4829 1.3267 1.1594 0.3455  -0.0462 -0.0204 616  LYS B CG  
5894  C  CD  . LYS B 616  ? 1.5670 1.4083 1.2428 0.3391  -0.0437 -0.0202 616  LYS B CD  
5895  C  CE  . LYS B 616  ? 1.6458 1.4734 1.2976 0.3504  -0.0454 -0.0196 616  LYS B CE  
5896  N  NZ  . LYS B 616  ? 1.6864 1.5194 1.3392 0.3456  -0.0473 -0.0226 616  LYS B NZ  
5897  N  N   . LEU B 617  ? 1.2916 1.2064 1.0236 0.3295  -0.0650 -0.0383 617  LEU B N   
5898  C  CA  . LEU B 617  ? 1.2301 1.1637 0.9658 0.3301  -0.0741 -0.0459 617  LEU B CA  
5899  C  C   . LEU B 617  ? 1.2739 1.2308 1.0214 0.3329  -0.0828 -0.0524 617  LEU B C   
5900  O  O   . LEU B 617  ? 1.4351 1.4028 1.1772 0.3406  -0.0915 -0.0581 617  LEU B O   
5901  C  CB  . LEU B 617  ? 1.2389 1.1797 0.9879 0.3167  -0.0720 -0.0473 617  LEU B CB  
5902  C  CG  . LEU B 617  ? 1.3059 1.2279 1.0409 0.3162  -0.0665 -0.0432 617  LEU B CG  
5903  C  CD1 . LEU B 617  ? 1.2661 1.1956 1.0147 0.3031  -0.0644 -0.0447 617  LEU B CD1 
5904  C  CD2 . LEU B 617  ? 1.3987 1.3160 1.1139 0.3283  -0.0725 -0.0457 617  LEU B CD2 
5905  N  N   . LEU B 618  ? 1.2291 1.1943 0.9924 0.3269  -0.0808 -0.0521 618  LEU B N   
5906  C  CA  . LEU B 618  ? 1.2288 1.2165 1.0043 0.3290  -0.0884 -0.0581 618  LEU B CA  
5907  C  C   . LEU B 618  ? 1.2908 1.2727 1.0554 0.3419  -0.0903 -0.0568 618  LEU B C   
5908  O  O   . LEU B 618  ? 1.2192 1.2192 0.9925 0.3452  -0.0965 -0.0616 618  LEU B O   
5909  C  CB  . LEU B 618  ? 1.2656 1.2668 1.0643 0.3159  -0.0857 -0.0589 618  LEU B CB  
5910  C  CG  . LEU B 618  ? 1.2334 1.2522 1.0479 0.3045  -0.0881 -0.0640 618  LEU B CG  
5911  C  CD1 . LEU B 618  ? 1.2843 1.2890 1.0959 0.2964  -0.0813 -0.0599 618  LEU B CD1 
5912  C  CD2 . LEU B 618  ? 1.2008 1.2379 1.0372 0.2955  -0.0884 -0.0666 618  LEU B CD2 
5913  N  N   . GLY B 619  ? 0.9980 0.9551 0.7437 0.3492  -0.0848 -0.0503 619  GLY B N   
5914  C  CA  . GLY B 619  ? 0.9971 0.9458 0.7306 0.3617  -0.0858 -0.0485 619  GLY B CA  
5915  C  C   . GLY B 619  ? 1.0230 0.9770 0.7695 0.3582  -0.0836 -0.0477 619  GLY B C   
5916  O  O   . GLY B 619  ? 1.0122 0.9757 0.7587 0.3666  -0.0891 -0.0507 619  GLY B O   
5917  N  N   . LEU B 620  ? 1.4711 1.4193 1.2286 0.3464  -0.0758 -0.0437 620  LEU B N   
5918  C  CA  . LEU B 620  ? 1.4107 1.3630 1.1810 0.3418  -0.0731 -0.0427 620  LEU B CA  
5919  C  C   . LEU B 620  ? 1.4274 1.3556 1.1828 0.3486  -0.0670 -0.0363 620  LEU B C   
5920  O  O   . LEU B 620  ? 1.4298 1.3360 1.1710 0.3498  -0.0607 -0.0308 620  LEU B O   
5921  C  CB  . LEU B 620  ? 1.3279 1.2856 1.1169 0.3259  -0.0679 -0.0417 620  LEU B CB  
5922  C  CG  . LEU B 620  ? 1.3297 1.3097 1.1340 0.3177  -0.0729 -0.0477 620  LEU B CG  
5923  C  CD1 . LEU B 620  ? 1.3162 1.2974 1.1359 0.3028  -0.0667 -0.0456 620  LEU B CD1 
5924  C  CD2 . LEU B 620  ? 1.3668 1.3716 1.1827 0.3204  -0.0812 -0.0546 620  LEU B CD2 
5925  N  N   . PRO B 621  ? 1.3212 1.2524 1.0792 0.3530  -0.0682 -0.0368 621  PRO B N   
5926  C  CA  . PRO B 621  ? 1.2944 1.2020 1.0367 0.3605  -0.0629 -0.0311 621  PRO B CA  
5927  C  C   . PRO B 621  ? 1.3262 1.2201 1.0749 0.3499  -0.0532 -0.0256 621  PRO B C   
5928  O  O   . PRO B 621  ? 1.3874 1.2819 1.1437 0.3477  -0.0514 -0.0250 621  PRO B O   
5929  C  CB  . PRO B 621  ? 1.3977 1.3176 1.1417 0.3695  -0.0693 -0.0350 621  PRO B CB  
5930  C  CG  . PRO B 621  ? 1.3424 1.2903 1.1105 0.3602  -0.0738 -0.0409 621  PRO B CG  
5931  C  CD  . PRO B 621  ? 1.2837 1.2400 1.0590 0.3514  -0.0745 -0.0427 621  PRO B CD  
5932  N  N   . PHE B 622  ? 1.3569 1.2380 1.1024 0.3433  -0.0469 -0.0216 622  PHE B N   
5933  C  CA  . PHE B 622  ? 1.3628 1.2293 1.1128 0.3338  -0.0374 -0.0161 622  PHE B CA  
5934  C  C   . PHE B 622  ? 1.3174 1.1596 1.0500 0.3358  -0.0305 -0.0103 622  PHE B C   
5935  O  O   . PHE B 622  ? 1.3468 1.1878 1.0695 0.3402  -0.0329 -0.0110 622  PHE B O   
5936  C  CB  . PHE B 622  ? 1.3306 1.2127 1.1032 0.3189  -0.0361 -0.0179 622  PHE B CB  
5937  C  CG  . PHE B 622  ? 1.3002 1.2046 1.0907 0.3154  -0.0414 -0.0229 622  PHE B CG  
5938  C  CD1 . PHE B 622  ? 1.2029 1.1298 1.0005 0.3176  -0.0501 -0.0294 622  PHE B CD1 
5939  C  CD2 . PHE B 622  ? 1.3401 1.2431 1.1404 0.3099  -0.0377 -0.0213 622  PHE B CD2 
5940  C  CE1 . PHE B 622  ? 1.1683 1.1157 0.9824 0.3144  -0.0544 -0.0339 622  PHE B CE1 
5941  C  CE2 . PHE B 622  ? 1.2517 1.1747 1.0678 0.3070  -0.0422 -0.0259 622  PHE B CE2 
5942  C  CZ  . PHE B 622  ? 1.1409 1.0861 0.9639 0.3093  -0.0504 -0.0320 622  PHE B CZ  
5943  N  N   . ASN B 623  ? 1.6224 1.4451 1.3513 0.3326  -0.0218 -0.0046 623  ASN B N   
5944  C  CA  . ASN B 623  ? 1.7439 1.5421 1.4559 0.3346  -0.0141 0.0014  623  ASN B CA  
5945  C  C   . ASN B 623  ? 1.6848 1.4842 1.4054 0.3235  -0.0095 0.0029  623  ASN B C   
5946  O  O   . ASN B 623  ? 1.7211 1.5074 1.4281 0.3264  -0.0063 0.0058  623  ASN B O   
5947  C  CB  . ASN B 623  ? 1.7390 1.5157 1.4439 0.3350  -0.0062 0.0068  623  ASN B CB  
5948  C  CG  . ASN B 623  ? 1.8292 1.5790 1.5100 0.3430  -0.0002 0.0123  623  ASN B CG  
5949  O  OD1 . ASN B 623  ? 1.7761 1.5202 1.4498 0.3428  0.0020  0.0140  623  ASN B OD1 
5950  N  ND2 . ASN B 623  ? 2.0004 1.7328 1.6681 0.3503  0.0028  0.0152  623  ASN B ND2 
5951  N  N   . ALA B 624  ? 1.1799 0.9939 0.9220 0.3112  -0.0089 0.0012  624  ALA B N   
5952  C  CA  . ALA B 624  ? 1.1572 0.9738 0.9095 0.3000  -0.0046 0.0025  624  ALA B CA  
5953  C  C   . ALA B 624  ? 1.1621 0.9560 0.9074 0.2964  0.0061  0.0093  624  ALA B C   
5954  O  O   . ALA B 624  ? 1.0283 0.8231 0.7835 0.2864  0.0110  0.0110  624  ALA B O   
5955  C  CB  . ALA B 624  ? 1.0813 0.9062 0.8293 0.3025  -0.0096 -0.0005 624  ALA B CB  
5956  N  N   . ASP B 625  ? 1.3305 1.1039 1.0587 0.3044  0.0101  0.0133  625  ASP B N   
5957  C  CA  . ASP B 625  ? 1.3286 1.0799 1.0504 0.3008  0.0207  0.0197  625  ASP B CA  
5958  C  C   . ASP B 625  ? 1.2637 1.0123 0.9965 0.2943  0.0249  0.0211  625  ASP B C   
5959  O  O   . ASP B 625  ? 1.2141 0.9486 0.9476 0.2880  0.0339  0.0258  625  ASP B O   
5960  C  CB  . ASP B 625  ? 1.4414 1.1697 1.1375 0.3128  0.0237  0.0236  625  ASP B CB  
5961  C  CG  . ASP B 625  ? 1.5317 1.2551 1.2157 0.3165  0.0240  0.0246  625  ASP B CG  
5962  O  OD1 . ASP B 625  ? 1.5172 1.2523 1.2130 0.3085  0.0236  0.0231  625  ASP B OD1 
5963  O  OD2 . ASP B 625  ? 1.5804 1.2876 1.2425 0.3276  0.0247  0.0268  625  ASP B OD2 
5964  N  N   . ARG B 626  ? 1.5154 1.2773 1.2568 0.2955  0.0187  0.0171  626  ARG B N   
5965  C  CA  . ARG B 626  ? 1.6093 1.3703 1.3620 0.2891  0.0220  0.0178  626  ARG B CA  
5966  C  C   . ARG B 626  ? 1.5143 1.2883 1.2889 0.2751  0.0241  0.0170  626  ARG B C   
5967  O  O   . ARG B 626  ? 1.4172 1.1879 1.2010 0.2682  0.0285  0.0184  626  ARG B O   
5968  C  CB  . ARG B 626  ? 1.5965 1.3683 1.3513 0.2952  0.0145  0.0135  626  ARG B CB  
5969  C  CG  . ARG B 626  ? 1.6417 1.3984 1.3749 0.3091  0.0132  0.0147  626  ARG B CG  
5970  C  CD  . ARG B 626  ? 1.5366 1.3021 1.2733 0.3139  0.0075  0.0112  626  ARG B CD  
5971  N  NE  . ARG B 626  ? 1.6402 1.4047 1.3898 0.3051  0.0116  0.0119  626  ARG B NE  
5972  C  CZ  . ARG B 626  ? 1.7140 1.4856 1.4692 0.3069  0.0079  0.0091  626  ARG B CZ  
5973  N  NH1 . ARG B 626  ? 1.6594 1.4404 1.4093 0.3173  0.0001  0.0054  626  ARG B NH1 
5974  N  NH2 . ARG B 626  ? 1.7225 1.4921 1.4890 0.2983  0.0119  0.0099  626  ARG B NH2 
5975  N  N   . LEU B 627  ? 1.4208 1.2092 1.2034 0.2711  0.0210  0.0147  627  LEU B N   
5976  C  CA  . LEU B 627  ? 1.3517 1.1507 1.1532 0.2584  0.0237  0.0145  627  LEU B CA  
5977  C  C   . LEU B 627  ? 1.4170 1.1993 1.2163 0.2526  0.0337  0.0200  627  LEU B C   
5978  O  O   . LEU B 627  ? 1.3859 1.1739 1.2005 0.2421  0.0372  0.0206  627  LEU B O   
5979  C  CB  . LEU B 627  ? 1.2737 1.0912 1.0827 0.2562  0.0179  0.0105  627  LEU B CB  
5980  C  CG  . LEU B 627  ? 1.2921 1.1294 1.1067 0.2601  0.0080  0.0044  627  LEU B CG  
5981  C  CD1 . LEU B 627  ? 1.2617 1.1162 1.0852 0.2558  0.0036  0.0007  627  LEU B CD1 
5982  C  CD2 . LEU B 627  ? 1.2724 1.1191 1.1010 0.2558  0.0066  0.0025  627  LEU B CD2 
5983  N  N   . ILE B 628  ? 1.3957 1.1579 1.1761 0.2593  0.0384  0.0241  628  ILE B N   
5984  C  CA  . ILE B 628  ? 1.3105 1.0555 1.0875 0.2545  0.0486  0.0296  628  ILE B CA  
5985  C  C   . ILE B 628  ? 1.3863 1.1183 1.1635 0.2524  0.0541  0.0322  628  ILE B C   
5986  O  O   . ILE B 628  ? 1.4029 1.1278 1.1702 0.2600  0.0519  0.0318  628  ILE B O   
5987  C  CB  . ILE B 628  ? 1.2416 0.9700 0.9975 0.2627  0.0516  0.0330  628  ILE B CB  
5988  C  CG1 . ILE B 628  ? 1.3150 1.0565 1.0702 0.2651  0.0455  0.0298  628  ILE B CG1 
5989  C  CG2 . ILE B 628  ? 1.2059 0.9171 0.9588 0.2574  0.0627  0.0387  628  ILE B CG2 
5990  C  CD1 . ILE B 628  ? 1.4676 1.1945 1.2006 0.2750  0.0465  0.0320  628  ILE B CD1 
5991  N  N   . GLY B 629  ? 1.1512 0.8801 0.9397 0.2422  0.0612  0.0348  629  GLY B N   
5992  C  CA  . GLY B 629  ? 1.1797 0.8961 0.9693 0.2390  0.0668  0.0371  629  GLY B CA  
5993  C  C   . GLY B 629  ? 1.1403 0.8581 0.9456 0.2267  0.0736  0.0390  629  GLY B C   
5994  O  O   . GLY B 629  ? 1.0684 0.7960 0.8828 0.2212  0.0743  0.0388  629  GLY B O   
5995  N  N   . THR B 630  ? 1.6003 1.3082 1.4085 0.2227  0.0786  0.0406  630  THR B N   
5996  C  CA  . THR B 630  ? 1.7295 1.4376 1.5525 0.2112  0.0853  0.0422  630  THR B CA  
5997  C  C   . THR B 630  ? 1.6955 1.4202 1.5375 0.2044  0.0806  0.0381  630  THR B C   
5998  O  O   . THR B 630  ? 1.6581 1.3960 1.5029 0.2081  0.0722  0.0340  630  THR B O   
5999  C  CB  . THR B 630  ? 1.8062 1.4905 1.6190 0.2107  0.0950  0.0469  630  THR B CB  
6000  O  OG1 . THR B 630  ? 1.8267 1.5123 1.6546 0.1992  0.1016  0.0484  630  THR B OG1 
6001  C  CG2 . THR B 630  ? 1.7110 1.3861 1.5170 0.2149  0.0934  0.0460  630  THR B CG2 
6002  N  N   . GLU B 631  ? 1.6463 1.3705 1.5014 0.1945  0.0860  0.0392  631  GLU B N   
6003  C  CA  . GLU B 631  ? 1.6226 1.3613 1.4954 0.1878  0.0822  0.0355  631  GLU B CA  
6004  C  C   . GLU B 631  ? 1.7114 1.4438 1.5790 0.1918  0.0795  0.0338  631  GLU B C   
6005  O  O   . GLU B 631  ? 1.7143 1.4606 1.5931 0.1896  0.0736  0.0299  631  GLU B O   
6006  C  CB  . GLU B 631  ? 1.6280 1.3669 1.5154 0.1766  0.0889  0.0370  631  GLU B CB  
6007  C  CG  . GLU B 631  ? 1.7895 1.5436 1.6957 0.1690  0.0852  0.0333  631  GLU B CG  
6008  C  CD  . GLU B 631  ? 1.9679 1.7423 1.8895 0.1637  0.0819  0.0313  631  GLU B CD  
6009  O  OE1 . GLU B 631  ? 1.9211 1.6967 1.8394 0.1647  0.0834  0.0331  631  GLU B OE1 
6010  O  OE2 . GLU B 631  ? 2.1441 1.9326 2.0802 0.1586  0.0778  0.0280  631  GLU B OE2 
6011  N  N   . ALA B 632  ? 1.4453 1.1567 1.2954 0.1980  0.0837  0.0367  632  ALA B N   
6012  C  CA  . ALA B 632  ? 1.3894 1.0924 1.2336 0.2018  0.0820  0.0355  632  ALA B CA  
6013  C  C   . ALA B 632  ? 1.3796 1.0944 1.2204 0.2102  0.0723  0.0315  632  ALA B C   
6014  O  O   . ALA B 632  ? 1.3876 1.1046 1.2311 0.2111  0.0688  0.0288  632  ALA B O   
6015  C  CB  . ALA B 632  ? 1.4477 1.1241 1.2724 0.2070  0.0892  0.0398  632  ALA B CB  
6016  N  N   . ASP B 633  ? 1.8116 1.5343 1.6467 0.2164  0.0678  0.0308  633  ASP B N   
6017  C  CA  . ASP B 633  ? 1.7858 1.5202 1.6174 0.2248  0.0587  0.0270  633  ASP B CA  
6018  C  C   . ASP B 633  ? 1.7344 1.4926 1.5794 0.2217  0.0524  0.0235  633  ASP B C   
6019  O  O   . ASP B 633  ? 1.7224 1.4895 1.5621 0.2290  0.0460  0.0212  633  ASP B O   
6020  C  CB  . ASP B 633  ? 1.9134 1.6337 1.7226 0.2372  0.0582  0.0288  633  ASP B CB  
6021  C  CG  . ASP B 633  ? 1.9441 1.6624 1.7463 0.2390  0.0602  0.0312  633  ASP B CG  
6022  O  OD1 . ASP B 633  ? 1.9187 1.6391 1.7304 0.2303  0.0650  0.0329  633  ASP B OD1 
6023  O  OD2 . ASP B 633  ? 2.0161 1.7310 1.8031 0.2493  0.0567  0.0311  633  ASP B OD2 
6024  N  N   . ASP B 634  ? 1.6053 1.3741 1.4678 0.2110  0.0543  0.0231  634  ASP B N   
6025  C  CA  . ASP B 634  ? 1.5418 1.3316 1.4166 0.2075  0.0492  0.0202  634  ASP B CA  
6026  C  C   . ASP B 634  ? 1.4786 1.2855 1.3598 0.2103  0.0405  0.0151  634  ASP B C   
6027  O  O   . ASP B 634  ? 1.3939 1.2141 1.2756 0.2136  0.0347  0.0125  634  ASP B O   
6028  C  CB  . ASP B 634  ? 1.5439 1.3402 1.4356 0.1958  0.0533  0.0209  634  ASP B CB  
6029  C  CG  . ASP B 634  ? 1.6200 1.4369 1.5242 0.1918  0.0486  0.0180  634  ASP B CG  
6030  O  OD1 . ASP B 634  ? 1.5951 1.4172 1.4927 0.1973  0.0446  0.0169  634  ASP B OD1 
6031  O  OD2 . ASP B 634  ? 1.5026 1.3302 1.4229 0.1834  0.0488  0.0168  634  ASP B OD2 
6032  N  N   . ARG B 635  ? 1.3980 1.2050 1.2842 0.2089  0.0396  0.0136  635  ARG B N   
6033  C  CA  . ARG B 635  ? 1.3716 1.1949 1.2643 0.2114  0.0318  0.0089  635  ARG B CA  
6034  C  C   . ARG B 635  ? 1.3654 1.1878 1.2439 0.2233  0.0267  0.0075  635  ARG B C   
6035  O  O   . ARG B 635  ? 1.2634 1.1031 1.1467 0.2261  0.0198  0.0035  635  ARG B O   
6036  C  CB  . ARG B 635  ? 1.3838 1.2051 1.2832 0.2080  0.0325  0.0078  635  ARG B CB  
6037  C  CG  . ARG B 635  ? 1.2853 1.1086 1.1994 0.1964  0.0370  0.0086  635  ARG B CG  
6038  C  CD  . ARG B 635  ? 1.1614 1.0060 1.0914 0.1903  0.0332  0.0059  635  ARG B CD  
6039  N  NE  . ARG B 635  ? 1.1793 1.0394 1.1147 0.1930  0.0260  0.0015  635  ARG B NE  
6040  C  CZ  . ARG B 635  ? 1.1430 1.0091 1.0880 0.1893  0.0244  -0.0008 635  ARG B CZ  
6041  N  NH1 . ARG B 635  ? 1.1090 0.9675 1.0597 0.1826  0.0289  0.0006  635  ARG B NH1 
6042  N  NH2 . ARG B 635  ? 1.0851 0.9652 1.0341 0.1925  0.0181  -0.0047 635  ARG B NH2 
6043  N  N   . GLU B 636  ? 1.3210 1.1238 1.1820 0.2306  0.0300  0.0106  636  GLU B N   
6044  C  CA  . GLU B 636  ? 1.3633 1.1644 1.2095 0.2427  0.0252  0.0094  636  GLU B CA  
6045  C  C   . GLU B 636  ? 1.3533 1.1639 1.1973 0.2453  0.0219  0.0085  636  GLU B C   
6046  O  O   . GLU B 636  ? 1.3377 1.1599 1.1790 0.2524  0.0148  0.0051  636  GLU B O   
6047  C  CB  . GLU B 636  ? 1.4399 1.2157 1.2667 0.2498  0.0303  0.0134  636  GLU B CB  
6048  C  CG  . GLU B 636  ? 1.5342 1.3053 1.3429 0.2632  0.0262  0.0130  636  GLU B CG  
6049  C  CD  . GLU B 636  ? 1.6265 1.3706 1.4149 0.2698  0.0323  0.0176  636  GLU B CD  
6050  O  OE1 . GLU B 636  ? 1.6492 1.3787 1.4383 0.2638  0.0395  0.0207  636  GLU B OE1 
6051  O  OE2 . GLU B 636  ? 1.6100 1.3476 1.3817 0.2810  0.0298  0.0181  636  GLU B OE2 
6052  N  N   . ARG B 637  ? 1.3268 1.1332 1.1723 0.2396  0.0268  0.0113  637  ARG B N   
6053  C  CA  . ARG B 637  ? 1.2686 1.0838 1.1126 0.2411  0.0239  0.0104  637  ARG B CA  
6054  C  C   . ARG B 637  ? 1.1435 0.9834 1.0045 0.2359  0.0177  0.0056  637  ARG B C   
6055  O  O   . ARG B 637  ? 1.0927 0.9441 0.9520 0.2401  0.0119  0.0026  637  ARG B O   
6056  C  CB  . ARG B 637  ? 1.2405 1.0447 1.0823 0.2359  0.0313  0.0147  637  ARG B CB  
6057  C  CG  . ARG B 637  ? 1.2253 1.0046 1.0490 0.2412  0.0380  0.0196  637  ARG B CG  
6058  C  CD  . ARG B 637  ? 1.2207 0.9910 1.0423 0.2366  0.0450  0.0236  637  ARG B CD  
6059  N  NE  . ARG B 637  ? 1.3093 1.0816 1.1466 0.2249  0.0504  0.0250  637  ARG B NE  
6060  C  CZ  . ARG B 637  ? 1.3210 1.1074 1.1728 0.2169  0.0500  0.0238  637  ARG B CZ  
6061  N  NH1 . ARG B 637  ? 1.2970 1.0965 1.1501 0.2186  0.0447  0.0212  637  ARG B NH1 
6062  N  NH2 . ARG B 637  ? 1.2831 1.0704 1.1484 0.2071  0.0550  0.0251  637  ARG B NH2 
6063  N  N   . GLN B 638  ? 1.0776 0.9257 0.9548 0.2268  0.0188  0.0047  638  GLN B N   
6064  C  CA  . GLN B 638  ? 1.1198 0.9904 1.0127 0.2219  0.0133  0.0003  638  GLN B CA  
6065  C  C   . GLN B 638  ? 1.1371 1.0192 1.0293 0.2289  0.0059  -0.0040 638  GLN B C   
6066  O  O   . GLN B 638  ? 1.0985 0.9984 0.9976 0.2287  0.0002  -0.0080 638  GLN B O   
6067  C  CB  . GLN B 638  ? 1.1376 1.0130 1.0466 0.2113  0.0164  0.0005  638  GLN B CB  
6068  C  CG  . GLN B 638  ? 1.1209 0.9893 1.0338 0.2035  0.0232  0.0042  638  GLN B CG  
6069  C  CD  . GLN B 638  ? 1.0033 0.8774 0.9323 0.1937  0.0255  0.0040  638  GLN B CD  
6070  O  OE1 . GLN B 638  ? 1.0097 0.8926 0.9466 0.1926  0.0221  0.0012  638  GLN B OE1 
6071  N  NE2 . GLN B 638  ? 1.0274 0.8966 0.9612 0.1868  0.0314  0.0069  638  GLN B NE2 
6072  N  N   . GLN B 639  ? 1.0739 0.9461 0.9580 0.2350  0.0060  -0.0035 639  GLN B N   
6073  C  CA  . GLN B 639  ? 1.0826 0.9647 0.9646 0.2430  -0.0009 -0.0075 639  GLN B CA  
6074  C  C   . GLN B 639  ? 1.1205 1.0046 0.9905 0.2524  -0.0053 -0.0088 639  GLN B C   
6075  O  O   . GLN B 639  ? 1.0773 0.9784 0.9512 0.2560  -0.0122 -0.0132 639  GLN B O   
6076  C  CB  . GLN B 639  ? 1.1312 0.9998 1.0055 0.2478  0.0008  -0.0063 639  GLN B CB  
6077  C  CG  . GLN B 639  ? 1.2087 1.0784 1.0956 0.2394  0.0035  -0.0063 639  GLN B CG  
6078  C  CD  . GLN B 639  ? 1.2910 1.1449 1.1689 0.2441  0.0057  -0.0049 639  GLN B CD  
6079  O  OE1 . GLN B 639  ? 1.1985 1.0422 1.0609 0.2544  0.0046  -0.0043 639  GLN B OE1 
6080  N  NE2 . GLN B 639  ? 1.3324 1.1838 1.2194 0.2367  0.0088  -0.0046 639  GLN B NE2 
6081  N  N   . TYR B 640  ? 1.3130 1.1800 1.1682 0.2565  -0.0015 -0.0050 640  TYR B N   
6082  C  CA  . TYR B 640  ? 1.2860 1.1541 1.1288 0.2656  -0.0058 -0.0062 640  TYR B CA  
6083  C  C   . TYR B 640  ? 1.1891 1.0745 1.0416 0.2606  -0.0093 -0.0091 640  TYR B C   
6084  O  O   . TYR B 640  ? 1.2375 1.1346 1.0874 0.2665  -0.0158 -0.0128 640  TYR B O   
6085  C  CB  . TYR B 640  ? 1.3133 1.1578 1.1374 0.2708  -0.0002 -0.0011 640  TYR B CB  
6086  C  CG  . TYR B 640  ? 1.3317 1.1740 1.1395 0.2828  -0.0048 -0.0022 640  TYR B CG  
6087  C  CD1 . TYR B 640  ? 1.4265 1.2642 1.2225 0.2941  -0.0084 -0.0032 640  TYR B CD1 
6088  C  CD2 . TYR B 640  ? 1.3137 1.1584 1.1175 0.2831  -0.0058 -0.0023 640  TYR B CD2 
6089  C  CE1 . TYR B 640  ? 1.5149 1.3511 1.2957 0.3057  -0.0129 -0.0043 640  TYR B CE1 
6090  C  CE2 . TYR B 640  ? 1.3583 1.2013 1.1469 0.2942  -0.0104 -0.0036 640  TYR B CE2 
6091  C  CZ  . TYR B 640  ? 1.4551 1.2941 1.2324 0.3056  -0.0141 -0.0046 640  TYR B CZ  
6092  O  OH  . TYR B 640  ? 1.4677 1.3054 1.2297 0.3172  -0.0190 -0.0060 640  TYR B OH  
6093  N  N   . LEU B 641  ? 1.0255 0.9128 0.8892 0.2497  -0.0050 -0.0076 641  LEU B N   
6094  C  CA  . LEU B 641  ? 1.0621 0.9656 0.9357 0.2442  -0.0080 -0.0104 641  LEU B CA  
6095  C  C   . LEU B 641  ? 0.9110 0.8369 0.7985 0.2424  -0.0146 -0.0159 641  LEU B C   
6096  O  O   . LEU B 641  ? 0.8303 0.7709 0.7214 0.2426  -0.0197 -0.0198 641  LEU B O   
6097  C  CB  . LEU B 641  ? 1.0607 0.9606 0.9431 0.2334  -0.0016 -0.0074 641  LEU B CB  
6098  C  CG  . LEU B 641  ? 1.0039 0.9174 0.8951 0.2274  -0.0036 -0.0097 641  LEU B CG  
6099  C  CD1 . LEU B 641  ? 0.9840 0.8955 0.8622 0.2343  -0.0066 -0.0106 641  LEU B CD1 
6100  C  CD2 . LEU B 641  ? 1.0185 0.9271 0.9176 0.2175  0.0031  -0.0064 641  LEU B CD2 
6101  N  N   . GLU B 642  ? 1.1039 1.0327 0.9992 0.2404  -0.0143 -0.0165 642  GLU B N   
6102  C  CA  . GLU B 642  ? 1.0697 1.0190 0.9769 0.2396  -0.0203 -0.0216 642  GLU B CA  
6103  C  C   . GLU B 642  ? 1.1071 1.0632 1.0059 0.2506  -0.0270 -0.0251 642  GLU B C   
6104  O  O   . GLU B 642  ? 1.0120 0.9871 0.9185 0.2504  -0.0327 -0.0298 642  GLU B O   
6105  C  CB  . GLU B 642  ? 1.0113 0.9600 0.9264 0.2364  -0.0184 -0.0212 642  GLU B CB  
6106  C  CG  . GLU B 642  ? 1.1420 1.1110 1.0690 0.2359  -0.0239 -0.0262 642  GLU B CG  
6107  C  CD  . GLU B 642  ? 1.2307 1.1981 1.1646 0.2329  -0.0220 -0.0258 642  GLU B CD  
6108  O  OE1 . GLU B 642  ? 1.2912 1.2429 1.2224 0.2297  -0.0163 -0.0219 642  GLU B OE1 
6109  O  OE2 . GLU B 642  ? 1.1805 1.1626 1.1226 0.2335  -0.0261 -0.0296 642  GLU B OE2 
6110  N  N   . GLN B 643  ? 1.1663 1.1072 1.0492 0.2603  -0.0264 -0.0229 643  GLN B N   
6111  C  CA  . GLN B 643  ? 1.1499 1.0962 1.0233 0.2719  -0.0329 -0.0261 643  GLN B CA  
6112  C  C   . GLN B 643  ? 1.2002 1.1520 1.0688 0.2742  -0.0363 -0.0278 643  GLN B C   
6113  O  O   . GLN B 643  ? 1.1897 1.1566 1.0589 0.2797  -0.0432 -0.0326 643  GLN B O   
6114  C  CB  . GLN B 643  ? 1.2697 1.1959 1.1256 0.2819  -0.0307 -0.0228 643  GLN B CB  
6115  C  CG  . GLN B 643  ? 1.3569 1.2765 1.2159 0.2807  -0.0278 -0.0214 643  GLN B CG  
6116  C  CD  . GLN B 643  ? 1.3789 1.3191 1.2513 0.2801  -0.0331 -0.0264 643  GLN B CD  
6117  O  OE1 . GLN B 643  ? 1.4014 1.3492 1.2884 0.2709  -0.0314 -0.0270 643  GLN B OE1 
6118  N  NE2 . GLN B 643  ? 1.3496 1.2992 1.2170 0.2902  -0.0395 -0.0300 643  GLN B NE2 
6119  N  N   . LEU B 644  ? 1.1295 1.0696 0.9934 0.2700  -0.0314 -0.0243 644  LEU B N   
6120  C  CA  . LEU B 644  ? 1.0734 1.0171 0.9316 0.2721  -0.0343 -0.0258 644  LEU B CA  
6121  C  C   . LEU B 644  ? 0.9720 0.9373 0.8465 0.2638  -0.0381 -0.0304 644  LEU B C   
6122  O  O   . LEU B 644  ? 0.8412 0.8167 0.7137 0.2668  -0.0434 -0.0342 644  LEU B O   
6123  C  CB  . LEU B 644  ? 0.9966 0.9203 0.8442 0.2703  -0.0275 -0.0204 644  LEU B CB  
6124  C  CG  . LEU B 644  ? 0.9522 0.8754 0.7912 0.2728  -0.0295 -0.0212 644  LEU B CG  
6125  C  CD1 . LEU B 644  ? 0.9171 0.8442 0.7440 0.2852  -0.0367 -0.0246 644  LEU B CD1 
6126  C  CD2 . LEU B 644  ? 0.9485 0.8496 0.7758 0.2721  -0.0217 -0.0152 644  LEU B CD2 
6127  N  N   . SER B 645  ? 1.1999 1.1724 1.0903 0.2535  -0.0354 -0.0304 645  SER B N   
6128  C  CA  . SER B 645  ? 1.1073 1.0993 1.0130 0.2452  -0.0382 -0.0345 645  SER B CA  
6129  C  C   . SER B 645  ? 1.0937 1.1063 1.0060 0.2491  -0.0459 -0.0407 645  SER B C   
6130  O  O   . SER B 645  ? 0.9413 0.9709 0.8656 0.2428  -0.0487 -0.0446 645  SER B O   
6131  C  CB  . SER B 645  ? 0.9545 0.9481 0.8745 0.2341  -0.0334 -0.0327 645  SER B CB  
6132  O  OG  . SER B 645  ? 1.0782 1.0804 1.0067 0.2341  -0.0350 -0.0346 645  SER B OG  
6133  N  N   . LYS B 646  ? 1.1515 1.1629 1.0561 0.2591  -0.0491 -0.0416 646  LYS B N   
6134  C  CA  . LYS B 646  ? 1.0633 1.0948 0.9739 0.2637  -0.0564 -0.0475 646  LYS B CA  
6135  C  C   . LYS B 646  ? 1.0386 1.0791 0.9440 0.2687  -0.0624 -0.0515 646  LYS B C   
6136  O  O   . LYS B 646  ? 0.9047 0.9643 0.8167 0.2714  -0.0688 -0.0571 646  LYS B O   
6137  C  CB  . LYS B 646  ? 0.9234 0.9499 0.8268 0.2735  -0.0577 -0.0470 646  LYS B CB  
6138  C  CG  . LYS B 646  ? 1.0345 1.0686 0.9506 0.2691  -0.0566 -0.0477 646  LYS B CG  
6139  C  CD  . LYS B 646  ? 1.2187 1.2383 1.1377 0.2608  -0.0490 -0.0426 646  LYS B CD  
6140  C  CE  . LYS B 646  ? 1.3378 1.3563 1.2611 0.2614  -0.0476 -0.0421 646  LYS B CE  
6141  N  NZ  . LYS B 646  ? 1.2765 1.2880 1.2081 0.2510  -0.0414 -0.0388 646  LYS B NZ  
6142  N  N   . VAL B 647  ? 1.0598 1.0875 0.9535 0.2700  -0.0607 -0.0491 647  VAL B N   
6143  C  CA  . VAL B 647  ? 1.1070 1.1424 0.9949 0.2746  -0.0665 -0.0531 647  VAL B CA  
6144  C  C   . VAL B 647  ? 0.9687 1.0172 0.8687 0.2642  -0.0674 -0.0562 647  VAL B C   
6145  O  O   . VAL B 647  ? 0.9291 0.9845 0.8255 0.2665  -0.0722 -0.0599 647  VAL B O   
6146  C  CB  . VAL B 647  ? 1.1104 1.1250 0.9779 0.2824  -0.0646 -0.0491 647  VAL B CB  
6147  C  CG1 . VAL B 647  ? 0.9749 0.9751 0.8288 0.2932  -0.0636 -0.0459 647  VAL B CG1 
6148  C  CG2 . VAL B 647  ? 0.9840 0.9833 0.8501 0.2740  -0.0570 -0.0440 647  VAL B CG2 
6149  N  N   . ASN B 648  ? 0.8107 0.8623 0.7245 0.2529  -0.0630 -0.0550 648  ASN B N   
6150  C  CA  . ASN B 648  ? 0.7573 0.8208 0.6826 0.2428  -0.0634 -0.0579 648  ASN B CA  
6151  C  C   . ASN B 648  ? 0.7801 0.8677 0.7159 0.2429  -0.0706 -0.0652 648  ASN B C   
6152  O  O   . ASN B 648  ? 0.8178 0.9163 0.7612 0.2448  -0.0728 -0.0673 648  ASN B O   
6153  C  CB  . ASN B 648  ? 0.7323 0.7938 0.6698 0.2316  -0.0571 -0.0549 648  ASN B CB  
6154  C  CG  . ASN B 648  ? 0.8039 0.8444 0.7334 0.2289  -0.0499 -0.0485 648  ASN B CG  
6155  O  OD1 . ASN B 648  ? 0.8339 0.8623 0.7498 0.2337  -0.0494 -0.0466 648  ASN B OD1 
6156  N  ND2 . ASN B 648  ? 0.7853 0.8218 0.7234 0.2214  -0.0443 -0.0452 648  ASN B ND2 
6157  N  N   . GLY B 649  ? 0.7552 0.8511 0.6916 0.2407  -0.0742 -0.0691 649  GLY B N   
6158  C  CA  . GLY B 649  ? 0.8253 0.9444 0.7722 0.2396  -0.0809 -0.0764 649  GLY B CA  
6159  C  C   . GLY B 649  ? 0.8952 1.0201 0.8324 0.2496  -0.0882 -0.0808 649  GLY B C   
6160  O  O   . GLY B 649  ? 0.9740 1.1186 0.9198 0.2481  -0.0940 -0.0874 649  GLY B O   
6161  N  N   . THR B 650  ? 1.2968 1.4053 1.2163 0.2598  -0.0882 -0.0775 650  THR B N   
6162  C  CA  . THR B 650  ? 1.4176 1.5307 1.3265 0.2703  -0.0955 -0.0815 650  THR B CA  
6163  C  C   . THR B 650  ? 1.3994 1.5167 1.3076 0.2657  -0.0980 -0.0850 650  THR B C   
6164  O  O   . THR B 650  ? 1.3144 1.4171 1.2170 0.2607  -0.0930 -0.0812 650  THR B O   
6165  C  CB  . THR B 650  ? 1.4077 1.4995 1.2962 0.2820  -0.0939 -0.0765 650  THR B CB  
6166  O  OG1 . THR B 650  ? 1.4017 1.4720 1.2842 0.2772  -0.0856 -0.0695 650  THR B OG1 
6167  C  CG2 . THR B 650  ? 1.4736 1.5663 1.3613 0.2899  -0.0948 -0.0756 650  THR B CG2 
6168  N  N   . ILE B 651  ? 1.4468 1.5845 1.3609 0.2672  -0.1058 -0.0925 651  ILE B N   
6169  C  CA  . ILE B 651  ? 1.4434 1.5871 1.3580 0.2624  -0.1089 -0.0969 651  ILE B CA  
6170  C  C   . ILE B 651  ? 1.4547 1.5831 1.3486 0.2720  -0.1109 -0.0954 651  ILE B C   
6171  O  O   . ILE B 651  ? 1.4857 1.6103 1.3676 0.2845  -0.1145 -0.0952 651  ILE B O   
6172  C  CB  . ILE B 651  ? 1.4722 1.6433 1.4004 0.2608  -0.1167 -0.1057 651  ILE B CB  
6173  C  CG1 . ILE B 651  ? 1.5253 1.7100 1.4740 0.2486  -0.1135 -0.1071 651  ILE B CG1 
6174  C  CG2 . ILE B 651  ? 1.4780 1.6545 1.4025 0.2595  -0.1218 -0.1111 651  ILE B CG2 
6175  C  CD1 . ILE B 651  ? 1.5822 1.7928 1.5456 0.2436  -0.1196 -0.1157 651  ILE B CD1 
6176  N  N   . ALA B 652  ? 1.2913 1.4102 1.1803 0.2664  -0.1084 -0.0944 652  ALA B N   
6177  C  CA  . ALA B 652  ? 1.3419 1.4453 1.2110 0.2744  -0.1095 -0.0929 652  ALA B CA  
6178  C  C   . ALA B 652  ? 1.3552 1.4684 1.2254 0.2704  -0.1147 -0.0992 652  ALA B C   
6179  O  O   . ALA B 652  ? 1.3735 1.4913 1.2547 0.2584  -0.1121 -0.1005 652  ALA B O   
6180  C  CB  . ALA B 652  ? 1.2884 1.3662 1.1472 0.2724  -0.1003 -0.0843 652  ALA B CB  
6181  N  N   . ARG B 653  ? 1.1524 1.2682 1.0105 0.2806  -0.1220 -0.1032 653  ARG B N   
6182  C  CA  . ARG B 653  ? 1.1766 1.3014 1.0338 0.2785  -0.1280 -0.1098 653  ARG B CA  
6183  C  C   . ARG B 653  ? 1.1225 1.2249 0.9623 0.2795  -0.1241 -0.1056 653  ARG B C   
6184  O  O   . ARG B 653  ? 1.1366 1.2284 0.9579 0.2908  -0.1270 -0.1049 653  ARG B O   
6185  C  CB  . ARG B 653  ? 1.2382 1.3782 1.0914 0.2894  -0.1384 -0.1167 653  ARG B CB  
6186  C  CG  . ARG B 653  ? 1.2106 1.3627 1.0642 0.2872  -0.1457 -0.1247 653  ARG B CG  
6187  C  CD  . ARG B 653  ? 1.2864 1.4424 1.1260 0.3019  -0.1547 -0.1289 653  ARG B CD  
6188  N  NE  . ARG B 653  ? 1.3520 1.5309 1.2000 0.2999  -0.1640 -0.1390 653  ARG B NE  
6189  C  CZ  . ARG B 653  ? 1.3736 1.5776 1.2362 0.3007  -0.1705 -0.1457 653  ARG B CZ  
6190  N  NH1 . ARG B 653  ? 1.3841 1.5940 1.2544 0.3036  -0.1689 -0.1434 653  ARG B NH1 
6191  N  NH2 . ARG B 653  ? 1.3377 1.5617 1.2074 0.2984  -0.1788 -0.1551 653  ARG B NH2 
6192  N  N   . ILE B 654  ? 1.0238 1.1187 0.8691 0.2680  -0.1173 -0.1027 654  ILE B N   
6193  C  CA  . ILE B 654  ? 1.0507 1.1243 0.8808 0.2681  -0.1126 -0.0982 654  ILE B CA  
6194  C  C   . ILE B 654  ? 1.1094 1.1892 0.9345 0.2679  -0.1191 -0.1050 654  ILE B C   
6195  O  O   . ILE B 654  ? 1.0022 1.0972 0.8411 0.2581  -0.1216 -0.1108 654  ILE B O   
6196  C  CB  . ILE B 654  ? 0.9949 1.0586 0.8329 0.2563  -0.1029 -0.0927 654  ILE B CB  
6197  C  CG1 . ILE B 654  ? 1.0225 1.0799 0.8653 0.2566  -0.0967 -0.0862 654  ILE B CG1 
6198  C  CG2 . ILE B 654  ? 0.9737 1.0165 0.7964 0.2565  -0.0981 -0.0885 654  ILE B CG2 
6199  C  CD1 . ILE B 654  ? 0.8918 0.9394 0.7419 0.2459  -0.0873 -0.0806 654  ILE B CD1 
6200  N  N   . GLU B 655  ? 1.0392 1.1067 0.8440 0.2787  -0.1218 -0.1044 655  GLU B N   
6201  C  CA  . GLU B 655  ? 1.0001 1.0700 0.7968 0.2796  -0.1278 -0.1103 655  GLU B CA  
6202  C  C   . GLU B 655  ? 0.9974 1.0441 0.7802 0.2777  -0.1208 -0.1048 655  GLU B C   
6203  O  O   . GLU B 655  ? 0.9917 1.0186 0.7574 0.2864  -0.1167 -0.0984 655  GLU B O   
6204  C  CB  . GLU B 655  ? 1.1141 1.1884 0.8974 0.2940  -0.1369 -0.1145 655  GLU B CB  
6205  C  CG  . GLU B 655  ? 1.2812 1.3655 1.0610 0.2942  -0.1454 -0.1230 655  GLU B CG  
6206  C  CD  . GLU B 655  ? 1.3961 1.4908 1.1673 0.3076  -0.1558 -0.1286 655  GLU B CD  
6207  O  OE1 . GLU B 655  ? 1.4669 1.5610 1.2349 0.3169  -0.1562 -0.1257 655  GLU B OE1 
6208  O  OE2 . GLU B 655  ? 1.4573 1.5608 1.2247 0.3090  -0.1636 -0.1360 655  GLU B OE2 
6209  N  N   . TYR B 656  ? 1.3223 1.3714 1.1123 0.2666  -0.1193 -0.1073 656  TYR B N   
6210  C  CA  . TYR B 656  ? 1.4324 1.4607 1.2118 0.2633  -0.1118 -0.1020 656  TYR B CA  
6211  C  C   . TYR B 656  ? 1.5448 1.5693 1.3097 0.2670  -0.1172 -0.1068 656  TYR B C   
6212  O  O   . TYR B 656  ? 1.5593 1.5678 1.3039 0.2775  -0.1170 -0.1037 656  TYR B O   
6213  C  CB  . TYR B 656  ? 1.3232 1.3541 1.1192 0.2485  -0.1054 -0.1006 656  TYR B CB  
6214  C  CG  . TYR B 656  ? 1.2786 1.2895 1.0657 0.2444  -0.0973 -0.0952 656  TYR B CG  
6215  C  CD1 . TYR B 656  ? 1.2830 1.2721 1.0545 0.2514  -0.0908 -0.0872 656  TYR B CD1 
6216  C  CD2 . TYR B 656  ? 1.2567 1.2704 1.0513 0.2333  -0.0958 -0.0979 656  TYR B CD2 
6217  C  CE1 . TYR B 656  ? 1.2529 1.2245 1.0169 0.2477  -0.0831 -0.0823 656  TYR B CE1 
6218  C  CE2 . TYR B 656  ? 1.3220 1.3178 1.1087 0.2299  -0.0884 -0.0930 656  TYR B CE2 
6219  C  CZ  . TYR B 656  ? 1.2898 1.2651 1.0615 0.2371  -0.0821 -0.0852 656  TYR B CZ  
6220  O  OH  . TYR B 656  ? 1.3081 1.2662 1.0723 0.2338  -0.0745 -0.0804 656  TYR B OH  
6221  N  N   . ARG B 657  ? 1.4061 1.4449 1.1809 0.2585  -0.1220 -0.1144 657  ARG B N   
6222  C  CA  . ARG B 657  ? 1.4182 1.4555 1.1808 0.2610  -0.1280 -0.1202 657  ARG B CA  
6223  C  C   . ARG B 657  ? 1.4922 1.5554 1.2685 0.2570  -0.1380 -0.1309 657  ARG B C   
6224  O  O   . ARG B 657  ? 1.4946 1.5661 1.2810 0.2460  -0.1388 -0.1359 657  ARG B O   
6225  C  CB  . ARG B 657  ? 1.3121 1.3341 1.0699 0.2532  -0.1213 -0.1174 657  ARG B CB  
6226  C  CG  . ARG B 657  ? 1.2623 1.2580 1.0013 0.2600  -0.1133 -0.1083 657  ARG B CG  
6227  C  CD  . ARG B 657  ? 1.2863 1.2684 1.0263 0.2505  -0.1041 -0.1036 657  ARG B CD  
6228  N  NE  . ARG B 657  ? 1.3715 1.3294 1.0940 0.2573  -0.0963 -0.0951 657  ARG B NE  
6229  C  CZ  . ARG B 657  ? 1.3403 1.2834 1.0614 0.2515  -0.0870 -0.0891 657  ARG B CZ  
6230  N  NH1 . ARG B 657  ? 1.3193 1.2680 1.0544 0.2392  -0.0841 -0.0905 657  ARG B NH1 
6231  N  NH2 . ARG B 657  ? 1.2821 1.2041 0.9871 0.2585  -0.0802 -0.0815 657  ARG B NH2 
6232  N  N   . GLY B 658  ? 1.7050 1.7813 1.4814 0.2662  -0.1456 -0.1346 658  GLY B N   
6233  C  CA  . GLY B 658  ? 1.6378 1.7401 1.4273 0.2638  -0.1554 -0.1449 658  GLY B CA  
6234  C  C   . GLY B 658  ? 1.6567 1.7781 1.4706 0.2540  -0.1542 -0.1466 658  GLY B C   
6235  O  O   . GLY B 658  ? 1.6435 1.7875 1.4709 0.2497  -0.1613 -0.1553 658  GLY B O   
6236  N  N   . GLY B 659  ? 1.1136 1.2268 0.9336 0.2505  -0.1454 -0.1387 659  GLY B N   
6237  C  CA  . GLY B 659  ? 1.0125 1.1420 0.8550 0.2410  -0.1433 -0.1397 659  GLY B CA  
6238  C  C   . GLY B 659  ? 0.9499 1.0787 0.7945 0.2478  -0.1408 -0.1342 659  GLY B C   
6239  O  O   . GLY B 659  ? 0.9788 1.0882 0.8096 0.2550  -0.1357 -0.1265 659  GLY B O   
6240  N  N   . ILE B 660  ? 1.2749 1.4253 1.1367 0.2453  -0.1442 -0.1384 660  ILE B N   
6241  C  CA  . ILE B 660  ? 1.3688 1.5207 1.2359 0.2497  -0.1415 -0.1337 660  ILE B CA  
6242  C  C   . ILE B 660  ? 1.3930 1.5524 1.2800 0.2367  -0.1354 -0.1322 660  ILE B C   
6243  O  O   . ILE B 660  ? 1.4479 1.6251 1.3503 0.2273  -0.1381 -0.1386 660  ILE B O   
6244  C  CB  . ILE B 660  ? 1.3910 1.5615 1.2603 0.2597  -0.1506 -0.1394 660  ILE B CB  
6245  C  CG1 . ILE B 660  ? 1.4111 1.6078 1.2962 0.2528  -0.1581 -0.1498 660  ILE B CG1 
6246  C  CG2 . ILE B 660  ? 1.4074 1.5666 1.2545 0.2745  -0.1554 -0.1390 660  ILE B CG2 
6247  C  CD1 . ILE B 660  ? 1.2877 1.5058 1.1787 0.2613  -0.1667 -0.1558 660  ILE B CD1 
6248  N  N   . ILE B 661  ? 1.3199 1.4653 1.2064 0.2360  -0.1271 -0.1238 661  ILE B N   
6249  C  CA  . ILE B 661  ? 1.3358 1.4849 1.2390 0.2240  -0.1206 -0.1215 661  ILE B CA  
6250  C  C   . ILE B 661  ? 1.4232 1.5842 1.3384 0.2257  -0.1206 -0.1208 661  ILE B C   
6251  O  O   . ILE B 661  ? 1.3934 1.5677 1.3260 0.2161  -0.1190 -0.1228 661  ILE B O   
6252  C  CB  . ILE B 661  ? 1.2266 1.3524 1.1229 0.2198  -0.1108 -0.1129 661  ILE B CB  
6253  C  CG1 . ILE B 661  ? 1.1931 1.3233 1.1059 0.2059  -0.1050 -0.1120 661  ILE B CG1 
6254  C  CG2 . ILE B 661  ? 1.2723 1.3829 1.1593 0.2283  -0.1063 -0.1052 661  ILE B CG2 
6255  C  CD1 . ILE B 661  ? 1.2046 1.3143 1.1128 0.2023  -0.0953 -0.1035 661  ILE B CD1 
6256  N  N   . GLU B 662  ? 1.4417 1.5977 1.3476 0.2377  -0.1221 -0.1179 662  GLU B N   
6257  C  CA  . GLU B 662  ? 1.4624 1.6294 1.3780 0.2408  -0.1227 -0.1176 662  GLU B CA  
6258  C  C   . GLU B 662  ? 1.3484 1.5140 1.2776 0.2305  -0.1148 -0.1132 662  GLU B C   
6259  O  O   . GLU B 662  ? 1.3309 1.5142 1.2772 0.2238  -0.1157 -0.1168 662  GLU B O   
6260  C  CB  . GLU B 662  ? 1.5753 1.7688 1.5021 0.2421  -0.1316 -0.1267 662  GLU B CB  
6261  C  CG  . GLU B 662  ? 1.6508 1.8471 1.5641 0.2550  -0.1400 -0.1308 662  GLU B CG  
6262  C  CD  . GLU B 662  ? 1.6208 1.8426 1.5447 0.2597  -0.1483 -0.1382 662  GLU B CD  
6263  O  OE1 . GLU B 662  ? 1.4497 1.6868 1.3914 0.2531  -0.1470 -0.1399 662  GLU B OE1 
6264  O  OE2 . GLU B 662  ? 1.6404 1.8675 1.5549 0.2701  -0.1561 -0.1426 662  GLU B OE2 
6265  N  N   . ILE B 663  ? 1.0092 1.1533 0.9303 0.2298  -0.1071 -0.1052 663  ILE B N   
6266  C  CA  . ILE B 663  ? 0.9537 1.0936 0.8855 0.2205  -0.0993 -0.1004 663  ILE B CA  
6267  C  C   . ILE B 663  ? 0.9807 1.1107 0.9082 0.2274  -0.0958 -0.0944 663  ILE B C   
6268  O  O   . ILE B 663  ? 1.0208 1.1367 0.9323 0.2376  -0.0960 -0.0911 663  ILE B O   
6269  C  CB  . ILE B 663  ? 0.8902 1.0145 0.8179 0.2127  -0.0930 -0.0965 663  ILE B CB  
6270  C  CG1 . ILE B 663  ? 0.8260 0.9490 0.7666 0.2024  -0.0857 -0.0927 663  ILE B CG1 
6271  C  CG2 . ILE B 663  ? 0.8432 0.9448 0.7516 0.2207  -0.0899 -0.0907 663  ILE B CG2 
6272  C  CD1 . ILE B 663  ? 0.8308 0.9417 0.7697 0.1940  -0.0798 -0.0897 663  ILE B CD1 
6273  N  N   . PRO B 664  ? 0.8424 0.9789 0.7830 0.2226  -0.0928 -0.0930 664  PRO B N   
6274  C  CA  . PRO B 664  ? 0.7531 0.8790 0.6896 0.2285  -0.0891 -0.0873 664  PRO B CA  
6275  C  C   . PRO B 664  ? 0.7007 0.8026 0.6269 0.2275  -0.0814 -0.0795 664  PRO B C   
6276  O  O   . PRO B 664  ? 0.6867 0.7821 0.6137 0.2198  -0.0774 -0.0780 664  PRO B O   
6277  C  CB  . PRO B 664  ? 0.7847 0.9240 0.7392 0.2212  -0.0873 -0.0882 664  PRO B CB  
6278  C  CG  . PRO B 664  ? 0.7785 0.9285 0.7448 0.2094  -0.0870 -0.0920 664  PRO B CG  
6279  C  CD  . PRO B 664  ? 0.8339 0.9891 0.7936 0.2124  -0.0932 -0.0973 664  PRO B CD  
6280  N  N   . ILE B 665  ? 0.7733 0.8621 0.6899 0.2356  -0.0791 -0.0747 665  ILE B N   
6281  C  CA  . ILE B 665  ? 0.7771 0.8428 0.6828 0.2360  -0.0718 -0.0673 665  ILE B CA  
6282  C  C   . ILE B 665  ? 0.6868 0.7486 0.6024 0.2296  -0.0653 -0.0628 665  ILE B C   
6283  O  O   . ILE B 665  ? 0.6355 0.7094 0.5624 0.2282  -0.0667 -0.0647 665  ILE B O   
6284  C  CB  . ILE B 665  ? 0.8205 0.8713 0.7072 0.2488  -0.0726 -0.0644 665  ILE B CB  
6285  C  CG1 . ILE B 665  ? 0.8630 0.9129 0.7504 0.2546  -0.0722 -0.0624 665  ILE B CG1 
6286  C  CG2 . ILE B 665  ? 0.8001 0.8579 0.6778 0.2566  -0.0805 -0.0698 665  ILE B CG2 
6287  C  CD1 . ILE B 665  ? 0.9693 0.9992 0.8379 0.2656  -0.0701 -0.0576 665  ILE B CD1 
6288  N  N   . TRP B 666  ? 0.8503 0.8949 0.7613 0.2259  -0.0580 -0.0569 666  TRP B N   
6289  C  CA  . TRP B 666  ? 0.8779 0.9157 0.7960 0.2206  -0.0515 -0.0520 666  TRP B CA  
6290  C  C   . TRP B 666  ? 0.8404 0.8553 0.7452 0.2238  -0.0451 -0.0453 666  TRP B C   
6291  O  O   . TRP B 666  ? 0.9112 0.9161 0.8049 0.2259  -0.0441 -0.0440 666  TRP B O   
6292  C  CB  . TRP B 666  ? 0.8517 0.8972 0.7847 0.2083  -0.0485 -0.0526 666  TRP B CB  
6293  C  CG  . TRP B 666  ? 0.8677 0.9097 0.8097 0.2031  -0.0430 -0.0487 666  TRP B CG  
6294  C  CD1 . TRP B 666  ? 0.8832 0.9108 0.8240 0.1989  -0.0358 -0.0430 666  TRP B CD1 
6295  C  CD2 . TRP B 666  ? 0.7786 0.8322 0.7322 0.2015  -0.0443 -0.0504 666  TRP B CD2 
6296  N  NE1 . TRP B 666  ? 0.7224 0.7520 0.6733 0.1949  -0.0329 -0.0412 666  TRP B NE1 
6297  C  CE2 . TRP B 666  ? 0.7813 0.8264 0.7399 0.1964  -0.0380 -0.0456 666  TRP B CE2 
6298  C  CE3 . TRP B 666  ? 0.7631 0.8339 0.7236 0.2041  -0.0502 -0.0555 666  TRP B CE3 
6299  C  CZ2 . TRP B 666  ? 0.8433 0.8956 0.8125 0.1940  -0.0376 -0.0459 666  TRP B CZ2 
6300  C  CZ3 . TRP B 666  ? 0.8412 0.9191 0.8122 0.2017  -0.0494 -0.0556 666  TRP B CZ3 
6301  C  CH2 . TRP B 666  ? 0.8575 0.9259 0.8325 0.1967  -0.0432 -0.0508 666  TRP B CH2 
6302  N  N   . LEU B 667  ? 0.7037 0.7102 0.6098 0.2241  -0.0406 -0.0410 667  LEU B N   
6303  C  CA  . LEU B 667  ? 0.7948 0.7797 0.6890 0.2272  -0.0342 -0.0346 667  LEU B CA  
6304  C  C   . LEU B 667  ? 0.7882 0.7666 0.6898 0.2174  -0.0269 -0.0306 667  LEU B C   
6305  O  O   . LEU B 667  ? 0.7998 0.7839 0.7144 0.2108  -0.0248 -0.0302 667  LEU B O   
6306  C  CB  . LEU B 667  ? 0.7170 0.6953 0.6069 0.2337  -0.0335 -0.0324 667  LEU B CB  
6307  C  CG  . LEU B 667  ? 0.7854 0.7628 0.6620 0.2461  -0.0392 -0.0345 667  LEU B CG  
6308  C  CD1 . LEU B 667  ? 0.9089 0.8741 0.7783 0.2526  -0.0367 -0.0310 667  LEU B CD1 
6309  C  CD2 . LEU B 667  ? 0.8616 0.8290 0.7227 0.2513  -0.0396 -0.0338 667  LEU B CD2 
6310  N  N   . LEU B 668  ? 0.7842 0.7506 0.6771 0.2167  -0.0232 -0.0278 668  LEU B N   
6311  C  CA  . LEU B 668  ? 0.7019 0.6601 0.5997 0.2087  -0.0158 -0.0235 668  LEU B CA  
6312  C  C   . LEU B 668  ? 0.7594 0.6966 0.6437 0.2133  -0.0096 -0.0175 668  LEU B C   
6313  O  O   . LEU B 668  ? 0.8276 0.7553 0.6979 0.2185  -0.0094 -0.0166 668  LEU B O   
6314  C  CB  . LEU B 668  ? 0.7644 0.7278 0.6650 0.2031  -0.0162 -0.0255 668  LEU B CB  
6315  C  CG  . LEU B 668  ? 0.6646 0.6222 0.5715 0.1945  -0.0092 -0.0218 668  LEU B CG  
6316  C  CD1 . LEU B 668  ? 0.7786 0.7413 0.6999 0.1883  -0.0065 -0.0205 668  LEU B CD1 
6317  C  CD2 . LEU B 668  ? 0.6908 0.6561 0.6014 0.1891  -0.0110 -0.0250 668  LEU B CD2 
6318  N  N   . PRO B 669  ? 0.9322 0.8612 0.8196 0.2116  -0.0043 -0.0135 669  PRO B N   
6319  C  CA  . PRO B 669  ? 1.0506 0.9593 0.9243 0.2167  0.0014  -0.0081 669  PRO B CA  
6320  C  C   . PRO B 669  ? 1.1309 1.0275 0.9968 0.2153  0.0069  -0.0046 669  PRO B C   
6321  O  O   . PRO B 669  ? 1.1811 1.0634 1.0307 0.2225  0.0087  -0.0021 669  PRO B O   
6322  C  CB  . PRO B 669  ? 0.8439 0.7495 0.7268 0.2122  0.0061  -0.0052 669  PRO B CB  
6323  C  CG  . PRO B 669  ? 0.8684 0.7918 0.7640 0.2102  0.0001  -0.0099 669  PRO B CG  
6324  C  CD  . PRO B 669  ? 0.9439 0.8820 0.8462 0.2061  -0.0041 -0.0142 669  PRO B CD  
6325  N  N   . GLY B 670  ? 0.9540 0.8556 0.8304 0.2066  0.0097  -0.0043 670  GLY B N   
6326  C  CA  . GLY B 670  ? 1.0395 0.9293 0.9093 0.2050  0.0157  -0.0006 670  GLY B CA  
6327  C  C   . GLY B 670  ? 0.9068 0.7944 0.7639 0.2101  0.0126  -0.0025 670  GLY B C   
6328  O  O   . GLY B 670  ? 0.8250 0.7016 0.6747 0.2098  0.0176  0.0006  670  GLY B O   
6329  N  N   . HIS B 671  ? 1.0975 0.9955 0.9520 0.2147  0.0044  -0.0077 671  HIS B N   
6330  C  CA  . HIS B 671  ? 1.0337 0.9317 0.8773 0.2189  0.0005  -0.0104 671  HIS B CA  
6331  C  C   . HIS B 671  ? 1.1683 1.0473 0.9918 0.2278  0.0036  -0.0066 671  HIS B C   
6332  O  O   . HIS B 671  ? 1.2116 1.0808 1.0279 0.2334  0.0056  -0.0037 671  HIS B O   
6333  C  CB  . HIS B 671  ? 1.0032 0.9174 0.8490 0.2223  -0.0092 -0.0171 671  HIS B CB  
6334  C  CG  . HIS B 671  ? 1.1436 1.0664 0.9891 0.2204  -0.0138 -0.0218 671  HIS B CG  
6335  N  ND1 . HIS B 671  ? 1.2052 1.1173 1.0362 0.2243  -0.0129 -0.0209 671  HIS B ND1 
6336  C  CD2 . HIS B 671  ? 1.1381 1.0788 0.9955 0.2150  -0.0193 -0.0274 671  HIS B CD2 
6337  C  CE1 . HIS B 671  ? 1.1484 1.0715 0.9826 0.2212  -0.0178 -0.0261 671  HIS B CE1 
6338  N  NE2 . HIS B 671  ? 1.0817 1.0221 0.9320 0.2154  -0.0216 -0.0301 671  HIS B NE2 
6339  N  N   . ALA B 672  ? 1.0812 0.9544 0.8950 0.2291  0.0043  -0.0066 672  ALA B N   
6340  C  CA  . ALA B 672  ? 1.1106 0.9663 0.9040 0.2381  0.0067  -0.0034 672  ALA B CA  
6341  C  C   . ALA B 672  ? 1.1908 1.0496 0.9731 0.2483  -0.0014 -0.0072 672  ALA B C   
6342  O  O   . ALA B 672  ? 1.1567 1.0321 0.9453 0.2480  -0.0095 -0.0134 672  ALA B O   
6343  C  CB  . ALA B 672  ? 1.0488 0.8982 0.8349 0.2367  0.0092  -0.0028 672  ALA B CB  
6344  N  N   . GLU B 673  ? 1.1942 1.0367 0.9598 0.2573  0.0012  -0.0035 673  GLU B N   
6345  C  CA  . GLU B 673  ? 1.2008 1.0445 0.9545 0.2682  -0.0060 -0.0066 673  GLU B CA  
6346  C  C   . GLU B 673  ? 1.2962 1.1438 1.0400 0.2727  -0.0123 -0.0110 673  GLU B C   
6347  O  O   . GLU B 673  ? 1.2272 1.0680 0.9658 0.2704  -0.0090 -0.0097 673  GLU B O   
6348  C  CB  . GLU B 673  ? 1.2693 1.0925 1.0062 0.2769  -0.0009 -0.0010 673  GLU B CB  
6349  C  CG  . GLU B 673  ? 1.4193 1.2440 1.1456 0.2882  -0.0079 -0.0037 673  GLU B CG  
6350  C  CD  . GLU B 673  ? 1.5130 1.3154 1.2211 0.2970  -0.0023 0.0021  673  GLU B CD  
6351  O  OE1 . GLU B 673  ? 1.4387 1.2256 1.1447 0.2932  0.0073  0.0081  673  GLU B OE1 
6352  O  OE2 . GLU B 673  ? 1.5803 1.3805 1.2759 0.3079  -0.0075 0.0006  673  GLU B OE2 
6353  N  N   . ASP B 674  ? 1.4931 1.3525 1.2347 0.2792  -0.0216 -0.0166 674  ASP B N   
6354  C  CA  . ASP B 674  ? 1.4596 1.3254 1.1927 0.2840  -0.0292 -0.0220 674  ASP B CA  
6355  C  C   . ASP B 674  ? 1.4697 1.3489 1.2161 0.2737  -0.0311 -0.0261 674  ASP B C   
6356  O  O   . ASP B 674  ? 1.5575 1.4362 1.2957 0.2753  -0.0340 -0.0288 674  ASP B O   
6357  C  CB  . ASP B 674  ? 1.5079 1.3535 1.2174 0.2932  -0.0264 -0.0185 674  ASP B CB  
6358  C  CG  . ASP B 674  ? 1.6438 1.4778 1.3374 0.3053  -0.0270 -0.0160 674  ASP B CG  
6359  O  OD1 . ASP B 674  ? 1.6186 1.4620 1.3193 0.3074  -0.0309 -0.0180 674  ASP B OD1 
6360  O  OD2 . ASP B 674  ? 1.8102 1.6251 1.4839 0.3130  -0.0232 -0.0120 674  ASP B OD2 
6361  N  N   . SER B 675  ? 1.2682 1.1587 1.0345 0.2633  -0.0293 -0.0265 675  SER B N   
6362  C  CA  . SER B 675  ? 1.1734 1.0768 0.9532 0.2532  -0.0307 -0.0303 675  SER B CA  
6363  C  C   . SER B 675  ? 1.1297 1.0536 0.9292 0.2472  -0.0352 -0.0346 675  SER B C   
6364  O  O   . SER B 675  ? 1.0967 1.0212 0.9038 0.2461  -0.0325 -0.0320 675  SER B O   
6365  C  CB  . SER B 675  ? 1.2134 1.1061 0.9967 0.2452  -0.0214 -0.0250 675  SER B CB  
6366  O  OG  . SER B 675  ? 1.1993 1.1041 0.9957 0.2356  -0.0227 -0.0286 675  SER B OG  
6367  N  N   . ILE B 676  ? 0.9895 0.9298 0.7968 0.2432  -0.0417 -0.0413 676  ILE B N   
6368  C  CA  . ILE B 676  ? 0.8989 0.8598 0.7248 0.2371  -0.0461 -0.0460 676  ILE B CA  
6369  C  C   . ILE B 676  ? 0.8945 0.8629 0.7327 0.2256  -0.0446 -0.0481 676  ILE B C   
6370  O  O   . ILE B 676  ? 0.9252 0.8928 0.7576 0.2246  -0.0465 -0.0508 676  ILE B O   
6371  C  CB  . ILE B 676  ? 0.8306 0.8065 0.6553 0.2437  -0.0562 -0.0529 676  ILE B CB  
6372  C  CG1 . ILE B 676  ? 0.7797 0.7470 0.5910 0.2560  -0.0576 -0.0507 676  ILE B CG1 
6373  C  CG2 . ILE B 676  ? 0.8432 0.8406 0.6876 0.2369  -0.0602 -0.0578 676  ILE B CG2 
6374  C  CD1 . ILE B 676  ? 0.9231 0.9037 0.7307 0.2642  -0.0676 -0.0573 676  ILE B CD1 
6375  N  N   . THR B 677  ? 0.9949 0.9701 0.8493 0.2172  -0.0413 -0.0468 677  THR B N   
6376  C  CA  . THR B 677  ? 0.9643 0.9463 0.8308 0.2062  -0.0393 -0.0483 677  THR B CA  
6377  C  C   . THR B 677  ? 0.8860 0.8895 0.7664 0.2016  -0.0459 -0.0553 677  THR B C   
6378  O  O   . THR B 677  ? 0.8475 0.8610 0.7368 0.2023  -0.0480 -0.0563 677  THR B O   
6379  C  CB  . THR B 677  ? 0.9505 0.9259 0.8257 0.1995  -0.0310 -0.0425 677  THR B CB  
6380  O  OG1 . THR B 677  ? 1.0763 1.0323 0.9393 0.2027  -0.0244 -0.0364 677  THR B OG1 
6381  C  CG2 . THR B 677  ? 0.8887 0.8723 0.7767 0.1886  -0.0295 -0.0444 677  THR B CG2 
6382  N  N   . LEU B 678  ? 1.0311 1.0414 0.9131 0.1970  -0.0490 -0.0601 678  LEU B N   
6383  C  CA  . LEU B 678  ? 1.0233 1.0539 0.9186 0.1915  -0.0548 -0.0671 678  LEU B CA  
6384  C  C   . LEU B 678  ? 1.0133 1.0460 0.9194 0.1799  -0.0506 -0.0670 678  LEU B C   
6385  O  O   . LEU B 678  ? 1.0020 1.0241 0.9014 0.1773  -0.0473 -0.0655 678  LEU B O   
6386  C  CB  . LEU B 678  ? 1.0444 1.0823 0.9324 0.1960  -0.0629 -0.0738 678  LEU B CB  
6387  C  CG  . LEU B 678  ? 0.9768 1.0188 0.8575 0.2072  -0.0691 -0.0758 678  LEU B CG  
6388  C  CD1 . LEU B 678  ? 1.0633 1.1112 0.9356 0.2118  -0.0769 -0.0823 678  LEU B CD1 
6389  C  CD2 . LEU B 678  ? 1.0294 1.0879 0.9244 0.2063  -0.0718 -0.0781 678  LEU B CD2 
6390  N  N   . ASN B 679  ? 0.9163 0.9620 0.8384 0.1733  -0.0504 -0.0685 679  ASN B N   
6391  C  CA  . ASN B 679  ? 0.8660 0.9132 0.7986 0.1626  -0.0458 -0.0678 679  ASN B CA  
6392  C  C   . ASN B 679  ? 0.7834 0.8442 0.7226 0.1563  -0.0504 -0.0750 679  ASN B C   
6393  O  O   . ASN B 679  ? 0.8395 0.9161 0.7849 0.1572  -0.0566 -0.0806 679  ASN B O   
6394  C  CB  . ASN B 679  ? 0.7734 0.8255 0.7190 0.1589  -0.0424 -0.0649 679  ASN B CB  
6395  C  CG  . ASN B 679  ? 0.7385 0.7755 0.6790 0.1624  -0.0362 -0.0574 679  ASN B CG  
6396  O  OD1 . ASN B 679  ? 0.7213 0.7432 0.6504 0.1652  -0.0327 -0.0537 679  ASN B OD1 
6397  N  ND2 . ASN B 679  ? 0.7895 0.8304 0.7384 0.1623  -0.0348 -0.0554 679  ASN B ND2 
6398  N  N   . LEU B 680  ? 0.8961 0.9506 0.8339 0.1499  -0.0473 -0.0748 680  LEU B N   
6399  C  CA  . LEU B 680  ? 1.0201 1.0846 0.9624 0.1433  -0.0508 -0.0814 680  LEU B CA  
6400  C  C   . LEU B 680  ? 0.9546 1.0317 0.9137 0.1340  -0.0494 -0.0832 680  LEU B C   
6401  O  O   . LEU B 680  ? 1.0147 1.0902 0.9808 0.1320  -0.0447 -0.0787 680  LEU B O   
6402  C  CB  . LEU B 680  ? 1.0988 1.1497 1.0314 0.1405  -0.0476 -0.0804 680  LEU B CB  
6403  C  CG  . LEU B 680  ? 1.0856 1.1220 1.0005 0.1491  -0.0480 -0.0782 680  LEU B CG  
6404  C  CD1 . LEU B 680  ? 1.0412 1.0624 0.9481 0.1458  -0.0426 -0.0753 680  LEU B CD1 
6405  C  CD2 . LEU B 680  ? 1.1693 1.2139 1.0780 0.1543  -0.0566 -0.0850 680  LEU B CD2 
6406  N  N   . GLY B 681  ? 0.6729 0.7623 0.6380 0.1283  -0.0534 -0.0900 681  GLY B N   
6407  C  CA  . GLY B 681  ? 0.7150 0.8151 0.6946 0.1187  -0.0516 -0.0921 681  GLY B CA  
6408  C  C   . GLY B 681  ? 0.7430 0.8621 0.7350 0.1186  -0.0558 -0.0961 681  GLY B C   
6409  O  O   . GLY B 681  ? 0.7767 0.9025 0.7806 0.1124  -0.0528 -0.0955 681  GLY B O   
6410  N  N   . TYR B 682  ? 0.9871 1.1152 0.9765 0.1257  -0.0626 -0.1001 682  TYR B N   
6411  C  CA  . TYR B 682  ? 0.9972 1.1438 0.9978 0.1268  -0.0669 -0.1040 682  TYR B CA  
6412  C  C   . TYR B 682  ? 1.0820 1.2432 1.0839 0.1271  -0.0746 -0.1125 682  TYR B C   
6413  O  O   . TYR B 682  ? 1.1059 1.2617 1.0983 0.1280  -0.0771 -0.1151 682  TYR B O   
6414  C  CB  . TYR B 682  ? 1.0299 1.1740 1.0268 0.1368  -0.0676 -0.1000 682  TYR B CB  
6415  C  CG  . TYR B 682  ? 1.0432 1.1770 1.0423 0.1357  -0.0605 -0.0926 682  TYR B CG  
6416  C  CD1 . TYR B 682  ? 0.9704 1.0849 0.9587 0.1383  -0.0556 -0.0862 682  TYR B CD1 
6417  C  CD2 . TYR B 682  ? 1.0719 1.2155 1.0839 0.1323  -0.0589 -0.0921 682  TYR B CD2 
6418  C  CE1 . TYR B 682  ? 0.9735 1.0794 0.9645 0.1372  -0.0494 -0.0798 682  TYR B CE1 
6419  C  CE2 . TYR B 682  ? 1.0123 1.1468 1.0262 0.1314  -0.0529 -0.0857 682  TYR B CE2 
6420  C  CZ  . TYR B 682  ? 0.9563 1.0722 0.9600 0.1338  -0.0483 -0.0797 682  TYR B CZ  
6421  O  OH  . TYR B 682  ? 0.8313 0.9390 0.8376 0.1327  -0.0426 -0.0737 682  TYR B OH  
6422  N  N   . GLY B 683  ? 1.2209 1.4013 1.2349 0.1265  -0.0783 -0.1171 683  GLY B N   
6423  C  CA  . GLY B 683  ? 1.2658 1.4628 1.2829 0.1272  -0.0861 -0.1255 683  GLY B CA  
6424  C  C   . GLY B 683  ? 1.2438 1.4493 1.2690 0.1160  -0.0863 -0.1315 683  GLY B C   
6425  O  O   . GLY B 683  ? 1.3030 1.5203 1.3292 0.1160  -0.0928 -0.1388 683  GLY B O   
6426  N  N   . ARG B 684  ? 0.8728 1.0724 0.9035 0.1065  -0.0795 -0.1286 684  ARG B N   
6427  C  CA  . ARG B 684  ? 0.9554 1.1616 0.9934 0.0952  -0.0789 -0.1340 684  ARG B CA  
6428  C  C   . ARG B 684  ? 0.9717 1.2018 1.0246 0.0919  -0.0833 -0.1411 684  ARG B C   
6429  O  O   . ARG B 684  ? 0.9511 1.1915 1.0113 0.0960  -0.0841 -0.1403 684  ARG B O   
6430  C  CB  . ARG B 684  ? 0.8811 1.0761 0.9220 0.0867  -0.0704 -0.1289 684  ARG B CB  
6431  C  CG  . ARG B 684  ? 0.8526 1.0250 0.8797 0.0889  -0.0659 -0.1225 684  ARG B CG  
6432  C  CD  . ARG B 684  ? 0.8498 1.0120 0.8801 0.0815  -0.0576 -0.1172 684  ARG B CD  
6433  N  NE  . ARG B 684  ? 0.8668 1.0347 0.9048 0.0704  -0.0559 -0.1216 684  ARG B NE  
6434  C  CZ  . ARG B 684  ? 0.8915 1.0481 0.9235 0.0645  -0.0530 -0.1219 684  ARG B CZ  
6435  N  NH1 . ARG B 684  ? 0.9630 1.1025 0.9813 0.0687  -0.0516 -0.1182 684  ARG B NH1 
6436  N  NH2 . ARG B 684  ? 0.8371 0.9994 0.8765 0.0542  -0.0514 -0.1261 684  ARG B NH2 
6437  N  N   . THR B 685  ? 1.1675 1.4067 1.2249 0.0844  -0.0860 -0.1484 685  THR B N   
6438  C  CA  . THR B 685  ? 1.1931 1.4559 1.2656 0.0799  -0.0898 -0.1559 685  THR B CA  
6439  C  C   . THR B 685  ? 1.1102 1.3773 1.1939 0.0663  -0.0847 -0.1581 685  THR B C   
6440  O  O   . THR B 685  ? 1.0923 1.3778 1.1903 0.0621  -0.0854 -0.1622 685  THR B O   
6441  C  CB  . THR B 685  ? 1.2418 1.5162 1.3121 0.0828  -0.0986 -0.1643 685  THR B CB  
6442  O  OG1 . THR B 685  ? 1.2347 1.5000 1.2986 0.0760  -0.0982 -0.1671 685  THR B OG1 
6443  C  CG2 . THR B 685  ? 1.1955 1.4654 1.2537 0.0968  -0.1039 -0.1623 685  THR B CG2 
6444  N  N   . HIS B 686  ? 1.0086 1.2592 1.0859 0.0596  -0.0794 -0.1554 686  HIS B N   
6445  C  CA  . HIS B 686  ? 1.0175 1.2693 1.1034 0.0469  -0.0739 -0.1570 686  HIS B CA  
6446  C  C   . HIS B 686  ? 1.0000 1.2360 1.0839 0.0445  -0.0653 -0.1485 686  HIS B C   
6447  O  O   . HIS B 686  ? 1.0108 1.2388 1.0953 0.0354  -0.0598 -0.1478 686  HIS B O   
6448  C  CB  . HIS B 686  ? 1.0470 1.2941 1.1279 0.0399  -0.0752 -0.1623 686  HIS B CB  
6449  C  CG  . HIS B 686  ? 1.0040 1.2717 1.0937 0.0364  -0.0820 -0.1724 686  HIS B CG  
6450  N  ND1 . HIS B 686  ? 0.9939 1.2675 1.0779 0.0436  -0.0904 -0.1773 686  HIS B ND1 
6451  C  CD2 . HIS B 686  ? 0.8896 1.1735 0.9936 0.0266  -0.0816 -0.1787 686  HIS B CD2 
6452  C  CE1 . HIS B 686  ? 1.0384 1.3319 1.1332 0.0384  -0.0952 -0.1864 686  HIS B CE1 
6453  N  NE2 . HIS B 686  ? 0.9253 1.2254 1.0327 0.0277  -0.0899 -0.1874 686  HIS B NE2 
6454  N  N   . ALA B 687  ? 1.3437 1.5750 1.4251 0.0529  -0.0640 -0.1420 687  ALA B N   
6455  C  CA  . ALA B 687  ? 1.2626 1.4819 1.3441 0.0512  -0.0565 -0.1343 687  ALA B CA  
6456  C  C   . ALA B 687  ? 1.4407 1.6739 1.5369 0.0455  -0.0537 -0.1354 687  ALA B C   
6457  O  O   . ALA B 687  ? 1.4934 1.7455 1.5998 0.0433  -0.0575 -0.1418 687  ALA B O   
6458  C  CB  . ALA B 687  ? 1.2562 1.4651 1.3294 0.0619  -0.0563 -0.1275 687  ALA B CB  
6459  N  N   . GLY B 688  ? 1.4391 1.6631 1.5363 0.0434  -0.0470 -0.1291 688  GLY B N   
6460  C  CA  . GLY B 688  ? 1.3441 1.5786 1.4538 0.0378  -0.0435 -0.1294 688  GLY B CA  
6461  C  C   . GLY B 688  ? 1.3397 1.5889 1.4568 0.0447  -0.0470 -0.1299 688  GLY B C   
6462  O  O   . GLY B 688  ? 1.3808 1.6333 1.4939 0.0536  -0.0525 -0.1306 688  GLY B O   
6463  N  N   . ARG B 689  ? 0.8610 1.1186 0.9886 0.0404  -0.0433 -0.1294 689  ARG B N   
6464  C  CA  . ARG B 689  ? 0.7730 1.0449 0.9085 0.0462  -0.0459 -0.1299 689  ARG B CA  
6465  C  C   . ARG B 689  ? 0.7971 1.0589 0.9247 0.0568  -0.0466 -0.1238 689  ARG B C   
6466  O  O   . ARG B 689  ? 0.7750 1.0463 0.9043 0.0647  -0.0512 -0.1249 689  ARG B O   
6467  C  CB  . ARG B 689  ? 0.6943 0.9735 0.8407 0.0397  -0.0406 -0.1295 689  ARG B CB  
6468  C  CG  . ARG B 689  ? 0.7480 1.0103 0.8902 0.0354  -0.0332 -0.1230 689  ARG B CG  
6469  C  CD  . ARG B 689  ? 0.8940 1.1631 1.0460 0.0264  -0.0279 -0.1241 689  ARG B CD  
6470  N  NE  . ARG B 689  ? 0.8894 1.1650 1.0456 0.0171  -0.0278 -0.1304 689  ARG B NE  
6471  C  CZ  . ARG B 689  ? 0.8991 1.1798 1.0630 0.0079  -0.0229 -0.1322 689  ARG B CZ  
6472  N  NH1 . ARG B 689  ? 0.8272 1.1072 0.9951 0.0070  -0.0178 -0.1282 689  ARG B NH1 
6473  N  NH2 . ARG B 689  ? 0.8879 1.1740 1.0552 -0.0006 -0.0230 -0.1381 689  ARG B NH2 
6474  N  N   . VAL B 690  ? 1.1056 1.3485 1.2246 0.0570  -0.0421 -0.1173 690  VAL B N   
6475  C  CA  . VAL B 690  ? 1.0577 1.2893 1.1684 0.0662  -0.0425 -0.1114 690  VAL B CA  
6476  C  C   . VAL B 690  ? 1.1473 1.3708 1.2466 0.0714  -0.0464 -0.1121 690  VAL B C   
6477  O  O   . VAL B 690  ? 1.1530 1.3675 1.2465 0.0669  -0.0451 -0.1127 690  VAL B O   
6478  C  CB  . VAL B 690  ? 1.0241 1.2400 1.1316 0.0641  -0.0357 -0.1043 690  VAL B CB  
6479  C  CG1 . VAL B 690  ? 1.0062 1.2088 1.1042 0.0728  -0.0358 -0.0985 690  VAL B CG1 
6480  C  CG2 . VAL B 690  ? 1.1857 1.4092 1.3034 0.0607  -0.0322 -0.1033 690  VAL B CG2 
6481  N  N   . GLY B 691  ? 1.0390 1.2652 1.1344 0.0811  -0.0512 -0.1121 691  GLY B N   
6482  C  CA  . GLY B 691  ? 1.1478 1.3659 1.2313 0.0872  -0.0551 -0.1124 691  GLY B CA  
6483  C  C   . GLY B 691  ? 1.1692 1.3980 1.2532 0.0855  -0.0607 -0.1200 691  GLY B C   
6484  O  O   . GLY B 691  ? 1.1287 1.3485 1.2023 0.0878  -0.0628 -0.1205 691  GLY B O   
6485  N  N   . ASN B 692  ? 1.0476 1.2960 1.1437 0.0817  -0.0634 -0.1262 692  ASN B N   
6486  C  CA  . ASN B 692  ? 0.9632 1.2231 1.0613 0.0789  -0.0687 -0.1341 692  ASN B CA  
6487  C  C   . ASN B 692  ? 1.0081 1.2722 1.0992 0.0895  -0.0763 -0.1367 692  ASN B C   
6488  O  O   . ASN B 692  ? 1.2256 1.4926 1.3128 0.0890  -0.0809 -0.1419 692  ASN B O   
6489  C  CB  . ASN B 692  ? 1.0423 1.3227 1.1561 0.0717  -0.0691 -0.1400 692  ASN B CB  
6490  C  CG  . ASN B 692  ? 1.0769 1.3656 1.1939 0.0640  -0.0719 -0.1475 692  ASN B CG  
6491  O  OD1 . ASN B 692  ? 1.0425 1.3195 1.1499 0.0625  -0.0724 -0.1479 692  ASN B OD1 
6492  N  ND2 . ASN B 692  ? 1.1857 1.4948 1.3164 0.0590  -0.0736 -0.1538 692  ASN B ND2 
6493  N  N   . ASN B 693  ? 0.8327 1.0965 0.9214 0.0991  -0.0776 -0.1333 693  ASN B N   
6494  C  CA  . ASN B 693  ? 0.9379 1.2036 1.0182 0.1104  -0.0843 -0.1348 693  ASN B CA  
6495  C  C   . ASN B 693  ? 0.9331 1.1853 1.0049 0.1195  -0.0822 -0.1274 693  ASN B C   
6496  O  O   . ASN B 693  ? 0.8312 1.0908 0.9048 0.1273  -0.0849 -0.1273 693  ASN B O   
6497  C  CB  . ASN B 693  ? 0.9049 1.1946 0.9955 0.1128  -0.0908 -0.1422 693  ASN B CB  
6498  C  CG  . ASN B 693  ? 0.9841 1.2865 1.0803 0.1055  -0.0946 -0.1505 693  ASN B CG  
6499  O  OD1 . ASN B 693  ? 1.1100 1.4194 1.2169 0.0947  -0.0914 -0.1531 693  ASN B OD1 
6500  N  ND2 . ASN B 693  ? 0.9799 1.2849 1.0685 0.1116  -0.1015 -0.1548 693  ASN B ND2 
6501  N  N   . VAL B 694  ? 0.8872 1.1189 0.9496 0.1189  -0.0770 -0.1210 694  VAL B N   
6502  C  CA  . VAL B 694  ? 0.8317 1.0491 0.8859 0.1265  -0.0743 -0.1137 694  VAL B CA  
6503  C  C   . VAL B 694  ? 0.9005 1.1020 0.9385 0.1329  -0.0755 -0.1114 694  VAL B C   
6504  O  O   . VAL B 694  ? 0.8496 1.0440 0.8824 0.1285  -0.0747 -0.1123 694  VAL B O   
6505  C  CB  . VAL B 694  ? 0.7489 0.9563 0.8069 0.1204  -0.0664 -0.1076 694  VAL B CB  
6506  C  CG1 . VAL B 694  ? 0.6799 0.9021 0.7525 0.1160  -0.0652 -0.1093 694  VAL B CG1 
6507  C  CG2 . VAL B 694  ? 0.8644 1.0613 0.9198 0.1120  -0.0622 -0.1065 694  VAL B CG2 
6508  N  N   . GLY B 695  ? 1.3247 1.5203 1.3542 0.1435  -0.0773 -0.1084 695  GLY B N   
6509  C  CA  . GLY B 695  ? 1.2668 1.4462 1.2801 0.1505  -0.0779 -0.1055 695  GLY B CA  
6510  C  C   . GLY B 695  ? 1.2880 1.4744 1.2952 0.1547  -0.0852 -0.1118 695  GLY B C   
6511  O  O   . GLY B 695  ? 1.2475 1.4521 1.2638 0.1515  -0.0900 -0.1189 695  GLY B O   
6512  N  N   . ILE B 696  ? 0.8186 0.9903 0.8100 0.1621  -0.0860 -0.1092 696  ILE B N   
6513  C  CA  . ILE B 696  ? 0.7965 0.9714 0.7790 0.1673  -0.0928 -0.1145 696  ILE B CA  
6514  C  C   . ILE B 696  ? 0.7898 0.9499 0.7628 0.1632  -0.0900 -0.1131 696  ILE B C   
6515  O  O   . ILE B 696  ? 0.7957 0.9371 0.7601 0.1641  -0.0840 -0.1062 696  ILE B O   
6516  C  CB  . ILE B 696  ? 0.8740 1.0440 0.8442 0.1811  -0.0966 -0.1128 696  ILE B CB  
6517  C  CG1 . ILE B 696  ? 0.7672 0.9486 0.7459 0.1854  -0.0980 -0.1127 696  ILE B CG1 
6518  C  CG2 . ILE B 696  ? 0.9713 1.1476 0.9334 0.1868  -0.1047 -0.1192 696  ILE B CG2 
6519  C  CD1 . ILE B 696  ? 0.7122 0.9183 0.7021 0.1855  -0.1053 -0.1211 696  ILE B CD1 
6520  N  N   . ASP B 697  ? 1.1241 1.2927 1.0987 0.1586  -0.0943 -0.1199 697  ASP B N   
6521  C  CA  . ASP B 697  ? 1.1511 1.3065 1.1171 0.1540  -0.0918 -0.1194 697  ASP B CA  
6522  C  C   . ASP B 697  ? 1.0904 1.2292 1.0372 0.1641  -0.0928 -0.1163 697  ASP B C   
6523  O  O   . ASP B 697  ? 1.1141 1.2580 1.0538 0.1730  -0.0996 -0.1198 697  ASP B O   
6524  C  CB  . ASP B 697  ? 1.1051 1.2740 1.0772 0.1469  -0.0967 -0.1280 697  ASP B CB  
6525  C  CG  . ASP B 697  ? 1.1244 1.2806 1.0917 0.1389  -0.0924 -0.1273 697  ASP B CG  
6526  O  OD1 . ASP B 697  ? 1.1856 1.3242 1.1468 0.1383  -0.0854 -0.1200 697  ASP B OD1 
6527  O  OD2 . ASP B 697  ? 1.1955 1.3594 1.1651 0.1332  -0.0961 -0.1341 697  ASP B OD2 
6528  N  N   . VAL B 698  ? 0.6815 0.8005 0.6196 0.1630  -0.0859 -0.1096 698  VAL B N   
6529  C  CA  . VAL B 698  ? 0.7138 0.8151 0.6332 0.1717  -0.0854 -0.1059 698  VAL B CA  
6530  C  C   . VAL B 698  ? 0.7949 0.8887 0.7055 0.1684  -0.0861 -0.1087 698  VAL B C   
6531  O  O   . VAL B 698  ? 0.8097 0.8908 0.7038 0.1760  -0.0872 -0.1073 698  VAL B O   
6532  C  CB  . VAL B 698  ? 0.7202 0.8036 0.6347 0.1737  -0.0771 -0.0965 698  VAL B CB  
6533  C  CG1 . VAL B 698  ? 0.8973 0.9648 0.7931 0.1849  -0.0771 -0.0927 698  VAL B CG1 
6534  C  CG2 . VAL B 698  ? 0.7327 0.8241 0.6592 0.1735  -0.0753 -0.0941 698  VAL B CG2 
6535  N  N   . TYR B 699  ? 1.0520 1.1529 0.9724 0.1575  -0.0854 -0.1127 699  TYR B N   
6536  C  CA  . TYR B 699  ? 1.0796 1.1731 0.9916 0.1538  -0.0860 -0.1157 699  TYR B CA  
6537  C  C   . TYR B 699  ? 1.0676 1.1675 0.9709 0.1600  -0.0950 -0.1228 699  TYR B C   
6538  O  O   . TYR B 699  ? 1.1281 1.2151 1.0171 0.1623  -0.0952 -0.1228 699  TYR B O   
6539  C  CB  . TYR B 699  ? 0.9451 1.0457 0.8702 0.1406  -0.0835 -0.1188 699  TYR B CB  
6540  C  CG  . TYR B 699  ? 0.8777 0.9654 0.8053 0.1347  -0.0741 -0.1116 699  TYR B CG  
6541  C  CD1 . TYR B 699  ? 0.9507 1.0187 0.8656 0.1356  -0.0689 -0.1068 699  TYR B CD1 
6542  C  CD2 . TYR B 699  ? 0.9727 1.0682 0.9152 0.1288  -0.0703 -0.1096 699  TYR B CD2 
6543  C  CE1 . TYR B 699  ? 1.0389 1.0960 0.9565 0.1307  -0.0605 -0.1004 699  TYR B CE1 
6544  C  CE2 . TYR B 699  ? 0.9351 1.0193 0.8798 0.1239  -0.0621 -0.1032 699  TYR B CE2 
6545  C  CZ  . TYR B 699  ? 0.9406 1.0061 0.8732 0.1249  -0.0573 -0.0987 699  TYR B CZ  
6546  O  OH  . TYR B 699  ? 0.9285 0.9836 0.8635 0.1204  -0.0493 -0.0924 699  TYR B OH  
6547  N  N   . PRO B 700  ? 1.0465 1.1656 0.9572 0.1629  -0.1026 -0.1289 700  PRO B N   
6548  C  CA  . PRO B 700  ? 1.1289 1.2533 1.0300 0.1698  -0.1115 -0.1356 700  PRO B CA  
6549  C  C   . PRO B 700  ? 1.0724 1.1799 0.9533 0.1824  -0.1118 -0.1310 700  PRO B C   
6550  O  O   . PRO B 700  ? 1.1266 1.2277 0.9943 0.1858  -0.1154 -0.1341 700  PRO B O   
6551  C  CB  . PRO B 700  ? 1.0637 1.2118 0.9779 0.1717  -0.1183 -0.1413 700  PRO B CB  
6552  C  CG  . PRO B 700  ? 1.0538 1.2115 0.9865 0.1605  -0.1136 -0.1410 700  PRO B CG  
6553  C  CD  . PRO B 700  ? 1.0841 1.2225 1.0131 0.1588  -0.1039 -0.1314 700  PRO B CD  
6554  N  N   . ILE B 701  ? 0.8068 0.9066 0.6845 0.1894  -0.1080 -0.1239 701  ILE B N   
6555  C  CA  . ILE B 701  ? 0.8013 0.8835 0.6592 0.2012  -0.1074 -0.1191 701  ILE B CA  
6556  C  C   . ILE B 701  ? 0.8176 0.8775 0.6644 0.1988  -0.0995 -0.1129 701  ILE B C   
6557  O  O   . ILE B 701  ? 0.8523 0.8965 0.6811 0.2075  -0.0988 -0.1097 701  ILE B O   
6558  C  CB  . ILE B 701  ? 0.6399 0.7203 0.4973 0.2095  -0.1057 -0.1136 701  ILE B CB  
6559  C  CG1 . ILE B 701  ? 0.7970 0.8620 0.6558 0.2058  -0.0952 -0.1044 701  ILE B CG1 
6560  C  CG2 . ILE B 701  ? 0.6668 0.7701 0.5405 0.2084  -0.1109 -0.1185 701  ILE B CG2 
6561  C  CD1 . ILE B 701  ? 1.0108 1.0693 0.8654 0.2145  -0.0928 -0.0984 701  ILE B CD1 
6562  N  N   . ARG B 702  ? 0.9789 1.0369 0.8355 0.1876  -0.0934 -0.1112 702  ARG B N   
6563  C  CA  . ARG B 702  ? 1.0482 1.0860 0.8950 0.1852  -0.0859 -0.1057 702  ARG B CA  
6564  C  C   . ARG B 702  ? 1.1696 1.2020 1.0036 0.1860  -0.0899 -0.1105 702  ARG B C   
6565  O  O   . ARG B 702  ? 1.2151 1.2613 1.0547 0.1817  -0.0965 -0.1188 702  ARG B O   
6566  C  CB  . ARG B 702  ? 1.0326 1.0710 0.8933 0.1732  -0.0790 -0.1032 702  ARG B CB  
6567  C  CG  . ARG B 702  ? 1.0013 1.0195 0.8553 0.1724  -0.0694 -0.0947 702  ARG B CG  
6568  C  CD  . ARG B 702  ? 0.9653 0.9844 0.8314 0.1605  -0.0638 -0.0937 702  ARG B CD  
6569  N  NE  . ARG B 702  ? 0.9969 0.9987 0.8584 0.1600  -0.0546 -0.0855 702  ARG B NE  
6570  C  CZ  . ARG B 702  ? 1.0489 1.0465 0.9165 0.1514  -0.0487 -0.0834 702  ARG B CZ  
6571  N  NH1 . ARG B 702  ? 1.0226 1.0307 0.9007 0.1422  -0.0504 -0.0886 702  ARG B NH1 
6572  N  NH2 . ARG B 702  ? 0.9654 0.9479 0.8286 0.1521  -0.0407 -0.0758 702  ARG B NH2 
6573  N  N   . THR B 703  ? 1.2222 1.2344 1.0392 0.1913  -0.0856 -0.1055 703  THR B N   
6574  C  CA  . THR B 703  ? 1.1256 1.1301 0.9273 0.1942  -0.0892 -0.1094 703  THR B CA  
6575  C  C   . THR B 703  ? 1.0878 1.0758 0.8841 0.1883  -0.0815 -0.1055 703  THR B C   
6576  O  O   . THR B 703  ? 1.0952 1.0734 0.8944 0.1858  -0.0729 -0.0981 703  THR B O   
6577  C  CB  . THR B 703  ? 1.2578 1.2521 1.0404 0.2081  -0.0920 -0.1074 703  THR B CB  
6578  O  OG1 . THR B 703  ? 1.2462 1.2257 1.0236 0.2128  -0.0840 -0.0979 703  THR B OG1 
6579  C  CG2 . THR B 703  ? 1.2612 1.2728 1.0471 0.2146  -0.1016 -0.1133 703  THR B CG2 
6580  N  N   . SER B 704  ? 1.0906 1.0758 0.8788 0.1862  -0.0849 -0.1109 704  SER B N   
6581  C  CA  . SER B 704  ? 1.0673 1.0373 0.8498 0.1806  -0.0781 -0.1081 704  SER B CA  
6582  C  C   . SER B 704  ? 1.0646 1.0127 0.8286 0.1893  -0.0722 -0.1006 704  SER B C   
6583  O  O   . SER B 704  ? 1.0218 0.9566 0.7842 0.1857  -0.0637 -0.0947 704  SER B O   
6584  C  CB  . SER B 704  ? 1.0917 1.0651 0.8709 0.1756  -0.0836 -0.1166 704  SER B CB  
6585  O  OG  . SER B 704  ? 1.1190 1.1137 0.9144 0.1686  -0.0900 -0.1243 704  SER B OG  
6586  N  N   . ASP B 705  ? 1.6194 1.5634 1.3692 0.2008  -0.0765 -0.1007 705  ASP B N   
6587  C  CA  . ASP B 705  ? 1.6560 1.5785 1.3869 0.2093  -0.0708 -0.0938 705  ASP B CA  
6588  C  C   . ASP B 705  ? 1.6456 1.5596 1.3812 0.2095  -0.0612 -0.0842 705  ASP B C   
6589  O  O   . ASP B 705  ? 1.6400 1.5371 1.3674 0.2099  -0.0530 -0.0779 705  ASP B O   
6590  C  CB  . ASP B 705  ? 1.6199 1.5404 1.3346 0.2219  -0.0776 -0.0960 705  ASP B CB  
6591  C  CG  . ASP B 705  ? 1.6643 1.6015 1.3883 0.2257  -0.0840 -0.0986 705  ASP B CG  
6592  O  OD1 . ASP B 705  ? 1.7125 1.6567 1.4517 0.2215  -0.0804 -0.0952 705  ASP B OD1 
6593  O  OD2 . ASP B 705  ? 1.7262 1.6698 1.4422 0.2333  -0.0928 -0.1041 705  ASP B OD2 
6594  N  N   . SER B 706  ? 1.5468 1.4727 1.2957 0.2090  -0.0621 -0.0832 706  SER B N   
6595  C  CA  . SER B 706  ? 1.5000 1.4201 1.2558 0.2080  -0.0536 -0.0749 706  SER B CA  
6596  C  C   . SER B 706  ? 1.3945 1.3321 1.1724 0.1996  -0.0545 -0.0766 706  SER B C   
6597  O  O   . SER B 706  ? 1.3874 1.3386 1.1718 0.2023  -0.0604 -0.0798 706  SER B O   
6598  C  CB  . SER B 706  ? 1.5649 1.4763 1.3092 0.2195  -0.0527 -0.0700 706  SER B CB  
6599  O  OG  . SER B 706  ? 1.5127 1.4076 1.2357 0.2277  -0.0519 -0.0684 706  SER B OG  
6600  N  N   . PRO B 707  ? 1.0950 1.0327 0.8843 0.1897  -0.0487 -0.0747 707  PRO B N   
6601  C  CA  . PRO B 707  ? 1.0551 1.0093 0.8648 0.1813  -0.0495 -0.0767 707  PRO B CA  
6602  C  C   . PRO B 707  ? 0.9817 0.9356 0.8005 0.1815  -0.0440 -0.0701 707  PRO B C   
6603  O  O   . PRO B 707  ? 0.9594 0.9276 0.7943 0.1761  -0.0454 -0.0719 707  PRO B O   
6604  C  CB  . PRO B 707  ? 0.9631 0.9154 0.7783 0.1710  -0.0458 -0.0778 707  PRO B CB  
6605  C  CG  . PRO B 707  ? 1.0113 0.9431 0.8116 0.1743  -0.0391 -0.0722 707  PRO B CG  
6606  C  CD  . PRO B 707  ? 1.0263 0.9488 0.8095 0.1862  -0.0412 -0.0706 707  PRO B CD  
6607  N  N   . TRP B 708  ? 1.1821 1.1203 0.9912 0.1874  -0.0378 -0.0628 708  TRP B N   
6608  C  CA  . TRP B 708  ? 1.1492 1.0861 0.9664 0.1875  -0.0323 -0.0566 708  TRP B CA  
6609  C  C   . TRP B 708  ? 1.1260 1.0567 0.9333 0.1980  -0.0329 -0.0534 708  TRP B C   
6610  O  O   . TRP B 708  ? 1.0565 0.9905 0.8720 0.1984  -0.0310 -0.0503 708  TRP B O   
6611  C  CB  . TRP B 708  ? 1.2115 1.1354 1.0293 0.1832  -0.0225 -0.0499 708  TRP B CB  
6612  C  CG  . TRP B 708  ? 1.1523 1.0782 0.9761 0.1741  -0.0209 -0.0523 708  TRP B CG  
6613  C  CD1 . TRP B 708  ? 1.1184 1.0339 0.9313 0.1736  -0.0192 -0.0528 708  TRP B CD1 
6614  C  CD2 . TRP B 708  ? 1.0705 1.0085 0.9116 0.1644  -0.0206 -0.0542 708  TRP B CD2 
6615  N  NE1 . TRP B 708  ? 1.0807 1.0009 0.9030 0.1643  -0.0179 -0.0551 708  TRP B NE1 
6616  C  CE2 . TRP B 708  ? 1.1421 1.0759 0.9815 0.1585  -0.0187 -0.0559 708  TRP B CE2 
6617  C  CE3 . TRP B 708  ? 1.0238 0.9752 0.8809 0.1604  -0.0216 -0.0547 708  TRP B CE3 
6618  C  CZ2 . TRP B 708  ? 1.1887 1.1308 1.0416 0.1489  -0.0176 -0.0578 708  TRP B CZ2 
6619  C  CZ3 . TRP B 708  ? 1.0514 1.0114 0.9219 0.1509  -0.0206 -0.0566 708  TRP B CZ3 
6620  C  CH2 . TRP B 708  ? 1.1938 1.1489 1.0620 0.1452  -0.0185 -0.0581 708  TRP B CH2 
6621  N  N   . PHE B 709  ? 1.3565 1.2777 1.1459 0.2066  -0.0354 -0.0541 709  PHE B N   
6622  C  CA  . PHE B 709  ? 1.2864 1.1994 1.0639 0.2173  -0.0356 -0.0508 709  PHE B CA  
6623  C  C   . PHE B 709  ? 1.3524 1.2742 1.1228 0.2245  -0.0457 -0.0574 709  PHE B C   
6624  O  O   . PHE B 709  ? 1.3903 1.3220 1.1623 0.2216  -0.0520 -0.0643 709  PHE B O   
6625  C  CB  . PHE B 709  ? 1.3155 1.2067 1.0758 0.2227  -0.0285 -0.0445 709  PHE B CB  
6626  C  CG  . PHE B 709  ? 1.3268 1.2091 1.0933 0.2163  -0.0185 -0.0380 709  PHE B CG  
6627  C  CD1 . PHE B 709  ? 1.3552 1.2446 1.1384 0.2104  -0.0151 -0.0354 709  PHE B CD1 
6628  C  CD2 . PHE B 709  ? 1.3768 1.2441 1.1325 0.2166  -0.0125 -0.0346 709  PHE B CD2 
6629  C  CE1 . PHE B 709  ? 1.4225 1.3047 1.2119 0.2048  -0.0063 -0.0297 709  PHE B CE1 
6630  C  CE2 . PHE B 709  ? 1.3477 1.2079 1.1098 0.2110  -0.0034 -0.0288 709  PHE B CE2 
6631  C  CZ  . PHE B 709  ? 1.3620 1.2299 1.1411 0.2051  -0.0004 -0.0265 709  PHE B CZ  
6632  N  N   . GLY B 710  ? 1.0813 0.9995 0.8436 0.2341  -0.0472 -0.0553 710  GLY B N   
6633  C  CA  . GLY B 710  ? 0.9977 0.9235 0.7521 0.2426  -0.0566 -0.0609 710  GLY B CA  
6634  C  C   . GLY B 710  ? 1.1665 1.0748 0.8988 0.2550  -0.0554 -0.0570 710  GLY B C   
6635  O  O   . GLY B 710  ? 1.2225 1.1135 0.9474 0.2568  -0.0468 -0.0495 710  GLY B O   
6636  N  N   . ALA B 711  ? 1.3758 1.2890 1.0978 0.2635  -0.0641 -0.0624 711  ALA B N   
6637  C  CA  . ALA B 711  ? 1.4616 1.3584 1.1608 0.2762  -0.0640 -0.0594 711  ALA B CA  
6638  C  C   . ALA B 711  ? 1.4022 1.3022 1.0984 0.2856  -0.0677 -0.0590 711  ALA B C   
6639  O  O   . ALA B 711  ? 1.4092 1.2975 1.1023 0.2886  -0.0611 -0.0520 711  ALA B O   
6640  C  CB  . ALA B 711  ? 1.5714 1.4683 1.2572 0.2805  -0.0710 -0.0655 711  ALA B CB  
6641  N  N   . GLY B 712  ? 1.1429 1.0586 0.8400 0.2902  -0.0782 -0.0663 712  GLY B N   
6642  C  CA  . GLY B 712  ? 1.1233 1.0431 0.8170 0.3000  -0.0826 -0.0666 712  GLY B CA  
6643  C  C   . GLY B 712  ? 1.1913 1.1368 0.9041 0.2959  -0.0904 -0.0737 712  GLY B C   
6644  O  O   . GLY B 712  ? 1.2749 1.2357 0.9968 0.2898  -0.0963 -0.0808 712  GLY B O   
6645  N  N   . ALA B 713  ? 1.2138 1.1636 0.9324 0.2993  -0.0903 -0.0717 713  ALA B N   
6646  C  CA  . ALA B 713  ? 1.2192 1.1930 0.9571 0.2952  -0.0964 -0.0774 713  ALA B CA  
6647  C  C   . ALA B 713  ? 1.1932 1.1701 0.9260 0.3067  -0.1007 -0.0775 713  ALA B C   
6648  O  O   . ALA B 713  ? 1.2863 1.2452 1.0039 0.3155  -0.0965 -0.0714 713  ALA B O   
6649  C  CB  . ALA B 713  ? 1.1967 1.1755 0.9548 0.2824  -0.0898 -0.0746 713  ALA B CB  
6650  N  N   . ARG B 714  ? 1.3149 1.3149 1.0605 0.3065  -0.1090 -0.0847 714  ARG B N   
6651  C  CA  . ARG B 714  ? 1.4482 1.4555 1.1922 0.3168  -0.1140 -0.0859 714  ARG B CA  
6652  C  C   . ARG B 714  ? 1.4181 1.4410 1.1842 0.3088  -0.1128 -0.0866 714  ARG B C   
6653  O  O   . ARG B 714  ? 1.4576 1.5006 1.2412 0.2999  -0.1167 -0.0926 714  ARG B O   
6654  C  CB  . ARG B 714  ? 1.5539 1.5763 1.2928 0.3250  -0.1257 -0.0944 714  ARG B CB  
6655  C  CG  . ARG B 714  ? 1.7179 1.7405 1.4461 0.3399  -0.1307 -0.0945 714  ARG B CG  
6656  C  CD  . ARG B 714  ? 1.7337 1.7478 1.4393 0.3526  -0.1364 -0.0964 714  ARG B CD  
6657  N  NE  . ARG B 714  ? 1.7409 1.7737 1.4516 0.3504  -0.1458 -0.1058 714  ARG B NE  
6658  C  CZ  . ARG B 714  ? 1.7650 1.8184 1.4796 0.3568  -0.1563 -0.1136 714  ARG B CZ  
6659  N  NH1 . ARG B 714  ? 1.7959 1.8545 1.5098 0.3663  -0.1591 -0.1132 714  ARG B NH1 
6660  N  NH2 . ARG B 714  ? 1.7916 1.8611 1.5113 0.3534  -0.1642 -0.1222 714  ARG B NH2 
6661  N  N   . VAL B 715  ? 1.4086 1.4217 1.1736 0.3118  -0.1073 -0.0804 715  VAL B N   
6662  C  CA  . VAL B 715  ? 1.5107 1.5352 1.2956 0.3037  -0.1047 -0.0799 715  VAL B CA  
6663  C  C   . VAL B 715  ? 1.5534 1.6014 1.3486 0.3077  -0.1135 -0.0867 715  VAL B C   
6664  O  O   . VAL B 715  ? 1.4903 1.5576 1.3053 0.2985  -0.1153 -0.0911 715  VAL B O   
6665  C  CB  . VAL B 715  ? 1.6513 1.6570 1.4313 0.3055  -0.0958 -0.0712 715  VAL B CB  
6666  C  CG1 . VAL B 715  ? 1.5401 1.5306 1.3209 0.2959  -0.0864 -0.0654 715  VAL B CG1 
6667  C  CG2 . VAL B 715  ? 1.6435 1.6326 1.4013 0.3203  -0.0964 -0.0678 715  VAL B CG2 
6668  N  N   . THR B 716  ? 1.3531 1.3996 1.1351 0.3217  -0.1187 -0.0877 716  THR B N   
6669  C  CA  . THR B 716  ? 1.3666 1.4353 1.1562 0.3276  -0.1277 -0.0945 716  THR B CA  
6670  C  C   . THR B 716  ? 1.3359 1.4182 1.1455 0.3208  -0.1257 -0.0946 716  THR B C   
6671  O  O   . THR B 716  ? 1.2908 1.3927 1.1194 0.3107  -0.1279 -0.0997 716  THR B O   
6672  C  CB  . THR B 716  ? 1.4200 1.5082 1.2153 0.3252  -0.1365 -0.1035 716  THR B CB  
6673  O  OG1 . THR B 716  ? 1.4444 1.5183 1.2209 0.3303  -0.1375 -0.1030 716  THR B OG1 
6674  C  CG2 . THR B 716  ? 1.3796 1.4892 1.1789 0.3341  -0.1465 -0.1106 716  THR B CG2 
6675  N  N   . ASN B 717  ? 1.1680 1.2391 0.9730 0.3262  -0.1214 -0.0891 717  ASN B N   
6676  C  CA  . ASN B 717  ? 1.0733 1.1568 0.8955 0.3215  -0.1201 -0.0894 717  ASN B CA  
6677  C  C   . ASN B 717  ? 1.0309 1.1398 0.8619 0.3269  -0.1297 -0.0973 717  ASN B C   
6678  O  O   . ASN B 717  ? 1.1489 1.2591 0.9673 0.3397  -0.1362 -0.0999 717  ASN B O   
6679  C  CB  . ASN B 717  ? 1.0056 1.0702 0.8192 0.3270  -0.1137 -0.0819 717  ASN B CB  
6680  C  CG  . ASN B 717  ? 1.0768 1.1538 0.9064 0.3238  -0.1129 -0.0824 717  ASN B CG  
6681  O  OD1 . ASN B 717  ? 1.1933 1.2872 1.0421 0.3129  -0.1131 -0.0858 717  ASN B OD1 
6682  N  ND2 . ASN B 717  ? 1.0242 1.0921 0.8452 0.3333  -0.1119 -0.0791 717  ASN B ND2 
6683  N  N   . THR B 718  ? 0.7420 0.8714 0.5946 0.3172  -0.1305 -0.1013 718  THR B N   
6684  C  CA  . THR B 718  ? 0.7758 0.9321 0.6400 0.3200  -0.1393 -0.1095 718  THR B CA  
6685  C  C   . THR B 718  ? 0.9098 1.0761 0.7850 0.3214  -0.1387 -0.1093 718  THR B C   
6686  O  O   . THR B 718  ? 1.0384 1.2281 0.9247 0.3237  -0.1453 -0.1160 718  THR B O   
6687  C  CB  . THR B 718  ? 0.8519 1.0271 0.7327 0.3073  -0.1418 -0.1159 718  THR B CB  
6688  O  OG1 . THR B 718  ? 0.8067 0.9828 0.7030 0.2939  -0.1347 -0.1132 718  THR B OG1 
6689  C  CG2 . THR B 718  ? 0.9203 1.0854 0.7901 0.3055  -0.1423 -0.1164 718  THR B CG2 
6690  N  N   . GLY B 719  ? 1.4746 1.6242 1.3472 0.3205  -0.1310 -0.1021 719  GLY B N   
6691  C  CA  . GLY B 719  ? 1.5189 1.6789 1.4048 0.3188  -0.1297 -0.1022 719  GLY B CA  
6692  C  C   . GLY B 719  ? 1.4751 1.6530 1.3831 0.3040  -0.1285 -0.1058 719  GLY B C   
6693  O  O   . GLY B 719  ? 1.5327 1.7038 1.4440 0.2932  -0.1238 -0.1038 719  GLY B O   
6694  N  N   . ARG B 720  ? 1.4149 1.6158 1.3378 0.3037  -0.1326 -0.1111 720  ARG B N   
6695  C  CA  . ARG B 720  ? 1.5586 1.7799 1.5026 0.2907  -0.1327 -0.1158 720  ARG B CA  
6696  C  C   . ARG B 720  ? 1.5576 1.7672 1.5081 0.2776  -0.1238 -0.1105 720  ARG B C   
6697  O  O   . ARG B 720  ? 1.5349 1.7422 1.4883 0.2681  -0.1217 -0.1108 720  ARG B O   
6698  C  CB  . ARG B 720  ? 1.5497 1.7850 1.4965 0.2880  -0.1390 -0.1228 720  ARG B CB  
6699  C  CG  . ARG B 720  ? 1.4991 1.7460 1.4387 0.3011  -0.1484 -0.1284 720  ARG B CG  
6700  C  CD  . ARG B 720  ? 1.5840 1.8535 1.5343 0.2960  -0.1551 -0.1373 720  ARG B CD  
6701  N  NE  . ARG B 720  ? 1.6565 1.9230 1.6138 0.2814  -0.1508 -0.1371 720  ARG B NE  
6702  C  CZ  . ARG B 720  ? 1.6222 1.8766 1.5687 0.2798  -0.1509 -0.1366 720  ARG B CZ  
6703  N  NH1 . ARG B 720  ? 1.6165 1.8601 1.5444 0.2915  -0.1549 -0.1360 720  ARG B NH1 
6704  N  NH2 . ARG B 720  ? 1.5707 1.8228 1.5245 0.2663  -0.1466 -0.1364 720  ARG B NH2 
6705  N  N   . THR B 721  ? 1.4929 1.6950 1.4455 0.2778  -0.1187 -0.1057 721  THR B N   
6706  C  CA  . THR B 721  ? 1.4478 1.6366 1.4046 0.2672  -0.1102 -0.1000 721  THR B CA  
6707  C  C   . THR B 721  ? 1.3781 1.5833 1.3540 0.2535  -0.1090 -0.1036 721  THR B C   
6708  O  O   . THR B 721  ? 1.3333 1.5610 1.3218 0.2522  -0.1136 -0.1098 721  THR B O   
6709  C  CB  . THR B 721  ? 1.4765 1.6551 1.4317 0.2707  -0.1058 -0.0949 721  THR B CB  
6710  O  OG1 . THR B 721  ? 1.3997 1.5696 1.3620 0.2595  -0.0982 -0.0904 721  THR B OG1 
6711  C  CG2 . THR B 721  ? 1.3651 1.5635 1.3308 0.2745  -0.1098 -0.0993 721  THR B CG2 
6712  N  N   . TYR B 722  ? 1.1107 1.3042 1.0884 0.2434  -0.1026 -0.0996 722  TYR B N   
6713  C  CA  . TYR B 722  ? 0.9628 1.1674 0.9567 0.2301  -0.1000 -0.1017 722  TYR B CA  
6714  C  C   . TYR B 722  ? 1.0175 1.2102 1.0153 0.2238  -0.0922 -0.0955 722  TYR B C   
6715  O  O   . TYR B 722  ? 1.0355 1.2077 1.0221 0.2266  -0.0878 -0.0893 722  TYR B O   
6716  C  CB  . TYR B 722  ? 0.9850 1.1880 0.9774 0.2233  -0.1003 -0.1036 722  TYR B CB  
6717  C  CG  . TYR B 722  ? 1.0183 1.2295 1.0254 0.2094  -0.0969 -0.1051 722  TYR B CG  
6718  C  CD1 . TYR B 722  ? 0.9933 1.2274 1.0156 0.2044  -0.1002 -0.1115 722  TYR B CD1 
6719  C  CD2 . TYR B 722  ? 1.0566 1.2525 1.0622 0.2014  -0.0901 -0.1000 722  TYR B CD2 
6720  C  CE1 . TYR B 722  ? 0.9529 1.1933 0.9878 0.1918  -0.0966 -0.1127 722  TYR B CE1 
6721  C  CE2 . TYR B 722  ? 1.0426 1.2450 1.0607 0.1892  -0.0869 -0.1013 722  TYR B CE2 
6722  C  CZ  . TYR B 722  ? 1.0432 1.2674 1.0755 0.1844  -0.0900 -0.1075 722  TYR B CZ  
6723  O  OH  . TYR B 722  ? 1.0804 1.3100 1.1242 0.1724  -0.0864 -0.1086 722  TYR B OH  
6724  N  N   . LEU B 723  ? 1.1381 1.3437 1.1517 0.2153  -0.0903 -0.0973 723  LEU B N   
6725  C  CA  . LEU B 723  ? 1.1032 1.3001 1.1216 0.2099  -0.0837 -0.0921 723  LEU B CA  
6726  C  C   . LEU B 723  ? 1.0633 1.2477 1.0812 0.2004  -0.0780 -0.0885 723  LEU B C   
6727  O  O   . LEU B 723  ? 1.1242 1.3173 1.1505 0.1915  -0.0778 -0.0914 723  LEU B O   
6728  C  CB  . LEU B 723  ? 1.0464 1.2619 1.0809 0.2052  -0.0839 -0.0955 723  LEU B CB  
6729  C  CG  . LEU B 723  ? 1.0774 1.2857 1.1176 0.1996  -0.0775 -0.0909 723  LEU B CG  
6730  C  CD1 . LEU B 723  ? 1.0733 1.2657 1.1031 0.2079  -0.0757 -0.0858 723  LEU B CD1 
6731  C  CD2 . LEU B 723  ? 1.0885 1.3160 1.1443 0.1951  -0.0780 -0.0946 723  LEU B CD2 
6732  N  N   . LEU B 724  ? 1.0593 1.2230 1.0672 0.2022  -0.0732 -0.0820 724  LEU B N   
6733  C  CA  . LEU B 724  ? 1.1095 1.2604 1.1171 0.1939  -0.0672 -0.0778 724  LEU B CA  
6734  C  C   . LEU B 724  ? 1.0954 1.2421 1.1103 0.1891  -0.0617 -0.0738 724  LEU B C   
6735  O  O   . LEU B 724  ? 1.1206 1.2637 1.1334 0.1948  -0.0614 -0.0719 724  LEU B O   
6736  C  CB  . LEU B 724  ? 0.9782 1.1091 0.9698 0.1989  -0.0653 -0.0734 724  LEU B CB  
6737  C  CG  . LEU B 724  ? 1.0021 1.1342 0.9860 0.2010  -0.0694 -0.0767 724  LEU B CG  
6738  C  CD1 . LEU B 724  ? 0.9730 1.0837 0.9409 0.2053  -0.0663 -0.0717 724  LEU B CD1 
6739  C  CD2 . LEU B 724  ? 1.0795 1.2221 1.0735 0.1906  -0.0694 -0.0804 724  LEU B CD2 
6740  N  N   . VAL B 725  ? 0.9723 1.1192 0.9954 0.1789  -0.0576 -0.0728 725  VAL B N   
6741  C  CA  . VAL B 725  ? 0.9359 1.0824 0.9680 0.1734  -0.0532 -0.0702 725  VAL B CA  
6742  C  C   . VAL B 725  ? 0.8984 1.0273 0.9264 0.1691  -0.0469 -0.0643 725  VAL B C   
6743  O  O   . VAL B 725  ? 0.9474 1.0712 0.9730 0.1646  -0.0452 -0.0636 725  VAL B O   
6744  C  CB  . VAL B 725  ? 0.9334 1.0975 0.9799 0.1652  -0.0537 -0.0745 725  VAL B CB  
6745  C  CG1 . VAL B 725  ? 0.9745 1.1565 1.0246 0.1693  -0.0601 -0.0808 725  VAL B CG1 
6746  C  CG2 . VAL B 725  ? 0.9689 1.1317 1.0175 0.1566  -0.0516 -0.0749 725  VAL B CG2 
6747  N  N   . SER B 726  ? 1.0556 1.1751 1.0827 0.1707  -0.0435 -0.0601 726  SER B N   
6748  C  CA  . SER B 726  ? 1.0725 1.1755 1.0961 0.1675  -0.0376 -0.0544 726  SER B CA  
6749  C  C   . SER B 726  ? 1.1312 1.2356 1.1644 0.1624  -0.0342 -0.0526 726  SER B C   
6750  O  O   . SER B 726  ? 1.1155 1.2277 1.1535 0.1648  -0.0361 -0.0543 726  SER B O   
6751  C  CB  . SER B 726  ? 1.0878 1.1748 1.0981 0.1755  -0.0366 -0.0507 726  SER B CB  
6752  O  OG  . SER B 726  ? 1.0776 1.1495 1.0857 0.1722  -0.0306 -0.0453 726  SER B OG  
6753  N  N   . THR B 727  ? 0.8957 0.9925 0.9315 0.1558  -0.0293 -0.0492 727  THR B N   
6754  C  CA  . THR B 727  ? 0.7553 0.8533 0.8002 0.1504  -0.0261 -0.0476 727  THR B CA  
6755  C  C   . THR B 727  ? 0.6584 0.7434 0.6996 0.1532  -0.0230 -0.0433 727  THR B C   
6756  O  O   . THR B 727  ? 0.7922 0.8777 0.8404 0.1494  -0.0206 -0.0420 727  THR B O   
6757  C  CB  . THR B 727  ? 0.7229 0.8204 0.7731 0.1417  -0.0225 -0.0465 727  THR B CB  
6758  O  OG1 . THR B 727  ? 0.6503 0.7350 0.6922 0.1420  -0.0199 -0.0435 727  THR B OG1 
6759  C  CG2 . THR B 727  ? 0.6491 0.7612 0.7058 0.1374  -0.0251 -0.0512 727  THR B CG2 
6760  N  N   . GLN B 728  ? 0.5913 0.6644 0.6214 0.1596  -0.0228 -0.0411 728  GLN B N   
6761  C  CA  . GLN B 728  ? 0.6501 0.7096 0.6761 0.1619  -0.0194 -0.0369 728  GLN B CA  
6762  C  C   . GLN B 728  ? 0.8806 0.9368 0.8990 0.1708  -0.0221 -0.0374 728  GLN B C   
6763  O  O   . GLN B 728  ? 1.0003 1.0542 1.0207 0.1720  -0.0214 -0.0366 728  GLN B O   
6764  C  CB  . GLN B 728  ? 0.6152 0.6596 0.6343 0.1606  -0.0148 -0.0326 728  GLN B CB  
6765  C  CG  . GLN B 728  ? 0.6092 0.6407 0.6273 0.1601  -0.0102 -0.0283 728  GLN B CG  
6766  C  CD  . GLN B 728  ? 0.6634 0.6846 0.6804 0.1554  -0.0049 -0.0243 728  GLN B CD  
6767  O  OE1 . GLN B 728  ? 0.7043 0.7305 0.7265 0.1499  -0.0040 -0.0248 728  GLN B OE1 
6768  N  NE2 . GLN B 728  ? 0.7815 0.7880 0.7918 0.1578  -0.0010 -0.0205 728  GLN B NE2 
6769  N  N   . ASP B 729  ? 0.9963 1.0515 1.0053 0.1773  -0.0252 -0.0387 729  ASP B N   
6770  C  CA  . ASP B 729  ? 1.1282 1.1813 1.1289 0.1869  -0.0285 -0.0397 729  ASP B CA  
6771  C  C   . ASP B 729  ? 1.1661 1.2008 1.1577 0.1908  -0.0247 -0.0351 729  ASP B C   
6772  O  O   . ASP B 729  ? 1.2549 1.2846 1.2373 0.1993  -0.0267 -0.0352 729  ASP B O   
6773  C  CB  . ASP B 729  ? 1.1839 1.2519 1.1927 0.1883  -0.0323 -0.0436 729  ASP B CB  
6774  C  CG  . ASP B 729  ? 1.3548 1.4411 1.3699 0.1871  -0.0370 -0.0488 729  ASP B CG  
6775  O  OD1 . ASP B 729  ? 1.3820 1.4688 1.3921 0.1882  -0.0388 -0.0499 729  ASP B OD1 
6776  O  OD2 . ASP B 729  ? 1.3208 1.4210 1.3460 0.1849  -0.0388 -0.0519 729  ASP B OD2 
6777  N  N   . HIS B 730  ? 0.9723 0.9966 0.9658 0.1850  -0.0191 -0.0312 730  HIS B N   
6778  C  CA  . HIS B 730  ? 0.9492 0.9552 0.9342 0.1877  -0.0147 -0.0267 730  HIS B CA  
6779  C  C   . HIS B 730  ? 0.9394 0.9350 0.9224 0.1828  -0.0096 -0.0230 730  HIS B C   
6780  O  O   . HIS B 730  ? 0.9327 0.9328 0.9256 0.1749  -0.0072 -0.0225 730  HIS B O   
6781  C  CB  . HIS B 730  ? 0.9114 0.9154 0.9024 0.1855  -0.0129 -0.0259 730  HIS B CB  
6782  C  CG  . HIS B 730  ? 0.9350 0.9224 0.9156 0.1910  -0.0104 -0.0229 730  HIS B CG  
6783  N  ND1 . HIS B 730  ? 0.8697 0.8538 0.8400 0.2005  -0.0135 -0.0239 730  HIS B ND1 
6784  C  CD2 . HIS B 730  ? 0.9498 0.9225 0.9286 0.1883  -0.0049 -0.0189 730  HIS B CD2 
6785  C  CE1 . HIS B 730  ? 0.8215 0.7887 0.7833 0.2034  -0.0099 -0.0205 730  HIS B CE1 
6786  N  NE2 . HIS B 730  ? 0.8809 0.8410 0.8479 0.1959  -0.0045 -0.0176 730  HIS B NE2 
6787  N  N   . TRP B 731  ? 1.0232 1.0050 0.9932 0.1879  -0.0076 -0.0202 731  TRP B N   
6788  C  CA  . TRP B 731  ? 0.9263 0.8988 0.8927 0.1846  -0.0031 -0.0170 731  TRP B CA  
6789  C  C   . TRP B 731  ? 0.9203 0.8759 0.8832 0.1832  0.0036  -0.0120 731  TRP B C   
6790  O  O   . TRP B 731  ? 0.9428 0.8887 0.9008 0.1818  0.0079  -0.0088 731  TRP B O   
6791  C  CB  . TRP B 731  ? 1.0216 0.9904 0.9753 0.1911  -0.0053 -0.0175 731  TRP B CB  
6792  C  CG  . TRP B 731  ? 1.0656 1.0503 1.0213 0.1936  -0.0122 -0.0227 731  TRP B CG  
6793  C  CD1 . TRP B 731  ? 0.9448 0.9469 0.9132 0.1892  -0.0158 -0.0268 731  TRP B CD1 
6794  C  CD2 . TRP B 731  ? 1.0585 1.0432 1.0030 0.2008  -0.0162 -0.0246 731  TRP B CD2 
6795  N  NE1 . TRP B 731  ? 0.9521 0.9655 0.9186 0.1929  -0.0217 -0.0312 731  TRP B NE1 
6796  C  CE2 . TRP B 731  ? 1.0349 1.0383 0.9870 0.2002  -0.0223 -0.0301 731  TRP B CE2 
6797  C  CE3 . TRP B 731  ? 0.9409 0.9116 0.8696 0.2079  -0.0152 -0.0223 731  TRP B CE3 
6798  C  CZ2 . TRP B 731  ? 0.9800 0.9892 0.9250 0.2062  -0.0278 -0.0336 731  TRP B CZ2 
6799  C  CZ3 . TRP B 731  ? 1.0444 1.0203 0.9652 0.2144  -0.0207 -0.0256 731  TRP B CZ3 
6800  C  CH2 . TRP B 731  ? 1.0332 1.0286 0.9625 0.2134  -0.0271 -0.0314 731  TRP B CH2 
6801  N  N   . THR B 732  ? 1.0048 0.9565 0.9698 0.1836  0.0046  -0.0113 732  THR B N   
6802  C  CA  . THR B 732  ? 1.0017 0.9372 0.9632 0.1823  0.0109  -0.0069 732  THR B CA  
6803  C  C   . THR B 732  ? 0.9919 0.9305 0.9648 0.1768  0.0121  -0.0072 732  THR B C   
6804  O  O   . THR B 732  ? 1.0465 0.9930 1.0230 0.1787  0.0080  -0.0102 732  THR B O   
6805  C  CB  . THR B 732  ? 1.0402 0.9607 0.9860 0.1912  0.0116  -0.0052 732  THR B CB  
6806  O  OG1 . THR B 732  ? 1.1782 1.1063 1.1219 0.1976  0.0056  -0.0087 732  THR B OG1 
6807  C  CG2 . THR B 732  ? 1.1260 1.0378 1.0591 0.1956  0.0129  -0.0032 732  THR B CG2 
6808  N  N   . LEU B 733  ? 1.1004 1.0331 1.0790 0.1702  0.0176  -0.0043 733  LEU B N   
6809  C  CA  . LEU B 733  ? 1.0998 1.0334 1.0882 0.1652  0.0191  -0.0044 733  LEU B CA  
6810  C  C   . LEU B 733  ? 1.2026 1.1209 1.1824 0.1691  0.0217  -0.0024 733  LEU B C   
6811  O  O   . LEU B 733  ? 1.2972 1.2005 1.2678 0.1708  0.0264  0.0011  733  LEU B O   
6812  C  CB  . LEU B 733  ? 1.1239 1.0582 1.1222 0.1567  0.0237  -0.0023 733  LEU B CB  
6813  C  CG  . LEU B 733  ? 1.1745 1.0944 1.1685 0.1547  0.0306  0.0021  733  LEU B CG  
6814  C  CD1 . LEU B 733  ? 1.0729 0.9966 1.0799 0.1462  0.0340  0.0031  733  LEU B CD1 
6815  C  CD2 . LEU B 733  ? 1.0882 1.0046 1.0733 0.1577  0.0316  0.0036  733  LEU B CD2 
6816  N  N   . GLU B 734  ? 0.9199 0.8414 0.9022 0.1707  0.0187  -0.0047 734  GLU B N   
6817  C  CA  . GLU B 734  ? 0.9366 0.8439 0.9092 0.1758  0.0201  -0.0036 734  GLU B CA  
6818  C  C   . GLU B 734  ? 0.9757 0.8725 0.9527 0.1696  0.0259  -0.0011 734  GLU B C   
6819  O  O   . GLU B 734  ? 0.9588 0.8557 0.9409 0.1676  0.0254  -0.0024 734  GLU B O   
6820  C  CB  . GLU B 734  ? 0.9965 0.9118 0.9696 0.1804  0.0145  -0.0073 734  GLU B CB  
6821  C  CG  . GLU B 734  ? 0.9943 0.9205 0.9632 0.1869  0.0087  -0.0101 734  GLU B CG  
6822  C  CD  . GLU B 734  ? 0.9789 0.8930 0.9314 0.1957  0.0090  -0.0083 734  GLU B CD  
6823  O  OE1 . GLU B 734  ? 0.9828 0.8830 0.9253 0.2007  0.0105  -0.0069 734  GLU B OE1 
6824  O  OE2 . GLU B 734  ? 1.0029 0.9207 0.9516 0.1976  0.0075  -0.0085 734  GLU B OE2 
6825  N  N   . GLY B 735  ? 1.2871 1.1745 1.2618 0.1667  0.0315  0.0025  735  GLY B N   
6826  C  CA  . GLY B 735  ? 1.2822 1.1586 1.2603 0.1610  0.0377  0.0051  735  GLY B CA  
6827  C  C   . GLY B 735  ? 1.2501 1.1365 1.2439 0.1531  0.0371  0.0032  735  GLY B C   
6828  O  O   . GLY B 735  ? 1.1545 1.0347 1.1504 0.1511  0.0386  0.0029  735  GLY B O   
6829  N  N   . ARG B 736  ? 1.1320 1.0334 1.1364 0.1489  0.0349  0.0017  736  ARG B N   
6830  C  CA  . ARG B 736  ? 1.0053 0.9174 1.0243 0.1420  0.0339  -0.0002 736  ARG B CA  
6831  C  C   . ARG B 736  ? 0.9280 0.8441 0.9555 0.1355  0.0375  0.0016  736  ARG B C   
6832  O  O   . ARG B 736  ? 0.9726 0.8850 0.9950 0.1365  0.0401  0.0040  736  ARG B O   
6833  C  CB  . ARG B 736  ? 0.9878 0.9156 1.0118 0.1436  0.0272  -0.0042 736  ARG B CB  
6834  C  CG  . ARG B 736  ? 1.0019 0.9274 1.0200 0.1493  0.0237  -0.0063 736  ARG B CG  
6835  C  CD  . ARG B 736  ? 0.9941 0.9343 1.0137 0.1529  0.0175  -0.0098 736  ARG B CD  
6836  N  NE  . ARG B 736  ? 1.1147 1.0516 1.1266 0.1599  0.0144  -0.0116 736  ARG B NE  
6837  C  CZ  . ARG B 736  ? 1.0030 0.9520 1.0165 0.1634  0.0091  -0.0150 736  ARG B CZ  
6838  N  NH1 . ARG B 736  ? 1.0009 0.9658 1.0234 0.1603  0.0063  -0.0171 736  ARG B NH1 
6839  N  NH2 . ARG B 736  ? 0.8583 0.8031 0.8641 0.1702  0.0067  -0.0163 736  ARG B NH2 
6840  N  N   . ASP B 737  ? 0.8476 0.7712 0.8878 0.1291  0.0375  0.0004  737  ASP B N   
6841  C  CA  . ASP B 737  ? 0.8726 0.8006 0.9219 0.1229  0.0408  0.0020  737  ASP B CA  
6842  C  C   . ASP B 737  ? 0.8906 0.8337 0.9458 0.1219  0.0370  0.0002  737  ASP B C   
6843  O  O   . ASP B 737  ? 0.9001 0.8530 0.9664 0.1170  0.0361  -0.0010 737  ASP B O   
6844  C  CB  . ASP B 737  ? 0.8776 0.8056 0.9374 0.1168  0.0428  0.0016  737  ASP B CB  
6845  C  CG  . ASP B 737  ? 0.8097 0.7380 0.8769 0.1112  0.0478  0.0040  737  ASP B CG  
6846  O  OD1 . ASP B 737  ? 0.9076 0.8312 0.9693 0.1125  0.0511  0.0067  737  ASP B OD1 
6847  O  OD2 . ASP B 737  ? 0.8428 0.7763 0.9212 0.1057  0.0483  0.0030  737  ASP B OD2 
6848  N  N   . ILE B 738  ? 0.9629 0.9074 1.0101 0.1266  0.0349  0.0000  738  ILE B N   
6849  C  CA  . ILE B 738  ? 0.8871 0.8446 0.9385 0.1257  0.0317  -0.0017 738  ILE B CA  
6850  C  C   . ILE B 738  ? 0.8872 0.8437 0.9396 0.1229  0.0356  0.0009  738  ILE B C   
6851  O  O   . ILE B 738  ? 0.8235 0.7893 0.8843 0.1187  0.0353  0.0003  738  ILE B O   
6852  C  CB  . ILE B 738  ? 0.8320 0.7930 0.8752 0.1319  0.0270  -0.0038 738  ILE B CB  
6853  C  CG1 . ILE B 738  ? 0.8563 0.8140 0.8952 0.1362  0.0243  -0.0054 738  ILE B CG1 
6854  C  CG2 . ILE B 738  ? 0.7284 0.7045 0.7780 0.1301  0.0230  -0.0066 738  ILE B CG2 
6855  C  CD1 . ILE B 738  ? 0.7867 0.7524 0.8355 0.1331  0.0220  -0.0079 738  ILE B CD1 
6856  N  N   . TYR B 739  ? 0.9255 0.8702 0.9686 0.1255  0.0395  0.0038  739  TYR B N   
6857  C  CA  . TYR B 739  ? 0.7690 0.7112 0.8109 0.1239  0.0434  0.0064  739  TYR B CA  
6858  C  C   . TYR B 739  ? 0.7740 0.7042 0.8153 0.1219  0.0501  0.0099  739  TYR B C   
6859  O  O   . TYR B 739  ? 0.8627 0.7814 0.8961 0.1250  0.0520  0.0112  739  TYR B O   
6860  C  CB  . TYR B 739  ? 0.8120 0.7515 0.8421 0.1294  0.0418  0.0064  739  TYR B CB  
6861  C  CG  . TYR B 739  ? 0.8257 0.7675 0.8557 0.1277  0.0437  0.0076  739  TYR B CG  
6862  C  CD1 . TYR B 739  ? 0.8940 0.8257 0.9199 0.1272  0.0497  0.0113  739  TYR B CD1 
6863  C  CD2 . TYR B 739  ? 0.8521 0.8058 0.8859 0.1265  0.0396  0.0050  739  TYR B CD2 
6864  C  CE1 . TYR B 739  ? 0.8899 0.8232 0.9151 0.1260  0.0515  0.0123  739  TYR B CE1 
6865  C  CE2 . TYR B 739  ? 0.9301 0.8849 0.9631 0.1250  0.0414  0.0059  739  TYR B CE2 
6866  C  CZ  . TYR B 739  ? 0.9147 0.8593 0.9433 0.1250  0.0472  0.0096  739  TYR B CZ  
6867  O  OH  . TYR B 739  ? 0.8501 0.7953 0.8773 0.1238  0.0490  0.0105  739  TYR B OH  
6868  N  N   . ARG B 740  ? 0.5409 0.4737 0.5904 0.1168  0.0538  0.0115  740  ARG B N   
6869  C  CA  . ARG B 740  ? 0.5681 0.4916 0.6194 0.1140  0.0605  0.0147  740  ARG B CA  
6870  C  C   . ARG B 740  ? 0.5943 0.5131 0.6409 0.1145  0.0651  0.0178  740  ARG B C   
6871  O  O   . ARG B 740  ? 0.5688 0.4956 0.6188 0.1132  0.0641  0.0173  740  ARG B O   
6872  C  CB  . ARG B 740  ? 0.5935 0.5247 0.6596 0.1076  0.0612  0.0138  740  ARG B CB  
6873  C  CG  . ARG B 740  ? 0.5815 0.5152 0.6520 0.1068  0.0576  0.0111  740  ARG B CG  
6874  C  CD  . ARG B 740  ? 0.6078 0.5462 0.6916 0.1006  0.0593  0.0106  740  ARG B CD  
6875  N  NE  . ARG B 740  ? 0.5833 0.5252 0.6715 0.0998  0.0551  0.0075  740  ARG B NE  
6876  C  CZ  . ARG B 740  ? 0.6442 0.5913 0.7437 0.0949  0.0550  0.0061  740  ARG B CZ  
6877  N  NH1 . ARG B 740  ? 0.7541 0.7043 0.8626 0.0903  0.0587  0.0074  740  ARG B NH1 
6878  N  NH2 . ARG B 740  ? 0.6079 0.5573 0.7097 0.0949  0.0511  0.0032  740  ARG B NH2 
6879  N  N   . VAL B 741  ? 0.9252 0.8301 0.9631 0.1165  0.0705  0.0209  741  VAL B N   
6880  C  CA  . VAL B 741  ? 0.8092 0.7075 0.8407 0.1177  0.0755  0.0241  741  VAL B CA  
6881  C  C   . VAL B 741  ? 0.9015 0.7904 0.9357 0.1144  0.0833  0.0274  741  VAL B C   
6882  O  O   . VAL B 741  ? 0.8829 0.7645 0.9165 0.1139  0.0851  0.0278  741  VAL B O   
6883  C  CB  . VAL B 741  ? 0.7943 0.6836 0.8091 0.1249  0.0743  0.0247  741  VAL B CB  
6884  C  CG1 . VAL B 741  ? 0.8856 0.7684 0.8934 0.1263  0.0792  0.0278  741  VAL B CG1 
6885  C  CG2 . VAL B 741  ? 0.8909 0.7902 0.9040 0.1279  0.0663  0.0210  741  VAL B CG2 
6886  N  N   . GLY B 742  ? 0.8036 0.6929 0.8408 0.1122  0.0882  0.0298  742  GLY B N   
6887  C  CA  . GLY B 742  ? 0.8204 0.7018 0.8605 0.1091  0.0962  0.0330  742  GLY B CA  
6888  C  C   . GLY B 742  ? 0.7812 0.6562 0.8140 0.1110  0.1016  0.0364  742  GLY B C   
6889  O  O   . GLY B 742  ? 0.7540 0.6301 0.7787 0.1150  0.0989  0.0361  742  GLY B O   
6890  N  N   . GLU B 743  ? 1.0762 0.9447 1.1121 0.1081  0.1095  0.0395  743  GLU B N   
6891  C  CA  . GLU B 743  ? 0.9716 0.8338 1.0018 0.1094  0.1159  0.0431  743  GLU B CA  
6892  C  C   . GLU B 743  ? 1.0205 0.8929 1.0653 0.1041  0.1191  0.0435  743  GLU B C   
6893  O  O   . GLU B 743  ? 1.1085 0.9886 1.1674 0.0988  0.1191  0.0422  743  GLU B O   
6894  C  CB  . GLU B 743  ? 1.1136 0.9589 1.1343 0.1108  0.1236  0.0468  743  GLU B CB  
6895  C  CG  . GLU B 743  ? 1.2370 1.0694 1.2381 0.1183  0.1224  0.0478  743  GLU B CG  
6896  C  CD  . GLU B 743  ? 1.4053 1.2319 1.4014 0.1203  0.1190  0.0463  743  GLU B CD  
6897  O  OE1 . GLU B 743  ? 1.4415 1.2719 1.4488 0.1154  0.1187  0.0448  743  GLU B OE1 
6898  O  OE2 . GLU B 743  ? 1.4376 1.2556 1.4184 0.1269  0.1166  0.0465  743  GLU B OE2 
6899  N  N   . PHE B 744  ? 0.7119 0.5844 0.7530 0.1059  0.1217  0.0453  744  PHE B N   
6900  C  CA  . PHE B 744  ? 0.7872 0.6696 0.8411 0.1019  0.1245  0.0458  744  PHE B CA  
6901  C  C   . PHE B 744  ? 0.9118 0.7901 0.9730 0.0979  0.1331  0.0486  744  PHE B C   
6902  O  O   . PHE B 744  ? 0.9314 0.8201 1.0077 0.0931  0.1344  0.0480  744  PHE B O   
6903  C  CB  . PHE B 744  ? 0.8659 0.7487 0.9128 0.1053  0.1250  0.0469  744  PHE B CB  
6904  C  CG  . PHE B 744  ? 0.9087 0.8020 0.9678 0.1020  0.1271  0.0472  744  PHE B CG  
6905  C  CD1 . PHE B 744  ? 0.8100 0.7172 0.8831 0.0982  0.1225  0.0443  744  PHE B CD1 
6906  C  CD2 . PHE B 744  ? 0.9453 0.8343 1.0012 0.1032  0.1338  0.0504  744  PHE B CD2 
6907  C  CE1 . PHE B 744  ? 0.8005 0.7173 0.8843 0.0958  0.1243  0.0445  744  PHE B CE1 
6908  C  CE2 . PHE B 744  ? 0.8920 0.7908 0.9589 0.1008  0.1357  0.0506  744  PHE B CE2 
6909  C  CZ  . PHE B 744  ? 0.8176 0.7303 0.8984 0.0972  0.1309  0.0477  744  PHE B CZ  
6910  N  N   . LYS B 745  ? 1.2310 1.0944 1.2815 0.0999  0.1392  0.0517  745  LYS B N   
6911  C  CA  . LYS B 745  ? 1.2475 1.1064 1.3048 0.0958  0.1481  0.0544  745  LYS B CA  
6912  C  C   . LYS B 745  ? 1.2338 1.0981 1.3048 0.0899  0.1470  0.0522  745  LYS B C   
6913  O  O   . LYS B 745  ? 1.2327 1.1031 1.3177 0.0845  0.1515  0.0525  745  LYS B O   
6914  C  CB  . LYS B 745  ? 1.3261 1.1664 1.3675 0.0995  0.1548  0.0582  745  LYS B CB  
6915  C  CG  . LYS B 745  ? 1.3760 1.2111 1.4099 0.1025  0.1610  0.0617  745  LYS B CG  
6916  C  CD  . LYS B 745  ? 1.5567 1.3732 1.5767 0.1052  0.1691  0.0658  745  LYS B CD  
6917  C  CE  . LYS B 745  ? 1.6908 1.4957 1.6937 0.1110  0.1648  0.0654  745  LYS B CE  
6918  N  NZ  . LYS B 745  ? 1.6030 1.4063 1.5920 0.1178  0.1602  0.0651  745  LYS B NZ  
6919  N  N   . LYS B 746  ? 0.9995 0.8620 1.0669 0.0909  0.1410  0.0497  746  LYS B N   
6920  C  CA  . LYS B 746  ? 1.0075 0.8752 1.0872 0.0855  0.1391  0.0470  746  LYS B CA  
6921  C  C   . LYS B 746  ? 0.9360 0.8219 1.0302 0.0826  0.1324  0.0434  746  LYS B C   
6922  O  O   . LYS B 746  ? 0.9179 0.8113 1.0263 0.0771  0.1323  0.0415  746  LYS B O   
6923  C  CB  . LYS B 746  ? 0.9599 0.8179 1.0294 0.0881  0.1355  0.0458  746  LYS B CB  
6924  C  CG  . LYS B 746  ? 0.9362 0.7750 0.9912 0.0909  0.1422  0.0494  746  LYS B CG  
6925  C  CD  . LYS B 746  ? 0.9280 0.7577 0.9732 0.0938  0.1383  0.0479  746  LYS B CD  
6926  C  CE  . LYS B 746  ? 1.2174 1.0268 1.2473 0.0969  0.1453  0.0517  746  LYS B CE  
6927  N  NZ  . LYS B 746  ? 1.2550 1.0550 1.2751 0.1001  0.1416  0.0503  746  LYS B NZ  
6928  N  N   . PHE B 747  ? 0.7602 0.6529 0.8507 0.0862  0.1269  0.0422  747  PHE B N   
6929  C  CA  . PHE B 747  ? 0.7503 0.6592 0.8531 0.0839  0.1209  0.0390  747  PHE B CA  
6930  C  C   . PHE B 747  ? 0.8116 0.7297 0.9279 0.0800  0.1252  0.0399  747  PHE B C   
6931  O  O   . PHE B 747  ? 0.8055 0.7361 0.9356 0.0763  0.1220  0.0374  747  PHE B O   
6932  C  CB  . PHE B 747  ? 0.7337 0.6462 0.8281 0.0886  0.1148  0.0379  747  PHE B CB  
6933  C  CG  . PHE B 747  ? 0.7685 0.6964 0.8738 0.0867  0.1095  0.0351  747  PHE B CG  
6934  C  CD1 . PHE B 747  ? 0.6947 0.6303 0.8055 0.0854  0.1026  0.0315  747  PHE B CD1 
6935  C  CD2 . PHE B 747  ? 0.8107 0.7449 0.9198 0.0867  0.1114  0.0362  747  PHE B CD2 
6936  C  CE1 . PHE B 747  ? 0.6503 0.5992 0.7700 0.0840  0.0980  0.0292  747  PHE B CE1 
6937  C  CE2 . PHE B 747  ? 0.6969 0.6442 0.8148 0.0854  0.1067  0.0339  747  PHE B CE2 
6938  C  CZ  . PHE B 747  ? 0.6106 0.5651 0.7337 0.0840  0.1000  0.0304  747  PHE B CZ  
6939  N  N   . LYS B 748  ? 1.2437 1.1558 1.3562 0.0810  0.1325  0.0435  748  LYS B N   
6940  C  CA  . LYS B 748  ? 1.2767 1.1977 1.4018 0.0779  0.1370  0.0445  748  LYS B CA  
6941  C  C   . LYS B 748  ? 1.3399 1.2655 1.4801 0.0716  0.1399  0.0435  748  LYS B C   
6942  O  O   . LYS B 748  ? 1.3170 1.2561 1.4719 0.0683  0.1385  0.0417  748  LYS B O   
6943  C  CB  . LYS B 748  ? 1.3302 1.2424 1.4471 0.0805  0.1449  0.0487  748  LYS B CB  
6944  C  CG  . LYS B 748  ? 1.2983 1.2104 1.4049 0.0858  0.1424  0.0494  748  LYS B CG  
6945  C  CD  . LYS B 748  ? 1.3857 1.2855 1.4802 0.0892  0.1499  0.0535  748  LYS B CD  
6946  C  CE  . LYS B 748  ? 1.2892 1.1896 1.3933 0.0858  0.1590  0.0561  748  LYS B CE  
6947  N  NZ  . LYS B 748  ? 1.2089 1.1247 1.3282 0.0833  0.1585  0.0550  748  LYS B NZ  
6948  N  N   . GLU B 749  ? 1.4280 1.3421 1.5642 0.0699  0.1438  0.0444  749  GLU B N   
6949  C  CA  . GLU B 749  ? 1.3981 1.3155 1.5483 0.0634  0.1469  0.0433  749  GLU B CA  
6950  C  C   . GLU B 749  ? 1.3639 1.2915 1.5236 0.0606  0.1388  0.0387  749  GLU B C   
6951  O  O   . GLU B 749  ? 1.4556 1.3939 1.6312 0.0555  0.1389  0.0366  749  GLU B O   
6952  C  CB  . GLU B 749  ? 1.4056 1.3064 1.5476 0.0624  0.1534  0.0456  749  GLU B CB  
6953  C  CG  . GLU B 749  ? 1.6761 1.5630 1.8023 0.0673  0.1598  0.0501  749  GLU B CG  
6954  C  CD  . GLU B 749  ? 1.7869 1.6793 1.9186 0.0670  0.1658  0.0526  749  GLU B CD  
6955  O  OE1 . GLU B 749  ? 1.7461 1.6470 1.8935 0.0616  0.1699  0.0522  749  GLU B OE1 
6956  O  OE2 . GLU B 749  ? 1.6100 1.4984 1.7304 0.0724  0.1664  0.0548  749  GLU B OE2 
6957  N  N   . ASP B 750  ? 1.1998 1.1247 1.3501 0.0642  0.1319  0.0369  750  ASP B N   
6958  C  CA  . ASP B 750  ? 1.2482 1.1821 1.4059 0.0622  0.1241  0.0326  750  ASP B CA  
6959  C  C   . ASP B 750  ? 1.1821 1.1176 1.3301 0.0675  0.1165  0.0312  750  ASP B C   
6960  O  O   . ASP B 750  ? 1.2120 1.1366 1.3463 0.0713  0.1154  0.0319  750  ASP B O   
6961  C  CB  . ASP B 750  ? 1.2428 1.1687 1.4010 0.0590  0.1249  0.0313  750  ASP B CB  
6962  C  CG  . ASP B 750  ? 1.3026 1.2391 1.4717 0.0557  0.1180  0.0267  750  ASP B CG  
6963  O  OD1 . ASP B 750  ? 1.3127 1.2630 1.4893 0.0560  0.1129  0.0247  750  ASP B OD1 
6964  O  OD2 . ASP B 750  ? 1.3914 1.3218 1.5610 0.0530  0.1178  0.0251  750  ASP B OD2 
6965  N  N   . PRO B 751  ? 0.8714 0.8203 1.0260 0.0678  0.1112  0.0292  751  PRO B N   
6966  C  CA  . PRO B 751  ? 0.8023 0.7532 0.9483 0.0722  0.1042  0.0277  751  PRO B CA  
6967  C  C   . PRO B 751  ? 0.7447 0.6949 0.8889 0.0723  0.0982  0.0246  751  PRO B C   
6968  O  O   . PRO B 751  ? 0.6340 0.5849 0.7703 0.0761  0.0928  0.0233  751  PRO B O   
6969  C  CB  . PRO B 751  ? 0.6699 0.6351 0.8251 0.0717  0.1013  0.0264  751  PRO B CB  
6970  C  CG  . PRO B 751  ? 0.7242 0.6971 0.8950 0.0665  0.1037  0.0256  751  PRO B CG  
6971  C  CD  . PRO B 751  ? 0.8462 0.8089 1.0161 0.0644  0.1115  0.0282  751  PRO B CD  
6972  N  N   . LYS B 752  ? 0.9810 0.9300 1.1323 0.0683  0.0990  0.0231  752  LYS B N   
6973  C  CA  . LYS B 752  ? 0.9921 0.9409 1.1425 0.0682  0.0933  0.0199  752  LYS B CA  
6974  C  C   . LYS B 752  ? 1.0065 0.9398 1.1457 0.0698  0.0956  0.0210  752  LYS B C   
6975  O  O   . LYS B 752  ? 0.9334 0.8647 1.0721 0.0694  0.0921  0.0185  752  LYS B O   
6976  C  CB  . LYS B 752  ? 1.0023 0.9606 1.1681 0.0627  0.0916  0.0169  752  LYS B CB  
6977  C  CG  . LYS B 752  ? 0.9711 0.9375 1.1395 0.0632  0.0835  0.0129  752  LYS B CG  
6978  C  CD  . LYS B 752  ? 0.8354 0.8117 1.0191 0.0580  0.0819  0.0099  752  LYS B CD  
6979  C  CE  . LYS B 752  ? 0.9521 0.9389 1.1467 0.0559  0.0845  0.0108  752  LYS B CE  
6980  N  NZ  . LYS B 752  ? 0.7572 0.7547 0.9668 0.0511  0.0825  0.0076  752  LYS B NZ  
6981  N  N   . TYR B 753  ? 1.0698 0.9915 1.1990 0.0722  0.1015  0.0247  753  TYR B N   
6982  C  CA  . TYR B 753  ? 1.1065 1.0123 1.2252 0.0735  0.1049  0.0261  753  TYR B CA  
6983  C  C   . TYR B 753  ? 1.1226 1.0233 1.2284 0.0792  0.0993  0.0249  753  TYR B C   
6984  O  O   . TYR B 753  ? 1.0909 0.9816 1.1907 0.0800  0.0994  0.0244  753  TYR B O   
6985  C  CB  . TYR B 753  ? 0.9942 0.8890 1.1058 0.0745  0.1133  0.0306  753  TYR B CB  
6986  C  CG  . TYR B 753  ? 0.9878 0.8738 1.0823 0.0816  0.1130  0.0328  753  TYR B CG  
6987  C  CD1 . TYR B 753  ? 0.9757 0.8682 1.0681 0.0844  0.1115  0.0336  753  TYR B CD1 
6988  C  CD2 . TYR B 753  ? 1.0556 0.9262 1.1357 0.0854  0.1143  0.0341  753  TYR B CD2 
6989  C  CE1 . TYR B 753  ? 0.9474 0.8322 1.0245 0.0907  0.1110  0.0352  753  TYR B CE1 
6990  C  CE2 . TYR B 753  ? 1.0565 0.9197 1.1211 0.0922  0.1137  0.0359  753  TYR B CE2 
6991  C  CZ  . TYR B 753  ? 0.9972 0.8677 1.0605 0.0946  0.1119  0.0363  753  TYR B CZ  
6992  O  OH  . TYR B 753  ? 0.9948 0.8580 1.0426 0.1012  0.1110  0.0378  753  TYR B OH  
6993  N  N   . ILE B 754  ? 0.9485 0.8561 1.0500 0.0833  0.0944  0.0242  754  ILE B N   
6994  C  CA  . ILE B 754  ? 0.8452 0.7498 0.9355 0.0888  0.0887  0.0227  754  ILE B CA  
6995  C  C   . ILE B 754  ? 0.8787 0.7887 0.9750 0.0872  0.0832  0.0189  754  ILE B C   
6996  O  O   . ILE B 754  ? 0.9168 0.8192 1.0048 0.0902  0.0810  0.0180  754  ILE B O   
6997  C  CB  . ILE B 754  ? 0.7595 0.6716 0.8456 0.0926  0.0848  0.0225  754  ILE B CB  
6998  C  CG1 . ILE B 754  ? 0.8154 0.7256 0.9000 0.0927  0.0903  0.0258  754  ILE B CG1 
6999  C  CG2 . ILE B 754  ? 0.7516 0.6578 0.8236 0.0991  0.0807  0.0218  754  ILE B CG2 
7000  C  CD1 . ILE B 754  ? 0.8096 0.7252 0.8887 0.0964  0.0868  0.0255  754  ILE B CD1 
7001  N  N   . ALA B 755  ? 0.8538 0.7768 0.9640 0.0827  0.0806  0.0166  755  ALA B N   
7002  C  CA  . ALA B 755  ? 0.7292 0.6577 0.8452 0.0812  0.0753  0.0128  755  ALA B CA  
7003  C  C   . ALA B 755  ? 0.8606 0.7796 0.9782 0.0779  0.0785  0.0125  755  ALA B C   
7004  O  O   . ALA B 755  ? 0.9004 0.8170 1.0157 0.0788  0.0748  0.0101  755  ALA B O   
7005  C  CB  . ALA B 755  ? 0.7707 0.7151 0.9004 0.0776  0.0720  0.0106  755  ALA B CB  
7006  N  N   . LYS B 756  ? 0.9399 0.8531 1.0612 0.0741  0.0855  0.0149  756  LYS B N   
7007  C  CA  . LYS B 756  ? 1.0114 0.9146 1.1339 0.0705  0.0891  0.0146  756  LYS B CA  
7008  C  C   . LYS B 756  ? 1.0672 0.9539 1.1736 0.0753  0.0904  0.0160  756  LYS B C   
7009  O  O   . LYS B 756  ? 1.1034 0.9828 1.2078 0.0745  0.0897  0.0144  756  LYS B O   
7010  C  CB  . LYS B 756  ? 1.0435 0.9449 1.1741 0.0651  0.0968  0.0169  756  LYS B CB  
7011  C  CG  . LYS B 756  ? 0.9417 0.8595 1.0894 0.0601  0.0953  0.0149  756  LYS B CG  
7012  C  CD  . LYS B 756  ? 0.9933 0.9103 1.1503 0.0545  0.1029  0.0167  756  LYS B CD  
7013  C  CE  . LYS B 756  ? 1.0882 1.0224 1.2623 0.0502  0.1008  0.0144  756  LYS B CE  
7014  N  NZ  . LYS B 756  ? 1.2502 1.1854 1.4350 0.0445  0.1080  0.0157  756  LYS B NZ  
7015  N  N   . GLU B 757  ? 1.5257 1.4062 1.6199 0.0808  0.0920  0.0190  757  GLU B N   
7016  C  CA  . GLU B 757  ? 1.5066 1.3742 1.5846 0.0871  0.0911  0.0198  757  GLU B CA  
7017  C  C   . GLU B 757  ? 1.5328 1.4081 1.6092 0.0908  0.0825  0.0162  757  GLU B C   
7018  O  O   . GLU B 757  ? 1.4985 1.3885 1.5856 0.0885  0.0777  0.0134  757  GLU B O   
7019  C  CB  . GLU B 757  ? 1.4979 1.3588 1.5637 0.0923  0.0942  0.0235  757  GLU B CB  
7020  C  CG  . GLU B 757  ? 1.6368 1.4883 1.7024 0.0893  0.1034  0.0273  757  GLU B CG  
7021  C  CD  . GLU B 757  ? 1.7158 1.5605 1.7687 0.0948  0.1063  0.0309  757  GLU B CD  
7022  O  OE1 . GLU B 757  ? 1.6069 1.4566 1.6532 0.1002  0.1008  0.0300  757  GLU B OE1 
7023  O  OE2 . GLU B 757  ? 1.7519 1.5865 1.8015 0.0936  0.1141  0.0344  757  GLU B OE2 
7024  N  N   . VAL B 758  ? 1.3048 1.1699 1.3674 0.0968  0.0809  0.0163  758  VAL B N   
7025  C  CA  . VAL B 758  ? 1.3313 1.2019 1.3913 0.1008  0.0734  0.0130  758  VAL B CA  
7026  C  C   . VAL B 758  ? 1.2308 1.1034 1.2996 0.0962  0.0715  0.0098  758  VAL B C   
7027  O  O   . VAL B 758  ? 1.2494 1.1132 1.3111 0.0988  0.0702  0.0086  758  VAL B O   
7028  C  CB  . VAL B 758  ? 1.2482 1.1349 1.3122 0.1026  0.0676  0.0114  758  VAL B CB  
7029  C  CG1 . VAL B 758  ? 1.1151 1.0091 1.1791 0.1054  0.0603  0.0076  758  VAL B CG1 
7030  C  CG2 . VAL B 758  ? 1.3191 1.2026 1.3722 0.1079  0.0686  0.0139  758  VAL B CG2 
7031  N  N   . TYR B 759  ? 0.9303 0.8145 1.0142 0.0898  0.0712  0.0083  759  TYR B N   
7032  C  CA  . TYR B 759  ? 0.9923 0.8794 1.0852 0.0853  0.0690  0.0049  759  TYR B CA  
7033  C  C   . TYR B 759  ? 1.0082 0.8794 1.0978 0.0826  0.0743  0.0057  759  TYR B C   
7034  O  O   . TYR B 759  ? 1.1105 0.9783 1.2008 0.0814  0.0721  0.0030  759  TYR B O   
7035  C  CB  . TYR B 759  ? 0.9385 0.8406 1.0478 0.0792  0.0679  0.0033  759  TYR B CB  
7036  C  CG  . TYR B 759  ? 0.8780 0.7956 0.9909 0.0814  0.0621  0.0018  759  TYR B CG  
7037  C  CD1 . TYR B 759  ? 0.9060 0.8262 1.0117 0.0869  0.0565  0.0001  759  TYR B CD1 
7038  C  CD2 . TYR B 759  ? 0.8813 0.8111 1.0051 0.0780  0.0625  0.0021  759  TYR B CD2 
7039  C  CE1 . TYR B 759  ? 0.9058 0.8398 1.0149 0.0885  0.0516  -0.0012 759  TYR B CE1 
7040  C  CE2 . TYR B 759  ? 0.8525 0.7952 0.9789 0.0799  0.0576  0.0009  759  TYR B CE2 
7041  C  CZ  . TYR B 759  ? 0.8984 0.8430 1.0174 0.0849  0.0523  -0.0008 759  TYR B CZ  
7042  O  OH  . TYR B 759  ? 0.7185 0.6757 0.8403 0.0863  0.0479  -0.0021 759  TYR B OH  
7043  N  N   . GLN B 760  ? 0.8626 0.7232 0.9482 0.0814  0.0816  0.0095  760  GLN B N   
7044  C  CA  . GLN B 760  ? 0.8982 0.7415 0.9783 0.0794  0.0874  0.0107  760  GLN B CA  
7045  C  C   . GLN B 760  ? 0.9383 0.7676 1.0011 0.0868  0.0861  0.0112  760  GLN B C   
7046  O  O   . GLN B 760  ? 1.0378 0.8566 1.0970 0.0860  0.0866  0.0098  760  GLN B O   
7047  C  CB  . GLN B 760  ? 0.8038 0.6395 0.8839 0.0764  0.0961  0.0147  760  GLN B CB  
7048  C  CG  . GLN B 760  ? 0.7711 0.5934 0.8527 0.0706  0.1028  0.0152  760  GLN B CG  
7049  C  CD  . GLN B 760  ? 0.9034 0.7366 1.0039 0.0615  0.1044  0.0132  760  GLN B CD  
7050  O  OE1 . GLN B 760  ? 0.9969 0.8469 1.1088 0.0598  0.1014  0.0122  760  GLN B OE1 
7051  N  NE2 . GLN B 760  ? 1.0754 0.8990 1.1792 0.0555  0.1091  0.0125  760  GLN B NE2 
7052  N  N   . GLU B 761  ? 1.1266 0.9555 1.1785 0.0941  0.0843  0.0130  761  GLU B N   
7053  C  CA  . GLU B 761  ? 1.2022 1.0189 1.2374 0.1020  0.0827  0.0135  761  GLU B CA  
7054  C  C   . GLU B 761  ? 1.2336 1.0576 1.2695 0.1049  0.0749  0.0094  761  GLU B C   
7055  O  O   . GLU B 761  ? 1.3493 1.1624 1.3732 0.1104  0.0737  0.0090  761  GLU B O   
7056  C  CB  . GLU B 761  ? 1.2794 1.0948 1.3033 0.1090  0.0828  0.0163  761  GLU B CB  
7057  C  CG  . GLU B 761  ? 1.4294 1.2334 1.4484 0.1078  0.0911  0.0209  761  GLU B CG  
7058  C  CD  . GLU B 761  ? 1.5496 1.3493 1.5544 0.1158  0.0909  0.0235  761  GLU B CD  
7059  O  OE1 . GLU B 761  ? 1.5638 1.3711 1.5642 0.1217  0.0841  0.0216  761  GLU B OE1 
7060  O  OE2 . GLU B 761  ? 1.5099 1.2987 1.5079 0.1161  0.0977  0.0274  761  GLU B OE2 
7061  N  N   . GLU B 762  ? 1.2916 1.1334 1.3407 0.1017  0.0698  0.0063  762  GLU B N   
7062  C  CA  . GLU B 762  ? 1.3163 1.1658 1.3669 0.1041  0.0626  0.0023  762  GLU B CA  
7063  C  C   . GLU B 762  ? 1.3172 1.1652 1.3758 0.0983  0.0624  -0.0006 762  GLU B C   
7064  O  O   . GLU B 762  ? 1.3805 1.2247 1.4342 0.1013  0.0589  -0.0031 762  GLU B O   
7065  C  CB  . GLU B 762  ? 1.3114 1.1807 1.3704 0.1044  0.0570  0.0006  762  GLU B CB  
7066  C  CG  . GLU B 762  ? 1.4257 1.2980 1.4767 0.1104  0.0558  0.0025  762  GLU B CG  
7067  C  CD  . GLU B 762  ? 1.4853 1.3509 1.5221 0.1189  0.0528  0.0021  762  GLU B CD  
7068  O  OE1 . GLU B 762  ? 1.5161 1.3821 1.5522 0.1207  0.0489  -0.0008 762  GLU B OE1 
7069  O  OE2 . GLU B 762  ? 1.4168 1.2768 1.4429 0.1242  0.0541  0.0045  762  GLU B OE2 
7070  N  N   . TYR B 763  ? 1.0024 0.8535 1.0733 0.0903  0.0659  -0.0006 763  TYR B N   
7071  C  CA  . TYR B 763  ? 1.0489 0.9010 1.1293 0.0842  0.0650  -0.0040 763  TYR B CA  
7072  C  C   . TYR B 763  ? 1.0268 0.8664 1.1097 0.0777  0.0723  -0.0027 763  TYR B C   
7073  O  O   . TYR B 763  ? 1.1344 0.9708 1.2222 0.0732  0.0719  -0.0056 763  TYR B O   
7074  C  CB  . TYR B 763  ? 1.0156 0.8874 1.1118 0.0798  0.0607  -0.0067 763  TYR B CB  
7075  C  CG  . TYR B 763  ? 0.9544 0.8395 1.0496 0.0851  0.0540  -0.0081 763  TYR B CG  
7076  C  CD1 . TYR B 763  ? 0.9577 0.8429 1.0472 0.0896  0.0486  -0.0109 763  TYR B CD1 
7077  C  CD2 . TYR B 763  ? 0.8713 0.7684 0.9710 0.0855  0.0533  -0.0066 763  TYR B CD2 
7078  C  CE1 . TYR B 763  ? 0.9687 0.8663 1.0578 0.0942  0.0429  -0.0122 763  TYR B CE1 
7079  C  CE2 . TYR B 763  ? 0.8568 0.7656 0.9557 0.0898  0.0475  -0.0080 763  TYR B CE2 
7080  C  CZ  . TYR B 763  ? 0.8151 0.7244 0.9090 0.0940  0.0425  -0.0108 763  TYR B CZ  
7081  O  OH  . TYR B 763  ? 0.6957 0.6170 0.7893 0.0979  0.0372  -0.0122 763  TYR B OH  
7082  N  N   . GLY B 764  ? 0.9109 0.7435 0.9909 0.0768  0.0790  0.0014  764  GLY B N   
7083  C  CA  . GLY B 764  ? 0.9661 0.7882 1.0498 0.0701  0.0865  0.0027  764  GLY B CA  
7084  C  C   . GLY B 764  ? 0.9742 0.8094 1.0758 0.0620  0.0883  0.0019  764  GLY B C   
7085  O  O   . GLY B 764  ? 1.0310 0.8591 1.1369 0.0561  0.0952  0.0033  764  GLY B O   
7086  N  N   . ARG B 765  ? 1.1331 0.9872 1.2452 0.0616  0.0824  -0.0003 765  ARG B N   
7087  C  CA  . ARG B 765  ? 1.1568 1.0249 1.2856 0.0550  0.0833  -0.0011 765  ARG B CA  
7088  C  C   . ARG B 765  ? 1.1185 0.9980 1.2485 0.0583  0.0824  0.0012  765  ARG B C   
7089  O  O   . ARG B 765  ? 1.1428 1.0215 1.2621 0.0652  0.0797  0.0026  765  ARG B O   
7090  C  CB  . ARG B 765  ? 1.2386 1.1189 1.3794 0.0513  0.0771  -0.0062 765  ARG B CB  
7091  C  CG  . ARG B 765  ? 1.2164 1.1028 1.3519 0.0572  0.0691  -0.0086 765  ARG B CG  
7092  C  CD  . ARG B 765  ? 1.0925 0.9874 1.2376 0.0537  0.0636  -0.0137 765  ARG B CD  
7093  N  NE  . ARG B 765  ? 0.9877 0.8938 1.1315 0.0586  0.0561  -0.0157 765  ARG B NE  
7094  C  CZ  . ARG B 765  ? 1.0179 0.9189 1.1517 0.0639  0.0521  -0.0172 765  ARG B CZ  
7095  N  NH1 . ARG B 765  ? 1.0828 0.9673 1.2063 0.0653  0.0545  -0.0170 765  ARG B NH1 
7096  N  NH2 . ARG B 765  ? 0.9433 0.8559 1.0773 0.0678  0.0458  -0.0190 765  ARG B NH2 
7097  N  N   . GLU B 766  ? 1.4658 1.3560 1.6091 0.0532  0.0847  0.0016  766  GLU B N   
7098  C  CA  . GLU B 766  ? 1.4893 1.3896 1.6344 0.0556  0.0847  0.0039  766  GLU B CA  
7099  C  C   . GLU B 766  ? 1.4422 1.3596 1.5941 0.0570  0.0770  0.0010  766  GLU B C   
7100  O  O   . GLU B 766  ? 1.4344 1.3604 1.5875 0.0591  0.0764  0.0026  766  GLU B O   
7101  C  CB  . GLU B 766  ? 1.5094 1.4124 1.6646 0.0501  0.0914  0.0059  766  GLU B CB  
7102  C  CG  . GLU B 766  ? 1.6891 1.6046 1.8621 0.0431  0.0899  0.0024  766  GLU B CG  
7103  C  CD  . GLU B 766  ? 1.7840 1.7041 1.9677 0.0382  0.0964  0.0044  766  GLU B CD  
7104  O  OE1 . GLU B 766  ? 1.8058 1.7169 1.9825 0.0397  0.1029  0.0086  766  GLU B OE1 
7105  O  OE2 . GLU B 766  ? 1.8242 1.7570 2.0232 0.0332  0.0949  0.0017  766  GLU B OE2 
7106  N  N   . THR B 767  ? 1.2184 1.1404 1.3742 0.0560  0.0714  -0.0031 767  THR B N   
7107  C  CA  . THR B 767  ? 1.2189 1.1566 1.3811 0.0571  0.0644  -0.0058 767  THR B CA  
7108  C  C   . THR B 767  ? 1.3000 1.2358 1.4558 0.0606  0.0584  -0.0089 767  THR B C   
7109  O  O   . THR B 767  ? 1.3885 1.3172 1.5443 0.0582  0.0583  -0.0111 767  THR B O   
7110  C  CB  . THR B 767  ? 1.1681 1.1179 1.3468 0.0509  0.0637  -0.0083 767  THR B CB  
7111  O  OG1 . THR B 767  ? 1.0764 1.0299 1.2613 0.0485  0.0689  -0.0055 767  THR B OG1 
7112  C  CG2 . THR B 767  ? 1.1449 1.1094 1.3287 0.0525  0.0563  -0.0113 767  THR B CG2 
7113  N  N   . PRO B 768  ? 1.0252 0.9671 1.1754 0.0660  0.0536  -0.0091 768  PRO B N   
7114  C  CA  . PRO B 768  ? 0.9816 0.9232 1.1263 0.0695  0.0479  -0.0121 768  PRO B CA  
7115  C  C   . PRO B 768  ? 0.9380 0.8923 1.0934 0.0668  0.0427  -0.0161 768  PRO B C   
7116  O  O   . PRO B 768  ? 1.0167 0.9838 1.1771 0.0675  0.0397  -0.0165 768  PRO B O   
7117  C  CB  . PRO B 768  ? 0.9359 0.8799 1.0713 0.0761  0.0457  -0.0105 768  PRO B CB  
7118  C  CG  . PRO B 768  ? 0.8764 0.8291 1.0175 0.0747  0.0477  -0.0083 768  PRO B CG  
7119  C  CD  . PRO B 768  ? 0.8841 0.8333 1.0327 0.0690  0.0535  -0.0068 768  PRO B CD  
7120  N  N   . ASN B 769  ? 1.2461 1.1962 1.4045 0.0637  0.0417  -0.0190 769  ASN B N   
7121  C  CA  . ASN B 769  ? 1.2344 1.1954 1.4028 0.0608  0.0369  -0.0231 769  ASN B CA  
7122  C  C   . ASN B 769  ? 1.3017 1.2671 1.4642 0.0660  0.0307  -0.0254 769  ASN B C   
7123  O  O   . ASN B 769  ? 1.4504 1.4123 1.6109 0.0663  0.0277  -0.0285 769  ASN B O   
7124  C  CB  . ASN B 769  ? 1.4226 1.3773 1.5963 0.0553  0.0382  -0.0257 769  ASN B CB  
7125  C  CG  . ASN B 769  ? 1.5110 1.4605 1.6900 0.0501  0.0451  -0.0233 769  ASN B CG  
7126  O  OD1 . ASN B 769  ? 1.4246 1.3800 1.6078 0.0496  0.0479  -0.0206 769  ASN B OD1 
7127  N  ND2 . ASN B 769  ? 1.6060 1.5440 1.7847 0.0462  0.0481  -0.0244 769  ASN B ND2 
7128  N  N   . TYR B 770  ? 1.3128 1.2859 1.4726 0.0699  0.0290  -0.0238 770  TYR B N   
7129  C  CA  . TYR B 770  ? 1.2367 1.2154 1.3919 0.0746  0.0236  -0.0258 770  TYR B CA  
7130  C  C   . TYR B 770  ? 1.1641 1.1531 1.3279 0.0723  0.0190  -0.0296 770  TYR B C   
7131  O  O   . TYR B 770  ? 1.2281 1.2262 1.4017 0.0688  0.0190  -0.0298 770  TYR B O   
7132  C  CB  . TYR B 770  ? 1.2551 1.2407 1.4069 0.0783  0.0232  -0.0235 770  TYR B CB  
7133  C  CG  . TYR B 770  ? 1.3586 1.3347 1.5004 0.0818  0.0267  -0.0202 770  TYR B CG  
7134  C  CD1 . TYR B 770  ? 1.3851 1.3482 1.5175 0.0844  0.0278  -0.0201 770  TYR B CD1 
7135  C  CD2 . TYR B 770  ? 1.3562 1.3358 1.4970 0.0828  0.0287  -0.0173 770  TYR B CD2 
7136  C  CE1 . TYR B 770  ? 1.4550 1.4093 1.5775 0.0881  0.0308  -0.0171 770  TYR B CE1 
7137  C  CE2 . TYR B 770  ? 1.3419 1.3128 1.4730 0.0862  0.0316  -0.0145 770  TYR B CE2 
7138  C  CZ  . TYR B 770  ? 1.3991 1.3576 1.5210 0.0890  0.0325  -0.0143 770  TYR B CZ  
7139  O  OH  . TYR B 770  ? 1.3090 1.2586 1.4204 0.0930  0.0352  -0.0116 770  TYR B OH  
7140  N  N   . GLN B 771  ? 0.7455 0.7329 0.9051 0.0747  0.0151  -0.0326 771  GLN B N   
7141  C  CA  . GLN B 771  ? 0.8079 0.8037 0.9738 0.0733  0.0104  -0.0364 771  GLN B CA  
7142  C  C   . GLN B 771  ? 0.8060 0.8078 0.9663 0.0787  0.0061  -0.0376 771  GLN B C   
7143  O  O   . GLN B 771  ? 0.8190 0.8148 0.9698 0.0832  0.0059  -0.0371 771  GLN B O   
7144  C  CB  . GLN B 771  ? 0.8761 0.8638 1.0431 0.0704  0.0099  -0.0395 771  GLN B CB  
7145  C  CG  . GLN B 771  ? 0.8420 0.8237 1.0151 0.0645  0.0146  -0.0385 771  GLN B CG  
7146  C  CD  . GLN B 771  ? 0.8430 0.8155 1.0166 0.0612  0.0143  -0.0417 771  GLN B CD  
7147  O  OE1 . GLN B 771  ? 0.8611 0.8319 1.0305 0.0635  0.0103  -0.0449 771  GLN B OE1 
7148  N  NE2 . GLN B 771  ? 1.0191 0.9853 1.1976 0.0558  0.0189  -0.0411 771  GLN B NE2 
7149  N  N   . SER B 772  ? 0.8602 0.8739 1.0262 0.0783  0.0027  -0.0392 772  SER B N   
7150  C  CA  . SER B 772  ? 0.8245 0.8452 0.9863 0.0827  -0.0009 -0.0403 772  SER B CA  
7151  C  C   . SER B 772  ? 0.8505 0.8751 1.0147 0.0826  -0.0053 -0.0443 772  SER B C   
7152  O  O   . SER B 772  ? 0.8981 0.9235 1.0693 0.0786  -0.0061 -0.0463 772  SER B O   
7153  C  CB  . SER B 772  ? 0.7611 0.7921 0.9260 0.0830  -0.0005 -0.0381 772  SER B CB  
7154  O  OG  . SER B 772  ? 0.6869 0.7252 0.8486 0.0866  -0.0037 -0.0394 772  SER B OG  
7155  N  N   . LEU B 773  ? 0.7531 0.7803 0.9115 0.0871  -0.0082 -0.0457 773  LEU B N   
7156  C  CA  . LEU B 773  ? 0.7169 0.7480 0.8759 0.0880  -0.0125 -0.0495 773  LEU B CA  
7157  C  C   . LEU B 773  ? 0.6718 0.7153 0.8335 0.0891  -0.0147 -0.0497 773  LEU B C   
7158  O  O   . LEU B 773  ? 0.7337 0.7811 0.8958 0.0900  -0.0182 -0.0526 773  LEU B O   
7159  C  CB  . LEU B 773  ? 0.7151 0.7398 0.8650 0.0925  -0.0141 -0.0512 773  LEU B CB  
7160  C  CG  . LEU B 773  ? 0.7013 0.7128 0.8479 0.0916  -0.0131 -0.0524 773  LEU B CG  
7161  C  CD1 . LEU B 773  ? 0.7463 0.7519 0.8829 0.0972  -0.0145 -0.0536 773  LEU B CD1 
7162  C  CD2 . LEU B 773  ? 0.7729 0.7837 0.9257 0.0872  -0.0151 -0.0557 773  LEU B CD2 
7163  N  N   . GLN B 774  ? 0.6852 0.7340 0.8481 0.0892  -0.0126 -0.0466 774  GLN B N   
7164  C  CA  . GLN B 774  ? 0.6228 0.6821 0.7874 0.0902  -0.0140 -0.0464 774  GLN B CA  
7165  C  C   . GLN B 774  ? 0.5933 0.6579 0.7659 0.0866  -0.0130 -0.0453 774  GLN B C   
7166  O  O   . GLN B 774  ? 0.5881 0.6495 0.7638 0.0839  -0.0099 -0.0431 774  GLN B O   
7167  C  CB  . GLN B 774  ? 0.5877 0.6496 0.7472 0.0931  -0.0125 -0.0442 774  GLN B CB  
7168  C  CG  . GLN B 774  ? 0.6070 0.6644 0.7587 0.0972  -0.0132 -0.0450 774  GLN B CG  
7169  C  CD  . GLN B 774  ? 0.5786 0.6379 0.7279 0.0998  -0.0167 -0.0484 774  GLN B CD  
7170  O  OE1 . GLN B 774  ? 0.5478 0.6138 0.6999 0.0993  -0.0186 -0.0498 774  GLN B OE1 
7171  N  NE2 . GLN B 774  ? 0.6549 0.7078 0.7982 0.1029  -0.0174 -0.0498 774  GLN B NE2 
7172  N  N   . PRO B 775  ? 0.6905 0.7630 0.8660 0.0867  -0.0155 -0.0466 775  PRO B N   
7173  C  CA  . PRO B 775  ? 0.7218 0.7996 0.9047 0.0839  -0.0149 -0.0458 775  PRO B CA  
7174  C  C   . PRO B 775  ? 0.7466 0.8279 0.9295 0.0840  -0.0119 -0.0421 775  PRO B C   
7175  O  O   . PRO B 775  ? 0.7025 0.7843 0.8905 0.0815  -0.0095 -0.0402 775  PRO B O   
7176  C  CB  . PRO B 775  ? 0.6963 0.7806 0.8805 0.0851  -0.0190 -0.0486 775  PRO B CB  
7177  C  CG  . PRO B 775  ? 0.6422 0.7266 0.8186 0.0890  -0.0204 -0.0495 775  PRO B CG  
7178  C  CD  . PRO B 775  ? 0.6940 0.7703 0.8658 0.0898  -0.0190 -0.0492 775  PRO B CD  
7179  N  N   . GLY B 776  ? 0.5454 0.6290 0.7224 0.0868  -0.0117 -0.0413 776  GLY B N   
7180  C  CA  . GLY B 776  ? 0.4882 0.5752 0.6646 0.0869  -0.0091 -0.0383 776  GLY B CA  
7181  C  C   . GLY B 776  ? 0.5685 0.6625 0.7482 0.0866  -0.0100 -0.0382 776  GLY B C   
7182  O  O   . GLY B 776  ? 0.6188 0.7163 0.7994 0.0875  -0.0131 -0.0406 776  GLY B O   
7183  N  N   . ASP B 777  ? 0.6748 0.7705 0.8558 0.0857  -0.0072 -0.0353 777  ASP B N   
7184  C  CA  . ASP B 777  ? 0.7389 0.8403 0.9223 0.0858  -0.0075 -0.0347 777  ASP B CA  
7185  C  C   . ASP B 777  ? 0.8480 0.9495 1.0379 0.0835  -0.0054 -0.0331 777  ASP B C   
7186  O  O   . ASP B 777  ? 0.7884 0.8853 0.9802 0.0816  -0.0032 -0.0319 777  ASP B O   
7187  C  CB  . ASP B 777  ? 0.7423 0.8459 0.9203 0.0872  -0.0058 -0.0329 777  ASP B CB  
7188  C  CG  . ASP B 777  ? 0.8150 0.9239 0.9925 0.0886  -0.0072 -0.0333 777  ASP B CG  
7189  O  OD1 . ASP B 777  ? 0.8809 0.9923 1.0620 0.0890  -0.0100 -0.0353 777  ASP B OD1 
7190  O  OD2 . ASP B 777  ? 0.8133 0.9236 0.9867 0.0894  -0.0055 -0.0318 777  ASP B OD2 
7191  N  N   . ASP B 778  ? 1.2099 1.3167 1.4031 0.0838  -0.0061 -0.0328 778  ASP B N   
7192  C  CA  . ASP B 778  ? 1.2783 1.3869 1.4790 0.0819  -0.0048 -0.0319 778  ASP B CA  
7193  C  C   . ASP B 778  ? 1.3286 1.4356 1.5282 0.0815  -0.0004 -0.0282 778  ASP B C   
7194  O  O   . ASP B 778  ? 1.3451 1.4484 1.5474 0.0795  0.0024  -0.0268 778  ASP B O   
7195  C  CB  . ASP B 778  ? 1.2630 1.3784 1.4676 0.0831  -0.0078 -0.0336 778  ASP B CB  
7196  C  CG  . ASP B 778  ? 1.4706 1.5888 1.6848 0.0809  -0.0082 -0.0345 778  ASP B CG  
7197  O  OD1 . ASP B 778  ? 1.4235 1.5378 1.6413 0.0781  -0.0059 -0.0340 778  ASP B OD1 
7198  O  OD2 . ASP B 778  ? 1.5861 1.7106 1.8044 0.0819  -0.0107 -0.0359 778  ASP B OD2 
7199  N  N   . TYR B 779  ? 0.8025 0.9117 0.9979 0.0833  0.0004  -0.0267 779  TYR B N   
7200  C  CA  . TYR B 779  ? 0.7503 0.8579 0.9440 0.0832  0.0044  -0.0233 779  TYR B CA  
7201  C  C   . TYR B 779  ? 0.8296 0.9392 1.0308 0.0820  0.0060  -0.0222 779  TYR B C   
7202  O  O   . TYR B 779  ? 0.9769 1.0830 1.1797 0.0805  0.0093  -0.0203 779  TYR B O   
7203  C  CB  . TYR B 779  ? 0.7905 0.8921 0.9795 0.0823  0.0071  -0.0218 779  TYR B CB  
7204  C  CG  . TYR B 779  ? 0.6704 0.7704 0.8534 0.0833  0.0054  -0.0233 779  TYR B CG  
7205  C  CD1 . TYR B 779  ? 0.6158 0.7181 0.7934 0.0848  0.0047  -0.0235 779  TYR B CD1 
7206  C  CD2 . TYR B 779  ? 0.7158 0.8118 0.8982 0.0828  0.0047  -0.0245 779  TYR B CD2 
7207  C  CE1 . TYR B 779  ? 0.7132 0.8151 0.8861 0.0857  0.0034  -0.0250 779  TYR B CE1 
7208  C  CE2 . TYR B 779  ? 0.6014 0.6966 0.7786 0.0841  0.0032  -0.0259 779  TYR B CE2 
7209  C  CZ  . TYR B 779  ? 0.6259 0.7245 0.7987 0.0856  0.0025  -0.0262 779  TYR B CZ  
7210  O  OH  . TYR B 779  ? 0.6524 0.7511 0.8206 0.0870  0.0011  -0.0278 779  TYR B OH  
7211  N  N   . THR B 780  ? 0.6606 0.7761 0.8663 0.0831  0.0037  -0.0234 780  THR B N   
7212  C  CA  . THR B 780  ? 0.7553 0.8745 0.9689 0.0825  0.0050  -0.0227 780  THR B CA  
7213  C  C   . THR B 780  ? 0.7863 0.9076 0.9976 0.0849  0.0068  -0.0202 780  THR B C   
7214  O  O   . THR B 780  ? 0.6894 0.8085 0.9010 0.0844  0.0107  -0.0175 780  THR B O   
7215  C  CB  . THR B 780  ? 0.6352 0.7604 0.8566 0.0820  0.0009  -0.0260 780  THR B CB  
7216  O  OG1 . THR B 780  ? 0.6986 0.8268 0.9160 0.0848  -0.0030 -0.0280 780  THR B OG1 
7217  C  CG2 . THR B 780  ? 0.6352 0.7572 0.8602 0.0789  0.0001  -0.0281 780  THR B CG2 
7218  N  N   . GLY B 781  ? 0.8609 0.9857 1.0692 0.0877  0.0042  -0.0211 781  GLY B N   
7219  C  CA  . GLY B 781  ? 0.8410 0.9670 1.0462 0.0904  0.0058  -0.0189 781  GLY B CA  
7220  C  C   . GLY B 781  ? 0.7498 0.8705 0.9448 0.0912  0.0083  -0.0168 781  GLY B C   
7221  O  O   . GLY B 781  ? 0.6887 0.8092 0.8796 0.0936  0.0098  -0.0150 781  GLY B O   
7222  N  N   . ARG B 782  ? 0.6597 0.7759 0.8504 0.0894  0.0089  -0.0170 782  ARG B N   
7223  C  CA  . ARG B 782  ? 0.6662 0.7781 0.8480 0.0897  0.0109  -0.0156 782  ARG B CA  
7224  C  C   . ARG B 782  ? 0.6159 0.7226 0.7959 0.0878  0.0147  -0.0135 782  ARG B C   
7225  O  O   . ARG B 782  ? 0.6730 0.7788 0.8581 0.0862  0.0156  -0.0132 782  ARG B O   
7226  C  CB  . ARG B 782  ? 0.6341 0.7459 0.8118 0.0896  0.0084  -0.0179 782  ARG B CB  
7227  C  CG  . ARG B 782  ? 0.6316 0.7425 0.8126 0.0877  0.0069  -0.0196 782  ARG B CG  
7228  C  CD  . ARG B 782  ? 0.6335 0.7455 0.8114 0.0885  0.0039  -0.0222 782  ARG B CD  
7229  N  NE  . ARG B 782  ? 0.5853 0.7016 0.7670 0.0898  0.0001  -0.0246 782  ARG B NE  
7230  C  CZ  . ARG B 782  ? 0.6318 0.7492 0.8124 0.0904  -0.0030 -0.0273 782  ARG B CZ  
7231  N  NH1 . ARG B 782  ? 0.5289 0.6438 0.7051 0.0900  -0.0028 -0.0280 782  ARG B NH1 
7232  N  NH2 . ARG B 782  ? 0.7752 0.8963 0.9591 0.0916  -0.0066 -0.0296 782  ARG B NH2 
7233  N  N   . ASN B 783  ? 0.6034 0.7065 0.7759 0.0879  0.0169  -0.0121 783  ASN B N   
7234  C  CA  . ASN B 783  ? 0.5625 0.6604 0.7320 0.0863  0.0201  -0.0104 783  ASN B CA  
7235  C  C   . ASN B 783  ? 0.4987 0.5952 0.6682 0.0847  0.0188  -0.0120 783  ASN B C   
7236  O  O   . ASN B 783  ? 0.5817 0.6801 0.7498 0.0849  0.0162  -0.0141 783  ASN B O   
7237  C  CB  . ASN B 783  ? 0.6722 0.7668 0.8336 0.0864  0.0225  -0.0091 783  ASN B CB  
7238  C  CG  . ASN B 783  ? 0.7963 0.8902 0.9565 0.0882  0.0246  -0.0070 783  ASN B CG  
7239  O  OD1 . ASN B 783  ? 0.8032 0.8984 0.9685 0.0890  0.0254  -0.0059 783  ASN B OD1 
7240  N  ND2 . ASN B 783  ? 0.8075 0.8991 0.9606 0.0887  0.0258  -0.0064 783  ASN B ND2 
7241  N  N   . ALA B 784  ? 0.6988 0.7916 0.8694 0.0836  0.0208  -0.0108 784  ALA B N   
7242  C  CA  . ALA B 784  ? 0.7706 0.8610 0.9403 0.0827  0.0200  -0.0119 784  ALA B CA  
7243  C  C   . ALA B 784  ? 0.8436 0.9287 1.0081 0.0822  0.0230  -0.0101 784  ALA B C   
7244  O  O   . ALA B 784  ? 0.8927 0.9747 1.0586 0.0818  0.0258  -0.0081 784  ALA B O   
7245  C  CB  . ALA B 784  ? 0.7431 0.8336 0.9195 0.0819  0.0191  -0.0127 784  ALA B CB  
7246  N  N   . TRP B 785  ? 0.5307 0.6150 0.6892 0.0821  0.0225  -0.0110 785  TRP B N   
7247  C  CA  . TRP B 785  ? 0.5178 0.5975 0.6708 0.0818  0.0249  -0.0097 785  TRP B CA  
7248  C  C   . TRP B 785  ? 0.5850 0.6611 0.7377 0.0819  0.0248  -0.0099 785  TRP B C   
7249  O  O   . TRP B 785  ? 0.5796 0.6571 0.7330 0.0823  0.0222  -0.0118 785  TRP B O   
7250  C  CB  . TRP B 785  ? 0.4726 0.5536 0.6200 0.0814  0.0243  -0.0109 785  TRP B CB  
7251  C  CG  . TRP B 785  ? 0.5117 0.5956 0.6586 0.0814  0.0244  -0.0109 785  TRP B CG  
7252  C  CD1 . TRP B 785  ? 0.5510 0.6390 0.6971 0.0815  0.0224  -0.0127 785  TRP B CD1 
7253  C  CD2 . TRP B 785  ? 0.5108 0.5930 0.6571 0.0816  0.0268  -0.0088 785  TRP B CD2 
7254  N  NE1 . TRP B 785  ? 0.5385 0.6270 0.6832 0.0817  0.0235  -0.0118 785  TRP B NE1 
7255  C  CE2 . TRP B 785  ? 0.5212 0.6062 0.6660 0.0820  0.0262  -0.0095 785  TRP B CE2 
7256  C  CE3 . TRP B 785  ? 0.5566 0.6351 0.7032 0.0819  0.0297  -0.0064 785  TRP B CE3 
7257  C  CZ2 . TRP B 785  ? 0.6654 0.7491 0.8085 0.0828  0.0281  -0.0078 785  TRP B CZ2 
7258  C  CZ3 . TRP B 785  ? 0.5987 0.6766 0.7442 0.0827  0.0316  -0.0048 785  TRP B CZ3 
7259  C  CH2 . TRP B 785  ? 0.6829 0.7632 0.8264 0.0832  0.0307  -0.0055 785  TRP B CH2 
7260  N  N   . GLY B 786  ? 0.9961 1.0670 1.1471 0.0818  0.0278  -0.0077 786  GLY B N   
7261  C  CA  . GLY B 786  ? 0.8888 0.9549 1.0382 0.0823  0.0283  -0.0074 786  GLY B CA  
7262  C  C   . GLY B 786  ? 0.8772 0.9380 1.0203 0.0827  0.0309  -0.0057 786  GLY B C   
7263  O  O   . GLY B 786  ? 0.9290 0.9893 1.0700 0.0823  0.0329  -0.0045 786  GLY B O   
7264  N  N   . MET B 787  ? 0.4471 0.5033 0.5866 0.0837  0.0310  -0.0057 787  MET B N   
7265  C  CA  . MET B 787  ? 0.4080 0.4588 0.5405 0.0846  0.0329  -0.0045 787  MET B CA  
7266  C  C   . MET B 787  ? 0.3981 0.4420 0.5293 0.0856  0.0349  -0.0030 787  MET B C   
7267  O  O   . MET B 787  ? 0.3701 0.4134 0.5035 0.0860  0.0336  -0.0038 787  MET B O   
7268  C  CB  . MET B 787  ? 0.4562 0.5089 0.5831 0.0853  0.0302  -0.0068 787  MET B CB  
7269  C  CG  . MET B 787  ? 0.4262 0.4740 0.5455 0.0863  0.0316  -0.0061 787  MET B CG  
7270  S  SD  . MET B 787  ? 0.5748 0.6272 0.6893 0.0865  0.0282  -0.0093 787  MET B SD  
7271  C  CE  . MET B 787  ? 0.4707 0.5296 0.5889 0.0837  0.0280  -0.0102 787  MET B CE  
7272  N  N   . THR B 788  ? 0.7229 0.7610 0.8497 0.0862  0.0383  -0.0007 788  THR B N   
7273  C  CA  . THR B 788  ? 0.7088 0.7393 0.8332 0.0873  0.0410  0.0012  788  THR B CA  
7274  C  C   . THR B 788  ? 0.7064 0.7313 0.8211 0.0893  0.0418  0.0018  788  THR B C   
7275  O  O   . THR B 788  ? 0.7211 0.7462 0.8326 0.0890  0.0428  0.0022  788  THR B O   
7276  C  CB  . THR B 788  ? 0.7235 0.7521 0.8531 0.0861  0.0453  0.0038  788  THR B CB  
7277  O  OG1 . THR B 788  ? 0.9129 0.9484 1.0517 0.0842  0.0440  0.0029  788  THR B OG1 
7278  C  CG2 . THR B 788  ? 0.8267 0.8478 0.9552 0.0867  0.0482  0.0055  788  THR B CG2 
7279  N  N   . ILE B 789  ? 0.5154 0.5349 0.6249 0.0915  0.0414  0.0017  789  ILE B N   
7280  C  CA  . ILE B 789  ? 0.5791 0.5930 0.6787 0.0941  0.0417  0.0020  789  ILE B CA  
7281  C  C   . ILE B 789  ? 0.6258 0.6300 0.7218 0.0955  0.0460  0.0051  789  ILE B C   
7282  O  O   . ILE B 789  ? 0.7021 0.7027 0.7991 0.0961  0.0466  0.0055  789  ILE B O   
7283  C  CB  . ILE B 789  ? 0.5199 0.5358 0.6151 0.0963  0.0372  -0.0007 789  ILE B CB  
7284  C  CG1 . ILE B 789  ? 0.5311 0.5571 0.6314 0.0946  0.0334  -0.0037 789  ILE B CG1 
7285  C  CG2 . ILE B 789  ? 0.3893 0.4011 0.4746 0.0989  0.0369  -0.0009 789  ILE B CG2 
7286  C  CD1 . ILE B 789  ? 0.4694 0.4990 0.5660 0.0968  0.0291  -0.0066 789  ILE B CD1 
7287  N  N   . ASN B 790  ? 0.6381 0.6376 0.7294 0.0960  0.0494  0.0071  790  ASN B N   
7288  C  CA  . ASN B 790  ? 0.6166 0.6066 0.7038 0.0974  0.0542  0.0102  790  ASN B CA  
7289  C  C   . ASN B 790  ? 0.7029 0.6858 0.7783 0.1013  0.0532  0.0100  790  ASN B C   
7290  O  O   . ASN B 790  ? 0.6825 0.6654 0.7514 0.1026  0.0519  0.0091  790  ASN B O   
7291  C  CB  . ASN B 790  ? 0.6448 0.6332 0.7327 0.0963  0.0586  0.0126  790  ASN B CB  
7292  C  CG  . ASN B 790  ? 0.6721 0.6524 0.7593 0.0969  0.0644  0.0160  790  ASN B CG  
7293  O  OD1 . ASN B 790  ? 0.6258 0.6016 0.7129 0.0974  0.0653  0.0166  790  ASN B OD1 
7294  N  ND2 . ASN B 790  ? 0.8471 0.8251 0.9336 0.0967  0.0685  0.0182  790  ASN B ND2 
7295  N  N   . LEU B 791  ? 0.8496 0.8265 0.9223 0.1032  0.0538  0.0107  791  LEU B N   
7296  C  CA  . LEU B 791  ? 0.7555 0.7253 0.8165 0.1077  0.0527  0.0106  791  LEU B CA  
7297  C  C   . LEU B 791  ? 0.7249 0.6855 0.7771 0.1097  0.0570  0.0133  791  LEU B C   
7298  O  O   . LEU B 791  ? 0.6947 0.6511 0.7364 0.1135  0.0554  0.0127  791  LEU B O   
7299  C  CB  . LEU B 791  ? 0.6733 0.6379 0.7329 0.1095  0.0526  0.0108  791  LEU B CB  
7300  C  CG  . LEU B 791  ? 0.6841 0.6566 0.7499 0.1086  0.0478  0.0078  791  LEU B CG  
7301  C  CD1 . LEU B 791  ? 0.8269 0.7923 0.8908 0.1103  0.0485  0.0084  791  LEU B CD1 
7302  C  CD2 . LEU B 791  ? 0.6693 0.6484 0.7312 0.1107  0.0422  0.0045  791  LEU B CD2 
7303  N  N   . ASN B 792  ? 0.8890 0.8469 0.9453 0.1076  0.0624  0.0162  792  ASN B N   
7304  C  CA  . ASN B 792  ? 0.9481 0.8974 0.9963 0.1095  0.0670  0.0190  792  ASN B CA  
7305  C  C   . ASN B 792  ? 1.0638 1.0160 1.1077 0.1098  0.0653  0.0177  792  ASN B C   
7306  O  O   . ASN B 792  ? 1.0408 0.9855 1.0757 0.1122  0.0681  0.0194  792  ASN B O   
7307  C  CB  . ASN B 792  ? 1.1138 1.0606 1.1686 0.1070  0.0735  0.0223  792  ASN B CB  
7308  C  CG  . ASN B 792  ? 1.1259 1.0629 1.1778 0.1082  0.0778  0.0248  792  ASN B CG  
7309  O  OD1 . ASN B 792  ? 1.1793 1.1175 1.2403 0.1052  0.0804  0.0257  792  ASN B OD1 
7310  N  ND2 . ASN B 792  ? 1.1306 1.0575 1.1694 0.1126  0.0787  0.0259  792  ASN B ND2 
7311  N  N   . ALA B 793  ? 0.7850 0.7472 0.8347 0.1075  0.0610  0.0148  793  ALA B N   
7312  C  CA  . ALA B 793  ? 0.7021 0.6670 0.7482 0.1071  0.0595  0.0134  793  ALA B CA  
7313  C  C   . ALA B 793  ? 0.6850 0.6542 0.7264 0.1083  0.0535  0.0096  793  ALA B C   
7314  O  O   . ALA B 793  ? 0.7100 0.6795 0.7461 0.1085  0.0522  0.0082  793  ALA B O   
7315  C  CB  . ALA B 793  ? 0.6574 0.6298 0.7133 0.1031  0.0602  0.0132  793  ALA B CB  
7316  N  N   . CYS B 794  ? 0.7120 0.6848 0.7554 0.1092  0.0497  0.0077  794  CYS B N   
7317  C  CA  . CYS B 794  ? 0.7768 0.7552 0.8168 0.1105  0.0440  0.0038  794  CYS B CA  
7318  C  C   . CYS B 794  ? 0.7974 0.7684 0.8247 0.1152  0.0432  0.0037  794  CYS B C   
7319  O  O   . CYS B 794  ? 0.8465 0.8089 0.8681 0.1186  0.0455  0.0059  794  CYS B O   
7320  C  CB  . CYS B 794  ? 0.7566 0.7410 0.8023 0.1106  0.0404  0.0019  794  CYS B CB  
7321  S  SG  . CYS B 794  ? 0.7967 0.7908 0.8409 0.1115  0.0334  -0.0031 794  CYS B SG  
7322  N  N   . ILE B 795  ? 0.6079 0.5821 0.6306 0.1154  0.0400  0.0009  795  ILE B N   
7323  C  CA  . ILE B 795  ? 0.5676 0.5361 0.5781 0.1198  0.0384  0.0000  795  ILE B CA  
7324  C  C   . ILE B 795  ? 0.5895 0.5662 0.5986 0.1213  0.0318  -0.0046 795  ILE B C   
7325  O  O   . ILE B 795  ? 0.6691 0.6427 0.6685 0.1252  0.0295  -0.0061 795  ILE B O   
7326  C  CB  . ILE B 795  ? 0.5380 0.5011 0.5422 0.1193  0.0411  0.0008  795  ILE B CB  
7327  C  CG1 . ILE B 795  ? 0.6078 0.5795 0.6175 0.1146  0.0390  -0.0020 795  ILE B CG1 
7328  C  CG2 . ILE B 795  ? 0.5347 0.4893 0.5393 0.1189  0.0479  0.0056  795  ILE B CG2 
7329  C  CD1 . ILE B 795  ? 0.5883 0.5545 0.5915 0.1139  0.0414  -0.0016 795  ILE B CD1 
7330  N  N   . GLY B 796  ? 0.8883 0.8757 0.9070 0.1184  0.0288  -0.0071 796  GLY B N   
7331  C  CA  . GLY B 796  ? 0.7881 0.7844 0.8066 0.1197  0.0228  -0.0115 796  GLY B CA  
7332  C  C   . GLY B 796  ? 0.7557 0.7573 0.7723 0.1175  0.0201  -0.0151 796  GLY B C   
7333  O  O   . GLY B 796  ? 0.7711 0.7777 0.7841 0.1199  0.0153  -0.0187 796  GLY B O   
7334  N  N   . CYS B 797  ? 0.8338 0.8347 0.8529 0.1131  0.0230  -0.0142 797  CYS B N   
7335  C  CA  . CYS B 797  ? 0.8590 0.8638 0.8761 0.1105  0.0209  -0.0176 797  CYS B CA  
7336  C  C   . CYS B 797  ? 0.9105 0.9283 0.9353 0.1071  0.0168  -0.0219 797  CYS B C   
7337  O  O   . CYS B 797  ? 0.9562 0.9784 0.9795 0.1049  0.0144  -0.0254 797  CYS B O   
7338  C  CB  . CYS B 797  ? 0.8492 0.8486 0.8663 0.1068  0.0256  -0.0153 797  CYS B CB  
7339  S  SG  . CYS B 797  ? 1.0010 1.0037 1.0301 0.1024  0.0292  -0.0126 797  CYS B SG  
7340  N  N   . ASN B 798  ? 0.9724 0.9964 1.0055 0.1066  0.0160  -0.0217 798  ASN B N   
7341  C  CA  . ASN B 798  ? 0.8942 0.9307 0.9348 0.1039  0.0124  -0.0256 798  ASN B CA  
7342  C  C   . ASN B 798  ? 0.7469 0.7874 0.7920 0.0977  0.0137  -0.0268 798  ASN B C   
7343  O  O   . ASN B 798  ? 0.7267 0.7767 0.7756 0.0950  0.0108  -0.0308 798  ASN B O   
7344  C  CB  . ASN B 798  ? 0.9390 0.9818 0.9760 0.1070  0.0070  -0.0298 798  ASN B CB  
7345  C  CG  . ASN B 798  ? 0.8862 0.9286 0.9216 0.1128  0.0049  -0.0293 798  ASN B CG  
7346  O  OD1 . ASN B 798  ? 0.8329 0.8761 0.8740 0.1128  0.0060  -0.0275 798  ASN B OD1 
7347  N  ND2 . ASN B 798  ? 0.9102 0.9512 0.9375 0.1179  0.0018  -0.0310 798  ASN B ND2 
7348  N  N   . ALA B 799  ? 0.8792 0.9123 0.9238 0.0956  0.0183  -0.0235 799  ALA B N   
7349  C  CA  . ALA B 799  ? 0.8910 0.9265 0.9392 0.0902  0.0201  -0.0242 799  ALA B CA  
7350  C  C   . ALA B 799  ? 0.8726 0.9148 0.9305 0.0875  0.0205  -0.0239 799  ALA B C   
7351  O  O   . ALA B 799  ? 0.9313 0.9791 0.9930 0.0832  0.0204  -0.0259 799  ALA B O   
7352  C  CB  . ALA B 799  ? 0.8995 0.9246 0.9430 0.0895  0.0248  -0.0209 799  ALA B CB  
7353  N  N   . CYS B 800  ? 0.6531 0.6945 0.7147 0.0898  0.0212  -0.0214 800  CYS B N   
7354  C  CA  . CYS B 800  ? 0.6668 0.7144 0.7371 0.0877  0.0214  -0.0211 800  CYS B CA  
7355  C  C   . CYS B 800  ? 0.5917 0.6501 0.6661 0.0871  0.0173  -0.0251 800  CYS B C   
7356  O  O   . CYS B 800  ? 0.5590 0.6236 0.6395 0.0841  0.0173  -0.0260 800  CYS B O   
7357  C  CB  . CYS B 800  ? 0.7904 0.8341 0.8634 0.0903  0.0229  -0.0178 800  CYS B CB  
7358  S  SG  . CYS B 800  ? 0.6477 0.6871 0.7150 0.0961  0.0210  -0.0175 800  CYS B SG  
7359  N  N   . VAL B 801  ? 0.4678 0.5287 0.5386 0.0903  0.0138  -0.0275 801  VAL B N   
7360  C  CA  . VAL B 801  ? 0.5076 0.5796 0.5825 0.0902  0.0098  -0.0315 801  VAL B CA  
7361  C  C   . VAL B 801  ? 0.5303 0.6088 0.6070 0.0853  0.0093  -0.0348 801  VAL B C   
7362  O  O   . VAL B 801  ? 0.5592 0.6464 0.6421 0.0826  0.0085  -0.0369 801  VAL B O   
7363  C  CB  . VAL B 801  ? 0.4925 0.5656 0.5629 0.0955  0.0061  -0.0332 801  VAL B CB  
7364  C  CG1 . VAL B 801  ? 0.5159 0.6009 0.5914 0.0962  0.0022  -0.0369 801  VAL B CG1 
7365  C  CG2 . VAL B 801  ? 0.5686 0.6327 0.6357 0.1000  0.0075  -0.0295 801  VAL B CG2 
7366  N  N   . VAL B 802  ? 0.7625 0.8363 0.8332 0.0840  0.0100  -0.0354 802  VAL B N   
7367  C  CA  . VAL B 802  ? 0.8321 0.9110 0.9040 0.0789  0.0098  -0.0388 802  VAL B CA  
7368  C  C   . VAL B 802  ? 0.8758 0.9528 0.9513 0.0742  0.0137  -0.0369 802  VAL B C   
7369  O  O   . VAL B 802  ? 0.8603 0.9437 0.9397 0.0697  0.0138  -0.0394 802  VAL B O   
7370  C  CB  . VAL B 802  ? 0.7733 0.8467 0.8370 0.0788  0.0093  -0.0401 802  VAL B CB  
7371  C  CG1 . VAL B 802  ? 0.8997 0.9782 0.9646 0.0731  0.0089  -0.0441 802  VAL B CG1 
7372  C  CG2 . VAL B 802  ? 0.7831 0.8578 0.8423 0.0843  0.0052  -0.0418 802  VAL B CG2 
7373  N  N   . ALA B 803  ? 0.9374 1.0059 1.0119 0.0752  0.0172  -0.0325 803  ALA B N   
7374  C  CA  . ALA B 803  ? 0.9242 0.9913 1.0022 0.0717  0.0207  -0.0305 803  ALA B CA  
7375  C  C   . ALA B 803  ? 0.9114 0.9868 0.9971 0.0711  0.0197  -0.0312 803  ALA B C   
7376  O  O   . ALA B 803  ? 1.0326 1.1113 1.1213 0.0672  0.0211  -0.0319 803  ALA B O   
7377  C  CB  . ALA B 803  ? 0.8828 0.9400 0.9585 0.0736  0.0242  -0.0258 803  ALA B CB  
7378  N  N   . CYS B 804  ? 0.4384 0.5169 0.5268 0.0749  0.0174  -0.0308 804  CYS B N   
7379  C  CA  . CYS B 804  ? 0.4963 0.5826 0.5914 0.0747  0.0162  -0.0317 804  CYS B CA  
7380  C  C   . CYS B 804  ? 0.5056 0.6021 0.6034 0.0723  0.0139  -0.0361 804  CYS B C   
7381  O  O   . CYS B 804  ? 0.5283 0.6305 0.6308 0.0697  0.0146  -0.0370 804  CYS B O   
7382  C  CB  . CYS B 804  ? 0.6092 0.6955 0.7055 0.0796  0.0142  -0.0307 804  CYS B CB  
7383  S  SG  . CYS B 804  ? 0.4197 0.5136 0.5236 0.0799  0.0130  -0.0312 804  CYS B SG  
7384  N  N   . GLN B 805  ? 0.4640 0.5633 0.5588 0.0730  0.0113  -0.0391 805  GLN B N   
7385  C  CA  . GLN B 805  ? 0.5001 0.6100 0.5981 0.0704  0.0091  -0.0437 805  GLN B CA  
7386  C  C   . GLN B 805  ? 0.6007 0.7104 0.6990 0.0641  0.0120  -0.0446 805  GLN B C   
7387  O  O   . GLN B 805  ? 0.5468 0.6646 0.6500 0.0608  0.0122  -0.0470 805  GLN B O   
7388  C  CB  . GLN B 805  ? 0.5819 0.6947 0.6763 0.0729  0.0054  -0.0467 805  GLN B CB  
7389  C  CG  . GLN B 805  ? 0.6092 0.7357 0.7086 0.0722  0.0019  -0.0516 805  GLN B CG  
7390  C  CD  . GLN B 805  ? 0.6202 0.7501 0.7166 0.0775  -0.0026 -0.0539 805  GLN B CD  
7391  O  OE1 . GLN B 805  ? 0.7835 0.9049 0.8732 0.0811  -0.0030 -0.0521 805  GLN B OE1 
7392  N  NE2 . GLN B 805  ? 0.5756 0.7182 0.6770 0.0782  -0.0059 -0.0580 805  GLN B NE2 
7393  N  N   . ALA B 806  ? 0.6533 0.7533 0.7460 0.0625  0.0147  -0.0428 806  ALA B N   
7394  C  CA  . ALA B 806  ? 0.6455 0.7436 0.7373 0.0566  0.0177  -0.0436 806  ALA B CA  
7395  C  C   . ALA B 806  ? 0.6587 0.7549 0.7534 0.0548  0.0212  -0.0409 806  ALA B C   
7396  O  O   . ALA B 806  ? 0.5714 0.6688 0.6669 0.0500  0.0235  -0.0421 806  ALA B O   
7397  C  CB  . ALA B 806  ? 0.6414 0.7289 0.7255 0.0560  0.0194  -0.0425 806  ALA B CB  
7398  N  N   . GLU B 807  ? 0.4809 0.5738 0.5769 0.0585  0.0217  -0.0373 807  GLU B N   
7399  C  CA  . GLU B 807  ? 0.4418 0.5327 0.5401 0.0574  0.0246  -0.0347 807  GLU B CA  
7400  C  C   . GLU B 807  ? 0.4561 0.5563 0.5606 0.0574  0.0233  -0.0361 807  GLU B C   
7401  O  O   . GLU B 807  ? 0.4377 0.5385 0.5438 0.0549  0.0257  -0.0356 807  GLU B O   
7402  C  CB  . GLU B 807  ? 0.4438 0.5269 0.5408 0.0612  0.0259  -0.0304 807  GLU B CB  
7403  C  CG  . GLU B 807  ? 0.5350 0.6171 0.6351 0.0612  0.0280  -0.0278 807  GLU B CG  
7404  C  CD  . GLU B 807  ? 0.5156 0.5908 0.6119 0.0585  0.0320  -0.0260 807  GLU B CD  
7405  O  OE1 . GLU B 807  ? 0.4906 0.5599 0.5816 0.0570  0.0334  -0.0261 807  GLU B OE1 
7406  O  OE2 . GLU B 807  ? 0.5608 0.6359 0.6589 0.0580  0.0337  -0.0246 807  GLU B OE2 
7407  N  N   . ASN B 808  ? 0.5415 0.6487 0.6492 0.0605  0.0197  -0.0379 808  ASN B N   
7408  C  CA  . ASN B 808  ? 0.5188 0.6339 0.6321 0.0616  0.0184  -0.0388 808  ASN B CA  
7409  C  C   . ASN B 808  ? 0.5324 0.6587 0.6491 0.0601  0.0162  -0.0433 808  ASN B C   
7410  O  O   . ASN B 808  ? 0.5535 0.6872 0.6744 0.0623  0.0142  -0.0445 808  ASN B O   
7411  C  CB  . ASN B 808  ? 0.4899 0.6037 0.6043 0.0669  0.0163  -0.0370 808  ASN B CB  
7412  C  CG  . ASN B 808  ? 0.4607 0.5652 0.5735 0.0681  0.0186  -0.0328 808  ASN B CG  
7413  O  OD1 . ASN B 808  ? 0.5123 0.6097 0.6215 0.0695  0.0192  -0.0309 808  ASN B OD1 
7414  N  ND2 . ASN B 808  ? 0.4983 0.6032 0.6139 0.0675  0.0201  -0.0314 808  ASN B ND2 
7415  N  N   . ASN B 809  ? 0.4202 0.5482 0.5353 0.0564  0.0165  -0.0460 809  ASN B N   
7416  C  CA  . ASN B 809  ? 0.3977 0.5372 0.5168 0.0538  0.0149  -0.0506 809  ASN B CA  
7417  C  C   . ASN B 809  ? 0.3498 0.4978 0.4720 0.0587  0.0104  -0.0527 809  ASN B C   
7418  O  O   . ASN B 809  ? 0.3706 0.5293 0.4981 0.0585  0.0092  -0.0555 809  ASN B O   
7419  C  CB  . ASN B 809  ? 0.4331 0.5770 0.5561 0.0500  0.0178  -0.0510 809  ASN B CB  
7420  C  CG  . ASN B 809  ? 0.4332 0.5684 0.5524 0.0453  0.0224  -0.0492 809  ASN B CG  
7421  O  OD1 . ASN B 809  ? 0.4458 0.5735 0.5600 0.0438  0.0233  -0.0486 809  ASN B OD1 
7422  N  ND2 . ASN B 809  ? 0.5666 0.7025 0.6875 0.0431  0.0255  -0.0482 809  ASN B ND2 
7423  N  N   . ILE B 810  ? 0.3826 0.5256 0.5010 0.0634  0.0081  -0.0514 810  ILE B N   
7424  C  CA  . ILE B 810  ? 0.3893 0.5384 0.5091 0.0688  0.0039  -0.0530 810  ILE B CA  
7425  C  C   . ILE B 810  ? 0.4471 0.6061 0.5683 0.0679  0.0010  -0.0579 810  ILE B C   
7426  O  O   . ILE B 810  ? 0.5316 0.6883 0.6494 0.0654  0.0009  -0.0593 810  ILE B O   
7427  C  CB  . ILE B 810  ? 0.4308 0.5702 0.5452 0.0739  0.0029  -0.0499 810  ILE B CB  
7428  C  CG1 . ILE B 810  ? 0.3866 0.5177 0.5009 0.0746  0.0057  -0.0455 810  ILE B CG1 
7429  C  CG2 . ILE B 810  ? 0.5516 0.6961 0.6660 0.0798  -0.0013 -0.0516 810  ILE B CG2 
7430  C  CD1 . ILE B 810  ? 0.4514 0.5720 0.5607 0.0784  0.0058  -0.0421 810  ILE B CD1 
7431  N  N   . ALA B 811  ? 0.6457 0.8163 0.7720 0.0700  -0.0016 -0.0608 811  ALA B N   
7432  C  CA  . ALA B 811  ? 0.7007 0.8832 0.8301 0.0690  -0.0045 -0.0660 811  ALA B CA  
7433  C  C   . ALA B 811  ? 0.6574 0.8386 0.7817 0.0740  -0.0086 -0.0671 811  ALA B C   
7434  O  O   . ALA B 811  ? 0.6833 0.8551 0.8022 0.0789  -0.0092 -0.0639 811  ALA B O   
7435  C  CB  . ALA B 811  ? 0.8003 0.9960 0.9368 0.0703  -0.0058 -0.0686 811  ALA B CB  
7436  N  N   . VAL B 812  ? 0.5551 0.7460 0.6813 0.0727  -0.0114 -0.0720 812  VAL B N   
7437  C  CA  . VAL B 812  ? 0.6647 0.8560 0.7861 0.0774  -0.0158 -0.0739 812  VAL B CA  
7438  C  C   . VAL B 812  ? 0.6735 0.8801 0.8002 0.0812  -0.0202 -0.0783 812  VAL B C   
7439  O  O   . VAL B 812  ? 0.6953 0.9147 0.8289 0.0770  -0.0207 -0.0827 812  VAL B O   
7440  C  CB  . VAL B 812  ? 0.6051 0.7940 0.7231 0.0728  -0.0158 -0.0761 812  VAL B CB  
7441  C  CG1 . VAL B 812  ? 0.6201 0.8122 0.7339 0.0779  -0.0211 -0.0791 812  VAL B CG1 
7442  C  CG2 . VAL B 812  ? 0.5579 0.7307 0.6695 0.0706  -0.0118 -0.0714 812  VAL B CG2 
7443  N  N   . VAL B 813  ? 0.6110 0.8162 0.7344 0.0892  -0.0231 -0.0772 813  VAL B N   
7444  C  CA  . VAL B 813  ? 0.6543 0.8729 0.7815 0.0943  -0.0275 -0.0810 813  VAL B CA  
7445  C  C   . VAL B 813  ? 0.7289 0.9500 0.8513 0.0982  -0.0323 -0.0841 813  VAL B C   
7446  O  O   . VAL B 813  ? 0.8256 1.0356 0.9402 0.0985  -0.0321 -0.0824 813  VAL B O   
7447  C  CB  . VAL B 813  ? 0.6441 0.8597 0.7701 0.1013  -0.0280 -0.0781 813  VAL B CB  
7448  C  CG1 . VAL B 813  ? 0.5714 0.7826 0.7009 0.0976  -0.0234 -0.0748 813  VAL B CG1 
7449  C  CG2 . VAL B 813  ? 0.6396 0.8416 0.7556 0.1076  -0.0292 -0.0747 813  VAL B CG2 
7450  N  N   . GLY B 814  ? 0.7937 1.0299 0.9206 0.1014  -0.0366 -0.0889 814  GLY B N   
7451  C  CA  . GLY B 814  ? 0.9933 1.2337 1.1161 0.1055  -0.0417 -0.0926 814  GLY B CA  
7452  C  C   . GLY B 814  ? 1.0295 1.2600 1.1423 0.1152  -0.0443 -0.0897 814  GLY B C   
7453  O  O   . GLY B 814  ? 1.0119 1.2330 1.1216 0.1188  -0.0423 -0.0852 814  GLY B O   
7454  N  N   . LYS B 815  ? 0.8899 1.1225 0.9973 0.1195  -0.0489 -0.0926 815  LYS B N   
7455  C  CA  . LYS B 815  ? 0.8779 1.1017 0.9749 0.1294  -0.0517 -0.0904 815  LYS B CA  
7456  C  C   . LYS B 815  ? 0.8489 1.0799 0.9485 0.1365  -0.0539 -0.0909 815  LYS B C   
7457  O  O   . LYS B 815  ? 0.7825 1.0023 0.8748 0.1432  -0.0535 -0.0869 815  LYS B O   
7458  C  CB  . LYS B 815  ? 0.9488 1.1752 1.0397 0.1328  -0.0567 -0.0942 815  LYS B CB  
7459  C  CG  . LYS B 815  ? 0.9011 1.1193 0.9806 0.1438  -0.0600 -0.0924 815  LYS B CG  
7460  C  CD  . LYS B 815  ? 0.8418 1.0677 0.9171 0.1480  -0.0661 -0.0975 815  LYS B CD  
7461  C  CE  . LYS B 815  ? 0.8823 1.1025 0.9468 0.1601  -0.0698 -0.0963 815  LYS B CE  
7462  N  NZ  . LYS B 815  ? 0.8237 1.0539 0.8848 0.1653  -0.0766 -0.1019 815  LYS B NZ  
7463  N  N   . ASP B 816  ? 1.5492 1.7985 1.6591 0.1352  -0.0559 -0.0957 816  ASP B N   
7464  C  CA  . ASP B 816  ? 1.5946 1.8517 1.7073 0.1420  -0.0579 -0.0964 816  ASP B CA  
7465  C  C   . ASP B 816  ? 1.5041 1.7515 1.6171 0.1414  -0.0532 -0.0913 816  ASP B C   
7466  O  O   . ASP B 816  ? 1.5230 1.7658 1.6317 0.1490  -0.0541 -0.0893 816  ASP B O   
7467  C  CB  . ASP B 816  ? 1.7260 2.0054 1.8508 0.1396  -0.0602 -0.1026 816  ASP B CB  
7468  C  CG  . ASP B 816  ? 1.7184 2.0072 1.8458 0.1475  -0.0627 -0.1038 816  ASP B CG  
7469  O  OD1 . ASP B 816  ? 1.6577 1.9385 1.7760 0.1570  -0.0650 -0.1018 816  ASP B OD1 
7470  O  OD2 . ASP B 816  ? 1.8264 2.1303 1.9647 0.1445  -0.0620 -0.1069 816  ASP B OD2 
7471  N  N   . GLN B 817  ? 0.7663 1.0100 0.8841 0.1326  -0.0482 -0.0893 817  GLN B N   
7472  C  CA  . GLN B 817  ? 0.7004 0.9355 0.8189 0.1316  -0.0440 -0.0848 817  GLN B CA  
7473  C  C   . GLN B 817  ? 0.7112 0.9265 0.8193 0.1348  -0.0422 -0.0792 817  GLN B C   
7474  O  O   . GLN B 817  ? 0.6216 0.8294 0.7282 0.1375  -0.0403 -0.0758 817  GLN B O   
7475  C  CB  . GLN B 817  ? 0.6816 0.9191 0.8079 0.1217  -0.0394 -0.0844 817  GLN B CB  
7476  C  CG  . GLN B 817  ? 0.7630 1.0195 0.9003 0.1181  -0.0401 -0.0894 817  GLN B CG  
7477  C  CD  . GLN B 817  ? 0.6778 0.9422 0.8188 0.1236  -0.0412 -0.0902 817  GLN B CD  
7478  O  OE1 . GLN B 817  ? 0.6017 0.8582 0.7415 0.1247  -0.0385 -0.0865 817  GLN B OE1 
7479  N  NE2 . GLN B 817  ? 0.8026 1.0833 0.9484 0.1272  -0.0451 -0.0952 817  GLN B NE2 
7480  N  N   . VAL B 818  ? 0.7428 0.9496 0.8438 0.1345  -0.0426 -0.0783 818  VAL B N   
7481  C  CA  . VAL B 818  ? 0.6726 0.8610 0.7635 0.1381  -0.0407 -0.0731 818  VAL B CA  
7482  C  C   . VAL B 818  ? 0.6574 0.8428 0.7406 0.1484  -0.0442 -0.0730 818  VAL B C   
7483  O  O   . VAL B 818  ? 0.6286 0.8006 0.7056 0.1522  -0.0423 -0.0687 818  VAL B O   
7484  C  CB  . VAL B 818  ? 0.6709 0.8506 0.7561 0.1346  -0.0396 -0.0721 818  VAL B CB  
7485  C  CG1 . VAL B 818  ? 0.4464 0.6074 0.5214 0.1383  -0.0372 -0.0667 818  VAL B CG1 
7486  C  CG2 . VAL B 818  ? 0.7071 0.8886 0.7991 0.1247  -0.0358 -0.0721 818  VAL B CG2 
7487  N  N   . SER B 819  ? 0.7360 0.9336 0.8195 0.1532  -0.0493 -0.0777 819  SER B N   
7488  C  CA  . SER B 819  ? 0.8031 0.9985 0.8790 0.1638  -0.0529 -0.0778 819  SER B CA  
7489  C  C   . SER B 819  ? 0.8348 1.0294 0.9129 0.1671  -0.0517 -0.0761 819  SER B C   
7490  O  O   . SER B 819  ? 0.8479 1.0316 0.9174 0.1745  -0.0520 -0.0734 819  SER B O   
7491  C  CB  . SER B 819  ? 0.8026 1.0142 0.8803 0.1680  -0.0589 -0.0837 819  SER B CB  
7492  O  OG  . SER B 819  ? 0.8956 1.1249 0.9849 0.1660  -0.0600 -0.0876 819  SER B OG  
7493  N  N   . ARG B 820  ? 0.8447 1.0501 0.9337 0.1619  -0.0502 -0.0776 820  ARG B N   
7494  C  CA  . ARG B 820  ? 0.8966 1.1013 0.9881 0.1642  -0.0488 -0.0762 820  ARG B CA  
7495  C  C   . ARG B 820  ? 0.9020 1.0917 0.9922 0.1597  -0.0436 -0.0710 820  ARG B C   
7496  O  O   . ARG B 820  ? 0.8404 1.0296 0.9337 0.1599  -0.0420 -0.0699 820  ARG B O   
7497  C  CB  . ARG B 820  ? 0.8825 1.1059 0.9860 0.1611  -0.0495 -0.0803 820  ARG B CB  
7498  C  CG  . ARG B 820  ? 0.8287 1.0695 0.9361 0.1631  -0.0542 -0.0861 820  ARG B CG  
7499  C  CD  . ARG B 820  ? 0.9370 1.1959 1.0573 0.1580  -0.0536 -0.0900 820  ARG B CD  
7500  N  NE  . ARG B 820  ? 0.8725 1.1487 0.9980 0.1581  -0.0577 -0.0958 820  ARG B NE  
7501  C  CZ  . ARG B 820  ? 0.8699 1.1591 0.9971 0.1656  -0.0622 -0.0996 820  ARG B CZ  
7502  N  NH1 . ARG B 820  ? 0.9466 1.2329 1.0698 0.1739  -0.0632 -0.0983 820  ARG B NH1 
7503  N  NH2 . ARG B 820  ? 0.8701 1.1756 1.0029 0.1647  -0.0659 -0.1052 820  ARG B NH2 
7504  N  N   . GLY B 821  ? 0.9394 1.1174 1.0251 0.1559  -0.0411 -0.0680 821  GLY B N   
7505  C  CA  . GLY B 821  ? 0.8987 1.0628 0.9833 0.1520  -0.0364 -0.0631 821  GLY B CA  
7506  C  C   . GLY B 821  ? 0.8822 1.0517 0.9764 0.1440  -0.0333 -0.0631 821  GLY B C   
7507  O  O   . GLY B 821  ? 0.7596 0.9240 0.8555 0.1433  -0.0310 -0.0607 821  GLY B O   
7508  N  N   . ARG B 822  ? 0.8311 1.0107 0.9315 0.1379  -0.0332 -0.0657 822  ARG B N   
7509  C  CA  . ARG B 822  ? 0.7695 0.9545 0.8785 0.1304  -0.0301 -0.0659 822  ARG B CA  
7510  C  C   . ARG B 822  ? 0.8399 1.0204 0.9491 0.1231  -0.0273 -0.0647 822  ARG B C   
7511  O  O   . ARG B 822  ? 0.9096 1.0981 1.0254 0.1167  -0.0258 -0.0665 822  ARG B O   
7512  C  CB  . ARG B 822  ? 0.8073 1.0102 0.9246 0.1296  -0.0320 -0.0706 822  ARG B CB  
7513  C  CG  . ARG B 822  ? 0.8331 1.0411 0.9511 0.1365  -0.0343 -0.0718 822  ARG B CG  
7514  C  CD  . ARG B 822  ? 0.8108 1.0379 0.9371 0.1361  -0.0363 -0.0768 822  ARG B CD  
7515  N  NE  . ARG B 822  ? 0.8228 1.0550 0.9501 0.1425  -0.0380 -0.0778 822  ARG B NE  
7516  C  CZ  . ARG B 822  ? 0.8563 1.1050 0.9903 0.1442  -0.0399 -0.0821 822  ARG B CZ  
7517  N  NH1 . ARG B 822  ? 0.9231 1.1855 1.0639 0.1395  -0.0406 -0.0860 822  ARG B NH1 
7518  N  NH2 . ARG B 822  ? 0.8300 1.0815 0.9638 0.1506  -0.0412 -0.0826 822  ARG B NH2 
7519  N  N   . GLU B 823  ? 0.9924 1.1596 1.0940 0.1240  -0.0262 -0.0615 823  GLU B N   
7520  C  CA  . GLU B 823  ? 0.9905 1.1520 1.0916 0.1176  -0.0232 -0.0600 823  GLU B CA  
7521  C  C   . GLU B 823  ? 0.9682 1.1248 1.0734 0.1125  -0.0189 -0.0569 823  GLU B C   
7522  O  O   . GLU B 823  ? 1.0842 1.2355 1.1893 0.1149  -0.0179 -0.0544 823  GLU B O   
7523  C  CB  . GLU B 823  ? 0.9868 1.1352 1.0783 0.1205  -0.0230 -0.0573 823  GLU B CB  
7524  C  CG  . GLU B 823  ? 0.9899 1.1243 1.0768 0.1234  -0.0205 -0.0525 823  GLU B CG  
7525  C  CD  . GLU B 823  ? 1.1440 1.2758 1.2254 0.1317  -0.0233 -0.0524 823  GLU B CD  
7526  O  OE1 . GLU B 823  ? 1.1961 1.3384 1.2784 0.1355  -0.0273 -0.0562 823  GLU B OE1 
7527  O  OE2 . GLU B 823  ? 1.1833 1.3025 1.2596 0.1343  -0.0213 -0.0487 823  GLU B OE2 
7528  N  N   . MET B 824  ? 0.7946 0.9530 0.9033 0.1056  -0.0164 -0.0572 824  MET B N   
7529  C  CA  . MET B 824  ? 0.8766 1.0310 0.9889 0.1007  -0.0124 -0.0545 824  MET B CA  
7530  C  C   . MET B 824  ? 0.9040 1.0461 1.0115 0.0981  -0.0094 -0.0510 824  MET B C   
7531  O  O   . MET B 824  ? 1.0858 1.2281 1.1923 0.0942  -0.0086 -0.0520 824  MET B O   
7532  C  CB  . MET B 824  ? 0.9312 1.0965 1.0506 0.0951  -0.0113 -0.0572 824  MET B CB  
7533  C  CG  . MET B 824  ? 0.9227 1.1024 1.0469 0.0973  -0.0145 -0.0616 824  MET B CG  
7534  S  SD  . MET B 824  ? 0.7881 0.9708 0.9160 0.1009  -0.0146 -0.0609 824  MET B SD  
7535  C  CE  . MET B 824  ? 0.7591 0.9373 0.8903 0.0944  -0.0097 -0.0581 824  MET B CE  
7536  N  N   . HIS B 825  ? 0.7586 0.8901 0.8634 0.1002  -0.0076 -0.0470 825  HIS B N   
7537  C  CA  . HIS B 825  ? 0.7316 0.8516 0.8324 0.0982  -0.0044 -0.0435 825  HIS B CA  
7538  C  C   . HIS B 825  ? 0.6235 0.7367 0.7261 0.0982  -0.0019 -0.0399 825  HIS B C   
7539  O  O   . HIS B 825  ? 0.6848 0.7959 0.7868 0.1024  -0.0031 -0.0391 825  HIS B O   
7540  C  CB  . HIS B 825  ? 0.8401 0.9527 0.9329 0.1024  -0.0056 -0.0427 825  HIS B CB  
7541  C  CG  . HIS B 825  ? 0.8812 0.9971 0.9711 0.1009  -0.0070 -0.0454 825  HIS B CG  
7542  N  ND1 . HIS B 825  ? 0.7883 0.9084 0.8745 0.1052  -0.0110 -0.0483 825  HIS B ND1 
7543  C  CD2 . HIS B 825  ? 0.8372 0.9526 0.9272 0.0956  -0.0051 -0.0459 825  HIS B CD2 
7544  C  CE1 . HIS B 825  ? 0.7788 0.9014 0.8633 0.1024  -0.0117 -0.0507 825  HIS B CE1 
7545  N  NE2 . HIS B 825  ? 0.7831 0.9024 0.8696 0.0964  -0.0080 -0.0492 825  HIS B NE2 
7546  N  N   . TRP B 826  ? 0.5191 0.6288 0.6238 0.0937  0.0015  -0.0378 826  TRP B N   
7547  C  CA  . TRP B 826  ? 0.6484 0.7527 0.7554 0.0934  0.0036  -0.0347 826  TRP B CA  
7548  C  C   . TRP B 826  ? 0.6285 0.7214 0.7311 0.0956  0.0053  -0.0312 826  TRP B C   
7549  O  O   . TRP B 826  ? 0.8212 0.9098 0.9258 0.0964  0.0065  -0.0291 826  TRP B O   
7550  C  CB  . TRP B 826  ? 0.6038 0.7092 0.7146 0.0883  0.0064  -0.0339 826  TRP B CB  
7551  C  CG  . TRP B 826  ? 0.6014 0.7171 0.7167 0.0859  0.0056  -0.0368 826  TRP B CG  
7552  C  CD1 . TRP B 826  ? 0.6381 0.7631 0.7551 0.0874  0.0027  -0.0403 826  TRP B CD1 
7553  C  CD2 . TRP B 826  ? 0.5902 0.7080 0.7089 0.0817  0.0080  -0.0365 826  TRP B CD2 
7554  N  NE1 . TRP B 826  ? 0.6378 0.7706 0.7593 0.0841  0.0034  -0.0422 826  TRP B NE1 
7555  C  CE2 . TRP B 826  ? 0.6471 0.7752 0.7693 0.0806  0.0066  -0.0398 826  TRP B CE2 
7556  C  CE3 . TRP B 826  ? 0.5857 0.6977 0.7045 0.0791  0.0112  -0.0337 826  TRP B CE3 
7557  C  CZ2 . TRP B 826  ? 0.6337 0.7655 0.7589 0.0767  0.0087  -0.0402 826  TRP B CZ2 
7558  C  CZ3 . TRP B 826  ? 0.6384 0.7540 0.7599 0.0757  0.0129  -0.0342 826  TRP B CZ3 
7559  C  CH2 . TRP B 826  ? 0.6457 0.7707 0.7700 0.0745  0.0118  -0.0373 826  TRP B CH2 
7560  N  N   . ILE B 827  ? 0.2831 0.3711 0.3799 0.0966  0.0056  -0.0308 827  ILE B N   
7561  C  CA  . ILE B 827  ? 0.2885 0.3654 0.3803 0.0989  0.0076  -0.0275 827  ILE B CA  
7562  C  C   . ILE B 827  ? 0.4687 0.5435 0.5533 0.1032  0.0054  -0.0286 827  ILE B C   
7563  O  O   . ILE B 827  ? 0.5763 0.6567 0.6592 0.1029  0.0032  -0.0316 827  ILE B O   
7564  C  CB  . ILE B 827  ? 0.2998 0.3706 0.3909 0.0955  0.0115  -0.0248 827  ILE B CB  
7565  C  CG1 . ILE B 827  ? 0.3265 0.3861 0.4130 0.0978  0.0141  -0.0213 827  ILE B CG1 
7566  C  CG2 . ILE B 827  ? 0.3497 0.4228 0.4377 0.0931  0.0112  -0.0268 827  ILE B CG2 
7567  C  CD1 . ILE B 827  ? 0.3350 0.3891 0.4222 0.0949  0.0182  -0.0183 827  ILE B CD1 
7568  N  N   . ARG B 828  ? 0.7303 0.7968 0.8104 0.1073  0.0059  -0.0265 828  ARG B N   
7569  C  CA  . ARG B 828  ? 0.7626 0.8257 0.8348 0.1124  0.0039  -0.0272 828  ARG B CA  
7570  C  C   . ARG B 828  ? 0.8301 0.8799 0.8961 0.1146  0.0071  -0.0232 828  ARG B C   
7571  O  O   . ARG B 828  ? 0.8023 0.8468 0.8712 0.1135  0.0100  -0.0205 828  ARG B O   
7572  C  CB  . ARG B 828  ? 0.7993 0.8676 0.8715 0.1169  0.0001  -0.0295 828  ARG B CB  
7573  C  CG  . ARG B 828  ? 0.8686 0.9325 0.9431 0.1183  0.0011  -0.0276 828  ARG B CG  
7574  C  CD  . ARG B 828  ? 0.9298 0.9952 1.0010 0.1242  -0.0022 -0.0294 828  ARG B CD  
7575  N  NE  . ARG B 828  ? 0.9786 1.0356 1.0489 0.1263  -0.0007 -0.0270 828  ARG B NE  
7576  C  CZ  . ARG B 828  ? 1.0153 1.0758 1.0913 0.1256  -0.0013 -0.0277 828  ARG B CZ  
7577  N  NH1 . ARG B 828  ? 0.9697 1.0418 1.0525 0.1232  -0.0032 -0.0304 828  ARG B NH1 
7578  N  NH2 . ARG B 828  ? 0.8556 0.9073 0.9301 0.1273  0.0003  -0.0257 828  ARG B NH2 
7579  N  N   . ILE B 829  ? 0.7376 0.7822 0.7950 0.1176  0.0068  -0.0231 829  ILE B N   
7580  C  CA  . ILE B 829  ? 0.7501 0.7817 0.8002 0.1203  0.0100  -0.0194 829  ILE B CA  
7581  C  C   . ILE B 829  ? 0.7671 0.7948 0.8096 0.1269  0.0076  -0.0199 829  ILE B C   
7582  O  O   . ILE B 829  ? 0.8459 0.8794 0.8849 0.1301  0.0034  -0.0231 829  ILE B O   
7583  C  CB  . ILE B 829  ? 0.7701 0.7968 0.8145 0.1192  0.0120  -0.0185 829  ILE B CB  
7584  C  CG1 . ILE B 829  ? 0.7238 0.7516 0.7746 0.1132  0.0153  -0.0171 829  ILE B CG1 
7585  C  CG2 . ILE B 829  ? 0.9111 0.9246 0.9461 0.1233  0.0148  -0.0152 829  ILE B CG2 
7586  C  CD1 . ILE B 829  ? 0.7787 0.8168 0.8342 0.1092  0.0131  -0.0205 829  ILE B CD1 
7587  N  N   . ASP B 830  ? 0.7693 0.7874 0.8094 0.1292  0.0103  -0.0168 830  ASP B N   
7588  C  CA  . ASP B 830  ? 0.8913 0.9040 0.9239 0.1356  0.0086  -0.0168 830  ASP B CA  
7589  C  C   . ASP B 830  ? 1.0281 1.0264 1.0505 0.1388  0.0123  -0.0132 830  ASP B C   
7590  O  O   . ASP B 830  ? 1.1383 1.1289 1.1622 0.1358  0.0173  -0.0098 830  ASP B O   
7591  C  CB  . ASP B 830  ? 0.8351 0.8473 0.8726 0.1358  0.0088  -0.0164 830  ASP B CB  
7592  C  CG  . ASP B 830  ? 0.9291 0.9550 0.9753 0.1338  0.0051  -0.0199 830  ASP B CG  
7593  O  OD1 . ASP B 830  ? 1.0000 1.0355 1.0463 0.1347  0.0013  -0.0233 830  ASP B OD1 
7594  O  OD2 . ASP B 830  ? 0.8396 0.8668 0.8927 0.1314  0.0060  -0.0195 830  ASP B OD2 
7595  N  N   . ARG B 831  ? 1.1144 1.1093 1.1262 0.1448  0.0098  -0.0141 831  ARG B N   
7596  C  CA  . ARG B 831  ? 1.2136 1.1938 1.2139 0.1491  0.0131  -0.0107 831  ARG B CA  
7597  C  C   . ARG B 831  ? 1.1361 1.1098 1.1304 0.1551  0.0123  -0.0102 831  ARG B C   
7598  O  O   . ARG B 831  ? 1.0335 1.0150 1.0291 0.1581  0.0076  -0.0133 831  ARG B O   
7599  C  CB  . ARG B 831  ? 1.2790 1.2578 1.2699 0.1523  0.0114  -0.0118 831  ARG B CB  
7600  C  CG  . ARG B 831  ? 1.0974 1.0783 1.0796 0.1597  0.0061  -0.0146 831  ARG B CG  
7601  C  CD  . ARG B 831  ? 1.1757 1.1734 1.1656 0.1585  0.0002  -0.0198 831  ARG B CD  
7602  N  NE  . ARG B 831  ? 1.0748 1.0760 1.0566 0.1655  -0.0052 -0.0230 831  ARG B NE  
7603  C  CZ  . ARG B 831  ? 1.1079 1.1086 1.0856 0.1719  -0.0079 -0.0238 831  ARG B CZ  
7604  N  NH1 . ARG B 831  ? 1.1711 1.1672 1.1516 0.1720  -0.0057 -0.0217 831  ARG B NH1 
7605  N  NH2 . ARG B 831  ? 1.1429 1.1477 1.1133 0.1785  -0.0131 -0.0269 831  ARG B NH2 
7606  N  N   . TYR B 832  ? 1.1481 1.1070 1.1356 0.1569  0.0172  -0.0061 832  TYR B N   
7607  C  CA  . TYR B 832  ? 1.1996 1.1504 1.1826 0.1612  0.0177  -0.0050 832  TYR B CA  
7608  C  C   . TYR B 832  ? 1.1379 1.0735 1.1055 0.1682  0.0198  -0.0023 832  TYR B C   
7609  O  O   . TYR B 832  ? 1.2293 1.1561 1.1919 0.1718  0.0209  -0.0010 832  TYR B O   
7610  C  CB  . TYR B 832  ? 1.2109 1.1580 1.2026 0.1557  0.0222  -0.0026 832  TYR B CB  
7611  C  CG  . TYR B 832  ? 1.0753 1.0351 1.0794 0.1517  0.0191  -0.0055 832  TYR B CG  
7612  C  CD1 . TYR B 832  ? 1.0343 0.9989 1.0378 0.1558  0.0146  -0.0083 832  TYR B CD1 
7613  C  CD2 . TYR B 832  ? 1.0399 1.0070 1.0560 0.1444  0.0207  -0.0055 832  TYR B CD2 
7614  C  CE1 . TYR B 832  ? 0.9679 0.9438 0.9821 0.1525  0.0120  -0.0109 832  TYR B CE1 
7615  C  CE2 . TYR B 832  ? 1.1103 1.0884 1.1368 0.1412  0.0179  -0.0081 832  TYR B CE2 
7616  C  CZ  . TYR B 832  ? 0.9781 0.9606 1.0037 0.1452  0.0137  -0.0108 832  TYR B CZ  
7617  O  OH  . TYR B 832  ? 0.9788 0.9719 1.0142 0.1422  0.0112  -0.0133 832  TYR B OH  
7618  N  N   . PHE B 833  ? 0.8645 0.7959 0.8236 0.1703  0.0205  -0.0015 833  PHE B N   
7619  C  CA  . PHE B 833  ? 0.9077 0.8250 0.8506 0.1777  0.0220  0.0007  833  PHE B CA  
7620  C  C   . PHE B 833  ? 0.8220 0.7243 0.7591 0.1802  0.0266  0.0043  833  PHE B C   
7621  O  O   . PHE B 833  ? 0.8521 0.7513 0.7823 0.1865  0.0238  0.0034  833  PHE B O   
7622  C  CB  . PHE B 833  ? 0.7654 0.6887 0.7004 0.1852  0.0150  -0.0030 833  PHE B CB  
7623  C  CG  . PHE B 833  ? 0.7577 0.6923 0.6946 0.1839  0.0110  -0.0063 833  PHE B CG  
7624  C  CD1 . PHE B 833  ? 0.7756 0.7048 0.7086 0.1818  0.0143  -0.0044 833  PHE B CD1 
7625  C  CD2 . PHE B 833  ? 0.7963 0.7467 0.7386 0.1847  0.0041  -0.0114 833  PHE B CD2 
7626  C  CE1 . PHE B 833  ? 0.8543 0.7931 0.7885 0.1804  0.0106  -0.0077 833  PHE B CE1 
7627  C  CE2 . PHE B 833  ? 0.8862 0.8468 0.8303 0.1830  0.0005  -0.0147 833  PHE B CE2 
7628  C  CZ  . PHE B 833  ? 0.8604 0.8150 0.8003 0.1807  0.0037  -0.0129 833  PHE B CZ  
7629  N  N   . ALA B 834  ? 0.6550 0.5481 0.5948 0.1754  0.0335  0.0082  834  ALA B N   
7630  C  CA  . ALA B 834  ? 0.7359 0.6155 0.6724 0.1760  0.0383  0.0113  834  ALA B CA  
7631  C  C   . ALA B 834  ? 0.7904 0.6530 0.7157 0.1778  0.0453  0.0160  834  ALA B C   
7632  O  O   . ALA B 834  ? 0.8480 0.7101 0.7717 0.1764  0.0474  0.0172  834  ALA B O   
7633  C  CB  . ALA B 834  ? 0.7918 0.6763 0.7436 0.1679  0.0407  0.0115  834  ALA B CB  
7634  N  N   . GLY B 835  ? 1.0790 0.9268 0.9960 0.1810  0.0490  0.0186  835  GLY B N   
7635  C  CA  . GLY B 835  ? 1.2169 1.0467 1.1226 0.1829  0.0564  0.0234  835  GLY B CA  
7636  C  C   . GLY B 835  ? 1.2738 1.0896 1.1611 0.1926  0.0559  0.0245  835  GLY B C   
7637  O  O   . GLY B 835  ? 1.2867 1.1067 1.1703 0.1982  0.0498  0.0216  835  GLY B O   
7638  N  N   . GLU B 836  ? 1.2728 1.0713 1.1481 0.1949  0.0628  0.0290  836  GLU B N   
7639  C  CA  . GLU B 836  ? 1.2661 1.0495 1.1218 0.2048  0.0630  0.0306  836  GLU B CA  
7640  C  C   . GLU B 836  ? 1.3215 1.1107 1.1676 0.2120  0.0567  0.0282  836  GLU B C   
7641  O  O   . GLU B 836  ? 1.4095 1.2118 1.2632 0.2087  0.0537  0.0260  836  GLU B O   
7642  C  CB  . GLU B 836  ? 1.2169 0.9797 1.0623 0.2050  0.0727  0.0362  836  GLU B CB  
7643  C  CG  . GLU B 836  ? 1.4510 1.2066 1.3045 0.1984  0.0790  0.0383  836  GLU B CG  
7644  C  CD  . GLU B 836  ? 1.5722 1.3083 1.4171 0.1974  0.0894  0.0438  836  GLU B CD  
7645  O  OE1 . GLU B 836  ? 1.4920 1.2223 1.3273 0.2004  0.0920  0.0460  836  GLU B OE1 
7646  O  OE2 . GLU B 836  ? 1.6152 1.3415 1.4626 0.1936  0.0949  0.0458  836  GLU B OE2 
7647  N  N   . ASP B 837  ? 1.6653 1.4442 1.4941 0.2221  0.0547  0.0285  837  ASP B N   
7648  C  CA  . ASP B 837  ? 1.7811 1.5642 1.5988 0.2304  0.0483  0.0261  837  ASP B CA  
7649  C  C   . ASP B 837  ? 1.7517 1.5561 1.5794 0.2306  0.0386  0.0201  837  ASP B C   
7650  O  O   . ASP B 837  ? 1.8746 1.6813 1.6930 0.2393  0.0323  0.0174  837  ASP B O   
7651  C  CB  . ASP B 837  ? 1.9216 1.7027 1.7356 0.2289  0.0512  0.0277  837  ASP B CB  
7652  C  CG  . ASP B 837  ? 1.9422 1.7210 1.7397 0.2388  0.0463  0.0262  837  ASP B CG  
7653  O  OD1 . ASP B 837  ? 1.9129 1.6899 1.7006 0.2474  0.0415  0.0246  837  ASP B OD1 
7654  O  OD2 . ASP B 837  ? 1.9732 1.7520 1.7673 0.2382  0.0474  0.0267  837  ASP B OD2 
7655  N  N   . LEU B 838  ? 1.1095 0.9297 0.9558 0.2215  0.0372  0.0178  838  LEU B N   
7656  C  CA  . LEU B 838  ? 1.0470 0.8881 0.9042 0.2203  0.0288  0.0122  838  LEU B CA  
7657  C  C   . LEU B 838  ? 1.1044 0.9522 0.9538 0.2258  0.0230  0.0092  838  LEU B C   
7658  O  O   . LEU B 838  ? 1.0260 0.8909 0.8827 0.2259  0.0157  0.0042  838  LEU B O   
7659  C  CB  . LEU B 838  ? 0.9967 0.8426 0.8564 0.2236  0.0245  0.0097  838  LEU B CB  
7660  C  CG  . LEU B 838  ? 0.9291 0.7758 0.8019 0.2162  0.0279  0.0106  838  LEU B CG  
7661  C  CD1 . LEU B 838  ? 0.9816 0.8339 0.8562 0.2201  0.0229  0.0077  838  LEU B CD1 
7662  C  CD2 . LEU B 838  ? 0.8765 0.7375 0.7673 0.2058  0.0281  0.0092  838  LEU B CD2 
7663  N  N   . ASP B 839  ? 1.8880 1.7225 1.7225 0.2305  0.0261  0.0120  839  ASP B N   
7664  C  CA  . ASP B 839  ? 1.9148 1.7545 1.7423 0.2343  0.0216  0.0094  839  ASP B CA  
7665  C  C   . ASP B 839  ? 1.9600 1.7978 1.7905 0.2279  0.0263  0.0114  839  ASP B C   
7666  O  O   . ASP B 839  ? 1.9642 1.8087 1.7924 0.2288  0.0225  0.0088  839  ASP B O   
7667  C  CB  . ASP B 839  ? 1.9792 1.8051 1.7851 0.2462  0.0205  0.0107  839  ASP B CB  
7668  C  CG  . ASP B 839  ? 1.9936 1.8313 1.7961 0.2538  0.0108  0.0054  839  ASP B CG  
7669  O  OD1 . ASP B 839  ? 1.9529 1.8070 1.7693 0.2505  0.0060  0.0015  839  ASP B OD1 
7670  O  OD2 . ASP B 839  ? 2.0510 1.8820 1.8369 0.2634  0.0081  0.0050  839  ASP B OD2 
7671  N  N   . ASN B 840  ? 1.8722 1.7011 1.7077 0.2217  0.0345  0.0159  840  ASN B N   
7672  C  CA  . ASN B 840  ? 1.8440 1.6734 1.6861 0.2144  0.0394  0.0177  840  ASN B CA  
7673  C  C   . ASN B 840  ? 1.7689 1.6043 1.6290 0.2048  0.0430  0.0186  840  ASN B C   
7674  O  O   . ASN B 840  ? 1.8779 1.7026 1.7392 0.2012  0.0508  0.0230  840  ASN B O   
7675  C  CB  . ASN B 840  ? 1.8244 1.6343 1.6517 0.2177  0.0470  0.0229  840  ASN B CB  
7676  C  CG  . ASN B 840  ? 1.8102 1.6169 1.6222 0.2248  0.0437  0.0216  840  ASN B CG  
7677  O  OD1 . ASN B 840  ? 1.8136 1.6333 1.6268 0.2269  0.0356  0.0166  840  ASN B OD1 
7678  N  ND2 . ASN B 840  ? 1.8852 1.6745 1.6827 0.2287  0.0501  0.0260  840  ASN B ND2 
7679  N  N   . PRO B 841  ? 1.1747 1.0272 1.0489 0.2005  0.0374  0.0144  841  PRO B N   
7680  C  CA  . PRO B 841  ? 1.1107 0.9686 1.0008 0.1927  0.0400  0.0150  841  PRO B CA  
7681  C  C   . PRO B 841  ? 1.0763 0.9429 0.9798 0.1839  0.0422  0.0149  841  PRO B C   
7682  O  O   . PRO B 841  ? 1.1520 1.0276 1.0571 0.1828  0.0388  0.0123  841  PRO B O   
7683  C  CB  . PRO B 841  ? 1.0848 0.9557 0.9811 0.1943  0.0325  0.0104  841  PRO B CB  
7684  C  CG  . PRO B 841  ? 1.0344 0.9156 0.9270 0.1976  0.0257  0.0063  841  PRO B CG  
7685  C  CD  . PRO B 841  ? 1.1115 0.9796 0.9880 0.2028  0.0284  0.0088  841  PRO B CD  
7686  N  N   . SER B 842  ? 1.0743 0.9381 0.9873 0.1776  0.0480  0.0177  842  SER B N   
7687  C  CA  . SER B 842  ? 1.1088 0.9828 1.0364 0.1693  0.0494  0.0172  842  SER B CA  
7688  C  C   . SER B 842  ? 1.0560 0.9473 0.9957 0.1663  0.0426  0.0125  842  SER B C   
7689  O  O   . SER B 842  ? 1.0710 0.9655 1.0132 0.1678  0.0395  0.0109  842  SER B O   
7690  C  CB  . SER B 842  ? 1.1361 1.0038 1.0714 0.1638  0.0567  0.0210  842  SER B CB  
7691  O  OG  . SER B 842  ? 1.0707 0.9340 1.0067 0.1647  0.0570  0.0213  842  SER B OG  
7692  N  N   . ILE B 843  ? 0.9785 0.8807 0.9252 0.1621  0.0405  0.0104  843  ILE B N   
7693  C  CA  . ILE B 843  ? 0.9241 0.8428 0.8815 0.1591  0.0345  0.0059  843  ILE B CA  
7694  C  C   . ILE B 843  ? 0.9643 0.8894 0.9367 0.1511  0.0372  0.0066  843  ILE B C   
7695  O  O   . ILE B 843  ? 0.9739 0.8963 0.9490 0.1473  0.0419  0.0090  843  ILE B O   
7696  C  CB  . ILE B 843  ? 0.8191 0.7454 0.7732 0.1601  0.0298  0.0026  843  ILE B CB  
7697  C  CG1 . ILE B 843  ? 0.9005 0.8183 0.8383 0.1684  0.0280  0.0025  843  ILE B CG1 
7698  C  CG2 . ILE B 843  ? 0.8971 0.8398 0.8607 0.1581  0.0234  -0.0023 843  ILE B CG2 
7699  C  CD1 . ILE B 843  ? 1.0039 0.9210 0.9349 0.1690  0.0275  0.0017  843  ILE B CD1 
7700  N  N   . TYR B 844  ? 1.1092 1.0432 1.0913 0.1488  0.0342  0.0044  844  TYR B N   
7701  C  CA  . TYR B 844  ? 1.1285 1.0685 1.1245 0.1419  0.0363  0.0049  844  TYR B CA  
7702  C  C   . TYR B 844  ? 1.1144 1.0701 1.1195 0.1389  0.0310  0.0007  844  TYR B C   
7703  O  O   . TYR B 844  ? 1.1571 1.1195 1.1644 0.1406  0.0265  -0.0021 844  TYR B O   
7704  C  CB  . TYR B 844  ? 1.1381 1.0732 1.1372 0.1417  0.0382  0.0062  844  TYR B CB  
7705  C  CG  . TYR B 844  ? 1.1917 1.1109 1.1832 0.1435  0.0445  0.0105  844  TYR B CG  
7706  C  CD1 . TYR B 844  ? 1.1939 1.1069 1.1838 0.1415  0.0500  0.0137  844  TYR B CD1 
7707  C  CD2 . TYR B 844  ? 1.1603 1.0706 1.1461 0.1471  0.0452  0.0114  844  TYR B CD2 
7708  C  CE1 . TYR B 844  ? 1.2601 1.1587 1.2433 0.1429  0.0563  0.0177  844  TYR B CE1 
7709  C  CE2 . TYR B 844  ? 1.1255 1.0206 1.1041 0.1484  0.0514  0.0154  844  TYR B CE2 
7710  C  CZ  . TYR B 844  ? 1.2138 1.1033 1.1913 0.1462  0.0570  0.0185  844  TYR B CZ  
7711  O  OH  . TYR B 844  ? 1.2319 1.1063 1.2024 0.1473  0.0638  0.0226  844  TYR B OH  
7712  N  N   . MET B 845  ? 0.8902 0.8514 0.9004 0.1345  0.0318  0.0004  845  MET B N   
7713  C  CA  . MET B 845  ? 0.9186 0.8937 0.9375 0.1309  0.0277  -0.0032 845  MET B CA  
7714  C  C   . MET B 845  ? 0.8996 0.8797 0.9310 0.1253  0.0295  -0.0025 845  MET B C   
7715  O  O   . MET B 845  ? 0.9224 0.8976 0.9568 0.1224  0.0344  0.0005  845  MET B O   
7716  C  CB  . MET B 845  ? 0.9507 0.9287 0.9673 0.1293  0.0273  -0.0042 845  MET B CB  
7717  C  CG  . MET B 845  ? 0.9050 0.8753 0.9082 0.1345  0.0268  -0.0040 845  MET B CG  
7718  S  SD  . MET B 845  ? 0.9771 0.9555 0.9754 0.1395  0.0191  -0.0090 845  MET B SD  
7719  C  CE  . MET B 845  ? 0.9679 0.9585 0.9718 0.1344  0.0161  -0.0129 845  MET B CE  
7720  N  N   . MET B 846  ? 0.8357 0.8259 0.8741 0.1240  0.0256  -0.0055 846  MET B N   
7721  C  CA  . MET B 846  ? 0.7997 0.7952 0.8493 0.1194  0.0265  -0.0053 846  MET B CA  
7722  C  C   . MET B 846  ? 0.7125 0.7212 0.7690 0.1168  0.0224  -0.0089 846  MET B C   
7723  O  O   . MET B 846  ? 0.6539 0.6685 0.7093 0.1193  0.0181  -0.0119 846  MET B O   
7724  C  CB  . MET B 846  ? 0.6845 0.6758 0.7352 0.1211  0.0267  -0.0047 846  MET B CB  
7725  C  CG  . MET B 846  ? 0.5808 0.5738 0.6417 0.1165  0.0290  -0.0036 846  MET B CG  
7726  S  SD  . MET B 846  ? 0.8112 0.8002 0.8733 0.1182  0.0283  -0.0039 846  MET B SD  
7727  C  CE  . MET B 846  ? 0.6175 0.6145 0.6762 0.1226  0.0219  -0.0080 846  MET B CE  
7728  N  N   . PRO B 847  ? 0.4869 0.5003 0.5504 0.1120  0.0239  -0.0087 847  PRO B N   
7729  C  CA  . PRO B 847  ? 0.4815 0.5067 0.5514 0.1092  0.0207  -0.0118 847  PRO B CA  
7730  C  C   . PRO B 847  ? 0.5862 0.6161 0.6638 0.1081  0.0195  -0.0126 847  PRO B C   
7731  O  O   . PRO B 847  ? 0.5623 0.5879 0.6436 0.1069  0.0221  -0.0104 847  PRO B O   
7732  C  CB  . PRO B 847  ? 0.4373 0.4633 0.5102 0.1049  0.0235  -0.0107 847  PRO B CB  
7733  C  CG  . PRO B 847  ? 0.4777 0.4929 0.5451 0.1060  0.0278  -0.0072 847  PRO B CG  
7734  C  CD  . PRO B 847  ? 0.4800 0.4882 0.5449 0.1092  0.0287  -0.0056 847  PRO B CD  
7735  N  N   . VAL B 848  ? 0.6808 0.7199 0.7609 0.1085  0.0155  -0.0160 848  VAL B N   
7736  C  CA  . VAL B 848  ? 0.6167 0.6608 0.7031 0.1079  0.0139  -0.0172 848  VAL B CA  
7737  C  C   . VAL B 848  ? 0.7090 0.7643 0.8012 0.1049  0.0119  -0.0199 848  VAL B C   
7738  O  O   . VAL B 848  ? 0.7057 0.7669 0.7958 0.1055  0.0095  -0.0224 848  VAL B O   
7739  C  CB  . VAL B 848  ? 0.5471 0.5899 0.6296 0.1128  0.0112  -0.0185 848  VAL B CB  
7740  C  CG1 . VAL B 848  ? 0.5914 0.6395 0.6801 0.1123  0.0094  -0.0200 848  VAL B CG1 
7741  C  CG2 . VAL B 848  ? 0.5947 0.6250 0.6708 0.1158  0.0137  -0.0156 848  VAL B CG2 
7742  N  N   . ASN B 849  ? 0.7244 0.7826 0.8236 0.1017  0.0129  -0.0194 849  ASN B N   
7743  C  CA  . ASN B 849  ? 0.6149 0.6829 0.7193 0.0991  0.0113  -0.0217 849  ASN B CA  
7744  C  C   . ASN B 849  ? 0.6757 0.7459 0.7855 0.0990  0.0104  -0.0221 849  ASN B C   
7745  O  O   . ASN B 849  ? 0.6338 0.6991 0.7426 0.1015  0.0101  -0.0215 849  ASN B O   
7746  C  CB  . ASN B 849  ? 0.5615 0.6304 0.6677 0.0950  0.0137  -0.0207 849  ASN B CB  
7747  C  CG  . ASN B 849  ? 0.5991 0.6617 0.7076 0.0934  0.0171  -0.0175 849  ASN B CG  
7748  O  OD1 . ASN B 849  ? 0.5848 0.6402 0.6914 0.0951  0.0186  -0.0155 849  ASN B OD1 
7749  N  ND2 . ASN B 849  ? 0.8564 0.9218 0.9689 0.0902  0.0186  -0.0169 849  ASN B ND2 
7750  N  N   . CYS B 850  ? 0.8704 0.9473 0.9853 0.0962  0.0101  -0.0232 850  CYS B N   
7751  C  CA  . CYS B 850  ? 0.8619 0.9408 0.9818 0.0961  0.0093  -0.0236 850  CYS B CA  
7752  C  C   . CYS B 850  ? 0.8172 0.8895 0.9395 0.0947  0.0118  -0.0209 850  CYS B C   
7753  O  O   . CYS B 850  ? 0.8010 0.8722 0.9249 0.0921  0.0142  -0.0191 850  CYS B O   
7754  C  CB  . CYS B 850  ? 0.8023 0.8897 0.9262 0.0937  0.0086  -0.0253 850  CYS B CB  
7755  S  SG  . CYS B 850  ? 0.8400 0.9304 0.9688 0.0941  0.0070  -0.0264 850  CYS B SG  
7756  N  N   . MET B 851  ? 0.7127 0.7806 0.8354 0.0965  0.0113  -0.0206 851  MET B N   
7757  C  CA  . MET B 851  ? 0.7122 0.7745 0.8383 0.0949  0.0137  -0.0184 851  MET B CA  
7758  C  C   . MET B 851  ? 0.7298 0.7969 0.8625 0.0923  0.0135  -0.0188 851  MET B C   
7759  O  O   . MET B 851  ? 0.7432 0.8075 0.8797 0.0905  0.0155  -0.0171 851  MET B O   
7760  C  CB  . MET B 851  ? 0.5940 0.6497 0.7184 0.0972  0.0134  -0.0182 851  MET B CB  
7761  C  CG  . MET B 851  ? 0.6382 0.6885 0.7549 0.1007  0.0133  -0.0180 851  MET B CG  
7762  S  SD  . MET B 851  ? 0.7153 0.7558 0.8280 0.1003  0.0177  -0.0143 851  MET B SD  
7763  C  CE  . MET B 851  ? 0.6282 0.6726 0.7361 0.1009  0.0171  -0.0148 851  MET B CE  
7764  N  N   . GLN B 852  ? 0.6040 0.6785 0.7382 0.0922  0.0112  -0.0210 852  GLN B N   
7765  C  CA  . GLN B 852  ? 0.6234 0.7025 0.7628 0.0904  0.0106  -0.0216 852  GLN B CA  
7766  C  C   . GLN B 852  ? 0.5855 0.6617 0.7288 0.0904  0.0100  -0.0217 852  GLN B C   
7767  O  O   . GLN B 852  ? 0.5441 0.6193 0.6916 0.0885  0.0114  -0.0204 852  GLN B O   
7768  C  CB  . GLN B 852  ? 0.5814 0.6613 0.7223 0.0879  0.0131  -0.0197 852  GLN B CB  
7769  C  CG  . GLN B 852  ? 0.5074 0.5884 0.6440 0.0874  0.0141  -0.0196 852  GLN B CG  
7770  C  CD  . GLN B 852  ? 0.6079 0.6961 0.7442 0.0870  0.0126  -0.0218 852  GLN B CD  
7771  O  OE1 . GLN B 852  ? 0.6618 0.7539 0.8011 0.0867  0.0115  -0.0228 852  GLN B OE1 
7772  N  NE2 . GLN B 852  ? 0.6162 0.7061 0.7488 0.0868  0.0127  -0.0226 852  GLN B NE2 
7773  N  N   . CYS B 853  ? 0.5422 0.6171 0.6838 0.0927  0.0079  -0.0234 853  CYS B N   
7774  C  CA  . CYS B 853  ? 0.5389 0.6098 0.6832 0.0927  0.0073  -0.0238 853  CYS B CA  
7775  C  C   . CYS B 853  ? 0.5879 0.6641 0.7374 0.0913  0.0057  -0.0252 853  CYS B C   
7776  O  O   . CYS B 853  ? 0.6045 0.6867 0.7536 0.0921  0.0037  -0.0270 853  CYS B O   
7777  C  CB  . CYS B 853  ? 0.5794 0.6474 0.7195 0.0959  0.0053  -0.0255 853  CYS B CB  
7778  S  SG  . CYS B 853  ? 0.4692 0.5345 0.6017 0.0989  0.0058  -0.0248 853  CYS B SG  
7779  N  N   . GLU B 854  ? 0.7660 0.8400 0.9205 0.0892  0.0066  -0.0245 854  GLU B N   
7780  C  CA  . GLU B 854  ? 0.6940 0.7728 0.8533 0.0882  0.0047  -0.0260 854  GLU B CA  
7781  C  C   . GLU B 854  ? 0.6773 0.7571 0.8354 0.0901  0.0014  -0.0289 854  GLU B C   
7782  O  O   . GLU B 854  ? 0.7591 0.8444 0.9181 0.0906  -0.0006 -0.0306 854  GLU B O   
7783  C  CB  . GLU B 854  ? 0.7515 0.8280 0.9169 0.0858  0.0059  -0.0251 854  GLU B CB  
7784  C  CG  . GLU B 854  ? 0.7943 0.8711 0.9617 0.0842  0.0091  -0.0223 854  GLU B CG  
7785  C  CD  . GLU B 854  ? 0.8132 0.8893 0.9877 0.0819  0.0103  -0.0217 854  GLU B CD  
7786  O  OE1 . GLU B 854  ? 0.7518 0.8277 0.9299 0.0812  0.0083  -0.0238 854  GLU B OE1 
7787  O  OE2 . GLU B 854  ? 0.8389 0.9147 1.0153 0.0807  0.0133  -0.0194 854  GLU B OE2 
7788  N  N   . LYS B 855  ? 0.6799 0.7538 0.8352 0.0915  0.0010  -0.0295 855  LYS B N   
7789  C  CA  . LYS B 855  ? 0.6770 0.7509 0.8297 0.0940  -0.0018 -0.0322 855  LYS B CA  
7790  C  C   . LYS B 855  ? 0.6523 0.7261 0.7988 0.0971  -0.0020 -0.0323 855  LYS B C   
7791  O  O   . LYS B 855  ? 0.6853 0.7531 0.8278 0.0993  -0.0021 -0.0325 855  LYS B O   
7792  C  CB  . LYS B 855  ? 0.6905 0.7572 0.8444 0.0935  -0.0022 -0.0331 855  LYS B CB  
7793  C  CG  . LYS B 855  ? 0.6604 0.7296 0.8199 0.0916  -0.0042 -0.0350 855  LYS B CG  
7794  C  CD  . LYS B 855  ? 0.7045 0.7664 0.8670 0.0893  -0.0034 -0.0353 855  LYS B CD  
7795  C  CE  . LYS B 855  ? 0.7178 0.7790 0.8854 0.0860  -0.0003 -0.0328 855  LYS B CE  
7796  N  NZ  . LYS B 855  ? 0.7697 0.8257 0.9422 0.0830  0.0005  -0.0335 855  LYS B NZ  
7797  N  N   . ALA B 856  ? 0.5246 0.6053 0.6702 0.0974  -0.0020 -0.0323 856  ALA B N   
7798  C  CA  . ALA B 856  ? 0.4893 0.5716 0.6301 0.0999  -0.0021 -0.0324 856  ALA B CA  
7799  C  C   . ALA B 856  ? 0.5542 0.6375 0.6919 0.1035  -0.0047 -0.0350 856  ALA B C   
7800  O  O   . ALA B 856  ? 0.5646 0.6535 0.7036 0.1041  -0.0064 -0.0369 856  ALA B O   
7801  C  CB  . ALA B 856  ? 0.5298 0.6194 0.6712 0.0985  -0.0013 -0.0321 856  ALA B CB  
7802  N  N   . PRO B 857  ? 0.6518 0.7299 0.7848 0.1065  -0.0049 -0.0351 857  PRO B N   
7803  C  CA  . PRO B 857  ? 0.6293 0.7084 0.7588 0.1107  -0.0074 -0.0375 857  PRO B CA  
7804  C  C   . PRO B 857  ? 0.6342 0.7231 0.7630 0.1125  -0.0085 -0.0391 857  PRO B C   
7805  O  O   . PRO B 857  ? 0.7011 0.7931 0.8282 0.1158  -0.0105 -0.0414 857  PRO B O   
7806  C  CB  . PRO B 857  ? 0.5859 0.6558 0.7100 0.1136  -0.0069 -0.0366 857  PRO B CB  
7807  C  CG  . PRO B 857  ? 0.5581 0.6256 0.6820 0.1115  -0.0043 -0.0339 857  PRO B CG  
7808  C  CD  . PRO B 857  ? 0.6362 0.7065 0.7663 0.1067  -0.0029 -0.0328 857  PRO B CD  
7809  N  N   . CYS B 858  ? 0.6097 0.7036 0.7396 0.1105  -0.0071 -0.0380 858  CYS B N   
7810  C  CA  . CYS B 858  ? 0.5589 0.6625 0.6888 0.1114  -0.0079 -0.0397 858  CYS B CA  
7811  C  C   . CYS B 858  ? 0.6951 0.8057 0.8286 0.1097  -0.0081 -0.0410 858  CYS B C   
7812  O  O   . CYS B 858  ? 0.6934 0.8123 0.8272 0.1104  -0.0086 -0.0427 858  CYS B O   
7813  C  CB  . CYS B 858  ? 0.5946 0.7004 0.7244 0.1093  -0.0062 -0.0384 858  CYS B CB  
7814  S  SG  . CYS B 858  ? 0.7105 0.8149 0.8440 0.1038  -0.0034 -0.0358 858  CYS B SG  
7815  N  N   . GLU B 859  ? 0.9853 1.0928 1.1213 0.1075  -0.0078 -0.0403 859  GLU B N   
7816  C  CA  . GLU B 859  ? 1.0332 1.1463 1.1717 0.1062  -0.0080 -0.0413 859  GLU B CA  
7817  C  C   . GLU B 859  ? 0.9599 1.0730 1.0974 0.1091  -0.0103 -0.0436 859  GLU B C   
7818  O  O   . GLU B 859  ? 0.9626 1.0815 1.1007 0.1094  -0.0107 -0.0449 859  GLU B O   
7819  C  CB  . GLU B 859  ? 0.9557 1.0661 1.0973 0.1026  -0.0067 -0.0394 859  GLU B CB  
7820  C  CG  . GLU B 859  ? 0.8694 0.9798 1.0116 0.0998  -0.0042 -0.0371 859  GLU B CG  
7821  C  CD  . GLU B 859  ? 0.9787 1.0850 1.1237 0.0971  -0.0029 -0.0351 859  GLU B CD  
7822  O  OE1 . GLU B 859  ? 1.0011 1.1046 1.1481 0.0972  -0.0041 -0.0355 859  GLU B OE1 
7823  O  OE2 . GLU B 859  ? 1.0019 1.1079 1.1473 0.0948  -0.0007 -0.0331 859  GLU B OE2 
7824  N  N   . VAL B 860  ? 0.6940 0.8003 0.8295 0.1114  -0.0116 -0.0440 860  VAL B N   
7825  C  CA  . VAL B 860  ? 0.6780 0.7828 0.8121 0.1141  -0.0138 -0.0463 860  VAL B CA  
7826  C  C   . VAL B 860  ? 0.7101 0.8184 0.8406 0.1187  -0.0150 -0.0482 860  VAL B C   
7827  O  O   . VAL B 860  ? 0.8448 0.9507 0.9729 0.1220  -0.0168 -0.0501 860  VAL B O   
7828  C  CB  . VAL B 860  ? 0.7760 0.8707 0.9098 0.1138  -0.0144 -0.0460 860  VAL B CB  
7829  C  CG1 . VAL B 860  ? 0.8193 0.9121 0.9575 0.1094  -0.0133 -0.0444 860  VAL B CG1 
7830  C  CG2 . VAL B 860  ? 0.6656 0.7538 0.7958 0.1156  -0.0137 -0.0449 860  VAL B CG2 
7831  N  N   . VAL B 861  ? 0.5311 0.6454 0.6614 0.1191  -0.0141 -0.0480 861  VAL B N   
7832  C  CA  . VAL B 861  ? 0.5918 0.7108 0.7194 0.1237  -0.0154 -0.0499 861  VAL B CA  
7833  C  C   . VAL B 861  ? 0.5538 0.6847 0.6837 0.1232  -0.0147 -0.0512 861  VAL B C   
7834  O  O   . VAL B 861  ? 0.6484 0.7852 0.7771 0.1271  -0.0158 -0.0533 861  VAL B O   
7835  C  CB  . VAL B 861  ? 0.6023 0.7168 0.7265 0.1260  -0.0156 -0.0491 861  VAL B CB  
7836  C  CG1 . VAL B 861  ? 0.5534 0.6561 0.6742 0.1278  -0.0162 -0.0485 861  VAL B CG1 
7837  C  CG2 . VAL B 861  ? 0.6938 0.8084 0.8198 0.1221  -0.0136 -0.0468 861  VAL B CG2 
7838  N  N   . CYS B 862  ? 0.5344 0.6692 0.6675 0.1187  -0.0127 -0.0500 862  CYS B N   
7839  C  CA  . CYS B 862  ? 0.6342 0.7796 0.7694 0.1177  -0.0116 -0.0511 862  CYS B CA  
7840  C  C   . CYS B 862  ? 0.5837 0.7329 0.7194 0.1181  -0.0114 -0.0525 862  CYS B C   
7841  O  O   . CYS B 862  ? 0.7344 0.8804 0.8709 0.1155  -0.0107 -0.0513 862  CYS B O   
7842  C  CB  . CYS B 862  ? 0.6135 0.7599 0.7508 0.1127  -0.0092 -0.0492 862  CYS B CB  
7843  S  SG  . CYS B 862  ? 0.5815 0.7390 0.7208 0.1111  -0.0078 -0.0506 862  CYS B SG  
7844  N  N   . PRO B 863  ? 0.5373 0.6936 0.6726 0.1214  -0.0121 -0.0548 863  PRO B N   
7845  C  CA  . PRO B 863  ? 0.6805 0.8389 0.8152 0.1226  -0.0121 -0.0561 863  PRO B CA  
7846  C  C   . PRO B 863  ? 0.5836 0.7467 0.7203 0.1187  -0.0094 -0.0555 863  PRO B C   
7847  O  O   . PRO B 863  ? 0.6260 0.7884 0.7614 0.1194  -0.0094 -0.0560 863  PRO B O   
7848  C  CB  . PRO B 863  ? 0.6891 0.8546 0.8229 0.1275  -0.0131 -0.0588 863  PRO B CB  
7849  C  CG  . PRO B 863  ? 0.6094 0.7803 0.7450 0.1273  -0.0128 -0.0590 863  PRO B CG  
7850  C  CD  . PRO B 863  ? 0.5912 0.7531 0.7260 0.1250  -0.0131 -0.0566 863  PRO B CD  
7851  N  N   . VAL B 864  ? 0.3129 0.4799 0.4518 0.1149  -0.0072 -0.0545 864  VAL B N   
7852  C  CA  . VAL B 864  ? 0.3949 0.5656 0.5349 0.1111  -0.0042 -0.0538 864  VAL B CA  
7853  C  C   . VAL B 864  ? 0.3977 0.5615 0.5376 0.1073  -0.0032 -0.0511 864  VAL B C   
7854  O  O   . VAL B 864  ? 0.3201 0.4855 0.4603 0.1039  -0.0004 -0.0500 864  VAL B O   
7855  C  CB  . VAL B 864  ? 0.3399 0.5202 0.4825 0.1091  -0.0020 -0.0548 864  VAL B CB  
7856  C  CG1 . VAL B 864  ? 0.4256 0.6145 0.5688 0.1128  -0.0025 -0.0577 864  VAL B CG1 
7857  C  CG2 . VAL B 864  ? 0.3646 0.5442 0.5084 0.1077  -0.0026 -0.0543 864  VAL B CG2 
7858  N  N   . ALA B 865  ? 0.7259 0.8817 0.8653 0.1079  -0.0051 -0.0499 865  ALA B N   
7859  C  CA  . ALA B 865  ? 0.6247 0.7741 0.7644 0.1048  -0.0043 -0.0474 865  ALA B CA  
7860  C  C   . ALA B 865  ? 0.6104 0.7611 0.7512 0.1009  -0.0016 -0.0458 865  ALA B C   
7861  O  O   . ALA B 865  ? 0.6022 0.7502 0.7429 0.0981  0.0002  -0.0439 865  ALA B O   
7862  C  CB  . ALA B 865  ? 0.6599 0.8080 0.7986 0.1047  -0.0040 -0.0472 865  ALA B CB  
7863  N  N   . ALA B 866  ? 0.6040 0.7588 0.7455 0.1008  -0.0014 -0.0466 866  ALA B N   
7864  C  CA  . ALA B 866  ? 0.4970 0.6528 0.6392 0.0970  0.0009  -0.0455 866  ALA B CA  
7865  C  C   . ALA B 866  ? 0.5744 0.7224 0.7161 0.0957  0.0008  -0.0432 866  ALA B C   
7866  O  O   . ALA B 866  ? 0.5252 0.6719 0.6669 0.0924  0.0029  -0.0417 866  ALA B O   
7867  C  CB  . ALA B 866  ? 0.4786 0.6420 0.6218 0.0973  0.0008  -0.0476 866  ALA B CB  
7868  N  N   . THR B 867  ? 0.8444 0.9869 0.9857 0.0983  -0.0014 -0.0428 867  THR B N   
7869  C  CA  . THR B 867  ? 0.6683 0.8031 0.8094 0.0972  -0.0012 -0.0405 867  THR B CA  
7870  C  C   . THR B 867  ? 0.7214 0.8509 0.8633 0.0977  -0.0021 -0.0396 867  THR B C   
7871  O  O   . THR B 867  ? 0.7676 0.8950 0.9092 0.1004  -0.0042 -0.0408 867  THR B O   
7872  C  CB  . THR B 867  ? 0.7954 0.9279 0.9351 0.0997  -0.0027 -0.0409 867  THR B CB  
7873  O  OG1 . THR B 867  ? 0.8329 0.9723 0.9722 0.1002  -0.0028 -0.0427 867  THR B OG1 
7874  C  CG2 . THR B 867  ? 0.7509 0.8762 0.8900 0.0980  -0.0016 -0.0384 867  THR B CG2 
7875  N  N   . VAL B 868  ? 0.5898 0.7171 0.7327 0.0951  -0.0004 -0.0378 868  VAL B N   
7876  C  CA  . VAL B 868  ? 0.5990 0.7223 0.7433 0.0953  -0.0013 -0.0371 868  VAL B CA  
7877  C  C   . VAL B 868  ? 0.5249 0.6430 0.6706 0.0931  0.0001  -0.0345 868  VAL B C   
7878  O  O   . VAL B 868  ? 0.6242 0.7408 0.7690 0.0919  0.0017  -0.0334 868  VAL B O   
7879  C  CB  . VAL B 868  ? 0.6166 0.7432 0.7605 0.0951  -0.0010 -0.0376 868  VAL B CB  
7880  C  CG1 . VAL B 868  ? 0.6068 0.7383 0.7493 0.0975  -0.0023 -0.0401 868  VAL B CG1 
7881  C  CG2 . VAL B 868  ? 0.4836 0.6115 0.6264 0.0923  0.0020  -0.0360 868  VAL B CG2 
7882  N  N   . HIS B 869  ? 0.5757 0.6912 0.7235 0.0928  -0.0004 -0.0338 869  HIS B N   
7883  C  CA  . HIS B 869  ? 0.6127 0.7239 0.7625 0.0910  0.0011  -0.0315 869  HIS B CA  
7884  C  C   . HIS B 869  ? 0.6590 0.7715 0.8090 0.0898  0.0025  -0.0302 869  HIS B C   
7885  O  O   . HIS B 869  ? 0.7288 0.8445 0.8778 0.0906  0.0018  -0.0312 869  HIS B O   
7886  C  CB  . HIS B 869  ? 0.6941 0.8012 0.8470 0.0915  -0.0006 -0.0317 869  HIS B CB  
7887  C  CG  . HIS B 869  ? 0.6162 0.7183 0.7704 0.0903  0.0012  -0.0297 869  HIS B CG  
7888  N  ND1 . HIS B 869  ? 0.5485 0.6475 0.7004 0.0909  0.0017  -0.0294 869  HIS B ND1 
7889  C  CD2 . HIS B 869  ? 0.6588 0.7584 0.8161 0.0886  0.0027  -0.0277 869  HIS B CD2 
7890  C  CE1 . HIS B 869  ? 0.6373 0.7315 0.7903 0.0897  0.0036  -0.0273 869  HIS B CE1 
7891  N  NE2 . HIS B 869  ? 0.6559 0.7506 0.8126 0.0882  0.0043  -0.0263 869  HIS B NE2 
7892  N  N   . ASP B 870  ? 0.8032 0.9129 0.9540 0.0881  0.0047  -0.0279 870  ASP B N   
7893  C  CA  . ASP B 870  ? 0.8425 0.9526 0.9926 0.0872  0.0066  -0.0263 870  ASP B CA  
7894  C  C   . ASP B 870  ? 0.8245 0.9334 0.9784 0.0877  0.0057  -0.0255 870  ASP B C   
7895  O  O   . ASP B 870  ? 0.8565 0.9637 1.0141 0.0878  0.0044  -0.0259 870  ASP B O   
7896  C  CB  . ASP B 870  ? 0.8537 0.9613 1.0015 0.0854  0.0097  -0.0243 870  ASP B CB  
7897  C  CG  . ASP B 870  ? 0.9233 1.0303 1.0689 0.0846  0.0120  -0.0226 870  ASP B CG  
7898  O  OD1 . ASP B 870  ? 1.0546 1.1642 1.1977 0.0848  0.0122  -0.0234 870  ASP B OD1 
7899  O  OD2 . ASP B 870  ? 0.9966 1.1004 1.1428 0.0840  0.0138  -0.0205 870  ASP B OD2 
7900  N  N   . TYR B 871  ? 0.5774 0.6873 0.7302 0.0880  0.0065  -0.0246 871  TYR B N   
7901  C  CA  . TYR B 871  ? 0.6001 0.7100 0.7568 0.0886  0.0057  -0.0239 871  TYR B CA  
7902  C  C   . TYR B 871  ? 0.5801 0.6870 0.7402 0.0874  0.0075  -0.0220 871  TYR B C   
7903  O  O   . TYR B 871  ? 0.5443 0.6514 0.7097 0.0874  0.0063  -0.0222 871  TYR B O   
7904  C  CB  . TYR B 871  ? 0.6340 0.7449 0.7877 0.0897  0.0066  -0.0230 871  TYR B CB  
7905  C  CG  . TYR B 871  ? 0.5946 0.7066 0.7519 0.0912  0.0053  -0.0226 871  TYR B CG  
7906  C  CD1 . TYR B 871  ? 0.5948 0.7098 0.7550 0.0927  0.0016  -0.0248 871  TYR B CD1 
7907  C  CD2 . TYR B 871  ? 0.6403 0.7508 0.7983 0.0911  0.0076  -0.0202 871  TYR B CD2 
7908  C  CE1 . TYR B 871  ? 0.5564 0.6735 0.7204 0.0941  0.0000  -0.0249 871  TYR B CE1 
7909  C  CE2 . TYR B 871  ? 0.5709 0.6835 0.7327 0.0928  0.0063  -0.0200 871  TYR B CE2 
7910  C  CZ  . TYR B 871  ? 0.5149 0.6312 0.6800 0.0942  0.0023  -0.0224 871  TYR B CZ  
7911  O  OH  . TYR B 871  ? 0.5064 0.6258 0.6759 0.0959  0.0006  -0.0226 871  TYR B OH  
7912  N  N   . GLU B 872  ? 0.8142 0.9183 0.9712 0.0861  0.0104  -0.0202 872  GLU B N   
7913  C  CA  . GLU B 872  ? 0.8064 0.9070 0.9654 0.0851  0.0127  -0.0182 872  GLU B CA  
7914  C  C   . GLU B 872  ? 0.8932 0.9913 1.0535 0.0844  0.0123  -0.0187 872  GLU B C   
7915  O  O   . GLU B 872  ? 0.8771 0.9716 1.0377 0.0836  0.0146  -0.0169 872  GLU B O   
7916  C  CB  . GLU B 872  ? 0.7947 0.8926 0.9489 0.0843  0.0160  -0.0161 872  GLU B CB  
7917  C  CG  . GLU B 872  ? 0.8698 0.9677 1.0235 0.0851  0.0175  -0.0144 872  GLU B CG  
7918  C  CD  . GLU B 872  ? 0.9870 1.0865 1.1362 0.0858  0.0173  -0.0151 872  GLU B CD  
7919  O  OE1 . GLU B 872  ? 0.9760 1.0766 1.1222 0.0851  0.0168  -0.0165 872  GLU B OE1 
7920  O  OE2 . GLU B 872  ? 1.0322 1.1320 1.1808 0.0874  0.0177  -0.0141 872  GLU B OE2 
7921  N  N   . GLY B 873  ? 0.7935 0.8929 0.9539 0.0851  0.0097  -0.0209 873  GLY B N   
7922  C  CA  . GLY B 873  ? 0.7866 0.8829 0.9472 0.0850  0.0093  -0.0214 873  GLY B CA  
7923  C  C   . GLY B 873  ? 0.7015 0.7966 0.8570 0.0851  0.0102  -0.0215 873  GLY B C   
7924  O  O   . GLY B 873  ? 0.6912 0.7832 0.8458 0.0857  0.0099  -0.0217 873  GLY B O   
7925  N  N   . LEU B 874  ? 0.4454 0.5426 0.5974 0.0847  0.0113  -0.0213 874  LEU B N   
7926  C  CA  . LEU B 874  ? 0.3504 0.4477 0.4981 0.0845  0.0118  -0.0218 874  LEU B CA  
7927  C  C   . LEU B 874  ? 0.4796 0.5807 0.6266 0.0860  0.0092  -0.0245 874  LEU B C   
7928  O  O   . LEU B 874  ? 0.5672 0.6710 0.7159 0.0869  0.0073  -0.0259 874  LEU B O   
7929  C  CB  . LEU B 874  ? 0.5205 0.6190 0.6652 0.0830  0.0140  -0.0210 874  LEU B CB  
7930  C  CG  . LEU B 874  ? 0.5405 0.6393 0.6811 0.0821  0.0150  -0.0216 874  LEU B CG  
7931  C  CD1 . LEU B 874  ? 0.5432 0.6369 0.6824 0.0821  0.0161  -0.0201 874  LEU B CD1 
7932  C  CD2 . LEU B 874  ? 0.4836 0.5832 0.6214 0.0801  0.0172  -0.0211 874  LEU B CD2 
7933  N  N   . ASN B 875  ? 0.4326 0.5338 0.5767 0.0865  0.0089  -0.0253 875  ASN B N   
7934  C  CA  . ASN B 875  ? 0.4724 0.5776 0.6157 0.0883  0.0066  -0.0279 875  ASN B CA  
7935  C  C   . ASN B 875  ? 0.4097 0.5205 0.5511 0.0872  0.0073  -0.0290 875  ASN B C   
7936  O  O   . ASN B 875  ? 0.4512 0.5622 0.5903 0.0863  0.0084  -0.0289 875  ASN B O   
7937  C  CB  . ASN B 875  ? 0.4576 0.5597 0.5989 0.0902  0.0057  -0.0282 875  ASN B CB  
7938  C  CG  . ASN B 875  ? 0.4563 0.5624 0.5965 0.0928  0.0031  -0.0309 875  ASN B CG  
7939  O  OD1 . ASN B 875  ? 0.4686 0.5798 0.6099 0.0931  0.0021  -0.0325 875  ASN B OD1 
7940  N  ND2 . ASN B 875  ? 0.6540 0.7577 0.7916 0.0951  0.0023  -0.0313 875  ASN B ND2 
7941  N  N   . ASN B 876  ? 0.8535 0.9686 0.9956 0.0873  0.0067  -0.0303 876  ASN B N   
7942  C  CA  . ASN B 876  ? 0.7913 0.9117 0.9320 0.0858  0.0080  -0.0313 876  ASN B CA  
7943  C  C   . ASN B 876  ? 0.8009 0.9266 0.9411 0.0873  0.0063  -0.0339 876  ASN B C   
7944  O  O   . ASN B 876  ? 0.8985 1.0262 1.0395 0.0899  0.0041  -0.0354 876  ASN B O   
7945  C  CB  . ASN B 876  ? 0.8287 0.9510 0.9696 0.0856  0.0084  -0.0314 876  ASN B CB  
7946  C  CG  . ASN B 876  ? 0.9144 1.0321 1.0557 0.0846  0.0098  -0.0290 876  ASN B CG  
7947  O  OD1 . ASN B 876  ? 1.0003 1.1138 1.1415 0.0836  0.0111  -0.0271 876  ASN B OD1 
7948  N  ND2 . ASN B 876  ? 0.9439 1.0626 1.0853 0.0854  0.0095  -0.0290 876  ASN B ND2 
7949  N  N   . MET B 877  ? 0.3587 0.4869 0.4976 0.0858  0.0073  -0.0346 877  MET B N   
7950  C  CA  . MET B 877  ? 0.3920 0.5271 0.5311 0.0870  0.0059  -0.0373 877  MET B CA  
7951  C  C   . MET B 877  ? 0.4551 0.5961 0.5944 0.0840  0.0080  -0.0385 877  MET B C   
7952  O  O   . MET B 877  ? 0.4191 0.5592 0.5573 0.0809  0.0101  -0.0379 877  MET B O   
7953  C  CB  . MET B 877  ? 0.4643 0.5981 0.6019 0.0880  0.0049  -0.0376 877  MET B CB  
7954  C  CG  . MET B 877  ? 0.4611 0.6031 0.5990 0.0888  0.0036  -0.0406 877  MET B CG  
7955  S  SD  . MET B 877  ? 0.5308 0.6779 0.6698 0.0937  0.0006  -0.0430 877  MET B SD  
7956  C  CE  . MET B 877  ? 0.5104 0.6693 0.6521 0.0918  0.0015  -0.0459 877  MET B CE  
7957  N  N   . VAL B 878  ? 0.6362 0.7828 0.7767 0.0848  0.0078  -0.0401 878  VAL B N   
7958  C  CA  . VAL B 878  ? 0.6208 0.7724 0.7615 0.0818  0.0104  -0.0410 878  VAL B CA  
7959  C  C   . VAL B 878  ? 0.6853 0.8460 0.8278 0.0820  0.0097  -0.0441 878  VAL B C   
7960  O  O   . VAL B 878  ? 0.7274 0.8927 0.8712 0.0855  0.0075  -0.0459 878  VAL B O   
7961  C  CB  . VAL B 878  ? 0.4403 0.5918 0.5805 0.0827  0.0110  -0.0406 878  VAL B CB  
7962  C  CG1 . VAL B 878  ? 0.5375 0.6913 0.6766 0.0792  0.0146  -0.0406 878  VAL B CG1 
7963  C  CG2 . VAL B 878  ? 0.5227 0.6664 0.6620 0.0839  0.0104  -0.0381 878  VAL B CG2 
7964  N  N   . TYR B 879  ? 0.6799 0.8435 0.8226 0.0783  0.0116  -0.0449 879  TYR B N   
7965  C  CA  . TYR B 879  ? 0.6614 0.8345 0.8067 0.0782  0.0106  -0.0482 879  TYR B CA  
7966  C  C   . TYR B 879  ? 0.6250 0.8066 0.7727 0.0781  0.0117  -0.0502 879  TYR B C   
7967  O  O   . TYR B 879  ? 0.6396 0.8291 0.7898 0.0809  0.0097  -0.0528 879  TYR B O   
7968  C  CB  . TYR B 879  ? 0.5023 0.6760 0.6472 0.0737  0.0122  -0.0488 879  TYR B CB  
7969  C  CG  . TYR B 879  ? 0.5470 0.7113 0.6888 0.0733  0.0121  -0.0463 879  TYR B CG  
7970  C  CD1 . TYR B 879  ? 0.6659 0.8274 0.8067 0.0771  0.0090  -0.0460 879  TYR B CD1 
7971  C  CD2 . TYR B 879  ? 0.6204 0.7781 0.7596 0.0694  0.0152  -0.0443 879  TYR B CD2 
7972  C  CE1 . TYR B 879  ? 0.6495 0.8023 0.7872 0.0768  0.0093  -0.0437 879  TYR B CE1 
7973  C  CE2 . TYR B 879  ? 0.6537 0.8030 0.7899 0.0693  0.0153  -0.0420 879  TYR B CE2 
7974  C  CZ  . TYR B 879  ? 0.5392 0.6863 0.6749 0.0729  0.0124  -0.0418 879  TYR B CZ  
7975  O  OH  . TYR B 879  ? 0.4895 0.6282 0.6221 0.0728  0.0129  -0.0394 879  TYR B OH  
7976  N  N   . ASN B 880  ? 0.7681 0.9480 0.9147 0.0752  0.0152  -0.0491 880  ASN B N   
7977  C  CA  . ASN B 880  ? 0.8025 0.9903 0.9510 0.0745  0.0171  -0.0510 880  ASN B CA  
7978  C  C   . ASN B 880  ? 0.9105 1.1003 1.0593 0.0797  0.0149  -0.0515 880  ASN B C   
7979  O  O   . ASN B 880  ? 0.9164 1.1143 1.0672 0.0804  0.0157  -0.0536 880  ASN B O   
7980  C  CB  . ASN B 880  ? 0.7574 0.9412 0.9032 0.0704  0.0217  -0.0493 880  ASN B CB  
7981  C  CG  . ASN B 880  ? 0.8624 1.0360 1.0042 0.0720  0.0217  -0.0460 880  ASN B CG  
7982  O  OD1 . ASN B 880  ? 0.9634 1.1342 1.1050 0.0762  0.0186  -0.0453 880  ASN B OD1 
7983  N  ND2 . ASN B 880  ? 0.7655 0.9333 0.9040 0.0686  0.0254  -0.0440 880  ASN B ND2 
7984  N  N   . ARG B 881  ? 0.8053 0.9879 0.9521 0.0832  0.0122  -0.0498 881  ARG B N   
7985  C  CA  . ARG B 881  ? 0.7838 0.9672 0.9304 0.0881  0.0099  -0.0505 881  ARG B CA  
7986  C  C   . ARG B 881  ? 0.7435 0.9306 0.8915 0.0923  0.0063  -0.0525 881  ARG B C   
7987  O  O   . ARG B 881  ? 0.7465 0.9378 0.8950 0.0961  0.0049  -0.0541 881  ARG B O   
7988  C  CB  . ARG B 881  ? 0.8091 0.9828 0.9528 0.0895  0.0090  -0.0480 881  ARG B CB  
7989  C  CG  . ARG B 881  ? 0.6991 0.8723 0.8420 0.0942  0.0065  -0.0488 881  ARG B CG  
7990  C  CD  . ARG B 881  ? 0.6507 0.8296 0.7931 0.0948  0.0083  -0.0502 881  ARG B CD  
7991  N  NE  . ARG B 881  ? 0.7889 0.9666 0.9299 0.0995  0.0058  -0.0510 881  ARG B NE  
7992  C  CZ  . ARG B 881  ? 0.8942 1.0754 1.0339 0.1011  0.0069  -0.0522 881  ARG B CZ  
7993  N  NH1 . ARG B 881  ? 0.8965 1.0827 1.0362 0.0985  0.0107  -0.0524 881  ARG B NH1 
7994  N  NH2 . ARG B 881  ? 0.9106 1.0898 1.0485 0.1055  0.0042  -0.0531 881  ARG B NH2 
7995  N  N   . CYS B 882  ? 0.4671 0.6524 0.6153 0.0920  0.0048  -0.0523 882  CYS B N   
7996  C  CA  . CYS B 882  ? 0.6024 0.7902 0.7510 0.0964  0.0014  -0.0539 882  CYS B CA  
7997  C  C   . CYS B 882  ? 0.5777 0.7777 0.7294 0.0978  0.0011  -0.0573 882  CYS B C   
7998  O  O   . CYS B 882  ? 0.4859 0.6931 0.6404 0.0940  0.0031  -0.0587 882  CYS B O   
7999  C  CB  . CYS B 882  ? 0.5534 0.7371 0.7010 0.0955  0.0005  -0.0530 882  CYS B CB  
8000  S  SG  . CYS B 882  ? 0.4084 0.5924 0.5547 0.1013  -0.0035 -0.0544 882  CYS B SG  
8001  N  N   . VAL B 883  ? 0.6405 0.8431 0.7919 0.1031  -0.0012 -0.0588 883  VAL B N   
8002  C  CA  . VAL B 883  ? 0.6051 0.8198 0.7596 0.1055  -0.0018 -0.0621 883  VAL B CA  
8003  C  C   . VAL B 883  ? 0.6167 0.8344 0.7714 0.1088  -0.0050 -0.0636 883  VAL B C   
8004  O  O   . VAL B 883  ? 0.6496 0.8788 0.8078 0.1098  -0.0055 -0.0666 883  VAL B O   
8005  C  CB  . VAL B 883  ? 0.6269 0.8434 0.7806 0.1100  -0.0024 -0.0631 883  VAL B CB  
8006  C  CG1 . VAL B 883  ? 0.5573 0.7744 0.7113 0.1069  0.0011  -0.0624 883  VAL B CG1 
8007  C  CG2 . VAL B 883  ? 0.4731 0.6789 0.6225 0.1143  -0.0052 -0.0616 883  VAL B CG2 
8008  N  N   . GLY B 884  ? 0.8704 1.0782 1.0214 0.1105  -0.0070 -0.0617 884  GLY B N   
8009  C  CA  . GLY B 884  ? 0.7896 0.9983 0.9394 0.1137  -0.0098 -0.0627 884  GLY B CA  
8010  C  C   . GLY B 884  ? 0.7710 0.9771 0.9175 0.1210  -0.0129 -0.0633 884  GLY B C   
8011  O  O   . GLY B 884  ? 0.7903 1.0023 0.9366 0.1250  -0.0153 -0.0654 884  GLY B O   
8012  N  N   . THR B 885  ? 0.9445 1.1418 1.0880 0.1231  -0.0131 -0.0617 885  THR B N   
8013  C  CA  . THR B 885  ? 0.8887 1.0820 1.0283 0.1299  -0.0158 -0.0623 885  THR B CA  
8014  C  C   . THR B 885  ? 0.8893 1.0750 1.0245 0.1326  -0.0178 -0.0612 885  THR B C   
8015  O  O   . THR B 885  ? 0.8847 1.0679 1.0161 0.1388  -0.0201 -0.0620 885  THR B O   
8016  C  CB  . THR B 885  ? 0.8091 0.9936 0.9464 0.1306  -0.0155 -0.0609 885  THR B CB  
8017  O  OG1 . THR B 885  ? 0.8953 1.0674 1.0300 0.1283  -0.0151 -0.0579 885  THR B OG1 
8018  C  CG2 . THR B 885  ? 0.8584 1.0481 0.9990 0.1270  -0.0131 -0.0612 885  THR B CG2 
8019  N  N   . LYS B 886  ? 0.7395 0.9207 0.8745 0.1285  -0.0167 -0.0593 886  LYS B N   
8020  C  CA  . LYS B 886  ? 0.6731 0.8462 0.8034 0.1306  -0.0180 -0.0579 886  LYS B CA  
8021  C  C   . LYS B 886  ? 0.6567 0.8166 0.7818 0.1339  -0.0186 -0.0559 886  LYS B C   
8022  O  O   . LYS B 886  ? 0.6254 0.7777 0.7455 0.1370  -0.0197 -0.0548 886  LYS B O   
8023  C  CB  . LYS B 886  ? 0.6527 0.8338 0.7821 0.1352  -0.0207 -0.0605 886  LYS B CB  
8024  C  CG  . LYS B 886  ? 0.5957 0.7896 0.7304 0.1313  -0.0201 -0.0627 886  LYS B CG  
8025  C  CD  . LYS B 886  ? 0.6872 0.8923 0.8226 0.1363  -0.0231 -0.0662 886  LYS B CD  
8026  C  CE  . LYS B 886  ? 0.7777 0.9900 0.9150 0.1407  -0.0239 -0.0683 886  LYS B CE  
8027  N  NZ  . LYS B 886  ? 0.6576 0.8786 0.8013 0.1358  -0.0213 -0.0694 886  LYS B NZ  
8028  N  N   . TYR B 887  ? 0.7426 0.8991 0.8686 0.1332  -0.0179 -0.0554 887  TYR B N   
8029  C  CA  . TYR B 887  ? 0.8225 0.9669 0.9443 0.1356  -0.0183 -0.0539 887  TYR B CA  
8030  C  C   . TYR B 887  ? 0.7650 0.8991 0.8866 0.1310  -0.0164 -0.0508 887  TYR B C   
8031  O  O   . TYR B 887  ? 0.7563 0.8794 0.8739 0.1327  -0.0166 -0.0492 887  TYR B O   
8032  C  CB  . TYR B 887  ? 0.7892 0.9355 0.9122 0.1368  -0.0187 -0.0553 887  TYR B CB  
8033  C  CG  . TYR B 887  ? 0.7168 0.8515 0.8359 0.1392  -0.0194 -0.0546 887  TYR B CG  
8034  C  CD1 . TYR B 887  ? 0.8401 0.9641 0.9537 0.1422  -0.0201 -0.0534 887  TYR B CD1 
8035  C  CD2 . TYR B 887  ? 0.7880 0.9222 0.9084 0.1383  -0.0193 -0.0553 887  TYR B CD2 
8036  C  CE1 . TYR B 887  ? 0.9244 1.0374 1.0345 0.1437  -0.0204 -0.0529 887  TYR B CE1 
8037  C  CE2 . TYR B 887  ? 0.8343 0.9580 0.9513 0.1401  -0.0201 -0.0550 887  TYR B CE2 
8038  C  CZ  . TYR B 887  ? 0.9527 1.0659 1.0648 0.1425  -0.0206 -0.0539 887  TYR B CZ  
8039  O  OH  . TYR B 887  ? 1.0227 1.1249 1.1315 0.1438  -0.0211 -0.0538 887  TYR B OH  
8040  N  N   . CYS B 888  ? 0.7694 0.9071 0.8950 0.1254  -0.0145 -0.0498 888  CYS B N   
8041  C  CA  . CYS B 888  ? 0.7573 0.8866 0.8833 0.1212  -0.0125 -0.0469 888  CYS B CA  
8042  C  C   . CYS B 888  ? 0.7344 0.8584 0.8571 0.1214  -0.0121 -0.0453 888  CYS B C   
8043  O  O   . CYS B 888  ? 0.6847 0.7996 0.8065 0.1194  -0.0106 -0.0427 888  CYS B O   
8044  C  CB  . CYS B 888  ? 0.8414 0.9756 0.9719 0.1158  -0.0105 -0.0464 888  CYS B CB  
8045  S  SG  . CYS B 888  ? 1.0815 1.2253 1.2144 0.1126  -0.0093 -0.0473 888  CYS B SG  
8046  N  N   . SER B 889  ? 0.7836 0.9126 0.9042 0.1245  -0.0136 -0.0468 889  SER B N   
8047  C  CA  . SER B 889  ? 0.7097 0.8326 0.8257 0.1259  -0.0136 -0.0454 889  SER B CA  
8048  C  C   . SER B 889  ? 0.7451 0.8582 0.8551 0.1312  -0.0146 -0.0447 889  SER B C   
8049  O  O   . SER B 889  ? 0.7170 0.8197 0.8231 0.1313  -0.0134 -0.0422 889  SER B O   
8050  C  CB  . SER B 889  ? 0.7889 0.9213 0.9048 0.1270  -0.0150 -0.0475 889  SER B CB  
8051  O  OG  . SER B 889  ? 0.7319 0.8582 0.8428 0.1286  -0.0151 -0.0463 889  SER B OG  
8052  N  N   . ASN B 890  ? 0.6641 0.7797 0.7730 0.1357  -0.0166 -0.0467 890  ASN B N   
8053  C  CA  . ASN B 890  ? 0.5589 0.6644 0.6612 0.1412  -0.0176 -0.0462 890  ASN B CA  
8054  C  C   . ASN B 890  ? 0.5201 0.6133 0.6218 0.1386  -0.0156 -0.0438 890  ASN B C   
8055  O  O   . ASN B 890  ? 0.5418 0.6235 0.6376 0.1412  -0.0151 -0.0422 890  ASN B O   
8056  C  CB  . ASN B 890  ? 0.5076 0.6188 0.6090 0.1465  -0.0200 -0.0490 890  ASN B CB  
8057  C  CG  . ASN B 890  ? 0.6608 0.7860 0.7642 0.1488  -0.0220 -0.0518 890  ASN B CG  
8058  O  OD1 . ASN B 890  ? 0.7452 0.8735 0.8483 0.1480  -0.0221 -0.0517 890  ASN B OD1 
8059  N  ND2 . ASN B 890  ? 0.6021 0.7360 0.7077 0.1516  -0.0235 -0.0545 890  ASN B ND2 
8060  N  N   . ASN B 891  ? 0.3807 0.4759 0.4882 0.1336  -0.0144 -0.0435 891  ASN B N   
8061  C  CA  . ASN B 891  ? 0.4157 0.5008 0.5239 0.1307  -0.0127 -0.0416 891  ASN B CA  
8062  C  C   . ASN B 891  ? 0.4917 0.5724 0.6014 0.1261  -0.0100 -0.0387 891  ASN B C   
8063  O  O   . ASN B 891  ? 0.5060 0.5787 0.6169 0.1234  -0.0084 -0.0370 891  ASN B O   
8064  C  CB  . ASN B 891  ? 0.4598 0.5492 0.5731 0.1281  -0.0131 -0.0429 891  ASN B CB  
8065  C  CG  . ASN B 891  ? 0.5572 0.6365 0.6698 0.1277  -0.0128 -0.0424 891  ASN B CG  
8066  O  OD1 . ASN B 891  ? 0.5077 0.5771 0.6152 0.1304  -0.0126 -0.0416 891  ASN B OD1 
8067  N  ND2 . ASN B 891  ? 0.5468 0.6282 0.6642 0.1243  -0.0128 -0.0429 891  ASN B ND2 
8068  N  N   . CYS B 892  ? 0.6030 0.6887 0.7128 0.1251  -0.0096 -0.0383 892  CYS B N   
8069  C  CA  . CYS B 892  ? 0.5400 0.6211 0.6505 0.1213  -0.0069 -0.0356 892  CYS B CA  
8070  C  C   . CYS B 892  ? 0.5411 0.6111 0.6448 0.1241  -0.0059 -0.0337 892  CYS B C   
8071  O  O   . CYS B 892  ? 0.5634 0.6342 0.6620 0.1284  -0.0073 -0.0344 892  CYS B O   
8072  C  CB  . CYS B 892  ? 0.5864 0.6762 0.6988 0.1190  -0.0067 -0.0360 892  CYS B CB  
8073  S  SG  . CYS B 892  ? 0.5701 0.6542 0.6826 0.1146  -0.0034 -0.0328 892  CYS B SG  
8074  N  N   . PRO B 893  ? 0.6852 0.7451 0.7888 0.1221  -0.0035 -0.0313 893  PRO B N   
8075  C  CA  . PRO B 893  ? 0.7315 0.7797 0.8279 0.1250  -0.0021 -0.0293 893  PRO B CA  
8076  C  C   . PRO B 893  ? 0.9380 0.9854 1.0306 0.1255  -0.0010 -0.0279 893  PRO B C   
8077  O  O   . PRO B 893  ? 1.0652 1.1057 1.1501 0.1299  -0.0009 -0.0271 893  PRO B O   
8078  C  CB  . PRO B 893  ? 0.8923 0.9317 0.9916 0.1213  0.0008  -0.0273 893  PRO B CB  
8079  C  CG  . PRO B 893  ? 0.8801 0.9264 0.9869 0.1181  -0.0004 -0.0290 893  PRO B CG  
8080  C  CD  . PRO B 893  ? 0.8088 0.8675 0.9186 0.1173  -0.0020 -0.0305 893  PRO B CD  
8081  N  N   . TYR B 894  ? 0.6545 0.7082 0.7514 0.1215  0.0000  -0.0275 894  TYR B N   
8082  C  CA  . TYR B 894  ? 0.5884 0.6409 0.6817 0.1214  0.0012  -0.0261 894  TYR B CA  
8083  C  C   . TYR B 894  ? 0.5399 0.6024 0.6320 0.1234  -0.0017 -0.0287 894  TYR B C   
8084  O  O   . TYR B 894  ? 0.6793 0.7408 0.7673 0.1242  -0.0014 -0.0282 894  TYR B O   
8085  C  CB  . TYR B 894  ? 0.5195 0.5718 0.6177 0.1158  0.0042  -0.0241 894  TYR B CB  
8086  C  CG  . TYR B 894  ? 0.6088 0.6546 0.7109 0.1130  0.0067  -0.0222 894  TYR B CG  
8087  C  CD1 . TYR B 894  ? 0.5833 0.6179 0.6820 0.1131  0.0099  -0.0194 894  TYR B CD1 
8088  C  CD2 . TYR B 894  ? 0.5312 0.5822 0.6403 0.1102  0.0060  -0.0233 894  TYR B CD2 
8089  C  CE1 . TYR B 894  ? 0.5042 0.5337 0.6073 0.1101  0.0122  -0.0180 894  TYR B CE1 
8090  C  CE2 . TYR B 894  ? 0.5348 0.5807 0.6479 0.1076  0.0078  -0.0221 894  TYR B CE2 
8091  C  CZ  . TYR B 894  ? 0.5142 0.5498 0.6248 0.1073  0.0109  -0.0195 894  TYR B CZ  
8092  O  OH  . TYR B 894  ? 0.5385 0.5698 0.6540 0.1043  0.0129  -0.0185 894  TYR B OH  
8093  N  N   . LYS B 895  ? 0.5674 0.6395 0.6630 0.1243  -0.0045 -0.0316 895  LYS B N   
8094  C  CA  . LYS B 895  ? 0.6456 0.7287 0.7413 0.1259  -0.0072 -0.0346 895  LYS B CA  
8095  C  C   . LYS B 895  ? 0.6747 0.7625 0.7727 0.1215  -0.0060 -0.0344 895  LYS B C   
8096  O  O   . LYS B 895  ? 0.6926 0.7813 0.7866 0.1229  -0.0068 -0.0349 895  LYS B O   
8097  C  CB  . LYS B 895  ? 0.6578 0.7384 0.7458 0.1325  -0.0095 -0.0355 895  LYS B CB  
8098  C  CG  . LYS B 895  ? 0.6781 0.7553 0.7633 0.1375  -0.0111 -0.0362 895  LYS B CG  
8099  C  CD  . LYS B 895  ? 0.7779 0.8667 0.8690 0.1375  -0.0132 -0.0393 895  LYS B CD  
8100  C  CE  . LYS B 895  ? 0.7727 0.8578 0.8603 0.1429  -0.0149 -0.0402 895  LYS B CE  
8101  N  NZ  . LYS B 895  ? 0.7228 0.7949 0.8088 0.1418  -0.0125 -0.0377 895  LYS B NZ  
8102  N  N   . VAL B 896  ? 0.6111 0.7013 0.7151 0.1163  -0.0042 -0.0337 896  VAL B N   
8103  C  CA  . VAL B 896  ? 0.5695 0.6627 0.6755 0.1117  -0.0025 -0.0333 896  VAL B CA  
8104  C  C   . VAL B 896  ? 0.5385 0.6436 0.6500 0.1090  -0.0035 -0.0359 896  VAL B C   
8105  O  O   . VAL B 896  ? 0.6421 0.7493 0.7561 0.1045  -0.0017 -0.0355 896  VAL B O   
8106  C  CB  . VAL B 896  ? 0.5698 0.6553 0.6776 0.1080  0.0010  -0.0300 896  VAL B CB  
8107  C  CG1 . VAL B 896  ? 0.6474 0.7215 0.7497 0.1103  0.0026  -0.0273 896  VAL B CG1 
8108  C  CG2 . VAL B 896  ? 0.7446 0.8312 0.8578 0.1064  0.0013  -0.0298 896  VAL B CG2 
8109  N  N   . ARG B 897  ? 0.5904 0.7026 0.7034 0.1117  -0.0060 -0.0386 897  ARG B N   
8110  C  CA  . ARG B 897  ? 0.5525 0.6761 0.6707 0.1093  -0.0066 -0.0412 897  ARG B CA  
8111  C  C   . ARG B 897  ? 0.5712 0.7039 0.6886 0.1115  -0.0092 -0.0444 897  ARG B C   
8112  O  O   . ARG B 897  ? 0.7222 0.8549 0.8362 0.1169  -0.0117 -0.0455 897  ARG B O   
8113  C  CB  . ARG B 897  ? 0.5578 0.6836 0.6791 0.1105  -0.0073 -0.0418 897  ARG B CB  
8114  C  CG  . ARG B 897  ? 0.6172 0.7346 0.7396 0.1085  -0.0053 -0.0391 897  ARG B CG  
8115  C  CD  . ARG B 897  ? 0.6218 0.7415 0.7469 0.1097  -0.0062 -0.0402 897  ARG B CD  
8116  N  NE  . ARG B 897  ? 0.6002 0.7278 0.7297 0.1064  -0.0054 -0.0413 897  ARG B NE  
8117  C  CZ  . ARG B 897  ? 0.6212 0.7467 0.7533 0.1031  -0.0037 -0.0398 897  ARG B CZ  
8118  N  NH1 . ARG B 897  ? 0.7416 0.8586 0.8734 0.1024  -0.0027 -0.0375 897  ARG B NH1 
8119  N  NH2 . ARG B 897  ? 0.6443 0.7766 0.7792 0.1006  -0.0028 -0.0409 897  ARG B NH2 
8120  N  N   . ARG B 898  ? 0.7520 0.8924 0.8725 0.1074  -0.0086 -0.0461 898  ARG B N   
8121  C  CA  . ARG B 898  ? 0.8278 0.9783 0.9488 0.1085  -0.0109 -0.0496 898  ARG B CA  
8122  C  C   . ARG B 898  ? 0.7742 0.9368 0.9014 0.1064  -0.0110 -0.0524 898  ARG B C   
8123  O  O   . ARG B 898  ? 0.7880 0.9510 0.9186 0.1020  -0.0084 -0.0515 898  ARG B O   
8124  C  CB  . ARG B 898  ? 0.7755 0.9247 0.8945 0.1051  -0.0101 -0.0496 898  ARG B CB  
8125  C  CG  . ARG B 898  ? 0.7711 0.9080 0.8836 0.1071  -0.0094 -0.0466 898  ARG B CG  
8126  C  CD  . ARG B 898  ? 0.9065 1.0415 1.0139 0.1140  -0.0125 -0.0473 898  ARG B CD  
8127  N  NE  . ARG B 898  ? 0.8397 0.9649 0.9400 0.1158  -0.0121 -0.0453 898  ARG B NE  
8128  C  CZ  . ARG B 898  ? 0.9007 1.0141 0.9961 0.1188  -0.0109 -0.0421 898  ARG B CZ  
8129  N  NH1 . ARG B 898  ? 0.9910 1.1006 1.0877 0.1201  -0.0103 -0.0407 898  ARG B NH1 
8130  N  NH2 . ARG B 898  ? 0.8618 0.9667 0.9503 0.1203  -0.0103 -0.0404 898  ARG B NH2 
8131  N  N   . PHE B 899  ? 0.5591 0.7316 0.6877 0.1099  -0.0138 -0.0558 899  PHE B N   
8132  C  CA  . PHE B 899  ? 0.4605 0.6453 0.5951 0.1088  -0.0139 -0.0587 899  PHE B CA  
8133  C  C   . PHE B 899  ? 0.4465 0.6431 0.5844 0.1064  -0.0148 -0.0624 899  PHE B C   
8134  O  O   . PHE B 899  ? 0.4692 0.6674 0.6045 0.1090  -0.0174 -0.0639 899  PHE B O   
8135  C  CB  . PHE B 899  ? 0.4365 0.6243 0.5708 0.1153  -0.0164 -0.0599 899  PHE B CB  
8136  C  CG  . PHE B 899  ? 0.4712 0.6705 0.6113 0.1145  -0.0159 -0.0624 899  PHE B CG  
8137  C  CD1 . PHE B 899  ? 0.5385 0.7355 0.6808 0.1114  -0.0132 -0.0609 899  PHE B CD1 
8138  C  CD2 . PHE B 899  ? 0.4806 0.6931 0.6239 0.1171  -0.0181 -0.0663 899  PHE B CD2 
8139  C  CE1 . PHE B 899  ? 0.5947 0.8017 0.7417 0.1109  -0.0124 -0.0630 899  PHE B CE1 
8140  C  CE2 . PHE B 899  ? 0.5524 0.7757 0.7013 0.1164  -0.0173 -0.0685 899  PHE B CE2 
8141  C  CZ  . PHE B 899  ? 0.6288 0.8488 0.7791 0.1133  -0.0142 -0.0668 899  PHE B CZ  
8142  N  N   . ASN B 900  ? 0.5250 0.7299 0.6686 0.1014  -0.0127 -0.0639 900  ASN B N   
8143  C  CA  . ASN B 900  ? 0.5329 0.7504 0.6812 0.0982  -0.0131 -0.0679 900  ASN B CA  
8144  C  C   . ASN B 900  ? 0.5593 0.7898 0.7115 0.1029  -0.0158 -0.0715 900  ASN B C   
8145  O  O   . ASN B 900  ? 0.5673 0.8064 0.7247 0.1013  -0.0142 -0.0730 900  ASN B O   
8146  C  CB  . ASN B 900  ? 0.4150 0.6344 0.5671 0.0905  -0.0089 -0.0678 900  ASN B CB  
8147  C  CG  . ASN B 900  ? 0.5161 0.7240 0.6641 0.0861  -0.0066 -0.0649 900  ASN B CG  
8148  O  OD1 . ASN B 900  ? 0.6233 0.8331 0.7715 0.0821  -0.0062 -0.0665 900  ASN B OD1 
8149  N  ND2 . ASN B 900  ? 0.4964 0.6927 0.6411 0.0867  -0.0049 -0.0608 900  ASN B ND2 
8150  N  N   . PHE B 901  ? 0.4834 0.7149 0.6324 0.1092  -0.0198 -0.0727 901  PHE B N   
8151  C  CA  . PHE B 901  ? 0.4066 0.6503 0.5586 0.1147  -0.0227 -0.0762 901  PHE B CA  
8152  C  C   . PHE B 901  ? 0.4527 0.7132 0.6127 0.1107  -0.0226 -0.0807 901  PHE B C   
8153  O  O   . PHE B 901  ? 0.5077 0.7797 0.6729 0.1127  -0.0229 -0.0832 901  PHE B O   
8154  C  CB  . PHE B 901  ? 0.4726 0.7136 0.6187 0.1223  -0.0271 -0.0766 901  PHE B CB  
8155  C  CG  . PHE B 901  ? 0.4780 0.7032 0.6164 0.1267  -0.0270 -0.0725 901  PHE B CG  
8156  C  CD1 . PHE B 901  ? 0.5314 0.7547 0.6685 0.1321  -0.0277 -0.0718 901  PHE B CD1 
8157  C  CD2 . PHE B 901  ? 0.4871 0.6991 0.6196 0.1253  -0.0262 -0.0693 901  PHE B CD2 
8158  C  CE1 . PHE B 901  ? 0.5577 0.7661 0.6879 0.1356  -0.0274 -0.0682 901  PHE B CE1 
8159  C  CE2 . PHE B 901  ? 0.4561 0.6537 0.5821 0.1288  -0.0257 -0.0656 901  PHE B CE2 
8160  C  CZ  . PHE B 901  ? 0.4846 0.6804 0.6096 0.1338  -0.0264 -0.0651 901  PHE B CZ  
8161  N  N   . LEU B 902  ? 0.4644 0.7264 0.6256 0.1049  -0.0219 -0.0819 902  LEU B N   
8162  C  CA  . LEU B 902  ? 0.4474 0.7243 0.6166 0.0995  -0.0211 -0.0862 902  LEU B CA  
8163  C  C   . LEU B 902  ? 0.3660 0.6373 0.5360 0.0904  -0.0165 -0.0847 902  LEU B C   
8164  O  O   . LEU B 902  ? 0.4106 0.6678 0.5757 0.0890  -0.0141 -0.0803 902  LEU B O   
8165  C  CB  . LEU B 902  ? 0.4624 0.7490 0.6326 0.1017  -0.0255 -0.0904 902  LEU B CB  
8166  C  CG  . LEU B 902  ? 0.4653 0.7585 0.6345 0.1113  -0.0303 -0.0923 902  LEU B CG  
8167  C  CD1 . LEU B 902  ? 0.5580 0.8570 0.7257 0.1142  -0.0350 -0.0957 902  LEU B CD1 
8168  C  CD2 . LEU B 902  ? 0.5906 0.8991 0.7680 0.1124  -0.0298 -0.0953 902  LEU B CD2 
8169  N  N   . GLN B 903  ? 0.3968 0.6789 0.5729 0.0842  -0.0153 -0.0884 903  GLN B N   
8170  C  CA  . GLN B 903  ? 0.4299 0.7062 0.6060 0.0755  -0.0110 -0.0873 903  GLN B CA  
8171  C  C   . GLN B 903  ? 0.5316 0.8005 0.7025 0.0743  -0.0128 -0.0872 903  GLN B C   
8172  O  O   . GLN B 903  ? 0.5256 0.8034 0.6989 0.0731  -0.0155 -0.0914 903  GLN B O   
8173  C  CB  . GLN B 903  ? 0.3350 0.6251 0.5196 0.0689  -0.0083 -0.0912 903  GLN B CB  
8174  C  CG  . GLN B 903  ? 0.3183 0.6019 0.5023 0.0598  -0.0037 -0.0904 903  GLN B CG  
8175  C  CD  . GLN B 903  ? 0.5135 0.7832 0.6928 0.0584  0.0007  -0.0851 903  GLN B CD  
8176  O  OE1 . GLN B 903  ? 0.5477 0.8167 0.7271 0.0623  0.0013  -0.0831 903  GLN B OE1 
8177  N  NE2 . GLN B 903  ? 0.6127 0.8713 0.7877 0.0530  0.0036  -0.0830 903  GLN B NE2 
8178  N  N   . TYR B 904  ? 0.5480 0.8006 0.7115 0.0747  -0.0114 -0.0825 904  TYR B N   
8179  C  CA  . TYR B 904  ? 0.4979 0.7417 0.6552 0.0745  -0.0129 -0.0818 904  TYR B CA  
8180  C  C   . TYR B 904  ? 0.5950 0.8325 0.7511 0.0663  -0.0090 -0.0811 904  TYR B C   
8181  O  O   . TYR B 904  ? 0.6302 0.8659 0.7835 0.0643  -0.0104 -0.0828 904  TYR B O   
8182  C  CB  . TYR B 904  ? 0.4469 0.6765 0.5965 0.0803  -0.0137 -0.0770 904  TYR B CB  
8183  C  CG  . TYR B 904  ? 0.5530 0.7859 0.7014 0.0889  -0.0179 -0.0776 904  TYR B CG  
8184  C  CD1 . TYR B 904  ? 0.6219 0.8673 0.7728 0.0922  -0.0222 -0.0822 904  TYR B CD1 
8185  C  CD2 . TYR B 904  ? 0.5704 0.7939 0.7149 0.0939  -0.0177 -0.0737 904  TYR B CD2 
8186  C  CE1 . TYR B 904  ? 0.6154 0.8633 0.7643 0.1007  -0.0260 -0.0826 904  TYR B CE1 
8187  C  CE2 . TYR B 904  ? 0.5538 0.7791 0.6963 0.1018  -0.0213 -0.0742 904  TYR B CE2 
8188  C  CZ  . TYR B 904  ? 0.6446 0.8817 0.7889 0.1055  -0.0254 -0.0785 904  TYR B CZ  
8189  O  OH  . TYR B 904  ? 0.7085 0.9468 0.8499 0.1139  -0.0288 -0.0789 904  TYR B OH  
8190  N  N   . SER B 905  ? 0.6329 0.8664 0.7904 0.0617  -0.0043 -0.0788 905  SER B N   
8191  C  CA  . SER B 905  ? 0.6498 0.8757 0.8051 0.0544  -0.0002 -0.0778 905  SER B CA  
8192  C  C   . SER B 905  ? 0.7093 0.9464 0.8701 0.0479  0.0004  -0.0829 905  SER B C   
8193  O  O   . SER B 905  ? 0.7073 0.9578 0.8754 0.0470  0.0004  -0.0861 905  SER B O   
8194  C  CB  . SER B 905  ? 0.6834 0.9019 0.8381 0.0522  0.0046  -0.0739 905  SER B CB  
8195  O  OG  . SER B 905  ? 0.7000 0.9086 0.8502 0.0577  0.0040  -0.0695 905  SER B OG  
8196  N  N   . ASP B 906  ? 0.9205 1.1518 1.0778 0.0432  0.0012  -0.0837 906  ASP B N   
8197  C  CA  . ASP B 906  ? 0.9172 1.1579 1.0792 0.0363  0.0018  -0.0888 906  ASP B CA  
8198  C  C   . ASP B 906  ? 0.9774 1.2186 1.1429 0.0292  0.0077  -0.0884 906  ASP B C   
8199  O  O   . ASP B 906  ? 0.9887 1.2178 1.1496 0.0280  0.0118  -0.0839 906  ASP B O   
8200  C  CB  . ASP B 906  ? 0.9791 1.2118 1.1352 0.0336  0.0009  -0.0896 906  ASP B CB  
8201  C  CG  . ASP B 906  ? 1.1423 1.3827 1.3027 0.0253  0.0020  -0.0948 906  ASP B CG  
8202  O  OD1 . ASP B 906  ? 1.1340 1.3883 1.2998 0.0257  -0.0021 -0.1002 906  ASP B OD1 
8203  O  OD2 . ASP B 906  ? 1.2670 1.4996 1.4254 0.0184  0.0071  -0.0938 906  ASP B OD2 
8204  N  N   . THR B 907  ? 0.8337 1.0892 1.0072 0.0245  0.0083  -0.0933 907  THR B N   
8205  C  CA  . THR B 907  ? 0.9141 1.1712 1.0913 0.0178  0.0143  -0.0933 907  THR B CA  
8206  C  C   . THR B 907  ? 1.0382 1.3003 1.2188 0.0087  0.0163  -0.0980 907  THR B C   
8207  O  O   . THR B 907  ? 1.0041 1.2600 1.1834 0.0019  0.0221  -0.0970 907  THR B O   
8208  C  CB  . THR B 907  ? 0.9056 1.1757 1.0902 0.0207  0.0143  -0.0944 907  THR B CB  
8209  O  OG1 . THR B 907  ? 0.9399 1.2273 1.1321 0.0219  0.0099  -0.1000 907  THR B OG1 
8210  C  CG2 . THR B 907  ? 0.8746 1.1386 1.0554 0.0292  0.0126  -0.0898 907  THR B CG2 
8211  N  N   . THR B 908  ? 1.0815 1.3545 1.2660 0.0086  0.0116  -0.1033 908  THR B N   
8212  C  CA  . THR B 908  ? 1.0487 1.3293 1.2381 -0.0002 0.0130  -0.1087 908  THR B CA  
8213  C  C   . THR B 908  ? 1.0759 1.3429 1.2575 -0.0048 0.0138  -0.1085 908  THR B C   
8214  O  O   . THR B 908  ? 1.0392 1.3030 1.2211 -0.0136 0.0185  -0.1099 908  THR B O   
8215  C  CB  . THR B 908  ? 1.1007 1.4009 1.2988 0.0018  0.0071  -0.1151 908  THR B CB  
8216  O  OG1 . THR B 908  ? 1.0940 1.3909 1.2866 0.0076  0.0010  -0.1156 908  THR B OG1 
8217  C  CG2 . THR B 908  ? 1.1916 1.5046 1.3965 0.0076  0.0060  -0.1152 908  THR B CG2 
8218  N  N   . THR B 909  ? 1.0666 1.3251 1.2408 0.0009  0.0096  -0.1066 909  THR B N   
8219  C  CA  . THR B 909  ? 0.9785 1.2243 1.1449 -0.0027 0.0100  -0.1066 909  THR B CA  
8220  C  C   . THR B 909  ? 0.9633 1.1918 1.1226 -0.0064 0.0166  -0.1013 909  THR B C   
8221  O  O   . THR B 909  ? 1.0674 1.2871 1.2226 -0.0013 0.0181  -0.0957 909  THR B O   
8222  C  CB  . THR B 909  ? 0.9805 1.2207 1.1401 0.0052  0.0044  -0.1052 909  THR B CB  
8223  O  OG1 . THR B 909  ? 0.9763 1.2322 1.1418 0.0106  -0.0017 -0.1091 909  THR B OG1 
8224  C  CG2 . THR B 909  ? 1.0469 1.2778 1.1996 0.0014  0.0038  -0.1069 909  THR B CG2 
8225  N  N   . GLU B 910  ? 0.7504 0.9737 0.9080 -0.0151 0.0206  -0.1033 910  GLU B N   
8226  C  CA  . GLU B 910  ? 0.8901 1.0972 1.0408 -0.0187 0.0272  -0.0986 910  GLU B CA  
8227  C  C   . GLU B 910  ? 0.8168 1.0066 0.9564 -0.0144 0.0266  -0.0940 910  GLU B C   
8228  O  O   . GLU B 910  ? 0.9230 1.1007 1.0571 -0.0122 0.0302  -0.0884 910  GLU B O   
8229  C  CB  . GLU B 910  ? 0.9464 1.1524 1.0980 -0.0294 0.0319  -0.1023 910  GLU B CB  
8230  C  CG  . GLU B 910  ? 1.0337 1.2553 1.1962 -0.0346 0.0342  -0.1062 910  GLU B CG  
8231  C  CD  . GLU B 910  ? 0.9512 1.1708 1.1144 -0.0328 0.0389  -0.1015 910  GLU B CD  
8232  O  OE1 . GLU B 910  ? 0.9492 1.1527 1.1040 -0.0325 0.0432  -0.0962 910  GLU B OE1 
8233  O  OE2 . GLU B 910  ? 1.0861 1.3205 1.2582 -0.0314 0.0382  -0.1033 910  GLU B OE2 
8234  N  N   . THR B 911  ? 0.9724 1.1611 1.1086 -0.0128 0.0221  -0.0964 911  THR B N   
8235  C  CA  . THR B 911  ? 0.9538 1.1262 1.0794 -0.0089 0.0219  -0.0922 911  THR B CA  
8236  C  C   . THR B 911  ? 0.9735 1.1428 1.0973 0.0003  0.0201  -0.0869 911  THR B C   
8237  O  O   . THR B 911  ? 0.9474 1.1026 1.0642 0.0027  0.0228  -0.0816 911  THR B O   
8238  C  CB  . THR B 911  ? 0.9917 1.1644 1.1140 -0.0089 0.0172  -0.0963 911  THR B CB  
8239  O  OG1 . THR B 911  ? 1.0329 1.2195 1.1605 -0.0032 0.0108  -0.0991 911  THR B OG1 
8240  C  CG2 . THR B 911  ? 1.0142 1.1898 1.1385 -0.0186 0.0189  -0.1019 911  THR B CG2 
8241  N  N   . PHE B 912  ? 0.6543 0.8365 0.7846 0.0054  0.0157  -0.0884 912  PHE B N   
8242  C  CA  . PHE B 912  ? 0.5202 0.6996 0.6492 0.0136  0.0143  -0.0836 912  PHE B CA  
8243  C  C   . PHE B 912  ? 0.6732 0.8484 0.8032 0.0130  0.0193  -0.0793 912  PHE B C   
8244  O  O   . PHE B 912  ? 0.6083 0.7745 0.7342 0.0180  0.0199  -0.0743 912  PHE B O   
8245  C  CB  . PHE B 912  ? 0.6742 0.8683 0.8096 0.0191  0.0088  -0.0864 912  PHE B CB  
8246  C  CG  . PHE B 912  ? 0.7986 0.9943 0.9307 0.0228  0.0033  -0.0891 912  PHE B CG  
8247  C  CD1 . PHE B 912  ? 0.8449 1.0278 0.9683 0.0224  0.0035  -0.0879 912  PHE B CD1 
8248  C  CD2 . PHE B 912  ? 0.6326 0.8424 0.7700 0.0272  -0.0021 -0.0928 912  PHE B CD2 
8249  C  CE1 . PHE B 912  ? 0.7632 0.9470 0.8826 0.0261  -0.0015 -0.0903 912  PHE B CE1 
8250  C  CE2 . PHE B 912  ? 0.6461 0.8569 0.7796 0.0312  -0.0073 -0.0952 912  PHE B CE2 
8251  C  CZ  . PHE B 912  ? 0.6975 0.8952 0.8219 0.0306  -0.0070 -0.0940 912  PHE B CZ  
8252  N  N   . LYS B 913  ? 0.8205 1.0018 0.9557 0.0070  0.0228  -0.0814 913  LYS B N   
8253  C  CA  . LYS B 913  ? 0.6331 0.8092 0.7679 0.0061  0.0278  -0.0774 913  LYS B CA  
8254  C  C   . LYS B 913  ? 0.6770 0.8356 0.8028 0.0041  0.0322  -0.0733 913  LYS B C   
8255  O  O   . LYS B 913  ? 0.7123 0.8633 0.8352 0.0067  0.0349  -0.0686 913  LYS B O   
8256  C  CB  . LYS B 913  ? 0.6103 0.7965 0.7520 -0.0003 0.0310  -0.0807 913  LYS B CB  
8257  C  CG  . LYS B 913  ? 0.7719 0.9756 0.9230 0.0026  0.0276  -0.0839 913  LYS B CG  
8258  C  CD  . LYS B 913  ? 0.8076 1.0226 0.9661 -0.0047 0.0307  -0.0883 913  LYS B CD  
8259  C  CE  . LYS B 913  ? 0.8223 1.0297 0.9785 -0.0090 0.0377  -0.0852 913  LYS B CE  
8260  N  NZ  . LYS B 913  ? 0.7516 0.9709 0.9156 -0.0155 0.0410  -0.0892 913  LYS B NZ  
8261  N  N   . LEU B 914  ? 0.5624 0.7145 0.6834 -0.0001 0.0327  -0.0751 914  LEU B N   
8262  C  CA  . LEU B 914  ? 0.5306 0.6656 0.6423 -0.0013 0.0367  -0.0713 914  LEU B CA  
8263  C  C   . LEU B 914  ? 0.5346 0.6607 0.6406 0.0059  0.0344  -0.0670 914  LEU B C   
8264  O  O   . LEU B 914  ? 0.5620 0.6748 0.6613 0.0067  0.0378  -0.0628 914  LEU B O   
8265  C  CB  . LEU B 914  ? 0.5149 0.6456 0.6229 -0.0082 0.0379  -0.0750 914  LEU B CB  
8266  C  CG  . LEU B 914  ? 0.5745 0.7078 0.6852 -0.0170 0.0425  -0.0781 914  LEU B CG  
8267  C  CD1 . LEU B 914  ? 0.5784 0.7090 0.6862 -0.0235 0.0425  -0.0827 914  LEU B CD1 
8268  C  CD2 . LEU B 914  ? 0.7257 0.8473 0.8314 -0.0185 0.0490  -0.0734 914  LEU B CD2 
8269  N  N   . ALA B 915  ? 0.5782 0.7113 0.6869 0.0114  0.0291  -0.0680 915  ALA B N   
8270  C  CA  . ALA B 915  ? 0.4724 0.5971 0.5759 0.0181  0.0272  -0.0641 915  ALA B CA  
8271  C  C   . ALA B 915  ? 0.4871 0.6112 0.5926 0.0234  0.0276  -0.0597 915  ALA B C   
8272  O  O   . ALA B 915  ? 0.4343 0.5498 0.5355 0.0281  0.0275  -0.0557 915  ALA B O   
8273  C  CB  . ALA B 915  ? 0.3972 0.5280 0.5012 0.0219  0.0215  -0.0669 915  ALA B CB  
8274  N  N   . PHE B 916  ? 0.7633 0.8964 0.8752 0.0227  0.0282  -0.0604 916  PHE B N   
8275  C  CA  . PHE B 916  ? 0.6958 0.8290 0.8098 0.0277  0.0282  -0.0568 916  PHE B CA  
8276  C  C   . PHE B 916  ? 0.6858 0.8063 0.7944 0.0280  0.0323  -0.0519 916  PHE B C   
8277  O  O   . PHE B 916  ? 0.7651 0.8791 0.8701 0.0233  0.0365  -0.0515 916  PHE B O   
8278  C  CB  . PHE B 916  ? 0.6949 0.8399 0.8161 0.0264  0.0284  -0.0589 916  PHE B CB  
8279  C  CG  . PHE B 916  ? 0.5996 0.7581 0.7269 0.0291  0.0236  -0.0626 916  PHE B CG  
8280  C  CD1 . PHE B 916  ? 0.5151 0.6738 0.6418 0.0359  0.0194  -0.0615 916  PHE B CD1 
8281  C  CD2 . PHE B 916  ? 0.6186 0.7894 0.7520 0.0251  0.0234  -0.0673 916  PHE B CD2 
8282  C  CE1 . PHE B 916  ? 0.5099 0.6804 0.6414 0.0390  0.0150  -0.0648 916  PHE B CE1 
8283  C  CE2 . PHE B 916  ? 0.5935 0.7773 0.7325 0.0281  0.0188  -0.0708 916  PHE B CE2 
8284  C  CZ  . PHE B 916  ? 0.4894 0.6727 0.6271 0.0354  0.0145  -0.0695 916  PHE B CZ  
8285  N  N   . ASN B 917  ? 0.7157 0.8327 0.8239 0.0337  0.0312  -0.0482 917  ASN B N   
8286  C  CA  . ASN B 917  ? 0.7000 0.8065 0.8041 0.0349  0.0346  -0.0436 917  ASN B CA  
8287  C  C   . ASN B 917  ? 0.6993 0.8091 0.8064 0.0341  0.0368  -0.0428 917  ASN B C   
8288  O  O   . ASN B 917  ? 0.7734 0.8909 0.8856 0.0372  0.0345  -0.0432 917  ASN B O   
8289  C  CB  . ASN B 917  ? 0.6859 0.7879 0.7890 0.0409  0.0326  -0.0404 917  ASN B CB  
8290  C  CG  . ASN B 917  ? 0.6749 0.7682 0.7753 0.0426  0.0355  -0.0359 917  ASN B CG  
8291  O  OD1 . ASN B 917  ? 0.8017 0.8880 0.8978 0.0397  0.0393  -0.0347 917  ASN B OD1 
8292  N  ND2 . ASN B 917  ? 0.6707 0.7643 0.7735 0.0475  0.0338  -0.0335 917  ASN B ND2 
8293  N  N   . PRO B 918  ? 0.5206 0.6243 0.6240 0.0303  0.0414  -0.0418 918  PRO B N   
8294  C  CA  . PRO B 918  ? 0.5657 0.6728 0.6714 0.0293  0.0437  -0.0414 918  PRO B CA  
8295  C  C   . PRO B 918  ? 0.6376 0.7433 0.7441 0.0347  0.0429  -0.0379 918  PRO B C   
8296  O  O   . PRO B 918  ? 0.5807 0.6904 0.6893 0.0348  0.0441  -0.0379 918  PRO B O   
8297  C  CB  . PRO B 918  ? 0.5947 0.6927 0.6942 0.0243  0.0491  -0.0406 918  PRO B CB  
8298  C  CG  . PRO B 918  ? 0.5036 0.5911 0.5971 0.0249  0.0494  -0.0389 918  PRO B CG  
8299  C  CD  . PRO B 918  ? 0.4852 0.5781 0.5817 0.0269  0.0447  -0.0409 918  PRO B CD  
8300  N  N   . ASP B 919  ? 0.8403 0.9407 0.9453 0.0391  0.0412  -0.0352 919  ASP B N   
8301  C  CA  . ASP B 919  ? 0.8051 0.9045 0.9114 0.0439  0.0402  -0.0323 919  ASP B CA  
8302  C  C   . ASP B 919  ? 0.8407 0.9489 0.9530 0.0476  0.0358  -0.0336 919  ASP B C   
8303  O  O   . ASP B 919  ? 0.8892 0.9971 1.0030 0.0515  0.0346  -0.0317 919  ASP B O   
8304  C  CB  . ASP B 919  ? 0.7537 0.8434 0.8561 0.0467  0.0408  -0.0287 919  ASP B CB  
8305  C  CG  . ASP B 919  ? 1.0101 1.0908 1.1067 0.0454  0.0452  -0.0262 919  ASP B CG  
8306  O  OD1 . ASP B 919  ? 1.0467 1.1284 1.1429 0.0447  0.0470  -0.0259 919  ASP B OD1 
8307  O  OD2 . ASP B 919  ? 1.2520 1.3242 1.3438 0.0454  0.0468  -0.0244 919  ASP B OD2 
8308  N  N   . VAL B 920  ? 0.7190 0.8346 0.8343 0.0467  0.0333  -0.0369 920  VAL B N   
8309  C  CA  . VAL B 920  ? 0.7433 0.8668 0.8635 0.0506  0.0292  -0.0383 920  VAL B CA  
8310  C  C   . VAL B 920  ? 0.7334 0.8678 0.8577 0.0483  0.0286  -0.0422 920  VAL B C   
8311  O  O   . VAL B 920  ? 0.6748 0.8120 0.7990 0.0442  0.0294  -0.0448 920  VAL B O   
8312  C  CB  . VAL B 920  ? 0.7163 0.8379 0.8356 0.0532  0.0262  -0.0384 920  VAL B CB  
8313  C  CG1 . VAL B 920  ? 0.7444 0.8737 0.8679 0.0572  0.0222  -0.0400 920  VAL B CG1 
8314  C  CG2 . VAL B 920  ? 0.6078 0.7193 0.7237 0.0555  0.0272  -0.0345 920  VAL B CG2 
8315  N  N   . THR B 921  ? 0.6526 0.7934 0.7807 0.0509  0.0272  -0.0427 921  THR B N   
8316  C  CA  . THR B 921  ? 0.6349 0.7870 0.7675 0.0494  0.0266  -0.0464 921  THR B CA  
8317  C  C   . THR B 921  ? 0.5862 0.7451 0.7214 0.0508  0.0228  -0.0494 921  THR B C   
8318  O  O   . THR B 921  ? 0.4861 0.6422 0.6203 0.0550  0.0197  -0.0484 921  THR B O   
8319  C  CB  . THR B 921  ? 0.6656 0.8225 0.8011 0.0527  0.0259  -0.0461 921  THR B CB  
8320  O  OG1 . THR B 921  ? 0.7920 0.9517 0.9296 0.0580  0.0216  -0.0465 921  THR B OG1 
8321  C  CG2 . THR B 921  ? 0.5858 0.7344 0.7180 0.0535  0.0283  -0.0426 921  THR B CG2 
8322  N  N   . VAL B 922  ? 0.6880 0.8558 0.8264 0.0473  0.0230  -0.0532 922  VAL B N   
8323  C  CA  . VAL B 922  ? 0.6259 0.8018 0.7670 0.0487  0.0191  -0.0567 922  VAL B CA  
8324  C  C   . VAL B 922  ? 0.6570 0.8434 0.8032 0.0527  0.0165  -0.0585 922  VAL B C   
8325  O  O   . VAL B 922  ? 0.7489 0.9425 0.8987 0.0507  0.0185  -0.0600 922  VAL B O   
8326  C  CB  . VAL B 922  ? 0.5597 0.7408 0.7022 0.0427  0.0203  -0.0603 922  VAL B CB  
8327  C  CG1 . VAL B 922  ? 0.6330 0.8224 0.7780 0.0448  0.0157  -0.0640 922  VAL B CG1 
8328  C  CG2 . VAL B 922  ? 0.6696 0.8391 0.8064 0.0385  0.0234  -0.0584 922  VAL B CG2 
8329  N  N   . ARG B 923  ? 0.6591 0.8458 0.8049 0.0586  0.0125  -0.0583 923  ARG B N   
8330  C  CA  . ARG B 923  ? 0.7296 0.9237 0.8788 0.0634  0.0100  -0.0593 923  ARG B CA  
8331  C  C   . ARG B 923  ? 0.7686 0.9771 0.9233 0.0628  0.0085  -0.0641 923  ARG B C   
8332  O  O   . ARG B 923  ? 0.8491 1.0620 1.0046 0.0608  0.0071  -0.0668 923  ARG B O   
8333  C  CB  . ARG B 923  ? 0.7293 0.9181 0.8757 0.0697  0.0064  -0.0576 923  ARG B CB  
8334  C  CG  . ARG B 923  ? 0.6693 0.8473 0.8126 0.0716  0.0076  -0.0534 923  ARG B CG  
8335  C  CD  . ARG B 923  ? 0.6694 0.8366 0.8086 0.0687  0.0099  -0.0505 923  ARG B CD  
8336  N  NE  . ARG B 923  ? 0.7457 0.9095 0.8818 0.0700  0.0079  -0.0507 923  ARG B NE  
8337  C  CZ  . ARG B 923  ? 0.6269 0.7825 0.7591 0.0677  0.0095  -0.0490 923  ARG B CZ  
8338  N  NH1 . ARG B 923  ? 0.6876 0.8372 0.8183 0.0639  0.0132  -0.0468 923  ARG B NH1 
8339  N  NH2 . ARG B 923  ? 0.5892 0.7420 0.7182 0.0695  0.0075  -0.0494 923  ARG B NH2 
8340  N  N   . ILE B 924  ? 0.4583 0.6747 0.6169 0.0646  0.0086  -0.0652 924  ILE B N   
8341  C  CA  . ILE B 924  ? 0.4525 0.6838 0.6171 0.0647  0.0073  -0.0697 924  ILE B CA  
8342  C  C   . ILE B 924  ? 0.5571 0.7926 0.7221 0.0724  0.0026  -0.0706 924  ILE B C   
8343  O  O   . ILE B 924  ? 0.5461 0.7721 0.7065 0.0769  0.0008  -0.0677 924  ILE B O   
8344  C  CB  . ILE B 924  ? 0.4894 0.7270 0.6579 0.0616  0.0112  -0.0704 924  ILE B CB  
8345  C  CG1 . ILE B 924  ? 0.5120 0.7650 0.6876 0.0584  0.0115  -0.0753 924  ILE B CG1 
8346  C  CG2 . ILE B 924  ? 0.5116 0.7489 0.6799 0.0671  0.0105  -0.0689 924  ILE B CG2 
8347  C  CD1 . ILE B 924  ? 0.5545 0.8130 0.7337 0.0542  0.0163  -0.0760 924  ILE B CD1 
8348  N  N   . ARG B 925  ? 0.7971 1.0467 0.9675 0.0741  0.0007  -0.0746 925  ARG B N   
8349  C  CA  . ARG B 925  ? 0.7114 0.9653 0.8818 0.0819  -0.0037 -0.0758 925  ARG B CA  
8350  C  C   . ARG B 925  ? 0.7245 0.9740 0.8932 0.0861  -0.0032 -0.0734 925  ARG B C   
8351  O  O   . ARG B 925  ? 0.7625 1.0148 0.9337 0.0838  0.0000  -0.0732 925  ARG B O   
8352  C  CB  . ARG B 925  ? 0.7124 0.9836 0.8895 0.0826  -0.0056 -0.0809 925  ARG B CB  
8353  C  CG  . ARG B 925  ? 0.7713 1.0489 0.9493 0.0906  -0.0088 -0.0821 925  ARG B CG  
8354  C  CD  . ARG B 925  ? 0.8308 1.1251 1.0148 0.0925  -0.0118 -0.0872 925  ARG B CD  
8355  N  NE  . ARG B 925  ? 0.9920 1.2993 1.1840 0.0866  -0.0085 -0.0903 925  ARG B NE  
8356  C  CZ  . ARG B 925  ? 1.0344 1.3510 1.2311 0.0880  -0.0069 -0.0917 925  ARG B CZ  
8357  N  NH1 . ARG B 925  ? 0.8271 1.1415 1.0212 0.0953  -0.0085 -0.0903 925  ARG B NH1 
8358  N  NH2 . ARG B 925  ? 1.1036 1.4317 1.3076 0.0819  -0.0035 -0.0944 925  ARG B NH2 
8359  N  N   . GLY B 926  ? 0.7479 0.9902 0.9121 0.0924  -0.0063 -0.0716 926  GLY B N   
8360  C  CA  . GLY B 926  ? 0.8384 1.0772 1.0010 0.0971  -0.0066 -0.0700 926  GLY B CA  
8361  C  C   . GLY B 926  ? 0.8424 1.0668 1.0004 0.0965  -0.0050 -0.0657 926  GLY B C   
8362  O  O   . GLY B 926  ? 0.9056 1.1272 1.0627 0.0994  -0.0049 -0.0647 926  GLY B O   
8363  N  N   . VAL B 927  ? 0.5790 0.7942 0.7341 0.0931  -0.0039 -0.0634 927  VAL B N   
8364  C  CA  . VAL B 927  ? 0.5286 0.7310 0.6800 0.0923  -0.0024 -0.0595 927  VAL B CA  
8365  C  C   . VAL B 927  ? 0.5372 0.7299 0.6840 0.0947  -0.0043 -0.0575 927  VAL B C   
8366  O  O   . VAL B 927  ? 0.5093 0.7044 0.6550 0.0963  -0.0065 -0.0590 927  VAL B O   
8367  C  CB  . VAL B 927  ? 0.3467 0.5462 0.4985 0.0858  0.0017  -0.0580 927  VAL B CB  
8368  C  CG1 . VAL B 927  ? 0.4658 0.6741 0.6215 0.0835  0.0041  -0.0597 927  VAL B CG1 
8369  C  CG2 . VAL B 927  ? 0.4578 0.6569 0.6091 0.0816  0.0024  -0.0585 927  VAL B CG2 
8370  N  N   . MET B 928  ? 0.5893 0.7710 0.7332 0.0950  -0.0034 -0.0541 928  MET B N   
8371  C  CA  . MET B 928  ? 0.4823 0.6537 0.6219 0.0972  -0.0045 -0.0518 928  MET B CA  
8372  C  C   . MET B 928  ? 0.5548 0.7186 0.6929 0.0925  -0.0018 -0.0491 928  MET B C   
8373  O  O   . MET B 928  ? 0.6220 0.7857 0.7616 0.0885  0.0009  -0.0483 928  MET B O   
8374  C  CB  . MET B 928  ? 0.4773 0.6419 0.6152 0.1012  -0.0056 -0.0502 928  MET B CB  
8375  C  CG  . MET B 928  ? 0.5561 0.7121 0.6895 0.1050  -0.0073 -0.0487 928  MET B CG  
8376  S  SD  . MET B 928  ? 0.5600 0.7222 0.6915 0.1109  -0.0109 -0.0517 928  MET B SD  
8377  C  CE  . MET B 928  ? 0.5823 0.7410 0.7121 0.1167  -0.0127 -0.0516 928  MET B CE  
8378  N  N   . GLU B 929  ? 0.6460 0.8029 0.7804 0.0936  -0.0024 -0.0478 929  GLU B N   
8379  C  CA  . GLU B 929  ? 0.6130 0.7619 0.7453 0.0900  0.0001  -0.0451 929  GLU B CA  
8380  C  C   . GLU B 929  ? 0.5621 0.7004 0.6907 0.0929  -0.0003 -0.0423 929  GLU B C   
8381  O  O   . GLU B 929  ? 0.6013 0.7382 0.7279 0.0974  -0.0026 -0.0427 929  GLU B O   
8382  C  CB  . GLU B 929  ? 0.5792 0.7309 0.7103 0.0872  0.0003  -0.0467 929  GLU B CB  
8383  C  CG  . GLU B 929  ? 0.5670 0.7306 0.7019 0.0849  0.0000  -0.0504 929  GLU B CG  
8384  C  CD  . GLU B 929  ? 0.5080 0.6744 0.6418 0.0823  -0.0003 -0.0524 929  GLU B CD  
8385  O  OE1 . GLU B 929  ? 0.4227 0.5808 0.5521 0.0822  0.0000  -0.0506 929  GLU B OE1 
8386  O  OE2 . GLU B 929  ? 0.5783 0.7553 0.7157 0.0805  -0.0010 -0.0559 929  GLU B OE2 
8387  N  N   . LYS B 930  ? 0.6194 0.7500 0.7471 0.0902  0.0023  -0.0393 930  LYS B N   
8388  C  CA  . LYS B 930  ? 0.6598 0.7803 0.7846 0.0920  0.0028  -0.0364 930  LYS B CA  
8389  C  C   . LYS B 930  ? 0.6178 0.7324 0.7422 0.0883  0.0061  -0.0338 930  LYS B C   
8390  O  O   . LYS B 930  ? 0.5668 0.6845 0.6928 0.0847  0.0078  -0.0341 930  LYS B O   
8391  C  CB  . LYS B 930  ? 0.6743 0.7920 0.8003 0.0950  0.0018  -0.0357 930  LYS B CB  
8392  C  CG  . LYS B 930  ? 0.6280 0.7472 0.7579 0.0931  0.0028  -0.0352 930  LYS B CG  
8393  C  CD  . LYS B 930  ? 0.6002 0.7114 0.7305 0.0915  0.0050  -0.0321 930  LYS B CD  
8394  C  CE  . LYS B 930  ? 0.6709 0.7836 0.8047 0.0902  0.0054  -0.0318 930  LYS B CE  
8395  N  NZ  . LYS B 930  ? 0.6952 0.8014 0.8300 0.0888  0.0074  -0.0290 930  LYS B NZ  
8396  N  N   . CYS B 931  ? 0.3877 0.4935 0.5097 0.0894  0.0072  -0.0311 931  CYS B N   
8397  C  CA  . CYS B 931  ? 0.3282 0.4282 0.4495 0.0866  0.0103  -0.0284 931  CYS B CA  
8398  C  C   . CYS B 931  ? 0.3200 0.4203 0.4452 0.0847  0.0117  -0.0273 931  CYS B C   
8399  O  O   . CYS B 931  ? 0.3626 0.4624 0.4905 0.0864  0.0107  -0.0269 931  CYS B O   
8400  C  CB  . CYS B 931  ? 0.4498 0.5408 0.5680 0.0885  0.0113  -0.0259 931  CYS B CB  
8401  S  SG  . CYS B 931  ? 0.3781 0.4619 0.4969 0.0860  0.0152  -0.0222 931  CYS B SG  
8402  N  N   . THR B 932  ? 0.4055 0.5062 0.5308 0.0815  0.0139  -0.0267 932  THR B N   
8403  C  CA  . THR B 932  ? 0.3834 0.4849 0.5115 0.0800  0.0152  -0.0258 932  THR B CA  
8404  C  C   . THR B 932  ? 0.3533 0.4483 0.4808 0.0789  0.0179  -0.0227 932  THR B C   
8405  O  O   . THR B 932  ? 0.3182 0.4135 0.4467 0.0775  0.0194  -0.0219 932  THR B O   
8406  C  CB  . THR B 932  ? 0.3541 0.4616 0.4824 0.0775  0.0157  -0.0277 932  THR B CB  
8407  O  OG1 . THR B 932  ? 0.3085 0.4143 0.4335 0.0748  0.0176  -0.0277 932  THR B OG1 
8408  C  CG2 . THR B 932  ? 0.3811 0.4963 0.5110 0.0788  0.0131  -0.0308 932  THR B CG2 
8409  N  N   . TYR B 933  ? 0.6407 0.7297 0.7663 0.0798  0.0188  -0.0210 933  TYR B N   
8410  C  CA  . TYR B 933  ? 0.7575 0.8405 0.8822 0.0790  0.0218  -0.0181 933  TYR B CA  
8411  C  C   . TYR B 933  ? 0.6993 0.7820 0.8213 0.0763  0.0240  -0.0179 933  TYR B C   
8412  O  O   . TYR B 933  ? 0.6522 0.7315 0.7742 0.0757  0.0264  -0.0158 933  TYR B O   
8413  C  CB  . TYR B 933  ? 0.6501 0.7324 0.7795 0.0798  0.0221  -0.0165 933  TYR B CB  
8414  C  CG  . TYR B 933  ? 0.6991 0.7781 0.8304 0.0817  0.0215  -0.0156 933  TYR B CG  
8415  C  CD1 . TYR B 933  ? 0.7403 0.8157 0.8683 0.0830  0.0214  -0.0155 933  TYR B CD1 
8416  C  CD2 . TYR B 933  ? 0.7243 0.8034 0.8605 0.0822  0.0213  -0.0148 933  TYR B CD2 
8417  C  CE1 . TYR B 933  ? 0.8200 0.8911 0.9490 0.0846  0.0215  -0.0144 933  TYR B CE1 
8418  C  CE2 . TYR B 933  ? 0.7481 0.8237 0.8863 0.0833  0.0212  -0.0140 933  TYR B CE2 
8419  C  CZ  . TYR B 933  ? 0.7807 0.8519 0.9151 0.0845  0.0215  -0.0137 933  TYR B CZ  
8420  O  OH  . TYR B 933  ? 0.7671 0.8337 0.9027 0.0856  0.0220  -0.0127 933  TYR B OH  
8421  N  N   . CYS B 934  ? 0.6602 0.7462 0.7799 0.0748  0.0234  -0.0202 934  CYS B N   
8422  C  CA  . CYS B 934  ? 0.6794 0.7650 0.7962 0.0717  0.0256  -0.0206 934  CYS B CA  
8423  C  C   . CYS B 934  ? 0.6849 0.7713 0.8035 0.0710  0.0269  -0.0196 934  CYS B C   
8424  O  O   . CYS B 934  ? 0.6676 0.7491 0.7844 0.0705  0.0295  -0.0174 934  CYS B O   
8425  C  CB  . CYS B 934  ? 0.6930 0.7712 0.8050 0.0710  0.0281  -0.0188 934  CYS B CB  
8426  S  SG  . CYS B 934  ? 0.5110 0.5881 0.6191 0.0716  0.0265  -0.0205 934  CYS B SG  
8427  N  N   . VAL B 935  ? 0.4381 0.5306 0.5599 0.0714  0.0250  -0.0213 935  VAL B N   
8428  C  CA  . VAL B 935  ? 0.3633 0.4569 0.4868 0.0716  0.0257  -0.0204 935  VAL B CA  
8429  C  C   . VAL B 935  ? 0.2639 0.3550 0.3835 0.0690  0.0288  -0.0198 935  VAL B C   
8430  O  O   . VAL B 935  ? 0.2672 0.3561 0.3864 0.0697  0.0302  -0.0181 935  VAL B O   
8431  C  CB  . VAL B 935  ? 0.2560 0.3566 0.3827 0.0726  0.0231  -0.0227 935  VAL B CB  
8432  C  CG1 . VAL B 935  ? 0.2568 0.3624 0.3823 0.0702  0.0235  -0.0252 935  VAL B CG1 
8433  C  CG2 . VAL B 935  ? 0.2547 0.3556 0.3831 0.0739  0.0231  -0.0217 935  VAL B CG2 
8434  N  N   . GLN B 936  ? 0.3661 0.4570 0.4825 0.0661  0.0301  -0.0213 936  GLN B N   
8435  C  CA  . GLN B 936  ? 0.4458 0.5331 0.5578 0.0633  0.0335  -0.0207 936  GLN B CA  
8436  C  C   . GLN B 936  ? 0.5888 0.6679 0.6976 0.0642  0.0359  -0.0176 936  GLN B C   
8437  O  O   . GLN B 936  ? 0.5768 0.6522 0.6826 0.0638  0.0385  -0.0161 936  GLN B O   
8438  C  CB  . GLN B 936  ? 0.5508 0.6393 0.6605 0.0597  0.0342  -0.0232 936  GLN B CB  
8439  C  CG  . GLN B 936  ? 0.5549 0.6410 0.6632 0.0600  0.0331  -0.0235 936  GLN B CG  
8440  C  CD  . GLN B 936  ? 0.5015 0.5941 0.6135 0.0618  0.0294  -0.0256 936  GLN B CD  
8441  O  OE1 . GLN B 936  ? 0.5119 0.6109 0.6278 0.0629  0.0275  -0.0269 936  GLN B OE1 
8442  N  NE2 . GLN B 936  ? 0.4336 0.5239 0.5436 0.0626  0.0283  -0.0259 936  GLN B NE2 
8443  N  N   . ARG B 937  ? 0.5394 0.6153 0.6484 0.0658  0.0354  -0.0164 937  ARG B N   
8444  C  CA  . ARG B 937  ? 0.4800 0.5488 0.5866 0.0671  0.0378  -0.0134 937  ARG B CA  
8445  C  C   . ARG B 937  ? 0.5181 0.5878 0.6287 0.0701  0.0372  -0.0115 937  ARG B C   
8446  O  O   . ARG B 937  ? 0.6045 0.6698 0.7131 0.0712  0.0394  -0.0092 937  ARG B O   
8447  C  CB  . ARG B 937  ? 0.4815 0.5467 0.5869 0.0678  0.0377  -0.0128 937  ARG B CB  
8448  C  CG  . ARG B 937  ? 0.4861 0.5517 0.5883 0.0653  0.0372  -0.0153 937  ARG B CG  
8449  C  CD  . ARG B 937  ? 0.4536 0.5135 0.5524 0.0662  0.0379  -0.0143 937  ARG B CD  
8450  N  NE  . ARG B 937  ? 0.4169 0.4761 0.5114 0.0636  0.0377  -0.0167 937  ARG B NE  
8451  C  CZ  . ARG B 937  ? 0.4425 0.4963 0.5325 0.0639  0.0384  -0.0164 937  ARG B CZ  
8452  N  NH1 . ARG B 937  ? 0.4056 0.4537 0.4944 0.0666  0.0398  -0.0135 937  ARG B NH1 
8453  N  NH2 . ARG B 937  ? 0.4688 0.5231 0.5552 0.0614  0.0376  -0.0192 937  ARG B NH2 
8454  N  N   . ILE B 938  ? 0.6579 0.7332 0.7738 0.0717  0.0341  -0.0125 938  ILE B N   
8455  C  CA  . ILE B 938  ? 0.6397 0.7166 0.7598 0.0742  0.0331  -0.0113 938  ILE B CA  
8456  C  C   . ILE B 938  ? 0.6614 0.7394 0.7797 0.0742  0.0338  -0.0113 938  ILE B C   
8457  O  O   . ILE B 938  ? 0.6758 0.7522 0.7943 0.0762  0.0346  -0.0095 938  ILE B O   
8458  C  CB  . ILE B 938  ? 0.6718 0.7537 0.7975 0.0756  0.0297  -0.0127 938  ILE B CB  
8459  C  CG1 . ILE B 938  ? 0.7300 0.8094 0.8565 0.0760  0.0295  -0.0122 938  ILE B CG1 
8460  C  CG2 . ILE B 938  ? 0.7327 0.8169 0.8628 0.0778  0.0282  -0.0121 938  ILE B CG2 
8461  C  CD1 . ILE B 938  ? 0.6319 0.7146 0.7628 0.0774  0.0265  -0.0134 938  ILE B CD1 
8462  N  N   . SER B 939  ? 0.7487 0.8296 0.8652 0.0722  0.0337  -0.0133 939  SER B N   
8463  C  CA  . SER B 939  ? 0.7966 0.8778 0.9105 0.0722  0.0349  -0.0133 939  SER B CA  
8464  C  C   . SER B 939  ? 0.7294 0.8034 0.8370 0.0714  0.0387  -0.0112 939  SER B C   
8465  O  O   . SER B 939  ? 0.7708 0.8428 0.8762 0.0733  0.0398  -0.0098 939  SER B O   
8466  C  CB  . SER B 939  ? 0.8199 0.9059 0.9334 0.0699  0.0345  -0.0159 939  SER B CB  
8467  O  OG  . SER B 939  ? 0.9743 1.0665 1.0930 0.0711  0.0309  -0.0178 939  SER B OG  
8468  N  N   . GLY B 940  ? 0.6910 0.7606 0.7952 0.0690  0.0408  -0.0111 940  GLY B N   
8469  C  CA  . GLY B 940  ? 0.8118 0.8736 0.9094 0.0684  0.0446  -0.0093 940  GLY B CA  
8470  C  C   . GLY B 940  ? 0.7663 0.8243 0.8640 0.0720  0.0452  -0.0064 940  GLY B C   
8471  O  O   . GLY B 940  ? 0.7947 0.8480 0.8878 0.0734  0.0475  -0.0046 940  GLY B O   
8472  N  N   . ALA B 941  ? 0.6743 0.7344 0.7772 0.0738  0.0433  -0.0059 941  ALA B N   
8473  C  CA  . ALA B 941  ? 0.7096 0.7674 0.8139 0.0771  0.0439  -0.0034 941  ALA B CA  
8474  C  C   . ALA B 941  ? 0.7565 0.8185 0.8643 0.0801  0.0421  -0.0030 941  ALA B C   
8475  O  O   . ALA B 941  ? 0.8002 0.8597 0.9066 0.0829  0.0433  -0.0010 941  ALA B O   
8476  C  CB  . ALA B 941  ? 0.6126 0.6714 0.7217 0.0777  0.0428  -0.0030 941  ALA B CB  
8477  N  N   . ARG B 942  ? 0.6247 0.6930 0.7367 0.0798  0.0390  -0.0051 942  ARG B N   
8478  C  CA  . ARG B 942  ? 0.6680 0.7403 0.7827 0.0827  0.0369  -0.0051 942  ARG B CA  
8479  C  C   . ARG B 942  ? 0.6517 0.7205 0.7595 0.0834  0.0390  -0.0044 942  ARG B C   
8480  O  O   . ARG B 942  ? 0.6556 0.7240 0.7628 0.0868  0.0389  -0.0030 942  ARG B O   
8481  C  CB  . ARG B 942  ? 0.6272 0.7062 0.7470 0.0822  0.0333  -0.0076 942  ARG B CB  
8482  C  CG  . ARG B 942  ? 0.5912 0.6742 0.7132 0.0850  0.0308  -0.0082 942  ARG B CG  
8483  C  CD  . ARG B 942  ? 0.5806 0.6696 0.7083 0.0849  0.0271  -0.0106 942  ARG B CD  
8484  N  NE  . ARG B 942  ? 0.6349 0.7256 0.7600 0.0828  0.0271  -0.0125 942  ARG B NE  
8485  C  CZ  . ARG B 942  ? 0.7211 0.8140 0.8486 0.0810  0.0260  -0.0141 942  ARG B CZ  
8486  N  NH1 . ARG B 942  ? 0.6385 0.7314 0.7703 0.0811  0.0248  -0.0140 942  ARG B NH1 
8487  N  NH2 . ARG B 942  ? 0.7574 0.8526 0.8828 0.0793  0.0261  -0.0159 942  ARG B NH2 
8488  N  N   . ILE B 943  ? 0.3864 0.4527 0.4888 0.0803  0.0411  -0.0052 943  ILE B N   
8489  C  CA  . ILE B 943  ? 0.3443 0.4060 0.4392 0.0806  0.0439  -0.0044 943  ILE B CA  
8490  C  C   . ILE B 943  ? 0.4167 0.4706 0.5060 0.0823  0.0470  -0.0016 943  ILE B C   
8491  O  O   . ILE B 943  ? 0.4468 0.4976 0.5318 0.0855  0.0481  -0.0001 943  ILE B O   
8492  C  CB  . ILE B 943  ? 0.4024 0.4632 0.4935 0.0761  0.0459  -0.0061 943  ILE B CB  
8493  C  CG1 . ILE B 943  ? 0.4527 0.5214 0.5482 0.0755  0.0430  -0.0086 943  ILE B CG1 
8494  C  CG2 . ILE B 943  ? 0.4224 0.4756 0.5043 0.0756  0.0501  -0.0048 943  ILE B CG2 
8495  C  CD1 . ILE B 943  ? 0.4972 0.5670 0.5907 0.0711  0.0447  -0.0107 943  ILE B CD1 
8496  N  N   . ALA B 944  ? 0.7556 0.8059 0.8446 0.0808  0.0486  -0.0010 944  ALA B N   
8497  C  CA  . ALA B 944  ? 0.7708 0.8133 0.8542 0.0827  0.0517  0.0016  944  ALA B CA  
8498  C  C   . ALA B 944  ? 0.7906 0.8357 0.8782 0.0878  0.0501  0.0033  944  ALA B C   
8499  O  O   . ALA B 944  ? 0.7819 0.8221 0.8645 0.0911  0.0521  0.0054  944  ALA B O   
8500  C  CB  . ALA B 944  ? 0.7179 0.7564 0.8003 0.0801  0.0534  0.0017  944  ALA B CB  
8501  N  N   . ALA B 945  ? 0.7711 0.8240 0.8679 0.0886  0.0465  0.0023  945  ALA B N   
8502  C  CA  . ALA B 945  ? 0.8023 0.8590 0.9044 0.0929  0.0447  0.0034  945  ALA B CA  
8503  C  C   . ALA B 945  ? 0.7975 0.8565 0.8981 0.0962  0.0431  0.0032  945  ALA B C   
8504  O  O   . ALA B 945  ? 0.8290 0.8874 0.9287 0.1005  0.0433  0.0048  945  ALA B O   
8505  C  CB  . ALA B 945  ? 0.8704 0.9343 0.9826 0.0923  0.0415  0.0021  945  ALA B CB  
8506  N  N   . LYS B 946  ? 0.7013 0.7630 0.8013 0.0946  0.0415  0.0013  946  LYS B N   
8507  C  CA  . LYS B 946  ? 0.6637 0.7269 0.7610 0.0978  0.0401  0.0011  946  LYS B CA  
8508  C  C   . LYS B 946  ? 0.5742 0.6287 0.6607 0.0995  0.0440  0.0033  946  LYS B C   
8509  O  O   . LYS B 946  ? 0.5725 0.6264 0.6562 0.1043  0.0435  0.0044  946  LYS B O   
8510  C  CB  . LYS B 946  ? 0.4451 0.5124 0.5435 0.0956  0.0381  -0.0013 946  LYS B CB  
8511  C  CG  . LYS B 946  ? 0.5196 0.5952 0.6279 0.0951  0.0338  -0.0035 946  LYS B CG  
8512  C  CD  . LYS B 946  ? 0.5111 0.5904 0.6196 0.0936  0.0319  -0.0059 946  LYS B CD  
8513  C  CE  . LYS B 946  ? 0.4646 0.5512 0.5820 0.0938  0.0275  -0.0080 946  LYS B CE  
8514  N  NZ  . LYS B 946  ? 0.5247 0.6149 0.6418 0.0931  0.0257  -0.0103 946  LYS B NZ  
8515  N  N   . ARG B 947  ? 0.6344 0.6819 0.7145 0.0958  0.0479  0.0037  947  ARG B N   
8516  C  CA  . ARG B 947  ? 0.7236 0.7614 0.7925 0.0969  0.0522  0.0057  947  ARG B CA  
8517  C  C   . ARG B 947  ? 0.7304 0.7637 0.7969 0.1012  0.0536  0.0083  947  ARG B C   
8518  O  O   . ARG B 947  ? 0.7329 0.7609 0.7920 0.1053  0.0553  0.0101  947  ARG B O   
8519  C  CB  . ARG B 947  ? 0.6438 0.6754 0.7072 0.0913  0.0559  0.0051  947  ARG B CB  
8520  C  CG  . ARG B 947  ? 0.5506 0.5707 0.6019 0.0915  0.0609  0.0071  947  ARG B CG  
8521  C  CD  . ARG B 947  ? 0.6420 0.6556 0.6892 0.0860  0.0645  0.0066  947  ARG B CD  
8522  N  NE  . ARG B 947  ? 0.5525 0.5726 0.6057 0.0808  0.0629  0.0037  947  ARG B NE  
8523  C  CZ  . ARG B 947  ? 0.6160 0.6348 0.6699 0.0762  0.0639  0.0025  947  ARG B CZ  
8524  N  NH1 . ARG B 947  ? 0.6914 0.7021 0.7403 0.0760  0.0667  0.0039  947  ARG B NH1 
8525  N  NH2 . ARG B 947  ? 0.6328 0.6586 0.6924 0.0722  0.0620  -0.0003 947  ARG B NH2 
8526  N  N   . ALA B 948  ? 0.8741 0.9094 0.9466 0.1006  0.0532  0.0085  948  ALA B N   
8527  C  CA  . ALA B 948  ? 0.8110 0.8433 0.8823 0.1049  0.0546  0.0109  948  ALA B CA  
8528  C  C   . ALA B 948  ? 0.8356 0.8750 0.9123 0.1106  0.0511  0.0111  948  ALA B C   
8529  O  O   . ALA B 948  ? 0.9272 0.9639 1.0007 0.1155  0.0523  0.0132  948  ALA B O   
8530  C  CB  . ALA B 948  ? 0.8522 0.8850 0.9286 0.1028  0.0552  0.0111  948  ALA B CB  
8531  N  N   . ALA B 949  ? 0.6345 0.6832 0.7194 0.1101  0.0468  0.0089  949  ALA B N   
8532  C  CA  . ALA B 949  ? 0.7292 0.7854 0.8199 0.1150  0.0430  0.0086  949  ALA B CA  
8533  C  C   . ALA B 949  ? 0.8224 0.8758 0.9049 0.1191  0.0427  0.0091  949  ALA B C   
8534  O  O   . ALA B 949  ? 0.8843 0.9398 0.9668 0.1249  0.0413  0.0100  949  ALA B O   
8535  C  CB  . ALA B 949  ? 0.8294 0.8956 0.9312 0.1128  0.0384  0.0058  949  ALA B CB  
8536  N  N   . VAL B 950  ? 0.8027 0.8516 0.8782 0.1165  0.0442  0.0085  950  VAL B N   
8537  C  CA  . VAL B 950  ? 0.8127 0.8580 0.8794 0.1205  0.0444  0.0091  950  VAL B CA  
8538  C  C   . VAL B 950  ? 0.7865 0.8203 0.8412 0.1231  0.0493  0.0121  950  VAL B C   
8539  O  O   . VAL B 950  ? 0.8315 0.8625 0.8795 0.1289  0.0492  0.0134  950  VAL B O   
8540  C  CB  . VAL B 950  ? 0.7692 0.8145 0.8332 0.1167  0.0445  0.0074  950  VAL B CB  
8541  C  CG1 . VAL B 950  ? 0.7236 0.7623 0.7833 0.1106  0.0489  0.0075  950  VAL B CG1 
8542  C  CG2 . VAL B 950  ? 0.7584 0.8000 0.8131 0.1211  0.0448  0.0081  950  VAL B CG2 
8543  N  N   . GLN B 951  ? 0.8253 0.8520 0.8765 0.1193  0.0535  0.0132  951  GLN B N   
8544  C  CA  . GLN B 951  ? 0.8424 0.8569 0.8815 0.1215  0.0583  0.0159  951  GLN B CA  
8545  C  C   . GLN B 951  ? 0.8431 0.8585 0.8832 0.1282  0.0576  0.0178  951  GLN B C   
8546  O  O   . GLN B 951  ? 0.8366 0.8432 0.8661 0.1328  0.0605  0.0201  951  GLN B O   
8547  C  CB  . GLN B 951  ? 0.8009 0.8080 0.8367 0.1155  0.0626  0.0161  951  GLN B CB  
8548  C  CG  . GLN B 951  ? 0.8615 0.8638 0.8916 0.1098  0.0651  0.0149  951  GLN B CG  
8549  C  CD  . GLN B 951  ? 0.8552 0.8504 0.8820 0.1039  0.0690  0.0148  951  GLN B CD  
8550  O  OE1 . GLN B 951  ? 1.0204 1.0161 1.0512 0.1034  0.0690  0.0151  951  GLN B OE1 
8551  N  NE2 . GLN B 951  ? 0.8542 0.8430 0.8738 0.0993  0.0724  0.0141  951  GLN B NE2 
8552  N  N   . ALA B 952  ? 0.8508 0.8764 0.9032 0.1290  0.0541  0.0168  952  ALA B N   
8553  C  CA  . ALA B 952  ? 0.9100 0.9391 0.9655 0.1354  0.0529  0.0182  952  ALA B CA  
8554  C  C   . ALA B 952  ? 1.0312 1.0693 1.0910 0.1408  0.0480  0.0171  952  ALA B C   
8555  O  O   . ALA B 952  ? 1.0372 1.0782 1.0983 0.1471  0.0469  0.0181  952  ALA B O   
8556  C  CB  . ALA B 952  ? 0.8378 0.8731 0.9044 0.1332  0.0523  0.0178  952  ALA B CB  
8557  N  N   . GLY B 953  ? 1.2655 1.3081 1.3274 0.1388  0.0450  0.0149  953  GLY B N   
8558  C  CA  . GLY B 953  ? 1.2787 1.3296 1.3443 0.1437  0.0400  0.0135  953  GLY B CA  
8559  C  C   . GLY B 953  ? 1.3462 1.4104 1.4271 0.1438  0.0351  0.0113  953  GLY B C   
8560  O  O   . GLY B 953  ? 1.4432 1.5144 1.5278 0.1494  0.0314  0.0106  953  GLY B O   
8561  N  N   . GLN B 954  ? 0.9177 0.9855 1.0074 0.1378  0.0351  0.0101  954  GLN B N   
8562  C  CA  . GLN B 954  ? 0.9322 1.0115 1.0364 0.1371  0.0313  0.0082  954  GLN B CA  
8563  C  C   . GLN B 954  ? 1.0199 1.1064 1.1312 0.1337  0.0270  0.0050  954  GLN B C   
8564  O  O   . GLN B 954  ? 1.0964 1.1927 1.2180 0.1349  0.0227  0.0029  954  GLN B O   
8565  C  CB  . GLN B 954  ? 0.9811 1.0594 1.0906 0.1332  0.0342  0.0092  954  GLN B CB  
8566  C  CG  . GLN B 954  ? 1.0302 1.1071 1.1393 0.1374  0.0367  0.0116  954  GLN B CG  
8567  C  CD  . GLN B 954  ? 0.9962 1.0649 1.1015 0.1340  0.0418  0.0135  954  GLN B CD  
8568  O  OE1 . GLN B 954  ? 0.8983 0.9653 1.0052 0.1281  0.0426  0.0127  954  GLN B OE1 
8569  N  NE2 . GLN B 954  ? 1.0929 1.1564 1.1930 0.1380  0.0451  0.0161  954  GLN B NE2 
8570  N  N   . SER B 955  ? 1.1304 1.2122 1.2363 0.1297  0.0281  0.0044  955  SER B N   
8571  C  CA  . SER B 955  ? 1.1341 1.2217 1.2462 0.1261  0.0246  0.0014  955  SER B CA  
8572  C  C   . SER B 955  ? 1.2319 1.3260 1.3563 0.1224  0.0231  0.0001  955  SER B C   
8573  O  O   . SER B 955  ? 1.2319 1.3331 1.3642 0.1213  0.0191  -0.0026 955  SER B O   
8574  C  CB  . SER B 955  ? 1.1509 1.2442 1.2635 0.1303  0.0199  -0.0006 955  SER B CB  
8575  O  OG  . SER B 955  ? 1.0900 1.1920 1.2120 0.1334  0.0162  -0.0016 955  SER B OG  
8576  N  N   . SER B 956  ? 1.6682 1.7591 1.7938 0.1207  0.0266  0.0019  956  SER B N   
8577  C  CA  . SER B 956  ? 1.6680 1.7640 1.8044 0.1176  0.0259  0.0011  956  SER B CA  
8578  C  C   . SER B 956  ? 1.6469 1.7411 1.7842 0.1119  0.0263  0.0000  956  SER B C   
8579  O  O   . SER B 956  ? 1.6934 1.7932 1.8385 0.1098  0.0233  -0.0023 956  SER B O   
8580  C  CB  . SER B 956  ? 1.7117 1.8050 1.8487 0.1187  0.0295  0.0037  956  SER B CB  
8581  O  OG  . SER B 956  ? 1.7610 1.8444 1.8883 0.1170  0.0341  0.0057  956  SER B OG  
8582  N  N   . TYR B 957  ? 1.0628 1.1490 1.1918 0.1096  0.0301  0.0013  957  TYR B N   
8583  C  CA  . TYR B 957  ? 0.9941 1.0787 1.1234 0.1046  0.0308  0.0003  957  TYR B CA  
8584  C  C   . TYR B 957  ? 1.0133 1.1008 1.1512 0.1025  0.0306  0.0002  957  TYR B C   
8585  O  O   . TYR B 957  ? 1.0956 1.1889 1.2413 0.1014  0.0275  -0.0018 957  TYR B O   
8586  C  CB  . TYR B 957  ? 0.9072 0.9952 1.0369 0.1033  0.0276  -0.0023 957  TYR B CB  
8587  C  CG  . TYR B 957  ? 0.9014 0.9904 1.0342 0.0989  0.0270  -0.0039 957  TYR B CG  
8588  C  CD1 . TYR B 957  ? 0.8552 0.9392 0.9847 0.0958  0.0301  -0.0031 957  TYR B CD1 
8589  C  CD2 . TYR B 957  ? 0.9185 1.0133 1.0571 0.0983  0.0231  -0.0065 957  TYR B CD2 
8590  C  CE1 . TYR B 957  ? 0.8750 0.9602 1.0071 0.0924  0.0293  -0.0046 957  TYR B CE1 
8591  C  CE2 . TYR B 957  ? 0.8884 0.9838 1.0293 0.0950  0.0225  -0.0079 957  TYR B CE2 
8592  C  CZ  . TYR B 957  ? 0.8853 0.9762 1.0230 0.0922  0.0255  -0.0070 957  TYR B CZ  
8593  O  OH  . TYR B 957  ? 0.9622 1.0539 1.1018 0.0895  0.0247  -0.0085 957  TYR B OH  
8594  N  N   . VAL B 958  ? 0.7312 0.8139 0.8672 0.1022  0.0343  0.0023  958  VAL B N   
8595  C  CA  . VAL B 958  ? 0.7337 0.8178 0.8765 0.1005  0.0351  0.0027  958  VAL B CA  
8596  C  C   . VAL B 958  ? 0.7387 0.8154 0.8753 0.0976  0.0386  0.0038  958  VAL B C   
8597  O  O   . VAL B 958  ? 0.8534 0.9236 0.9816 0.0982  0.0415  0.0053  958  VAL B O   
8598  C  CB  . VAL B 958  ? 0.7136 0.8005 0.8615 0.1037  0.0360  0.0042  958  VAL B CB  
8599  C  CG1 . VAL B 958  ? 0.8947 0.9756 1.0343 0.1068  0.0393  0.0067  958  VAL B CG1 
8600  C  CG2 . VAL B 958  ? 0.7310 0.8185 0.8853 0.1017  0.0376  0.0048  958  VAL B CG2 
8601  N  N   . ILE B 959  ? 0.9009 0.9781 1.0410 0.0945  0.0381  0.0028  959  ILE B N   
8602  C  CA  . ILE B 959  ? 0.9357 1.0067 1.0703 0.0918  0.0406  0.0033  959  ILE B CA  
8603  C  C   . ILE B 959  ? 0.9986 1.0677 1.1361 0.0920  0.0431  0.0050  959  ILE B C   
8604  O  O   . ILE B 959  ? 1.0315 1.1051 1.1771 0.0922  0.0420  0.0048  959  ILE B O   
8605  C  CB  . ILE B 959  ? 0.8683 0.9409 1.0035 0.0888  0.0384  0.0010  959  ILE B CB  
8606  C  CG1 . ILE B 959  ? 0.9663 1.0424 1.1005 0.0890  0.0357  -0.0008 959  ILE B CG1 
8607  C  CG2 . ILE B 959  ? 0.8205 0.8872 0.9490 0.0863  0.0406  0.0011  959  ILE B CG2 
8608  C  CD1 . ILE B 959  ? 0.8263 0.9041 0.9602 0.0864  0.0338  -0.0031 959  ILE B CD1 
8609  N  N   . SER B 960  ? 1.2697 1.3317 1.4002 0.0919  0.0466  0.0067  960  SER B N   
8610  C  CA  . SER B 960  ? 1.2498 1.3089 1.3815 0.0922  0.0494  0.0085  960  SER B CA  
8611  C  C   . SER B 960  ? 1.3360 1.3952 1.4703 0.0896  0.0486  0.0074  960  SER B C   
8612  O  O   . SER B 960  ? 1.3897 1.4505 1.5235 0.0875  0.0461  0.0054  960  SER B O   
8613  C  CB  . SER B 960  ? 1.3114 1.3621 1.4338 0.0927  0.0533  0.0102  960  SER B CB  
8614  O  OG  . SER B 960  ? 1.3932 1.4403 1.5156 0.0928  0.0560  0.0117  960  SER B OG  
8615  N  N   . ASP B 961  ? 0.8987 0.9560 1.0352 0.0900  0.0510  0.0090  961  ASP B N   
8616  C  CA  . ASP B 961  ? 0.7899 0.8461 0.9279 0.0881  0.0507  0.0084  961  ASP B CA  
8617  C  C   . ASP B 961  ? 0.7878 0.8380 0.9170 0.0864  0.0512  0.0078  961  ASP B C   
8618  O  O   . ASP B 961  ? 0.8716 0.9230 1.0004 0.0846  0.0487  0.0058  961  ASP B O   
8619  C  CB  . ASP B 961  ? 0.9101 0.9654 1.0524 0.0891  0.0537  0.0104  961  ASP B CB  
8620  C  CG  . ASP B 961  ? 0.9732 1.0278 1.1181 0.0874  0.0533  0.0099  961  ASP B CG  
8621  O  OD1 . ASP B 961  ? 0.9309 0.9875 1.0763 0.0859  0.0500  0.0077  961  ASP B OD1 
8622  O  OD2 . ASP B 961  ? 0.8717 0.9234 1.0178 0.0879  0.0564  0.0117  961  ASP B OD2 
8623  N  N   . GLY B 962  ? 0.8374 0.8812 0.9595 0.0870  0.0544  0.0093  962  GLY B N   
8624  C  CA  . GLY B 962  ? 0.9536 0.9917 1.0673 0.0852  0.0549  0.0084  962  GLY B CA  
8625  C  C   . GLY B 962  ? 0.8811 0.9190 0.9899 0.0836  0.0536  0.0067  962  GLY B C   
8626  O  O   . GLY B 962  ? 0.8578 0.8907 0.9593 0.0819  0.0544  0.0059  962  GLY B O   
8627  N  N   . ALA B 963  ? 0.6874 0.7304 0.7997 0.0838  0.0516  0.0059  963  ALA B N   
8628  C  CA  . ALA B 963  ? 0.6875 0.7299 0.7948 0.0822  0.0510  0.0045  963  ALA B CA  
8629  C  C   . ALA B 963  ? 0.6675 0.7119 0.7738 0.0793  0.0486  0.0018  963  ALA B C   
8630  O  O   . ALA B 963  ? 0.6147 0.6563 0.7150 0.0771  0.0493  0.0005  963  ALA B O   
8631  C  CB  . ALA B 963  ? 0.6316 0.6789 0.7426 0.0838  0.0495  0.0044  963  ALA B CB  
8632  N  N   . ILE B 964  ? 0.8238 0.8731 0.9359 0.0793  0.0459  0.0006  964  ILE B N   
8633  C  CA  . ILE B 964  ? 0.7740 0.8261 0.8858 0.0773  0.0434  -0.0020 964  ILE B CA  
8634  C  C   . ILE B 964  ? 0.7464 0.7952 0.8565 0.0774  0.0437  -0.0018 964  ILE B C   
8635  O  O   . ILE B 964  ? 0.7978 0.8455 0.9109 0.0791  0.0445  -0.0002 964  ILE B O   
8636  C  CB  . ILE B 964  ? 0.6850 0.7443 0.8034 0.0778  0.0400  -0.0035 964  ILE B CB  
8637  C  CG1 . ILE B 964  ? 0.7138 0.7758 0.8339 0.0786  0.0398  -0.0031 964  ILE B CG1 
8638  C  CG2 . ILE B 964  ? 0.6148 0.6774 0.7321 0.0760  0.0375  -0.0063 964  ILE B CG2 
8639  C  CD1 . ILE B 964  ? 0.6654 0.7340 0.7917 0.0794  0.0364  -0.0046 964  ILE B CD1 
8640  N  N   . GLN B 965  ? 0.7120 0.7595 0.8171 0.0756  0.0432  -0.0037 965  GLN B N   
8641  C  CA  . GLN B 965  ? 0.7597 0.8042 0.8620 0.0760  0.0429  -0.0040 965  GLN B CA  
8642  C  C   . GLN B 965  ? 0.7228 0.7714 0.8240 0.0743  0.0399  -0.0072 965  GLN B C   
8643  O  O   . GLN B 965  ? 0.7469 0.7953 0.8442 0.0720  0.0401  -0.0089 965  GLN B O   
8644  C  CB  . GLN B 965  ? 0.7990 0.8356 0.8944 0.0760  0.0461  -0.0025 965  GLN B CB  
8645  C  CG  . GLN B 965  ? 0.8615 0.8942 0.9582 0.0783  0.0493  0.0008  965  GLN B CG  
8646  C  CD  . GLN B 965  ? 0.8394 0.8639 0.9285 0.0786  0.0525  0.0021  965  GLN B CD  
8647  O  OE1 . GLN B 965  ? 0.7127 0.7342 0.7954 0.0770  0.0522  0.0004  965  GLN B OE1 
8648  N  NE2 . GLN B 965  ? 0.9818 1.0028 1.0716 0.0808  0.0556  0.0050  965  GLN B NE2 
8649  N  N   . THR B 966  ? 0.6311 0.6831 0.7356 0.0756  0.0373  -0.0082 966  THR B N   
8650  C  CA  . THR B 966  ? 0.6208 0.6773 0.7245 0.0748  0.0343  -0.0113 966  THR B CA  
8651  C  C   . THR B 966  ? 0.6979 0.7507 0.7951 0.0742  0.0345  -0.0123 966  THR B C   
8652  O  O   . THR B 966  ? 0.7059 0.7518 0.7989 0.0752  0.0368  -0.0104 966  THR B O   
8653  C  CB  . THR B 966  ? 0.6918 0.7517 0.7996 0.0770  0.0316  -0.0119 966  THR B CB  
8654  O  OG1 . THR B 966  ? 0.6927 0.7468 0.7990 0.0791  0.0329  -0.0098 966  THR B OG1 
8655  C  CG2 . THR B 966  ? 0.8028 0.8668 0.9170 0.0773  0.0309  -0.0115 966  THR B CG2 
8656  N  N   . ALA B 967  ? 0.5004 0.5580 0.5966 0.0728  0.0321  -0.0156 967  ALA B N   
8657  C  CA  . ALA B 967  ? 0.5113 0.5664 0.6014 0.0719  0.0318  -0.0173 967  ALA B CA  
8658  C  C   . ALA B 967  ? 0.5240 0.5749 0.6109 0.0752  0.0311  -0.0164 967  ALA B C   
8659  O  O   . ALA B 967  ? 0.5610 0.6057 0.6416 0.0755  0.0324  -0.0160 967  ALA B O   
8660  C  CB  . ALA B 967  ? 0.5260 0.5889 0.6171 0.0698  0.0290  -0.0213 967  ALA B CB  
8661  N  N   . CYS B 968  ? 0.6680 0.7213 0.7583 0.0779  0.0292  -0.0161 968  CYS B N   
8662  C  CA  . CYS B 968  ? 0.6899 0.7380 0.7765 0.0813  0.0290  -0.0149 968  CYS B CA  
8663  C  C   . CYS B 968  ? 0.6823 0.7223 0.7675 0.0823  0.0330  -0.0111 968  CYS B C   
8664  O  O   . CYS B 968  ? 0.6593 0.6929 0.7391 0.0845  0.0340  -0.0098 968  CYS B O   
8665  C  CB  . CYS B 968  ? 0.7367 0.7886 0.8270 0.0838  0.0264  -0.0155 968  CYS B CB  
8666  S  SG  . CYS B 968  ? 0.8000 0.8548 0.8987 0.0833  0.0271  -0.0139 968  CYS B SG  
8667  N  N   . GLU B 969  ? 0.7056 0.7458 0.7952 0.0810  0.0352  -0.0092 969  GLU B N   
8668  C  CA  . GLU B 969  ? 0.6349 0.6686 0.7240 0.0819  0.0391  -0.0057 969  GLU B CA  
8669  C  C   . GLU B 969  ? 0.7315 0.7593 0.8137 0.0811  0.0416  -0.0052 969  GLU B C   
8670  O  O   . GLU B 969  ? 0.8633 0.8841 0.9413 0.0829  0.0442  -0.0030 969  GLU B O   
8671  C  CB  . GLU B 969  ? 0.6710 0.7076 0.7672 0.0811  0.0403  -0.0042 969  GLU B CB  
8672  C  CG  . GLU B 969  ? 0.6895 0.7210 0.7865 0.0822  0.0443  -0.0008 969  GLU B CG  
8673  C  CD  . GLU B 969  ? 0.8292 0.8647 0.9335 0.0817  0.0449  0.0003  969  GLU B CD  
8674  O  OE1 . GLU B 969  ? 0.8390 0.8805 0.9466 0.0805  0.0425  -0.0015 969  GLU B OE1 
8675  O  OE2 . GLU B 969  ? 0.8547 0.8878 0.9615 0.0827  0.0478  0.0029  969  GLU B OE2 
8676  N  N   . GLN B 970  ? 0.6452 0.6751 0.7257 0.0784  0.0410  -0.0072 970  GLN B N   
8677  C  CA  . GLN B 970  ? 0.6530 0.6766 0.7265 0.0773  0.0433  -0.0070 970  GLN B CA  
8678  C  C   . GLN B 970  ? 0.6811 0.7014 0.7474 0.0781  0.0420  -0.0087 970  GLN B C   
8679  O  O   . GLN B 970  ? 0.8658 0.8786 0.9253 0.0787  0.0443  -0.0076 970  GLN B O   
8680  C  CB  . GLN B 970  ? 0.7026 0.7289 0.7762 0.0738  0.0434  -0.0088 970  GLN B CB  
8681  C  CG  . GLN B 970  ? 0.7017 0.7299 0.7805 0.0734  0.0450  -0.0069 970  GLN B CG  
8682  C  CD  . GLN B 970  ? 0.6079 0.6337 0.6833 0.0707  0.0470  -0.0073 970  GLN B CD  
8683  O  OE1 . GLN B 970  ? 0.7563 0.7774 0.8250 0.0691  0.0478  -0.0085 970  GLN B OE1 
8684  N  NE2 . GLN B 970  ? 0.6662 0.6948 0.7456 0.0704  0.0477  -0.0064 970  GLN B NE2 
8685  N  N   . ALA B 971  ? 0.4854 0.5112 0.5525 0.0784  0.0381  -0.0115 971  ALA B N   
8686  C  CA  . ALA B 971  ? 0.5116 0.5352 0.5718 0.0795  0.0362  -0.0137 971  ALA B CA  
8687  C  C   . ALA B 971  ? 0.5706 0.5868 0.6261 0.0835  0.0376  -0.0111 971  ALA B C   
8688  O  O   . ALA B 971  ? 0.5556 0.5656 0.6032 0.0846  0.0383  -0.0112 971  ALA B O   
8689  C  CB  . ALA B 971  ? 0.6155 0.6479 0.6783 0.0792  0.0315  -0.0174 971  ALA B CB  
8690  N  N   . CYS B 972  ? 0.6553 0.6718 0.7155 0.0858  0.0382  -0.0087 972  CYS B N   
8691  C  CA  . CYS B 972  ? 0.6729 0.6825 0.7291 0.0895  0.0399  -0.0062 972  CYS B CA  
8692  C  C   . CYS B 972  ? 0.6879 0.6885 0.7383 0.0902  0.0442  -0.0035 972  CYS B C   
8693  O  O   . CYS B 972  ? 0.7373 0.7365 0.7913 0.0892  0.0477  -0.0010 972  CYS B O   
8694  C  CB  . CYS B 972  ? 0.6792 0.6905 0.7425 0.0906  0.0407  -0.0041 972  CYS B CB  
8695  S  SG  . CYS B 972  ? 0.7435 0.7466 0.8021 0.0950  0.0425  -0.0014 972  CYS B SG  
8696  N  N   . PRO B 973  ? 0.8733 0.8677 0.9143 0.0923  0.0442  -0.0040 973  PRO B N   
8697  C  CA  . PRO B 973  ? 0.9188 0.9040 0.9535 0.0934  0.0486  -0.0014 973  PRO B CA  
8698  C  C   . PRO B 973  ? 0.8956 0.8754 0.9315 0.0960  0.0527  0.0028  973  PRO B C   
8699  O  O   . PRO B 973  ? 0.9125 0.8863 0.9461 0.0966  0.0572  0.0056  973  PRO B O   
8700  C  CB  . PRO B 973  ? 0.8785 0.8591 0.9026 0.0951  0.0466  -0.0036 973  PRO B CB  
8701  C  CG  . PRO B 973  ? 0.8405 0.8262 0.8654 0.0968  0.0421  -0.0059 973  PRO B CG  
8702  C  CD  . PRO B 973  ? 0.8481 0.8438 0.8837 0.0941  0.0400  -0.0071 973  PRO B CD  
8703  N  N   . THR B 974  ? 0.5968 0.5786 0.6364 0.0976  0.0517  0.0034  974  THR B N   
8704  C  CA  . THR B 974  ? 0.5655 0.5423 0.6070 0.0995  0.0558  0.0072  974  THR B CA  
8705  C  C   . THR B 974  ? 0.6304 0.6125 0.6832 0.0973  0.0575  0.0088  974  THR B C   
8706  O  O   . THR B 974  ? 0.6233 0.6020 0.6789 0.0980  0.0617  0.0119  974  THR B O   
8707  C  CB  . THR B 974  ? 0.5737 0.5484 0.6125 0.1025  0.0542  0.0072  974  THR B CB  
8708  O  OG1 . THR B 974  ? 0.6592 0.6423 0.7050 0.1012  0.0500  0.0048  974  THR B OG1 
8709  C  CG2 . THR B 974  ? 0.7060 0.6757 0.7332 0.1054  0.0521  0.0055  974  THR B CG2 
8710  N  N   . GLY B 975  ? 0.7278 0.7183 0.7871 0.0945  0.0544  0.0065  975  GLY B N   
8711  C  CA  . GLY B 975  ? 0.7229 0.7188 0.7926 0.0927  0.0554  0.0076  975  GLY B CA  
8712  C  C   . GLY B 975  ? 0.6075 0.6056 0.6830 0.0933  0.0545  0.0080  975  GLY B C   
8713  O  O   . GLY B 975  ? 0.5553 0.5544 0.6379 0.0927  0.0571  0.0100  975  GLY B O   
8714  N  N   . ALA B 976  ? 0.6635 0.6624 0.7361 0.0945  0.0510  0.0060  976  ALA B N   
8715  C  CA  . ALA B 976  ? 0.6969 0.6967 0.7739 0.0953  0.0501  0.0062  976  ALA B CA  
8716  C  C   . ALA B 976  ? 0.6950 0.7037 0.7813 0.0930  0.0473  0.0044  976  ALA B C   
8717  O  O   . ALA B 976  ? 0.7075 0.7171 0.7992 0.0930  0.0473  0.0049  976  ALA B O   
8718  C  CB  . ALA B 976  ? 0.6893 0.6861 0.7588 0.0983  0.0474  0.0047  976  ALA B CB  
8719  N  N   . ILE B 977  ? 0.6382 0.6531 0.7261 0.0911  0.0450  0.0023  977  ILE B N   
8720  C  CA  . ILE B 977  ? 0.6524 0.6756 0.7480 0.0892  0.0423  0.0005  977  ILE B CA  
8721  C  C   . ILE B 977  ? 0.6412 0.6667 0.7425 0.0873  0.0446  0.0020  977  ILE B C   
8722  O  O   . ILE B 977  ? 0.6260 0.6497 0.7241 0.0866  0.0464  0.0026  977  ILE B O   
8723  C  CB  . ILE B 977  ? 0.6355 0.6642 0.7289 0.0884  0.0382  -0.0029 977  ILE B CB  
8724  C  CG1 . ILE B 977  ? 0.5836 0.6107 0.6713 0.0910  0.0357  -0.0045 977  ILE B CG1 
8725  C  CG2 . ILE B 977  ? 0.6307 0.6676 0.7315 0.0867  0.0358  -0.0046 977  ILE B CG2 
8726  C  CD1 . ILE B 977  ? 0.6229 0.6567 0.7094 0.0904  0.0316  -0.0082 977  ILE B CD1 
8727  N  N   . VAL B 978  ? 0.4846 0.5137 0.5940 0.0866  0.0445  0.0024  978  VAL B N   
8728  C  CA  . VAL B 978  ? 0.4622 0.4945 0.5777 0.0853  0.0462  0.0036  978  VAL B CA  
8729  C  C   . VAL B 978  ? 0.4572 0.4971 0.5791 0.0842  0.0428  0.0015  978  VAL B C   
8730  O  O   . VAL B 978  ? 0.4535 0.4952 0.5790 0.0844  0.0409  0.0006  978  VAL B O   
8731  C  CB  . VAL B 978  ? 0.4482 0.4774 0.5680 0.0858  0.0500  0.0064  978  VAL B CB  
8732  C  CG1 . VAL B 978  ? 0.4280 0.4608 0.5533 0.0851  0.0517  0.0075  978  VAL B CG1 
8733  C  CG2 . VAL B 978  ? 0.5254 0.5463 0.6381 0.0873  0.0534  0.0085  978  VAL B CG2 
8734  N  N   . PHE B 979  ? 0.4976 0.5414 0.6202 0.0831  0.0422  0.0008  979  PHE B N   
8735  C  CA  . PHE B 979  ? 0.5016 0.5523 0.6292 0.0822  0.0392  -0.0011 979  PHE B CA  
8736  C  C   . PHE B 979  ? 0.5128 0.5660 0.6450 0.0820  0.0406  0.0002  979  PHE B C   
8737  O  O   . PHE B 979  ? 0.4638 0.5140 0.5934 0.0823  0.0434  0.0019  979  PHE B O   
8738  C  CB  . PHE B 979  ? 0.4839 0.5373 0.6071 0.0813  0.0369  -0.0035 979  PHE B CB  
8739  C  CG  . PHE B 979  ? 0.5708 0.6307 0.6981 0.0805  0.0345  -0.0052 979  PHE B CG  
8740  C  CD1 . PHE B 979  ? 0.6340 0.6981 0.7644 0.0808  0.0313  -0.0072 979  PHE B CD1 
8741  C  CD2 . PHE B 979  ? 0.6230 0.6841 0.7500 0.0797  0.0356  -0.0047 979  PHE B CD2 
8742  C  CE1 . PHE B 979  ? 0.7031 0.7728 0.8366 0.0804  0.0293  -0.0087 979  PHE B CE1 
8743  C  CE2 . PHE B 979  ? 0.5608 0.6273 0.6906 0.0794  0.0336  -0.0061 979  PHE B CE2 
8744  C  CZ  . PHE B 979  ? 0.6273 0.6983 0.7605 0.0796  0.0304  -0.0082 979  PHE B CZ  
8745  N  N   . GLY B 980  ? 0.9428 1.0014 1.0816 0.0819  0.0385  -0.0008 980  GLY B N   
8746  C  CA  . GLY B 980  ? 1.0586 1.1204 1.2022 0.0822  0.0392  0.0001  980  GLY B CA  
8747  C  C   . GLY B 980  ? 0.9468 1.0143 1.0976 0.0821  0.0363  -0.0014 980  GLY B C   
8748  O  O   . GLY B 980  ? 0.8779 0.9468 1.0295 0.0817  0.0337  -0.0033 980  GLY B O   
8749  N  N   . ASP B 981  ? 0.8784 0.9493 1.0344 0.0827  0.0368  -0.0007 981  ASP B N   
8750  C  CA  . ASP B 981  ? 0.8673 0.9441 1.0303 0.0828  0.0338  -0.0024 981  ASP B CA  
8751  C  C   . ASP B 981  ? 0.8290 0.9058 0.9986 0.0820  0.0341  -0.0023 981  ASP B C   
8752  O  O   . ASP B 981  ? 0.9936 1.0681 1.1654 0.0820  0.0374  -0.0003 981  ASP B O   
8753  C  CB  . ASP B 981  ? 0.8777 0.9585 1.0434 0.0841  0.0339  -0.0018 981  ASP B CB  
8754  C  CG  . ASP B 981  ? 0.8412 0.9284 1.0129 0.0845  0.0302  -0.0039 981  ASP B CG  
8755  O  OD1 . ASP B 981  ? 0.9105 0.9987 1.0830 0.0836  0.0274  -0.0060 981  ASP B OD1 
8756  O  OD2 . ASP B 981  ? 0.7973 0.8884 0.9727 0.0859  0.0299  -0.0036 981  ASP B OD2 
8757  N  N   . ILE B 982  ? 0.5277 0.6067 0.7003 0.0813  0.0310  -0.0046 982  ILE B N   
8758  C  CA  . ILE B 982  ? 0.6173 0.6955 0.7959 0.0802  0.0313  -0.0048 982  ILE B CA  
8759  C  C   . ILE B 982  ? 0.6156 0.6994 0.8031 0.0799  0.0310  -0.0051 982  ILE B C   
8760  O  O   . ILE B 982  ? 0.6042 0.6875 0.7973 0.0788  0.0334  -0.0041 982  ILE B O   
8761  C  CB  . ILE B 982  ? 0.6541 0.7317 0.8318 0.0798  0.0281  -0.0073 982  ILE B CB  
8762  C  CG1 . ILE B 982  ? 0.6222 0.6948 0.7915 0.0804  0.0285  -0.0070 982  ILE B CG1 
8763  C  CG2 . ILE B 982  ? 0.6761 0.7524 0.8599 0.0783  0.0285  -0.0078 982  ILE B CG2 
8764  C  CD1 . ILE B 982  ? 0.5572 0.6231 0.7237 0.0803  0.0323  -0.0046 982  ILE B CD1 
8765  N  N   . ASN B 983  ? 0.7600 0.8496 0.9492 0.0809  0.0282  -0.0065 983  ASN B N   
8766  C  CA  . ASN B 983  ? 0.7359 0.8320 0.9339 0.0810  0.0269  -0.0074 983  ASN B CA  
8767  C  C   . ASN B 983  ? 0.7728 0.8701 0.9734 0.0820  0.0303  -0.0050 983  ASN B C   
8768  O  O   . ASN B 983  ? 0.7232 0.8247 0.9325 0.0813  0.0308  -0.0052 983  ASN B O   
8769  C  CB  . ASN B 983  ? 0.6967 0.7979 0.8942 0.0825  0.0227  -0.0096 983  ASN B CB  
8770  C  CG  . ASN B 983  ? 0.7353 0.8369 0.9330 0.0816  0.0191  -0.0125 983  ASN B CG  
8771  O  OD1 . ASN B 983  ? 0.7806 0.8790 0.9800 0.0798  0.0194  -0.0130 983  ASN B OD1 
8772  N  ND2 . ASN B 983  ? 0.7758 0.8807 0.9712 0.0830  0.0157  -0.0143 983  ASN B ND2 
8773  N  N   . ASP B 984  ? 0.9680 1.0619 1.1616 0.0835  0.0327  -0.0028 984  ASP B N   
8774  C  CA  . ASP B 984  ? 1.0187 1.1128 1.2136 0.0848  0.0362  -0.0004 984  ASP B CA  
8775  C  C   . ASP B 984  ? 1.0190 1.1094 1.2166 0.0833  0.0402  0.0013  984  ASP B C   
8776  O  O   . ASP B 984  ? 0.9647 1.0481 1.1556 0.0828  0.0424  0.0026  984  ASP B O   
8777  C  CB  . ASP B 984  ? 1.1069 1.1968 1.2922 0.0866  0.0378  0.0013  984  ASP B CB  
8778  C  CG  . ASP B 984  ? 1.1368 1.2257 1.3221 0.0884  0.0418  0.0040  984  ASP B CG  
8779  O  OD1 . ASP B 984  ? 1.1825 1.2768 1.3760 0.0892  0.0423  0.0042  984  ASP B OD1 
8780  O  OD2 . ASP B 984  ? 1.0879 1.1706 1.2650 0.0891  0.0445  0.0058  984  ASP B OD2 
8781  N  N   . SER B 985  ? 0.8764 0.9716 1.0837 0.0827  0.0412  0.0013  985  SER B N   
8782  C  CA  . SER B 985  ? 0.8033 0.8952 1.0142 0.0807  0.0451  0.0027  985  SER B CA  
8783  C  C   . SER B 985  ? 0.8721 0.9585 1.0775 0.0821  0.0501  0.0060  985  SER B C   
8784  O  O   . SER B 985  ? 0.9745 1.0549 1.1782 0.0809  0.0536  0.0075  985  SER B O   
8785  C  CB  . SER B 985  ? 0.9204 1.0197 1.1439 0.0794  0.0451  0.0015  985  SER B CB  
8786  O  OG  . SER B 985  ? 0.9593 1.0650 1.1869 0.0818  0.0458  0.0023  985  SER B OG  
8787  N  N   . ASN B 986  ? 0.8708 0.9583 1.0728 0.0848  0.0507  0.0072  986  ASN B N   
8788  C  CA  . ASN B 986  ? 0.8646 0.9466 1.0609 0.0864  0.0555  0.0102  986  ASN B CA  
8789  C  C   . ASN B 986  ? 0.8287 0.9020 1.0128 0.0866  0.0559  0.0109  986  ASN B C   
8790  O  O   . ASN B 986  ? 0.9200 0.9875 1.0982 0.0877  0.0597  0.0132  986  ASN B O   
8791  C  CB  . ASN B 986  ? 0.9805 1.0668 1.1780 0.0895  0.0562  0.0112  986  ASN B CB  
8792  C  CG  . ASN B 986  ? 1.0131 1.1082 1.2230 0.0898  0.0569  0.0110  986  ASN B CG  
8793  O  OD1 . ASN B 986  ? 0.9553 1.0526 1.1730 0.0871  0.0575  0.0102  986  ASN B OD1 
8794  N  ND2 . ASN B 986  ? 1.0821 1.1823 1.2938 0.0931  0.0568  0.0115  986  ASN B ND2 
8795  N  N   . SER B 987  ? 0.7659 0.8385 0.9463 0.0855  0.0521  0.0088  987  SER B N   
8796  C  CA  . SER B 987  ? 0.7709 0.8365 0.9407 0.0854  0.0522  0.0090  987  SER B CA  
8797  C  C   . SER B 987  ? 0.7325 0.7914 0.8995 0.0845  0.0549  0.0102  987  SER B C   
8798  O  O   . SER B 987  ? 0.7223 0.7819 0.8955 0.0833  0.0560  0.0103  987  SER B O   
8799  C  CB  . SER B 987  ? 0.7942 0.8618 0.9619 0.0845  0.0476  0.0063  987  SER B CB  
8800  O  OG  . SER B 987  ? 0.7385 0.8063 0.9095 0.0829  0.0458  0.0049  987  SER B OG  
8801  N  N   . ARG B 988  ? 0.8520 0.9043 1.0092 0.0850  0.0561  0.0109  988  ARG B N   
8802  C  CA  . ARG B 988  ? 0.7955 0.8407 0.9483 0.0848  0.0586  0.0121  988  ARG B CA  
8803  C  C   . ARG B 988  ? 0.7509 0.7958 0.9049 0.0835  0.0559  0.0103  988  ARG B C   
8804  O  O   . ARG B 988  ? 0.8168 0.8574 0.9710 0.0832  0.0581  0.0113  988  ARG B O   
8805  C  CB  . ARG B 988  ? 0.7671 0.8057 0.9088 0.0858  0.0596  0.0127  988  ARG B CB  
8806  C  CG  . ARG B 988  ? 0.8057 0.8423 0.9445 0.0873  0.0629  0.0147  988  ARG B CG  
8807  C  CD  . ARG B 988  ? 0.7207 0.7529 0.8494 0.0876  0.0623  0.0141  988  ARG B CD  
8808  N  NE  . ARG B 988  ? 0.9283 0.9649 1.0569 0.0865  0.0580  0.0116  988  ARG B NE  
8809  C  CZ  . ARG B 988  ? 1.0684 1.1025 1.1895 0.0859  0.0568  0.0103  988  ARG B CZ  
8810  N  NH1 . ARG B 988  ? 1.1177 1.1449 1.2304 0.0863  0.0590  0.0111  988  ARG B NH1 
8811  N  NH2 . ARG B 988  ? 1.1046 1.1433 1.2265 0.0847  0.0534  0.0081  988  ARG B NH2 
8812  N  N   . VAL B 989  ? 0.4969 0.5459 0.6511 0.0830  0.0514  0.0077  989  VAL B N   
8813  C  CA  . VAL B 989  ? 0.4142 0.4629 0.5691 0.0822  0.0487  0.0059  989  VAL B CA  
8814  C  C   . VAL B 989  ? 0.4995 0.5513 0.6639 0.0809  0.0488  0.0056  989  VAL B C   
8815  O  O   . VAL B 989  ? 0.5507 0.5986 0.7154 0.0802  0.0493  0.0055  989  VAL B O   
8816  C  CB  . VAL B 989  ? 0.3706 0.4233 0.5233 0.0821  0.0441  0.0032  989  VAL B CB  
8817  C  CG1 . VAL B 989  ? 0.4978 0.5499 0.6504 0.0818  0.0413  0.0013  989  VAL B CG1 
8818  C  CG2 . VAL B 989  ? 0.4641 0.5142 0.6082 0.0828  0.0442  0.0033  989  VAL B CG2 
8819  N  N   . ALA B 990  ? 0.7435 0.8020 0.9155 0.0805  0.0482  0.0052  990  ALA B N   
8820  C  CA  . ALA B 990  ? 0.7504 0.8128 0.9323 0.0789  0.0481  0.0045  990  ALA B CA  
8821  C  C   . ALA B 990  ? 0.7981 0.8561 0.9824 0.0781  0.0532  0.0068  990  ALA B C   
8822  O  O   . ALA B 990  ? 0.8611 0.9184 1.0507 0.0762  0.0537  0.0062  990  ALA B O   
8823  C  CB  . ALA B 990  ? 0.7202 0.7912 0.9094 0.0792  0.0465  0.0037  990  ALA B CB  
8824  N  N   . LYS B 991  ? 0.7369 0.7915 0.9172 0.0794  0.0571  0.0094  991  LYS B N   
8825  C  CA  . LYS B 991  ? 0.7004 0.7502 0.8820 0.0790  0.0624  0.0119  991  LYS B CA  
8826  C  C   . LYS B 991  ? 0.7185 0.7589 0.8922 0.0790  0.0636  0.0125  991  LYS B C   
8827  O  O   . LYS B 991  ? 0.7862 0.8226 0.9624 0.0777  0.0669  0.0136  991  LYS B O   
8828  C  CB  . LYS B 991  ? 0.7731 0.8217 0.9519 0.0809  0.0663  0.0145  991  LYS B CB  
8829  C  CG  . LYS B 991  ? 0.7586 0.8158 0.9458 0.0813  0.0664  0.0145  991  LYS B CG  
8830  C  CD  . LYS B 991  ? 0.8917 0.9466 1.0752 0.0837  0.0707  0.0172  991  LYS B CD  
8831  C  CE  . LYS B 991  ? 0.9349 0.9986 1.1269 0.0848  0.0708  0.0172  991  LYS B CE  
8832  N  NZ  . LYS B 991  ? 1.0353 1.0964 1.2231 0.0875  0.0750  0.0199  991  LYS B NZ  
8833  N  N   . TRP B 992  ? 0.6432 0.6803 0.8076 0.0804  0.0609  0.0117  992  TRP B N   
8834  C  CA  . TRP B 992  ? 0.6260 0.6545 0.7823 0.0812  0.0615  0.0121  992  TRP B CA  
8835  C  C   . TRP B 992  ? 0.6303 0.6587 0.7896 0.0799  0.0589  0.0101  992  TRP B C   
8836  O  O   . TRP B 992  ? 0.6870 0.7082 0.8434 0.0799  0.0611  0.0110  992  TRP B O   
8837  C  CB  . TRP B 992  ? 0.6737 0.6998 0.8197 0.0832  0.0592  0.0115  992  TRP B CB  
8838  C  CG  . TRP B 992  ? 0.6859 0.7062 0.8244 0.0849  0.0629  0.0138  992  TRP B CG  
8839  C  CD1 . TRP B 992  ? 0.6827 0.7042 0.8172 0.0858  0.0627  0.0140  992  TRP B CD1 
8840  C  CD2 . TRP B 992  ? 0.7224 0.7340 0.8558 0.0860  0.0674  0.0164  992  TRP B CD2 
8841  N  NE1 . TRP B 992  ? 0.6239 0.6381 0.7512 0.0874  0.0666  0.0163  992  TRP B NE1 
8842  C  CE2 . TRP B 992  ? 0.6429 0.6511 0.7693 0.0877  0.0696  0.0178  992  TRP B CE2 
8843  C  CE3 . TRP B 992  ? 0.7215 0.7273 0.8549 0.0858  0.0702  0.0175  992  TRP B CE3 
8844  C  CZ2 . TRP B 992  ? 0.6627 0.6623 0.7822 0.0894  0.0742  0.0204  992  TRP B CZ2 
8845  C  CZ3 . TRP B 992  ? 0.7124 0.7093 0.8388 0.0874  0.0750  0.0203  992  TRP B CZ3 
8846  C  CH2 . TRP B 992  ? 0.7462 0.7403 0.8658 0.0893  0.0768  0.0217  992  TRP B CH2 
8847  N  N   . LYS B 993  ? 0.6828 0.7185 0.8473 0.0790  0.0544  0.0074  993  LYS B N   
8848  C  CA  . LYS B 993  ? 0.7290 0.7646 0.8962 0.0779  0.0517  0.0053  993  LYS B CA  
8849  C  C   . LYS B 993  ? 0.6655 0.7008 0.8413 0.0752  0.0544  0.0056  993  LYS B C   
8850  O  O   . LYS B 993  ? 0.6468 0.6788 0.8234 0.0742  0.0535  0.0044  993  LYS B O   
8851  C  CB  . LYS B 993  ? 0.7051 0.7486 0.8752 0.0778  0.0463  0.0023  993  LYS B CB  
8852  C  CG  . LYS B 993  ? 0.5955 0.6392 0.7573 0.0798  0.0433  0.0013  993  LYS B CG  
8853  C  CD  . LYS B 993  ? 0.6152 0.6634 0.7781 0.0799  0.0383  -0.0018 993  LYS B CD  
8854  C  CE  . LYS B 993  ? 0.5189 0.5667 0.6735 0.0818  0.0359  -0.0028 993  LYS B CE  
8855  N  NZ  . LYS B 993  ? 0.6254 0.6759 0.7800 0.0823  0.0317  -0.0057 993  LYS B NZ  
8856  N  N   . ALA B 994  ? 0.6777 0.7162 0.8600 0.0742  0.0578  0.0072  994  ALA B N   
8857  C  CA  . ALA B 994  ? 0.6866 0.7259 0.8783 0.0713  0.0609  0.0075  994  ALA B CA  
8858  C  C   . ALA B 994  ? 0.7537 0.7830 0.9413 0.0709  0.0666  0.0102  994  ALA B C   
8859  O  O   . ALA B 994  ? 0.8061 0.8348 1.0010 0.0681  0.0699  0.0105  994  ALA B O   
8860  C  CB  . ALA B 994  ? 0.6611 0.7093 0.8622 0.0705  0.0621  0.0079  994  ALA B CB  
8861  N  N   . GLU B 995  ? 0.7839 0.8052 0.9599 0.0737  0.0679  0.0120  995  GLU B N   
8862  C  CA  . GLU B 995  ? 0.7380 0.7488 0.9084 0.0740  0.0735  0.0148  995  GLU B CA  
8863  C  C   . GLU B 995  ? 0.7202 0.7242 0.8892 0.0728  0.0733  0.0138  995  GLU B C   
8864  O  O   . GLU B 995  ? 0.7841 0.7902 0.9533 0.0726  0.0684  0.0110  995  GLU B O   
8865  C  CB  . GLU B 995  ? 0.7464 0.7506 0.9039 0.0778  0.0742  0.0166  995  GLU B CB  
8866  C  CG  . GLU B 995  ? 0.8239 0.8315 0.9812 0.0790  0.0762  0.0182  995  GLU B CG  
8867  C  CD  . GLU B 995  ? 0.8504 0.8583 1.0146 0.0775  0.0823  0.0206  995  GLU B CD  
8868  O  OE1 . GLU B 995  ? 0.8569 0.8574 1.0201 0.0766  0.0869  0.0223  995  GLU B OE1 
8869  O  OE2 . GLU B 995  ? 0.9198 0.9352 1.0902 0.0773  0.0828  0.0209  995  GLU B OE2 
8870  N  N   . GLY B 996  ? 0.6548 0.6499 0.8217 0.0720  0.0791  0.0162  996  GLY B N   
8871  C  CA  . GLY B 996  ? 0.7650 0.7520 0.9300 0.0707  0.0799  0.0157  996  GLY B CA  
8872  C  C   . GLY B 996  ? 0.7855 0.7645 0.9375 0.0746  0.0769  0.0153  996  GLY B C   
8873  O  O   . GLY B 996  ? 0.7540 0.7286 0.9044 0.0742  0.0752  0.0138  996  GLY B O   
8874  N  N   . HIS B 997  ? 0.6774 0.6546 0.8199 0.0784  0.0762  0.0165  997  HIS B N   
8875  C  CA  . HIS B 997  ? 0.6881 0.6584 0.8180 0.0825  0.0735  0.0162  997  HIS B CA  
8876  C  C   . HIS B 997  ? 0.7136 0.6921 0.8428 0.0841  0.0666  0.0131  997  HIS B C   
8877  O  O   . HIS B 997  ? 0.7769 0.7521 0.8962 0.0877  0.0640  0.0127  997  HIS B O   
8878  C  CB  . HIS B 997  ? 0.7009 0.6628 0.8196 0.0859  0.0772  0.0192  997  HIS B CB  
8879  C  CG  . HIS B 997  ? 0.7200 0.6879 0.8403 0.0861  0.0781  0.0202  997  HIS B CG  
8880  N  ND1 . HIS B 997  ? 0.7613 0.7338 0.8910 0.0833  0.0819  0.0215  997  HIS B ND1 
8881  C  CD2 . HIS B 997  ? 0.6866 0.6563 0.8000 0.0890  0.0756  0.0199  997  HIS B CD2 
8882  C  CE1 . HIS B 997  ? 0.7066 0.6830 0.8345 0.0847  0.0819  0.0222  997  HIS B CE1 
8883  N  NE2 . HIS B 997  ? 0.6323 0.6066 0.7503 0.0879  0.0781  0.0212  997  HIS B NE2 
8884  N  N   . ASN B 998  ? 0.6607 0.6501 0.8001 0.0815  0.0636  0.0110  998  ASN B N   
8885  C  CA  . ASN B 998  ? 0.6704 0.6675 0.8095 0.0827  0.0574  0.0082  998  ASN B CA  
8886  C  C   . ASN B 998  ? 0.6323 0.6283 0.7711 0.0829  0.0538  0.0057  998  ASN B C   
8887  O  O   . ASN B 998  ? 0.6840 0.6803 0.8301 0.0800  0.0543  0.0047  998  ASN B O   
8888  C  CB  . ASN B 998  ? 0.7439 0.7523 0.8928 0.0804  0.0559  0.0072  998  ASN B CB  
8889  C  CG  . ASN B 998  ? 0.7802 0.7965 0.9297 0.0811  0.0499  0.0041  998  ASN B CG  
8890  O  OD1 . ASN B 998  ? 0.7192 0.7386 0.8645 0.0827  0.0482  0.0039  998  ASN B OD1 
8891  N  ND2 . ASN B 998  ? 0.8830 0.9023 1.0377 0.0798  0.0469  0.0017  998  ASN B ND2 
8892  N  N   . TYR B 999  ? 0.5430 0.5380 0.6738 0.0862  0.0501  0.0043  999  TYR B N   
8893  C  CA  . TYR B 999  ? 0.6273 0.6205 0.7563 0.0873  0.0467  0.0020  999  TYR B CA  
8894  C  C   . TYR B 999  ? 0.6011 0.6013 0.7270 0.0898  0.0412  -0.0005 999  TYR B C   
8895  O  O   . TYR B 999  ? 0.5991 0.6030 0.7220 0.0910  0.0405  -0.0002 999  TYR B O   
8896  C  CB  . TYR B 999  ? 0.6297 0.6101 0.7496 0.0897  0.0493  0.0035  999  TYR B CB  
8897  C  CG  . TYR B 999  ? 0.5870 0.5630 0.6950 0.0945  0.0486  0.0044  999  TYR B CG  
8898  C  CD1 . TYR B 999  ? 0.6209 0.5931 0.7242 0.0955  0.0522  0.0071  999  TYR B CD1 
8899  C  CD2 . TYR B 999  ? 0.5907 0.5665 0.6921 0.0983  0.0442  0.0023  999  TYR B CD2 
8900  C  CE1 . TYR B 999  ? 0.6696 0.6378 0.7617 0.0999  0.0512  0.0075  999  TYR B CE1 
8901  C  CE2 . TYR B 999  ? 0.6435 0.6161 0.7345 0.1029  0.0432  0.0027  999  TYR B CE2 
8902  C  CZ  . TYR B 999  ? 0.7170 0.6857 0.8033 0.1036  0.0466  0.0052  999  TYR B CZ  
8903  O  OH  . TYR B 999  ? 0.7286 0.6944 0.8044 0.1081  0.0452  0.0053  999  TYR B OH  
8904  N  N   . GLY B 1000 ? 0.6543 0.6560 0.7809 0.0904  0.0376  -0.0031 1000 GLY B N   
8905  C  CA  . GLY B 1000 ? 0.6442 0.6528 0.7686 0.0927  0.0325  -0.0057 1000 GLY B CA  
8906  C  C   . GLY B 1000 ? 0.6581 0.6608 0.7743 0.0967  0.0306  -0.0068 1000 GLY B C   
8907  O  O   . GLY B 1000 ? 0.7434 0.7384 0.8584 0.0968  0.0318  -0.0066 1000 GLY B O   
8908  N  N   . LEU B 1001 ? 0.8306 0.8371 0.9412 0.1000  0.0276  -0.0080 1001 LEU B N   
8909  C  CA  . LEU B 1001 ? 0.9518 0.9534 1.0538 0.1047  0.0256  -0.0089 1001 LEU B CA  
8910  C  C   . LEU B 1001 ? 0.9210 0.9241 1.0253 0.1053  0.0226  -0.0115 1001 LEU B C   
8911  O  O   . LEU B 1001 ? 0.9686 0.9805 1.0797 0.1032  0.0201  -0.0135 1001 LEU B O   
8912  C  CB  . LEU B 1001 ? 0.9225 0.9297 1.0194 0.1077  0.0229  -0.0100 1001 LEU B CB  
8913  C  CG  . LEU B 1001 ? 0.9680 0.9678 1.0551 0.1112  0.0246  -0.0082 1001 LEU B CG  
8914  C  CD1 . LEU B 1001 ? 0.8237 0.8309 0.9071 0.1137  0.0211  -0.0101 1001 LEU B CD1 
8915  C  CD2 . LEU B 1001 ? 0.9611 0.9498 1.0405 0.1151  0.0253  -0.0074 1001 LEU B CD2 
8916  N  N   . LEU B 1002 ? 0.6436 0.6372 0.7411 0.1085  0.0228  -0.0114 1002 LEU B N   
8917  C  CA  . LEU B 1002 ? 0.5759 0.5691 0.6732 0.1101  0.0200  -0.0138 1002 LEU B CA  
8918  C  C   . LEU B 1002 ? 0.6912 0.6876 0.7982 0.1053  0.0199  -0.0150 1002 LEU B C   
8919  O  O   . LEU B 1002 ? 0.6927 0.6969 0.8038 0.1051  0.0164  -0.0177 1002 LEU B O   
8920  C  CB  . LEU B 1002 ? 0.5566 0.5586 0.6516 0.1139  0.0152  -0.0165 1002 LEU B CB  
8921  C  CG  . LEU B 1002 ? 0.5460 0.5469 0.6321 0.1188  0.0144  -0.0161 1002 LEU B CG  
8922  C  CD1 . LEU B 1002 ? 0.6425 0.6536 0.7280 0.1220  0.0097  -0.0193 1002 LEU B CD1 
8923  C  CD2 . LEU B 1002 ? 0.5538 0.5409 0.6303 0.1228  0.0164  -0.0145 1002 LEU B CD2 
8924  N  N   . GLY B 1003 ? 0.7798 0.7703 0.8906 0.1015  0.0239  -0.0130 1003 GLY B N   
8925  C  CA  . GLY B 1003 ? 0.9045 0.8982 1.0250 0.0968  0.0239  -0.0143 1003 GLY B CA  
8926  C  C   . GLY B 1003 ? 0.9264 0.9155 1.0464 0.0972  0.0221  -0.0166 1003 GLY B C   
8927  O  O   . GLY B 1003 ? 0.8734 0.8673 1.0011 0.0940  0.0205  -0.0186 1003 GLY B O   
8928  N  N   . PHE B 1004 ? 0.9929 0.9725 1.1034 0.1014  0.0222  -0.0164 1004 PHE B N   
8929  C  CA  . PHE B 1004 ? 0.9371 0.9109 1.0459 0.1021  0.0206  -0.0187 1004 PHE B CA  
8930  C  C   . PHE B 1004 ? 0.9256 0.9098 1.0374 0.1034  0.0154  -0.0221 1004 PHE B C   
8931  O  O   . PHE B 1004 ? 1.0518 1.0355 1.1670 0.1018  0.0138  -0.0244 1004 PHE B O   
8932  C  CB  . PHE B 1004 ? 0.9065 0.8676 1.0032 0.1072  0.0218  -0.0176 1004 PHE B CB  
8933  C  CG  . PHE B 1004 ? 0.8942 0.8594 0.9834 0.1136  0.0187  -0.0181 1004 PHE B CG  
8934  C  CD1 . PHE B 1004 ? 0.8690 0.8374 0.9555 0.1151  0.0195  -0.0162 1004 PHE B CD1 
8935  C  CD2 . PHE B 1004 ? 0.9709 0.9368 1.0557 0.1180  0.0149  -0.0207 1004 PHE B CD2 
8936  C  CE1 . PHE B 1004 ? 0.9176 0.8906 0.9978 0.1206  0.0165  -0.0170 1004 PHE B CE1 
8937  C  CE2 . PHE B 1004 ? 0.9697 0.9406 1.0485 0.1238  0.0120  -0.0214 1004 PHE B CE2 
8938  C  CZ  . PHE B 1004 ? 0.9391 0.9137 1.0158 0.1250  0.0127  -0.0197 1004 PHE B CZ  
8939  N  N   . LEU B 1005 ? 0.8858 0.8792 0.9962 0.1063  0.0129  -0.0225 1005 LEU B N   
8940  C  CA  . LEU B 1005 ? 0.8905 0.8954 1.0053 0.1065  0.0088  -0.0253 1005 LEU B CA  
8941  C  C   . LEU B 1005 ? 0.8842 0.8972 1.0091 0.1012  0.0092  -0.0253 1005 LEU B C   
8942  O  O   . LEU B 1005 ? 1.0194 1.0356 1.1464 0.0995  0.0112  -0.0232 1005 LEU B O   
8943  C  CB  . LEU B 1005 ? 0.7963 0.8087 0.9069 0.1107  0.0065  -0.0258 1005 LEU B CB  
8944  C  CG  . LEU B 1005 ? 0.8289 0.8352 0.9294 0.1168  0.0056  -0.0260 1005 LEU B CG  
8945  C  CD1 . LEU B 1005 ? 0.8372 0.8511 0.9348 0.1199  0.0042  -0.0260 1005 LEU B CD1 
8946  C  CD2 . LEU B 1005 ? 1.0268 1.0325 1.1253 0.1198  0.0026  -0.0289 1005 LEU B CD2 
8947  N  N   . ASN B 1006 ? 0.7888 0.8046 0.9193 0.0989  0.0073  -0.0276 1006 ASN B N   
8948  C  CA  . ASN B 1006 ? 0.8838 0.9070 1.0237 0.0943  0.0074  -0.0277 1006 ASN B CA  
8949  C  C   . ASN B 1006 ? 0.9456 0.9803 1.0872 0.0952  0.0054  -0.0282 1006 ASN B C   
8950  O  O   . ASN B 1006 ? 0.9551 0.9968 1.0993 0.0953  0.0024  -0.0305 1006 ASN B O   
8951  C  CB  . ASN B 1006 ? 0.8019 0.8244 0.9467 0.0920  0.0056  -0.0304 1006 ASN B CB  
8952  C  CG  . ASN B 1006 ? 0.8945 0.9053 1.0386 0.0901  0.0082  -0.0300 1006 ASN B CG  
8953  O  OD1 . ASN B 1006 ? 1.0646 1.0703 1.2093 0.0880  0.0122  -0.0274 1006 ASN B OD1 
8954  N  ND2 . ASN B 1006 ? 0.8735 0.8795 1.0159 0.0906  0.0062  -0.0327 1006 ASN B ND2 
8955  N  N   . THR B 1007 ? 0.6170 0.6531 0.7564 0.0957  0.0073  -0.0259 1007 THR B N   
8956  C  CA  . THR B 1007 ? 0.5625 0.6084 0.7031 0.0959  0.0061  -0.0260 1007 THR B CA  
8957  C  C   . THR B 1007 ? 0.6007 0.6506 0.7476 0.0922  0.0081  -0.0243 1007 THR B C   
8958  O  O   . THR B 1007 ? 0.5730 0.6310 0.7224 0.0916  0.0068  -0.0250 1007 THR B O   
8959  C  CB  . THR B 1007 ? 0.5067 0.5523 0.6405 0.0990  0.0066  -0.0249 1007 THR B CB  
8960  O  OG1 . THR B 1007 ? 0.6130 0.6501 0.7437 0.0989  0.0099  -0.0223 1007 THR B OG1 
8961  C  CG2 . THR B 1007 ? 0.4760 0.5212 0.6042 0.1034  0.0038  -0.0271 1007 THR B CG2 
8962  N  N   . VAL B 1008 ? 0.7746 0.8189 0.9240 0.0898  0.0113  -0.0223 1008 VAL B N   
8963  C  CA  . VAL B 1008 ? 0.7841 0.8318 0.9393 0.0867  0.0135  -0.0206 1008 VAL B CA  
8964  C  C   . VAL B 1008 ? 0.7911 0.8433 0.9436 0.0876  0.0141  -0.0192 1008 VAL B C   
8965  O  O   . VAL B 1008 ? 0.7891 0.8488 0.9444 0.0870  0.0128  -0.0199 1008 VAL B O   
8966  C  CB  . VAL B 1008 ? 0.7437 0.7976 0.9067 0.0845  0.0115  -0.0224 1008 VAL B CB  
8967  C  CG1 . VAL B 1008 ? 0.7577 0.8132 0.9273 0.0814  0.0143  -0.0206 1008 VAL B CG1 
8968  C  CG2 . VAL B 1008 ? 0.8170 0.8673 0.9813 0.0841  0.0097  -0.0248 1008 VAL B CG2 
8969  N  N   . PRO B 1009 ? 0.6936 0.7410 0.8401 0.0892  0.0162  -0.0174 1009 PRO B N   
8970  C  CA  . PRO B 1009 ? 0.5980 0.6494 0.7416 0.0898  0.0165  -0.0166 1009 PRO B CA  
8971  C  C   . PRO B 1009 ? 0.6172 0.6706 0.7651 0.0872  0.0192  -0.0146 1009 PRO B C   
8972  O  O   . PRO B 1009 ? 0.6288 0.6786 0.7804 0.0854  0.0218  -0.0130 1009 PRO B O   
8973  C  CB  . PRO B 1009 ? 0.6483 0.6929 0.7841 0.0923  0.0179  -0.0153 1009 PRO B CB  
8974  C  CG  . PRO B 1009 ? 0.7440 0.7798 0.8799 0.0919  0.0202  -0.0141 1009 PRO B CG  
8975  C  CD  . PRO B 1009 ? 0.7896 0.8273 0.9308 0.0908  0.0180  -0.0163 1009 PRO B CD  
8976  N  N   . ARG B 1010 ? 0.8479 0.9072 0.9953 0.0870  0.0186  -0.0147 1010 ARG B N   
8977  C  CA  . ARG B 1010 ? 0.8156 0.8763 0.9656 0.0852  0.0212  -0.0128 1010 ARG B CA  
8978  C  C   . ARG B 1010 ? 0.7785 0.8346 0.9230 0.0858  0.0240  -0.0106 1010 ARG B C   
8979  O  O   . ARG B 1010 ? 0.7755 0.8305 0.9214 0.0846  0.0269  -0.0085 1010 ARG B O   
8980  C  CB  . ARG B 1010 ? 0.7326 0.8009 0.8843 0.0846  0.0195  -0.0139 1010 ARG B CB  
8981  C  CG  . ARG B 1010 ? 0.8627 0.9355 1.0200 0.0841  0.0170  -0.0158 1010 ARG B CG  
8982  C  CD  . ARG B 1010 ? 0.9368 1.0159 1.0954 0.0836  0.0162  -0.0162 1010 ARG B CD  
8983  N  NE  . ARG B 1010 ? 0.8950 0.9780 1.0591 0.0832  0.0142  -0.0175 1010 ARG B NE  
8984  C  CZ  . ARG B 1010 ? 0.9089 0.9924 1.0786 0.0821  0.0152  -0.0166 1010 ARG B CZ  
8985  N  NH1 . ARG B 1010 ? 0.9814 1.0619 1.1523 0.0813  0.0186  -0.0142 1010 ARG B NH1 
8986  N  NH2 . ARG B 1010 ? 0.8810 0.9687 1.0554 0.0821  0.0128  -0.0183 1010 ARG B NH2 
8987  N  N   . THR B 1011 ? 0.8258 0.8792 0.9636 0.0879  0.0231  -0.0112 1011 THR B N   
8988  C  CA  . THR B 1011 ? 0.8022 0.8505 0.9338 0.0889  0.0254  -0.0094 1011 THR B CA  
8989  C  C   . THR B 1011 ? 0.8090 0.8486 0.9383 0.0901  0.0275  -0.0079 1011 THR B C   
8990  O  O   . THR B 1011 ? 0.9161 0.9531 1.0424 0.0921  0.0257  -0.0090 1011 THR B O   
8991  C  CB  . THR B 1011 ? 0.7823 0.8332 0.9081 0.0907  0.0230  -0.0112 1011 THR B CB  
8992  O  OG1 . THR B 1011 ? 0.8700 0.9282 0.9979 0.0891  0.0218  -0.0125 1011 THR B OG1 
8993  C  CG2 . THR B 1011 ? 0.8240 0.8692 0.9428 0.0920  0.0249  -0.0097 1011 THR B CG2 
8994  N  N   . THR B 1012 ? 0.4196 0.4546 0.5500 0.0889  0.0315  -0.0052 1012 THR B N   
8995  C  CA  . THR B 1012 ? 0.3913 0.4175 0.5197 0.0895  0.0344  -0.0034 1012 THR B CA  
8996  C  C   . THR B 1012 ? 0.4456 0.4652 0.5662 0.0913  0.0373  -0.0012 1012 THR B C   
8997  O  O   . THR B 1012 ? 0.3585 0.3803 0.4761 0.0915  0.0372  -0.0010 1012 THR B O   
8998  C  CB  . THR B 1012 ? 0.3917 0.4178 0.5285 0.0866  0.0371  -0.0021 1012 THR B CB  
8999  O  OG1 . THR B 1012 ? 0.5001 0.5293 0.6398 0.0852  0.0394  -0.0005 1012 THR B OG1 
9000  C  CG2 . THR B 1012 ? 0.5230 0.5552 0.6670 0.0851  0.0339  -0.0046 1012 THR B CG2 
9001  N  N   . TYR B 1013 ? 0.8146 0.8251 0.9312 0.0926  0.0399  0.0005  1013 TYR B N   
9002  C  CA  . TYR B 1013 ? 0.7270 0.7296 0.8351 0.0948  0.0429  0.0028  1013 TYR B CA  
9003  C  C   . TYR B 1013 ? 0.7268 0.7228 0.8372 0.0932  0.0485  0.0059  1013 TYR B C   
9004  O  O   . TYR B 1013 ? 0.7888 0.7839 0.9054 0.0911  0.0498  0.0060  1013 TYR B O   
9005  C  CB  . TYR B 1013 ? 0.6278 0.6244 0.7266 0.0988  0.0411  0.0021  1013 TYR B CB  
9006  C  CG  . TYR B 1013 ? 0.6676 0.6710 0.7635 0.1008  0.0360  -0.0009 1013 TYR B CG  
9007  C  CD1 . TYR B 1013 ? 0.8192 0.8283 0.9189 0.1008  0.0321  -0.0036 1013 TYR B CD1 
9008  C  CD2 . TYR B 1013 ? 0.6067 0.6108 0.6960 0.1026  0.0350  -0.0012 1013 TYR B CD2 
9009  C  CE1 . TYR B 1013 ? 0.8236 0.8395 0.9212 0.1026  0.0277  -0.0064 1013 TYR B CE1 
9010  C  CE2 . TYR B 1013 ? 0.6690 0.6802 0.7566 0.1040  0.0304  -0.0043 1013 TYR B CE2 
9011  C  CZ  . TYR B 1013 ? 0.7540 0.7712 0.8459 0.1040  0.0270  -0.0068 1013 TYR B CZ  
9012  O  OH  . TYR B 1013 ? 0.7733 0.7982 0.8640 0.1053  0.0227  -0.0098 1013 TYR B OH  
9013  N  N   . LEU B 1014 ? 0.4852 0.4769 0.5907 0.0941  0.0519  0.0082  1014 LEU B N   
9014  C  CA  . LEU B 1014 ? 0.4734 0.4580 0.5795 0.0932  0.0578  0.0114  1014 LEU B CA  
9015  C  C   . LEU B 1014 ? 0.6276 0.6007 0.7224 0.0967  0.0599  0.0130  1014 LEU B C   
9016  O  O   . LEU B 1014 ? 0.5677 0.5385 0.6533 0.0999  0.0586  0.0129  1014 LEU B O   
9017  C  CB  . LEU B 1014 ? 0.5421 0.5291 0.6499 0.0922  0.0607  0.0131  1014 LEU B CB  
9018  C  CG  . LEU B 1014 ? 0.4392 0.4364 0.5579 0.0891  0.0595  0.0120  1014 LEU B CG  
9019  C  CD1 . LEU B 1014 ? 0.5169 0.5167 0.6337 0.0894  0.0605  0.0129  1014 LEU B CD1 
9020  C  CD2 . LEU B 1014 ? 0.4610 0.4591 0.5895 0.0862  0.0629  0.0132  1014 LEU B CD2 
9021  N  N   . ALA B 1015 ? 0.7583 0.7241 0.8534 0.0962  0.0629  0.0143  1015 ALA B N   
9022  C  CA  . ALA B 1015 ? 0.6620 0.6158 0.7457 0.1000  0.0648  0.0158  1015 ALA B CA  
9023  C  C   . ALA B 1015 ? 0.7083 0.6557 0.7835 0.1023  0.0686  0.0186  1015 ALA B C   
9024  O  O   . ALA B 1015 ? 0.7609 0.7099 0.8406 0.1001  0.0724  0.0203  1015 ALA B O   
9025  C  CB  . ALA B 1015 ? 0.6824 0.6287 0.7686 0.0982  0.0686  0.0171  1015 ALA B CB  
9026  N  N   . ARG B 1016 ? 0.7010 0.6412 0.7637 0.1070  0.0675  0.0187  1016 ARG B N   
9027  C  CA  . ARG B 1016 ? 0.6819 0.6150 0.7349 0.1098  0.0708  0.0211  1016 ARG B CA  
9028  C  C   . ARG B 1016 ? 0.7599 0.6819 0.8108 0.1094  0.0782  0.0249  1016 ARG B C   
9029  O  O   . ARG B 1016 ? 0.8579 0.7724 0.9070 0.1098  0.0801  0.0257  1016 ARG B O   
9030  C  CB  . ARG B 1016 ? 0.5927 0.5214 0.6325 0.1154  0.0670  0.0199  1016 ARG B CB  
9031  C  CG  . ARG B 1016 ? 0.5559 0.4766 0.5845 0.1188  0.0701  0.0222  1016 ARG B CG  
9032  C  CD  . ARG B 1016 ? 0.6431 0.5636 0.6607 0.1238  0.0649  0.0199  1016 ARG B CD  
9033  N  NE  . ARG B 1016 ? 0.6755 0.5889 0.6824 0.1269  0.0674  0.0217  1016 ARG B NE  
9034  C  CZ  . ARG B 1016 ? 0.7518 0.6641 0.7481 0.1313  0.0635  0.0200  1016 ARG B CZ  
9035  N  NH1 . ARG B 1016 ? 0.7783 0.6969 0.7736 0.1334  0.0571  0.0165  1016 ARG B NH1 
9036  N  NH2 . ARG B 1016 ? 0.7833 0.6884 0.7698 0.1339  0.0662  0.0217  1016 ARG B NH2 
9037  N  N   . VAL B 1017 ? 0.7422 0.6628 0.7933 0.1085  0.0829  0.0273  1017 VAL B N   
9038  C  CA  . VAL B 1017 ? 0.6497 0.5600 0.6984 0.1083  0.0906  0.0312  1017 VAL B CA  
9039  C  C   . VAL B 1017 ? 0.7824 0.6836 0.8166 0.1131  0.0926  0.0331  1017 VAL B C   
9040  O  O   . VAL B 1017 ? 0.9233 0.8291 0.9547 0.1144  0.0900  0.0321  1017 VAL B O   
9041  C  CB  . VAL B 1017 ? 0.6737 0.5903 0.7353 0.1034  0.0949  0.0324  1017 VAL B CB  
9042  C  CG1 . VAL B 1017 ? 0.7723 0.6789 0.8319 0.1030  0.1033  0.0364  1017 VAL B CG1 
9043  C  CG2 . VAL B 1017 ? 0.7288 0.6551 0.8045 0.0988  0.0922  0.0301  1017 VAL B CG2 
9044  N  N   . ARG B 1018 ? 0.9284 0.8162 0.9528 0.1160  0.0972  0.0358  1018 ARG B N   
9045  C  CA  . ARG B 1018 ? 0.8888 0.7663 0.8981 0.1211  0.0995  0.0379  1018 ARG B CA  
9046  C  C   . ARG B 1018 ? 0.8511 0.7207 0.8599 0.1200  0.1085  0.0421  1018 ARG B C   
9047  O  O   . ARG B 1018 ? 0.7582 0.6279 0.7768 0.1157  0.1133  0.0436  1018 ARG B O   
9048  C  CB  . ARG B 1018 ? 0.8957 0.7627 0.8914 0.1265  0.0977  0.0378  1018 ARG B CB  
9049  C  CG  . ARG B 1018 ? 0.8517 0.7264 0.8464 0.1286  0.0888  0.0337  1018 ARG B CG  
9050  C  CD  . ARG B 1018 ? 0.9276 0.7918 0.9079 0.1349  0.0872  0.0338  1018 ARG B CD  
9051  N  NE  . ARG B 1018 ? 0.9839 0.8374 0.9489 0.1403  0.0896  0.0359  1018 ARG B NE  
9052  C  CZ  . ARG B 1018 ? 1.0202 0.8585 0.9745 0.1434  0.0956  0.0395  1018 ARG B CZ  
9053  N  NH1 . ARG B 1018 ? 1.0210 0.8524 0.9782 0.1414  0.1001  0.0414  1018 ARG B NH1 
9054  N  NH2 . ARG B 1018 ? 1.1138 0.9432 1.0538 0.1487  0.0973  0.0412  1018 ARG B NH2 
9055  N  N   . ASN B 1019 ? 1.0538 0.9169 1.0514 0.1238  0.1108  0.0439  1019 ASN B N   
9056  C  CA  . ASN B 1019 ? 1.1081 0.9629 1.1031 0.1237  0.1195  0.0480  1019 ASN B CA  
9057  C  C   . ASN B 1019 ? 1.1538 0.9934 1.1297 0.1302  0.1219  0.0502  1019 ASN B C   
9058  O  O   . ASN B 1019 ? 1.2715 1.1082 1.2380 0.1337  0.1220  0.0507  1019 ASN B O   
9059  C  CB  . ASN B 1019 ? 1.1616 1.0242 1.1624 0.1219  0.1206  0.0481  1019 ASN B CB  
9060  C  CG  . ASN B 1019 ? 1.2123 1.0698 1.2155 0.1205  0.1300  0.0521  1019 ASN B CG  
9061  O  OD1 . ASN B 1019 ? 1.2302 1.0799 1.2336 0.1194  0.1359  0.0547  1019 ASN B OD1 
9062  N  ND2 . ASN B 1019 ? 1.2625 1.1242 1.2675 0.1203  0.1316  0.0527  1019 ASN B ND2 
9063  N  N   . PRO B 1020 ? 0.7528 0.5819 0.7220 0.1321  0.1239  0.0516  1020 PRO B N   
9064  C  CA  . PRO B 1020 ? 0.8140 0.6279 0.7639 0.1390  0.1259  0.0537  1020 PRO B CA  
9065  C  C   . PRO B 1020 ? 0.9166 0.7183 0.8613 0.1393  0.1362  0.0586  1020 PRO B C   
9066  O  O   . PRO B 1020 ? 0.9420 0.7451 0.8981 0.1339  0.1424  0.0605  1020 PRO B O   
9067  C  CB  . PRO B 1020 ? 0.8148 0.6232 0.7606 0.1408  0.1232  0.0528  1020 PRO B CB  
9068  C  CG  . PRO B 1020 ? 0.7852 0.5997 0.7477 0.1337  0.1255  0.0526  1020 PRO B CG  
9069  C  CD  . PRO B 1020 ? 0.7934 0.6234 0.7716 0.1284  0.1240  0.0510  1020 PRO B CD  
9070  N  N   . SER B 1021 ? 1.2903 1.0803 1.2174 0.1457  0.1379  0.0604  1021 SER B N   
9071  C  CA  . SER B 1021 ? 1.4036 1.1806 1.3230 0.1470  0.1478  0.0652  1021 SER B CA  
9072  C  C   . SER B 1021 ? 1.5020 1.2651 1.4157 0.1476  0.1535  0.0681  1021 SER B C   
9073  O  O   . SER B 1021 ? 1.5452 1.3043 1.4527 0.1505  0.1490  0.0666  1021 SER B O   
9074  C  CB  . SER B 1021 ? 1.4490 1.2177 1.3504 0.1540  0.1474  0.0660  1021 SER B CB  
9075  O  OG  . SER B 1021 ? 1.5331 1.3136 1.4392 0.1533  0.1424  0.0633  1021 SER B OG  
9076  N  N   . GLU B 1022 ? 1.7557 1.5114 1.6716 0.1450  0.1637  0.0722  1022 GLU B N   
9077  C  CA  . GLU B 1022 ? 1.8625 1.6041 1.7733 0.1447  0.1703  0.0752  1022 GLU B CA  
9078  C  C   . GLU B 1022 ? 1.8651 1.5883 1.7522 0.1533  0.1720  0.0776  1022 GLU B C   
9079  O  O   . GLU B 1022 ? 1.8965 1.6078 1.7756 0.1552  0.1738  0.0789  1022 GLU B O   
9080  C  CB  . GLU B 1022 ? 1.9521 1.6922 1.8734 0.1388  0.1810  0.0786  1022 GLU B CB  
9081  C  CG  . GLU B 1022 ? 1.9879 1.7457 1.9329 0.1303  0.1797  0.0762  1022 GLU B CG  
9082  C  CD  . GLU B 1022 ? 1.9677 1.7386 1.9206 0.1294  0.1779  0.0752  1022 GLU B CD  
9083  O  OE1 . GLU B 1022 ? 1.9361 1.7018 1.8760 0.1349  0.1781  0.0763  1022 GLU B OE1 
9084  O  OE2 . GLU B 1022 ? 1.9062 1.6921 1.8777 0.1233  0.1763  0.0731  1022 GLU B OE2 
9085  N  N   . GLU B 1023 ? 1.4391 1.1592 1.3140 0.1588  0.1715  0.0783  1023 GLU B N   
9086  C  CA  . GLU B 1023 ? 1.3706 1.0731 1.2220 0.1676  0.1730  0.0806  1023 GLU B CA  
9087  C  C   . GLU B 1023 ? 1.3571 1.0596 1.1994 0.1731  0.1631  0.0772  1023 GLU B C   
9088  O  O   . GLU B 1023 ? 1.4405 1.1277 1.2658 0.1794  0.1644  0.0790  1023 GLU B O   
9089  C  CB  . GLU B 1023 ? 1.4159 1.1156 1.2570 0.1719  0.1747  0.0818  1023 GLU B CB  
9090  C  CG  . GLU B 1023 ? 1.6081 1.2874 1.4251 0.1803  0.1793  0.0854  1023 GLU B CG  
9091  C  CD  . GLU B 1023 ? 1.5311 1.2049 1.3412 0.1822  0.1862  0.0885  1023 GLU B CD  
9092  O  OE1 . GLU B 1023 ? 1.3911 1.0736 1.2161 0.1760  0.1908  0.0893  1023 GLU B OE1 
9093  O  OE2 . GLU B 1023 ? 1.4162 1.0769 1.2055 0.1903  0.1868  0.0900  1023 GLU B OE2 
9094  N  N   . LEU B 1024 ? 1.3329 1.0522 1.1859 0.1710  0.1534  0.0723  1024 LEU B N   
9095  C  CA  . LEU B 1024 ? 1.3622 1.0835 1.2083 0.1760  0.1439  0.0687  1024 LEU B CA  
9096  C  C   . LEU B 1024 ? 1.4319 1.1537 1.2859 0.1728  0.1430  0.0679  1024 LEU B C   
9097  O  O   . LEU B 1024 ? 1.4052 1.1188 1.2475 0.1784  0.1399  0.0674  1024 LEU B O   
9098  C  CB  . LEU B 1024 ? 1.3182 1.0570 1.1717 0.1753  0.1342  0.0637  1024 LEU B CB  
9099  C  CG  . LEU B 1024 ? 1.2787 1.0150 1.1171 0.1821  0.1305  0.0627  1024 LEU B CG  
9100  C  CD1 . LEU B 1024 ? 1.1757 0.9299 1.0245 0.1792  0.1224  0.0579  1024 LEU B CD1 
9101  C  CD2 . LEU B 1024 ? 1.3463 1.0723 1.1661 0.1910  0.1262  0.0621  1024 LEU B CD2 
9102  N  N   . GLU B 1025 ? 1.8013 1.5327 1.6747 0.1642  0.1454  0.0675  1025 GLU B N   
9103  C  CA  . GLU B 1025 ? 1.7975 1.5298 1.6791 0.1607  0.1443  0.0664  1025 GLU B CA  
9104  C  C   . GLU B 1025 ? 1.9555 1.6684 1.8272 0.1619  0.1530  0.0706  1025 GLU B C   
9105  O  O   . GLU B 1025 ? 1.9866 1.6926 1.8526 0.1643  0.1510  0.0700  1025 GLU B O   
9106  C  CB  . GLU B 1025 ? 1.7401 1.4881 1.6450 0.1512  0.1443  0.0646  1025 GLU B CB  
9107  C  CG  . GLU B 1025 ? 1.7015 1.4685 1.6168 0.1496  0.1349  0.0599  1025 GLU B CG  
9108  C  CD  . GLU B 1025 ? 1.8516 1.6226 1.7638 0.1531  0.1257  0.0561  1025 GLU B CD  
9109  O  OE1 . GLU B 1025 ? 2.1901 1.9558 2.1027 0.1525  0.1262  0.0562  1025 GLU B OE1 
9110  O  OE2 . GLU B 1025 ? 1.6184 1.3981 1.5279 0.1563  0.1182  0.0530  1025 GLU B OE2 
9111  N  N   . LYS B 1026 ? 2.2524 1.9561 2.1217 0.1603  0.1629  0.0749  1026 LYS B N   
9112  C  CA  . LYS B 1026 ? 2.2859 1.9707 2.1463 0.1606  0.1724  0.0793  1026 LYS B CA  
9113  C  C   . LYS B 1026 ? 2.1009 1.7675 1.9367 0.1701  0.1753  0.0825  1026 LYS B C   
9114  O  O   . LYS B 1026 ? 1.9386 1.5949 1.7679 0.1706  0.1844  0.0867  1026 LYS B O   
9115  C  CB  . LYS B 1026 ? 2.2822 1.9679 2.1561 0.1524  0.1824  0.0821  1026 LYS B CB  
9116  C  CG  . LYS B 1026 ? 2.2143 1.9185 2.1128 0.1432  0.1797  0.0789  1026 LYS B CG  
9117  C  CD  . LYS B 1026 ? 2.1726 1.8750 2.0762 0.1402  0.1776  0.0771  1026 LYS B CD  
9118  C  CE  . LYS B 1026 ? 2.0252 1.7448 1.9530 0.1307  0.1760  0.0742  1026 LYS B CE  
9119  N  NZ  . LYS B 1026 ? 2.0166 1.7324 1.9492 0.1270  0.1757  0.0728  1026 LYS B NZ  
9120  N  N   . GLU C 16   ? 2.0418 1.9322 1.7915 0.4321  -0.0473 -0.0982 16   GLU C N   
9121  C  CA  . GLU C 16   ? 1.9599 1.8814 1.7265 0.4309  -0.0483 -0.0994 16   GLU C CA  
9122  C  C   . GLU C 16   ? 1.8952 1.8250 1.6721 0.4251  -0.0475 -0.1019 16   GLU C C   
9123  O  O   . GLU C 16   ? 1.8968 1.8095 1.6704 0.4202  -0.0465 -0.1027 16   GLU C O   
9124  C  CB  . GLU C 16   ? 1.9326 1.8667 1.7115 0.4255  -0.0491 -0.0978 16   GLU C CB  
9125  C  CG  . GLU C 16   ? 2.0482 1.9832 1.8200 0.4323  -0.0505 -0.0958 16   GLU C CG  
9126  C  CD  . GLU C 16   ? 2.0501 2.0105 1.8274 0.4386  -0.0521 -0.0971 16   GLU C CD  
9127  O  OE1 . GLU C 16   ? 2.0269 2.0073 1.8172 0.4359  -0.0519 -0.0991 16   GLU C OE1 
9128  O  OE2 . GLU C 16   ? 1.9825 1.9430 1.7513 0.4463  -0.0534 -0.0960 16   GLU C OE2 
9129  N  N   . ALA C 17   ? 1.7709 1.7267 1.5599 0.4256  -0.0478 -0.1033 17   ALA C N   
9130  C  CA  . ALA C 17   ? 1.6930 1.6590 1.4917 0.4208  -0.0468 -0.1055 17   ALA C CA  
9131  C  C   . ALA C 17   ? 1.6751 1.6679 1.4938 0.4144  -0.0469 -0.1057 17   ALA C C   
9132  O  O   . ALA C 17   ? 1.6838 1.6920 1.5083 0.4162  -0.0479 -0.1048 17   ALA C O   
9133  C  CB  . ALA C 17   ? 1.7580 1.7285 1.5505 0.4284  -0.0464 -0.1073 17   ALA C CB  
9134  N  N   . TYR C 18   ? 1.3241 1.3218 1.1527 0.4070  -0.0458 -0.1070 18   TYR C N   
9135  C  CA  . TYR C 18   ? 1.2153 1.2372 1.0625 0.4003  -0.0454 -0.1072 18   TYR C CA  
9136  C  C   . TYR C 18   ? 1.2403 1.2855 1.0950 0.4033  -0.0446 -0.1088 18   TYR C C   
9137  O  O   . TYR C 18   ? 1.1528 1.2198 1.0230 0.3983  -0.0441 -0.1090 18   TYR C O   
9138  C  CB  . TYR C 18   ? 1.1934 1.2102 1.0477 0.3910  -0.0445 -0.1079 18   TYR C CB  
9139  C  CG  . TYR C 18   ? 1.1758 1.1749 1.0275 0.3861  -0.0451 -0.1063 18   TYR C CG  
9140  C  CD1 . TYR C 18   ? 1.1256 1.1313 0.9837 0.3837  -0.0459 -0.1043 18   TYR C CD1 
9141  C  CD2 . TYR C 18   ? 1.2094 1.1849 1.0523 0.3839  -0.0448 -0.1070 18   TYR C CD2 
9142  C  CE1 . TYR C 18   ? 1.0802 1.0696 0.9358 0.3794  -0.0461 -0.1027 18   TYR C CE1 
9143  C  CE2 . TYR C 18   ? 1.0931 1.0523 0.9340 0.3792  -0.0450 -0.1056 18   TYR C CE2 
9144  C  CZ  . TYR C 18   ? 1.0165 0.9827 0.8636 0.3771  -0.0455 -0.1034 18   TYR C CZ  
9145  O  OH  . TYR C 18   ? 0.9344 0.8842 0.7793 0.3726  -0.0454 -0.1019 18   TYR C OH  
9146  N  N   . LEU C 19   ? 1.6280 1.6689 1.4722 0.4111  -0.0443 -0.1099 19   LEU C N   
9147  C  CA  . LEU C 19   ? 1.6643 1.7266 1.5147 0.4148  -0.0433 -0.1113 19   LEU C CA  
9148  C  C   . LEU C 19   ? 1.7132 1.7684 1.5489 0.4259  -0.0441 -0.1114 19   LEU C C   
9149  O  O   . LEU C 19   ? 1.7936 1.8303 1.6158 0.4299  -0.0437 -0.1119 19   LEU C O   
9150  C  CB  . LEU C 19   ? 1.6708 1.7364 1.5257 0.4110  -0.0413 -0.1130 19   LEU C CB  
9151  C  CG  . LEU C 19   ? 1.6891 1.7777 1.5520 0.4135  -0.0395 -0.1144 19   LEU C CG  
9152  C  CD1 . LEU C 19   ? 1.6582 1.7723 1.5385 0.4087  -0.0392 -0.1140 19   LEU C CD1 
9153  C  CD2 . LEU C 19   ? 1.6298 1.7167 1.4937 0.4104  -0.0375 -0.1159 19   LEU C CD2 
9154  N  N   . LEU C 20   ? 1.8451 1.9150 1.6834 0.4309  -0.0451 -0.1110 20   LEU C N   
9155  C  CA  . LEU C 20   ? 1.9789 2.0406 1.8024 0.4416  -0.0463 -0.1107 20   LEU C CA  
9156  C  C   . LEU C 20   ? 2.0475 2.1175 1.8677 0.4486  -0.0452 -0.1124 20   LEU C C   
9157  O  O   . LEU C 20   ? 1.9860 2.0377 1.7916 0.4539  -0.0449 -0.1127 20   LEU C O   
9158  C  CB  . LEU C 20   ? 1.9329 2.0057 1.7593 0.4446  -0.0483 -0.1097 20   LEU C CB  
9159  C  CG  . LEU C 20   ? 1.9612 2.0300 1.7928 0.4377  -0.0494 -0.1080 20   LEU C CG  
9160  C  CD1 . LEU C 20   ? 1.9516 2.0392 1.7905 0.4396  -0.0513 -0.1078 20   LEU C CD1 
9161  C  CD2 . LEU C 20   ? 1.9768 2.0156 1.7921 0.4392  -0.0499 -0.1062 20   LEU C CD2 
9162  N  N   . PRO C 21   ? 2.1680 2.2644 2.0011 0.4489  -0.0444 -0.1136 21   PRO C N   
9163  C  CA  . PRO C 21   ? 2.0706 2.1753 1.8993 0.4573  -0.0436 -0.1150 21   PRO C CA  
9164  C  C   . PRO C 21   ? 2.0973 2.1992 1.9259 0.4553  -0.0410 -0.1162 21   PRO C C   
9165  O  O   . PRO C 21   ? 2.1559 2.2487 1.9871 0.4478  -0.0402 -0.1162 21   PRO C O   
9166  C  CB  . PRO C 21   ? 2.0217 2.1563 1.8661 0.4570  -0.0436 -0.1158 21   PRO C CB  
9167  C  CG  . PRO C 21   ? 2.0266 2.1708 1.8870 0.4455  -0.0429 -0.1155 21   PRO C CG  
9168  C  CD  . PRO C 21   ? 2.0440 2.1638 1.8970 0.4406  -0.0438 -0.1140 21   PRO C CD  
9169  N  N   . GLY C 22   ? 2.1203 2.2303 1.9457 0.4625  -0.0399 -0.1175 22   GLY C N   
9170  C  CA  . GLY C 22   ? 2.1516 2.2612 1.9768 0.4617  -0.0373 -0.1188 22   GLY C CA  
9171  C  C   . GLY C 22   ? 2.1131 2.2480 1.9572 0.4551  -0.0349 -0.1197 22   GLY C C   
9172  O  O   . GLY C 22   ? 2.2195 2.3710 2.0681 0.4590  -0.0330 -0.1208 22   GLY C O   
9173  N  N   . GLU C 23   ? 1.7671 1.9051 1.6224 0.4450  -0.0347 -0.1191 23   GLU C N   
9174  C  CA  . GLU C 23   ? 1.7089 1.8699 1.5822 0.4379  -0.0322 -0.1198 23   GLU C CA  
9175  C  C   . GLU C 23   ? 1.7692 1.9289 1.6413 0.4370  -0.0292 -0.1209 23   GLU C C   
9176  O  O   . GLU C 23   ? 1.8489 1.9875 1.7082 0.4387  -0.0295 -0.1211 23   GLU C O   
9177  C  CB  . GLU C 23   ? 1.7033 1.8657 1.5874 0.4276  -0.0328 -0.1188 23   GLU C CB  
9178  C  CG  . GLU C 23   ? 1.7555 1.9201 1.6416 0.4277  -0.0356 -0.1177 23   GLU C CG  
9179  C  CD  . GLU C 23   ? 1.6982 1.8909 1.6005 0.4258  -0.0352 -0.1183 23   GLU C CD  
9180  O  OE1 . GLU C 23   ? 1.6295 1.8384 1.5453 0.4195  -0.0325 -0.1190 23   GLU C OE1 
9181  O  OE2 . GLU C 23   ? 1.7001 1.8983 1.6012 0.4306  -0.0374 -0.1182 23   GLU C OE2 
9182  N  N   . THR C 24   ? 1.7558 1.9382 1.6414 0.4344  -0.0262 -0.1217 24   THR C N   
9183  C  CA  . THR C 24   ? 1.7710 1.9554 1.6578 0.4327  -0.0229 -0.1226 24   THR C CA  
9184  C  C   . THR C 24   ? 1.7376 1.9334 1.6397 0.4218  -0.0209 -0.1224 24   THR C C   
9185  O  O   . THR C 24   ? 1.6802 1.8875 1.5940 0.4164  -0.0216 -0.1217 24   THR C O   
9186  C  CB  . THR C 24   ? 1.8356 2.0367 1.7243 0.4394  -0.0203 -0.1237 24   THR C CB  
9187  O  OG1 . THR C 24   ? 1.8799 2.0751 1.7572 0.4494  -0.0226 -0.1237 24   THR C OG1 
9188  C  CG2 . THR C 24   ? 1.8246 2.0202 1.7077 0.4407  -0.0173 -0.1245 24   THR C CG2 
9189  N  N   . TYR C 25   ? 1.4238 1.6152 1.3248 0.4188  -0.0184 -0.1229 25   TYR C N   
9190  C  CA  . TYR C 25   ? 1.3521 1.5543 1.2669 0.4090  -0.0161 -0.1227 25   TYR C CA  
9191  C  C   . TYR C 25   ? 1.3433 1.5734 1.2748 0.4064  -0.0134 -0.1228 25   TYR C C   
9192  O  O   . TYR C 25   ? 1.3793 1.6202 1.3239 0.3983  -0.0129 -0.1222 25   TYR C O   
9193  C  CB  . TYR C 25   ? 1.3475 1.5417 1.2572 0.4078  -0.0136 -0.1234 25   TYR C CB  
9194  C  CG  . TYR C 25   ? 1.3083 1.4754 1.2007 0.4112  -0.0161 -0.1240 25   TYR C CG  
9195  C  CD1 . TYR C 25   ? 1.2802 1.4314 1.1701 0.4055  -0.0186 -0.1236 25   TYR C CD1 
9196  C  CD2 . TYR C 25   ? 1.3678 1.5251 1.2463 0.4199  -0.0160 -0.1249 25   TYR C CD2 
9197  C  CE1 . TYR C 25   ? 1.3112 1.4374 1.1857 0.4082  -0.0209 -0.1244 25   TYR C CE1 
9198  C  CE2 . TYR C 25   ? 1.4403 1.5722 1.3029 0.4227  -0.0184 -0.1256 25   TYR C CE2 
9199  C  CZ  . TYR C 25   ? 1.3371 1.4536 1.1979 0.4166  -0.0208 -0.1254 25   TYR C CZ  
9200  O  OH  . TYR C 25   ? 1.2009 1.2922 1.0463 0.4189  -0.0230 -0.1265 25   TYR C OH  
9201  N  N   . THR C 26   ? 1.1766 1.4187 1.1081 0.4131  -0.0116 -0.1236 26   THR C N   
9202  C  CA  . THR C 26   ? 1.2070 1.4760 1.1546 0.4110  -0.0091 -0.1240 26   THR C CA  
9203  C  C   . THR C 26   ? 1.1915 1.4679 1.1442 0.4114  -0.0125 -0.1238 26   THR C C   
9204  O  O   . THR C 26   ? 1.1210 1.4177 1.0890 0.4064  -0.0113 -0.1240 26   THR C O   
9205  C  CB  . THR C 26   ? 1.1962 1.4759 1.1423 0.4183  -0.0061 -0.1251 26   THR C CB  
9206  O  OG1 . THR C 26   ? 1.2394 1.5060 1.1752 0.4203  -0.0039 -0.1253 26   THR C OG1 
9207  C  CG2 . THR C 26   ? 1.1432 1.4503 1.1075 0.4138  -0.0020 -0.1257 26   THR C CG2 
9208  N  N   . SER C 27   ? 1.8463 2.1060 1.7861 0.4173  -0.0166 -0.1233 27   SER C N   
9209  C  CA  . SER C 27   ? 1.8848 2.1492 1.8278 0.4178  -0.0201 -0.1230 27   SER C CA  
9210  C  C   . SER C 27   ? 1.8193 2.0839 1.7717 0.4078  -0.0210 -0.1220 27   SER C C   
9211  O  O   . SER C 27   ? 1.7682 2.0490 1.7326 0.4043  -0.0217 -0.1221 27   SER C O   
9212  C  CB  . SER C 27   ? 1.9154 2.1595 1.8408 0.4265  -0.0238 -0.1225 27   SER C CB  
9213  O  OG  . SER C 27   ? 1.8451 2.0903 1.7621 0.4362  -0.0231 -0.1234 27   SER C OG  
9214  N  N   . ILE C 28   ? 1.3751 1.6220 1.3221 0.4033  -0.0212 -0.1211 28   ILE C N   
9215  C  CA  . ILE C 28   ? 1.2897 1.5363 1.2455 0.3937  -0.0218 -0.1201 28   ILE C CA  
9216  C  C   . ILE C 28   ? 1.2027 1.4712 1.1757 0.3859  -0.0181 -0.1205 28   ILE C C   
9217  O  O   . ILE C 28   ? 1.0900 1.3697 1.0749 0.3795  -0.0186 -0.1201 28   ILE C O   
9218  C  CB  . ILE C 28   ? 1.2769 1.4995 1.2227 0.3910  -0.0227 -0.1194 28   ILE C CB  
9219  C  CG1 . ILE C 28   ? 1.2781 1.4790 1.2086 0.3970  -0.0265 -0.1187 28   ILE C CG1 
9220  C  CG2 . ILE C 28   ? 1.2823 1.5070 1.2387 0.3805  -0.0224 -0.1185 28   ILE C CG2 
9221  C  CD1 . ILE C 28   ? 1.2763 1.4524 1.1949 0.3960  -0.0273 -0.1186 28   ILE C CD1 
9222  N  N   . SER C 29   ? 1.1871 1.4617 1.1614 0.3865  -0.0142 -0.1213 29   SER C N   
9223  C  CA  . SER C 29   ? 1.1514 1.4452 1.1411 0.3791  -0.0100 -0.1216 29   SER C CA  
9224  C  C   . SER C 29   ? 1.1441 1.4620 1.1473 0.3785  -0.0094 -0.1224 29   SER C C   
9225  O  O   . SER C 29   ? 1.1281 1.4593 1.1451 0.3704  -0.0083 -0.1223 29   SER C O   
9226  C  CB  . SER C 29   ? 1.1702 1.4643 1.1567 0.3811  -0.0058 -0.1222 29   SER C CB  
9227  O  OG  . SER C 29   ? 1.1542 1.4262 1.1283 0.3813  -0.0066 -0.1218 29   SER C OG  
9228  N  N   . ALA C 30   ? 1.3721 1.6960 1.3715 0.3870  -0.0102 -0.1234 30   ALA C N   
9229  C  CA  . ALA C 30   ? 1.3867 1.7344 1.3990 0.3870  -0.0097 -0.1247 30   ALA C CA  
9230  C  C   . ALA C 30   ? 1.3361 1.6855 1.3521 0.3848  -0.0140 -0.1244 30   ALA C C   
9231  O  O   . ALA C 30   ? 1.3666 1.7349 1.3972 0.3794  -0.0134 -0.1252 30   ALA C O   
9232  C  CB  . ALA C 30   ? 1.3929 1.7463 1.3996 0.3972  -0.0094 -0.1259 30   ALA C CB  
9233  N  N   . LYS C 31   ? 1.2881 1.6178 1.2910 0.3890  -0.0182 -0.1234 31   LYS C N   
9234  C  CA  . LYS C 31   ? 1.3024 1.6325 1.3070 0.3881  -0.0223 -0.1231 31   LYS C CA  
9235  C  C   . LYS C 31   ? 1.3273 1.6591 1.3422 0.3773  -0.0222 -0.1222 31   LYS C C   
9236  O  O   . LYS C 31   ? 1.2996 1.6435 1.3240 0.3738  -0.0238 -0.1226 31   LYS C O   
9237  C  CB  . LYS C 31   ? 1.2351 1.5422 1.2220 0.3955  -0.0263 -0.1221 31   LYS C CB  
9238  C  CG  . LYS C 31   ? 1.2389 1.5477 1.2249 0.3982  -0.0306 -0.1220 31   LYS C CG  
9239  C  CD  . LYS C 31   ? 1.3478 1.6328 1.3151 0.4061  -0.0339 -0.1209 31   LYS C CD  
9240  C  CE  . LYS C 31   ? 1.3455 1.6223 1.3005 0.4149  -0.0327 -0.1214 31   LYS C CE  
9241  N  NZ  . LYS C 31   ? 1.2904 1.5410 1.2266 0.4212  -0.0354 -0.1201 31   LYS C NZ  
9242  N  N   . ILE C 32   ? 1.3297 1.6495 1.3425 0.3720  -0.0203 -0.1210 32   ILE C N   
9243  C  CA  . ILE C 32   ? 1.1835 1.5045 1.2057 0.3618  -0.0200 -0.1201 32   ILE C CA  
9244  C  C   . ILE C 32   ? 1.2091 1.5516 1.2475 0.3547  -0.0156 -0.1209 32   ILE C C   
9245  O  O   . ILE C 32   ? 1.2570 1.6082 1.3067 0.3467  -0.0154 -0.1207 32   ILE C O   
9246  C  CB  . ILE C 32   ? 1.1066 1.4050 1.1196 0.3593  -0.0203 -0.1186 32   ILE C CB  
9247  C  CG1 . ILE C 32   ? 1.1232 1.3998 1.1195 0.3669  -0.0242 -0.1179 32   ILE C CG1 
9248  C  CG2 . ILE C 32   ? 0.9907 1.2891 1.0124 0.3496  -0.0206 -0.1174 32   ILE C CG2 
9249  C  CD1 . ILE C 32   ? 1.1097 1.3634 1.0968 0.3644  -0.0249 -0.1167 32   ILE C CD1 
9250  N  N   . GLY C 33   ? 1.6134 1.9644 1.6531 0.3574  -0.0118 -0.1219 33   GLY C N   
9251  C  CA  . GLY C 33   ? 1.6066 1.9777 1.6611 0.3509  -0.0070 -0.1227 33   GLY C CA  
9252  C  C   . GLY C 33   ? 1.7161 2.1105 1.7832 0.3507  -0.0069 -0.1245 33   GLY C C   
9253  O  O   . GLY C 33   ? 1.6695 2.0811 1.7509 0.3435  -0.0034 -0.1251 33   GLY C O   
9254  N  N   . ASP C 34   ? 2.2922 2.6873 2.3540 0.3584  -0.0107 -0.1253 34   ASP C N   
9255  C  CA  . ASP C 34   ? 2.3283 2.7456 2.4014 0.3590  -0.0113 -0.1273 34   ASP C CA  
9256  C  C   . ASP C 34   ? 2.3082 2.7320 2.3907 0.3521  -0.0139 -0.1275 34   ASP C C   
9257  O  O   . ASP C 34   ? 2.3157 2.7604 2.4112 0.3494  -0.0134 -0.1294 34   ASP C O   
9258  C  CB  . ASP C 34   ? 2.3465 2.7620 2.4098 0.3704  -0.0146 -0.1283 34   ASP C CB  
9259  C  CG  . ASP C 34   ? 2.3884 2.8112 2.4502 0.3765  -0.0111 -0.1294 34   ASP C CG  
9260  O  OD1 . ASP C 34   ? 2.3290 2.7586 2.3976 0.3719  -0.0060 -0.1294 34   ASP C OD1 
9261  O  OD2 . ASP C 34   ? 2.4302 2.8516 2.4834 0.3863  -0.0134 -0.1302 34   ASP C OD2 
9262  N  N   . VAL C 35   ? 1.7677 2.1744 1.8439 0.3493  -0.0166 -0.1256 35   VAL C N   
9263  C  CA  . VAL C 35   ? 1.7343 2.1457 1.8184 0.3427  -0.0191 -0.1255 35   VAL C CA  
9264  C  C   . VAL C 35   ? 1.6620 2.0877 1.7617 0.3320  -0.0147 -0.1259 35   VAL C C   
9265  O  O   . VAL C 35   ? 1.6128 2.0559 1.7250 0.3274  -0.0150 -0.1274 35   VAL C O   
9266  C  CB  . VAL C 35   ? 1.6850 2.0736 1.7581 0.3426  -0.0227 -0.1233 35   VAL C CB  
9267  C  CG1 . VAL C 35   ? 1.5578 1.9511 1.6400 0.3345  -0.0243 -0.1230 35   VAL C CG1 
9268  C  CG2 . VAL C 35   ? 1.6465 2.0226 1.7051 0.3530  -0.0270 -0.1232 35   VAL C CG2 
9269  N  N   . PRO C 36   ? 1.6355 2.0547 1.7350 0.3275  -0.0106 -0.1246 36   PRO C N   
9270  C  CA  . PRO C 36   ? 1.5968 2.0318 1.7109 0.3184  -0.0056 -0.1252 36   PRO C CA  
9271  C  C   . PRO C 36   ? 1.7335 2.1846 1.8533 0.3211  -0.0012 -0.1268 36   PRO C C   
9272  O  O   . PRO C 36   ? 1.8061 2.2577 1.9194 0.3300  -0.0026 -0.1278 36   PRO C O   
9273  C  CB  . PRO C 36   ? 1.5298 1.9492 1.6392 0.3137  -0.0035 -0.1230 36   PRO C CB  
9274  C  CG  . PRO C 36   ? 1.6344 2.0345 1.7274 0.3221  -0.0053 -0.1221 36   PRO C CG  
9275  C  CD  . PRO C 36   ? 1.6026 1.9994 1.6887 0.3299  -0.0105 -0.1227 36   PRO C CD  
9276  N  N   . LEU C 37   ? 1.2045 1.6683 1.3360 0.3135  0.0043  -0.1272 37   LEU C N   
9277  C  CA  . LEU C 37   ? 1.2287 1.7088 1.3673 0.3146  0.0095  -0.1287 37   LEU C CA  
9278  C  C   . LEU C 37   ? 1.3135 1.8128 1.4601 0.3181  0.0079  -0.1314 37   LEU C C   
9279  O  O   . LEU C 37   ? 1.2570 1.7704 1.4092 0.3202  0.0118  -0.1328 37   LEU C O   
9280  C  CB  . LEU C 37   ? 1.1349 1.6031 1.2609 0.3221  0.0114  -0.1279 37   LEU C CB  
9281  C  CG  . LEU C 37   ? 1.1401 1.5895 1.2574 0.3196  0.0131  -0.1256 37   LEU C CG  
9282  C  CD1 . LEU C 37   ? 1.2294 1.6666 1.3331 0.3280  0.0140  -0.1252 37   LEU C CD1 
9283  C  CD2 . LEU C 37   ? 1.2008 1.6591 1.3292 0.3098  0.0190  -0.1252 37   LEU C CD2 
9284  N  N   . THR C 38   ? 1.7770 2.2771 1.9239 0.3190  0.0023  -0.1321 38   THR C N   
9285  C  CA  . THR C 38   ? 1.6514 2.1706 1.8065 0.3219  0.0004  -0.1349 38   THR C CA  
9286  C  C   . THR C 38   ? 1.6442 2.1852 1.8180 0.3121  0.0043  -0.1368 38   THR C C   
9287  O  O   . THR C 38   ? 1.6207 2.1600 1.8002 0.3030  0.0054  -0.1359 38   THR C O   
9288  C  CB  . THR C 38   ? 1.5829 2.0957 1.7320 0.3258  -0.0068 -0.1352 38   THR C CB  
9289  O  OG1 . THR C 38   ? 1.6596 2.1487 1.7911 0.3327  -0.0098 -0.1329 38   THR C OG1 
9290  C  CG2 . THR C 38   ? 1.6151 2.1445 1.7684 0.3320  -0.0094 -0.1381 38   THR C CG2 
9291  N  N   . PRO C 39   ? 1.4736 2.0350 1.6573 0.3135  0.0067  -0.1394 39   PRO C N   
9292  C  CA  . PRO C 39   ? 1.4818 2.0640 1.6836 0.3039  0.0106  -0.1413 39   PRO C CA  
9293  C  C   . PRO C 39   ? 1.4998 2.0859 1.7077 0.2982  0.0061  -0.1424 39   PRO C C   
9294  O  O   . PRO C 39   ? 1.4663 2.0469 1.6672 0.3040  -0.0004 -0.1428 39   PRO C O   
9295  C  CB  . PRO C 39   ? 1.4810 2.0832 1.6902 0.3089  0.0122  -0.1443 39   PRO C CB  
9296  C  CG  . PRO C 39   ? 1.4917 2.0818 1.6867 0.3194  0.0122  -0.1430 39   PRO C CG  
9297  C  CD  . PRO C 39   ? 1.4987 2.0646 1.6774 0.3237  0.0067  -0.1405 39   PRO C CD  
9298  N  N   . PRO C 40   ? 1.3722 1.9670 1.5926 0.2871  0.0095  -0.1428 40   PRO C N   
9299  C  CA  . PRO C 40   ? 1.3421 1.9398 1.5681 0.2813  0.0053  -0.1437 40   PRO C CA  
9300  C  C   . PRO C 40   ? 1.3693 1.9824 1.6007 0.2852  0.0005  -0.1472 40   PRO C C   
9301  O  O   . PRO C 40   ? 1.3719 1.9810 1.6006 0.2856  -0.0053 -0.1476 40   PRO C O   
9302  C  CB  . PRO C 40   ? 1.3679 1.9756 1.6078 0.2688  0.0113  -0.1440 40   PRO C CB  
9303  C  CG  . PRO C 40   ? 1.4068 2.0066 1.6426 0.2685  0.0177  -0.1416 40   PRO C CG  
9304  C  CD  . PRO C 40   ? 1.3584 1.9584 1.5868 0.2793  0.0175  -0.1420 40   PRO C CD  
9305  N  N   . LEU C 41   ? 1.3841 2.0151 1.6230 0.2883  0.0027  -0.1498 41   LEU C N   
9306  C  CA  . LEU C 41   ? 1.3344 1.9811 1.5784 0.2927  -0.0020 -0.1535 41   LEU C CA  
9307  C  C   . LEU C 41   ? 1.3794 2.0143 1.6080 0.3054  -0.0082 -0.1529 41   LEU C C   
9308  O  O   . LEU C 41   ? 1.3573 2.0019 1.5873 0.3099  -0.0132 -0.1557 41   LEU C O   
9309  C  CB  . LEU C 41   ? 1.3327 2.0027 1.5902 0.2921  0.0027  -0.1565 41   LEU C CB  
9310  C  CG  . LEU C 41   ? 1.3298 2.0193 1.6063 0.2800  0.0068  -0.1590 41   LEU C CG  
9311  C  CD1 . LEU C 41   ? 1.3718 2.0543 1.6512 0.2706  0.0139  -0.1563 41   LEU C CD1 
9312  C  CD2 . LEU C 41   ? 1.1513 1.8650 1.4404 0.2814  0.0095  -0.1627 41   LEU C CD2 
9313  N  N   . LYS C 42   ? 1.5697 2.1837 1.7830 0.3111  -0.0080 -0.1496 42   LYS C N   
9314  C  CA  . LYS C 42   ? 1.5434 2.1440 1.7408 0.3229  -0.0133 -0.1488 42   LYS C CA  
9315  C  C   . LYS C 42   ? 1.4288 2.0071 1.6139 0.3231  -0.0178 -0.1461 42   LYS C C   
9316  O  O   . LYS C 42   ? 1.4011 1.9622 1.5706 0.3318  -0.0209 -0.1444 42   LYS C O   
9317  C  CB  . LYS C 42   ? 1.5649 2.1579 1.7531 0.3303  -0.0101 -0.1473 42   LYS C CB  
9318  C  CG  . LYS C 42   ? 1.5697 2.1599 1.7466 0.3433  -0.0143 -0.1482 42   LYS C CG  
9319  C  CD  . LYS C 42   ? 1.6242 2.2393 1.8124 0.3463  -0.0136 -0.1520 42   LYS C CD  
9320  C  CE  . LYS C 42   ? 1.5138 2.1405 1.7114 0.3430  -0.0061 -0.1523 42   LYS C CE  
9321  N  NZ  . LYS C 42   ? 1.5724 2.2262 1.7851 0.3430  -0.0048 -0.1562 42   LYS C NZ  
9322  N  N   . THR C 43   ? 0.8338 1.4120 1.0257 0.3136  -0.0179 -0.1458 43   THR C N   
9323  C  CA  . THR C 43   ? 0.6678 1.2256 0.8492 0.3131  -0.0218 -0.1432 43   THR C CA  
9324  C  C   . THR C 43   ? 0.6714 1.2279 0.8459 0.3206  -0.0287 -0.1445 43   THR C C   
9325  O  O   . THR C 43   ? 0.8341 1.4091 1.0181 0.3203  -0.0308 -0.1479 43   THR C O   
9326  C  CB  . THR C 43   ? 0.6467 1.2066 0.8381 0.3010  -0.0201 -0.1427 43   THR C CB  
9327  O  OG1 . THR C 43   ? 0.6563 1.2162 0.8528 0.2946  -0.0135 -0.1413 43   THR C OG1 
9328  C  CG2 . THR C 43   ? 0.7165 1.2559 0.8975 0.3006  -0.0241 -0.1401 43   THR C CG2 
9329  N  N   . PRO C 44   ? 1.0746 1.6097 1.2326 0.3276  -0.0323 -0.1421 44   PRO C N   
9330  C  CA  . PRO C 44   ? 1.2386 1.7711 1.3889 0.3350  -0.0386 -0.1431 44   PRO C CA  
9331  C  C   . PRO C 44   ? 1.2354 1.7741 1.3935 0.3282  -0.0415 -0.1443 44   PRO C C   
9332  O  O   . PRO C 44   ? 1.2470 1.7823 1.4107 0.3187  -0.0395 -0.1430 44   PRO C O   
9333  C  CB  . PRO C 44   ? 1.2551 1.7606 1.3865 0.3416  -0.0406 -0.1396 44   PRO C CB  
9334  C  CG  . PRO C 44   ? 1.1704 1.6642 1.3018 0.3347  -0.0361 -0.1368 44   PRO C CG  
9335  C  CD  . PRO C 44   ? 1.1291 1.6414 1.2743 0.3295  -0.0307 -0.1385 44   PRO C CD  
9336  N  N   . LYS C 45   ? 1.0386 1.5866 1.1965 0.3335  -0.0463 -0.1470 45   LYS C N   
9337  C  CA  . LYS C 45   ? 0.9993 1.5551 1.1647 0.3278  -0.0494 -0.1488 45   LYS C CA  
9338  C  C   . LYS C 45   ? 1.0707 1.6048 1.2255 0.3267  -0.0521 -0.1456 45   LYS C C   
9339  O  O   . LYS C 45   ? 1.0570 1.5939 1.2186 0.3190  -0.0529 -0.1460 45   LYS C O   
9340  C  CB  . LYS C 45   ? 0.9963 1.5672 1.1631 0.3347  -0.0541 -0.1527 45   LYS C CB  
9341  C  CG  . LYS C 45   ? 0.9617 1.5577 1.1422 0.3342  -0.0517 -0.1564 45   LYS C CG  
9342  C  CD  . LYS C 45   ? 1.1273 1.7395 1.3107 0.3398  -0.0567 -0.1607 45   LYS C CD  
9343  C  CE  . LYS C 45   ? 1.0997 1.7156 1.2883 0.3338  -0.0603 -0.1623 45   LYS C CE  
9344  N  NZ  . LYS C 45   ? 0.5687 1.1997 0.7592 0.3398  -0.0657 -0.1667 45   LYS C NZ  
9345  N  N   . GLY C 46   ? 1.5433 2.0557 1.6814 0.3342  -0.0532 -0.1425 46   GLY C N   
9346  C  CA  . GLY C 46   ? 1.5116 2.0028 1.6396 0.3332  -0.0554 -0.1394 46   GLY C CA  
9347  C  C   . GLY C 46   ? 1.4170 1.9018 1.5510 0.3224  -0.0515 -0.1371 46   GLY C C   
9348  O  O   . GLY C 46   ? 1.3716 1.8492 1.5056 0.3174  -0.0530 -0.1358 46   GLY C O   
9349  N  N   . TRP C 47   ? 1.0946 1.5818 1.2333 0.3191  -0.0465 -0.1364 47   TRP C N   
9350  C  CA  . TRP C 47   ? 1.0961 1.5792 1.2412 0.3088  -0.0425 -0.1345 47   TRP C CA  
9351  C  C   . TRP C 47   ? 1.1284 1.6290 1.2894 0.2991  -0.0419 -0.1367 47   TRP C C   
9352  O  O   . TRP C 47   ? 1.1327 1.6270 1.2964 0.2914  -0.0411 -0.1352 47   TRP C O   
9353  C  CB  . TRP C 47   ? 1.1041 1.5880 1.2510 0.3079  -0.0371 -0.1338 47   TRP C CB  
9354  C  CG  . TRP C 47   ? 1.0564 1.5331 1.2071 0.2988  -0.0330 -0.1315 47   TRP C CG  
9355  C  CD1 . TRP C 47   ? 1.0284 1.4840 1.1688 0.2993  -0.0321 -0.1283 47   TRP C CD1 
9356  C  CD2 . TRP C 47   ? 1.0242 1.5145 1.1899 0.2881  -0.0292 -0.1325 47   TRP C CD2 
9357  N  NE1 . TRP C 47   ? 1.0075 1.4632 1.1554 0.2898  -0.0281 -0.1271 47   TRP C NE1 
9358  C  CE2 . TRP C 47   ? 1.0140 1.4905 1.1771 0.2828  -0.0262 -0.1295 47   TRP C CE2 
9359  C  CE3 . TRP C 47   ? 0.9878 1.5006 1.1686 0.2823  -0.0280 -0.1356 47   TRP C CE3 
9360  C  CZ2 . TRP C 47   ? 0.9818 1.4658 1.1563 0.2724  -0.0219 -0.1295 47   TRP C CZ2 
9361  C  CZ3 . TRP C 47   ? 1.0094 1.5293 1.2017 0.2715  -0.0236 -0.1356 47   TRP C CZ3 
9362  C  CH2 . TRP C 47   ? 0.9706 1.4760 1.1594 0.2668  -0.0206 -0.1324 47   TRP C CH2 
9363  N  N   . LEU C 48   ? 1.0771 1.5997 1.2486 0.2992  -0.0421 -0.1405 48   LEU C N   
9364  C  CA  . LEU C 48   ? 1.1032 1.6432 1.2900 0.2897  -0.0415 -0.1431 48   LEU C CA  
9365  C  C   . LEU C 48   ? 1.1007 1.6362 1.2849 0.2889  -0.0466 -0.1434 48   LEU C C   
9366  O  O   . LEU C 48   ? 1.1009 1.6392 1.2932 0.2798  -0.0458 -0.1435 48   LEU C O   
9367  C  CB  . LEU C 48   ? 1.1271 1.6916 1.3253 0.2907  -0.0409 -0.1474 48   LEU C CB  
9368  C  CG  . LEU C 48   ? 0.9738 1.5457 1.1762 0.2914  -0.0355 -0.1475 48   LEU C CG  
9369  C  CD1 . LEU C 48   ? 1.1774 1.7720 1.3886 0.2949  -0.0360 -0.1517 48   LEU C CD1 
9370  C  CD2 . LEU C 48   ? 0.8358 1.4103 1.0482 0.2803  -0.0293 -0.1464 48   LEU C CD2 
9371  N  N   . ALA C 49   ? 0.9574 1.4855 1.1300 0.2986  -0.0517 -0.1434 49   ALA C N   
9372  C  CA  . ALA C 49   ? 0.9251 1.4475 1.0936 0.2988  -0.0566 -0.1435 49   ALA C CA  
9373  C  C   . ALA C 49   ? 0.9539 1.4550 1.1153 0.2948  -0.0559 -0.1394 49   ALA C C   
9374  O  O   . ALA C 49   ? 0.9377 1.4386 1.1033 0.2886  -0.0571 -0.1394 49   ALA C O   
9375  C  CB  . ALA C 49   ? 0.8334 1.3516 0.9897 0.3108  -0.0618 -0.1444 49   ALA C CB  
9376  N  N   . GLY C 50   ? 1.3046 1.7878 1.4555 0.2984  -0.0539 -0.1359 50   GLY C N   
9377  C  CA  . GLY C 50   ? 1.2810 1.7443 1.4256 0.2946  -0.0531 -0.1321 50   GLY C CA  
9378  C  C   . GLY C 50   ? 1.2850 1.7536 1.4417 0.2829  -0.0489 -0.1317 50   GLY C C   
9379  O  O   . GLY C 50   ? 1.2502 1.7109 1.4073 0.2774  -0.0494 -0.1301 50   GLY C O   
9380  N  N   . PHE C 51   ? 1.5808 2.0627 1.7473 0.2790  -0.0444 -0.1330 51   PHE C N   
9381  C  CA  . PHE C 51   ? 1.5503 2.0381 1.7283 0.2678  -0.0400 -0.1327 51   PHE C CA  
9382  C  C   . PHE C 51   ? 1.5242 2.0268 1.7139 0.2607  -0.0413 -0.1354 51   PHE C C   
9383  O  O   . PHE C 51   ? 1.5994 2.1004 1.7949 0.2519  -0.0393 -0.1345 51   PHE C O   
9384  C  CB  . PHE C 51   ? 1.5212 2.0200 1.7065 0.2659  -0.0346 -0.1336 51   PHE C CB  
9385  C  CG  . PHE C 51   ? 1.4635 1.9676 1.6596 0.2549  -0.0294 -0.1332 51   PHE C CG  
9386  C  CD1 . PHE C 51   ? 1.4176 1.9055 1.6091 0.2511  -0.0274 -0.1298 51   PHE C CD1 
9387  C  CD2 . PHE C 51   ? 1.5043 2.0297 1.7153 0.2483  -0.0264 -0.1363 51   PHE C CD2 
9388  C  CE1 . PHE C 51   ? 1.4339 1.9263 1.6346 0.2414  -0.0225 -0.1294 51   PHE C CE1 
9389  C  CE2 . PHE C 51   ? 1.5637 2.0932 1.7840 0.2382  -0.0213 -0.1358 51   PHE C CE2 
9390  C  CZ  . PHE C 51   ? 1.4529 1.9658 1.6677 0.2349  -0.0193 -0.1323 51   PHE C CZ  
9391  N  N   . SER C 52   ? 1.2143 1.7312 1.4074 0.2644  -0.0448 -0.1389 52   SER C N   
9392  C  CA  . SER C 52   ? 1.2424 1.7729 1.4459 0.2581  -0.0467 -0.1418 52   SER C CA  
9393  C  C   . SER C 52   ? 1.2682 1.7844 1.4644 0.2578  -0.0505 -0.1400 52   SER C C   
9394  O  O   . SER C 52   ? 1.2606 1.7803 1.4643 0.2493  -0.0500 -0.1405 52   SER C O   
9395  C  CB  . SER C 52   ? 1.1964 1.7451 1.4043 0.2631  -0.0500 -0.1462 52   SER C CB  
9396  O  OG  . SER C 52   ? 1.2966 1.8357 1.4914 0.2733  -0.0556 -0.1459 52   SER C OG  
9397  N  N   . VAL C 53   ? 1.1484 1.6480 1.3297 0.2669  -0.0541 -0.1378 53   VAL C N   
9398  C  CA  . VAL C 53   ? 1.1283 1.6124 1.3016 0.2671  -0.0573 -0.1356 53   VAL C CA  
9399  C  C   . VAL C 53   ? 1.1614 1.6327 1.3351 0.2597  -0.0536 -0.1321 53   VAL C C   
9400  O  O   . VAL C 53   ? 1.1020 1.5704 1.2785 0.2539  -0.0543 -0.1315 53   VAL C O   
9401  C  CB  . VAL C 53   ? 1.1123 1.5803 1.2688 0.2787  -0.0611 -0.1338 53   VAL C CB  
9402  C  CG1 . VAL C 53   ? 1.0813 1.5292 1.2283 0.2787  -0.0629 -0.1304 53   VAL C CG1 
9403  C  CG2 . VAL C 53   ? 1.0766 1.5571 1.2323 0.2857  -0.0657 -0.1374 53   VAL C CG2 
9404  N  N   . ALA C 54   ? 1.2857 1.7494 1.4568 0.2600  -0.0496 -0.1299 54   ALA C N   
9405  C  CA  . ALA C 54   ? 1.2318 1.6834 1.4029 0.2536  -0.0462 -0.1267 54   ALA C CA  
9406  C  C   . ALA C 54   ? 1.2304 1.6957 1.4162 0.2423  -0.0426 -0.1281 54   ALA C C   
9407  O  O   . ALA C 54   ? 1.2071 1.6648 1.3942 0.2360  -0.0414 -0.1262 54   ALA C O   
9408  C  CB  . ALA C 54   ? 1.1426 1.5841 1.3074 0.2569  -0.0429 -0.1245 54   ALA C CB  
9409  N  N   . PHE C 55   ? 1.1727 1.6583 1.3696 0.2396  -0.0408 -0.1315 55   PHE C N   
9410  C  CA  . PHE C 55   ? 1.1507 1.6496 1.3616 0.2286  -0.0371 -0.1331 55   PHE C CA  
9411  C  C   . PHE C 55   ? 1.1238 1.6279 1.3393 0.2244  -0.0406 -0.1349 55   PHE C C   
9412  O  O   . PHE C 55   ? 1.0629 1.5683 1.2853 0.2154  -0.0383 -0.1347 55   PHE C O   
9413  C  CB  . PHE C 55   ? 1.1367 1.6557 1.3583 0.2268  -0.0339 -0.1363 55   PHE C CB  
9414  C  CG  . PHE C 55   ? 1.1940 1.7242 1.4289 0.2155  -0.0286 -0.1374 55   PHE C CG  
9415  C  CD1 . PHE C 55   ? 1.1119 1.6331 1.3463 0.2108  -0.0235 -0.1344 55   PHE C CD1 
9416  C  CD2 . PHE C 55   ? 1.1448 1.6943 1.3924 0.2095  -0.0286 -0.1414 55   PHE C CD2 
9417  C  CE1 . PHE C 55   ? 1.1136 1.6444 1.3594 0.2006  -0.0182 -0.1353 55   PHE C CE1 
9418  C  CE2 . PHE C 55   ? 1.2110 1.7700 1.4704 0.1988  -0.0233 -0.1423 55   PHE C CE2 
9419  C  CZ  . PHE C 55   ? 1.1822 1.7317 1.4405 0.1944  -0.0179 -0.1392 55   PHE C CZ  
9420  N  N   . PHE C 56   ? 1.0287 1.5358 1.2402 0.2309  -0.0460 -0.1369 56   PHE C N   
9421  C  CA  . PHE C 56   ? 1.0281 1.5388 1.2422 0.2280  -0.0498 -0.1386 56   PHE C CA  
9422  C  C   . PHE C 56   ? 1.0489 1.5405 1.2556 0.2262  -0.0505 -0.1349 56   PHE C C   
9423  O  O   . PHE C 56   ? 0.9988 1.4928 1.2116 0.2187  -0.0502 -0.1354 56   PHE C O   
9424  C  CB  . PHE C 56   ? 0.9572 1.4726 1.1660 0.2368  -0.0557 -0.1411 56   PHE C CB  
9425  C  CG  . PHE C 56   ? 0.9621 1.4781 1.1707 0.2356  -0.0603 -0.1426 56   PHE C CG  
9426  C  CD1 . PHE C 56   ? 1.0146 1.5467 1.2361 0.2269  -0.0600 -0.1462 56   PHE C CD1 
9427  C  CD2 . PHE C 56   ? 0.9738 1.4739 1.1689 0.2431  -0.0646 -0.1405 56   PHE C CD2 
9428  C  CE1 . PHE C 56   ? 1.0252 1.5578 1.2461 0.2260  -0.0643 -0.1478 56   PHE C CE1 
9429  C  CE2 . PHE C 56   ? 1.0145 1.5149 1.2088 0.2424  -0.0687 -0.1418 56   PHE C CE2 
9430  C  CZ  . PHE C 56   ? 1.0378 1.5546 1.2450 0.2339  -0.0688 -0.1455 56   PHE C CZ  
9431  N  N   . MET C 57   ? 1.0612 1.5337 1.2547 0.2332  -0.0513 -0.1312 57   MET C N   
9432  C  CA  . MET C 57   ? 0.9766 1.4305 1.1631 0.2317  -0.0515 -0.1275 57   MET C CA  
9433  C  C   . MET C 57   ? 0.9683 1.4203 1.1616 0.2226  -0.0461 -0.1257 57   MET C C   
9434  O  O   . MET C 57   ? 0.9957 1.4385 1.1883 0.2181  -0.0458 -0.1237 57   MET C O   
9435  C  CB  . MET C 57   ? 1.0103 1.4445 1.1815 0.2410  -0.0532 -0.1242 57   MET C CB  
9436  C  CG  . MET C 57   ? 1.0261 1.4606 1.1890 0.2509  -0.0581 -0.1256 57   MET C CG  
9437  S  SD  . MET C 57   ? 1.1552 1.5628 1.2993 0.2599  -0.0608 -0.1214 57   MET C SD  
9438  C  CE  . MET C 57   ? 1.1810 1.5822 1.3184 0.2660  -0.0583 -0.1202 57   MET C CE  
9439  N  N   . LEU C 58   ? 0.8079 1.2683 1.0073 0.2200  -0.0417 -0.1264 58   LEU C N   
9440  C  CA  . LEU C 58   ? 0.7635 1.2234 0.9694 0.2114  -0.0363 -0.1250 58   LEU C CA  
9441  C  C   . LEU C 58   ? 0.7726 1.2460 0.9907 0.2017  -0.0351 -0.1275 58   LEU C C   
9442  O  O   . LEU C 58   ? 0.7758 1.2441 0.9967 0.1949  -0.0325 -0.1259 58   LEU C O   
9443  C  CB  . LEU C 58   ? 0.8154 1.2812 1.0241 0.2117  -0.0318 -0.1253 58   LEU C CB  
9444  C  CG  . LEU C 58   ? 0.6982 1.1640 0.9130 0.2035  -0.0257 -0.1239 58   LEU C CG  
9445  C  CD1 . LEU C 58   ? 0.6171 1.0627 0.8235 0.2034  -0.0254 -0.1200 58   LEU C CD1 
9446  C  CD2 . LEU C 58   ? 0.5779 1.0508 0.7952 0.2046  -0.0214 -0.1245 58   LEU C CD2 
9447  N  N   . MET C 59   ? 1.0711 1.5620 1.2968 0.2011  -0.0370 -0.1316 59   MET C N   
9448  C  CA  . MET C 59   ? 1.0762 1.5795 1.3129 0.1921  -0.0365 -0.1343 59   MET C CA  
9449  C  C   . MET C 59   ? 1.0218 1.5151 1.2538 0.1918  -0.0405 -0.1333 59   MET C C   
9450  O  O   . MET C 59   ? 0.9792 1.4748 1.2176 0.1835  -0.0389 -0.1337 59   MET C O   
9451  C  CB  . MET C 59   ? 0.9876 1.5117 1.2331 0.1920  -0.0382 -0.1393 59   MET C CB  
9452  C  CG  . MET C 59   ? 1.0898 1.6247 1.3399 0.1933  -0.0346 -0.1405 59   MET C CG  
9453  S  SD  . MET C 59   ? 1.4156 1.9478 1.6705 0.1856  -0.0262 -0.1380 59   MET C SD  
9454  C  CE  . MET C 59   ? 1.2534 1.8093 1.5260 0.1746  -0.0223 -0.1427 59   MET C CE  
9455  N  N   . ILE C 60   ? 0.6935 1.1753 0.9138 0.2009  -0.0454 -0.1318 60   ILE C N   
9456  C  CA  . ILE C 60   ? 0.5970 1.0665 0.8110 0.2015  -0.0487 -0.1301 60   ILE C CA  
9457  C  C   . ILE C 60   ? 0.5883 1.0429 0.7999 0.1973  -0.0452 -0.1260 60   ILE C C   
9458  O  O   . ILE C 60   ? 0.5709 1.0217 0.7842 0.1922  -0.0453 -0.1254 60   ILE C O   
9459  C  CB  . ILE C 60   ? 0.6804 1.1392 0.8813 0.2127  -0.0539 -0.1290 60   ILE C CB  
9460  C  CG1 . ILE C 60   ? 0.7275 1.2019 0.9312 0.2166  -0.0581 -0.1335 60   ILE C CG1 
9461  C  CG2 . ILE C 60   ? 0.5543 0.9969 0.7470 0.2140  -0.0564 -0.1262 60   ILE C CG2 
9462  C  CD1 . ILE C 60   ? 0.7613 1.2258 0.9517 0.2277  -0.0632 -0.1327 60   ILE C CD1 
9463  N  N   . PHE C 61   ? 0.8320 1.2781 1.0394 0.1994  -0.0419 -0.1234 61   PHE C N   
9464  C  CA  . PHE C 61   ? 0.7989 1.2318 1.0044 0.1954  -0.0384 -0.1198 61   PHE C CA  
9465  C  C   . PHE C 61   ? 0.8240 1.2670 1.0413 0.1846  -0.0340 -0.1211 61   PHE C C   
9466  O  O   . PHE C 61   ? 0.7793 1.2146 0.9969 0.1798  -0.0327 -0.1192 61   PHE C O   
9467  C  CB  . PHE C 61   ? 0.8354 1.2593 1.0347 0.1998  -0.0360 -0.1175 61   PHE C CB  
9468  C  CG  . PHE C 61   ? 0.8640 1.2759 1.0618 0.1958  -0.0322 -0.1143 61   PHE C CG  
9469  C  CD1 . PHE C 61   ? 0.7841 1.1786 0.9741 0.1974  -0.0339 -0.1112 61   PHE C CD1 
9470  C  CD2 . PHE C 61   ? 0.8494 1.2673 1.0535 0.1906  -0.0269 -0.1145 61   PHE C CD2 
9471  C  CE1 . PHE C 61   ? 0.8250 1.2089 1.0139 0.1939  -0.0306 -0.1085 61   PHE C CE1 
9472  C  CE2 . PHE C 61   ? 0.7666 1.1736 0.9689 0.1874  -0.0237 -0.1117 61   PHE C CE2 
9473  C  CZ  . PHE C 61   ? 0.8049 1.1952 0.9998 0.1890  -0.0257 -0.1088 61   PHE C CZ  
9474  N  N   . PHE C 62   ? 0.9749 1.4352 1.2020 0.1806  -0.0312 -0.1242 62   PHE C N   
9475  C  CA  . PHE C 62   ? 0.9374 1.4073 1.1755 0.1701  -0.0263 -0.1254 62   PHE C CA  
9476  C  C   . PHE C 62   ? 0.8822 1.3570 1.1254 0.1644  -0.0284 -0.1274 62   PHE C C   
9477  O  O   . PHE C 62   ? 0.8714 1.3441 1.1187 0.1569  -0.0253 -0.1266 62   PHE C O   
9478  C  CB  . PHE C 62   ? 1.0326 1.5201 1.2799 0.1673  -0.0229 -0.1285 62   PHE C CB  
9479  C  CG  . PHE C 62   ? 1.0447 1.5282 1.2893 0.1695  -0.0186 -0.1264 62   PHE C CG  
9480  C  CD1 . PHE C 62   ? 1.0348 1.5027 1.2731 0.1694  -0.0161 -0.1226 62   PHE C CD1 
9481  C  CD2 . PHE C 62   ? 1.0456 1.5409 1.2937 0.1719  -0.0170 -0.1285 62   PHE C CD2 
9482  C  CE1 . PHE C 62   ? 1.0008 1.4649 1.2361 0.1717  -0.0124 -0.1210 62   PHE C CE1 
9483  C  CE2 . PHE C 62   ? 1.0358 1.5273 1.2810 0.1742  -0.0130 -0.1267 62   PHE C CE2 
9484  C  CZ  . PHE C 62   ? 0.9637 1.4395 1.2023 0.1742  -0.0108 -0.1230 62   PHE C CZ  
9485  N  N   . VAL C 63   ? 0.6091 1.0901 0.8517 0.1682  -0.0338 -0.1300 63   VAL C N   
9486  C  CA  . VAL C 63   ? 0.6619 1.1472 0.9086 0.1637  -0.0364 -0.1321 63   VAL C CA  
9487  C  C   . VAL C 63   ? 0.6001 1.0676 0.8387 0.1649  -0.0379 -0.1285 63   VAL C C   
9488  O  O   . VAL C 63   ? 0.6348 1.0982 0.8750 0.1567  -0.0366 -0.1279 63   VAL C O   
9489  C  CB  . VAL C 63   ? 0.6097 1.1053 0.8564 0.1687  -0.0422 -0.1358 63   VAL C CB  
9490  C  CG1 . VAL C 63   ? 0.3380 0.8356 0.5866 0.1654  -0.0458 -0.1378 63   VAL C CG1 
9491  C  CG2 . VAL C 63   ? 0.6981 1.2134 0.9550 0.1659  -0.0404 -0.1399 63   VAL C CG2 
9492  N  N   . SER C 64   ? 0.6861 1.1379 0.9130 0.1734  -0.0400 -0.1250 64   SER C N   
9493  C  CA  . SER C 64   ? 0.7172 1.1486 0.9342 0.1739  -0.0411 -0.1208 64   SER C CA  
9494  C  C   . SER C 64   ? 0.7397 1.1581 0.9555 0.1645  -0.0354 -0.1168 64   SER C C   
9495  O  O   . SER C 64   ? 0.6959 1.1029 0.9085 0.1581  -0.0348 -0.1144 64   SER C O   
9496  C  CB  . SER C 64   ? 0.7704 1.1891 0.9761 0.1853  -0.0442 -0.1184 64   SER C CB  
9497  O  OG  . SER C 64   ? 0.8338 1.2588 1.0364 0.1921  -0.0486 -0.1207 64   SER C OG  
9498  N  N   . VAL C 65   ? 0.7889 1.2087 1.0068 0.1639  -0.0313 -0.1160 65   VAL C N   
9499  C  CA  . VAL C 65   ? 0.6988 1.1064 0.9148 0.1559  -0.0261 -0.1123 65   VAL C CA  
9500  C  C   . VAL C 65   ? 0.6636 1.0789 0.8880 0.1446  -0.0226 -0.1137 65   VAL C C   
9501  O  O   . VAL C 65   ? 0.6588 1.0612 0.8798 0.1374  -0.0202 -0.1105 65   VAL C O   
9502  C  CB  . VAL C 65   ? 0.6492 1.0574 0.8652 0.1587  -0.0227 -0.1115 65   VAL C CB  
9503  C  CG1 . VAL C 65   ? 0.5809 0.9806 0.7968 0.1498  -0.0169 -0.1085 65   VAL C CG1 
9504  C  CG2 . VAL C 65   ? 0.6160 1.0110 0.8215 0.1686  -0.0256 -0.1092 65   VAL C CG2 
9505  N  N   . THR C 66   ? 0.7411 1.1774 0.9763 0.1428  -0.0224 -0.1186 66   THR C N   
9506  C  CA  . THR C 66   ? 0.7967 1.2409 1.0401 0.1316  -0.0189 -0.1204 66   THR C CA  
9507  C  C   . THR C 66   ? 0.8099 1.2458 1.0499 0.1275  -0.0216 -0.1198 66   THR C C   
9508  O  O   . THR C 66   ? 0.8014 1.2289 1.0408 0.1186  -0.0181 -0.1178 66   THR C O   
9509  C  CB  . THR C 66   ? 0.8316 1.3011 1.0879 0.1311  -0.0187 -0.1263 66   THR C CB  
9510  O  OG1 . THR C 66   ? 0.8905 1.3672 1.1497 0.1346  -0.0155 -0.1267 66   THR C OG1 
9511  C  CG2 . THR C 66   ? 0.6948 1.1718 0.9595 0.1189  -0.0149 -0.1285 66   THR C CG2 
9512  N  N   . TRP C 67   ? 0.7804 1.2179 1.0174 0.1345  -0.0277 -0.1214 67   TRP C N   
9513  C  CA  . TRP C 67   ? 0.7317 1.1608 0.9645 0.1314  -0.0305 -0.1208 67   TRP C CA  
9514  C  C   . TRP C 67   ? 0.7595 1.1643 0.9810 0.1306  -0.0293 -0.1148 67   TRP C C   
9515  O  O   . TRP C 67   ? 0.8333 1.2293 1.0525 0.1241  -0.0285 -0.1133 67   TRP C O   
9516  C  CB  . TRP C 67   ? 0.8299 1.2661 1.0611 0.1401  -0.0374 -0.1238 67   TRP C CB  
9517  C  CG  . TRP C 67   ? 0.8346 1.2640 1.0619 0.1372  -0.0403 -0.1238 67   TRP C CG  
9518  C  CD1 . TRP C 67   ? 0.8066 1.2221 1.0231 0.1434  -0.0444 -0.1214 67   TRP C CD1 
9519  C  CD2 . TRP C 67   ? 0.9007 1.3361 1.1340 0.1274  -0.0392 -0.1264 67   TRP C CD2 
9520  N  NE1 . TRP C 67   ? 0.8603 1.2732 1.0757 0.1384  -0.0460 -0.1223 67   TRP C NE1 
9521  C  CE2 . TRP C 67   ? 0.9334 1.3583 1.1590 0.1285  -0.0430 -0.1255 67   TRP C CE2 
9522  C  CE3 . TRP C 67   ? 0.7617 1.2099 1.0059 0.1176  -0.0351 -0.1295 67   TRP C CE3 
9523  C  CZ2 . TRP C 67   ? 0.8051 1.2318 1.0333 0.1204  -0.0431 -0.1276 67   TRP C CZ2 
9524  C  CZ3 . TRP C 67   ? 0.7805 1.2302 1.0274 0.1093  -0.0351 -0.1316 67   TRP C CZ3 
9525  C  CH2 . TRP C 67   ? 0.7122 1.1512 0.9511 0.1108  -0.0392 -0.1307 67   TRP C CH2 
9526  N  N   . LEU C 68   ? 0.5781 0.9722 0.7927 0.1370  -0.0292 -0.1115 68   LEU C N   
9527  C  CA  . LEU C 68   ? 0.5535 0.9256 0.7584 0.1359  -0.0278 -0.1060 68   LEU C CA  
9528  C  C   . LEU C 68   ? 0.5557 0.9224 0.7627 0.1260  -0.0220 -0.1037 68   LEU C C   
9529  O  O   . LEU C 68   ? 0.5475 0.8996 0.7492 0.1216  -0.0208 -0.1004 68   LEU C O   
9530  C  CB  . LEU C 68   ? 0.5774 0.9403 0.7752 0.1446  -0.0288 -0.1035 68   LEU C CB  
9531  C  CG  . LEU C 68   ? 0.5567 0.8989 0.7463 0.1429  -0.0265 -0.0981 68   LEU C CG  
9532  C  CD1 . LEU C 68   ? 0.5093 0.8368 0.6911 0.1435  -0.0290 -0.0955 68   LEU C CD1 
9533  C  CD2 . LEU C 68   ? 0.5944 0.9315 0.7796 0.1501  -0.0266 -0.0968 68   LEU C CD2 
9534  N  N   . PHE C 69   ? 0.8376 1.2156 1.0520 0.1227  -0.0181 -0.1055 69   PHE C N   
9535  C  CA  . PHE C 69   ? 0.8520 1.2250 1.0678 0.1136  -0.0123 -0.1035 69   PHE C CA  
9536  C  C   . PHE C 69   ? 0.7556 1.1323 0.9758 0.1047  -0.0110 -0.1051 69   PHE C C   
9537  O  O   . PHE C 69   ? 0.7025 1.0676 0.9196 0.0980  -0.0078 -0.1022 69   PHE C O   
9538  C  CB  . PHE C 69   ? 0.8526 1.2366 1.0744 0.1129  -0.0082 -0.1049 69   PHE C CB  
9539  C  CG  . PHE C 69   ? 0.8744 1.2496 1.0902 0.1192  -0.0077 -0.1021 69   PHE C CG  
9540  C  CD1 . PHE C 69   ? 0.9325 1.2899 1.1387 0.1231  -0.0099 -0.0982 69   PHE C CD1 
9541  C  CD2 . PHE C 69   ? 0.9231 1.3081 1.1431 0.1211  -0.0049 -0.1035 69   PHE C CD2 
9542  C  CE1 . PHE C 69   ? 0.8985 1.2478 1.0993 0.1284  -0.0096 -0.0959 69   PHE C CE1 
9543  C  CE2 . PHE C 69   ? 0.9397 1.3163 1.1536 0.1269  -0.0045 -0.1012 69   PHE C CE2 
9544  C  CZ  . PHE C 69   ? 0.8755 1.2342 1.0799 0.1305  -0.0071 -0.0975 69   PHE C CZ  
9545  N  N   . ILE C 70   ? 0.5012 0.8939 0.7284 0.1046  -0.0137 -0.1100 70   ILE C N   
9546  C  CA  . ILE C 70   ? 0.5101 0.9075 0.7421 0.0958  -0.0126 -0.1124 70   ILE C CA  
9547  C  C   . ILE C 70   ? 0.5948 0.9771 0.8187 0.0950  -0.0152 -0.1099 70   ILE C C   
9548  O  O   . ILE C 70   ? 0.5638 0.9373 0.7860 0.0872  -0.0121 -0.1081 70   ILE C O   
9549  C  CB  . ILE C 70   ? 0.4723 0.8919 0.7144 0.0962  -0.0152 -0.1187 70   ILE C CB  
9550  C  CG1 . ILE C 70   ? 0.4233 0.8583 0.6749 0.0942  -0.0110 -0.1212 70   ILE C CG1 
9551  C  CG2 . ILE C 70   ? 0.4263 0.8491 0.6718 0.0883  -0.0157 -0.1215 70   ILE C CG2 
9552  C  CD1 . ILE C 70   ? 0.4327 0.8913 0.6953 0.0953  -0.0136 -0.1277 70   ILE C CD1 
9553  N  N   . ARG C 71   ? 0.6835 1.0623 0.9020 0.1034  -0.0207 -0.1096 71   ARG C N   
9554  C  CA  . ARG C 71   ? 0.6217 0.9875 0.8326 0.1034  -0.0234 -0.1077 71   ARG C CA  
9555  C  C   . ARG C 71   ? 0.6311 0.9758 0.8322 0.1049  -0.0219 -0.1016 71   ARG C C   
9556  O  O   . ARG C 71   ? 0.6078 0.9406 0.8051 0.0992  -0.0196 -0.0988 71   ARG C O   
9557  C  CB  . ARG C 71   ? 0.6506 1.0225 0.8597 0.1115  -0.0299 -0.1104 71   ARG C CB  
9558  C  CG  . ARG C 71   ? 0.7679 1.1280 0.9694 0.1115  -0.0327 -0.1090 71   ARG C CG  
9559  C  CD  . ARG C 71   ? 0.8340 1.2003 1.0403 0.1028  -0.0321 -0.1122 71   ARG C CD  
9560  N  NE  . ARG C 71   ? 0.9162 1.2693 1.1143 0.1024  -0.0340 -0.1103 71   ARG C NE  
9561  C  CZ  . ARG C 71   ? 1.0184 1.3733 1.2127 0.1083  -0.0395 -0.1123 71   ARG C CZ  
9562  N  NH1 . ARG C 71   ? 1.0501 1.4195 1.2480 0.1152  -0.0440 -0.1163 71   ARG C NH1 
9563  N  NH2 . ARG C 71   ? 1.1164 1.4580 1.3026 0.1075  -0.0406 -0.1102 71   ARG C NH2 
9564  N  N   . GLY C 72   ? 0.5647 0.9050 0.7618 0.1127  -0.0231 -0.0996 72   GLY C N   
9565  C  CA  . GLY C 72   ? 0.5766 0.8980 0.7651 0.1143  -0.0220 -0.0944 72   GLY C CA  
9566  C  C   . GLY C 72   ? 0.5098 0.8243 0.6913 0.1241  -0.0261 -0.0930 72   GLY C C   
9567  O  O   . GLY C 72   ? 0.6216 0.9454 0.8039 0.1301  -0.0302 -0.0961 72   GLY C O   
9568  N  N   . VAL C 73   ? 0.5301 0.8281 0.7044 0.1257  -0.0251 -0.0886 73   VAL C N   
9569  C  CA  . VAL C 73   ? 0.6019 0.8911 0.7688 0.1345  -0.0283 -0.0869 73   VAL C CA  
9570  C  C   . VAL C 73   ? 0.7034 0.9866 0.8646 0.1369  -0.0316 -0.0866 73   VAL C C   
9571  O  O   . VAL C 73   ? 0.7792 1.0545 0.9334 0.1443  -0.0343 -0.0853 73   VAL C O   
9572  C  CB  . VAL C 73   ? 0.6018 0.8753 0.7633 0.1347  -0.0260 -0.0825 73   VAL C CB  
9573  C  CG1 . VAL C 73   ? 0.6389 0.9183 0.8046 0.1341  -0.0235 -0.0831 73   VAL C CG1 
9574  C  CG2 . VAL C 73   ? 0.6086 0.8701 0.7678 0.1277  -0.0233 -0.0792 73   VAL C CG2 
9575  N  N   . GLY C 74   ? 1.0512 1.3373 1.2149 0.1308  -0.0312 -0.0877 74   GLY C N   
9576  C  CA  . GLY C 74   ? 1.1121 1.3940 1.2705 0.1331  -0.0344 -0.0880 74   GLY C CA  
9577  C  C   . GLY C 74   ? 1.0440 1.3384 1.2033 0.1401  -0.0393 -0.0922 74   GLY C C   
9578  O  O   . GLY C 74   ? 0.9281 1.2181 1.0815 0.1438  -0.0425 -0.0923 74   GLY C O   
9579  N  N   . ILE C 75   ? 0.8984 1.2083 1.0647 0.1423  -0.0400 -0.0957 75   ILE C N   
9580  C  CA  . ILE C 75   ? 0.9240 1.2469 1.0916 0.1499  -0.0448 -0.0998 75   ILE C CA  
9581  C  C   . ILE C 75   ? 0.9238 1.2368 1.0819 0.1605  -0.0477 -0.0978 75   ILE C C   
9582  O  O   . ILE C 75   ? 0.9794 1.2985 1.1350 0.1681  -0.0522 -0.1003 75   ILE C O   
9583  C  CB  . ILE C 75   ? 0.9748 1.3179 1.1533 0.1492  -0.0443 -0.1042 75   ILE C CB  
9584  C  CG1 . ILE C 75   ? 0.8125 1.1526 0.9908 0.1519  -0.0417 -0.1021 75   ILE C CG1 
9585  C  CG2 . ILE C 75   ? 0.9163 1.2687 1.1039 0.1383  -0.0411 -0.1063 75   ILE C CG2 
9586  C  CD1 . ILE C 75   ? 0.7465 1.1059 0.9346 0.1525  -0.0410 -0.1062 75   ILE C CD1 
9587  N  N   . TRP C 76   ? 0.9112 1.2089 1.0637 0.1613  -0.0451 -0.0933 76   TRP C N   
9588  C  CA  . TRP C 76   ? 1.0976 1.3834 1.2404 0.1705  -0.0471 -0.0910 76   TRP C CA  
9589  C  C   . TRP C 76   ? 1.0458 1.3169 1.1792 0.1717  -0.0484 -0.0883 76   TRP C C   
9590  O  O   . TRP C 76   ? 1.0691 1.3412 1.2037 0.1665  -0.0484 -0.0889 76   TRP C O   
9591  C  CB  . TRP C 76   ? 1.1045 1.3802 1.2455 0.1703  -0.0439 -0.0878 76   TRP C CB  
9592  C  CG  . TRP C 76   ? 1.0720 1.3611 1.2209 0.1700  -0.0426 -0.0903 76   TRP C CG  
9593  C  CD1 . TRP C 76   ? 0.9969 1.3049 1.1525 0.1731  -0.0446 -0.0949 76   TRP C CD1 
9594  C  CD2 . TRP C 76   ? 0.9565 1.2414 1.1072 0.1666  -0.0388 -0.0884 76   TRP C CD2 
9595  N  NE1 . TRP C 76   ? 0.9495 1.2650 1.1110 0.1718  -0.0420 -0.0958 76   TRP C NE1 
9596  C  CE2 . TRP C 76   ? 0.9483 1.2495 1.1065 0.1680  -0.0385 -0.0918 76   TRP C CE2 
9597  C  CE3 . TRP C 76   ? 0.9198 1.1891 1.0667 0.1628  -0.0358 -0.0843 76   TRP C CE3 
9598  C  CZ2 . TRP C 76   ? 0.9262 1.2277 1.0872 0.1657  -0.0351 -0.0911 76   TRP C CZ2 
9599  C  CZ3 . TRP C 76   ? 0.8763 1.1463 1.0263 0.1606  -0.0329 -0.0837 76   TRP C CZ3 
9600  C  CH2 . TRP C 76   ? 0.8504 1.1360 1.0070 0.1622  -0.0325 -0.0871 76   TRP C CH2 
9601  N  N   . GLY C 77   ? 0.7268 0.9835 0.8503 0.1787  -0.0492 -0.0854 77   GLY C N   
9602  C  CA  . GLY C 77   ? 0.7172 0.9591 0.8310 0.1806  -0.0500 -0.0826 77   GLY C CA  
9603  C  C   . GLY C 77   ? 0.7652 0.9886 0.8746 0.1760  -0.0460 -0.0775 77   GLY C C   
9604  O  O   . GLY C 77   ? 0.7941 1.0028 0.8945 0.1785  -0.0460 -0.0745 77   GLY C O   
9605  N  N   . ILE C 78   ? 0.9187 1.1429 1.0344 0.1695  -0.0425 -0.0765 78   ILE C N   
9606  C  CA  . ILE C 78   ? 0.9022 1.1103 1.0148 0.1651  -0.0389 -0.0720 78   ILE C CA  
9607  C  C   . ILE C 78   ? 0.8622 1.0649 0.9743 0.1586  -0.0372 -0.0703 78   ILE C C   
9608  O  O   . ILE C 78   ? 0.8199 1.0332 0.9375 0.1540  -0.0375 -0.0727 78   ILE C O   
9609  C  CB  . ILE C 78   ? 0.8010 1.0124 0.9202 0.1607  -0.0360 -0.0718 78   ILE C CB  
9610  C  CG1 . ILE C 78   ? 0.8578 1.0852 0.9869 0.1543  -0.0351 -0.0748 78   ILE C CG1 
9611  C  CG2 . ILE C 78   ? 0.8428 1.0556 0.9604 0.1677  -0.0374 -0.0728 78   ILE C CG2 
9612  C  CD1 . ILE C 78   ? 0.8357 1.0669 0.9707 0.1504  -0.0322 -0.0748 78   ILE C CD1 
9613  N  N   . ASN C 79   ? 0.9729 1.1589 1.0784 0.1582  -0.0353 -0.0662 79   ASN C N   
9614  C  CA  . ASN C 79   ? 0.9292 1.1082 1.0331 0.1527  -0.0334 -0.0641 79   ASN C CA  
9615  C  C   . ASN C 79   ? 0.8865 1.0534 0.9906 0.1478  -0.0294 -0.0600 79   ASN C C   
9616  O  O   . ASN C 79   ? 0.8194 0.9869 0.9272 0.1465  -0.0281 -0.0597 79   ASN C O   
9617  C  CB  . ASN C 79   ? 0.8985 1.0695 0.9931 0.1582  -0.0355 -0.0632 79   ASN C CB  
9618  C  CG  . ASN C 79   ? 0.9073 1.0667 0.9935 0.1658  -0.0362 -0.0612 79   ASN C CG  
9619  O  OD1 . ASN C 79   ? 0.9821 1.1384 1.0694 0.1667  -0.0350 -0.0603 79   ASN C OD1 
9620  N  ND2 . ASN C 79   ? 0.9740 1.1262 1.0511 0.1716  -0.0379 -0.0605 79   ASN C ND2 
9621  N  N   . ILE C 80   ? 1.0617 1.2174 1.1615 0.1451  -0.0275 -0.0571 80   ILE C N   
9622  C  CA  . ILE C 80   ? 1.0593 1.2044 1.1599 0.1401  -0.0237 -0.0534 80   ILE C CA  
9623  C  C   . ILE C 80   ? 1.2309 1.3637 1.3263 0.1444  -0.0231 -0.0509 80   ILE C C   
9624  O  O   . ILE C 80   ? 1.3332 1.4639 1.4320 0.1422  -0.0215 -0.0499 80   ILE C O   
9625  C  CB  . ILE C 80   ? 1.0794 1.2177 1.1778 0.1358  -0.0216 -0.0512 80   ILE C CB  
9626  C  CG1 . ILE C 80   ? 1.1610 1.3103 1.2654 0.1299  -0.0213 -0.0535 80   ILE C CG1 
9627  C  CG2 . ILE C 80   ? 1.0377 1.1638 1.1357 0.1323  -0.0179 -0.0471 80   ILE C CG2 
9628  C  CD1 . ILE C 80   ? 0.9688 1.1259 1.0813 0.1253  -0.0197 -0.0544 80   ILE C CD1 
9629  N  N   . PRO C 81   ? 0.8603 0.9844 0.9471 0.1506  -0.0244 -0.0499 81   PRO C N   
9630  C  CA  . PRO C 81   ? 0.7745 0.8862 0.8563 0.1542  -0.0234 -0.0476 81   PRO C CA  
9631  C  C   . PRO C 81   ? 0.8483 0.9656 0.9317 0.1583  -0.0254 -0.0499 81   PRO C C   
9632  O  O   . PRO C 81   ? 0.9576 1.0703 1.0428 0.1569  -0.0239 -0.0489 81   PRO C O   
9633  C  CB  . PRO C 81   ? 0.6693 0.7711 0.7408 0.1601  -0.0242 -0.0462 81   PRO C CB  
9634  C  CG  . PRO C 81   ? 0.7913 0.9043 0.8628 0.1620  -0.0273 -0.0492 81   PRO C CG  
9635  C  CD  . PRO C 81   ? 0.7133 0.8371 0.7940 0.1543  -0.0264 -0.0505 81   PRO C CD  
9636  N  N   . VAL C 82   ? 0.6976 0.8252 0.7804 0.1636  -0.0288 -0.0531 82   VAL C N   
9637  C  CA  . VAL C 82   ? 0.7539 0.8887 0.8385 0.1680  -0.0307 -0.0556 82   VAL C CA  
9638  C  C   . VAL C 82   ? 0.6728 0.8233 0.7677 0.1631  -0.0307 -0.0583 82   VAL C C   
9639  O  O   . VAL C 82   ? 0.5527 0.7171 0.6510 0.1648  -0.0330 -0.0617 82   VAL C O   
9640  C  CB  . VAL C 82   ? 0.8180 0.9560 0.8964 0.1771  -0.0344 -0.0578 82   VAL C CB  
9641  C  CG1 . VAL C 82   ? 0.7527 0.8954 0.8318 0.1823  -0.0360 -0.0599 82   VAL C CG1 
9642  C  CG2 . VAL C 82   ? 0.7832 0.9054 0.8506 0.1817  -0.0342 -0.0550 82   VAL C CG2 
9643  N  N   . GLY C 83   ? 0.9464 1.0949 1.0462 0.1573  -0.0280 -0.0570 83   GLY C N   
9644  C  CA  . GLY C 83   ? 0.9416 1.1034 1.0501 0.1528  -0.0274 -0.0592 83   GLY C CA  
9645  C  C   . GLY C 83   ? 0.8931 1.0629 1.0036 0.1571  -0.0289 -0.0618 83   GLY C C   
9646  O  O   . GLY C 83   ? 0.9113 1.0935 1.0288 0.1542  -0.0284 -0.0640 83   GLY C O   
9647  N  N   . TRP C 84   ? 0.7704 0.9330 0.8745 0.1640  -0.0304 -0.0616 84   TRP C N   
9648  C  CA  . TRP C 84   ? 0.7753 0.9440 0.8800 0.1693  -0.0318 -0.0640 84   TRP C CA  
9649  C  C   . TRP C 84   ? 0.8136 0.9838 0.9124 0.1782  -0.0351 -0.0656 84   TRP C C   
9650  O  O   . TRP C 84   ? 0.8615 1.0183 0.9516 0.1826  -0.0356 -0.0636 84   TRP C O   
9651  C  CB  . TRP C 84   ? 0.7827 0.9399 0.8848 0.1694  -0.0305 -0.0623 84   TRP C CB  
9652  C  CG  . TRP C 84   ? 0.7468 0.9076 0.8556 0.1628  -0.0282 -0.0621 84   TRP C CG  
9653  C  CD1 . TRP C 84   ? 0.7523 0.9236 0.8683 0.1567  -0.0268 -0.0628 84   TRP C CD1 
9654  C  CD2 . TRP C 84   ? 0.7518 0.9053 0.8600 0.1619  -0.0271 -0.0613 84   TRP C CD2 
9655  N  NE1 . TRP C 84   ? 0.8092 0.9800 0.9288 0.1524  -0.0248 -0.0623 84   TRP C NE1 
9656  C  CE2 . TRP C 84   ? 0.7555 0.9158 0.8706 0.1555  -0.0251 -0.0614 84   TRP C CE2 
9657  C  CE3 . TRP C 84   ? 0.7707 0.9122 0.8729 0.1658  -0.0275 -0.0605 84   TRP C CE3 
9658  C  CZ2 . TRP C 84   ? 0.7499 0.9059 0.8659 0.1534  -0.0240 -0.0609 84   TRP C CZ2 
9659  C  CZ3 . TRP C 84   ? 0.6896 0.8270 0.7933 0.1632  -0.0264 -0.0603 84   TRP C CZ3 
9660  C  CH2 . TRP C 84   ? 0.7666 0.9115 0.8771 0.1572  -0.0248 -0.0605 84   TRP C CH2 
9661  N  N   . GLY C 85   ? 0.9661 1.1525 1.0693 0.1809  -0.0372 -0.0692 85   GLY C N   
9662  C  CA  . GLY C 85   ? 1.0213 1.2115 1.1196 0.1899  -0.0407 -0.0712 85   GLY C CA  
9663  C  C   . GLY C 85   ? 1.0068 1.2032 1.1052 0.1965  -0.0420 -0.0736 85   GLY C C   
9664  O  O   . GLY C 85   ? 1.0264 1.2147 1.1229 0.1967  -0.0405 -0.0724 85   GLY C O   
9665  N  N   . MET C 86   ? 0.8820 1.0931 0.9827 0.2020  -0.0449 -0.0772 86   MET C N   
9666  C  CA  . MET C 86   ? 0.8991 1.1176 1.0002 0.2088  -0.0462 -0.0796 86   MET C CA  
9667  C  C   . MET C 86   ? 0.8742 1.1020 0.9841 0.2034  -0.0437 -0.0808 86   MET C C   
9668  O  O   . MET C 86   ? 0.9537 1.1841 1.0631 0.2082  -0.0438 -0.0821 86   MET C O   
9669  C  CB  . MET C 86   ? 0.9471 1.1810 1.0496 0.2159  -0.0500 -0.0834 86   MET C CB  
9670  C  CG  . MET C 86   ? 0.9707 1.1955 1.0625 0.2242  -0.0530 -0.0826 86   MET C CG  
9671  S  SD  . MET C 86   ? 1.0727 1.3177 1.1679 0.2305  -0.0578 -0.0874 86   MET C SD  
9672  C  CE  . MET C 86   ? 0.8181 1.0861 0.9267 0.2287  -0.0571 -0.0916 86   MET C CE  
9673  N  N   . ASP C 87   ? 1.0468 1.2792 1.1641 0.1938  -0.0413 -0.0803 87   ASP C N   
9674  C  CA  . ASP C 87   ? 1.0209 1.2603 1.1455 0.1884  -0.0384 -0.0810 87   ASP C CA  
9675  C  C   . ASP C 87   ? 0.9873 1.2125 1.1071 0.1888  -0.0367 -0.0786 87   ASP C C   
9676  O  O   . ASP C 87   ? 0.9990 1.2292 1.1224 0.1876  -0.0351 -0.0795 87   ASP C O   
9677  C  CB  . ASP C 87   ? 0.9988 1.2425 1.1304 0.1782  -0.0359 -0.0804 87   ASP C CB  
9678  C  CG  . ASP C 87   ? 1.0715 1.2991 1.1984 0.1737  -0.0348 -0.0765 87   ASP C CG  
9679  O  OD1 . ASP C 87   ? 1.0344 1.2479 1.1529 0.1782  -0.0358 -0.0744 87   ASP C OD1 
9680  O  OD2 . ASP C 87   ? 1.0177 1.2465 1.1491 0.1657  -0.0326 -0.0756 87   ASP C OD2 
9681  N  N   . ILE C 88   ? 0.7283 0.9360 0.8398 0.1903  -0.0370 -0.0757 88   ILE C N   
9682  C  CA  . ILE C 88   ? 0.7496 0.9433 0.8560 0.1911  -0.0359 -0.0738 88   ILE C CA  
9683  C  C   . ILE C 88   ? 0.7886 0.9753 0.8863 0.2010  -0.0381 -0.0744 88   ILE C C   
9684  O  O   . ILE C 88   ? 0.7912 0.9731 0.8864 0.2036  -0.0376 -0.0747 88   ILE C O   
9685  C  CB  . ILE C 88   ? 0.7508 0.9290 0.8545 0.1850  -0.0340 -0.0701 88   ILE C CB  
9686  C  CG1 . ILE C 88   ? 0.7300 0.9145 0.8416 0.1756  -0.0317 -0.0694 88   ILE C CG1 
9687  C  CG2 . ILE C 88   ? 0.6458 0.8105 0.7449 0.1856  -0.0331 -0.0687 88   ILE C CG2 
9688  C  CD1 . ILE C 88   ? 0.6896 0.8799 0.8066 0.1720  -0.0297 -0.0703 88   ILE C CD1 
9689  N  N   . ILE C 89   ? 0.7721 0.9588 0.8650 0.2071  -0.0405 -0.0749 89   ILE C N   
9690  C  CA  . ILE C 89   ? 0.8231 1.0025 0.9067 0.2172  -0.0426 -0.0754 89   ILE C CA  
9691  C  C   . ILE C 89   ? 0.8347 1.0267 0.9211 0.2228  -0.0436 -0.0787 89   ILE C C   
9692  O  O   . ILE C 89   ? 0.9759 1.1599 1.0568 0.2275  -0.0435 -0.0788 89   ILE C O   
9693  C  CB  . ILE C 89   ? 0.7910 0.9694 0.8690 0.2228  -0.0452 -0.0753 89   ILE C CB  
9694  C  CG1 . ILE C 89   ? 0.7827 0.9466 0.8567 0.2178  -0.0437 -0.0717 89   ILE C CG1 
9695  C  CG2 . ILE C 89   ? 0.7017 0.8737 0.7694 0.2346  -0.0475 -0.0761 89   ILE C CG2 
9696  C  CD1 . ILE C 89   ? 0.7339 0.8982 0.8034 0.2216  -0.0459 -0.0716 89   ILE C CD1 
9697  N  N   . ASN C 90   ? 0.9662 1.1782 1.0612 0.2224  -0.0444 -0.0816 90   ASN C N   
9698  C  CA  . ASN C 90   ? 0.9645 1.1906 1.0636 0.2272  -0.0449 -0.0850 90   ASN C CA  
9699  C  C   . ASN C 90   ? 1.0406 1.2650 1.1426 0.2228  -0.0420 -0.0846 90   ASN C C   
9700  O  O   . ASN C 90   ? 1.0709 1.2986 1.1717 0.2283  -0.0421 -0.0864 90   ASN C O   
9701  C  CB  . ASN C 90   ? 1.1250 1.3734 1.2344 0.2256  -0.0458 -0.0882 90   ASN C CB  
9702  C  CG  . ASN C 90   ? 1.1259 1.3767 1.2329 0.2290  -0.0490 -0.0887 90   ASN C CG  
9703  O  OD1 . ASN C 90   ? 0.9463 1.1829 1.0430 0.2346  -0.0506 -0.0869 90   ASN C OD1 
9704  N  ND2 . ASN C 90   ? 1.0788 1.3475 1.1949 0.2259  -0.0498 -0.0914 90   ASN C ND2 
9705  N  N   . PHE C 91   ? 0.9039 1.1229 1.0094 0.2133  -0.0395 -0.0824 91   PHE C N   
9706  C  CA  . PHE C 91   ? 0.8499 1.0660 0.9572 0.2093  -0.0370 -0.0820 91   PHE C CA  
9707  C  C   . PHE C 91   ? 0.8373 1.0361 0.9349 0.2140  -0.0374 -0.0808 91   PHE C C   
9708  O  O   . PHE C 91   ? 0.9858 1.1856 1.0823 0.2172  -0.0370 -0.0821 91   PHE C O   
9709  C  CB  . PHE C 91   ? 0.8217 1.0351 0.9339 0.1987  -0.0345 -0.0797 91   PHE C CB  
9710  C  CG  . PHE C 91   ? 0.8256 1.0308 0.9371 0.1948  -0.0324 -0.0785 91   PHE C CG  
9711  C  CD1 . PHE C 91   ? 0.8415 1.0561 0.9571 0.1946  -0.0309 -0.0803 91   PHE C CD1 
9712  C  CD2 . PHE C 91   ? 0.7901 0.9784 0.8969 0.1916  -0.0319 -0.0757 91   PHE C CD2 
9713  C  CE1 . PHE C 91   ? 0.8831 1.0900 0.9974 0.1915  -0.0292 -0.0794 91   PHE C CE1 
9714  C  CE2 . PHE C 91   ? 0.8273 1.0087 0.9336 0.1882  -0.0304 -0.0749 91   PHE C CE2 
9715  C  CZ  . PHE C 91   ? 0.8532 1.0437 0.9630 0.1883  -0.0293 -0.0768 91   PHE C CZ  
9716  N  N   . VAL C 92   ? 0.6437 0.8263 0.7341 0.2143  -0.0381 -0.0782 92   VAL C N   
9717  C  CA  . VAL C 92   ? 0.6815 0.8465 0.7625 0.2182  -0.0383 -0.0772 92   VAL C CA  
9718  C  C   . VAL C 92   ? 0.7612 0.9274 0.8358 0.2292  -0.0404 -0.0793 92   VAL C C   
9719  O  O   . VAL C 92   ? 0.7642 0.9223 0.8332 0.2332  -0.0403 -0.0799 92   VAL C O   
9720  C  CB  . VAL C 92   ? 0.6800 0.8277 0.7550 0.2157  -0.0380 -0.0740 92   VAL C CB  
9721  C  CG1 . VAL C 92   ? 0.7146 0.8437 0.7799 0.2194  -0.0380 -0.0730 92   VAL C CG1 
9722  C  CG2 . VAL C 92   ? 0.8137 0.9607 0.8952 0.2052  -0.0359 -0.0719 92   VAL C CG2 
9723  N  N   . TRP C 93   ? 0.9620 1.1383 1.0370 0.2346  -0.0424 -0.0807 93   TRP C N   
9724  C  CA  . TRP C 93   ? 0.9893 1.1683 1.0586 0.2458  -0.0445 -0.0828 93   TRP C CA  
9725  C  C   . TRP C 93   ? 1.0018 1.1935 1.0759 0.2480  -0.0439 -0.0857 93   TRP C C   
9726  O  O   . TRP C 93   ? 1.0577 1.2430 1.1250 0.2549  -0.0443 -0.0866 93   TRP C O   
9727  C  CB  . TRP C 93   ? 0.9802 1.1700 1.0503 0.2506  -0.0470 -0.0840 93   TRP C CB  
9728  C  CG  . TRP C 93   ? 1.0940 1.2821 1.1553 0.2621  -0.0495 -0.0854 93   TRP C CG  
9729  C  CD1 . TRP C 93   ? 1.1042 1.2736 1.1525 0.2685  -0.0503 -0.0836 93   TRP C CD1 
9730  C  CD2 . TRP C 93   ? 1.0595 1.2628 1.1226 0.2654  -0.0507 -0.0879 93   TRP C CD2 
9731  N  NE1 . TRP C 93   ? 1.1215 1.2934 1.1628 0.2757  -0.0522 -0.0848 93   TRP C NE1 
9732  C  CE2 . TRP C 93   ? 0.9980 1.1909 1.0485 0.2741  -0.0525 -0.0875 93   TRP C CE2 
9733  C  CE3 . TRP C 93   ? 0.9909 1.2154 1.0651 0.2618  -0.0502 -0.0905 93   TRP C CE3 
9734  C  CZ2 . TRP C 93   ? 1.0201 1.2237 1.0689 0.2795  -0.0542 -0.0897 93   TRP C CZ2 
9735  C  CZ3 . TRP C 93   ? 0.9807 1.2158 1.0536 0.2669  -0.0517 -0.0927 93   TRP C CZ3 
9736  C  CH2 . TRP C 93   ? 1.0292 1.2541 1.0896 0.2758  -0.0538 -0.0923 93   TRP C CH2 
9737  N  N   . TRP C 94   ? 0.6694 0.8787 0.7549 0.2421  -0.0426 -0.0871 94   TRP C N   
9738  C  CA  . TRP C 94   ? 0.6713 0.8934 0.7619 0.2438  -0.0414 -0.0897 94   TRP C CA  
9739  C  C   . TRP C 94   ? 0.7241 0.9341 0.8110 0.2413  -0.0395 -0.0887 94   TRP C C   
9740  O  O   . TRP C 94   ? 0.6795 0.8889 0.7625 0.2475  -0.0395 -0.0903 94   TRP C O   
9741  C  CB  . TRP C 94   ? 0.6245 0.8665 0.7278 0.2370  -0.0398 -0.0911 94   TRP C CB  
9742  C  CG  . TRP C 94   ? 0.7089 0.9669 0.8162 0.2399  -0.0416 -0.0933 94   TRP C CG  
9743  C  CD1 . TRP C 94   ? 0.8037 1.0713 0.9173 0.2362  -0.0426 -0.0938 94   TRP C CD1 
9744  C  CD2 . TRP C 94   ? 0.7848 1.0501 0.8892 0.2457  -0.0428 -0.0952 94   TRP C CD2 
9745  N  NE1 . TRP C 94   ? 0.8282 1.1089 0.9433 0.2394  -0.0444 -0.0960 94   TRP C NE1 
9746  C  CE2 . TRP C 94   ? 0.7628 1.0425 0.8724 0.2453  -0.0445 -0.0969 94   TRP C CE2 
9747  C  CE3 . TRP C 94   ? 0.8253 1.0865 0.9231 0.2515  -0.0425 -0.0958 94   TRP C CE3 
9748  C  CZ2 . TRP C 94   ? 0.6785 0.9690 0.7874 0.2504  -0.0460 -0.0991 94   TRP C CZ2 
9749  C  CZ3 . TRP C 94   ? 0.8148 1.0864 0.9117 0.2566  -0.0438 -0.0978 94   TRP C CZ3 
9750  C  CH2 . TRP C 94   ? 0.7102 0.9965 0.8127 0.2560  -0.0456 -0.0995 94   TRP C CH2 
9751  N  N   . ILE C 95   ? 0.9085 1.1088 0.9965 0.2324  -0.0379 -0.0862 95   ILE C N   
9752  C  CA  . ILE C 95   ? 0.8762 1.0657 0.9612 0.2295  -0.0364 -0.0855 95   ILE C CA  
9753  C  C   . ILE C 95   ? 0.8865 1.0579 0.9598 0.2360  -0.0378 -0.0851 95   ILE C C   
9754  O  O   . ILE C 95   ? 0.9682 1.1320 1.0380 0.2362  -0.0371 -0.0856 95   ILE C O   
9755  C  CB  . ILE C 95   ? 0.8862 1.0696 0.9750 0.2189  -0.0347 -0.0829 95   ILE C CB  
9756  C  CG1 . ILE C 95   ? 0.8729 1.0548 0.9632 0.2149  -0.0329 -0.0832 95   ILE C CG1 
9757  C  CG2 . ILE C 95   ? 0.9521 1.1169 1.0340 0.2179  -0.0356 -0.0803 95   ILE C CG2 
9758  C  CD1 . ILE C 95   ? 0.9868 1.1866 1.0843 0.2145  -0.0311 -0.0853 95   ILE C CD1 
9759  N  N   . GLY C 96   ? 0.6402 0.8041 0.7069 0.2415  -0.0396 -0.0844 96   GLY C N   
9760  C  CA  . GLY C 96   ? 0.7862 0.9323 0.8411 0.2480  -0.0407 -0.0841 96   GLY C CA  
9761  C  C   . GLY C 96   ? 0.8132 0.9647 0.8634 0.2590  -0.0419 -0.0868 96   GLY C C   
9762  O  O   . GLY C 96   ? 0.7562 0.8940 0.7968 0.2646  -0.0424 -0.0871 96   GLY C O   
9763  N  N   . ILE C 97   ? 1.1502 1.3218 1.2075 0.2620  -0.0425 -0.0888 97   ILE C N   
9764  C  CA  . ILE C 97   ? 1.2043 1.3809 1.2565 0.2687  -0.0433 -0.0903 97   ILE C CA  
9765  C  C   . ILE C 97   ? 1.2726 1.4473 1.3229 0.2698  -0.0419 -0.0917 97   ILE C C   
9766  O  O   . ILE C 97   ? 1.3190 1.4861 1.3599 0.2765  -0.0426 -0.0923 97   ILE C O   
9767  C  CB  . ILE C 97   ? 1.1863 1.3847 1.2471 0.2675  -0.0437 -0.0917 97   ILE C CB  
9768  C  CG1 . ILE C 97   ? 1.1982 1.3960 1.2564 0.2698  -0.0460 -0.0908 97   ILE C CG1 
9769  C  CG2 . ILE C 97   ? 1.1680 1.3758 1.2273 0.2724  -0.0437 -0.0938 97   ILE C CG2 
9770  C  CD1 . ILE C 97   ? 1.1779 1.3627 1.2224 0.2787  -0.0480 -0.0903 97   ILE C CD1 
9771  N  N   . GLY C 98   ? 1.3557 1.5368 1.4143 0.2637  -0.0400 -0.0922 98   GLY C N   
9772  C  CA  . GLY C 98   ? 1.2805 1.4613 1.3378 0.2646  -0.0385 -0.0937 98   GLY C CA  
9773  C  C   . GLY C 98   ? 1.3264 1.4871 1.3750 0.2662  -0.0388 -0.0935 98   GLY C C   
9774  O  O   . GLY C 98   ? 1.3248 1.4842 1.3712 0.2676  -0.0379 -0.0949 98   GLY C O   
9775  N  N   . HIS C 99   ? 1.3793 1.5229 1.4219 0.2641  -0.0398 -0.0913 99   HIS C N   
9776  C  CA  . HIS C 99   ? 1.3888 1.5119 1.4228 0.2629  -0.0398 -0.0907 99   HIS C CA  
9777  C  C   . HIS C 99   ? 1.4158 1.5302 1.4388 0.2734  -0.0408 -0.0926 99   HIS C C   
9778  O  O   . HIS C 99   ? 1.3099 1.4145 1.3276 0.2736  -0.0405 -0.0937 99   HIS C O   
9779  C  CB  . HIS C 99   ? 1.4042 1.5115 1.4349 0.2580  -0.0402 -0.0879 99   HIS C CB  
9780  C  CG  . HIS C 99   ? 1.4788 1.5667 1.5032 0.2543  -0.0400 -0.0874 99   HIS C CG  
9781  N  ND1 . HIS C 99   ? 1.4424 1.5256 1.4717 0.2442  -0.0391 -0.0858 99   HIS C ND1 
9782  C  CD2 . HIS C 99   ? 1.4380 1.5102 1.4518 0.2593  -0.0406 -0.0886 99   HIS C CD2 
9783  C  CE1 . HIS C 99   ? 1.3840 1.4503 1.4066 0.2429  -0.0393 -0.0861 99   HIS C CE1 
9784  N  NE2 . HIS C 99   ? 1.3799 1.4388 1.3928 0.2518  -0.0402 -0.0879 99   HIS C NE2 
9785  N  N   . ALA C 100  ? 1.5171 1.6341 1.5355 0.2810  -0.0419 -0.0928 100  ALA C N   
9786  C  CA  . ALA C 100  ? 1.5003 1.6074 1.5066 0.2887  -0.0426 -0.0936 100  ALA C CA  
9787  C  C   . ALA C 100  ? 1.4238 1.5419 1.4318 0.2904  -0.0416 -0.0958 100  ALA C C   
9788  O  O   . ALA C 100  ? 1.4558 1.5628 1.4551 0.2943  -0.0416 -0.0970 100  ALA C O   
9789  C  CB  . ALA C 100  ? 1.5175 1.6255 1.5182 0.2943  -0.0440 -0.0926 100  ALA C CB  
9790  N  N   . GLY C 101  ? 1.3052 1.4447 1.3240 0.2874  -0.0407 -0.0963 101  GLY C N   
9791  C  CA  . GLY C 101  ? 1.4409 1.5913 1.4619 0.2886  -0.0392 -0.0982 101  GLY C CA  
9792  C  C   . GLY C 101  ? 1.4789 1.6233 1.5005 0.2853  -0.0380 -0.0991 101  GLY C C   
9793  O  O   . GLY C 101  ? 1.4399 1.5816 1.4561 0.2888  -0.0374 -0.1007 101  GLY C O   
9794  N  N   . THR C 102  ? 1.2946 1.4368 1.3224 0.2787  -0.0377 -0.0983 102  THR C N   
9795  C  CA  . THR C 102  ? 1.1623 1.2966 1.1897 0.2750  -0.0371 -0.0991 102  THR C CA  
9796  C  C   . THR C 102  ? 1.1144 1.2261 1.1289 0.2784  -0.0385 -0.0996 102  THR C C   
9797  O  O   . THR C 102  ? 1.1250 1.2304 1.1355 0.2781  -0.0383 -0.1011 102  THR C O   
9798  C  CB  . THR C 102  ? 1.0609 1.1953 1.0960 0.2634  -0.0365 -0.0967 102  THR C CB  
9799  O  OG1 . THR C 102  ? 1.1259 1.2795 1.1720 0.2605  -0.0353 -0.0961 102  THR C OG1 
9800  C  CG2 . THR C 102  ? 0.8750 1.0059 0.9110 0.2573  -0.0355 -0.0970 102  THR C CG2 
9801  N  N   . LEU C 103  ? 0.8869 0.9859 0.8945 0.2818  -0.0400 -0.0986 103  LEU C N   
9802  C  CA  . LEU C 103  ? 0.8953 0.9722 0.8900 0.2856  -0.0410 -0.0992 103  LEU C CA  
9803  C  C   . LEU C 103  ? 0.9707 1.0473 0.9570 0.2946  -0.0411 -0.1014 103  LEU C C   
9804  O  O   . LEU C 103  ? 0.9504 1.0141 0.9288 0.2969  -0.0414 -0.1032 103  LEU C O   
9805  C  CB  . LEU C 103  ? 0.8335 0.8969 0.8223 0.2869  -0.0420 -0.0972 103  LEU C CB  
9806  C  CG  . LEU C 103  ? 0.7146 0.7531 0.6896 0.2901  -0.0427 -0.0975 103  LEU C CG  
9807  C  CD1 . LEU C 103  ? 0.6161 0.6403 0.5903 0.2829  -0.0425 -0.0948 103  LEU C CD1 
9808  C  CD2 . LEU C 103  ? 0.6988 0.7332 0.6633 0.3012  -0.0432 -0.0980 103  LEU C CD2 
9809  N  N   . ILE C 104  ? 1.6813 1.7715 1.6688 0.2982  -0.0408 -0.1008 104  ILE C N   
9810  C  CA  . ILE C 104  ? 1.7449 1.8354 1.7244 0.3052  -0.0407 -0.1022 104  ILE C CA  
9811  C  C   . ILE C 104  ? 1.7805 1.8791 1.7631 0.3042  -0.0392 -0.1042 104  ILE C C   
9812  O  O   . ILE C 104  ? 1.8158 1.9052 1.7891 0.3088  -0.0393 -0.1058 104  ILE C O   
9813  C  CB  . ILE C 104  ? 1.8095 1.9144 1.7909 0.3091  -0.0408 -0.1013 104  ILE C CB  
9814  C  CG1 . ILE C 104  ? 1.8102 1.9044 1.7856 0.3115  -0.0424 -0.0994 104  ILE C CG1 
9815  C  CG2 . ILE C 104  ? 1.7866 1.8946 1.7611 0.3162  -0.0405 -0.1028 104  ILE C CG2 
9816  C  CD1 . ILE C 104  ? 1.8785 1.9855 1.8543 0.3160  -0.0432 -0.0989 104  ILE C CD1 
9817  N  N   . SER C 105  ? 1.1128 1.2280 1.1079 0.2981  -0.0378 -0.1040 105  SER C N   
9818  C  CA  . SER C 105  ? 1.1039 1.2284 1.1022 0.2972  -0.0359 -0.1056 105  SER C CA  
9819  C  C   . SER C 105  ? 1.0874 1.1997 1.0832 0.2944  -0.0362 -0.1070 105  SER C C   
9820  O  O   . SER C 105  ? 1.0266 1.1426 1.0218 0.2950  -0.0349 -0.1086 105  SER C O   
9821  C  CB  . SER C 105  ? 1.1047 1.2518 1.1169 0.2919  -0.0338 -0.1050 105  SER C CB  
9822  O  OG  . SER C 105  ? 1.0872 1.2433 1.1023 0.2910  -0.0315 -0.1063 105  SER C OG  
9823  N  N   . ALA C 106  ? 1.2583 1.3560 1.2524 0.2916  -0.0378 -0.1066 106  ALA C N   
9824  C  CA  . ALA C 106  ? 1.1973 1.2835 1.1895 0.2850  -0.0383 -0.1070 106  ALA C CA  
9825  C  C   . ALA C 106  ? 1.2240 1.2862 1.2050 0.2857  -0.0404 -0.1074 106  ALA C C   
9826  O  O   . ALA C 106  ? 1.2474 1.2983 1.2206 0.2872  -0.0411 -0.1096 106  ALA C O   
9827  C  CB  . ALA C 106  ? 1.1099 1.2029 1.1131 0.2738  -0.0377 -0.1046 106  ALA C CB  
9828  N  N   . ILE C 107  ? 1.0897 1.1436 1.0697 0.2844  -0.0412 -0.1055 107  ILE C N   
9829  C  CA  . ILE C 107  ? 1.0325 1.0631 1.0026 0.2838  -0.0426 -0.1056 107  ILE C CA  
9830  C  C   . ILE C 107  ? 1.0879 1.1071 1.0446 0.2945  -0.0432 -0.1080 107  ILE C C   
9831  O  O   . ILE C 107  ? 1.0760 1.0779 1.0238 0.2943  -0.0442 -0.1098 107  ILE C O   
9832  C  CB  . ILE C 107  ? 0.9651 0.9899 0.9368 0.2805  -0.0428 -0.1027 107  ILE C CB  
9833  C  CG1 . ILE C 107  ? 0.8956 0.9297 0.8797 0.2695  -0.0422 -0.1005 107  ILE C CG1 
9834  C  CG2 . ILE C 107  ? 0.9737 0.9737 0.9344 0.2803  -0.0437 -0.1029 107  ILE C CG2 
9835  C  CD1 . ILE C 107  ? 0.9044 0.9291 0.8892 0.2646  -0.0423 -0.0977 107  ILE C CD1 
9836  N  N   . LEU C 108  ? 1.2732 1.3020 1.2283 0.3041  -0.0427 -0.1083 108  LEU C N   
9837  C  CA  . LEU C 108  ? 1.2546 1.2734 1.1966 0.3116  -0.0430 -0.1093 108  LEU C CA  
9838  C  C   . LEU C 108  ? 1.2588 1.2786 1.1974 0.3135  -0.0427 -0.1121 108  LEU C C   
9839  O  O   . LEU C 108  ? 1.3416 1.3472 1.2679 0.3187  -0.0432 -0.1136 108  LEU C O   
9840  C  CB  . LEU C 108  ? 1.2435 1.2744 1.1854 0.3165  -0.0424 -0.1074 108  LEU C CB  
9841  C  CG  . LEU C 108  ? 1.1174 1.1437 1.0583 0.3168  -0.0430 -0.1048 108  LEU C CG  
9842  C  CD1 . LEU C 108  ? 1.2003 1.2398 1.1407 0.3222  -0.0429 -0.1036 108  LEU C CD1 
9843  C  CD2 . LEU C 108  ? 1.1014 1.1012 1.0292 0.3190  -0.0437 -0.1048 108  LEU C CD2 
9844  N  N   . LEU C 109  ? 1.1600 1.1958 1.1088 0.3095  -0.0417 -0.1127 109  LEU C N   
9845  C  CA  . LEU C 109  ? 1.1702 1.2061 1.1153 0.3110  -0.0413 -0.1153 109  LEU C CA  
9846  C  C   . LEU C 109  ? 1.1599 1.1750 1.0976 0.3086  -0.0432 -0.1176 109  LEU C C   
9847  O  O   . LEU C 109  ? 1.1502 1.1555 1.0780 0.3135  -0.0437 -0.1204 109  LEU C O   
9848  C  CB  . LEU C 109  ? 1.1730 1.2297 1.1304 0.3067  -0.0395 -0.1151 109  LEU C CB  
9849  C  CG  . LEU C 109  ? 1.0507 1.1102 1.0050 0.3084  -0.0386 -0.1174 109  LEU C CG  
9850  C  CD1 . LEU C 109  ? 1.1513 1.2068 1.0945 0.3163  -0.0383 -0.1184 109  LEU C CD1 
9851  C  CD2 . LEU C 109  ? 0.9633 1.0448 0.9297 0.3044  -0.0361 -0.1165 109  LEU C CD2 
9852  N  N   . LEU C 110  ? 1.1757 1.1840 1.1181 0.2988  -0.0441 -0.1158 110  LEU C N   
9853  C  CA  . LEU C 110  ? 1.1937 1.1823 1.1298 0.2933  -0.0459 -0.1172 110  LEU C CA  
9854  C  C   . LEU C 110  ? 1.2562 1.2232 1.1795 0.2983  -0.0469 -0.1180 110  LEU C C   
9855  O  O   . LEU C 110  ? 1.3445 1.2947 1.2585 0.2982  -0.0482 -0.1206 110  LEU C O   
9856  C  CB  . LEU C 110  ? 1.1781 1.1677 1.1242 0.2812  -0.0464 -0.1150 110  LEU C CB  
9857  C  CG  . LEU C 110  ? 1.0765 1.0865 1.0355 0.2755  -0.0452 -0.1136 110  LEU C CG  
9858  C  CD1 . LEU C 110  ? 1.0769 1.0864 1.0448 0.2646  -0.0456 -0.1111 110  LEU C CD1 
9859  C  CD2 . LEU C 110  ? 0.9451 0.9587 0.9024 0.2759  -0.0454 -0.1161 110  LEU C CD2 
9860  N  N   . LEU C 111  ? 1.1178 1.0843 1.0400 0.3026  -0.0462 -0.1159 111  LEU C N   
9861  C  CA  . LEU C 111  ? 1.1294 1.0748 1.0386 0.3079  -0.0466 -0.1163 111  LEU C CA  
9862  C  C   . LEU C 111  ? 1.1708 1.1106 1.0676 0.3196  -0.0466 -0.1189 111  LEU C C   
9863  O  O   . LEU C 111  ? 1.1563 1.0770 1.0406 0.3232  -0.0468 -0.1191 111  LEU C O   
9864  C  CB  . LEU C 111  ? 1.1511 1.0983 1.0624 0.3094  -0.0458 -0.1130 111  LEU C CB  
9865  C  CG  . LEU C 111  ? 1.1051 1.0413 1.0195 0.2998  -0.0458 -0.1106 111  LEU C CG  
9866  C  CD1 . LEU C 111  ? 1.0526 1.0016 0.9812 0.2884  -0.0459 -0.1095 111  LEU C CD1 
9867  C  CD2 . LEU C 111  ? 1.1320 1.0683 1.0453 0.3038  -0.0450 -0.1076 111  LEU C CD2 
9868  N  N   . ASN C 112  ? 1.3991 1.3557 1.2991 0.3220  -0.0459 -0.1195 112  ASN C N   
9869  C  CA  . ASN C 112  ? 1.3857 1.3400 1.2750 0.3294  -0.0455 -0.1205 112  ASN C CA  
9870  C  C   . ASN C 112  ? 1.4735 1.4261 1.3564 0.3353  -0.0449 -0.1180 112  ASN C C   
9871  O  O   . ASN C 112  ? 1.5708 1.5093 1.4402 0.3411  -0.0451 -0.1187 112  ASN C O   
9872  C  CB  . ASN C 112  ? 1.4586 1.3912 1.3355 0.3305  -0.0468 -0.1241 112  ASN C CB  
9873  C  CG  . ASN C 112  ? 1.4864 1.4211 1.3550 0.3370  -0.0464 -0.1257 112  ASN C CG  
9874  O  OD1 . ASN C 112  ? 1.4363 1.3902 1.3099 0.3399  -0.0450 -0.1244 112  ASN C OD1 
9875  N  ND2 . ASN C 112  ? 1.4793 1.3938 1.3352 0.3390  -0.0476 -0.1287 112  ASN C ND2 
9876  N  N   . GLN C 113  ? 1.6041 1.5707 1.4961 0.3338  -0.0443 -0.1150 113  GLN C N   
9877  C  CA  . GLN C 113  ? 1.5896 1.5573 1.4766 0.3395  -0.0440 -0.1126 113  GLN C CA  
9878  C  C   . GLN C 113  ? 1.6526 1.6410 1.5429 0.3442  -0.0432 -0.1125 113  GLN C C   
9879  O  O   . GLN C 113  ? 1.5762 1.5849 1.4789 0.3407  -0.0423 -0.1125 113  GLN C O   
9880  C  CB  . GLN C 113  ? 1.5585 1.5302 1.4530 0.3357  -0.0441 -0.1098 113  GLN C CB  
9881  C  CG  . GLN C 113  ? 1.6114 1.5610 1.5012 0.3319  -0.0445 -0.1096 113  GLN C CG  
9882  C  CD  . GLN C 113  ? 1.6984 1.6231 1.5711 0.3369  -0.0447 -0.1104 113  GLN C CD  
9883  O  OE1 . GLN C 113  ? 1.7823 1.7050 1.6461 0.3438  -0.0445 -0.1093 113  GLN C OE1 
9884  N  NE2 . GLN C 113  ? 1.7059 1.6111 1.5738 0.3332  -0.0451 -0.1125 113  GLN C NE2 
9885  N  N   . GLY C 114  ? 1.4089 1.3920 1.2881 0.3520  -0.0432 -0.1123 114  GLY C N   
9886  C  CA  . GLY C 114  ? 1.3918 1.3925 1.2725 0.3573  -0.0424 -0.1126 114  GLY C CA  
9887  C  C   . GLY C 114  ? 1.4027 1.4227 1.2915 0.3588  -0.0422 -0.1105 114  GLY C C   
9888  O  O   . GLY C 114  ? 1.4573 1.4935 1.3487 0.3628  -0.0415 -0.1109 114  GLY C O   
9889  N  N   . TRP C 115  ? 1.3059 1.3248 1.1986 0.3557  -0.0429 -0.1085 115  TRP C N   
9890  C  CA  . TRP C 115  ? 1.2476 1.2841 1.1474 0.3570  -0.0432 -0.1068 115  TRP C CA  
9891  C  C   . TRP C 115  ? 1.1976 1.2553 1.1148 0.3494  -0.0424 -0.1064 115  TRP C C   
9892  O  O   . TRP C 115  ? 1.1998 1.2709 1.1241 0.3488  -0.0429 -0.1051 115  TRP C O   
9893  C  CB  . TRP C 115  ? 1.2620 1.2848 1.1546 0.3589  -0.0444 -0.1046 115  TRP C CB  
9894  C  CG  . TRP C 115  ? 1.2626 1.2700 1.1557 0.3525  -0.0445 -0.1038 115  TRP C CG  
9895  C  CD1 . TRP C 115  ? 1.2721 1.2562 1.1558 0.3514  -0.0444 -0.1046 115  TRP C CD1 
9896  C  CD2 . TRP C 115  ? 1.2861 1.3001 1.1896 0.3462  -0.0447 -0.1020 115  TRP C CD2 
9897  N  NE1 . TRP C 115  ? 1.2648 1.2411 1.1530 0.3449  -0.0444 -0.1035 115  TRP C NE1 
9898  C  CE2 . TRP C 115  ? 1.2450 1.2392 1.1450 0.3418  -0.0446 -0.1018 115  TRP C CE2 
9899  C  CE3 . TRP C 115  ? 1.2373 1.2717 1.1525 0.3438  -0.0449 -0.1009 115  TRP C CE3 
9900  C  CZ2 . TRP C 115  ? 1.1595 1.1540 1.0674 0.3354  -0.0446 -0.1002 115  TRP C CZ2 
9901  C  CZ3 . TRP C 115  ? 1.1363 1.1707 1.0590 0.3375  -0.0450 -0.0993 115  TRP C CZ3 
9902  C  CH2 . TRP C 115  ? 1.1392 1.1539 1.0582 0.3335  -0.0448 -0.0989 115  TRP C CH2 
9903  N  N   . ARG C 116  ? 1.5579 1.6186 1.4816 0.3439  -0.0414 -0.1077 116  ARG C N   
9904  C  CA  . ARG C 116  ? 1.5638 1.6442 1.5034 0.3367  -0.0403 -0.1074 116  ARG C CA  
9905  C  C   . ARG C 116  ? 1.4963 1.5969 1.4425 0.3379  -0.0385 -0.1087 116  ARG C C   
9906  O  O   . ARG C 116  ? 1.4488 1.5668 1.4080 0.3321  -0.0372 -0.1085 116  ARG C O   
9907  C  CB  . ARG C 116  ? 1.5704 1.6424 1.5136 0.3296  -0.0401 -0.1080 116  ARG C CB  
9908  C  CG  . ARG C 116  ? 1.5626 1.6259 1.4995 0.3309  -0.0397 -0.1103 116  ARG C CG  
9909  C  CD  . ARG C 116  ? 1.5811 1.6433 1.5250 0.3234  -0.0394 -0.1111 116  ARG C CD  
9910  N  NE  . ARG C 116  ? 1.5452 1.6296 1.5034 0.3183  -0.0377 -0.1105 116  ARG C NE  
9911  C  CZ  . ARG C 116  ? 1.5409 1.6380 1.5030 0.3181  -0.0358 -0.1117 116  ARG C CZ  
9912  N  NH1 . ARG C 116  ? 1.5000 1.5904 1.4529 0.3230  -0.0355 -0.1136 116  ARG C NH1 
9913  N  NH2 . ARG C 116  ? 1.4996 1.6160 1.4748 0.3129  -0.0340 -0.1109 116  ARG C NH2 
9914  N  N   . ASN C 117  ? 1.2112 1.3097 1.1485 0.3450  -0.0382 -0.1098 117  ASN C N   
9915  C  CA  . ASN C 117  ? 1.2043 1.3200 1.1469 0.3462  -0.0361 -0.1111 117  ASN C CA  
9916  C  C   . ASN C 117  ? 1.2312 1.3695 1.1834 0.3471  -0.0355 -0.1106 117  ASN C C   
9917  O  O   . ASN C 117  ? 1.2478 1.4044 1.2097 0.3447  -0.0332 -0.1113 117  ASN C O   
9918  C  CB  . ASN C 117  ? 1.2169 1.3220 1.1463 0.3538  -0.0359 -0.1126 117  ASN C CB  
9919  C  CG  . ASN C 117  ? 1.1949 1.2796 1.1158 0.3525  -0.0364 -0.1139 117  ASN C CG  
9920  O  OD1 . ASN C 117  ? 1.1890 1.2773 1.1147 0.3481  -0.0352 -0.1149 117  ASN C OD1 
9921  N  ND2 . ASN C 117  ? 1.1271 1.1900 1.0349 0.3562  -0.0382 -0.1139 117  ASN C ND2 
9922  N  N   . SER C 118  ? 1.3177 1.4549 1.2672 0.3504  -0.0374 -0.1095 118  SER C N   
9923  C  CA  . SER C 118  ? 1.3155 1.4733 1.2728 0.3522  -0.0373 -0.1095 118  SER C CA  
9924  C  C   . SER C 118  ? 1.2715 1.4406 1.2409 0.3455  -0.0379 -0.1083 118  SER C C   
9925  O  O   . SER C 118  ? 1.2248 1.4126 1.2025 0.3457  -0.0378 -0.1086 118  SER C O   
9926  C  CB  . SER C 118  ? 1.4062 1.5573 1.3518 0.3615  -0.0393 -0.1093 118  SER C CB  
9927  O  OG  . SER C 118  ? 1.3039 1.4407 1.2436 0.3617  -0.0415 -0.1077 118  SER C OG  
9928  N  N   . ILE C 119  ? 1.0582 1.2164 1.0289 0.3395  -0.0384 -0.1071 119  ILE C N   
9929  C  CA  . ILE C 119  ? 1.1007 1.2672 1.0815 0.3334  -0.0391 -0.1059 119  ILE C CA  
9930  C  C   . ILE C 119  ? 1.0797 1.2487 1.0703 0.3243  -0.0376 -0.1056 119  ILE C C   
9931  O  O   . ILE C 119  ? 0.9241 1.0996 0.9233 0.3187  -0.0379 -0.1045 119  ILE C O   
9932  C  CB  . ILE C 119  ? 1.0550 1.2058 1.0274 0.3359  -0.0417 -0.1042 119  ILE C CB  
9933  C  CG1 . ILE C 119  ? 1.0810 1.2066 1.0423 0.3362  -0.0420 -0.1037 119  ILE C CG1 
9934  C  CG2 . ILE C 119  ? 1.0858 1.2384 1.0505 0.3446  -0.0433 -0.1044 119  ILE C CG2 
9935  C  CD1 . ILE C 119  ? 1.1345 1.2423 1.0857 0.3393  -0.0439 -0.1020 119  ILE C CD1 
9936  N  N   . ASN C 120  ? 1.3672 1.5310 1.3562 0.3228  -0.0360 -0.1065 120  ASN C N   
9937  C  CA  . ASN C 120  ? 1.2488 1.4141 1.2461 0.3146  -0.0347 -0.1062 120  ASN C CA  
9938  C  C   . ASN C 120  ? 1.1401 1.3288 1.1520 0.3092  -0.0324 -0.1064 120  ASN C C   
9939  O  O   . ASN C 120  ? 1.1495 1.3426 1.1703 0.3019  -0.0318 -0.1056 120  ASN C O   
9940  C  CB  . ASN C 120  ? 1.1343 1.2872 1.1250 0.3151  -0.0339 -0.1075 120  ASN C CB  
9941  C  CG  . ASN C 120  ? 1.1190 1.2843 1.1116 0.3170  -0.0313 -0.1090 120  ASN C CG  
9942  O  OD1 . ASN C 120  ? 1.1681 1.3446 1.1610 0.3216  -0.0307 -0.1094 120  ASN C OD1 
9943  N  ND2 . ASN C 120  ? 1.2698 1.4331 1.2635 0.3137  -0.0298 -0.1098 120  ASN C ND2 
9944  N  N   . ARG C 121  ? 1.0647 1.2683 1.0792 0.3126  -0.0309 -0.1076 121  ARG C N   
9945  C  CA  . ARG C 121  ? 1.0701 1.2958 1.0985 0.3073  -0.0283 -0.1080 121  ARG C CA  
9946  C  C   . ARG C 121  ? 1.1118 1.3482 1.1488 0.3038  -0.0296 -0.1072 121  ARG C C   
9947  O  O   . ARG C 121  ? 1.0274 1.2729 1.0751 0.2963  -0.0283 -0.1067 121  ARG C O   
9948  C  CB  . ARG C 121  ? 1.1011 1.3395 1.1297 0.3121  -0.0262 -0.1095 121  ARG C CB  
9949  C  CG  . ARG C 121  ? 1.0747 1.3371 1.1177 0.3076  -0.0237 -0.1101 121  ARG C CG  
9950  C  CD  . ARG C 121  ? 1.1227 1.3909 1.1734 0.3005  -0.0201 -0.1100 121  ARG C CD  
9951  N  NE  . ARG C 121  ? 1.1684 1.4248 1.2104 0.3032  -0.0188 -0.1105 121  ARG C NE  
9952  C  CZ  . ARG C 121  ? 1.1796 1.4400 1.2179 0.3081  -0.0167 -0.1117 121  ARG C CZ  
9953  N  NH1 . ARG C 121  ? 1.1612 1.4375 1.2042 0.3110  -0.0155 -0.1126 121  ARG C NH1 
9954  N  NH2 . ARG C 121  ? 1.2081 1.4566 1.2380 0.3102  -0.0158 -0.1121 121  ARG C NH2 
9955  N  N   . PHE C 122  ? 1.1920 1.4272 1.2240 0.3095  -0.0321 -0.1071 122  PHE C N   
9956  C  CA  . PHE C 122  ? 1.0750 1.3195 1.1139 0.3070  -0.0338 -0.1066 122  PHE C CA  
9957  C  C   . PHE C 122  ? 1.0092 1.2422 1.0486 0.3016  -0.0351 -0.1048 122  PHE C C   
9958  O  O   . PHE C 122  ? 1.0071 1.2504 1.0566 0.2955  -0.0349 -0.1043 122  PHE C O   
9959  C  CB  . PHE C 122  ? 0.9793 1.2226 1.0106 0.3151  -0.0365 -0.1069 122  PHE C CB  
9960  C  CG  . PHE C 122  ? 1.0612 1.3221 1.1015 0.3139  -0.0377 -0.1076 122  PHE C CG  
9961  C  CD1 . PHE C 122  ? 1.1595 1.4170 1.2011 0.3113  -0.0400 -0.1064 122  PHE C CD1 
9962  C  CD2 . PHE C 122  ? 1.1178 1.3987 1.1654 0.3153  -0.0365 -0.1096 122  PHE C CD2 
9963  C  CE1 . PHE C 122  ? 1.1010 1.3745 1.1504 0.3102  -0.0413 -0.1073 122  PHE C CE1 
9964  C  CE2 . PHE C 122  ? 1.2030 1.5004 1.2591 0.3140  -0.0378 -0.1106 122  PHE C CE2 
9965  C  CZ  . PHE C 122  ? 1.1424 1.4359 1.1991 0.3115  -0.0404 -0.1095 122  PHE C CZ  
9966  N  N   . ALA C 123  ? 1.1771 1.3889 1.2059 0.3038  -0.0362 -0.1038 123  ALA C N   
9967  C  CA  . ALA C 123  ? 1.1798 1.3798 1.2087 0.2990  -0.0373 -0.1021 123  ALA C CA  
9968  C  C   . ALA C 123  ? 1.1784 1.3853 1.2180 0.2903  -0.0351 -0.1019 123  ALA C C   
9969  O  O   . ALA C 123  ? 1.2556 1.4665 1.3026 0.2846  -0.0353 -0.1009 123  ALA C O   
9970  C  CB  . ALA C 123  ? 1.3246 1.5002 1.3400 0.3030  -0.0386 -0.1015 123  ALA C CB  
9971  N  N   . GLU C 124  ? 1.2281 1.4360 1.2681 0.2895  -0.0328 -0.1030 124  GLU C N   
9972  C  CA  . GLU C 124  ? 1.2104 1.4244 1.2596 0.2818  -0.0306 -0.1028 124  GLU C CA  
9973  C  C   . GLU C 124  ? 1.1560 1.3916 1.2183 0.2767  -0.0288 -0.1030 124  GLU C C   
9974  O  O   . GLU C 124  ? 1.2006 1.4408 1.2712 0.2696  -0.0277 -0.1022 124  GLU C O   
9975  C  CB  . GLU C 124  ? 1.3563 1.5672 1.4020 0.2829  -0.0285 -0.1040 124  GLU C CB  
9976  C  CG  . GLU C 124  ? 1.3972 1.6126 1.4506 0.2757  -0.0262 -0.1038 124  GLU C CG  
9977  C  CD  . GLU C 124  ? 1.4426 1.6419 1.4931 0.2726  -0.0278 -0.1030 124  GLU C CD  
9978  O  OE1 . GLU C 124  ? 1.3513 1.5399 1.3982 0.2734  -0.0303 -0.1019 124  GLU C OE1 
9979  O  OE2 . GLU C 124  ? 1.4563 1.6535 1.5080 0.2695  -0.0264 -0.1034 124  GLU C OE2 
9980  N  N   . ALA C 125  ? 0.8020 1.0512 0.8664 0.2802  -0.0283 -0.1041 125  ALA C N   
9981  C  CA  . ALA C 125  ? 0.8246 1.0944 0.9017 0.2754  -0.0269 -0.1047 125  ALA C CA  
9982  C  C   . ALA C 125  ? 0.7325 1.0021 0.8131 0.2722  -0.0293 -0.1036 125  ALA C C   
9983  O  O   . ALA C 125  ? 0.7243 1.0052 0.8155 0.2652  -0.0280 -0.1034 125  ALA C O   
9984  C  CB  . ALA C 125  ? 0.8762 1.1597 0.9543 0.2805  -0.0265 -0.1064 125  ALA C CB  
9985  N  N   . MET C 126  ? 0.9575 1.2139 1.0289 0.2773  -0.0326 -0.1027 126  MET C N   
9986  C  CA  . MET C 126  ? 0.8944 1.1483 0.9676 0.2748  -0.0349 -0.1015 126  MET C CA  
9987  C  C   . MET C 126  ? 0.9353 1.1809 1.0115 0.2680  -0.0341 -0.0999 126  MET C C   
9988  O  O   . MET C 126  ? 0.9116 1.1626 0.9948 0.2628  -0.0345 -0.0992 126  MET C O   
9989  C  CB  . MET C 126  ? 0.8298 1.0695 0.8909 0.2824  -0.0381 -0.1008 126  MET C CB  
9990  C  CG  . MET C 126  ? 0.8498 1.0988 0.9083 0.2892  -0.0394 -0.1023 126  MET C CG  
9991  S  SD  . MET C 126  ? 1.1235 1.3532 1.1656 0.2986  -0.0428 -0.1012 126  MET C SD  
9992  C  CE  . MET C 126  ? 0.9943 1.2206 1.0386 0.2951  -0.0450 -0.0995 126  MET C CE  
9993  N  N   . THR C 127  ? 1.2589 1.4915 1.3299 0.2681  -0.0332 -0.0995 127  THR C N   
9994  C  CA  . THR C 127  ? 1.2184 1.4437 1.2925 0.2619  -0.0326 -0.0982 127  THR C CA  
9995  C  C   . THR C 127  ? 1.1512 1.3928 1.2378 0.2543  -0.0297 -0.0985 127  THR C C   
9996  O  O   . THR C 127  ? 1.2331 1.4765 1.3260 0.2485  -0.0297 -0.0975 127  THR C O   
9997  C  CB  . THR C 127  ? 1.2843 1.4936 1.3504 0.2638  -0.0324 -0.0984 127  THR C CB  
9998  O  OG1 . THR C 127  ? 1.4129 1.6302 1.4808 0.2639  -0.0299 -0.0998 127  THR C OG1 
9999  C  CG2 . THR C 127  ? 1.2105 1.4036 1.2637 0.2714  -0.0347 -0.0983 127  THR C CG2 
10000 N  N   . LEU C 128  ? 1.1082 1.3614 1.1982 0.2544  -0.0271 -0.1000 128  LEU C N   
10001 C  CA  . LEU C 128  ? 1.1526 1.4208 1.2538 0.2474  -0.0237 -0.1003 128  LEU C CA  
10002 C  C   . LEU C 128  ? 1.1674 1.4498 1.2778 0.2435  -0.0240 -0.1005 128  LEU C C   
10003 O  O   . LEU C 128  ? 1.1976 1.4862 1.3163 0.2364  -0.0225 -0.0999 128  LEU C O   
10004 C  CB  . LEU C 128  ? 1.0641 1.3419 1.1664 0.2490  -0.0206 -0.1018 128  LEU C CB  
10005 C  CG  . LEU C 128  ? 1.1059 1.3754 1.2041 0.2489  -0.0186 -0.1018 128  LEU C CG  
10006 C  CD1 . LEU C 128  ? 1.2077 1.4582 1.2932 0.2553  -0.0213 -0.1018 128  LEU C CD1 
10007 C  CD2 . LEU C 128  ? 1.2052 1.4878 1.3069 0.2491  -0.0146 -0.1032 128  LEU C CD2 
10008 N  N   . PHE C 129  ? 1.0056 1.2933 1.1145 0.2481  -0.0261 -0.1013 129  PHE C N   
10009 C  CA  . PHE C 129  ? 1.0551 1.3567 1.1724 0.2448  -0.0268 -0.1020 129  PHE C CA  
10010 C  C   . PHE C 129  ? 1.0571 1.3495 1.1732 0.2427  -0.0294 -0.1003 129  PHE C C   
10011 O  O   . PHE C 129  ? 1.0056 1.3073 1.1302 0.2370  -0.0291 -0.1004 129  PHE C O   
10012 C  CB  . PHE C 129  ? 1.0239 1.3344 1.1397 0.2509  -0.0285 -0.1037 129  PHE C CB  
10013 C  CG  . PHE C 129  ? 0.9723 1.2930 1.0897 0.2532  -0.0258 -0.1054 129  PHE C CG  
10014 C  CD1 . PHE C 129  ? 0.9717 1.3003 1.0962 0.2478  -0.0215 -0.1057 129  PHE C CD1 
10015 C  CD2 . PHE C 129  ? 0.9765 1.2987 1.0881 0.2610  -0.0274 -0.1066 129  PHE C CD2 
10016 C  CE1 . PHE C 129  ? 1.0198 1.3575 1.1455 0.2501  -0.0186 -0.1072 129  PHE C CE1 
10017 C  CE2 . PHE C 129  ? 1.1015 1.4332 1.2147 0.2633  -0.0247 -0.1081 129  PHE C CE2 
10018 C  CZ  . PHE C 129  ? 1.0809 1.4204 1.2013 0.2578  -0.0203 -0.1084 129  PHE C CZ  
10019 N  N   . ALA C 130  ? 0.9410 1.2150 1.0467 0.2473  -0.0319 -0.0989 130  ALA C N   
10020 C  CA  . ALA C 130  ? 0.8570 1.1212 0.9611 0.2455  -0.0340 -0.0971 130  ALA C CA  
10021 C  C   . ALA C 130  ? 0.8635 1.1251 0.9732 0.2380  -0.0320 -0.0959 130  ALA C C   
10022 O  O   . ALA C 130  ? 0.8906 1.1533 1.0048 0.2337  -0.0326 -0.0949 130  ALA C O   
10023 C  CB  . ALA C 130  ? 0.9213 1.1658 1.0125 0.2522  -0.0365 -0.0959 130  ALA C CB  
10024 N  N   . VAL C 131  ? 1.0589 1.3167 1.1681 0.2368  -0.0298 -0.0959 131  VAL C N   
10025 C  CA  . VAL C 131  ? 1.0146 1.2677 1.1270 0.2268  -0.0276 -0.0938 131  VAL C CA  
10026 C  C   . VAL C 131  ? 1.0604 1.3313 1.1842 0.2201  -0.0250 -0.0945 131  VAL C C   
10027 O  O   . VAL C 131  ? 1.1625 1.4314 1.2900 0.2118  -0.0241 -0.0926 131  VAL C O   
10028 C  CB  . VAL C 131  ? 0.9985 1.2420 1.1058 0.2265  -0.0261 -0.0935 131  VAL C CB  
10029 C  CG1 . VAL C 131  ? 1.1105 1.3526 1.2220 0.2165  -0.0235 -0.0916 131  VAL C CG1 
10030 C  CG2 . VAL C 131  ? 1.0450 1.2685 1.1413 0.2308  -0.0286 -0.0925 131  VAL C CG2 
10031 N  N   . ALA C 132  ? 0.9170 1.2053 1.0465 0.2235  -0.0236 -0.0972 132  ALA C N   
10032 C  CA  . ALA C 132  ? 0.9682 1.2739 1.1089 0.2171  -0.0209 -0.0983 132  ALA C CA  
10033 C  C   . ALA C 132  ? 1.0261 1.3371 1.1713 0.2147  -0.0231 -0.0983 132  ALA C C   
10034 O  O   . ALA C 132  ? 1.0171 1.3340 1.1692 0.2063  -0.0212 -0.0978 132  ALA C O   
10035 C  CB  . ALA C 132  ? 0.9645 1.2855 1.1090 0.2199  -0.0188 -0.1007 132  ALA C CB  
10036 N  N   . CYS C 133  ? 1.1905 1.4975 1.3303 0.2212  -0.0269 -0.0986 133  CYS C N   
10037 C  CA  . CYS C 133  ? 1.1642 1.4748 1.3068 0.2197  -0.0294 -0.0987 133  CYS C CA  
10038 C  C   . CYS C 133  ? 1.1433 1.4382 1.2822 0.2146  -0.0300 -0.0955 133  CYS C C   
10039 O  O   . CYS C 133  ? 1.1730 1.4714 1.3168 0.2082  -0.0299 -0.0950 133  CYS C O   
10040 C  CB  . CYS C 133  ? 1.0997 1.4084 1.2353 0.2274  -0.0331 -0.0994 133  CYS C CB  
10041 S  SG  . CYS C 133  ? 1.1562 1.4830 1.2956 0.2307  -0.0326 -0.1025 133  CYS C SG  
10042 N  N   . ALA C 134  ? 1.0129 1.2891 1.1426 0.2163  -0.0305 -0.0933 134  ALA C N   
10043 C  CA  . ALA C 134  ? 0.9640 1.2241 1.0899 0.2105  -0.0307 -0.0900 134  ALA C CA  
10044 C  C   . ALA C 134  ? 0.9679 1.2287 1.0993 0.2003  -0.0273 -0.0884 134  ALA C C   
10045 O  O   . ALA C 134  ? 0.9801 1.2317 1.1108 0.1944  -0.0272 -0.0859 134  ALA C O   
10046 C  CB  . ALA C 134  ? 0.8360 1.0767 0.9512 0.2148  -0.0320 -0.0883 134  ALA C CB  
10047 N  N   . GLY C 135  ? 1.1652 1.4360 1.3014 0.1984  -0.0245 -0.0898 135  GLY C N   
10048 C  CA  . GLY C 135  ? 1.1471 1.4175 1.2873 0.1894  -0.0211 -0.0882 135  GLY C CA  
10049 C  C   . GLY C 135  ? 1.1896 1.4712 1.3381 0.1823  -0.0196 -0.0884 135  GLY C C   
10050 O  O   . GLY C 135  ? 1.1972 1.4780 1.3487 0.1747  -0.0166 -0.0870 135  GLY C O   
10051 N  N   . LEU C 136  ? 1.0357 1.3274 1.1877 0.1848  -0.0216 -0.0903 136  LEU C N   
10052 C  CA  . LEU C 136  ? 0.9577 1.2602 1.1177 0.1781  -0.0205 -0.0910 136  LEU C CA  
10053 C  C   . LEU C 136  ? 0.8991 1.1910 1.0563 0.1746  -0.0223 -0.0887 136  LEU C C   
10054 O  O   . LEU C 136  ? 0.9612 1.2555 1.1230 0.1668  -0.0205 -0.0880 136  LEU C O   
10055 C  CB  . LEU C 136  ? 0.9355 1.2567 1.1018 0.1823  -0.0218 -0.0949 136  LEU C CB  
10056 C  CG  . LEU C 136  ? 0.9471 1.2803 1.1163 0.1873  -0.0203 -0.0975 136  LEU C CG  
10057 C  CD1 . LEU C 136  ? 0.9912 1.3398 1.1643 0.1944  -0.0231 -0.1012 136  LEU C CD1 
10058 C  CD2 . LEU C 136  ? 0.8641 1.2068 1.0407 0.1797  -0.0152 -0.0980 136  LEU C CD2 
10059 N  N   . TYR C 137  ? 0.9391 1.2190 1.0887 0.1802  -0.0256 -0.0875 137  TYR C N   
10060 C  CA  . TYR C 137  ? 0.9633 1.2330 1.1099 0.1773  -0.0270 -0.0852 137  TYR C CA  
10061 C  C   . TYR C 137  ? 0.9552 1.2135 1.1010 0.1692  -0.0245 -0.0820 137  TYR C C   
10062 O  O   . TYR C 137  ? 0.9099 1.1673 1.0578 0.1637  -0.0241 -0.0808 137  TYR C O   
10063 C  CB  . TYR C 137  ? 0.9555 1.2134 1.0931 0.1852  -0.0304 -0.0844 137  TYR C CB  
10064 C  CG  . TYR C 137  ? 1.0344 1.3022 1.1722 0.1923  -0.0336 -0.0871 137  TYR C CG  
10065 C  CD1 . TYR C 137  ? 1.0062 1.2792 1.1465 0.1902  -0.0351 -0.0876 137  TYR C CD1 
10066 C  CD2 . TYR C 137  ? 1.0531 1.3251 1.1882 0.2014  -0.0353 -0.0892 137  TYR C CD2 
10067 C  CE1 . TYR C 137  ? 0.9519 1.2344 1.0922 0.1970  -0.0385 -0.0903 137  TYR C CE1 
10068 C  CE2 . TYR C 137  ? 0.9985 1.2801 1.1336 0.2085  -0.0385 -0.0917 137  TYR C CE2 
10069 C  CZ  . TYR C 137  ? 0.8473 1.1343 0.9851 0.2062  -0.0402 -0.0923 137  TYR C CZ  
10070 O  OH  . TYR C 137  ? 0.8222 1.1192 0.9599 0.2136  -0.0437 -0.0950 137  TYR C OH  
10071 N  N   . PRO C 138  ? 1.1357 1.3852 1.2786 0.1683  -0.0229 -0.0805 138  PRO C N   
10072 C  CA  . PRO C 138  ? 1.1381 1.3789 1.2812 0.1606  -0.0206 -0.0776 138  PRO C CA  
10073 C  C   . PRO C 138  ? 1.0779 1.3292 1.2282 0.1532  -0.0174 -0.0781 138  PRO C C   
10074 O  O   . PRO C 138  ? 0.9983 1.2432 1.1490 0.1468  -0.0157 -0.0757 138  PRO C O   
10075 C  CB  . PRO C 138  ? 1.0788 1.3116 1.2179 0.1623  -0.0198 -0.0770 138  PRO C CB  
10076 C  CG  . PRO C 138  ? 1.0921 1.3221 1.2259 0.1711  -0.0226 -0.0783 138  PRO C CG  
10077 C  CD  . PRO C 138  ? 1.1215 1.3664 1.2594 0.1748  -0.0237 -0.0811 138  PRO C CD  
10078 N  N   . ILE C 139  ? 0.8471 1.1141 1.0032 0.1539  -0.0163 -0.0810 139  ILE C N   
10079 C  CA  . ILE C 139  ? 0.8181 1.0953 0.9812 0.1465  -0.0131 -0.0817 139  ILE C CA  
10080 C  C   . ILE C 139  ? 0.8527 1.1379 1.0198 0.1450  -0.0146 -0.0832 139  ILE C C   
10081 O  O   . ILE C 139  ? 0.8670 1.1529 1.0372 0.1379  -0.0128 -0.0825 139  ILE C O   
10082 C  CB  . ILE C 139  ? 0.7882 1.0779 0.9558 0.1471  -0.0103 -0.0840 139  ILE C CB  
10083 C  CG1 . ILE C 139  ? 0.8376 1.1189 1.0000 0.1498  -0.0093 -0.0827 139  ILE C CG1 
10084 C  CG2 . ILE C 139  ? 0.6819 0.9798 0.8559 0.1387  -0.0061 -0.0843 139  ILE C CG2 
10085 C  CD1 . ILE C 139  ? 0.8642 1.1567 1.0300 0.1509  -0.0063 -0.0847 139  ILE C CD1 
10086 N  N   . LEU C 140  ? 0.7637 1.0546 0.9305 0.1518  -0.0181 -0.0854 140  LEU C N   
10087 C  CA  . LEU C 140  ? 0.7426 1.0430 0.9134 0.1509  -0.0200 -0.0875 140  LEU C CA  
10088 C  C   . LEU C 140  ? 0.7325 1.0206 0.8987 0.1486  -0.0216 -0.0850 140  LEU C C   
10089 O  O   . LEU C 140  ? 0.7623 1.0550 0.9320 0.1435  -0.0213 -0.0857 140  LEU C O   
10090 C  CB  . LEU C 140  ? 0.7655 1.0756 0.9365 0.1598  -0.0236 -0.0907 140  LEU C CB  
10091 C  CG  . LEU C 140  ? 0.7533 1.0801 0.9309 0.1620  -0.0221 -0.0940 140  LEU C CG  
10092 C  CD1 . LEU C 140  ? 0.8037 1.1402 0.9814 0.1713  -0.0261 -0.0971 140  LEU C CD1 
10093 C  CD2 . LEU C 140  ? 0.6530 0.9934 0.8401 0.1536  -0.0187 -0.0959 140  LEU C CD2 
10094 N  N   . HIS C 141  ? 0.6251 0.8975 0.7835 0.1520  -0.0230 -0.0822 141  HIS C N   
10095 C  CA  . HIS C 141  ? 0.7277 0.9879 0.8813 0.1504  -0.0242 -0.0796 141  HIS C CA  
10096 C  C   . HIS C 141  ? 0.7058 0.9580 0.8600 0.1420  -0.0210 -0.0767 141  HIS C C   
10097 O  O   . HIS C 141  ? 0.6916 0.9331 0.8420 0.1402  -0.0214 -0.0743 141  HIS C O   
10098 C  CB  . HIS C 141  ? 0.6981 0.9442 0.8431 0.1571  -0.0265 -0.0777 141  HIS C CB  
10099 C  CG  . HIS C 141  ? 0.6651 0.8969 0.8064 0.1545  -0.0246 -0.0745 141  HIS C CG  
10100 N  ND1 . HIS C 141  ? 0.7331 0.9651 0.8752 0.1545  -0.0229 -0.0746 141  HIS C ND1 
10101 C  CD2 . HIS C 141  ? 0.6087 0.8259 0.7457 0.1519  -0.0242 -0.0712 141  HIS C CD2 
10102 C  CE1 . HIS C 141  ? 0.7517 0.9702 0.8902 0.1520  -0.0219 -0.0717 141  HIS C CE1 
10103 N  NE2 . HIS C 141  ? 0.6549 0.8645 0.7907 0.1503  -0.0226 -0.0696 141  HIS C NE2 
10104 N  N   . LEU C 142  ? 0.7872 1.0443 0.9458 0.1372  -0.0176 -0.0769 142  LEU C N   
10105 C  CA  . LEU C 142  ? 0.8309 1.0790 0.9889 0.1304  -0.0146 -0.0739 142  LEU C CA  
10106 C  C   . LEU C 142  ? 0.8869 1.1358 1.0471 0.1242  -0.0136 -0.0735 142  LEU C C   
10107 O  O   . LEU C 142  ? 0.8966 1.1347 1.0541 0.1202  -0.0123 -0.0706 142  LEU C O   
10108 C  CB  . LEU C 142  ? 0.7827 1.0354 0.9437 0.1276  -0.0112 -0.0743 142  LEU C CB  
10109 C  CG  . LEU C 142  ? 0.7938 1.0343 0.9514 0.1245  -0.0092 -0.0710 142  LEU C CG  
10110 C  CD1 . LEU C 142  ? 0.7924 1.0213 0.9441 0.1299  -0.0117 -0.0695 142  LEU C CD1 
10111 C  CD2 . LEU C 142  ? 0.7790 1.0249 0.9390 0.1222  -0.0058 -0.0715 142  LEU C CD2 
10112 N  N   . GLY C 143  ? 1.5190 1.7806 1.6839 0.1234  -0.0144 -0.0766 143  GLY C N   
10113 C  CA  . GLY C 143  ? 1.4872 1.7511 1.6548 0.1168  -0.0131 -0.0769 143  GLY C CA  
10114 C  C   . GLY C 143  ? 1.6161 1.8844 1.7882 0.1093  -0.0086 -0.0770 143  GLY C C   
10115 O  O   . GLY C 143  ? 1.7967 2.0727 1.9731 0.1042  -0.0073 -0.0790 143  GLY C O   
10116 N  N   . ARG C 144  ? 0.7760 1.0386 0.9465 0.1085  -0.0060 -0.0749 144  ARG C N   
10117 C  CA  . ARG C 144  ? 0.7284 0.9954 0.9023 0.1029  -0.0014 -0.0751 144  ARG C CA  
10118 C  C   . ARG C 144  ? 0.7350 1.0062 0.9094 0.1073  -0.0009 -0.0759 144  ARG C C   
10119 O  O   . ARG C 144  ? 0.7485 1.0111 0.9192 0.1076  0.0005  -0.0735 144  ARG C O   
10120 C  CB  . ARG C 144  ? 0.6717 0.9262 0.8421 0.0976  0.0014  -0.0714 144  ARG C CB  
10121 C  CG  . ARG C 144  ? 0.6166 0.8689 0.7873 0.0922  0.0020  -0.0711 144  ARG C CG  
10122 C  CD  . ARG C 144  ? 0.6133 0.8600 0.7831 0.0854  0.0067  -0.0690 144  ARG C CD  
10123 N  NE  . ARG C 144  ? 0.6626 0.8958 0.8271 0.0864  0.0071  -0.0651 144  ARG C NE  
10124 C  CZ  . ARG C 144  ? 0.6469 0.8728 0.8092 0.0819  0.0105  -0.0627 144  ARG C CZ  
10125 N  NH1 . ARG C 144  ? 0.5539 0.7833 0.7180 0.0759  0.0143  -0.0634 144  ARG C NH1 
10126 N  NH2 . ARG C 144  ? 0.5982 0.8131 0.7562 0.0835  0.0103  -0.0595 144  ARG C NH2 
10127 N  N   . PRO C 145  ? 0.5317 0.8162 0.7104 0.1109  -0.0021 -0.0793 145  PRO C N   
10128 C  CA  . PRO C 145  ? 0.5066 0.7940 0.6845 0.1167  -0.0024 -0.0801 145  PRO C CA  
10129 C  C   . PRO C 145  ? 0.4129 0.7010 0.5915 0.1135  0.0022  -0.0794 145  PRO C C   
10130 O  O   . PRO C 145  ? 0.4140 0.6967 0.5887 0.1175  0.0022  -0.0783 145  PRO C O   
10131 C  CB  . PRO C 145  ? 0.4861 0.7893 0.6695 0.1207  -0.0044 -0.0842 145  PRO C CB  
10132 C  CG  . PRO C 145  ? 0.4665 0.7778 0.6553 0.1145  -0.0036 -0.0860 145  PRO C CG  
10133 C  CD  . PRO C 145  ? 0.4510 0.7485 0.6352 0.1106  -0.0038 -0.0829 145  PRO C CD  
10134 N  N   . TRP C 146  ? 0.6446 0.9388 0.8276 0.1066  0.0063  -0.0800 146  TRP C N   
10135 C  CA  . TRP C 146  ? 0.6655 0.9613 0.8489 0.1038  0.0112  -0.0795 146  TRP C CA  
10136 C  C   . TRP C 146  ? 0.6206 0.9012 0.7970 0.1030  0.0124  -0.0756 146  TRP C C   
10137 O  O   . TRP C 146  ? 0.6293 0.9094 0.8045 0.1019  0.0161  -0.0749 146  TRP C O   
10138 C  CB  . TRP C 146  ? 0.6643 0.9686 0.8534 0.0959  0.0156  -0.0809 146  TRP C CB  
10139 C  CG  . TRP C 146  ? 0.6892 0.9850 0.8766 0.0898  0.0163  -0.0790 146  TRP C CG  
10140 C  CD1 . TRP C 146  ? 0.7584 1.0432 0.9415 0.0850  0.0198  -0.0758 146  TRP C CD1 
10141 C  CD2 . TRP C 146  ? 0.6754 0.9724 0.8646 0.0882  0.0133  -0.0801 146  TRP C CD2 
10142 N  NE1 . TRP C 146  ? 0.7734 1.0527 0.9558 0.0805  0.0194  -0.0749 146  TRP C NE1 
10143 C  CE2 . TRP C 146  ? 0.7455 1.0320 0.9316 0.0822  0.0155  -0.0775 146  TRP C CE2 
10144 C  CE3 . TRP C 146  ? 0.7334 1.0392 0.9261 0.0916  0.0091  -0.0830 146  TRP C CE3 
10145 C  CZ2 . TRP C 146  ? 0.7766 1.0609 0.9629 0.0794  0.0136  -0.0778 146  TRP C CZ2 
10146 C  CZ3 . TRP C 146  ? 0.7988 1.1025 0.9916 0.0889  0.0070  -0.0834 146  TRP C CZ3 
10147 C  CH2 . TRP C 146  ? 0.8831 1.1760 1.0726 0.0828  0.0093  -0.0807 146  TRP C CH2 
10148 N  N   . LEU C 147  ? 0.5393 0.8078 0.7113 0.1037  0.0096  -0.0732 147  LEU C N   
10149 C  CA  . LEU C 147  ? 0.5499 0.8048 0.7160 0.1034  0.0102  -0.0698 147  LEU C CA  
10150 C  C   . LEU C 147  ? 0.5054 0.7536 0.6671 0.1102  0.0065  -0.0693 147  LEU C C   
10151 O  O   . LEU C 147  ? 0.4964 0.7326 0.6535 0.1104  0.0055  -0.0667 147  LEU C O   
10152 C  CB  . LEU C 147  ? 0.6500 0.8955 0.8142 0.0989  0.0101  -0.0673 147  LEU C CB  
10153 C  CG  . LEU C 147  ? 0.6322 0.8806 0.7991 0.0915  0.0140  -0.0673 147  LEU C CG  
10154 C  CD1 . LEU C 147  ? 0.6193 0.8581 0.7838 0.0885  0.0130  -0.0651 147  LEU C CD1 
10155 C  CD2 . LEU C 147  ? 0.5345 0.7815 0.6997 0.0883  0.0188  -0.0661 147  LEU C CD2 
10156 N  N   . PHE C 148  ? 0.6365 0.8922 0.7995 0.1159  0.0046  -0.0718 148  PHE C N   
10157 C  CA  . PHE C 148  ? 0.7412 0.9899 0.8995 0.1225  0.0012  -0.0715 148  PHE C CA  
10158 C  C   . PHE C 148  ? 0.7968 1.0384 0.9508 0.1230  0.0026  -0.0701 148  PHE C C   
10159 O  O   . PHE C 148  ? 0.7265 0.9580 0.8759 0.1262  0.0000  -0.0690 148  PHE C O   
10160 C  CB  . PHE C 148  ? 0.7189 0.9776 0.8791 0.1287  -0.0008 -0.0746 148  PHE C CB  
10161 C  CG  . PHE C 148  ? 0.7659 1.0352 0.9288 0.1294  0.0024  -0.0766 148  PHE C CG  
10162 C  CD1 . PHE C 148  ? 0.8745 1.1567 1.0440 0.1252  0.0055  -0.0784 148  PHE C CD1 
10163 C  CD2 . PHE C 148  ? 0.6678 0.9340 0.8266 0.1342  0.0023  -0.0768 148  PHE C CD2 
10164 C  CE1 . PHE C 148  ? 0.8439 1.1360 1.0160 0.1257  0.0089  -0.0801 148  PHE C CE1 
10165 C  CE2 . PHE C 148  ? 0.6327 0.9084 0.7935 0.1351  0.0055  -0.0785 148  PHE C CE2 
10166 C  CZ  . PHE C 148  ? 0.7136 1.0024 0.8812 0.1308  0.0090  -0.0800 148  PHE C CZ  
10167 N  N   . TYR C 149  ? 0.7873 1.0339 0.9425 0.1200  0.0068  -0.0702 149  TYR C N   
10168 C  CA  . TYR C 149  ? 0.7140 0.9542 0.8644 0.1209  0.0083  -0.0690 149  TYR C CA  
10169 C  C   . TYR C 149  ? 0.7814 1.0088 0.9280 0.1179  0.0078  -0.0659 149  TYR C C   
10170 O  O   . TYR C 149  ? 0.8582 1.0790 1.0003 0.1193  0.0080  -0.0649 149  TYR C O   
10171 C  CB  . TYR C 149  ? 0.7387 0.9869 0.8909 0.1182  0.0134  -0.0696 149  TYR C CB  
10172 C  CG  . TYR C 149  ? 0.6969 0.9463 0.8516 0.1107  0.0173  -0.0684 149  TYR C CG  
10173 C  CD1 . TYR C 149  ? 0.6955 0.9551 0.8566 0.1073  0.0185  -0.0701 149  TYR C CD1 
10174 C  CD2 . TYR C 149  ? 0.6747 0.9149 0.8252 0.1073  0.0196  -0.0656 149  TYR C CD2 
10175 C  CE1 . TYR C 149  ? 0.6853 0.9452 0.8483 0.1003  0.0221  -0.0692 149  TYR C CE1 
10176 C  CE2 . TYR C 149  ? 0.7761 1.0163 0.9280 0.1007  0.0233  -0.0644 149  TYR C CE2 
10177 C  CZ  . TYR C 149  ? 0.7507 1.0003 0.9087 0.0970  0.0247  -0.0662 149  TYR C CZ  
10178 O  OH  . TYR C 149  ? 0.7169 0.9658 0.8760 0.0902  0.0285  -0.0652 149  TYR C OH  
10179 N  N   . TRP C 150  ? 0.7808 1.0048 0.9290 0.1142  0.0072  -0.0645 150  TRP C N   
10180 C  CA  . TRP C 150  ? 0.7837 0.9961 0.9287 0.1119  0.0066  -0.0617 150  TRP C CA  
10181 C  C   . TRP C 150  ? 0.7567 0.9604 0.8984 0.1164  0.0024  -0.0613 150  TRP C C   
10182 O  O   . TRP C 150  ? 0.7521 0.9468 0.8910 0.1155  0.0017  -0.0594 150  TRP C O   
10183 C  CB  . TRP C 150  ? 0.7452 0.9563 0.8926 0.1071  0.0071  -0.0604 150  TRP C CB  
10184 C  CG  . TRP C 150  ? 0.7611 0.9743 0.9094 0.1014  0.0117  -0.0594 150  TRP C CG  
10185 C  CD1 . TRP C 150  ? 0.7955 1.0111 0.9425 0.1001  0.0154  -0.0594 150  TRP C CD1 
10186 C  CD2 . TRP C 150  ? 0.7438 0.9560 0.8937 0.0961  0.0132  -0.0583 150  TRP C CD2 
10187 N  NE1 . TRP C 150  ? 0.8425 1.0582 0.9901 0.0943  0.0193  -0.0583 150  TRP C NE1 
10188 C  CE2 . TRP C 150  ? 0.7889 1.0026 0.9384 0.0917  0.0180  -0.0577 150  TRP C CE2 
10189 C  CE3 . TRP C 150  ? 0.8174 1.0270 0.9686 0.0948  0.0113  -0.0578 150  TRP C CE3 
10190 C  CZ2 . TRP C 150  ? 0.7527 0.9652 0.9030 0.0860  0.0207  -0.0567 150  TRP C CZ2 
10191 C  CZ3 . TRP C 150  ? 0.7649 0.9737 0.9170 0.0893  0.0138  -0.0569 150  TRP C CZ3 
10192 C  CH2 . TRP C 150  ? 0.7636 0.9737 0.9152 0.0849  0.0184  -0.0564 150  TRP C CH2 
10193 N  N   . LEU C 151  ? 0.7481 0.9544 0.8901 0.1212  -0.0004 -0.0632 151  LEU C N   
10194 C  CA  . LEU C 151  ? 0.7680 0.9657 0.9063 0.1255  -0.0040 -0.0633 151  LEU C CA  
10195 C  C   . LEU C 151  ? 0.8082 1.0041 0.9428 0.1287  -0.0042 -0.0642 151  LEU C C   
10196 O  O   . LEU C 151  ? 0.9691 1.1568 1.1003 0.1317  -0.0070 -0.0642 151  LEU C O   
10197 C  CB  . LEU C 151  ? 0.8390 1.0391 0.9777 0.1300  -0.0068 -0.0650 151  LEU C CB  
10198 C  CG  . LEU C 151  ? 0.6600 0.8570 0.7999 0.1286  -0.0082 -0.0639 151  LEU C CG  
10199 C  CD1 . LEU C 151  ? 0.6715 0.8785 0.8160 0.1253  -0.0063 -0.0645 151  LEU C CD1 
10200 C  CD2 . LEU C 151  ? 0.6935 0.8870 0.8307 0.1343  -0.0116 -0.0650 151  LEU C CD2 
10201 N  N   . ILE C 152  ? 0.7593 0.9622 0.8943 0.1282  -0.0010 -0.0649 152  ILE C N   
10202 C  CA  . ILE C 152  ? 0.7455 0.9472 0.8764 0.1315  -0.0008 -0.0658 152  ILE C CA  
10203 C  C   . ILE C 152  ? 0.7625 0.9587 0.8908 0.1281  0.0011  -0.0638 152  ILE C C   
10204 O  O   . ILE C 152  ? 0.8751 1.0739 1.0054 0.1234  0.0043  -0.0623 152  ILE C O   
10205 C  CB  . ILE C 152  ? 0.6084 0.8214 0.7407 0.1337  0.0019  -0.0679 152  ILE C CB  
10206 C  CG1 . ILE C 152  ? 0.6788 0.8986 0.8142 0.1372  0.0000  -0.0700 152  ILE C CG1 
10207 C  CG2 . ILE C 152  ? 0.6433 0.8544 0.7706 0.1378  0.0021  -0.0689 152  ILE C CG2 
10208 C  CD1 . ILE C 152  ? 0.6043 0.8372 0.7427 0.1390  0.0028  -0.0723 152  ILE C CD1 
10209 N  N   . PRO C 153  ? 0.9461 1.1346 1.0698 0.1305  -0.0010 -0.0637 153  PRO C N   
10210 C  CA  . PRO C 153  ? 1.0170 1.2007 1.1377 0.1281  0.0005  -0.0620 153  PRO C CA  
10211 C  C   . PRO C 153  ? 0.9689 1.1583 1.0876 0.1279  0.0049  -0.0621 153  PRO C C   
10212 O  O   . PRO C 153  ? 0.9672 1.1567 1.0818 0.1318  0.0048  -0.0635 153  PRO C O   
10213 C  CB  . PRO C 153  ? 0.9760 1.1512 1.0924 0.1315  -0.0035 -0.0627 153  PRO C CB  
10214 C  CG  . PRO C 153  ? 0.9631 1.1399 1.0788 0.1364  -0.0057 -0.0652 153  PRO C CG  
10215 C  CD  . PRO C 153  ? 0.9677 1.1507 1.0883 0.1355  -0.0050 -0.0654 153  PRO C CD  
10216 N  N   . TYR C 154  ? 0.7821 0.9758 0.9035 0.1232  0.0089  -0.0607 154  TYR C N   
10217 C  CA  . TYR C 154  ? 0.7570 0.9557 0.8767 0.1220  0.0139  -0.0606 154  TYR C CA  
10218 C  C   . TYR C 154  ? 0.8469 1.0402 0.9640 0.1179  0.0167  -0.0579 154  TYR C C   
10219 O  O   . TYR C 154  ? 0.8988 1.0880 1.0177 0.1146  0.0159  -0.0562 154  TYR C O   
10220 C  CB  . TYR C 154  ? 0.7076 0.9175 0.8331 0.1199  0.0170  -0.0619 154  TYR C CB  
10221 C  CG  . TYR C 154  ? 0.7697 0.9809 0.8995 0.1139  0.0189  -0.0605 154  TYR C CG  
10222 C  CD1 . TYR C 154  ? 0.7527 0.9619 0.8858 0.1129  0.0155  -0.0603 154  TYR C CD1 
10223 C  CD2 . TYR C 154  ? 0.8909 1.1048 1.0210 0.1092  0.0243  -0.0595 154  TYR C CD2 
10224 C  CE1 . TYR C 154  ? 0.7615 0.9715 0.8979 0.1076  0.0172  -0.0591 154  TYR C CE1 
10225 C  CE2 . TYR C 154  ? 0.9092 1.1235 1.0426 0.1036  0.0260  -0.0584 154  TYR C CE2 
10226 C  CZ  . TYR C 154  ? 0.8363 1.0489 0.9729 0.1029  0.0223  -0.0583 154  TYR C CZ  
10227 O  OH  . TYR C 154  ? 0.8785 1.0911 1.0179 0.0975  0.0240  -0.0573 154  TYR C OH  
10228 N  N   . PRO C 155  ? 0.6520 0.8445 0.7640 0.1184  0.0202  -0.0573 155  PRO C N   
10229 C  CA  . PRO C 155  ? 0.5973 0.7840 0.7056 0.1150  0.0233  -0.0545 155  PRO C CA  
10230 C  C   . PRO C 155  ? 0.5614 0.7522 0.6741 0.1090  0.0274  -0.0535 155  PRO C C   
10231 O  O   . PRO C 155  ? 0.6355 0.8344 0.7511 0.1073  0.0312  -0.0547 155  PRO C O   
10232 C  CB  . PRO C 155  ? 0.5910 0.7771 0.6925 0.1176  0.0266  -0.0545 155  PRO C CB  
10233 C  CG  . PRO C 155  ? 0.5705 0.7597 0.6714 0.1232  0.0236  -0.0572 155  PRO C CG  
10234 C  CD  . PRO C 155  ? 0.6027 0.7989 0.7112 0.1226  0.0217  -0.0590 155  PRO C CD  
10235 N  N   . ASN C 156  ? 0.7274 0.9125 0.8407 0.1058  0.0267  -0.0515 156  ASN C N   
10236 C  CA  . ASN C 156  ? 0.8282 1.0157 0.9454 0.1000  0.0300  -0.0507 156  ASN C CA  
10237 C  C   . ASN C 156  ? 0.8161 0.9955 0.9282 0.0971  0.0330  -0.0477 156  ASN C C   
10238 O  O   . ASN C 156  ? 0.7773 0.9493 0.8840 0.0998  0.0315  -0.0462 156  ASN C O   
10239 C  CB  . ASN C 156  ? 0.8778 1.0665 1.0008 0.0989  0.0261  -0.0512 156  ASN C CB  
10240 C  CG  . ASN C 156  ? 0.8395 1.0202 0.9610 0.1014  0.0212  -0.0502 156  ASN C CG  
10241 O  OD1 . ASN C 156  ? 0.8354 1.0097 0.9519 0.1034  0.0206  -0.0489 156  ASN C OD1 
10242 N  ND2 . ASN C 156  ? 0.8856 1.0666 1.0114 0.1013  0.0178  -0.0507 156  ASN C ND2 
10243 N  N   . THR C 157  ? 0.8355 1.0164 0.9494 0.0916  0.0372  -0.0470 157  THR C N   
10244 C  CA  . THR C 157  ? 0.7336 0.9064 0.8427 0.0885  0.0406  -0.0441 157  THR C CA  
10245 C  C   . THR C 157  ? 0.7883 0.9545 0.8980 0.0881  0.0371  -0.0424 157  THR C C   
10246 O  O   . THR C 157  ? 0.7515 0.9106 0.8572 0.0859  0.0395  -0.0400 157  THR C O   
10247 C  CB  . THR C 157  ? 0.8303 1.0067 0.9412 0.0824  0.0465  -0.0442 157  THR C CB  
10248 O  OG1 . THR C 157  ? 0.9796 1.1588 1.0967 0.0789  0.0449  -0.0450 157  THR C OG1 
10249 C  CG2 . THR C 157  ? 0.7163 0.9022 0.8295 0.0824  0.0496  -0.0465 157  THR C CG2 
10250 N  N   . HIS C 158  ? 0.8674 1.0354 0.9817 0.0902  0.0318  -0.0436 158  HIS C N   
10251 C  CA  . HIS C 158  ? 0.8091 0.9718 0.9249 0.0896  0.0287  -0.0422 158  HIS C CA  
10252 C  C   . HIS C 158  ? 0.7483 0.9055 0.8618 0.0941  0.0243  -0.0416 158  HIS C C   
10253 O  O   . HIS C 158  ? 0.7226 0.8732 0.8340 0.0939  0.0238  -0.0395 158  HIS C O   
10254 C  CB  . HIS C 158  ? 0.6081 0.7760 0.7306 0.0884  0.0262  -0.0439 158  HIS C CB  
10255 C  CG  . HIS C 158  ? 0.5610 0.7368 0.6870 0.0849  0.0294  -0.0455 158  HIS C CG  
10256 N  ND1 . HIS C 158  ? 0.5594 0.7441 0.6900 0.0864  0.0278  -0.0483 158  HIS C ND1 
10257 C  CD2 . HIS C 158  ? 0.5885 0.7648 0.7142 0.0798  0.0341  -0.0450 158  HIS C CD2 
10258 C  CE1 . HIS C 158  ? 0.6780 0.8693 0.8117 0.0824  0.0312  -0.0496 158  HIS C CE1 
10259 N  NE2 . HIS C 158  ? 0.6652 0.8514 0.7960 0.0780  0.0352  -0.0476 158  HIS C NE2 
10260 N  N   . GLY C 159  ? 0.8830 1.0431 0.9972 0.0981  0.0211  -0.0436 159  GLY C N   
10261 C  CA  . GLY C 159  ? 0.9142 1.0698 1.0273 0.1019  0.0164  -0.0437 159  GLY C CA  
10262 C  C   . GLY C 159  ? 0.9177 1.0738 1.0361 0.1026  0.0121  -0.0447 159  GLY C C   
10263 O  O   . GLY C 159  ? 0.8714 1.0227 0.9901 0.1040  0.0087  -0.0442 159  GLY C O   
10264 N  N   . MET C 160  ? 1.1053 1.2669 1.2278 0.1016  0.0121  -0.0462 160  MET C N   
10265 C  CA  . MET C 160  ? 1.1329 1.2944 1.2596 0.1024  0.0085  -0.0470 160  MET C CA  
10266 C  C   . MET C 160  ? 1.1183 1.2823 1.2450 0.1067  0.0055  -0.0496 160  MET C C   
10267 O  O   . MET C 160  ? 1.1929 1.3621 1.3184 0.1083  0.0070  -0.0511 160  MET C O   
10268 C  CB  . MET C 160  ? 1.0672 1.2330 1.1977 0.0991  0.0101  -0.0471 160  MET C CB  
10269 C  CG  . MET C 160  ? 0.9982 1.1594 1.1292 0.0953  0.0116  -0.0447 160  MET C CG  
10270 S  SD  . MET C 160  ? 1.1402 1.2934 1.2718 0.0965  0.0079  -0.0432 160  MET C SD  
10271 C  CE  . MET C 160  ? 1.0690 1.2240 1.2040 0.0989  0.0042  -0.0451 160  MET C CE  
10272 N  N   . TRP C 161  ? 0.8139 0.9737 0.9418 0.1086  0.0015  -0.0500 161  TRP C N   
10273 C  CA  . TRP C 161  ? 0.8572 1.0175 0.9846 0.1128  -0.0016 -0.0524 161  TRP C CA  
10274 C  C   . TRP C 161  ? 0.8577 1.0185 0.9884 0.1131  -0.0034 -0.0530 161  TRP C C   
10275 O  O   . TRP C 161  ? 0.9752 1.1336 1.1081 0.1104  -0.0032 -0.0514 161  TRP C O   
10276 C  CB  . TRP C 161  ? 1.0234 1.1772 1.1487 0.1150  -0.0049 -0.0527 161  TRP C CB  
10277 C  CG  . TRP C 161  ? 0.9460 1.0985 1.0672 0.1156  -0.0040 -0.0522 161  TRP C CG  
10278 C  CD1 . TRP C 161  ? 0.9568 1.1072 1.0770 0.1131  -0.0019 -0.0499 161  TRP C CD1 
10279 C  CD2 . TRP C 161  ? 0.9525 1.1052 1.0693 0.1194  -0.0050 -0.0540 161  TRP C CD2 
10280 N  NE1 . TRP C 161  ? 1.0835 1.2327 1.1987 0.1153  -0.0017 -0.0502 161  TRP C NE1 
10281 C  CE2 . TRP C 161  ? 0.9843 1.1349 1.0974 0.1190  -0.0036 -0.0527 161  TRP C CE2 
10282 C  CE3 . TRP C 161  ? 0.9073 1.0612 1.0224 0.1233  -0.0070 -0.0566 161  TRP C CE3 
10283 C  CZ2 . TRP C 161  ? 0.9140 1.0639 1.0216 0.1225  -0.0041 -0.0539 161  TRP C CZ2 
10284 C  CZ3 . TRP C 161  ? 0.9875 1.1407 1.0974 0.1266  -0.0074 -0.0579 161  TRP C CZ3 
10285 C  CH2 . TRP C 161  ? 0.9686 1.1199 1.0748 0.1261  -0.0061 -0.0565 161  TRP C CH2 
10286 N  N   . PRO C 162  ? 0.6202 0.7836 0.7504 0.1168  -0.0051 -0.0552 162  PRO C N   
10287 C  CA  . PRO C 162  ? 0.5906 0.7522 0.7224 0.1182  -0.0074 -0.0558 162  PRO C CA  
10288 C  C   . PRO C 162  ? 0.6845 0.8369 0.8160 0.1182  -0.0101 -0.0550 162  PRO C C   
10289 O  O   . PRO C 162  ? 0.7395 0.8879 0.8694 0.1183  -0.0111 -0.0549 162  PRO C O   
10290 C  CB  . PRO C 162  ? 0.6190 0.7846 0.7492 0.1230  -0.0086 -0.0585 162  PRO C CB  
10291 C  CG  . PRO C 162  ? 0.6085 0.7810 0.7379 0.1230  -0.0057 -0.0591 162  PRO C CG  
10292 C  CD  . PRO C 162  ? 0.6753 0.8437 0.8032 0.1201  -0.0045 -0.0573 162  PRO C CD  
10293 N  N   . GLN C 163  ? 1.1168 1.2658 1.2496 0.1181  -0.0113 -0.0545 163  GLN C N   
10294 C  CA  . GLN C 163  ? 1.1622 1.3026 1.2954 0.1173  -0.0132 -0.0536 163  GLN C CA  
10295 C  C   . GLN C 163  ? 1.1731 1.3087 1.3038 0.1207  -0.0161 -0.0556 163  GLN C C   
10296 O  O   . GLN C 163  ? 1.3017 1.4317 1.4327 0.1197  -0.0176 -0.0555 163  GLN C O   
10297 C  CB  . GLN C 163  ? 1.0475 1.1849 1.1821 0.1163  -0.0132 -0.0524 163  GLN C CB  
10298 C  CG  . GLN C 163  ? 1.0664 1.1952 1.2020 0.1148  -0.0143 -0.0511 163  GLN C CG  
10299 C  CD  . GLN C 163  ? 1.1906 1.3154 1.3266 0.1144  -0.0141 -0.0499 163  GLN C CD  
10300 O  OE1 . GLN C 163  ? 1.2369 1.3548 1.3739 0.1129  -0.0144 -0.0487 163  GLN C OE1 
10301 N  NE2 . GLN C 163  ? 1.2547 1.3840 1.3898 0.1158  -0.0134 -0.0502 163  GLN C NE2 
10302 N  N   . PHE C 164  ? 0.8407 0.9785 0.9690 0.1247  -0.0171 -0.0577 164  PHE C N   
10303 C  CA  . PHE C 164  ? 0.8876 1.0204 1.0126 0.1284  -0.0197 -0.0599 164  PHE C CA  
10304 C  C   . PHE C 164  ? 0.7687 0.8920 0.8936 0.1281  -0.0216 -0.0596 164  PHE C C   
10305 O  O   . PHE C 164  ? 0.7461 0.8640 0.8679 0.1310  -0.0237 -0.0615 164  PHE C O   
10306 C  CB  . PHE C 164  ? 0.8863 1.0188 1.0097 0.1285  -0.0205 -0.0609 164  PHE C CB  
10307 C  CG  . PHE C 164  ? 0.8850 1.0255 1.0070 0.1299  -0.0186 -0.0615 164  PHE C CG  
10308 C  CD1 . PHE C 164  ? 0.9621 1.1085 1.0830 0.1332  -0.0177 -0.0629 164  PHE C CD1 
10309 C  CD2 . PHE C 164  ? 0.7783 0.9207 0.9000 0.1281  -0.0174 -0.0608 164  PHE C CD2 
10310 C  CE1 . PHE C 164  ? 1.0093 1.1634 1.1294 0.1341  -0.0155 -0.0635 164  PHE C CE1 
10311 C  CE2 . PHE C 164  ? 0.9036 1.0525 1.0233 0.1292  -0.0150 -0.0612 164  PHE C CE2 
10312 C  CZ  . PHE C 164  ? 0.9681 1.1230 1.0874 0.1320  -0.0139 -0.0626 164  PHE C CZ  
10313 N  N   . ARG C 165  ? 0.6935 0.8142 0.8214 0.1245  -0.0206 -0.0573 165  ARG C N   
10314 C  CA  . ARG C 165  ? 0.6414 0.7533 0.7693 0.1239  -0.0215 -0.0567 165  ARG C CA  
10315 C  C   . ARG C 165  ? 0.6531 0.7642 0.7795 0.1259  -0.0208 -0.0561 165  ARG C C   
10316 O  O   . ARG C 165  ? 0.5599 0.6628 0.6850 0.1261  -0.0213 -0.0556 165  ARG C O   
10317 C  CB  . ARG C 165  ? 0.6252 0.7342 0.7572 0.1191  -0.0206 -0.0545 165  ARG C CB  
10318 C  CG  . ARG C 165  ? 0.7949 0.9067 0.9287 0.1172  -0.0210 -0.0547 165  ARG C CG  
10319 C  CD  . ARG C 165  ? 0.7003 0.8087 0.8382 0.1132  -0.0206 -0.0529 165  ARG C CD  
10320 N  NE  . ARG C 165  ? 0.6398 0.7533 0.7795 0.1113  -0.0194 -0.0518 165  ARG C NE  
10321 C  CZ  . ARG C 165  ? 0.6797 0.7920 0.8225 0.1088  -0.0198 -0.0510 165  ARG C CZ  
10322 N  NH1 . ARG C 165  ? 0.5748 0.6816 0.7203 0.1074  -0.0212 -0.0513 165  ARG C NH1 
10323 N  NH2 . ARG C 165  ? 0.7101 0.8267 0.8532 0.1078  -0.0186 -0.0498 165  ARG C NH2 
10324 N  N   . SER C 166  ? 0.7811 0.9005 0.9075 0.1272  -0.0197 -0.0562 166  SER C N   
10325 C  CA  . SER C 166  ? 0.7514 0.8713 0.8757 0.1302  -0.0197 -0.0562 166  SER C CA  
10326 C  C   . SER C 166  ? 0.8386 0.9593 0.9589 0.1359  -0.0214 -0.0588 166  SER C C   
10327 O  O   . SER C 166  ? 0.9311 1.0542 1.0506 0.1374  -0.0221 -0.0605 166  SER C O   
10328 C  CB  . SER C 166  ? 0.8157 0.9449 0.9427 0.1286  -0.0178 -0.0554 166  SER C CB  
10329 O  OG  . SER C 166  ? 0.7985 0.9373 0.9256 0.1308  -0.0177 -0.0574 166  SER C OG  
10330 N  N   . ALA C 167  ? 0.7552 0.8737 0.8725 0.1396  -0.0220 -0.0590 167  ALA C N   
10331 C  CA  . ALA C 167  ? 0.6453 0.7641 0.7582 0.1458  -0.0236 -0.0613 167  ALA C CA  
10332 C  C   . ALA C 167  ? 0.7007 0.8326 0.8151 0.1483  -0.0231 -0.0629 167  ALA C C   
10333 O  O   . ALA C 167  ? 0.8483 0.9825 0.9598 0.1535  -0.0242 -0.0651 167  ALA C O   
10334 C  CB  . ALA C 167  ? 0.6704 0.7805 0.7785 0.1494  -0.0244 -0.0609 167  ALA C CB  
10335 N  N   . LEU C 168  ? 1.0478 1.1884 1.1668 0.1448  -0.0214 -0.0619 168  LEU C N   
10336 C  CA  . LEU C 168  ? 1.1653 1.3190 1.2867 0.1464  -0.0206 -0.0636 168  LEU C CA  
10337 C  C   . LEU C 168  ? 1.1660 1.3246 1.2886 0.1453  -0.0195 -0.0646 168  LEU C C   
10338 O  O   . LEU C 168  ? 1.2674 1.4351 1.3906 0.1482  -0.0191 -0.0666 168  LEU C O   
10339 C  CB  . LEU C 168  ? 1.1593 1.3202 1.2849 0.1426  -0.0190 -0.0625 168  LEU C CB  
10340 C  CG  . LEU C 168  ? 1.0766 1.2340 1.2005 0.1441  -0.0201 -0.0617 168  LEU C CG  
10341 C  CD1 . LEU C 168  ? 0.9116 1.0789 1.0395 0.1414  -0.0189 -0.0617 168  LEU C CD1 
10342 C  CD2 . LEU C 168  ? 1.0053 1.1610 1.1244 0.1514  -0.0223 -0.0634 168  LEU C CD2 
10343 N  N   . ALA C 169  ? 0.8512 1.0041 0.9743 0.1415  -0.0191 -0.0634 169  ALA C N   
10344 C  CA  . ALA C 169  ? 0.8807 1.0364 1.0034 0.1413  -0.0184 -0.0644 169  ALA C CA  
10345 C  C   . ALA C 169  ? 0.9903 1.1418 1.1083 0.1467  -0.0205 -0.0666 169  ALA C C   
10346 O  O   . ALA C 169  ? 0.9946 1.1521 1.1116 0.1493  -0.0199 -0.0683 169  ALA C O   
10347 C  CB  . ALA C 169  ? 0.9174 1.0679 1.0414 0.1363  -0.0179 -0.0626 169  ALA C CB  
10348 N  N   . TRP C 170  ? 0.7033 0.8441 0.8181 0.1483  -0.0227 -0.0666 170  TRP C N   
10349 C  CA  . TRP C 170  ? 0.6729 0.8087 0.7823 0.1539  -0.0246 -0.0688 170  TRP C CA  
10350 C  C   . TRP C 170  ? 0.7175 0.8612 0.8258 0.1594  -0.0245 -0.0704 170  TRP C C   
10351 O  O   . TRP C 170  ? 0.8203 0.9659 0.9253 0.1641  -0.0251 -0.0726 170  TRP C O   
10352 C  CB  . TRP C 170  ? 0.6006 0.7232 0.7067 0.1543  -0.0265 -0.0684 170  TRP C CB  
10353 C  CG  . TRP C 170  ? 0.5853 0.7008 0.6938 0.1487  -0.0265 -0.0667 170  TRP C CG  
10354 C  CD1 . TRP C 170  ? 0.5608 0.6786 0.6723 0.1445  -0.0259 -0.0662 170  TRP C CD1 
10355 C  CD2 . TRP C 170  ? 0.6368 0.7418 0.7447 0.1467  -0.0270 -0.0653 170  TRP C CD2 
10356 N  NE1 . TRP C 170  ? 0.5059 0.6163 0.6194 0.1402  -0.0263 -0.0647 170  TRP C NE1 
10357 C  CE2 . TRP C 170  ? 0.6107 0.7132 0.7224 0.1412  -0.0267 -0.0642 170  TRP C CE2 
10358 C  CE3 . TRP C 170  ? 0.5480 0.6453 0.6523 0.1493  -0.0274 -0.0649 170  TRP C CE3 
10359 C  CZ2 . TRP C 170  ? 0.5969 0.6904 0.7097 0.1380  -0.0268 -0.0627 170  TRP C CZ2 
10360 C  CZ3 . TRP C 170  ? 0.4715 0.5589 0.5762 0.1459  -0.0272 -0.0633 170  TRP C CZ3 
10361 C  CH2 . TRP C 170  ? 0.5434 0.6292 0.6527 0.1402  -0.0268 -0.0623 170  TRP C CH2 
10362 N  N   . ASP C 171  ? 1.2882 1.4369 1.3990 0.1592  -0.0239 -0.0695 171  ASP C N   
10363 C  CA  . ASP C 171  ? 1.3859 1.5427 1.4960 0.1647  -0.0242 -0.0712 171  ASP C CA  
10364 C  C   . ASP C 171  ? 1.3280 1.4982 1.4414 0.1651  -0.0224 -0.0728 171  ASP C C   
10365 O  O   . ASP C 171  ? 1.3696 1.5453 1.4813 0.1708  -0.0227 -0.0749 171  ASP C O   
10366 C  CB  . ASP C 171  ? 1.5636 1.7228 1.6758 0.1639  -0.0242 -0.0700 171  ASP C CB  
10367 C  CG  . ASP C 171  ? 1.7349 1.9011 1.8457 0.1705  -0.0253 -0.0719 171  ASP C CG  
10368 O  OD1 . ASP C 171  ? 1.8229 1.9905 1.9306 0.1760  -0.0260 -0.0739 171  ASP C OD1 
10369 O  OD2 . ASP C 171  ? 1.6805 1.8507 1.7930 0.1704  -0.0255 -0.0713 171  ASP C OD2 
10370 N  N   . VAL C 172  ? 0.9630 1.1382 1.0809 0.1592  -0.0201 -0.0716 172  VAL C N   
10371 C  CA  . VAL C 172  ? 1.0015 1.1886 1.1224 0.1589  -0.0177 -0.0728 172  VAL C CA  
10372 C  C   . VAL C 172  ? 1.0344 1.2189 1.1509 0.1625  -0.0179 -0.0744 172  VAL C C   
10373 O  O   . VAL C 172  ? 1.0158 1.2084 1.1320 0.1667  -0.0171 -0.0764 172  VAL C O   
10374 C  CB  . VAL C 172  ? 0.9838 1.1744 1.1091 0.1516  -0.0149 -0.0710 172  VAL C CB  
10375 C  CG1 . VAL C 172  ? 1.0240 1.2231 1.1507 0.1510  -0.0120 -0.0719 172  VAL C CG1 
10376 C  CG2 . VAL C 172  ? 0.9773 1.1739 1.1073 0.1487  -0.0142 -0.0702 172  VAL C CG2 
10377 N  N   . PHE C 173  ? 0.9834 1.1567 1.0964 0.1611  -0.0192 -0.0737 173  PHE C N   
10378 C  CA  . PHE C 173  ? 0.8612 1.0308 0.9693 0.1646  -0.0200 -0.0753 173  PHE C CA  
10379 C  C   . PHE C 173  ? 0.9486 1.1151 1.0518 0.1719  -0.0220 -0.0775 173  PHE C C   
10380 O  O   . PHE C 173  ? 0.9830 1.1516 1.0828 0.1763  -0.0219 -0.0795 173  PHE C O   
10381 C  CB  . PHE C 173  ? 0.8248 0.9831 0.9306 0.1614  -0.0214 -0.0744 173  PHE C CB  
10382 C  CG  . PHE C 173  ? 0.8750 1.0363 0.9826 0.1570  -0.0194 -0.0733 173  PHE C CG  
10383 C  CD1 . PHE C 173  ? 0.9882 1.1537 1.1009 0.1514  -0.0173 -0.0711 173  PHE C CD1 
10384 C  CD2 . PHE C 173  ? 0.9085 1.0677 1.0120 0.1587  -0.0196 -0.0745 173  PHE C CD2 
10385 C  CE1 . PHE C 173  ? 0.9760 1.1433 1.0894 0.1478  -0.0152 -0.0699 173  PHE C CE1 
10386 C  CE2 . PHE C 173  ? 0.8324 0.9937 0.9366 0.1552  -0.0178 -0.0734 173  PHE C CE2 
10387 C  CZ  . PHE C 173  ? 0.9041 1.0693 1.0131 0.1498  -0.0155 -0.0710 173  PHE C CZ  
10388 N  N   . ALA C 174  ? 0.7437 0.9047 0.8458 0.1735  -0.0239 -0.0771 174  ALA C N   
10389 C  CA  . ALA C 174  ? 0.7032 0.8592 0.7994 0.1807  -0.0259 -0.0789 174  ALA C CA  
10390 C  C   . ALA C 174  ? 0.6961 0.8650 0.7937 0.1860  -0.0249 -0.0806 174  ALA C C   
10391 O  O   . ALA C 174  ? 0.7261 0.8954 0.8194 0.1920  -0.0253 -0.0828 174  ALA C O   
10392 C  CB  . ALA C 174  ? 0.7056 0.8513 0.7996 0.1809  -0.0277 -0.0777 174  ALA C CB  
10393 N  N   . ILE C 175  ? 0.8730 1.0526 0.9766 0.1841  -0.0236 -0.0800 175  ILE C N   
10394 C  CA  . ILE C 175  ? 0.8515 1.0450 0.9577 0.1888  -0.0228 -0.0819 175  ILE C CA  
10395 C  C   . ILE C 175  ? 0.9128 1.1155 1.0206 0.1890  -0.0202 -0.0833 175  ILE C C   
10396 O  O   . ILE C 175  ? 0.9450 1.1541 1.0514 0.1952  -0.0199 -0.0855 175  ILE C O   
10397 C  CB  . ILE C 175  ? 0.7999 1.0033 0.9127 0.1857  -0.0221 -0.0812 175  ILE C CB  
10398 C  CG1 . ILE C 175  ? 0.8859 1.0800 0.9959 0.1866  -0.0245 -0.0798 175  ILE C CG1 
10399 C  CG2 . ILE C 175  ? 0.6285 0.8480 0.7452 0.1900  -0.0212 -0.0836 175  ILE C CG2 
10400 C  CD1 . ILE C 175  ? 1.0467 1.2475 1.1626 0.1819  -0.0239 -0.0787 175  ILE C CD1 
10401 N  N   . SER C 176  ? 0.8067 1.0099 0.9172 0.1826  -0.0180 -0.0819 176  SER C N   
10402 C  CA  . SER C 176  ? 0.7229 0.9336 0.8341 0.1826  -0.0151 -0.0829 176  SER C CA  
10403 C  C   . SER C 176  ? 0.8007 1.0043 0.9044 0.1885  -0.0164 -0.0846 176  SER C C   
10404 O  O   . SER C 176  ? 0.7408 0.9522 0.8437 0.1930  -0.0148 -0.0865 176  SER C O   
10405 C  CB  . SER C 176  ? 0.7245 0.9341 0.8382 0.1749  -0.0129 -0.0808 176  SER C CB  
10406 O  OG  . SER C 176  ? 0.8054 1.0217 0.9257 0.1695  -0.0114 -0.0795 176  SER C OG  
10407 N  N   . THR C 177  ? 0.8672 1.0559 0.9652 0.1885  -0.0191 -0.0841 177  THR C N   
10408 C  CA  . THR C 177  ? 0.8581 1.0387 0.9484 0.1939  -0.0207 -0.0859 177  THR C CA  
10409 C  C   . THR C 177  ? 0.8856 1.0671 0.9724 0.2020  -0.0221 -0.0879 177  THR C C   
10410 O  O   . THR C 177  ? 0.9832 1.1665 1.0658 0.2078  -0.0217 -0.0900 177  THR C O   
10411 C  CB  . THR C 177  ? 0.8848 1.0495 0.9707 0.1914  -0.0235 -0.0852 177  THR C CB  
10412 O  OG1 . THR C 177  ? 0.8155 0.9801 0.9048 0.1843  -0.0223 -0.0833 177  THR C OG1 
10413 C  CG2 . THR C 177  ? 0.9265 1.0827 1.0042 0.1964  -0.0251 -0.0875 177  THR C CG2 
10414 N  N   . TYR C 178  ? 0.7429 0.9230 0.8309 0.2030  -0.0237 -0.0873 178  TYR C N   
10415 C  CA  . TYR C 178  ? 0.7650 0.9456 0.8492 0.2112  -0.0251 -0.0890 178  TYR C CA  
10416 C  C   . TYR C 178  ? 0.8381 1.0357 0.9262 0.2153  -0.0229 -0.0908 178  TYR C C   
10417 O  O   . TYR C 178  ? 0.9306 1.1293 1.0141 0.2229  -0.0232 -0.0929 178  TYR C O   
10418 C  CB  . TYR C 178  ? 0.8038 0.9804 0.8886 0.2111  -0.0270 -0.0877 178  TYR C CB  
10419 C  CG  . TYR C 178  ? 0.8449 1.0188 0.9239 0.2200  -0.0289 -0.0892 178  TYR C CG  
10420 C  CD1 . TYR C 178  ? 0.8037 0.9711 0.8749 0.2269  -0.0298 -0.0912 178  TYR C CD1 
10421 C  CD2 . TYR C 178  ? 0.8688 1.0460 0.9496 0.2218  -0.0299 -0.0886 178  TYR C CD2 
10422 C  CE1 . TYR C 178  ? 0.8031 0.9674 0.8683 0.2355  -0.0314 -0.0924 178  TYR C CE1 
10423 C  CE2 . TYR C 178  ? 0.8967 1.0710 0.9715 0.2305  -0.0318 -0.0898 178  TYR C CE2 
10424 C  CZ  . TYR C 178  ? 0.9143 1.0821 0.9813 0.2374  -0.0324 -0.0917 178  TYR C CZ  
10425 O  OH  . TYR C 178  ? 1.0519 1.2162 1.1123 0.2466  -0.0341 -0.0929 178  TYR C OH  
10426 N  N   . ALA C 179  ? 0.7211 0.9323 0.8179 0.2103  -0.0204 -0.0901 179  ALA C N   
10427 C  CA  . ALA C 179  ? 0.7225 0.9513 0.8246 0.2134  -0.0180 -0.0919 179  ALA C CA  
10428 C  C   . ALA C 179  ? 0.7947 1.0266 0.8946 0.2152  -0.0154 -0.0931 179  ALA C C   
10429 O  O   . ALA C 179  ? 0.8783 1.1185 0.9776 0.2218  -0.0145 -0.0953 179  ALA C O   
10430 C  CB  . ALA C 179  ? 0.6724 0.9139 0.7843 0.2067  -0.0159 -0.0909 179  ALA C CB  
10431 N  N   . THR C 180  ? 1.0554 1.2808 1.1539 0.2097  -0.0142 -0.0918 180  THR C N   
10432 C  CA  . THR C 180  ? 1.1266 1.3546 1.2224 0.2113  -0.0115 -0.0928 180  THR C CA  
10433 C  C   . THR C 180  ? 1.0846 1.3028 1.1708 0.2191  -0.0136 -0.0946 180  THR C C   
10434 O  O   . THR C 180  ? 1.0603 1.2849 1.1445 0.2244  -0.0117 -0.0965 180  THR C O   
10435 C  CB  . THR C 180  ? 1.0938 1.3165 1.1896 0.2039  -0.0099 -0.0908 180  THR C CB  
10436 O  OG1 . THR C 180  ? 1.1562 1.3640 1.2483 0.2012  -0.0135 -0.0894 180  THR C OG1 
10437 C  CG2 . THR C 180  ? 1.1134 1.3478 1.2182 0.1968  -0.0065 -0.0893 180  THR C CG2 
10438 N  N   . VAL C 181  ? 0.9158 1.1183 0.9959 0.2198  -0.0174 -0.0943 181  VAL C N   
10439 C  CA  . VAL C 181  ? 0.9627 1.1541 1.0330 0.2268  -0.0195 -0.0962 181  VAL C CA  
10440 C  C   . VAL C 181  ? 0.9330 1.1297 1.0016 0.2355  -0.0201 -0.0981 181  VAL C C   
10441 O  O   . VAL C 181  ? 1.0070 1.2031 1.0697 0.2425  -0.0198 -0.1002 181  VAL C O   
10442 C  CB  . VAL C 181  ? 0.9885 1.1615 1.0532 0.2244  -0.0232 -0.0955 181  VAL C CB  
10443 C  CG1 . VAL C 181  ? 0.8459 1.0067 0.9002 0.2316  -0.0256 -0.0977 181  VAL C CG1 
10444 C  CG2 . VAL C 181  ? 0.9507 1.1192 1.0165 0.2169  -0.0228 -0.0940 181  VAL C CG2 
10445 N  N   . SER C 182  ? 0.9405 1.1426 1.0138 0.2357  -0.0210 -0.0975 182  SER C N   
10446 C  CA  . SER C 182  ? 0.9648 1.1731 1.0369 0.2445  -0.0217 -0.0993 182  SER C CA  
10447 C  C   . SER C 182  ? 0.9592 1.1861 1.0366 0.2475  -0.0182 -0.1010 182  SER C C   
10448 O  O   . SER C 182  ? 1.0164 1.2472 1.0904 0.2562  -0.0183 -0.1031 182  SER C O   
10449 C  CB  . SER C 182  ? 0.9934 1.2039 1.0694 0.2439  -0.0236 -0.0983 182  SER C CB  
10450 O  OG  . SER C 182  ? 0.9603 1.1871 1.0471 0.2386  -0.0214 -0.0977 182  SER C OG  
10451 N  N   . LEU C 183  ? 0.7331 0.9712 0.8187 0.2405  -0.0149 -0.1001 183  LEU C N   
10452 C  CA  . LEU C 183  ? 0.6926 0.9486 0.7840 0.2425  -0.0109 -0.1016 183  LEU C CA  
10453 C  C   . LEU C 183  ? 0.7659 1.0183 0.8503 0.2466  -0.0090 -0.1028 183  LEU C C   
10454 O  O   . LEU C 183  ? 0.7932 1.0542 0.8768 0.2530  -0.0074 -0.1047 183  LEU C O   
10455 C  CB  . LEU C 183  ? 0.6239 0.8915 0.7254 0.2333  -0.0076 -0.1002 183  LEU C CB  
10456 C  CG  . LEU C 183  ? 0.6158 0.9021 0.7244 0.2335  -0.0026 -0.1016 183  LEU C CG  
10457 C  CD1 . LEU C 183  ? 0.5850 0.8852 0.6987 0.2379  -0.0031 -0.1034 183  LEU C CD1 
10458 C  CD2 . LEU C 183  ? 0.5853 0.8781 0.7015 0.2234  0.0010  -0.0998 183  LEU C CD2 
10459 N  N   . VAL C 184  ? 0.9162 1.1556 0.9951 0.2426  -0.0094 -0.1017 184  VAL C N   
10460 C  CA  . VAL C 184  ? 0.8931 1.1283 0.9645 0.2465  -0.0078 -0.1029 184  VAL C CA  
10461 C  C   . VAL C 184  ? 1.0224 1.2472 1.0839 0.2558  -0.0108 -0.1050 184  VAL C C   
10462 O  O   . VAL C 184  ? 1.2188 1.4457 1.2753 0.2623  -0.0091 -0.1068 184  VAL C O   
10463 C  CB  . VAL C 184  ? 0.7502 0.9744 0.8181 0.2398  -0.0077 -0.1013 184  VAL C CB  
10464 C  CG1 . VAL C 184  ? 0.7094 0.9436 0.7864 0.2311  -0.0043 -0.0992 184  VAL C CG1 
10465 C  CG2 . VAL C 184  ? 0.8912 1.0978 0.9540 0.2379  -0.0126 -0.1005 184  VAL C CG2 
10466 N  N   . PHE C 185  ? 0.9346 1.1478 0.9926 0.2570  -0.0150 -0.1047 185  PHE C N   
10467 C  CA  . PHE C 185  ? 0.9944 1.1970 1.0425 0.2660  -0.0177 -0.1066 185  PHE C CA  
10468 C  C   . PHE C 185  ? 1.0387 1.2528 1.0879 0.2717  -0.0166 -0.1074 185  PHE C C   
10469 O  O   . PHE C 185  ? 1.1888 1.3988 1.2298 0.2780  -0.0167 -0.1086 185  PHE C O   
10470 C  CB  . PHE C 185  ? 1.0903 1.2767 1.1341 0.2646  -0.0219 -0.1056 185  PHE C CB  
10471 C  CG  . PHE C 185  ? 1.1224 1.2940 1.1544 0.2728  -0.0246 -0.1075 185  PHE C CG  
10472 C  CD1 . PHE C 185  ? 1.0807 1.2402 1.1035 0.2746  -0.0252 -0.1089 185  PHE C CD1 
10473 C  CD2 . PHE C 185  ? 1.1304 1.2995 1.1596 0.2783  -0.0265 -0.1076 185  PHE C CD2 
10474 C  CE1 . PHE C 185  ? 1.0634 1.2085 1.0749 0.2820  -0.0276 -0.1108 185  PHE C CE1 
10475 C  CE2 . PHE C 185  ? 1.2348 1.3885 1.2519 0.2847  -0.0287 -0.1087 185  PHE C CE2 
10476 C  CZ  . PHE C 185  ? 1.1270 1.2691 1.1357 0.2872  -0.0292 -0.1107 185  PHE C CZ  
10477 N  N   . TRP C 186  ? 0.9610 1.1887 1.0198 0.2683  -0.0158 -0.1063 186  TRP C N   
10478 C  CA  . TRP C 186  ? 1.0036 1.2432 1.0643 0.2719  -0.0150 -0.1067 186  TRP C CA  
10479 C  C   . TRP C 186  ? 1.0395 1.2910 1.1019 0.2732  -0.0107 -0.1077 186  TRP C C   
10480 O  O   . TRP C 186  ? 1.1164 1.3706 1.1744 0.2791  -0.0104 -0.1087 186  TRP C O   
10481 C  CB  . TRP C 186  ? 0.9749 1.2269 1.0460 0.2673  -0.0151 -0.1057 186  TRP C CB  
10482 C  CG  . TRP C 186  ? 0.8742 1.1352 0.9460 0.2717  -0.0159 -0.1063 186  TRP C CG  
10483 C  CD1 . TRP C 186  ? 0.9291 1.1808 0.9916 0.2788  -0.0189 -0.1067 186  TRP C CD1 
10484 C  CD2 . TRP C 186  ? 0.8484 1.1295 0.9307 0.2692  -0.0138 -0.1067 186  TRP C CD2 
10485 N  NE1 . TRP C 186  ? 1.0007 1.2658 1.0670 0.2814  -0.0189 -0.1073 186  TRP C NE1 
10486 C  CE2 . TRP C 186  ? 0.9676 1.2510 1.0464 0.2754  -0.0159 -0.1075 186  TRP C CE2 
10487 C  CE3 . TRP C 186  ? 0.8480 1.1451 0.9422 0.2623  -0.0102 -0.1067 186  TRP C CE3 
10488 C  CZ2 . TRP C 186  ? 0.9868 1.2886 1.0740 0.2750  -0.0149 -0.1084 186  TRP C CZ2 
10489 C  CZ3 . TRP C 186  ? 0.8564 1.1714 0.9591 0.2615  -0.0090 -0.1077 186  TRP C CZ3 
10490 C  CH2 . TRP C 186  ? 0.9389 1.2564 1.0383 0.2678  -0.0115 -0.1086 186  TRP C CH2 
10491 N  N   . LEU C 187  ? 0.9813 1.2398 1.0498 0.2678  -0.0072 -0.1074 187  LEU C N   
10492 C  CA  . LEU C 187  ? 0.9455 1.2150 1.0155 0.2687  -0.0025 -0.1082 187  LEU C CA  
10493 C  C   . LEU C 187  ? 1.1488 1.4063 1.2066 0.2750  -0.0027 -0.1094 187  LEU C C   
10494 O  O   . LEU C 187  ? 1.2139 1.4777 1.2695 0.2792  -0.0001 -0.1103 187  LEU C O   
10495 C  CB  . LEU C 187  ? 0.9674 1.2460 1.0460 0.2614  0.0016  -0.1074 187  LEU C CB  
10496 C  CG  . LEU C 187  ? 0.9495 1.2424 1.0409 0.2548  0.0027  -0.1066 187  LEU C CG  
10497 C  CD1 . LEU C 187  ? 0.8018 1.1031 0.9005 0.2480  0.0075  -0.1059 187  LEU C CD1 
10498 C  CD2 . LEU C 187  ? 0.9279 1.2353 1.0245 0.2569  0.0036  -0.1075 187  LEU C CD2 
10499 N  N   . VAL C 188  ? 1.2012 1.4413 1.2511 0.2757  -0.0057 -0.1095 188  VAL C N   
10500 C  CA  . VAL C 188  ? 1.1908 1.4178 1.2282 0.2818  -0.0066 -0.1110 188  VAL C CA  
10501 C  C   . VAL C 188  ? 1.2070 1.4300 1.2373 0.2890  -0.0086 -0.1118 188  VAL C C   
10502 O  O   . VAL C 188  ? 1.3706 1.5925 1.3938 0.2946  -0.0073 -0.1130 188  VAL C O   
10503 C  CB  . VAL C 188  ? 1.1689 1.3779 1.2000 0.2807  -0.0100 -0.1114 188  VAL C CB  
10504 C  CG1 . VAL C 188  ? 1.1452 1.3382 1.1623 0.2875  -0.0123 -0.1133 188  VAL C CG1 
10505 C  CG2 . VAL C 188  ? 1.2086 1.4202 1.2435 0.2744  -0.0076 -0.1106 188  VAL C CG2 
10506 N  N   . GLY C 189  ? 1.0773 1.2981 1.1089 0.2893  -0.0118 -0.1112 189  GLY C N   
10507 C  CA  . GLY C 189  ? 1.1349 1.3525 1.1598 0.2964  -0.0136 -0.1118 189  GLY C CA  
10508 C  C   . GLY C 189  ? 1.2087 1.4447 1.2394 0.2984  -0.0106 -0.1120 189  GLY C C   
10509 O  O   . GLY C 189  ? 1.2206 1.4552 1.2445 0.3053  -0.0111 -0.1129 189  GLY C O   
10510 N  N   . LEU C 190  ? 1.2248 1.4782 1.2680 0.2925  -0.0075 -0.1114 190  LEU C N   
10511 C  CA  . LEU C 190  ? 1.2123 1.4846 1.2627 0.2936  -0.0044 -0.1118 190  LEU C CA  
10512 C  C   . LEU C 190  ? 1.2381 1.5162 1.2869 0.2956  0.0002  -0.1127 190  LEU C C   
10513 O  O   . LEU C 190  ? 1.2731 1.5648 1.3256 0.2982  0.0026  -0.1134 190  LEU C O   
10514 C  CB  . LEU C 190  ? 1.2227 1.5112 1.2875 0.2860  -0.0028 -0.1111 190  LEU C CB  
10515 C  CG  . LEU C 190  ? 1.1627 1.4526 1.2315 0.2847  -0.0065 -0.1105 190  LEU C CG  
10516 C  CD1 . LEU C 190  ? 1.0920 1.3953 1.1742 0.2761  -0.0046 -0.1098 190  LEU C CD1 
10517 C  CD2 . LEU C 190  ? 1.0711 1.3686 1.1391 0.2908  -0.0077 -0.1114 190  LEU C CD2 
10518 N  N   . ILE C 191  ? 1.2884 1.5568 1.3317 0.2946  0.0013  -0.1127 191  ILE C N   
10519 C  CA  . ILE C 191  ? 1.3104 1.5844 1.3521 0.2961  0.0061  -0.1133 191  ILE C CA  
10520 C  C   . ILE C 191  ? 1.2807 1.5534 1.3141 0.3046  0.0062  -0.1145 191  ILE C C   
10521 O  O   . ILE C 191  ? 1.2649 1.5520 1.3030 0.3057  0.0105  -0.1149 191  ILE C O   
10522 C  CB  . ILE C 191  ? 1.3154 1.5772 1.3510 0.2942  0.0066  -0.1133 191  ILE C CB  
10523 C  CG1 . ILE C 191  ? 1.3984 1.6679 1.4445 0.2856  0.0089  -0.1120 191  ILE C CG1 
10524 C  CG2 . ILE C 191  ? 1.3373 1.5986 1.3657 0.2985  0.0103  -0.1142 191  ILE C CG2 
10525 C  CD1 . ILE C 191  ? 1.4004 1.6591 1.4409 0.2837  0.0094  -0.1120 191  ILE C CD1 
10526 N  N   . PRO C 192  ? 1.1676 1.4238 1.1889 0.3107  0.0020  -0.1153 192  PRO C N   
10527 C  CA  . PRO C 192  ? 1.1572 1.4132 1.1708 0.3190  0.0023  -0.1163 192  PRO C CA  
10528 C  C   . PRO C 192  ? 1.2161 1.4883 1.2376 0.3207  0.0028  -0.1163 192  PRO C C   
10529 O  O   . PRO C 192  ? 1.2770 1.5589 1.2986 0.3250  0.0057  -0.1171 192  PRO C O   
10530 C  CB  . PRO C 192  ? 1.0907 1.3246 1.0905 0.3241  -0.0028 -0.1170 192  PRO C CB  
10531 C  CG  . PRO C 192  ? 1.1635 1.3857 1.1626 0.3186  -0.0045 -0.1166 192  PRO C CG  
10532 C  CD  . PRO C 192  ? 1.1862 1.4230 1.1998 0.3107  -0.0029 -0.1152 192  PRO C CD  
10533 N  N   . ASP C 193  ? 1.3947 1.6705 1.4229 0.3176  0.0000  -0.1156 193  ASP C N   
10534 C  CA  . ASP C 193  ? 1.2898 1.5822 1.3261 0.3188  0.0002  -0.1159 193  ASP C CA  
10535 C  C   . ASP C 193  ? 1.2634 1.5772 1.3131 0.3139  0.0056  -0.1161 193  ASP C C   
10536 O  O   . ASP C 193  ? 1.3283 1.6568 1.3830 0.3167  0.0073  -0.1169 193  ASP C O   
10537 C  CB  . ASP C 193  ? 1.2357 1.5265 1.2758 0.3163  -0.0039 -0.1151 193  ASP C CB  
10538 C  CG  . ASP C 193  ? 1.2563 1.5266 1.2832 0.3217  -0.0088 -0.1150 193  ASP C CG  
10539 O  OD1 . ASP C 193  ? 1.2821 1.5381 1.2972 0.3265  -0.0092 -0.1155 193  ASP C OD1 
10540 O  OD2 . ASP C 193  ? 1.3179 1.5858 1.3458 0.3212  -0.0122 -0.1144 193  ASP C OD2 
10541 N  N   . PHE C 194  ? 0.9353 1.2515 0.9910 0.3066  0.0085  -0.1153 194  PHE C N   
10542 C  CA  . PHE C 194  ? 1.0235 1.3582 1.0904 0.3019  0.0144  -0.1154 194  PHE C CA  
10543 C  C   . PHE C 194  ? 1.0686 1.4062 1.1305 0.3074  0.0184  -0.1163 194  PHE C C   
10544 O  O   . PHE C 194  ? 1.1468 1.5017 1.2170 0.3071  0.0225  -0.1169 194  PHE C O   
10545 C  CB  . PHE C 194  ? 1.0180 1.3517 1.0898 0.2937  0.0168  -0.1143 194  PHE C CB  
10546 C  CG  . PHE C 194  ? 0.9420 1.2773 1.0217 0.2873  0.0141  -0.1135 194  PHE C CG  
10547 C  CD1 . PHE C 194  ? 0.8993 1.2464 0.9873 0.2864  0.0123  -0.1139 194  PHE C CD1 
10548 C  CD2 . PHE C 194  ? 0.9580 1.2832 1.0367 0.2822  0.0133  -0.1124 194  PHE C CD2 
10549 C  CE1 . PHE C 194  ? 0.9460 1.2942 1.0406 0.2806  0.0098  -0.1132 194  PHE C CE1 
10550 C  CE2 . PHE C 194  ? 1.0010 1.3275 1.0867 0.2764  0.0109  -0.1115 194  PHE C CE2 
10551 C  CZ  . PHE C 194  ? 0.9980 1.3358 1.0915 0.2755  0.0092  -0.1119 194  PHE C CZ  
10552 N  N   . ALA C 195  ? 1.1410 1.4615 1.1891 0.3124  0.0173  -0.1164 195  ALA C N   
10553 C  CA  . ALA C 195  ? 1.2545 1.5760 1.2962 0.3182  0.0208  -0.1172 195  ALA C CA  
10554 C  C   . ALA C 195  ? 1.2598 1.5882 1.3005 0.3254  0.0198  -0.1182 195  ALA C C   
10555 O  O   . ALA C 195  ? 1.3490 1.6900 1.3931 0.3277  0.0242  -0.1188 195  ALA C O   
10556 C  CB  . ALA C 195  ? 1.3272 1.6276 1.3536 0.3221  0.0191  -0.1173 195  ALA C CB  
10557 N  N   . THR C 196  ? 0.9702 1.2903 1.0059 0.3291  0.0142  -0.1184 196  THR C N   
10558 C  CA  . THR C 196  ? 0.9467 1.2731 0.9809 0.3363  0.0128  -0.1193 196  THR C CA  
10559 C  C   . THR C 196  ? 0.9145 1.2643 0.9642 0.3329  0.0150  -0.1198 196  THR C C   
10560 O  O   . THR C 196  ? 0.9062 1.2670 0.9575 0.3382  0.0161  -0.1209 196  THR C O   
10561 C  CB  . THR C 196  ? 0.9486 1.2595 0.9731 0.3410  0.0064  -0.1193 196  THR C CB  
10562 O  OG1 . THR C 196  ? 1.0949 1.4094 1.1277 0.3353  0.0037  -0.1186 196  THR C OG1 
10563 C  CG2 . THR C 196  ? 0.9627 1.2499 0.9727 0.3432  0.0042  -0.1191 196  THR C CG2 
10564 N  N   . LEU C 197  ? 1.1476 1.5056 1.2089 0.3243  0.0155  -0.1192 197  LEU C N   
10565 C  CA  . LEU C 197  ? 1.2033 1.5836 1.2798 0.3203  0.0175  -0.1199 197  LEU C CA  
10566 C  C   . LEU C 197  ? 1.2114 1.6071 1.2962 0.3175  0.0247  -0.1204 197  LEU C C   
10567 O  O   . LEU C 197  ? 1.2443 1.6571 1.3370 0.3192  0.0269  -0.1217 197  LEU C O   
10568 C  CB  . LEU C 197  ? 1.1593 1.5423 1.2449 0.3120  0.0156  -0.1192 197  LEU C CB  
10569 C  CG  . LEU C 197  ? 1.0900 1.4645 1.1716 0.3143  0.0090  -0.1190 197  LEU C CG  
10570 C  CD1 . LEU C 197  ? 1.1395 1.5233 1.2332 0.3060  0.0080  -0.1187 197  LEU C CD1 
10571 C  CD2 . LEU C 197  ? 1.0469 1.4259 1.1249 0.3228  0.0065  -0.1203 197  LEU C CD2 
10572 N  N   . ARG C 198  ? 1.4338 1.8240 1.5170 0.3134  0.0285  -0.1194 198  ARG C N   
10573 C  CA  . ARG C 198  ? 1.5233 1.9263 1.6128 0.3110  0.0359  -0.1196 198  ARG C CA  
10574 C  C   . ARG C 198  ? 1.5599 1.9618 1.6411 0.3197  0.0380  -0.1204 198  ARG C C   
10575 O  O   . ARG C 198  ? 1.5463 1.9610 1.6332 0.3188  0.0442  -0.1208 198  ARG C O   
10576 C  CB  . ARG C 198  ? 1.5246 1.9206 1.6131 0.3048  0.0394  -0.1183 198  ARG C CB  
10577 C  CG  . ARG C 198  ? 1.4834 1.8565 1.5559 0.3087  0.0367  -0.1175 198  ARG C CG  
10578 C  CD  . ARG C 198  ? 1.4796 1.8483 1.5428 0.3141  0.0408  -0.1177 198  ARG C CD  
10579 N  NE  . ARG C 198  ? 1.4776 1.8248 1.5263 0.3168  0.0382  -0.1173 198  ARG C NE  
10580 C  CZ  . ARG C 198  ? 1.6487 1.9870 1.6858 0.3224  0.0401  -0.1176 198  ARG C CZ  
10581 N  NH1 . ARG C 198  ? 1.7577 2.1060 1.7955 0.3262  0.0448  -0.1181 198  ARG C NH1 
10582 N  NH2 . ARG C 198  ? 1.6805 1.9992 1.7050 0.3241  0.0371  -0.1175 198  ARG C NH2 
10583 N  N   . ASP C 199  ? 1.5349 1.9218 1.6025 0.3278  0.0331  -0.1206 199  ASP C N   
10584 C  CA  . ASP C 199  ? 1.5201 1.9062 1.5797 0.3367  0.0344  -0.1215 199  ASP C CA  
10585 C  C   . ASP C 199  ? 1.5359 1.9368 1.6017 0.3411  0.0331  -0.1228 199  ASP C C   
10586 O  O   . ASP C 199  ? 1.6140 2.0212 1.6778 0.3471  0.0358  -0.1237 199  ASP C O   
10587 C  CB  . ASP C 199  ? 1.5717 1.9342 1.6132 0.3435  0.0300  -0.1213 199  ASP C CB  
10588 C  CG  . ASP C 199  ? 1.6030 1.9532 1.6359 0.3427  0.0329  -0.1206 199  ASP C CG  
10589 O  OD1 . ASP C 199  ? 1.5551 1.9155 1.5947 0.3384  0.0391  -0.1203 199  ASP C OD1 
10590 O  OD2 . ASP C 199  ? 1.5702 1.9001 1.5892 0.3463  0.0291  -0.1206 199  ASP C OD2 
10591 N  N   . ARG C 200  ? 1.4819 1.8883 1.5548 0.3384  0.0290  -0.1231 200  ARG C N   
10592 C  CA  . ARG C 200  ? 1.4597 1.8802 1.5386 0.3424  0.0271  -0.1245 200  ARG C CA  
10593 C  C   . ARG C 200  ? 1.4464 1.8891 1.5438 0.3345  0.0294  -0.1253 200  ARG C C   
10594 O  O   . ARG C 200  ? 1.3819 1.8373 1.4858 0.3367  0.0272  -0.1268 200  ARG C O   
10595 C  CB  . ARG C 200  ? 1.3817 1.7893 1.4516 0.3474  0.0196  -0.1244 200  ARG C CB  
10596 C  CG  . ARG C 200  ? 1.5323 1.9166 1.5836 0.3547  0.0169  -0.1238 200  ARG C CG  
10597 C  CD  . ARG C 200  ? 1.6072 1.9781 1.6502 0.3584  0.0100  -0.1235 200  ARG C CD  
10598 N  NE  . ARG C 200  ? 1.6429 2.0271 1.6914 0.3620  0.0076  -0.1246 200  ARG C NE  
10599 C  CZ  . ARG C 200  ? 1.5750 1.9645 1.6196 0.3705  0.0075  -0.1258 200  ARG C CZ  
10600 N  NH1 . ARG C 200  ? 1.6256 2.0081 1.6605 0.3766  0.0098  -0.1259 200  ARG C NH1 
10601 N  NH2 . ARG C 200  ? 1.4501 1.8523 1.5003 0.3733  0.0050  -0.1269 200  ARG C NH2 
10602 N  N   . ALA C 201  ? 1.8493 2.2965 1.9550 0.3254  0.0338  -0.1246 201  ALA C N   
10603 C  CA  . ALA C 201  ? 1.9182 2.3842 2.0409 0.3169  0.0357  -0.1253 201  ALA C CA  
10604 C  C   . ALA C 201  ? 1.8984 2.3868 2.0328 0.3173  0.0405  -0.1271 201  ALA C C   
10605 O  O   . ALA C 201  ? 1.9121 2.4177 2.0608 0.3115  0.0411  -0.1284 201  ALA C O   
10606 C  CB  . ALA C 201  ? 1.9532 2.4165 2.0805 0.3073  0.0393  -0.1239 201  ALA C CB  
10607 N  N   . LYS C 202  ? 1.5714 2.0601 1.7001 0.3236  0.0441  -0.1274 202  LYS C N   
10608 C  CA  . LYS C 202  ? 1.6454 2.1548 1.7845 0.3248  0.0489  -0.1291 202  LYS C CA  
10609 C  C   . LYS C 202  ? 1.7000 2.2256 1.8548 0.3145  0.0559  -0.1294 202  LYS C C   
10610 O  O   . LYS C 202  ? 1.6857 2.2153 1.8418 0.3134  0.0630  -0.1290 202  LYS C O   
10611 C  CB  . LYS C 202  ? 1.6599 2.1808 1.8038 0.3295  0.0439  -0.1312 202  LYS C CB  
10612 C  CG  . LYS C 202  ? 1.6702 2.2110 1.8226 0.3330  0.0479  -0.1332 202  LYS C CG  
10613 C  CD  . LYS C 202  ? 1.6197 2.1771 1.7825 0.3335  0.0439  -0.1355 202  LYS C CD  
10614 C  CE  . LYS C 202  ? 1.7456 2.3157 1.9241 0.3220  0.0450  -0.1362 202  LYS C CE  
10615 N  NZ  . LYS C 202  ? 1.8176 2.4012 2.0081 0.3144  0.0538  -0.1364 202  LYS C NZ  
10616 N  N   . ASN C 203  ? 1.8208 2.3556 1.9872 0.3068  0.0541  -0.1300 203  ASN C N   
10617 C  CA  . ASN C 203  ? 1.7763 2.3264 1.9579 0.2964  0.0605  -0.1304 203  ASN C CA  
10618 C  C   . ASN C 203  ? 1.7334 2.2714 1.9101 0.2911  0.0654  -0.1281 203  ASN C C   
10619 O  O   . ASN C 203  ? 1.7098 2.2284 1.8745 0.2925  0.0618  -0.1263 203  ASN C O   
10620 C  CB  . ASN C 203  ? 1.7527 2.3125 1.9460 0.2895  0.0567  -0.1316 203  ASN C CB  
10621 C  CG  . ASN C 203  ? 1.7582 2.3339 1.9674 0.2784  0.0633  -0.1322 203  ASN C CG  
10622 O  OD1 . ASN C 203  ? 1.7435 2.3163 1.9566 0.2703  0.0629  -0.1314 203  ASN C OD1 
10623 N  ND2 . ASN C 203  ? 1.8606 2.4532 2.0791 0.2778  0.0696  -0.1337 203  ASN C ND2 
10624 N  N   . ILE C 204  ? 2.4288 2.9787 2.6150 0.2848  0.0738  -0.1281 204  ILE C N   
10625 C  CA  . ILE C 204  ? 2.4830 3.0221 2.6636 0.2807  0.0794  -0.1260 204  ILE C CA  
10626 C  C   . ILE C 204  ? 2.4295 2.9628 2.6130 0.2719  0.0778  -0.1248 204  ILE C C   
10627 O  O   . ILE C 204  ? 2.4276 2.9447 2.6012 0.2710  0.0782  -0.1228 204  ILE C O   
10628 C  CB  . ILE C 204  ? 2.5606 3.1134 2.7493 0.2772  0.0895  -0.1262 204  ILE C CB  
10629 C  CG1 . ILE C 204  ? 2.4765 3.0163 2.6564 0.2749  0.0954  -0.1239 204  ILE C CG1 
10630 C  CG2 . ILE C 204  ? 2.4730 3.0468 2.6808 0.2677  0.0930  -0.1278 204  ILE C CG2 
10631 C  CD1 . ILE C 204  ? 2.4255 2.9438 2.5863 0.2837  0.0916  -0.1225 204  ILE C CD1 
10632 N  N   . TRP C 205  ? 1.6616 2.2078 1.8583 0.2655  0.0759  -0.1262 205  TRP C N   
10633 C  CA  . TRP C 205  ? 1.6012 2.1426 1.8011 0.2570  0.0746  -0.1252 205  TRP C CA  
10634 C  C   . TRP C 205  ? 1.5624 2.0898 1.7543 0.2601  0.0653  -0.1246 205  TRP C C   
10635 O  O   . TRP C 205  ? 1.4487 1.9665 1.6389 0.2549  0.0639  -0.1232 205  TRP C O   
10636 C  CB  . TRP C 205  ? 1.6044 2.1657 1.8222 0.2474  0.0778  -0.1269 205  TRP C CB  
10637 C  CG  . TRP C 205  ? 1.5743 2.1452 1.7996 0.2409  0.0881  -0.1266 205  TRP C CG  
10638 C  CD1 . TRP C 205  ? 1.6087 2.1995 1.8471 0.2378  0.0938  -0.1285 205  TRP C CD1 
10639 C  CD2 . TRP C 205  ? 1.5923 2.1528 1.8119 0.2367  0.0943  -0.1242 205  TRP C CD2 
10640 N  NE1 . TRP C 205  ? 1.6629 2.2559 1.9040 0.2317  0.1034  -0.1274 205  TRP C NE1 
10641 C  CE2 . TRP C 205  ? 1.6984 2.2730 1.9278 0.2311  0.1039  -0.1247 205  TRP C CE2 
10642 C  CE3 . TRP C 205  ? 1.5766 2.1176 1.7838 0.2372  0.0926  -0.1218 205  TRP C CE3 
10643 C  CZ2 . TRP C 205  ? 1.7356 2.3043 1.9616 0.2262  0.1121  -0.1226 205  TRP C CZ2 
10644 C  CZ3 . TRP C 205  ? 1.6566 2.1924 1.8607 0.2327  0.1003  -0.1199 205  TRP C CZ3 
10645 C  CH2 . TRP C 205  ? 1.6981 2.2474 1.9112 0.2273  0.1100  -0.1203 205  TRP C CH2 
10646 N  N   . VAL C 206  ? 1.7019 2.2278 1.8889 0.2685  0.0592  -0.1257 206  VAL C N   
10647 C  CA  . VAL C 206  ? 1.6751 2.1834 1.8507 0.2730  0.0512  -0.1247 206  VAL C CA  
10648 C  C   . VAL C 206  ? 1.6798 2.1677 1.8402 0.2769  0.0517  -0.1226 206  VAL C C   
10649 O  O   . VAL C 206  ? 1.6653 2.1374 1.8182 0.2760  0.0477  -0.1212 206  VAL C O   
10650 C  CB  . VAL C 206  ? 1.6741 2.1850 1.8467 0.2815  0.0451  -0.1263 206  VAL C CB  
10651 C  CG1 . VAL C 206  ? 1.6048 2.0975 1.7662 0.2854  0.0373  -0.1253 206  VAL C CG1 
10652 C  CG2 . VAL C 206  ? 1.7077 2.2402 1.8957 0.2778  0.0449  -0.1287 206  VAL C CG2 
10653 N  N   . LYS C 207  ? 1.3463 1.8342 1.5018 0.2813  0.0567  -0.1226 207  LYS C N   
10654 C  CA  . LYS C 207  ? 1.2455 1.7166 1.3885 0.2832  0.0588  -0.1208 207  LYS C CA  
10655 C  C   . LYS C 207  ? 1.1963 1.6679 1.3445 0.2738  0.0640  -0.1195 207  LYS C C   
10656 O  O   . LYS C 207  ? 1.2181 1.7039 1.3798 0.2657  0.0668  -0.1200 207  LYS C O   
10657 C  CB  . LYS C 207  ? 1.3941 1.8666 1.5312 0.2900  0.0633  -0.1211 207  LYS C CB  
10658 C  CG  . LYS C 207  ? 1.4207 1.8899 1.5501 0.3003  0.0583  -0.1222 207  LYS C CG  
10659 C  CD  . LYS C 207  ? 1.3341 1.8103 1.4618 0.3060  0.0636  -0.1229 207  LYS C CD  
10660 C  CE  . LYS C 207  ? 1.2741 1.7467 1.3935 0.3165  0.0586  -0.1240 207  LYS C CE  
10661 N  NZ  . LYS C 207  ? 1.2383 1.6875 1.3410 0.3221  0.0526  -0.1230 207  LYS C NZ  
10662 N  N   . ARG C 208  ? 1.4939 1.9492 1.6304 0.2749  0.0652  -0.1178 208  ARG C N   
10663 C  CA  . ARG C 208  ? 1.5064 1.9585 1.6446 0.2672  0.0695  -0.1163 208  ARG C CA  
10664 C  C   . ARG C 208  ? 1.4847 1.9339 1.6277 0.2610  0.0648  -0.1158 208  ARG C C   
10665 O  O   . ARG C 208  ? 1.5035 1.9462 1.6456 0.2555  0.0667  -0.1144 208  ARG C O   
10666 C  CB  . ARG C 208  ? 1.5339 2.0029 1.6833 0.2610  0.0787  -0.1165 208  ARG C CB  
10667 C  CG  . ARG C 208  ? 1.5610 2.0338 1.7064 0.2666  0.0843  -0.1169 208  ARG C CG  
10668 C  CD  . ARG C 208  ? 1.5751 2.0675 1.7344 0.2603  0.0930  -0.1175 208  ARG C CD  
10669 N  NE  . ARG C 208  ? 1.7910 2.2848 1.9454 0.2645  0.0998  -0.1173 208  ARG C NE  
10670 C  CZ  . ARG C 208  ? 1.7266 2.2356 1.8909 0.2601  0.1085  -0.1177 208  ARG C CZ  
10671 N  NH1 . ARG C 208  ? 1.7118 2.2363 1.8918 0.2511  0.1114  -0.1185 208  ARG C NH1 
10672 N  NH2 . ARG C 208  ? 1.6336 2.1419 1.7917 0.2647  0.1144  -0.1173 208  ARG C NH2 
10673 N  N   . LEU C 209  ? 1.1758 1.6296 1.3236 0.2620  0.0588  -0.1170 209  LEU C N   
10674 C  CA  . LEU C 209  ? 1.0579 1.5071 1.2086 0.2574  0.0535  -0.1165 209  LEU C CA  
10675 C  C   . LEU C 209  ? 1.1244 1.5534 1.2615 0.2636  0.0463  -0.1158 209  LEU C C   
10676 O  O   . LEU C 209  ? 1.2073 1.6239 1.3401 0.2606  0.0445  -0.1144 209  LEU C O   
10677 C  CB  . LEU C 209  ? 0.9737 1.4391 1.1370 0.2548  0.0511  -0.1182 209  LEU C CB  
10678 C  CG  . LEU C 209  ? 0.8752 1.3417 1.0458 0.2472  0.0482  -0.1180 209  LEU C CG  
10679 C  CD1 . LEU C 209  ? 0.7277 1.1982 0.9048 0.2380  0.0546  -0.1170 209  LEU C CD1 
10680 C  CD2 . LEU C 209  ? 0.8388 1.3208 1.0203 0.2460  0.0453  -0.1200 209  LEU C CD2 
10681 N  N   . TYR C 210  ? 1.2179 1.6434 1.3482 0.2720  0.0424  -0.1167 210  TYR C N   
10682 C  CA  . TYR C 210  ? 1.1961 1.6010 1.3118 0.2785  0.0368  -0.1160 210  TYR C CA  
10683 C  C   . TYR C 210  ? 1.2842 1.6767 1.3888 0.2813  0.0398  -0.1152 210  TYR C C   
10684 O  O   . TYR C 210  ? 1.3015 1.6758 1.3948 0.2841  0.0358  -0.1146 210  TYR C O   
10685 C  CB  . TYR C 210  ? 1.2162 1.6203 1.3267 0.2870  0.0324  -0.1172 210  TYR C CB  
10686 C  CG  . TYR C 210  ? 1.2473 1.6618 1.3664 0.2858  0.0285  -0.1181 210  TYR C CG  
10687 C  CD1 . TYR C 210  ? 1.2865 1.6946 1.4069 0.2819  0.0239  -0.1174 210  TYR C CD1 
10688 C  CD2 . TYR C 210  ? 1.2701 1.7007 1.3958 0.2888  0.0293  -0.1198 210  TYR C CD2 
10689 C  CE1 . TYR C 210  ? 1.2568 1.6738 1.3841 0.2811  0.0202  -0.1183 210  TYR C CE1 
10690 C  CE2 . TYR C 210  ? 1.2466 1.6866 1.3796 0.2881  0.0254  -0.1209 210  TYR C CE2 
10691 C  CZ  . TYR C 210  ? 1.2523 1.6852 1.3857 0.2843  0.0209  -0.1201 210  TYR C CZ  
10692 O  OH  . TYR C 210  ? 1.2736 1.7154 1.4133 0.2839  0.0169  -0.1212 210  TYR C OH  
10693 N  N   . GLY C 211  ? 1.5689 1.9706 1.6761 0.2806  0.0468  -0.1153 211  GLY C N   
10694 C  CA  . GLY C 211  ? 1.6446 2.0345 1.7405 0.2836  0.0498  -0.1146 211  GLY C CA  
10695 C  C   . GLY C 211  ? 1.5954 1.9745 1.6884 0.2783  0.0499  -0.1132 211  GLY C C   
10696 O  O   . GLY C 211  ? 1.6515 2.0131 1.7320 0.2819  0.0471  -0.1129 211  GLY C O   
10697 N  N   . ILE C 212  ? 1.1262 1.5155 1.2305 0.2696  0.0532  -0.1126 212  ILE C N   
10698 C  CA  . ILE C 212  ? 1.1719 1.5516 1.2741 0.2645  0.0532  -0.1112 212  ILE C CA  
10699 C  C   . ILE C 212  ? 1.0868 1.4548 1.1863 0.2646  0.0453  -0.1110 212  ILE C C   
10700 O  O   . ILE C 212  ? 1.0935 1.4488 1.1874 0.2628  0.0435  -0.1100 212  ILE C O   
10701 C  CB  . ILE C 212  ? 1.2305 1.6241 1.3452 0.2552  0.0593  -0.1105 212  ILE C CB  
10702 C  CG1 . ILE C 212  ? 1.2348 1.6392 1.3622 0.2499  0.0563  -0.1111 212  ILE C CG1 
10703 C  CG2 . ILE C 212  ? 1.3395 1.7461 1.4582 0.2549  0.0675  -0.1108 212  ILE C CG2 
10704 C  CD1 . ILE C 212  ? 1.2410 1.6554 1.3795 0.2401  0.0611  -0.1104 212  ILE C CD1 
10705 N  N   . ALA C 213  ? 0.9473 1.3191 1.0503 0.2667  0.0405  -0.1118 213  ALA C N   
10706 C  CA  . ALA C 213  ? 0.9662 1.3253 1.0650 0.2676  0.0332  -0.1116 213  ALA C CA  
10707 C  C   . ALA C 213  ? 1.0817 1.4220 1.1652 0.2754  0.0293  -0.1118 213  ALA C C   
10708 O  O   . ALA C 213  ? 1.0987 1.4240 1.1759 0.2751  0.0252  -0.1113 213  ALA C O   
10709 C  CB  . ALA C 213  ? 0.8474 1.2158 0.9536 0.2678  0.0296  -0.1124 213  ALA C CB  
10710 N  N   . ALA C 214  ? 1.4723 1.8134 1.5498 0.2823  0.0305  -0.1128 214  ALA C N   
10711 C  CA  . ALA C 214  ? 1.4280 1.7514 1.4904 0.2896  0.0275  -0.1133 214  ALA C CA  
10712 C  C   . ALA C 214  ? 1.4456 1.7598 1.5006 0.2890  0.0304  -0.1129 214  ALA C C   
10713 O  O   . ALA C 214  ? 1.3762 1.6739 1.4183 0.2941  0.0274  -0.1135 214  ALA C O   
10714 C  CB  . ALA C 214  ? 1.3683 1.6957 1.4264 0.2973  0.0282  -0.1145 214  ALA C CB  
10715 N  N   . LEU C 215  ? 1.4027 1.7267 1.4649 0.2831  0.0362  -0.1120 215  LEU C N   
10716 C  CA  . LEU C 215  ? 1.4031 1.7194 1.4581 0.2825  0.0396  -0.1115 215  LEU C CA  
10717 C  C   . LEU C 215  ? 1.4387 1.7492 1.4821 0.2901  0.0414  -0.1124 215  LEU C C   
10718 O  O   . LEU C 215  ? 1.4584 1.7562 1.4909 0.2923  0.0415  -0.1125 215  LEU C O   
10719 C  CB  . LEU C 215  ? 1.4134 1.7133 1.4624 0.2809  0.0347  -0.1112 215  LEU C CB  
10720 C  CG  . LEU C 215  ? 1.3921 1.6952 1.4511 0.2738  0.0323  -0.1102 215  LEU C CG  
10721 C  CD1 . LEU C 215  ? 1.3129 1.5983 1.3646 0.2738  0.0267  -0.1102 215  LEU C CD1 
10722 C  CD2 . LEU C 215  ? 1.3380 1.6542 1.4071 0.2664  0.0385  -0.1090 215  LEU C CD2 
10723 N  N   . GLY C 216  ? 1.6948 2.0146 1.7401 0.2943  0.0428  -0.1132 216  GLY C N   
10724 C  CA  . GLY C 216  ? 1.7172 2.0306 1.7510 0.3022  0.0438  -0.1141 216  GLY C CA  
10725 C  C   . GLY C 216  ? 1.6709 1.9636 1.6907 0.3078  0.0371  -0.1150 216  GLY C C   
10726 O  O   . GLY C 216  ? 1.7040 1.9837 1.7126 0.3100  0.0370  -0.1153 216  GLY C O   
10727 N  N   . TRP C 217  ? 1.4055 1.6949 1.4255 0.3100  0.0315  -0.1156 217  TRP C N   
10728 C  CA  . TRP C 217  ? 1.3452 1.6144 1.3533 0.3139  0.0249  -0.1165 217  TRP C CA  
10729 C  C   . TRP C 217  ? 1.4220 1.6796 1.4153 0.3217  0.0249  -0.1178 217  TRP C C   
10730 O  O   . TRP C 217  ? 1.4917 1.7335 1.4745 0.3228  0.0227  -0.1185 217  TRP C O   
10731 C  CB  . TRP C 217  ? 1.2874 1.5562 1.2982 0.3154  0.0199  -0.1167 217  TRP C CB  
10732 C  CG  . TRP C 217  ? 1.2012 1.4494 1.1990 0.3204  0.0138  -0.1177 217  TRP C CG  
10733 C  CD1 . TRP C 217  ? 1.2524 1.4948 1.2431 0.3273  0.0108  -0.1186 217  TRP C CD1 
10734 C  CD2 . TRP C 217  ? 1.1559 1.3866 1.1464 0.3188  0.0101  -0.1182 217  TRP C CD2 
10735 N  NE1 . TRP C 217  ? 1.2344 1.4562 1.2137 0.3298  0.0057  -0.1195 217  TRP C NE1 
10736 C  CE2 . TRP C 217  ? 1.1599 1.3746 1.1392 0.3245  0.0051  -0.1194 217  TRP C CE2 
10737 C  CE3 . TRP C 217  ? 1.1653 1.3924 1.1576 0.3131  0.0105  -0.1177 217  TRP C CE3 
10738 C  CZ2 . TRP C 217  ? 1.1865 1.3821 1.1572 0.3244  0.0006  -0.1204 217  TRP C CZ2 
10739 C  CZ3 . TRP C 217  ? 1.1865 1.3951 1.1703 0.3133  0.0058  -0.1187 217  TRP C CZ3 
10740 C  CH2 . TRP C 217  ? 1.2210 1.4142 1.1944 0.3187  0.0009  -0.1201 217  TRP C CH2 
10741 N  N   . ARG C 218  ? 1.6074 1.8726 1.5997 0.3271  0.0273  -0.1183 218  ARG C N   
10742 C  CA  . ARG C 218  ? 1.5880 1.8431 1.5664 0.3349  0.0275  -0.1195 218  ARG C CA  
10743 C  C   . ARG C 218  ? 1.5471 1.7807 1.5125 0.3390  0.0206  -0.1208 218  ARG C C   
10744 O  O   . ARG C 218  ? 1.5654 1.7840 1.5204 0.3399  0.0190  -0.1217 218  ARG C O   
10745 C  CB  . ARG C 218  ? 1.5583 1.8132 1.5325 0.3342  0.0327  -0.1192 218  ARG C CB  
10746 C  CG  . ARG C 218  ? 1.5776 1.8244 1.5380 0.3422  0.0339  -0.1203 218  ARG C CG  
10747 C  CD  . ARG C 218  ? 1.6167 1.8597 1.5710 0.3412  0.0381  -0.1201 218  ARG C CD  
10748 N  NE  . ARG C 218  ? 1.5944 1.8176 1.5368 0.3418  0.0332  -0.1212 218  ARG C NE  
10749 C  CZ  . ARG C 218  ? 1.5397 1.7593 1.4836 0.3362  0.0331  -0.1207 218  ARG C CZ  
10750 N  NH1 . ARG C 218  ? 1.5284 1.7620 1.4845 0.3296  0.0377  -0.1188 218  ARG C NH1 
10751 N  NH2 . ARG C 218  ? 1.5946 1.7961 1.5274 0.3374  0.0281  -0.1222 218  ARG C NH2 
10752 N  N   . GLY C 219  ? 1.3544 1.5868 1.3208 0.3413  0.0167  -0.1210 219  GLY C N   
10753 C  CA  . GLY C 219  ? 1.3833 1.5960 1.3391 0.3444  0.0104  -0.1221 219  GLY C CA  
10754 C  C   . GLY C 219  ? 1.4362 1.6323 1.3755 0.3509  0.0091  -0.1239 219  GLY C C   
10755 O  O   . GLY C 219  ? 1.5430 1.7389 1.4758 0.3578  0.0098  -0.1245 219  GLY C O   
10756 N  N   . SER C 220  ? 1.1702 1.3523 1.1026 0.3489  0.0072  -0.1248 220  SER C N   
10757 C  CA  . SER C 220  ? 1.1919 1.3580 1.1086 0.3544  0.0059  -0.1267 220  SER C CA  
10758 C  C   . SER C 220  ? 1.1589 1.3054 1.0681 0.3524  0.0003  -0.1283 220  SER C C   
10759 O  O   . SER C 220  ? 1.1940 1.3405 1.1110 0.3464  -0.0018 -0.1277 220  SER C O   
10760 C  CB  . SER C 220  ? 1.2716 1.4441 1.1868 0.3544  0.0112  -0.1265 220  SER C CB  
10761 O  OG  . SER C 220  ? 1.2012 1.3728 1.1201 0.3480  0.0115  -0.1261 220  SER C OG  
10762 N  N   . ALA C 221  ? 1.2080 1.3377 1.1023 0.3576  -0.0021 -0.1306 221  ALA C N   
10763 C  CA  . ALA C 221  ? 1.2463 1.3573 1.1329 0.3557  -0.0071 -0.1327 221  ALA C CA  
10764 C  C   . ALA C 221  ? 1.3188 1.4332 1.2094 0.3502  -0.0056 -0.1326 221  ALA C C   
10765 O  O   . ALA C 221  ? 1.3395 1.4689 1.2366 0.3486  -0.0003 -0.1308 221  ALA C O   
10766 C  CB  . ALA C 221  ? 1.4404 1.5333 1.3098 0.3624  -0.0098 -0.1355 221  ALA C CB  
10767 N  N   . ARG C 222  ? 1.8913 1.9914 1.7780 0.3473  -0.0103 -0.1344 222  ARG C N   
10768 C  CA  . ARG C 222  ? 1.9309 2.0329 1.8219 0.3417  -0.0100 -0.1343 222  ARG C CA  
10769 C  C   . ARG C 222  ? 1.8762 1.9941 1.7837 0.3350  -0.0076 -0.1314 222  ARG C C   
10770 O  O   . ARG C 222  ? 1.9893 2.1095 1.9022 0.3297  -0.0075 -0.1309 222  ARG C O   
10771 C  CB  . ARG C 222  ? 1.9609 2.0660 1.8456 0.3440  -0.0061 -0.1346 222  ARG C CB  
10772 C  CG  . ARG C 222  ? 2.0725 2.1612 1.9401 0.3504  -0.0087 -0.1377 222  ARG C CG  
10773 C  CD  . ARG C 222  ? 1.9924 2.0798 1.8530 0.3510  -0.0067 -0.1384 222  ARG C CD  
10774 N  NE  . ARG C 222  ? 1.9730 2.0787 1.8415 0.3497  0.0006  -0.1352 222  ARG C NE  
10775 C  CZ  . ARG C 222  ? 2.0222 2.1335 1.8856 0.3544  0.0054  -0.1345 222  ARG C CZ  
10776 N  NH1 . ARG C 222  ? 2.0052 2.1058 1.8555 0.3612  0.0038  -0.1365 222  ARG C NH1 
10777 N  NH2 . ARG C 222  ? 1.9658 2.0937 1.8375 0.3522  0.0123  -0.1317 222  ARG C NH2 
10778 N  N   . HIS C 223  ? 1.4730 1.6021 1.3884 0.3354  -0.0058 -0.1295 223  HIS C N   
10779 C  CA  . HIS C 223  ? 1.4910 1.6345 1.4218 0.3294  -0.0042 -0.1269 223  HIS C CA  
10780 C  C   . HIS C 223  ? 1.3807 1.5187 1.3144 0.3286  -0.0085 -0.1268 223  HIS C C   
10781 O  O   . HIS C 223  ? 1.3309 1.4719 1.2739 0.3228  -0.0097 -0.1256 223  HIS C O   
10782 C  CB  . HIS C 223  ? 1.4257 1.5893 1.3648 0.3298  0.0018  -0.1249 223  HIS C CB  
10783 C  CG  . HIS C 223  ? 1.3544 1.5270 1.2953 0.3280  0.0072  -0.1241 223  HIS C CG  
10784 N  ND1 . HIS C 223  ? 1.2555 1.4473 1.2087 0.3240  0.0128  -0.1219 223  HIS C ND1 
10785 C  CD2 . HIS C 223  ? 1.3808 1.5454 1.3119 0.3297  0.0080  -0.1252 223  HIS C CD2 
10786 C  CE1 . HIS C 223  ? 1.2450 1.4398 1.1960 0.3233  0.0171  -0.1215 223  HIS C CE1 
10787 N  NE2 . HIS C 223  ? 1.3404 1.5189 1.2778 0.3269  0.0142  -0.1235 223  HIS C NE2 
10788 N  N   . TRP C 224  ? 1.3540 1.4835 1.2792 0.3346  -0.0105 -0.1278 224  TRP C N   
10789 C  CA  . TRP C 224  ? 1.2897 1.4112 1.2153 0.3346  -0.0145 -0.1277 224  TRP C CA  
10790 C  C   . TRP C 224  ? 1.3085 1.4119 1.2292 0.3319  -0.0194 -0.1296 224  TRP C C   
10791 O  O   . TRP C 224  ? 1.3516 1.4513 1.2771 0.3286  -0.0220 -0.1288 224  TRP C O   
10792 C  CB  . TRP C 224  ? 1.3383 1.4541 1.2545 0.3422  -0.0153 -0.1285 224  TRP C CB  
10793 C  CG  . TRP C 224  ? 1.3215 1.4555 1.2444 0.3447  -0.0114 -0.1267 224  TRP C CG  
10794 C  CD1 . TRP C 224  ? 1.4133 1.5532 1.3316 0.3504  -0.0083 -0.1270 224  TRP C CD1 
10795 C  CD2 . TRP C 224  ? 1.3126 1.4614 1.2483 0.3416  -0.0105 -0.1245 224  TRP C CD2 
10796 N  NE1 . TRP C 224  ? 1.3788 1.5367 1.3067 0.3510  -0.0054 -0.1253 224  TRP C NE1 
10797 C  CE2 . TRP C 224  ? 1.3067 1.4703 1.2452 0.3455  -0.0069 -0.1238 224  TRP C CE2 
10798 C  CE3 . TRP C 224  ? 1.3348 1.4857 1.2797 0.3358  -0.0124 -0.1232 224  TRP C CE3 
10799 C  CZ2 . TRP C 224  ? 1.3345 1.5151 1.2848 0.3439  -0.0054 -0.1222 224  TRP C CZ2 
10800 C  CZ3 . TRP C 224  ? 1.3364 1.5037 1.2924 0.3343  -0.0109 -0.1214 224  TRP C CZ3 
10801 C  CH2 . TRP C 224  ? 1.3649 1.5469 1.3235 0.3382  -0.0075 -0.1210 224  TRP C CH2 
10802 N  N   . HIS C 225  ? 1.2416 1.3334 1.1526 0.3332  -0.0208 -0.1320 225  HIS C N   
10803 C  CA  . HIS C 225  ? 1.2428 1.3177 1.1495 0.3305  -0.0256 -0.1343 225  HIS C CA  
10804 C  C   . HIS C 225  ? 1.2141 1.2961 1.1332 0.3229  -0.0258 -0.1329 225  HIS C C   
10805 O  O   . HIS C 225  ? 1.2485 1.3227 1.1707 0.3185  -0.0292 -0.1326 225  HIS C O   
10806 C  CB  . HIS C 225  ? 1.2760 1.3393 1.1704 0.3334  -0.0269 -0.1375 225  HIS C CB  
10807 C  CG  . HIS C 225  ? 1.2771 1.3195 1.1634 0.3327  -0.0326 -0.1410 225  HIS C CG  
10808 N  ND1 . HIS C 225  ? 1.3574 1.3889 1.2431 0.3321  -0.0358 -0.1413 225  HIS C ND1 
10809 C  CD2 . HIS C 225  ? 1.2855 1.3159 1.1642 0.3309  -0.0357 -0.1437 225  HIS C CD2 
10810 C  CE1 . HIS C 225  ? 1.4572 1.4708 1.3357 0.3294  -0.0404 -0.1441 225  HIS C CE1 
10811 N  NE2 . HIS C 225  ? 1.4068 1.4198 1.2812 0.3280  -0.0407 -0.1455 225  HIS C NE2 
10812 N  N   . ARG C 226  ? 1.2624 1.3585 1.1883 0.3201  -0.0220 -0.1315 226  ARG C N   
10813 C  CA  . ARG C 226  ? 1.2355 1.3383 1.1729 0.3097  -0.0220 -0.1285 226  ARG C CA  
10814 C  C   . ARG C 226  ? 1.2031 1.3169 1.1522 0.3076  -0.0209 -0.1261 226  ARG C C   
10815 O  O   . ARG C 226  ? 1.1831 1.2968 1.1400 0.2994  -0.0226 -0.1240 226  ARG C O   
10816 C  CB  . ARG C 226  ? 1.1408 1.2553 1.0815 0.3070  -0.0177 -0.1271 226  ARG C CB  
10817 C  CG  . ARG C 226  ? 1.1982 1.3018 1.1272 0.3085  -0.0191 -0.1292 226  ARG C CG  
10818 C  CD  . ARG C 226  ? 1.2308 1.3429 1.1635 0.3032  -0.0158 -0.1271 226  ARG C CD  
10819 N  NE  . ARG C 226  ? 1.2397 1.3416 1.1602 0.3058  -0.0171 -0.1293 226  ARG C NE  
10820 C  CZ  . ARG C 226  ? 1.3008 1.4046 1.2128 0.3133  -0.0137 -0.1307 226  ARG C CZ  
10821 N  NH1 . ARG C 226  ? 1.3391 1.4552 1.2541 0.3191  -0.0087 -0.1303 226  ARG C NH1 
10822 N  NH2 . ARG C 226  ? 1.4255 1.5188 1.3259 0.3153  -0.0155 -0.1328 226  ARG C NH2 
10823 N  N   . TYR C 227  ? 1.3895 1.5126 1.3397 0.3132  -0.0184 -0.1258 227  TYR C N   
10824 C  CA  . TYR C 227  ? 1.3035 1.4365 1.2638 0.3108  -0.0179 -0.1234 227  TYR C CA  
10825 C  C   . TYR C 227  ? 1.2901 1.4084 1.2472 0.3110  -0.0227 -0.1239 227  TYR C C   
10826 O  O   . TYR C 227  ? 1.2844 1.4056 1.2501 0.3063  -0.0237 -0.1223 227  TYR C O   
10827 C  CB  . TYR C 227  ? 1.3100 1.4551 1.2710 0.3153  -0.0146 -0.1225 227  TYR C CB  
10828 C  CG  . TYR C 227  ? 1.2624 1.4213 1.2349 0.3126  -0.0136 -0.1202 227  TYR C CG  
10829 C  CD1 . TYR C 227  ? 1.1971 1.3747 1.1821 0.3076  -0.0097 -0.1184 227  TYR C CD1 
10830 C  CD2 . TYR C 227  ? 1.3403 1.4932 1.3105 0.3153  -0.0166 -0.1199 227  TYR C CD2 
10831 C  CE1 . TYR C 227  ? 1.2128 1.4030 1.2081 0.3051  -0.0091 -0.1167 227  TYR C CE1 
10832 C  CE2 . TYR C 227  ? 1.3731 1.5384 1.3530 0.3132  -0.0160 -0.1181 227  TYR C CE2 
10833 C  CZ  . TYR C 227  ? 1.3391 1.5232 1.3317 0.3081  -0.0124 -0.1166 227  TYR C CZ  
10834 O  OH  . TYR C 227  ? 1.4697 1.6661 1.4718 0.3059  -0.0122 -0.1151 227  TYR C OH  
10835 N  N   . GLU C 228  ? 1.3816 1.4834 1.3259 0.3163  -0.0254 -0.1262 228  GLU C N   
10836 C  CA  . GLU C 228  ? 1.4162 1.5024 1.3563 0.3167  -0.0294 -0.1268 228  GLU C CA  
10837 C  C   . GLU C 228  ? 1.3562 1.4325 1.2987 0.3093  -0.0325 -0.1270 228  GLU C C   
10838 O  O   . GLU C 228  ? 1.4414 1.5127 1.3878 0.3051  -0.0344 -0.1255 228  GLU C O   
10839 C  CB  . GLU C 228  ? 1.4632 1.5332 1.3882 0.3237  -0.0313 -0.1292 228  GLU C CB  
10840 C  CG  . GLU C 228  ? 1.5933 1.6709 1.5153 0.3298  -0.0290 -0.1281 228  GLU C CG  
10841 C  CD  . GLU C 228  ? 1.8264 1.8997 1.7478 0.3317  -0.0306 -0.1267 228  GLU C CD  
10842 O  OE1 . GLU C 228  ? 1.9073 1.9623 1.8175 0.3353  -0.0332 -0.1282 228  GLU C OE1 
10843 O  OE2 . GLU C 228  ? 1.7138 1.8017 1.6457 0.3294  -0.0291 -0.1242 228  GLU C OE2 
10844 N  N   . MET C 229  ? 1.2922 1.3648 1.2321 0.3052  -0.0330 -0.1278 229  MET C N   
10845 C  CA  . MET C 229  ? 1.3102 1.3735 1.2524 0.2956  -0.0362 -0.1272 229  MET C CA  
10846 C  C   . MET C 229  ? 1.3197 1.3960 1.2758 0.2872  -0.0347 -0.1236 229  MET C C   
10847 O  O   . MET C 229  ? 1.3100 1.3799 1.2703 0.2804  -0.0371 -0.1223 229  MET C O   
10848 C  CB  . MET C 229  ? 1.3192 1.3760 1.2546 0.2943  -0.0374 -0.1293 229  MET C CB  
10849 C  CG  . MET C 229  ? 1.2784 1.3251 1.2156 0.2851  -0.0413 -0.1293 229  MET C CG  
10850 S  SD  . MET C 229  ? 1.4134 1.4392 1.3447 0.2842  -0.0458 -0.1311 229  MET C SD  
10851 C  CE  . MET C 229  ? 1.3353 1.3512 1.2674 0.2745  -0.0501 -0.1322 229  MET C CE  
10852 N  N   . ALA C 230  ? 1.1570 1.2513 1.1204 0.2875  -0.0305 -0.1220 230  ALA C N   
10853 C  CA  . ALA C 230  ? 1.1107 1.2175 1.0869 0.2798  -0.0288 -0.1187 230  ALA C CA  
10854 C  C   . ALA C 230  ? 1.0244 1.1337 1.0062 0.2801  -0.0293 -0.1173 230  ALA C C   
10855 O  O   . ALA C 230  ? 0.9756 1.0860 0.9651 0.2728  -0.0301 -0.1150 230  ALA C O   
10856 C  CB  . ALA C 230  ? 0.9626 1.0874 0.9447 0.2801  -0.0238 -0.1175 230  ALA C CB  
10857 N  N   . SER C 231  ? 1.0333 1.1434 1.0108 0.2889  -0.0288 -0.1186 231  SER C N   
10858 C  CA  . SER C 231  ? 0.9735 1.0851 0.9548 0.2904  -0.0296 -0.1174 231  SER C CA  
10859 C  C   . SER C 231  ? 1.0301 1.1227 1.0064 0.2874  -0.0336 -0.1174 231  SER C C   
10860 O  O   . SER C 231  ? 1.1519 1.2449 1.1340 0.2836  -0.0344 -0.1154 231  SER C O   
10861 C  CB  . SER C 231  ? 1.0015 1.1181 0.9783 0.3008  -0.0283 -0.1188 231  SER C CB  
10862 O  OG  . SER C 231  ? 1.1997 1.2980 1.1634 0.3063  -0.0309 -0.1208 231  SER C OG  
10863 N  N   . ILE C 232  ? 0.9624 1.0381 0.9281 0.2889  -0.0361 -0.1198 232  ILE C N   
10864 C  CA  . ILE C 232  ? 0.9867 1.0439 0.9480 0.2851  -0.0396 -0.1200 232  ILE C CA  
10865 C  C   . ILE C 232  ? 1.0216 1.0798 0.9917 0.2739  -0.0404 -0.1178 232  ILE C C   
10866 O  O   . ILE C 232  ? 1.0330 1.0853 1.0063 0.2694  -0.0417 -0.1162 232  ILE C O   
10867 C  CB  . ILE C 232  ? 0.9456 0.9853 0.8938 0.2888  -0.0419 -0.1235 232  ILE C CB  
10868 C  CG1 . ILE C 232  ? 1.0544 1.0878 0.9925 0.2998  -0.0417 -0.1254 232  ILE C CG1 
10869 C  CG2 . ILE C 232  ? 0.8222 0.8447 0.7684 0.2815  -0.0453 -0.1239 232  ILE C CG2 
10870 C  CD1 . ILE C 232  ? 1.1755 1.2007 1.1124 0.3012  -0.0427 -0.1241 232  ILE C CD1 
10871 N  N   . LEU C 233  ? 1.0835 1.1487 1.0571 0.2696  -0.0396 -0.1177 233  LEU C N   
10872 C  CA  . LEU C 233  ? 1.0226 1.0896 1.0045 0.2595  -0.0402 -0.1157 233  LEU C CA  
10873 C  C   . LEU C 233  ? 0.9899 1.0701 0.9831 0.2559  -0.0381 -0.1123 233  LEU C C   
10874 O  O   . LEU C 233  ? 0.9447 1.0218 0.9434 0.2488  -0.0392 -0.1104 233  LEU C O   
10875 C  CB  . LEU C 233  ? 1.0140 1.0864 0.9963 0.2569  -0.0395 -0.1162 233  LEU C CB  
10876 C  CG  . LEU C 233  ? 1.1074 1.1659 1.0795 0.2582  -0.0424 -0.1195 233  LEU C CG  
10877 C  CD1 . LEU C 233  ? 1.2022 1.2679 1.1738 0.2575  -0.0411 -0.1199 233  LEU C CD1 
10878 C  CD2 . LEU C 233  ? 0.9727 1.0172 0.9448 0.2515  -0.0463 -0.1200 233  LEU C CD2 
10879 N  N   . LEU C 234  ? 0.9618 1.0571 0.9586 0.2605  -0.0350 -0.1117 234  LEU C N   
10880 C  CA  . LEU C 234  ? 0.9351 1.0438 0.9427 0.2571  -0.0330 -0.1089 234  LEU C CA  
10881 C  C   . LEU C 234  ? 0.9396 1.0410 0.9469 0.2579  -0.0348 -0.1080 234  LEU C C   
10882 O  O   . LEU C 234  ? 0.9697 1.0738 0.9844 0.2518  -0.0349 -0.1056 234  LEU C O   
10883 C  CB  . LEU C 234  ? 0.9203 1.0468 0.9318 0.2623  -0.0294 -0.1091 234  LEU C CB  
10884 C  CG  . LEU C 234  ? 0.9802 1.1197 0.9978 0.2579  -0.0261 -0.1082 234  LEU C CG  
10885 C  CD1 . LEU C 234  ? 0.9992 1.1527 1.0172 0.2647  -0.0225 -0.1094 234  LEU C CD1 
10886 C  CD2 . LEU C 234  ? 1.0187 1.1670 1.0474 0.2495  -0.0250 -0.1052 234  LEU C CD2 
10887 N  N   . ALA C 235  ? 0.9023 0.9940 0.9005 0.2657  -0.0362 -0.1099 235  ALA C N   
10888 C  CA  . ALA C 235  ? 0.8599 0.9424 0.8559 0.2670  -0.0378 -0.1090 235  ALA C CA  
10889 C  C   . ALA C 235  ? 0.8439 0.9106 0.8387 0.2595  -0.0401 -0.1083 235  ALA C C   
10890 O  O   . ALA C 235  ? 0.9069 0.9705 0.9051 0.2560  -0.0406 -0.1062 235  ALA C O   
10891 C  CB  . ALA C 235  ? 0.9583 1.0325 0.9435 0.2775  -0.0385 -0.1112 235  ALA C CB  
10892 N  N   . GLY C 236  ? 0.7263 0.7828 0.7162 0.2571  -0.0417 -0.1101 236  GLY C N   
10893 C  CA  . GLY C 236  ? 0.7596 0.8023 0.7493 0.2496  -0.0439 -0.1098 236  GLY C CA  
10894 C  C   . GLY C 236  ? 0.8053 0.8567 0.8062 0.2404  -0.0432 -0.1071 236  GLY C C   
10895 O  O   . GLY C 236  ? 0.8237 0.8666 0.8270 0.2341  -0.0444 -0.1059 236  GLY C O   
10896 N  N   . LEU C 237  ? 1.1715 1.2396 1.1794 0.2394  -0.0410 -0.1060 237  LEU C N   
10897 C  CA  . LEU C 237  ? 1.1281 1.2048 1.1462 0.2311  -0.0400 -0.1033 237  LEU C CA  
10898 C  C   . LEU C 237  ? 1.2120 1.2972 1.2367 0.2305  -0.0385 -0.1007 237  LEU C C   
10899 O  O   . LEU C 237  ? 1.2940 1.3791 1.3250 0.2238  -0.0385 -0.0984 237  LEU C O   
10900 C  CB  . LEU C 237  ? 1.0701 1.1594 1.0918 0.2298  -0.0381 -0.1033 237  LEU C CB  
10901 C  CG  . LEU C 237  ? 1.1774 1.2601 1.1946 0.2280  -0.0396 -0.1052 237  LEU C CG  
10902 C  CD1 . LEU C 237  ? 1.2484 1.3428 1.2653 0.2308  -0.0371 -0.1058 237  LEU C CD1 
10903 C  CD2 . LEU C 237  ? 1.2925 1.3721 1.3153 0.2191  -0.0410 -0.1037 237  LEU C CD2 
10904 N  N   . SER C 238  ? 0.6872 0.7801 0.7107 0.2378  -0.0372 -0.1011 238  SER C N   
10905 C  CA  . SER C 238  ? 0.5829 0.6852 0.6127 0.2377  -0.0361 -0.0990 238  SER C CA  
10906 C  C   . SER C 238  ? 0.5015 0.5910 0.5277 0.2383  -0.0378 -0.0981 238  SER C C   
10907 O  O   . SER C 238  ? 0.6489 0.7438 0.6805 0.2364  -0.0372 -0.0960 238  SER C O   
10908 C  CB  . SER C 238  ? 0.5159 0.6319 0.5462 0.2455  -0.0343 -0.1002 238  SER C CB  
10909 O  OG  . SER C 238  ? 0.7157 0.8234 0.7360 0.2541  -0.0354 -0.1026 238  SER C OG  
10910 N  N   . THR C 239  ? 0.7251 0.7974 0.7420 0.2408  -0.0396 -0.0996 239  THR C N   
10911 C  CA  . THR C 239  ? 0.8215 0.8801 0.8342 0.2409  -0.0408 -0.0985 239  THR C CA  
10912 C  C   . THR C 239  ? 0.8494 0.9046 0.8687 0.2313  -0.0408 -0.0960 239  THR C C   
10913 O  O   . THR C 239  ? 0.8911 0.9475 0.9132 0.2303  -0.0403 -0.0938 239  THR C O   
10914 C  CB  . THR C 239  ? 0.8384 0.8786 0.8393 0.2454  -0.0424 -0.1009 239  THR C CB  
10915 O  OG1 . THR C 239  ? 0.9236 0.9668 0.9180 0.2556  -0.0421 -0.1028 239  THR C OG1 
10916 C  CG2 . THR C 239  ? 0.8513 0.8754 0.8479 0.2439  -0.0431 -0.0996 239  THR C CG2 
10917 N  N   . PRO C 240  ? 1.0027 1.0542 1.0245 0.2243  -0.0415 -0.0963 240  PRO C N   
10918 C  CA  . PRO C 240  ? 1.0086 1.0595 1.0378 0.2154  -0.0413 -0.0938 240  PRO C CA  
10919 C  C   . PRO C 240  ? 1.0622 1.1301 1.1011 0.2123  -0.0394 -0.0916 240  PRO C C   
10920 O  O   . PRO C 240  ? 1.1467 1.2148 1.1912 0.2064  -0.0389 -0.0891 240  PRO C O   
10921 C  CB  . PRO C 240  ? 1.0668 1.1112 1.0960 0.2101  -0.0427 -0.0953 240  PRO C CB  
10922 C  CG  . PRO C 240  ? 1.0842 1.1209 1.1039 0.2163  -0.0441 -0.0987 240  PRO C CG  
10923 C  CD  . PRO C 240  ? 1.1006 1.1480 1.1185 0.2243  -0.0427 -0.0990 240  PRO C CD  
10924 N  N   . LEU C 241  ? 0.6448 0.7268 0.6859 0.2157  -0.0382 -0.0924 241  LEU C N   
10925 C  CA  . LEU C 241  ? 0.6355 0.7337 0.6857 0.2126  -0.0361 -0.0905 241  LEU C CA  
10926 C  C   . LEU C 241  ? 0.7357 0.8371 0.7879 0.2143  -0.0357 -0.0888 241  LEU C C   
10927 O  O   . LEU C 241  ? 0.7994 0.9035 0.8577 0.2086  -0.0351 -0.0865 241  LEU C O   
10928 C  CB  . LEU C 241  ? 0.5609 0.6727 0.6123 0.2163  -0.0345 -0.0920 241  LEU C CB  
10929 C  CG  . LEU C 241  ? 0.5482 0.6777 0.6082 0.2149  -0.0321 -0.0907 241  LEU C CG  
10930 C  CD1 . LEU C 241  ? 0.6127 0.7458 0.6801 0.2059  -0.0310 -0.0884 241  LEU C CD1 
10931 C  CD2 . LEU C 241  ? 0.5425 0.6844 0.6028 0.2196  -0.0302 -0.0925 241  LEU C CD2 
10932 N  N   . VAL C 242  ? 0.7199 0.8207 0.7666 0.2226  -0.0362 -0.0901 242  VAL C N   
10933 C  CA  . VAL C 242  ? 0.7228 0.8269 0.7704 0.2253  -0.0362 -0.0888 242  VAL C CA  
10934 C  C   . VAL C 242  ? 0.6899 0.7790 0.7347 0.2221  -0.0370 -0.0868 242  VAL C C   
10935 O  O   . VAL C 242  ? 0.6650 0.7571 0.7133 0.2203  -0.0367 -0.0848 242  VAL C O   
10936 C  CB  . VAL C 242  ? 0.7484 0.8551 0.7900 0.2358  -0.0367 -0.0908 242  VAL C CB  
10937 C  CG1 . VAL C 242  ? 0.6385 0.7275 0.6689 0.2407  -0.0381 -0.0923 242  VAL C CG1 
10938 C  CG2 . VAL C 242  ? 0.8141 0.9258 0.8568 0.2393  -0.0370 -0.0896 242  VAL C CG2 
10939 N  N   . VAL C 243  ? 0.7849 0.8576 0.8233 0.2211  -0.0381 -0.0875 243  VAL C N   
10940 C  CA  . VAL C 243  ? 0.7950 0.8532 0.8313 0.2171  -0.0384 -0.0857 243  VAL C CA  
10941 C  C   . VAL C 243  ? 0.8695 0.9325 0.9150 0.2078  -0.0374 -0.0833 243  VAL C C   
10942 O  O   . VAL C 243  ? 0.8230 0.8835 0.8704 0.2052  -0.0368 -0.0810 243  VAL C O   
10943 C  CB  . VAL C 243  ? 0.7349 0.7752 0.7632 0.2173  -0.0395 -0.0873 243  VAL C CB  
10944 C  CG1 . VAL C 243  ? 0.7074 0.7341 0.7357 0.2110  -0.0393 -0.0854 243  VAL C CG1 
10945 C  CG2 . VAL C 243  ? 0.7627 0.7954 0.7805 0.2269  -0.0402 -0.0891 243  VAL C CG2 
10946 N  N   . SER C 244  ? 1.2272 1.2971 1.2781 0.2030  -0.0372 -0.0839 244  SER C N   
10947 C  CA  . SER C 244  ? 1.2010 1.2755 1.2602 0.1946  -0.0363 -0.0817 244  SER C CA  
10948 C  C   . SER C 244  ? 1.1482 1.2371 1.2140 0.1938  -0.0348 -0.0800 244  SER C C   
10949 O  O   . SER C 244  ? 1.1547 1.2445 1.2256 0.1882  -0.0339 -0.0777 244  SER C O   
10950 C  CB  . SER C 244  ? 1.1205 1.1983 1.1827 0.1906  -0.0365 -0.0829 244  SER C CB  
10951 O  OG  . SER C 244  ? 1.1217 1.2130 1.1856 0.1936  -0.0356 -0.0840 244  SER C OG  
10952 N  N   . VAL C 245  ? 0.7675 0.8680 0.8334 0.1994  -0.0344 -0.0813 245  VAL C N   
10953 C  CA  . VAL C 245  ? 0.7687 0.8836 0.8411 0.1987  -0.0331 -0.0802 245  VAL C CA  
10954 C  C   . VAL C 245  ? 0.7146 0.8243 0.7854 0.1996  -0.0335 -0.0784 245  VAL C C   
10955 O  O   . VAL C 245  ? 0.7112 0.8238 0.7872 0.1943  -0.0327 -0.0763 245  VAL C O   
10956 C  CB  . VAL C 245  ? 0.7183 0.8466 0.7911 0.2050  -0.0327 -0.0823 245  VAL C CB  
10957 C  CG1 . VAL C 245  ? 0.7003 0.8421 0.7789 0.2053  -0.0320 -0.0817 245  VAL C CG1 
10958 C  CG2 . VAL C 245  ? 0.7130 0.8489 0.7889 0.2027  -0.0315 -0.0834 245  VAL C CG2 
10959 N  N   . HIS C 246  ? 1.1422 1.2433 1.2051 0.2066  -0.0348 -0.0792 246  HIS C N   
10960 C  CA  . HIS C 246  ? 1.1960 1.2912 1.2559 0.2084  -0.0351 -0.0774 246  HIS C CA  
10961 C  C   . HIS C 246  ? 1.1772 1.2582 1.2363 0.2021  -0.0346 -0.0751 246  HIS C C   
10962 O  O   . HIS C 246  ? 1.0832 1.1615 1.1425 0.2008  -0.0341 -0.0730 246  HIS C O   
10963 C  CB  . HIS C 246  ? 1.1853 1.2740 1.2359 0.2181  -0.0364 -0.0788 246  HIS C CB  
10964 C  CG  . HIS C 246  ? 1.2496 1.3537 1.3016 0.2249  -0.0368 -0.0809 246  HIS C CG  
10965 N  ND1 . HIS C 246  ? 1.2408 1.3513 1.2931 0.2275  -0.0367 -0.0833 246  HIS C ND1 
10966 C  CD2 . HIS C 246  ? 1.2763 1.3913 1.3299 0.2294  -0.0374 -0.0811 246  HIS C CD2 
10967 C  CE1 . HIS C 246  ? 1.2175 1.3425 1.2720 0.2334  -0.0369 -0.0848 246  HIS C CE1 
10968 N  NE2 . HIS C 246  ? 1.2854 1.4137 1.3410 0.2346  -0.0375 -0.0837 246  HIS C NE2 
10969 N  N   . SER C 247  ? 1.0207 1.0927 1.0789 0.1983  -0.0347 -0.0757 247  SER C N   
10970 C  CA  . SER C 247  ? 0.9623 1.0231 1.0217 0.1914  -0.0340 -0.0737 247  SER C CA  
10971 C  C   . SER C 247  ? 0.9062 0.9768 0.9749 0.1842  -0.0327 -0.0717 247  SER C C   
10972 O  O   . SER C 247  ? 0.9662 1.0308 1.0365 0.1797  -0.0318 -0.0694 247  SER C O   
10973 C  CB  . SER C 247  ? 0.9122 0.9626 0.9692 0.1891  -0.0347 -0.0752 247  SER C CB  
10974 O  OG  . SER C 247  ? 0.8831 0.9234 0.9307 0.1958  -0.0358 -0.0772 247  SER C OG  
10975 N  N   . ILE C 248  ? 0.6963 0.7814 0.7709 0.1830  -0.0324 -0.0726 248  ILE C N   
10976 C  CA  . ILE C 248  ? 0.7516 0.8459 0.8343 0.1765  -0.0311 -0.0707 248  ILE C CA  
10977 C  C   . ILE C 248  ? 0.8313 0.9326 0.9157 0.1779  -0.0305 -0.0694 248  ILE C C   
10978 O  O   . ILE C 248  ? 0.8695 0.9709 0.9576 0.1729  -0.0294 -0.0672 248  ILE C O   
10979 C  CB  . ILE C 248  ? 0.7137 0.8197 0.8012 0.1747  -0.0306 -0.0721 248  ILE C CB  
10980 C  CG1 . ILE C 248  ? 0.7081 0.8068 0.7953 0.1710  -0.0311 -0.0726 248  ILE C CG1 
10981 C  CG2 . ILE C 248  ? 0.6419 0.7598 0.7368 0.1699  -0.0289 -0.0705 248  ILE C CG2 
10982 C  CD1 . ILE C 248  ? 0.6722 0.7795 0.7609 0.1714  -0.0310 -0.0744 248  ILE C CD1 
10983 N  N   . ILE C 249  ? 0.9800 1.0872 1.0615 0.1848  -0.0313 -0.0710 249  ILE C N   
10984 C  CA  . ILE C 249  ? 0.9263 1.0392 1.0084 0.1871  -0.0314 -0.0702 249  ILE C CA  
10985 C  C   . ILE C 249  ? 0.9041 1.0027 0.9806 0.1875  -0.0315 -0.0680 249  ILE C C   
10986 O  O   . ILE C 249  ? 0.9886 1.0897 1.0659 0.1874  -0.0313 -0.0666 249  ILE C O   
10987 C  CB  . ILE C 249  ? 0.9658 1.0880 1.0456 0.1954  -0.0326 -0.0726 249  ILE C CB  
10988 C  CG1 . ILE C 249  ? 1.0312 1.1659 1.1156 0.1952  -0.0320 -0.0747 249  ILE C CG1 
10989 C  CG2 . ILE C 249  ? 0.9908 1.1222 1.0728 0.1972  -0.0330 -0.0722 249  ILE C CG2 
10990 C  CD1 . ILE C 249  ? 1.1060 1.2554 1.1995 0.1895  -0.0304 -0.0743 249  ILE C CD1 
10991 N  N   . SER C 250  ? 0.9777 1.0611 1.0485 0.1879  -0.0316 -0.0678 250  SER C N   
10992 C  CA  . SER C 250  ? 1.0514 1.1203 1.1177 0.1866  -0.0309 -0.0655 250  SER C CA  
10993 C  C   . SER C 250  ? 1.0971 1.1633 1.1694 0.1777  -0.0293 -0.0634 250  SER C C   
10994 O  O   . SER C 250  ? 1.1740 1.2339 1.2455 0.1754  -0.0281 -0.0610 250  SER C O   
10995 C  CB  . SER C 250  ? 1.0545 1.1074 1.1119 0.1905  -0.0314 -0.0663 250  SER C CB  
10996 O  OG  . SER C 250  ? 1.0156 1.0615 1.0752 0.1847  -0.0310 -0.0666 250  SER C OG  
10997 N  N   . LEU C 251  ? 0.9278 0.9987 1.0057 0.1730  -0.0292 -0.0643 251  LEU C N   
10998 C  CA  . LEU C 251  ? 0.9000 0.9687 0.9835 0.1650  -0.0279 -0.0624 251  LEU C CA  
10999 C  C   . LEU C 251  ? 0.9045 0.9827 0.9938 0.1614  -0.0266 -0.0605 251  LEU C C   
11000 O  O   . LEU C 251  ? 0.8577 0.9315 0.9497 0.1561  -0.0252 -0.0583 251  LEU C O   
11001 C  CB  . LEU C 251  ? 0.8202 0.8920 0.9075 0.1617  -0.0284 -0.0640 251  LEU C CB  
11002 C  CG  . LEU C 251  ? 0.9360 0.9954 1.0191 0.1620  -0.0294 -0.0655 251  LEU C CG  
11003 C  CD1 . LEU C 251  ? 0.9315 0.9944 1.0192 0.1577  -0.0300 -0.0667 251  LEU C CD1 
11004 C  CD2 . LEU C 251  ? 0.8855 0.9306 0.9661 0.1595  -0.0284 -0.0637 251  LEU C CD2 
11005 N  N   . ASP C 252  ? 1.4051 1.4962 1.4962 0.1642  -0.0270 -0.0615 252  ASP C N   
11006 C  CA  . ASP C 252  ? 1.4258 1.5259 1.5222 0.1605  -0.0258 -0.0600 252  ASP C CA  
11007 C  C   . ASP C 252  ? 1.4434 1.5360 1.5368 0.1604  -0.0251 -0.0577 252  ASP C C   
11008 O  O   . ASP C 252  ? 1.4560 1.5502 1.5534 0.1554  -0.0237 -0.0558 252  ASP C O   
11009 C  CB  . ASP C 252  ? 1.4959 1.6112 1.5949 0.1636  -0.0264 -0.0620 252  ASP C CB  
11010 C  CG  . ASP C 252  ? 1.6193 1.7350 1.7126 0.1715  -0.0281 -0.0633 252  ASP C CG  
11011 O  OD1 . ASP C 252  ? 1.6640 1.7673 1.7507 0.1746  -0.0285 -0.0623 252  ASP C OD1 
11012 O  OD2 . ASP C 252  ? 1.6266 1.7551 1.7221 0.1747  -0.0288 -0.0653 252  ASP C OD2 
11013 N  N   . PHE C 253  ? 0.8770 0.9606 0.9629 0.1662  -0.0260 -0.0578 253  PHE C N   
11014 C  CA  . PHE C 253  ? 0.7828 0.8568 0.8646 0.1664  -0.0250 -0.0553 253  PHE C CA  
11015 C  C   . PHE C 253  ? 0.8290 0.8881 0.9091 0.1624  -0.0234 -0.0536 253  PHE C C   
11016 O  O   . PHE C 253  ? 0.8236 0.8772 0.9043 0.1588  -0.0215 -0.0510 253  PHE C O   
11017 C  CB  . PHE C 253  ? 0.7656 0.8361 0.8391 0.1747  -0.0264 -0.0560 253  PHE C CB  
11018 C  CG  . PHE C 253  ? 0.7849 0.8705 0.8600 0.1795  -0.0283 -0.0584 253  PHE C CG  
11019 C  CD1 . PHE C 253  ? 0.7644 0.8625 0.8451 0.1772  -0.0283 -0.0584 253  PHE C CD1 
11020 C  CD2 . PHE C 253  ? 0.9045 0.9916 0.9756 0.1864  -0.0301 -0.0608 253  PHE C CD2 
11021 C  CE1 . PHE C 253  ? 0.7958 0.9085 0.8788 0.1811  -0.0300 -0.0609 253  PHE C CE1 
11022 C  CE2 . PHE C 253  ? 0.9443 1.0462 1.0176 0.1909  -0.0317 -0.0631 253  PHE C CE2 
11023 C  CZ  . PHE C 253  ? 0.8826 0.9977 0.9623 0.1880  -0.0317 -0.0632 253  PHE C CZ  
11024 N  N   . ALA C 254  ? 0.6524 0.7052 0.7308 0.1629  -0.0240 -0.0550 254  ALA C N   
11025 C  CA  . ALA C 254  ? 0.6525 0.6911 0.7294 0.1593  -0.0226 -0.0538 254  ALA C CA  
11026 C  C   . ALA C 254  ? 0.7397 0.7811 0.8250 0.1511  -0.0213 -0.0527 254  ALA C C   
11027 O  O   . ALA C 254  ? 0.7102 0.7416 0.7958 0.1472  -0.0195 -0.0511 254  ALA C O   
11028 C  CB  . ALA C 254  ? 0.7853 0.8166 0.8579 0.1621  -0.0239 -0.0562 254  ALA C CB  
11029 N  N   . ILE C 255  ? 0.9116 0.9662 1.0035 0.1487  -0.0219 -0.0535 255  ILE C N   
11030 C  CA  . ILE C 255  ? 0.8582 0.9156 0.9574 0.1417  -0.0207 -0.0523 255  ILE C CA  
11031 C  C   . ILE C 255  ? 0.8884 0.9452 0.9894 0.1386  -0.0185 -0.0494 255  ILE C C   
11032 O  O   . ILE C 255  ? 0.8695 0.9225 0.9744 0.1334  -0.0169 -0.0477 255  ILE C O   
11033 C  CB  . ILE C 255  ? 0.7894 0.8600 0.8937 0.1405  -0.0217 -0.0539 255  ILE C CB  
11034 C  CG1 . ILE C 255  ? 0.8787 0.9481 0.9814 0.1426  -0.0235 -0.0567 255  ILE C CG1 
11035 C  CG2 . ILE C 255  ? 0.7863 0.8611 0.8976 0.1340  -0.0203 -0.0523 255  ILE C CG2 
11036 C  CD1 . ILE C 255  ? 0.8976 0.9560 1.0001 0.1397  -0.0237 -0.0570 255  ILE C CD1 
11037 N  N   . SER C 256  ? 0.8224 0.8827 0.9204 0.1421  -0.0185 -0.0488 256  SER C N   
11038 C  CA  . SER C 256  ? 0.7080 0.7681 0.8069 0.1397  -0.0166 -0.0462 256  SER C CA  
11039 C  C   . SER C 256  ? 0.7171 0.7626 0.8120 0.1389  -0.0146 -0.0439 256  SER C C   
11040 O  O   . SER C 256  ? 0.6814 0.7168 0.7724 0.1404  -0.0147 -0.0445 256  SER C O   
11041 C  CB  . SER C 256  ? 0.7574 0.8247 0.8534 0.1442  -0.0176 -0.0467 256  SER C CB  
11042 O  OG  . SER C 256  ? 0.7987 0.8569 0.8866 0.1496  -0.0179 -0.0462 256  SER C OG  
11043 N  N   . GLN C 257  ? 1.0621 1.1064 1.1577 0.1365  -0.0125 -0.0414 257  GLN C N   
11044 C  CA  . GLN C 257  ? 0.9448 0.9759 1.0368 0.1353  -0.0099 -0.0389 257  GLN C CA  
11045 C  C   . GLN C 257  ? 0.8106 0.8359 0.8940 0.1407  -0.0096 -0.0377 257  GLN C C   
11046 O  O   . GLN C 257  ? 0.8918 0.9059 0.9713 0.1402  -0.0070 -0.0353 257  GLN C O   
11047 C  CB  . GLN C 257  ? 0.9141 0.9463 1.0122 0.1290  -0.0074 -0.0366 257  GLN C CB  
11048 C  CG  . GLN C 257  ? 0.9930 1.0297 1.0993 0.1238  -0.0075 -0.0374 257  GLN C CG  
11049 C  CD  . GLN C 257  ? 0.9350 0.9721 1.0467 0.1183  -0.0048 -0.0349 257  GLN C CD  
11050 O  OE1 . GLN C 257  ? 0.8381 0.8785 0.9495 0.1180  -0.0037 -0.0334 257  GLN C OE1 
11051 N  NE2 . GLN C 257  ? 0.9789 1.0126 1.0956 0.1141  -0.0039 -0.0348 257  GLN C NE2 
11052 N  N   . VAL C 258  ? 0.5751 0.6081 0.6556 0.1460  -0.0121 -0.0394 258  VAL C N   
11053 C  CA  . VAL C 258  ? 0.6831 0.7118 0.7551 0.1518  -0.0123 -0.0386 258  VAL C CA  
11054 C  C   . VAL C 258  ? 0.7317 0.7446 0.7951 0.1556  -0.0113 -0.0378 258  VAL C C   
11055 O  O   . VAL C 258  ? 0.8722 0.8819 0.9348 0.1569  -0.0124 -0.0396 258  VAL C O   
11056 C  CB  . VAL C 258  ? 0.6467 0.6879 0.7181 0.1571  -0.0157 -0.0412 258  VAL C CB  
11057 C  CG1 . VAL C 258  ? 0.6878 0.7272 0.7517 0.1626  -0.0163 -0.0405 258  VAL C CG1 
11058 C  CG2 . VAL C 258  ? 0.5025 0.5590 0.5831 0.1525  -0.0163 -0.0424 258  VAL C CG2 
11059 N  N   . PRO C 259  ? 0.7593 0.7610 0.8156 0.1574  -0.0091 -0.0352 259  PRO C N   
11060 C  CA  . PRO C 259  ? 0.9865 0.9713 1.0341 0.1603  -0.0074 -0.0342 259  PRO C CA  
11061 C  C   . PRO C 259  ? 1.0857 1.0688 1.1266 0.1677  -0.0102 -0.0365 259  PRO C C   
11062 O  O   . PRO C 259  ? 1.0650 1.0384 1.1033 0.1678  -0.0096 -0.0372 259  PRO C O   
11063 C  CB  . PRO C 259  ? 1.0901 1.0660 1.1302 0.1624  -0.0050 -0.0311 259  PRO C CB  
11064 C  CG  . PRO C 259  ? 0.9879 0.9732 1.0355 0.1571  -0.0041 -0.0300 259  PRO C CG  
11065 C  CD  . PRO C 259  ? 0.9283 0.9311 0.9841 0.1561  -0.0076 -0.0330 259  PRO C CD  
11066 N  N   . GLY C 260  ? 0.7495 0.7421 0.7877 0.1738  -0.0132 -0.0380 260  GLY C N   
11067 C  CA  . GLY C 260  ? 0.7497 0.7421 0.7820 0.1814  -0.0158 -0.0404 260  GLY C CA  
11068 C  C   . GLY C 260  ? 0.8461 0.8490 0.8853 0.1801  -0.0181 -0.0435 260  GLY C C   
11069 O  O   . GLY C 260  ? 0.8850 0.8865 0.9194 0.1861  -0.0199 -0.0455 260  GLY C O   
11070 N  N   . TRP C 261  ? 0.9902 1.0029 1.0401 0.1729  -0.0178 -0.0439 261  TRP C N   
11071 C  CA  . TRP C 261  ? 0.8730 0.8962 0.9294 0.1715  -0.0197 -0.0467 261  TRP C CA  
11072 C  C   . TRP C 261  ? 0.9865 1.0017 1.0455 0.1667  -0.0185 -0.0469 261  TRP C C   
11073 O  O   . TRP C 261  ? 1.0067 1.0233 1.0655 0.1686  -0.0202 -0.0494 261  TRP C O   
11074 C  CB  . TRP C 261  ? 0.7637 0.8034 0.8296 0.1671  -0.0203 -0.0472 261  TRP C CB  
11075 C  CG  . TRP C 261  ? 0.7150 0.7667 0.7802 0.1720  -0.0224 -0.0486 261  TRP C CG  
11076 C  CD1 . TRP C 261  ? 0.8115 0.8606 0.8686 0.1799  -0.0239 -0.0490 261  TRP C CD1 
11077 C  CD2 . TRP C 261  ? 0.6909 0.7591 0.7639 0.1695  -0.0234 -0.0499 261  TRP C CD2 
11078 N  NE1 . TRP C 261  ? 0.8660 0.9300 0.9260 0.1824  -0.0260 -0.0507 261  TRP C NE1 
11079 C  CE2 . TRP C 261  ? 0.8012 0.8769 0.8710 0.1757  -0.0255 -0.0513 261  TRP C CE2 
11080 C  CE3 . TRP C 261  ? 0.6880 0.7652 0.7701 0.1626  -0.0225 -0.0500 261  TRP C CE3 
11081 C  CZ2 . TRP C 261  ? 0.8659 0.9581 0.9420 0.1746  -0.0268 -0.0531 261  TRP C CZ2 
11082 C  CZ3 . TRP C 261  ? 0.7311 0.8232 0.8184 0.1617  -0.0234 -0.0515 261  TRP C CZ3 
11083 C  CH2 . TRP C 261  ? 0.8249 0.9246 0.9096 0.1673  -0.0255 -0.0531 261  TRP C CH2 
11084 N  N   . GLN C 262  ? 1.0902 1.0975 1.1517 0.1605  -0.0158 -0.0447 262  GLN C N   
11085 C  CA  . GLN C 262  ? 1.0516 1.0515 1.1160 0.1557  -0.0149 -0.0452 262  GLN C CA  
11086 C  C   . GLN C 262  ? 1.1365 1.1199 1.1912 0.1597  -0.0142 -0.0453 262  GLN C C   
11087 O  O   . GLN C 262  ? 1.2389 1.2089 1.2899 0.1578  -0.0113 -0.0431 262  GLN C O   
11088 C  CB  . GLN C 262  ? 1.0558 1.0539 1.1268 0.1478  -0.0121 -0.0429 262  GLN C CB  
11089 C  CG  . GLN C 262  ? 1.0012 0.9925 1.0761 0.1426  -0.0114 -0.0437 262  GLN C CG  
11090 C  CD  . GLN C 262  ? 1.0944 1.0949 1.1800 0.1356  -0.0111 -0.0436 262  GLN C CD  
11091 O  OE1 . GLN C 262  ? 1.1861 1.1962 1.2759 0.1341  -0.0108 -0.0424 262  GLN C OE1 
11092 N  NE2 . GLN C 262  ? 1.1046 1.1019 1.1944 0.1314  -0.0113 -0.0450 262  GLN C NE2 
11093 N  N   . VAL C 263  ? 0.9076 0.8920 0.9579 0.1655  -0.0166 -0.0479 263  VAL C N   
11094 C  CA  . VAL C 263  ? 0.9587 0.9276 0.9994 0.1696  -0.0163 -0.0485 263  VAL C CA  
11095 C  C   . VAL C 263  ? 0.9397 0.9105 0.9832 0.1685  -0.0182 -0.0517 263  VAL C C   
11096 O  O   . VAL C 263  ? 0.9437 0.9274 0.9904 0.1709  -0.0208 -0.0539 263  VAL C O   
11097 C  CB  . VAL C 263  ? 0.9854 0.9522 1.0158 0.1794  -0.0175 -0.0486 263  VAL C CB  
11098 C  CG1 . VAL C 263  ? 0.9624 0.9130 0.9824 0.1841  -0.0172 -0.0495 263  VAL C CG1 
11099 C  CG2 . VAL C 263  ? 1.0008 0.9652 1.0277 0.1807  -0.0158 -0.0456 263  VAL C CG2 
11100 N  N   . THR C 264  ? 0.7900 0.7476 0.8322 0.1648  -0.0169 -0.0521 264  THR C N   
11101 C  CA  . THR C 264  ? 0.7062 0.6654 0.7521 0.1622  -0.0187 -0.0552 264  THR C CA  
11102 C  C   . THR C 264  ? 0.7719 0.7292 0.8101 0.1699  -0.0211 -0.0579 264  THR C C   
11103 O  O   . THR C 264  ? 0.8356 0.7989 0.8769 0.1694  -0.0233 -0.0607 264  THR C O   
11104 C  CB  . THR C 264  ? 0.7116 0.6575 0.7588 0.1557  -0.0166 -0.0551 264  THR C CB  
11105 O  OG1 . THR C 264  ? 0.8442 0.7912 0.8977 0.1494  -0.0140 -0.0522 264  THR C OG1 
11106 C  CG2 . THR C 264  ? 0.7729 0.7231 0.8262 0.1516  -0.0188 -0.0582 264  THR C CG2 
11107 N  N   . VAL C 265  ? 1.0391 0.9885 1.0669 0.1773  -0.0207 -0.0572 265  VAL C N   
11108 C  CA  . VAL C 265  ? 1.0346 0.9804 1.0540 0.1852  -0.0227 -0.0596 265  VAL C CA  
11109 C  C   . VAL C 265  ? 1.0231 0.9863 1.0443 0.1912  -0.0252 -0.0608 265  VAL C C   
11110 O  O   . VAL C 265  ? 1.0825 1.0454 1.0969 0.1991  -0.0268 -0.0626 265  VAL C O   
11111 C  CB  . VAL C 265  ? 1.0352 0.9622 1.0414 0.1908  -0.0209 -0.0584 265  VAL C CB  
11112 C  CG1 . VAL C 265  ? 1.0634 0.9942 1.0648 0.1973  -0.0208 -0.0562 265  VAL C CG1 
11113 C  CG2 . VAL C 265  ? 1.0208 0.9387 1.0181 0.1967  -0.0224 -0.0612 265  VAL C CG2 
11114 N  N   . PHE C 266  ? 1.0690 1.0475 1.0997 0.1874  -0.0254 -0.0598 266  PHE C N   
11115 C  CA  . PHE C 266  ? 1.0952 1.0909 1.1287 0.1921  -0.0274 -0.0609 266  PHE C CA  
11116 C  C   . PHE C 266  ? 1.1078 1.1118 1.1428 0.1948  -0.0296 -0.0642 266  PHE C C   
11117 O  O   . PHE C 266  ? 1.1341 1.1459 1.1661 0.2021  -0.0311 -0.0656 266  PHE C O   
11118 C  CB  . PHE C 266  ? 1.1038 1.1130 1.1471 0.1864  -0.0268 -0.0593 266  PHE C CB  
11119 C  CG  . PHE C 266  ? 1.0742 1.0830 1.1145 0.1887  -0.0259 -0.0569 266  PHE C CG  
11120 C  CD1 . PHE C 266  ? 1.1394 1.1351 1.1689 0.1950  -0.0254 -0.0559 266  PHE C CD1 
11121 C  CD2 . PHE C 266  ? 1.1272 1.1483 1.1751 0.1849  -0.0256 -0.0557 266  PHE C CD2 
11122 C  CE1 . PHE C 266  ? 1.1698 1.1648 1.1957 0.1976  -0.0248 -0.0538 266  PHE C CE1 
11123 C  CE2 . PHE C 266  ? 1.2188 1.2394 1.2635 0.1872  -0.0251 -0.0537 266  PHE C CE2 
11124 C  CZ  . PHE C 266  ? 1.1772 1.1850 1.2109 0.1937  -0.0248 -0.0528 266  PHE C CZ  
11125 N  N   . PRO C 267  ? 0.9490 0.9524 0.9882 0.1896  -0.0299 -0.0657 267  PRO C N   
11126 C  CA  . PRO C 267  ? 0.9545 0.9661 0.9945 0.1927  -0.0318 -0.0688 267  PRO C CA  
11127 C  C   . PRO C 267  ? 1.0330 1.0363 1.0623 0.2016  -0.0328 -0.0707 267  PRO C C   
11128 O  O   . PRO C 267  ? 1.0639 1.0779 1.0924 0.2080  -0.0341 -0.0722 267  PRO C O   
11129 C  CB  . PRO C 267  ? 0.9214 0.9296 0.9661 0.1855  -0.0319 -0.0699 267  PRO C CB  
11130 C  CG  . PRO C 267  ? 0.9134 0.9211 0.9645 0.1778  -0.0301 -0.0672 267  PRO C CG  
11131 C  CD  . PRO C 267  ? 0.9447 0.9437 0.9902 0.1804  -0.0286 -0.0647 267  PRO C CD  
11132 N  N   . PRO C 268  ? 0.8434 0.8280 0.8643 0.2026  -0.0322 -0.0707 268  PRO C N   
11133 C  CA  . PRO C 268  ? 0.7376 0.7140 0.7474 0.2118  -0.0331 -0.0724 268  PRO C CA  
11134 C  C   . PRO C 268  ? 0.8043 0.7821 0.8082 0.2197  -0.0331 -0.0710 268  PRO C C   
11135 O  O   . PRO C 268  ? 0.8750 0.8558 0.8732 0.2284  -0.0345 -0.0727 268  PRO C O   
11136 C  CB  . PRO C 268  ? 0.7055 0.6604 0.7083 0.2093  -0.0320 -0.0726 268  PRO C CB  
11137 C  CG  . PRO C 268  ? 0.6699 0.6249 0.6819 0.1985  -0.0310 -0.0716 268  PRO C CG  
11138 C  CD  . PRO C 268  ? 0.7981 0.7677 0.8185 0.1958  -0.0304 -0.0692 268  PRO C CD  
11139 N  N   . TYR C 269  ? 1.2414 1.2173 1.2464 0.2172  -0.0316 -0.0680 269  TYR C N   
11140 C  CA  . TYR C 269  ? 1.3059 1.2842 1.3056 0.2247  -0.0319 -0.0668 269  TYR C CA  
11141 C  C   . TYR C 269  ? 1.2871 1.2874 1.2934 0.2283  -0.0339 -0.0683 269  TYR C C   
11142 O  O   . TYR C 269  ? 1.2966 1.3009 1.2974 0.2373  -0.0353 -0.0691 269  TYR C O   
11143 C  CB  . TYR C 269  ? 1.2920 1.2645 1.2923 0.2202  -0.0299 -0.0633 269  TYR C CB  
11144 C  CG  . TYR C 269  ? 1.3377 1.3151 1.3341 0.2268  -0.0304 -0.0619 269  TYR C CG  
11145 C  CD1 . TYR C 269  ? 1.4190 1.3852 1.4027 0.2362  -0.0307 -0.0617 269  TYR C CD1 
11146 C  CD2 . TYR C 269  ? 1.2671 1.2599 1.2722 0.2236  -0.0308 -0.0610 269  TYR C CD2 
11147 C  CE1 . TYR C 269  ? 1.4181 1.3891 1.3979 0.2426  -0.0316 -0.0606 269  TYR C CE1 
11148 C  CE2 . TYR C 269  ? 1.3855 1.3831 1.3872 0.2294  -0.0317 -0.0601 269  TYR C CE2 
11149 C  CZ  . TYR C 269  ? 1.4761 1.4631 1.4652 0.2390  -0.0322 -0.0599 269  TYR C CZ  
11150 O  OH  . TYR C 269  ? 1.5213 1.5134 1.5067 0.2453  -0.0335 -0.0592 269  TYR C OH  
11151 N  N   . PHE C 270  ? 1.0681 1.0828 1.0860 0.2214  -0.0340 -0.0687 270  PHE C N   
11152 C  CA  . PHE C 270  ? 1.0666 1.1022 1.0914 0.2238  -0.0354 -0.0702 270  PHE C CA  
11153 C  C   . PHE C 270  ? 1.1384 1.1787 1.1607 0.2299  -0.0368 -0.0734 270  PHE C C   
11154 O  O   . PHE C 270  ? 1.2650 1.3182 1.2880 0.2364  -0.0380 -0.0749 270  PHE C O   
11155 C  CB  . PHE C 270  ? 0.9483 0.9962 0.9852 0.2145  -0.0346 -0.0696 270  PHE C CB  
11156 C  CG  . PHE C 270  ? 0.9498 1.0044 0.9911 0.2117  -0.0340 -0.0675 270  PHE C CG  
11157 C  CD1 . PHE C 270  ? 1.0067 1.0483 1.0438 0.2099  -0.0328 -0.0647 270  PHE C CD1 
11158 C  CD2 . PHE C 270  ? 0.9765 1.0500 1.0260 0.2108  -0.0346 -0.0683 270  PHE C CD2 
11159 C  CE1 . PHE C 270  ? 1.0022 1.0495 1.0427 0.2076  -0.0322 -0.0628 270  PHE C CE1 
11160 C  CE2 . PHE C 270  ? 0.9824 1.0617 1.0356 0.2082  -0.0342 -0.0666 270  PHE C CE2 
11161 C  CZ  . PHE C 270  ? 1.0106 1.0767 1.0591 0.2067  -0.0332 -0.0638 270  PHE C CZ  
11162 N  N   . VAL C 271  ? 0.9049 0.9355 0.9248 0.2279  -0.0366 -0.0746 271  VAL C N   
11163 C  CA  . VAL C 271  ? 0.8621 0.8954 0.8785 0.2339  -0.0377 -0.0776 271  VAL C CA  
11164 C  C   . VAL C 271  ? 0.9005 0.9263 0.9056 0.2448  -0.0386 -0.0783 271  VAL C C   
11165 O  O   . VAL C 271  ? 0.9747 1.0114 0.9790 0.2522  -0.0397 -0.0803 271  VAL C O   
11166 C  CB  . VAL C 271  ? 0.8864 0.9090 0.9016 0.2292  -0.0376 -0.0788 271  VAL C CB  
11167 C  CG1 . VAL C 271  ? 0.9254 0.9462 0.9338 0.2367  -0.0387 -0.0818 271  VAL C CG1 
11168 C  CG2 . VAL C 271  ? 0.8293 0.8626 0.8557 0.2202  -0.0371 -0.0787 271  VAL C CG2 
11169 N  N   . ALA C 272  ? 0.7854 0.7925 0.7814 0.2460  -0.0379 -0.0765 272  ALA C N   
11170 C  CA  . ALA C 272  ? 0.7937 0.7917 0.7775 0.2567  -0.0385 -0.0769 272  ALA C CA  
11171 C  C   . ALA C 272  ? 0.8835 0.8958 0.8690 0.2630  -0.0397 -0.0765 272  ALA C C   
11172 O  O   . ALA C 272  ? 0.9534 0.9694 0.9332 0.2731  -0.0411 -0.0781 272  ALA C O   
11173 C  CB  . ALA C 272  ? 0.6596 0.6338 0.6334 0.2559  -0.0369 -0.0748 272  ALA C CB  
11174 N  N   . GLY C 273  ? 1.1304 1.1512 1.1236 0.2573  -0.0393 -0.0745 273  GLY C N   
11175 C  CA  . GLY C 273  ? 1.1689 1.2042 1.1645 0.2625  -0.0407 -0.0745 273  GLY C CA  
11176 C  C   . GLY C 273  ? 1.1503 1.2080 1.1545 0.2648  -0.0420 -0.0774 273  GLY C C   
11177 O  O   . GLY C 273  ? 1.2062 1.2746 1.2092 0.2731  -0.0437 -0.0788 273  GLY C O   
11178 N  N   . ALA C 274  ? 1.1060 1.1714 1.1190 0.2576  -0.0412 -0.0783 274  ALA C N   
11179 C  CA  . ALA C 274  ? 1.1795 1.2655 1.2006 0.2592  -0.0418 -0.0809 274  ALA C CA  
11180 C  C   . ALA C 274  ? 1.2253 1.3109 1.2391 0.2697  -0.0429 -0.0835 274  ALA C C   
11181 O  O   . ALA C 274  ? 1.2591 1.3597 1.2750 0.2765  -0.0441 -0.0853 274  ALA C O   
11182 C  CB  . ALA C 274  ? 1.1350 1.2260 1.1649 0.2497  -0.0404 -0.0812 274  ALA C CB  
11183 N  N   . VAL C 275  ? 1.4355 1.5042 1.4407 0.2711  -0.0425 -0.0838 275  VAL C N   
11184 C  CA  . VAL C 275  ? 1.4198 1.4862 1.4169 0.2813  -0.0434 -0.0862 275  VAL C CA  
11185 C  C   . VAL C 275  ? 1.4361 1.4971 1.4234 0.2913  -0.0446 -0.0857 275  VAL C C   
11186 O  O   . VAL C 275  ? 1.5129 1.5781 1.4949 0.2971  -0.0454 -0.0868 275  VAL C O   
11187 C  CB  . VAL C 275  ? 1.3269 1.3750 1.3167 0.2796  -0.0427 -0.0868 275  VAL C CB  
11188 C  CG1 . VAL C 275  ? 1.4302 1.4555 1.4115 0.2770  -0.0420 -0.0845 275  VAL C CG1 
11189 C  CG2 . VAL C 275  ? 1.3194 1.3657 1.3010 0.2897  -0.0434 -0.0895 275  VAL C CG2 
11190 N  N   . PHE C 276  ? 1.3435 1.3944 1.3273 0.2901  -0.0445 -0.0832 276  PHE C N   
11191 C  CA  . PHE C 276  ? 1.3768 1.4234 1.3512 0.2974  -0.0456 -0.0820 276  PHE C CA  
11192 C  C   . PHE C 276  ? 1.3916 1.4614 1.3729 0.2987  -0.0472 -0.0828 276  PHE C C   
11193 O  O   . PHE C 276  ? 1.3326 1.4064 1.3079 0.3051  -0.0484 -0.0837 276  PHE C O   
11194 C  CB  . PHE C 276  ? 1.4084 1.4406 1.3786 0.2960  -0.0449 -0.0792 276  PHE C CB  
11195 C  CG  . PHE C 276  ? 1.3974 1.4203 1.3551 0.3031  -0.0457 -0.0775 276  PHE C CG  
11196 C  CD1 . PHE C 276  ? 1.4481 1.4628 1.3938 0.3104  -0.0462 -0.0780 276  PHE C CD1 
11197 C  CD2 . PHE C 276  ? 1.4162 1.4383 1.3736 0.3025  -0.0459 -0.0752 276  PHE C CD2 
11198 C  CE1 . PHE C 276  ? 1.5000 1.5059 1.4335 0.3171  -0.0469 -0.0763 276  PHE C CE1 
11199 C  CE2 . PHE C 276  ? 1.4178 1.4312 1.3630 0.3092  -0.0466 -0.0736 276  PHE C CE2 
11200 C  CZ  . PHE C 276  ? 1.5150 1.5203 1.4482 0.3166  -0.0471 -0.0741 276  PHE C CZ  
11201 N  N   . ALA C 277  ? 1.2337 1.3188 1.2275 0.2926  -0.0472 -0.0827 277  ALA C N   
11202 C  CA  . ALA C 277  ? 1.1452 1.2525 1.1466 0.2929  -0.0486 -0.0839 277  ALA C CA  
11203 C  C   . ALA C 277  ? 1.1398 1.2620 1.1462 0.2935  -0.0485 -0.0865 277  ALA C C   
11204 O  O   . ALA C 277  ? 1.1349 1.2718 1.1431 0.2967  -0.0497 -0.0878 277  ALA C O   
11205 C  CB  . ALA C 277  ? 1.0759 1.1950 1.0895 0.2855  -0.0484 -0.0834 277  ALA C CB  
11206 N  N   . GLY C 278  ? 0.9821 1.1008 0.9907 0.2906  -0.0469 -0.0873 278  GLY C N   
11207 C  CA  . GLY C 278  ? 0.9851 1.1168 0.9977 0.2913  -0.0463 -0.0896 278  GLY C CA  
11208 C  C   . GLY C 278  ? 0.9831 1.1101 0.9846 0.3000  -0.0473 -0.0905 278  GLY C C   
11209 O  O   . GLY C 278  ? 1.0163 1.1589 1.0209 0.3027  -0.0478 -0.0921 278  GLY C O   
11210 N  N   . PHE C 279  ? 1.1423 1.2473 1.1308 0.3045  -0.0474 -0.0895 279  PHE C N   
11211 C  CA  . PHE C 279  ? 1.0800 1.1784 1.0564 0.3132  -0.0483 -0.0900 279  PHE C CA  
11212 C  C   . PHE C 279  ? 1.1307 1.2377 1.1047 0.3182  -0.0502 -0.0897 279  PHE C C   
11213 O  O   . PHE C 279  ? 1.1146 1.2276 1.0842 0.3246  -0.0511 -0.0910 279  PHE C O   
11214 C  CB  . PHE C 279  ? 1.0944 1.1660 1.0568 0.3164  -0.0478 -0.0888 279  PHE C CB  
11215 C  CG  . PHE C 279  ? 1.1487 1.2119 1.1083 0.3160  -0.0467 -0.0904 279  PHE C CG  
11216 C  CD1 . PHE C 279  ? 1.1851 1.2466 1.1368 0.3225  -0.0469 -0.0919 279  PHE C CD1 
11217 C  CD2 . PHE C 279  ? 1.1784 1.2352 1.1431 0.3094  -0.0455 -0.0906 279  PHE C CD2 
11218 C  CE1 . PHE C 279  ? 1.1640 1.2174 1.1124 0.3223  -0.0460 -0.0935 279  PHE C CE1 
11219 C  CE2 . PHE C 279  ? 1.2241 1.2730 1.1858 0.3093  -0.0448 -0.0924 279  PHE C CE2 
11220 C  CZ  . PHE C 279  ? 1.1970 1.2441 1.1504 0.3157  -0.0450 -0.0938 279  PHE C CZ  
11221 N  N   . ALA C 280  ? 1.4405 1.5483 1.4171 0.3158  -0.0510 -0.0881 280  ALA C N   
11222 C  CA  . ALA C 280  ? 1.3574 1.4745 1.3323 0.3204  -0.0532 -0.0882 280  ALA C CA  
11223 C  C   . ALA C 280  ? 1.3854 1.5291 1.3726 0.3188  -0.0539 -0.0907 280  ALA C C   
11224 O  O   . ALA C 280  ? 1.3473 1.5000 1.3316 0.3249  -0.0555 -0.0920 280  ALA C O   
11225 C  CB  . ALA C 280  ? 1.4014 1.5131 1.3764 0.3178  -0.0538 -0.0860 280  ALA C CB  
11226 N  N   . MET C 281  ? 1.2278 1.3842 1.2287 0.3106  -0.0525 -0.0914 281  MET C N   
11227 C  CA  . MET C 281  ? 1.0852 1.2663 1.0983 0.3082  -0.0525 -0.0938 281  MET C CA  
11228 C  C   . MET C 281  ? 1.1937 1.3798 1.2051 0.3121  -0.0516 -0.0957 281  MET C C   
11229 O  O   . MET C 281  ? 1.1940 1.3973 1.2099 0.3145  -0.0523 -0.0977 281  MET C O   
11230 C  CB  . MET C 281  ? 1.1859 1.3771 1.2130 0.2983  -0.0507 -0.0939 281  MET C CB  
11231 C  CG  . MET C 281  ? 1.2344 1.4506 1.2746 0.2947  -0.0509 -0.0960 281  MET C CG  
11232 S  SD  . MET C 281  ? 1.4210 1.6447 1.4629 0.2954  -0.0539 -0.0960 281  MET C SD  
11233 C  CE  . MET C 281  ? 1.2444 1.4970 1.2991 0.2938  -0.0540 -0.0996 281  MET C CE  
11234 N  N   . VAL C 282  ? 1.2769 1.4484 1.2821 0.3128  -0.0501 -0.0952 282  VAL C N   
11235 C  CA  . VAL C 282  ? 1.3173 1.4927 1.3204 0.3166  -0.0491 -0.0970 282  VAL C CA  
11236 C  C   . VAL C 282  ? 1.2491 1.4212 1.2409 0.3264  -0.0509 -0.0975 282  VAL C C   
11237 O  O   . VAL C 282  ? 1.2392 1.4252 1.2332 0.3300  -0.0509 -0.0994 282  VAL C O   
11238 C  CB  . VAL C 282  ? 1.3938 1.5535 1.3924 0.3149  -0.0473 -0.0966 282  VAL C CB  
11239 C  CG1 . VAL C 282  ? 1.2684 1.4271 1.2606 0.3208  -0.0467 -0.0982 282  VAL C CG1 
11240 C  CG2 . VAL C 282  ? 1.4222 1.5902 1.4334 0.3057  -0.0453 -0.0968 282  VAL C CG2 
11241 N  N   . LEU C 283  ? 0.9129 1.0664 0.8921 0.3311  -0.0523 -0.0957 283  LEU C N   
11242 C  CA  . LEU C 283  ? 0.9110 1.0612 0.8788 0.3407  -0.0542 -0.0959 283  LEU C CA  
11243 C  C   . LEU C 283  ? 0.9321 1.1033 0.9068 0.3423  -0.0562 -0.0973 283  LEU C C   
11244 O  O   . LEU C 283  ? 0.9351 1.1154 0.9072 0.3487  -0.0572 -0.0990 283  LEU C O   
11245 C  CB  . LEU C 283  ? 0.8891 1.0151 0.8423 0.3448  -0.0550 -0.0934 283  LEU C CB  
11246 C  CG  . LEU C 283  ? 0.8774 0.9792 0.8198 0.3456  -0.0534 -0.0923 283  LEU C CG  
11247 C  CD1 . LEU C 283  ? 0.8732 0.9529 0.8032 0.3481  -0.0538 -0.0897 283  LEU C CD1 
11248 C  CD2 . LEU C 283  ? 1.0037 1.1028 0.9378 0.3525  -0.0532 -0.0938 283  LEU C CD2 
11249 N  N   . LEU C 284  ? 1.3528 1.5319 1.3364 0.3365  -0.0569 -0.0969 284  LEU C N   
11250 C  CA  . LEU C 284  ? 1.2964 1.4951 1.2868 0.3375  -0.0590 -0.0985 284  LEU C CA  
11251 C  C   . LEU C 284  ? 1.2852 1.5073 1.2878 0.3355  -0.0581 -0.1015 284  LEU C C   
11252 O  O   . LEU C 284  ? 1.2735 1.5109 1.2785 0.3395  -0.0600 -0.1035 284  LEU C O   
11253 C  CB  . LEU C 284  ? 1.3040 1.5056 1.3017 0.3309  -0.0597 -0.0975 284  LEU C CB  
11254 C  CG  . LEU C 284  ? 1.3174 1.5268 1.3140 0.3344  -0.0628 -0.0981 284  LEU C CG  
11255 C  CD1 . LEU C 284  ? 1.3095 1.5011 1.2885 0.3440  -0.0646 -0.0966 284  LEU C CD1 
11256 C  CD2 . LEU C 284  ? 1.3289 1.5403 1.3330 0.3271  -0.0631 -0.0971 284  LEU C CD2 
11257 N  N   . LEU C 285  ? 1.1782 1.4034 1.1883 0.3296  -0.0552 -0.1017 285  LEU C N   
11258 C  CA  . LEU C 285  ? 1.1281 1.3749 1.1502 0.3268  -0.0537 -0.1043 285  LEU C CA  
11259 C  C   . LEU C 285  ? 1.1284 1.3738 1.1448 0.3325  -0.0524 -0.1053 285  LEU C C   
11260 O  O   . LEU C 285  ? 1.1225 1.3861 1.1470 0.3325  -0.0513 -0.1075 285  LEU C O   
11261 C  CB  . LEU C 285  ? 1.1323 1.3856 1.1671 0.3164  -0.0510 -0.1040 285  LEU C CB  
11262 C  CG  . LEU C 285  ? 1.0230 1.2884 1.0689 0.3096  -0.0517 -0.1042 285  LEU C CG  
11263 C  CD1 . LEU C 285  ? 0.9105 1.1824 0.9683 0.2998  -0.0487 -0.1041 285  LEU C CD1 
11264 C  CD2 . LEU C 285  ? 0.9858 1.2719 1.0381 0.3119  -0.0535 -0.1069 285  LEU C CD2 
11265 N  N   . MET C 286  ? 1.0399 1.2641 1.0427 0.3374  -0.0523 -0.1038 286  MET C N   
11266 C  CA  . MET C 286  ? 0.9954 1.2169 0.9918 0.3431  -0.0511 -0.1048 286  MET C CA  
11267 C  C   . MET C 286  ? 0.9975 1.2170 0.9828 0.3536  -0.0534 -0.1054 286  MET C C   
11268 O  O   . MET C 286  ? 0.9952 1.2211 0.9788 0.3585  -0.0527 -0.1070 286  MET C O   
11269 C  CB  . MET C 286  ? 1.0143 1.2138 1.0019 0.3424  -0.0497 -0.1033 286  MET C CB  
11270 C  CG  . MET C 286  ? 1.1059 1.3069 1.0926 0.3441  -0.0474 -0.1046 286  MET C CG  
11271 S  SD  . MET C 286  ? 1.1894 1.4066 1.1925 0.3341  -0.0441 -0.1056 286  MET C SD  
11272 C  CE  . MET C 286  ? 1.0935 1.2950 1.0975 0.3263  -0.0440 -0.1034 286  MET C CE  
11273 N  N   . ILE C 287  ? 0.9733 1.1840 0.9507 0.3574  -0.0561 -0.1042 287  ILE C N   
11274 C  CA  . ILE C 287  ? 1.0077 1.2173 0.9743 0.3677  -0.0584 -0.1049 287  ILE C CA  
11275 C  C   . ILE C 287  ? 1.0321 1.2677 1.0087 0.3695  -0.0593 -0.1078 287  ILE C C   
11276 O  O   . ILE C 287  ? 1.0217 1.2607 0.9928 0.3770  -0.0595 -0.1091 287  ILE C O   
11277 C  CB  . ILE C 287  ? 1.0354 1.2302 0.9916 0.3709  -0.0608 -0.1029 287  ILE C CB  
11278 C  CG1 . ILE C 287  ? 0.9995 1.1661 0.9422 0.3720  -0.0597 -0.1002 287  ILE C CG1 
11279 C  CG2 . ILE C 287  ? 0.9877 1.1874 0.9359 0.3808  -0.0636 -0.1040 287  ILE C CG2 
11280 C  CD1 . ILE C 287  ? 0.9847 1.1353 0.9175 0.3741  -0.0613 -0.0978 287  ILE C CD1 
11281 N  N   . PRO C 288  ? 0.9160 1.1702 0.9068 0.3631  -0.0597 -0.1090 288  PRO C N   
11282 C  CA  . PRO C 288  ? 0.9732 1.2526 0.9743 0.3644  -0.0602 -0.1122 288  PRO C CA  
11283 C  C   . PRO C 288  ? 0.9228 1.2123 0.9310 0.3624  -0.0568 -0.1135 288  PRO C C   
11284 O  O   . PRO C 288  ? 0.9492 1.2521 0.9590 0.3675  -0.0569 -0.1157 288  PRO C O   
11285 C  CB  . PRO C 288  ? 0.9725 1.2666 0.9870 0.3566  -0.0610 -0.1130 288  PRO C CB  
11286 C  CG  . PRO C 288  ? 0.8181 1.0934 0.8252 0.3550  -0.0623 -0.1102 288  PRO C CG  
11287 C  CD  . PRO C 288  ? 0.8319 1.0855 0.8295 0.3553  -0.0601 -0.1078 288  PRO C CD  
11288 N  N   . VAL C 289  ? 0.8885 1.1719 0.9009 0.3552  -0.0538 -0.1123 289  VAL C N   
11289 C  CA  . VAL C 289  ? 0.9148 1.2060 0.9327 0.3535  -0.0504 -0.1134 289  VAL C CA  
11290 C  C   . VAL C 289  ? 0.9407 1.2210 0.9450 0.3630  -0.0504 -0.1134 289  VAL C C   
11291 O  O   . VAL C 289  ? 0.8582 1.1505 0.8655 0.3659  -0.0488 -0.1152 289  VAL C O   
11292 C  CB  . VAL C 289  ? 0.9293 1.2137 0.9524 0.3445  -0.0476 -0.1120 289  VAL C CB  
11293 C  CG1 . VAL C 289  ? 0.8866 1.1719 0.9100 0.3447  -0.0442 -0.1126 289  VAL C CG1 
11294 C  CG2 . VAL C 289  ? 0.9171 1.2176 0.9560 0.3349  -0.0468 -0.1125 289  VAL C CG2 
11295 N  N   . ARG C 290  ? 1.4570 1.7142 1.4460 0.3679  -0.0520 -0.1115 290  ARG C N   
11296 C  CA  . ARG C 290  ? 1.3968 1.6419 1.3717 0.3771  -0.0520 -0.1114 290  ARG C CA  
11297 C  C   . ARG C 290  ? 1.5362 1.7925 1.5079 0.3860  -0.0542 -0.1132 290  ARG C C   
11298 O  O   . ARG C 290  ? 1.6128 1.8738 1.5815 0.3919  -0.0533 -0.1145 290  ARG C O   
11299 C  CB  . ARG C 290  ? 1.4412 1.6582 1.4006 0.3797  -0.0530 -0.1090 290  ARG C CB  
11300 C  CG  . ARG C 290  ? 1.5524 1.7556 1.4950 0.3906  -0.0541 -0.1088 290  ARG C CG  
11301 C  CD  . ARG C 290  ? 1.6286 1.8054 1.5564 0.3930  -0.0553 -0.1063 290  ARG C CD  
11302 N  NE  . ARG C 290  ? 1.6559 1.8183 1.5668 0.4033  -0.0561 -0.1061 290  ARG C NE  
11303 C  CZ  . ARG C 290  ? 1.6835 1.8442 1.5852 0.4114  -0.0586 -0.1059 290  ARG C CZ  
11304 N  NH1 . ARG C 290  ? 1.7468 1.9195 1.6544 0.4107  -0.0607 -0.1061 290  ARG C NH1 
11305 N  NH2 . ARG C 290  ? 1.6371 1.7835 1.5229 0.4205  -0.0589 -0.1056 290  ARG C NH2 
11306 N  N   . THR C 291  ? 1.5506 1.8117 1.5228 0.3875  -0.0572 -0.1133 291  THR C N   
11307 C  CA  . THR C 291  ? 1.6040 1.8738 1.5713 0.3967  -0.0598 -0.1150 291  THR C CA  
11308 C  C   . THR C 291  ? 1.5601 1.8587 1.5425 0.3954  -0.0594 -0.1181 291  THR C C   
11309 O  O   . THR C 291  ? 1.6466 1.9544 1.6259 0.4035  -0.0611 -0.1200 291  THR C O   
11310 C  CB  . THR C 291  ? 1.6629 1.9258 1.6236 0.3994  -0.0634 -0.1140 291  THR C CB  
11311 O  OG1 . THR C 291  ? 1.6755 1.9388 1.6254 0.4106  -0.0659 -0.1150 291  THR C OG1 
11312 C  CG2 . THR C 291  ? 1.6688 1.9505 1.6448 0.3921  -0.0644 -0.1153 291  THR C CG2 
11313 N  N   . PHE C 292  ? 1.0487 1.3615 1.0472 0.3855  -0.0571 -0.1189 292  PHE C N   
11314 C  CA  . PHE C 292  ? 1.0794 1.4194 1.0931 0.3833  -0.0563 -0.1219 292  PHE C CA  
11315 C  C   . PHE C 292  ? 1.1222 1.4686 1.1382 0.3848  -0.0528 -0.1229 292  PHE C C   
11316 O  O   . PHE C 292  ? 1.3125 1.6716 1.3290 0.3913  -0.0531 -0.1250 292  PHE C O   
11317 C  CB  . PHE C 292  ? 1.2353 1.5879 1.2651 0.3718  -0.0553 -0.1223 292  PHE C CB  
11318 C  CG  . PHE C 292  ? 1.2415 1.5973 1.2727 0.3711  -0.0590 -0.1227 292  PHE C CG  
11319 C  CD1 . PHE C 292  ? 1.1238 1.4776 1.1450 0.3805  -0.0628 -0.1234 292  PHE C CD1 
11320 C  CD2 . PHE C 292  ? 1.2119 1.5725 1.2538 0.3613  -0.0586 -0.1224 292  PHE C CD2 
11321 C  CE1 . PHE C 292  ? 1.0678 1.4243 1.0896 0.3803  -0.0663 -0.1239 292  PHE C CE1 
11322 C  CE2 . PHE C 292  ? 1.1384 1.5018 1.1813 0.3608  -0.0621 -0.1228 292  PHE C CE2 
11323 C  CZ  . PHE C 292  ? 1.1052 1.4665 1.1379 0.3704  -0.0660 -0.1236 292  PHE C CZ  
11324 N  N   . TYR C 293  ? 1.4285 1.7662 1.4457 0.3791  -0.0494 -0.1214 293  TYR C N   
11325 C  CA  . TYR C 293  ? 1.5779 1.9184 1.5950 0.3811  -0.0461 -0.1220 293  TYR C CA  
11326 C  C   . TYR C 293  ? 1.5804 1.9008 1.5790 0.3910  -0.0470 -0.1209 293  TYR C C   
11327 O  O   . TYR C 293  ? 1.5881 1.8888 1.5741 0.3941  -0.0495 -0.1191 293  TYR C O   
11328 C  CB  . TYR C 293  ? 1.5125 1.8509 1.5369 0.3718  -0.0422 -0.1210 293  TYR C CB  
11329 C  CG  . TYR C 293  ? 1.5103 1.8665 1.5522 0.3615  -0.0409 -0.1218 293  TYR C CG  
11330 C  CD1 . TYR C 293  ? 1.5252 1.9047 1.5809 0.3586  -0.0382 -0.1241 293  TYR C CD1 
11331 C  CD2 . TYR C 293  ? 1.4941 1.8432 1.5384 0.3547  -0.0421 -0.1203 293  TYR C CD2 
11332 C  CE1 . TYR C 293  ? 1.5316 1.9267 1.6030 0.3490  -0.0368 -0.1249 293  TYR C CE1 
11333 C  CE2 . TYR C 293  ? 1.4707 1.8355 1.5305 0.3453  -0.0409 -0.1211 293  TYR C CE2 
11334 C  CZ  . TYR C 293  ? 1.4764 1.8638 1.5495 0.3424  -0.0382 -0.1234 293  TYR C CZ  
11335 O  OH  . TYR C 293  ? 1.3656 1.7679 1.4537 0.3329  -0.0368 -0.1243 293  TYR C OH  
11336 N  N   . GLY C 294  ? 1.7496 2.0747 1.7463 0.3959  -0.0449 -0.1220 294  GLY C N   
11337 C  CA  . GLY C 294  ? 1.7301 2.0370 1.7095 0.4053  -0.0455 -0.1212 294  GLY C CA  
11338 C  C   . GLY C 294  ? 1.7752 2.0584 1.7454 0.4025  -0.0442 -0.1190 294  GLY C C   
11339 O  O   . GLY C 294  ? 1.8639 2.1400 1.8280 0.4054  -0.0420 -0.1190 294  GLY C O   
11340 N  N   . PHE C 295  ? 1.2453 1.5162 1.2144 0.3971  -0.0455 -0.1172 295  PHE C N   
11341 C  CA  . PHE C 295  ? 1.2892 1.5388 1.2516 0.3932  -0.0443 -0.1154 295  PHE C CA  
11342 C  C   . PHE C 295  ? 1.2789 1.5031 1.2238 0.3989  -0.0468 -0.1136 295  PHE C C   
11343 O  O   . PHE C 295  ? 1.2729 1.4787 1.2128 0.3949  -0.0465 -0.1120 295  PHE C O   
11344 C  CB  . PHE C 295  ? 1.2504 1.5044 1.2253 0.3819  -0.0433 -0.1147 295  PHE C CB  
11345 C  CG  . PHE C 295  ? 1.2639 1.5387 1.2546 0.3753  -0.0401 -0.1160 295  PHE C CG  
11346 C  CD1 . PHE C 295  ? 1.3032 1.5862 1.2944 0.3788  -0.0375 -0.1174 295  PHE C CD1 
11347 C  CD2 . PHE C 295  ? 1.1779 1.4636 1.1825 0.3657  -0.0393 -0.1159 295  PHE C CD2 
11348 C  CE1 . PHE C 295  ? 1.2722 1.5738 1.2776 0.3728  -0.0340 -0.1186 295  PHE C CE1 
11349 C  CE2 . PHE C 295  ? 1.2285 1.5326 1.2470 0.3595  -0.0359 -0.1171 295  PHE C CE2 
11350 C  CZ  . PHE C 295  ? 1.2919 1.6038 1.3108 0.3631  -0.0331 -0.1184 295  PHE C CZ  
11351 N  N   . GLU C 296  ? 1.4398 1.6626 1.3753 0.4082  -0.0492 -0.1139 296  GLU C N   
11352 C  CA  . GLU C 296  ? 1.4768 1.6749 1.3946 0.4141  -0.0512 -0.1122 296  GLU C CA  
11353 C  C   . GLU C 296  ? 1.6173 1.7951 1.5224 0.4172  -0.0496 -0.1117 296  GLU C C   
11354 O  O   . GLU C 296  ? 1.7215 1.8757 1.6131 0.4194  -0.0505 -0.1100 296  GLU C O   
11355 C  CB  . GLU C 296  ? 1.5100 1.7122 1.4202 0.4240  -0.0539 -0.1127 296  GLU C CB  
11356 C  CG  . GLU C 296  ? 1.6450 1.8550 1.5603 0.4222  -0.0565 -0.1125 296  GLU C CG  
11357 C  CD  . GLU C 296  ? 1.7000 1.9396 1.6307 0.4211  -0.0570 -0.1150 296  GLU C CD  
11358 O  OE1 . GLU C 296  ? 1.6411 1.8957 1.5817 0.4188  -0.0546 -0.1166 296  GLU C OE1 
11359 O  OE2 . GLU C 296  ? 1.7029 1.9504 1.6357 0.4226  -0.0598 -0.1155 296  GLU C OE2 
11360 N  N   . ASN C 297  ? 1.4935 1.6799 1.4025 0.4174  -0.0472 -0.1131 297  ASN C N   
11361 C  CA  . ASN C 297  ? 1.5001 1.6683 1.3976 0.4200  -0.0457 -0.1130 297  ASN C CA  
11362 C  C   . ASN C 297  ? 1.5164 1.6731 1.4168 0.4110  -0.0442 -0.1122 297  ASN C C   
11363 O  O   . ASN C 297  ? 1.4662 1.6022 1.3550 0.4125  -0.0437 -0.1119 297  ASN C O   
11364 C  CB  . ASN C 297  ? 1.5927 1.7744 1.4927 0.4241  -0.0436 -0.1148 297  ASN C CB  
11365 C  CG  . ASN C 297  ? 1.6177 1.8097 1.5136 0.4338  -0.0450 -0.1158 297  ASN C CG  
11366 O  OD1 . ASN C 297  ? 1.5999 1.7839 1.4869 0.4392  -0.0477 -0.1150 297  ASN C OD1 
11367 N  ND2 . ASN C 297  ? 1.5540 1.7638 1.4563 0.4364  -0.0432 -0.1176 297  ASN C ND2 
11368 N  N   . TYR C 298  ? 1.3506 1.5202 1.2662 0.4019  -0.0435 -0.1121 298  TYR C N   
11369 C  CA  . TYR C 298  ? 1.2624 1.4236 1.1822 0.3931  -0.0421 -0.1115 298  TYR C CA  
11370 C  C   . TYR C 298  ? 1.2912 1.4393 1.2096 0.3887  -0.0439 -0.1096 298  TYR C C   
11371 O  O   . TYR C 298  ? 1.3112 1.4396 1.2229 0.3861  -0.0437 -0.1089 298  TYR C O   
11372 C  CB  . TYR C 298  ? 1.0686 1.2521 1.0059 0.3856  -0.0397 -0.1125 298  TYR C CB  
11373 C  CG  . TYR C 298  ? 1.1363 1.3347 1.0765 0.3896  -0.0375 -0.1142 298  TYR C CG  
11374 C  CD1 . TYR C 298  ? 1.2115 1.3981 1.1393 0.3962  -0.0368 -0.1149 298  TYR C CD1 
11375 C  CD2 . TYR C 298  ? 1.2068 1.4309 1.1620 0.3865  -0.0360 -0.1153 298  TYR C CD2 
11376 C  CE1 . TYR C 298  ? 1.2274 1.4275 1.1576 0.4001  -0.0346 -0.1164 298  TYR C CE1 
11377 C  CE2 . TYR C 298  ? 1.2797 1.5175 1.2378 0.3901  -0.0337 -0.1169 298  TYR C CE2 
11378 C  CZ  . TYR C 298  ? 1.2130 1.4388 1.1585 0.3970  -0.0329 -0.1173 298  TYR C CZ  
11379 O  OH  . TYR C 298  ? 1.1945 1.4339 1.1428 0.4007  -0.0304 -0.1187 298  TYR C OH  
11380 N  N   . ILE C 299  ? 1.2823 1.4411 1.2068 0.3879  -0.0455 -0.1091 299  ILE C N   
11381 C  CA  . ILE C 299  ? 1.2342 1.3813 1.1569 0.3844  -0.0472 -0.1072 299  ILE C CA  
11382 C  C   . ILE C 299  ? 1.2882 1.4226 1.1961 0.3935  -0.0494 -0.1063 299  ILE C C   
11383 O  O   . ILE C 299  ? 1.3188 1.4651 1.2282 0.3975  -0.0511 -0.1065 299  ILE C O   
11384 C  CB  . ILE C 299  ? 1.1770 1.3429 1.1155 0.3773  -0.0475 -0.1071 299  ILE C CB  
11385 C  CG1 . ILE C 299  ? 1.1338 1.3177 1.0871 0.3703  -0.0449 -0.1084 299  ILE C CG1 
11386 C  CG2 . ILE C 299  ? 1.1948 1.3470 1.1324 0.3720  -0.0484 -0.1050 299  ILE C CG2 
11387 C  CD1 . ILE C 299  ? 0.8886 1.0928 0.8578 0.3635  -0.0449 -0.1086 299  ILE C CD1 
11388 N  N   . THR C 300  ? 1.4258 1.5353 1.3188 0.3968  -0.0494 -0.1053 300  THR C N   
11389 C  CA  . THR C 300  ? 1.5253 1.6197 1.4020 0.4058  -0.0511 -0.1043 300  THR C CA  
11390 C  C   . THR C 300  ? 1.4353 1.5176 1.3084 0.4038  -0.0524 -0.1021 300  THR C C   
11391 O  O   . THR C 300  ? 1.4705 1.5580 1.3545 0.3957  -0.0523 -0.1014 300  THR C O   
11392 C  CB  . THR C 300  ? 1.5156 1.5885 1.3773 0.4105  -0.0501 -0.1045 300  THR C CB  
11393 O  OG1 . THR C 300  ? 1.4828 1.5347 1.3406 0.4048  -0.0494 -0.1034 300  THR C OG1 
11394 C  CG2 . THR C 300  ? 1.5237 1.6078 1.3904 0.4107  -0.0484 -0.1066 300  THR C CG2 
11395 N  N   . LEU C 301  ? 1.3148 1.3805 1.1722 0.4114  -0.0536 -0.1008 301  LEU C N   
11396 C  CA  . LEU C 301  ? 1.3654 1.4174 1.2173 0.4103  -0.0545 -0.0984 301  LEU C CA  
11397 C  C   . LEU C 301  ? 1.3881 1.4171 1.2356 0.4043  -0.0530 -0.0971 301  LEU C C   
11398 O  O   . LEU C 301  ? 1.3509 1.3728 1.1999 0.3997  -0.0531 -0.0953 301  LEU C O   
11399 C  CB  . LEU C 301  ? 1.4266 1.4677 1.2621 0.4207  -0.0561 -0.0974 301  LEU C CB  
11400 C  CG  . LEU C 301  ? 1.3772 1.4399 1.2163 0.4267  -0.0583 -0.0986 301  LEU C CG  
11401 C  CD1 . LEU C 301  ? 1.2794 1.3287 1.1004 0.4374  -0.0597 -0.0975 301  LEU C CD1 
11402 C  CD2 . LEU C 301  ? 1.3383 1.4172 1.1912 0.4206  -0.0595 -0.0984 301  LEU C CD2 
11403 N  N   . HIS C 302  ? 1.7316 1.7489 1.5737 0.4043  -0.0515 -0.0981 302  HIS C N   
11404 C  CA  . HIS C 302  ? 1.6927 1.6892 1.5317 0.3982  -0.0501 -0.0974 302  HIS C CA  
11405 C  C   . HIS C 302  ? 1.6762 1.6845 1.5320 0.3879  -0.0494 -0.0977 302  HIS C C   
11406 O  O   . HIS C 302  ? 1.6842 1.6785 1.5401 0.3819  -0.0487 -0.0966 302  HIS C O   
11407 C  CB  . HIS C 302  ? 1.6768 1.6592 1.5063 0.4008  -0.0489 -0.0989 302  HIS C CB  
11408 C  CG  . HIS C 302  ? 1.6435 1.5996 1.4651 0.3966  -0.0478 -0.0983 302  HIS C CG  
11409 N  ND1 . HIS C 302  ? 1.7025 1.6455 1.5179 0.3963  -0.0468 -0.1001 302  HIS C ND1 
11410 C  CD2 . HIS C 302  ? 1.5407 1.4813 1.3598 0.3924  -0.0474 -0.0964 302  HIS C CD2 
11411 C  CE1 . HIS C 302  ? 1.5963 1.5169 1.4060 0.3919  -0.0460 -0.0995 302  HIS C CE1 
11412 N  NE2 . HIS C 302  ? 1.4726 1.3913 1.2846 0.3894  -0.0462 -0.0972 302  HIS C NE2 
11413 N  N   . HIS C 303  ? 1.5120 1.5459 1.3822 0.3855  -0.0495 -0.0992 303  HIS C N   
11414 C  CA  . HIS C 303  ? 1.5020 1.5487 1.3883 0.3759  -0.0489 -0.0992 303  HIS C CA  
11415 C  C   . HIS C 303  ? 1.4448 1.4912 1.3343 0.3729  -0.0499 -0.0971 303  HIS C C   
11416 O  O   . HIS C 303  ? 1.4434 1.4814 1.3366 0.3660  -0.0493 -0.0961 303  HIS C O   
11417 C  CB  . HIS C 303  ? 1.5151 1.5894 1.4153 0.3745  -0.0486 -0.1011 303  HIS C CB  
11418 C  CG  . HIS C 303  ? 1.4483 1.5241 1.3490 0.3743  -0.0470 -0.1030 303  HIS C CG  
11419 N  ND1 . HIS C 303  ? 1.5257 1.5965 1.4157 0.3822  -0.0469 -0.1041 303  HIS C ND1 
11420 C  CD2 . HIS C 303  ? 1.3602 1.4420 1.2704 0.3674  -0.0454 -0.1041 303  HIS C CD2 
11421 C  CE1 . HIS C 303  ? 1.5723 1.6456 1.4650 0.3802  -0.0453 -0.1057 303  HIS C CE1 
11422 N  NE2 . HIS C 303  ? 1.4697 1.5497 1.3745 0.3713  -0.0444 -0.1058 303  HIS C NE2 
11423 N  N   . LEU C 304  ? 1.1516 1.2068 1.0393 0.3782  -0.0516 -0.0966 304  LEU C N   
11424 C  CA  . LEU C 304  ? 1.0841 1.1387 0.9734 0.3762  -0.0527 -0.0947 304  LEU C CA  
11425 C  C   . LEU C 304  ? 1.1199 1.1465 0.9962 0.3766  -0.0521 -0.0923 304  LEU C C   
11426 O  O   . LEU C 304  ? 1.1885 1.2107 1.0681 0.3716  -0.0520 -0.0906 304  LEU C O   
11427 C  CB  . LEU C 304  ? 1.0470 1.1148 0.9346 0.3832  -0.0548 -0.0949 304  LEU C CB  
11428 C  CG  . LEU C 304  ? 1.0012 1.0950 0.8990 0.3848  -0.0553 -0.0975 304  LEU C CG  
11429 C  CD1 . LEU C 304  ? 0.9909 1.0952 0.8852 0.3924  -0.0577 -0.0979 304  LEU C CD1 
11430 C  CD2 . LEU C 304  ? 1.0156 1.1289 0.9322 0.3753  -0.0544 -0.0984 304  LEU C CD2 
11431 N  N   . ASP C 305  ? 1.5293 1.5366 1.3905 0.3824  -0.0515 -0.0923 305  ASP C N   
11432 C  CA  . ASP C 305  ? 1.5979 1.5772 1.4459 0.3826  -0.0505 -0.0902 305  ASP C CA  
11433 C  C   . ASP C 305  ? 1.5832 1.5529 1.4375 0.3734  -0.0489 -0.0901 305  ASP C C   
11434 O  O   . ASP C 305  ? 1.5633 1.5221 1.4170 0.3694  -0.0482 -0.0881 305  ASP C O   
11435 C  CB  . ASP C 305  ? 1.6323 1.5935 1.4631 0.3905  -0.0501 -0.0904 305  ASP C CB  
11436 C  CG  . ASP C 305  ? 1.6435 1.5747 1.4598 0.3907  -0.0486 -0.0883 305  ASP C CG  
11437 O  OD1 . ASP C 305  ? 1.7484 1.6719 1.5560 0.3948  -0.0490 -0.0860 305  ASP C OD1 
11438 O  OD2 . ASP C 305  ? 1.6039 1.5191 1.4172 0.3868  -0.0470 -0.0890 305  ASP C OD2 
11439 N  N   . VAL C 306  ? 1.9112 1.8848 1.7710 0.3701  -0.0481 -0.0923 306  VAL C N   
11440 C  CA  . VAL C 306  ? 1.8717 1.8360 1.7369 0.3618  -0.0468 -0.0927 306  VAL C CA  
11441 C  C   . VAL C 306  ? 1.8442 1.8248 1.7256 0.3541  -0.0470 -0.0921 306  VAL C C   
11442 O  O   . VAL C 306  ? 1.8701 1.8407 1.7544 0.3478  -0.0461 -0.0912 306  VAL C O   
11443 C  CB  . VAL C 306  ? 1.8295 1.7936 1.6953 0.3611  -0.0462 -0.0954 306  VAL C CB  
11444 C  CG1 . VAL C 306  ? 1.7247 1.7163 1.6034 0.3604  -0.0467 -0.0971 306  VAL C CG1 
11445 C  CG2 . VAL C 306  ? 1.7566 1.7077 1.6254 0.3534  -0.0452 -0.0961 306  VAL C CG2 
11446 N  N   . MET C 307  ? 1.4874 1.4930 1.3795 0.3544  -0.0480 -0.0925 307  MET C N   
11447 C  CA  . MET C 307  ? 1.3763 1.3976 1.2834 0.3471  -0.0481 -0.0920 307  MET C CA  
11448 C  C   . MET C 307  ? 1.3106 1.3231 1.2143 0.3467  -0.0486 -0.0893 307  MET C C   
11449 O  O   . MET C 307  ? 1.3143 1.3258 1.2254 0.3398  -0.0480 -0.0883 307  MET C O   
11450 C  CB  . MET C 307  ? 1.4134 1.4626 1.3319 0.3476  -0.0490 -0.0933 307  MET C CB  
11451 C  CG  . MET C 307  ? 1.4952 1.5552 1.4195 0.3464  -0.0480 -0.0958 307  MET C CG  
11452 S  SD  . MET C 307  ? 1.4957 1.5871 1.4320 0.3477  -0.0485 -0.0974 307  MET C SD  
11453 C  CE  . MET C 307  ? 1.4882 1.5948 1.4415 0.3378  -0.0483 -0.0967 307  MET C CE  
11454 N  N   . ALA C 308  ? 1.0828 1.0887 0.9748 0.3543  -0.0495 -0.0881 308  ALA C N   
11455 C  CA  . ALA C 308  ? 1.1000 1.0952 0.9866 0.3547  -0.0497 -0.0854 308  ALA C CA  
11456 C  C   . ALA C 308  ? 1.1000 1.0682 0.9780 0.3518  -0.0477 -0.0839 308  ALA C C   
11457 O  O   . ALA C 308  ? 1.0756 1.0364 0.9543 0.3482  -0.0470 -0.0818 308  ALA C O   
11458 C  CB  . ALA C 308  ? 1.1422 1.1359 1.0169 0.3641  -0.0512 -0.0847 308  ALA C CB  
11459 N  N   . LYS C 309  ? 1.3182 1.2713 1.1881 0.3532  -0.0466 -0.0850 309  LYS C N   
11460 C  CA  . LYS C 309  ? 1.3295 1.2571 1.1922 0.3496  -0.0446 -0.0841 309  LYS C CA  
11461 C  C   . LYS C 309  ? 1.2605 1.1926 1.1368 0.3401  -0.0438 -0.0847 309  LYS C C   
11462 O  O   . LYS C 309  ? 1.3164 1.2344 1.1916 0.3358  -0.0424 -0.0830 309  LYS C O   
11463 C  CB  . LYS C 309  ? 1.2867 1.1983 1.1381 0.3532  -0.0438 -0.0858 309  LYS C CB  
11464 C  CG  . LYS C 309  ? 1.3754 1.2663 1.2080 0.3606  -0.0432 -0.0841 309  LYS C CG  
11465 C  CD  . LYS C 309  ? 1.4223 1.2930 1.2435 0.3622  -0.0420 -0.0858 309  LYS C CD  
11466 C  CE  . LYS C 309  ? 1.4180 1.3023 1.2407 0.3665  -0.0434 -0.0885 309  LYS C CE  
11467 N  NZ  . LYS C 309  ? 1.4148 1.2781 1.2235 0.3697  -0.0424 -0.0899 309  LYS C NZ  
11468 N  N   . VAL C 310  ? 0.9653 0.9166 0.8544 0.3367  -0.0445 -0.0870 310  VAL C N   
11469 C  CA  . VAL C 310  ? 0.9522 0.9100 0.8548 0.3279  -0.0440 -0.0875 310  VAL C CA  
11470 C  C   . VAL C 310  ? 0.9712 0.9391 0.8820 0.3245  -0.0443 -0.0853 310  VAL C C   
11471 O  O   . VAL C 310  ? 0.9269 0.8884 0.8425 0.3185  -0.0433 -0.0843 310  VAL C O   
11472 C  CB  . VAL C 310  ? 0.9580 0.9349 0.8714 0.3256  -0.0446 -0.0902 310  VAL C CB  
11473 C  CG1 . VAL C 310  ? 0.8486 0.8332 0.7759 0.3168  -0.0441 -0.0907 310  VAL C CG1 
11474 C  CG2 . VAL C 310  ? 0.9989 0.9643 0.9033 0.3289  -0.0443 -0.0925 310  VAL C CG2 
11475 N  N   . MET C 311  ? 1.2594 1.2429 1.1719 0.3285  -0.0457 -0.0847 311  MET C N   
11476 C  CA  . MET C 311  ? 1.1116 1.1049 1.0312 0.3258  -0.0462 -0.0828 311  MET C CA  
11477 C  C   . MET C 311  ? 1.0883 1.0599 0.9975 0.3266  -0.0451 -0.0799 311  MET C C   
11478 O  O   . MET C 311  ? 1.1499 1.1215 1.0650 0.3216  -0.0445 -0.0784 311  MET C O   
11479 C  CB  . MET C 311  ? 1.1020 1.1157 1.0244 0.3304  -0.0482 -0.0833 311  MET C CB  
11480 C  CG  . MET C 311  ? 1.2776 1.3036 1.2080 0.3276  -0.0491 -0.0820 311  MET C CG  
11481 S  SD  . MET C 311  ? 1.3925 1.4453 1.3287 0.3318  -0.0517 -0.0835 311  MET C SD  
11482 C  CE  . MET C 311  ? 1.2313 1.2693 1.1486 0.3426  -0.0529 -0.0822 311  MET C CE  
11483 N  N   . LEU C 312  ? 1.0212 0.9736 0.9144 0.3329  -0.0445 -0.0791 312  LEU C N   
11484 C  CA  . LEU C 312  ? 1.0883 1.0180 0.9703 0.3336  -0.0429 -0.0763 312  LEU C CA  
11485 C  C   . LEU C 312  ? 1.1222 1.0357 1.0062 0.3264  -0.0405 -0.0761 312  LEU C C   
11486 O  O   . LEU C 312  ? 1.0481 0.9518 0.9315 0.3231  -0.0390 -0.0737 312  LEU C O   
11487 C  CB  . LEU C 312  ? 1.1139 1.0262 0.9778 0.3419  -0.0425 -0.0755 312  LEU C CB  
11488 C  CG  . LEU C 312  ? 1.2053 1.0883 1.0552 0.3421  -0.0398 -0.0729 312  LEU C CG  
11489 C  CD1 . LEU C 312  ? 1.1414 1.0232 0.9887 0.3430  -0.0396 -0.0698 312  LEU C CD1 
11490 C  CD2 . LEU C 312  ? 1.2119 1.0772 1.0448 0.3491  -0.0392 -0.0730 312  LEU C CD2 
11491 N  N   . THR C 313  ? 0.9919 0.9025 0.8782 0.3240  -0.0402 -0.0787 313  THR C N   
11492 C  CA  . THR C 313  ? 0.9592 0.8554 0.8480 0.3171  -0.0384 -0.0792 313  THR C CA  
11493 C  C   . THR C 313  ? 1.0223 0.9333 0.9269 0.3079  -0.0384 -0.0783 313  THR C C   
11494 O  O   . THR C 313  ? 1.0553 0.9553 0.9610 0.2994  -0.0364 -0.0759 313  THR C O   
11495 C  CB  . THR C 313  ? 0.8400 0.7327 0.7285 0.3164  -0.0387 -0.0826 313  THR C CB  
11496 O  OG1 . THR C 313  ? 0.9031 0.7782 0.7755 0.3227  -0.0382 -0.0827 313  THR C OG1 
11497 C  CG2 . THR C 313  ? 0.7202 0.6034 0.6143 0.3043  -0.0372 -0.0826 313  THR C CG2 
11498 N  N   . THR C 314  ? 1.3535 1.2898 1.2706 0.3075  -0.0403 -0.0798 314  THR C N   
11499 C  CA  . THR C 314  ? 1.3593 1.3106 1.2913 0.2971  -0.0401 -0.0785 314  THR C CA  
11500 C  C   . THR C 314  ? 1.3745 1.3250 1.3055 0.2973  -0.0397 -0.0755 314  THR C C   
11501 O  O   . THR C 314  ? 1.3019 1.2519 1.2397 0.2877  -0.0383 -0.0733 314  THR C O   
11502 C  CB  . THR C 314  ? 1.2359 1.2135 1.1803 0.2973  -0.0418 -0.0809 314  THR C CB  
11503 O  OG1 . THR C 314  ? 1.3739 1.3636 1.3159 0.3062  -0.0435 -0.0812 314  THR C OG1 
11504 C  CG2 . THR C 314  ? 1.1288 1.1062 1.0733 0.2972  -0.0420 -0.0838 314  THR C CG2 
11505 N  N   . GLY C 315  ? 1.0898 1.0402 1.0120 0.3085  -0.0409 -0.0752 315  GLY C N   
11506 C  CA  . GLY C 315  ? 1.0942 1.0416 1.0133 0.3094  -0.0406 -0.0723 315  GLY C CA  
11507 C  C   . GLY C 315  ? 1.0624 0.9836 0.9717 0.3058  -0.0375 -0.0693 315  GLY C C   
11508 O  O   . GLY C 315  ? 1.0431 0.9621 0.9545 0.3007  -0.0362 -0.0666 315  GLY C O   
11509 N  N   . MET C 316  ? 1.0957 0.9969 0.9943 0.3078  -0.0361 -0.0699 316  MET C N   
11510 C  CA  . MET C 316  ? 1.1503 1.0262 1.0403 0.3028  -0.0327 -0.0673 316  MET C CA  
11511 C  C   . MET C 316  ? 1.0896 0.9669 0.9918 0.2882  -0.0309 -0.0666 316  MET C C   
11512 O  O   . MET C 316  ? 1.0580 0.9227 0.9587 0.2821  -0.0281 -0.0638 316  MET C O   
11513 C  CB  . MET C 316  ? 1.2614 1.1157 1.1370 0.3083  -0.0316 -0.0686 316  MET C CB  
11514 C  CG  . MET C 316  ? 1.1914 1.0358 1.0509 0.3198  -0.0318 -0.0673 316  MET C CG  
11515 S  SD  . MET C 316  ? 1.2808 1.1238 1.1361 0.3216  -0.0309 -0.0630 316  MET C SD  
11516 C  CE  . MET C 316  ? 1.0801 0.8897 0.9246 0.3173  -0.0258 -0.0604 316  MET C CE  
11517 N  N   . ILE C 317  ? 1.0262 0.9184 0.9404 0.2827  -0.0324 -0.0692 317  ILE C N   
11518 C  CA  . ILE C 317  ? 1.0386 0.9348 0.9653 0.2695  -0.0312 -0.0686 317  ILE C CA  
11519 C  C   . ILE C 317  ? 1.0297 0.9395 0.9657 0.2651  -0.0311 -0.0662 317  ILE C C   
11520 O  O   . ILE C 317  ? 0.9521 0.8577 0.8936 0.2556  -0.0290 -0.0642 317  ILE C O   
11521 C  CB  . ILE C 317  ? 0.9989 0.9081 0.9350 0.2658  -0.0329 -0.0719 317  ILE C CB  
11522 C  CG1 . ILE C 317  ? 1.0234 0.9176 0.9493 0.2700  -0.0330 -0.0744 317  ILE C CG1 
11523 C  CG2 . ILE C 317  ? 0.9861 0.8996 0.9346 0.2528  -0.0319 -0.0714 317  ILE C CG2 
11524 C  CD1 . ILE C 317  ? 1.0127 0.9181 0.9462 0.2671  -0.0347 -0.0777 317  ILE C CD1 
11525 N  N   . VAL C 318  ? 1.0321 0.9585 0.9701 0.2720  -0.0333 -0.0666 318  VAL C N   
11526 C  CA  . VAL C 318  ? 1.0361 0.9749 0.9818 0.2687  -0.0334 -0.0646 318  VAL C CA  
11527 C  C   . VAL C 318  ? 1.0962 1.0177 1.0322 0.2697  -0.0311 -0.0611 318  VAL C C   
11528 O  O   . VAL C 318  ? 1.1543 1.0759 1.0958 0.2620  -0.0294 -0.0587 318  VAL C O   
11529 C  CB  . VAL C 318  ? 1.0433 1.0039 0.9932 0.2761  -0.0366 -0.0664 318  VAL C CB  
11530 C  CG1 . VAL C 318  ? 1.1543 1.1253 1.1098 0.2738  -0.0369 -0.0644 318  VAL C CG1 
11531 C  CG2 . VAL C 318  ? 1.0136 0.9924 0.9748 0.2732  -0.0381 -0.0694 318  VAL C CG2 
11532 N  N   . VAL C 319  ? 1.1194 1.0252 1.0402 0.2794  -0.0308 -0.0607 319  VAL C N   
11533 C  CA  . VAL C 319  ? 1.1001 0.9866 1.0096 0.2808  -0.0281 -0.0572 319  VAL C CA  
11534 C  C   . VAL C 319  ? 1.1291 0.9989 1.0397 0.2699  -0.0242 -0.0555 319  VAL C C   
11535 O  O   . VAL C 319  ? 1.1156 0.9774 1.0254 0.2654  -0.0214 -0.0523 319  VAL C O   
11536 C  CB  . VAL C 319  ? 1.1106 0.9822 1.0026 0.2937  -0.0284 -0.0572 319  VAL C CB  
11537 C  CG1 . VAL C 319  ? 1.0528 0.9000 0.9315 0.2944  -0.0246 -0.0535 319  VAL C CG1 
11538 C  CG2 . VAL C 319  ? 1.0563 0.9453 0.9476 0.3045  -0.0322 -0.0585 319  VAL C CG2 
11539 N  N   . TYR C 320  ? 1.0584 0.9234 0.9713 0.2656  -0.0239 -0.0576 320  TYR C N   
11540 C  CA  . TYR C 320  ? 1.0692 0.9218 0.9857 0.2544  -0.0207 -0.0567 320  TYR C CA  
11541 C  C   . TYR C 320  ? 1.0236 0.8909 0.9554 0.2441  -0.0203 -0.0555 320  TYR C C   
11542 O  O   . TYR C 320  ? 0.9754 0.8331 0.9093 0.2361  -0.0171 -0.0533 320  TYR C O   
11543 C  CB  . TYR C 320  ? 1.0084 0.8563 0.9256 0.2521  -0.0213 -0.0600 320  TYR C CB  
11544 C  CG  . TYR C 320  ? 0.9694 0.8132 0.8957 0.2393  -0.0194 -0.0602 320  TYR C CG  
11545 C  CD1 . TYR C 320  ? 1.0652 0.8875 0.9856 0.2342  -0.0155 -0.0584 320  TYR C CD1 
11546 C  CD2 . TYR C 320  ? 0.8429 0.7044 0.7836 0.2325  -0.0214 -0.0622 320  TYR C CD2 
11547 C  CE1 . TYR C 320  ? 0.9813 0.8010 0.9108 0.2226  -0.0140 -0.0589 320  TYR C CE1 
11548 C  CE2 . TYR C 320  ? 0.8630 0.7215 0.8120 0.2214  -0.0201 -0.0625 320  TYR C CE2 
11549 C  CZ  . TYR C 320  ? 0.9222 0.7603 0.8661 0.2165  -0.0165 -0.0610 320  TYR C CZ  
11550 O  OH  . TYR C 320  ? 0.9931 0.8294 0.9461 0.2054  -0.0153 -0.0617 320  TYR C OH  
11551 N  N   . GLY C 321  ? 1.0049 0.8956 0.9475 0.2443  -0.0234 -0.0571 321  GLY C N   
11552 C  CA  . GLY C 321  ? 1.0073 0.9120 0.9635 0.2354  -0.0231 -0.0559 321  GLY C CA  
11553 C  C   . GLY C 321  ? 1.0909 0.9941 1.0443 0.2364  -0.0217 -0.0526 321  GLY C C   
11554 O  O   . GLY C 321  ? 1.0592 0.9625 1.0192 0.2281  -0.0195 -0.0504 321  GLY C O   
11555 N  N   . TYR C 322  ? 1.1473 1.0493 1.0907 0.2469  -0.0229 -0.0521 322  TYR C N   
11556 C  CA  . TYR C 322  ? 1.0207 0.9188 0.9591 0.2491  -0.0217 -0.0490 322  TYR C CA  
11557 C  C   . TYR C 322  ? 1.0311 0.9061 0.9620 0.2447  -0.0170 -0.0458 322  TYR C C   
11558 O  O   . TYR C 322  ? 0.9956 0.8693 0.9296 0.2392  -0.0146 -0.0431 322  TYR C O   
11559 C  CB  . TYR C 322  ? 0.9838 0.8825 0.9109 0.2622  -0.0241 -0.0495 322  TYR C CB  
11560 C  CG  . TYR C 322  ? 0.9810 0.9040 0.9157 0.2669  -0.0286 -0.0525 322  TYR C CG  
11561 C  CD1 . TYR C 322  ? 0.9490 0.8924 0.8985 0.2600  -0.0298 -0.0532 322  TYR C CD1 
11562 C  CD2 . TYR C 322  ? 1.0969 1.0223 1.0239 0.2784  -0.0313 -0.0546 322  TYR C CD2 
11563 C  CE1 . TYR C 322  ? 1.0616 1.0270 1.0184 0.2639  -0.0335 -0.0561 322  TYR C CE1 
11564 C  CE2 . TYR C 322  ? 1.1505 1.0987 1.0851 0.2826  -0.0351 -0.0575 322  TYR C CE2 
11565 C  CZ  . TYR C 322  ? 1.1144 1.0825 1.0641 0.2750  -0.0360 -0.0583 322  TYR C CZ  
11566 O  OH  . TYR C 322  ? 1.0215 1.0123 0.9791 0.2786  -0.0394 -0.0613 322  TYR C OH  
11567 N  N   . PHE C 323  ? 1.2679 1.1241 1.1889 0.2469  -0.0153 -0.0462 323  PHE C N   
11568 C  CA  . PHE C 323  ? 1.2873 1.1203 1.2007 0.2427  -0.0103 -0.0434 323  PHE C CA  
11569 C  C   . PHE C 323  ? 1.3133 1.1484 1.2397 0.2293  -0.0080 -0.0429 323  PHE C C   
11570 O  O   . PHE C 323  ? 1.3184 1.1431 1.2438 0.2240  -0.0040 -0.0399 323  PHE C O   
11571 C  CB  . PHE C 323  ? 1.3125 1.1256 1.2130 0.2475  -0.0092 -0.0445 323  PHE C CB  
11572 C  CG  . PHE C 323  ? 1.4383 1.2425 1.3224 0.2609  -0.0100 -0.0438 323  PHE C CG  
11573 C  CD1 . PHE C 323  ? 1.4969 1.3066 1.3771 0.2669  -0.0108 -0.0416 323  PHE C CD1 
11574 C  CD2 . PHE C 323  ? 1.4570 1.2473 1.3293 0.2678  -0.0102 -0.0454 323  PHE C CD2 
11575 C  CE1 . PHE C 323  ? 1.4792 1.2811 1.3441 0.2799  -0.0119 -0.0411 323  PHE C CE1 
11576 C  CE2 . PHE C 323  ? 1.5350 1.3169 1.3917 0.2808  -0.0110 -0.0447 323  PHE C CE2 
11577 C  CZ  . PHE C 323  ? 1.6437 1.4317 1.4968 0.2870  -0.0119 -0.0426 323  PHE C CZ  
11578 N  N   . MET C 324  ? 1.3279 1.1762 1.2662 0.2239  -0.0103 -0.0459 324  MET C N   
11579 C  CA  . MET C 324  ? 1.3081 1.1597 1.2591 0.2118  -0.0086 -0.0457 324  MET C CA  
11580 C  C   . MET C 324  ? 1.3027 1.1672 1.2627 0.2073  -0.0081 -0.0434 324  MET C C   
11581 O  O   . MET C 324  ? 1.2897 1.1499 1.2552 0.1988  -0.0049 -0.0415 324  MET C O   
11582 C  CB  . MET C 324  ? 1.2555 1.1191 1.2161 0.2083  -0.0116 -0.0495 324  MET C CB  
11583 C  CG  . MET C 324  ? 1.2919 1.1404 1.2455 0.2092  -0.0113 -0.0518 324  MET C CG  
11584 S  SD  . MET C 324  ? 1.5396 1.3624 1.4876 0.2022  -0.0058 -0.0498 324  MET C SD  
11585 C  CE  . MET C 324  ? 1.4932 1.2944 1.4201 0.2139  -0.0043 -0.0487 324  MET C CE  
11586 N  N   . GLU C 325  ? 1.4158 1.2963 1.3774 0.2129  -0.0111 -0.0438 325  GLU C N   
11587 C  CA  . GLU C 325  ? 1.4222 1.3137 1.3908 0.2095  -0.0107 -0.0417 325  GLU C CA  
11588 C  C   . GLU C 325  ? 1.3820 1.2580 1.3408 0.2110  -0.0070 -0.0379 325  GLU C C   
11589 O  O   . GLU C 325  ? 1.2906 1.1668 1.2549 0.2042  -0.0043 -0.0355 325  GLU C O   
11590 C  CB  . GLU C 325  ? 1.4015 1.3129 1.3734 0.2153  -0.0149 -0.0433 325  GLU C CB  
11591 C  CG  . GLU C 325  ? 1.3901 1.3195 1.3737 0.2123  -0.0180 -0.0466 325  GLU C CG  
11592 C  CD  . GLU C 325  ? 1.5972 1.5450 1.5829 0.2189  -0.0218 -0.0485 325  GLU C CD  
11593 O  OE1 . GLU C 325  ? 1.4727 1.4208 1.4520 0.2251  -0.0224 -0.0474 325  GLU C OE1 
11594 O  OE2 . GLU C 325  ? 1.6818 1.6437 1.6753 0.2180  -0.0241 -0.0513 325  GLU C OE2 
11595 N  N   . VAL C 326  ? 1.1153 0.9776 1.0593 0.2202  -0.0066 -0.0372 326  VAL C N   
11596 C  CA  . VAL C 326  ? 1.0599 0.9055 0.9926 0.2225  -0.0028 -0.0334 326  VAL C CA  
11597 C  C   . VAL C 326  ? 1.0406 0.8688 0.9733 0.2139  0.0026  -0.0315 326  VAL C C   
11598 O  O   . VAL C 326  ? 1.0646 0.8864 0.9971 0.2098  0.0064  -0.0282 326  VAL C O   
11599 C  CB  . VAL C 326  ? 0.9563 0.7908 0.8723 0.2350  -0.0038 -0.0332 326  VAL C CB  
11600 C  CG1 . VAL C 326  ? 0.6865 0.5000 0.5890 0.2373  0.0009  -0.0292 326  VAL C CG1 
11601 C  CG2 . VAL C 326  ? 0.9701 0.8233 0.8869 0.2433  -0.0089 -0.0350 326  VAL C CG2 
11602 N  N   . PHE C 327  ? 1.2523 1.0726 1.1854 0.2111  0.0030  -0.0335 327  PHE C N   
11603 C  CA  . PHE C 327  ? 1.2885 1.0933 1.2229 0.2023  0.0079  -0.0323 327  PHE C CA  
11604 C  C   . PHE C 327  ? 1.2130 1.0302 1.1635 0.1914  0.0089  -0.0318 327  PHE C C   
11605 O  O   . PHE C 327  ? 1.2337 1.0411 1.1855 0.1848  0.0136  -0.0293 327  PHE C O   
11606 C  CB  . PHE C 327  ? 1.2808 1.0767 1.2133 0.2013  0.0074  -0.0353 327  PHE C CB  
11607 C  CG  . PHE C 327  ? 1.2530 1.0364 1.1899 0.1909  0.0117  -0.0351 327  PHE C CG  
11608 C  CD1 . PHE C 327  ? 1.2899 1.0498 1.2154 0.1907  0.0170  -0.0326 327  PHE C CD1 
11609 C  CD2 . PHE C 327  ? 1.2543 1.0496 1.2066 0.1815  0.0104  -0.0373 327  PHE C CD2 
11610 C  CE1 . PHE C 327  ? 1.3283 1.0774 1.2586 0.1807  0.0212  -0.0327 327  PHE C CE1 
11611 C  CE2 . PHE C 327  ? 1.3021 1.0871 1.2591 0.1720  0.0141  -0.0374 327  PHE C CE2 
11612 C  CZ  . PHE C 327  ? 1.3199 1.0821 1.2664 0.1713  0.0195  -0.0352 327  PHE C CZ  
11613 N  N   . ALA C 328  ? 1.0975 0.9362 1.0602 0.1895  0.0047  -0.0341 328  ALA C N   
11614 C  CA  . ALA C 328  ? 1.1528 1.0038 1.1302 0.1798  0.0053  -0.0337 328  ALA C CA  
11615 C  C   . ALA C 328  ? 1.2104 1.0634 1.1876 0.1795  0.0076  -0.0301 328  ALA C C   
11616 O  O   . ALA C 328  ? 1.2155 1.0674 1.1997 0.1716  0.0110  -0.0283 328  ALA C O   
11617 C  CB  . ALA C 328  ? 1.0490 0.9215 1.0379 0.1788  0.0004  -0.0369 328  ALA C CB  
11618 N  N   . SER C 329  ? 1.4374 1.2935 1.4065 0.1881  0.0057  -0.0293 329  SER C N   
11619 C  CA  . SER C 329  ? 1.3686 1.2259 1.3361 0.1885  0.0076  -0.0262 329  SER C CA  
11620 C  C   . SER C 329  ? 1.3476 1.1833 1.3053 0.1876  0.0135  -0.0225 329  SER C C   
11621 O  O   . SER C 329  ? 1.3489 1.1837 1.3092 0.1833  0.0168  -0.0197 329  SER C O   
11622 C  CB  . SER C 329  ? 1.3563 1.2222 1.3172 0.1984  0.0037  -0.0267 329  SER C CB  
11623 O  OG  . SER C 329  ? 1.3720 1.2595 1.3435 0.1979  -0.0010 -0.0297 329  SER C OG  
11624 N  N   . LEU C 330  ? 1.0502 0.8679 0.9962 0.1917  0.0153  -0.0225 330  LEU C N   
11625 C  CA  . LEU C 330  ? 1.0016 0.7971 0.9373 0.1909  0.0214  -0.0190 330  LEU C CA  
11626 C  C   . LEU C 330  ? 0.9970 0.7851 0.9410 0.1798  0.0258  -0.0188 330  LEU C C   
11627 O  O   . LEU C 330  ? 1.0868 0.8614 1.0272 0.1763  0.0316  -0.0155 330  LEU C O   
11628 C  CB  . LEU C 330  ? 0.9983 0.7762 0.9167 0.2004  0.0217  -0.0189 330  LEU C CB  
11629 C  CG  . LEU C 330  ? 0.9123 0.6929 0.8190 0.2126  0.0184  -0.0184 330  LEU C CG  
11630 C  CD1 . LEU C 330  ? 0.8646 0.6271 0.7545 0.2217  0.0188  -0.0186 330  LEU C CD1 
11631 C  CD2 . LEU C 330  ? 0.9584 0.7363 0.8604 0.2139  0.0211  -0.0147 330  LEU C CD2 
11632 N  N   . TYR C 331  ? 1.0366 0.8335 0.9917 0.1744  0.0232  -0.0222 331  TYR C N   
11633 C  CA  . TYR C 331  ? 1.0115 0.8019 0.9746 0.1642  0.0268  -0.0227 331  TYR C CA  
11634 C  C   . TYR C 331  ? 1.0840 0.8861 1.0612 0.1555  0.0285  -0.0214 331  TYR C C   
11635 O  O   . TYR C 331  ? 1.0498 0.8427 1.0303 0.1482  0.0336  -0.0197 331  TYR C O   
11636 C  CB  . TYR C 331  ? 1.0458 0.8411 1.0146 0.1623  0.0229  -0.0272 331  TYR C CB  
11637 C  CG  . TYR C 331  ? 1.0602 0.8450 1.0340 0.1534  0.0261  -0.0284 331  TYR C CG  
11638 C  CD1 . TYR C 331  ? 1.1066 0.8688 1.0687 0.1543  0.0300  -0.0279 331  TYR C CD1 
11639 C  CD2 . TYR C 331  ? 1.0892 0.8868 1.0791 0.1442  0.0251  -0.0303 331  TYR C CD2 
11640 C  CE1 . TYR C 331  ? 1.2131 0.9659 1.1802 0.1456  0.0329  -0.0294 331  TYR C CE1 
11641 C  CE2 . TYR C 331  ? 1.0526 0.8417 1.0477 0.1359  0.0276  -0.0319 331  TYR C CE2 
11642 C  CZ  . TYR C 331  ? 1.1877 0.9547 1.1717 0.1364  0.0315  -0.0316 331  TYR C CZ  
11643 O  OH  . TYR C 331  ? 1.2219 0.9807 1.2116 0.1277  0.0340  -0.0335 331  TYR C OH  
11644 N  N   . SER C 332  ? 1.2916 1.1137 1.2773 0.1560  0.0245  -0.0221 332  SER C N   
11645 C  CA  . SER C 332  ? 1.3193 1.1532 1.3180 0.1483  0.0258  -0.0210 332  SER C CA  
11646 C  C   . SER C 332  ? 1.4216 1.2504 1.4148 0.1498  0.0297  -0.0168 332  SER C C   
11647 O  O   . SER C 332  ? 1.3989 1.2228 1.3801 0.1581  0.0292  -0.0153 332  SER C O   
11648 C  CB  . SER C 332  ? 1.3822 1.2385 1.3915 0.1482  0.0202  -0.0235 332  SER C CB  
11649 O  OG  . SER C 332  ? 1.4314 1.2944 1.4339 0.1567  0.0169  -0.0233 332  SER C OG  
11650 N  N   . GLY C 333  ? 1.3904 1.2207 1.3925 0.1419  0.0336  -0.0150 333  GLY C N   
11651 C  CA  . GLY C 333  ? 1.4002 1.2265 1.3982 0.1425  0.0376  -0.0110 333  GLY C CA  
11652 C  C   . GLY C 333  ? 1.4909 1.3357 1.4963 0.1426  0.0346  -0.0109 333  GLY C C   
11653 O  O   . GLY C 333  ? 1.5214 1.3660 1.5274 0.1408  0.0379  -0.0079 333  GLY C O   
11654 N  N   . ASN C 334  ? 1.5202 1.3805 1.5310 0.1445  0.0286  -0.0141 334  ASN C N   
11655 C  CA  . ASN C 334  ? 1.4667 1.3448 1.4848 0.1442  0.0256  -0.0144 334  ASN C CA  
11656 C  C   . ASN C 334  ? 1.4381 1.3159 1.4454 0.1524  0.0243  -0.0130 334  ASN C C   
11657 O  O   . ASN C 334  ? 1.4989 1.3716 1.4958 0.1600  0.0220  -0.0139 334  ASN C O   
11658 C  CB  . ASN C 334  ? 1.4081 1.3023 1.4355 0.1433  0.0201  -0.0183 334  ASN C CB  
11659 C  CG  . ASN C 334  ? 1.6656 1.5632 1.7052 0.1348  0.0208  -0.0197 334  ASN C CG  
11660 O  OD1 . ASN C 334  ? 1.7154 1.6126 1.7617 0.1285  0.0244  -0.0180 334  ASN C OD1 
11661 N  ND2 . ASN C 334  ? 1.6811 1.5825 1.7235 0.1350  0.0173  -0.0231 334  ASN C ND2 
11662 N  N   . GLU C 335  ? 1.3873 1.2709 1.3968 0.1510  0.0255  -0.0109 335  GLU C N   
11663 C  CA  . GLU C 335  ? 1.2947 1.1792 1.2946 0.1583  0.0240  -0.0099 335  GLU C CA  
11664 C  C   . GLU C 335  ? 1.2111 1.1103 1.2122 0.1634  0.0174  -0.0134 335  GLU C C   
11665 O  O   . GLU C 335  ? 1.1478 1.0461 1.1390 0.1714  0.0151  -0.0135 335  GLU C O   
11666 C  CB  . GLU C 335  ? 1.1309 1.0198 1.1344 0.1548  0.0264  -0.0075 335  GLU C CB  
11667 C  CG  . GLU C 335  ? 1.1912 1.0821 1.1856 0.1617  0.0246  -0.0067 335  GLU C CG  
11668 C  CD  . GLU C 335  ? 1.3884 1.2624 1.3663 0.1695  0.0263  -0.0048 335  GLU C CD  
11669 O  OE1 . GLU C 335  ? 1.4524 1.3102 1.4252 0.1677  0.0320  -0.0019 335  GLU C OE1 
11670 O  OE2 . GLU C 335  ? 1.3609 1.2380 1.3310 0.1775  0.0221  -0.0062 335  GLU C OE2 
11671 N  N   . PHE C 336  ? 0.8987 0.8116 0.9116 0.1591  0.0144  -0.0162 336  PHE C N   
11672 C  CA  . PHE C 336  ? 0.8139 0.7426 0.8296 0.1629  0.0088  -0.0194 336  PHE C CA  
11673 C  C   . PHE C 336  ? 0.8574 0.7829 0.8668 0.1692  0.0059  -0.0217 336  PHE C C   
11674 O  O   . PHE C 336  ? 0.7990 0.7325 0.8048 0.1758  0.0019  -0.0236 336  PHE C O   
11675 C  CB  . PHE C 336  ? 0.6585 0.6026 0.6887 0.1559  0.0073  -0.0212 336  PHE C CB  
11676 C  CG  . PHE C 336  ? 0.5945 0.5409 0.6310 0.1495  0.0104  -0.0189 336  PHE C CG  
11677 C  CD1 . PHE C 336  ? 0.5892 0.5439 0.6259 0.1503  0.0095  -0.0183 336  PHE C CD1 
11678 C  CD2 . PHE C 336  ? 0.5736 0.5138 0.6159 0.1427  0.0143  -0.0174 336  PHE C CD2 
11679 C  CE1 . PHE C 336  ? 0.6352 0.5913 0.6771 0.1448  0.0125  -0.0162 336  PHE C CE1 
11680 C  CE2 . PHE C 336  ? 0.5966 0.5392 0.6448 0.1373  0.0173  -0.0153 336  PHE C CE2 
11681 C  CZ  . PHE C 336  ? 0.6272 0.5774 0.6749 0.1385  0.0165  -0.0146 336  PHE C CZ  
11682 N  N   . GLU C 337  ? 1.5416 1.4559 1.5499 0.1674  0.0078  -0.0218 337  GLU C N   
11683 C  CA  . GLU C 337  ? 1.5522 1.4602 1.5523 0.1741  0.0057  -0.0237 337  GLU C CA  
11684 C  C   . GLU C 337  ? 1.5968 1.4920 1.5815 0.1826  0.0067  -0.0218 337  GLU C C   
11685 O  O   . GLU C 337  ? 1.6131 1.5098 1.5906 0.1909  0.0032  -0.0235 337  GLU C O   
11686 C  CB  . GLU C 337  ? 1.5806 1.4783 1.5826 0.1696  0.0078  -0.0244 337  GLU C CB  
11687 C  CG  . GLU C 337  ? 1.6606 1.5708 1.6768 0.1623  0.0061  -0.0267 337  GLU C CG  
11688 C  CD  . GLU C 337  ? 1.6076 1.5300 1.6260 0.1662  0.0010  -0.0304 337  GLU C CD  
11689 O  OE1 . GLU C 337  ? 1.6046 1.5230 1.6134 0.1743  -0.0009 -0.0314 337  GLU C OE1 
11690 O  OE2 . GLU C 337  ? 1.5350 1.4710 1.5645 0.1615  -0.0010 -0.0323 337  GLU C OE2 
11691 N  N   . GLU C 338  ? 0.8881 0.7704 0.8672 0.1812  0.0114  -0.0182 338  GLU C N   
11692 C  CA  . GLU C 338  ? 0.7808 0.6498 0.7442 0.1895  0.0126  -0.0160 338  GLU C CA  
11693 C  C   . GLU C 338  ? 0.6522 0.5337 0.6129 0.1960  0.0084  -0.0168 338  GLU C C   
11694 O  O   . GLU C 338  ? 0.6659 0.5442 0.6155 0.2055  0.0059  -0.0175 338  GLU C O   
11695 C  CB  . GLU C 338  ? 0.8647 0.7177 0.8233 0.1858  0.0191  -0.0118 338  GLU C CB  
11696 C  CG  . GLU C 338  ? 0.8977 0.7375 0.8586 0.1793  0.0237  -0.0110 338  GLU C CG  
11697 C  CD  . GLU C 338  ? 1.0750 0.9019 1.0339 0.1743  0.0305  -0.0071 338  GLU C CD  
11698 O  OE1 . GLU C 338  ? 1.2034 1.0245 1.1528 0.1790  0.0322  -0.0043 338  GLU C OE1 
11699 O  OE2 . GLU C 338  ? 1.1368 0.9598 1.1038 0.1660  0.0340  -0.0068 338  GLU C OE2 
11700 N  N   . TYR C 339  ? 0.7734 0.6692 0.7439 0.1912  0.0074  -0.0170 339  TYR C N   
11701 C  CA  . TYR C 339  ? 0.7466 0.6549 0.7154 0.1966  0.0033  -0.0183 339  TYR C CA  
11702 C  C   . TYR C 339  ? 0.7338 0.6571 0.7065 0.2008  -0.0025 -0.0224 339  TYR C C   
11703 O  O   . TYR C 339  ? 0.7079 0.6381 0.6754 0.2082  -0.0062 -0.0239 339  TYR C O   
11704 C  CB  . TYR C 339  ? 0.7053 0.6245 0.6835 0.1900  0.0040  -0.0175 339  TYR C CB  
11705 C  CG  . TYR C 339  ? 0.6652 0.5908 0.6380 0.1954  0.0014  -0.0177 339  TYR C CG  
11706 C  CD1 . TYR C 339  ? 0.8107 0.7230 0.7714 0.1994  0.0041  -0.0146 339  TYR C CD1 
11707 C  CD2 . TYR C 339  ? 0.5522 0.4968 0.5316 0.1966  -0.0038 -0.0212 339  TYR C CD2 
11708 C  CE1 . TYR C 339  ? 0.8976 0.8158 0.8529 0.2046  0.0013  -0.0151 339  TYR C CE1 
11709 C  CE2 . TYR C 339  ? 0.7405 0.6914 0.7152 0.2013  -0.0065 -0.0218 339  TYR C CE2 
11710 C  CZ  . TYR C 339  ? 0.8672 0.8049 0.8298 0.2054  -0.0042 -0.0189 339  TYR C CZ  
11711 O  OH  . TYR C 339  ? 0.8335 0.7775 0.7912 0.2102  -0.0072 -0.0198 339  TYR C OH  
11712 N  N   . LEU C 340  ? 0.9090 0.8379 0.8909 0.1962  -0.0032 -0.0245 340  LEU C N   
11713 C  CA  . LEU C 340  ? 0.9594 0.9009 0.9441 0.2006  -0.0081 -0.0283 340  LEU C CA  
11714 C  C   . LEU C 340  ? 0.9771 0.9085 0.9483 0.2109  -0.0094 -0.0287 340  LEU C C   
11715 O  O   . LEU C 340  ? 0.9878 0.9294 0.9566 0.2182  -0.0137 -0.0310 340  LEU C O   
11716 C  CB  . LEU C 340  ? 0.8827 0.8290 0.8781 0.1940  -0.0080 -0.0301 340  LEU C CB  
11717 C  CG  . LEU C 340  ? 0.7799 0.7347 0.7761 0.1990  -0.0121 -0.0337 340  LEU C CG  
11718 C  CD1 . LEU C 340  ? 0.7361 0.7126 0.7408 0.1993  -0.0160 -0.0364 340  LEU C CD1 
11719 C  CD2 . LEU C 340  ? 0.9251 0.8760 0.9265 0.1940  -0.0110 -0.0347 340  LEU C CD2 
11720 N  N   . LEU C 341  ? 1.1165 1.0279 1.0787 0.2117  -0.0057 -0.0265 341  LEU C N   
11721 C  CA  . LEU C 341  ? 1.0712 0.9705 1.0188 0.2219  -0.0064 -0.0264 341  LEU C CA  
11722 C  C   . LEU C 341  ? 1.1345 1.0317 1.0713 0.2299  -0.0075 -0.0251 341  LEU C C   
11723 O  O   . LEU C 341  ? 1.1634 1.0624 1.0919 0.2398  -0.0110 -0.0266 341  LEU C O   
11724 C  CB  . LEU C 341  ? 1.1446 1.0213 1.0847 0.2200  -0.0015 -0.0241 341  LEU C CB  
11725 C  CG  . LEU C 341  ? 1.1943 1.0561 1.1192 0.2298  -0.0018 -0.0242 341  LEU C CG  
11726 C  CD1 . LEU C 341  ? 1.2001 1.0746 1.1276 0.2352  -0.0070 -0.0283 341  LEU C CD1 
11727 C  CD2 . LEU C 341  ? 1.2053 1.0454 1.1247 0.2259  0.0035  -0.0223 341  LEU C CD2 
11728 N  N   . TYR C 342  ? 0.9775 0.8714 0.9141 0.2260  -0.0046 -0.0222 342  TYR C N   
11729 C  CA  . TYR C 342  ? 0.9558 0.8477 0.8818 0.2335  -0.0057 -0.0210 342  TYR C CA  
11730 C  C   . TYR C 342  ? 1.0376 0.9516 0.9697 0.2368  -0.0118 -0.0245 342  TYR C C   
11731 O  O   . TYR C 342  ? 1.0602 0.9760 0.9831 0.2465  -0.0151 -0.0254 342  TYR C O   
11732 C  CB  . TYR C 342  ? 1.0173 0.9001 0.9418 0.2282  -0.0009 -0.0172 342  TYR C CB  
11733 C  CG  . TYR C 342  ? 1.0578 0.9395 0.9720 0.2352  -0.0022 -0.0160 342  TYR C CG  
11734 C  CD1 . TYR C 342  ? 1.0619 0.9265 0.9583 0.2446  -0.0010 -0.0140 342  TYR C CD1 
11735 C  CD2 . TYR C 342  ? 1.0961 0.9932 1.0175 0.2325  -0.0045 -0.0170 342  TYR C CD2 
11736 C  CE1 . TYR C 342  ? 1.2641 1.1276 1.1504 0.2516  -0.0024 -0.0130 342  TYR C CE1 
11737 C  CE2 . TYR C 342  ? 1.1596 1.0557 1.0713 0.2390  -0.0060 -0.0163 342  TYR C CE2 
11738 C  CZ  . TYR C 342  ? 1.3293 1.2089 1.2234 0.2486  -0.0051 -0.0143 342  TYR C CZ  
11739 O  OH  . TYR C 342  ? 1.4626 1.3411 1.3465 0.2555  -0.0068 -0.0137 342  TYR C OH  
11740 N  N   . ASN C 343  ? 1.0358 0.9672 0.9835 0.2289  -0.0132 -0.0265 343  ASN C N   
11741 C  CA  . ASN C 343  ? 1.0395 0.9923 0.9941 0.2310  -0.0185 -0.0300 343  ASN C CA  
11742 C  C   . ASN C 343  ? 1.0463 1.0075 1.0002 0.2383  -0.0229 -0.0335 343  ASN C C   
11743 O  O   . ASN C 343  ? 1.0346 1.0105 0.9896 0.2436  -0.0275 -0.0364 343  ASN C O   
11744 C  CB  . ASN C 343  ? 0.9343 0.9016 0.9048 0.2204  -0.0182 -0.0310 343  ASN C CB  
11745 C  CG  . ASN C 343  ? 0.9484 0.9369 0.9261 0.2213  -0.0229 -0.0343 343  ASN C CG  
11746 O  OD1 . ASN C 343  ? 1.0673 1.0589 1.0380 0.2286  -0.0259 -0.0353 343  ASN C OD1 
11747 N  ND2 . ASN C 343  ? 1.0166 1.0195 1.0083 0.2137  -0.0235 -0.0362 343  ASN C ND2 
11748 N  N   . ARG C 344  ? 1.0132 0.9655 0.9655 0.2386  -0.0215 -0.0336 344  ARG C N   
11749 C  CA  . ARG C 344  ? 1.0054 0.9638 0.9556 0.2463  -0.0252 -0.0367 344  ARG C CA  
11750 C  C   . ARG C 344  ? 1.0342 0.9809 0.9677 0.2584  -0.0263 -0.0359 344  ARG C C   
11751 O  O   . ARG C 344  ? 1.0520 1.0089 0.9831 0.2670  -0.0308 -0.0388 344  ARG C O   
11752 C  CB  . ARG C 344  ? 0.9240 0.8766 0.8778 0.2425  -0.0234 -0.0372 344  ARG C CB  
11753 C  CG  . ARG C 344  ? 0.8765 0.8446 0.8467 0.2330  -0.0238 -0.0391 344  ARG C CG  
11754 C  CD  . ARG C 344  ? 0.9759 0.9376 0.9484 0.2302  -0.0225 -0.0399 344  ARG C CD  
11755 N  NE  . ARG C 344  ? 0.9214 0.8983 0.9085 0.2224  -0.0233 -0.0420 344  ARG C NE  
11756 C  CZ  . ARG C 344  ? 0.8283 0.8029 0.8196 0.2186  -0.0226 -0.0431 344  ARG C CZ  
11757 N  NH1 . ARG C 344  ? 1.0551 1.0129 1.0378 0.2213  -0.0209 -0.0425 344  ARG C NH1 
11758 N  NH2 . ARG C 344  ? 0.8191 0.8081 0.8231 0.2120  -0.0234 -0.0449 344  ARG C NH2 
11759 N  N   . LEU C 345  ? 1.0888 1.0142 1.0104 0.2595  -0.0221 -0.0320 345  LEU C N   
11760 C  CA  . LEU C 345  ? 1.1883 1.0989 1.0922 0.2711  -0.0224 -0.0308 345  LEU C CA  
11761 C  C   . LEU C 345  ? 1.2096 1.1248 1.1066 0.2778  -0.0251 -0.0306 345  LEU C C   
11762 O  O   . LEU C 345  ? 1.2271 1.1443 1.1150 0.2890  -0.0289 -0.0321 345  LEU C O   
11763 C  CB  . LEU C 345  ? 1.2395 1.1237 1.1327 0.2693  -0.0163 -0.0267 345  LEU C CB  
11764 C  CG  . LEU C 345  ? 1.1821 1.0559 1.0744 0.2681  -0.0144 -0.0272 345  LEU C CG  
11765 C  CD1 . LEU C 345  ? 1.1356 0.9852 1.0207 0.2633  -0.0077 -0.0233 345  LEU C CD1 
11766 C  CD2 . LEU C 345  ? 1.1189 0.9904 1.0002 0.2806  -0.0178 -0.0291 345  LEU C CD2 
11767 N  N   . PHE C 346  ? 1.1657 1.0826 1.0666 0.2714  -0.0233 -0.0288 346  PHE C N   
11768 C  CA  . PHE C 346  ? 1.1319 1.0514 1.0254 0.2773  -0.0256 -0.0285 346  PHE C CA  
11769 C  C   . PHE C 346  ? 1.0349 0.9744 0.9421 0.2703  -0.0279 -0.0304 346  PHE C C   
11770 O  O   . PHE C 346  ? 1.0931 1.0332 0.9955 0.2723  -0.0287 -0.0297 346  PHE C O   
11771 C  CB  . PHE C 346  ? 1.1867 1.0826 1.0656 0.2787  -0.0204 -0.0236 346  PHE C CB  
11772 C  CG  . PHE C 346  ? 1.2456 1.1189 1.1124 0.2825  -0.0164 -0.0211 346  PHE C CG  
11773 C  CD1 . PHE C 346  ? 1.3015 1.1681 1.1546 0.2949  -0.0189 -0.0218 346  PHE C CD1 
11774 C  CD2 . PHE C 346  ? 1.2816 1.1403 1.1505 0.2736  -0.0101 -0.0181 346  PHE C CD2 
11775 C  CE1 . PHE C 346  ? 1.1987 1.0433 1.0398 0.2983  -0.0150 -0.0195 346  PHE C CE1 
11776 C  CE2 . PHE C 346  ? 1.2399 1.0774 1.0977 0.2765  -0.0063 -0.0160 346  PHE C CE2 
11777 C  CZ  . PHE C 346  ? 1.2622 1.0919 1.1056 0.2888  -0.0086 -0.0167 346  PHE C CZ  
11778 N  N   . GLY C 347  ? 1.2403 1.1953 1.1637 0.2622  -0.0288 -0.0328 347  GLY C N   
11779 C  CA  . GLY C 347  ? 1.3461 1.3190 1.2822 0.2552  -0.0305 -0.0346 347  GLY C CA  
11780 C  C   . GLY C 347  ? 1.3123 1.3046 1.2506 0.2615  -0.0369 -0.0389 347  GLY C C   
11781 O  O   . GLY C 347  ? 1.2917 1.2845 1.2217 0.2720  -0.0402 -0.0406 347  GLY C O   
11782 N  N   . PRO C 348  ? 0.8607 0.8696 0.8105 0.2550  -0.0385 -0.0409 348  PRO C N   
11783 C  CA  . PRO C 348  ? 0.7800 0.8094 0.7342 0.2596  -0.0446 -0.0456 348  PRO C CA  
11784 C  C   . PRO C 348  ? 0.9026 0.9463 0.8644 0.2621  -0.0476 -0.0493 348  PRO C C   
11785 O  O   . PRO C 348  ? 0.9203 0.9796 0.8837 0.2682  -0.0527 -0.0532 348  PRO C O   
11786 C  CB  . PRO C 348  ? 0.6897 0.7311 0.6553 0.2498  -0.0443 -0.0464 348  PRO C CB  
11787 C  CG  . PRO C 348  ? 0.8535 0.8857 0.8250 0.2397  -0.0388 -0.0432 348  PRO C CG  
11788 C  CD  . PRO C 348  ? 0.7661 0.7754 0.7251 0.2434  -0.0349 -0.0392 348  PRO C CD  
11789 N  N   . SER C 349  ? 1.1807 1.2199 1.1472 0.2578  -0.0448 -0.0485 349  SER C N   
11790 C  CA  . SER C 349  ? 1.1222 1.1735 1.0953 0.2602  -0.0472 -0.0518 349  SER C CA  
11791 C  C   . SER C 349  ? 1.0820 1.1172 1.0447 0.2669  -0.0457 -0.0502 349  SER C C   
11792 O  O   . SER C 349  ? 1.0882 1.1272 1.0560 0.2663  -0.0457 -0.0517 349  SER C O   
11793 C  CB  . SER C 349  ? 1.1999 1.2626 1.1888 0.2492  -0.0456 -0.0529 349  SER C CB  
11794 O  OG  . SER C 349  ? 1.1610 1.2397 1.1595 0.2436  -0.0471 -0.0548 349  SER C OG  
11795 N  N   . SER C 350  ? 1.3576 1.3738 1.3049 0.2734  -0.0443 -0.0472 350  SER C N   
11796 C  CA  . SER C 350  ? 1.3814 1.3800 1.3174 0.2797  -0.0425 -0.0455 350  SER C CA  
11797 C  C   . SER C 350  ? 1.3634 1.3712 1.2966 0.2903  -0.0469 -0.0490 350  SER C C   
11798 O  O   . SER C 350  ? 1.4286 1.4248 1.3549 0.2947  -0.0457 -0.0484 350  SER C O   
11799 C  CB  . SER C 350  ? 1.3863 1.3625 1.3055 0.2846  -0.0398 -0.0415 350  SER C CB  
11800 O  OG  . SER C 350  ? 1.3979 1.3792 1.3095 0.2935  -0.0437 -0.0426 350  SER C OG  
11801 N  N   . TRP C 351  ? 0.8013 0.8297 0.7399 0.2943  -0.0520 -0.0528 351  TRP C N   
11802 C  CA  . TRP C 351  ? 0.7941 0.8331 0.7308 0.3048  -0.0563 -0.0563 351  TRP C CA  
11803 C  C   . TRP C 351  ? 0.8992 0.9443 0.8447 0.3018  -0.0556 -0.0581 351  TRP C C   
11804 O  O   . TRP C 351  ? 0.9689 1.0113 0.9082 0.3105  -0.0568 -0.0593 351  TRP C O   
11805 C  CB  . TRP C 351  ? 0.8040 0.8666 0.7478 0.3077  -0.0617 -0.0604 351  TRP C CB  
11806 C  CG  . TRP C 351  ? 0.7987 0.8792 0.7600 0.2958  -0.0616 -0.0623 351  TRP C CG  
11807 C  CD1 . TRP C 351  ? 0.8218 0.9029 0.7875 0.2874  -0.0602 -0.0610 351  TRP C CD1 
11808 C  CD2 . TRP C 351  ? 0.8061 0.9057 0.7823 0.2912  -0.0625 -0.0658 351  TRP C CD2 
11809 N  NE1 . TRP C 351  ? 0.8048 0.9037 0.7868 0.2779  -0.0602 -0.0634 351  TRP C NE1 
11810 C  CE2 . TRP C 351  ? 0.8142 0.9248 0.8030 0.2799  -0.0616 -0.0663 351  TRP C CE2 
11811 C  CE3 . TRP C 351  ? 0.8057 0.9139 0.7854 0.2958  -0.0639 -0.0684 351  TRP C CE3 
11812 C  CZ2 . TRP C 351  ? 0.7654 0.8945 0.7696 0.2730  -0.0618 -0.0692 351  TRP C CZ2 
11813 C  CZ3 . TRP C 351  ? 0.7791 0.9062 0.7745 0.2889  -0.0640 -0.0714 351  TRP C CZ3 
11814 C  CH2 . TRP C 351  ? 0.7691 0.9062 0.7764 0.2776  -0.0629 -0.0717 351  TRP C CH2 
11815 N  N   . ALA C 352  ? 0.8846 0.9375 0.8440 0.2898  -0.0534 -0.0583 352  ALA C N   
11816 C  CA  . ALA C 352  ? 0.7979 0.8565 0.7655 0.2867  -0.0526 -0.0600 352  ALA C CA  
11817 C  C   . ALA C 352  ? 0.7818 0.8175 0.7403 0.2869  -0.0488 -0.0571 352  ALA C C   
11818 O  O   . ALA C 352  ? 0.8467 0.8820 0.8044 0.2904  -0.0491 -0.0586 352  ALA C O   
11819 C  CB  . ALA C 352  ? 0.7427 0.8152 0.7267 0.2742  -0.0514 -0.0609 352  ALA C CB  
11820 N  N   . TYR C 353  ? 1.0026 1.0190 0.9539 0.2830  -0.0451 -0.0530 353  TYR C N   
11821 C  CA  . TYR C 353  ? 1.1421 1.1358 1.0842 0.2830  -0.0413 -0.0504 353  TYR C CA  
11822 C  C   . TYR C 353  ? 1.2249 1.2066 1.1510 0.2962  -0.0426 -0.0503 353  TYR C C   
11823 O  O   . TYR C 353  ? 1.2563 1.2271 1.1772 0.2988  -0.0413 -0.0503 353  TYR C O   
11824 C  CB  . TYR C 353  ? 1.1551 1.1319 1.0938 0.2757  -0.0368 -0.0461 353  TYR C CB  
11825 C  CG  . TYR C 353  ? 1.1301 1.0880 1.0658 0.2707  -0.0323 -0.0439 353  TYR C CG  
11826 C  CD1 . TYR C 353  ? 1.1363 1.1003 1.0837 0.2625  -0.0314 -0.0453 353  TYR C CD1 
11827 C  CD2 . TYR C 353  ? 1.1359 1.0697 1.0570 0.2741  -0.0289 -0.0406 353  TYR C CD2 
11828 C  CE1 . TYR C 353  ? 1.2194 1.1667 1.1644 0.2578  -0.0277 -0.0437 353  TYR C CE1 
11829 C  CE2 . TYR C 353  ? 1.1018 1.0185 1.0207 0.2690  -0.0247 -0.0389 353  TYR C CE2 
11830 C  CZ  . TYR C 353  ? 1.1809 1.1048 1.1121 0.2608  -0.0244 -0.0406 353  TYR C CZ  
11831 O  OH  . TYR C 353  ? 1.1703 1.0779 1.0996 0.2555  -0.0206 -0.0394 353  TYR C OH  
11832 N  N   . TRP C 354  ? 1.2312 1.2146 1.1490 0.3049  -0.0453 -0.0503 354  TRP C N   
11833 C  CA  . TRP C 354  ? 1.2734 1.2461 1.1754 0.3180  -0.0468 -0.0503 354  TRP C CA  
11834 C  C   . TRP C 354  ? 1.3429 1.3313 1.2490 0.3211  -0.0502 -0.0540 354  TRP C C   
11835 O  O   . TRP C 354  ? 1.4849 1.4621 1.3806 0.3261  -0.0496 -0.0536 354  TRP C O   
11836 C  CB  . TRP C 354  ? 1.3354 1.3073 1.2276 0.3236  -0.0488 -0.0492 354  TRP C CB  
11837 C  CG  . TRP C 354  ? 1.4330 1.3844 1.3164 0.3223  -0.0447 -0.0448 354  TRP C CG  
11838 C  CD1 . TRP C 354  ? 1.3265 1.2823 1.2133 0.3172  -0.0445 -0.0437 354  TRP C CD1 
11839 C  CD2 . TRP C 354  ? 1.5106 1.4341 1.3803 0.3229  -0.0396 -0.0408 354  TRP C CD2 
11840 N  NE1 . TRP C 354  ? 1.3276 1.2604 1.2038 0.3149  -0.0395 -0.0390 354  TRP C NE1 
11841 C  CE2 . TRP C 354  ? 1.4445 1.3574 1.3104 0.3180  -0.0363 -0.0372 354  TRP C CE2 
11842 C  CE3 . TRP C 354  ? 1.5254 1.4321 1.3858 0.3253  -0.0371 -0.0398 354  TRP C CE3 
11843 C  CZ2 . TRP C 354  ? 1.4309 1.3170 1.2843 0.3169  -0.0305 -0.0328 354  TRP C CZ2 
11844 C  CZ3 . TRP C 354  ? 1.5303 1.4099 1.3782 0.3248  -0.0316 -0.0356 354  TRP C CZ3 
11845 C  CH2 . TRP C 354  ? 1.4120 1.2817 1.2567 0.3204  -0.0283 -0.0321 354  TRP C CH2 
11846 N  N   . GLY C 355  ? 1.1845 1.1984 1.1053 0.3182  -0.0535 -0.0575 355  GLY C N   
11847 C  CA  . GLY C 355  ? 1.1988 1.2282 1.1250 0.3201  -0.0561 -0.0610 355  GLY C CA  
11848 C  C   . GLY C 355  ? 1.3236 1.3466 1.2535 0.3164  -0.0534 -0.0612 355  GLY C C   
11849 O  O   . GLY C 355  ? 1.3844 1.4075 1.3103 0.3205  -0.0541 -0.0626 355  GLY C O   
11850 N  N   . LEU C 356  ? 1.4154 1.4330 1.3528 0.3090  -0.0503 -0.0599 356  LEU C N   
11851 C  CA  . LEU C 356  ? 1.4039 1.4124 1.3433 0.3046  -0.0475 -0.0598 356  LEU C CA  
11852 C  C   . LEU C 356  ? 1.3357 1.3198 1.2584 0.3112  -0.0456 -0.0578 356  LEU C C   
11853 O  O   . LEU C 356  ? 1.4469 1.4291 1.3669 0.3136  -0.0458 -0.0593 356  LEU C O   
11854 C  CB  . LEU C 356  ? 1.3548 1.3591 1.3029 0.2907  -0.0440 -0.0575 356  LEU C CB  
11855 C  CG  . LEU C 356  ? 1.1983 1.1919 1.1490 0.2831  -0.0407 -0.0569 356  LEU C CG  
11856 C  CD1 . LEU C 356  ? 1.1299 1.1334 1.0953 0.2702  -0.0393 -0.0566 356  LEU C CD1 
11857 C  CD2 . LEU C 356  ? 1.1733 1.1395 1.1108 0.2835  -0.0370 -0.0535 356  LEU C CD2 
11858 N  N   . LEU C 357  ? 1.1176 1.0824 1.0283 0.3132  -0.0434 -0.0544 357  LEU C N   
11859 C  CA  . LEU C 357  ? 1.1842 1.1237 1.0784 0.3177  -0.0407 -0.0520 357  LEU C CA  
11860 C  C   . LEU C 357  ? 1.2612 1.2025 1.1449 0.3265  -0.0434 -0.0532 357  LEU C C   
11861 O  O   . LEU C 357  ? 1.2819 1.2082 1.1556 0.3297  -0.0419 -0.0528 357  LEU C O   
11862 C  CB  . LEU C 357  ? 1.1940 1.1137 1.0777 0.3178  -0.0374 -0.0480 357  LEU C CB  
11863 C  CG  . LEU C 357  ? 1.0946 1.0078 0.9862 0.3041  -0.0332 -0.0455 357  LEU C CG  
11864 C  CD1 . LEU C 357  ? 1.2938 1.1881 1.1742 0.3041  -0.0297 -0.0413 357  LEU C CD1 
11865 C  CD2 . LEU C 357  ? 0.9083 0.8109 0.8022 0.2977  -0.0303 -0.0457 357  LEU C CD2 
11866 N  N   . PHE C 358  ? 1.4427 1.4022 1.3284 0.3305  -0.0474 -0.0548 358  PHE C N   
11867 C  CA  . PHE C 358  ? 1.5973 1.5599 1.4733 0.3392  -0.0502 -0.0562 358  PHE C CA  
11868 C  C   . PHE C 358  ? 1.5854 1.5622 1.4696 0.3391  -0.0519 -0.0596 358  PHE C C   
11869 O  O   . PHE C 358  ? 1.5775 1.5469 1.4516 0.3451  -0.0521 -0.0600 358  PHE C O   
11870 C  CB  . PHE C 358  ? 1.6179 1.5959 1.4937 0.3436  -0.0542 -0.0572 358  PHE C CB  
11871 C  CG  . PHE C 358  ? 1.6854 1.6720 1.5544 0.3522  -0.0578 -0.0595 358  PHE C CG  
11872 C  CD1 . PHE C 358  ? 1.5890 1.5573 1.4390 0.3604  -0.0572 -0.0575 358  PHE C CD1 
11873 C  CD2 . PHE C 358  ? 1.6043 1.6172 1.4859 0.3520  -0.0614 -0.0636 358  PHE C CD2 
11874 C  CE1 . PHE C 358  ? 1.6067 1.5830 1.4502 0.3688  -0.0605 -0.0597 358  PHE C CE1 
11875 C  CE2 . PHE C 358  ? 1.5064 1.5276 1.3820 0.3600  -0.0646 -0.0659 358  PHE C CE2 
11876 C  CZ  . PHE C 358  ? 1.4925 1.4956 1.3491 0.3686  -0.0642 -0.0639 358  PHE C CZ  
11877 N  N   . CYS C 359  ? 1.4135 1.4100 1.3152 0.3324  -0.0528 -0.0621 359  CYS C N   
11878 C  CA  . CYS C 359  ? 1.4663 1.4792 1.3764 0.3324  -0.0544 -0.0655 359  CYS C CA  
11879 C  C   . CYS C 359  ? 1.4671 1.4667 1.3758 0.3301  -0.0516 -0.0654 359  CYS C C   
11880 O  O   . CYS C 359  ? 1.4252 1.4187 1.3254 0.3355  -0.0518 -0.0661 359  CYS C O   
11881 C  CB  . CYS C 359  ? 1.3639 1.4026 1.2928 0.3258  -0.0561 -0.0681 359  CYS C CB  
11882 S  SG  . CYS C 359  ? 1.4214 1.4817 1.3537 0.3293  -0.0606 -0.0702 359  CYS C SG  
11883 N  N   . ASN C 360  ? 1.6145 1.6095 1.5313 0.3223  -0.0491 -0.0646 360  ASN C N   
11884 C  CA  . ASN C 360  ? 1.5071 1.4929 1.4253 0.3191  -0.0469 -0.0653 360  ASN C CA  
11885 C  C   . ASN C 360  ? 1.4637 1.4201 1.3674 0.3208  -0.0436 -0.0626 360  ASN C C   
11886 O  O   . ASN C 360  ? 1.4979 1.4441 1.4025 0.3174  -0.0416 -0.0631 360  ASN C O   
11887 C  CB  . ASN C 360  ? 1.3916 1.3875 1.3260 0.3099  -0.0459 -0.0662 360  ASN C CB  
11888 C  CG  . ASN C 360  ? 1.3335 1.3577 1.2825 0.3073  -0.0485 -0.0689 360  ASN C CG  
11889 O  OD1 . ASN C 360  ? 1.3747 1.4119 1.3228 0.3122  -0.0510 -0.0705 360  ASN C OD1 
11890 N  ND2 . ASN C 360  ? 1.3015 1.3355 1.2641 0.2994  -0.0477 -0.0694 360  ASN C ND2 
11891 N  N   . ALA C 361  ? 1.4097 1.3521 1.2999 0.3258  -0.0430 -0.0600 361  ALA C N   
11892 C  CA  . ALA C 361  ? 1.4724 1.3859 1.3480 0.3272  -0.0395 -0.0573 361  ALA C CA  
11893 C  C   . ALA C 361  ? 1.5370 1.4389 1.3949 0.3364  -0.0400 -0.0562 361  ALA C C   
11894 O  O   . ALA C 361  ? 1.5562 1.4394 1.4030 0.3388  -0.0379 -0.0556 361  ALA C O   
11895 C  CB  . ALA C 361  ? 1.4039 1.3046 1.2788 0.3224  -0.0364 -0.0542 361  ALA C CB  
11896 N  N   . VAL C 362  ? 1.2497 1.1624 1.1045 0.3418  -0.0428 -0.0559 362  VAL C N   
11897 C  CA  . VAL C 362  ? 1.1171 1.0201 0.9548 0.3512  -0.0436 -0.0549 362  VAL C CA  
11898 C  C   . VAL C 362  ? 1.1055 1.0243 0.9447 0.3567  -0.0470 -0.0583 362  VAL C C   
11899 O  O   . VAL C 362  ? 1.1336 1.0402 0.9599 0.3628  -0.0466 -0.0581 362  VAL C O   
11900 C  CB  . VAL C 362  ? 1.1582 1.0627 0.9900 0.3549  -0.0449 -0.0530 362  VAL C CB  
11901 C  CG1 . VAL C 362  ? 1.1760 1.0730 0.9903 0.3653  -0.0464 -0.0524 362  VAL C CG1 
11902 C  CG2 . VAL C 362  ? 1.2095 1.0950 1.0374 0.3501  -0.0408 -0.0493 362  VAL C CG2 
11903 N  N   . ALA C 363  ? 1.3912 1.3370 1.2459 0.3544  -0.0502 -0.0613 363  ALA C N   
11904 C  CA  . ALA C 363  ? 1.3581 1.3207 1.2150 0.3595  -0.0532 -0.0645 363  ALA C CA  
11905 C  C   . ALA C 363  ? 1.3984 1.3574 1.2573 0.3579  -0.0518 -0.0661 363  ALA C C   
11906 O  O   . ALA C 363  ? 1.4850 1.4519 1.3415 0.3633  -0.0536 -0.0682 363  ALA C O   
11907 C  CB  . ALA C 363  ? 1.3938 1.3860 1.2670 0.3568  -0.0565 -0.0673 363  ALA C CB  
11908 N  N   . ILE C 364  ? 1.2386 1.1860 1.1016 0.3508  -0.0488 -0.0653 364  ILE C N   
11909 C  CA  . ILE C 364  ? 1.2265 1.1696 1.0909 0.3492  -0.0476 -0.0670 364  ILE C CA  
11910 C  C   . ILE C 364  ? 1.1837 1.0997 1.0302 0.3539  -0.0453 -0.0654 364  ILE C C   
11911 O  O   . ILE C 364  ? 1.2626 1.1738 1.1074 0.3543  -0.0446 -0.0671 364  ILE C O   
11912 C  CB  . ILE C 364  ? 1.1709 1.1153 1.0485 0.3394  -0.0457 -0.0675 364  ILE C CB  
11913 C  CG1 . ILE C 364  ? 1.1594 1.0781 1.0296 0.3359  -0.0421 -0.0646 364  ILE C CG1 
11914 C  CG2 . ILE C 364  ? 1.1736 1.1419 1.0678 0.3342  -0.0474 -0.0685 364  ILE C CG2 
11915 C  CD1 . ILE C 364  ? 1.0931 1.0092 0.9738 0.3273  -0.0402 -0.0655 364  ILE C CD1 
11916 N  N   . GLN C 365  ? 1.1896 1.0875 1.0223 0.3573  -0.0438 -0.0623 365  GLN C N   
11917 C  CA  . GLN C 365  ? 1.2841 1.1549 1.0988 0.3615  -0.0412 -0.0605 365  GLN C CA  
11918 C  C   . GLN C 365  ? 1.3295 1.2020 1.1341 0.3707  -0.0432 -0.0619 365  GLN C C   
11919 O  O   . GLN C 365  ? 1.2919 1.1477 1.0870 0.3724  -0.0414 -0.0622 365  GLN C O   
11920 C  CB  . GLN C 365  ? 1.2772 1.1294 1.0796 0.3630  -0.0390 -0.0566 365  GLN C CB  
11921 C  CG  . GLN C 365  ? 1.2682 1.1138 1.0782 0.3542  -0.0362 -0.0548 365  GLN C CG  
11922 C  CD  . GLN C 365  ? 1.2437 1.0803 1.0600 0.3468  -0.0337 -0.0560 365  GLN C CD  
11923 O  OE1 . GLN C 365  ? 1.1631 0.9809 0.9693 0.3480  -0.0316 -0.0561 365  GLN C OE1 
11924 N  NE2 . GLN C 365  ? 1.3838 1.2336 1.2167 0.3391  -0.0339 -0.0572 365  GLN C NE2 
11925 N  N   . PRO C 366  ? 1.3512 1.2428 1.1569 0.3768  -0.0468 -0.0631 366  PRO C N   
11926 C  CA  . PRO C 366  ? 1.3595 1.2535 1.1560 0.3856  -0.0486 -0.0647 366  PRO C CA  
11927 C  C   . PRO C 366  ? 1.3401 1.2404 1.1433 0.3838  -0.0486 -0.0676 366  PRO C C   
11928 O  O   . PRO C 366  ? 1.3780 1.2743 1.1714 0.3907  -0.0492 -0.0686 366  PRO C O   
11929 C  CB  . PRO C 366  ? 1.3175 1.2356 1.1191 0.3903  -0.0527 -0.0661 366  PRO C CB  
11930 C  CG  . PRO C 366  ? 1.2959 1.2126 1.0992 0.3872  -0.0524 -0.0638 366  PRO C CG  
11931 C  CD  . PRO C 366  ? 1.2912 1.1995 1.1033 0.3770  -0.0492 -0.0628 366  PRO C CD  
11932 N  N   . LEU C 367  ? 1.4314 1.3409 1.2502 0.3752  -0.0480 -0.0691 367  LEU C N   
11933 C  CA  . LEU C 367  ? 1.3241 1.2382 1.1485 0.3734  -0.0478 -0.0718 367  LEU C CA  
11934 C  C   . LEU C 367  ? 1.3009 1.1878 1.1125 0.3738  -0.0450 -0.0711 367  LEU C C   
11935 O  O   . LEU C 367  ? 1.3574 1.2451 1.1694 0.3744  -0.0450 -0.0734 367  LEU C O   
11936 C  CB  . LEU C 367  ? 1.1947 1.1246 1.0383 0.3639  -0.0478 -0.0733 367  LEU C CB  
11937 C  CG  . LEU C 367  ? 1.1454 1.1056 1.0040 0.3628  -0.0505 -0.0751 367  LEU C CG  
11938 C  CD1 . LEU C 367  ? 1.1786 1.1503 1.0545 0.3529  -0.0498 -0.0761 367  LEU C CD1 
11939 C  CD2 . LEU C 367  ? 1.0690 1.0443 0.9280 0.3686  -0.0525 -0.0778 367  LEU C CD2 
11940 N  N   . TRP C 368  ? 1.4026 1.2654 1.2026 0.3732  -0.0423 -0.0681 368  TRP C N   
11941 C  CA  . TRP C 368  ? 1.4860 1.3217 1.2734 0.3731  -0.0393 -0.0676 368  TRP C CA  
11942 C  C   . TRP C 368  ? 1.5900 1.4192 1.3629 0.3824  -0.0401 -0.0683 368  TRP C C   
11943 O  O   . TRP C 368  ? 1.7362 1.5523 1.5033 0.3824  -0.0388 -0.0696 368  TRP C O   
11944 C  CB  . TRP C 368  ? 1.5492 1.3608 1.3268 0.3707  -0.0360 -0.0641 368  TRP C CB  
11945 C  CG  . TRP C 368  ? 1.4789 1.2884 1.2682 0.3605  -0.0341 -0.0637 368  TRP C CG  
11946 C  CD1 . TRP C 368  ? 1.3952 1.2138 1.1933 0.3566  -0.0342 -0.0621 368  TRP C CD1 
11947 C  CD2 . TRP C 368  ? 1.4485 1.2458 1.2415 0.3533  -0.0318 -0.0652 368  TRP C CD2 
11948 N  NE1 . TRP C 368  ? 1.3314 1.1444 1.1386 0.3475  -0.0320 -0.0623 368  TRP C NE1 
11949 C  CE2 . TRP C 368  ? 1.3302 1.1303 1.1346 0.3453  -0.0306 -0.0643 368  TRP C CE2 
11950 C  CE3 . TRP C 368  ? 1.5811 1.3653 1.3688 0.3529  -0.0308 -0.0673 368  TRP C CE3 
11951 C  CZ2 . TRP C 368  ? 1.3126 1.1034 1.1234 0.3371  -0.0286 -0.0656 368  TRP C CZ2 
11952 C  CZ3 . TRP C 368  ? 1.5269 1.3017 1.3208 0.3446  -0.0290 -0.0688 368  TRP C CZ3 
11953 C  CH2 . TRP C 368  ? 1.4110 1.1894 1.2165 0.3369  -0.0279 -0.0679 368  TRP C CH2 
11954 N  N   . PHE C 369  ? 1.5503 1.3885 1.3172 0.3905  -0.0423 -0.0676 369  PHE C N   
11955 C  CA  . PHE C 369  ? 1.6217 1.4530 1.3735 0.4002  -0.0430 -0.0679 369  PHE C CA  
11956 C  C   . PHE C 369  ? 1.7091 1.5613 1.4691 0.4028  -0.0455 -0.0714 369  PHE C C   
11957 O  O   . PHE C 369  ? 1.6934 1.5680 1.4708 0.3978  -0.0470 -0.0735 369  PHE C O   
11958 C  CB  . PHE C 369  ? 1.5518 1.3835 1.2928 0.4082  -0.0444 -0.0658 369  PHE C CB  
11959 C  CG  . PHE C 369  ? 1.5190 1.3280 1.2491 0.4068  -0.0415 -0.0620 369  PHE C CG  
11960 C  CD1 . PHE C 369  ? 1.4606 1.2736 1.2006 0.3997  -0.0408 -0.0606 369  PHE C CD1 
11961 C  CD2 . PHE C 369  ? 1.6314 1.4145 1.3409 0.4124  -0.0391 -0.0597 369  PHE C CD2 
11962 C  CE1 . PHE C 369  ? 1.5115 1.3034 1.2413 0.3984  -0.0377 -0.0569 369  PHE C CE1 
11963 C  CE2 . PHE C 369  ? 1.8313 1.5930 1.5304 0.4108  -0.0359 -0.0561 369  PHE C CE2 
11964 C  CZ  . PHE C 369  ? 1.7027 1.4689 1.4121 0.4038  -0.0352 -0.0547 369  PHE C CZ  
11965 N  N   . LYS C 370  ? 2.0134 1.8576 1.7603 0.4107  -0.0457 -0.0720 370  LYS C N   
11966 C  CA  . LYS C 370  ? 1.9096 1.7701 1.6618 0.4138  -0.0476 -0.0752 370  LYS C CA  
11967 C  C   . LYS C 370  ? 1.9326 1.8172 1.6880 0.4209  -0.0510 -0.0763 370  LYS C C   
11968 O  O   . LYS C 370  ? 1.8866 1.7950 1.6558 0.4196  -0.0527 -0.0790 370  LYS C O   
11969 C  CB  . LYS C 370  ? 2.0038 1.8435 1.7402 0.4187  -0.0460 -0.0756 370  LYS C CB  
11970 C  CG  . LYS C 370  ? 2.0888 1.9150 1.8280 0.4112  -0.0437 -0.0768 370  LYS C CG  
11971 C  CD  . LYS C 370  ? 2.1923 1.9973 1.9291 0.4040  -0.0408 -0.0745 370  LYS C CD  
11972 C  CE  . LYS C 370  ? 2.2546 2.0339 1.9710 0.4094  -0.0387 -0.0715 370  LYS C CE  
11973 N  NZ  . LYS C 370  ? 2.0726 1.8325 1.7871 0.4022  -0.0356 -0.0690 370  LYS C NZ  
11974 N  N   . LYS C 371  ? 1.6623 1.5411 1.4051 0.4285  -0.0518 -0.0745 371  LYS C N   
11975 C  CA  . LYS C 371  ? 1.6108 1.5120 1.3560 0.4356  -0.0553 -0.0759 371  LYS C CA  
11976 C  C   . LYS C 371  ? 1.6013 1.5283 1.3660 0.4295  -0.0572 -0.0770 371  LYS C C   
11977 O  O   . LYS C 371  ? 1.5047 1.4569 1.2801 0.4312  -0.0597 -0.0797 371  LYS C O   
11978 C  CB  . LYS C 371  ? 1.6184 1.5064 1.3453 0.4447  -0.0559 -0.0735 371  LYS C CB  
11979 C  CG  . LYS C 371  ? 1.6519 1.5619 1.3799 0.4528  -0.0597 -0.0752 371  LYS C CG  
11980 C  CD  . LYS C 371  ? 1.5693 1.4880 1.3021 0.4511  -0.0613 -0.0741 371  LYS C CD  
11981 C  CE  . LYS C 371  ? 1.5477 1.4963 1.2903 0.4553  -0.0654 -0.0771 371  LYS C CE  
11982 N  NZ  . LYS C 371  ? 1.4674 1.4262 1.2169 0.4524  -0.0671 -0.0765 371  LYS C NZ  
11983 N  N   . VAL C 372  ? 1.4602 1.3810 1.2298 0.4222  -0.0560 -0.0751 372  VAL C N   
11984 C  CA  . VAL C 372  ? 1.4687 1.4125 1.2568 0.4156  -0.0576 -0.0761 372  VAL C CA  
11985 C  C   . VAL C 372  ? 1.4001 1.3592 1.2051 0.4083  -0.0571 -0.0787 372  VAL C C   
11986 O  O   . VAL C 372  ? 1.3204 1.3052 1.1406 0.4057  -0.0590 -0.0809 372  VAL C O   
11987 C  CB  . VAL C 372  ? 1.3438 1.2753 1.1317 0.4099  -0.0560 -0.0732 372  VAL C CB  
11988 C  CG1 . VAL C 372  ? 1.2797 1.2347 1.0859 0.4035  -0.0578 -0.0742 372  VAL C CG1 
11989 C  CG2 . VAL C 372  ? 1.3802 1.2947 1.1496 0.4174  -0.0560 -0.0704 372  VAL C CG2 
11990 N  N   . ARG C 373  ? 1.2690 1.2124 1.0712 0.4049  -0.0546 -0.0786 373  ARG C N   
11991 C  CA  . ARG C 373  ? 1.2696 1.2257 1.0863 0.3984  -0.0541 -0.0811 373  ARG C CA  
11992 C  C   . ARG C 373  ? 1.3391 1.3133 1.1590 0.4036  -0.0557 -0.0839 373  ARG C C   
11993 O  O   . ARG C 373  ? 1.2280 1.2195 1.0622 0.3986  -0.0556 -0.0861 373  ARG C O   
11994 C  CB  . ARG C 373  ? 1.2386 1.1719 1.0501 0.3940  -0.0512 -0.0806 373  ARG C CB  
11995 C  CG  . ARG C 373  ? 1.0968 1.0379 0.9244 0.3837  -0.0502 -0.0817 373  ARG C CG  
11996 C  CD  . ARG C 373  ? 1.0743 0.9902 0.8966 0.3783  -0.0474 -0.0804 373  ARG C CD  
11997 N  NE  . ARG C 373  ? 1.0658 0.9622 0.8749 0.3819  -0.0461 -0.0811 373  ARG C NE  
11998 C  CZ  . ARG C 373  ? 1.0980 0.9674 0.8913 0.3841  -0.0442 -0.0792 373  ARG C CZ  
11999 N  NH1 . ARG C 373  ? 1.1083 0.9663 0.8965 0.3832  -0.0432 -0.0762 373  ARG C NH1 
12000 N  NH2 . ARG C 373  ? 1.2109 1.0639 0.9928 0.3872  -0.0432 -0.0802 373  ARG C NH2 
12001 N  N   . GLN C 374  ? 1.6311 1.6018 1.4378 0.4136  -0.0568 -0.0840 374  GLN C N   
12002 C  CA  . GLN C 374  ? 1.5615 1.5494 1.3703 0.4194  -0.0583 -0.0866 374  GLN C CA  
12003 C  C   . GLN C 374  ? 1.5395 1.5512 1.3548 0.4233  -0.0613 -0.0878 374  GLN C C   
12004 O  O   . GLN C 374  ? 1.4887 1.5168 1.3068 0.4282  -0.0625 -0.0902 374  GLN C O   
12005 C  CB  . GLN C 374  ? 1.6651 1.6344 1.4551 0.4284  -0.0577 -0.0862 374  GLN C CB  
12006 C  CG  . GLN C 374  ? 1.7355 1.6844 1.5201 0.4250  -0.0550 -0.0861 374  GLN C CG  
12007 C  CD  . GLN C 374  ? 1.7970 1.7573 1.5870 0.4257  -0.0549 -0.0889 374  GLN C CD  
12008 O  OE1 . GLN C 374  ? 1.9044 1.8742 1.6903 0.4336  -0.0561 -0.0903 374  GLN C OE1 
12009 N  NE2 . GLN C 374  ? 1.6725 1.6318 1.4714 0.4177  -0.0533 -0.0899 374  GLN C NE2 
12010 N  N   . ASN C 375  ? 1.6874 1.7015 1.5052 0.4212  -0.0624 -0.0865 375  ASN C N   
12011 C  CA  . ASN C 375  ? 1.6680 1.7045 1.4923 0.4243  -0.0654 -0.0880 375  ASN C CA  
12012 C  C   . ASN C 375  ? 1.5522 1.6130 1.3982 0.4152  -0.0657 -0.0898 375  ASN C C   
12013 O  O   . ASN C 375  ? 1.6197 1.6764 1.4733 0.4065  -0.0643 -0.0886 375  ASN C O   
12014 C  CB  . ASN C 375  ? 1.6211 1.6467 1.4352 0.4276  -0.0666 -0.0856 375  ASN C CB  
12015 C  CG  . ASN C 375  ? 1.6340 1.6778 1.4480 0.4348  -0.0701 -0.0874 375  ASN C CG  
12016 O  OD1 . ASN C 375  ? 1.6892 1.7464 1.5037 0.4407  -0.0715 -0.0898 375  ASN C OD1 
12017 N  ND2 . ASN C 375  ? 1.6740 1.7183 1.4872 0.4345  -0.0716 -0.0862 375  ASN C ND2 
12018 N  N   . ILE C 376  ? 1.1757 1.2613 1.0314 0.4172  -0.0675 -0.0928 376  ILE C N   
12019 C  CA  . ILE C 376  ? 1.2535 1.3632 1.1298 0.4087  -0.0675 -0.0949 376  ILE C CA  
12020 C  C   . ILE C 376  ? 1.3046 1.4242 1.1881 0.4053  -0.0694 -0.0947 376  ILE C C   
12021 O  O   . ILE C 376  ? 1.2274 1.3512 1.1228 0.3959  -0.0683 -0.0942 376  ILE C O   
12022 C  CB  . ILE C 376  ? 1.2321 1.3645 1.1162 0.4119  -0.0682 -0.0983 376  ILE C CB  
12023 C  CG1 . ILE C 376  ? 1.2161 1.3407 1.0971 0.4124  -0.0657 -0.0986 376  ILE C CG1 
12024 C  CG2 . ILE C 376  ? 1.1801 1.3389 1.0846 0.4041  -0.0686 -0.1005 376  ILE C CG2 
12025 C  CD1 . ILE C 376  ? 1.0178 1.1642 0.9071 0.4147  -0.0657 -0.1016 376  ILE C CD1 
12026 N  N   . PRO C 377  ? 1.5564 1.6802 1.4332 0.4124  -0.0723 -0.0951 377  PRO C N   
12027 C  CA  . PRO C 377  ? 1.5283 1.6612 1.4120 0.4088  -0.0742 -0.0951 377  PRO C CA  
12028 C  C   . PRO C 377  ? 1.4911 1.6039 1.3703 0.4038  -0.0727 -0.0916 377  PRO C C   
12029 O  O   . PRO C 377  ? 1.4188 1.5399 1.3091 0.3965  -0.0729 -0.0915 377  PRO C O   
12030 C  CB  . PRO C 377  ? 1.5638 1.7006 1.4372 0.4193  -0.0776 -0.0961 377  PRO C CB  
12031 C  CG  . PRO C 377  ? 1.4956 1.6367 1.3643 0.4265  -0.0777 -0.0980 377  PRO C CG  
12032 C  CD  . PRO C 377  ? 1.5440 1.6665 1.4077 0.4241  -0.0742 -0.0960 377  PRO C CD  
12033 N  N   . ALA C 378  ? 1.2666 1.3528 1.1298 0.4073  -0.0709 -0.0888 378  ALA C N   
12034 C  CA  . ALA C 378  ? 1.1888 1.2548 1.0478 0.4022  -0.0689 -0.0854 378  ALA C CA  
12035 C  C   . ALA C 378  ? 1.1667 1.2358 1.0401 0.3913  -0.0665 -0.0854 378  ALA C C   
12036 O  O   . ALA C 378  ? 1.1072 1.1725 0.9858 0.3845  -0.0656 -0.0838 378  ALA C O   
12037 C  CB  . ALA C 378  ? 1.2509 1.2878 1.0898 0.4081  -0.0671 -0.0826 378  ALA C CB  
12038 N  N   . LEU C 379  ? 1.1727 1.2486 1.0522 0.3896  -0.0653 -0.0873 379  LEU C N   
12039 C  CA  . LEU C 379  ? 1.1046 1.1844 0.9974 0.3796  -0.0631 -0.0876 379  LEU C CA  
12040 C  C   . LEU C 379  ? 1.0868 1.1911 0.9977 0.3728  -0.0642 -0.0892 379  LEU C C   
12041 O  O   . LEU C 379  ? 1.1526 1.2569 1.0728 0.3642  -0.0628 -0.0884 379  LEU C O   
12042 C  CB  . LEU C 379  ? 1.0696 1.1509 0.9635 0.3803  -0.0617 -0.0893 379  LEU C CB  
12043 C  CG  . LEU C 379  ? 1.1983 1.2529 1.0775 0.3831  -0.0596 -0.0876 379  LEU C CG  
12044 C  CD1 . LEU C 379  ? 1.3376 1.3961 1.2177 0.3847  -0.0586 -0.0897 379  LEU C CD1 
12045 C  CD2 . LEU C 379  ? 1.2261 1.2641 1.1063 0.3755  -0.0574 -0.0855 379  LEU C CD2 
12046 N  N   . LEU C 380  ? 1.1676 1.2928 1.0835 0.3764  -0.0667 -0.0917 380  LEU C N   
12047 C  CA  . LEU C 380  ? 1.1474 1.2958 1.0801 0.3700  -0.0677 -0.0935 380  LEU C CA  
12048 C  C   . LEU C 380  ? 1.1681 1.3117 1.1005 0.3673  -0.0688 -0.0917 380  LEU C C   
12049 O  O   . LEU C 380  ? 1.1958 1.3477 1.1407 0.3588  -0.0681 -0.0918 380  LEU C O   
12050 C  CB  . LEU C 380  ? 1.1522 1.3231 1.0896 0.3749  -0.0702 -0.0969 380  LEU C CB  
12051 C  CG  . LEU C 380  ? 1.1559 1.3383 1.0982 0.3761  -0.0690 -0.0992 380  LEU C CG  
12052 C  CD1 . LEU C 380  ? 1.1629 1.3674 1.1096 0.3813  -0.0715 -0.1025 380  LEU C CD1 
12053 C  CD2 . LEU C 380  ? 1.1770 1.3684 1.1344 0.3660  -0.0663 -0.0997 380  LEU C CD2 
12054 N  N   . ILE C 381  ? 1.2579 1.3874 1.1753 0.3746  -0.0703 -0.0901 381  ILE C N   
12055 C  CA  . ILE C 381  ? 1.2491 1.3726 1.1644 0.3728  -0.0712 -0.0882 381  ILE C CA  
12056 C  C   . ILE C 381  ? 1.2846 1.3900 1.1998 0.3659  -0.0681 -0.0851 381  ILE C C   
12057 O  O   . ILE C 381  ? 1.3943 1.5032 1.3176 0.3594  -0.0679 -0.0843 381  ILE C O   
12058 C  CB  . ILE C 381  ? 1.2121 1.3239 1.1100 0.3830  -0.0732 -0.0870 381  ILE C CB  
12059 C  CG1 . ILE C 381  ? 1.2519 1.3842 1.1516 0.3897  -0.0767 -0.0905 381  ILE C CG1 
12060 C  CG2 . ILE C 381  ? 1.0602 1.1627 0.9542 0.3815  -0.0737 -0.0846 381  ILE C CG2 
12061 C  CD1 . ILE C 381  ? 1.2177 1.3392 1.0994 0.4007  -0.0788 -0.0897 381  ILE C CD1 
12062 N  N   . ILE C 382  ? 1.0967 1.1825 1.0028 0.3671  -0.0656 -0.0835 382  ILE C N   
12063 C  CA  . ILE C 382  ? 1.1258 1.1938 1.0317 0.3606  -0.0626 -0.0808 382  ILE C CA  
12064 C  C   . ILE C 382  ? 1.1040 1.1864 1.0278 0.3506  -0.0614 -0.0821 382  ILE C C   
12065 O  O   . ILE C 382  ? 1.1708 1.2488 1.1001 0.3439  -0.0601 -0.0806 382  ILE C O   
12066 C  CB  . ILE C 382  ? 1.1066 1.1511 0.9989 0.3642  -0.0603 -0.0794 382  ILE C CB  
12067 C  CG1 . ILE C 382  ? 1.1227 1.1484 0.9959 0.3728  -0.0608 -0.0772 382  ILE C CG1 
12068 C  CG2 . ILE C 382  ? 1.0199 1.0497 0.9152 0.3564  -0.0572 -0.0777 382  ILE C CG2 
12069 C  CD1 . ILE C 382  ? 1.1744 1.1754 1.0331 0.3763  -0.0584 -0.0757 382  ILE C CD1 
12070 N  N   . SER C 383  ? 1.0789 1.1786 1.0120 0.3496  -0.0616 -0.0850 383  SER C N   
12071 C  CA  . SER C 383  ? 1.1882 1.3020 1.1379 0.3404  -0.0603 -0.0862 383  SER C CA  
12072 C  C   . SER C 383  ? 1.1293 1.2596 1.0907 0.3352  -0.0616 -0.0867 383  SER C C   
12073 O  O   . SER C 383  ? 1.1168 1.2490 1.0879 0.3271  -0.0602 -0.0861 383  SER C O   
12074 C  CB  . SER C 383  ? 1.1622 1.2913 1.1184 0.3411  -0.0601 -0.0891 383  SER C CB  
12075 O  OG  . SER C 383  ? 1.1699 1.2835 1.1147 0.3461  -0.0589 -0.0887 383  SER C OG  
12076 N  N   . LEU C 384  ? 0.9776 1.1199 0.9382 0.3400  -0.0645 -0.0881 384  LEU C N   
12077 C  CA  . LEU C 384  ? 0.9272 1.0844 0.8978 0.3355  -0.0660 -0.0888 384  LEU C CA  
12078 C  C   . LEU C 384  ? 0.9760 1.1170 0.9416 0.3332  -0.0655 -0.0857 384  LEU C C   
12079 O  O   . LEU C 384  ? 0.9100 1.0576 0.8861 0.3258  -0.0649 -0.0855 384  LEU C O   
12080 C  CB  . LEU C 384  ? 0.9206 1.0925 0.8898 0.3420  -0.0695 -0.0912 384  LEU C CB  
12081 C  CG  . LEU C 384  ? 0.9415 1.1341 0.9235 0.3372  -0.0715 -0.0933 384  LEU C CG  
12082 C  CD1 . LEU C 384  ? 0.9942 1.2040 0.9936 0.3279  -0.0696 -0.0951 384  LEU C CD1 
12083 C  CD2 . LEU C 384  ? 0.8410 1.0476 0.8207 0.3443  -0.0751 -0.0961 384  LEU C CD2 
12084 N  N   . ILE C 385  ? 1.1750 1.2945 1.1243 0.3396  -0.0654 -0.0832 385  ILE C N   
12085 C  CA  . ILE C 385  ? 1.1457 1.2481 1.0889 0.3380  -0.0644 -0.0800 385  ILE C CA  
12086 C  C   . ILE C 385  ? 1.1475 1.2402 1.0966 0.3299  -0.0610 -0.0784 385  ILE C C   
12087 O  O   . ILE C 385  ? 1.1132 1.2029 1.0666 0.3245  -0.0601 -0.0768 385  ILE C O   
12088 C  CB  . ILE C 385  ? 1.1537 1.2341 1.0772 0.3468  -0.0644 -0.0776 385  ILE C CB  
12089 C  CG1 . ILE C 385  ? 1.0877 1.1783 1.0055 0.3547  -0.0681 -0.0792 385  ILE C CG1 
12090 C  CG2 . ILE C 385  ? 1.2485 1.3082 1.1649 0.3446  -0.0623 -0.0739 385  ILE C CG2 
12091 C  CD1 . ILE C 385  ? 1.2302 1.2999 1.1278 0.3639  -0.0682 -0.0769 385  ILE C CD1 
12092 N  N   . VAL C 386  ? 1.1866 1.2747 1.1360 0.3290  -0.0592 -0.0789 386  VAL C N   
12093 C  CA  . VAL C 386  ? 1.1720 1.2513 1.1268 0.3217  -0.0563 -0.0779 386  VAL C CA  
12094 C  C   . VAL C 386  ? 1.0749 1.1739 1.0473 0.3131  -0.0562 -0.0793 386  VAL C C   
12095 O  O   . VAL C 386  ? 1.0926 1.1865 1.0702 0.3068  -0.0545 -0.0778 386  VAL C O   
12096 C  CB  . VAL C 386  ? 1.1162 1.1868 1.0666 0.3234  -0.0548 -0.0786 386  VAL C CB  
12097 C  CG1 . VAL C 386  ? 1.2402 1.3111 1.2009 0.3152  -0.0526 -0.0790 386  VAL C CG1 
12098 C  CG2 . VAL C 386  ? 1.2102 1.2547 1.1428 0.3295  -0.0538 -0.0764 386  VAL C CG2 
12099 N  N   . SER C 387  ? 1.1728 1.2944 1.1546 0.3127  -0.0577 -0.0822 387  SER C N   
12100 C  CA  . SER C 387  ? 1.1090 1.2496 1.1073 0.3045  -0.0574 -0.0836 387  SER C CA  
12101 C  C   . SER C 387  ? 1.2197 1.3630 1.2213 0.3016  -0.0584 -0.0825 387  SER C C   
12102 O  O   . SER C 387  ? 1.1477 1.2943 1.1587 0.2940  -0.0570 -0.0820 387  SER C O   
12103 C  CB  . SER C 387  ? 1.0832 1.2468 1.0899 0.3051  -0.0586 -0.0870 387  SER C CB  
12104 O  OG  . SER C 387  ? 1.1994 1.3610 1.2036 0.3075  -0.0574 -0.0879 387  SER C OG  
12105 N  N   . VAL C 388  ? 0.9562 1.0979 0.9494 0.3078  -0.0608 -0.0822 388  VAL C N   
12106 C  CA  . VAL C 388  ? 0.7457 0.8885 0.7402 0.3059  -0.0619 -0.0812 388  VAL C CA  
12107 C  C   . VAL C 388  ? 0.7869 0.9084 0.7760 0.3033  -0.0594 -0.0776 388  VAL C C   
12108 O  O   . VAL C 388  ? 0.8897 1.0135 0.8858 0.2975  -0.0587 -0.0768 388  VAL C O   
12109 C  CB  . VAL C 388  ? 0.7094 0.8537 0.6944 0.3141  -0.0652 -0.0817 388  VAL C CB  
12110 C  CG1 . VAL C 388  ? 0.7488 0.8925 0.7338 0.3127  -0.0664 -0.0806 388  VAL C CG1 
12111 C  CG2 . VAL C 388  ? 0.8075 0.9746 0.7995 0.3161  -0.0676 -0.0856 388  VAL C CG2 
12112 N  N   . GLY C 389  ? 1.1265 1.2267 1.1030 0.3075  -0.0578 -0.0756 389  GLY C N   
12113 C  CA  . GLY C 389  ? 1.1569 1.2362 1.1283 0.3049  -0.0551 -0.0724 389  GLY C CA  
12114 C  C   . GLY C 389  ? 1.1011 1.1827 1.0843 0.2962  -0.0527 -0.0725 389  GLY C C   
12115 O  O   . GLY C 389  ? 1.1114 1.1840 1.0960 0.2910  -0.0508 -0.0703 389  GLY C O   
12116 N  N   . MET C 390  ? 1.1622 1.2555 1.1535 0.2939  -0.0526 -0.0749 390  MET C N   
12117 C  CA  . MET C 390  ? 1.1336 1.2304 1.1361 0.2858  -0.0505 -0.0753 390  MET C CA  
12118 C  C   . MET C 390  ? 1.1397 1.2521 1.1546 0.2772  -0.0506 -0.0753 390  MET C C   
12119 O  O   . MET C 390  ? 1.2070 1.3139 1.2263 0.2671  -0.0482 -0.0732 390  MET C O   
12120 C  CB  . MET C 390  ? 1.0701 1.1755 1.0770 0.2855  -0.0503 -0.0777 390  MET C CB  
12121 C  CG  . MET C 390  ? 1.2240 1.3110 1.2192 0.2903  -0.0494 -0.0773 390  MET C CG  
12122 S  SD  . MET C 390  ? 1.1065 1.1657 1.0932 0.2865  -0.0467 -0.0737 390  MET C SD  
12123 C  CE  . MET C 390  ? 1.0238 1.0862 1.0221 0.2735  -0.0444 -0.0739 390  MET C CE  
12124 N  N   . TRP C 391  ? 0.9414 1.0729 0.9616 0.2804  -0.0532 -0.0777 391  TRP C N   
12125 C  CA  . TRP C 391  ? 0.8519 0.9974 0.8829 0.2734  -0.0535 -0.0780 391  TRP C CA  
12126 C  C   . TRP C 391  ? 0.8535 0.9850 0.8782 0.2708  -0.0528 -0.0747 391  TRP C C   
12127 O  O   . TRP C 391  ? 0.8100 0.9426 0.8413 0.2611  -0.0512 -0.0732 391  TRP C O   
12128 C  CB  . TRP C 391  ? 0.8429 1.0097 0.8792 0.2762  -0.0564 -0.0812 391  TRP C CB  
12129 C  CG  . TRP C 391  ? 0.8917 1.0761 0.9416 0.2690  -0.0565 -0.0826 391  TRP C CG  
12130 C  CD1 . TRP C 391  ? 0.8536 1.0543 0.9164 0.2625  -0.0552 -0.0847 391  TRP C CD1 
12131 C  CD2 . TRP C 391  ? 0.8771 1.0630 0.9278 0.2667  -0.0576 -0.0819 391  TRP C CD2 
12132 N  NE1 . TRP C 391  ? 0.8296 1.0414 0.9012 0.2555  -0.0554 -0.0852 391  TRP C NE1 
12133 C  CE2 . TRP C 391  ? 0.8740 1.0770 0.9383 0.2577  -0.0569 -0.0835 391  TRP C CE2 
12134 C  CE3 . TRP C 391  ? 0.8136 0.9872 0.8541 0.2708  -0.0589 -0.0798 391  TRP C CE3 
12135 C  CZ2 . TRP C 391  ? 0.8533 1.0612 0.9212 0.2526  -0.0576 -0.0833 391  TRP C CZ2 
12136 C  CZ3 . TRP C 391  ? 0.8410 1.0199 0.8851 0.2660  -0.0596 -0.0795 391  TRP C CZ3 
12137 C  CH2 . TRP C 391  ? 0.8382 1.0341 0.8959 0.2570  -0.0591 -0.0814 391  TRP C CH2 
12138 N  N   . LEU C 392  ? 0.8944 1.0120 0.9057 0.2796  -0.0540 -0.0734 392  LEU C N   
12139 C  CA  . LEU C 392  ? 0.8719 0.9745 0.8758 0.2778  -0.0529 -0.0700 392  LEU C CA  
12140 C  C   . LEU C 392  ? 0.8452 0.9296 0.8476 0.2692  -0.0488 -0.0666 392  LEU C C   
12141 O  O   . LEU C 392  ? 0.8556 0.9334 0.8584 0.2628  -0.0471 -0.0640 392  LEU C O   
12142 C  CB  . LEU C 392  ? 0.8089 0.8998 0.7977 0.2900  -0.0547 -0.0693 392  LEU C CB  
12143 C  CG  . LEU C 392  ? 0.7695 0.8761 0.7577 0.2962  -0.0588 -0.0718 392  LEU C CG  
12144 C  CD1 . LEU C 392  ? 0.7603 0.8515 0.7311 0.3054  -0.0598 -0.0701 392  LEU C CD1 
12145 C  CD2 . LEU C 392  ? 0.8386 0.9579 0.8354 0.2920  -0.0601 -0.0724 392  LEU C CD2 
12146 N  N   . GLU C 393  ? 1.1553 1.2315 1.1559 0.2691  -0.0473 -0.0667 393  GLU C N   
12147 C  CA  . GLU C 393  ? 1.1274 1.1871 1.1272 0.2608  -0.0437 -0.0639 393  GLU C CA  
12148 C  C   . GLU C 393  ? 1.0797 1.1502 1.0932 0.2491  -0.0422 -0.0639 393  GLU C C   
12149 O  O   . GLU C 393  ? 1.1042 1.1654 1.1188 0.2414  -0.0397 -0.0611 393  GLU C O   
12150 C  CB  . GLU C 393  ? 1.1873 1.2359 1.1815 0.2639  -0.0428 -0.0646 393  GLU C CB  
12151 C  CG  . GLU C 393  ? 1.2340 1.2720 1.2317 0.2541  -0.0397 -0.0631 393  GLU C CG  
12152 C  CD  . GLU C 393  ? 1.3645 1.3994 1.3610 0.2559  -0.0397 -0.0650 393  GLU C CD  
12153 O  OE1 . GLU C 393  ? 1.4052 1.4390 1.3941 0.2658  -0.0413 -0.0667 393  GLU C OE1 
12154 O  OE2 . GLU C 393  ? 1.3813 1.4150 1.3841 0.2478  -0.0381 -0.0650 393  GLU C OE2 
12155 N  N   . ARG C 394  ? 0.9691 1.0592 0.9931 0.2476  -0.0436 -0.0668 394  ARG C N   
12156 C  CA  . ARG C 394  ? 0.9340 1.0347 0.9703 0.2370  -0.0422 -0.0668 394  ARG C CA  
12157 C  C   . ARG C 394  ? 1.0308 1.1356 1.0699 0.2331  -0.0422 -0.0655 394  ARG C C   
12158 O  O   . ARG C 394  ? 1.0465 1.1502 1.0915 0.2240  -0.0401 -0.0637 394  ARG C O   
12159 C  CB  . ARG C 394  ? 0.9306 1.0513 0.9765 0.2370  -0.0433 -0.0703 394  ARG C CB  
12160 C  CG  . ARG C 394  ? 1.0532 1.1713 1.1016 0.2340  -0.0418 -0.0709 394  ARG C CG  
12161 C  CD  . ARG C 394  ? 1.0276 1.1401 1.0678 0.2435  -0.0430 -0.0724 394  ARG C CD  
12162 N  NE  . ARG C 394  ? 1.0706 1.1757 1.1106 0.2405  -0.0415 -0.0727 394  ARG C NE  
12163 C  CZ  . ARG C 394  ? 1.2322 1.3359 1.2677 0.2471  -0.0422 -0.0746 394  ARG C CZ  
12164 N  NH1 . ARG C 394  ? 1.2922 1.4016 1.3232 0.2571  -0.0443 -0.0765 394  ARG C NH1 
12165 N  NH2 . ARG C 394  ? 1.2256 1.3221 1.2611 0.2436  -0.0409 -0.0749 394  ARG C NH2 
12166 N  N   . TYR C 395  ? 0.9504 1.0601 0.9851 0.2403  -0.0448 -0.0664 395  TYR C N   
12167 C  CA  . TYR C 395  ? 0.8127 0.9252 0.8486 0.2375  -0.0451 -0.0653 395  TYR C CA  
12168 C  C   . TYR C 395  ? 0.8409 0.9328 0.8689 0.2347  -0.0425 -0.0612 395  TYR C C   
12169 O  O   . TYR C 395  ? 0.8610 0.9524 0.8932 0.2272  -0.0408 -0.0594 395  TYR C O   
12170 C  CB  . TYR C 395  ? 0.8706 0.9925 0.9026 0.2468  -0.0489 -0.0675 395  TYR C CB  
12171 C  CG  . TYR C 395  ? 0.7974 0.9254 0.8314 0.2443  -0.0500 -0.0673 395  TYR C CG  
12172 C  CD1 . TYR C 395  ? 0.8623 0.9749 0.8862 0.2460  -0.0493 -0.0643 395  TYR C CD1 
12173 C  CD2 . TYR C 395  ? 0.8171 0.9657 0.8626 0.2402  -0.0515 -0.0703 395  TYR C CD2 
12174 C  CE1 . TYR C 395  ? 0.9531 1.0707 0.9781 0.2440  -0.0504 -0.0642 395  TYR C CE1 
12175 C  CE2 . TYR C 395  ? 0.9005 1.0542 0.9473 0.2378  -0.0527 -0.0704 395  TYR C CE2 
12176 C  CZ  . TYR C 395  ? 0.9289 1.0671 0.9653 0.2399  -0.0522 -0.0674 395  TYR C CZ  
12177 O  OH  . TYR C 395  ? 0.9049 1.0478 0.9422 0.2377  -0.0534 -0.0676 395  TYR C OH  
12178 N  N   . VAL C 396  ? 0.7711 0.8455 0.7874 0.2408  -0.0418 -0.0596 396  VAL C N   
12179 C  CA  . VAL C 396  ? 0.7745 0.8284 0.7827 0.2384  -0.0388 -0.0557 396  VAL C CA  
12180 C  C   . VAL C 396  ? 0.8291 0.8781 0.8446 0.2275  -0.0354 -0.0539 396  VAL C C   
12181 O  O   . VAL C 396  ? 0.8571 0.8985 0.8729 0.2216  -0.0329 -0.0512 396  VAL C O   
12182 C  CB  . VAL C 396  ? 0.8460 0.8819 0.8401 0.2471  -0.0385 -0.0546 396  VAL C CB  
12183 C  CG1 . VAL C 396  ? 0.7796 0.7937 0.7677 0.2423  -0.0343 -0.0508 396  VAL C CG1 
12184 C  CG2 . VAL C 396  ? 0.8580 0.8943 0.8424 0.2575  -0.0412 -0.0550 396  VAL C CG2 
12185 N  N   . ILE C 397  ? 1.0438 1.0971 1.0651 0.2249  -0.0353 -0.0556 397  ILE C N   
12186 C  CA  . ILE C 397  ? 1.0446 1.0933 1.0724 0.2153  -0.0325 -0.0543 397  ILE C CA  
12187 C  C   . ILE C 397  ? 1.0791 1.1401 1.1177 0.2071  -0.0318 -0.0540 397  ILE C C   
12188 O  O   . ILE C 397  ? 1.0605 1.1143 1.1014 0.1999  -0.0292 -0.0515 397  ILE C O   
12189 C  CB  . ILE C 397  ? 1.0348 1.0861 1.0656 0.2155  -0.0329 -0.0566 397  ILE C CB  
12190 C  CG1 . ILE C 397  ? 1.2225 1.2563 1.2419 0.2215  -0.0325 -0.0562 397  ILE C CG1 
12191 C  CG2 . ILE C 397  ? 0.9930 1.0459 1.0331 0.2054  -0.0309 -0.0560 397  ILE C CG2 
12192 C  CD1 . ILE C 397  ? 1.3201 1.3542 1.3412 0.2217  -0.0329 -0.0584 397  ILE C CD1 
12193 N  N   . ILE C 398  ? 0.7675 0.8469 0.8126 0.2079  -0.0341 -0.0566 398  ILE C N   
12194 C  CA  . ILE C 398  ? 0.7510 0.8427 0.8066 0.1999  -0.0334 -0.0567 398  ILE C CA  
12195 C  C   . ILE C 398  ? 0.8308 0.9228 0.8846 0.1993  -0.0335 -0.0554 398  ILE C C   
12196 O  O   . ILE C 398  ? 0.8377 0.9237 0.8933 0.1928  -0.0311 -0.0528 398  ILE C O   
12197 C  CB  . ILE C 398  ? 0.7914 0.9027 0.8554 0.2002  -0.0353 -0.0603 398  ILE C CB  
12198 C  CG1 . ILE C 398  ? 0.7086 0.8191 0.7736 0.2011  -0.0350 -0.0616 398  ILE C CG1 
12199 C  CG2 . ILE C 398  ? 0.7577 0.8804 0.8318 0.1917  -0.0342 -0.0604 398  ILE C CG2 
12200 C  CD1 . ILE C 398  ? 0.7035 0.8325 0.7762 0.2018  -0.0363 -0.0650 398  ILE C CD1 
12201 N  N   . VAL C 399  ? 0.7942 0.8936 0.8446 0.2062  -0.0364 -0.0572 399  VAL C N   
12202 C  CA  . VAL C 399  ? 0.6495 0.7532 0.6998 0.2054  -0.0372 -0.0568 399  VAL C CA  
12203 C  C   . VAL C 399  ? 0.6178 0.7032 0.6586 0.2060  -0.0352 -0.0531 399  VAL C C   
12204 O  O   . VAL C 399  ? 0.6717 0.7549 0.7143 0.2002  -0.0334 -0.0512 399  VAL C O   
12205 C  CB  . VAL C 399  ? 0.6486 0.7657 0.6978 0.2132  -0.0413 -0.0602 399  VAL C CB  
12206 C  CG1 . VAL C 399  ? 0.6575 0.7763 0.7041 0.2135  -0.0425 -0.0598 399  VAL C CG1 
12207 C  CG2 . VAL C 399  ? 0.7703 0.9074 0.8307 0.2109  -0.0426 -0.0638 399  VAL C CG2 
12208 N  N   . ILE C 400  ? 0.8737 0.9452 0.9037 0.2131  -0.0352 -0.0519 400  ILE C N   
12209 C  CA  . ILE C 400  ? 0.9480 1.0015 0.9679 0.2143  -0.0329 -0.0483 400  ILE C CA  
12210 C  C   . ILE C 400  ? 0.9767 1.0203 1.0003 0.2050  -0.0286 -0.0453 400  ILE C C   
12211 O  O   . ILE C 400  ? 0.9810 1.0175 1.0023 0.2019  -0.0264 -0.0427 400  ILE C O   
12212 C  CB  . ILE C 400  ? 0.9482 0.9877 0.9554 0.2235  -0.0332 -0.0477 400  ILE C CB  
12213 C  CG1 . ILE C 400  ? 0.9047 0.9534 0.9069 0.2337  -0.0376 -0.0504 400  ILE C CG1 
12214 C  CG2 . ILE C 400  ? 0.8894 0.9079 0.8863 0.2236  -0.0298 -0.0436 400  ILE C CG2 
12215 C  CD1 . ILE C 400  ? 1.0159 1.0498 1.0038 0.2438  -0.0380 -0.0495 400  ILE C CD1 
12216 N  N   . SER C 401  ? 0.8636 0.9070 0.8931 0.2007  -0.0274 -0.0457 401  SER C N   
12217 C  CA  . SER C 401  ? 0.8236 0.8589 0.8575 0.1921  -0.0237 -0.0432 401  SER C CA  
12218 C  C   . SER C 401  ? 0.6963 0.7424 0.7396 0.1845  -0.0230 -0.0430 401  SER C C   
12219 O  O   . SER C 401  ? 0.6129 0.6515 0.6575 0.1787  -0.0199 -0.0403 401  SER C O   
12220 C  CB  . SER C 401  ? 0.8237 0.8576 0.8617 0.1897  -0.0232 -0.0443 401  SER C CB  
12221 O  OG  . SER C 401  ? 0.9274 0.9526 0.9690 0.1820  -0.0199 -0.0421 401  SER C OG  
12222 N  N   . LEU C 402  ? 0.8821 0.9455 0.9319 0.1845  -0.0256 -0.0459 402  LEU C N   
12223 C  CA  . LEU C 402  ? 0.9444 1.0178 1.0027 0.1773  -0.0249 -0.0459 402  LEU C CA  
12224 C  C   . LEU C 402  ? 0.8858 0.9590 0.9403 0.1782  -0.0251 -0.0450 402  LEU C C   
12225 O  O   . LEU C 402  ? 0.9122 0.9892 0.9718 0.1720  -0.0237 -0.0441 402  LEU C O   
12226 C  CB  . LEU C 402  ? 0.9371 1.0288 1.0042 0.1762  -0.0271 -0.0494 402  LEU C CB  
12227 C  CG  . LEU C 402  ? 0.8283 0.9236 0.9033 0.1705  -0.0258 -0.0499 402  LEU C CG  
12228 C  CD1 . LEU C 402  ? 0.9596 1.0729 1.0422 0.1698  -0.0276 -0.0532 402  LEU C CD1 
12229 C  CD2 . LEU C 402  ? 0.7832 0.8732 0.8623 0.1624  -0.0226 -0.0472 402  LEU C CD2 
12230 N  N   . GLU C 403  ? 0.9766 1.0451 1.0216 0.1861  -0.0270 -0.0451 403  GLU C N   
12231 C  CA  . GLU C 403  ? 0.9250 0.9942 0.9657 0.1878  -0.0278 -0.0446 403  GLU C CA  
12232 C  C   . GLU C 403  ? 0.9765 1.0310 1.0130 0.1839  -0.0238 -0.0406 403  GLU C C   
12233 O  O   . GLU C 403  ? 1.0153 1.0728 1.0538 0.1801  -0.0231 -0.0399 403  GLU C O   
12234 C  CB  . GLU C 403  ? 0.9493 1.0173 0.9802 0.1981  -0.0310 -0.0460 403  GLU C CB  
12235 C  CG  . GLU C 403  ? 1.0166 1.1035 1.0524 0.2017  -0.0355 -0.0504 403  GLU C CG  
12236 C  CD  . GLU C 403  ? 1.1921 1.2781 1.2179 0.2125  -0.0390 -0.0518 403  GLU C CD  
12237 O  OE1 . GLU C 403  ? 1.3512 1.4207 1.3654 0.2174  -0.0377 -0.0490 403  GLU C OE1 
12238 O  OE2 . GLU C 403  ? 1.1845 1.2865 1.2140 0.2162  -0.0429 -0.0556 403  GLU C OE2 
12239 N  N   . ARG C 404  ? 0.8214 0.8601 0.8523 0.1848  -0.0210 -0.0378 404  ARG C N   
12240 C  CA  . ARG C 404  ? 0.8322 0.8560 0.8584 0.1818  -0.0169 -0.0339 404  ARG C CA  
12241 C  C   . ARG C 404  ? 0.7718 0.7898 0.8043 0.1749  -0.0134 -0.0323 404  ARG C C   
12242 O  O   . ARG C 404  ? 0.8597 0.8698 0.8897 0.1766  -0.0128 -0.0321 404  ARG C O   
12243 C  CB  . ARG C 404  ? 0.8468 0.8554 0.8591 0.1896  -0.0163 -0.0320 404  ARG C CB  
12244 C  CG  . ARG C 404  ? 0.8791 0.8941 0.8847 0.1976  -0.0204 -0.0340 404  ARG C CG  
12245 C  CD  . ARG C 404  ? 0.9020 0.9012 0.8932 0.2040  -0.0190 -0.0313 404  ARG C CD  
12246 N  NE  . ARG C 404  ? 0.9270 0.9338 0.9136 0.2093  -0.0227 -0.0330 404  ARG C NE  
12247 C  CZ  . ARG C 404  ? 0.8513 0.8472 0.8248 0.2160  -0.0225 -0.0313 404  ARG C CZ  
12248 N  NH1 . ARG C 404  ? 0.8356 0.8118 0.7990 0.2181  -0.0185 -0.0275 404  ARG C NH1 
12249 N  NH2 . ARG C 404  ? 0.8072 0.8120 0.7776 0.2206  -0.0265 -0.0335 404  ARG C NH2 
12250 N  N   . ASP C 405  ? 0.7886 0.8106 0.8291 0.1672  -0.0113 -0.0312 405  ASP C N   
12251 C  CA  . ASP C 405  ? 0.7958 0.8156 0.8439 0.1602  -0.0086 -0.0302 405  ASP C CA  
12252 C  C   . ASP C 405  ? 0.8985 0.9045 0.9439 0.1568  -0.0040 -0.0263 405  ASP C C   
12253 O  O   . ASP C 405  ? 0.9531 0.9475 0.9886 0.1611  -0.0025 -0.0243 405  ASP C O   
12254 C  CB  . ASP C 405  ? 0.8680 0.9030 0.9270 0.1546  -0.0098 -0.0320 405  ASP C CB  
12255 C  CG  . ASP C 405  ? 1.1672 1.2119 1.2313 0.1555  -0.0125 -0.0352 405  ASP C CG  
12256 O  OD1 . ASP C 405  ? 1.2736 1.3115 1.3349 0.1581  -0.0127 -0.0354 405  ASP C OD1 
12257 O  OD2 . ASP C 405  ? 1.2010 1.2597 1.2715 0.1536  -0.0144 -0.0374 405  ASP C OD2 
12258 N  N   . PHE C 406  ? 0.8844 0.8919 0.9383 0.1494  -0.0015 -0.0253 406  PHE C N   
12259 C  CA  . PHE C 406  ? 0.9399 0.9356 0.9928 0.1457  0.0032  -0.0218 406  PHE C CA  
12260 C  C   . PHE C 406  ? 0.8586 0.8530 0.9078 0.1457  0.0047  -0.0198 406  PHE C C   
12261 O  O   . PHE C 406  ? 0.9114 0.8933 0.9526 0.1478  0.0077  -0.0171 406  PHE C O   
12262 C  CB  . PHE C 406  ? 0.9831 0.9822 1.0468 0.1383  0.0048  -0.0216 406  PHE C CB  
12263 C  CG  . PHE C 406  ? 0.9463 0.9480 1.0141 0.1380  0.0029  -0.0239 406  PHE C CG  
12264 C  CD1 . PHE C 406  ? 0.9283 0.9183 0.9925 0.1390  0.0043  -0.0234 406  PHE C CD1 
12265 C  CD2 . PHE C 406  ? 0.8892 0.9046 0.9640 0.1366  -0.0002 -0.0267 406  PHE C CD2 
12266 C  CE1 . PHE C 406  ? 0.9062 0.8981 0.9736 0.1389  0.0023  -0.0258 406  PHE C CE1 
12267 C  CE2 . PHE C 406  ? 0.8328 0.8503 0.9107 0.1367  -0.0020 -0.0288 406  PHE C CE2 
12268 C  CZ  . PHE C 406  ? 0.8726 0.8784 0.9468 0.1379  -0.0009 -0.0285 406  PHE C CZ  
12269 N  N   . LEU C 407  ? 0.7208 0.7274 0.7752 0.1433  0.0031  -0.0211 407  LEU C N   
12270 C  CA  . LEU C 407  ? 0.7571 0.7630 0.8081 0.1431  0.0043  -0.0197 407  LEU C CA  
12271 C  C   . LEU C 407  ? 0.8417 0.8479 0.8833 0.1503  0.0013  -0.0210 407  LEU C C   
12272 O  O   . LEU C 407  ? 0.8706 0.8883 0.9142 0.1527  -0.0030 -0.0243 407  LEU C O   
12273 C  CB  . LEU C 407  ? 0.8653 0.8833 0.9250 0.1377  0.0038  -0.0208 407  LEU C CB  
12274 C  CG  . LEU C 407  ? 0.8570 0.8744 0.9251 0.1308  0.0071  -0.0190 407  LEU C CG  
12275 C  CD1 . LEU C 407  ? 0.7511 0.7768 0.8241 0.1266  0.0074  -0.0192 407  LEU C CD1 
12276 C  CD2 . LEU C 407  ? 0.5614 0.5649 0.6261 0.1299  0.0117  -0.0155 407  LEU C CD2 
12277 N  N   . PRO C 408  ? 0.7743 0.7686 0.8056 0.1542  0.0032  -0.0186 408  PRO C N   
12278 C  CA  . PRO C 408  ? 0.6900 0.6845 0.7116 0.1619  -0.0001 -0.0199 408  PRO C CA  
12279 C  C   . PRO C 408  ? 0.6724 0.6802 0.6966 0.1614  -0.0034 -0.0225 408  PRO C C   
12280 O  O   . PRO C 408  ? 0.7442 0.7583 0.7643 0.1671  -0.0077 -0.0252 408  PRO C O   
12281 C  CB  . PRO C 408  ? 0.7059 0.6837 0.7162 0.1649  0.0037  -0.0162 408  PRO C CB  
12282 C  CG  . PRO C 408  ? 0.7717 0.7397 0.7857 0.1599  0.0087  -0.0133 408  PRO C CG  
12283 C  CD  . PRO C 408  ? 0.7855 0.7651 0.8132 0.1523  0.0086  -0.0145 408  PRO C CD  
12284 N  N   . SER C 409  ? 0.8707 0.8828 0.9014 0.1549  -0.0016 -0.0219 409  SER C N   
12285 C  CA  . SER C 409  ? 0.9232 0.9471 0.9563 0.1537  -0.0044 -0.0245 409  SER C CA  
12286 C  C   . SER C 409  ? 0.9698 1.0095 1.0110 0.1530  -0.0085 -0.0286 409  SER C C   
12287 O  O   . SER C 409  ? 1.0661 1.1162 1.1079 0.1539  -0.0118 -0.0316 409  SER C O   
12288 C  CB  . SER C 409  ? 0.9340 0.9576 0.9718 0.1469  -0.0009 -0.0226 409  SER C CB  
12289 O  OG  . SER C 409  ? 0.9889 1.0133 1.0358 0.1412  0.0015  -0.0216 409  SER C OG  
12290 N  N   . SER C 410  ? 1.2252 1.2669 1.2726 0.1512  -0.0082 -0.0289 410  SER C N   
12291 C  CA  . SER C 410  ? 1.2783 1.3342 1.3331 0.1507  -0.0116 -0.0326 410  SER C CA  
12292 C  C   . SER C 410  ? 1.3357 1.3933 1.3857 0.1583  -0.0151 -0.0347 410  SER C C   
12293 O  O   . SER C 410  ? 1.4217 1.4854 1.4765 0.1587  -0.0165 -0.0366 410  SER C O   
12294 C  CB  . SER C 410  ? 1.3424 1.4001 1.4062 0.1450  -0.0095 -0.0320 410  SER C CB  
12295 O  OG  . SER C 410  ? 1.3102 1.3662 1.3781 0.1386  -0.0063 -0.0300 410  SER C OG  
12296 N  N   . TRP C 411  ? 0.8947 0.9467 0.9347 0.1647  -0.0165 -0.0345 411  TRP C N   
12297 C  CA  . TRP C 411  ? 0.7604 0.8130 0.7944 0.1730  -0.0198 -0.0363 411  TRP C CA  
12298 C  C   . TRP C 411  ? 0.6936 0.7604 0.7281 0.1763  -0.0246 -0.0403 411  TRP C C   
12299 O  O   . TRP C 411  ? 0.8597 0.9285 0.8923 0.1753  -0.0251 -0.0406 411  TRP C O   
12300 C  CB  . TRP C 411  ? 0.8739 0.9094 0.8952 0.1789  -0.0181 -0.0333 411  TRP C CB  
12301 C  CG  . TRP C 411  ? 0.8886 0.9102 0.9090 0.1766  -0.0138 -0.0299 411  TRP C CG  
12302 C  CD1 . TRP C 411  ? 0.9026 0.9257 0.9325 0.1697  -0.0116 -0.0294 411  TRP C CD1 
12303 C  CD2 . TRP C 411  ? 0.8936 0.8975 0.9031 0.1810  -0.0111 -0.0268 411  TRP C CD2 
12304 N  NE1 . TRP C 411  ? 0.9522 0.9606 0.9784 0.1693  -0.0079 -0.0265 411  TRP C NE1 
12305 C  CE2 . TRP C 411  ? 0.8873 0.8834 0.9011 0.1760  -0.0073 -0.0248 411  TRP C CE2 
12306 C  CE3 . TRP C 411  ? 0.8582 0.8520 0.8544 0.1888  -0.0115 -0.0257 411  TRP C CE3 
12307 C  CZ2 . TRP C 411  ? 0.8436 0.8221 0.8494 0.1778  -0.0037 -0.0217 411  TRP C CZ2 
12308 C  CZ3 . TRP C 411  ? 0.8774 0.8529 0.8648 0.1911  -0.0077 -0.0223 411  TRP C CZ3 
12309 C  CH2 . TRP C 411  ? 0.9018 0.8699 0.8943 0.1853  -0.0037 -0.0203 411  TRP C CH2 
12310 N  N   . ASP C 412  ? 0.4926 0.5695 0.5298 0.1803  -0.0280 -0.0435 412  ASP C N   
12311 C  CA  . ASP C 412  ? 0.5669 0.6587 0.6054 0.1839  -0.0327 -0.0478 412  ASP C CA  
12312 C  C   . ASP C 412  ? 0.6528 0.7490 0.6896 0.1914  -0.0358 -0.0500 412  ASP C C   
12313 O  O   . ASP C 412  ? 0.7639 0.8515 0.7987 0.1929  -0.0341 -0.0483 412  ASP C O   
12314 C  CB  . ASP C 412  ? 0.6470 0.7543 0.6975 0.1762  -0.0331 -0.0504 412  ASP C CB  
12315 C  CG  . ASP C 412  ? 0.7098 0.8317 0.7617 0.1784  -0.0375 -0.0548 412  ASP C CG  
12316 O  OD1 . ASP C 412  ? 0.7092 0.8283 0.7559 0.1789  -0.0382 -0.0546 412  ASP C OD1 
12317 O  OD2 . ASP C 412  ? 0.7921 0.9284 0.8504 0.1798  -0.0403 -0.0585 412  ASP C OD2 
12318 N  N   . ILE C 413  ? 0.7234 0.8330 0.7608 0.1961  -0.0404 -0.0540 413  ILE C N   
12319 C  CA  . ILE C 413  ? 0.7595 0.8749 0.7949 0.2043  -0.0437 -0.0565 413  ILE C CA  
12320 C  C   . ILE C 413  ? 0.8559 0.9911 0.9038 0.2011  -0.0456 -0.0606 413  ILE C C   
12321 O  O   . ILE C 413  ? 0.7685 0.9154 0.8246 0.1948  -0.0459 -0.0627 413  ILE C O   
12322 C  CB  . ILE C 413  ? 0.7799 0.8949 0.8050 0.2140  -0.0477 -0.0579 413  ILE C CB  
12323 C  CG1 . ILE C 413  ? 0.9301 1.0467 0.9508 0.2236  -0.0505 -0.0595 413  ILE C CG1 
12324 C  CG2 . ILE C 413  ? 0.6871 0.8188 0.7177 0.2123  -0.0513 -0.0619 413  ILE C CG2 
12325 C  CD1 . ILE C 413  ? 1.0989 1.2133 1.1080 0.2343  -0.0544 -0.0605 413  ILE C CD1 
12326 N  N   . TYR C 414  ? 1.1049 1.2433 1.1539 0.2055  -0.0466 -0.0619 414  TYR C N   
12327 C  CA  . TYR C 414  ? 1.0643 1.2209 1.1245 0.2035  -0.0480 -0.0657 414  TYR C CA  
12328 C  C   . TYR C 414  ? 1.0857 1.2546 1.1442 0.2126  -0.0529 -0.0697 414  TYR C C   
12329 O  O   . TYR C 414  ? 1.1267 1.2884 1.1766 0.2215  -0.0543 -0.0692 414  TYR C O   
12330 C  CB  . TYR C 414  ? 1.0156 1.1678 1.0787 0.2018  -0.0455 -0.0644 414  TYR C CB  
12331 C  CG  . TYR C 414  ? 1.0052 1.1750 1.0781 0.2013  -0.0468 -0.0682 414  TYR C CG  
12332 C  CD1 . TYR C 414  ? 1.0366 1.2188 1.1207 0.1928  -0.0455 -0.0698 414  TYR C CD1 
12333 C  CD2 . TYR C 414  ? 1.0359 1.2095 1.1064 0.2096  -0.0491 -0.0702 414  TYR C CD2 
12334 C  CE1 . TYR C 414  ? 0.9769 1.1749 1.0697 0.1922  -0.0462 -0.0731 414  TYR C CE1 
12335 C  CE2 . TYR C 414  ? 1.0579 1.2479 1.1373 0.2093  -0.0500 -0.0736 414  TYR C CE2 
12336 C  CZ  . TYR C 414  ? 1.0145 1.2167 1.1052 0.2005  -0.0484 -0.0750 414  TYR C CZ  
12337 O  OH  . TYR C 414  ? 1.0595 1.2776 1.1589 0.2001  -0.0487 -0.0783 414  TYR C OH  
12338 N  N   . ILE C 415  ? 1.0752 1.2623 1.1419 0.2104  -0.0555 -0.0737 415  ILE C N   
12339 C  CA  . ILE C 415  ? 1.0550 1.2572 1.1224 0.2183  -0.0604 -0.0782 415  ILE C CA  
12340 C  C   . ILE C 415  ? 1.0779 1.3000 1.1590 0.2142  -0.0606 -0.0821 415  ILE C C   
12341 O  O   . ILE C 415  ? 1.0816 1.3142 1.1719 0.2059  -0.0598 -0.0838 415  ILE C O   
12342 C  CB  . ILE C 415  ? 1.1063 1.3132 1.1704 0.2205  -0.0639 -0.0802 415  ILE C CB  
12343 C  CG1 . ILE C 415  ? 1.1107 1.2966 1.1616 0.2227  -0.0626 -0.0758 415  ILE C CG1 
12344 C  CG2 . ILE C 415  ? 1.0725 1.2933 1.1357 0.2304  -0.0694 -0.0846 415  ILE C CG2 
12345 C  CD1 . ILE C 415  ? 1.1592 1.3479 1.2064 0.2236  -0.0655 -0.0773 415  ILE C CD1 
12346 N  N   . PRO C 416  ? 1.0302 1.2574 1.1125 0.2198  -0.0614 -0.0834 416  PRO C N   
12347 C  CA  . PRO C 416  ? 0.9621 1.2079 1.0571 0.2160  -0.0610 -0.0869 416  PRO C CA  
12348 C  C   . PRO C 416  ? 0.9689 1.2360 1.0715 0.2165  -0.0648 -0.0922 416  PRO C C   
12349 O  O   . PRO C 416  ? 1.0375 1.3068 1.1346 0.2234  -0.0689 -0.0939 416  PRO C O   
12350 C  CB  . PRO C 416  ? 0.9170 1.1613 1.0089 0.2240  -0.0614 -0.0871 416  PRO C CB  
12351 C  CG  . PRO C 416  ? 1.0382 1.2692 1.1163 0.2342  -0.0639 -0.0854 416  PRO C CG  
12352 C  CD  . PRO C 416  ? 1.0579 1.2732 1.1295 0.2298  -0.0622 -0.0818 416  PRO C CD  
12353 N  N   . THR C 417  ? 0.6899 0.9724 0.8052 0.2089  -0.0632 -0.0948 417  THR C N   
12354 C  CA  . THR C 417  ? 0.8285 1.1323 0.9529 0.2076  -0.0662 -0.1002 417  THR C CA  
12355 C  C   . THR C 417  ? 0.8633 1.1840 0.9932 0.2144  -0.0684 -0.1041 417  THR C C   
12356 O  O   . THR C 417  ? 0.8517 1.1659 0.9756 0.2223  -0.0686 -0.1027 417  THR C O   
12357 C  CB  . THR C 417  ? 0.8216 1.1320 0.9563 0.1949  -0.0628 -0.1008 417  THR C CB  
12358 O  OG1 . THR C 417  ? 0.7765 1.0879 0.9171 0.1903  -0.0586 -0.0997 417  THR C OG1 
12359 C  CG2 . THR C 417  ? 0.8745 1.1681 1.0030 0.1890  -0.0608 -0.0969 417  THR C CG2 
12360 N  N   . ILE C 418  ? 0.7266 1.0693 0.8683 0.2114  -0.0699 -0.1092 418  ILE C N   
12361 C  CA  . ILE C 418  ? 0.6649 1.0258 0.8134 0.2173  -0.0716 -0.1133 418  ILE C CA  
12362 C  C   . ILE C 418  ? 0.6587 1.0254 0.8162 0.2111  -0.0668 -0.1131 418  ILE C C   
12363 O  O   . ILE C 418  ? 0.7279 1.1036 0.8882 0.2170  -0.0671 -0.1149 418  ILE C O   
12364 C  CB  . ILE C 418  ? 0.6515 1.0348 0.8084 0.2180  -0.0760 -0.1194 418  ILE C CB  
12365 C  CG1 . ILE C 418  ? 0.5040 0.9008 0.6634 0.2237  -0.0777 -0.1226 418  ILE C CG1 
12366 C  CG2 . ILE C 418  ? 0.7468 1.1405 0.9156 0.2050  -0.0732 -0.1214 418  ILE C CG2 
12367 C  CD1 . ILE C 418  ? 0.5951 1.0103 0.7597 0.2240  -0.0821 -0.1281 418  ILE C CD1 
12368 N  N   . TRP C 419  ? 0.8267 1.1877 0.9881 0.1999  -0.0623 -0.1109 419  TRP C N   
12369 C  CA  . TRP C 419  ? 0.9352 1.3032 1.1056 0.1936  -0.0577 -0.1112 419  TRP C CA  
12370 C  C   . TRP C 419  ? 0.9985 1.3526 1.1625 0.1972  -0.0552 -0.1074 419  TRP C C   
12371 O  O   . TRP C 419  ? 1.0495 1.4121 1.2188 0.1981  -0.0533 -0.1086 419  TRP C O   
12372 C  CB  . TRP C 419  ? 0.8829 1.2493 1.0588 0.1808  -0.0539 -0.1102 419  TRP C CB  
12373 C  CG  . TRP C 419  ? 0.8499 1.2326 1.0340 0.1762  -0.0558 -0.1148 419  TRP C CG  
12374 C  CD1 . TRP C 419  ? 0.8908 1.2694 1.0721 0.1732  -0.0578 -0.1150 419  TRP C CD1 
12375 C  CD2 . TRP C 419  ? 0.8628 1.2690 1.0597 0.1740  -0.0559 -0.1201 419  TRP C CD2 
12376 N  NE1 . TRP C 419  ? 0.9251 1.3228 1.1164 0.1690  -0.0594 -0.1203 419  TRP C NE1 
12377 C  CE2 . TRP C 419  ? 0.9232 1.3384 1.1246 0.1693  -0.0581 -0.1236 419  TRP C CE2 
12378 C  CE3 . TRP C 419  ? 0.8066 1.2270 1.0115 0.1755  -0.0540 -0.1225 419  TRP C CE3 
12379 C  CZ2 . TRP C 419  ? 0.8712 1.3094 1.0853 0.1656  -0.0587 -0.1294 419  TRP C CZ2 
12380 C  CZ3 . TRP C 419  ? 0.8519 1.2953 1.0696 0.1720  -0.0543 -0.1280 419  TRP C CZ3 
12381 C  CH2 . TRP C 419  ? 0.9089 1.3612 1.1314 0.1669  -0.0566 -0.1315 419  TRP C CH2 
12382 N  N   . ASP C 420  ? 1.2861 1.6188 1.4387 0.1992  -0.0551 -0.1028 420  ASP C N   
12383 C  CA  . ASP C 420  ? 1.4040 1.7230 1.5501 0.2029  -0.0531 -0.0996 420  ASP C CA  
12384 C  C   . ASP C 420  ? 1.3839 1.7071 1.5259 0.2149  -0.0563 -0.1015 420  ASP C C   
12385 O  O   . ASP C 420  ? 1.4135 1.7344 1.5545 0.2179  -0.0546 -0.1009 420  ASP C O   
12386 C  CB  . ASP C 420  ? 1.3648 1.6604 1.5005 0.2016  -0.0521 -0.0946 420  ASP C CB  
12387 C  CG  . ASP C 420  ? 1.3365 1.6259 1.4644 0.2063  -0.0556 -0.0942 420  ASP C CG  
12388 O  OD1 . ASP C 420  ? 1.3627 1.6659 1.4929 0.2112  -0.0595 -0.0980 420  ASP C OD1 
12389 O  OD2 . ASP C 420  ? 1.3823 1.6532 1.5019 0.2051  -0.0546 -0.0902 420  ASP C OD2 
12390 N  N   . TRP C 421  ? 0.8204 1.1494 0.9594 0.2222  -0.0609 -0.1038 421  TRP C N   
12391 C  CA  . TRP C 421  ? 0.8246 1.1585 0.9593 0.2319  -0.0636 -0.1057 421  TRP C CA  
12392 C  C   . TRP C 421  ? 0.8281 1.1806 0.9730 0.2287  -0.0622 -0.1091 421  TRP C C   
12393 O  O   . TRP C 421  ? 0.8780 1.2292 1.0199 0.2324  -0.0612 -0.1088 421  TRP C O   
12394 C  CB  . TRP C 421  ? 0.8095 1.1447 0.9378 0.2382  -0.0686 -0.1072 421  TRP C CB  
12395 C  CG  . TRP C 421  ? 0.7959 1.1100 0.9100 0.2449  -0.0700 -0.1035 421  TRP C CG  
12396 C  CD1 . TRP C 421  ? 0.7779 1.0853 0.8878 0.2457  -0.0718 -0.1025 421  TRP C CD1 
12397 C  CD2 . TRP C 421  ? 0.8342 1.1307 0.9360 0.2519  -0.0694 -0.1004 421  TRP C CD2 
12398 N  NE1 . TRP C 421  ? 0.8412 1.1275 0.9368 0.2525  -0.0721 -0.0987 421  TRP C NE1 
12399 C  CE2 . TRP C 421  ? 0.8219 1.1013 0.9125 0.2563  -0.0706 -0.0974 421  TRP C CE2 
12400 C  CE3 . TRP C 421  ? 0.8280 1.1213 0.9269 0.2549  -0.0677 -0.0998 421  TRP C CE3 
12401 C  CZ2 . TRP C 421  ? 0.7851 1.0442 0.8621 0.2631  -0.0700 -0.0940 421  TRP C CZ2 
12402 C  CZ3 . TRP C 421  ? 0.8453 1.1187 0.9307 0.2617  -0.0676 -0.0966 421  TRP C CZ3 
12403 C  CH2 . TRP C 421  ? 0.7808 1.0372 0.8555 0.2655  -0.0686 -0.0937 421  TRP C CH2 
12404 N  N   . SER C 422  ? 0.7911 1.1610 0.9480 0.2216  -0.0619 -0.1124 422  SER C N   
12405 C  CA  . SER C 422  ? 0.7785 1.1664 0.9460 0.2175  -0.0599 -0.1156 422  SER C CA  
12406 C  C   . SER C 422  ? 0.8874 1.2707 1.0568 0.2145  -0.0551 -0.1135 422  SER C C   
12407 O  O   . SER C 422  ? 0.8932 1.2841 1.0649 0.2159  -0.0537 -0.1148 422  SER C O   
12408 C  CB  . SER C 422  ? 0.6936 1.0984 0.8737 0.2090  -0.0597 -0.1191 422  SER C CB  
12409 O  OG  . SER C 422  ? 0.8949 1.3050 1.0733 0.2120  -0.0646 -0.1216 422  SER C OG  
12410 N  N   . LEU C 423  ? 0.8768 1.2477 1.0450 0.2108  -0.0525 -0.1103 423  LEU C N   
12411 C  CA  . LEU C 423  ? 0.7647 1.1292 0.9331 0.2088  -0.0483 -0.1081 423  LEU C CA  
12412 C  C   . LEU C 423  ? 0.7679 1.1197 0.9251 0.2174  -0.0492 -0.1062 423  LEU C C   
12413 O  O   . LEU C 423  ? 0.8124 1.1647 0.9702 0.2176  -0.0466 -0.1060 423  LEU C O   
12414 C  CB  . LEU C 423  ? 0.7274 1.0762 0.8934 0.2008  -0.0453 -0.1041 423  LEU C CB  
12415 C  CG  . LEU C 423  ? 0.7701 1.1263 0.9457 0.1890  -0.0411 -0.1045 423  LEU C CG  
12416 C  CD1 . LEU C 423  ? 0.8553 1.1932 1.0260 0.1817  -0.0387 -0.1000 423  LEU C CD1 
12417 C  CD2 . LEU C 423  ? 0.7150 1.0812 0.8969 0.1881  -0.0376 -0.1058 423  LEU C CD2 
12418 N  N   . TYR C 424  ? 1.0899 1.4299 1.2364 0.2245  -0.0528 -0.1048 424  TYR C N   
12419 C  CA  . TYR C 424  ? 1.1142 1.4408 1.2491 0.2327  -0.0536 -0.1030 424  TYR C CA  
12420 C  C   . TYR C 424  ? 1.0963 1.4347 1.2318 0.2373  -0.0545 -0.1058 424  TYR C C   
12421 O  O   . TYR C 424  ? 1.1760 1.5120 1.3096 0.2392  -0.0525 -0.1053 424  TYR C O   
12422 C  CB  . TYR C 424  ? 1.1869 1.4980 1.3100 0.2391  -0.0568 -0.1009 424  TYR C CB  
12423 C  CG  . TYR C 424  ? 1.1272 1.4190 1.2379 0.2457  -0.0565 -0.0981 424  TYR C CG  
12424 C  CD1 . TYR C 424  ? 0.9960 1.2806 1.1070 0.2435  -0.0532 -0.0965 424  TYR C CD1 
12425 C  CD2 . TYR C 424  ? 1.1494 1.4298 1.2477 0.2541  -0.0595 -0.0970 424  TYR C CD2 
12426 C  CE1 . TYR C 424  ? 1.0999 1.3667 1.1996 0.2492  -0.0531 -0.0943 424  TYR C CE1 
12427 C  CE2 . TYR C 424  ? 1.1455 1.4075 1.2322 0.2598  -0.0589 -0.0945 424  TYR C CE2 
12428 C  CZ  . TYR C 424  ? 1.1407 1.3962 1.2285 0.2571  -0.0558 -0.0933 424  TYR C CZ  
12429 O  OH  . TYR C 424  ? 1.1982 1.4353 1.2746 0.2626  -0.0554 -0.0912 424  TYR C OH  
12430 N  N   . ILE C 425  ? 0.4791 0.8303 0.6169 0.2394  -0.0577 -0.1087 425  ILE C N   
12431 C  CA  . ILE C 425  ? 0.4928 0.8576 0.6327 0.2432  -0.0585 -0.1118 425  ILE C CA  
12432 C  C   . ILE C 425  ? 0.5304 0.9084 0.6816 0.2367  -0.0543 -0.1133 425  ILE C C   
12433 O  O   . ILE C 425  ? 0.5247 0.9069 0.6753 0.2401  -0.0532 -0.1141 425  ILE C O   
12434 C  CB  . ILE C 425  ? 0.3488 0.7272 0.4913 0.2452  -0.0626 -0.1152 425  ILE C CB  
12435 C  CG1 . ILE C 425  ? 0.4733 0.8380 0.6022 0.2538  -0.0668 -0.1137 425  ILE C CG1 
12436 C  CG2 . ILE C 425  ? 0.3923 0.7888 0.5407 0.2470  -0.0629 -0.1189 425  ILE C CG2 
12437 C  CD1 . ILE C 425  ? 0.5653 0.9198 0.6915 0.2514  -0.0679 -0.1117 425  ILE C CD1 
12438 N  N   . GLY C 426  ? 0.7497 1.1340 0.9110 0.2274  -0.0517 -0.1135 426  GLY C N   
12439 C  CA  . GLY C 426  ? 0.7195 1.1150 0.8908 0.2210  -0.0472 -0.1146 426  GLY C CA  
12440 C  C   . GLY C 426  ? 0.8409 1.2245 1.0069 0.2227  -0.0441 -0.1120 426  GLY C C   
12441 O  O   . GLY C 426  ? 0.9219 1.3134 1.0916 0.2225  -0.0414 -0.1131 426  GLY C O   
12442 N  N   . THR C 427  ? 0.9946 1.3590 1.1520 0.2245  -0.0444 -0.1085 427  THR C N   
12443 C  CA  . THR C 427  ? 0.9799 1.3320 1.1315 0.2265  -0.0419 -0.1063 427  THR C CA  
12444 C  C   . THR C 427  ? 1.0226 1.3712 1.1656 0.2355  -0.0436 -0.1067 427  THR C C   
12445 O  O   . THR C 427  ? 1.0976 1.4447 1.2393 0.2369  -0.0412 -0.1064 427  THR C O   
12446 C  CB  . THR C 427  ? 0.9438 1.2764 1.0886 0.2261  -0.0421 -0.1028 427  THR C CB  
12447 O  OG1 . THR C 427  ? 1.0059 1.3305 1.1435 0.2307  -0.0460 -0.1020 427  THR C OG1 
12448 C  CG2 . THR C 427  ? 0.9824 1.3180 1.1359 0.2169  -0.0392 -0.1022 427  THR C CG2 
12449 N  N   . PHE C 428  ? 0.9237 1.2705 1.0602 0.2421  -0.0476 -0.1072 428  PHE C N   
12450 C  CA  . PHE C 428  ? 0.9470 1.2923 1.0756 0.2508  -0.0492 -0.1080 428  PHE C CA  
12451 C  C   . PHE C 428  ? 1.0262 1.3908 1.1634 0.2499  -0.0475 -0.1111 428  PHE C C   
12452 O  O   . PHE C 428  ? 1.0468 1.4100 1.1801 0.2545  -0.0464 -0.1112 428  PHE C O   
12453 C  CB  . PHE C 428  ? 0.8288 1.1705 0.9495 0.2577  -0.0539 -0.1083 428  PHE C CB  
12454 C  CG  . PHE C 428  ? 0.8466 1.1656 0.9544 0.2621  -0.0553 -0.1050 428  PHE C CG  
12455 C  CD1 . PHE C 428  ? 0.8521 1.1565 0.9486 0.2689  -0.0551 -0.1034 428  PHE C CD1 
12456 C  CD2 . PHE C 428  ? 0.9480 1.2602 1.0550 0.2595  -0.0565 -0.1035 428  PHE C CD2 
12457 C  CE1 . PHE C 428  ? 0.9139 1.1971 0.9987 0.2726  -0.0561 -0.1004 428  PHE C CE1 
12458 C  CE2 . PHE C 428  ? 0.9208 1.2118 1.0160 0.2635  -0.0574 -0.1003 428  PHE C CE2 
12459 C  CZ  . PHE C 428  ? 0.9255 1.2020 1.0098 0.2698  -0.0571 -0.0988 428  PHE C CZ  
12460 N  N   . GLY C 429  ? 0.8963 1.2790 1.0455 0.2439  -0.0472 -0.1137 429  GLY C N   
12461 C  CA  . GLY C 429  ? 0.9016 1.3034 1.0598 0.2426  -0.0453 -0.1168 429  GLY C CA  
12462 C  C   . GLY C 429  ? 0.8456 1.2488 1.0085 0.2381  -0.0401 -0.1161 429  GLY C C   
12463 O  O   . GLY C 429  ? 0.8964 1.3066 1.0603 0.2410  -0.0384 -0.1173 429  GLY C O   
12464 N  N   . LEU C 430  ? 0.8344 1.2310 1.0001 0.2312  -0.0375 -0.1141 430  LEU C N   
12465 C  CA  . LEU C 430  ? 0.9064 1.3024 1.0750 0.2275  -0.0326 -0.1132 430  LEU C CA  
12466 C  C   . LEU C 430  ? 0.8812 1.2624 1.0384 0.2347  -0.0326 -0.1114 430  LEU C C   
12467 O  O   . LEU C 430  ? 0.8913 1.2762 1.0494 0.2355  -0.0295 -0.1118 430  LEU C O   
12468 C  CB  . LEU C 430  ? 0.7985 1.1893 0.9713 0.2193  -0.0302 -0.1114 430  LEU C CB  
12469 C  CG  . LEU C 430  ? 0.6308 1.0150 0.8029 0.2167  -0.0258 -0.1097 430  LEU C CG  
12470 C  CD1 . LEU C 430  ? 0.7286 1.1298 0.9113 0.2113  -0.0211 -0.1117 430  LEU C CD1 
12471 C  CD2 . LEU C 430  ? 0.6940 1.0660 0.8650 0.2120  -0.0252 -0.1071 430  LEU C CD2 
12472 N  N   . PHE C 431  ? 0.7931 1.1571 0.9392 0.2400  -0.0359 -0.1093 431  PHE C N   
12473 C  CA  . PHE C 431  ? 0.7778 1.1268 0.9123 0.2471  -0.0362 -0.1078 431  PHE C CA  
12474 C  C   . PHE C 431  ? 0.8257 1.1828 0.9578 0.2540  -0.0369 -0.1099 431  PHE C C   
12475 O  O   . PHE C 431  ? 0.8449 1.1993 0.9737 0.2569  -0.0348 -0.1098 431  PHE C O   
12476 C  CB  . PHE C 431  ? 0.8280 1.1580 0.9515 0.2514  -0.0397 -0.1055 431  PHE C CB  
12477 C  CG  . PHE C 431  ? 0.7419 1.0555 0.8528 0.2588  -0.0403 -0.1042 431  PHE C CG  
12478 C  CD1 . PHE C 431  ? 0.7896 1.0939 0.8980 0.2575  -0.0376 -0.1031 431  PHE C CD1 
12479 C  CD2 . PHE C 431  ? 0.7854 1.0925 0.8864 0.2673  -0.0436 -0.1043 431  PHE C CD2 
12480 C  CE1 . PHE C 431  ? 0.8689 1.1579 0.9656 0.2643  -0.0383 -0.1022 431  PHE C CE1 
12481 C  CE2 . PHE C 431  ? 0.8196 1.1110 0.9086 0.2740  -0.0440 -0.1032 431  PHE C CE2 
12482 C  CZ  . PHE C 431  ? 0.8657 1.1480 0.9526 0.2723  -0.0414 -0.1023 431  PHE C CZ  
12483 N  N   . PHE C 432  ? 0.9706 1.3378 1.1043 0.2571  -0.0399 -0.1118 432  PHE C N   
12484 C  CA  . PHE C 432  ? 0.9929 1.3680 1.1239 0.2643  -0.0409 -0.1138 432  PHE C CA  
12485 C  C   . PHE C 432  ? 1.0251 1.4197 1.1676 0.2606  -0.0373 -0.1163 432  PHE C C   
12486 O  O   . PHE C 432  ? 1.0659 1.4644 1.2059 0.2659  -0.0365 -0.1173 432  PHE C O   
12487 C  CB  . PHE C 432  ? 0.9343 1.3138 1.0628 0.2692  -0.0455 -0.1153 432  PHE C CB  
12488 C  CG  . PHE C 432  ? 0.9250 1.2846 1.0388 0.2765  -0.0489 -0.1131 432  PHE C CG  
12489 C  CD1 . PHE C 432  ? 0.8656 1.2128 0.9680 0.2841  -0.0489 -0.1120 432  PHE C CD1 
12490 C  CD2 . PHE C 432  ? 0.9872 1.3400 1.0982 0.2758  -0.0517 -0.1121 432  PHE C CD2 
12491 C  CE1 . PHE C 432  ? 0.8722 1.2004 0.9609 0.2906  -0.0516 -0.1100 432  PHE C CE1 
12492 C  CE2 . PHE C 432  ? 1.0041 1.3380 1.1013 0.2825  -0.0543 -0.1099 432  PHE C CE2 
12493 C  CZ  . PHE C 432  ? 0.9576 1.2791 1.0437 0.2898  -0.0542 -0.1088 432  PHE C CZ  
12494 N  N   . THR C 433  ? 0.9545 1.3612 1.1093 0.2515  -0.0349 -0.1172 433  THR C N   
12495 C  CA  . THR C 433  ? 0.8786 1.3024 1.0443 0.2470  -0.0306 -0.1192 433  THR C CA  
12496 C  C   . THR C 433  ? 0.8868 1.3025 1.0486 0.2476  -0.0266 -0.1175 433  THR C C   
12497 O  O   . THR C 433  ? 0.9974 1.4214 1.1607 0.2503  -0.0242 -0.1188 433  THR C O   
12498 C  CB  . THR C 433  ? 0.8465 1.2821 1.0250 0.2367  -0.0284 -0.1202 433  THR C CB  
12499 O  OG1 . THR C 433  ? 0.8884 1.3337 1.0711 0.2364  -0.0322 -0.1224 433  THR C OG1 
12500 C  CG2 . THR C 433  ? 0.8313 1.2829 1.0206 0.2315  -0.0231 -0.1219 433  THR C CG2 
12501 N  N   . LEU C 434  ? 0.7740 1.1735 0.9306 0.2454  -0.0259 -0.1148 434  LEU C N   
12502 C  CA  . LEU C 434  ? 0.7875 1.1782 0.9395 0.2461  -0.0225 -0.1134 434  LEU C CA  
12503 C  C   . LEU C 434  ? 0.7730 1.1540 0.9132 0.2559  -0.0243 -0.1131 434  LEU C C   
12504 O  O   . LEU C 434  ? 0.8684 1.2498 1.0068 0.2581  -0.0214 -0.1134 434  LEU C O   
12505 C  CB  . LEU C 434  ? 0.7686 1.1441 0.9176 0.2417  -0.0220 -0.1107 434  LEU C CB  
12506 C  CG  . LEU C 434  ? 0.6125 0.9947 0.7709 0.2326  -0.0173 -0.1105 434  LEU C CG  
12507 C  CD1 . LEU C 434  ? 0.5838 0.9841 0.7547 0.2261  -0.0165 -0.1124 434  LEU C CD1 
12508 C  CD2 . LEU C 434  ? 0.6178 0.9840 0.7721 0.2295  -0.0176 -0.1079 434  LEU C CD2 
12509 N  N   . LEU C 435  ? 0.7111 1.0829 0.8428 0.2621  -0.0289 -0.1127 435  LEU C N   
12510 C  CA  . LEU C 435  ? 0.8428 1.2049 0.9627 0.2717  -0.0306 -0.1126 435  LEU C CA  
12511 C  C   . LEU C 435  ? 0.8939 1.2723 1.0173 0.2760  -0.0300 -0.1152 435  LEU C C   
12512 O  O   . LEU C 435  ? 0.9548 1.3302 1.0725 0.2814  -0.0287 -0.1154 435  LEU C O   
12513 C  CB  . LEU C 435  ? 0.8630 1.2110 0.9725 0.2771  -0.0353 -0.1114 435  LEU C CB  
12514 C  CG  . LEU C 435  ? 0.8432 1.1675 0.9411 0.2791  -0.0360 -0.1088 435  LEU C CG  
12515 C  CD1 . LEU C 435  ? 0.7618 1.0736 0.8504 0.2840  -0.0402 -0.1076 435  LEU C CD1 
12516 C  CD2 . LEU C 435  ? 0.7708 1.0871 0.8605 0.2846  -0.0345 -0.1088 435  LEU C CD2 
12517 N  N   . PHE C 436  ? 0.7272 1.1232 0.8603 0.2737  -0.0309 -0.1174 436  PHE C N   
12518 C  CA  . PHE C 436  ? 0.7667 1.1799 0.9045 0.2774  -0.0303 -0.1201 436  PHE C CA  
12519 C  C   . PHE C 436  ? 0.7839 1.2074 0.9294 0.2734  -0.0248 -0.1208 436  PHE C C   
12520 O  O   . PHE C 436  ? 0.7945 1.2245 0.9390 0.2786  -0.0235 -0.1221 436  PHE C O   
12521 C  CB  . PHE C 436  ? 0.7952 1.2250 0.9422 0.2751  -0.0327 -0.1226 436  PHE C CB  
12522 C  CG  . PHE C 436  ? 0.7720 1.1976 0.9103 0.2834  -0.0381 -0.1231 436  PHE C CG  
12523 C  CD1 . PHE C 436  ? 0.8642 1.2987 1.0005 0.2911  -0.0394 -0.1253 436  PHE C CD1 
12524 C  CD2 . PHE C 436  ? 0.6363 1.0489 0.7681 0.2837  -0.0417 -0.1215 436  PHE C CD2 
12525 C  CE1 . PHE C 436  ? 0.8123 1.2426 0.9399 0.2991  -0.0443 -0.1258 436  PHE C CE1 
12526 C  CE2 . PHE C 436  ? 0.6051 1.0131 0.7281 0.2917  -0.0463 -0.1219 436  PHE C CE2 
12527 C  CZ  . PHE C 436  ? 0.6108 1.0276 0.7314 0.2995  -0.0477 -0.1241 436  PHE C CZ  
12528 N  N   . LEU C 437  ? 1.0722 1.4974 1.2253 0.2644  -0.0213 -0.1200 437  LEU C N   
12529 C  CA  . LEU C 437  ? 1.0955 1.5282 1.2545 0.2608  -0.0156 -0.1203 437  LEU C CA  
12530 C  C   . LEU C 437  ? 1.0928 1.5101 1.2403 0.2661  -0.0143 -0.1185 437  LEU C C   
12531 O  O   . LEU C 437  ? 1.1606 1.5840 1.3093 0.2678  -0.0106 -0.1193 437  LEU C O   
12532 C  CB  . LEU C 437  ? 1.0899 1.5265 1.2583 0.2502  -0.0122 -0.1196 437  LEU C CB  
12533 C  CG  . LEU C 437  ? 1.0348 1.4884 1.2161 0.2434  -0.0124 -0.1217 437  LEU C CG  
12534 C  CD1 . LEU C 437  ? 1.0834 1.5394 1.2729 0.2332  -0.0082 -0.1209 437  LEU C CD1 
12535 C  CD2 . LEU C 437  ? 1.0195 1.4932 1.2090 0.2450  -0.0112 -0.1248 437  LEU C CD2 
12536 N  N   . PHE C 438  ? 1.0355 1.4325 1.1719 0.2689  -0.0172 -0.1164 438  PHE C N   
12537 C  CA  . PHE C 438  ? 1.0723 1.4536 1.1973 0.2739  -0.0164 -0.1151 438  PHE C CA  
12538 C  C   . PHE C 438  ? 1.0383 1.4193 1.1555 0.2836  -0.0179 -0.1162 438  PHE C C   
12539 O  O   . PHE C 438  ? 1.0892 1.4694 1.2029 0.2869  -0.0152 -0.1164 438  PHE C O   
12540 C  CB  . PHE C 438  ? 1.1183 1.4783 1.2341 0.2739  -0.0193 -0.1127 438  PHE C CB  
12541 C  CG  . PHE C 438  ? 1.1490 1.4910 1.2504 0.2818  -0.0208 -0.1119 438  PHE C CG  
12542 C  CD1 . PHE C 438  ? 1.1504 1.4864 1.2476 0.2827  -0.0178 -0.1117 438  PHE C CD1 
12543 C  CD2 . PHE C 438  ? 1.1808 1.5113 1.2723 0.2883  -0.0252 -0.1115 438  PHE C CD2 
12544 C  CE1 . PHE C 438  ? 1.0831 1.4022 1.1669 0.2897  -0.0193 -0.1112 438  PHE C CE1 
12545 C  CE2 . PHE C 438  ? 1.1319 1.4451 1.2098 0.2953  -0.0264 -0.1108 438  PHE C CE2 
12546 C  CZ  . PHE C 438  ? 1.1073 1.4149 1.1816 0.2959  -0.0236 -0.1108 438  PHE C CZ  
12547 N  N   . ILE C 439  ? 1.3413 1.7228 1.4553 0.2887  -0.0222 -0.1168 439  ILE C N   
12548 C  CA  . ILE C 439  ? 1.3997 1.7808 1.5057 0.2984  -0.0239 -0.1179 439  ILE C CA  
12549 C  C   . ILE C 439  ? 1.3951 1.7977 1.5104 0.2991  -0.0211 -0.1204 439  ILE C C   
12550 O  O   . ILE C 439  ? 1.5045 1.9080 1.6139 0.3071  -0.0215 -0.1213 439  ILE C O   
12551 C  CB  . ILE C 439  ? 1.3631 1.7384 1.4622 0.3040  -0.0292 -0.1179 439  ILE C CB  
12552 C  CG1 . ILE C 439  ? 1.4343 1.8289 1.5451 0.3007  -0.0306 -0.1199 439  ILE C CG1 
12553 C  CG2 . ILE C 439  ? 1.3295 1.6839 1.4201 0.3029  -0.0315 -0.1154 439  ILE C CG2 
12554 C  CD1 . ILE C 439  ? 1.4078 1.7984 1.5118 0.3067  -0.0358 -0.1202 439  ILE C CD1 
12555 N  N   . ARG C 440  ? 1.1133 1.5330 1.2430 0.2910  -0.0183 -0.1215 440  ARG C N   
12556 C  CA  . ARG C 440  ? 1.1453 1.5859 1.2850 0.2907  -0.0151 -0.1239 440  ARG C CA  
12557 C  C   . ARG C 440  ? 1.1778 1.6195 1.3191 0.2887  -0.0093 -0.1234 440  ARG C C   
12558 O  O   . ARG C 440  ? 1.2770 1.7280 1.4194 0.2929  -0.0069 -0.1248 440  ARG C O   
12559 C  CB  . ARG C 440  ? 1.1807 1.6400 1.3354 0.2829  -0.0147 -0.1257 440  ARG C CB  
12560 C  CG  . ARG C 440  ? 1.1847 1.6667 1.3506 0.2827  -0.0118 -0.1286 440  ARG C CG  
12561 C  CD  . ARG C 440  ? 1.3670 1.8515 1.5263 0.2933  -0.0148 -0.1301 440  ARG C CD  
12562 N  NE  . ARG C 440  ? 1.4288 1.9344 1.5982 0.2937  -0.0117 -0.1327 440  ARG C NE  
12563 C  CZ  . ARG C 440  ? 1.3628 1.8708 1.5317 0.2961  -0.0072 -0.1326 440  ARG C CZ  
12564 N  NH1 . ARG C 440  ? 1.3512 1.8420 1.5094 0.2984  -0.0055 -0.1302 440  ARG C NH1 
12565 N  NH2 . ARG C 440  ? 1.3995 1.9276 1.5785 0.2962  -0.0043 -0.1352 440  ARG C NH2 
12566 N  N   . VAL C 441  ? 0.9227 1.3550 1.0637 0.2826  -0.0069 -0.1215 441  VAL C N   
12567 C  CA  . VAL C 441  ? 0.8477 1.2811 0.9902 0.2801  -0.0011 -0.1211 441  VAL C CA  
12568 C  C   . VAL C 441  ? 0.8665 1.2809 0.9943 0.2868  -0.0015 -0.1196 441  VAL C C   
12569 O  O   . VAL C 441  ? 0.9637 1.3804 1.0885 0.2912  0.0013  -0.1202 441  VAL C O   
12570 C  CB  . VAL C 441  ? 0.7900 1.2251 0.9407 0.2697  0.0021  -0.1201 441  VAL C CB  
12571 C  CG1 . VAL C 441  ? 0.8146 1.2510 0.9664 0.2674  0.0083  -0.1196 441  VAL C CG1 
12572 C  CG2 . VAL C 441  ? 0.7967 1.2503 0.9617 0.2629  0.0024  -0.1218 441  VAL C CG2 
12573 N  N   . LEU C 442  ? 1.2073 1.6026 1.3257 0.2876  -0.0050 -0.1179 442  LEU C N   
12574 C  CA  . LEU C 442  ? 1.1426 1.5186 1.2475 0.2925  -0.0054 -0.1167 442  LEU C CA  
12575 C  C   . LEU C 442  ? 1.2233 1.5879 1.3161 0.3019  -0.0101 -0.1168 442  LEU C C   
12576 O  O   . LEU C 442  ? 1.3733 1.7407 1.4668 0.3037  -0.0138 -0.1172 442  LEU C O   
12577 C  CB  . LEU C 442  ? 1.1325 1.4939 1.2348 0.2871  -0.0059 -0.1148 442  LEU C CB  
12578 C  CG  . LEU C 442  ? 1.2141 1.5845 1.3269 0.2779  -0.0013 -0.1144 442  LEU C CG  
12579 C  CD1 . LEU C 442  ? 1.2549 1.6106 1.3647 0.2732  -0.0024 -0.1126 442  LEU C CD1 
12580 C  CD2 . LEU C 442  ? 1.2105 1.5865 1.3235 0.2789  0.0040  -0.1150 442  LEU C CD2 
12581 N  N   . PRO C 443  ? 1.0058 1.3570 1.0865 0.3082  -0.0100 -0.1165 443  PRO C N   
12582 C  CA  . PRO C 443  ? 1.0559 1.3940 1.1238 0.3171  -0.0142 -0.1164 443  PRO C CA  
12583 C  C   . PRO C 443  ? 1.0603 1.3807 1.1217 0.3159  -0.0182 -0.1149 443  PRO C C   
12584 O  O   . PRO C 443  ? 1.0866 1.3962 1.1467 0.3111  -0.0176 -0.1137 443  PRO C O   
12585 C  CB  . PRO C 443  ? 1.1806 1.5085 1.2380 0.3227  -0.0123 -0.1166 443  PRO C CB  
12586 C  CG  . PRO C 443  ? 1.0555 1.3834 1.1173 0.3160  -0.0084 -0.1161 443  PRO C CG  
12587 C  CD  . PRO C 443  ? 1.0353 1.3828 1.1132 0.3079  -0.0058 -0.1163 443  PRO C CD  
12588 N  N   . MET C 444  ? 1.2592 1.5770 1.3164 0.3205  -0.0221 -0.1149 444  MET C N   
12589 C  CA  . MET C 444  ? 1.2441 1.5463 1.2956 0.3195  -0.0257 -0.1133 444  MET C CA  
12590 C  C   . MET C 444  ? 1.2942 1.5725 1.3298 0.3252  -0.0275 -0.1124 444  MET C C   
12591 O  O   . MET C 444  ? 1.2469 1.5102 1.2775 0.3238  -0.0298 -0.1110 444  MET C O   
12592 C  CB  . MET C 444  ? 1.1832 1.4924 1.2363 0.3221  -0.0291 -0.1138 444  MET C CB  
12593 C  CG  . MET C 444  ? 1.2808 1.5898 1.3252 0.3323  -0.0309 -0.1148 444  MET C CG  
12594 S  SD  . MET C 444  ? 1.5425 1.8628 1.5900 0.3352  -0.0348 -0.1157 444  MET C SD  
12595 C  CE  . MET C 444  ? 1.4348 1.7850 1.5015 0.3289  -0.0318 -0.1180 444  MET C CE  
12596 N  N   . ILE C 445  ? 1.0949 1.3692 1.1227 0.3313  -0.0263 -0.1132 445  ILE C N   
12597 C  CA  . ILE C 445  ? 0.9934 1.2449 1.0061 0.3365  -0.0276 -0.1127 445  ILE C CA  
12598 C  C   . ILE C 445  ? 1.0634 1.3124 1.0748 0.3352  -0.0244 -0.1133 445  ILE C C   
12599 O  O   . ILE C 445  ? 1.1648 1.4280 1.1812 0.3361  -0.0214 -0.1144 445  ILE C O   
12600 C  CB  . ILE C 445  ? 1.0979 1.3440 1.0993 0.3467  -0.0298 -0.1133 445  ILE C CB  
12601 C  CG1 . ILE C 445  ? 1.1140 1.3603 1.1148 0.3484  -0.0332 -0.1126 445  ILE C CG1 
12602 C  CG2 . ILE C 445  ? 1.1405 1.3631 1.1262 0.3516  -0.0307 -0.1130 445  ILE C CG2 
12603 C  CD1 . ILE C 445  ? 1.1208 1.3653 1.1118 0.3585  -0.0352 -0.1133 445  ILE C CD1 
12604 N  N   . ASN C 446  ? 1.2019 1.4330 1.2069 0.3330  -0.0250 -0.1126 446  ASN C N   
12605 C  CA  . ASN C 446  ? 1.2451 1.4719 1.2476 0.3320  -0.0224 -0.1133 446  ASN C CA  
12606 C  C   . ASN C 446  ? 1.3066 1.5286 1.2982 0.3408  -0.0220 -0.1145 446  ASN C C   
12607 O  O   . ASN C 446  ? 1.3541 1.5600 1.3333 0.3469  -0.0246 -0.1145 446  ASN C O   
12608 C  CB  . ASN C 446  ? 1.2569 1.4645 1.2539 0.3284  -0.0238 -0.1127 446  ASN C CB  
12609 C  CG  . ASN C 446  ? 1.2685 1.4754 1.2665 0.3251  -0.0211 -0.1133 446  ASN C CG  
12610 O  OD1 . ASN C 446  ? 1.3580 1.5772 1.3593 0.3260  -0.0178 -0.1141 446  ASN C OD1 
12611 N  ND2 . ASN C 446  ? 1.1781 1.3707 1.1731 0.3213  -0.0223 -0.1131 446  ASN C ND2 
12612 N  N   . ILE C 447  ? 1.0689 1.3043 1.0649 0.3414  -0.0184 -0.1154 447  ILE C N   
12613 C  CA  . ILE C 447  ? 1.1198 1.3549 1.1074 0.3500  -0.0177 -0.1166 447  ILE C CA  
12614 C  C   . ILE C 447  ? 1.1955 1.4110 1.1695 0.3534  -0.0179 -0.1172 447  ILE C C   
12615 O  O   . ILE C 447  ? 1.2140 1.4158 1.1751 0.3607  -0.0200 -0.1176 447  ILE C O   
12616 C  CB  . ILE C 447  ? 1.0442 1.3020 1.0422 0.3494  -0.0136 -0.1174 447  ILE C CB  
12617 C  CG1 . ILE C 447  ? 0.9215 1.1988 0.9340 0.3447  -0.0135 -0.1171 447  ILE C CG1 
12618 C  CG2 . ILE C 447  ? 1.2619 1.5213 1.2521 0.3587  -0.0131 -0.1185 447  ILE C CG2 
12619 C  CD1 . ILE C 447  ? 0.9292 1.2292 0.9543 0.3418  -0.0089 -0.1179 447  ILE C CD1 
12620 N  N   . PHE C 448  ? 1.2504 1.4636 1.2264 0.3483  -0.0158 -0.1173 448  PHE C N   
12621 C  CA  . PHE C 448  ? 1.3830 1.5788 1.3463 0.3516  -0.0160 -0.1184 448  PHE C CA  
12622 C  C   . PHE C 448  ? 1.3678 1.5402 1.3200 0.3529  -0.0202 -0.1183 448  PHE C C   
12623 O  O   . PHE C 448  ? 1.4529 1.6091 1.3918 0.3583  -0.0213 -0.1194 448  PHE C O   
12624 C  CB  . PHE C 448  ? 1.4352 1.6340 1.4031 0.3458  -0.0131 -0.1186 448  PHE C CB  
12625 C  CG  . PHE C 448  ? 1.3834 1.5739 1.3546 0.3385  -0.0148 -0.1179 448  PHE C CG  
12626 C  CD1 . PHE C 448  ? 1.2815 1.4850 1.2662 0.3314  -0.0141 -0.1166 448  PHE C CD1 
12627 C  CD2 . PHE C 448  ? 1.3655 1.5355 1.3264 0.3388  -0.0171 -0.1188 448  PHE C CD2 
12628 C  CE1 . PHE C 448  ? 1.2349 1.4310 1.2227 0.3249  -0.0156 -0.1159 448  PHE C CE1 
12629 C  CE2 . PHE C 448  ? 1.2376 1.4005 1.2020 0.3322  -0.0187 -0.1183 448  PHE C CE2 
12630 C  CZ  . PHE C 448  ? 1.2136 1.3896 1.1913 0.3254  -0.0179 -0.1168 448  PHE C CZ  
12631 N  N   . GLU C 449  ? 1.2264 1.3966 1.1838 0.3481  -0.0223 -0.1171 449  GLU C N   
12632 C  CA  . GLU C 449  ? 1.3769 1.5252 1.3241 0.3494  -0.0259 -0.1169 449  GLU C CA  
12633 C  C   . GLU C 449  ? 1.4833 1.6248 1.4205 0.3576  -0.0278 -0.1168 449  GLU C C   
12634 O  O   . GLU C 449  ? 1.4937 1.6145 1.4180 0.3614  -0.0299 -0.1173 449  GLU C O   
12635 C  CB  . GLU C 449  ? 1.3425 1.4910 1.2981 0.3422  -0.0273 -0.1154 449  GLU C CB  
12636 C  CG  . GLU C 449  ? 1.3879 1.5360 1.3498 0.3346  -0.0264 -0.1156 449  GLU C CG  
12637 C  CD  . GLU C 449  ? 1.4828 1.6172 1.4444 0.3300  -0.0290 -0.1148 449  GLU C CD  
12638 O  OE1 . GLU C 449  ? 1.4239 1.5587 1.3877 0.3298  -0.0305 -0.1133 449  GLU C OE1 
12639 O  OE2 . GLU C 449  ? 1.5646 1.6879 1.5238 0.3267  -0.0295 -0.1156 449  GLU C OE2 
12640 N  N   . MET C 450  ? 1.3166 1.4751 1.2597 0.3605  -0.0270 -0.1164 450  MET C N   
12641 C  CA  . MET C 450  ? 1.3325 1.4857 1.2661 0.3688  -0.0289 -0.1163 450  MET C CA  
12642 C  C   . MET C 450  ? 1.3238 1.4700 1.2456 0.3764  -0.0280 -0.1177 450  MET C C   
12643 O  O   . MET C 450  ? 1.3289 1.4580 1.2370 0.3827  -0.0300 -0.1179 450  MET C O   
12644 C  CB  . MET C 450  ? 1.2492 1.4236 1.1929 0.3696  -0.0286 -0.1158 450  MET C CB  
12645 C  CG  . MET C 450  ? 1.1304 1.3061 1.0803 0.3650  -0.0307 -0.1143 450  MET C CG  
12646 S  SD  . MET C 450  ? 1.3105 1.4635 1.2454 0.3709  -0.0345 -0.1133 450  MET C SD  
12647 C  CE  . MET C 450  ? 1.3980 1.5487 1.3203 0.3826  -0.0345 -0.1144 450  MET C CE  
12648 N  N   . ARG C 451  ? 1.5211 1.6799 1.4477 0.3762  -0.0249 -0.1187 451  ARG C N   
12649 C  CA  . ARG C 451  ? 1.6026 1.7547 1.5179 0.3834  -0.0239 -0.1200 451  ARG C CA  
12650 C  C   . ARG C 451  ? 1.5759 1.7043 1.4788 0.3833  -0.0252 -0.1209 451  ARG C C   
12651 O  O   . ARG C 451  ? 1.5665 1.6814 1.4557 0.3902  -0.0259 -0.1219 451  ARG C O   
12652 C  CB  . ARG C 451  ? 1.5947 1.7663 1.5183 0.3829  -0.0199 -0.1207 451  ARG C CB  
12653 C  CG  . ARG C 451  ? 1.4805 1.6561 1.4120 0.3749  -0.0176 -0.1208 451  ARG C CG  
12654 C  CD  . ARG C 451  ? 1.5273 1.7183 1.4635 0.3758  -0.0132 -0.1215 451  ARG C CD  
12655 N  NE  . ARG C 451  ? 1.5150 1.7294 1.4633 0.3759  -0.0110 -0.1211 451  ARG C NE  
12656 C  CZ  . ARG C 451  ? 1.4862 1.7189 1.4496 0.3689  -0.0083 -0.1206 451  ARG C CZ  
12657 N  NH1 . ARG C 451  ? 1.4578 1.6886 1.4260 0.3614  -0.0071 -0.1202 451  ARG C NH1 
12658 N  NH2 . ARG C 451  ? 1.4741 1.7273 1.4479 0.3694  -0.0066 -0.1206 451  ARG C NH2 
12659 N  N   . LEU C 452  ? 1.3276 1.4504 1.2350 0.3756  -0.0257 -0.1208 452  LEU C N   
12660 C  CA  . LEU C 452  ? 1.3644 1.4640 1.2605 0.3751  -0.0275 -0.1220 452  LEU C CA  
12661 C  C   . LEU C 452  ? 1.3331 1.4131 1.2185 0.3783  -0.0307 -0.1216 452  LEU C C   
12662 O  O   . LEU C 452  ? 1.3640 1.4240 1.2355 0.3822  -0.0320 -0.1229 452  LEU C O   
12663 C  CB  . LEU C 452  ? 1.4044 1.5042 1.3088 0.3661  -0.0273 -0.1220 452  LEU C CB  
12664 C  CG  . LEU C 452  ? 1.3908 1.4670 1.2859 0.3641  -0.0299 -0.1234 452  LEU C CG  
12665 C  CD1 . LEU C 452  ? 1.4181 1.4829 1.3009 0.3687  -0.0296 -0.1257 452  LEU C CD1 
12666 C  CD2 . LEU C 452  ? 1.3497 1.4287 1.2549 0.3552  -0.0300 -0.1231 452  LEU C CD2 
12667 N  N   . PHE C 453  ? 1.3100 1.3952 1.2014 0.3767  -0.0318 -0.1198 453  PHE C N   
12668 C  CA  . PHE C 453  ? 1.3705 1.4379 1.2514 0.3803  -0.0344 -0.1191 453  PHE C CA  
12669 C  C   . PHE C 453  ? 1.4265 1.4889 1.2951 0.3901  -0.0346 -0.1195 453  PHE C C   
12670 O  O   . PHE C 453  ? 1.3719 1.4128 1.2264 0.3942  -0.0362 -0.1198 453  PHE C O   
12671 C  CB  . PHE C 453  ? 1.2148 1.2911 1.1050 0.3770  -0.0353 -0.1170 453  PHE C CB  
12672 C  CG  . PHE C 453  ? 1.2198 1.2770 1.0999 0.3795  -0.0377 -0.1159 453  PHE C CG  
12673 C  CD1 . PHE C 453  ? 1.2669 1.3000 1.1371 0.3780  -0.0389 -0.1166 453  PHE C CD1 
12674 C  CD2 . PHE C 453  ? 1.2965 1.3595 1.1768 0.3832  -0.0386 -0.1144 453  PHE C CD2 
12675 C  CE1 . PHE C 453  ? 1.2458 1.2605 1.1064 0.3801  -0.0405 -0.1155 453  PHE C CE1 
12676 C  CE2 . PHE C 453  ? 1.2841 1.3288 1.1542 0.3857  -0.0405 -0.1132 453  PHE C CE2 
12677 C  CZ  . PHE C 453  ? 1.2442 1.2645 1.1046 0.3840  -0.0412 -0.1136 453  PHE C CZ  
12678 N  N   . LEU C 454  ? 1.5078 1.5897 1.3815 0.3940  -0.0328 -0.1196 454  LEU C N   
12679 C  CA  . LEU C 454  ? 1.4442 1.5229 1.3066 0.4038  -0.0328 -0.1201 454  LEU C CA  
12680 C  C   . LEU C 454  ? 1.4225 1.4850 1.2722 0.4070  -0.0324 -0.1219 454  LEU C C   
12681 O  O   . LEU C 454  ? 1.4607 1.5068 1.2956 0.4139  -0.0336 -0.1223 454  LEU C O   
12682 C  CB  . LEU C 454  ? 1.3816 1.4861 1.2538 0.4066  -0.0307 -0.1200 454  LEU C CB  
12683 C  CG  . LEU C 454  ? 1.3795 1.4847 1.2420 0.4165  -0.0301 -0.1208 454  LEU C CG  
12684 C  CD1 . LEU C 454  ? 1.4256 1.5191 1.2766 0.4237  -0.0326 -0.1200 454  LEU C CD1 
12685 C  CD2 . LEU C 454  ? 1.4554 1.5876 1.3300 0.4174  -0.0274 -0.1211 454  LEU C CD2 
12686 N  N   . TYR C 455  ? 1.5394 1.6060 1.3942 0.4022  -0.0308 -0.1231 455  TYR C N   
12687 C  CA  . TYR C 455  ? 1.6248 1.6759 1.4676 0.4048  -0.0307 -0.1251 455  TYR C CA  
12688 C  C   . TYR C 455  ? 1.6714 1.6954 1.5026 0.4035  -0.0334 -0.1258 455  TYR C C   
12689 O  O   . TYR C 455  ? 1.7064 1.7125 1.5229 0.4085  -0.0342 -0.1272 455  TYR C O   
12690 C  CB  . TYR C 455  ? 1.5317 1.5932 1.3826 0.3996  -0.0284 -0.1261 455  TYR C CB  
12691 C  CG  . TYR C 455  ? 1.6309 1.6757 1.4699 0.4010  -0.0287 -0.1284 455  TYR C CG  
12692 C  CD1 . TYR C 455  ? 1.6533 1.6934 1.4808 0.4091  -0.0279 -0.1295 455  TYR C CD1 
12693 C  CD2 . TYR C 455  ? 1.7279 1.7616 1.5671 0.3945  -0.0300 -0.1296 455  TYR C CD2 
12694 C  CE1 . TYR C 455  ? 1.6661 1.6906 1.4823 0.4104  -0.0284 -0.1318 455  TYR C CE1 
12695 C  CE2 . TYR C 455  ? 1.6901 1.7086 1.5182 0.3958  -0.0306 -0.1321 455  TYR C CE2 
12696 C  CZ  . TYR C 455  ? 1.6564 1.6701 1.4728 0.4036  -0.0299 -0.1332 455  TYR C CZ  
12697 O  OH  . TYR C 455  ? 1.6883 1.6866 1.4933 0.4049  -0.0307 -0.1358 455  TYR C OH  
12698 N  N   . GLN C 456  ? 1.3896 1.4101 1.2273 0.3966  -0.0347 -0.1249 456  GLN C N   
12699 C  CA  . GLN C 456  ? 1.3577 1.3528 1.1856 0.3946  -0.0371 -0.1256 456  GLN C CA  
12700 C  C   . GLN C 456  ? 1.3974 1.3781 1.2128 0.4013  -0.0383 -0.1247 456  GLN C C   
12701 O  O   . GLN C 456  ? 1.4191 1.3765 1.2205 0.4035  -0.0396 -0.1260 456  GLN C O   
12702 C  CB  . GLN C 456  ? 1.3629 1.3594 1.2018 0.3857  -0.0379 -0.1247 456  GLN C CB  
12703 C  CG  . GLN C 456  ? 1.3766 1.3799 1.2243 0.3788  -0.0372 -0.1260 456  GLN C CG  
12704 C  CD  . GLN C 456  ? 1.3421 1.3487 1.2014 0.3704  -0.0379 -0.1249 456  GLN C CD  
12705 O  OE1 . GLN C 456  ? 1.2319 1.2389 1.0942 0.3696  -0.0386 -0.1228 456  GLN C OE1 
12706 N  NE2 . GLN C 456  ? 1.2849 1.2938 1.1503 0.3643  -0.0377 -0.1262 456  GLN C NE2 
12707 N  N   . GLU C 457  ? 1.7069 1.7004 1.5266 0.4046  -0.0381 -0.1226 457  GLU C N   
12708 C  CA  . GLU C 457  ? 1.7587 1.7394 1.5659 0.4117  -0.0392 -0.1215 457  GLU C CA  
12709 C  C   . GLU C 457  ? 1.7281 1.7023 1.5220 0.4205  -0.0387 -0.1228 457  GLU C C   
12710 O  O   . GLU C 457  ? 1.7337 1.6875 1.5125 0.4256  -0.0397 -0.1228 457  GLU C O   
12711 C  CB  . GLU C 457  ? 1.8178 1.8156 1.6332 0.4134  -0.0393 -0.1192 457  GLU C CB  
12712 C  CG  . GLU C 457  ? 1.7291 1.7299 1.5551 0.4056  -0.0401 -0.1177 457  GLU C CG  
12713 C  CD  . GLU C 457  ? 1.8079 1.7880 1.6237 0.4069  -0.0417 -0.1162 457  GLU C CD  
12714 O  OE1 . GLU C 457  ? 1.7763 1.7330 1.5776 0.4096  -0.0421 -0.1171 457  GLU C OE1 
12715 O  OE2 . GLU C 457  ? 1.9859 1.9729 1.8080 0.4052  -0.0423 -0.1143 457  GLU C OE2 
12716 N  N   . THR C 458  ? 1.7038 1.6950 1.5030 0.4224  -0.0369 -0.1238 458  THR C N   
12717 C  CA  . THR C 458  ? 1.7213 1.7065 1.5080 0.4306  -0.0363 -0.1251 458  THR C CA  
12718 C  C   . THR C 458  ? 1.7557 1.7163 1.5296 0.4297  -0.0372 -0.1273 458  THR C C   
12719 O  O   . THR C 458  ? 1.8561 1.7995 1.6143 0.4362  -0.0378 -0.1280 458  THR C O   
12720 C  CB  . THR C 458  ? 1.6364 1.6453 1.4324 0.4319  -0.0338 -0.1256 458  THR C CB  
12721 O  OG1 . THR C 458  ? 1.5667 1.5980 1.3739 0.4332  -0.0331 -0.1240 458  THR C OG1 
12722 C  CG2 . THR C 458  ? 1.6440 1.6465 1.4270 0.4403  -0.0329 -0.1270 458  THR C CG2 
12723 N  N   . GLU C 459  ? 1.8669 1.8252 1.6470 0.4215  -0.0374 -0.1285 459  GLU C N   
12724 C  CA  . GLU C 459  ? 1.9059 1.8410 1.6746 0.4199  -0.0386 -0.1311 459  GLU C CA  
12725 C  C   . GLU C 459  ? 1.9116 1.8219 1.6695 0.4197  -0.0405 -0.1308 459  GLU C C   
12726 O  O   . GLU C 459  ? 1.9238 1.8122 1.6668 0.4224  -0.0414 -0.1326 459  GLU C O   
12727 C  CB  . GLU C 459  ? 1.8938 1.8335 1.6724 0.4112  -0.0387 -0.1325 459  GLU C CB  
12728 C  CG  . GLU C 459  ? 1.9241 1.8840 1.7106 0.4115  -0.0364 -0.1331 459  GLU C CG  
12729 C  CD  . GLU C 459  ? 2.1197 2.0735 1.8934 0.4190  -0.0357 -0.1348 459  GLU C CD  
12730 O  OE1 . GLU C 459  ? 2.0982 2.0296 1.8585 0.4199  -0.0374 -0.1371 459  GLU C OE1 
12731 O  OE2 . GLU C 459  ? 2.2387 2.2098 2.0157 0.4238  -0.0334 -0.1340 459  GLU C OE2 
12732 N  N   . LYS C 460  ? 1.7431 1.6560 1.5080 0.4162  -0.0410 -0.1286 460  LYS C N   
12733 C  CA  . LYS C 460  ? 1.7331 1.6227 1.4878 0.4159  -0.0423 -0.1280 460  LYS C CA  
12734 C  C   . LYS C 460  ? 1.7924 1.6717 1.5322 0.4256  -0.0422 -0.1271 460  LYS C C   
12735 O  O   . LYS C 460  ? 1.8146 1.6689 1.5398 0.4272  -0.0429 -0.1279 460  LYS C O   
12736 C  CB  . LYS C 460  ? 1.7426 1.6389 1.5084 0.4105  -0.0426 -0.1255 460  LYS C CB  
12737 C  CG  . LYS C 460  ? 1.7319 1.6300 1.5091 0.4005  -0.0431 -0.1265 460  LYS C CG  
12738 C  CD  . LYS C 460  ? 1.6590 1.5626 1.4461 0.3957  -0.0433 -0.1239 460  LYS C CD  
12739 C  CE  . LYS C 460  ? 1.6532 1.5599 1.4521 0.3860  -0.0437 -0.1247 460  LYS C CE  
12740 N  NZ  . LYS C 460  ? 1.6965 1.6101 1.5056 0.3814  -0.0438 -0.1221 460  LYS C NZ  
12741 N  N   . ALA C 461  ? 1.4467 1.3448 1.1897 0.4320  -0.0414 -0.1256 461  ALA C N   
12742 C  CA  . ALA C 461  ? 1.4297 1.3197 1.1585 0.4419  -0.0413 -0.1248 461  ALA C CA  
12743 C  C   . ALA C 461  ? 1.3808 1.2583 1.0964 0.4467  -0.0411 -0.1273 461  ALA C C   
12744 O  O   . ALA C 461  ? 1.3442 1.2038 1.0439 0.4532  -0.0414 -0.1273 461  ALA C O   
12745 C  CB  . ALA C 461  ? 1.2894 1.2045 1.0261 0.4474  -0.0406 -0.1230 461  ALA C CB  
12746 N  N   . LYS C 462  ? 1.6509 1.5372 1.3725 0.4436  -0.0404 -0.1294 462  LYS C N   
12747 C  CA  . LYS C 462  ? 1.6660 1.5397 1.3751 0.4476  -0.0403 -0.1319 462  LYS C CA  
12748 C  C   . LYS C 462  ? 1.7277 1.5714 1.4242 0.4443  -0.0418 -0.1338 462  LYS C C   
12749 O  O   . LYS C 462  ? 1.7442 1.5695 1.4244 0.4499  -0.0421 -0.1350 462  LYS C O   
12750 C  CB  . LYS C 462  ? 1.6378 1.5279 1.3565 0.4445  -0.0392 -0.1336 462  LYS C CB  
12751 C  CG  . LYS C 462  ? 1.6913 1.6033 1.4138 0.4513  -0.0372 -0.1329 462  LYS C CG  
12752 C  CD  . LYS C 462  ? 1.7406 1.6596 1.4653 0.4501  -0.0360 -0.1350 462  LYS C CD  
12753 C  CE  . LYS C 462  ? 1.5963 1.5453 1.3361 0.4502  -0.0334 -0.1338 462  LYS C CE  
12754 N  NZ  . LYS C 462  ? 1.6381 1.5935 1.3797 0.4490  -0.0318 -0.1356 462  LYS C NZ  
12755 N  N   . GLN C 463  ? 1.7277 1.5658 1.4313 0.4352  -0.0428 -0.1342 463  GLN C N   
12756 C  CA  . GLN C 463  ? 1.6849 1.4951 1.3781 0.4310  -0.0442 -0.1362 463  GLN C CA  
12757 C  C   . GLN C 463  ? 1.6536 1.4466 1.3377 0.4330  -0.0442 -0.1341 463  GLN C C   
12758 O  O   . GLN C 463  ? 1.6896 1.4581 1.3646 0.4294  -0.0450 -0.1355 463  GLN C O   
12759 C  CB  . GLN C 463  ? 1.7366 1.5482 1.4416 0.4204  -0.0451 -0.1376 463  GLN C CB  
12760 C  CG  . GLN C 463  ? 1.8842 1.6920 1.5876 0.4174  -0.0460 -0.1415 463  GLN C CG  
12761 C  CD  . GLN C 463  ? 1.9861 1.8034 1.7041 0.4080  -0.0468 -0.1425 463  GLN C CD  
12762 O  OE1 . GLN C 463  ? 2.0167 1.8327 1.7422 0.4021  -0.0472 -0.1413 463  GLN C OE1 
12763 N  NE2 . GLN C 463  ? 1.9369 1.7636 1.6587 0.4067  -0.0469 -0.1448 463  GLN C NE2 
12764 N  N   . ARG C 464  ? 1.7328 1.5380 1.4189 0.4385  -0.0435 -0.1309 464  ARG C N   
12765 C  CA  . ARG C 464  ? 1.8107 1.6012 1.4878 0.4414  -0.0434 -0.1285 464  ARG C CA  
12766 C  C   . ARG C 464  ? 1.8947 1.6722 1.5755 0.4325  -0.0438 -0.1281 464  ARG C C   
12767 O  O   . ARG C 464  ? 1.8585 1.6374 1.5419 0.4323  -0.0435 -0.1252 464  ARG C O   
12768 C  CB  . ARG C 464  ? 1.7455 1.5126 1.4020 0.4485  -0.0432 -0.1294 464  ARG C CB  
12769 C  CG  . ARG C 464  ? 1.7631 1.5413 1.4143 0.4582  -0.0427 -0.1296 464  ARG C CG  
12770 C  CD  . ARG C 464  ? 1.7944 1.5507 1.4287 0.4616  -0.0429 -0.1323 464  ARG C CD  
12771 N  NE  . ARG C 464  ? 1.9099 1.6639 1.5482 0.4549  -0.0436 -0.1358 464  ARG C NE  
12772 C  CZ  . ARG C 464  ? 1.9386 1.6682 1.5683 0.4499  -0.0445 -0.1385 464  ARG C CZ  
12773 N  NH1 . ARG C 464  ? 1.9044 1.6090 1.5209 0.4503  -0.0444 -0.1381 464  ARG C NH1 
12774 N  NH2 . ARG C 464  ? 1.8970 1.6272 1.5310 0.4442  -0.0454 -0.1418 464  ARG C NH2 
12775 N  N   . VAL D 5    ? 1.5314 1.7812 1.4032 0.3884  0.1010  -0.1163 5    VAL D N   
12776 C  CA  . VAL D 5    ? 1.4612 1.6921 1.3163 0.3897  0.0987  -0.1164 5    VAL D CA  
12777 C  C   . VAL D 5    ? 1.6237 1.8431 1.4775 0.3865  0.0897  -0.1176 5    VAL D C   
12778 O  O   . VAL D 5    ? 1.6311 1.8326 1.4702 0.3887  0.0849  -0.1187 5    VAL D O   
12779 C  CB  . VAL D 5    ? 1.5581 1.7933 1.4134 0.3854  0.1075  -0.1139 5    VAL D CB  
12780 C  CG1 . VAL D 5    ? 1.6099 1.8254 1.4450 0.3892  0.1058  -0.1141 5    VAL D CG1 
12781 C  CG2 . VAL D 5    ? 1.4803 1.7316 1.3428 0.3864  0.1174  -0.1126 5    VAL D CG2 
12782 N  N   . TYR D 6    ? 1.5506 1.7804 1.4198 0.3812  0.0872  -0.1176 6    TYR D N   
12783 C  CA  . TYR D 6    ? 1.5535 1.7731 1.4226 0.3779  0.0789  -0.1188 6    TYR D CA  
12784 C  C   . TYR D 6    ? 1.6308 1.8349 1.4884 0.3843  0.0704  -0.1214 6    TYR D C   
12785 O  O   . TYR D 6    ? 1.6888 1.8766 1.5371 0.3842  0.0638  -0.1229 6    TYR D O   
12786 C  CB  . TYR D 6    ? 1.5648 1.7999 1.4534 0.3706  0.0789  -0.1180 6    TYR D CB  
12787 C  CG  . TYR D 6    ? 1.6237 1.8494 1.5134 0.3672  0.0705  -0.1191 6    TYR D CG  
12788 C  CD1 . TYR D 6    ? 1.6414 1.8552 1.5246 0.3641  0.0680  -0.1191 6    TYR D CD1 
12789 C  CD2 . TYR D 6    ? 1.5776 1.8064 1.4750 0.3671  0.0652  -0.1200 6    TYR D CD2 
12790 C  CE1 . TYR D 6    ? 1.6266 1.8322 1.5114 0.3608  0.0606  -0.1202 6    TYR D CE1 
12791 C  CE2 . TYR D 6    ? 1.5877 1.8077 1.4862 0.3639  0.0580  -0.1209 6    TYR D CE2 
12792 C  CZ  . TYR D 6    ? 1.6403 1.8490 1.5329 0.3606  0.0557  -0.1211 6    TYR D CZ  
12793 O  OH  . TYR D 6    ? 1.6351 1.8353 1.5293 0.3573  0.0487  -0.1221 6    TYR D OH  
12794 N  N   . GLY D 7    ? 1.1665 1.3749 1.0243 0.3900  0.0704  -0.1221 7    GLY D N   
12795 C  CA  . GLY D 7    ? 1.0967 1.2899 0.9429 0.3963  0.0629  -0.1245 7    GLY D CA  
12796 C  C   . GLY D 7    ? 1.0992 1.3007 0.9480 0.4021  0.0641  -0.1248 7    GLY D C   
12797 O  O   . GLY D 7    ? 1.1408 1.3580 0.9971 0.4027  0.0712  -0.1234 7    GLY D O   
12798 N  N   . VAL D 8    ? 1.0061 1.1963 0.8483 0.4064  0.0570  -0.1267 8    VAL D N   
12799 C  CA  . VAL D 8    ? 0.9921 1.1873 0.8346 0.4129  0.0569  -0.1271 8    VAL D CA  
12800 C  C   . VAL D 8    ? 0.9349 1.1295 0.7840 0.4112  0.0506  -0.1278 8    VAL D C   
12801 O  O   . VAL D 8    ? 0.8647 1.0481 0.7121 0.4073  0.0450  -0.1286 8    VAL D O   
12802 C  CB  . VAL D 8    ? 1.0526 1.2317 0.8759 0.4220  0.0551  -0.1288 8    VAL D CB  
12803 C  CG1 . VAL D 8    ? 1.0836 1.2711 0.9081 0.4289  0.0569  -0.1288 8    VAL D CG1 
12804 C  CG2 . VAL D 8    ? 1.0343 1.2091 0.8482 0.4230  0.0598  -0.1283 8    VAL D CG2 
12805 N  N   . MET D 9    ? 1.5051 1.7116 1.3616 0.4144  0.0515  -0.1276 9    MET D N   
12806 C  CA  . MET D 9    ? 1.4306 1.6385 1.2941 0.4130  0.0463  -0.1279 9    MET D CA  
12807 C  C   . MET D 9    ? 1.4542 1.6531 1.3073 0.4219  0.0425  -0.1292 9    MET D C   
12808 O  O   . MET D 9    ? 1.5584 1.7563 1.4030 0.4289  0.0452  -0.1296 9    MET D O   
12809 C  CB  . MET D 9    ? 1.5347 1.7665 1.4183 0.4080  0.0502  -0.1264 9    MET D CB  
12810 C  CG  . MET D 9    ? 1.5709 1.8086 1.4657 0.3982  0.0513  -0.1252 9    MET D CG  
12811 S  SD  . MET D 9    ? 1.6280 1.8534 1.5236 0.3937  0.0427  -0.1259 9    MET D SD  
12812 C  CE  . MET D 9    ? 1.5059 1.7494 1.4212 0.3828  0.0463  -0.1240 9    MET D CE  
12813 N  N   . ALA D 10   ? 1.8761 2.0682 1.7296 0.4215  0.0364  -0.1299 10   ALA D N   
12814 C  CA  . ALA D 10   ? 1.9120 2.0917 1.7539 0.4294  0.0320  -0.1312 10   ALA D CA  
12815 C  C   . ALA D 10   ? 1.9938 2.1853 1.8451 0.4311  0.0308  -0.1306 10   ALA D C   
12816 O  O   . ALA D 10   ? 2.1009 2.2931 1.9467 0.4389  0.0310  -0.1310 10   ALA D O   
12817 C  CB  . ALA D 10   ? 1.8219 1.9773 1.6511 0.4289  0.0251  -0.1328 10   ALA D CB  
12818 N  N   . GLU D 11   ? 1.7885 1.9887 1.6533 0.4242  0.0293  -0.1297 11   GLU D N   
12819 C  CA  . GLU D 11   ? 1.7798 1.9929 1.6547 0.4251  0.0282  -0.1291 11   GLU D CA  
12820 C  C   . GLU D 11   ? 1.7802 1.9779 1.6426 0.4325  0.0227  -0.1301 11   GLU D C   
12821 O  O   . GLU D 11   ? 1.8222 2.0267 1.6838 0.4392  0.0234  -0.1302 11   GLU D O   
12822 C  CB  . GLU D 11   ? 1.7872 2.0234 1.6728 0.4271  0.0343  -0.1284 11   GLU D CB  
12823 C  CG  . GLU D 11   ? 1.7697 2.0264 1.6737 0.4223  0.0351  -0.1276 11   GLU D CG  
12824 C  CD  . GLU D 11   ? 1.8692 2.1257 1.7720 0.4276  0.0306  -0.1280 11   GLU D CD  
12825 O  OE1 . GLU D 11   ? 1.9196 2.1832 1.8204 0.4350  0.0322  -0.1284 11   GLU D OE1 
12826 O  OE2 . GLU D 11   ? 1.8359 2.0850 1.7394 0.4246  0.0256  -0.1279 11   GLU D OE2 
12827 N  N   . PHE D 12   ? 1.4039 1.5806 1.2563 0.4312  0.0175  -0.1310 12   PHE D N   
12828 C  CA  . PHE D 12   ? 1.4524 1.6123 1.2919 0.4377  0.0125  -0.1319 12   PHE D CA  
12829 C  C   . PHE D 12   ? 1.4333 1.6009 1.2813 0.4371  0.0100  -0.1311 12   PHE D C   
12830 O  O   . PHE D 12   ? 1.4577 1.6340 1.3185 0.4295  0.0096  -0.1301 12   PHE D O   
12831 C  CB  . PHE D 12   ? 1.3750 1.5098 1.2015 0.4360  0.0079  -0.1334 12   PHE D CB  
12832 C  CG  . PHE D 12   ? 1.4331 1.5536 1.2438 0.4413  0.0084  -0.1349 12   PHE D CG  
12833 C  CD1 . PHE D 12   ? 1.4580 1.5804 1.2686 0.4382  0.0115  -0.1352 12   PHE D CD1 
12834 C  CD2 . PHE D 12   ? 1.5205 1.6249 1.3155 0.4493  0.0057  -0.1362 12   PHE D CD2 
12835 C  CE1 . PHE D 12   ? 1.6056 1.7145 1.4009 0.4433  0.0118  -0.1367 12   PHE D CE1 
12836 C  CE2 . PHE D 12   ? 1.6370 1.7277 1.4171 0.4542  0.0059  -0.1377 12   PHE D CE2 
12837 C  CZ  . PHE D 12   ? 1.7025 1.7956 1.4827 0.4512  0.0089  -0.1380 12   PHE D CZ  
12838 N  N   . PRO D 13   ? 1.6813 1.8460 1.5224 0.4451  0.0083  -0.1313 13   PRO D N   
12839 C  CA  . PRO D 13   ? 1.7307 1.9065 1.5810 0.4452  0.0067  -0.1304 13   PRO D CA  
12840 C  C   . PRO D 13   ? 1.6323 1.7937 1.4802 0.4415  0.0014  -0.1302 13   PRO D C   
12841 O  O   . PRO D 13   ? 1.5410 1.7134 1.4017 0.4359  0.0007  -0.1292 13   PRO D O   
12842 C  CB  . PRO D 13   ? 1.7782 1.9546 1.6200 0.4559  0.0068  -0.1307 13   PRO D CB  
12843 C  CG  . PRO D 13   ? 1.8257 1.9821 1.6497 0.4612  0.0063  -0.1320 13   PRO D CG  
12844 C  CD  . PRO D 13   ? 1.7587 1.9144 1.5851 0.4548  0.0089  -0.1323 13   PRO D CD  
12845 N  N   . THR D 14   ? 1.5146 1.6513 1.3466 0.4442  -0.0022 -0.1312 14   THR D N   
12846 C  CA  . THR D 14   ? 1.4708 1.5917 1.2990 0.4415  -0.0070 -0.1311 14   THR D CA  
12847 C  C   . THR D 14   ? 1.5393 1.6468 1.3658 0.4341  -0.0085 -0.1319 14   THR D C   
12848 O  O   . THR D 14   ? 1.5720 1.6741 1.3930 0.4339  -0.0070 -0.1330 14   THR D O   
12849 C  CB  . THR D 14   ? 1.5602 1.6620 1.3713 0.4501  -0.0101 -0.1318 14   THR D CB  
12850 O  OG1 . THR D 14   ? 1.5494 1.6315 1.3544 0.4470  -0.0143 -0.1320 14   THR D OG1 
12851 C  CG2 . THR D 14   ? 1.6032 1.6933 1.4001 0.4559  -0.0089 -0.1333 14   THR D CG2 
12852 N  N   . PRO D 15   ? 1.6674 1.7695 1.4987 0.4280  -0.0114 -0.1313 15   PRO D N   
12853 C  CA  . PRO D 15   ? 1.6784 1.7687 1.5090 0.4208  -0.0129 -0.1322 15   PRO D CA  
12854 C  C   . PRO D 15   ? 1.7317 1.7973 1.5448 0.4241  -0.0154 -0.1344 15   PRO D C   
12855 O  O   . PRO D 15   ? 1.6948 1.7544 1.5057 0.4205  -0.0152 -0.1357 15   PRO D O   
12856 C  CB  . PRO D 15   ? 1.5207 1.6091 1.3585 0.4152  -0.0159 -0.1311 15   PRO D CB  
12857 C  CG  . PRO D 15   ? 1.5925 1.6834 1.4284 0.4212  -0.0169 -0.1301 15   PRO D CG  
12858 C  CD  . PRO D 15   ? 1.6405 1.7482 1.4786 0.4272  -0.0134 -0.1299 15   PRO D CD  
12859 N  N   . GLU D 16   ? 1.6105 1.6613 1.4106 0.4310  -0.0176 -0.1349 16   GLU D N   
12860 C  CA  . GLU D 16   ? 1.5184 1.5449 1.3012 0.4341  -0.0200 -0.1373 16   GLU D CA  
12861 C  C   . GLU D 16   ? 1.5589 1.5876 1.3358 0.4378  -0.0173 -0.1385 16   GLU D C   
12862 O  O   . GLU D 16   ? 1.6578 1.6709 1.4250 0.4368  -0.0188 -0.1407 16   GLU D O   
12863 C  CB  . GLU D 16   ? 1.5543 1.5656 1.3244 0.4411  -0.0224 -0.1373 16   GLU D CB  
12864 C  CG  . GLU D 16   ? 1.6172 1.6184 1.3885 0.4375  -0.0255 -0.1366 16   GLU D CG  
12865 C  CD  . GLU D 16   ? 1.6194 1.6403 1.4047 0.4362  -0.0246 -0.1340 16   GLU D CD  
12866 O  OE1 . GLU D 16   ? 1.5947 1.6346 1.3858 0.4403  -0.0218 -0.1330 16   GLU D OE1 
12867 O  OE2 . GLU D 16   ? 1.5973 1.6147 1.3878 0.4310  -0.0266 -0.1331 16   GLU D OE2 
12868 N  N   . ALA D 17   ? 1.3020 1.3499 1.0845 0.4419  -0.0134 -0.1373 17   ALA D N   
12869 C  CA  . ALA D 17   ? 1.3646 1.4158 1.1421 0.4454  -0.0103 -0.1382 17   ALA D CA  
12870 C  C   . ALA D 17   ? 1.3870 1.4429 1.1712 0.4381  -0.0088 -0.1386 17   ALA D C   
12871 O  O   . ALA D 17   ? 1.3816 1.4288 1.1565 0.4394  -0.0083 -0.1403 17   ALA D O   
12872 C  CB  . ALA D 17   ? 1.3286 1.4010 1.1126 0.4509  -0.0060 -0.1367 17   ALA D CB  
12873 N  N   . LEU D 18   ? 1.6074 1.6769 1.4072 0.4304  -0.0080 -0.1372 18   LEU D N   
12874 C  CA  . LEU D 18   ? 1.5650 1.6383 1.3710 0.4232  -0.0068 -0.1374 18   LEU D CA  
12875 C  C   . LEU D 18   ? 1.5329 1.5833 1.3281 0.4206  -0.0111 -0.1398 18   LEU D C   
12876 O  O   . LEU D 18   ? 1.4845 1.5306 1.2754 0.4191  -0.0105 -0.1412 18   LEU D O   
12877 C  CB  . LEU D 18   ? 1.4654 1.5562 1.2897 0.4156  -0.0056 -0.1354 18   LEU D CB  
12878 C  CG  . LEU D 18   ? 1.3503 1.4520 1.1838 0.4089  -0.0024 -0.1349 18   LEU D CG  
12879 C  CD1 . LEU D 18   ? 1.3866 1.5009 1.2201 0.4129  0.0029  -0.1345 18   LEU D CD1 
12880 C  CD2 . LEU D 18   ? 1.3373 1.4548 1.1883 0.4014  -0.0016 -0.1330 18   LEU D CD2 
12881 N  N   . ILE D 19   ? 1.7860 1.8212 1.5767 0.4200  -0.0155 -0.1405 19   ILE D N   
12882 C  CA  . ILE D 19   ? 1.8091 1.8215 1.5894 0.4174  -0.0199 -0.1432 19   ILE D CA  
12883 C  C   . ILE D 19   ? 1.8545 1.8525 1.6182 0.4236  -0.0204 -0.1456 19   ILE D C   
12884 O  O   . ILE D 19   ? 1.9099 1.8987 1.6679 0.4212  -0.0217 -0.1478 19   ILE D O   
12885 C  CB  . ILE D 19   ? 1.8390 1.8374 1.6168 0.4165  -0.0239 -0.1433 19   ILE D CB  
12886 C  CG1 . ILE D 19   ? 1.7633 1.7775 1.5571 0.4117  -0.0231 -0.1405 19   ILE D CG1 
12887 C  CG2 . ILE D 19   ? 1.9092 1.8862 1.6795 0.4121  -0.0282 -0.1461 19   ILE D CG2 
12888 C  CD1 . ILE D 19   ? 1.7389 1.7414 1.5299 0.4122  -0.0261 -0.1400 19   ILE D CD1 
12889 N  N   . GLU D 20   ? 2.2893 2.2851 2.0445 0.4317  -0.0195 -0.1453 20   GLU D N   
12890 C  CA  . GLU D 20   ? 2.3156 2.2969 2.0541 0.4380  -0.0201 -0.1476 20   GLU D CA  
12891 C  C   . GLU D 20   ? 2.2843 2.2763 2.0237 0.4386  -0.0165 -0.1477 20   GLU D C   
12892 O  O   . GLU D 20   ? 2.3264 2.3051 2.0544 0.4395  -0.0179 -0.1502 20   GLU D O   
12893 C  CB  . GLU D 20   ? 2.3914 2.3704 2.1219 0.4469  -0.0195 -0.1469 20   GLU D CB  
12894 C  CG  . GLU D 20   ? 2.4332 2.3997 2.1604 0.4474  -0.0228 -0.1466 20   GLU D CG  
12895 C  CD  . GLU D 20   ? 2.5941 2.5327 2.3067 0.4466  -0.0273 -0.1497 20   GLU D CD  
12896 O  OE1 . GLU D 20   ? 2.6118 2.5403 2.3154 0.4468  -0.0282 -0.1522 20   GLU D OE1 
12897 O  OE2 . GLU D 20   ? 2.6194 2.5461 2.3296 0.4457  -0.0300 -0.1496 20   GLU D OE2 
12898 N  N   . ALA D 21   ? 1.4899 1.5056 1.2426 0.4379  -0.0117 -0.1451 21   ALA D N   
12899 C  CA  . ALA D 21   ? 1.4814 1.5079 1.2353 0.4385  -0.0074 -0.1448 21   ALA D CA  
12900 C  C   . ALA D 21   ? 1.4982 1.5207 1.2537 0.4314  -0.0086 -0.1460 21   ALA D C   
12901 O  O   . ALA D 21   ? 1.4878 1.5047 1.2346 0.4331  -0.0078 -0.1475 21   ALA D O   
12902 C  CB  . ALA D 21   ? 1.4018 1.4546 1.1709 0.4383  -0.0019 -0.1418 21   ALA D CB  
12903 N  N   . THR D 22   ? 1.4646 1.4901 1.2312 0.4238  -0.0104 -0.1454 22   THR D N   
12904 C  CA  . THR D 22   ? 1.3790 1.3997 1.1470 0.4172  -0.0121 -0.1468 22   THR D CA  
12905 C  C   . THR D 22   ? 1.4369 1.4329 1.1886 0.4186  -0.0172 -0.1505 22   THR D C   
12906 O  O   . THR D 22   ? 1.4917 1.4825 1.2384 0.4168  -0.0179 -0.1523 22   THR D O   
12907 C  CB  . THR D 22   ? 1.3318 1.3587 1.1140 0.4092  -0.0135 -0.1455 22   THR D CB  
12908 O  OG1 . THR D 22   ? 1.2790 1.3286 1.0760 0.4080  -0.0090 -0.1423 22   THR D OG1 
12909 C  CG2 . THR D 22   ? 1.3345 1.3592 1.1194 0.4026  -0.0147 -0.1466 22   THR D CG2 
12910 N  N   . ARG D 23   ? 1.6168 1.5972 1.3598 0.4218  -0.0208 -0.1519 23   ARG D N   
12911 C  CA  . ARG D 23   ? 1.6217 1.5779 1.3489 0.4230  -0.0256 -0.1558 23   ARG D CA  
12912 C  C   . ARG D 23   ? 1.6033 1.5540 1.3165 0.4303  -0.0243 -0.1571 23   ARG D C   
12913 O  O   . ARG D 23   ? 1.6060 1.5407 1.3073 0.4304  -0.0276 -0.1605 23   ARG D O   
12914 C  CB  . ARG D 23   ? 1.6758 1.6166 1.3979 0.4240  -0.0294 -0.1567 23   ARG D CB  
12915 C  CG  . ARG D 23   ? 1.6967 1.6384 1.4305 0.4164  -0.0315 -0.1559 23   ARG D CG  
12916 C  CD  . ARG D 23   ? 1.7327 1.6574 1.4601 0.4175  -0.0349 -0.1567 23   ARG D CD  
12917 N  NE  . ARG D 23   ? 1.7199 1.6470 1.4590 0.4106  -0.0363 -0.1556 23   ARG D NE  
12918 C  CZ  . ARG D 23   ? 1.8243 1.7408 1.5648 0.4039  -0.0399 -0.1578 23   ARG D CZ  
12919 N  NH1 . ARG D 23   ? 1.9226 1.8251 1.6537 0.4027  -0.0428 -0.1616 23   ARG D NH1 
12920 N  NH2 . ARG D 23   ? 1.8340 1.7540 1.5857 0.3981  -0.0407 -0.1563 23   ARG D NH2 
12921 N  N   . LYS D 24   ? 1.6531 1.6169 1.3674 0.4364  -0.0196 -0.1547 24   LYS D N   
12922 C  CA  . LYS D 24   ? 1.6193 1.5803 1.3214 0.4432  -0.0175 -0.1556 24   LYS D CA  
12923 C  C   . LYS D 24   ? 1.6740 1.6416 1.3778 0.4402  -0.0155 -0.1558 24   LYS D C   
12924 O  O   . LYS D 24   ? 1.7804 1.7355 1.4710 0.4426  -0.0171 -0.1583 24   LYS D O   
12925 C  CB  . LYS D 24   ? 1.5941 1.5693 1.2986 0.4500  -0.0127 -0.1529 24   LYS D CB  
12926 C  CG  . LYS D 24   ? 1.6468 1.6126 1.3452 0.4551  -0.0148 -0.1530 24   LYS D CG  
12927 C  CD  . LYS D 24   ? 1.5707 1.5511 1.2711 0.4624  -0.0102 -0.1506 24   LYS D CD  
12928 C  CE  . LYS D 24   ? 1.5807 1.5552 1.2781 0.4667  -0.0122 -0.1500 24   LYS D CE  
12929 N  NZ  . LYS D 24   ? 1.7163 1.6638 1.3962 0.4695  -0.0170 -0.1530 24   LYS D NZ  
12930 N  N   . ALA D 25   ? 1.5389 1.5256 1.2583 0.4349  -0.0119 -0.1532 25   ALA D N   
12931 C  CA  . ALA D 25   ? 1.4429 1.4341 1.1647 0.4306  -0.0106 -0.1534 25   ALA D CA  
12932 C  C   . ALA D 25   ? 1.5410 1.5164 1.2595 0.4249  -0.0168 -0.1565 25   ALA D C   
12933 O  O   . ALA D 25   ? 1.5745 1.5353 1.2888 0.4242  -0.0217 -0.1585 25   ALA D O   
12934 C  CB  . ALA D 25   ? 1.4605 1.4755 1.2001 0.4261  -0.0052 -0.1498 25   ALA D CB  
12935 N  N   . LYS D 26   ? 1.8967 1.8748 1.6170 0.4207  -0.0165 -0.1569 26   LYS D N   
12936 C  CA  . LYS D 26   ? 1.9486 1.9122 1.6648 0.4157  -0.0225 -0.1603 26   LYS D CA  
12937 C  C   . LYS D 26   ? 2.0319 1.9735 1.7296 0.4201  -0.0273 -0.1645 26   LYS D C   
12938 O  O   . LYS D 26   ? 2.0928 2.0260 1.7821 0.4195  -0.0298 -0.1672 26   LYS D O   
12939 C  CB  . LYS D 26   ? 1.8811 1.8432 1.6079 0.4094  -0.0258 -0.1604 26   LYS D CB  
12940 C  CG  . LYS D 26   ? 1.8853 1.8341 1.6101 0.4036  -0.0318 -0.1639 26   LYS D CG  
12941 C  CD  . LYS D 26   ? 1.8679 1.8195 1.6060 0.3971  -0.0337 -0.1630 26   LYS D CD  
12942 C  CE  . LYS D 26   ? 1.8175 1.7557 1.5541 0.3913  -0.0397 -0.1668 26   LYS D CE  
12943 N  NZ  . LYS D 26   ? 1.7573 1.6998 1.4932 0.3892  -0.0395 -0.1676 26   LYS D NZ  
12944 N  N   . ALA D 27   ? 1.7341 1.6659 1.4248 0.4247  -0.0287 -0.1653 27   ALA D N   
12945 C  CA  . ALA D 27   ? 1.6702 1.5828 1.3426 0.4301  -0.0320 -0.1688 27   ALA D CA  
12946 C  C   . ALA D 27   ? 1.6341 1.5519 1.2984 0.4360  -0.0280 -0.1680 27   ALA D C   
12947 O  O   . ALA D 27   ? 1.5400 1.4448 1.1910 0.4379  -0.0309 -0.1712 27   ALA D O   
12948 C  CB  . ALA D 27   ? 1.6451 1.5483 1.3119 0.4346  -0.0330 -0.1689 27   ALA D CB  
12949 N  N   . ALA D 28   ? 1.4183 1.3552 1.0906 0.4387  -0.0213 -0.1639 28   ALA D N   
12950 C  CA  . ALA D 28   ? 1.3735 1.3173 1.0400 0.4435  -0.0166 -0.1628 28   ALA D CA  
12951 C  C   . ALA D 28   ? 1.3958 1.3423 1.0636 0.4389  -0.0166 -0.1632 28   ALA D C   
12952 O  O   . ALA D 28   ? 1.3367 1.2804 0.9941 0.4426  -0.0152 -0.1638 28   ALA D O   
12953 C  CB  . ALA D 28   ? 1.3445 1.3095 1.0216 0.4463  -0.0092 -0.1584 28   ALA D CB  
12954 N  N   . GLY D 29   ? 1.7632 1.7149 1.4430 0.4312  -0.0182 -0.1629 29   GLY D N   
12955 C  CA  . GLY D 29   ? 1.7536 1.7087 1.4355 0.4267  -0.0181 -0.1630 29   GLY D CA  
12956 C  C   . GLY D 29   ? 1.7614 1.7384 1.4590 0.4229  -0.0115 -0.1587 29   GLY D C   
12957 O  O   . GLY D 29   ? 1.7776 1.7583 1.4779 0.4189  -0.0111 -0.1584 29   GLY D O   
12958 N  N   . TYR D 30   ? 1.7082 1.7001 1.4161 0.4242  -0.0065 -0.1554 30   TYR D N   
12959 C  CA  . TYR D 30   ? 1.6742 1.6873 1.3982 0.4199  -0.0004 -0.1515 30   TYR D CA  
12960 C  C   . TYR D 30   ? 1.7318 1.7470 1.4676 0.4117  -0.0035 -0.1515 30   TYR D C   
12961 O  O   . TYR D 30   ? 1.7457 1.7543 1.4846 0.4096  -0.0081 -0.1528 30   TYR D O   
12962 C  CB  . TYR D 30   ? 1.6454 1.6731 1.3782 0.4228  0.0046  -0.1486 30   TYR D CB  
12963 C  CG  . TYR D 30   ? 1.6214 1.6544 1.3473 0.4299  0.0102  -0.1473 30   TYR D CG  
12964 C  CD1 . TYR D 30   ? 1.6602 1.7082 1.3916 0.4291  0.0174  -0.1446 30   TYR D CD1 
12965 C  CD2 . TYR D 30   ? 1.6738 1.6966 1.3876 0.4374  0.0086  -0.1488 30   TYR D CD2 
12966 C  CE1 . TYR D 30   ? 1.6721 1.7250 1.3975 0.4355  0.0228  -0.1434 30   TYR D CE1 
12967 C  CE2 . TYR D 30   ? 1.6766 1.7044 1.3843 0.4441  0.0138  -0.1477 30   TYR D CE2 
12968 C  CZ  . TYR D 30   ? 1.6514 1.6945 1.3652 0.4430  0.0210  -0.1450 30   TYR D CZ  
12969 O  OH  . TYR D 30   ? 1.7285 1.7765 1.4364 0.4496  0.0265  -0.1438 30   TYR D OH  
12970 N  N   . THR D 31   ? 2.0871 2.1110 1.8291 0.4070  -0.0008 -0.1500 31   THR D N   
12971 C  CA  . THR D 31   ? 2.0792 2.1061 1.8325 0.3992  -0.0032 -0.1499 31   THR D CA  
12972 C  C   . THR D 31   ? 2.0083 2.0563 1.7768 0.3951  0.0038  -0.1457 31   THR D C   
12973 O  O   . THR D 31   ? 2.0048 2.0644 1.7745 0.3980  0.0105  -0.1432 31   THR D O   
12974 C  CB  . THR D 31   ? 1.9947 2.0077 1.7390 0.3971  -0.0084 -0.1530 31   THR D CB  
12975 O  OG1 . THR D 31   ? 2.0321 2.0486 1.7881 0.3896  -0.0107 -0.1528 31   THR D OG1 
12976 C  CG2 . THR D 31   ? 1.9414 1.9572 1.6782 0.3994  -0.0043 -0.1520 31   THR D CG2 
12977 N  N   . LYS D 32   ? 1.5171 1.5699 1.2973 0.3880  0.0023  -0.1450 32   LYS D N   
12978 C  CA  . LYS D 32   ? 1.5531 1.6256 1.3494 0.3829  0.0083  -0.1412 32   LYS D CA  
12979 C  C   . LYS D 32   ? 1.5824 1.6689 1.3878 0.3849  0.0127  -0.1389 32   LYS D C   
12980 O  O   . LYS D 32   ? 1.5729 1.6751 1.3852 0.3847  0.0197  -0.1361 32   LYS D O   
12981 C  CB  . LYS D 32   ? 1.4760 1.5548 1.2701 0.3824  0.0139  -0.1395 32   LYS D CB  
12982 C  CG  . LYS D 32   ? 1.4516 1.5190 1.2387 0.3798  0.0097  -0.1415 32   LYS D CG  
12983 C  CD  . LYS D 32   ? 1.3581 1.4322 1.1431 0.3793  0.0158  -0.1392 32   LYS D CD  
12984 C  CE  . LYS D 32   ? 1.2147 1.2788 0.9940 0.3765  0.0115  -0.1409 32   LYS D CE  
12985 N  NZ  . LYS D 32   ? 1.3228 1.3676 1.0858 0.3808  0.0043  -0.1453 32   LYS D NZ  
12986 N  N   . MET D 33   ? 2.0838 2.1640 1.8888 0.3867  0.0083  -0.1402 33   MET D N   
12987 C  CA  . MET D 33   ? 2.0698 2.1616 1.8828 0.3889  0.0111  -0.1384 33   MET D CA  
12988 C  C   . MET D 33   ? 2.1233 2.2199 1.9494 0.3833  0.0084  -0.1377 33   MET D C   
12989 O  O   . MET D 33   ? 2.1598 2.2440 1.9841 0.3803  0.0026  -0.1395 33   MET D O   
12990 C  CB  . MET D 33   ? 2.0335 2.1136 1.8337 0.3967  0.0085  -0.1404 33   MET D CB  
12991 C  CG  . MET D 33   ? 2.0578 2.1151 1.8454 0.3976  0.0009  -0.1440 33   MET D CG  
12992 S  SD  . MET D 33   ? 2.2501 2.2939 2.0255 0.4056  -0.0024 -0.1459 33   MET D SD  
12993 C  CE  . MET D 33   ? 2.0938 2.1126 1.8586 0.4034  -0.0111 -0.1501 33   MET D CE  
12994 N  N   . ASP D 34   ? 1.7660 1.8807 1.6056 0.3818  0.0125  -0.1351 34   ASP D N   
12995 C  CA  . ASP D 34   ? 1.6206 1.7415 1.4731 0.3768  0.0104  -0.1340 34   ASP D CA  
12996 C  C   . ASP D 34   ? 1.4510 1.5799 1.3075 0.3808  0.0113  -0.1331 34   ASP D C   
12997 O  O   . ASP D 34   ? 1.5240 1.6626 1.3802 0.3852  0.0159  -0.1323 34   ASP D O   
12998 C  CB  . ASP D 34   ? 1.6832 1.8201 1.5506 0.3692  0.0143  -0.1316 34   ASP D CB  
12999 C  CG  . ASP D 34   ? 1.6551 1.7923 1.5327 0.3630  0.0105  -0.1312 34   ASP D CG  
13000 O  OD1 . ASP D 34   ? 1.6340 1.7575 1.5063 0.3642  0.0047  -0.1329 34   ASP D OD1 
13001 O  OD2 . ASP D 34   ? 1.5471 1.6979 1.4378 0.3568  0.0135  -0.1292 34   ASP D OD2 
13002 N  N   . ALA D 35   ? 1.2263 1.3510 1.0865 0.3794  0.0069  -0.1333 35   ALA D N   
13003 C  CA  . ALA D 35   ? 1.2927 1.4231 1.1557 0.3833  0.0068  -0.1326 35   ALA D CA  
13004 C  C   . ALA D 35   ? 1.2703 1.4155 1.1500 0.3774  0.0073  -0.1306 35   ALA D C   
13005 O  O   . ALA D 35   ? 1.2553 1.3963 1.1398 0.3714  0.0043  -0.1305 35   ALA D O   
13006 C  CB  . ALA D 35   ? 1.3322 1.4424 1.1823 0.3881  0.0010  -0.1347 35   ALA D CB  
13007 N  N   . PHE D 36   ? 1.1981 1.3605 1.0864 0.3792  0.0108  -0.1291 36   PHE D N   
13008 C  CA  . PHE D 36   ? 1.0923 1.2712 0.9969 0.3738  0.0119  -0.1273 36   PHE D CA  
13009 C  C   . PHE D 36   ? 1.1658 1.3432 1.0699 0.3778  0.0085  -0.1273 36   PHE D C   
13010 O  O   . PHE D 36   ? 1.2679 1.4465 1.1663 0.3849  0.0094  -0.1277 36   PHE D O   
13011 C  CB  . PHE D 36   ? 1.1002 1.3013 1.0162 0.3720  0.0187  -0.1258 36   PHE D CB  
13012 C  CG  . PHE D 36   ? 1.1347 1.3359 1.0475 0.3706  0.0229  -0.1258 36   PHE D CG  
13013 C  CD1 . PHE D 36   ? 1.1383 1.3431 1.0583 0.3630  0.0244  -0.1249 36   PHE D CD1 
13014 C  CD2 . PHE D 36   ? 1.1952 1.3925 1.0971 0.3770  0.0255  -0.1266 36   PHE D CD2 
13015 C  CE1 . PHE D 36   ? 1.1379 1.3421 1.0539 0.3620  0.0284  -0.1247 36   PHE D CE1 
13016 C  CE2 . PHE D 36   ? 1.2894 1.4861 1.1874 0.3760  0.0295  -0.1264 36   PHE D CE2 
13017 C  CZ  . PHE D 36   ? 1.2311 1.4310 1.1359 0.3685  0.0310  -0.1255 36   PHE D CZ  
13018 N  N   . SER D 37   ? 1.1274 1.3021 1.0371 0.3735  0.0048  -0.1268 37   SER D N   
13019 C  CA  . SER D 37   ? 1.1052 1.2762 1.0133 0.3769  0.0013  -0.1267 37   SER D CA  
13020 C  C   . SER D 37   ? 1.1737 1.3571 1.0965 0.3708  0.0007  -0.1251 37   SER D C   
13021 O  O   . SER D 37   ? 1.1641 1.3498 1.0945 0.3633  0.0009  -0.1245 37   SER D O   
13022 C  CB  . SER D 37   ? 1.0329 1.1790 0.9268 0.3795  -0.0041 -0.1282 37   SER D CB  
13023 O  OG  . SER D 37   ? 1.2237 1.3656 1.1170 0.3816  -0.0074 -0.1278 37   SER D OG  
13024 N  N   . PRO D 38   ? 1.3827 1.5742 1.3093 0.3739  -0.0001 -0.1246 38   PRO D N   
13025 C  CA  . PRO D 38   ? 1.3078 1.5106 1.2476 0.3682  -0.0010 -0.1232 38   PRO D CA  
13026 C  C   . PRO D 38   ? 1.2916 1.4792 1.2293 0.3641  -0.0056 -0.1230 38   PRO D C   
13027 O  O   . PRO D 38   ? 1.3497 1.5447 1.2985 0.3569  -0.0056 -0.1219 38   PRO D O   
13028 C  CB  . PRO D 38   ? 1.3188 1.5300 1.2594 0.3743  -0.0016 -0.1231 38   PRO D CB  
13029 C  CG  . PRO D 38   ? 1.3861 1.5845 1.3111 0.3833  -0.0022 -0.1243 38   PRO D CG  
13030 C  CD  . PRO D 38   ? 1.4656 1.6596 1.3860 0.3825  0.0005  -0.1251 38   PRO D CD  
13031 N  N   . PHE D 39   ? 1.1271 1.2935 1.0508 0.3684  -0.0093 -0.1240 39   PHE D N   
13032 C  CA  . PHE D 39   ? 1.1953 1.3453 1.1158 0.3649  -0.0134 -0.1240 39   PHE D CA  
13033 C  C   . PHE D 39   ? 1.2741 1.4052 1.1831 0.3651  -0.0148 -0.1258 39   PHE D C   
13034 O  O   . PHE D 39   ? 1.3018 1.4288 1.2017 0.3702  -0.0135 -0.1271 39   PHE D O   
13035 C  CB  . PHE D 39   ? 1.1943 1.3346 1.1083 0.3696  -0.0169 -0.1237 39   PHE D CB  
13036 C  CG  . PHE D 39   ? 1.2021 1.3287 1.1005 0.3784  -0.0179 -0.1251 39   PHE D CG  
13037 C  CD1 . PHE D 39   ? 1.2228 1.3260 1.1078 0.3798  -0.0207 -0.1266 39   PHE D CD1 
13038 C  CD2 . PHE D 39   ? 1.1924 1.3295 1.0896 0.3851  -0.0161 -0.1250 39   PHE D CD2 
13039 C  CE1 . PHE D 39   ? 1.2406 1.3306 1.1109 0.3878  -0.0216 -0.1279 39   PHE D CE1 
13040 C  CE2 . PHE D 39   ? 1.2291 1.3534 1.1117 0.3934  -0.0170 -0.1261 39   PHE D CE2 
13041 C  CZ  . PHE D 39   ? 1.2587 1.3592 1.1276 0.3947  -0.0197 -0.1275 39   PHE D CZ  
13042 N  N   . PRO D 40   ? 1.7918 1.9116 1.7011 0.3596  -0.0175 -0.1261 40   PRO D N   
13043 C  CA  . PRO D 40   ? 1.7685 1.8695 1.6668 0.3598  -0.0195 -0.1283 40   PRO D CA  
13044 C  C   . PRO D 40   ? 1.8878 1.9700 1.7703 0.3670  -0.0221 -0.1299 40   PRO D C   
13045 O  O   . PRO D 40   ? 1.9974 2.0693 1.8763 0.3683  -0.0249 -0.1296 40   PRO D O   
13046 C  CB  . PRO D 40   ? 1.6966 1.7910 1.6004 0.3525  -0.0221 -0.1281 40   PRO D CB  
13047 C  CG  . PRO D 40   ? 1.7518 1.8559 1.6655 0.3502  -0.0224 -0.1258 40   PRO D CG  
13048 C  CD  . PRO D 40   ? 1.8163 1.9409 1.7368 0.3528  -0.0187 -0.1245 40   PRO D CD  
13049 N  N   . ILE D 41   ? 1.8163 1.8937 1.6889 0.3719  -0.0210 -0.1316 41   ILE D N   
13050 C  CA  . ILE D 41   ? 1.8448 1.9046 1.7017 0.3791  -0.0232 -0.1332 41   ILE D CA  
13051 C  C   . ILE D 41   ? 1.8711 1.9075 1.7195 0.3769  -0.0276 -0.1351 41   ILE D C   
13052 O  O   . ILE D 41   ? 1.9943 2.0155 1.8329 0.3809  -0.0299 -0.1357 41   ILE D O   
13053 C  CB  . ILE D 41   ? 1.8424 1.9025 1.6908 0.3844  -0.0209 -0.1347 41   ILE D CB  
13054 C  CG1 . ILE D 41   ? 1.7192 1.8029 1.5769 0.3862  -0.0161 -0.1328 41   ILE D CG1 
13055 C  CG2 . ILE D 41   ? 1.9033 1.9450 1.7351 0.3920  -0.0231 -0.1363 41   ILE D CG2 
13056 C  CD1 . ILE D 41   ? 1.7189 1.8079 1.5748 0.3930  -0.0156 -0.1318 41   ILE D CD1 
13057 N  N   . GLU D 42   ? 1.5012 1.5343 1.3532 0.3706  -0.0286 -0.1362 42   GLU D N   
13058 C  CA  . GLU D 42   ? 1.5546 1.5666 1.3997 0.3676  -0.0327 -0.1386 42   GLU D CA  
13059 C  C   . GLU D 42   ? 1.6048 1.5987 1.4334 0.3726  -0.0344 -0.1419 42   GLU D C   
13060 O  O   . GLU D 42   ? 1.6339 1.6095 1.4557 0.3702  -0.0379 -0.1446 42   GLU D O   
13061 C  CB  . GLU D 42   ? 1.6374 1.6395 1.4830 0.3660  -0.0352 -0.1377 42   GLU D CB  
13062 C  CG  . GLU D 42   ? 1.7828 1.8003 1.6441 0.3603  -0.0342 -0.1348 42   GLU D CG  
13063 C  CD  . GLU D 42   ? 1.7746 1.7946 1.6447 0.3525  -0.0349 -0.1353 42   GLU D CD  
13064 O  OE1 . GLU D 42   ? 1.8114 1.8156 1.6748 0.3507  -0.0376 -0.1382 42   GLU D OE1 
13065 O  OE2 . GLU D 42   ? 1.6395 1.6774 1.5231 0.3481  -0.0329 -0.1330 42   GLU D OE2 
13066 N  N   . GLU D 43   ? 2.1905 2.1890 2.0126 0.3793  -0.0321 -0.1418 43   GLU D N   
13067 C  CA  . GLU D 43   ? 2.2804 2.2635 2.0869 0.3844  -0.0334 -0.1448 43   GLU D CA  
13068 C  C   . GLU D 43   ? 2.1640 2.1568 1.9705 0.3851  -0.0308 -0.1455 43   GLU D C   
13069 O  O   . GLU D 43   ? 2.2169 2.1972 2.0141 0.3851  -0.0328 -0.1485 43   GLU D O   
13070 C  CB  . GLU D 43   ? 2.2912 2.2693 2.0879 0.3926  -0.0328 -0.1443 43   GLU D CB  
13071 C  CG  . GLU D 43   ? 2.2910 2.2591 2.0863 0.3929  -0.0349 -0.1433 43   GLU D CG  
13072 C  CD  . GLU D 43   ? 2.3367 2.2785 2.1205 0.3914  -0.0390 -0.1462 43   GLU D CD  
13073 O  OE1 . GLU D 43   ? 2.2707 2.2007 2.0447 0.3922  -0.0404 -0.1493 43   GLU D OE1 
13074 O  OE2 . GLU D 43   ? 2.3220 2.2549 2.1065 0.3893  -0.0406 -0.1454 43   GLU D OE2 
13075 N  N   . VAL D 44   ? 1.3818 1.3965 1.1982 0.3857  -0.0264 -0.1428 44   VAL D N   
13076 C  CA  . VAL D 44   ? 1.3369 1.3622 1.1552 0.3852  -0.0232 -0.1429 44   VAL D CA  
13077 C  C   . VAL D 44   ? 1.4593 1.4857 1.2848 0.3774  -0.0243 -0.1434 44   VAL D C   
13078 O  O   . VAL D 44   ? 1.5012 1.5257 1.3225 0.3769  -0.0240 -0.1450 44   VAL D O   
13079 C  CB  . VAL D 44   ? 1.3627 1.4113 1.1908 0.3871  -0.0179 -0.1399 44   VAL D CB  
13080 C  CG1 . VAL D 44   ? 1.3037 1.3643 1.1356 0.3854  -0.0139 -0.1395 44   VAL D CG1 
13081 C  CG2 . VAL D 44   ? 1.4032 1.4503 1.2227 0.3957  -0.0169 -0.1398 44   VAL D CG2 
13082 N  N   . ILE D 45   ? 2.0120 2.0412 1.8480 0.3716  -0.0258 -0.1422 45   ILE D N   
13083 C  CA  . ILE D 45   ? 2.0269 2.0588 1.8712 0.3642  -0.0266 -0.1423 45   ILE D CA  
13084 C  C   . ILE D 45   ? 2.1049 2.1174 1.9385 0.3633  -0.0309 -0.1462 45   ILE D C   
13085 O  O   . ILE D 45   ? 2.1621 2.1766 1.9965 0.3605  -0.0308 -0.1472 45   ILE D O   
13086 C  CB  . ILE D 45   ? 1.9106 1.9471 1.7670 0.3587  -0.0277 -0.1403 45   ILE D CB  
13087 C  CG1 . ILE D 45   ? 1.8710 1.9240 1.7356 0.3607  -0.0245 -0.1371 45   ILE D CG1 
13088 C  CG2 . ILE D 45   ? 1.9102 1.9545 1.7774 0.3512  -0.0275 -0.1398 45   ILE D CG2 
13089 C  CD1 . ILE D 45   ? 1.8155 1.8908 1.6906 0.3592  -0.0193 -0.1350 45   ILE D CD1 
13090 N  N   . GLU D 46   ? 2.3784 2.3715 2.2016 0.3656  -0.0349 -0.1486 46   GLU D N   
13091 C  CA  . GLU D 46   ? 2.4331 2.4070 2.2462 0.3643  -0.0394 -0.1528 46   GLU D CA  
13092 C  C   . GLU D 46   ? 2.3836 2.3534 2.1847 0.3691  -0.0389 -0.1550 46   GLU D C   
13093 O  O   . GLU D 46   ? 2.3601 2.3198 2.1552 0.3673  -0.0419 -0.1584 46   GLU D O   
13094 C  CB  . GLU D 46   ? 2.4615 2.4153 2.2667 0.3650  -0.0433 -0.1548 46   GLU D CB  
13095 C  CG  . GLU D 46   ? 2.5178 2.4668 2.3136 0.3724  -0.0421 -0.1540 46   GLU D CG  
13096 C  CD  . GLU D 46   ? 2.6433 2.5707 2.4218 0.3764  -0.0451 -0.1580 46   GLU D CD  
13097 O  OE1 . GLU D 46   ? 2.6572 2.5714 2.4314 0.3727  -0.0489 -0.1617 46   GLU D OE1 
13098 O  OE2 . GLU D 46   ? 2.6563 2.5801 2.4256 0.3832  -0.0439 -0.1576 46   GLU D OE2 
13099 N  N   . GLU D 47   ? 1.9410 1.9187 1.7384 0.3754  -0.0351 -0.1533 47   GLU D N   
13100 C  CA  . GLU D 47   ? 1.9574 1.9302 1.7424 0.3806  -0.0345 -0.1553 47   GLU D CA  
13101 C  C   . GLU D 47   ? 1.8764 1.8608 1.6656 0.3781  -0.0320 -0.1549 47   GLU D C   
13102 O  O   . GLU D 47   ? 1.8523 1.8269 1.6316 0.3790  -0.0341 -0.1578 47   GLU D O   
13103 C  CB  . GLU D 47   ? 1.9776 1.9561 1.7579 0.3881  -0.0309 -0.1535 47   GLU D CB  
13104 C  CG  . GLU D 47   ? 2.0407 2.0068 1.8043 0.3945  -0.0316 -0.1561 47   GLU D CG  
13105 C  CD  . GLU D 47   ? 2.1187 2.0608 1.8691 0.3964  -0.0367 -0.1596 47   GLU D CD  
13106 O  OE1 . GLU D 47   ? 2.1480 2.0832 1.9021 0.3931  -0.0393 -0.1596 47   GLU D OE1 
13107 O  OE2 . GLU D 47   ? 2.0737 2.0037 1.8099 0.4010  -0.0380 -0.1622 47   GLU D OE2 
13108 N  N   . ILE D 48   ? 1.6355 1.6399 1.4387 0.3751  -0.0277 -0.1513 48   ILE D N   
13109 C  CA  . ILE D 48   ? 1.5541 1.5704 1.3611 0.3732  -0.0243 -0.1503 48   ILE D CA  
13110 C  C   . ILE D 48   ? 1.5527 1.5740 1.3707 0.3655  -0.0253 -0.1498 48   ILE D C   
13111 O  O   . ILE D 48   ? 1.5259 1.5533 1.3450 0.3637  -0.0234 -0.1495 48   ILE D O   
13112 C  CB  . ILE D 48   ? 1.4790 1.5152 1.2926 0.3759  -0.0174 -0.1466 48   ILE D CB  
13113 C  CG1 . ILE D 48   ? 1.4900 1.5385 1.3166 0.3740  -0.0158 -0.1437 48   ILE D CG1 
13114 C  CG2 . ILE D 48   ? 1.6133 1.6449 1.4140 0.3840  -0.0158 -0.1475 48   ILE D CG2 
13115 C  CD1 . ILE D 48   ? 1.3798 1.4478 1.2132 0.3766  -0.0095 -0.1407 48   ILE D CD1 
13116 N  N   . ALA D 49   ? 2.0227 2.0416 1.8487 0.3610  -0.0282 -0.1495 49   ALA D N   
13117 C  CA  . ALA D 49   ? 1.9437 1.9683 1.7812 0.3536  -0.0290 -0.1487 49   ALA D CA  
13118 C  C   . ALA D 49   ? 2.0220 2.0309 1.8588 0.3503  -0.0350 -0.1513 49   ALA D C   
13119 O  O   . ALA D 49   ? 2.0700 2.0813 1.9154 0.3475  -0.0355 -0.1496 49   ALA D O   
13120 C  CB  . ALA D 49   ? 1.9487 1.9939 1.8019 0.3504  -0.0243 -0.1443 49   ALA D CB  
13121 N  N   . HIS D 50   ? 2.1305 2.1231 1.9570 0.3504  -0.0396 -0.1555 50   HIS D N   
13122 C  CA  . HIS D 50   ? 2.2333 2.2105 2.0591 0.3466  -0.0453 -0.1586 50   HIS D CA  
13123 C  C   . HIS D 50   ? 2.1880 2.1663 2.0190 0.3370  -0.0481 -0.1581 50   HIS D C   
13124 O  O   . HIS D 50   ? 2.1731 2.1482 1.9963 0.3382  -0.0491 -0.1602 50   HIS D O   
13125 C  CB  . HIS D 50   ? 2.3407 2.2969 2.1509 0.3507  -0.0494 -0.1628 50   HIS D CB  
13126 C  CG  . HIS D 50   ? 2.4848 2.4263 2.2950 0.3478  -0.0534 -0.1646 50   HIS D CG  
13127 N  ND1 . HIS D 50   ? 2.4504 2.3929 2.2644 0.3486  -0.0519 -0.1619 50   HIS D ND1 
13128 C  CD2 . HIS D 50   ? 2.5309 2.4572 2.3387 0.3409  -0.0589 -0.1673 50   HIS D CD2 
13129 C  CE1 . HIS D 50   ? 2.4019 2.3287 2.2143 0.3456  -0.0558 -0.1642 50   HIS D CE1 
13130 N  NE2 . HIS D 50   ? 2.4855 2.4028 2.2949 0.3394  -0.0601 -0.1669 50   HIS D NE2 
13131 N  N   . GLY D 51   ? 1.7815 1.7641 1.6251 0.3281  -0.0492 -0.1554 51   GLY D N   
13132 C  CA  . GLY D 51   ? 1.7053 1.6901 1.5553 0.3189  -0.0517 -0.1545 51   GLY D CA  
13133 C  C   . GLY D 51   ? 1.6164 1.6138 1.4825 0.3112  -0.0498 -0.1499 51   GLY D C   
13134 O  O   . GLY D 51   ? 1.5543 1.5584 1.4266 0.3129  -0.0470 -0.1476 51   GLY D O   
13135 N  N   . ASP D 52   ? 2.0467 2.0472 1.9192 0.3031  -0.0516 -0.1487 52   ASP D N   
13136 C  CA  . ASP D 52   ? 2.0124 2.0242 1.8998 0.2953  -0.0501 -0.1444 52   ASP D CA  
13137 C  C   . ASP D 52   ? 1.9213 1.9516 1.8155 0.2977  -0.0436 -0.1407 52   ASP D C   
13138 O  O   . ASP D 52   ? 1.8958 1.9322 1.7857 0.3012  -0.0406 -0.1406 52   ASP D O   
13139 C  CB  . ASP D 52   ? 2.0004 2.0112 1.8922 0.2868  -0.0534 -0.1441 52   ASP D CB  
13140 C  CG  . ASP D 52   ? 1.9834 2.0036 1.8899 0.2785  -0.0524 -0.1400 52   ASP D CG  
13141 O  OD1 . ASP D 52   ? 1.8819 1.9048 1.7944 0.2783  -0.0508 -0.1382 52   ASP D OD1 
13142 O  OD2 . ASP D 52   ? 1.9557 1.9802 1.8673 0.2724  -0.0532 -0.1386 52   ASP D OD2 
13143 N  N   . THR D 53   ? 1.4202 1.4593 1.3249 0.2956  -0.0412 -0.1377 53   THR D N   
13144 C  CA  . THR D 53   ? 1.3028 1.3604 1.2158 0.2965  -0.0353 -0.1343 53   THR D CA  
13145 C  C   . THR D 53   ? 1.3078 1.3742 1.2276 0.2894  -0.0337 -0.1316 53   THR D C   
13146 O  O   . THR D 53   ? 1.2901 1.3697 1.2132 0.2907  -0.0285 -0.1296 53   THR D O   
13147 C  CB  . THR D 53   ? 1.3162 1.3808 1.2389 0.2955  -0.0339 -0.1320 53   THR D CB  
13148 O  OG1 . THR D 53   ? 1.4248 1.4865 1.3557 0.2865  -0.0368 -0.1303 53   THR D OG1 
13149 C  CG2 . THR D 53   ? 1.3997 1.4546 1.3147 0.3030  -0.0353 -0.1344 53   THR D CG2 
13150 N  N   . GLY D 54   ? 1.4469 1.5060 1.3689 0.2821  -0.0380 -0.1317 54   GLY D N   
13151 C  CA  . GLY D 54   ? 1.5053 1.5721 1.4345 0.2751  -0.0370 -0.1289 54   GLY D CA  
13152 C  C   . GLY D 54   ? 1.4430 1.5196 1.3861 0.2684  -0.0352 -0.1251 54   GLY D C   
13153 O  O   . GLY D 54   ? 1.3706 1.4509 1.3199 0.2616  -0.0353 -0.1229 54   GLY D O   
13154 N  N   . VAL D 55   ? 1.4296 1.5101 1.3772 0.2706  -0.0337 -0.1244 55   VAL D N   
13155 C  CA  . VAL D 55   ? 1.2939 1.3827 1.2542 0.2644  -0.0325 -0.1211 55   VAL D CA  
13156 C  C   . VAL D 55   ? 1.2809 1.3600 1.2445 0.2571  -0.0373 -0.1210 55   VAL D C   
13157 O  O   . VAL D 55   ? 1.2675 1.3530 1.2405 0.2501  -0.0365 -0.1180 55   VAL D O   
13158 C  CB  . VAL D 55   ? 1.3670 1.4616 1.3301 0.2693  -0.0304 -0.1207 55   VAL D CB  
13159 C  CG1 . VAL D 55   ? 1.3713 1.4734 1.3466 0.2632  -0.0297 -0.1176 55   VAL D CG1 
13160 C  CG2 . VAL D 55   ? 1.3291 1.4361 1.2910 0.2757  -0.0251 -0.1207 55   VAL D CG2 
13161 N  N   . PRO D 56   ? 0.9378 1.0017 0.8946 0.2580  -0.0421 -0.1240 56   PRO D N   
13162 C  CA  . PRO D 56   ? 0.8432 0.8991 0.8048 0.2505  -0.0460 -0.1236 56   PRO D CA  
13163 C  C   . PRO D 56   ? 0.8855 0.9438 0.8516 0.2436  -0.0472 -0.1225 56   PRO D C   
13164 O  O   . PRO D 56   ? 0.8888 0.9494 0.8640 0.2367  -0.0477 -0.1201 56   PRO D O   
13165 C  CB  . PRO D 56   ? 0.7792 0.8181 0.7308 0.2535  -0.0504 -0.1278 56   PRO D CB  
13166 C  CG  . PRO D 56   ? 0.9714 1.0104 0.9158 0.2627  -0.0482 -0.1291 56   PRO D CG  
13167 C  CD  . PRO D 56   ? 1.0008 1.0540 0.9460 0.2658  -0.0437 -0.1276 56   PRO D CD  
13168 N  N   . ARG D 57   ? 1.1530 1.2107 1.1125 0.2455  -0.0477 -0.1240 57   ARG D N   
13169 C  CA  . ARG D 57   ? 1.1995 1.2585 1.1622 0.2395  -0.0493 -0.1231 57   ARG D CA  
13170 C  C   . ARG D 57   ? 1.1028 1.1756 1.0755 0.2352  -0.0449 -0.1185 57   ARG D C   
13171 O  O   . ARG D 57   ? 1.0486 1.1227 1.0280 0.2285  -0.0461 -0.1168 57   ARG D O   
13172 C  CB  . ARG D 57   ? 1.3027 1.3582 1.2551 0.2434  -0.0505 -0.1257 57   ARG D CB  
13173 C  CG  . ARG D 57   ? 1.3320 1.3969 1.2805 0.2490  -0.0451 -0.1244 57   ARG D CG  
13174 C  CD  . ARG D 57   ? 1.5043 1.5617 1.4394 0.2570  -0.0461 -0.1282 57   ARG D CD  
13175 N  NE  . ARG D 57   ? 1.5649 1.6102 1.4928 0.2563  -0.0521 -0.1319 57   ARG D NE  
13176 C  CZ  . ARG D 57   ? 1.7096 1.7454 1.6252 0.2623  -0.0545 -0.1359 57   ARG D CZ  
13177 N  NH1 . ARG D 57   ? 1.5503 1.5870 1.4589 0.2700  -0.0512 -0.1367 57   ARG D NH1 
13178 N  NH2 . ARG D 57   ? 1.8695 1.8950 1.7796 0.2607  -0.0604 -0.1394 57   ARG D NH2 
13179 N  N   . LEU D 58   ? 1.0745 1.1578 1.0487 0.2388  -0.0396 -0.1167 58   LEU D N   
13180 C  CA  . LEU D 58   ? 1.0396 1.1359 1.0234 0.2345  -0.0351 -0.1127 58   LEU D CA  
13181 C  C   . LEU D 58   ? 1.0305 1.1281 1.0243 0.2290  -0.0359 -0.1107 58   LEU D C   
13182 O  O   . LEU D 58   ? 0.9791 1.0822 0.9808 0.2228  -0.0348 -0.1078 58   LEU D O   
13183 C  CB  . LEU D 58   ? 1.0733 1.1807 1.0568 0.2396  -0.0294 -0.1118 58   LEU D CB  
13184 C  CG  . LEU D 58   ? 1.1008 1.2074 1.0738 0.2461  -0.0277 -0.1137 58   LEU D CG  
13185 C  CD1 . LEU D 58   ? 1.1265 1.2442 1.1004 0.2514  -0.0220 -0.1131 58   LEU D CD1 
13186 C  CD2 . LEU D 58   ? 1.1723 1.2800 1.1433 0.2431  -0.0267 -0.1124 58   LEU D CD2 
13187 N  N   . VAL D 59   ? 1.3435 1.4355 1.3365 0.2315  -0.0377 -0.1121 59   VAL D N   
13188 C  CA  . VAL D 59   ? 1.3269 1.4194 1.3283 0.2270  -0.0382 -0.1101 59   VAL D CA  
13189 C  C   . VAL D 59   ? 1.3179 1.4029 1.3227 0.2200  -0.0420 -0.1099 59   VAL D C   
13190 O  O   . VAL D 59   ? 1.3884 1.4781 1.4019 0.2140  -0.0412 -0.1070 59   VAL D O   
13191 C  CB  . VAL D 59   ? 1.3661 1.4526 1.3639 0.2322  -0.0393 -0.1118 59   VAL D CB  
13192 C  CG1 . VAL D 59   ? 1.3671 1.4508 1.3717 0.2276  -0.0406 -0.1102 59   VAL D CG1 
13193 C  CG2 . VAL D 59   ? 1.3523 1.4493 1.3495 0.2388  -0.0352 -0.1116 59   VAL D CG2 
13194 N  N   . LEU D 60   ? 0.8070 0.8804 0.8049 0.2205  -0.0463 -0.1130 60   LEU D N   
13195 C  CA  . LEU D 60   ? 0.8041 0.8707 0.8055 0.2139  -0.0501 -0.1133 60   LEU D CA  
13196 C  C   . LEU D 60   ? 0.7861 0.8602 0.7923 0.2093  -0.0492 -0.1110 60   LEU D C   
13197 O  O   . LEU D 60   ? 0.7250 0.8001 0.7390 0.2029  -0.0499 -0.1091 60   LEU D O   
13198 C  CB  . LEU D 60   ? 0.7673 0.8206 0.7602 0.2157  -0.0549 -0.1177 60   LEU D CB  
13199 C  CG  . LEU D 60   ? 0.6155 0.6610 0.6123 0.2090  -0.0593 -0.1187 60   LEU D CG  
13200 C  CD1 . LEU D 60   ? 0.6863 0.7304 0.6908 0.2047  -0.0586 -0.1165 60   LEU D CD1 
13201 C  CD2 . LEU D 60   ? 0.6976 0.7300 0.6859 0.2109  -0.0640 -0.1237 60   LEU D CD2 
13202 N  N   . LEU D 61   ? 1.0877 1.1665 1.0888 0.2126  -0.0474 -0.1112 61   LEU D N   
13203 C  CA  . LEU D 61   ? 1.0979 1.1828 1.1020 0.2089  -0.0462 -0.1090 61   LEU D CA  
13204 C  C   . LEU D 61   ? 1.0896 1.1847 1.1037 0.2045  -0.0421 -0.1047 61   LEU D C   
13205 O  O   . LEU D 61   ? 1.1271 1.2234 1.1474 0.1986  -0.0428 -0.1028 61   LEU D O   
13206 C  CB  . LEU D 61   ? 0.9815 1.0691 0.9772 0.2140  -0.0442 -0.1098 61   LEU D CB  
13207 C  CG  . LEU D 61   ? 0.9573 1.0503 0.9541 0.2112  -0.0425 -0.1074 61   LEU D CG  
13208 C  CD1 . LEU D 61   ? 0.9785 1.0649 0.9755 0.2075  -0.0478 -0.1088 61   LEU D CD1 
13209 C  CD2 . LEU D 61   ? 1.1153 1.2110 1.1031 0.2169  -0.0394 -0.1078 61   LEU D CD2 
13210 N  N   . PHE D 62   ? 1.2602 1.3629 1.2758 0.2072  -0.0378 -0.1034 62   PHE D N   
13211 C  CA  . PHE D 62   ? 1.3077 1.4206 1.3326 0.2031  -0.0338 -0.0997 62   PHE D CA  
13212 C  C   . PHE D 62   ? 1.3198 1.4301 1.3521 0.1986  -0.0356 -0.0986 62   PHE D C   
13213 O  O   . PHE D 62   ? 1.2452 1.3606 1.2850 0.1932  -0.0340 -0.0957 62   PHE D O   
13214 C  CB  . PHE D 62   ? 1.3650 1.4876 1.3901 0.2073  -0.0289 -0.0991 62   PHE D CB  
13215 C  CG  . PHE D 62   ? 1.4478 1.5762 1.4684 0.2097  -0.0252 -0.0987 62   PHE D CG  
13216 C  CD1 . PHE D 62   ? 1.4901 1.6246 1.5146 0.2052  -0.0220 -0.0958 62   PHE D CD1 
13217 C  CD2 . PHE D 62   ? 1.4587 1.5856 1.4707 0.2166  -0.0245 -0.1011 62   PHE D CD2 
13218 C  CE1 . PHE D 62   ? 1.5308 1.6697 1.5505 0.2074  -0.0180 -0.0952 62   PHE D CE1 
13219 C  CE2 . PHE D 62   ? 1.4531 1.5848 1.4605 0.2189  -0.0206 -0.1006 62   PHE D CE2 
13220 C  CZ  . PHE D 62   ? 1.4343 1.5718 1.4455 0.2142  -0.0172 -0.0976 62   PHE D CZ  
13221 N  N   . GLY D 63   ? 1.1686 1.2703 1.1981 0.2008  -0.0388 -0.1009 63   GLY D N   
13222 C  CA  . GLY D 63   ? 1.0801 1.1779 1.1155 0.1968  -0.0403 -0.0999 63   GLY D CA  
13223 C  C   . GLY D 63   ? 1.0400 1.1335 1.0796 0.1903  -0.0430 -0.0991 63   GLY D C   
13224 O  O   . GLY D 63   ? 1.0868 1.1829 1.1340 0.1853  -0.0421 -0.0965 63   GLY D O   
13225 N  N   . LEU D 64   ? 0.8628 0.9497 0.8974 0.1904  -0.0463 -0.1016 64   LEU D N   
13226 C  CA  . LEU D 64   ? 0.8833 0.9674 0.9222 0.1846  -0.0490 -0.1012 64   LEU D CA  
13227 C  C   . LEU D 64   ? 0.8764 0.9699 0.9203 0.1813  -0.0461 -0.0978 64   LEU D C   
13228 O  O   . LEU D 64   ? 0.9187 1.0130 0.9695 0.1758  -0.0465 -0.0958 64   LEU D O   
13229 C  CB  . LEU D 64   ? 0.9437 1.0198 0.9760 0.1860  -0.0535 -0.1050 64   LEU D CB  
13230 C  CG  . LEU D 64   ? 0.9973 1.0619 1.0251 0.1878  -0.0570 -0.1086 64   LEU D CG  
13231 C  CD1 . LEU D 64   ? 1.0833 1.1407 1.1051 0.1885  -0.0617 -0.1127 64   LEU D CD1 
13232 C  CD2 . LEU D 64   ? 0.9132 0.9733 0.9480 0.1827  -0.0577 -0.1076 64   LEU D CD2 
13233 N  N   . ILE D 65   ? 0.9342 1.0344 0.9745 0.1846  -0.0429 -0.0971 65   ILE D N   
13234 C  CA  . ILE D 65   ? 0.9532 1.0619 0.9976 0.1815  -0.0393 -0.0937 65   ILE D CA  
13235 C  C   . ILE D 65   ? 0.9749 1.0894 1.0276 0.1779  -0.0362 -0.0906 65   ILE D C   
13236 O  O   . ILE D 65   ? 1.0133 1.1308 1.0719 0.1730  -0.0352 -0.0880 65   ILE D O   
13237 C  CB  . ILE D 65   ? 1.0594 1.1735 1.0977 0.1859  -0.0357 -0.0936 65   ILE D CB  
13238 C  CG1 . ILE D 65   ? 1.0809 1.1890 1.1103 0.1892  -0.0388 -0.0963 65   ILE D CG1 
13239 C  CG2 . ILE D 65   ? 0.8452 0.9678 0.8877 0.1826  -0.0310 -0.0899 65   ILE D CG2 
13240 C  CD1 . ILE D 65   ? 0.8986 1.0107 0.9207 0.1941  -0.0352 -0.0963 65   ILE D CD1 
13241 N  N   . GLY D 66   ? 1.0319 1.1479 1.0851 0.1806  -0.0350 -0.0911 66   GLY D N   
13242 C  CA  . GLY D 66   ? 1.0607 1.1826 1.1213 0.1778  -0.0324 -0.0886 66   GLY D CA  
13243 C  C   . GLY D 66   ? 1.0967 1.2132 1.1628 0.1727  -0.0348 -0.0875 66   GLY D C   
13244 O  O   . GLY D 66   ? 1.1512 1.2722 1.2237 0.1682  -0.0329 -0.0847 66   GLY D O   
13245 N  N   . ALA D 67   ? 0.8188 0.9253 0.8823 0.1733  -0.0388 -0.0899 67   ALA D N   
13246 C  CA  . ALA D 67   ? 0.7946 0.8955 0.8632 0.1684  -0.0408 -0.0890 67   ALA D CA  
13247 C  C   . ALA D 67   ? 0.8229 0.9254 0.8955 0.1634  -0.0413 -0.0875 67   ALA D C   
13248 O  O   . ALA D 67   ? 0.8937 0.9981 0.9729 0.1588  -0.0403 -0.0849 67   ALA D O   
13249 C  CB  . ALA D 67   ? 0.8357 0.9251 0.9002 0.1698  -0.0447 -0.0922 67   ALA D CB  
13250 N  N   . ALA D 68   ? 0.6064 0.7081 0.6747 0.1647  -0.0430 -0.0891 68   ALA D N   
13251 C  CA  . ALA D 68   ? 0.5678 0.6712 0.6391 0.1609  -0.0437 -0.0878 68   ALA D CA  
13252 C  C   . ALA D 68   ? 0.6408 0.7529 0.7161 0.1587  -0.0392 -0.0840 68   ALA D C   
13253 O  O   . ALA D 68   ? 0.6844 0.7977 0.7650 0.1542  -0.0388 -0.0818 68   ALA D O   
13254 C  CB  . ALA D 68   ? 0.5786 0.6798 0.6431 0.1638  -0.0462 -0.0903 68   ALA D CB  
13255 N  N   . SER D 69   ? 0.6756 0.7937 0.7483 0.1616  -0.0355 -0.0833 69   SER D N   
13256 C  CA  . SER D 69   ? 0.6813 0.8074 0.7576 0.1592  -0.0310 -0.0800 69   SER D CA  
13257 C  C   . SER D 69   ? 0.7645 0.8924 0.8484 0.1550  -0.0298 -0.0777 69   SER D C   
13258 O  O   . SER D 69   ? 0.7044 0.8355 0.7924 0.1510  -0.0277 -0.0750 69   SER D O   
13259 C  CB  . SER D 69   ? 0.6963 0.8289 0.7691 0.1631  -0.0272 -0.0802 69   SER D CB  
13260 O  OG  . SER D 69   ? 0.8335 0.9643 0.8986 0.1670  -0.0277 -0.0820 69   SER D OG  
13261 N  N   . GLY D 70   ? 0.8316 0.9567 0.9166 0.1561  -0.0310 -0.0788 70   GLY D N   
13262 C  CA  . GLY D 70   ? 0.7992 0.9253 0.8904 0.1527  -0.0299 -0.0767 70   GLY D CA  
13263 C  C   . GLY D 70   ? 0.7326 0.8538 0.8281 0.1479  -0.0318 -0.0755 70   GLY D C   
13264 O  O   . GLY D 70   ? 0.6712 0.7952 0.7718 0.1440  -0.0299 -0.0729 70   GLY D O   
13265 N  N   . PHE D 71   ? 0.6511 0.7650 0.7446 0.1482  -0.0356 -0.0777 71   PHE D N   
13266 C  CA  . PHE D 71   ? 0.7219 0.8319 0.8200 0.1436  -0.0375 -0.0769 71   PHE D CA  
13267 C  C   . PHE D 71   ? 0.8090 0.9236 0.9089 0.1412  -0.0362 -0.0749 71   PHE D C   
13268 O  O   . PHE D 71   ? 0.7932 0.9086 0.8985 0.1372  -0.0354 -0.0726 71   PHE D O   
13269 C  CB  . PHE D 71   ? 0.6916 0.7936 0.7875 0.1443  -0.0419 -0.0802 71   PHE D CB  
13270 C  CG  . PHE D 71   ? 0.6720 0.7692 0.7737 0.1396  -0.0436 -0.0798 71   PHE D CG  
13271 C  CD1 . PHE D 71   ? 0.6819 0.7736 0.7854 0.1385  -0.0435 -0.0797 71   PHE D CD1 
13272 C  CD2 . PHE D 71   ? 0.7088 0.8072 0.8140 0.1366  -0.0450 -0.0794 71   PHE D CD2 
13273 C  CE1 . PHE D 71   ? 0.7058 0.7930 0.8147 0.1340  -0.0446 -0.0793 71   PHE D CE1 
13274 C  CE2 . PHE D 71   ? 0.6956 0.7906 0.8069 0.1322  -0.0463 -0.0791 71   PHE D CE2 
13275 C  CZ  . PHE D 71   ? 0.6032 0.6925 0.7165 0.1307  -0.0459 -0.0791 71   PHE D CZ  
13276 N  N   . ILE D 72   ? 0.8363 0.9535 0.9311 0.1441  -0.0359 -0.0757 72   ILE D N   
13277 C  CA  . ILE D 72   ? 0.7842 0.9049 0.8792 0.1425  -0.0346 -0.0737 72   ILE D CA  
13278 C  C   . ILE D 72   ? 0.8176 0.9441 0.9162 0.1398  -0.0299 -0.0703 72   ILE D C   
13279 O  O   . ILE D 72   ? 0.8901 1.0176 0.9920 0.1365  -0.0288 -0.0679 72   ILE D O   
13280 C  CB  . ILE D 72   ? 0.7605 0.8820 0.8480 0.1466  -0.0348 -0.0752 72   ILE D CB  
13281 C  CG1 . ILE D 72   ? 0.7406 0.8562 0.8248 0.1487  -0.0400 -0.0789 72   ILE D CG1 
13282 C  CG2 . ILE D 72   ? 0.6574 0.7824 0.7439 0.1455  -0.0324 -0.0727 72   ILE D CG2 
13283 C  CD1 . ILE D 72   ? 0.7427 0.8554 0.8320 0.1452  -0.0434 -0.0791 72   ILE D CD1 
13284 N  N   . LEU D 73   ? 0.7375 0.8679 0.8354 0.1413  -0.0271 -0.0701 73   LEU D N   
13285 C  CA  . LEU D 73   ? 0.7279 0.8643 0.8293 0.1387  -0.0228 -0.0673 73   LEU D CA  
13286 C  C   . LEU D 73   ? 0.6597 0.7945 0.7673 0.1344  -0.0229 -0.0654 73   LEU D C   
13287 O  O   . LEU D 73   ? 0.7556 0.8926 0.8659 0.1311  -0.0205 -0.0628 73   LEU D O   
13288 C  CB  . LEU D 73   ? 0.7193 0.8608 0.8197 0.1412  -0.0204 -0.0680 73   LEU D CB  
13289 C  CG  . LEU D 73   ? 0.7640 0.9127 0.8679 0.1385  -0.0159 -0.0658 73   LEU D CG  
13290 C  CD1 . LEU D 73   ? 0.8045 0.9571 0.9053 0.1383  -0.0124 -0.0647 73   LEU D CD1 
13291 C  CD2 . LEU D 73   ? 0.8499 1.0034 0.9552 0.1407  -0.0150 -0.0669 73   LEU D CD2 
13292 N  N   . GLN D 74   ? 0.7724 0.9026 0.8818 0.1347  -0.0255 -0.0666 74   GLN D N   
13293 C  CA  . GLN D 74   ? 0.7203 0.8484 0.8351 0.1310  -0.0254 -0.0648 74   GLN D CA  
13294 C  C   . GLN D 74   ? 0.7804 0.9058 0.8979 0.1278  -0.0265 -0.0636 74   GLN D C   
13295 O  O   . GLN D 74   ? 0.7949 0.9216 0.9163 0.1244  -0.0246 -0.0610 74   GLN D O   
13296 C  CB  . GLN D 74   ? 0.7704 0.8930 0.8854 0.1323  -0.0277 -0.0664 74   GLN D CB  
13297 C  CG  . GLN D 74   ? 0.8053 0.9306 0.9182 0.1356  -0.0265 -0.0672 74   GLN D CG  
13298 C  CD  . GLN D 74   ? 0.7894 0.9079 0.9013 0.1373  -0.0287 -0.0686 74   GLN D CD  
13299 O  OE1 . GLN D 74   ? 0.6946 0.8117 0.8090 0.1360  -0.0279 -0.0672 74   GLN D OE1 
13300 N  NE2 . GLN D 74   ? 0.8962 1.0097 1.0038 0.1404  -0.0314 -0.0714 74   GLN D NE2 
13301 N  N   . TYR D 75   ? 0.7486 0.8705 0.8642 0.1290  -0.0298 -0.0656 75   TYR D N   
13302 C  CA  . TYR D 75   ? 0.7176 0.8377 0.8363 0.1264  -0.0315 -0.0650 75   TYR D CA  
13303 C  C   . TYR D 75   ? 0.7424 0.8667 0.8606 0.1254  -0.0289 -0.0625 75   TYR D C   
13304 O  O   . TYR D 75   ? 0.7586 0.8830 0.8808 0.1223  -0.0280 -0.0604 75   TYR D O   
13305 C  CB  . TYR D 75   ? 0.6091 0.7253 0.7255 0.1283  -0.0358 -0.0683 75   TYR D CB  
13306 C  CG  . TYR D 75   ? 0.6468 0.7608 0.7682 0.1254  -0.0384 -0.0685 75   TYR D CG  
13307 C  CD1 . TYR D 75   ? 0.6811 0.7980 0.8035 0.1246  -0.0384 -0.0672 75   TYR D CD1 
13308 C  CD2 . TYR D 75   ? 0.7122 0.8211 0.8372 0.1235  -0.0408 -0.0701 75   TYR D CD2 
13309 C  CE1 . TYR D 75   ? 0.7671 0.8830 0.8947 0.1221  -0.0409 -0.0676 75   TYR D CE1 
13310 C  CE2 . TYR D 75   ? 0.8032 0.9109 0.9337 0.1205  -0.0429 -0.0706 75   TYR D CE2 
13311 C  CZ  . TYR D 75   ? 0.8412 0.9530 0.9733 0.1199  -0.0431 -0.0694 75   TYR D CZ  
13312 O  OH  . TYR D 75   ? 0.8448 0.9566 0.9830 0.1172  -0.0453 -0.0700 75   TYR D OH  
13313 N  N   . ILE D 76   ? 0.8221 0.9494 0.9349 0.1281  -0.0273 -0.0628 76   ILE D N   
13314 C  CA  . ILE D 76   ? 0.8354 0.9656 0.9464 0.1273  -0.0244 -0.0603 76   ILE D CA  
13315 C  C   . ILE D 76   ? 0.9130 1.0462 1.0273 0.1241  -0.0202 -0.0574 76   ILE D C   
13316 O  O   . ILE D 76   ? 0.9279 1.0613 1.0435 0.1217  -0.0183 -0.0550 76   ILE D O   
13317 C  CB  . ILE D 76   ? 0.8335 0.9655 0.9373 0.1310  -0.0233 -0.0613 76   ILE D CB  
13318 C  CG1 . ILE D 76   ? 0.8595 0.9881 0.9595 0.1344  -0.0278 -0.0643 76   ILE D CG1 
13319 C  CG2 . ILE D 76   ? 0.7201 0.8540 0.8212 0.1302  -0.0195 -0.0586 76   ILE D CG2 
13320 C  CD1 . ILE D 76   ? 0.8461 0.9726 0.9481 0.1333  -0.0309 -0.0642 76   ILE D CD1 
13321 N  N   . GLY D 77   ? 1.0024 1.1378 1.1177 0.1242  -0.0187 -0.0578 77   GLY D N   
13322 C  CA  . GLY D 77   ? 0.9822 1.1212 1.1000 0.1214  -0.0148 -0.0556 77   GLY D CA  
13323 C  C   . GLY D 77   ? 0.9857 1.1223 1.1087 0.1179  -0.0149 -0.0537 77   GLY D C   
13324 O  O   . GLY D 77   ? 0.9853 1.1231 1.1095 0.1151  -0.0121 -0.0513 77   GLY D O   
13325 N  N   . ASN D 78   ? 0.6747 0.8075 0.8004 0.1179  -0.0178 -0.0548 78   ASN D N   
13326 C  CA  . ASN D 78   ? 0.6636 0.7940 0.7940 0.1148  -0.0176 -0.0531 78   ASN D CA  
13327 C  C   . ASN D 78   ? 0.7219 0.8485 0.8551 0.1134  -0.0198 -0.0528 78   ASN D C   
13328 O  O   . ASN D 78   ? 0.7941 0.9192 0.9312 0.1105  -0.0188 -0.0508 78   ASN D O   
13329 C  CB  . ASN D 78   ? 0.7121 0.8406 0.8438 0.1155  -0.0185 -0.0541 78   ASN D CB  
13330 C  CG  . ASN D 78   ? 0.7376 0.8710 0.8681 0.1165  -0.0162 -0.0541 78   ASN D CG  
13331 O  OD1 . ASN D 78   ? 0.7244 0.8586 0.8528 0.1195  -0.0173 -0.0561 78   ASN D OD1 
13332 N  ND2 . ASN D 78   ? 0.8095 0.9464 0.9413 0.1139  -0.0131 -0.0520 78   ASN D ND2 
13333 N  N   . LEU D 79   ? 0.6746 0.7998 0.8060 0.1153  -0.0227 -0.0548 79   LEU D N   
13334 C  CA  . LEU D 79   ? 0.7058 0.8286 0.8406 0.1140  -0.0252 -0.0550 79   LEU D CA  
13335 C  C   . LEU D 79   ? 0.6713 0.7960 0.8038 0.1151  -0.0257 -0.0546 79   LEU D C   
13336 O  O   . LEU D 79   ? 0.7228 0.8466 0.8581 0.1146  -0.0281 -0.0552 79   LEU D O   
13337 C  CB  . LEU D 79   ? 0.7539 0.8728 0.8894 0.1151  -0.0292 -0.0582 79   LEU D CB  
13338 C  CG  . LEU D 79   ? 0.7192 0.8351 0.8550 0.1152  -0.0290 -0.0590 79   LEU D CG  
13339 C  CD1 . LEU D 79   ? 0.6568 0.7677 0.7924 0.1161  -0.0328 -0.0622 79   LEU D CD1 
13340 C  CD2 . LEU D 79   ? 0.6904 0.8050 0.8305 0.1120  -0.0267 -0.0564 79   LEU D CD2 
13341 N  N   . VAL D 80   ? 0.7345 0.8618 0.8618 0.1168  -0.0232 -0.0538 80   VAL D N   
13342 C  CA  . VAL D 80   ? 0.6842 0.8124 0.8079 0.1184  -0.0233 -0.0532 80   VAL D CA  
13343 C  C   . VAL D 80   ? 0.6829 0.8129 0.8038 0.1173  -0.0184 -0.0502 80   VAL D C   
13344 O  O   . VAL D 80   ? 0.7649 0.8944 0.8869 0.1158  -0.0170 -0.0479 80   VAL D O   
13345 C  CB  . VAL D 80   ? 0.6680 0.7961 0.7859 0.1224  -0.0257 -0.0560 80   VAL D CB  
13346 C  CG1 . VAL D 80   ? 0.6153 0.7438 0.7278 0.1246  -0.0252 -0.0550 80   VAL D CG1 
13347 C  CG2 . VAL D 80   ? 0.7571 0.8827 0.8774 0.1231  -0.0308 -0.0592 80   VAL D CG2 
13348 N  N   . ASP D 81   ? 0.7166 0.8486 0.8338 0.1181  -0.0158 -0.0503 81   ASP D N   
13349 C  CA  . ASP D 81   ? 0.8590 0.9927 0.9731 0.1170  -0.0110 -0.0479 81   ASP D CA  
13350 C  C   . ASP D 81   ? 0.8271 0.9606 0.9453 0.1130  -0.0083 -0.0454 81   ASP D C   
13351 O  O   . ASP D 81   ? 0.8505 0.9828 0.9672 0.1118  -0.0059 -0.0430 81   ASP D O   
13352 C  CB  . ASP D 81   ? 0.8681 1.0050 0.9789 0.1181  -0.0086 -0.0489 81   ASP D CB  
13353 C  CG  . ASP D 81   ? 0.9815 1.1197 1.0880 0.1172  -0.0036 -0.0469 81   ASP D CG  
13354 O  OD1 . ASP D 81   ? 1.0518 1.1871 1.1550 0.1174  -0.0026 -0.0452 81   ASP D OD1 
13355 O  OD2 . ASP D 81   ? 0.9595 1.1014 1.0657 0.1164  -0.0004 -0.0472 81   ASP D OD2 
13356 N  N   . TYR D 82   ? 0.8799 1.0141 1.0029 0.1113  -0.0088 -0.0458 82   TYR D N   
13357 C  CA  . TYR D 82   ? 0.7576 0.8913 0.8843 0.1078  -0.0066 -0.0437 82   TYR D CA  
13358 C  C   . TYR D 82   ? 0.7630 0.8945 0.8949 0.1071  -0.0095 -0.0443 82   TYR D C   
13359 O  O   . TYR D 82   ? 0.7376 0.8697 0.8710 0.1073  -0.0102 -0.0456 82   TYR D O   
13360 C  CB  . TYR D 82   ? 0.8230 0.9601 0.9492 0.1062  -0.0031 -0.0433 82   TYR D CB  
13361 C  CG  . TYR D 82   ? 0.7276 0.8641 0.8545 0.1027  0.0004  -0.0407 82   TYR D CG  
13362 C  CD1 . TYR D 82   ? 0.7809 0.9166 0.9037 0.1019  0.0036  -0.0390 82   TYR D CD1 
13363 C  CD2 . TYR D 82   ? 0.7728 0.9089 0.9036 0.1004  0.0007  -0.0400 82   TYR D CD2 
13364 C  CE1 . TYR D 82   ? 0.7950 0.9293 0.9179 0.0987  0.0069  -0.0368 82   TYR D CE1 
13365 C  CE2 . TYR D 82   ? 0.8311 0.9662 0.9621 0.0973  0.0038  -0.0378 82   TYR D CE2 
13366 C  CZ  . TYR D 82   ? 0.7643 0.8983 0.8913 0.0964  0.0069  -0.0363 82   TYR D CZ  
13367 O  OH  . TYR D 82   ? 0.7194 0.8516 0.8460 0.0932  0.0101  -0.0342 82   TYR D OH  
13368 N  N   . PRO D 83   ? 0.6064 0.7354 0.7412 0.1064  -0.0110 -0.0435 83   PRO D N   
13369 C  CA  . PRO D 83   ? 0.6522 0.7787 0.7920 0.1055  -0.0136 -0.0443 83   PRO D CA  
13370 C  C   . PRO D 83   ? 0.6726 0.7978 0.8156 0.1027  -0.0114 -0.0423 83   PRO D C   
13371 O  O   . PRO D 83   ? 0.6817 0.8051 0.8279 0.1008  -0.0107 -0.0406 83   PRO D O   
13372 C  CB  . PRO D 83   ? 0.7383 0.8638 0.8800 0.1058  -0.0157 -0.0442 83   PRO D CB  
13373 C  CG  . PRO D 83   ? 0.6475 0.7746 0.7838 0.1079  -0.0149 -0.0437 83   PRO D CG  
13374 C  CD  . PRO D 83   ? 0.5643 0.6926 0.6974 0.1068  -0.0107 -0.0421 83   PRO D CD  
13375 N  N   . LEU D 84   ? 0.7462 0.8727 0.8881 0.1027  -0.0102 -0.0428 84   LEU D N   
13376 C  CA  . LEU D 84   ? 0.7914 0.9165 0.9354 0.1006  -0.0084 -0.0413 84   LEU D CA  
13377 C  C   . LEU D 84   ? 0.8966 1.0176 1.0439 0.1004  -0.0105 -0.0418 84   LEU D C   
13378 O  O   . LEU D 84   ? 0.6832 0.8029 0.8300 0.1023  -0.0130 -0.0441 84   LEU D O   
13379 C  CB  . LEU D 84   ? 0.6589 0.7873 0.8008 0.1009  -0.0069 -0.0418 84   LEU D CB  
13380 C  CG  . LEU D 84   ? 0.6608 0.7930 0.8001 0.0998  -0.0038 -0.0409 84   LEU D CG  
13381 C  CD1 . LEU D 84   ? 0.7176 0.8543 0.8559 0.1001  -0.0026 -0.0421 84   LEU D CD1 
13382 C  CD2 . LEU D 84   ? 0.6113 0.7413 0.7515 0.0969  -0.0013 -0.0382 84   LEU D CD2 
13383 N  N   . ASN D 85   ? 1.3198 1.4381 1.4701 0.0982  -0.0092 -0.0398 85   ASN D N   
13384 C  CA  . ASN D 85   ? 1.2924 1.4061 1.4454 0.0975  -0.0101 -0.0398 85   ASN D CA  
13385 C  C   . ASN D 85   ? 1.1936 1.3063 1.3446 0.0979  -0.0088 -0.0395 85   ASN D C   
13386 O  O   . ASN D 85   ? 1.2061 1.3196 1.3565 0.0965  -0.0064 -0.0377 85   ASN D O   
13387 C  CB  . ASN D 85   ? 1.3282 1.4396 1.4852 0.0952  -0.0089 -0.0378 85   ASN D CB  
13388 C  CG  . ASN D 85   ? 1.3411 1.4474 1.5009 0.0942  -0.0091 -0.0376 85   ASN D CG  
13389 O  OD1 . ASN D 85   ? 1.2567 1.3605 1.4166 0.0951  -0.0112 -0.0396 85   ASN D OD1 
13390 N  ND2 . ASN D 85   ? 1.2485 1.3525 1.4102 0.0922  -0.0065 -0.0351 85   ASN D ND2 
13391 N  N   . VAL D 86   ? 0.5391 0.6499 0.6887 0.0999  -0.0107 -0.0414 86   VAL D N   
13392 C  CA  . VAL D 86   ? 0.5281 0.6380 0.6753 0.1012  -0.0101 -0.0415 86   VAL D CA  
13393 C  C   . VAL D 86   ? 0.5326 0.6352 0.6803 0.1014  -0.0107 -0.0414 86   VAL D C   
13394 O  O   . VAL D 86   ? 0.6720 0.7715 0.8196 0.1026  -0.0129 -0.0432 86   VAL D O   
13395 C  CB  . VAL D 86   ? 0.5032 0.6176 0.6473 0.1042  -0.0112 -0.0437 86   VAL D CB  
13396 C  CG1 . VAL D 86   ? 0.5306 0.6518 0.6741 0.1034  -0.0095 -0.0434 86   VAL D CG1 
13397 C  CG2 . VAL D 86   ? 0.6071 0.7202 0.7504 0.1063  -0.0139 -0.0461 86   VAL D CG2 
13398 N  N   . GLY D 87   ? 0.3959 0.4952 0.5439 0.1000  -0.0087 -0.0392 87   GLY D N   
13399 C  CA  . GLY D 87   ? 0.3791 0.4707 0.5268 0.1001  -0.0085 -0.0387 87   GLY D CA  
13400 C  C   . GLY D 87   ? 0.4228 0.5103 0.5746 0.0981  -0.0091 -0.0389 87   GLY D C   
13401 O  O   . GLY D 87   ? 0.5237 0.6044 0.6748 0.0984  -0.0094 -0.0394 87   GLY D O   
13402 N  N   . GLY D 88   ? 0.4442 0.5353 0.5999 0.0961  -0.0093 -0.0387 88   GLY D N   
13403 C  CA  . GLY D 88   ? 0.5208 0.6094 0.6811 0.0943  -0.0103 -0.0395 88   GLY D CA  
13404 C  C   . GLY D 88   ? 0.5637 0.6511 0.7231 0.0958  -0.0135 -0.0427 88   GLY D C   
13405 O  O   . GLY D 88   ? 0.4896 0.5743 0.6528 0.0941  -0.0147 -0.0439 88   GLY D O   
13406 N  N   . ARG D 89   ? 0.6838 0.7733 0.8386 0.0989  -0.0149 -0.0443 89   ARG D N   
13407 C  CA  . ARG D 89   ? 0.7168 0.8050 0.8699 0.1008  -0.0180 -0.0475 89   ARG D CA  
13408 C  C   . ARG D 89   ? 0.8393 0.9319 0.9955 0.0999  -0.0199 -0.0488 89   ARG D C   
13409 O  O   . ARG D 89   ? 0.7788 0.8769 0.9362 0.0993  -0.0190 -0.0474 89   ARG D O   
13410 C  CB  . ARG D 89   ? 0.7677 0.8584 0.9153 0.1047  -0.0187 -0.0487 89   ARG D CB  
13411 C  CG  . ARG D 89   ? 0.7134 0.8004 0.8573 0.1065  -0.0174 -0.0479 89   ARG D CG  
13412 C  CD  . ARG D 89   ? 0.7650 0.8425 0.9076 0.1068  -0.0179 -0.0486 89   ARG D CD  
13413 N  NE  . ARG D 89   ? 0.7549 0.8285 0.8934 0.1088  -0.0164 -0.0473 89   ARG D NE  
13414 C  CZ  . ARG D 89   ? 0.7047 0.7751 0.8439 0.1071  -0.0139 -0.0447 89   ARG D CZ  
13415 N  NH1 . ARG D 89   ? 0.6662 0.7371 0.8105 0.1031  -0.0123 -0.0429 89   ARG D NH1 
13416 N  NH2 . ARG D 89   ? 0.8107 0.8774 0.9451 0.1098  -0.0130 -0.0438 89   ARG D NH2 
13417 N  N   . PRO D 90   ? 0.9142 1.0040 1.0714 0.0999  -0.0227 -0.0515 90   PRO D N   
13418 C  CA  . PRO D 90   ? 0.8886 0.9824 1.0489 0.0991  -0.0249 -0.0529 90   PRO D CA  
13419 C  C   . PRO D 90   ? 0.8949 0.9947 1.0514 0.1020  -0.0258 -0.0536 90   PRO D C   
13420 O  O   . PRO D 90   ? 0.8886 0.9890 1.0400 0.1048  -0.0258 -0.0543 90   PRO D O   
13421 C  CB  . PRO D 90   ? 0.9383 1.0271 1.0995 0.0988  -0.0278 -0.0562 90   PRO D CB  
13422 C  CG  . PRO D 90   ? 0.9269 1.0097 1.0828 0.1009  -0.0274 -0.0568 90   PRO D CG  
13423 C  CD  . PRO D 90   ? 0.7885 0.8708 0.9437 0.1006  -0.0238 -0.0534 90   PRO D CD  
13424 N  N   . LEU D 91   ? 0.8939 0.9982 1.0527 0.1013  -0.0265 -0.0533 91   LEU D N   
13425 C  CA  . LEU D 91   ? 0.8936 1.0028 1.0485 0.1039  -0.0273 -0.0539 91   LEU D CA  
13426 C  C   . LEU D 91   ? 0.9569 1.0663 1.1112 0.1054  -0.0313 -0.0573 91   LEU D C   
13427 O  O   . LEU D 91   ? 0.9186 1.0315 1.0695 0.1077  -0.0322 -0.0579 91   LEU D O   
13428 C  CB  . LEU D 91   ? 0.8305 0.9439 0.9866 0.1029  -0.0251 -0.0511 91   LEU D CB  
13429 C  CG  . LEU D 91   ? 0.8984 1.0127 1.0531 0.1021  -0.0211 -0.0482 91   LEU D CG  
13430 C  CD1 . LEU D 91   ? 0.8393 0.9552 0.9968 0.1001  -0.0189 -0.0453 91   LEU D CD1 
13431 C  CD2 . LEU D 91   ? 0.9538 1.0712 1.1028 0.1045  -0.0202 -0.0485 91   LEU D CD2 
13432 N  N   . ASP D 92   ? 0.9464 1.0515 1.1034 0.1042  -0.0337 -0.0596 92   ASP D N   
13433 C  CA  . ASP D 92   ? 0.8761 0.9809 1.0330 0.1052  -0.0379 -0.0633 92   ASP D CA  
13434 C  C   . ASP D 92   ? 0.8916 0.9922 1.0428 0.1079  -0.0395 -0.0661 92   ASP D C   
13435 O  O   . ASP D 92   ? 0.9175 1.0174 1.0643 0.1098  -0.0374 -0.0650 92   ASP D O   
13436 C  CB  . ASP D 92   ? 0.8973 1.0002 1.0617 0.1015  -0.0394 -0.0645 92   ASP D CB  
13437 C  CG  . ASP D 92   ? 1.0879 1.1942 1.2583 0.0988  -0.0368 -0.0613 92   ASP D CG  
13438 O  OD1 . ASP D 92   ? 1.1653 1.2764 1.3344 0.1001  -0.0358 -0.0593 92   ASP D OD1 
13439 O  OD2 . ASP D 92   ? 1.1173 1.2206 1.2932 0.0954  -0.0357 -0.0607 92   ASP D OD2 
13440 N  N   . ILE D 93   ? 0.5314 0.6294 0.6825 0.1082  -0.0434 -0.0698 93   ILE D N   
13441 C  CA  . ILE D 93   ? 0.4518 0.5442 0.5977 0.1104  -0.0449 -0.0726 93   ILE D CA  
13442 C  C   . ILE D 93   ? 0.4205 0.5058 0.5679 0.1082  -0.0432 -0.0720 93   ILE D C   
13443 O  O   . ILE D 93   ? 0.3554 0.4356 0.4977 0.1105  -0.0433 -0.0732 93   ILE D O   
13444 C  CB  . ILE D 93   ? 0.4200 0.5110 0.5650 0.1111  -0.0497 -0.0770 93   ILE D CB  
13445 C  CG1 . ILE D 93   ? 0.4051 0.4912 0.5425 0.1148  -0.0512 -0.0798 93   ILE D CG1 
13446 C  CG2 . ILE D 93   ? 0.4094 0.4973 0.5617 0.1066  -0.0513 -0.0787 93   ILE D CG2 
13447 C  CD1 . ILE D 93   ? 0.3632 0.4531 0.4938 0.1194  -0.0495 -0.0786 93   ILE D CD1 
13448 N  N   . THR D 94   ? 0.7463 0.8311 0.9003 0.1041  -0.0414 -0.0699 94   THR D N   
13449 C  CA  . THR D 94   ? 0.7811 0.8589 0.9359 0.1022  -0.0390 -0.0687 94   THR D CA  
13450 C  C   . THR D 94   ? 0.8023 0.8796 0.9520 0.1050  -0.0360 -0.0662 94   THR D C   
13451 O  O   . THR D 94   ? 0.8962 0.9669 1.0443 0.1047  -0.0344 -0.0654 94   THR D O   
13452 C  CB  . THR D 94   ? 0.8077 0.8860 0.9705 0.0975  -0.0371 -0.0667 94   THR D CB  
13453 O  OG1 . THR D 94   ? 0.9465 1.0324 1.1116 0.0975  -0.0354 -0.0638 94   THR D OG1 
13454 C  CG2 . THR D 94   ? 0.7693 0.8470 0.9378 0.0944  -0.0401 -0.0699 94   THR D CG2 
13455 N  N   . ASN D 95   ? 0.5880 0.6721 0.7349 0.1077  -0.0354 -0.0650 95   ASN D N   
13456 C  CA  . ASN D 95   ? 0.5613 0.6461 0.7029 0.1109  -0.0334 -0.0637 95   ASN D CA  
13457 C  C   . ASN D 95   ? 0.6266 0.7090 0.7618 0.1151  -0.0354 -0.0667 95   ASN D C   
13458 O  O   . ASN D 95   ? 0.6592 0.7452 0.7902 0.1185  -0.0344 -0.0663 95   ASN D O   
13459 C  CB  . ASN D 95   ? 0.5877 0.6809 0.7294 0.1114  -0.0314 -0.0614 95   ASN D CB  
13460 C  CG  . ASN D 95   ? 0.7308 0.8257 0.8697 0.1132  -0.0287 -0.0595 95   ASN D CG  
13461 O  OD1 . ASN D 95   ? 0.7808 0.8707 0.9191 0.1132  -0.0277 -0.0588 95   ASN D OD1 
13462 N  ND2 . ASN D 95   ? 0.7493 0.8511 0.8864 0.1147  -0.0275 -0.0588 95   ASN D ND2 
13463 N  N   . TRP D 96   ? 0.7538 0.8301 0.8882 0.1149  -0.0382 -0.0698 96   TRP D N   
13464 C  CA  . TRP D 96   ? 0.7593 0.8321 0.8869 0.1192  -0.0401 -0.0728 96   TRP D CA  
13465 C  C   . TRP D 96   ? 0.7137 0.7817 0.8368 0.1220  -0.0383 -0.0720 96   TRP D C   
13466 O  O   . TRP D 96   ? 0.6785 0.7475 0.7957 0.1267  -0.0388 -0.0733 96   TRP D O   
13467 C  CB  . TRP D 96   ? 0.6583 0.7250 0.7859 0.1180  -0.0436 -0.0765 96   TRP D CB  
13468 C  CG  . TRP D 96   ? 0.6981 0.7544 0.8262 0.1158  -0.0435 -0.0774 96   TRP D CG  
13469 C  CD1 . TRP D 96   ? 0.7200 0.7730 0.8545 0.1106  -0.0433 -0.0771 96   TRP D CD1 
13470 C  CD2 . TRP D 96   ? 0.7841 0.8316 0.9056 0.1188  -0.0433 -0.0786 96   TRP D CD2 
13471 N  NE1 . TRP D 96   ? 0.8276 0.8698 0.9598 0.1097  -0.0426 -0.0780 96   TRP D NE1 
13472 C  CE2 . TRP D 96   ? 0.8834 0.9216 1.0073 0.1149  -0.0427 -0.0789 96   TRP D CE2 
13473 C  CE3 . TRP D 96   ? 0.7845 0.8309 0.8982 0.1245  -0.0434 -0.0794 96   TRP D CE3 
13474 C  CZ2 . TRP D 96   ? 0.8872 0.9142 1.0051 0.1167  -0.0422 -0.0798 96   TRP D CZ2 
13475 C  CZ3 . TRP D 96   ? 0.8520 0.8881 0.9602 0.1266  -0.0431 -0.0804 96   TRP D CZ3 
13476 C  CH2 . TRP D 96   ? 0.8511 0.8770 0.9609 0.1228  -0.0425 -0.0806 96   TRP D CH2 
13477 N  N   . PRO D 97   ? 0.6912 0.7541 0.8161 0.1199  -0.0363 -0.0699 97   PRO D N   
13478 C  CA  . PRO D 97   ? 0.7661 0.8269 0.8865 0.1232  -0.0343 -0.0685 97   PRO D CA  
13479 C  C   . PRO D 97   ? 0.7842 0.8552 0.9054 0.1245  -0.0324 -0.0663 97   PRO D C   
13480 O  O   . PRO D 97   ? 0.8151 0.8923 0.9412 0.1215  -0.0315 -0.0646 97   PRO D O   
13481 C  CB  . PRO D 97   ? 0.7912 0.8442 0.9137 0.1201  -0.0324 -0.0666 97   PRO D CB  
13482 C  CG  . PRO D 97   ? 0.8184 0.8674 0.9455 0.1155  -0.0338 -0.0681 97   PRO D CG  
13483 C  CD  . PRO D 97   ? 0.7126 0.7709 0.8433 0.1147  -0.0355 -0.0689 97   PRO D CD  
13484 N  N   . ALA D 98   ? 0.9098 0.9826 1.0262 0.1291  -0.0319 -0.0664 98   ALA D N   
13485 C  CA  . ALA D 98   ? 0.9876 1.0704 1.1043 0.1308  -0.0302 -0.0650 98   ALA D CA  
13486 C  C   . ALA D 98   ? 0.9978 1.0883 1.1142 0.1320  -0.0309 -0.0664 98   ALA D C   
13487 O  O   . ALA D 98   ? 0.9768 1.0760 1.0944 0.1322  -0.0292 -0.0652 98   ALA D O   
13488 C  CB  . ALA D 98   ? 0.9333 1.0198 1.0550 0.1270  -0.0277 -0.0618 98   ALA D CB  
13489 N  N   . MET D 99   ? 0.9445 1.0317 1.0591 0.1326  -0.0334 -0.0690 99   MET D N   
13490 C  CA  . MET D 99   ? 1.0111 1.1042 1.1234 0.1350  -0.0342 -0.0706 99   MET D CA  
13491 C  C   . MET D 99   ? 0.9406 1.0302 1.0465 0.1401  -0.0360 -0.0737 99   MET D C   
13492 O  O   . MET D 99   ? 0.9568 1.0512 1.0598 0.1429  -0.0362 -0.0751 99   MET D O   
13493 C  CB  . MET D 99   ? 0.9219 1.0154 1.0369 0.1318  -0.0357 -0.0711 99   MET D CB  
13494 C  CG  . MET D 99   ? 0.7648 0.8628 0.8855 0.1275  -0.0338 -0.0681 99   MET D CG  
13495 S  SD  . MET D 99   ? 0.7880 0.8865 0.9117 0.1247  -0.0361 -0.0689 99   MET D SD  
13496 C  CE  . MET D 99   ? 0.9760 1.0807 1.0944 0.1286  -0.0363 -0.0702 99   MET D CE  
13497 N  N   . ILE D 100  ? 0.6147 0.6953 0.7178 0.1414  -0.0370 -0.0747 100  ILE D N   
13498 C  CA  . ILE D 100  ? 0.7266 0.8021 0.8228 0.1467  -0.0386 -0.0776 100  ILE D CA  
13499 C  C   . ILE D 100  ? 0.7142 0.7968 0.8074 0.1518  -0.0369 -0.0774 100  ILE D C   
13500 O  O   . ILE D 100  ? 0.6926 0.7770 0.7813 0.1561  -0.0377 -0.0796 100  ILE D O   
13501 C  CB  . ILE D 100  ? 0.6023 0.6653 0.6960 0.1465  -0.0395 -0.0784 100  ILE D CB  
13502 C  CG1 . ILE D 100  ? 0.6686 0.7256 0.7662 0.1409  -0.0410 -0.0790 100  ILE D CG1 
13503 C  CG2 . ILE D 100  ? 0.6275 0.6843 0.7132 0.1522  -0.0411 -0.0814 100  ILE D CG2 
13504 C  CD1 . ILE D 100  ? 0.8047 0.8602 0.9003 0.1412  -0.0441 -0.0824 100  ILE D CD1 
13505 N  N   . PRO D 101  ? 0.8251 0.9120 0.9207 0.1518  -0.0348 -0.0750 101  PRO D N   
13506 C  CA  . PRO D 101  ? 0.7949 0.8886 0.8878 0.1572  -0.0336 -0.0755 101  PRO D CA  
13507 C  C   . PRO D 101  ? 0.7892 0.8941 0.8831 0.1581  -0.0325 -0.0759 101  PRO D C   
13508 O  O   . PRO D 101  ? 0.7988 0.9059 0.8884 0.1632  -0.0328 -0.0780 101  PRO D O   
13509 C  CB  . PRO D 101  ? 0.8403 0.9363 0.9363 0.1559  -0.0319 -0.0729 101  PRO D CB  
13510 C  CG  . PRO D 101  ? 0.8269 0.9126 0.9242 0.1517  -0.0324 -0.0716 101  PRO D CG  
13511 C  CD  . PRO D 101  ? 0.8834 0.9683 0.9833 0.1477  -0.0334 -0.0722 101  PRO D CD  
13512 N  N   . ILE D 102  ? 0.9014 1.0127 1.0004 0.1535  -0.0309 -0.0741 102  ILE D N   
13513 C  CA  . ILE D 102  ? 0.9386 1.0598 1.0382 0.1541  -0.0292 -0.0742 102  ILE D CA  
13514 C  C   . ILE D 102  ? 0.9127 1.0310 1.0074 0.1568  -0.0309 -0.0767 102  ILE D C   
13515 O  O   . ILE D 102  ? 0.9946 1.1187 1.0865 0.1604  -0.0298 -0.0780 102  ILE D O   
13516 C  CB  . ILE D 102  ? 0.9052 1.0313 1.0102 0.1484  -0.0273 -0.0717 102  ILE D CB  
13517 C  CG1 . ILE D 102  ? 0.9595 1.0875 1.0687 0.1459  -0.0258 -0.0694 102  ILE D CG1 
13518 C  CG2 . ILE D 102  ? 0.8076 0.9431 0.9126 0.1489  -0.0249 -0.0717 102  ILE D CG2 
13519 C  CD1 . ILE D 102  ? 0.9621 1.1007 1.0731 0.1472  -0.0233 -0.0690 102  ILE D CD1 
13520 N  N   . THR D 103  ? 0.6085 0.7178 0.7020 0.1549  -0.0335 -0.0777 103  THR D N   
13521 C  CA  . THR D 103  ? 0.7573 0.8629 0.8457 0.1574  -0.0357 -0.0804 103  THR D CA  
13522 C  C   . THR D 103  ? 0.8480 0.9503 0.9300 0.1637  -0.0366 -0.0830 103  THR D C   
13523 O  O   . THR D 103  ? 0.8305 0.9354 0.9080 0.1676  -0.0366 -0.0848 103  THR D O   
13524 C  CB  . THR D 103  ? 0.7864 0.8833 0.8757 0.1539  -0.0387 -0.0812 103  THR D CB  
13525 O  OG1 . THR D 103  ? 0.6267 0.7277 0.7212 0.1490  -0.0379 -0.0791 103  THR D OG1 
13526 C  CG2 . THR D 103  ? 0.8435 0.9352 0.9269 0.1568  -0.0416 -0.0847 103  THR D CG2 
13527 N  N   . PHE D 104  ? 0.8174 0.9135 0.8984 0.1650  -0.0373 -0.0831 104  PHE D N   
13528 C  CA  . PHE D 104  ? 0.7723 0.8641 0.8466 0.1714  -0.0382 -0.0855 104  PHE D CA  
13529 C  C   . PHE D 104  ? 0.8080 0.9108 0.8816 0.1760  -0.0358 -0.0854 104  PHE D C   
13530 O  O   . PHE D 104  ? 0.9133 1.0167 0.9815 0.1813  -0.0360 -0.0877 104  PHE D O   
13531 C  CB  . PHE D 104  ? 0.6457 0.7282 0.7187 0.1718  -0.0390 -0.0852 104  PHE D CB  
13532 C  CG  . PHE D 104  ? 0.8065 0.8841 0.8720 0.1789  -0.0397 -0.0873 104  PHE D CG  
13533 C  CD1 . PHE D 104  ? 0.9243 0.9911 0.9831 0.1812  -0.0421 -0.0903 104  PHE D CD1 
13534 C  CD2 . PHE D 104  ? 0.8499 0.9335 0.9150 0.1834  -0.0380 -0.0865 104  PHE D CD2 
13535 C  CE1 . PHE D 104  ? 1.0021 1.0636 1.0533 0.1881  -0.0426 -0.0922 104  PHE D CE1 
13536 C  CE2 . PHE D 104  ? 0.8927 0.9718 0.9506 0.1905  -0.0387 -0.0885 104  PHE D CE2 
13537 C  CZ  . PHE D 104  ? 0.9834 1.0511 1.0341 0.1929  -0.0408 -0.0912 104  PHE D CZ  
13538 N  N   . GLU D 105  ? 0.9568 1.0687 1.0361 0.1741  -0.0333 -0.0830 105  GLU D N   
13539 C  CA  . GLU D 105  ? 0.9880 1.1115 1.0680 0.1780  -0.0309 -0.0832 105  GLU D CA  
13540 C  C   . GLU D 105  ? 1.0678 1.1986 1.1472 0.1784  -0.0293 -0.0839 105  GLU D C   
13541 O  O   . GLU D 105  ? 1.0865 1.2233 1.1632 0.1834  -0.0280 -0.0854 105  GLU D O   
13542 C  CB  . GLU D 105  ? 1.0863 1.2179 1.1729 0.1749  -0.0288 -0.0807 105  GLU D CB  
13543 C  CG  . GLU D 105  ? 1.1233 1.2481 1.2098 0.1752  -0.0301 -0.0798 105  GLU D CG  
13544 C  CD  . GLU D 105  ? 1.1780 1.3008 1.2592 0.1825  -0.0310 -0.0816 105  GLU D CD  
13545 O  OE1 . GLU D 105  ? 1.1905 1.3205 1.2699 0.1873  -0.0302 -0.0834 105  GLU D OE1 
13546 O  OE2 . GLU D 105  ? 1.1573 1.2710 1.2358 0.1837  -0.0323 -0.0813 105  GLU D OE2 
13547 N  N   . SER D 106  ? 1.1029 1.2330 1.1843 0.1734  -0.0292 -0.0828 106  SER D N   
13548 C  CA  . SER D 106  ? 1.1564 1.2921 1.2361 0.1739  -0.0274 -0.0832 106  SER D CA  
13549 C  C   . SER D 106  ? 1.1709 1.3008 1.2427 0.1791  -0.0294 -0.0862 106  SER D C   
13550 O  O   . SER D 106  ? 1.1507 1.2865 1.2195 0.1828  -0.0275 -0.0872 106  SER D O   
13551 C  CB  . SER D 106  ? 1.0591 1.1943 1.1419 0.1680  -0.0272 -0.0813 106  SER D CB  
13552 O  OG  . SER D 106  ? 1.0962 1.2361 1.1856 0.1633  -0.0253 -0.0786 106  SER D OG  
13553 N  N   . GLY D 107  ? 0.8720 0.9903 0.9404 0.1793  -0.0331 -0.0877 107  GLY D N   
13554 C  CA  . GLY D 107  ? 0.8603 0.9719 0.9207 0.1841  -0.0353 -0.0909 107  GLY D CA  
13555 C  C   . GLY D 107  ? 0.9372 1.0506 0.9932 0.1911  -0.0344 -0.0926 107  GLY D C   
13556 O  O   . GLY D 107  ? 1.0385 1.1530 1.0888 0.1958  -0.0340 -0.0945 107  GLY D O   
13557 N  N   . ILE D 108  ? 0.6302 0.7437 0.6883 0.1922  -0.0342 -0.0918 108  ILE D N   
13558 C  CA  . ILE D 108  ? 0.6234 0.7390 0.6775 0.1994  -0.0335 -0.0934 108  ILE D CA  
13559 C  C   . ILE D 108  ? 0.6612 0.7911 0.7175 0.2018  -0.0298 -0.0931 108  ILE D C   
13560 O  O   . ILE D 108  ? 0.7418 0.8739 0.7931 0.2081  -0.0291 -0.0951 108  ILE D O   
13561 C  CB  . ILE D 108  ? 0.6543 0.7673 0.7103 0.2001  -0.0340 -0.0924 108  ILE D CB  
13562 C  CG1 . ILE D 108  ? 0.5821 0.6799 0.6353 0.1978  -0.0371 -0.0928 108  ILE D CG1 
13563 C  CG2 . ILE D 108  ? 0.7017 0.8180 0.7536 0.2081  -0.0333 -0.0940 108  ILE D CG2 
13564 C  CD1 . ILE D 108  ? 0.6197 0.7059 0.6637 0.2023  -0.0395 -0.0960 108  ILE D CD1 
13565 N  N   . LEU D 109  ? 0.7268 0.8665 0.7905 0.1967  -0.0272 -0.0907 109  LEU D N   
13566 C  CA  . LEU D 109  ? 0.8102 0.9638 0.8768 0.1980  -0.0232 -0.0903 109  LEU D CA  
13567 C  C   . LEU D 109  ? 0.8449 0.9987 0.9060 0.2003  -0.0221 -0.0917 109  LEU D C   
13568 O  O   . LEU D 109  ? 0.8572 1.0176 0.9160 0.2056  -0.0199 -0.0931 109  LEU D O   
13569 C  CB  . LEU D 109  ? 0.7568 0.9188 0.8319 0.1912  -0.0207 -0.0875 109  LEU D CB  
13570 C  CG  . LEU D 109  ? 0.7390 0.9153 0.8180 0.1911  -0.0161 -0.0871 109  LEU D CG  
13571 C  CD1 . LEU D 109  ? 0.8536 1.0384 0.9333 0.1971  -0.0150 -0.0887 109  LEU D CD1 
13572 C  CD2 . LEU D 109  ? 0.6729 0.8556 0.7595 0.1840  -0.0138 -0.0844 109  LEU D CD2 
13573 N  N   . LEU D 110  ? 0.9704 1.1173 1.0293 0.1968  -0.0235 -0.0913 110  LEU D N   
13574 C  CA  . LEU D 110  ? 1.0021 1.1485 1.0549 0.1992  -0.0226 -0.0925 110  LEU D CA  
13575 C  C   . LEU D 110  ? 1.0352 1.1745 1.0793 0.2063  -0.0248 -0.0958 110  LEU D C   
13576 O  O   . LEU D 110  ? 1.1119 1.2550 1.1512 0.2109  -0.0227 -0.0970 110  LEU D O   
13577 C  CB  . LEU D 110  ? 0.9872 1.1274 1.0393 0.1942  -0.0244 -0.0916 110  LEU D CB  
13578 C  CG  . LEU D 110  ? 0.9584 1.1063 1.0161 0.1887  -0.0209 -0.0886 110  LEU D CG  
13579 C  CD1 . LEU D 110  ? 0.9880 1.1300 1.0423 0.1862  -0.0225 -0.0883 110  LEU D CD1 
13580 C  CD2 . LEU D 110  ? 0.7487 0.9084 0.8075 0.1905  -0.0156 -0.0881 110  LEU D CD2 
13581 N  N   . ALA D 111  ? 0.8252 0.9536 0.8666 0.2072  -0.0289 -0.0972 111  ALA D N   
13582 C  CA  . ALA D 111  ? 0.8275 0.9476 0.8600 0.2139  -0.0311 -0.1004 111  ALA D CA  
13583 C  C   . ALA D 111  ? 0.8424 0.9702 0.8738 0.2206  -0.0285 -0.1011 111  ALA D C   
13584 O  O   . ALA D 111  ? 0.8605 0.9879 0.8850 0.2267  -0.0278 -0.1033 111  ALA D O   
13585 C  CB  . ALA D 111  ? 0.7566 0.8631 0.7869 0.2128  -0.0354 -0.1015 111  ALA D CB  
13586 N  N   . SER D 112  ? 0.9993 1.1346 1.0376 0.2199  -0.0270 -0.0995 112  SER D N   
13587 C  CA  . SER D 112  ? 1.0122 1.1562 1.0504 0.2264  -0.0248 -0.1004 112  SER D CA  
13588 C  C   . SER D 112  ? 1.0248 1.1821 1.0649 0.2277  -0.0203 -0.1003 112  SER D C   
13589 O  O   . SER D 112  ? 1.0770 1.2380 1.1127 0.2346  -0.0188 -0.1022 112  SER D O   
13590 C  CB  . SER D 112  ? 1.1592 1.3088 1.2047 0.2250  -0.0246 -0.0989 112  SER D CB  
13591 O  OG  . SER D 112  ? 1.2531 1.3897 1.2958 0.2246  -0.0283 -0.0990 112  SER D OG  
13592 N  N   . PHE D 113  ? 0.9399 1.1041 0.9860 0.2212  -0.0178 -0.0981 113  PHE D N   
13593 C  CA  . PHE D 113  ? 0.8828 1.0586 0.9303 0.2217  -0.0130 -0.0977 113  PHE D CA  
13594 C  C   . PHE D 113  ? 0.8959 1.0658 0.9336 0.2264  -0.0129 -0.0996 113  PHE D C   
13595 O  O   . PHE D 113  ? 0.9780 1.1557 1.0139 0.2310  -0.0093 -0.1005 113  PHE D O   
13596 C  CB  . PHE D 113  ? 0.8641 1.0453 0.9183 0.2136  -0.0105 -0.0949 113  PHE D CB  
13597 C  CG  . PHE D 113  ? 0.8351 1.0285 0.8994 0.2102  -0.0080 -0.0933 113  PHE D CG  
13598 C  CD1 . PHE D 113  ? 0.8933 1.0927 0.9606 0.2143  -0.0084 -0.0944 113  PHE D CD1 
13599 C  CD2 . PHE D 113  ? 0.7615 0.9602 0.8320 0.2029  -0.0053 -0.0908 113  PHE D CD2 
13600 C  CE1 . PHE D 113  ? 1.0790 1.2901 1.1556 0.2112  -0.0065 -0.0933 113  PHE D CE1 
13601 C  CE2 . PHE D 113  ? 0.8775 1.0871 0.9571 0.1995  -0.0032 -0.0897 113  PHE D CE2 
13602 C  CZ  . PHE D 113  ? 1.0753 1.2915 1.1582 0.2036  -0.0039 -0.0911 113  PHE D CZ  
13603 N  N   . ALA D 114  ? 0.7062 0.8626 0.7378 0.2252  -0.0168 -0.1003 114  ALA D N   
13604 C  CA  . ALA D 114  ? 0.7995 0.9494 0.8211 0.2295  -0.0174 -0.1024 114  ALA D CA  
13605 C  C   . ALA D 114  ? 0.8420 0.9890 0.8565 0.2381  -0.0181 -0.1053 114  ALA D C   
13606 O  O   . ALA D 114  ? 0.8127 0.9613 0.8208 0.2432  -0.0159 -0.1067 114  ALA D O   
13607 C  CB  . ALA D 114  ? 0.7553 0.8917 0.7725 0.2261  -0.0221 -0.1029 114  ALA D CB  
13608 N  N   . ALA D 115  ? 0.9267 1.0691 0.9417 0.2402  -0.0209 -0.1062 115  ALA D N   
13609 C  CA  . ALA D 115  ? 0.8345 0.9729 0.8421 0.2489  -0.0217 -0.1089 115  ALA D CA  
13610 C  C   . ALA D 115  ? 0.8369 0.9903 0.8473 0.2540  -0.0169 -0.1090 115  ALA D C   
13611 O  O   . ALA D 115  ? 0.9609 1.1142 0.9640 0.2609  -0.0155 -0.1110 115  ALA D O   
13612 C  CB  . ALA D 115  ? 0.7732 0.9027 0.7805 0.2497  -0.0254 -0.1095 115  ALA D CB  
13613 N  N   . ALA D 116  ? 1.0977 1.2641 1.1186 0.2508  -0.0142 -0.1069 116  ALA D N   
13614 C  CA  . ALA D 116  ? 1.1185 1.3008 1.1437 0.2551  -0.0097 -0.1072 116  ALA D CA  
13615 C  C   . ALA D 116  ? 1.1780 1.3678 1.2024 0.2545  -0.0049 -0.1068 116  ALA D C   
13616 O  O   . ALA D 116  ? 1.2331 1.4277 1.2533 0.2612  -0.0021 -0.1084 116  ALA D O   
13617 C  CB  . ALA D 116  ? 1.1029 1.2974 1.1399 0.2510  -0.0084 -0.1054 116  ALA D CB  
13618 N  N   . ILE D 117  ? 0.7984 0.9888 0.8262 0.2469  -0.0036 -0.1046 117  ILE D N   
13619 C  CA  . ILE D 117  ? 0.7674 0.9633 0.7934 0.2461  0.0012  -0.1039 117  ILE D CA  
13620 C  C   . ILE D 117  ? 0.8744 1.0590 0.8876 0.2516  -0.0002 -0.1059 117  ILE D C   
13621 O  O   . ILE D 117  ? 1.0260 1.2156 1.0350 0.2558  0.0040  -0.1066 117  ILE D O   
13622 C  CB  . ILE D 117  ? 0.7967 0.9935 0.8280 0.2370  0.0025  -0.1010 117  ILE D CB  
13623 C  CG1 . ILE D 117  ? 0.7326 0.9414 0.7764 0.2316  0.0043  -0.0991 117  ILE D CG1 
13624 C  CG2 . ILE D 117  ? 0.8114 1.0115 0.8390 0.2364  0.0074  -0.1001 117  ILE D CG2 
13625 C  CD1 . ILE D 117  ? 0.6903 0.8995 0.7390 0.2228  0.0057  -0.0963 117  ILE D CD1 
13626 N  N   . GLY D 118  ? 0.9557 1.1249 0.9624 0.2518  -0.0060 -0.1072 118  GLY D N   
13627 C  CA  . GLY D 118  ? 1.0380 1.1957 1.0322 0.2567  -0.0080 -0.1095 118  GLY D CA  
13628 C  C   . GLY D 118  ? 1.1320 1.2906 1.1197 0.2662  -0.0069 -0.1121 118  GLY D C   
13629 O  O   . GLY D 118  ? 1.1490 1.3064 1.1284 0.2709  -0.0048 -0.1134 118  GLY D O   
13630 N  N   . MET D 119  ? 1.1570 1.3173 1.1476 0.2696  -0.0083 -0.1130 119  MET D N   
13631 C  CA  . MET D 119  ? 1.0853 1.2472 1.0701 0.2792  -0.0070 -0.1154 119  MET D CA  
13632 C  C   . MET D 119  ? 1.1390 1.3168 1.1269 0.2818  -0.0003 -0.1149 119  MET D C   
13633 O  O   . MET D 119  ? 1.2419 1.4191 1.2217 0.2892  0.0017  -0.1168 119  MET D O   
13634 C  CB  . MET D 119  ? 1.0079 1.1706 0.9964 0.2820  -0.0093 -0.1160 119  MET D CB  
13635 C  CG  . MET D 119  ? 1.1318 1.2938 1.1130 0.2927  -0.0089 -0.1187 119  MET D CG  
13636 S  SD  . MET D 119  ? 1.3706 1.5551 1.3616 0.2966  -0.0033 -0.1180 119  MET D SD  
13637 C  CE  . MET D 119  ? 1.3750 1.5671 1.3797 0.2892  -0.0047 -0.1157 119  MET D CE  
13638 N  N   . ILE D 120  ? 1.0406 1.2325 1.0401 0.2758  0.0035  -0.1124 120  ILE D N   
13639 C  CA  . ILE D 120  ? 1.0768 1.2845 1.0806 0.2771  0.0105  -0.1117 120  ILE D CA  
13640 C  C   . ILE D 120  ? 1.1139 1.3173 1.1097 0.2768  0.0134  -0.1113 120  ILE D C   
13641 O  O   . ILE D 120  ? 1.2067 1.4148 1.1976 0.2827  0.0176  -0.1124 120  ILE D O   
13642 C  CB  . ILE D 120  ? 1.0403 1.2629 1.0585 0.2698  0.0135  -0.1093 120  ILE D CB  
13643 C  CG1 . ILE D 120  ? 1.0507 1.2782 1.0760 0.2713  0.0107  -0.1100 120  ILE D CG1 
13644 C  CG2 . ILE D 120  ? 1.0667 1.3053 1.0898 0.2699  0.0212  -0.1087 120  ILE D CG2 
13645 C  CD1 . ILE D 120  ? 1.0875 1.3274 1.1263 0.2637  0.0124  -0.1079 120  ILE D CD1 
13646 N  N   . VAL D 121  ? 0.9224 1.1168 0.9164 0.2704  0.0111  -0.1098 121  VAL D N   
13647 C  CA  . VAL D 121  ? 0.8995 1.0901 0.8859 0.2697  0.0139  -0.1091 121  VAL D CA  
13648 C  C   . VAL D 121  ? 1.0292 1.2068 1.0011 0.2774  0.0111  -0.1120 121  VAL D C   
13649 O  O   . VAL D 121  ? 1.0917 1.2705 1.0563 0.2818  0.0151  -0.1125 121  VAL D O   
13650 C  CB  . VAL D 121  ? 0.8574 1.0427 0.8463 0.2610  0.0121  -0.1067 121  VAL D CB  
13651 C  CG1 . VAL D 121  ? 0.8601 1.0391 0.8392 0.2615  0.0139  -0.1062 121  VAL D CG1 
13652 C  CG2 . VAL D 121  ? 0.9618 1.1602 0.9641 0.2537  0.0159  -0.1039 121  VAL D CG2 
13653 N  N   . LEU D 122  ? 1.0840 1.2485 1.0512 0.2788  0.0042  -0.1140 122  LEU D N   
13654 C  CA  . LEU D 122  ? 1.0644 1.2152 1.0175 0.2855  0.0009  -0.1171 122  LEU D CA  
13655 C  C   . LEU D 122  ? 1.0679 1.2237 1.0159 0.2950  0.0044  -0.1191 122  LEU D C   
13656 O  O   . LEU D 122  ? 1.1466 1.2971 1.0834 0.3006  0.0056  -0.1207 122  LEU D O   
13657 C  CB  . LEU D 122  ? 0.9693 1.1058 0.9196 0.2848  -0.0067 -0.1190 122  LEU D CB  
13658 C  CG  . LEU D 122  ? 0.9176 1.0447 0.8683 0.2773  -0.0113 -0.1183 122  LEU D CG  
13659 C  CD1 . LEU D 122  ? 0.9955 1.1094 0.9442 0.2767  -0.0181 -0.1204 122  LEU D CD1 
13660 C  CD2 . LEU D 122  ? 0.8715 0.9920 0.8120 0.2784  -0.0114 -0.1190 122  LEU D CD2 
13661 N  N   . ASN D 123  ? 1.0967 1.2628 1.0527 0.2973  0.0061  -0.1191 123  ASN D N   
13662 C  CA  . ASN D 123  ? 1.1539 1.3267 1.1065 0.3065  0.0097  -0.1209 123  ASN D CA  
13663 C  C   . ASN D 123  ? 1.0963 1.2839 1.0521 0.3069  0.0178  -0.1194 123  ASN D C   
13664 O  O   . ASN D 123  ? 1.1503 1.3434 1.1032 0.3125  0.0211  -0.1199 123  ASN D O   
13665 C  CB  . ASN D 123  ? 1.2016 1.3812 1.1617 0.3087  0.0086  -0.1212 123  ASN D CB  
13666 C  CG  . ASN D 123  ? 1.2261 1.3895 1.1786 0.3121  0.0018  -0.1234 123  ASN D CG  
13667 O  OD1 . ASN D 123  ? 1.2268 1.3750 1.1674 0.3152  -0.0015 -0.1257 123  ASN D OD1 
13668 N  ND2 . ASN D 123  ? 1.1851 1.3511 1.1437 0.3113  -0.0002 -0.1227 123  ASN D ND2 
13669 N  N   . GLY D 124  ? 0.9863 1.1787 0.9474 0.2991  0.0207  -0.1166 124  GLY D N   
13670 C  CA  . GLY D 124  ? 1.0703 1.2783 1.0371 0.2982  0.0290  -0.1148 124  GLY D CA  
13671 C  C   . GLY D 124  ? 1.0872 1.3126 1.0664 0.2994  0.0322  -0.1149 124  GLY D C   
13672 O  O   . GLY D 124  ? 1.1428 1.3787 1.1234 0.3012  0.0379  -0.1143 124  GLY D O   
13673 N  N   . LEU D 125  ? 2.2713 2.4981 2.2589 0.2960  0.0279  -0.1147 125  LEU D N   
13674 C  CA  . LEU D 125  ? 2.3429 2.5822 2.3400 0.2960  0.0287  -0.1143 125  LEU D CA  
13675 C  C   . LEU D 125  ? 2.4503 2.7092 2.4593 0.2916  0.0360  -0.1126 125  LEU D C   
13676 O  O   . LEU D 125  ? 2.4860 2.7550 2.4982 0.2941  0.0387  -0.1128 125  LEU D O   
13677 C  CB  . LEU D 125  ? 2.3640 2.5999 2.3671 0.2933  0.0227  -0.1144 125  LEU D CB  
13678 C  CG  . LEU D 125  ? 2.4616 2.7021 2.4678 0.2963  0.0207  -0.1148 125  LEU D CG  
13679 C  CD1 . LEU D 125  ? 2.4192 2.6519 2.4131 0.3045  0.0200  -0.1164 125  LEU D CD1 
13680 C  CD2 . LEU D 125  ? 2.4208 2.6535 2.4292 0.2945  0.0143  -0.1149 125  LEU D CD2 
13681 N  N   . PRO D 126  ? 1.3975 1.6627 1.4135 0.2850  0.0397  -0.1111 126  PRO D N   
13682 C  CA  . PRO D 126  ? 1.4148 1.6987 1.4423 0.2805  0.0470  -0.1097 126  PRO D CA  
13683 C  C   . PRO D 126  ? 1.4706 1.7592 1.4929 0.2844  0.0534  -0.1097 126  PRO D C   
13684 O  O   . PRO D 126  ? 1.5258 1.8164 1.5463 0.2823  0.0594  -0.1085 126  PRO D O   
13685 C  CB  . PRO D 126  ? 1.3347 1.6179 1.3665 0.2714  0.0488  -0.1072 126  PRO D CB  
13686 C  CG  . PRO D 126  ? 1.2534 1.5188 1.2789 0.2693  0.0410  -0.1068 126  PRO D CG  
13687 C  CD  . PRO D 126  ? 1.1899 1.4429 1.2026 0.2784  0.0370  -0.1093 126  PRO D CD  
13688 N  N   . SER D 127  ? 1.1706 1.4605 1.1900 0.2902  0.0524  -0.1109 127  SER D N   
13689 C  CA  . SER D 127  ? 1.1450 1.4392 1.1593 0.2947  0.0581  -0.1110 127  SER D CA  
13690 C  C   . SER D 127  ? 1.0879 1.3977 1.1121 0.2955  0.0599  -0.1114 127  SER D C   
13691 O  O   . SER D 127  ? 1.0005 1.3067 1.0195 0.3020  0.0565  -0.1127 127  SER D O   
13692 C  CB  . SER D 127  ? 1.1133 1.3903 1.1105 0.3027  0.0547  -0.1124 127  SER D CB  
13693 O  OG  . SER D 127  ? 1.1530 1.4202 1.1465 0.3062  0.0468  -0.1139 127  SER D OG  
13694 N  N   . PRO D 128  ? 1.1953 1.5225 1.2337 0.2891  0.0650  -0.1105 128  PRO D N   
13695 C  CA  . PRO D 128  ? 1.2520 1.5953 1.3004 0.2899  0.0668  -0.1112 128  PRO D CA  
13696 C  C   . PRO D 128  ? 1.3208 1.6660 1.3627 0.2965  0.0707  -0.1118 128  PRO D C   
13697 O  O   . PRO D 128  ? 1.3166 1.6671 1.3601 0.3011  0.0689  -0.1129 128  PRO D O   
13698 C  CB  . PRO D 128  ? 1.3210 1.6811 1.3846 0.2809  0.0727  -0.1102 128  PRO D CB  
13699 C  CG  . PRO D 128  ? 1.2563 1.6079 1.3193 0.2755  0.0706  -0.1091 128  PRO D CG  
13700 C  CD  . PRO D 128  ? 1.2203 1.5531 1.2667 0.2807  0.0688  -0.1090 128  PRO D CD  
13701 N  N   . TYR D 129  ? 1.7739 2.1143 1.8077 0.2975  0.0762  -0.1110 129  TYR D N   
13702 C  CA  . TYR D 129  ? 1.7377 2.0793 1.7645 0.3035  0.0808  -0.1113 129  TYR D CA  
13703 C  C   . TYR D 129  ? 1.7693 2.0904 1.7776 0.3108  0.0766  -0.1120 129  TYR D C   
13704 O  O   . TYR D 129  ? 1.7713 2.0794 1.7720 0.3095  0.0743  -0.1115 129  TYR D O   
13705 C  CB  . TYR D 129  ? 1.7846 2.1359 1.8154 0.2991  0.0908  -0.1099 129  TYR D CB  
13706 C  CG  . TYR D 129  ? 1.7810 2.1305 1.8022 0.3051  0.0964  -0.1098 129  TYR D CG  
13707 C  CD1 . TYR D 129  ? 1.7649 2.0974 1.7693 0.3095  0.0962  -0.1094 129  TYR D CD1 
13708 C  CD2 . TYR D 129  ? 1.7483 2.1134 1.7774 0.3062  0.1018  -0.1102 129  TYR D CD2 
13709 C  CE1 . TYR D 129  ? 1.8149 2.1454 1.8100 0.3151  0.1013  -0.1093 129  TYR D CE1 
13710 C  CE2 . TYR D 129  ? 1.7648 2.1283 1.7853 0.3117  0.1072  -0.1101 129  TYR D CE2 
13711 C  CZ  . TYR D 129  ? 1.8289 2.1749 1.8321 0.3161  0.1069  -0.1095 129  TYR D CZ  
13712 O  OH  . TYR D 129  ? 1.9158 2.2598 1.9099 0.3216  0.1122  -0.1093 129  TYR D OH  
13713 N  N   . HIS D 130  ? 1.2815 1.6000 1.2826 0.3186  0.0754  -0.1131 130  HIS D N   
13714 C  CA  . HIS D 130  ? 1.1907 1.4905 1.1740 0.3259  0.0719  -0.1141 130  HIS D CA  
13715 C  C   . HIS D 130  ? 1.2166 1.5210 1.1954 0.3325  0.0760  -0.1145 130  HIS D C   
13716 O  O   . HIS D 130  ? 1.2496 1.5683 1.2383 0.3332  0.0775  -0.1149 130  HIS D O   
13717 C  CB  . HIS D 130  ? 1.1856 1.4718 1.1629 0.3292  0.0623  -0.1155 130  HIS D CB  
13718 C  CG  . HIS D 130  ? 1.1456 1.4105 1.1058 0.3335  0.0581  -0.1165 130  HIS D CG  
13719 N  ND1 . HIS D 130  ? 1.1465 1.3997 1.0935 0.3417  0.0548  -0.1181 130  HIS D ND1 
13720 C  CD2 . HIS D 130  ? 1.1015 1.3548 1.0554 0.3309  0.0565  -0.1163 130  HIS D CD2 
13721 C  CE1 . HIS D 130  ? 1.1827 1.4181 1.1164 0.3436  0.0512  -0.1191 130  HIS D CE1 
13722 N  NE2 . HIS D 130  ? 1.0766 1.3119 1.0142 0.3372  0.0521  -0.1180 130  HIS D NE2 
13723 N  N   . PRO D 131  ? 0.9434 1.2364 0.9076 0.3375  0.0780  -0.1146 131  PRO D N   
13724 C  CA  . PRO D 131  ? 1.0156 1.3118 0.9745 0.3445  0.0817  -0.1151 131  PRO D CA  
13725 C  C   . PRO D 131  ? 1.0382 1.3337 0.9962 0.3505  0.0761  -0.1167 131  PRO D C   
13726 O  O   . PRO D 131  ? 1.0603 1.3669 1.0220 0.3541  0.0795  -0.1170 131  PRO D O   
13727 C  CB  . PRO D 131  ? 1.0542 1.3329 0.9947 0.3491  0.0818  -0.1152 131  PRO D CB  
13728 C  CG  . PRO D 131  ? 1.0481 1.3220 0.9888 0.3426  0.0825  -0.1141 131  PRO D CG  
13729 C  CD  . PRO D 131  ? 0.9439 1.2210 0.8958 0.3371  0.0770  -0.1143 131  PRO D CD  
13730 N  N   . VAL D 132  ? 1.4231 1.7057 1.3762 0.3515  0.0677  -0.1178 132  VAL D N   
13731 C  CA  . VAL D 132  ? 1.4189 1.6976 1.3688 0.3576  0.0619  -0.1193 132  VAL D CA  
13732 C  C   . VAL D 132  ? 1.4364 1.7350 1.4013 0.3566  0.0639  -0.1191 132  VAL D C   
13733 O  O   . VAL D 132  ? 1.4614 1.7628 1.4240 0.3631  0.0634  -0.1200 132  VAL D O   
13734 C  CB  . VAL D 132  ? 1.4178 1.6808 1.3627 0.3566  0.0533  -0.1202 132  VAL D CB  
13735 C  CG1 . VAL D 132  ? 1.4215 1.6836 1.3669 0.3609  0.0480  -0.1212 132  VAL D CG1 
13736 C  CG2 . VAL D 132  ? 1.4498 1.6917 1.3771 0.3603  0.0504  -0.1212 132  VAL D CG2 
13737 N  N   . PHE D 133  ? 1.5706 1.8835 1.5511 0.3485  0.0663  -0.1181 133  PHE D N   
13738 C  CA  . PHE D 133  ? 1.5736 1.9054 1.5690 0.3470  0.0673  -0.1183 133  PHE D CA  
13739 C  C   . PHE D 133  ? 1.5718 1.9179 1.5708 0.3504  0.0742  -0.1184 133  PHE D C   
13740 O  O   . PHE D 133  ? 1.5683 1.9280 1.5764 0.3520  0.0740  -0.1191 133  PHE D O   
13741 C  CB  . PHE D 133  ? 1.5768 1.9209 1.5879 0.3370  0.0690  -0.1173 133  PHE D CB  
13742 C  CG  . PHE D 133  ? 1.5355 1.8683 1.5456 0.3334  0.0621  -0.1172 133  PHE D CG  
13743 C  CD1 . PHE D 133  ? 1.5152 1.8419 1.5232 0.3367  0.0548  -0.1181 133  PHE D CD1 
13744 C  CD2 . PHE D 133  ? 1.5108 1.8392 1.5219 0.3268  0.0633  -0.1161 133  PHE D CD2 
13745 C  CE1 . PHE D 133  ? 1.5049 1.8211 1.5121 0.3332  0.0489  -0.1179 133  PHE D CE1 
13746 C  CE2 . PHE D 133  ? 1.5102 1.8287 1.5209 0.3234  0.0572  -0.1160 133  PHE D CE2 
13747 C  CZ  . PHE D 133  ? 1.4862 1.7986 1.4952 0.3265  0.0500  -0.1169 133  PHE D CZ  
13748 N  N   . ASN D 134  ? 1.6239 1.9671 1.6159 0.3518  0.0802  -0.1178 134  ASN D N   
13749 C  CA  . ASN D 134  ? 1.6124 1.9694 1.6084 0.3546  0.0874  -0.1178 134  ASN D CA  
13750 C  C   . ASN D 134  ? 1.6405 1.9968 1.6308 0.3639  0.0844  -0.1192 134  ASN D C   
13751 O  O   . ASN D 134  ? 1.6149 1.9874 1.6137 0.3658  0.0886  -0.1196 134  ASN D O   
13752 C  CB  . ASN D 134  ? 1.5378 1.8883 1.5241 0.3553  0.0939  -0.1168 134  ASN D CB  
13753 C  CG  . ASN D 134  ? 1.5561 1.9187 1.5538 0.3464  0.1017  -0.1153 134  ASN D CG  
13754 O  OD1 . ASN D 134  ? 1.6059 1.9874 1.6200 0.3413  0.1053  -0.1153 134  ASN D OD1 
13755 N  ND2 . ASN D 134  ? 1.6623 2.0136 1.6507 0.3444  0.1043  -0.1141 134  ASN D ND2 
13756 N  N   . VAL D 135  ? 1.2509 1.5885 1.2270 0.3699  0.0772  -0.1200 135  VAL D N   
13757 C  CA  . VAL D 135  ? 1.2335 1.5686 1.2030 0.3789  0.0738  -0.1213 135  VAL D CA  
13758 C  C   . VAL D 135  ? 1.3224 1.6740 1.3065 0.3776  0.0719  -0.1218 135  VAL D C   
13759 O  O   . VAL D 135  ? 1.3611 1.7143 1.3531 0.3717  0.0680  -0.1216 135  VAL D O   
13760 C  CB  . VAL D 135  ? 1.2242 1.5355 1.1767 0.3840  0.0659  -0.1221 135  VAL D CB  
13761 C  CG1 . VAL D 135  ? 1.1162 1.4246 1.0625 0.3929  0.0620  -0.1233 135  VAL D CG1 
13762 C  CG2 . VAL D 135  ? 1.2890 1.5845 1.2264 0.3862  0.0677  -0.1220 135  VAL D CG2 
13763 N  N   . PRO D 136  ? 1.5679 1.9323 1.5560 0.3829  0.0743  -0.1226 136  PRO D N   
13764 C  CA  . PRO D 136  ? 1.5478 1.9307 1.5515 0.3808  0.0732  -0.1232 136  PRO D CA  
13765 C  C   . PRO D 136  ? 1.4995 1.8738 1.5003 0.3827  0.0644  -0.1238 136  PRO D C   
13766 O  O   . PRO D 136  ? 1.4489 1.8330 1.4621 0.3769  0.0624  -0.1237 136  PRO D O   
13767 C  CB  . PRO D 136  ? 1.5188 1.9139 1.5239 0.3879  0.0773  -0.1240 136  PRO D CB  
13768 C  CG  . PRO D 136  ? 1.5106 1.8881 1.4969 0.3957  0.0774  -0.1240 136  PRO D CG  
13769 C  CD  . PRO D 136  ? 1.5608 1.9249 1.5405 0.3905  0.0786  -0.1229 136  PRO D CD  
13770 N  N   . ARG D 137  ? 1.7841 2.1401 1.7687 0.3905  0.0593  -0.1243 137  ARG D N   
13771 C  CA  . ARG D 137  ? 1.8914 2.2388 1.8723 0.3931  0.0515  -0.1248 137  ARG D CA  
13772 C  C   . ARG D 137  ? 1.9205 2.2526 1.8978 0.3875  0.0467  -0.1242 137  ARG D C   
13773 O  O   . ARG D 137  ? 1.9577 2.2796 1.9302 0.3895  0.0403  -0.1245 137  ARG D O   
13774 C  CB  . ARG D 137  ? 1.8194 2.1535 1.7843 0.4039  0.0482  -0.1257 137  ARG D CB  
13775 C  CG  . ARG D 137  ? 1.7251 2.0750 1.6945 0.4104  0.0508  -0.1264 137  ARG D CG  
13776 C  CD  . ARG D 137  ? 1.7723 2.1081 1.7257 0.4212  0.0468  -0.1272 137  ARG D CD  
13777 N  NE  . ARG D 137  ? 1.8183 2.1354 1.7624 0.4218  0.0394  -0.1273 137  ARG D NE  
13778 C  CZ  . ARG D 137  ? 1.7979 2.1178 1.7457 0.4228  0.0347  -0.1275 137  ARG D CZ  
13779 N  NH1 . ARG D 137  ? 1.7874 2.1282 1.7480 0.4233  0.0360  -0.1279 137  ARG D NH1 
13780 N  NH2 . ARG D 137  ? 1.7696 2.0708 1.7078 0.4232  0.0286  -0.1274 137  ARG D NH2 
13781 N  N   . PHE D 138  ? 1.2943 1.6242 1.2736 0.3807  0.0498  -0.1233 138  PHE D N   
13782 C  CA  . PHE D 138  ? 1.2103 1.5280 1.1882 0.3749  0.0454  -0.1228 138  PHE D CA  
13783 C  C   . PHE D 138  ? 1.2567 1.5869 1.2498 0.3681  0.0436  -0.1224 138  PHE D C   
13784 O  O   . PHE D 138  ? 1.2673 1.5876 1.2595 0.3642  0.0390  -0.1220 138  PHE D O   
13785 C  CB  . PHE D 138  ? 1.2264 1.5384 1.2018 0.3698  0.0491  -0.1220 138  PHE D CB  
13786 C  CG  . PHE D 138  ? 1.2521 1.5447 1.2191 0.3672  0.0438  -0.1220 138  PHE D CG  
13787 C  CD1 . PHE D 138  ? 1.1786 1.4502 1.1284 0.3734  0.0396  -0.1230 138  PHE D CD1 
13788 C  CD2 . PHE D 138  ? 1.3429 1.6382 1.3192 0.3587  0.0429  -0.1211 138  PHE D CD2 
13789 C  CE1 . PHE D 138  ? 1.1633 1.4175 1.1061 0.3708  0.0346  -0.1232 138  PHE D CE1 
13790 C  CE2 . PHE D 138  ? 1.2567 1.5347 1.2258 0.3564  0.0381  -0.1212 138  PHE D CE2 
13791 C  CZ  . PHE D 138  ? 1.1838 1.4414 1.1364 0.3623  0.0339  -0.1223 138  PHE D CZ  
13792 N  N   . GLN D 139  ? 1.8001 2.1519 1.8071 0.3667  0.0470  -0.1226 139  GLN D N   
13793 C  CA  . GLN D 139  ? 1.7756 2.1389 1.7959 0.3614  0.0445  -0.1226 139  GLN D CA  
13794 C  C   . GLN D 139  ? 1.7790 2.1321 1.7924 0.3666  0.0370  -0.1231 139  GLN D C   
13795 O  O   . GLN D 139  ? 1.8598 2.2117 1.8781 0.3622  0.0329  -0.1227 139  GLN D O   
13796 C  CB  . GLN D 139  ? 1.7847 2.1731 1.8207 0.3596  0.0494  -0.1231 139  GLN D CB  
13797 C  CG  . GLN D 139  ? 1.8244 2.2188 1.8567 0.3686  0.0507  -0.1242 139  GLN D CG  
13798 C  CD  . GLN D 139  ? 1.9046 2.3246 1.9534 0.3664  0.0555  -0.1251 139  GLN D CD  
13799 O  OE1 . GLN D 139  ? 1.8339 2.2670 1.8968 0.3593  0.0555  -0.1252 139  GLN D OE1 
13800 N  NE2 . GLN D 139  ? 1.9512 2.3785 1.9984 0.3725  0.0597  -0.1257 139  GLN D NE2 
13801 N  N   . TYR D 140  ? 1.5331 1.8780 1.5345 0.3760  0.0353  -0.1238 140  TYR D N   
13802 C  CA  . TYR D 140  ? 1.5337 1.8669 1.5265 0.3817  0.0286  -0.1242 140  TYR D CA  
13803 C  C   . TYR D 140  ? 1.5608 1.8687 1.5393 0.3821  0.0242  -0.1239 140  TYR D C   
13804 O  O   . TYR D 140  ? 1.6002 1.8955 1.5699 0.3868  0.0189  -0.1242 140  TYR D O   
13805 C  CB  . TYR D 140  ? 1.5282 1.8632 1.5139 0.3919  0.0287  -0.1252 140  TYR D CB  
13806 C  CG  . TYR D 140  ? 1.5624 1.9221 1.5613 0.3922  0.0338  -0.1258 140  TYR D CG  
13807 C  CD1 . TYR D 140  ? 1.4527 1.8301 1.4657 0.3892  0.0328  -0.1263 140  TYR D CD1 
13808 C  CD2 . TYR D 140  ? 1.6391 2.0042 1.6363 0.3954  0.0395  -0.1261 140  TYR D CD2 
13809 C  CE1 . TYR D 140  ? 1.5266 1.9269 1.5523 0.3893  0.0374  -0.1271 140  TYR D CE1 
13810 C  CE2 . TYR D 140  ? 1.6708 2.0585 1.6805 0.3955  0.0444  -0.1268 140  TYR D CE2 
13811 C  CZ  . TYR D 140  ? 1.6955 2.1010 1.7198 0.3923  0.0433  -0.1274 140  TYR D CZ  
13812 O  OH  . TYR D 140  ? 1.6637 2.0922 1.7011 0.3921  0.0482  -0.1283 140  TYR D OH  
13813 N  N   . ALA D 141  ? 1.3503 1.6505 1.3263 0.3774  0.0262  -0.1234 141  ALA D N   
13814 C  CA  . ALA D 141  ? 1.3687 1.6452 1.3314 0.3779  0.0220  -0.1235 141  ALA D CA  
13815 C  C   . ALA D 141  ? 1.4156 1.6852 1.3805 0.3741  0.0165  -0.1231 141  ALA D C   
13816 O  O   . ALA D 141  ? 1.4039 1.6537 1.3570 0.3767  0.0118  -0.1235 141  ALA D O   
13817 C  CB  . ALA D 141  ? 1.2850 1.5569 1.2462 0.3730  0.0252  -0.1232 141  ALA D CB  
13818 N  N   . SER D 142  ? 1.5011 1.7863 1.4810 0.3679  0.0171  -0.1224 142  SER D N   
13819 C  CA  . SER D 142  ? 1.4094 1.6886 1.3916 0.3644  0.0121  -0.1218 142  SER D CA  
13820 C  C   . SER D 142  ? 1.4763 1.7525 1.4534 0.3713  0.0080  -0.1223 142  SER D C   
13821 O  O   . SER D 142  ? 1.4785 1.7414 1.4504 0.3713  0.0032  -0.1220 142  SER D O   
13822 C  CB  . SER D 142  ? 1.3969 1.6933 1.3962 0.3555  0.0140  -0.1210 142  SER D CB  
13823 O  OG  . SER D 142  ? 1.3519 1.6463 1.3540 0.3486  0.0166  -0.1204 142  SER D OG  
13824 N  N   . GLN D 143  ? 1.4466 1.7344 1.4245 0.3775  0.0099  -0.1230 143  GLN D N   
13825 C  CA  . GLN D 143  ? 1.4670 1.7522 1.4389 0.3852  0.0062  -0.1234 143  GLN D CA  
13826 C  C   . GLN D 143  ? 1.4678 1.7401 1.4241 0.3942  0.0063  -0.1242 143  GLN D C   
13827 O  O   . GLN D 143  ? 1.4271 1.7105 1.3845 0.3986  0.0099  -0.1248 143  GLN D O   
13828 C  CB  . GLN D 143  ? 1.4866 1.7953 1.4713 0.3859  0.0077  -0.1239 143  GLN D CB  
13829 C  CG  . GLN D 143  ? 1.3946 1.7207 1.3969 0.3766  0.0088  -0.1234 143  GLN D CG  
13830 C  CD  . GLN D 143  ? 1.3752 1.7156 1.3884 0.3704  0.0150  -0.1234 143  GLN D CD  
13831 O  OE1 . GLN D 143  ? 1.3883 1.7193 1.3972 0.3675  0.0171  -0.1229 143  GLN D OE1 
13832 N  NE2 . GLN D 143  ? 1.3941 1.7573 1.4214 0.3683  0.0181  -0.1240 143  GLN D NE2 
13833 N  N   . ASP D 144  ? 1.9961 2.2451 1.9380 0.3970  0.0025  -0.1243 144  ASP D N   
13834 C  CA  . ASP D 144  ? 1.9883 2.2218 1.9138 0.4050  0.0022  -0.1252 144  ASP D CA  
13835 C  C   . ASP D 144  ? 2.0575 2.2947 1.9836 0.4031  0.0070  -0.1255 144  ASP D C   
13836 O  O   . ASP D 144  ? 2.0884 2.3276 2.0214 0.3953  0.0086  -0.1250 144  ASP D O   
13837 C  CB  . ASP D 144  ? 2.0290 2.2671 1.9499 0.4143  0.0015  -0.1256 144  ASP D CB  
13838 C  CG  . ASP D 144  ? 2.1709 2.3888 2.0777 0.4199  -0.0036 -0.1257 144  ASP D CG  
13839 O  OD1 . ASP D 144  ? 2.1791 2.3762 2.0760 0.4183  -0.0060 -0.1258 144  ASP D OD1 
13840 O  OD2 . ASP D 144  ? 2.2280 2.4507 2.1335 0.4259  -0.0052 -0.1257 144  ASP D OD2 
13841 N  N   . ALA D 145  ? 1.8657 2.1035 1.7845 0.4103  0.0095  -0.1262 145  ALA D N   
13842 C  CA  . ALA D 145  ? 1.8455 2.0884 1.7647 0.4095  0.0147  -0.1265 145  ALA D CA  
13843 C  C   . ALA D 145  ? 1.8573 2.0850 1.7708 0.4044  0.0141  -0.1265 145  ALA D C   
13844 O  O   . ALA D 145  ? 1.8314 2.0672 1.7544 0.3970  0.0169  -0.1259 145  ALA D O   
13845 C  CB  . ALA D 145  ? 1.8211 2.0902 1.7580 0.4049  0.0199  -0.1259 145  ALA D CB  
13846 N  N   . PHE D 146  ? 1.5048 1.7097 1.4023 0.4086  0.0103  -0.1275 146  PHE D N   
13847 C  CA  . PHE D 146  ? 1.4707 1.6596 1.3609 0.4049  0.0092  -0.1281 146  PHE D CA  
13848 C  C   . PHE D 146  ? 1.5193 1.7099 1.4048 0.4069  0.0137  -0.1286 146  PHE D C   
13849 O  O   . PHE D 146  ? 1.6656 1.8611 1.5469 0.4136  0.0163  -0.1289 146  PHE D O   
13850 C  CB  . PHE D 146  ? 1.4401 1.6039 1.3148 0.4085  0.0036  -0.1292 146  PHE D CB  
13851 C  CG  . PHE D 146  ? 1.4865 1.6467 1.3637 0.4076  -0.0007 -0.1287 146  PHE D CG  
13852 C  CD1 . PHE D 146  ? 1.5122 1.6791 1.3898 0.4134  -0.0013 -0.1282 146  PHE D CD1 
13853 C  CD2 . PHE D 146  ? 1.5019 1.6516 1.3805 0.4012  -0.0040 -0.1285 146  PHE D CD2 
13854 C  CE1 . PHE D 146  ? 1.5437 1.7067 1.4227 0.4128  -0.0051 -0.1276 146  PHE D CE1 
13855 C  CE2 . PHE D 146  ? 1.5242 1.6700 1.4046 0.4005  -0.0076 -0.1278 146  PHE D CE2 
13856 C  CZ  . PHE D 146  ? 1.5054 1.6576 1.3856 0.4064  -0.0081 -0.1273 146  PHE D CZ  
13857 N  N   . PHE D 147  ? 1.2307 1.4173 1.1168 0.4011  0.0147  -0.1286 147  PHE D N   
13858 C  CA  . PHE D 147  ? 1.2367 1.4263 1.1196 0.4019  0.0195  -0.1287 147  PHE D CA  
13859 C  C   . PHE D 147  ? 1.2620 1.4308 1.1317 0.4013  0.0168  -0.1301 147  PHE D C   
13860 O  O   . PHE D 147  ? 1.2255 1.3814 1.0929 0.3978  0.0120  -0.1308 147  PHE D O   
13861 C  CB  . PHE D 147  ? 1.2232 1.4331 1.1221 0.3947  0.0250  -0.1272 147  PHE D CB  
13862 C  CG  . PHE D 147  ? 1.2910 1.5229 1.2010 0.3964  0.0298  -0.1263 147  PHE D CG  
13863 C  CD1 . PHE D 147  ? 1.2829 1.5255 1.2028 0.3959  0.0279  -0.1259 147  PHE D CD1 
13864 C  CD2 . PHE D 147  ? 1.3697 1.6118 1.2806 0.3985  0.0361  -0.1261 147  PHE D CD2 
13865 C  CE1 . PHE D 147  ? 1.3037 1.5672 1.2345 0.3974  0.0320  -0.1255 147  PHE D CE1 
13866 C  CE2 . PHE D 147  ? 1.4156 1.6786 1.3377 0.3997  0.0406  -0.1255 147  PHE D CE2 
13867 C  CZ  . PHE D 147  ? 1.3346 1.6086 1.2669 0.3991  0.0384  -0.1254 147  PHE D CZ  
13868 N  N   . LEU D 148  ? 1.4633 1.6290 1.3243 0.4049  0.0200  -0.1307 148  LEU D N   
13869 C  CA  . LEU D 148  ? 1.4681 1.6166 1.3171 0.4043  0.0181  -0.1322 148  LEU D CA  
13870 C  C   . LEU D 148  ? 1.4638 1.6206 1.3126 0.4044  0.0243  -0.1315 148  LEU D C   
13871 O  O   . LEU D 148  ? 1.5105 1.6783 1.3603 0.4089  0.0290  -0.1308 148  LEU D O   
13872 C  CB  . LEU D 148  ? 1.5232 1.6502 1.3541 0.4115  0.0135  -0.1344 148  LEU D CB  
13873 C  CG  . LEU D 148  ? 1.4450 1.5539 1.2619 0.4119  0.0115  -0.1365 148  LEU D CG  
13874 C  CD1 . LEU D 148  ? 1.4848 1.5857 1.3048 0.4044  0.0076  -0.1371 148  LEU D CD1 
13875 C  CD2 . LEU D 148  ? 1.3623 1.4518 1.1616 0.4195  0.0077  -0.1387 148  LEU D CD2 
13876 N  N   . CYS D 149  ? 1.4193 1.5706 1.2665 0.3995  0.0243  -0.1317 149  CYS D N   
13877 C  CA  . CYS D 149  ? 1.4679 1.6269 1.3153 0.3986  0.0304  -0.1308 149  CYS D CA  
13878 C  C   . CYS D 149  ? 1.5687 1.7100 1.4024 0.3987  0.0280  -0.1324 149  CYS D C   
13879 O  O   . CYS D 149  ? 1.5566 1.6856 1.3878 0.3952  0.0224  -0.1337 149  CYS D O   
13880 C  CB  . CYS D 149  ? 1.3183 1.4964 1.1833 0.3907  0.0351  -0.1285 149  CYS D CB  
13881 S  SG  . CYS D 149  ? 1.4473 1.6325 1.3121 0.3883  0.0427  -0.1271 149  CYS D SG  
13882 N  N   . ILE D 150  ? 1.4685 1.6089 1.2934 0.4027  0.0321  -0.1324 150  ILE D N   
13883 C  CA  . ILE D 150  ? 1.4166 1.5421 1.2282 0.4032  0.0305  -0.1338 150  ILE D CA  
13884 C  C   . ILE D 150  ? 1.3810 1.5184 1.1978 0.3997  0.0376  -0.1316 150  ILE D C   
13885 O  O   . ILE D 150  ? 1.2874 1.4364 1.1062 0.4025  0.0442  -0.1301 150  ILE D O   
13886 C  CB  . ILE D 150  ? 1.3788 1.4895 1.1723 0.4117  0.0288  -0.1358 150  ILE D CB  
13887 C  CG1 . ILE D 150  ? 1.4141 1.5150 1.2033 0.4157  0.0231  -0.1375 150  ILE D CG1 
13888 C  CG2 . ILE D 150  ? 1.4274 1.5210 1.2068 0.4118  0.0256  -0.1378 150  ILE D CG2 
13889 C  CD1 . ILE D 150  ? 1.4596 1.5439 1.2303 0.4238  0.0207  -0.1398 150  ILE D CD1 
13890 N  N   . GLU D 151  ? 1.8405 1.9747 1.6592 0.3937  0.0364  -0.1315 151  GLU D N   
13891 C  CA  . GLU D 151  ? 1.8487 1.9939 1.6730 0.3897  0.0432  -0.1292 151  GLU D CA  
13892 C  C   . GLU D 151  ? 1.8541 1.9906 1.6629 0.3945  0.0459  -0.1295 151  GLU D C   
13893 O  O   . GLU D 151  ? 1.8962 2.0158 1.6896 0.3997  0.0410  -0.1320 151  GLU D O   
13894 C  CB  . GLU D 151  ? 1.8447 1.9889 1.6756 0.3819  0.0407  -0.1288 151  GLU D CB  
13895 C  CG  . GLU D 151  ? 1.8251 1.9772 1.6711 0.3767  0.0380  -0.1284 151  GLU D CG  
13896 C  CD  . GLU D 151  ? 1.8376 1.9829 1.6863 0.3706  0.0333  -0.1290 151  GLU D CD  
13897 O  OE1 . GLU D 151  ? 1.8638 1.9984 1.7027 0.3705  0.0320  -0.1299 151  GLU D OE1 
13898 O  OE2 . GLU D 151  ? 1.8600 2.0104 1.7203 0.3660  0.0308  -0.1286 151  GLU D OE2 
13899 N  N   . ALA D 152  ? 1.3797 1.5279 1.1928 0.3925  0.0539  -0.1270 152  ALA D N   
13900 C  CA  . ALA D 152  ? 1.3715 1.5119 1.1703 0.3963  0.0572  -0.1268 152  ALA D CA  
13901 C  C   . ALA D 152  ? 1.3842 1.5088 1.1725 0.3946  0.0520  -0.1283 152  ALA D C   
13902 O  O   . ALA D 152  ? 1.4662 1.5787 1.2387 0.3992  0.0515  -0.1292 152  ALA D O   
13903 C  CB  . ALA D 152  ? 1.3689 1.5256 1.1757 0.3937  0.0675  -0.1235 152  ALA D CB  
13904 N  N   . THR D 153  ? 1.5975 1.7221 1.3942 0.3882  0.0481  -0.1285 153  THR D N   
13905 C  CA  . THR D 153  ? 1.6439 1.7541 1.4318 0.3864  0.0425  -0.1303 153  THR D CA  
13906 C  C   . THR D 153  ? 1.7125 1.8033 1.4853 0.3917  0.0341  -0.1342 153  THR D C   
13907 O  O   . THR D 153  ? 1.7751 1.8525 1.5374 0.3917  0.0295  -0.1362 153  THR D O   
13908 C  CB  . THR D 153  ? 1.7118 1.8268 1.5131 0.3786  0.0398  -0.1298 153  THR D CB  
13909 O  OG1 . THR D 153  ? 1.7505 1.8653 1.5588 0.3781  0.0346  -0.1313 153  THR D OG1 
13910 C  CG2 . THR D 153  ? 1.7102 1.8440 1.5262 0.3731  0.0481  -0.1261 153  THR D CG2 
13911 N  N   . ASP D 154  ? 2.4838 2.5727 2.2553 0.3960  0.0321  -0.1354 154  ASP D N   
13912 C  CA  . ASP D 154  ? 2.5591 2.6295 2.3154 0.4014  0.0251  -0.1391 154  ASP D CA  
13913 C  C   . ASP D 154  ? 2.6341 2.6946 2.3734 0.4064  0.0263  -0.1399 154  ASP D C   
13914 O  O   . ASP D 154  ? 2.6841 2.7529 2.4219 0.4094  0.0336  -0.1375 154  ASP D O   
13915 C  CB  . ASP D 154  ? 2.5912 2.6633 2.3484 0.4061  0.0249  -0.1395 154  ASP D CB  
13916 C  CG  . ASP D 154  ? 2.6220 2.6744 2.3639 0.4115  0.0177  -0.1433 154  ASP D CG  
13917 O  OD1 . ASP D 154  ? 2.6505 2.6887 2.3778 0.4139  0.0146  -0.1456 154  ASP D OD1 
13918 O  OD2 . ASP D 154  ? 2.5877 2.6384 2.3318 0.4133  0.0151  -0.1441 154  ASP D OD2 
13919 N  N   . PRO D 155  ? 1.7893 1.8327 1.5161 0.4072  0.0194  -0.1432 155  PRO D N   
13920 C  CA  . PRO D 155  ? 1.7785 1.8121 1.4885 0.4120  0.0200  -0.1439 155  PRO D CA  
13921 C  C   . PRO D 155  ? 1.7628 1.7953 1.4632 0.4197  0.0237  -0.1436 155  PRO D C   
13922 O  O   . PRO D 155  ? 1.7583 1.7903 1.4495 0.4231  0.0282  -0.1422 155  PRO D O   
13923 C  CB  . PRO D 155  ? 1.7117 1.7262 1.4108 0.4119  0.0101  -0.1486 155  PRO D CB  
13924 C  CG  . PRO D 155  ? 1.7862 1.7996 1.4955 0.4080  0.0048  -0.1503 155  PRO D CG  
13925 C  CD  . PRO D 155  ? 1.7344 1.7671 1.4622 0.4032  0.0108  -0.1463 155  PRO D CD  
13926 N  N   . LEU D 156  ? 1.6920 1.7236 1.3939 0.4227  0.0219  -0.1446 156  LEU D N   
13927 C  CA  . LEU D 156  ? 1.7282 1.7587 1.4211 0.4304  0.0252  -0.1443 156  LEU D CA  
13928 C  C   . LEU D 156  ? 1.8274 1.8755 1.5274 0.4310  0.0355  -0.1401 156  LEU D C   
13929 O  O   . LEU D 156  ? 1.9402 1.9860 1.6293 0.4363  0.0396  -0.1394 156  LEU D O   
13930 C  CB  . LEU D 156  ? 1.6731 1.7012 1.3682 0.4331  0.0218  -0.1458 156  LEU D CB  
13931 C  CG  . LEU D 156  ? 1.6589 1.6684 1.3464 0.4325  0.0120  -0.1501 156  LEU D CG  
13932 C  CD1 . LEU D 156  ? 1.5929 1.5991 1.2809 0.4358  0.0095  -0.1511 156  LEU D CD1 
13933 C  CD2 . LEU D 156  ? 1.6265 1.6182 1.2950 0.4363  0.0078  -0.1532 156  LEU D CD2 
13934 N  N   . PHE D 157  ? 2.3665 2.4321 2.0847 0.4255  0.0399  -0.1374 157  PHE D N   
13935 C  CA  . PHE D 157  ? 2.4199 2.5035 2.1472 0.4247  0.0500  -0.1336 157  PHE D CA  
13936 C  C   . PHE D 157  ? 2.3914 2.4781 2.1134 0.4322  0.0543  -0.1332 157  PHE D C   
13937 O  O   . PHE D 157  ? 2.3743 2.4676 2.0939 0.4345  0.0618  -0.1310 157  PHE D O   
13938 C  CB  . PHE D 157  ? 2.4081 2.4911 2.1306 0.4224  0.0541  -0.1319 157  PHE D CB  
13939 C  CG  . PHE D 157  ? 2.3572 2.4584 2.0959 0.4157  0.0617  -0.1284 157  PHE D CG  
13940 C  CD1 . PHE D 157  ? 2.3769 2.4962 2.1295 0.4149  0.0684  -0.1262 157  PHE D CD1 
13941 C  CD2 . PHE D 157  ? 2.3135 2.4136 2.0533 0.4102  0.0621  -0.1274 157  PHE D CD2 
13942 C  CE1 . PHE D 157  ? 2.4315 2.5675 2.1993 0.4083  0.0753  -0.1232 157  PHE D CE1 
13943 C  CE2 . PHE D 157  ? 2.2987 2.4148 2.0530 0.4038  0.0692  -0.1241 157  PHE D CE2 
13944 C  CZ  . PHE D 157  ? 2.3919 2.5260 2.1604 0.4027  0.0759  -0.1221 157  PHE D CZ  
13945 N  N   . ASP D 158  ? 2.7418 2.8234 2.4618 0.4362  0.0496  -0.1352 158  ASP D N   
13946 C  CA  . ASP D 158  ? 2.8064 2.8866 2.5178 0.4445  0.0520  -0.1354 158  ASP D CA  
13947 C  C   . ASP D 158  ? 2.7008 2.8023 2.4254 0.4449  0.0609  -0.1324 158  ASP D C   
13948 O  O   . ASP D 158  ? 2.7214 2.8248 2.4394 0.4511  0.0657  -0.1317 158  ASP D O   
13949 C  CB  . ASP D 158  ? 2.8951 2.9634 2.6006 0.4484  0.0445  -0.1383 158  ASP D CB  
13950 C  CG  . ASP D 158  ? 2.9356 2.9814 2.6256 0.4493  0.0360  -0.1419 158  ASP D CG  
13951 O  OD1 . ASP D 158  ? 2.9263 2.9648 2.6068 0.4491  0.0361  -0.1422 158  ASP D OD1 
13952 O  OD2 . ASP D 158  ? 2.9669 3.0022 2.6541 0.4501  0.0292  -0.1444 158  ASP D OD2 
13953 N  N   . ARG D 159  ? 1.5583 1.6759 1.3016 0.4383  0.0632  -0.1307 159  ARG D N   
13954 C  CA  . ARG D 159  ? 1.5672 1.7063 1.3253 0.4377  0.0709  -0.1283 159  ARG D CA  
13955 C  C   . ARG D 159  ? 1.5697 1.7102 1.3259 0.4450  0.0699  -0.1293 159  ARG D C   
13956 O  O   . ARG D 159  ? 1.5373 1.6786 1.2996 0.4445  0.0650  -0.1303 159  ARG D O   
13957 C  CB  . ARG D 159  ? 1.5839 1.7313 1.3413 0.4378  0.0803  -0.1259 159  ARG D CB  
13958 C  CG  . ARG D 159  ? 1.5979 1.7692 1.3738 0.4345  0.0887  -0.1235 159  ARG D CG  
13959 C  CD  . ARG D 159  ? 1.6773 1.8562 1.4540 0.4323  0.0983  -0.1210 159  ARG D CD  
13960 N  NE  . ARG D 159  ? 1.7702 1.9719 1.5644 0.4295  0.1065  -0.1191 159  ARG D NE  
13961 C  CZ  . ARG D 159  ? 1.7004 1.9169 1.5122 0.4211  0.1095  -0.1178 159  ARG D CZ  
13962 N  NH1 . ARG D 159  ? 1.6832 1.8946 1.4976 0.4148  0.1051  -0.1178 159  ARG D NH1 
13963 N  NH2 . ARG D 159  ? 1.6111 1.8482 1.4383 0.4189  0.1169  -0.1165 159  ARG D NH2 
13964 N  N   . SER D 160  ? 1.8423 1.9831 1.5899 0.4518  0.0747  -0.1289 160  SER D N   
13965 C  CA  . SER D 160  ? 1.8128 1.9569 1.5593 0.4590  0.0748  -0.1295 160  SER D CA  
13966 C  C   . SER D 160  ? 1.7723 1.8969 1.5057 0.4637  0.0656  -0.1324 160  SER D C   
13967 O  O   . SER D 160  ? 1.7728 1.9000 1.5094 0.4670  0.0631  -0.1331 160  SER D O   
13968 C  CB  . SER D 160  ? 1.7575 1.9051 1.4967 0.4653  0.0821  -0.1285 160  SER D CB  
13969 O  OG  . SER D 160  ? 1.9031 2.0323 1.6233 0.4687  0.0804  -0.1294 160  SER D OG  
13970 N  N   . ARG D 161  ? 1.8976 2.0023 1.6158 0.4642  0.0605  -0.1342 161  ARG D N   
13971 C  CA  . ARG D 161  ? 1.8822 1.9676 1.5884 0.4675  0.0515  -0.1372 161  ARG D CA  
13972 C  C   . ARG D 161  ? 1.9483 2.0353 1.6660 0.4616  0.0462  -0.1378 161  ARG D C   
13973 O  O   . ARG D 161  ? 1.9413 2.0210 1.6560 0.4648  0.0413  -0.1393 161  ARG D O   
13974 C  CB  . ARG D 161  ? 1.9161 1.9812 1.6051 0.4682  0.0472  -0.1393 161  ARG D CB  
13975 C  CG  . ARG D 161  ? 2.0449 2.1045 1.7193 0.4750  0.0512  -0.1391 161  ARG D CG  
13976 C  CD  . ARG D 161  ? 2.0914 2.1282 1.7470 0.4769  0.0447  -0.1421 161  ARG D CD  
13977 N  NE  . ARG D 161  ? 2.1676 2.1877 1.8130 0.4808  0.0370  -0.1453 161  ARG D NE  
13978 C  CZ  . ARG D 161  ? 2.1196 2.1282 1.7645 0.4766  0.0292  -0.1478 161  ARG D CZ  
13979 N  NH1 . ARG D 161  ? 2.0485 2.0605 1.7027 0.4686  0.0277  -0.1476 161  ARG D NH1 
13980 N  NH2 . ARG D 161  ? 1.9753 1.9684 1.6102 0.4805  0.0230  -0.1507 161  ARG D NH2 
13981 N  N   . THR D 162  ? 1.7501 1.8462 1.4805 0.4532  0.0474  -0.1365 162  THR D N   
13982 C  CA  . THR D 162  ? 1.6796 1.7792 1.4223 0.4474  0.0431  -0.1367 162  THR D CA  
13983 C  C   . THR D 162  ? 1.6567 1.7716 1.4114 0.4492  0.0454  -0.1354 162  THR D C   
13984 O  O   . THR D 162  ? 1.6696 1.7798 1.4258 0.4496  0.0401  -0.1365 162  THR D O   
13985 C  CB  . THR D 162  ? 1.7022 1.8105 1.4567 0.4383  0.0450  -0.1352 162  THR D CB  
13986 O  OG1 . THR D 162  ? 1.7115 1.8049 1.4540 0.4372  0.0423  -0.1365 162  THR D OG1 
13987 C  CG2 . THR D 162  ? 1.6307 1.7419 1.3975 0.4324  0.0404  -0.1354 162  THR D CG2 
13988 N  N   . SER D 163  ? 1.6057 1.7391 1.3692 0.4502  0.0532  -0.1333 163  SER D N   
13989 C  CA  . SER D 163  ? 1.5909 1.7395 1.3651 0.4528  0.0555  -0.1324 163  SER D CA  
13990 C  C   . SER D 163  ? 1.6440 1.7808 1.4050 0.4620  0.0518  -0.1341 163  SER D C   
13991 O  O   . SER D 163  ? 1.6286 1.7681 1.3942 0.4637  0.0488  -0.1344 163  SER D O   
13992 C  CB  . SER D 163  ? 1.5238 1.6933 1.3084 0.4525  0.0649  -0.1302 163  SER D CB  
13993 O  OG  . SER D 163  ? 1.5849 1.7677 1.3769 0.4569  0.0670  -0.1298 163  SER D OG  
13994 N  N   . GLN D 164  ? 1.9030 2.0258 1.6469 0.4680  0.0518  -0.1352 164  GLN D N   
13995 C  CA  . GLN D 164  ? 1.8361 1.9457 1.5659 0.4768  0.0482  -0.1369 164  GLN D CA  
13996 C  C   . GLN D 164  ? 1.9066 1.9975 1.6292 0.4759  0.0393  -0.1391 164  GLN D C   
13997 O  O   . GLN D 164  ? 1.9409 2.0270 1.6599 0.4807  0.0361  -0.1399 164  GLN D O   
13998 C  CB  . GLN D 164  ? 1.8381 1.9369 1.5510 0.4831  0.0504  -0.1376 164  GLN D CB  
13999 C  CG  . GLN D 164  ? 1.9959 2.1108 1.7126 0.4879  0.0587  -0.1357 164  GLN D CG  
14000 C  CD  . GLN D 164  ? 1.9888 2.1084 1.7056 0.4953  0.0586  -0.1359 164  GLN D CD  
14001 O  OE1 . GLN D 164  ? 2.0267 2.1319 1.7343 0.4991  0.0523  -0.1376 164  GLN D OE1 
14002 N  NE2 . GLN D 164  ? 1.8899 2.0296 1.6171 0.4974  0.0658  -0.1341 164  GLN D NE2 
14003 N  N   . PHE D 165  ? 1.9041 1.9842 1.6243 0.4698  0.0355  -0.1402 165  PHE D N   
14004 C  CA  . PHE D 165  ? 1.9058 1.9695 1.6214 0.4677  0.0274  -0.1424 165  PHE D CA  
14005 C  C   . PHE D 165  ? 1.8909 1.9658 1.6214 0.4643  0.0263  -0.1412 165  PHE D C   
14006 O  O   . PHE D 165  ? 1.8884 1.9528 1.6142 0.4668  0.0214  -0.1425 165  PHE D O   
14007 C  CB  . PHE D 165  ? 1.8646 1.9178 1.5774 0.4611  0.0240  -0.1437 165  PHE D CB  
14008 C  CG  . PHE D 165  ? 1.8790 1.9195 1.5920 0.4568  0.0166  -0.1456 165  PHE D CG  
14009 C  CD1 . PHE D 165  ? 1.8233 1.8422 1.5212 0.4608  0.0106  -0.1486 165  PHE D CD1 
14010 C  CD2 . PHE D 165  ? 1.9753 2.0251 1.7035 0.4487  0.0160  -0.1445 165  PHE D CD2 
14011 C  CE1 . PHE D 165  ? 1.9604 1.9672 1.6586 0.4566  0.0042  -0.1504 165  PHE D CE1 
14012 C  CE2 . PHE D 165  ? 1.9905 2.0284 1.7189 0.4449  0.0095  -0.1462 165  PHE D CE2 
14013 C  CZ  . PHE D 165  ? 2.0249 2.0413 1.7384 0.4487  0.0037  -0.1491 165  PHE D CZ  
14014 N  N   . LEU D 166  ? 1.3211 1.4168 1.0692 0.4587  0.0309  -0.1389 166  LEU D N   
14015 C  CA  . LEU D 166  ? 1.3265 1.4346 1.0893 0.4557  0.0302  -0.1377 166  LEU D CA  
14016 C  C   . LEU D 166  ? 1.4286 1.5440 1.1913 0.4634  0.0318  -0.1372 166  LEU D C   
14017 O  O   . LEU D 166  ? 1.4144 1.5303 1.1809 0.4642  0.0285  -0.1373 166  LEU D O   
14018 C  CB  . LEU D 166  ? 1.2107 1.3398 0.9922 0.4479  0.0351  -0.1355 166  LEU D CB  
14019 C  CG  . LEU D 166  ? 1.1697 1.2940 0.9554 0.4392  0.0325  -0.1356 166  LEU D CG  
14020 C  CD1 . LEU D 166  ? 1.2356 1.3808 1.0415 0.4317  0.0360  -0.1334 166  LEU D CD1 
14021 C  CD2 . LEU D 166  ? 1.2257 1.3307 1.0040 0.4383  0.0244  -0.1377 166  LEU D CD2 
14022 N  N   . ARG D 167  ? 1.7684 1.8890 1.5260 0.4695  0.0369  -0.1368 167  ARG D N   
14023 C  CA  . ARG D 167  ? 1.7015 1.8279 1.4574 0.4777  0.0383  -0.1366 167  ARG D CA  
14024 C  C   . ARG D 167  ? 1.7350 1.8391 1.4732 0.4845  0.0323  -0.1386 167  ARG D C   
14025 O  O   . ARG D 167  ? 1.7217 1.8275 1.4592 0.4900  0.0311  -0.1386 167  ARG D O   
14026 C  CB  . ARG D 167  ? 1.6505 1.7879 1.4055 0.4822  0.0456  -0.1356 167  ARG D CB  
14027 C  CG  . ARG D 167  ? 1.5238 1.6877 1.2984 0.4775  0.0526  -0.1335 167  ARG D CG  
14028 C  CD  . ARG D 167  ? 1.5423 1.7217 1.3299 0.4784  0.0522  -0.1329 167  ARG D CD  
14029 N  NE  . ARG D 167  ? 1.5923 1.7975 1.3984 0.4745  0.0591  -0.1312 167  ARG D NE  
14030 C  CZ  . ARG D 167  ? 1.5535 1.7764 1.3739 0.4740  0.0599  -0.1307 167  ARG D CZ  
14031 N  NH1 . ARG D 167  ? 1.5889 1.8069 1.4072 0.4775  0.0542  -0.1314 167  ARG D NH1 
14032 N  NH2 . ARG D 167  ? 1.3872 1.6330 1.2241 0.4698  0.0664  -0.1295 167  ARG D NH2 
14033 N  N   . SER D 168  ? 1.8851 1.9681 1.6087 0.4843  0.0286  -0.1405 168  SER D N   
14034 C  CA  . SER D 168  ? 1.9563 2.0166 1.6633 0.4896  0.0226  -0.1428 168  SER D CA  
14035 C  C   . SER D 168  ? 2.0452 2.1011 1.7573 0.4863  0.0174  -0.1430 168  SER D C   
14036 O  O   . SER D 168  ? 2.0667 2.1156 1.7726 0.4920  0.0149  -0.1434 168  SER D O   
14037 C  CB  . SER D 168  ? 1.9252 1.9648 1.6171 0.4888  0.0194  -0.1451 168  SER D CB  
14038 O  OG  . SER D 168  ? 1.8714 1.8882 1.5495 0.4914  0.0129  -0.1475 168  SER D OG  
14039 N  N   . LEU D 169  ? 2.1287 2.1879 1.8515 0.4773  0.0159  -0.1427 169  LEU D N   
14040 C  CA  . LEU D 169  ? 2.0889 2.1499 1.8208 0.4734  0.0125  -0.1421 169  LEU D CA  
14041 C  C   . LEU D 169  ? 2.0775 2.1599 1.8218 0.4762  0.0162  -0.1400 169  LEU D C   
14042 O  O   . LEU D 169  ? 2.1243 2.2235 1.8748 0.4781  0.0219  -0.1387 169  LEU D O   
14043 C  CB  . LEU D 169  ? 2.0217 2.0859 1.7646 0.4632  0.0113  -0.1418 169  LEU D CB  
14044 C  CG  . LEU D 169  ? 1.9969 2.0391 1.7305 0.4591  0.0055  -0.1443 169  LEU D CG  
14045 C  CD1 . LEU D 169  ? 1.8963 1.9208 1.6117 0.4638  0.0042  -0.1466 169  LEU D CD1 
14046 C  CD2 . LEU D 169  ? 1.9706 2.0203 1.7164 0.4495  0.0058  -0.1436 169  LEU D CD2 
14047 N  N   . ASN D 170  ? 1.6135 1.6952 1.3612 0.4766  0.0129  -0.1396 170  ASN D N   
14048 C  CA  . ASN D 170  ? 1.7022 1.8028 1.4596 0.4805  0.0157  -0.1380 170  ASN D CA  
14049 C  C   . ASN D 170  ? 1.6031 1.7262 1.3814 0.4729  0.0182  -0.1362 170  ASN D C   
14050 O  O   . ASN D 170  ? 1.5610 1.6830 1.3459 0.4679  0.0147  -0.1359 170  ASN D O   
14051 C  CB  . ASN D 170  ? 1.7373 1.8267 1.4869 0.4861  0.0112  -0.1384 170  ASN D CB  
14052 C  CG  . ASN D 170  ? 1.7503 1.8580 1.5073 0.4917  0.0137  -0.1371 170  ASN D CG  
14053 O  OD1 . ASN D 170  ? 1.7789 1.9004 1.5387 0.4958  0.0186  -0.1366 170  ASN D OD1 
14054 N  ND2 . ASN D 170  ? 1.6977 1.8056 1.4581 0.4920  0.0105  -0.1366 170  ASN D ND2 
14055 N  N   . PRO D 171  ? 2.1231 2.2668 1.9123 0.4720  0.0243  -0.1351 171  PRO D N   
14056 C  CA  . PRO D 171  ? 2.0923 2.2568 1.9014 0.4639  0.0269  -0.1336 171  PRO D CA  
14057 C  C   . PRO D 171  ? 2.0937 2.2805 1.9151 0.4669  0.0299  -0.1326 171  PRO D C   
14058 O  O   . PRO D 171  ? 2.1535 2.3470 1.9718 0.4738  0.0334  -0.1326 171  PRO D O   
14059 C  CB  . PRO D 171  ? 1.9929 2.1627 1.8047 0.4597  0.0318  -0.1332 171  PRO D CB  
14060 C  CG  . PRO D 171  ? 2.1356 2.2964 1.9317 0.4684  0.0339  -0.1341 171  PRO D CG  
14061 C  CD  . PRO D 171  ? 2.2262 2.3738 2.0099 0.4767  0.0294  -0.1351 171  PRO D CD  
14062 N  N   . MET D 172  ? 1.8710 2.0697 1.7065 0.4617  0.0286  -0.1318 172  MET D N   
14063 C  CA  . MET D 172  ? 1.8166 2.0394 1.6663 0.4631  0.0319  -0.1310 172  MET D CA  
14064 C  C   . MET D 172  ? 1.8315 2.0725 1.6913 0.4603  0.0393  -0.1304 172  MET D C   
14065 O  O   . MET D 172  ? 1.8979 2.1550 1.7634 0.4648  0.0434  -0.1303 172  MET D O   
14066 C  CB  . MET D 172  ? 1.8295 2.0618 1.6928 0.4570  0.0291  -0.1304 172  MET D CB  
14067 C  CG  . MET D 172  ? 1.9279 2.1474 1.7830 0.4615  0.0228  -0.1308 172  MET D CG  
14068 S  SD  . MET D 172  ? 1.9044 2.1383 1.7763 0.4553  0.0202  -0.1299 172  MET D SD  
14069 C  CE  . MET D 172  ? 1.6585 1.9239 1.5473 0.4565  0.0260  -0.1297 172  MET D CE  
14070 N  N   . GLN D 173  ? 1.7517 1.9902 1.6137 0.4532  0.0413  -0.1300 173  GLN D N   
14071 C  CA  . GLN D 173  ? 1.8071 2.0606 1.6774 0.4501  0.0488  -0.1292 173  GLN D CA  
14072 C  C   . GLN D 173  ? 1.8190 2.0604 1.6838 0.4445  0.0493  -0.1290 173  GLN D C   
14073 O  O   . GLN D 173  ? 1.8121 2.0458 1.6787 0.4382  0.0453  -0.1290 173  GLN D O   
14074 C  CB  . GLN D 173  ? 1.7882 2.0673 1.6802 0.4438  0.0523  -0.1283 173  GLN D CB  
14075 C  CG  . GLN D 173  ? 1.7221 2.0164 1.6238 0.4390  0.0604  -0.1275 173  GLN D CG  
14076 C  CD  . GLN D 173  ? 1.7157 2.0337 1.6388 0.4317  0.0634  -0.1268 173  GLN D CD  
14077 O  OE1 . GLN D 173  ? 1.5547 1.8800 1.4855 0.4315  0.0597  -0.1272 173  GLN D OE1 
14078 N  NE2 . GLN D 173  ? 1.8975 2.2272 1.8299 0.4257  0.0703  -0.1260 173  GLN D NE2 
14079 N  N   . VAL D 174  ? 1.4794 1.7190 1.3373 0.4470  0.0541  -0.1290 174  VAL D N   
14080 C  CA  . VAL D 174  ? 1.3966 1.6266 1.2491 0.4423  0.0555  -0.1287 174  VAL D CA  
14081 C  C   . VAL D 174  ? 1.4182 1.6680 1.2849 0.4364  0.0634  -0.1272 174  VAL D C   
14082 O  O   . VAL D 174  ? 1.3498 1.6141 1.2216 0.4396  0.0694  -0.1268 174  VAL D O   
14083 C  CB  . VAL D 174  ? 1.3640 1.5754 1.1964 0.4495  0.0551  -0.1298 174  VAL D CB  
14084 C  CG1 . VAL D 174  ? 1.3633 1.5700 1.1919 0.4453  0.0584  -0.1293 174  VAL D CG1 
14085 C  CG2 . VAL D 174  ? 1.3823 1.5711 1.2004 0.4530  0.0470  -0.1314 174  VAL D CG2 
14086 N  N   . SER D 175  ? 1.6220 1.8722 1.4952 0.4277  0.0637  -0.1265 175  SER D N   
14087 C  CA  . SER D 175  ? 1.6373 1.9051 1.5243 0.4210  0.0711  -0.1250 175  SER D CA  
14088 C  C   . SER D 175  ? 1.6261 1.8827 1.5056 0.4169  0.0726  -0.1244 175  SER D C   
14089 O  O   . SER D 175  ? 1.5548 1.7927 1.4233 0.4167  0.0667  -0.1253 175  SER D O   
14090 C  CB  . SER D 175  ? 1.6609 1.9446 1.5668 0.4132  0.0705  -0.1243 175  SER D CB  
14091 O  OG  . SER D 175  ? 1.7161 2.0083 1.6276 0.4172  0.0679  -0.1250 175  SER D OG  
14092 N  N   . GLU D 176  ? 1.9470 2.2151 1.8324 0.4137  0.0807  -0.1231 176  GLU D N   
14093 C  CA  . GLU D 176  ? 1.9898 2.2495 1.8690 0.4097  0.0833  -0.1222 176  GLU D CA  
14094 C  C   . GLU D 176  ? 1.9496 2.2223 1.8452 0.3995  0.0859  -0.1208 176  GLU D C   
14095 O  O   . GLU D 176  ? 1.9707 2.2613 1.8787 0.3957  0.0935  -0.1196 176  GLU D O   
14096 C  CB  . GLU D 176  ? 1.9977 2.2592 1.8698 0.4138  0.0909  -0.1215 176  GLU D CB  
14097 C  CG  . GLU D 176  ? 2.0672 2.3168 1.9232 0.4241  0.0887  -0.1228 176  GLU D CG  
14098 C  CD  . GLU D 176  ? 2.2223 2.4710 2.0695 0.4279  0.0960  -0.1220 176  GLU D CD  
14099 O  OE1 . GLU D 176  ? 2.2502 2.5064 2.1029 0.4224  0.1027  -0.1203 176  GLU D OE1 
14100 O  OE2 . GLU D 176  ? 2.1479 2.3879 1.9820 0.4365  0.0951  -0.1229 176  GLU D OE2 
14101 N  N   . VAL D 177  ? 1.7851 2.0483 1.6805 0.3949  0.0798  -0.1211 177  VAL D N   
14102 C  CA  . VAL D 177  ? 1.7262 2.0001 1.6364 0.3853  0.0814  -0.1199 177  VAL D CA  
14103 C  C   . VAL D 177  ? 1.7332 2.0060 1.6408 0.3812  0.0876  -0.1184 177  VAL D C   
14104 O  O   . VAL D 177  ? 1.7783 2.0342 1.6705 0.3838  0.0859  -0.1187 177  VAL D O   
14105 C  CB  . VAL D 177  ? 1.7548 2.0184 1.6652 0.3821  0.0729  -0.1207 177  VAL D CB  
14106 C  CG1 . VAL D 177  ? 1.6467 1.8867 1.5389 0.3856  0.0672  -0.1219 177  VAL D CG1 
14107 C  CG2 . VAL D 177  ? 1.8329 2.1058 1.7570 0.3723  0.0746  -0.1193 177  VAL D CG2 
14108 N  N   . ALA D 178  ? 1.5193 1.8099 1.4415 0.3748  0.0949  -0.1168 178  ALA D N   
14109 C  CA  . ALA D 178  ? 1.6468 1.9381 1.5677 0.3704  0.1020  -0.1151 178  ALA D CA  
14110 C  C   . ALA D 178  ? 1.6976 1.9967 1.6318 0.3605  0.1028  -0.1139 178  ALA D C   
14111 O  O   . ALA D 178  ? 1.7158 2.0234 1.6625 0.3569  0.0991  -0.1144 178  ALA D O   
14112 C  CB  . ALA D 178  ? 1.7749 2.0797 1.6996 0.3719  0.1118  -0.1141 178  ALA D CB  
14113 N  N   . TYR D 179  ? 1.9272 2.2231 1.8581 0.3564  0.1077  -0.1123 179  TYR D N   
14114 C  CA  . TYR D 179  ? 1.8597 2.1615 1.8015 0.3471  0.1092  -0.1110 179  TYR D CA  
14115 C  C   . TYR D 179  ? 1.9049 2.2297 1.8664 0.3410  0.1158  -0.1103 179  TYR D C   
14116 O  O   . TYR D 179  ? 1.9567 2.2890 1.9276 0.3330  0.1200  -0.1089 179  TYR D O   
14117 C  CB  . TYR D 179  ? 1.8859 2.1778 1.8175 0.3450  0.1135  -0.1093 179  TYR D CB  
14118 C  CG  . TYR D 179  ? 1.9021 2.1716 1.8137 0.3510  0.1073  -0.1103 179  TYR D CG  
14119 C  CD1 . TYR D 179  ? 1.9074 2.1649 1.8155 0.3498  0.0986  -0.1114 179  TYR D CD1 
14120 C  CD2 . TYR D 179  ? 1.8873 2.1480 1.7839 0.3579  0.1100  -0.1103 179  TYR D CD2 
14121 C  CE1 . TYR D 179  ? 1.9387 2.1760 1.8291 0.3550  0.0927  -0.1127 179  TYR D CE1 
14122 C  CE2 . TYR D 179  ? 1.8369 2.0772 1.7152 0.3633  0.1040  -0.1115 179  TYR D CE2 
14123 C  CZ  . TYR D 179  ? 1.9054 2.1343 1.7809 0.3617  0.0953  -0.1128 179  TYR D CZ  
14124 O  OH  . TYR D 179  ? 1.9358 2.1448 1.7936 0.3667  0.0891  -0.1145 179  TYR D OH  
14125 N  N   . CYS E 26   ? 1.2846 1.5668 1.4671 0.0465  0.0571  -0.0729 26   CYS E N   
14126 C  CA  . CYS E 26   ? 1.1739 1.4627 1.3586 0.0545  0.0518  -0.0742 26   CYS E CA  
14127 C  C   . CYS E 26   ? 1.1075 1.3899 1.2902 0.0585  0.0450  -0.0732 26   CYS E C   
14128 O  O   . CYS E 26   ? 1.1520 1.4366 1.3349 0.0654  0.0402  -0.0737 26   CYS E O   
14129 C  CB  . CYS E 26   ? 1.1404 1.4249 1.3197 0.0597  0.0533  -0.0721 26   CYS E CB  
14130 S  SG  . CYS E 26   ? 1.1569 1.4490 1.3379 0.0561  0.0617  -0.0731 26   CYS E SG  
14131 N  N   . HIS E 27   ? 0.9946 1.2683 1.1748 0.0542  0.0449  -0.0717 27   HIS E N   
14132 C  CA  . HIS E 27   ? 0.9406 1.2085 1.1192 0.0572  0.0391  -0.0708 27   HIS E CA  
14133 C  C   . HIS E 27   ? 1.0552 1.3225 1.2356 0.0510  0.0394  -0.0718 27   HIS E C   
14134 O  O   . HIS E 27   ? 1.1094 1.3865 1.2956 0.0508  0.0365  -0.0751 27   HIS E O   
14135 C  CB  . HIS E 27   ? 0.9920 1.2448 1.1624 0.0606  0.0379  -0.0666 27   HIS E CB  
14136 C  CG  . HIS E 27   ? 0.9790 1.2264 1.1479 0.0647  0.0321  -0.0657 27   HIS E CG  
14137 N  ND1 . HIS E 27   ? 0.8749 1.1299 1.0476 0.0695  0.0273  -0.0680 27   HIS E ND1 
14138 C  CD2 . HIS E 27   ? 0.9706 1.2057 1.1346 0.0647  0.0306  -0.0627 27   HIS E CD2 
14139 C  CE1 . HIS E 27   ? 0.9661 1.2130 1.1358 0.0722  0.0233  -0.0664 27   HIS E CE1 
14140 N  NE2 . HIS E 27   ? 1.0638 1.2989 1.2285 0.0692  0.0252  -0.0632 27   HIS E NE2 
14141 N  N   . GLN E 28   ? 1.1202 1.3758 1.2952 0.0464  0.0429  -0.0691 28   GLN E N   
14142 C  CA  . GLN E 28   ? 1.0172 1.2708 1.1929 0.0397  0.0443  -0.0699 28   GLN E CA  
14143 C  C   . GLN E 28   ? 0.9615 1.2163 1.1389 0.0419  0.0383  -0.0711 28   GLN E C   
14144 O  O   . GLN E 28   ? 1.0163 1.2795 1.1988 0.0387  0.0373  -0.0746 28   GLN E O   
14145 C  CB  . GLN E 28   ? 0.9725 1.2375 1.1545 0.0331  0.0487  -0.0735 28   GLN E CB  
14146 C  CG  . GLN E 28   ? 0.9911 1.2511 1.1697 0.0286  0.0560  -0.0718 28   GLN E CG  
14147 C  CD  . GLN E 28   ? 0.9889 1.2417 1.1650 0.0204  0.0603  -0.0715 28   GLN E CD  
14148 O  OE1 . GLN E 28   ? 0.9511 1.2010 1.1271 0.0185  0.0576  -0.0721 28   GLN E OE1 
14149 N  NE2 . GLN E 28   ? 0.9410 1.1904 1.1145 0.0157  0.0672  -0.0705 28   GLN E NE2 
14150 N  N   . ASP E 29   ? 0.8189 1.0650 0.9918 0.0476  0.0345  -0.0684 29   ASP E N   
14151 C  CA  . ASP E 29   ? 0.8630 1.1091 1.0365 0.0504  0.0291  -0.0692 29   ASP E CA  
14152 C  C   . ASP E 29   ? 0.9536 1.1882 1.1223 0.0469  0.0296  -0.0671 29   ASP E C   
14153 O  O   . ASP E 29   ? 1.0850 1.3226 1.2557 0.0424  0.0297  -0.0694 29   ASP E O   
14154 C  CB  . ASP E 29   ? 0.8784 1.1218 1.0499 0.0584  0.0246  -0.0677 29   ASP E CB  
14155 C  CG  . ASP E 29   ? 0.9642 1.2205 1.1411 0.0630  0.0210  -0.0712 29   ASP E CG  
14156 O  OD1 . ASP E 29   ? 0.9417 1.2106 1.1246 0.0602  0.0225  -0.0747 29   ASP E OD1 
14157 O  OD2 . ASP E 29   ? 0.8653 1.1192 1.0404 0.0694  0.0168  -0.0705 29   ASP E OD2 
14158 N  N   . MET E 30   ? 0.6557 0.8774 0.8183 0.0489  0.0299  -0.0630 30   MET E N   
14159 C  CA  . MET E 30   ? 0.6347 0.8447 0.7922 0.0457  0.0312  -0.0606 30   MET E CA  
14160 C  C   . MET E 30   ? 0.6691 0.8717 0.8225 0.0412  0.0369  -0.0584 30   MET E C   
14161 O  O   . MET E 30   ? 0.6043 0.7953 0.7522 0.0400  0.0383  -0.0555 30   MET E O   
14162 C  CB  . MET E 30   ? 0.5466 0.7472 0.7001 0.0510  0.0276  -0.0575 30   MET E CB  
14163 C  CG  . MET E 30   ? 0.5421 0.7449 0.6969 0.0533  0.0230  -0.0590 30   MET E CG  
14164 S  SD  . MET E 30   ? 0.6955 0.8905 0.8473 0.0605  0.0187  -0.0561 30   MET E SD  
14165 C  CE  . MET E 30   ? 0.5452 0.7494 0.7006 0.0658  0.0166  -0.0578 30   MET E CE  
14166 N  N   . TYR E 31   ? 0.8443 1.0533 1.0000 0.0389  0.0405  -0.0597 31   TYR E N   
14167 C  CA  . TYR E 31   ? 0.7155 0.9170 0.8665 0.0348  0.0465  -0.0576 31   TYR E CA  
14168 C  C   . TYR E 31   ? 0.6799 0.8767 0.8291 0.0279  0.0496  -0.0582 31   TYR E C   
14169 O  O   . TYR E 31   ? 0.6735 0.8579 0.8159 0.0261  0.0525  -0.0551 31   TYR E O   
14170 C  CB  . TYR E 31   ? 0.6709 0.8812 0.8250 0.0336  0.0500  -0.0593 31   TYR E CB  
14171 C  CG  . TYR E 31   ? 0.6442 0.8567 0.7981 0.0402  0.0481  -0.0583 31   TYR E CG  
14172 C  CD1 . TYR E 31   ? 0.7601 0.9713 0.9139 0.0466  0.0424  -0.0575 31   TYR E CD1 
14173 C  CD2 . TYR E 31   ? 0.7381 0.9537 0.8916 0.0400  0.0522  -0.0584 31   TYR E CD2 
14174 C  CE1 . TYR E 31   ? 0.8810 1.0937 1.0343 0.0524  0.0407  -0.0569 31   TYR E CE1 
14175 C  CE2 . TYR E 31   ? 0.7681 0.9854 0.9209 0.0461  0.0503  -0.0577 31   TYR E CE2 
14176 C  CZ  . TYR E 31   ? 0.7744 0.9903 0.9272 0.0523  0.0444  -0.0570 31   TYR E CZ  
14177 O  OH  . TYR E 31   ? 0.7460 0.9630 0.8977 0.0582  0.0425  -0.0566 31   TYR E OH  
14178 N  N   . ASP E 32   ? 0.9707 1.1771 1.1257 0.0240  0.0488  -0.0622 32   ASP E N   
14179 C  CA  . ASP E 32   ? 1.0529 1.2557 1.2068 0.0175  0.0508  -0.0635 32   ASP E CA  
14180 C  C   . ASP E 32   ? 1.1809 1.3871 1.3372 0.0196  0.0450  -0.0655 32   ASP E C   
14181 O  O   . ASP E 32   ? 1.2800 1.4989 1.4429 0.0218  0.0413  -0.0688 32   ASP E O   
14182 C  CB  . ASP E 32   ? 1.0890 1.3005 1.2476 0.0104  0.0552  -0.0671 32   ASP E CB  
14183 C  CG  . ASP E 32   ? 1.1564 1.3623 1.3110 0.0077  0.0619  -0.0649 32   ASP E CG  
14184 O  OD1 . ASP E 32   ? 1.2041 1.4009 1.3527 0.0122  0.0624  -0.0608 32   ASP E OD1 
14185 O  OD2 . ASP E 32   ? 1.0881 1.2986 1.2454 0.0011  0.0667  -0.0673 32   ASP E OD2 
14186 N  N   . GLN E 33   ? 0.9371 1.1320 1.0878 0.0193  0.0443  -0.0633 33   GLN E N   
14187 C  CA  . GLN E 33   ? 0.8457 1.0415 0.9970 0.0222  0.0390  -0.0644 33   GLN E CA  
14188 C  C   . GLN E 33   ? 0.8542 1.0485 1.0046 0.0162  0.0397  -0.0669 33   GLN E C   
14189 O  O   . GLN E 33   ? 0.8573 1.0457 1.0048 0.0101  0.0446  -0.0667 33   GLN E O   
14190 C  CB  . GLN E 33   ? 0.8821 1.0664 1.0276 0.0278  0.0369  -0.0599 33   GLN E CB  
14191 C  CG  . GLN E 33   ? 0.9533 1.1397 1.1001 0.0342  0.0348  -0.0581 33   GLN E CG  
14192 C  CD  . GLN E 33   ? 0.8865 1.0616 1.0282 0.0388  0.0333  -0.0539 33   GLN E CD  
14193 O  OE1 . GLN E 33   ? 0.8312 0.9988 0.9693 0.0386  0.0325  -0.0527 33   GLN E OE1 
14194 N  NE2 . GLN E 33   ? 0.9219 1.0958 1.0632 0.0431  0.0329  -0.0518 33   GLN E NE2 
14195 N  N   . GLN E 34   ? 0.7558 0.9548 0.9082 0.0184  0.0347  -0.0692 34   GLN E N   
14196 C  CA  . GLN E 34   ? 0.7469 0.9462 0.8990 0.0133  0.0343  -0.0724 34   GLN E CA  
14197 C  C   . GLN E 34   ? 0.8457 1.0287 0.9892 0.0112  0.0367  -0.0692 34   GLN E C   
14198 O  O   . GLN E 34   ? 0.7884 0.9687 0.9302 0.0052  0.0386  -0.0713 34   GLN E O   
14199 C  CB  . GLN E 34   ? 0.6171 0.8247 0.7723 0.0174  0.0279  -0.0753 34   GLN E CB  
14200 C  CG  . GLN E 34   ? 0.7193 0.9431 0.8827 0.0204  0.0251  -0.0785 34   GLN E CG  
14201 C  CD  . GLN E 34   ? 0.7075 0.9306 0.8701 0.0290  0.0216  -0.0758 34   GLN E CD  
14202 O  OE1 . GLN E 34   ? 0.7372 0.9513 0.8946 0.0333  0.0192  -0.0731 34   GLN E OE1 
14203 N  NE2 . GLN E 34   ? 0.7389 0.9714 0.9066 0.0315  0.0216  -0.0766 34   GLN E NE2 
14204 N  N   . LYS E 35   ? 0.9206 1.0929 1.0587 0.0161  0.0367  -0.0643 35   LYS E N   
14205 C  CA  . LYS E 35   ? 0.7403 0.8977 0.8704 0.0149  0.0391  -0.0611 35   LYS E CA  
14206 C  C   . LYS E 35   ? 0.8248 0.9758 0.9516 0.0084  0.0454  -0.0606 35   LYS E C   
14207 O  O   . LYS E 35   ? 0.8552 1.0113 0.9850 0.0063  0.0483  -0.0611 35   LYS E O   
14208 C  CB  . LYS E 35   ? 0.7092 0.8579 0.8353 0.0213  0.0382  -0.0561 35   LYS E CB  
14209 C  CG  . LYS E 35   ? 0.7558 0.9039 0.8824 0.0232  0.0406  -0.0535 35   LYS E CG  
14210 C  CD  . LYS E 35   ? 0.7601 0.9009 0.8838 0.0295  0.0390  -0.0491 35   LYS E CD  
14211 C  CE  . LYS E 35   ? 0.7105 0.8495 0.8335 0.0312  0.0414  -0.0466 35   LYS E CE  
14212 N  NZ  . LYS E 35   ? 0.6868 0.8219 0.8091 0.0375  0.0389  -0.0433 35   LYS E NZ  
14213 N  N   . TYR E 36   ? 0.8206 0.9599 0.9406 0.0055  0.0477  -0.0594 36   TYR E N   
14214 C  CA  . TYR E 36   ? 0.7496 0.8805 0.8649 -0.0007 0.0538  -0.0588 36   TYR E CA  
14215 C  C   . TYR E 36   ? 0.7981 0.9156 0.9059 0.0028  0.0567  -0.0532 36   TYR E C   
14216 O  O   . TYR E 36   ? 0.8264 0.9347 0.9291 0.0060  0.0556  -0.0506 36   TYR E O   
14217 C  CB  . TYR E 36   ? 0.7998 0.9259 0.9117 -0.0064 0.0547  -0.0616 36   TYR E CB  
14218 C  CG  . TYR E 36   ? 0.7804 0.9192 0.8994 -0.0123 0.0539  -0.0676 36   TYR E CG  
14219 C  CD1 . TYR E 36   ? 0.8602 1.0024 0.9818 -0.0188 0.0588  -0.0695 36   TYR E CD1 
14220 C  CD2 . TYR E 36   ? 0.7195 0.8672 0.8427 -0.0114 0.0484  -0.0714 36   TYR E CD2 
14221 C  CE1 . TYR E 36   ? 0.9075 1.0625 1.0366 -0.0246 0.0582  -0.0753 36   TYR E CE1 
14222 C  CE2 . TYR E 36   ? 0.7570 0.9176 0.8874 -0.0166 0.0473  -0.0773 36   TYR E CE2 
14223 C  CZ  . TYR E 36   ? 0.8859 1.0505 1.0197 -0.0234 0.0522  -0.0793 36   TYR E CZ  
14224 O  OH  . TYR E 36   ? 0.9235 1.1020 1.0654 -0.0289 0.0513  -0.0853 36   TYR E OH  
14225 N  N   . THR E 37   ? 0.9989 1.1156 1.1063 0.0023  0.0606  -0.0515 37   THR E N   
14226 C  CA  . THR E 37   ? 0.9797 1.0845 1.0800 0.0057  0.0633  -0.0465 37   THR E CA  
14227 C  C   . THR E 37   ? 1.0085 1.0989 1.0998 0.0016  0.0681  -0.0450 37   THR E C   
14228 O  O   . THR E 37   ? 1.0194 1.1083 1.1097 -0.0031 0.0684  -0.0478 37   THR E O   
14229 C  CB  . THR E 37   ? 1.0707 1.1789 1.1724 0.0070  0.0656  -0.0452 37   THR E CB  
14230 O  OG1 . THR E 37   ? 1.1694 1.2756 1.2690 0.0003  0.0714  -0.0466 37   THR E OG1 
14231 C  CG2 . THR E 37   ? 0.9385 1.0618 1.0493 0.0098  0.0613  -0.0476 37   THR E CG2 
14232 N  N   . THR E 38   ? 1.0026 1.0825 1.0871 0.0036  0.0719  -0.0409 38   THR E N   
14233 C  CA  . THR E 38   ? 1.0959 1.1606 1.1706 0.0012  0.0763  -0.0389 38   THR E CA  
14234 C  C   . THR E 38   ? 1.1412 1.2038 1.2140 -0.0074 0.0811  -0.0420 38   THR E C   
14235 O  O   . THR E 38   ? 1.2384 1.2955 1.3080 -0.0115 0.0819  -0.0438 38   THR E O   
14236 C  CB  . THR E 38   ? 1.0381 1.0929 1.1059 0.0059  0.0791  -0.0340 38   THR E CB  
14237 O  OG1 . THR E 38   ? 0.8939 0.9516 0.9645 0.0133  0.0744  -0.0316 38   THR E OG1 
14238 C  CG2 . THR E 38   ? 1.0503 1.0889 1.1075 0.0044  0.0834  -0.0316 38   THR E CG2 
14239 N  N   . TYR E 39   ? 0.5667 0.6334 0.6413 -0.0103 0.0846  -0.0427 39   TYR E N   
14240 C  CA  . TYR E 39   ? 0.5230 0.5873 0.5959 -0.0189 0.0901  -0.0454 39   TYR E CA  
14241 C  C   . TYR E 39   ? 0.5463 0.6273 0.6300 -0.0234 0.0889  -0.0504 39   TYR E C   
14242 O  O   . TYR E 39   ? 0.5818 0.6634 0.6659 -0.0302 0.0940  -0.0525 39   TYR E O   
14243 C  CB  . TYR E 39   ? 0.6865 0.7394 0.7508 -0.0194 0.0968  -0.0420 39   TYR E CB  
14244 C  CG  . TYR E 39   ? 0.6710 0.7054 0.7231 -0.0184 0.1002  -0.0383 39   TYR E CG  
14245 C  CD1 . TYR E 39   ? 0.7138 0.7426 0.7633 -0.0186 0.0980  -0.0389 39   TYR E CD1 
14246 C  CD2 . TYR E 39   ? 0.7379 0.7603 0.7806 -0.0167 0.1056  -0.0344 39   TYR E CD2 
14247 C  CE1 . TYR E 39   ? 0.8289 0.8406 0.8670 -0.0173 0.1012  -0.0356 39   TYR E CE1 
14248 C  CE2 . TYR E 39   ? 0.7523 0.7577 0.7835 -0.0152 0.1086  -0.0311 39   TYR E CE2 
14249 C  CZ  . TYR E 39   ? 0.7656 0.7659 0.7947 -0.0155 0.1064  -0.0317 39   TYR E CZ  
14250 O  OH  . TYR E 39   ? 0.6381 0.6215 0.6556 -0.0136 0.1096  -0.0284 39   TYR E OH  
14251 N  N   . GLU E 40   ? 0.7631 0.8574 0.8555 -0.0197 0.0825  -0.0524 40   GLU E N   
14252 C  CA  . GLU E 40   ? 0.7715 0.8827 0.8745 -0.0229 0.0808  -0.0572 40   GLU E CA  
14253 C  C   . GLU E 40   ? 0.8140 0.9273 0.9190 -0.0315 0.0823  -0.0621 40   GLU E C   
14254 O  O   . GLU E 40   ? 0.9880 1.0968 1.0905 -0.0321 0.0797  -0.0631 40   GLU E O   
14255 C  CB  . GLU E 40   ? 0.7391 0.8624 0.8496 -0.0165 0.0733  -0.0582 40   GLU E CB  
14256 C  CG  . GLU E 40   ? 0.8069 0.9485 0.9284 -0.0184 0.0710  -0.0630 40   GLU E CG  
14257 C  CD  . GLU E 40   ? 0.9785 1.1302 1.1058 -0.0107 0.0644  -0.0629 40   GLU E CD  
14258 O  OE1 . GLU E 40   ? 0.9185 1.0642 1.0422 -0.0041 0.0630  -0.0587 40   GLU E OE1 
14259 O  OE2 . GLU E 40   ? 1.0347 1.2002 1.1701 -0.0111 0.0605  -0.0672 40   GLU E OE2 
14260 N  N   . PRO E 41   ? 0.6291 0.7489 0.7384 -0.0384 0.0865  -0.0652 41   PRO E N   
14261 C  CA  . PRO E 41   ? 0.6482 0.7707 0.7601 -0.0473 0.0878  -0.0704 41   PRO E CA  
14262 C  C   . PRO E 41   ? 0.7073 0.8446 0.8283 -0.0463 0.0805  -0.0751 41   PRO E C   
14263 O  O   . PRO E 41   ? 0.7167 0.8669 0.8450 -0.0408 0.0758  -0.0757 41   PRO E O   
14264 C  CB  . PRO E 41   ? 0.6085 0.7373 0.7248 -0.0539 0.0938  -0.0725 41   PRO E CB  
14265 C  CG  . PRO E 41   ? 0.6456 0.7818 0.7654 -0.0473 0.0929  -0.0699 41   PRO E CG  
14266 C  CD  . PRO E 41   ? 0.6984 0.8232 0.8103 -0.0386 0.0904  -0.0643 41   PRO E CD  
14267 N  N   . SER E 42   ? 0.8112 0.9457 0.9308 -0.0514 0.0796  -0.0785 42   SER E N   
14268 C  CA  . SER E 42   ? 0.9330 1.0792 1.0592 -0.0503 0.0726  -0.0830 42   SER E CA  
14269 C  C   . SER E 42   ? 0.9124 1.0665 1.0442 -0.0600 0.0737  -0.0896 42   SER E C   
14270 O  O   . SER E 42   ? 0.7631 0.9065 0.8895 -0.0674 0.0792  -0.0903 42   SER E O   
14271 C  CB  . SER E 42   ? 0.9563 1.0911 1.0746 -0.0456 0.0688  -0.0807 42   SER E CB  
14272 O  OG  . SER E 42   ? 0.9231 1.0680 1.0464 -0.0449 0.0624  -0.0852 42   SER E OG  
14273 N  N   . SER E 43   ? 1.3784 1.5511 1.5211 -0.0597 0.0685  -0.0947 43   SER E N   
14274 C  CA  . SER E 43   ? 1.4219 1.6052 1.5717 -0.0684 0.0683  -0.1017 43   SER E CA  
14275 C  C   . SER E 43   ? 1.4083 1.5911 1.5563 -0.0682 0.0624  -0.1051 43   SER E C   
14276 O  O   . SER E 43   ? 1.3732 1.5643 1.5266 -0.0753 0.0615  -0.1115 43   SER E O   
14277 C  CB  . SER E 43   ? 1.4944 1.7000 1.6579 -0.0685 0.0663  -0.1058 43   SER E CB  
14278 O  OG  . SER E 43   ? 1.5708 1.7869 1.7384 -0.0596 0.0585  -0.1060 43   SER E OG  
14279 N  N   . PHE E 44   ? 1.1526 1.3261 1.2932 -0.0603 0.0585  -0.1013 44   PHE E N   
14280 C  CA  . PHE E 44   ? 1.0976 1.2691 1.2350 -0.0595 0.0532  -0.1040 44   PHE E CA  
14281 C  C   . PHE E 44   ? 0.9868 1.1407 1.1141 -0.0658 0.0573  -0.1039 44   PHE E C   
14282 O  O   . PHE E 44   ? 0.9784 1.1330 1.1050 -0.0694 0.0544  -0.1086 44   PHE E O   
14283 C  CB  . PHE E 44   ? 1.0286 1.1968 1.1620 -0.0486 0.0478  -0.0999 44   PHE E CB  
14284 C  CG  . PHE E 44   ? 0.8981 1.0634 1.0271 -0.0468 0.0425  -0.1022 44   PHE E CG  
14285 C  CD1 . PHE E 44   ? 0.8837 1.0645 1.0201 -0.0469 0.0364  -0.1083 44   PHE E CD1 
14286 C  CD2 . PHE E 44   ? 0.8784 1.0255 0.9958 -0.0445 0.0435  -0.0983 44   PHE E CD2 
14287 C  CE1 . PHE E 44   ? 0.8534 1.0310 0.9849 -0.0448 0.0314  -0.1104 44   PHE E CE1 
14288 C  CE2 . PHE E 44   ? 0.8733 1.0171 0.9860 -0.0426 0.0389  -0.1003 44   PHE E CE2 
14289 C  CZ  . PHE E 44   ? 0.8613 1.0201 0.9807 -0.0427 0.0328  -0.1064 44   PHE E CZ  
14290 N  N   . PHE E 45   ? 0.8116 0.9496 0.9307 -0.0668 0.0639  -0.0988 45   PHE E N   
14291 C  CA  . PHE E 45   ? 0.8462 0.9662 0.9548 -0.0724 0.0686  -0.0983 45   PHE E CA  
14292 C  C   . PHE E 45   ? 0.9232 1.0441 1.0346 -0.0836 0.0748  -0.1021 45   PHE E C   
14293 O  O   . PHE E 45   ? 0.9781 1.1114 1.0985 -0.0863 0.0768  -0.1036 45   PHE E O   
14294 C  CB  . PHE E 45   ? 0.8222 0.9236 0.9194 -0.0670 0.0724  -0.0906 45   PHE E CB  
14295 C  CG  . PHE E 45   ? 0.8484 0.9467 0.9419 -0.0570 0.0670  -0.0869 45   PHE E CG  
14296 C  CD1 . PHE E 45   ? 0.8313 0.9214 0.9180 -0.0558 0.0641  -0.0877 45   PHE E CD1 
14297 C  CD2 . PHE E 45   ? 0.9344 1.0379 1.0311 -0.0489 0.0651  -0.0828 45   PHE E CD2 
14298 C  CE1 . PHE E 45   ? 0.7955 0.8826 0.8789 -0.0468 0.0597  -0.0842 45   PHE E CE1 
14299 C  CE2 . PHE E 45   ? 0.8762 0.9767 0.9698 -0.0402 0.0605  -0.0795 45   PHE E CE2 
14300 C  CZ  . PHE E 45   ? 0.7922 0.8845 0.8792 -0.0392 0.0580  -0.0801 45   PHE E CZ  
14301 N  N   . ALA E 46   ? 0.7547 0.8617 0.8579 -0.0902 0.0782  -0.1036 46   ALA E N   
14302 C  CA  . ALA E 46   ? 0.7322 0.8394 0.8379 -0.1019 0.0840  -0.1080 46   ALA E CA  
14303 C  C   . ALA E 46   ? 0.7645 0.8623 0.8662 -0.1039 0.0925  -0.1033 46   ALA E C   
14304 O  O   . ALA E 46   ? 0.7696 0.8766 0.8789 -0.1102 0.0965  -0.1058 46   ALA E O   
14305 C  CB  . ALA E 46   ? 0.6245 0.7183 0.7218 -0.1082 0.0850  -0.1111 46   ALA E CB  
14306 N  N   . ASP E 47   ? 1.1792 1.2586 1.2686 -0.0984 0.0956  -0.0965 47   ASP E N   
14307 C  CA  . ASP E 47   ? 1.2145 1.2824 1.2977 -0.0997 0.1037  -0.0918 47   ASP E CA  
14308 C  C   . ASP E 47   ? 1.2057 1.2836 1.2948 -0.0930 0.1033  -0.0881 47   ASP E C   
14309 O  O   . ASP E 47   ? 1.1052 1.1735 1.1885 -0.0923 0.1094  -0.0835 47   ASP E O   
14310 C  CB  . ASP E 47   ? 1.2647 1.3088 1.3321 -0.0962 0.1070  -0.0862 47   ASP E CB  
14311 C  CG  . ASP E 47   ? 1.3031 1.3452 1.3673 -0.0849 0.1011  -0.0818 47   ASP E CG  
14312 O  OD1 . ASP E 47   ? 1.3104 1.3685 1.3840 -0.0799 0.0944  -0.0831 47   ASP E OD1 
14313 O  OD2 . ASP E 47   ? 1.3147 1.3391 1.3668 -0.0809 0.1034  -0.0770 47   ASP E OD2 
14314 N  N   . GLY E 48   ? 1.1074 1.2037 1.2073 -0.0880 0.0963  -0.0900 48   GLY E N   
14315 C  CA  . GLY E 48   ? 0.9584 1.0648 1.0643 -0.0820 0.0957  -0.0872 48   GLY E CA  
14316 C  C   . GLY E 48   ? 0.8700 0.9648 0.9674 -0.0726 0.0958  -0.0798 48   GLY E C   
14317 O  O   . GLY E 48   ? 0.9749 1.0684 1.0713 -0.0705 0.0998  -0.0763 48   GLY E O   
14318 N  N   . ARG E 49   ? 0.9272 1.0141 1.0186 -0.0667 0.0916  -0.0775 49   ARG E N   
14319 C  CA  . ARG E 49   ? 0.8749 0.9511 0.9587 -0.0578 0.0914  -0.0709 49   ARG E CA  
14320 C  C   . ARG E 49   ? 0.9246 1.0051 1.0102 -0.0503 0.0838  -0.0703 49   ARG E C   
14321 O  O   . ARG E 49   ? 1.0234 1.1014 1.1070 -0.0518 0.0810  -0.0729 49   ARG E O   
14322 C  CB  . ARG E 49   ? 0.8000 0.8543 0.8700 -0.0594 0.0973  -0.0672 49   ARG E CB  
14323 C  CG  . ARG E 49   ? 0.8065 0.8522 0.8710 -0.0598 0.1043  -0.0632 49   ARG E CG  
14324 C  CD  . ARG E 49   ? 0.9870 1.0110 1.0370 -0.0577 0.1085  -0.0584 49   ARG E CD  
14325 N  NE  . ARG E 49   ? 1.0704 1.0838 1.1141 -0.0641 0.1105  -0.0611 49   ARG E NE  
14326 C  CZ  . ARG E 49   ? 1.0016 1.0049 1.0395 -0.0724 0.1174  -0.0625 49   ARG E CZ  
14327 N  NH1 . ARG E 49   ? 1.0421 1.0441 1.0794 -0.0753 0.1234  -0.0612 49   ARG E NH1 
14328 N  NH2 . ARG E 49   ? 1.0543 1.0480 1.0866 -0.0779 0.1184  -0.0652 49   ARG E NH2 
14329 N  N   . SER E 50   ? 0.7993 0.8855 0.8880 -0.0422 0.0806  -0.0671 50   SER E N   
14330 C  CA  . SER E 50   ? 0.8551 0.9436 0.9446 -0.0347 0.0740  -0.0659 50   SER E CA  
14331 C  C   . SER E 50   ? 0.9824 1.0535 1.0608 -0.0307 0.0752  -0.0612 50   SER E C   
14332 O  O   . SER E 50   ? 0.9743 1.0434 1.0508 -0.0275 0.0711  -0.0613 50   SER E O   
14333 C  CB  . SER E 50   ? 0.7482 0.8480 0.8446 -0.0277 0.0704  -0.0641 50   SER E CB  
14334 O  OG  . SER E 50   ? 0.7495 0.8408 0.8409 -0.0235 0.0737  -0.0588 50   SER E OG  
14335 N  N   . SER E 51   ? 0.7879 0.8464 0.8587 -0.0306 0.0808  -0.0571 51   SER E N   
14336 C  CA  . SER E 51   ? 0.7035 0.7452 0.7634 -0.0272 0.0826  -0.0529 51   SER E CA  
14337 C  C   . SER E 51   ? 0.7627 0.7944 0.8161 -0.0335 0.0849  -0.0555 51   SER E C   
14338 O  O   . SER E 51   ? 0.8804 0.9135 0.9349 -0.0417 0.0879  -0.0594 51   SER E O   
14339 C  CB  . SER E 51   ? 0.6707 0.7021 0.7240 -0.0248 0.0878  -0.0479 51   SER E CB  
14340 O  OG  . SER E 51   ? 0.6335 0.6726 0.6918 -0.0180 0.0851  -0.0451 51   SER E OG  
14341 N  N   . ARG E 52   ? 0.7982 0.8198 0.8446 -0.0298 0.0835  -0.0535 52   ARG E N   
14342 C  CA  . ARG E 52   ? 0.8597 0.8727 0.9000 -0.0350 0.0844  -0.0565 52   ARG E CA  
14343 C  C   . ARG E 52   ? 0.8003 0.7932 0.8275 -0.0339 0.0895  -0.0524 52   ARG E C   
14344 O  O   . ARG E 52   ? 0.7314 0.7182 0.7546 -0.0267 0.0899  -0.0471 52   ARG E O   
14345 C  CB  . ARG E 52   ? 0.8550 0.8740 0.8981 -0.0320 0.0779  -0.0587 52   ARG E CB  
14346 C  CG  . ARG E 52   ? 0.7538 0.7921 0.8090 -0.0333 0.0727  -0.0635 52   ARG E CG  
14347 C  CD  . ARG E 52   ? 0.7839 0.8264 0.8415 -0.0427 0.0734  -0.0700 52   ARG E CD  
14348 N  NE  . ARG E 52   ? 0.7493 0.7954 0.8106 -0.0490 0.0781  -0.0713 52   ARG E NE  
14349 C  CZ  . ARG E 52   ? 0.9627 1.0071 1.0235 -0.0583 0.0817  -0.0756 52   ARG E CZ  
14350 N  NH1 . ARG E 52   ? 0.9724 1.0114 1.0290 -0.0626 0.0807  -0.0792 52   ARG E NH1 
14351 N  NH2 . ARG E 52   ? 1.0935 1.1415 1.1580 -0.0636 0.0864  -0.0763 52   ARG E NH2 
14352 N  N   . PRO E 53   ? 0.8207 0.8028 0.8407 -0.0409 0.0935  -0.0548 53   PRO E N   
14353 C  CA  . PRO E 53   ? 0.9074 0.8694 0.9138 -0.0396 0.0984  -0.0511 53   PRO E CA  
14354 C  C   . PRO E 53   ? 0.8668 0.8228 0.8684 -0.0336 0.0950  -0.0494 53   PRO E C   
14355 O  O   . PRO E 53   ? 0.8701 0.8361 0.8777 -0.0315 0.0892  -0.0516 53   PRO E O   
14356 C  CB  . PRO E 53   ? 0.8898 0.8437 0.8912 -0.0497 0.1031  -0.0552 53   PRO E CB  
14357 C  CG  . PRO E 53   ? 0.8723 0.8423 0.8845 -0.0552 0.0985  -0.0617 53   PRO E CG  
14358 C  CD  . PRO E 53   ? 0.7927 0.7808 0.8169 -0.0506 0.0940  -0.0612 53   PRO E CD  
14359 N  N   . ASN E 54   ? 1.0828 1.0217 1.0727 -0.0304 0.0990  -0.0452 54   ASN E N   
14360 C  CA  . ASN E 54   ? 1.0835 1.0156 1.0680 -0.0241 0.0968  -0.0429 54   ASN E CA  
14361 C  C   . ASN E 54   ? 1.0797 1.0070 1.0599 -0.0288 0.0956  -0.0474 54   ASN E C   
14362 O  O   . ASN E 54   ? 1.1248 1.0449 1.1002 -0.0366 0.0991  -0.0507 54   ASN E O   
14363 C  CB  . ASN E 54   ? 0.9884 0.9041 0.9618 -0.0190 0.1016  -0.0372 54   ASN E CB  
14364 C  CG  . ASN E 54   ? 1.1067 1.0281 1.0844 -0.0106 0.1001  -0.0322 54   ASN E CG  
14365 O  OD1 . ASN E 54   ? 1.2024 1.1385 1.1906 -0.0077 0.0951  -0.0327 54   ASN E OD1 
14366 N  ND2 . ASN E 54   ? 1.1737 1.0831 1.1431 -0.0065 0.1044  -0.0275 54   ASN E ND2 
14367 N  N   . VAL E 55   ? 1.0490 0.9801 1.0307 -0.0242 0.0907  -0.0476 55   VAL E N   
14368 C  CA  . VAL E 55   ? 1.0399 0.9643 1.0155 -0.0271 0.0894  -0.0513 55   VAL E CA  
14369 C  C   . VAL E 55   ? 1.0582 0.9618 1.0193 -0.0259 0.0947  -0.0483 55   VAL E C   
14370 O  O   . VAL E 55   ? 1.0896 0.9867 1.0467 -0.0187 0.0966  -0.0426 55   VAL E O   
14371 C  CB  . VAL E 55   ? 1.0601 0.9930 1.0400 -0.0213 0.0831  -0.0516 55   VAL E CB  
14372 C  CG1 . VAL E 55   ? 1.1166 1.0443 1.0905 -0.0244 0.0811  -0.0560 55   VAL E CG1 
14373 C  CG2 . VAL E 55   ? 1.1095 1.0624 1.1031 -0.0209 0.0781  -0.0536 55   VAL E CG2 
14374 N  N   . PRO E 56   ? 0.9604 0.8531 0.9135 -0.0328 0.0973  -0.0520 56   PRO E N   
14375 C  CA  . PRO E 56   ? 1.0509 0.9226 0.9895 -0.0323 0.1033  -0.0491 56   PRO E CA  
14376 C  C   . PRO E 56   ? 1.0911 0.9540 1.0227 -0.0227 0.1033  -0.0440 56   PRO E C   
14377 O  O   . PRO E 56   ? 1.0500 0.9050 0.9768 -0.0176 0.1070  -0.0386 56   PRO E O   
14378 C  CB  . PRO E 56   ? 1.1045 0.9689 1.0372 -0.0406 0.1038  -0.0551 56   PRO E CB  
14379 C  CG  . PRO E 56   ? 1.0522 0.9333 0.9971 -0.0480 0.1008  -0.0607 56   PRO E CG  
14380 C  CD  . PRO E 56   ? 0.9661 0.8656 0.9234 -0.0418 0.0952  -0.0592 56   PRO E CD  
14381 N  N   . GLY E 57   ? 0.9725 0.8369 0.9034 -0.0200 0.0992  -0.0454 57   GLY E N   
14382 C  CA  . GLY E 57   ? 0.9438 0.7989 0.8673 -0.0115 0.0998  -0.0409 57   GLY E CA  
14383 C  C   . GLY E 57   ? 0.9975 0.8648 0.9299 -0.0033 0.0958  -0.0373 57   GLY E C   
14384 O  O   . GLY E 57   ? 1.0683 0.9317 0.9970 0.0030  0.0949  -0.0349 57   GLY E O   
14385 N  N   . THR E 58   ? 1.2508 1.1324 1.1947 -0.0033 0.0939  -0.0368 58   THR E N   
14386 C  CA  . THR E 58   ? 1.1169 1.0111 1.0701 0.0035  0.0899  -0.0340 58   THR E CA  
14387 C  C   . THR E 58   ? 1.1734 1.0651 1.1267 0.0095  0.0928  -0.0282 58   THR E C   
14388 O  O   . THR E 58   ? 1.2813 1.1713 1.2343 0.0070  0.0960  -0.0274 58   THR E O   
14389 C  CB  . THR E 58   ? 1.1501 1.0623 1.1160 0.0002  0.0852  -0.0377 58   THR E CB  
14390 O  OG1 . THR E 58   ? 1.2297 1.1451 1.1957 -0.0045 0.0819  -0.0433 58   THR E OG1 
14391 C  CG2 . THR E 58   ? 1.3174 1.2414 1.2923 0.0073  0.0813  -0.0347 58   THR E CG2 
14392 N  N   . THR E 59   ? 1.0837 0.9754 1.0374 0.0173  0.0918  -0.0242 59   THR E N   
14393 C  CA  . THR E 59   ? 1.0712 0.9623 1.0260 0.0237  0.0937  -0.0189 59   THR E CA  
14394 C  C   . THR E 59   ? 1.1103 1.0161 1.0768 0.0286  0.0892  -0.0174 59   THR E C   
14395 O  O   . THR E 59   ? 1.1578 1.0697 1.1280 0.0292  0.0855  -0.0192 59   THR E O   
14396 C  CB  . THR E 59   ? 1.2953 1.1718 1.2395 0.0291  0.0975  -0.0151 59   THR E CB  
14397 O  OG1 . THR E 59   ? 1.3285 1.2056 1.2723 0.0325  0.0951  -0.0152 59   THR E OG1 
14398 C  CG2 . THR E 59   ? 1.3389 1.1993 1.2704 0.0246  0.1022  -0.0165 59   THR E CG2 
14399 N  N   . PRO E 60   ? 0.8974 0.8087 0.8694 0.0321  0.0895  -0.0142 60   PRO E N   
14400 C  CA  . PRO E 60   ? 0.8350 0.7599 0.8182 0.0362  0.0853  -0.0130 60   PRO E CA  
14401 C  C   . PRO E 60   ? 0.7876 0.7110 0.7704 0.0426  0.0846  -0.0102 60   PRO E C   
14402 O  O   . PRO E 60   ? 0.7651 0.6771 0.7390 0.0441  0.0871  -0.0092 60   PRO E O   
14403 C  CB  . PRO E 60   ? 0.7121 0.6405 0.6990 0.0383  0.0865  -0.0104 60   PRO E CB  
14404 C  CG  . PRO E 60   ? 0.7738 0.6935 0.7533 0.0334  0.0906  -0.0114 60   PRO E CG  
14405 C  CD  . PRO E 60   ? 0.9070 0.8128 0.8754 0.0317  0.0934  -0.0122 60   PRO E CD  
14406 N  N   . PHE E 61   ? 0.7703 0.7048 0.7628 0.0464  0.0813  -0.0089 61   PHE E N   
14407 C  CA  . PHE E 61   ? 0.7215 0.6559 0.7151 0.0521  0.0807  -0.0062 61   PHE E CA  
14408 C  C   . PHE E 61   ? 0.6923 0.6214 0.6837 0.0577  0.0840  -0.0016 61   PHE E C   
14409 O  O   . PHE E 61   ? 0.7398 0.6723 0.7347 0.0590  0.0844  0.0000  61   PHE E O   
14410 C  CB  . PHE E 61   ? 0.6882 0.6359 0.6927 0.0536  0.0762  -0.0067 61   PHE E CB  
14411 C  CG  . PHE E 61   ? 0.7665 0.7144 0.7726 0.0590  0.0758  -0.0041 61   PHE E CG  
14412 C  CD1 . PHE E 61   ? 0.7881 0.7282 0.7870 0.0598  0.0768  -0.0044 61   PHE E CD1 
14413 C  CD2 . PHE E 61   ? 0.6146 0.5701 0.6292 0.0631  0.0746  -0.0015 61   PHE E CD2 
14414 C  CE1 . PHE E 61   ? 0.8013 0.7412 0.8015 0.0647  0.0770  -0.0019 61   PHE E CE1 
14415 C  CE2 . PHE E 61   ? 0.6193 0.5750 0.6358 0.0676  0.0748  0.0008  61   PHE E CE2 
14416 C  CZ  . PHE E 61   ? 0.7433 0.6911 0.7525 0.0684  0.0761  0.0008  61   PHE E CZ  
14417 N  N   . GLU E 62   ? 0.8884 0.8093 0.8739 0.0615  0.0862  0.0004  62   GLU E N   
14418 C  CA  . GLU E 62   ? 0.8930 0.8092 0.8764 0.0675  0.0893  0.0048  62   GLU E CA  
14419 C  C   . GLU E 62   ? 0.9456 0.8538 0.9223 0.0671  0.0927  0.0058  62   GLU E C   
14420 O  O   . GLU E 62   ? 0.9712 0.8797 0.9491 0.0719  0.0942  0.0090  62   GLU E O   
14421 C  CB  . GLU E 62   ? 0.9080 0.8358 0.9029 0.0718  0.0871  0.0070  62   GLU E CB  
14422 C  CG  . GLU E 62   ? 1.1633 1.0939 1.1616 0.0750  0.0861  0.0081  62   GLU E CG  
14423 C  CD  . GLU E 62   ? 1.2219 1.1636 1.2317 0.0785  0.0841  0.0101  62   GLU E CD  
14424 O  OE1 . GLU E 62   ? 1.3332 1.2814 1.3487 0.0783  0.0827  0.0102  62   GLU E OE1 
14425 O  OE2 . GLU E 62   ? 1.1822 1.1259 1.1952 0.0814  0.0840  0.0114  62   GLU E OE2 
14426 N  N   . VAL E 63   ? 0.9298 0.8307 0.8991 0.0615  0.0941  0.0031  63   VAL E N   
14427 C  CA  . VAL E 63   ? 0.9395 0.8305 0.9003 0.0605  0.0980  0.0039  63   VAL E CA  
14428 C  C   . VAL E 63   ? 0.9766 0.8525 0.9246 0.0588  0.1014  0.0029  63   VAL E C   
14429 O  O   . VAL E 63   ? 1.0729 0.9462 1.0178 0.0524  0.1008  -0.0009 63   VAL E O   
14430 C  CB  . VAL E 63   ? 0.9165 0.8122 0.8803 0.0547  0.0971  0.0013  63   VAL E CB  
14431 C  CG1 . VAL E 63   ? 0.9612 0.8445 0.9146 0.0534  0.1018  0.0022  63   VAL E CG1 
14432 C  CG2 . VAL E 63   ? 0.8671 0.7771 0.8429 0.0569  0.0937  0.0023  63   VAL E CG2 
14433 N  N   . VAL E 64   ? 0.6809 0.5469 0.6215 0.0644  0.1048  0.0063  64   VAL E N   
14434 C  CA  . VAL E 64   ? 0.7916 0.6425 0.7194 0.0639  0.1082  0.0058  64   VAL E CA  
14435 C  C   . VAL E 64   ? 0.8912 0.7286 0.8078 0.0622  0.1127  0.0062  64   VAL E C   
14436 O  O   . VAL E 64   ? 0.9273 0.7641 0.8436 0.0661  0.1144  0.0092  64   VAL E O   
14437 C  CB  . VAL E 64   ? 0.7818 0.6295 0.7075 0.0714  0.1096  0.0091  64   VAL E CB  
14438 C  CG1 . VAL E 64   ? 0.7730 0.6216 0.7002 0.0784  0.1115  0.0136  64   VAL E CG1 
14439 C  CG2 . VAL E 64   ? 0.9564 0.7882 0.8684 0.0710  0.1129  0.0083  64   VAL E CG2 
14440 N  N   . LYS E 65   ? 1.1832 1.0097 1.0904 0.0564  0.1145  0.0030  65   LYS E N   
14441 C  CA  . LYS E 65   ? 1.3027 1.1144 1.1979 0.0537  0.1192  0.0030  65   LYS E CA  
14442 C  C   . LYS E 65   ? 1.3677 1.1620 1.2488 0.0576  0.1236  0.0048  65   LYS E C   
14443 O  O   . LYS E 65   ? 1.4040 1.1837 1.2733 0.0533  0.1271  0.0031  65   LYS E O   
14444 C  CB  . LYS E 65   ? 1.4695 1.2803 1.3638 0.0437  0.1187  -0.0021 65   LYS E CB  
14445 C  CG  . LYS E 65   ? 1.4011 1.2171 1.2999 0.0397  0.1191  -0.0026 65   LYS E CG  
14446 C  CD  . LYS E 65   ? 1.3434 1.1785 1.2574 0.0416  0.1144  -0.0020 65   LYS E CD  
14447 C  CE  . LYS E 65   ? 1.4201 1.2618 1.3392 0.0355  0.1140  -0.0042 65   LYS E CE  
14448 N  NZ  . LYS E 65   ? 1.4792 1.3399 1.4133 0.0361  0.1088  -0.0049 65   LYS E NZ  
14449 N  N   . THR E 66   ? 1.2141 1.0095 1.0960 0.0657  0.1237  0.0083  66   THR E N   
14450 C  CA  . THR E 66   ? 1.3374 1.1171 1.2062 0.0699  0.1277  0.0099  66   THR E CA  
14451 C  C   . THR E 66   ? 1.4504 1.2165 1.3082 0.0734  0.1328  0.0129  66   THR E C   
14452 O  O   . THR E 66   ? 1.5699 1.3188 1.4135 0.0715  0.1368  0.0120  66   THR E O   
14453 C  CB  . THR E 66   ? 1.3766 1.1625 1.2504 0.0776  0.1266  0.0127  66   THR E CB  
14454 O  OG1 . THR E 66   ? 1.3084 1.1006 1.1870 0.0743  0.1231  0.0098  66   THR E OG1 
14455 C  CG2 . THR E 66   ? 1.4666 1.2371 1.3274 0.0840  0.1314  0.0156  66   THR E CG2 
14456 N  N   . ASP E 67   ? 1.6329 1.4060 1.4963 0.0787  0.1326  0.0163  67   ASP E N   
14457 C  CA  . ASP E 67   ? 1.6633 1.4240 1.5160 0.0833  0.1372  0.0194  67   ASP E CA  
14458 C  C   . ASP E 67   ? 1.6587 1.4087 1.5028 0.0759  0.1399  0.0172  67   ASP E C   
14459 O  O   . ASP E 67   ? 1.6443 1.4034 1.4963 0.0695  0.1376  0.0148  67   ASP E O   
14460 C  CB  . ASP E 67   ? 1.7129 1.4854 1.5746 0.0902  0.1356  0.0230  67   ASP E CB  
14461 C  CG  . ASP E 67   ? 1.7163 1.4765 1.5666 0.0967  0.1400  0.0266  67   ASP E CG  
14462 O  OD1 . ASP E 67   ? 1.6167 1.3599 1.4528 0.0987  0.1444  0.0274  67   ASP E OD1 
14463 O  OD2 . ASP E 67   ? 1.6910 1.4582 1.5460 0.1000  0.1391  0.0286  67   ASP E OD2 
14464 N  N   . GLU E 68   ? 1.5009 1.2309 1.3285 0.0766  0.1452  0.0179  68   GLU E N   
14465 C  CA  . GLU E 68   ? 1.5757 1.2932 1.3938 0.0692  0.1487  0.0158  68   GLU E CA  
14466 C  C   . GLU E 68   ? 1.6448 1.3600 1.4602 0.0724  0.1510  0.0188  68   GLU E C   
14467 O  O   . GLU E 68   ? 1.6192 1.3355 1.4359 0.0658  0.1515  0.0170  68   GLU E O   
14468 C  CB  . GLU E 68   ? 1.6193 1.3150 1.4200 0.0681  0.1535  0.0149  68   GLU E CB  
14469 C  CG  . GLU E 68   ? 1.6410 1.3370 1.4426 0.0627  0.1513  0.0108  68   GLU E CG  
14470 C  CD  . GLU E 68   ? 1.6030 1.3097 1.4142 0.0522  0.1477  0.0057  68   GLU E CD  
14471 O  OE1 . GLU E 68   ? 1.7261 1.4287 1.5348 0.0457  0.1498  0.0041  68   GLU E OE1 
14472 O  OE2 . GLU E 68   ? 1.5792 1.2986 1.4004 0.0505  0.1429  0.0033  68   GLU E OE2 
14473 N  N   . PHE E 69   ? 2.0474 1.7596 1.8588 0.0827  0.1526  0.0235  69   PHE E N   
14474 C  CA  . PHE E 69   ? 2.0200 1.7303 1.8284 0.0869  0.1545  0.0265  69   PHE E CA  
14475 C  C   . PHE E 69   ? 1.8965 1.6261 1.7203 0.0845  0.1499  0.0257  69   PHE E C   
14476 O  O   . PHE E 69   ? 1.9006 1.6281 1.7219 0.0832  0.1515  0.0264  69   PHE E O   
14477 C  CB  . PHE E 69   ? 2.1274 1.8345 1.9311 0.0992  0.1558  0.0313  69   PHE E CB  
14478 C  CG  . PHE E 69   ? 2.2359 1.9200 2.0203 0.1027  0.1618  0.0330  69   PHE E CG  
14479 C  CD1 . PHE E 69   ? 2.1118 1.7798 1.8821 0.1031  0.1667  0.0345  69   PHE E CD1 
14480 C  CD2 . PHE E 69   ? 2.4382 2.1161 2.2178 0.1057  0.1628  0.0331  69   PHE E CD2 
14481 C  CE1 . PHE E 69   ? 2.3699 2.0157 2.1216 0.1065  0.1724  0.0361  69   PHE E CE1 
14482 C  CE2 . PHE E 69   ? 2.5247 2.1808 2.2860 0.1092  0.1684  0.0345  69   PHE E CE2 
14483 C  CZ  . PHE E 69   ? 2.5363 2.1761 2.2834 0.1096  0.1732  0.0360  69   PHE E CZ  
14484 N  N   . LEU E 70   ? 1.6259 1.3737 1.4653 0.0840  0.1445  0.0244  70   LEU E N   
14485 C  CA  . LEU E 70   ? 1.6133 1.3792 1.4673 0.0814  0.1400  0.0232  70   LEU E CA  
14486 C  C   . LEU E 70   ? 1.6755 1.4416 1.5307 0.0704  0.1401  0.0191  70   LEU E C   
14487 O  O   . LEU E 70   ? 1.7359 1.5139 1.6003 0.0679  0.1377  0.0183  70   LEU E O   
14488 C  CB  . LEU E 70   ? 1.6099 1.3937 1.4792 0.0834  0.1345  0.0227  70   LEU E CB  
14489 C  CG  . LEU E 70   ? 1.5257 1.3285 1.4100 0.0851  0.1298  0.0232  70   LEU E CG  
14490 C  CD1 . LEU E 70   ? 1.4357 1.2370 1.3167 0.0928  0.1311  0.0270  70   LEU E CD1 
14491 C  CD2 . LEU E 70   ? 1.5557 1.3734 1.4533 0.0875  0.1252  0.0230  70   LEU E CD2 
14492 N  N   . TYR E 71   ? 1.3097 1.0632 1.1559 0.0638  0.1430  0.0163  71   TYR E N   
14493 C  CA  . TYR E 71   ? 1.2777 1.0324 1.1260 0.0529  0.1430  0.0119  71   TYR E CA  
14494 C  C   . TYR E 71   ? 1.2977 1.0318 1.1301 0.0475  0.1492  0.0108  71   TYR E C   
14495 O  O   . TYR E 71   ? 1.3658 1.1005 1.1997 0.0382  0.1500  0.0072  71   TYR E O   
14496 C  CB  . TYR E 71   ? 1.1319 0.8967 0.9893 0.0478  0.1386  0.0078  71   TYR E CB  
14497 C  CG  . TYR E 71   ? 1.1337 0.9195 1.0077 0.0510  0.1325  0.0081  71   TYR E CG  
14498 C  CD1 . TYR E 71   ? 1.1703 0.9707 1.0559 0.0470  0.1294  0.0064  71   TYR E CD1 
14499 C  CD2 . TYR E 71   ? 1.1511 0.9416 1.0288 0.0580  0.1302  0.0102  71   TYR E CD2 
14500 C  CE1 . TYR E 71   ? 1.2186 1.0371 1.1186 0.0499  0.1239  0.0066  71   TYR E CE1 
14501 C  CE2 . TYR E 71   ? 1.2381 1.0469 1.1306 0.0606  0.1250  0.0105  71   TYR E CE2 
14502 C  CZ  . TYR E 71   ? 1.2296 1.0519 1.1329 0.0566  0.1218  0.0087  71   TYR E CZ  
14503 O  OH  . TYR E 71   ? 1.0260 0.8654 0.9433 0.0592  0.1168  0.0089  71   TYR E OH  
14504 N  N   . THR E 72   ? 1.6369 1.3531 1.4545 0.0528  0.1538  0.0136  72   THR E N   
14505 C  CA  . THR E 72   ? 1.7514 1.4464 1.5527 0.0481  0.1602  0.0129  72   THR E CA  
14506 C  C   . THR E 72   ? 1.8517 1.5303 1.6383 0.0578  0.1647  0.0178  72   THR E C   
14507 O  O   . THR E 72   ? 1.8803 1.5616 1.6679 0.0667  0.1631  0.0206  72   THR E O   
14508 C  CB  . THR E 72   ? 1.8229 1.5097 1.6196 0.0399  0.1609  0.0083  72   THR E CB  
14509 O  OG1 . THR E 72   ? 1.9485 1.6158 1.7308 0.0337  0.1672  0.0070  72   THR E OG1 
14510 C  CG2 . THR E 72   ? 1.8118 1.4927 1.6032 0.0463  0.1604  0.0095  72   THR E CG2 
14511 N  N   . GLY E 73   ? 1.5523 1.2141 1.3253 0.0561  0.1707  0.0189  73   GLY E N   
14512 C  CA  . GLY E 73   ? 1.6129 1.2579 1.3706 0.0654  0.1753  0.0236  73   GLY E CA  
14513 C  C   . GLY E 73   ? 1.7817 1.4062 1.5237 0.0662  0.1795  0.0234  73   GLY E C   
14514 O  O   . GLY E 73   ? 1.8796 1.4878 1.6069 0.0737  0.1840  0.0271  73   GLY E O   
14515 N  N   . LEU E 74   ? 1.2962 0.9210 1.0406 0.0590  0.1780  0.0191  74   LEU E N   
14516 C  CA  . LEU E 74   ? 1.3795 0.9841 1.1084 0.0585  0.1819  0.0182  74   LEU E CA  
14517 C  C   . LEU E 74   ? 1.4008 1.0118 1.1338 0.0657  0.1785  0.0191  74   LEU E C   
14518 O  O   . LEU E 74   ? 1.4944 1.1243 1.2429 0.0641  0.1727  0.0172  74   LEU E O   
14519 C  CB  . LEU E 74   ? 1.4834 1.0817 1.2102 0.0451  0.1831  0.0124  74   LEU E CB  
14520 C  CG  . LEU E 74   ? 1.3508 0.9415 1.0731 0.0368  0.1874  0.0111  74   LEU E CG  
14521 C  CD1 . LEU E 74   ? 1.3554 0.9435 1.0786 0.0231  0.1878  0.0046  74   LEU E CD1 
14522 C  CD2 . LEU E 74   ? 1.3485 0.9150 1.0507 0.0418  0.1949  0.0151  74   LEU E CD2 
14523 N  N   . ILE E 75   ? 1.7770 1.3717 1.4957 0.0738  0.1823  0.0222  75   ILE E N   
14524 C  CA  . ILE E 75   ? 1.8722 1.4704 1.5926 0.0809  0.1802  0.0233  75   ILE E CA  
14525 C  C   . ILE E 75   ? 1.9654 1.5476 1.6743 0.0754  0.1824  0.0197  75   ILE E C   
14526 O  O   . ILE E 75   ? 2.0493 1.6368 1.7621 0.0768  0.1796  0.0184  75   ILE E O   
14527 C  CB  . ILE E 75   ? 1.8373 1.4303 1.5508 0.0946  0.1824  0.0290  75   ILE E CB  
14528 C  CG1 . ILE E 75   ? 1.9065 1.5118 1.6288 0.1021  0.1789  0.0304  75   ILE E CG1 
14529 C  CG2 . ILE E 75   ? 1.8648 1.4301 1.5555 0.0973  0.1895  0.0305  75   ILE E CG2 
14530 C  CD1 . ILE E 75   ? 1.8917 1.4944 1.6091 0.1157  0.1808  0.0358  75   ILE E CD1 
14531 N  N   . ASP E 76   ? 2.1142 1.6763 1.8084 0.0690  0.1876  0.0179  76   ASP E N   
14532 C  CA  . ASP E 76   ? 2.1645 1.7100 1.8468 0.0627  0.1900  0.0140  76   ASP E CA  
14533 C  C   . ASP E 76   ? 2.1169 1.6496 1.7917 0.0509  0.1937  0.0103  76   ASP E C   
14534 O  O   . ASP E 76   ? 2.2105 1.7226 1.8701 0.0466  0.1978  0.0079  76   ASP E O   
14535 C  CB  . ASP E 76   ? 2.2225 1.7476 1.8869 0.0720  0.1947  0.0172  76   ASP E CB  
14536 C  CG  . ASP E 76   ? 2.3411 1.8757 2.0112 0.0799  0.1913  0.0184  76   ASP E CG  
14537 O  OD1 . ASP E 76   ? 2.3522 1.9016 2.0347 0.0751  0.1861  0.0150  76   ASP E OD1 
14538 O  OD2 . ASP E 76   ? 2.3912 1.9182 2.0531 0.0911  0.1939  0.0228  76   ASP E OD2 
14539 N  N   . GLY E 77   ? 1.5351 1.0792 1.2200 0.0453  0.1926  0.0096  77   GLY E N   
14540 C  CA  . GLY E 77   ? 1.5795 1.1118 1.2575 0.0349  0.1970  0.0069  77   GLY E CA  
14541 C  C   . GLY E 77   ? 1.6273 1.1447 1.2927 0.0395  0.2032  0.0114  77   GLY E C   
14542 O  O   . GLY E 77   ? 1.5948 1.1004 1.2530 0.0311  0.2079  0.0097  77   GLY E O   
14543 N  N   . GLN E 78   ? 2.2939 1.8116 1.9564 0.0526  0.2035  0.0172  78   GLN E N   
14544 C  CA  . GLN E 78   ? 2.3163 1.8199 1.9660 0.0590  0.2090  0.0220  78   GLN E CA  
14545 C  C   . GLN E 78   ? 2.2216 1.7443 1.8835 0.0686  0.2050  0.0263  78   GLN E C   
14546 O  O   . GLN E 78   ? 2.1833 1.7275 1.8616 0.0716  0.1986  0.0261  78   GLN E O   
14547 C  CB  . GLN E 78   ? 2.3549 1.8334 1.9833 0.0670  0.2144  0.0249  78   GLN E CB  
14548 C  CG  . GLN E 78   ? 2.4679 1.9269 2.0835 0.0584  0.2180  0.0205  78   GLN E CG  
14549 C  CD  . GLN E 78   ? 2.5751 2.0086 2.1689 0.0669  0.2236  0.0236  78   GLN E CD  
14550 O  OE1 . GLN E 78   ? 2.6178 2.0426 2.2020 0.0771  0.2270  0.0289  78   GLN E OE1 
14551 N  NE2 . GLN E 78   ? 2.5186 1.9397 2.1040 0.0630  0.2247  0.0202  78   GLN E NE2 
14552 N  N   . GLU E 79   ? 1.9009 1.4151 1.5541 0.0734  0.2089  0.0302  79   GLU E N   
14553 C  CA  . GLU E 79   ? 1.8163 1.3466 1.4791 0.0828  0.2055  0.0343  79   GLU E CA  
14554 C  C   . GLU E 79   ? 1.8049 1.3337 1.4632 0.0971  0.2048  0.0386  79   GLU E C   
14555 O  O   . GLU E 79   ? 1.9200 1.4312 1.5641 0.1006  0.2084  0.0392  79   GLU E O   
14556 C  CB  . GLU E 79   ? 1.8207 1.3419 1.4750 0.0828  0.2100  0.0367  79   GLU E CB  
14557 C  CG  . GLU E 79   ? 1.7757 1.3104 1.4427 0.0721  0.2082  0.0336  79   GLU E CG  
14558 C  CD  . GLU E 79   ? 1.7612 1.2826 1.4217 0.0581  0.2127  0.0290  79   GLU E CD  
14559 O  OE1 . GLU E 79   ? 1.8508 1.3608 1.5043 0.0544  0.2142  0.0264  79   GLU E OE1 
14560 O  OE2 . GLU E 79   ? 1.6706 1.1933 1.3332 0.0506  0.2148  0.0278  79   GLU E OE2 
14561 N  N   . VAL E 80   ? 1.5109 1.0588 1.1817 0.1055  0.2001  0.0414  80   VAL E N   
14562 C  CA  . VAL E 80   ? 1.5180 1.0702 1.1893 0.1185  0.1983  0.0450  80   VAL E CA  
14563 C  C   . VAL E 80   ? 1.5318 1.0842 1.1988 0.1303  0.1990  0.0500  80   VAL E C   
14564 O  O   . VAL E 80   ? 1.6125 1.1607 1.2732 0.1419  0.1997  0.0533  80   VAL E O   
14565 C  CB  . VAL E 80   ? 1.5370 1.1147 1.2296 0.1186  0.1911  0.0433  80   VAL E CB  
14566 C  CG1 . VAL E 80   ? 1.6958 1.2743 1.3927 0.1072  0.1899  0.0382  80   VAL E CG1 
14567 C  CG2 . VAL E 80   ? 1.5558 1.1562 1.2658 0.1185  0.1859  0.0436  80   VAL E CG2 
14568 N  N   . ASP E 81   ? 1.6887 1.2458 1.3585 0.1282  0.1987  0.0505  81   ASP E N   
14569 C  CA  . ASP E 81   ? 1.7104 1.2716 1.3788 0.1394  0.1980  0.0548  81   ASP E CA  
14570 C  C   . ASP E 81   ? 1.7096 1.2934 1.3942 0.1484  0.1915  0.0562  81   ASP E C   
14571 O  O   . ASP E 81   ? 1.6193 1.2011 1.2986 0.1608  0.1918  0.0598  81   ASP E O   
14572 C  CB  . ASP E 81   ? 1.7976 1.3329 1.4421 0.1478  0.2048  0.0586  81   ASP E CB  
14573 C  CG  . ASP E 81   ? 1.8180 1.3516 1.4567 0.1547  0.2058  0.0621  81   ASP E CG  
14574 O  OD1 . ASP E 81   ? 1.6820 1.2351 1.3332 0.1623  0.2003  0.0637  81   ASP E OD1 
14575 O  OD2 . ASP E 81   ? 1.8353 1.3478 1.4565 0.1525  0.2120  0.0632  81   ASP E OD2 
14576 N  N   . ALA E 82   ? 1.5024 1.1081 1.2072 0.1421  0.1857  0.0532  82   ALA E N   
14577 C  CA  . ALA E 82   ? 1.4144 1.0429 1.1366 0.1487  0.1795  0.0539  82   ALA E CA  
14578 C  C   . ALA E 82   ? 1.3286 0.9790 1.0705 0.1408  0.1738  0.0510  82   ALA E C   
14579 O  O   . ALA E 82   ? 1.3005 0.9486 1.0426 0.1305  0.1748  0.0482  82   ALA E O   
14580 C  CB  . ALA E 82   ? 1.4251 1.0536 1.1488 0.1510  0.1792  0.0535  82   ALA E CB  
14581 N  N   . MET E 83   ? 1.7500 1.4220 1.5086 0.1458  0.1680  0.0514  83   MET E N   
14582 C  CA  . MET E 83   ? 1.8105 1.5038 1.5878 0.1400  0.1624  0.0490  83   MET E CA  
14583 C  C   . MET E 83   ? 1.9108 1.6211 1.7041 0.1401  0.1577  0.0477  83   MET E C   
14584 O  O   . MET E 83   ? 2.0133 1.7268 1.8079 0.1491  0.1571  0.0499  83   MET E O   
14585 C  CB  . MET E 83   ? 1.7178 1.4212 1.4997 0.1464  0.1597  0.0512  83   MET E CB  
14586 C  CG  . MET E 83   ? 1.7006 1.4229 1.4990 0.1399  0.1546  0.0486  83   MET E CG  
14587 S  SD  . MET E 83   ? 1.9295 1.6600 1.7298 0.1474  0.1522  0.0510  83   MET E SD  
14588 C  CE  . MET E 83   ? 1.6182 1.3704 1.4384 0.1384  0.1464  0.0474  83   MET E CE  
14589 N  N   . PRO E 84   ? 1.4763 1.1975 1.2816 0.1305  0.1545  0.0440  84   PRO E N   
14590 C  CA  . PRO E 84   ? 1.3358 1.0704 1.1541 0.1302  0.1508  0.0427  84   PRO E CA  
14591 C  C   . PRO E 84   ? 1.3444 1.0974 1.1765 0.1385  0.1463  0.0447  84   PRO E C   
14592 O  O   . PRO E 84   ? 1.4015 1.1598 1.2387 0.1425  0.1454  0.0454  84   PRO E O   
14593 C  CB  . PRO E 84   ? 1.2879 1.0311 1.1160 0.1186  0.1480  0.0385  84   PRO E CB  
14594 C  CG  . PRO E 84   ? 1.3619 1.1033 1.1874 0.1147  0.1487  0.0380  84   PRO E CG  
14595 C  CD  . PRO E 84   ? 1.3830 1.1042 1.1899 0.1196  0.1545  0.0409  84   PRO E CD  
14596 N  N   . PHE E 85   ? 1.2238 0.9870 1.0623 0.1409  0.1436  0.0455  85   PHE E N   
14597 C  CA  . PHE E 85   ? 1.2255 1.0066 1.0775 0.1483  0.1391  0.0470  85   PHE E CA  
14598 C  C   . PHE E 85   ? 1.3355 1.1135 1.1806 0.1574  0.1399  0.0500  85   PHE E C   
14599 O  O   . PHE E 85   ? 1.4111 1.1765 1.2440 0.1561  0.1429  0.0505  85   PHE E O   
14600 C  CB  . PHE E 85   ? 1.1286 0.9294 0.9985 0.1425  0.1335  0.0444  85   PHE E CB  
14601 C  CG  . PHE E 85   ? 1.1275 0.9258 0.9957 0.1338  0.1336  0.0421  85   PHE E CG  
14602 C  CD1 . PHE E 85   ? 1.1871 0.9850 1.0521 0.1358  0.1335  0.0431  85   PHE E CD1 
14603 C  CD2 . PHE E 85   ? 1.1467 0.9432 1.0164 0.1238  0.1338  0.0389  85   PHE E CD2 
14604 C  CE1 . PHE E 85   ? 1.1624 0.9583 1.0260 0.1278  0.1340  0.0410  85   PHE E CE1 
14605 C  CE2 . PHE E 85   ? 1.1715 0.9668 1.0404 0.1157  0.1340  0.0366  85   PHE E CE2 
14606 C  CZ  . PHE E 85   ? 1.1353 0.9303 1.0013 0.1177  0.1344  0.0377  85   PHE E CZ  
14607 N  N   . PRO E 86   ? 1.3211 1.1101 1.1734 0.1668  0.1374  0.0520  86   PRO E N   
14608 C  CA  . PRO E 86   ? 1.3178 1.1046 1.1635 0.1764  0.1377  0.0548  86   PRO E CA  
14609 C  C   . PRO E 86   ? 1.3738 1.1670 1.2229 0.1739  0.1349  0.0539  86   PRO E C   
14610 O  O   . PRO E 86   ? 1.3207 1.1263 1.1824 0.1665  0.1313  0.0513  86   PRO E O   
14611 C  CB  . PRO E 86   ? 1.1874 0.9897 1.0450 0.1852  0.1344  0.0560  86   PRO E CB  
14612 C  CG  . PRO E 86   ? 1.2814 1.0855 1.1446 0.1816  0.1351  0.0550  86   PRO E CG  
14613 C  CD  . PRO E 86   ? 1.2624 1.0651 1.1280 0.1694  0.1348  0.0519  86   PRO E CD  
14614 N  N   . VAL E 87   ? 1.5058 1.2900 1.3428 0.1808  0.1367  0.0563  87   VAL E N   
14615 C  CA  . VAL E 87   ? 1.4280 1.2156 1.2652 0.1796  0.1348  0.0559  87   VAL E CA  
14616 C  C   . VAL E 87   ? 1.3388 1.1479 1.1917 0.1854  0.1283  0.0557  87   VAL E C   
14617 O  O   . VAL E 87   ? 1.4262 1.2413 1.2820 0.1948  0.1267  0.0573  87   VAL E O   
14618 C  CB  . VAL E 87   ? 1.3045 1.0721 1.1208 0.1850  0.1398  0.0587  87   VAL E CB  
14619 C  CG1 . VAL E 87   ? 1.3204 1.0917 1.1363 0.1849  0.1379  0.0586  87   VAL E CG1 
14620 C  CG2 . VAL E 87   ? 1.2599 1.0058 1.0609 0.1781  0.1464  0.0584  87   VAL E CG2 
14621 N  N   . THR E 88   ? 1.3888 1.2099 1.2522 0.1797  0.1244  0.0535  88   THR E N   
14622 C  CA  . THR E 88   ? 1.4517 1.2928 1.3299 0.1840  0.1180  0.0527  88   THR E CA  
14623 C  C   . THR E 88   ? 1.4832 1.3233 1.3565 0.1844  0.1169  0.0527  88   THR E C   
14624 O  O   . THR E 88   ? 1.5155 1.3434 1.3788 0.1783  0.1206  0.0524  88   THR E O   
14625 C  CB  . THR E 88   ? 1.5078 1.3664 1.4054 0.1768  0.1135  0.0498  88   THR E CB  
14626 O  OG1 . THR E 88   ? 1.6063 1.4612 1.5050 0.1736  0.1160  0.0495  88   THR E OG1 
14627 C  CG2 . THR E 88   ? 1.4793 1.3580 1.3924 0.1828  0.1075  0.0493  88   THR E CG2 
14628 N  N   . LYS E 89   ? 1.5992 1.4523 1.4795 0.1918  0.1120  0.0529  89   LYS E N   
14629 C  CA  . LYS E 89   ? 1.5562 1.4097 1.4325 0.1929  0.1104  0.0528  89   LYS E CA  
14630 C  C   . LYS E 89   ? 1.5861 1.4466 1.4713 0.1821  0.1087  0.0498  89   LYS E C   
14631 O  O   . LYS E 89   ? 1.6521 1.5041 1.5284 0.1786  0.1110  0.0498  89   LYS E O   
14632 C  CB  . LYS E 89   ? 1.6694 1.5373 1.5529 0.2027  0.1047  0.0531  89   LYS E CB  
14633 C  CG  . LYS E 89   ? 1.7827 1.6479 1.6579 0.2066  0.1036  0.0536  89   LYS E CG  
14634 C  CD  . LYS E 89   ? 1.7283 1.5701 1.5806 0.2095  0.1103  0.0566  89   LYS E CD  
14635 C  CE  . LYS E 89   ? 1.7537 1.5915 1.5970 0.2120  0.1100  0.0571  89   LYS E CE  
14636 N  NZ  . LYS E 89   ? 1.8781 1.7287 1.7260 0.2227  0.1039  0.0572  89   LYS E NZ  
14637 N  N   . ASP E 90   ? 1.4197 1.2955 1.3223 0.1768  0.1048  0.0473  90   ASP E N   
14638 C  CA  . ASP E 90   ? 1.4283 1.3104 1.3393 0.1666  0.1033  0.0444  90   ASP E CA  
14639 C  C   . ASP E 90   ? 1.2857 1.1525 1.1867 0.1582  0.1091  0.0441  90   ASP E C   
14640 O  O   . ASP E 90   ? 1.1678 1.0333 1.0681 0.1511  0.1099  0.0425  90   ASP E O   
14641 C  CB  . ASP E 90   ? 1.3763 1.2763 1.3066 0.1634  0.0984  0.0421  90   ASP E CB  
14642 C  CG  . ASP E 90   ? 1.4450 1.3616 1.3869 0.1700  0.0923  0.0416  90   ASP E CG  
14643 O  OD1 . ASP E 90   ? 1.4450 1.3606 1.3808 0.1763  0.0911  0.0426  90   ASP E OD1 
14644 O  OD2 . ASP E 90   ? 1.6154 1.5459 1.5725 0.1688  0.0886  0.0401  90   ASP E OD2 
14645 N  N   . LEU E 91   ? 1.1266 0.9821 1.0201 0.1587  0.1132  0.0455  91   LEU E N   
14646 C  CA  . LEU E 91   ? 1.1891 1.0291 1.0722 0.1509  0.1188  0.0450  91   LEU E CA  
14647 C  C   . LEU E 91   ? 1.1823 1.0061 1.0484 0.1514  0.1236  0.0466  91   LEU E C   
14648 O  O   . LEU E 91   ? 1.1705 0.9872 1.0324 0.1428  0.1267  0.0451  91   LEU E O   
14649 C  CB  . LEU E 91   ? 1.2277 1.0586 1.1057 0.1524  0.1220  0.0461  91   LEU E CB  
14650 C  CG  . LEU E 91   ? 1.1923 1.0073 1.0602 0.1443  0.1274  0.0452  91   LEU E CG  
14651 C  CD1 . LEU E 91   ? 1.0905 0.9154 0.9707 0.1338  0.1251  0.0416  91   LEU E CD1 
14652 C  CD2 . LEU E 91   ? 1.2805 1.0847 1.1404 0.1486  0.1307  0.0470  91   LEU E CD2 
14653 N  N   . LEU E 92   ? 1.0051 0.8229 0.8614 0.1615  0.1243  0.0495  92   LEU E N   
14654 C  CA  . LEU E 92   ? 1.0137 0.8156 0.8530 0.1628  0.1290  0.0513  92   LEU E CA  
14655 C  C   . LEU E 92   ? 1.0273 0.8378 0.8717 0.1594  0.1265  0.0498  92   LEU E C   
14656 O  O   . LEU E 92   ? 1.0226 0.8216 0.8568 0.1545  0.1309  0.0498  92   LEU E O   
14657 C  CB  . LEU E 92   ? 1.1138 0.9078 0.9411 0.1755  0.1299  0.0549  92   LEU E CB  
14658 C  CG  . LEU E 92   ? 1.0818 0.8583 0.8953 0.1790  0.1353  0.0572  92   LEU E CG  
14659 C  CD1 . LEU E 92   ? 1.0953 0.8666 0.8986 0.1927  0.1354  0.0605  92   LEU E CD1 
14660 C  CD2 . LEU E 92   ? 0.8972 0.6526 0.6952 0.1714  0.1427  0.0573  92   LEU E CD2 
14661 N  N   . LEU E 93   ? 1.1898 1.0200 1.0498 0.1617  0.1196  0.0483  93   LEU E N   
14662 C  CA  . LEU E 93   ? 1.1245 0.9637 0.9903 0.1583  0.1169  0.0465  93   LEU E CA  
14663 C  C   . LEU E 93   ? 1.0973 0.9380 0.9689 0.1458  0.1184  0.0436  93   LEU E C   
14664 O  O   . LEU E 93   ? 1.1878 1.0247 1.0549 0.1413  0.1206  0.0430  93   LEU E O   
14665 C  CB  . LEU E 93   ? 1.1698 1.0298 1.0515 0.1631  0.1091  0.0452  93   LEU E CB  
14666 C  CG  . LEU E 93   ? 1.1506 1.0121 1.0276 0.1753  0.1065  0.0474  93   LEU E CG  
14667 C  CD1 . LEU E 93   ? 1.2690 1.1521 1.1641 0.1786  0.0987  0.0455  93   LEU E CD1 
14668 C  CD2 . LEU E 93   ? 1.3478 1.2001 1.2113 0.1782  0.1087  0.0488  93   LEU E CD2 
14669 N  N   . ARG E 94   ? 0.9406 0.7871 0.8223 0.1405  0.1172  0.0418  94   ARG E N   
14670 C  CA  . ARG E 94   ? 0.9222 0.7700 0.8090 0.1291  0.1185  0.0389  94   ARG E CA  
14671 C  C   . ARG E 94   ? 1.0589 0.8872 0.9300 0.1238  0.1259  0.0395  94   ARG E C   
14672 O  O   . ARG E 94   ? 1.1059 0.9334 0.9774 0.1156  0.1279  0.0375  94   ARG E O   
14673 C  CB  . ARG E 94   ? 0.9977 0.8541 0.8965 0.1256  0.1158  0.0371  94   ARG E CB  
14674 C  CG  . ARG E 94   ? 1.1125 0.9690 1.0153 0.1143  0.1173  0.0340  94   ARG E CG  
14675 C  CD  . ARG E 94   ? 1.1385 1.0091 1.0529 0.1095  0.1135  0.0313  94   ARG E CD  
14676 N  NE  . ARG E 94   ? 1.0939 0.9737 1.0200 0.1019  0.1112  0.0281  94   ARG E NE  
14677 C  CZ  . ARG E 94   ? 1.2544 1.1486 1.1929 0.0980  0.1070  0.0255  94   ARG E CZ  
14678 N  NH1 . ARG E 94   ? 1.2648 1.1661 1.2061 0.1006  0.1047  0.0256  94   ARG E NH1 
14679 N  NH2 . ARG E 94   ? 1.2019 1.1031 1.1496 0.0917  0.1051  0.0228  94   ARG E NH2 
14680 N  N   . GLY E 95   ? 1.4102 1.2226 1.2675 0.1285  0.1303  0.0421  95   GLY E N   
14681 C  CA  . GLY E 95   ? 1.3643 1.1565 1.2054 0.1238  0.1378  0.0428  95   GLY E CA  
14682 C  C   . GLY E 95   ? 1.3471 1.1319 1.1781 0.1247  0.1408  0.0441  95   GLY E C   
14683 O  O   . GLY E 95   ? 1.3766 1.1519 1.2010 0.1168  0.1459  0.0431  95   GLY E O   
14684 N  N   . GLN E 96   ? 1.1467 0.9360 0.9763 0.1344  0.1379  0.0462  96   GLN E N   
14685 C  CA  . GLN E 96   ? 1.1949 0.9783 1.0151 0.1360  0.1404  0.0475  96   GLN E CA  
14686 C  C   . GLN E 96   ? 1.2445 1.0399 1.0758 0.1275  0.1386  0.0444  96   GLN E C   
14687 O  O   . GLN E 96   ? 1.2775 1.0642 1.1006 0.1228  0.1434  0.0444  96   GLN E O   
14688 C  CB  . GLN E 96   ? 1.2083 0.9963 1.0262 0.1486  0.1365  0.0499  96   GLN E CB  
14689 C  CG  . GLN E 96   ? 1.2192 1.0017 1.0270 0.1515  0.1384  0.0514  96   GLN E CG  
14690 C  CD  . GLN E 96   ? 1.2286 1.0169 1.0348 0.1642  0.1337  0.0533  96   GLN E CD  
14691 O  OE1 . GLN E 96   ? 1.2224 1.0256 1.0411 0.1691  0.1273  0.0526  96   GLN E OE1 
14692 N  NE2 . GLN E 96   ? 1.3164 1.0932 1.1072 0.1697  0.1369  0.0558  96   GLN E NE2 
14693 N  N   . LEU E 97   ? 1.0089 0.8242 0.8587 0.1254  0.1319  0.0417  97   LEU E N   
14694 C  CA  . LEU E 97   ? 0.9515 0.7791 0.8126 0.1177  0.1298  0.0386  97   LEU E CA  
14695 C  C   . LEU E 97   ? 0.8857 0.7065 0.7454 0.1061  0.1348  0.0363  97   LEU E C   
14696 O  O   . LEU E 97   ? 0.8694 0.6884 0.7269 0.1004  0.1378  0.0353  97   LEU E O   
14697 C  CB  . LEU E 97   ? 0.9633 0.8121 0.8437 0.1182  0.1219  0.0362  97   LEU E CB  
14698 C  CG  . LEU E 97   ? 0.9104 0.7731 0.8033 0.1111  0.1190  0.0329  97   LEU E CG  
14699 C  CD1 . LEU E 97   ? 0.9492 0.8137 0.8384 0.1147  0.1185  0.0336  97   LEU E CD1 
14700 C  CD2 . LEU E 97   ? 0.8757 0.7568 0.7866 0.1108  0.1119  0.0306  97   LEU E CD2 
14701 N  N   . LYS E 98   ? 0.7532 0.5705 0.6144 0.1025  0.1356  0.0355  98   LYS E N   
14702 C  CA  . LYS E 98   ? 0.8115 0.6229 0.6719 0.0914  0.1399  0.0329  98   LYS E CA  
14703 C  C   . LYS E 98   ? 0.9253 0.7158 0.7675 0.0891  0.1482  0.0346  98   LYS E C   
14704 O  O   . LYS E 98   ? 0.9006 0.6877 0.7420 0.0795  0.1521  0.0324  98   LYS E O   
14705 C  CB  . LYS E 98   ? 0.8395 0.6510 0.7042 0.0890  0.1387  0.0317  98   LYS E CB  
14706 C  CG  . LYS E 98   ? 0.8923 0.7241 0.7756 0.0884  0.1314  0.0293  98   LYS E CG  
14707 C  CD  . LYS E 98   ? 0.7975 0.6432 0.6923 0.0820  0.1288  0.0262  98   LYS E CD  
14708 C  CE  . LYS E 98   ? 0.7856 0.6505 0.6978 0.0827  0.1214  0.0242  98   LYS E CE  
14709 N  NZ  . LYS E 98   ? 0.9191 0.7979 0.8419 0.0786  0.1184  0.0216  98   LYS E NZ  
14710 N  N   . TYR E 99   ? 1.0067 0.7831 0.8342 0.0977  0.1511  0.0385  99   TYR E N   
14711 C  CA  . TYR E 99   ? 0.9475 0.7026 0.7563 0.0963  0.1593  0.0405  99   TYR E CA  
14712 C  C   . TYR E 99   ? 0.9642 0.7213 0.7712 0.0949  0.1610  0.0406  99   TYR E C   
14713 O  O   . TYR E 99   ? 1.0358 0.7827 0.8357 0.0872  0.1674  0.0399  99   TYR E O   
14714 C  CB  . TYR E 99   ? 0.9878 0.7278 0.7810 0.1071  0.1616  0.0448  99   TYR E CB  
14715 C  CG  . TYR E 99   ? 1.1255 0.8415 0.8974 0.1071  0.1703  0.0474  99   TYR E CG  
14716 C  CD1 . TYR E 99   ? 1.1191 0.8302 0.8818 0.1118  0.1725  0.0497  99   TYR E CD1 
14717 C  CD2 . TYR E 99   ? 1.0549 0.7525 0.8152 0.1026  0.1765  0.0476  99   TYR E CD2 
14718 C  CE1 . TYR E 99   ? 1.0684 0.7567 0.8109 0.1118  0.1809  0.0524  99   TYR E CE1 
14719 C  CE2 . TYR E 99   ? 1.0761 0.7507 0.8163 0.1024  0.1849  0.0500  99   TYR E CE2 
14720 C  CZ  . TYR E 99   ? 1.1342 0.8041 0.8655 0.1070  0.1872  0.0525  99   TYR E CZ  
14721 O  OH  . TYR E 99   ? 1.2161 0.8621 0.9266 0.1069  0.1960  0.0551  99   TYR E OH  
14722 N  N   . ASN E 100  ? 0.7904 0.5606 0.6040 0.1023  0.1555  0.0414  100  ASN E N   
14723 C  CA  . ASN E 100  ? 0.7438 0.5159 0.5551 0.1019  0.1568  0.0416  100  ASN E CA  
14724 C  C   . ASN E 100  ? 0.8109 0.5947 0.6349 0.0907  0.1566  0.0376  100  ASN E C   
14725 O  O   . ASN E 100  ? 0.8990 0.6788 0.7181 0.0868  0.1610  0.0375  100  ASN E O   
14726 C  CB  . ASN E 100  ? 0.7637 0.5479 0.5797 0.1125  0.1502  0.0430  100  ASN E CB  
14727 C  CG  . ASN E 100  ? 0.8319 0.6021 0.6312 0.1240  0.1521  0.0473  100  ASN E CG  
14728 O  OD1 . ASN E 100  ? 0.8272 0.5793 0.6124 0.1250  0.1577  0.0495  100  ASN E OD1 
14729 N  ND2 . ASN E 100  ? 0.9172 0.6957 0.7177 0.1330  0.1474  0.0484  100  ASN E ND2 
14730 N  N   . ILE E 101  ? 1.2008 0.9986 1.0405 0.0856  0.1518  0.0344  101  ILE E N   
14731 C  CA  . ILE E 101  ? 1.1355 0.9456 0.9879 0.0756  0.1510  0.0303  101  ILE E CA  
14732 C  C   . ILE E 101  ? 1.2358 1.0338 1.0821 0.0650  0.1581  0.0287  101  ILE E C   
14733 O  O   . ILE E 101  ? 1.2773 1.0733 1.1217 0.0584  0.1626  0.0275  101  ILE E O   
14734 C  CB  . ILE E 101  ? 1.0158 0.8455 0.8869 0.0747  0.1430  0.0275  101  ILE E CB  
14735 C  CG1 . ILE E 101  ? 0.9790 0.8216 0.8570 0.0840  0.1361  0.0286  101  ILE E CG1 
14736 C  CG2 . ILE E 101  ? 1.0753 0.9166 0.9585 0.0644  0.1424  0.0232  101  ILE E CG2 
14737 C  CD1 . ILE E 101  ? 1.1266 0.9855 1.0208 0.0848  0.1287  0.0266  101  ILE E CD1 
14738 N  N   . TYR E 102  ? 1.1513 0.9412 0.9946 0.0631  0.1592  0.0284  102  TYR E N   
14739 C  CA  . TYR E 102  ? 1.1069 0.8872 0.9466 0.0524  0.1648  0.0260  102  TYR E CA  
14740 C  C   . TYR E 102  ? 1.1390 0.8945 0.9583 0.0525  0.1734  0.0288  102  TYR E C   
14741 O  O   . TYR E 102  ? 1.2243 0.9709 1.0386 0.0432  0.1797  0.0271  102  TYR E O   
14742 C  CB  . TYR E 102  ? 1.1441 0.9298 0.9924 0.0494  0.1610  0.0235  102  TYR E CB  
14743 C  CG  . TYR E 102  ? 1.1345 0.9432 1.0024 0.0479  0.1531  0.0204  102  TYR E CG  
14744 C  CD1 . TYR E 102  ? 1.0869 0.9062 0.9655 0.0381  0.1526  0.0160  102  TYR E CD1 
14745 C  CD2 . TYR E 102  ? 1.0922 0.9121 0.9679 0.0564  0.1463  0.0217  102  TYR E CD2 
14746 C  CE1 . TYR E 102  ? 1.0528 0.8922 0.9484 0.0373  0.1455  0.0133  102  TYR E CE1 
14747 C  CE2 . TYR E 102  ? 1.1037 0.9434 0.9965 0.0551  0.1395  0.0189  102  TYR E CE2 
14748 C  CZ  . TYR E 102  ? 1.1192 0.9682 1.0215 0.0457  0.1392  0.0148  102  TYR E CZ  
14749 O  OH  . TYR E 102  ? 1.1666 1.0343 1.0849 0.0449  0.1325  0.0122  102  TYR E OH  
14750 N  N   . CYS E 103  ? 1.1795 0.9238 0.9870 0.0627  0.1739  0.0329  103  CYS E N   
14751 C  CA  . CYS E 103  ? 1.2193 0.9387 1.0067 0.0635  0.1817  0.0355  103  CYS E CA  
14752 C  C   . CYS E 103  ? 1.2976 1.0042 1.0699 0.0686  0.1870  0.0392  103  CYS E C   
14753 O  O   . CYS E 103  ? 1.2302 0.9165 0.9869 0.0650  0.1953  0.0405  103  CYS E O   
14754 C  CB  . CYS E 103  ? 1.2447 0.9576 1.0268 0.0719  0.1796  0.0378  103  CYS E CB  
14755 S  SG  . CYS E 103  ? 1.2771 1.0022 1.0743 0.0669  0.1741  0.0340  103  CYS E SG  
14756 N  N   . ALA E 104  ? 1.4075 1.1248 1.1835 0.0769  0.1825  0.0410  104  ALA E N   
14757 C  CA  . ALA E 104  ? 1.3608 1.0656 1.1212 0.0833  0.1870  0.0447  104  ALA E CA  
14758 C  C   . ALA E 104  ? 1.4182 1.1166 1.1742 0.0739  0.1942  0.0436  104  ALA E C   
14759 O  O   . ALA E 104  ? 1.4795 1.1571 1.2172 0.0743  0.2023  0.0464  104  ALA E O   
14760 C  CB  . ALA E 104  ? 1.3572 1.0770 1.1243 0.0936  0.1799  0.0461  104  ALA E CB  
14761 N  N   . VAL E 105  ? 1.1714 0.8874 0.9438 0.0655  0.1916  0.0397  105  VAL E N   
14762 C  CA  . VAL E 105  ? 1.2355 0.9470 1.0055 0.0556  0.1986  0.0382  105  VAL E CA  
14763 C  C   . VAL E 105  ? 1.2416 0.9359 1.0030 0.0462  0.2060  0.0370  105  VAL E C   
14764 O  O   . VAL E 105  ? 1.2494 0.9425 1.0136 0.0446  0.2039  0.0356  105  VAL E O   
14765 C  CB  . VAL E 105  ? 1.1256 0.8606 0.9160 0.0488  0.1938  0.0339  105  VAL E CB  
14766 C  CG1 . VAL E 105  ? 1.0603 0.8115 0.8588 0.0582  0.1862  0.0349  105  VAL E CG1 
14767 C  CG2 . VAL E 105  ? 1.1761 0.9224 0.9812 0.0415  0.1895  0.0296  105  VAL E CG2 
14768 N  N   . CYS E 106  ? 1.4962 1.1761 1.2462 0.0402  0.2151  0.0376  106  CYS E N   
14769 C  CA  . CYS E 106  ? 1.6575 1.3215 1.4000 0.0293  0.2231  0.0359  106  CYS E CA  
14770 C  C   . CYS E 106  ? 1.6194 1.2610 1.3446 0.0341  0.2265  0.0389  106  CYS E C   
14771 O  O   . CYS E 106  ? 1.7602 1.3863 1.4774 0.0257  0.2331  0.0375  106  CYS E O   
14772 C  CB  . CYS E 106  ? 1.6173 1.2974 1.3785 0.0177  0.2197  0.0300  106  CYS E CB  
14773 S  SG  . CYS E 106  ? 1.5554 1.2201 1.3113 0.0025  0.2281  0.0264  106  CYS E SG  
14774 N  N   . HIS E 107  ? 1.6185 1.2572 1.3370 0.0475  0.2225  0.0428  107  HIS E N   
14775 C  CA  . HIS E 107  ? 1.6971 1.3184 1.4027 0.0518  0.2243  0.0447  107  HIS E CA  
14776 C  C   . HIS E 107  ? 1.6498 1.2629 1.3424 0.0674  0.2229  0.0501  107  HIS E C   
14777 O  O   . HIS E 107  ? 1.7258 1.3222 1.4045 0.0732  0.2251  0.0527  107  HIS E O   
14778 C  CB  . HIS E 107  ? 1.6646 1.3000 1.3859 0.0486  0.2174  0.0411  107  HIS E CB  
14779 C  CG  . HIS E 107  ? 1.6366 1.2542 1.3471 0.0473  0.2207  0.0412  107  HIS E CG  
14780 N  ND1 . HIS E 107  ? 1.7827 1.3893 1.4898 0.0349  0.2268  0.0381  107  HIS E ND1 
14781 C  CD2 . HIS E 107  ? 1.6272 1.2387 1.3320 0.0561  0.2181  0.0433  107  HIS E CD2 
14782 C  CE1 . HIS E 107  ? 1.7996 1.3918 1.4972 0.0364  0.2283  0.0386  107  HIS E CE1 
14783 N  NE2 . HIS E 107  ? 1.7814 1.3766 1.4777 0.0493  0.2231  0.0418  107  HIS E NE2 
14784 N  N   . GLY E 108  ? 1.4596 1.0845 1.1563 0.0742  0.2191  0.0516  108  GLY E N   
14785 C  CA  . GLY E 108  ? 1.4720 1.0892 1.1553 0.0889  0.2182  0.0565  108  GLY E CA  
14786 C  C   . GLY E 108  ? 1.4645 1.1034 1.1619 0.0986  0.2075  0.0565  108  GLY E C   
14787 O  O   . GLY E 108  ? 1.5040 1.1553 1.2145 0.0984  0.2013  0.0544  108  GLY E O   
14788 N  N   . GLU E 109  ? 1.3210 0.9640 1.0151 0.1073  0.2054  0.0588  109  GLU E N   
14789 C  CA  . GLU E 109  ? 1.1690 0.8316 0.8752 0.1171  0.1954  0.0588  109  GLU E CA  
14790 C  C   . GLU E 109  ? 1.1798 0.8351 0.8774 0.1291  0.1931  0.0619  109  GLU E C   
14791 O  O   . GLU E 109  ? 1.0918 0.7627 0.8029 0.1330  0.1854  0.0607  109  GLU E O   
14792 C  CB  . GLU E 109  ? 1.3157 0.9845 1.0203 0.1226  0.1939  0.0601  109  GLU E CB  
14793 C  CG  . GLU E 109  ? 1.3679 1.0572 1.0849 0.1325  0.1835  0.0598  109  GLU E CG  
14794 C  CD  . GLU E 109  ? 1.3964 1.1103 1.1381 0.1258  0.1762  0.0553  109  GLU E CD  
14795 O  OE1 . GLU E 109  ? 1.4496 1.1676 1.1993 0.1139  0.1787  0.0523  109  GLU E OE1 
14796 O  OE2 . GLU E 109  ? 1.3039 1.0328 1.0567 0.1325  0.1679  0.0548  109  GLU E OE2 
14797 N  N   . ALA E 110  ? 1.6833 1.3151 1.3584 0.1352  0.1997  0.0659  110  ALA E N   
14798 C  CA  . ALA E 110  ? 1.5928 1.2157 1.2577 0.1469  0.1984  0.0690  110  ALA E CA  
14799 C  C   . ALA E 110  ? 1.5190 1.1250 1.1756 0.1424  0.2037  0.0691  110  ALA E C   
14800 O  O   . ALA E 110  ? 1.5065 1.1040 1.1542 0.1517  0.2033  0.0715  110  ALA E O   
14801 C  CB  . ALA E 110  ? 1.4939 1.1012 1.1379 0.1588  0.2017  0.0736  110  ALA E CB  
14802 N  N   . GLY E 111  ? 1.0754 0.6767 0.7347 0.1285  0.2087  0.0663  111  GLY E N   
14803 C  CA  . GLY E 111  ? 1.0686 0.6541 0.7205 0.1230  0.2137  0.0657  111  GLY E CA  
14804 C  C   . GLY E 111  ? 1.1509 0.7070 0.7792 0.1204  0.2247  0.0682  111  GLY E C   
14805 O  O   . GLY E 111  ? 1.2279 0.7680 0.8471 0.1173  0.2292  0.0682  111  GLY E O   
14806 N  N   . TYR E 112  ? 1.2891 0.8368 0.9066 0.1215  0.2295  0.0703  112  TYR E N   
14807 C  CA  . TYR E 112  ? 1.3040 0.8226 0.8979 0.1193  0.2405  0.0730  112  TYR E CA  
14808 C  C   . TYR E 112  ? 1.3449 0.8589 0.9417 0.1025  0.2473  0.0697  112  TYR E C   
14809 O  O   . TYR E 112  ? 1.3611 0.8504 0.9395 0.0983  0.2572  0.0713  112  TYR E O   
14810 C  CB  . TYR E 112  ? 1.3509 0.8604 0.9291 0.1300  0.2429  0.0775  112  TYR E CB  
14811 C  CG  . TYR E 112  ? 1.2689 0.7703 0.8339 0.1467  0.2403  0.0817  112  TYR E CG  
14812 C  CD1 . TYR E 112  ? 1.2148 0.6884 0.7568 0.1513  0.2476  0.0851  112  TYR E CD1 
14813 C  CD2 . TYR E 112  ? 1.2870 0.8087 0.8629 0.1580  0.2306  0.0822  112  TYR E CD2 
14814 C  CE1 . TYR E 112  ? 1.2380 0.7048 0.7679 0.1672  0.2451  0.0890  112  TYR E CE1 
14815 C  CE2 . TYR E 112  ? 1.1647 0.6804 0.7294 0.1734  0.2280  0.0858  112  TYR E CE2 
14816 C  CZ  . TYR E 112  ? 1.1394 0.6279 0.6812 0.1782  0.2353  0.0892  112  TYR E CZ  
14817 O  OH  . TYR E 112  ? 1.0820 0.5650 0.6127 0.1941  0.2326  0.0927  112  TYR E OH  
14818 N  N   . GLY E 113  ? 1.3078 0.8450 0.9272 0.0930  0.2424  0.0651  113  GLY E N   
14819 C  CA  . GLY E 113  ? 1.2982 0.8345 0.9227 0.0772  0.2480  0.0614  113  GLY E CA  
14820 C  C   . GLY E 113  ? 1.3344 0.8707 0.9564 0.0738  0.2526  0.0620  113  GLY E C   
14821 O  O   . GLY E 113  ? 1.3292 0.8628 0.9538 0.0607  0.2585  0.0592  113  GLY E O   
14822 N  N   . ALA E 114  ? 1.4048 0.9443 1.0218 0.0853  0.2501  0.0654  114  ALA E N   
14823 C  CA  . ALA E 114  ? 1.3589 0.8987 0.9728 0.0834  0.2543  0.0663  114  ALA E CA  
14824 C  C   . ALA E 114  ? 1.3152 0.8854 0.9537 0.0801  0.2460  0.0626  114  ALA E C   
14825 O  O   . ALA E 114  ? 1.2941 0.8811 0.9422 0.0894  0.2367  0.0628  114  ALA E O   
14826 C  CB  . ALA E 114  ? 1.3715 0.8976 0.9657 0.0978  0.2560  0.0719  114  ALA E CB  
14827 N  N   . SER E 115  ? 1.3804 0.9574 1.0287 0.0668  0.2496  0.0590  115  SER E N   
14828 C  CA  . SER E 115  ? 1.3797 0.9848 1.0510 0.0628  0.2424  0.0552  115  SER E CA  
14829 C  C   . SER E 115  ? 1.4830 1.0882 1.1556 0.0525  0.2495  0.0536  115  SER E C   
14830 O  O   . SER E 115  ? 1.5836 1.1689 1.2427 0.0454  0.2597  0.0544  115  SER E O   
14831 C  CB  . SER E 115  ? 1.3566 0.9786 1.0478 0.0560  0.2357  0.0505  115  SER E CB  
14832 O  OG  . SER E 115  ? 1.3089 0.9222 0.9999 0.0425  0.2422  0.0475  115  SER E OG  
14833 N  N   . MET E 116  ? 1.3901 1.0180 1.0790 0.0516  0.2440  0.0514  116  MET E N   
14834 C  CA  . MET E 116  ? 1.4071 1.0390 1.1003 0.0417  0.2499  0.0494  116  MET E CA  
14835 C  C   . MET E 116  ? 1.3043 0.9385 1.0076 0.0261  0.2535  0.0446  116  MET E C   
14836 O  O   . MET E 116  ? 1.3102 0.9393 1.0116 0.0162  0.2618  0.0433  116  MET E O   
14837 C  CB  . MET E 116  ? 1.3535 1.0104 1.0631 0.0448  0.2423  0.0477  116  MET E CB  
14838 C  CG  . MET E 116  ? 1.2634 0.9250 0.9762 0.0371  0.2481  0.0463  116  MET E CG  
14839 S  SD  . MET E 116  ? 1.2792 0.9158 0.9655 0.0428  0.2589  0.0519  116  MET E SD  
14840 C  CE  . MET E 116  ? 1.4822 1.1218 1.1746 0.0274  0.2684  0.0488  116  MET E CE  
14841 N  N   . VAL E 117  ? 1.1576 0.7994 0.8716 0.0238  0.2476  0.0418  117  VAL E N   
14842 C  CA  . VAL E 117  ? 1.1994 0.8448 0.9237 0.0095  0.2499  0.0368  117  VAL E CA  
14843 C  C   . VAL E 117  ? 1.2805 0.8988 0.9867 0.0029  0.2609  0.0379  117  VAL E C   
14844 O  O   . VAL E 117  ? 1.2805 0.8965 0.9894 -0.0100 0.2676  0.0348  117  VAL E O   
14845 C  CB  . VAL E 117  ? 1.0259 0.6858 0.7649 0.0101  0.2403  0.0338  117  VAL E CB  
14846 C  CG1 . VAL E 117  ? 1.0121 0.6751 0.7608 -0.0041 0.2423  0.0285  117  VAL E CG1 
14847 C  CG2 . VAL E 117  ? 0.9894 0.6757 0.7465 0.0157  0.2300  0.0325  117  VAL E CG2 
14848 N  N   . ALA E 118  ? 1.4850 1.0821 1.1722 0.0116  0.2631  0.0423  118  ALA E N   
14849 C  CA  . ALA E 118  ? 1.5611 1.1303 1.2293 0.0061  0.2737  0.0436  118  ALA E CA  
14850 C  C   . ALA E 118  ? 1.5833 1.1387 1.2390 0.0019  0.2845  0.0456  118  ALA E C   
14851 O  O   . ALA E 118  ? 1.6380 1.1744 1.2830 -0.0075 0.2942  0.0451  118  ALA E O   
14852 C  CB  . ALA E 118  ? 1.6175 1.1673 1.2674 0.0181  0.2735  0.0483  118  ALA E CB  
14853 N  N   . GLU E 119  ? 1.5142 1.0784 1.1709 0.0085  0.2832  0.0478  119  GLU E N   
14854 C  CA  . GLU E 119  ? 1.6309 1.1824 1.2755 0.0050  0.2936  0.0499  119  GLU E CA  
14855 C  C   . GLU E 119  ? 1.6993 1.2609 1.3580 -0.0115 0.2983  0.0448  119  GLU E C   
14856 O  O   . GLU E 119  ? 1.7107 1.2547 1.3582 -0.0202 0.3096  0.0451  119  GLU E O   
14857 C  CB  . GLU E 119  ? 1.5885 1.1483 1.2312 0.0167  0.2901  0.0533  119  GLU E CB  
14858 C  CG  . GLU E 119  ? 1.7816 1.3379 1.4196 0.0117  0.2988  0.0541  119  GLU E CG  
14859 C  CD  . GLU E 119  ? 1.7271 1.2840 1.3561 0.0253  0.2968  0.0585  119  GLU E CD  
14860 O  OE1 . GLU E 119  ? 1.5905 1.1371 1.2061 0.0386  0.2935  0.0626  119  GLU E OE1 
14861 O  OE2 . GLU E 119  ? 1.8149 1.3828 1.4503 0.0228  0.2984  0.0577  119  GLU E OE2 
14862 N  N   . ARG E 120  ? 1.6621 1.2517 1.3452 -0.0161 0.2900  0.0398  120  ARG E N   
14863 C  CA  . ARG E 120  ? 1.5887 1.1919 1.2878 -0.0310 0.2930  0.0344  120  ARG E CA  
14864 C  C   . ARG E 120  ? 1.6366 1.2459 1.3476 -0.0402 0.2893  0.0293  120  ARG E C   
14865 O  O   . ARG E 120  ? 1.5600 1.1902 1.2879 -0.0379 0.2788  0.0265  120  ARG E O   
14866 C  CB  . ARG E 120  ? 1.5120 1.1425 1.2292 -0.0292 0.2865  0.0326  120  ARG E CB  
14867 C  CG  . ARG E 120  ? 1.5631 1.1907 1.2697 -0.0164 0.2862  0.0377  120  ARG E CG  
14868 C  CD  . ARG E 120  ? 1.5507 1.2064 1.2760 -0.0106 0.2754  0.0360  120  ARG E CD  
14869 N  NE  . ARG E 120  ? 1.6237 1.2972 1.3646 -0.0201 0.2771  0.0320  120  ARG E NE  
14870 C  CZ  . ARG E 120  ? 1.5734 1.2535 1.3144 -0.0168 0.2787  0.0333  120  ARG E CZ  
14871 N  NH1 . ARG E 120  ? 1.4913 1.1618 1.2174 -0.0043 0.2786  0.0385  120  ARG E NH1 
14872 N  NH2 . ARG E 120  ? 1.5213 1.2183 1.2775 -0.0261 0.2803  0.0293  120  ARG E NH2 
14873 N  N   . GLY E 121  ? 1.5910 1.1817 1.2928 -0.0505 0.2981  0.0279  121  GLY E N   
14874 C  CA  . GLY E 121  ? 1.3751 0.9700 1.0869 -0.0599 0.2954  0.0227  121  GLY E CA  
14875 C  C   . GLY E 121  ? 1.4753 1.0426 1.1683 -0.0604 0.3007  0.0244  121  GLY E C   
14876 O  O   . GLY E 121  ? 1.5744 1.1387 1.2713 -0.0712 0.3022  0.0200  121  GLY E O   
14877 N  N   . GLY E 122  ? 1.3643 0.9110 1.0363 -0.0485 0.3034  0.0307  122  GLY E N   
14878 C  CA  . GLY E 122  ? 1.4728 0.9921 1.1252 -0.0471 0.3083  0.0329  122  GLY E CA  
14879 C  C   . GLY E 122  ? 1.5125 1.0386 1.1723 -0.0441 0.2993  0.0308  122  GLY E C   
14880 O  O   . GLY E 122  ? 1.4812 0.9949 1.1366 -0.0515 0.3021  0.0283  122  GLY E O   
14881 N  N   . ILE E 123  ? 1.8255 1.3709 1.4963 -0.0333 0.2884  0.0318  123  ILE E N   
14882 C  CA  . ILE E 123  ? 1.7890 1.3435 1.4687 -0.0302 0.2794  0.0297  123  ILE E CA  
14883 C  C   . ILE E 123  ? 1.8099 1.3397 1.4690 -0.0218 0.2817  0.0338  123  ILE E C   
14884 O  O   . ILE E 123  ? 1.7406 1.2669 1.4007 -0.0244 0.2793  0.0314  123  ILE E O   
14885 C  CB  . ILE E 123  ? 1.6395 1.2214 1.3366 -0.0212 0.2678  0.0297  123  ILE E CB  
14886 C  CG1 . ILE E 123  ? 1.5954 1.2013 1.3125 -0.0297 0.2657  0.0255  123  ILE E CG1 
14887 C  CG2 . ILE E 123  ? 1.6170 1.2080 1.3230 -0.0177 0.2588  0.0279  123  ILE E CG2 
14888 C  CD1 . ILE E 123  ? 1.4719 1.0871 1.2031 -0.0441 0.2653  0.0188  123  ILE E CD1 
14889 N  N   . VAL E 124  ? 1.4888 1.0007 1.1285 -0.0116 0.2864  0.0398  124  VAL E N   
14890 C  CA  . VAL E 124  ? 1.4827 0.9725 1.1021 -0.0003 0.2879  0.0446  124  VAL E CA  
14891 C  C   . VAL E 124  ? 1.3974 0.8983 1.0263 0.0052  0.2782  0.0432  124  VAL E C   
14892 O  O   . VAL E 124  ? 1.3040 0.7943 0.9291 0.0003  0.2796  0.0411  124  VAL E O   
14893 C  CB  . VAL E 124  ? 1.4310 0.8887 1.0286 -0.0070 0.2999  0.0456  124  VAL E CB  
14894 C  CG1 . VAL E 124  ? 1.4245 0.8818 1.0302 -0.0230 0.3023  0.0394  124  VAL E CG1 
14895 C  CG2 . VAL E 124  ? 1.2838 0.7178 0.8591 0.0058  0.3016  0.0508  124  VAL E CG2 
14896 N  N   . PRO E 125  ? 1.3574 0.8794 0.9987 0.0151  0.2685  0.0442  125  PRO E N   
14897 C  CA  . PRO E 125  ? 1.3468 0.8793 0.9969 0.0209  0.2596  0.0432  125  PRO E CA  
14898 C  C   . PRO E 125  ? 1.3440 0.8547 0.9741 0.0322  0.2616  0.0478  125  PRO E C   
14899 O  O   . PRO E 125  ? 1.4951 0.9843 1.1048 0.0378  0.2687  0.0523  125  PRO E O   
14900 C  CB  . PRO E 125  ? 1.2478 0.8075 0.9153 0.0284  0.2499  0.0434  125  PRO E CB  
14901 C  CG  . PRO E 125  ? 1.2959 0.8511 0.9547 0.0328  0.2541  0.0468  125  PRO E CG  
14902 C  CD  . PRO E 125  ? 1.2968 0.8350 0.9457 0.0208  0.2650  0.0458  125  PRO E CD  
14903 N  N   . ALA E 126  ? 1.1751 0.6917 0.8111 0.0361  0.2553  0.0468  126  ALA E N   
14904 C  CA  . ALA E 126  ? 1.2432 0.7406 0.8619 0.0465  0.2568  0.0506  126  ALA E CA  
14905 C  C   . ALA E 126  ? 1.2607 0.7619 0.8748 0.0629  0.2526  0.0557  126  ALA E C   
14906 O  O   . ALA E 126  ? 1.1513 0.6754 0.7806 0.0667  0.2455  0.0554  126  ALA E O   
14907 C  CB  . ALA E 126  ? 1.3122 0.8155 0.9392 0.0451  0.2515  0.0477  126  ALA E CB  
14908 N  N   . ASN E 127  ? 1.4649 0.9433 1.0575 0.0727  0.2570  0.0602  127  ASN E N   
14909 C  CA  . ASN E 127  ? 1.4451 0.9243 1.0307 0.0891  0.2535  0.0651  127  ASN E CA  
14910 C  C   . ASN E 127  ? 1.4599 0.9430 1.0479 0.0983  0.2476  0.0658  127  ASN E C   
14911 O  O   . ASN E 127  ? 1.4462 0.9103 1.0213 0.0982  0.2518  0.0664  127  ASN E O   
14912 C  CB  . ASN E 127  ? 1.4395 0.8906 0.9984 0.0951  0.2627  0.0701  127  ASN E CB  
14913 C  CG  . ASN E 127  ? 1.4660 0.9195 1.0180 0.1119  0.2589  0.0749  127  ASN E CG  
14914 O  OD1 . ASN E 127  ? 1.5046 0.9810 1.0722 0.1190  0.2494  0.0744  127  ASN E OD1 
14915 N  ND2 . ASN E 127  ? 1.4262 0.8557 0.9545 0.1185  0.2664  0.0794  127  ASN E ND2 
14916 N  N   . PHE E 128  ? 1.3854 0.8927 0.9897 0.1060  0.2380  0.0658  128  PHE E N   
14917 C  CA  . PHE E 128  ? 1.3444 0.8588 0.9540 0.1140  0.2319  0.0660  128  PHE E CA  
14918 C  C   . PHE E 128  ? 1.4958 0.9904 1.0845 0.1278  0.2349  0.0710  128  PHE E C   
14919 O  O   . PHE E 128  ? 1.5962 1.0886 1.1839 0.1328  0.2329  0.0713  128  PHE E O   
14920 C  CB  . PHE E 128  ? 1.2772 0.8220 0.9089 0.1190  0.2214  0.0649  128  PHE E CB  
14921 C  CG  . PHE E 128  ? 1.2893 0.8553 0.9430 0.1068  0.2172  0.0599  128  PHE E CG  
14922 C  CD1 . PHE E 128  ? 1.2568 0.8189 0.9140 0.0942  0.2199  0.0560  128  PHE E CD1 
14923 C  CD2 . PHE E 128  ? 1.3001 0.8899 0.9707 0.1080  0.2105  0.0588  128  PHE E CD2 
14924 C  CE1 . PHE E 128  ? 1.1451 0.7271 0.8223 0.0836  0.2158  0.0513  128  PHE E CE1 
14925 C  CE2 . PHE E 128  ? 1.1564 0.7653 0.8466 0.0973  0.2067  0.0542  128  PHE E CE2 
14926 C  CZ  . PHE E 128  ? 1.1233 0.7285 0.8168 0.0853  0.2093  0.0505  128  PHE E CZ  
14927 N  N   . HIS E 129  ? 1.6349 1.1149 1.2065 0.1345  0.2397  0.0750  129  HIS E N   
14928 C  CA  . HIS E 129  ? 1.6866 1.1496 1.2385 0.1494  0.2417  0.0799  129  HIS E CA  
14929 C  C   . HIS E 129  ? 1.7272 1.1570 1.2544 0.1473  0.2520  0.0818  129  HIS E C   
14930 O  O   . HIS E 129  ? 1.8244 1.2354 1.3310 0.1591  0.2557  0.0863  129  HIS E O   
14931 C  CB  . HIS E 129  ? 1.6478 1.1138 1.1941 0.1598  0.2404  0.0833  129  HIS E CB  
14932 C  CG  . HIS E 129  ? 1.5712 1.0684 1.1409 0.1606  0.2309  0.0812  129  HIS E CG  
14933 N  ND1 . HIS E 129  ? 1.5984 1.1039 1.1731 0.1564  0.2308  0.0805  129  HIS E ND1 
14934 C  CD2 . HIS E 129  ? 1.5107 1.0322 1.0998 0.1648  0.2213  0.0795  129  HIS E CD2 
14935 C  CE1 . HIS E 129  ? 1.4977 1.0310 1.0937 0.1582  0.2215  0.0784  129  HIS E CE1 
14936 N  NE2 . HIS E 129  ? 1.4729 1.0163 1.0781 0.1631  0.2157  0.0778  129  HIS E NE2 
14937 N  N   . GLN E 130  ? 1.6967 1.1187 1.2252 0.1328  0.2567  0.0783  130  GLN E N   
14938 C  CA  . GLN E 130  ? 1.8263 1.2176 1.3328 0.1302  0.2658  0.0794  130  GLN E CA  
14939 C  C   . GLN E 130  ? 1.8724 1.2621 1.3791 0.1352  0.2629  0.0790  130  GLN E C   
14940 O  O   . GLN E 130  ? 1.8553 1.2685 1.3822 0.1355  0.2546  0.0765  130  GLN E O   
14941 C  CB  . GLN E 130  ? 1.8664 1.2492 1.3736 0.1122  0.2724  0.0755  130  GLN E CB  
14942 C  CG  . GLN E 130  ? 1.8226 1.2236 1.3513 0.1002  0.2675  0.0697  130  GLN E CG  
14943 C  CD  . GLN E 130  ? 1.8037 1.1969 1.3331 0.0825  0.2739  0.0655  130  GLN E CD  
14944 O  OE1 . GLN E 130  ? 1.8727 1.2469 1.3869 0.0787  0.2825  0.0671  130  GLN E OE1 
14945 N  NE2 . GLN E 130  ? 1.8291 1.2373 1.3762 0.0718  0.2698  0.0602  130  GLN E NE2 
14946 N  N   . GLN E 131  ? 2.2127 1.5736 1.6960 0.1395  0.2700  0.0817  131  GLN E N   
14947 C  CA  . GLN E 131  ? 2.3124 1.6695 1.7926 0.1469  0.2678  0.0822  131  GLN E CA  
14948 C  C   . GLN E 131  ? 2.3268 1.6918 1.8209 0.1347  0.2657  0.0769  131  GLN E C   
14949 O  O   . GLN E 131  ? 2.2491 1.6217 1.7493 0.1404  0.2609  0.0765  131  GLN E O   
14950 C  CB  . GLN E 131  ? 2.3829 1.7054 1.8331 0.1542  0.2766  0.0862  131  GLN E CB  
14951 C  CG  . GLN E 131  ? 2.4410 1.7598 1.8791 0.1735  0.2750  0.0918  131  GLN E CG  
14952 C  CD  . GLN E 131  ? 2.4408 1.7826 1.8943 0.1843  0.2654  0.0919  131  GLN E CD  
14953 O  OE1 . GLN E 131  ? 2.4510 1.8036 1.9179 0.1791  0.2617  0.0885  131  GLN E OE1 
14954 N  NE2 . GLN E 131  ? 2.3095 1.6591 1.7612 0.1995  0.2613  0.0956  131  GLN E NE2 
14955 N  N   . ARG E 132  ? 2.1201 1.4840 1.6195 0.1185  0.2690  0.0728  132  ARG E N   
14956 C  CA  . ARG E 132  ? 2.0124 1.3836 1.5244 0.1069  0.2668  0.0675  132  ARG E CA  
14957 C  C   . ARG E 132  ? 1.8866 1.2919 1.4260 0.1072  0.2561  0.0649  132  ARG E C   
14958 O  O   . ARG E 132  ? 1.9364 1.3492 1.4839 0.1075  0.2518  0.0629  132  ARG E O   
14959 C  CB  . ARG E 132  ? 1.9709 1.3330 1.4820 0.0895  0.2730  0.0635  132  ARG E CB  
14960 C  CG  . ARG E 132  ? 2.0003 1.3653 1.5205 0.0776  0.2717  0.0579  132  ARG E CG  
14961 C  CD  . ARG E 132  ? 1.9999 1.3625 1.5241 0.0599  0.2763  0.0533  132  ARG E CD  
14962 N  NE  . ARG E 132  ? 1.9662 1.3563 1.5123 0.0547  0.2709  0.0511  132  ARG E NE  
14963 C  CZ  . ARG E 132  ? 2.0082 1.4050 1.5644 0.0397  0.2726  0.0465  132  ARG E CZ  
14964 N  NH1 . ARG E 132  ? 2.0986 1.4772 1.6458 0.0276  0.2794  0.0432  132  ARG E NH1 
14965 N  NH2 . ARG E 132  ? 1.9190 1.3414 1.4948 0.0367  0.2673  0.0449  132  ARG E NH2 
14966 N  N   . LEU E 133  ? 1.3948 0.8204 0.9482 0.1072  0.2518  0.0649  133  LEU E N   
14967 C  CA  . LEU E 133  ? 1.3922 0.8497 0.9709 0.1080  0.2418  0.0627  133  LEU E CA  
14968 C  C   . LEU E 133  ? 1.3821 0.8500 0.9632 0.1244  0.2359  0.0664  133  LEU E C   
14969 O  O   . LEU E 133  ? 1.3505 0.8440 0.9519 0.1261  0.2276  0.0648  133  LEU E O   
14970 C  CB  . LEU E 133  ? 1.3187 0.7939 0.9120 0.1004  0.2396  0.0606  133  LEU E CB  
14971 C  CG  . LEU E 133  ? 1.3499 0.8174 0.9426 0.0841  0.2455  0.0569  133  LEU E CG  
14972 C  CD1 . LEU E 133  ? 1.3269 0.8068 0.9280 0.0801  0.2452  0.0565  133  LEU E CD1 
14973 C  CD2 . LEU E 133  ? 1.2477 0.7265 0.8555 0.0731  0.2420  0.0513  133  LEU E CD2 
14974 N  N   . ARG E 134  ? 1.6936 1.1425 1.2545 0.1363  0.2399  0.0711  134  ARG E N   
14975 C  CA  . ARG E 134  ? 1.7500 1.2085 1.3129 0.1520  0.2344  0.0743  134  ARG E CA  
14976 C  C   . ARG E 134  ? 1.8092 1.2657 1.3727 0.1550  0.2330  0.0736  134  ARG E C   
14977 O  O   . ARG E 134  ? 1.6532 1.1289 1.2303 0.1625  0.2259  0.0738  134  ARG E O   
14978 C  CB  . ARG E 134  ? 1.8030 1.2430 1.3443 0.1647  0.2389  0.0796  134  ARG E CB  
14979 C  CG  . ARG E 134  ? 1.7688 1.2214 1.3151 0.1689  0.2359  0.0812  134  ARG E CG  
14980 C  CD  . ARG E 134  ? 1.8658 1.3102 1.3971 0.1862  0.2360  0.0863  134  ARG E CD  
14981 N  NE  . ARG E 134  ? 1.8255 1.2419 1.3316 0.1877  0.2450  0.0896  134  ARG E NE  
14982 C  CZ  . ARG E 134  ? 1.8466 1.2621 1.3465 0.1924  0.2458  0.0920  134  ARG E CZ  
14983 N  NH1 . ARG E 134  ? 1.7397 1.1806 1.2565 0.1959  0.2380  0.0913  134  ARG E NH1 
14984 N  NH2 . ARG E 134  ? 1.9810 1.3687 1.4564 0.1935  0.2547  0.0951  134  ARG E NH2 
14985 N  N   . GLU E 135  ? 2.0675 1.5008 1.6162 0.1491  0.2397  0.0727  135  GLU E N   
14986 C  CA  . GLU E 135  ? 2.0457 1.4750 1.5936 0.1504  0.2390  0.0716  135  GLU E CA  
14987 C  C   . GLU E 135  ? 2.0007 1.4454 1.5673 0.1373  0.2352  0.0661  135  GLU E C   
14988 O  O   . GLU E 135  ? 2.0607 1.5035 1.6280 0.1373  0.2344  0.0647  135  GLU E O   
14989 C  CB  . GLU E 135  ? 2.0279 1.4232 1.5492 0.1510  0.2482  0.0733  135  GLU E CB  
14990 C  CG  . GLU E 135  ? 2.1330 1.5078 1.6322 0.1615  0.2539  0.0785  135  GLU E CG  
14991 C  CD  . GLU E 135  ? 2.2649 1.6479 1.7633 0.1797  0.2494  0.0827  135  GLU E CD  
14992 O  OE1 . GLU E 135  ? 2.2652 1.6689 1.7798 0.1843  0.2424  0.0819  135  GLU E OE1 
14993 O  OE2 . GLU E 135  ? 2.3072 1.6757 1.7884 0.1894  0.2531  0.0870  135  GLU E OE2 
14994 N  N   . ALA E 136  ? 1.9363 1.3960 1.5175 0.1266  0.2329  0.0630  136  ALA E N   
14995 C  CA  . ALA E 136  ? 1.8934 1.3681 1.4921 0.1142  0.2292  0.0577  136  ALA E CA  
14996 C  C   . ALA E 136  ? 1.9554 1.4567 1.5745 0.1198  0.2202  0.0570  136  ALA E C   
14997 O  O   . ALA E 136  ? 2.0023 1.5181 1.6287 0.1294  0.2157  0.0597  136  ALA E O   
14998 C  CB  . ALA E 136  ? 1.9149 1.3983 1.5231 0.1020  0.2295  0.0547  136  ALA E CB  
14999 N  N   . PRO E 137  ? 1.4288 0.9365 1.0570 0.1137  0.2176  0.0535  137  PRO E N   
15000 C  CA  . PRO E 137  ? 1.3742 0.9060 1.0211 0.1185  0.2096  0.0529  137  PRO E CA  
15001 C  C   . PRO E 137  ? 1.3230 0.8812 0.9915 0.1141  0.2033  0.0509  137  PRO E C   
15002 O  O   . PRO E 137  ? 1.3431 0.9026 1.0142 0.1049  0.2046  0.0489  137  PRO E O   
15003 C  CB  . PRO E 137  ? 1.3901 0.9180 1.0383 0.1114  0.2097  0.0492  137  PRO E CB  
15004 C  CG  . PRO E 137  ? 1.3250 0.8229 0.9506 0.1074  0.2181  0.0492  137  PRO E CG  
15005 C  CD  . PRO E 137  ? 1.3663 0.8572 0.9857 0.1034  0.2222  0.0501  137  PRO E CD  
15006 N  N   . LEU E 138  ? 1.3589 0.9384 1.0430 0.1209  0.1964  0.0514  138  LEU E N   
15007 C  CA  . LEU E 138  ? 1.3245 0.9296 1.0296 0.1173  0.1898  0.0495  138  LEU E CA  
15008 C  C   . LEU E 138  ? 1.3990 1.0120 1.1153 0.1036  0.1882  0.0443  138  LEU E C   
15009 O  O   . LEU E 138  ? 1.3953 1.0195 1.1216 0.0964  0.1864  0.0421  138  LEU E O   
15010 C  CB  . LEU E 138  ? 1.2594 0.8840 0.9781 0.1272  0.1832  0.0510  138  LEU E CB  
15011 C  CG  . LEU E 138  ? 1.2697 0.9004 0.9880 0.1392  0.1813  0.0549  138  LEU E CG  
15012 C  CD1 . LEU E 138  ? 1.3347 0.9762 1.0606 0.1351  0.1793  0.0541  138  LEU E CD1 
15013 C  CD2 . LEU E 138  ? 1.3725 0.9802 1.0686 0.1482  0.1873  0.0589  138  LEU E CD2 
15014 N  N   . SER E 139  ? 1.4567 1.0642 1.1714 0.1003  0.1887  0.0422  139  SER E N   
15015 C  CA  . SER E 139  ? 1.3773 0.9917 1.1017 0.0878  0.1870  0.0370  139  SER E CA  
15016 C  C   . SER E 139  ? 1.3697 0.9712 1.0860 0.0766  0.1922  0.0346  139  SER E C   
15017 O  O   . SER E 139  ? 1.3222 0.9338 1.0494 0.0659  0.1902  0.0302  139  SER E O   
15018 C  CB  . SER E 139  ? 1.4911 1.0997 1.2128 0.0875  0.1868  0.0355  139  SER E CB  
15019 O  OG  . SER E 139  ? 1.5957 1.1792 1.2966 0.0915  0.1932  0.0377  139  SER E OG  
15020 N  N   . HIS E 140  ? 1.4363 1.0158 1.1337 0.0789  0.1991  0.0373  140  HIS E N   
15021 C  CA  . HIS E 140  ? 1.4712 1.0391 1.1613 0.0685  0.2046  0.0353  140  HIS E CA  
15022 C  C   . HIS E 140  ? 1.3802 0.9647 1.0825 0.0658  0.2021  0.0350  140  HIS E C   
15023 O  O   . HIS E 140  ? 1.3434 0.9315 1.0513 0.0543  0.2032  0.0314  140  HIS E O   
15024 C  CB  . HIS E 140  ? 1.5016 1.0412 1.1677 0.0726  0.2129  0.0388  140  HIS E CB  
15025 C  CG  . HIS E 140  ? 1.4492 0.9766 1.1072 0.0634  0.2192  0.0377  140  HIS E CG  
15026 N  ND1 . HIS E 140  ? 1.4434 0.9634 1.1002 0.0496  0.2225  0.0330  140  HIS E ND1 
15027 C  CD2 . HIS E 140  ? 1.4256 0.9470 1.0761 0.0659  0.2229  0.0407  140  HIS E CD2 
15028 C  CE1 . HIS E 140  ? 1.4433 0.9535 1.0929 0.0437  0.2283  0.0332  140  HIS E CE1 
15029 N  NE2 . HIS E 140  ? 1.4919 1.0024 1.1372 0.0535  0.2288  0.0379  140  HIS E NE2 
15030 N  N   . PHE E 141  ? 1.3691 0.9644 1.0759 0.0764  0.1987  0.0387  141  PHE E N   
15031 C  CA  . PHE E 141  ? 1.3159 0.9290 1.0357 0.0746  0.1954  0.0383  141  PHE E CA  
15032 C  C   . PHE E 141  ? 1.2590 0.8956 1.0003 0.0674  0.1887  0.0338  141  PHE E C   
15033 O  O   . PHE E 141  ? 1.2003 0.8467 0.9505 0.0592  0.1880  0.0311  141  PHE E O   
15034 C  CB  . PHE E 141  ? 1.3885 1.0087 1.1089 0.0880  0.1923  0.0428  141  PHE E CB  
15035 C  CG  . PHE E 141  ? 1.4481 1.0467 1.1476 0.0957  0.1986  0.0472  141  PHE E CG  
15036 C  CD1 . PHE E 141  ? 1.4392 1.0228 1.1267 0.0899  0.2053  0.0475  141  PHE E CD1 
15037 C  CD2 . PHE E 141  ? 1.4863 1.0797 1.1779 0.1088  0.1980  0.0512  141  PHE E CD2 
15038 C  CE1 . PHE E 141  ? 1.4367 0.9992 1.1038 0.0974  0.2113  0.0518  141  PHE E CE1 
15039 C  CE2 . PHE E 141  ? 1.5266 1.0997 1.1981 0.1166  0.2036  0.0553  141  PHE E CE2 
15040 C  CZ  . PHE E 141  ? 1.5432 1.1004 1.2020 0.1109  0.2103  0.0557  141  PHE E CZ  
15041 N  N   . PHE E 142  ? 1.2512 0.8966 1.0004 0.0706  0.1840  0.0331  142  PHE E N   
15042 C  CA  . PHE E 142  ? 1.1692 0.8360 0.9378 0.0647  0.1775  0.0291  142  PHE E CA  
15043 C  C   . PHE E 142  ? 1.1372 0.8010 0.9071 0.0510  0.1796  0.0241  142  PHE E C   
15044 O  O   . PHE E 142  ? 1.1672 0.8466 0.9507 0.0439  0.1765  0.0209  142  PHE E O   
15045 C  CB  . PHE E 142  ? 1.1680 0.8414 0.9420 0.0709  0.1732  0.0296  142  PHE E CB  
15046 C  CG  . PHE E 142  ? 1.1180 0.8128 0.9111 0.0663  0.1666  0.0260  142  PHE E CG  
15047 C  CD1 . PHE E 142  ? 1.0824 0.7982 0.8909 0.0702  0.1607  0.0267  142  PHE E CD1 
15048 C  CD2 . PHE E 142  ? 1.2216 0.9153 1.0167 0.0581  0.1661  0.0219  142  PHE E CD2 
15049 C  CE1 . PHE E 142  ? 1.1276 0.8619 0.9527 0.0662  0.1548  0.0236  142  PHE E CE1 
15050 C  CE2 . PHE E 142  ? 1.2000 0.9128 1.0117 0.0544  0.1600  0.0188  142  PHE E CE2 
15051 C  CZ  . PHE E 142  ? 1.1641 0.8969 0.9906 0.0585  0.1545  0.0197  142  PHE E CZ  
15052 N  N   . VAL E 143  ? 0.9646 0.6083 0.7203 0.0473  0.1848  0.0232  143  VAL E N   
15053 C  CA  . VAL E 143  ? 0.9858 0.6262 0.7426 0.0341  0.1867  0.0179  143  VAL E CA  
15054 C  C   . VAL E 143  ? 1.0507 0.6872 0.8050 0.0262  0.1913  0.0169  143  VAL E C   
15055 O  O   . VAL E 143  ? 1.0393 0.6813 0.8007 0.0148  0.1913  0.0121  143  VAL E O   
15056 C  CB  . VAL E 143  ? 1.0244 0.6436 0.7661 0.0324  0.1910  0.0171  143  VAL E CB  
15057 C  CG1 . VAL E 143  ? 1.1102 0.7038 0.8309 0.0341  0.1994  0.0201  143  VAL E CG1 
15058 C  CG2 . VAL E 143  ? 1.1683 0.7896 0.9152 0.0196  0.1903  0.0108  143  VAL E CG2 
15059 N  N   . VAL E 144  ? 1.1123 0.7398 0.8568 0.0322  0.1953  0.0212  144  VAL E N   
15060 C  CA  . VAL E 144  ? 1.0776 0.7019 0.8198 0.0253  0.1999  0.0206  144  VAL E CA  
15061 C  C   . VAL E 144  ? 1.0572 0.7067 0.8185 0.0236  0.1943  0.0191  144  VAL E C   
15062 O  O   . VAL E 144  ? 1.0651 0.7204 0.8328 0.0135  0.1956  0.0156  144  VAL E O   
15063 C  CB  . VAL E 144  ? 1.0621 0.6667 0.7857 0.0328  0.2063  0.0259  144  VAL E CB  
15064 C  CG1 . VAL E 144  ? 1.1769 0.7841 0.9014 0.0291  0.2094  0.0263  144  VAL E CG1 
15065 C  CG2 . VAL E 144  ? 1.1343 0.7113 0.8380 0.0300  0.2139  0.0261  144  VAL E CG2 
15066 N  N   . ILE E 145  ? 1.0814 0.7462 0.8520 0.0334  0.1880  0.0215  145  ILE E N   
15067 C  CA  . ILE E 145  ? 1.0505 0.7394 0.8395 0.0321  0.1821  0.0199  145  ILE E CA  
15068 C  C   . ILE E 145  ? 1.1775 0.8805 0.9810 0.0227  0.1779  0.0144  145  ILE E C   
15069 O  O   . ILE E 145  ? 1.0906 0.8083 0.9063 0.0163  0.1758  0.0115  145  ILE E O   
15070 C  CB  . ILE E 145  ? 0.9516 0.6530 0.7473 0.0443  0.1761  0.0234  145  ILE E CB  
15071 C  CG1 . ILE E 145  ? 0.9864 0.6735 0.7670 0.0545  0.1799  0.0287  145  ILE E CG1 
15072 C  CG2 . ILE E 145  ? 0.8966 0.6212 0.7098 0.0432  0.1704  0.0219  145  ILE E CG2 
15073 C  CD1 . ILE E 145  ? 0.9387 0.6352 0.7238 0.0670  0.1744  0.0320  145  ILE E CD1 
15074 N  N   . THR E 146  ? 1.2746 0.9733 1.0766 0.0221  0.1766  0.0129  146  THR E N   
15075 C  CA  . THR E 146  ? 1.1734 0.8857 0.9886 0.0145  0.1719  0.0077  146  THR E CA  
15076 C  C   . THR E 146  ? 1.2158 0.9225 1.0293 0.0014  0.1761  0.0030  146  THR E C   
15077 O  O   . THR E 146  ? 1.2082 0.9307 1.0351 -0.0058 0.1732  -0.0009 146  THR E O   
15078 C  CB  . THR E 146  ? 1.1697 0.8783 0.9826 0.0185  0.1694  0.0077  146  THR E CB  
15079 O  OG1 . THR E 146  ? 1.0899 0.8041 0.9049 0.0305  0.1660  0.0120  146  THR E OG1 
15080 C  CG2 . THR E 146  ? 1.1761 0.8995 1.0025 0.0117  0.1640  0.0025  146  THR E CG2 
15081 N  N   . ASN E 147  ? 1.3450 1.0291 1.1421 -0.0019 0.1829  0.0032  147  ASN E N   
15082 C  CA  . ASN E 147  ? 1.3866 1.0638 1.1814 -0.0148 0.1870  -0.0017 147  ASN E CA  
15083 C  C   . ASN E 147  ? 1.4023 1.0704 1.1901 -0.0197 0.1941  -0.0008 147  ASN E C   
15084 O  O   . ASN E 147  ? 1.4800 1.1585 1.2774 -0.0288 0.1945  -0.0045 147  ASN E O   
15085 C  CB  . ASN E 147  ? 1.3498 1.0072 1.1309 -0.0167 0.1902  -0.0028 147  ASN E CB  
15086 C  CG  . ASN E 147  ? 1.2897 0.9559 1.0776 -0.0131 0.1836  -0.0043 147  ASN E CG  
15087 O  OD1 . ASN E 147  ? 1.3516 1.0392 1.1560 -0.0141 0.1769  -0.0067 147  ASN E OD1 
15088 N  ND2 . ASN E 147  ? 1.3611 1.0104 1.1357 -0.0087 0.1857  -0.0027 147  ASN E ND2 
15089 N  N   . GLY E 148  ? 1.4964 1.1452 1.2676 -0.0134 0.1999  0.0041  148  GLY E N   
15090 C  CA  . GLY E 148  ? 1.5288 1.1656 1.2905 -0.0172 0.2076  0.0055  148  GLY E CA  
15091 C  C   . GLY E 148  ? 1.7089 1.3166 1.4478 -0.0146 0.2153  0.0087  148  GLY E C   
15092 O  O   . GLY E 148  ? 1.8273 1.4263 1.5582 -0.0063 0.2140  0.0112  148  GLY E O   
15093 N  N   . VAL E 149  ? 1.1830 0.7754 0.9114 -0.0216 0.2235  0.0085  149  VAL E N   
15094 C  CA  . VAL E 149  ? 1.2891 0.8519 0.9946 -0.0198 0.2317  0.0115  149  VAL E CA  
15095 C  C   . VAL E 149  ? 1.4047 0.9542 1.1044 -0.0304 0.2349  0.0067  149  VAL E C   
15096 O  O   . VAL E 149  ? 1.3664 0.8998 1.0537 -0.0261 0.2361  0.0079  149  VAL E O   
15097 C  CB  . VAL E 149  ? 1.1533 0.7037 0.8477 -0.0205 0.2396  0.0146  149  VAL E CB  
15098 C  CG1 . VAL E 149  ? 1.2370 0.7951 0.9408 -0.0346 0.2427  0.0100  149  VAL E CG1 
15099 C  CG2 . VAL E 149  ? 1.3179 0.8364 0.9873 -0.0178 0.2483  0.0180  149  VAL E CG2 
15100 N  N   . TYR E 150  ? 1.5284 1.0849 1.2374 -0.0442 0.2362  0.0010  150  TYR E N   
15101 C  CA  . TYR E 150  ? 1.5566 1.1030 1.2622 -0.0555 0.2386  -0.0044 150  TYR E CA  
15102 C  C   . TYR E 150  ? 1.5618 1.1252 1.2838 -0.0693 0.2378  -0.0107 150  TYR E C   
15103 O  O   . TYR E 150  ? 1.5739 1.1421 1.2995 -0.0728 0.2412  -0.0101 150  TYR E O   
15104 C  CB  . TYR E 150  ? 1.5534 1.0671 1.2352 -0.0578 0.2488  -0.0026 150  TYR E CB  
15105 C  CG  . TYR E 150  ? 1.5658 1.0704 1.2426 -0.0669 0.2575  -0.0030 150  TYR E CG  
15106 C  CD1 . TYR E 150  ? 1.5343 1.0365 1.2059 -0.0603 0.2610  0.0024  150  TYR E CD1 
15107 C  CD2 . TYR E 150  ? 1.6301 1.1278 1.3067 -0.0822 0.2623  -0.0088 150  TYR E CD2 
15108 C  CE1 . TYR E 150  ? 1.4520 0.9451 1.1182 -0.0685 0.2694  0.0023  150  TYR E CE1 
15109 C  CE2 . TYR E 150  ? 1.5977 1.0869 1.2699 -0.0910 0.2708  -0.0091 150  TYR E CE2 
15110 C  CZ  . TYR E 150  ? 1.4575 0.9442 1.1243 -0.0840 0.2745  -0.0034 150  TYR E CZ  
15111 O  OH  . TYR E 150  ? 1.6711 1.1488 1.3329 -0.0925 0.2834  -0.0036 150  TYR E OH  
15112 N  N   . ARG E 151  ? 2.2537 1.8262 1.9853 -0.0766 0.2331  -0.0168 151  ARG E N   
15113 C  CA  . ARG E 151  ? 2.3370 1.9271 2.0851 -0.0894 0.2314  -0.0234 151  ARG E CA  
15114 C  C   . ARG E 151  ? 2.4130 1.9851 2.1515 -0.1027 0.2407  -0.0267 151  ARG E C   
15115 O  O   . ARG E 151  ? 2.4252 1.9704 2.1437 -0.1017 0.2483  -0.0238 151  ARG E O   
15116 C  CB  . ARG E 151  ? 2.3258 1.9329 2.0875 -0.0916 0.2225  -0.0286 151  ARG E CB  
15117 N  N   . GLY E 152  ? 3.0174 2.6044 2.7703 -0.1152 0.2401  -0.0330 152  GLY E N   
15118 C  CA  . GLY E 152  ? 3.1192 2.6916 2.8654 -0.1291 0.2487  -0.0370 152  GLY E CA  
15119 C  C   . GLY E 152  ? 3.2522 2.8061 2.9870 -0.1341 0.2500  -0.0405 152  GLY E C   
15120 O  O   . GLY E 152  ? 3.1948 2.7593 2.9376 -0.1342 0.2425  -0.0445 152  GLY E O   
15121 N  N   . ASP E 153  ? 2.7229 2.2482 2.4382 -0.1379 0.2598  -0.0391 153  ASP E N   
15122 C  CA  . ASP E 153  ? 2.7276 2.2328 2.4304 -0.1435 0.2621  -0.0426 153  ASP E CA  
15123 C  C   . ASP E 153  ? 2.7691 2.2870 2.4858 -0.1590 0.2599  -0.0520 153  ASP E C   
15124 O  O   . ASP E 153  ? 2.7337 2.2656 2.4632 -0.1685 0.2616  -0.0553 153  ASP E O   
15125 C  CB  . ASP E 153  ? 2.7104 2.1820 2.3894 -0.1453 0.2739  -0.0392 153  ASP E CB  
15126 C  CG  . ASP E 153  ? 2.6118 2.0699 2.2758 -0.1296 0.2762  -0.0301 153  ASP E CG  
15127 O  OD1 . ASP E 153  ? 2.5506 2.0234 2.2215 -0.1173 0.2684  -0.0267 153  ASP E OD1 
15128 O  OD2 . ASP E 153  ? 2.6039 2.0364 2.2490 -0.1296 0.2859  -0.0263 153  ASP E OD2 
15129 N  N   . PRO E 154  ? 2.7558 2.2694 2.4703 -0.1617 0.2559  -0.0567 154  PRO E N   
15130 C  CA  . PRO E 154  ? 2.7802 2.3063 2.5078 -0.1763 0.2532  -0.0661 154  PRO E CA  
15131 C  C   . PRO E 154  ? 2.8154 2.3266 2.5371 -0.1915 0.2631  -0.0700 154  PRO E C   
15132 O  O   . PRO E 154  ? 2.7553 2.2823 2.4922 -0.2043 0.2619  -0.0773 154  PRO E O   
15133 C  CB  . PRO E 154  ? 2.7944 2.3132 2.5156 -0.1738 0.2478  -0.0690 154  PRO E CB  
15134 C  CG  . PRO E 154  ? 2.7982 2.2902 2.4970 -0.1623 0.2524  -0.0616 154  PRO E CG  
15135 C  CD  . PRO E 154  ? 2.7702 2.2677 2.4700 -0.1515 0.2538  -0.0537 154  PRO E CD  
15136 N  N   . GLU E 155  ? 3.1749 2.6563 2.8752 -0.1904 0.2731  -0.0653 155  GLU E N   
15137 C  CA  . GLU E 155  ? 3.2035 2.6677 2.8961 -0.2043 0.2838  -0.0682 155  GLU E CA  
15138 C  C   . GLU E 155  ? 3.2009 2.6546 2.8847 -0.2000 0.2925  -0.0608 155  GLU E C   
15139 O  O   . GLU E 155  ? 3.1492 2.5998 2.8258 -0.1852 0.2914  -0.0531 155  GLU E O   
15140 C  CB  . GLU E 155  ? 3.2630 2.6962 2.9350 -0.2089 0.2891  -0.0702 155  GLU E CB  
15141 C  CG  . GLU E 155  ? 3.2958 2.7369 2.9762 -0.2185 0.2829  -0.0795 155  GLU E CG  
15142 C  CD  . GLU E 155  ? 3.2593 2.7051 2.9388 -0.2067 0.2732  -0.0785 155  GLU E CD  
15143 O  OE1 . GLU E 155  ? 3.2280 2.6601 2.8934 -0.1926 0.2739  -0.0709 155  GLU E OE1 
15144 O  OE2 . GLU E 155  ? 3.2106 2.6738 2.9033 -0.2113 0.2650  -0.0854 155  GLU E OE2 
15145 N  N   . ASN E 156  ? 3.0904 2.5391 2.7749 -0.2132 0.3012  -0.0636 156  ASN E N   
15146 C  CA  . ASN E 156  ? 3.1550 2.5919 2.8301 -0.2112 0.3108  -0.0573 156  ASN E CA  
15147 C  C   . ASN E 156  ? 3.0481 2.5093 2.7366 -0.2006 0.3055  -0.0525 156  ASN E C   
15148 O  O   . ASN E 156  ? 2.9861 2.4368 2.6635 -0.1914 0.3103  -0.0450 156  ASN E O   
15149 C  CB  . ASN E 156  ? 3.1488 2.5495 2.7952 -0.2031 0.3187  -0.0505 156  ASN E CB  
15150 C  CG  . ASN E 156  ? 3.1647 2.5384 2.7958 -0.2140 0.3252  -0.0550 156  ASN E CG  
15151 O  OD1 . ASN E 156  ? 3.1591 2.5335 2.7965 -0.2304 0.3297  -0.0617 156  ASN E OD1 
15152 N  ND2 . ASN E 156  ? 3.1811 2.5309 2.7922 -0.2051 0.3258  -0.0515 156  ASN E ND2 
15153 N  N   . GLY E 157  ? 2.4317 1.9253 2.1438 -0.2016 0.2955  -0.0569 157  GLY E N   
15154 C  CA  . GLY E 157  ? 2.2972 1.8145 2.0228 -0.1922 0.2902  -0.0530 157  GLY E CA  
15155 C  C   . GLY E 157  ? 2.3002 1.8146 2.0178 -0.1740 0.2846  -0.0457 157  GLY E C   
15156 O  O   . GLY E 157  ? 2.3519 1.8513 2.0574 -0.1683 0.2827  -0.0446 157  GLY E O   
15157 N  N   . GLY E 158  ? 2.5232 2.0527 2.2482 -0.1649 0.2820  -0.0410 158  GLY E N   
15158 C  CA  . GLY E 158  ? 2.3970 1.9271 2.1169 -0.1477 0.2766  -0.0341 158  GLY E CA  
15159 C  C   . GLY E 158  ? 2.1915 1.7518 1.9310 -0.1418 0.2690  -0.0331 158  GLY E C   
15160 O  O   . GLY E 158  ? 2.1361 1.7200 1.8951 -0.1497 0.2649  -0.0386 158  GLY E O   
15161 N  N   . TYR E 159  ? 2.1157 1.6754 1.8497 -0.1272 0.2669  -0.0261 159  TYR E N   
15162 C  CA  . TYR E 159  ? 2.0155 1.6014 1.7659 -0.1203 0.2601  -0.0244 159  TYR E CA  
15163 C  C   . TYR E 159  ? 1.9570 1.5421 1.7018 -0.1036 0.2545  -0.0182 159  TYR E C   
15164 O  O   . TYR E 159  ? 1.9571 1.5192 1.6830 -0.0966 0.2583  -0.0137 159  TYR E O   
15165 C  CB  . TYR E 159  ? 2.0013 1.5889 1.7524 -0.1232 0.2668  -0.0223 159  TYR E CB  
15166 C  CG  . TYR E 159  ? 1.9468 1.5074 1.6751 -0.1166 0.2758  -0.0153 159  TYR E CG  
15167 C  CD1 . TYR E 159  ? 1.9613 1.4942 1.6718 -0.1241 0.2861  -0.0155 159  TYR E CD1 
15168 C  CD2 . TYR E 159  ? 1.8843 1.4470 1.6086 -0.1028 0.2739  -0.0087 159  TYR E CD2 
15169 C  CE1 . TYR E 159  ? 2.0355 1.5430 1.7242 -0.1175 0.2943  -0.0090 159  TYR E CE1 
15170 C  CE2 . TYR E 159  ? 1.8629 1.4011 1.5658 -0.0960 0.2817  -0.0024 159  TYR E CE2 
15171 C  CZ  . TYR E 159  ? 2.0380 1.5484 1.7228 -0.1032 0.2920  -0.0024 159  TYR E CZ  
15172 O  OH  . TYR E 159  ? 2.1476 1.6328 1.8102 -0.0960 0.2999  0.0041  159  TYR E OH  
15173 N  N   . GLN E 160  ? 1.9346 1.5454 1.6964 -0.0973 0.2456  -0.0180 160  GLN E N   
15174 C  CA  . GLN E 160  ? 1.8607 1.4748 1.6204 -0.0819 0.2397  -0.0126 160  GLN E CA  
15175 C  C   . GLN E 160  ? 1.7476 1.3617 1.5034 -0.0743 0.2425  -0.0069 160  GLN E C   
15176 O  O   . GLN E 160  ? 1.7484 1.3758 1.5144 -0.0792 0.2436  -0.0083 160  GLN E O   
15177 C  CB  . GLN E 160  ? 1.7685 1.4095 1.5480 -0.0791 0.2285  -0.0155 160  GLN E CB  
15178 C  CG  . GLN E 160  ? 1.7830 1.4229 1.5588 -0.0660 0.2224  -0.0117 160  GLN E CG  
15179 C  CD  . GLN E 160  ? 1.7922 1.4541 1.5852 -0.0657 0.2125  -0.0156 160  GLN E CD  
15180 O  OE1 . GLN E 160  ? 1.7830 1.4618 1.5908 -0.0746 0.2096  -0.0211 160  GLN E OE1 
15181 N  NE2 . GLN E 160  ? 1.7651 1.4269 1.5559 -0.0552 0.2074  -0.0127 160  GLN E NE2 
15182 N  N   . SER E 161  ? 1.5996 1.1990 1.3405 -0.0620 0.2437  -0.0006 161  SER E N   
15183 C  CA  . SER E 161  ? 1.6587 1.2549 1.3928 -0.0537 0.2466  0.0050  161  SER E CA  
15184 C  C   . SER E 161  ? 1.6132 1.2276 1.3569 -0.0408 0.2375  0.0080  161  SER E C   
15185 O  O   . SER E 161  ? 1.6653 1.2966 1.4198 -0.0390 0.2349  0.0085  161  SER E O   
15186 C  CB  . SER E 161  ? 1.7207 1.2856 1.4295 -0.0489 0.2553  0.0100  161  SER E CB  
15187 O  OG  . SER E 161  ? 1.7860 1.3331 1.4854 -0.0614 0.2645  0.0073  161  SER E OG  
15188 N  N   . MET E 162  ? 1.4318 1.0432 1.1720 -0.0319 0.2328  0.0100  162  MET E N   
15189 C  CA  . MET E 162  ? 1.3735 1.0014 1.1225 -0.0197 0.2244  0.0128  162  MET E CA  
15190 C  C   . MET E 162  ? 1.2650 0.9209 1.0371 -0.0235 0.2157  0.0082  162  MET E C   
15191 O  O   . MET E 162  ? 1.2324 0.9059 1.0153 -0.0161 0.2093  0.0098  162  MET E O   
15192 C  CB  . MET E 162  ? 1.4333 1.0484 1.1710 -0.0095 0.2229  0.0162  162  MET E CB  
15193 C  CG  . MET E 162  ? 1.3352 0.9658 1.0814 0.0029  0.2144  0.0189  162  MET E CG  
15194 S  SD  . MET E 162  ? 1.2517 0.8874 0.9958 0.0147  0.2135  0.0244  162  MET E SD  
15195 C  CE  . MET E 162  ? 1.4091 1.0743 1.1757 0.0201  0.2015  0.0229  162  MET E CE  
15196 N  N   . TYR E 163  ? 1.2666 0.9265 1.0461 -0.0346 0.2152  0.0025  163  TYR E N   
15197 C  CA  . TYR E 163  ? 1.2352 0.9204 1.0358 -0.0407 0.2085  -0.0027 163  TYR E CA  
15198 C  C   . TYR E 163  ? 1.2677 0.9694 1.0797 -0.0328 0.1987  -0.0025 163  TYR E C   
15199 O  O   . TYR E 163  ? 1.2573 0.9781 1.0854 -0.0373 0.1928  -0.0069 163  TYR E O   
15200 C  CB  . TYR E 163  ? 1.1518 0.8510 0.9619 -0.0435 0.2092  -0.0030 163  TYR E CB  
15201 C  CG  . TYR E 163  ? 1.2148 0.9285 1.0392 -0.0564 0.2088  -0.0095 163  TYR E CG  
15202 C  CD1 . TYR E 163  ? 1.2936 0.9952 1.1120 -0.0681 0.2166  -0.0125 163  TYR E CD1 
15203 C  CD2 . TYR E 163  ? 1.1316 0.8711 0.9756 -0.0568 0.2006  -0.0128 163  TYR E CD2 
15204 C  CE1 . TYR E 163  ? 1.2580 0.9739 1.0903 -0.0800 0.2161  -0.0188 163  TYR E CE1 
15205 C  CE2 . TYR E 163  ? 1.1653 0.9188 1.0226 -0.0680 0.1999  -0.0189 163  TYR E CE2 
15206 C  CZ  . TYR E 163  ? 1.2168 0.9590 1.0685 -0.0796 0.2076  -0.0219 163  TYR E CZ  
15207 O  OH  . TYR E 163  ? 1.2722 1.0292 1.1377 -0.0908 0.2069  -0.0282 163  TYR E OH  
15208 N  N   . GLY E 164  ? 1.5907 1.2854 1.3947 -0.0209 0.1971  0.0024  164  GLY E N   
15209 C  CA  . GLY E 164  ? 1.5676 1.2753 1.3807 -0.0135 0.1888  0.0027  164  GLY E CA  
15210 C  C   . GLY E 164  ? 1.5325 1.2637 1.3618 -0.0088 0.1820  0.0031  164  GLY E C   
15211 O  O   . GLY E 164  ? 1.5551 1.2969 1.3923 -0.0134 0.1825  0.0016  164  GLY E O   
15212 N  N   . TYR E 165  ? 1.3565 1.0958 1.1906 0.0005  0.1758  0.0052  165  TYR E N   
15213 C  CA  . TYR E 165  ? 1.3642 1.1247 1.2128 0.0061  0.1689  0.0059  165  TYR E CA  
15214 C  C   . TYR E 165  ? 1.3663 1.1383 1.2247 0.0098  0.1617  0.0048  165  TYR E C   
15215 O  O   . TYR E 165  ? 1.3584 1.1374 1.2205 0.0193  0.1573  0.0078  165  TYR E O   
15216 C  CB  . TYR E 165  ? 1.2736 1.0301 1.1154 0.0165  0.1698  0.0112  165  TYR E CB  
15217 C  CG  . TYR E 165  ? 1.3400 1.0936 1.1778 0.0136  0.1748  0.0120  165  TYR E CG  
15218 C  CD1 . TYR E 165  ? 1.4129 1.1451 1.2339 0.0109  0.1834  0.0136  165  TYR E CD1 
15219 C  CD2 . TYR E 165  ? 1.3839 1.1555 1.2341 0.0137  0.1712  0.0112  165  TYR E CD2 
15220 C  CE1 . TYR E 165  ? 1.4656 1.1944 1.2824 0.0083  0.1884  0.0145  165  TYR E CE1 
15221 C  CE2 . TYR E 165  ? 1.4120 1.1808 1.2583 0.0113  0.1760  0.0119  165  TYR E CE2 
15222 C  CZ  . TYR E 165  ? 1.4432 1.1906 1.2727 0.0086  0.1847  0.0137  165  TYR E CZ  
15223 O  OH  . TYR E 165  ? 1.2999 1.0441 1.1250 0.0062  0.1899  0.0146  165  TYR E OH  
15224 N  N   . ALA E 166  ? 1.2741 1.0482 1.1369 0.0023  0.1604  0.0004  166  ALA E N   
15225 C  CA  . ALA E 166  ? 1.2087 0.9907 1.0784 0.0057  0.1544  -0.0005 166  ALA E CA  
15226 C  C   . ALA E 166  ? 1.1287 0.9343 1.0162 0.0073  0.1471  -0.0019 166  ALA E C   
15227 O  O   . ALA E 166  ? 1.0353 0.8485 0.9280 0.0152  0.1423  0.0002  166  ALA E O   
15228 C  CB  . ALA E 166  ? 1.1776 0.9531 1.0447 -0.0026 0.1555  -0.0049 166  ALA E CB  
15229 N  N   . SER E 167  ? 1.0911 0.9085 0.9881 -0.0001 0.1463  -0.0055 167  SER E N   
15230 C  CA  . SER E 167  ? 1.0158 0.8552 0.9295 0.0006  0.1393  -0.0075 167  SER E CA  
15231 C  C   . SER E 167  ? 1.0151 0.8631 0.9333 0.0088  0.1368  -0.0039 167  SER E C   
15232 O  O   . SER E 167  ? 1.0697 0.9323 0.9990 0.0130  0.1306  -0.0040 167  SER E O   
15233 C  CB  . SER E 167  ? 0.9669 0.8163 0.8892 -0.0095 0.1394  -0.0126 167  SER E CB  
15234 O  OG  . SER E 167  ? 1.0450 0.8882 0.9619 -0.0132 0.1453  -0.0120 167  SER E OG  
15235 N  N   . ARG E 168  ? 1.0878 0.9265 0.9971 0.0112  0.1416  -0.0008 168  ARG E N   
15236 C  CA  . ARG E 168  ? 0.9896 0.8369 0.9031 0.0182  0.1392  0.0020  168  ARG E CA  
15237 C  C   . ARG E 168  ? 0.9404 0.7844 0.8500 0.0291  0.1370  0.0064  168  ARG E C   
15238 O  O   . ARG E 168  ? 0.8982 0.7527 0.8142 0.0354  0.1332  0.0081  168  ARG E O   
15239 C  CB  . ARG E 168  ? 1.0517 0.8912 0.9572 0.0162  0.1452  0.0034  168  ARG E CB  
15240 C  CG  . ARG E 168  ? 1.0314 0.8835 0.9468 0.0088  0.1451  -0.0002 168  ARG E CG  
15241 C  CD  . ARG E 168  ? 1.0009 0.8409 0.9058 0.0043  0.1529  0.0005  168  ARG E CD  
15242 N  NE  . ARG E 168  ? 1.1912 1.0166 1.0874 -0.0036 0.1586  -0.0013 168  ARG E NE  
15243 C  CZ  . ARG E 168  ? 1.2093 1.0216 1.0955 -0.0092 0.1664  -0.0012 168  ARG E CZ  
15244 N  NH1 . ARG E 168  ? 1.1821 0.9938 1.0652 -0.0076 0.1696  0.0009  168  ARG E NH1 
15245 N  NH2 . ARG E 168  ? 1.2176 1.0167 1.0963 -0.0166 0.1711  -0.0032 168  ARG E NH2 
15246 N  N   . ILE E 169  ? 0.7992 0.6295 0.6989 0.0317  0.1392  0.0081  169  ILE E N   
15247 C  CA  . ILE E 169  ? 0.7701 0.5959 0.6648 0.0423  0.1381  0.0124  169  ILE E CA  
15248 C  C   . ILE E 169  ? 0.7830 0.6110 0.6814 0.0445  0.1347  0.0119  169  ILE E C   
15249 O  O   . ILE E 169  ? 0.6582 0.4794 0.5533 0.0389  0.1364  0.0096  169  ILE E O   
15250 C  CB  . ILE E 169  ? 0.6834 0.4883 0.5600 0.0455  0.1449  0.0159  169  ILE E CB  
15251 C  CG1 . ILE E 169  ? 0.6369 0.4379 0.5086 0.0422  0.1492  0.0161  169  ILE E CG1 
15252 C  CG2 . ILE E 169  ? 0.6487 0.4513 0.5213 0.0573  0.1432  0.0202  169  ILE E CG2 
15253 C  CD1 . ILE E 169  ? 0.7326 0.5143 0.5866 0.0475  0.1553  0.0203  169  ILE E CD1 
15254 N  N   . THR E 170  ? 1.0286 0.8659 0.9337 0.0526  0.1300  0.0141  170  THR E N   
15255 C  CA  . THR E 170  ? 0.8735 0.7127 0.7818 0.0558  0.1272  0.0142  170  THR E CA  
15256 C  C   . THR E 170  ? 0.9670 0.7882 0.8606 0.0604  0.1317  0.0172  170  THR E C   
15257 O  O   . THR E 170  ? 1.0510 0.8623 0.9346 0.0652  0.1352  0.0203  170  THR E O   
15258 C  CB  . THR E 170  ? 0.9130 0.7682 0.8335 0.0626  0.1212  0.0156  170  THR E CB  
15259 O  OG1 . THR E 170  ? 1.1432 1.0139 1.0762 0.0583  0.1173  0.0128  170  THR E OG1 
15260 C  CG2 . THR E 170  ? 0.9585 0.8162 0.8829 0.0657  0.1187  0.0158  170  THR E CG2 
15261 N  N   . PRO E 171  ? 1.1686 0.9841 1.0596 0.0591  0.1321  0.0162  171  PRO E N   
15262 C  CA  . PRO E 171  ? 1.1121 0.9100 0.9887 0.0639  0.1365  0.0190  171  PRO E CA  
15263 C  C   . PRO E 171  ? 1.1113 0.9087 0.9853 0.0751  0.1361  0.0235  171  PRO E C   
15264 O  O   . PRO E 171  ? 1.2021 0.9840 1.0621 0.0794  0.1407  0.0263  171  PRO E O   
15265 C  CB  . PRO E 171  ? 1.0484 0.8463 0.9271 0.0619  0.1349  0.0170  171  PRO E CB  
15266 C  CG  . PRO E 171  ? 0.9938 0.8014 0.8817 0.0524  0.1324  0.0123  171  PRO E CG  
15267 C  CD  . PRO E 171  ? 1.0174 0.8403 0.9164 0.0524  0.1292  0.0122  171  PRO E CD  
15268 N  N   . GLU E 172  ? 1.2633 1.0772 1.1503 0.0802  0.1306  0.0242  172  GLU E N   
15269 C  CA  . GLU E 172  ? 1.2691 1.0844 1.1550 0.0907  0.1298  0.0281  172  GLU E CA  
15270 C  C   . GLU E 172  ? 1.3083 1.1205 1.1886 0.0931  0.1315  0.0298  172  GLU E C   
15271 O  O   . GLU E 172  ? 1.2858 1.0892 1.1564 0.1009  0.1338  0.0331  172  GLU E O   
15272 C  CB  . GLU E 172  ? 1.3631 1.1973 1.2651 0.0945  0.1236  0.0279  172  GLU E CB  
15273 C  CG  . GLU E 172  ? 1.5036 1.3396 1.4095 0.0946  0.1224  0.0273  172  GLU E CG  
15274 C  CD  . GLU E 172  ? 1.6171 1.4618 1.5323 0.0862  0.1196  0.0234  172  GLU E CD  
15275 O  OE1 . GLU E 172  ? 1.6331 1.4877 1.5562 0.0818  0.1171  0.0214  172  GLU E OE1 
15276 O  OE2 . GLU E 172  ? 1.6390 1.4805 1.5533 0.0844  0.1200  0.0224  172  GLU E OE2 
15277 N  N   . ASP E 173  ? 1.3336 1.1528 1.2194 0.0868  0.1305  0.0275  173  ASP E N   
15278 C  CA  . ASP E 173  ? 1.2552 1.0697 1.1342 0.0883  0.1329  0.0290  173  ASP E CA  
15279 C  C   . ASP E 173  ? 1.1848 0.9775 1.0456 0.0863  0.1402  0.0302  173  ASP E C   
15280 O  O   . ASP E 173  ? 1.3115 1.0951 1.1618 0.0914  0.1432  0.0330  173  ASP E O   
15281 C  CB  . ASP E 173  ? 1.2611 1.0882 1.1503 0.0817  0.1304  0.0261  173  ASP E CB  
15282 C  CG  . ASP E 173  ? 1.3056 1.1533 1.2123 0.0832  0.1233  0.0247  173  ASP E CG  
15283 O  OD1 . ASP E 173  ? 1.2781 1.1311 1.1887 0.0909  0.1203  0.0267  173  ASP E OD1 
15284 O  OD2 . ASP E 173  ? 1.3389 1.1974 1.2553 0.0767  0.1209  0.0217  173  ASP E OD2 
15285 N  N   . ARG E 174  ? 0.9294 0.7131 0.7859 0.0790  0.1432  0.0280  174  ARG E N   
15286 C  CA  . ARG E 174  ? 0.9961 0.7578 0.8348 0.0768  0.1504  0.0289  174  ARG E CA  
15287 C  C   . ARG E 174  ? 1.0297 0.7785 0.8561 0.0869  0.1528  0.0330  174  ARG E C   
15288 O  O   . ARG E 174  ? 1.0217 0.7542 0.8328 0.0900  0.1580  0.0356  174  ARG E O   
15289 C  CB  . ARG E 174  ? 0.9803 0.7361 0.8180 0.0669  0.1524  0.0252  174  ARG E CB  
15290 C  CG  . ARG E 174  ? 1.0690 0.8291 0.9115 0.0559  0.1534  0.0214  174  ARG E CG  
15291 C  CD  . ARG E 174  ? 1.1167 0.8733 0.9598 0.0466  0.1542  0.0173  174  ARG E CD  
15292 N  NE  . ARG E 174  ? 1.1396 0.9155 0.9995 0.0436  0.1477  0.0141  174  ARG E NE  
15293 C  CZ  . ARG E 174  ? 1.1453 0.9235 1.0093 0.0352  0.1469  0.0097  174  ARG E CZ  
15294 N  NH1 . ARG E 174  ? 1.2129 0.9760 1.0665 0.0282  0.1519  0.0077  174  ARG E NH1 
15295 N  NH2 . ARG E 174  ? 1.1178 0.9138 0.9967 0.0337  0.1407  0.0072  174  ARG E NH2 
15296 N  N   . TRP E 175  ? 0.8560 0.6116 0.6885 0.0925  0.1492  0.0337  175  TRP E N   
15297 C  CA  . TRP E 175  ? 0.9183 0.6641 0.7407 0.1030  0.1509  0.0376  175  TRP E CA  
15298 C  C   . TRP E 175  ? 0.8769 0.6276 0.6989 0.1123  0.1493  0.0407  175  TRP E C   
15299 O  O   . TRP E 175  ? 0.9080 0.6453 0.7163 0.1200  0.1528  0.0441  175  TRP E O   
15300 C  CB  . TRP E 175  ? 0.9437 0.6976 0.7743 0.1064  0.1475  0.0374  175  TRP E CB  
15301 C  CG  . TRP E 175  ? 0.9255 0.6693 0.7511 0.1001  0.1500  0.0352  175  TRP E CG  
15302 C  CD1 . TRP E 175  ? 0.9802 0.7339 0.8168 0.0932  0.1469  0.0317  175  TRP E CD1 
15303 C  CD2 . TRP E 175  ? 0.9585 0.6801 0.7663 0.1001  0.1562  0.0361  175  TRP E CD2 
15304 N  NE1 . TRP E 175  ? 1.0248 0.7642 0.8517 0.0890  0.1504  0.0303  175  TRP E NE1 
15305 C  CE2 . TRP E 175  ? 1.0078 0.7271 0.8170 0.0929  0.1562  0.0329  175  TRP E CE2 
15306 C  CE3 . TRP E 175  ? 0.9720 0.6746 0.7622 0.1058  0.1617  0.0394  175  TRP E CE3 
15307 C  CZ2 . TRP E 175  ? 1.0541 0.7532 0.8480 0.0909  0.1615  0.0326  175  TRP E CZ2 
15308 C  CZ3 . TRP E 175  ? 1.0086 0.6907 0.7834 0.1038  0.1671  0.0393  175  TRP E CZ3 
15309 C  CH2 . TRP E 175  ? 1.0579 0.7384 0.8348 0.0963  0.1670  0.0358  175  TRP E CH2 
15310 N  N   . ALA E 176  ? 1.0498 0.8192 0.8864 0.1119  0.1440  0.0396  176  ALA E N   
15311 C  CA  . ALA E 176  ? 1.0627 0.8371 0.8990 0.1200  0.1421  0.0421  176  ALA E CA  
15312 C  C   . ALA E 176  ? 1.0908 0.8503 0.9123 0.1189  0.1475  0.0433  176  ALA E C   
15313 O  O   . ALA E 176  ? 1.1012 0.8542 0.9131 0.1276  0.1487  0.0465  176  ALA E O   
15314 C  CB  . ALA E 176  ? 1.0087 0.8057 0.8636 0.1189  0.1353  0.0401  176  ALA E CB  
15315 N  N   . ILE E 177  ? 0.9861 0.7403 0.8057 0.1082  0.1508  0.0408  177  ILE E N   
15316 C  CA  . ILE E 177  ? 0.9949 0.7334 0.7999 0.1061  0.1569  0.0420  177  ILE E CA  
15317 C  C   . ILE E 177  ? 1.0176 0.7328 0.8027 0.1105  0.1633  0.0449  177  ILE E C   
15318 O  O   . ILE E 177  ? 1.0486 0.7509 0.8195 0.1160  0.1672  0.0480  177  ILE E O   
15319 C  CB  . ILE E 177  ? 0.9096 0.6488 0.7184 0.0930  0.1591  0.0383  177  ILE E CB  
15320 C  CG1 . ILE E 177  ? 0.8452 0.6054 0.6705 0.0902  0.1537  0.0361  177  ILE E CG1 
15321 C  CG2 . ILE E 177  ? 0.9530 0.6719 0.7445 0.0894  0.1672  0.0394  177  ILE E CG2 
15322 C  CD1 . ILE E 177  ? 0.8593 0.6223 0.6897 0.0779  0.1555  0.0322  177  ILE E CD1 
15323 N  N   . ALA E 178  ? 1.1072 0.8159 0.8903 0.1086  0.1645  0.0441  178  ALA E N   
15324 C  CA  . ALA E 178  ? 1.1590 0.8451 0.9230 0.1131  0.1704  0.0468  178  ALA E CA  
15325 C  C   . ALA E 178  ? 1.2112 0.8967 0.9700 0.1274  0.1688  0.0510  178  ALA E C   
15326 O  O   . ALA E 178  ? 1.3353 1.0023 1.0761 0.1334  0.1739  0.0541  178  ALA E O   
15327 C  CB  . ALA E 178  ? 1.1674 0.8484 0.9315 0.1085  0.1712  0.0448  178  ALA E CB  
15328 N  N   . ALA E 179  ? 1.1741 0.8798 0.9483 0.1329  0.1619  0.0509  179  ALA E N   
15329 C  CA  . ALA E 179  ? 1.1946 0.9026 0.9660 0.1464  0.1598  0.0544  179  ALA E CA  
15330 C  C   . ALA E 179  ? 1.2480 0.9544 1.0130 0.1513  0.1602  0.0564  179  ALA E C   
15331 O  O   . ALA E 179  ? 1.1930 0.8895 0.9453 0.1617  0.1620  0.0599  179  ALA E O   
15332 C  CB  . ALA E 179  ? 1.1780 0.9089 0.9688 0.1499  0.1524  0.0534  179  ALA E CB  
15333 N  N   . TYR E 180  ? 1.2555 0.9712 1.0285 0.1443  0.1586  0.0543  180  TYR E N   
15334 C  CA  . TYR E 180  ? 1.2390 0.9525 1.0052 0.1485  0.1593  0.0561  180  TYR E CA  
15335 C  C   . TYR E 180  ? 1.2075 0.8953 0.9514 0.1475  0.1678  0.0582  180  TYR E C   
15336 O  O   . TYR E 180  ? 1.3090 0.9885 1.0407 0.1555  0.1697  0.0613  180  TYR E O   
15337 C  CB  . TYR E 180  ? 1.2437 0.9737 1.0243 0.1411  0.1556  0.0531  180  TYR E CB  
15338 C  CG  . TYR E 180  ? 1.1827 0.9118 0.9571 0.1454  0.1559  0.0547  180  TYR E CG  
15339 C  CD1 . TYR E 180  ? 1.1674 0.9024 0.9409 0.1576  0.1520  0.0571  180  TYR E CD1 
15340 C  CD2 . TYR E 180  ? 1.1129 0.8356 0.8823 0.1375  0.1602  0.0538  180  TYR E CD2 
15341 C  CE1 . TYR E 180  ? 1.2903 1.0241 1.0574 0.1620  0.1521  0.0585  180  TYR E CE1 
15342 C  CE2 . TYR E 180  ? 1.2366 0.9579 0.9997 0.1417  0.1608  0.0554  180  TYR E CE2 
15343 C  CZ  . TYR E 180  ? 1.3597 1.0862 1.1212 0.1541  0.1566  0.0578  180  TYR E CZ  
15344 O  OH  . TYR E 180  ? 1.4226 1.1475 1.1769 0.1587  0.1570  0.0593  180  TYR E OH  
15345 N  N   . ILE E 181  ? 0.8570 0.5320 0.5952 0.1377  0.1732  0.0566  181  ILE E N   
15346 C  CA  . ILE E 181  ? 0.8746 0.5236 0.5911 0.1363  0.1819  0.0586  181  ILE E CA  
15347 C  C   . ILE E 181  ? 0.9996 0.6332 0.7000 0.1484  0.1843  0.0626  181  ILE E C   
15348 O  O   . ILE E 181  ? 1.0088 0.6248 0.6909 0.1539  0.1894  0.0658  181  ILE E O   
15349 C  CB  . ILE E 181  ? 0.9301 0.5698 0.6454 0.1229  0.1865  0.0554  181  ILE E CB  
15350 C  CG1 . ILE E 181  ? 0.9044 0.5561 0.6319 0.1114  0.1855  0.0518  181  ILE E CG1 
15351 C  CG2 . ILE E 181  ? 0.9917 0.6023 0.6834 0.1222  0.1956  0.0575  181  ILE E CG2 
15352 C  CD1 . ILE E 181  ? 1.0070 0.6509 0.7340 0.0980  0.1897  0.0483  181  ILE E CD1 
15353 N  N   . ARG E 182  ? 1.4065 1.0465 1.1133 0.1530  0.1808  0.0625  182  ARG E N   
15354 C  CA  . ARG E 182  ? 1.4621 1.0904 1.1556 0.1656  0.1824  0.0662  182  ARG E CA  
15355 C  C   . ARG E 182  ? 1.4649 1.1006 1.1573 0.1780  0.1788  0.0691  182  ARG E C   
15356 O  O   . ARG E 182  ? 1.4083 1.0282 1.0830 0.1879  0.1823  0.0727  182  ARG E O   
15357 C  CB  . ARG E 182  ? 1.4386 1.0754 1.1417 0.1677  0.1790  0.0653  182  ARG E CB  
15358 C  CG  . ARG E 182  ? 1.4545 1.0738 1.1480 0.1613  0.1845  0.0643  182  ARG E CG  
15359 C  CD  . ARG E 182  ? 1.5997 1.1924 1.2687 0.1687  0.1914  0.0680  182  ARG E CD  
15360 N  NE  . ARG E 182  ? 1.7775 1.3530 1.4369 0.1630  0.1965  0.0669  182  ARG E NE  
15361 C  CZ  . ARG E 182  ? 1.7363 1.2916 1.3821 0.1541  0.2034  0.0660  182  ARG E CZ  
15362 N  NH1 . ARG E 182  ? 1.7583 1.3073 1.3981 0.1497  0.2066  0.0662  182  ARG E NH1 
15363 N  NH2 . ARG E 182  ? 1.6510 1.1917 1.2889 0.1493  0.2073  0.0646  182  ARG E NH2 
15364 N  N   . ALA E 183  ? 1.2281 0.8875 0.9390 0.1780  0.1717  0.0674  183  ALA E N   
15365 C  CA  . ALA E 183  ? 1.1592 0.8270 0.8701 0.1892  0.1676  0.0695  183  ALA E CA  
15366 C  C   . ALA E 183  ? 1.1860 0.8390 0.8806 0.1899  0.1724  0.0714  183  ALA E C   
15367 O  O   . ALA E 183  ? 1.2087 0.8552 0.8913 0.2015  0.1727  0.0746  183  ALA E O   
15368 C  CB  . ALA E 183  ? 1.1906 0.8866 0.9251 0.1878  0.1590  0.0667  183  ALA E CB  
15369 N  N   . LEU E 184  ? 1.0803 0.7279 0.7741 0.1778  0.1764  0.0695  184  LEU E N   
15370 C  CA  . LEU E 184  ? 1.0983 0.7300 0.7757 0.1775  0.1822  0.0715  184  LEU E CA  
15371 C  C   . LEU E 184  ? 1.1203 0.7234 0.7727 0.1824  0.1903  0.0750  184  LEU E C   
15372 O  O   . LEU E 184  ? 1.1727 0.7628 0.8086 0.1903  0.1935  0.0783  184  LEU E O   
15373 C  CB  . LEU E 184  ? 1.0063 0.6392 0.6896 0.1626  0.1851  0.0683  184  LEU E CB  
15374 C  CG  . LEU E 184  ? 0.9492 0.6066 0.6525 0.1584  0.1785  0.0654  184  LEU E CG  
15375 C  CD1 . LEU E 184  ? 0.8855 0.5432 0.5944 0.1435  0.1819  0.0622  184  LEU E CD1 
15376 C  CD2 . LEU E 184  ? 1.0550 0.7152 0.7531 0.1677  0.1765  0.0677  184  LEU E CD2 
15377 N  N   . GLN E 185  ? 1.3696 0.9620 1.0183 0.1782  0.1937  0.0744  185  GLN E N   
15378 C  CA  . GLN E 185  ? 1.4118 0.9761 1.0364 0.1828  0.2015  0.0776  185  GLN E CA  
15379 C  C   . GLN E 185  ? 1.4422 1.0042 1.0577 0.1999  0.1992  0.0815  185  GLN E C   
15380 O  O   . GLN E 185  ? 1.4616 1.0018 1.0549 0.2073  0.2049  0.0852  185  GLN E O   
15381 C  CB  . GLN E 185  ? 1.3952 0.9506 1.0192 0.1750  0.2047  0.0757  185  GLN E CB  
15382 C  CG  . GLN E 185  ? 1.4398 0.9837 1.0605 0.1595  0.2109  0.0731  185  GLN E CG  
15383 C  CD  . GLN E 185  ? 1.4077 0.9435 1.0282 0.1520  0.2134  0.0707  185  GLN E CD  
15384 O  OE1 . GLN E 185  ? 1.4372 0.9796 1.0635 0.1572  0.2096  0.0707  185  GLN E OE1 
15385 N  NE2 . GLN E 185  ? 1.4487 0.9703 1.0625 0.1395  0.2198  0.0687  185  GLN E NE2 
15386 N  N   . LEU E 186  ? 1.2966 0.8809 0.9289 0.2063  0.1910  0.0807  186  LEU E N   
15387 C  CA  . LEU E 186  ? 1.1877 0.7734 0.8141 0.2227  0.1880  0.0839  186  LEU E CA  
15388 C  C   . LEU E 186  ? 1.2233 0.8128 0.8453 0.2302  0.1858  0.0856  186  LEU E C   
15389 O  O   . LEU E 186  ? 1.3108 0.8880 0.9159 0.2427  0.1876  0.0892  186  LEU E O   
15390 C  CB  . LEU E 186  ? 1.1823 0.7919 0.8293 0.2265  0.1801  0.0821  186  LEU E CB  
15391 C  CG  . LEU E 186  ? 1.1199 0.7407 0.7686 0.2423  0.1744  0.0843  186  LEU E CG  
15392 C  CD1 . LEU E 186  ? 1.1286 0.7283 0.7556 0.2542  0.1793  0.0882  186  LEU E CD1 
15393 C  CD2 . LEU E 186  ? 1.2754 0.9232 0.9485 0.2432  0.1664  0.0818  186  LEU E CD2 
15394 N  N   . SER E 187  ? 1.8191 1.4251 1.4555 0.2231  0.1820  0.0830  187  SER E N   
15395 C  CA  . SER E 187  ? 1.8740 1.4848 1.5072 0.2299  0.1794  0.0843  187  SER E CA  
15396 C  C   . SER E 187  ? 1.8197 1.4039 1.4274 0.2317  0.1879  0.0876  187  SER E C   
15397 O  O   . SER E 187  ? 1.8873 1.4703 1.4865 0.2407  0.1867  0.0897  187  SER E O   
15398 C  CB  . SER E 187  ? 1.8597 1.4923 1.5132 0.2208  0.1742  0.0807  187  SER E CB  
15399 O  OG  . SER E 187  ? 1.8035 1.4267 1.4545 0.2071  0.1802  0.0792  187  SER E OG  
15400 N  N   . GLN E 188  ? 1.1641 0.7265 0.7591 0.2233  0.1964  0.0880  188  GLN E N   
15401 C  CA  . GLN E 188  ? 1.1985 0.7332 0.7681 0.2241  0.2055  0.0912  188  GLN E CA  
15402 C  C   . GLN E 188  ? 1.2773 0.7881 0.8252 0.2334  0.2109  0.0949  188  GLN E C   
15403 O  O   . GLN E 188  ? 1.3487 0.8327 0.8749 0.2314  0.2200  0.0972  188  GLN E O   
15404 C  CB  . GLN E 188  ? 1.1398 0.6655 0.7094 0.2072  0.2121  0.0890  188  GLN E CB  
15405 C  CG  . GLN E 188  ? 1.0293 0.5766 0.6184 0.1980  0.2078  0.0855  188  GLN E CG  
15406 C  CD  . GLN E 188  ? 1.0558 0.6092 0.6417 0.2065  0.2049  0.0873  188  GLN E CD  
15407 O  OE1 . GLN E 188  ? 1.0680 0.6055 0.6381 0.2058  0.2113  0.0893  188  GLN E OE1 
15408 N  NE2 . GLN E 188  ? 1.0602 0.6368 0.6613 0.2145  0.1953  0.0864  188  GLN E NE2 
15409 N  N   . ASN E 189  ? 1.4622 0.9821 1.0153 0.2436  0.2057  0.0955  189  ASN E N   
15410 C  CA  . ASN E 189  ? 1.4735 0.9725 1.0068 0.2540  0.2101  0.0989  189  ASN E CA  
15411 C  C   . ASN E 189  ? 1.3725 0.8815 0.9049 0.2719  0.2038  0.1013  189  ASN E C   
15412 O  O   . ASN E 189  ? 1.2907 0.8160 0.8367 0.2770  0.1979  0.1002  189  ASN E O   
15413 C  CB  . ASN E 189  ? 1.2840 0.7810 0.8230 0.2478  0.2114  0.0971  189  ASN E CB  
15414 C  CG  . ASN E 189  ? 1.3905 0.8616 0.9146 0.2362  0.2212  0.0969  189  ASN E CG  
15415 O  OD1 . ASN E 189  ? 1.5123 0.9633 1.0184 0.2346  0.2281  0.0989  189  ASN E OD1 
15416 N  ND2 . ASN E 189  ? 1.5858 1.0570 1.1172 0.2280  0.2220  0.0944  189  ASN E ND2 
15417 N  N   . ILE F 11   ? 2.4176 1.8374 2.1291 0.1960  -0.0628 -0.2083 11   ILE F N   
15418 C  CA  . ILE F 11   ? 2.4503 1.8481 2.1596 0.1871  -0.0576 -0.2073 11   ILE F CA  
15419 C  C   . ILE F 11   ? 2.4641 1.8612 2.1871 0.1697  -0.0598 -0.2127 11   ILE F C   
15420 O  O   . ILE F 11   ? 2.4640 1.8619 2.1982 0.1598  -0.0563 -0.2098 11   ILE F O   
15421 C  CB  . ILE F 11   ? 2.3708 1.7351 2.0553 0.1945  -0.0540 -0.2087 11   ILE F CB  
15422 C  CG1 . ILE F 11   ? 2.3778 1.7445 2.0495 0.2122  -0.0520 -0.2035 11   ILE F CG1 
15423 C  CG2 . ILE F 11   ? 2.2997 1.6405 1.9812 0.1856  -0.0478 -0.2072 11   ILE F CG2 
15424 C  CD1 . ILE F 11   ? 2.3623 1.7431 2.0425 0.2151  -0.0479 -0.1949 11   ILE F CD1 
15425 N  N   . PRO F 12   ? 2.7970 2.1930 2.5193 0.1660  -0.0657 -0.2207 12   PRO F N   
15426 C  CA  . PRO F 12   ? 2.7876 2.1870 2.5252 0.1496  -0.0685 -0.2259 12   PRO F CA  
15427 C  C   . PRO F 12   ? 2.7857 2.2167 2.5471 0.1434  -0.0705 -0.2227 12   PRO F C   
15428 O  O   . PRO F 12   ? 2.7807 2.2144 2.5566 0.1300  -0.0695 -0.2235 12   PRO F O   
15429 C  CB  . PRO F 12   ? 2.8467 2.2411 2.5771 0.1499  -0.0751 -0.2349 12   PRO F CB  
15430 C  CG  . PRO F 12   ? 2.8421 2.2407 2.5591 0.1664  -0.0765 -0.2332 12   PRO F CG  
15431 C  CD  . PRO F 12   ? 2.8717 2.2596 2.5779 0.1757  -0.0696 -0.2257 12   PRO F CD  
15432 N  N   . GLN F 13   ? 2.9940 2.4488 2.7597 0.1528  -0.0730 -0.2192 13   GLN F N   
15433 C  CA  . GLN F 13   ? 2.9328 2.4170 2.7200 0.1479  -0.0744 -0.2155 13   GLN F CA  
15434 C  C   . GLN F 13   ? 2.9451 2.4296 2.7393 0.1446  -0.0678 -0.2082 13   GLN F C   
15435 O  O   . GLN F 13   ? 2.9509 2.4505 2.7634 0.1347  -0.0677 -0.2066 13   GLN F O   
15436 C  CB  . GLN F 13   ? 2.8176 2.3250 2.6060 0.1594  -0.0777 -0.2130 13   GLN F CB  
15437 C  CG  . GLN F 13   ? 2.9711 2.4772 2.7500 0.1649  -0.0836 -0.2196 13   GLN F CG  
15438 C  CD  . GLN F 13   ? 3.0547 2.5431 2.8114 0.1785  -0.0816 -0.2194 13   GLN F CD  
15439 O  OE1 . GLN F 13   ? 2.9851 2.4696 2.7352 0.1865  -0.0766 -0.2132 13   GLN F OE1 
15440 N  NE2 . GLN F 13   ? 3.0185 2.4961 2.7632 0.1815  -0.0858 -0.2262 13   GLN F NE2 
15441 N  N   . LEU F 14   ? 1.8006 1.2686 1.5800 0.1531  -0.0623 -0.2036 14   LEU F N   
15442 C  CA  . LEU F 14   ? 1.6741 1.1395 1.4579 0.1505  -0.0558 -0.1967 14   LEU F CA  
15443 C  C   . LEU F 14   ? 1.7576 1.2061 1.5460 0.1359  -0.0527 -0.1993 14   LEU F C   
15444 O  O   . LEU F 14   ? 1.7083 1.1640 1.5097 0.1282  -0.0492 -0.1952 14   LEU F O   
15445 C  CB  . LEU F 14   ? 1.6443 1.0943 1.4095 0.1638  -0.0510 -0.1918 14   LEU F CB  
15446 C  CG  . LEU F 14   ? 1.5747 1.0439 1.3378 0.1780  -0.0525 -0.1875 14   LEU F CG  
15447 C  CD1 . LEU F 14   ? 1.6578 1.1085 1.4002 0.1915  -0.0485 -0.1844 14   LEU F CD1 
15448 C  CD2 . LEU F 14   ? 1.6057 1.1010 1.3869 0.1758  -0.0515 -0.1813 14   LEU F CD2 
15449 N  N   . GLY F 15   ? 2.9207 2.3468 2.6986 0.1318  -0.0538 -0.2062 15   GLY F N   
15450 C  CA  . GLY F 15   ? 2.9112 2.3216 2.6941 0.1171  -0.0510 -0.2094 15   GLY F CA  
15451 C  C   . GLY F 15   ? 2.8500 2.2819 2.6560 0.1039  -0.0553 -0.2128 15   GLY F C   
15452 O  O   . GLY F 15   ? 2.8780 2.3088 2.6958 0.0920  -0.0518 -0.2120 15   GLY F O   
15453 N  N   . GLN F 16   ? 2.4057 1.8573 2.2181 0.1061  -0.0627 -0.2168 16   GLN F N   
15454 C  CA  . GLN F 16   ? 2.3966 1.8713 2.2310 0.0952  -0.0673 -0.2196 16   GLN F CA  
15455 C  C   . GLN F 16   ? 2.3981 1.8949 2.2485 0.0940  -0.0644 -0.2120 16   GLN F C   
15456 O  O   . GLN F 16   ? 2.3587 1.8650 2.2264 0.0821  -0.0639 -0.2123 16   GLN F O   
15457 C  CB  . GLN F 16   ? 2.4782 1.9684 2.3136 0.0998  -0.0757 -0.2249 16   GLN F CB  
15458 C  CG  . GLN F 16   ? 2.4794 1.9980 2.3368 0.0921  -0.0807 -0.2263 16   GLN F CG  
15459 C  CD  . GLN F 16   ? 2.4807 2.0207 2.3388 0.1018  -0.0866 -0.2264 16   GLN F CD  
15460 O  OE1 . GLN F 16   ? 2.4769 2.0130 2.3204 0.1145  -0.0864 -0.2244 16   GLN F OE1 
15461 N  NE2 . GLN F 16   ? 2.5144 2.0774 2.3894 0.0959  -0.0918 -0.2286 16   GLN F NE2 
15462 N  N   . VAL F 17   ? 1.9112 1.4166 1.7563 0.1063  -0.0626 -0.2052 17   VAL F N   
15463 C  CA  . VAL F 17   ? 1.8175 1.3420 1.6760 0.1059  -0.0595 -0.1977 17   VAL F CA  
15464 C  C   . VAL F 17   ? 1.7642 1.2735 1.6239 0.0985  -0.0520 -0.1940 17   VAL F C   
15465 O  O   . VAL F 17   ? 1.7061 1.2286 1.5821 0.0906  -0.0500 -0.1909 17   VAL F O   
15466 C  CB  . VAL F 17   ? 1.7780 1.3129 1.6289 0.1209  -0.0591 -0.1917 17   VAL F CB  
15467 C  CG1 . VAL F 17   ? 1.6686 1.2175 1.5300 0.1210  -0.0547 -0.1836 17   VAL F CG1 
15468 C  CG2 . VAL F 17   ? 1.7716 1.3265 1.6256 0.1266  -0.0661 -0.1946 17   VAL F CG2 
15469 N  N   . GLN F 18   ? 2.4294 1.9099 2.2713 0.1011  -0.0475 -0.1942 18   GLN F N   
15470 C  CA  . GLN F 18   ? 2.4155 1.8785 2.2564 0.0943  -0.0399 -0.1908 18   GLN F CA  
15471 C  C   . GLN F 18   ? 2.4062 1.8683 2.2619 0.0774  -0.0399 -0.1957 18   GLN F C   
15472 O  O   . GLN F 18   ? 2.3483 1.8131 2.2151 0.0693  -0.0351 -0.1920 18   GLN F O   
15473 C  CB  . GLN F 18   ? 2.3948 1.8256 2.2120 0.1009  -0.0354 -0.1908 18   GLN F CB  
15474 C  CG  . GLN F 18   ? 2.3510 1.7637 2.1632 0.0982  -0.0267 -0.1851 18   GLN F CG  
15475 C  CD  . GLN F 18   ? 2.4187 1.8088 2.2307 0.0844  -0.0231 -0.1898 18   GLN F CD  
15476 O  OE1 . GLN F 18   ? 2.3772 1.7659 2.1936 0.0765  -0.0276 -0.1975 18   GLN F OE1 
15477 N  NE2 . GLN F 18   ? 2.4775 1.8496 2.2842 0.0815  -0.0150 -0.1851 18   GLN F NE2 
15478 N  N   . MET F 19   ? 2.6000 2.0584 2.4561 0.0719  -0.0453 -0.2042 19   MET F N   
15479 C  CA  . MET F 19   ? 2.5797 2.0389 2.4508 0.0557  -0.0460 -0.2096 19   MET F CA  
15480 C  C   . MET F 19   ? 2.5550 2.0459 2.4500 0.0499  -0.0491 -0.2082 19   MET F C   
15481 O  O   . MET F 19   ? 2.5625 2.0568 2.4721 0.0378  -0.0462 -0.2081 19   MET F O   
15482 C  CB  . MET F 19   ? 2.5927 2.0418 2.4583 0.0522  -0.0519 -0.2195 19   MET F CB  
15483 C  CG  . MET F 19   ? 2.6996 2.1135 2.5457 0.0515  -0.0477 -0.2225 19   MET F CG  
15484 S  SD  . MET F 19   ? 2.8515 2.2482 2.7064 0.0326  -0.0418 -0.2256 19   MET F SD  
15485 C  CE  . MET F 19   ? 2.7078 2.0730 2.5419 0.0387  -0.0310 -0.2183 19   MET F CE  
15486 N  N   . LEU F 20   ? 2.0469 1.5609 1.9458 0.0584  -0.0547 -0.2070 20   LEU F N   
15487 C  CA  . LEU F 20   ? 1.9617 1.5054 1.8818 0.0540  -0.0575 -0.2051 20   LEU F CA  
15488 C  C   . LEU F 20   ? 1.8935 1.4429 1.8205 0.0536  -0.0507 -0.1964 20   LEU F C   
15489 O  O   . LEU F 20   ? 1.9058 1.4694 1.8509 0.0441  -0.0498 -0.1955 20   LEU F O   
15490 C  CB  . LEU F 20   ? 1.9831 1.5479 1.9035 0.0641  -0.0643 -0.2053 20   LEU F CB  
15491 C  CG  . LEU F 20   ? 2.0465 1.6125 1.9645 0.0637  -0.0723 -0.2140 20   LEU F CG  
15492 C  CD1 . LEU F 20   ? 1.9717 1.5586 1.8893 0.0745  -0.0778 -0.2129 20   LEU F CD1 
15493 C  CD2 . LEU F 20   ? 2.0168 1.5905 1.9519 0.0493  -0.0757 -0.2203 20   LEU F CD2 
15494 N  N   . GLY F 21   ? 1.9082 1.4471 1.8208 0.0640  -0.0459 -0.1902 21   GLY F N   
15495 C  CA  . GLY F 21   ? 1.8403 1.3828 1.7577 0.0641  -0.0394 -0.1821 21   GLY F CA  
15496 C  C   . GLY F 21   ? 1.8858 1.4114 1.8065 0.0523  -0.0327 -0.1819 21   GLY F C   
15497 O  O   . GLY F 21   ? 1.8489 1.3843 1.7824 0.0466  -0.0289 -0.1775 21   GLY F O   
15498 N  N   . LEU F 22   ? 1.8606 1.3602 1.7696 0.0485  -0.0310 -0.1867 22   LEU F N   
15499 C  CA  . LEU F 22   ? 1.8334 1.3157 1.7455 0.0362  -0.0245 -0.1873 22   LEU F CA  
15500 C  C   . LEU F 22   ? 1.8337 1.3330 1.7688 0.0218  -0.0271 -0.1918 22   LEU F C   
15501 O  O   . LEU F 22   ? 1.7860 1.2859 1.7321 0.0125  -0.0215 -0.1891 22   LEU F O   
15502 C  CB  . LEU F 22   ? 1.8411 1.2914 1.7349 0.0353  -0.0224 -0.1920 22   LEU F CB  
15503 C  CG  . LEU F 22   ? 1.9292 1.3545 1.8005 0.0457  -0.0159 -0.1865 22   LEU F CG  
15504 C  CD1 . LEU F 22   ? 1.9995 1.3925 1.8540 0.0429  -0.0138 -0.1919 22   LEU F CD1 
15505 C  CD2 . LEU F 22   ? 1.9260 1.3490 1.8007 0.0435  -0.0077 -0.1786 22   LEU F CD2 
15506 N  N   . ALA F 23   ? 2.0748 1.5883 2.0171 0.0201  -0.0355 -0.1986 23   ALA F N   
15507 C  CA  . ALA F 23   ? 2.0321 1.5634 1.9964 0.0073  -0.0389 -0.2033 23   ALA F CA  
15508 C  C   . ALA F 23   ? 2.0073 1.5659 1.9890 0.0072  -0.0385 -0.1974 23   ALA F C   
15509 O  O   . ALA F 23   ? 2.0124 1.5797 2.0111 -0.0040 -0.0362 -0.1976 23   ALA F O   
15510 C  CB  . ALA F 23   ? 1.9533 1.4934 1.9197 0.0070  -0.0485 -0.2119 23   ALA F CB  
15511 N  N   . ALA F 24   ? 2.0386 1.6109 2.0163 0.0195  -0.0406 -0.1922 24   ALA F N   
15512 C  CA  . ALA F 24   ? 1.9936 1.5905 1.9862 0.0200  -0.0400 -0.1863 24   ALA F CA  
15513 C  C   . ALA F 24   ? 1.9827 1.5706 1.9756 0.0174  -0.0307 -0.1792 24   ALA F C   
15514 O  O   . ALA F 24   ? 2.0018 1.6054 2.0110 0.0113  -0.0287 -0.1762 24   ALA F O   
15515 C  CB  . ALA F 24   ? 1.9246 1.5365 1.9116 0.0338  -0.0440 -0.1827 24   ALA F CB  
15516 N  N   . ALA F 25   ? 1.4975 1.0600 1.4722 0.0221  -0.0250 -0.1764 25   ALA F N   
15517 C  CA  . ALA F 25   ? 1.3947 0.9467 1.3675 0.0205  -0.0160 -0.1695 25   ALA F CA  
15518 C  C   . ALA F 25   ? 1.4942 1.0380 1.4780 0.0051  -0.0113 -0.1722 25   ALA F C   
15519 O  O   . ALA F 25   ? 1.4452 0.9961 1.4401 -0.0001 -0.0061 -0.1675 25   ALA F O   
15520 C  CB  . ALA F 25   ? 1.3286 0.8549 1.2777 0.0304  -0.0114 -0.1661 25   ALA F CB  
15521 N  N   . VAL F 26   ? 1.6653 1.1944 1.6466 -0.0023 -0.0127 -0.1798 26   VAL F N   
15522 C  CA  . VAL F 26   ? 1.6628 1.1832 1.6545 -0.0175 -0.0079 -0.1828 26   VAL F CA  
15523 C  C   . VAL F 26   ? 1.6658 1.2144 1.6831 -0.0270 -0.0118 -0.1854 26   VAL F C   
15524 O  O   . VAL F 26   ? 1.6352 1.1853 1.6654 -0.0378 -0.0064 -0.1844 26   VAL F O   
15525 C  CB  . VAL F 26   ? 1.6141 1.1102 1.5954 -0.0230 -0.0085 -0.1906 26   VAL F CB  
15526 C  CG1 . VAL F 26   ? 1.6258 1.1351 1.6125 -0.0235 -0.0189 -0.1990 26   VAL F CG1 
15527 C  CG2 . VAL F 26   ? 1.5048 0.9878 1.4944 -0.0383 -0.0017 -0.1928 26   VAL F CG2 
15528 N  N   . ILE F 27   ? 1.9050 1.4761 1.9296 -0.0230 -0.0208 -0.1886 27   ILE F N   
15529 C  CA  . ILE F 27   ? 1.9276 1.5265 1.9757 -0.0304 -0.0248 -0.1906 27   ILE F CA  
15530 C  C   . ILE F 27   ? 1.9583 1.5725 2.0151 -0.0279 -0.0204 -0.1820 27   ILE F C   
15531 O  O   . ILE F 27   ? 1.9976 1.6229 2.0717 -0.0374 -0.0175 -0.1814 27   ILE F O   
15532 C  CB  . ILE F 27   ? 1.8791 1.4968 1.9309 -0.0257 -0.0355 -0.1960 27   ILE F CB  
15533 C  CG1 . ILE F 27   ? 1.8022 1.4083 1.8512 -0.0321 -0.0402 -0.2059 27   ILE F CG1 
15534 C  CG2 . ILE F 27   ? 1.7467 1.3954 1.8203 -0.0292 -0.0394 -0.1956 27   ILE F CG2 
15535 C  CD1 . ILE F 27   ? 1.6779 1.2989 1.7270 -0.0263 -0.0506 -0.2114 27   ILE F CD1 
15536 N  N   . GLY F 28   ? 2.2733 1.8884 2.3183 -0.0150 -0.0197 -0.1754 28   GLY F N   
15537 C  CA  . GLY F 28   ? 2.1252 1.7541 2.1770 -0.0119 -0.0157 -0.1673 28   GLY F CA  
15538 C  C   . GLY F 28   ? 2.2164 1.8302 2.2681 -0.0183 -0.0057 -0.1627 28   GLY F C   
15539 O  O   . GLY F 28   ? 2.2605 1.8879 2.3265 -0.0232 -0.0024 -0.1591 28   GLY F O   
15540 N  N   . ILE F 29   ? 1.9645 1.5496 1.9996 -0.0180 -0.0004 -0.1627 29   ILE F N   
15541 C  CA  . ILE F 29   ? 1.9813 1.5494 2.0144 -0.0241 0.0097  -0.1584 29   ILE F CA  
15542 C  C   . ILE F 29   ? 2.0314 1.6037 2.0833 -0.0401 0.0118  -0.1629 29   ILE F C   
15543 O  O   . ILE F 29   ? 2.0205 1.5945 2.0813 -0.0463 0.0188  -0.1587 29   ILE F O   
15544 C  CB  . ILE F 29   ? 2.0574 1.5925 2.0670 -0.0196 0.0146  -0.1577 29   ILE F CB  
15545 C  CG1 . ILE F 29   ? 2.0131 1.5454 2.0054 -0.0034 0.0139  -0.1518 29   ILE F CG1 
15546 C  CG2 . ILE F 29   ? 2.0443 1.5591 2.0519 -0.0279 0.0252  -0.1546 29   ILE F CG2 
15547 C  CD1 . ILE F 29   ? 1.8416 1.3878 1.8386 0.0016  0.0173  -0.1434 29   ILE F CD1 
15548 N  N   . GLY F 30   ? 2.4328 2.0077 2.4912 -0.0469 0.0058  -0.1717 30   GLY F N   
15549 C  CA  . GLY F 30   ? 2.4509 2.0308 2.5278 -0.0624 0.0073  -0.1769 30   GLY F CA  
15550 C  C   . GLY F 30   ? 2.4565 2.0665 2.5560 -0.0662 0.0057  -0.1750 30   GLY F C   
15551 O  O   . GLY F 30   ? 2.5753 2.1875 2.6872 -0.0757 0.0120  -0.1733 30   GLY F O   
15552 N  N   . VAL F 31   ? 1.8791 1.5125 1.9838 -0.0587 -0.0026 -0.1753 31   VAL F N   
15553 C  CA  . VAL F 31   ? 1.8759 1.5378 2.0008 -0.0612 -0.0045 -0.1733 31   VAL F CA  
15554 C  C   . VAL F 31   ? 1.9314 1.5948 2.0544 -0.0563 0.0028  -0.1635 31   VAL F C   
15555 O  O   . VAL F 31   ? 1.9050 1.5846 2.0444 -0.0616 0.0053  -0.1610 31   VAL F O   
15556 C  CB  . VAL F 31   ? 1.7798 1.4645 1.9092 -0.0542 -0.0152 -0.1764 31   VAL F CB  
15557 C  CG1 . VAL F 31   ? 1.7905 1.4704 1.9013 -0.0394 -0.0173 -0.1720 31   VAL F CG1 
15558 C  CG2 . VAL F 31   ? 1.7775 1.4913 1.9274 -0.0566 -0.0173 -0.1746 31   VAL F CG2 
15559 N  N   . LEU F 32   ? 2.4852 2.1318 2.5884 -0.0461 0.0062  -0.1580 32   LEU F N   
15560 C  CA  . LEU F 32   ? 2.4655 2.1105 2.5653 -0.0418 0.0136  -0.1489 32   LEU F CA  
15561 C  C   . LEU F 32   ? 2.4526 2.0832 2.5565 -0.0525 0.0234  -0.1472 32   LEU F C   
15562 O  O   . LEU F 32   ? 2.4037 2.0436 2.5171 -0.0548 0.0285  -0.1420 32   LEU F O   
15563 C  CB  . LEU F 32   ? 2.3949 2.0243 2.4719 -0.0284 0.0147  -0.1440 32   LEU F CB  
15564 C  CG  . LEU F 32   ? 2.3005 1.9360 2.3737 -0.0198 0.0185  -0.1350 32   LEU F CG  
15565 C  CD1 . LEU F 32   ? 2.2262 1.8926 2.3164 -0.0189 0.0136  -0.1338 32   LEU F CD1 
15566 C  CD2 . LEU F 32   ? 2.2185 1.8418 2.2702 -0.0060 0.0176  -0.1317 32   LEU F CD2 
15567 N  N   . ALA F 33   ? 2.0236 1.6310 2.1200 -0.0591 0.0265  -0.1516 33   ALA F N   
15568 C  CA  . ALA F 33   ? 2.0707 1.6638 2.1715 -0.0704 0.0362  -0.1507 33   ALA F CA  
15569 C  C   . ALA F 33   ? 2.1306 1.7448 2.2572 -0.0830 0.0355  -0.1545 33   ALA F C   
15570 O  O   . ALA F 33   ? 2.1981 1.8117 2.3334 -0.0903 0.0435  -0.1511 33   ALA F O   
15571 C  CB  . ALA F 33   ? 2.0365 1.5997 2.1232 -0.0747 0.0393  -0.1551 33   ALA F CB  
15572 N  N   . ALA F 34   ? 1.8521 1.4852 1.9910 -0.0856 0.0260  -0.1617 34   ALA F N   
15573 C  CA  . ALA F 34   ? 1.8251 1.4813 1.9891 -0.0963 0.0243  -0.1654 34   ALA F CA  
15574 C  C   . ALA F 34   ? 1.9115 1.5896 2.0861 -0.0922 0.0256  -0.1586 34   ALA F C   
15575 O  O   . ALA F 34   ? 1.9932 1.6810 2.1840 -0.1008 0.0305  -0.1575 34   ALA F O   
15576 C  CB  . ALA F 34   ? 1.8290 1.5006 2.0019 -0.0981 0.0132  -0.1743 34   ALA F CB  
15577 N  N   . GLY F 35   ? 2.3011 1.9874 2.4668 -0.0791 0.0213  -0.1540 35   GLY F N   
15578 C  CA  . GLY F 35   ? 2.3321 2.0371 2.5056 -0.0745 0.0228  -0.1473 35   GLY F CA  
15579 C  C   . GLY F 35   ? 2.3382 2.0294 2.5059 -0.0750 0.0338  -0.1395 35   GLY F C   
15580 O  O   . GLY F 35   ? 2.3211 2.0265 2.5006 -0.0768 0.0373  -0.1352 35   GLY F O   
15581 N  N   . TYR F 36   ? 1.9793 1.6423 2.1280 -0.0729 0.0394  -0.1375 36   TYR F N   
15582 C  CA  . TYR F 36   ? 1.9455 1.5929 2.0873 -0.0734 0.0503  -0.1303 36   TYR F CA  
15583 C  C   . TYR F 36   ? 1.9275 1.5742 2.0850 -0.0880 0.0574  -0.1321 36   TYR F C   
15584 O  O   . TYR F 36   ? 1.8763 1.5273 2.0400 -0.0900 0.0643  -0.1264 36   TYR F O   
15585 C  CB  . TYR F 36   ? 1.9427 1.5591 2.0596 -0.0675 0.0544  -0.1283 36   TYR F CB  
15586 C  CG  . TYR F 36   ? 1.8846 1.4800 1.9935 -0.0704 0.0663  -0.1223 36   TYR F CG  
15587 C  CD1 . TYR F 36   ? 1.8675 1.4630 1.9689 -0.0619 0.0708  -0.1137 36   TYR F CD1 
15588 C  CD2 . TYR F 36   ? 1.9577 1.5327 2.0660 -0.0815 0.0732  -0.1253 36   TYR F CD2 
15589 C  CE1 . TYR F 36   ? 1.9012 1.4771 1.9943 -0.0640 0.0817  -0.1082 36   TYR F CE1 
15590 C  CE2 . TYR F 36   ? 1.9269 1.4819 2.0271 -0.0839 0.0846  -0.1196 36   TYR F CE2 
15591 C  CZ  . TYR F 36   ? 1.8927 1.4481 1.9850 -0.0749 0.0887  -0.1110 36   TYR F CZ  
15592 O  OH  . TYR F 36   ? 1.8959 1.4310 1.9792 -0.0769 0.1000  -0.1052 36   TYR F OH  
15593 N  N   . PHE F 37   ? 2.2110 1.8523 2.3751 -0.0983 0.0559  -0.1400 37   PHE F N   
15594 C  CA  . PHE F 37   ? 2.2747 1.9169 2.4554 -0.1130 0.0624  -0.1425 37   PHE F CA  
15595 C  C   . PHE F 37   ? 2.2792 1.9530 2.4840 -0.1170 0.0596  -0.1427 37   PHE F C   
15596 O  O   . PHE F 37   ? 2.2319 1.9092 2.4491 -0.1253 0.0671  -0.1407 37   PHE F O   
15597 C  CB  . PHE F 37   ? 2.3510 1.9824 2.5341 -0.1230 0.0601  -0.1517 37   PHE F CB  
15598 C  CG  . PHE F 37   ? 2.4864 2.1172 2.6863 -0.1389 0.0669  -0.1550 37   PHE F CG  
15599 C  CD1 . PHE F 37   ? 2.5152 2.1221 2.7073 -0.1442 0.0790  -0.1509 37   PHE F CD1 
15600 C  CD2 . PHE F 37   ? 2.5153 2.1696 2.7388 -0.1483 0.0614  -0.1622 37   PHE F CD2 
15601 C  CE1 . PHE F 37   ? 2.6157 2.2222 2.8237 -0.1592 0.0858  -0.1539 37   PHE F CE1 
15602 C  CE2 . PHE F 37   ? 2.5686 2.2235 2.8086 -0.1631 0.0678  -0.1654 37   PHE F CE2 
15603 C  CZ  . PHE F 37   ? 2.6438 2.2748 2.8763 -0.1688 0.0802  -0.1613 37   PHE F CZ  
15604 N  N   . LEU F 38   ? 2.4449 2.1415 2.6560 -0.1108 0.0492  -0.1452 38   LEU F N   
15605 C  CA  . LEU F 38   ? 2.4441 2.1707 2.6765 -0.1129 0.0463  -0.1449 38   LEU F CA  
15606 C  C   . LEU F 38   ? 2.3814 2.1134 2.6108 -0.1054 0.0513  -0.1354 38   LEU F C   
15607 O  O   . LEU F 38   ? 2.3048 2.0510 2.5498 -0.1105 0.0554  -0.1331 38   LEU F O   
15608 C  CB  . LEU F 38   ? 2.3877 2.1354 2.6263 -0.1082 0.0338  -0.1503 38   LEU F CB  
15609 C  CG  . LEU F 38   ? 2.3392 2.0862 2.5831 -0.1155 0.0273  -0.1605 38   LEU F CG  
15610 C  CD1 . LEU F 38   ? 2.3915 2.1600 2.6401 -0.1092 0.0151  -0.1647 38   LEU F CD1 
15611 C  CD2 . LEU F 38   ? 2.3086 2.0613 2.5728 -0.1307 0.0311  -0.1654 38   LEU F CD2 
15612 N  N   . SER F 39   ? 2.3986 2.1199 2.6084 -0.0932 0.0510  -0.1300 39   SER F N   
15613 C  CA  . SER F 39   ? 2.3570 2.0818 2.5619 -0.0853 0.0553  -0.1212 39   SER F CA  
15614 C  C   . SER F 39   ? 2.3170 2.0175 2.4968 -0.0756 0.0588  -0.1160 39   SER F C   
15615 O  O   . SER F 39   ? 2.2965 1.9938 2.4640 -0.0670 0.0522  -0.1175 39   SER F O   
15616 C  CB  . SER F 39   ? 2.3062 2.0583 2.5195 -0.0781 0.0473  -0.1203 39   SER F CB  
15617 O  OG  . SER F 39   ? 2.1369 1.8910 2.3434 -0.0697 0.0509  -0.1120 39   SER F OG  
15618 N  N   . PRO F 40   ? 1.8955 1.5788 2.0670 -0.0764 0.0689  -0.1100 40   PRO F N   
15619 C  CA  . PRO F 40   ? 1.8762 1.5353 2.0231 -0.0669 0.0722  -0.1054 40   PRO F CA  
15620 C  C   . PRO F 40   ? 1.8278 1.4961 1.9655 -0.0531 0.0682  -0.0999 40   PRO F C   
15621 O  O   . PRO F 40   ? 1.7797 1.4341 1.8985 -0.0436 0.0664  -0.0985 40   PRO F O   
15622 C  CB  . PRO F 40   ? 1.8619 1.5022 2.0048 -0.0725 0.0845  -0.1005 40   PRO F CB  
15623 C  CG  . PRO F 40   ? 1.8789 1.5399 2.0440 -0.0808 0.0872  -0.1000 40   PRO F CG  
15624 C  CD  . PRO F 40   ? 1.8564 1.5398 2.0400 -0.0864 0.0781  -0.1078 40   PRO F CD  
15625 N  N   . THR F 41   ? 2.2518 1.9429 2.4021 -0.0516 0.0668  -0.0969 41   THR F N   
15626 C  CA  . THR F 41   ? 2.1728 1.8726 2.3147 -0.0391 0.0635  -0.0917 41   THR F CA  
15627 C  C   . THR F 41   ? 2.0739 1.7845 2.2134 -0.0322 0.0528  -0.0959 41   THR F C   
15628 O  O   . THR F 41   ? 2.0221 1.7255 2.1454 -0.0215 0.0505  -0.0935 41   THR F O   
15629 C  CB  . THR F 41   ? 2.0779 1.7986 2.2341 -0.0400 0.0651  -0.0877 41   THR F CB  
15630 O  OG1 . THR F 41   ? 2.2020 1.9121 2.3600 -0.0463 0.0754  -0.0838 41   THR F OG1 
15631 C  CG2 . THR F 41   ? 1.9159 1.6444 2.0629 -0.0275 0.0621  -0.0823 41   THR F CG2 
15632 N  N   . SER F 42   ? 1.7267 1.4548 1.8820 -0.0379 0.0463  -0.1021 42   SER F N   
15633 C  CA  . SER F 42   ? 1.6623 1.4020 1.8161 -0.0316 0.0363  -0.1061 42   SER F CA  
15634 C  C   . SER F 42   ? 1.6058 1.3250 1.7417 -0.0271 0.0343  -0.1088 42   SER F C   
15635 O  O   . SER F 42   ? 1.5040 1.2280 1.6323 -0.0183 0.0276  -0.1099 42   SER F O   
15636 C  CB  . SER F 42   ? 1.6767 1.4364 1.8501 -0.0394 0.0302  -0.1127 42   SER F CB  
15637 O  OG  . SER F 42   ? 1.6569 1.4049 1.8330 -0.0487 0.0309  -0.1190 42   SER F OG  
15638 N  N   . PHE F 43   ? 2.0946 1.7907 2.2236 -0.0329 0.0404  -0.1100 43   PHE F N   
15639 C  CA  . PHE F 43   ? 2.0817 1.7558 2.1920 -0.0283 0.0394  -0.1122 43   PHE F CA  
15640 C  C   . PHE F 43   ? 1.9879 1.6537 2.0795 -0.0149 0.0403  -0.1060 43   PHE F C   
15641 O  O   . PHE F 43   ? 1.9909 1.6551 2.0716 -0.0063 0.0345  -0.1076 43   PHE F O   
15642 C  CB  . PHE F 43   ? 2.1750 1.8248 2.2812 -0.0376 0.0470  -0.1139 43   PHE F CB  
15643 C  CG  . PHE F 43   ? 2.2073 1.8299 2.2909 -0.0316 0.0487  -0.1139 43   PHE F CG  
15644 C  CD1 . PHE F 43   ? 2.2026 1.8199 2.2803 -0.0303 0.0422  -0.1203 43   PHE F CD1 
15645 C  CD2 . PHE F 43   ? 2.1617 1.7636 2.2292 -0.0268 0.0567  -0.1075 43   PHE F CD2 
15646 C  CE1 . PHE F 43   ? 2.0863 1.6782 2.1427 -0.0244 0.0438  -0.1203 43   PHE F CE1 
15647 C  CE2 . PHE F 43   ? 2.1882 1.7648 2.2344 -0.0207 0.0582  -0.1074 43   PHE F CE2 
15648 C  CZ  . PHE F 43   ? 2.1404 1.7119 2.1810 -0.0194 0.0519  -0.1138 43   PHE F CZ  
15649 N  N   . PHE F 44   ? 1.7224 1.3829 1.8099 -0.0128 0.0475  -0.0990 44   PHE F N   
15650 C  CA  . PHE F 44   ? 1.7077 1.3611 1.7780 -0.0001 0.0484  -0.0932 44   PHE F CA  
15651 C  C   . PHE F 44   ? 1.6264 1.3037 1.7012 0.0082  0.0411  -0.0919 44   PHE F C   
15652 O  O   . PHE F 44   ? 1.5858 1.2603 1.6470 0.0193  0.0381  -0.0901 44   PHE F O   
15653 C  CB  . PHE F 44   ? 1.7892 1.4311 1.8542 -0.0003 0.0579  -0.0862 44   PHE F CB  
15654 C  CG  . PHE F 44   ? 1.8769 1.4900 1.9306 -0.0050 0.0657  -0.0862 44   PHE F CG  
15655 C  CD1 . PHE F 44   ? 1.8354 1.4256 1.8666 0.0038  0.0677  -0.0840 44   PHE F CD1 
15656 C  CD2 . PHE F 44   ? 1.8889 1.4975 1.9541 -0.0181 0.0713  -0.0883 44   PHE F CD2 
15657 C  CE1 . PHE F 44   ? 1.8007 1.3630 1.8204 -0.0002 0.0753  -0.0837 44   PHE F CE1 
15658 C  CE2 . PHE F 44   ? 1.8975 1.4786 1.9519 -0.0228 0.0791  -0.0881 44   PHE F CE2 
15659 C  CZ  . PHE F 44   ? 1.8719 1.4293 1.9031 -0.0138 0.0811  -0.0858 44   PHE F CZ  
15660 N  N   . GLU F 45   ? 1.7956 1.4964 1.8892 0.0032  0.0384  -0.0928 45   GLU F N   
15661 C  CA  . GLU F 45   ? 1.7094 1.4326 1.8075 0.0105  0.0317  -0.0918 45   GLU F CA  
15662 C  C   . GLU F 45   ? 1.6288 1.3553 1.7222 0.0154  0.0234  -0.0970 45   GLU F C   
15663 O  O   . GLU F 45   ? 1.5429 1.2765 1.6291 0.0254  0.0192  -0.0952 45   GLU F O   
15664 C  CB  . GLU F 45   ? 1.7161 1.4624 1.8351 0.0036  0.0305  -0.0923 45   GLU F CB  
15665 C  CG  . GLU F 45   ? 1.7518 1.4960 1.8775 -0.0024 0.0388  -0.0878 45   GLU F CG  
15666 C  CD  . GLU F 45   ? 1.7313 1.4823 1.8533 0.0050  0.0411  -0.0808 45   GLU F CD  
15667 O  OE1 . GLU F 45   ? 1.7025 1.4495 1.8106 0.0153  0.0390  -0.0783 45   GLU F OE1 
15668 O  OE2 . GLU F 45   ? 1.8241 1.5847 1.9574 0.0005  0.0449  -0.0779 45   GLU F OE2 
15669 N  N   . SER F 46   ? 1.6011 1.3226 1.6984 0.0085  0.0210  -0.1035 46   SER F N   
15670 C  CA  . SER F 46   ? 1.5304 1.2532 1.6222 0.0129  0.0134  -0.1088 46   SER F CA  
15671 C  C   . SER F 46   ? 1.4941 1.1941 1.5647 0.0205  0.0148  -0.1082 46   SER F C   
15672 O  O   . SER F 46   ? 1.4567 1.1592 1.5189 0.0290  0.0092  -0.1097 46   SER F O   
15673 C  CB  . SER F 46   ? 1.5623 1.2882 1.6659 0.0027  0.0100  -0.1164 46   SER F CB  
15674 O  OG  . SER F 46   ? 1.5212 1.2689 1.6445 -0.0038 0.0084  -0.1171 46   SER F OG  
15675 N  N   . TYR F 47   ? 1.3678 1.0452 1.4292 0.0180  0.0224  -0.1059 47   TYR F N   
15676 C  CA  . TYR F 47   ? 1.3734 1.0276 1.4136 0.0256  0.0241  -0.1051 47   TYR F CA  
15677 C  C   . TYR F 47   ? 1.3672 1.0249 1.3959 0.0388  0.0233  -0.0996 47   TYR F C   
15678 O  O   . TYR F 47   ? 1.2693 0.9173 1.2830 0.0478  0.0209  -0.1002 47   TYR F O   
15679 C  CB  . TYR F 47   ? 1.4273 1.0563 1.4601 0.0198  0.0330  -0.1034 47   TYR F CB  
15680 C  CG  . TYR F 47   ? 1.3860 0.9885 1.3970 0.0262  0.0348  -0.1038 47   TYR F CG  
15681 C  CD1 . TYR F 47   ? 1.4050 0.9946 1.4119 0.0222  0.0326  -0.1103 47   TYR F CD1 
15682 C  CD2 . TYR F 47   ? 1.4413 1.0317 1.4355 0.0366  0.0386  -0.0977 47   TYR F CD2 
15683 C  CE1 . TYR F 47   ? 1.4464 1.0110 1.4326 0.0284  0.0344  -0.1106 47   TYR F CE1 
15684 C  CE2 . TYR F 47   ? 1.4662 1.0323 1.4400 0.0432  0.0402  -0.0980 47   TYR F CE2 
15685 C  CZ  . TYR F 47   ? 1.4982 1.0512 1.4679 0.0390  0.0383  -0.1043 47   TYR F CZ  
15686 O  OH  . TYR F 47   ? 1.4939 1.0219 1.4427 0.0459  0.0400  -0.1046 47   TYR F OH  
15687 N  N   . ILE F 48   ? 1.4618 1.1334 1.4976 0.0402  0.0253  -0.0943 48   ILE F N   
15688 C  CA  . ILE F 48   ? 1.3617 1.0394 1.3886 0.0522  0.0239  -0.0894 48   ILE F CA  
15689 C  C   . ILE F 48   ? 1.2848 0.9792 1.3134 0.0584  0.0154  -0.0926 48   ILE F C   
15690 O  O   . ILE F 48   ? 1.2531 0.9436 1.2685 0.0688  0.0131  -0.0919 48   ILE F O   
15691 C  CB  . ILE F 48   ? 1.3425 1.0328 1.3780 0.0513  0.0274  -0.0837 48   ILE F CB  
15692 C  CG1 . ILE F 48   ? 1.3647 1.0360 1.3945 0.0475  0.0365  -0.0796 48   ILE F CG1 
15693 C  CG2 . ILE F 48   ? 1.3228 1.0244 1.3523 0.0628  0.0245  -0.0798 48   ILE F CG2 
15694 C  CD1 . ILE F 48   ? 1.3808 1.0629 1.4175 0.0472  0.0403  -0.0739 48   ILE F CD1 
15695 N  N   . TYR F 49   ? 1.4218 1.1354 1.4666 0.0524  0.0107  -0.0963 49   TYR F N   
15696 C  CA  . TYR F 49   ? 1.3756 1.1051 1.4224 0.0578  0.0029  -0.0994 49   TYR F CA  
15697 C  C   . TYR F 49   ? 1.4183 1.1342 1.4537 0.0607  -0.0004 -0.1045 49   TYR F C   
15698 O  O   . TYR F 49   ? 1.4590 1.1789 1.4864 0.0698  -0.0048 -0.1051 49   TYR F O   
15699 C  CB  . TYR F 49   ? 1.3795 1.1307 1.4456 0.0504  -0.0010 -0.1022 49   TYR F CB  
15700 C  CG  . TYR F 49   ? 1.2910 1.0547 1.3594 0.0533  -0.0091 -0.1072 49   TYR F CG  
15701 C  CD1 . TYR F 49   ? 1.2941 1.0678 1.3566 0.0634  -0.0129 -0.1055 49   TYR F CD1 
15702 C  CD2 . TYR F 49   ? 1.2333 0.9989 1.3097 0.0459  -0.0128 -0.1136 49   TYR F CD2 
15703 C  CE1 . TYR F 49   ? 1.2754 1.0599 1.3394 0.0662  -0.0197 -0.1099 49   TYR F CE1 
15704 C  CE2 . TYR F 49   ? 1.3343 1.1107 1.4119 0.0489  -0.0201 -0.1181 49   TYR F CE2 
15705 C  CZ  . TYR F 49   ? 1.3163 1.1018 1.3873 0.0591  -0.0233 -0.1161 49   TYR F CZ  
15706 O  OH  . TYR F 49   ? 1.3111 1.1068 1.3828 0.0623  -0.0301 -0.1204 49   TYR F OH  
15707 N  N   . GLY F 50   ? 1.1338 0.8335 1.1684 0.0529  0.0018  -0.1083 50   GLY F N   
15708 C  CA  . GLY F 50   ? 1.1910 0.8758 1.2138 0.0554  -0.0010 -0.1133 50   GLY F CA  
15709 C  C   . GLY F 50   ? 1.1928 0.8595 1.1951 0.0660  0.0016  -0.1101 50   GLY F C   
15710 O  O   . GLY F 50   ? 1.1998 0.8631 1.1917 0.0736  -0.0025 -0.1127 50   GLY F O   
15711 N  N   . TYR F 51   ? 1.2193 0.8744 1.2153 0.0672  0.0085  -0.1046 51   TYR F N   
15712 C  CA  . TYR F 51   ? 1.2000 0.8389 1.1764 0.0782  0.0109  -0.1012 51   TYR F CA  
15713 C  C   . TYR F 51   ? 1.1922 0.8480 1.1662 0.0896  0.0065  -0.0987 51   TYR F C   
15714 O  O   . TYR F 51   ? 1.1799 0.8279 1.1394 0.0998  0.0048  -0.0988 51   TYR F O   
15715 C  CB  . TYR F 51   ? 1.1175 0.7413 1.0883 0.0768  0.0192  -0.0956 51   TYR F CB  
15716 C  CG  . TYR F 51   ? 1.2462 0.8493 1.1954 0.0875  0.0223  -0.0924 51   TYR F CG  
15717 C  CD1 . TYR F 51   ? 1.4217 0.9999 1.3566 0.0879  0.0242  -0.0953 51   TYR F CD1 
15718 C  CD2 . TYR F 51   ? 1.3251 0.9337 1.2680 0.0973  0.0232  -0.0868 51   TYR F CD2 
15719 C  CE1 . TYR F 51   ? 1.4693 1.0283 1.3839 0.0983  0.0270  -0.0924 51   TYR F CE1 
15720 C  CE2 . TYR F 51   ? 1.3638 0.9543 1.2870 0.1077  0.0257  -0.0840 51   TYR F CE2 
15721 C  CZ  . TYR F 51   ? 1.4201 0.9858 1.3290 0.1084  0.0276  -0.0867 51   TYR F CZ  
15722 O  OH  . TYR F 51   ? 1.4345 0.9818 1.3231 0.1194  0.0301  -0.0839 51   TYR F OH  
15723 N  N   . TYR F 52   ? 1.3204 0.9993 1.3084 0.0882  0.0047  -0.0965 52   TYR F N   
15724 C  CA  . TYR F 52   ? 1.2598 0.9556 1.2467 0.0981  0.0010  -0.0940 52   TYR F CA  
15725 C  C   . TYR F 52   ? 1.2399 0.9450 1.2265 0.1021  -0.0060 -0.0989 52   TYR F C   
15726 O  O   . TYR F 52   ? 1.2044 0.9137 1.1825 0.1126  -0.0086 -0.0980 52   TYR F O   
15727 C  CB  . TYR F 52   ? 1.1673 0.8841 1.1693 0.0945  0.0012  -0.0906 52   TYR F CB  
15728 C  CG  . TYR F 52   ? 1.1637 0.8958 1.1640 0.1041  -0.0010 -0.0870 52   TYR F CG  
15729 C  CD1 . TYR F 52   ? 1.1941 0.9180 1.1825 0.1121  0.0024  -0.0823 52   TYR F CD1 
15730 C  CD2 . TYR F 52   ? 1.1369 0.8918 1.1476 0.1050  -0.0064 -0.0885 52   TYR F CD2 
15731 C  CE1 . TYR F 52   ? 1.1987 0.9373 1.1863 0.1205  0.0002  -0.0794 52   TYR F CE1 
15732 C  CE2 . TYR F 52   ? 1.1366 0.9053 1.1461 0.1131  -0.0082 -0.0854 52   TYR F CE2 
15733 C  CZ  . TYR F 52   ? 1.1689 0.9299 1.1673 0.1206  -0.0050 -0.0811 52   TYR F CZ  
15734 O  OH  . TYR F 52   ? 1.1554 0.9310 1.1534 0.1283  -0.0069 -0.0784 52   TYR F OH  
15735 N  N   . VAL F 53   ? 1.0092 0.7178 1.0048 0.0942  -0.0092 -0.1043 53   VAL F N   
15736 C  CA  . VAL F 53   ? 0.9770 0.6948 0.9724 0.0979  -0.0159 -0.1090 53   VAL F CA  
15737 C  C   . VAL F 53   ? 1.0151 0.7123 0.9943 0.1026  -0.0165 -0.1125 53   VAL F C   
15738 O  O   . VAL F 53   ? 1.0110 0.7123 0.9835 0.1106  -0.0208 -0.1146 53   VAL F O   
15739 C  CB  . VAL F 53   ? 0.9922 0.7241 1.0040 0.0883  -0.0198 -0.1134 53   VAL F CB  
15740 C  CG1 . VAL F 53   ? 1.0334 0.7498 1.0475 0.0779  -0.0175 -0.1172 53   VAL F CG1 
15741 C  CG2 . VAL F 53   ? 1.0099 0.7533 1.0216 0.0928  -0.0267 -0.1178 53   VAL F CG2 
15742 N  N   . ALA F 54   ? 1.5327 1.2073 1.5049 0.0980  -0.0119 -0.1132 54   ALA F N   
15743 C  CA  . ALA F 54   ? 1.6111 1.2640 1.5670 0.1022  -0.0120 -0.1165 54   ALA F CA  
15744 C  C   . ALA F 54   ? 1.6765 1.3189 1.6152 0.1147  -0.0097 -0.1123 54   ALA F C   
15745 O  O   . ALA F 54   ? 1.7058 1.3353 1.6304 0.1215  -0.0112 -0.1149 54   ALA F O   
15746 C  CB  . ALA F 54   ? 1.5165 1.1481 1.4709 0.0923  -0.0076 -0.1188 54   ALA F CB  
15747 N  N   . MET F 55   ? 1.6702 1.3179 1.6095 0.1182  -0.0063 -0.1062 55   MET F N   
15748 C  CA  . MET F 55   ? 1.6183 1.2577 1.5420 0.1304  -0.0043 -0.1022 55   MET F CA  
15749 C  C   . MET F 55   ? 1.6087 1.2636 1.5297 0.1412  -0.0097 -0.1028 55   MET F C   
15750 O  O   . MET F 55   ? 1.5597 1.2081 1.4672 0.1522  -0.0089 -0.1005 55   MET F O   
15751 C  CB  . MET F 55   ? 1.5833 1.2252 1.5095 0.1304  0.0006  -0.0957 55   MET F CB  
15752 C  CG  . MET F 55   ? 1.6117 1.2387 1.5202 0.1413  0.0040  -0.0916 55   MET F CG  
15753 S  SD  . MET F 55   ? 1.8581 1.4489 1.7488 0.1401  0.0099  -0.0923 55   MET F SD  
15754 C  CE  . MET F 55   ? 1.7113 1.2924 1.5865 0.1518  0.0144  -0.0854 55   MET F CE  
15755 N  N   . THR F 56   ? 1.4805 1.1556 1.4137 0.1384  -0.0149 -0.1058 56   THR F N   
15756 C  CA  . THR F 56   ? 1.4748 1.1671 1.4073 0.1480  -0.0194 -0.1058 56   THR F CA  
15757 C  C   . THR F 56   ? 1.5080 1.1891 1.4262 0.1562  -0.0219 -0.1095 56   THR F C   
15758 O  O   . THR F 56   ? 1.4748 1.1623 1.3860 0.1671  -0.0234 -0.1082 56   THR F O   
15759 C  CB  . THR F 56   ? 1.3160 1.0323 1.2654 0.1425  -0.0237 -0.1077 56   THR F CB  
15760 O  OG1 . THR F 56   ? 1.2783 0.9902 1.2316 0.1350  -0.0264 -0.1134 56   THR F OG1 
15761 C  CG2 . THR F 56   ? 1.2861 1.0138 1.2490 0.1355  -0.0212 -0.1037 56   THR F CG2 
15762 N  N   . ILE F 57   ? 1.7286 1.3935 1.6422 0.1513  -0.0222 -0.1143 57   ILE F N   
15763 C  CA  . ILE F 57   ? 1.8123 1.4655 1.7119 0.1587  -0.0247 -0.1182 57   ILE F CA  
15764 C  C   . ILE F 57   ? 1.7910 1.4259 1.6725 0.1689  -0.0210 -0.1152 57   ILE F C   
15765 O  O   . ILE F 57   ? 1.7697 1.4080 1.6423 0.1803  -0.0230 -0.1152 57   ILE F O   
15766 C  CB  . ILE F 57   ? 1.8807 1.5202 1.7799 0.1502  -0.0260 -0.1243 57   ILE F CB  
15767 C  CG1 . ILE F 57   ? 1.8698 1.5291 1.7860 0.1420  -0.0307 -0.1278 57   ILE F CG1 
15768 C  CG2 . ILE F 57   ? 1.8956 1.5195 1.7780 0.1584  -0.0277 -0.1281 57   ILE F CG2 
15769 C  CD1 . ILE F 57   ? 1.8909 1.5553 1.8224 0.1294  -0.0285 -0.1268 57   ILE F CD1 
15770 N  N   . PRO F 58   ? 1.6399 1.2552 1.5149 0.1659  -0.0154 -0.1125 58   PRO F N   
15771 C  CA  . PRO F 58   ? 1.6730 1.2701 1.5291 0.1769  -0.0122 -0.1097 58   PRO F CA  
15772 C  C   . PRO F 58   ? 1.6231 1.2353 1.4788 0.1869  -0.0122 -0.1047 58   PRO F C   
15773 O  O   . PRO F 58   ? 1.6263 1.2344 1.4689 0.1991  -0.0129 -0.1041 58   PRO F O   
15774 C  CB  . PRO F 58   ? 1.7745 1.3486 1.6258 0.1696  -0.0059 -0.1079 58   PRO F CB  
15775 C  CG  . PRO F 58   ? 1.7276 1.3153 1.5980 0.1569  -0.0054 -0.1074 58   PRO F CG  
15776 C  CD  . PRO F 58   ? 1.7012 1.3085 1.5844 0.1531  -0.0116 -0.1122 58   PRO F CD  
15777 N  N   . LEU F 59   ? 1.1863 0.8157 1.0558 0.1822  -0.0115 -0.1011 59   LEU F N   
15778 C  CA  . LEU F 59   ? 1.1321 0.7761 1.0017 0.1910  -0.0116 -0.0965 59   LEU F CA  
15779 C  C   . LEU F 59   ? 1.0920 0.7561 0.9644 0.1988  -0.0169 -0.0985 59   LEU F C   
15780 O  O   . LEU F 59   ? 1.0811 0.7480 0.9446 0.2105  -0.0175 -0.0968 59   LEU F O   
15781 C  CB  . LEU F 59   ? 1.0675 0.7253 0.9517 0.1835  -0.0097 -0.0927 59   LEU F CB  
15782 C  CG  . LEU F 59   ? 1.0698 0.7100 0.9495 0.1792  -0.0035 -0.0889 59   LEU F CG  
15783 C  CD1 . LEU F 59   ? 1.0682 0.7246 0.9630 0.1724  -0.0022 -0.0853 59   LEU F CD1 
15784 C  CD2 . LEU F 59   ? 1.1871 0.8122 1.0485 0.1911  -0.0008 -0.0856 59   LEU F CD2 
15785 N  N   . GLY F 60   ? 1.1707 0.8492 1.0552 0.1926  -0.0208 -0.1021 60   GLY F N   
15786 C  CA  . GLY F 60   ? 1.1843 0.8807 1.0709 0.1995  -0.0254 -0.1042 60   GLY F CA  
15787 C  C   . GLY F 60   ? 1.1939 0.8771 1.0645 0.2092  -0.0267 -0.1071 60   GLY F C   
15788 O  O   . GLY F 60   ? 1.0392 0.7335 0.9063 0.2193  -0.0288 -0.1070 60   GLY F O   
15789 N  N   . CYS F 61   ? 1.7540 1.4133 1.6146 0.2063  -0.0252 -0.1099 61   CYS F N   
15790 C  CA  . CYS F 61   ? 1.7888 1.4330 1.6327 0.2158  -0.0260 -0.1127 61   CYS F CA  
15791 C  C   . CYS F 61   ? 1.7622 1.3986 1.5923 0.2281  -0.0234 -0.1089 61   CYS F C   
15792 O  O   . CYS F 61   ? 1.7844 1.4231 1.6055 0.2395  -0.0253 -0.1098 61   CYS F O   
15793 C  CB  . CYS F 61   ? 1.7074 1.3264 1.5436 0.2091  -0.0246 -0.1166 61   CYS F CB  
15794 S  SG  . CYS F 61   ? 1.8502 1.4759 1.6961 0.1999  -0.0295 -0.1234 61   CYS F SG  
15795 N  N   . LEU F 62   ? 1.5634 1.1906 1.3915 0.2262  -0.0191 -0.1045 62   LEU F N   
15796 C  CA  . LEU F 62   ? 1.6147 1.2347 1.4296 0.2381  -0.0168 -0.1006 62   LEU F CA  
15797 C  C   . LEU F 62   ? 1.6417 1.2880 1.4635 0.2461  -0.0196 -0.0985 62   LEU F C   
15798 O  O   . LEU F 62   ? 1.6115 1.2578 1.4226 0.2589  -0.0203 -0.0980 62   LEU F O   
15799 C  CB  . LEU F 62   ? 1.6044 1.2099 1.4166 0.2336  -0.0115 -0.0963 62   LEU F CB  
15800 C  CG  . LEU F 62   ? 1.6060 1.2039 1.4047 0.2454  -0.0090 -0.0919 62   LEU F CG  
15801 C  CD1 . LEU F 62   ? 1.6621 1.2373 1.4399 0.2558  -0.0082 -0.0935 62   LEU F CD1 
15802 C  CD2 . LEU F 62   ? 1.6605 1.2479 1.4593 0.2396  -0.0039 -0.0874 62   LEU F CD2 
15803 N  N   . GLY F 63   ? 1.8116 1.4803 1.6511 0.2389  -0.0210 -0.0974 63   GLY F N   
15804 C  CA  . GLY F 63   ? 1.7954 1.4893 1.6423 0.2454  -0.0234 -0.0956 63   GLY F CA  
15805 C  C   . GLY F 63   ? 1.7407 1.4464 1.5866 0.2526  -0.0273 -0.0991 63   GLY F C   
15806 O  O   . GLY F 63   ? 1.7226 1.4381 1.5645 0.2636  -0.0284 -0.0981 63   GLY F O   
15807 N  N   . PHE F 64   ? 1.3286 1.0338 1.1782 0.2468  -0.0295 -0.1034 64   PHE F N   
15808 C  CA  . PHE F 64   ? 1.3412 1.0565 1.1892 0.2535  -0.0330 -0.1069 64   PHE F CA  
15809 C  C   . PHE F 64   ? 1.4676 1.1654 1.2967 0.2654  -0.0325 -0.1083 64   PHE F C   
15810 O  O   . PHE F 64   ? 1.5359 1.2442 1.3618 0.2752  -0.0345 -0.1095 64   PHE F O   
15811 C  CB  . PHE F 64   ? 1.3074 1.0253 1.1631 0.2444  -0.0356 -0.1112 64   PHE F CB  
15812 C  CG  . PHE F 64   ? 1.3009 1.0446 1.1745 0.2382  -0.0378 -0.1108 64   PHE F CG  
15813 C  CD1 . PHE F 64   ? 1.3046 1.0691 1.1823 0.2448  -0.0401 -0.1111 64   PHE F CD1 
15814 C  CD2 . PHE F 64   ? 1.2981 1.0451 1.1840 0.2258  -0.0373 -0.1101 64   PHE F CD2 
15815 C  CE1 . PHE F 64   ? 1.2396 1.0266 1.1328 0.2392  -0.0417 -0.1105 64   PHE F CE1 
15816 C  CE2 . PHE F 64   ? 1.1657 0.9355 1.0671 0.2206  -0.0392 -0.1096 64   PHE F CE2 
15817 C  CZ  . PHE F 64   ? 1.2045 0.9938 1.1092 0.2272  -0.0414 -0.1098 64   PHE F CZ  
15818 N  N   . LEU F 65   ? 1.3038 0.9749 1.1204 0.2646  -0.0296 -0.1082 65   LEU F N   
15819 C  CA  . LEU F 65   ? 1.3538 1.0063 1.1510 0.2764  -0.0287 -0.1091 65   LEU F CA  
15820 C  C   . LEU F 65   ? 1.3879 1.0489 1.1802 0.2888  -0.0281 -0.1054 65   LEU F C   
15821 O  O   . LEU F 65   ? 1.4045 1.0675 1.1879 0.3008  -0.0295 -0.1066 65   LEU F O   
15822 C  CB  . LEU F 65   ? 1.3866 1.0081 1.1716 0.2722  -0.0250 -0.1091 65   LEU F CB  
15823 C  CG  . LEU F 65   ? 1.4040 1.0020 1.1671 0.2839  -0.0234 -0.1097 65   LEU F CG  
15824 C  CD1 . LEU F 65   ? 1.5515 1.1466 1.3084 0.2881  -0.0264 -0.1150 65   LEU F CD1 
15825 C  CD2 . LEU F 65   ? 1.3849 0.9531 1.1370 0.2790  -0.0188 -0.1085 65   LEU F CD2 
15826 N  N   . MET F 66   ? 1.5132 1.1795 1.3113 0.2862  -0.0261 -0.1010 66   MET F N   
15827 C  CA  . MET F 66   ? 1.5209 1.1960 1.3150 0.2975  -0.0259 -0.0976 66   MET F CA  
15828 C  C   . MET F 66   ? 1.3841 1.0899 1.1905 0.3014  -0.0293 -0.0981 66   MET F C   
15829 O  O   . MET F 66   ? 1.2870 1.0011 1.0882 0.3135  -0.0302 -0.0973 66   MET F O   
15830 C  CB  . MET F 66   ? 1.4063 1.0772 1.2025 0.2931  -0.0228 -0.0929 66   MET F CB  
15831 C  CG  . MET F 66   ? 1.4772 1.1184 1.2550 0.2973  -0.0188 -0.0910 66   MET F CG  
15832 S  SD  . MET F 66   ? 1.7518 1.3778 1.5336 0.2833  -0.0142 -0.0880 66   MET F SD  
15833 C  CE  . MET F 66   ? 1.4689 1.1218 1.2662 0.2816  -0.0149 -0.0838 66   MET F CE  
15834 N  N   . VAL F 67   ? 1.3343 1.0574 1.1570 0.2915  -0.0312 -0.0995 67   VAL F N   
15835 C  CA  . VAL F 67   ? 1.3573 1.1088 1.1917 0.2944  -0.0340 -0.1001 67   VAL F CA  
15836 C  C   . VAL F 67   ? 1.4420 1.1952 1.2692 0.3034  -0.0361 -0.1038 67   VAL F C   
15837 O  O   . VAL F 67   ? 1.5074 1.2763 1.3349 0.3131  -0.0373 -0.1037 67   VAL F O   
15838 C  CB  . VAL F 67   ? 1.2814 1.0489 1.1338 0.2815  -0.0351 -0.1003 67   VAL F CB  
15839 C  CG1 . VAL F 67   ? 1.1775 0.9696 1.0396 0.2838  -0.0379 -0.1023 67   VAL F CG1 
15840 C  CG2 . VAL F 67   ? 1.1627 0.9370 1.0241 0.2757  -0.0334 -0.0960 67   VAL F CG2 
15841 N  N   . GLN F 68   ? 1.3927 1.1299 1.2133 0.3004  -0.0364 -0.1074 68   GLN F N   
15842 C  CA  . GLN F 68   ? 1.4105 1.1474 1.2230 0.3091  -0.0382 -0.1111 68   GLN F CA  
15843 C  C   . GLN F 68   ? 1.4548 1.1802 1.2508 0.3218  -0.0370 -0.1099 68   GLN F C   
15844 O  O   . GLN F 68   ? 1.5462 1.2814 1.3389 0.3282  -0.0383 -0.1107 68   GLN F O   
15845 C  CB  . GLN F 68   ? 1.4333 1.1552 1.2425 0.3021  -0.0390 -0.1152 68   GLN F CB  
15846 C  CG  . GLN F 68   ? 1.4501 1.1406 1.2448 0.3005  -0.0368 -0.1158 68   GLN F CG  
15847 C  CD  . GLN F 68   ? 1.5524 1.2261 1.3284 0.3125  -0.0367 -0.1182 68   GLN F CD  
15848 O  OE1 . GLN F 68   ? 1.6355 1.3228 1.4106 0.3200  -0.0384 -0.1193 68   GLN F OE1 
15849 N  NE2 . GLN F 68   ? 1.5322 1.1774 1.2938 0.3125  -0.0342 -0.1184 68   GLN F NE2 
15850 N  N   . HIS F 69   ? 1.3329 1.0412 1.1201 0.3221  -0.0343 -0.1067 69   HIS F N   
15851 C  CA  . HIS F 69   ? 1.3767 1.0798 1.1506 0.3306  -0.0332 -0.1037 69   HIS F CA  
15852 C  C   . HIS F 69   ? 1.3894 1.1188 1.1707 0.3363  -0.0343 -0.1007 69   HIS F C   
15853 O  O   . HIS F 69   ? 1.3256 1.0617 1.1003 0.3444  -0.0350 -0.0999 69   HIS F O   
15854 C  CB  . HIS F 69   ? 1.4410 1.1185 1.2031 0.3292  -0.0298 -0.1009 69   HIS F CB  
15855 C  CG  . HIS F 69   ? 1.5339 1.1832 1.2817 0.3277  -0.0282 -0.1033 69   HIS F CG  
15856 N  ND1 . HIS F 69   ? 1.6243 1.2561 1.3733 0.3186  -0.0273 -0.1062 69   HIS F ND1 
15857 C  CD2 . HIS F 69   ? 1.4595 1.0950 1.1916 0.3340  -0.0275 -0.1034 69   HIS F CD2 
15858 C  CE1 . HIS F 69   ? 1.5447 1.1531 1.2794 0.3189  -0.0260 -0.1081 69   HIS F CE1 
15859 N  NE2 . HIS F 69   ? 1.4846 1.0946 1.2087 0.3283  -0.0261 -0.1064 69   HIS F NE2 
15860 N  N   . LEU F 70   ? 1.5353 1.2799 1.3304 0.3320  -0.0346 -0.0991 70   LEU F N   
15861 C  CA  . LEU F 70   ? 1.4950 1.2656 1.2985 0.3362  -0.0358 -0.0967 70   LEU F CA  
15862 C  C   . LEU F 70   ? 1.4349 1.2281 1.2468 0.3384  -0.0382 -0.0993 70   LEU F C   
15863 O  O   . LEU F 70   ? 1.4404 1.2478 1.2509 0.3452  -0.0391 -0.0984 70   LEU F O   
15864 C  CB  . LEU F 70   ? 1.4240 1.2040 1.2400 0.3304  -0.0354 -0.0945 70   LEU F CB  
15865 C  CG  . LEU F 70   ? 1.2915 1.0590 1.1003 0.3313  -0.0332 -0.0904 70   LEU F CG  
15866 C  CD1 . LEU F 70   ? 1.3331 1.1122 1.1553 0.3256  -0.0330 -0.0885 70   LEU F CD1 
15867 C  CD2 . LEU F 70   ? 1.2483 1.0211 1.0480 0.3407  -0.0336 -0.0879 70   LEU F CD2 
15868 N  N   . THR F 71   ? 1.6141 1.4109 1.4346 0.3325  -0.0392 -0.1026 71   THR F N   
15869 C  CA  . THR F 71   ? 1.6399 1.4561 1.4678 0.3338  -0.0411 -0.1052 71   THR F CA  
15870 C  C   . THR F 71   ? 1.6438 1.4436 1.4627 0.3338  -0.0415 -0.1091 71   THR F C   
15871 O  O   . THR F 71   ? 1.6429 1.4343 1.4653 0.3273  -0.0420 -0.1119 71   THR F O   
15872 C  CB  . THR F 71   ? 1.6193 1.4556 1.4653 0.3273  -0.0420 -0.1058 71   THR F CB  
15873 O  OG1 . THR F 71   ? 1.5915 1.4150 1.4401 0.3190  -0.0421 -0.1080 71   THR F OG1 
15874 C  CG2 . THR F 71   ? 1.5975 1.4456 1.4514 0.3261  -0.0414 -0.1020 71   THR F CG2 
15875 N  N   . GLY F 72   ? 2.1990 1.9940 2.0060 0.3412  -0.0415 -0.1094 72   GLY F N   
15876 C  CA  . GLY F 72   ? 2.3338 2.1124 2.1308 0.3417  -0.0419 -0.1131 72   GLY F CA  
15877 C  C   . GLY F 72   ? 2.3173 2.1111 2.1233 0.3397  -0.0437 -0.1166 72   GLY F C   
15878 O  O   . GLY F 72   ? 2.3821 2.2000 2.1969 0.3422  -0.0443 -0.1159 72   GLY F O   
15879 N  N   . GLY F 73   ? 1.7676 1.5468 1.5709 0.3350  -0.0445 -0.1205 73   GLY F N   
15880 C  CA  . GLY F 73   ? 1.8281 1.6186 1.6381 0.3330  -0.0464 -0.1241 73   GLY F CA  
15881 C  C   . GLY F 73   ? 1.8005 1.5691 1.5995 0.3317  -0.0474 -0.1286 73   GLY F C   
15882 O  O   . GLY F 73   ? 1.8035 1.5480 1.5904 0.3315  -0.0464 -0.1288 73   GLY F O   
15883 N  N   . ALA F 74   ? 1.7856 1.5626 1.5884 0.3306  -0.0492 -0.1322 74   ALA F N   
15884 C  CA  . ALA F 74   ? 1.8593 1.6169 1.6522 0.3291  -0.0507 -0.1370 74   ALA F CA  
15885 C  C   . ALA F 74   ? 1.8056 1.5482 1.6016 0.3175  -0.0513 -0.1384 74   ALA F C   
15886 O  O   . ALA F 74   ? 1.8887 1.6072 1.6734 0.3157  -0.0514 -0.1410 74   ALA F O   
15887 C  CB  . ALA F 74   ? 1.8364 1.6083 1.6329 0.3304  -0.0525 -0.1401 74   ALA F CB  
15888 N  N   . TRP F 75   ? 1.3178 1.0761 1.1302 0.3077  -0.0516 -0.1360 75   TRP F N   
15889 C  CA  . TRP F 75   ? 1.3689 1.1169 1.1868 0.2945  -0.0519 -0.1362 75   TRP F CA  
15890 C  C   . TRP F 75   ? 1.4082 1.1359 1.2185 0.2938  -0.0494 -0.1339 75   TRP F C   
15891 O  O   . TRP F 75   ? 1.4520 1.1626 1.2607 0.2850  -0.0492 -0.1353 75   TRP F O   
15892 C  CB  . TRP F 75   ? 1.4314 1.2016 1.2682 0.2853  -0.0525 -0.1337 75   TRP F CB  
15893 C  CG  . TRP F 75   ? 1.4242 1.2083 1.2680 0.2881  -0.0504 -0.1288 75   TRP F CG  
15894 C  CD1 . TRP F 75   ? 1.3723 1.1776 1.2210 0.2953  -0.0501 -0.1270 75   TRP F CD1 
15895 C  CD2 . TRP F 75   ? 1.3751 1.1528 1.2213 0.2836  -0.0483 -0.1251 75   TRP F CD2 
15896 N  NE1 . TRP F 75   ? 1.3273 1.1399 1.1816 0.2955  -0.0483 -0.1227 75   TRP F NE1 
15897 C  CE2 . TRP F 75   ? 1.2967 1.0925 1.1492 0.2887  -0.0472 -0.1213 75   TRP F CE2 
15898 C  CE3 . TRP F 75   ? 1.3605 1.1190 1.2043 0.2757  -0.0471 -0.1246 75   TRP F CE3 
15899 C  CZ2 . TRP F 75   ? 1.3031 1.0980 1.1588 0.2866  -0.0452 -0.1172 75   TRP F CZ2 
15900 C  CZ3 . TRP F 75   ? 1.2275 0.9849 1.0745 0.2736  -0.0447 -0.1203 75   TRP F CZ3 
15901 C  CH2 . TRP F 75   ? 1.3048 1.0802 1.1574 0.2792  -0.0439 -0.1166 75   TRP F CH2 
15902 N  N   . GLY F 76   ? 1.5530 1.2824 1.3585 0.3030  -0.0473 -0.1305 76   GLY F N   
15903 C  CA  . GLY F 76   ? 1.6629 1.3723 1.4598 0.3034  -0.0446 -0.1281 76   GLY F CA  
15904 C  C   . GLY F 76   ? 1.7018 1.3830 1.4796 0.3085  -0.0439 -0.1311 76   GLY F C   
15905 O  O   . GLY F 76   ? 1.6267 1.2862 1.3986 0.3026  -0.0422 -0.1311 76   GLY F O   
15906 N  N   . VAL F 77   ? 1.5024 1.1837 1.2704 0.3190  -0.0450 -0.1335 77   VAL F N   
15907 C  CA  . VAL F 77   ? 1.4470 1.1044 1.1978 0.3214  -0.0442 -0.1354 77   VAL F CA  
15908 C  C   . VAL F 77   ? 1.4370 1.0782 1.1859 0.3140  -0.0462 -0.1414 77   VAL F C   
15909 O  O   . VAL F 77   ? 1.4760 1.0919 1.2122 0.3120  -0.0452 -0.1433 77   VAL F O   
15910 C  CB  . VAL F 77   ? 1.4754 1.1425 1.2189 0.3313  -0.0446 -0.1347 77   VAL F CB  
15911 C  CG1 . VAL F 77   ? 1.5985 1.2406 1.3234 0.3346  -0.0436 -0.1360 77   VAL F CG1 
15912 C  CG2 . VAL F 77   ? 1.5253 1.2113 1.2728 0.3380  -0.0433 -0.1293 77   VAL F CG2 
15913 N  N   . THR F 78   ? 1.2845 0.9441 1.0480 0.3060  -0.0488 -0.1430 78   THR F N   
15914 C  CA  . THR F 78   ? 1.2884 0.9384 1.0528 0.2962  -0.0512 -0.1478 78   THR F CA  
15915 C  C   . THR F 78   ? 1.3688 1.0023 1.1356 0.2840  -0.0497 -0.1473 78   THR F C   
15916 O  O   . THR F 78   ? 1.3186 0.9312 1.0774 0.2792  -0.0502 -0.1514 78   THR F O   
15917 C  CB  . THR F 78   ? 1.1799 0.8547 0.9596 0.2909  -0.0542 -0.1490 78   THR F CB  
15918 O  OG1 . THR F 78   ? 1.2469 0.9363 1.0239 0.3021  -0.0550 -0.1494 78   THR F OG1 
15919 C  CG2 . THR F 78   ? 1.2840 0.9496 1.0642 0.2816  -0.0572 -0.1543 78   THR F CG2 
15920 N  N   . VAL F 79   ? 1.7085 1.3511 1.4863 0.2789  -0.0477 -0.1426 79   VAL F N   
15921 C  CA  . VAL F 79   ? 1.7134 1.3434 1.4957 0.2668  -0.0460 -0.1418 79   VAL F CA  
15922 C  C   . VAL F 79   ? 1.7143 1.3310 1.4890 0.2704  -0.0416 -0.1372 79   VAL F C   
15923 O  O   . VAL F 79   ? 1.7421 1.3555 1.5239 0.2615  -0.0395 -0.1347 79   VAL F O   
15924 C  CB  . VAL F 79   ? 1.6224 1.2738 1.4254 0.2553  -0.0475 -0.1407 79   VAL F CB  
15925 C  CG1 . VAL F 79   ? 1.6894 1.3511 1.4984 0.2514  -0.0518 -0.1455 79   VAL F CG1 
15926 C  CG2 . VAL F 79   ? 1.4968 1.1716 1.3097 0.2595  -0.0466 -0.1355 79   VAL F CG2 
15927 N  N   . ARG F 80   ? 1.5482 1.1571 1.3083 0.2839  -0.0403 -0.1361 80   ARG F N   
15928 C  CA  . ARG F 80   ? 1.5584 1.1542 1.3097 0.2887  -0.0363 -0.1317 80   ARG F CA  
15929 C  C   . ARG F 80   ? 1.6148 1.1810 1.3570 0.2813  -0.0334 -0.1326 80   ARG F C   
15930 O  O   . ARG F 80   ? 1.5958 1.1564 1.3413 0.2754  -0.0302 -0.1290 80   ARG F O   
15931 C  CB  . ARG F 80   ? 1.6300 1.2227 1.3664 0.3054  -0.0358 -0.1309 80   ARG F CB  
15932 C  CG  . ARG F 80   ? 1.6288 1.2089 1.3552 0.3088  -0.0317 -0.1255 80   ARG F CG  
15933 C  CD  . ARG F 80   ? 1.6518 1.2411 1.3699 0.3204  -0.0316 -0.1222 80   ARG F CD  
15934 N  NE  . ARG F 80   ? 1.6541 1.2744 1.3845 0.3251  -0.0341 -0.1212 80   ARG F NE  
15935 C  CZ  . ARG F 80   ? 1.6646 1.2993 1.3924 0.3343  -0.0342 -0.1179 80   ARG F CZ  
15936 N  NH1 . ARG F 80   ? 1.7104 1.3320 1.4234 0.3408  -0.0322 -0.1152 80   ARG F NH1 
15937 N  NH2 . ARG F 80   ? 1.6121 1.2752 1.3526 0.3370  -0.0364 -0.1175 80   ARG F NH2 
15938 N  N   . ARG F 81   ? 1.6677 1.2143 1.3982 0.2812  -0.0341 -0.1375 81   ARG F N   
15939 C  CA  . ARG F 81   ? 1.6572 1.1747 1.3787 0.2736  -0.0312 -0.1390 81   ARG F CA  
15940 C  C   . ARG F 81   ? 1.6145 1.1368 1.3526 0.2568  -0.0312 -0.1395 81   ARG F C   
15941 O  O   . ARG F 81   ? 1.5935 1.0982 1.3295 0.2495  -0.0274 -0.1381 81   ARG F O   
15942 C  CB  . ARG F 81   ? 1.6563 1.1533 1.3626 0.2768  -0.0325 -0.1447 81   ARG F CB  
15943 C  CG  . ARG F 81   ? 1.7842 1.2715 1.4728 0.2897  -0.0307 -0.1424 81   ARG F CG  
15944 C  CD  . ARG F 81   ? 1.7231 1.1879 1.4002 0.2888  -0.0252 -0.1382 81   ARG F CD  
15945 N  NE  . ARG F 81   ? 1.7886 1.2586 1.4566 0.3004  -0.0235 -0.1327 81   ARG F NE  
15946 C  CZ  . ARG F 81   ? 1.9334 1.3913 1.5857 0.3072  -0.0226 -0.1325 81   ARG F CZ  
15947 N  NH1 . ARG F 81   ? 1.9359 1.3756 1.5795 0.3038  -0.0231 -0.1374 81   ARG F NH1 
15948 N  NH2 . ARG F 81   ? 2.0338 1.4985 1.6790 0.3177  -0.0214 -0.1274 81   ARG F NH2 
15949 N  N   . MET F 82   ? 1.7892 1.3347 1.5435 0.2508  -0.0353 -0.1416 82   MET F N   
15950 C  CA  . MET F 82   ? 1.8328 1.3856 1.6040 0.2355  -0.0357 -0.1421 82   MET F CA  
15951 C  C   . MET F 82   ? 1.7659 1.3295 1.5474 0.2325  -0.0326 -0.1359 82   MET F C   
15952 O  O   . MET F 82   ? 1.6862 1.2438 1.4750 0.2212  -0.0303 -0.1350 82   MET F O   
15953 C  CB  . MET F 82   ? 1.7951 1.3704 1.5798 0.2314  -0.0410 -0.1456 82   MET F CB  
15954 C  CG  . MET F 82   ? 1.8788 1.4433 1.6543 0.2326  -0.0443 -0.1523 82   MET F CG  
15955 S  SD  . MET F 82   ? 2.0592 1.6508 1.8489 0.2299  -0.0504 -0.1559 82   MET F SD  
15956 C  CE  . MET F 82   ? 1.8389 1.4367 1.6476 0.2119  -0.0511 -0.1568 82   MET F CE  
15957 N  N   . LEU F 83   ? 1.6911 1.2707 1.4734 0.2425  -0.0325 -0.1317 83   LEU F N   
15958 C  CA  . LEU F 83   ? 1.6623 1.2514 1.4528 0.2408  -0.0297 -0.1259 83   LEU F CA  
15959 C  C   . LEU F 83   ? 1.6936 1.2571 1.4707 0.2422  -0.0245 -0.1229 83   LEU F C   
15960 O  O   . LEU F 83   ? 1.6385 1.2006 1.4223 0.2349  -0.0213 -0.1195 83   LEU F O   
15961 C  CB  . LEU F 83   ? 1.6066 1.2188 1.4005 0.2515  -0.0312 -0.1228 83   LEU F CB  
15962 C  CG  . LEU F 83   ? 1.4661 1.1073 1.2763 0.2488  -0.0353 -0.1240 83   LEU F CG  
15963 C  CD1 . LEU F 83   ? 1.4615 1.1211 1.2709 0.2612  -0.0366 -0.1220 83   LEU F CD1 
15964 C  CD2 . LEU F 83   ? 1.4201 1.0753 1.2484 0.2367  -0.0349 -0.1217 83   LEU F CD2 
15965 N  N   . GLU F 84   ? 1.6879 1.2303 1.4455 0.2520  -0.0233 -0.1241 84   GLU F N   
15966 C  CA  . GLU F 84   ? 1.6841 1.1995 1.4269 0.2538  -0.0180 -0.1214 84   GLU F CA  
15967 C  C   . GLU F 84   ? 1.6846 1.1807 1.4290 0.2397  -0.0154 -0.1236 84   GLU F C   
15968 O  O   . GLU F 84   ? 1.6453 1.1283 1.3877 0.2351  -0.0106 -0.1202 84   GLU F O   
15969 C  CB  . GLU F 84   ? 1.6268 1.1238 1.3478 0.2677  -0.0175 -0.1226 84   GLU F CB  
15970 C  CG  . GLU F 84   ? 1.6334 1.1476 1.3516 0.2827  -0.0193 -0.1200 84   GLU F CG  
15971 C  CD  . GLU F 84   ? 1.7031 1.2082 1.4050 0.2933  -0.0199 -0.1213 84   GLU F CD  
15972 O  OE1 . GLU F 84   ? 1.7270 1.2087 1.4175 0.2901  -0.0186 -0.1242 84   GLU F OE1 
15973 O  OE2 . GLU F 84   ? 1.7432 1.2672 1.4452 0.3030  -0.0216 -0.1189 84   GLU F OE2 
15974 N  N   . ALA F 85   ? 1.8236 1.3179 1.5715 0.2326  -0.0185 -0.1295 85   ALA F N   
15975 C  CA  . ALA F 85   ? 1.8497 1.3274 1.6005 0.2185  -0.0164 -0.1323 85   ALA F CA  
15976 C  C   . ALA F 85   ? 1.8232 1.3172 1.5943 0.2061  -0.0156 -0.1300 85   ALA F C   
15977 O  O   . ALA F 85   ? 1.8355 1.3150 1.6079 0.1965  -0.0113 -0.1290 85   ALA F O   
15978 C  CB  . ALA F 85   ? 1.9088 1.3829 1.6592 0.2145  -0.0207 -0.1396 85   ALA F CB  
15979 N  N   . GLY F 86   ? 1.4458 0.9697 1.2327 0.2061  -0.0194 -0.1290 86   GLY F N   
15980 C  CA  . GLY F 86   ? 1.4035 0.9437 1.2093 0.1952  -0.0187 -0.1265 86   GLY F CA  
15981 C  C   . GLY F 86   ? 1.3787 0.9162 1.1829 0.1974  -0.0136 -0.1198 86   GLY F C   
15982 O  O   . GLY F 86   ? 1.3627 0.8993 1.1762 0.1872  -0.0104 -0.1178 86   GLY F O   
15983 N  N   . ALA F 87   ? 1.8479 1.3843 1.6402 0.2110  -0.0128 -0.1164 87   ALA F N   
15984 C  CA  . ALA F 87   ? 1.8548 1.3885 1.6439 0.2145  -0.0084 -0.1102 87   ALA F CA  
15985 C  C   . ALA F 87   ? 1.8887 1.3905 1.6628 0.2130  -0.0023 -0.1088 87   ALA F C   
15986 O  O   . ALA F 87   ? 1.8545 1.3517 1.6283 0.2115  0.0021  -0.1039 87   ALA F O   
15987 C  CB  . ALA F 87   ? 1.7418 1.2864 1.5237 0.2299  -0.0100 -0.1074 87   ALA F CB  
15988 N  N   . ALA F 88   ? 1.6332 1.1122 1.3941 0.2133  -0.0019 -0.1130 88   ALA F N   
15989 C  CA  . ALA F 88   ? 1.6205 1.0672 1.3658 0.2117  0.0042  -0.1119 88   ALA F CA  
15990 C  C   . ALA F 88   ? 1.7477 1.1872 1.5037 0.1954  0.0079  -0.1123 88   ALA F C   
15991 O  O   . ALA F 88   ? 1.8079 1.2211 1.5526 0.1925  0.0139  -0.1109 88   ALA F O   
15992 C  CB  . ALA F 88   ? 1.6710 1.0952 1.3987 0.2170  0.0035  -0.1166 88   ALA F CB  
15993 N  N   . THR F 89   ? 1.7466 1.2083 1.5236 0.1848  0.0048  -0.1141 89   THR F N   
15994 C  CA  . THR F 89   ? 1.7157 1.1741 1.5051 0.1692  0.0080  -0.1147 89   THR F CA  
15995 C  C   . THR F 89   ? 1.6462 1.1130 1.4437 0.1666  0.0121  -0.1083 89   THR F C   
15996 O  O   . THR F 89   ? 1.5599 1.0253 1.3683 0.1539  0.0154  -0.1081 89   THR F O   
15997 C  CB  . THR F 89   ? 1.6686 1.1471 1.4768 0.1592  0.0025  -0.1199 89   THR F CB  
15998 O  OG1 . THR F 89   ? 1.6090 1.1184 1.4320 0.1615  -0.0013 -0.1175 89   THR F OG1 
15999 C  CG2 . THR F 89   ? 1.6887 1.1615 1.4889 0.1630  -0.0023 -0.1262 89   THR F CG2 
16000 N  N   . LEU F 90   ? 1.5903 1.0659 1.3827 0.1782  0.0121  -0.1034 90   LEU F N   
16001 C  CA  . LEU F 90   ? 1.5360 1.0210 1.3360 0.1764  0.0155  -0.0975 90   LEU F CA  
16002 C  C   . LEU F 90   ? 1.5739 1.0333 1.3652 0.1713  0.0235  -0.0942 90   LEU F C   
16003 O  O   . LEU F 90   ? 1.6135 1.0798 1.4172 0.1622  0.0266  -0.0916 90   LEU F O   
16004 C  CB  . LEU F 90   ? 1.5254 1.0238 1.3200 0.1907  0.0135  -0.0934 90   LEU F CB  
16005 C  CG  . LEU F 90   ? 1.4441 0.9755 1.2543 0.1926  0.0070  -0.0944 90   LEU F CG  
16006 C  CD1 . LEU F 90   ? 1.4073 0.9478 1.2088 0.2080  0.0048  -0.0918 90   LEU F CD1 
16007 C  CD2 . LEU F 90   ? 1.2124 0.7633 1.0424 0.1825  0.0075  -0.0921 90   LEU F CD2 
16008 N  N   . PRO F 91   ? 1.8847 1.3147 1.6551 0.1768  0.0275  -0.0940 91   PRO F N   
16009 C  CA  . PRO F 91   ? 1.9226 1.3280 1.6851 0.1712  0.0357  -0.0907 91   PRO F CA  
16010 C  C   . PRO F 91   ? 1.9735 1.3753 1.7497 0.1538  0.0384  -0.0936 91   PRO F C   
16011 O  O   . PRO F 91   ? 1.9254 1.3218 1.7057 0.1465  0.0444  -0.0900 91   PRO F O   
16012 C  CB  . PRO F 91   ? 1.8407 1.2152 1.5779 0.1806  0.0384  -0.0912 91   PRO F CB  
16013 C  CG  . PRO F 91   ? 1.8909 1.2728 1.6259 0.1868  0.0315  -0.0964 91   PRO F CG  
16014 C  CD  . PRO F 91   ? 1.9113 1.3284 1.6630 0.1896  0.0253  -0.0960 91   PRO F CD  
16015 N  N   . ILE F 92   ? 1.7401 1.1449 1.5235 0.1469  0.0342  -0.1002 92   ILE F N   
16016 C  CA  . ILE F 92   ? 1.7299 1.1343 1.5281 0.1301  0.0360  -0.1036 92   ILE F CA  
16017 C  C   . ILE F 92   ? 1.6933 1.1262 1.5142 0.1229  0.0346  -0.1015 92   ILE F C   
16018 O  O   . ILE F 92   ? 1.7022 1.1336 1.5342 0.1105  0.0389  -0.1011 92   ILE F O   
16019 C  CB  . ILE F 92   ? 1.7161 1.1192 1.5167 0.1254  0.0308  -0.1115 92   ILE F CB  
16020 C  CG1 . ILE F 92   ? 1.6596 1.0364 1.4366 0.1350  0.0313  -0.1134 92   ILE F CG1 
16021 C  CG2 . ILE F 92   ? 1.6981 1.0959 1.5115 0.1082  0.0333  -0.1155 92   ILE F CG2 
16022 C  CD1 . ILE F 92   ? 1.5586 0.9009 1.3202 0.1313  0.0398  -0.1121 92   ILE F CD1 
16023 N  N   . MET F 93   ? 1.9534 1.4124 1.7816 0.1304  0.0289  -0.1002 93   MET F N   
16024 C  CA  . MET F 93   ? 1.9351 1.4210 1.7838 0.1246  0.0276  -0.0980 93   MET F CA  
16025 C  C   . MET F 93   ? 1.8957 1.3760 1.7427 0.1242  0.0345  -0.0912 93   MET F C   
16026 O  O   . MET F 93   ? 1.7728 1.2652 1.6358 0.1146  0.0364  -0.0898 93   MET F O   
16027 C  CB  . MET F 93   ? 1.8360 1.3487 1.6905 0.1337  0.0205  -0.0978 93   MET F CB  
16028 C  CG  . MET F 93   ? 1.7991 1.3203 1.6568 0.1340  0.0135  -0.1043 93   MET F CG  
16029 S  SD  . MET F 93   ? 1.8596 1.3889 1.7370 0.1169  0.0114  -0.1103 93   MET F SD  
16030 C  CE  . MET F 93   ? 1.9502 1.4512 1.8123 0.1157  0.0115  -0.1166 93   MET F CE  
16031 N  N   . GLY F 94   ? 1.9660 1.4281 1.7935 0.1348  0.0382  -0.0871 94   GLY F N   
16032 C  CA  . GLY F 94   ? 1.8929 1.3477 1.7167 0.1351  0.0449  -0.0807 94   GLY F CA  
16033 C  C   . GLY F 94   ? 1.9341 1.3710 1.7606 0.1219  0.0523  -0.0806 94   GLY F C   
16034 O  O   . GLY F 94   ? 1.9197 1.3624 1.7555 0.1158  0.0565  -0.0768 94   GLY F O   
16035 N  N   . LEU F 95   ? 1.8618 1.2767 1.6804 0.1171  0.0542  -0.0849 95   LEU F N   
16036 C  CA  . LEU F 95   ? 1.8815 1.2809 1.7049 0.1029  0.0608  -0.0858 95   LEU F CA  
16037 C  C   . LEU F 95   ? 1.8515 1.2752 1.7010 0.0895  0.0583  -0.0887 95   LEU F C   
16038 O  O   . LEU F 95   ? 1.8962 1.3174 1.7549 0.0788  0.0641  -0.0871 95   LEU F O   
16039 C  CB  . LEU F 95   ? 1.8854 1.2577 1.6957 0.1003  0.0624  -0.0907 95   LEU F CB  
16040 C  CG  . LEU F 95   ? 1.8855 1.2413 1.7013 0.0846  0.0689  -0.0931 95   LEU F CG  
16041 C  CD1 . LEU F 95   ? 1.8943 1.2315 1.7015 0.0833  0.0789  -0.0866 95   LEU F CD1 
16042 C  CD2 . LEU F 95   ? 1.8823 1.2148 1.6865 0.0822  0.0686  -0.0991 95   LEU F CD2 
16043 N  N   . LEU F 96   ? 1.6639 1.1112 1.5252 0.0903  0.0498  -0.0929 96   LEU F N   
16044 C  CA  . LEU F 96   ? 1.6050 1.0765 1.4906 0.0788  0.0466  -0.0958 96   LEU F CA  
16045 C  C   . LEU F 96   ? 1.6465 1.1378 1.5441 0.0785  0.0482  -0.0902 96   LEU F C   
16046 O  O   . LEU F 96   ? 1.6282 1.1364 1.5453 0.0682  0.0476  -0.0915 96   LEU F O   
16047 C  CB  . LEU F 96   ? 1.5597 1.0507 1.4529 0.0812  0.0371  -0.1013 96   LEU F CB  
16048 C  CG  . LEU F 96   ? 1.5589 1.0341 1.4443 0.0791  0.0346  -0.1081 96   LEU F CG  
16049 C  CD1 . LEU F 96   ? 1.5006 0.9979 1.3963 0.0801  0.0253  -0.1135 96   LEU F CD1 
16050 C  CD2 . LEU F 96   ? 1.5655 1.0246 1.4559 0.0646  0.0398  -0.1113 96   LEU F CD2 
16051 N  N   . PHE F 97   ? 1.8432 1.3327 1.7293 0.0898  0.0500  -0.0842 97   PHE F N   
16052 C  CA  . PHE F 97   ? 1.8147 1.3198 1.7098 0.0900  0.0521  -0.0787 97   PHE F CA  
16053 C  C   . PHE F 97   ? 1.7881 1.2774 1.6827 0.0820  0.0615  -0.0749 97   PHE F C   
16054 O  O   . PHE F 97   ? 1.7483 1.2510 1.6535 0.0791  0.0637  -0.0711 97   PHE F O   
16055 C  CB  . PHE F 97   ? 1.7511 1.2605 1.6339 0.1052  0.0502  -0.0741 97   PHE F CB  
16056 C  CG  . PHE F 97   ? 1.7398 1.2658 1.6309 0.1063  0.0516  -0.0686 97   PHE F CG  
16057 C  CD1 . PHE F 97   ? 1.7300 1.2854 1.6392 0.1041  0.0462  -0.0694 97   PHE F CD1 
16058 C  CD2 . PHE F 97   ? 1.7000 1.2112 1.5799 0.1098  0.0586  -0.0627 97   PHE F CD2 
16059 C  CE1 . PHE F 97   ? 1.6645 1.2345 1.5809 0.1051  0.0476  -0.0646 97   PHE F CE1 
16060 C  CE2 . PHE F 97   ? 1.6297 1.1558 1.5168 0.1108  0.0598  -0.0579 97   PHE F CE2 
16061 C  CZ  . PHE F 97   ? 1.5612 1.1167 1.4666 0.1084  0.0543  -0.0589 97   PHE F CZ  
16062 N  N   . ILE F 98   ? 1.3686 0.8294 1.2509 0.0783  0.0672  -0.0760 98   ILE F N   
16063 C  CA  . ILE F 98   ? 1.4079 0.8513 1.2882 0.0708  0.0770  -0.0723 98   ILE F CA  
16064 C  C   . ILE F 98   ? 1.4161 0.8770 1.3201 0.0569  0.0784  -0.0734 98   ILE F C   
16065 O  O   . ILE F 98   ? 1.4195 0.8812 1.3267 0.0544  0.0844  -0.0682 98   ILE F O   
16066 C  CB  . ILE F 98   ? 1.4129 0.8230 1.2768 0.0683  0.0825  -0.0742 98   ILE F CB  
16067 C  CG1 . ILE F 98   ? 1.5074 0.8982 1.3458 0.0836  0.0830  -0.0712 98   ILE F CG1 
16068 C  CG2 . ILE F 98   ? 1.4179 0.8119 1.2837 0.0573  0.0927  -0.0716 98   ILE F CG2 
16069 C  CD1 . ILE F 98   ? 1.5469 0.9388 1.3769 0.0932  0.0862  -0.0636 98   ILE F CD1 
16070 N  N   . PRO F 99   ? 1.6459 1.1211 1.5666 0.0477  0.0734  -0.0797 99   PRO F N   
16071 C  CA  . PRO F 99   ? 1.6776 1.1711 1.6212 0.0353  0.0746  -0.0804 99   PRO F CA  
16072 C  C   . PRO F 99   ? 1.6523 1.1702 1.6059 0.0394  0.0729  -0.0757 99   PRO F C   
16073 O  O   . PRO F 99   ? 1.6242 1.1471 1.5883 0.0323  0.0782  -0.0727 99   PRO F O   
16074 C  CB  . PRO F 99   ? 1.6507 1.1574 1.6079 0.0284  0.0672  -0.0884 99   PRO F CB  
16075 C  CG  . PRO F 99   ? 1.5556 1.0389 1.4957 0.0317  0.0665  -0.0921 99   PRO F CG  
16076 C  CD  . PRO F 99   ? 1.5940 1.0652 1.5126 0.0468  0.0676  -0.0868 99   PRO F CD  
16077 N  N   . ILE F 100  ? 1.6125 1.1456 1.5633 0.0504  0.0658  -0.0750 100  ILE F N   
16078 C  CA  . ILE F 100  ? 1.5090 1.0650 1.4689 0.0543  0.0640  -0.0708 100  ILE F CA  
16079 C  C   . ILE F 100  ? 1.5294 1.0730 1.4781 0.0590  0.0715  -0.0636 100  ILE F C   
16080 O  O   . ILE F 100  ? 1.5643 1.1196 1.5231 0.0558  0.0743  -0.0599 100  ILE F O   
16081 C  CB  . ILE F 100  ? 1.4780 1.0514 1.4363 0.0652  0.0551  -0.0719 100  ILE F CB  
16082 C  CG1 . ILE F 100  ? 1.5019 1.0866 1.4703 0.0607  0.0479  -0.0791 100  ILE F CG1 
16083 C  CG2 . ILE F 100  ? 1.4476 1.0444 1.4154 0.0686  0.0533  -0.0678 100  ILE F CG2 
16084 C  CD1 . ILE F 100  ? 1.4142 1.0165 1.3819 0.0706  0.0395  -0.0803 100  ILE F CD1 
16085 N  N   . ALA F 101  ? 1.7188 1.2379 1.6458 0.0671  0.0748  -0.0614 101  ALA F N   
16086 C  CA  . ALA F 101  ? 1.6978 1.2028 1.6120 0.0722  0.0821  -0.0546 101  ALA F CA  
16087 C  C   . ALA F 101  ? 1.6949 1.1884 1.6148 0.0603  0.0912  -0.0528 101  ALA F C   
16088 O  O   . ALA F 101  ? 1.6458 1.1405 1.5661 0.0607  0.0964  -0.0474 101  ALA F O   
16089 C  CB  . ALA F 101  ? 1.7130 1.1930 1.6021 0.0835  0.0835  -0.0531 101  ALA F CB  
16090 N  N   . LEU F 102  ? 1.4480 0.9304 1.3725 0.0496  0.0935  -0.0575 102  LEU F N   
16091 C  CA  . LEU F 102  ? 1.4602 0.9339 1.3928 0.0369  0.1022  -0.0565 102  LEU F CA  
16092 C  C   . LEU F 102  ? 1.4110 0.9118 1.3664 0.0298  0.1013  -0.0558 102  LEU F C   
16093 O  O   . LEU F 102  ? 1.4874 0.9843 1.4481 0.0228  0.1091  -0.0525 102  LEU F O   
16094 C  CB  . LEU F 102  ? 1.4129 0.8730 1.3484 0.0262  0.1034  -0.0627 102  LEU F CB  
16095 C  CG  . LEU F 102  ? 1.3912 0.8193 1.3036 0.0308  0.1067  -0.0634 102  LEU F CG  
16096 C  CD1 . LEU F 102  ? 1.3127 0.7308 1.2309 0.0190  0.1070  -0.0703 102  LEU F CD1 
16097 C  CD2 . LEU F 102  ? 1.5462 0.9494 1.4419 0.0336  0.1171  -0.0567 102  LEU F CD2 
16098 N  N   . GLY F 103  ? 1.7931 1.3207 1.7616 0.0317  0.0922  -0.0586 103  GLY F N   
16099 C  CA  . GLY F 103  ? 1.8411 1.3946 1.8310 0.0254  0.0910  -0.0582 103  GLY F CA  
16100 C  C   . GLY F 103  ? 1.8035 1.3624 1.7903 0.0315  0.0944  -0.0511 103  GLY F C   
16101 O  O   . GLY F 103  ? 1.8421 1.4070 1.8401 0.0244  0.0996  -0.0487 103  GLY F O   
16102 N  N   . TYR F 104  ? 1.5066 1.0637 1.4785 0.0448  0.0915  -0.0479 104  TYR F N   
16103 C  CA  . TYR F 104  ? 1.4435 1.0073 1.4122 0.0515  0.0936  -0.0417 104  TYR F CA  
16104 C  C   . TYR F 104  ? 1.5027 1.0403 1.4529 0.0552  0.1027  -0.0361 104  TYR F C   
16105 O  O   . TYR F 104  ? 1.4357 0.9755 1.3794 0.0623  0.1044  -0.0308 104  TYR F O   
16106 C  CB  . TYR F 104  ? 1.4577 1.0369 1.4220 0.0637  0.0852  -0.0413 104  TYR F CB  
16107 C  CG  . TYR F 104  ? 1.4141 0.9785 1.3588 0.0746  0.0822  -0.0422 104  TYR F CG  
16108 C  CD1 . TYR F 104  ? 1.4036 0.9444 1.3273 0.0823  0.0876  -0.0379 104  TYR F CD1 
16109 C  CD2 . TYR F 104  ? 1.4969 1.0716 1.4439 0.0778  0.0738  -0.0471 104  TYR F CD2 
16110 C  CE1 . TYR F 104  ? 1.5079 1.0358 1.4137 0.0928  0.0847  -0.0386 104  TYR F CE1 
16111 C  CE2 . TYR F 104  ? 1.5136 1.0756 1.4430 0.0882  0.0711  -0.0479 104  TYR F CE2 
16112 C  CZ  . TYR F 104  ? 1.5269 1.0658 1.4360 0.0957  0.0765  -0.0437 104  TYR F CZ  
16113 O  OH  . TYR F 104  ? 1.5287 1.0553 1.4203 0.1065  0.0738  -0.0445 104  TYR F OH  
16114 N  N   . PHE F 105  ? 1.6472 1.1597 1.5882 0.0505  0.1086  -0.0372 105  PHE F N   
16115 C  CA  . PHE F 105  ? 1.6568 1.1430 1.5807 0.0525  0.1183  -0.0319 105  PHE F CA  
16116 C  C   . PHE F 105  ? 1.7027 1.1863 1.6389 0.0394  0.1269  -0.0307 105  PHE F C   
16117 O  O   . PHE F 105  ? 1.7753 1.2793 1.7333 0.0297  0.1249  -0.0337 105  PHE F O   
16118 C  CB  . PHE F 105  ? 1.6397 1.0977 1.5437 0.0564  0.1201  -0.0334 105  PHE F CB  
16119 C  CG  . PHE F 105  ? 1.5483 0.9979 1.4311 0.0725  0.1171  -0.0304 105  PHE F CG  
16120 C  CD1 . PHE F 105  ? 1.4924 0.9338 1.3620 0.0807  0.1217  -0.0238 105  PHE F CD1 
16121 C  CD2 . PHE F 105  ? 1.4780 0.9283 1.3542 0.0797  0.1095  -0.0344 105  PHE F CD2 
16122 C  CE1 . PHE F 105  ? 1.3998 0.8346 1.2504 0.0957  0.1186  -0.0214 105  PHE F CE1 
16123 C  CE2 . PHE F 105  ? 1.4959 0.9396 1.3532 0.0946  0.1067  -0.0318 105  PHE F CE2 
16124 C  CZ  . PHE F 105  ? 1.4909 0.9272 1.3357 0.1027  0.1111  -0.0254 105  PHE F CZ  
16125 N  N   . ASP F 106  ? 1.4281 0.8863 1.3501 0.0390  0.1369  -0.0262 106  ASP F N   
16126 C  CA  . ASP F 106  ? 1.5521 1.0056 1.4843 0.0267  0.1463  -0.0248 106  ASP F CA  
16127 C  C   . ASP F 106  ? 1.6211 1.0698 1.5649 0.0130  0.1479  -0.0309 106  ASP F C   
16128 O  O   . ASP F 106  ? 1.6059 1.0515 1.5601 0.0015  0.1556  -0.0305 106  ASP F O   
16129 C  CB  . ASP F 106  ? 1.6602 1.0860 1.5723 0.0305  0.1569  -0.0182 106  ASP F CB  
16130 C  CG  . ASP F 106  ? 1.7070 1.1383 1.6287 0.0242  0.1647  -0.0138 106  ASP F CG  
16131 O  OD1 . ASP F 106  ? 1.7085 1.1659 1.6525 0.0175  0.1615  -0.0157 106  ASP F OD1 
16132 O  OD2 . ASP F 106  ? 1.7274 1.1366 1.6339 0.0263  0.1742  -0.0084 106  ASP F OD2 
16133 N  N   . THR F 107  ? 1.8787 1.3271 1.8213 0.0139  0.1407  -0.0366 107  THR F N   
16134 C  CA  . THR F 107  ? 1.8764 1.3221 1.8308 0.0009  0.1411  -0.0432 107  THR F CA  
16135 C  C   . THR F 107  ? 1.9286 1.4032 1.9111 -0.0099 0.1379  -0.0467 107  THR F C   
16136 O  O   . THR F 107  ? 2.0048 1.4787 2.0001 -0.0226 0.1399  -0.0515 107  THR F O   
16137 C  CB  . THR F 107  ? 1.8478 1.2881 1.7939 0.0056  0.1334  -0.0486 107  THR F CB  
16138 O  OG1 . THR F 107  ? 1.7693 1.1901 1.6900 0.0194  0.1339  -0.0447 107  THR F OG1 
16139 C  CG2 . THR F 107  ? 1.9032 1.3272 1.8518 -0.0062 0.1367  -0.0542 107  THR F CG2 
16140 N  N   . TYR F 108  ? 2.5545 2.0544 2.5469 -0.0051 0.1330  -0.0445 108  TYR F N   
16141 C  CA  . TYR F 108  ? 2.5605 2.0871 2.5785 -0.0145 0.1308  -0.0469 108  TYR F CA  
16142 C  C   . TYR F 108  ? 2.6878 2.2074 2.7135 -0.0252 0.1419  -0.0443 108  TYR F C   
16143 O  O   . TYR F 108  ? 2.6934 2.1888 2.7038 -0.0240 0.1511  -0.0396 108  TYR F O   
16144 C  CB  . TYR F 108  ? 2.5045 2.0569 2.5286 -0.0060 0.1239  -0.0445 108  TYR F CB  
16145 C  CG  . TYR F 108  ? 2.6121 2.1675 2.6351 -0.0031 0.1299  -0.0375 108  TYR F CG  
16146 C  CD1 . TYR F 108  ? 2.5383 2.1076 2.5798 -0.0124 0.1342  -0.0367 108  TYR F CD1 
16147 C  CD2 . TYR F 108  ? 2.5749 2.1195 2.5782 0.0093  0.1312  -0.0318 108  TYR F CD2 
16148 C  CE1 . TYR F 108  ? 2.4507 2.0223 2.4904 -0.0094 0.1397  -0.0303 108  TYR F CE1 
16149 C  CE2 . TYR F 108  ? 2.4458 1.9927 2.4473 0.0123  0.1364  -0.0256 108  TYR F CE2 
16150 C  CZ  . TYR F 108  ? 2.4868 2.0468 2.5063 0.0029  0.1407  -0.0248 108  TYR F CZ  
16151 O  OH  . TYR F 108  ? 2.6060 2.1679 2.6232 0.0060  0.1460  -0.0186 108  TYR F OH  
16152 N  N   . LYS F 109  ? 2.3926 1.9338 2.4424 -0.0357 0.1409  -0.0475 109  LYS F N   
16153 C  CA  . LYS F 109  ? 2.4007 1.9391 2.4634 -0.0489 0.1502  -0.0474 109  LYS F CA  
16154 C  C   . LYS F 109  ? 2.3998 1.9207 2.4624 -0.0590 0.1529  -0.0531 109  LYS F C   
16155 O  O   . LYS F 109  ? 2.4188 1.9430 2.4976 -0.0721 0.1578  -0.0560 109  LYS F O   
16156 C  CB  . LYS F 109  ? 2.3106 1.8337 2.3620 -0.0464 0.1611  -0.0395 109  LYS F CB  
16157 C  CG  . LYS F 109  ? 2.2455 1.7897 2.3046 -0.0416 0.1603  -0.0348 109  LYS F CG  
16158 C  CD  . LYS F 109  ? 2.2225 1.7488 2.2650 -0.0359 0.1698  -0.0267 109  LYS F CD  
16159 C  CE  . LYS F 109  ? 2.2514 1.7593 2.2952 -0.0470 0.1825  -0.0253 109  LYS F CE  
16160 N  NZ  . LYS F 109  ? 2.2991 1.7878 2.3249 -0.0409 0.1921  -0.0173 109  LYS F NZ  
16161 N  N   . ALA F 110  ? 1.7645 1.2669 1.8091 -0.0529 0.1499  -0.0548 110  ALA F N   
16162 C  CA  . ALA F 110  ? 1.7328 1.2229 1.7778 -0.0607 0.1489  -0.0616 110  ALA F CA  
16163 C  C   . ALA F 110  ? 1.7120 1.2201 1.7629 -0.0568 0.1359  -0.0677 110  ALA F C   
16164 O  O   . ALA F 110  ? 1.6853 1.2131 1.7383 -0.0477 0.1285  -0.0661 110  ALA F O   
16165 C  CB  . ALA F 110  ? 1.7274 1.1814 1.7466 -0.0567 0.1554  -0.0594 110  ALA F CB  
16166 N  N   . LEU F 111  ? 1.7275 1.2286 1.7811 -0.0639 0.1332  -0.0748 111  LEU F N   
16167 C  CA  . LEU F 111  ? 1.7633 1.2793 1.8226 -0.0618 0.1214  -0.0814 111  LEU F CA  
16168 C  C   . LEU F 111  ? 1.8006 1.3513 1.8849 -0.0660 0.1145  -0.0844 111  LEU F C   
16169 O  O   . LEU F 111  ? 1.8225 1.3887 1.9124 -0.0634 0.1043  -0.0894 111  LEU F O   
16170 C  CB  . LEU F 111  ? 1.6965 1.2078 1.7362 -0.0460 0.1152  -0.0792 111  LEU F CB  
16171 C  CG  . LEU F 111  ? 1.6447 1.1259 1.6611 -0.0410 0.1166  -0.0802 111  LEU F CG  
16172 C  CD1 . LEU F 111  ? 1.6700 1.1219 1.6704 -0.0417 0.1287  -0.0746 111  LEU F CD1 
16173 C  CD2 . LEU F 111  ? 1.5363 1.0205 1.5381 -0.0255 0.1087  -0.0788 111  LEU F CD2 
16174 N  N   . GLY F 112  ? 2.1044 1.6675 2.2033 -0.0719 0.1199  -0.0813 112  GLY F N   
16175 C  CA  . GLY F 112  ? 2.0415 1.6365 2.1642 -0.0763 0.1142  -0.0839 112  GLY F CA  
16176 C  C   . GLY F 112  ? 2.0069 1.6221 2.1309 -0.0658 0.1097  -0.0791 112  GLY F C   
16177 O  O   . GLY F 112  ? 1.9916 1.6334 2.1344 -0.0684 0.1046  -0.0811 112  GLY F O   
16178 N  N   . LEU F 113  ? 2.0736 1.6770 2.1781 -0.0541 0.1115  -0.0728 113  LEU F N   
16179 C  CA  . LEU F 113  ? 2.0237 1.6451 2.1280 -0.0438 0.1070  -0.0684 113  LEU F CA  
16180 C  C   . LEU F 113  ? 1.9781 1.6042 2.0887 -0.0461 0.1149  -0.0624 113  LEU F C   
16181 O  O   . LEU F 113  ? 1.9883 1.5943 2.0852 -0.0441 0.1236  -0.0570 113  LEU F O   
16182 C  CB  . LEU F 113  ? 1.9918 1.5996 2.0729 -0.0299 0.1045  -0.0650 113  LEU F CB  
16183 C  CG  . LEU F 113  ? 1.9422 1.5485 2.0165 -0.0253 0.0957  -0.0704 113  LEU F CG  
16184 C  CD1 . LEU F 113  ? 1.8450 1.4412 1.8978 -0.0107 0.0935  -0.0665 113  LEU F CD1 
16185 C  CD2 . LEU F 113  ? 1.8822 1.5170 1.9749 -0.0273 0.0860  -0.0755 113  LEU F CD2 
16186 N  N   . GLU F 114  ? 1.9118 1.5643 2.0426 -0.0500 0.1120  -0.0633 114  GLU F N   
16187 C  CA  . GLU F 114  ? 1.9407 1.6001 2.0781 -0.0514 0.1188  -0.0576 114  GLU F CA  
16188 C  C   . GLU F 114  ? 1.8250 1.4822 1.9469 -0.0384 0.1188  -0.0508 114  GLU F C   
16189 O  O   . GLU F 114  ? 1.7878 1.4303 1.8992 -0.0364 0.1273  -0.0449 114  GLU F O   
16190 C  CB  . GLU F 114  ? 2.0195 1.7083 2.1816 -0.0576 0.1148  -0.0605 114  GLU F CB  
16191 C  CG  . GLU F 114  ? 1.9713 1.6686 2.1418 -0.0595 0.1218  -0.0552 114  GLU F CG  
16192 C  CD  . GLU F 114  ? 1.8370 1.5640 2.0311 -0.0643 0.1172  -0.0580 114  GLU F CD  
16193 O  OE1 . GLU F 114  ? 1.8444 1.5857 2.0472 -0.0650 0.1080  -0.0639 114  GLU F OE1 
16194 O  OE2 . GLU F 114  ? 1.6708 1.4063 1.8740 -0.0669 0.1229  -0.0544 114  GLU F OE2 
16195 N  N   . HIS F 115  ? 2.1068 1.7786 2.2271 -0.0296 0.1093  -0.0516 115  HIS F N   
16196 C  CA  . HIS F 115  ? 2.0615 1.7327 2.1675 -0.0171 0.1079  -0.0461 115  HIS F CA  
16197 C  C   . HIS F 115  ? 2.0411 1.6998 2.1292 -0.0080 0.1026  -0.0474 115  HIS F C   
16198 O  O   . HIS F 115  ? 2.0578 1.7172 2.1485 -0.0104 0.0971  -0.0533 115  HIS F O   
16199 C  CB  . HIS F 115  ? 1.9861 1.6853 2.1047 -0.0137 0.1015  -0.0455 115  HIS F CB  
16200 C  CG  . HIS F 115  ? 2.0573 1.7741 2.1855 -0.0136 0.0911  -0.0516 115  HIS F CG  
16201 N  ND1 . HIS F 115  ? 2.1436 1.8722 2.2898 -0.0235 0.0887  -0.0573 115  HIS F ND1 
16202 C  CD2 . HIS F 115  ? 2.1026 1.8274 2.2248 -0.0047 0.0826  -0.0528 115  HIS F CD2 
16203 C  CE1 . HIS F 115  ? 2.2029 1.9452 2.3529 -0.0204 0.0791  -0.0617 115  HIS F CE1 
16204 N  NE2 . HIS F 115  ? 2.2173 1.9575 2.3530 -0.0092 0.0755  -0.0590 115  HIS F NE2 
16205 N  N   . PRO F 116  ? 1.5979 1.2447 1.6673 0.0026  0.1043  -0.0422 116  PRO F N   
16206 C  CA  . PRO F 116  ? 1.5484 1.1826 1.6001 0.0118  0.0999  -0.0433 116  PRO F CA  
16207 C  C   . PRO F 116  ? 1.5755 1.2291 1.6337 0.0156  0.0889  -0.0479 116  PRO F C   
16208 O  O   . PRO F 116  ? 1.5149 1.1924 1.5879 0.0146  0.0842  -0.0487 116  PRO F O   
16209 C  CB  . PRO F 116  ? 1.4613 1.0867 1.4960 0.0228  0.1029  -0.0366 116  PRO F CB  
16210 C  CG  . PRO F 116  ? 1.5216 1.1423 1.5601 0.0172  0.1123  -0.0321 116  PRO F CG  
16211 C  CD  . PRO F 116  ? 1.5972 1.2391 1.6600 0.0063  0.1112  -0.0352 116  PRO F CD  
16212 N  N   . LEU F 117  ? 1.5960 1.2382 1.6421 0.0205  0.0849  -0.0509 117  LEU F N   
16213 C  CA  . LEU F 117  ? 1.5134 1.1714 1.5644 0.0237  0.0750  -0.0557 117  LEU F CA  
16214 C  C   . LEU F 117  ? 1.4356 1.1104 1.4847 0.0341  0.0696  -0.0529 117  LEU F C   
16215 O  O   . LEU F 117  ? 1.3649 1.0604 1.4246 0.0347  0.0622  -0.0559 117  LEU F O   
16216 C  CB  . LEU F 117  ? 1.5200 1.1596 1.5568 0.0270  0.0729  -0.0593 117  LEU F CB  
16217 C  CG  . LEU F 117  ? 1.5626 1.2145 1.6023 0.0301  0.0632  -0.0648 117  LEU F CG  
16218 C  CD1 . LEU F 117  ? 1.5539 1.2225 1.6142 0.0195  0.0596  -0.0703 117  LEU F CD1 
16219 C  CD2 . LEU F 117  ? 1.6247 1.2546 1.6473 0.0343  0.0626  -0.0673 117  LEU F CD2 
16220 N  N   . TYR F 118  ? 1.5484 1.2146 1.5839 0.0422  0.0731  -0.0472 118  TYR F N   
16221 C  CA  . TYR F 118  ? 1.5528 1.2339 1.5859 0.0518  0.0685  -0.0443 118  TYR F CA  
16222 C  C   . TYR F 118  ? 1.5292 1.2164 1.5667 0.0509  0.0736  -0.0390 118  TYR F C   
16223 O  O   . TYR F 118  ? 1.4758 1.1486 1.5103 0.0467  0.0817  -0.0360 118  TYR F O   
16224 C  CB  . TYR F 118  ? 1.4614 1.1289 1.4738 0.0639  0.0671  -0.0427 118  TYR F CB  
16225 C  CG  . TYR F 118  ? 1.4848 1.1533 1.4936 0.0676  0.0600  -0.0477 118  TYR F CG  
16226 C  CD1 . TYR F 118  ? 1.4568 1.1451 1.4697 0.0736  0.0522  -0.0493 118  TYR F CD1 
16227 C  CD2 . TYR F 118  ? 1.4856 1.1347 1.4866 0.0650  0.0616  -0.0510 118  TYR F CD2 
16228 C  CE1 . TYR F 118  ? 1.4024 1.0914 1.4117 0.0772  0.0461  -0.0539 118  TYR F CE1 
16229 C  CE2 . TYR F 118  ? 1.4457 1.0952 1.4428 0.0687  0.0552  -0.0556 118  TYR F CE2 
16230 C  CZ  . TYR F 118  ? 1.4582 1.1279 1.4595 0.0749  0.0475  -0.0570 118  TYR F CZ  
16231 O  OH  . TYR F 118  ? 1.4880 1.1580 1.4851 0.0787  0.0415  -0.0616 118  TYR F OH  
16232 N  N   . GLU F 119  ? 1.8634 1.5716 1.9078 0.0550  0.0689  -0.0378 119  GLU F N   
16233 C  CA  . GLU F 119  ? 1.8402 1.5557 1.8892 0.0545  0.0729  -0.0330 119  GLU F CA  
16234 C  C   . GLU F 119  ? 1.7987 1.4976 1.8296 0.0623  0.0780  -0.0276 119  GLU F C   
16235 O  O   . GLU F 119  ? 1.8229 1.5160 1.8534 0.0598  0.0849  -0.0235 119  GLU F O   
16236 C  CB  . GLU F 119  ? 1.7876 1.5286 1.8471 0.0573  0.0664  -0.0334 119  GLU F CB  
16237 C  CG  . GLU F 119  ? 1.8805 1.6386 1.9560 0.0514  0.0604  -0.0389 119  GLU F CG  
16238 C  CD  . GLU F 119  ? 1.9873 1.7690 2.0769 0.0503  0.0573  -0.0382 119  GLU F CD  
16239 O  OE1 . GLU F 119  ? 1.8798 1.6645 1.9669 0.0538  0.0600  -0.0336 119  GLU F OE1 
16240 O  OE2 . GLU F 119  ? 2.1119 1.9087 2.2144 0.0462  0.0523  -0.0423 119  GLU F OE2 
16241 N  N   . TRP F 120  ? 1.3192 1.0102 1.3346 0.0723  0.0746  -0.0275 120  TRP F N   
16242 C  CA  . TRP F 120  ? 1.2729 0.9487 1.2701 0.0811  0.0785  -0.0226 120  TRP F CA  
16243 C  C   . TRP F 120  ? 1.3873 1.0357 1.3722 0.0788  0.0865  -0.0208 120  TRP F C   
16244 O  O   . TRP F 120  ? 1.3501 0.9834 1.3187 0.0860  0.0905  -0.0165 120  TRP F O   
16245 C  CB  . TRP F 120  ? 1.2240 0.9019 1.2094 0.0929  0.0718  -0.0234 120  TRP F CB  
16246 C  CG  . TRP F 120  ? 1.2985 0.9746 1.2832 0.0930  0.0668  -0.0286 120  TRP F CG  
16247 C  CD1 . TRP F 120  ? 1.3259 1.0209 1.3211 0.0928  0.0592  -0.0328 120  TRP F CD1 
16248 C  CD2 . TRP F 120  ? 1.3585 1.0119 1.3305 0.0939  0.0692  -0.0301 120  TRP F CD2 
16249 N  NE1 . TRP F 120  ? 1.2773 0.9632 1.2673 0.0934  0.0566  -0.0369 120  TRP F NE1 
16250 C  CE2 . TRP F 120  ? 1.3488 1.0091 1.3245 0.0940  0.0626  -0.0354 120  TRP F CE2 
16251 C  CE3 . TRP F 120  ? 1.3458 0.9730 1.3029 0.0946  0.0765  -0.0273 120  TRP F CE3 
16252 C  CZ2 . TRP F 120  ? 1.3791 1.0211 1.3444 0.0949  0.0628  -0.0382 120  TRP F CZ2 
16253 C  CZ3 . TRP F 120  ? 1.3744 0.9831 1.3211 0.0953  0.0769  -0.0301 120  TRP F CZ3 
16254 C  CH2 . TRP F 120  ? 1.4077 1.0240 1.3586 0.0954  0.0700  -0.0356 120  TRP F CH2 
16255 N  N   . ALA F 121  ? 1.5562 1.1973 1.5480 0.0692  0.0891  -0.0241 121  ALA F N   
16256 C  CA  . ALA F 121  ? 1.5887 1.2035 1.5701 0.0655  0.0974  -0.0227 121  ALA F CA  
16257 C  C   . ALA F 121  ? 1.6091 1.2229 1.6018 0.0547  0.1054  -0.0208 121  ALA F C   
16258 O  O   . ALA F 121  ? 1.5146 1.1069 1.5000 0.0504  0.1133  -0.0194 121  ALA F O   
16259 C  CB  . ALA F 121  ? 1.5945 1.1986 1.5739 0.0622  0.0954  -0.0280 121  ALA F CB  
16260 N  N   . ASN F 122  ? 1.8189 1.4552 1.8290 0.0503  0.1036  -0.0207 122  ASN F N   
16261 C  CA  . ASN F 122  ? 1.8036 1.4415 1.8257 0.0404  0.1110  -0.0190 122  ASN F CA  
16262 C  C   . ASN F 122  ? 1.7851 1.4152 1.7968 0.0455  0.1174  -0.0123 122  ASN F C   
16263 O  O   . ASN F 122  ? 1.7036 1.3463 1.7136 0.0530  0.1134  -0.0100 122  ASN F O   
16264 C  CB  . ASN F 122  ? 1.7460 1.4112 1.7907 0.0340  0.1062  -0.0219 122  ASN F CB  
16265 C  CG  . ASN F 122  ? 1.7756 1.4430 1.8354 0.0221  0.1132  -0.0218 122  ASN F CG  
16266 O  OD1 . ASN F 122  ? 1.8282 1.4763 1.8831 0.0168  0.1212  -0.0207 122  ASN F OD1 
16267 N  ND2 . ASN F 122  ? 1.7934 1.4843 1.8715 0.0179  0.1103  -0.0229 122  ASN F ND2 
16268 N  N   . PRO F 123  ? 1.6658 1.2752 1.6701 0.0416  0.1273  -0.0091 123  PRO F N   
16269 C  CA  . PRO F 123  ? 1.5976 1.1987 1.5909 0.0470  0.1336  -0.0025 123  PRO F CA  
16270 C  C   . PRO F 123  ? 1.5779 1.1999 1.5858 0.0443  0.1339  -0.0006 123  PRO F C   
16271 O  O   . PRO F 123  ? 1.5587 1.1788 1.5576 0.0508  0.1363  0.0043  123  PRO F O   
16272 C  CB  . PRO F 123  ? 1.5815 1.1568 1.5669 0.0410  0.1446  -0.0004 123  PRO F CB  
16273 C  CG  . PRO F 123  ? 1.6538 1.2190 1.6385 0.0367  0.1427  -0.0055 123  PRO F CG  
16274 C  CD  . PRO F 123  ? 1.6653 1.2561 1.6689 0.0330  0.1332  -0.0112 123  PRO F CD  
16275 N  N   . GLU F 124  ? 2.0514 1.6930 2.0810 0.0352  0.1313  -0.0043 124  GLU F N   
16276 C  CA  . GLU F 124  ? 2.0963 1.7580 2.1402 0.0327  0.1315  -0.0026 124  GLU F CA  
16277 C  C   . GLU F 124  ? 2.0637 1.7444 2.1082 0.0412  0.1226  -0.0026 124  GLU F C   
16278 O  O   . GLU F 124  ? 2.0379 1.7338 2.0913 0.0408  0.1227  -0.0007 124  GLU F O   
16279 C  CB  . GLU F 124  ? 2.1286 1.8051 2.1955 0.0205  0.1315  -0.0068 124  GLU F CB  
16280 C  CG  . GLU F 124  ? 2.0701 1.7302 2.1389 0.0110  0.1380  -0.0089 124  GLU F CG  
16281 C  CD  . GLU F 124  ? 2.1501 1.7923 2.2119 0.0081  0.1499  -0.0038 124  GLU F CD  
16282 O  OE1 . GLU F 124  ? 2.0293 1.6788 2.0939 0.0094  0.1534  0.0004  124  GLU F OE1 
16283 O  OE2 . GLU F 124  ? 2.3271 1.9473 2.3803 0.0045  0.1560  -0.0039 124  GLU F OE2 
16284 N  N   . VAL F 125  ? 1.2924 0.9722 1.3275 0.0488  0.1154  -0.0047 125  VAL F N   
16285 C  CA  . VAL F 125  ? 1.1028 0.8016 1.1398 0.0560  0.1066  -0.0056 125  VAL F CA  
16286 C  C   . VAL F 125  ? 1.1087 0.7983 1.1260 0.0681  0.1056  -0.0021 125  VAL F C   
16287 O  O   . VAL F 125  ? 1.1670 0.8672 1.1837 0.0733  0.1037  0.0004  125  VAL F O   
16288 C  CB  . VAL F 125  ? 1.0651 0.7752 1.1101 0.0547  0.0981  -0.0116 125  VAL F CB  
16289 C  CG1 . VAL F 125  ? 1.0136 0.7403 1.0577 0.0631  0.0896  -0.0123 125  VAL F CG1 
16290 C  CG2 . VAL F 125  ? 1.1417 0.8653 1.2078 0.0435  0.0979  -0.0153 125  VAL F CG2 
16291 N  N   . VAL F 126  ? 1.4851 1.1547 1.4860 0.0730  0.1066  -0.0021 126  VAL F N   
16292 C  CA  . VAL F 126  ? 1.5434 1.2053 1.5257 0.0854  0.1044  0.0005  126  VAL F CA  
16293 C  C   . VAL F 126  ? 1.5539 1.2019 1.5234 0.0892  0.1118  0.0064  126  VAL F C   
16294 O  O   . VAL F 126  ? 1.5649 1.2097 1.5203 0.0997  0.1097  0.0088  126  VAL F O   
16295 C  CB  . VAL F 126  ? 1.6120 1.2573 1.5802 0.0903  0.1025  -0.0016 126  VAL F CB  
16296 C  CG1 . VAL F 126  ? 1.5977 1.2588 1.5744 0.0909  0.0933  -0.0070 126  VAL F CG1 
16297 C  CG2 . VAL F 126  ? 1.6875 1.3116 1.6530 0.0827  0.1103  -0.0017 126  VAL F CG2 
16298 N  N   . THR F 127  ? 1.5703 1.2102 1.5444 0.0812  0.1204  0.0088  127  THR F N   
16299 C  CA  . THR F 127  ? 1.5643 1.1895 1.5252 0.0849  0.1281  0.0146  127  THR F CA  
16300 C  C   . THR F 127  ? 1.5137 1.1560 1.4847 0.0837  0.1285  0.0169  127  THR F C   
16301 O  O   . THR F 127  ? 1.5064 1.1632 1.4963 0.0746  0.1291  0.0152  127  THR F O   
16302 C  CB  . THR F 127  ? 1.6067 1.2104 1.5644 0.0775  0.1385  0.0163  127  THR F CB  
16303 O  OG1 . THR F 127  ? 1.6580 1.2737 1.6368 0.0652  0.1412  0.0144  127  THR F OG1 
16304 C  CG2 . THR F 127  ? 1.5995 1.1850 1.5468 0.0783  0.1383  0.0138  127  THR F CG2 
16305 N  N   . PRO F 128  ? 1.4741 1.1154 1.4330 0.0929  0.1280  0.0205  128  PRO F N   
16306 C  CA  . PRO F 128  ? 1.3987 1.0545 1.3658 0.0919  0.1289  0.0229  128  PRO F CA  
16307 C  C   . PRO F 128  ? 1.4162 1.0636 1.3881 0.0837  0.1393  0.0260  128  PRO F C   
16308 O  O   . PRO F 128  ? 1.5093 1.1343 1.4693 0.0833  0.1471  0.0287  128  PRO F O   
16309 C  CB  . PRO F 128  ? 1.3469 0.9980 1.2961 0.1041  0.1269  0.0261  128  PRO F CB  
16310 C  CG  . PRO F 128  ? 1.4348 1.0631 1.3646 0.1105  0.1285  0.0268  128  PRO F CG  
16311 C  CD  . PRO F 128  ? 1.5653 1.1932 1.5026 0.1050  0.1259  0.0223  128  PRO F CD  
16312 N  N   . GLY F 129  ? 1.3285 0.9939 1.3177 0.0775  0.1397  0.0257  129  GLY F N   
16313 C  CA  . GLY F 129  ? 1.3588 1.0201 1.3563 0.0687  0.1491  0.0280  129  GLY F CA  
16314 C  C   . GLY F 129  ? 1.3736 1.0368 1.3866 0.0573  0.1510  0.0242  129  GLY F C   
16315 O  O   . GLY F 129  ? 1.4016 1.0619 1.4229 0.0492  0.1591  0.0256  129  GLY F O   
16316 N  N   . GLY F 130  ? 1.3842 1.0524 1.4015 0.0566  0.1438  0.0193  130  GLY F N   
16317 C  CA  . GLY F 130  ? 1.4522 1.1238 1.4848 0.0459  0.1445  0.0151  130  GLY F CA  
16318 C  C   . GLY F 130  ? 1.4834 1.1803 1.5388 0.0391  0.1412  0.0124  130  GLY F C   
16319 O  O   . GLY F 130  ? 1.4913 1.2044 1.5508 0.0431  0.1371  0.0133  130  GLY F O   
16320 N  N   . ALA F 131  ? 1.5273 1.2275 1.5977 0.0287  0.1432  0.0089  131  ALA F N   
16321 C  CA  . ALA F 131  ? 1.5674 1.2913 1.6601 0.0218  0.1405  0.0062  131  ALA F CA  
16322 C  C   . ALA F 131  ? 1.6199 1.3629 1.7193 0.0252  0.1290  0.0021  131  ALA F C   
16323 O  O   . ALA F 131  ? 1.6683 1.4317 1.7806 0.0243  0.1255  0.0014  131  ALA F O   
16324 C  CB  . ALA F 131  ? 1.5316 1.2540 1.6385 0.0098  0.1452  0.0031  131  ALA F CB  
16325 N  N   . GLU F 132  ? 1.8416 1.5782 1.9320 0.0294  0.1234  -0.0007 132  GLU F N   
16326 C  CA  . GLU F 132  ? 1.7311 1.4842 1.8268 0.0326  0.1129  -0.0048 132  GLU F CA  
16327 C  C   . GLU F 132  ? 1.6553 1.4037 1.7338 0.0442  0.1081  -0.0032 132  GLU F C   
16328 O  O   . GLU F 132  ? 1.6050 1.3550 1.6800 0.0478  0.1013  -0.0065 132  GLU F O   
16329 C  CB  . GLU F 132  ? 1.7159 1.4685 1.8188 0.0267  0.1096  -0.0105 132  GLU F CB  
16330 C  CG  . GLU F 132  ? 1.7990 1.5538 1.9179 0.0149  0.1147  -0.0125 132  GLU F CG  
16331 C  CD  . GLU F 132  ? 1.8794 1.6280 2.0016 0.0091  0.1126  -0.0179 132  GLU F CD  
16332 O  OE1 . GLU F 132  ? 1.8397 1.5819 1.9512 0.0147  0.1073  -0.0199 132  GLU F OE1 
16333 O  OE2 . GLU F 132  ? 1.9033 1.6535 2.0387 -0.0009 0.1164  -0.0203 132  GLU F OE2 
16334 N  N   . PHE F 133  ? 1.4710 1.2139 1.5387 0.0502  0.1117  0.0018  133  PHE F N   
16335 C  CA  . PHE F 133  ? 1.3986 1.1362 1.4494 0.0613  0.1077  0.0035  133  PHE F CA  
16336 C  C   . PHE F 133  ? 1.2856 1.0442 1.3428 0.0653  0.0981  0.0007  133  PHE F C   
16337 O  O   . PHE F 133  ? 1.3002 1.0759 1.3688 0.0634  0.0965  0.0010  133  PHE F O   
16338 C  CB  . PHE F 133  ? 1.3721 1.1009 1.4112 0.0663  0.1135  0.0092  133  PHE F CB  
16339 C  CG  . PHE F 133  ? 1.3549 1.0795 1.3771 0.0780  0.1093  0.0108  133  PHE F CG  
16340 C  CD1 . PHE F 133  ? 1.4031 1.1119 1.4102 0.0837  0.1082  0.0102  133  PHE F CD1 
16341 C  CD2 . PHE F 133  ? 1.3831 1.1201 1.4048 0.0832  0.1063  0.0126  133  PHE F CD2 
16342 C  CE1 . PHE F 133  ? 1.3632 1.0693 1.3553 0.0947  0.1041  0.0115  133  PHE F CE1 
16343 C  CE2 . PHE F 133  ? 1.4060 1.1403 1.4130 0.0937  0.1022  0.0137  133  PHE F CE2 
16344 C  CZ  . PHE F 133  ? 1.2803 0.9997 1.2728 0.0995  0.1010  0.0131  133  PHE F CZ  
16345 N  N   . ASP F 134  ? 1.3716 1.1284 1.4210 0.0710  0.0920  -0.0018 134  ASP F N   
16346 C  CA  . ASP F 134  ? 1.2443 1.0191 1.2973 0.0759  0.0831  -0.0042 134  ASP F CA  
16347 C  C   . ASP F 134  ? 1.2828 1.0506 1.3183 0.0869  0.0806  -0.0024 134  ASP F C   
16348 O  O   . ASP F 134  ? 1.3413 1.0950 1.3649 0.0909  0.0802  -0.0033 134  ASP F O   
16349 C  CB  . ASP F 134  ? 1.1665 0.9487 1.2282 0.0724  0.0774  -0.0097 134  ASP F CB  
16350 C  CG  . ASP F 134  ? 1.2316 1.0342 1.2998 0.0758  0.0690  -0.0121 134  ASP F CG  
16351 O  OD1 . ASP F 134  ? 1.2317 1.0350 1.2897 0.0842  0.0650  -0.0117 134  ASP F OD1 
16352 O  OD2 . ASP F 134  ? 1.2355 1.0537 1.3192 0.0699  0.0666  -0.0145 134  ASP F OD2 
16353 N  N   . PRO F 135  ? 1.2435 1.0204 1.2766 0.0921  0.0789  -0.0001 135  PRO F N   
16354 C  CA  . PRO F 135  ? 1.2020 0.9720 1.2183 0.1027  0.0768  0.0016  135  PRO F CA  
16355 C  C   . PRO F 135  ? 1.2045 0.9789 1.2170 0.1082  0.0694  -0.0021 135  PRO F C   
16356 O  O   . PRO F 135  ? 1.2586 1.0216 1.2558 0.1163  0.0686  -0.0013 135  PRO F O   
16357 C  CB  . PRO F 135  ? 1.2086 0.9914 1.2272 0.1052  0.0758  0.0039  135  PRO F CB  
16358 C  CG  . PRO F 135  ? 1.2259 1.0138 1.2577 0.0964  0.0808  0.0051  135  PRO F CG  
16359 C  CD  . PRO F 135  ? 1.2601 1.0520 1.3047 0.0886  0.0797  0.0013  135  PRO F CD  
16360 N  N   . ILE F 136  ? 1.0489 0.8393 1.0746 0.1045  0.0639  -0.0060 136  ILE F N   
16361 C  CA  . ILE F 136  ? 1.0124 0.8076 1.0349 0.1097  0.0571  -0.0095 136  ILE F CA  
16362 C  C   . ILE F 136  ? 1.0354 0.8134 1.0500 0.1098  0.0585  -0.0112 136  ILE F C   
16363 O  O   . ILE F 136  ? 1.0764 0.8476 1.0789 0.1176  0.0556  -0.0120 136  ILE F O   
16364 C  CB  . ILE F 136  ? 0.9445 0.7609 0.9827 0.1057  0.0513  -0.0131 136  ILE F CB  
16365 C  CG1 . ILE F 136  ? 0.9294 0.7606 0.9763 0.1038  0.0514  -0.0112 136  ILE F CG1 
16366 C  CG2 . ILE F 136  ? 0.9359 0.7594 0.9700 0.1124  0.0442  -0.0162 136  ILE F CG2 
16367 C  CD1 . ILE F 136  ? 0.7195 0.5702 0.7818 0.0992  0.0468  -0.0143 136  ILE F CD1 
16368 N  N   . ILE F 137  ? 0.9782 0.7486 0.9994 0.1013  0.0629  -0.0118 137  ILE F N   
16369 C  CA  . ILE F 137  ? 0.9830 0.7356 0.9966 0.1005  0.0648  -0.0135 137  ILE F CA  
16370 C  C   . ILE F 137  ? 1.0702 0.8006 1.0656 0.1061  0.0705  -0.0095 137  ILE F C   
16371 O  O   . ILE F 137  ? 1.0957 0.8121 1.0780 0.1116  0.0698  -0.0103 137  ILE F O   
16372 C  CB  . ILE F 137  ? 1.0007 0.7523 1.0275 0.0891  0.0680  -0.0156 137  ILE F CB  
16373 C  CG1 . ILE F 137  ? 1.0310 0.8050 1.0752 0.0843  0.0621  -0.0194 137  ILE F CG1 
16374 C  CG2 . ILE F 137  ? 1.0439 0.7766 1.0628 0.0878  0.0699  -0.0177 137  ILE F CG2 
16375 C  CD1 . ILE F 137  ? 0.9244 0.6991 0.9820 0.0736  0.0639  -0.0224 137  ILE F CD1 
16376 N  N   . ALA F 138  ? 1.2728 0.9992 1.2663 0.1053  0.0762  -0.0052 138  ALA F N   
16377 C  CA  . ALA F 138  ? 1.3459 1.0503 1.3214 0.1105  0.0822  -0.0011 138  ALA F CA  
16378 C  C   . ALA F 138  ? 1.4086 1.1121 1.3692 0.1229  0.0781  0.0002  138  ALA F C   
16379 O  O   . ALA F 138  ? 1.5548 1.2389 1.4981 0.1292  0.0815  0.0026  138  ALA F O   
16380 C  CB  . ALA F 138  ? 1.3813 1.0822 1.3594 0.1059  0.0896  0.0031  138  ALA F CB  
16381 N  N   . HIS F 139  ? 1.3727 1.0964 1.3393 0.1266  0.0710  -0.0015 139  HIS F N   
16382 C  CA  . HIS F 139  ? 1.3720 1.0969 1.3259 0.1382  0.0665  -0.0010 139  HIS F CA  
16383 C  C   . HIS F 139  ? 1.3984 1.1118 1.3407 0.1444  0.0640  -0.0032 139  HIS F C   
16384 O  O   . HIS F 139  ? 1.4398 1.1470 1.3674 0.1547  0.0623  -0.0020 139  HIS F O   
16385 C  CB  . HIS F 139  ? 1.3117 1.0616 1.2764 0.1394  0.0595  -0.0030 139  HIS F CB  
16386 C  CG  . HIS F 139  ? 1.3283 1.0831 1.2834 0.1503  0.0535  -0.0041 139  HIS F CG  
16387 N  ND1 . HIS F 139  ? 1.3973 1.1488 1.3403 0.1585  0.0537  -0.0013 139  HIS F ND1 
16388 C  CD2 . HIS F 139  ? 1.3253 1.0886 1.2813 0.1542  0.0471  -0.0079 139  HIS F CD2 
16389 C  CE1 . HIS F 139  ? 1.3286 1.0870 1.2661 0.1670  0.0475  -0.0034 139  HIS F CE1 
16390 N  NE2 . HIS F 139  ? 1.2642 1.0298 1.2095 0.1646  0.0437  -0.0073 139  HIS F NE2 
16391 N  N   . LYS F 140  ? 1.3327 1.0427 1.2809 0.1385  0.0639  -0.0064 140  LYS F N   
16392 C  CA  . LYS F 140  ? 1.3051 1.0039 1.2430 0.1436  0.0616  -0.0088 140  LYS F CA  
16393 C  C   . LYS F 140  ? 1.4674 1.1401 1.3951 0.1409  0.0688  -0.0073 140  LYS F C   
16394 O  O   . LYS F 140  ? 1.4448 1.1083 1.3698 0.1399  0.0681  -0.0102 140  LYS F O   
16395 C  CB  . LYS F 140  ? 1.2602 0.9737 1.2110 0.1396  0.0556  -0.0139 140  LYS F CB  
16396 C  CG  . LYS F 140  ? 1.3114 1.0502 1.2724 0.1418  0.0488  -0.0155 140  LYS F CG  
16397 C  CD  . LYS F 140  ? 1.1269 0.8797 1.1020 0.1361  0.0441  -0.0202 140  LYS F CD  
16398 C  CE  . LYS F 140  ? 1.0413 0.8043 1.0335 0.1250  0.0461  -0.0204 140  LYS F CE  
16399 N  NZ  . LYS F 140  ? 1.1137 0.8958 1.1145 0.1252  0.0440  -0.0190 140  LYS F NZ  
16400 N  N   . VAL F 141  ? 2.0587 1.7187 1.9802 0.1397  0.0759  -0.0029 141  VAL F N   
16401 C  CA  . VAL F 141  ? 1.9840 1.6194 1.8974 0.1354  0.0839  -0.0012 141  VAL F CA  
16402 C  C   . VAL F 141  ? 2.0011 1.6147 1.8934 0.1447  0.0846  -0.0007 141  VAL F C   
16403 O  O   . VAL F 141  ? 2.0485 1.6438 1.9360 0.1406  0.0889  -0.0015 141  VAL F O   
16404 C  CB  . VAL F 141  ? 2.1391 1.7675 2.0521 0.1313  0.0919  0.0036  141  VAL F CB  
16405 C  CG1 . VAL F 141  ? 2.0625 1.6861 1.9601 0.1420  0.0925  0.0078  141  VAL F CG1 
16406 C  CG2 . VAL F 141  ? 2.1921 1.7974 2.1007 0.1243  0.1006  0.0048  141  VAL F CG2 
16407 N  N   . PRO F 142  ? 1.4998 1.1137 1.3786 0.1573  0.0806  0.0005  142  PRO F N   
16408 C  CA  . PRO F 142  ? 1.4252 1.0181 1.2842 0.1662  0.0812  0.0006  142  PRO F CA  
16409 C  C   . PRO F 142  ? 1.4441 1.0429 1.3061 0.1678  0.0748  -0.0045 142  PRO F C   
16410 O  O   . PRO F 142  ? 1.4227 1.0027 1.2743 0.1689  0.0768  -0.0056 142  PRO F O   
16411 C  CB  . PRO F 142  ? 1.4063 0.9998 1.2513 0.1790  0.0791  0.0036  142  PRO F CB  
16412 C  CG  . PRO F 142  ? 1.4271 1.0488 1.2872 0.1781  0.0731  0.0024  142  PRO F CG  
16413 C  CD  . PRO F 142  ? 1.4616 1.0934 1.3414 0.1643  0.0758  0.0017  142  PRO F CD  
16414 N  N   . TRP F 143  ? 1.6273 1.2516 1.5030 0.1677  0.0673  -0.0076 143  TRP F N   
16415 C  CA  . TRP F 143  ? 1.5332 1.1649 1.4122 0.1695  0.0610  -0.0124 143  TRP F CA  
16416 C  C   . TRP F 143  ? 1.5434 1.1724 1.4337 0.1579  0.0626  -0.0157 143  TRP F C   
16417 O  O   . TRP F 143  ? 1.5714 1.1871 1.4548 0.1587  0.0625  -0.0182 143  TRP F O   
16418 C  CB  . TRP F 143  ? 1.5004 1.1601 1.3905 0.1727  0.0532  -0.0145 143  TRP F CB  
16419 C  CG  . TRP F 143  ? 1.4708 1.1400 1.3643 0.1754  0.0466  -0.0193 143  TRP F CG  
16420 C  CD1 . TRP F 143  ? 1.4460 1.1332 1.3564 0.1685  0.0425  -0.0231 143  TRP F CD1 
16421 C  CD2 . TRP F 143  ? 1.5125 1.1735 1.3917 0.1861  0.0436  -0.0207 143  TRP F CD2 
16422 N  NE1 . TRP F 143  ? 1.4715 1.1621 1.3788 0.1741  0.0372  -0.0268 143  TRP F NE1 
16423 C  CE2 . TRP F 143  ? 1.5276 1.2026 1.4162 0.1849  0.0378  -0.0255 143  TRP F CE2 
16424 C  CE3 . TRP F 143  ? 1.5741 1.2174 1.4331 0.1971  0.0452  -0.0185 143  TRP F CE3 
16425 C  CZ2 . TRP F 143  ? 1.5020 1.1739 1.3807 0.1941  0.0338  -0.0280 143  TRP F CZ2 
16426 C  CZ3 . TRP F 143  ? 1.5531 1.1936 1.4024 0.2064  0.0411  -0.0210 143  TRP F CZ3 
16427 C  CH2 . TRP F 143  ? 1.4790 1.1338 1.3384 0.2048  0.0355  -0.0257 143  TRP F CH2 
16428 N  N   . LEU F 144  ? 1.1684 0.8100 1.0762 0.1471  0.0640  -0.0159 144  LEU F N   
16429 C  CA  . LEU F 144  ? 1.1499 0.7910 1.0702 0.1355  0.0653  -0.0192 144  LEU F CA  
16430 C  C   . LEU F 144  ? 1.0955 0.7144 1.0108 0.1288  0.0745  -0.0166 144  LEU F C   
16431 O  O   . LEU F 144  ? 1.0780 0.7010 1.0045 0.1199  0.0788  -0.0151 144  LEU F O   
16432 C  CB  . LEU F 144  ? 1.0952 0.7619 1.0370 0.1277  0.0618  -0.0211 144  LEU F CB  
16433 C  CG  . LEU F 144  ? 0.9193 0.6073 0.8687 0.1313  0.0530  -0.0249 144  LEU F CG  
16434 C  CD1 . LEU F 144  ? 0.8824 0.5934 0.8519 0.1234  0.0506  -0.0262 144  LEU F CD1 
16435 C  CD2 . LEU F 144  ? 0.9739 0.6547 0.9201 0.1316  0.0501  -0.0295 144  LEU F CD2 
16436 N  N   . SER F 145  ? 1.5618 1.1563 1.4596 0.1334  0.0778  -0.0160 145  SER F N   
16437 C  CA  . SER F 145  ? 1.6605 1.2308 1.5514 0.1274  0.0868  -0.0139 145  SER F CA  
16438 C  C   . SER F 145  ? 1.6186 1.1736 1.5055 0.1241  0.0871  -0.0179 145  SER F C   
16439 O  O   . SER F 145  ? 1.5617 1.1174 1.4423 0.1311  0.0813  -0.0208 145  SER F O   
16440 C  CB  . SER F 145  ? 1.7348 1.2854 1.6048 0.1367  0.0920  -0.0084 145  SER F CB  
16441 O  OG  . SER F 145  ? 1.7286 1.2925 1.6014 0.1400  0.0917  -0.0049 145  SER F OG  
16442 N  N   . PRO F 146  ? 1.2873 0.8285 1.1780 0.1132  0.0938  -0.0183 146  PRO F N   
16443 C  CA  . PRO F 146  ? 1.3853 0.9110 1.2721 0.1094  0.0942  -0.0224 146  PRO F CA  
16444 C  C   . PRO F 146  ? 1.4902 0.9925 1.3528 0.1206  0.0950  -0.0214 146  PRO F C   
16445 O  O   . PRO F 146  ? 1.5230 1.0205 1.3814 0.1226  0.0910  -0.0255 146  PRO F O   
16446 C  CB  . PRO F 146  ? 1.3901 0.9034 1.2835 0.0962  0.1029  -0.0218 146  PRO F CB  
16447 C  CG  . PRO F 146  ? 1.3052 0.8379 1.2142 0.0911  0.1042  -0.0193 146  PRO F CG  
16448 C  CD  . PRO F 146  ? 1.2611 0.8021 1.1615 0.1034  0.1010  -0.0154 146  PRO F CD  
16449 N  N   . LEU F 147  ? 1.7273 1.2148 1.5734 0.1284  0.1000  -0.0159 147  LEU F N   
16450 C  CA  . LEU F 147  ? 1.7758 1.2416 1.5981 0.1404  0.1005  -0.0146 147  LEU F CA  
16451 C  C   . LEU F 147  ? 1.7503 1.2321 1.5695 0.1526  0.0910  -0.0165 147  LEU F C   
16452 O  O   . LEU F 147  ? 1.8075 1.2793 1.6153 0.1592  0.0881  -0.0189 147  LEU F O   
16453 C  CB  . LEU F 147  ? 1.8837 1.3303 1.6890 0.1460  0.1081  -0.0082 147  LEU F CB  
16454 C  CG  . LEU F 147  ? 1.9396 1.3569 1.7184 0.1565  0.1112  -0.0063 147  LEU F CG  
16455 C  CD1 . LEU F 147  ? 1.9298 1.3227 1.7040 0.1481  0.1171  -0.0085 147  LEU F CD1 
16456 C  CD2 . LEU F 147  ? 1.9110 1.3144 1.6736 0.1640  0.1172  0.0002  147  LEU F CD2 
16457 N  N   . TRP F 148  ? 1.6117 1.1182 1.4410 0.1555  0.0863  -0.0154 148  TRP F N   
16458 C  CA  . TRP F 148  ? 1.6322 1.1553 1.4597 0.1665  0.0777  -0.0171 148  TRP F CA  
16459 C  C   . TRP F 148  ? 1.6952 1.2323 1.5349 0.1628  0.0710  -0.0231 148  TRP F C   
16460 O  O   . TRP F 148  ? 1.6837 1.2216 1.5154 0.1718  0.0658  -0.0255 148  TRP F O   
16461 C  CB  . TRP F 148  ? 1.6048 1.1507 1.4409 0.1693  0.0747  -0.0146 148  TRP F CB  
16462 C  CG  . TRP F 148  ? 1.6224 1.1563 1.4431 0.1772  0.0791  -0.0091 148  TRP F CG  
16463 C  CD1 . TRP F 148  ? 1.6433 1.1547 1.4542 0.1744  0.0880  -0.0050 148  TRP F CD1 
16464 C  CD2 . TRP F 148  ? 1.6593 1.2034 1.4727 0.1894  0.0748  -0.0071 148  TRP F CD2 
16465 N  NE1 . TRP F 148  ? 1.6183 1.1246 1.4153 0.1844  0.0894  -0.0004 148  TRP F NE1 
16466 C  CE2 . TRP F 148  ? 1.6651 1.1916 1.4636 0.1938  0.0811  -0.0018 148  TRP F CE2 
16467 C  CE3 . TRP F 148  ? 1.6175 1.1839 1.4355 0.1969  0.0662  -0.0094 148  TRP F CE3 
16468 C  CZ2 . TRP F 148  ? 1.6581 1.1889 1.4462 0.2055  0.0787  0.0010  148  TRP F CZ2 
16469 C  CZ3 . TRP F 148  ? 1.6214 1.1925 1.4299 0.2081  0.0640  -0.0067 148  TRP F CZ3 
16470 C  CH2 . TRP F 148  ? 1.7366 1.2902 1.5303 0.2124  0.0700  -0.0017 148  TRP F CH2 
16471 N  N   . VAL F 149  ? 1.3448 0.8934 1.2036 0.1498  0.0711  -0.0257 149  VAL F N   
16472 C  CA  . VAL F 149  ? 1.3348 0.8966 1.2052 0.1459  0.0648  -0.0315 149  VAL F CA  
16473 C  C   . VAL F 149  ? 1.3965 0.9361 1.2547 0.1467  0.0659  -0.0345 149  VAL F C   
16474 O  O   . VAL F 149  ? 1.4746 1.0188 1.3303 0.1522  0.0600  -0.0382 149  VAL F O   
16475 C  CB  . VAL F 149  ? 1.3507 0.9288 1.2437 0.1320  0.0649  -0.0335 149  VAL F CB  
16476 C  CG1 . VAL F 149  ? 1.4122 0.9989 1.3151 0.1272  0.0594  -0.0397 149  VAL F CG1 
16477 C  CG2 . VAL F 149  ? 1.3166 0.9194 1.2218 0.1327  0.0622  -0.0313 149  VAL F CG2 
16478 N  N   . THR F 150  ? 1.4558 0.9705 1.3058 0.1413  0.0738  -0.0330 150  THR F N   
16479 C  CA  . THR F 150  ? 1.5300 1.0213 1.3673 0.1417  0.0754  -0.0358 150  THR F CA  
16480 C  C   . THR F 150  ? 1.4918 0.9707 1.3075 0.1572  0.0735  -0.0345 150  THR F C   
16481 O  O   . THR F 150  ? 1.4949 0.9659 1.3030 0.1610  0.0705  -0.0382 150  THR F O   
16482 C  CB  . THR F 150  ? 1.6190 1.0855 1.4517 0.1326  0.0850  -0.0340 150  THR F CB  
16483 O  OG1 . THR F 150  ? 1.5865 1.0667 1.4403 0.1187  0.0868  -0.0349 150  THR F OG1 
16484 C  CG2 . THR F 150  ? 1.6271 1.0705 1.4493 0.1307  0.0866  -0.0377 150  THR F CG2 
16485 N  N   . ALA F 151  ? 1.1840 0.6615 0.9894 0.1666  0.0751  -0.0294 151  ALA F N   
16486 C  CA  . ALA F 151  ? 1.1530 0.6208 0.9383 0.1821  0.0728  -0.0282 151  ALA F CA  
16487 C  C   . ALA F 151  ? 1.1993 0.6904 0.9907 0.1893  0.0634  -0.0318 151  ALA F C   
16488 O  O   . ALA F 151  ? 1.2314 0.7142 1.0104 0.1982  0.0605  -0.0339 151  ALA F O   
16489 C  CB  . ALA F 151  ? 1.1872 0.6501 0.9611 0.1903  0.0763  -0.0221 151  ALA F CB  
16490 N  N   . ARG F 152  ? 1.6208 1.1407 1.4310 0.1856  0.0588  -0.0325 152  ARG F N   
16491 C  CA  . ARG F 152  ? 1.6501 1.1930 1.4676 0.1913  0.0502  -0.0360 152  ARG F CA  
16492 C  C   . ARG F 152  ? 1.6665 1.2083 1.4886 0.1865  0.0472  -0.0417 152  ARG F C   
16493 O  O   . ARG F 152  ? 1.6218 1.1673 1.4383 0.1949  0.0421  -0.0444 152  ARG F O   
16494 C  CB  . ARG F 152  ? 1.6445 1.2169 1.4815 0.1868  0.0467  -0.0356 152  ARG F CB  
16495 C  CG  . ARG F 152  ? 1.6433 1.2263 1.4756 0.1969  0.0450  -0.0319 152  ARG F CG  
16496 C  CD  . ARG F 152  ? 1.6104 1.2211 1.4622 0.1912  0.0420  -0.0317 152  ARG F CD  
16497 N  NE  . ARG F 152  ? 1.6568 1.2641 1.5167 0.1804  0.0477  -0.0291 152  ARG F NE  
16498 C  CZ  . ARG F 152  ? 1.6082 1.2351 1.4871 0.1712  0.0466  -0.0297 152  ARG F CZ  
16499 N  NH1 . ARG F 152  ? 1.6513 1.3022 1.5430 0.1711  0.0400  -0.0328 152  ARG F NH1 
16500 N  NH2 . ARG F 152  ? 1.5621 1.1841 1.4470 0.1622  0.0524  -0.0272 152  ARG F NH2 
16501 N  N   . ILE F 153  ? 1.5312 1.0680 1.3635 0.1731  0.0503  -0.0436 153  ILE F N   
16502 C  CA  . ILE F 153  ? 1.5589 1.0941 1.3958 0.1678  0.0475  -0.0493 153  ILE F CA  
16503 C  C   . ILE F 153  ? 1.6332 1.1412 1.4493 0.1746  0.0494  -0.0504 153  ILE F C   
16504 O  O   . ILE F 153  ? 1.6228 1.1321 1.4358 0.1789  0.0446  -0.0545 153  ILE F O   
16505 C  CB  . ILE F 153  ? 1.5750 1.1109 1.4276 0.1517  0.0505  -0.0511 153  ILE F CB  
16506 C  CG1 . ILE F 153  ? 1.4845 1.0502 1.3587 0.1458  0.0470  -0.0512 153  ILE F CG1 
16507 C  CG2 . ILE F 153  ? 1.5808 1.1087 1.4346 0.1462  0.0487  -0.0570 153  ILE F CG2 
16508 C  CD1 . ILE F 153  ? 1.4774 1.0662 1.3600 0.1497  0.0386  -0.0549 153  ILE F CD1 
16509 N  N   . ALA F 154  ? 1.6117 1.0942 1.4125 0.1762  0.0566  -0.0466 154  ALA F N   
16510 C  CA  . ALA F 154  ? 1.6055 1.0600 1.3849 0.1830  0.0590  -0.0472 154  ALA F CA  
16511 C  C   . ALA F 154  ? 1.5331 0.9910 1.2990 0.1996  0.0542  -0.0468 154  ALA F C   
16512 O  O   . ALA F 154  ? 1.5353 0.9820 1.2901 0.2056  0.0521  -0.0498 154  ALA F O   
16513 C  CB  . ALA F 154  ? 1.5598 0.9863 1.3255 0.1811  0.0683  -0.0428 154  ALA F CB  
16514 N  N   . ILE F 155  ? 1.3390 0.8125 1.1060 0.2073  0.0522  -0.0432 155  ILE F N   
16515 C  CA  . ILE F 155  ? 1.3327 0.8124 1.0887 0.2230  0.0472  -0.0430 155  ILE F CA  
16516 C  C   . ILE F 155  ? 1.2497 0.7505 1.0164 0.2242  0.0395  -0.0481 155  ILE F C   
16517 O  O   . ILE F 155  ? 1.3286 0.8253 1.0839 0.2347  0.0363  -0.0502 155  ILE F O   
16518 C  CB  . ILE F 155  ? 1.3810 0.8743 1.1374 0.2298  0.0467  -0.0384 155  ILE F CB  
16519 C  CG1 . ILE F 155  ? 1.3635 0.8314 1.1028 0.2329  0.0541  -0.0331 155  ILE F CG1 
16520 C  CG2 . ILE F 155  ? 1.3569 0.8657 1.1087 0.2441  0.0400  -0.0392 155  ILE F CG2 
16521 C  CD1 . ILE F 155  ? 1.3536 0.8335 1.0938 0.2379  0.0542  -0.0286 155  ILE F CD1 
16522 N  N   . PHE F 156  ? 1.4661 0.9895 1.2543 0.2137  0.0366  -0.0504 156  PHE F N   
16523 C  CA  . PHE F 156  ? 1.5687 1.1115 1.3672 0.2141  0.0297  -0.0553 156  PHE F CA  
16524 C  C   . PHE F 156  ? 1.4977 1.0230 1.2891 0.2120  0.0297  -0.0598 156  PHE F C   
16525 O  O   . PHE F 156  ? 1.3987 0.9294 1.1867 0.2191  0.0249  -0.0631 156  PHE F O   
16526 C  CB  . PHE F 156  ? 1.4987 1.0669 1.3208 0.2028  0.0272  -0.0565 156  PHE F CB  
16527 C  CG  . PHE F 156  ? 1.5116 1.0996 1.3417 0.2050  0.0263  -0.0527 156  PHE F CG  
16528 C  CD1 . PHE F 156  ? 1.5030 1.0921 1.3216 0.2180  0.0254  -0.0497 156  PHE F CD1 
16529 C  CD2 . PHE F 156  ? 1.4886 1.0940 1.3375 0.1944  0.0263  -0.0522 156  PHE F CD2 
16530 C  CE1 . PHE F 156  ? 1.4497 1.0568 1.2755 0.2198  0.0243  -0.0466 156  PHE F CE1 
16531 C  CE2 . PHE F 156  ? 1.3913 1.0140 1.2470 0.1963  0.0255  -0.0489 156  PHE F CE2 
16532 C  CZ  . PHE F 156  ? 1.4362 1.0596 1.2803 0.2089  0.0245  -0.0462 156  PHE F CZ  
16533 N  N   . PHE F 157  ? 1.6082 1.1123 1.3971 0.2023  0.0353  -0.0600 157  PHE F N   
16534 C  CA  . PHE F 157  ? 1.6328 1.1189 1.4149 0.1993  0.0356  -0.0646 157  PHE F CA  
16535 C  C   . PHE F 157  ? 1.5948 1.0580 1.3528 0.2125  0.0368  -0.0640 157  PHE F C   
16536 O  O   . PHE F 157  ? 1.5406 0.9975 1.2921 0.2160  0.0339  -0.0682 157  PHE F O   
16537 C  CB  . PHE F 157  ? 1.6792 1.1491 1.4657 0.1848  0.0415  -0.0650 157  PHE F CB  
16538 C  CG  . PHE F 157  ? 1.7551 1.2440 1.5640 0.1715  0.0386  -0.0689 157  PHE F CG  
16539 C  CD1 . PHE F 157  ? 1.6551 1.1535 1.4697 0.1706  0.0326  -0.0746 157  PHE F CD1 
16540 C  CD2 . PHE F 157  ? 1.8636 1.3609 1.6874 0.1604  0.0417  -0.0668 157  PHE F CD2 
16541 C  CE1 . PHE F 157  ? 1.7081 1.2239 1.5426 0.1590  0.0296  -0.0782 157  PHE F CE1 
16542 C  CE2 . PHE F 157  ? 1.7821 1.2973 1.6263 0.1488  0.0388  -0.0704 157  PHE F CE2 
16543 C  CZ  . PHE F 157  ? 1.7409 1.2653 1.5903 0.1482  0.0326  -0.0761 157  PHE F CZ  
16544 N  N   . ILE F 158  ? 1.4294 0.8794 1.1733 0.2203  0.0411  -0.0588 158  ILE F N   
16545 C  CA  . ILE F 158  ? 1.4094 0.8387 1.1296 0.2344  0.0420  -0.0578 158  ILE F CA  
16546 C  C   . ILE F 158  ? 1.3979 0.8467 1.1177 0.2469  0.0346  -0.0598 158  ILE F C   
16547 O  O   . ILE F 158  ? 1.4852 0.9226 1.1916 0.2555  0.0330  -0.0623 158  ILE F O   
16548 C  CB  . ILE F 158  ? 1.3829 0.7961 1.0887 0.2404  0.0478  -0.0517 158  ILE F CB  
16549 C  CG1 . ILE F 158  ? 1.4581 0.8450 1.1593 0.2294  0.0562  -0.0501 158  ILE F CG1 
16550 C  CG2 . ILE F 158  ? 1.3503 0.7529 1.0350 0.2563  0.0469  -0.0500 158  ILE F CG2 
16551 C  CD1 . ILE F 158  ? 1.5873 0.9470 1.2757 0.2274  0.0587  -0.0536 158  ILE F CD1 
16552 N  N   . ILE F 159  ? 1.3565 0.8349 1.0912 0.2480  0.0303  -0.0588 159  ILE F N   
16553 C  CA  . ILE F 159  ? 1.3019 0.8013 1.0382 0.2590  0.0236  -0.0607 159  ILE F CA  
16554 C  C   . ILE F 159  ? 1.4189 0.9256 1.1627 0.2552  0.0193  -0.0665 159  ILE F C   
16555 O  O   . ILE F 159  ? 1.4436 0.9492 1.1781 0.2653  0.0160  -0.0690 159  ILE F O   
16556 C  CB  . ILE F 159  ? 1.2986 0.8277 1.0503 0.2592  0.0205  -0.0584 159  ILE F CB  
16557 C  CG1 . ILE F 159  ? 1.3878 0.9098 1.1285 0.2670  0.0237  -0.0529 159  ILE F CG1 
16558 C  CG2 . ILE F 159  ? 1.1415 0.6956 0.8997 0.2672  0.0135  -0.0612 159  ILE F CG2 
16559 C  CD1 . ILE F 159  ? 1.3412 0.8908 1.0955 0.2676  0.0207  -0.0507 159  ILE F CD1 
16560 N  N   . TRP F 160  ? 1.5590 1.0732 1.3193 0.2407  0.0192  -0.0689 160  TRP F N   
16561 C  CA  . TRP F 160  ? 1.5320 1.0548 1.3005 0.2365  0.0147  -0.0746 160  TRP F CA  
16562 C  C   . TRP F 160  ? 1.4858 0.9812 1.2378 0.2386  0.0164  -0.0777 160  TRP F C   
16563 O  O   . TRP F 160  ? 1.5542 1.0524 1.3021 0.2449  0.0123  -0.0815 160  TRP F O   
16564 C  CB  . TRP F 160  ? 1.5463 1.0821 1.3355 0.2206  0.0144  -0.0763 160  TRP F CB  
16565 C  CG  . TRP F 160  ? 1.4908 1.0549 1.2970 0.2183  0.0121  -0.0738 160  TRP F CG  
16566 C  CD1 . TRP F 160  ? 1.4097 0.9936 1.2175 0.2282  0.0085  -0.0722 160  TRP F CD1 
16567 C  CD2 . TRP F 160  ? 1.4433 1.0188 1.2671 0.2054  0.0134  -0.0729 160  TRP F CD2 
16568 N  NE1 . TRP F 160  ? 1.3934 0.9995 1.2183 0.2219  0.0076  -0.0703 160  TRP F NE1 
16569 C  CE2 . TRP F 160  ? 1.3799 0.9812 1.2146 0.2082  0.0105  -0.0706 160  TRP F CE2 
16570 C  CE3 . TRP F 160  ? 1.4347 1.0013 1.2663 0.1916  0.0168  -0.0740 160  TRP F CE3 
16571 C  CZ2 . TRP F 160  ? 1.3553 0.9727 1.2073 0.1982  0.0110  -0.0692 160  TRP F CZ2 
16572 C  CZ3 . TRP F 160  ? 1.3446 0.9283 1.1941 0.1819  0.0172  -0.0726 160  TRP F CZ3 
16573 C  CH2 . TRP F 160  ? 1.3287 0.9371 1.1878 0.1854  0.0143  -0.0701 160  TRP F CH2 
16574 N  N   . SER F 161  ? 1.4707 0.9389 1.2129 0.2333  0.0226  -0.0763 161  SER F N   
16575 C  CA  . SER F 161  ? 1.4800 0.9201 1.2059 0.2345  0.0248  -0.0793 161  SER F CA  
16576 C  C   . SER F 161  ? 1.5101 0.9388 1.2150 0.2518  0.0241  -0.0783 161  SER F C   
16577 O  O   . SER F 161  ? 1.5980 1.0167 1.2932 0.2566  0.0221  -0.0822 161  SER F O   
16578 C  CB  . SER F 161  ? 1.4894 0.9030 1.2096 0.2248  0.0323  -0.0775 161  SER F CB  
16579 O  OG  . SER F 161  ? 1.4725 0.8968 1.2125 0.2087  0.0328  -0.0791 161  SER F OG  
16580 N  N   . ALA F 162  ? 1.2912 0.7213 0.9887 0.2615  0.0255  -0.0732 162  ALA F N   
16581 C  CA  . ALA F 162  ? 1.3103 0.7403 0.9931 0.2744  0.0242  -0.0710 162  ALA F CA  
16582 C  C   . ALA F 162  ? 1.2958 0.7493 0.9844 0.2821  0.0171  -0.0743 162  ALA F C   
16583 O  O   . ALA F 162  ? 1.3750 0.8244 1.0529 0.2888  0.0155  -0.0756 162  ALA F O   
16584 C  CB  . ALA F 162  ? 1.2083 0.6432 0.8865 0.2804  0.0263  -0.0645 162  ALA F CB  
16585 N  N   . LEU F 163  ? 1.4840 0.9623 1.1895 0.2812  0.0131  -0.0758 163  LEU F N   
16586 C  CA  . LEU F 163  ? 1.5045 1.0065 1.2167 0.2879  0.0067  -0.0788 163  LEU F CA  
16587 C  C   . LEU F 163  ? 1.5119 1.0066 1.2236 0.2845  0.0047  -0.0849 163  LEU F C   
16588 O  O   . LEU F 163  ? 1.5132 1.0133 1.2192 0.2918  0.0016  -0.0866 163  LEU F O   
16589 C  CB  . LEU F 163  ? 1.5177 1.0504 1.2504 0.2845  0.0033  -0.0784 163  LEU F CB  
16590 C  CG  . LEU F 163  ? 1.3783 0.9253 1.1117 0.2927  0.0029  -0.0739 163  LEU F CG  
16591 C  CD1 . LEU F 163  ? 1.5225 1.0985 1.2783 0.2840  0.0006  -0.0732 163  LEU F CD1 
16592 C  CD2 . LEU F 163  ? 1.4445 1.0055 1.1717 0.3047  -0.0007 -0.0735 163  LEU F CD2 
16593 N  N   . ALA F 164  ? 1.4541 0.9428 1.1751 0.2701  0.0061  -0.0871 164  ALA F N   
16594 C  CA  . ALA F 164  ? 1.5178 1.0032 1.2408 0.2649  0.0036  -0.0930 164  ALA F CA  
16595 C  C   . ALA F 164  ? 1.5638 1.0177 1.2646 0.2710  0.0060  -0.0949 164  ALA F C   
16596 O  O   . ALA F 164  ? 1.5567 1.0117 1.2527 0.2760  0.0027  -0.0987 164  ALA F O   
16597 C  CB  . ALA F 164  ? 1.5659 1.0540 1.3051 0.2473  0.0044  -0.0948 164  ALA F CB  
16598 N  N   . LEU F 165  ? 1.5583 0.9880 1.2474 0.2688  0.0120  -0.0916 165  LEU F N   
16599 C  CA  . LEU F 165  ? 1.4075 0.8129 1.0792 0.2701  0.0147  -0.0921 165  LEU F CA  
16600 C  C   . LEU F 165  ? 1.5008 0.9132 1.1608 0.2838  0.0128  -0.0895 165  LEU F C   
16601 O  O   . LEU F 165  ? 1.6462 1.0484 1.2953 0.2873  0.0120  -0.0919 165  LEU F O   
16602 C  CB  . LEU F 165  ? 1.3147 0.6945 0.9779 0.2634  0.0220  -0.0886 165  LEU F CB  
16603 C  CG  . LEU F 165  ? 1.2902 0.6581 0.9628 0.2486  0.0248  -0.0916 165  LEU F CG  
16604 C  CD1 . LEU F 165  ? 1.4342 0.7766 1.0973 0.2423  0.0327  -0.0878 165  LEU F CD1 
16605 C  CD2 . LEU F 165  ? 1.4262 0.7874 1.1006 0.2427  0.0219  -0.0990 165  LEU F CD2 
16606 N  N   . THR F 166  ? 1.3184 0.7483 0.9804 0.2916  0.0119  -0.0849 166  THR F N   
16607 C  CA  . THR F 166  ? 1.3907 0.8294 1.0427 0.3045  0.0096  -0.0827 166  THR F CA  
16608 C  C   . THR F 166  ? 1.4308 0.8892 1.0892 0.3094  0.0037  -0.0870 166  THR F C   
16609 O  O   . THR F 166  ? 1.5430 0.9980 1.1901 0.3169  0.0024  -0.0878 166  THR F O   
16610 C  CB  . THR F 166  ? 1.3473 0.8012 1.0011 0.3108  0.0097  -0.0772 166  THR F CB  
16611 O  OG1 . THR F 166  ? 1.2515 0.6851 0.8969 0.3072  0.0155  -0.0729 166  THR F OG1 
16612 C  CG2 . THR F 166  ? 1.5031 0.9678 1.1474 0.3241  0.0069  -0.0754 166  THR F CG2 
16613 N  N   . LEU F 167  ? 1.6124 1.0914 1.2885 0.3052  0.0003  -0.0897 167  LEU F N   
16614 C  CA  . LEU F 167  ? 1.7558 1.2538 1.4386 0.3092  -0.0050 -0.0938 167  LEU F CA  
16615 C  C   . LEU F 167  ? 1.8021 1.2829 1.4780 0.3056  -0.0054 -0.0990 167  LEU F C   
16616 O  O   . LEU F 167  ? 1.8107 1.2967 1.4813 0.3124  -0.0081 -0.1010 167  LEU F O   
16617 C  CB  . LEU F 167  ? 1.7139 1.2362 1.4169 0.3047  -0.0083 -0.0956 167  LEU F CB  
16618 C  CG  . LEU F 167  ? 1.7187 1.2665 1.4304 0.3105  -0.0099 -0.0916 167  LEU F CG  
16619 C  CD1 . LEU F 167  ? 1.7308 1.3014 1.4622 0.3056  -0.0131 -0.0939 167  LEU F CD1 
16620 C  CD2 . LEU F 167  ? 1.6725 1.2336 1.3775 0.3223  -0.0124 -0.0904 167  LEU F CD2 
16621 N  N   . ARG F 168  ? 1.6861 1.1463 1.3620 0.2948  -0.0026 -0.1013 168  ARG F N   
16622 C  CA  . ARG F 168  ? 1.5733 1.0159 1.2424 0.2907  -0.0030 -0.1066 168  ARG F CA  
16623 C  C   . ARG F 168  ? 1.7127 1.1355 1.3617 0.2971  -0.0004 -0.1049 168  ARG F C   
16624 O  O   . ARG F 168  ? 1.8737 1.2926 1.5157 0.3004  -0.0025 -0.1083 168  ARG F O   
16625 C  CB  . ARG F 168  ? 1.4361 0.8612 1.1101 0.2769  -0.0004 -0.1095 168  ARG F CB  
16626 C  CG  . ARG F 168  ? 1.4673 0.8814 1.1400 0.2710  -0.0026 -0.1165 168  ARG F CG  
16627 C  CD  . ARG F 168  ? 1.4794 0.8757 1.1570 0.2568  -0.0001 -0.1196 168  ARG F CD  
16628 N  NE  . ARG F 168  ? 1.6773 1.0473 1.3429 0.2530  0.0065  -0.1162 168  ARG F NE  
16629 C  CZ  . ARG F 168  ? 1.7854 1.1334 1.4499 0.2410  0.0098  -0.1191 168  ARG F CZ  
16630 N  NH1 . ARG F 168  ? 1.7337 1.0878 1.4111 0.2295  0.0067  -0.1247 168  ARG F NH1 
16631 N  NH2 . ARG F 168  ? 1.7328 1.0580 1.3861 0.2383  0.0163  -0.1155 168  ARG F NH2 
16632 N  N   . ALA F 169  ? 1.5560 0.9663 1.1952 0.2992  0.0042  -0.0995 169  ALA F N   
16633 C  CA  . ALA F 169  ? 1.5721 0.9636 1.1916 0.3060  0.0067  -0.0975 169  ALA F CA  
16634 C  C   . ALA F 169  ? 1.6493 1.0580 1.2639 0.3192  0.0028  -0.0967 169  ALA F C   
16635 O  O   . ALA F 169  ? 1.7443 1.1418 1.3457 0.3243  0.0026  -0.0982 169  ALA F O   
16636 C  CB  . ALA F 169  ? 1.4762 0.8528 1.0865 0.3061  0.0122  -0.0916 169  ALA F CB  
16637 N  N   . TRP F 170  ? 1.8696 1.3056 1.4949 0.3248  -0.0002 -0.0945 170  TRP F N   
16638 C  CA  . TRP F 170  ? 1.9734 1.4283 1.5962 0.3366  -0.0040 -0.0941 170  TRP F CA  
16639 C  C   . TRP F 170  ? 2.0692 1.5329 1.6972 0.3363  -0.0080 -0.0997 170  TRP F C   
16640 O  O   . TRP F 170  ? 2.1297 1.5968 1.7492 0.3450  -0.0099 -0.1004 170  TRP F O   
16641 C  CB  . TRP F 170  ? 1.9806 1.4633 1.6150 0.3412  -0.0062 -0.0908 170  TRP F CB  
16642 C  CG  . TRP F 170  ? 2.0212 1.4982 1.6469 0.3458  -0.0033 -0.0850 170  TRP F CG  
16643 C  CD1 . TRP F 170  ? 1.9767 1.4281 1.5842 0.3479  0.0009  -0.0823 170  TRP F CD1 
16644 C  CD2 . TRP F 170  ? 2.0794 1.5766 1.7136 0.3489  -0.0043 -0.0813 170  TRP F CD2 
16645 N  NE1 . TRP F 170  ? 1.9463 1.4007 1.5501 0.3524  0.0024  -0.0771 170  TRP F NE1 
16646 C  CE2 . TRP F 170  ? 1.9930 1.4754 1.6131 0.3531  -0.0008 -0.0765 170  TRP F CE2 
16647 C  CE3 . TRP F 170  ? 1.9509 1.4770 1.6030 0.3485  -0.0078 -0.0816 170  TRP F CE3 
16648 C  CZ2 . TRP F 170  ? 1.9592 1.4549 1.5823 0.3569  -0.0010 -0.0723 170  TRP F CZ2 
16649 C  CZ3 . TRP F 170  ? 1.8455 1.3848 1.5010 0.3520  -0.0079 -0.0775 170  TRP F CZ3 
16650 C  CH2 . TRP F 170  ? 1.8736 1.3978 1.5147 0.3562  -0.0046 -0.0729 170  TRP F CH2 
16651 N  N   . SER F 171  ? 2.1029 1.5702 1.7442 0.3267  -0.0094 -0.1038 171  SER F N   
16652 C  CA  . SER F 171  ? 2.0852 1.5597 1.7308 0.3260  -0.0132 -0.1094 171  SER F CA  
16653 C  C   . SER F 171  ? 2.1192 1.5673 1.7494 0.3247  -0.0118 -0.1125 171  SER F C   
16654 O  O   . SER F 171  ? 2.1312 1.5829 1.7570 0.3297  -0.0144 -0.1155 171  SER F O   
16655 C  CB  . SER F 171  ? 2.0590 1.5437 1.7221 0.3161  -0.0152 -0.1130 171  SER F CB  
16656 O  OG  . SER F 171  ? 2.1951 1.6876 1.8622 0.3157  -0.0191 -0.1184 171  SER F OG  
16657 N  N   . ARG F 172  ? 1.8413 1.2627 1.4634 0.3178  -0.0074 -0.1119 172  ARG F N   
16658 C  CA  . ARG F 172  ? 1.8042 1.1993 1.4107 0.3166  -0.0055 -0.1145 172  ARG F CA  
16659 C  C   . ARG F 172  ? 1.9228 1.3138 1.5126 0.3290  -0.0049 -0.1114 172  ARG F C   
16660 O  O   . ARG F 172  ? 1.9625 1.3458 1.5426 0.3327  -0.0062 -0.1144 172  ARG F O   
16661 C  CB  . ARG F 172  ? 1.8192 1.1873 1.4211 0.3062  -0.0004 -0.1141 172  ARG F CB  
16662 C  CG  . ARG F 172  ? 1.7257 1.0955 1.3434 0.2932  -0.0007 -0.1173 172  ARG F CG  
16663 C  CD  . ARG F 172  ? 1.7806 1.1448 1.4010 0.2865  -0.0037 -0.1247 172  ARG F CD  
16664 N  NE  . ARG F 172  ? 1.8400 1.2037 1.4744 0.2736  -0.0039 -0.1281 172  ARG F NE  
16665 C  CZ  . ARG F 172  ? 1.8856 1.2273 1.5184 0.2628  0.0004  -0.1286 172  ARG F CZ  
16666 N  NH1 . ARG F 172  ? 1.8480 1.1658 1.4657 0.2630  0.0056  -0.1259 172  ARG F NH1 
16667 N  NH2 . ARG F 172  ? 1.8647 1.2088 1.5114 0.2515  -0.0004 -0.1319 172  ARG F NH2 
16668 N  N   . GLN F 173  ? 1.8329 1.2291 1.4189 0.3358  -0.0032 -0.1056 173  GLN F N   
16669 C  CA  . GLN F 173  ? 1.8622 1.2562 1.4325 0.3482  -0.0029 -0.1025 173  GLN F CA  
16670 C  C   . GLN F 173  ? 1.8703 1.2886 1.4446 0.3574  -0.0078 -0.1041 173  GLN F C   
16671 O  O   . GLN F 173  ? 1.9671 1.3814 1.5278 0.3669  -0.0082 -0.1034 173  GLN F O   
16672 C  CB  . GLN F 173  ? 1.8345 1.2307 1.4010 0.3531  -0.0005 -0.0962 173  GLN F CB  
16673 C  CG  . GLN F 173  ? 1.8209 1.1888 1.3771 0.3470  0.0053  -0.0936 173  GLN F CG  
16674 C  CD  . GLN F 173  ? 1.8439 1.2158 1.3976 0.3515  0.0075  -0.0874 173  GLN F CD  
16675 O  OE1 . GLN F 173  ? 1.8344 1.2290 1.3920 0.3603  0.0045  -0.0851 173  GLN F OE1 
16676 N  NE2 . GLN F 173  ? 1.9632 1.3130 1.5103 0.3453  0.0128  -0.0848 173  GLN F NE2 
16677 N  N   . GLN F 174  ? 2.1469 1.5901 1.7393 0.3547  -0.0114 -0.1062 174  GLN F N   
16678 C  CA  . GLN F 174  ? 2.1947 1.6612 1.7918 0.3624  -0.0157 -0.1079 174  GLN F CA  
16679 C  C   . GLN F 174  ? 2.2565 1.7112 1.8450 0.3628  -0.0169 -0.1127 174  GLN F C   
16680 O  O   . GLN F 174  ? 2.2664 1.7323 1.8511 0.3717  -0.0192 -0.1133 174  GLN F O   
16681 C  CB  . GLN F 174  ? 2.1986 1.6924 1.8170 0.3581  -0.0188 -0.1093 174  GLN F CB  
16682 C  CG  . GLN F 174  ? 2.2008 1.7237 1.8259 0.3671  -0.0224 -0.1090 174  GLN F CG  
16683 C  CD  . GLN F 174  ? 2.1852 1.7332 1.8306 0.3620  -0.0252 -0.1110 174  GLN F CD  
16684 O  OE1 . GLN F 174  ? 2.1635 1.7062 1.8172 0.3521  -0.0252 -0.1138 174  GLN F OE1 
16685 N  NE2 . GLN F 174  ? 2.1371 1.7126 1.7908 0.3687  -0.0277 -0.1098 174  GLN F NE2 
16686 N  N   . ASP F 175  ? 2.0755 1.5075 1.6609 0.3533  -0.0152 -0.1162 175  ASP F N   
16687 C  CA  . ASP F 175  ? 2.0200 1.4381 1.5963 0.3528  -0.0163 -0.1210 175  ASP F CA  
16688 C  C   . ASP F 175  ? 1.9881 1.3845 1.5430 0.3600  -0.0137 -0.1192 175  ASP F C   
16689 O  O   . ASP F 175  ? 1.9035 1.2861 1.4488 0.3602  -0.0142 -0.1230 175  ASP F O   
16690 C  CB  . ASP F 175  ? 1.9886 1.3904 1.5696 0.3393  -0.0156 -0.1258 175  ASP F CB  
16691 C  CG  . ASP F 175  ? 2.0131 1.4355 1.6147 0.3322  -0.0185 -0.1280 175  ASP F CG  
16692 O  OD1 . ASP F 175  ? 1.9897 1.4389 1.6018 0.3376  -0.0207 -0.1258 175  ASP F OD1 
16693 O  OD2 . ASP F 175  ? 2.0575 1.4693 1.6647 0.3210  -0.0184 -0.1320 175  ASP F OD2 
16694 N  N   . ALA F 176  ? 1.9529 1.3456 1.4996 0.3660  -0.0110 -0.1137 176  ALA F N   
16695 C  CA  . ALA F 176  ? 1.9644 1.3365 1.4899 0.3736  -0.0085 -0.1115 176  ALA F CA  
16696 C  C   . ALA F 176  ? 1.9993 1.3889 1.5194 0.3878  -0.0108 -0.1091 176  ALA F C   
16697 O  O   . ALA F 176  ? 2.0135 1.3970 1.5221 0.3942  -0.0117 -0.1109 176  ALA F O   
16698 C  CB  . ALA F 176  ? 1.9008 1.2538 1.4184 0.3708  -0.0036 -0.1071 176  ALA F CB  
16699 N  N   . GLY F 177  ? 1.7833 1.1947 1.3116 0.3926  -0.0118 -0.1052 177  GLY F N   
16700 C  CA  . GLY F 177  ? 1.8033 1.2330 1.3278 0.4056  -0.0141 -0.1031 177  GLY F CA  
16701 C  C   . GLY F 177  ? 1.7751 1.2291 1.3116 0.4083  -0.0152 -0.0993 177  GLY F C   
16702 O  O   . GLY F 177  ? 1.7208 1.1724 1.2639 0.4016  -0.0134 -0.0973 177  GLY F O   
16703 N  N   . GLY F 178  ? 2.2268 1.7046 1.7662 0.4180  -0.0183 -0.0986 178  GLY F N   
16704 C  CA  . GLY F 178  ? 2.2570 1.7600 1.8076 0.4215  -0.0198 -0.0955 178  GLY F CA  
16705 C  C   . GLY F 178  ? 2.3732 1.8960 1.9459 0.4125  -0.0214 -0.0970 178  GLY F C   
16706 O  O   . GLY F 178  ? 2.4747 2.0016 2.0549 0.4084  -0.0204 -0.0944 178  GLY F O   
16707 N  N   . ASP F 179  ? 3.0289 2.5640 2.6116 0.4097  -0.0238 -0.1011 179  ASP F N   
16708 C  CA  . ASP F 179  ? 3.0579 2.6109 2.6610 0.4011  -0.0254 -0.1029 179  ASP F CA  
16709 C  C   . ASP F 179  ? 3.0668 2.6537 2.6843 0.4055  -0.0282 -0.1017 179  ASP F C   
16710 O  O   . ASP F 179  ? 2.9659 2.5681 2.5997 0.3992  -0.0289 -0.1015 179  ASP F O   
16711 C  CB  . ASP F 179  ? 3.0792 2.6276 2.6857 0.3951  -0.0266 -0.1081 179  ASP F CB  
16712 C  CG  . ASP F 179  ? 3.1764 2.7388 2.7814 0.4028  -0.0292 -0.1104 179  ASP F CG  
16713 O  OD1 . ASP F 179  ? 3.2218 2.7938 2.8208 0.4130  -0.0297 -0.1080 179  ASP F OD1 
16714 O  OD2 . ASP F 179  ? 3.1798 2.7437 2.7897 0.3986  -0.0307 -0.1146 179  ASP F OD2 
16715 N  N   . ALA F 180  ? 2.2537 1.8528 1.8658 0.4161  -0.0297 -0.1009 180  ALA F N   
16716 C  CA  . ALA F 180  ? 2.2247 1.8565 1.8506 0.4201  -0.0323 -0.1003 180  ALA F CA  
16717 C  C   . ALA F 180  ? 2.2419 1.8821 1.8685 0.4240  -0.0320 -0.0960 180  ALA F C   
16718 O  O   . ALA F 180  ? 2.1562 1.8162 1.7984 0.4201  -0.0331 -0.0951 180  ALA F O   
16719 C  CB  . ALA F 180  ? 2.2642 1.9065 1.8849 0.4294  -0.0340 -0.1018 180  ALA F CB  
16720 N  N   . LYS F 181  ? 3.0268 2.6519 2.6362 0.4316  -0.0307 -0.0934 181  LYS F N   
16721 C  CA  . LYS F 181  ? 3.1003 2.7327 2.7085 0.4362  -0.0308 -0.0895 181  LYS F CA  
16722 C  C   . LYS F 181  ? 2.9618 2.5859 2.5756 0.4274  -0.0289 -0.0875 181  LYS F C   
16723 O  O   . LYS F 181  ? 2.8312 2.4741 2.4572 0.4259  -0.0300 -0.0859 181  LYS F O   
16724 C  CB  . LYS F 181  ? 3.1900 2.8055 2.7766 0.4464  -0.0297 -0.0873 181  LYS F CB  
16725 C  CG  . LYS F 181  ? 3.1202 2.7458 2.7010 0.4564  -0.0317 -0.0889 181  LYS F CG  
16726 C  CD  . LYS F 181  ? 3.1265 2.7843 2.7184 0.4624  -0.0347 -0.0884 181  LYS F CD  
16727 C  CE  . LYS F 181  ? 3.2170 2.8743 2.8011 0.4686  -0.0346 -0.0847 181  LYS F CE  
16728 N  NZ  . LYS F 181  ? 3.1894 2.8780 2.7839 0.4746  -0.0377 -0.0846 181  LYS F NZ  
16729 N  N   . LYS F 182  ? 2.1947 1.7907 1.7998 0.4213  -0.0258 -0.0876 182  LYS F N   
16730 C  CA  . LYS F 182  ? 2.0714 1.6564 1.6806 0.4125  -0.0234 -0.0858 182  LYS F CA  
16731 C  C   . LYS F 182  ? 1.9744 1.5506 1.5920 0.4013  -0.0226 -0.0893 182  LYS F C   
16732 O  O   . LYS F 182  ? 2.0251 1.6066 1.6464 0.4006  -0.0244 -0.0931 182  LYS F O   
16733 C  CB  . LYS F 182  ? 2.2600 1.8179 1.8502 0.4153  -0.0199 -0.0823 182  LYS F CB  
16734 C  CG  . LYS F 182  ? 2.3442 1.9098 1.9251 0.4266  -0.0209 -0.0789 182  LYS F CG  
16735 C  CD  . LYS F 182  ? 2.3884 1.9273 1.9516 0.4282  -0.0171 -0.0752 182  LYS F CD  
16736 C  CE  . LYS F 182  ? 2.3988 1.9086 1.9437 0.4294  -0.0144 -0.0761 182  LYS F CE  
16737 N  NZ  . LYS F 182  ? 2.3512 1.8658 1.8856 0.4408  -0.0166 -0.0771 182  LYS F NZ  
16738 N  N   . LEU F 183  ? 1.9344 1.4971 1.5546 0.3925  -0.0200 -0.0881 183  LEU F N   
16739 C  CA  . LEU F 183  ? 1.9501 1.5020 1.5776 0.3811  -0.0189 -0.0913 183  LEU F CA  
16740 C  C   . LEU F 183  ? 1.9310 1.5081 1.5781 0.3768  -0.0222 -0.0945 183  LEU F C   
16741 O  O   . LEU F 183  ? 1.8945 1.4652 1.5481 0.3681  -0.0221 -0.0979 183  LEU F O   
16742 C  CB  . LEU F 183  ? 1.8947 1.4204 1.5081 0.3799  -0.0173 -0.0941 183  LEU F CB  
16743 C  CG  . LEU F 183  ? 1.8980 1.3972 1.4906 0.3843  -0.0137 -0.0911 183  LEU F CG  
16744 C  CD1 . LEU F 183  ? 1.9599 1.4375 1.5392 0.3844  -0.0129 -0.0943 183  LEU F CD1 
16745 C  CD2 . LEU F 183  ? 1.8645 1.3472 1.4565 0.3766  -0.0098 -0.0884 183  LEU F CD2 
16746 N  N   . ALA F 184  ? 2.8876 2.4929 2.5440 0.3826  -0.0251 -0.0937 184  ALA F N   
16747 C  CA  . ALA F 184  ? 2.8773 2.5088 2.5529 0.3788  -0.0279 -0.0960 184  ALA F CA  
16748 C  C   . ALA F 184  ? 2.8020 2.4573 2.4898 0.3799  -0.0290 -0.0930 184  ALA F C   
16749 O  O   . ALA F 184  ? 2.7662 2.4368 2.4704 0.3733  -0.0300 -0.0939 184  ALA F O   
16750 C  CB  . ALA F 184  ? 2.8998 2.5443 2.5756 0.3844  -0.0305 -0.0990 184  ALA F CB  
16751 N  N   . THR F 185  ? 2.7438 2.4025 2.4238 0.3881  -0.0290 -0.0897 185  THR F N   
16752 C  CA  . THR F 185  ? 2.7414 2.4199 2.4310 0.3892  -0.0300 -0.0868 185  THR F CA  
16753 C  C   . THR F 185  ? 2.6927 2.3553 2.3793 0.3844  -0.0272 -0.0836 185  THR F C   
16754 O  O   . THR F 185  ? 2.7535 2.4300 2.4529 0.3802  -0.0276 -0.0823 185  THR F O   
16755 C  CB  . THR F 185  ? 2.7970 2.4878 2.4796 0.4006  -0.0317 -0.0851 185  THR F CB  
16756 O  OG1 . THR F 185  ? 2.8601 2.5623 2.5432 0.4053  -0.0337 -0.0880 185  THR F OG1 
16757 C  CG2 . THR F 185  ? 2.7941 2.5099 2.4890 0.4015  -0.0335 -0.0832 185  THR F CG2 
16758 N  N   . ARG F 186  ? 2.1222 1.7559 1.7922 0.3848  -0.0241 -0.0824 186  ARG F N   
16759 C  CA  . ARG F 186  ? 2.1866 1.8026 1.8527 0.3797  -0.0207 -0.0793 186  ARG F CA  
16760 C  C   . ARG F 186  ? 2.0571 1.6724 1.7373 0.3679  -0.0198 -0.0811 186  ARG F C   
16761 O  O   . ARG F 186  ? 1.9960 1.6148 1.6837 0.3634  -0.0188 -0.0788 186  ARG F O   
16762 C  CB  . ARG F 186  ? 2.3133 1.8973 1.9588 0.3816  -0.0172 -0.0782 186  ARG F CB  
16763 C  CG  . ARG F 186  ? 2.3585 1.9404 1.9881 0.3936  -0.0178 -0.0763 186  ARG F CG  
16764 C  CD  . ARG F 186  ? 2.2802 1.8320 1.8905 0.3948  -0.0135 -0.0731 186  ARG F CD  
16765 N  NE  . ARG F 186  ? 2.3219 1.8474 1.9237 0.3894  -0.0107 -0.0753 186  ARG F NE  
16766 C  CZ  . ARG F 186  ? 2.3750 1.8717 1.9592 0.3896  -0.0066 -0.0734 186  ARG F CZ  
16767 N  NH1 . ARG F 186  ? 2.4603 1.9497 2.0326 0.3955  -0.0048 -0.0690 186  ARG F NH1 
16768 N  NH2 . ARG F 186  ? 2.3600 1.8346 1.9383 0.3838  -0.0043 -0.0760 186  ARG F NH2 
16769 N  N   . MET F 187  ? 1.9587 1.5691 1.6422 0.3630  -0.0203 -0.0852 187  MET F N   
16770 C  CA  . MET F 187  ? 1.9458 1.5564 1.6428 0.3521  -0.0200 -0.0874 187  MET F CA  
16771 C  C   . MET F 187  ? 1.8521 1.4933 1.5684 0.3506  -0.0229 -0.0877 187  MET F C   
16772 O  O   . MET F 187  ? 1.8217 1.4656 1.5494 0.3427  -0.0223 -0.0877 187  MET F O   
16773 C  CB  . MET F 187  ? 2.0513 1.6507 1.7466 0.3480  -0.0205 -0.0923 187  MET F CB  
16774 C  CG  . MET F 187  ? 2.0704 1.6383 1.7472 0.3482  -0.0174 -0.0925 187  MET F CG  
16775 S  SD  . MET F 187  ? 2.0985 1.6539 1.7729 0.3436  -0.0185 -0.0988 187  MET F SD  
16776 C  CE  . MET F 187  ? 1.9460 1.4952 1.6337 0.3296  -0.0175 -0.1012 187  MET F CE  
16777 N  N   . ARG F 188  ? 1.8351 1.4993 1.5552 0.3579  -0.0260 -0.0879 188  ARG F N   
16778 C  CA  . ARG F 188  ? 1.7692 1.4631 1.5073 0.3564  -0.0286 -0.0881 188  ARG F CA  
16779 C  C   . ARG F 188  ? 1.7568 1.4571 1.4986 0.3563  -0.0278 -0.0840 188  ARG F C   
16780 O  O   . ARG F 188  ? 1.8407 1.5535 1.5968 0.3502  -0.0282 -0.0838 188  ARG F O   
16781 C  CB  . ARG F 188  ? 1.8056 1.5215 1.5461 0.3640  -0.0316 -0.0894 188  ARG F CB  
16782 C  CG  . ARG F 188  ? 1.7441 1.4909 1.5037 0.3618  -0.0340 -0.0902 188  ARG F CG  
16783 C  CD  . ARG F 188  ? 1.8566 1.6212 1.6194 0.3667  -0.0364 -0.0928 188  ARG F CD  
16784 N  NE  . ARG F 188  ? 1.9953 1.7613 1.7466 0.3768  -0.0369 -0.0915 188  ARG F NE  
16785 C  CZ  . ARG F 188  ? 1.9707 1.7239 1.7086 0.3823  -0.0367 -0.0928 188  ARG F CZ  
16786 N  NH1 . ARG F 188  ? 2.0232 1.7609 1.7571 0.3786  -0.0360 -0.0957 188  ARG F NH1 
16787 N  NH2 . ARG F 188  ? 1.9316 1.6877 1.6596 0.3918  -0.0373 -0.0914 188  ARG F NH2 
16788 N  N   . ARG F 189  ? 1.5391 1.2310 1.2676 0.3633  -0.0267 -0.0808 189  ARG F N   
16789 C  CA  . ARG F 189  ? 1.5294 1.2261 1.2597 0.3637  -0.0261 -0.0770 189  ARG F CA  
16790 C  C   . ARG F 189  ? 1.4616 1.1389 1.1917 0.3553  -0.0225 -0.0754 189  ARG F C   
16791 O  O   . ARG F 189  ? 1.4557 1.1423 1.1954 0.3515  -0.0223 -0.0735 189  ARG F O   
16792 C  CB  . ARG F 189  ? 1.6770 1.3684 1.3917 0.3737  -0.0259 -0.0742 189  ARG F CB  
16793 C  CG  . ARG F 189  ? 1.7195 1.4289 1.4333 0.3825  -0.0292 -0.0758 189  ARG F CG  
16794 C  CD  . ARG F 189  ? 1.7158 1.4169 1.4124 0.3926  -0.0290 -0.0732 189  ARG F CD  
16795 N  NE  . ARG F 189  ? 1.6720 1.3410 1.3506 0.3929  -0.0255 -0.0720 189  ARG F NE  
16796 C  CZ  . ARG F 189  ? 1.6566 1.3123 1.3172 0.4013  -0.0247 -0.0699 189  ARG F CZ  
16797 N  NH1 . ARG F 189  ? 1.5455 1.2170 1.2033 0.4105  -0.0273 -0.0689 189  ARG F NH1 
16798 N  NH2 . ARG F 189  ? 1.8050 1.4308 1.4500 0.4004  -0.0210 -0.0689 189  ARG F NH2 
16799 N  N   . LEU F 190  ? 1.3849 1.0350 1.1040 0.3521  -0.0195 -0.0761 190  LEU F N   
16800 C  CA  . LEU F 190  ? 1.4484 1.0794 1.1678 0.3433  -0.0158 -0.0750 190  LEU F CA  
16801 C  C   . LEU F 190  ? 1.4868 1.1305 1.2247 0.3344  -0.0170 -0.0776 190  LEU F C   
16802 O  O   . LEU F 190  ? 1.4653 1.1071 1.2098 0.3283  -0.0152 -0.0758 190  LEU F O   
16803 C  CB  . LEU F 190  ? 1.6009 1.2010 1.3055 0.3410  -0.0125 -0.0761 190  LEU F CB  
16804 C  CG  . LEU F 190  ? 1.5274 1.1035 1.2278 0.3331  -0.0076 -0.0740 190  LEU F CG  
16805 C  CD1 . LEU F 190  ? 1.4118 0.9819 1.1024 0.3377  -0.0051 -0.0687 190  LEU F CD1 
16806 C  CD2 . LEU F 190  ? 1.5557 1.1037 1.2449 0.3289  -0.0047 -0.0763 190  LEU F CD2 
16807 N  N   . SER F 191  ? 2.4505 2.1072 2.1966 0.3338  -0.0201 -0.0817 191  SER F N   
16808 C  CA  . SER F 191  ? 2.3746 2.0456 2.1384 0.3262  -0.0216 -0.0842 191  SER F CA  
16809 C  C   . SER F 191  ? 2.3812 2.0792 2.1585 0.3272  -0.0236 -0.0822 191  SER F C   
16810 O  O   . SER F 191  ? 2.3810 2.0865 2.1713 0.3204  -0.0236 -0.0825 191  SER F O   
16811 C  CB  . SER F 191  ? 2.3189 1.9969 2.0867 0.3260  -0.0244 -0.0891 191  SER F CB  
16812 O  OG  . SER F 191  ? 2.4412 2.0941 2.1959 0.3251  -0.0228 -0.0913 191  SER F OG  
16813 N  N   . GLY F 192  ? 1.7378 1.4506 1.5125 0.3355  -0.0253 -0.0804 192  GLY F N   
16814 C  CA  . GLY F 192  ? 1.6604 1.3988 1.4477 0.3362  -0.0273 -0.0788 192  GLY F CA  
16815 C  C   . GLY F 192  ? 1.5588 1.2909 1.3471 0.3326  -0.0250 -0.0752 192  GLY F C   
16816 O  O   . GLY F 192  ? 1.4964 1.2423 1.2987 0.3273  -0.0256 -0.0750 192  GLY F O   
16817 N  N   . ILE F 193  ? 1.3548 1.0655 1.1277 0.3355  -0.0221 -0.0722 193  ILE F N   
16818 C  CA  . ILE F 193  ? 1.2907 0.9925 1.0627 0.3320  -0.0193 -0.0685 193  ILE F CA  
16819 C  C   . ILE F 193  ? 1.3016 0.9870 1.0778 0.3221  -0.0163 -0.0695 193  ILE F C   
16820 O  O   . ILE F 193  ? 1.2096 0.8954 0.9925 0.3169  -0.0146 -0.0675 193  ILE F O   
16821 C  CB  . ILE F 193  ? 1.3289 1.0128 1.0824 0.3385  -0.0169 -0.0649 193  ILE F CB  
16822 C  CG1 . ILE F 193  ? 1.3240 1.0008 1.0765 0.3356  -0.0140 -0.0608 193  ILE F CG1 
16823 C  CG2 . ILE F 193  ? 1.4117 1.0678 1.1502 0.3384  -0.0141 -0.0657 193  ILE F CG2 
16824 C  CD1 . ILE F 193  ? 1.3930 1.0958 1.1573 0.3370  -0.0169 -0.0596 193  ILE F CD1 
16825 N  N   . GLY F 194  ? 1.4066 1.0775 1.1788 0.3192  -0.0156 -0.0727 194  GLY F N   
16826 C  CA  . GLY F 194  ? 1.3956 1.0507 1.1716 0.3093  -0.0130 -0.0742 194  GLY F CA  
16827 C  C   . GLY F 194  ? 1.3251 1.0048 1.1231 0.2978  -0.0151 -0.0751 194  GLY F C   
16828 O  O   . GLY F 194  ? 1.2675 0.9437 1.0737 0.2857  -0.0128 -0.0739 194  GLY F O   
16829 N  N   . VAL F 195  ? 1.8101 1.5146 1.6177 0.3015  -0.0193 -0.0772 195  VAL F N   
16830 C  CA  . VAL F 195  ? 1.8490 1.5770 1.6768 0.2913  -0.0213 -0.0781 195  VAL F CA  
16831 C  C   . VAL F 195  ? 1.8803 1.6174 1.7168 0.2861  -0.0199 -0.0742 195  VAL F C   
16832 O  O   . VAL F 195  ? 1.8526 1.5933 1.7010 0.2739  -0.0188 -0.0736 195  VAL F O   
16833 C  CB  . VAL F 195  ? 1.8454 1.5975 1.6802 0.2975  -0.0255 -0.0808 195  VAL F CB  
16834 C  CG1 . VAL F 195  ? 1.7105 1.4890 1.5649 0.2895  -0.0272 -0.0803 195  VAL F CG1 
16835 C  CG2 . VAL F 195  ? 1.7812 1.5271 1.6124 0.2978  -0.0268 -0.0851 195  VAL F CG2 
16836 N  N   . ALA F 196  ? 1.5241 1.2650 1.3548 0.2955  -0.0201 -0.0716 196  ALA F N   
16837 C  CA  . ALA F 196  ? 1.3714 1.1189 1.2084 0.2914  -0.0187 -0.0679 196  ALA F CA  
16838 C  C   . ALA F 196  ? 1.3975 1.1212 1.2284 0.2841  -0.0139 -0.0652 196  ALA F C   
16839 O  O   . ALA F 196  ? 1.5150 1.2435 1.3564 0.2741  -0.0122 -0.0632 196  ALA F O   
16840 C  CB  . ALA F 196  ? 1.1974 0.9523 1.0276 0.3040  -0.0201 -0.0660 196  ALA F CB  
16841 N  N   . LEU F 197  ? 1.1877 0.8853 1.0015 0.2890  -0.0113 -0.0651 197  LEU F N   
16842 C  CA  . LEU F 197  ? 1.2368 0.9102 1.0442 0.2816  -0.0061 -0.0628 197  LEU F CA  
16843 C  C   . LEU F 197  ? 1.2161 0.8901 1.0366 0.2668  -0.0053 -0.0648 197  LEU F C   
16844 O  O   . LEU F 197  ? 1.1535 0.8233 0.9801 0.2569  -0.0020 -0.0626 197  LEU F O   
16845 C  CB  . LEU F 197  ? 1.3288 0.9737 1.1148 0.2898  -0.0036 -0.0628 197  LEU F CB  
16846 C  CG  . LEU F 197  ? 1.2361 0.8697 1.0057 0.3021  -0.0019 -0.0592 197  LEU F CG  
16847 C  CD1 . LEU F 197  ? 1.3066 0.9185 1.0573 0.3086  -0.0005 -0.0596 197  LEU F CD1 
16848 C  CD2 . LEU F 197  ? 1.1230 0.7461 0.8916 0.2959  0.0028  -0.0548 197  LEU F CD2 
16849 N  N   . PHE F 198  ? 1.2990 0.9786 1.1238 0.2653  -0.0082 -0.0691 198  PHE F N   
16850 C  CA  . PHE F 198  ? 1.3418 1.0216 1.1782 0.2520  -0.0080 -0.0715 198  PHE F CA  
16851 C  C   . PHE F 198  ? 1.3049 1.0086 1.1609 0.2431  -0.0094 -0.0707 198  PHE F C   
16852 O  O   . PHE F 198  ? 1.3133 1.0150 1.1786 0.2312  -0.0075 -0.0706 198  PHE F O   
16853 C  CB  . PHE F 198  ? 1.3326 1.0128 1.1674 0.2539  -0.0112 -0.0765 198  PHE F CB  
16854 C  CG  . PHE F 198  ? 1.2920 0.9796 1.1410 0.2415  -0.0125 -0.0796 198  PHE F CG  
16855 C  CD1 . PHE F 198  ? 1.4225 1.0905 1.2690 0.2328  -0.0101 -0.0813 198  PHE F CD1 
16856 C  CD2 . PHE F 198  ? 1.2684 0.9821 1.1327 0.2389  -0.0164 -0.0811 198  PHE F CD2 
16857 C  CE1 . PHE F 198  ? 1.3300 1.0054 1.1896 0.2219  -0.0118 -0.0845 198  PHE F CE1 
16858 C  CE2 . PHE F 198  ? 1.2617 0.9819 1.1381 0.2282  -0.0179 -0.0840 198  PHE F CE2 
16859 C  CZ  . PHE F 198  ? 1.2325 0.9341 1.1068 0.2199  -0.0158 -0.0858 198  PHE F CZ  
16860 N  N   . VAL F 199  ? 1.3044 1.0309 1.1669 0.2487  -0.0126 -0.0701 199  VAL F N   
16861 C  CA  . VAL F 199  ? 1.2559 1.0050 1.1363 0.2409  -0.0138 -0.0692 199  VAL F CA  
16862 C  C   . VAL F 199  ? 1.3184 1.0620 1.2005 0.2356  -0.0100 -0.0649 199  VAL F C   
16863 O  O   . VAL F 199  ? 1.3226 1.0715 1.2170 0.2245  -0.0088 -0.0643 199  VAL F O   
16864 C  CB  . VAL F 199  ? 1.1801 0.9537 1.0660 0.2484  -0.0178 -0.0697 199  VAL F CB  
16865 C  CG1 . VAL F 199  ? 1.1075 0.9012 1.0087 0.2418  -0.0182 -0.0676 199  VAL F CG1 
16866 C  CG2 . VAL F 199  ? 1.1589 0.9419 1.0480 0.2501  -0.0213 -0.0740 199  VAL F CG2 
16867 N  N   . ILE F 200  ? 1.2998 1.0324 1.1691 0.2437  -0.0079 -0.0618 200  ILE F N   
16868 C  CA  . ILE F 200  ? 1.2948 1.0216 1.1642 0.2398  -0.0041 -0.0576 200  ILE F CA  
16869 C  C   . ILE F 200  ? 1.3228 1.0290 1.1909 0.2297  0.0006  -0.0570 200  ILE F C   
16870 O  O   . ILE F 200  ? 1.3936 1.1030 1.2718 0.2200  0.0030  -0.0552 200  ILE F O   
16871 C  CB  . ILE F 200  ? 1.2997 1.0181 1.1540 0.2519  -0.0031 -0.0546 200  ILE F CB  
16872 C  CG1 . ILE F 200  ? 1.2638 1.0051 1.1214 0.2611  -0.0079 -0.0554 200  ILE F CG1 
16873 C  CG2 . ILE F 200  ? 1.2261 0.9363 1.0789 0.2480  0.0012  -0.0501 200  ILE F CG2 
16874 C  CD1 . ILE F 200  ? 1.2707 1.0363 1.1453 0.2549  -0.0096 -0.0546 200  ILE F CD1 
16875 N  N   . THR F 201  ? 1.1484 0.8333 1.0043 0.2318  0.0021  -0.0588 201  THR F N   
16876 C  CA  . THR F 201  ? 1.2121 0.8756 1.0654 0.2225  0.0071  -0.0584 201  THR F CA  
16877 C  C   . THR F 201  ? 1.1955 0.8691 1.0661 0.2092  0.0061  -0.0611 201  THR F C   
16878 O  O   . THR F 201  ? 1.1977 0.8660 1.0748 0.1991  0.0099  -0.0596 201  THR F O   
16879 C  CB  . THR F 201  ? 1.2446 0.8829 1.0804 0.2280  0.0086  -0.0601 201  THR F CB  
16880 O  OG1 . THR F 201  ? 1.2189 0.8655 1.0556 0.2320  0.0038  -0.0646 201  THR F OG1 
16881 C  CG2 . THR F 201  ? 1.2279 0.8522 1.0452 0.2405  0.0107  -0.0568 201  THR F CG2 
16882 N  N   . VAL F 202  ? 1.2706 0.9591 1.1488 0.2092  0.0012  -0.0652 202  VAL F N   
16883 C  CA  . VAL F 202  ? 1.2956 0.9937 1.1894 0.1974  -0.0002 -0.0681 202  VAL F CA  
16884 C  C   . VAL F 202  ? 1.2529 0.9714 1.1627 0.1911  -0.0004 -0.0657 202  VAL F C   
16885 O  O   . VAL F 202  ? 1.2136 0.9341 1.1348 0.1800  0.0010  -0.0661 202  VAL F O   
16886 C  CB  . VAL F 202  ? 1.2645 0.9724 1.1605 0.2002  -0.0054 -0.0729 202  VAL F CB  
16887 C  CG1 . VAL F 202  ? 1.1801 0.9038 1.0937 0.1894  -0.0078 -0.0755 202  VAL F CG1 
16888 C  CG2 . VAL F 202  ? 1.2656 0.9507 1.1473 0.2033  -0.0046 -0.0757 202  VAL F CG2 
16889 N  N   . THR F 203  ? 1.1382 0.8722 1.0491 0.1981  -0.0023 -0.0635 203  THR F N   
16890 C  CA  . THR F 203  ? 1.0929 0.8454 1.0178 0.1926  -0.0024 -0.0612 203  THR F CA  
16891 C  C   . THR F 203  ? 1.1056 0.8462 1.0305 0.1862  0.0031  -0.0575 203  THR F C   
16892 O  O   . THR F 203  ? 1.0596 0.8081 0.9976 0.1764  0.0042  -0.0570 203  THR F O   
16893 C  CB  . THR F 203  ? 1.1117 0.8806 1.0359 0.2019  -0.0050 -0.0596 203  THR F CB  
16894 O  OG1 . THR F 203  ? 1.0922 0.8743 1.0185 0.2068  -0.0098 -0.0631 203  THR F OG1 
16895 C  CG2 . THR F 203  ? 1.1103 0.8966 1.0477 0.1963  -0.0048 -0.0571 203  THR F CG2 
16896 N  N   . PHE F 204  ? 1.5175 1.2386 1.4272 0.1920  0.0067  -0.0548 204  PHE F N   
16897 C  CA  . PHE F 204  ? 1.5272 1.2352 1.4353 0.1865  0.0125  -0.0511 204  PHE F CA  
16898 C  C   . PHE F 204  ? 1.5403 1.2330 1.4509 0.1761  0.0160  -0.0528 204  PHE F C   
16899 O  O   . PHE F 204  ? 1.4735 1.1626 1.3903 0.1675  0.0202  -0.0507 204  PHE F O   
16900 C  CB  . PHE F 204  ? 1.3250 1.0164 1.2151 0.1964  0.0155  -0.0476 204  PHE F CB  
16901 C  CG  . PHE F 204  ? 1.3142 1.0200 1.2044 0.2034  0.0138  -0.0447 204  PHE F CG  
16902 C  CD1 . PHE F 204  ? 1.2740 0.9908 1.1747 0.1974  0.0154  -0.0420 204  PHE F CD1 
16903 C  CD2 . PHE F 204  ? 1.4049 1.1138 1.2849 0.2161  0.0106  -0.0450 204  PHE F CD2 
16904 C  CE1 . PHE F 204  ? 1.3117 1.0416 1.2124 0.2036  0.0136  -0.0397 204  PHE F CE1 
16905 C  CE2 . PHE F 204  ? 1.5164 1.2393 1.3970 0.2223  0.0087  -0.0428 204  PHE F CE2 
16906 C  CZ  . PHE F 204  ? 1.3711 1.1042 1.2619 0.2159  0.0102  -0.0402 204  PHE F CZ  
16907 N  N   . PHE F 205  ? 1.2697 0.9533 1.1754 0.1766  0.0143  -0.0568 205  PHE F N   
16908 C  CA  . PHE F 205  ? 1.2388 0.9106 1.1488 0.1659  0.0166  -0.0594 205  PHE F CA  
16909 C  C   . PHE F 205  ? 1.1979 0.8895 1.1282 0.1553  0.0144  -0.0612 205  PHE F C   
16910 O  O   . PHE F 205  ? 1.1906 0.8776 1.1287 0.1449  0.0179  -0.0611 205  PHE F O   
16911 C  CB  . PHE F 205  ? 1.2738 0.9331 1.1742 0.1694  0.0145  -0.0637 205  PHE F CB  
16912 C  CG  . PHE F 205  ? 1.2647 0.9158 1.1714 0.1582  0.0154  -0.0675 205  PHE F CG  
16913 C  CD1 . PHE F 205  ? 1.1989 0.8261 1.0986 0.1527  0.0212  -0.0669 205  PHE F CD1 
16914 C  CD2 . PHE F 205  ? 1.2542 0.9213 1.1737 0.1533  0.0104  -0.0720 205  PHE F CD2 
16915 C  CE1 . PHE F 205  ? 1.2049 0.8252 1.1112 0.1421  0.0219  -0.0709 205  PHE F CE1 
16916 C  CE2 . PHE F 205  ? 1.1946 0.8548 1.1201 0.1432  0.0107  -0.0760 205  PHE F CE2 
16917 C  CZ  . PHE F 205  ? 1.1919 0.8291 1.1112 0.1374  0.0164  -0.0755 205  PHE F CZ  
16918 N  N   . SER F 206  ? 1.3814 1.0953 1.3202 0.1580  0.0088  -0.0630 206  SER F N   
16919 C  CA  . SER F 206  ? 1.3566 1.0900 1.3138 0.1491  0.0065  -0.0645 206  SER F CA  
16920 C  C   . SER F 206  ? 1.3562 1.0976 1.3217 0.1448  0.0096  -0.0602 206  SER F C   
16921 O  O   . SER F 206  ? 1.3755 1.1244 1.3546 0.1350  0.0104  -0.0607 206  SER F O   
16922 C  CB  . SER F 206  ? 1.2572 1.0113 1.2198 0.1539  0.0003  -0.0670 206  SER F CB  
16923 O  OG  . SER F 206  ? 1.2051 0.9777 1.1845 0.1460  -0.0019 -0.0682 206  SER F OG  
16924 N  N   . PHE F 207  ? 1.1846 0.9248 1.1421 0.1522  0.0113  -0.0561 207  PHE F N   
16925 C  CA  . PHE F 207  ? 1.1477 0.8934 1.1112 0.1487  0.0147  -0.0519 207  PHE F CA  
16926 C  C   . PHE F 207  ? 1.2230 0.9508 1.1854 0.1408  0.0211  -0.0502 207  PHE F C   
16927 O  O   . PHE F 207  ? 1.1371 0.8717 1.1110 0.1328  0.0235  -0.0486 207  PHE F O   
16928 C  CB  . PHE F 207  ? 1.0928 0.8396 1.0462 0.1591  0.0148  -0.0483 207  PHE F CB  
16929 C  CG  . PHE F 207  ? 1.0711 0.8410 1.0307 0.1642  0.0094  -0.0491 207  PHE F CG  
16930 C  CD1 . PHE F 207  ? 1.0839 0.8716 1.0571 0.1594  0.0054  -0.0522 207  PHE F CD1 
16931 C  CD2 . PHE F 207  ? 1.0886 0.8623 1.0402 0.1739  0.0084  -0.0468 207  PHE F CD2 
16932 C  CE1 . PHE F 207  ? 1.0295 0.8376 1.0080 0.1638  0.0010  -0.0528 207  PHE F CE1 
16933 C  CE2 . PHE F 207  ? 1.0090 0.8041 0.9668 0.1781  0.0038  -0.0477 207  PHE F CE2 
16934 C  CZ  . PHE F 207  ? 0.9933 0.8052 0.9644 0.1728  0.0003  -0.0506 207  PHE F CZ  
16935 N  N   . ASP F 208  ? 1.5190 1.2236 1.4677 0.1430  0.0242  -0.0504 208  ASP F N   
16936 C  CA  . ASP F 208  ? 1.4411 1.1266 1.3867 0.1364  0.0311  -0.0483 208  ASP F CA  
16937 C  C   . ASP F 208  ? 1.4426 1.1278 1.4007 0.1240  0.0319  -0.0519 208  ASP F C   
16938 O  O   . ASP F 208  ? 1.4000 1.0838 1.3663 0.1153  0.0364  -0.0502 208  ASP F O   
16939 C  CB  . ASP F 208  ? 1.5643 1.2240 1.4897 0.1433  0.0345  -0.0473 208  ASP F CB  
16940 C  CG  . ASP F 208  ? 1.7113 1.3677 1.6238 0.1542  0.0356  -0.0428 208  ASP F CG  
16941 O  OD1 . ASP F 208  ? 1.6424 1.3136 1.5618 0.1545  0.0353  -0.0400 208  ASP F OD1 
16942 O  OD2 . ASP F 208  ? 1.8082 1.4470 1.7033 0.1628  0.0367  -0.0422 208  ASP F OD2 
16943 N  N   . VAL F 209  ? 1.3844 1.0713 1.3442 0.1232  0.0275  -0.0569 209  VAL F N   
16944 C  CA  . VAL F 209  ? 1.3575 1.0409 1.3268 0.1121  0.0281  -0.0608 209  VAL F CA  
16945 C  C   . VAL F 209  ? 1.3046 1.0119 1.2941 0.1046  0.0249  -0.0623 209  VAL F C   
16946 O  O   . VAL F 209  ? 1.3407 1.0485 1.3411 0.0944  0.0280  -0.0625 209  VAL F O   
16947 C  CB  . VAL F 209  ? 1.2053 0.8792 1.1671 0.1145  0.0246  -0.0658 209  VAL F CB  
16948 C  CG1 . VAL F 209  ? 1.1381 0.8109 1.1109 0.1028  0.0243  -0.0706 209  VAL F CG1 
16949 C  CG2 . VAL F 209  ? 1.2607 0.9087 1.2021 0.1214  0.0285  -0.0643 209  VAL F CG2 
16950 N  N   . ALA F 210  ? 1.0148 0.7421 1.0092 0.1095  0.0190  -0.0633 210  ALA F N   
16951 C  CA  . ALA F 210  ? 0.9983 0.7475 1.0104 0.1032  0.0153  -0.0653 210  ALA F CA  
16952 C  C   . ALA F 210  ? 0.9890 0.7548 1.0089 0.1039  0.0159  -0.0611 210  ALA F C   
16953 O  O   . ALA F 210  ? 0.9155 0.6912 0.9491 0.0959  0.0170  -0.0608 210  ALA F O   
16954 C  CB  . ALA F 210  ? 1.0244 0.7848 1.0376 0.1073  0.0083  -0.0697 210  ALA F CB  
16955 N  N   . MET F 211  ? 1.2018 0.9710 1.2134 0.1134  0.0150  -0.0582 211  MET F N   
16956 C  CA  . MET F 211  ? 1.1337 0.9191 1.1524 0.1142  0.0150  -0.0547 211  MET F CA  
16957 C  C   . MET F 211  ? 1.1934 0.9709 1.2131 0.1096  0.0215  -0.0504 211  MET F C   
16958 O  O   . MET F 211  ? 1.1766 0.9675 1.2065 0.1062  0.0222  -0.0483 211  MET F O   
16959 C  CB  . MET F 211  ? 1.1683 0.9591 1.1778 0.1254  0.0124  -0.0530 211  MET F CB  
16960 C  CG  . MET F 211  ? 1.1711 0.9814 1.1888 0.1263  0.0111  -0.0505 211  MET F CG  
16961 S  SD  . MET F 211  ? 1.3193 1.1409 1.3298 0.1382  0.0065  -0.0502 211  MET F SD  
16962 C  CE  . MET F 211  ? 1.0534 0.8628 1.0511 0.1446  0.0109  -0.0452 211  MET F CE  
16963 N  N   . SER F 212  ? 1.1336 0.8892 1.1424 0.1096  0.0266  -0.0491 212  SER F N   
16964 C  CA  . SER F 212  ? 1.1148 0.8611 1.1233 0.1054  0.0334  -0.0449 212  SER F CA  
16965 C  C   . SER F 212  ? 1.1927 0.9424 1.2162 0.0933  0.0360  -0.0462 212  SER F C   
16966 O  O   . SER F 212  ? 1.2519 0.9943 1.2764 0.0889  0.0421  -0.0430 212  SER F O   
16967 C  CB  . SER F 212  ? 1.2291 0.9496 1.2202 0.1093  0.0384  -0.0431 212  SER F CB  
16968 O  OG  . SER F 212  ? 1.3019 1.0079 1.2938 0.1017  0.0413  -0.0457 212  SER F OG  
16969 N  N   . LEU F 213  ? 0.9979 0.7585 1.0327 0.0881  0.0316  -0.0509 213  LEU F N   
16970 C  CA  . LEU F 213  ? 0.9968 0.7630 1.0470 0.0768  0.0334  -0.0525 213  LEU F CA  
16971 C  C   . LEU F 213  ? 1.0043 0.7877 1.0660 0.0745  0.0342  -0.0494 213  LEU F C   
16972 O  O   . LEU F 213  ? 1.0416 0.8254 1.1128 0.0666  0.0385  -0.0484 213  LEU F O   
16973 C  CB  . LEU F 213  ? 0.9951 0.7699 1.0539 0.0729  0.0276  -0.0585 213  LEU F CB  
16974 C  CG  . LEU F 213  ? 0.9046 0.6614 0.9573 0.0698  0.0283  -0.0624 213  LEU F CG  
16975 C  CD1 . LEU F 213  ? 0.7939 0.5609 0.8541 0.0675  0.0216  -0.0684 213  LEU F CD1 
16976 C  CD2 . LEU F 213  ? 0.8869 0.6313 0.9439 0.0602  0.0352  -0.0617 213  LEU F CD2 
16977 N  N   . ASP F 214  ? 1.8544 1.6520 1.9156 0.0813  0.0302  -0.0480 214  ASP F N   
16978 C  CA  . ASP F 214  ? 1.8604 1.6732 1.9303 0.0805  0.0309  -0.0448 214  ASP F CA  
16979 C  C   . ASP F 214  ? 1.7379 1.5474 1.7956 0.0894  0.0321  -0.0406 214  ASP F C   
16980 O  O   . ASP F 214  ? 1.7113 1.5305 1.7658 0.0964  0.0273  -0.0410 214  ASP F O   
16981 C  CB  . ASP F 214  ? 1.7982 1.6330 1.8803 0.0794  0.0247  -0.0476 214  ASP F CB  
16982 C  CG  . ASP F 214  ? 1.8276 1.6771 1.9207 0.0764  0.0260  -0.0448 214  ASP F CG  
16983 O  OD1 . ASP F 214  ? 1.8941 1.7385 1.9913 0.0710  0.0315  -0.0425 214  ASP F OD1 
16984 O  OD2 . ASP F 214  ? 1.8174 1.6831 1.9149 0.0794  0.0217  -0.0450 214  ASP F OD2 
16985 N  N   . PRO F 215  ? 1.2805 1.0764 1.3311 0.0896  0.0384  -0.0365 215  PRO F N   
16986 C  CA  . PRO F 215  ? 1.3028 1.0946 1.3408 0.0985  0.0393  -0.0326 215  PRO F CA  
16987 C  C   . PRO F 215  ? 1.3030 1.1135 1.3472 0.1009  0.0369  -0.0307 215  PRO F C   
16988 O  O   . PRO F 215  ? 1.3048 1.1142 1.3394 0.1084  0.0369  -0.0280 215  PRO F O   
16989 C  CB  . PRO F 215  ? 1.4064 1.1794 1.4371 0.0964  0.0473  -0.0289 215  PRO F CB  
16990 C  CG  . PRO F 215  ? 1.4593 1.2226 1.4954 0.0876  0.0501  -0.0316 215  PRO F CG  
16991 C  CD  . PRO F 215  ? 1.3374 1.1198 1.3902 0.0817  0.0451  -0.0355 215  PRO F CD  
16992 N  N   . HIS F 216  ? 1.3176 1.1449 1.3771 0.0949  0.0349  -0.0321 216  HIS F N   
16993 C  CA  . HIS F 216  ? 1.2430 1.0876 1.3084 0.0967  0.0327  -0.0305 216  HIS F CA  
16994 C  C   . HIS F 216  ? 1.1822 1.0400 1.2473 0.1024  0.0259  -0.0331 216  HIS F C   
16995 O  O   . HIS F 216  ? 1.2696 1.1406 1.3374 0.1050  0.0239  -0.0318 216  HIS F O   
16996 C  CB  . HIS F 216  ? 1.2010 1.0574 1.2823 0.0882  0.0338  -0.0307 216  HIS F CB  
16997 C  CG  . HIS F 216  ? 1.1641 1.0096 1.2476 0.0820  0.0408  -0.0284 216  HIS F CG  
16998 N  ND1 . HIS F 216  ? 1.2015 1.0434 1.2935 0.0739  0.0426  -0.0308 216  HIS F ND1 
16999 C  CD2 . HIS F 216  ? 1.1507 0.9885 1.2293 0.0825  0.0465  -0.0239 216  HIS F CD2 
17000 C  CE1 . HIS F 216  ? 1.2481 1.0807 1.3407 0.0695  0.0495  -0.0279 216  HIS F CE1 
17001 N  NE2 . HIS F 216  ? 1.1826 1.0122 1.2668 0.0748  0.0520  -0.0236 216  HIS F NE2 
17002 N  N   . TRP F 217  ? 0.9503 0.8048 1.0123 0.1041  0.0225  -0.0367 217  TRP F N   
17003 C  CA  . TRP F 217  ? 0.9526 0.8201 1.0156 0.1087  0.0163  -0.0395 217  TRP F CA  
17004 C  C   . TRP F 217  ? 0.9513 0.8082 1.0006 0.1165  0.0146  -0.0406 217  TRP F C   
17005 O  O   . TRP F 217  ? 0.9936 0.8333 1.0353 0.1163  0.0172  -0.0410 217  TRP F O   
17006 C  CB  . TRP F 217  ? 0.9548 0.8322 1.0297 0.1027  0.0130  -0.0434 217  TRP F CB  
17007 C  CG  . TRP F 217  ? 0.9217 0.8115 0.9974 0.1070  0.0070  -0.0464 217  TRP F CG  
17008 C  CD1 . TRP F 217  ? 0.8782 0.7853 0.9598 0.1086  0.0041  -0.0461 217  TRP F CD1 
17009 C  CD2 . TRP F 217  ? 0.9750 0.8605 1.0452 0.1103  0.0036  -0.0500 217  TRP F CD2 
17010 N  NE1 . TRP F 217  ? 0.9047 0.8187 0.9849 0.1125  -0.0007 -0.0492 217  TRP F NE1 
17011 C  CE2 . TRP F 217  ? 0.9602 0.8614 1.0334 0.1139  -0.0012 -0.0517 217  TRP F CE2 
17012 C  CE3 . TRP F 217  ? 0.9425 0.8118 1.0050 0.1107  0.0044  -0.0521 217  TRP F CE3 
17013 C  CZ2 . TRP F 217  ? 0.9047 0.8064 0.9738 0.1179  -0.0051 -0.0552 217  TRP F CZ2 
17014 C  CZ3 . TRP F 217  ? 1.0362 0.9056 1.0943 0.1148  0.0002  -0.0557 217  TRP F CZ3 
17015 C  CH2 . TRP F 217  ? 1.0220 0.9078 1.0834 0.1184  -0.0045 -0.0572 217  TRP F CH2 
17016 N  N   . PHE F 218  ? 1.1184 0.9857 1.1647 0.1235  0.0105  -0.0413 218  PHE F N   
17017 C  CA  . PHE F 218  ? 1.1413 1.0014 1.1755 0.1318  0.0083  -0.0426 218  PHE F CA  
17018 C  C   . PHE F 218  ? 1.0920 0.9691 1.1298 0.1358  0.0027  -0.0452 218  PHE F C   
17019 O  O   . PHE F 218  ? 1.0586 0.9517 1.1048 0.1342  0.0012  -0.0446 218  PHE F O   
17020 C  CB  . PHE F 218  ? 1.1174 0.9675 1.1387 0.1389  0.0108  -0.0392 218  PHE F CB  
17021 C  CG  . PHE F 218  ? 1.0986 0.9627 1.1218 0.1425  0.0095  -0.0371 218  PHE F CG  
17022 C  CD1 . PHE F 218  ? 1.1721 1.0411 1.2019 0.1378  0.0123  -0.0343 218  PHE F CD1 
17023 C  CD2 . PHE F 218  ? 1.0516 0.9241 1.0699 0.1508  0.0055  -0.0382 218  PHE F CD2 
17024 C  CE1 . PHE F 218  ? 1.2009 1.0821 1.2319 0.1409  0.0109  -0.0326 218  PHE F CE1 
17025 C  CE2 . PHE F 218  ? 1.0859 0.9714 1.1062 0.1536  0.0042  -0.0367 218  PHE F CE2 
17026 C  CZ  . PHE F 218  ? 1.1987 1.0881 1.2251 0.1486  0.0068  -0.0339 218  PHE F CZ  
17027 N  N   . SER F 219  ? 0.9462 0.8192 0.9770 0.1409  0.0000  -0.0480 219  SER F N   
17028 C  CA  . SER F 219  ? 0.9665 0.8542 0.9992 0.1455  -0.0049 -0.0505 219  SER F CA  
17029 C  C   . SER F 219  ? 0.8867 0.7669 0.9064 0.1551  -0.0062 -0.0513 219  SER F C   
17030 O  O   . SER F 219  ? 0.9352 0.7990 0.9464 0.1565  -0.0050 -0.0523 219  SER F O   
17031 C  CB  . SER F 219  ? 0.9725 0.8665 1.0138 0.1403  -0.0077 -0.0542 219  SER F CB  
17032 O  OG  . SER F 219  ? 1.0210 0.9280 1.0631 0.1451  -0.0119 -0.0566 219  SER F OG  
17033 N  N   . THR F 220  ? 0.9529 0.8450 0.9710 0.1618  -0.0087 -0.0510 220  THR F N   
17034 C  CA  . THR F 220  ? 0.9872 0.8741 0.9933 0.1718  -0.0101 -0.0518 220  THR F CA  
17035 C  C   . THR F 220  ? 1.0707 0.9584 1.0754 0.1741  -0.0132 -0.0558 220  THR F C   
17036 O  O   . THR F 220  ? 1.1551 1.0302 1.1485 0.1802  -0.0133 -0.0568 220  THR F O   
17037 C  CB  . THR F 220  ? 1.0747 0.9756 1.0807 0.1778  -0.0119 -0.0505 220  THR F CB  
17038 O  OG1 . THR F 220  ? 1.1036 1.0235 1.1224 0.1729  -0.0136 -0.0511 220  THR F OG1 
17039 C  CG2 . THR F 220  ? 1.1573 1.0506 1.1575 0.1795  -0.0088 -0.0467 220  THR F CG2 
17040 N  N   . ILE F 221  ? 1.0551 0.9568 1.0703 0.1697  -0.0157 -0.0580 221  ILE F N   
17041 C  CA  . ILE F 221  ? 1.0555 0.9581 1.0695 0.1717  -0.0186 -0.0619 221  ILE F CA  
17042 C  C   . ILE F 221  ? 1.0481 0.9329 1.0581 0.1679  -0.0174 -0.0636 221  ILE F C   
17043 O  O   . ILE F 221  ? 1.1072 0.9868 1.1118 0.1712  -0.0193 -0.0667 221  ILE F O   
17044 C  CB  . ILE F 221  ? 0.9306 0.8519 0.9564 0.1678  -0.0213 -0.0637 221  ILE F CB  
17045 C  CG1 . ILE F 221  ? 0.9197 0.8473 0.9423 0.1740  -0.0246 -0.0669 221  ILE F CG1 
17046 C  CG2 . ILE F 221  ? 0.8580 0.7769 0.8920 0.1584  -0.0209 -0.0648 221  ILE F CG2 
17047 C  CD1 . ILE F 221  ? 0.9047 0.8499 0.9375 0.1709  -0.0270 -0.0686 221  ILE F CD1 
17048 N  N   . TYR F 222  ? 1.2758 1.1510 1.2883 0.1609  -0.0140 -0.0617 222  TYR F N   
17049 C  CA  . TYR F 222  ? 1.3402 1.1991 1.3501 0.1561  -0.0125 -0.0635 222  TYR F CA  
17050 C  C   . TYR F 222  ? 1.4815 1.3215 1.4759 0.1632  -0.0112 -0.0636 222  TYR F C   
17051 O  O   . TYR F 222  ? 1.5468 1.3827 1.5329 0.1698  -0.0097 -0.0608 222  TYR F O   
17052 C  CB  . TYR F 222  ? 1.3839 1.2380 1.4007 0.1471  -0.0087 -0.0612 222  TYR F CB  
17053 C  CG  . TYR F 222  ? 1.4700 1.3102 1.4875 0.1402  -0.0073 -0.0635 222  TYR F CG  
17054 C  CD1 . TYR F 222  ? 1.5154 1.3629 1.5420 0.1346  -0.0103 -0.0673 222  TYR F CD1 
17055 C  CD2 . TYR F 222  ? 1.5246 1.3445 1.5337 0.1391  -0.0029 -0.0621 222  TYR F CD2 
17056 C  CE1 . TYR F 222  ? 1.5545 1.3902 1.5824 0.1280  -0.0093 -0.0699 222  TYR F CE1 
17057 C  CE2 . TYR F 222  ? 1.6490 1.4563 1.6594 0.1321  -0.0014 -0.0644 222  TYR F CE2 
17058 C  CZ  . TYR F 222  ? 1.6490 1.4648 1.6691 0.1265  -0.0047 -0.0685 222  TYR F CZ  
17059 O  OH  . TYR F 222  ? 1.6458 1.4498 1.6676 0.1192  -0.0036 -0.0713 222  TYR F OH  
17060 N  N   . GLY F 223  ? 1.4109 1.2392 1.4010 0.1620  -0.0119 -0.0669 223  GLY F N   
17061 C  CA  . GLY F 223  ? 1.4542 1.2649 1.4289 0.1695  -0.0111 -0.0675 223  GLY F CA  
17062 C  C   . GLY F 223  ? 1.4569 1.2745 1.4274 0.1771  -0.0153 -0.0707 223  GLY F C   
17063 O  O   . GLY F 223  ? 1.4775 1.2836 1.4411 0.1786  -0.0163 -0.0739 223  GLY F O   
17064 N  N   . ALA F 224  ? 1.2399 1.0763 1.2147 0.1819  -0.0178 -0.0700 224  ALA F N   
17065 C  CA  . ALA F 224  ? 1.1513 0.9979 1.1252 0.1878  -0.0217 -0.0732 224  ALA F CA  
17066 C  C   . ALA F 224  ? 1.1995 1.0526 1.1825 0.1808  -0.0241 -0.0767 224  ALA F C   
17067 O  O   . ALA F 224  ? 1.2817 1.1330 1.2605 0.1841  -0.0265 -0.0802 224  ALA F O   
17068 C  CB  . ALA F 224  ? 1.0420 0.9083 1.0200 0.1932  -0.0234 -0.0717 224  ALA F CB  
17069 N  N   . HIS F 225  ? 1.1036 0.9643 1.0988 0.1716  -0.0235 -0.0758 225  HIS F N   
17070 C  CA  . HIS F 225  ? 1.0841 0.9486 1.0876 0.1644  -0.0256 -0.0791 225  HIS F CA  
17071 C  C   . HIS F 225  ? 1.2013 1.0461 1.1980 0.1618  -0.0250 -0.0819 225  HIS F C   
17072 O  O   . HIS F 225  ? 1.1902 1.0351 1.1878 0.1603  -0.0278 -0.0860 225  HIS F O   
17073 C  CB  . HIS F 225  ? 1.0213 0.8956 1.0382 0.1553  -0.0245 -0.0773 225  HIS F CB  
17074 C  CG  . HIS F 225  ? 1.1149 0.9952 1.1410 0.1482  -0.0270 -0.0805 225  HIS F CG  
17075 N  ND1 . HIS F 225  ? 1.1640 1.0344 1.1938 0.1401  -0.0259 -0.0820 225  HIS F ND1 
17076 C  CD2 . HIS F 225  ? 1.1211 1.0165 1.1536 0.1481  -0.0305 -0.0827 225  HIS F CD2 
17077 C  CE1 . HIS F 225  ? 1.1347 1.0143 1.1728 0.1356  -0.0291 -0.0851 225  HIS F CE1 
17078 N  NE2 . HIS F 225  ? 1.1785 1.0728 1.2178 0.1405  -0.0318 -0.0854 225  HIS F NE2 
17079 N  N   . TYR F 226  ? 1.2241 1.0512 1.2134 0.1612  -0.0212 -0.0799 226  TYR F N   
17080 C  CA  . TYR F 226  ? 1.1945 1.0013 1.1767 0.1585  -0.0200 -0.0826 226  TYR F CA  
17081 C  C   . TYR F 226  ? 1.1950 0.9931 1.1640 0.1675  -0.0220 -0.0853 226  TYR F C   
17082 O  O   . TYR F 226  ? 1.2086 0.9966 1.1742 0.1654  -0.0233 -0.0892 226  TYR F O   
17083 C  CB  . TYR F 226  ? 1.1463 0.9359 1.1233 0.1560  -0.0148 -0.0793 226  TYR F CB  
17084 C  CG  . TYR F 226  ? 1.1446 0.9121 1.1144 0.1521  -0.0128 -0.0818 226  TYR F CG  
17085 C  CD1 . TYR F 226  ? 1.1270 0.8943 1.1046 0.1435  -0.0146 -0.0859 226  TYR F CD1 
17086 C  CD2 . TYR F 226  ? 1.2429 0.9893 1.1978 0.1570  -0.0093 -0.0802 226  TYR F CD2 
17087 C  CE1 . TYR F 226  ? 1.1706 0.9176 1.1420 0.1394  -0.0128 -0.0886 226  TYR F CE1 
17088 C  CE2 . TYR F 226  ? 1.1961 0.9212 1.1440 0.1532  -0.0072 -0.0826 226  TYR F CE2 
17089 C  CZ  . TYR F 226  ? 1.1503 0.8758 1.1067 0.1441  -0.0089 -0.0869 226  TYR F CZ  
17090 O  OH  . TYR F 226  ? 1.2221 0.9264 1.1718 0.1397  -0.0068 -0.0895 226  TYR F OH  
17091 N  N   . MET F 227  ? 1.5093 1.3113 1.4709 0.1776  -0.0223 -0.0834 227  MET F N   
17092 C  CA  . MET F 227  ? 1.4874 1.2822 1.4365 0.1869  -0.0241 -0.0859 227  MET F CA  
17093 C  C   . MET F 227  ? 1.5186 1.3264 1.4728 0.1873  -0.0285 -0.0899 227  MET F C   
17094 O  O   . MET F 227  ? 1.6237 1.4215 1.5704 0.1896  -0.0300 -0.0936 227  MET F O   
17095 C  CB  . MET F 227  ? 1.5111 1.3090 1.4522 0.1979  -0.0236 -0.0830 227  MET F CB  
17096 C  CG  . MET F 227  ? 1.5111 1.2918 1.4425 0.1999  -0.0194 -0.0794 227  MET F CG  
17097 S  SD  . MET F 227  ? 1.6919 1.4753 1.6119 0.2143  -0.0195 -0.0769 227  MET F SD  
17098 C  CE  . MET F 227  ? 1.6322 1.4423 1.5670 0.2122  -0.0206 -0.0741 227  MET F CE  
17099 N  N   . ALA F 228  ? 0.9453 0.7749 0.9116 0.1852  -0.0304 -0.0892 228  ALA F N   
17100 C  CA  . ALA F 228  ? 0.9864 0.8284 0.9577 0.1851  -0.0342 -0.0928 228  ALA F CA  
17101 C  C   . ALA F 228  ? 1.0488 0.8840 1.0245 0.1762  -0.0354 -0.0963 228  ALA F C   
17102 O  O   . ALA F 228  ? 1.0830 0.9177 1.0561 0.1775  -0.0383 -0.1004 228  ALA F O   
17103 C  CB  . ALA F 228  ? 0.9537 0.8192 0.9366 0.1843  -0.0353 -0.0910 228  ALA F CB  
17104 N  N   . ASN F 229  ? 1.3578 1.1882 1.3402 0.1672  -0.0332 -0.0949 229  ASN F N   
17105 C  CA  . ASN F 229  ? 1.3833 1.2071 1.3703 0.1584  -0.0343 -0.0985 229  ASN F CA  
17106 C  C   . ASN F 229  ? 1.4129 1.2147 1.3874 0.1601  -0.0340 -0.1017 229  ASN F C   
17107 O  O   . ASN F 229  ? 1.4376 1.2363 1.4116 0.1578  -0.0369 -0.1063 229  ASN F O   
17108 C  CB  . ASN F 229  ? 1.4282 1.2521 1.4255 0.1488  -0.0315 -0.0961 229  ASN F CB  
17109 C  CG  . ASN F 229  ? 1.4556 1.2812 1.4625 0.1391  -0.0336 -0.0998 229  ASN F CG  
17110 O  OD1 . ASN F 229  ? 1.5101 1.3321 1.5141 0.1392  -0.0368 -0.1044 229  ASN F OD1 
17111 N  ND2 . ASN F 229  ? 1.5095 1.3408 1.5279 0.1310  -0.0318 -0.0979 229  ASN F ND2 
17112 N  N   . ALA F 230  ? 1.3346 1.1203 1.2982 0.1642  -0.0304 -0.0993 230  ALA F N   
17113 C  CA  . ALA F 230  ? 1.3722 1.1354 1.3223 0.1664  -0.0296 -0.1021 230  ALA F CA  
17114 C  C   . ALA F 230  ? 1.3826 1.1466 1.3234 0.1759  -0.0329 -0.1051 230  ALA F C   
17115 O  O   . ALA F 230  ? 1.4734 1.2236 1.4065 0.1759  -0.0341 -0.1093 230  ALA F O   
17116 C  CB  . ALA F 230  ? 1.2686 1.0144 1.2083 0.1696  -0.0248 -0.0984 230  ALA F CB  
17117 N  N   . GLY F 231  ? 1.2764 1.0565 1.2178 0.1838  -0.0343 -0.1033 231  GLY F N   
17118 C  CA  . GLY F 231  ? 1.3586 1.1414 1.2922 0.1928  -0.0371 -0.1061 231  GLY F CA  
17119 C  C   . GLY F 231  ? 1.3898 1.1809 1.3294 0.1888  -0.0411 -0.1106 231  GLY F C   
17120 O  O   . GLY F 231  ? 1.3851 1.1684 1.3159 0.1931  -0.0432 -0.1145 231  GLY F O   
17121 N  N   . LEU F 232  ? 1.4029 1.2096 1.3571 0.1810  -0.0424 -0.1102 232  LEU F N   
17122 C  CA  . LEU F 232  ? 1.3718 1.1862 1.3318 0.1770  -0.0463 -0.1144 232  LEU F CA  
17123 C  C   . LEU F 232  ? 1.3657 1.1627 1.3227 0.1703  -0.0471 -0.1187 232  LEU F C   
17124 O  O   . LEU F 232  ? 1.4468 1.2419 1.4008 0.1709  -0.0504 -0.1234 232  LEU F O   
17125 C  CB  . LEU F 232  ? 1.3724 1.2068 1.3480 0.1705  -0.0472 -0.1127 232  LEU F CB  
17126 C  CG  . LEU F 232  ? 1.3617 1.2070 1.3442 0.1669  -0.0513 -0.1165 232  LEU F CG  
17127 C  CD1 . LEU F 232  ? 1.3193 1.1652 1.2925 0.1753  -0.0539 -0.1196 232  LEU F CD1 
17128 C  CD2 . LEU F 232  ? 1.3061 1.1724 1.3020 0.1634  -0.0517 -0.1138 232  LEU F CD2 
17129 N  N   . MET F 233  ? 1.0866 0.8708 1.0446 0.1639  -0.0439 -0.1173 233  MET F N   
17130 C  CA  . MET F 233  ? 1.1256 0.8931 1.0816 0.1566  -0.0442 -0.1214 233  MET F CA  
17131 C  C   . MET F 233  ? 1.2256 0.9735 1.1650 0.1632  -0.0443 -0.1245 233  MET F C   
17132 O  O   . MET F 233  ? 1.2407 0.9812 1.1770 0.1608  -0.0472 -0.1297 233  MET F O   
17133 C  CB  . MET F 233  ? 1.2682 1.0266 1.2291 0.1484  -0.0399 -0.1188 233  MET F CB  
17134 C  CG  . MET F 233  ? 1.3007 1.0393 1.2582 0.1410  -0.0392 -0.1228 233  MET F CG  
17135 S  SD  . MET F 233  ? 1.3090 1.0580 1.2831 0.1284  -0.0428 -0.1273 233  MET F SD  
17136 C  CE  . MET F 233  ? 1.2750 1.0322 1.2629 0.1205  -0.0384 -0.1220 233  MET F CE  
17137 N  N   . THR F 234  ? 1.2168 0.9556 1.1447 0.1718  -0.0413 -0.1213 234  THR F N   
17138 C  CA  . THR F 234  ? 1.2203 0.9397 1.1312 0.1790  -0.0411 -0.1239 234  THR F CA  
17139 C  C   . THR F 234  ? 1.2290 0.9567 1.1350 0.1871  -0.0452 -0.1270 234  THR F C   
17140 O  O   . THR F 234  ? 1.3049 1.0174 1.1987 0.1910  -0.0462 -0.1308 234  THR F O   
17141 C  CB  . THR F 234  ? 1.1997 0.9075 1.0993 0.1866  -0.0369 -0.1195 234  THR F CB  
17142 O  OG1 . THR F 234  ? 1.2156 0.9011 1.0983 0.1924  -0.0362 -0.1221 234  THR F OG1 
17143 C  CG2 . THR F 234  ? 1.2508 0.9769 1.1515 0.1961  -0.0374 -0.1159 234  THR F CG2 
17144 N  N   . LEU F 235  ? 1.2355 0.9864 1.1502 0.1899  -0.0472 -0.1255 235  LEU F N   
17145 C  CA  . LEU F 235  ? 1.1629 0.9225 1.0739 0.1969  -0.0507 -0.1285 235  LEU F CA  
17146 C  C   . LEU F 235  ? 1.2306 0.9901 1.1455 0.1902  -0.0546 -0.1340 235  LEU F C   
17147 O  O   . LEU F 235  ? 1.3701 1.1225 1.2755 0.1949  -0.0570 -0.1382 235  LEU F O   
17148 C  CB  . LEU F 235  ? 1.1184 0.9025 1.0377 0.2013  -0.0512 -0.1253 235  LEU F CB  
17149 C  CG  . LEU F 235  ? 1.1173 0.9040 1.0290 0.2126  -0.0491 -0.1219 235  LEU F CG  
17150 C  CD1 . LEU F 235  ? 1.0023 0.8143 0.9237 0.2155  -0.0499 -0.1195 235  LEU F CD1 
17151 C  CD2 . LEU F 235  ? 1.0923 0.8657 0.9881 0.2221  -0.0498 -0.1250 235  LEU F CD2 
17152 N  N   . ALA F 236  ? 1.1315 0.8994 1.0602 0.1797  -0.0555 -0.1341 236  ALA F N   
17153 C  CA  . ALA F 236  ? 1.1213 0.8886 1.0541 0.1729  -0.0594 -0.1395 236  ALA F CA  
17154 C  C   . ALA F 236  ? 1.2220 0.9651 1.1456 0.1693  -0.0592 -0.1436 236  ALA F C   
17155 O  O   . ALA F 236  ? 1.2669 1.0047 1.1867 0.1682  -0.0628 -0.1492 236  ALA F O   
17156 C  CB  . ALA F 236  ? 1.1290 0.9108 1.0789 0.1628  -0.0602 -0.1384 236  ALA F CB  
17157 N  N   . PHE F 237  ? 1.4448 1.1725 1.3644 0.1673  -0.0548 -0.1411 237  PHE F N   
17158 C  CA  . PHE F 237  ? 1.5581 1.2608 1.4674 0.1643  -0.0538 -0.1447 237  PHE F CA  
17159 C  C   . PHE F 237  ? 1.6013 1.2912 1.4932 0.1749  -0.0547 -0.1472 237  PHE F C   
17160 O  O   . PHE F 237  ? 1.6372 1.3121 1.5214 0.1731  -0.0566 -0.1526 237  PHE F O   
17161 C  CB  . PHE F 237  ? 1.6645 1.3537 1.5726 0.1606  -0.0482 -0.1408 237  PHE F CB  
17162 C  CG  . PHE F 237  ? 1.6055 1.2665 1.4987 0.1610  -0.0458 -0.1431 237  PHE F CG  
17163 C  CD1 . PHE F 237  ? 1.5977 1.2457 1.4916 0.1517  -0.0470 -0.1485 237  PHE F CD1 
17164 C  CD2 . PHE F 237  ? 1.6234 1.2706 1.5016 0.1707  -0.0423 -0.1401 237  PHE F CD2 
17165 C  CE1 . PHE F 237  ? 1.7319 1.3531 1.6117 0.1518  -0.0445 -0.1508 237  PHE F CE1 
17166 C  CE2 . PHE F 237  ? 1.7028 1.3229 1.5663 0.1713  -0.0399 -0.1421 237  PHE F CE2 
17167 C  CZ  . PHE F 237  ? 1.7596 1.3663 1.6238 0.1617  -0.0408 -0.1474 237  PHE F CZ  
17168 N  N   . LEU F 238  ? 1.4179 1.1139 1.3034 0.1861  -0.0534 -0.1436 238  LEU F N   
17169 C  CA  . LEU F 238  ? 1.3929 1.0785 1.2621 0.1971  -0.0541 -0.1458 238  LEU F CA  
17170 C  C   . LEU F 238  ? 1.3657 1.0603 1.2351 0.1989  -0.0591 -0.1507 238  LEU F C   
17171 O  O   . LEU F 238  ? 1.5041 1.1843 1.3607 0.2032  -0.0606 -0.1550 238  LEU F O   
17172 C  CB  . LEU F 238  ? 1.3042 0.9972 1.1684 0.2086  -0.0517 -0.1408 238  LEU F CB  
17173 C  CG  . LEU F 238  ? 1.3458 1.0228 1.2014 0.2116  -0.0469 -0.1367 238  LEU F CG  
17174 C  CD1 . LEU F 238  ? 1.4127 1.1030 1.2672 0.2219  -0.0454 -0.1319 238  LEU F CD1 
17175 C  CD2 . LEU F 238  ? 1.3558 1.0054 1.1934 0.2155  -0.0458 -0.1399 238  LEU F CD2 
17176 N  N   . ALA F 239  ? 1.0892 0.8068 0.9723 0.1958  -0.0616 -0.1501 239  ALA F N   
17177 C  CA  . ALA F 239  ? 1.1918 0.9181 1.0752 0.1973  -0.0663 -0.1546 239  ALA F CA  
17178 C  C   . ALA F 239  ? 1.2511 0.9650 1.1342 0.1887  -0.0694 -0.1608 239  ALA F C   
17179 O  O   . ALA F 239  ? 1.1762 0.8847 1.0510 0.1919  -0.0727 -0.1658 239  ALA F O   
17180 C  CB  . ALA F 239  ? 1.1461 0.8989 1.0439 0.1957  -0.0678 -0.1522 239  ALA F CB  
17181 N  N   . LEU F 240  ? 1.5085 1.2182 1.4008 0.1775  -0.0684 -0.1606 240  LEU F N   
17182 C  CA  . LEU F 240  ? 1.4458 1.1439 1.3389 0.1685  -0.0712 -0.1667 240  LEU F CA  
17183 C  C   . LEU F 240  ? 1.5232 1.1946 1.3991 0.1717  -0.0701 -0.1702 240  LEU F C   
17184 O  O   . LEU F 240  ? 1.6047 1.2675 1.4742 0.1711  -0.0738 -0.1764 240  LEU F O   
17185 C  CB  . LEU F 240  ? 1.4567 1.1564 1.3639 0.1561  -0.0696 -0.1655 240  LEU F CB  
17186 C  CG  . LEU F 240  ? 1.3922 1.1158 1.3171 0.1500  -0.0722 -0.1645 240  LEU F CG  
17187 C  CD1 . LEU F 240  ? 1.3355 1.0633 1.2724 0.1425  -0.0682 -0.1598 240  LEU F CD1 
17188 C  CD2 . LEU F 240  ? 1.2020 0.9269 1.1318 0.1429  -0.0776 -0.1714 240  LEU F CD2 
17189 N  N   . MET F 241  ? 1.6080 1.2653 1.4755 0.1753  -0.0651 -0.1664 241  MET F N   
17190 C  CA  . MET F 241  ? 1.6693 1.2995 1.5196 0.1784  -0.0635 -0.1693 241  MET F CA  
17191 C  C   . MET F 241  ? 1.7400 1.3673 1.5757 0.1910  -0.0654 -0.1713 241  MET F C   
17192 O  O   . MET F 241  ? 1.8755 1.4824 1.6974 0.1929  -0.0661 -0.1759 241  MET F O   
17193 C  CB  . MET F 241  ? 1.6165 1.2326 1.4613 0.1794  -0.0574 -0.1642 241  MET F CB  
17194 C  CG  . MET F 241  ? 1.5997 1.2115 1.4556 0.1664  -0.0547 -0.1632 241  MET F CG  
17195 S  SD  . MET F 241  ? 1.8268 1.4230 1.6839 0.1540  -0.0574 -0.1713 241  MET F SD  
17196 C  CE  . MET F 241  ? 1.7795 1.3997 1.6613 0.1412  -0.0596 -0.1711 241  MET F CE  
17197 N  N   . MET F 242  ? 1.6337 1.2808 1.4720 0.1995  -0.0661 -0.1681 242  MET F N   
17198 C  CA  . MET F 242  ? 1.6159 1.2628 1.4419 0.2111  -0.0681 -0.1703 242  MET F CA  
17199 C  C   . MET F 242  ? 1.5610 1.2101 1.3874 0.2080  -0.0735 -0.1769 242  MET F C   
17200 O  O   . MET F 242  ? 1.6192 1.2556 1.4316 0.2140  -0.0751 -0.1812 242  MET F O   
17201 C  CB  . MET F 242  ? 1.6067 1.2756 1.4369 0.2201  -0.0672 -0.1654 242  MET F CB  
17202 C  CG  . MET F 242  ? 1.6484 1.3139 1.4637 0.2340  -0.0671 -0.1661 242  MET F CG  
17203 S  SD  . MET F 242  ? 1.8577 1.5397 1.6746 0.2449  -0.0636 -0.1591 242  MET F SD  
17204 C  CE  . MET F 242  ? 1.6584 1.3702 1.4972 0.2371  -0.0650 -0.1562 242  MET F CE  
17205 N  N   . SER F 243  ? 1.5605 1.2258 1.4026 0.1989  -0.0764 -0.1778 243  SER F N   
17206 C  CA  . SER F 243  ? 1.5793 1.2468 1.4224 0.1952  -0.0819 -0.1842 243  SER F CA  
17207 C  C   . SER F 243  ? 1.6824 1.3266 1.5188 0.1881  -0.0832 -0.1902 243  SER F C   
17208 O  O   . SER F 243  ? 1.7487 1.3876 1.5791 0.1881  -0.0876 -0.1965 243  SER F O   
17209 C  CB  . SER F 243  ? 1.5708 1.2611 1.4324 0.1874  -0.0845 -0.1834 243  SER F CB  
17210 O  OG  . SER F 243  ? 1.6139 1.3051 1.4769 0.1828  -0.0901 -0.1899 243  SER F OG  
17211 N  N   . ARG F 244  ? 1.6949 1.3246 1.5318 0.1819  -0.0793 -0.1886 244  ARG F N   
17212 C  CA  . ARG F 244  ? 1.7397 1.3463 1.5706 0.1743  -0.0798 -0.1941 244  ARG F CA  
17213 C  C   . ARG F 244  ? 1.8281 1.4113 1.6376 0.1832  -0.0788 -0.1967 244  ARG F C   
17214 O  O   . ARG F 244  ? 1.9640 1.5321 1.7656 0.1804  -0.0817 -0.2035 244  ARG F O   
17215 C  CB  . ARG F 244  ? 1.8350 1.4339 1.6736 0.1645  -0.0753 -0.1912 244  ARG F CB  
17216 C  CG  . ARG F 244  ? 1.9046 1.5169 1.7624 0.1513  -0.0776 -0.1926 244  ARG F CG  
17217 C  CD  . ARG F 244  ? 1.9392 1.5465 1.7973 0.1447  -0.0832 -0.2011 244  ARG F CD  
17218 N  NE  . ARG F 244  ? 2.0824 1.6929 1.9559 0.1305  -0.0839 -0.2033 244  ARG F NE  
17219 C  CZ  . ARG F 244  ? 2.2140 1.8251 2.0928 0.1226  -0.0892 -0.2105 244  ARG F CZ  
17220 N  NH1 . ARG F 244  ? 2.2920 1.9001 2.1614 0.1274  -0.0944 -0.2163 244  ARG F NH1 
17221 N  NH2 . ARG F 244  ? 2.1765 1.7917 2.0704 0.1098  -0.0893 -0.2120 244  ARG F NH2 
17222 N  N   . VAL F 245  ? 1.5187 1.0985 1.3184 0.1941  -0.0747 -0.1917 245  VAL F N   
17223 C  CA  . VAL F 245  ? 1.5907 1.1467 1.3697 0.2030  -0.0728 -0.1933 245  VAL F CA  
17224 C  C   . VAL F 245  ? 1.5519 1.1174 1.3220 0.2170  -0.0745 -0.1931 245  VAL F C   
17225 O  O   . VAL F 245  ? 1.5706 1.1246 1.3258 0.2281  -0.0717 -0.1914 245  VAL F O   
17226 C  CB  . VAL F 245  ? 1.5802 1.1212 1.3533 0.2046  -0.0664 -0.1880 245  VAL F CB  
17227 C  CG1 . VAL F 245  ? 1.5046 1.0628 1.2809 0.2139  -0.0637 -0.1807 245  VAL F CG1 
17228 C  CG2 . VAL F 245  ? 1.6533 1.1636 1.4051 0.2098  -0.0643 -0.1909 245  VAL F CG2 
17229 N  N   . ARG F 246  ? 1.8624 1.4485 1.6412 0.2168  -0.0790 -0.1950 246  ARG F N   
17230 C  CA  . ARG F 246  ? 1.9426 1.5401 1.7148 0.2293  -0.0803 -0.1945 246  ARG F CA  
17231 C  C   . ARG F 246  ? 2.0576 1.6355 1.8102 0.2371  -0.0817 -0.1998 246  ARG F C   
17232 O  O   . ARG F 246  ? 2.0391 1.6237 1.7840 0.2488  -0.0819 -0.1993 246  ARG F O   
17233 C  CB  . ARG F 246  ? 1.8373 1.4599 1.6229 0.2264  -0.0845 -0.1955 246  ARG F CB  
17234 C  CG  . ARG F 246  ? 1.7720 1.3897 1.5581 0.2190  -0.0900 -0.2030 246  ARG F CG  
17235 C  CD  . ARG F 246  ? 1.6826 1.3244 1.4787 0.2189  -0.0941 -0.2037 246  ARG F CD  
17236 N  NE  . ARG F 246  ? 1.6768 1.3373 1.4923 0.2100  -0.0940 -0.2001 246  ARG F NE  
17237 C  CZ  . ARG F 246  ? 1.6866 1.3685 1.5131 0.2082  -0.0971 -0.2000 246  ARG F CZ  
17238 N  NH1 . ARG F 246  ? 1.6509 1.3388 1.4712 0.2145  -0.1005 -0.2031 246  ARG F NH1 
17239 N  NH2 . ARG F 246  ? 1.6835 1.3806 1.5269 0.2002  -0.0966 -0.1965 246  ARG F NH2 
17240 N  N   . ASP F 247  ? 2.4792 2.0332 2.2236 0.2310  -0.0824 -0.2050 247  ASP F N   
17241 C  CA  . ASP F 247  ? 2.4835 2.0174 2.2090 0.2375  -0.0841 -0.2107 247  ASP F CA  
17242 C  C   . ASP F 247  ? 2.5611 2.0647 2.2731 0.2365  -0.0803 -0.2115 247  ASP F C   
17243 O  O   . ASP F 247  ? 2.6030 2.0867 2.3081 0.2301  -0.0821 -0.2175 247  ASP F O   
17244 C  CB  . ASP F 247  ? 2.4763 2.0114 2.2043 0.2306  -0.0903 -0.2182 247  ASP F CB  
17245 C  CG  . ASP F 247  ? 2.5977 2.1323 2.3398 0.2146  -0.0919 -0.2204 247  ASP F CG  
17246 O  OD1 . ASP F 247  ? 2.5706 2.1054 2.3214 0.2087  -0.0880 -0.2158 247  ASP F OD1 
17247 O  OD2 . ASP F 247  ? 2.5867 2.1210 2.3313 0.2080  -0.0971 -0.2270 247  ASP F OD2 
17248 N  N   . ALA F 248  ? 2.3174 1.8173 2.0251 0.2430  -0.0751 -0.2053 248  ALA F N   
17249 C  CA  . ALA F 248  ? 2.3970 1.8685 2.0914 0.2431  -0.0707 -0.2049 248  ALA F CA  
17250 C  C   . ALA F 248  ? 2.4979 1.9527 2.1703 0.2579  -0.0690 -0.2054 248  ALA F C   
17251 O  O   . ALA F 248  ? 2.4540 1.8884 2.1147 0.2608  -0.0645 -0.2030 248  ALA F O   
17252 C  CB  . ALA F 248  ? 2.3416 1.8173 2.0446 0.2403  -0.0658 -0.1977 248  ALA F CB  
17253 N  N   . ALA F 249  ? 2.3577 1.8217 2.0246 0.2671  -0.0722 -0.2079 249  ALA F N   
17254 C  CA  . ALA F 249  ? 2.3138 1.7737 1.9656 0.2783  -0.0702 -0.2055 249  ALA F CA  
17255 C  C   . ALA F 249  ? 2.3090 1.7791 1.9602 0.2880  -0.0655 -0.1971 249  ALA F C   
17256 O  O   . ALA F 249  ? 2.3454 1.8160 1.9856 0.2980  -0.0639 -0.1945 249  ALA F O   
17257 C  CB  . ALA F 249  ? 2.2169 1.6475 1.8526 0.2756  -0.0688 -0.2085 249  ALA F CB  
17258 N  N   . LEU F 250  ? 2.0004 1.4787 1.6627 0.2853  -0.0634 -0.1930 250  LEU F N   
17259 C  CA  . LEU F 250  ? 1.8888 1.3811 1.5530 0.2941  -0.0597 -0.1853 250  LEU F CA  
17260 C  C   . LEU F 250  ? 1.7666 1.2894 1.4457 0.2973  -0.0617 -0.1835 250  LEU F C   
17261 O  O   . LEU F 250  ? 1.6713 1.2104 1.3498 0.3071  -0.0605 -0.1792 250  LEU F O   
17262 C  CB  . LEU F 250  ? 1.7558 1.2364 1.4213 0.2896  -0.0554 -0.1812 250  LEU F CB  
17263 C  CG  . LEU F 250  ? 1.6881 1.1383 1.3388 0.2866  -0.0521 -0.1815 250  LEU F CG  
17264 C  CD1 . LEU F 250  ? 1.6084 1.0489 1.2626 0.2808  -0.0480 -0.1777 250  LEU F CD1 
17265 C  CD2 . LEU F 250  ? 1.8194 1.2643 1.4545 0.2979  -0.0498 -0.1784 250  LEU F CD2 
17266 N  N   . PHE F 251  ? 2.4378 1.9703 2.1314 0.2882  -0.0647 -0.1862 251  PHE F N   
17267 C  CA  . PHE F 251  ? 2.3751 1.9392 2.0845 0.2886  -0.0666 -0.1839 251  PHE F CA  
17268 C  C   . PHE F 251  ? 2.3404 1.9119 2.0438 0.2965  -0.0697 -0.1878 251  PHE F C   
17269 O  O   . PHE F 251  ? 2.3168 1.9094 2.0246 0.3044  -0.0694 -0.1851 251  PHE F O   
17270 C  CB  . PHE F 251  ? 2.3646 1.9406 2.0927 0.2735  -0.0687 -0.1842 251  PHE F CB  
17271 C  CG  . PHE F 251  ? 2.3390 1.9174 2.0775 0.2666  -0.0654 -0.1790 251  PHE F CG  
17272 C  CD1 . PHE F 251  ? 2.4509 2.0050 2.1823 0.2617  -0.0626 -0.1789 251  PHE F CD1 
17273 C  CD2 . PHE F 251  ? 2.2420 1.8462 1.9969 0.2648  -0.0650 -0.1741 251  PHE F CD2 
17274 C  CE1 . PHE F 251  ? 2.2851 1.8411 2.0256 0.2556  -0.0593 -0.1740 251  PHE F CE1 
17275 C  CE2 . PHE F 251  ? 2.3077 1.9138 2.0717 0.2587  -0.0620 -0.1693 251  PHE F CE2 
17276 C  CZ  . PHE F 251  ? 2.2855 1.8676 2.0422 0.2542  -0.0591 -0.1692 251  PHE F CZ  
17277 N  N   . ARG F 252  ? 1.8420 1.3960 1.5350 0.2943  -0.0725 -0.1943 252  ARG F N   
17278 C  CA  . ARG F 252  ? 1.8642 1.4258 1.5525 0.2996  -0.0757 -0.1981 252  ARG F CA  
17279 C  C   . ARG F 252  ? 1.8322 1.4026 1.5124 0.3118  -0.0729 -0.1933 252  ARG F C   
17280 O  O   . ARG F 252  ? 1.8548 1.4417 1.5363 0.3172  -0.0744 -0.1938 252  ARG F O   
17281 C  CB  . ARG F 252  ? 2.0084 1.5479 1.6861 0.2942  -0.0788 -0.2051 252  ARG F CB  
17282 C  CG  . ARG F 252  ? 1.9766 1.5114 1.6650 0.2789  -0.0815 -0.2086 252  ARG F CG  
17283 C  CD  . ARG F 252  ? 1.9635 1.5233 1.6679 0.2728  -0.0857 -0.2096 252  ARG F CD  
17284 N  NE  . ARG F 252  ? 1.9039 1.4661 1.5997 0.2795  -0.0892 -0.2143 252  ARG F NE  
17285 C  CZ  . ARG F 252  ? 1.8879 1.4695 1.5933 0.2768  -0.0930 -0.2158 252  ARG F CZ  
17286 N  NH1 . ARG F 252  ? 1.8141 1.4148 1.5383 0.2677  -0.0939 -0.2131 252  ARG F NH1 
17287 N  NH2 . ARG F 252  ? 1.9019 1.4832 1.5972 0.2838  -0.0958 -0.2201 252  ARG F NH2 
17288 N  N   . GLU F 253  ? 2.0850 1.6450 1.7568 0.3161  -0.0688 -0.1888 253  GLU F N   
17289 C  CA  . GLU F 253  ? 2.0606 1.6266 1.7235 0.3276  -0.0664 -0.1848 253  GLU F CA  
17290 C  C   . GLU F 253  ? 2.0441 1.6307 1.7157 0.3333  -0.0634 -0.1779 253  GLU F C   
17291 O  O   . GLU F 253  ? 2.0932 1.6900 1.7601 0.3428  -0.0618 -0.1747 253  GLU F O   
17292 C  CB  . GLU F 253  ? 2.1622 1.7021 1.8076 0.3299  -0.0642 -0.1848 253  GLU F CB  
17293 C  CG  . GLU F 253  ? 2.2390 1.7558 1.8754 0.3231  -0.0669 -0.1916 253  GLU F CG  
17294 C  CD  . GLU F 253  ? 2.3578 1.8728 1.9828 0.3293  -0.0688 -0.1947 253  GLU F CD  
17295 O  OE1 . GLU F 253  ? 2.3828 1.9085 2.0031 0.3398  -0.0670 -0.1908 253  GLU F OE1 
17296 O  OE2 . GLU F 253  ? 2.4151 1.9181 2.0359 0.3237  -0.0721 -0.2011 253  GLU F OE2 
17297 N  N   . TYR F 254  ? 1.6733 1.2664 1.3574 0.3277  -0.0626 -0.1757 254  TYR F N   
17298 C  CA  . TYR F 254  ? 1.6448 1.2556 1.3366 0.3325  -0.0597 -0.1692 254  TYR F CA  
17299 C  C   . TYR F 254  ? 1.5950 1.2275 1.3053 0.3280  -0.0607 -0.1682 254  TYR F C   
17300 O  O   . TYR F 254  ? 1.5903 1.2397 1.3083 0.3316  -0.0586 -0.1630 254  TYR F O   
17301 C  CB  . TYR F 254  ? 1.7207 1.3145 1.4060 0.3322  -0.0563 -0.1655 254  TYR F CB  
17302 C  CG  . TYR F 254  ? 1.6666 1.2426 1.3338 0.3389  -0.0545 -0.1647 254  TYR F CG  
17303 C  CD1 . TYR F 254  ? 1.6962 1.2456 1.3510 0.3349  -0.0550 -0.1690 254  TYR F CD1 
17304 C  CD2 . TYR F 254  ? 1.6064 1.1924 1.2691 0.3491  -0.0523 -0.1598 254  TYR F CD2 
17305 C  CE1 . TYR F 254  ? 1.7458 1.2784 1.3838 0.3411  -0.0532 -0.1682 254  TYR F CE1 
17306 C  CE2 . TYR F 254  ? 1.6347 1.2044 1.2806 0.3557  -0.0508 -0.1591 254  TYR F CE2 
17307 C  CZ  . TYR F 254  ? 1.7165 1.2593 1.3498 0.3517  -0.0511 -0.1632 254  TYR F CZ  
17308 O  OH  . TYR F 254  ? 1.6110 1.1372 1.2273 0.3583  -0.0494 -0.1624 254  TYR F OH  
17309 N  N   . VAL F 255  ? 1.4931 1.1260 1.2108 0.3203  -0.0640 -0.1730 255  VAL F N   
17310 C  CA  . VAL F 255  ? 1.3547 1.0075 1.0904 0.3142  -0.0649 -0.1717 255  VAL F CA  
17311 C  C   . VAL F 255  ? 1.2554 0.9260 0.9976 0.3135  -0.0679 -0.1743 255  VAL F C   
17312 O  O   . VAL F 255  ? 1.2578 0.9183 0.9940 0.3107  -0.0710 -0.1796 255  VAL F O   
17313 C  CB  . VAL F 255  ? 1.3097 0.9531 1.0535 0.2997  -0.0654 -0.1718 255  VAL F CB  
17314 C  CG1 . VAL F 255  ? 1.3661 1.0334 1.1300 0.2901  -0.0669 -0.1698 255  VAL F CG1 
17315 C  CG2 . VAL F 255  ? 1.2840 0.9139 1.0237 0.3004  -0.0617 -0.1679 255  VAL F CG2 
17316 N  N   . SER F 256  ? 1.3525 1.0492 1.1067 0.3159  -0.0671 -0.1706 256  SER F N   
17317 C  CA  . SER F 256  ? 1.3367 1.0522 1.0979 0.3153  -0.0692 -0.1721 256  SER F CA  
17318 C  C   . SER F 256  ? 1.4055 1.1387 1.1858 0.3037  -0.0701 -0.1696 256  SER F C   
17319 O  O   . SER F 256  ? 1.4729 1.2003 1.2597 0.2947  -0.0698 -0.1679 256  SER F O   
17320 C  CB  . SER F 256  ? 1.3636 1.0944 1.1221 0.3282  -0.0670 -0.1703 256  SER F CB  
17321 O  OG  . SER F 256  ? 1.3957 1.1398 1.1624 0.3304  -0.0639 -0.1646 256  SER F OG  
17322 N  N   . VAL F 257  ? 1.5703 1.3247 1.3591 0.3039  -0.0709 -0.1691 257  VAL F N   
17323 C  CA  . VAL F 257  ? 1.5351 1.3070 1.3413 0.2938  -0.0717 -0.1667 257  VAL F CA  
17324 C  C   . VAL F 257  ? 1.5316 1.3203 1.3489 0.2946  -0.0684 -0.1606 257  VAL F C   
17325 O  O   . VAL F 257  ? 1.5483 1.3489 1.3797 0.2858  -0.0686 -0.1581 257  VAL F O   
17326 C  CB  . VAL F 257  ? 1.5282 1.3150 1.3384 0.2934  -0.0738 -0.1686 257  VAL F CB  
17327 C  CG1 . VAL F 257  ? 1.6876 1.4592 1.4896 0.2898  -0.0780 -0.1748 257  VAL F CG1 
17328 C  CG2 . VAL F 257  ? 1.4314 1.2303 1.2368 0.3055  -0.0715 -0.1676 257  VAL F CG2 
17329 N  N   . LYS F 258  ? 1.6495 1.4396 1.4606 0.3052  -0.0655 -0.1585 258  LYS F N   
17330 C  CA  . LYS F 258  ? 1.6540 1.4605 1.4755 0.3063  -0.0627 -0.1531 258  LYS F CA  
17331 C  C   . LYS F 258  ? 1.5767 1.3750 1.4034 0.2985  -0.0620 -0.1504 258  LYS F C   
17332 O  O   . LYS F 258  ? 1.5355 1.3489 1.3761 0.2924  -0.0612 -0.1468 258  LYS F O   
17333 C  CB  . LYS F 258  ? 1.6803 1.4901 1.4936 0.3200  -0.0602 -0.1520 258  LYS F CB  
17334 C  CG  . LYS F 258  ? 1.6320 1.4581 1.4549 0.3221  -0.0575 -0.1470 258  LYS F CG  
17335 C  CD  . LYS F 258  ? 1.6594 1.4885 1.4741 0.3341  -0.0553 -0.1455 258  LYS F CD  
17336 C  CE  . LYS F 258  ? 1.7320 1.5795 1.5570 0.3350  -0.0531 -0.1403 258  LYS F CE  
17337 N  NZ  . LYS F 258  ? 1.6612 1.5329 1.5015 0.3318  -0.0527 -0.1394 258  LYS F NZ  
17338 N  N   . PRO F 259  ? 1.5941 1.3686 1.4101 0.2983  -0.0619 -0.1518 259  PRO F N   
17339 C  CA  . PRO F 259  ? 1.7000 1.4672 1.5216 0.2901  -0.0607 -0.1490 259  PRO F CA  
17340 C  C   . PRO F 259  ? 1.6751 1.4475 1.5098 0.2765  -0.0627 -0.1494 259  PRO F C   
17341 O  O   . PRO F 259  ? 1.7360 1.5151 1.5815 0.2700  -0.0614 -0.1457 259  PRO F O   
17342 C  CB  . PRO F 259  ? 1.7227 1.4614 1.5284 0.2927  -0.0602 -0.1514 259  PRO F CB  
17343 C  CG  . PRO F 259  ? 1.6675 1.4025 1.4595 0.3056  -0.0601 -0.1536 259  PRO F CG  
17344 C  CD  . PRO F 259  ? 1.6668 1.4201 1.4647 0.3062  -0.0621 -0.1554 259  PRO F CD  
17345 N  N   . ILE F 260  ? 1.2566 1.0262 1.0903 0.2725  -0.0658 -0.1539 260  ILE F N   
17346 C  CA  . ILE F 260  ? 1.2524 1.0282 1.0987 0.2602  -0.0681 -0.1546 260  ILE F CA  
17347 C  C   . ILE F 260  ? 1.2681 1.0699 1.1290 0.2583  -0.0676 -0.1510 260  ILE F C   
17348 O  O   . ILE F 260  ? 1.2771 1.0865 1.1506 0.2492  -0.0676 -0.1488 260  ILE F O   
17349 C  CB  . ILE F 260  ? 1.2920 1.0592 1.1329 0.2574  -0.0720 -0.1607 260  ILE F CB  
17350 C  CG1 . ILE F 260  ? 1.3894 1.1300 1.2145 0.2600  -0.0722 -0.1645 260  ILE F CG1 
17351 C  CG2 . ILE F 260  ? 1.3503 1.1228 1.2040 0.2447  -0.0746 -0.1618 260  ILE F CG2 
17352 C  CD1 . ILE F 260  ? 1.4437 1.1754 1.2608 0.2596  -0.0761 -0.1708 260  ILE F CD1 
17353 N  N   . HIS F 261  ? 1.3662 1.1820 1.2256 0.2670  -0.0669 -0.1504 261  HIS F N   
17354 C  CA  . HIS F 261  ? 1.3404 1.1805 1.2130 0.2655  -0.0659 -0.1469 261  HIS F CA  
17355 C  C   . HIS F 261  ? 1.4195 1.2668 1.2997 0.2649  -0.0629 -0.1417 261  HIS F C   
17356 O  O   . HIS F 261  ? 1.3784 1.2401 1.2719 0.2583  -0.0624 -0.1387 261  HIS F O   
17357 C  CB  . HIS F 261  ? 1.3138 1.1661 1.1824 0.2751  -0.0653 -0.1476 261  HIS F CB  
17358 C  CG  . HIS F 261  ? 1.3619 1.2370 1.2428 0.2723  -0.0649 -0.1455 261  HIS F CG  
17359 N  ND1 . HIS F 261  ? 1.4202 1.3129 1.3098 0.2743  -0.0620 -0.1411 261  HIS F ND1 
17360 C  CD2 . HIS F 261  ? 1.4211 1.3039 1.3066 0.2676  -0.0670 -0.1472 261  HIS F CD2 
17361 C  CE1 . HIS F 261  ? 1.4299 1.3394 1.3287 0.2707  -0.0620 -0.1401 261  HIS F CE1 
17362 N  NE2 . HIS F 261  ? 1.4000 1.3038 1.2963 0.2669  -0.0650 -0.1436 261  HIS F NE2 
17363 N  N   . ASP F 262  ? 1.8249 1.6621 1.6964 0.2720  -0.0609 -0.1405 262  ASP F N   
17364 C  CA  . ASP F 262  ? 1.7600 1.6032 1.6373 0.2722  -0.0582 -0.1357 262  ASP F CA  
17365 C  C   . ASP F 262  ? 1.7410 1.5763 1.6250 0.2613  -0.0581 -0.1342 262  ASP F C   
17366 O  O   . ASP F 262  ? 1.7695 1.6167 1.6645 0.2570  -0.0568 -0.1303 262  ASP F O   
17367 C  CB  . ASP F 262  ? 1.7328 1.5657 1.5978 0.2831  -0.0564 -0.1352 262  ASP F CB  
17368 C  CG  . ASP F 262  ? 1.8337 1.6763 1.6931 0.2944  -0.0560 -0.1364 262  ASP F CG  
17369 O  OD1 . ASP F 262  ? 1.8274 1.6853 1.6929 0.2935  -0.0568 -0.1374 262  ASP F OD1 
17370 O  OD2 . ASP F 262  ? 1.9265 1.7615 1.7752 0.3044  -0.0547 -0.1363 262  ASP F OD2 
17371 N  N   . ILE F 263  ? 1.2822 1.0974 1.1597 0.2566  -0.0595 -0.1373 263  ILE F N   
17372 C  CA  . ILE F 263  ? 1.2852 1.0926 1.1693 0.2459  -0.0591 -0.1361 263  ILE F CA  
17373 C  C   . ILE F 263  ? 1.3097 1.1325 1.2086 0.2362  -0.0609 -0.1359 263  ILE F C   
17374 O  O   . ILE F 263  ? 1.3222 1.1500 1.2315 0.2289  -0.0597 -0.1328 263  ILE F O   
17375 C  CB  . ILE F 263  ? 1.2581 1.0398 1.1313 0.2434  -0.0598 -0.1398 263  ILE F CB  
17376 C  CG1 . ILE F 263  ? 1.3350 1.1003 1.1954 0.2511  -0.0570 -0.1382 263  ILE F CG1 
17377 C  CG2 . ILE F 263  ? 1.2174 0.9939 1.0996 0.2304  -0.0604 -0.1402 263  ILE F CG2 
17378 C  CD1 . ILE F 263  ? 1.5218 1.2605 1.3689 0.2502  -0.0572 -0.1420 263  ILE F CD1 
17379 N  N   . GLY F 264  ? 1.3687 1.1991 1.2684 0.2365  -0.0636 -0.1391 264  GLY F N   
17380 C  CA  . GLY F 264  ? 1.3612 1.2076 1.2742 0.2288  -0.0652 -0.1386 264  GLY F CA  
17381 C  C   . GLY F 264  ? 1.3283 1.1952 1.2518 0.2297  -0.0630 -0.1337 264  GLY F C   
17382 O  O   . GLY F 264  ? 1.2592 1.1355 1.1947 0.2218  -0.0629 -0.1316 264  GLY F O   
17383 N  N   . LYS F 265  ? 1.2060 1.0801 1.1251 0.2392  -0.0611 -0.1321 265  LYS F N   
17384 C  CA  . LYS F 265  ? 1.1953 1.0883 1.1239 0.2402  -0.0588 -0.1277 265  LYS F CA  
17385 C  C   . LYS F 265  ? 1.1221 1.0114 1.0550 0.2365  -0.0567 -0.1239 265  LYS F C   
17386 O  O   . LYS F 265  ? 1.0116 0.9145 0.9557 0.2320  -0.0556 -0.1206 265  LYS F O   
17387 C  CB  . LYS F 265  ? 1.2514 1.1527 1.1743 0.2514  -0.0574 -0.1273 265  LYS F CB  
17388 C  CG  . LYS F 265  ? 1.2081 1.1197 1.1301 0.2549  -0.0585 -0.1297 265  LYS F CG  
17389 C  CD  . LYS F 265  ? 1.1757 1.0971 1.0935 0.2657  -0.0564 -0.1291 265  LYS F CD  
17390 C  CE  . LYS F 265  ? 1.1039 1.0086 1.0070 0.2745  -0.0564 -0.1313 265  LYS F CE  
17391 N  NZ  . LYS F 265  ? 1.0183 0.9327 0.9167 0.2855  -0.0548 -0.1316 265  LYS F NZ  
17392 N  N   . LEU F 266  ? 1.3005 1.1708 1.2241 0.2384  -0.0560 -0.1244 266  LEU F N   
17393 C  CA  . LEU F 266  ? 1.2973 1.1618 1.2235 0.2350  -0.0538 -0.1209 266  LEU F CA  
17394 C  C   . LEU F 266  ? 1.2150 1.0785 1.1513 0.2229  -0.0543 -0.1205 266  LEU F C   
17395 O  O   . LEU F 266  ? 1.1770 1.0467 1.1217 0.2185  -0.0525 -0.1167 266  LEU F O   
17396 C  CB  . LEU F 266  ? 1.2388 1.0815 1.1511 0.2402  -0.0526 -0.1217 266  LEU F CB  
17397 C  CG  . LEU F 266  ? 1.1926 1.0368 1.0963 0.2523  -0.0511 -0.1202 266  LEU F CG  
17398 C  CD1 . LEU F 266  ? 1.3611 1.1812 1.2492 0.2576  -0.0503 -0.1217 266  LEU F CD1 
17399 C  CD2 . LEU F 266  ? 1.1392 0.9958 1.0505 0.2527  -0.0490 -0.1155 266  LEU F CD2 
17400 N  N   . ILE F 267  ? 0.9189 0.7749 0.8547 0.2175  -0.0568 -0.1244 267  ILE F N   
17401 C  CA  . ILE F 267  ? 0.8753 0.7320 0.8215 0.2062  -0.0577 -0.1245 267  ILE F CA  
17402 C  C   . ILE F 267  ? 0.8661 0.7448 0.8255 0.2028  -0.0579 -0.1220 267  ILE F C   
17403 O  O   . ILE F 267  ? 0.9019 0.7857 0.8713 0.1956  -0.0569 -0.1193 267  ILE F O   
17404 C  CB  . ILE F 267  ? 0.8592 0.7046 0.8019 0.2019  -0.0609 -0.1298 267  ILE F CB  
17405 C  CG1 . ILE F 267  ? 1.0499 0.8713 0.9808 0.2028  -0.0600 -0.1319 267  ILE F CG1 
17406 C  CG2 . ILE F 267  ? 0.8315 0.6829 0.7869 0.1908  -0.0624 -0.1303 267  ILE F CG2 
17407 C  CD1 . ILE F 267  ? 1.1614 0.9707 1.0876 0.1991  -0.0632 -0.1377 267  ILE F CD1 
17408 N  N   . PHE F 268  ? 1.0885 0.9802 1.0476 0.2080  -0.0591 -0.1229 268  PHE F N   
17409 C  CA  . PHE F 268  ? 1.0680 0.9801 1.0385 0.2054  -0.0589 -0.1205 268  PHE F CA  
17410 C  C   . PHE F 268  ? 1.0356 0.9568 1.0116 0.2064  -0.0558 -0.1156 268  PHE F C   
17411 O  O   . PHE F 268  ? 0.9995 0.9313 0.9863 0.2003  -0.0551 -0.1130 268  PHE F O   
17412 C  CB  . PHE F 268  ? 1.0910 1.0136 1.0584 0.2116  -0.0601 -0.1224 268  PHE F CB  
17413 C  CG  . PHE F 268  ? 1.0073 0.9502 0.9849 0.2100  -0.0593 -0.1198 268  PHE F CG  
17414 C  CD1 . PHE F 268  ? 0.9758 0.9254 0.9616 0.2027  -0.0610 -0.1202 268  PHE F CD1 
17415 C  CD2 . PHE F 268  ? 0.9881 0.9435 0.9670 0.2158  -0.0568 -0.1170 268  PHE F CD2 
17416 C  CE1 . PHE F 268  ? 0.9192 0.8861 0.9133 0.2014  -0.0600 -0.1177 268  PHE F CE1 
17417 C  CE2 . PHE F 268  ? 0.9837 0.9570 0.9716 0.2138  -0.0557 -0.1147 268  PHE F CE2 
17418 C  CZ  . PHE F 268  ? 0.9271 0.9055 0.9222 0.2067  -0.0572 -0.1149 268  PHE F CZ  
17419 N  N   . ALA F 269  ? 1.0703 0.9874 1.0386 0.2143  -0.0540 -0.1145 269  ALA F N   
17420 C  CA  . ALA F 269  ? 0.9883 0.9145 0.9611 0.2160  -0.0515 -0.1102 269  ALA F CA  
17421 C  C   . ALA F 269  ? 0.8746 0.7922 0.8511 0.2094  -0.0500 -0.1076 269  ALA F C   
17422 O  O   . ALA F 269  ? 0.9083 0.8362 0.8931 0.2065  -0.0484 -0.1041 269  ALA F O   
17423 C  CB  . ALA F 269  ? 1.0028 0.9269 0.9660 0.2269  -0.0503 -0.1100 269  ALA F CB  
17424 N  N   . PHE F 270  ? 0.8932 0.7919 0.8635 0.2068  -0.0502 -0.1094 270  PHE F N   
17425 C  CA  . PHE F 270  ? 0.9786 0.8682 0.9520 0.2002  -0.0484 -0.1070 270  PHE F CA  
17426 C  C   . PHE F 270  ? 1.0000 0.8965 0.9858 0.1898  -0.0492 -0.1068 270  PHE F C   
17427 O  O   . PHE F 270  ? 1.0806 0.9771 1.0727 0.1842  -0.0472 -0.1039 270  PHE F O   
17428 C  CB  . PHE F 270  ? 1.0786 0.9450 1.0411 0.2007  -0.0478 -0.1090 270  PHE F CB  
17429 C  CG  . PHE F 270  ? 1.0972 0.9539 1.0505 0.2076  -0.0452 -0.1064 270  PHE F CG  
17430 C  CD1 . PHE F 270  ? 1.0883 0.9455 1.0321 0.2186  -0.0454 -0.1070 270  PHE F CD1 
17431 C  CD2 . PHE F 270  ? 1.1063 0.9535 1.0601 0.2035  -0.0424 -0.1034 270  PHE F CD2 
17432 C  CE1 . PHE F 270  ? 1.0932 0.9419 1.0282 0.2256  -0.0432 -0.1047 270  PHE F CE1 
17433 C  CE2 . PHE F 270  ? 1.1144 0.9523 1.0588 0.2104  -0.0400 -0.1010 270  PHE F CE2 
17434 C  CZ  . PHE F 270  ? 1.1322 0.9708 1.0670 0.2216  -0.0406 -0.1017 270  PHE F CZ  
17435 N  N   . THR F 271  ? 0.9775 0.8802 0.9667 0.1873  -0.0520 -0.1100 271  THR F N   
17436 C  CA  . THR F 271  ? 0.9728 0.8838 0.9738 0.1783  -0.0531 -0.1098 271  THR F CA  
17437 C  C   . THR F 271  ? 1.0290 0.9586 1.0395 0.1776  -0.0517 -0.1059 271  THR F C   
17438 O  O   . THR F 271  ? 1.0995 1.0328 1.1188 0.1709  -0.0505 -0.1035 271  THR F O   
17439 C  CB  . THR F 271  ? 0.9937 0.9063 0.9946 0.1769  -0.0567 -0.1143 271  THR F CB  
17440 O  OG1 . THR F 271  ? 1.0125 0.9073 1.0071 0.1745  -0.0581 -0.1181 271  THR F OG1 
17441 C  CG2 . THR F 271  ? 0.9496 0.8750 0.9627 0.1695  -0.0580 -0.1138 271  THR F CG2 
17442 N  N   . VAL F 272  ? 1.0176 0.9588 1.0263 0.1844  -0.0517 -0.1054 272  VAL F N   
17443 C  CA  . VAL F 272  ? 0.9560 0.9143 0.9732 0.1838  -0.0502 -0.1019 272  VAL F CA  
17444 C  C   . VAL F 272  ? 0.9958 0.9526 1.0132 0.1849  -0.0473 -0.0981 272  VAL F C   
17445 O  O   . VAL F 272  ? 0.9849 0.9524 1.0106 0.1817  -0.0459 -0.0950 272  VAL F O   
17446 C  CB  . VAL F 272  ? 0.8229 0.7941 0.8384 0.1903  -0.0506 -0.1027 272  VAL F CB  
17447 C  CG1 . VAL F 272  ? 0.8220 0.7940 0.8364 0.1893  -0.0534 -0.1063 272  VAL F CG1 
17448 C  CG2 . VAL F 272  ? 0.8983 0.8651 0.9040 0.1996  -0.0497 -0.1031 272  VAL F CG2 
17449 N  N   . LEU F 273  ? 1.0130 0.9560 1.0209 0.1896  -0.0464 -0.0984 273  LEU F N   
17450 C  CA  . LEU F 273  ? 1.0111 0.9510 1.0181 0.1909  -0.0439 -0.0948 273  LEU F CA  
17451 C  C   . LEU F 273  ? 1.0045 0.9378 1.0174 0.1821  -0.0425 -0.0930 273  LEU F C   
17452 O  O   . LEU F 273  ? 1.0245 0.9640 1.0431 0.1798  -0.0406 -0.0895 273  LEU F O   
17453 C  CB  . LEU F 273  ? 0.9120 0.8376 0.9061 0.1988  -0.0433 -0.0956 273  LEU F CB  
17454 C  CG  . LEU F 273  ? 0.9638 0.8856 0.9550 0.2019  -0.0408 -0.0921 273  LEU F CG  
17455 C  CD1 . LEU F 273  ? 1.0352 0.9756 1.0315 0.2058  -0.0404 -0.0899 273  LEU F CD1 
17456 C  CD2 . LEU F 273  ? 1.0635 0.9682 1.0406 0.2094  -0.0402 -0.0931 273  LEU F CD2 
17457 N  N   . TRP F 274  ? 0.9694 0.8902 0.9811 0.1770  -0.0434 -0.0955 274  TRP F N   
17458 C  CA  . TRP F 274  ? 1.0242 0.9394 1.0424 0.1683  -0.0419 -0.0940 274  TRP F CA  
17459 C  C   . TRP F 274  ? 0.9957 0.9271 1.0268 0.1622  -0.0423 -0.0925 274  TRP F C   
17460 O  O   . TRP F 274  ? 0.9748 0.9080 1.0119 0.1576  -0.0400 -0.0893 274  TRP F O   
17461 C  CB  . TRP F 274  ? 0.9521 0.8524 0.9675 0.1637  -0.0432 -0.0977 274  TRP F CB  
17462 C  CG  . TRP F 274  ? 1.0170 0.9162 1.0421 0.1536  -0.0424 -0.0972 274  TRP F CG  
17463 C  CD1 . TRP F 274  ? 1.0356 0.9242 1.0614 0.1491  -0.0392 -0.0951 274  TRP F CD1 
17464 C  CD2 . TRP F 274  ? 1.0565 0.9659 1.0919 0.1471  -0.0448 -0.0990 274  TRP F CD2 
17465 N  NE1 . TRP F 274  ? 1.0726 0.9648 1.1093 0.1400  -0.0394 -0.0954 274  TRP F NE1 
17466 C  CE2 . TRP F 274  ? 1.0591 0.9642 1.1018 0.1388  -0.0430 -0.0979 274  TRP F CE2 
17467 C  CE3 . TRP F 274  ? 1.0259 0.9476 1.0648 0.1478  -0.0482 -0.1013 274  TRP F CE3 
17468 C  CZ2 . TRP F 274  ? 1.1439 1.0573 1.1977 0.1314  -0.0447 -0.0992 274  TRP F CZ2 
17469 C  CZ3 . TRP F 274  ? 1.0283 0.9573 1.0773 0.1407  -0.0499 -0.1025 274  TRP F CZ3 
17470 C  CH2 . TRP F 274  ? 1.0877 1.0129 1.1443 0.1327  -0.0483 -0.1015 274  TRP F CH2 
17471 N  N   . THR F 275  ? 0.8569 0.7998 0.8916 0.1624  -0.0449 -0.0946 275  THR F N   
17472 C  CA  . THR F 275  ? 0.9270 0.8850 0.9728 0.1574  -0.0451 -0.0930 275  THR F CA  
17473 C  C   . THR F 275  ? 0.8386 0.8079 0.8874 0.1599  -0.0429 -0.0890 275  THR F C   
17474 O  O   . THR F 275  ? 0.6591 0.6361 0.7164 0.1549  -0.0416 -0.0864 275  THR F O   
17475 C  CB  . THR F 275  ? 0.8742 0.8411 0.9213 0.1583  -0.0482 -0.0960 275  THR F CB  
17476 O  OG1 . THR F 275  ? 0.8715 0.8273 0.9145 0.1568  -0.0506 -0.1002 275  THR F OG1 
17477 C  CG2 . THR F 275  ? 0.6950 0.6753 0.7529 0.1526  -0.0485 -0.0946 275  THR F CG2 
17478 N  N   . TYR F 276  ? 1.2306 1.2013 1.2726 0.1677  -0.0424 -0.0887 276  TYR F N   
17479 C  CA  . TYR F 276  ? 1.1023 1.0842 1.1470 0.1704  -0.0405 -0.0854 276  TYR F CA  
17480 C  C   . TYR F 276  ? 1.1288 1.1038 1.1739 0.1681  -0.0380 -0.0821 276  TYR F C   
17481 O  O   . TYR F 276  ? 1.2094 1.1936 1.2610 0.1656  -0.0365 -0.0792 276  TYR F O   
17482 C  CB  . TYR F 276  ? 1.0989 1.0842 1.1363 0.1796  -0.0409 -0.0863 276  TYR F CB  
17483 C  CG  . TYR F 276  ? 1.1068 1.0967 1.1432 0.1838  -0.0390 -0.0834 276  TYR F CG  
17484 C  CD1 . TYR F 276  ? 1.0309 1.0364 1.0750 0.1823  -0.0381 -0.0813 276  TYR F CD1 
17485 C  CD2 . TYR F 276  ? 1.1636 1.1420 1.1911 0.1893  -0.0383 -0.0830 276  TYR F CD2 
17486 C  CE1 . TYR F 276  ? 0.9953 1.0055 1.0387 0.1861  -0.0368 -0.0791 276  TYR F CE1 
17487 C  CE2 . TYR F 276  ? 1.1000 1.0829 1.1263 0.1936  -0.0370 -0.0806 276  TYR F CE2 
17488 C  CZ  . TYR F 276  ? 1.0630 1.0622 1.0975 0.1919  -0.0364 -0.0788 276  TYR F CZ  
17489 O  OH  . TYR F 276  ? 1.1373 1.1413 1.1707 0.1961  -0.0355 -0.0768 276  TYR F OH  
17490 N  N   . MET F 277  ? 1.1219 1.0801 1.1597 0.1690  -0.0372 -0.0826 277  MET F N   
17491 C  CA  . MET F 277  ? 1.1428 1.0928 1.1801 0.1668  -0.0344 -0.0794 277  MET F CA  
17492 C  C   . MET F 277  ? 1.0641 1.0157 1.1112 0.1575  -0.0334 -0.0781 277  MET F C   
17493 O  O   . MET F 277  ? 0.9562 0.9117 1.0077 0.1551  -0.0313 -0.0747 277  MET F O   
17494 C  CB  . MET F 277  ? 1.1496 1.0799 1.1761 0.1697  -0.0335 -0.0803 277  MET F CB  
17495 C  CG  . MET F 277  ? 1.2433 1.1705 1.2591 0.1795  -0.0346 -0.0818 277  MET F CG  
17496 S  SD  . MET F 277  ? 1.3887 1.2951 1.3914 0.1845  -0.0320 -0.0803 277  MET F SD  
17497 C  CE  . MET F 277  ? 1.1665 1.0838 1.1703 0.1892  -0.0306 -0.0762 277  MET F CE  
17498 N  N   . SER F 278  ? 0.9604 0.9091 1.0111 0.1522  -0.0350 -0.0808 278  SER F N   
17499 C  CA  . SER F 278  ? 0.8402 0.7905 0.9005 0.1435  -0.0342 -0.0799 278  SER F CA  
17500 C  C   . SER F 278  ? 0.9137 0.8814 0.9833 0.1414  -0.0343 -0.0779 278  SER F C   
17501 O  O   . SER F 278  ? 0.8522 0.8224 0.9282 0.1366  -0.0322 -0.0751 278  SER F O   
17502 C  CB  . SER F 278  ? 0.8991 0.8439 0.9612 0.1390  -0.0365 -0.0838 278  SER F CB  
17503 O  OG  . SER F 278  ? 1.1927 1.1467 1.2551 0.1415  -0.0398 -0.0866 278  SER F OG  
17504 N  N   . TYR F 279  ? 0.9928 0.9721 1.0629 0.1448  -0.0365 -0.0792 279  TYR F N   
17505 C  CA  . TYR F 279  ? 0.8697 0.8647 0.9475 0.1431  -0.0362 -0.0773 279  TYR F CA  
17506 C  C   . TYR F 279  ? 0.8591 0.8584 0.9366 0.1454  -0.0337 -0.0737 279  TYR F C   
17507 O  O   . TYR F 279  ? 0.8984 0.9055 0.9828 0.1417  -0.0324 -0.0712 279  TYR F O   
17508 C  CB  . TYR F 279  ? 0.8610 0.8664 0.9384 0.1465  -0.0386 -0.0795 279  TYR F CB  
17509 C  CG  . TYR F 279  ? 0.8911 0.9119 0.9746 0.1459  -0.0377 -0.0773 279  TYR F CG  
17510 C  CD1 . TYR F 279  ? 0.9102 0.9372 1.0020 0.1399  -0.0374 -0.0760 279  TYR F CD1 
17511 C  CD2 . TYR F 279  ? 0.9386 0.9675 1.0194 0.1514  -0.0370 -0.0765 279  TYR F CD2 
17512 C  CE1 . TYR F 279  ? 0.8642 0.9039 0.9607 0.1392  -0.0364 -0.0740 279  TYR F CE1 
17513 C  CE2 . TYR F 279  ? 0.9144 0.9567 1.0007 0.1503  -0.0360 -0.0746 279  TYR F CE2 
17514 C  CZ  . TYR F 279  ? 0.8682 0.9152 0.9619 0.1442  -0.0356 -0.0733 279  TYR F CZ  
17515 O  OH  . TYR F 279  ? 0.9277 0.9869 1.0262 0.1431  -0.0343 -0.0714 279  TYR F OH  
17516 N  N   . GLY F 280  ? 1.2258 1.2200 1.2951 0.1519  -0.0333 -0.0736 280  GLY F N   
17517 C  CA  . GLY F 280  ? 1.3236 1.3216 1.3921 0.1546  -0.0313 -0.0705 280  GLY F CA  
17518 C  C   . GLY F 280  ? 1.2840 1.2749 1.3548 0.1499  -0.0287 -0.0676 280  GLY F C   
17519 O  O   . GLY F 280  ? 1.2054 1.2038 1.2808 0.1481  -0.0273 -0.0649 280  GLY F O   
17520 N  N   . GLN F 281  ? 1.0132 0.9891 1.0806 0.1477  -0.0279 -0.0681 281  GLN F N   
17521 C  CA  . GLN F 281  ? 0.9743 0.9429 1.0442 0.1427  -0.0249 -0.0653 281  GLN F CA  
17522 C  C   . GLN F 281  ? 1.0086 0.9863 1.0896 0.1353  -0.0246 -0.0644 281  GLN F C   
17523 O  O   . GLN F 281  ? 1.0343 1.0139 1.1191 0.1325  -0.0222 -0.0613 281  GLN F O   
17524 C  CB  . GLN F 281  ? 1.0794 1.0301 1.1439 0.1410  -0.0239 -0.0664 281  GLN F CB  
17525 C  CG  . GLN F 281  ? 0.9846 0.9274 1.0523 0.1351  -0.0203 -0.0638 281  GLN F CG  
17526 C  CD  . GLN F 281  ? 1.1210 1.0465 1.1846 0.1322  -0.0190 -0.0653 281  GLN F CD  
17527 O  OE1 . GLN F 281  ? 1.2049 1.1203 1.2593 0.1367  -0.0199 -0.0672 281  GLN F OE1 
17528 N  NE2 . GLN F 281  ? 1.1122 1.0342 1.1826 0.1246  -0.0168 -0.0644 281  GLN F NE2 
17529 N  N   . LEU F 282  ? 0.8961 0.8795 0.9821 0.1326  -0.0271 -0.0671 282  LEU F N   
17530 C  CA  . LEU F 282  ? 0.8676 0.8593 0.9638 0.1261  -0.0270 -0.0664 282  LEU F CA  
17531 C  C   . LEU F 282  ? 0.7422 0.7477 0.8425 0.1268  -0.0264 -0.0640 282  LEU F C   
17532 O  O   . LEU F 282  ? 0.6846 0.6931 0.7905 0.1227  -0.0244 -0.0614 282  LEU F O   
17533 C  CB  . LEU F 282  ? 0.8462 0.8407 0.9454 0.1241  -0.0302 -0.0701 282  LEU F CB  
17534 C  CG  . LEU F 282  ? 0.7036 0.7095 0.8125 0.1192  -0.0310 -0.0699 282  LEU F CG  
17535 C  CD1 . LEU F 282  ? 0.6313 0.6339 0.7470 0.1127  -0.0287 -0.0681 282  LEU F CD1 
17536 C  CD2 . LEU F 282  ? 0.8149 0.8231 0.9247 0.1188  -0.0347 -0.0739 282  LEU F CD2 
17537 N  N   . VAL F 283  ? 0.6484 0.6622 0.7459 0.1319  -0.0279 -0.0649 283  VAL F N   
17538 C  CA  . VAL F 283  ? 0.6099 0.6370 0.7115 0.1321  -0.0273 -0.0630 283  VAL F CA  
17539 C  C   . VAL F 283  ? 0.6158 0.6417 0.7157 0.1332  -0.0248 -0.0598 283  VAL F C   
17540 O  O   . VAL F 283  ? 0.6440 0.6777 0.7488 0.1308  -0.0235 -0.0576 283  VAL F O   
17541 C  CB  . VAL F 283  ? 0.6721 0.7083 0.7712 0.1370  -0.0292 -0.0650 283  VAL F CB  
17542 C  CG1 . VAL F 283  ? 0.7617 0.7936 0.8525 0.1439  -0.0294 -0.0657 283  VAL F CG1 
17543 C  CG2 . VAL F 283  ? 0.6383 0.6882 0.7425 0.1359  -0.0284 -0.0633 283  VAL F CG2 
17544 N  N   . ILE F 284  ? 0.7534 0.7692 0.8458 0.1372  -0.0241 -0.0596 284  ILE F N   
17545 C  CA  . ILE F 284  ? 0.8297 0.8436 0.9195 0.1388  -0.0219 -0.0567 284  ILE F CA  
17546 C  C   . ILE F 284  ? 0.7503 0.7594 0.8447 0.1327  -0.0192 -0.0541 284  ILE F C   
17547 O  O   . ILE F 284  ? 0.7770 0.7909 0.8738 0.1315  -0.0176 -0.0515 284  ILE F O   
17548 C  CB  . ILE F 284  ? 0.8390 0.8421 0.9187 0.1451  -0.0219 -0.0571 284  ILE F CB  
17549 C  CG1 . ILE F 284  ? 0.7978 0.8090 0.8737 0.1519  -0.0241 -0.0590 284  ILE F CG1 
17550 C  CG2 . ILE F 284  ? 0.7119 0.7088 0.7880 0.1460  -0.0193 -0.0539 284  ILE F CG2 
17551 C  CD1 . ILE F 284  ? 0.9401 0.9411 1.0056 0.1590  -0.0244 -0.0597 284  ILE F CD1 
17552 N  N   . ILE F 285  ? 0.8063 0.8059 0.9020 0.1287  -0.0187 -0.0548 285  ILE F N   
17553 C  CA  . ILE F 285  ? 0.7900 0.7854 0.8907 0.1228  -0.0159 -0.0526 285  ILE F CA  
17554 C  C   . ILE F 285  ? 0.7433 0.7504 0.8538 0.1178  -0.0163 -0.0522 285  ILE F C   
17555 O  O   . ILE F 285  ? 0.7428 0.7516 0.8577 0.1143  -0.0139 -0.0496 285  ILE F O   
17556 C  CB  . ILE F 285  ? 0.8125 0.7941 0.9117 0.1199  -0.0151 -0.0538 285  ILE F CB  
17557 C  CG1 . ILE F 285  ? 0.7468 0.7147 0.8353 0.1246  -0.0136 -0.0531 285  ILE F CG1 
17558 C  CG2 . ILE F 285  ? 0.7592 0.7387 0.8659 0.1128  -0.0124 -0.0521 285  ILE F CG2 
17559 C  CD1 . ILE F 285  ? 0.8288 0.7814 0.9152 0.1213  -0.0119 -0.0540 285  ILE F CD1 
17560 N  N   . TRP F 286  ? 0.7417 0.7569 0.8552 0.1179  -0.0192 -0.0548 286  TRP F N   
17561 C  CA  . TRP F 286  ? 0.7879 0.8131 0.9098 0.1136  -0.0197 -0.0546 286  TRP F CA  
17562 C  C   . TRP F 286  ? 0.8195 0.8551 0.9432 0.1144  -0.0187 -0.0523 286  TRP F C   
17563 O  O   . TRP F 286  ? 0.8086 0.8475 0.9377 0.1105  -0.0170 -0.0502 286  TRP F O   
17564 C  CB  . TRP F 286  ? 0.7867 0.8164 0.9098 0.1140  -0.0231 -0.0581 286  TRP F CB  
17565 C  CG  . TRP F 286  ? 0.6859 0.7245 0.8168 0.1101  -0.0240 -0.0583 286  TRP F CG  
17566 C  CD1 . TRP F 286  ? 0.7168 0.7540 0.8541 0.1050  -0.0242 -0.0589 286  TRP F CD1 
17567 C  CD2 . TRP F 286  ? 0.6753 0.7257 0.8083 0.1110  -0.0248 -0.0580 286  TRP F CD2 
17568 N  NE1 . TRP F 286  ? 0.7521 0.7994 0.8949 0.1033  -0.0252 -0.0589 286  TRP F NE1 
17569 C  CE2 . TRP F 286  ? 0.7168 0.7716 0.8566 0.1069  -0.0255 -0.0582 286  TRP F CE2 
17570 C  CE3 . TRP F 286  ? 0.6947 0.7523 0.8244 0.1149  -0.0248 -0.0576 286  TRP F CE3 
17571 C  CZ2 . TRP F 286  ? 0.7395 0.8046 0.8819 0.1069  -0.0260 -0.0578 286  TRP F CZ2 
17572 C  CZ3 . TRP F 286  ? 0.7064 0.7742 0.8392 0.1142  -0.0251 -0.0573 286  TRP F CZ3 
17573 C  CH2 . TRP F 286  ? 0.7581 0.8290 0.8967 0.1104  -0.0257 -0.0573 286  TRP F CH2 
17574 N  N   . SER F 287  ? 0.7953 0.8362 0.9146 0.1193  -0.0198 -0.0529 287  SER F N   
17575 C  CA  . SER F 287  ? 0.7370 0.7882 0.8582 0.1196  -0.0189 -0.0512 287  SER F CA  
17576 C  C   . SER F 287  ? 0.7394 0.7871 0.8593 0.1192  -0.0163 -0.0482 287  SER F C   
17577 O  O   . SER F 287  ? 0.9038 0.9571 1.0277 0.1165  -0.0147 -0.0462 287  SER F O   
17578 C  CB  . SER F 287  ? 0.7965 0.8545 0.9138 0.1248  -0.0206 -0.0529 287  SER F CB  
17579 O  OG  . SER F 287  ? 0.7268 0.7867 0.8441 0.1257  -0.0229 -0.0557 287  SER F OG  
17580 N  N   . GLY F 288  ? 0.8829 0.9210 0.9967 0.1221  -0.0156 -0.0477 288  GLY F N   
17581 C  CA  . GLY F 288  ? 0.8785 0.9115 0.9902 0.1219  -0.0129 -0.0448 288  GLY F CA  
17582 C  C   . GLY F 288  ? 0.8177 0.8419 0.9324 0.1170  -0.0105 -0.0433 288  GLY F C   
17583 O  O   . GLY F 288  ? 0.8391 0.8518 0.9498 0.1175  -0.0097 -0.0435 288  GLY F O   
17584 N  N   . ASP F 289  ? 0.7700 0.7993 0.8916 0.1123  -0.0091 -0.0418 289  ASP F N   
17585 C  CA  . ASP F 289  ? 0.7740 0.7976 0.9006 0.1071  -0.0071 -0.0408 289  ASP F CA  
17586 C  C   . ASP F 289  ? 0.7493 0.7635 0.8725 0.1067  -0.0034 -0.0378 289  ASP F C   
17587 O  O   . ASP F 289  ? 0.7798 0.7949 0.9070 0.1034  -0.0008 -0.0354 289  ASP F O   
17588 C  CB  . ASP F 289  ? 0.8097 0.8430 0.9447 0.1030  -0.0071 -0.0404 289  ASP F CB  
17589 C  CG  . ASP F 289  ? 0.7923 0.8223 0.9339 0.0979  -0.0062 -0.0407 289  ASP F CG  
17590 O  OD1 . ASP F 289  ? 0.7764 0.8046 0.9192 0.0972  -0.0084 -0.0435 289  ASP F OD1 
17591 O  OD2 . ASP F 289  ? 0.8532 0.8830 0.9990 0.0946  -0.0034 -0.0383 289  ASP F OD2 
17592 N  N   . VAL F 290  ? 0.8662 0.8706 0.9813 0.1106  -0.0030 -0.0379 290  VAL F N   
17593 C  CA  . VAL F 290  ? 0.8997 0.8932 1.0098 0.1110  0.0006  -0.0351 290  VAL F CA  
17594 C  C   . VAL F 290  ? 0.9071 0.8909 1.0202 0.1061  0.0031  -0.0349 290  VAL F C   
17595 O  O   . VAL F 290  ? 0.9395 0.9196 1.0533 0.1053  0.0015  -0.0375 290  VAL F O   
17596 C  CB  . VAL F 290  ? 0.8467 0.8332 0.9459 0.1176  0.0000  -0.0352 290  VAL F CB  
17597 C  CG1 . VAL F 290  ? 0.9096 0.8843 1.0025 0.1185  0.0038  -0.0320 290  VAL F CG1 
17598 C  CG2 . VAL F 290  ? 0.8690 0.8668 0.9665 0.1221  -0.0027 -0.0359 290  VAL F CG2 
17599 N  N   . ALA F 291  ? 0.5558 0.5356 0.6711 0.1029  0.0071  -0.0320 291  ALA F N   
17600 C  CA  . ALA F 291  ? 0.6354 0.6085 0.7560 0.0972  0.0098  -0.0319 291  ALA F CA  
17601 C  C   . ALA F 291  ? 0.7404 0.6978 0.8537 0.0982  0.0116  -0.0322 291  ALA F C   
17602 O  O   . ALA F 291  ? 0.7307 0.6823 0.8484 0.0934  0.0133  -0.0331 291  ALA F O   
17603 C  CB  . ALA F 291  ? 0.5999 0.5736 0.7250 0.0936  0.0140  -0.0286 291  ALA F CB  
17604 N  N   . GLU F 292  ? 1.3888 1.3393 1.4911 0.1044  0.0114  -0.0316 292  GLU F N   
17605 C  CA  . GLU F 292  ? 1.4272 1.3616 1.5211 0.1060  0.0133  -0.0317 292  GLU F CA  
17606 C  C   . GLU F 292  ? 1.4448 1.3774 1.5377 0.1068  0.0098  -0.0356 292  GLU F C   
17607 O  O   . GLU F 292  ? 1.4702 1.3889 1.5573 0.1070  0.0114  -0.0362 292  GLU F O   
17608 C  CB  . GLU F 292  ? 1.5008 1.4277 1.5822 0.1130  0.0143  -0.0295 292  GLU F CB  
17609 C  CG  . GLU F 292  ? 1.7228 1.6435 1.8018 0.1120  0.0192  -0.0254 292  GLU F CG  
17610 C  CD  . GLU F 292  ? 1.8287 1.7603 1.9079 0.1146  0.0182  -0.0238 292  GLU F CD  
17611 O  OE1 . GLU F 292  ? 1.7828 1.7285 1.8675 0.1150  0.0143  -0.0257 292  GLU F OE1 
17612 O  OE2 . GLU F 292  ? 1.7859 1.7114 1.8594 0.1163  0.0214  -0.0206 292  GLU F OE2 
17613 N  N   . PHE F 293  ? 1.0096 0.9552 1.1075 0.1075  0.0053  -0.0383 293  PHE F N   
17614 C  CA  . PHE F 293  ? 0.8836 0.8282 0.9803 0.1087  0.0018  -0.0421 293  PHE F CA  
17615 C  C   . PHE F 293  ? 0.9311 0.8848 1.0388 0.1032  -0.0005 -0.0448 293  PHE F C   
17616 O  O   . PHE F 293  ? 1.1836 1.1360 1.2906 0.1035  -0.0035 -0.0482 293  PHE F O   
17617 C  CB  . PHE F 293  ? 0.9576 0.9083 1.0480 0.1161  -0.0018 -0.0433 293  PHE F CB  
17618 C  CG  . PHE F 293  ? 0.9981 0.9422 1.0780 0.1224  -0.0003 -0.0409 293  PHE F CG  
17619 C  CD1 . PHE F 293  ? 1.0936 1.0218 1.1633 0.1256  0.0013  -0.0407 293  PHE F CD1 
17620 C  CD2 . PHE F 293  ? 0.9840 0.9376 1.0637 0.1252  -0.0007 -0.0391 293  PHE F CD2 
17621 C  CE1 . PHE F 293  ? 1.0333 0.9554 1.0927 0.1321  0.0024  -0.0386 293  PHE F CE1 
17622 C  CE2 . PHE F 293  ? 0.9979 0.9461 1.0679 0.1313  0.0002  -0.0372 293  PHE F CE2 
17623 C  CZ  . PHE F 293  ? 0.9763 0.9089 1.0361 0.1350  0.0017  -0.0369 293  PHE F CZ  
17624 N  N   . THR F 294  ? 0.8126 0.7749 0.9297 0.0984  0.0006  -0.0434 294  THR F N   
17625 C  CA  . THR F 294  ? 0.8389 0.8108 0.9664 0.0936  -0.0017 -0.0458 294  THR F CA  
17626 C  C   . THR F 294  ? 0.8839 0.8485 1.0166 0.0876  -0.0004 -0.0476 294  THR F C   
17627 O  O   . THR F 294  ? 0.7287 0.6983 0.8669 0.0852  -0.0037 -0.0510 294  THR F O   
17628 C  CB  . THR F 294  ? 0.8337 0.8177 0.9688 0.0914  -0.0010 -0.0436 294  THR F CB  
17629 O  OG1 . THR F 294  ? 0.8179 0.7964 0.9524 0.0899  0.0038  -0.0399 294  THR F OG1 
17630 C  CG2 . THR F 294  ? 0.8119 0.8063 0.9444 0.0962  -0.0035 -0.0434 294  THR F CG2 
17631 N  N   . PRO F 295  ? 1.3658 1.3191 1.4974 0.0847  0.0042  -0.0455 295  PRO F N   
17632 C  CA  . PRO F 295  ? 1.3328 1.2804 1.4707 0.0781  0.0055  -0.0476 295  PRO F CA  
17633 C  C   . PRO F 295  ? 1.3533 1.2942 1.4876 0.0785  0.0024  -0.0519 295  PRO F C   
17634 O  O   . PRO F 295  ? 1.3251 1.2663 1.4668 0.0730  0.0015  -0.0549 295  PRO F O   
17635 C  CB  . PRO F 295  ? 1.2026 1.1372 1.3369 0.0763  0.0117  -0.0443 295  PRO F CB  
17636 C  CG  . PRO F 295  ? 1.3259 1.2652 1.4574 0.0798  0.0134  -0.0402 295  PRO F CG  
17637 C  CD  . PRO F 295  ? 1.2914 1.2379 1.4173 0.0864  0.0088  -0.0413 295  PRO F CD  
17638 N  N   . TRP F 296  ? 0.9913 0.9263 1.1145 0.0850  0.0008  -0.0524 296  TRP F N   
17639 C  CA  . TRP F 296  ? 0.9441 0.8723 1.0630 0.0859  -0.0022 -0.0565 296  TRP F CA  
17640 C  C   . TRP F 296  ? 0.9211 0.8622 1.0475 0.0846  -0.0074 -0.0602 296  TRP F C   
17641 O  O   . TRP F 296  ? 0.9877 0.9269 1.1188 0.0801  -0.0089 -0.0638 296  TRP F O   
17642 C  CB  . TRP F 296  ? 0.9925 0.9135 1.0980 0.0941  -0.0030 -0.0561 296  TRP F CB  
17643 C  CG  . TRP F 296  ? 1.0837 0.9922 1.1823 0.0951  -0.0044 -0.0595 296  TRP F CG  
17644 C  CD1 . TRP F 296  ? 1.1164 1.0074 1.2092 0.0932  -0.0009 -0.0595 296  TRP F CD1 
17645 C  CD2 . TRP F 296  ? 0.9736 0.8855 1.0698 0.0983  -0.0093 -0.0635 296  TRP F CD2 
17646 N  NE1 . TRP F 296  ? 1.0968 0.9798 1.1836 0.0950  -0.0035 -0.0634 296  TRP F NE1 
17647 C  CE2 . TRP F 296  ? 0.9404 0.8362 1.0292 0.0982  -0.0087 -0.0659 296  TRP F CE2 
17648 C  CE3 . TRP F 296  ? 0.9198 0.8463 1.0189 0.1012  -0.0138 -0.0653 296  TRP F CE3 
17649 C  CZ2 . TRP F 296  ? 0.9856 0.8796 1.0698 0.1012  -0.0128 -0.0700 296  TRP F CZ2 
17650 C  CZ3 . TRP F 296  ? 0.9077 0.8325 1.0023 0.1042  -0.0176 -0.0692 296  TRP F CZ3 
17651 C  CH2 . TRP F 296  ? 0.9490 0.8579 1.0363 0.1043  -0.0172 -0.0716 296  TRP F CH2 
17652 N  N   . TYR F 297  ? 0.8036 0.7579 0.9309 0.0885  -0.0100 -0.0595 297  TYR F N   
17653 C  CA  . TYR F 297  ? 0.7760 0.7424 0.9093 0.0878  -0.0147 -0.0627 297  TYR F CA  
17654 C  C   . TYR F 297  ? 0.8237 0.7991 0.9696 0.0814  -0.0146 -0.0629 297  TYR F C   
17655 O  O   . TYR F 297  ? 0.8031 0.7874 0.9543 0.0803  -0.0184 -0.0659 297  TYR F O   
17656 C  CB  . TYR F 297  ? 0.7123 0.6892 0.8422 0.0938  -0.0169 -0.0618 297  TYR F CB  
17657 C  CG  . TYR F 297  ? 0.7369 0.7086 0.8565 0.1002  -0.0191 -0.0636 297  TYR F CG  
17658 C  CD1 . TYR F 297  ? 0.7506 0.7214 0.8688 0.1009  -0.0228 -0.0679 297  TYR F CD1 
17659 C  CD2 . TYR F 297  ? 0.7781 0.7457 0.8890 0.1059  -0.0174 -0.0613 297  TYR F CD2 
17660 C  CE1 . TYR F 297  ? 0.7825 0.7485 0.8911 0.1071  -0.0245 -0.0696 297  TYR F CE1 
17661 C  CE2 . TYR F 297  ? 0.7953 0.7587 0.8969 0.1122  -0.0193 -0.0630 297  TYR F CE2 
17662 C  CZ  . TYR F 297  ? 0.7844 0.7469 0.8849 0.1127  -0.0227 -0.0671 297  TYR F CZ  
17663 O  OH  . TYR F 297  ? 0.8330 0.7913 0.9241 0.1193  -0.0244 -0.0688 297  TYR F OH  
17664 N  N   . VAL F 298  ? 1.1172 1.0907 1.2676 0.0775  -0.0102 -0.0598 298  VAL F N   
17665 C  CA  . VAL F 298  ? 1.0637 1.0455 1.2264 0.0715  -0.0099 -0.0602 298  VAL F CA  
17666 C  C   . VAL F 298  ? 1.1469 1.1229 1.3145 0.0659  -0.0106 -0.0641 298  VAL F C   
17667 O  O   . VAL F 298  ? 1.1586 1.1435 1.3347 0.0628  -0.0140 -0.0672 298  VAL F O   
17668 C  CB  . VAL F 298  ? 1.0353 1.0169 1.2011 0.0694  -0.0047 -0.0556 298  VAL F CB  
17669 C  CG1 . VAL F 298  ? 1.0454 1.0310 1.2234 0.0623  -0.0031 -0.0563 298  VAL F CG1 
17670 C  CG2 . VAL F 298  ? 1.0509 1.0427 1.2156 0.0734  -0.0050 -0.0526 298  VAL F CG2 
17671 N  N   . HIS F 299  ? 1.0456 1.0065 1.2077 0.0646  -0.0076 -0.0642 299  HIS F N   
17672 C  CA  . HIS F 299  ? 1.0164 0.9706 1.1830 0.0586  -0.0079 -0.0680 299  HIS F CA  
17673 C  C   . HIS F 299  ? 0.9236 0.8792 1.0882 0.0602  -0.0137 -0.0732 299  HIS F C   
17674 O  O   . HIS F 299  ? 0.8843 0.8427 1.0567 0.0552  -0.0162 -0.0772 299  HIS F O   
17675 C  CB  . HIS F 299  ? 1.0648 1.0007 1.2241 0.0573  -0.0029 -0.0667 299  HIS F CB  
17676 C  CG  . HIS F 299  ? 1.0884 1.0211 1.2475 0.0567  0.0032  -0.0615 299  HIS F CG  
17677 N  ND1 . HIS F 299  ? 1.0940 1.0385 1.2629 0.0541  0.0047  -0.0591 299  HIS F ND1 
17678 C  CD2 . HIS F 299  ? 1.0047 0.9233 1.1543 0.0586  0.0080  -0.0582 299  HIS F CD2 
17679 C  CE1 . HIS F 299  ? 1.0597 0.9975 1.2251 0.0543  0.0103  -0.0546 299  HIS F CE1 
17680 N  NE2 . HIS F 299  ? 0.9539 0.8760 1.1076 0.0571  0.0124  -0.0539 299  HIS F NE2 
17681 N  N   . ARG F 300  ? 0.8661 0.8201 1.0203 0.0672  -0.0161 -0.0732 300  ARG F N   
17682 C  CA  . ARG F 300  ? 0.8812 0.8357 1.0321 0.0695  -0.0214 -0.0779 300  ARG F CA  
17683 C  C   . ARG F 300  ? 0.9248 0.8958 1.0828 0.0699  -0.0260 -0.0797 300  ARG F C   
17684 O  O   . ARG F 300  ? 1.0007 0.9733 1.1570 0.0713  -0.0307 -0.0839 300  ARG F O   
17685 C  CB  . ARG F 300  ? 0.9256 0.8730 1.0630 0.0773  -0.0220 -0.0773 300  ARG F CB  
17686 C  CG  . ARG F 300  ? 0.9904 0.9190 1.1184 0.0775  -0.0195 -0.0780 300  ARG F CG  
17687 C  CD  . ARG F 300  ? 0.9857 0.9055 1.1124 0.0757  -0.0134 -0.0736 300  ARG F CD  
17688 N  NE  . ARG F 300  ? 1.0567 0.9576 1.1729 0.0768  -0.0106 -0.0738 300  ARG F NE  
17689 C  CZ  . ARG F 300  ? 1.2275 1.1171 1.3401 0.0756  -0.0051 -0.0703 300  ARG F CZ  
17690 N  NH1 . ARG F 300  ? 1.2178 1.1134 1.3367 0.0732  -0.0016 -0.0664 300  ARG F NH1 
17691 N  NH2 . ARG F 300  ? 1.2041 1.0755 1.3060 0.0770  -0.0027 -0.0707 300  ARG F NH2 
17692 N  N   . THR F 301  ? 0.8830 0.8656 1.0481 0.0691  -0.0249 -0.0766 301  THR F N   
17693 C  CA  . THR F 301  ? 0.8616 0.8593 1.0334 0.0694  -0.0288 -0.0779 301  THR F CA  
17694 C  C   . THR F 301  ? 0.9506 0.9556 1.1354 0.0630  -0.0283 -0.0784 301  THR F C   
17695 O  O   . THR F 301  ? 1.1024 1.1203 1.2933 0.0633  -0.0305 -0.0783 301  THR F O   
17696 C  CB  . THR F 301  ? 0.8907 0.8969 1.0593 0.0747  -0.0282 -0.0741 301  THR F CB  
17697 O  OG1 . THR F 301  ? 0.9395 0.9444 1.1096 0.0735  -0.0232 -0.0695 301  THR F OG1 
17698 C  CG2 . THR F 301  ? 0.7933 0.7951 0.9502 0.0813  -0.0295 -0.0744 301  THR F CG2 
17699 N  N   . GLN F 302  ? 1.0995 1.0966 1.2886 0.0572  -0.0252 -0.0790 302  GLN F N   
17700 C  CA  . GLN F 302  ? 1.1087 1.1126 1.3108 0.0509  -0.0239 -0.0791 302  GLN F CA  
17701 C  C   . GLN F 302  ? 1.1589 1.1593 1.3669 0.0450  -0.0261 -0.0845 302  GLN F C   
17702 O  O   . GLN F 302  ? 1.2790 1.2673 1.4802 0.0448  -0.0265 -0.0871 302  GLN F O   
17703 C  CB  . GLN F 302  ? 1.1367 1.1354 1.3402 0.0484  -0.0172 -0.0744 302  GLN F CB  
17704 C  CG  . GLN F 302  ? 1.1731 1.1563 1.3744 0.0442  -0.0133 -0.0750 302  GLN F CG  
17705 C  CD  . GLN F 302  ? 1.2059 1.1843 1.4088 0.0417  -0.0064 -0.0702 302  GLN F CD  
17706 O  OE1 . GLN F 302  ? 1.3334 1.3208 1.5404 0.0426  -0.0047 -0.0667 302  GLN F OE1 
17707 N  NE2 . GLN F 302  ? 1.2330 1.1964 1.4321 0.0387  -0.0022 -0.0700 302  GLN F NE2 
17708 N  N   . HIS F 303  ? 0.9960 1.0074 1.2168 0.0404  -0.0274 -0.0864 303  HIS F N   
17709 C  CA  . HIS F 303  ? 1.1126 1.1232 1.3418 0.0337  -0.0293 -0.0916 303  HIS F CA  
17710 C  C   . HIS F 303  ? 1.0709 1.0765 1.2937 0.0354  -0.0348 -0.0970 303  HIS F C   
17711 O  O   . HIS F 303  ? 1.1257 1.1207 1.3478 0.0312  -0.0346 -0.1006 303  HIS F O   
17712 C  CB  . HIS F 303  ? 1.2054 1.2044 1.4373 0.0275  -0.0231 -0.0905 303  HIS F CB  
17713 C  CG  . HIS F 303  ? 1.2661 1.2701 1.5051 0.0253  -0.0176 -0.0857 303  HIS F CG  
17714 N  ND1 . HIS F 303  ? 1.3022 1.3216 1.5539 0.0229  -0.0187 -0.0859 303  HIS F ND1 
17715 C  CD2 . HIS F 303  ? 1.2884 1.2839 1.5232 0.0254  -0.0110 -0.0806 303  HIS F CD2 
17716 C  CE1 . HIS F 303  ? 1.3493 1.3694 1.6045 0.0216  -0.0129 -0.0811 303  HIS F CE1 
17717 N  NE2 . HIS F 303  ? 1.3002 1.3058 1.5451 0.0230  -0.0082 -0.0778 303  HIS F NE2 
17718 N  N   . GLY F 304  ? 1.4029 1.4156 1.6205 0.0416  -0.0395 -0.0977 304  GLY F N   
17719 C  CA  . GLY F 304  ? 1.4743 1.4841 1.6859 0.0438  -0.0451 -0.1028 304  GLY F CA  
17720 C  C   . GLY F 304  ? 1.4821 1.4782 1.6792 0.0487  -0.0442 -0.1022 304  GLY F C   
17721 O  O   . GLY F 304  ? 1.5072 1.5013 1.6979 0.0519  -0.0488 -0.1060 304  GLY F O   
17722 N  N   . TRP F 305  ? 1.0700 1.0567 1.2615 0.0497  -0.0386 -0.0976 305  TRP F N   
17723 C  CA  . TRP F 305  ? 1.0404 1.0144 1.2179 0.0549  -0.0378 -0.0970 305  TRP F CA  
17724 C  C   . TRP F 305  ? 0.9943 0.9752 1.1643 0.0630  -0.0407 -0.0958 305  TRP F C   
17725 O  O   . TRP F 305  ? 0.9864 0.9591 1.1452 0.0680  -0.0415 -0.0966 305  TRP F O   
17726 C  CB  . TRP F 305  ? 1.0492 1.0125 1.2223 0.0547  -0.0312 -0.0921 305  TRP F CB  
17727 C  CG  . TRP F 305  ? 1.0814 1.0324 1.2574 0.0477  -0.0276 -0.0935 305  TRP F CG  
17728 C  CD1 . TRP F 305  ? 1.1377 1.0902 1.3239 0.0411  -0.0236 -0.0919 305  TRP F CD1 
17729 C  CD2 . TRP F 305  ? 1.1644 1.0993 1.3329 0.0465  -0.0276 -0.0968 305  TRP F CD2 
17730 N  NE1 . TRP F 305  ? 1.1690 1.1075 1.3547 0.0355  -0.0207 -0.0940 305  TRP F NE1 
17731 C  CE2 . TRP F 305  ? 1.2131 1.1402 1.3878 0.0387  -0.0232 -0.0971 305  TRP F CE2 
17732 C  CE3 . TRP F 305  ? 1.1537 1.0797 1.3106 0.0514  -0.0306 -0.0997 305  TRP F CE3 
17733 C  CZ2 . TRP F 305  ? 1.3149 1.2251 1.4843 0.0353  -0.0216 -0.1000 305  TRP F CZ2 
17734 C  CZ3 . TRP F 305  ? 1.2075 1.1166 1.3588 0.0484  -0.0293 -0.1026 305  TRP F CZ3 
17735 C  CH2 . TRP F 305  ? 1.3019 1.2030 1.4594 0.0403  -0.0248 -0.1027 305  TRP F CH2 
17736 N  N   . VAL F 306  ? 1.0469 1.0425 1.2227 0.0644  -0.0421 -0.0941 306  VAL F N   
17737 C  CA  . VAL F 306  ? 1.1115 1.1142 1.2808 0.0714  -0.0446 -0.0931 306  VAL F CA  
17738 C  C   . VAL F 306  ? 1.1062 1.1088 1.2712 0.0738  -0.0502 -0.0984 306  VAL F C   
17739 O  O   . VAL F 306  ? 1.0675 1.0684 1.2228 0.0799  -0.0516 -0.0985 306  VAL F O   
17740 C  CB  . VAL F 306  ? 1.1828 1.2002 1.3592 0.0718  -0.0444 -0.0901 306  VAL F CB  
17741 C  CG1 . VAL F 306  ? 1.2658 1.2912 1.4543 0.0662  -0.0467 -0.0928 306  VAL F CG1 
17742 C  CG2 . VAL F 306  ? 1.0629 1.0880 1.2334 0.0783  -0.0472 -0.0898 306  VAL F CG2 
17743 N  N   . PHE F 307  ? 0.8814 0.8859 1.0535 0.0690  -0.0535 -0.1030 307  PHE F N   
17744 C  CA  . PHE F 307  ? 0.7916 0.7956 0.9594 0.0710  -0.0592 -0.1084 307  PHE F CA  
17745 C  C   . PHE F 307  ? 0.7762 0.7651 0.9325 0.0735  -0.0589 -0.1103 307  PHE F C   
17746 O  O   . PHE F 307  ? 0.7728 0.7605 0.9209 0.0786  -0.0623 -0.1128 307  PHE F O   
17747 C  CB  . PHE F 307  ? 0.8107 0.8189 0.9888 0.0647  -0.0627 -0.1133 307  PHE F CB  
17748 C  CG  . PHE F 307  ? 0.9469 0.9697 1.1366 0.0624  -0.0630 -0.1117 307  PHE F CG  
17749 C  CD1 . PHE F 307  ? 0.9875 1.0217 1.1760 0.0675  -0.0646 -0.1095 307  PHE F CD1 
17750 C  CD2 . PHE F 307  ? 1.0321 1.0571 1.2338 0.0551  -0.0615 -0.1124 307  PHE F CD2 
17751 C  CE1 . PHE F 307  ? 1.0340 1.0809 1.2324 0.0657  -0.0648 -0.1079 307  PHE F CE1 
17752 C  CE2 . PHE F 307  ? 1.1011 1.1398 1.3134 0.0534  -0.0617 -0.1110 307  PHE F CE2 
17753 C  CZ  . PHE F 307  ? 1.1363 1.1857 1.3466 0.0589  -0.0635 -0.1087 307  PHE F CZ  
17754 N  N   . VAL F 308  ? 0.8039 0.7806 0.9590 0.0703  -0.0546 -0.1090 308  VAL F N   
17755 C  CA  . VAL F 308  ? 0.7434 0.7046 0.8866 0.0733  -0.0536 -0.1101 308  VAL F CA  
17756 C  C   . VAL F 308  ? 0.8128 0.7750 0.9459 0.0818  -0.0526 -0.1066 308  VAL F C   
17757 O  O   . VAL F 308  ? 0.8305 0.7869 0.9536 0.0870  -0.0547 -0.1088 308  VAL F O   
17758 C  CB  . VAL F 308  ? 0.7896 0.7374 0.9334 0.0682  -0.0485 -0.1087 308  VAL F CB  
17759 C  CG1 . VAL F 308  ? 0.8213 0.7522 0.9514 0.0722  -0.0472 -0.1093 308  VAL F CG1 
17760 C  CG2 . VAL F 308  ? 0.8854 0.8325 1.0397 0.0594  -0.0495 -0.1127 308  VAL F CG2 
17761 N  N   . ALA F 309  ? 0.9938 0.9635 1.1295 0.0833  -0.0494 -0.1014 309  ALA F N   
17762 C  CA  . ALA F 309  ? 0.9947 0.9666 1.1220 0.0908  -0.0484 -0.0982 309  ALA F CA  
17763 C  C   . ALA F 309  ? 1.0159 0.9975 1.1406 0.0956  -0.0527 -0.1002 309  ALA F C   
17764 O  O   . ALA F 309  ? 1.0672 1.0464 1.1825 0.1020  -0.0533 -0.1004 309  ALA F O   
17765 C  CB  . ALA F 309  ? 0.9463 0.9248 1.0779 0.0907  -0.0443 -0.0925 309  ALA F CB  
17766 N  N   . LEU F 310  ? 0.9295 0.9222 1.0624 0.0929  -0.0557 -0.1018 310  LEU F N   
17767 C  CA  . LEU F 310  ? 0.9405 0.9419 1.0704 0.0975  -0.0596 -0.1037 310  LEU F CA  
17768 C  C   . LEU F 310  ? 0.9640 0.9573 1.0861 0.0998  -0.0633 -0.1089 310  LEU F C   
17769 O  O   . LEU F 310  ? 1.0729 1.0681 1.1872 0.1060  -0.0650 -0.1096 310  LEU F O   
17770 C  CB  . LEU F 310  ? 1.0082 1.0221 1.1480 0.0942  -0.0620 -0.1043 310  LEU F CB  
17771 C  CG  . LEU F 310  ? 0.9968 1.0196 1.1439 0.0925  -0.0585 -0.0992 310  LEU F CG  
17772 C  CD1 . LEU F 310  ? 0.9357 0.9693 1.0927 0.0890  -0.0611 -0.1004 310  LEU F CD1 
17773 C  CD2 . LEU F 310  ? 0.8791 0.9074 1.0204 0.0984  -0.0566 -0.0954 310  LEU F CD2 
17774 N  N   . ALA F 311  ? 0.6951 0.6793 0.8192 0.0948  -0.0645 -0.1126 311  ALA F N   
17775 C  CA  . ALA F 311  ? 0.7202 0.6950 0.8362 0.0968  -0.0680 -0.1178 311  ALA F CA  
17776 C  C   . ALA F 311  ? 0.7880 0.7523 0.8918 0.1028  -0.0657 -0.1165 311  ALA F C   
17777 O  O   . ALA F 311  ? 0.8486 0.8103 0.9434 0.1083  -0.0682 -0.1192 311  ALA F O   
17778 C  CB  . ALA F 311  ? 0.6676 0.6338 0.7885 0.0894  -0.0692 -0.1220 311  ALA F CB  
17779 N  N   . LEU F 312  ? 0.9958 0.9540 1.0987 0.1024  -0.0608 -0.1125 312  LEU F N   
17780 C  CA  . LEU F 312  ? 1.0006 0.9498 1.0921 0.1088  -0.0586 -0.1109 312  LEU F CA  
17781 C  C   . LEU F 312  ? 1.0047 0.9647 1.0921 0.1161  -0.0590 -0.1088 312  LEU F C   
17782 O  O   . LEU F 312  ? 1.0061 0.9616 1.0836 0.1226  -0.0595 -0.1098 312  LEU F O   
17783 C  CB  . LEU F 312  ? 0.9466 0.8882 1.0383 0.1070  -0.0534 -0.1068 312  LEU F CB  
17784 C  CG  . LEU F 312  ? 1.0465 0.9747 1.1403 0.1002  -0.0518 -0.1084 312  LEU F CG  
17785 C  CD1 . LEU F 312  ? 1.0351 0.9577 1.1293 0.0989  -0.0462 -0.1035 312  LEU F CD1 
17786 C  CD2 . LEU F 312  ? 1.0959 1.0087 1.1793 0.1022  -0.0534 -0.1128 312  LEU F CD2 
17787 N  N   . MET F 313  ? 1.2893 1.2634 1.3843 0.1151  -0.0585 -0.1059 313  MET F N   
17788 C  CA  . MET F 313  ? 1.2514 1.2359 1.3433 0.1213  -0.0583 -0.1037 313  MET F CA  
17789 C  C   . MET F 313  ? 1.3030 1.2899 1.3893 0.1255  -0.0623 -0.1076 313  MET F C   
17790 O  O   . MET F 313  ? 1.3103 1.2999 1.3897 0.1320  -0.0619 -0.1070 313  MET F O   
17791 C  CB  . MET F 313  ? 1.1881 1.1861 1.2893 0.1186  -0.0570 -0.1001 313  MET F CB  
17792 C  CG  . MET F 313  ? 1.3928 1.3905 1.4970 0.1171  -0.0525 -0.0953 313  MET F CG  
17793 S  SD  . MET F 313  ? 1.7199 1.7321 1.8350 0.1134  -0.0511 -0.0916 313  MET F SD  
17794 C  CE  . MET F 313  ? 1.2557 1.2799 1.3677 0.1187  -0.0534 -0.0922 313  MET F CE  
17795 N  N   . LEU F 314  ? 1.2410 1.2274 1.3303 0.1219  -0.0661 -0.1117 314  LEU F N   
17796 C  CA  . LEU F 314  ? 1.2857 1.2747 1.3699 0.1256  -0.0702 -0.1156 314  LEU F CA  
17797 C  C   . LEU F 314  ? 1.2657 1.2411 1.3411 0.1273  -0.0725 -0.1204 314  LEU F C   
17798 O  O   . LEU F 314  ? 1.2103 1.1837 1.2763 0.1338  -0.0733 -0.1217 314  LEU F O   
17799 C  CB  . LEU F 314  ? 1.3250 1.3229 1.4172 0.1215  -0.0736 -0.1175 314  LEU F CB  
17800 C  CG  . LEU F 314  ? 1.2508 1.2515 1.3379 0.1250  -0.0783 -0.1217 314  LEU F CG  
17801 C  CD1 . LEU F 314  ? 1.2419 1.2514 1.3239 0.1316  -0.0771 -0.1191 314  LEU F CD1 
17802 C  CD2 . LEU F 314  ? 1.1170 1.1240 1.2123 0.1201  -0.0822 -0.1244 314  LEU F CD2 
17803 N  N   . PHE F 315  ? 1.2286 1.1943 1.3069 0.1214  -0.0733 -0.1230 315  PHE F N   
17804 C  CA  . PHE F 315  ? 1.1336 1.0854 1.2036 0.1223  -0.0756 -0.1279 315  PHE F CA  
17805 C  C   . PHE F 315  ? 1.1247 1.0646 1.1846 0.1272  -0.0723 -0.1264 315  PHE F C   
17806 O  O   . PHE F 315  ? 1.1869 1.1169 1.2367 0.1313  -0.0739 -0.1298 315  PHE F O   
17807 C  CB  . PHE F 315  ? 1.0610 1.0060 1.1376 0.1139  -0.0772 -0.1314 315  PHE F CB  
17808 C  CG  . PHE F 315  ? 1.1723 1.1278 1.2576 0.1099  -0.0815 -0.1344 315  PHE F CG  
17809 C  CD1 . PHE F 315  ? 1.0829 1.0464 1.1646 0.1146  -0.0854 -0.1365 315  PHE F CD1 
17810 C  CD2 . PHE F 315  ? 1.2204 1.1779 1.3173 0.1016  -0.0817 -0.1351 315  PHE F CD2 
17811 C  CE1 . PHE F 315  ? 1.0455 1.0186 1.1345 0.1115  -0.0897 -0.1392 315  PHE F CE1 
17812 C  CE2 . PHE F 315  ? 1.2080 1.1759 1.3130 0.0983  -0.0860 -0.1380 315  PHE F CE2 
17813 C  CZ  . PHE F 315  ? 1.1361 1.1116 1.2368 0.1034  -0.0902 -0.1400 315  PHE F CZ  
17814 N  N   . ALA F 316  ? 1.0220 0.9624 1.0840 0.1272  -0.0677 -0.1213 316  ALA F N   
17815 C  CA  . ALA F 316  ? 0.9750 0.9041 1.0275 0.1321  -0.0646 -0.1197 316  ALA F CA  
17816 C  C   . ALA F 316  ? 0.9622 0.8997 1.0101 0.1400  -0.0628 -0.1163 316  ALA F C   
17817 O  O   . ALA F 316  ? 0.9426 0.8720 0.9819 0.1454  -0.0608 -0.1153 316  ALA F O   
17818 C  CB  . ALA F 316  ? 0.9147 0.8359 0.9709 0.1271  -0.0606 -0.1167 316  ALA F CB  
17819 N  N   . PHE F 317  ? 1.0247 0.9780 1.0780 0.1409  -0.0635 -0.1146 317  PHE F N   
17820 C  CA  . PHE F 317  ? 1.0035 0.9656 1.0530 0.1480  -0.0618 -0.1119 317  PHE F CA  
17821 C  C   . PHE F 317  ? 1.0730 1.0434 1.1198 0.1519  -0.0647 -0.1143 317  PHE F C   
17822 O  O   . PHE F 317  ? 1.1664 1.1329 1.2038 0.1584  -0.0653 -0.1163 317  PHE F O   
17823 C  CB  . PHE F 317  ? 0.9157 0.8889 0.9735 0.1460  -0.0587 -0.1068 317  PHE F CB  
17824 C  CG  . PHE F 317  ? 0.9681 0.9530 1.0240 0.1521  -0.0573 -0.1044 317  PHE F CG  
17825 C  CD1 . PHE F 317  ? 1.0566 1.0382 1.1039 0.1593  -0.0561 -0.1043 317  PHE F CD1 
17826 C  CD2 . PHE F 317  ? 0.9542 0.9533 1.0168 0.1505  -0.0572 -0.1026 317  PHE F CD2 
17827 C  CE1 . PHE F 317  ? 1.0378 1.0310 1.0842 0.1645  -0.0548 -0.1025 317  PHE F CE1 
17828 C  CE2 . PHE F 317  ? 0.9886 0.9982 1.0497 0.1555  -0.0556 -0.1006 317  PHE F CE2 
17829 C  CZ  . PHE F 317  ? 0.9768 0.9839 1.0302 0.1623  -0.0544 -0.1007 317  PHE F CZ  
17830 N  N   . ALA F 318  ? 1.0787 1.0603 1.1329 0.1486  -0.0663 -0.1142 318  ALA F N   
17831 C  CA  . ALA F 318  ? 1.0407 1.0311 1.0919 0.1528  -0.0681 -0.1155 318  ALA F CA  
17832 C  C   . ALA F 318  ? 1.1058 1.0875 1.1485 0.1556  -0.0719 -0.1209 318  ALA F C   
17833 O  O   . ALA F 318  ? 1.1584 1.1410 1.1929 0.1623  -0.0721 -0.1220 318  ALA F O   
17834 C  CB  . ALA F 318  ? 1.0867 1.0889 1.1469 0.1485  -0.0692 -0.1143 318  ALA F CB  
17835 N  N   . LEU F 319  ? 1.1634 1.1369 1.2080 0.1503  -0.0748 -0.1244 319  LEU F N   
17836 C  CA  . LEU F 319  ? 1.1190 1.0836 1.1555 0.1524  -0.0787 -0.1300 319  LEU F CA  
17837 C  C   . LEU F 319  ? 1.1395 1.0922 1.1646 0.1584  -0.0775 -0.1311 319  LEU F C   
17838 O  O   . LEU F 319  ? 1.1866 1.1379 1.2028 0.1644  -0.0792 -0.1338 319  LEU F O   
17839 C  CB  . LEU F 319  ? 1.1324 1.0908 1.1744 0.1447  -0.0820 -0.1337 319  LEU F CB  
17840 C  CG  . LEU F 319  ? 1.2836 1.2339 1.3187 0.1456  -0.0869 -0.1401 319  LEU F CG  
17841 C  CD1 . LEU F 319  ? 1.1561 1.1172 1.1900 0.1489  -0.0901 -0.1416 319  LEU F CD1 
17842 C  CD2 . LEU F 319  ? 1.3315 1.2745 1.3728 0.1372  -0.0893 -0.1437 319  LEU F CD2 
17843 N  N   . PRO F 320  ? 0.9059 0.8495 0.9299 0.1577  -0.0745 -0.1292 320  PRO F N   
17844 C  CA  . PRO F 320  ? 0.8879 0.8207 0.9000 0.1647  -0.0732 -0.1301 320  PRO F CA  
17845 C  C   . PRO F 320  ? 0.9125 0.8552 0.9206 0.1728  -0.0710 -0.1273 320  PRO F C   
17846 O  O   . PRO F 320  ? 0.9713 0.9090 0.9691 0.1799  -0.0714 -0.1294 320  PRO F O   
17847 C  CB  . PRO F 320  ? 0.7765 0.6986 0.7895 0.1616  -0.0702 -0.1279 320  PRO F CB  
17848 C  CG  . PRO F 320  ? 0.7433 0.6658 0.7668 0.1520  -0.0712 -0.1283 320  PRO F CG  
17849 C  CD  . PRO F 320  ? 0.8584 0.7985 0.8904 0.1506  -0.0724 -0.1269 320  PRO F CD  
17850 N  N   . PHE F 321  ? 0.9977 0.9542 1.0139 0.1718  -0.0686 -0.1229 321  PHE F N   
17851 C  CA  . PHE F 321  ? 1.0075 0.9743 1.0211 0.1787  -0.0662 -0.1203 321  PHE F CA  
17852 C  C   . PHE F 321  ? 1.0992 1.0721 1.1081 0.1833  -0.0681 -0.1228 321  PHE F C   
17853 O  O   . PHE F 321  ? 1.1249 1.0991 1.1264 0.1908  -0.0669 -0.1231 321  PHE F O   
17854 C  CB  . PHE F 321  ? 0.9167 0.8966 0.9405 0.1755  -0.0634 -0.1154 321  PHE F CB  
17855 C  CG  . PHE F 321  ? 0.9213 0.9147 0.9448 0.1810  -0.0611 -0.1131 321  PHE F CG  
17856 C  CD1 . PHE F 321  ? 0.8708 0.8656 0.8913 0.1864  -0.0583 -0.1110 321  PHE F CD1 
17857 C  CD2 . PHE F 321  ? 1.0481 1.0530 1.0748 0.1805  -0.0618 -0.1130 321  PHE F CD2 
17858 C  CE1 . PHE F 321  ? 0.9041 0.9122 0.9254 0.1909  -0.0561 -0.1091 321  PHE F CE1 
17859 C  CE2 . PHE F 321  ? 0.9978 1.0148 1.0245 0.1849  -0.0592 -0.1109 321  PHE F CE2 
17860 C  CZ  . PHE F 321  ? 0.9241 0.9431 0.9486 0.1898  -0.0564 -0.1091 321  PHE F CZ  
17861 N  N   . PHE F 322  ? 1.4082 1.3849 1.4209 0.1792  -0.0710 -0.1247 322  PHE F N   
17862 C  CA  . PHE F 322  ? 1.4395 1.4217 1.4471 0.1835  -0.0728 -0.1269 322  PHE F CA  
17863 C  C   . PHE F 322  ? 1.4989 1.4685 1.4953 0.1876  -0.0757 -0.1320 322  PHE F C   
17864 O  O   . PHE F 322  ? 1.4572 1.4288 1.4457 0.1944  -0.0756 -0.1333 322  PHE F O   
17865 C  CB  . PHE F 322  ? 1.4036 1.3940 1.4183 0.1783  -0.0751 -0.1271 322  PHE F CB  
17866 C  CG  . PHE F 322  ? 1.5193 1.5240 1.5422 0.1768  -0.0720 -0.1223 322  PHE F CG  
17867 C  CD1 . PHE F 322  ? 1.4927 1.5068 1.5130 0.1823  -0.0690 -0.1201 322  PHE F CD1 
17868 C  CD2 . PHE F 322  ? 1.5384 1.5473 1.5717 0.1697  -0.0718 -0.1201 322  PHE F CD2 
17869 C  CE1 . PHE F 322  ? 1.4945 1.5210 1.5219 0.1805  -0.0660 -0.1159 322  PHE F CE1 
17870 C  CE2 . PHE F 322  ? 1.5844 1.6055 1.6245 0.1683  -0.0689 -0.1157 322  PHE F CE2 
17871 C  CZ  . PHE F 322  ? 1.6027 1.6324 1.6398 0.1736  -0.0661 -0.1137 322  PHE F CZ  
17872 N  N   . VAL F 323  ? 1.2247 1.1812 1.2201 0.1834  -0.0782 -0.1351 323  VAL F N   
17873 C  CA  . VAL F 323  ? 1.1357 1.0790 1.1201 0.1868  -0.0811 -0.1403 323  VAL F CA  
17874 C  C   . VAL F 323  ? 1.1625 1.0990 1.1370 0.1947  -0.0785 -0.1399 323  VAL F C   
17875 O  O   . VAL F 323  ? 1.2531 1.1870 1.2177 0.2015  -0.0793 -0.1425 323  VAL F O   
17876 C  CB  . VAL F 323  ? 1.0904 1.0212 1.0770 0.1795  -0.0840 -0.1437 323  VAL F CB  
17877 C  CG1 . VAL F 323  ? 1.2103 1.1255 1.1847 0.1830  -0.0865 -0.1490 323  VAL F CG1 
17878 C  CG2 . VAL F 323  ? 1.0282 0.9665 1.0236 0.1729  -0.0874 -0.1452 323  VAL F CG2 
17879 N  N   . LEU F 324  ? 0.8650 0.7986 0.8416 0.1943  -0.0752 -0.1366 324  LEU F N   
17880 C  CA  . LEU F 324  ? 0.9047 0.8320 0.8721 0.2022  -0.0727 -0.1359 324  LEU F CA  
17881 C  C   . LEU F 324  ? 0.9290 0.8710 0.8966 0.2090  -0.0698 -0.1329 324  LEU F C   
17882 O  O   . LEU F 324  ? 0.9113 0.8505 0.8718 0.2163  -0.0677 -0.1323 324  LEU F O   
17883 C  CB  . LEU F 324  ? 0.9022 0.8205 0.8713 0.1997  -0.0703 -0.1335 324  LEU F CB  
17884 C  CG  . LEU F 324  ? 0.9668 0.8661 0.9313 0.1954  -0.0723 -0.1371 324  LEU F CG  
17885 C  CD1 . LEU F 324  ? 0.8780 0.7686 0.8442 0.1926  -0.0693 -0.1342 324  LEU F CD1 
17886 C  CD2 . LEU F 324  ? 0.9628 0.8495 0.9134 0.2021  -0.0740 -0.1416 324  LEU F CD2 
17887 N  N   . LEU F 325  ? 1.1185 1.0758 1.0938 0.2067  -0.0695 -0.1309 325  LEU F N   
17888 C  CA  . LEU F 325  ? 1.1092 1.0806 1.0850 0.2125  -0.0665 -0.1284 325  LEU F CA  
17889 C  C   . LEU F 325  ? 1.1695 1.1390 1.1343 0.2205  -0.0672 -0.1315 325  LEU F C   
17890 O  O   . LEU F 325  ? 1.2716 1.2478 1.2334 0.2275  -0.0643 -0.1302 325  LEU F O   
17891 C  CB  . LEU F 325  ? 0.9824 0.9687 0.9681 0.2077  -0.0659 -0.1258 325  LEU F CB  
17892 C  CG  . LEU F 325  ? 1.0158 1.0178 1.0070 0.2100  -0.0619 -0.1216 325  LEU F CG  
17893 C  CD1 . LEU F 325  ? 0.9778 0.9789 0.9718 0.2104  -0.0593 -0.1187 325  LEU F CD1 
17894 C  CD2 . LEU F 325  ? 1.1963 1.2098 1.1968 0.2040  -0.0615 -0.1193 325  LEU F CD2 
17895 N  N   . PHE F 326  ? 1.2056 1.1664 1.1645 0.2198  -0.0709 -0.1359 326  PHE F N   
17896 C  CA  . PHE F 326  ? 1.2278 1.1865 1.1760 0.2272  -0.0718 -0.1391 326  PHE F CA  
17897 C  C   . PHE F 326  ? 1.2421 1.1878 1.1794 0.2340  -0.0713 -0.1411 326  PHE F C   
17898 O  O   . PHE F 326  ? 1.2171 1.1513 1.1537 0.2318  -0.0716 -0.1412 326  PHE F O   
17899 C  CB  . PHE F 326  ? 1.1869 1.1404 1.1321 0.2241  -0.0764 -0.1433 326  PHE F CB  
17900 C  CG  . PHE F 326  ? 1.1794 1.1451 1.1338 0.2186  -0.0771 -0.1416 326  PHE F CG  
17901 C  CD1 . PHE F 326  ? 1.1237 1.1023 1.0781 0.2222  -0.0751 -0.1399 326  PHE F CD1 
17902 C  CD2 . PHE F 326  ? 1.1306 1.0949 1.0936 0.2099  -0.0795 -0.1417 326  PHE F CD2 
17903 C  CE1 . PHE F 326  ? 1.0458 1.0347 1.0076 0.2175  -0.0755 -0.1382 326  PHE F CE1 
17904 C  CE2 . PHE F 326  ? 1.1539 1.1293 1.1249 0.2054  -0.0802 -0.1401 326  PHE F CE2 
17905 C  CZ  . PHE F 326  ? 1.1022 1.0894 1.0722 0.2094  -0.0782 -0.1383 326  PHE F CZ  
17906 N  N   . ARG F 327  ? 1.2503 1.1975 1.1786 0.2425  -0.0704 -0.1426 327  ARG F N   
17907 C  CA  . ARG F 327  ? 1.3643 1.2986 1.2808 0.2499  -0.0701 -0.1449 327  ARG F CA  
17908 C  C   . ARG F 327  ? 1.3194 1.2349 1.2282 0.2474  -0.0743 -0.1498 327  ARG F C   
17909 O  O   . ARG F 327  ? 1.3294 1.2303 1.2316 0.2492  -0.0743 -0.1511 327  ARG F O   
17910 C  CB  . ARG F 327  ? 1.2941 1.2352 1.2031 0.2596  -0.0681 -0.1456 327  ARG F CB  
17911 C  CG  . ARG F 327  ? 1.2651 1.1963 1.1632 0.2685  -0.0668 -0.1469 327  ARG F CG  
17912 C  CD  . ARG F 327  ? 1.4240 1.3660 1.3177 0.2779  -0.0638 -0.1465 327  ARG F CD  
17913 N  NE  . ARG F 327  ? 1.5363 1.4738 1.4233 0.2864  -0.0616 -0.1463 327  ARG F NE  
17914 C  CZ  . ARG F 327  ? 1.6834 1.6073 1.5567 0.2938  -0.0625 -0.1498 327  ARG F CZ  
17915 N  NH1 . ARG F 327  ? 1.7169 1.6298 1.5816 0.2935  -0.0657 -0.1541 327  ARG F NH1 
17916 N  NH2 . ARG F 327  ? 1.7181 1.6392 1.5860 0.3019  -0.0603 -0.1492 327  ARG F NH2 
17917 N  N   . GLY F 328  ? 1.3931 1.3082 1.3021 0.2433  -0.0779 -0.1528 328  GLY F N   
17918 C  CA  . GLY F 328  ? 1.2848 1.1838 1.1894 0.2386  -0.0822 -0.1575 328  GLY F CA  
17919 C  C   . GLY F 328  ? 1.3822 1.2780 1.2970 0.2290  -0.0828 -0.1560 328  GLY F C   
17920 O  O   . GLY F 328  ? 1.3840 1.2906 1.3093 0.2257  -0.0801 -0.1513 328  GLY F O   
17921 N  N   . THR F 329  ? 1.5002 1.3804 1.4115 0.2243  -0.0862 -0.1603 329  THR F N   
17922 C  CA  . THR F 329  ? 1.4313 1.3055 1.3510 0.2150  -0.0867 -0.1597 329  THR F CA  
17923 C  C   . THR F 329  ? 1.4801 1.3463 1.3982 0.2166  -0.0828 -0.1566 329  THR F C   
17924 O  O   . THR F 329  ? 1.4353 1.2919 1.3569 0.2099  -0.0827 -0.1566 329  THR F O   
17925 C  CB  . THR F 329  ? 1.4234 1.3133 1.3578 0.2077  -0.0868 -0.1566 329  THR F CB  
17926 O  OG1 . THR F 329  ? 1.4741 1.3763 1.4147 0.2099  -0.0823 -0.1507 329  THR F OG1 
17927 C  CG2 . THR F 329  ? 1.4527 1.3520 1.3876 0.2078  -0.0902 -0.1590 329  THR F CG2 
17928 N  N   . LYS F 330  ? 1.5036 1.3732 1.4159 0.2256  -0.0796 -0.1541 330  LYS F N   
17929 C  CA  . LYS F 330  ? 1.6024 1.4617 1.5096 0.2292  -0.0765 -0.1521 330  LYS F CA  
17930 C  C   . LYS F 330  ? 1.6487 1.4941 1.5400 0.2384  -0.0765 -0.1553 330  LYS F C   
17931 O  O   . LYS F 330  ? 1.6185 1.4480 1.5027 0.2398  -0.0754 -0.1557 330  LYS F O   
17932 C  CB  . LYS F 330  ? 1.5960 1.4704 1.5100 0.2324  -0.0724 -0.1464 330  LYS F CB  
17933 C  CG  . LYS F 330  ? 1.5963 1.4905 1.5147 0.2360  -0.0717 -0.1448 330  LYS F CG  
17934 C  CD  . LYS F 330  ? 1.5881 1.4961 1.5131 0.2388  -0.0677 -0.1395 330  LYS F CD  
17935 C  CE  . LYS F 330  ? 1.5524 1.4599 1.4867 0.2315  -0.0665 -0.1361 330  LYS F CE  
17936 N  NZ  . LYS F 330  ? 1.5285 1.4530 1.4714 0.2327  -0.0633 -0.1312 330  LYS F NZ  
17937 N  N   . ARG F 331  ? 1.5191 1.3696 1.4041 0.2448  -0.0777 -0.1577 331  ARG F N   
17938 C  CA  . ARG F 331  ? 1.5657 1.4024 1.4350 0.2534  -0.0781 -0.1612 331  ARG F CA  
17939 C  C   . ARG F 331  ? 1.5978 1.4149 1.4598 0.2489  -0.0819 -0.1669 331  ARG F C   
17940 O  O   . ARG F 331  ? 1.6273 1.4264 1.4771 0.2531  -0.0817 -0.1693 331  ARG F O   
17941 C  CB  . ARG F 331  ? 1.5083 1.3566 1.3733 0.2614  -0.0779 -0.1620 331  ARG F CB  
17942 C  CG  . ARG F 331  ? 1.6220 1.4570 1.4704 0.2710  -0.0784 -0.1659 331  ARG F CG  
17943 C  CD  . ARG F 331  ? 1.6526 1.5004 1.4977 0.2816  -0.0752 -0.1639 331  ARG F CD  
17944 N  NE  . ARG F 331  ? 1.5929 1.4499 1.4442 0.2843  -0.0712 -0.1588 331  ARG F NE  
17945 C  CZ  . ARG F 331  ? 1.6541 1.5205 1.5025 0.2939  -0.0680 -0.1569 331  ARG F CZ  
17946 N  NH1 . ARG F 331  ? 1.5846 1.4524 1.4241 0.3020  -0.0678 -0.1594 331  ARG F NH1 
17947 N  NH2 . ARG F 331  ? 1.7287 1.6034 1.5834 0.2956  -0.0649 -0.1526 331  ARG F NH2 
17948 N  N   . ASN F 332  ? 1.4343 1.2547 1.3036 0.2403  -0.0855 -0.1692 332  ASN F N   
17949 C  CA  . ASN F 332  ? 1.4703 1.2738 1.3343 0.2350  -0.0895 -0.1750 332  ASN F CA  
17950 C  C   . ASN F 332  ? 1.5293 1.3214 1.3983 0.2267  -0.0885 -0.1741 332  ASN F C   
17951 O  O   . ASN F 332  ? 1.5744 1.3767 1.4569 0.2196  -0.0875 -0.1706 332  ASN F O   
17952 C  CB  . ASN F 332  ? 1.4948 1.3074 1.3647 0.2296  -0.0939 -0.1780 332  ASN F CB  
17953 C  CG  . ASN F 332  ? 1.5265 1.3227 1.3899 0.2253  -0.0987 -0.1849 332  ASN F CG  
17954 O  OD1 . ASN F 332  ? 1.6490 1.4262 1.5019 0.2269  -0.0985 -0.1876 332  ASN F OD1 
17955 N  ND2 . ASN F 332  ? 1.4556 1.2590 1.3249 0.2198  -0.1031 -0.1879 332  ASN F ND2 
17956 N  N   . LEU F 333  ? 1.4553 1.2259 1.3130 0.2277  -0.0886 -0.1773 333  LEU F N   
17957 C  CA  . LEU F 333  ? 1.4833 1.2408 1.3440 0.2202  -0.0870 -0.1764 333  LEU F CA  
17958 C  C   . LEU F 333  ? 1.5129 1.2716 1.3849 0.2078  -0.0903 -0.1792 333  LEU F C   
17959 O  O   . LEU F 333  ? 1.5064 1.2659 1.3885 0.2000  -0.0884 -0.1764 333  LEU F O   
17960 C  CB  . LEU F 333  ? 1.6041 1.3369 1.4488 0.2244  -0.0862 -0.1796 333  LEU F CB  
17961 C  CG  . LEU F 333  ? 1.7102 1.4271 1.5544 0.2195  -0.0830 -0.1777 333  LEU F CG  
17962 C  CD1 . LEU F 333  ? 1.6251 1.3548 1.4794 0.2193  -0.0789 -0.1707 333  LEU F CD1 
17963 C  CD2 . LEU F 333  ? 1.6363 1.3305 1.4623 0.2271  -0.0813 -0.1796 333  LEU F CD2 
17964 N  N   . ASN F 334  ? 1.6080 1.3670 1.4782 0.2060  -0.0952 -0.1846 334  ASN F N   
17965 C  CA  . ASN F 334  ? 1.6686 1.4296 1.5495 0.1946  -0.0989 -0.1879 334  ASN F CA  
17966 C  C   . ASN F 334  ? 1.7056 1.4878 1.6034 0.1894  -0.0982 -0.1832 334  ASN F C   
17967 O  O   . ASN F 334  ? 1.7481 1.5307 1.6570 0.1800  -0.0977 -0.1823 334  ASN F O   
17968 C  CB  . ASN F 334  ? 1.7117 1.4712 1.5869 0.1952  -0.1047 -0.1946 334  ASN F CB  
17969 C  CG  . ASN F 334  ? 1.8300 1.5660 1.6931 0.1940  -0.1067 -0.2009 334  ASN F CG  
17970 O  OD1 . ASN F 334  ? 1.8947 1.6185 1.7608 0.1858  -0.1061 -0.2023 334  ASN F OD1 
17971 N  ND2 . ASN F 334  ? 1.8302 1.5595 1.6793 0.2019  -0.1090 -0.2049 334  ASN F ND2 
17972 N  N   . THR F 335  ? 1.4033 1.2029 1.3032 0.1955  -0.0977 -0.1802 335  THR F N   
17973 C  CA  . THR F 335  ? 1.3886 1.2080 1.3035 0.1912  -0.0969 -0.1757 335  THR F CA  
17974 C  C   . THR F 335  ? 1.3501 1.1709 1.2718 0.1891  -0.0918 -0.1697 335  THR F C   
17975 O  O   . THR F 335  ? 1.2974 1.1263 1.2321 0.1812  -0.0913 -0.1673 335  THR F O   
17976 C  CB  . THR F 335  ? 1.3340 1.1699 1.2480 0.1986  -0.0969 -0.1737 335  THR F CB  
17977 O  OG1 . THR F 335  ? 1.4045 1.2351 1.3075 0.2034  -0.1007 -0.1791 335  THR F OG1 
17978 C  CG2 . THR F 335  ? 1.2247 1.0792 1.1531 0.1929  -0.0979 -0.1713 335  THR F CG2 
17979 N  N   . LEU F 336  ? 1.2820 1.0949 1.1946 0.1963  -0.0881 -0.1673 336  LEU F N   
17980 C  CA  . LEU F 336  ? 1.2133 1.0266 1.1308 0.1952  -0.0834 -0.1617 336  LEU F CA  
17981 C  C   . LEU F 336  ? 1.2028 1.0026 1.1243 0.1857  -0.0829 -0.1627 336  LEU F C   
17982 O  O   . LEU F 336  ? 1.1424 0.9477 1.0741 0.1803  -0.0803 -0.1586 336  LEU F O   
17983 C  CB  . LEU F 336  ? 1.1474 0.9537 1.0530 0.2057  -0.0801 -0.1597 336  LEU F CB  
17984 C  CG  . LEU F 336  ? 1.2279 1.0355 1.1368 0.2066  -0.0753 -0.1538 336  LEU F CG  
17985 C  CD1 . LEU F 336  ? 1.1860 1.0160 1.1080 0.2052  -0.0741 -0.1490 336  LEU F CD1 
17986 C  CD2 . LEU F 336  ? 1.2965 1.0956 1.1921 0.2176  -0.0728 -0.1528 336  LEU F CD2 
17987 N  N   . ALA F 337  ? 1.4794 1.2613 1.3927 0.1835  -0.0852 -0.1682 337  ALA F N   
17988 C  CA  . ALA F 337  ? 1.5221 1.2907 1.4394 0.1738  -0.0845 -0.1696 337  ALA F CA  
17989 C  C   . ALA F 337  ? 1.5037 1.2848 1.4370 0.1633  -0.0870 -0.1703 337  ALA F C   
17990 O  O   . ALA F 337  ? 1.4701 1.2496 1.4124 0.1554  -0.0846 -0.1682 337  ALA F O   
17991 C  CB  . ALA F 337  ? 1.4724 1.2191 1.3770 0.1736  -0.0866 -0.1759 337  ALA F CB  
17992 N  N   . THR F 338  ? 1.2381 1.0318 1.1750 0.1634  -0.0915 -0.1732 338  THR F N   
17993 C  CA  . THR F 338  ? 1.2016 1.0088 1.1537 0.1545  -0.0941 -0.1738 338  THR F CA  
17994 C  C   . THR F 338  ? 1.0712 0.8940 1.0350 0.1531  -0.0905 -0.1669 338  THR F C   
17995 O  O   . THR F 338  ? 1.0581 0.8850 1.0340 0.1445  -0.0898 -0.1657 338  THR F O   
17996 C  CB  . THR F 338  ? 1.1967 1.0141 1.1485 0.1565  -0.0996 -0.1779 338  THR F CB  
17997 O  OG1 . THR F 338  ? 1.1872 0.9895 1.1258 0.1597  -0.1027 -0.1840 338  THR F OG1 
17998 C  CG2 . THR F 338  ? 1.1866 1.0145 1.1526 0.1470  -0.1031 -0.1798 338  THR F CG2 
17999 N  N   . ILE F 339  ? 1.1481 0.9800 1.1085 0.1616  -0.0880 -0.1625 339  ILE F N   
18000 C  CA  . ILE F 339  ? 1.1194 0.9655 1.0898 0.1608  -0.0845 -0.1560 339  ILE F CA  
18001 C  C   . ILE F 339  ? 1.1783 1.0137 1.1498 0.1575  -0.0799 -0.1527 339  ILE F C   
18002 O  O   . ILE F 339  ? 1.2559 1.0987 1.2387 0.1515  -0.0779 -0.1492 339  ILE F O   
18003 C  CB  . ILE F 339  ? 1.0852 0.9428 1.0512 0.1705  -0.0829 -0.1526 339  ILE F CB  
18004 C  CG1 . ILE F 339  ? 1.0158 0.8840 0.9809 0.1734  -0.0869 -0.1555 339  ILE F CG1 
18005 C  CG2 . ILE F 339  ? 1.1561 1.0271 1.1318 0.1697  -0.0791 -0.1461 339  ILE F CG2 
18006 C  CD1 . ILE F 339  ? 0.9906 0.8694 0.9677 0.1655  -0.0901 -0.1568 339  ILE F CD1 
18007 N  N   . ALA F 340  ? 1.0415 0.8590 1.0006 0.1616  -0.0782 -0.1539 340  ALA F N   
18008 C  CA  . ALA F 340  ? 1.0373 0.8426 0.9954 0.1592  -0.0737 -0.1508 340  ALA F CA  
18009 C  C   . ALA F 340  ? 1.1415 0.9405 1.1085 0.1475  -0.0739 -0.1526 340  ALA F C   
18010 O  O   . ALA F 340  ? 1.1261 0.9238 1.0992 0.1430  -0.0700 -0.1487 340  ALA F O   
18011 C  CB  . ALA F 340  ? 1.0780 0.8638 1.0196 0.1663  -0.0722 -0.1522 340  ALA F CB  
18012 N  N   . GLY F 341  ? 1.4271 1.2226 1.3953 0.1424  -0.0782 -0.1586 341  GLY F N   
18013 C  CA  . GLY F 341  ? 1.3619 1.1538 1.3402 0.1308  -0.0787 -0.1608 341  GLY F CA  
18014 C  C   . GLY F 341  ? 1.3634 1.1746 1.3583 0.1252  -0.0785 -0.1575 341  GLY F C   
18015 O  O   . GLY F 341  ? 1.4645 1.2740 1.4681 0.1175  -0.0757 -0.1556 341  GLY F O   
18016 N  N   . TRP F 342  ? 1.2767 1.1059 1.2755 0.1290  -0.0812 -0.1567 342  TRP F N   
18017 C  CA  . TRP F 342  ? 1.3455 1.1932 1.3588 0.1249  -0.0808 -0.1530 342  TRP F CA  
18018 C  C   . TRP F 342  ? 1.3733 1.2230 1.3886 0.1264  -0.0751 -0.1461 342  TRP F C   
18019 O  O   . TRP F 342  ? 1.3574 1.2130 1.3840 0.1200  -0.0729 -0.1432 342  TRP F O   
18020 C  CB  . TRP F 342  ? 1.2467 1.1113 1.2614 0.1298  -0.0843 -0.1533 342  TRP F CB  
18021 C  CG  . TRP F 342  ? 1.3246 1.2075 1.3534 0.1257  -0.0843 -0.1501 342  TRP F CG  
18022 C  CD1 . TRP F 342  ? 1.3245 1.2209 1.3565 0.1296  -0.0819 -0.1446 342  TRP F CD1 
18023 C  CD2 . TRP F 342  ? 1.4579 1.3475 1.4991 0.1170  -0.0869 -0.1524 342  TRP F CD2 
18024 N  NE1 . TRP F 342  ? 1.3838 1.2940 1.4288 0.1240  -0.0826 -0.1432 342  TRP F NE1 
18025 C  CE2 . TRP F 342  ? 1.4705 1.3772 1.5215 0.1165  -0.0858 -0.1478 342  TRP F CE2 
18026 C  CE3 . TRP F 342  ? 1.4604 1.3434 1.5056 0.1095  -0.0902 -0.1580 342  TRP F CE3 
18027 C  CZ2 . TRP F 342  ? 1.4711 1.3883 1.5353 0.1094  -0.0877 -0.1485 342  TRP F CZ2 
18028 C  CZ3 . TRP F 342  ? 1.5342 1.4288 1.5934 0.1023  -0.0922 -0.1589 342  TRP F CZ3 
18029 C  CH2 . TRP F 342  ? 1.4850 1.3964 1.5533 0.1026  -0.0909 -0.1541 342  TRP F CH2 
18030 N  N   . ILE F 343  ? 1.0600 0.9050 1.0645 0.1352  -0.0726 -0.1435 343  ILE F N   
18031 C  CA  . ILE F 343  ? 0.9593 0.8056 0.9645 0.1375  -0.0675 -0.1373 343  ILE F CA  
18032 C  C   . ILE F 343  ? 1.0351 0.8665 1.0411 0.1311  -0.0639 -0.1363 343  ILE F C   
18033 O  O   . ILE F 343  ? 1.0236 0.8597 1.0377 0.1273  -0.0606 -0.1320 343  ILE F O   
18034 C  CB  . ILE F 343  ? 0.8593 0.7030 0.8521 0.1486  -0.0661 -0.1355 343  ILE F CB  
18035 C  CG1 . ILE F 343  ? 0.9635 0.8249 0.9578 0.1542  -0.0685 -0.1351 343  ILE F CG1 
18036 C  CG2 . ILE F 343  ? 0.9295 0.7705 0.9210 0.1510  -0.0611 -0.1298 343  ILE F CG2 
18037 C  CD1 . ILE F 343  ? 0.9959 0.8576 0.9797 0.1650  -0.0670 -0.1333 343  ILE F CD1 
18038 N  N   . VAL F 344  ? 1.1542 0.9668 1.1517 0.1298  -0.0643 -0.1405 344  VAL F N   
18039 C  CA  . VAL F 344  ? 1.2141 1.0106 1.2113 0.1235  -0.0605 -0.1399 344  VAL F CA  
18040 C  C   . VAL F 344  ? 1.2328 1.0371 1.2458 0.1124  -0.0605 -0.1400 344  VAL F C   
18041 O  O   . VAL F 344  ? 1.2241 1.0260 1.2423 0.1080  -0.0560 -0.1362 344  VAL F O   
18042 C  CB  . VAL F 344  ? 1.2240 0.9989 1.2092 0.1235  -0.0613 -0.1451 344  VAL F CB  
18043 C  CG1 . VAL F 344  ? 1.2450 1.0059 1.2341 0.1133  -0.0586 -0.1463 344  VAL F CG1 
18044 C  CG2 . VAL F 344  ? 1.3090 1.0718 1.2781 0.1340  -0.0590 -0.1432 344  VAL F CG2 
18045 N  N   . VAL F 345  ? 1.0870 0.9013 1.1078 0.1082  -0.0654 -0.1445 345  VAL F N   
18046 C  CA  . VAL F 345  ? 1.0914 0.9152 1.1279 0.0982  -0.0659 -0.1450 345  VAL F CA  
18047 C  C   . VAL F 345  ? 1.1110 0.9507 1.1569 0.0985  -0.0632 -0.1387 345  VAL F C   
18048 O  O   . VAL F 345  ? 1.1382 0.9790 1.1935 0.0916  -0.0600 -0.1362 345  VAL F O   
18049 C  CB  . VAL F 345  ? 0.9649 0.7981 1.0071 0.0953  -0.0724 -0.1509 345  VAL F CB  
18050 C  CG1 . VAL F 345  ? 0.8384 0.6868 0.8977 0.0872  -0.0733 -0.1505 345  VAL F CG1 
18051 C  CG2 . VAL F 345  ? 0.9436 0.7599 0.9791 0.0921  -0.0748 -0.1576 345  VAL F CG2 
18052 N  N   . MET F 346  ? 1.5051 1.3569 1.5483 0.1065  -0.0641 -0.1359 346  MET F N   
18053 C  CA  . MET F 346  ? 1.4545 1.3213 1.5059 0.1071  -0.0617 -0.1302 346  MET F CA  
18054 C  C   . MET F 346  ? 1.4760 1.3339 1.5239 0.1081  -0.0558 -0.1250 346  MET F C   
18055 O  O   . MET F 346  ? 1.5405 1.4056 1.5973 0.1044  -0.0528 -0.1209 346  MET F O   
18056 C  CB  . MET F 346  ? 1.4034 1.2840 1.4518 0.1153  -0.0638 -0.1288 346  MET F CB  
18057 C  CG  . MET F 346  ? 1.4782 1.3731 1.5339 0.1135  -0.0688 -0.1318 346  MET F CG  
18058 S  SD  . MET F 346  ? 1.5363 1.4439 1.6096 0.1040  -0.0684 -0.1302 346  MET F SD  
18059 C  CE  . MET F 346  ? 1.5781 1.4833 1.6557 0.0976  -0.0741 -0.1379 346  MET F CE  
18060 N  N   . ARG F 347  ? 1.0773 0.9193 1.1118 0.1135  -0.0539 -0.1251 347  ARG F N   
18061 C  CA  . ARG F 347  ? 1.0970 0.9295 1.1269 0.1151  -0.0485 -0.1202 347  ARG F CA  
18062 C  C   . ARG F 347  ? 1.0743 0.8985 1.1111 0.1055  -0.0451 -0.1197 347  ARG F C   
18063 O  O   . ARG F 347  ? 1.1028 0.9277 1.1428 0.1042  -0.0407 -0.1148 347  ARG F O   
18064 C  CB  . ARG F 347  ? 1.0575 0.8731 1.0709 0.1229  -0.0474 -0.1209 347  ARG F CB  
18065 C  CG  . ARG F 347  ? 1.0757 0.8990 1.0814 0.1333  -0.0498 -0.1210 347  ARG F CG  
18066 C  CD  . ARG F 347  ? 1.0792 0.9124 1.0844 0.1398  -0.0473 -0.1153 347  ARG F CD  
18067 N  NE  . ARG F 347  ? 1.0949 0.9438 1.1136 0.1347  -0.0464 -0.1119 347  ARG F NE  
18068 C  CZ  . ARG F 347  ? 1.1041 0.9713 1.1312 0.1343  -0.0492 -0.1121 347  ARG F CZ  
18069 N  NH1 . ARG F 347  ? 1.2307 1.1035 1.2545 0.1385  -0.0530 -0.1154 347  ARG F NH1 
18070 N  NH2 . ARG F 347  ? 1.0126 0.8922 1.0511 0.1296  -0.0479 -0.1089 347  ARG F NH2 
18071 N  N   . PHE F 348  ? 1.1794 0.9959 1.2188 0.0985  -0.0470 -0.1249 348  PHE F N   
18072 C  CA  . PHE F 348  ? 1.2439 1.0538 1.2915 0.0884  -0.0437 -0.1250 348  PHE F CA  
18073 C  C   . PHE F 348  ? 1.2009 1.0289 1.2641 0.0832  -0.0432 -0.1221 348  PHE F C   
18074 O  O   . PHE F 348  ? 1.2036 1.0287 1.2720 0.0784  -0.0384 -0.1186 348  PHE F O   
18075 C  CB  . PHE F 348  ? 1.2815 1.0827 1.3305 0.0817  -0.0468 -0.1319 348  PHE F CB  
18076 C  CG  . PHE F 348  ? 1.3294 1.1066 1.3643 0.0829  -0.0447 -0.1340 348  PHE F CG  
18077 C  CD1 . PHE F 348  ? 1.3209 1.0901 1.3407 0.0929  -0.0458 -0.1343 348  PHE F CD1 
18078 C  CD2 . PHE F 348  ? 1.3949 1.1571 1.4316 0.0741  -0.0415 -0.1359 348  PHE F CD2 
18079 C  CE1 . PHE F 348  ? 1.3202 1.0666 1.3263 0.0945  -0.0439 -0.1363 348  PHE F CE1 
18080 C  CE2 . PHE F 348  ? 1.4848 1.2237 1.5078 0.0751  -0.0393 -0.1380 348  PHE F CE2 
18081 C  CZ  . PHE F 348  ? 1.4439 1.1745 1.4512 0.0856  -0.0406 -0.1381 348  PHE F CZ  
18082 N  N   . VAL F 349  ? 1.1437 0.9900 1.2141 0.0844  -0.0478 -0.1233 349  VAL F N   
18083 C  CA  . VAL F 349  ? 1.1921 1.0558 1.2769 0.0801  -0.0476 -0.1207 349  VAL F CA  
18084 C  C   . VAL F 349  ? 1.1947 1.0636 1.2783 0.0847  -0.0435 -0.1139 349  VAL F C   
18085 O  O   . VAL F 349  ? 1.1649 1.0395 1.2577 0.0801  -0.0403 -0.1105 349  VAL F O   
18086 C  CB  . VAL F 349  ? 1.0436 0.9242 1.1345 0.0810  -0.0537 -0.1238 349  VAL F CB  
18087 C  CG1 . VAL F 349  ? 0.8601 0.7579 0.9655 0.0766  -0.0534 -0.1213 349  VAL F CG1 
18088 C  CG2 . VAL F 349  ? 0.9979 0.8728 1.0889 0.0770  -0.0582 -0.1310 349  VAL F CG2 
18089 N  N   . ASP F 350  ? 1.1858 1.0531 1.2583 0.0939  -0.0435 -0.1120 350  ASP F N   
18090 C  CA  . ASP F 350  ? 1.1454 1.0177 1.2163 0.0986  -0.0400 -0.1060 350  ASP F CA  
18091 C  C   . ASP F 350  ? 1.0454 0.9046 1.1145 0.0956  -0.0342 -0.1026 350  ASP F C   
18092 O  O   . ASP F 350  ? 1.0285 0.8944 1.1037 0.0939  -0.0310 -0.0982 350  ASP F O   
18093 C  CB  . ASP F 350  ? 1.2333 1.1050 1.2922 0.1090  -0.0411 -0.1054 350  ASP F CB  
18094 C  CG  . ASP F 350  ? 1.3317 1.2107 1.3896 0.1141  -0.0383 -0.0997 350  ASP F CG  
18095 O  OD1 . ASP F 350  ? 1.3301 1.2219 1.3982 0.1108  -0.0374 -0.0969 350  ASP F OD1 
18096 O  OD2 . ASP F 350  ? 1.3175 1.1895 1.3644 0.1216  -0.0370 -0.0982 350  ASP F OD2 
18097 N  N   . MET F 351  ? 1.2493 1.0893 1.3095 0.0949  -0.0325 -0.1046 351  MET F N   
18098 C  CA  . MET F 351  ? 1.2660 1.0916 1.3233 0.0920  -0.0265 -0.1014 351  MET F CA  
18099 C  C   . MET F 351  ? 1.2712 1.1007 1.3424 0.0815  -0.0244 -0.1012 351  MET F C   
18100 O  O   . MET F 351  ? 1.2488 1.0757 1.3222 0.0792  -0.0194 -0.0969 351  MET F O   
18101 C  CB  . MET F 351  ? 1.2818 1.0850 1.3261 0.0933  -0.0253 -0.1040 351  MET F CB  
18102 C  CG  . MET F 351  ? 1.3124 1.1124 1.3436 0.1036  -0.0281 -0.1052 351  MET F CG  
18103 S  SD  . MET F 351  ? 1.5791 1.3533 1.5910 0.1100  -0.0242 -0.1041 351  MET F SD  
18104 C  CE  . MET F 351  ? 1.4112 1.1911 1.4128 0.1220  -0.0289 -0.1058 351  MET F CE  
18105 N  N   . ALA F 352  ? 1.3894 1.2253 1.4699 0.0752  -0.0282 -0.1061 352  ALA F N   
18106 C  CA  . ALA F 352  ? 1.3723 1.2153 1.4676 0.0656  -0.0268 -0.1063 352  ALA F CA  
18107 C  C   . ALA F 352  ? 1.3695 1.2302 1.4737 0.0665  -0.0260 -0.1017 352  ALA F C   
18108 O  O   . ALA F 352  ? 1.3986 1.2611 1.5111 0.0609  -0.0219 -0.0989 352  ALA F O   
18109 C  CB  . ALA F 352  ? 1.3942 1.2431 1.4977 0.0600  -0.0321 -0.1128 352  ALA F CB  
18110 N  N   . TRP F 353  ? 1.1474 1.0210 1.2500 0.0734  -0.0295 -0.1008 353  TRP F N   
18111 C  CA  . TRP F 353  ? 1.0663 0.9561 1.1763 0.0745  -0.0288 -0.0965 353  TRP F CA  
18112 C  C   . TRP F 353  ? 1.0992 0.9831 1.2039 0.0775  -0.0233 -0.0906 353  TRP F C   
18113 O  O   . TRP F 353  ? 1.1335 1.0269 1.2454 0.0758  -0.0210 -0.0869 353  TRP F O   
18114 C  CB  . TRP F 353  ? 0.9803 0.8838 1.0887 0.0811  -0.0336 -0.0972 353  TRP F CB  
18115 C  CG  . TRP F 353  ? 0.9461 0.8666 1.0622 0.0820  -0.0335 -0.0935 353  TRP F CG  
18116 C  CD1 . TRP F 353  ? 0.9658 0.8987 1.0949 0.0764  -0.0341 -0.0935 353  TRP F CD1 
18117 C  CD2 . TRP F 353  ? 0.8537 0.7809 0.9651 0.0889  -0.0326 -0.0896 353  TRP F CD2 
18118 N  NE1 . TRP F 353  ? 0.8970 0.8427 1.0289 0.0795  -0.0336 -0.0896 353  TRP F NE1 
18119 C  CE2 . TRP F 353  ? 0.8163 0.7589 0.9377 0.0869  -0.0326 -0.0872 353  TRP F CE2 
18120 C  CE3 . TRP F 353  ? 0.8236 0.7453 0.9232 0.0968  -0.0319 -0.0879 353  TRP F CE3 
18121 C  CZ2 . TRP F 353  ? 0.8037 0.7557 0.9236 0.0918  -0.0318 -0.0834 353  TRP F CZ2 
18122 C  CZ3 . TRP F 353  ? 0.8028 0.7351 0.9018 0.1017  -0.0313 -0.0843 353  TRP F CZ3 
18123 C  CH2 . TRP F 353  ? 0.8086 0.7556 0.9177 0.0989  -0.0312 -0.0821 353  TRP F CH2 
18124 N  N   . ILE F 354  ? 1.0513 0.9194 1.1428 0.0822  -0.0211 -0.0898 354  ILE F N   
18125 C  CA  . ILE F 354  ? 0.9873 0.8494 1.0723 0.0861  -0.0163 -0.0844 354  ILE F CA  
18126 C  C   . ILE F 354  ? 1.0086 0.8573 1.0949 0.0795  -0.0106 -0.0827 354  ILE F C   
18127 O  O   . ILE F 354  ? 1.0919 0.9421 1.1805 0.0788  -0.0064 -0.0782 354  ILE F O   
18128 C  CB  . ILE F 354  ? 1.0121 0.8648 1.0817 0.0956  -0.0168 -0.0840 354  ILE F CB  
18129 C  CG1 . ILE F 354  ? 1.0540 0.9208 1.1229 0.1019  -0.0220 -0.0857 354  ILE F CG1 
18130 C  CG2 . ILE F 354  ? 1.0363 0.8829 1.0987 0.1001  -0.0122 -0.0787 354  ILE F CG2 
18131 C  CD1 . ILE F 354  ? 1.2035 1.0629 1.2582 0.1115  -0.0228 -0.0857 354  ILE F CD1 
18132 N  N   . ILE F 355  ? 0.9118 0.7470 0.9966 0.0746  -0.0100 -0.0864 355  ILE F N   
18133 C  CA  . ILE F 355  ? 0.9300 0.7492 1.0136 0.0688  -0.0039 -0.0850 355  ILE F CA  
18134 C  C   . ILE F 355  ? 0.9503 0.7764 1.0497 0.0581  -0.0028 -0.0865 355  ILE F C   
18135 O  O   . ILE F 355  ? 0.9830 0.8071 1.0869 0.0539  0.0026  -0.0830 355  ILE F O   
18136 C  CB  . ILE F 355  ? 0.8605 0.6583 0.9313 0.0700  -0.0031 -0.0879 355  ILE F CB  
18137 C  CG1 . ILE F 355  ? 0.9126 0.7069 0.9691 0.0811  -0.0057 -0.0874 355  ILE F CG1 
18138 C  CG2 . ILE F 355  ? 0.8881 0.6671 0.9539 0.0662  0.0042  -0.0851 355  ILE F CG2 
18139 C  CD1 . ILE F 355  ? 0.9515 0.7402 0.9981 0.0883  -0.0017 -0.0817 355  ILE F CD1 
18140 N  N   . LEU F 356  ? 1.4694 1.3039 1.5773 0.0538  -0.0077 -0.0919 356  LEU F N   
18141 C  CA  . LEU F 356  ? 1.5244 1.3642 1.6471 0.0435  -0.0069 -0.0942 356  LEU F CA  
18142 C  C   . LEU F 356  ? 1.5786 1.4346 1.7138 0.0408  -0.0052 -0.0905 356  LEU F C   
18143 O  O   . LEU F 356  ? 1.6418 1.4967 1.7864 0.0329  -0.0011 -0.0901 356  LEU F O   
18144 C  CB  . LEU F 356  ? 1.5284 1.3752 1.6571 0.0404  -0.0135 -0.1010 356  LEU F CB  
18145 C  CG  . LEU F 356  ? 1.5466 1.3762 1.6657 0.0400  -0.0149 -0.1059 356  LEU F CG  
18146 C  CD1 . LEU F 356  ? 1.4402 1.2783 1.5675 0.0357  -0.0213 -0.1127 356  LEU F CD1 
18147 C  CD2 . LEU F 356  ? 1.6284 1.4384 1.7444 0.0340  -0.0082 -0.1052 356  LEU F CD2 
18148 N  N   . PRO F 357  ? 1.1349 1.0061 1.2714 0.0467  -0.0078 -0.0879 357  PRO F N   
18149 C  CA  . PRO F 357  ? 1.1364 1.0217 1.2844 0.0440  -0.0057 -0.0844 357  PRO F CA  
18150 C  C   . PRO F 357  ? 1.1264 1.0023 1.2732 0.0416  0.0018  -0.0795 357  PRO F C   
18151 O  O   . PRO F 357  ? 1.1549 1.0391 1.3132 0.0363  0.0045  -0.0778 357  PRO F O   
18152 C  CB  . PRO F 357  ? 0.9690 0.8672 1.1137 0.0522  -0.0091 -0.0821 357  PRO F CB  
18153 C  CG  . PRO F 357  ? 0.9930 0.8916 1.1326 0.0558  -0.0151 -0.0867 357  PRO F CG  
18154 C  CD  . PRO F 357  ? 1.0447 0.9229 1.1742 0.0551  -0.0131 -0.0887 357  PRO F CD  
18155 N  N   . GLU F 358  ? 1.2354 1.0941 1.3683 0.0457  0.0054  -0.0771 358  GLU F N   
18156 C  CA  . GLU F 358  ? 1.3142 1.1627 1.4442 0.0442  0.0128  -0.0722 358  GLU F CA  
18157 C  C   . GLU F 358  ? 1.3773 1.2191 1.5161 0.0340  0.0172  -0.0738 358  GLU F C   
18158 O  O   . GLU F 358  ? 1.4152 1.2575 1.5595 0.0301  0.0227  -0.0703 358  GLU F O   
18159 C  CB  . GLU F 358  ? 1.3040 1.1343 1.4160 0.0513  0.0153  -0.0699 358  GLU F CB  
18160 C  CG  . GLU F 358  ? 1.3043 1.1416 1.4078 0.0616  0.0115  -0.0681 358  GLU F CG  
18161 C  CD  . GLU F 358  ? 1.4069 1.2491 1.5089 0.0654  0.0147  -0.0624 358  GLU F CD  
18162 O  OE1 . GLU F 358  ? 1.3955 1.2334 1.5011 0.0607  0.0203  -0.0594 358  GLU F OE1 
18163 O  OE2 . GLU F 358  ? 1.3252 1.1755 1.4223 0.0730  0.0116  -0.0609 358  GLU F OE2 
18164 N  N   . PHE F 359  ? 1.3219 1.1577 1.4624 0.0292  0.0150  -0.0793 359  PHE F N   
18165 C  CA  . PHE F 359  ? 1.3490 1.1788 1.4986 0.0188  0.0189  -0.0816 359  PHE F CA  
18166 C  C   . PHE F 359  ? 1.3574 1.2070 1.5256 0.0124  0.0150  -0.0852 359  PHE F C   
18167 O  O   . PHE F 359  ? 1.4099 1.2668 1.5897 0.0067  0.0188  -0.0834 359  PHE F O   
18168 C  CB  . PHE F 359  ? 1.3515 1.1629 1.4930 0.0164  0.0187  -0.0861 359  PHE F CB  
18169 C  CG  . PHE F 359  ? 1.3320 1.1279 1.4543 0.0255  0.0186  -0.0845 359  PHE F CG  
18170 C  CD1 . PHE F 359  ? 1.3778 1.1628 1.4887 0.0309  0.0241  -0.0786 359  PHE F CD1 
18171 C  CD2 . PHE F 359  ? 1.3033 1.0958 1.4187 0.0291  0.0129  -0.0891 359  PHE F CD2 
18172 C  CE1 . PHE F 359  ? 1.2787 1.0502 1.3720 0.0397  0.0237  -0.0774 359  PHE F CE1 
18173 C  CE2 . PHE F 359  ? 1.3360 1.1149 1.4340 0.0378  0.0127  -0.0878 359  PHE F CE2 
18174 C  CZ  . PHE F 359  ? 1.2467 1.0153 1.3338 0.0432  0.0181  -0.0820 359  PHE F CZ  
18175 N  N   . ARG F 360  ? 1.6707 1.5290 1.8411 0.0137  0.0075  -0.0903 360  ARG F N   
18176 C  CA  . ARG F 360  ? 1.7208 1.5957 1.9078 0.0074  0.0033  -0.0949 360  ARG F CA  
18177 C  C   . ARG F 360  ? 1.7940 1.6890 1.9912 0.0089  0.0025  -0.0917 360  ARG F C   
18178 O  O   . ARG F 360  ? 1.8624 1.7687 2.0747 0.0022  0.0031  -0.0929 360  ARG F O   
18179 C  CB  . ARG F 360  ? 1.7124 1.5903 1.8970 0.0096  -0.0046 -0.1009 360  ARG F CB  
18180 C  CG  . ARG F 360  ? 1.7528 1.6103 1.9266 0.0083  -0.0042 -0.1045 360  ARG F CG  
18181 C  CD  . ARG F 360  ? 1.8073 1.6572 1.9901 -0.0029 -0.0005 -0.1078 360  ARG F CD  
18182 N  NE  . ARG F 360  ? 1.8038 1.6397 1.9834 -0.0060 0.0085  -0.1031 360  ARG F NE  
18183 C  CZ  . ARG F 360  ? 1.8195 1.6327 1.9868 -0.0065 0.0131  -0.1027 360  ARG F CZ  
18184 N  NH1 . ARG F 360  ? 1.8085 1.6098 1.9650 -0.0040 0.0096  -0.1068 360  ARG F NH1 
18185 N  NH2 . ARG F 360  ? 1.8569 1.6584 2.0217 -0.0092 0.0215  -0.0981 360  ARG F NH2 
18186 N  N   . GLU F 361  ? 1.7057 1.6058 1.8952 0.0175  0.0010  -0.0877 361  GLU F N   
18187 C  CA  . GLU F 361  ? 1.7520 1.6693 1.9488 0.0199  0.0005  -0.0843 361  GLU F CA  
18188 C  C   . GLU F 361  ? 1.6758 1.6118 1.8848 0.0181  -0.0060 -0.0884 361  GLU F C   
18189 O  O   . GLU F 361  ? 1.6556 1.6065 1.8703 0.0205  -0.0072 -0.0861 361  GLU F O   
18190 C  CB  . GLU F 361  ? 1.8336 1.7503 2.0368 0.0155  0.0078  -0.0798 361  GLU F CB  
18191 C  CG  . GLU F 361  ? 1.8738 1.8043 2.0810 0.0190  0.0086  -0.0751 361  GLU F CG  
18192 C  CD  . GLU F 361  ? 1.8746 1.8185 2.0987 0.0124  0.0100  -0.0755 361  GLU F CD  
18193 O  OE1 . GLU F 361  ? 1.8578 1.7993 2.0905 0.0046  0.0113  -0.0790 361  GLU F OE1 
18194 O  OE2 . GLU F 361  ? 1.9031 1.8598 2.1317 0.0149  0.0098  -0.0724 361  GLU F OE2 
18195 N  N   . HIS F 362  ? 1.6039 1.5390 1.8162 0.0144  -0.0103 -0.0947 362  HIS F N   
18196 C  CA  . HIS F 362  ? 1.5160 1.4674 1.7379 0.0136  -0.0172 -0.0992 362  HIS F CA  
18197 C  C   . HIS F 362  ? 1.5221 1.4669 1.7368 0.0150  -0.0227 -0.1049 362  HIS F C   
18198 O  O   . HIS F 362  ? 1.6023 1.5306 1.8102 0.0127  -0.0206 -0.1067 362  HIS F O   
18199 C  CB  . HIS F 362  ? 1.5634 1.5242 1.8025 0.0046  -0.0164 -0.1019 362  HIS F CB  
18200 C  CG  . HIS F 362  ? 1.6173 1.5886 1.8651 0.0037  -0.0122 -0.0970 362  HIS F CG  
18201 N  ND1 . HIS F 362  ? 1.4978 1.4875 1.7534 0.0063  -0.0158 -0.0964 362  HIS F ND1 
18202 C  CD2 . HIS F 362  ? 1.6884 1.6538 1.9379 0.0007  -0.0046 -0.0924 362  HIS F CD2 
18203 C  CE1 . HIS F 362  ? 1.5806 1.5754 1.8423 0.0050  -0.0106 -0.0917 362  HIS F CE1 
18204 N  NE2 . HIS F 362  ? 1.6322 1.6126 1.8905 0.0016  -0.0038 -0.0893 362  HIS F NE2 
18205 N  N   . LEU F 363  ? 1.0046 0.9617 1.2204 0.0190  -0.0296 -0.1076 363  LEU F N   
18206 C  CA  . LEU F 363  ? 0.9430 0.8948 1.1526 0.0203  -0.0352 -0.1135 363  LEU F CA  
18207 C  C   . LEU F 363  ? 1.0048 0.9543 1.2238 0.0113  -0.0365 -0.1196 363  LEU F C   
18208 O  O   . LEU F 363  ? 1.0729 1.0090 1.2851 0.0098  -0.0376 -0.1237 363  LEU F O   
18209 C  CB  . LEU F 363  ? 0.8725 0.8385 1.0813 0.0265  -0.0419 -0.1149 363  LEU F CB  
18210 C  CG  . LEU F 363  ? 0.8374 0.7958 1.0339 0.0317  -0.0467 -0.1187 363  LEU F CG  
18211 C  CD1 . LEU F 363  ? 0.8108 0.7519 0.9927 0.0358  -0.0426 -0.1157 363  LEU F CD1 
18212 C  CD2 . LEU F 363  ? 0.8632 0.8351 1.0576 0.0387  -0.0520 -0.1188 363  LEU F CD2 
18213 N  N   . TRP F 364  ? 1.5558 1.5183 1.7905 0.0052  -0.0364 -0.1206 364  TRP F N   
18214 C  CA  . TRP F 364  ? 1.5740 1.5360 1.8194 -0.0040 -0.0376 -0.1267 364  TRP F CA  
18215 C  C   . TRP F 364  ? 1.6179 1.5626 1.8620 -0.0105 -0.0302 -0.1257 364  TRP F C   
18216 O  O   . TRP F 364  ? 1.6957 1.6321 1.9420 -0.0171 -0.0309 -0.1312 364  TRP F O   
18217 C  CB  . TRP F 364  ? 1.6124 1.5944 1.8756 -0.0082 -0.0394 -0.1280 364  TRP F CB  
18218 C  CG  . TRP F 364  ? 1.6932 1.6852 1.9602 -0.0051 -0.0356 -0.1213 364  TRP F CG  
18219 C  CD1 . TRP F 364  ? 1.7385 1.7304 2.0129 -0.0097 -0.0286 -0.1172 364  TRP F CD1 
18220 C  CD2 . TRP F 364  ? 1.6568 1.6605 1.9204 0.0030  -0.0386 -0.1180 364  TRP F CD2 
18221 N  NE1 . TRP F 364  ? 1.7399 1.7423 2.0153 -0.0047 -0.0271 -0.1117 364  TRP F NE1 
18222 C  CE2 . TRP F 364  ? 1.6888 1.6984 1.9577 0.0030  -0.0332 -0.1121 364  TRP F CE2 
18223 C  CE3 . TRP F 364  ? 1.6076 1.6167 1.8638 0.0103  -0.0449 -0.1194 364  TRP F CE3 
18224 C  CZ2 . TRP F 364  ? 1.6371 1.6575 1.9042 0.0097  -0.0341 -0.1078 364  TRP F CZ2 
18225 C  CZ3 . TRP F 364  ? 1.6471 1.6670 1.9017 0.0168  -0.0455 -0.1150 364  TRP F CZ3 
18226 C  CH2 . TRP F 364  ? 1.7020 1.7273 1.9619 0.0163  -0.0402 -0.1093 364  TRP F CH2 
18227 N  N   . ASP F 365  ? 1.6333 1.5718 1.8733 -0.0089 -0.0231 -0.1189 365  ASP F N   
18228 C  CA  . ASP F 365  ? 1.6710 1.5920 1.9083 -0.0145 -0.0155 -0.1173 365  ASP F CA  
18229 C  C   . ASP F 365  ? 1.6557 1.5557 1.8774 -0.0126 -0.0153 -0.1192 365  ASP F C   
18230 O  O   . ASP F 365  ? 1.6179 1.5017 1.8372 -0.0182 -0.0096 -0.1193 365  ASP F O   
18231 C  CB  . ASP F 365  ? 1.6654 1.5845 1.9002 -0.0120 -0.0083 -0.1094 365  ASP F CB  
18232 C  CG  . ASP F 365  ? 1.7221 1.6548 1.9736 -0.0181 -0.0051 -0.1079 365  ASP F CG  
18233 O  OD1 . ASP F 365  ? 1.7202 1.6664 1.9857 -0.0232 -0.0092 -0.1129 365  ASP F OD1 
18234 O  OD2 . ASP F 365  ? 1.8425 1.7724 2.0929 -0.0174 0.0015  -0.1019 365  ASP F OD2 
18235 N  N   . ILE F 366  ? 1.1733 1.0726 1.3841 -0.0049 -0.0210 -0.1207 366  ILE F N   
18236 C  CA  . ILE F 366  ? 1.1069 0.9869 1.3031 -0.0028 -0.0215 -0.1233 366  ILE F CA  
18237 C  C   . ILE F 366  ? 1.0579 0.9308 1.2603 -0.0123 -0.0223 -0.1301 366  ILE F C   
18238 O  O   . ILE F 366  ? 1.0361 0.9224 1.2502 -0.0164 -0.0279 -0.1356 366  ILE F O   
18239 C  CB  . ILE F 366  ? 1.1374 1.0216 1.3236 0.0066  -0.0284 -0.1247 366  ILE F CB  
18240 C  CG1 . ILE F 366  ? 1.0988 0.9869 1.2771 0.0159  -0.0266 -0.1179 366  ILE F CG1 
18241 C  CG2 . ILE F 366  ? 1.1133 0.9792 1.2862 0.0081  -0.0299 -0.1287 366  ILE F CG2 
18242 C  CD1 . ILE F 366  ? 0.8894 0.7804 1.0571 0.0251  -0.0324 -0.1189 366  ILE F CD1 
18243 N  N   . ALA F 367  ? 1.6644 1.5162 1.8589 -0.0157 -0.0168 -0.1300 367  ALA F N   
18244 C  CA  . ALA F 367  ? 1.7792 1.6217 1.9790 -0.0257 -0.0163 -0.1362 367  ALA F CA  
18245 C  C   . ALA F 367  ? 1.8170 1.6460 2.0038 -0.0228 -0.0210 -0.1414 367  ALA F C   
18246 O  O   . ALA F 367  ? 1.7597 1.5874 1.9340 -0.0130 -0.0245 -0.1402 367  ALA F O   
18247 C  CB  . ALA F 367  ? 1.8263 1.6531 2.0258 -0.0323 -0.0067 -0.1329 367  ALA F CB  
18248 N  N   . ILE F 368  ? 1.5264 1.3452 1.7164 -0.0316 -0.0208 -0.1475 368  ILE F N   
18249 C  CA  . ILE F 368  ? 1.4545 1.2594 1.6324 -0.0298 -0.0251 -0.1531 368  ILE F CA  
18250 C  C   . ILE F 368  ? 1.4200 1.2000 1.5782 -0.0246 -0.0195 -0.1492 368  ILE F C   
18251 O  O   . ILE F 368  ? 1.4151 1.1844 1.5588 -0.0182 -0.0229 -0.1513 368  ILE F O   
18252 C  CB  . ILE F 368  ? 1.4752 1.2776 1.6634 -0.0414 -0.0270 -0.1614 368  ILE F CB  
18253 C  CG1 . ILE F 368  ? 1.5643 1.3547 1.7408 -0.0392 -0.0327 -0.1679 368  ILE F CG1 
18254 C  CG2 . ILE F 368  ? 1.4652 1.2529 1.6569 -0.0512 -0.0179 -0.1601 368  ILE F CG2 
18255 C  CD1 . ILE F 368  ? 1.5232 1.3268 1.6950 -0.0293 -0.0412 -0.1692 368  ILE F CD1 
18256 N  N   . THR F 369  ? 1.3125 1.0829 1.4692 -0.0266 -0.0108 -0.1433 369  THR F N   
18257 C  CA  . THR F 369  ? 1.3875 1.1341 1.5250 -0.0211 -0.0053 -0.1393 369  THR F CA  
18258 C  C   . THR F 369  ? 1.3745 1.1248 1.4995 -0.0076 -0.0077 -0.1345 369  THR F C   
18259 O  O   . THR F 369  ? 1.3502 1.0830 1.4574 -0.0007 -0.0066 -0.1333 369  THR F O   
18260 C  CB  . THR F 369  ? 1.4334 1.1694 1.5724 -0.0264 0.0046  -0.1340 369  THR F CB  
18261 O  OG1 . THR F 369  ? 1.5036 1.2571 1.6514 -0.0240 0.0063  -0.1282 369  THR F OG1 
18262 C  CG2 . THR F 369  ? 1.5671 1.2992 1.7189 -0.0403 0.0074  -0.1391 369  THR F CG2 
18263 N  N   . ASP F 370  ? 1.9025 1.6753 2.0362 -0.0037 -0.0109 -0.1318 370  ASP F N   
18264 C  CA  . ASP F 370  ? 1.8854 1.6635 2.0087 0.0086  -0.0135 -0.1277 370  ASP F CA  
18265 C  C   . ASP F 370  ? 1.8190 1.5953 1.9330 0.0145  -0.0206 -0.1326 370  ASP F C   
18266 O  O   . ASP F 370  ? 1.8390 1.6121 1.9398 0.0248  -0.0216 -0.1300 370  ASP F O   
18267 C  CB  . ASP F 370  ? 1.9087 1.7111 2.0442 0.0104  -0.0154 -0.1244 370  ASP F CB  
18268 C  CG  . ASP F 370  ? 1.8935 1.6972 2.0358 0.0066  -0.0081 -0.1185 370  ASP F CG  
18269 O  OD1 . ASP F 370  ? 1.7741 1.5590 1.9085 0.0049  -0.0013 -0.1159 370  ASP F OD1 
18270 O  OD2 . ASP F 370  ? 1.9542 1.7770 2.1088 0.0057  -0.0090 -0.1165 370  ASP F OD2 
18271 N  N   . VAL F 371  ? 1.3265 1.1054 1.4472 0.0084  -0.0255 -0.1399 371  VAL F N   
18272 C  CA  . VAL F 371  ? 1.3241 1.0983 1.4348 0.0134  -0.0318 -0.1451 371  VAL F CA  
18273 C  C   . VAL F 371  ? 1.2933 1.0412 1.3910 0.0113  -0.0289 -0.1481 371  VAL F C   
18274 O  O   . VAL F 371  ? 1.3126 1.0504 1.3959 0.0184  -0.0318 -0.1500 371  VAL F O   
18275 C  CB  . VAL F 371  ? 1.2475 1.0391 1.3713 0.0089  -0.0394 -0.1517 371  VAL F CB  
18276 C  CG1 . VAL F 371  ? 1.2148 1.0021 1.3278 0.0145  -0.0461 -0.1571 371  VAL F CG1 
18277 C  CG2 . VAL F 371  ? 1.2571 1.0736 1.3931 0.0110  -0.0417 -0.1485 371  VAL F CG2 
18278 N  N   . ALA F 372  ? 1.1551 0.8910 1.2571 0.0019  -0.0229 -0.1483 372  ALA F N   
18279 C  CA  . ALA F 372  ? 1.2259 0.9358 1.3161 -0.0013 -0.0199 -0.1514 372  ALA F CA  
18280 C  C   . ALA F 372  ? 1.2353 0.9262 1.3057 0.0081  -0.0150 -0.1459 372  ALA F C   
18281 O  O   . ALA F 372  ? 1.2510 0.9257 1.3060 0.0132  -0.0165 -0.1485 372  ALA F O   
18282 C  CB  . ALA F 372  ? 1.3482 1.0513 1.4493 -0.0145 -0.0142 -0.1529 372  ALA F CB  
18283 N  N   . ALA F 373  ? 1.5801 1.2727 1.6503 0.0109  -0.0093 -0.1385 373  ALA F N   
18284 C  CA  . ALA F 373  ? 1.5890 1.2630 1.6406 0.0194  -0.0042 -0.1331 373  ALA F CA  
18285 C  C   . ALA F 373  ? 1.6182 1.2926 1.6558 0.0324  -0.0090 -0.1329 373  ALA F C   
18286 O  O   . ALA F 373  ? 1.6201 1.2734 1.6403 0.0378  -0.0069 -0.1327 373  ALA F O   
18287 C  CB  . ALA F 373  ? 1.5678 1.2468 1.6231 0.0204  0.0020  -0.1254 373  ALA F CB  
18288 N  N   . PRO F 374  ? 1.6353 1.3319 1.6788 0.0380  -0.0151 -0.1327 374  PRO F N   
18289 C  CA  . PRO F 374  ? 1.5808 1.2769 1.6107 0.0501  -0.0192 -0.1327 374  PRO F CA  
18290 C  C   . PRO F 374  ? 1.6818 1.3638 1.7018 0.0505  -0.0228 -0.1393 374  PRO F C   
18291 O  O   . PRO F 374  ? 1.7049 1.3709 1.7076 0.0587  -0.0219 -0.1387 374  PRO F O   
18292 C  CB  . PRO F 374  ? 1.5093 1.2330 1.5506 0.0531  -0.0248 -0.1321 374  PRO F CB  
18293 C  CG  . PRO F 374  ? 1.5177 1.2543 1.5778 0.0419  -0.0255 -0.1344 374  PRO F CG  
18294 C  CD  . PRO F 374  ? 1.5712 1.2937 1.6329 0.0344  -0.0179 -0.1320 374  PRO F CD  
18295 N  N   . ILE F 375  ? 1.5192 1.2066 1.5495 0.0421  -0.0271 -0.1459 375  ILE F N   
18296 C  CA  . ILE F 375  ? 1.4387 1.1125 1.4599 0.0419  -0.0308 -0.1528 375  ILE F CA  
18297 C  C   . ILE F 375  ? 1.4439 1.0891 1.4536 0.0382  -0.0248 -0.1534 375  ILE F C   
18298 O  O   . ILE F 375  ? 1.4654 1.0927 1.4591 0.0432  -0.0255 -0.1560 375  ILE F O   
18299 C  CB  . ILE F 375  ? 1.4723 1.1597 1.5081 0.0334  -0.0370 -0.1599 375  ILE F CB  
18300 C  CG1 . ILE F 375  ? 1.4282 1.1430 1.4743 0.0377  -0.0426 -0.1588 375  ILE F CG1 
18301 C  CG2 . ILE F 375  ? 1.4558 1.1291 1.4816 0.0334  -0.0413 -0.1673 375  ILE F CG2 
18302 C  CD1 . ILE F 375  ? 1.3650 1.0831 1.3985 0.0507  -0.0460 -0.1572 375  ILE F CD1 
18303 N  N   . GLY F 376  ? 1.1080 0.7477 1.1250 0.0294  -0.0184 -0.1509 376  GLY F N   
18304 C  CA  . GLY F 376  ? 1.1697 0.7816 1.1763 0.0248  -0.0120 -0.1515 376  GLY F CA  
18305 C  C   . GLY F 376  ? 1.1599 0.7528 1.1456 0.0359  -0.0077 -0.1464 376  GLY F C   
18306 O  O   . GLY F 376  ? 1.2372 0.8054 1.2079 0.0367  -0.0053 -0.1485 376  GLY F O   
18307 N  N   . LEU F 377  ? 1.3992 1.0034 1.3834 0.0447  -0.0067 -0.1397 377  LEU F N   
18308 C  CA  . LEU F 377  ? 1.3765 0.9650 1.3416 0.0560  -0.0030 -0.1347 377  LEU F CA  
18309 C  C   . LEU F 377  ? 1.4281 1.0181 1.3810 0.0680  -0.0087 -0.1365 377  LEU F C   
18310 O  O   . LEU F 377  ? 1.4604 1.0305 1.3948 0.0759  -0.0065 -0.1355 377  LEU F O   
18311 C  CB  . LEU F 377  ? 1.3834 0.9825 1.3520 0.0600  0.0009  -0.1268 377  LEU F CB  
18312 C  CG  . LEU F 377  ? 1.3094 0.9015 1.2850 0.0504  0.0085  -0.1236 377  LEU F CG  
18313 C  CD1 . LEU F 377  ? 1.2175 0.8191 1.1944 0.0558  0.0120  -0.1158 377  LEU F CD1 
18314 C  CD2 . LEU F 377  ? 1.4083 0.9689 1.3694 0.0477  0.0147  -0.1243 377  LEU F CD2 
18315 N  N   . ILE F 378  ? 1.5895 1.2023 1.5519 0.0699  -0.0158 -0.1391 378  ILE F N   
18316 C  CA  . ILE F 378  ? 1.5549 1.1692 1.5061 0.0809  -0.0210 -0.1412 378  ILE F CA  
18317 C  C   . ILE F 378  ? 1.6187 1.2135 1.5598 0.0788  -0.0229 -0.1480 378  ILE F C   
18318 O  O   . ILE F 378  ? 1.6465 1.2319 1.5723 0.0884  -0.0248 -0.1493 378  ILE F O   
18319 C  CB  . ILE F 378  ? 1.4147 1.0577 1.3784 0.0831  -0.0276 -0.1421 378  ILE F CB  
18320 C  CG1 . ILE F 378  ? 1.4470 1.0932 1.3984 0.0964  -0.0313 -0.1419 378  ILE F CG1 
18321 C  CG2 . ILE F 378  ? 1.3697 1.0207 1.3456 0.0735  -0.0327 -0.1490 378  ILE F CG2 
18322 C  CD1 . ILE F 378  ? 1.3229 0.9967 1.2849 0.1002  -0.0362 -0.1409 378  ILE F CD1 
18323 N  N   . GLY F 379  ? 1.6403 1.2288 1.5897 0.0662  -0.0224 -0.1527 379  GLY F N   
18324 C  CA  . GLY F 379  ? 1.6251 1.1931 1.5646 0.0633  -0.0237 -0.1594 379  GLY F CA  
18325 C  C   . GLY F 379  ? 1.6340 1.1723 1.5534 0.0679  -0.0175 -0.1571 379  GLY F C   
18326 O  O   . GLY F 379  ? 1.8022 1.3245 1.7061 0.0736  -0.0192 -0.1606 379  GLY F O   
18327 N  N   . LEU F 380  ? 1.2588 0.7890 1.1776 0.0660  -0.0101 -0.1512 380  LEU F N   
18328 C  CA  . LEU F 380  ? 1.3170 0.8195 1.2155 0.0719  -0.0039 -0.1480 380  LEU F CA  
18329 C  C   . LEU F 380  ? 1.3310 0.8351 1.2150 0.0882  -0.0057 -0.1444 380  LEU F C   
18330 O  O   . LEU F 380  ? 1.4608 0.9428 1.3254 0.0958  -0.0039 -0.1447 380  LEU F O   
18331 C  CB  . LEU F 380  ? 1.1831 0.6782 1.0847 0.0666  0.0043  -0.1422 380  LEU F CB  
18332 C  CG  . LEU F 380  ? 1.1882 0.6726 1.0989 0.0509  0.0086  -0.1453 380  LEU F CG  
18333 C  CD1 . LEU F 380  ? 1.2409 0.7161 1.1512 0.0479  0.0175  -0.1385 380  LEU F CD1 
18334 C  CD2 . LEU F 380  ? 1.4893 0.9472 1.3870 0.0477  0.0090  -0.1514 380  LEU F CD2 
18335 N  N   . VAL F 381  ? 1.1987 0.7288 1.0920 0.0939  -0.0091 -0.1412 381  VAL F N   
18336 C  CA  . VAL F 381  ? 1.2524 0.7869 1.1339 0.1090  -0.0110 -0.1380 381  VAL F CA  
18337 C  C   . VAL F 381  ? 1.2755 0.8073 1.1481 0.1150  -0.0168 -0.1437 381  VAL F C   
18338 O  O   . VAL F 381  ? 1.4046 0.9238 1.2597 0.1263  -0.0164 -0.1429 381  VAL F O   
18339 C  CB  . VAL F 381  ? 1.2028 0.7664 1.0977 0.1122  -0.0131 -0.1334 381  VAL F CB  
18340 C  CG1 . VAL F 381  ? 1.1638 0.7352 1.0487 0.1271  -0.0160 -0.1313 381  VAL F CG1 
18341 C  CG2 . VAL F 381  ? 1.1785 0.7420 1.0786 0.1085  -0.0069 -0.1272 381  VAL F CG2 
18342 N  N   . ILE F 382  ? 1.4301 0.9734 1.3140 0.1078  -0.0223 -0.1497 382  ILE F N   
18343 C  CA  . ILE F 382  ? 1.5041 1.0454 1.3797 0.1132  -0.0280 -0.1554 382  ILE F CA  
18344 C  C   . ILE F 382  ? 1.5468 1.0568 1.4054 0.1125  -0.0255 -0.1593 382  ILE F C   
18345 O  O   . ILE F 382  ? 1.5781 1.0775 1.4208 0.1224  -0.0273 -0.1611 382  ILE F O   
18346 C  CB  . ILE F 382  ? 1.4851 1.0464 1.3771 0.1055  -0.0345 -0.1609 382  ILE F CB  
18347 C  CG1 . ILE F 382  ? 1.4114 1.0028 1.3180 0.1078  -0.0370 -0.1569 382  ILE F CG1 
18348 C  CG2 . ILE F 382  ? 1.3695 0.9261 1.2519 0.1104  -0.0402 -0.1673 382  ILE F CG2 
18349 C  CD1 . ILE F 382  ? 1.4201 1.0187 1.3178 0.1219  -0.0369 -0.1520 382  ILE F CD1 
18350 N  N   . ALA F 383  ? 1.2882 0.7827 1.1497 0.1009  -0.0211 -0.1605 383  ALA F N   
18351 C  CA  . ALA F 383  ? 1.3154 0.7787 1.1609 0.0991  -0.0182 -0.1643 383  ALA F CA  
18352 C  C   . ALA F 383  ? 1.3617 0.8049 1.1860 0.1113  -0.0133 -0.1593 383  ALA F C   
18353 O  O   . ALA F 383  ? 1.6187 1.0427 1.4253 0.1181  -0.0138 -0.1622 383  ALA F O   
18354 C  CB  . ALA F 383  ? 1.3290 0.7811 1.1833 0.0836  -0.0137 -0.1660 383  ALA F CB  
18355 N  N   . LEU F 384  ? 1.4598 0.9069 1.2851 0.1147  -0.0085 -0.1519 384  LEU F N   
18356 C  CA  . LEU F 384  ? 1.5590 0.9892 1.3646 0.1273  -0.0042 -0.1469 384  LEU F CA  
18357 C  C   . LEU F 384  ? 1.6256 1.0670 1.4231 0.1422  -0.0091 -0.1466 384  LEU F C   
18358 O  O   . LEU F 384  ? 1.6451 1.0683 1.4229 0.1531  -0.0076 -0.1458 384  LEU F O   
18359 C  CB  . LEU F 384  ? 1.5307 0.9643 1.3402 0.1272  0.0016  -0.1392 384  LEU F CB  
18360 C  CG  . LEU F 384  ? 1.6479 1.0683 1.4636 0.1135  0.0080  -0.1385 384  LEU F CG  
18361 C  CD1 . LEU F 384  ? 1.7562 1.1831 1.5761 0.1148  0.0131  -0.1307 384  LEU F CD1 
18362 C  CD2 . LEU F 384  ? 1.5732 0.9581 1.3705 0.1119  0.0129  -0.1408 384  LEU F CD2 
18363 N  N   . PHE F 385  ? 1.7180 1.1888 1.5302 0.1431  -0.0149 -0.1471 385  PHE F N   
18364 C  CA  . PHE F 385  ? 1.7361 1.2189 1.5419 0.1564  -0.0195 -0.1473 385  PHE F CA  
18365 C  C   . PHE F 385  ? 1.8473 1.3162 1.6409 0.1593  -0.0230 -0.1540 385  PHE F C   
18366 O  O   . PHE F 385  ? 1.9146 1.3770 1.6929 0.1721  -0.0239 -0.1538 385  PHE F O   
18367 C  CB  . PHE F 385  ? 1.6412 1.1577 1.4659 0.1553  -0.0244 -0.1465 385  PHE F CB  
18368 C  CG  . PHE F 385  ? 1.6597 1.1897 1.4806 0.1659  -0.0299 -0.1486 385  PHE F CG  
18369 C  CD1 . PHE F 385  ? 1.5748 1.1121 1.3883 0.1793  -0.0295 -0.1442 385  PHE F CD1 
18370 C  CD2 . PHE F 385  ? 1.6885 1.2244 1.5134 0.1624  -0.0355 -0.1551 385  PHE F CD2 
18371 C  CE1 . PHE F 385  ? 1.5922 1.1424 1.4028 0.1888  -0.0341 -0.1461 385  PHE F CE1 
18372 C  CE2 . PHE F 385  ? 1.6442 1.1921 1.4653 0.1722  -0.0402 -0.1568 385  PHE F CE2 
18373 C  CZ  . PHE F 385  ? 1.6297 1.1848 1.4438 0.1853  -0.0392 -0.1523 385  PHE F CZ  
18374 N  N   . ALA F 386  ? 2.0498 1.5141 1.8501 0.1476  -0.0252 -0.1602 386  ALA F N   
18375 C  CA  . ALA F 386  ? 2.0467 1.4972 1.8354 0.1495  -0.0288 -0.1671 386  ALA F CA  
18376 C  C   . ALA F 386  ? 2.1151 1.5314 1.8819 0.1536  -0.0239 -0.1673 386  ALA F C   
18377 O  O   . ALA F 386  ? 2.2422 1.6462 1.9932 0.1624  -0.0258 -0.1705 386  ALA F O   
18378 C  CB  . ALA F 386  ? 2.0900 1.5451 1.8922 0.1355  -0.0327 -0.1739 386  ALA F CB  
18379 N  N   . ALA F 387  ? 1.6053 1.0053 1.3704 0.1474  -0.0172 -0.1640 387  ALA F N   
18380 C  CA  . ALA F 387  ? 1.5866 0.9529 1.3300 0.1516  -0.0118 -0.1636 387  ALA F CA  
18381 C  C   . ALA F 387  ? 1.6401 1.0032 1.3673 0.1690  -0.0103 -0.1583 387  ALA F C   
18382 O  O   . ALA F 387  ? 1.6634 1.0043 1.3702 0.1777  -0.0093 -0.1598 387  ALA F O   
18383 C  CB  . ALA F 387  ? 1.5623 0.9127 1.3082 0.1405  -0.0046 -0.1610 387  ALA F CB  
18384 N  N   . ASN F 388  ? 2.1276 1.5129 1.8637 0.1743  -0.0102 -0.1523 388  ASN F N   
18385 C  CA  . ASN F 388  ? 2.1417 1.5265 1.8641 0.1906  -0.0090 -0.1473 388  ASN F CA  
18386 C  C   . ASN F 388  ? 2.1153 1.5113 1.8325 0.2020  -0.0149 -0.1504 388  ASN F C   
18387 O  O   . ASN F 388  ? 2.1620 1.5485 1.8623 0.2159  -0.0140 -0.1487 388  ASN F O   
18388 C  CB  . ASN F 388  ? 2.0530 1.4589 1.7872 0.1923  -0.0074 -0.1404 388  ASN F CB  
18389 C  CG  . ASN F 388  ? 2.1528 1.5435 1.8865 0.1851  -0.0004 -0.1360 388  ASN F CG  
18390 O  OD1 . ASN F 388  ? 2.2622 1.6251 1.9853 0.1798  0.0039  -0.1378 388  ASN F OD1 
18391 N  ND2 . ASN F 388  ? 2.1417 1.5501 1.8865 0.1849  0.0011  -0.1304 388  ASN F ND2 
18392 N  N   . VAL F 389  ? 2.2546 1.6706 1.9857 0.1966  -0.0208 -0.1549 389  VAL F N   
18393 C  CA  . VAL F 389  ? 2.2511 1.6779 1.9774 0.2071  -0.0261 -0.1578 389  VAL F CA  
18394 C  C   . VAL F 389  ? 2.3097 1.7118 2.0194 0.2086  -0.0271 -0.1641 389  VAL F C   
18395 O  O   . VAL F 389  ? 2.2694 1.6702 1.9670 0.2207  -0.0295 -0.1657 389  VAL F O   
18396 C  CB  . VAL F 389  ? 2.2224 1.6810 1.9691 0.2020  -0.0318 -0.1596 389  VAL F CB  
18397 C  CG1 . VAL F 389  ? 2.2038 1.6596 1.9593 0.1883  -0.0347 -0.1662 389  VAL F CG1 
18398 C  CG2 . VAL F 389  ? 2.2347 1.7088 1.9774 0.2149  -0.0360 -0.1603 389  VAL F CG2 
18399 N  N   . GLN F 390  ? 1.9557 1.3377 1.6645 0.1965  -0.0253 -0.1680 390  GLN F N   
18400 C  CA  . GLN F 390  ? 1.9173 1.2719 1.6086 0.1976  -0.0255 -0.1738 390  GLN F CA  
18401 C  C   . GLN F 390  ? 1.8287 1.1535 1.4974 0.2064  -0.0195 -0.1707 390  GLN F C   
18402 O  O   . GLN F 390  ? 1.7203 1.0218 1.3712 0.2108  -0.0194 -0.1748 390  GLN F O   
18403 C  CB  . GLN F 390  ? 1.9369 1.2816 1.6362 0.1807  -0.0260 -0.1797 390  GLN F CB  
18404 C  CG  . GLN F 390  ? 1.9411 1.3079 1.6562 0.1739  -0.0332 -0.1853 390  GLN F CG  
18405 C  CD  . GLN F 390  ? 2.0528 1.4149 1.7802 0.1562  -0.0335 -0.1902 390  GLN F CD  
18406 O  OE1 . GLN F 390  ? 2.0981 1.4442 1.8255 0.1479  -0.0279 -0.1885 390  GLN F OE1 
18407 N  NE2 . GLN F 390  ? 2.0854 1.4616 1.8233 0.1504  -0.0401 -0.1964 390  GLN F NE2 
18408 N  N   . GLN F 391  ? 2.4331 1.7579 2.1017 0.2093  -0.0145 -0.1636 391  GLN F N   
18409 C  CA  . GLN F 391  ? 2.4577 1.7575 2.1061 0.2175  -0.0085 -0.1595 391  GLN F CA  
18410 C  C   . GLN F 391  ? 2.4515 1.7596 2.0888 0.2325  -0.0103 -0.1572 391  GLN F C   
18411 O  O   . GLN F 391  ? 2.5046 1.7949 2.1261 0.2363  -0.0079 -0.1568 391  GLN F O   
18412 C  CB  . GLN F 391  ? 2.3725 1.6742 2.0245 0.2176  -0.0034 -0.1522 391  GLN F CB  
18413 C  CG  . GLN F 391  ? 2.3320 1.6100 1.9824 0.2053  0.0030  -0.1515 391  GLN F CG  
18414 C  CD  . GLN F 391  ? 2.3936 1.6743 2.0468 0.2064  0.0082  -0.1439 391  GLN F CD  
18415 O  OE1 . GLN F 391  ? 2.3970 1.6791 2.0406 0.2173  0.0107  -0.1376 391  GLN F OE1 
18416 N  NE2 . GLN F 391  ? 2.4677 1.7592 2.1394 0.1926  0.0098  -0.1427 391  GLN F NE2 
18417 N  N   . ALA F 392  ? 1.8534 1.1884 1.4988 0.2411  -0.0145 -0.1557 392  ALA F N   
18418 C  CA  . ALA F 392  ? 1.7352 1.0820 1.3724 0.2554  -0.0161 -0.1529 392  ALA F CA  
18419 C  C   . ALA F 392  ? 1.6506 1.0170 1.2947 0.2586  -0.0227 -0.1579 392  ALA F C   
18420 O  O   . ALA F 392  ? 1.5733 0.9508 1.2314 0.2515  -0.0264 -0.1620 392  ALA F O   
18421 C  CB  . ALA F 392  ? 1.7389 1.1018 1.3790 0.2640  -0.0141 -0.1452 392  ALA F CB  
18422 N  N   . PRO F 393  ? 1.9769 1.3479 1.6113 0.2692  -0.0244 -0.1578 393  PRO F N   
18423 C  CA  . PRO F 393  ? 1.9314 1.3223 1.5721 0.2730  -0.0302 -0.1619 393  PRO F CA  
18424 C  C   . PRO F 393  ? 1.8686 1.2897 1.5240 0.2777  -0.0324 -0.1587 393  PRO F C   
18425 O  O   . PRO F 393  ? 1.8799 1.3086 1.5374 0.2820  -0.0295 -0.1525 393  PRO F O   
18426 C  CB  . PRO F 393  ? 1.9734 1.3594 1.5983 0.2838  -0.0301 -0.1612 393  PRO F CB  
18427 C  CG  . PRO F 393  ? 1.9999 1.3748 1.6141 0.2892  -0.0248 -0.1546 393  PRO F CG  
18428 C  CD  . PRO F 393  ? 2.0777 1.4346 1.6943 0.2779  -0.0210 -0.1541 393  PRO F CD  
18429 N  N   . LEU F 394  ? 1.9969 1.4353 1.6622 0.2768  -0.0375 -0.1632 394  LEU F N   
18430 C  CA  . LEU F 394  ? 1.9590 1.4269 1.6390 0.2805  -0.0398 -0.1610 394  LEU F CA  
18431 C  C   . LEU F 394  ? 2.0628 1.5479 1.7385 0.2935  -0.0406 -0.1580 394  LEU F C   
18432 O  O   . LEU F 394  ? 2.1980 1.6740 1.8606 0.2990  -0.0407 -0.1593 394  LEU F O   
18433 C  CB  . LEU F 394  ? 1.9063 1.3900 1.6021 0.2709  -0.0446 -0.1656 394  LEU F CB  
18434 C  CG  . LEU F 394  ? 2.0046 1.4833 1.7123 0.2537  -0.0443 -0.1671 394  LEU F CG  
18435 C  CD1 . LEU F 394  ? 2.0039 1.4568 1.7011 0.2475  -0.0451 -0.1736 394  LEU F CD1 
18436 C  CD2 . LEU F 394  ? 1.9950 1.5032 1.7246 0.2455  -0.0480 -0.1673 394  LEU F CD2 
18437 N  N   . LEU F 395  ? 2.4046 1.9150 2.0917 0.2981  -0.0411 -0.1541 395  LEU F N   
18438 C  CA  . LEU F 395  ? 2.4502 1.9815 2.1367 0.3094  -0.0420 -0.1512 395  LEU F CA  
18439 C  C   . LEU F 395  ? 2.5233 2.0434 2.1942 0.3180  -0.0387 -0.1470 395  LEU F C   
18440 O  O   . LEU F 395  ? 2.6465 2.1526 2.3040 0.3213  -0.0388 -0.1492 395  LEU F O   
18441 C  CB  . LEU F 395  ? 2.4012 1.9416 2.0881 0.3114  -0.0460 -0.1562 395  LEU F CB  
18442 C  CG  . LEU F 395  ? 2.3829 1.9443 2.0862 0.3070  -0.0498 -0.1593 395  LEU F CG  
18443 C  CD1 . LEU F 395  ? 2.3566 1.9067 2.0665 0.2939  -0.0513 -0.1636 395  LEU F CD1 
18444 C  CD2 . LEU F 395  ? 2.4305 2.0042 2.1321 0.3125  -0.0528 -0.1623 395  LEU F CD2 
18445 N  N   . PRO F 396  ? 1.8058 1.3318 1.4777 0.3221  -0.0360 -0.1410 396  PRO F N   
18446 C  CA  . PRO F 396  ? 1.8569 1.3729 1.5137 0.3308  -0.0333 -0.1370 396  PRO F CA  
18447 C  C   . PRO F 396  ? 1.9105 1.4404 1.5623 0.3414  -0.0352 -0.1370 396  PRO F C   
18448 O  O   . PRO F 396  ? 1.8512 1.4070 1.5124 0.3468  -0.0365 -0.1347 396  PRO F O   
18449 C  CB  . PRO F 396  ? 1.8998 1.4249 1.5621 0.3325  -0.0309 -0.1310 396  PRO F CB  
18450 C  CG  . PRO F 396  ? 1.8519 1.4012 1.5335 0.3283  -0.0333 -0.1315 396  PRO F CG  
18451 C  CD  . PRO F 396  ? 1.7203 1.2624 1.4069 0.3191  -0.0355 -0.1377 396  PRO F CD  
18452 N  N   . LEU F 397  ? 1.7339 1.2465 1.3711 0.3442  -0.0352 -0.1397 397  LEU F N   
18453 C  CA  . LEU F 397  ? 1.6658 1.1901 1.2976 0.3540  -0.0369 -0.1401 397  LEU F CA  
18454 C  C   . LEU F 397  ? 1.6266 1.1627 1.2548 0.3646  -0.0355 -0.1344 397  LEU F C   
18455 O  O   . LEU F 397  ? 1.6263 1.1851 1.2592 0.3716  -0.0372 -0.1335 397  LEU F O   
18456 C  CB  . LEU F 397  ? 1.7369 1.2378 1.3524 0.3549  -0.0369 -0.1438 397  LEU F CB  
18457 C  CG  . LEU F 397  ? 1.6466 1.1413 1.2646 0.3474  -0.0398 -0.1505 397  LEU F CG  
18458 C  CD1 . LEU F 397  ? 1.4977 0.9752 1.1198 0.3348  -0.0390 -0.1531 397  LEU F CD1 
18459 C  CD2 . LEU F 397  ? 1.6586 1.1379 1.2604 0.3520  -0.0403 -0.1536 397  LEU F CD2 
18460 N  N   . ARG F 398  ? 1.7205 1.2415 1.3401 0.3656  -0.0324 -0.1306 398  ARG F N   
18461 C  CA  . ARG F 398  ? 1.8600 1.3908 1.4753 0.3755  -0.0313 -0.1253 398  ARG F CA  
18462 C  C   . ARG F 398  ? 1.9227 1.4751 1.5541 0.3733  -0.0315 -0.1222 398  ARG F C   
18463 O  O   . ARG F 398  ? 1.9771 1.5208 1.6092 0.3692  -0.0292 -0.1194 398  ARG F O   
18464 C  CB  . ARG F 398  ? 2.0364 1.5407 1.6338 0.3781  -0.0279 -0.1227 398  ARG F CB  
18465 C  CG  . ARG F 398  ? 1.9520 1.4365 1.5320 0.3823  -0.0276 -0.1252 398  ARG F CG  
18466 C  CD  . ARG F 398  ? 1.9933 1.4520 1.5556 0.3851  -0.0240 -0.1222 398  ARG F CD  
18467 N  NE  . ARG F 398  ? 1.9934 1.4628 1.5543 0.3928  -0.0230 -0.1166 398  ARG F NE  
18468 C  CZ  . ARG F 398  ? 2.0080 1.4865 1.5609 0.4046  -0.0238 -0.1144 398  ARG F CZ  
18469 N  NH1 . ARG F 398  ? 2.0800 1.5582 1.6253 0.4105  -0.0253 -0.1170 398  ARG F NH1 
18470 N  NH2 . ARG F 398  ? 1.9796 1.4680 1.5322 0.4108  -0.0231 -0.1097 398  ARG F NH2 
18471 N  N   . ASP F 399  ? 2.3763 1.9569 2.0206 0.3758  -0.0340 -0.1226 399  ASP F N   
18472 C  CA  . ASP F 399  ? 2.3583 1.9621 2.0190 0.3739  -0.0346 -0.1199 399  ASP F CA  
18473 C  C   . ASP F 399  ? 2.3194 1.9528 1.9888 0.3805  -0.0368 -0.1197 399  ASP F C   
18474 O  O   . ASP F 399  ? 2.2957 1.9365 1.9683 0.3802  -0.0387 -0.1233 399  ASP F O   
18475 C  CB  . ASP F 399  ? 2.3096 1.9131 1.9833 0.3624  -0.0351 -0.1224 399  ASP F CB  
18476 C  CG  . ASP F 399  ? 2.3899 2.0040 2.0752 0.3589  -0.0342 -0.1187 399  ASP F CG  
18477 O  OD1 . ASP F 399  ? 2.3194 1.9543 2.0102 0.3647  -0.0346 -0.1154 399  ASP F OD1 
18478 O  OD2 . ASP F 399  ? 2.4725 2.0742 2.1614 0.3501  -0.0330 -0.1193 399  ASP F OD2 
18479 N  N   . PRO F 400  ? 1.8401 1.4908 1.5132 0.3864  -0.0367 -0.1158 400  PRO F N   
18480 C  CA  . PRO F 400  ? 1.7494 1.4291 1.4317 0.3920  -0.0386 -0.1157 400  PRO F CA  
18481 C  C   . PRO F 400  ? 1.7213 1.4208 1.4215 0.3853  -0.0402 -0.1180 400  PRO F C   
18482 O  O   . PRO F 400  ? 1.6631 1.3832 1.3696 0.3888  -0.0415 -0.1191 400  PRO F O   
18483 C  CB  . PRO F 400  ? 1.8024 1.4946 1.4863 0.3974  -0.0381 -0.1112 400  PRO F CB  
18484 C  CG  . PRO F 400  ? 1.9446 1.6184 1.6251 0.3923  -0.0362 -0.1089 400  PRO F CG  
18485 C  CD  . PRO F 400  ? 1.9249 1.5688 1.5928 0.3886  -0.0348 -0.1113 400  PRO F CD  
18486 N  N   . ASN F 401  ? 2.1924 1.8862 1.9007 0.3759  -0.0400 -0.1188 401  ASN F N   
18487 C  CA  . ASN F 401  ? 2.1580 1.8690 1.8825 0.3694  -0.0416 -0.1211 401  ASN F CA  
18488 C  C   . ASN F 401  ? 2.1951 1.8965 1.9167 0.3660  -0.0429 -0.1261 401  ASN F C   
18489 O  O   . ASN F 401  ? 2.2250 1.9404 1.9587 0.3614  -0.0445 -0.1284 401  ASN F O   
18490 C  CB  . ASN F 401  ? 2.1744 1.8846 1.9094 0.3610  -0.0410 -0.1198 401  ASN F CB  
18491 C  CG  . ASN F 401  ? 2.1539 1.8798 1.8955 0.3636  -0.0403 -0.1152 401  ASN F CG  
18492 O  OD1 . ASN F 401  ? 2.1272 1.8768 1.8758 0.3683  -0.0412 -0.1140 401  ASN F OD1 
18493 N  ND2 . ASN F 401  ? 2.0721 1.7848 1.8115 0.3604  -0.0386 -0.1127 401  ASN F ND2 
18494 N  N   . MET F 402  ? 1.8338 1.5115 1.5393 0.3682  -0.0424 -0.1279 402  MET F N   
18495 C  CA  . MET F 402  ? 1.7664 1.4342 1.4680 0.3652  -0.0440 -0.1330 402  MET F CA  
18496 C  C   . MET F 402  ? 1.6948 1.3828 1.3999 0.3704  -0.0455 -0.1346 402  MET F C   
18497 O  O   . MET F 402  ? 1.6611 1.3490 1.3684 0.3669  -0.0473 -0.1387 402  MET F O   
18498 C  CB  . MET F 402  ? 1.7928 1.4309 1.4756 0.3669  -0.0429 -0.1344 402  MET F CB  
18499 C  CG  . MET F 402  ? 1.7035 1.3242 1.3825 0.3601  -0.0443 -0.1399 402  MET F CG  
18500 S  SD  . MET F 402  ? 1.7460 1.3496 1.4306 0.3475  -0.0437 -0.1412 402  MET F SD  
18501 C  CE  . MET F 402  ? 1.8289 1.4195 1.5110 0.3408  -0.0466 -0.1487 402  MET F CE  
18502 N  N   . GLU F 403  ? 1.9177 1.6230 1.6234 0.3786  -0.0449 -0.1314 403  GLU F N   
18503 C  CA  . GLU F 403  ? 1.8795 1.6057 1.5898 0.3832  -0.0459 -0.1325 403  GLU F CA  
18504 C  C   . GLU F 403  ? 1.9355 1.6828 1.6636 0.3770  -0.0470 -0.1337 403  GLU F C   
18505 O  O   . GLU F 403  ? 2.1046 1.8644 1.8359 0.3784  -0.0479 -0.1357 403  GLU F O   
18506 C  CB  . GLU F 403  ? 1.9387 1.6803 1.6477 0.3924  -0.0450 -0.1289 403  GLU F CB  
18507 C  CG  . GLU F 403  ? 2.0733 1.7964 1.7637 0.4003  -0.0441 -0.1281 403  GLU F CG  
18508 C  CD  . GLU F 403  ? 2.0785 1.8178 1.7681 0.4095  -0.0435 -0.1248 403  GLU F CD  
18509 O  OE1 . GLU F 403  ? 2.0421 1.8063 1.7460 0.4090  -0.0437 -0.1230 403  GLU F OE1 
18510 O  OE2 . GLU F 403  ? 2.0733 1.8006 1.7479 0.4172  -0.0429 -0.1241 403  GLU F OE2 
18511 N  N   . GLN F 404  ? 1.5825 1.3335 1.3215 0.3703  -0.0469 -0.1322 404  GLN F N   
18512 C  CA  . GLN F 404  ? 1.6176 1.3871 1.3731 0.3640  -0.0479 -0.1332 404  GLN F CA  
18513 C  C   . GLN F 404  ? 1.6788 1.4378 1.4339 0.3580  -0.0497 -0.1381 404  GLN F C   
18514 O  O   . GLN F 404  ? 1.7257 1.5003 1.4927 0.3540  -0.0508 -0.1395 404  GLN F O   
18515 C  CB  . GLN F 404  ? 1.5550 1.3294 1.3212 0.3587  -0.0472 -0.1303 404  GLN F CB  
18516 C  CG  . GLN F 404  ? 1.5970 1.3887 1.3677 0.3638  -0.0460 -0.1258 404  GLN F CG  
18517 C  CD  . GLN F 404  ? 1.5213 1.3160 1.3012 0.3587  -0.0454 -0.1229 404  GLN F CD  
18518 O  OE1 . GLN F 404  ? 1.4721 1.2532 1.2535 0.3517  -0.0456 -0.1240 404  GLN F OE1 
18519 N  NE2 . GLN F 404  ? 1.5277 1.3405 1.3139 0.3620  -0.0448 -0.1194 404  GLN F NE2 
18520 N  N   . LEU F 405  ? 1.6047 1.3376 1.3462 0.3572  -0.0502 -0.1408 405  LEU F N   
18521 C  CA  . LEU F 405  ? 1.5462 1.2680 1.2859 0.3518  -0.0524 -0.1461 405  LEU F CA  
18522 C  C   . LEU F 405  ? 1.6397 1.3658 1.3730 0.3571  -0.0534 -0.1488 405  LEU F C   
18523 O  O   . LEU F 405  ? 1.6631 1.3865 1.3972 0.3531  -0.0556 -0.1532 405  LEU F O   
18524 C  CB  . LEU F 405  ? 1.6302 1.3214 1.3584 0.3475  -0.0524 -0.1483 405  LEU F CB  
18525 C  CG  . LEU F 405  ? 1.5894 1.2736 1.3252 0.3393  -0.0519 -0.1475 405  LEU F CG  
18526 C  CD1 . LEU F 405  ? 1.4981 1.1516 1.2225 0.3342  -0.0518 -0.1504 405  LEU F CD1 
18527 C  CD2 . LEU F 405  ? 1.6620 1.3626 1.4141 0.3327  -0.0539 -0.1494 405  LEU F CD2 
18528 N  N   . GLN F 406  ? 1.7830 1.5154 1.5096 0.3660  -0.0520 -0.1464 406  GLN F N   
18529 C  CA  . GLN F 406  ? 1.7833 1.5219 1.5043 0.3716  -0.0526 -0.1484 406  GLN F CA  
18530 C  C   . GLN F 406  ? 1.8392 1.6062 1.5741 0.3718  -0.0525 -0.1477 406  GLN F C   
18531 O  O   . GLN F 406  ? 1.8592 1.6321 1.5912 0.3750  -0.0530 -0.1498 406  GLN F O   
18532 C  CB  . GLN F 406  ? 1.7941 1.5284 1.5025 0.3813  -0.0510 -0.1462 406  GLN F CB  
18533 C  CG  . GLN F 406  ? 1.8609 1.5657 1.5514 0.3826  -0.0512 -0.1483 406  GLN F CG  
18534 C  CD  . GLN F 406  ? 1.8440 1.5470 1.5215 0.3924  -0.0505 -0.1483 406  GLN F CD  
18535 O  OE1 . GLN F 406  ? 1.7348 1.4536 1.4139 0.3995  -0.0492 -0.1449 406  GLN F OE1 
18536 N  NE2 . GLN F 406  ? 1.8503 1.5338 1.5149 0.3927  -0.0517 -0.1521 406  GLN F NE2 
18537 N  N   . LEU G 32   ? 1.3948 1.6319 1.3589 0.2582  0.0898  -0.0902 32   LEU G N   
18538 C  CA  . LEU G 32   ? 1.4874 1.7146 1.4382 0.2587  0.0946  -0.0878 32   LEU G CA  
18539 C  C   . LEU G 32   ? 1.4395 1.6594 1.3909 0.2508  0.0929  -0.0848 32   LEU G C   
18540 O  O   . LEU G 32   ? 1.3912 1.6190 1.3558 0.2429  0.0936  -0.0836 32   LEU G O   
18541 C  CB  . LEU G 32   ? 1.4310 1.6688 1.3829 0.2588  0.1064  -0.0865 32   LEU G CB  
18542 C  CG  . LEU G 32   ? 1.3902 1.6179 1.3272 0.2602  0.1128  -0.0838 32   LEU G CG  
18543 C  CD1 . LEU G 32   ? 1.3410 1.5533 1.2602 0.2693  0.1071  -0.0855 32   LEU G CD1 
18544 C  CD2 . LEU G 32   ? 1.1380 1.3773 1.0773 0.2604  0.1249  -0.0828 32   LEU G CD2 
18545 N  N   . SER G 33   ? 2.1317 2.3364 2.0685 0.2531  0.0906  -0.0837 33   SER G N   
18546 C  CA  . SER G 33   ? 2.0870 2.2838 2.0231 0.2467  0.0885  -0.0810 33   SER G CA  
18547 C  C   . SER G 33   ? 2.0059 2.2073 1.9445 0.2403  0.0986  -0.0772 33   SER G C   
18548 O  O   . SER G 33   ? 2.0004 2.2010 1.9449 0.2328  0.0983  -0.0749 33   SER G O   
18549 C  CB  . SER G 33   ? 2.0933 2.2731 2.0129 0.2517  0.0827  -0.0812 33   SER G CB  
18550 O  OG  . SER G 33   ? 2.0612 2.2361 1.9668 0.2571  0.0891  -0.0803 33   SER G OG  
18551 N  N   . ARG G 34   ? 1.7205 1.9262 1.6544 0.2432  0.1079  -0.0765 34   ARG G N   
18552 C  CA  . ARG G 34   ? 1.7599 1.9687 1.6949 0.2371  0.1183  -0.0730 34   ARG G CA  
18553 C  C   . ARG G 34   ? 1.7348 1.9578 1.6886 0.2279  0.1211  -0.0725 34   ARG G C   
18554 O  O   . ARG G 34   ? 1.7382 1.9594 1.6951 0.2203  0.1241  -0.0696 34   ARG G O   
18555 C  CB  . ARG G 34   ? 1.7924 2.0042 1.7196 0.2422  0.1280  -0.0727 34   ARG G CB  
18556 C  CG  . ARG G 34   ? 1.8563 2.0523 1.7632 0.2475  0.1300  -0.0708 34   ARG G CG  
18557 C  CD  . ARG G 34   ? 1.9626 2.1596 1.8599 0.2563  0.1349  -0.0722 34   ARG G CD  
18558 N  NE  . ARG G 34   ? 2.0154 2.1996 1.8944 0.2600  0.1404  -0.0696 34   ARG G NE  
18559 C  CZ  . ARG G 34   ? 1.9871 2.1733 1.8638 0.2568  0.1522  -0.0664 34   ARG G CZ  
18560 N  NH1 . ARG G 34   ? 1.9112 2.1123 1.8034 0.2494  0.1598  -0.0656 34   ARG G NH1 
18561 N  NH2 . ARG G 34   ? 2.0049 2.1777 1.8632 0.2611  0.1565  -0.0640 34   ARG G NH2 
18562 N  N   . LEU G 35   ? 1.5050 1.7419 1.4711 0.2287  0.1200  -0.0753 35   LEU G N   
18563 C  CA  . LEU G 35   ? 1.4231 1.6744 1.4073 0.2205  0.1222  -0.0754 35   LEU G CA  
18564 C  C   . LEU G 35   ? 1.4189 1.6658 1.4092 0.2153  0.1136  -0.0751 35   LEU G C   
18565 O  O   . LEU G 35   ? 1.3975 1.6495 1.3978 0.2067  0.1161  -0.0735 35   LEU G O   
18566 C  CB  . LEU G 35   ? 1.5088 1.7762 1.5039 0.2238  0.1226  -0.0788 35   LEU G CB  
18567 C  CG  . LEU G 35   ? 1.4750 1.7468 1.4635 0.2308  0.1298  -0.0797 35   LEU G CG  
18568 C  CD1 . LEU G 35   ? 1.4901 1.7785 1.4904 0.2344  0.1293  -0.0832 35   LEU G CD1 
18569 C  CD2 . LEU G 35   ? 1.2949 1.5695 1.2821 0.2260  0.1419  -0.0767 35   LEU G CD2 
18570 N  N   . MET G 36   ? 1.5670 1.8040 1.5513 0.2202  0.1037  -0.0766 36   MET G N   
18571 C  CA  . MET G 36   ? 1.5406 1.7730 1.5304 0.2157  0.0956  -0.0764 36   MET G CA  
18572 C  C   . MET G 36   ? 1.5523 1.7737 1.5359 0.2106  0.0968  -0.0729 36   MET G C   
18573 O  O   . MET G 36   ? 1.5920 1.8145 1.5840 0.2034  0.0951  -0.0716 36   MET G O   
18574 C  CB  . MET G 36   ? 1.5326 1.7569 1.5171 0.2223  0.0853  -0.0791 36   MET G CB  
18575 C  CG  . MET G 36   ? 1.5316 1.7662 1.5272 0.2239  0.0811  -0.0822 36   MET G CG  
18576 S  SD  . MET G 36   ? 1.7291 1.9519 1.7194 0.2294  0.0687  -0.0849 36   MET G SD  
18577 C  CE  . MET G 36   ? 1.7471 1.9821 1.7454 0.2347  0.0675  -0.0885 36   MET G CE  
18578 N  N   . ILE G 37   ? 1.4854 1.6958 1.4537 0.2146  0.0997  -0.0713 37   ILE G N   
18579 C  CA  . ILE G 37   ? 1.4769 1.6768 1.4382 0.2105  0.1017  -0.0678 37   ILE G CA  
18580 C  C   . ILE G 37   ? 1.4301 1.6377 1.3985 0.2026  0.1119  -0.0651 37   ILE G C   
18581 O  O   . ILE G 37   ? 1.5195 1.7232 1.4901 0.1960  0.1125  -0.0626 37   ILE G O   
18582 C  CB  . ILE G 37   ? 1.4559 1.6422 1.3982 0.2177  0.1022  -0.0670 37   ILE G CB  
18583 C  CG1 . ILE G 37   ? 1.4688 1.6461 1.4045 0.2239  0.0910  -0.0696 37   ILE G CG1 
18584 C  CG2 . ILE G 37   ? 1.4013 1.5778 1.3354 0.2140  0.1065  -0.0629 37   ILE G CG2 
18585 C  CD1 . ILE G 37   ? 1.4708 1.6423 1.4107 0.2196  0.0830  -0.0691 37   ILE G CD1 
18586 N  N   . ALA G 38   ? 0.9311 1.1496 0.9033 0.2031  0.1200  -0.0658 38   ALA G N   
18587 C  CA  . ALA G 38   ? 0.8548 1.0819 0.8351 0.1950  0.1299  -0.0638 38   ALA G CA  
18588 C  C   . ALA G 38   ? 0.8865 1.1235 0.8839 0.1870  0.1271  -0.0646 38   ALA G C   
18589 O  O   . ALA G 38   ? 0.8468 1.0828 0.8479 0.1790  0.1309  -0.0622 38   ALA G O   
18590 C  CB  . ALA G 38   ? 0.8338 1.0724 0.8162 0.1974  0.1387  -0.0650 38   ALA G CB  
18591 N  N   . GLY G 39   ? 1.7639 2.0099 1.7711 0.1892  0.1203  -0.0679 39   GLY G N   
18592 C  CA  . GLY G 39   ? 1.7431 1.9975 1.7653 0.1825  0.1166  -0.0687 39   GLY G CA  
18593 C  C   . GLY G 39   ? 1.6825 1.9251 1.7023 0.1790  0.1102  -0.0668 39   GLY G C   
18594 O  O   . GLY G 39   ? 1.6170 1.8636 1.6467 0.1715  0.1100  -0.0662 39   GLY G O   
18595 N  N   . LEU G 40   ? 1.3958 1.6239 1.4024 0.1844  0.1049  -0.0662 40   LEU G N   
18596 C  CA  . LEU G 40   ? 1.3396 1.5564 1.3433 0.1815  0.0991  -0.0644 40   LEU G CA  
18597 C  C   . LEU G 40   ? 1.2936 1.5045 1.2930 0.1756  0.1062  -0.0606 40   LEU G C   
18598 O  O   . LEU G 40   ? 1.2828 1.4927 1.2883 0.1689  0.1052  -0.0591 40   LEU G O   
18599 C  CB  . LEU G 40   ? 1.3924 1.5963 1.3835 0.1891  0.0915  -0.0651 40   LEU G CB  
18600 C  CG  . LEU G 40   ? 1.4326 1.6246 1.4192 0.1866  0.0866  -0.0629 40   LEU G CG  
18601 C  CD1 . LEU G 40   ? 1.5363 1.7330 1.5361 0.1809  0.0812  -0.0635 40   LEU G CD1 
18602 C  CD2 . LEU G 40   ? 1.4576 1.6374 1.4314 0.1940  0.0796  -0.0639 40   LEU G CD2 
18603 N  N   . MET G 41   ? 1.4185 1.6247 1.4068 0.1781  0.1138  -0.0588 41   MET G N   
18604 C  CA  . MET G 41   ? 1.3768 1.5762 1.3597 0.1727  0.1213  -0.0551 41   MET G CA  
18605 C  C   . MET G 41   ? 1.3516 1.5622 1.3485 0.1632  0.1276  -0.0546 41   MET G C   
18606 O  O   . MET G 41   ? 1.3379 1.5431 1.3346 0.1568  0.1304  -0.0520 41   MET G O   
18607 C  CB  . MET G 41   ? 1.4051 1.5984 1.3737 0.1775  0.1292  -0.0535 41   MET G CB  
18608 C  CG  . MET G 41   ? 1.5433 1.7246 1.4967 0.1870  0.1232  -0.0539 41   MET G CG  
18609 S  SD  . MET G 41   ? 1.7860 1.9564 1.7370 0.1880  0.1107  -0.0540 41   MET G SD  
18610 C  CE  . MET G 41   ? 1.6882 1.8438 1.6182 0.1984  0.1077  -0.0538 41   MET G CE  
18611 N  N   . VAL G 42   ? 1.1394 1.3657 1.1484 0.1623  0.1296  -0.0574 42   VAL G N   
18612 C  CA  . VAL G 42   ? 1.0863 1.3249 1.1099 0.1532  0.1345  -0.0578 42   VAL G CA  
18613 C  C   . VAL G 42   ? 1.1296 1.3685 1.1623 0.1486  0.1268  -0.0582 42   VAL G C   
18614 O  O   . VAL G 42   ? 1.0926 1.3317 1.1306 0.1405  0.1299  -0.0567 42   VAL G O   
18615 C  CB  . VAL G 42   ? 1.0958 1.3522 1.1304 0.1543  0.1377  -0.0611 42   VAL G CB  
18616 C  CG1 . VAL G 42   ? 1.0737 1.3444 1.1254 0.1453  0.1403  -0.0624 42   VAL G CG1 
18617 C  CG2 . VAL G 42   ? 0.9934 1.2502 1.0199 0.1572  0.1475  -0.0602 42   VAL G CG2 
18618 N  N   . PHE G 43   ? 1.2509 1.4891 1.2851 0.1537  0.1167  -0.0603 43   PHE G N   
18619 C  CA  . PHE G 43   ? 1.2139 1.4516 1.2558 0.1499  0.1093  -0.0606 43   PHE G CA  
18620 C  C   . PHE G 43   ? 1.1709 1.3937 1.2044 0.1473  0.1080  -0.0573 43   PHE G C   
18621 O  O   . PHE G 43   ? 1.1127 1.3354 1.1528 0.1409  0.1068  -0.0563 43   PHE G O   
18622 C  CB  . PHE G 43   ? 1.2342 1.4731 1.2781 0.1563  0.0994  -0.0634 43   PHE G CB  
18623 C  CG  . PHE G 43   ? 1.2270 1.4594 1.2733 0.1545  0.0910  -0.0631 43   PHE G CG  
18624 C  CD1 . PHE G 43   ? 1.2083 1.4476 1.2667 0.1478  0.0899  -0.0633 43   PHE G CD1 
18625 C  CD2 . PHE G 43   ? 1.2751 1.4948 1.3116 0.1595  0.0843  -0.0626 43   PHE G CD2 
18626 C  CE1 . PHE G 43   ? 1.2218 1.4550 1.2822 0.1462  0.0826  -0.0629 43   PHE G CE1 
18627 C  CE2 . PHE G 43   ? 1.2878 1.5021 1.3271 0.1577  0.0769  -0.0623 43   PHE G CE2 
18628 C  CZ  . PHE G 43   ? 1.2460 1.4669 1.2971 0.1511  0.0763  -0.0623 43   PHE G CZ  
18629 N  N   . LEU G 44   ? 1.1533 1.3633 1.1719 0.1527  0.1082  -0.0555 44   LEU G N   
18630 C  CA  . LEU G 44   ? 1.1040 1.2999 1.1134 0.1510  0.1076  -0.0522 44   LEU G CA  
18631 C  C   . LEU G 44   ? 1.0546 1.2495 1.0645 0.1433  0.1169  -0.0494 44   LEU G C   
18632 O  O   . LEU G 44   ? 1.1412 1.3301 1.1518 0.1384  0.1160  -0.0474 44   LEU G O   
18633 C  CB  . LEU G 44   ? 1.1133 1.2968 1.1062 0.1590  0.1061  -0.0512 44   LEU G CB  
18634 C  CG  . LEU G 44   ? 1.1252 1.2940 1.1080 0.1596  0.1030  -0.0484 44   LEU G CG  
18635 C  CD1 . LEU G 44   ? 1.1528 1.3206 1.1425 0.1584  0.0932  -0.0494 44   LEU G CD1 
18636 C  CD2 . LEU G 44   ? 1.1654 1.3236 1.1320 0.1681  0.1017  -0.0480 44   LEU G CD2 
18637 N  N   . VAL G 45   ? 1.2336 1.4339 1.2428 0.1420  0.1263  -0.0492 45   VAL G N   
18638 C  CA  . VAL G 45   ? 1.3037 1.5028 1.3133 0.1341  0.1360  -0.0466 45   VAL G CA  
18639 C  C   . VAL G 45   ? 1.2831 1.4927 1.3087 0.1255  0.1356  -0.0480 45   VAL G C   
18640 O  O   . VAL G 45   ? 1.2166 1.4204 1.2424 0.1191  0.1377  -0.0458 45   VAL G O   
18641 C  CB  . VAL G 45   ? 1.2515 1.4547 1.2574 0.1346  0.1464  -0.0464 45   VAL G CB  
18642 C  CG1 . VAL G 45   ? 1.0843 1.2891 1.0940 0.1251  0.1566  -0.0446 45   VAL G CG1 
18643 C  CG2 . VAL G 45   ? 1.1618 1.3515 1.1492 0.1426  0.1478  -0.0443 45   VAL G CG2 
18644 N  N   . LEU G 46   ? 1.0968 1.3217 1.1356 0.1255  0.1328  -0.0516 46   LEU G N   
18645 C  CA  . LEU G 46   ? 1.0267 1.2626 1.0809 0.1178  0.1319  -0.0533 46   LEU G CA  
18646 C  C   . LEU G 46   ? 1.0441 1.2721 1.0990 0.1158  0.1244  -0.0523 46   LEU G C   
18647 O  O   . LEU G 46   ? 1.0241 1.2528 1.0849 0.1080  0.1264  -0.0515 46   LEU G O   
18648 C  CB  . LEU G 46   ? 1.0835 1.3362 1.1500 0.1203  0.1284  -0.0575 46   LEU G CB  
18649 C  CG  . LEU G 46   ? 1.1061 1.3721 1.1888 0.1131  0.1275  -0.0598 46   LEU G CG  
18650 C  CD1 . LEU G 46   ? 1.0975 1.3675 1.1845 0.1039  0.1375  -0.0589 46   LEU G CD1 
18651 C  CD2 . LEU G 46   ? 1.0760 1.3582 1.1694 0.1170  0.1241  -0.0638 46   LEU G CD2 
18652 N  N   . SER G 47   ? 1.1551 1.3758 1.2043 0.1225  0.1157  -0.0523 47   SER G N   
18653 C  CA  . SER G 47   ? 1.0674 1.2812 1.1177 0.1212  0.1083  -0.0515 47   SER G CA  
18654 C  C   . SER G 47   ? 1.0270 1.2269 1.0679 0.1179  0.1117  -0.0476 47   SER G C   
18655 O  O   . SER G 47   ? 1.0901 1.2876 1.1353 0.1125  0.1102  -0.0467 47   SER G O   
18656 C  CB  . SER G 47   ? 1.0527 1.2618 1.0986 0.1292  0.0990  -0.0526 47   SER G CB  
18657 O  OG  . SER G 47   ? 1.1946 1.3916 1.2258 0.1345  0.0999  -0.0506 47   SER G OG  
18658 N  N   . LEU G 48   ? 0.8318 1.0217 0.8589 0.1217  0.1161  -0.0454 48   LEU G N   
18659 C  CA  . LEU G 48   ? 0.8418 1.0180 0.8588 0.1193  0.1200  -0.0415 48   LEU G CA  
18660 C  C   . LEU G 48   ? 0.8352 1.0141 0.8575 0.1099  0.1285  -0.0405 48   LEU G C   
18661 O  O   . LEU G 48   ? 0.7136 0.8836 0.7328 0.1057  0.1297  -0.0380 48   LEU G O   
18662 C  CB  . LEU G 48   ? 0.9188 1.0843 0.9194 0.1257  0.1236  -0.0395 48   LEU G CB  
18663 C  CG  . LEU G 48   ? 0.9310 1.0852 0.9207 0.1335  0.1157  -0.0387 48   LEU G CG  
18664 C  CD1 . LEU G 48   ? 0.7418 0.8856 0.7283 0.1309  0.1131  -0.0361 48   LEU G CD1 
18665 C  CD2 . LEU G 48   ? 1.0945 1.2556 1.0907 0.1384  0.1061  -0.0422 48   LEU G CD2 
18666 N  N   . VAL G 49   ? 1.1131 1.3045 1.1434 0.1065  0.1347  -0.0424 49   VAL G N   
18667 C  CA  . VAL G 49   ? 1.0638 1.2598 1.1014 0.0968  0.1424  -0.0422 49   VAL G CA  
18668 C  C   . VAL G 49   ? 1.0354 1.2375 1.0856 0.0913  0.1368  -0.0438 49   VAL G C   
18669 O  O   . VAL G 49   ? 1.0371 1.2349 1.0885 0.0842  0.1400  -0.0424 49   VAL G O   
18670 C  CB  . VAL G 49   ? 1.1435 1.3528 1.1876 0.0947  0.1500  -0.0443 49   VAL G CB  
18671 C  CG1 . VAL G 49   ? 1.0543 1.2710 1.1088 0.0840  0.1569  -0.0450 49   VAL G CG1 
18672 C  CG2 . VAL G 49   ? 1.1643 1.3655 1.1944 0.0991  0.1572  -0.0420 49   VAL G CG2 
18673 N  N   . VAL G 50   ? 0.8338 1.0454 0.8928 0.0948  0.1284  -0.0468 50   VAL G N   
18674 C  CA  . VAL G 50   ? 0.7720 0.9891 0.8423 0.0905  0.1227  -0.0484 50   VAL G CA  
18675 C  C   . VAL G 50   ? 0.7539 0.9569 0.8175 0.0906  0.1181  -0.0457 50   VAL G C   
18676 O  O   . VAL G 50   ? 0.6955 0.8975 0.7640 0.0843  0.1180  -0.0452 50   VAL G O   
18677 C  CB  . VAL G 50   ? 0.7601 0.9894 0.8399 0.0951  0.1149  -0.0520 50   VAL G CB  
18678 C  CG1 . VAL G 50   ? 0.7071 0.9389 0.7957 0.0922  0.1080  -0.0531 50   VAL G CG1 
18679 C  CG2 . VAL G 50   ? 0.7949 1.0402 0.8837 0.0939  0.1197  -0.0550 50   VAL G CG2 
18680 N  N   . LEU G 51   ? 0.7478 0.9400 0.8002 0.0978  0.1141  -0.0439 51   LEU G N   
18681 C  CA  . LEU G 51   ? 0.7799 0.9592 0.8258 0.0984  0.1098  -0.0413 51   LEU G CA  
18682 C  C   . LEU G 51   ? 0.7747 0.9437 0.8133 0.0931  0.1175  -0.0380 51   LEU G C   
18683 O  O   . LEU G 51   ? 0.7657 0.9284 0.8045 0.0896  0.1158  -0.0365 51   LEU G O   
18684 C  CB  . LEU G 51   ? 0.7013 0.8722 0.7367 0.1074  0.1043  -0.0405 51   LEU G CB  
18685 C  CG  . LEU G 51   ? 0.6231 0.8004 0.6645 0.1126  0.0951  -0.0435 51   LEU G CG  
18686 C  CD1 . LEU G 51   ? 0.8395 1.0097 0.8700 0.1212  0.0915  -0.0433 51   LEU G CD1 
18687 C  CD2 . LEU G 51   ? 0.8287 1.0049 0.8767 0.1105  0.0881  -0.0436 51   LEU G CD2 
18688 N  N   . LEU G 52   ? 0.8991 1.0656 0.9307 0.0924  0.1263  -0.0368 52   LEU G N   
18689 C  CA  . LEU G 52   ? 0.8777 1.0338 0.9019 0.0869  0.1345  -0.0336 52   LEU G CA  
18690 C  C   . LEU G 52   ? 0.9226 1.0861 0.9584 0.0770  0.1382  -0.0349 52   LEU G C   
18691 O  O   . LEU G 52   ? 0.9396 1.0941 0.9722 0.0720  0.1408  -0.0328 52   LEU G O   
18692 C  CB  . LEU G 52   ? 0.8884 1.0401 0.9022 0.0887  0.1434  -0.0320 52   LEU G CB  
18693 C  CG  . LEU G 52   ? 0.8164 0.9554 0.8202 0.0837  0.1529  -0.0284 52   LEU G CG  
18694 C  CD1 . LEU G 52   ? 0.7759 0.8986 0.7680 0.0871  0.1491  -0.0251 52   LEU G CD1 
18695 C  CD2 . LEU G 52   ? 0.8892 1.0250 0.8833 0.0855  0.1620  -0.0270 52   LEU G CD2 
18696 N  N   . ALA G 53   ? 1.2244 1.4042 1.2734 0.0742  0.1384  -0.0386 53   ALA G N   
18697 C  CA  . ALA G 53   ? 1.2076 1.3960 1.2685 0.0649  0.1413  -0.0405 53   ALA G CA  
18698 C  C   . ALA G 53   ? 1.2503 1.4380 1.3172 0.0631  0.1336  -0.0410 53   ALA G C   
18699 O  O   . ALA G 53   ? 1.1962 1.3850 1.2688 0.0553  0.1361  -0.0415 53   ALA G O   
18700 C  CB  . ALA G 53   ? 1.2497 1.4569 1.3236 0.0633  0.1427  -0.0446 53   ALA G CB  
18701 N  N   . GLY G 54   ? 1.3273 1.5127 1.3928 0.0700  0.1245  -0.0410 54   GLY G N   
18702 C  CA  . GLY G 54   ? 1.2820 1.4659 1.3524 0.0686  0.1175  -0.0412 54   GLY G CA  
18703 C  C   . GLY G 54   ? 1.2421 1.4105 1.3033 0.0664  0.1193  -0.0376 54   GLY G C   
18704 O  O   . GLY G 54   ? 1.2308 1.3982 1.2966 0.0610  0.1185  -0.0377 54   GLY G O   
18705 N  N   . ARG G 55   ? 0.9906 1.1463 1.0380 0.0710  0.1216  -0.0344 55   ARG G N   
18706 C  CA  . ARG G 55   ? 1.0426 1.1827 1.0794 0.0699  0.1240  -0.0307 55   ARG G CA  
18707 C  C   . ARG G 55   ? 1.0970 1.2307 1.1272 0.0643  0.1350  -0.0288 55   ARG G C   
18708 O  O   . ARG G 55   ? 1.0060 1.1249 1.0231 0.0657  0.1386  -0.0252 55   ARG G O   
18709 C  CB  . ARG G 55   ? 1.0063 1.1358 1.0314 0.0787  0.1195  -0.0283 55   ARG G CB  
18710 C  CG  . ARG G 55   ? 1.1656 1.2989 1.1962 0.0837  0.1088  -0.0298 55   ARG G CG  
18711 C  CD  . ARG G 55   ? 1.2379 1.3590 1.2608 0.0871  0.1045  -0.0271 55   ARG G CD  
18712 N  NE  . ARG G 55   ? 1.2958 1.4108 1.3190 0.0810  0.1073  -0.0254 55   ARG G NE  
18713 C  CZ  . ARG G 55   ? 1.2906 1.4108 1.3239 0.0768  0.1037  -0.0269 55   ARG G CZ  
18714 N  NH1 . ARG G 55   ? 1.1042 1.2361 1.1486 0.0777  0.0975  -0.0299 55   ARG G NH1 
18715 N  NH2 . ARG G 55   ? 1.4061 1.5192 1.4379 0.0718  0.1065  -0.0251 55   ARG G NH2 
18716 N  N   . LEU G 56   ? 2.5569 2.7015 2.5959 0.0580  0.1405  -0.0313 56   LEU G N   
18717 C  CA  . LEU G 56   ? 2.6208 2.7603 2.6540 0.0525  0.1517  -0.0298 56   LEU G CA  
18718 C  C   . LEU G 56   ? 2.7213 2.8475 2.7483 0.0466  0.1561  -0.0272 56   LEU G C   
18719 O  O   . LEU G 56   ? 2.7526 2.8649 2.7659 0.0471  0.1630  -0.0238 56   LEU G O   
18720 C  CB  . LEU G 56   ? 2.5482 2.7043 2.5943 0.0465  0.1561  -0.0336 56   LEU G CB  
18721 C  CG  . LEU G 56   ? 2.5698 2.7231 2.6109 0.0416  0.1681  -0.0325 56   LEU G CG  
18722 C  CD1 . LEU G 56   ? 2.6044 2.7464 2.6299 0.0492  0.1711  -0.0292 56   LEU G CD1 
18723 C  CD2 . LEU G 56   ? 2.6325 2.8049 2.6879 0.0371  0.1713  -0.0367 56   LEU G CD2 
18724 N  N   . PRO G 57   ? 1.4542 1.5829 1.4895 0.0412  0.1529  -0.0286 57   PRO G N   
18725 C  CA  . PRO G 57   ? 1.3459 1.4603 1.3738 0.0361  0.1572  -0.0259 57   PRO G CA  
18726 C  C   . PRO G 57   ? 1.3243 1.4223 1.3379 0.0434  0.1543  -0.0218 57   PRO G C   
18727 O  O   . PRO G 57   ? 1.3758 1.4720 1.3911 0.0461  0.1466  -0.0216 57   PRO G O   
18728 C  CB  . PRO G 57   ? 1.1779 1.3003 1.2186 0.0304  0.1525  -0.0288 57   PRO G CB  
18729 C  CG  . PRO G 57   ? 1.1572 1.2993 1.2126 0.0301  0.1488  -0.0332 57   PRO G CG  
18730 C  CD  . PRO G 57   ? 1.2197 1.3637 1.2708 0.0393  0.1457  -0.0325 57   PRO G CD  
18731 N  N   . PHE G 58   ? 1.0732 1.1594 1.0725 0.0467  0.1604  -0.0186 58   PHE G N   
18732 C  CA  . PHE G 58   ? 0.9920 1.0627 0.9767 0.0541  0.1580  -0.0147 58   PHE G CA  
18733 C  C   . PHE G 58   ? 0.9878 1.0470 0.9687 0.0505  0.1584  -0.0127 58   PHE G C   
18734 O  O   . PHE G 58   ? 1.0417 1.1013 1.0275 0.0416  0.1632  -0.0137 58   PHE G O   
18735 C  CB  . PHE G 58   ? 1.0521 1.1116 1.0213 0.0577  0.1657  -0.0116 58   PHE G CB  
18736 C  CG  . PHE G 58   ? 1.1768 1.2457 1.1475 0.0625  0.1652  -0.0132 58   PHE G CG  
18737 C  CD1 . PHE G 58   ? 1.0730 1.1457 1.0435 0.0716  0.1561  -0.0139 58   PHE G CD1 
18738 C  CD2 . PHE G 58   ? 1.2069 1.2810 1.1792 0.0580  0.1739  -0.0141 58   PHE G CD2 
18739 C  CE1 . PHE G 58   ? 0.9293 1.0099 0.9005 0.0762  0.1557  -0.0154 58   PHE G CE1 
18740 C  CE2 . PHE G 58   ? 1.0730 1.1557 1.0464 0.0628  0.1737  -0.0156 58   PHE G CE2 
18741 C  CZ  . PHE G 58   ? 0.9696 1.0551 0.9420 0.0721  0.1645  -0.0162 58   PHE G CZ  
18742 N  N   . THR G 59   ? 0.8572 0.9062 0.8292 0.0575  0.1532  -0.0101 59   THR G N   
18743 C  CA  . THR G 59   ? 0.8979 0.9355 0.8653 0.0554  0.1533  -0.0080 59   THR G CA  
18744 C  C   . THR G 59   ? 0.9631 0.9858 0.9181 0.0508  0.1644  -0.0051 59   THR G C   
18745 O  O   . THR G 59   ? 1.0574 1.0714 0.9998 0.0546  0.1697  -0.0026 59   THR G O   
18746 C  CB  . THR G 59   ? 0.8434 0.8737 0.8035 0.0647  0.1457  -0.0057 59   THR G CB  
18747 O  OG1 . THR G 59   ? 0.8866 0.9054 0.8416 0.0630  0.1464  -0.0035 59   THR G OG1 
18748 C  CG2 . THR G 59   ? 0.9467 0.9681 0.8921 0.0730  0.1475  -0.0030 59   THR G CG2 
18749 N  N   . PRO G 60   ? 1.1515 1.1703 1.1091 0.0425  0.1683  -0.0054 60   PRO G N   
18750 C  CA  . PRO G 60   ? 1.0968 1.1010 1.0428 0.0372  0.1793  -0.0028 60   PRO G CA  
18751 C  C   . PRO G 60   ? 1.1657 1.1502 1.0927 0.0444  0.1808  0.0021  60   PRO G C   
18752 O  O   . PRO G 60   ? 1.1428 1.1245 1.0675 0.0514  0.1731  0.0033  60   PRO G O   
18753 C  CB  . PRO G 60   ? 1.0384 1.0439 0.9928 0.0273  0.1809  -0.0048 60   PRO G CB  
18754 C  CG  . PRO G 60   ? 0.9986 1.0237 0.9715 0.0261  0.1723  -0.0092 60   PRO G CG  
18755 C  CD  . PRO G 60   ? 1.0473 1.0760 1.0194 0.0368  0.1633  -0.0085 60   PRO G CD  
18756 N  N   . GLN G 61   ? 1.5448 1.5156 1.4581 0.0427  0.1910  0.0049  61   GLN G N   
18757 C  CA  . GLN G 61   ? 1.5754 1.5258 1.4689 0.0492  0.1941  0.0098  61   GLN G CA  
18758 C  C   . GLN G 61   ? 1.5326 1.4681 1.4183 0.0410  0.2038  0.0115  61   GLN G C   
18759 O  O   . GLN G 61   ? 1.5108 1.4396 1.3897 0.0363  0.2142  0.0125  61   GLN G O   
18760 C  CB  . GLN G 61   ? 1.7697 1.7151 1.6508 0.0564  0.1974  0.0120  61   GLN G CB  
18761 C  CG  . GLN G 61   ? 1.7272 1.6810 1.6102 0.0670  0.1871  0.0114  61   GLN G CG  
18762 C  CD  . GLN G 61   ? 1.8760 1.8386 1.7602 0.0694  0.1888  0.0101  61   GLN G CD  
18763 O  OE1 . GLN G 61   ? 1.9666 1.9231 1.8430 0.0664  0.1987  0.0114  61   GLN G OE1 
18764 N  NE2 . GLN G 61   ? 1.9343 1.9108 1.8279 0.0748  0.1794  0.0075  61   GLN G NE2 
18765 N  N   . PRO G 62   ? 1.2436 1.1735 1.1302 0.0388  0.2012  0.0118  62   PRO G N   
18766 C  CA  . PRO G 62   ? 1.2404 1.1555 1.1195 0.0307  0.2103  0.0131  62   PRO G CA  
18767 C  C   . PRO G 62   ? 1.2874 1.1803 1.1439 0.0354  0.2185  0.0182  62   PRO G C   
18768 O  O   . PRO G 62   ? 1.3402 1.2269 1.1857 0.0463  0.2149  0.0212  62   PRO G O   
18769 C  CB  . PRO G 62   ? 1.2167 1.1305 1.1002 0.0304  0.2038  0.0127  62   PRO G CB  
18770 C  CG  . PRO G 62   ? 1.2336 1.1677 1.1338 0.0338  0.1924  0.0093  62   PRO G CG  
18771 C  CD  . PRO G 62   ? 1.2331 1.1706 1.1287 0.0428  0.1901  0.0105  62   PRO G CD  
18772 N  N   . ALA G 63   ? 1.4355 1.3161 1.2849 0.0269  0.2295  0.0192  63   ALA G N   
18773 C  CA  . ALA G 63   ? 1.5528 1.4105 1.3798 0.0306  0.2383  0.0242  63   ALA G CA  
18774 C  C   . ALA G 63   ? 1.6536 1.4962 1.4679 0.0386  0.2342  0.0277  63   ALA G C   
18775 O  O   . ALA G 63   ? 1.7268 1.5722 1.5489 0.0362  0.2289  0.0262  63   ALA G O   
18776 C  CB  . ALA G 63   ? 1.6413 1.4886 1.4642 0.0187  0.2511  0.0242  63   ALA G CB  
18777 N  N   . PRO G 64   ? 1.4277 1.2546 1.2226 0.0485  0.2363  0.0322  64   PRO G N   
18778 C  CA  . PRO G 64   ? 1.4987 1.3112 1.2812 0.0566  0.2326  0.0356  64   PRO G CA  
18779 C  C   . PRO G 64   ? 1.6342 1.4306 1.4100 0.0490  0.2398  0.0367  64   PRO G C   
18780 O  O   . PRO G 64   ? 1.7114 1.4995 1.4831 0.0398  0.2505  0.0368  64   PRO G O   
18781 C  CB  . PRO G 64   ? 1.5219 1.3202 1.2837 0.0676  0.2356  0.0401  64   PRO G CB  
18782 C  CG  . PRO G 64   ? 1.6022 1.4131 1.3698 0.0673  0.2367  0.0384  64   PRO G CG  
18783 C  CD  . PRO G 64   ? 1.4334 1.2557 1.2169 0.0534  0.2416  0.0344  64   PRO G CD  
18784 N  N   . VAL G 65   ? 1.5551 1.3473 1.3299 0.0528  0.2338  0.0375  65   VAL G N   
18785 C  CA  . VAL G 65   ? 1.6085 1.3857 1.3774 0.0461  0.2395  0.0383  65   VAL G CA  
18786 C  C   . VAL G 65   ? 1.7333 1.4842 1.4777 0.0482  0.2507  0.0432  65   VAL G C   
18787 O  O   . VAL G 65   ? 1.6436 1.3860 1.3734 0.0584  0.2513  0.0468  65   VAL G O   
18788 C  CB  . VAL G 65   ? 1.3743 1.1522 1.1462 0.0513  0.2306  0.0384  65   VAL G CB  
18789 C  CG1 . VAL G 65   ? 1.1764 0.9785 0.9722 0.0474  0.2210  0.0335  65   VAL G CG1 
18790 C  CG2 . VAL G 65   ? 1.4689 1.2401 1.2281 0.0662  0.2252  0.0422  65   VAL G CG2 
18791 N  N   . THR G 66   ? 2.2271 1.9645 1.9666 0.0383  0.2597  0.0433  66   THR G N   
18792 C  CA  . THR G 66   ? 2.2283 1.9387 1.9438 0.0395  0.2708  0.0480  66   THR G CA  
18793 C  C   . THR G 66   ? 2.1993 1.8942 1.8986 0.0520  0.2669  0.0523  66   THR G C   
18794 O  O   . THR G 66   ? 2.2105 1.9156 1.9183 0.0578  0.2563  0.0512  66   THR G O   
18795 C  CB  . THR G 66   ? 2.1015 1.8014 1.8166 0.0254  0.2808  0.0466  66   THR G CB  
18796 O  OG1 . THR G 66   ? 1.9380 1.6105 1.6289 0.0265  0.2924  0.0513  66   THR G OG1 
18797 C  CG2 . THR G 66   ? 2.1509 1.8518 1.8736 0.0220  0.2755  0.0446  66   THR G CG2 
18798 N  N   . GLY G 67   ? 2.5767 2.2466 2.2520 0.0561  0.2760  0.0571  67   GLY G N   
18799 C  CA  . GLY G 67   ? 2.5784 2.2335 2.2362 0.0698  0.2726  0.0615  67   GLY G CA  
18800 C  C   . GLY G 67   ? 2.5899 2.2418 2.2505 0.0698  0.2678  0.0610  67   GLY G C   
18801 O  O   . GLY G 67   ? 2.4963 2.1525 2.1571 0.0805  0.2585  0.0620  67   GLY G O   
18802 N  N   . ASN G 68   ? 1.9321 1.5767 1.5950 0.0578  0.2742  0.0594  68   ASN G N   
18803 C  CA  . ASN G 68   ? 1.8193 1.4573 1.4819 0.0576  0.2712  0.0593  68   ASN G CA  
18804 C  C   . ASN G 68   ? 1.8335 1.4966 1.5193 0.0577  0.2586  0.0551  68   ASN G C   
18805 O  O   . ASN G 68   ? 1.7965 1.4788 1.5021 0.0484  0.2563  0.0505  68   ASN G O   
18806 C  CB  . ASN G 68   ? 1.8989 1.5228 1.5581 0.0440  0.2815  0.0581  68   ASN G CB  
18807 C  CG  . ASN G 68   ? 1.9207 1.5190 1.5603 0.0480  0.2857  0.0618  68   ASN G CG  
18808 O  OD1 . ASN G 68   ? 1.8478 1.4408 1.4781 0.0610  0.2801  0.0649  68   ASN G OD1 
18809 N  ND2 . ASN G 68   ? 2.0387 1.6211 1.6719 0.0368  0.2955  0.0612  68   ASN G ND2 
18810 N  N   . THR G 69   ? 1.6784 1.3414 1.3619 0.0684  0.2505  0.0567  69   THR G N   
18811 C  CA  . THR G 69   ? 1.5143 1.1992 1.2181 0.0695  0.2387  0.0533  69   THR G CA  
18812 C  C   . THR G 69   ? 1.3857 1.0608 1.0834 0.0749  0.2356  0.0549  69   THR G C   
18813 O  O   . THR G 69   ? 1.3828 1.0351 1.0600 0.0799  0.2414  0.0590  69   THR G O   
18814 C  CB  . THR G 69   ? 1.5744 1.2773 1.2863 0.0792  0.2293  0.0529  69   THR G CB  
18815 O  OG1 . THR G 69   ? 1.6381 1.3269 1.3301 0.0908  0.2316  0.0575  69   THR G OG1 
18816 C  CG2 . THR G 69   ? 1.5657 1.2873 1.2934 0.0717  0.2289  0.0492  69   THR G CG2 
18817 N  N   . TYR G 70   ? 1.2501 0.9426 0.9656 0.0741  0.2264  0.0518  70   TYR G N   
18818 C  CA  . TYR G 70   ? 1.2026 0.8898 0.9155 0.0797  0.2220  0.0529  70   TYR G CA  
18819 C  C   . TYR G 70   ? 1.1641 0.8520 0.8702 0.0952  0.2152  0.0560  70   TYR G C   
18820 O  O   . TYR G 70   ? 1.1283 0.8095 0.8292 0.1016  0.2125  0.0577  70   TYR G O   
18821 C  CB  . TYR G 70   ? 1.1766 0.8829 0.9114 0.0733  0.2147  0.0484  70   TYR G CB  
18822 C  CG  . TYR G 70   ? 1.1221 0.8529 0.8742 0.0785  0.2038  0.0463  70   TYR G CG  
18823 C  CD1 . TYR G 70   ? 1.1746 0.9200 0.9368 0.0749  0.2029  0.0440  70   TYR G CD1 
18824 C  CD2 . TYR G 70   ? 1.0499 0.7888 0.8078 0.0870  0.1949  0.0466  70   TYR G CD2 
18825 C  CE1 . TYR G 70   ? 1.0885 0.8550 0.8656 0.0797  0.1932  0.0420  70   TYR G CE1 
18826 C  CE2 . TYR G 70   ? 0.9970 0.7573 0.7703 0.0913  0.1853  0.0445  70   TYR G CE2 
18827 C  CZ  . TYR G 70   ? 0.9803 0.7540 0.7629 0.0876  0.1845  0.0423  70   TYR G CZ  
18828 O  OH  . TYR G 70   ? 1.0269 0.8209 0.8242 0.0918  0.1751  0.0402  70   TYR G OH  
18829 N  N   . ARG G 71   ? 1.5321 1.2284 1.2386 0.1014  0.2123  0.0566  71   ARG G N   
18830 C  CA  . ARG G 71   ? 1.5430 1.2449 1.2473 0.1155  0.2041  0.0584  71   ARG G CA  
18831 C  C   . ARG G 71   ? 1.5264 1.2055 1.2074 0.1258  0.2079  0.0634  71   ARG G C   
18832 O  O   . ARG G 71   ? 1.5052 1.1865 1.1853 0.1360  0.2013  0.0646  71   ARG G O   
18833 C  CB  . ARG G 71   ? 1.7106 1.4241 1.4181 0.1194  0.2011  0.0579  71   ARG G CB  
18834 C  CG  . ARG G 71   ? 1.6777 1.4178 1.4096 0.1149  0.1927  0.0532  71   ARG G CG  
18835 C  CD  . ARG G 71   ? 1.7603 1.5093 1.4939 0.1167  0.1919  0.0525  71   ARG G CD  
18836 N  NE  . ARG G 71   ? 1.6880 1.4618 1.4438 0.1141  0.1832  0.0481  71   ARG G NE  
18837 C  CZ  . ARG G 71   ? 1.6521 1.4376 1.4222 0.1031  0.1846  0.0446  71   ARG G CZ  
18838 N  NH1 . ARG G 71   ? 1.6670 1.4429 1.4329 0.0931  0.1941  0.0445  71   ARG G NH1 
18839 N  NH2 . ARG G 71   ? 1.6083 1.4154 1.3972 0.1022  0.1762  0.0409  71   ARG G NH2 
18840 N  N   . THR G 72   ? 1.4984 1.1554 1.1604 0.1233  0.2189  0.0663  72   THR G N   
18841 C  CA  . THR G 72   ? 1.5108 1.1446 1.1490 0.1334  0.2232  0.0712  72   THR G CA  
18842 C  C   . THR G 72   ? 1.4773 1.1023 1.1134 0.1332  0.2231  0.0717  72   THR G C   
18843 O  O   . THR G 72   ? 1.5083 1.1243 1.1328 0.1448  0.2209  0.0748  72   THR G O   
18844 C  CB  . THR G 72   ? 1.4449 1.0562 1.0629 0.1302  0.2356  0.0742  72   THR G CB  
18845 O  OG1 . THR G 72   ? 1.5705 1.1570 1.1645 0.1392  0.2405  0.0790  72   THR G OG1 
18846 C  CG2 . THR G 72   ? 1.4313 1.0393 1.0555 0.1136  0.2436  0.0716  72   THR G CG2 
18847 N  N   . TYR G 73   ? 1.2717 0.8996 0.9191 0.1204  0.2254  0.0686  73   TYR G N   
18848 C  CA  . TYR G 73   ? 1.3115 0.9321 0.9580 0.1198  0.2250  0.0686  73   TYR G CA  
18849 C  C   . TYR G 73   ? 1.3031 0.9416 0.9629 0.1282  0.2133  0.0676  73   TYR G C   
18850 O  O   . TYR G 73   ? 1.2979 0.9275 0.9490 0.1368  0.2118  0.0700  73   TYR G O   
18851 C  CB  . TYR G 73   ? 1.3639 0.9861 1.0210 0.1040  0.2291  0.0649  73   TYR G CB  
18852 C  CG  . TYR G 73   ? 1.4295 1.0310 1.0724 0.0948  0.2415  0.0659  73   TYR G CG  
18853 C  CD1 . TYR G 73   ? 1.4107 0.9867 1.0350 0.0945  0.2493  0.0685  73   TYR G CD1 
18854 C  CD2 . TYR G 73   ? 1.5075 1.1148 1.1554 0.0864  0.2458  0.0641  73   TYR G CD2 
18855 C  CE1 . TYR G 73   ? 1.5048 1.0612 1.1160 0.0855  0.2610  0.0693  73   TYR G CE1 
18856 C  CE2 . TYR G 73   ? 1.5569 1.1456 1.1924 0.0775  0.2576  0.0649  73   TYR G CE2 
18857 C  CZ  . TYR G 73   ? 1.5413 1.1044 1.1584 0.0769  0.2652  0.0675  73   TYR G CZ  
18858 O  OH  . TYR G 73   ? 1.4900 1.0339 1.0947 0.0675  0.2773  0.0682  73   TYR G OH  
18859 N  N   . VAL G 74   ? 1.5500 1.2136 1.2310 0.1259  0.2052  0.0640  74   VAL G N   
18860 C  CA  . VAL G 74   ? 1.4634 1.1450 1.1591 0.1323  0.1945  0.0625  74   VAL G CA  
18861 C  C   . VAL G 74   ? 1.4589 1.1395 1.1451 0.1479  0.1897  0.0656  74   VAL G C   
18862 O  O   . VAL G 74   ? 1.4822 1.1651 1.1695 0.1559  0.1845  0.0665  74   VAL G O   
18863 C  CB  . VAL G 74   ? 1.4088 1.1164 1.1287 0.1254  0.1876  0.0578  74   VAL G CB  
18864 C  CG1 . VAL G 74   ? 1.4667 1.1930 1.2009 0.1330  0.1765  0.0566  74   VAL G CG1 
18865 C  CG2 . VAL G 74   ? 1.4638 1.1738 1.1942 0.1110  0.1910  0.0545  74   VAL G CG2 
18866 N  N   . ASN G 75   ? 1.2719 0.9494 0.9487 0.1526  0.1914  0.0673  75   ASN G N   
18867 C  CA  . ASN G 75   ? 1.2461 0.9226 0.9131 0.1677  0.1867  0.0700  75   ASN G CA  
18868 C  C   . ASN G 75   ? 1.2005 0.8544 0.8464 0.1762  0.1913  0.0743  75   ASN G C   
18869 O  O   . ASN G 75   ? 1.1656 0.8227 0.8099 0.1878  0.1852  0.0756  75   ASN G O   
18870 C  CB  . ASN G 75   ? 1.2160 0.8914 0.8752 0.1706  0.1886  0.0709  75   ASN G CB  
18871 C  CG  . ASN G 75   ? 1.1869 0.8864 0.8669 0.1654  0.1823  0.0668  75   ASN G CG  
18872 O  OD1 . ASN G 75   ? 1.2328 0.9518 0.9320 0.1646  0.1737  0.0637  75   ASN G OD1 
18873 N  ND2 . ASN G 75   ? 1.2094 0.9070 0.8851 0.1620  0.1868  0.0667  75   ASN G ND2 
18874 N  N   . ASP G 76   ? 1.7443 1.3754 1.3738 0.1706  0.2021  0.0765  76   ASP G N   
18875 C  CA  . ASP G 76   ? 1.8637 1.4714 1.4717 0.1785  0.2072  0.0807  76   ASP G CA  
18876 C  C   . ASP G 76   ? 1.8563 1.4672 1.4719 0.1792  0.2033  0.0799  76   ASP G C   
18877 O  O   . ASP G 76   ? 1.8723 1.4762 1.4779 0.1910  0.2012  0.0825  76   ASP G O   
18878 C  CB  . ASP G 76   ? 1.8344 1.4166 1.4241 0.1707  0.2201  0.0829  76   ASP G CB  
18879 C  CG  . ASP G 76   ? 1.9666 1.5417 1.5444 0.1721  0.2252  0.0847  76   ASP G CG  
18880 O  OD1 . ASP G 76   ? 2.0575 1.6444 1.6376 0.1812  0.2186  0.0849  76   ASP G OD1 
18881 O  OD2 . ASP G 76   ? 2.0356 1.5931 1.6017 0.1638  0.2358  0.0858  76   ASP G OD2 
18882 N  N   . ALA G 77   ? 1.6498 1.2713 1.2828 0.1670  0.2024  0.0761  77   ALA G N   
18883 C  CA  . ALA G 77   ? 1.5952 1.2185 1.2346 0.1669  0.1996  0.0753  77   ALA G CA  
18884 C  C   . ALA G 77   ? 1.4527 1.0966 1.1060 0.1766  0.1884  0.0744  77   ALA G C   
18885 O  O   . ALA G 77   ? 1.4549 1.0947 1.1039 0.1846  0.1863  0.0760  77   ALA G O   
18886 C  CB  . ALA G 77   ? 1.5763 1.2059 1.2305 0.1514  0.2014  0.0713  77   ALA G CB  
18887 N  N   . ARG G 78   ? 1.1569 0.8231 0.8271 0.1759  0.1811  0.0716  78   ARG G N   
18888 C  CA  . ARG G 78   ? 1.1544 0.8405 0.8383 0.1846  0.1705  0.0704  78   ARG G CA  
18889 C  C   . ARG G 78   ? 1.3270 1.0066 0.9961 0.2003  0.1684  0.0739  78   ARG G C   
18890 O  O   . ARG G 78   ? 1.3109 0.9989 0.9850 0.2092  0.1620  0.0741  78   ARG G O   
18891 C  CB  . ARG G 78   ? 1.2278 0.9380 0.9323 0.1797  0.1638  0.0666  78   ARG G CB  
18892 C  CG  . ARG G 78   ? 1.3019 1.0227 1.0240 0.1657  0.1637  0.0627  78   ARG G CG  
18893 C  CD  . ARG G 78   ? 1.3367 1.0831 1.0820 0.1658  0.1536  0.0593  78   ARG G CD  
18894 N  NE  . ARG G 78   ? 1.3483 1.1096 1.1022 0.1666  0.1488  0.0575  78   ARG G NE  
18895 C  CZ  . ARG G 78   ? 1.4620 1.2354 1.2295 0.1568  0.1479  0.0542  78   ARG G CZ  
18896 N  NH1 . ARG G 78   ? 1.4382 1.2116 1.2129 0.1453  0.1512  0.0521  78   ARG G NH1 
18897 N  NH2 . ARG G 78   ? 1.5419 1.3278 1.3156 0.1589  0.1435  0.0528  78   ARG G NH2 
18898 N  N   . THR G 79   ? 1.2895 0.9542 0.9403 0.2042  0.1738  0.0766  79   THR G N   
18899 C  CA  . THR G 79   ? 1.2427 0.8976 0.8760 0.2196  0.1728  0.0803  79   THR G CA  
18900 C  C   . THR G 79   ? 1.3616 0.9978 0.9802 0.2249  0.1772  0.0834  79   THR G C   
18901 O  O   . THR G 79   ? 1.4292 1.0657 1.0423 0.2380  0.1729  0.0852  79   THR G O   
18902 C  CB  . THR G 79   ? 1.3050 0.9459 0.9203 0.2219  0.1786  0.0827  79   THR G CB  
18903 O  OG1 . THR G 79   ? 1.4131 1.0710 1.0424 0.2160  0.1751  0.0796  79   THR G OG1 
18904 C  CG2 . THR G 79   ? 1.3419 0.9755 0.9404 0.2389  0.1761  0.0861  79   THR G CG2 
18905 N  N   . LEU G 80   ? 1.3179 0.9379 0.9300 0.2150  0.1858  0.0839  80   LEU G N   
18906 C  CA  . LEU G 80   ? 1.3333 0.9353 0.9322 0.2189  0.1901  0.0865  80   LEU G CA  
18907 C  C   . LEU G 80   ? 1.2664 0.8850 0.8823 0.2211  0.1826  0.0845  80   LEU G C   
18908 O  O   . LEU G 80   ? 1.2876 0.8985 0.8946 0.2310  0.1821  0.0868  80   LEU G O   
18909 C  CB  . LEU G 80   ? 1.3827 0.9650 0.9726 0.2063  0.2007  0.0867  80   LEU G CB  
18910 C  CG  . LEU G 80   ? 1.3722 0.9280 0.9406 0.2108  0.2079  0.0903  80   LEU G CG  
18911 C  CD1 . LEU G 80   ? 1.5427 1.0774 1.0850 0.2221  0.2131  0.0951  80   LEU G CD1 
18912 C  CD2 . LEU G 80   ? 1.2956 0.8377 0.8619 0.1960  0.2164  0.0890  80   LEU G CD2 
18913 N  N   . LEU G 81   ? 1.2897 0.9307 0.9297 0.2123  0.1768  0.0802  81   LEU G N   
18914 C  CA  . LEU G 81   ? 1.2903 0.9482 0.9479 0.2134  0.1697  0.0781  81   LEU G CA  
18915 C  C   . LEU G 81   ? 1.3108 0.9847 0.9748 0.2268  0.1606  0.0783  81   LEU G C   
18916 O  O   . LEU G 81   ? 1.3544 1.0451 1.0351 0.2278  0.1541  0.0763  81   LEU G O   
18917 C  CB  . LEU G 81   ? 1.1708 0.8470 0.8513 0.1998  0.1667  0.0736  81   LEU G CB  
18918 C  CG  . LEU G 81   ? 1.1186 0.7832 0.7978 0.1864  0.1739  0.0725  81   LEU G CG  
18919 C  CD1 . LEU G 81   ? 1.0815 0.7667 0.7846 0.1751  0.1693  0.0679  81   LEU G CD1 
18920 C  CD2 . LEU G 81   ? 1.0861 0.7339 0.7534 0.1899  0.1780  0.0747  81   LEU G CD2 
18921 N  N   . ASN G 82   ? 1.3154 0.9847 0.9668 0.2368  0.1599  0.0805  82   ASN G N   
18922 C  CA  . ASN G 82   ? 1.3516 1.0342 1.0065 0.2506  0.1515  0.0808  82   ASN G CA  
18923 C  C   . ASN G 82   ? 1.3819 1.0444 1.0110 0.2636  0.1553  0.0852  82   ASN G C   
18924 O  O   . ASN G 82   ? 1.3290 0.9673 0.9381 0.2615  0.1647  0.0881  82   ASN G O   
18925 C  CB  . ASN G 82   ? 1.2508 0.9561 0.9223 0.2493  0.1437  0.0775  82   ASN G CB  
18926 C  CG  . ASN G 82   ? 1.2939 1.0187 0.9902 0.2369  0.1399  0.0732  82   ASN G CG  
18927 O  OD1 . ASN G 82   ? 1.2822 1.0140 0.9864 0.2282  0.1398  0.0710  82   ASN G OD1 
18928 N  ND2 . ASN G 82   ? 1.3884 1.1217 1.0967 0.2364  0.1368  0.0721  82   ASN G ND2 
18929 N  N   . SER G 83   ? 2.3781 2.0509 2.0078 0.2772  0.1480  0.0856  83   SER G N   
18930 C  CA  . SER G 83   ? 2.5478 2.2058 2.1547 0.2914  0.1496  0.0893  83   SER G CA  
18931 C  C   . SER G 83   ? 2.6271 2.2600 2.2125 0.2972  0.1572  0.0935  83   SER G C   
18932 O  O   . SER G 83   ? 2.6196 2.2332 2.1814 0.3066  0.1615  0.0972  83   SER G O   
18933 C  CB  . SER G 83   ? 2.6061 2.2545 2.2008 0.2893  0.1536  0.0903  83   SER G CB  
18934 O  OG  . SER G 83   ? 2.6377 2.2603 2.2144 0.2824  0.1651  0.0930  83   SER G OG  
18935 N  N   . TYR G 84   ? 1.7714 1.4034 1.3636 0.2922  0.1589  0.0930  84   TYR G N   
18936 C  CA  . TYR G 84   ? 1.7145 1.3238 1.2877 0.2979  0.1654  0.0966  84   TYR G CA  
18937 C  C   . TYR G 84   ? 1.7504 1.3295 1.2978 0.2951  0.1766  0.1001  84   TYR G C   
18938 O  O   . TYR G 84   ? 1.7664 1.3416 1.3158 0.2821  0.1813  0.0988  84   TYR G O   
18939 C  CB  . TYR G 84   ? 1.5914 1.2037 1.1577 0.3160  0.1601  0.0986  84   TYR G CB  
18940 C  CG  . TYR G 84   ? 1.5814 1.2219 1.1724 0.3189  0.1501  0.0953  84   TYR G CG  
18941 C  CD1 . TYR G 84   ? 1.6193 1.2849 1.2278 0.3208  0.1408  0.0922  84   TYR G CD1 
18942 C  CD2 . TYR G 84   ? 1.4872 1.1287 1.0836 0.3198  0.1503  0.0954  84   TYR G CD2 
18943 C  CE1 . TYR G 84   ? 1.6225 1.3134 1.2536 0.3229  0.1320  0.0892  84   TYR G CE1 
18944 C  CE2 . TYR G 84   ? 1.3570 1.0241 0.9759 0.3222  0.1417  0.0925  84   TYR G CE2 
18945 C  CZ  . TYR G 84   ? 1.5097 1.2014 1.1461 0.3236  0.1327  0.0894  84   TYR G CZ  
18946 O  OH  . TYR G 84   ? 1.6068 1.3235 1.2657 0.3255  0.1246  0.0865  84   TYR G OH  
18947 N  N   . GLY G 85   ? 1.2582 0.8160 0.7814 0.3072  0.1809  0.1043  85   GLY G N   
18948 C  CA  . GLY G 85   ? 1.3183 0.8454 0.8148 0.3062  0.1918  0.1081  85   GLY G CA  
18949 C  C   . GLY G 85   ? 1.3661 0.8697 0.8476 0.3055  0.1998  0.1105  85   GLY G C   
18950 O  O   . GLY G 85   ? 1.3915 0.9024 0.8833 0.3057  0.1971  0.1094  85   GLY G O   
18951 N  N   . TYR G 86   ? 2.0293 1.5034 1.4855 0.3047  0.2102  0.1140  86   TYR G N   
18952 C  CA  . TYR G 86   ? 2.0067 1.4538 1.4447 0.3032  0.2194  0.1166  86   TYR G CA  
18953 C  C   . TYR G 86   ? 1.9620 1.3941 1.3966 0.2857  0.2289  0.1157  86   TYR G C   
18954 O  O   . TYR G 86   ? 1.8788 1.3027 1.3046 0.2821  0.2334  0.1166  86   TYR G O   
18955 C  CB  . TYR G 86   ? 2.0016 1.4233 1.4093 0.3192  0.2241  0.1219  86   TYR G CB  
18956 C  CG  . TYR G 86   ? 2.1553 1.5931 1.5654 0.3363  0.2147  0.1222  86   TYR G CG  
18957 C  CD1 . TYR G 86   ? 2.2288 1.6919 1.6623 0.3388  0.2054  0.1195  86   TYR G CD1 
18958 C  CD2 . TYR G 86   ? 2.1958 1.6277 1.5871 0.3479  0.2148  0.1237  86   TYR G CD2 
18959 C  CE1 . TYR G 86   ? 2.2200 1.7024 1.6584 0.3517  0.1965  0.1185  86   TYR G CE1 
18960 C  CE2 . TYR G 86   ? 2.2161 1.6667 1.6115 0.3613  0.2056  0.1228  86   TYR G CE2 
18961 C  CZ  . TYR G 86   ? 2.1773 1.6534 1.5966 0.3627  0.1965  0.1202  86   TYR G CZ  
18962 O  OH  . TYR G 86   ? 2.0096 1.5052 1.4339 0.3750  0.1874  0.1191  86   TYR G OH  
18963 N  N   . THR G 87   ? 2.5063 1.9352 1.9478 0.2751  0.2319  0.1138  87   THR G N   
18964 C  CA  . THR G 87   ? 2.5575 1.9729 1.9966 0.2581  0.2407  0.1124  87   THR G CA  
18965 C  C   . THR G 87   ? 2.5565 1.9347 1.9641 0.2602  0.2526  0.1168  87   THR G C   
18966 O  O   . THR G 87   ? 2.6232 1.9860 2.0107 0.2751  0.2539  0.1209  87   THR G O   
18967 C  CB  . THR G 87   ? 2.5677 1.9943 2.0263 0.2458  0.2389  0.1083  87   THR G CB  
18968 O  OG1 . THR G 87   ? 2.5476 1.9641 2.0062 0.2287  0.2465  0.1064  87   THR G OG1 
18969 C  CG2 . THR G 87   ? 2.5857 1.9992 2.0344 0.2527  0.2404  0.1100  87   THR G CG2 
18970 N  N   . MET G 88   ? 1.9431 1.3066 1.3463 0.2450  0.2615  0.1157  88   MET G N   
18971 C  CA  . MET G 88   ? 2.0296 1.3574 1.4030 0.2452  0.2738  0.1197  88   MET G CA  
18972 C  C   . MET G 88   ? 2.0382 1.3455 1.3972 0.2494  0.2778  0.1214  88   MET G C   
18973 O  O   . MET G 88   ? 2.1584 1.4536 1.4994 0.2601  0.2801  0.1221  88   MET G O   
18974 C  CB  . MET G 88   ? 2.0736 1.3934 1.4484 0.2267  0.2820  0.1176  88   MET G CB  
18975 C  CG  . MET G 88   ? 2.1365 1.4624 1.5118 0.2254  0.2827  0.1180  88   MET G CG  
18976 S  SD  . MET G 88   ? 2.2219 1.5458 1.6055 0.2027  0.2909  0.1145  88   MET G SD  
18977 C  CE  . MET G 88   ? 2.0517 1.4187 1.4724 0.1963  0.2785  0.1090  88   MET G CE  
18978 N  N   . GLU G 89   ? 2.1582 1.4725 1.5320 0.2389  0.2766  0.1177  89   GLU G N   
18979 C  CA  . GLU G 89   ? 2.1941 1.4910 1.5563 0.2402  0.2807  0.1178  89   GLU G CA  
18980 C  C   . GLU G 89   ? 2.2163 1.5290 1.5875 0.2527  0.2717  0.1177  89   GLU G C   
18981 O  O   . GLU G 89   ? 2.2862 1.5901 1.6501 0.2545  0.2738  0.1167  89   GLU G O   
18982 C  CB  . GLU G 89   ? 2.2822 1.5723 1.6513 0.2219  0.2859  0.1148  89   GLU G CB  
18983 C  CG  . GLU G 89   ? 2.2321 1.5556 1.6340 0.2109  0.2774  0.1092  89   GLU G CG  
18984 C  CD  . GLU G 89   ? 2.3018 1.6399 1.7182 0.2138  0.2703  0.1071  89   GLU G CD  
18985 O  OE1 . GLU G 89   ? 2.3577 1.6765 1.7590 0.2187  0.2742  0.1089  89   GLU G OE1 
18986 O  OE2 . GLU G 89   ? 2.1690 1.5374 1.6113 0.2111  0.2611  0.1038  89   GLU G OE2 
18987 N  N   . GLY G 90   ? 2.0668 1.4055 1.4553 0.2605  0.2617  0.1178  90   GLY G N   
18988 C  CA  . GLY G 90   ? 2.1399 1.4957 1.5400 0.2710  0.2532  0.1173  90   GLY G CA  
18989 C  C   . GLY G 90   ? 2.0443 1.4119 1.4411 0.2886  0.2465  0.1191  90   GLY G C   
18990 O  O   . GLY G 90   ? 1.8825 1.2383 1.2606 0.2949  0.2501  0.1209  90   GLY G O   
18991 N  N   . LYS G 91   ? 3.3627 2.7555 2.7788 0.2959  0.2365  0.1179  91   LYS G N   
18992 C  CA  . LYS G 91   ? 3.5023 2.9108 2.9185 0.3116  0.2289  0.1186  91   LYS G CA  
18993 C  C   . LYS G 91   ? 3.3977 2.8285 2.8303 0.3154  0.2207  0.1180  91   LYS G C   
18994 O  O   . LYS G 91   ? 3.4357 2.8655 2.8579 0.3229  0.2199  0.1196  91   LYS G O   
18995 C  CB  . LYS G 91   ? 3.4895 2.9116 2.9151 0.3177  0.2236  0.1174  91   LYS G CB  
18996 N  N   . VAL G 92   ? 1.4848 0.9421 0.9454 0.3075  0.2137  0.1140  92   VAL G N   
18997 C  CA  . VAL G 92   ? 1.4947 0.9808 0.9750 0.3097  0.2040  0.1116  92   VAL G CA  
18998 C  C   . VAL G 92   ? 1.4100 0.9165 0.9163 0.2929  0.2009  0.1068  92   VAL G C   
18999 O  O   . VAL G 92   ? 1.2866 0.7924 0.8008 0.2830  0.2031  0.1049  92   VAL G O   
19000 C  CB  . VAL G 92   ? 1.5633 1.0682 1.0525 0.3251  0.1949  0.1117  92   VAL G CB  
19001 C  CG1 . VAL G 92   ? 1.4883 1.0059 0.9949 0.3212  0.1919  0.1094  92   VAL G CG1 
19002 C  CG2 . VAL G 92   ? 1.5729 1.1041 1.0780 0.3292  0.1854  0.1097  92   VAL G CG2 
19003 N  N   . HIS G 93   ? 2.0449 1.5689 1.5635 0.2901  0.1959  0.1048  93   HIS G N   
19004 C  CA  . HIS G 93   ? 1.8767 1.4237 1.4213 0.2764  0.1914  0.1002  93   HIS G CA  
19005 C  C   . HIS G 93   ? 1.8163 1.3927 1.3847 0.2812  0.1806  0.0975  93   HIS G C   
19006 O  O   . HIS G 93   ? 1.8537 1.4357 1.4196 0.2956  0.1758  0.0990  93   HIS G O   
19007 C  CB  . HIS G 93   ? 1.8728 1.4244 1.4190 0.2713  0.1913  0.0993  93   HIS G CB  
19008 C  CG  . HIS G 93   ? 1.9161 1.4458 1.4485 0.2599  0.2016  0.1002  93   HIS G CG  
19009 N  ND1 . HIS G 93   ? 1.7880 1.3170 1.3178 0.2553  0.2037  0.1000  93   HIS G ND1 
19010 C  CD2 . HIS G 93   ? 1.9962 1.5042 1.5171 0.2517  0.2105  0.1009  93   HIS G CD2 
19011 C  CE1 . HIS G 93   ? 1.8931 1.4014 1.4108 0.2447  0.2136  0.1007  93   HIS G CE1 
19012 N  NE2 . HIS G 93   ? 2.0114 1.5066 1.5237 0.2422  0.2178  0.1012  93   HIS G NE2 
19013 N  N   . ILE G 94   ? 1.6256 1.2209 1.2171 0.2690  0.1769  0.0935  94   ILE G N   
19014 C  CA  . ILE G 94   ? 1.5412 1.1660 1.1575 0.2712  0.1668  0.0904  94   ILE G CA  
19015 C  C   . ILE G 94   ? 1.5079 1.1513 1.1431 0.2600  0.1629  0.0867  94   ILE G C   
19016 O  O   . ILE G 94   ? 1.5228 1.1613 1.1609 0.2463  0.1674  0.0851  94   ILE G O   
19017 C  CB  . ILE G 94   ? 1.5585 1.1878 1.1848 0.2689  0.1661  0.0893  94   ILE G CB  
19018 C  CG1 . ILE G 94   ? 1.4935 1.1019 1.0993 0.2795  0.1711  0.0931  94   ILE G CG1 
19019 C  CG2 . ILE G 94   ? 1.4903 1.1496 1.1415 0.2719  0.1560  0.0865  94   ILE G CG2 
19020 C  CD1 . ILE G 94   ? 1.6152 1.2300 1.2308 0.2803  0.1694  0.0923  94   ILE G CD1 
19021 N  N   . PRO G 95   ? 1.1422 0.8066 0.7901 0.2652  0.1546  0.0851  95   PRO G N   
19022 C  CA  . PRO G 95   ? 1.1031 0.7849 0.7686 0.2550  0.1508  0.0815  95   PRO G CA  
19023 C  C   . PRO G 95   ? 1.2136 0.9110 0.9012 0.2440  0.1480  0.0779  95   PRO G C   
19024 O  O   . PRO G 95   ? 1.2711 0.9746 0.9660 0.2471  0.1455  0.0777  95   PRO G O   
19025 C  CB  . PRO G 95   ? 1.1889 0.8891 0.8619 0.2654  0.1419  0.0807  95   PRO G CB  
19026 C  CG  . PRO G 95   ? 1.3044 0.9912 0.9578 0.2808  0.1431  0.0845  95   PRO G CG  
19027 C  CD  . PRO G 95   ? 1.2496 0.9218 0.8949 0.2811  0.1485  0.0864  95   PRO G CD  
19028 N  N   . ILE G 96   ? 2.1038 1.8076 1.8016 0.2313  0.1485  0.0752  96   ILE G N   
19029 C  CA  . ILE G 96   ? 2.0864 1.8066 1.8058 0.2212  0.1451  0.0716  96   ILE G CA  
19030 C  C   . ILE G 96   ? 2.1513 1.8975 1.8906 0.2265  0.1351  0.0694  96   ILE G C   
19031 O  O   . ILE G 96   ? 2.1559 1.9091 1.8939 0.2360  0.1304  0.0699  96   ILE G O   
19032 C  CB  . ILE G 96   ? 2.0006 1.7216 1.7257 0.2069  0.1480  0.0691  96   ILE G CB  
19033 C  CG1 . ILE G 96   ? 1.9193 1.6448 1.6570 0.1959  0.1487  0.0665  96   ILE G CG1 
19034 C  CG2 . ILE G 96   ? 2.1344 1.8748 1.8731 0.2061  0.1415  0.0667  96   ILE G CG2 
19035 C  CD1 . ILE G 96   ? 1.8284 1.5334 1.5520 0.1952  0.1556  0.0685  96   ILE G CD1 
19036 N  N   . ASP G 97   ? 1.9674 1.7278 1.7250 0.2202  0.1317  0.0667  97   ASP G N   
19037 C  CA  . ASP G 97   ? 2.0099 1.7936 1.7869 0.2244  0.1231  0.0646  97   ASP G CA  
19038 C  C   . ASP G 97   ? 1.9841 1.7674 1.7558 0.2380  0.1211  0.0669  97   ASP G C   
19039 O  O   . ASP G 97   ? 1.9553 1.7578 1.7418 0.2432  0.1139  0.0654  97   ASP G O   
19040 C  CB  . ASP G 97   ? 2.0694 1.8703 1.8578 0.2242  0.1167  0.0622  97   ASP G CB  
19041 C  CG  . ASP G 97   ? 2.2174 2.0426 2.0301 0.2212  0.1091  0.0588  97   ASP G CG  
19042 O  OD1 . ASP G 97   ? 2.1088 1.9380 1.9295 0.2200  0.1088  0.0585  97   ASP G OD1 
19043 O  OD2 . ASP G 97   ? 2.4070 2.2469 2.2304 0.2201  0.1037  0.0564  97   ASP G OD2 
19044 N  N   . ARG G 98   ? 1.1981 0.9600 0.9491 0.2440  0.1273  0.0704  98   ARG G N   
19045 C  CA  . ARG G 98   ? 1.2092 0.9679 0.9532 0.2567  0.1266  0.0729  98   ARG G CA  
19046 C  C   . ARG G 98   ? 1.1754 0.9172 0.9096 0.2551  0.1332  0.0747  98   ARG G C   
19047 O  O   . ARG G 98   ? 1.1584 0.9055 0.8974 0.2611  0.1314  0.0752  98   ARG G O   
19048 C  CB  . ARG G 98   ? 1.3548 1.1024 1.0799 0.2688  0.1274  0.0758  98   ARG G CB  
19049 C  CG  . ARG G 98   ? 1.4437 1.1836 1.1573 0.2826  0.1280  0.0788  98   ARG G CG  
19050 C  CD  . ARG G 98   ? 1.5265 1.2908 1.2587 0.2899  0.1195  0.0769  98   ARG G CD  
19051 N  NE  . ARG G 98   ? 1.5473 1.3067 1.2746 0.2985  0.1211  0.0790  98   ARG G NE  
19052 C  CZ  . ARG G 98   ? 1.4356 1.1869 1.1480 0.3128  0.1214  0.0818  98   ARG G CZ  
19053 N  NH1 . ARG G 98   ? 1.5798 1.3263 1.2800 0.3205  0.1201  0.0831  98   ARG G NH1 
19054 N  NH2 . ARG G 98   ? 1.3383 1.0859 1.0475 0.3199  0.1229  0.0835  98   ARG G NH2 
19055 N  N   . ALA G 99   ? 1.4020 1.1238 1.1229 0.2468  0.1409  0.0756  99   ALA G N   
19056 C  CA  . ALA G 99   ? 1.3761 1.0828 1.0896 0.2431  0.1469  0.0766  99   ALA G CA  
19057 C  C   . ALA G 99   ? 1.3461 1.0682 1.0801 0.2340  0.1439  0.0733  99   ALA G C   
19058 O  O   . ALA G 99   ? 1.4240 1.1404 1.1566 0.2342  0.1463  0.0739  99   ALA G O   
19059 C  CB  . ALA G 99   ? 1.2015 0.8838 0.8968 0.2354  0.1557  0.0777  99   ALA G CB  
19060 N  N   . MET G 100  ? 1.4469 1.1879 1.1993 0.2263  0.1389  0.0701  100  MET G N   
19061 C  CA  . MET G 100  ? 1.4382 1.1946 1.2102 0.2185  0.1356  0.0671  100  MET G CA  
19062 C  C   . MET G 100  ? 1.4440 1.2151 1.2270 0.2275  0.1305  0.0673  100  MET G C   
19063 O  O   . MET G 100  ? 1.4649 1.2401 1.2564 0.2244  0.1305  0.0664  100  MET G O   
19064 C  CB  . MET G 100  ? 1.5083 1.2814 1.2966 0.2094  0.1312  0.0637  100  MET G CB  
19065 C  CG  . MET G 100  ? 1.4660 1.2271 1.2468 0.1986  0.1364  0.0629  100  MET G CG  
19066 S  SD  . MET G 100  ? 1.5528 1.3306 1.3463 0.1933  0.1315  0.0601  100  MET G SD  
19067 C  CE  . MET G 100  ? 1.3474 1.1485 1.1669 0.1856  0.1252  0.0562  100  MET G CE  
19068 N  N   . ASP G 101  ? 1.5984 1.3776 1.3816 0.2387  0.1261  0.0683  101  ASP G N   
19069 C  CA  . ASP G 101  ? 1.5831 1.3757 1.3757 0.2481  0.1216  0.0685  101  ASP G CA  
19070 C  C   . ASP G 101  ? 1.6066 1.3828 1.3847 0.2550  0.1269  0.0715  101  ASP G C   
19071 O  O   . ASP G 101  ? 1.6765 1.4613 1.4635 0.2584  0.1253  0.0714  101  ASP G O   
19072 C  CB  . ASP G 101  ? 1.5827 1.3879 1.3783 0.2585  0.1155  0.0686  101  ASP G CB  
19073 C  CG  . ASP G 101  ? 1.6309 1.4512 1.4396 0.2523  0.1103  0.0656  101  ASP G CG  
19074 O  OD1 . ASP G 101  ? 1.7340 1.5725 1.5628 0.2460  0.1059  0.0627  101  ASP G OD1 
19075 O  OD2 . ASP G 101  ? 1.6734 1.4870 1.4717 0.2539  0.1108  0.0663  101  ASP G OD2 
19076 N  N   . LEU G 102  ? 1.1389 0.8911 0.8942 0.2572  0.1334  0.0743  102  LEU G N   
19077 C  CA  . LEU G 102  ? 1.1738 0.9080 0.9137 0.2630  0.1391  0.0771  102  LEU G CA  
19078 C  C   . LEU G 102  ? 1.1993 0.9279 0.9427 0.2525  0.1429  0.0758  102  LEU G C   
19079 O  O   . LEU G 102  ? 1.2153 0.9403 0.9569 0.2567  0.1447  0.0769  102  LEU G O   
19080 C  CB  . LEU G 102  ? 1.2020 0.9105 0.9158 0.2675  0.1455  0.0804  102  LEU G CB  
19081 C  CG  . LEU G 102  ? 1.2248 0.9303 0.9266 0.2834  0.1440  0.0832  102  LEU G CG  
19082 C  CD1 . LEU G 102  ? 1.2950 1.0033 0.9972 0.2943  0.1431  0.0847  102  LEU G CD1 
19083 C  CD2 . LEU G 102  ? 1.2758 1.0017 0.9898 0.2869  0.1363  0.0816  102  LEU G CD2 
19084 N  N   . ILE G 103  ? 1.3668 1.0951 1.1153 0.2390  0.1440  0.0734  103  ILE G N   
19085 C  CA  . ILE G 103  ? 1.2668 0.9906 1.0189 0.2286  0.1472  0.0718  103  ILE G CA  
19086 C  C   . ILE G 103  ? 1.2394 0.9834 1.0116 0.2287  0.1422  0.0700  103  ILE G C   
19087 O  O   . ILE G 103  ? 1.2428 0.9811 1.0131 0.2291  0.1448  0.0705  103  ILE G O   
19088 C  CB  . ILE G 103  ? 1.2905 1.0123 1.0453 0.2146  0.1487  0.0693  103  ILE G CB  
19089 C  CG1 . ILE G 103  ? 1.2463 0.9450 0.9796 0.2137  0.1553  0.0712  103  ILE G CG1 
19090 C  CG2 . ILE G 103  ? 1.3090 1.0303 1.0708 0.2040  0.1503  0.0669  103  ILE G CG2 
19091 C  CD1 . ILE G 103  ? 1.0879 0.7618 0.8016 0.2152  0.1627  0.0734  103  ILE G CD1 
19092 N  N   . VAL G 104  ? 1.3680 1.1351 1.1591 0.2283  0.1352  0.0680  104  VAL G N   
19093 C  CA  . VAL G 104  ? 1.3528 1.1394 1.1634 0.2284  0.1306  0.0663  104  VAL G CA  
19094 C  C   . VAL G 104  ? 1.4581 1.2466 1.2666 0.2412  0.1302  0.0686  104  VAL G C   
19095 O  O   . VAL G 104  ? 1.5033 1.3015 1.3230 0.2416  0.1290  0.0680  104  VAL G O   
19096 C  CB  . VAL G 104  ? 1.3152 1.1254 1.1460 0.2253  0.1233  0.0636  104  VAL G CB  
19097 C  CG1 . VAL G 104  ? 1.3470 1.1561 1.1802 0.2130  0.1237  0.0612  104  VAL G CG1 
19098 C  CG2 . VAL G 104  ? 1.4108 1.2289 1.2411 0.2359  0.1192  0.0646  104  VAL G CG2 
19099 N  N   . GLU G 105  ? 1.5594 1.3390 1.3537 0.2520  0.1312  0.0713  105  GLU G N   
19100 C  CA  . GLU G 105  ? 1.5974 1.3784 1.3887 0.2650  0.1310  0.0735  105  GLU G CA  
19101 C  C   . GLU G 105  ? 1.5625 1.3232 1.3388 0.2662  0.1379  0.0756  105  GLU G C   
19102 O  O   . GLU G 105  ? 1.5816 1.3483 1.3646 0.2696  0.1379  0.0757  105  GLU G O   
19103 C  CB  . GLU G 105  ? 1.5141 1.2925 1.2947 0.2769  0.1294  0.0755  105  GLU G CB  
19104 C  CG  . GLU G 105  ? 1.5679 1.3483 1.3449 0.2914  0.1288  0.0777  105  GLU G CG  
19105 C  CD  . GLU G 105  ? 1.6142 1.3915 1.3794 0.3036  0.1271  0.0796  105  GLU G CD  
19106 O  OE1 . GLU G 105  ? 1.6025 1.3751 1.3617 0.3006  0.1266  0.0794  105  GLU G OE1 
19107 O  OE2 . GLU G 105  ? 1.5309 1.3106 1.2929 0.3164  0.1262  0.0814  105  GLU G OE2 
19108 N  N   . ARG G 106  ? 1.3170 1.0534 1.0727 0.2635  0.1442  0.0771  106  ARG G N   
19109 C  CA  . ARG G 106  ? 1.3103 1.0255 1.0501 0.2645  0.1510  0.0789  106  ARG G CA  
19110 C  C   . ARG G 106  ? 1.3009 1.0155 1.0481 0.2520  0.1528  0.0765  106  ARG G C   
19111 O  O   . ARG G 106  ? 1.4138 1.1199 1.1559 0.2535  0.1563  0.0773  106  ARG G O   
19112 C  CB  . ARG G 106  ? 1.3879 1.0762 1.1023 0.2661  0.1573  0.0814  106  ARG G CB  
19113 C  CG  . ARG G 106  ? 1.4506 1.1315 1.1621 0.2535  0.1593  0.0797  106  ARG G CG  
19114 C  CD  . ARG G 106  ? 1.4742 1.1319 1.1620 0.2572  0.1647  0.0825  106  ARG G CD  
19115 N  NE  . ARG G 106  ? 1.5422 1.2029 1.2242 0.2719  0.1621  0.0851  106  ARG G NE  
19116 C  CZ  . ARG G 106  ? 1.4812 1.1232 1.1421 0.2787  0.1661  0.0880  106  ARG G CZ  
19117 N  NH1 . ARG G 106  ? 1.4187 1.0369 1.0621 0.2718  0.1733  0.0888  106  ARG G NH1 
19118 N  NH2 . ARG G 106  ? 1.3043 0.9516 0.9616 0.2926  0.1628  0.0900  106  ARG G NH2 
19119 N  N   . GLY G 107  ? 1.3729 1.0962 1.1315 0.2401  0.1505  0.0736  107  GLY G N   
19120 C  CA  . GLY G 107  ? 1.3856 1.1114 1.1532 0.2286  0.1511  0.0710  107  GLY G CA  
19121 C  C   . GLY G 107  ? 1.2914 0.9929 1.0420 0.2210  0.1580  0.0709  107  GLY G C   
19122 O  O   . GLY G 107  ? 1.2094 0.8897 0.9396 0.2252  0.1633  0.0733  107  GLY G O   
19123 N  N   . LEU G 108  ? 1.2537 0.9584 1.0128 0.2093  0.1579  0.0680  108  LEU G N   
19124 C  CA  . LEU G 108  ? 1.2641 0.9491 1.0107 0.2001  0.1636  0.0669  108  LEU G CA  
19125 C  C   . LEU G 108  ? 1.3491 1.0332 1.0988 0.1979  0.1646  0.0658  108  LEU G C   
19126 O  O   . LEU G 108  ? 1.4463 1.1489 1.2125 0.1995  0.1602  0.0650  108  LEU G O   
19127 C  CB  . LEU G 108  ? 1.1649 0.8539 0.9181 0.1871  0.1625  0.0637  108  LEU G CB  
19128 C  CG  . LEU G 108  ? 1.1480 0.8232 0.8876 0.1849  0.1661  0.0645  108  LEU G CG  
19129 C  CD1 . LEU G 108  ? 1.2390 0.9249 0.9820 0.1935  0.1624  0.0664  108  LEU G CD1 
19130 C  CD2 . LEU G 108  ? 1.1161 0.7924 0.8609 0.1706  0.1665  0.0610  108  LEU G CD2 
19131 N  N   . PRO G 109  ? 1.1797 0.8419 0.9132 0.1945  0.1706  0.0658  109  PRO G N   
19132 C  CA  . PRO G 109  ? 1.3104 0.9706 1.0457 0.1922  0.1716  0.0647  109  PRO G CA  
19133 C  C   . PRO G 109  ? 1.2050 0.8808 0.9579 0.1810  0.1676  0.0608  109  PRO G C   
19134 O  O   . PRO G 109  ? 1.1297 0.8064 0.8853 0.1711  0.1670  0.0584  109  PRO G O   
19135 C  CB  . PRO G 109  ? 1.3361 0.9679 1.0490 0.1893  0.1789  0.0650  109  PRO G CB  
19136 C  CG  . PRO G 109  ? 1.1864 0.8078 0.8895 0.1859  0.1813  0.0653  109  PRO G CG  
19137 C  CD  . PRO G 109  ? 1.1437 0.7807 0.8552 0.1939  0.1769  0.0673  109  PRO G CD  
19138 N  N   . VAL G 110  ? 1.6143 1.3026 1.3789 0.1830  0.1650  0.0603  110  VAL G N   
19139 C  CA  . VAL G 110  ? 1.7133 1.4174 1.4950 0.1741  0.1609  0.0570  110  VAL G CA  
19140 C  C   . VAL G 110  ? 1.7763 1.4722 1.5539 0.1715  0.1633  0.0559  110  VAL G C   
19141 O  O   . VAL G 110  ? 1.8950 1.5836 1.6650 0.1798  0.1660  0.0582  110  VAL G O   
19142 C  CB  . VAL G 110  ? 1.6235 1.3531 1.4255 0.1785  0.1547  0.0573  110  VAL G CB  
19143 C  CG1 . VAL G 110  ? 1.6544 1.3992 1.4730 0.1692  0.1507  0.0539  110  VAL G CG1 
19144 C  CG2 . VAL G 110  ? 1.4945 1.2313 1.2991 0.1820  0.1522  0.0583  110  VAL G CG2 
19145 N  N   . ARG G 111  ? 1.9467 1.6439 1.7289 0.1603  0.1623  0.0523  111  ARG G N   
19146 C  CA  . ARG G 111  ? 2.1670 1.8583 1.9467 0.1568  0.1638  0.0506  111  ARG G CA  
19147 C  C   . ARG G 111  ? 2.1498 1.8158 1.9080 0.1595  0.1702  0.0518  111  ARG G C   
19148 O  O   . ARG G 111  ? 2.0136 1.6645 1.7612 0.1513  0.1730  0.0495  111  ARG G O   
19149 C  CB  . ARG G 111  ? 2.1387 1.8460 1.9319 0.1627  0.1609  0.0516  111  ARG G CB  
19150 C  CG  . ARG G 111  ? 2.1162 1.8177 1.9065 0.1603  0.1624  0.0502  111  ARG G CG  
19151 C  CD  . ARG G 111  ? 2.1533 1.8634 1.9537 0.1491  0.1590  0.0462  111  ARG G CD  
19152 N  NE  . ARG G 111  ? 2.3870 2.0811 2.1755 0.1400  0.1615  0.0433  111  ARG G NE  
19153 C  CZ  . ARG G 111  ? 2.3884 2.0873 2.1832 0.1297  0.1590  0.0394  111  ARG G CZ  
19154 N  NH1 . ARG G 111  ? 2.3211 2.0396 2.1331 0.1272  0.1539  0.0380  111  ARG G NH1 
19155 N  NH2 . ARG G 111  ? 2.3252 2.0090 2.1086 0.1217  0.1616  0.0366  111  ARG G NH2 
19156 N  N   . VAL H 11   ? 1.3497 1.5117 1.2474 0.2870  0.0530  -0.1006 11   VAL I N   
19157 C  CA  . VAL H 11   ? 1.5139 1.6735 1.4196 0.2838  0.0443  -0.1022 11   VAL I CA  
19158 C  C   . VAL H 11   ? 1.4882 1.6388 1.3928 0.2780  0.0392  -0.1008 11   VAL I C   
19159 O  O   . VAL H 11   ? 1.5284 1.6840 1.4448 0.2703  0.0386  -0.0987 11   VAL I O   
19160 C  CB  . VAL H 11   ? 1.5285 1.6802 1.4269 0.2913  0.0378  -0.1066 11   VAL I CB  
19161 C  CG1 . VAL H 11   ? 1.4290 1.5736 1.3320 0.2877  0.0283  -0.1082 11   VAL I CG1 
19162 C  CG2 . VAL H 11   ? 1.5226 1.6850 1.4257 0.2961  0.0420  -0.1080 11   VAL I CG2 
19163 N  N   . LYS H 12   ? 2.1154 2.2531 2.0060 0.2818  0.0352  -0.1020 12   LYS I N   
19164 C  CA  . LYS H 12   ? 2.1939 2.3239 2.0825 0.2771  0.0311  -0.1005 12   LYS I CA  
19165 C  C   . LYS H 12   ? 2.2053 2.3412 2.0982 0.2712  0.0384  -0.0959 12   LYS I C   
19166 O  O   . LYS H 12   ? 2.1219 2.2568 2.0211 0.2646  0.0357  -0.0940 12   LYS I O   
19167 C  CB  . LYS H 12   ? 2.1723 2.2885 2.0439 0.2833  0.0263  -0.1028 12   LYS I CB  
19168 C  CG  . LYS H 12   ? 2.1854 2.2933 2.0529 0.2875  0.0175  -0.1075 12   LYS I CG  
19169 C  CD  . LYS H 12   ? 2.1946 2.3023 2.0741 0.2811  0.0105  -0.1082 12   LYS I CD  
19170 C  CE  . LYS H 12   ? 2.2819 2.3818 2.1579 0.2851  0.0029  -0.1130 12   LYS I CE  
19171 N  NZ  . LYS H 12   ? 2.2588 2.3457 2.1195 0.2902  -0.0026 -0.1161 12   LYS I NZ  
19172 N  N   . PRO H 13   ? 1.7618 1.9035 1.6514 0.2730  0.0479  -0.0939 13   PRO I N   
19173 C  CA  . PRO H 13   ? 1.6822 1.8300 1.5777 0.2663  0.0553  -0.0895 13   PRO I CA  
19174 C  C   . PRO H 13   ? 1.6697 1.8286 1.5832 0.2582  0.0559  -0.0882 13   PRO I C   
19175 O  O   . PRO H 13   ? 1.5512 1.7101 1.4697 0.2514  0.0567  -0.0854 13   PRO I O   
19176 C  CB  . PRO H 13   ? 1.7061 1.8591 1.5958 0.2704  0.0654  -0.0885 13   PRO I CB  
19177 C  CG  . PRO H 13   ? 1.7358 1.8791 1.6099 0.2797  0.0623  -0.0914 13   PRO I CG  
19178 C  CD  . PRO H 13   ? 1.7818 1.9213 1.6589 0.2815  0.0520  -0.0953 13   PRO I CD  
19179 N  N   . VAL H 14   ? 2.1192 2.2874 2.0424 0.2590  0.0555  -0.0903 14   VAL I N   
19180 C  CA  . VAL H 14   ? 2.0185 2.1978 1.9584 0.2516  0.0564  -0.0891 14   VAL I CA  
19181 C  C   . VAL H 14   ? 2.0083 2.1817 1.9533 0.2475  0.0475  -0.0896 14   VAL I C   
19182 O  O   . VAL H 14   ? 1.9746 2.1536 1.9311 0.2402  0.0479  -0.0877 14   VAL I O   
19183 C  CB  . VAL H 14   ? 2.0962 2.2880 2.0449 0.2542  0.0589  -0.0911 14   VAL I CB  
19184 C  CG1 . VAL H 14   ? 2.0683 2.2665 2.0122 0.2586  0.0680  -0.0908 14   VAL I CG1 
19185 C  CG2 . VAL H 14   ? 2.1364 2.3232 2.0833 0.2596  0.0506  -0.0949 14   VAL I CG2 
19186 N  N   . PHE H 15   ? 1.8831 2.0452 1.8198 0.2519  0.0395  -0.0923 15   PHE I N   
19187 C  CA  . PHE H 15   ? 1.8321 1.9877 1.7728 0.2477  0.0313  -0.0927 15   PHE I CA  
19188 C  C   . PHE H 15   ? 1.8290 1.9804 1.7684 0.2424  0.0320  -0.0895 15   PHE I C   
19189 O  O   . PHE H 15   ? 1.8125 1.9644 1.7606 0.2361  0.0290  -0.0882 15   PHE I O   
19190 C  CB  . PHE H 15   ? 1.8115 1.9556 1.7429 0.2535  0.0230  -0.0965 15   PHE I CB  
19191 C  CG  . PHE H 15   ? 1.7878 1.9288 1.7269 0.2502  0.0151  -0.0981 15   PHE I CG  
19192 C  CD1 . PHE H 15   ? 1.7686 1.9173 1.7189 0.2484  0.0149  -0.0986 15   PHE I CD1 
19193 C  CD2 . PHE H 15   ? 1.7771 1.9075 1.7119 0.2490  0.0079  -0.0991 15   PHE I CD2 
19194 C  CE1 . PHE H 15   ? 1.7569 1.9018 1.7133 0.2455  0.0081  -0.0998 15   PHE I CE1 
19195 C  CE2 . PHE H 15   ? 1.7494 1.8767 1.6912 0.2456  0.0011  -0.1005 15   PHE I CE2 
19196 C  CZ  . PHE H 15   ? 1.6943 1.8284 1.6467 0.2439  0.0014  -0.1007 15   PHE I CZ  
19197 N  N   . LEU H 16   ? 1.8125 1.9591 1.7402 0.2453  0.0361  -0.0881 16   LEU I N   
19198 C  CA  . LEU H 16   ? 1.7869 1.9295 1.7122 0.2409  0.0379  -0.0848 16   LEU I CA  
19199 C  C   . LEU H 16   ? 1.7879 1.9407 1.7242 0.2338  0.0456  -0.0813 16   LEU I C   
19200 O  O   . LEU H 16   ? 1.7120 1.8636 1.6527 0.2278  0.0452  -0.0788 16   LEU I O   
19201 C  CB  . LEU H 16   ? 1.7573 1.8916 1.6662 0.2466  0.0407  -0.0842 16   LEU I CB  
19202 C  CG  . LEU H 16   ? 1.7573 1.8840 1.6599 0.2442  0.0405  -0.0813 16   LEU I CG  
19203 C  CD1 . LEU H 16   ? 1.4773 1.5959 1.3790 0.2441  0.0301  -0.0833 16   LEU I CD1 
19204 C  CD2 . LEU H 16   ? 1.8805 2.0009 1.7669 0.2500  0.0458  -0.0802 16   LEU I CD2 
19205 N  N   . ALA H 17   ? 2.0081 2.1711 1.9488 0.2345  0.0525  -0.0813 17   ALA I N   
19206 C  CA  . ALA H 17   ? 1.9292 2.1028 1.8807 0.2275  0.0600  -0.0785 17   ALA I CA  
19207 C  C   . ALA H 17   ? 1.8790 2.0584 1.8453 0.2211  0.0558  -0.0786 17   ALA I C   
19208 O  O   . ALA H 17   ? 1.8142 1.9953 1.7867 0.2141  0.0579  -0.0759 17   ALA I O   
19209 C  CB  . ALA H 17   ? 1.8597 2.0441 1.8134 0.2300  0.0680  -0.0790 17   ALA I CB  
19210 N  N   . VAL H 18   ? 1.4019 1.5836 1.3732 0.2237  0.0499  -0.0817 18   VAL I N   
19211 C  CA  . VAL H 18   ? 1.2741 1.4599 1.2581 0.2183  0.0454  -0.0819 18   VAL I CA  
19212 C  C   . VAL H 18   ? 1.3132 1.4889 1.2957 0.2151  0.0388  -0.0810 18   VAL I C   
19213 O  O   . VAL H 18   ? 1.3550 1.5333 1.3476 0.2097  0.0360  -0.0804 18   VAL I O   
19214 C  CB  . VAL H 18   ? 1.2528 1.4422 1.2412 0.2224  0.0407  -0.0853 18   VAL I CB  
19215 C  CG1 . VAL H 18   ? 1.3361 1.5366 1.3267 0.2260  0.0469  -0.0864 18   VAL I CG1 
19216 C  CG2 . VAL H 18   ? 1.3154 1.4926 1.2934 0.2285  0.0333  -0.0880 18   VAL I CG2 
19217 N  N   . THR H 19   ? 1.6089 1.7736 1.5792 0.2187  0.0363  -0.0811 19   THR I N   
19218 C  CA  . THR H 19   ? 1.6103 1.7663 1.5791 0.2158  0.0306  -0.0802 19   THR I CA  
19219 C  C   . THR H 19   ? 1.5546 1.7108 1.5239 0.2103  0.0359  -0.0762 19   THR I C   
19220 O  O   . THR H 19   ? 1.4622 1.6184 1.4389 0.2045  0.0339  -0.0746 19   THR I O   
19221 C  CB  . THR H 19   ? 1.6227 1.7672 1.5782 0.2220  0.0251  -0.0823 19   THR I CB  
19222 O  OG1 . THR H 19   ? 1.5915 1.7347 1.5467 0.2265  0.0197  -0.0862 19   THR I OG1 
19223 C  CG2 . THR H 19   ? 1.4772 1.6140 1.4319 0.2190  0.0193  -0.0815 19   THR I CG2 
19224 N  N   . LEU H 20   ? 1.7750 1.9306 1.7360 0.2123  0.0430  -0.0744 20   LEU I N   
19225 C  CA  . LEU H 20   ? 1.7208 1.8758 1.6813 0.2072  0.0491  -0.0705 20   LEU I CA  
19226 C  C   . LEU H 20   ? 1.6198 1.7852 1.5946 0.1997  0.0531  -0.0691 20   LEU I C   
19227 O  O   . LEU H 20   ? 1.5091 1.6732 1.4878 0.1938  0.0540  -0.0665 20   LEU I O   
19228 C  CB  . LEU H 20   ? 1.7517 1.9045 1.7006 0.2108  0.0569  -0.0690 20   LEU I CB  
19229 C  CG  . LEU H 20   ? 1.7474 1.8875 1.6800 0.2163  0.0549  -0.0685 20   LEU I CG  
19230 C  CD1 . LEU H 20   ? 1.7177 1.8514 1.6461 0.2215  0.0447  -0.0721 20   LEU I CD1 
19231 C  CD2 . LEU H 20   ? 1.7565 1.8957 1.6780 0.2210  0.0629  -0.0676 20   LEU I CD2 
19232 N  N   . THR H 21   ? 1.3374 1.5134 1.3201 0.1999  0.0555  -0.0708 21   THR I N   
19233 C  CA  . THR H 21   ? 1.3361 1.5230 1.3330 0.1931  0.0584  -0.0701 21   THR I CA  
19234 C  C   . THR H 21   ? 1.3154 1.5003 1.3202 0.1888  0.0514  -0.0701 21   THR I C   
19235 O  O   . THR H 21   ? 1.2853 1.4736 1.2979 0.1820  0.0536  -0.0681 21   THR I O   
19236 C  CB  . THR H 21   ? 1.3334 1.5319 1.3372 0.1955  0.0602  -0.0727 21   THR I CB  
19237 O  OG1 . THR H 21   ? 1.3628 1.5640 1.3600 0.1990  0.0677  -0.0724 21   THR I OG1 
19238 C  CG2 . THR H 21   ? 1.3090 1.5192 1.3276 0.1888  0.0624  -0.0723 21   THR I CG2 
19239 N  N   . GLY H 22   ? 1.4120 1.5912 1.4148 0.1927  0.0431  -0.0724 22   GLY I N   
19240 C  CA  . GLY H 22   ? 1.3865 1.5637 1.3967 0.1888  0.0367  -0.0725 22   GLY I CA  
19241 C  C   . GLY H 22   ? 1.4173 1.5873 1.4252 0.1847  0.0361  -0.0697 22   GLY I C   
19242 O  O   . GLY H 22   ? 1.4047 1.5774 1.4210 0.1786  0.0364  -0.0680 22   GLY I O   
19243 N  N   . MET H 23   ? 1.8323 1.9930 1.8284 0.1884  0.0352  -0.0692 23   MET I N   
19244 C  CA  . MET H 23   ? 1.7941 1.9478 1.7871 0.1855  0.0342  -0.0665 23   MET I CA  
19245 C  C   . MET H 23   ? 1.8194 1.9760 1.8141 0.1801  0.0425  -0.0630 23   MET I C   
19246 O  O   . MET H 23   ? 1.8390 1.9938 1.8377 0.1751  0.0422  -0.0608 23   MET I O   
19247 C  CB  . MET H 23   ? 1.8249 1.9684 1.8041 0.1914  0.0314  -0.0670 23   MET I CB  
19248 C  CG  . MET H 23   ? 1.8876 2.0304 1.8563 0.1970  0.0362  -0.0675 23   MET I CG  
19249 S  SD  . MET H 23   ? 2.0180 2.1584 1.9789 0.1951  0.0462  -0.0631 23   MET I SD  
19250 C  CE  . MET H 23   ? 1.8706 1.9976 1.8175 0.1997  0.0412  -0.0624 23   MET I CE  
19251 N  N   . VAL H 24   ? 1.4112 1.5723 1.4030 0.1811  0.0501  -0.0625 24   VAL I N   
19252 C  CA  . VAL H 24   ? 1.4151 1.5802 1.4101 0.1752  0.0585  -0.0596 24   VAL I CA  
19253 C  C   . VAL H 24   ? 1.4181 1.5903 1.4271 0.1682  0.0577  -0.0594 24   VAL I C   
19254 O  O   . VAL H 24   ? 1.4233 1.5928 1.4342 0.1629  0.0593  -0.0568 24   VAL I O   
19255 C  CB  . VAL H 24   ? 1.4168 1.5884 1.4098 0.1768  0.0665  -0.0599 24   VAL I CB  
19256 C  CG1 . VAL H 24   ? 1.4122 1.5909 1.4128 0.1693  0.0746  -0.0578 24   VAL I CG1 
19257 C  CG2 . VAL H 24   ? 1.4176 1.5800 1.3949 0.1823  0.0695  -0.0587 24   VAL I CG2 
19258 N  N   . ALA H 25   ? 1.3859 1.5666 1.4042 0.1685  0.0546  -0.0621 25   ALA I N   
19259 C  CA  . ALA H 25   ? 1.3119 1.4996 1.3432 0.1624  0.0535  -0.0621 25   ALA I CA  
19260 C  C   . ALA H 25   ? 1.3555 1.5360 1.3881 0.1598  0.0477  -0.0610 25   ALA I C   
19261 O  O   . ALA H 25   ? 1.3670 1.5491 1.4059 0.1536  0.0494  -0.0592 25   ALA I O   
19262 C  CB  . ALA H 25   ? 1.3005 1.4970 1.3395 0.1648  0.0503  -0.0654 25   ALA I CB  
19263 N  N   . PHE H 26   ? 1.2615 1.4340 1.2884 0.1644  0.0408  -0.0621 26   PHE I N   
19264 C  CA  . PHE H 26   ? 1.2337 1.4001 1.2625 0.1622  0.0351  -0.0612 26   PHE I CA  
19265 C  C   . PHE H 26   ? 1.2330 1.3939 1.2578 0.1586  0.0388  -0.0577 26   PHE I C   
19266 O  O   . PHE H 26   ? 1.2733 1.4344 1.3044 0.1534  0.0384  -0.0562 26   PHE I O   
19267 C  CB  . PHE H 26   ? 1.2801 1.4392 1.3028 0.1679  0.0277  -0.0634 26   PHE I CB  
19268 C  CG  . PHE H 26   ? 1.2810 1.4361 1.3085 0.1657  0.0210  -0.0635 26   PHE I CG  
19269 C  CD1 . PHE H 26   ? 1.2547 1.4148 1.2929 0.1624  0.0186  -0.0643 26   PHE I CD1 
19270 C  CD2 . PHE H 26   ? 1.2993 1.4461 1.3206 0.1672  0.0171  -0.0629 26   PHE I CD2 
19271 C  CE1 . PHE H 26   ? 1.2692 1.4255 1.3118 0.1603  0.0130  -0.0643 26   PHE I CE1 
19272 C  CE2 . PHE H 26   ? 1.2645 1.4084 1.2910 0.1651  0.0113  -0.0631 26   PHE I CE2 
19273 C  CZ  . PHE H 26   ? 1.2852 1.4336 1.3223 0.1615  0.0094  -0.0637 26   PHE I CZ  
19274 N  N   . LEU H 27   ? 1.4087 1.5641 1.4224 0.1617  0.0425  -0.0564 27   LEU I N   
19275 C  CA  . LEU H 27   ? 1.4722 1.6214 1.4804 0.1590  0.0467  -0.0529 27   LEU I CA  
19276 C  C   . LEU H 27   ? 1.4474 1.6025 1.4635 0.1516  0.0531  -0.0511 27   LEU I C   
19277 O  O   . LEU H 27   ? 1.4870 1.6391 1.5056 0.1471  0.0533  -0.0490 27   LEU I O   
19278 C  CB  . LEU H 27   ? 1.4493 1.5926 1.4438 0.1637  0.0511  -0.0519 27   LEU I CB  
19279 C  CG  . LEU H 27   ? 1.4985 1.6362 1.4838 0.1715  0.0453  -0.0540 27   LEU I CG  
19280 C  CD1 . LEU H 27   ? 1.5107 1.6412 1.4813 0.1759  0.0502  -0.0523 27   LEU I CD1 
19281 C  CD2 . LEU H 27   ? 1.4969 1.6295 1.4833 0.1725  0.0365  -0.0549 27   LEU I CD2 
19282 N  N   . LEU H 28   ? 1.3174 1.4810 1.3373 0.1505  0.0585  -0.0521 28   LEU I N   
19283 C  CA  . LEU H 28   ? 1.3050 1.4764 1.3341 0.1435  0.0642  -0.0513 28   LEU I CA  
19284 C  C   . LEU H 28   ? 1.3099 1.4843 1.3498 0.1390  0.0594  -0.0517 28   LEU I C   
19285 O  O   . LEU H 28   ? 1.3305 1.5026 1.3727 0.1335  0.0616  -0.0496 28   LEU I O   
19286 C  CB  . LEU H 28   ? 1.2859 1.4680 1.3194 0.1445  0.0679  -0.0536 28   LEU I CB  
19287 C  CG  . LEU H 28   ? 1.3056 1.4855 1.3289 0.1479  0.0744  -0.0528 28   LEU I CG  
19288 C  CD1 . LEU H 28   ? 1.3085 1.5010 1.3392 0.1462  0.0800  -0.0545 28   LEU I CD1 
19289 C  CD2 . LEU H 28   ? 1.3139 1.4852 1.3290 0.1449  0.0806  -0.0491 28   LEU I CD2 
19290 N  N   . MET H 29   ? 1.4957 1.6746 1.5417 0.1415  0.0530  -0.0545 29   MET I N   
19291 C  CA  . MET H 29   ? 1.4762 1.6580 1.5321 0.1378  0.0485  -0.0550 29   MET I CA  
19292 C  C   . MET H 29   ? 1.5134 1.6858 1.5668 0.1364  0.0448  -0.0529 29   MET I C   
19293 O  O   . MET H 29   ? 1.4546 1.6274 1.5135 0.1311  0.0455  -0.0515 29   MET I O   
19294 C  CB  . MET H 29   ? 1.5069 1.6931 1.5674 0.1418  0.0425  -0.0582 29   MET I CB  
19295 C  CG  . MET H 29   ? 1.4659 1.6624 1.5298 0.1436  0.0456  -0.0605 29   MET I CG  
19296 S  SD  . MET H 29   ? 1.6017 1.8107 1.6796 0.1384  0.0466  -0.0617 29   MET I SD  
19297 C  CE  . MET H 29   ? 1.4828 1.6950 1.5618 0.1313  0.0559  -0.0594 29   MET I CE  
19298 N  N   . VAL H 30   ? 0.8353 0.9996 0.8805 0.1414  0.0407  -0.0529 30   VAL I N   
19299 C  CA  . VAL H 30   ? 0.8393 0.9956 0.8825 0.1408  0.0367  -0.0513 30   VAL I CA  
19300 C  C   . VAL H 30   ? 0.8509 1.0032 0.8911 0.1365  0.0424  -0.0479 30   VAL I C   
19301 O  O   . VAL H 30   ? 0.8884 1.0381 0.9322 0.1329  0.0410  -0.0464 30   VAL I O   
19302 C  CB  . VAL H 30   ? 0.7915 0.9407 0.8259 0.1472  0.0317  -0.0522 30   VAL I CB  
19303 C  CG1 . VAL H 30   ? 0.7790 0.9200 0.8092 0.1469  0.0295  -0.0500 30   VAL I CG1 
19304 C  CG2 . VAL H 30   ? 0.8320 0.9833 0.8707 0.1502  0.0248  -0.0555 30   VAL I CG2 
19305 N  N   . TRP H 31   ? 1.5011 1.6524 1.5343 0.1368  0.0493  -0.0466 31   TRP I N   
19306 C  CA  . TRP H 31   ? 1.5303 1.6769 1.5598 0.1326  0.0556  -0.0433 31   TRP I CA  
19307 C  C   . TRP H 31   ? 1.5356 1.6879 1.5756 0.1252  0.0578  -0.0430 31   TRP I C   
19308 O  O   . TRP H 31   ? 1.6083 1.7556 1.6485 0.1218  0.0581  -0.0408 31   TRP I O   
19309 C  CB  . TRP H 31   ? 1.5159 1.6615 1.5371 0.1337  0.0633  -0.0423 31   TRP I CB  
19310 C  CG  . TRP H 31   ? 1.5923 1.7311 1.6073 0.1299  0.0704  -0.0389 31   TRP I CG  
19311 C  CD1 . TRP H 31   ? 1.5872 1.7206 1.6028 0.1262  0.0704  -0.0366 31   TRP I CD1 
19312 C  CD2 . TRP H 31   ? 1.6318 1.7680 1.6387 0.1297  0.0789  -0.0373 31   TRP I CD2 
19313 N  NE1 . TRP H 31   ? 1.6199 1.7469 1.6278 0.1236  0.0783  -0.0337 31   TRP I NE1 
19314 C  CE2 . TRP H 31   ? 1.6344 1.7629 1.6369 0.1255  0.0838  -0.0340 31   TRP I CE2 
19315 C  CE3 . TRP H 31   ? 1.6084 1.7478 1.6110 0.1326  0.0833  -0.0382 31   TRP I CE3 
19316 C  CZ2 . TRP H 31   ? 1.6361 1.7594 1.6298 0.1240  0.0929  -0.0316 31   TRP I CZ2 
19317 C  CZ3 . TRP H 31   ? 1.6571 1.7918 1.6514 0.1311  0.0924  -0.0358 31   TRP I CZ3 
19318 C  CH2 . TRP H 31   ? 1.6539 1.7805 1.6438 0.1267  0.0972  -0.0325 31   TRP I CH2 
19319 N  N   . LEU H 32   ? 1.0189 1.1816 1.0675 0.1231  0.0590  -0.0452 32   LEU I N   
19320 C  CA  . LEU H 32   ? 1.0670 1.2360 1.1254 0.1163  0.0614  -0.0453 32   LEU I CA  
19321 C  C   . LEU H 32   ? 1.0668 1.2341 1.1311 0.1147  0.0552  -0.0452 32   LEU I C   
19322 O  O   . LEU H 32   ? 1.0878 1.2532 1.1547 0.1095  0.0570  -0.0436 32   LEU I O   
19323 C  CB  . LEU H 32   ? 1.0781 1.2596 1.1446 0.1155  0.0629  -0.0482 32   LEU I CB  
19324 C  CG  . LEU H 32   ? 1.0452 1.2349 1.1228 0.1090  0.0642  -0.0490 32   LEU I CG  
19325 C  CD1 . LEU H 32   ? 1.0367 1.2237 1.1126 0.1025  0.0716  -0.0468 32   LEU I CD1 
19326 C  CD2 . LEU H 32   ? 1.0419 1.2446 1.1273 0.1096  0.0647  -0.0522 32   LEU I CD2 
19327 N  N   . PHE H 33   ? 1.1142 1.2819 1.1804 0.1190  0.0480  -0.0470 33   PHE I N   
19328 C  CA  . PHE H 33   ? 1.1141 1.2811 1.1867 0.1176  0.0423  -0.0472 33   PHE I CA  
19329 C  C   . PHE H 33   ? 1.2099 1.3671 1.2773 0.1191  0.0390  -0.0452 33   PHE I C   
19330 O  O   . PHE H 33   ? 1.2042 1.3602 1.2766 0.1181  0.0344  -0.0453 33   PHE I O   
19331 C  CB  . PHE H 33   ? 1.1247 1.2969 1.2025 0.1211  0.0366  -0.0503 33   PHE I CB  
19332 C  CG  . PHE H 33   ? 1.1197 1.3022 1.2026 0.1207  0.0392  -0.0525 33   PHE I CG  
19333 C  CD1 . PHE H 33   ? 1.0944 1.2839 1.1846 0.1153  0.0427  -0.0525 33   PHE I CD1 
19334 C  CD2 . PHE H 33   ? 1.1105 1.2961 1.1912 0.1260  0.0380  -0.0547 33   PHE I CD2 
19335 C  CE1 . PHE H 33   ? 1.1200 1.3203 1.2157 0.1151  0.0449  -0.0548 33   PHE I CE1 
19336 C  CE2 . PHE H 33   ? 1.1517 1.3475 1.2374 0.1261  0.0405  -0.0568 33   PHE I CE2 
19337 C  CZ  . PHE H 33   ? 1.1749 1.3785 1.2685 0.1207  0.0438  -0.0569 33   PHE I CZ  
19338 N  N   . ALA H 34   ? 1.3640 1.5143 1.4216 0.1216  0.0412  -0.0435 34   ALA I N   
19339 C  CA  . ALA H 34   ? 1.2886 1.4302 1.3412 0.1235  0.0380  -0.0418 34   ALA I CA  
19340 C  C   . ALA H 34   ? 1.3446 1.4794 1.3895 0.1217  0.0438  -0.0385 34   ALA I C   
19341 O  O   . ALA H 34   ? 1.4478 1.5807 1.4955 0.1172  0.0458  -0.0367 34   ALA I O   
19342 C  CB  . ALA H 34   ? 1.2477 1.3862 1.2944 0.1302  0.0329  -0.0433 34   ALA I CB  
19343 N  N   . PHE H 35   ? 2.0439 2.1743 2.0786 0.1254  0.0468  -0.0377 35   PHE I N   
19344 C  CA  . PHE H 35   ? 2.0872 2.2091 2.1123 0.1249  0.0522  -0.0344 35   PHE I CA  
19345 C  C   . PHE H 35   ? 2.1001 2.2238 2.1246 0.1200  0.0610  -0.0333 35   PHE I C   
19346 O  O   . PHE H 35   ? 2.1101 2.2292 2.1251 0.1215  0.0665  -0.0319 35   PHE I O   
19347 C  CB  . PHE H 35   ? 2.0633 2.1785 2.0766 0.1319  0.0507  -0.0339 35   PHE I CB  
19348 C  CG  . PHE H 35   ? 2.0821 2.1986 2.0972 0.1369  0.0421  -0.0365 35   PHE I CG  
19349 C  CD1 . PHE H 35   ? 2.0687 2.1843 2.0890 0.1368  0.0360  -0.0367 35   PHE I CD1 
19350 C  CD2 . PHE H 35   ? 2.1256 2.2443 2.1373 0.1417  0.0403  -0.0389 35   PHE I CD2 
19351 C  CE1 . PHE H 35   ? 2.0721 2.1889 2.0944 0.1408  0.0283  -0.0393 35   PHE I CE1 
19352 C  CE2 . PHE H 35   ? 2.0845 2.2039 2.0977 0.1459  0.0325  -0.0415 35   PHE I CE2 
19353 C  CZ  . PHE H 35   ? 2.0740 2.1926 2.0927 0.1453  0.0265  -0.0418 35   PHE I CZ  
19354 N  N   . TYR H 36   ? 1.4288 1.5592 1.4635 0.1139  0.0625  -0.0341 36   TYR I N   
19355 C  CA  . TYR H 36   ? 1.3941 1.5277 1.4303 0.1082  0.0705  -0.0337 36   TYR I CA  
19356 C  C   . TYR H 36   ? 1.4284 1.5595 1.4683 0.1018  0.0728  -0.0320 36   TYR I C   
19357 O  O   . TYR H 36   ? 1.4423 1.5653 1.4746 0.0996  0.0785  -0.0293 36   TYR I O   
19358 C  CB  . TYR H 36   ? 1.3915 1.5375 1.4369 0.1070  0.0704  -0.0369 36   TYR I CB  
19359 C  CG  . TYR H 36   ? 1.4254 1.5762 1.4724 0.1018  0.0788  -0.0370 36   TYR I CG  
19360 C  CD1 . TYR H 36   ? 1.3867 1.5327 1.4240 0.1029  0.0856  -0.0354 36   TYR I CD1 
19361 C  CD2 . TYR H 36   ? 1.3880 1.5482 1.4461 0.0958  0.0801  -0.0387 36   TYR I CD2 
19362 C  CE1 . TYR H 36   ? 1.3364 1.4870 1.3756 0.0978  0.0937  -0.0356 36   TYR I CE1 
19363 C  CE2 . TYR H 36   ? 1.3839 1.5494 1.4444 0.0907  0.0877  -0.0392 36   TYR I CE2 
19364 C  CZ  . TYR H 36   ? 1.3530 1.5137 1.4042 0.0914  0.0946  -0.0376 36   TYR I CZ  
19365 O  OH  . TYR H 36   ? 1.4490 1.6151 1.5030 0.0859  0.1027  -0.0381 36   TYR I OH  
19366 N  N   . TRP H 37   ? 2.3270 2.4642 2.3774 0.0988  0.0687  -0.0336 37   TRP I N   
19367 C  CA  . TRP H 37   ? 2.3565 2.4918 2.4109 0.0929  0.0702  -0.0324 37   TRP I CA  
19368 C  C   . TRP H 37   ? 2.3646 2.5008 2.4188 0.0864  0.0786  -0.0320 37   TRP I C   
19369 O  O   . TRP H 37   ? 2.4123 2.5393 2.4581 0.0848  0.0840  -0.0293 37   TRP I O   
19370 C  CB  . TRP H 37   ? 2.2732 2.3971 2.3204 0.0948  0.0687  -0.0295 37   TRP I CB  
19371 C  CG  . TRP H 37   ? 2.2929 2.4152 2.3388 0.1013  0.0612  -0.0299 37   TRP I CG  
19372 C  CD1 . TRP H 37   ? 2.2629 2.3905 2.3171 0.1026  0.0543  -0.0319 37   TRP I CD1 
19373 C  CD2 . TRP H 37   ? 2.3444 2.4592 2.3801 0.1074  0.0599  -0.0285 37   TRP I CD2 
19374 N  NE1 . TRP H 37   ? 2.2706 2.3947 2.3210 0.1086  0.0489  -0.0319 37   TRP I NE1 
19375 C  CE2 . TRP H 37   ? 2.3697 2.4864 2.4089 0.1118  0.0519  -0.0300 37   TRP I CE2 
19376 C  CE3 . TRP H 37   ? 2.3461 2.4526 2.3696 0.1098  0.0648  -0.0262 37   TRP I CE3 
19377 C  CZ2 . TRP H 37   ? 2.3214 2.4328 2.3530 0.1181  0.0483  -0.0296 37   TRP I CZ2 
19378 C  CZ3 . TRP H 37   ? 2.3756 2.4765 2.3909 0.1167  0.0611  -0.0255 37   TRP I CZ3 
19379 C  CH2 . TRP H 37   ? 2.3470 2.4508 2.3668 0.1207  0.0527  -0.0274 37   TRP I CH2 
19380 FE FE  . HEC I .    ? 0.7345 0.8827 0.8600 0.0777  0.0259  -0.0370 301  HEC A FE  
19381 C  CHA . HEC I .    ? 0.7158 0.8788 0.8435 0.0703  0.0339  -0.0412 301  HEC A CHA 
19382 C  CHB . HEC I .    ? 0.6840 0.8450 0.8198 0.0827  0.0176  -0.0422 301  HEC A CHB 
19383 C  CHC . HEC I .    ? 0.6602 0.7967 0.7869 0.0840  0.0185  -0.0337 301  HEC A CHC 
19384 C  CHD . HEC I .    ? 0.7212 0.8526 0.8343 0.0732  0.0346  -0.0311 301  HEC A CHD 
19385 N  NA  . HEC I .    ? 0.7225 0.8828 0.8537 0.0766  0.0254  -0.0410 301  HEC A NA  
19386 C  C1A . HEC I .    ? 0.7111 0.8771 0.8425 0.0740  0.0290  -0.0424 301  HEC A C1A 
19387 C  C2A . HEC I .    ? 0.6936 0.8689 0.8294 0.0758  0.0269  -0.0454 301  HEC A C2A 
19388 C  C3A . HEC I .    ? 0.6890 0.8632 0.8264 0.0795  0.0224  -0.0456 301  HEC A C3A 
19389 C  C4A . HEC I .    ? 0.7037 0.8686 0.8385 0.0798  0.0214  -0.0428 301  HEC A C4A 
19390 C  CMA . HEC I .    ? 0.6667 0.8483 0.8078 0.0831  0.0189  -0.0483 301  HEC A CMA 
19391 C  CAA . HEC I .    ? 0.6772 0.8622 0.8156 0.0739  0.0297  -0.0479 301  HEC A CAA 
19392 C  CBA . HEC I .    ? 0.6782 0.8684 0.8207 0.0700  0.0300  -0.0496 301  HEC A CBA 
19393 C  CGA . HEC I .    ? 0.6967 0.8989 0.8439 0.0691  0.0313  -0.0529 301  HEC A CGA 
19394 O  O1A . HEC I .    ? 0.7114 0.9169 0.8578 0.0706  0.0332  -0.0535 301  HEC A O1A 
19395 O  O2A . HEC I .    ? 0.7053 0.9140 0.8569 0.0671  0.0303  -0.0551 301  HEC A O2A 
19396 N  NB  . HEC I .    ? 0.7082 0.8563 0.8383 0.0822  0.0193  -0.0377 301  HEC A NB  
19397 C  C1B . HEC I .    ? 0.6872 0.8405 0.8210 0.0836  0.0167  -0.0399 301  HEC A C1B 
19398 C  C2B . HEC I .    ? 0.6480 0.7974 0.7831 0.0863  0.0130  -0.0394 301  HEC A C2B 
19399 C  C3B . HEC I .    ? 0.6385 0.7818 0.7719 0.0863  0.0133  -0.0372 301  HEC A C3B 
19400 C  C4B . HEC I .    ? 0.6680 0.8102 0.7978 0.0841  0.0171  -0.0360 301  HEC A C4B 
19401 C  CMB . HEC I .    ? 0.6117 0.7638 0.7497 0.0889  0.0096  -0.0412 301  HEC A CMB 
19402 C  CAB . HEC I .    ? 0.5871 0.7252 0.7218 0.0883  0.0103  -0.0361 301  HEC A CAB 
19403 C  CBB . HEC I .    ? 0.6024 0.7417 0.7379 0.0920  0.0070  -0.0378 301  HEC A CBB 
19404 N  NC  . HEC I .    ? 0.7224 0.8591 0.8436 0.0784  0.0262  -0.0330 301  HEC A NC  
19405 C  C1C . HEC I .    ? 0.6907 0.8246 0.8132 0.0818  0.0225  -0.0323 301  HEC A C1C 
19406 C  C2C . HEC I .    ? 0.6837 0.8116 0.8019 0.0828  0.0237  -0.0300 301  HEC A C2C 
19407 C  C3C . HEC I .    ? 0.6964 0.8220 0.8104 0.0800  0.0282  -0.0290 301  HEC A C3C 
19408 C  C4C . HEC I .    ? 0.7197 0.8510 0.8357 0.0770  0.0300  -0.0310 301  HEC A C4C 
19409 C  CMC . HEC I .    ? 0.6329 0.7570 0.7520 0.0858  0.0205  -0.0288 301  HEC A CMC 
19410 C  CAC . HEC I .    ? 0.6524 0.7707 0.7601 0.0806  0.0308  -0.0263 301  HEC A CAC 
19411 C  CBC . HEC I .    ? 0.6387 0.7513 0.7452 0.0781  0.0329  -0.0242 301  HEC A CBC 
19412 N  ND  . HEC I .    ? 0.7389 0.8855 0.8598 0.0721  0.0332  -0.0361 301  HEC A ND  
19413 C  C1D . HEC I .    ? 0.7312 0.8697 0.8466 0.0710  0.0362  -0.0335 301  HEC A C1D 
19414 C  C2D . HEC I .    ? 0.7187 0.8576 0.8310 0.0673  0.0415  -0.0337 301  HEC A C2D 
19415 C  C3D . HEC I .    ? 0.7177 0.8672 0.8353 0.0660  0.0413  -0.0370 301  HEC A C3D 
19416 C  C4D . HEC I .    ? 0.7299 0.8836 0.8524 0.0695  0.0359  -0.0383 301  HEC A C4D 
19417 C  CMD . HEC I .    ? 0.6960 0.8263 0.8009 0.0652  0.0465  -0.0312 301  HEC A CMD 
19418 C  CAD . HEC I .    ? 0.7005 0.8552 0.8184 0.0618  0.0462  -0.0386 301  HEC A CAD 
19419 C  CBD . HEC I .    ? 0.7023 0.8625 0.8202 0.0649  0.0463  -0.0398 301  HEC A CBD 
19420 C  CGD . HEC I .    ? 0.7042 0.8686 0.8216 0.0608  0.0520  -0.0410 301  HEC A CGD 
19421 O  O1D . HEC I .    ? 0.7053 0.8682 0.8227 0.0552  0.0557  -0.0411 301  HEC A O1D 
19422 O  O2D . HEC I .    ? 0.7180 0.8871 0.8352 0.0630  0.0531  -0.0420 301  HEC A O2D 
19423 FE FE  . HEC J .    ? 0.8161 0.9009 0.8975 0.0838  0.0420  -0.0146 302  HEC A FE  
19424 C  CHA . HEC J .    ? 0.7934 0.8750 0.8828 0.0875  0.0370  -0.0116 302  HEC A CHA 
19425 C  CHB . HEC J .    ? 0.8165 0.9095 0.9097 0.0731  0.0427  -0.0183 302  HEC A CHB 
19426 C  CHC . HEC J .    ? 0.8358 0.9254 0.9105 0.0796  0.0488  -0.0175 302  HEC A CHC 
19427 C  CHD . HEC J .    ? 0.8321 0.9060 0.8968 0.0952  0.0425  -0.0105 302  HEC A CHD 
19428 N  NA  . HEC J .    ? 0.8032 0.8896 0.8928 0.0808  0.0401  -0.0147 302  HEC A NA  
19429 C  C1A . HEC J .    ? 0.7933 0.8769 0.8844 0.0829  0.0386  -0.0131 302  HEC A C1A 
19430 C  C2A . HEC J .    ? 0.7888 0.8724 0.8836 0.0796  0.0389  -0.0133 302  HEC A C2A 
19431 C  C3A . HEC J .    ? 0.7952 0.8819 0.8908 0.0758  0.0402  -0.0153 302  HEC A C3A 
19432 C  C4A . HEC J .    ? 0.8079 0.8967 0.9007 0.0763  0.0411  -0.0162 302  HEC A C4A 
19433 C  CMA . HEC J .    ? 0.7958 0.8838 0.8946 0.0717  0.0406  -0.0164 302  HEC A CMA 
19434 C  CAA . HEC J .    ? 0.7695 0.8505 0.8669 0.0804  0.0381  -0.0118 302  HEC A CAA 
19435 C  CBA . HEC J .    ? 0.7587 0.8445 0.8628 0.0838  0.0334  -0.0123 302  HEC A CBA 
19436 C  CGA . HEC J .    ? 0.7423 0.8294 0.8522 0.0826  0.0320  -0.0124 302  HEC A CGA 
19437 O  O1A . HEC J .    ? 0.7399 0.8298 0.8554 0.0848  0.0289  -0.0125 302  HEC A O1A 
19438 O  O2A . HEC J .    ? 0.7450 0.8300 0.8537 0.0792  0.0341  -0.0126 302  HEC A O2A 
19439 N  NB  . HEC J .    ? 0.8248 0.9151 0.9086 0.0772  0.0452  -0.0173 302  HEC A NB  
19440 C  C1B . HEC J .    ? 0.8252 0.9194 0.9149 0.0735  0.0444  -0.0189 302  HEC A C1B 
19441 C  C2B . HEC J .    ? 0.8330 0.9331 0.9245 0.0705  0.0459  -0.0213 302  HEC A C2B 
19442 C  C3B . HEC J .    ? 0.8329 0.9323 0.9196 0.0720  0.0479  -0.0210 302  HEC A C3B 
19443 C  C4B . HEC J .    ? 0.8325 0.9253 0.9139 0.0764  0.0474  -0.0185 302  HEC A C4B 
19444 C  CMB . HEC J .    ? 0.8411 0.9475 0.9388 0.0665  0.0452  -0.0237 302  HEC A CMB 
19445 C  CAB . HEC J .    ? 0.8357 0.9406 0.9226 0.0699  0.0504  -0.0231 302  HEC A CAB 
19446 C  CBB . HEC J .    ? 0.8455 0.9481 0.9300 0.0638  0.0560  -0.0233 302  HEC A CBB 
19447 N  NC  . HEC J .    ? 0.8289 0.9101 0.8999 0.0865  0.0453  -0.0139 302  HEC A NC  
19448 C  C1C . HEC J .    ? 0.8376 0.9216 0.9071 0.0843  0.0478  -0.0153 302  HEC A C1C 
19449 C  C2C . HEC J .    ? 0.8523 0.9319 0.9133 0.0879  0.0496  -0.0141 302  HEC A C2C 
19450 C  C3C . HEC J .    ? 0.8435 0.9194 0.9020 0.0927  0.0471  -0.0124 302  HEC A C3C 
19451 C  C4C . HEC J .    ? 0.8337 0.9104 0.8985 0.0916  0.0448  -0.0121 302  HEC A C4C 
19452 C  CMC . HEC J .    ? 0.8659 0.9477 0.9234 0.0873  0.0523  -0.0153 302  HEC A CMC 
19453 C  CAC . HEC J .    ? 0.8439 0.9148 0.8934 0.0985  0.0471  -0.0109 302  HEC A CAC 
19454 C  CBC . HEC J .    ? 0.8629 0.9239 0.9011 0.0973  0.0540  -0.0084 302  HEC A CBC 
19455 N  ND  . HEC J .    ? 0.8161 0.8954 0.8945 0.0901  0.0397  -0.0116 302  HEC A ND  
19456 C  C1D . HEC J .    ? 0.8251 0.9003 0.8962 0.0944  0.0404  -0.0103 302  HEC A C1D 
19457 C  C2D . HEC J .    ? 0.8287 0.9014 0.8998 0.0982  0.0385  -0.0085 302  HEC A C2D 
19458 C  C3D . HEC J .    ? 0.8107 0.8860 0.8901 0.0955  0.0371  -0.0088 302  HEC A C3D 
19459 C  C4D . HEC J .    ? 0.8031 0.8820 0.8860 0.0907  0.0379  -0.0108 302  HEC A C4D 
19460 C  CMD . HEC J .    ? 0.8406 0.9090 0.9048 0.1041  0.0381  -0.0067 302  HEC A CMD 
19461 C  CAD . HEC J .    ? 0.7923 0.8668 0.8752 0.0978  0.0354  -0.0074 302  HEC A CAD 
19462 C  CBD . HEC J .    ? 0.7832 0.8657 0.8763 0.0985  0.0301  -0.0094 302  HEC A CBD 
19463 C  CGD . HEC J .    ? 0.7653 0.8474 0.8631 0.0992  0.0294  -0.0081 302  HEC A CGD 
19464 O  O1D . HEC J .    ? 0.7705 0.8583 0.8767 0.0998  0.0256  -0.0094 302  HEC A O1D 
19465 O  O2D . HEC J .    ? 0.7628 0.8387 0.8558 0.0992  0.0328  -0.0058 302  HEC A O2D 
19466 FE FE  . HEC K .    ? 0.7622 0.7915 0.7889 0.0485  0.0918  -0.0093 303  HEC A FE  
19467 C  CHA . HEC K .    ? 0.7433 0.7944 0.7894 0.0326  0.0930  -0.0181 303  HEC A CHA 
19468 C  CHB . HEC K .    ? 0.8061 0.8047 0.8091 0.0384  0.1087  -0.0061 303  HEC A CHB 
19469 C  CHC . HEC K .    ? 0.7388 0.7497 0.7484 0.0657  0.0888  -0.0014 303  HEC A CHC 
19470 C  CHD . HEC K .    ? 0.6983 0.7535 0.7426 0.0587  0.0783  -0.0124 303  HEC A CHD 
19471 N  NA  . HEC K .    ? 0.7809 0.8069 0.8061 0.0370  0.0997  -0.0117 303  HEC A NA  
19472 C  C1A . HEC K .    ? 0.7681 0.8048 0.8033 0.0312  0.0984  -0.0155 303  HEC A C1A 
19473 C  C2A . HEC K .    ? 0.7842 0.8140 0.8158 0.0238  0.1038  -0.0164 303  HEC A C2A 
19474 C  C3A . HEC K .    ? 0.8005 0.8151 0.8199 0.0252  0.1084  -0.0131 303  HEC A C3A 
19475 C  C4A . HEC K .    ? 0.7971 0.8093 0.8123 0.0338  0.1058  -0.0100 303  HEC A C4A 
19476 C  CMA . HEC K .    ? 0.8165 0.8179 0.8274 0.0189  0.1151  -0.0127 303  HEC A CMA 
19477 C  CAA . HEC K .    ? 0.7669 0.8054 0.8071 0.0159  0.1040  -0.0208 303  HEC A CAA 
19478 C  CBA . HEC K .    ? 0.7732 0.8092 0.8151 0.0147  0.1011  -0.0214 303  HEC A CBA 
19479 C  CGA . HEC K .    ? 0.7567 0.8008 0.8057 0.0207  0.0934  -0.0213 303  HEC A CGA 
19480 O  O1A . HEC K .    ? 0.7320 0.7882 0.7888 0.0229  0.0898  -0.0229 303  HEC A O1A 
19481 O  O2A . HEC K .    ? 0.7490 0.7873 0.7958 0.0233  0.0912  -0.0197 303  HEC A O2A 
19482 N  NB  . HEC K .    ? 0.7710 0.7790 0.7795 0.0520  0.0979  -0.0042 303  HEC A NB  
19483 C  C1B . HEC K .    ? 0.7917 0.7885 0.7924 0.0468  0.1044  -0.0035 303  HEC A C1B 
19484 C  C2B . HEC K .    ? 0.7890 0.7726 0.7792 0.0515  0.1058  0.0001  303  HEC A C2B 
19485 C  C3B . HEC K .    ? 0.7661 0.7538 0.7586 0.0592  0.1002  0.0013  303  HEC A C3B 
19486 C  C4B . HEC K .    ? 0.7573 0.7601 0.7613 0.0594  0.0952  -0.0014 303  HEC A C4B 
19487 C  CMB . HEC K .    ? 0.8065 0.7738 0.7849 0.0483  0.1126  0.0020  303  HEC A CMB 
19488 C  CAB . HEC K .    ? 0.7616 0.7397 0.7459 0.0666  0.0994  0.0049  303  HEC A CAB 
19489 C  CBB . HEC K .    ? 0.7843 0.7614 0.7628 0.0742  0.0982  0.0068  303  HEC A CBB 
19490 N  NC  . HEC K .    ? 0.7287 0.7613 0.7557 0.0597  0.0850  -0.0072 303  HEC A NC  
19491 C  C1C . HEC K .    ? 0.7223 0.7465 0.7424 0.0656  0.0842  -0.0042 303  HEC A C1C 
19492 C  C2C . HEC K .    ? 0.6938 0.7253 0.7186 0.0719  0.0781  -0.0043 303  HEC A C2C 
19493 C  C3C . HEC K .    ? 0.6771 0.7202 0.7117 0.0698  0.0749  -0.0073 303  HEC A C3C 
19494 C  C4C . HEC K .    ? 0.7038 0.7482 0.7397 0.0624  0.0793  -0.0092 303  HEC A C4C 
19495 C  CMC . HEC K .    ? 0.6574 0.6850 0.6791 0.0792  0.0747  -0.0019 303  HEC A CMC 
19496 C  CAC . HEC K .    ? 0.6370 0.6899 0.6792 0.0747  0.0680  -0.0087 303  HEC A CAC 
19497 C  CBC . HEC K .    ? 0.6343 0.6943 0.6782 0.0749  0.0678  -0.0106 303  HEC A CBC 
19498 N  ND  . HEC K .    ? 0.7289 0.7786 0.7713 0.0461  0.0868  -0.0142 303  HEC A ND  
19499 C  C1D . HEC K .    ? 0.7051 0.7634 0.7533 0.0516  0.0809  -0.0147 303  HEC A C1D 
19500 C  C2D . HEC K .    ? 0.6817 0.7526 0.7406 0.0488  0.0779  -0.0183 303  HEC A C2D 
19501 C  C3D . HEC K .    ? 0.6841 0.7546 0.7440 0.0409  0.0822  -0.0201 303  HEC A C3D 
19502 C  C4D . HEC K .    ? 0.7208 0.7775 0.7700 0.0394  0.0877  -0.0174 303  HEC A C4D 
19503 C  CMD . HEC K .    ? 0.6264 0.7086 0.6938 0.0529  0.0715  -0.0200 303  HEC A CMD 
19504 C  CAD . HEC K .    ? 0.6498 0.7321 0.7196 0.0358  0.0808  -0.0242 303  HEC A CAD 
19505 C  CBD . HEC K .    ? 0.6445 0.7258 0.7174 0.0338  0.0782  -0.0249 303  HEC A CBD 
19506 C  CGD . HEC K .    ? 0.6112 0.7044 0.6935 0.0297  0.0761  -0.0290 303  HEC A CGD 
19507 O  O1D . HEC K .    ? 0.6047 0.6985 0.6901 0.0284  0.0734  -0.0300 303  HEC A O1D 
19508 O  O2D . HEC K .    ? 0.6004 0.7025 0.6870 0.0279  0.0772  -0.0313 303  HEC A O2D 
19509 FE FE  . HEC L .    ? 0.8938 0.8430 0.8579 0.0132  0.1439  -0.0041 304  HEC A FE  
19510 C  CHA . HEC L .    ? 0.8518 0.8410 0.8500 -0.0010 0.1385  -0.0152 304  HEC A CHA 
19511 C  CHB . HEC L .    ? 0.8387 0.8125 0.8160 0.0324  0.1275  -0.0026 304  HEC A CHB 
19512 C  CHC . HEC L .    ? 0.9190 0.8286 0.8467 0.0295  0.1501  0.0070  304  HEC A CHC 
19513 C  CHD . HEC L .    ? 0.9305 0.8537 0.8824 -0.0062 0.1576  -0.0066 304  HEC A CHD 
19514 N  NA  . HEC L .    ? 0.8523 0.8283 0.8363 0.0154  0.1346  -0.0079 304  HEC A NA  
19515 C  C1A . HEC L .    ? 0.8412 0.8309 0.8369 0.0086  0.1342  -0.0122 304  HEC A C1A 
19516 C  C2A . HEC L .    ? 0.8070 0.8117 0.8120 0.0134  0.1284  -0.0133 304  HEC A C2A 
19517 C  C3A . HEC L .    ? 0.8042 0.8042 0.8033 0.0223  0.1255  -0.0099 304  HEC A C3A 
19518 C  C4A . HEC L .    ? 0.8387 0.8211 0.8248 0.0238  0.1292  -0.0065 304  HEC A C4A 
19519 C  CMA . HEC L .    ? 0.7773 0.7884 0.7823 0.0296  0.1191  -0.0100 304  HEC A CMA 
19520 C  CAA . HEC L .    ? 0.7592 0.7823 0.7782 0.0095  0.1259  -0.0177 304  HEC A CAA 
19521 C  CBA . HEC L .    ? 0.7576 0.7885 0.7865 0.0047  0.1220  -0.0213 304  HEC A CBA 
19522 C  CGA . HEC L .    ? 0.7082 0.7580 0.7509 0.0049  0.1167  -0.0249 304  HEC A CGA 
19523 O  O1A . HEC L .    ? 0.7074 0.7657 0.7589 0.0003  0.1141  -0.0284 304  HEC A O1A 
19524 O  O2A . HEC L .    ? 0.6813 0.7371 0.7255 0.0099  0.1150  -0.0243 304  HEC A O2A 
19525 N  NB  . HEC L .    ? 0.8815 0.8251 0.8366 0.0280  0.1393  0.0012  304  HEC A NB  
19526 C  C1B . HEC L .    ? 0.8586 0.8148 0.8212 0.0344  0.1326  0.0009  304  HEC A C1B 
19527 C  C2B . HEC L .    ? 0.8621 0.8096 0.8143 0.0437  0.1319  0.0049  304  HEC A C2B 
19528 C  C3B . HEC L .    ? 0.8808 0.8109 0.8193 0.0434  0.1380  0.0076  304  HEC A C3B 
19529 C  C4B . HEC L .    ? 0.8965 0.8233 0.8363 0.0332  0.1430  0.0054  304  HEC A C4B 
19530 C  CMB . HEC L .    ? 0.8466 0.8035 0.8029 0.0525  0.1249  0.0055  304  HEC A CMB 
19531 C  CAB . HEC L .    ? 0.8832 0.7989 0.8065 0.0523  0.1395  0.0122  304  HEC A CAB 
19532 C  CBB . HEC L .    ? 0.8893 0.8026 0.8049 0.0556  0.1428  0.0137  304  HEC A CBB 
19533 N  NC  . HEC L .    ? 0.9251 0.8460 0.8686 0.0119  0.1524  -0.0002 304  HEC A NC  
19534 C  C1C . HEC L .    ? 0.9353 0.8419 0.8647 0.0196  0.1545  0.0045  304  HEC A C1C 
19535 C  C2C . HEC L .    ? 0.9601 0.8479 0.8766 0.0156  0.1617  0.0060  304  HEC A C2C 
19536 C  C3C . HEC L .    ? 0.9585 0.8493 0.8813 0.0051  0.1643  0.0021  304  HEC A C3C 
19537 C  C4C . HEC L .    ? 0.9397 0.8522 0.8801 0.0029  0.1581  -0.0018 304  HEC A C4C 
19538 C  CMC . HEC L .    ? 0.9792 0.8463 0.8767 0.0220  0.1667  0.0110  304  HEC A CMC 
19539 C  CAC . HEC L .    ? 0.9759 0.8495 0.8884 -0.0026 0.1722  0.0020  304  HEC A CAC 
19540 C  CBC . HEC L .    ? 0.9635 0.8401 0.8830 -0.0079 0.1690  -0.0013 304  HEC A CBC 
19541 N  ND  . HEC L .    ? 0.8944 0.8504 0.8688 -0.0016 0.1471  -0.0100 304  HEC A ND  
19542 C  C1D . HEC L .    ? 0.9148 0.8574 0.8814 -0.0086 0.1537  -0.0103 304  HEC A C1D 
19543 C  C2D . HEC L .    ? 0.9082 0.8605 0.8845 -0.0188 0.1556  -0.0151 304  HEC A C2D 
19544 C  C3D . HEC L .    ? 0.8854 0.8590 0.8764 -0.0167 0.1495  -0.0177 304  HEC A C3D 
19545 C  C4D . HEC L .    ? 0.8764 0.8503 0.8648 -0.0060 0.1446  -0.0142 304  HEC A C4D 
19546 C  CMD . HEC L .    ? 0.9098 0.8532 0.8827 -0.0295 0.1624  -0.0175 304  HEC A CMD 
19547 C  CAD . HEC L .    ? 0.8601 0.8513 0.8655 -0.0242 0.1487  -0.0231 304  HEC A CAD 
19548 C  CBD . HEC L .    ? 0.8726 0.8616 0.8748 -0.0297 0.1572  -0.0234 304  HEC A CBD 
19549 C  CGD . HEC L .    ? 0.8586 0.8558 0.8627 -0.0234 0.1559  -0.0220 304  HEC A CGD 
19550 O  O1D . HEC L .    ? 0.8346 0.8427 0.8458 -0.0165 0.1479  -0.0221 304  HEC A O1D 
19551 O  O2D . HEC L .    ? 0.8681 0.8606 0.8663 -0.0251 0.1629  -0.0207 304  HEC A O2D 
19552 FE FE  . HEC M .    ? 1.0933 0.8967 0.9595 -0.0444 0.2212  0.0007  305  HEC A FE  
19553 C  CHA . HEC M .    ? 1.1214 0.9011 0.9657 -0.0538 0.2452  0.0045  305  HEC A CHA 
19554 C  CHB . HEC M .    ? 1.0547 0.9098 0.9657 -0.0644 0.2157  -0.0129 305  HEC A CHB 
19555 C  CHC . HEC M .    ? 1.0299 0.8567 0.9170 -0.0339 0.1984  -0.0023 305  HEC A CHC 
19556 C  CHD . HEC M .    ? 1.1142 0.8644 0.9344 -0.0251 0.2275  0.0132  305  HEC A CHD 
19557 N  NA  . HEC M .    ? 1.0943 0.9101 0.9710 -0.0571 0.2288  -0.0035 305  HEC A NA  
19558 C  C1A . HEC M .    ? 1.1050 0.9082 0.9703 -0.0598 0.2390  -0.0012 305  HEC A C1A 
19559 C  C2A . HEC M .    ? 1.0973 0.9162 0.9763 -0.0697 0.2420  -0.0057 305  HEC A C2A 
19560 C  C3A . HEC M .    ? 1.0797 0.9197 0.9771 -0.0724 0.2336  -0.0105 305  HEC A C3A 
19561 C  C4A . HEC M .    ? 1.0749 0.9129 0.9709 -0.0646 0.2253  -0.0092 305  HEC A C4A 
19562 C  CMA . HEC M .    ? 1.0690 0.9316 0.9857 -0.0818 0.2331  -0.0165 305  HEC A CMA 
19563 C  CAA . HEC M .    ? 1.1088 0.9210 0.9817 -0.0758 0.2532  -0.0049 305  HEC A CAA 
19564 C  CBA . HEC M .    ? 1.1421 0.9326 1.0028 -0.0856 0.2635  -0.0051 305  HEC A CBA 
19565 C  CGA . HEC M .    ? 1.1667 0.9472 1.0182 -0.0899 0.2751  -0.0032 305  HEC A CGA 
19566 O  O1A . HEC M .    ? 1.1539 0.9428 1.0068 -0.0838 0.2748  -0.0011 305  HEC A O1A 
19567 O  O2A . HEC M .    ? 1.1984 0.9622 1.0410 -0.0994 0.2849  -0.0037 305  HEC A O2A 
19568 N  NB  . HEC M .    ? 1.0529 0.8877 0.9466 -0.0483 0.2090  -0.0062 305  HEC A NB  
19569 C  C1B . HEC M .    ? 1.0421 0.8951 0.9516 -0.0570 0.2083  -0.0114 305  HEC A C1B 
19570 C  C2B . HEC M .    ? 1.0094 0.8792 0.9336 -0.0567 0.1988  -0.0151 305  HEC A C2B 
19571 C  C3B . HEC M .    ? 0.9999 0.8615 0.9174 -0.0486 0.1943  -0.0121 305  HEC A C3B 
19572 C  C4B . HEC M .    ? 1.0288 0.8687 0.9273 -0.0430 0.2004  -0.0065 305  HEC A C4B 
19573 C  CMB . HEC M .    ? 0.9907 0.8836 0.9345 -0.0642 0.1948  -0.0213 305  HEC A CMB 
19574 C  CAB . HEC M .    ? 0.9614 0.8342 0.8889 -0.0451 0.1844  -0.0140 305  HEC A CAB 
19575 C  CBB . HEC M .    ? 0.9389 0.8324 0.8795 -0.0382 0.1763  -0.0142 305  HEC A CBB 
19576 N  NC  . HEC M .    ? 1.0853 0.8761 0.9414 -0.0326 0.2143  0.0045  305  HEC A NC  
19577 C  C1C . HEC M .    ? 1.0587 0.8638 0.9269 -0.0289 0.2045  0.0027  305  HEC A C1C 
19578 C  C2C . HEC M .    ? 1.0563 0.8493 0.9133 -0.0184 0.2020  0.0071  305  HEC A C2C 
19579 C  C3C . HEC M .    ? 1.0795 0.8515 0.9180 -0.0158 0.2097  0.0112  305  HEC A C3C 
19580 C  C4C . HEC M .    ? 1.0976 0.8675 0.9349 -0.0247 0.2178  0.0098  305  HEC A C4C 
19581 C  CMC . HEC M .    ? 1.0231 0.8251 0.8877 -0.0118 0.1924  0.0069  305  HEC A CMC 
19582 C  CAC . HEC M .    ? 1.0879 0.8421 0.9098 -0.0047 0.2099  0.0166  305  HEC A CAC 
19583 C  CBC . HEC M .    ? 1.1162 0.8455 0.9213 -0.0093 0.2183  0.0177  305  HEC A CBC 
19584 N  ND  . HEC M .    ? 1.1206 0.8901 0.9571 -0.0403 0.2341  0.0077  305  HEC A ND  
19585 C  C1D . HEC M .    ? 1.1269 0.8772 0.9465 -0.0314 0.2347  0.0126  305  HEC A C1D 
19586 C  C2D . HEC M .    ? 1.1501 0.8802 0.9509 -0.0296 0.2443  0.0169  305  HEC A C2D 
19587 C  C3D . HEC M .    ? 1.1547 0.8938 0.9631 -0.0388 0.2501  0.0142  305  HEC A C3D 
19588 C  C4D . HEC M .    ? 1.1279 0.8920 0.9589 -0.0450 0.2431  0.0085  305  HEC A C4D 
19589 C  CMD . HEC M .    ? 1.1903 0.8953 0.9682 -0.0199 0.2481  0.0229  305  HEC A CMD 
19590 C  CAD . HEC M .    ? 1.1991 0.9238 0.9937 -0.0411 0.2614  0.0170  305  HEC A CAD 
19591 C  CBD . HEC M .    ? 1.2657 0.9655 1.0451 -0.0489 0.2717  0.0177  305  HEC A CBD 
19592 C  CGD . HEC M .    ? 1.2972 0.9881 1.0691 -0.0557 0.2832  0.0185  305  HEC A CGD 
19593 O  O1D . HEC M .    ? 1.2844 0.9911 1.0657 -0.0554 0.2826  0.0177  305  HEC A O1D 
19594 O  O2D . HEC M .    ? 1.3397 1.0074 1.0961 -0.0613 0.2933  0.0199  305  HEC A O2D 
19595 FE FE1 . SF4 N .    ? 0.9324 0.9396 0.9730 0.1030  0.0296  -0.0103 1101 SF4 B FE1 
19596 FE FE2 . SF4 N .    ? 0.8697 0.8773 0.9252 0.0984  0.0360  -0.0052 1101 SF4 B FE2 
19597 FE FE3 . SF4 N .    ? 0.8916 0.9142 0.9500 0.0994  0.0266  -0.0121 1101 SF4 B FE3 
19598 FE FE4 . SF4 N .    ? 0.8912 0.8950 0.9393 0.1060  0.0319  -0.0061 1101 SF4 B FE4 
19599 S  S1  . SF4 N .    ? 0.8474 0.8620 0.9113 0.0998  0.0324  -0.0064 1101 SF4 B S1  
19600 S  S2  . SF4 N .    ? 0.9295 0.9443 0.9741 0.1067  0.0242  -0.0127 1101 SF4 B S2  
19601 S  S3  . SF4 N .    ? 0.8913 0.8854 0.9317 0.1048  0.0373  -0.0034 1101 SF4 B S3  
19602 S  S4  . SF4 N .    ? 0.8909 0.9083 0.9443 0.0957  0.0303  -0.0113 1101 SF4 B S4  
19603 FE FE1 . SF4 O .    ? 0.6174 0.6964 0.7274 0.0766  0.0225  -0.0212 1102 SF4 B FE1 
19604 FE FE2 . SF4 O .    ? 0.6110 0.6918 0.7243 0.0827  0.0181  -0.0217 1102 SF4 B FE2 
19605 FE FE3 . SF4 O .    ? 0.5982 0.6820 0.7040 0.0804  0.0171  -0.0255 1102 SF4 B FE3 
19606 FE FE4 . SF4 O .    ? 0.6564 0.7246 0.7603 0.0820  0.0224  -0.0187 1102 SF4 B FE4 
19607 S  S1  . SF4 O .    ? 0.6246 0.7000 0.7293 0.0859  0.0169  -0.0223 1102 SF4 B S1  
19608 S  S2  . SF4 O .    ? 0.6292 0.7026 0.7304 0.0772  0.0224  -0.0221 1102 SF4 B S2  
19609 S  S3  . SF4 O .    ? 0.6435 0.7155 0.7562 0.0804  0.0234  -0.0173 1102 SF4 B S3  
19610 S  S4  . SF4 O .    ? 0.5803 0.6711 0.6943 0.0783  0.0174  -0.0256 1102 SF4 B S4  
19611 FE FE1 . SF4 P .    ? 0.5403 0.6281 0.6681 0.0991  0.0037  -0.0282 1103 SF4 B FE1 
19612 FE FE2 . SF4 P .    ? 0.5419 0.6353 0.6722 0.1027  -0.0007 -0.0322 1103 SF4 B FE2 
19613 FE FE3 . SF4 P .    ? 0.5330 0.6170 0.6538 0.1072  -0.0002 -0.0306 1103 SF4 B FE3 
19614 FE FE4 . SF4 P .    ? 0.5062 0.5822 0.6345 0.1017  0.0031  -0.0275 1103 SF4 B FE4 
19615 S  S1  . SF4 P .    ? 0.5204 0.6012 0.6452 0.1074  -0.0014 -0.0315 1103 SF4 B S1  
19616 S  S2  . SF4 P .    ? 0.5223 0.5965 0.6438 0.1028  0.0046  -0.0260 1103 SF4 B S2  
19617 S  S3  . SF4 P .    ? 0.5179 0.6054 0.6524 0.0975  0.0032  -0.0283 1103 SF4 B S3  
19618 S  S4  . SF4 P .    ? 0.5502 0.6486 0.6763 0.1031  -0.0004 -0.0326 1103 SF4 B S4  
19626 FE FE  . HEC R .    ? 1.4481 1.0643 1.1694 0.0299  0.2194  0.0329  301  HEC E FE  
19627 C  CHA . HEC R .    ? 1.5207 1.0766 1.2009 0.0203  0.2371  0.0333  301  HEC E CHA 
19628 C  CHB . HEC R .    ? 1.3885 1.0078 1.1074 0.0567  0.2075  0.0388  301  HEC E CHB 
19629 C  CHC . HEC R .    ? 1.3287 1.0069 1.0947 0.0360  0.2004  0.0302  301  HEC E CHC 
19630 C  CHD . HEC R .    ? 1.4703 1.0893 1.1991 0.0017  0.2316  0.0261  301  HEC E CHD 
19631 N  NA  . HEC R .    ? 1.4579 1.0504 1.1610 0.0373  0.2215  0.0356  301  HEC E NA  
19632 C  C1A . HEC R .    ? 1.4915 1.0590 1.1774 0.0325  0.2296  0.0357  301  HEC E C1A 
19633 C  C2A . HEC R .    ? 1.4956 1.0511 1.1706 0.0424  0.2289  0.0386  301  HEC E C2A 
19634 C  C3A . HEC R .    ? 1.4564 1.0299 1.1424 0.0524  0.2208  0.0401  301  HEC E C3A 
19635 C  C4A . HEC R .    ? 1.4330 1.0299 1.1369 0.0493  0.2160  0.0383  301  HEC E C4A 
19636 C  CMA . HEC R .    ? 1.4406 1.0105 1.1213 0.0649  0.2176  0.0433  301  HEC E CMA 
19637 C  CAA . HEC R .    ? 1.5313 1.0578 1.1852 0.0414  0.2364  0.0396  301  HEC E CAA 
19638 C  CBA . HEC R .    ? 1.5196 1.0483 1.1804 0.0327  0.2345  0.0347  301  HEC E CBA 
19639 C  CGA . HEC R .    ? 1.5688 1.0682 1.2088 0.0295  0.2426  0.0350  301  HEC E CGA 
19640 O  O1A . HEC R .    ? 1.5653 1.0620 1.2069 0.0236  0.2417  0.0314  301  HEC E O1A 
19641 O  O2A . HEC R .    ? 1.6174 1.0955 1.2385 0.0331  0.2500  0.0388  301  HEC E O2A 
19642 N  NB  . HEC R .    ? 1.3801 1.0235 1.1189 0.0440  0.2064  0.0346  301  HEC E NB  
19643 C  C1B . HEC R .    ? 1.3654 1.0068 1.1017 0.0529  0.2028  0.0365  301  HEC E C1B 
19644 C  C2B . HEC R .    ? 1.2972 0.9633 1.0521 0.0575  0.1934  0.0356  301  HEC E C2B 
19645 C  C3B . HEC R .    ? 1.2878 0.9694 1.0551 0.0519  0.1914  0.0332  301  HEC E C3B 
19646 C  C4B . HEC R .    ? 1.3379 1.0060 1.0955 0.0435  0.1995  0.0326  301  HEC E C4B 
19647 C  CMB . HEC R .    ? 1.2222 0.8950 0.9815 0.0673  0.1873  0.0371  301  HEC E CMB 
19648 C  CAB . HEC R .    ? 1.2228 0.9314 1.0109 0.0536  0.1826  0.0314  301  HEC E CAB 
19649 C  CBB . HEC R .    ? 1.1806 0.9018 0.9831 0.0474  0.1777  0.0272  301  HEC E CBB 
19650 N  NC  . HEC R .    ? 1.4193 1.0633 1.1629 0.0206  0.2161  0.0288  301  HEC E NC  
19651 C  C1C . HEC R .    ? 1.3740 1.0411 1.1333 0.0258  0.2082  0.0287  301  HEC E C1C 
19652 C  C2C . HEC R .    ? 1.3629 1.0422 1.1324 0.0177  0.2091  0.0259  301  HEC E C2C 
19653 C  C3C . HEC R .    ? 1.3933 1.0557 1.1514 0.0094  0.2182  0.0254  301  HEC E C3C 
19654 C  C4C . HEC R .    ? 1.4320 1.0724 1.1746 0.0100  0.2225  0.0267  301  HEC E C4C 
19655 C  CMC . HEC R .    ? 1.3082 1.0107 1.0928 0.0219  0.2024  0.0257  301  HEC E CMC 
19656 C  CAC . HEC R .    ? 1.3810 1.0480 1.1436 -0.0007 0.2231  0.0230  301  HEC E CAC 
19657 C  CBC . HEC R .    ? 1.3306 1.0182 1.1136 -0.0114 0.2186  0.0167  301  HEC E CBC 
19658 N  ND  . HEC R .    ? 1.4956 1.0877 1.2034 0.0126  0.2320  0.0298  301  HEC E ND  
19659 C  C1D . HEC R .    ? 1.5000 1.0959 1.2119 0.0034  0.2363  0.0278  301  HEC E C1D 
19660 C  C2D . HEC R .    ? 1.5380 1.1089 1.2329 -0.0042 0.2467  0.0278  301  HEC E C2D 
19661 C  C3D . HEC R .    ? 1.5484 1.0988 1.2275 0.0017  0.2483  0.0301  301  HEC E C3D 
19662 C  C4D . HEC R .    ? 1.5216 1.0874 1.2103 0.0121  0.2388  0.0312  301  HEC E C4D 
19663 C  CMD . HEC R .    ? 1.5665 1.1322 1.2595 -0.0159 0.2548  0.0260  301  HEC E CMD 
19664 C  CAD . HEC R .    ? 1.5864 1.1057 1.2437 -0.0028 0.2583  0.0309  301  HEC E CAD 
19665 C  CBD . HEC R .    ? 1.6163 1.1357 1.2802 -0.0161 0.2586  0.0248  301  HEC E CBD 
19666 C  CGD . HEC R .    ? 1.6537 1.1424 1.2964 -0.0219 0.2689  0.0252  301  HEC E CGD 
19667 O  O1D . HEC R .    ? 1.6674 1.1520 1.3123 -0.0330 0.2704  0.0202  301  HEC E O1D 
19668 O  O2D . HEC R .    ? 1.6651 1.1331 1.2885 -0.0152 0.2756  0.0303  301  HEC E O2D 
# 
