data_9DZU
# 
_entry.id   9DZU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9DZU         pdb_00009dzu 10.2210/pdb9dzu/pdb 
WWPDB D_1000289168 ?            ?                   
EMDB  EMD-47338    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-05 ? 
2 'EM metadata'     1 0 2025-02-05 ? 
3 FSC               1 0 2025-02-05 ? 
4 Image             1 0 2025-02-05 ? 
5 'Primary map'     1 0 2025-02-05 ? 
6 'Structure model' 1 1 2025-05-21 ? 
7 'EM metadata'     1 1 2025-05-21 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 FSC               repository 'Initial release' ? ? 
4 4 Image             repository 'Initial release' ? ? 
5 5 'Primary map'     repository 'Initial release' ? ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 6 'Structure model' 'Data collection'      
2 6 'Structure model' 'Derived calculations' 
3 6 'Structure model' 'Structure summary'    
4 7 'EM metadata'     'Experimental summary' 
5 7 'EM metadata'     'Structure summary'    
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 6 'Structure model' chem_comp           
2 6 'Structure model' chem_comp_atom      
3 6 'Structure model' chem_comp_bond      
4 6 'Structure model' em_admin            
5 6 'Structure model' entity              
6 6 'Structure model' pdbx_entity_nonpoly 
7 7 'EM metadata'     em_admin            
8 7 'EM metadata'     entity              
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  6 'Structure model' '_chem_comp.name'                    
2  6 'Structure model' '_chem_comp_atom.atom_id'            
3  6 'Structure model' '_chem_comp_bond.atom_id_1'          
4  6 'Structure model' '_chem_comp_bond.atom_id_2'          
5  6 'Structure model' '_chem_comp_bond.pdbx_stereo_config' 
6  6 'Structure model' '_chem_comp_bond.value_order'        
7  6 'Structure model' '_em_admin.last_update'              
8  6 'Structure model' '_entity.pdbx_description'           
9  6 'Structure model' '_pdbx_entity_nonpoly.name'          
10 7 'EM metadata'     '_chem_comp.name'                    
11 7 'EM metadata'     '_em_admin.last_update'              
12 7 'EM metadata'     '_entity.pdbx_description'           
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DZU 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB .                                                                                                             EMD-47334 
'consensus EM volume'  
EMDB .                                                                                                             EMD-47335 
'focused EM volume'    
EMDB 'Cryo-EM structure of the C. neoformans lipid flippase Apt1-Cdc50 bound with butyrolactol A in the E2P state' EMD-47338 
'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              huilin.li@vai.org 
_pdbx_contact_author.name_first         Huilin 
_pdbx_contact_author.name_last          Li 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8085-8928 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Duan, H.D.' 1 0000-0001-5069-0191 
'Li, H.'     2 0000-0001-8085-8928 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Butyrolactol A is a phospholipid flippase inhibitor that potentiates the bioactivity of caspofungin against resistant fungi.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2025.01.06.630955 
_citation.pdbx_database_id_PubMed   39829750 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chen, X.'       1  0009-0006-6304-5777 
primary 'Duan, H.D.'     2  ?                   
primary 'Hoy, M.J.'      3  ?                   
primary 'Koteva, K.'     4  ?                   
primary 'Spitzer, M.'    5  ?                   
primary 'Guitor, A.K.'   6  ?                   
primary 'Puumala, E.'    7  ?                   
primary 'Hu, G.'         8  ?                   
primary 'Yiu, B.'        9  ?                   
primary 'Chou, S.'       10 ?                   
primary 'Bian, Z.'       11 ?                   
primary 'Guo, A.B.Y.'    12 ?                   
primary 'Sun, S.'        13 ?                   
primary 'Robbins, N.'    14 ?                   
primary 'Cook, M.A.'     15 ?                   
primary 'Truant, R.'     16 ?                   
primary 'MacNeil, L.T.'  17 ?                   
primary 'Brown, E.D.'    18 ?                   
primary 'Kronstad, J.W.' 19 ?                   
primary 'Cowen, L.E.'    20 ?                   
primary 'Heitman, J.'    21 0000-0001-6369-5995 
primary 'Li, H.'         22 0000-0001-8085-8928 
primary 'Wright, G.D.'   23 0000-0002-9129-7131 
# 
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     man 'Transcription regulator' 45937.961  1 ?       ? ? ? 
2 polymer     man 'Phospholipid-transporting ATPase' 176534.609 1 7.6.2.1 ? ? ? 
3 branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401    2 ?       ? 
? ? 
4 branched    man 
;alpha-D-mannopyranose-(1-4)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
1072.964   1 ?       ? ? ? 
5 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208    1 ?       ? ? ? 
6 non-polymer syn 'BERYLLIUM TRIFLUORIDE ION' 66.007     1 ?       ? ? ? 
7 non-polymer syn 'MAGNESIUM ION' 24.305     1 ?       ? ? ? 
8 non-polymer syn 
;(3R,4R,5S)-3,4-dihydroxy-5-[(1R,2R,3S,4S,5R,6R,8E,10E,14E,16Z)-1,2,3,4,5-pentahydroxy-6,20,20-trimethylhenicosa-8,10,14,16-tetraen-1-yl]oxolan-2-one
;
526.659    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 
;MAIFNRKPKARLDGEPAPTEKEKVKWSKRPANTAFKQQRLKAWQPILTPKSVLPTLLIIGIIFAPIGALIVWGSGKVTTI
TLDYTECDVDAPTDGSYQAMPNSAYQYDLATSSSVSESSIASPTWTFSNDSSREVGETARCEIEFEVPYDLGPGLFLYYK
LTNYYQNHRRYSSSFDATQLIGDSRSLSQINGGNCKPITSRDGKPYYPCGLIANSLFNDTFPSVVLLNPTNGAQNQTYNF
SESGIAWGGIKKNYASTLTYISPSDVLPPPNWALKYPNGYVDGFPNLREDEHFQVWMRVAALPTFRKLWARNDGEIMSQG
RYRIVANMNYPVKQFSGTKSIVISTVSWIGGKQPFLGWAYIAAAILCVVLAVAGLIRHLVKPRKLGDMSLLSWNQPNANG
LHHHHHHHHHH
;
;MAIFNRKPKARLDGEPAPTEKEKVKWSKRPANTAFKQQRLKAWQPILTPKSVLPTLLIIGIIFAPIGALIVWGSGKVTTI
TLDYTECDVDAPTDGSYQAMPNSAYQYDLATSSSVSESSIASPTWTFSNDSSREVGETARCEIEFEVPYDLGPGLFLYYK
LTNYYQNHRRYSSSFDATQLIGDSRSLSQINGGNCKPITSRDGKPYYPCGLIANSLFNDTFPSVVLLNPTNGAQNQTYNF
SESGIAWGGIKKNYASTLTYISPSDVLPPPNWALKYPNGYVDGFPNLREDEHFQVWMRVAALPTFRKLWARNDGEIMSQG
RYRIVANMNYPVKQFSGTKSIVISTVSWIGGKQPFLGWAYIAAAILCVVLAVAGLIRHLVKPRKLGDMSLLSWNQPNANG
LHHHHHHHHHH
;
B ? 
2 'polypeptide(L)' no no 
;MGASKPPLVPRSKKHNPSWLDRNIVKPLESLAPSKLFARRRSPPVPRSVFINEPLPSEYYDKKGKILRAHHFATNQNVTS
KYTVITFIPKNLFEQFRRVANCFFLAISILQFFPKFSTISPGLVILPLIIVLAITALKDGYEDIKRHQADHRTNHAIVHV
LGGQDYTNQNPMASKDKTFIPAIPLPKRRSKKAKKAEEEAALNMQGRSSSTENFAAEPVPGAEPRGQDELQRMRSQVSNW
DEDPEAGDSPGELGWHRTIWEDVKVGDFVKIYENEQFPADIVICATSEEEDVAYIETKNLDGETNLKSRNGVPGLSHLNT
AEACAKAHLCIDLDAPESNMFRLNGAVINLEEYDEDEQHPIHPITLETTMLRGCVLKNTAWVIGIIVYTGEDTKIIRNAG
ATPSKRSKVEKQMNPQVIINLVILAAIAVVCAIVDHVNEVEWDRQQAYWMLFADTSGDNPNINGLVTFANAFITFQNIVP
ISLYISIEAVRTIQAAFIYWDRDIKYKKDGVTTRTTARSWNLSDDLGQIEYIFSDKTGTLTQNAMIFRQCSVGGKIYTGD
GLPPSHPTITHQHQPPPVHQHDDQDDPIAKSASESDDSDPKKISTEDPDEIKVTLPKEVLATFHDAELDKDLEAHDSEQS
RILHGFFAVLGLCHTVLAAETEPGVIEYKAQSPDEAALVQSAADVGFVFRGRDHNILRMSTPFSDVSDEYELLHVLEFNS
ARKRMSVILRKLDEDGRIFLLCKGADNVIFERLTKDSNQREMREKTDQDLQYFASEGLRTLCLAYRILDPQVYEQWAKEY
HNATVALQDREERIESVSSSIERDLILLGATAIEDKLQDGVPDTISDLKRAGIKVWVATGDKLETAVAIGYTTNLLTKDT
NLIVVREGRHSIGDQLREALEEFFGEDAGLRTTLSRIDSRRNSMDPPRLTRVNTGVRSLVGRDNGTRPGGFSLVIEGHAL
AHCFDDEETEALLLALSTRCNTVICCRVSPLQKAQIVHLIKDNLGVMCLAIGDGANDVSMIQAADVGVGISGEEGLQAVN
SSDYAIAQFRYLKRLLLVHGHWSYFRNSSMILNFFYKNIIGIGVLFWFMIYCGWSTTYVFAYVYLLFWNVFWTLVPVIAI
GLFDRNIDDETLMALPELYRASREGKYFGLMRFAYYIFEGVYQSAVIYFFLNYTYVTTTARGDGYDVYMYEMSTTQAIGA
VMVANLFSGLNIDAWTGWVWFAIWFGPFLIWVFTAVYSVIPPSSFYTGVYGNDVFLFRSAAYWFGWPFVTIIALLPRYLI
KTFRQNIFPNDVDTMRLVRKYHPEVDLYNHPMLGGKLAPKKDEDESDYGEEPFDGPEGRRSSIKMANLRHSHGAFGRGDQ
AGDMELGMGRKSLGNRPGLRSSMDSSRFGIHSGARGSTVDMSTGLEQPPSRGFGFTMEEGGVAIQRMQSRLSQTSSHASR
SRWPRFNNNSSSSHPFETKPPSSMSKLRSRAGSILTRKRADTTDTRNSDDKSLSSPVKTGFFGRHMPGQNHGQHEGRSMG
TPLKSETGRGDNWEEEELEDESLGRGFGVGQNMAPPEIPRMDYKDDDDKI
;
;MGASKPPLVPRSKKHNPSWLDRNIVKPLESLAPSKLFARRRSPPVPRSVFINEPLPSEYYDKKGKILRAHHFATNQNVTS
KYTVITFIPKNLFEQFRRVANCFFLAISILQFFPKFSTISPGLVILPLIIVLAITALKDGYEDIKRHQADHRTNHAIVHV
LGGQDYTNQNPMASKDKTFIPAIPLPKRRSKKAKKAEEEAALNMQGRSSSTENFAAEPVPGAEPRGQDELQRMRSQVSNW
DEDPEAGDSPGELGWHRTIWEDVKVGDFVKIYENEQFPADIVICATSEEEDVAYIETKNLDGETNLKSRNGVPGLSHLNT
AEACAKAHLCIDLDAPESNMFRLNGAVINLEEYDEDEQHPIHPITLETTMLRGCVLKNTAWVIGIIVYTGEDTKIIRNAG
ATPSKRSKVEKQMNPQVIINLVILAAIAVVCAIVDHVNEVEWDRQQAYWMLFADTSGDNPNINGLVTFANAFITFQNIVP
ISLYISIEAVRTIQAAFIYWDRDIKYKKDGVTTRTTARSWNLSDDLGQIEYIFSDKTGTLTQNAMIFRQCSVGGKIYTGD
GLPPSHPTITHQHQPPPVHQHDDQDDPIAKSASESDDSDPKKISTEDPDEIKVTLPKEVLATFHDAELDKDLEAHDSEQS
RILHGFFAVLGLCHTVLAAETEPGVIEYKAQSPDEAALVQSAADVGFVFRGRDHNILRMSTPFSDVSDEYELLHVLEFNS
ARKRMSVILRKLDEDGRIFLLCKGADNVIFERLTKDSNQREMREKTDQDLQYFASEGLRTLCLAYRILDPQVYEQWAKEY
HNATVALQDREERIESVSSSIERDLILLGATAIEDKLQDGVPDTISDLKRAGIKVWVATGDKLETAVAIGYTTNLLTKDT
NLIVVREGRHSIGDQLREALEEFFGEDAGLRTTLSRIDSRRNSMDPPRLTRVNTGVRSLVGRDNGTRPGGFSLVIEGHAL
AHCFDDEETEALLLALSTRCNTVICCRVSPLQKAQIVHLIKDNLGVMCLAIGDGANDVSMIQAADVGVGISGEEGLQAVN
SSDYAIAQFRYLKRLLLVHGHWSYFRNSSMILNFFYKNIIGIGVLFWFMIYCGWSTTYVFAYVYLLFWNVFWTLVPVIAI
GLFDRNIDDETLMALPELYRASREGKYFGLMRFAYYIFEGVYQSAVIYFFLNYTYVTTTARGDGYDVYMYEMSTTQAIGA
VMVANLFSGLNIDAWTGWVWFAIWFGPFLIWVFTAVYSVIPPSSFYTGVYGNDVFLFRSAAYWFGWPFVTIIALLPRYLI
KTFRQNIFPNDVDTMRLVRKYHPEVDLYNHPMLGGKLAPKKDEDESDYGEEPFDGPEGRRSSIKMANLRHSHGAFGRGDQ
AGDMELGMGRKSLGNRPGLRSSMDSSRFGIHSGARGSTVDMSTGLEQPPSRGFGFTMEEGGVAIQRMQSRLSQTSSHASR
SRWPRFNNNSSSSHPFETKPPSSMSKLRSRAGSILTRKRADTTDTRNSDDKSLSSPVKTGFFGRHMPGQNHGQHEGRSMG
TPLKSETGRGDNWEEEELEDESLGRGFGVGQNMAPPEIPRMDYKDDDDKI
;
A ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
5 2-acetamido-2-deoxy-beta-D-glucopyranose NAG   
6 'BERYLLIUM TRIFLUORIDE ION' BEF   
7 'MAGNESIUM ION' MG    
8 
;(3R,4R,5S)-3,4-dihydroxy-5-[(1R,2R,3S,4S,5R,6R,8E,10E,14E,16Z)-1,2,3,4,5-pentahydroxy-6,20,20-trimethylhenicosa-8,10,14,16-tetraen-1-yl]oxolan-2-one
;
A1BD6 
# 
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    ILE n 
1 4    PHE n 
1 5    ASN n 
1 6    ARG n 
1 7    LYS n 
1 8    PRO n 
1 9    LYS n 
1 10   ALA n 
1 11   ARG n 
1 12   LEU n 
1 13   ASP n 
1 14   GLY n 
1 15   GLU n 
1 16   PRO n 
1 17   ALA n 
1 18   PRO n 
1 19   THR n 
1 20   GLU n 
1 21   LYS n 
1 22   GLU n 
1 23   LYS n 
1 24   VAL n 
1 25   LYS n 
1 26   TRP n 
1 27   SER n 
1 28   LYS n 
1 29   ARG n 
1 30   PRO n 
1 31   ALA n 
1 32   ASN n 
1 33   THR n 
1 34   ALA n 
1 35   PHE n 
1 36   LYS n 
1 37   GLN n 
1 38   GLN n 
1 39   ARG n 
1 40   LEU n 
1 41   LYS n 
1 42   ALA n 
1 43   TRP n 
1 44   GLN n 
1 45   PRO n 
1 46   ILE n 
1 47   LEU n 
1 48   THR n 
1 49   PRO n 
1 50   LYS n 
1 51   SER n 
1 52   VAL n 
1 53   LEU n 
1 54   PRO n 
1 55   THR n 
1 56   LEU n 
1 57   LEU n 
1 58   ILE n 
1 59   ILE n 
1 60   GLY n 
1 61   ILE n 
1 62   ILE n 
1 63   PHE n 
1 64   ALA n 
1 65   PRO n 
1 66   ILE n 
1 67   GLY n 
1 68   ALA n 
1 69   LEU n 
1 70   ILE n 
1 71   VAL n 
1 72   TRP n 
1 73   GLY n 
1 74   SER n 
1 75   GLY n 
1 76   LYS n 
1 77   VAL n 
1 78   THR n 
1 79   THR n 
1 80   ILE n 
1 81   THR n 
1 82   LEU n 
1 83   ASP n 
1 84   TYR n 
1 85   THR n 
1 86   GLU n 
1 87   CYS n 
1 88   ASP n 
1 89   VAL n 
1 90   ASP n 
1 91   ALA n 
1 92   PRO n 
1 93   THR n 
1 94   ASP n 
1 95   GLY n 
1 96   SER n 
1 97   TYR n 
1 98   GLN n 
1 99   ALA n 
1 100  MET n 
1 101  PRO n 
1 102  ASN n 
1 103  SER n 
1 104  ALA n 
1 105  TYR n 
1 106  GLN n 
1 107  TYR n 
1 108  ASP n 
1 109  LEU n 
1 110  ALA n 
1 111  THR n 
1 112  SER n 
1 113  SER n 
1 114  SER n 
1 115  VAL n 
1 116  SER n 
1 117  GLU n 
1 118  SER n 
1 119  SER n 
1 120  ILE n 
1 121  ALA n 
1 122  SER n 
1 123  PRO n 
1 124  THR n 
1 125  TRP n 
1 126  THR n 
1 127  PHE n 
1 128  SER n 
1 129  ASN n 
1 130  ASP n 
1 131  SER n 
1 132  SER n 
1 133  ARG n 
1 134  GLU n 
1 135  VAL n 
1 136  GLY n 
1 137  GLU n 
1 138  THR n 
1 139  ALA n 
1 140  ARG n 
1 141  CYS n 
1 142  GLU n 
1 143  ILE n 
1 144  GLU n 
1 145  PHE n 
1 146  GLU n 
1 147  VAL n 
1 148  PRO n 
1 149  TYR n 
1 150  ASP n 
1 151  LEU n 
1 152  GLY n 
1 153  PRO n 
1 154  GLY n 
1 155  LEU n 
1 156  PHE n 
1 157  LEU n 
1 158  TYR n 
1 159  TYR n 
1 160  LYS n 
1 161  LEU n 
1 162  THR n 
1 163  ASN n 
1 164  TYR n 
1 165  TYR n 
1 166  GLN n 
1 167  ASN n 
1 168  HIS n 
1 169  ARG n 
1 170  ARG n 
1 171  TYR n 
1 172  SER n 
1 173  SER n 
1 174  SER n 
1 175  PHE n 
1 176  ASP n 
1 177  ALA n 
1 178  THR n 
1 179  GLN n 
1 180  LEU n 
1 181  ILE n 
1 182  GLY n 
1 183  ASP n 
1 184  SER n 
1 185  ARG n 
1 186  SER n 
1 187  LEU n 
1 188  SER n 
1 189  GLN n 
1 190  ILE n 
1 191  ASN n 
1 192  GLY n 
1 193  GLY n 
1 194  ASN n 
1 195  CYS n 
1 196  LYS n 
1 197  PRO n 
1 198  ILE n 
1 199  THR n 
1 200  SER n 
1 201  ARG n 
1 202  ASP n 
1 203  GLY n 
1 204  LYS n 
1 205  PRO n 
1 206  TYR n 
1 207  TYR n 
1 208  PRO n 
1 209  CYS n 
1 210  GLY n 
1 211  LEU n 
1 212  ILE n 
1 213  ALA n 
1 214  ASN n 
1 215  SER n 
1 216  LEU n 
1 217  PHE n 
1 218  ASN n 
1 219  ASP n 
1 220  THR n 
1 221  PHE n 
1 222  PRO n 
1 223  SER n 
1 224  VAL n 
1 225  VAL n 
1 226  LEU n 
1 227  LEU n 
1 228  ASN n 
1 229  PRO n 
1 230  THR n 
1 231  ASN n 
1 232  GLY n 
1 233  ALA n 
1 234  GLN n 
1 235  ASN n 
1 236  GLN n 
1 237  THR n 
1 238  TYR n 
1 239  ASN n 
1 240  PHE n 
1 241  SER n 
1 242  GLU n 
1 243  SER n 
1 244  GLY n 
1 245  ILE n 
1 246  ALA n 
1 247  TRP n 
1 248  GLY n 
1 249  GLY n 
1 250  ILE n 
1 251  LYS n 
1 252  LYS n 
1 253  ASN n 
1 254  TYR n 
1 255  ALA n 
1 256  SER n 
1 257  THR n 
1 258  LEU n 
1 259  THR n 
1 260  TYR n 
1 261  ILE n 
1 262  SER n 
1 263  PRO n 
1 264  SER n 
1 265  ASP n 
1 266  VAL n 
1 267  LEU n 
1 268  PRO n 
1 269  PRO n 
1 270  PRO n 
1 271  ASN n 
1 272  TRP n 
1 273  ALA n 
1 274  LEU n 
1 275  LYS n 
1 276  TYR n 
1 277  PRO n 
1 278  ASN n 
1 279  GLY n 
1 280  TYR n 
1 281  VAL n 
1 282  ASP n 
1 283  GLY n 
1 284  PHE n 
1 285  PRO n 
1 286  ASN n 
1 287  LEU n 
1 288  ARG n 
1 289  GLU n 
1 290  ASP n 
1 291  GLU n 
1 292  HIS n 
1 293  PHE n 
1 294  GLN n 
1 295  VAL n 
1 296  TRP n 
1 297  MET n 
1 298  ARG n 
1 299  VAL n 
1 300  ALA n 
1 301  ALA n 
1 302  LEU n 
1 303  PRO n 
1 304  THR n 
1 305  PHE n 
1 306  ARG n 
1 307  LYS n 
1 308  LEU n 
1 309  TRP n 
1 310  ALA n 
1 311  ARG n 
1 312  ASN n 
1 313  ASP n 
1 314  GLY n 
1 315  GLU n 
1 316  ILE n 
1 317  MET n 
1 318  SER n 
1 319  GLN n 
1 320  GLY n 
1 321  ARG n 
1 322  TYR n 
1 323  ARG n 
1 324  ILE n 
1 325  VAL n 
1 326  ALA n 
1 327  ASN n 
1 328  MET n 
1 329  ASN n 
1 330  TYR n 
1 331  PRO n 
1 332  VAL n 
1 333  LYS n 
1 334  GLN n 
1 335  PHE n 
1 336  SER n 
1 337  GLY n 
1 338  THR n 
1 339  LYS n 
1 340  SER n 
1 341  ILE n 
1 342  VAL n 
1 343  ILE n 
1 344  SER n 
1 345  THR n 
1 346  VAL n 
1 347  SER n 
1 348  TRP n 
1 349  ILE n 
1 350  GLY n 
1 351  GLY n 
1 352  LYS n 
1 353  GLN n 
1 354  PRO n 
1 355  PHE n 
1 356  LEU n 
1 357  GLY n 
1 358  TRP n 
1 359  ALA n 
1 360  TYR n 
1 361  ILE n 
1 362  ALA n 
1 363  ALA n 
1 364  ALA n 
1 365  ILE n 
1 366  LEU n 
1 367  CYS n 
1 368  VAL n 
1 369  VAL n 
1 370  LEU n 
1 371  ALA n 
1 372  VAL n 
1 373  ALA n 
1 374  GLY n 
1 375  LEU n 
1 376  ILE n 
1 377  ARG n 
1 378  HIS n 
1 379  LEU n 
1 380  VAL n 
1 381  LYS n 
1 382  PRO n 
1 383  ARG n 
1 384  LYS n 
1 385  LEU n 
1 386  GLY n 
1 387  ASP n 
1 388  MET n 
1 389  SER n 
1 390  LEU n 
1 391  LEU n 
1 392  SER n 
1 393  TRP n 
1 394  ASN n 
1 395  GLN n 
1 396  PRO n 
1 397  ASN n 
1 398  ALA n 
1 399  ASN n 
1 400  GLY n 
1 401  LEU n 
1 402  HIS n 
1 403  HIS n 
1 404  HIS n 
1 405  HIS n 
1 406  HIS n 
1 407  HIS n 
1 408  HIS n 
1 409  HIS n 
1 410  HIS n 
1 411  HIS n 
2 1    MET n 
2 2    GLY n 
2 3    ALA n 
2 4    SER n 
2 5    LYS n 
2 6    PRO n 
2 7    PRO n 
2 8    LEU n 
2 9    VAL n 
2 10   PRO n 
2 11   ARG n 
2 12   SER n 
2 13   LYS n 
2 14   LYS n 
2 15   HIS n 
2 16   ASN n 
2 17   PRO n 
2 18   SER n 
2 19   TRP n 
2 20   LEU n 
2 21   ASP n 
2 22   ARG n 
2 23   ASN n 
2 24   ILE n 
2 25   VAL n 
2 26   LYS n 
2 27   PRO n 
2 28   LEU n 
2 29   GLU n 
2 30   SER n 
2 31   LEU n 
2 32   ALA n 
2 33   PRO n 
2 34   SER n 
2 35   LYS n 
2 36   LEU n 
2 37   PHE n 
2 38   ALA n 
2 39   ARG n 
2 40   ARG n 
2 41   ARG n 
2 42   SER n 
2 43   PRO n 
2 44   PRO n 
2 45   VAL n 
2 46   PRO n 
2 47   ARG n 
2 48   SER n 
2 49   VAL n 
2 50   PHE n 
2 51   ILE n 
2 52   ASN n 
2 53   GLU n 
2 54   PRO n 
2 55   LEU n 
2 56   PRO n 
2 57   SER n 
2 58   GLU n 
2 59   TYR n 
2 60   TYR n 
2 61   ASP n 
2 62   LYS n 
2 63   LYS n 
2 64   GLY n 
2 65   LYS n 
2 66   ILE n 
2 67   LEU n 
2 68   ARG n 
2 69   ALA n 
2 70   HIS n 
2 71   HIS n 
2 72   PHE n 
2 73   ALA n 
2 74   THR n 
2 75   ASN n 
2 76   GLN n 
2 77   ASN n 
2 78   VAL n 
2 79   THR n 
2 80   SER n 
2 81   LYS n 
2 82   TYR n 
2 83   THR n 
2 84   VAL n 
2 85   ILE n 
2 86   THR n 
2 87   PHE n 
2 88   ILE n 
2 89   PRO n 
2 90   LYS n 
2 91   ASN n 
2 92   LEU n 
2 93   PHE n 
2 94   GLU n 
2 95   GLN n 
2 96   PHE n 
2 97   ARG n 
2 98   ARG n 
2 99   VAL n 
2 100  ALA n 
2 101  ASN n 
2 102  CYS n 
2 103  PHE n 
2 104  PHE n 
2 105  LEU n 
2 106  ALA n 
2 107  ILE n 
2 108  SER n 
2 109  ILE n 
2 110  LEU n 
2 111  GLN n 
2 112  PHE n 
2 113  PHE n 
2 114  PRO n 
2 115  LYS n 
2 116  PHE n 
2 117  SER n 
2 118  THR n 
2 119  ILE n 
2 120  SER n 
2 121  PRO n 
2 122  GLY n 
2 123  LEU n 
2 124  VAL n 
2 125  ILE n 
2 126  LEU n 
2 127  PRO n 
2 128  LEU n 
2 129  ILE n 
2 130  ILE n 
2 131  VAL n 
2 132  LEU n 
2 133  ALA n 
2 134  ILE n 
2 135  THR n 
2 136  ALA n 
2 137  LEU n 
2 138  LYS n 
2 139  ASP n 
2 140  GLY n 
2 141  TYR n 
2 142  GLU n 
2 143  ASP n 
2 144  ILE n 
2 145  LYS n 
2 146  ARG n 
2 147  HIS n 
2 148  GLN n 
2 149  ALA n 
2 150  ASP n 
2 151  HIS n 
2 152  ARG n 
2 153  THR n 
2 154  ASN n 
2 155  HIS n 
2 156  ALA n 
2 157  ILE n 
2 158  VAL n 
2 159  HIS n 
2 160  VAL n 
2 161  LEU n 
2 162  GLY n 
2 163  GLY n 
2 164  GLN n 
2 165  ASP n 
2 166  TYR n 
2 167  THR n 
2 168  ASN n 
2 169  GLN n 
2 170  ASN n 
2 171  PRO n 
2 172  MET n 
2 173  ALA n 
2 174  SER n 
2 175  LYS n 
2 176  ASP n 
2 177  LYS n 
2 178  THR n 
2 179  PHE n 
2 180  ILE n 
2 181  PRO n 
2 182  ALA n 
2 183  ILE n 
2 184  PRO n 
2 185  LEU n 
2 186  PRO n 
2 187  LYS n 
2 188  ARG n 
2 189  ARG n 
2 190  SER n 
2 191  LYS n 
2 192  LYS n 
2 193  ALA n 
2 194  LYS n 
2 195  LYS n 
2 196  ALA n 
2 197  GLU n 
2 198  GLU n 
2 199  GLU n 
2 200  ALA n 
2 201  ALA n 
2 202  LEU n 
2 203  ASN n 
2 204  MET n 
2 205  GLN n 
2 206  GLY n 
2 207  ARG n 
2 208  SER n 
2 209  SER n 
2 210  SER n 
2 211  THR n 
2 212  GLU n 
2 213  ASN n 
2 214  PHE n 
2 215  ALA n 
2 216  ALA n 
2 217  GLU n 
2 218  PRO n 
2 219  VAL n 
2 220  PRO n 
2 221  GLY n 
2 222  ALA n 
2 223  GLU n 
2 224  PRO n 
2 225  ARG n 
2 226  GLY n 
2 227  GLN n 
2 228  ASP n 
2 229  GLU n 
2 230  LEU n 
2 231  GLN n 
2 232  ARG n 
2 233  MET n 
2 234  ARG n 
2 235  SER n 
2 236  GLN n 
2 237  VAL n 
2 238  SER n 
2 239  ASN n 
2 240  TRP n 
2 241  ASP n 
2 242  GLU n 
2 243  ASP n 
2 244  PRO n 
2 245  GLU n 
2 246  ALA n 
2 247  GLY n 
2 248  ASP n 
2 249  SER n 
2 250  PRO n 
2 251  GLY n 
2 252  GLU n 
2 253  LEU n 
2 254  GLY n 
2 255  TRP n 
2 256  HIS n 
2 257  ARG n 
2 258  THR n 
2 259  ILE n 
2 260  TRP n 
2 261  GLU n 
2 262  ASP n 
2 263  VAL n 
2 264  LYS n 
2 265  VAL n 
2 266  GLY n 
2 267  ASP n 
2 268  PHE n 
2 269  VAL n 
2 270  LYS n 
2 271  ILE n 
2 272  TYR n 
2 273  GLU n 
2 274  ASN n 
2 275  GLU n 
2 276  GLN n 
2 277  PHE n 
2 278  PRO n 
2 279  ALA n 
2 280  ASP n 
2 281  ILE n 
2 282  VAL n 
2 283  ILE n 
2 284  CYS n 
2 285  ALA n 
2 286  THR n 
2 287  SER n 
2 288  GLU n 
2 289  GLU n 
2 290  GLU n 
2 291  ASP n 
2 292  VAL n 
2 293  ALA n 
2 294  TYR n 
2 295  ILE n 
2 296  GLU n 
2 297  THR n 
2 298  LYS n 
2 299  ASN n 
2 300  LEU n 
2 301  ASP n 
2 302  GLY n 
2 303  GLU n 
2 304  THR n 
2 305  ASN n 
2 306  LEU n 
2 307  LYS n 
2 308  SER n 
2 309  ARG n 
2 310  ASN n 
2 311  GLY n 
2 312  VAL n 
2 313  PRO n 
2 314  GLY n 
2 315  LEU n 
2 316  SER n 
2 317  HIS n 
2 318  LEU n 
2 319  ASN n 
2 320  THR n 
2 321  ALA n 
2 322  GLU n 
2 323  ALA n 
2 324  CYS n 
2 325  ALA n 
2 326  LYS n 
2 327  ALA n 
2 328  HIS n 
2 329  LEU n 
2 330  CYS n 
2 331  ILE n 
2 332  ASP n 
2 333  LEU n 
2 334  ASP n 
2 335  ALA n 
2 336  PRO n 
2 337  GLU n 
2 338  SER n 
2 339  ASN n 
2 340  MET n 
2 341  PHE n 
2 342  ARG n 
2 343  LEU n 
2 344  ASN n 
2 345  GLY n 
2 346  ALA n 
2 347  VAL n 
2 348  ILE n 
2 349  ASN n 
2 350  LEU n 
2 351  GLU n 
2 352  GLU n 
2 353  TYR n 
2 354  ASP n 
2 355  GLU n 
2 356  ASP n 
2 357  GLU n 
2 358  GLN n 
2 359  HIS n 
2 360  PRO n 
2 361  ILE n 
2 362  HIS n 
2 363  PRO n 
2 364  ILE n 
2 365  THR n 
2 366  LEU n 
2 367  GLU n 
2 368  THR n 
2 369  THR n 
2 370  MET n 
2 371  LEU n 
2 372  ARG n 
2 373  GLY n 
2 374  CYS n 
2 375  VAL n 
2 376  LEU n 
2 377  LYS n 
2 378  ASN n 
2 379  THR n 
2 380  ALA n 
2 381  TRP n 
2 382  VAL n 
2 383  ILE n 
2 384  GLY n 
2 385  ILE n 
2 386  ILE n 
2 387  VAL n 
2 388  TYR n 
2 389  THR n 
2 390  GLY n 
2 391  GLU n 
2 392  ASP n 
2 393  THR n 
2 394  LYS n 
2 395  ILE n 
2 396  ILE n 
2 397  ARG n 
2 398  ASN n 
2 399  ALA n 
2 400  GLY n 
2 401  ALA n 
2 402  THR n 
2 403  PRO n 
2 404  SER n 
2 405  LYS n 
2 406  ARG n 
2 407  SER n 
2 408  LYS n 
2 409  VAL n 
2 410  GLU n 
2 411  LYS n 
2 412  GLN n 
2 413  MET n 
2 414  ASN n 
2 415  PRO n 
2 416  GLN n 
2 417  VAL n 
2 418  ILE n 
2 419  ILE n 
2 420  ASN n 
2 421  LEU n 
2 422  VAL n 
2 423  ILE n 
2 424  LEU n 
2 425  ALA n 
2 426  ALA n 
2 427  ILE n 
2 428  ALA n 
2 429  VAL n 
2 430  VAL n 
2 431  CYS n 
2 432  ALA n 
2 433  ILE n 
2 434  VAL n 
2 435  ASP n 
2 436  HIS n 
2 437  VAL n 
2 438  ASN n 
2 439  GLU n 
2 440  VAL n 
2 441  GLU n 
2 442  TRP n 
2 443  ASP n 
2 444  ARG n 
2 445  GLN n 
2 446  GLN n 
2 447  ALA n 
2 448  TYR n 
2 449  TRP n 
2 450  MET n 
2 451  LEU n 
2 452  PHE n 
2 453  ALA n 
2 454  ASP n 
2 455  THR n 
2 456  SER n 
2 457  GLY n 
2 458  ASP n 
2 459  ASN n 
2 460  PRO n 
2 461  ASN n 
2 462  ILE n 
2 463  ASN n 
2 464  GLY n 
2 465  LEU n 
2 466  VAL n 
2 467  THR n 
2 468  PHE n 
2 469  ALA n 
2 470  ASN n 
2 471  ALA n 
2 472  PHE n 
2 473  ILE n 
2 474  THR n 
2 475  PHE n 
2 476  GLN n 
2 477  ASN n 
2 478  ILE n 
2 479  VAL n 
2 480  PRO n 
2 481  ILE n 
2 482  SER n 
2 483  LEU n 
2 484  TYR n 
2 485  ILE n 
2 486  SER n 
2 487  ILE n 
2 488  GLU n 
2 489  ALA n 
2 490  VAL n 
2 491  ARG n 
2 492  THR n 
2 493  ILE n 
2 494  GLN n 
2 495  ALA n 
2 496  ALA n 
2 497  PHE n 
2 498  ILE n 
2 499  TYR n 
2 500  TRP n 
2 501  ASP n 
2 502  ARG n 
2 503  ASP n 
2 504  ILE n 
2 505  LYS n 
2 506  TYR n 
2 507  LYS n 
2 508  LYS n 
2 509  ASP n 
2 510  GLY n 
2 511  VAL n 
2 512  THR n 
2 513  THR n 
2 514  ARG n 
2 515  THR n 
2 516  THR n 
2 517  ALA n 
2 518  ARG n 
2 519  SER n 
2 520  TRP n 
2 521  ASN n 
2 522  LEU n 
2 523  SER n 
2 524  ASP n 
2 525  ASP n 
2 526  LEU n 
2 527  GLY n 
2 528  GLN n 
2 529  ILE n 
2 530  GLU n 
2 531  TYR n 
2 532  ILE n 
2 533  PHE n 
2 534  SER n 
2 535  ASP n 
2 536  LYS n 
2 537  THR n 
2 538  GLY n 
2 539  THR n 
2 540  LEU n 
2 541  THR n 
2 542  GLN n 
2 543  ASN n 
2 544  ALA n 
2 545  MET n 
2 546  ILE n 
2 547  PHE n 
2 548  ARG n 
2 549  GLN n 
2 550  CYS n 
2 551  SER n 
2 552  VAL n 
2 553  GLY n 
2 554  GLY n 
2 555  LYS n 
2 556  ILE n 
2 557  TYR n 
2 558  THR n 
2 559  GLY n 
2 560  ASP n 
2 561  GLY n 
2 562  LEU n 
2 563  PRO n 
2 564  PRO n 
2 565  SER n 
2 566  HIS n 
2 567  PRO n 
2 568  THR n 
2 569  ILE n 
2 570  THR n 
2 571  HIS n 
2 572  GLN n 
2 573  HIS n 
2 574  GLN n 
2 575  PRO n 
2 576  PRO n 
2 577  PRO n 
2 578  VAL n 
2 579  HIS n 
2 580  GLN n 
2 581  HIS n 
2 582  ASP n 
2 583  ASP n 
2 584  GLN n 
2 585  ASP n 
2 586  ASP n 
2 587  PRO n 
2 588  ILE n 
2 589  ALA n 
2 590  LYS n 
2 591  SER n 
2 592  ALA n 
2 593  SER n 
2 594  GLU n 
2 595  SER n 
2 596  ASP n 
2 597  ASP n 
2 598  SER n 
2 599  ASP n 
2 600  PRO n 
2 601  LYS n 
2 602  LYS n 
2 603  ILE n 
2 604  SER n 
2 605  THR n 
2 606  GLU n 
2 607  ASP n 
2 608  PRO n 
2 609  ASP n 
2 610  GLU n 
2 611  ILE n 
2 612  LYS n 
2 613  VAL n 
2 614  THR n 
2 615  LEU n 
2 616  PRO n 
2 617  LYS n 
2 618  GLU n 
2 619  VAL n 
2 620  LEU n 
2 621  ALA n 
2 622  THR n 
2 623  PHE n 
2 624  HIS n 
2 625  ASP n 
2 626  ALA n 
2 627  GLU n 
2 628  LEU n 
2 629  ASP n 
2 630  LYS n 
2 631  ASP n 
2 632  LEU n 
2 633  GLU n 
2 634  ALA n 
2 635  HIS n 
2 636  ASP n 
2 637  SER n 
2 638  GLU n 
2 639  GLN n 
2 640  SER n 
2 641  ARG n 
2 642  ILE n 
2 643  LEU n 
2 644  HIS n 
2 645  GLY n 
2 646  PHE n 
2 647  PHE n 
2 648  ALA n 
2 649  VAL n 
2 650  LEU n 
2 651  GLY n 
2 652  LEU n 
2 653  CYS n 
2 654  HIS n 
2 655  THR n 
2 656  VAL n 
2 657  LEU n 
2 658  ALA n 
2 659  ALA n 
2 660  GLU n 
2 661  THR n 
2 662  GLU n 
2 663  PRO n 
2 664  GLY n 
2 665  VAL n 
2 666  ILE n 
2 667  GLU n 
2 668  TYR n 
2 669  LYS n 
2 670  ALA n 
2 671  GLN n 
2 672  SER n 
2 673  PRO n 
2 674  ASP n 
2 675  GLU n 
2 676  ALA n 
2 677  ALA n 
2 678  LEU n 
2 679  VAL n 
2 680  GLN n 
2 681  SER n 
2 682  ALA n 
2 683  ALA n 
2 684  ASP n 
2 685  VAL n 
2 686  GLY n 
2 687  PHE n 
2 688  VAL n 
2 689  PHE n 
2 690  ARG n 
2 691  GLY n 
2 692  ARG n 
2 693  ASP n 
2 694  HIS n 
2 695  ASN n 
2 696  ILE n 
2 697  LEU n 
2 698  ARG n 
2 699  MET n 
2 700  SER n 
2 701  THR n 
2 702  PRO n 
2 703  PHE n 
2 704  SER n 
2 705  ASP n 
2 706  VAL n 
2 707  SER n 
2 708  ASP n 
2 709  GLU n 
2 710  TYR n 
2 711  GLU n 
2 712  LEU n 
2 713  LEU n 
2 714  HIS n 
2 715  VAL n 
2 716  LEU n 
2 717  GLU n 
2 718  PHE n 
2 719  ASN n 
2 720  SER n 
2 721  ALA n 
2 722  ARG n 
2 723  LYS n 
2 724  ARG n 
2 725  MET n 
2 726  SER n 
2 727  VAL n 
2 728  ILE n 
2 729  LEU n 
2 730  ARG n 
2 731  LYS n 
2 732  LEU n 
2 733  ASP n 
2 734  GLU n 
2 735  ASP n 
2 736  GLY n 
2 737  ARG n 
2 738  ILE n 
2 739  PHE n 
2 740  LEU n 
2 741  LEU n 
2 742  CYS n 
2 743  LYS n 
2 744  GLY n 
2 745  ALA n 
2 746  ASP n 
2 747  ASN n 
2 748  VAL n 
2 749  ILE n 
2 750  PHE n 
2 751  GLU n 
2 752  ARG n 
2 753  LEU n 
2 754  THR n 
2 755  LYS n 
2 756  ASP n 
2 757  SER n 
2 758  ASN n 
2 759  GLN n 
2 760  ARG n 
2 761  GLU n 
2 762  MET n 
2 763  ARG n 
2 764  GLU n 
2 765  LYS n 
2 766  THR n 
2 767  ASP n 
2 768  GLN n 
2 769  ASP n 
2 770  LEU n 
2 771  GLN n 
2 772  TYR n 
2 773  PHE n 
2 774  ALA n 
2 775  SER n 
2 776  GLU n 
2 777  GLY n 
2 778  LEU n 
2 779  ARG n 
2 780  THR n 
2 781  LEU n 
2 782  CYS n 
2 783  LEU n 
2 784  ALA n 
2 785  TYR n 
2 786  ARG n 
2 787  ILE n 
2 788  LEU n 
2 789  ASP n 
2 790  PRO n 
2 791  GLN n 
2 792  VAL n 
2 793  TYR n 
2 794  GLU n 
2 795  GLN n 
2 796  TRP n 
2 797  ALA n 
2 798  LYS n 
2 799  GLU n 
2 800  TYR n 
2 801  HIS n 
2 802  ASN n 
2 803  ALA n 
2 804  THR n 
2 805  VAL n 
2 806  ALA n 
2 807  LEU n 
2 808  GLN n 
2 809  ASP n 
2 810  ARG n 
2 811  GLU n 
2 812  GLU n 
2 813  ARG n 
2 814  ILE n 
2 815  GLU n 
2 816  SER n 
2 817  VAL n 
2 818  SER n 
2 819  SER n 
2 820  SER n 
2 821  ILE n 
2 822  GLU n 
2 823  ARG n 
2 824  ASP n 
2 825  LEU n 
2 826  ILE n 
2 827  LEU n 
2 828  LEU n 
2 829  GLY n 
2 830  ALA n 
2 831  THR n 
2 832  ALA n 
2 833  ILE n 
2 834  GLU n 
2 835  ASP n 
2 836  LYS n 
2 837  LEU n 
2 838  GLN n 
2 839  ASP n 
2 840  GLY n 
2 841  VAL n 
2 842  PRO n 
2 843  ASP n 
2 844  THR n 
2 845  ILE n 
2 846  SER n 
2 847  ASP n 
2 848  LEU n 
2 849  LYS n 
2 850  ARG n 
2 851  ALA n 
2 852  GLY n 
2 853  ILE n 
2 854  LYS n 
2 855  VAL n 
2 856  TRP n 
2 857  VAL n 
2 858  ALA n 
2 859  THR n 
2 860  GLY n 
2 861  ASP n 
2 862  LYS n 
2 863  LEU n 
2 864  GLU n 
2 865  THR n 
2 866  ALA n 
2 867  VAL n 
2 868  ALA n 
2 869  ILE n 
2 870  GLY n 
2 871  TYR n 
2 872  THR n 
2 873  THR n 
2 874  ASN n 
2 875  LEU n 
2 876  LEU n 
2 877  THR n 
2 878  LYS n 
2 879  ASP n 
2 880  THR n 
2 881  ASN n 
2 882  LEU n 
2 883  ILE n 
2 884  VAL n 
2 885  VAL n 
2 886  ARG n 
2 887  GLU n 
2 888  GLY n 
2 889  ARG n 
2 890  HIS n 
2 891  SER n 
2 892  ILE n 
2 893  GLY n 
2 894  ASP n 
2 895  GLN n 
2 896  LEU n 
2 897  ARG n 
2 898  GLU n 
2 899  ALA n 
2 900  LEU n 
2 901  GLU n 
2 902  GLU n 
2 903  PHE n 
2 904  PHE n 
2 905  GLY n 
2 906  GLU n 
2 907  ASP n 
2 908  ALA n 
2 909  GLY n 
2 910  LEU n 
2 911  ARG n 
2 912  THR n 
2 913  THR n 
2 914  LEU n 
2 915  SER n 
2 916  ARG n 
2 917  ILE n 
2 918  ASP n 
2 919  SER n 
2 920  ARG n 
2 921  ARG n 
2 922  ASN n 
2 923  SER n 
2 924  MET n 
2 925  ASP n 
2 926  PRO n 
2 927  PRO n 
2 928  ARG n 
2 929  LEU n 
2 930  THR n 
2 931  ARG n 
2 932  VAL n 
2 933  ASN n 
2 934  THR n 
2 935  GLY n 
2 936  VAL n 
2 937  ARG n 
2 938  SER n 
2 939  LEU n 
2 940  VAL n 
2 941  GLY n 
2 942  ARG n 
2 943  ASP n 
2 944  ASN n 
2 945  GLY n 
2 946  THR n 
2 947  ARG n 
2 948  PRO n 
2 949  GLY n 
2 950  GLY n 
2 951  PHE n 
2 952  SER n 
2 953  LEU n 
2 954  VAL n 
2 955  ILE n 
2 956  GLU n 
2 957  GLY n 
2 958  HIS n 
2 959  ALA n 
2 960  LEU n 
2 961  ALA n 
2 962  HIS n 
2 963  CYS n 
2 964  PHE n 
2 965  ASP n 
2 966  ASP n 
2 967  GLU n 
2 968  GLU n 
2 969  THR n 
2 970  GLU n 
2 971  ALA n 
2 972  LEU n 
2 973  LEU n 
2 974  LEU n 
2 975  ALA n 
2 976  LEU n 
2 977  SER n 
2 978  THR n 
2 979  ARG n 
2 980  CYS n 
2 981  ASN n 
2 982  THR n 
2 983  VAL n 
2 984  ILE n 
2 985  CYS n 
2 986  CYS n 
2 987  ARG n 
2 988  VAL n 
2 989  SER n 
2 990  PRO n 
2 991  LEU n 
2 992  GLN n 
2 993  LYS n 
2 994  ALA n 
2 995  GLN n 
2 996  ILE n 
2 997  VAL n 
2 998  HIS n 
2 999  LEU n 
2 1000 ILE n 
2 1001 LYS n 
2 1002 ASP n 
2 1003 ASN n 
2 1004 LEU n 
2 1005 GLY n 
2 1006 VAL n 
2 1007 MET n 
2 1008 CYS n 
2 1009 LEU n 
2 1010 ALA n 
2 1011 ILE n 
2 1012 GLY n 
2 1013 ASP n 
2 1014 GLY n 
2 1015 ALA n 
2 1016 ASN n 
2 1017 ASP n 
2 1018 VAL n 
2 1019 SER n 
2 1020 MET n 
2 1021 ILE n 
2 1022 GLN n 
2 1023 ALA n 
2 1024 ALA n 
2 1025 ASP n 
2 1026 VAL n 
2 1027 GLY n 
2 1028 VAL n 
2 1029 GLY n 
2 1030 ILE n 
2 1031 SER n 
2 1032 GLY n 
2 1033 GLU n 
2 1034 GLU n 
2 1035 GLY n 
2 1036 LEU n 
2 1037 GLN n 
2 1038 ALA n 
2 1039 VAL n 
2 1040 ASN n 
2 1041 SER n 
2 1042 SER n 
2 1043 ASP n 
2 1044 TYR n 
2 1045 ALA n 
2 1046 ILE n 
2 1047 ALA n 
2 1048 GLN n 
2 1049 PHE n 
2 1050 ARG n 
2 1051 TYR n 
2 1052 LEU n 
2 1053 LYS n 
2 1054 ARG n 
2 1055 LEU n 
2 1056 LEU n 
2 1057 LEU n 
2 1058 VAL n 
2 1059 HIS n 
2 1060 GLY n 
2 1061 HIS n 
2 1062 TRP n 
2 1063 SER n 
2 1064 TYR n 
2 1065 PHE n 
2 1066 ARG n 
2 1067 ASN n 
2 1068 SER n 
2 1069 SER n 
2 1070 MET n 
2 1071 ILE n 
2 1072 LEU n 
2 1073 ASN n 
2 1074 PHE n 
2 1075 PHE n 
2 1076 TYR n 
2 1077 LYS n 
2 1078 ASN n 
2 1079 ILE n 
2 1080 ILE n 
2 1081 GLY n 
2 1082 ILE n 
2 1083 GLY n 
2 1084 VAL n 
2 1085 LEU n 
2 1086 PHE n 
2 1087 TRP n 
2 1088 PHE n 
2 1089 MET n 
2 1090 ILE n 
2 1091 TYR n 
2 1092 CYS n 
2 1093 GLY n 
2 1094 TRP n 
2 1095 SER n 
2 1096 THR n 
2 1097 THR n 
2 1098 TYR n 
2 1099 VAL n 
2 1100 PHE n 
2 1101 ALA n 
2 1102 TYR n 
2 1103 VAL n 
2 1104 TYR n 
2 1105 LEU n 
2 1106 LEU n 
2 1107 PHE n 
2 1108 TRP n 
2 1109 ASN n 
2 1110 VAL n 
2 1111 PHE n 
2 1112 TRP n 
2 1113 THR n 
2 1114 LEU n 
2 1115 VAL n 
2 1116 PRO n 
2 1117 VAL n 
2 1118 ILE n 
2 1119 ALA n 
2 1120 ILE n 
2 1121 GLY n 
2 1122 LEU n 
2 1123 PHE n 
2 1124 ASP n 
2 1125 ARG n 
2 1126 ASN n 
2 1127 ILE n 
2 1128 ASP n 
2 1129 ASP n 
2 1130 GLU n 
2 1131 THR n 
2 1132 LEU n 
2 1133 MET n 
2 1134 ALA n 
2 1135 LEU n 
2 1136 PRO n 
2 1137 GLU n 
2 1138 LEU n 
2 1139 TYR n 
2 1140 ARG n 
2 1141 ALA n 
2 1142 SER n 
2 1143 ARG n 
2 1144 GLU n 
2 1145 GLY n 
2 1146 LYS n 
2 1147 TYR n 
2 1148 PHE n 
2 1149 GLY n 
2 1150 LEU n 
2 1151 MET n 
2 1152 ARG n 
2 1153 PHE n 
2 1154 ALA n 
2 1155 TYR n 
2 1156 TYR n 
2 1157 ILE n 
2 1158 PHE n 
2 1159 GLU n 
2 1160 GLY n 
2 1161 VAL n 
2 1162 TYR n 
2 1163 GLN n 
2 1164 SER n 
2 1165 ALA n 
2 1166 VAL n 
2 1167 ILE n 
2 1168 TYR n 
2 1169 PHE n 
2 1170 PHE n 
2 1171 LEU n 
2 1172 ASN n 
2 1173 TYR n 
2 1174 THR n 
2 1175 TYR n 
2 1176 VAL n 
2 1177 THR n 
2 1178 THR n 
2 1179 THR n 
2 1180 ALA n 
2 1181 ARG n 
2 1182 GLY n 
2 1183 ASP n 
2 1184 GLY n 
2 1185 TYR n 
2 1186 ASP n 
2 1187 VAL n 
2 1188 TYR n 
2 1189 MET n 
2 1190 TYR n 
2 1191 GLU n 
2 1192 MET n 
2 1193 SER n 
2 1194 THR n 
2 1195 THR n 
2 1196 GLN n 
2 1197 ALA n 
2 1198 ILE n 
2 1199 GLY n 
2 1200 ALA n 
2 1201 VAL n 
2 1202 MET n 
2 1203 VAL n 
2 1204 ALA n 
2 1205 ASN n 
2 1206 LEU n 
2 1207 PHE n 
2 1208 SER n 
2 1209 GLY n 
2 1210 LEU n 
2 1211 ASN n 
2 1212 ILE n 
2 1213 ASP n 
2 1214 ALA n 
2 1215 TRP n 
2 1216 THR n 
2 1217 GLY n 
2 1218 TRP n 
2 1219 VAL n 
2 1220 TRP n 
2 1221 PHE n 
2 1222 ALA n 
2 1223 ILE n 
2 1224 TRP n 
2 1225 PHE n 
2 1226 GLY n 
2 1227 PRO n 
2 1228 PHE n 
2 1229 LEU n 
2 1230 ILE n 
2 1231 TRP n 
2 1232 VAL n 
2 1233 PHE n 
2 1234 THR n 
2 1235 ALA n 
2 1236 VAL n 
2 1237 TYR n 
2 1238 SER n 
2 1239 VAL n 
2 1240 ILE n 
2 1241 PRO n 
2 1242 PRO n 
2 1243 SER n 
2 1244 SER n 
2 1245 PHE n 
2 1246 TYR n 
2 1247 THR n 
2 1248 GLY n 
2 1249 VAL n 
2 1250 TYR n 
2 1251 GLY n 
2 1252 ASN n 
2 1253 ASP n 
2 1254 VAL n 
2 1255 PHE n 
2 1256 LEU n 
2 1257 PHE n 
2 1258 ARG n 
2 1259 SER n 
2 1260 ALA n 
2 1261 ALA n 
2 1262 TYR n 
2 1263 TRP n 
2 1264 PHE n 
2 1265 GLY n 
2 1266 TRP n 
2 1267 PRO n 
2 1268 PHE n 
2 1269 VAL n 
2 1270 THR n 
2 1271 ILE n 
2 1272 ILE n 
2 1273 ALA n 
2 1274 LEU n 
2 1275 LEU n 
2 1276 PRO n 
2 1277 ARG n 
2 1278 TYR n 
2 1279 LEU n 
2 1280 ILE n 
2 1281 LYS n 
2 1282 THR n 
2 1283 PHE n 
2 1284 ARG n 
2 1285 GLN n 
2 1286 ASN n 
2 1287 ILE n 
2 1288 PHE n 
2 1289 PRO n 
2 1290 ASN n 
2 1291 ASP n 
2 1292 VAL n 
2 1293 ASP n 
2 1294 THR n 
2 1295 MET n 
2 1296 ARG n 
2 1297 LEU n 
2 1298 VAL n 
2 1299 ARG n 
2 1300 LYS n 
2 1301 TYR n 
2 1302 HIS n 
2 1303 PRO n 
2 1304 GLU n 
2 1305 VAL n 
2 1306 ASP n 
2 1307 LEU n 
2 1308 TYR n 
2 1309 ASN n 
2 1310 HIS n 
2 1311 PRO n 
2 1312 MET n 
2 1313 LEU n 
2 1314 GLY n 
2 1315 GLY n 
2 1316 LYS n 
2 1317 LEU n 
2 1318 ALA n 
2 1319 PRO n 
2 1320 LYS n 
2 1321 LYS n 
2 1322 ASP n 
2 1323 GLU n 
2 1324 ASP n 
2 1325 GLU n 
2 1326 SER n 
2 1327 ASP n 
2 1328 TYR n 
2 1329 GLY n 
2 1330 GLU n 
2 1331 GLU n 
2 1332 PRO n 
2 1333 PHE n 
2 1334 ASP n 
2 1335 GLY n 
2 1336 PRO n 
2 1337 GLU n 
2 1338 GLY n 
2 1339 ARG n 
2 1340 ARG n 
2 1341 SER n 
2 1342 SER n 
2 1343 ILE n 
2 1344 LYS n 
2 1345 MET n 
2 1346 ALA n 
2 1347 ASN n 
2 1348 LEU n 
2 1349 ARG n 
2 1350 HIS n 
2 1351 SER n 
2 1352 HIS n 
2 1353 GLY n 
2 1354 ALA n 
2 1355 PHE n 
2 1356 GLY n 
2 1357 ARG n 
2 1358 GLY n 
2 1359 ASP n 
2 1360 GLN n 
2 1361 ALA n 
2 1362 GLY n 
2 1363 ASP n 
2 1364 MET n 
2 1365 GLU n 
2 1366 LEU n 
2 1367 GLY n 
2 1368 MET n 
2 1369 GLY n 
2 1370 ARG n 
2 1371 LYS n 
2 1372 SER n 
2 1373 LEU n 
2 1374 GLY n 
2 1375 ASN n 
2 1376 ARG n 
2 1377 PRO n 
2 1378 GLY n 
2 1379 LEU n 
2 1380 ARG n 
2 1381 SER n 
2 1382 SER n 
2 1383 MET n 
2 1384 ASP n 
2 1385 SER n 
2 1386 SER n 
2 1387 ARG n 
2 1388 PHE n 
2 1389 GLY n 
2 1390 ILE n 
2 1391 HIS n 
2 1392 SER n 
2 1393 GLY n 
2 1394 ALA n 
2 1395 ARG n 
2 1396 GLY n 
2 1397 SER n 
2 1398 THR n 
2 1399 VAL n 
2 1400 ASP n 
2 1401 MET n 
2 1402 SER n 
2 1403 THR n 
2 1404 GLY n 
2 1405 LEU n 
2 1406 GLU n 
2 1407 GLN n 
2 1408 PRO n 
2 1409 PRO n 
2 1410 SER n 
2 1411 ARG n 
2 1412 GLY n 
2 1413 PHE n 
2 1414 GLY n 
2 1415 PHE n 
2 1416 THR n 
2 1417 MET n 
2 1418 GLU n 
2 1419 GLU n 
2 1420 GLY n 
2 1421 GLY n 
2 1422 VAL n 
2 1423 ALA n 
2 1424 ILE n 
2 1425 GLN n 
2 1426 ARG n 
2 1427 MET n 
2 1428 GLN n 
2 1429 SER n 
2 1430 ARG n 
2 1431 LEU n 
2 1432 SER n 
2 1433 GLN n 
2 1434 THR n 
2 1435 SER n 
2 1436 SER n 
2 1437 HIS n 
2 1438 ALA n 
2 1439 SER n 
2 1440 ARG n 
2 1441 SER n 
2 1442 ARG n 
2 1443 TRP n 
2 1444 PRO n 
2 1445 ARG n 
2 1446 PHE n 
2 1447 ASN n 
2 1448 ASN n 
2 1449 ASN n 
2 1450 SER n 
2 1451 SER n 
2 1452 SER n 
2 1453 SER n 
2 1454 HIS n 
2 1455 PRO n 
2 1456 PHE n 
2 1457 GLU n 
2 1458 THR n 
2 1459 LYS n 
2 1460 PRO n 
2 1461 PRO n 
2 1462 SER n 
2 1463 SER n 
2 1464 MET n 
2 1465 SER n 
2 1466 LYS n 
2 1467 LEU n 
2 1468 ARG n 
2 1469 SER n 
2 1470 ARG n 
2 1471 ALA n 
2 1472 GLY n 
2 1473 SER n 
2 1474 ILE n 
2 1475 LEU n 
2 1476 THR n 
2 1477 ARG n 
2 1478 LYS n 
2 1479 ARG n 
2 1480 ALA n 
2 1481 ASP n 
2 1482 THR n 
2 1483 THR n 
2 1484 ASP n 
2 1485 THR n 
2 1486 ARG n 
2 1487 ASN n 
2 1488 SER n 
2 1489 ASP n 
2 1490 ASP n 
2 1491 LYS n 
2 1492 SER n 
2 1493 LEU n 
2 1494 SER n 
2 1495 SER n 
2 1496 PRO n 
2 1497 VAL n 
2 1498 LYS n 
2 1499 THR n 
2 1500 GLY n 
2 1501 PHE n 
2 1502 PHE n 
2 1503 GLY n 
2 1504 ARG n 
2 1505 HIS n 
2 1506 MET n 
2 1507 PRO n 
2 1508 GLY n 
2 1509 GLN n 
2 1510 ASN n 
2 1511 HIS n 
2 1512 GLY n 
2 1513 GLN n 
2 1514 HIS n 
2 1515 GLU n 
2 1516 GLY n 
2 1517 ARG n 
2 1518 SER n 
2 1519 MET n 
2 1520 GLY n 
2 1521 THR n 
2 1522 PRO n 
2 1523 LEU n 
2 1524 LYS n 
2 1525 SER n 
2 1526 GLU n 
2 1527 THR n 
2 1528 GLY n 
2 1529 ARG n 
2 1530 GLY n 
2 1531 ASP n 
2 1532 ASN n 
2 1533 TRP n 
2 1534 GLU n 
2 1535 GLU n 
2 1536 GLU n 
2 1537 GLU n 
2 1538 LEU n 
2 1539 GLU n 
2 1540 ASP n 
2 1541 GLU n 
2 1542 SER n 
2 1543 LEU n 
2 1544 GLY n 
2 1545 ARG n 
2 1546 GLY n 
2 1547 PHE n 
2 1548 GLY n 
2 1549 VAL n 
2 1550 GLY n 
2 1551 GLN n 
2 1552 ASN n 
2 1553 MET n 
2 1554 ALA n 
2 1555 PRO n 
2 1556 PRO n 
2 1557 GLU n 
2 1558 ILE n 
2 1559 PRO n 
2 1560 ARG n 
2 1561 MET n 
2 1562 ASP n 
2 1563 TYR n 
2 1564 LYS n 
2 1565 ASP n 
2 1566 ASP n 
2 1567 ASP n 
2 1568 ASP n 
2 1569 LYS n 
2 1570 ILE n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 411  ? ? CNAG_06465 ? ? ? ? ? ? 'Cryptococcus neoformans var. grubii H99' 235443 ? ? ? ? ? ? ? 
;brewer's yeast
;
'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 1570 ? ? CNAG_06469 ? ? ? ? ? ? 'Cryptococcus neoformans var. grubii H99' 235443 ? ? ? ? ? ? ? 
;brewer's yeast
;
'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
3 oligosaccharide 
4 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 3 DGlcpNAcb1-4DGlcpNAcb1-ROH                                                                                                  
'Glycam Condensed Sequence' GMML       1.0   
2 3 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1'                                                                       
WURCS                       PDB2Glycan 1.1.0 
3 3 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'                                                                             
LINUCS                      PDB-CARE   ?     
4 4 'DManpa1-4DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH'                                                          
'Glycam Condensed Sequence' GMML       1.0   
5 4 'WURCS=2.0/3,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e4-f1'         
WURCS                       PDB2Glycan 1.1.0 
6 4 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(4+1)][a-D-Manp]{}}}}}' 
LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 3 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
3 4 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
4 4 4 MAN C1 O1 3 BMA O6 HO6 sing ? 
5 4 5 MAN C1 O1 4 MAN O4 HO4 sing ? 
6 4 6 MAN C1 O1 3 BMA O3 HO3 sing ? 
# 
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 
A1BD6 non-polymer                   . 
;(3R,4R,5S)-3,4-dihydroxy-5-[(1R,2R,3S,4S,5R,6R,8E,10E,14E,16Z)-1,2,3,4,5-pentahydroxy-6,20,20-trimethylhenicosa-8,10,14,16-tetraen-1-yl]oxolan-2-one
;
? 'C28 H46 O9'     526.659 
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 
BEF   non-polymer                   . 'BERYLLIUM TRIFLUORIDE ION' ? 'Be F3 -1'       66.007  
BMA   'D-saccharide, beta linking'  . beta-D-mannopyranose 'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'      180.156 
CYS   'L-peptide linking'           y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking'           y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking'           y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'             y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking'           y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
ILE   'L-peptide linking'           y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking'           y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking'           y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MAN   'D-saccharide, alpha linking' . alpha-D-mannopyranose 'alpha-D-mannose; D-mannose; mannose' 'C6 H12 O6'      180.156 
MET   'L-peptide linking'           y METHIONINE ? 'C5 H11 N O2 S'  149.211 
MG    non-polymer                   . 'MAGNESIUM ION' ? 'Mg 2'           24.305  
NAG   'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE   'L-peptide linking'           y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking'           y PROLINE ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking'           y SERINE ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking'           y THREONINE ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking'           y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking'           y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking'           y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
MAN 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpa                         
MAN 'COMMON NAME'                         GMML     1.0 a-D-mannopyranose              
MAN 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Manp                       
MAN 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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    ?    ?   ?   B . n 
A 1 2    ALA 2    2    ?    ?   ?   B . n 
A 1 3    ILE 3    3    ?    ?   ?   B . n 
A 1 4    PHE 4    4    ?    ?   ?   B . n 
A 1 5    ASN 5    5    ?    ?   ?   B . n 
A 1 6    ARG 6    6    ?    ?   ?   B . n 
A 1 7    LYS 7    7    ?    ?   ?   B . n 
A 1 8    PRO 8    8    ?    ?   ?   B . n 
A 1 9    LYS 9    9    ?    ?   ?   B . n 
A 1 10   ALA 10   10   ?    ?   ?   B . n 
A 1 11   ARG 11   11   ?    ?   ?   B . n 
A 1 12   LEU 12   12   ?    ?   ?   B . n 
A 1 13   ASP 13   13   ?    ?   ?   B . n 
A 1 14   GLY 14   14   ?    ?   ?   B . n 
A 1 15   GLU 15   15   ?    ?   ?   B . n 
A 1 16   PRO 16   16   ?    ?   ?   B . n 
A 1 17   ALA 17   17   ?    ?   ?   B . n 
A 1 18   PRO 18   18   ?    ?   ?   B . n 
A 1 19   THR 19   19   ?    ?   ?   B . n 
A 1 20   GLU 20   20   ?    ?   ?   B . n 
A 1 21   LYS 21   21   ?    ?   ?   B . n 
A 1 22   GLU 22   22   ?    ?   ?   B . n 
A 1 23   LYS 23   23   ?    ?   ?   B . n 
A 1 24   VAL 24   24   ?    ?   ?   B . n 
A 1 25   LYS 25   25   ?    ?   ?   B . n 
A 1 26   TRP 26   26   ?    ?   ?   B . n 
A 1 27   SER 27   27   ?    ?   ?   B . n 
A 1 28   LYS 28   28   ?    ?   ?   B . n 
A 1 29   ARG 29   29   ?    ?   ?   B . n 
A 1 30   PRO 30   30   ?    ?   ?   B . n 
A 1 31   ALA 31   31   ?    ?   ?   B . n 
A 1 32   ASN 32   32   ?    ?   ?   B . n 
A 1 33   THR 33   33   ?    ?   ?   B . n 
A 1 34   ALA 34   34   ?    ?   ?   B . n 
A 1 35   PHE 35   35   ?    ?   ?   B . n 
A 1 36   LYS 36   36   ?    ?   ?   B . n 
A 1 37   GLN 37   37   ?    ?   ?   B . n 
A 1 38   GLN 38   38   ?    ?   ?   B . n 
A 1 39   ARG 39   39   ?    ?   ?   B . n 
A 1 40   LEU 40   40   ?    ?   ?   B . n 
A 1 41   LYS 41   41   ?    ?   ?   B . n 
A 1 42   ALA 42   42   ?    ?   ?   B . n 
A 1 43   TRP 43   43   ?    ?   ?   B . n 
A 1 44   GLN 44   44   ?    ?   ?   B . n 
A 1 45   PRO 45   45   ?    ?   ?   B . n 
A 1 46   ILE 46   46   ?    ?   ?   B . n 
A 1 47   LEU 47   47   ?    ?   ?   B . n 
A 1 48   THR 48   48   48   THR THR B . n 
A 1 49   PRO 49   49   49   PRO PRO B . n 
A 1 50   LYS 50   50   50   LYS LYS B . n 
A 1 51   SER 51   51   51   SER SER B . n 
A 1 52   VAL 52   52   52   VAL VAL B . n 
A 1 53   LEU 53   53   53   LEU LEU B . n 
A 1 54   PRO 54   54   54   PRO PRO B . n 
A 1 55   THR 55   55   55   THR THR B . n 
A 1 56   LEU 56   56   56   LEU LEU B . n 
A 1 57   LEU 57   57   57   LEU LEU B . n 
A 1 58   ILE 58   58   58   ILE ILE B . n 
A 1 59   ILE 59   59   59   ILE ILE B . n 
A 1 60   GLY 60   60   60   GLY GLY B . n 
A 1 61   ILE 61   61   61   ILE ILE B . n 
A 1 62   ILE 62   62   62   ILE ILE B . n 
A 1 63   PHE 63   63   63   PHE PHE B . n 
A 1 64   ALA 64   64   64   ALA ALA B . n 
A 1 65   PRO 65   65   65   PRO PRO B . n 
A 1 66   ILE 66   66   66   ILE ILE B . n 
A 1 67   GLY 67   67   67   GLY GLY B . n 
A 1 68   ALA 68   68   68   ALA ALA B . n 
A 1 69   LEU 69   69   69   LEU LEU B . n 
A 1 70   ILE 70   70   70   ILE ILE B . n 
A 1 71   VAL 71   71   71   VAL VAL B . n 
A 1 72   TRP 72   72   72   TRP TRP B . n 
A 1 73   GLY 73   73   73   GLY GLY B . n 
A 1 74   SER 74   74   74   SER SER B . n 
A 1 75   GLY 75   75   75   GLY GLY B . n 
A 1 76   LYS 76   76   76   LYS LYS B . n 
A 1 77   VAL 77   77   77   VAL VAL B . n 
A 1 78   THR 78   78   78   THR THR B . n 
A 1 79   THR 79   79   79   THR THR B . n 
A 1 80   ILE 80   80   80   ILE ILE B . n 
A 1 81   THR 81   81   81   THR THR B . n 
A 1 82   LEU 82   82   82   LEU LEU B . n 
A 1 83   ASP 83   83   83   ASP ASP B . n 
A 1 84   TYR 84   84   84   TYR TYR B . n 
A 1 85   THR 85   85   85   THR THR B . n 
A 1 86   GLU 86   86   86   GLU GLU B . n 
A 1 87   CYS 87   87   87   CYS CYS B . n 
A 1 88   ASP 88   88   88   ASP ASP B . n 
A 1 89   VAL 89   89   89   VAL VAL B . n 
A 1 90   ASP 90   90   90   ASP ASP B . n 
A 1 91   ALA 91   91   91   ALA ALA B . n 
A 1 92   PRO 92   92   92   PRO PRO B . n 
A 1 93   THR 93   93   93   THR THR B . n 
A 1 94   ASP 94   94   94   ASP ASP B . n 
A 1 95   GLY 95   95   95   GLY GLY B . n 
A 1 96   SER 96   96   96   SER SER B . n 
A 1 97   TYR 97   97   97   TYR TYR B . n 
A 1 98   GLN 98   98   98   GLN GLN B . n 
A 1 99   ALA 99   99   99   ALA ALA B . n 
A 1 100  MET 100  100  100  MET MET B . n 
A 1 101  PRO 101  101  101  PRO PRO B . n 
A 1 102  ASN 102  102  102  ASN ASN B . n 
A 1 103  SER 103  103  103  SER SER B . n 
A 1 104  ALA 104  104  104  ALA ALA B . n 
A 1 105  TYR 105  105  105  TYR TYR B . n 
A 1 106  GLN 106  106  106  GLN GLN B . n 
A 1 107  TYR 107  107  107  TYR TYR B . n 
A 1 108  ASP 108  108  108  ASP ASP B . n 
A 1 109  LEU 109  109  109  LEU LEU B . n 
A 1 110  ALA 110  110  110  ALA ALA B . n 
A 1 111  THR 111  111  111  THR THR B . n 
A 1 112  SER 112  112  112  SER SER B . n 
A 1 113  SER 113  113  113  SER SER B . n 
A 1 114  SER 114  114  114  SER SER B . n 
A 1 115  VAL 115  115  115  VAL VAL B . n 
A 1 116  SER 116  116  116  SER SER B . n 
A 1 117  GLU 117  117  117  GLU GLU B . n 
A 1 118  SER 118  118  118  SER SER B . n 
A 1 119  SER 119  119  119  SER SER B . n 
A 1 120  ILE 120  120  120  ILE ILE B . n 
A 1 121  ALA 121  121  121  ALA ALA B . n 
A 1 122  SER 122  122  122  SER SER B . n 
A 1 123  PRO 123  123  123  PRO PRO B . n 
A 1 124  THR 124  124  124  THR THR B . n 
A 1 125  TRP 125  125  125  TRP TRP B . n 
A 1 126  THR 126  126  126  THR THR B . n 
A 1 127  PHE 127  127  127  PHE PHE B . n 
A 1 128  SER 128  128  128  SER SER B . n 
A 1 129  ASN 129  129  129  ASN ASN B . n 
A 1 130  ASP 130  130  130  ASP ASP B . n 
A 1 131  SER 131  131  131  SER SER B . n 
A 1 132  SER 132  132  132  SER SER B . n 
A 1 133  ARG 133  133  133  ARG ARG B . n 
A 1 134  GLU 134  134  134  GLU GLU B . n 
A 1 135  VAL 135  135  135  VAL VAL B . n 
A 1 136  GLY 136  136  136  GLY GLY B . n 
A 1 137  GLU 137  137  137  GLU GLU B . n 
A 1 138  THR 138  138  138  THR THR B . n 
A 1 139  ALA 139  139  139  ALA ALA B . n 
A 1 140  ARG 140  140  140  ARG ARG B . n 
A 1 141  CYS 141  141  141  CYS CYS B . n 
A 1 142  GLU 142  142  142  GLU GLU B . n 
A 1 143  ILE 143  143  143  ILE ILE B . n 
A 1 144  GLU 144  144  144  GLU GLU B . n 
A 1 145  PHE 145  145  145  PHE PHE B . n 
A 1 146  GLU 146  146  146  GLU GLU B . n 
A 1 147  VAL 147  147  147  VAL VAL B . n 
A 1 148  PRO 148  148  148  PRO PRO B . n 
A 1 149  TYR 149  149  149  TYR TYR B . n 
A 1 150  ASP 150  150  150  ASP ASP B . n 
A 1 151  LEU 151  151  151  LEU LEU B . n 
A 1 152  GLY 152  152  152  GLY GLY B . n 
A 1 153  PRO 153  153  153  PRO PRO B . n 
A 1 154  GLY 154  154  154  GLY GLY B . n 
A 1 155  LEU 155  155  155  LEU LEU B . n 
A 1 156  PHE 156  156  156  PHE PHE B . n 
A 1 157  LEU 157  157  157  LEU LEU B . n 
A 1 158  TYR 158  158  158  TYR TYR B . n 
A 1 159  TYR 159  159  159  TYR TYR B . n 
A 1 160  LYS 160  160  160  LYS LYS B . n 
A 1 161  LEU 161  161  161  LEU LEU B . n 
A 1 162  THR 162  162  162  THR THR B . n 
A 1 163  ASN 163  163  163  ASN ASN B . n 
A 1 164  TYR 164  164  164  TYR TYR B . n 
A 1 165  TYR 165  165  165  TYR TYR B . n 
A 1 166  GLN 166  166  166  GLN GLN B . n 
A 1 167  ASN 167  167  167  ASN ASN B . n 
A 1 168  HIS 168  168  168  HIS HIS B . n 
A 1 169  ARG 169  169  169  ARG ARG B . n 
A 1 170  ARG 170  170  170  ARG ARG B . n 
A 1 171  TYR 171  171  171  TYR TYR B . n 
A 1 172  SER 172  172  172  SER SER B . n 
A 1 173  SER 173  173  173  SER SER B . n 
A 1 174  SER 174  174  174  SER SER B . n 
A 1 175  PHE 175  175  175  PHE PHE B . n 
A 1 176  ASP 176  176  176  ASP ASP B . n 
A 1 177  ALA 177  177  177  ALA ALA B . n 
A 1 178  THR 178  178  178  THR THR B . n 
A 1 179  GLN 179  179  179  GLN GLN B . n 
A 1 180  LEU 180  180  180  LEU LEU B . n 
A 1 181  ILE 181  181  181  ILE ILE B . n 
A 1 182  GLY 182  182  182  GLY GLY B . n 
A 1 183  ASP 183  183  183  ASP ASP B . n 
A 1 184  SER 184  184  184  SER SER B . n 
A 1 185  ARG 185  185  185  ARG ARG B . n 
A 1 186  SER 186  186  186  SER SER B . n 
A 1 187  LEU 187  187  187  LEU LEU B . n 
A 1 188  SER 188  188  188  SER SER B . n 
A 1 189  GLN 189  189  189  GLN GLN B . n 
A 1 190  ILE 190  190  190  ILE ILE B . n 
A 1 191  ASN 191  191  191  ASN ASN B . n 
A 1 192  GLY 192  192  192  GLY GLY B . n 
A 1 193  GLY 193  193  193  GLY GLY B . n 
A 1 194  ASN 194  194  194  ASN ASN B . n 
A 1 195  CYS 195  195  195  CYS CYS B . n 
A 1 196  LYS 196  196  196  LYS LYS B . n 
A 1 197  PRO 197  197  197  PRO PRO B . n 
A 1 198  ILE 198  198  198  ILE ILE B . n 
A 1 199  THR 199  199  199  THR THR B . n 
A 1 200  SER 200  200  200  SER SER B . n 
A 1 201  ARG 201  201  201  ARG ARG B . n 
A 1 202  ASP 202  202  202  ASP ASP B . n 
A 1 203  GLY 203  203  203  GLY GLY B . n 
A 1 204  LYS 204  204  204  LYS LYS B . n 
A 1 205  PRO 205  205  205  PRO PRO B . n 
A 1 206  TYR 206  206  206  TYR TYR B . n 
A 1 207  TYR 207  207  207  TYR TYR B . n 
A 1 208  PRO 208  208  208  PRO PRO B . n 
A 1 209  CYS 209  209  209  CYS CYS B . n 
A 1 210  GLY 210  210  210  GLY GLY B . n 
A 1 211  LEU 211  211  211  LEU LEU B . n 
A 1 212  ILE 212  212  212  ILE ILE B . n 
A 1 213  ALA 213  213  213  ALA ALA B . n 
A 1 214  ASN 214  214  214  ASN ASN B . n 
A 1 215  SER 215  215  215  SER SER B . n 
A 1 216  LEU 216  216  216  LEU LEU B . n 
A 1 217  PHE 217  217  217  PHE PHE B . n 
A 1 218  ASN 218  218  218  ASN ASN B . n 
A 1 219  ASP 219  219  219  ASP ASP B . n 
A 1 220  THR 220  220  220  THR THR B . n 
A 1 221  PHE 221  221  221  PHE PHE B . n 
A 1 222  PRO 222  222  222  PRO PRO B . n 
A 1 223  SER 223  223  223  SER SER B . n 
A 1 224  VAL 224  224  224  VAL VAL B . n 
A 1 225  VAL 225  225  225  VAL VAL B . n 
A 1 226  LEU 226  226  226  LEU LEU B . n 
A 1 227  LEU 227  227  227  LEU LEU B . n 
A 1 228  ASN 228  228  228  ASN ASN B . n 
A 1 229  PRO 229  229  229  PRO PRO B . n 
A 1 230  THR 230  230  230  THR THR B . n 
A 1 231  ASN 231  231  231  ASN ASN B . n 
A 1 232  GLY 232  232  232  GLY GLY B . n 
A 1 233  ALA 233  233  233  ALA ALA B . n 
A 1 234  GLN 234  234  234  GLN GLN B . n 
A 1 235  ASN 235  235  235  ASN ASN B . n 
A 1 236  GLN 236  236  236  GLN GLN B . n 
A 1 237  THR 237  237  237  THR THR B . n 
A 1 238  TYR 238  238  238  TYR TYR B . n 
A 1 239  ASN 239  239  239  ASN ASN B . n 
A 1 240  PHE 240  240  240  PHE PHE B . n 
A 1 241  SER 241  241  241  SER SER B . n 
A 1 242  GLU 242  242  242  GLU GLU B . n 
A 1 243  SER 243  243  243  SER SER B . n 
A 1 244  GLY 244  244  244  GLY GLY B . n 
A 1 245  ILE 245  245  245  ILE ILE B . n 
A 1 246  ALA 246  246  246  ALA ALA B . n 
A 1 247  TRP 247  247  247  TRP TRP B . n 
A 1 248  GLY 248  248  248  GLY GLY B . n 
A 1 249  GLY 249  249  249  GLY GLY B . n 
A 1 250  ILE 250  250  250  ILE ILE B . n 
A 1 251  LYS 251  251  251  LYS LYS B . n 
A 1 252  LYS 252  252  252  LYS LYS B . n 
A 1 253  ASN 253  253  253  ASN ASN B . n 
A 1 254  TYR 254  254  254  TYR TYR B . n 
A 1 255  ALA 255  255  255  ALA ALA B . n 
A 1 256  SER 256  256  256  SER SER B . n 
A 1 257  THR 257  257  257  THR THR B . n 
A 1 258  LEU 258  258  258  LEU LEU B . n 
A 1 259  THR 259  259  259  THR THR B . n 
A 1 260  TYR 260  260  260  TYR TYR B . n 
A 1 261  ILE 261  261  261  ILE ILE B . n 
A 1 262  SER 262  262  262  SER SER B . n 
A 1 263  PRO 263  263  263  PRO PRO B . n 
A 1 264  SER 264  264  264  SER SER B . n 
A 1 265  ASP 265  265  265  ASP ASP B . n 
A 1 266  VAL 266  266  266  VAL VAL B . n 
A 1 267  LEU 267  267  267  LEU LEU B . n 
A 1 268  PRO 268  268  268  PRO PRO B . n 
A 1 269  PRO 269  269  269  PRO PRO B . n 
A 1 270  PRO 270  270  270  PRO PRO B . n 
A 1 271  ASN 271  271  271  ASN ASN B . n 
A 1 272  TRP 272  272  272  TRP TRP B . n 
A 1 273  ALA 273  273  273  ALA ALA B . n 
A 1 274  LEU 274  274  274  LEU LEU B . n 
A 1 275  LYS 275  275  275  LYS LYS B . n 
A 1 276  TYR 276  276  276  TYR TYR B . n 
A 1 277  PRO 277  277  277  PRO PRO B . n 
A 1 278  ASN 278  278  278  ASN ASN B . n 
A 1 279  GLY 279  279  279  GLY GLY B . n 
A 1 280  TYR 280  280  280  TYR TYR B . n 
A 1 281  VAL 281  281  281  VAL VAL B . n 
A 1 282  ASP 282  282  282  ASP ASP B . n 
A 1 283  GLY 283  283  283  GLY GLY B . n 
A 1 284  PHE 284  284  284  PHE PHE B . n 
A 1 285  PRO 285  285  285  PRO PRO B . n 
A 1 286  ASN 286  286  286  ASN ASN B . n 
A 1 287  LEU 287  287  287  LEU LEU B . n 
A 1 288  ARG 288  288  288  ARG ARG B . n 
A 1 289  GLU 289  289  289  GLU GLU B . n 
A 1 290  ASP 290  290  290  ASP ASP B . n 
A 1 291  GLU 291  291  291  GLU GLU B . n 
A 1 292  HIS 292  292  292  HIS HIS B . n 
A 1 293  PHE 293  293  293  PHE PHE B . n 
A 1 294  GLN 294  294  294  GLN GLN B . n 
A 1 295  VAL 295  295  295  VAL VAL B . n 
A 1 296  TRP 296  296  296  TRP TRP B . n 
A 1 297  MET 297  297  297  MET MET B . n 
A 1 298  ARG 298  298  298  ARG ARG B . n 
A 1 299  VAL 299  299  299  VAL VAL B . n 
A 1 300  ALA 300  300  300  ALA ALA B . n 
A 1 301  ALA 301  301  301  ALA ALA B . n 
A 1 302  LEU 302  302  302  LEU LEU B . n 
A 1 303  PRO 303  303  303  PRO PRO B . n 
A 1 304  THR 304  304  304  THR THR B . n 
A 1 305  PHE 305  305  305  PHE PHE B . n 
A 1 306  ARG 306  306  306  ARG ARG B . n 
A 1 307  LYS 307  307  307  LYS LYS B . n 
A 1 308  LEU 308  308  308  LEU LEU B . n 
A 1 309  TRP 309  309  309  TRP TRP B . n 
A 1 310  ALA 310  310  310  ALA ALA B . n 
A 1 311  ARG 311  311  311  ARG ARG B . n 
A 1 312  ASN 312  312  312  ASN ASN B . n 
A 1 313  ASP 313  313  313  ASP ASP B . n 
A 1 314  GLY 314  314  314  GLY GLY B . n 
A 1 315  GLU 315  315  315  GLU GLU B . n 
A 1 316  ILE 316  316  316  ILE ILE B . n 
A 1 317  MET 317  317  317  MET MET B . n 
A 1 318  SER 318  318  318  SER SER B . n 
A 1 319  GLN 319  319  319  GLN GLN B . n 
A 1 320  GLY 320  320  320  GLY GLY B . n 
A 1 321  ARG 321  321  321  ARG ARG B . n 
A 1 322  TYR 322  322  322  TYR TYR B . n 
A 1 323  ARG 323  323  323  ARG ARG B . n 
A 1 324  ILE 324  324  324  ILE ILE B . n 
A 1 325  VAL 325  325  325  VAL VAL B . n 
A 1 326  ALA 326  326  326  ALA ALA B . n 
A 1 327  ASN 327  327  327  ASN ASN B . n 
A 1 328  MET 328  328  328  MET MET B . n 
A 1 329  ASN 329  329  329  ASN ASN B . n 
A 1 330  TYR 330  330  330  TYR TYR B . n 
A 1 331  PRO 331  331  331  PRO PRO B . n 
A 1 332  VAL 332  332  332  VAL VAL B . n 
A 1 333  LYS 333  333  333  LYS LYS B . n 
A 1 334  GLN 334  334  334  GLN GLN B . n 
A 1 335  PHE 335  335  335  PHE PHE B . n 
A 1 336  SER 336  336  336  SER SER B . n 
A 1 337  GLY 337  337  337  GLY GLY B . n 
A 1 338  THR 338  338  338  THR THR B . n 
A 1 339  LYS 339  339  339  LYS LYS B . n 
A 1 340  SER 340  340  340  SER SER B . n 
A 1 341  ILE 341  341  341  ILE ILE B . n 
A 1 342  VAL 342  342  342  VAL VAL B . n 
A 1 343  ILE 343  343  343  ILE ILE B . n 
A 1 344  SER 344  344  344  SER SER B . n 
A 1 345  THR 345  345  345  THR THR B . n 
A 1 346  VAL 346  346  346  VAL VAL B . n 
A 1 347  SER 347  347  347  SER SER B . n 
A 1 348  TRP 348  348  348  TRP TRP B . n 
A 1 349  ILE 349  349  349  ILE ILE B . n 
A 1 350  GLY 350  350  350  GLY GLY B . n 
A 1 351  GLY 351  351  351  GLY GLY B . n 
A 1 352  LYS 352  352  352  LYS LYS B . n 
A 1 353  GLN 353  353  353  GLN GLN B . n 
A 1 354  PRO 354  354  354  PRO PRO B . n 
A 1 355  PHE 355  355  355  PHE PHE B . n 
A 1 356  LEU 356  356  356  LEU LEU B . n 
A 1 357  GLY 357  357  357  GLY GLY B . n 
A 1 358  TRP 358  358  358  TRP TRP B . n 
A 1 359  ALA 359  359  359  ALA ALA B . n 
A 1 360  TYR 360  360  360  TYR TYR B . n 
A 1 361  ILE 361  361  361  ILE ILE B . n 
A 1 362  ALA 362  362  362  ALA ALA B . n 
A 1 363  ALA 363  363  363  ALA ALA B . n 
A 1 364  ALA 364  364  364  ALA ALA B . n 
A 1 365  ILE 365  365  365  ILE ILE B . n 
A 1 366  LEU 366  366  366  LEU LEU B . n 
A 1 367  CYS 367  367  367  CYS CYS B . n 
A 1 368  VAL 368  368  368  VAL VAL B . n 
A 1 369  VAL 369  369  369  VAL VAL B . n 
A 1 370  LEU 370  370  370  LEU LEU B . n 
A 1 371  ALA 371  371  371  ALA ALA B . n 
A 1 372  VAL 372  372  372  VAL VAL B . n 
A 1 373  ALA 373  373  373  ALA ALA B . n 
A 1 374  GLY 374  374  374  GLY GLY B . n 
A 1 375  LEU 375  375  375  LEU LEU B . n 
A 1 376  ILE 376  376  376  ILE ILE B . n 
A 1 377  ARG 377  377  377  ARG ARG B . n 
A 1 378  HIS 378  378  378  HIS HIS B . n 
A 1 379  LEU 379  379  379  LEU LEU B . n 
A 1 380  VAL 380  380  380  VAL VAL B . n 
A 1 381  LYS 381  381  381  LYS LYS B . n 
A 1 382  PRO 382  382  382  PRO PRO B . n 
A 1 383  ARG 383  383  383  ARG ARG B . n 
A 1 384  LYS 384  384  384  LYS LYS B . n 
A 1 385  LEU 385  385  385  LEU LEU B . n 
A 1 386  GLY 386  386  386  GLY GLY B . n 
A 1 387  ASP 387  387  387  ASP ASP B . n 
A 1 388  MET 388  388  388  MET MET B . n 
A 1 389  SER 389  389  389  SER SER B . n 
A 1 390  LEU 390  390  390  LEU LEU B . n 
A 1 391  LEU 391  391  391  LEU LEU B . n 
A 1 392  SER 392  392  392  SER SER B . n 
A 1 393  TRP 393  393  393  TRP TRP B . n 
A 1 394  ASN 394  394  394  ASN ASN B . n 
A 1 395  GLN 395  395  395  GLN GLN B . n 
A 1 396  PRO 396  396  396  PRO PRO B . n 
A 1 397  ASN 397  397  397  ASN ASN B . n 
A 1 398  ALA 398  398  ?    ?   ?   B . n 
A 1 399  ASN 399  399  ?    ?   ?   B . n 
A 1 400  GLY 400  400  ?    ?   ?   B . n 
A 1 401  LEU 401  401  ?    ?   ?   B . n 
A 1 402  HIS 402  402  ?    ?   ?   B . n 
A 1 403  HIS 403  403  ?    ?   ?   B . n 
A 1 404  HIS 404  404  ?    ?   ?   B . n 
A 1 405  HIS 405  405  ?    ?   ?   B . n 
A 1 406  HIS 406  406  ?    ?   ?   B . n 
A 1 407  HIS 407  407  ?    ?   ?   B . n 
A 1 408  HIS 408  408  ?    ?   ?   B . n 
A 1 409  HIS 409  409  ?    ?   ?   B . n 
A 1 410  HIS 410  410  ?    ?   ?   B . n 
A 1 411  HIS 411  411  ?    ?   ?   B . n 
B 2 1    MET 1    1    ?    ?   ?   A . n 
B 2 2    GLY 2    2    ?    ?   ?   A . n 
B 2 3    ALA 3    3    ?    ?   ?   A . n 
B 2 4    SER 4    4    ?    ?   ?   A . n 
B 2 5    LYS 5    5    ?    ?   ?   A . n 
B 2 6    PRO 6    6    ?    ?   ?   A . n 
B 2 7    PRO 7    7    ?    ?   ?   A . n 
B 2 8    LEU 8    8    ?    ?   ?   A . n 
B 2 9    VAL 9    9    ?    ?   ?   A . n 
B 2 10   PRO 10   10   ?    ?   ?   A . n 
B 2 11   ARG 11   11   ?    ?   ?   A . n 
B 2 12   SER 12   12   ?    ?   ?   A . n 
B 2 13   LYS 13   13   ?    ?   ?   A . n 
B 2 14   LYS 14   14   ?    ?   ?   A . n 
B 2 15   HIS 15   15   ?    ?   ?   A . n 
B 2 16   ASN 16   16   ?    ?   ?   A . n 
B 2 17   PRO 17   17   ?    ?   ?   A . n 
B 2 18   SER 18   18   ?    ?   ?   A . n 
B 2 19   TRP 19   19   ?    ?   ?   A . n 
B 2 20   LEU 20   20   ?    ?   ?   A . n 
B 2 21   ASP 21   21   ?    ?   ?   A . n 
B 2 22   ARG 22   22   ?    ?   ?   A . n 
B 2 23   ASN 23   23   ?    ?   ?   A . n 
B 2 24   ILE 24   24   ?    ?   ?   A . n 
B 2 25   VAL 25   25   ?    ?   ?   A . n 
B 2 26   LYS 26   26   ?    ?   ?   A . n 
B 2 27   PRO 27   27   ?    ?   ?   A . n 
B 2 28   LEU 28   28   ?    ?   ?   A . n 
B 2 29   GLU 29   29   ?    ?   ?   A . n 
B 2 30   SER 30   30   ?    ?   ?   A . n 
B 2 31   LEU 31   31   ?    ?   ?   A . n 
B 2 32   ALA 32   32   ?    ?   ?   A . n 
B 2 33   PRO 33   33   ?    ?   ?   A . n 
B 2 34   SER 34   34   ?    ?   ?   A . n 
B 2 35   LYS 35   35   ?    ?   ?   A . n 
B 2 36   LEU 36   36   ?    ?   ?   A . n 
B 2 37   PHE 37   37   ?    ?   ?   A . n 
B 2 38   ALA 38   38   ?    ?   ?   A . n 
B 2 39   ARG 39   39   ?    ?   ?   A . n 
B 2 40   ARG 40   40   ?    ?   ?   A . n 
B 2 41   ARG 41   41   ?    ?   ?   A . n 
B 2 42   SER 42   42   ?    ?   ?   A . n 
B 2 43   PRO 43   43   ?    ?   ?   A . n 
B 2 44   PRO 44   44   44   PRO PRO A . n 
B 2 45   VAL 45   45   45   VAL VAL A . n 
B 2 46   PRO 46   46   46   PRO PRO A . n 
B 2 47   ARG 47   47   47   ARG ARG A . n 
B 2 48   SER 48   48   48   SER SER A . n 
B 2 49   VAL 49   49   49   VAL VAL A . n 
B 2 50   PHE 50   50   50   PHE PHE A . n 
B 2 51   ILE 51   51   51   ILE ILE A . n 
B 2 52   ASN 52   52   52   ASN ASN A . n 
B 2 53   GLU 53   53   53   GLU GLU A . n 
B 2 54   PRO 54   54   54   PRO PRO A . n 
B 2 55   LEU 55   55   55   LEU LEU A . n 
B 2 56   PRO 56   56   56   PRO PRO A . n 
B 2 57   SER 57   57   57   SER SER A . n 
B 2 58   GLU 58   58   58   GLU GLU A . n 
B 2 59   TYR 59   59   59   TYR TYR A . n 
B 2 60   TYR 60   60   ?    ?   ?   A . n 
B 2 61   ASP 61   61   ?    ?   ?   A . n 
B 2 62   LYS 62   62   ?    ?   ?   A . n 
B 2 63   LYS 63   63   ?    ?   ?   A . n 
B 2 64   GLY 64   64   ?    ?   ?   A . n 
B 2 65   LYS 65   65   ?    ?   ?   A . n 
B 2 66   ILE 66   66   ?    ?   ?   A . n 
B 2 67   LEU 67   67   ?    ?   ?   A . n 
B 2 68   ARG 68   68   ?    ?   ?   A . n 
B 2 69   ALA 69   69   ?    ?   ?   A . n 
B 2 70   HIS 70   70   70   HIS HIS A . n 
B 2 71   HIS 71   71   71   HIS HIS A . n 
B 2 72   PHE 72   72   72   PHE PHE A . n 
B 2 73   ALA 73   73   73   ALA ALA A . n 
B 2 74   THR 74   74   74   THR THR A . n 
B 2 75   ASN 75   75   75   ASN ASN A . n 
B 2 76   GLN 76   76   76   GLN GLN A . n 
B 2 77   ASN 77   77   77   ASN ASN A . n 
B 2 78   VAL 78   78   78   VAL VAL A . n 
B 2 79   THR 79   79   79   THR THR A . n 
B 2 80   SER 80   80   80   SER SER A . n 
B 2 81   LYS 81   81   81   LYS LYS A . n 
B 2 82   TYR 82   82   82   TYR TYR A . n 
B 2 83   THR 83   83   83   THR THR A . n 
B 2 84   VAL 84   84   84   VAL VAL A . n 
B 2 85   ILE 85   85   85   ILE ILE A . n 
B 2 86   THR 86   86   86   THR THR A . n 
B 2 87   PHE 87   87   87   PHE PHE A . n 
B 2 88   ILE 88   88   88   ILE ILE A . n 
B 2 89   PRO 89   89   89   PRO PRO A . n 
B 2 90   LYS 90   90   90   LYS LYS A . n 
B 2 91   ASN 91   91   91   ASN ASN A . n 
B 2 92   LEU 92   92   92   LEU LEU A . n 
B 2 93   PHE 93   93   93   PHE PHE A . n 
B 2 94   GLU 94   94   94   GLU GLU A . n 
B 2 95   GLN 95   95   95   GLN GLN A . n 
B 2 96   PHE 96   96   96   PHE PHE A . n 
B 2 97   ARG 97   97   97   ARG ARG A . n 
B 2 98   ARG 98   98   98   ARG ARG A . n 
B 2 99   VAL 99   99   99   VAL VAL A . n 
B 2 100  ALA 100  100  100  ALA ALA A . n 
B 2 101  ASN 101  101  101  ASN ASN A . n 
B 2 102  CYS 102  102  102  CYS CYS A . n 
B 2 103  PHE 103  103  103  PHE PHE A . n 
B 2 104  PHE 104  104  104  PHE PHE A . n 
B 2 105  LEU 105  105  105  LEU LEU A . n 
B 2 106  ALA 106  106  106  ALA ALA A . n 
B 2 107  ILE 107  107  107  ILE ILE A . n 
B 2 108  SER 108  108  108  SER SER A . n 
B 2 109  ILE 109  109  109  ILE ILE A . n 
B 2 110  LEU 110  110  110  LEU LEU A . n 
B 2 111  GLN 111  111  111  GLN GLN A . n 
B 2 112  PHE 112  112  112  PHE PHE A . n 
B 2 113  PHE 113  113  113  PHE PHE A . n 
B 2 114  PRO 114  114  114  PRO PRO A . n 
B 2 115  LYS 115  115  115  LYS LYS A . n 
B 2 116  PHE 116  116  116  PHE PHE A . n 
B 2 117  SER 117  117  117  SER SER A . n 
B 2 118  THR 118  118  118  THR THR A . n 
B 2 119  ILE 119  119  119  ILE ILE A . n 
B 2 120  SER 120  120  120  SER SER A . n 
B 2 121  PRO 121  121  121  PRO PRO A . n 
B 2 122  GLY 122  122  122  GLY GLY A . n 
B 2 123  LEU 123  123  123  LEU LEU A . n 
B 2 124  VAL 124  124  124  VAL VAL A . n 
B 2 125  ILE 125  125  125  ILE ILE A . n 
B 2 126  LEU 126  126  126  LEU LEU A . n 
B 2 127  PRO 127  127  127  PRO PRO A . n 
B 2 128  LEU 128  128  128  LEU LEU A . n 
B 2 129  ILE 129  129  129  ILE ILE A . n 
B 2 130  ILE 130  130  130  ILE ILE A . n 
B 2 131  VAL 131  131  131  VAL VAL A . n 
B 2 132  LEU 132  132  132  LEU LEU A . n 
B 2 133  ALA 133  133  133  ALA ALA A . n 
B 2 134  ILE 134  134  134  ILE ILE A . n 
B 2 135  THR 135  135  135  THR THR A . n 
B 2 136  ALA 136  136  136  ALA ALA A . n 
B 2 137  LEU 137  137  137  LEU LEU A . n 
B 2 138  LYS 138  138  138  LYS LYS A . n 
B 2 139  ASP 139  139  139  ASP ASP A . n 
B 2 140  GLY 140  140  140  GLY GLY A . n 
B 2 141  TYR 141  141  141  TYR TYR A . n 
B 2 142  GLU 142  142  142  GLU GLU A . n 
B 2 143  ASP 143  143  143  ASP ASP A . n 
B 2 144  ILE 144  144  144  ILE ILE A . n 
B 2 145  LYS 145  145  145  LYS LYS A . n 
B 2 146  ARG 146  146  146  ARG ARG A . n 
B 2 147  HIS 147  147  147  HIS HIS A . n 
B 2 148  GLN 148  148  148  GLN GLN A . n 
B 2 149  ALA 149  149  149  ALA ALA A . n 
B 2 150  ASP 150  150  150  ASP ASP A . n 
B 2 151  HIS 151  151  151  HIS HIS A . n 
B 2 152  ARG 152  152  152  ARG ARG A . n 
B 2 153  THR 153  153  153  THR THR A . n 
B 2 154  ASN 154  154  154  ASN ASN A . n 
B 2 155  HIS 155  155  155  HIS HIS A . n 
B 2 156  ALA 156  156  156  ALA ALA A . n 
B 2 157  ILE 157  157  157  ILE ILE A . n 
B 2 158  VAL 158  158  158  VAL VAL A . n 
B 2 159  HIS 159  159  159  HIS HIS A . n 
B 2 160  VAL 160  160  160  VAL VAL A . n 
B 2 161  LEU 161  161  161  LEU LEU A . n 
B 2 162  GLY 162  162  162  GLY GLY A . n 
B 2 163  GLY 163  163  163  GLY GLY A . n 
B 2 164  GLN 164  164  164  GLN GLN A . n 
B 2 165  ASP 165  165  ?    ?   ?   A . n 
B 2 166  TYR 166  166  ?    ?   ?   A . n 
B 2 167  THR 167  167  ?    ?   ?   A . n 
B 2 168  ASN 168  168  ?    ?   ?   A . n 
B 2 169  GLN 169  169  ?    ?   ?   A . n 
B 2 170  ASN 170  170  ?    ?   ?   A . n 
B 2 171  PRO 171  171  ?    ?   ?   A . n 
B 2 172  MET 172  172  ?    ?   ?   A . n 
B 2 173  ALA 173  173  ?    ?   ?   A . n 
B 2 174  SER 174  174  ?    ?   ?   A . n 
B 2 175  LYS 175  175  ?    ?   ?   A . n 
B 2 176  ASP 176  176  ?    ?   ?   A . n 
B 2 177  LYS 177  177  ?    ?   ?   A . n 
B 2 178  THR 178  178  ?    ?   ?   A . n 
B 2 179  PHE 179  179  ?    ?   ?   A . n 
B 2 180  ILE 180  180  ?    ?   ?   A . n 
B 2 181  PRO 181  181  ?    ?   ?   A . n 
B 2 182  ALA 182  182  ?    ?   ?   A . n 
B 2 183  ILE 183  183  ?    ?   ?   A . n 
B 2 184  PRO 184  184  ?    ?   ?   A . n 
B 2 185  LEU 185  185  ?    ?   ?   A . n 
B 2 186  PRO 186  186  ?    ?   ?   A . n 
B 2 187  LYS 187  187  ?    ?   ?   A . n 
B 2 188  ARG 188  188  ?    ?   ?   A . n 
B 2 189  ARG 189  189  ?    ?   ?   A . n 
B 2 190  SER 190  190  ?    ?   ?   A . n 
B 2 191  LYS 191  191  ?    ?   ?   A . n 
B 2 192  LYS 192  192  ?    ?   ?   A . n 
B 2 193  ALA 193  193  ?    ?   ?   A . n 
B 2 194  LYS 194  194  ?    ?   ?   A . n 
B 2 195  LYS 195  195  ?    ?   ?   A . n 
B 2 196  ALA 196  196  ?    ?   ?   A . n 
B 2 197  GLU 197  197  ?    ?   ?   A . n 
B 2 198  GLU 198  198  ?    ?   ?   A . n 
B 2 199  GLU 199  199  ?    ?   ?   A . n 
B 2 200  ALA 200  200  ?    ?   ?   A . n 
B 2 201  ALA 201  201  ?    ?   ?   A . n 
B 2 202  LEU 202  202  ?    ?   ?   A . n 
B 2 203  ASN 203  203  ?    ?   ?   A . n 
B 2 204  MET 204  204  ?    ?   ?   A . n 
B 2 205  GLN 205  205  ?    ?   ?   A . n 
B 2 206  GLY 206  206  ?    ?   ?   A . n 
B 2 207  ARG 207  207  ?    ?   ?   A . n 
B 2 208  SER 208  208  ?    ?   ?   A . n 
B 2 209  SER 209  209  ?    ?   ?   A . n 
B 2 210  SER 210  210  ?    ?   ?   A . n 
B 2 211  THR 211  211  ?    ?   ?   A . n 
B 2 212  GLU 212  212  ?    ?   ?   A . n 
B 2 213  ASN 213  213  ?    ?   ?   A . n 
B 2 214  PHE 214  214  ?    ?   ?   A . n 
B 2 215  ALA 215  215  ?    ?   ?   A . n 
B 2 216  ALA 216  216  ?    ?   ?   A . n 
B 2 217  GLU 217  217  ?    ?   ?   A . n 
B 2 218  PRO 218  218  ?    ?   ?   A . n 
B 2 219  VAL 219  219  ?    ?   ?   A . n 
B 2 220  PRO 220  220  ?    ?   ?   A . n 
B 2 221  GLY 221  221  ?    ?   ?   A . n 
B 2 222  ALA 222  222  ?    ?   ?   A . n 
B 2 223  GLU 223  223  ?    ?   ?   A . n 
B 2 224  PRO 224  224  ?    ?   ?   A . n 
B 2 225  ARG 225  225  ?    ?   ?   A . n 
B 2 226  GLY 226  226  ?    ?   ?   A . n 
B 2 227  GLN 227  227  ?    ?   ?   A . n 
B 2 228  ASP 228  228  ?    ?   ?   A . n 
B 2 229  GLU 229  229  ?    ?   ?   A . n 
B 2 230  LEU 230  230  ?    ?   ?   A . n 
B 2 231  GLN 231  231  ?    ?   ?   A . n 
B 2 232  ARG 232  232  ?    ?   ?   A . n 
B 2 233  MET 233  233  ?    ?   ?   A . n 
B 2 234  ARG 234  234  ?    ?   ?   A . n 
B 2 235  SER 235  235  ?    ?   ?   A . n 
B 2 236  GLN 236  236  ?    ?   ?   A . n 
B 2 237  VAL 237  237  ?    ?   ?   A . n 
B 2 238  SER 238  238  ?    ?   ?   A . n 
B 2 239  ASN 239  239  ?    ?   ?   A . n 
B 2 240  TRP 240  240  ?    ?   ?   A . n 
B 2 241  ASP 241  241  ?    ?   ?   A . n 
B 2 242  GLU 242  242  ?    ?   ?   A . n 
B 2 243  ASP 243  243  ?    ?   ?   A . n 
B 2 244  PRO 244  244  ?    ?   ?   A . n 
B 2 245  GLU 245  245  ?    ?   ?   A . n 
B 2 246  ALA 246  246  ?    ?   ?   A . n 
B 2 247  GLY 247  247  ?    ?   ?   A . n 
B 2 248  ASP 248  248  ?    ?   ?   A . n 
B 2 249  SER 249  249  ?    ?   ?   A . n 
B 2 250  PRO 250  250  ?    ?   ?   A . n 
B 2 251  GLY 251  251  251  GLY GLY A . n 
B 2 252  GLU 252  252  252  GLU GLU A . n 
B 2 253  LEU 253  253  253  LEU LEU A . n 
B 2 254  GLY 254  254  254  GLY GLY A . n 
B 2 255  TRP 255  255  255  TRP TRP A . n 
B 2 256  HIS 256  256  256  HIS HIS A . n 
B 2 257  ARG 257  257  257  ARG ARG A . n 
B 2 258  THR 258  258  258  THR THR A . n 
B 2 259  ILE 259  259  259  ILE ILE A . n 
B 2 260  TRP 260  260  260  TRP TRP A . n 
B 2 261  GLU 261  261  261  GLU GLU A . n 
B 2 262  ASP 262  262  262  ASP ASP A . n 
B 2 263  VAL 263  263  263  VAL VAL A . n 
B 2 264  LYS 264  264  264  LYS LYS A . n 
B 2 265  VAL 265  265  265  VAL VAL A . n 
B 2 266  GLY 266  266  266  GLY GLY A . n 
B 2 267  ASP 267  267  267  ASP ASP A . n 
B 2 268  PHE 268  268  268  PHE PHE A . n 
B 2 269  VAL 269  269  269  VAL VAL A . n 
B 2 270  LYS 270  270  270  LYS LYS A . n 
B 2 271  ILE 271  271  271  ILE ILE A . n 
B 2 272  TYR 272  272  272  TYR TYR A . n 
B 2 273  GLU 273  273  273  GLU GLU A . n 
B 2 274  ASN 274  274  274  ASN ASN A . n 
B 2 275  GLU 275  275  275  GLU GLU A . n 
B 2 276  GLN 276  276  276  GLN GLN A . n 
B 2 277  PHE 277  277  277  PHE PHE A . n 
B 2 278  PRO 278  278  278  PRO PRO A . n 
B 2 279  ALA 279  279  279  ALA ALA A . n 
B 2 280  ASP 280  280  280  ASP ASP A . n 
B 2 281  ILE 281  281  281  ILE ILE A . n 
B 2 282  VAL 282  282  282  VAL VAL A . n 
B 2 283  ILE 283  283  283  ILE ILE A . n 
B 2 284  CYS 284  284  284  CYS CYS A . n 
B 2 285  ALA 285  285  285  ALA ALA A . n 
B 2 286  THR 286  286  286  THR THR A . n 
B 2 287  SER 287  287  287  SER SER A . n 
B 2 288  GLU 288  288  288  GLU GLU A . n 
B 2 289  GLU 289  289  289  GLU GLU A . n 
B 2 290  GLU 290  290  290  GLU GLU A . n 
B 2 291  ASP 291  291  291  ASP ASP A . n 
B 2 292  VAL 292  292  292  VAL VAL A . n 
B 2 293  ALA 293  293  293  ALA ALA A . n 
B 2 294  TYR 294  294  294  TYR TYR A . n 
B 2 295  ILE 295  295  295  ILE ILE A . n 
B 2 296  GLU 296  296  296  GLU GLU A . n 
B 2 297  THR 297  297  297  THR THR A . n 
B 2 298  LYS 298  298  298  LYS LYS A . n 
B 2 299  ASN 299  299  299  ASN ASN A . n 
B 2 300  LEU 300  300  300  LEU LEU A . n 
B 2 301  ASP 301  301  301  ASP ASP A . n 
B 2 302  GLY 302  302  302  GLY GLY A . n 
B 2 303  GLU 303  303  303  GLU GLU A . n 
B 2 304  THR 304  304  304  THR THR A . n 
B 2 305  ASN 305  305  305  ASN ASN A . n 
B 2 306  LEU 306  306  306  LEU LEU A . n 
B 2 307  LYS 307  307  307  LYS LYS A . n 
B 2 308  SER 308  308  308  SER SER A . n 
B 2 309  ARG 309  309  309  ARG ARG A . n 
B 2 310  ASN 310  310  310  ASN ASN A . n 
B 2 311  GLY 311  311  311  GLY GLY A . n 
B 2 312  VAL 312  312  312  VAL VAL A . n 
B 2 313  PRO 313  313  313  PRO PRO A . n 
B 2 314  GLY 314  314  314  GLY GLY A . n 
B 2 315  LEU 315  315  315  LEU LEU A . n 
B 2 316  SER 316  316  316  SER SER A . n 
B 2 317  HIS 317  317  317  HIS HIS A . n 
B 2 318  LEU 318  318  318  LEU LEU A . n 
B 2 319  ASN 319  319  319  ASN ASN A . n 
B 2 320  THR 320  320  320  THR THR A . n 
B 2 321  ALA 321  321  321  ALA ALA A . n 
B 2 322  GLU 322  322  322  GLU GLU A . n 
B 2 323  ALA 323  323  323  ALA ALA A . n 
B 2 324  CYS 324  324  324  CYS CYS A . n 
B 2 325  ALA 325  325  325  ALA ALA A . n 
B 2 326  LYS 326  326  326  LYS LYS A . n 
B 2 327  ALA 327  327  327  ALA ALA A . n 
B 2 328  HIS 328  328  328  HIS HIS A . n 
B 2 329  LEU 329  329  329  LEU LEU A . n 
B 2 330  CYS 330  330  330  CYS CYS A . n 
B 2 331  ILE 331  331  331  ILE ILE A . n 
B 2 332  ASP 332  332  332  ASP ASP A . n 
B 2 333  LEU 333  333  333  LEU LEU A . n 
B 2 334  ASP 334  334  334  ASP ASP A . n 
B 2 335  ALA 335  335  335  ALA ALA A . n 
B 2 336  PRO 336  336  336  PRO PRO A . n 
B 2 337  GLU 337  337  337  GLU GLU A . n 
B 2 338  SER 338  338  338  SER SER A . n 
B 2 339  ASN 339  339  339  ASN ASN A . n 
B 2 340  MET 340  340  340  MET MET A . n 
B 2 341  PHE 341  341  341  PHE PHE A . n 
B 2 342  ARG 342  342  342  ARG ARG A . n 
B 2 343  LEU 343  343  343  LEU LEU A . n 
B 2 344  ASN 344  344  344  ASN ASN A . n 
B 2 345  GLY 345  345  345  GLY GLY A . n 
B 2 346  ALA 346  346  346  ALA ALA A . n 
B 2 347  VAL 347  347  347  VAL VAL A . n 
B 2 348  ILE 348  348  348  ILE ILE A . n 
B 2 349  ASN 349  349  349  ASN ASN A . n 
B 2 350  LEU 350  350  350  LEU LEU A . n 
B 2 351  GLU 351  351  351  GLU GLU A . n 
B 2 352  GLU 352  352  352  GLU GLU A . n 
B 2 353  TYR 353  353  353  TYR TYR A . n 
B 2 354  ASP 354  354  354  ASP ASP A . n 
B 2 355  GLU 355  355  355  GLU GLU A . n 
B 2 356  ASP 356  356  356  ASP ASP A . n 
B 2 357  GLU 357  357  357  GLU GLU A . n 
B 2 358  GLN 358  358  358  GLN GLN A . n 
B 2 359  HIS 359  359  359  HIS HIS A . n 
B 2 360  PRO 360  360  360  PRO PRO A . n 
B 2 361  ILE 361  361  361  ILE ILE A . n 
B 2 362  HIS 362  362  362  HIS HIS A . n 
B 2 363  PRO 363  363  363  PRO PRO A . n 
B 2 364  ILE 364  364  364  ILE ILE A . n 
B 2 365  THR 365  365  365  THR THR A . n 
B 2 366  LEU 366  366  366  LEU LEU A . n 
B 2 367  GLU 367  367  367  GLU GLU A . n 
B 2 368  THR 368  368  368  THR THR A . n 
B 2 369  THR 369  369  369  THR THR A . n 
B 2 370  MET 370  370  370  MET MET A . n 
B 2 371  LEU 371  371  371  LEU LEU A . n 
B 2 372  ARG 372  372  372  ARG ARG A . n 
B 2 373  GLY 373  373  373  GLY GLY A . n 
B 2 374  CYS 374  374  374  CYS CYS A . n 
B 2 375  VAL 375  375  375  VAL VAL A . n 
B 2 376  LEU 376  376  376  LEU LEU A . n 
B 2 377  LYS 377  377  377  LYS LYS A . n 
B 2 378  ASN 378  378  378  ASN ASN A . n 
B 2 379  THR 379  379  379  THR THR A . n 
B 2 380  ALA 380  380  380  ALA ALA A . n 
B 2 381  TRP 381  381  381  TRP TRP A . n 
B 2 382  VAL 382  382  382  VAL VAL A . n 
B 2 383  ILE 383  383  383  ILE ILE A . n 
B 2 384  GLY 384  384  384  GLY GLY A . n 
B 2 385  ILE 385  385  385  ILE ILE A . n 
B 2 386  ILE 386  386  386  ILE ILE A . n 
B 2 387  VAL 387  387  387  VAL VAL A . n 
B 2 388  TYR 388  388  388  TYR TYR A . n 
B 2 389  THR 389  389  389  THR THR A . n 
B 2 390  GLY 390  390  390  GLY GLY A . n 
B 2 391  GLU 391  391  391  GLU GLU A . n 
B 2 392  ASP 392  392  392  ASP ASP A . n 
B 2 393  THR 393  393  393  THR THR A . n 
B 2 394  LYS 394  394  394  LYS LYS A . n 
B 2 395  ILE 395  395  395  ILE ILE A . n 
B 2 396  ILE 396  396  396  ILE ILE A . n 
B 2 397  ARG 397  397  397  ARG ARG A . n 
B 2 398  ASN 398  398  398  ASN ASN A . n 
B 2 399  ALA 399  399  399  ALA ALA A . n 
B 2 400  GLY 400  400  400  GLY GLY A . n 
B 2 401  ALA 401  401  401  ALA ALA A . n 
B 2 402  THR 402  402  402  THR THR A . n 
B 2 403  PRO 403  403  403  PRO PRO A . n 
B 2 404  SER 404  404  404  SER SER A . n 
B 2 405  LYS 405  405  405  LYS LYS A . n 
B 2 406  ARG 406  406  406  ARG ARG A . n 
B 2 407  SER 407  407  407  SER SER A . n 
B 2 408  LYS 408  408  408  LYS LYS A . n 
B 2 409  VAL 409  409  409  VAL VAL A . n 
B 2 410  GLU 410  410  410  GLU GLU A . n 
B 2 411  LYS 411  411  411  LYS LYS A . n 
B 2 412  GLN 412  412  412  GLN GLN A . n 
B 2 413  MET 413  413  413  MET MET A . n 
B 2 414  ASN 414  414  414  ASN ASN A . n 
B 2 415  PRO 415  415  415  PRO PRO A . n 
B 2 416  GLN 416  416  416  GLN GLN A . n 
B 2 417  VAL 417  417  417  VAL VAL A . n 
B 2 418  ILE 418  418  418  ILE ILE A . n 
B 2 419  ILE 419  419  419  ILE ILE A . n 
B 2 420  ASN 420  420  420  ASN ASN A . n 
B 2 421  LEU 421  421  421  LEU LEU A . n 
B 2 422  VAL 422  422  422  VAL VAL A . n 
B 2 423  ILE 423  423  423  ILE ILE A . n 
B 2 424  LEU 424  424  424  LEU LEU A . n 
B 2 425  ALA 425  425  425  ALA ALA A . n 
B 2 426  ALA 426  426  426  ALA ALA A . n 
B 2 427  ILE 427  427  427  ILE ILE A . n 
B 2 428  ALA 428  428  428  ALA ALA A . n 
B 2 429  VAL 429  429  429  VAL VAL A . n 
B 2 430  VAL 430  430  430  VAL VAL A . n 
B 2 431  CYS 431  431  431  CYS CYS A . n 
B 2 432  ALA 432  432  432  ALA ALA A . n 
B 2 433  ILE 433  433  433  ILE ILE A . n 
B 2 434  VAL 434  434  434  VAL VAL A . n 
B 2 435  ASP 435  435  435  ASP ASP A . n 
B 2 436  HIS 436  436  436  HIS HIS A . n 
B 2 437  VAL 437  437  437  VAL VAL A . n 
B 2 438  ASN 438  438  438  ASN ASN A . n 
B 2 439  GLU 439  439  439  GLU GLU A . n 
B 2 440  VAL 440  440  440  VAL VAL A . n 
B 2 441  GLU 441  441  441  GLU GLU A . n 
B 2 442  TRP 442  442  442  TRP TRP A . n 
B 2 443  ASP 443  443  443  ASP ASP A . n 
B 2 444  ARG 444  444  444  ARG ARG A . n 
B 2 445  GLN 445  445  445  GLN GLN A . n 
B 2 446  GLN 446  446  446  GLN GLN A . n 
B 2 447  ALA 447  447  447  ALA ALA A . n 
B 2 448  TYR 448  448  448  TYR TYR A . n 
B 2 449  TRP 449  449  449  TRP TRP A . n 
B 2 450  MET 450  450  450  MET MET A . n 
B 2 451  LEU 451  451  451  LEU LEU A . n 
B 2 452  PHE 452  452  452  PHE PHE A . n 
B 2 453  ALA 453  453  453  ALA ALA A . n 
B 2 454  ASP 454  454  454  ASP ASP A . n 
B 2 455  THR 455  455  455  THR THR A . n 
B 2 456  SER 456  456  456  SER SER A . n 
B 2 457  GLY 457  457  457  GLY GLY A . n 
B 2 458  ASP 458  458  458  ASP ASP A . n 
B 2 459  ASN 459  459  459  ASN ASN A . n 
B 2 460  PRO 460  460  460  PRO PRO A . n 
B 2 461  ASN 461  461  461  ASN ASN A . n 
B 2 462  ILE 462  462  462  ILE ILE A . n 
B 2 463  ASN 463  463  463  ASN ASN A . n 
B 2 464  GLY 464  464  464  GLY GLY A . n 
B 2 465  LEU 465  465  465  LEU LEU A . n 
B 2 466  VAL 466  466  466  VAL VAL A . n 
B 2 467  THR 467  467  467  THR THR A . n 
B 2 468  PHE 468  468  468  PHE PHE A . n 
B 2 469  ALA 469  469  469  ALA ALA A . n 
B 2 470  ASN 470  470  470  ASN ASN A . n 
B 2 471  ALA 471  471  471  ALA ALA A . n 
B 2 472  PHE 472  472  472  PHE PHE A . n 
B 2 473  ILE 473  473  473  ILE ILE A . n 
B 2 474  THR 474  474  474  THR THR A . n 
B 2 475  PHE 475  475  475  PHE PHE A . n 
B 2 476  GLN 476  476  476  GLN GLN A . n 
B 2 477  ASN 477  477  477  ASN ASN A . n 
B 2 478  ILE 478  478  478  ILE ILE A . n 
B 2 479  VAL 479  479  479  VAL VAL A . n 
B 2 480  PRO 480  480  480  PRO PRO A . n 
B 2 481  ILE 481  481  481  ILE ILE A . n 
B 2 482  SER 482  482  482  SER SER A . n 
B 2 483  LEU 483  483  483  LEU LEU A . n 
B 2 484  TYR 484  484  484  TYR TYR A . n 
B 2 485  ILE 485  485  485  ILE ILE A . n 
B 2 486  SER 486  486  486  SER SER A . n 
B 2 487  ILE 487  487  487  ILE ILE A . n 
B 2 488  GLU 488  488  488  GLU GLU A . n 
B 2 489  ALA 489  489  489  ALA ALA A . n 
B 2 490  VAL 490  490  490  VAL VAL A . n 
B 2 491  ARG 491  491  491  ARG ARG A . n 
B 2 492  THR 492  492  492  THR THR A . n 
B 2 493  ILE 493  493  493  ILE ILE A . n 
B 2 494  GLN 494  494  494  GLN GLN A . n 
B 2 495  ALA 495  495  495  ALA ALA A . n 
B 2 496  ALA 496  496  496  ALA ALA A . n 
B 2 497  PHE 497  497  497  PHE PHE A . n 
B 2 498  ILE 498  498  498  ILE ILE A . n 
B 2 499  TYR 499  499  499  TYR TYR A . n 
B 2 500  TRP 500  500  500  TRP TRP A . n 
B 2 501  ASP 501  501  501  ASP ASP A . n 
B 2 502  ARG 502  502  502  ARG ARG A . n 
B 2 503  ASP 503  503  503  ASP ASP A . n 
B 2 504  ILE 504  504  504  ILE ILE A . n 
B 2 505  LYS 505  505  505  LYS LYS A . n 
B 2 506  TYR 506  506  506  TYR TYR A . n 
B 2 507  LYS 507  507  507  LYS LYS A . n 
B 2 508  LYS 508  508  508  LYS LYS A . n 
B 2 509  ASP 509  509  509  ASP ASP A . n 
B 2 510  GLY 510  510  510  GLY GLY A . n 
B 2 511  VAL 511  511  511  VAL VAL A . n 
B 2 512  THR 512  512  512  THR THR A . n 
B 2 513  THR 513  513  513  THR THR A . n 
B 2 514  ARG 514  514  514  ARG ARG A . n 
B 2 515  THR 515  515  515  THR THR A . n 
B 2 516  THR 516  516  516  THR THR A . n 
B 2 517  ALA 517  517  517  ALA ALA A . n 
B 2 518  ARG 518  518  518  ARG ARG A . n 
B 2 519  SER 519  519  519  SER SER A . n 
B 2 520  TRP 520  520  520  TRP TRP A . n 
B 2 521  ASN 521  521  521  ASN ASN A . n 
B 2 522  LEU 522  522  522  LEU LEU A . n 
B 2 523  SER 523  523  523  SER SER A . n 
B 2 524  ASP 524  524  524  ASP ASP A . n 
B 2 525  ASP 525  525  525  ASP ASP A . n 
B 2 526  LEU 526  526  526  LEU LEU A . n 
B 2 527  GLY 527  527  527  GLY GLY A . n 
B 2 528  GLN 528  528  528  GLN GLN A . n 
B 2 529  ILE 529  529  529  ILE ILE A . n 
B 2 530  GLU 530  530  530  GLU GLU A . n 
B 2 531  TYR 531  531  531  TYR TYR A . n 
B 2 532  ILE 532  532  532  ILE ILE A . n 
B 2 533  PHE 533  533  533  PHE PHE A . n 
B 2 534  SER 534  534  534  SER SER A . n 
B 2 535  ASP 535  535  535  ASP ASP A . n 
B 2 536  LYS 536  536  536  LYS LYS A . n 
B 2 537  THR 537  537  537  THR THR A . n 
B 2 538  GLY 538  538  538  GLY GLY A . n 
B 2 539  THR 539  539  539  THR THR A . n 
B 2 540  LEU 540  540  540  LEU LEU A . n 
B 2 541  THR 541  541  541  THR THR A . n 
B 2 542  GLN 542  542  542  GLN GLN A . n 
B 2 543  ASN 543  543  543  ASN ASN A . n 
B 2 544  ALA 544  544  544  ALA ALA A . n 
B 2 545  MET 545  545  545  MET MET A . n 
B 2 546  ILE 546  546  546  ILE ILE A . n 
B 2 547  PHE 547  547  547  PHE PHE A . n 
B 2 548  ARG 548  548  548  ARG ARG A . n 
B 2 549  GLN 549  549  549  GLN GLN A . n 
B 2 550  CYS 550  550  550  CYS CYS A . n 
B 2 551  SER 551  551  551  SER SER A . n 
B 2 552  VAL 552  552  552  VAL VAL A . n 
B 2 553  GLY 553  553  553  GLY GLY A . n 
B 2 554  GLY 554  554  554  GLY GLY A . n 
B 2 555  LYS 555  555  555  LYS LYS A . n 
B 2 556  ILE 556  556  556  ILE ILE A . n 
B 2 557  TYR 557  557  557  TYR TYR A . n 
B 2 558  THR 558  558  558  THR THR A . n 
B 2 559  GLY 559  559  ?    ?   ?   A . n 
B 2 560  ASP 560  560  ?    ?   ?   A . n 
B 2 561  GLY 561  561  ?    ?   ?   A . n 
B 2 562  LEU 562  562  ?    ?   ?   A . n 
B 2 563  PRO 563  563  ?    ?   ?   A . n 
B 2 564  PRO 564  564  ?    ?   ?   A . n 
B 2 565  SER 565  565  ?    ?   ?   A . n 
B 2 566  HIS 566  566  ?    ?   ?   A . n 
B 2 567  PRO 567  567  ?    ?   ?   A . n 
B 2 568  THR 568  568  ?    ?   ?   A . n 
B 2 569  ILE 569  569  ?    ?   ?   A . n 
B 2 570  THR 570  570  ?    ?   ?   A . n 
B 2 571  HIS 571  571  ?    ?   ?   A . n 
B 2 572  GLN 572  572  ?    ?   ?   A . n 
B 2 573  HIS 573  573  ?    ?   ?   A . n 
B 2 574  GLN 574  574  ?    ?   ?   A . n 
B 2 575  PRO 575  575  ?    ?   ?   A . n 
B 2 576  PRO 576  576  ?    ?   ?   A . n 
B 2 577  PRO 577  577  ?    ?   ?   A . n 
B 2 578  VAL 578  578  ?    ?   ?   A . n 
B 2 579  HIS 579  579  ?    ?   ?   A . n 
B 2 580  GLN 580  580  ?    ?   ?   A . n 
B 2 581  HIS 581  581  ?    ?   ?   A . n 
B 2 582  ASP 582  582  ?    ?   ?   A . n 
B 2 583  ASP 583  583  ?    ?   ?   A . n 
B 2 584  GLN 584  584  ?    ?   ?   A . n 
B 2 585  ASP 585  585  ?    ?   ?   A . n 
B 2 586  ASP 586  586  ?    ?   ?   A . n 
B 2 587  PRO 587  587  ?    ?   ?   A . n 
B 2 588  ILE 588  588  ?    ?   ?   A . n 
B 2 589  ALA 589  589  ?    ?   ?   A . n 
B 2 590  LYS 590  590  ?    ?   ?   A . n 
B 2 591  SER 591  591  ?    ?   ?   A . n 
B 2 592  ALA 592  592  ?    ?   ?   A . n 
B 2 593  SER 593  593  ?    ?   ?   A . n 
B 2 594  GLU 594  594  ?    ?   ?   A . n 
B 2 595  SER 595  595  ?    ?   ?   A . n 
B 2 596  ASP 596  596  ?    ?   ?   A . n 
B 2 597  ASP 597  597  ?    ?   ?   A . n 
B 2 598  SER 598  598  ?    ?   ?   A . n 
B 2 599  ASP 599  599  ?    ?   ?   A . n 
B 2 600  PRO 600  600  ?    ?   ?   A . n 
B 2 601  LYS 601  601  ?    ?   ?   A . n 
B 2 602  LYS 602  602  ?    ?   ?   A . n 
B 2 603  ILE 603  603  ?    ?   ?   A . n 
B 2 604  SER 604  604  ?    ?   ?   A . n 
B 2 605  THR 605  605  ?    ?   ?   A . n 
B 2 606  GLU 606  606  ?    ?   ?   A . n 
B 2 607  ASP 607  607  ?    ?   ?   A . n 
B 2 608  PRO 608  608  ?    ?   ?   A . n 
B 2 609  ASP 609  609  ?    ?   ?   A . n 
B 2 610  GLU 610  610  ?    ?   ?   A . n 
B 2 611  ILE 611  611  ?    ?   ?   A . n 
B 2 612  LYS 612  612  ?    ?   ?   A . n 
B 2 613  VAL 613  613  ?    ?   ?   A . n 
B 2 614  THR 614  614  ?    ?   ?   A . n 
B 2 615  LEU 615  615  ?    ?   ?   A . n 
B 2 616  PRO 616  616  ?    ?   ?   A . n 
B 2 617  LYS 617  617  ?    ?   ?   A . n 
B 2 618  GLU 618  618  ?    ?   ?   A . n 
B 2 619  VAL 619  619  ?    ?   ?   A . n 
B 2 620  LEU 620  620  ?    ?   ?   A . n 
B 2 621  ALA 621  621  ?    ?   ?   A . n 
B 2 622  THR 622  622  ?    ?   ?   A . n 
B 2 623  PHE 623  623  ?    ?   ?   A . n 
B 2 624  HIS 624  624  ?    ?   ?   A . n 
B 2 625  ASP 625  625  ?    ?   ?   A . n 
B 2 626  ALA 626  626  ?    ?   ?   A . n 
B 2 627  GLU 627  627  ?    ?   ?   A . n 
B 2 628  LEU 628  628  628  LEU LEU A . n 
B 2 629  ASP 629  629  629  ASP ASP A . n 
B 2 630  LYS 630  630  630  LYS LYS A . n 
B 2 631  ASP 631  631  631  ASP ASP A . n 
B 2 632  LEU 632  632  632  LEU LEU A . n 
B 2 633  GLU 633  633  633  GLU GLU A . n 
B 2 634  ALA 634  634  634  ALA ALA A . n 
B 2 635  HIS 635  635  635  HIS HIS A . n 
B 2 636  ASP 636  636  636  ASP ASP A . n 
B 2 637  SER 637  637  637  SER SER A . n 
B 2 638  GLU 638  638  638  GLU GLU A . n 
B 2 639  GLN 639  639  639  GLN GLN A . n 
B 2 640  SER 640  640  640  SER SER A . n 
B 2 641  ARG 641  641  641  ARG ARG A . n 
B 2 642  ILE 642  642  642  ILE ILE A . n 
B 2 643  LEU 643  643  643  LEU LEU A . n 
B 2 644  HIS 644  644  644  HIS HIS A . n 
B 2 645  GLY 645  645  645  GLY GLY A . n 
B 2 646  PHE 646  646  646  PHE PHE A . n 
B 2 647  PHE 647  647  647  PHE PHE A . n 
B 2 648  ALA 648  648  648  ALA ALA A . n 
B 2 649  VAL 649  649  649  VAL VAL A . n 
B 2 650  LEU 650  650  650  LEU LEU A . n 
B 2 651  GLY 651  651  651  GLY GLY A . n 
B 2 652  LEU 652  652  652  LEU LEU A . n 
B 2 653  CYS 653  653  653  CYS CYS A . n 
B 2 654  HIS 654  654  654  HIS HIS A . n 
B 2 655  THR 655  655  655  THR THR A . n 
B 2 656  VAL 656  656  656  VAL VAL A . n 
B 2 657  LEU 657  657  657  LEU LEU A . n 
B 2 658  ALA 658  658  658  ALA ALA A . n 
B 2 659  ALA 659  659  659  ALA ALA A . n 
B 2 660  GLU 660  660  660  GLU GLU A . n 
B 2 661  THR 661  661  661  THR THR A . n 
B 2 662  GLU 662  662  662  GLU GLU A . n 
B 2 663  PRO 663  663  663  PRO PRO A . n 
B 2 664  GLY 664  664  664  GLY GLY A . n 
B 2 665  VAL 665  665  665  VAL VAL A . n 
B 2 666  ILE 666  666  666  ILE ILE A . n 
B 2 667  GLU 667  667  667  GLU GLU A . n 
B 2 668  TYR 668  668  668  TYR TYR A . n 
B 2 669  LYS 669  669  669  LYS LYS A . n 
B 2 670  ALA 670  670  670  ALA ALA A . n 
B 2 671  GLN 671  671  671  GLN GLN A . n 
B 2 672  SER 672  672  672  SER SER A . n 
B 2 673  PRO 673  673  673  PRO PRO A . n 
B 2 674  ASP 674  674  674  ASP ASP A . n 
B 2 675  GLU 675  675  675  GLU GLU A . n 
B 2 676  ALA 676  676  676  ALA ALA A . n 
B 2 677  ALA 677  677  677  ALA ALA A . n 
B 2 678  LEU 678  678  678  LEU LEU A . n 
B 2 679  VAL 679  679  679  VAL VAL A . n 
B 2 680  GLN 680  680  680  GLN GLN A . n 
B 2 681  SER 681  681  681  SER SER A . n 
B 2 682  ALA 682  682  682  ALA ALA A . n 
B 2 683  ALA 683  683  683  ALA ALA A . n 
B 2 684  ASP 684  684  684  ASP ASP A . n 
B 2 685  VAL 685  685  685  VAL VAL A . n 
B 2 686  GLY 686  686  686  GLY GLY A . n 
B 2 687  PHE 687  687  687  PHE PHE A . n 
B 2 688  VAL 688  688  688  VAL VAL A . n 
B 2 689  PHE 689  689  689  PHE PHE A . n 
B 2 690  ARG 690  690  690  ARG ARG A . n 
B 2 691  GLY 691  691  691  GLY GLY A . n 
B 2 692  ARG 692  692  692  ARG ARG A . n 
B 2 693  ASP 693  693  693  ASP ASP A . n 
B 2 694  HIS 694  694  694  HIS HIS A . n 
B 2 695  ASN 695  695  695  ASN ASN A . n 
B 2 696  ILE 696  696  696  ILE ILE A . n 
B 2 697  LEU 697  697  697  LEU LEU A . n 
B 2 698  ARG 698  698  698  ARG ARG A . n 
B 2 699  MET 699  699  699  MET MET A . n 
B 2 700  SER 700  700  700  SER SER A . n 
B 2 701  THR 701  701  701  THR THR A . n 
B 2 702  PRO 702  702  702  PRO PRO A . n 
B 2 703  PHE 703  703  703  PHE PHE A . n 
B 2 704  SER 704  704  704  SER SER A . n 
B 2 705  ASP 705  705  705  ASP ASP A . n 
B 2 706  VAL 706  706  706  VAL VAL A . n 
B 2 707  SER 707  707  707  SER SER A . n 
B 2 708  ASP 708  708  708  ASP ASP A . n 
B 2 709  GLU 709  709  709  GLU GLU A . n 
B 2 710  TYR 710  710  710  TYR TYR A . n 
B 2 711  GLU 711  711  711  GLU GLU A . n 
B 2 712  LEU 712  712  712  LEU LEU A . n 
B 2 713  LEU 713  713  713  LEU LEU A . n 
B 2 714  HIS 714  714  714  HIS HIS A . n 
B 2 715  VAL 715  715  715  VAL VAL A . n 
B 2 716  LEU 716  716  716  LEU LEU A . n 
B 2 717  GLU 717  717  717  GLU GLU A . n 
B 2 718  PHE 718  718  718  PHE PHE A . n 
B 2 719  ASN 719  719  719  ASN ASN A . n 
B 2 720  SER 720  720  720  SER SER A . n 
B 2 721  ALA 721  721  721  ALA ALA A . n 
B 2 722  ARG 722  722  722  ARG ARG A . n 
B 2 723  LYS 723  723  723  LYS LYS A . n 
B 2 724  ARG 724  724  724  ARG ARG A . n 
B 2 725  MET 725  725  725  MET MET A . n 
B 2 726  SER 726  726  726  SER SER A . n 
B 2 727  VAL 727  727  727  VAL VAL A . n 
B 2 728  ILE 728  728  728  ILE ILE A . n 
B 2 729  LEU 729  729  729  LEU LEU A . n 
B 2 730  ARG 730  730  730  ARG ARG A . n 
B 2 731  LYS 731  731  731  LYS LYS A . n 
B 2 732  LEU 732  732  732  LEU LEU A . n 
B 2 733  ASP 733  733  733  ASP ASP A . n 
B 2 734  GLU 734  734  734  GLU GLU A . n 
B 2 735  ASP 735  735  735  ASP ASP A . n 
B 2 736  GLY 736  736  736  GLY GLY A . n 
B 2 737  ARG 737  737  737  ARG ARG A . n 
B 2 738  ILE 738  738  738  ILE ILE A . n 
B 2 739  PHE 739  739  739  PHE PHE A . n 
B 2 740  LEU 740  740  740  LEU LEU A . n 
B 2 741  LEU 741  741  741  LEU LEU A . n 
B 2 742  CYS 742  742  742  CYS CYS A . n 
B 2 743  LYS 743  743  743  LYS LYS A . n 
B 2 744  GLY 744  744  744  GLY GLY A . n 
B 2 745  ALA 745  745  745  ALA ALA A . n 
B 2 746  ASP 746  746  746  ASP ASP A . n 
B 2 747  ASN 747  747  747  ASN ASN A . n 
B 2 748  VAL 748  748  748  VAL VAL A . n 
B 2 749  ILE 749  749  749  ILE ILE A . n 
B 2 750  PHE 750  750  750  PHE PHE A . n 
B 2 751  GLU 751  751  751  GLU GLU A . n 
B 2 752  ARG 752  752  752  ARG ARG A . n 
B 2 753  LEU 753  753  753  LEU LEU A . n 
B 2 754  THR 754  754  754  THR THR A . n 
B 2 755  LYS 755  755  755  LYS LYS A . n 
B 2 756  ASP 756  756  756  ASP ASP A . n 
B 2 757  SER 757  757  757  SER SER A . n 
B 2 758  ASN 758  758  758  ASN ASN A . n 
B 2 759  GLN 759  759  759  GLN GLN A . n 
B 2 760  ARG 760  760  760  ARG ARG A . n 
B 2 761  GLU 761  761  761  GLU GLU A . n 
B 2 762  MET 762  762  762  MET MET A . n 
B 2 763  ARG 763  763  763  ARG ARG A . n 
B 2 764  GLU 764  764  764  GLU GLU A . n 
B 2 765  LYS 765  765  765  LYS LYS A . n 
B 2 766  THR 766  766  766  THR THR A . n 
B 2 767  ASP 767  767  767  ASP ASP A . n 
B 2 768  GLN 768  768  768  GLN GLN A . n 
B 2 769  ASP 769  769  769  ASP ASP A . n 
B 2 770  LEU 770  770  770  LEU LEU A . n 
B 2 771  GLN 771  771  771  GLN GLN A . n 
B 2 772  TYR 772  772  772  TYR TYR A . n 
B 2 773  PHE 773  773  773  PHE PHE A . n 
B 2 774  ALA 774  774  774  ALA ALA A . n 
B 2 775  SER 775  775  775  SER SER A . n 
B 2 776  GLU 776  776  776  GLU GLU A . n 
B 2 777  GLY 777  777  777  GLY GLY A . n 
B 2 778  LEU 778  778  778  LEU LEU A . n 
B 2 779  ARG 779  779  779  ARG ARG A . n 
B 2 780  THR 780  780  780  THR THR A . n 
B 2 781  LEU 781  781  781  LEU LEU A . n 
B 2 782  CYS 782  782  782  CYS CYS A . n 
B 2 783  LEU 783  783  783  LEU LEU A . n 
B 2 784  ALA 784  784  784  ALA ALA A . n 
B 2 785  TYR 785  785  785  TYR TYR A . n 
B 2 786  ARG 786  786  786  ARG ARG A . n 
B 2 787  ILE 787  787  787  ILE ILE A . n 
B 2 788  LEU 788  788  788  LEU LEU A . n 
B 2 789  ASP 789  789  789  ASP ASP A . n 
B 2 790  PRO 790  790  790  PRO PRO A . n 
B 2 791  GLN 791  791  791  GLN GLN A . n 
B 2 792  VAL 792  792  792  VAL VAL A . n 
B 2 793  TYR 793  793  793  TYR TYR A . n 
B 2 794  GLU 794  794  794  GLU GLU A . n 
B 2 795  GLN 795  795  795  GLN GLN A . n 
B 2 796  TRP 796  796  796  TRP TRP A . n 
B 2 797  ALA 797  797  797  ALA ALA A . n 
B 2 798  LYS 798  798  798  LYS LYS A . n 
B 2 799  GLU 799  799  799  GLU GLU A . n 
B 2 800  TYR 800  800  800  TYR TYR A . n 
B 2 801  HIS 801  801  801  HIS HIS A . n 
B 2 802  ASN 802  802  802  ASN ASN A . n 
B 2 803  ALA 803  803  803  ALA ALA A . n 
B 2 804  THR 804  804  804  THR THR A . n 
B 2 805  VAL 805  805  805  VAL VAL A . n 
B 2 806  ALA 806  806  806  ALA ALA A . n 
B 2 807  LEU 807  807  807  LEU LEU A . n 
B 2 808  GLN 808  808  808  GLN GLN A . n 
B 2 809  ASP 809  809  809  ASP ASP A . n 
B 2 810  ARG 810  810  810  ARG ARG A . n 
B 2 811  GLU 811  811  811  GLU GLU A . n 
B 2 812  GLU 812  812  812  GLU GLU A . n 
B 2 813  ARG 813  813  813  ARG ARG A . n 
B 2 814  ILE 814  814  814  ILE ILE A . n 
B 2 815  GLU 815  815  815  GLU GLU A . n 
B 2 816  SER 816  816  816  SER SER A . n 
B 2 817  VAL 817  817  817  VAL VAL A . n 
B 2 818  SER 818  818  818  SER SER A . n 
B 2 819  SER 819  819  819  SER SER A . n 
B 2 820  SER 820  820  820  SER SER A . n 
B 2 821  ILE 821  821  821  ILE ILE A . n 
B 2 822  GLU 822  822  822  GLU GLU A . n 
B 2 823  ARG 823  823  823  ARG ARG A . n 
B 2 824  ASP 824  824  824  ASP ASP A . n 
B 2 825  LEU 825  825  825  LEU LEU A . n 
B 2 826  ILE 826  826  826  ILE ILE A . n 
B 2 827  LEU 827  827  827  LEU LEU A . n 
B 2 828  LEU 828  828  828  LEU LEU A . n 
B 2 829  GLY 829  829  829  GLY GLY A . n 
B 2 830  ALA 830  830  830  ALA ALA A . n 
B 2 831  THR 831  831  831  THR THR A . n 
B 2 832  ALA 832  832  832  ALA ALA A . n 
B 2 833  ILE 833  833  833  ILE ILE A . n 
B 2 834  GLU 834  834  834  GLU GLU A . n 
B 2 835  ASP 835  835  835  ASP ASP A . n 
B 2 836  LYS 836  836  836  LYS LYS A . n 
B 2 837  LEU 837  837  837  LEU LEU A . n 
B 2 838  GLN 838  838  838  GLN GLN A . n 
B 2 839  ASP 839  839  839  ASP ASP A . n 
B 2 840  GLY 840  840  840  GLY GLY A . n 
B 2 841  VAL 841  841  841  VAL VAL A . n 
B 2 842  PRO 842  842  842  PRO PRO A . n 
B 2 843  ASP 843  843  843  ASP ASP A . n 
B 2 844  THR 844  844  844  THR THR A . n 
B 2 845  ILE 845  845  845  ILE ILE A . n 
B 2 846  SER 846  846  846  SER SER A . n 
B 2 847  ASP 847  847  847  ASP ASP A . n 
B 2 848  LEU 848  848  848  LEU LEU A . n 
B 2 849  LYS 849  849  849  LYS LYS A . n 
B 2 850  ARG 850  850  850  ARG ARG A . n 
B 2 851  ALA 851  851  851  ALA ALA A . n 
B 2 852  GLY 852  852  852  GLY GLY A . n 
B 2 853  ILE 853  853  853  ILE ILE A . n 
B 2 854  LYS 854  854  854  LYS LYS A . n 
B 2 855  VAL 855  855  855  VAL VAL A . n 
B 2 856  TRP 856  856  856  TRP TRP A . n 
B 2 857  VAL 857  857  857  VAL VAL A . n 
B 2 858  ALA 858  858  858  ALA ALA A . n 
B 2 859  THR 859  859  859  THR THR A . n 
B 2 860  GLY 860  860  860  GLY GLY A . n 
B 2 861  ASP 861  861  861  ASP ASP A . n 
B 2 862  LYS 862  862  862  LYS LYS A . n 
B 2 863  LEU 863  863  863  LEU LEU A . n 
B 2 864  GLU 864  864  864  GLU GLU A . n 
B 2 865  THR 865  865  865  THR THR A . n 
B 2 866  ALA 866  866  866  ALA ALA A . n 
B 2 867  VAL 867  867  867  VAL VAL A . n 
B 2 868  ALA 868  868  868  ALA ALA A . n 
B 2 869  ILE 869  869  869  ILE ILE A . n 
B 2 870  GLY 870  870  870  GLY GLY A . n 
B 2 871  TYR 871  871  871  TYR TYR A . n 
B 2 872  THR 872  872  872  THR THR A . n 
B 2 873  THR 873  873  873  THR THR A . n 
B 2 874  ASN 874  874  874  ASN ASN A . n 
B 2 875  LEU 875  875  875  LEU LEU A . n 
B 2 876  LEU 876  876  876  LEU LEU A . n 
B 2 877  THR 877  877  877  THR THR A . n 
B 2 878  LYS 878  878  878  LYS LYS A . n 
B 2 879  ASP 879  879  879  ASP ASP A . n 
B 2 880  THR 880  880  880  THR THR A . n 
B 2 881  ASN 881  881  881  ASN ASN A . n 
B 2 882  LEU 882  882  882  LEU LEU A . n 
B 2 883  ILE 883  883  883  ILE ILE A . n 
B 2 884  VAL 884  884  884  VAL VAL A . n 
B 2 885  VAL 885  885  885  VAL VAL A . n 
B 2 886  ARG 886  886  886  ARG ARG A . n 
B 2 887  GLU 887  887  887  GLU GLU A . n 
B 2 888  GLY 888  888  888  GLY GLY A . n 
B 2 889  ARG 889  889  889  ARG ARG A . n 
B 2 890  HIS 890  890  890  HIS HIS A . n 
B 2 891  SER 891  891  891  SER SER A . n 
B 2 892  ILE 892  892  892  ILE ILE A . n 
B 2 893  GLY 893  893  893  GLY GLY A . n 
B 2 894  ASP 894  894  894  ASP ASP A . n 
B 2 895  GLN 895  895  895  GLN GLN A . n 
B 2 896  LEU 896  896  896  LEU LEU A . n 
B 2 897  ARG 897  897  897  ARG ARG A . n 
B 2 898  GLU 898  898  898  GLU GLU A . n 
B 2 899  ALA 899  899  899  ALA ALA A . n 
B 2 900  LEU 900  900  900  LEU LEU A . n 
B 2 901  GLU 901  901  901  GLU GLU A . n 
B 2 902  GLU 902  902  902  GLU GLU A . n 
B 2 903  PHE 903  903  903  PHE PHE A . n 
B 2 904  PHE 904  904  904  PHE PHE A . n 
B 2 905  GLY 905  905  905  GLY GLY A . n 
B 2 906  GLU 906  906  906  GLU GLU A . n 
B 2 907  ASP 907  907  907  ASP ASP A . n 
B 2 908  ALA 908  908  908  ALA ALA A . n 
B 2 909  GLY 909  909  909  GLY GLY A . n 
B 2 910  LEU 910  910  910  LEU LEU A . n 
B 2 911  ARG 911  911  911  ARG ARG A . n 
B 2 912  THR 912  912  912  THR THR A . n 
B 2 913  THR 913  913  913  THR THR A . n 
B 2 914  LEU 914  914  914  LEU LEU A . n 
B 2 915  SER 915  915  915  SER SER A . n 
B 2 916  ARG 916  916  916  ARG ARG A . n 
B 2 917  ILE 917  917  917  ILE ILE A . n 
B 2 918  ASP 918  918  ?    ?   ?   A . n 
B 2 919  SER 919  919  ?    ?   ?   A . n 
B 2 920  ARG 920  920  ?    ?   ?   A . n 
B 2 921  ARG 921  921  ?    ?   ?   A . n 
B 2 922  ASN 922  922  ?    ?   ?   A . n 
B 2 923  SER 923  923  ?    ?   ?   A . n 
B 2 924  MET 924  924  ?    ?   ?   A . n 
B 2 925  ASP 925  925  ?    ?   ?   A . n 
B 2 926  PRO 926  926  ?    ?   ?   A . n 
B 2 927  PRO 927  927  ?    ?   ?   A . n 
B 2 928  ARG 928  928  ?    ?   ?   A . n 
B 2 929  LEU 929  929  ?    ?   ?   A . n 
B 2 930  THR 930  930  ?    ?   ?   A . n 
B 2 931  ARG 931  931  ?    ?   ?   A . n 
B 2 932  VAL 932  932  ?    ?   ?   A . n 
B 2 933  ASN 933  933  ?    ?   ?   A . n 
B 2 934  THR 934  934  ?    ?   ?   A . n 
B 2 935  GLY 935  935  ?    ?   ?   A . n 
B 2 936  VAL 936  936  ?    ?   ?   A . n 
B 2 937  ARG 937  937  ?    ?   ?   A . n 
B 2 938  SER 938  938  ?    ?   ?   A . n 
B 2 939  LEU 939  939  939  LEU LEU A . n 
B 2 940  VAL 940  940  940  VAL VAL A . n 
B 2 941  GLY 941  941  941  GLY GLY A . n 
B 2 942  ARG 942  942  942  ARG ARG A . n 
B 2 943  ASP 943  943  943  ASP ASP A . n 
B 2 944  ASN 944  944  944  ASN ASN A . n 
B 2 945  GLY 945  945  945  GLY GLY A . n 
B 2 946  THR 946  946  946  THR THR A . n 
B 2 947  ARG 947  947  947  ARG ARG A . n 
B 2 948  PRO 948  948  948  PRO PRO A . n 
B 2 949  GLY 949  949  949  GLY GLY A . n 
B 2 950  GLY 950  950  950  GLY GLY A . n 
B 2 951  PHE 951  951  951  PHE PHE A . n 
B 2 952  SER 952  952  952  SER SER A . n 
B 2 953  LEU 953  953  953  LEU LEU A . n 
B 2 954  VAL 954  954  954  VAL VAL A . n 
B 2 955  ILE 955  955  955  ILE ILE A . n 
B 2 956  GLU 956  956  956  GLU GLU A . n 
B 2 957  GLY 957  957  957  GLY GLY A . n 
B 2 958  HIS 958  958  958  HIS HIS A . n 
B 2 959  ALA 959  959  959  ALA ALA A . n 
B 2 960  LEU 960  960  960  LEU LEU A . n 
B 2 961  ALA 961  961  961  ALA ALA A . n 
B 2 962  HIS 962  962  962  HIS HIS A . n 
B 2 963  CYS 963  963  963  CYS CYS A . n 
B 2 964  PHE 964  964  964  PHE PHE A . n 
B 2 965  ASP 965  965  965  ASP ASP A . n 
B 2 966  ASP 966  966  966  ASP ASP A . n 
B 2 967  GLU 967  967  967  GLU GLU A . n 
B 2 968  GLU 968  968  968  GLU GLU A . n 
B 2 969  THR 969  969  969  THR THR A . n 
B 2 970  GLU 970  970  970  GLU GLU A . n 
B 2 971  ALA 971  971  971  ALA ALA A . n 
B 2 972  LEU 972  972  972  LEU LEU A . n 
B 2 973  LEU 973  973  973  LEU LEU A . n 
B 2 974  LEU 974  974  974  LEU LEU A . n 
B 2 975  ALA 975  975  975  ALA ALA A . n 
B 2 976  LEU 976  976  976  LEU LEU A . n 
B 2 977  SER 977  977  977  SER SER A . n 
B 2 978  THR 978  978  978  THR THR A . n 
B 2 979  ARG 979  979  979  ARG ARG A . n 
B 2 980  CYS 980  980  980  CYS CYS A . n 
B 2 981  ASN 981  981  981  ASN ASN A . n 
B 2 982  THR 982  982  982  THR THR A . n 
B 2 983  VAL 983  983  983  VAL VAL A . n 
B 2 984  ILE 984  984  984  ILE ILE A . n 
B 2 985  CYS 985  985  985  CYS CYS A . n 
B 2 986  CYS 986  986  986  CYS CYS A . n 
B 2 987  ARG 987  987  987  ARG ARG A . n 
B 2 988  VAL 988  988  988  VAL VAL A . n 
B 2 989  SER 989  989  989  SER SER A . n 
B 2 990  PRO 990  990  990  PRO PRO A . n 
B 2 991  LEU 991  991  991  LEU LEU A . n 
B 2 992  GLN 992  992  992  GLN GLN A . n 
B 2 993  LYS 993  993  993  LYS LYS A . n 
B 2 994  ALA 994  994  994  ALA ALA A . n 
B 2 995  GLN 995  995  995  GLN GLN A . n 
B 2 996  ILE 996  996  996  ILE ILE A . n 
B 2 997  VAL 997  997  997  VAL VAL A . n 
B 2 998  HIS 998  998  998  HIS HIS A . n 
B 2 999  LEU 999  999  999  LEU LEU A . n 
B 2 1000 ILE 1000 1000 1000 ILE ILE A . n 
B 2 1001 LYS 1001 1001 1001 LYS LYS A . n 
B 2 1002 ASP 1002 1002 1002 ASP ASP A . n 
B 2 1003 ASN 1003 1003 1003 ASN ASN A . n 
B 2 1004 LEU 1004 1004 1004 LEU LEU A . n 
B 2 1005 GLY 1005 1005 1005 GLY GLY A . n 
B 2 1006 VAL 1006 1006 1006 VAL VAL A . n 
B 2 1007 MET 1007 1007 1007 MET MET A . n 
B 2 1008 CYS 1008 1008 1008 CYS CYS A . n 
B 2 1009 LEU 1009 1009 1009 LEU LEU A . n 
B 2 1010 ALA 1010 1010 1010 ALA ALA A . n 
B 2 1011 ILE 1011 1011 1011 ILE ILE A . n 
B 2 1012 GLY 1012 1012 1012 GLY GLY A . n 
B 2 1013 ASP 1013 1013 1013 ASP ASP A . n 
B 2 1014 GLY 1014 1014 1014 GLY GLY A . n 
B 2 1015 ALA 1015 1015 1015 ALA ALA A . n 
B 2 1016 ASN 1016 1016 1016 ASN ASN A . n 
B 2 1017 ASP 1017 1017 1017 ASP ASP A . n 
B 2 1018 VAL 1018 1018 1018 VAL VAL A . n 
B 2 1019 SER 1019 1019 1019 SER SER A . n 
B 2 1020 MET 1020 1020 1020 MET MET A . n 
B 2 1021 ILE 1021 1021 1021 ILE ILE A . n 
B 2 1022 GLN 1022 1022 1022 GLN GLN A . n 
B 2 1023 ALA 1023 1023 1023 ALA ALA A . n 
B 2 1024 ALA 1024 1024 1024 ALA ALA A . n 
B 2 1025 ASP 1025 1025 1025 ASP ASP A . n 
B 2 1026 VAL 1026 1026 1026 VAL VAL A . n 
B 2 1027 GLY 1027 1027 1027 GLY GLY A . n 
B 2 1028 VAL 1028 1028 1028 VAL VAL A . n 
B 2 1029 GLY 1029 1029 1029 GLY GLY A . n 
B 2 1030 ILE 1030 1030 1030 ILE ILE A . n 
B 2 1031 SER 1031 1031 1031 SER SER A . n 
B 2 1032 GLY 1032 1032 1032 GLY GLY A . n 
B 2 1033 GLU 1033 1033 1033 GLU GLU A . n 
B 2 1034 GLU 1034 1034 1034 GLU GLU A . n 
B 2 1035 GLY 1035 1035 1035 GLY GLY A . n 
B 2 1036 LEU 1036 1036 1036 LEU LEU A . n 
B 2 1037 GLN 1037 1037 1037 GLN GLN A . n 
B 2 1038 ALA 1038 1038 1038 ALA ALA A . n 
B 2 1039 VAL 1039 1039 1039 VAL VAL A . n 
B 2 1040 ASN 1040 1040 1040 ASN ASN A . n 
B 2 1041 SER 1041 1041 1041 SER SER A . n 
B 2 1042 SER 1042 1042 1042 SER SER A . n 
B 2 1043 ASP 1043 1043 1043 ASP ASP A . n 
B 2 1044 TYR 1044 1044 1044 TYR TYR A . n 
B 2 1045 ALA 1045 1045 1045 ALA ALA A . n 
B 2 1046 ILE 1046 1046 1046 ILE ILE A . n 
B 2 1047 ALA 1047 1047 1047 ALA ALA A . n 
B 2 1048 GLN 1048 1048 1048 GLN GLN A . n 
B 2 1049 PHE 1049 1049 1049 PHE PHE A . n 
B 2 1050 ARG 1050 1050 1050 ARG ARG A . n 
B 2 1051 TYR 1051 1051 1051 TYR TYR A . n 
B 2 1052 LEU 1052 1052 1052 LEU LEU A . n 
B 2 1053 LYS 1053 1053 1053 LYS LYS A . n 
B 2 1054 ARG 1054 1054 1054 ARG ARG A . n 
B 2 1055 LEU 1055 1055 1055 LEU LEU A . n 
B 2 1056 LEU 1056 1056 1056 LEU LEU A . n 
B 2 1057 LEU 1057 1057 1057 LEU LEU A . n 
B 2 1058 VAL 1058 1058 1058 VAL VAL A . n 
B 2 1059 HIS 1059 1059 1059 HIS HIS A . n 
B 2 1060 GLY 1060 1060 1060 GLY GLY A . n 
B 2 1061 HIS 1061 1061 1061 HIS HIS A . n 
B 2 1062 TRP 1062 1062 1062 TRP TRP A . n 
B 2 1063 SER 1063 1063 1063 SER SER A . n 
B 2 1064 TYR 1064 1064 1064 TYR TYR A . n 
B 2 1065 PHE 1065 1065 1065 PHE PHE A . n 
B 2 1066 ARG 1066 1066 1066 ARG ARG A . n 
B 2 1067 ASN 1067 1067 1067 ASN ASN A . n 
B 2 1068 SER 1068 1068 1068 SER SER A . n 
B 2 1069 SER 1069 1069 1069 SER SER A . n 
B 2 1070 MET 1070 1070 1070 MET MET A . n 
B 2 1071 ILE 1071 1071 1071 ILE ILE A . n 
B 2 1072 LEU 1072 1072 1072 LEU LEU A . n 
B 2 1073 ASN 1073 1073 1073 ASN ASN A . n 
B 2 1074 PHE 1074 1074 1074 PHE PHE A . n 
B 2 1075 PHE 1075 1075 1075 PHE PHE A . n 
B 2 1076 TYR 1076 1076 1076 TYR TYR A . n 
B 2 1077 LYS 1077 1077 1077 LYS LYS A . n 
B 2 1078 ASN 1078 1078 1078 ASN ASN A . n 
B 2 1079 ILE 1079 1079 1079 ILE ILE A . n 
B 2 1080 ILE 1080 1080 1080 ILE ILE A . n 
B 2 1081 GLY 1081 1081 1081 GLY GLY A . n 
B 2 1082 ILE 1082 1082 1082 ILE ILE A . n 
B 2 1083 GLY 1083 1083 1083 GLY GLY A . n 
B 2 1084 VAL 1084 1084 1084 VAL VAL A . n 
B 2 1085 LEU 1085 1085 1085 LEU LEU A . n 
B 2 1086 PHE 1086 1086 1086 PHE PHE A . n 
B 2 1087 TRP 1087 1087 1087 TRP TRP A . n 
B 2 1088 PHE 1088 1088 1088 PHE PHE A . n 
B 2 1089 MET 1089 1089 1089 MET MET A . n 
B 2 1090 ILE 1090 1090 1090 ILE ILE A . n 
B 2 1091 TYR 1091 1091 1091 TYR TYR A . n 
B 2 1092 CYS 1092 1092 1092 CYS CYS A . n 
B 2 1093 GLY 1093 1093 1093 GLY GLY A . n 
B 2 1094 TRP 1094 1094 1094 TRP TRP A . n 
B 2 1095 SER 1095 1095 1095 SER SER A . n 
B 2 1096 THR 1096 1096 1096 THR THR A . n 
B 2 1097 THR 1097 1097 1097 THR THR A . n 
B 2 1098 TYR 1098 1098 1098 TYR TYR A . n 
B 2 1099 VAL 1099 1099 1099 VAL VAL A . n 
B 2 1100 PHE 1100 1100 1100 PHE PHE A . n 
B 2 1101 ALA 1101 1101 1101 ALA ALA A . n 
B 2 1102 TYR 1102 1102 1102 TYR TYR A . n 
B 2 1103 VAL 1103 1103 1103 VAL VAL A . n 
B 2 1104 TYR 1104 1104 1104 TYR TYR A . n 
B 2 1105 LEU 1105 1105 1105 LEU LEU A . n 
B 2 1106 LEU 1106 1106 1106 LEU LEU A . n 
B 2 1107 PHE 1107 1107 1107 PHE PHE A . n 
B 2 1108 TRP 1108 1108 1108 TRP TRP A . n 
B 2 1109 ASN 1109 1109 1109 ASN ASN A . n 
B 2 1110 VAL 1110 1110 1110 VAL VAL A . n 
B 2 1111 PHE 1111 1111 1111 PHE PHE A . n 
B 2 1112 TRP 1112 1112 1112 TRP TRP A . n 
B 2 1113 THR 1113 1113 1113 THR THR A . n 
B 2 1114 LEU 1114 1114 1114 LEU LEU A . n 
B 2 1115 VAL 1115 1115 1115 VAL VAL A . n 
B 2 1116 PRO 1116 1116 1116 PRO PRO A . n 
B 2 1117 VAL 1117 1117 1117 VAL VAL A . n 
B 2 1118 ILE 1118 1118 1118 ILE ILE A . n 
B 2 1119 ALA 1119 1119 1119 ALA ALA A . n 
B 2 1120 ILE 1120 1120 1120 ILE ILE A . n 
B 2 1121 GLY 1121 1121 1121 GLY GLY A . n 
B 2 1122 LEU 1122 1122 1122 LEU LEU A . n 
B 2 1123 PHE 1123 1123 1123 PHE PHE A . n 
B 2 1124 ASP 1124 1124 1124 ASP ASP A . n 
B 2 1125 ARG 1125 1125 1125 ARG ARG A . n 
B 2 1126 ASN 1126 1126 1126 ASN ASN A . n 
B 2 1127 ILE 1127 1127 1127 ILE ILE A . n 
B 2 1128 ASP 1128 1128 1128 ASP ASP A . n 
B 2 1129 ASP 1129 1129 1129 ASP ASP A . n 
B 2 1130 GLU 1130 1130 1130 GLU GLU A . n 
B 2 1131 THR 1131 1131 1131 THR THR A . n 
B 2 1132 LEU 1132 1132 1132 LEU LEU A . n 
B 2 1133 MET 1133 1133 1133 MET MET A . n 
B 2 1134 ALA 1134 1134 1134 ALA ALA A . n 
B 2 1135 LEU 1135 1135 1135 LEU LEU A . n 
B 2 1136 PRO 1136 1136 1136 PRO PRO A . n 
B 2 1137 GLU 1137 1137 1137 GLU GLU A . n 
B 2 1138 LEU 1138 1138 1138 LEU LEU A . n 
B 2 1139 TYR 1139 1139 1139 TYR TYR A . n 
B 2 1140 ARG 1140 1140 1140 ARG ARG A . n 
B 2 1141 ALA 1141 1141 1141 ALA ALA A . n 
B 2 1142 SER 1142 1142 1142 SER SER A . n 
B 2 1143 ARG 1143 1143 1143 ARG ARG A . n 
B 2 1144 GLU 1144 1144 1144 GLU GLU A . n 
B 2 1145 GLY 1145 1145 1145 GLY GLY A . n 
B 2 1146 LYS 1146 1146 1146 LYS LYS A . n 
B 2 1147 TYR 1147 1147 1147 TYR TYR A . n 
B 2 1148 PHE 1148 1148 1148 PHE PHE A . n 
B 2 1149 GLY 1149 1149 1149 GLY GLY A . n 
B 2 1150 LEU 1150 1150 1150 LEU LEU A . n 
B 2 1151 MET 1151 1151 1151 MET MET A . n 
B 2 1152 ARG 1152 1152 1152 ARG ARG A . n 
B 2 1153 PHE 1153 1153 1153 PHE PHE A . n 
B 2 1154 ALA 1154 1154 1154 ALA ALA A . n 
B 2 1155 TYR 1155 1155 1155 TYR TYR A . n 
B 2 1156 TYR 1156 1156 1156 TYR TYR A . n 
B 2 1157 ILE 1157 1157 1157 ILE ILE A . n 
B 2 1158 PHE 1158 1158 1158 PHE PHE A . n 
B 2 1159 GLU 1159 1159 1159 GLU GLU A . n 
B 2 1160 GLY 1160 1160 1160 GLY GLY A . n 
B 2 1161 VAL 1161 1161 1161 VAL VAL A . n 
B 2 1162 TYR 1162 1162 1162 TYR TYR A . n 
B 2 1163 GLN 1163 1163 1163 GLN GLN A . n 
B 2 1164 SER 1164 1164 1164 SER SER A . n 
B 2 1165 ALA 1165 1165 1165 ALA ALA A . n 
B 2 1166 VAL 1166 1166 1166 VAL VAL A . n 
B 2 1167 ILE 1167 1167 1167 ILE ILE A . n 
B 2 1168 TYR 1168 1168 1168 TYR TYR A . n 
B 2 1169 PHE 1169 1169 1169 PHE PHE A . n 
B 2 1170 PHE 1170 1170 1170 PHE PHE A . n 
B 2 1171 LEU 1171 1171 1171 LEU LEU A . n 
B 2 1172 ASN 1172 1172 1172 ASN ASN A . n 
B 2 1173 TYR 1173 1173 1173 TYR TYR A . n 
B 2 1174 THR 1174 1174 1174 THR THR A . n 
B 2 1175 TYR 1175 1175 1175 TYR TYR A . n 
B 2 1176 VAL 1176 1176 1176 VAL VAL A . n 
B 2 1177 THR 1177 1177 1177 THR THR A . n 
B 2 1178 THR 1178 1178 1178 THR THR A . n 
B 2 1179 THR 1179 1179 1179 THR THR A . n 
B 2 1180 ALA 1180 1180 1180 ALA ALA A . n 
B 2 1181 ARG 1181 1181 1181 ARG ARG A . n 
B 2 1182 GLY 1182 1182 1182 GLY GLY A . n 
B 2 1183 ASP 1183 1183 1183 ASP ASP A . n 
B 2 1184 GLY 1184 1184 1184 GLY GLY A . n 
B 2 1185 TYR 1185 1185 1185 TYR TYR A . n 
B 2 1186 ASP 1186 1186 1186 ASP ASP A . n 
B 2 1187 VAL 1187 1187 1187 VAL VAL A . n 
B 2 1188 TYR 1188 1188 1188 TYR TYR A . n 
B 2 1189 MET 1189 1189 1189 MET MET A . n 
B 2 1190 TYR 1190 1190 1190 TYR TYR A . n 
B 2 1191 GLU 1191 1191 1191 GLU GLU A . n 
B 2 1192 MET 1192 1192 1192 MET MET A . n 
B 2 1193 SER 1193 1193 1193 SER SER A . n 
B 2 1194 THR 1194 1194 1194 THR THR A . n 
B 2 1195 THR 1195 1195 1195 THR THR A . n 
B 2 1196 GLN 1196 1196 1196 GLN GLN A . n 
B 2 1197 ALA 1197 1197 1197 ALA ALA A . n 
B 2 1198 ILE 1198 1198 1198 ILE ILE A . n 
B 2 1199 GLY 1199 1199 1199 GLY GLY A . n 
B 2 1200 ALA 1200 1200 1200 ALA ALA A . n 
B 2 1201 VAL 1201 1201 1201 VAL VAL A . n 
B 2 1202 MET 1202 1202 1202 MET MET A . n 
B 2 1203 VAL 1203 1203 1203 VAL VAL A . n 
B 2 1204 ALA 1204 1204 1204 ALA ALA A . n 
B 2 1205 ASN 1205 1205 1205 ASN ASN A . n 
B 2 1206 LEU 1206 1206 1206 LEU LEU A . n 
B 2 1207 PHE 1207 1207 1207 PHE PHE A . n 
B 2 1208 SER 1208 1208 1208 SER SER A . n 
B 2 1209 GLY 1209 1209 1209 GLY GLY A . n 
B 2 1210 LEU 1210 1210 1210 LEU LEU A . n 
B 2 1211 ASN 1211 1211 1211 ASN ASN A . n 
B 2 1212 ILE 1212 1212 1212 ILE ILE A . n 
B 2 1213 ASP 1213 1213 1213 ASP ASP A . n 
B 2 1214 ALA 1214 1214 1214 ALA ALA A . n 
B 2 1215 TRP 1215 1215 1215 TRP TRP A . n 
B 2 1216 THR 1216 1216 1216 THR THR A . n 
B 2 1217 GLY 1217 1217 1217 GLY GLY A . n 
B 2 1218 TRP 1218 1218 1218 TRP TRP A . n 
B 2 1219 VAL 1219 1219 1219 VAL VAL A . n 
B 2 1220 TRP 1220 1220 1220 TRP TRP A . n 
B 2 1221 PHE 1221 1221 1221 PHE PHE A . n 
B 2 1222 ALA 1222 1222 1222 ALA ALA A . n 
B 2 1223 ILE 1223 1223 1223 ILE ILE A . n 
B 2 1224 TRP 1224 1224 1224 TRP TRP A . n 
B 2 1225 PHE 1225 1225 1225 PHE PHE A . n 
B 2 1226 GLY 1226 1226 1226 GLY GLY A . n 
B 2 1227 PRO 1227 1227 1227 PRO PRO A . n 
B 2 1228 PHE 1228 1228 1228 PHE PHE A . n 
B 2 1229 LEU 1229 1229 1229 LEU LEU A . n 
B 2 1230 ILE 1230 1230 1230 ILE ILE A . n 
B 2 1231 TRP 1231 1231 1231 TRP TRP A . n 
B 2 1232 VAL 1232 1232 1232 VAL VAL A . n 
B 2 1233 PHE 1233 1233 1233 PHE PHE A . n 
B 2 1234 THR 1234 1234 1234 THR THR A . n 
B 2 1235 ALA 1235 1235 1235 ALA ALA A . n 
B 2 1236 VAL 1236 1236 1236 VAL VAL A . n 
B 2 1237 TYR 1237 1237 1237 TYR TYR A . n 
B 2 1238 SER 1238 1238 1238 SER SER A . n 
B 2 1239 VAL 1239 1239 1239 VAL VAL A . n 
B 2 1240 ILE 1240 1240 1240 ILE ILE A . n 
B 2 1241 PRO 1241 1241 1241 PRO PRO A . n 
B 2 1242 PRO 1242 1242 1242 PRO PRO A . n 
B 2 1243 SER 1243 1243 1243 SER SER A . n 
B 2 1244 SER 1244 1244 1244 SER SER A . n 
B 2 1245 PHE 1245 1245 1245 PHE PHE A . n 
B 2 1246 TYR 1246 1246 1246 TYR TYR A . n 
B 2 1247 THR 1247 1247 1247 THR THR A . n 
B 2 1248 GLY 1248 1248 1248 GLY GLY A . n 
B 2 1249 VAL 1249 1249 1249 VAL VAL A . n 
B 2 1250 TYR 1250 1250 1250 TYR TYR A . n 
B 2 1251 GLY 1251 1251 1251 GLY GLY A . n 
B 2 1252 ASN 1252 1252 1252 ASN ASN A . n 
B 2 1253 ASP 1253 1253 1253 ASP ASP A . n 
B 2 1254 VAL 1254 1254 1254 VAL VAL A . n 
B 2 1255 PHE 1255 1255 1255 PHE PHE A . n 
B 2 1256 LEU 1256 1256 1256 LEU LEU A . n 
B 2 1257 PHE 1257 1257 1257 PHE PHE A . n 
B 2 1258 ARG 1258 1258 1258 ARG ARG A . n 
B 2 1259 SER 1259 1259 1259 SER SER A . n 
B 2 1260 ALA 1260 1260 1260 ALA ALA A . n 
B 2 1261 ALA 1261 1261 1261 ALA ALA A . n 
B 2 1262 TYR 1262 1262 1262 TYR TYR A . n 
B 2 1263 TRP 1263 1263 1263 TRP TRP A . n 
B 2 1264 PHE 1264 1264 1264 PHE PHE A . n 
B 2 1265 GLY 1265 1265 1265 GLY GLY A . n 
B 2 1266 TRP 1266 1266 1266 TRP TRP A . n 
B 2 1267 PRO 1267 1267 1267 PRO PRO A . n 
B 2 1268 PHE 1268 1268 1268 PHE PHE A . n 
B 2 1269 VAL 1269 1269 1269 VAL VAL A . n 
B 2 1270 THR 1270 1270 1270 THR THR A . n 
B 2 1271 ILE 1271 1271 1271 ILE ILE A . n 
B 2 1272 ILE 1272 1272 1272 ILE ILE A . n 
B 2 1273 ALA 1273 1273 1273 ALA ALA A . n 
B 2 1274 LEU 1274 1274 1274 LEU LEU A . n 
B 2 1275 LEU 1275 1275 1275 LEU LEU A . n 
B 2 1276 PRO 1276 1276 1276 PRO PRO A . n 
B 2 1277 ARG 1277 1277 1277 ARG ARG A . n 
B 2 1278 TYR 1278 1278 1278 TYR TYR A . n 
B 2 1279 LEU 1279 1279 1279 LEU LEU A . n 
B 2 1280 ILE 1280 1280 1280 ILE ILE A . n 
B 2 1281 LYS 1281 1281 1281 LYS LYS A . n 
B 2 1282 THR 1282 1282 1282 THR THR A . n 
B 2 1283 PHE 1283 1283 1283 PHE PHE A . n 
B 2 1284 ARG 1284 1284 1284 ARG ARG A . n 
B 2 1285 GLN 1285 1285 1285 GLN GLN A . n 
B 2 1286 ASN 1286 1286 1286 ASN ASN A . n 
B 2 1287 ILE 1287 1287 1287 ILE ILE A . n 
B 2 1288 PHE 1288 1288 1288 PHE PHE A . n 
B 2 1289 PRO 1289 1289 1289 PRO PRO A . n 
B 2 1290 ASN 1290 1290 1290 ASN ASN A . n 
B 2 1291 ASP 1291 1291 1291 ASP ASP A . n 
B 2 1292 VAL 1292 1292 1292 VAL VAL A . n 
B 2 1293 ASP 1293 1293 1293 ASP ASP A . n 
B 2 1294 THR 1294 1294 1294 THR THR A . n 
B 2 1295 MET 1295 1295 1295 MET MET A . n 
B 2 1296 ARG 1296 1296 1296 ARG ARG A . n 
B 2 1297 LEU 1297 1297 1297 LEU LEU A . n 
B 2 1298 VAL 1298 1298 1298 VAL VAL A . n 
B 2 1299 ARG 1299 1299 1299 ARG ARG A . n 
B 2 1300 LYS 1300 1300 1300 LYS LYS A . n 
B 2 1301 TYR 1301 1301 1301 TYR TYR A . n 
B 2 1302 HIS 1302 1302 1302 HIS HIS A . n 
B 2 1303 PRO 1303 1303 1303 PRO PRO A . n 
B 2 1304 GLU 1304 1304 1304 GLU GLU A . n 
B 2 1305 VAL 1305 1305 1305 VAL VAL A . n 
B 2 1306 ASP 1306 1306 1306 ASP ASP A . n 
B 2 1307 LEU 1307 1307 1307 LEU LEU A . n 
B 2 1308 TYR 1308 1308 1308 TYR TYR A . n 
B 2 1309 ASN 1309 1309 1309 ASN ASN A . n 
B 2 1310 HIS 1310 1310 1310 HIS HIS A . n 
B 2 1311 PRO 1311 1311 1311 PRO PRO A . n 
B 2 1312 MET 1312 1312 1312 MET MET A . n 
B 2 1313 LEU 1313 1313 1313 LEU LEU A . n 
B 2 1314 GLY 1314 1314 1314 GLY GLY A . n 
B 2 1315 GLY 1315 1315 1315 GLY GLY A . n 
B 2 1316 LYS 1316 1316 1316 LYS LYS A . n 
B 2 1317 LEU 1317 1317 1317 LEU LEU A . n 
B 2 1318 ALA 1318 1318 1318 ALA ALA A . n 
B 2 1319 PRO 1319 1319 ?    ?   ?   A . n 
B 2 1320 LYS 1320 1320 ?    ?   ?   A . n 
B 2 1321 LYS 1321 1321 ?    ?   ?   A . n 
B 2 1322 ASP 1322 1322 ?    ?   ?   A . n 
B 2 1323 GLU 1323 1323 ?    ?   ?   A . n 
B 2 1324 ASP 1324 1324 ?    ?   ?   A . n 
B 2 1325 GLU 1325 1325 ?    ?   ?   A . n 
B 2 1326 SER 1326 1326 ?    ?   ?   A . n 
B 2 1327 ASP 1327 1327 ?    ?   ?   A . n 
B 2 1328 TYR 1328 1328 ?    ?   ?   A . n 
B 2 1329 GLY 1329 1329 ?    ?   ?   A . n 
B 2 1330 GLU 1330 1330 ?    ?   ?   A . n 
B 2 1331 GLU 1331 1331 ?    ?   ?   A . n 
B 2 1332 PRO 1332 1332 ?    ?   ?   A . n 
B 2 1333 PHE 1333 1333 ?    ?   ?   A . n 
B 2 1334 ASP 1334 1334 ?    ?   ?   A . n 
B 2 1335 GLY 1335 1335 ?    ?   ?   A . n 
B 2 1336 PRO 1336 1336 ?    ?   ?   A . n 
B 2 1337 GLU 1337 1337 ?    ?   ?   A . n 
B 2 1338 GLY 1338 1338 ?    ?   ?   A . n 
B 2 1339 ARG 1339 1339 ?    ?   ?   A . n 
B 2 1340 ARG 1340 1340 ?    ?   ?   A . n 
B 2 1341 SER 1341 1341 ?    ?   ?   A . n 
B 2 1342 SER 1342 1342 ?    ?   ?   A . n 
B 2 1343 ILE 1343 1343 ?    ?   ?   A . n 
B 2 1344 LYS 1344 1344 ?    ?   ?   A . n 
B 2 1345 MET 1345 1345 ?    ?   ?   A . n 
B 2 1346 ALA 1346 1346 ?    ?   ?   A . n 
B 2 1347 ASN 1347 1347 ?    ?   ?   A . n 
B 2 1348 LEU 1348 1348 ?    ?   ?   A . n 
B 2 1349 ARG 1349 1349 ?    ?   ?   A . n 
B 2 1350 HIS 1350 1350 ?    ?   ?   A . n 
B 2 1351 SER 1351 1351 ?    ?   ?   A . n 
B 2 1352 HIS 1352 1352 ?    ?   ?   A . n 
B 2 1353 GLY 1353 1353 ?    ?   ?   A . n 
B 2 1354 ALA 1354 1354 ?    ?   ?   A . n 
B 2 1355 PHE 1355 1355 ?    ?   ?   A . n 
B 2 1356 GLY 1356 1356 ?    ?   ?   A . n 
B 2 1357 ARG 1357 1357 ?    ?   ?   A . n 
B 2 1358 GLY 1358 1358 ?    ?   ?   A . n 
B 2 1359 ASP 1359 1359 ?    ?   ?   A . n 
B 2 1360 GLN 1360 1360 ?    ?   ?   A . n 
B 2 1361 ALA 1361 1361 ?    ?   ?   A . n 
B 2 1362 GLY 1362 1362 ?    ?   ?   A . n 
B 2 1363 ASP 1363 1363 ?    ?   ?   A . n 
B 2 1364 MET 1364 1364 ?    ?   ?   A . n 
B 2 1365 GLU 1365 1365 ?    ?   ?   A . n 
B 2 1366 LEU 1366 1366 ?    ?   ?   A . n 
B 2 1367 GLY 1367 1367 ?    ?   ?   A . n 
B 2 1368 MET 1368 1368 ?    ?   ?   A . n 
B 2 1369 GLY 1369 1369 ?    ?   ?   A . n 
B 2 1370 ARG 1370 1370 ?    ?   ?   A . n 
B 2 1371 LYS 1371 1371 ?    ?   ?   A . n 
B 2 1372 SER 1372 1372 ?    ?   ?   A . n 
B 2 1373 LEU 1373 1373 ?    ?   ?   A . n 
B 2 1374 GLY 1374 1374 ?    ?   ?   A . n 
B 2 1375 ASN 1375 1375 ?    ?   ?   A . n 
B 2 1376 ARG 1376 1376 ?    ?   ?   A . n 
B 2 1377 PRO 1377 1377 ?    ?   ?   A . n 
B 2 1378 GLY 1378 1378 ?    ?   ?   A . n 
B 2 1379 LEU 1379 1379 ?    ?   ?   A . n 
B 2 1380 ARG 1380 1380 ?    ?   ?   A . n 
B 2 1381 SER 1381 1381 ?    ?   ?   A . n 
B 2 1382 SER 1382 1382 ?    ?   ?   A . n 
B 2 1383 MET 1383 1383 ?    ?   ?   A . n 
B 2 1384 ASP 1384 1384 ?    ?   ?   A . n 
B 2 1385 SER 1385 1385 ?    ?   ?   A . n 
B 2 1386 SER 1386 1386 ?    ?   ?   A . n 
B 2 1387 ARG 1387 1387 ?    ?   ?   A . n 
B 2 1388 PHE 1388 1388 ?    ?   ?   A . n 
B 2 1389 GLY 1389 1389 ?    ?   ?   A . n 
B 2 1390 ILE 1390 1390 ?    ?   ?   A . n 
B 2 1391 HIS 1391 1391 ?    ?   ?   A . n 
B 2 1392 SER 1392 1392 ?    ?   ?   A . n 
B 2 1393 GLY 1393 1393 ?    ?   ?   A . n 
B 2 1394 ALA 1394 1394 ?    ?   ?   A . n 
B 2 1395 ARG 1395 1395 ?    ?   ?   A . n 
B 2 1396 GLY 1396 1396 ?    ?   ?   A . n 
B 2 1397 SER 1397 1397 ?    ?   ?   A . n 
B 2 1398 THR 1398 1398 ?    ?   ?   A . n 
B 2 1399 VAL 1399 1399 ?    ?   ?   A . n 
B 2 1400 ASP 1400 1400 ?    ?   ?   A . n 
B 2 1401 MET 1401 1401 ?    ?   ?   A . n 
B 2 1402 SER 1402 1402 ?    ?   ?   A . n 
B 2 1403 THR 1403 1403 ?    ?   ?   A . n 
B 2 1404 GLY 1404 1404 ?    ?   ?   A . n 
B 2 1405 LEU 1405 1405 ?    ?   ?   A . n 
B 2 1406 GLU 1406 1406 ?    ?   ?   A . n 
B 2 1407 GLN 1407 1407 ?    ?   ?   A . n 
B 2 1408 PRO 1408 1408 ?    ?   ?   A . n 
B 2 1409 PRO 1409 1409 ?    ?   ?   A . n 
B 2 1410 SER 1410 1410 ?    ?   ?   A . n 
B 2 1411 ARG 1411 1411 1411 ARG ARG A . n 
B 2 1412 GLY 1412 1412 1412 GLY GLY A . n 
B 2 1413 PHE 1413 1413 1413 PHE PHE A . n 
B 2 1414 GLY 1414 1414 1414 GLY GLY A . n 
B 2 1415 PHE 1415 1415 1415 PHE PHE A . n 
B 2 1416 THR 1416 1416 1416 THR THR A . n 
B 2 1417 MET 1417 1417 1417 MET MET A . n 
B 2 1418 GLU 1418 1418 1418 GLU GLU A . n 
B 2 1419 GLU 1419 1419 1419 GLU GLU A . n 
B 2 1420 GLY 1420 1420 1420 GLY GLY A . n 
B 2 1421 GLY 1421 1421 1421 GLY GLY A . n 
B 2 1422 VAL 1422 1422 1422 VAL VAL A . n 
B 2 1423 ALA 1423 1423 1423 ALA ALA A . n 
B 2 1424 ILE 1424 1424 1424 ILE ILE A . n 
B 2 1425 GLN 1425 1425 1425 GLN GLN A . n 
B 2 1426 ARG 1426 1426 1426 ARG ARG A . n 
B 2 1427 MET 1427 1427 1427 MET MET A . n 
B 2 1428 GLN 1428 1428 1428 GLN GLN A . n 
B 2 1429 SER 1429 1429 1429 SER SER A . n 
B 2 1430 ARG 1430 1430 1430 ARG ARG A . n 
B 2 1431 LEU 1431 1431 1431 LEU LEU A . n 
B 2 1432 SER 1432 1432 ?    ?   ?   A . n 
B 2 1433 GLN 1433 1433 ?    ?   ?   A . n 
B 2 1434 THR 1434 1434 ?    ?   ?   A . n 
B 2 1435 SER 1435 1435 ?    ?   ?   A . n 
B 2 1436 SER 1436 1436 ?    ?   ?   A . n 
B 2 1437 HIS 1437 1437 ?    ?   ?   A . n 
B 2 1438 ALA 1438 1438 ?    ?   ?   A . n 
B 2 1439 SER 1439 1439 ?    ?   ?   A . n 
B 2 1440 ARG 1440 1440 ?    ?   ?   A . n 
B 2 1441 SER 1441 1441 ?    ?   ?   A . n 
B 2 1442 ARG 1442 1442 ?    ?   ?   A . n 
B 2 1443 TRP 1443 1443 ?    ?   ?   A . n 
B 2 1444 PRO 1444 1444 ?    ?   ?   A . n 
B 2 1445 ARG 1445 1445 ?    ?   ?   A . n 
B 2 1446 PHE 1446 1446 ?    ?   ?   A . n 
B 2 1447 ASN 1447 1447 ?    ?   ?   A . n 
B 2 1448 ASN 1448 1448 ?    ?   ?   A . n 
B 2 1449 ASN 1449 1449 ?    ?   ?   A . n 
B 2 1450 SER 1450 1450 ?    ?   ?   A . n 
B 2 1451 SER 1451 1451 ?    ?   ?   A . n 
B 2 1452 SER 1452 1452 ?    ?   ?   A . n 
B 2 1453 SER 1453 1453 ?    ?   ?   A . n 
B 2 1454 HIS 1454 1454 ?    ?   ?   A . n 
B 2 1455 PRO 1455 1455 ?    ?   ?   A . n 
B 2 1456 PHE 1456 1456 ?    ?   ?   A . n 
B 2 1457 GLU 1457 1457 ?    ?   ?   A . n 
B 2 1458 THR 1458 1458 ?    ?   ?   A . n 
B 2 1459 LYS 1459 1459 ?    ?   ?   A . n 
B 2 1460 PRO 1460 1460 ?    ?   ?   A . n 
B 2 1461 PRO 1461 1461 ?    ?   ?   A . n 
B 2 1462 SER 1462 1462 ?    ?   ?   A . n 
B 2 1463 SER 1463 1463 ?    ?   ?   A . n 
B 2 1464 MET 1464 1464 ?    ?   ?   A . n 
B 2 1465 SER 1465 1465 ?    ?   ?   A . n 
B 2 1466 LYS 1466 1466 ?    ?   ?   A . n 
B 2 1467 LEU 1467 1467 ?    ?   ?   A . n 
B 2 1468 ARG 1468 1468 ?    ?   ?   A . n 
B 2 1469 SER 1469 1469 ?    ?   ?   A . n 
B 2 1470 ARG 1470 1470 ?    ?   ?   A . n 
B 2 1471 ALA 1471 1471 ?    ?   ?   A . n 
B 2 1472 GLY 1472 1472 ?    ?   ?   A . n 
B 2 1473 SER 1473 1473 ?    ?   ?   A . n 
B 2 1474 ILE 1474 1474 ?    ?   ?   A . n 
B 2 1475 LEU 1475 1475 ?    ?   ?   A . n 
B 2 1476 THR 1476 1476 ?    ?   ?   A . n 
B 2 1477 ARG 1477 1477 ?    ?   ?   A . n 
B 2 1478 LYS 1478 1478 ?    ?   ?   A . n 
B 2 1479 ARG 1479 1479 ?    ?   ?   A . n 
B 2 1480 ALA 1480 1480 ?    ?   ?   A . n 
B 2 1481 ASP 1481 1481 ?    ?   ?   A . n 
B 2 1482 THR 1482 1482 ?    ?   ?   A . n 
B 2 1483 THR 1483 1483 ?    ?   ?   A . n 
B 2 1484 ASP 1484 1484 ?    ?   ?   A . n 
B 2 1485 THR 1485 1485 ?    ?   ?   A . n 
B 2 1486 ARG 1486 1486 ?    ?   ?   A . n 
B 2 1487 ASN 1487 1487 ?    ?   ?   A . n 
B 2 1488 SER 1488 1488 ?    ?   ?   A . n 
B 2 1489 ASP 1489 1489 ?    ?   ?   A . n 
B 2 1490 ASP 1490 1490 ?    ?   ?   A . n 
B 2 1491 LYS 1491 1491 ?    ?   ?   A . n 
B 2 1492 SER 1492 1492 ?    ?   ?   A . n 
B 2 1493 LEU 1493 1493 ?    ?   ?   A . n 
B 2 1494 SER 1494 1494 ?    ?   ?   A . n 
B 2 1495 SER 1495 1495 ?    ?   ?   A . n 
B 2 1496 PRO 1496 1496 ?    ?   ?   A . n 
B 2 1497 VAL 1497 1497 ?    ?   ?   A . n 
B 2 1498 LYS 1498 1498 ?    ?   ?   A . n 
B 2 1499 THR 1499 1499 ?    ?   ?   A . n 
B 2 1500 GLY 1500 1500 ?    ?   ?   A . n 
B 2 1501 PHE 1501 1501 ?    ?   ?   A . n 
B 2 1502 PHE 1502 1502 ?    ?   ?   A . n 
B 2 1503 GLY 1503 1503 ?    ?   ?   A . n 
B 2 1504 ARG 1504 1504 ?    ?   ?   A . n 
B 2 1505 HIS 1505 1505 ?    ?   ?   A . n 
B 2 1506 MET 1506 1506 ?    ?   ?   A . n 
B 2 1507 PRO 1507 1507 ?    ?   ?   A . n 
B 2 1508 GLY 1508 1508 ?    ?   ?   A . n 
B 2 1509 GLN 1509 1509 ?    ?   ?   A . n 
B 2 1510 ASN 1510 1510 ?    ?   ?   A . n 
B 2 1511 HIS 1511 1511 ?    ?   ?   A . n 
B 2 1512 GLY 1512 1512 ?    ?   ?   A . n 
B 2 1513 GLN 1513 1513 ?    ?   ?   A . n 
B 2 1514 HIS 1514 1514 ?    ?   ?   A . n 
B 2 1515 GLU 1515 1515 ?    ?   ?   A . n 
B 2 1516 GLY 1516 1516 ?    ?   ?   A . n 
B 2 1517 ARG 1517 1517 ?    ?   ?   A . n 
B 2 1518 SER 1518 1518 ?    ?   ?   A . n 
B 2 1519 MET 1519 1519 ?    ?   ?   A . n 
B 2 1520 GLY 1520 1520 ?    ?   ?   A . n 
B 2 1521 THR 1521 1521 ?    ?   ?   A . n 
B 2 1522 PRO 1522 1522 ?    ?   ?   A . n 
B 2 1523 LEU 1523 1523 ?    ?   ?   A . n 
B 2 1524 LYS 1524 1524 ?    ?   ?   A . n 
B 2 1525 SER 1525 1525 ?    ?   ?   A . n 
B 2 1526 GLU 1526 1526 ?    ?   ?   A . n 
B 2 1527 THR 1527 1527 ?    ?   ?   A . n 
B 2 1528 GLY 1528 1528 ?    ?   ?   A . n 
B 2 1529 ARG 1529 1529 ?    ?   ?   A . n 
B 2 1530 GLY 1530 1530 ?    ?   ?   A . n 
B 2 1531 ASP 1531 1531 ?    ?   ?   A . n 
B 2 1532 ASN 1532 1532 ?    ?   ?   A . n 
B 2 1533 TRP 1533 1533 ?    ?   ?   A . n 
B 2 1534 GLU 1534 1534 ?    ?   ?   A . n 
B 2 1535 GLU 1535 1535 ?    ?   ?   A . n 
B 2 1536 GLU 1536 1536 ?    ?   ?   A . n 
B 2 1537 GLU 1537 1537 ?    ?   ?   A . n 
B 2 1538 LEU 1538 1538 ?    ?   ?   A . n 
B 2 1539 GLU 1539 1539 ?    ?   ?   A . n 
B 2 1540 ASP 1540 1540 ?    ?   ?   A . n 
B 2 1541 GLU 1541 1541 ?    ?   ?   A . n 
B 2 1542 SER 1542 1542 ?    ?   ?   A . n 
B 2 1543 LEU 1543 1543 ?    ?   ?   A . n 
B 2 1544 GLY 1544 1544 ?    ?   ?   A . n 
B 2 1545 ARG 1545 1545 ?    ?   ?   A . n 
B 2 1546 GLY 1546 1546 ?    ?   ?   A . n 
B 2 1547 PHE 1547 1547 ?    ?   ?   A . n 
B 2 1548 GLY 1548 1548 ?    ?   ?   A . n 
B 2 1549 VAL 1549 1549 ?    ?   ?   A . n 
B 2 1550 GLY 1550 1550 ?    ?   ?   A . n 
B 2 1551 GLN 1551 1551 ?    ?   ?   A . n 
B 2 1552 ASN 1552 1552 ?    ?   ?   A . n 
B 2 1553 MET 1553 1553 ?    ?   ?   A . n 
B 2 1554 ALA 1554 1554 ?    ?   ?   A . n 
B 2 1555 PRO 1555 1555 ?    ?   ?   A . n 
B 2 1556 PRO 1556 1556 ?    ?   ?   A . n 
B 2 1557 GLU 1557 1557 ?    ?   ?   A . n 
B 2 1558 ILE 1558 1558 ?    ?   ?   A . n 
B 2 1559 PRO 1559 1559 ?    ?   ?   A . n 
B 2 1560 ARG 1560 1560 ?    ?   ?   A . n 
B 2 1561 MET 1561 1561 ?    ?   ?   A . n 
B 2 1562 ASP 1562 1562 ?    ?   ?   A . n 
B 2 1563 TYR 1563 1563 ?    ?   ?   A . n 
B 2 1564 LYS 1564 1564 ?    ?   ?   A . n 
B 2 1565 ASP 1565 1565 ?    ?   ?   A . n 
B 2 1566 ASP 1566 1566 ?    ?   ?   A . n 
B 2 1567 ASP 1567 1567 ?    ?   ?   A . n 
B 2 1568 ASP 1568 1568 ?    ?   ?   A . n 
B 2 1569 LYS 1569 1569 ?    ?   ?   A . n 
B 2 1570 ILE 1570 1570 ?    ?   ?   A . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
C 3 NAG 1 D NAG 1 D NAG 1 n 
C 3 NAG 2 D NAG 2 D NAG 2 n 
D 4 NAG 1 E NAG 1 E NAG 1 n 
D 4 NAG 2 E NAG 2 E NAG 2 n 
D 4 BMA 3 E BMA 3 E BMA 3 n 
D 4 MAN 4 E MAN 4 E MAN 4 n 
D 4 MAN 5 E MAN 5 E MAN 5 n 
D 4 MAN 6 E MAN 6 E MAN 6 n 
E 3 NAG 1 G NAG 1 G NAG 1 n 
E 3 NAG 2 G NAG 2 G NAG 2 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BD6 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BD6 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
F 5 NAG   1 501  406  NAG   NAG B . 
G 6 BEF   1 1601 1433 BEF   BEF A . 
H 7 MG    1 1602 1434 MG    MG  A . 
I 8 A1BD6 1 1603 1432 A1BD6 WVC A . 
# 
_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                     9DZU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         9DZU 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DZU 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9DZU 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
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 
'ELECTRON MICROSCOPY' ? 0.003  ? 12056 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.484  ? 16393 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 11.965 ? 4349  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.042  ? 1867  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004  ? 2075  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9DZU 
_struct.title                        
'Cryo-EM structure of the C. neoformans lipid flippase Apt1-Cdc50 bound with butyrolactol A in the E2P state' 
_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        9DZU 
_struct_keywords.text            
'Cryptococcus neoformans, lipid flippase, P4-ATPase, Cdc50 protein, butyrolactol A, TRANSLOCASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   TRANSLOCASE/INHIBITOR 
# 
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 3 ? 
F N N 5 ? 
G N N 6 ? 
H N N 7 ? 
I N N 8 ? 
# 
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 J9VW44_CRYNH J9VW44 ? 1 
;MAIFNRKPKARLDGEPAPTEKEKVKWSKRPANTAFKQQRLKAWQPILTPKSVLPTLLIIGIIFAPIGALIVWGSGKVTTI
TLDYTECDVDAPTDGSYQAMPNSAYQYDLATSSSVSESSIASPTWTFSNDSSREVGETARCEIEFEVPYDLGPGLFLYYK
LTNYYQNHRRYSSSFDATQLIGDSRSLSQINGGNCKPITSRDGKPYYPCGLIANSLFNDTFPSVVLLNPTNGAQNQTYNF
SESGIAWGGIKKNYASTLTYISPSDVLPPPNWALKYPNGYVDGFPNLREDEHFQVWMRVAALPTFRKLWARNDGEIMSQG
RYRIVANMNYPVKQFSGTKSIVISTVSWIGGKQPFLGWAYIAAAILCVVLAVAGLIRHLVKPRKLGDMSLLSWNQPNANG
L
;
1 
2 UNP J9VZ19_CRYNH J9VZ19 ? 2 
;MGASKPPLVPRSKKHNPSWLDRNIVKPLESLAPSKLFARRRSPPVPRSVFINEPLPSEYYDKKGKILRAHHFATNQNVTS
KYTVITFIPKNLFEQFRRVANCFFLAISILQFFPKFSTISPGLVILPLIIVLAITALKDGYEDIKRHQADHRTNHAIVHV
LGGQDYTNQNPMASKDKTFIPAIPLPKRRSKKAKKAEEEAALNMQGRSSSTENFAAEPVPGAEPRGQDELQRMRSQVSNW
DEDPEAGDSPGELGWHRTIWEDVKVGDFVKIYENEQFPADIVICATSEEEDVAYIETKNLDGETNLKSRNGVPGLSHLNT
AEACAKAHLCIDLDAPESNMFRLNGAVINLEEYDEDEQHPIHPITLETTMLRGCVLKNTAWVIGIIVYTGEDTKIIRNAG
ATPSKRSKVEKQMNPQVIINLVILAAIAVVCAIVDHVNEVEWDRQQAYWMLFADTSGDNPNINGLVTFANAFITFQNIVP
ISLYISIEAVRTIQAAFIYWDRDIKYKKDGVTTRTTARSWNLSDDLGQIEYIFSDKTGTLTQNAMIFRQCSVGGKIYTGD
GLPPSHPTITHQHQPPPVHQHDDQDDPIAKSASESDDSDPKKISTEDPDEIKVTLPKEVLATFHDAELDKDLEAHDSEQS
RILHGFFAVLGLCHTVLAAETEPGVIEYKAQSPDEAALVQSAADVGFVFRGRDHNILRMSTPFSDVSDEYELLHVLEFNS
ARKRMSVILRKLDEDGRIFLLCKGADNVIFERLTKDSNQREMREKTDQDLQYFASEGLRTLCLAYRILDPQVYEQWAKEY
HNATVALQDREERIESVSSSIERDLILLGATAIEDKLQDGVPDTISDLKRAGIKVWVATGDKLETAVAIGYTTNLLTKDT
NLIVVREGRHSIGDQLREALEEFFGEDAGLRTTLSRIDSRRNSMDPPRLTRVNTGVRSLVGRDNGTRPGGFSLVIEGHAL
AHCFDDEETEALLLALSTRCNTVICCRVSPLQKAQIVHLIKDNLGVMCLAIGDGANDVSMIQAADVGVGISGEEGLQAVN
SSDYAIAQFRYLKRLLLVHGHWSYFRNSSMILNFFYKNIIGIGVLFWFMIYCGWSTTYVFAYVYLLFWNVFWTLVPVIAI
GLFDRNIDDETLMALPELYRASREGKYFGLMRFAYYIFEGVYQSAVIYFFLNYTYVTTTARGDGYDVYMYEMSTTQAIGA
VMVANLFSGLNIDAWTGWVWFAIWFGPFLIWVFTAVYSVIPPSSFYTGVYGNDVFLFRSAAYWFGWPFVTIIALLPRYLI
KTFRQNIFPNDVDTMRLVRKYHPEVDLYNHPMLGGKLAPKKDEDESDYGEEPFDGPEGRRSSIKMANLRHSHGAFGRGDQ
AGDMELGMGRKSLGNRPGLRSSMDSSRFGIHSGARGSTVDMSTGLEQPPSRGFGFTMEEGGVAIQRMQSRLSQTSSHASR
SRWPRFNNNSSSSHPFETKPPSSMSKLRSRAGSILTRKRADTTDTRNSDDKSLSSPVKTGFFGRHMPGQNHGQHEGRSMG
TPLKSETGRGDNWEEEELEDESLGRGFGVGQNMAPPEIPRM
;
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 9DZU B 1 ? 401  ? J9VW44 1 ? 401  ? 1 401  
2 2 9DZU A 1 ? 1561 ? J9VZ19 1 ? 1561 ? 1 1561 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9DZU HIS B 402  ? UNP J9VW44 ? ? 'expression tag' 402  1  
1 9DZU HIS B 403  ? UNP J9VW44 ? ? 'expression tag' 403  2  
1 9DZU HIS B 404  ? UNP J9VW44 ? ? 'expression tag' 404  3  
1 9DZU HIS B 405  ? UNP J9VW44 ? ? 'expression tag' 405  4  
1 9DZU HIS B 406  ? UNP J9VW44 ? ? 'expression tag' 406  5  
1 9DZU HIS B 407  ? UNP J9VW44 ? ? 'expression tag' 407  6  
1 9DZU HIS B 408  ? UNP J9VW44 ? ? 'expression tag' 408  7  
1 9DZU HIS B 409  ? UNP J9VW44 ? ? 'expression tag' 409  8  
1 9DZU HIS B 410  ? UNP J9VW44 ? ? 'expression tag' 410  9  
1 9DZU HIS B 411  ? UNP J9VW44 ? ? 'expression tag' 411  10 
2 9DZU ASP A 1562 ? UNP J9VZ19 ? ? 'expression tag' 1562 11 
2 9DZU TYR A 1563 ? UNP J9VZ19 ? ? 'expression tag' 1563 12 
2 9DZU LYS A 1564 ? UNP J9VZ19 ? ? 'expression tag' 1564 13 
2 9DZU ASP A 1565 ? UNP J9VZ19 ? ? 'expression tag' 1565 14 
2 9DZU ASP A 1566 ? UNP J9VZ19 ? ? 'expression tag' 1566 15 
2 9DZU ASP A 1567 ? UNP J9VZ19 ? ? 'expression tag' 1567 16 
2 9DZU ASP A 1568 ? UNP J9VZ19 ? ? 'expression tag' 1568 17 
2 9DZU LYS A 1569 ? UNP J9VZ19 ? ? 'expression tag' 1569 18 
2 9DZU ILE A 1570 ? UNP J9VZ19 ? ? 'expression tag' 1570 19 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_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   ? 
_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 THR A 48   ? SER A 51   ? THR B 48   SER B 51   5 ? 4  
HELX_P HELX_P2  AA2 VAL A 52   ? LYS A 76   ? VAL B 52   LYS B 76   1 ? 25 
HELX_P HELX_P3  AA3 GLU A 86   ? ALA A 91   ? GLU B 86   ALA B 91   1 ? 6  
HELX_P HELX_P4  AA4 PRO A 101  ? SER A 103  ? PRO B 101  SER B 103  5 ? 3  
HELX_P HELX_P5  AA5 HIS A 168  ? SER A 173  ? HIS B 168  SER B 173  1 ? 6  
HELX_P HELX_P6  AA6 ASP A 176  ? ILE A 181  ? ASP B 176  ILE B 181  1 ? 6  
HELX_P HELX_P7  AA7 SER A 186  ? GLY A 192  ? SER B 186  GLY B 192  1 ? 7  
HELX_P HELX_P8  AA8 GLY A 210  ? SER A 215  ? GLY B 210  SER B 215  1 ? 6  
HELX_P HELX_P9  AA9 GLY A 249  ? TYR A 254  ? GLY B 249  TYR B 254  5 ? 6  
HELX_P HELX_P10 AB1 SER A 262  ? VAL A 266  ? SER B 262  VAL B 266  5 ? 5  
HELX_P HELX_P11 AB2 PRO A 269  ? ALA A 273  ? PRO B 269  ALA B 273  5 ? 5  
HELX_P HELX_P12 AB3 ASP A 290  ? ARG A 298  ? ASP B 290  ARG B 298  1 ? 9  
HELX_P HELX_P13 AB4 VAL A 332  ? SER A 336  ? VAL B 332  SER B 336  5 ? 5  
HELX_P HELX_P14 AB5 PRO A 354  ? LYS A 381  ? PRO B 354  LYS B 381  1 ? 28 
HELX_P HELX_P15 AB6 PHE B 87   ? ARG B 97   ? PHE A 87   ARG A 97   1 ? 11 
HELX_P HELX_P16 AB7 VAL B 99   ? PHE B 113  ? VAL A 99   PHE A 113  1 ? 15 
HELX_P HELX_P17 AB8 PRO B 114  ? SER B 117  ? PRO A 114  SER A 117  5 ? 4  
HELX_P HELX_P18 AB9 SER B 120  ? ASN B 154  ? SER A 120  ASN A 154  1 ? 35 
HELX_P HELX_P19 AC1 ASN B 319  ? LYS B 326  ? ASN A 319  LYS A 326  1 ? 8  
HELX_P HELX_P20 AC2 THR B 389  ? ASP B 392  ? THR A 389  ASP A 392  5 ? 4  
HELX_P HELX_P21 AC3 THR B 393  ? ALA B 399  ? THR A 393  ALA A 399  1 ? 7  
HELX_P HELX_P22 AC4 SER B 407  ? GLN B 445  ? SER A 407  GLN A 445  1 ? 39 
HELX_P HELX_P23 AC5 ASN B 461  ? PHE B 475  ? ASN A 461  PHE A 475  1 ? 15 
HELX_P HELX_P24 AC6 GLN B 476  ? VAL B 479  ? GLN A 476  VAL A 479  5 ? 4  
HELX_P HELX_P25 AC7 ILE B 481  ? ASP B 501  ? ILE A 481  ASP A 501  1 ? 21 
HELX_P HELX_P26 AC8 ARG B 502  ? LYS B 505  ? ARG A 502  LYS A 505  5 ? 4  
HELX_P HELX_P27 AC9 SER B 523  ? ILE B 529  ? SER A 523  ILE A 529  5 ? 7  
HELX_P HELX_P28 AD1 ASP B 629  ? GLU B 633  ? ASP A 629  GLU A 633  1 ? 5  
HELX_P HELX_P29 AD2 SER B 637  ? CYS B 653  ? SER A 637  CYS A 653  1 ? 17 
HELX_P HELX_P30 AD3 SER B 672  ? VAL B 685  ? SER A 672  VAL A 685  1 ? 14 
HELX_P HELX_P31 AD4 ALA B 745  ? ARG B 752  ? ALA A 745  ARG A 752  1 ? 8  
HELX_P HELX_P32 AD5 SER B 757  ? GLY B 777  ? SER A 757  GLY A 777  1 ? 21 
HELX_P HELX_P33 AD6 ASP B 789  ? VAL B 805  ? ASP A 789  VAL A 805  1 ? 17 
HELX_P HELX_P34 AD7 ASP B 809  ? GLU B 822  ? ASP A 809  GLU A 822  1 ? 14 
HELX_P HELX_P35 AD8 GLY B 840  ? ALA B 851  ? GLY A 840  ALA A 851  1 ? 12 
HELX_P HELX_P36 AD9 LYS B 862  ? THR B 873  ? LYS A 862  THR A 873  1 ? 12 
HELX_P HELX_P37 AE1 SER B 891  ? PHE B 904  ? SER A 891  PHE A 904  1 ? 14 
HELX_P HELX_P38 AE2 GLY B 909  ? LEU B 914  ? GLY A 909  LEU A 914  1 ? 6  
HELX_P HELX_P39 AE3 GLY B 957  ? ASP B 966  ? GLY A 957  ASP A 966  1 ? 10 
HELX_P HELX_P40 AE4 GLU B 967  ? CYS B 980  ? GLU A 967  CYS A 980  1 ? 14 
HELX_P HELX_P41 AE5 SER B 989  ? LEU B 1004 ? SER A 989  LEU A 1004 1 ? 16 
HELX_P HELX_P42 AE6 GLY B 1014 ? ALA B 1023 ? GLY A 1014 ALA A 1023 1 ? 10 
HELX_P HELX_P43 AE7 LEU B 1036 ? SER B 1041 ? LEU A 1036 SER A 1041 1 ? 6  
HELX_P HELX_P44 AE8 GLN B 1048 ? CYS B 1092 ? GLN A 1048 CYS A 1092 1 ? 45 
HELX_P HELX_P45 AE9 ALA B 1101 ? PHE B 1107 ? ALA A 1101 PHE A 1107 1 ? 7  
HELX_P HELX_P46 AF1 LEU B 1114 ? ASP B 1124 ? LEU A 1114 ASP A 1124 1 ? 11 
HELX_P HELX_P47 AF2 ASP B 1128 ? LEU B 1135 ? ASP A 1128 LEU A 1135 1 ? 8  
HELX_P HELX_P48 AF3 PRO B 1136 ? LEU B 1138 ? PRO A 1136 LEU A 1138 5 ? 3  
HELX_P HELX_P49 AF4 TYR B 1139 ? GLU B 1144 ? TYR A 1139 GLU A 1144 1 ? 6  
HELX_P HELX_P50 AF5 GLY B 1149 ? VAL B 1176 ? GLY A 1149 VAL A 1176 1 ? 28 
HELX_P HELX_P51 AF6 TYR B 1188 ? ASN B 1211 ? TYR A 1188 ASN A 1211 1 ? 24 
HELX_P HELX_P52 AF7 THR B 1216 ? SER B 1238 ? THR A 1216 SER A 1238 1 ? 23 
HELX_P HELX_P53 AF8 GLY B 1251 ? LEU B 1256 ? GLY A 1251 LEU A 1256 1 ? 6  
HELX_P HELX_P54 AF9 SER B 1259 ? PHE B 1288 ? SER A 1259 PHE A 1288 1 ? 30 
HELX_P HELX_P55 AG1 ASN B 1290 ? HIS B 1302 ? ASN A 1290 HIS A 1302 1 ? 13 
HELX_P HELX_P56 AG2 GLY B 1421 ? LEU B 1431 ? GLY A 1421 LEU A 1431 1 ? 11 
# 
_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 
disulf1  disulf ?    ? A CYS 87   SG  ? ? ? 1_555 A CYS 141 SG ? ? B CYS 87   B CYS 141  1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf2  disulf ?    ? A CYS 195  SG  ? ? ? 1_555 A CYS 209 SG ? ? B CYS 195  B CYS 209  1_555 ? ? ? ? ? ? ? 2.032 ? ? 
covale1  covale one  ? A ASN 129  ND2 ? ? ? 1_555 C NAG .   C1 ? ? B ASN 129  D NAG 1    1_555 ? ? ? ? ? ? ? 1.438 ? 
N-Glycosylation 
covale2  covale one  ? A ASN 218  ND2 ? ? ? 1_555 D NAG .   C1 ? ? B ASN 218  E NAG 1    1_555 ? ? ? ? ? ? ? 1.436 ? 
N-Glycosylation 
covale3  covale one  ? A ASN 235  ND2 ? ? ? 1_555 F NAG .   C1 ? ? B ASN 235  B NAG 501  1_555 ? ? ? ? ? ? ? 1.440 ? 
N-Glycosylation 
covale4  covale one  ? A ASN 239  ND2 ? ? ? 1_555 E NAG .   C1 ? ? B ASN 239  G NAG 1    1_555 ? ? ? ? ? ? ? 1.441 ? 
N-Glycosylation 
covale5  covale both ? C NAG .    O4  ? ? ? 1_555 C NAG .   C1 ? ? D NAG 1    D NAG 2    1_555 ? ? ? ? ? ? ? 1.444 ? ? 
covale6  covale both ? D NAG .    O4  ? ? ? 1_555 D NAG .   C1 ? ? E NAG 1    E NAG 2    1_555 ? ? ? ? ? ? ? 1.448 ? ? 
covale7  covale both ? D NAG .    O4  ? ? ? 1_555 D BMA .   C1 ? ? E NAG 2    E BMA 3    1_555 ? ? ? ? ? ? ? 1.447 ? ? 
covale8  covale both ? D BMA .    O6  ? ? ? 1_555 D MAN .   C1 ? ? E BMA 3    E MAN 4    1_555 ? ? ? ? ? ? ? 1.444 ? ? 
covale9  covale both ? D BMA .    O3  ? ? ? 1_555 D MAN .   C1 ? ? E BMA 3    E MAN 6    1_555 ? ? ? ? ? ? ? 1.443 ? ? 
covale10 covale both ? D MAN .    O4  ? ? ? 1_555 D MAN .   C1 ? ? E MAN 4    E MAN 5    1_555 ? ? ? ? ? ? ? 1.455 ? ? 
covale11 covale both ? E NAG .    O4  ? ? ? 1_555 E NAG .   C1 ? ? G NAG 1    G NAG 2    1_555 ? ? ? ? ? ? ? 1.440 ? ? 
metalc1  metalc ?    ? B ASP 535  OD1 ? ? ? 1_555 G BEF .   BE ? ? A ASP 535  A BEF 1601 1_555 ? ? ? ? ? ? ? 1.571 ? ? 
metalc2  metalc ?    ? B ASP 535  OD2 ? ? ? 1_555 H MG  .   MG ? ? A ASP 535  A MG  1602 1_555 ? ? ? ? ? ? ? 2.091 ? ? 
metalc3  metalc ?    ? B THR 537  O   ? ? ? 1_555 H MG  .   MG ? ? A THR 537  A MG  1602 1_555 ? ? ? ? ? ? ? 2.086 ? ? 
metalc4  metalc ?    ? B ASP 1013 OD1 ? ? ? 1_555 H MG  .   MG ? ? A ASP 1013 A MG  1602 1_555 ? ? ? ? ? ? ? 2.146 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
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 OD1 ? B ASP 535 ? A ASP 535  ? 1_555 BE ? G BEF . ? A BEF 1601 ? 1_555 F1  ? G BEF .    ? A BEF 1601 ? 1_555 111.1 ? 
2 OD1 ? B ASP 535 ? A ASP 535  ? 1_555 BE ? G BEF . ? A BEF 1601 ? 1_555 F2  ? G BEF .    ? A BEF 1601 ? 1_555 109.8 ? 
3 F1  ? G BEF .   ? A BEF 1601 ? 1_555 BE ? G BEF . ? A BEF 1601 ? 1_555 F2  ? G BEF .    ? A BEF 1601 ? 1_555 112.3 ? 
4 OD1 ? B ASP 535 ? A ASP 535  ? 1_555 BE ? G BEF . ? A BEF 1601 ? 1_555 F3  ? G BEF .    ? A BEF 1601 ? 1_555 106.1 ? 
5 F1  ? G BEF .   ? A BEF 1601 ? 1_555 BE ? G BEF . ? A BEF 1601 ? 1_555 F3  ? G BEF .    ? A BEF 1601 ? 1_555 109.8 ? 
6 F2  ? G BEF .   ? A BEF 1601 ? 1_555 BE ? G BEF . ? A BEF 1601 ? 1_555 F3  ? G BEF .    ? A BEF 1601 ? 1_555 107.4 ? 
7 OD2 ? B ASP 535 ? A ASP 535  ? 1_555 MG ? H MG  . ? A MG  1602 ? 1_555 O   ? B THR 537  ? A THR 537  ? 1_555 75.7  ? 
8 OD2 ? B ASP 535 ? A ASP 535  ? 1_555 MG ? H MG  . ? A MG  1602 ? 1_555 OD1 ? B ASP 1013 ? A ASP 1013 ? 1_555 124.2 ? 
9 O   ? B THR 537 ? A THR 537  ? 1_555 MG ? H MG  . ? A MG  1602 ? 1_555 OD1 ? B ASP 1013 ? A ASP 1013 ? 1_555 101.9 ? 
# 
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 NAG C .   ? ASN A 129 ? NAG D 1   ? 1_555 ASN B 129 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG D .   ? ASN A 218 ? NAG E 1   ? 1_555 ASN B 218 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 NAG E .   ? ASN A 239 ? NAG G 1   ? 1_555 ASN B 239 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4 NAG F .   ? ASN A 235 ? NAG B 501 ? 1_555 ASN B 235 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5 CYS A 87  ? CYS A 141 ? CYS B 87  ? 1_555 CYS B 141 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
6 CYS A 195 ? CYS A 209 ? CYS B 195 ? 1_555 CYS B 209 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LYS 196 A . ? LYS 196 B PRO 197 A ? PRO 197 B 1 1.30  
2 TYR 207 A . ? TYR 207 B PRO 208 A ? PRO 208 B 1 -4.92 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 6 ? 
AA3 ? 2 ? 
AA4 ? 6 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 9 ? 
AA8 ? 7 ? 
AA9 ? 6 ? 
AB1 ? 2 ? 
AB2 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? parallel      
AA7 6 7 ? parallel      
AA7 7 8 ? parallel      
AA7 8 9 ? parallel      
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA8 6 7 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 5 6 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? 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 TYR A 105  ? ASP A 108  ? TYR B 105  ASP B 108  
AA1 2 THR A 79   ? ASP A 83   ? THR B 79   ASP B 83   
AA1 3 THR A 338  ? SER A 344  ? THR B 338  SER B 344  
AA1 4 LEU A 155  ? THR A 162  ? LEU B 155  THR B 162  
AA1 5 PHE A 305  ? ASN A 312  ? PHE B 305  ASN B 312  
AA2 1 GLN A 98   ? ALA A 99   ? GLN B 98   ALA B 99   
AA2 2 THR A 124  ? ASN A 129  ? THR B 124  ASN B 129  
AA2 3 ALA A 139  ? VAL A 147  ? ALA B 139  VAL B 147  
AA2 4 GLY A 320  ? ASN A 327  ? GLY B 320  ASN B 327  
AA2 5 VAL A 224  ? LEU A 226  ? VAL B 224  LEU B 226  
AA2 6 GLN A 236  ? TYR A 238  ? GLN B 236  TYR B 238  
AA3 1 SER A 200  ? ARG A 201  ? SER B 200  ARG B 201  
AA3 2 LYS A 204  ? PRO A 205  ? LYS B 204  PRO B 205  
AA4 1 GLY B 254  ? THR B 258  ? GLY A 254  THR A 258  
AA4 2 VAL B 158  ? GLY B 162  ? VAL A 158  GLY A 162  
AA4 3 GLY B 266  ? LYS B 270  ? GLY A 266  LYS A 270  
AA4 4 VAL B 382  ? VAL B 387  ? VAL A 382  VAL A 387  
AA4 5 ASP B 280  ? THR B 286  ? ASP A 280  THR A 286  
AA4 6 THR B 369  ? MET B 370  ? THR A 369  MET A 370  
AA5 1 ALA B 293  ? TYR B 294  ? ALA A 293  TYR A 294  
AA5 2 LEU B 306  ? LYS B 307  ? LEU A 306  LYS A 307  
AA6 1 TYR B 506  ? LYS B 508  ? TYR A 506  LYS A 508  
AA6 2 VAL B 511  ? THR B 513  ? VAL A 511  THR A 513  
AA7 1 THR B 516  ? ALA B 517  ? THR A 516  ALA A 517  
AA7 2 TYR B 1044 ? ILE B 1046 ? TYR A 1044 ILE A 1046 
AA7 3 VAL B 1026 ? ILE B 1030 ? VAL A 1026 ILE A 1030 
AA7 4 CYS B 1008 ? GLY B 1012 ? CYS A 1008 GLY A 1012 
AA7 5 TYR B 531  ? SER B 534  ? TYR A 531  SER A 534  
AA7 6 LYS B 854  ? THR B 859  ? LYS A 854  THR A 859  
AA7 7 VAL B 983  ? CYS B 986  ? VAL A 983  CYS A 986  
AA7 8 PHE B 951  ? GLU B 956  ? PHE A 951  GLU A 956  
AA7 9 ASN B 881  ? VAL B 885  ? ASN A 881  VAL A 885  
AA8 1 LYS B 555  ? TYR B 557  ? LYS A 555  TYR A 557  
AA8 2 THR B 541  ? VAL B 552  ? THR A 541  VAL A 552  
AA8 3 ILE B 826  ? LEU B 837  ? ILE A 826  LEU A 837  
AA8 4 CYS B 782  ? TYR B 785  ? CYS A 782  TYR A 785  
AA8 5 ILE B 738  ? GLY B 744  ? ILE A 738  GLY A 744  
AA8 6 ARG B 724  ? LEU B 729  ? ARG A 724  LEU A 729  
AA8 7 TYR B 710  ? HIS B 714  ? TYR A 710  HIS A 714  
AA9 1 LYS B 555  ? TYR B 557  ? LYS A 555  TYR A 557  
AA9 2 THR B 541  ? VAL B 552  ? THR A 541  VAL A 552  
AA9 3 ILE B 826  ? LEU B 837  ? ILE A 826  LEU A 837  
AA9 4 CYS B 782  ? TYR B 785  ? CYS A 782  TYR A 785  
AA9 5 ILE B 738  ? GLY B 744  ? ILE A 738  GLY A 744  
AA9 6 ILE B 787  ? LEU B 788  ? ILE A 787  LEU A 788  
AB1 1 VAL B 656  ? ALA B 659  ? VAL A 656  ALA A 659  
AB1 2 GLU B 667  ? ALA B 670  ? GLU A 667  ALA A 670  
AB2 1 VAL B 688  ? GLY B 691  ? VAL A 688  GLY A 691  
AB2 2 ARG B 698  ? SER B 700  ? ARG A 698  SER A 700  
AB2 3 VAL B 706  ? SER B 707  ? VAL A 706  SER A 707  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ASP A 108  ? O ASP B 108  N THR A 79   ? N THR B 79   
AA1 2 3 N ILE A 80   ? N ILE B 80   O ILE A 343  ? O ILE B 343  
AA1 3 4 O VAL A 342  ? O VAL B 342  N TYR A 158  ? N TYR B 158  
AA1 4 5 N LEU A 157  ? N LEU B 157  O TRP A 309  ? O TRP B 309  
AA2 1 2 N GLN A 98   ? N GLN B 98   O TRP A 125  ? O TRP B 125  
AA2 2 3 N THR A 124  ? N THR B 124  O GLU A 144  ? O GLU B 144  
AA2 3 4 N PHE A 145  ? N PHE B 145  O TYR A 322  ? O TYR B 322  
AA2 4 5 O ARG A 323  ? O ARG B 323  N VAL A 225  ? N VAL B 225  
AA2 5 6 N LEU A 226  ? N LEU B 226  O GLN A 236  ? O GLN B 236  
AA3 1 2 N ARG A 201  ? N ARG B 201  O LYS A 204  ? O LYS B 204  
AA4 1 2 O HIS B 256  ? O HIS A 256  N VAL B 160  ? N VAL A 160  
AA4 2 3 N HIS B 159  ? N HIS A 159  O LYS B 270  ? O LYS A 270  
AA4 3 4 N GLY B 266  ? N GLY A 266  O ILE B 386  ? O ILE A 386  
AA4 4 5 O VAL B 387  ? O VAL A 387  N ASP B 280  ? N ASP A 280  
AA4 5 6 N ILE B 281  ? N ILE A 281  O MET B 370  ? O MET A 370  
AA5 1 2 N ALA B 293  ? N ALA A 293  O LYS B 307  ? O LYS A 307  
AA6 1 2 N TYR B 506  ? N TYR A 506  O THR B 513  ? O THR A 513  
AA7 1 2 N THR B 516  ? N THR A 516  O ALA B 1045 ? O ALA A 1045 
AA7 2 3 O TYR B 1044 ? O TYR A 1044 N GLY B 1029 ? N GLY A 1029 
AA7 3 4 O VAL B 1028 ? O VAL A 1028 N ALA B 1010 ? N ALA A 1010 
AA7 4 5 O LEU B 1009 ? O LEU A 1009 N PHE B 533  ? N PHE A 533  
AA7 5 6 N ILE B 532  ? N ILE A 532  O TRP B 856  ? O TRP A 856  
AA7 6 7 N VAL B 857  ? N VAL A 857  O CYS B 985  ? O CYS A 985  
AA7 7 8 O ILE B 984  ? O ILE A 984  N LEU B 953  ? N LEU A 953  
AA7 8 9 O VAL B 954  ? O VAL A 954  N VAL B 885  ? N VAL A 885  
AA8 1 2 O LYS B 555  ? O LYS A 555  N VAL B 552  ? N VAL A 552  
AA8 2 3 N SER B 551  ? N SER A 551  O ALA B 830  ? O ALA A 830  
AA8 3 4 O ILE B 826  ? O ILE A 826  N TYR B 785  ? N TYR A 785  
AA8 4 5 O CYS B 782  ? O CYS A 782  N GLY B 744  ? N GLY A 744  
AA8 5 6 O LYS B 743  ? O LYS A 743  N MET B 725  ? N MET A 725  
AA8 6 7 O SER B 726  ? O SER A 726  N HIS B 714  ? N HIS A 714  
AA9 1 2 O LYS B 555  ? O LYS A 555  N VAL B 552  ? N VAL A 552  
AA9 2 3 N SER B 551  ? N SER A 551  O ALA B 830  ? O ALA A 830  
AA9 3 4 O ILE B 826  ? O ILE A 826  N TYR B 785  ? N TYR A 785  
AA9 4 5 O CYS B 782  ? O CYS A 782  N GLY B 744  ? N GLY A 744  
AA9 5 6 N ILE B 738  ? N ILE A 738  O LEU B 788  ? O LEU A 788  
AB1 1 2 N ALA B 659  ? N ALA A 659  O GLU B 667  ? O GLU A 667  
AB2 1 2 N VAL B 688  ? N VAL A 688  O SER B 700  ? O SER A 700  
AB2 2 3 N MET B 699  ? N MET A 699  O VAL B 706  ? O VAL A 706  
# 
_pdbx_entry_details.entry_id                   9DZU 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER B 215  ? ? -98.77  34.70   
2  1 ALA B 233  ? ? 64.32   159.65  
3  1 ALA B 310  ? ? 68.95   149.28  
4  1 SER B 347  ? ? -117.48 -168.32 
5  1 ASN B 394  ? ? -92.14  51.23   
6  1 ALA A 73   ? ? -151.68 13.70   
7  1 THR A 74   ? ? 56.73   -133.31 
8  1 ASN A 75   ? ? -162.40 -165.50 
9  1 GLN A 76   ? ? 72.06   140.95  
10 1 VAL A 99   ? ? 63.67   -53.12  
11 1 SER A 120  ? ? -174.21 148.55  
12 1 THR A 258  ? ? -127.85 -169.84 
13 1 ASP A 267  ? ? 58.13   -175.09 
14 1 TYR A 272  ? ? 58.83   -141.08 
15 1 GLU A 288  ? ? -93.95  -66.21  
16 1 GLU A 289  ? ? -176.50 144.51  
17 1 GLU A 290  ? ? 52.39   18.73   
18 1 GLU A 296  ? ? -128.81 -168.00 
19 1 THR A 297  ? ? -78.15  -152.02 
20 1 LYS A 298  ? ? 76.55   -4.43   
21 1 LEU A 300  ? ? 71.34   172.56  
22 1 ASP A 301  ? ? 62.53   175.71  
23 1 ARG A 309  ? ? 179.98  175.37  
24 1 LEU A 315  ? ? 59.04   -167.75 
25 1 HIS A 317  ? ? -140.34 33.36   
26 1 LEU A 329  ? ? -156.95 -157.53 
27 1 CYS A 330  ? ? 74.45   45.91   
28 1 ILE A 348  ? ? 69.51   -52.06  
29 1 ASN A 349  ? ? 71.67   140.93  
30 1 VAL A 375  ? ? -136.13 -59.00  
31 1 ALA A 380  ? ? -77.22  -163.97 
32 1 ASN A 461  ? ? 68.13   -66.51  
33 1 PHE A 475  ? ? -97.41  34.00   
34 1 GLU A 660  ? ? -99.58  33.92   
35 1 PRO A 702  ? ? -75.41  39.91   
36 1 SER A 704  ? ? -171.10 -169.34 
37 1 ARG A 752  ? ? -98.81  37.27   
38 1 ASP A 756  ? ? -95.50  -67.35  
39 1 SER A 757  ? ? -136.40 -42.09  
40 1 ARG A 786  ? ? -171.17 141.85  
41 1 LEU A 807  ? ? 57.40   -95.85  
42 1 ARG A 889  ? ? 55.93   -101.71 
43 1 ASN A 944  ? ? 72.65   140.95  
44 1 ASP A 1013 ? ? -141.07 48.87   
45 1 LEU A 1114 ? ? -130.43 -38.77  
46 1 ALA A 1180 ? ? 67.60   -0.29   
47 1 THR A 1247 ? ? 71.30   -14.66  
48 1 PHE A 1288 ? ? -117.65 72.45   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9DZU 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9DZU 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.72 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               639772 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.4 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Apt1-Cdc50 heterodimer bound with butyrolactol A' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1,2 
# 
_em_imaging.entry_id                        9DZU 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1300 
_em_imaging.nominal_defocus_max             1700 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              9DZU 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9DZU 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 B MET 1    ? A MET 1    
2   1 Y 1 B ALA 2    ? A ALA 2    
3   1 Y 1 B ILE 3    ? A ILE 3    
4   1 Y 1 B PHE 4    ? A PHE 4    
5   1 Y 1 B ASN 5    ? A ASN 5    
6   1 Y 1 B ARG 6    ? A ARG 6    
7   1 Y 1 B LYS 7    ? A LYS 7    
8   1 Y 1 B PRO 8    ? A PRO 8    
9   1 Y 1 B LYS 9    ? A LYS 9    
10  1 Y 1 B ALA 10   ? A ALA 10   
11  1 Y 1 B ARG 11   ? A ARG 11   
12  1 Y 1 B LEU 12   ? A LEU 12   
13  1 Y 1 B ASP 13   ? A ASP 13   
14  1 Y 1 B GLY 14   ? A GLY 14   
15  1 Y 1 B GLU 15   ? A GLU 15   
16  1 Y 1 B PRO 16   ? A PRO 16   
17  1 Y 1 B ALA 17   ? A ALA 17   
18  1 Y 1 B PRO 18   ? A PRO 18   
19  1 Y 1 B THR 19   ? A THR 19   
20  1 Y 1 B GLU 20   ? A GLU 20   
21  1 Y 1 B LYS 21   ? A LYS 21   
22  1 Y 1 B GLU 22   ? A GLU 22   
23  1 Y 1 B LYS 23   ? A LYS 23   
24  1 Y 1 B VAL 24   ? A VAL 24   
25  1 Y 1 B LYS 25   ? A LYS 25   
26  1 Y 1 B TRP 26   ? A TRP 26   
27  1 Y 1 B SER 27   ? A SER 27   
28  1 Y 1 B LYS 28   ? A LYS 28   
29  1 Y 1 B ARG 29   ? A ARG 29   
30  1 Y 1 B PRO 30   ? A PRO 30   
31  1 Y 1 B ALA 31   ? A ALA 31   
32  1 Y 1 B ASN 32   ? A ASN 32   
33  1 Y 1 B THR 33   ? A THR 33   
34  1 Y 1 B ALA 34   ? A ALA 34   
35  1 Y 1 B PHE 35   ? A PHE 35   
36  1 Y 1 B LYS 36   ? A LYS 36   
37  1 Y 1 B GLN 37   ? A GLN 37   
38  1 Y 1 B GLN 38   ? A GLN 38   
39  1 Y 1 B ARG 39   ? A ARG 39   
40  1 Y 1 B LEU 40   ? A LEU 40   
41  1 Y 1 B LYS 41   ? A LYS 41   
42  1 Y 1 B ALA 42   ? A ALA 42   
43  1 Y 1 B TRP 43   ? A TRP 43   
44  1 Y 1 B GLN 44   ? A GLN 44   
45  1 Y 1 B PRO 45   ? A PRO 45   
46  1 Y 1 B ILE 46   ? A ILE 46   
47  1 Y 1 B LEU 47   ? A LEU 47   
48  1 Y 1 B ALA 398  ? A ALA 398  
49  1 Y 1 B ASN 399  ? A ASN 399  
50  1 Y 1 B GLY 400  ? A GLY 400  
51  1 Y 1 B LEU 401  ? A LEU 401  
52  1 Y 1 B HIS 402  ? A HIS 402  
53  1 Y 1 B HIS 403  ? A HIS 403  
54  1 Y 1 B HIS 404  ? A HIS 404  
55  1 Y 1 B HIS 405  ? A HIS 405  
56  1 Y 1 B HIS 406  ? A HIS 406  
57  1 Y 1 B HIS 407  ? A HIS 407  
58  1 Y 1 B HIS 408  ? A HIS 408  
59  1 Y 1 B HIS 409  ? A HIS 409  
60  1 Y 1 B HIS 410  ? A HIS 410  
61  1 Y 1 B HIS 411  ? A HIS 411  
62  1 Y 1 A MET 1    ? B MET 1    
63  1 Y 1 A GLY 2    ? B GLY 2    
64  1 Y 1 A ALA 3    ? B ALA 3    
65  1 Y 1 A SER 4    ? B SER 4    
66  1 Y 1 A LYS 5    ? B LYS 5    
67  1 Y 1 A PRO 6    ? B PRO 6    
68  1 Y 1 A PRO 7    ? B PRO 7    
69  1 Y 1 A LEU 8    ? B LEU 8    
70  1 Y 1 A VAL 9    ? B VAL 9    
71  1 Y 1 A PRO 10   ? B PRO 10   
72  1 Y 1 A ARG 11   ? B ARG 11   
73  1 Y 1 A SER 12   ? B SER 12   
74  1 Y 1 A LYS 13   ? B LYS 13   
75  1 Y 1 A LYS 14   ? B LYS 14   
76  1 Y 1 A HIS 15   ? B HIS 15   
77  1 Y 1 A ASN 16   ? B ASN 16   
78  1 Y 1 A PRO 17   ? B PRO 17   
79  1 Y 1 A SER 18   ? B SER 18   
80  1 Y 1 A TRP 19   ? B TRP 19   
81  1 Y 1 A LEU 20   ? B LEU 20   
82  1 Y 1 A ASP 21   ? B ASP 21   
83  1 Y 1 A ARG 22   ? B ARG 22   
84  1 Y 1 A ASN 23   ? B ASN 23   
85  1 Y 1 A ILE 24   ? B ILE 24   
86  1 Y 1 A VAL 25   ? B VAL 25   
87  1 Y 1 A LYS 26   ? B LYS 26   
88  1 Y 1 A PRO 27   ? B PRO 27   
89  1 Y 1 A LEU 28   ? B LEU 28   
90  1 Y 1 A GLU 29   ? B GLU 29   
91  1 Y 1 A SER 30   ? B SER 30   
92  1 Y 1 A LEU 31   ? B LEU 31   
93  1 Y 1 A ALA 32   ? B ALA 32   
94  1 Y 1 A PRO 33   ? B PRO 33   
95  1 Y 1 A SER 34   ? B SER 34   
96  1 Y 1 A LYS 35   ? B LYS 35   
97  1 Y 1 A LEU 36   ? B LEU 36   
98  1 Y 1 A PHE 37   ? B PHE 37   
99  1 Y 1 A ALA 38   ? B ALA 38   
100 1 Y 1 A ARG 39   ? B ARG 39   
101 1 Y 1 A ARG 40   ? B ARG 40   
102 1 Y 1 A ARG 41   ? B ARG 41   
103 1 Y 1 A SER 42   ? B SER 42   
104 1 Y 1 A PRO 43   ? B PRO 43   
105 1 Y 1 A TYR 60   ? B TYR 60   
106 1 Y 1 A ASP 61   ? B ASP 61   
107 1 Y 1 A LYS 62   ? B LYS 62   
108 1 Y 1 A LYS 63   ? B LYS 63   
109 1 Y 1 A GLY 64   ? B GLY 64   
110 1 Y 1 A LYS 65   ? B LYS 65   
111 1 Y 1 A ILE 66   ? B ILE 66   
112 1 Y 1 A LEU 67   ? B LEU 67   
113 1 Y 1 A ARG 68   ? B ARG 68   
114 1 Y 1 A ALA 69   ? B ALA 69   
115 1 Y 1 A ASP 165  ? B ASP 165  
116 1 Y 1 A TYR 166  ? B TYR 166  
117 1 Y 1 A THR 167  ? B THR 167  
118 1 Y 1 A ASN 168  ? B ASN 168  
119 1 Y 1 A GLN 169  ? B GLN 169  
120 1 Y 1 A ASN 170  ? B ASN 170  
121 1 Y 1 A PRO 171  ? B PRO 171  
122 1 Y 1 A MET 172  ? B MET 172  
123 1 Y 1 A ALA 173  ? B ALA 173  
124 1 Y 1 A SER 174  ? B SER 174  
125 1 Y 1 A LYS 175  ? B LYS 175  
126 1 Y 1 A ASP 176  ? B ASP 176  
127 1 Y 1 A LYS 177  ? B LYS 177  
128 1 Y 1 A THR 178  ? B THR 178  
129 1 Y 1 A PHE 179  ? B PHE 179  
130 1 Y 1 A ILE 180  ? B ILE 180  
131 1 Y 1 A PRO 181  ? B PRO 181  
132 1 Y 1 A ALA 182  ? B ALA 182  
133 1 Y 1 A ILE 183  ? B ILE 183  
134 1 Y 1 A PRO 184  ? B PRO 184  
135 1 Y 1 A LEU 185  ? B LEU 185  
136 1 Y 1 A PRO 186  ? B PRO 186  
137 1 Y 1 A LYS 187  ? B LYS 187  
138 1 Y 1 A ARG 188  ? B ARG 188  
139 1 Y 1 A ARG 189  ? B ARG 189  
140 1 Y 1 A SER 190  ? B SER 190  
141 1 Y 1 A LYS 191  ? B LYS 191  
142 1 Y 1 A LYS 192  ? B LYS 192  
143 1 Y 1 A ALA 193  ? B ALA 193  
144 1 Y 1 A LYS 194  ? B LYS 194  
145 1 Y 1 A LYS 195  ? B LYS 195  
146 1 Y 1 A ALA 196  ? B ALA 196  
147 1 Y 1 A GLU 197  ? B GLU 197  
148 1 Y 1 A GLU 198  ? B GLU 198  
149 1 Y 1 A GLU 199  ? B GLU 199  
150 1 Y 1 A ALA 200  ? B ALA 200  
151 1 Y 1 A ALA 201  ? B ALA 201  
152 1 Y 1 A LEU 202  ? B LEU 202  
153 1 Y 1 A ASN 203  ? B ASN 203  
154 1 Y 1 A MET 204  ? B MET 204  
155 1 Y 1 A GLN 205  ? B GLN 205  
156 1 Y 1 A GLY 206  ? B GLY 206  
157 1 Y 1 A ARG 207  ? B ARG 207  
158 1 Y 1 A SER 208  ? B SER 208  
159 1 Y 1 A SER 209  ? B SER 209  
160 1 Y 1 A SER 210  ? B SER 210  
161 1 Y 1 A THR 211  ? B THR 211  
162 1 Y 1 A GLU 212  ? B GLU 212  
163 1 Y 1 A ASN 213  ? B ASN 213  
164 1 Y 1 A PHE 214  ? B PHE 214  
165 1 Y 1 A ALA 215  ? B ALA 215  
166 1 Y 1 A ALA 216  ? B ALA 216  
167 1 Y 1 A GLU 217  ? B GLU 217  
168 1 Y 1 A PRO 218  ? B PRO 218  
169 1 Y 1 A VAL 219  ? B VAL 219  
170 1 Y 1 A PRO 220  ? B PRO 220  
171 1 Y 1 A GLY 221  ? B GLY 221  
172 1 Y 1 A ALA 222  ? B ALA 222  
173 1 Y 1 A GLU 223  ? B GLU 223  
174 1 Y 1 A PRO 224  ? B PRO 224  
175 1 Y 1 A ARG 225  ? B ARG 225  
176 1 Y 1 A GLY 226  ? B GLY 226  
177 1 Y 1 A GLN 227  ? B GLN 227  
178 1 Y 1 A ASP 228  ? B ASP 228  
179 1 Y 1 A GLU 229  ? B GLU 229  
180 1 Y 1 A LEU 230  ? B LEU 230  
181 1 Y 1 A GLN 231  ? B GLN 231  
182 1 Y 1 A ARG 232  ? B ARG 232  
183 1 Y 1 A MET 233  ? B MET 233  
184 1 Y 1 A ARG 234  ? B ARG 234  
185 1 Y 1 A SER 235  ? B SER 235  
186 1 Y 1 A GLN 236  ? B GLN 236  
187 1 Y 1 A VAL 237  ? B VAL 237  
188 1 Y 1 A SER 238  ? B SER 238  
189 1 Y 1 A ASN 239  ? B ASN 239  
190 1 Y 1 A TRP 240  ? B TRP 240  
191 1 Y 1 A ASP 241  ? B ASP 241  
192 1 Y 1 A GLU 242  ? B GLU 242  
193 1 Y 1 A ASP 243  ? B ASP 243  
194 1 Y 1 A PRO 244  ? B PRO 244  
195 1 Y 1 A GLU 245  ? B GLU 245  
196 1 Y 1 A ALA 246  ? B ALA 246  
197 1 Y 1 A GLY 247  ? B GLY 247  
198 1 Y 1 A ASP 248  ? B ASP 248  
199 1 Y 1 A SER 249  ? B SER 249  
200 1 Y 1 A PRO 250  ? B PRO 250  
201 1 Y 1 A GLY 559  ? B GLY 559  
202 1 Y 1 A ASP 560  ? B ASP 560  
203 1 Y 1 A GLY 561  ? B GLY 561  
204 1 Y 1 A LEU 562  ? B LEU 562  
205 1 Y 1 A PRO 563  ? B PRO 563  
206 1 Y 1 A PRO 564  ? B PRO 564  
207 1 Y 1 A SER 565  ? B SER 565  
208 1 Y 1 A HIS 566  ? B HIS 566  
209 1 Y 1 A PRO 567  ? B PRO 567  
210 1 Y 1 A THR 568  ? B THR 568  
211 1 Y 1 A ILE 569  ? B ILE 569  
212 1 Y 1 A THR 570  ? B THR 570  
213 1 Y 1 A HIS 571  ? B HIS 571  
214 1 Y 1 A GLN 572  ? B GLN 572  
215 1 Y 1 A HIS 573  ? B HIS 573  
216 1 Y 1 A GLN 574  ? B GLN 574  
217 1 Y 1 A PRO 575  ? B PRO 575  
218 1 Y 1 A PRO 576  ? B PRO 576  
219 1 Y 1 A PRO 577  ? B PRO 577  
220 1 Y 1 A VAL 578  ? B VAL 578  
221 1 Y 1 A HIS 579  ? B HIS 579  
222 1 Y 1 A GLN 580  ? B GLN 580  
223 1 Y 1 A HIS 581  ? B HIS 581  
224 1 Y 1 A ASP 582  ? B ASP 582  
225 1 Y 1 A ASP 583  ? B ASP 583  
226 1 Y 1 A GLN 584  ? B GLN 584  
227 1 Y 1 A ASP 585  ? B ASP 585  
228 1 Y 1 A ASP 586  ? B ASP 586  
229 1 Y 1 A PRO 587  ? B PRO 587  
230 1 Y 1 A ILE 588  ? B ILE 588  
231 1 Y 1 A ALA 589  ? B ALA 589  
232 1 Y 1 A LYS 590  ? B LYS 590  
233 1 Y 1 A SER 591  ? B SER 591  
234 1 Y 1 A ALA 592  ? B ALA 592  
235 1 Y 1 A SER 593  ? B SER 593  
236 1 Y 1 A GLU 594  ? B GLU 594  
237 1 Y 1 A SER 595  ? B SER 595  
238 1 Y 1 A ASP 596  ? B ASP 596  
239 1 Y 1 A ASP 597  ? B ASP 597  
240 1 Y 1 A SER 598  ? B SER 598  
241 1 Y 1 A ASP 599  ? B ASP 599  
242 1 Y 1 A PRO 600  ? B PRO 600  
243 1 Y 1 A LYS 601  ? B LYS 601  
244 1 Y 1 A LYS 602  ? B LYS 602  
245 1 Y 1 A ILE 603  ? B ILE 603  
246 1 Y 1 A SER 604  ? B SER 604  
247 1 Y 1 A THR 605  ? B THR 605  
248 1 Y 1 A GLU 606  ? B GLU 606  
249 1 Y 1 A ASP 607  ? B ASP 607  
250 1 Y 1 A PRO 608  ? B PRO 608  
251 1 Y 1 A ASP 609  ? B ASP 609  
252 1 Y 1 A GLU 610  ? B GLU 610  
253 1 Y 1 A ILE 611  ? B ILE 611  
254 1 Y 1 A LYS 612  ? B LYS 612  
255 1 Y 1 A VAL 613  ? B VAL 613  
256 1 Y 1 A THR 614  ? B THR 614  
257 1 Y 1 A LEU 615  ? B LEU 615  
258 1 Y 1 A PRO 616  ? B PRO 616  
259 1 Y 1 A LYS 617  ? B LYS 617  
260 1 Y 1 A GLU 618  ? B GLU 618  
261 1 Y 1 A VAL 619  ? B VAL 619  
262 1 Y 1 A LEU 620  ? B LEU 620  
263 1 Y 1 A ALA 621  ? B ALA 621  
264 1 Y 1 A THR 622  ? B THR 622  
265 1 Y 1 A PHE 623  ? B PHE 623  
266 1 Y 1 A HIS 624  ? B HIS 624  
267 1 Y 1 A ASP 625  ? B ASP 625  
268 1 Y 1 A ALA 626  ? B ALA 626  
269 1 Y 1 A GLU 627  ? B GLU 627  
270 1 Y 1 A ASP 918  ? B ASP 918  
271 1 Y 1 A SER 919  ? B SER 919  
272 1 Y 1 A ARG 920  ? B ARG 920  
273 1 Y 1 A ARG 921  ? B ARG 921  
274 1 Y 1 A ASN 922  ? B ASN 922  
275 1 Y 1 A SER 923  ? B SER 923  
276 1 Y 1 A MET 924  ? B MET 924  
277 1 Y 1 A ASP 925  ? B ASP 925  
278 1 Y 1 A PRO 926  ? B PRO 926  
279 1 Y 1 A PRO 927  ? B PRO 927  
280 1 Y 1 A ARG 928  ? B ARG 928  
281 1 Y 1 A LEU 929  ? B LEU 929  
282 1 Y 1 A THR 930  ? B THR 930  
283 1 Y 1 A ARG 931  ? B ARG 931  
284 1 Y 1 A VAL 932  ? B VAL 932  
285 1 Y 1 A ASN 933  ? B ASN 933  
286 1 Y 1 A THR 934  ? B THR 934  
287 1 Y 1 A GLY 935  ? B GLY 935  
288 1 Y 1 A VAL 936  ? B VAL 936  
289 1 Y 1 A ARG 937  ? B ARG 937  
290 1 Y 1 A SER 938  ? B SER 938  
291 1 Y 1 A PRO 1319 ? B PRO 1319 
292 1 Y 1 A LYS 1320 ? B LYS 1320 
293 1 Y 1 A LYS 1321 ? B LYS 1321 
294 1 Y 1 A ASP 1322 ? B ASP 1322 
295 1 Y 1 A GLU 1323 ? B GLU 1323 
296 1 Y 1 A ASP 1324 ? B ASP 1324 
297 1 Y 1 A GLU 1325 ? B GLU 1325 
298 1 Y 1 A SER 1326 ? B SER 1326 
299 1 Y 1 A ASP 1327 ? B ASP 1327 
300 1 Y 1 A TYR 1328 ? B TYR 1328 
301 1 Y 1 A GLY 1329 ? B GLY 1329 
302 1 Y 1 A GLU 1330 ? B GLU 1330 
303 1 Y 1 A GLU 1331 ? B GLU 1331 
304 1 Y 1 A PRO 1332 ? B PRO 1332 
305 1 Y 1 A PHE 1333 ? B PHE 1333 
306 1 Y 1 A ASP 1334 ? B ASP 1334 
307 1 Y 1 A GLY 1335 ? B GLY 1335 
308 1 Y 1 A PRO 1336 ? B PRO 1336 
309 1 Y 1 A GLU 1337 ? B GLU 1337 
310 1 Y 1 A GLY 1338 ? B GLY 1338 
311 1 Y 1 A ARG 1339 ? B ARG 1339 
312 1 Y 1 A ARG 1340 ? B ARG 1340 
313 1 Y 1 A SER 1341 ? B SER 1341 
314 1 Y 1 A SER 1342 ? B SER 1342 
315 1 Y 1 A ILE 1343 ? B ILE 1343 
316 1 Y 1 A LYS 1344 ? B LYS 1344 
317 1 Y 1 A MET 1345 ? B MET 1345 
318 1 Y 1 A ALA 1346 ? B ALA 1346 
319 1 Y 1 A ASN 1347 ? B ASN 1347 
320 1 Y 1 A LEU 1348 ? B LEU 1348 
321 1 Y 1 A ARG 1349 ? B ARG 1349 
322 1 Y 1 A HIS 1350 ? B HIS 1350 
323 1 Y 1 A SER 1351 ? B SER 1351 
324 1 Y 1 A HIS 1352 ? B HIS 1352 
325 1 Y 1 A GLY 1353 ? B GLY 1353 
326 1 Y 1 A ALA 1354 ? B ALA 1354 
327 1 Y 1 A PHE 1355 ? B PHE 1355 
328 1 Y 1 A GLY 1356 ? B GLY 1356 
329 1 Y 1 A ARG 1357 ? B ARG 1357 
330 1 Y 1 A GLY 1358 ? B GLY 1358 
331 1 Y 1 A ASP 1359 ? B ASP 1359 
332 1 Y 1 A GLN 1360 ? B GLN 1360 
333 1 Y 1 A ALA 1361 ? B ALA 1361 
334 1 Y 1 A GLY 1362 ? B GLY 1362 
335 1 Y 1 A ASP 1363 ? B ASP 1363 
336 1 Y 1 A MET 1364 ? B MET 1364 
337 1 Y 1 A GLU 1365 ? B GLU 1365 
338 1 Y 1 A LEU 1366 ? B LEU 1366 
339 1 Y 1 A GLY 1367 ? B GLY 1367 
340 1 Y 1 A MET 1368 ? B MET 1368 
341 1 Y 1 A GLY 1369 ? B GLY 1369 
342 1 Y 1 A ARG 1370 ? B ARG 1370 
343 1 Y 1 A LYS 1371 ? B LYS 1371 
344 1 Y 1 A SER 1372 ? B SER 1372 
345 1 Y 1 A LEU 1373 ? B LEU 1373 
346 1 Y 1 A GLY 1374 ? B GLY 1374 
347 1 Y 1 A ASN 1375 ? B ASN 1375 
348 1 Y 1 A ARG 1376 ? B ARG 1376 
349 1 Y 1 A PRO 1377 ? B PRO 1377 
350 1 Y 1 A GLY 1378 ? B GLY 1378 
351 1 Y 1 A LEU 1379 ? B LEU 1379 
352 1 Y 1 A ARG 1380 ? B ARG 1380 
353 1 Y 1 A SER 1381 ? B SER 1381 
354 1 Y 1 A SER 1382 ? B SER 1382 
355 1 Y 1 A MET 1383 ? B MET 1383 
356 1 Y 1 A ASP 1384 ? B ASP 1384 
357 1 Y 1 A SER 1385 ? B SER 1385 
358 1 Y 1 A SER 1386 ? B SER 1386 
359 1 Y 1 A ARG 1387 ? B ARG 1387 
360 1 Y 1 A PHE 1388 ? B PHE 1388 
361 1 Y 1 A GLY 1389 ? B GLY 1389 
362 1 Y 1 A ILE 1390 ? B ILE 1390 
363 1 Y 1 A HIS 1391 ? B HIS 1391 
364 1 Y 1 A SER 1392 ? B SER 1392 
365 1 Y 1 A GLY 1393 ? B GLY 1393 
366 1 Y 1 A ALA 1394 ? B ALA 1394 
367 1 Y 1 A ARG 1395 ? B ARG 1395 
368 1 Y 1 A GLY 1396 ? B GLY 1396 
369 1 Y 1 A SER 1397 ? B SER 1397 
370 1 Y 1 A THR 1398 ? B THR 1398 
371 1 Y 1 A VAL 1399 ? B VAL 1399 
372 1 Y 1 A ASP 1400 ? B ASP 1400 
373 1 Y 1 A MET 1401 ? B MET 1401 
374 1 Y 1 A SER 1402 ? B SER 1402 
375 1 Y 1 A THR 1403 ? B THR 1403 
376 1 Y 1 A GLY 1404 ? B GLY 1404 
377 1 Y 1 A LEU 1405 ? B LEU 1405 
378 1 Y 1 A GLU 1406 ? B GLU 1406 
379 1 Y 1 A GLN 1407 ? B GLN 1407 
380 1 Y 1 A PRO 1408 ? B PRO 1408 
381 1 Y 1 A PRO 1409 ? B PRO 1409 
382 1 Y 1 A SER 1410 ? B SER 1410 
383 1 Y 1 A SER 1432 ? B SER 1432 
384 1 Y 1 A GLN 1433 ? B GLN 1433 
385 1 Y 1 A THR 1434 ? B THR 1434 
386 1 Y 1 A SER 1435 ? B SER 1435 
387 1 Y 1 A SER 1436 ? B SER 1436 
388 1 Y 1 A HIS 1437 ? B HIS 1437 
389 1 Y 1 A ALA 1438 ? B ALA 1438 
390 1 Y 1 A SER 1439 ? B SER 1439 
391 1 Y 1 A ARG 1440 ? B ARG 1440 
392 1 Y 1 A SER 1441 ? B SER 1441 
393 1 Y 1 A ARG 1442 ? B ARG 1442 
394 1 Y 1 A TRP 1443 ? B TRP 1443 
395 1 Y 1 A PRO 1444 ? B PRO 1444 
396 1 Y 1 A ARG 1445 ? B ARG 1445 
397 1 Y 1 A PHE 1446 ? B PHE 1446 
398 1 Y 1 A ASN 1447 ? B ASN 1447 
399 1 Y 1 A ASN 1448 ? B ASN 1448 
400 1 Y 1 A ASN 1449 ? B ASN 1449 
401 1 Y 1 A SER 1450 ? B SER 1450 
402 1 Y 1 A SER 1451 ? B SER 1451 
403 1 Y 1 A SER 1452 ? B SER 1452 
404 1 Y 1 A SER 1453 ? B SER 1453 
405 1 Y 1 A HIS 1454 ? B HIS 1454 
406 1 Y 1 A PRO 1455 ? B PRO 1455 
407 1 Y 1 A PHE 1456 ? B PHE 1456 
408 1 Y 1 A GLU 1457 ? B GLU 1457 
409 1 Y 1 A THR 1458 ? B THR 1458 
410 1 Y 1 A LYS 1459 ? B LYS 1459 
411 1 Y 1 A PRO 1460 ? B PRO 1460 
412 1 Y 1 A PRO 1461 ? B PRO 1461 
413 1 Y 1 A SER 1462 ? B SER 1462 
414 1 Y 1 A SER 1463 ? B SER 1463 
415 1 Y 1 A MET 1464 ? B MET 1464 
416 1 Y 1 A SER 1465 ? B SER 1465 
417 1 Y 1 A LYS 1466 ? B LYS 1466 
418 1 Y 1 A LEU 1467 ? B LEU 1467 
419 1 Y 1 A ARG 1468 ? B ARG 1468 
420 1 Y 1 A SER 1469 ? B SER 1469 
421 1 Y 1 A ARG 1470 ? B ARG 1470 
422 1 Y 1 A ALA 1471 ? B ALA 1471 
423 1 Y 1 A GLY 1472 ? B GLY 1472 
424 1 Y 1 A SER 1473 ? B SER 1473 
425 1 Y 1 A ILE 1474 ? B ILE 1474 
426 1 Y 1 A LEU 1475 ? B LEU 1475 
427 1 Y 1 A THR 1476 ? B THR 1476 
428 1 Y 1 A ARG 1477 ? B ARG 1477 
429 1 Y 1 A LYS 1478 ? B LYS 1478 
430 1 Y 1 A ARG 1479 ? B ARG 1479 
431 1 Y 1 A ALA 1480 ? B ALA 1480 
432 1 Y 1 A ASP 1481 ? B ASP 1481 
433 1 Y 1 A THR 1482 ? B THR 1482 
434 1 Y 1 A THR 1483 ? B THR 1483 
435 1 Y 1 A ASP 1484 ? B ASP 1484 
436 1 Y 1 A THR 1485 ? B THR 1485 
437 1 Y 1 A ARG 1486 ? B ARG 1486 
438 1 Y 1 A ASN 1487 ? B ASN 1487 
439 1 Y 1 A SER 1488 ? B SER 1488 
440 1 Y 1 A ASP 1489 ? B ASP 1489 
441 1 Y 1 A ASP 1490 ? B ASP 1490 
442 1 Y 1 A LYS 1491 ? B LYS 1491 
443 1 Y 1 A SER 1492 ? B SER 1492 
444 1 Y 1 A LEU 1493 ? B LEU 1493 
445 1 Y 1 A SER 1494 ? B SER 1494 
446 1 Y 1 A SER 1495 ? B SER 1495 
447 1 Y 1 A PRO 1496 ? B PRO 1496 
448 1 Y 1 A VAL 1497 ? B VAL 1497 
449 1 Y 1 A LYS 1498 ? B LYS 1498 
450 1 Y 1 A THR 1499 ? B THR 1499 
451 1 Y 1 A GLY 1500 ? B GLY 1500 
452 1 Y 1 A PHE 1501 ? B PHE 1501 
453 1 Y 1 A PHE 1502 ? B PHE 1502 
454 1 Y 1 A GLY 1503 ? B GLY 1503 
455 1 Y 1 A ARG 1504 ? B ARG 1504 
456 1 Y 1 A HIS 1505 ? B HIS 1505 
457 1 Y 1 A MET 1506 ? B MET 1506 
458 1 Y 1 A PRO 1507 ? B PRO 1507 
459 1 Y 1 A GLY 1508 ? B GLY 1508 
460 1 Y 1 A GLN 1509 ? B GLN 1509 
461 1 Y 1 A ASN 1510 ? B ASN 1510 
462 1 Y 1 A HIS 1511 ? B HIS 1511 
463 1 Y 1 A GLY 1512 ? B GLY 1512 
464 1 Y 1 A GLN 1513 ? B GLN 1513 
465 1 Y 1 A HIS 1514 ? B HIS 1514 
466 1 Y 1 A GLU 1515 ? B GLU 1515 
467 1 Y 1 A GLY 1516 ? B GLY 1516 
468 1 Y 1 A ARG 1517 ? B ARG 1517 
469 1 Y 1 A SER 1518 ? B SER 1518 
470 1 Y 1 A MET 1519 ? B MET 1519 
471 1 Y 1 A GLY 1520 ? B GLY 1520 
472 1 Y 1 A THR 1521 ? B THR 1521 
473 1 Y 1 A PRO 1522 ? B PRO 1522 
474 1 Y 1 A LEU 1523 ? B LEU 1523 
475 1 Y 1 A LYS 1524 ? B LYS 1524 
476 1 Y 1 A SER 1525 ? B SER 1525 
477 1 Y 1 A GLU 1526 ? B GLU 1526 
478 1 Y 1 A THR 1527 ? B THR 1527 
479 1 Y 1 A GLY 1528 ? B GLY 1528 
480 1 Y 1 A ARG 1529 ? B ARG 1529 
481 1 Y 1 A GLY 1530 ? B GLY 1530 
482 1 Y 1 A ASP 1531 ? B ASP 1531 
483 1 Y 1 A ASN 1532 ? B ASN 1532 
484 1 Y 1 A TRP 1533 ? B TRP 1533 
485 1 Y 1 A GLU 1534 ? B GLU 1534 
486 1 Y 1 A GLU 1535 ? B GLU 1535 
487 1 Y 1 A GLU 1536 ? B GLU 1536 
488 1 Y 1 A GLU 1537 ? B GLU 1537 
489 1 Y 1 A LEU 1538 ? B LEU 1538 
490 1 Y 1 A GLU 1539 ? B GLU 1539 
491 1 Y 1 A ASP 1540 ? B ASP 1540 
492 1 Y 1 A GLU 1541 ? B GLU 1541 
493 1 Y 1 A SER 1542 ? B SER 1542 
494 1 Y 1 A LEU 1543 ? B LEU 1543 
495 1 Y 1 A GLY 1544 ? B GLY 1544 
496 1 Y 1 A ARG 1545 ? B ARG 1545 
497 1 Y 1 A GLY 1546 ? B GLY 1546 
498 1 Y 1 A PHE 1547 ? B PHE 1547 
499 1 Y 1 A GLY 1548 ? B GLY 1548 
500 1 Y 1 A VAL 1549 ? B VAL 1549 
501 1 Y 1 A GLY 1550 ? B GLY 1550 
502 1 Y 1 A GLN 1551 ? B GLN 1551 
503 1 Y 1 A ASN 1552 ? B ASN 1552 
504 1 Y 1 A MET 1553 ? B MET 1553 
505 1 Y 1 A ALA 1554 ? B ALA 1554 
506 1 Y 1 A PRO 1555 ? B PRO 1555 
507 1 Y 1 A PRO 1556 ? B PRO 1556 
508 1 Y 1 A GLU 1557 ? B GLU 1557 
509 1 Y 1 A ILE 1558 ? B ILE 1558 
510 1 Y 1 A PRO 1559 ? B PRO 1559 
511 1 Y 1 A ARG 1560 ? B ARG 1560 
512 1 Y 1 A MET 1561 ? B MET 1561 
513 1 Y 1 A ASP 1562 ? B ASP 1562 
514 1 Y 1 A TYR 1563 ? B TYR 1563 
515 1 Y 1 A LYS 1564 ? B LYS 1564 
516 1 Y 1 A ASP 1565 ? B ASP 1565 
517 1 Y 1 A ASP 1566 ? B ASP 1566 
518 1 Y 1 A ASP 1567 ? B ASP 1567 
519 1 Y 1 A ASP 1568 ? B ASP 1568 
520 1 Y 1 A LYS 1569 ? B LYS 1569 
521 1 Y 1 A ILE 1570 ? B ILE 1570 
# 
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 
A1BD6 C01  C  N N 1   
A1BD6 C02  C  N N 2   
A1BD6 C03  C  N N 3   
A1BD6 C04  C  N N 4   
A1BD6 C05  C  N N 5   
A1BD6 C06  C  N N 6   
A1BD6 C07  C  N N 7   
A1BD6 C08  C  N N 8   
A1BD6 C09  C  N N 9   
A1BD6 C10  C  N N 10  
A1BD6 C11  C  N N 11  
A1BD6 C12  C  N N 12  
A1BD6 C13  C  N N 13  
A1BD6 C14  C  N N 14  
A1BD6 C15  C  N N 15  
A1BD6 C16  C  N N 16  
A1BD6 C17  C  N N 17  
A1BD6 C18  C  N R 18  
A1BD6 C19  C  N N 19  
A1BD6 C20  C  N R 20  
A1BD6 C22  C  N S 21  
A1BD6 C24  C  N S 22  
A1BD6 C26  C  N R 23  
A1BD6 C28  C  N R 24  
A1BD6 O30  O  N N 25  
A1BD6 O33  O  N N 26  
A1BD6 O35  O  N N 27  
A1BD6 O36  O  N N 28  
A1BD6 O37  O  N N 29  
A1BD6 O21  O  N N 30  
A1BD6 O23  O  N N 31  
A1BD6 O25  O  N N 32  
A1BD6 O27  O  N N 33  
A1BD6 C29  C  N S 34  
A1BD6 C31  C  N N 35  
A1BD6 C32  C  N R 36  
A1BD6 C34  C  N R 37  
A1BD6 H1   H  N N 38  
A1BD6 H2   H  N N 39  
A1BD6 H3   H  N N 40  
A1BD6 H4   H  N N 41  
A1BD6 H5   H  N N 42  
A1BD6 H6   H  N N 43  
A1BD6 H7   H  N N 44  
A1BD6 H8   H  N N 45  
A1BD6 H9   H  N N 46  
A1BD6 H10  H  N N 47  
A1BD6 H11  H  N N 48  
A1BD6 H12  H  N N 49  
A1BD6 H13  H  N N 50  
A1BD6 H14  H  N N 51  
A1BD6 H15  H  N N 52  
A1BD6 H16  H  N N 53  
A1BD6 H17  H  N N 54  
A1BD6 H18  H  N N 55  
A1BD6 H19  H  N N 56  
A1BD6 H20  H  N N 57  
A1BD6 H21  H  N N 58  
A1BD6 H22  H  N N 59  
A1BD6 H23  H  N N 60  
A1BD6 H24  H  N N 61  
A1BD6 H26  H  N N 62  
A1BD6 H28  H  N N 63  
A1BD6 H29  H  N N 64  
A1BD6 H30  H  N N 65  
A1BD6 H31  H  N N 66  
A1BD6 H32  H  N N 67  
A1BD6 H33  H  N N 68  
A1BD6 H34  H  N N 69  
A1BD6 H35  H  N N 70  
A1BD6 H36  H  N N 71  
A1BD6 H37  H  N N 72  
A1BD6 H38  H  N N 73  
A1BD6 H39  H  N N 74  
A1BD6 H40  H  N N 75  
A1BD6 H41  H  N N 76  
A1BD6 H42  H  N N 77  
A1BD6 H43  H  N N 78  
A1BD6 H44  H  N N 79  
A1BD6 H45  H  N N 80  
A1BD6 H46  H  N N 81  
A1BD6 H47  H  N N 82  
A1BD6 H48  H  N N 83  
ALA   N    N  N N 84  
ALA   CA   C  N S 85  
ALA   C    C  N N 86  
ALA   O    O  N N 87  
ALA   CB   C  N N 88  
ALA   OXT  O  N N 89  
ALA   H    H  N N 90  
ALA   H2   H  N N 91  
ALA   HA   H  N N 92  
ALA   HB1  H  N N 93  
ALA   HB2  H  N N 94  
ALA   HB3  H  N N 95  
ALA   HXT  H  N N 96  
ARG   N    N  N N 97  
ARG   CA   C  N S 98  
ARG   C    C  N N 99  
ARG   O    O  N N 100 
ARG   CB   C  N N 101 
ARG   CG   C  N N 102 
ARG   CD   C  N N 103 
ARG   NE   N  N N 104 
ARG   CZ   C  N N 105 
ARG   NH1  N  N N 106 
ARG   NH2  N  N N 107 
ARG   OXT  O  N N 108 
ARG   H    H  N N 109 
ARG   H2   H  N N 110 
ARG   HA   H  N N 111 
ARG   HB2  H  N N 112 
ARG   HB3  H  N N 113 
ARG   HG2  H  N N 114 
ARG   HG3  H  N N 115 
ARG   HD2  H  N N 116 
ARG   HD3  H  N N 117 
ARG   HE   H  N N 118 
ARG   HH11 H  N N 119 
ARG   HH12 H  N N 120 
ARG   HH21 H  N N 121 
ARG   HH22 H  N N 122 
ARG   HXT  H  N N 123 
ASN   N    N  N N 124 
ASN   CA   C  N S 125 
ASN   C    C  N N 126 
ASN   O    O  N N 127 
ASN   CB   C  N N 128 
ASN   CG   C  N N 129 
ASN   OD1  O  N N 130 
ASN   ND2  N  N N 131 
ASN   OXT  O  N N 132 
ASN   H    H  N N 133 
ASN   H2   H  N N 134 
ASN   HA   H  N N 135 
ASN   HB2  H  N N 136 
ASN   HB3  H  N N 137 
ASN   HD21 H  N N 138 
ASN   HD22 H  N N 139 
ASN   HXT  H  N N 140 
ASP   N    N  N N 141 
ASP   CA   C  N S 142 
ASP   C    C  N N 143 
ASP   O    O  N N 144 
ASP   CB   C  N N 145 
ASP   CG   C  N N 146 
ASP   OD1  O  N N 147 
ASP   OD2  O  N N 148 
ASP   OXT  O  N N 149 
ASP   H    H  N N 150 
ASP   H2   H  N N 151 
ASP   HA   H  N N 152 
ASP   HB2  H  N N 153 
ASP   HB3  H  N N 154 
ASP   HD2  H  N N 155 
ASP   HXT  H  N N 156 
BEF   BE   BE N N 157 
BEF   F1   F  N N 158 
BEF   F2   F  N N 159 
BEF   F3   F  N N 160 
BMA   C1   C  N R 161 
BMA   C2   C  N S 162 
BMA   C3   C  N S 163 
BMA   C4   C  N S 164 
BMA   C5   C  N R 165 
BMA   C6   C  N N 166 
BMA   O1   O  N N 167 
BMA   O2   O  N N 168 
BMA   O3   O  N N 169 
BMA   O4   O  N N 170 
BMA   O5   O  N N 171 
BMA   O6   O  N N 172 
BMA   H1   H  N N 173 
BMA   H2   H  N N 174 
BMA   H3   H  N N 175 
BMA   H4   H  N N 176 
BMA   H5   H  N N 177 
BMA   H61  H  N N 178 
BMA   H62  H  N N 179 
BMA   HO1  H  N N 180 
BMA   HO2  H  N N 181 
BMA   HO3  H  N N 182 
BMA   HO4  H  N N 183 
BMA   HO6  H  N N 184 
CYS   N    N  N N 185 
CYS   CA   C  N R 186 
CYS   C    C  N N 187 
CYS   O    O  N N 188 
CYS   CB   C  N N 189 
CYS   SG   S  N N 190 
CYS   OXT  O  N N 191 
CYS   H    H  N N 192 
CYS   H2   H  N N 193 
CYS   HA   H  N N 194 
CYS   HB2  H  N N 195 
CYS   HB3  H  N N 196 
CYS   HG   H  N N 197 
CYS   HXT  H  N N 198 
GLN   N    N  N N 199 
GLN   CA   C  N S 200 
GLN   C    C  N N 201 
GLN   O    O  N N 202 
GLN   CB   C  N N 203 
GLN   CG   C  N N 204 
GLN   CD   C  N N 205 
GLN   OE1  O  N N 206 
GLN   NE2  N  N N 207 
GLN   OXT  O  N N 208 
GLN   H    H  N N 209 
GLN   H2   H  N N 210 
GLN   HA   H  N N 211 
GLN   HB2  H  N N 212 
GLN   HB3  H  N N 213 
GLN   HG2  H  N N 214 
GLN   HG3  H  N N 215 
GLN   HE21 H  N N 216 
GLN   HE22 H  N N 217 
GLN   HXT  H  N N 218 
GLU   N    N  N N 219 
GLU   CA   C  N S 220 
GLU   C    C  N N 221 
GLU   O    O  N N 222 
GLU   CB   C  N N 223 
GLU   CG   C  N N 224 
GLU   CD   C  N N 225 
GLU   OE1  O  N N 226 
GLU   OE2  O  N N 227 
GLU   OXT  O  N N 228 
GLU   H    H  N N 229 
GLU   H2   H  N N 230 
GLU   HA   H  N N 231 
GLU   HB2  H  N N 232 
GLU   HB3  H  N N 233 
GLU   HG2  H  N N 234 
GLU   HG3  H  N N 235 
GLU   HE2  H  N N 236 
GLU   HXT  H  N N 237 
GLY   N    N  N N 238 
GLY   CA   C  N N 239 
GLY   C    C  N N 240 
GLY   O    O  N N 241 
GLY   OXT  O  N N 242 
GLY   H    H  N N 243 
GLY   H2   H  N N 244 
GLY   HA2  H  N N 245 
GLY   HA3  H  N N 246 
GLY   HXT  H  N N 247 
HIS   N    N  N N 248 
HIS   CA   C  N S 249 
HIS   C    C  N N 250 
HIS   O    O  N N 251 
HIS   CB   C  N N 252 
HIS   CG   C  Y N 253 
HIS   ND1  N  Y N 254 
HIS   CD2  C  Y N 255 
HIS   CE1  C  Y N 256 
HIS   NE2  N  Y N 257 
HIS   OXT  O  N N 258 
HIS   H    H  N N 259 
HIS   H2   H  N N 260 
HIS   HA   H  N N 261 
HIS   HB2  H  N N 262 
HIS   HB3  H  N N 263 
HIS   HD1  H  N N 264 
HIS   HD2  H  N N 265 
HIS   HE1  H  N N 266 
HIS   HE2  H  N N 267 
HIS   HXT  H  N N 268 
ILE   N    N  N N 269 
ILE   CA   C  N S 270 
ILE   C    C  N N 271 
ILE   O    O  N N 272 
ILE   CB   C  N S 273 
ILE   CG1  C  N N 274 
ILE   CG2  C  N N 275 
ILE   CD1  C  N N 276 
ILE   OXT  O  N N 277 
ILE   H    H  N N 278 
ILE   H2   H  N N 279 
ILE   HA   H  N N 280 
ILE   HB   H  N N 281 
ILE   HG12 H  N N 282 
ILE   HG13 H  N N 283 
ILE   HG21 H  N N 284 
ILE   HG22 H  N N 285 
ILE   HG23 H  N N 286 
ILE   HD11 H  N N 287 
ILE   HD12 H  N N 288 
ILE   HD13 H  N N 289 
ILE   HXT  H  N N 290 
LEU   N    N  N N 291 
LEU   CA   C  N S 292 
LEU   C    C  N N 293 
LEU   O    O  N N 294 
LEU   CB   C  N N 295 
LEU   CG   C  N N 296 
LEU   CD1  C  N N 297 
LEU   CD2  C  N N 298 
LEU   OXT  O  N N 299 
LEU   H    H  N N 300 
LEU   H2   H  N N 301 
LEU   HA   H  N N 302 
LEU   HB2  H  N N 303 
LEU   HB3  H  N N 304 
LEU   HG   H  N N 305 
LEU   HD11 H  N N 306 
LEU   HD12 H  N N 307 
LEU   HD13 H  N N 308 
LEU   HD21 H  N N 309 
LEU   HD22 H  N N 310 
LEU   HD23 H  N N 311 
LEU   HXT  H  N N 312 
LYS   N    N  N N 313 
LYS   CA   C  N S 314 
LYS   C    C  N N 315 
LYS   O    O  N N 316 
LYS   CB   C  N N 317 
LYS   CG   C  N N 318 
LYS   CD   C  N N 319 
LYS   CE   C  N N 320 
LYS   NZ   N  N N 321 
LYS   OXT  O  N N 322 
LYS   H    H  N N 323 
LYS   H2   H  N N 324 
LYS   HA   H  N N 325 
LYS   HB2  H  N N 326 
LYS   HB3  H  N N 327 
LYS   HG2  H  N N 328 
LYS   HG3  H  N N 329 
LYS   HD2  H  N N 330 
LYS   HD3  H  N N 331 
LYS   HE2  H  N N 332 
LYS   HE3  H  N N 333 
LYS   HZ1  H  N N 334 
LYS   HZ2  H  N N 335 
LYS   HZ3  H  N N 336 
LYS   HXT  H  N N 337 
MAN   C1   C  N S 338 
MAN   C2   C  N S 339 
MAN   C3   C  N S 340 
MAN   C4   C  N S 341 
MAN   C5   C  N R 342 
MAN   C6   C  N N 343 
MAN   O1   O  N N 344 
MAN   O2   O  N N 345 
MAN   O3   O  N N 346 
MAN   O4   O  N N 347 
MAN   O5   O  N N 348 
MAN   O6   O  N N 349 
MAN   H1   H  N N 350 
MAN   H2   H  N N 351 
MAN   H3   H  N N 352 
MAN   H4   H  N N 353 
MAN   H5   H  N N 354 
MAN   H61  H  N N 355 
MAN   H62  H  N N 356 
MAN   HO1  H  N N 357 
MAN   HO2  H  N N 358 
MAN   HO3  H  N N 359 
MAN   HO4  H  N N 360 
MAN   HO6  H  N N 361 
MET   N    N  N N 362 
MET   CA   C  N S 363 
MET   C    C  N N 364 
MET   O    O  N N 365 
MET   CB   C  N N 366 
MET   CG   C  N N 367 
MET   SD   S  N N 368 
MET   CE   C  N N 369 
MET   OXT  O  N N 370 
MET   H    H  N N 371 
MET   H2   H  N N 372 
MET   HA   H  N N 373 
MET   HB2  H  N N 374 
MET   HB3  H  N N 375 
MET   HG2  H  N N 376 
MET   HG3  H  N N 377 
MET   HE1  H  N N 378 
MET   HE2  H  N N 379 
MET   HE3  H  N N 380 
MET   HXT  H  N N 381 
MG    MG   MG N N 382 
NAG   C1   C  N R 383 
NAG   C2   C  N R 384 
NAG   C3   C  N R 385 
NAG   C4   C  N S 386 
NAG   C5   C  N R 387 
NAG   C6   C  N N 388 
NAG   C7   C  N N 389 
NAG   C8   C  N N 390 
NAG   N2   N  N N 391 
NAG   O1   O  N N 392 
NAG   O3   O  N N 393 
NAG   O4   O  N N 394 
NAG   O5   O  N N 395 
NAG   O6   O  N N 396 
NAG   O7   O  N N 397 
NAG   H1   H  N N 398 
NAG   H2   H  N N 399 
NAG   H3   H  N N 400 
NAG   H4   H  N N 401 
NAG   H5   H  N N 402 
NAG   H61  H  N N 403 
NAG   H62  H  N N 404 
NAG   H81  H  N N 405 
NAG   H82  H  N N 406 
NAG   H83  H  N N 407 
NAG   HN2  H  N N 408 
NAG   HO1  H  N N 409 
NAG   HO3  H  N N 410 
NAG   HO4  H  N N 411 
NAG   HO6  H  N N 412 
PHE   N    N  N N 413 
PHE   CA   C  N S 414 
PHE   C    C  N N 415 
PHE   O    O  N N 416 
PHE   CB   C  N N 417 
PHE   CG   C  Y N 418 
PHE   CD1  C  Y N 419 
PHE   CD2  C  Y N 420 
PHE   CE1  C  Y N 421 
PHE   CE2  C  Y N 422 
PHE   CZ   C  Y N 423 
PHE   OXT  O  N N 424 
PHE   H    H  N N 425 
PHE   H2   H  N N 426 
PHE   HA   H  N N 427 
PHE   HB2  H  N N 428 
PHE   HB3  H  N N 429 
PHE   HD1  H  N N 430 
PHE   HD2  H  N N 431 
PHE   HE1  H  N N 432 
PHE   HE2  H  N N 433 
PHE   HZ   H  N N 434 
PHE   HXT  H  N N 435 
PRO   N    N  N N 436 
PRO   CA   C  N S 437 
PRO   C    C  N N 438 
PRO   O    O  N N 439 
PRO   CB   C  N N 440 
PRO   CG   C  N N 441 
PRO   CD   C  N N 442 
PRO   OXT  O  N N 443 
PRO   H    H  N N 444 
PRO   HA   H  N N 445 
PRO   HB2  H  N N 446 
PRO   HB3  H  N N 447 
PRO   HG2  H  N N 448 
PRO   HG3  H  N N 449 
PRO   HD2  H  N N 450 
PRO   HD3  H  N N 451 
PRO   HXT  H  N N 452 
SER   N    N  N N 453 
SER   CA   C  N S 454 
SER   C    C  N N 455 
SER   O    O  N N 456 
SER   CB   C  N N 457 
SER   OG   O  N N 458 
SER   OXT  O  N N 459 
SER   H    H  N N 460 
SER   H2   H  N N 461 
SER   HA   H  N N 462 
SER   HB2  H  N N 463 
SER   HB3  H  N N 464 
SER   HG   H  N N 465 
SER   HXT  H  N N 466 
THR   N    N  N N 467 
THR   CA   C  N S 468 
THR   C    C  N N 469 
THR   O    O  N N 470 
THR   CB   C  N R 471 
THR   OG1  O  N N 472 
THR   CG2  C  N N 473 
THR   OXT  O  N N 474 
THR   H    H  N N 475 
THR   H2   H  N N 476 
THR   HA   H  N N 477 
THR   HB   H  N N 478 
THR   HG1  H  N N 479 
THR   HG21 H  N N 480 
THR   HG22 H  N N 481 
THR   HG23 H  N N 482 
THR   HXT  H  N N 483 
TRP   N    N  N N 484 
TRP   CA   C  N S 485 
TRP   C    C  N N 486 
TRP   O    O  N N 487 
TRP   CB   C  N N 488 
TRP   CG   C  Y N 489 
TRP   CD1  C  Y N 490 
TRP   CD2  C  Y N 491 
TRP   NE1  N  Y N 492 
TRP   CE2  C  Y N 493 
TRP   CE3  C  Y N 494 
TRP   CZ2  C  Y N 495 
TRP   CZ3  C  Y N 496 
TRP   CH2  C  Y N 497 
TRP   OXT  O  N N 498 
TRP   H    H  N N 499 
TRP   H2   H  N N 500 
TRP   HA   H  N N 501 
TRP   HB2  H  N N 502 
TRP   HB3  H  N N 503 
TRP   HD1  H  N N 504 
TRP   HE1  H  N N 505 
TRP   HE3  H  N N 506 
TRP   HZ2  H  N N 507 
TRP   HZ3  H  N N 508 
TRP   HH2  H  N N 509 
TRP   HXT  H  N N 510 
TYR   N    N  N N 511 
TYR   CA   C  N S 512 
TYR   C    C  N N 513 
TYR   O    O  N N 514 
TYR   CB   C  N N 515 
TYR   CG   C  Y N 516 
TYR   CD1  C  Y N 517 
TYR   CD2  C  Y N 518 
TYR   CE1  C  Y N 519 
TYR   CE2  C  Y N 520 
TYR   CZ   C  Y N 521 
TYR   OH   O  N N 522 
TYR   OXT  O  N N 523 
TYR   H    H  N N 524 
TYR   H2   H  N N 525 
TYR   HA   H  N N 526 
TYR   HB2  H  N N 527 
TYR   HB3  H  N N 528 
TYR   HD1  H  N N 529 
TYR   HD2  H  N N 530 
TYR   HE1  H  N N 531 
TYR   HE2  H  N N 532 
TYR   HH   H  N N 533 
TYR   HXT  H  N N 534 
VAL   N    N  N N 535 
VAL   CA   C  N S 536 
VAL   C    C  N N 537 
VAL   O    O  N N 538 
VAL   CB   C  N N 539 
VAL   CG1  C  N N 540 
VAL   CG2  C  N N 541 
VAL   OXT  O  N N 542 
VAL   H    H  N N 543 
VAL   H2   H  N N 544 
VAL   HA   H  N N 545 
VAL   HB   H  N N 546 
VAL   HG11 H  N N 547 
VAL   HG12 H  N N 548 
VAL   HG13 H  N N 549 
VAL   HG21 H  N N 550 
VAL   HG22 H  N N 551 
VAL   HG23 H  N N 552 
VAL   HXT  H  N N 553 
# 
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 
A1BD6 C03 C02  sing N N 1   
A1BD6 C01 C02  sing N N 2   
A1BD6 C11 C10  sing N N 3   
A1BD6 C11 C12  sing N N 4   
A1BD6 C02 C04  sing N N 5   
A1BD6 C02 C05  sing N N 6   
A1BD6 C10 C09  doub N E 7   
A1BD6 C12 C13  sing N N 8   
A1BD6 C06 C05  sing N N 9   
A1BD6 C06 C07  sing N N 10  
A1BD6 C09 C08  sing N N 11  
A1BD6 C13 C14  doub N E 12  
A1BD6 C07 C08  doub N Z 13  
A1BD6 C14 C15  sing N N 14  
A1BD6 C15 C16  doub N E 15  
A1BD6 C16 C17  sing N N 16  
A1BD6 C17 C18  sing N N 17  
A1BD6 C19 C18  sing N N 18  
A1BD6 C18 C20  sing N N 19  
A1BD6 C22 O23  sing N N 20  
A1BD6 C22 C20  sing N N 21  
A1BD6 C22 C24  sing N N 22  
A1BD6 O37 C28  sing N N 23  
A1BD6 O25 C24  sing N N 24  
A1BD6 C20 O21  sing N N 25  
A1BD6 C24 C26  sing N N 26  
A1BD6 C28 C26  sing N N 27  
A1BD6 C28 C29  sing N N 28  
A1BD6 C26 O27  sing N N 29  
A1BD6 O30 C29  sing N N 30  
A1BD6 O30 C31  sing N N 31  
A1BD6 C29 C34  sing N N 32  
A1BD6 C34 C32  sing N N 33  
A1BD6 C34 O35  sing N N 34  
A1BD6 C31 O36  doub N N 35  
A1BD6 C31 C32  sing N N 36  
A1BD6 O33 C32  sing N N 37  
A1BD6 C01 H1   sing N N 38  
A1BD6 C01 H2   sing N N 39  
A1BD6 C01 H3   sing N N 40  
A1BD6 C03 H4   sing N N 41  
A1BD6 C03 H5   sing N N 42  
A1BD6 C03 H6   sing N N 43  
A1BD6 C04 H7   sing N N 44  
A1BD6 C04 H8   sing N N 45  
A1BD6 C04 H9   sing N N 46  
A1BD6 C05 H10  sing N N 47  
A1BD6 C05 H11  sing N N 48  
A1BD6 C06 H12  sing N N 49  
A1BD6 C06 H13  sing N N 50  
A1BD6 C07 H14  sing N N 51  
A1BD6 C08 H15  sing N N 52  
A1BD6 C09 H16  sing N N 53  
A1BD6 C10 H17  sing N N 54  
A1BD6 C11 H18  sing N N 55  
A1BD6 C11 H19  sing N N 56  
A1BD6 C12 H20  sing N N 57  
A1BD6 C12 H21  sing N N 58  
A1BD6 C13 H22  sing N N 59  
A1BD6 C14 H23  sing N N 60  
A1BD6 C15 H24  sing N N 61  
A1BD6 C16 H26  sing N N 62  
A1BD6 C17 H28  sing N N 63  
A1BD6 C17 H29  sing N N 64  
A1BD6 C18 H30  sing N N 65  
A1BD6 C19 H31  sing N N 66  
A1BD6 C19 H32  sing N N 67  
A1BD6 C19 H33  sing N N 68  
A1BD6 C20 H34  sing N N 69  
A1BD6 C22 H35  sing N N 70  
A1BD6 C24 H36  sing N N 71  
A1BD6 C26 H37  sing N N 72  
A1BD6 C28 H38  sing N N 73  
A1BD6 O33 H39  sing N N 74  
A1BD6 O35 H40  sing N N 75  
A1BD6 O37 H41  sing N N 76  
A1BD6 O21 H42  sing N N 77  
A1BD6 O23 H43  sing N N 78  
A1BD6 O25 H44  sing N N 79  
A1BD6 O27 H45  sing N N 80  
A1BD6 C29 H46  sing N N 81  
A1BD6 C32 H47  sing N N 82  
A1BD6 C34 H48  sing N N 83  
ALA   N   CA   sing N N 84  
ALA   N   H    sing N N 85  
ALA   N   H2   sing N N 86  
ALA   CA  C    sing N N 87  
ALA   CA  CB   sing N N 88  
ALA   CA  HA   sing N N 89  
ALA   C   O    doub N N 90  
ALA   C   OXT  sing N N 91  
ALA   CB  HB1  sing N N 92  
ALA   CB  HB2  sing N N 93  
ALA   CB  HB3  sing N N 94  
ALA   OXT HXT  sing N N 95  
ARG   N   CA   sing N N 96  
ARG   N   H    sing N N 97  
ARG   N   H2   sing N N 98  
ARG   CA  C    sing N N 99  
ARG   CA  CB   sing N N 100 
ARG   CA  HA   sing N N 101 
ARG   C   O    doub N N 102 
ARG   C   OXT  sing N N 103 
ARG   CB  CG   sing N N 104 
ARG   CB  HB2  sing N N 105 
ARG   CB  HB3  sing N N 106 
ARG   CG  CD   sing N N 107 
ARG   CG  HG2  sing N N 108 
ARG   CG  HG3  sing N N 109 
ARG   CD  NE   sing N N 110 
ARG   CD  HD2  sing N N 111 
ARG   CD  HD3  sing N N 112 
ARG   NE  CZ   sing N N 113 
ARG   NE  HE   sing N N 114 
ARG   CZ  NH1  sing N N 115 
ARG   CZ  NH2  doub N N 116 
ARG   NH1 HH11 sing N N 117 
ARG   NH1 HH12 sing N N 118 
ARG   NH2 HH21 sing N N 119 
ARG   NH2 HH22 sing N N 120 
ARG   OXT HXT  sing N N 121 
ASN   N   CA   sing N N 122 
ASN   N   H    sing N N 123 
ASN   N   H2   sing N N 124 
ASN   CA  C    sing N N 125 
ASN   CA  CB   sing N N 126 
ASN   CA  HA   sing N N 127 
ASN   C   O    doub N N 128 
ASN   C   OXT  sing N N 129 
ASN   CB  CG   sing N N 130 
ASN   CB  HB2  sing N N 131 
ASN   CB  HB3  sing N N 132 
ASN   CG  OD1  doub N N 133 
ASN   CG  ND2  sing N N 134 
ASN   ND2 HD21 sing N N 135 
ASN   ND2 HD22 sing N N 136 
ASN   OXT HXT  sing N N 137 
ASP   N   CA   sing N N 138 
ASP   N   H    sing N N 139 
ASP   N   H2   sing N N 140 
ASP   CA  C    sing N N 141 
ASP   CA  CB   sing N N 142 
ASP   CA  HA   sing N N 143 
ASP   C   O    doub N N 144 
ASP   C   OXT  sing N N 145 
ASP   CB  CG   sing N N 146 
ASP   CB  HB2  sing N N 147 
ASP   CB  HB3  sing N N 148 
ASP   CG  OD1  doub N N 149 
ASP   CG  OD2  sing N N 150 
ASP   OD2 HD2  sing N N 151 
ASP   OXT HXT  sing N N 152 
BEF   BE  F1   sing N N 153 
BEF   BE  F2   sing N N 154 
BEF   BE  F3   sing N N 155 
BMA   C1  C2   sing N N 156 
BMA   C1  O1   sing N N 157 
BMA   C1  O5   sing N N 158 
BMA   C1  H1   sing N N 159 
BMA   C2  C3   sing N N 160 
BMA   C2  O2   sing N N 161 
BMA   C2  H2   sing N N 162 
BMA   C3  C4   sing N N 163 
BMA   C3  O3   sing N N 164 
BMA   C3  H3   sing N N 165 
BMA   C4  C5   sing N N 166 
BMA   C4  O4   sing N N 167 
BMA   C4  H4   sing N N 168 
BMA   C5  C6   sing N N 169 
BMA   C5  O5   sing N N 170 
BMA   C5  H5   sing N N 171 
BMA   C6  O6   sing N N 172 
BMA   C6  H61  sing N N 173 
BMA   C6  H62  sing N N 174 
BMA   O1  HO1  sing N N 175 
BMA   O2  HO2  sing N N 176 
BMA   O3  HO3  sing N N 177 
BMA   O4  HO4  sing N N 178 
BMA   O6  HO6  sing N N 179 
CYS   N   CA   sing N N 180 
CYS   N   H    sing N N 181 
CYS   N   H2   sing N N 182 
CYS   CA  C    sing N N 183 
CYS   CA  CB   sing N N 184 
CYS   CA  HA   sing N N 185 
CYS   C   O    doub N N 186 
CYS   C   OXT  sing N N 187 
CYS   CB  SG   sing N N 188 
CYS   CB  HB2  sing N N 189 
CYS   CB  HB3  sing N N 190 
CYS   SG  HG   sing N N 191 
CYS   OXT HXT  sing N N 192 
GLN   N   CA   sing N N 193 
GLN   N   H    sing N N 194 
GLN   N   H2   sing N N 195 
GLN   CA  C    sing N N 196 
GLN   CA  CB   sing N N 197 
GLN   CA  HA   sing N N 198 
GLN   C   O    doub N N 199 
GLN   C   OXT  sing N N 200 
GLN   CB  CG   sing N N 201 
GLN   CB  HB2  sing N N 202 
GLN   CB  HB3  sing N N 203 
GLN   CG  CD   sing N N 204 
GLN   CG  HG2  sing N N 205 
GLN   CG  HG3  sing N N 206 
GLN   CD  OE1  doub N N 207 
GLN   CD  NE2  sing N N 208 
GLN   NE2 HE21 sing N N 209 
GLN   NE2 HE22 sing N N 210 
GLN   OXT HXT  sing N N 211 
GLU   N   CA   sing N N 212 
GLU   N   H    sing N N 213 
GLU   N   H2   sing N N 214 
GLU   CA  C    sing N N 215 
GLU   CA  CB   sing N N 216 
GLU   CA  HA   sing N N 217 
GLU   C   O    doub N N 218 
GLU   C   OXT  sing N N 219 
GLU   CB  CG   sing N N 220 
GLU   CB  HB2  sing N N 221 
GLU   CB  HB3  sing N N 222 
GLU   CG  CD   sing N N 223 
GLU   CG  HG2  sing N N 224 
GLU   CG  HG3  sing N N 225 
GLU   CD  OE1  doub N N 226 
GLU   CD  OE2  sing N N 227 
GLU   OE2 HE2  sing N N 228 
GLU   OXT HXT  sing N N 229 
GLY   N   CA   sing N N 230 
GLY   N   H    sing N N 231 
GLY   N   H2   sing N N 232 
GLY   CA  C    sing N N 233 
GLY   CA  HA2  sing N N 234 
GLY   CA  HA3  sing N N 235 
GLY   C   O    doub N N 236 
GLY   C   OXT  sing N N 237 
GLY   OXT HXT  sing N N 238 
HIS   N   CA   sing N N 239 
HIS   N   H    sing N N 240 
HIS   N   H2   sing N N 241 
HIS   CA  C    sing N N 242 
HIS   CA  CB   sing N N 243 
HIS   CA  HA   sing N N 244 
HIS   C   O    doub N N 245 
HIS   C   OXT  sing N N 246 
HIS   CB  CG   sing N N 247 
HIS   CB  HB2  sing N N 248 
HIS   CB  HB3  sing N N 249 
HIS   CG  ND1  sing Y N 250 
HIS   CG  CD2  doub Y N 251 
HIS   ND1 CE1  doub Y N 252 
HIS   ND1 HD1  sing N N 253 
HIS   CD2 NE2  sing Y N 254 
HIS   CD2 HD2  sing N N 255 
HIS   CE1 NE2  sing Y N 256 
HIS   CE1 HE1  sing N N 257 
HIS   NE2 HE2  sing N N 258 
HIS   OXT HXT  sing N N 259 
ILE   N   CA   sing N N 260 
ILE   N   H    sing N N 261 
ILE   N   H2   sing N N 262 
ILE   CA  C    sing N N 263 
ILE   CA  CB   sing N N 264 
ILE   CA  HA   sing N N 265 
ILE   C   O    doub N N 266 
ILE   C   OXT  sing N N 267 
ILE   CB  CG1  sing N N 268 
ILE   CB  CG2  sing N N 269 
ILE   CB  HB   sing N N 270 
ILE   CG1 CD1  sing N N 271 
ILE   CG1 HG12 sing N N 272 
ILE   CG1 HG13 sing N N 273 
ILE   CG2 HG21 sing N N 274 
ILE   CG2 HG22 sing N N 275 
ILE   CG2 HG23 sing N N 276 
ILE   CD1 HD11 sing N N 277 
ILE   CD1 HD12 sing N N 278 
ILE   CD1 HD13 sing N N 279 
ILE   OXT HXT  sing N N 280 
LEU   N   CA   sing N N 281 
LEU   N   H    sing N N 282 
LEU   N   H2   sing N N 283 
LEU   CA  C    sing N N 284 
LEU   CA  CB   sing N N 285 
LEU   CA  HA   sing N N 286 
LEU   C   O    doub N N 287 
LEU   C   OXT  sing N N 288 
LEU   CB  CG   sing N N 289 
LEU   CB  HB2  sing N N 290 
LEU   CB  HB3  sing N N 291 
LEU   CG  CD1  sing N N 292 
LEU   CG  CD2  sing N N 293 
LEU   CG  HG   sing N N 294 
LEU   CD1 HD11 sing N N 295 
LEU   CD1 HD12 sing N N 296 
LEU   CD1 HD13 sing N N 297 
LEU   CD2 HD21 sing N N 298 
LEU   CD2 HD22 sing N N 299 
LEU   CD2 HD23 sing N N 300 
LEU   OXT HXT  sing N N 301 
LYS   N   CA   sing N N 302 
LYS   N   H    sing N N 303 
LYS   N   H2   sing N N 304 
LYS   CA  C    sing N N 305 
LYS   CA  CB   sing N N 306 
LYS   CA  HA   sing N N 307 
LYS   C   O    doub N N 308 
LYS   C   OXT  sing N N 309 
LYS   CB  CG   sing N N 310 
LYS   CB  HB2  sing N N 311 
LYS   CB  HB3  sing N N 312 
LYS   CG  CD   sing N N 313 
LYS   CG  HG2  sing N N 314 
LYS   CG  HG3  sing N N 315 
LYS   CD  CE   sing N N 316 
LYS   CD  HD2  sing N N 317 
LYS   CD  HD3  sing N N 318 
LYS   CE  NZ   sing N N 319 
LYS   CE  HE2  sing N N 320 
LYS   CE  HE3  sing N N 321 
LYS   NZ  HZ1  sing N N 322 
LYS   NZ  HZ2  sing N N 323 
LYS   NZ  HZ3  sing N N 324 
LYS   OXT HXT  sing N N 325 
MAN   C1  C2   sing N N 326 
MAN   C1  O1   sing N N 327 
MAN   C1  O5   sing N N 328 
MAN   C1  H1   sing N N 329 
MAN   C2  C3   sing N N 330 
MAN   C2  O2   sing N N 331 
MAN   C2  H2   sing N N 332 
MAN   C3  C4   sing N N 333 
MAN   C3  O3   sing N N 334 
MAN   C3  H3   sing N N 335 
MAN   C4  C5   sing N N 336 
MAN   C4  O4   sing N N 337 
MAN   C4  H4   sing N N 338 
MAN   C5  C6   sing N N 339 
MAN   C5  O5   sing N N 340 
MAN   C5  H5   sing N N 341 
MAN   C6  O6   sing N N 342 
MAN   C6  H61  sing N N 343 
MAN   C6  H62  sing N N 344 
MAN   O1  HO1  sing N N 345 
MAN   O2  HO2  sing N N 346 
MAN   O3  HO3  sing N N 347 
MAN   O4  HO4  sing N N 348 
MAN   O6  HO6  sing N N 349 
MET   N   CA   sing N N 350 
MET   N   H    sing N N 351 
MET   N   H2   sing N N 352 
MET   CA  C    sing N N 353 
MET   CA  CB   sing N N 354 
MET   CA  HA   sing N N 355 
MET   C   O    doub N N 356 
MET   C   OXT  sing N N 357 
MET   CB  CG   sing N N 358 
MET   CB  HB2  sing N N 359 
MET   CB  HB3  sing N N 360 
MET   CG  SD   sing N N 361 
MET   CG  HG2  sing N N 362 
MET   CG  HG3  sing N N 363 
MET   SD  CE   sing N N 364 
MET   CE  HE1  sing N N 365 
MET   CE  HE2  sing N N 366 
MET   CE  HE3  sing N N 367 
MET   OXT HXT  sing N N 368 
NAG   C1  C2   sing N N 369 
NAG   C1  O1   sing N N 370 
NAG   C1  O5   sing N N 371 
NAG   C1  H1   sing N N 372 
NAG   C2  C3   sing N N 373 
NAG   C2  N2   sing N N 374 
NAG   C2  H2   sing N N 375 
NAG   C3  C4   sing N N 376 
NAG   C3  O3   sing N N 377 
NAG   C3  H3   sing N N 378 
NAG   C4  C5   sing N N 379 
NAG   C4  O4   sing N N 380 
NAG   C4  H4   sing N N 381 
NAG   C5  C6   sing N N 382 
NAG   C5  O5   sing N N 383 
NAG   C5  H5   sing N N 384 
NAG   C6  O6   sing N N 385 
NAG   C6  H61  sing N N 386 
NAG   C6  H62  sing N N 387 
NAG   C7  C8   sing N N 388 
NAG   C7  N2   sing N N 389 
NAG   C7  O7   doub N N 390 
NAG   C8  H81  sing N N 391 
NAG   C8  H82  sing N N 392 
NAG   C8  H83  sing N N 393 
NAG   N2  HN2  sing N N 394 
NAG   O1  HO1  sing N N 395 
NAG   O3  HO3  sing N N 396 
NAG   O4  HO4  sing N N 397 
NAG   O6  HO6  sing N N 398 
PHE   N   CA   sing N N 399 
PHE   N   H    sing N N 400 
PHE   N   H2   sing N N 401 
PHE   CA  C    sing N N 402 
PHE   CA  CB   sing N N 403 
PHE   CA  HA   sing N N 404 
PHE   C   O    doub N N 405 
PHE   C   OXT  sing N N 406 
PHE   CB  CG   sing N N 407 
PHE   CB  HB2  sing N N 408 
PHE   CB  HB3  sing N N 409 
PHE   CG  CD1  doub Y N 410 
PHE   CG  CD2  sing Y N 411 
PHE   CD1 CE1  sing Y N 412 
PHE   CD1 HD1  sing N N 413 
PHE   CD2 CE2  doub Y N 414 
PHE   CD2 HD2  sing N N 415 
PHE   CE1 CZ   doub Y N 416 
PHE   CE1 HE1  sing N N 417 
PHE   CE2 CZ   sing Y N 418 
PHE   CE2 HE2  sing N N 419 
PHE   CZ  HZ   sing N N 420 
PHE   OXT HXT  sing N N 421 
PRO   N   CA   sing N N 422 
PRO   N   CD   sing N N 423 
PRO   N   H    sing N N 424 
PRO   CA  C    sing N N 425 
PRO   CA  CB   sing N N 426 
PRO   CA  HA   sing N N 427 
PRO   C   O    doub N N 428 
PRO   C   OXT  sing N N 429 
PRO   CB  CG   sing N N 430 
PRO   CB  HB2  sing N N 431 
PRO   CB  HB3  sing N N 432 
PRO   CG  CD   sing N N 433 
PRO   CG  HG2  sing N N 434 
PRO   CG  HG3  sing N N 435 
PRO   CD  HD2  sing N N 436 
PRO   CD  HD3  sing N N 437 
PRO   OXT HXT  sing N N 438 
SER   N   CA   sing N N 439 
SER   N   H    sing N N 440 
SER   N   H2   sing N N 441 
SER   CA  C    sing N N 442 
SER   CA  CB   sing N N 443 
SER   CA  HA   sing N N 444 
SER   C   O    doub N N 445 
SER   C   OXT  sing N N 446 
SER   CB  OG   sing N N 447 
SER   CB  HB2  sing N N 448 
SER   CB  HB3  sing N N 449 
SER   OG  HG   sing N N 450 
SER   OXT HXT  sing N N 451 
THR   N   CA   sing N N 452 
THR   N   H    sing N N 453 
THR   N   H2   sing N N 454 
THR   CA  C    sing N N 455 
THR   CA  CB   sing N N 456 
THR   CA  HA   sing N N 457 
THR   C   O    doub N N 458 
THR   C   OXT  sing N N 459 
THR   CB  OG1  sing N N 460 
THR   CB  CG2  sing N N 461 
THR   CB  HB   sing N N 462 
THR   OG1 HG1  sing N N 463 
THR   CG2 HG21 sing N N 464 
THR   CG2 HG22 sing N N 465 
THR   CG2 HG23 sing N N 466 
THR   OXT HXT  sing N N 467 
TRP   N   CA   sing N N 468 
TRP   N   H    sing N N 469 
TRP   N   H2   sing N N 470 
TRP   CA  C    sing N N 471 
TRP   CA  CB   sing N N 472 
TRP   CA  HA   sing N N 473 
TRP   C   O    doub N N 474 
TRP   C   OXT  sing N N 475 
TRP   CB  CG   sing N N 476 
TRP   CB  HB2  sing N N 477 
TRP   CB  HB3  sing N N 478 
TRP   CG  CD1  doub Y N 479 
TRP   CG  CD2  sing Y N 480 
TRP   CD1 NE1  sing Y N 481 
TRP   CD1 HD1  sing N N 482 
TRP   CD2 CE2  doub Y N 483 
TRP   CD2 CE3  sing Y N 484 
TRP   NE1 CE2  sing Y N 485 
TRP   NE1 HE1  sing N N 486 
TRP   CE2 CZ2  sing Y N 487 
TRP   CE3 CZ3  doub Y N 488 
TRP   CE3 HE3  sing N N 489 
TRP   CZ2 CH2  doub Y N 490 
TRP   CZ2 HZ2  sing N N 491 
TRP   CZ3 CH2  sing Y N 492 
TRP   CZ3 HZ3  sing N N 493 
TRP   CH2 HH2  sing N N 494 
TRP   OXT HXT  sing N N 495 
TYR   N   CA   sing N N 496 
TYR   N   H    sing N N 497 
TYR   N   H2   sing N N 498 
TYR   CA  C    sing N N 499 
TYR   CA  CB   sing N N 500 
TYR   CA  HA   sing N N 501 
TYR   C   O    doub N N 502 
TYR   C   OXT  sing N N 503 
TYR   CB  CG   sing N N 504 
TYR   CB  HB2  sing N N 505 
TYR   CB  HB3  sing N N 506 
TYR   CG  CD1  doub Y N 507 
TYR   CG  CD2  sing Y N 508 
TYR   CD1 CE1  sing Y N 509 
TYR   CD1 HD1  sing N N 510 
TYR   CD2 CE2  doub Y N 511 
TYR   CD2 HD2  sing N N 512 
TYR   CE1 CZ   doub Y N 513 
TYR   CE1 HE1  sing N N 514 
TYR   CE2 CZ   sing Y N 515 
TYR   CE2 HE2  sing N N 516 
TYR   CZ  OH   sing N N 517 
TYR   OH  HH   sing N N 518 
TYR   OXT HXT  sing N N 519 
VAL   N   CA   sing N N 520 
VAL   N   H    sing N N 521 
VAL   N   H2   sing N N 522 
VAL   CA  C    sing N N 523 
VAL   CA  CB   sing N N 524 
VAL   CA  HA   sing N N 525 
VAL   C   O    doub N N 526 
VAL   C   OXT  sing N N 527 
VAL   CB  CG1  sing N N 528 
VAL   CB  CG2  sing N N 529 
VAL   CB  HB   sing N N 530 
VAL   CG1 HG11 sing N N 531 
VAL   CG1 HG12 sing N N 532 
VAL   CG1 HG13 sing N N 533 
VAL   CG2 HG21 sing N N 534 
VAL   CG2 HG22 sing N N 535 
VAL   CG2 HG23 sing N N 536 
VAL   OXT HXT  sing N N 537 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-10-17 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9DZU 
_em_admin.last_update        2025-05-21 
_em_admin.map_release_date   2025-02-05 
_em_admin.title              
'Cryo-EM structure of the C. neoformans lipid flippase Apt1-Cdc50 bound with butyrolactol A in the E2P state' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.222 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          235443 
_em_entity_assembly_naturalsource.organism             'Cryptococcus neoformans var. grubii H99' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          4932 
_em_entity_assembly_recombinant.organism             'Saccharomyces cerevisiae' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         60 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'MODEL REFINEMENT'              ? 1  ? ? ? PHENIX 1.20.1_4487: 
'IMAGE ACQUISITION'             ? 2  1 1 1 ?      ?            
'PARTICLE SELECTION'            ? 3  1 1 1 ?      ?            
'VOLUME SELECTION'              ? 4  1 1 1 ?      ?            
CLASSIFICATION                  ? 5  1 1 1 ?      ?            
MASKING                         ? 6  1 1 1 ?      ?            
RECONSTRUCTION                  ? 7  1 1 1 ?      ?            
'INITIAL EULER ASSIGNMENT'      ? 8  1 1 1 ?      ?            
'FINAL EULER ASSIGNMENT'        ? 9  1 1 1 ?      ?            
'CTF CORRECTION'                ? 10 1 1 1 ?      ?            
'LAYERLINE INDEXING'            ? 11 1 1 1 ?      ?            
'DIFFRACTION INDEXING'          ? 12 1 1 1 ?      ?            
'MODEL FITTING'                 ? 13 1 1 1 ?      ?            
'SERIES ALIGNMENT'              ? 14 1 1 1 ?      ?            
'MOLECULAR REPLACEMENT'         ? 15 1 1 1 ?      ?            
'LATTICE DISTORTION CORRECTION' ? 16 1 1 1 ?      ?            
'SYMMETRY DETERMINATION'        ? 17 1 1 1 ?      ?            
'CRYSTALLOGRAPHY MERGING'       ? 18 1 1 1 ?      ?            
OTHER                           ? 19 1 1 1 ?      ?            
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health/National Cancer Institute (NIH/NCI)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           CA231466 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
3 NAG 1 n 
3 NAG 2 n 
4 NAG 1 n 
4 NAG 2 n 
4 BMA 3 n 
4 MAN 4 n 
4 MAN 5 n 
4 MAN 6 n 
# 
_atom_sites.entry_id                    9DZU 
_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]   1.000000 
_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]   1.000000 
_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]   1.000000 
_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 
BE 
C  
F  
MG 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . THR   A 1 48   ? 126.869 97.817  127.459 1.00 84.64  ? 48   THR   B N   1 
ATOM   2     C  CA  . THR   A 1 48   ? 127.001 99.010  128.291 1.00 84.66  ? 48   THR   B CA  1 
ATOM   3     C  C   . THR   A 1 48   ? 126.448 98.821  129.717 1.00 85.62  ? 48   THR   B C   1 
ATOM   4     O  O   . THR   A 1 48   ? 127.113 99.218  130.674 1.00 87.14  ? 48   THR   B O   1 
ATOM   5     C  CB  . THR   A 1 48   ? 126.319 100.232 127.632 1.00 87.32  ? 48   THR   B CB  1 
ATOM   6     O  OG1 . THR   A 1 48   ? 126.834 100.411 126.307 1.00 85.07  ? 48   THR   B OG1 1 
ATOM   7     C  CG2 . THR   A 1 48   ? 126.578 101.492 128.442 1.00 84.82  ? 48   THR   B CG2 1 
ATOM   8     N  N   . PRO   A 1 49   ? 125.255 98.227  129.879 1.00 82.97  ? 49   PRO   B N   1 
ATOM   9     C  CA  . PRO   A 1 49   ? 124.779 97.962  131.248 1.00 83.42  ? 49   PRO   B CA  1 
ATOM   10    C  C   . PRO   A 1 49   ? 125.698 97.044  132.030 1.00 79.79  ? 49   PRO   B C   1 
ATOM   11    O  O   . PRO   A 1 49   ? 125.691 97.080  133.269 1.00 84.51  ? 49   PRO   B O   1 
ATOM   12    C  CB  . PRO   A 1 49   ? 123.398 97.329  131.024 1.00 80.23  ? 49   PRO   B CB  1 
ATOM   13    C  CG  . PRO   A 1 49   ? 122.968 97.837  129.712 1.00 80.43  ? 49   PRO   B CG  1 
ATOM   14    C  CD  . PRO   A 1 49   ? 124.218 97.876  128.891 1.00 82.21  ? 49   PRO   B CD  1 
ATOM   15    N  N   . LYS   A 1 50   ? 126.487 96.217  131.340 1.00 76.03  ? 50   LYS   B N   1 
ATOM   16    C  CA  . LYS   A 1 50   ? 127.519 95.431  132.003 1.00 85.00  ? 50   LYS   B CA  1 
ATOM   17    C  C   . LYS   A 1 50   ? 128.537 96.318  132.706 1.00 87.09  ? 50   LYS   B C   1 
ATOM   18    O  O   . LYS   A 1 50   ? 129.182 95.870  133.660 1.00 87.92  ? 50   LYS   B O   1 
ATOM   19    C  CB  . LYS   A 1 50   ? 128.216 94.525  130.984 1.00 87.50  ? 50   LYS   B CB  1 
ATOM   20    C  CG  . LYS   A 1 50   ? 129.205 93.534  131.580 1.00 88.06  ? 50   LYS   B CG  1 
ATOM   21    C  CD  . LYS   A 1 50   ? 128.516 92.559  132.520 1.00 88.11  ? 50   LYS   B CD  1 
ATOM   22    C  CE  . LYS   A 1 50   ? 129.507 91.570  133.111 1.00 86.78  ? 50   LYS   B CE  1 
ATOM   23    N  NZ  . LYS   A 1 50   ? 130.192 90.771  132.058 1.00 86.18  ? 50   LYS   B NZ  1 
ATOM   24    N  N   . SER   A 1 51   ? 128.698 97.561  132.253 1.00 80.74  ? 51   SER   B N   1 
ATOM   25    C  CA  . SER   A 1 51   ? 129.535 98.545  132.924 1.00 77.92  ? 51   SER   B CA  1 
ATOM   26    C  C   . SER   A 1 51   ? 128.725 99.564  133.713 1.00 75.72  ? 51   SER   B C   1 
ATOM   27    O  O   . SER   A 1 51   ? 129.291 100.556 134.181 1.00 77.44  ? 51   SER   B O   1 
ATOM   28    C  CB  . SER   A 1 51   ? 130.424 99.268  131.906 1.00 79.86  ? 51   SER   B CB  1 
ATOM   29    O  OG  . SER   A 1 51   ? 129.643 99.932  130.927 1.00 81.71  ? 51   SER   B OG  1 
ATOM   30    N  N   . VAL   A 1 52   ? 127.423 99.350  133.869 1.00 65.74  ? 52   VAL   B N   1 
ATOM   31    C  CA  . VAL   A 1 52   ? 126.551 100.274 134.585 1.00 67.48  ? 52   VAL   B CA  1 
ATOM   32    C  C   . VAL   A 1 52   ? 126.065 99.678  135.898 1.00 67.92  ? 52   VAL   B C   1 
ATOM   33    O  O   . VAL   A 1 52   ? 126.085 100.342 136.934 1.00 75.34  ? 52   VAL   B O   1 
ATOM   34    C  CB  . VAL   A 1 52   ? 125.366 100.690 133.685 1.00 68.08  ? 52   VAL   B CB  1 
ATOM   35    C  CG1 . VAL   A 1 52   ? 124.280 101.371 134.503 1.00 64.07  ? 52   VAL   B CG1 1 
ATOM   36    C  CG2 . VAL   A 1 52   ? 125.853 101.599 132.572 1.00 68.15  ? 52   VAL   B CG2 1 
ATOM   37    N  N   . LEU   A 1 53   ? 125.617 98.425  135.869 1.00 60.79  ? 53   LEU   B N   1 
ATOM   38    C  CA  . LEU   A 1 53   ? 125.181 97.766  137.099 1.00 60.94  ? 53   LEU   B CA  1 
ATOM   39    C  C   . LEU   A 1 53   ? 126.292 97.660  138.139 1.00 65.74  ? 53   LEU   B C   1 
ATOM   40    O  O   . LEU   A 1 53   ? 126.038 97.980  139.316 1.00 73.42  ? 53   LEU   B O   1 
ATOM   41    C  CB  . LEU   A 1 53   ? 124.588 96.394  136.763 1.00 64.26  ? 53   LEU   B CB  1 
ATOM   42    C  CG  . LEU   A 1 53   ? 123.107 96.301  136.382 1.00 67.91  ? 53   LEU   B CG  1 
ATOM   43    C  CD1 . LEU   A 1 53   ? 122.723 97.293  135.293 1.00 68.35  ? 53   LEU   B CD1 1 
ATOM   44    C  CD2 . LEU   A 1 53   ? 122.788 94.887  135.938 1.00 65.78  ? 53   LEU   B CD2 1 
ATOM   45    N  N   . PRO   A 1 54   ? 127.514 97.226  137.805 1.00 60.98  ? 54   PRO   B N   1 
ATOM   46    C  CA  . PRO   A 1 54   ? 128.582 97.260  138.814 1.00 61.06  ? 54   PRO   B CA  1 
ATOM   47    C  C   . PRO   A 1 54   ? 128.870 98.654  139.328 1.00 65.21  ? 54   PRO   B C   1 
ATOM   48    O  O   . PRO   A 1 54   ? 129.254 98.804  140.491 1.00 69.51  ? 54   PRO   B O   1 
ATOM   49    C  CB  . PRO   A 1 54   ? 129.788 96.668  138.073 1.00 64.33  ? 54   PRO   B CB  1 
ATOM   50    C  CG  . PRO   A 1 54   ? 129.484 96.863  136.641 1.00 67.72  ? 54   PRO   B CG  1 
ATOM   51    C  CD  . PRO   A 1 54   ? 128.007 96.670  136.533 1.00 68.55  ? 54   PRO   B CD  1 
ATOM   52    N  N   . THR   A 1 55   ? 128.695 99.684  138.498 1.00 63.75  ? 55   THR   B N   1 
ATOM   53    C  CA  . THR   A 1 55   ? 128.870 101.050 138.979 1.00 62.00  ? 55   THR   B CA  1 
ATOM   54    C  C   . THR   A 1 55   ? 127.852 101.385 140.062 1.00 61.43  ? 55   THR   B C   1 
ATOM   55    O  O   . THR   A 1 55   ? 128.204 101.973 141.090 1.00 68.18  ? 55   THR   B O   1 
ATOM   56    C  CB  . THR   A 1 55   ? 128.765 102.036 137.817 1.00 65.66  ? 55   THR   B CB  1 
ATOM   57    O  OG1 . THR   A 1 55   ? 129.809 101.773 136.872 1.00 68.51  ? 55   THR   B OG1 1 
ATOM   58    C  CG2 . THR   A 1 55   ? 128.893 103.466 138.318 1.00 66.84  ? 55   THR   B CG2 1 
ATOM   59    N  N   . LEU   A 1 56   ? 126.588 101.007 139.858 1.00 49.79  ? 56   LEU   B N   1 
ATOM   60    C  CA  . LEU   A 1 56   ? 125.575 101.228 140.886 1.00 52.28  ? 56   LEU   B CA  1 
ATOM   61    C  C   . LEU   A 1 56   ? 125.895 100.449 142.155 1.00 60.09  ? 56   LEU   B C   1 
ATOM   62    O  O   . LEU   A 1 56   ? 125.751 100.976 143.267 1.00 67.41  ? 56   LEU   B O   1 
ATOM   63    C  CB  . LEU   A 1 56   ? 124.194 100.841 140.363 1.00 50.42  ? 56   LEU   B CB  1 
ATOM   64    C  CG  . LEU   A 1 56   ? 123.552 101.744 139.312 1.00 59.38  ? 56   LEU   B CG  1 
ATOM   65    C  CD1 . LEU   A 1 56   ? 122.194 101.203 138.912 1.00 55.38  ? 56   LEU   B CD1 1 
ATOM   66    C  CD2 . LEU   A 1 56   ? 123.425 103.154 139.843 1.00 60.38  ? 56   LEU   B CD2 1 
ATOM   67    N  N   . LEU   A 1 57   ? 126.325 99.193  142.012 1.00 51.98  ? 57   LEU   B N   1 
ATOM   68    C  CA  . LEU   A 1 57   ? 126.670 98.402  143.190 1.00 47.00  ? 57   LEU   B CA  1 
ATOM   69    C  C   . LEU   A 1 57   ? 127.825 99.030  143.960 1.00 53.95  ? 57   LEU   B C   1 
ATOM   70    O  O   . LEU   A 1 57   ? 127.787 99.108  145.193 1.00 64.20  ? 57   LEU   B O   1 
ATOM   71    C  CB  . LEU   A 1 57   ? 127.011 96.970  142.786 1.00 51.91  ? 57   LEU   B CB  1 
ATOM   72    C  CG  . LEU   A 1 57   ? 125.828 96.085  142.403 1.00 58.01  ? 57   LEU   B CG  1 
ATOM   73    C  CD1 . LEU   A 1 57   ? 126.305 94.714  141.951 1.00 57.70  ? 57   LEU   B CD1 1 
ATOM   74    C  CD2 . LEU   A 1 57   ? 124.873 95.962  143.573 1.00 61.05  ? 57   LEU   B CD2 1 
ATOM   75    N  N   . ILE   A 1 58   ? 128.859 99.485  143.251 1.00 51.11  ? 58   ILE   B N   1 
ATOM   76    C  CA  . ILE   A 1 58   ? 130.004 100.111 143.906 1.00 48.91  ? 58   ILE   B CA  1 
ATOM   77    C  C   . ILE   A 1 58   ? 129.586 101.406 144.586 1.00 53.88  ? 58   ILE   B C   1 
ATOM   78    O  O   . ILE   A 1 58   ? 130.013 101.700 145.709 1.00 60.56  ? 58   ILE   B O   1 
ATOM   79    C  CB  . ILE   A 1 58   ? 131.140 100.339 142.892 1.00 49.42  ? 58   ILE   B CB  1 
ATOM   80    C  CG1 . ILE   A 1 58   ? 131.737 99.002  142.455 1.00 55.32  ? 58   ILE   B CG1 1 
ATOM   81    C  CG2 . ILE   A 1 58   ? 132.216 101.232 143.479 1.00 51.79  ? 58   ILE   B CG2 1 
ATOM   82    C  CD1 . ILE   A 1 58   ? 132.835 99.132  141.423 1.00 52.63  ? 58   ILE   B CD1 1 
ATOM   83    N  N   . ILE   A 1 59   ? 128.738 102.197 143.924 1.00 51.32  ? 59   ILE   B N   1 
ATOM   84    C  CA  . ILE   A 1 59   ? 128.269 103.446 144.517 1.00 50.33  ? 59   ILE   B CA  1 
ATOM   85    C  C   . ILE   A 1 59   ? 127.521 103.167 145.812 1.00 43.24  ? 59   ILE   B C   1 
ATOM   86    O  O   . ILE   A 1 59   ? 127.736 103.836 146.826 1.00 53.97  ? 59   ILE   B O   1 
ATOM   87    C  CB  . ILE   A 1 59   ? 127.400 104.227 143.515 1.00 53.70  ? 59   ILE   B CB  1 
ATOM   88    C  CG1 . ILE   A 1 59   ? 128.274 104.879 142.443 1.00 54.97  ? 59   ILE   B CG1 1 
ATOM   89    C  CG2 . ILE   A 1 59   ? 126.572 105.279 144.228 1.00 51.16  ? 59   ILE   B CG2 1 
ATOM   90    C  CD1 . ILE   A 1 59   ? 127.492 105.664 141.415 1.00 55.81  ? 59   ILE   B CD1 1 
ATOM   91    N  N   . GLY   A 1 60   ? 126.643 102.163 145.805 1.00 38.88  ? 60   GLY   B N   1 
ATOM   92    C  CA  . GLY   A 1 60   ? 125.908 101.840 147.019 1.00 47.21  ? 60   GLY   B CA  1 
ATOM   93    C  C   . GLY   A 1 60   ? 126.801 101.320 148.131 1.00 44.67  ? 60   GLY   B C   1 
ATOM   94    O  O   . GLY   A 1 60   ? 126.688 101.739 149.289 1.00 55.51  ? 60   GLY   B O   1 
ATOM   95    N  N   . ILE   A 1 61   ? 127.708 100.400 147.791 1.00 37.67  ? 61   ILE   B N   1 
ATOM   96    C  CA  . ILE   A 1 61   ? 128.585 99.787  148.781 1.00 44.75  ? 61   ILE   B CA  1 
ATOM   97    C  C   . ILE   A 1 61   ? 129.586 100.786 149.347 1.00 51.55  ? 61   ILE   B C   1 
ATOM   98    O  O   . ILE   A 1 61   ? 130.072 100.603 150.467 1.00 54.28  ? 61   ILE   B O   1 
ATOM   99    C  CB  . ILE   A 1 61   ? 129.282 98.560  148.154 1.00 50.83  ? 61   ILE   B CB  1 
ATOM   100   C  CG1 . ILE   A 1 61   ? 128.251 97.481  147.823 1.00 52.14  ? 61   ILE   B CG1 1 
ATOM   101   C  CG2 . ILE   A 1 61   ? 130.342 97.978  149.076 1.00 49.75  ? 61   ILE   B CG2 1 
ATOM   102   C  CD1 . ILE   A 1 61   ? 128.839 96.260  147.152 1.00 51.91  ? 61   ILE   B CD1 1 
ATOM   103   N  N   . ILE   A 1 62   ? 129.913 101.844 148.609 1.00 49.31  ? 62   ILE   B N   1 
ATOM   104   C  CA  . ILE   A 1 62   ? 130.757 102.895 149.164 1.00 40.10  ? 62   ILE   B CA  1 
ATOM   105   C  C   . ILE   A 1 62   ? 129.939 103.928 149.938 1.00 49.72  ? 62   ILE   B C   1 
ATOM   106   O  O   . ILE   A 1 62   ? 130.391 104.423 150.975 1.00 56.55  ? 62   ILE   B O   1 
ATOM   107   C  CB  . ILE   A 1 62   ? 131.583 103.560 148.050 1.00 44.58  ? 62   ILE   B CB  1 
ATOM   108   C  CG1 . ILE   A 1 62   ? 132.573 102.560 147.452 1.00 51.15  ? 62   ILE   B CG1 1 
ATOM   109   C  CG2 . ILE   A 1 62   ? 132.323 104.773 148.574 1.00 48.76  ? 62   ILE   B CG2 1 
ATOM   110   C  CD1 . ILE   A 1 62   ? 133.468 103.152 146.385 1.00 51.02  ? 62   ILE   B CD1 1 
ATOM   111   N  N   . PHE   A 1 63   ? 128.731 104.253 149.468 1.00 44.24  ? 63   PHE   B N   1 
ATOM   112   C  CA  . PHE   A 1 63   ? 127.922 105.274 150.122 1.00 37.64  ? 63   PHE   B CA  1 
ATOM   113   C  C   . PHE   A 1 63   ? 127.428 104.815 151.487 1.00 41.99  ? 63   PHE   B C   1 
ATOM   114   O  O   . PHE   A 1 63   ? 127.368 105.617 152.426 1.00 54.26  ? 63   PHE   B O   1 
ATOM   115   C  CB  . PHE   A 1 63   ? 126.739 105.659 149.233 1.00 35.11  ? 63   PHE   B CB  1 
ATOM   116   C  CG  . PHE   A 1 63   ? 127.058 106.723 148.223 1.00 42.80  ? 63   PHE   B CG  1 
ATOM   117   C  CD1 . PHE   A 1 63   ? 128.365 107.103 147.986 1.00 45.34  ? 63   PHE   B CD1 1 
ATOM   118   C  CD2 . PHE   A 1 63   ? 126.047 107.357 147.524 1.00 40.84  ? 63   PHE   B CD2 1 
ATOM   119   C  CE1 . PHE   A 1 63   ? 128.657 108.086 147.063 1.00 48.16  ? 63   PHE   B CE1 1 
ATOM   120   C  CE2 . PHE   A 1 63   ? 126.334 108.341 146.603 1.00 39.29  ? 63   PHE   B CE2 1 
ATOM   121   C  CZ  . PHE   A 1 63   ? 127.639 108.705 146.371 1.00 44.20  ? 63   PHE   B CZ  1 
ATOM   122   N  N   . ALA   A 1 64   ? 127.054 103.542 151.617 1.00 36.60  ? 64   ALA   B N   1 
ATOM   123   C  CA  . ALA   A 1 64   ? 126.485 103.078 152.882 1.00 38.13  ? 64   ALA   B CA  1 
ATOM   124   C  C   . ALA   A 1 64   ? 127.430 103.259 154.067 1.00 47.02  ? 64   ALA   B C   1 
ATOM   125   O  O   . ALA   A 1 64   ? 126.986 103.791 155.101 1.00 51.72  ? 64   ALA   B O   1 
ATOM   126   C  CB  . ALA   A 1 64   ? 126.027 101.623 152.740 1.00 39.41  ? 64   ALA   B CB  1 
ATOM   127   N  N   . PRO   A 1 65   ? 128.705 102.847 154.012 1.00 43.23  ? 65   PRO   B N   1 
ATOM   128   C  CA  . PRO   A 1 65   ? 129.591 103.113 155.158 1.00 36.70  ? 65   PRO   B CA  1 
ATOM   129   C  C   . PRO   A 1 65   ? 129.783 104.588 155.450 1.00 45.66  ? 65   PRO   B C   1 
ATOM   130   O  O   . PRO   A 1 65   ? 129.855 104.974 156.622 1.00 57.14  ? 65   PRO   B O   1 
ATOM   131   C  CB  . PRO   A 1 65   ? 130.909 102.445 154.743 1.00 45.90  ? 65   PRO   B CB  1 
ATOM   132   C  CG  . PRO   A 1 65   ? 130.523 101.435 153.741 1.00 48.31  ? 65   PRO   B CG  1 
ATOM   133   C  CD  . PRO   A 1 65   ? 129.393 102.049 152.987 1.00 48.40  ? 65   PRO   B CD  1 
ATOM   134   N  N   . ILE   A 1 66   ? 129.867 105.428 154.417 1.00 37.10  ? 66   ILE   B N   1 
ATOM   135   C  CA  . ILE   A 1 66   ? 130.050 106.860 154.638 1.00 32.73  ? 66   ILE   B CA  1 
ATOM   136   C  C   . ILE   A 1 66   ? 128.836 107.449 155.343 1.00 40.83  ? 66   ILE   B C   1 
ATOM   137   O  O   . ILE   A 1 66   ? 128.967 108.239 156.287 1.00 53.14  ? 66   ILE   B O   1 
ATOM   138   C  CB  . ILE   A 1 66   ? 130.334 107.575 153.304 1.00 39.35  ? 66   ILE   B CB  1 
ATOM   139   C  CG1 . ILE   A 1 66   ? 131.655 107.087 152.712 1.00 43.39  ? 66   ILE   B CG1 1 
ATOM   140   C  CG2 . ILE   A 1 66   ? 130.367 109.080 153.502 1.00 46.73  ? 66   ILE   B CG2 1 
ATOM   141   C  CD1 . ILE   A 1 66   ? 132.038 107.776 151.424 1.00 44.58  ? 66   ILE   B CD1 1 
ATOM   142   N  N   . GLY   A 1 67   ? 127.637 107.068 154.904 1.00 42.20  ? 67   GLY   B N   1 
ATOM   143   C  CA  . GLY   A 1 67   ? 126.436 107.547 155.565 1.00 45.02  ? 67   GLY   B CA  1 
ATOM   144   C  C   . GLY   A 1 67   ? 126.317 107.050 156.991 1.00 44.40  ? 67   GLY   B C   1 
ATOM   145   O  O   . GLY   A 1 67   ? 125.921 107.798 157.888 1.00 51.65  ? 67   GLY   B O   1 
ATOM   146   N  N   . ALA   A 1 68   ? 126.657 105.780 157.219 1.00 38.63  ? 68   ALA   B N   1 
ATOM   147   C  CA  . ALA   A 1 68   ? 126.633 105.249 158.576 1.00 34.81  ? 68   ALA   B CA  1 
ATOM   148   C  C   . ALA   A 1 68   ? 127.616 105.991 159.470 1.00 40.71  ? 68   ALA   B C   1 
ATOM   149   O  O   . ALA   A 1 68   ? 127.303 106.305 160.623 1.00 53.58  ? 68   ALA   B O   1 
ATOM   150   C  CB  . ALA   A 1 68   ? 126.941 103.752 158.561 1.00 39.16  ? 68   ALA   B CB  1 
ATOM   151   N  N   . LEU   A 1 69   ? 128.806 106.290 158.948 1.00 32.94  ? 69   LEU   B N   1 
ATOM   152   C  CA  . LEU   A 1 69   ? 129.804 107.015 159.723 1.00 30.20  ? 69   LEU   B CA  1 
ATOM   153   C  C   . LEU   A 1 69   ? 129.338 108.430 160.042 1.00 38.79  ? 69   LEU   B C   1 
ATOM   154   O  O   . LEU   A 1 69   ? 129.536 108.915 161.162 1.00 48.66  ? 69   LEU   B O   1 
ATOM   155   C  CB  . LEU   A 1 69   ? 131.127 107.036 158.960 1.00 35.99  ? 69   LEU   B CB  1 
ATOM   156   C  CG  . LEU   A 1 69   ? 132.415 107.126 159.774 1.00 46.26  ? 69   LEU   B CG  1 
ATOM   157   C  CD1 . LEU   A 1 69   ? 132.531 105.940 160.716 1.00 48.94  ? 69   LEU   B CD1 1 
ATOM   158   C  CD2 . LEU   A 1 69   ? 133.617 107.197 158.849 1.00 39.39  ? 69   LEU   B CD2 1 
ATOM   159   N  N   . ILE   A 1 70   ? 128.716 109.107 159.075 1.00 37.17  ? 70   ILE   B N   1 
ATOM   160   C  CA  . ILE   A 1 70   ? 128.214 110.455 159.323 1.00 29.69  ? 70   ILE   B CA  1 
ATOM   161   C  C   . ILE   A 1 70   ? 127.102 110.432 160.366 1.00 37.03  ? 70   ILE   B C   1 
ATOM   162   O  O   . ILE   A 1 70   ? 127.056 111.286 161.262 1.00 50.77  ? 70   ILE   B O   1 
ATOM   163   C  CB  . ILE   A 1 70   ? 127.749 111.106 158.009 1.00 37.16  ? 70   ILE   B CB  1 
ATOM   164   C  CG1 . ILE   A 1 70   ? 128.942 111.364 157.089 1.00 40.46  ? 70   ILE   B CG1 1 
ATOM   165   C  CG2 . ILE   A 1 70   ? 127.011 112.401 158.285 1.00 43.18  ? 70   ILE   B CG2 1 
ATOM   166   C  CD1 . ILE   A 1 70   ? 128.565 112.012 155.779 1.00 42.55  ? 70   ILE   B CD1 1 
ATOM   167   N  N   . VAL   A 1 71   ? 126.190 109.462 160.270 1.00 36.96  ? 71   VAL   B N   1 
ATOM   168   C  CA  . VAL   A 1 71   ? 125.114 109.347 161.251 1.00 33.88  ? 71   VAL   B CA  1 
ATOM   169   C  C   . VAL   A 1 71   ? 125.680 109.074 162.637 1.00 35.26  ? 71   VAL   B C   1 
ATOM   170   O  O   . VAL   A 1 71   ? 125.231 109.651 163.633 1.00 48.97  ? 71   VAL   B O   1 
ATOM   171   C  CB  . VAL   A 1 71   ? 124.113 108.260 160.819 1.00 35.43  ? 71   VAL   B CB  1 
ATOM   172   C  CG1 . VAL   A 1 71   ? 123.148 107.948 161.943 1.00 37.67  ? 71   VAL   B CG1 1 
ATOM   173   C  CG2 . VAL   A 1 71   ? 123.354 108.706 159.589 1.00 39.72  ? 71   VAL   B CG2 1 
ATOM   174   N  N   . TRP   A 1 72   ? 126.676 108.192 162.722 1.00 28.00  ? 72   TRP   B N   1 
ATOM   175   C  CA  . TRP   A 1 72   ? 127.311 107.881 163.998 1.00 36.89  ? 72   TRP   B CA  1 
ATOM   176   C  C   . TRP   A 1 72   ? 127.975 109.115 164.601 1.00 49.50  ? 72   TRP   B C   1 
ATOM   177   O  O   . TRP   A 1 72   ? 127.809 109.412 165.793 1.00 52.69  ? 72   TRP   B O   1 
ATOM   178   C  CB  . TRP   A 1 72   ? 128.320 106.753 163.775 1.00 34.82  ? 72   TRP   B CB  1 
ATOM   179   C  CG  . TRP   A 1 72   ? 129.178 106.394 164.932 1.00 37.40  ? 72   TRP   B CG  1 
ATOM   180   C  CD1 . TRP   A 1 72   ? 128.803 105.719 166.052 1.00 41.25  ? 72   TRP   B CD1 1 
ATOM   181   C  CD2 . TRP   A 1 72   ? 130.579 106.649 165.065 1.00 46.76  ? 72   TRP   B CD2 1 
ATOM   182   N  NE1 . TRP   A 1 72   ? 129.880 105.556 166.887 1.00 53.65  ? 72   TRP   B NE1 1 
ATOM   183   C  CE2 . TRP   A 1 72   ? 130.983 106.118 166.302 1.00 50.51  ? 72   TRP   B CE2 1 
ATOM   184   C  CE3 . TRP   A 1 72   ? 131.529 107.286 164.263 1.00 41.42  ? 72   TRP   B CE3 1 
ATOM   185   C  CZ2 . TRP   A 1 72   ? 132.294 106.204 166.757 1.00 47.20  ? 72   TRP   B CZ2 1 
ATOM   186   C  CZ3 . TRP   A 1 72   ? 132.828 107.370 164.714 1.00 41.19  ? 72   TRP   B CZ3 1 
ATOM   187   C  CH2 . TRP   A 1 72   ? 133.200 106.833 165.949 1.00 46.30  ? 72   TRP   B CH2 1 
ATOM   188   N  N   . GLY   A 1 73   ? 128.710 109.866 163.778 1.00 47.75  ? 73   GLY   B N   1 
ATOM   189   C  CA  . GLY   A 1 73   ? 129.352 111.074 164.268 1.00 40.22  ? 73   GLY   B CA  1 
ATOM   190   C  C   . GLY   A 1 73   ? 128.358 112.118 164.736 1.00 41.28  ? 73   GLY   B C   1 
ATOM   191   O  O   . GLY   A 1 73   ? 128.569 112.773 165.759 1.00 47.82  ? 73   GLY   B O   1 
ATOM   192   N  N   . SER   A 1 74   ? 127.264 112.292 163.992 1.00 37.42  ? 74   SER   B N   1 
ATOM   193   C  CA  . SER   A 1 74   ? 126.230 113.230 164.416 1.00 36.74  ? 74   SER   B CA  1 
ATOM   194   C  C   . SER   A 1 74   ? 125.572 112.776 165.711 1.00 44.14  ? 74   SER   B C   1 
ATOM   195   O  O   . SER   A 1 74   ? 125.255 113.601 166.576 1.00 57.69  ? 74   SER   B O   1 
ATOM   196   C  CB  . SER   A 1 74   ? 125.184 113.397 163.316 1.00 42.22  ? 74   SER   B CB  1 
ATOM   197   O  OG  . SER   A 1 74   ? 124.193 114.332 163.702 1.00 52.56  ? 74   SER   B OG  1 
ATOM   198   N  N   . GLY   A 1 75   ? 125.354 111.469 165.862 1.00 38.74  ? 75   GLY   B N   1 
ATOM   199   C  CA  . GLY   A 1 75   ? 124.751 110.950 167.073 1.00 36.32  ? 75   GLY   B CA  1 
ATOM   200   C  C   . GLY   A 1 75   ? 125.670 110.967 168.271 1.00 45.22  ? 75   GLY   B C   1 
ATOM   201   O  O   . GLY   A 1 75   ? 125.200 110.802 169.400 1.00 54.93  ? 75   GLY   B O   1 
ATOM   202   N  N   . LYS   A 1 76   ? 126.968 111.153 168.055 1.00 40.35  ? 76   LYS   B N   1 
ATOM   203   C  CA  . LYS   A 1 76   ? 127.896 111.321 169.168 1.00 33.95  ? 76   LYS   B CA  1 
ATOM   204   C  C   . LYS   A 1 76   ? 127.901 112.738 169.739 1.00 44.98  ? 76   LYS   B C   1 
ATOM   205   O  O   . LYS   A 1 76   ? 128.779 113.056 170.547 1.00 54.20  ? 76   LYS   B O   1 
ATOM   206   C  CB  . LYS   A 1 76   ? 129.310 110.936 168.733 1.00 41.06  ? 76   LYS   B CB  1 
ATOM   207   C  CG  . LYS   A 1 76   ? 129.873 109.744 169.479 1.00 47.50  ? 76   LYS   B CG  1 
ATOM   208   C  CD  . LYS   A 1 76   ? 131.217 109.321 168.921 1.00 49.41  ? 76   LYS   B CD  1 
ATOM   209   C  CE  . LYS   A 1 76   ? 131.814 108.194 169.745 1.00 52.75  ? 76   LYS   B CE  1 
ATOM   210   N  NZ  . LYS   A 1 76   ? 130.894 107.026 169.833 1.00 48.81  ? 76   LYS   B NZ  1 
ATOM   211   N  N   . VAL   A 1 77   ? 126.947 113.586 169.357 1.00 44.02  ? 77   VAL   B N   1 
ATOM   212   C  CA  . VAL   A 1 77   ? 126.920 114.990 169.748 1.00 37.56  ? 77   VAL   B CA  1 
ATOM   213   C  C   . VAL   A 1 77   ? 125.682 115.245 170.595 1.00 48.59  ? 77   VAL   B C   1 
ATOM   214   O  O   . VAL   A 1 77   ? 124.625 114.648 170.364 1.00 55.37  ? 77   VAL   B O   1 
ATOM   215   C  CB  . VAL   A 1 77   ? 126.936 115.919 168.515 1.00 39.20  ? 77   VAL   B CB  1 
ATOM   216   C  CG1 . VAL   A 1 77   ? 127.091 117.369 168.933 1.00 46.99  ? 77   VAL   B CG1 1 
ATOM   217   C  CG2 . VAL   A 1 77   ? 128.046 115.519 167.568 1.00 42.85  ? 77   VAL   B CG2 1 
ATOM   218   N  N   . THR   A 1 78   ? 125.816 116.132 171.578 1.00 44.67  ? 78   THR   B N   1 
ATOM   219   C  CA  . THR   A 1 78   ? 124.721 116.527 172.452 1.00 38.25  ? 78   THR   B CA  1 
ATOM   220   C  C   . THR   A 1 78   ? 124.445 118.016 172.296 1.00 44.95  ? 78   THR   B C   1 
ATOM   221   O  O   . THR   A 1 78   ? 125.368 118.834 172.337 1.00 46.51  ? 78   THR   B O   1 
ATOM   222   C  CB  . THR   A 1 78   ? 125.044 116.211 173.914 1.00 43.02  ? 78   THR   B CB  1 
ATOM   223   O  OG1 . THR   A 1 78   ? 125.225 114.798 174.069 1.00 55.55  ? 78   THR   B OG1 1 
ATOM   224   C  CG2 . THR   A 1 78   ? 123.921 116.676 174.823 1.00 38.36  ? 78   THR   B CG2 1 
ATOM   225   N  N   . THR   A 1 79   ? 123.172 118.363 172.115 1.00 49.19  ? 79   THR   B N   1 
ATOM   226   C  CA  . THR   A 1 79   ? 122.753 119.744 171.914 1.00 40.51  ? 79   THR   B CA  1 
ATOM   227   C  C   . THR   A 1 79   ? 121.629 120.081 172.881 1.00 47.47  ? 79   THR   B C   1 
ATOM   228   O  O   . THR   A 1 79   ? 120.660 119.325 172.999 1.00 59.02  ? 79   THR   B O   1 
ATOM   229   C  CB  . THR   A 1 79   ? 122.295 119.979 170.471 1.00 51.58  ? 79   THR   B CB  1 
ATOM   230   O  OG1 . THR   A 1 79   ? 123.362 119.661 169.570 1.00 63.91  ? 79   THR   B OG1 1 
ATOM   231   C  CG2 . THR   A 1 79   ? 121.887 121.425 170.267 1.00 48.40  ? 79   THR   B CG2 1 
ATOM   232   N  N   . ILE   A 1 80   ? 121.760 121.213 173.568 1.00 44.32  ? 80   ILE   B N   1 
ATOM   233   C  CA  . ILE   A 1 80   ? 120.727 121.735 174.457 1.00 38.85  ? 80   ILE   B CA  1 
ATOM   234   C  C   . ILE   A 1 80   ? 120.312 123.102 173.935 1.00 47.89  ? 80   ILE   B C   1 
ATOM   235   O  O   . ILE   A 1 80   ? 121.158 123.987 173.762 1.00 55.78  ? 80   ILE   B O   1 
ATOM   236   C  CB  . ILE   A 1 80   ? 121.216 121.831 175.909 1.00 36.27  ? 80   ILE   B CB  1 
ATOM   237   C  CG1 . ILE   A 1 80   ? 121.740 120.479 176.385 1.00 43.64  ? 80   ILE   B CG1 1 
ATOM   238   C  CG2 . ILE   A 1 80   ? 120.099 122.317 176.809 1.00 43.92  ? 80   ILE   B CG2 1 
ATOM   239   C  CD1 . ILE   A 1 80   ? 122.332 120.513 177.771 1.00 43.83  ? 80   ILE   B CD1 1 
ATOM   240   N  N   . THR   A 1 81   ? 119.018 123.275 173.687 1.00 49.17  ? 81   THR   B N   1 
ATOM   241   C  CA  . THR   A 1 81   ? 118.468 124.521 173.171 1.00 43.97  ? 81   THR   B CA  1 
ATOM   242   C  C   . THR   A 1 81   ? 117.503 125.108 174.191 1.00 52.34  ? 81   THR   B C   1 
ATOM   243   O  O   . THR   A 1 81   ? 116.642 124.396 174.716 1.00 60.61  ? 81   THR   B O   1 
ATOM   244   C  CB  . THR   A 1 81   ? 117.757 124.301 171.834 1.00 48.57  ? 81   THR   B CB  1 
ATOM   245   O  OG1 . THR   A 1 81   ? 118.689 123.792 170.874 1.00 53.53  ? 81   THR   B OG1 1 
ATOM   246   C  CG2 . THR   A 1 81   ? 117.177 125.605 171.317 1.00 49.08  ? 81   THR   B CG2 1 
ATOM   247   N  N   . LEU   A 1 82   ? 117.656 126.400 174.475 1.00 39.65  ? 82   LEU   B N   1 
ATOM   248   C  CA  . LEU   A 1 82   ? 116.816 127.108 175.436 1.00 31.36  ? 82   LEU   B CA  1 
ATOM   249   C  C   . LEU   A 1 82   ? 116.327 128.395 174.789 1.00 49.42  ? 82   LEU   B C   1 
ATOM   250   O  O   . LEU   A 1 82   ? 117.126 129.294 174.508 1.00 58.00  ? 82   LEU   B O   1 
ATOM   251   C  CB  . LEU   A 1 82   ? 117.584 127.405 176.722 1.00 37.99  ? 82   LEU   B CB  1 
ATOM   252   C  CG  . LEU   A 1 82   ? 118.223 126.218 177.437 1.00 35.32  ? 82   LEU   B CG  1 
ATOM   253   C  CD1 . LEU   A 1 82   ? 119.085 126.702 178.582 1.00 47.60  ? 82   LEU   B CD1 1 
ATOM   254   C  CD2 . LEU   A 1 82   ? 117.159 125.264 177.939 1.00 38.54  ? 82   LEU   B CD2 1 
ATOM   255   N  N   . ASP   A 1 83   ? 115.021 128.487 174.558 1.00 53.79  ? 83   ASP   B N   1 
ATOM   256   C  CA  . ASP   A 1 83   ? 114.416 129.655 173.926 1.00 42.64  ? 83   ASP   B CA  1 
ATOM   257   C  C   . ASP   A 1 83   ? 113.958 130.618 175.016 1.00 46.28  ? 83   ASP   B C   1 
ATOM   258   O  O   . ASP   A 1 83   ? 112.959 130.367 175.697 1.00 51.79  ? 83   ASP   B O   1 
ATOM   259   C  CB  . ASP   A 1 83   ? 113.254 129.234 173.031 1.00 47.05  ? 83   ASP   B CB  1 
ATOM   260   C  CG  . ASP   A 1 83   ? 112.701 130.379 172.209 1.00 54.92  ? 83   ASP   B CG  1 
ATOM   261   O  OD1 . ASP   A 1 83   ? 113.321 131.462 172.198 1.00 54.40  ? 83   ASP   B OD1 1 
ATOM   262   O  OD2 . ASP   A 1 83   ? 111.644 130.195 171.572 1.00 55.36  ? 83   ASP   B OD2 1 
ATOM   263   N  N   . TYR   A 1 84   ? 114.688 131.722 175.179 1.00 40.51  ? 84   TYR   B N   1 
ATOM   264   C  CA  . TYR   A 1 84   ? 114.417 132.706 176.219 1.00 42.14  ? 84   TYR   B CA  1 
ATOM   265   C  C   . TYR   A 1 84   ? 113.804 133.984 175.660 1.00 53.49  ? 84   TYR   B C   1 
ATOM   266   O  O   . TYR   A 1 84   ? 113.845 135.027 176.319 1.00 55.36  ? 84   TYR   B O   1 
ATOM   267   C  CB  . TYR   A 1 84   ? 115.697 133.026 176.992 1.00 45.13  ? 84   TYR   B CB  1 
ATOM   268   C  CG  . TYR   A 1 84   ? 116.740 133.768 176.190 1.00 39.49  ? 84   TYR   B CG  1 
ATOM   269   C  CD1 . TYR   A 1 84   ? 117.460 133.129 175.193 1.00 44.11  ? 84   TYR   B CD1 1 
ATOM   270   C  CD2 . TYR   A 1 84   ? 117.013 135.102 176.440 1.00 41.97  ? 84   TYR   B CD2 1 
ATOM   271   C  CE1 . TYR   A 1 84   ? 118.411 133.802 174.460 1.00 44.00  ? 84   TYR   B CE1 1 
ATOM   272   C  CE2 . TYR   A 1 84   ? 117.966 135.781 175.713 1.00 46.17  ? 84   TYR   B CE2 1 
ATOM   273   C  CZ  . TYR   A 1 84   ? 118.661 135.125 174.725 1.00 42.39  ? 84   TYR   B CZ  1 
ATOM   274   O  OH  . TYR   A 1 84   ? 119.611 135.796 173.996 1.00 48.41  ? 84   TYR   B OH  1 
ATOM   275   N  N   . THR   A 1 85   ? 113.238 133.922 174.454 1.00 54.51  ? 85   THR   B N   1 
ATOM   276   C  CA  . THR   A 1 85   ? 112.644 135.107 173.847 1.00 47.75  ? 85   THR   B CA  1 
ATOM   277   C  C   . THR   A 1 85   ? 111.458 135.613 174.657 1.00 54.99  ? 85   THR   B C   1 
ATOM   278   O  O   . THR   A 1 85   ? 111.311 136.823 174.864 1.00 63.31  ? 85   THR   B O   1 
ATOM   279   C  CB  . THR   A 1 85   ? 112.217 134.799 172.415 1.00 49.28  ? 85   THR   B CB  1 
ATOM   280   O  OG1 . THR   A 1 85   ? 113.318 134.220 171.705 1.00 58.71  ? 85   THR   B OG1 1 
ATOM   281   C  CG2 . THR   A 1 85   ? 111.778 136.065 171.706 1.00 53.29  ? 85   THR   B CG2 1 
ATOM   282   N  N   . GLU   A 1 86   ? 110.606 134.706 175.125 1.00 47.54  ? 86   GLU   B N   1 
ATOM   283   C  CA  . GLU   A 1 86   ? 109.409 135.067 175.869 1.00 48.64  ? 86   GLU   B CA  1 
ATOM   284   C  C   . GLU   A 1 86   ? 109.647 135.140 177.370 1.00 52.59  ? 86   GLU   B C   1 
ATOM   285   O  O   . GLU   A 1 86   ? 108.686 135.076 178.141 1.00 64.04  ? 86   GLU   B O   1 
ATOM   286   C  CB  . GLU   A 1 86   ? 108.286 134.074 175.569 1.00 49.87  ? 86   GLU   B CB  1 
ATOM   287   C  CG  . GLU   A 1 86   ? 107.898 134.000 174.103 1.00 59.19  ? 86   GLU   B CG  1 
ATOM   288   C  CD  . GLU   A 1 86   ? 107.200 135.253 173.616 1.00 62.62  ? 86   GLU   B CD  1 
ATOM   289   O  OE1 . GLU   A 1 86   ? 106.704 136.029 174.459 1.00 65.99  ? 86   GLU   B OE1 1 
ATOM   290   O  OE2 . GLU   A 1 86   ? 107.145 135.463 172.386 1.00 62.55  ? 86   GLU   B OE2 1 
ATOM   291   N  N   . CYS   A 1 87   ? 110.902 135.269 177.801 1.00 46.23  ? 87   CYS   B N   1 
ATOM   292   C  CA  . CYS   A 1 87   ? 111.197 135.377 179.223 1.00 48.05  ? 87   CYS   B CA  1 
ATOM   293   C  C   . CYS   A 1 87   ? 110.768 136.718 179.800 1.00 59.63  ? 87   CYS   B C   1 
ATOM   294   O  O   . CYS   A 1 87   ? 110.643 136.841 181.022 1.00 64.21  ? 87   CYS   B O   1 
ATOM   295   C  CB  . CYS   A 1 87   ? 112.691 135.149 179.454 1.00 49.63  ? 87   CYS   B CB  1 
ATOM   296   S  SG  . CYS   A 1 87   ? 113.205 134.963 181.172 1.00 68.01  ? 87   CYS   B SG  1 
ATOM   297   N  N   . ASP   A 1 88   ? 110.537 137.721 178.950 1.00 63.11  ? 88   ASP   B N   1 
ATOM   298   C  CA  . ASP   A 1 88   ? 110.133 139.037 179.437 1.00 57.79  ? 88   ASP   B CA  1 
ATOM   299   C  C   . ASP   A 1 88   ? 108.768 138.990 180.110 1.00 62.54  ? 88   ASP   B C   1 
ATOM   300   O  O   . ASP   A 1 88   ? 108.562 139.612 181.157 1.00 68.64  ? 88   ASP   B O   1 
ATOM   301   C  CB  . ASP   A 1 88   ? 110.115 140.039 178.285 1.00 59.10  ? 88   ASP   B CB  1 
ATOM   302   C  CG  . ASP   A 1 88   ? 111.485 140.270 177.692 1.00 67.21  ? 88   ASP   B CG  1 
ATOM   303   O  OD1 . ASP   A 1 88   ? 112.461 140.361 178.465 1.00 71.76  ? 88   ASP   B OD1 1 
ATOM   304   O  OD2 . ASP   A 1 88   ? 111.586 140.363 176.451 1.00 67.76  ? 88   ASP   B OD2 1 
ATOM   305   N  N   . VAL   A 1 89   ? 107.822 138.262 179.523 1.00 53.48  ? 89   VAL   B N   1 
ATOM   306   C  CA  . VAL   A 1 89   ? 106.440 138.298 179.978 1.00 57.05  ? 89   VAL   B CA  1 
ATOM   307   C  C   . VAL   A 1 89   ? 105.955 136.975 180.554 1.00 58.12  ? 89   VAL   B C   1 
ATOM   308   O  O   . VAL   A 1 89   ? 105.056 136.987 181.410 1.00 63.72  ? 89   VAL   B O   1 
ATOM   309   C  CB  . VAL   A 1 89   ? 105.502 138.755 178.842 1.00 58.27  ? 89   VAL   B CB  1 
ATOM   310   C  CG1 . VAL   A 1 89   ? 105.762 140.210 178.498 1.00 59.32  ? 89   VAL   B CG1 1 
ATOM   311   C  CG2 . VAL   A 1 89   ? 105.691 137.880 177.618 1.00 55.61  ? 89   VAL   B CG2 1 
ATOM   312   N  N   . ASP   A 1 90   ? 106.497 135.837 180.132 1.00 54.56  ? 90   ASP   B N   1 
ATOM   313   C  CA  . ASP   A 1 90   ? 106.013 134.538 180.578 1.00 52.13  ? 90   ASP   B CA  1 
ATOM   314   C  C   . ASP   A 1 90   ? 106.786 133.983 181.765 1.00 58.10  ? 90   ASP   B C   1 
ATOM   315   O  O   . ASP   A 1 90   ? 106.474 132.880 182.224 1.00 65.64  ? 90   ASP   B O   1 
ATOM   316   C  CB  . ASP   A 1 90   ? 106.060 133.533 179.424 1.00 60.45  ? 90   ASP   B CB  1 
ATOM   317   C  CG  . ASP   A 1 90   ? 105.122 133.900 178.293 1.00 63.63  ? 90   ASP   B CG  1 
ATOM   318   O  OD1 . ASP   A 1 90   ? 104.408 134.917 178.417 1.00 64.56  ? 90   ASP   B OD1 1 
ATOM   319   O  OD2 . ASP   A 1 90   ? 105.097 133.172 177.278 1.00 64.02  ? 90   ASP   B OD2 1 
ATOM   320   N  N   . ALA   A 1 91   ? 107.774 134.706 182.271 1.00 48.45  ? 91   ALA   B N   1 
ATOM   321   C  CA  . ALA   A 1 91   ? 108.555 134.199 183.384 1.00 48.15  ? 91   ALA   B CA  1 
ATOM   322   C  C   . ALA   A 1 91   ? 108.227 134.958 184.662 1.00 48.30  ? 91   ALA   B C   1 
ATOM   323   O  O   . ALA   A 1 91   ? 107.940 136.159 184.610 1.00 63.33  ? 91   ALA   B O   1 
ATOM   324   C  CB  . ALA   A 1 91   ? 110.057 134.314 183.100 1.00 50.89  ? 91   ALA   B CB  1 
ATOM   325   N  N   . PRO   A 1 92   ? 108.249 134.292 185.814 1.00 39.77  ? 92   PRO   B N   1 
ATOM   326   C  CA  . PRO   A 1 92   ? 107.929 134.981 187.066 1.00 49.48  ? 92   PRO   B CA  1 
ATOM   327   C  C   . PRO   A 1 92   ? 108.951 136.055 187.396 1.00 60.10  ? 92   PRO   B C   1 
ATOM   328   O  O   . PRO   A 1 92   ? 110.139 135.935 187.087 1.00 66.72  ? 92   PRO   B O   1 
ATOM   329   C  CB  . PRO   A 1 92   ? 107.949 133.855 188.106 1.00 55.90  ? 92   PRO   B CB  1 
ATOM   330   C  CG  . PRO   A 1 92   ? 108.804 132.803 187.503 1.00 61.01  ? 92   PRO   B CG  1 
ATOM   331   C  CD  . PRO   A 1 92   ? 108.552 132.869 186.030 1.00 54.48  ? 92   PRO   B CD  1 
ATOM   332   N  N   . THR   A 1 93   ? 108.468 137.118 188.034 1.00 55.52  ? 93   THR   B N   1 
ATOM   333   C  CA  . THR   A 1 93   ? 109.292 138.265 188.384 1.00 50.32  ? 93   THR   B CA  1 
ATOM   334   C  C   . THR   A 1 93   ? 109.514 138.397 189.884 1.00 53.79  ? 93   THR   B C   1 
ATOM   335   O  O   . THR   A 1 93   ? 110.125 139.374 190.325 1.00 57.57  ? 93   THR   B O   1 
ATOM   336   C  CB  . THR   A 1 93   ? 108.662 139.548 187.842 1.00 57.21  ? 93   THR   B CB  1 
ATOM   337   O  OG1 . THR   A 1 93   ? 107.368 139.730 188.429 1.00 62.75  ? 93   THR   B OG1 1 
ATOM   338   C  CG2 . THR   A 1 93   ? 108.518 139.472 186.333 1.00 56.31  ? 93   THR   B CG2 1 
ATOM   339   N  N   . ASP   A 1 94   ? 109.039 137.439 190.674 1.00 65.77  ? 94   ASP   B N   1 
ATOM   340   C  CA  . ASP   A 1 94   ? 109.139 137.500 192.125 1.00 64.63  ? 94   ASP   B CA  1 
ATOM   341   C  C   . ASP   A 1 94   ? 110.343 136.750 192.676 1.00 65.88  ? 94   ASP   B C   1 
ATOM   342   O  O   . ASP   A 1 94   ? 110.483 136.647 193.898 1.00 67.14  ? 94   ASP   B O   1 
ATOM   343   C  CB  . ASP   A 1 94   ? 107.857 136.952 192.760 1.00 64.53  ? 94   ASP   B CB  1 
ATOM   344   C  CG  . ASP   A 1 94   ? 107.411 135.646 192.135 1.00 70.69  ? 94   ASP   B CG  1 
ATOM   345   O  OD1 . ASP   A 1 94   ? 108.080 135.180 191.189 1.00 73.80  ? 94   ASP   B OD1 1 
ATOM   346   O  OD2 . ASP   A 1 94   ? 106.391 135.086 192.588 1.00 71.55  ? 94   ASP   B OD2 1 
ATOM   347   N  N   . GLY   A 1 95   ? 111.210 136.226 191.814 1.00 63.62  ? 95   GLY   B N   1 
ATOM   348   C  CA  . GLY   A 1 95   ? 112.357 135.456 192.240 1.00 61.70  ? 95   GLY   B CA  1 
ATOM   349   C  C   . GLY   A 1 95   ? 112.160 133.957 192.201 1.00 63.33  ? 95   GLY   B C   1 
ATOM   350   O  O   . GLY   A 1 95   ? 113.152 133.218 192.232 1.00 63.09  ? 95   GLY   B O   1 
ATOM   351   N  N   . SER   A 1 96   ? 110.919 133.488 192.134 1.00 56.80  ? 96   SER   B N   1 
ATOM   352   C  CA  . SER   A 1 96   ? 110.664 132.063 192.027 1.00 56.04  ? 96   SER   B CA  1 
ATOM   353   C  C   . SER   A 1 96   ? 110.964 131.576 190.613 1.00 60.22  ? 96   SER   B C   1 
ATOM   354   O  O   . SER   A 1 96   ? 111.168 132.362 189.685 1.00 63.20  ? 96   SER   B O   1 
ATOM   355   C  CB  . SER   A 1 96   ? 109.215 131.746 192.396 1.00 58.74  ? 96   SER   B CB  1 
ATOM   356   O  OG  . SER   A 1 96   ? 108.945 130.363 192.256 1.00 61.27  ? 96   SER   B OG  1 
ATOM   357   N  N   . TYR   A 1 97   ? 110.991 130.257 190.458 1.00 49.11  ? 97   TYR   B N   1 
ATOM   358   C  CA  . TYR   A 1 97   ? 111.269 129.621 189.179 1.00 43.83  ? 97   TYR   B CA  1 
ATOM   359   C  C   . TYR   A 1 97   ? 110.052 128.827 188.729 1.00 51.02  ? 97   TYR   B C   1 
ATOM   360   O  O   . TYR   A 1 97   ? 109.514 128.020 189.495 1.00 55.85  ? 97   TYR   B O   1 
ATOM   361   C  CB  . TYR   A 1 97   ? 112.491 128.708 189.278 1.00 44.77  ? 97   TYR   B CB  1 
ATOM   362   C  CG  . TYR   A 1 97   ? 113.804 129.449 189.363 1.00 49.07  ? 97   TYR   B CG  1 
ATOM   363   C  CD1 . TYR   A 1 97   ? 114.261 129.953 190.570 1.00 51.72  ? 97   TYR   B CD1 1 
ATOM   364   C  CD2 . TYR   A 1 97   ? 114.588 129.641 188.236 1.00 54.08  ? 97   TYR   B CD2 1 
ATOM   365   C  CE1 . TYR   A 1 97   ? 115.458 130.628 190.652 1.00 48.89  ? 97   TYR   B CE1 1 
ATOM   366   C  CE2 . TYR   A 1 97   ? 115.788 130.314 188.308 1.00 51.43  ? 97   TYR   B CE2 1 
ATOM   367   C  CZ  . TYR   A 1 97   ? 116.217 130.806 189.519 1.00 52.20  ? 97   TYR   B CZ  1 
ATOM   368   O  OH  . TYR   A 1 97   ? 117.412 131.479 189.598 1.00 59.05  ? 97   TYR   B OH  1 
ATOM   369   N  N   . GLN   A 1 98   ? 109.624 129.058 187.493 1.00 46.86  ? 98   GLN   B N   1 
ATOM   370   C  CA  . GLN   A 1 98   ? 108.501 128.353 186.899 1.00 41.31  ? 98   GLN   B CA  1 
ATOM   371   C  C   . GLN   A 1 98   ? 108.989 127.546 185.704 1.00 51.73  ? 98   GLN   B C   1 
ATOM   372   O  O   . GLN   A 1 98   ? 109.875 127.980 184.963 1.00 59.82  ? 98   GLN   B O   1 
ATOM   373   C  CB  . GLN   A 1 98   ? 107.403 129.328 186.463 1.00 45.98  ? 98   GLN   B CB  1 
ATOM   374   C  CG  . GLN   A 1 98   ? 106.080 128.672 186.121 1.00 54.50  ? 98   GLN   B CG  1 
ATOM   375   C  CD  . GLN   A 1 98   ? 105.056 129.665 185.615 1.00 57.47  ? 98   GLN   B CD  1 
ATOM   376   O  OE1 . GLN   A 1 98   ? 105.404 130.676 185.007 1.00 57.89  ? 98   GLN   B OE1 1 
ATOM   377   N  NE2 . GLN   A 1 98   ? 103.783 129.383 185.867 1.00 53.97  ? 98   GLN   B NE2 1 
ATOM   378   N  N   . ALA   A 1 99   ? 108.408 126.362 185.529 1.00 47.82  ? 99   ALA   B N   1 
ATOM   379   C  CA  . ALA   A 1 99   ? 108.833 125.473 184.458 1.00 41.41  ? 99   ALA   B CA  1 
ATOM   380   C  C   . ALA   A 1 99   ? 108.594 126.112 183.096 1.00 41.76  ? 99   ALA   B C   1 
ATOM   381   O  O   . ALA   A 1 99   ? 107.532 126.683 182.836 1.00 49.65  ? 99   ALA   B O   1 
ATOM   382   C  CB  . ALA   A 1 99   ? 108.090 124.140 184.552 1.00 50.34  ? 99   ALA   B CB  1 
ATOM   383   N  N   . MET   A 1 100  ? 109.595 126.015 182.228 1.00 38.75  ? 100  MET   B N   1 
ATOM   384   C  CA  . MET   A 1 100  ? 109.482 126.576 180.894 1.00 35.67  ? 100  MET   B CA  1 
ATOM   385   C  C   . MET   A 1 100  ? 108.506 125.756 180.054 1.00 44.70  ? 100  MET   B C   1 
ATOM   386   O  O   . MET   A 1 100  ? 108.333 124.556 180.285 1.00 58.47  ? 100  MET   B O   1 
ATOM   387   C  CB  . MET   A 1 100  ? 110.846 126.612 180.213 1.00 39.63  ? 100  MET   B CB  1 
ATOM   388   C  CG  . MET   A 1 100  ? 111.852 127.514 180.893 1.00 46.33  ? 100  MET   B CG  1 
ATOM   389   S  SD  . MET   A 1 100  ? 113.480 127.451 180.125 1.00 62.66  ? 100  MET   B SD  1 
ATOM   390   C  CE  . MET   A 1 100  ? 113.088 127.913 178.443 1.00 47.97  ? 100  MET   B CE  1 
ATOM   391   N  N   . PRO   A 1 101  ? 107.850 126.381 179.079 1.00 42.01  ? 101  PRO   B N   1 
ATOM   392   C  CA  . PRO   A 1 101  ? 106.957 125.625 178.199 1.00 44.26  ? 101  PRO   B CA  1 
ATOM   393   C  C   . PRO   A 1 101  ? 107.723 124.577 177.407 1.00 47.58  ? 101  PRO   B C   1 
ATOM   394   O  O   . PRO   A 1 101  ? 108.913 124.726 177.122 1.00 54.17  ? 101  PRO   B O   1 
ATOM   395   C  CB  . PRO   A 1 101  ? 106.366 126.701 177.282 1.00 48.88  ? 101  PRO   B CB  1 
ATOM   396   C  CG  . PRO   A 1 101  ? 106.494 127.962 178.056 1.00 51.71  ? 101  PRO   B CG  1 
ATOM   397   C  CD  . PRO   A 1 101  ? 107.765 127.829 178.835 1.00 50.11  ? 101  PRO   B CD  1 
ATOM   398   N  N   . ASN   A 1 102  ? 107.019 123.500 177.057 1.00 46.37  ? 102  ASN   B N   1 
ATOM   399   C  CA  . ASN   A 1 102  ? 107.645 122.395 176.343 1.00 45.59  ? 102  ASN   B CA  1 
ATOM   400   C  C   . ASN   A 1 102  ? 108.194 122.818 174.987 1.00 50.94  ? 102  ASN   B C   1 
ATOM   401   O  O   . ASN   A 1 102  ? 109.088 122.151 174.457 1.00 58.95  ? 102  ASN   B O   1 
ATOM   402   C  CB  . ASN   A 1 102  ? 106.640 121.254 176.172 1.00 48.90  ? 102  ASN   B CB  1 
ATOM   403   C  CG  . ASN   A 1 102  ? 107.307 119.897 176.078 1.00 56.20  ? 102  ASN   B CG  1 
ATOM   404   O  OD1 . ASN   A 1 102  ? 108.503 119.794 175.812 1.00 56.64  ? 102  ASN   B OD1 1 
ATOM   405   N  ND2 . ASN   A 1 102  ? 106.529 118.843 176.295 1.00 57.35  ? 102  ASN   B ND2 1 
ATOM   406   N  N   . SER   A 1 103  ? 107.684 123.908 174.415 1.00 47.12  ? 103  SER   B N   1 
ATOM   407   C  CA  . SER   A 1 103  ? 108.165 124.381 173.124 1.00 44.00  ? 103  SER   B CA  1 
ATOM   408   C  C   . SER   A 1 103  ? 109.339 125.341 173.242 1.00 46.68  ? 103  SER   B C   1 
ATOM   409   O  O   . SER   A 1 103  ? 109.875 125.763 172.212 1.00 55.63  ? 103  SER   B O   1 
ATOM   410   C  CB  . SER   A 1 103  ? 107.027 125.056 172.356 1.00 51.76  ? 103  SER   B CB  1 
ATOM   411   O  OG  . SER   A 1 103  ? 107.466 125.509 171.087 1.00 55.04  ? 103  SER   B OG  1 
ATOM   412   N  N   . ALA   A 1 104  ? 109.749 125.694 174.458 1.00 43.60  ? 104  ALA   B N   1 
ATOM   413   C  CA  . ALA   A 1 104  ? 110.842 126.631 174.669 1.00 41.42  ? 104  ALA   B CA  1 
ATOM   414   C  C   . ALA   A 1 104  ? 112.187 125.955 174.892 1.00 43.73  ? 104  ALA   B C   1 
ATOM   415   O  O   . ALA   A 1 104  ? 113.192 126.655 175.052 1.00 51.44  ? 104  ALA   B O   1 
ATOM   416   C  CB  . ALA   A 1 104  ? 110.531 127.545 175.860 1.00 47.85  ? 104  ALA   B CB  1 
ATOM   417   N  N   . TYR   A 1 105  ? 112.239 124.625 174.915 1.00 45.55  ? 105  TYR   B N   1 
ATOM   418   C  CA  . TYR   A 1 105  ? 113.498 123.915 175.066 1.00 36.74  ? 105  TYR   B CA  1 
ATOM   419   C  C   . TYR   A 1 105  ? 113.460 122.633 174.248 1.00 47.43  ? 105  TYR   B C   1 
ATOM   420   O  O   . TYR   A 1 105  ? 112.394 122.099 173.938 1.00 57.46  ? 105  TYR   B O   1 
ATOM   421   C  CB  . TYR   A 1 105  ? 113.812 123.603 176.536 1.00 42.66  ? 105  TYR   B CB  1 
ATOM   422   C  CG  . TYR   A 1 105  ? 112.814 122.707 177.231 1.00 44.62  ? 105  TYR   B CG  1 
ATOM   423   C  CD1 . TYR   A 1 105  ? 111.702 123.237 177.866 1.00 52.15  ? 105  TYR   B CD1 1 
ATOM   424   C  CD2 . TYR   A 1 105  ? 112.996 121.334 177.272 1.00 46.13  ? 105  TYR   B CD2 1 
ATOM   425   C  CE1 . TYR   A 1 105  ? 110.793 122.425 178.509 1.00 50.78  ? 105  TYR   B CE1 1 
ATOM   426   C  CE2 . TYR   A 1 105  ? 112.093 120.515 177.913 1.00 45.60  ? 105  TYR   B CE2 1 
ATOM   427   C  CZ  . TYR   A 1 105  ? 110.994 121.065 178.530 1.00 49.81  ? 105  TYR   B CZ  1 
ATOM   428   O  OH  . TYR   A 1 105  ? 110.091 120.252 179.170 1.00 57.98  ? 105  TYR   B OH  1 
ATOM   429   N  N   . GLN   A 1 106  ? 114.649 122.147 173.900 1.00 55.01  ? 106  GLN   B N   1 
ATOM   430   C  CA  . GLN   A 1 106  ? 114.767 120.934 173.096 1.00 52.59  ? 106  GLN   B CA  1 
ATOM   431   C  C   . GLN   A 1 106  ? 116.120 120.301 173.385 1.00 53.94  ? 106  GLN   B C   1 
ATOM   432   O  O   . GLN   A 1 106  ? 117.157 120.912 173.115 1.00 58.07  ? 106  GLN   B O   1 
ATOM   433   C  CB  . GLN   A 1 106  ? 114.611 121.249 171.614 1.00 54.03  ? 106  GLN   B CB  1 
ATOM   434   C  CG  . GLN   A 1 106  ? 114.609 120.025 170.717 1.00 58.85  ? 106  GLN   B CG  1 
ATOM   435   C  CD  . GLN   A 1 106  ? 114.334 120.365 169.266 1.00 62.91  ? 106  GLN   B CD  1 
ATOM   436   O  OE1 . GLN   A 1 106  ? 114.134 121.528 168.915 1.00 62.74  ? 106  GLN   B OE1 1 
ATOM   437   N  NE2 . GLN   A 1 106  ? 114.323 119.348 168.412 1.00 59.54  ? 106  GLN   B NE2 1 
ATOM   438   N  N   . TYR   A 1 107  ? 116.105 119.087 173.928 1.00 46.67  ? 107  TYR   B N   1 
ATOM   439   C  CA  . TYR   A 1 107  ? 117.321 118.321 174.159 1.00 41.10  ? 107  TYR   B CA  1 
ATOM   440   C  C   . TYR   A 1 107  ? 117.561 117.380 172.987 1.00 47.21  ? 107  TYR   B C   1 
ATOM   441   O  O   . TYR   A 1 107  ? 116.655 116.650 172.573 1.00 57.23  ? 107  TYR   B O   1 
ATOM   442   C  CB  . TYR   A 1 107  ? 117.222 117.515 175.454 1.00 43.08  ? 107  TYR   B CB  1 
ATOM   443   C  CG  . TYR   A 1 107  ? 117.339 118.322 176.724 1.00 42.00  ? 107  TYR   B CG  1 
ATOM   444   C  CD1 . TYR   A 1 107  ? 116.242 118.983 177.253 1.00 48.54  ? 107  TYR   B CD1 1 
ATOM   445   C  CD2 . TYR   A 1 107  ? 118.541 118.403 177.407 1.00 43.86  ? 107  TYR   B CD2 1 
ATOM   446   C  CE1 . TYR   A 1 107  ? 116.344 119.711 178.416 1.00 47.78  ? 107  TYR   B CE1 1 
ATOM   447   C  CE2 . TYR   A 1 107  ? 118.651 119.127 178.573 1.00 41.16  ? 107  TYR   B CE2 1 
ATOM   448   C  CZ  . TYR   A 1 107  ? 117.550 119.780 179.071 1.00 41.05  ? 107  TYR   B CZ  1 
ATOM   449   O  OH  . TYR   A 1 107  ? 117.654 120.505 180.232 1.00 50.02  ? 107  TYR   B OH  1 
ATOM   450   N  N   . ASP   A 1 108  ? 118.777 117.401 172.454 1.00 48.86  ? 108  ASP   B N   1 
ATOM   451   C  CA  . ASP   A 1 108  ? 119.207 116.471 171.411 1.00 47.19  ? 108  ASP   B CA  1 
ATOM   452   C  C   . ASP   A 1 108  ? 120.321 115.619 172.012 1.00 51.84  ? 108  ASP   B C   1 
ATOM   453   O  O   . ASP   A 1 108  ? 121.502 115.955 171.917 1.00 56.50  ? 108  ASP   B O   1 
ATOM   454   C  CB  . ASP   A 1 108  ? 119.666 117.209 170.159 1.00 52.56  ? 108  ASP   B CB  1 
ATOM   455   C  CG  . ASP   A 1 108  ? 118.519 117.869 169.420 1.00 59.93  ? 108  ASP   B CG  1 
ATOM   456   O  OD1 . ASP   A 1 108  ? 117.360 117.706 169.855 1.00 56.15  ? 108  ASP   B OD1 1 
ATOM   457   O  OD2 . ASP   A 1 108  ? 118.774 118.550 168.404 1.00 62.47  ? 108  ASP   B OD2 1 
ATOM   458   N  N   . LEU   A 1 109  ? 119.933 114.513 172.636 1.00 47.21  ? 109  LEU   B N   1 
ATOM   459   C  CA  . LEU   A 1 109  ? 120.870 113.678 173.367 1.00 41.06  ? 109  LEU   B CA  1 
ATOM   460   C  C   . LEU   A 1 109  ? 121.663 112.783 172.422 1.00 48.19  ? 109  LEU   B C   1 
ATOM   461   O  O   . LEU   A 1 109  ? 121.286 112.555 171.269 1.00 53.71  ? 109  LEU   B O   1 
ATOM   462   C  CB  . LEU   A 1 109  ? 120.133 112.826 174.397 1.00 39.79  ? 109  LEU   B CB  1 
ATOM   463   C  CG  . LEU   A 1 109  ? 119.311 113.606 175.418 1.00 44.71  ? 109  LEU   B CG  1 
ATOM   464   C  CD1 . LEU   A 1 109  ? 118.684 112.669 176.430 1.00 46.76  ? 109  LEU   B CD1 1 
ATOM   465   C  CD2 . LEU   A 1 109  ? 120.182 114.635 176.102 1.00 46.86  ? 109  LEU   B CD2 1 
ATOM   466   N  N   . ALA   A 1 110  ? 122.776 112.268 172.934 1.00 42.54  ? 110  ALA   B N   1 
ATOM   467   C  CA  . ALA   A 1 110  ? 123.612 111.366 172.165 1.00 44.24  ? 110  ALA   B CA  1 
ATOM   468   C  C   . ALA   A 1 110  ? 122.958 109.992 172.053 1.00 54.82  ? 110  ALA   B C   1 
ATOM   469   O  O   . ALA   A 1 110  ? 122.068 109.629 172.827 1.00 56.17  ? 110  ALA   B O   1 
ATOM   470   C  CB  . ALA   A 1 110  ? 124.993 111.238 172.804 1.00 43.32  ? 110  ALA   B CB  1 
ATOM   471   N  N   . THR   A 1 111  ? 123.414 109.224 171.061 1.00 49.01  ? 111  THR   B N   1 
ATOM   472   C  CA  . THR   A 1 111  ? 122.886 107.878 170.865 1.00 41.70  ? 111  THR   B CA  1 
ATOM   473   C  C   . THR   A 1 111  ? 123.279 106.960 172.016 1.00 45.48  ? 111  THR   B C   1 
ATOM   474   O  O   . THR   A 1 111  ? 122.554 106.012 172.338 1.00 49.13  ? 111  THR   B O   1 
ATOM   475   C  CB  . THR   A 1 111  ? 123.374 107.316 169.531 1.00 51.55  ? 111  THR   B CB  1 
ATOM   476   O  OG1 . THR   A 1 111  ? 123.164 108.287 168.499 1.00 54.91  ? 111  THR   B OG1 1 
ATOM   477   C  CG2 . THR   A 1 111  ? 122.617 106.048 169.173 1.00 53.72  ? 111  THR   B CG2 1 
ATOM   478   N  N   . SER   A 1 112  ? 124.412 107.234 172.656 1.00 42.32  ? 112  SER   B N   1 
ATOM   479   C  CA  . SER   A 1 112  ? 124.898 106.420 173.762 1.00 40.87  ? 112  SER   B CA  1 
ATOM   480   C  C   . SER   A 1 112  ? 124.271 106.788 175.100 1.00 47.95  ? 112  SER   B C   1 
ATOM   481   O  O   . SER   A 1 112  ? 124.585 106.145 176.107 1.00 50.71  ? 112  SER   B O   1 
ATOM   482   C  CB  . SER   A 1 112  ? 126.420 106.533 173.864 1.00 44.57  ? 112  SER   B CB  1 
ATOM   483   O  OG  . SER   A 1 112  ? 126.817 107.876 174.069 1.00 47.22  ? 112  SER   B OG  1 
ATOM   484   N  N   . SER   A 1 113  ? 123.407 107.799 175.141 1.00 50.60  ? 113  SER   B N   1 
ATOM   485   C  CA  . SER   A 1 113  ? 122.778 108.196 176.392 1.00 43.26  ? 113  SER   B CA  1 
ATOM   486   C  C   . SER   A 1 113  ? 121.842 107.107 176.896 1.00 44.52  ? 113  SER   B C   1 
ATOM   487   O  O   . SER   A 1 113  ? 121.136 106.460 176.118 1.00 51.24  ? 113  SER   B O   1 
ATOM   488   C  CB  . SER   A 1 113  ? 122.005 109.499 176.207 1.00 48.10  ? 113  SER   B CB  1 
ATOM   489   O  OG  . SER   A 1 113  ? 120.960 109.341 175.264 1.00 53.63  ? 113  SER   B OG  1 
ATOM   490   N  N   . SER   A 1 114  ? 121.842 106.906 178.211 1.00 49.77  ? 114  SER   B N   1 
ATOM   491   C  CA  . SER   A 1 114  ? 120.970 105.929 178.844 1.00 56.39  ? 114  SER   B CA  1 
ATOM   492   C  C   . SER   A 1 114  ? 119.642 106.519 179.296 1.00 56.23  ? 114  SER   B C   1 
ATOM   493   O  O   . SER   A 1 114  ? 118.788 105.774 179.787 1.00 54.92  ? 114  SER   B O   1 
ATOM   494   C  CB  . SER   A 1 114  ? 121.676 105.294 180.045 1.00 57.13  ? 114  SER   B CB  1 
ATOM   495   O  OG  . SER   A 1 114  ? 122.039 106.278 180.996 1.00 58.11  ? 114  SER   B OG  1 
ATOM   496   N  N   . VAL   A 1 115  ? 119.447 107.822 179.140 1.00 61.23  ? 115  VAL   B N   1 
ATOM   497   C  CA  . VAL   A 1 115  ? 118.230 108.479 179.565 1.00 55.48  ? 115  VAL   B CA  1 
ATOM   498   C  C   . VAL   A 1 115  ? 117.393 108.822 178.339 1.00 57.60  ? 115  VAL   B C   1 
ATOM   499   O  O   . VAL   A 1 115  ? 117.848 108.736 177.202 1.00 61.71  ? 115  VAL   B O   1 
ATOM   500   C  CB  . VAL   A 1 115  ? 118.523 109.738 180.412 1.00 51.92  ? 115  VAL   B CB  1 
ATOM   501   C  CG1 . VAL   A 1 115  ? 119.300 109.367 181.660 1.00 53.54  ? 115  VAL   B CG1 1 
ATOM   502   C  CG2 . VAL   A 1 115  ? 119.289 110.754 179.591 1.00 56.75  ? 115  VAL   B CG2 1 
ATOM   503   N  N   . SER   A 1 116  ? 116.148 109.216 178.573 1.00 61.61  ? 116  SER   B N   1 
ATOM   504   C  CA  . SER   A 1 116  ? 115.228 109.598 177.515 1.00 62.33  ? 116  SER   B CA  1 
ATOM   505   C  C   . SER   A 1 116  ? 114.963 111.096 177.574 1.00 68.89  ? 116  SER   B C   1 
ATOM   506   O  O   . SER   A 1 116  ? 115.257 111.768 178.566 1.00 72.05  ? 116  SER   B O   1 
ATOM   507   C  CB  . SER   A 1 116  ? 113.916 108.814 177.626 1.00 65.95  ? 116  SER   B CB  1 
ATOM   508   O  OG  . SER   A 1 116  ? 113.272 109.070 178.861 1.00 70.05  ? 116  SER   B OG  1 
ATOM   509   N  N   . GLU   A 1 117  ? 114.404 111.617 176.481 1.00 71.48  ? 117  GLU   B N   1 
ATOM   510   C  CA  . GLU   A 1 117  ? 114.119 113.046 176.406 1.00 67.63  ? 117  GLU   B CA  1 
ATOM   511   C  C   . GLU   A 1 117  ? 113.095 113.458 177.456 1.00 67.16  ? 117  GLU   B C   1 
ATOM   512   O  O   . GLU   A 1 117  ? 113.220 114.523 178.073 1.00 71.75  ? 117  GLU   B O   1 
ATOM   513   C  CB  . GLU   A 1 117  ? 113.634 113.406 175.001 1.00 68.01  ? 117  GLU   B CB  1 
ATOM   514   C  CG  . GLU   A 1 117  ? 114.023 114.801 174.533 1.00 70.24  ? 117  GLU   B CG  1 
ATOM   515   C  CD  . GLU   A 1 117  ? 113.132 115.889 175.101 1.00 74.00  ? 117  GLU   B CD  1 
ATOM   516   O  OE1 . GLU   A 1 117  ? 112.023 115.569 175.576 1.00 73.95  ? 117  GLU   B OE1 1 
ATOM   517   O  OE2 . GLU   A 1 117  ? 113.541 117.069 175.067 1.00 72.07  ? 117  GLU   B OE2 1 
ATOM   518   N  N   . SER   A 1 118  ? 112.072 112.628 177.673 1.00 59.47  ? 118  SER   B N   1 
ATOM   519   C  CA  . SER   A 1 118  ? 111.033 112.970 178.638 1.00 62.79  ? 118  SER   B CA  1 
ATOM   520   C  C   . SER   A 1 118  ? 111.508 112.792 180.074 1.00 62.40  ? 118  SER   B C   1 
ATOM   521   O  O   . SER   A 1 118  ? 110.899 113.342 180.998 1.00 66.45  ? 118  SER   B O   1 
ATOM   522   C  CB  . SER   A 1 118  ? 109.784 112.125 178.386 1.00 67.87  ? 118  SER   B CB  1 
ATOM   523   O  OG  . SER   A 1 118  ? 109.271 112.345 177.083 1.00 69.41  ? 118  SER   B OG  1 
ATOM   524   N  N   . SER   A 1 119  ? 112.585 112.033 180.285 1.00 55.48  ? 119  SER   B N   1 
ATOM   525   C  CA  . SER   A 1 119  ? 113.057 111.769 181.639 1.00 59.37  ? 119  SER   B CA  1 
ATOM   526   C  C   . SER   A 1 119  ? 113.736 112.977 182.271 1.00 64.56  ? 119  SER   B C   1 
ATOM   527   O  O   . SER   A 1 119  ? 113.736 113.096 183.500 1.00 65.96  ? 119  SER   B O   1 
ATOM   528   C  CB  . SER   A 1 119  ? 114.019 110.582 181.637 1.00 62.57  ? 119  SER   B CB  1 
ATOM   529   O  OG  . SER   A 1 119  ? 114.502 110.317 182.942 1.00 70.59  ? 119  SER   B OG  1 
ATOM   530   N  N   . ILE   A 1 120  ? 114.314 113.865 181.470 1.00 57.51  ? 120  ILE   B N   1 
ATOM   531   C  CA  . ILE   A 1 120  ? 115.036 115.018 181.994 1.00 53.38  ? 120  ILE   B CA  1 
ATOM   532   C  C   . ILE   A 1 120  ? 114.039 116.021 182.556 1.00 55.88  ? 120  ILE   B C   1 
ATOM   533   O  O   . ILE   A 1 120  ? 112.995 116.283 181.947 1.00 59.01  ? 120  ILE   B O   1 
ATOM   534   C  CB  . ILE   A 1 120  ? 115.908 115.654 180.901 1.00 55.62  ? 120  ILE   B CB  1 
ATOM   535   C  CG1 . ILE   A 1 120  ? 116.816 114.600 180.271 1.00 49.37  ? 120  ILE   B CG1 1 
ATOM   536   C  CG2 . ILE   A 1 120  ? 116.740 116.787 181.472 1.00 60.26  ? 120  ILE   B CG2 1 
ATOM   537   C  CD1 . ILE   A 1 120  ? 117.592 115.101 179.084 1.00 52.82  ? 120  ILE   B CD1 1 
ATOM   538   N  N   . ALA   A 1 121  ? 114.354 116.578 183.723 1.00 52.97  ? 121  ALA   B N   1 
ATOM   539   C  CA  . ALA   A 1 121  ? 113.477 117.560 184.343 1.00 56.93  ? 121  ALA   B CA  1 
ATOM   540   C  C   . ALA   A 1 121  ? 113.390 118.818 183.487 1.00 62.31  ? 121  ALA   B C   1 
ATOM   541   O  O   . ALA   A 1 121  ? 114.368 119.234 182.862 1.00 67.24  ? 121  ALA   B O   1 
ATOM   542   C  CB  . ALA   A 1 121  ? 113.979 117.908 185.744 1.00 55.04  ? 121  ALA   B CB  1 
ATOM   543   N  N   . SER   A 1 122  ? 112.205 119.419 183.460 1.00 57.72  ? 122  SER   B N   1 
ATOM   544   C  CA  . SER   A 1 122  ? 111.983 120.582 182.615 1.00 53.65  ? 122  SER   B CA  1 
ATOM   545   C  C   . SER   A 1 122  ? 112.742 121.789 183.162 1.00 53.61  ? 122  SER   B C   1 
ATOM   546   O  O   . SER   A 1 122  ? 112.748 122.021 184.375 1.00 61.63  ? 122  SER   B O   1 
ATOM   547   C  CB  . SER   A 1 122  ? 110.493 120.899 182.522 1.00 61.17  ? 122  SER   B CB  1 
ATOM   548   O  OG  . SER   A 1 122  ? 110.261 122.010 181.675 1.00 62.75  ? 122  SER   B OG  1 
ATOM   549   N  N   . PRO   A 1 123  ? 113.396 122.564 182.302 1.00 42.29  ? 123  PRO   B N   1 
ATOM   550   C  CA  . PRO   A 1 123  ? 114.101 123.758 182.774 1.00 41.62  ? 123  PRO   B CA  1 
ATOM   551   C  C   . PRO   A 1 123  ? 113.142 124.800 183.326 1.00 48.00  ? 123  PRO   B C   1 
ATOM   552   O  O   . PRO   A 1 123  ? 111.985 124.899 182.911 1.00 59.91  ? 123  PRO   B O   1 
ATOM   553   C  CB  . PRO   A 1 123  ? 114.812 124.273 181.517 1.00 44.84  ? 123  PRO   B CB  1 
ATOM   554   C  CG  . PRO   A 1 123  ? 114.843 123.118 180.584 1.00 47.23  ? 123  PRO   B CG  1 
ATOM   555   C  CD  . PRO   A 1 123  ? 113.601 122.339 180.863 1.00 48.61  ? 123  PRO   B CD  1 
ATOM   556   N  N   . THR   A 1 124  ? 113.642 125.585 184.276 1.00 42.05  ? 124  THR   B N   1 
ATOM   557   C  CA  . THR   A 1 124  ? 112.881 126.654 184.901 1.00 42.82  ? 124  THR   B CA  1 
ATOM   558   C  C   . THR   A 1 124  ? 113.605 127.980 184.711 1.00 50.82  ? 124  THR   B C   1 
ATOM   559   O  O   . THR   A 1 124  ? 114.836 128.027 184.641 1.00 56.66  ? 124  THR   B O   1 
ATOM   560   C  CB  . THR   A 1 124  ? 112.667 126.387 186.392 1.00 46.31  ? 124  THR   B CB  1 
ATOM   561   O  OG1 . THR   A 1 124  ? 113.937 126.270 187.044 1.00 49.85  ? 124  THR   B OG1 1 
ATOM   562   C  CG2 . THR   A 1 124  ? 111.882 125.102 186.594 1.00 51.60  ? 124  THR   B CG2 1 
ATOM   563   N  N   . TRP   A 1 125  ? 112.831 129.062 184.627 1.00 42.60  ? 125  TRP   B N   1 
ATOM   564   C  CA  . TRP   A 1 125  ? 113.389 130.381 184.368 1.00 35.03  ? 125  TRP   B CA  1 
ATOM   565   C  C   . TRP   A 1 125  ? 112.744 131.419 185.274 1.00 43.75  ? 125  TRP   B C   1 
ATOM   566   O  O   . TRP   A 1 125  ? 111.634 131.238 185.779 1.00 48.55  ? 125  TRP   B O   1 
ATOM   567   C  CB  . TRP   A 1 125  ? 113.227 130.791 182.895 1.00 41.89  ? 125  TRP   B CB  1 
ATOM   568   C  CG  . TRP   A 1 125  ? 111.817 130.764 182.364 1.00 43.06  ? 125  TRP   B CG  1 
ATOM   569   C  CD1 . TRP   A 1 125  ? 110.681 130.450 183.047 1.00 43.04  ? 125  TRP   B CD1 1 
ATOM   570   C  CD2 . TRP   A 1 125  ? 111.406 131.060 181.026 1.00 35.54  ? 125  TRP   B CD2 1 
ATOM   571   N  NE1 . TRP   A 1 125  ? 109.591 130.536 182.221 1.00 40.37  ? 125  TRP   B NE1 1 
ATOM   572   C  CE2 . TRP   A 1 125  ? 110.011 130.908 180.973 1.00 32.68  ? 125  TRP   B CE2 1 
ATOM   573   C  CE3 . TRP   A 1 125  ? 112.086 131.440 179.867 1.00 42.22  ? 125  TRP   B CE3 1 
ATOM   574   C  CZ2 . TRP   A 1 125  ? 109.283 131.123 179.809 1.00 40.68  ? 125  TRP   B CZ2 1 
ATOM   575   C  CZ3 . TRP   A 1 125  ? 111.362 131.651 178.714 1.00 47.01  ? 125  TRP   B CZ3 1 
ATOM   576   C  CH2 . TRP   A 1 125  ? 109.976 131.494 178.693 1.00 42.79  ? 125  TRP   B CH2 1 
ATOM   577   N  N   . THR   A 1 126  ? 113.471 132.516 185.477 1.00 47.90  ? 126  THR   B N   1 
ATOM   578   C  CA  . THR   A 1 126  ? 112.980 133.670 186.212 1.00 44.85  ? 126  THR   B CA  1 
ATOM   579   C  C   . THR   A 1 126  ? 113.456 134.930 185.506 1.00 51.30  ? 126  THR   B C   1 
ATOM   580   O  O   . THR   A 1 126  ? 114.433 134.911 184.753 1.00 58.30  ? 126  THR   B O   1 
ATOM   581   C  CB  . THR   A 1 126  ? 113.453 133.671 187.670 1.00 50.33  ? 126  THR   B CB  1 
ATOM   582   O  OG1 . THR   A 1 126  ? 112.861 134.775 188.367 1.00 60.42  ? 126  THR   B OG1 1 
ATOM   583   C  CG2 . THR   A 1 126  ? 114.961 133.796 187.740 1.00 48.10  ? 126  THR   B CG2 1 
ATOM   584   N  N   . PHE   A 1 127  ? 112.754 136.031 185.754 1.00 53.30  ? 127  PHE   B N   1 
ATOM   585   C  CA  . PHE   A 1 127  ? 113.046 137.300 185.106 1.00 47.65  ? 127  PHE   B CA  1 
ATOM   586   C  C   . PHE   A 1 127  ? 113.175 138.398 186.149 1.00 49.52  ? 127  PHE   B C   1 
ATOM   587   O  O   . PHE   A 1 127  ? 112.472 138.391 187.162 1.00 57.26  ? 127  PHE   B O   1 
ATOM   588   C  CB  . PHE   A 1 127  ? 111.956 137.662 184.097 1.00 49.93  ? 127  PHE   B CB  1 
ATOM   589   C  CG  . PHE   A 1 127  ? 112.244 138.905 183.312 1.00 55.82  ? 127  PHE   B CG  1 
ATOM   590   C  CD1 . PHE   A 1 127  ? 113.176 138.894 182.291 1.00 51.20  ? 127  PHE   B CD1 1 
ATOM   591   C  CD2 . PHE   A 1 127  ? 111.574 140.082 183.586 1.00 59.94  ? 127  PHE   B CD2 1 
ATOM   592   C  CE1 . PHE   A 1 127  ? 113.438 140.033 181.565 1.00 52.31  ? 127  PHE   B CE1 1 
ATOM   593   C  CE2 . PHE   A 1 127  ? 111.834 141.225 182.862 1.00 59.75  ? 127  PHE   B CE2 1 
ATOM   594   C  CZ  . PHE   A 1 127  ? 112.768 141.199 181.850 1.00 57.77  ? 127  PHE   B CZ  1 
ATOM   595   N  N   . SER   A 1 128  ? 114.078 139.340 185.892 1.00 54.78  ? 128  SER   B N   1 
ATOM   596   C  CA  . SER   A 1 128  ? 114.309 140.460 186.798 1.00 55.29  ? 128  SER   B CA  1 
ATOM   597   C  C   . SER   A 1 128  ? 114.732 141.666 185.976 1.00 57.54  ? 128  SER   B C   1 
ATOM   598   O  O   . SER   A 1 128  ? 115.797 141.646 185.352 1.00 62.55  ? 128  SER   B O   1 
ATOM   599   C  CB  . SER   A 1 128  ? 115.375 140.115 187.837 1.00 55.90  ? 128  SER   B CB  1 
ATOM   600   O  OG  . SER   A 1 128  ? 116.617 139.831 187.216 1.00 63.95  ? 128  SER   B OG  1 
ATOM   601   N  N   . ASN   A 1 129  ? 113.903 142.705 185.975 1.00 60.40  ? 129  ASN   B N   1 
ATOM   602   C  CA  . ASN   A 1 129  ? 114.159 143.941 185.238 1.00 59.38  ? 129  ASN   B CA  1 
ATOM   603   C  C   . ASN   A 1 129  ? 114.327 145.053 186.268 1.00 61.33  ? 129  ASN   B C   1 
ATOM   604   O  O   . ASN   A 1 129  ? 113.345 145.620 186.753 1.00 67.98  ? 129  ASN   B O   1 
ATOM   605   C  CB  . ASN   A 1 129  ? 113.026 144.237 184.256 1.00 61.42  ? 129  ASN   B CB  1 
ATOM   606   C  CG  . ASN   A 1 129  ? 113.303 145.444 183.378 1.00 65.59  ? 129  ASN   B CG  1 
ATOM   607   O  OD1 . ASN   A 1 129  ? 114.218 146.224 183.633 1.00 69.66  ? 129  ASN   B OD1 1 
ATOM   608   N  ND2 . ASN   A 1 129  ? 112.501 145.603 182.333 1.00 67.21  ? 129  ASN   B ND2 1 
ATOM   609   N  N   . ASP   A 1 130  ? 115.577 145.361 186.598 1.00 64.82  ? 130  ASP   B N   1 
ATOM   610   C  CA  . ASP   A 1 130  ? 115.912 146.388 187.574 1.00 66.57  ? 130  ASP   B CA  1 
ATOM   611   C  C   . ASP   A 1 130  ? 116.731 147.471 186.891 1.00 69.94  ? 130  ASP   B C   1 
ATOM   612   O  O   . ASP   A 1 130  ? 117.688 147.170 186.171 1.00 71.55  ? 130  ASP   B O   1 
ATOM   613   C  CB  . ASP   A 1 130  ? 116.685 145.793 188.751 1.00 67.08  ? 130  ASP   B CB  1 
ATOM   614   C  CG  . ASP   A 1 130  ? 116.968 146.809 189.833 1.00 72.61  ? 130  ASP   B CG  1 
ATOM   615   O  OD1 . ASP   A 1 130  ? 116.547 147.975 189.680 1.00 69.16  ? 130  ASP   B OD1 1 
ATOM   616   O  OD2 . ASP   A 1 130  ? 117.609 146.442 190.838 1.00 72.70  ? 130  ASP   B OD2 1 
ATOM   617   N  N   . SER   A 1 131  ? 116.356 148.727 187.119 1.00 66.28  ? 131  SER   B N   1 
ATOM   618   C  CA  . SER   A 1 131  ? 116.994 149.858 186.462 1.00 64.50  ? 131  SER   B CA  1 
ATOM   619   C  C   . SER   A 1 131  ? 118.206 150.387 187.216 1.00 64.93  ? 131  SER   B C   1 
ATOM   620   O  O   . SER   A 1 131  ? 118.858 151.316 186.731 1.00 71.53  ? 131  SER   B O   1 
ATOM   621   C  CB  . SER   A 1 131  ? 115.981 150.989 186.263 1.00 67.11  ? 131  SER   B CB  1 
ATOM   622   O  OG  . SER   A 1 131  ? 114.897 150.565 185.455 1.00 71.87  ? 131  SER   B OG  1 
ATOM   623   N  N   . SER   A 1 132  ? 118.524 149.827 188.383 1.00 59.46  ? 132  SER   B N   1 
ATOM   624   C  CA  . SER   A 1 132  ? 119.681 150.284 189.140 1.00 59.87  ? 132  SER   B CA  1 
ATOM   625   C  C   . SER   A 1 132  ? 120.972 149.590 188.730 1.00 63.15  ? 132  SER   B C   1 
ATOM   626   O  O   . SER   A 1 132  ? 122.039 149.960 189.231 1.00 69.27  ? 132  SER   B O   1 
ATOM   627   C  CB  . SER   A 1 132  ? 119.448 150.082 190.638 1.00 65.29  ? 132  SER   B CB  1 
ATOM   628   O  OG  . SER   A 1 132  ? 119.384 148.706 190.965 1.00 67.40  ? 132  SER   B OG  1 
ATOM   629   N  N   . ARG   A 1 133  ? 120.907 148.602 187.844 1.00 60.24  ? 133  ARG   B N   1 
ATOM   630   C  CA  . ARG   A 1 133  ? 122.098 147.933 187.350 1.00 61.78  ? 133  ARG   B CA  1 
ATOM   631   C  C   . ARG   A 1 133  ? 122.666 148.682 186.147 1.00 65.62  ? 133  ARG   B C   1 
ATOM   632   O  O   . ARG   A 1 133  ? 122.026 149.562 185.569 1.00 66.82  ? 133  ARG   B O   1 
ATOM   633   C  CB  . ARG   A 1 133  ? 121.788 146.481 186.989 1.00 65.86  ? 133  ARG   B CB  1 
ATOM   634   C  CG  . ARG   A 1 133  ? 121.516 145.593 188.191 1.00 66.52  ? 133  ARG   B CG  1 
ATOM   635   C  CD  . ARG   A 1 133  ? 121.482 144.125 187.805 1.00 65.72  ? 133  ARG   B CD  1 
ATOM   636   N  NE  . ARG   A 1 133  ? 120.236 143.750 187.148 1.00 61.96  ? 133  ARG   B NE  1 
ATOM   637   C  CZ  . ARG   A 1 133  ? 119.205 143.193 187.765 1.00 61.97  ? 133  ARG   B CZ  1 
ATOM   638   N  NH1 . ARG   A 1 133  ? 119.234 142.933 189.061 1.00 66.49  ? 133  ARG   B NH1 1 
ATOM   639   N  NH2 . ARG   A 1 133  ? 118.118 142.885 187.064 1.00 61.99  ? 133  ARG   B NH2 1 
ATOM   640   N  N   . GLU   A 1 134  ? 123.889 148.320 185.771 1.00 70.38  ? 134  GLU   B N   1 
ATOM   641   C  CA  . GLU   A 1 134  ? 124.571 149.016 184.693 1.00 66.92  ? 134  GLU   B CA  1 
ATOM   642   C  C   . GLU   A 1 134  ? 123.919 148.700 183.349 1.00 67.88  ? 134  GLU   B C   1 
ATOM   643   O  O   . GLU   A 1 134  ? 123.139 147.755 183.206 1.00 70.23  ? 134  GLU   B O   1 
ATOM   644   C  CB  . GLU   A 1 134  ? 126.055 148.650 184.667 1.00 68.86  ? 134  GLU   B CB  1 
ATOM   645   C  CG  . GLU   A 1 134  ? 126.346 147.159 184.613 1.00 70.41  ? 134  GLU   B CG  1 
ATOM   646   C  CD  . GLU   A 1 134  ? 126.395 146.518 185.988 1.00 75.32  ? 134  GLU   B CD  1 
ATOM   647   O  OE1 . GLU   A 1 134  ? 125.901 147.135 186.955 1.00 79.20  ? 134  GLU   B OE1 1 
ATOM   648   O  OE2 . GLU   A 1 134  ? 126.934 145.398 186.103 1.00 75.62  ? 134  GLU   B OE2 1 
ATOM   649   N  N   . VAL   A 1 135  ? 124.245 149.526 182.353 1.00 62.97  ? 135  VAL   B N   1 
ATOM   650   C  CA  . VAL   A 1 135  ? 123.676 149.369 181.021 1.00 57.23  ? 135  VAL   B CA  1 
ATOM   651   C  C   . VAL   A 1 135  ? 124.109 148.034 180.434 1.00 59.33  ? 135  VAL   B C   1 
ATOM   652   O  O   . VAL   A 1 135  ? 125.277 147.634 180.537 1.00 66.96  ? 135  VAL   B O   1 
ATOM   653   C  CB  . VAL   A 1 135  ? 124.099 150.539 180.117 1.00 57.53  ? 135  VAL   B CB  1 
ATOM   654   C  CG1 . VAL   A 1 135  ? 123.425 150.434 178.760 1.00 58.90  ? 135  VAL   B CG1 1 
ATOM   655   C  CG2 . VAL   A 1 135  ? 123.766 151.863 180.779 1.00 60.36  ? 135  VAL   B CG2 1 
ATOM   656   N  N   . GLY   A 1 136  ? 123.164 147.336 179.813 1.00 55.34  ? 136  GLY   B N   1 
ATOM   657   C  CA  . GLY   A 1 136  ? 123.419 146.027 179.258 1.00 59.07  ? 136  GLY   B CA  1 
ATOM   658   C  C   . GLY   A 1 136  ? 123.152 144.871 180.193 1.00 58.04  ? 136  GLY   B C   1 
ATOM   659   O  O   . GLY   A 1 136  ? 123.278 143.715 179.770 1.00 60.26  ? 136  GLY   B O   1 
ATOM   660   N  N   . GLU   A 1 137  ? 122.789 145.139 181.448 1.00 64.34  ? 137  GLU   B N   1 
ATOM   661   C  CA  . GLU   A 1 137  ? 122.480 144.086 182.405 1.00 62.38  ? 137  GLU   B CA  1 
ATOM   662   C  C   . GLU   A 1 137  ? 121.252 144.414 183.247 1.00 63.46  ? 137  GLU   B C   1 
ATOM   663   O  O   . GLU   A 1 137  ? 121.081 143.832 184.324 1.00 68.93  ? 137  GLU   B O   1 
ATOM   664   C  CB  . GLU   A 1 137  ? 123.684 143.817 183.315 1.00 66.93  ? 137  GLU   B CB  1 
ATOM   665   C  CG  . GLU   A 1 137  ? 123.785 142.376 183.800 1.00 74.72  ? 137  GLU   B CG  1 
ATOM   666   C  CD  . GLU   A 1 137  ? 124.951 142.153 184.740 1.00 74.19  ? 137  GLU   B CD  1 
ATOM   667   O  OE1 . GLU   A 1 137  ? 125.668 143.129 185.043 1.00 68.03  ? 137  GLU   B OE1 1 
ATOM   668   O  OE2 . GLU   A 1 137  ? 125.151 141.000 185.177 1.00 71.87  ? 137  GLU   B OE2 1 
ATOM   669   N  N   . THR   A 1 138  ? 120.397 145.330 182.791 1.00 56.13  ? 138  THR   B N   1 
ATOM   670   C  CA  . THR   A 1 138  ? 119.200 145.663 183.554 1.00 56.96  ? 138  THR   B CA  1 
ATOM   671   C  C   . THR   A 1 138  ? 118.209 144.507 183.563 1.00 57.28  ? 138  THR   B C   1 
ATOM   672   O  O   . THR   A 1 138  ? 117.651 144.168 184.612 1.00 65.23  ? 138  THR   B O   1 
ATOM   673   C  CB  . THR   A 1 138  ? 118.545 146.921 182.986 1.00 62.45  ? 138  THR   B CB  1 
ATOM   674   O  OG1 . THR   A 1 138  ? 118.151 146.687 181.629 1.00 70.40  ? 138  THR   B OG1 1 
ATOM   675   C  CG2 . THR   A 1 138  ? 119.513 148.089 183.031 1.00 59.98  ? 138  THR   B CG2 1 
ATOM   676   N  N   . ALA   A 1 139  ? 117.977 143.889 182.408 1.00 49.63  ? 139  ALA   B N   1 
ATOM   677   C  CA  . ALA   A 1 139  ? 117.049 142.773 182.284 1.00 51.59  ? 139  ALA   B CA  1 
ATOM   678   C  C   . ALA   A 1 139  ? 117.852 141.479 182.241 1.00 61.94  ? 139  ALA   B C   1 
ATOM   679   O  O   . ALA   A 1 139  ? 118.709 141.303 181.370 1.00 63.32  ? 139  ALA   B O   1 
ATOM   680   C  CB  . ALA   A 1 139  ? 116.181 142.924 181.038 1.00 56.80  ? 139  ALA   B CB  1 
ATOM   681   N  N   . ARG   A 1 140  ? 117.575 140.576 183.179 1.00 58.18  ? 140  ARG   B N   1 
ATOM   682   C  CA  . ARG   A 1 140  ? 118.282 139.309 183.290 1.00 50.15  ? 140  ARG   B CA  1 
ATOM   683   C  C   . ARG   A 1 140  ? 117.281 138.166 183.304 1.00 54.85  ? 140  ARG   B C   1 
ATOM   684   O  O   . ARG   A 1 140  ? 116.292 138.212 184.041 1.00 63.66  ? 140  ARG   B O   1 
ATOM   685   C  CB  . ARG   A 1 140  ? 119.142 139.261 184.554 1.00 49.86  ? 140  ARG   B CB  1 
ATOM   686   C  CG  . ARG   A 1 140  ? 120.125 140.407 184.684 1.00 56.16  ? 140  ARG   B CG  1 
ATOM   687   C  CD  . ARG   A 1 140  ? 121.454 139.923 185.234 1.00 53.83  ? 140  ARG   B CD  1 
ATOM   688   N  NE  . ARG   A 1 140  ? 121.286 139.089 186.417 1.00 59.02  ? 140  ARG   B NE  1 
ATOM   689   C  CZ  . ARG   A 1 140  ? 121.396 139.525 187.664 1.00 63.01  ? 140  ARG   B CZ  1 
ATOM   690   N  NH1 . ARG   A 1 140  ? 121.680 140.789 187.931 1.00 60.79  ? 140  ARG   B NH1 1 
ATOM   691   N  NH2 . ARG   A 1 140  ? 121.220 138.671 188.668 1.00 59.18  ? 140  ARG   B NH2 1 
ATOM   692   N  N   . CYS   A 1 141  ? 117.541 137.144 182.494 1.00 51.89  ? 141  CYS   B N   1 
ATOM   693   C  CA  . CYS   A 1 141  ? 116.746 135.920 182.481 1.00 45.98  ? 141  CYS   B CA  1 
ATOM   694   C  C   . CYS   A 1 141  ? 117.646 134.778 182.924 1.00 51.67  ? 141  CYS   B C   1 
ATOM   695   O  O   . CYS   A 1 141  ? 118.589 134.415 182.213 1.00 55.09  ? 141  CYS   B O   1 
ATOM   696   C  CB  . CYS   A 1 141  ? 116.159 135.650 181.098 1.00 50.46  ? 141  CYS   B CB  1 
ATOM   697   S  SG  . CYS   A 1 141  ? 115.082 134.204 181.025 1.00 62.83  ? 141  CYS   B SG  1 
ATOM   698   N  N   . GLU   A 1 142  ? 117.361 134.217 184.094 1.00 56.30  ? 142  GLU   B N   1 
ATOM   699   C  CA  . GLU   A 1 142  ? 118.152 133.133 184.662 1.00 52.70  ? 142  GLU   B CA  1 
ATOM   700   C  C   . GLU   A 1 142  ? 117.436 131.819 184.379 1.00 56.15  ? 142  GLU   B C   1 
ATOM   701   O  O   . GLU   A 1 142  ? 116.306 131.612 184.830 1.00 60.92  ? 142  GLU   B O   1 
ATOM   702   C  CB  . GLU   A 1 142  ? 118.355 133.342 186.160 1.00 52.32  ? 142  GLU   B CB  1 
ATOM   703   C  CG  . GLU   A 1 142  ? 119.006 134.666 186.510 1.00 56.67  ? 142  GLU   B CG  1 
ATOM   704   C  CD  . GLU   A 1 142  ? 119.113 134.889 188.003 1.00 60.69  ? 142  GLU   B CD  1 
ATOM   705   O  OE1 . GLU   A 1 142  ? 118.663 134.014 188.771 1.00 62.90  ? 142  GLU   B OE1 1 
ATOM   706   O  OE2 . GLU   A 1 142  ? 119.647 135.942 188.411 1.00 61.86  ? 142  GLU   B OE2 1 
ATOM   707   N  N   . ILE   A 1 143  ? 118.092 130.934 183.634 1.00 46.61  ? 143  ILE   B N   1 
ATOM   708   C  CA  . ILE   A 1 143  ? 117.518 129.656 183.232 1.00 38.60  ? 143  ILE   B CA  1 
ATOM   709   C  C   . ILE   A 1 143  ? 118.292 128.540 183.916 1.00 50.69  ? 143  ILE   B C   1 
ATOM   710   O  O   . ILE   A 1 143  ? 119.518 128.452 183.781 1.00 59.88  ? 143  ILE   B O   1 
ATOM   711   C  CB  . ILE   A 1 143  ? 117.544 129.480 181.705 1.00 40.02  ? 143  ILE   B CB  1 
ATOM   712   C  CG1 . ILE   A 1 143  ? 116.750 130.593 181.024 1.00 44.24  ? 143  ILE   B CG1 1 
ATOM   713   C  CG2 . ILE   A 1 143  ? 116.985 128.124 181.321 1.00 48.90  ? 143  ILE   B CG2 1 
ATOM   714   C  CD1 . ILE   A 1 143  ? 116.701 130.467 179.523 1.00 47.59  ? 143  ILE   B CD1 1 
ATOM   715   N  N   . GLU   A 1 144  ? 117.577 127.690 184.646 1.00 51.29  ? 144  GLU   B N   1 
ATOM   716   C  CA  . GLU   A 1 144  ? 118.159 126.516 185.280 1.00 40.15  ? 144  GLU   B CA  1 
ATOM   717   C  C   . GLU   A 1 144  ? 117.817 125.291 184.444 1.00 47.74  ? 144  GLU   B C   1 
ATOM   718   O  O   . GLU   A 1 144  ? 116.638 124.974 184.259 1.00 60.14  ? 144  GLU   B O   1 
ATOM   719   C  CB  . GLU   A 1 144  ? 117.644 126.349 186.708 1.00 47.19  ? 144  GLU   B CB  1 
ATOM   720   C  CG  . GLU   A 1 144  ? 118.109 127.421 187.668 1.00 56.84  ? 144  GLU   B CG  1 
ATOM   721   C  CD  . GLU   A 1 144  ? 117.661 127.155 189.090 1.00 62.29  ? 144  GLU   B CD  1 
ATOM   722   O  OE1 . GLU   A 1 144  ? 117.010 126.116 189.324 1.00 57.78  ? 144  GLU   B OE1 1 
ATOM   723   O  OE2 . GLU   A 1 144  ? 117.961 127.985 189.974 1.00 63.62  ? 144  GLU   B OE2 1 
ATOM   724   N  N   . PHE   A 1 145  ? 118.842 124.606 183.948 1.00 43.67  ? 145  PHE   B N   1 
ATOM   725   C  CA  . PHE   A 1 145  ? 118.660 123.435 183.107 1.00 38.99  ? 145  PHE   B CA  1 
ATOM   726   C  C   . PHE   A 1 145  ? 119.568 122.316 183.593 1.00 46.06  ? 145  PHE   B C   1 
ATOM   727   O  O   . PHE   A 1 145  ? 120.618 122.555 184.194 1.00 56.87  ? 145  PHE   B O   1 
ATOM   728   C  CB  . PHE   A 1 145  ? 118.944 123.749 181.630 1.00 42.67  ? 145  PHE   B CB  1 
ATOM   729   C  CG  . PHE   A 1 145  ? 120.373 124.105 181.344 1.00 39.89  ? 145  PHE   B CG  1 
ATOM   730   C  CD1 . PHE   A 1 145  ? 120.856 125.368 181.624 1.00 43.10  ? 145  PHE   B CD1 1 
ATOM   731   C  CD2 . PHE   A 1 145  ? 121.230 123.180 180.778 1.00 43.96  ? 145  PHE   B CD2 1 
ATOM   732   C  CE1 . PHE   A 1 145  ? 122.166 125.696 181.361 1.00 46.53  ? 145  PHE   B CE1 1 
ATOM   733   C  CE2 . PHE   A 1 145  ? 122.541 123.507 180.511 1.00 47.33  ? 145  PHE   B CE2 1 
ATOM   734   C  CZ  . PHE   A 1 145  ? 123.008 124.766 180.805 1.00 46.33  ? 145  PHE   B CZ  1 
ATOM   735   N  N   . GLU   A 1 146  ? 119.148 121.084 183.327 1.00 51.72  ? 146  GLU   B N   1 
ATOM   736   C  CA  . GLU   A 1 146  ? 119.865 119.895 183.761 1.00 45.85  ? 146  GLU   B CA  1 
ATOM   737   C  C   . GLU   A 1 146  ? 120.615 119.290 182.585 1.00 51.22  ? 146  GLU   B C   1 
ATOM   738   O  O   . GLU   A 1 146  ? 120.059 119.156 181.491 1.00 59.36  ? 146  GLU   B O   1 
ATOM   739   C  CB  . GLU   A 1 146  ? 118.910 118.862 184.360 1.00 47.09  ? 146  GLU   B CB  1 
ATOM   740   C  CG  . GLU   A 1 146  ? 118.335 119.258 185.703 1.00 54.58  ? 146  GLU   B CG  1 
ATOM   741   C  CD  . GLU   A 1 146  ? 117.470 118.173 186.307 1.00 62.14  ? 146  GLU   B CD  1 
ATOM   742   O  OE1 . GLU   A 1 146  ? 117.287 117.124 185.653 1.00 57.07  ? 146  GLU   B OE1 1 
ATOM   743   O  OE2 . GLU   A 1 146  ? 116.971 118.368 187.435 1.00 65.65  ? 146  GLU   B OE2 1 
ATOM   744   N  N   . VAL   A 1 147  ? 121.874 118.930 182.816 1.00 45.38  ? 147  VAL   B N   1 
ATOM   745   C  CA  . VAL   A 1 147  ? 122.684 118.213 181.836 1.00 42.66  ? 147  VAL   B CA  1 
ATOM   746   C  C   . VAL   A 1 147  ? 122.639 116.731 182.204 1.00 49.40  ? 147  VAL   B C   1 
ATOM   747   O  O   . VAL   A 1 147  ? 123.213 116.344 183.235 1.00 57.14  ? 147  VAL   B O   1 
ATOM   748   C  CB  . VAL   A 1 147  ? 124.122 118.739 181.800 1.00 44.65  ? 147  VAL   B CB  1 
ATOM   749   C  CG1 . VAL   A 1 147  ? 124.944 117.951 180.808 1.00 50.37  ? 147  VAL   B CG1 1 
ATOM   750   C  CG2 . VAL   A 1 147  ? 124.130 120.207 181.432 1.00 49.03  ? 147  VAL   B CG2 1 
ATOM   751   N  N   . PRO   A 1 148  ? 121.973 115.883 181.418 1.00 42.35  ? 148  PRO   B N   1 
ATOM   752   C  CA  . PRO   A 1 148  ? 121.737 114.498 181.861 1.00 42.59  ? 148  PRO   B CA  1 
ATOM   753   C  C   . PRO   A 1 148  ? 123.000 113.682 182.066 1.00 51.57  ? 148  PRO   B C   1 
ATOM   754   O  O   . PRO   A 1 148  ? 123.034 112.830 182.961 1.00 54.05  ? 148  PRO   B O   1 
ATOM   755   C  CB  . PRO   A 1 148  ? 120.869 113.922 180.735 1.00 42.96  ? 148  PRO   B CB  1 
ATOM   756   C  CG  . PRO   A 1 148  ? 121.200 114.751 179.548 1.00 45.42  ? 148  PRO   B CG  1 
ATOM   757   C  CD  . PRO   A 1 148  ? 121.450 116.129 180.065 1.00 40.81  ? 148  PRO   B CD  1 
ATOM   758   N  N   . TYR   A 1 149  ? 124.039 113.911 181.267 1.00 51.07  ? 149  TYR   B N   1 
ATOM   759   C  CA  . TYR   A 1 149  ? 125.268 113.139 181.356 1.00 37.47  ? 149  TYR   B CA  1 
ATOM   760   C  C   . TYR   A 1 149  ? 126.453 114.055 181.101 1.00 39.42  ? 149  TYR   B C   1 
ATOM   761   O  O   . TYR   A 1 149  ? 126.317 115.130 180.513 1.00 49.86  ? 149  TYR   B O   1 
ATOM   762   C  CB  . TYR   A 1 149  ? 125.273 111.968 180.366 1.00 39.53  ? 149  TYR   B CB  1 
ATOM   763   C  CG  . TYR   A 1 149  ? 124.871 112.347 178.961 1.00 37.58  ? 149  TYR   B CG  1 
ATOM   764   C  CD1 . TYR   A 1 149  ? 125.812 112.778 178.041 1.00 39.48  ? 149  TYR   B CD1 1 
ATOM   765   C  CD2 . TYR   A 1 149  ? 123.549 112.269 178.555 1.00 40.14  ? 149  TYR   B CD2 1 
ATOM   766   C  CE1 . TYR   A 1 149  ? 125.447 113.123 176.760 1.00 41.15  ? 149  TYR   B CE1 1 
ATOM   767   C  CE2 . TYR   A 1 149  ? 123.176 112.613 177.277 1.00 37.28  ? 149  TYR   B CE2 1 
ATOM   768   C  CZ  . TYR   A 1 149  ? 124.129 113.040 176.384 1.00 39.98  ? 149  TYR   B CZ  1 
ATOM   769   O  OH  . TYR   A 1 149  ? 123.760 113.383 175.106 1.00 52.38  ? 149  TYR   B OH  1 
ATOM   770   N  N   . ASP   A 1 150  ? 127.624 113.616 181.556 1.00 40.26  ? 150  ASP   B N   1 
ATOM   771   C  CA  . ASP   A 1 150  ? 128.826 114.426 181.415 1.00 43.28  ? 150  ASP   B CA  1 
ATOM   772   C  C   . ASP   A 1 150  ? 129.122 114.688 179.946 1.00 51.20  ? 150  ASP   B C   1 
ATOM   773   O  O   . ASP   A 1 150  ? 129.175 113.760 179.134 1.00 56.58  ? 150  ASP   B O   1 
ATOM   774   C  CB  . ASP   A 1 150  ? 130.013 113.729 182.078 1.00 43.47  ? 150  ASP   B CB  1 
ATOM   775   C  CG  . ASP   A 1 150  ? 129.802 113.503 183.558 1.00 55.59  ? 150  ASP   B CG  1 
ATOM   776   O  OD1 . ASP   A 1 150  ? 128.667 113.714 184.036 1.00 60.56  ? 150  ASP   B OD1 1 
ATOM   777   O  OD2 . ASP   A 1 150  ? 130.770 113.120 184.245 1.00 54.12  ? 150  ASP   B OD2 1 
ATOM   778   N  N   . LEU   A 1 151  ? 129.313 115.958 179.608 1.00 38.91  ? 151  LEU   B N   1 
ATOM   779   C  CA  . LEU   A 1 151  ? 129.605 116.373 178.245 1.00 34.86  ? 151  LEU   B CA  1 
ATOM   780   C  C   . LEU   A 1 151  ? 131.098 116.629 178.117 1.00 37.88  ? 151  LEU   B C   1 
ATOM   781   O  O   . LEU   A 1 151  ? 131.645 117.494 178.808 1.00 40.20  ? 151  LEU   B O   1 
ATOM   782   C  CB  . LEU   A 1 151  ? 128.808 117.623 177.873 1.00 41.77  ? 151  LEU   B CB  1 
ATOM   783   C  CG  . LEU   A 1 151  ? 127.289 117.481 177.970 1.00 40.04  ? 151  LEU   B CG  1 
ATOM   784   C  CD1 . LEU   A 1 151  ? 126.587 118.722 177.467 1.00 45.65  ? 151  LEU   B CD1 1 
ATOM   785   C  CD2 . LEU   A 1 151  ? 126.832 116.270 177.192 1.00 40.89  ? 151  LEU   B CD2 1 
ATOM   786   N  N   . GLY   A 1 152  ? 131.747 115.884 177.227 1.00 43.62  ? 152  GLY   B N   1 
ATOM   787   C  CA  . GLY   A 1 152  ? 133.185 115.887 177.127 1.00 37.93  ? 152  GLY   B CA  1 
ATOM   788   C  C   . GLY   A 1 152  ? 133.737 117.227 176.699 1.00 43.69  ? 152  GLY   B C   1 
ATOM   789   O  O   . GLY   A 1 152  ? 132.995 118.135 176.313 1.00 55.54  ? 152  GLY   B O   1 
ATOM   790   N  N   . PRO   A 1 153  ? 135.058 117.376 176.770 1.00 48.13  ? 153  PRO   B N   1 
ATOM   791   C  CA  . PRO   A 1 153  ? 135.675 118.662 176.425 1.00 51.80  ? 153  PRO   B CA  1 
ATOM   792   C  C   . PRO   A 1 153  ? 135.363 119.065 174.993 1.00 54.57  ? 153  PRO   B C   1 
ATOM   793   O  O   . PRO   A 1 153  ? 135.290 118.228 174.091 1.00 50.87  ? 153  PRO   B O   1 
ATOM   794   C  CB  . PRO   A 1 153  ? 137.172 118.404 176.628 1.00 51.92  ? 153  PRO   B CB  1 
ATOM   795   C  CG  . PRO   A 1 153  ? 137.319 116.920 176.610 1.00 52.54  ? 153  PRO   B CG  1 
ATOM   796   C  CD  . PRO   A 1 153  ? 136.056 116.381 177.190 1.00 49.38  ? 153  PRO   B CD  1 
ATOM   797   N  N   . GLY   A 1 154  ? 135.177 120.365 174.794 1.00 48.33  ? 154  GLY   B N   1 
ATOM   798   C  CA  . GLY   A 1 154  ? 134.754 120.870 173.507 1.00 48.38  ? 154  GLY   B CA  1 
ATOM   799   C  C   . GLY   A 1 154  ? 133.326 121.367 173.529 1.00 48.39  ? 154  GLY   B C   1 
ATOM   800   O  O   . GLY   A 1 154  ? 132.577 121.167 172.569 1.00 51.88  ? 154  GLY   B O   1 
ATOM   801   N  N   . LEU   A 1 155  ? 132.934 122.008 174.626 1.00 48.18  ? 155  LEU   B N   1 
ATOM   802   C  CA  . LEU   A 1 155  ? 131.590 122.548 174.767 1.00 39.77  ? 155  LEU   B CA  1 
ATOM   803   C  C   . LEU   A 1 155  ? 131.544 123.981 174.260 1.00 41.98  ? 155  LEU   B C   1 
ATOM   804   O  O   . LEU   A 1 155  ? 132.369 124.813 174.647 1.00 52.26  ? 155  LEU   B O   1 
ATOM   805   C  CB  . LEU   A 1 155  ? 131.136 122.479 176.222 1.00 33.85  ? 155  LEU   B CB  1 
ATOM   806   C  CG  . LEU   A 1 155  ? 130.528 121.125 176.567 1.00 41.27  ? 155  LEU   B CG  1 
ATOM   807   C  CD1 . LEU   A 1 155  ? 130.637 120.844 178.045 1.00 47.20  ? 155  LEU   B CD1 1 
ATOM   808   C  CD2 . LEU   A 1 155  ? 129.080 121.083 176.118 1.00 46.07  ? 155  LEU   B CD2 1 
ATOM   809   N  N   . PHE   A 1 156  ? 130.574 124.262 173.396 1.00 31.69  ? 156  PHE   B N   1 
ATOM   810   C  CA  . PHE   A 1 156  ? 130.437 125.557 172.752 1.00 29.62  ? 156  PHE   B CA  1 
ATOM   811   C  C   . PHE   A 1 156  ? 129.071 126.145 173.061 1.00 33.91  ? 156  PHE   B C   1 
ATOM   812   O  O   . PHE   A 1 156  ? 128.078 125.418 173.161 1.00 44.17  ? 156  PHE   B O   1 
ATOM   813   C  CB  . PHE   A 1 156  ? 130.622 125.440 171.238 1.00 33.46  ? 156  PHE   B CB  1 
ATOM   814   C  CG  . PHE   A 1 156  ? 131.998 125.011 170.829 1.00 39.72  ? 156  PHE   B CG  1 
ATOM   815   C  CD1 . PHE   A 1 156  ? 132.319 123.673 170.731 1.00 29.62  ? 156  PHE   B CD1 1 
ATOM   816   C  CD2 . PHE   A 1 156  ? 132.971 125.946 170.542 1.00 49.70  ? 156  PHE   B CD2 1 
ATOM   817   C  CE1 . PHE   A 1 156  ? 133.581 123.276 170.361 1.00 29.85  ? 156  PHE   B CE1 1 
ATOM   818   C  CE2 . PHE   A 1 156  ? 134.236 125.553 170.168 1.00 44.98  ? 156  PHE   B CE2 1 
ATOM   819   C  CZ  . PHE   A 1 156  ? 134.540 124.214 170.077 1.00 42.10  ? 156  PHE   B CZ  1 
ATOM   820   N  N   . LEU   A 1 157  ? 129.027 127.464 173.213 1.00 34.93  ? 157  LEU   B N   1 
ATOM   821   C  CA  . LEU   A 1 157  ? 127.802 128.190 173.521 1.00 35.10  ? 157  LEU   B CA  1 
ATOM   822   C  C   . LEU   A 1 157  ? 127.438 129.064 172.329 1.00 39.24  ? 157  LEU   B C   1 
ATOM   823   O  O   . LEU   A 1 157  ? 128.254 129.873 171.877 1.00 42.82  ? 157  LEU   B O   1 
ATOM   824   C  CB  . LEU   A 1 157  ? 127.977 129.032 174.785 1.00 35.01  ? 157  LEU   B CB  1 
ATOM   825   C  CG  . LEU   A 1 157  ? 126.785 129.848 175.279 1.00 32.95  ? 157  LEU   B CG  1 
ATOM   826   C  CD1 . LEU   A 1 157  ? 125.627 128.935 175.569 1.00 41.74  ? 157  LEU   B CD1 1 
ATOM   827   C  CD2 . LEU   A 1 157  ? 127.158 130.631 176.518 1.00 37.11  ? 157  LEU   B CD2 1 
ATOM   828   N  N   . TYR   A 1 158  ? 126.222 128.893 171.822 1.00 41.51  ? 158  TYR   B N   1 
ATOM   829   C  CA  . TYR   A 1 158  ? 125.729 129.631 170.673 1.00 25.56  ? 158  TYR   B CA  1 
ATOM   830   C  C   . TYR   A 1 158  ? 124.457 130.374 171.048 1.00 35.05  ? 158  TYR   B C   1 
ATOM   831   O  O   . TYR   A 1 158  ? 123.799 130.060 172.043 1.00 46.41  ? 158  TYR   B O   1 
ATOM   832   C  CB  . TYR   A 1 158  ? 125.430 128.706 169.485 1.00 35.54  ? 158  TYR   B CB  1 
ATOM   833   C  CG  . TYR   A 1 158  ? 126.598 127.898 168.975 1.00 40.68  ? 158  TYR   B CG  1 
ATOM   834   C  CD1 . TYR   A 1 158  ? 126.920 126.674 169.541 1.00 38.56  ? 158  TYR   B CD1 1 
ATOM   835   C  CD2 . TYR   A 1 158  ? 127.361 128.344 167.907 1.00 40.35  ? 158  TYR   B CD2 1 
ATOM   836   C  CE1 . TYR   A 1 158  ? 127.976 125.929 169.070 1.00 34.75  ? 158  TYR   B CE1 1 
ATOM   837   C  CE2 . TYR   A 1 158  ? 128.420 127.604 167.431 1.00 39.57  ? 158  TYR   B CE2 1 
ATOM   838   C  CZ  . TYR   A 1 158  ? 128.724 126.400 168.018 1.00 37.62  ? 158  TYR   B CZ  1 
ATOM   839   O  OH  . TYR   A 1 158  ? 129.781 125.658 167.545 1.00 48.02  ? 158  TYR   B OH  1 
ATOM   840   N  N   . TYR   A 1 159  ? 124.115 131.371 170.239 1.00 33.58  ? 159  TYR   B N   1 
ATOM   841   C  CA  . TYR   A 1 159  ? 122.793 131.978 170.267 1.00 35.79  ? 159  TYR   B CA  1 
ATOM   842   C  C   . TYR   A 1 159  ? 122.164 131.828 168.891 1.00 37.00  ? 159  TYR   B C   1 
ATOM   843   O  O   . TYR   A 1 159  ? 122.798 132.134 167.876 1.00 46.13  ? 159  TYR   B O   1 
ATOM   844   C  CB  . TYR   A 1 159  ? 122.842 133.450 170.695 1.00 36.14  ? 159  TYR   B CB  1 
ATOM   845   C  CG  . TYR   A 1 159  ? 123.725 134.351 169.866 1.00 37.01  ? 159  TYR   B CG  1 
ATOM   846   C  CD1 . TYR   A 1 159  ? 123.230 135.007 168.750 1.00 36.20  ? 159  TYR   B CD1 1 
ATOM   847   C  CD2 . TYR   A 1 159  ? 125.044 134.576 170.222 1.00 40.92  ? 159  TYR   B CD2 1 
ATOM   848   C  CE1 . TYR   A 1 159  ? 124.028 135.837 168.000 1.00 37.03  ? 159  TYR   B CE1 1 
ATOM   849   C  CE2 . TYR   A 1 159  ? 125.849 135.407 169.480 1.00 39.47  ? 159  TYR   B CE2 1 
ATOM   850   C  CZ  . TYR   A 1 159  ? 125.337 136.034 168.371 1.00 40.58  ? 159  TYR   B CZ  1 
ATOM   851   O  OH  . TYR   A 1 159  ? 126.140 136.864 167.627 1.00 44.73  ? 159  TYR   B OH  1 
ATOM   852   N  N   . LYS   A 1 160  ? 120.930 131.340 168.859 1.00 35.62  ? 160  LYS   B N   1 
ATOM   853   C  CA  . LYS   A 1 160  ? 120.217 131.072 167.620 1.00 32.11  ? 160  LYS   B CA  1 
ATOM   854   C  C   . LYS   A 1 160  ? 119.159 132.143 167.410 1.00 40.90  ? 160  LYS   B C   1 
ATOM   855   O  O   . LYS   A 1 160  ? 118.377 132.434 168.320 1.00 48.96  ? 160  LYS   B O   1 
ATOM   856   C  CB  . LYS   A 1 160  ? 119.567 129.687 167.648 1.00 39.65  ? 160  LYS   B CB  1 
ATOM   857   C  CG  . LYS   A 1 160  ? 119.016 129.234 166.311 1.00 43.10  ? 160  LYS   B CG  1 
ATOM   858   C  CD  . LYS   A 1 160  ? 117.772 128.382 166.483 1.00 45.97  ? 160  LYS   B CD  1 
ATOM   859   C  CE  . LYS   A 1 160  ? 118.017 127.222 167.421 1.00 40.17  ? 160  LYS   B CE  1 
ATOM   860   N  NZ  . LYS   A 1 160  ? 116.801 126.380 167.569 1.00 35.55  ? 160  LYS   B NZ  1 
ATOM   861   N  N   . LEU   A 1 161  ? 119.133 132.722 166.214 1.00 41.67  ? 161  LEU   B N   1 
ATOM   862   C  CA  . LEU   A 1 161  ? 118.148 133.731 165.852 1.00 34.19  ? 161  LEU   B CA  1 
ATOM   863   C  C   . LEU   A 1 161  ? 117.279 133.198 164.725 1.00 38.27  ? 161  LEU   B C   1 
ATOM   864   O  O   . LEU   A 1 161  ? 117.794 132.781 163.683 1.00 49.01  ? 161  LEU   B O   1 
ATOM   865   C  CB  . LEU   A 1 161  ? 118.822 135.036 165.431 1.00 34.97  ? 161  LEU   B CB  1 
ATOM   866   C  CG  . LEU   A 1 161  ? 119.557 135.799 166.531 1.00 34.10  ? 161  LEU   B CG  1 
ATOM   867   C  CD1 . LEU   A 1 161  ? 120.186 137.051 165.975 1.00 37.21  ? 161  LEU   B CD1 1 
ATOM   868   C  CD2 . LEU   A 1 161  ? 118.610 136.142 167.654 1.00 41.56  ? 161  LEU   B CD2 1 
ATOM   869   N  N   . THR   A 1 162  ? 115.968 133.212 164.935 1.00 48.46  ? 162  THR   B N   1 
ATOM   870   C  CA  . THR   A 1 162  ? 115.006 132.751 163.948 1.00 43.43  ? 162  THR   B CA  1 
ATOM   871   C  C   . THR   A 1 162  ? 114.284 133.943 163.337 1.00 46.02  ? 162  THR   B C   1 
ATOM   872   O  O   . THR   A 1 162  ? 114.081 134.969 163.993 1.00 52.18  ? 162  THR   B O   1 
ATOM   873   C  CB  . THR   A 1 162  ? 113.989 131.791 164.568 1.00 46.63  ? 162  THR   B CB  1 
ATOM   874   O  OG1 . THR   A 1 162  ? 113.182 132.499 165.517 1.00 53.54  ? 162  THR   B OG1 1 
ATOM   875   C  CG2 . THR   A 1 162  ? 114.701 130.650 165.272 1.00 48.21  ? 162  THR   B CG2 1 
ATOM   876   N  N   . ASN   A 1 163  ? 113.904 133.795 162.069 1.00 42.08  ? 163  ASN   B N   1 
ATOM   877   C  CA  . ASN   A 1 163  ? 113.266 134.864 161.301 1.00 36.99  ? 163  ASN   B CA  1 
ATOM   878   C  C   . ASN   A 1 163  ? 114.128 136.123 161.282 1.00 42.11  ? 163  ASN   B C   1 
ATOM   879   O  O   . ASN   A 1 163  ? 113.620 137.245 161.328 1.00 55.42  ? 163  ASN   B O   1 
ATOM   880   C  CB  . ASN   A 1 163  ? 111.865 135.175 161.831 1.00 43.12  ? 163  ASN   B CB  1 
ATOM   881   C  CG  . ASN   A 1 163  ? 110.843 134.142 161.415 1.00 43.95  ? 163  ASN   B CG  1 
ATOM   882   O  OD1 . ASN   A 1 163  ? 110.911 133.593 160.316 1.00 46.16  ? 163  ASN   B OD1 1 
ATOM   883   N  ND2 . ASN   A 1 163  ? 109.883 133.874 162.291 1.00 50.13  ? 163  ASN   B ND2 1 
ATOM   884   N  N   . TYR   A 1 164  ? 115.441 135.939 161.211 1.00 31.11  ? 164  TYR   B N   1 
ATOM   885   C  CA  . TYR   A 1 164  ? 116.392 137.043 161.121 1.00 32.11  ? 164  TYR   B CA  1 
ATOM   886   C  C   . TYR   A 1 164  ? 117.086 136.943 159.769 1.00 34.68  ? 164  TYR   B C   1 
ATOM   887   O  O   . TYR   A 1 164  ? 118.017 136.151 159.597 1.00 42.84  ? 164  TYR   B O   1 
ATOM   888   C  CB  . TYR   A 1 164  ? 117.395 137.008 162.267 1.00 33.87  ? 164  TYR   B CB  1 
ATOM   889   C  CG  . TYR   A 1 164  ? 118.045 138.341 162.536 1.00 33.30  ? 164  TYR   B CG  1 
ATOM   890   C  CD1 . TYR   A 1 164  ? 119.004 138.853 161.676 1.00 34.42  ? 164  TYR   B CD1 1 
ATOM   891   C  CD2 . TYR   A 1 164  ? 117.703 139.086 163.651 1.00 34.53  ? 164  TYR   B CD2 1 
ATOM   892   C  CE1 . TYR   A 1 164  ? 119.597 140.069 161.917 1.00 30.67  ? 164  TYR   B CE1 1 
ATOM   893   C  CE2 . TYR   A 1 164  ? 118.294 140.301 163.901 1.00 35.94  ? 164  TYR   B CE2 1 
ATOM   894   C  CZ  . TYR   A 1 164  ? 119.240 140.788 163.030 1.00 36.31  ? 164  TYR   B CZ  1 
ATOM   895   O  OH  . TYR   A 1 164  ? 119.834 142.002 163.275 1.00 49.56  ? 164  TYR   B OH  1 
ATOM   896   N  N   . TYR   A 1 165  ? 116.639 137.754 158.814 1.00 39.68  ? 165  TYR   B N   1 
ATOM   897   C  CA  . TYR   A 1 165  ? 117.134 137.689 157.441 1.00 33.69  ? 165  TYR   B CA  1 
ATOM   898   C  C   . TYR   A 1 165  ? 118.398 138.532 157.319 1.00 35.23  ? 165  TYR   B C   1 
ATOM   899   O  O   . TYR   A 1 165  ? 118.373 139.709 156.956 1.00 48.54  ? 165  TYR   B O   1 
ATOM   900   C  CB  . TYR   A 1 165  ? 116.055 138.139 156.467 1.00 34.18  ? 165  TYR   B CB  1 
ATOM   901   C  CG  . TYR   A 1 165  ? 114.942 137.136 156.300 1.00 38.20  ? 165  TYR   B CG  1 
ATOM   902   C  CD1 . TYR   A 1 165  ? 113.917 137.046 157.227 1.00 38.34  ? 165  TYR   B CD1 1 
ATOM   903   C  CD2 . TYR   A 1 165  ? 114.921 136.273 155.217 1.00 40.56  ? 165  TYR   B CD2 1 
ATOM   904   C  CE1 . TYR   A 1 165  ? 112.904 136.126 157.079 1.00 38.96  ? 165  TYR   B CE1 1 
ATOM   905   C  CE2 . TYR   A 1 165  ? 113.912 135.351 155.061 1.00 41.94  ? 165  TYR   B CE2 1 
ATOM   906   C  CZ  . TYR   A 1 165  ? 112.906 135.282 155.994 1.00 42.71  ? 165  TYR   B CZ  1 
ATOM   907   O  OH  . TYR   A 1 165  ? 111.895 134.363 155.841 1.00 48.06  ? 165  TYR   B OH  1 
ATOM   908   N  N   . GLN   A 1 166  ? 119.532 137.907 157.637 1.00 39.84  ? 166  GLN   B N   1 
ATOM   909   C  CA  . GLN   A 1 166  ? 120.819 138.518 157.339 1.00 37.20  ? 166  GLN   B CA  1 
ATOM   910   C  C   . GLN   A 1 166  ? 121.175 138.404 155.865 1.00 39.72  ? 166  GLN   B C   1 
ATOM   911   O  O   . GLN   A 1 166  ? 122.049 139.136 155.392 1.00 46.78  ? 166  GLN   B O   1 
ATOM   912   C  CB  . GLN   A 1 166  ? 121.925 137.885 158.179 1.00 39.66  ? 166  GLN   B CB  1 
ATOM   913   C  CG  . GLN   A 1 166  ? 122.093 138.488 159.552 1.00 38.76  ? 166  GLN   B CG  1 
ATOM   914   C  CD  . GLN   A 1 166  ? 123.483 138.275 160.104 1.00 44.69  ? 166  GLN   B CD  1 
ATOM   915   O  OE1 . GLN   A 1 166  ? 124.125 137.265 159.822 1.00 48.31  ? 166  GLN   B OE1 1 
ATOM   916   N  NE2 . GLN   A 1 166  ? 123.963 139.230 160.886 1.00 43.42  ? 166  GLN   B NE2 1 
ATOM   917   N  N   . ASN   A 1 167  ? 120.513 137.515 155.134 1.00 37.39  ? 167  ASN   B N   1 
ATOM   918   C  CA  . ASN   A 1 167  ? 120.802 137.277 153.730 1.00 39.01  ? 167  ASN   B CA  1 
ATOM   919   C  C   . ASN   A 1 167  ? 120.027 138.199 152.802 1.00 43.82  ? 167  ASN   B C   1 
ATOM   920   O  O   . ASN   A 1 167  ? 120.134 138.058 151.581 1.00 51.98  ? 167  ASN   B O   1 
ATOM   921   C  CB  . ASN   A 1 167  ? 120.512 135.816 153.381 1.00 43.63  ? 167  ASN   B CB  1 
ATOM   922   C  CG  . ASN   A 1 167  ? 119.232 135.314 154.010 1.00 44.96  ? 167  ASN   B CG  1 
ATOM   923   O  OD1 . ASN   A 1 167  ? 118.700 135.926 154.934 1.00 52.34  ? 167  ASN   B OD1 1 
ATOM   924   N  ND2 . ASN   A 1 167  ? 118.735 134.187 153.522 1.00 46.86  ? 167  ASN   B ND2 1 
ATOM   925   N  N   . HIS   A 1 168  ? 119.255 139.134 153.345 1.00 38.65  ? 168  HIS   B N   1 
ATOM   926   C  CA  . HIS   A 1 168  ? 118.559 140.105 152.516 1.00 36.27  ? 168  HIS   B CA  1 
ATOM   927   C  C   . HIS   A 1 168  ? 119.565 140.990 151.791 1.00 44.24  ? 168  HIS   B C   1 
ATOM   928   O  O   . HIS   A 1 168  ? 120.650 141.279 152.300 1.00 51.61  ? 168  HIS   B O   1 
ATOM   929   C  CB  . HIS   A 1 168  ? 117.620 140.954 153.368 1.00 37.75  ? 168  HIS   B CB  1 
ATOM   930   C  CG  . HIS   A 1 168  ? 116.520 141.607 152.593 1.00 43.59  ? 168  HIS   B CG  1 
ATOM   931   N  ND1 . HIS   A 1 168  ? 116.623 142.883 152.085 1.00 50.21  ? 168  HIS   B ND1 1 
ATOM   932   C  CD2 . HIS   A 1 168  ? 115.289 141.164 152.249 1.00 45.50  ? 168  HIS   B CD2 1 
ATOM   933   C  CE1 . HIS   A 1 168  ? 115.505 143.196 151.455 1.00 50.77  ? 168  HIS   B CE1 1 
ATOM   934   N  NE2 . HIS   A 1 168  ? 114.680 142.169 151.539 1.00 49.44  ? 168  HIS   B NE2 1 
ATOM   935   N  N   . ARG   A 1 169  ? 119.195 141.419 150.581 1.00 46.22  ? 169  ARG   B N   1 
ATOM   936   C  CA  . ARG   A 1 169  ? 120.140 142.141 149.733 1.00 43.82  ? 169  ARG   B CA  1 
ATOM   937   C  C   . ARG   A 1 169  ? 120.565 143.460 150.362 1.00 44.41  ? 169  ARG   B C   1 
ATOM   938   O  O   . ARG   A 1 169  ? 121.733 143.852 150.261 1.00 48.47  ? 169  ARG   B O   1 
ATOM   939   C  CB  . ARG   A 1 169  ? 119.536 142.380 148.353 1.00 38.09  ? 169  ARG   B CB  1 
ATOM   940   C  CG  . ARG   A 1 169  ? 120.574 142.420 147.254 1.00 40.16  ? 169  ARG   B CG  1 
ATOM   941   C  CD  . ARG   A 1 169  ? 119.992 142.903 145.947 1.00 43.12  ? 169  ARG   B CD  1 
ATOM   942   N  NE  . ARG   A 1 169  ? 120.781 142.437 144.815 1.00 45.93  ? 169  ARG   B NE  1 
ATOM   943   C  CZ  . ARG   A 1 169  ? 121.904 143.004 144.398 1.00 48.67  ? 169  ARG   B CZ  1 
ATOM   944   N  NH1 . ARG   A 1 169  ? 122.409 144.065 145.006 1.00 46.80  ? 169  ARG   B NH1 1 
ATOM   945   N  NH2 . ARG   A 1 169  ? 122.537 142.493 143.347 1.00 46.01  ? 169  ARG   B NH2 1 
ATOM   946   N  N   . ARG   A 1 170  ? 119.632 144.165 151.003 1.00 37.37  ? 170  ARG   B N   1 
ATOM   947   C  CA  . ARG   A 1 170  ? 119.984 145.409 151.678 1.00 33.65  ? 170  ARG   B CA  1 
ATOM   948   C  C   . ARG   A 1 170  ? 120.981 145.165 152.800 1.00 46.09  ? 170  ARG   B C   1 
ATOM   949   O  O   . ARG   A 1 170  ? 121.930 145.937 152.978 1.00 52.53  ? 170  ARG   B O   1 
ATOM   950   C  CB  . ARG   A 1 170  ? 118.731 146.080 152.232 1.00 36.12  ? 170  ARG   B CB  1 
ATOM   951   C  CG  . ARG   A 1 170  ? 117.799 146.635 151.186 1.00 49.08  ? 170  ARG   B CG  1 
ATOM   952   C  CD  . ARG   A 1 170  ? 116.761 147.512 151.846 1.00 45.72  ? 170  ARG   B CD  1 
ATOM   953   N  NE  . ARG   A 1 170  ? 117.378 148.410 152.813 1.00 41.99  ? 170  ARG   B NE  1 
ATOM   954   C  CZ  . ARG   A 1 170  ? 116.720 149.317 153.519 1.00 39.12  ? 170  ARG   B CZ  1 
ATOM   955   N  NH1 . ARG   A 1 170  ? 115.415 149.483 153.384 1.00 42.71  ? 170  ARG   B NH1 1 
ATOM   956   N  NH2 . ARG   A 1 170  ? 117.386 150.075 154.381 1.00 44.33  ? 170  ARG   B NH2 1 
ATOM   957   N  N   . TYR   A 1 171  ? 120.784 144.093 153.565 1.00 46.05  ? 171  TYR   B N   1 
ATOM   958   C  CA  . TYR   A 1 171  ? 121.592 143.847 154.751 1.00 43.62  ? 171  TYR   B CA  1 
ATOM   959   C  C   . TYR   A 1 171  ? 122.913 143.171 154.408 1.00 44.52  ? 171  TYR   B C   1 
ATOM   960   O  O   . TYR   A 1 171  ? 123.946 143.491 155.003 1.00 54.45  ? 171  TYR   B O   1 
ATOM   961   C  CB  . TYR   A 1 171  ? 120.792 142.994 155.736 1.00 45.10  ? 171  TYR   B CB  1 
ATOM   962   C  CG  . TYR   A 1 171  ? 121.396 142.856 157.112 1.00 43.04  ? 171  TYR   B CG  1 
ATOM   963   C  CD1 . TYR   A 1 171  ? 122.362 141.897 157.376 1.00 46.10  ? 171  TYR   B CD1 1 
ATOM   964   C  CD2 . TYR   A 1 171  ? 120.979 143.666 158.154 1.00 39.94  ? 171  TYR   B CD2 1 
ATOM   965   C  CE1 . TYR   A 1 171  ? 122.907 141.764 158.631 1.00 42.42  ? 171  TYR   B CE1 1 
ATOM   966   C  CE2 . TYR   A 1 171  ? 121.517 143.537 159.413 1.00 46.01  ? 171  TYR   B CE2 1 
ATOM   967   C  CZ  . TYR   A 1 171  ? 122.481 142.583 159.647 1.00 48.48  ? 171  TYR   B CZ  1 
ATOM   968   O  OH  . TYR   A 1 171  ? 123.023 142.452 160.903 1.00 55.91  ? 171  TYR   B OH  1 
ATOM   969   N  N   . SER   A 1 172  ? 122.900 142.241 153.451 1.00 47.48  ? 172  SER   B N   1 
ATOM   970   C  CA  . SER   A 1 172  ? 124.070 141.400 153.213 1.00 46.11  ? 172  SER   B CA  1 
ATOM   971   C  C   . SER   A 1 172  ? 125.273 142.205 152.742 1.00 51.69  ? 172  SER   B C   1 
ATOM   972   O  O   . SER   A 1 172  ? 126.416 141.811 152.996 1.00 57.91  ? 172  SER   B O   1 
ATOM   973   C  CB  . SER   A 1 172  ? 123.731 140.311 152.197 1.00 49.12  ? 172  SER   B CB  1 
ATOM   974   O  OG  . SER   A 1 172  ? 123.282 140.874 150.977 1.00 56.84  ? 172  SER   B OG  1 
ATOM   975   N  N   . SER   A 1 173  ? 125.045 143.324 152.060 1.00 49.70  ? 173  SER   B N   1 
ATOM   976   C  CA  . SER   A 1 173  ? 126.125 144.131 151.511 1.00 48.60  ? 173  SER   B CA  1 
ATOM   977   C  C   . SER   A 1 173  ? 126.239 145.498 152.173 1.00 50.60  ? 173  SER   B C   1 
ATOM   978   O  O   . SER   A 1 173  ? 126.935 146.372 151.647 1.00 58.42  ? 173  SER   B O   1 
ATOM   979   C  CB  . SER   A 1 173  ? 125.941 144.293 150.003 1.00 54.91  ? 173  SER   B CB  1 
ATOM   980   O  OG  . SER   A 1 173  ? 124.671 144.846 149.705 1.00 54.04  ? 173  SER   B OG  1 
ATOM   981   N  N   . SER   A 1 174  ? 125.580 145.706 153.311 1.00 45.91  ? 174  SER   B N   1 
ATOM   982   C  CA  . SER   A 1 174  ? 125.571 147.012 153.971 1.00 44.46  ? 174  SER   B CA  1 
ATOM   983   C  C   . SER   A 1 174  ? 126.749 147.112 154.938 1.00 47.59  ? 174  SER   B C   1 
ATOM   984   O  O   . SER   A 1 174  ? 126.608 147.084 156.161 1.00 54.98  ? 174  SER   B O   1 
ATOM   985   C  CB  . SER   A 1 174  ? 124.242 147.241 154.677 1.00 52.04  ? 174  SER   B CB  1 
ATOM   986   O  OG  . SER   A 1 174  ? 124.162 148.554 155.200 1.00 58.12  ? 174  SER   B OG  1 
ATOM   987   N  N   . PHE   A 1 175  ? 127.938 147.222 154.353 1.00 44.00  ? 175  PHE   B N   1 
ATOM   988   C  CA  . PHE   A 1 175  ? 129.152 147.464 155.118 1.00 48.37  ? 175  PHE   B CA  1 
ATOM   989   C  C   . PHE   A 1 175  ? 130.210 148.008 154.173 1.00 51.04  ? 175  PHE   B C   1 
ATOM   990   O  O   . PHE   A 1 175  ? 130.144 147.808 152.958 1.00 51.38  ? 175  PHE   B O   1 
ATOM   991   C  CB  . PHE   A 1 175  ? 129.645 146.197 155.825 1.00 46.33  ? 175  PHE   B CB  1 
ATOM   992   C  CG  . PHE   A 1 175  ? 130.064 145.099 154.891 1.00 49.91  ? 175  PHE   B CG  1 
ATOM   993   C  CD1 . PHE   A 1 175  ? 129.126 144.252 154.329 1.00 52.95  ? 175  PHE   B CD1 1 
ATOM   994   C  CD2 . PHE   A 1 175  ? 131.396 144.908 154.585 1.00 50.06  ? 175  PHE   B CD2 1 
ATOM   995   C  CE1 . PHE   A 1 175  ? 129.511 143.244 153.472 1.00 52.38  ? 175  PHE   B CE1 1 
ATOM   996   C  CE2 . PHE   A 1 175  ? 131.785 143.905 153.730 1.00 53.78  ? 175  PHE   B CE2 1 
ATOM   997   C  CZ  . PHE   A 1 175  ? 130.842 143.071 153.173 1.00 52.76  ? 175  PHE   B CZ  1 
ATOM   998   N  N   . ASP   A 1 176  ? 131.186 148.704 154.746 1.00 54.12  ? 176  ASP   B N   1 
ATOM   999   C  CA  . ASP   A 1 176  ? 132.293 149.276 153.986 1.00 53.53  ? 176  ASP   B CA  1 
ATOM   1000  C  C   . ASP   A 1 176  ? 133.579 148.612 154.454 1.00 58.99  ? 176  ASP   B C   1 
ATOM   1001  O  O   . ASP   A 1 176  ? 134.098 148.942 155.526 1.00 63.09  ? 176  ASP   B O   1 
ATOM   1002  C  CB  . ASP   A 1 176  ? 132.359 150.792 154.162 1.00 52.21  ? 176  ASP   B CB  1 
ATOM   1003  C  CG  . ASP   A 1 176  ? 133.216 151.462 153.108 1.00 61.48  ? 176  ASP   B CG  1 
ATOM   1004  O  OD1 . ASP   A 1 176  ? 132.753 151.583 151.955 1.00 60.12  ? 176  ASP   B OD1 1 
ATOM   1005  O  OD2 . ASP   A 1 176  ? 134.352 151.866 153.429 1.00 67.02  ? 176  ASP   B OD2 1 
ATOM   1006  N  N   . ALA   A 1 177  ? 134.091 147.679 153.650 1.00 48.75  ? 177  ALA   B N   1 
ATOM   1007  C  CA  . ALA   A 1 177  ? 135.312 146.973 154.021 1.00 46.21  ? 177  ALA   B CA  1 
ATOM   1008  C  C   . ALA   A 1 177  ? 136.500 147.922 154.083 1.00 51.14  ? 177  ALA   B C   1 
ATOM   1009  O  O   . ALA   A 1 177  ? 137.391 147.759 154.926 1.00 53.29  ? 177  ALA   B O   1 
ATOM   1010  C  CB  . ALA   A 1 177  ? 135.581 145.839 153.034 1.00 49.66  ? 177  ALA   B CB  1 
ATOM   1011  N  N   . THR   A 1 178  ? 136.531 148.918 153.196 1.00 50.69  ? 178  THR   B N   1 
ATOM   1012  C  CA  . THR   A 1 178  ? 137.650 149.854 153.168 1.00 47.95  ? 178  THR   B CA  1 
ATOM   1013  C  C   . THR   A 1 178  ? 137.726 150.669 154.453 1.00 52.02  ? 178  THR   B C   1 
ATOM   1014  O  O   . THR   A 1 178  ? 138.819 150.908 154.980 1.00 59.19  ? 178  THR   B O   1 
ATOM   1015  C  CB  . THR   A 1 178  ? 137.531 150.772 151.953 1.00 53.33  ? 178  THR   B CB  1 
ATOM   1016  O  OG1 . THR   A 1 178  ? 137.383 149.978 150.770 1.00 57.23  ? 178  THR   B OG1 1 
ATOM   1017  C  CG2 . THR   A 1 178  ? 138.770 151.636 151.817 1.00 55.67  ? 178  THR   B CG2 1 
ATOM   1018  N  N   . GLN   A 1 179  ? 136.580 151.112 154.972 1.00 50.21  ? 179  GLN   B N   1 
ATOM   1019  C  CA  . GLN   A 1 179  ? 136.588 151.845 156.233 1.00 50.27  ? 179  GLN   B CA  1 
ATOM   1020  C  C   . GLN   A 1 179  ? 136.913 150.928 157.401 1.00 56.42  ? 179  GLN   B C   1 
ATOM   1021  O  O   . GLN   A 1 179  ? 137.634 151.321 158.325 1.00 62.95  ? 179  GLN   B O   1 
ATOM   1022  C  CB  . GLN   A 1 179  ? 135.244 152.531 156.461 1.00 49.13  ? 179  GLN   B CB  1 
ATOM   1023  C  CG  . GLN   A 1 179  ? 135.217 153.403 157.701 1.00 52.22  ? 179  GLN   B CG  1 
ATOM   1024  C  CD  . GLN   A 1 179  ? 133.834 153.911 158.031 1.00 56.22  ? 179  GLN   B CD  1 
ATOM   1025  O  OE1 . GLN   A 1 179  ? 132.849 153.186 157.904 1.00 57.17  ? 179  GLN   B OE1 1 
ATOM   1026  N  NE2 . GLN   A 1 179  ? 133.750 155.165 158.455 1.00 55.17  ? 179  GLN   B NE2 1 
ATOM   1027  N  N   . LEU   A 1 180  ? 136.384 149.703 157.380 1.00 49.41  ? 180  LEU   B N   1 
ATOM   1028  C  CA  . LEU   A 1 180  ? 136.626 148.771 158.474 1.00 40.48  ? 180  LEU   B CA  1 
ATOM   1029  C  C   . LEU   A 1 180  ? 138.103 148.419 158.585 1.00 43.83  ? 180  LEU   B C   1 
ATOM   1030  O  O   . LEU   A 1 180  ? 138.643 148.321 159.692 1.00 48.55  ? 180  LEU   B O   1 
ATOM   1031  C  CB  . LEU   A 1 180  ? 135.782 147.512 158.285 1.00 45.51  ? 180  LEU   B CB  1 
ATOM   1032  C  CG  . LEU   A 1 180  ? 134.279 147.681 158.501 1.00 42.90  ? 180  LEU   B CG  1 
ATOM   1033  C  CD1 . LEU   A 1 180  ? 133.541 146.388 158.211 1.00 48.17  ? 180  LEU   B CD1 1 
ATOM   1034  C  CD2 . LEU   A 1 180  ? 134.013 148.143 159.915 1.00 43.74  ? 180  LEU   B CD2 1 
ATOM   1035  N  N   . ILE   A 1 181  ? 138.776 148.228 157.448 1.00 51.10  ? 181  ILE   B N   1 
ATOM   1036  C  CA  . ILE   A 1 181  ? 140.189 147.867 157.470 1.00 50.72  ? 181  ILE   B CA  1 
ATOM   1037  C  C   . ILE   A 1 181  ? 141.084 149.017 157.905 1.00 50.38  ? 181  ILE   B C   1 
ATOM   1038  O  O   . ILE   A 1 181  ? 142.271 148.800 158.170 1.00 55.52  ? 181  ILE   B O   1 
ATOM   1039  C  CB  . ILE   A 1 181  ? 140.624 147.339 156.088 1.00 49.20  ? 181  ILE   B CB  1 
ATOM   1040  C  CG1 . ILE   A 1 181  ? 141.832 146.413 156.226 1.00 47.88  ? 181  ILE   B CG1 1 
ATOM   1041  C  CG2 . ILE   A 1 181  ? 140.934 148.487 155.147 1.00 53.01  ? 181  ILE   B CG2 1 
ATOM   1042  C  CD1 . ILE   A 1 181  ? 142.326 145.863 154.914 1.00 51.46  ? 181  ILE   B CD1 1 
ATOM   1043  N  N   . GLY   A 1 182  ? 140.549 150.229 157.998 1.00 52.22  ? 182  GLY   B N   1 
ATOM   1044  C  CA  . GLY   A 1 182  ? 141.310 151.367 158.463 1.00 54.95  ? 182  GLY   B CA  1 
ATOM   1045  C  C   . GLY   A 1 182  ? 141.867 152.276 157.392 1.00 60.48  ? 182  GLY   B C   1 
ATOM   1046  O  O   . GLY   A 1 182  ? 142.640 153.182 157.721 1.00 62.39  ? 182  GLY   B O   1 
ATOM   1047  N  N   . ASP   A 1 183  ? 141.507 152.067 156.129 1.00 60.71  ? 183  ASP   B N   1 
ATOM   1048  C  CA  . ASP   A 1 183  ? 142.013 152.906 155.056 1.00 56.09  ? 183  ASP   B CA  1 
ATOM   1049  C  C   . ASP   A 1 183  ? 141.344 154.278 155.088 1.00 62.11  ? 183  ASP   B C   1 
ATOM   1050  O  O   . ASP   A 1 183  ? 140.351 154.506 155.785 1.00 66.00  ? 183  ASP   B O   1 
ATOM   1051  C  CB  . ASP   A 1 183  ? 141.791 152.240 153.700 1.00 58.89  ? 183  ASP   B CB  1 
ATOM   1052  C  CG  . ASP   A 1 183  ? 142.658 151.014 153.506 1.00 66.96  ? 183  ASP   B CG  1 
ATOM   1053  O  OD1 . ASP   A 1 183  ? 143.470 150.710 154.405 1.00 66.99  ? 183  ASP   B OD1 1 
ATOM   1054  O  OD2 . ASP   A 1 183  ? 142.528 150.353 152.455 1.00 66.87  ? 183  ASP   B OD2 1 
ATOM   1055  N  N   . SER   A 1 184  ? 141.907 155.203 154.315 1.00 67.16  ? 184  SER   B N   1 
ATOM   1056  C  CA  . SER   A 1 184  ? 141.422 156.577 154.274 1.00 65.17  ? 184  SER   B CA  1 
ATOM   1057  C  C   . SER   A 1 184  ? 140.208 156.654 153.356 1.00 66.94  ? 184  SER   B C   1 
ATOM   1058  O  O   . SER   A 1 184  ? 140.331 156.514 152.135 1.00 68.32  ? 184  SER   B O   1 
ATOM   1059  C  CB  . SER   A 1 184  ? 142.528 157.516 153.803 1.00 65.70  ? 184  SER   B CB  1 
ATOM   1060  O  OG  . SER   A 1 184  ? 142.077 158.858 153.767 1.00 65.71  ? 184  SER   B OG  1 
ATOM   1061  N  N   . ARG   A 1 185  ? 139.036 156.876 153.944 1.00 57.15  ? 185  ARG   B N   1 
ATOM   1062  C  CA  . ARG   A 1 185  ? 137.790 157.033 153.210 1.00 55.16  ? 185  ARG   B CA  1 
ATOM   1063  C  C   . ARG   A 1 185  ? 137.223 158.415 153.493 1.00 61.86  ? 185  ARG   B C   1 
ATOM   1064  O  O   . ARG   A 1 185  ? 137.101 158.813 154.656 1.00 64.02  ? 185  ARG   B O   1 
ATOM   1065  C  CB  . ARG   A 1 185  ? 136.779 155.951 153.600 1.00 56.04  ? 185  ARG   B CB  1 
ATOM   1066  C  CG  . ARG   A 1 185  ? 136.825 154.707 152.735 1.00 53.34  ? 185  ARG   B CG  1 
ATOM   1067  C  CD  . ARG   A 1 185  ? 136.073 154.926 151.441 1.00 55.85  ? 185  ARG   B CD  1 
ATOM   1068  N  NE  . ARG   A 1 185  ? 136.106 153.760 150.568 1.00 60.91  ? 185  ARG   B NE  1 
ATOM   1069  C  CZ  . ARG   A 1 185  ? 136.953 153.604 149.561 1.00 63.55  ? 185  ARG   B CZ  1 
ATOM   1070  N  NH1 . ARG   A 1 185  ? 137.860 154.522 149.273 1.00 61.39  ? 185  ARG   B NH1 1 
ATOM   1071  N  NH2 . ARG   A 1 185  ? 136.888 152.499 148.824 1.00 62.41  ? 185  ARG   B NH2 1 
ATOM   1072  N  N   . SER   A 1 186  ? 136.882 159.144 152.434 1.00 63.19  ? 186  SER   B N   1 
ATOM   1073  C  CA  . SER   A 1 186  ? 136.314 160.472 152.584 1.00 60.88  ? 186  SER   B CA  1 
ATOM   1074  C  C   . SER   A 1 186  ? 134.803 160.386 152.789 1.00 62.84  ? 186  SER   B C   1 
ATOM   1075  O  O   . SER   A 1 186  ? 134.192 159.319 152.692 1.00 66.71  ? 186  SER   B O   1 
ATOM   1076  C  CB  . SER   A 1 186  ? 136.638 161.335 151.367 1.00 62.89  ? 186  SER   B CB  1 
ATOM   1077  O  OG  . SER   A 1 186  ? 136.069 160.790 150.190 1.00 62.48  ? 186  SER   B OG  1 
ATOM   1078  N  N   . LEU   A 1 187  ? 134.200 161.540 153.082 1.00 59.97  ? 187  LEU   B N   1 
ATOM   1079  C  CA  . LEU   A 1 187  ? 132.761 161.582 153.320 1.00 58.76  ? 187  LEU   B CA  1 
ATOM   1080  C  C   . LEU   A 1 187  ? 131.980 161.210 152.067 1.00 63.19  ? 187  LEU   B C   1 
ATOM   1081  O  O   . LEU   A 1 187  ? 130.988 160.476 152.139 1.00 67.60  ? 187  LEU   B O   1 
ATOM   1082  C  CB  . LEU   A 1 187  ? 132.353 162.966 153.818 1.00 59.77  ? 187  LEU   B CB  1 
ATOM   1083  C  CG  . LEU   A 1 187  ? 130.883 163.132 154.197 1.00 58.02  ? 187  LEU   B CG  1 
ATOM   1084  C  CD1 . LEU   A 1 187  ? 130.520 162.185 155.319 1.00 59.31  ? 187  LEU   B CD1 1 
ATOM   1085  C  CD2 . LEU   A 1 187  ? 130.590 164.567 154.593 1.00 62.96  ? 187  LEU   B CD2 1 
ATOM   1086  N  N   . SER   A 1 188  ? 132.407 161.710 150.906 1.00 58.04  ? 188  SER   B N   1 
ATOM   1087  C  CA  . SER   A 1 188  ? 131.717 161.375 149.666 1.00 55.38  ? 188  SER   B CA  1 
ATOM   1088  C  C   . SER   A 1 188  ? 131.828 159.887 149.360 1.00 62.84  ? 188  SER   B C   1 
ATOM   1089  O  O   . SER   A 1 188  ? 130.856 159.261 148.918 1.00 67.66  ? 188  SER   B O   1 
ATOM   1090  C  CB  . SER   A 1 188  ? 132.278 162.204 148.513 1.00 62.65  ? 188  SER   B CB  1 
ATOM   1091  O  OG  . SER   A 1 188  ? 132.128 163.590 148.764 1.00 67.51  ? 188  SER   B OG  1 
ATOM   1092  N  N   . GLN   A 1 189  ? 133.006 159.304 149.590 1.00 57.64  ? 189  GLN   B N   1 
ATOM   1093  C  CA  . GLN   A 1 189  ? 133.203 157.888 149.300 1.00 54.78  ? 189  GLN   B CA  1 
ATOM   1094  C  C   . GLN   A 1 189  ? 132.336 157.006 150.190 1.00 59.14  ? 189  GLN   B C   1 
ATOM   1095  O  O   . GLN   A 1 189  ? 131.741 156.033 149.714 1.00 60.51  ? 189  GLN   B O   1 
ATOM   1096  C  CB  . GLN   A 1 189  ? 134.678 157.524 149.452 1.00 53.89  ? 189  GLN   B CB  1 
ATOM   1097  C  CG  . GLN   A 1 189  ? 135.579 158.137 148.400 1.00 57.88  ? 189  GLN   B CG  1 
ATOM   1098  C  CD  . GLN   A 1 189  ? 137.041 157.818 148.630 1.00 59.12  ? 189  GLN   B CD  1 
ATOM   1099  O  OE1 . GLN   A 1 189  ? 137.436 157.420 149.724 1.00 61.08  ? 189  GLN   B OE1 1 
ATOM   1100  N  NE2 . GLN   A 1 189  ? 137.854 157.989 147.595 1.00 58.45  ? 189  GLN   B NE2 1 
ATOM   1101  N  N   . ILE   A 1 190  ? 132.253 157.322 151.484 1.00 55.17  ? 190  ILE   B N   1 
ATOM   1102  C  CA  . ILE   A 1 190  ? 131.426 156.517 152.379 1.00 50.67  ? 190  ILE   B CA  1 
ATOM   1103  C  C   . ILE   A 1 190  ? 129.946 156.754 152.097 1.00 58.38  ? 190  ILE   B C   1 
ATOM   1104  O  O   . ILE   A 1 190  ? 129.120 155.846 152.252 1.00 67.69  ? 190  ILE   B O   1 
ATOM   1105  C  CB  . ILE   A 1 190  ? 131.789 156.790 153.852 1.00 49.46  ? 190  ILE   B CB  1 
ATOM   1106  C  CG1 . ILE   A 1 190  ? 131.040 155.827 154.773 1.00 55.76  ? 190  ILE   B CG1 1 
ATOM   1107  C  CG2 . ILE   A 1 190  ? 131.491 158.221 154.239 1.00 53.05  ? 190  ILE   B CG2 1 
ATOM   1108  C  CD1 . ILE   A 1 190  ? 131.348 156.019 156.240 1.00 57.50  ? 190  ILE   B CD1 1 
ATOM   1109  N  N   . ASN   A 1 191  ? 129.583 157.970 151.679 1.00 56.32  ? 191  ASN   B N   1 
ATOM   1110  C  CA  . ASN   A 1 191  ? 128.196 158.241 151.315 1.00 49.25  ? 191  ASN   B CA  1 
ATOM   1111  C  C   . ASN   A 1 191  ? 127.781 157.449 150.083 1.00 51.93  ? 191  ASN   B C   1 
ATOM   1112  O  O   . ASN   A 1 191  ? 126.660 156.930 150.020 1.00 58.21  ? 191  ASN   B O   1 
ATOM   1113  C  CB  . ASN   A 1 191  ? 127.991 159.736 151.083 1.00 49.96  ? 191  ASN   B CB  1 
ATOM   1114  C  CG  . ASN   A 1 191  ? 127.925 160.522 152.373 1.00 56.24  ? 191  ASN   B CG  1 
ATOM   1115  O  OD1 . ASN   A 1 191  ? 127.479 160.014 153.400 1.00 59.99  ? 191  ASN   B OD1 1 
ATOM   1116  N  ND2 . ASN   A 1 191  ? 128.369 161.771 152.328 1.00 58.54  ? 191  ASN   B ND2 1 
ATOM   1117  N  N   . GLY   A 1 192  ? 128.661 157.350 149.094 1.00 52.70  ? 192  GLY   B N   1 
ATOM   1118  C  CA  . GLY   A 1 192  ? 128.365 156.621 147.883 1.00 51.99  ? 192  GLY   B CA  1 
ATOM   1119  C  C   . GLY   A 1 192  ? 128.713 155.153 147.900 1.00 53.55  ? 192  GLY   B C   1 
ATOM   1120  O  O   . GLY   A 1 192  ? 128.569 154.482 146.875 1.00 58.39  ? 192  GLY   B O   1 
ATOM   1121  N  N   . GLY   A 1 193  ? 129.163 154.624 149.035 1.00 59.23  ? 193  GLY   B N   1 
ATOM   1122  C  CA  . GLY   A 1 193  ? 129.569 153.240 149.134 1.00 59.82  ? 193  GLY   B CA  1 
ATOM   1123  C  C   . GLY   A 1 193  ? 128.396 152.304 149.350 1.00 60.93  ? 193  GLY   B C   1 
ATOM   1124  O  O   . GLY   A 1 193  ? 127.228 152.663 149.193 1.00 67.15  ? 193  GLY   B O   1 
ATOM   1125  N  N   . ASN   A 1 194  ? 128.730 151.068 149.719 1.00 55.73  ? 194  ASN   B N   1 
ATOM   1126  C  CA  . ASN   A 1 194  ? 127.724 150.043 149.957 1.00 54.72  ? 194  ASN   B CA  1 
ATOM   1127  C  C   . ASN   A 1 194  ? 127.123 150.119 151.352 1.00 56.07  ? 194  ASN   B C   1 
ATOM   1128  O  O   . ASN   A 1 194  ? 126.238 149.318 151.670 1.00 54.41  ? 194  ASN   B O   1 
ATOM   1129  C  CB  . ASN   A 1 194  ? 128.324 148.653 149.737 1.00 52.13  ? 194  ASN   B CB  1 
ATOM   1130  C  CG  . ASN   A 1 194  ? 128.756 148.425 148.305 1.00 57.04  ? 194  ASN   B CG  1 
ATOM   1131  O  OD1 . ASN   A 1 194  ? 128.200 149.008 147.375 1.00 61.14  ? 194  ASN   B OD1 1 
ATOM   1132  N  ND2 . ASN   A 1 194  ? 129.753 147.569 148.119 1.00 57.97  ? 194  ASN   B ND2 1 
ATOM   1133  N  N   . CYS   A 1 195  ? 127.574 151.052 152.182 1.00 60.41  ? 195  CYS   B N   1 
ATOM   1134  C  CA  . CYS   A 1 195  ? 127.101 151.207 153.553 1.00 54.99  ? 195  CYS   B CA  1 
ATOM   1135  C  C   . CYS   A 1 195  ? 125.723 151.819 153.645 1.00 56.55  ? 195  CYS   B C   1 
ATOM   1136  O  O   . CYS   A 1 195  ? 125.301 152.138 154.763 1.00 58.62  ? 195  CYS   B O   1 
ATOM   1137  C  CB  . CYS   A 1 195  ? 128.097 152.047 154.354 1.00 56.85  ? 195  CYS   B CB  1 
ATOM   1138  S  SG  . CYS   A 1 195  ? 129.033 151.103 155.574 1.00 76.47  ? 195  CYS   B SG  1 
ATOM   1139  N  N   . LYS   A 1 196  ? 125.010 152.001 152.539 1.00 59.83  ? 196  LYS   B N   1 
ATOM   1140  C  CA  . LYS   A 1 196  ? 123.674 152.566 152.598 1.00 56.13  ? 196  LYS   B CA  1 
ATOM   1141  C  C   . LYS   A 1 196  ? 122.731 151.617 153.336 1.00 56.67  ? 196  LYS   B C   1 
ATOM   1142  O  O   . LYS   A 1 196  ? 122.903 150.396 153.285 1.00 62.16  ? 196  LYS   B O   1 
ATOM   1143  C  CB  . LYS   A 1 196  ? 123.149 152.833 151.191 1.00 57.43  ? 196  LYS   B CB  1 
ATOM   1144  C  CG  . LYS   A 1 196  ? 124.043 153.732 150.355 1.00 60.85  ? 196  LYS   B CG  1 
ATOM   1145  C  CD  . LYS   A 1 196  ? 123.445 153.972 148.978 1.00 62.14  ? 196  LYS   B CD  1 
ATOM   1146  C  CE  . LYS   A 1 196  ? 124.314 154.900 148.147 1.00 61.10  ? 196  LYS   B CE  1 
ATOM   1147  N  NZ  . LYS   A 1 196  ? 125.658 154.316 147.885 1.00 61.08  ? 196  LYS   B NZ  1 
ATOM   1148  N  N   . PRO   A 1 197  ? 121.718 152.152 154.030 1.00 48.79  ? 197  PRO   B N   1 
ATOM   1149  C  CA  . PRO   A 1 197  ? 121.352 153.566 154.171 1.00 48.56  ? 197  PRO   B CA  1 
ATOM   1150  C  C   . PRO   A 1 197  ? 122.006 154.271 155.354 1.00 53.57  ? 197  PRO   B C   1 
ATOM   1151  O  O   . PRO   A 1 197  ? 121.743 155.447 155.587 1.00 61.57  ? 197  PRO   B O   1 
ATOM   1152  C  CB  . PRO   A 1 197  ? 119.837 153.488 154.352 1.00 49.15  ? 197  PRO   B CB  1 
ATOM   1153  C  CG  . PRO   A 1 197  ? 119.667 152.248 155.175 1.00 52.05  ? 197  PRO   B CG  1 
ATOM   1154  C  CD  . PRO   A 1 197  ? 120.714 151.281 154.664 1.00 56.38  ? 197  PRO   B CD  1 
ATOM   1155  N  N   . ILE   A 1 198  ? 122.850 153.596 156.124 1.00 53.59  ? 198  ILE   B N   1 
ATOM   1156  C  CA  . ILE   A 1 198  ? 123.487 154.192 157.297 1.00 49.16  ? 198  ILE   B CA  1 
ATOM   1157  C  C   . ILE   A 1 198  ? 124.895 154.588 156.866 1.00 57.47  ? 198  ILE   B C   1 
ATOM   1158  O  O   . ILE   A 1 198  ? 125.843 153.807 156.963 1.00 62.72  ? 198  ILE   B O   1 
ATOM   1159  C  CB  . ILE   A 1 198  ? 123.488 153.240 158.490 1.00 50.08  ? 198  ILE   B CB  1 
ATOM   1160  C  CG1 . ILE   A 1 198  ? 122.063 152.789 158.806 1.00 54.85  ? 198  ILE   B CG1 1 
ATOM   1161  C  CG2 . ILE   A 1 198  ? 124.102 153.904 159.704 1.00 54.34  ? 198  ILE   B CG2 1 
ATOM   1162  C  CD1 . ILE   A 1 198  ? 121.966 151.855 159.980 1.00 55.16  ? 198  ILE   B CD1 1 
ATOM   1163  N  N   . THR   A 1 199  ? 125.035 155.822 156.381 1.00 56.92  ? 199  THR   B N   1 
ATOM   1164  C  CA  . THR   A 1 199  ? 126.315 156.308 155.874 1.00 51.81  ? 199  THR   B CA  1 
ATOM   1165  C  C   . THR   A 1 199  ? 126.876 157.449 156.712 1.00 54.15  ? 199  THR   B C   1 
ATOM   1166  O  O   . THR   A 1 199  ? 127.998 157.337 157.214 1.00 63.68  ? 199  THR   B O   1 
ATOM   1167  C  CB  . THR   A 1 199  ? 126.168 156.740 154.411 1.00 54.28  ? 199  THR   B CB  1 
ATOM   1168  O  OG1 . THR   A 1 199  ? 125.153 157.747 154.309 1.00 59.39  ? 199  THR   B OG1 1 
ATOM   1169  C  CG2 . THR   A 1 199  ? 125.784 155.554 153.544 1.00 58.36  ? 199  THR   B CG2 1 
ATOM   1170  N  N   . SER   A 1 200  ? 126.135 158.538 156.889 1.00 59.67  ? 200  SER   B N   1 
ATOM   1171  C  CA  . SER   A 1 200  ? 126.642 159.689 157.625 1.00 57.59  ? 200  SER   B CA  1 
ATOM   1172  C  C   . SER   A 1 200  ? 125.474 160.579 158.020 1.00 59.68  ? 200  SER   B C   1 
ATOM   1173  O  O   . SER   A 1 200  ? 124.373 160.464 157.475 1.00 65.60  ? 200  SER   B O   1 
ATOM   1174  C  CB  . SER   A 1 200  ? 127.656 160.481 156.798 1.00 61.96  ? 200  SER   B CB  1 
ATOM   1175  O  OG  . SER   A 1 200  ? 127.073 160.949 155.595 1.00 65.95  ? 200  SER   B OG  1 
ATOM   1176  N  N   . ARG   A 1 201  ? 125.731 161.468 158.977 1.00 60.18  ? 201  ARG   B N   1 
ATOM   1177  C  CA  . ARG   A 1 201  ? 124.755 162.471 159.383 1.00 63.13  ? 201  ARG   B CA  1 
ATOM   1178  C  C   . ARG   A 1 201  ? 125.482 163.744 159.781 1.00 64.89  ? 201  ARG   B C   1 
ATOM   1179  O  O   . ARG   A 1 201  ? 126.435 163.696 160.564 1.00 71.35  ? 201  ARG   B O   1 
ATOM   1180  C  CB  . ARG   A 1 201  ? 123.888 161.978 160.545 1.00 59.78  ? 201  ARG   B CB  1 
ATOM   1181  C  CG  . ARG   A 1 201  ? 122.646 161.223 160.112 1.00 66.57  ? 201  ARG   B CG  1 
ATOM   1182  C  CD  . ARG   A 1 201  ? 121.686 161.007 161.270 1.00 67.52  ? 201  ARG   B CD  1 
ATOM   1183  N  NE  . ARG   A 1 201  ? 121.210 162.262 161.840 1.00 67.81  ? 201  ARG   B NE  1 
ATOM   1184  C  CZ  . ARG   A 1 201  ? 121.676 162.803 162.957 1.00 66.74  ? 201  ARG   B CZ  1 
ATOM   1185  N  NH1 . ARG   A 1 201  ? 122.637 162.224 163.657 1.00 67.07  ? 201  ARG   B NH1 1 
ATOM   1186  N  NH2 . ARG   A 1 201  ? 121.163 163.954 163.382 1.00 63.90  ? 201  ARG   B NH2 1 
ATOM   1187  N  N   . ASP   A 1 202  ? 125.028 164.873 159.234 1.00 64.17  ? 202  ASP   B N   1 
ATOM   1188  C  CA  . ASP   A 1 202  ? 125.566 166.195 159.557 1.00 64.06  ? 202  ASP   B CA  1 
ATOM   1189  C  C   . ASP   A 1 202  ? 127.059 166.295 159.262 1.00 66.21  ? 202  ASP   B C   1 
ATOM   1190  O  O   . ASP   A 1 202  ? 127.795 166.991 159.965 1.00 69.30  ? 202  ASP   B O   1 
ATOM   1191  C  CB  . ASP   A 1 202  ? 125.284 166.565 161.015 1.00 68.03  ? 202  ASP   B CB  1 
ATOM   1192  C  CG  . ASP   A 1 202  ? 123.806 166.542 161.345 1.00 73.01  ? 202  ASP   B CG  1 
ATOM   1193  O  OD1 . ASP   A 1 202  ? 122.999 166.241 160.441 1.00 72.60  ? 202  ASP   B OD1 1 
ATOM   1194  O  OD2 . ASP   A 1 202  ? 123.451 166.823 162.509 1.00 73.12  ? 202  ASP   B OD2 1 
ATOM   1195  N  N   . GLY   A 1 203  ? 127.519 165.603 158.223 1.00 62.35  ? 203  GLY   B N   1 
ATOM   1196  C  CA  . GLY   A 1 203  ? 128.911 165.651 157.834 1.00 63.16  ? 203  GLY   B CA  1 
ATOM   1197  C  C   . GLY   A 1 203  ? 129.835 164.754 158.625 1.00 62.86  ? 203  GLY   B C   1 
ATOM   1198  O  O   . GLY   A 1 203  ? 131.039 164.732 158.341 1.00 63.82  ? 203  GLY   B O   1 
ATOM   1199  N  N   . LYS   A 1 204  ? 129.320 164.016 159.602 1.00 60.73  ? 204  LYS   B N   1 
ATOM   1200  C  CA  . LYS   A 1 204  ? 130.136 163.113 160.403 1.00 56.06  ? 204  LYS   B CA  1 
ATOM   1201  C  C   . LYS   A 1 204  ? 129.829 161.673 160.020 1.00 62.93  ? 204  LYS   B C   1 
ATOM   1202  O  O   . LYS   A 1 204  ? 128.705 161.202 160.255 1.00 70.16  ? 204  LYS   B O   1 
ATOM   1203  C  CB  . LYS   A 1 204  ? 129.880 163.339 161.893 1.00 56.40  ? 204  LYS   B CB  1 
ATOM   1204  C  CG  . LYS   A 1 204  ? 130.302 164.714 162.384 1.00 60.89  ? 204  LYS   B CG  1 
ATOM   1205  C  CD  . LYS   A 1 204  ? 130.021 164.889 163.865 1.00 62.31  ? 204  LYS   B CD  1 
ATOM   1206  C  CE  . LYS   A 1 204  ? 128.529 164.881 164.147 1.00 64.52  ? 204  LYS   B CE  1 
ATOM   1207  N  NZ  . LYS   A 1 204  ? 128.237 165.061 165.596 1.00 64.81  ? 204  LYS   B NZ  1 
ATOM   1208  N  N   . PRO   A 1 205  ? 130.772 160.943 159.430 1.00 53.16  ? 205  PRO   B N   1 
ATOM   1209  C  CA  . PRO   A 1 205  ? 130.479 159.579 158.982 1.00 47.80  ? 205  PRO   B CA  1 
ATOM   1210  C  C   . PRO   A 1 205  ? 130.282 158.621 160.146 1.00 56.19  ? 205  PRO   B C   1 
ATOM   1211  O  O   . PRO   A 1 205  ? 130.789 158.830 161.250 1.00 63.89  ? 205  PRO   B O   1 
ATOM   1212  C  CB  . PRO   A 1 205  ? 131.717 159.206 158.164 1.00 51.89  ? 205  PRO   B CB  1 
ATOM   1213  C  CG  . PRO   A 1 205  ? 132.805 160.021 158.765 1.00 57.12  ? 205  PRO   B CG  1 
ATOM   1214  C  CD  . PRO   A 1 205  ? 132.171 161.321 159.170 1.00 55.35  ? 205  PRO   B CD  1 
ATOM   1215  N  N   . TYR   A 1 206  ? 129.531 157.555 159.881 1.00 53.36  ? 206  TYR   B N   1 
ATOM   1216  C  CA  . TYR   A 1 206  ? 129.331 156.498 160.862 1.00 52.13  ? 206  TYR   B CA  1 
ATOM   1217  C  C   . TYR   A 1 206  ? 130.483 155.504 160.807 1.00 58.98  ? 206  TYR   B C   1 
ATOM   1218  O  O   . TYR   A 1 206  ? 130.850 155.026 159.729 1.00 64.54  ? 206  TYR   B O   1 
ATOM   1219  C  CB  . TYR   A 1 206  ? 128.013 155.768 160.611 1.00 49.48  ? 206  TYR   B CB  1 
ATOM   1220  C  CG  . TYR   A 1 206  ? 126.782 156.517 161.051 1.00 50.87  ? 206  TYR   B CG  1 
ATOM   1221  C  CD1 . TYR   A 1 206  ? 126.568 156.813 162.385 1.00 54.87  ? 206  TYR   B CD1 1 
ATOM   1222  C  CD2 . TYR   A 1 206  ? 125.822 156.910 160.133 1.00 56.35  ? 206  TYR   B CD2 1 
ATOM   1223  C  CE1 . TYR   A 1 206  ? 125.443 157.490 162.792 1.00 53.95  ? 206  TYR   B CE1 1 
ATOM   1224  C  CE2 . TYR   A 1 206  ? 124.691 157.585 160.532 1.00 50.94  ? 206  TYR   B CE2 1 
ATOM   1225  C  CZ  . TYR   A 1 206  ? 124.509 157.874 161.864 1.00 45.89  ? 206  TYR   B CZ  1 
ATOM   1226  O  OH  . TYR   A 1 206  ? 123.386 158.547 162.275 1.00 51.71  ? 206  TYR   B OH  1 
ATOM   1227  N  N   . TYR   A 1 207  ? 131.053 155.193 161.968 1.00 51.20  ? 207  TYR   B N   1 
ATOM   1228  C  CA  . TYR   A 1 207  ? 132.059 154.143 162.053 1.00 44.09  ? 207  TYR   B CA  1 
ATOM   1229  C  C   . TYR   A 1 207  ? 131.758 153.217 163.222 1.00 49.95  ? 207  TYR   B C   1 
ATOM   1230  O  O   . TYR   A 1 207  ? 131.754 153.656 164.378 1.00 59.46  ? 207  TYR   B O   1 
ATOM   1231  C  CB  . TYR   A 1 207  ? 133.462 154.729 162.199 1.00 45.67  ? 207  TYR   B CB  1 
ATOM   1232  C  CG  . TYR   A 1 207  ? 134.509 153.687 162.508 1.00 51.95  ? 207  TYR   B CG  1 
ATOM   1233  C  CD1 . TYR   A 1 207  ? 134.989 152.844 161.517 1.00 53.98  ? 207  TYR   B CD1 1 
ATOM   1234  C  CD2 . TYR   A 1 207  ? 135.011 153.538 163.790 1.00 51.92  ? 207  TYR   B CD2 1 
ATOM   1235  C  CE1 . TYR   A 1 207  ? 135.939 151.888 161.793 1.00 49.36  ? 207  TYR   B CE1 1 
ATOM   1236  C  CE2 . TYR   A 1 207  ? 135.962 152.584 164.076 1.00 51.62  ? 207  TYR   B CE2 1 
ATOM   1237  C  CZ  . TYR   A 1 207  ? 136.422 151.761 163.074 1.00 52.77  ? 207  TYR   B CZ  1 
ATOM   1238  O  OH  . TYR   A 1 207  ? 137.372 150.808 163.351 1.00 60.99  ? 207  TYR   B OH  1 
ATOM   1239  N  N   . PRO   A 1 208  ? 131.498 151.932 162.967 1.00 44.65  ? 208  PRO   B N   1 
ATOM   1240  C  CA  . PRO   A 1 208  ? 131.366 151.294 161.653 1.00 42.94  ? 208  PRO   B CA  1 
ATOM   1241  C  C   . PRO   A 1 208  ? 130.000 151.574 161.044 1.00 48.20  ? 208  PRO   B C   1 
ATOM   1242  O  O   . PRO   A 1 208  ? 129.009 151.657 161.762 1.00 58.51  ? 208  PRO   B O   1 
ATOM   1243  C  CB  . PRO   A 1 208  ? 131.571 149.812 161.976 1.00 48.98  ? 208  PRO   B CB  1 
ATOM   1244  C  CG  . PRO   A 1 208  ? 131.043 149.669 163.366 1.00 43.89  ? 208  PRO   B CG  1 
ATOM   1245  C  CD  . PRO   A 1 208  ? 131.403 150.954 164.062 1.00 45.93  ? 208  PRO   B CD  1 
ATOM   1246  N  N   . CYS   A 1 209  ? 129.908 151.726 159.727 1.00 47.60  ? 209  CYS   B N   1 
ATOM   1247  C  CA  . CYS   A 1 209  ? 128.643 152.055 159.097 1.00 47.61  ? 209  CYS   B CA  1 
ATOM   1248  C  C   . CYS   A 1 209  ? 127.934 150.785 158.632 1.00 52.18  ? 209  CYS   B C   1 
ATOM   1249  O  O   . CYS   A 1 209  ? 128.442 149.669 158.765 1.00 60.50  ? 209  CYS   B O   1 
ATOM   1250  C  CB  . CYS   A 1 209  ? 128.860 153.029 157.938 1.00 50.58  ? 209  CYS   B CB  1 
ATOM   1251  S  SG  . CYS   A 1 209  ? 130.030 152.504 156.657 1.00 71.21  ? 209  CYS   B SG  1 
ATOM   1252  N  N   . GLY   A 1 210  ? 126.741 150.959 158.076 1.00 42.91  ? 210  GLY   B N   1 
ATOM   1253  C  CA  . GLY   A 1 210  ? 126.001 149.863 157.494 1.00 45.34  ? 210  GLY   B CA  1 
ATOM   1254  C  C   . GLY   A 1 210  ? 124.993 149.245 158.445 1.00 43.06  ? 210  GLY   B C   1 
ATOM   1255  O  O   . GLY   A 1 210  ? 124.971 149.503 159.650 1.00 52.23  ? 210  GLY   B O   1 
ATOM   1256  N  N   . LEU   A 1 211  ? 124.133 148.405 157.870 1.00 40.91  ? 211  LEU   B N   1 
ATOM   1257  C  CA  . LEU   A 1 211  ? 123.094 147.742 158.645 1.00 39.96  ? 211  LEU   B CA  1 
ATOM   1258  C  C   . LEU   A 1 211  ? 123.642 146.608 159.500 1.00 44.67  ? 211  LEU   B C   1 
ATOM   1259  O  O   . LEU   A 1 211  ? 123.108 146.348 160.584 1.00 47.49  ? 211  LEU   B O   1 
ATOM   1260  C  CB  . LEU   A 1 211  ? 122.005 147.209 157.713 1.00 42.60  ? 211  LEU   B CB  1 
ATOM   1261  C  CG  . LEU   A 1 211  ? 121.183 148.239 156.938 1.00 38.22  ? 211  LEU   B CG  1 
ATOM   1262  C  CD1 . LEU   A 1 211  ? 120.250 147.547 155.967 1.00 44.84  ? 211  LEU   B CD1 1 
ATOM   1263  C  CD2 . LEU   A 1 211  ? 120.399 149.119 157.888 1.00 37.49  ? 211  LEU   B CD2 1 
ATOM   1264  N  N   . ILE   A 1 212  ? 124.685 145.917 159.035 1.00 40.54  ? 212  ILE   B N   1 
ATOM   1265  C  CA  . ILE   A 1 212  ? 125.216 144.781 159.785 1.00 37.48  ? 212  ILE   B CA  1 
ATOM   1266  C  C   . ILE   A 1 212  ? 125.803 145.247 161.109 1.00 45.49  ? 212  ILE   B C   1 
ATOM   1267  O  O   . ILE   A 1 212  ? 125.535 144.668 162.168 1.00 51.11  ? 212  ILE   B O   1 
ATOM   1268  C  CB  . ILE   A 1 212  ? 126.260 144.021 158.949 1.00 44.45  ? 212  ILE   B CB  1 
ATOM   1269  C  CG1 . ILE   A 1 212  ? 125.720 143.722 157.556 1.00 43.87  ? 212  ILE   B CG1 1 
ATOM   1270  C  CG2 . ILE   A 1 212  ? 126.641 142.725 159.638 1.00 48.22  ? 212  ILE   B CG2 1 
ATOM   1271  C  CD1 . ILE   A 1 212  ? 126.691 142.973 156.682 1.00 45.20  ? 212  ILE   B CD1 1 
ATOM   1272  N  N   . ALA   A 1 213  ? 126.618 146.301 161.068 1.00 40.06  ? 213  ALA   B N   1 
ATOM   1273  C  CA  . ALA   A 1 213  ? 127.228 146.808 162.289 1.00 38.05  ? 213  ALA   B CA  1 
ATOM   1274  C  C   . ALA   A 1 213  ? 126.197 147.437 163.213 1.00 43.01  ? 213  ALA   B C   1 
ATOM   1275  O  O   . ALA   A 1 213  ? 126.313 147.324 164.438 1.00 51.67  ? 213  ALA   B O   1 
ATOM   1276  C  CB  . ALA   A 1 213  ? 128.322 147.816 161.947 1.00 43.65  ? 213  ALA   B CB  1 
ATOM   1277  N  N   . ASN   A 1 214  ? 125.188 148.099 162.648 1.00 43.47  ? 214  ASN   B N   1 
ATOM   1278  C  CA  . ASN   A 1 214  ? 124.184 148.769 163.465 1.00 42.64  ? 214  ASN   B CA  1 
ATOM   1279  C  C   . ASN   A 1 214  ? 123.368 147.772 164.275 1.00 47.73  ? 214  ASN   B C   1 
ATOM   1280  O  O   . ASN   A 1 214  ? 122.905 148.088 165.376 1.00 55.18  ? 214  ASN   B O   1 
ATOM   1281  C  CB  . ASN   A 1 214  ? 123.268 149.606 162.576 1.00 36.67  ? 214  ASN   B CB  1 
ATOM   1282  C  CG  . ASN   A 1 214  ? 122.325 150.473 163.369 1.00 43.59  ? 214  ASN   B CG  1 
ATOM   1283  O  OD1 . ASN   A 1 214  ? 122.714 151.077 164.366 1.00 53.83  ? 214  ASN   B OD1 1 
ATOM   1284  N  ND2 . ASN   A 1 214  ? 121.073 150.536 162.938 1.00 47.12  ? 214  ASN   B ND2 1 
ATOM   1285  N  N   . SER   A 1 215  ? 123.185 146.564 163.749 1.00 38.87  ? 215  SER   B N   1 
ATOM   1286  C  CA  . SER   A 1 215  ? 122.316 145.558 164.353 1.00 35.34  ? 215  SER   B CA  1 
ATOM   1287  C  C   . SER   A 1 215  ? 123.099 144.543 165.170 1.00 40.63  ? 215  SER   B C   1 
ATOM   1288  O  O   . SER   A 1 215  ? 122.741 143.365 165.216 1.00 45.47  ? 215  SER   B O   1 
ATOM   1289  C  CB  . SER   A 1 215  ? 121.501 144.857 163.273 1.00 37.85  ? 215  SER   B CB  1 
ATOM   1290  O  OG  . SER   A 1 215  ? 122.345 144.164 162.372 1.00 43.15  ? 215  SER   B OG  1 
ATOM   1291  N  N   . LEU   A 1 216  ? 124.172 144.979 165.823 1.00 43.80  ? 216  LEU   B N   1 
ATOM   1292  C  CA  . LEU   A 1 216  ? 125.000 144.069 166.601 1.00 44.17  ? 216  LEU   B CA  1 
ATOM   1293  C  C   . LEU   A 1 216  ? 124.196 143.455 167.740 1.00 49.36  ? 216  LEU   B C   1 
ATOM   1294  O  O   . LEU   A 1 216  ? 123.477 144.154 168.460 1.00 46.56  ? 216  LEU   B O   1 
ATOM   1295  C  CB  . LEU   A 1 216  ? 126.219 144.809 167.148 1.00 44.44  ? 216  LEU   B CB  1 
ATOM   1296  C  CG  . LEU   A 1 216  ? 127.259 143.990 167.909 1.00 40.52  ? 216  LEU   B CG  1 
ATOM   1297  C  CD1 . LEU   A 1 216  ? 127.844 142.920 167.014 1.00 45.31  ? 216  LEU   B CD1 1 
ATOM   1298  C  CD2 . LEU   A 1 216  ? 128.351 144.890 168.448 1.00 44.82  ? 216  LEU   B CD2 1 
ATOM   1299  N  N   . PHE   A 1 217  ? 124.325 142.142 167.899 1.00 46.12  ? 217  PHE   B N   1 
ATOM   1300  C  CA  . PHE   A 1 217  ? 123.599 141.391 168.921 1.00 36.54  ? 217  PHE   B CA  1 
ATOM   1301  C  C   . PHE   A 1 217  ? 124.202 141.711 170.281 1.00 39.09  ? 217  PHE   B C   1 
ATOM   1302  O  O   . PHE   A 1 217  ? 125.289 141.239 170.618 1.00 52.63  ? 217  PHE   B O   1 
ATOM   1303  C  CB  . PHE   A 1 217  ? 123.672 139.902 168.610 1.00 41.75  ? 217  PHE   B CB  1 
ATOM   1304  C  CG  . PHE   A 1 217  ? 122.777 139.052 169.460 1.00 43.53  ? 217  PHE   B CG  1 
ATOM   1305  C  CD1 . PHE   A 1 217  ? 121.418 139.005 169.220 1.00 46.68  ? 217  PHE   B CD1 1 
ATOM   1306  C  CD2 . PHE   A 1 217  ? 123.298 138.275 170.477 1.00 41.91  ? 217  PHE   B CD2 1 
ATOM   1307  C  CE1 . PHE   A 1 217  ? 120.593 138.217 169.991 1.00 45.86  ? 217  PHE   B CE1 1 
ATOM   1308  C  CE2 . PHE   A 1 217  ? 122.479 137.480 171.247 1.00 42.05  ? 217  PHE   B CE2 1 
ATOM   1309  C  CZ  . PHE   A 1 217  ? 121.124 137.452 171.005 1.00 44.62  ? 217  PHE   B CZ  1 
ATOM   1310  N  N   . ASN   A 1 218  ? 123.499 142.517 171.073 1.00 34.62  ? 218  ASN   B N   1 
ATOM   1311  C  CA  . ASN   A 1 218  ? 124.004 143.007 172.352 1.00 40.16  ? 218  ASN   B CA  1 
ATOM   1312  C  C   . ASN   A 1 218  ? 123.384 142.271 173.535 1.00 48.98  ? 218  ASN   B C   1 
ATOM   1313  O  O   . ASN   A 1 218  ? 123.155 142.852 174.597 1.00 52.74  ? 218  ASN   B O   1 
ATOM   1314  C  CB  . ASN   A 1 218  ? 123.780 144.510 172.486 1.00 40.96  ? 218  ASN   B CB  1 
ATOM   1315  C  CG  . ASN   A 1 218  ? 122.349 144.916 172.222 1.00 46.67  ? 218  ASN   B CG  1 
ATOM   1316  O  OD1 . ASN   A 1 218  ? 121.472 144.074 172.032 1.00 53.54  ? 218  ASN   B OD1 1 
ATOM   1317  N  ND2 . ASN   A 1 218  ? 122.104 146.217 172.211 1.00 44.04  ? 218  ASN   B ND2 1 
ATOM   1318  N  N   . ASP   A 1 219  ? 123.109 140.984 173.362 1.00 53.08  ? 219  ASP   B N   1 
ATOM   1319  C  CA  . ASP   A 1 219  ? 122.615 140.125 174.428 1.00 44.50  ? 219  ASP   B CA  1 
ATOM   1320  C  C   . ASP   A 1 219  ? 123.751 139.220 174.882 1.00 49.32  ? 219  ASP   B C   1 
ATOM   1321  O  O   . ASP   A 1 219  ? 124.347 138.511 174.065 1.00 54.80  ? 219  ASP   B O   1 
ATOM   1322  C  CB  . ASP   A 1 219  ? 121.417 139.305 173.945 1.00 45.73  ? 219  ASP   B CB  1 
ATOM   1323  C  CG  . ASP   A 1 219  ? 120.623 138.697 175.077 1.00 49.02  ? 219  ASP   B CG  1 
ATOM   1324  O  OD1 . ASP   A 1 219  ? 121.231 138.179 176.037 1.00 51.96  ? 219  ASP   B OD1 1 
ATOM   1325  O  OD2 . ASP   A 1 219  ? 119.378 138.737 175.006 1.00 55.11  ? 219  ASP   B OD2 1 
ATOM   1326  N  N   . THR   A 1 220  ? 124.054 139.250 176.176 1.00 42.25  ? 220  THR   B N   1 
ATOM   1327  C  CA  . THR   A 1 220  ? 125.192 138.537 176.734 1.00 39.86  ? 220  THR   B CA  1 
ATOM   1328  C  C   . THR   A 1 220  ? 124.735 137.429 177.674 1.00 54.52  ? 220  THR   B C   1 
ATOM   1329  O  O   . THR   A 1 220  ? 123.645 137.476 178.249 1.00 63.43  ? 220  THR   B O   1 
ATOM   1330  C  CB  . THR   A 1 220  ? 126.128 139.493 177.483 1.00 43.47  ? 220  THR   B CB  1 
ATOM   1331  O  OG1 . THR   A 1 220  ? 125.422 140.108 178.567 1.00 53.92  ? 220  THR   B OG1 1 
ATOM   1332  C  CG2 . THR   A 1 220  ? 126.648 140.570 176.549 1.00 49.04  ? 220  THR   B CG2 1 
ATOM   1333  N  N   . PHE   A 1 221  ? 125.597 136.427 177.826 1.00 48.89  ? 221  PHE   B N   1 
ATOM   1334  C  CA  . PHE   A 1 221  ? 125.369 135.297 178.726 1.00 34.76  ? 221  PHE   B CA  1 
ATOM   1335  C  C   . PHE   A 1 221  ? 126.580 135.181 179.642 1.00 42.31  ? 221  PHE   B C   1 
ATOM   1336  O  O   . PHE   A 1 221  ? 127.419 134.287 179.482 1.00 49.09  ? 221  PHE   B O   1 
ATOM   1337  C  CB  . PHE   A 1 221  ? 125.138 134.004 177.945 1.00 35.72  ? 221  PHE   B CB  1 
ATOM   1338  C  CG  . PHE   A 1 221  ? 124.243 134.167 176.754 1.00 37.12  ? 221  PHE   B CG  1 
ATOM   1339  C  CD1 . PHE   A 1 221  ? 122.871 134.160 176.894 1.00 40.62  ? 221  PHE   B CD1 1 
ATOM   1340  C  CD2 . PHE   A 1 221  ? 124.777 134.324 175.491 1.00 39.65  ? 221  PHE   B CD2 1 
ATOM   1341  C  CE1 . PHE   A 1 221  ? 122.050 134.312 175.800 1.00 45.81  ? 221  PHE   B CE1 1 
ATOM   1342  C  CE2 . PHE   A 1 221  ? 123.960 134.475 174.393 1.00 43.47  ? 221  PHE   B CE2 1 
ATOM   1343  C  CZ  . PHE   A 1 221  ? 122.596 134.468 174.547 1.00 45.19  ? 221  PHE   B CZ  1 
ATOM   1344  N  N   . PRO   A 1 222  ? 126.702 136.086 180.616 1.00 41.02  ? 222  PRO   B N   1 
ATOM   1345  C  CA  . PRO   A 1 222  ? 127.966 136.195 181.364 1.00 45.35  ? 222  PRO   B CA  1 
ATOM   1346  C  C   . PRO   A 1 222  ? 128.356 134.954 182.150 1.00 51.42  ? 222  PRO   B C   1 
ATOM   1347  O  O   . PRO   A 1 222  ? 129.552 134.653 182.248 1.00 56.76  ? 222  PRO   B O   1 
ATOM   1348  C  CB  . PRO   A 1 222  ? 127.713 137.392 182.289 1.00 48.41  ? 222  PRO   B CB  1 
ATOM   1349  C  CG  . PRO   A 1 222  ? 126.237 137.451 182.432 1.00 48.67  ? 222  PRO   B CG  1 
ATOM   1350  C  CD  . PRO   A 1 222  ? 125.685 137.028 181.109 1.00 46.84  ? 222  PRO   B CD  1 
ATOM   1351  N  N   . SER   A 1 223  ? 127.400 134.222 182.718 1.00 46.00  ? 223  SER   B N   1 
ATOM   1352  C  CA  . SER   A 1 223  ? 127.740 133.160 183.656 1.00 43.00  ? 223  SER   B CA  1 
ATOM   1353  C  C   . SER   A 1 223  ? 126.924 131.907 183.389 1.00 51.69  ? 223  SER   B C   1 
ATOM   1354  O  O   . SER   A 1 223  ? 125.719 131.985 183.136 1.00 54.59  ? 223  SER   B O   1 
ATOM   1355  C  CB  . SER   A 1 223  ? 127.519 133.617 185.100 1.00 41.23  ? 223  SER   B CB  1 
ATOM   1356  O  OG  . SER   A 1 223  ? 126.147 133.856 185.351 1.00 54.23  ? 223  SER   B OG  1 
ATOM   1357  N  N   . VAL   A 1 224  ? 127.593 130.757 183.449 1.00 49.70  ? 224  VAL   B N   1 
ATOM   1358  C  CA  . VAL   A 1 224  ? 126.957 129.446 183.498 1.00 39.72  ? 224  VAL   B CA  1 
ATOM   1359  C  C   . VAL   A 1 224  ? 127.545 128.737 184.709 1.00 45.26  ? 224  VAL   B C   1 
ATOM   1360  O  O   . VAL   A 1 224  ? 128.746 128.441 184.739 1.00 57.37  ? 224  VAL   B O   1 
ATOM   1361  C  CB  . VAL   A 1 224  ? 127.186 128.637 182.215 1.00 40.95  ? 224  VAL   B CB  1 
ATOM   1362  C  CG1 . VAL   A 1 224  ? 126.500 127.289 182.312 1.00 50.18  ? 224  VAL   B CG1 1 
ATOM   1363  C  CG2 . VAL   A 1 224  ? 126.683 129.404 181.008 1.00 45.13  ? 224  VAL   B CG2 1 
ATOM   1364  N  N   . VAL   A 1 225  ? 126.710 128.464 185.707 1.00 39.52  ? 225  VAL   B N   1 
ATOM   1365  C  CA  . VAL   A 1 225  ? 127.167 128.003 187.012 1.00 38.43  ? 225  VAL   B CA  1 
ATOM   1366  C  C   . VAL   A 1 225  ? 126.472 126.693 187.347 1.00 51.40  ? 225  VAL   B C   1 
ATOM   1367  O  O   . VAL   A 1 225  ? 125.249 126.580 187.207 1.00 62.76  ? 225  VAL   B O   1 
ATOM   1368  C  CB  . VAL   A 1 225  ? 126.898 129.053 188.105 1.00 48.48  ? 225  VAL   B CB  1 
ATOM   1369  C  CG1 . VAL   A 1 225  ? 127.405 128.563 189.446 1.00 53.69  ? 225  VAL   B CG1 1 
ATOM   1370  C  CG2 . VAL   A 1 225  ? 127.548 130.375 187.741 1.00 54.48  ? 225  VAL   B CG2 1 
ATOM   1371  N  N   . LEU   A 1 226  ? 127.249 125.709 187.791 1.00 51.66  ? 226  LEU   B N   1 
ATOM   1372  C  CA  . LEU   A 1 226  ? 126.689 124.460 188.288 1.00 46.67  ? 226  LEU   B CA  1 
ATOM   1373  C  C   . LEU   A 1 226  ? 126.146 124.655 189.697 1.00 52.02  ? 226  LEU   B C   1 
ATOM   1374  O  O   . LEU   A 1 226  ? 126.802 125.252 190.554 1.00 56.99  ? 226  LEU   B O   1 
ATOM   1375  C  CB  . LEU   A 1 226  ? 127.749 123.359 188.279 1.00 50.92  ? 226  LEU   B CB  1 
ATOM   1376  C  CG  . LEU   A 1 226  ? 127.324 121.986 188.797 1.00 56.07  ? 226  LEU   B CG  1 
ATOM   1377  C  CD1 . LEU   A 1 226  ? 126.120 121.478 188.031 1.00 52.57  ? 226  LEU   B CD1 1 
ATOM   1378  C  CD2 . LEU   A 1 226  ? 128.472 121.003 188.698 1.00 58.89  ? 226  LEU   B CD2 1 
ATOM   1379  N  N   . LEU   A 1 227  ? 124.938 124.144 189.934 1.00 58.76  ? 227  LEU   B N   1 
ATOM   1380  C  CA  . LEU   A 1 227  ? 124.250 124.369 191.198 1.00 54.22  ? 227  LEU   B CA  1 
ATOM   1381  C  C   . LEU   A 1 227  ? 124.471 123.263 192.219 1.00 60.86  ? 227  LEU   B C   1 
ATOM   1382  O  O   . LEU   A 1 227  ? 124.363 123.524 193.422 1.00 63.35  ? 227  LEU   B O   1 
ATOM   1383  C  CB  . LEU   A 1 227  ? 122.748 124.534 190.959 1.00 55.02  ? 227  LEU   B CB  1 
ATOM   1384  C  CG  . LEU   A 1 227  ? 122.323 125.773 190.175 1.00 56.13  ? 227  LEU   B CG  1 
ATOM   1385  C  CD1 . LEU   A 1 227  ? 120.813 125.805 190.008 1.00 59.32  ? 227  LEU   B CD1 1 
ATOM   1386  C  CD2 . LEU   A 1 227  ? 122.813 127.028 190.866 1.00 59.04  ? 227  LEU   B CD2 1 
ATOM   1387  N  N   . ASN   A 1 228  ? 124.770 122.042 191.781 1.00 70.31  ? 228  ASN   B N   1 
ATOM   1388  C  CA  . ASN   A 1 228  ? 124.988 120.907 192.677 1.00 66.02  ? 228  ASN   B CA  1 
ATOM   1389  C  C   . ASN   A 1 228  ? 126.316 120.248 192.332 1.00 70.54  ? 228  ASN   B C   1 
ATOM   1390  O  O   . ASN   A 1 228  ? 126.351 119.145 191.771 1.00 75.76  ? 228  ASN   B O   1 
ATOM   1391  C  CB  . ASN   A 1 228  ? 123.834 119.906 192.591 1.00 67.45  ? 228  ASN   B CB  1 
ATOM   1392  C  CG  . ASN   A 1 228  ? 123.449 119.581 191.161 1.00 71.21  ? 228  ASN   B CG  1 
ATOM   1393  O  OD1 . ASN   A 1 228  ? 124.135 119.968 190.218 1.00 73.25  ? 228  ASN   B OD1 1 
ATOM   1394  N  ND2 . ASN   A 1 228  ? 122.345 118.863 190.994 1.00 70.28  ? 228  ASN   B ND2 1 
ATOM   1395  N  N   . PRO   A 1 229  ? 127.435 120.894 192.661 1.00 72.55  ? 229  PRO   B N   1 
ATOM   1396  C  CA  . PRO   A 1 229  ? 128.741 120.299 192.351 1.00 74.02  ? 229  PRO   B CA  1 
ATOM   1397  C  C   . PRO   A 1 229  ? 129.029 119.116 193.262 1.00 79.46  ? 229  PRO   B C   1 
ATOM   1398  O  O   . PRO   A 1 229  ? 128.807 119.176 194.473 1.00 78.74  ? 229  PRO   B O   1 
ATOM   1399  C  CB  . PRO   A 1 229  ? 129.720 121.452 192.591 1.00 72.39  ? 229  PRO   B CB  1 
ATOM   1400  C  CG  . PRO   A 1 229  ? 129.046 122.291 193.614 1.00 73.59  ? 229  PRO   B CG  1 
ATOM   1401  C  CD  . PRO   A 1 229  ? 127.569 122.191 193.345 1.00 74.22  ? 229  PRO   B CD  1 
ATOM   1402  N  N   . THR   A 1 230  ? 129.523 118.031 192.665 1.00 89.38  ? 230  THR   B N   1 
ATOM   1403  C  CA  . THR   A 1 230  ? 129.875 116.850 193.442 1.00 87.19  ? 230  THR   B CA  1 
ATOM   1404  C  C   . THR   A 1 230  ? 131.182 117.034 194.202 1.00 88.39  ? 230  THR   B C   1 
ATOM   1405  O  O   . THR   A 1 230  ? 131.377 116.408 195.250 1.00 88.79  ? 230  THR   B O   1 
ATOM   1406  C  CB  . THR   A 1 230  ? 129.972 115.626 192.530 1.00 90.99  ? 230  THR   B CB  1 
ATOM   1407  O  OG1 . THR   A 1 230  ? 130.974 115.850 191.530 1.00 90.05  ? 230  THR   B OG1 1 
ATOM   1408  C  CG2 . THR   A 1 230  ? 128.636 115.365 191.851 1.00 90.42  ? 230  THR   B CG2 1 
ATOM   1409  N  N   . ASN   A 1 231  ? 132.080 117.880 193.700 1.00 92.40  ? 231  ASN   B N   1 
ATOM   1410  C  CA  . ASN   A 1 231  ? 133.381 118.075 194.325 1.00 90.62  ? 231  ASN   B CA  1 
ATOM   1411  C  C   . ASN   A 1 231  ? 133.340 119.185 195.368 1.00 89.91  ? 231  ASN   B C   1 
ATOM   1412  O  O   . ASN   A 1 231  ? 134.156 120.111 195.330 1.00 91.39  ? 231  ASN   B O   1 
ATOM   1413  C  CB  . ASN   A 1 231  ? 134.438 118.385 193.263 1.00 92.35  ? 231  ASN   B CB  1 
ATOM   1414  C  CG  . ASN   A 1 231  ? 134.047 119.548 192.374 1.00 94.19  ? 231  ASN   B CG  1 
ATOM   1415  O  OD1 . ASN   A 1 231  ? 133.455 119.361 191.311 1.00 94.46  ? 231  ASN   B OD1 1 
ATOM   1416  N  ND2 . ASN   A 1 231  ? 134.377 120.760 192.806 1.00 90.95  ? 231  ASN   B ND2 1 
ATOM   1417  N  N   . GLY   A 1 232  ? 132.401 119.100 196.303 1.00 87.65  ? 232  GLY   B N   1 
ATOM   1418  C  CA  . GLY   A 1 232  ? 132.310 120.094 197.349 1.00 86.20  ? 232  GLY   B CA  1 
ATOM   1419  C  C   . GLY   A 1 232  ? 131.830 121.439 196.828 1.00 89.47  ? 232  GLY   B C   1 
ATOM   1420  O  O   . GLY   A 1 232  ? 131.365 121.582 195.696 1.00 92.24  ? 232  GLY   B O   1 
ATOM   1421  N  N   . ALA   A 1 233  ? 131.952 122.440 197.704 1.00 86.27  ? 233  ALA   B N   1 
ATOM   1422  C  CA  . ALA   A 1 233  ? 131.590 123.828 197.425 1.00 86.16  ? 233  ALA   B CA  1 
ATOM   1423  C  C   . ALA   A 1 233  ? 130.097 124.001 197.168 1.00 85.66  ? 233  ALA   B C   1 
ATOM   1424  O  O   . ALA   A 1 233  ? 129.392 123.039 196.849 1.00 86.88  ? 233  ALA   B O   1 
ATOM   1425  C  CB  . ALA   A 1 233  ? 132.395 124.370 196.239 1.00 83.92  ? 233  ALA   B CB  1 
ATOM   1426  N  N   . GLN   A 1 234  ? 129.603 125.231 197.319 1.00 84.66  ? 234  GLN   B N   1 
ATOM   1427  C  CA  . GLN   A 1 234  ? 128.192 125.496 197.071 1.00 84.16  ? 234  GLN   B CA  1 
ATOM   1428  C  C   . GLN   A 1 234  ? 127.868 125.506 195.584 1.00 87.06  ? 234  GLN   B C   1 
ATOM   1429  O  O   . GLN   A 1 234  ? 126.796 125.041 195.185 1.00 87.82  ? 234  GLN   B O   1 
ATOM   1430  C  CB  . GLN   A 1 234  ? 127.780 126.827 197.702 1.00 85.73  ? 234  GLN   B CB  1 
ATOM   1431  C  CG  . GLN   A 1 234  ? 127.817 126.849 199.224 1.00 87.59  ? 234  GLN   B CG  1 
ATOM   1432  C  CD  . GLN   A 1 234  ? 129.219 127.014 199.779 1.00 88.99  ? 234  GLN   B CD  1 
ATOM   1433  O  OE1 . GLN   A 1 234  ? 130.172 127.245 199.034 1.00 86.58  ? 234  GLN   B OE1 1 
ATOM   1434  N  NE2 . GLN   A 1 234  ? 129.352 126.897 201.095 1.00 90.03  ? 234  GLN   B NE2 1 
ATOM   1435  N  N   . ASN   A 1 235  ? 128.771 126.027 194.759 1.00 81.20  ? 235  ASN   B N   1 
ATOM   1436  C  CA  . ASN   A 1 235  ? 128.550 126.076 193.322 1.00 75.70  ? 235  ASN   B CA  1 
ATOM   1437  C  C   . ASN   A 1 235  ? 129.896 126.108 192.617 1.00 74.27  ? 235  ASN   B C   1 
ATOM   1438  O  O   . ASN   A 1 235  ? 130.922 126.450 193.210 1.00 80.36  ? 235  ASN   B O   1 
ATOM   1439  C  CB  . ASN   A 1 235  ? 127.701 127.288 192.926 1.00 76.21  ? 235  ASN   B CB  1 
ATOM   1440  C  CG  . ASN   A 1 235  ? 128.216 128.584 193.521 1.00 81.12  ? 235  ASN   B CG  1 
ATOM   1441  O  OD1 . ASN   A 1 235  ? 129.352 128.661 193.987 1.00 79.24  ? 235  ASN   B OD1 1 
ATOM   1442  N  ND2 . ASN   A 1 235  ? 127.379 129.613 193.506 1.00 84.77  ? 235  ASN   B ND2 1 
ATOM   1443  N  N   . GLN   A 1 236  ? 129.877 125.740 191.340 1.00 56.36  ? 236  GLN   B N   1 
ATOM   1444  C  CA  . GLN   A 1 236  ? 131.061 125.771 190.496 1.00 52.48  ? 236  GLN   B CA  1 
ATOM   1445  C  C   . GLN   A 1 236  ? 130.707 126.465 189.192 1.00 55.99  ? 236  GLN   B C   1 
ATOM   1446  O  O   . GLN   A 1 236  ? 129.710 126.117 188.552 1.00 62.20  ? 236  GLN   B O   1 
ATOM   1447  C  CB  . GLN   A 1 236  ? 131.587 124.361 190.223 1.00 57.52  ? 236  GLN   B CB  1 
ATOM   1448  C  CG  . GLN   A 1 236  ? 132.916 124.327 189.494 1.00 55.61  ? 236  GLN   B CG  1 
ATOM   1449  C  CD  . GLN   A 1 236  ? 133.294 122.934 189.043 1.00 59.18  ? 236  GLN   B CD  1 
ATOM   1450  O  OE1 . GLN   A 1 236  ? 132.449 122.045 188.964 1.00 58.54  ? 236  GLN   B OE1 1 
ATOM   1451  N  NE2 . GLN   A 1 236  ? 134.571 122.735 188.744 1.00 62.66  ? 236  GLN   B NE2 1 
ATOM   1452  N  N   . THR   A 1 237  ? 131.518 127.442 188.803 1.00 53.94  ? 237  THR   B N   1 
ATOM   1453  C  CA  . THR   A 1 237  ? 131.275 128.209 187.591 1.00 50.14  ? 237  THR   B CA  1 
ATOM   1454  C  C   . THR   A 1 237  ? 131.942 127.522 186.409 1.00 48.73  ? 237  THR   B C   1 
ATOM   1455  O  O   . THR   A 1 237  ? 133.145 127.251 186.442 1.00 57.27  ? 237  THR   B O   1 
ATOM   1456  C  CB  . THR   A 1 237  ? 131.808 129.634 187.739 1.00 49.55  ? 237  THR   B CB  1 
ATOM   1457  O  OG1 . THR   A 1 237  ? 131.206 130.256 188.881 1.00 52.39  ? 237  THR   B OG1 1 
ATOM   1458  C  CG2 . THR   A 1 237  ? 131.490 130.451 186.501 1.00 51.69  ? 237  THR   B CG2 1 
ATOM   1459  N  N   . TYR   A 1 238  ? 131.163 127.236 185.370 1.00 45.69  ? 238  TYR   B N   1 
ATOM   1460  C  CA  . TYR   A 1 238  ? 131.723 126.660 184.156 1.00 49.98  ? 238  TYR   B CA  1 
ATOM   1461  C  C   . TYR   A 1 238  ? 132.341 127.777 183.327 1.00 53.84  ? 238  TYR   B C   1 
ATOM   1462  O  O   . TYR   A 1 238  ? 131.655 128.733 182.949 1.00 57.57  ? 238  TYR   B O   1 
ATOM   1463  C  CB  . TYR   A 1 238  ? 130.658 125.912 183.361 1.00 50.27  ? 238  TYR   B CB  1 
ATOM   1464  C  CG  . TYR   A 1 238  ? 131.233 125.108 182.222 1.00 48.95  ? 238  TYR   B CG  1 
ATOM   1465  C  CD1 . TYR   A 1 238  ? 131.950 123.948 182.461 1.00 50.79  ? 238  TYR   B CD1 1 
ATOM   1466  C  CD2 . TYR   A 1 238  ? 131.067 125.514 180.909 1.00 51.71  ? 238  TYR   B CD2 1 
ATOM   1467  C  CE1 . TYR   A 1 238  ? 132.481 123.214 181.427 1.00 49.57  ? 238  TYR   B CE1 1 
ATOM   1468  C  CE2 . TYR   A 1 238  ? 131.596 124.786 179.866 1.00 52.60  ? 238  TYR   B CE2 1 
ATOM   1469  C  CZ  . TYR   A 1 238  ? 132.301 123.636 180.131 1.00 49.78  ? 238  TYR   B CZ  1 
ATOM   1470  O  OH  . TYR   A 1 238  ? 132.831 122.909 179.091 1.00 60.13  ? 238  TYR   B OH  1 
ATOM   1471  N  N   . ASN   A 1 239  ? 133.636 127.655 183.043 1.00 52.05  ? 239  ASN   B N   1 
ATOM   1472  C  CA  . ASN   A 1 239  ? 134.424 128.764 182.511 1.00 48.06  ? 239  ASN   B CA  1 
ATOM   1473  C  C   . ASN   A 1 239  ? 134.331 128.788 180.989 1.00 55.59  ? 239  ASN   B C   1 
ATOM   1474  O  O   . ASN   A 1 239  ? 135.205 128.308 180.264 1.00 63.74  ? 239  ASN   B O   1 
ATOM   1475  C  CB  . ASN   A 1 239  ? 135.865 128.662 182.990 1.00 53.72  ? 239  ASN   B CB  1 
ATOM   1476  C  CG  . ASN   A 1 239  ? 135.971 128.683 184.499 1.00 56.07  ? 239  ASN   B CG  1 
ATOM   1477  O  OD1 . ASN   A 1 239  ? 135.850 129.735 185.122 1.00 61.33  ? 239  ASN   B OD1 1 
ATOM   1478  N  ND2 . ASN   A 1 239  ? 136.196 127.521 185.096 1.00 50.70  ? 239  ASN   B ND2 1 
ATOM   1479  N  N   . PHE   A 1 240  ? 133.237 129.364 180.500 1.00 47.70  ? 240  PHE   B N   1 
ATOM   1480  C  CA  . PHE   A 1 240  ? 133.149 129.716 179.092 1.00 44.84  ? 240  PHE   B CA  1 
ATOM   1481  C  C   . PHE   A 1 240  ? 134.036 130.920 178.806 1.00 49.96  ? 240  PHE   B C   1 
ATOM   1482  O  O   . PHE   A 1 240  ? 134.004 131.921 179.527 1.00 54.58  ? 240  PHE   B O   1 
ATOM   1483  C  CB  . PHE   A 1 240  ? 131.707 130.032 178.703 1.00 37.96  ? 240  PHE   B CB  1 
ATOM   1484  C  CG  . PHE   A 1 240  ? 130.872 128.822 178.403 1.00 34.71  ? 240  PHE   B CG  1 
ATOM   1485  C  CD1 . PHE   A 1 240  ? 131.113 128.058 177.279 1.00 49.81  ? 240  PHE   B CD1 1 
ATOM   1486  C  CD2 . PHE   A 1 240  ? 129.822 128.471 179.228 1.00 41.20  ? 240  PHE   B CD2 1 
ATOM   1487  C  CE1 . PHE   A 1 240  ? 130.336 126.955 176.997 1.00 54.06  ? 240  PHE   B CE1 1 
ATOM   1488  C  CE2 . PHE   A 1 240  ? 129.042 127.371 178.946 1.00 38.42  ? 240  PHE   B CE2 1 
ATOM   1489  C  CZ  . PHE   A 1 240  ? 129.300 126.613 177.831 1.00 45.39  ? 240  PHE   B CZ  1 
ATOM   1490  N  N   . SER   A 1 241  ? 134.831 130.823 177.746 1.00 43.26  ? 241  SER   B N   1 
ATOM   1491  C  CA  . SER   A 1 241  ? 135.753 131.880 177.356 1.00 34.36  ? 241  SER   B CA  1 
ATOM   1492  C  C   . SER   A 1 241  ? 135.279 132.503 176.055 1.00 37.17  ? 241  SER   B C   1 
ATOM   1493  O  O   . SER   A 1 241  ? 135.023 131.791 175.079 1.00 41.12  ? 241  SER   B O   1 
ATOM   1494  C  CB  . SER   A 1 241  ? 137.175 131.342 177.198 1.00 37.24  ? 241  SER   B CB  1 
ATOM   1495  O  OG  . SER   A 1 241  ? 138.071 132.372 176.821 1.00 43.70  ? 241  SER   B OG  1 
ATOM   1496  N  N   . GLU   A 1 242  ? 135.177 133.830 176.039 1.00 40.29  ? 242  GLU   B N   1 
ATOM   1497  C  CA  . GLU   A 1 242  ? 134.752 134.554 174.849 1.00 43.60  ? 242  GLU   B CA  1 
ATOM   1498  C  C   . GLU   A 1 242  ? 135.885 134.775 173.858 1.00 48.64  ? 242  GLU   B C   1 
ATOM   1499  O  O   . GLU   A 1 242  ? 135.650 135.355 172.794 1.00 50.87  ? 242  GLU   B O   1 
ATOM   1500  C  CB  . GLU   A 1 242  ? 134.142 135.899 175.243 1.00 43.88  ? 242  GLU   B CB  1 
ATOM   1501  C  CG  . GLU   A 1 242  ? 133.013 135.792 176.247 1.00 45.25  ? 242  GLU   B CG  1 
ATOM   1502  C  CD  . GLU   A 1 242  ? 132.460 137.143 176.642 1.00 53.79  ? 242  GLU   B CD  1 
ATOM   1503  O  OE1 . GLU   A 1 242  ? 132.710 138.126 175.914 1.00 52.52  ? 242  GLU   B OE1 1 
ATOM   1504  O  OE2 . GLU   A 1 242  ? 131.778 137.227 177.683 1.00 58.71  ? 242  GLU   B OE2 1 
ATOM   1505  N  N   . SER   A 1 243  ? 137.096 134.337 174.180 1.00 51.39  ? 243  SER   B N   1 
ATOM   1506  C  CA  . SER   A 1 243  ? 138.227 134.442 173.274 1.00 40.14  ? 243  SER   B CA  1 
ATOM   1507  C  C   . SER   A 1 243  ? 138.292 133.220 172.369 1.00 46.25  ? 243  SER   B C   1 
ATOM   1508  O  O   . SER   A 1 243  ? 138.027 132.092 172.793 1.00 52.03  ? 243  SER   B O   1 
ATOM   1509  C  CB  . SER   A 1 243  ? 139.534 134.581 174.055 1.00 41.94  ? 243  SER   B CB  1 
ATOM   1510  O  OG  . SER   A 1 243  ? 139.497 135.710 174.909 1.00 51.84  ? 243  SER   B OG  1 
ATOM   1511  N  N   . GLY   A 1 244  ? 138.651 133.456 171.111 1.00 43.55  ? 244  GLY   B N   1 
ATOM   1512  C  CA  . GLY   A 1 244  ? 138.755 132.381 170.149 1.00 41.81  ? 244  GLY   B CA  1 
ATOM   1513  C  C   . GLY   A 1 244  ? 137.457 131.972 169.498 1.00 42.17  ? 244  GLY   B C   1 
ATOM   1514  O  O   . GLY   A 1 244  ? 137.448 131.002 168.733 1.00 52.87  ? 244  GLY   B O   1 
ATOM   1515  N  N   . ILE   A 1 245  ? 136.357 132.677 169.771 1.00 33.29  ? 245  ILE   B N   1 
ATOM   1516  C  CA  . ILE   A 1 245  ? 135.075 132.340 169.158 1.00 35.15  ? 245  ILE   B CA  1 
ATOM   1517  C  C   . ILE   A 1 245  ? 135.018 132.696 167.683 1.00 44.83  ? 245  ILE   B C   1 
ATOM   1518  O  O   . ILE   A 1 245  ? 134.067 132.302 166.997 1.00 48.99  ? 245  ILE   B O   1 
ATOM   1519  C  CB  . ILE   A 1 245  ? 133.918 133.028 169.903 1.00 41.19  ? 245  ILE   B CB  1 
ATOM   1520  C  CG1 . ILE   A 1 245  ? 134.015 134.545 169.760 1.00 43.81  ? 245  ILE   B CG1 1 
ATOM   1521  C  CG2 . ILE   A 1 245  ? 133.934 132.637 171.364 1.00 41.05  ? 245  ILE   B CG2 1 
ATOM   1522  C  CD1 . ILE   A 1 245  ? 132.942 135.295 170.506 1.00 40.93  ? 245  ILE   B CD1 1 
ATOM   1523  N  N   . ALA   A 1 246  ? 136.004 133.430 167.179 1.00 49.64  ? 246  ALA   B N   1 
ATOM   1524  C  CA  . ALA   A 1 246  ? 136.120 133.744 165.764 1.00 46.31  ? 246  ALA   B CA  1 
ATOM   1525  C  C   . ALA   A 1 246  ? 137.489 133.307 165.265 1.00 45.38  ? 246  ALA   B C   1 
ATOM   1526  O  O   . ALA   A 1 246  ? 138.461 133.274 166.025 1.00 51.83  ? 246  ALA   B O   1 
ATOM   1527  C  CB  . ALA   A 1 246  ? 135.921 135.237 165.503 1.00 43.37  ? 246  ALA   B CB  1 
ATOM   1528  N  N   . TRP   A 1 247  ? 137.556 132.955 163.983 1.00 37.04  ? 247  TRP   B N   1 
ATOM   1529  C  CA  . TRP   A 1 247  ? 138.819 132.525 163.401 1.00 35.43  ? 247  TRP   B CA  1 
ATOM   1530  C  C   . TRP   A 1 247  ? 139.831 133.662 163.449 1.00 42.50  ? 247  TRP   B C   1 
ATOM   1531  O  O   . TRP   A 1 247  ? 139.476 134.838 163.330 1.00 53.06  ? 247  TRP   B O   1 
ATOM   1532  C  CB  . TRP   A 1 247  ? 138.610 132.051 161.962 1.00 44.02  ? 247  TRP   B CB  1 
ATOM   1533  C  CG  . TRP   A 1 247  ? 139.823 131.415 161.357 1.00 40.27  ? 247  TRP   B CG  1 
ATOM   1534  C  CD1 . TRP   A 1 247  ? 140.465 130.299 161.798 1.00 43.03  ? 247  TRP   B CD1 1 
ATOM   1535  C  CD2 . TRP   A 1 247  ? 140.532 131.852 160.193 1.00 40.46  ? 247  TRP   B CD2 1 
ATOM   1536  N  NE1 . TRP   A 1 247  ? 141.535 130.018 160.987 1.00 46.03  ? 247  TRP   B NE1 1 
ATOM   1537  C  CE2 . TRP   A 1 247  ? 141.597 130.957 159.993 1.00 41.57  ? 247  TRP   B CE2 1 
ATOM   1538  C  CE3 . TRP   A 1 247  ? 140.370 132.916 159.302 1.00 43.96  ? 247  TRP   B CE3 1 
ATOM   1539  C  CZ2 . TRP   A 1 247  ? 142.497 131.092 158.942 1.00 44.33  ? 247  TRP   B CZ2 1 
ATOM   1540  C  CZ3 . TRP   A 1 247  ? 141.264 133.048 158.260 1.00 46.17  ? 247  TRP   B CZ3 1 
ATOM   1541  C  CH2 . TRP   A 1 247  ? 142.313 132.143 158.089 1.00 45.58  ? 247  TRP   B CH2 1 
ATOM   1542  N  N   . GLY   A 1 248  ? 141.103 133.305 163.630 1.00 41.21  ? 248  GLY   B N   1 
ATOM   1543  C  CA  . GLY   A 1 248  ? 142.138 134.298 163.861 1.00 41.56  ? 248  GLY   B CA  1 
ATOM   1544  C  C   . GLY   A 1 248  ? 142.374 135.244 162.703 1.00 46.24  ? 248  GLY   B C   1 
ATOM   1545  O  O   . GLY   A 1 248  ? 142.995 136.294 162.891 1.00 48.03  ? 248  GLY   B O   1 
ATOM   1546  N  N   . GLY   A 1 249  ? 141.902 134.899 161.508 1.00 45.75  ? 249  GLY   B N   1 
ATOM   1547  C  CA  . GLY   A 1 249  ? 142.073 135.772 160.365 1.00 43.29  ? 249  GLY   B CA  1 
ATOM   1548  C  C   . GLY   A 1 249  ? 140.996 136.815 160.179 1.00 53.06  ? 249  GLY   B C   1 
ATOM   1549  O  O   . GLY   A 1 249  ? 141.185 137.743 159.386 1.00 60.28  ? 249  GLY   B O   1 
ATOM   1550  N  N   . ILE   A 1 250  ? 139.870 136.688 160.885 1.00 48.24  ? 250  ILE   B N   1 
ATOM   1551  C  CA  . ILE   A 1 250  ? 138.811 137.684 160.787 1.00 41.31  ? 250  ILE   B CA  1 
ATOM   1552  C  C   . ILE   A 1 250  ? 139.246 139.015 161.386 1.00 43.08  ? 250  ILE   B C   1 
ATOM   1553  O  O   . ILE   A 1 250  ? 138.673 140.059 161.056 1.00 52.00  ? 250  ILE   B O   1 
ATOM   1554  C  CB  . ILE   A 1 250  ? 137.529 137.161 161.463 1.00 43.59  ? 250  ILE   B CB  1 
ATOM   1555  C  CG1 . ILE   A 1 250  ? 137.235 135.733 161.011 1.00 44.95  ? 250  ILE   B CG1 1 
ATOM   1556  C  CG2 . ILE   A 1 250  ? 136.338 138.043 161.126 1.00 45.89  ? 250  ILE   B CG2 1 
ATOM   1557  C  CD1 . ILE   A 1 250  ? 136.955 135.606 159.533 1.00 46.65  ? 250  ILE   B CD1 1 
ATOM   1558  N  N   . LYS   A 1 251  ? 140.264 139.005 162.248 1.00 38.22  ? 251  LYS   B N   1 
ATOM   1559  C  CA  . LYS   A 1 251  ? 140.748 140.244 162.847 1.00 40.72  ? 251  LYS   B CA  1 
ATOM   1560  C  C   . LYS   A 1 251  ? 141.278 141.203 161.791 1.00 46.64  ? 251  LYS   B C   1 
ATOM   1561  O  O   . LYS   A 1 251  ? 141.050 142.416 161.872 1.00 55.01  ? 251  LYS   B O   1 
ATOM   1562  C  CB  . LYS   A 1 251  ? 141.841 139.936 163.867 1.00 43.75  ? 251  LYS   B CB  1 
ATOM   1563  C  CG  . LYS   A 1 251  ? 141.413 139.026 164.996 1.00 51.31  ? 251  LYS   B CG  1 
ATOM   1564  C  CD  . LYS   A 1 251  ? 142.623 138.522 165.760 1.00 52.86  ? 251  LYS   B CD  1 
ATOM   1565  C  CE  . LYS   A 1 251  ? 143.545 139.662 166.149 1.00 46.84  ? 251  LYS   B CE  1 
ATOM   1566  N  NZ  . LYS   A 1 251  ? 144.754 139.174 166.866 1.00 49.78  ? 251  LYS   B NZ  1 
ATOM   1567  N  N   . LYS   A 1 252  ? 141.988 140.678 160.792 1.00 43.71  ? 252  LYS   B N   1 
ATOM   1568  C  CA  . LYS   A 1 252  ? 142.665 141.522 159.816 1.00 46.64  ? 252  LYS   B CA  1 
ATOM   1569  C  C   . LYS   A 1 252  ? 141.698 142.326 158.957 1.00 49.16  ? 252  LYS   B C   1 
ATOM   1570  O  O   . LYS   A 1 252  ? 142.113 143.314 158.343 1.00 56.25  ? 252  LYS   B O   1 
ATOM   1571  C  CB  . LYS   A 1 252  ? 143.565 140.659 158.935 1.00 46.79  ? 252  LYS   B CB  1 
ATOM   1572  C  CG  . LYS   A 1 252  ? 144.504 139.768 159.725 1.00 44.70  ? 252  LYS   B CG  1 
ATOM   1573  C  CD  . LYS   A 1 252  ? 145.293 138.849 158.816 1.00 47.40  ? 252  LYS   B CD  1 
ATOM   1574  C  CE  . LYS   A 1 252  ? 146.215 137.946 159.613 1.00 48.28  ? 252  LYS   B CE  1 
ATOM   1575  N  NZ  . LYS   A 1 252  ? 146.951 136.997 158.735 1.00 49.96  ? 252  LYS   B NZ  1 
ATOM   1576  N  N   . ASN   A 1 253  ? 140.427 141.928 158.894 1.00 41.67  ? 253  ASN   B N   1 
ATOM   1577  C  CA  . ASN   A 1 253  ? 139.429 142.713 158.181 1.00 41.81  ? 253  ASN   B CA  1 
ATOM   1578  C  C   . ASN   A 1 253  ? 139.112 144.031 158.874 1.00 50.90  ? 253  ASN   B C   1 
ATOM   1579  O  O   . ASN   A 1 253  ? 138.493 144.902 158.254 1.00 56.77  ? 253  ASN   B O   1 
ATOM   1580  C  CB  . ASN   A 1 253  ? 138.137 141.909 158.020 1.00 41.08  ? 253  ASN   B CB  1 
ATOM   1581  C  CG  . ASN   A 1 253  ? 138.287 140.743 157.075 1.00 44.89  ? 253  ASN   B CG  1 
ATOM   1582  O  OD1 . ASN   A 1 253  ? 138.916 140.856 156.025 1.00 45.37  ? 253  ASN   B OD1 1 
ATOM   1583  N  ND2 . ASN   A 1 253  ? 137.704 139.610 157.439 1.00 50.88  ? 253  ASN   B ND2 1 
ATOM   1584  N  N   . TYR   A 1 254  ? 139.516 144.198 160.130 1.00 38.08  ? 254  TYR   B N   1 
ATOM   1585  C  CA  . TYR   A 1 254  ? 139.142 145.355 160.926 1.00 39.06  ? 254  TYR   B CA  1 
ATOM   1586  C  C   . TYR   A 1 254  ? 140.389 145.984 161.529 1.00 40.81  ? 254  TYR   B C   1 
ATOM   1587  O  O   . TYR   A 1 254  ? 141.422 145.332 161.693 1.00 49.34  ? 254  TYR   B O   1 
ATOM   1588  C  CB  . TYR   A 1 254  ? 138.150 144.967 162.027 1.00 39.58  ? 254  TYR   B CB  1 
ATOM   1589  C  CG  . TYR   A 1 254  ? 137.029 144.086 161.531 1.00 34.39  ? 254  TYR   B CG  1 
ATOM   1590  C  CD1 . TYR   A 1 254  ? 135.903 144.632 160.939 1.00 41.52  ? 254  TYR   B CD1 1 
ATOM   1591  C  CD2 . TYR   A 1 254  ? 137.103 142.710 161.650 1.00 39.84  ? 254  TYR   B CD2 1 
ATOM   1592  C  CE1 . TYR   A 1 254  ? 134.883 143.830 160.481 1.00 42.53  ? 254  TYR   B CE1 1 
ATOM   1593  C  CE2 . TYR   A 1 254  ? 136.089 141.902 161.195 1.00 41.26  ? 254  TYR   B CE2 1 
ATOM   1594  C  CZ  . TYR   A 1 254  ? 134.982 142.467 160.612 1.00 43.14  ? 254  TYR   B CZ  1 
ATOM   1595  O  OH  . TYR   A 1 254  ? 133.969 141.659 160.157 1.00 46.59  ? 254  TYR   B OH  1 
ATOM   1596  N  N   . ALA   A 1 255  ? 140.280 147.268 161.859 1.00 43.09  ? 255  ALA   B N   1 
ATOM   1597  C  CA  . ALA   A 1 255  ? 141.398 148.046 162.368 1.00 46.19  ? 255  ALA   B CA  1 
ATOM   1598  C  C   . ALA   A 1 255  ? 141.168 148.409 163.827 1.00 47.47  ? 255  ALA   B C   1 
ATOM   1599  O  O   . ALA   A 1 255  ? 140.036 148.652 164.254 1.00 53.31  ? 255  ALA   B O   1 
ATOM   1600  C  CB  . ALA   A 1 255  ? 141.608 149.323 161.549 1.00 48.10  ? 255  ALA   B CB  1 
ATOM   1601  N  N   . SER   A 1 256  ? 142.261 148.440 164.593 1.00 50.96  ? 256  SER   B N   1 
ATOM   1602  C  CA  . SER   A 1 256  ? 142.165 148.805 166.002 1.00 53.55  ? 256  SER   B CA  1 
ATOM   1603  C  C   . SER   A 1 256  ? 141.818 150.279 166.172 1.00 56.43  ? 256  SER   B C   1 
ATOM   1604  O  O   . SER   A 1 256  ? 141.060 150.642 167.079 1.00 58.28  ? 256  SER   B O   1 
ATOM   1605  C  CB  . SER   A 1 256  ? 143.472 148.472 166.720 1.00 51.85  ? 256  SER   B CB  1 
ATOM   1606  O  OG  . SER   A 1 256  ? 144.564 149.166 166.146 1.00 53.36  ? 256  SER   B OG  1 
ATOM   1607  N  N   . THR   A 1 257  ? 142.357 151.141 165.313 1.00 56.89  ? 257  THR   B N   1 
ATOM   1608  C  CA  . THR   A 1 257  ? 142.107 152.571 165.411 1.00 52.09  ? 257  THR   B CA  1 
ATOM   1609  C  C   . THR   A 1 257  ? 142.207 153.194 164.028 1.00 53.49  ? 257  THR   B C   1 
ATOM   1610  O  O   . THR   A 1 257  ? 142.783 152.616 163.103 1.00 58.80  ? 257  THR   B O   1 
ATOM   1611  C  CB  . THR   A 1 257  ? 143.086 153.253 166.372 1.00 59.26  ? 257  THR   B CB  1 
ATOM   1612  O  OG1 . THR   A 1 257  ? 142.778 154.649 166.462 1.00 62.21  ? 257  THR   B OG1 1 
ATOM   1613  C  CG2 . THR   A 1 257  ? 144.515 153.086 165.881 1.00 57.74  ? 257  THR   B CG2 1 
ATOM   1614  N  N   . LEU   A 1 258  ? 141.633 154.386 163.899 1.00 59.49  ? 258  LEU   B N   1 
ATOM   1615  C  CA  . LEU   A 1 258  ? 141.647 155.144 162.655 1.00 60.02  ? 258  LEU   B CA  1 
ATOM   1616  C  C   . LEU   A 1 258  ? 142.607 156.316 162.791 1.00 59.20  ? 258  LEU   B C   1 
ATOM   1617  O  O   . LEU   A 1 258  ? 142.533 157.076 163.763 1.00 62.24  ? 258  LEU   B O   1 
ATOM   1618  C  CB  . LEU   A 1 258  ? 140.245 155.644 162.304 1.00 58.71  ? 258  LEU   B CB  1 
ATOM   1619  C  CG  . LEU   A 1 258  ? 139.353 154.750 161.443 1.00 56.72  ? 258  LEU   B CG  1 
ATOM   1620  C  CD1 . LEU   A 1 258  ? 139.256 153.349 162.007 1.00 56.70  ? 258  LEU   B CD1 1 
ATOM   1621  C  CD2 . LEU   A 1 258  ? 137.973 155.364 161.310 1.00 59.37  ? 258  LEU   B CD2 1 
ATOM   1622  N  N   . THR   A 1 259  ? 143.505 156.461 161.819 1.00 62.18  ? 259  THR   B N   1 
ATOM   1623  C  CA  . THR   A 1 259  ? 144.561 157.461 161.871 1.00 63.35  ? 259  THR   B CA  1 
ATOM   1624  C  C   . THR   A 1 259  ? 144.287 158.669 160.984 1.00 66.61  ? 259  THR   B C   1 
ATOM   1625  O  O   . THR   A 1 259  ? 145.188 159.487 160.777 1.00 69.96  ? 259  THR   B O   1 
ATOM   1626  C  CB  . THR   A 1 259  ? 145.899 156.831 161.482 1.00 63.89  ? 259  THR   B CB  1 
ATOM   1627  O  OG1 . THR   A 1 259  ? 145.832 156.358 160.132 1.00 63.51  ? 259  THR   B OG1 1 
ATOM   1628  C  CG2 . THR   A 1 259  ? 146.225 155.667 162.404 1.00 64.41  ? 259  THR   B CG2 1 
ATOM   1629  N  N   . TYR   A 1 260  ? 143.070 158.805 160.455 1.00 62.94  ? 260  TYR   B N   1 
ATOM   1630  C  CA  . TYR   A 1 260  ? 142.750 159.900 159.552 1.00 57.61  ? 260  TYR   B CA  1 
ATOM   1631  C  C   . TYR   A 1 260  ? 141.580 160.762 160.001 1.00 64.07  ? 260  TYR   B C   1 
ATOM   1632  O  O   . TYR   A 1 260  ? 141.420 161.870 159.476 1.00 67.32  ? 260  TYR   B O   1 
ATOM   1633  C  CB  . TYR   A 1 260  ? 142.465 159.363 158.139 1.00 58.66  ? 260  TYR   B CB  1 
ATOM   1634  C  CG  . TYR   A 1 260  ? 141.240 158.486 158.025 1.00 60.00  ? 260  TYR   B CG  1 
ATOM   1635  C  CD1 . TYR   A 1 260  ? 141.244 157.185 158.505 1.00 61.23  ? 260  TYR   B CD1 1 
ATOM   1636  C  CD2 . TYR   A 1 260  ? 140.089 158.951 157.409 1.00 60.41  ? 260  TYR   B CD2 1 
ATOM   1637  C  CE1 . TYR   A 1 260  ? 140.130 156.382 158.393 1.00 60.97  ? 260  TYR   B CE1 1 
ATOM   1638  C  CE2 . TYR   A 1 260  ? 138.972 158.155 157.293 1.00 60.25  ? 260  TYR   B CE2 1 
ATOM   1639  C  CZ  . TYR   A 1 260  ? 138.998 156.872 157.786 1.00 59.36  ? 260  TYR   B CZ  1 
ATOM   1640  O  OH  . TYR   A 1 260  ? 137.885 156.075 157.671 1.00 61.37  ? 260  TYR   B OH  1 
ATOM   1641  N  N   . ILE   A 1 261  ? 140.763 160.301 160.945 1.00 68.99  ? 261  ILE   B N   1 
ATOM   1642  C  CA  . ILE   A 1 261  ? 139.650 161.078 161.476 1.00 63.12  ? 261  ILE   B CA  1 
ATOM   1643  C  C   . ILE   A 1 261  ? 139.702 161.022 162.995 1.00 63.49  ? 261  ILE   B C   1 
ATOM   1644  O  O   . ILE   A 1 261  ? 139.896 159.951 163.580 1.00 70.02  ? 261  ILE   B O   1 
ATOM   1645  C  CB  . ILE   A 1 261  ? 138.290 160.564 160.954 1.00 66.83  ? 261  ILE   B CB  1 
ATOM   1646  C  CG1 . ILE   A 1 261  ? 138.124 160.895 159.472 1.00 68.91  ? 261  ILE   B CG1 1 
ATOM   1647  C  CG2 . ILE   A 1 261  ? 137.145 161.166 161.742 1.00 67.23  ? 261  ILE   B CG2 1 
ATOM   1648  C  CD1 . ILE   A 1 261  ? 136.777 160.499 158.907 1.00 68.85  ? 261  ILE   B CD1 1 
ATOM   1649  N  N   . SER   A 1 262  ? 139.542 162.178 163.633 1.00 61.75  ? 262  SER   B N   1 
ATOM   1650  C  CA  . SER   A 1 262  ? 139.495 162.231 165.083 1.00 62.26  ? 262  SER   B CA  1 
ATOM   1651  C  C   . SER   A 1 262  ? 138.230 161.541 165.594 1.00 66.40  ? 262  SER   B C   1 
ATOM   1652  O  O   . SER   A 1 262  ? 137.201 161.535 164.913 1.00 72.99  ? 262  SER   B O   1 
ATOM   1653  C  CB  . SER   A 1 262  ? 139.534 163.680 165.560 1.00 66.93  ? 262  SER   B CB  1 
ATOM   1654  O  OG  . SER   A 1 262  ? 139.540 163.765 166.974 1.00 69.60  ? 262  SER   B OG  1 
ATOM   1655  N  N   . PRO   A 1 263  ? 138.283 160.943 166.787 1.00 58.22  ? 263  PRO   B N   1 
ATOM   1656  C  CA  . PRO   A 1 263  ? 137.093 160.249 167.309 1.00 56.93  ? 263  PRO   B CA  1 
ATOM   1657  C  C   . PRO   A 1 263  ? 135.872 161.140 167.446 1.00 62.59  ? 263  PRO   B C   1 
ATOM   1658  O  O   . PRO   A 1 263  ? 134.745 160.652 167.295 1.00 66.83  ? 263  PRO   B O   1 
ATOM   1659  C  CB  . PRO   A 1 263  ? 137.566 159.732 168.673 1.00 60.09  ? 263  PRO   B CB  1 
ATOM   1660  C  CG  . PRO   A 1 263  ? 139.037 159.592 168.527 1.00 64.24  ? 263  PRO   B CG  1 
ATOM   1661  C  CD  . PRO   A 1 263  ? 139.468 160.714 167.631 1.00 62.94  ? 263  PRO   B CD  1 
ATOM   1662  N  N   . SER   A 1 264  ? 136.054 162.430 167.728 1.00 64.01  ? 264  SER   B N   1 
ATOM   1663  C  CA  . SER   A 1 264  ? 134.925 163.341 167.869 1.00 61.68  ? 264  SER   B CA  1 
ATOM   1664  C  C   . SER   A 1 264  ? 134.252 163.667 166.542 1.00 61.59  ? 264  SER   B C   1 
ATOM   1665  O  O   . SER   A 1 264  ? 133.162 164.249 166.549 1.00 64.90  ? 264  SER   B O   1 
ATOM   1666  C  CB  . SER   A 1 264  ? 135.375 164.638 168.545 1.00 61.91  ? 264  SER   B CB  1 
ATOM   1667  O  OG  . SER   A 1 264  ? 136.374 165.291 167.784 1.00 64.24  ? 264  SER   B OG  1 
ATOM   1668  N  N   . ASP   A 1 265  ? 134.864 163.314 165.415 1.00 63.17  ? 265  ASP   B N   1 
ATOM   1669  C  CA  . ASP   A 1 265  ? 134.288 163.551 164.099 1.00 63.41  ? 265  ASP   B CA  1 
ATOM   1670  C  C   . ASP   A 1 265  ? 133.612 162.313 163.526 1.00 62.09  ? 265  ASP   B C   1 
ATOM   1671  O  O   . ASP   A 1 265  ? 133.275 162.297 162.339 1.00 65.66  ? 265  ASP   B O   1 
ATOM   1672  C  CB  . ASP   A 1 265  ? 135.362 164.055 163.134 1.00 63.69  ? 265  ASP   B CB  1 
ATOM   1673  C  CG  . ASP   A 1 265  ? 135.932 165.396 163.545 1.00 69.09  ? 265  ASP   B CG  1 
ATOM   1674  O  OD1 . ASP   A 1 265  ? 135.216 166.166 164.218 1.00 71.97  ? 265  ASP   B OD1 1 
ATOM   1675  O  OD2 . ASP   A 1 265  ? 137.095 165.682 163.193 1.00 67.25  ? 265  ASP   B OD2 1 
ATOM   1676  N  N   . VAL   A 1 266  ? 133.412 161.281 164.338 1.00 57.80  ? 266  VAL   B N   1 
ATOM   1677  C  CA  . VAL   A 1 266  ? 132.780 160.039 163.916 1.00 55.51  ? 266  VAL   B CA  1 
ATOM   1678  C  C   . VAL   A 1 266  ? 131.550 159.809 164.781 1.00 59.70  ? 266  VAL   B C   1 
ATOM   1679  O  O   . VAL   A 1 266  ? 131.620 159.917 166.010 1.00 60.47  ? 266  VAL   B O   1 
ATOM   1680  C  CB  . VAL   A 1 266  ? 133.751 158.848 164.013 1.00 62.35  ? 266  VAL   B CB  1 
ATOM   1681  C  CG1 . VAL   A 1 266  ? 132.991 157.556 164.226 1.00 62.15  ? 266  VAL   B CG1 1 
ATOM   1682  C  CG2 . VAL   A 1 266  ? 134.598 158.759 162.760 1.00 59.47  ? 266  VAL   B CG2 1 
ATOM   1683  N  N   . LEU   A 1 267  ? 130.426 159.507 164.139 1.00 58.15  ? 267  LEU   B N   1 
ATOM   1684  C  CA  . LEU   A 1 267  ? 129.213 159.190 164.878 1.00 56.08  ? 267  LEU   B CA  1 
ATOM   1685  C  C   . LEU   A 1 267  ? 129.097 157.684 165.091 1.00 56.54  ? 267  LEU   B C   1 
ATOM   1686  O  O   . LEU   A 1 267  ? 129.319 156.907 164.159 1.00 59.90  ? 267  LEU   B O   1 
ATOM   1687  C  CB  . LEU   A 1 267  ? 127.980 159.692 164.135 1.00 55.22  ? 267  LEU   B CB  1 
ATOM   1688  C  CG  . LEU   A 1 267  ? 127.721 161.195 164.178 1.00 58.13  ? 267  LEU   B CG  1 
ATOM   1689  C  CD1 . LEU   A 1 267  ? 126.488 161.547 163.369 1.00 58.21  ? 267  LEU   B CD1 1 
ATOM   1690  C  CD2 . LEU   A 1 267  ? 127.571 161.658 165.615 1.00 55.32  ? 267  LEU   B CD2 1 
ATOM   1691  N  N   . PRO   A 1 268  ? 128.758 157.250 166.306 1.00 50.08  ? 268  PRO   B N   1 
ATOM   1692  C  CA  . PRO   A 1 268  ? 128.494 155.833 166.519 1.00 42.04  ? 268  PRO   B CA  1 
ATOM   1693  C  C   . PRO   A 1 268  ? 127.244 155.409 165.771 1.00 52.89  ? 268  PRO   B C   1 
ATOM   1694  O  O   . PRO   A 1 268  ? 126.385 156.247 165.449 1.00 65.33  ? 268  PRO   B O   1 
ATOM   1695  C  CB  . PRO   A 1 268  ? 128.296 155.734 168.043 1.00 48.91  ? 268  PRO   B CB  1 
ATOM   1696  C  CG  . PRO   A 1 268  ? 128.898 156.975 168.594 1.00 55.73  ? 268  PRO   B CG  1 
ATOM   1697  C  CD  . PRO   A 1 268  ? 128.675 158.019 167.556 1.00 57.10  ? 268  PRO   B CD  1 
ATOM   1698  N  N   . PRO   A 1 269  ? 127.101 154.121 165.465 1.00 41.82  ? 269  PRO   B N   1 
ATOM   1699  C  CA  . PRO   A 1 269  ? 125.910 153.673 164.755 1.00 40.79  ? 269  PRO   B CA  1 
ATOM   1700  C  C   . PRO   A 1 269  ? 124.662 153.993 165.551 1.00 47.92  ? 269  PRO   B C   1 
ATOM   1701  O  O   . PRO   A 1 269  ? 124.690 154.039 166.795 1.00 52.61  ? 269  PRO   B O   1 
ATOM   1702  C  CB  . PRO   A 1 269  ? 126.128 152.160 164.625 1.00 40.27  ? 269  PRO   B CB  1 
ATOM   1703  C  CG  . PRO   A 1 269  ? 127.596 152.001 164.656 1.00 46.86  ? 269  PRO   B CG  1 
ATOM   1704  C  CD  . PRO   A 1 269  ? 128.096 153.046 165.602 1.00 47.29  ? 269  PRO   B CD  1 
ATOM   1705  N  N   . PRO   A 1 270  ? 123.539 154.243 164.871 1.00 38.62  ? 270  PRO   B N   1 
ATOM   1706  C  CA  . PRO   A 1 270  ? 122.352 154.752 165.579 1.00 37.97  ? 270  PRO   B CA  1 
ATOM   1707  C  C   . PRO   A 1 270  ? 121.866 153.853 166.702 1.00 45.85  ? 270  PRO   B C   1 
ATOM   1708  O  O   . PRO   A 1 270  ? 121.388 154.358 167.725 1.00 54.93  ? 270  PRO   B O   1 
ATOM   1709  C  CB  . PRO   A 1 270  ? 121.309 154.871 164.459 1.00 36.99  ? 270  PRO   B CB  1 
ATOM   1710  C  CG  . PRO   A 1 270  ? 122.101 154.974 163.207 1.00 43.20  ? 270  PRO   B CG  1 
ATOM   1711  C  CD  . PRO   A 1 270  ? 123.311 154.126 163.423 1.00 40.28  ? 270  PRO   B CD  1 
ATOM   1712  N  N   . ASN   A 1 271  ? 121.974 152.537 166.548 1.00 43.10  ? 271  ASN   B N   1 
ATOM   1713  C  CA  . ASN   A 1 271  ? 121.517 151.608 167.572 1.00 38.92  ? 271  ASN   B CA  1 
ATOM   1714  C  C   . ASN   A 1 271  ? 122.567 151.343 168.642 1.00 44.28  ? 271  ASN   B C   1 
ATOM   1715  O  O   . ASN   A 1 271  ? 122.301 150.575 169.571 1.00 53.62  ? 271  ASN   B O   1 
ATOM   1716  C  CB  . ASN   A 1 271  ? 121.077 150.290 166.934 1.00 37.97  ? 271  ASN   B CB  1 
ATOM   1717  C  CG  . ASN   A 1 271  ? 119.952 150.475 165.940 1.00 39.49  ? 271  ASN   B CG  1 
ATOM   1718  O  OD1 . ASN   A 1 271  ? 119.783 151.553 165.374 1.00 46.96  ? 271  ASN   B OD1 1 
ATOM   1719  N  ND2 . ASN   A 1 271  ? 119.171 149.425 165.725 1.00 40.43  ? 271  ASN   B ND2 1 
ATOM   1720  N  N   . TRP   A 1 272  ? 123.746 151.950 168.536 1.00 37.63  ? 272  TRP   B N   1 
ATOM   1721  C  CA  . TRP   A 1 272  ? 124.759 151.882 169.578 1.00 36.18  ? 272  TRP   B CA  1 
ATOM   1722  C  C   . TRP   A 1 272  ? 124.690 153.075 170.521 1.00 41.20  ? 272  TRP   B C   1 
ATOM   1723  O  O   . TRP   A 1 272  ? 125.620 153.289 171.303 1.00 51.47  ? 272  TRP   B O   1 
ATOM   1724  C  CB  . TRP   A 1 272  ? 126.160 151.793 168.967 1.00 44.32  ? 272  TRP   B CB  1 
ATOM   1725  C  CG  . TRP   A 1 272  ? 126.427 150.562 168.149 1.00 44.23  ? 272  TRP   B CG  1 
ATOM   1726  C  CD1 . TRP   A 1 272  ? 125.508 149.708 167.618 1.00 46.54  ? 272  TRP   B CD1 1 
ATOM   1727  C  CD2 . TRP   A 1 272  ? 127.710 150.051 167.773 1.00 40.33  ? 272  TRP   B CD2 1 
ATOM   1728  N  NE1 . TRP   A 1 272  ? 126.137 148.701 166.932 1.00 43.57  ? 272  TRP   B NE1 1 
ATOM   1729  C  CE2 . TRP   A 1 272  ? 127.491 148.889 167.013 1.00 38.81  ? 272  TRP   B CE2 1 
ATOM   1730  C  CE3 . TRP   A 1 272  ? 129.023 150.465 168.004 1.00 42.73  ? 272  TRP   B CE3 1 
ATOM   1731  C  CZ2 . TRP   A 1 272  ? 128.534 148.138 166.484 1.00 38.93  ? 272  TRP   B CZ2 1 
ATOM   1732  C  CZ3 . TRP   A 1 272  ? 130.056 149.719 167.478 1.00 43.32  ? 272  TRP   B CZ3 1 
ATOM   1733  C  CH2 . TRP   A 1 272  ? 129.806 148.568 166.727 1.00 41.33  ? 272  TRP   B CH2 1 
ATOM   1734  N  N   . ALA   A 1 273  ? 123.616 153.864 170.450 1.00 43.45  ? 273  ALA   B N   1 
ATOM   1735  C  CA  . ALA   A 1 273  ? 123.518 155.069 171.265 1.00 42.88  ? 273  ALA   B CA  1 
ATOM   1736  C  C   . ALA   A 1 273  ? 123.490 154.738 172.750 1.00 49.95  ? 273  ALA   B C   1 
ATOM   1737  O  O   . ALA   A 1 273  ? 124.107 155.439 173.561 1.00 55.20  ? 273  ALA   B O   1 
ATOM   1738  C  CB  . ALA   A 1 273  ? 122.277 155.868 170.871 1.00 48.27  ? 273  ALA   B CB  1 
ATOM   1739  N  N   . LEU   A 1 274  ? 122.778 153.677 173.129 1.00 54.82  ? 274  LEU   B N   1 
ATOM   1740  C  CA  . LEU   A 1 274  ? 122.686 153.310 174.536 1.00 50.39  ? 274  LEU   B CA  1 
ATOM   1741  C  C   . LEU   A 1 274  ? 124.006 152.783 175.082 1.00 49.85  ? 274  LEU   B C   1 
ATOM   1742  O  O   . LEU   A 1 274  ? 124.210 152.799 176.299 1.00 54.44  ? 274  LEU   B O   1 
ATOM   1743  C  CB  . LEU   A 1 274  ? 121.578 152.277 174.731 1.00 48.44  ? 274  LEU   B CB  1 
ATOM   1744  C  CG  . LEU   A 1 274  ? 120.981 152.166 176.132 1.00 49.25  ? 274  LEU   B CG  1 
ATOM   1745  C  CD1 . LEU   A 1 274  ? 120.456 153.512 176.592 1.00 52.12  ? 274  LEU   B CD1 1 
ATOM   1746  C  CD2 . LEU   A 1 274  ? 119.875 151.125 176.153 1.00 53.75  ? 274  LEU   B CD2 1 
ATOM   1747  N  N   . LYS   A 1 275  ? 124.903 152.320 174.213 1.00 52.16  ? 275  LYS   B N   1 
ATOM   1748  C  CA  . LYS   A 1 275  ? 126.219 151.856 174.633 1.00 49.19  ? 275  LYS   B CA  1 
ATOM   1749  C  C   . LYS   A 1 275  ? 127.260 152.966 174.620 1.00 53.26  ? 275  LYS   B C   1 
ATOM   1750  O  O   . LYS   A 1 275  ? 128.147 152.985 175.481 1.00 59.86  ? 275  LYS   B O   1 
ATOM   1751  C  CB  . LYS   A 1 275  ? 126.676 150.707 173.731 1.00 52.21  ? 275  LYS   B CB  1 
ATOM   1752  C  CG  . LYS   A 1 275  ? 127.946 150.015 174.180 1.00 59.36  ? 275  LYS   B CG  1 
ATOM   1753  C  CD  . LYS   A 1 275  ? 128.279 148.850 173.261 1.00 61.67  ? 275  LYS   B CD  1 
ATOM   1754  C  CE  . LYS   A 1 275  ? 129.523 148.111 173.727 1.00 57.72  ? 275  LYS   B CE  1 
ATOM   1755  N  NZ  . LYS   A 1 275  ? 130.719 148.997 173.749 1.00 58.97  ? 275  LYS   B NZ  1 
ATOM   1756  N  N   . TYR   A 1 276  ? 127.169 153.892 173.666 1.00 53.73  ? 276  TYR   B N   1 
ATOM   1757  C  CA  . TYR   A 1 276  ? 128.043 155.061 173.587 1.00 46.36  ? 276  TYR   B CA  1 
ATOM   1758  C  C   . TYR   A 1 276  ? 127.149 156.292 173.604 1.00 52.58  ? 276  TYR   B C   1 
ATOM   1759  O  O   . TYR   A 1 276  ? 126.778 156.819 172.546 1.00 62.35  ? 276  TYR   B O   1 
ATOM   1760  C  CB  . TYR   A 1 276  ? 128.914 155.032 172.331 1.00 49.92  ? 276  TYR   B CB  1 
ATOM   1761  C  CG  . TYR   A 1 276  ? 129.842 153.845 172.228 1.00 52.14  ? 276  TYR   B CG  1 
ATOM   1762  C  CD1 . TYR   A 1 276  ? 131.064 153.837 172.882 1.00 53.39  ? 276  TYR   B CD1 1 
ATOM   1763  C  CD2 . TYR   A 1 276  ? 129.503 152.739 171.464 1.00 51.16  ? 276  TYR   B CD2 1 
ATOM   1764  C  CE1 . TYR   A 1 276  ? 131.915 152.759 172.788 1.00 57.32  ? 276  TYR   B CE1 1 
ATOM   1765  C  CE2 . TYR   A 1 276  ? 130.349 151.656 171.365 1.00 52.47  ? 276  TYR   B CE2 1 
ATOM   1766  C  CZ  . TYR   A 1 276  ? 131.554 151.671 172.028 1.00 56.24  ? 276  TYR   B CZ  1 
ATOM   1767  O  OH  . TYR   A 1 276  ? 132.402 150.594 171.932 1.00 57.69  ? 276  TYR   B OH  1 
ATOM   1768  N  N   . PRO   A 1 277  ? 126.775 156.775 174.792 1.00 46.48  ? 277  PRO   B N   1 
ATOM   1769  C  CA  . PRO   A 1 277  ? 125.798 157.878 174.849 1.00 49.13  ? 277  PRO   B CA  1 
ATOM   1770  C  C   . PRO   A 1 277  ? 126.312 159.175 174.250 1.00 54.00  ? 277  PRO   B C   1 
ATOM   1771  O  O   . PRO   A 1 277  ? 125.633 159.783 173.413 1.00 57.36  ? 277  PRO   B O   1 
ATOM   1772  C  CB  . PRO   A 1 277  ? 125.517 158.010 176.353 1.00 51.51  ? 277  PRO   B CB  1 
ATOM   1773  C  CG  . PRO   A 1 277  ? 125.958 156.715 176.952 1.00 52.75  ? 277  PRO   B CG  1 
ATOM   1774  C  CD  . PRO   A 1 277  ? 127.120 156.272 176.129 1.00 51.60  ? 277  PRO   B CD  1 
ATOM   1775  N  N   . ASN   A 1 278  ? 127.497 159.618 174.656 1.00 51.43  ? 278  ASN   B N   1 
ATOM   1776  C  CA  . ASN   A 1 278  ? 128.068 160.867 174.179 1.00 46.73  ? 278  ASN   B CA  1 
ATOM   1777  C  C   . ASN   A 1 278  ? 128.970 160.677 172.969 1.00 53.26  ? 278  ASN   B C   1 
ATOM   1778  O  O   . ASN   A 1 278  ? 129.598 161.641 172.521 1.00 58.00  ? 278  ASN   B O   1 
ATOM   1779  C  CB  . ASN   A 1 278  ? 128.846 161.551 175.303 1.00 49.19  ? 278  ASN   B CB  1 
ATOM   1780  C  CG  . ASN   A 1 278  ? 128.011 161.748 176.549 1.00 55.61  ? 278  ASN   B CG  1 
ATOM   1781  O  OD1 . ASN   A 1 278  ? 127.291 162.737 176.678 1.00 60.14  ? 278  ASN   B OD1 1 
ATOM   1782  N  ND2 . ASN   A 1 278  ? 128.103 160.804 177.477 1.00 56.58  ? 278  ASN   B ND2 1 
ATOM   1783  N  N   . GLY   A 1 279  ? 129.048 159.468 172.435 1.00 56.06  ? 279  GLY   B N   1 
ATOM   1784  C  CA  . GLY   A 1 279  ? 129.905 159.183 171.305 1.00 55.33  ? 279  GLY   B CA  1 
ATOM   1785  C  C   . GLY   A 1 279  ? 131.204 158.531 171.725 1.00 55.07  ? 279  GLY   B C   1 
ATOM   1786  O  O   . GLY   A 1 279  ? 131.401 158.121 172.872 1.00 58.45  ? 279  GLY   B O   1 
ATOM   1787  N  N   . TYR   A 1 280  ? 132.113 158.439 170.757 1.00 50.69  ? 280  TYR   B N   1 
ATOM   1788  C  CA  . TYR   A 1 280  ? 133.425 157.837 170.981 1.00 53.96  ? 280  TYR   B CA  1 
ATOM   1789  C  C   . TYR   A 1 280  ? 134.297 158.842 171.729 1.00 63.24  ? 280  TYR   B C   1 
ATOM   1790  O  O   . TYR   A 1 280  ? 135.204 159.471 171.178 1.00 66.09  ? 280  TYR   B O   1 
ATOM   1791  C  CB  . TYR   A 1 280  ? 134.051 157.414 169.660 1.00 55.23  ? 280  TYR   B CB  1 
ATOM   1792  C  CG  . TYR   A 1 280  ? 133.283 156.331 168.943 1.00 52.13  ? 280  TYR   B CG  1 
ATOM   1793  C  CD1 . TYR   A 1 280  ? 132.550 155.391 169.648 1.00 50.63  ? 280  TYR   B CD1 1 
ATOM   1794  C  CD2 . TYR   A 1 280  ? 133.289 156.252 167.561 1.00 57.78  ? 280  TYR   B CD2 1 
ATOM   1795  C  CE1 . TYR   A 1 280  ? 131.847 154.401 168.997 1.00 52.86  ? 280  TYR   B CE1 1 
ATOM   1796  C  CE2 . TYR   A 1 280  ? 132.588 155.265 166.902 1.00 56.64  ? 280  TYR   B CE2 1 
ATOM   1797  C  CZ  . TYR   A 1 280  ? 131.870 154.343 167.624 1.00 52.82  ? 280  TYR   B CZ  1 
ATOM   1798  O  OH  . TYR   A 1 280  ? 131.170 153.358 166.969 1.00 52.72  ? 280  TYR   B OH  1 
ATOM   1799  N  N   . VAL   A 1 281  ? 134.008 158.990 173.026 1.00 67.17  ? 281  VAL   B N   1 
ATOM   1800  C  CA  . VAL   A 1 281  ? 134.754 159.915 173.875 1.00 65.04  ? 281  VAL   B CA  1 
ATOM   1801  C  C   . VAL   A 1 281  ? 135.955 159.266 174.543 1.00 69.10  ? 281  VAL   B C   1 
ATOM   1802  O  O   . VAL   A 1 281  ? 136.755 159.971 175.177 1.00 72.62  ? 281  VAL   B O   1 
ATOM   1803  C  CB  . VAL   A 1 281  ? 133.844 160.527 174.958 1.00 68.47  ? 281  VAL   B CB  1 
ATOM   1804  C  CG1 . VAL   A 1 281  ? 132.685 161.271 174.316 1.00 67.79  ? 281  VAL   B CG1 1 
ATOM   1805  C  CG2 . VAL   A 1 281  ? 133.335 159.444 175.894 1.00 68.21  ? 281  VAL   B CG2 1 
ATOM   1806  N  N   . ASP   A 1 282  ? 136.110 157.948 174.427 1.00 77.93  ? 282  ASP   B N   1 
ATOM   1807  C  CA  . ASP   A 1 282  ? 137.249 157.232 174.985 1.00 75.77  ? 282  ASP   B CA  1 
ATOM   1808  C  C   . ASP   A 1 282  ? 138.054 156.541 173.890 1.00 75.80  ? 282  ASP   B C   1 
ATOM   1809  O  O   . ASP   A 1 282  ? 138.620 155.468 174.106 1.00 81.19  ? 282  ASP   B O   1 
ATOM   1810  C  CB  . ASP   A 1 282  ? 136.791 156.223 176.037 1.00 77.78  ? 282  ASP   B CB  1 
ATOM   1811  C  CG  . ASP   A 1 282  ? 135.708 155.293 175.521 1.00 84.51  ? 282  ASP   B CG  1 
ATOM   1812  O  OD1 . ASP   A 1 282  ? 136.031 154.373 174.740 1.00 83.37  ? 282  ASP   B OD1 1 
ATOM   1813  O  OD2 . ASP   A 1 282  ? 134.532 155.483 175.897 1.00 84.73  ? 282  ASP   B OD2 1 
ATOM   1814  N  N   . GLY   A 1 283  ? 138.111 157.149 172.712 1.00 64.06  ? 283  GLY   B N   1 
ATOM   1815  C  CA  . GLY   A 1 283  ? 138.783 156.571 171.570 1.00 65.00  ? 283  GLY   B CA  1 
ATOM   1816  C  C   . GLY   A 1 283  ? 137.847 155.725 170.724 1.00 62.75  ? 283  GLY   B C   1 
ATOM   1817  O  O   . GLY   A 1 283  ? 136.710 155.424 171.094 1.00 65.33  ? 283  GLY   B O   1 
ATOM   1818  N  N   . PHE   A 1 284  ? 138.354 155.340 169.558 1.00 57.20  ? 284  PHE   B N   1 
ATOM   1819  C  CA  . PHE   A 1 284  ? 137.584 154.512 168.649 1.00 54.42  ? 284  PHE   B CA  1 
ATOM   1820  C  C   . PHE   A 1 284  ? 137.330 153.137 169.262 1.00 58.13  ? 284  PHE   B C   1 
ATOM   1821  O  O   . PHE   A 1 284  ? 138.146 152.634 170.039 1.00 65.75  ? 284  PHE   B O   1 
ATOM   1822  C  CB  . PHE   A 1 284  ? 138.320 154.347 167.324 1.00 57.74  ? 284  PHE   B CB  1 
ATOM   1823  C  CG  . PHE   A 1 284  ? 138.235 155.542 166.428 1.00 60.00  ? 284  PHE   B CG  1 
ATOM   1824  C  CD1 . PHE   A 1 284  ? 137.163 155.700 165.572 1.00 61.87  ? 284  PHE   B CD1 1 
ATOM   1825  C  CD2 . PHE   A 1 284  ? 139.231 156.497 166.430 1.00 58.16  ? 284  PHE   B CD2 1 
ATOM   1826  C  CE1 . PHE   A 1 284  ? 137.082 156.793 164.740 1.00 63.91  ? 284  PHE   B CE1 1 
ATOM   1827  C  CE2 . PHE   A 1 284  ? 139.156 157.592 165.600 1.00 59.52  ? 284  PHE   B CE2 1 
ATOM   1828  C  CZ  . PHE   A 1 284  ? 138.079 157.741 164.755 1.00 64.22  ? 284  PHE   B CZ  1 
ATOM   1829  N  N   . PRO   A 1 285  ? 136.200 152.512 168.940 1.00 52.60  ? 285  PRO   B N   1 
ATOM   1830  C  CA  . PRO   A 1 285  ? 135.991 151.127 169.366 1.00 56.36  ? 285  PRO   B CA  1 
ATOM   1831  C  C   . PRO   A 1 285  ? 137.001 150.208 168.697 1.00 63.37  ? 285  PRO   B C   1 
ATOM   1832  O  O   . PRO   A 1 285  ? 137.276 150.321 167.501 1.00 63.06  ? 285  PRO   B O   1 
ATOM   1833  C  CB  . PRO   A 1 285  ? 134.560 150.828 168.909 1.00 55.67  ? 285  PRO   B CB  1 
ATOM   1834  C  CG  . PRO   A 1 285  ? 134.334 151.757 167.775 1.00 59.56  ? 285  PRO   B CG  1 
ATOM   1835  C  CD  . PRO   A 1 285  ? 135.083 153.010 168.122 1.00 59.26  ? 285  PRO   B CD  1 
ATOM   1836  N  N   . ASN   A 1 286  ? 137.559 149.292 169.484 1.00 58.92  ? 286  ASN   B N   1 
ATOM   1837  C  CA  . ASN   A 1 286  ? 138.581 148.373 168.989 1.00 49.56  ? 286  ASN   B CA  1 
ATOM   1838  C  C   . ASN   A 1 286  ? 137.870 147.214 168.307 1.00 49.77  ? 286  ASN   B C   1 
ATOM   1839  O  O   . ASN   A 1 286  ? 137.636 146.162 168.900 1.00 58.28  ? 286  ASN   B O   1 
ATOM   1840  C  CB  . ASN   A 1 286  ? 139.479 147.904 170.125 1.00 54.76  ? 286  ASN   B CB  1 
ATOM   1841  C  CG  . ASN   A 1 286  ? 140.785 147.322 169.631 1.00 59.51  ? 286  ASN   B CG  1 
ATOM   1842  O  OD1 . ASN   A 1 286  ? 140.871 146.820 168.511 1.00 62.38  ? 286  ASN   B OD1 1 
ATOM   1843  N  ND2 . ASN   A 1 286  ? 141.813 147.386 170.467 1.00 58.47  ? 286  ASN   B ND2 1 
ATOM   1844  N  N   . LEU   A 1 287  ? 137.522 147.413 167.035 1.00 45.86  ? 287  LEU   B N   1 
ATOM   1845  C  CA  . LEU   A 1 287  ? 136.813 146.392 166.276 1.00 49.47  ? 287  LEU   B CA  1 
ATOM   1846  C  C   . LEU   A 1 287  ? 137.667 145.163 165.998 1.00 56.86  ? 287  LEU   B C   1 
ATOM   1847  O  O   . LEU   A 1 287  ? 137.128 144.147 165.547 1.00 61.52  ? 287  LEU   B O   1 
ATOM   1848  C  CB  . LEU   A 1 287  ? 136.303 146.975 164.958 1.00 51.88  ? 287  LEU   B CB  1 
ATOM   1849  C  CG  . LEU   A 1 287  ? 135.264 148.092 165.058 1.00 54.70  ? 287  LEU   B CG  1 
ATOM   1850  C  CD1 . LEU   A 1 287  ? 134.835 148.539 163.674 1.00 54.59  ? 287  LEU   B CD1 1 
ATOM   1851  C  CD2 . LEU   A 1 287  ? 134.069 147.638 165.870 1.00 52.23  ? 287  LEU   B CD2 1 
ATOM   1852  N  N   . ARG   A 1 288  ? 138.972 145.229 166.248 1.00 52.96  ? 288  ARG   B N   1 
ATOM   1853  C  CA  . ARG   A 1 288  ? 139.855 144.087 166.055 1.00 44.61  ? 288  ARG   B CA  1 
ATOM   1854  C  C   . ARG   A 1 288  ? 139.943 143.207 167.297 1.00 46.42  ? 288  ARG   B C   1 
ATOM   1855  O  O   . ARG   A 1 288  ? 140.010 141.979 167.182 1.00 59.58  ? 288  ARG   B O   1 
ATOM   1856  C  CB  . ARG   A 1 288  ? 141.250 144.571 165.651 1.00 47.38  ? 288  ARG   B CB  1 
ATOM   1857  C  CG  . ARG   A 1 288  ? 142.337 143.519 165.748 1.00 53.07  ? 288  ARG   B CG  1 
ATOM   1858  C  CD  . ARG   A 1 288  ? 143.644 144.000 165.142 1.00 51.33  ? 288  ARG   B CD  1 
ATOM   1859  N  NE  . ARG   A 1 288  ? 143.575 144.069 163.689 1.00 45.82  ? 288  ARG   B NE  1 
ATOM   1860  C  CZ  . ARG   A 1 288  ? 144.630 144.168 162.893 1.00 49.41  ? 288  ARG   B CZ  1 
ATOM   1861  N  NH1 . ARG   A 1 288  ? 145.859 144.204 163.377 1.00 52.16  ? 288  ARG   B NH1 1 
ATOM   1862  N  NH2 . ARG   A 1 288  ? 144.446 144.224 161.577 1.00 52.11  ? 288  ARG   B NH2 1 
ATOM   1863  N  N   . GLU   A 1 289  ? 139.925 143.808 168.485 1.00 52.63  ? 289  GLU   B N   1 
ATOM   1864  C  CA  . GLU   A 1 289  ? 140.102 143.055 169.719 1.00 54.33  ? 289  GLU   B CA  1 
ATOM   1865  C  C   . GLU   A 1 289  ? 138.811 142.447 170.254 1.00 58.39  ? 289  GLU   B C   1 
ATOM   1866  O  O   . GLU   A 1 289  ? 138.873 141.658 171.202 1.00 64.21  ? 289  GLU   B O   1 
ATOM   1867  C  CB  . GLU   A 1 289  ? 140.730 143.946 170.792 1.00 57.67  ? 289  GLU   B CB  1 
ATOM   1868  C  CG  . GLU   A 1 289  ? 142.198 143.645 171.063 1.00 61.38  ? 289  GLU   B CG  1 
ATOM   1869  C  CD  . GLU   A 1 289  ? 143.080 143.855 169.847 1.00 67.02  ? 289  GLU   B CD  1 
ATOM   1870  O  OE1 . GLU   A 1 289  ? 142.756 144.727 169.013 1.00 66.38  ? 289  GLU   B OE1 1 
ATOM   1871  O  OE2 . GLU   A 1 289  ? 144.100 143.146 169.724 1.00 64.93  ? 289  GLU   B OE2 1 
ATOM   1872  N  N   . ASP   A 1 290  ? 137.655 142.782 169.687 1.00 55.95  ? 290  ASP   B N   1 
ATOM   1873  C  CA  . ASP   A 1 290  ? 136.394 142.176 170.089 1.00 53.92  ? 290  ASP   B CA  1 
ATOM   1874  C  C   . ASP   A 1 290  ? 135.937 141.191 169.023 1.00 58.94  ? 290  ASP   B C   1 
ATOM   1875  O  O   . ASP   A 1 290  ? 135.950 141.500 167.828 1.00 64.70  ? 290  ASP   B O   1 
ATOM   1876  C  CB  . ASP   A 1 290  ? 135.312 143.233 170.344 1.00 55.35  ? 290  ASP   B CB  1 
ATOM   1877  C  CG  . ASP   A 1 290  ? 134.915 143.981 169.093 1.00 58.69  ? 290  ASP   B CG  1 
ATOM   1878  O  OD1 . ASP   A 1 290  ? 135.774 144.165 168.210 1.00 53.89  ? 290  ASP   B OD1 1 
ATOM   1879  O  OD2 . ASP   A 1 290  ? 133.740 144.394 168.998 1.00 63.12  ? 290  ASP   B OD2 1 
ATOM   1880  N  N   . GLU   A 1 291  ? 135.552 139.993 169.461 1.00 55.30  ? 291  GLU   B N   1 
ATOM   1881  C  CA  . GLU   A 1 291  ? 135.221 138.917 168.543 1.00 49.95  ? 291  GLU   B CA  1 
ATOM   1882  C  C   . GLU   A 1 291  ? 133.730 138.744 168.307 1.00 47.98  ? 291  GLU   B C   1 
ATOM   1883  O  O   . GLU   A 1 291  ? 133.353 138.123 167.310 1.00 55.70  ? 291  GLU   B O   1 
ATOM   1884  C  CB  . GLU   A 1 291  ? 135.809 137.591 169.047 1.00 53.01  ? 291  GLU   B CB  1 
ATOM   1885  C  CG  . GLU   A 1 291  ? 137.325 137.609 169.179 1.00 51.39  ? 291  GLU   B CG  1 
ATOM   1886  C  CD  . GLU   A 1 291  ? 137.901 136.259 169.551 1.00 57.53  ? 291  GLU   B CD  1 
ATOM   1887  O  OE1 . GLU   A 1 291  ? 137.140 135.269 169.573 1.00 57.67  ? 291  GLU   B OE1 1 
ATOM   1888  O  OE2 . GLU   A 1 291  ? 139.118 136.186 169.820 1.00 61.12  ? 291  GLU   B OE2 1 
ATOM   1889  N  N   . HIS   A 1 292  ? 132.878 139.266 169.190 1.00 37.18  ? 292  HIS   B N   1 
ATOM   1890  C  CA  . HIS   A 1 292  ? 131.441 139.202 168.948 1.00 36.57  ? 292  HIS   B CA  1 
ATOM   1891  C  C   . HIS   A 1 292  ? 131.061 139.996 167.706 1.00 43.56  ? 292  HIS   B C   1 
ATOM   1892  O  O   . HIS   A 1 292  ? 130.238 139.549 166.898 1.00 50.64  ? 292  HIS   B O   1 
ATOM   1893  C  CB  . HIS   A 1 292  ? 130.681 139.712 170.169 1.00 33.52  ? 292  HIS   B CB  1 
ATOM   1894  C  CG  . HIS   A 1 292  ? 131.003 138.973 171.428 1.00 36.71  ? 292  HIS   B CG  1 
ATOM   1895  N  ND1 . HIS   A 1 292  ? 130.646 137.659 171.631 1.00 40.44  ? 292  HIS   B ND1 1 
ATOM   1896  C  CD2 . HIS   A 1 292  ? 131.651 139.364 172.550 1.00 43.63  ? 292  HIS   B CD2 1 
ATOM   1897  C  CE1 . HIS   A 1 292  ? 131.060 137.271 172.823 1.00 37.53  ? 292  HIS   B CE1 1 
ATOM   1898  N  NE2 . HIS   A 1 292  ? 131.670 138.288 173.402 1.00 38.90  ? 292  HIS   B NE2 1 
ATOM   1899  N  N   . PHE   A 1 293  ? 131.657 141.177 167.536 1.00 38.83  ? 293  PHE   B N   1 
ATOM   1900  C  CA  . PHE   A 1 293  ? 131.409 141.971 166.339 1.00 35.11  ? 293  PHE   B CA  1 
ATOM   1901  C  C   . PHE   A 1 293  ? 131.848 141.225 165.087 1.00 45.44  ? 293  PHE   B C   1 
ATOM   1902  O  O   . PHE   A 1 293  ? 131.130 141.207 164.080 1.00 53.07  ? 293  PHE   B O   1 
ATOM   1903  C  CB  . PHE   A 1 293  ? 132.133 143.311 166.453 1.00 41.68  ? 293  PHE   B CB  1 
ATOM   1904  C  CG  . PHE   A 1 293  ? 131.971 144.197 165.255 1.00 41.12  ? 293  PHE   B CG  1 
ATOM   1905  C  CD1 . PHE   A 1 293  ? 130.807 144.915 165.062 1.00 41.75  ? 293  PHE   B CD1 1 
ATOM   1906  C  CD2 . PHE   A 1 293  ? 132.990 144.326 164.332 1.00 43.10  ? 293  PHE   B CD2 1 
ATOM   1907  C  CE1 . PHE   A 1 293  ? 130.660 145.735 163.965 1.00 42.46  ? 293  PHE   B CE1 1 
ATOM   1908  C  CE2 . PHE   A 1 293  ? 132.846 145.144 163.234 1.00 50.02  ? 293  PHE   B CE2 1 
ATOM   1909  C  CZ  . PHE   A 1 293  ? 131.680 145.849 163.051 1.00 45.04  ? 293  PHE   B CZ  1 
ATOM   1910  N  N   . GLN   A 1 294  ? 133.022 140.593 165.136 1.00 42.88  ? 294  GLN   B N   1 
ATOM   1911  C  CA  . GLN   A 1 294  ? 133.523 139.856 163.981 1.00 33.58  ? 294  GLN   B CA  1 
ATOM   1912  C  C   . GLN   A 1 294  ? 132.634 138.664 163.658 1.00 40.41  ? 294  GLN   B C   1 
ATOM   1913  O  O   . GLN   A 1 294  ? 132.397 138.358 162.484 1.00 53.24  ? 294  GLN   B O   1 
ATOM   1914  C  CB  . GLN   A 1 294  ? 134.957 139.404 164.243 1.00 40.16  ? 294  GLN   B CB  1 
ATOM   1915  C  CG  . GLN   A 1 294  ? 135.884 140.532 164.654 1.00 38.95  ? 294  GLN   B CG  1 
ATOM   1916  C  CD  . GLN   A 1 294  ? 137.244 140.039 165.084 1.00 39.46  ? 294  GLN   B CD  1 
ATOM   1917  O  OE1 . GLN   A 1 294  ? 137.553 138.855 164.967 1.00 45.11  ? 294  GLN   B OE1 1 
ATOM   1918  N  NE2 . GLN   A 1 294  ? 138.068 140.946 165.590 1.00 44.44  ? 294  GLN   B NE2 1 
ATOM   1919  N  N   . VAL   A 1 295  ? 132.139 137.973 164.686 1.00 38.29  ? 295  VAL   B N   1 
ATOM   1920  C  CA  . VAL   A 1 295  ? 131.221 136.861 164.463 1.00 34.46  ? 295  VAL   B CA  1 
ATOM   1921  C  C   . VAL   A 1 295  ? 129.929 137.357 163.829 1.00 40.05  ? 295  VAL   B C   1 
ATOM   1922  O  O   . VAL   A 1 295  ? 129.398 136.739 162.899 1.00 47.22  ? 295  VAL   B O   1 
ATOM   1923  C  CB  . VAL   A 1 295  ? 130.956 136.115 165.784 1.00 35.05  ? 295  VAL   B CB  1 
ATOM   1924  C  CG1 . VAL   A 1 295  ? 129.788 135.165 165.631 1.00 40.35  ? 295  VAL   B CG1 1 
ATOM   1925  C  CG2 . VAL   A 1 295  ? 132.193 135.357 166.218 1.00 38.85  ? 295  VAL   B CG2 1 
ATOM   1926  N  N   . TRP   A 1 296  ? 129.406 138.484 164.316 1.00 39.31  ? 296  TRP   B N   1 
ATOM   1927  C  CA  . TRP   A 1 296  ? 128.142 138.993 163.794 1.00 35.20  ? 296  TRP   B CA  1 
ATOM   1928  C  C   . TRP   A 1 296  ? 128.277 139.469 162.353 1.00 42.69  ? 296  TRP   B C   1 
ATOM   1929  O  O   . TRP   A 1 296  ? 127.361 139.278 161.546 1.00 50.70  ? 296  TRP   B O   1 
ATOM   1930  C  CB  . TRP   A 1 296  ? 127.623 140.122 164.679 1.00 36.46  ? 296  TRP   B CB  1 
ATOM   1931  C  CG  . TRP   A 1 296  ? 126.316 140.653 164.215 1.00 37.75  ? 296  TRP   B CG  1 
ATOM   1932  C  CD1 . TRP   A 1 296  ? 126.103 141.774 163.475 1.00 44.11  ? 296  TRP   B CD1 1 
ATOM   1933  C  CD2 . TRP   A 1 296  ? 125.031 140.069 164.438 1.00 44.44  ? 296  TRP   B CD2 1 
ATOM   1934  N  NE1 . TRP   A 1 296  ? 124.763 141.931 163.230 1.00 42.66  ? 296  TRP   B NE1 1 
ATOM   1935  C  CE2 . TRP   A 1 296  ? 124.083 140.895 163.812 1.00 41.94  ? 296  TRP   B CE2 1 
ATOM   1936  C  CE3 . TRP   A 1 296  ? 124.589 138.928 165.111 1.00 49.59  ? 296  TRP   B CE3 1 
ATOM   1937  C  CZ2 . TRP   A 1 296  ? 122.723 140.618 163.837 1.00 44.35  ? 296  TRP   B CZ2 1 
ATOM   1938  C  CZ3 . TRP   A 1 296  ? 123.241 138.657 165.136 1.00 49.11  ? 296  TRP   B CZ3 1 
ATOM   1939  C  CH2 . TRP   A 1 296  ? 122.323 139.497 164.504 1.00 47.21  ? 296  TRP   B CH2 1 
ATOM   1940  N  N   . MET   A 1 297  ? 129.407 140.094 162.011 1.00 45.11  ? 297  MET   B N   1 
ATOM   1941  C  CA  . MET   A 1 297  ? 129.560 140.667 160.677 1.00 40.55  ? 297  MET   B CA  1 
ATOM   1942  C  C   . MET   A 1 297  ? 129.521 139.603 159.588 1.00 45.04  ? 297  MET   B C   1 
ATOM   1943  O  O   . MET   A 1 297  ? 129.152 139.901 158.447 1.00 52.82  ? 297  MET   B O   1 
ATOM   1944  C  CB  . MET   A 1 297  ? 130.862 141.461 160.592 1.00 44.51  ? 297  MET   B CB  1 
ATOM   1945  C  CG  . MET   A 1 297  ? 130.857 142.759 161.379 1.00 45.79  ? 297  MET   B CG  1 
ATOM   1946  S  SD  . MET   A 1 297  ? 129.793 144.023 160.667 1.00 55.65  ? 297  MET   B SD  1 
ATOM   1947  C  CE  . MET   A 1 297  ? 130.547 144.233 159.059 1.00 48.75  ? 297  MET   B CE  1 
ATOM   1948  N  N   . ARG   A 1 298  ? 129.897 138.369 159.911 1.00 44.83  ? 298  ARG   B N   1 
ATOM   1949  C  CA  . ARG   A 1 298  ? 129.822 137.273 158.951 1.00 39.81  ? 298  ARG   B CA  1 
ATOM   1950  C  C   . ARG   A 1 298  ? 128.360 136.951 158.668 1.00 43.11  ? 298  ARG   B C   1 
ATOM   1951  O  O   . ARG   A 1 298  ? 127.647 136.445 159.539 1.00 49.47  ? 298  ARG   B O   1 
ATOM   1952  C  CB  . ARG   A 1 298  ? 130.561 136.052 159.488 1.00 39.94  ? 298  ARG   B CB  1 
ATOM   1953  C  CG  . ARG   A 1 298  ? 132.067 136.140 159.352 1.00 41.27  ? 298  ARG   B CG  1 
ATOM   1954  C  CD  . ARG   A 1 298  ? 132.768 135.415 160.482 1.00 40.67  ? 298  ARG   B CD  1 
ATOM   1955  N  NE  . ARG   A 1 298  ? 132.360 134.020 160.585 1.00 51.21  ? 298  ARG   B NE  1 
ATOM   1956  C  CZ  . ARG   A 1 298  ? 132.954 133.019 159.954 1.00 52.89  ? 298  ARG   B CZ  1 
ATOM   1957  N  NH1 . ARG   A 1 298  ? 133.981 133.224 159.146 1.00 49.32  ? 298  ARG   B NH1 1 
ATOM   1958  N  NH2 . ARG   A 1 298  ? 132.507 131.780 160.137 1.00 47.05  ? 298  ARG   B NH2 1 
ATOM   1959  N  N   . VAL   A 1 299  ? 127.915 137.243 157.447 1.00 37.13  ? 299  VAL   B N   1 
ATOM   1960  C  CA  . VAL   A 1 299  ? 126.507 137.101 157.099 1.00 27.87  ? 299  VAL   B CA  1 
ATOM   1961  C  C   . VAL   A 1 299  ? 126.127 135.628 157.074 1.00 39.08  ? 299  VAL   B C   1 
ATOM   1962  O  O   . VAL   A 1 299  ? 126.824 134.798 156.476 1.00 50.06  ? 299  VAL   B O   1 
ATOM   1963  C  CB  . VAL   A 1 299  ? 126.221 137.776 155.751 1.00 37.78  ? 299  VAL   B CB  1 
ATOM   1964  C  CG1 . VAL   A 1 299  ? 124.810 137.469 155.293 1.00 43.09  ? 299  VAL   B CG1 1 
ATOM   1965  C  CG2 . VAL   A 1 299  ? 126.434 139.275 155.861 1.00 45.86  ? 299  VAL   B CG2 1 
ATOM   1966  N  N   . ALA   A 1 300  ? 125.016 135.300 157.724 1.00 35.67  ? 300  ALA   B N   1 
ATOM   1967  C  CA  . ALA   A 1 300  ? 124.528 133.933 157.776 1.00 36.69  ? 300  ALA   B CA  1 
ATOM   1968  C  C   . ALA   A 1 300  ? 123.750 133.580 156.515 1.00 44.57  ? 300  ALA   B C   1 
ATOM   1969  O  O   . ALA   A 1 300  ? 123.174 134.444 155.849 1.00 50.22  ? 300  ALA   B O   1 
ATOM   1970  C  CB  . ALA   A 1 300  ? 123.645 133.731 159.002 1.00 43.73  ? 300  ALA   B CB  1 
ATOM   1971  N  N   . ALA   A 1 301  ? 123.740 132.286 156.192 1.00 42.64  ? 301  ALA   B N   1 
ATOM   1972  C  CA  . ALA   A 1 301  ? 123.108 131.824 154.962 1.00 43.22  ? 301  ALA   B CA  1 
ATOM   1973  C  C   . ALA   A 1 301  ? 121.589 131.821 155.060 1.00 48.22  ? 301  ALA   B C   1 
ATOM   1974  O  O   . ALA   A 1 301  ? 120.904 132.212 154.109 1.00 58.14  ? 301  ALA   B O   1 
ATOM   1975  C  CB  . ALA   A 1 301  ? 123.619 130.429 154.607 1.00 45.88  ? 301  ALA   B CB  1 
ATOM   1976  N  N   . LEU   A 1 302  ? 121.045 131.393 156.190 1.00 38.64  ? 302  LEU   B N   1 
ATOM   1977  C  CA  . LEU   A 1 302  ? 119.616 131.194 156.362 1.00 39.88  ? 302  LEU   B CA  1 
ATOM   1978  C  C   . LEU   A 1 302  ? 119.079 132.093 157.468 1.00 45.89  ? 302  LEU   B C   1 
ATOM   1979  O  O   . LEU   A 1 302  ? 119.833 132.531 158.345 1.00 55.99  ? 302  LEU   B O   1 
ATOM   1980  C  CB  . LEU   A 1 302  ? 119.307 129.726 156.691 1.00 44.83  ? 302  LEU   B CB  1 
ATOM   1981  C  CG  . LEU   A 1 302  ? 119.179 128.740 155.528 1.00 47.22  ? 302  LEU   B CG  1 
ATOM   1982  C  CD1 . LEU   A 1 302  ? 120.504 128.532 154.822 1.00 46.05  ? 302  LEU   B CD1 1 
ATOM   1983  C  CD2 . LEU   A 1 302  ? 118.617 127.414 156.017 1.00 48.99  ? 302  LEU   B CD2 1 
ATOM   1984  N  N   . PRO   A 1 303  ? 117.780 132.406 157.446 1.00 34.21  ? 303  PRO   B N   1 
ATOM   1985  C  CA  . PRO   A 1 303  ? 117.209 133.219 158.531 1.00 34.46  ? 303  PRO   B CA  1 
ATOM   1986  C  C   . PRO   A 1 303  ? 117.363 132.595 159.905 1.00 39.07  ? 303  PRO   B C   1 
ATOM   1987  O  O   . PRO   A 1 303  ? 117.529 133.326 160.889 1.00 46.77  ? 303  PRO   B O   1 
ATOM   1988  C  CB  . PRO   A 1 303  ? 115.733 133.354 158.130 1.00 36.67  ? 303  PRO   B CB  1 
ATOM   1989  C  CG  . PRO   A 1 303  ? 115.497 132.277 157.130 1.00 38.65  ? 303  PRO   B CG  1 
ATOM   1990  C  CD  . PRO   A 1 303  ? 116.785 132.119 156.402 1.00 40.48  ? 303  PRO   B CD  1 
ATOM   1991  N  N   . THR   A 1 304  ? 117.311 131.270 160.008 1.00 38.57  ? 304  THR   B N   1 
ATOM   1992  C  CA  . THR   A 1 304  ? 117.572 130.577 161.265 1.00 37.91  ? 304  THR   B CA  1 
ATOM   1993  C  C   . THR   A 1 304  ? 119.051 130.220 161.306 1.00 39.88  ? 304  THR   B C   1 
ATOM   1994  O  O   . THR   A 1 304  ? 119.503 129.334 160.575 1.00 52.22  ? 304  THR   B O   1 
ATOM   1995  C  CB  . THR   A 1 304  ? 116.702 129.331 161.394 1.00 45.52  ? 304  THR   B CB  1 
ATOM   1996  O  OG1 . THR   A 1 304  ? 115.320 129.702 161.339 1.00 51.22  ? 304  THR   B OG1 1 
ATOM   1997  C  CG2 . THR   A 1 304  ? 116.977 128.631 162.710 1.00 43.48  ? 304  THR   B CG2 1 
ATOM   1998  N  N   . PHE   A 1 305  ? 119.808 130.912 162.153 1.00 31.65  ? 305  PHE   B N   1 
ATOM   1999  C  CA  . PHE   A 1 305  ? 121.249 130.732 162.200 1.00 30.08  ? 305  PHE   B CA  1 
ATOM   2000  C  C   . PHE   A 1 305  ? 121.738 130.785 163.637 1.00 34.25  ? 305  PHE   B C   1 
ATOM   2001  O  O   . PHE   A 1 305  ? 121.087 131.346 164.521 1.00 44.92  ? 305  PHE   B O   1 
ATOM   2002  C  CB  . PHE   A 1 305  ? 121.979 131.785 161.359 1.00 38.81  ? 305  PHE   B CB  1 
ATOM   2003  C  CG  . PHE   A 1 305  ? 121.725 133.201 161.792 1.00 41.50  ? 305  PHE   B CG  1 
ATOM   2004  C  CD1 . PHE   A 1 305  ? 122.541 133.813 162.727 1.00 40.32  ? 305  PHE   B CD1 1 
ATOM   2005  C  CD2 . PHE   A 1 305  ? 120.681 133.927 161.250 1.00 36.17  ? 305  PHE   B CD2 1 
ATOM   2006  C  CE1 . PHE   A 1 305  ? 122.310 135.110 163.120 1.00 39.57  ? 305  PHE   B CE1 1 
ATOM   2007  C  CE2 . PHE   A 1 305  ? 120.450 135.226 161.640 1.00 33.56  ? 305  PHE   B CE2 1 
ATOM   2008  C  CZ  . PHE   A 1 305  ? 121.266 135.817 162.576 1.00 38.05  ? 305  PHE   B CZ  1 
ATOM   2009  N  N   . ARG   A 1 306  ? 122.908 130.193 163.854 1.00 35.76  ? 306  ARG   B N   1 
ATOM   2010  C  CA  . ARG   A 1 306  ? 123.545 130.140 165.160 1.00 36.22  ? 306  ARG   B CA  1 
ATOM   2011  C  C   . ARG   A 1 306  ? 124.914 130.791 165.057 1.00 37.91  ? 306  ARG   B C   1 
ATOM   2012  O  O   . ARG   A 1 306  ? 125.667 130.509 164.121 1.00 46.79  ? 306  ARG   B O   1 
ATOM   2013  C  CB  . ARG   A 1 306  ? 123.675 128.695 165.649 1.00 35.45  ? 306  ARG   B CB  1 
ATOM   2014  C  CG  . ARG   A 1 306  ? 122.383 127.908 165.596 1.00 32.48  ? 306  ARG   B CG  1 
ATOM   2015  C  CD  . ARG   A 1 306  ? 122.557 126.627 164.807 1.00 34.06  ? 306  ARG   B CD  1 
ATOM   2016  N  NE  . ARG   A 1 306  ? 121.314 125.874 164.701 1.00 37.67  ? 306  ARG   B NE  1 
ATOM   2017  C  CZ  . ARG   A 1 306  ? 120.501 125.915 163.655 1.00 41.44  ? 306  ARG   B CZ  1 
ATOM   2018  N  NH1 . ARG   A 1 306  ? 120.769 126.666 162.601 1.00 41.68  ? 306  ARG   B NH1 1 
ATOM   2019  N  NH2 . ARG   A 1 306  ? 119.393 125.182 163.667 1.00 45.22  ? 306  ARG   B NH2 1 
ATOM   2020  N  N   . LYS   A 1 307  ? 125.230 131.662 166.009 1.00 31.00  ? 307  LYS   B N   1 
ATOM   2021  C  CA  . LYS   A 1 307  ? 126.516 132.342 166.054 1.00 31.82  ? 307  LYS   B CA  1 
ATOM   2022  C  C   . LYS   A 1 307  ? 127.188 132.079 167.393 1.00 38.04  ? 307  LYS   B C   1 
ATOM   2023  O  O   . LYS   A 1 307  ? 126.541 132.116 168.444 1.00 46.56  ? 307  LYS   B O   1 
ATOM   2024  C  CB  . LYS   A 1 307  ? 126.358 133.843 165.817 1.00 38.39  ? 307  LYS   B CB  1 
ATOM   2025  C  CG  . LYS   A 1 307  ? 125.951 134.186 164.397 1.00 44.31  ? 307  LYS   B CG  1 
ATOM   2026  C  CD  . LYS   A 1 307  ? 126.001 135.676 164.141 1.00 39.22  ? 307  LYS   B CD  1 
ATOM   2027  C  CE  . LYS   A 1 307  ? 125.755 135.982 162.679 1.00 34.88  ? 307  LYS   B CE  1 
ATOM   2028  N  NZ  . LYS   A 1 307  ? 126.750 135.313 161.803 1.00 42.69  ? 307  LYS   B NZ  1 
ATOM   2029  N  N   . LEU   A 1 308  ? 128.490 131.813 167.344 1.00 29.17  ? 308  LEU   B N   1 
ATOM   2030  C  CA  . LEU   A 1 308  ? 129.231 131.370 168.515 1.00 27.49  ? 308  LEU   B CA  1 
ATOM   2031  C  C   . LEU   A 1 308  ? 129.401 132.509 169.510 1.00 40.29  ? 308  LEU   B C   1 
ATOM   2032  O  O   . LEU   A 1 308  ? 129.755 133.631 169.134 1.00 43.85  ? 308  LEU   B O   1 
ATOM   2033  C  CB  . LEU   A 1 308  ? 130.593 130.818 168.097 1.00 33.96  ? 308  LEU   B CB  1 
ATOM   2034  C  CG  . LEU   A 1 308  ? 131.426 130.099 169.158 1.00 32.11  ? 308  LEU   B CG  1 
ATOM   2035  C  CD1 . LEU   A 1 308  ? 130.610 129.024 169.835 1.00 31.47  ? 308  LEU   B CD1 1 
ATOM   2036  C  CD2 . LEU   A 1 308  ? 132.668 129.499 168.539 1.00 32.64  ? 308  LEU   B CD2 1 
ATOM   2037  N  N   . TRP   A 1 309  ? 129.152 132.212 170.784 1.00 41.03  ? 309  TRP   B N   1 
ATOM   2038  C  CA  . TRP   A 1 309  ? 129.280 133.181 171.872 1.00 32.34  ? 309  TRP   B CA  1 
ATOM   2039  C  C   . TRP   A 1 309  ? 129.871 132.425 173.056 1.00 35.85  ? 309  TRP   B C   1 
ATOM   2040  O  O   . TRP   A 1 309  ? 129.155 131.686 173.738 1.00 50.55  ? 309  TRP   B O   1 
ATOM   2041  C  CB  . TRP   A 1 309  ? 127.932 133.801 172.222 1.00 44.16  ? 309  TRP   B CB  1 
ATOM   2042  C  CG  . TRP   A 1 309  ? 128.029 135.082 172.991 1.00 39.93  ? 309  TRP   B CG  1 
ATOM   2043  C  CD1 . TRP   A 1 309  ? 127.837 136.340 172.507 1.00 39.91  ? 309  TRP   B CD1 1 
ATOM   2044  C  CD2 . TRP   A 1 309  ? 128.341 135.230 174.379 1.00 31.38  ? 309  TRP   B CD2 1 
ATOM   2045  N  NE1 . TRP   A 1 309  ? 128.011 137.263 173.506 1.00 48.21  ? 309  TRP   B NE1 1 
ATOM   2046  C  CE2 . TRP   A 1 309  ? 128.323 136.606 174.666 1.00 36.97  ? 309  TRP   B CE2 1 
ATOM   2047  C  CE3 . TRP   A 1 309  ? 128.633 134.333 175.408 1.00 36.93  ? 309  TRP   B CE3 1 
ATOM   2048  C  CZ2 . TRP   A 1 309  ? 128.585 137.104 175.936 1.00 38.96  ? 309  TRP   B CZ2 1 
ATOM   2049  C  CZ3 . TRP   A 1 309  ? 128.899 134.830 176.664 1.00 37.73  ? 309  TRP   B CZ3 1 
ATOM   2050  C  CH2 . TRP   A 1 309  ? 128.872 136.201 176.919 1.00 40.77  ? 309  TRP   B CH2 1 
ATOM   2051  N  N   . ALA   A 1 310  ? 131.172 132.610 173.287 1.00 34.16  ? 310  ALA   B N   1 
ATOM   2052  C  CA  . ALA   A 1 310  ? 131.929 131.930 174.336 1.00 35.90  ? 310  ALA   B CA  1 
ATOM   2053  C  C   . ALA   A 1 310  ? 132.093 130.441 174.049 1.00 34.99  ? 310  ALA   B C   1 
ATOM   2054  O  O   . ALA   A 1 310  ? 131.235 129.818 173.417 1.00 41.24  ? 310  ALA   B O   1 
ATOM   2055  C  CB  . ALA   A 1 310  ? 131.290 132.138 175.712 1.00 40.10  ? 310  ALA   B CB  1 
ATOM   2056  N  N   . ARG   A 1 311  ? 133.204 129.870 174.511 1.00 44.98  ? 311  ARG   B N   1 
ATOM   2057  C  CA  . ARG   A 1 311  ? 133.540 128.480 174.250 1.00 29.85  ? 311  ARG   B CA  1 
ATOM   2058  C  C   . ARG   A 1 311  ? 134.395 127.956 175.391 1.00 41.13  ? 311  ARG   B C   1 
ATOM   2059  O  O   . ARG   A 1 311  ? 135.013 128.723 176.132 1.00 53.87  ? 311  ARG   B O   1 
ATOM   2060  C  CB  . ARG   A 1 311  ? 134.291 128.321 172.927 1.00 33.99  ? 311  ARG   B CB  1 
ATOM   2061  C  CG  . ARG   A 1 311  ? 135.610 129.068 172.890 1.00 45.14  ? 311  ARG   B CG  1 
ATOM   2062  C  CD  . ARG   A 1 311  ? 136.645 128.317 172.086 1.00 42.16  ? 311  ARG   B CD  1 
ATOM   2063  N  NE  . ARG   A 1 311  ? 136.302 128.246 170.673 1.00 35.73  ? 311  ARG   B NE  1 
ATOM   2064  C  CZ  . ARG   A 1 311  ? 136.930 127.481 169.793 1.00 36.94  ? 311  ARG   B CZ  1 
ATOM   2065  N  NH1 . ARG   A 1 311  ? 137.928 126.693 170.153 1.00 43.80  ? 311  ARG   B NH1 1 
ATOM   2066  N  NH2 . ARG   A 1 311  ? 136.544 127.504 168.522 1.00 39.89  ? 311  ARG   B NH2 1 
ATOM   2067  N  N   . ASN   A 1 312  ? 134.428 126.633 175.523 1.00 40.66  ? 312  ASN   B N   1 
ATOM   2068  C  CA  . ASN   A 1 312  ? 135.313 125.977 176.474 1.00 37.84  ? 312  ASN   B CA  1 
ATOM   2069  C  C   . ASN   A 1 312  ? 135.884 124.730 175.823 1.00 48.96  ? 312  ASN   B C   1 
ATOM   2070  O  O   . ASN   A 1 312  ? 135.155 123.985 175.161 1.00 59.14  ? 312  ASN   B O   1 
ATOM   2071  C  CB  . ASN   A 1 312  ? 134.582 125.621 177.769 1.00 37.59  ? 312  ASN   B CB  1 
ATOM   2072  C  CG  . ASN   A 1 312  ? 135.530 125.358 178.912 1.00 48.84  ? 312  ASN   B CG  1 
ATOM   2073  O  OD1 . ASN   A 1 312  ? 136.747 125.445 178.755 1.00 53.41  ? 312  ASN   B OD1 1 
ATOM   2074  N  ND2 . ASN   A 1 312  ? 134.981 125.052 180.076 1.00 52.50  ? 312  ASN   B ND2 1 
ATOM   2075  N  N   . ASP   A 1 313  ? 137.184 124.505 176.010 1.00 54.91  ? 313  ASP   B N   1 
ATOM   2076  C  CA  . ASP   A 1 313  ? 137.886 123.440 175.313 1.00 55.15  ? 313  ASP   B CA  1 
ATOM   2077  C  C   . ASP   A 1 313  ? 138.654 122.491 176.221 1.00 58.40  ? 313  ASP   B C   1 
ATOM   2078  O  O   . ASP   A 1 313  ? 139.286 121.560 175.709 1.00 64.33  ? 313  ASP   B O   1 
ATOM   2079  C  CB  . ASP   A 1 313  ? 138.863 124.032 174.285 1.00 58.75  ? 313  ASP   B CB  1 
ATOM   2080  C  CG  . ASP   A 1 313  ? 138.158 124.802 173.188 1.00 66.11  ? 313  ASP   B CG  1 
ATOM   2081  O  OD1 . ASP   A 1 313  ? 136.996 124.467 172.878 1.00 65.86  ? 313  ASP   B OD1 1 
ATOM   2082  O  OD2 . ASP   A 1 313  ? 138.766 125.741 172.633 1.00 67.78  ? 313  ASP   B OD2 1 
ATOM   2083  N  N   . GLY   A 1 314  ? 138.624 122.686 177.535 1.00 54.82  ? 314  GLY   B N   1 
ATOM   2084  C  CA  . GLY   A 1 314  ? 139.392 121.830 178.417 1.00 54.00  ? 314  GLY   B CA  1 
ATOM   2085  C  C   . GLY   A 1 314  ? 138.698 121.470 179.713 1.00 56.80  ? 314  GLY   B C   1 
ATOM   2086  O  O   . GLY   A 1 314  ? 139.360 121.156 180.707 1.00 61.81  ? 314  GLY   B O   1 
ATOM   2087  N  N   . GLU   A 1 315  ? 137.370 121.506 179.723 1.00 51.95  ? 315  GLU   B N   1 
ATOM   2088  C  CA  . GLU   A 1 315  ? 136.598 121.185 180.912 1.00 48.74  ? 315  GLU   B CA  1 
ATOM   2089  C  C   . GLU   A 1 315  ? 135.395 120.335 180.535 1.00 52.89  ? 315  GLU   B C   1 
ATOM   2090  O  O   . GLU   A 1 315  ? 134.957 120.322 179.381 1.00 60.22  ? 315  GLU   B O   1 
ATOM   2091  C  CB  . GLU   A 1 315  ? 136.130 122.448 181.641 1.00 55.22  ? 315  GLU   B CB  1 
ATOM   2092  C  CG  . GLU   A 1 315  ? 137.253 123.284 182.222 1.00 57.50  ? 315  GLU   B CG  1 
ATOM   2093  C  CD  . GLU   A 1 315  ? 136.755 124.564 182.860 1.00 62.22  ? 315  GLU   B CD  1 
ATOM   2094  O  OE1 . GLU   A 1 315  ? 135.550 124.864 182.729 1.00 61.59  ? 315  GLU   B OE1 1 
ATOM   2095  O  OE2 . GLU   A 1 315  ? 137.567 125.270 183.492 1.00 62.78  ? 315  GLU   B OE2 1 
ATOM   2096  N  N   . ILE   A 1 316  ? 134.863 119.629 181.527 1.00 46.10  ? 316  ILE   B N   1 
ATOM   2097  C  CA  . ILE   A 1 316  ? 133.735 118.724 181.351 1.00 47.94  ? 316  ILE   B CA  1 
ATOM   2098  C  C   . ILE   A 1 316  ? 132.561 119.259 182.155 1.00 45.27  ? 316  ILE   B C   1 
ATOM   2099  O  O   . ILE   A 1 316  ? 132.700 119.540 183.351 1.00 50.45  ? 316  ILE   B O   1 
ATOM   2100  C  CB  . ILE   A 1 316  ? 134.089 117.293 181.793 1.00 48.61  ? 316  ILE   B CB  1 
ATOM   2101  C  CG1 . ILE   A 1 316  ? 135.278 116.762 180.994 1.00 48.54  ? 316  ILE   B CG1 1 
ATOM   2102  C  CG2 . ILE   A 1 316  ? 132.888 116.374 181.641 1.00 49.90  ? 316  ILE   B CG2 1 
ATOM   2103  C  CD1 . ILE   A 1 316  ? 135.658 115.345 181.343 1.00 48.80  ? 316  ILE   B CD1 1 
ATOM   2104  N  N   . MET   A 1 317  ? 131.409 119.400 181.505 1.00 46.79  ? 317  MET   B N   1 
ATOM   2105  C  CA  . MET   A 1 317  ? 130.186 119.776 182.209 1.00 49.99  ? 317  MET   B CA  1 
ATOM   2106  C  C   . MET   A 1 317  ? 129.640 118.532 182.892 1.00 48.51  ? 317  MET   B C   1 
ATOM   2107  O  O   . MET   A 1 317  ? 129.021 117.677 182.256 1.00 57.68  ? 317  MET   B O   1 
ATOM   2108  C  CB  . MET   A 1 317  ? 129.159 120.383 181.261 1.00 52.32  ? 317  MET   B CB  1 
ATOM   2109  C  CG  . MET   A 1 317  ? 129.240 121.898 181.150 1.00 53.16  ? 317  MET   B CG  1 
ATOM   2110  S  SD  . MET   A 1 317  ? 127.673 122.682 180.720 1.00 58.20  ? 317  MET   B SD  1 
ATOM   2111  C  CE  . MET   A 1 317  ? 127.276 121.851 179.190 1.00 54.48  ? 317  MET   B CE  1 
ATOM   2112  N  N   . SER   A 1 318  ? 129.872 118.431 184.195 1.00 36.70  ? 318  SER   B N   1 
ATOM   2113  C  CA  . SER   A 1 318  ? 129.416 117.278 184.947 1.00 41.78  ? 318  SER   B CA  1 
ATOM   2114  C  C   . SER   A 1 318  ? 127.894 117.261 185.029 1.00 41.06  ? 318  SER   B C   1 
ATOM   2115  O  O   . SER   A 1 318  ? 127.219 118.270 184.818 1.00 52.76  ? 318  SER   B O   1 
ATOM   2116  C  CB  . SER   A 1 318  ? 130.023 117.283 186.348 1.00 51.18  ? 318  SER   B CB  1 
ATOM   2117  O  OG  . SER   A 1 318  ? 129.765 118.509 187.008 1.00 53.80  ? 318  SER   B OG  1 
ATOM   2118  N  N   . GLN   A 1 319  ? 127.356 116.082 185.323 1.00 50.19  ? 319  GLN   B N   1 
ATOM   2119  C  CA  . GLN   A 1 319  ? 125.916 115.934 185.467 1.00 52.87  ? 319  GLN   B CA  1 
ATOM   2120  C  C   . GLN   A 1 319  ? 125.417 116.775 186.633 1.00 58.94  ? 319  GLN   B C   1 
ATOM   2121  O  O   . GLN   A 1 319  ? 126.014 116.779 187.713 1.00 63.77  ? 319  GLN   B O   1 
ATOM   2122  C  CB  . GLN   A 1 319  ? 125.560 114.464 185.679 1.00 52.30  ? 319  GLN   B CB  1 
ATOM   2123  C  CG  . GLN   A 1 319  ? 124.082 114.203 185.888 1.00 52.35  ? 319  GLN   B CG  1 
ATOM   2124  C  CD  . GLN   A 1 319  ? 123.784 112.741 186.142 1.00 58.74  ? 319  GLN   B CD  1 
ATOM   2125  O  OE1 . GLN   A 1 319  ? 124.695 111.922 186.258 1.00 60.96  ? 319  GLN   B OE1 1 
ATOM   2126  N  NE2 . GLN   A 1 319  ? 122.503 112.404 186.228 1.00 63.00  ? 319  GLN   B NE2 1 
ATOM   2127  N  N   . GLY   A 1 320  ? 124.324 117.492 186.410 1.00 60.34  ? 320  GLY   B N   1 
ATOM   2128  C  CA  . GLY   A 1 320  ? 123.756 118.329 187.448 1.00 58.87  ? 320  GLY   B CA  1 
ATOM   2129  C  C   . GLY   A 1 320  ? 122.829 119.363 186.839 1.00 58.32  ? 320  GLY   B C   1 
ATOM   2130  O  O   . GLY   A 1 320  ? 122.399 119.232 185.696 1.00 61.88  ? 320  GLY   B O   1 
ATOM   2131  N  N   . ARG   A 1 321  ? 122.537 120.388 187.631 1.00 50.63  ? 321  ARG   B N   1 
ATOM   2132  C  CA  . ARG   A 1 321  ? 121.682 121.488 187.211 1.00 42.35  ? 321  ARG   B CA  1 
ATOM   2133  C  C   . ARG   A 1 321  ? 122.513 122.757 187.102 1.00 47.86  ? 321  ARG   B C   1 
ATOM   2134  O  O   . ARG   A 1 321  ? 123.203 123.136 188.054 1.00 56.12  ? 321  ARG   B O   1 
ATOM   2135  C  CB  . ARG   A 1 321  ? 120.523 121.685 188.189 1.00 46.59  ? 321  ARG   B CB  1 
ATOM   2136  C  CG  . ARG   A 1 321  ? 119.609 122.842 187.840 1.00 52.58  ? 321  ARG   B CG  1 
ATOM   2137  C  CD  . ARG   A 1 321  ? 118.314 122.783 188.630 1.00 52.72  ? 321  ARG   B CD  1 
ATOM   2138  N  NE  . ARG   A 1 321  ? 117.400 121.773 188.109 1.00 52.18  ? 321  ARG   B NE  1 
ATOM   2139  C  CZ  . ARG   A 1 321  ? 116.456 122.012 187.209 1.00 54.63  ? 321  ARG   B CZ  1 
ATOM   2140  N  NH1 . ARG   A 1 321  ? 116.273 123.219 186.703 1.00 57.31  ? 321  ARG   B NH1 1 
ATOM   2141  N  NH2 . ARG   A 1 321  ? 115.676 121.013 186.807 1.00 53.66  ? 321  ARG   B NH2 1 
ATOM   2142  N  N   . TYR   A 1 322  ? 122.447 123.404 185.945 1.00 44.05  ? 322  TYR   B N   1 
ATOM   2143  C  CA  . TYR   A 1 322  ? 123.221 124.601 185.658 1.00 36.57  ? 322  TYR   B CA  1 
ATOM   2144  C  C   . TYR   A 1 322  ? 122.292 125.796 185.514 1.00 48.64  ? 322  TYR   B C   1 
ATOM   2145  O  O   . TYR   A 1 322  ? 121.210 125.684 184.932 1.00 60.73  ? 322  TYR   B O   1 
ATOM   2146  C  CB  . TYR   A 1 322  ? 124.039 124.431 184.378 1.00 47.21  ? 322  TYR   B CB  1 
ATOM   2147  C  CG  . TYR   A 1 322  ? 125.174 123.441 184.483 1.00 51.67  ? 322  TYR   B CG  1 
ATOM   2148  C  CD1 . TYR   A 1 322  ? 124.938 122.078 184.420 1.00 51.15  ? 322  TYR   B CD1 1 
ATOM   2149  C  CD2 . TYR   A 1 322  ? 126.483 123.872 184.628 1.00 49.09  ? 322  TYR   B CD2 1 
ATOM   2150  C  CE1 . TYR   A 1 322  ? 125.969 121.175 184.510 1.00 46.97  ? 322  TYR   B CE1 1 
ATOM   2151  C  CE2 . TYR   A 1 322  ? 127.521 122.975 184.715 1.00 45.58  ? 322  TYR   B CE2 1 
ATOM   2152  C  CZ  . TYR   A 1 322  ? 127.258 121.628 184.656 1.00 46.28  ? 322  TYR   B CZ  1 
ATOM   2153  O  OH  . TYR   A 1 322  ? 128.291 120.726 184.746 1.00 62.19  ? 322  TYR   B OH  1 
ATOM   2154  N  N   . ARG   A 1 323  ? 122.720 126.940 186.039 1.00 50.15  ? 323  ARG   B N   1 
ATOM   2155  C  CA  . ARG   A 1 323  ? 121.975 128.188 185.929 1.00 43.46  ? 323  ARG   B CA  1 
ATOM   2156  C  C   . ARG   A 1 323  ? 122.720 129.121 184.987 1.00 48.29  ? 323  ARG   B C   1 
ATOM   2157  O  O   . ARG   A 1 323  ? 123.895 129.426 185.213 1.00 61.18  ? 323  ARG   B O   1 
ATOM   2158  C  CB  . ARG   A 1 323  ? 121.790 128.839 187.298 1.00 46.74  ? 323  ARG   B CB  1 
ATOM   2159  C  CG  . ARG   A 1 323  ? 121.371 130.294 187.239 1.00 53.78  ? 323  ARG   B CG  1 
ATOM   2160  C  CD  . ARG   A 1 323  ? 120.222 130.573 188.187 1.00 52.93  ? 323  ARG   B CD  1 
ATOM   2161  N  NE  . ARG   A 1 323  ? 120.455 130.005 189.508 1.00 57.43  ? 323  ARG   B NE  1 
ATOM   2162  C  CZ  . ARG   A 1 323  ? 121.120 130.614 190.479 1.00 56.44  ? 323  ARG   B CZ  1 
ATOM   2163  N  NH1 . ARG   A 1 323  ? 121.646 131.816 190.307 1.00 52.70  ? 323  ARG   B NH1 1 
ATOM   2164  N  NH2 . ARG   A 1 323  ? 121.260 130.004 191.652 1.00 53.32  ? 323  ARG   B NH2 1 
ATOM   2165  N  N   . ILE   A 1 324  ? 122.039 129.572 183.938 1.00 39.36  ? 324  ILE   B N   1 
ATOM   2166  C  CA  . ILE   A 1 324  ? 122.620 130.455 182.935 1.00 36.18  ? 324  ILE   B CA  1 
ATOM   2167  C  C   . ILE   A 1 324  ? 121.844 131.764 182.935 1.00 45.51  ? 324  ILE   B C   1 
ATOM   2168  O  O   . ILE   A 1 324  ? 120.606 131.763 182.925 1.00 51.74  ? 324  ILE   B O   1 
ATOM   2169  C  CB  . ILE   A 1 324  ? 122.628 129.801 181.541 1.00 32.64  ? 324  ILE   B CB  1 
ATOM   2170  C  CG1 . ILE   A 1 324  ? 123.213 130.755 180.502 1.00 39.56  ? 324  ILE   B CG1 1 
ATOM   2171  C  CG2 . ILE   A 1 324  ? 121.237 129.336 181.141 1.00 42.60  ? 324  ILE   B CG2 1 
ATOM   2172  C  CD1 . ILE   A 1 324  ? 123.367 130.137 179.141 1.00 45.13  ? 324  ILE   B CD1 1 
ATOM   2173  N  N   . VAL   A 1 325  ? 122.569 132.876 182.970 1.00 52.78  ? 325  VAL   B N   1 
ATOM   2174  C  CA  . VAL   A 1 325  ? 121.980 134.208 183.021 1.00 43.88  ? 325  VAL   B CA  1 
ATOM   2175  C  C   . VAL   A 1 325  ? 122.104 134.839 181.643 1.00 46.40  ? 325  VAL   B C   1 
ATOM   2176  O  O   . VAL   A 1 325  ? 123.196 134.879 181.066 1.00 56.10  ? 325  VAL   B O   1 
ATOM   2177  C  CB  . VAL   A 1 325  ? 122.659 135.079 184.088 1.00 41.12  ? 325  VAL   B CB  1 
ATOM   2178  C  CG1 . VAL   A 1 325  ? 122.048 136.466 184.105 1.00 45.33  ? 325  VAL   B CG1 1 
ATOM   2179  C  CG2 . VAL   A 1 325  ? 122.544 134.427 185.451 1.00 46.46  ? 325  VAL   B CG2 1 
ATOM   2180  N  N   . ALA   A 1 326  ? 120.989 135.332 181.114 1.00 48.48  ? 326  ALA   B N   1 
ATOM   2181  C  CA  . ALA   A 1 326  ? 120.960 136.018 179.831 1.00 46.71  ? 326  ALA   B CA  1 
ATOM   2182  C  C   . ALA   A 1 326  ? 120.498 137.451 180.046 1.00 52.60  ? 326  ALA   B C   1 
ATOM   2183  O  O   . ALA   A 1 326  ? 119.456 137.683 180.667 1.00 55.75  ? 326  ALA   B O   1 
ATOM   2184  C  CB  . ALA   A 1 326  ? 120.039 135.303 178.841 1.00 47.34  ? 326  ALA   B CB  1 
ATOM   2185  N  N   . ASN   A 1 327  ? 121.271 138.404 179.533 1.00 44.81  ? 327  ASN   B N   1 
ATOM   2186  C  CA  . ASN   A 1 327  ? 120.960 139.826 179.653 1.00 37.22  ? 327  ASN   B CA  1 
ATOM   2187  C  C   . ASN   A 1 327  ? 120.155 140.237 178.427 1.00 47.30  ? 327  ASN   B C   1 
ATOM   2188  O  O   . ASN   A 1 327  ? 120.719 140.591 177.390 1.00 55.34  ? 327  ASN   B O   1 
ATOM   2189  C  CB  . ASN   A 1 327  ? 122.236 140.647 179.791 1.00 43.00  ? 327  ASN   B CB  1 
ATOM   2190  C  CG  . ASN   A 1 327  ? 123.017 140.300 181.037 1.00 46.40  ? 327  ASN   B CG  1 
ATOM   2191  O  OD1 . ASN   A 1 327  ? 122.446 139.886 182.042 1.00 53.59  ? 327  ASN   B OD1 1 
ATOM   2192  N  ND2 . ASN   A 1 327  ? 124.330 140.468 180.978 1.00 51.93  ? 327  ASN   B ND2 1 
ATOM   2193  N  N   . MET   A 1 328  ? 118.831 140.208 178.556 1.00 52.19  ? 328  MET   B N   1 
ATOM   2194  C  CA  . MET   A 1 328  ? 117.941 140.445 177.425 1.00 48.45  ? 328  MET   B CA  1 
ATOM   2195  C  C   . MET   A 1 328  ? 117.998 141.910 177.013 1.00 52.98  ? 328  MET   B C   1 
ATOM   2196  O  O   . MET   A 1 328  ? 117.433 142.776 177.688 1.00 56.22  ? 328  MET   B O   1 
ATOM   2197  C  CB  . MET   A 1 328  ? 116.518 140.034 177.787 1.00 49.03  ? 328  MET   B CB  1 
ATOM   2198  C  CG  . MET   A 1 328  ? 116.387 138.585 178.208 1.00 54.66  ? 328  MET   B CG  1 
ATOM   2199  S  SD  . MET   A 1 328  ? 114.674 138.052 178.283 1.00 68.23  ? 328  MET   B SD  1 
ATOM   2200  C  CE  . MET   A 1 328  ? 114.190 138.274 176.575 1.00 55.44  ? 328  MET   B CE  1 
ATOM   2201  N  N   . ASN   A 1 329  ? 118.672 142.187 175.895 1.00 49.51  ? 329  ASN   B N   1 
ATOM   2202  C  CA  . ASN   A 1 329  ? 118.802 143.539 175.377 1.00 37.58  ? 329  ASN   B CA  1 
ATOM   2203  C  C   . ASN   A 1 329  ? 118.480 143.656 173.894 1.00 41.28  ? 329  ASN   B C   1 
ATOM   2204  O  O   . ASN   A 1 329  ? 118.378 144.779 173.390 1.00 51.90  ? 329  ASN   B O   1 
ATOM   2205  C  CB  . ASN   A 1 329  ? 120.222 144.072 175.613 1.00 41.72  ? 329  ASN   B CB  1 
ATOM   2206  C  CG  . ASN   A 1 329  ? 120.612 144.072 177.072 1.00 49.10  ? 329  ASN   B CG  1 
ATOM   2207  O  OD1 . ASN   A 1 329  ? 119.787 144.323 177.948 1.00 51.93  ? 329  ASN   B OD1 1 
ATOM   2208  N  ND2 . ASN   A 1 329  ? 121.879 143.791 177.344 1.00 50.58  ? 329  ASN   B ND2 1 
ATOM   2209  N  N   . TYR   A 1 330  ? 118.316 142.544 173.183 1.00 41.95  ? 330  TYR   B N   1 
ATOM   2210  C  CA  . TYR   A 1 330  ? 118.131 142.553 171.732 1.00 42.90  ? 330  TYR   B CA  1 
ATOM   2211  C  C   . TYR   A 1 330  ? 116.726 142.077 171.402 1.00 51.62  ? 330  TYR   B C   1 
ATOM   2212  O  O   . TYR   A 1 330  ? 116.480 140.860 171.331 1.00 56.20  ? 330  TYR   B O   1 
ATOM   2213  C  CB  . TYR   A 1 330  ? 119.172 141.664 171.057 1.00 41.70  ? 330  TYR   B CB  1 
ATOM   2214  C  CG  . TYR   A 1 330  ? 119.378 141.933 169.587 1.00 40.23  ? 330  TYR   B CG  1 
ATOM   2215  C  CD1 . TYR   A 1 330  ? 120.160 142.994 169.163 1.00 42.77  ? 330  TYR   B CD1 1 
ATOM   2216  C  CD2 . TYR   A 1 330  ? 118.813 141.112 168.624 1.00 43.51  ? 330  TYR   B CD2 1 
ATOM   2217  C  CE1 . TYR   A 1 330  ? 120.361 143.240 167.823 1.00 45.60  ? 330  TYR   B CE1 1 
ATOM   2218  C  CE2 . TYR   A 1 330  ? 119.010 141.349 167.281 1.00 44.34  ? 330  TYR   B CE2 1 
ATOM   2219  C  CZ  . TYR   A 1 330  ? 119.785 142.414 166.886 1.00 47.96  ? 330  TYR   B CZ  1 
ATOM   2220  O  OH  . TYR   A 1 330  ? 119.983 142.654 165.547 1.00 50.34  ? 330  TYR   B OH  1 
ATOM   2221  N  N   . PRO   A 1 331  ? 115.772 142.984 171.193 1.00 38.00  ? 331  PRO   B N   1 
ATOM   2222  C  CA  . PRO   A 1 331  ? 114.395 142.556 170.921 1.00 34.64  ? 331  PRO   B CA  1 
ATOM   2223  C  C   . PRO   A 1 331  ? 114.270 141.938 169.536 1.00 36.96  ? 331  PRO   B C   1 
ATOM   2224  O  O   . PRO   A 1 331  ? 114.792 142.468 168.553 1.00 43.82  ? 331  PRO   B O   1 
ATOM   2225  C  CB  . PRO   A 1 331  ? 113.591 143.855 171.037 1.00 34.44  ? 331  PRO   B CB  1 
ATOM   2226  C  CG  . PRO   A 1 331  ? 114.578 144.924 170.744 1.00 36.69  ? 331  PRO   B CG  1 
ATOM   2227  C  CD  . PRO   A 1 331  ? 115.888 144.448 171.284 1.00 37.13  ? 331  PRO   B CD  1 
ATOM   2228  N  N   . VAL   A 1 332  ? 113.568 140.808 169.469 1.00 35.00  ? 332  VAL   B N   1 
ATOM   2229  C  CA  . VAL   A 1 332  ? 113.354 140.096 168.215 1.00 35.77  ? 332  VAL   B CA  1 
ATOM   2230  C  C   . VAL   A 1 332  ? 111.874 139.774 168.064 1.00 40.11  ? 332  VAL   B C   1 
ATOM   2231  O  O   . VAL   A 1 332  ? 111.438 139.289 167.014 1.00 49.34  ? 332  VAL   B O   1 
ATOM   2232  C  CB  . VAL   A 1 332  ? 114.207 138.817 168.147 1.00 32.55  ? 332  VAL   B CB  1 
ATOM   2233  C  CG1 . VAL   A 1 332  ? 115.674 139.166 168.010 1.00 40.79  ? 332  VAL   B CG1 1 
ATOM   2234  C  CG2 . VAL   A 1 332  ? 113.980 137.968 169.383 1.00 42.39  ? 332  VAL   B CG2 1 
ATOM   2235  N  N   . LYS   A 1 333  ? 111.092 140.039 169.112 1.00 39.14  ? 333  LYS   B N   1 
ATOM   2236  C  CA  . LYS   A 1 333  ? 109.664 139.748 169.073 1.00 36.71  ? 333  LYS   B CA  1 
ATOM   2237  C  C   . LYS   A 1 333  ? 108.911 140.631 168.091 1.00 53.27  ? 333  LYS   B C   1 
ATOM   2238  O  O   . LYS   A 1 333  ? 107.819 140.254 167.653 1.00 57.19  ? 333  LYS   B O   1 
ATOM   2239  C  CB  . LYS   A 1 333  ? 109.048 139.908 170.462 1.00 39.65  ? 333  LYS   B CB  1 
ATOM   2240  C  CG  . LYS   A 1 333  ? 109.454 138.848 171.459 1.00 49.97  ? 333  LYS   B CG  1 
ATOM   2241  C  CD  . LYS   A 1 333  ? 108.617 138.942 172.721 1.00 48.82  ? 333  LYS   B CD  1 
ATOM   2242  C  CE  . LYS   A 1 333  ? 108.759 140.299 173.375 1.00 49.11  ? 333  LYS   B CE  1 
ATOM   2243  N  NZ  . LYS   A 1 333  ? 107.922 140.411 174.599 1.00 52.94  ? 333  LYS   B NZ  1 
ATOM   2244  N  N   . GLN   A 1 334  ? 109.459 141.796 167.742 1.00 53.24  ? 334  GLN   B N   1 
ATOM   2245  C  CA  . GLN   A 1 334  ? 108.734 142.729 166.887 1.00 44.44  ? 334  GLN   B CA  1 
ATOM   2246  C  C   . GLN   A 1 334  ? 108.486 142.143 165.503 1.00 52.03  ? 334  GLN   B C   1 
ATOM   2247  O  O   . GLN   A 1 334  ? 107.399 142.311 164.938 1.00 58.65  ? 334  GLN   B O   1 
ATOM   2248  C  CB  . GLN   A 1 334  ? 109.499 144.048 166.793 1.00 48.61  ? 334  GLN   B CB  1 
ATOM   2249  C  CG  . GLN   A 1 334  ? 110.983 143.885 166.543 1.00 51.17  ? 334  GLN   B CG  1 
ATOM   2250  C  CD  . GLN   A 1 334  ? 111.725 145.200 166.554 1.00 58.35  ? 334  GLN   B CD  1 
ATOM   2251  O  OE1 . GLN   A 1 334  ? 111.217 146.208 167.042 1.00 61.40  ? 334  GLN   B OE1 1 
ATOM   2252  N  NE2 . GLN   A 1 334  ? 112.937 145.200 166.010 1.00 57.38  ? 334  GLN   B NE2 1 
ATOM   2253  N  N   . PHE   A 1 335  ? 109.475 141.447 164.942 1.00 44.57  ? 335  PHE   B N   1 
ATOM   2254  C  CA  . PHE   A 1 335  ? 109.357 140.855 163.615 1.00 42.22  ? 335  PHE   B CA  1 
ATOM   2255  C  C   . PHE   A 1 335  ? 109.162 139.344 163.665 1.00 50.20  ? 335  PHE   B C   1 
ATOM   2256  O  O   . PHE   A 1 335  ? 109.646 138.627 162.783 1.00 59.10  ? 335  PHE   B O   1 
ATOM   2257  C  CB  . PHE   A 1 335  ? 110.573 141.209 162.759 1.00 47.53  ? 335  PHE   B CB  1 
ATOM   2258  C  CG  . PHE   A 1 335  ? 111.890 140.869 163.390 1.00 40.80  ? 335  PHE   B CG  1 
ATOM   2259  C  CD1 . PHE   A 1 335  ? 112.520 141.765 164.230 1.00 44.85  ? 335  PHE   B CD1 1 
ATOM   2260  C  CD2 . PHE   A 1 335  ? 112.512 139.666 163.122 1.00 43.53  ? 335  PHE   B CD2 1 
ATOM   2261  C  CE1 . PHE   A 1 335  ? 113.730 141.461 164.804 1.00 48.13  ? 335  PHE   B CE1 1 
ATOM   2262  C  CE2 . PHE   A 1 335  ? 113.724 139.357 163.695 1.00 50.25  ? 335  PHE   B CE2 1 
ATOM   2263  C  CZ  . PHE   A 1 335  ? 114.334 140.256 164.536 1.00 51.84  ? 335  PHE   B CZ  1 
ATOM   2264  N  N   . SER   A 1 336  ? 108.445 138.851 164.677 1.00 48.02  ? 336  SER   B N   1 
ATOM   2265  C  CA  . SER   A 1 336  ? 108.132 137.428 164.816 1.00 44.59  ? 336  SER   B CA  1 
ATOM   2266  C  C   . SER   A 1 336  ? 109.398 136.576 164.844 1.00 50.24  ? 336  SER   B C   1 
ATOM   2267  O  O   . SER   A 1 336  ? 109.456 135.496 164.253 1.00 59.20  ? 336  SER   B O   1 
ATOM   2268  C  CB  . SER   A 1 336  ? 107.186 136.960 163.708 1.00 51.52  ? 336  SER   B CB  1 
ATOM   2269  O  OG  . SER   A 1 336  ? 105.971 137.690 163.731 1.00 55.84  ? 336  SER   B OG  1 
ATOM   2270  N  N   . GLY   A 1 337  ? 110.421 137.066 165.534 1.00 42.89  ? 337  GLY   B N   1 
ATOM   2271  C  CA  . GLY   A 1 337  ? 111.665 136.336 165.659 1.00 34.32  ? 337  GLY   B CA  1 
ATOM   2272  C  C   . GLY   A 1 337  ? 111.905 135.843 167.069 1.00 41.75  ? 337  GLY   B C   1 
ATOM   2273  O  O   . GLY   A 1 337  ? 111.363 136.401 168.026 1.00 53.62  ? 337  GLY   B O   1 
ATOM   2274  N  N   . THR   A 1 338  ? 112.710 134.794 167.212 1.00 41.91  ? 338  THR   B N   1 
ATOM   2275  C  CA  . THR   A 1 338  ? 113.025 134.225 168.513 1.00 41.87  ? 338  THR   B CA  1 
ATOM   2276  C  C   . THR   A 1 338  ? 114.532 134.103 168.669 1.00 43.17  ? 338  THR   B C   1 
ATOM   2277  O  O   . THR   A 1 338  ? 115.247 133.839 167.698 1.00 49.56  ? 338  THR   B O   1 
ATOM   2278  C  CB  . THR   A 1 338  ? 112.379 132.848 168.704 1.00 42.37  ? 338  THR   B CB  1 
ATOM   2279  O  OG1 . THR   A 1 338  ? 112.829 131.961 167.675 1.00 50.32  ? 338  THR   B OG1 1 
ATOM   2280  C  CG2 . THR   A 1 338  ? 110.861 132.953 168.650 1.00 45.25  ? 338  THR   B CG2 1 
ATOM   2281  N  N   . LYS   A 1 339  ? 115.008 134.302 169.894 1.00 40.56  ? 339  LYS   B N   1 
ATOM   2282  C  CA  . LYS   A 1 339  ? 116.413 134.146 170.236 1.00 34.23  ? 339  LYS   B CA  1 
ATOM   2283  C  C   . LYS   A 1 339  ? 116.553 133.016 171.244 1.00 44.95  ? 339  LYS   B C   1 
ATOM   2284  O  O   . LYS   A 1 339  ? 115.793 132.948 172.215 1.00 58.34  ? 339  LYS   B O   1 
ATOM   2285  C  CB  . LYS   A 1 339  ? 116.999 135.445 170.792 1.00 40.96  ? 339  LYS   B CB  1 
ATOM   2286  C  CG  . LYS   A 1 339  ? 116.130 136.158 171.808 1.00 44.92  ? 339  LYS   B CG  1 
ATOM   2287  C  CD  . LYS   A 1 339  ? 116.772 137.469 172.225 1.00 46.41  ? 339  LYS   B CD  1 
ATOM   2288  C  CE  . LYS   A 1 339  ? 115.920 138.215 173.227 1.00 44.23  ? 339  LYS   B CE  1 
ATOM   2289  N  NZ  . LYS   A 1 339  ? 116.575 139.468 173.678 1.00 45.50  ? 339  LYS   B NZ  1 
ATOM   2290  N  N   . SER   A 1 340  ? 117.517 132.130 171.008 1.00 42.82  ? 340  SER   B N   1 
ATOM   2291  C  CA  . SER   A 1 340  ? 117.681 130.927 171.806 1.00 38.10  ? 340  SER   B CA  1 
ATOM   2292  C  C   . SER   A 1 340  ? 119.128 130.790 172.257 1.00 46.64  ? 340  SER   B C   1 
ATOM   2293  O  O   . SER   A 1 340  ? 120.025 131.479 171.769 1.00 53.76  ? 340  SER   B O   1 
ATOM   2294  C  CB  . SER   A 1 340  ? 117.260 129.677 171.025 1.00 44.52  ? 340  SER   B CB  1 
ATOM   2295  O  OG  . SER   A 1 340  ? 115.916 129.774 170.589 1.00 51.40  ? 340  SER   B OG  1 
ATOM   2296  N  N   . ILE   A 1 341  ? 119.337 129.887 173.211 1.00 48.24  ? 341  ILE   B N   1 
ATOM   2297  C  CA  . ILE   A 1 341  ? 120.659 129.538 173.717 1.00 36.66  ? 341  ILE   B CA  1 
ATOM   2298  C  C   . ILE   A 1 341  ? 120.928 128.091 173.335 1.00 44.71  ? 341  ILE   B C   1 
ATOM   2299  O  O   . ILE   A 1 341  ? 120.144 127.198 173.677 1.00 50.46  ? 341  ILE   B O   1 
ATOM   2300  C  CB  . ILE   A 1 341  ? 120.753 129.722 175.239 1.00 36.33  ? 341  ILE   B CB  1 
ATOM   2301  C  CG1 . ILE   A 1 341  ? 120.465 131.168 175.633 1.00 43.26  ? 341  ILE   B CG1 1 
ATOM   2302  C  CG2 . ILE   A 1 341  ? 122.113 129.303 175.738 1.00 41.85  ? 341  ILE   B CG2 1 
ATOM   2303  C  CD1 . ILE   A 1 341  ? 120.468 131.394 177.125 1.00 42.70  ? 341  ILE   B CD1 1 
ATOM   2304  N  N   . VAL   A 1 342  ? 122.031 127.854 172.633 1.00 44.38  ? 342  VAL   B N   1 
ATOM   2305  C  CA  . VAL   A 1 342  ? 122.394 126.521 172.165 1.00 37.85  ? 342  VAL   B CA  1 
ATOM   2306  C  C   . VAL   A 1 342  ? 123.731 126.140 172.783 1.00 45.30  ? 342  VAL   B C   1 
ATOM   2307  O  O   . VAL   A 1 342  ? 124.731 126.844 172.603 1.00 49.84  ? 342  VAL   B O   1 
ATOM   2308  C  CB  . VAL   A 1 342  ? 122.456 126.454 170.633 1.00 38.08  ? 342  VAL   B CB  1 
ATOM   2309  C  CG1 . VAL   A 1 342  ? 122.781 125.046 170.181 1.00 47.51  ? 342  VAL   B CG1 1 
ATOM   2310  C  CG2 . VAL   A 1 342  ? 121.143 126.914 170.031 1.00 42.58  ? 342  VAL   B CG2 1 
ATOM   2311  N  N   . ILE   A 1 343  ? 123.746 125.025 173.507 1.00 45.92  ? 343  ILE   B N   1 
ATOM   2312  C  CA  . ILE   A 1 343  ? 124.962 124.452 174.072 1.00 39.49  ? 343  ILE   B CA  1 
ATOM   2313  C  C   . ILE   A 1 343  ? 125.175 123.102 173.409 1.00 41.43  ? 343  ILE   B C   1 
ATOM   2314  O  O   . ILE   A 1 343  ? 124.326 122.209 173.520 1.00 47.87  ? 343  ILE   B O   1 
ATOM   2315  C  CB  . ILE   A 1 343  ? 124.870 124.310 175.598 1.00 37.41  ? 343  ILE   B CB  1 
ATOM   2316  C  CG1 . ILE   A 1 343  ? 124.427 125.629 176.226 1.00 39.41  ? 343  ILE   B CG1 1 
ATOM   2317  C  CG2 . ILE   A 1 343  ? 126.203 123.870 176.171 1.00 46.43  ? 343  ILE   B CG2 1 
ATOM   2318  C  CD1 . ILE   A 1 343  ? 124.396 125.607 177.724 1.00 39.52  ? 343  ILE   B CD1 1 
ATOM   2319  N  N   . SER   A 1 344  ? 126.304 122.945 172.726 1.00 38.89  ? 344  SER   B N   1 
ATOM   2320  C  CA  . SER   A 1 344  ? 126.545 121.755 171.929 1.00 34.38  ? 344  SER   B CA  1 
ATOM   2321  C  C   . SER   A 1 344  ? 128.008 121.355 172.006 1.00 35.78  ? 344  SER   B C   1 
ATOM   2322  O  O   . SER   A 1 344  ? 128.888 122.186 172.243 1.00 46.92  ? 344  SER   B O   1 
ATOM   2323  C  CB  . SER   A 1 344  ? 126.145 121.974 170.465 1.00 46.44  ? 344  SER   B CB  1 
ATOM   2324  O  OG  . SER   A 1 344  ? 126.388 120.815 169.689 1.00 48.12  ? 344  SER   B OG  1 
ATOM   2325  N  N   . THR   A 1 345  ? 128.254 120.065 171.802 1.00 33.34  ? 345  THR   B N   1 
ATOM   2326  C  CA  . THR   A 1 345  ? 129.592 119.528 171.645 1.00 29.65  ? 345  THR   B CA  1 
ATOM   2327  C  C   . THR   A 1 345  ? 129.920 119.434 170.158 1.00 40.23  ? 345  THR   B C   1 
ATOM   2328  O  O   . THR   A 1 345  ? 129.150 119.863 169.297 1.00 48.99  ? 345  THR   B O   1 
ATOM   2329  C  CB  . THR   A 1 345  ? 129.713 118.167 172.330 1.00 35.11  ? 345  THR   B CB  1 
ATOM   2330  O  OG1 . THR   A 1 345  ? 128.775 117.252 171.751 1.00 49.16  ? 345  THR   B OG1 1 
ATOM   2331  C  CG2 . THR   A 1 345  ? 129.426 118.296 173.808 1.00 41.00  ? 345  THR   B CG2 1 
ATOM   2332  N  N   . VAL   A 1 346  ? 131.083 118.871 169.850 1.00 41.58  ? 346  VAL   B N   1 
ATOM   2333  C  CA  . VAL   A 1 346  ? 131.549 118.752 168.475 1.00 34.92  ? 346  VAL   B CA  1 
ATOM   2334  C  C   . VAL   A 1 346  ? 132.090 117.350 168.245 1.00 42.35  ? 346  VAL   B C   1 
ATOM   2335  O  O   . VAL   A 1 346  ? 132.714 116.757 169.132 1.00 51.84  ? 346  VAL   B O   1 
ATOM   2336  C  CB  . VAL   A 1 346  ? 132.620 119.808 168.139 1.00 38.87  ? 346  VAL   B CB  1 
ATOM   2337  C  CG1 . VAL   A 1 346  ? 131.977 121.166 167.941 1.00 45.58  ? 346  VAL   B CG1 1 
ATOM   2338  C  CG2 . VAL   A 1 346  ? 133.665 119.868 169.238 1.00 41.70  ? 346  VAL   B CG2 1 
ATOM   2339  N  N   . SER   A 1 347  ? 131.839 116.822 167.055 1.00 41.27  ? 347  SER   B N   1 
ATOM   2340  C  CA  . SER   A 1 347  ? 132.400 115.567 166.581 1.00 41.08  ? 347  SER   B CA  1 
ATOM   2341  C  C   . SER   A 1 347  ? 133.261 115.855 165.352 1.00 45.43  ? 347  SER   B C   1 
ATOM   2342  O  O   . SER   A 1 347  ? 133.579 117.007 165.048 1.00 54.93  ? 347  SER   B O   1 
ATOM   2343  C  CB  . SER   A 1 347  ? 131.293 114.558 166.280 1.00 45.34  ? 347  SER   B CB  1 
ATOM   2344  O  OG  . SER   A 1 347  ? 130.425 115.044 165.273 1.00 53.87  ? 347  SER   B OG  1 
ATOM   2345  N  N   . TRP   A 1 348  ? 133.655 114.792 164.649 1.00 39.71  ? 348  TRP   B N   1 
ATOM   2346  C  CA  . TRP   A 1 348  ? 134.467 114.973 163.453 1.00 40.48  ? 348  TRP   B CA  1 
ATOM   2347  C  C   . TRP   A 1 348  ? 133.695 115.638 162.320 1.00 46.75  ? 348  TRP   B C   1 
ATOM   2348  O  O   . TRP   A 1 348  ? 134.317 116.159 161.389 1.00 49.60  ? 348  TRP   B O   1 
ATOM   2349  C  CB  . TRP   A 1 348  ? 135.045 113.631 162.994 1.00 42.65  ? 348  TRP   B CB  1 
ATOM   2350  C  CG  . TRP   A 1 348  ? 134.029 112.605 162.606 1.00 42.25  ? 348  TRP   B CG  1 
ATOM   2351  C  CD1 . TRP   A 1 348  ? 133.327 111.789 163.442 1.00 44.04  ? 348  TRP   B CD1 1 
ATOM   2352  C  CD2 . TRP   A 1 348  ? 133.616 112.267 161.277 1.00 37.27  ? 348  TRP   B CD2 1 
ATOM   2353  N  NE1 . TRP   A 1 348  ? 132.495 110.972 162.719 1.00 42.02  ? 348  TRP   B NE1 1 
ATOM   2354  C  CE2 . TRP   A 1 348  ? 132.654 111.247 161.387 1.00 40.35  ? 348  TRP   B CE2 1 
ATOM   2355  C  CE3 . TRP   A 1 348  ? 133.964 112.732 160.006 1.00 39.71  ? 348  TRP   B CE3 1 
ATOM   2356  C  CZ2 . TRP   A 1 348  ? 132.035 110.685 160.275 1.00 49.62  ? 348  TRP   B CZ2 1 
ATOM   2357  C  CZ3 . TRP   A 1 348  ? 133.348 112.174 158.906 1.00 45.55  ? 348  TRP   B CZ3 1 
ATOM   2358  C  CH2 . TRP   A 1 348  ? 132.396 111.160 159.046 1.00 48.53  ? 348  TRP   B CH2 1 
ATOM   2359  N  N   . ILE   A 1 349  ? 132.360 115.644 162.378 1.00 43.84  ? 349  ILE   B N   1 
ATOM   2360  C  CA  . ILE   A 1 349  ? 131.557 116.343 161.379 1.00 44.71  ? 349  ILE   B CA  1 
ATOM   2361  C  C   . ILE   A 1 349  ? 131.072 117.701 161.861 1.00 49.11  ? 349  ILE   B C   1 
ATOM   2362  O  O   . ILE   A 1 349  ? 130.445 118.433 161.079 1.00 55.66  ? 349  ILE   B O   1 
ATOM   2363  C  CB  . ILE   A 1 349  ? 130.342 115.503 160.931 1.00 45.11  ? 349  ILE   B CB  1 
ATOM   2364  C  CG1 . ILE   A 1 349  ? 129.331 115.377 162.067 1.00 46.75  ? 349  ILE   B CG1 1 
ATOM   2365  C  CG2 . ILE   A 1 349  ? 130.780 114.136 160.452 1.00 47.36  ? 349  ILE   B CG2 1 
ATOM   2366  C  CD1 . ILE   A 1 349  ? 128.025 114.777 161.631 1.00 47.20  ? 349  ILE   B CD1 1 
ATOM   2367  N  N   . GLY   A 1 350  ? 131.332 118.060 163.115 1.00 38.23  ? 350  GLY   B N   1 
ATOM   2368  C  CA  . GLY   A 1 350  ? 130.896 119.336 163.642 1.00 36.25  ? 350  GLY   B CA  1 
ATOM   2369  C  C   . GLY   A 1 350  ? 129.711 119.232 164.577 1.00 47.60  ? 350  GLY   B C   1 
ATOM   2370  O  O   . GLY   A 1 350  ? 129.785 118.577 165.620 1.00 55.33  ? 350  GLY   B O   1 
ATOM   2371  N  N   . GLY   A 1 351  ? 128.607 119.877 164.211 1.00 44.85  ? 351  GLY   B N   1 
ATOM   2372  C  CA  . GLY   A 1 351  ? 127.409 119.844 165.014 1.00 39.19  ? 351  GLY   B CA  1 
ATOM   2373  C  C   . GLY   A 1 351  ? 126.574 118.613 164.747 1.00 47.51  ? 351  GLY   B C   1 
ATOM   2374  O  O   . GLY   A 1 351  ? 126.942 117.716 163.990 1.00 48.50  ? 351  GLY   B O   1 
ATOM   2375  N  N   . LYS   A 1 352  ? 125.410 118.579 165.388 1.00 44.68  ? 352  LYS   B N   1 
ATOM   2376  C  CA  . LYS   A 1 352  ? 124.497 117.446 165.271 1.00 41.41  ? 352  LYS   B CA  1 
ATOM   2377  C  C   . LYS   A 1 352  ? 123.610 117.666 164.053 1.00 41.99  ? 352  LYS   B C   1 
ATOM   2378  O  O   . LYS   A 1 352  ? 122.643 118.429 164.103 1.00 50.90  ? 352  LYS   B O   1 
ATOM   2379  C  CB  . LYS   A 1 352  ? 123.676 117.283 166.543 1.00 41.69  ? 352  LYS   B CB  1 
ATOM   2380  C  CG  . LYS   A 1 352  ? 122.972 115.949 166.634 1.00 44.08  ? 352  LYS   B CG  1 
ATOM   2381  C  CD  . LYS   A 1 352  ? 122.444 115.693 168.026 1.00 44.88  ? 352  LYS   B CD  1 
ATOM   2382  C  CE  . LYS   A 1 352  ? 121.923 114.275 168.150 1.00 45.36  ? 352  LYS   B CE  1 
ATOM   2383  N  NZ  . LYS   A 1 352  ? 121.307 114.028 169.479 1.00 47.15  ? 352  LYS   B NZ  1 
ATOM   2384  N  N   . GLN   A 1 353  ? 123.943 116.995 162.954 1.00 35.52  ? 353  GLN   B N   1 
ATOM   2385  C  CA  . GLN   A 1 353  ? 123.144 117.053 161.731 1.00 38.58  ? 353  GLN   B CA  1 
ATOM   2386  C  C   . GLN   A 1 353  ? 123.376 115.761 160.962 1.00 41.05  ? 353  GLN   B C   1 
ATOM   2387  O  O   . GLN   A 1 353  ? 124.341 115.648 160.192 1.00 49.49  ? 353  GLN   B O   1 
ATOM   2388  C  CB  . GLN   A 1 353  ? 123.496 118.269 160.878 1.00 37.93  ? 353  GLN   B CB  1 
ATOM   2389  C  CG  . GLN   A 1 353  ? 122.651 118.413 159.630 1.00 37.81  ? 353  GLN   B CG  1 
ATOM   2390  C  CD  . GLN   A 1 353  ? 121.211 118.754 159.938 1.00 40.81  ? 353  GLN   B CD  1 
ATOM   2391  O  OE1 . GLN   A 1 353  ? 120.302 118.379 159.200 1.00 53.10  ? 353  GLN   B OE1 1 
ATOM   2392  N  NE2 . GLN   A 1 353  ? 120.994 119.479 161.028 1.00 38.67  ? 353  GLN   B NE2 1 
ATOM   2393  N  N   . PRO   A 1 354  ? 122.517 114.761 161.145 1.00 38.52  ? 354  PRO   B N   1 
ATOM   2394  C  CA  . PRO   A 1 354  ? 122.715 113.483 160.452 1.00 38.01  ? 354  PRO   B CA  1 
ATOM   2395  C  C   . PRO   A 1 354  ? 122.083 113.444 159.070 1.00 44.70  ? 354  PRO   B C   1 
ATOM   2396  O  O   . PRO   A 1 354  ? 121.877 112.361 158.515 1.00 56.94  ? 354  PRO   B O   1 
ATOM   2397  C  CB  . PRO   A 1 354  ? 122.046 112.481 161.395 1.00 39.25  ? 354  PRO   B CB  1 
ATOM   2398  C  CG  . PRO   A 1 354  ? 120.938 113.264 162.004 1.00 36.67  ? 354  PRO   B CG  1 
ATOM   2399  C  CD  . PRO   A 1 354  ? 121.427 114.686 162.133 1.00 39.32  ? 354  PRO   B CD  1 
ATOM   2400  N  N   . PHE   A 1 355  ? 121.762 114.611 158.510 1.00 38.61  ? 355  PHE   B N   1 
ATOM   2401  C  CA  . PHE   A 1 355  ? 121.059 114.644 157.232 1.00 37.09  ? 355  PHE   B CA  1 
ATOM   2402  C  C   . PHE   A 1 355  ? 121.894 114.032 156.116 1.00 40.93  ? 355  PHE   B C   1 
ATOM   2403  O  O   . PHE   A 1 355  ? 121.372 113.274 155.289 1.00 48.79  ? 355  PHE   B O   1 
ATOM   2404  C  CB  . PHE   A 1 355  ? 120.673 116.078 156.879 1.00 36.11  ? 355  PHE   B CB  1 
ATOM   2405  C  CG  . PHE   A 1 355  ? 120.051 116.218 155.521 1.00 38.64  ? 355  PHE   B CG  1 
ATOM   2406  C  CD1 . PHE   A 1 355  ? 118.711 115.945 155.330 1.00 37.00  ? 355  PHE   B CD1 1 
ATOM   2407  C  CD2 . PHE   A 1 355  ? 120.806 116.623 154.436 1.00 41.56  ? 355  PHE   B CD2 1 
ATOM   2408  C  CE1 . PHE   A 1 355  ? 118.138 116.071 154.085 1.00 37.95  ? 355  PHE   B CE1 1 
ATOM   2409  C  CE2 . PHE   A 1 355  ? 120.237 116.747 153.188 1.00 43.88  ? 355  PHE   B CE2 1 
ATOM   2410  C  CZ  . PHE   A 1 355  ? 118.901 116.474 153.015 1.00 44.94  ? 355  PHE   B CZ  1 
ATOM   2411  N  N   . LEU   A 1 356  ? 123.186 114.353 156.067 1.00 38.35  ? 356  LEU   B N   1 
ATOM   2412  C  CA  . LEU   A 1 356  ? 124.033 113.841 154.997 1.00 42.07  ? 356  LEU   B CA  1 
ATOM   2413  C  C   . LEU   A 1 356  ? 124.189 112.329 155.091 1.00 48.26  ? 356  LEU   B C   1 
ATOM   2414  O  O   . LEU   A 1 356  ? 124.198 111.635 154.067 1.00 54.23  ? 356  LEU   B O   1 
ATOM   2415  C  CB  . LEU   A 1 356  ? 125.392 114.534 155.033 1.00 39.96  ? 356  LEU   B CB  1 
ATOM   2416  C  CG  . LEU   A 1 356  ? 126.215 114.505 153.748 1.00 42.98  ? 356  LEU   B CG  1 
ATOM   2417  C  CD1 . LEU   A 1 356  ? 125.426 115.095 152.601 1.00 43.98  ? 356  LEU   B CD1 1 
ATOM   2418  C  CD2 . LEU   A 1 356  ? 127.505 115.269 153.948 1.00 44.99  ? 356  LEU   B CD2 1 
ATOM   2419  N  N   . GLY   A 1 357  ? 124.306 111.798 156.308 1.00 32.99  ? 357  GLY   B N   1 
ATOM   2420  C  CA  . GLY   A 1 357  ? 124.423 110.358 156.464 1.00 28.42  ? 357  GLY   B CA  1 
ATOM   2421  C  C   . GLY   A 1 357  ? 123.185 109.620 155.998 1.00 37.31  ? 357  GLY   B C   1 
ATOM   2422  O  O   . GLY   A 1 357  ? 123.277 108.595 155.314 1.00 54.28  ? 357  GLY   B O   1 
ATOM   2423  N  N   . TRP   A 1 358  ? 122.008 110.132 156.354 1.00 33.20  ? 358  TRP   B N   1 
ATOM   2424  C  CA  . TRP   A 1 358  ? 120.777 109.501 155.904 1.00 37.75  ? 358  TRP   B CA  1 
ATOM   2425  C  C   . TRP   A 1 358  ? 120.582 109.662 154.404 1.00 39.77  ? 358  TRP   B C   1 
ATOM   2426  O  O   . TRP   A 1 358  ? 120.039 108.762 153.755 1.00 48.15  ? 358  TRP   B O   1 
ATOM   2427  C  CB  . TRP   A 1 358  ? 119.587 110.069 156.673 1.00 41.24  ? 358  TRP   B CB  1 
ATOM   2428  C  CG  . TRP   A 1 358  ? 119.570 109.633 158.099 1.00 37.98  ? 358  TRP   B CG  1 
ATOM   2429  C  CD1 . TRP   A 1 358  ? 119.715 110.421 159.197 1.00 40.85  ? 358  TRP   B CD1 1 
ATOM   2430  C  CD2 . TRP   A 1 358  ? 119.418 108.294 158.582 1.00 41.83  ? 358  TRP   B CD2 1 
ATOM   2431  N  NE1 . TRP   A 1 358  ? 119.654 109.661 160.336 1.00 44.72  ? 358  TRP   B NE1 1 
ATOM   2432  C  CE2 . TRP   A 1 358  ? 119.472 108.350 159.985 1.00 37.99  ? 358  TRP   B CE2 1 
ATOM   2433  C  CE3 . TRP   A 1 358  ? 119.237 107.054 157.964 1.00 48.82  ? 358  TRP   B CE3 1 
ATOM   2434  C  CZ2 . TRP   A 1 358  ? 119.352 107.216 160.781 1.00 42.77  ? 358  TRP   B CZ2 1 
ATOM   2435  C  CZ3 . TRP   A 1 358  ? 119.120 105.931 158.755 1.00 49.13  ? 358  TRP   B CZ3 1 
ATOM   2436  C  CH2 . TRP   A 1 358  ? 119.177 106.018 160.148 1.00 46.96  ? 358  TRP   B CH2 1 
ATOM   2437  N  N   . ALA   A 1 359  ? 121.025 110.784 153.835 1.00 39.90  ? 359  ALA   B N   1 
ATOM   2438  C  CA  . ALA   A 1 359  ? 120.990 110.932 152.385 1.00 37.45  ? 359  ALA   B CA  1 
ATOM   2439  C  C   . ALA   A 1 359  ? 121.875 109.892 151.710 1.00 43.67  ? 359  ALA   B C   1 
ATOM   2440  O  O   . ALA   A 1 359  ? 121.482 109.291 150.703 1.00 53.49  ? 359  ALA   B O   1 
ATOM   2441  C  CB  . ALA   A 1 359  ? 121.419 112.344 151.991 1.00 39.86  ? 359  ALA   B CB  1 
ATOM   2442  N  N   . TYR   A 1 360  ? 123.070 109.660 152.258 1.00 44.08  ? 360  TYR   B N   1 
ATOM   2443  C  CA  . TYR   A 1 360  ? 123.951 108.628 151.720 1.00 35.28  ? 360  TYR   B CA  1 
ATOM   2444  C  C   . TYR   A 1 360  ? 123.321 107.246 151.823 1.00 39.52  ? 360  TYR   B C   1 
ATOM   2445  O  O   . TYR   A 1 360  ? 123.403 106.448 150.883 1.00 52.59  ? 360  TYR   B O   1 
ATOM   2446  C  CB  . TYR   A 1 360  ? 125.289 108.646 152.451 1.00 34.79  ? 360  TYR   B CB  1 
ATOM   2447  C  CG  . TYR   A 1 360  ? 126.360 109.491 151.809 1.00 42.24  ? 360  TYR   B CG  1 
ATOM   2448  C  CD1 . TYR   A 1 360  ? 127.158 108.981 150.799 1.00 45.18  ? 360  TYR   B CD1 1 
ATOM   2449  C  CD2 . TYR   A 1 360  ? 126.592 110.788 152.232 1.00 42.54  ? 360  TYR   B CD2 1 
ATOM   2450  C  CE1 . TYR   A 1 360  ? 128.144 109.744 150.218 1.00 46.12  ? 360  TYR   B CE1 1 
ATOM   2451  C  CE2 . TYR   A 1 360  ? 127.573 111.556 151.658 1.00 39.42  ? 360  TYR   B CE2 1 
ATOM   2452  C  CZ  . TYR   A 1 360  ? 128.347 111.030 150.651 1.00 42.30  ? 360  TYR   B CZ  1 
ATOM   2453  O  OH  . TYR   A 1 360  ? 129.331 111.794 150.073 1.00 44.37  ? 360  TYR   B OH  1 
ATOM   2454  N  N   . ILE   A 1 361  ? 122.700 106.939 152.963 1.00 30.11  ? 361  ILE   B N   1 
ATOM   2455  C  CA  . ILE   A 1 361  ? 122.080 105.626 153.137 1.00 35.09  ? 361  ILE   B CA  1 
ATOM   2456  C  C   . ILE   A 1 361  ? 120.925 105.442 152.159 1.00 47.42  ? 361  ILE   B C   1 
ATOM   2457  O  O   . ILE   A 1 361  ? 120.769 104.373 151.553 1.00 49.15  ? 361  ILE   B O   1 
ATOM   2458  C  CB  . ILE   A 1 361  ? 121.628 105.436 154.596 1.00 38.66  ? 361  ILE   B CB  1 
ATOM   2459  C  CG1 . ILE   A 1 361  ? 122.843 105.318 155.514 1.00 40.91  ? 361  ILE   B CG1 1 
ATOM   2460  C  CG2 . ILE   A 1 361  ? 120.740 104.210 154.728 1.00 46.82  ? 361  ILE   B CG2 1 
ATOM   2461  C  CD1 . ILE   A 1 361  ? 122.495 105.151 156.969 1.00 43.66  ? 361  ILE   B CD1 1 
ATOM   2462  N  N   . ALA   A 1 362  ? 120.097 106.475 151.989 1.00 43.49  ? 362  ALA   B N   1 
ATOM   2463  C  CA  . ALA   A 1 362  ? 118.993 106.394 151.040 1.00 33.39  ? 362  ALA   B CA  1 
ATOM   2464  C  C   . ALA   A 1 362  ? 119.501 106.231 149.614 1.00 36.51  ? 362  ALA   B C   1 
ATOM   2465  O  O   . ALA   A 1 362  ? 118.932 105.463 148.828 1.00 53.77  ? 362  ALA   B O   1 
ATOM   2466  C  CB  . ALA   A 1 362  ? 118.108 107.633 151.158 1.00 38.90  ? 362  ALA   B CB  1 
ATOM   2467  N  N   . ALA   A 1 363  ? 120.567 106.950 149.259 1.00 32.93  ? 363  ALA   B N   1 
ATOM   2468  C  CA  . ALA   A 1 363  ? 121.153 106.797 147.934 1.00 34.89  ? 363  ALA   B CA  1 
ATOM   2469  C  C   . ALA   A 1 363  ? 121.686 105.387 147.729 1.00 41.61  ? 363  ALA   B C   1 
ATOM   2470  O  O   . ALA   A 1 363  ? 121.523 104.806 146.651 1.00 52.75  ? 363  ALA   B O   1 
ATOM   2471  C  CB  . ALA   A 1 363  ? 122.264 107.825 147.727 1.00 37.40  ? 363  ALA   B CB  1 
ATOM   2472  N  N   . ALA   A 1 364  ? 122.322 104.818 148.754 1.00 36.76  ? 364  ALA   B N   1 
ATOM   2473  C  CA  . ALA   A 1 364  ? 122.815 103.449 148.654 1.00 35.48  ? 364  ALA   B CA  1 
ATOM   2474  C  C   . ALA   A 1 364  ? 121.673 102.460 148.462 1.00 43.91  ? 364  ALA   B C   1 
ATOM   2475  O  O   . ALA   A 1 364  ? 121.772 101.539 147.642 1.00 55.80  ? 364  ALA   B O   1 
ATOM   2476  C  CB  . ALA   A 1 364  ? 123.626 103.093 149.897 1.00 39.98  ? 364  ALA   B CB  1 
ATOM   2477  N  N   . ILE   A 1 365  ? 120.582 102.632 149.210 1.00 40.04  ? 365  ILE   B N   1 
ATOM   2478  C  CA  . ILE   A 1 365  ? 119.437 101.734 149.071 1.00 38.44  ? 365  ILE   B CA  1 
ATOM   2479  C  C   . ILE   A 1 365  ? 118.839 101.843 147.675 1.00 46.27  ? 365  ILE   B C   1 
ATOM   2480  O  O   . ILE   A 1 365  ? 118.519 100.830 147.037 1.00 53.20  ? 365  ILE   B O   1 
ATOM   2481  C  CB  . ILE   A 1 365  ? 118.389 102.026 150.160 1.00 40.68  ? 365  ILE   B CB  1 
ATOM   2482  C  CG1 . ILE   A 1 365  ? 118.947 101.689 151.542 1.00 49.87  ? 365  ILE   B CG1 1 
ATOM   2483  C  CG2 . ILE   A 1 365  ? 117.117 101.241 149.900 1.00 42.47  ? 365  ILE   B CG2 1 
ATOM   2484  C  CD1 . ILE   A 1 365  ? 117.978 101.949 152.671 1.00 51.03  ? 365  ILE   B CD1 1 
ATOM   2485  N  N   . LEU   A 1 366  ? 118.682 103.072 147.178 1.00 41.45  ? 366  LEU   B N   1 
ATOM   2486  C  CA  . LEU   A 1 366  ? 118.148 103.268 145.835 1.00 39.44  ? 366  LEU   B CA  1 
ATOM   2487  C  C   . LEU   A 1 366  ? 119.053 102.640 144.783 1.00 49.80  ? 366  LEU   B C   1 
ATOM   2488  O  O   . LEU   A 1 366  ? 118.570 102.004 143.838 1.00 55.30  ? 366  LEU   B O   1 
ATOM   2489  C  CB  . LEU   A 1 366  ? 117.965 104.760 145.564 1.00 38.74  ? 366  LEU   B CB  1 
ATOM   2490  C  CG  . LEU   A 1 366  ? 117.547 105.167 144.153 1.00 52.29  ? 366  LEU   B CG  1 
ATOM   2491  C  CD1 . LEU   A 1 366  ? 116.165 104.626 143.822 1.00 53.22  ? 366  LEU   B CD1 1 
ATOM   2492  C  CD2 . LEU   A 1 366  ? 117.588 106.677 144.005 1.00 48.65  ? 366  LEU   B CD2 1 
ATOM   2493  N  N   . CYS   A 1 367  ? 120.369 102.806 144.929 1.00 46.66  ? 367  CYS   B N   1 
ATOM   2494  C  CA  . CYS   A 1 367  ? 121.302 102.229 143.970 1.00 43.10  ? 367  CYS   B CA  1 
ATOM   2495  C  C   . CYS   A 1 367  ? 121.252 100.708 143.993 1.00 52.26  ? 367  CYS   B C   1 
ATOM   2496  O  O   . CYS   A 1 367  ? 121.305 100.067 142.938 1.00 63.39  ? 367  CYS   B O   1 
ATOM   2497  C  CB  . CYS   A 1 367  ? 122.718 102.727 144.251 1.00 46.02  ? 367  CYS   B CB  1 
ATOM   2498  S  SG  . CYS   A 1 367  ? 122.976 104.479 143.890 1.00 68.77  ? 367  CYS   B SG  1 
ATOM   2499  N  N   . VAL   A 1 368  ? 121.150 100.111 145.182 1.00 48.97  ? 368  VAL   B N   1 
ATOM   2500  C  CA  . VAL   A 1 368  ? 121.053 98.657  145.271 1.00 42.35  ? 368  VAL   B CA  1 
ATOM   2501  C  C   . VAL   A 1 368  ? 119.764 98.163  144.626 1.00 51.43  ? 368  VAL   B C   1 
ATOM   2502  O  O   . VAL   A 1 368  ? 119.763 97.156  143.906 1.00 61.65  ? 368  VAL   B O   1 
ATOM   2503  C  CB  . VAL   A 1 368  ? 121.171 98.202  146.736 1.00 48.76  ? 368  VAL   B CB  1 
ATOM   2504  C  CG1 . VAL   A 1 368  ? 120.807 96.735  146.867 1.00 54.09  ? 368  VAL   B CG1 1 
ATOM   2505  C  CG2 . VAL   A 1 368  ? 122.580 98.442  147.244 1.00 54.58  ? 368  VAL   B CG2 1 
ATOM   2506  N  N   . VAL   A 1 369  ? 118.650 98.858  144.866 1.00 43.41  ? 369  VAL   B N   1 
ATOM   2507  C  CA  . VAL   A 1 369  ? 117.381 98.461  144.256 1.00 43.83  ? 369  VAL   B CA  1 
ATOM   2508  C  C   . VAL   A 1 369  ? 117.472 98.546  142.737 1.00 52.10  ? 369  VAL   B C   1 
ATOM   2509  O  O   . VAL   A 1 369  ? 117.033 97.638  142.016 1.00 63.04  ? 369  VAL   B O   1 
ATOM   2510  C  CB  . VAL   A 1 369  ? 116.228 99.321  144.804 1.00 46.55  ? 369  VAL   B CB  1 
ATOM   2511  C  CG1 . VAL   A 1 369  ? 114.973 99.121  143.973 1.00 48.35  ? 369  VAL   B CG1 1 
ATOM   2512  C  CG2 . VAL   A 1 369  ? 115.957 98.975  146.254 1.00 51.24  ? 369  VAL   B CG2 1 
ATOM   2513  N  N   . LEU   A 1 370  ? 118.046 99.638  142.228 1.00 47.37  ? 370  LEU   B N   1 
ATOM   2514  C  CA  . LEU   A 1 370  ? 118.183 99.797  140.785 1.00 45.12  ? 370  LEU   B CA  1 
ATOM   2515  C  C   . LEU   A 1 370  ? 119.091 98.727  140.193 1.00 52.52  ? 370  LEU   B C   1 
ATOM   2516  O  O   . LEU   A 1 370  ? 118.812 98.198  139.112 1.00 60.06  ? 370  LEU   B O   1 
ATOM   2517  C  CB  . LEU   A 1 370  ? 118.710 101.192 140.455 1.00 47.19  ? 370  LEU   B CB  1 
ATOM   2518  C  CG  . LEU   A 1 370  ? 117.750 102.352 140.713 1.00 51.82  ? 370  LEU   B CG  1 
ATOM   2519  C  CD1 . LEU   A 1 370  ? 118.396 103.669 140.334 1.00 53.67  ? 370  LEU   B CD1 1 
ATOM   2520  C  CD2 . LEU   A 1 370  ? 116.453 102.152 139.949 1.00 57.85  ? 370  LEU   B CD2 1 
ATOM   2521  N  N   . ALA   A 1 371  ? 120.184 98.397  140.883 1.00 50.86  ? 371  ALA   B N   1 
ATOM   2522  C  CA  . ALA   A 1 371  ? 121.086 97.362  140.391 1.00 51.48  ? 371  ALA   B CA  1 
ATOM   2523  C  C   . ALA   A 1 371  ? 120.405 96.000  140.367 1.00 51.59  ? 371  ALA   B C   1 
ATOM   2524  O  O   . ALA   A 1 371  ? 120.585 95.230  139.417 1.00 58.41  ? 371  ALA   B O   1 
ATOM   2525  C  CB  . ALA   A 1 371  ? 122.350 97.318  141.246 1.00 56.02  ? 371  ALA   B CB  1 
ATOM   2526  N  N   . VAL   A 1 372  ? 119.620 95.685  141.399 1.00 51.00  ? 372  VAL   B N   1 
ATOM   2527  C  CA  . VAL   A 1 372  ? 118.891 94.419  141.420 1.00 55.22  ? 372  VAL   B CA  1 
ATOM   2528  C  C   . VAL   A 1 372  ? 117.892 94.358  140.272 1.00 61.08  ? 372  VAL   B C   1 
ATOM   2529  O  O   . VAL   A 1 372  ? 117.788 93.342  139.570 1.00 69.19  ? 372  VAL   B O   1 
ATOM   2530  C  CB  . VAL   A 1 372  ? 118.202 94.225  142.782 1.00 60.18  ? 372  VAL   B CB  1 
ATOM   2531  C  CG1 . VAL   A 1 372  ? 117.170 93.114  142.703 1.00 59.61  ? 372  VAL   B CG1 1 
ATOM   2532  C  CG2 . VAL   A 1 372  ? 119.234 93.918  143.853 1.00 60.83  ? 372  VAL   B CG2 1 
ATOM   2533  N  N   . ALA   A 1 373  ? 117.144 95.444  140.058 1.00 56.75  ? 373  ALA   B N   1 
ATOM   2534  C  CA  . ALA   A 1 373  ? 116.176 95.467  138.966 1.00 56.63  ? 373  ALA   B CA  1 
ATOM   2535  C  C   . ALA   A 1 373  ? 116.865 95.327  137.613 1.00 60.02  ? 373  ALA   B C   1 
ATOM   2536  O  O   . ALA   A 1 373  ? 116.384 94.602  136.733 1.00 65.98  ? 373  ALA   B O   1 
ATOM   2537  C  CB  . ALA   A 1 373  ? 115.354 96.754  139.020 1.00 56.07  ? 373  ALA   B CB  1 
ATOM   2538  N  N   . GLY   A 1 374  ? 117.991 96.017  137.428 1.00 67.30  ? 374  GLY   B N   1 
ATOM   2539  C  CA  . GLY   A 1 374  ? 118.717 95.910  136.175 1.00 69.66  ? 374  GLY   B CA  1 
ATOM   2540  C  C   . GLY   A 1 374  ? 119.277 94.522  135.941 1.00 73.16  ? 374  GLY   B C   1 
ATOM   2541  O  O   . GLY   A 1 374  ? 119.267 94.024  134.814 1.00 75.13  ? 374  GLY   B O   1 
ATOM   2542  N  N   . LEU   A 1 375  ? 119.777 93.880  136.999 1.00 68.77  ? 375  LEU   B N   1 
ATOM   2543  C  CA  . LEU   A 1 375  ? 120.263 92.510  136.874 1.00 65.39  ? 375  LEU   B CA  1 
ATOM   2544  C  C   . LEU   A 1 375  ? 119.133 91.565  136.494 1.00 67.44  ? 375  LEU   B C   1 
ATOM   2545  O  O   . LEU   A 1 375  ? 119.305 90.690  135.635 1.00 73.43  ? 375  LEU   B O   1 
ATOM   2546  C  CB  . LEU   A 1 375  ? 120.924 92.074  138.182 1.00 67.99  ? 375  LEU   B CB  1 
ATOM   2547  C  CG  . LEU   A 1 375  ? 122.023 91.010  138.138 1.00 73.27  ? 375  LEU   B CG  1 
ATOM   2548  C  CD1 . LEU   A 1 375  ? 121.447 89.611  137.986 1.00 73.80  ? 375  LEU   B CD1 1 
ATOM   2549  C  CD2 . LEU   A 1 375  ? 123.009 91.310  137.019 1.00 70.08  ? 375  LEU   B CD2 1 
ATOM   2550  N  N   . ILE   A 1 376  ? 117.964 91.735  137.116 1.00 63.56  ? 376  ILE   B N   1 
ATOM   2551  C  CA  . ILE   A 1 376  ? 116.814 90.901  136.775 1.00 70.72  ? 376  ILE   B CA  1 
ATOM   2552  C  C   . ILE   A 1 376  ? 116.433 91.097  135.313 1.00 76.45  ? 376  ILE   B C   1 
ATOM   2553  O  O   . ILE   A 1 376  ? 116.205 90.129  134.576 1.00 77.39  ? 376  ILE   B O   1 
ATOM   2554  C  CB  . ILE   A 1 376  ? 115.632 91.208  137.712 1.00 71.24  ? 376  ILE   B CB  1 
ATOM   2555  C  CG1 . ILE   A 1 376  ? 115.915 90.684  139.120 1.00 72.92  ? 376  ILE   B CG1 1 
ATOM   2556  C  CG2 . ILE   A 1 376  ? 114.344 90.616  137.164 1.00 72.49  ? 376  ILE   B CG2 1 
ATOM   2557  C  CD1 . ILE   A 1 376  ? 114.789 90.932  140.101 1.00 73.13  ? 376  ILE   B CD1 1 
ATOM   2558  N  N   . ARG   A 1 377  ? 116.375 92.354  134.867 1.00 76.80  ? 377  ARG   B N   1 
ATOM   2559  C  CA  . ARG   A 1 377  ? 115.992 92.634  133.486 1.00 73.14  ? 377  ARG   B CA  1 
ATOM   2560  C  C   . ARG   A 1 377  ? 117.014 92.072  132.504 1.00 74.68  ? 377  ARG   B C   1 
ATOM   2561  O  O   . ARG   A 1 377  ? 116.645 91.523  131.459 1.00 75.71  ? 377  ARG   B O   1 
ATOM   2562  C  CB  . ARG   A 1 377  ? 115.820 94.140  133.289 1.00 70.98  ? 377  ARG   B CB  1 
ATOM   2563  C  CG  . ARG   A 1 377  ? 115.030 94.534  132.052 1.00 73.33  ? 377  ARG   B CG  1 
ATOM   2564  C  CD  . ARG   A 1 377  ? 115.927 94.725  130.843 1.00 78.73  ? 377  ARG   B CD  1 
ATOM   2565  N  NE  . ARG   A 1 377  ? 116.942 95.746  131.072 1.00 78.86  ? 377  ARG   B NE  1 
ATOM   2566  C  CZ  . ARG   A 1 377  ? 116.776 97.037  130.820 1.00 78.26  ? 377  ARG   B CZ  1 
ATOM   2567  N  NH1 . ARG   A 1 377  ? 115.637 97.505  130.336 1.00 77.65  ? 377  ARG   B NH1 1 
ATOM   2568  N  NH2 . ARG   A 1 377  ? 117.777 97.878  131.059 1.00 78.46  ? 377  ARG   B NH2 1 
ATOM   2569  N  N   . HIS   A 1 378  ? 118.303 92.206  132.819 1.00 82.24  ? 378  HIS   B N   1 
ATOM   2570  C  CA  . HIS   A 1 378  ? 119.345 91.693  131.937 1.00 82.09  ? 378  HIS   B CA  1 
ATOM   2571  C  C   . HIS   A 1 378  ? 119.293 90.174  131.843 1.00 87.31  ? 378  HIS   B C   1 
ATOM   2572  O  O   . HIS   A 1 378  ? 119.470 89.610  130.757 1.00 87.70  ? 378  HIS   B O   1 
ATOM   2573  C  CB  . HIS   A 1 378  ? 120.716 92.156  132.425 1.00 76.93  ? 378  HIS   B CB  1 
ATOM   2574  C  CG  . HIS   A 1 378  ? 121.857 91.581  131.649 1.00 80.89  ? 378  HIS   B CG  1 
ATOM   2575  N  ND1 . HIS   A 1 378  ? 121.897 91.585  130.272 1.00 84.30  ? 378  HIS   B ND1 1 
ATOM   2576  C  CD2 . HIS   A 1 378  ? 123.001 90.983  132.057 1.00 84.31  ? 378  HIS   B CD2 1 
ATOM   2577  C  CE1 . HIS   A 1 378  ? 123.016 91.013  129.864 1.00 85.96  ? 378  HIS   B CE1 1 
ATOM   2578  N  NE2 . HIS   A 1 378  ? 123.704 90.640  130.928 1.00 85.91  ? 378  HIS   B NE2 1 
ATOM   2579  N  N   . LEU   A 1 379  ? 119.060 89.492  132.967 1.00 83.18  ? 379  LEU   B N   1 
ATOM   2580  C  CA  . LEU   A 1 379  ? 118.945 88.038  132.922 1.00 79.34  ? 379  LEU   B CA  1 
ATOM   2581  C  C   . LEU   A 1 379  ? 117.698 87.602  132.163 1.00 81.10  ? 379  LEU   B C   1 
ATOM   2582  O  O   . LEU   A 1 379  ? 117.725 86.594  131.448 1.00 82.62  ? 379  LEU   B O   1 
ATOM   2583  C  CB  . LEU   A 1 379  ? 118.941 87.462  134.336 1.00 80.54  ? 379  LEU   B CB  1 
ATOM   2584  C  CG  . LEU   A 1 379  ? 120.282 87.478  135.071 1.00 83.53  ? 379  LEU   B CG  1 
ATOM   2585  C  CD1 . LEU   A 1 379  ? 120.213 86.613  136.321 1.00 83.67  ? 379  LEU   B CD1 1 
ATOM   2586  C  CD2 . LEU   A 1 379  ? 121.405 87.019  134.154 1.00 80.92  ? 379  LEU   B CD2 1 
ATOM   2587  N  N   . VAL   A 1 380  ? 116.596 88.340  132.309 1.00 81.12  ? 380  VAL   B N   1 
ATOM   2588  C  CA  . VAL   A 1 380  ? 115.355 87.961  131.636 1.00 84.23  ? 380  VAL   B CA  1 
ATOM   2589  C  C   . VAL   A 1 380  ? 115.511 88.054  130.122 1.00 87.06  ? 380  VAL   B C   1 
ATOM   2590  O  O   . VAL   A 1 380  ? 115.201 87.104  129.393 1.00 85.25  ? 380  VAL   B O   1 
ATOM   2591  C  CB  . VAL   A 1 380  ? 114.185 88.827  132.136 1.00 81.92  ? 380  VAL   B CB  1 
ATOM   2592  C  CG1 . VAL   A 1 380  ? 113.014 88.743  131.172 1.00 82.50  ? 380  VAL   B CG1 1 
ATOM   2593  C  CG2 . VAL   A 1 380  ? 113.756 88.381  133.523 1.00 81.66  ? 380  VAL   B CG2 1 
ATOM   2594  N  N   . LYS   A 1 381  ? 115.998 89.191  129.626 1.00 92.36  ? 381  LYS   B N   1 
ATOM   2595  C  CA  . LYS   A 1 381  ? 116.146 89.429  128.189 1.00 89.11  ? 381  LYS   B CA  1 
ATOM   2596  C  C   . LYS   A 1 381  ? 117.509 90.049  127.912 1.00 88.71  ? 381  LYS   B C   1 
ATOM   2597  O  O   . LYS   A 1 381  ? 117.625 91.268  127.729 1.00 89.04  ? 381  LYS   B O   1 
ATOM   2598  C  CB  . LYS   A 1 381  ? 115.019 90.319  127.662 1.00 87.69  ? 381  LYS   B CB  1 
ATOM   2599  C  CG  . LYS   A 1 381  ? 114.978 90.437  126.146 1.00 90.02  ? 381  LYS   B CG  1 
ATOM   2600  C  CD  . LYS   A 1 381  ? 113.827 91.319  125.689 1.00 90.12  ? 381  LYS   B CD  1 
ATOM   2601  C  CE  . LYS   A 1 381  ? 112.487 90.744  126.116 1.00 91.62  ? 381  LYS   B CE  1 
ATOM   2602  N  NZ  . LYS   A 1 381  ? 112.257 89.387  125.547 1.00 90.30  ? 381  LYS   B NZ  1 
ATOM   2603  N  N   . PRO   A 1 382  ? 118.568 89.238  127.876 1.00 86.20  ? 382  PRO   B N   1 
ATOM   2604  C  CA  . PRO   A 1 382  ? 119.892 89.770  127.521 1.00 84.37  ? 382  PRO   B CA  1 
ATOM   2605  C  C   . PRO   A 1 382  ? 119.946 90.116  126.039 1.00 88.95  ? 382  PRO   B C   1 
ATOM   2606  O  O   . PRO   A 1 382  ? 119.541 89.321  125.187 1.00 93.00  ? 382  PRO   B O   1 
ATOM   2607  C  CB  . PRO   A 1 382  ? 120.843 88.618  127.863 1.00 84.03  ? 382  PRO   B CB  1 
ATOM   2608  C  CG  . PRO   A 1 382  ? 119.996 87.396  127.744 1.00 87.28  ? 382  PRO   B CG  1 
ATOM   2609  C  CD  . PRO   A 1 382  ? 118.612 87.798  128.180 1.00 88.00  ? 382  PRO   B CD  1 
ATOM   2610  N  N   . ARG   A 1 383  ? 120.444 91.309  125.736 1.00 88.01  ? 383  ARG   B N   1 
ATOM   2611  C  CA  . ARG   A 1 383  ? 120.516 91.797  124.368 1.00 89.49  ? 383  ARG   B CA  1 
ATOM   2612  C  C   . ARG   A 1 383  ? 121.965 91.861  123.905 1.00 90.62  ? 383  ARG   B C   1 
ATOM   2613  O  O   . ARG   A 1 383  ? 122.875 92.153  124.686 1.00 91.83  ? 383  ARG   B O   1 
ATOM   2614  C  CB  . ARG   A 1 383  ? 119.861 93.175  124.227 1.00 88.40  ? 383  ARG   B CB  1 
ATOM   2615  C  CG  . ARG   A 1 383  ? 120.428 94.257  125.134 1.00 90.85  ? 383  ARG   B CG  1 
ATOM   2616  C  CD  . ARG   A 1 383  ? 119.688 94.314  126.458 1.00 91.86  ? 383  ARG   B CD  1 
ATOM   2617  N  NE  . ARG   A 1 383  ? 118.243 94.341  126.268 1.00 91.92  ? 383  ARG   B NE  1 
ATOM   2618  C  CZ  . ARG   A 1 383  ? 117.531 95.446  126.096 1.00 91.78  ? 383  ARG   B CZ  1 
ATOM   2619  N  NH1 . ARG   A 1 383  ? 118.100 96.640  126.082 1.00 91.62  ? 383  ARG   B NH1 1 
ATOM   2620  N  NH2 . ARG   A 1 383  ? 116.214 95.351  125.934 1.00 91.32  ? 383  ARG   B NH2 1 
ATOM   2621  N  N   . LYS   A 1 384  ? 122.166 91.582  122.621 1.00 84.70  ? 384  LYS   B N   1 
ATOM   2622  C  CA  . LYS   A 1 384  ? 123.496 91.555  122.033 1.00 83.67  ? 384  LYS   B CA  1 
ATOM   2623  C  C   . LYS   A 1 384  ? 123.928 92.969  121.670 1.00 87.83  ? 384  LYS   B C   1 
ATOM   2624  O  O   . LYS   A 1 384  ? 123.186 93.703  121.011 1.00 88.90  ? 384  LYS   B O   1 
ATOM   2625  C  CB  . LYS   A 1 384  ? 123.522 90.653  120.799 1.00 84.29  ? 384  LYS   B CB  1 
ATOM   2626  C  CG  . LYS   A 1 384  ? 122.365 90.876  119.836 1.00 89.38  ? 384  LYS   B CG  1 
ATOM   2627  C  CD  . LYS   A 1 384  ? 122.421 89.898  118.672 1.00 90.04  ? 384  LYS   B CD  1 
ATOM   2628  C  CE  . LYS   A 1 384  ? 121.232 90.076  117.740 1.00 87.65  ? 384  LYS   B CE  1 
ATOM   2629  N  NZ  . LYS   A 1 384  ? 121.274 89.125  116.594 1.00 87.70  ? 384  LYS   B NZ  1 
ATOM   2630  N  N   . LEU   A 1 385  ? 125.122 93.347  122.114 1.00 87.89  ? 385  LEU   B N   1 
ATOM   2631  C  CA  . LEU   A 1 385  ? 125.649 94.666  121.802 1.00 86.92  ? 385  LEU   B CA  1 
ATOM   2632  C  C   . LEU   A 1 385  ? 126.136 94.714  120.361 1.00 86.08  ? 385  LEU   B C   1 
ATOM   2633  O  O   . LEU   A 1 385  ? 126.732 93.759  119.857 1.00 86.16  ? 385  LEU   B O   1 
ATOM   2634  C  CB  . LEU   A 1 385  ? 126.789 95.024  122.755 1.00 88.85  ? 385  LEU   B CB  1 
ATOM   2635  C  CG  . LEU   A 1 385  ? 126.429 95.076  124.240 1.00 90.99  ? 385  LEU   B CG  1 
ATOM   2636  C  CD1 . LEU   A 1 385  ? 127.646 95.442  125.074 1.00 87.51  ? 385  LEU   B CD1 1 
ATOM   2637  C  CD2 . LEU   A 1 385  ? 125.294 96.059  124.482 1.00 88.05  ? 385  LEU   B CD2 1 
ATOM   2638  N  N   . GLY   A 1 386  ? 125.881 95.838  119.701 1.00 83.55  ? 386  GLY   B N   1 
ATOM   2639  C  CA  . GLY   A 1 386  ? 126.327 96.005  118.328 1.00 81.51  ? 386  GLY   B CA  1 
ATOM   2640  C  C   . GLY   A 1 386  ? 125.651 95.080  117.341 1.00 82.80  ? 386  GLY   B C   1 
ATOM   2641  O  O   . GLY   A 1 386  ? 126.316 94.526  116.457 1.00 85.22  ? 386  GLY   B O   1 
ATOM   2642  N  N   . ASP   A 1 387  ? 124.341 94.893  117.474 1.00 77.02  ? 387  ASP   B N   1 
ATOM   2643  C  CA  . ASP   A 1 387  ? 123.603 94.091  116.514 1.00 74.99  ? 387  ASP   B CA  1 
ATOM   2644  C  C   . ASP   A 1 387  ? 123.303 94.924  115.272 1.00 77.06  ? 387  ASP   B C   1 
ATOM   2645  O  O   . ASP   A 1 387  ? 123.672 96.095  115.171 1.00 81.60  ? 387  ASP   B O   1 
ATOM   2646  C  CB  . ASP   A 1 387  ? 122.324 93.543  117.142 1.00 76.94  ? 387  ASP   B CB  1 
ATOM   2647  C  CG  . ASP   A 1 387  ? 121.510 94.613  117.838 1.00 82.54  ? 387  ASP   B CG  1 
ATOM   2648  O  OD1 . ASP   A 1 387  ? 121.953 95.780  117.863 1.00 80.66  ? 387  ASP   B OD1 1 
ATOM   2649  O  OD2 . ASP   A 1 387  ? 120.425 94.284  118.363 1.00 83.52  ? 387  ASP   B OD2 1 
ATOM   2650  N  N   . MET   A 1 388  ? 122.637 94.307  114.299 1.00 63.86  ? 388  MET   B N   1 
ATOM   2651  C  CA  . MET   A 1 388  ? 122.302 94.984  113.058 1.00 65.66  ? 388  MET   B CA  1 
ATOM   2652  C  C   . MET   A 1 388  ? 120.877 94.724  112.598 1.00 64.72  ? 388  MET   B C   1 
ATOM   2653  O  O   . MET   A 1 388  ? 120.506 95.172  111.509 1.00 71.17  ? 388  MET   B O   1 
ATOM   2654  C  CB  . MET   A 1 388  ? 123.279 94.574  111.945 1.00 64.86  ? 388  MET   B CB  1 
ATOM   2655  C  CG  . MET   A 1 388  ? 124.710 95.015  112.188 1.00 65.91  ? 388  MET   B CG  1 
ATOM   2656  S  SD  . MET   A 1 388  ? 125.878 94.272  111.041 1.00 72.23  ? 388  MET   B SD  1 
ATOM   2657  C  CE  . MET   A 1 388  ? 125.199 94.816  109.480 1.00 70.40  ? 388  MET   B CE  1 
ATOM   2658  N  N   . SER   A 1 389  ? 120.071 94.020  113.388 1.00 59.24  ? 389  SER   B N   1 
ATOM   2659  C  CA  . SER   A 1 389  ? 118.695 93.732  113.019 1.00 61.64  ? 389  SER   B CA  1 
ATOM   2660  C  C   . SER   A 1 389  ? 117.723 94.825  113.440 1.00 65.87  ? 389  SER   B C   1 
ATOM   2661  O  O   . SER   A 1 389  ? 116.554 94.775  113.043 1.00 70.99  ? 389  SER   B O   1 
ATOM   2662  C  CB  . SER   A 1 389  ? 118.253 92.397  113.628 1.00 69.15  ? 389  SER   B CB  1 
ATOM   2663  O  OG  . SER   A 1 389  ? 116.917 92.091  113.268 1.00 71.31  ? 389  SER   B OG  1 
ATOM   2664  N  N   . LEU   A 1 390  ? 118.165 95.801  114.230 1.00 61.66  ? 390  LEU   B N   1 
ATOM   2665  C  CA  . LEU   A 1 390  ? 117.307 96.897  114.656 1.00 62.46  ? 390  LEU   B CA  1 
ATOM   2666  C  C   . LEU   A 1 390  ? 117.614 98.205  113.938 1.00 63.77  ? 390  LEU   B C   1 
ATOM   2667  O  O   . LEU   A 1 390  ? 117.106 99.255  114.343 1.00 69.81  ? 390  LEU   B O   1 
ATOM   2668  C  CB  . LEU   A 1 390  ? 117.397 97.086  116.173 1.00 62.74  ? 390  LEU   B CB  1 
ATOM   2669  C  CG  . LEU   A 1 390  ? 118.723 96.835  116.890 1.00 66.82  ? 390  LEU   B CG  1 
ATOM   2670  C  CD1 . LEU   A 1 390  ? 119.778 97.847  116.482 1.00 68.03  ? 390  LEU   B CD1 1 
ATOM   2671  C  CD2 . LEU   A 1 390  ? 118.507 96.866  118.392 1.00 64.65  ? 390  LEU   B CD2 1 
ATOM   2672  N  N   . LEU   A 1 391  ? 118.432 98.168  112.890 1.00 59.74  ? 391  LEU   B N   1 
ATOM   2673  C  CA  . LEU   A 1 391  ? 118.653 99.350  112.074 1.00 58.14  ? 391  LEU   B CA  1 
ATOM   2674  C  C   . LEU   A 1 391  ? 117.397 99.678  111.273 1.00 62.02  ? 391  LEU   B C   1 
ATOM   2675  O  O   . LEU   A 1 391  ? 116.507 98.844  111.090 1.00 66.00  ? 391  LEU   B O   1 
ATOM   2676  C  CB  . LEU   A 1 391  ? 119.838 99.142  111.133 1.00 54.11  ? 391  LEU   B CB  1 
ATOM   2677  C  CG  . LEU   A 1 391  ? 121.203 98.965  111.794 1.00 53.67  ? 391  LEU   B CG  1 
ATOM   2678  C  CD1 . LEU   A 1 391  ? 122.189 98.369  110.810 1.00 58.31  ? 391  LEU   B CD1 1 
ATOM   2679  C  CD2 . LEU   A 1 391  ? 121.713 100.288 112.314 1.00 59.14  ? 391  LEU   B CD2 1 
ATOM   2680  N  N   . SER   A 1 392  ? 117.333 100.923 110.797 1.00 59.49  ? 392  SER   B N   1 
ATOM   2681  C  CA  . SER   A 1 392  ? 116.139 101.385 110.098 1.00 58.30  ? 392  SER   B CA  1 
ATOM   2682  C  C   . SER   A 1 392  ? 115.895 100.590 108.823 1.00 62.45  ? 392  SER   B C   1 
ATOM   2683  O  O   . SER   A 1 392  ? 114.760 100.190 108.540 1.00 65.94  ? 392  SER   B O   1 
ATOM   2684  C  CB  . SER   A 1 392  ? 116.262 102.876 109.785 1.00 60.98  ? 392  SER   B CB  1 
ATOM   2685  O  OG  . SER   A 1 392  ? 116.388 103.638 110.972 1.00 64.95  ? 392  SER   B OG  1 
ATOM   2686  N  N   . TRP   A 1 393  ? 116.945 100.346 108.040 1.00 62.49  ? 393  TRP   B N   1 
ATOM   2687  C  CA  . TRP   A 1 393  ? 116.768 99.642  106.777 1.00 63.74  ? 393  TRP   B CA  1 
ATOM   2688  C  C   . TRP   A 1 393  ? 116.587 98.141  106.966 1.00 67.04  ? 393  TRP   B C   1 
ATOM   2689  O  O   . TRP   A 1 393  ? 115.954 97.491  106.127 1.00 67.05  ? 393  TRP   B O   1 
ATOM   2690  C  CB  . TRP   A 1 393  ? 117.946 99.928  105.843 1.00 62.63  ? 393  TRP   B CB  1 
ATOM   2691  C  CG  . TRP   A 1 393  ? 119.295 99.750  106.463 1.00 57.83  ? 393  TRP   B CG  1 
ATOM   2692  C  CD1 . TRP   A 1 393  ? 120.032 98.609  106.500 1.00 56.77  ? 393  TRP   B CD1 1 
ATOM   2693  C  CD2 . TRP   A 1 393  ? 120.078 100.755 107.116 1.00 58.72  ? 393  TRP   B CD2 1 
ATOM   2694  N  NE1 . TRP   A 1 393  ? 121.221 98.833  107.144 1.00 59.16  ? 393  TRP   B NE1 1 
ATOM   2695  C  CE2 . TRP   A 1 393  ? 121.274 100.145 107.532 1.00 56.96  ? 393  TRP   B CE2 1 
ATOM   2696  C  CE3 . TRP   A 1 393  ? 119.881 102.110 107.395 1.00 64.44  ? 393  TRP   B CE3 1 
ATOM   2697  C  CZ2 . TRP   A 1 393  ? 122.269 100.842 108.210 1.00 58.41  ? 393  TRP   B CZ2 1 
ATOM   2698  C  CZ3 . TRP   A 1 393  ? 120.871 102.798 108.068 1.00 62.64  ? 393  TRP   B CZ3 1 
ATOM   2699  C  CH2 . TRP   A 1 393  ? 122.047 102.163 108.469 1.00 60.27  ? 393  TRP   B CH2 1 
ATOM   2700  N  N   . ASN   A 1 394  ? 117.123 97.574  108.043 1.00 69.07  ? 394  ASN   B N   1 
ATOM   2701  C  CA  . ASN   A 1 394  ? 116.998 96.139  108.304 1.00 66.40  ? 394  ASN   B CA  1 
ATOM   2702  C  C   . ASN   A 1 394  ? 115.781 95.823  109.169 1.00 70.82  ? 394  ASN   B C   1 
ATOM   2703  O  O   . ASN   A 1 394  ? 115.876 95.126  110.178 1.00 74.11  ? 394  ASN   B O   1 
ATOM   2704  C  CB  . ASN   A 1 394  ? 118.274 95.618  108.952 1.00 68.48  ? 394  ASN   B CB  1 
ATOM   2705  C  CG  . ASN   A 1 394  ? 119.481 95.759  108.054 1.00 72.86  ? 394  ASN   B CG  1 
ATOM   2706  O  OD1 . ASN   A 1 394  ? 119.376 95.646  106.834 1.00 76.80  ? 394  ASN   B OD1 1 
ATOM   2707  N  ND2 . ASN   A 1 394  ? 120.638 96.011  108.653 1.00 74.72  ? 394  ASN   B ND2 1 
ATOM   2708  N  N   . GLN   A 1 395  ? 114.619 96.331  108.769 1.00 82.20  ? 395  GLN   B N   1 
ATOM   2709  C  CA  . GLN   A 1 395  ? 113.366 96.069  109.459 1.00 84.08  ? 395  GLN   B CA  1 
ATOM   2710  C  C   . GLN   A 1 395  ? 112.252 95.988  108.430 1.00 87.39  ? 395  GLN   B C   1 
ATOM   2711  O  O   . GLN   A 1 395  ? 112.366 96.583  107.351 1.00 87.64  ? 395  GLN   B O   1 
ATOM   2712  C  CB  . GLN   A 1 395  ? 113.050 97.156  110.497 1.00 82.10  ? 395  GLN   B CB  1 
ATOM   2713  C  CG  . GLN   A 1 395  ? 113.850 97.038  111.781 1.00 82.25  ? 395  GLN   B CG  1 
ATOM   2714  C  CD  . GLN   A 1 395  ? 113.442 98.065  112.813 1.00 85.23  ? 395  GLN   B CD  1 
ATOM   2715  O  OE1 . GLN   A 1 395  ? 112.614 98.935  112.545 1.00 86.38  ? 395  GLN   B OE1 1 
ATOM   2716  N  NE2 . GLN   A 1 395  ? 114.021 97.969  114.004 1.00 82.96  ? 395  GLN   B NE2 1 
ATOM   2717  N  N   . PRO   A 1 396  ? 111.175 95.257  108.720 1.00 93.23  ? 396  PRO   B N   1 
ATOM   2718  C  CA  . PRO   A 1 396  ? 110.057 95.189  107.772 1.00 92.56  ? 396  PRO   B CA  1 
ATOM   2719  C  C   . PRO   A 1 396  ? 109.418 96.555  107.567 1.00 95.49  ? 396  PRO   B C   1 
ATOM   2720  O  O   . PRO   A 1 396  ? 109.371 97.382  108.480 1.00 94.90  ? 396  PRO   B O   1 
ATOM   2721  C  CB  . PRO   A 1 396  ? 109.086 94.208  108.438 1.00 91.49  ? 396  PRO   B CB  1 
ATOM   2722  C  CG  . PRO   A 1 396  ? 109.933 93.408  109.371 1.00 90.52  ? 396  PRO   B CG  1 
ATOM   2723  C  CD  . PRO   A 1 396  ? 110.980 94.355  109.867 1.00 91.35  ? 396  PRO   B CD  1 
ATOM   2724  N  N   . ASN   A 1 397  ? 108.927 96.779  106.350 1.00 104.56 ? 397  ASN   B N   1 
ATOM   2725  C  CA  . ASN   A 1 397  ? 108.287 98.036  105.967 1.00 106.05 ? 397  ASN   B CA  1 
ATOM   2726  C  C   . ASN   A 1 397  ? 109.206 99.230  106.207 1.00 105.82 ? 397  ASN   B C   1 
ATOM   2727  O  O   . ASN   A 1 397  ? 110.413 99.150  105.982 1.00 103.45 ? 397  ASN   B O   1 
ATOM   2728  C  CB  . ASN   A 1 397  ? 106.969 98.225  106.725 1.00 106.13 ? 397  ASN   B CB  1 
ATOM   2729  C  CG  . ASN   A 1 397  ? 106.280 99.531  106.383 1.00 106.68 ? 397  ASN   B CG  1 
ATOM   2730  O  OD1 . ASN   A 1 397  ? 106.487 100.548 107.045 1.00 105.66 ? 397  ASN   B OD1 1 
ATOM   2731  N  ND2 . ASN   A 1 397  ? 105.455 99.511  105.342 1.00 106.33 ? 397  ASN   B ND2 1 
ATOM   2732  N  N   . PRO   B 2 44   ? 113.954 151.737 82.870  1.00 110.19 ? 44   PRO   A N   1 
ATOM   2733  C  CA  . PRO   B 2 44   ? 113.512 153.135 82.872  1.00 110.72 ? 44   PRO   A CA  1 
ATOM   2734  C  C   . PRO   B 2 44   ? 113.294 153.691 81.468  1.00 110.19 ? 44   PRO   A C   1 
ATOM   2735  O  O   . PRO   B 2 44   ? 112.804 152.981 80.591  1.00 108.87 ? 44   PRO   A O   1 
ATOM   2736  C  CB  . PRO   B 2 44   ? 114.664 153.865 83.573  1.00 109.27 ? 44   PRO   A CB  1 
ATOM   2737  C  CG  . PRO   B 2 44   ? 115.847 152.979 83.383  1.00 109.35 ? 44   PRO   A CG  1 
ATOM   2738  C  CD  . PRO   B 2 44   ? 115.305 151.585 83.435  1.00 108.40 ? 44   PRO   A CD  1 
ATOM   2739  N  N   . VAL   B 2 45   ? 113.651 154.955 81.267  1.00 114.07 ? 45   VAL   A N   1 
ATOM   2740  C  CA  . VAL   B 2 45   ? 113.487 155.618 79.977  1.00 115.28 ? 45   VAL   A CA  1 
ATOM   2741  C  C   . VAL   B 2 45   ? 114.584 155.150 79.027  1.00 115.00 ? 45   VAL   A C   1 
ATOM   2742  O  O   . VAL   B 2 45   ? 115.624 154.653 79.484  1.00 113.24 ? 45   VAL   A O   1 
ATOM   2743  C  CB  . VAL   B 2 45   ? 113.503 157.147 80.135  1.00 113.88 ? 45   VAL   A CB  1 
ATOM   2744  C  CG1 . VAL   B 2 45   ? 112.355 157.601 81.023  1.00 111.90 ? 45   VAL   A CG1 1 
ATOM   2745  C  CG2 . VAL   B 2 45   ? 114.837 157.608 80.703  1.00 111.97 ? 45   VAL   A CG2 1 
ATOM   2746  N  N   . PRO   B 2 46   ? 114.396 155.270 77.714  1.00 103.64 ? 46   PRO   A N   1 
ATOM   2747  C  CA  . PRO   B 2 46   ? 115.484 154.966 76.777  1.00 100.19 ? 46   PRO   A CA  1 
ATOM   2748  C  C   . PRO   B 2 46   ? 116.678 155.882 77.001  1.00 101.25 ? 46   PRO   A C   1 
ATOM   2749  O  O   . PRO   B 2 46   ? 116.568 156.994 77.521  1.00 100.76 ? 46   PRO   A O   1 
ATOM   2750  C  CB  . PRO   B 2 46   ? 114.845 155.195 75.405  1.00 98.55  ? 46   PRO   A CB  1 
ATOM   2751  C  CG  . PRO   B 2 46   ? 113.392 154.977 75.633  1.00 99.27  ? 46   PRO   A CG  1 
ATOM   2752  C  CD  . PRO   B 2 46   ? 113.119 155.497 77.015  1.00 100.83 ? 46   PRO   A CD  1 
ATOM   2753  N  N   . ARG   B 2 47   ? 117.847 155.391 76.591  1.00 97.10  ? 47   ARG   A N   1 
ATOM   2754  C  CA  . ARG   B 2 47   ? 119.112 156.050 76.902  1.00 96.81  ? 47   ARG   A CA  1 
ATOM   2755  C  C   . ARG   B 2 47   ? 119.437 157.184 75.931  1.00 97.39  ? 47   ARG   A C   1 
ATOM   2756  O  O   . ARG   B 2 47   ? 119.626 158.329 76.353  1.00 99.48  ? 47   ARG   A O   1 
ATOM   2757  C  CB  . ARG   B 2 47   ? 120.238 155.014 76.915  1.00 95.92  ? 47   ARG   A CB  1 
ATOM   2758  C  CG  . ARG   B 2 47   ? 120.052 153.950 77.966  1.00 95.55  ? 47   ARG   A CG  1 
ATOM   2759  C  CD  . ARG   B 2 47   ? 121.108 152.881 77.855  1.00 95.03  ? 47   ARG   A CD  1 
ATOM   2760  N  NE  . ARG   B 2 47   ? 121.152 152.065 79.060  1.00 98.22  ? 47   ARG   A NE  1 
ATOM   2761  C  CZ  . ARG   B 2 47   ? 121.852 152.377 80.140  1.00 100.80 ? 47   ARG   A CZ  1 
ATOM   2762  N  NH1 . ARG   B 2 47   ? 122.578 153.479 80.195  1.00 99.60  ? 47   ARG   A NH1 1 
ATOM   2763  N  NH2 . ARG   B 2 47   ? 121.821 151.565 81.190  1.00 99.70  ? 47   ARG   A NH2 1 
ATOM   2764  N  N   . SER   B 2 48   ? 119.513 156.875 74.636  1.00 108.14 ? 48   SER   A N   1 
ATOM   2765  C  CA  . SER   B 2 48   ? 119.898 157.839 73.604  1.00 110.70 ? 48   SER   A CA  1 
ATOM   2766  C  C   . SER   B 2 48   ? 121.290 158.415 73.883  1.00 110.17 ? 48   SER   A C   1 
ATOM   2767  O  O   . SER   B 2 48   ? 121.463 159.602 74.166  1.00 112.12 ? 48   SER   A O   1 
ATOM   2768  C  CB  . SER   B 2 48   ? 118.850 158.949 73.468  1.00 108.82 ? 48   SER   A CB  1 
ATOM   2769  O  OG  . SER   B 2 48   ? 117.606 158.423 73.042  1.00 107.64 ? 48   SER   A OG  1 
ATOM   2770  N  N   . VAL   B 2 49   ? 122.285 157.536 73.805  1.00 101.56 ? 49   VAL   A N   1 
ATOM   2771  C  CA  . VAL   B 2 49   ? 123.681 157.878 74.057  1.00 101.22 ? 49   VAL   A CA  1 
ATOM   2772  C  C   . VAL   B 2 49   ? 124.296 158.466 72.793  1.00 100.02 ? 49   VAL   A C   1 
ATOM   2773  O  O   . VAL   B 2 49   ? 123.933 158.098 71.672  1.00 100.81 ? 49   VAL   A O   1 
ATOM   2774  C  CB  . VAL   B 2 49   ? 124.450 156.633 74.548  1.00 101.93 ? 49   VAL   A CB  1 
ATOM   2775  C  CG1 . VAL   B 2 49   ? 124.332 155.500 73.540  1.00 101.54 ? 49   VAL   A CG1 1 
ATOM   2776  C  CG2 . VAL   B 2 49   ? 125.908 156.965 74.833  1.00 100.80 ? 49   VAL   A CG2 1 
ATOM   2777  N  N   . PHE   B 2 50   ? 125.232 159.400 72.969  1.00 104.17 ? 50   PHE   A N   1 
ATOM   2778  C  CA  . PHE   B 2 50   ? 125.901 160.073 71.863  1.00 105.43 ? 50   PHE   A CA  1 
ATOM   2779  C  C   . PHE   B 2 50   ? 127.413 159.932 71.997  1.00 108.82 ? 50   PHE   A C   1 
ATOM   2780  O  O   . PHE   B 2 50   ? 127.958 160.022 73.102  1.00 109.66 ? 50   PHE   A O   1 
ATOM   2781  C  CB  . PHE   B 2 50   ? 125.519 161.552 71.813  1.00 107.30 ? 50   PHE   A CB  1 
ATOM   2782  C  CG  . PHE   B 2 50   ? 124.058 161.806 72.040  1.00 109.00 ? 50   PHE   A CG  1 
ATOM   2783  C  CD1 . PHE   B 2 50   ? 123.127 161.495 71.064  1.00 108.26 ? 50   PHE   A CD1 1 
ATOM   2784  C  CD2 . PHE   B 2 50   ? 123.615 162.359 73.229  1.00 110.34 ? 50   PHE   A CD2 1 
ATOM   2785  C  CE1 . PHE   B 2 50   ? 121.783 161.728 71.271  1.00 108.22 ? 50   PHE   A CE1 1 
ATOM   2786  C  CE2 . PHE   B 2 50   ? 122.271 162.596 73.441  1.00 111.42 ? 50   PHE   A CE2 1 
ATOM   2787  C  CZ  . PHE   B 2 50   ? 121.354 162.280 72.460  1.00 109.19 ? 50   PHE   A CZ  1 
ATOM   2788  N  N   . ILE   B 2 51   ? 128.084 159.712 70.866  1.00 102.92 ? 51   ILE   A N   1 
ATOM   2789  C  CA  . ILE   B 2 51   ? 129.537 159.570 70.804  1.00 100.70 ? 51   ILE   A CA  1 
ATOM   2790  C  C   . ILE   B 2 51   ? 130.094 160.697 69.948  1.00 101.52 ? 51   ILE   A C   1 
ATOM   2791  O  O   . ILE   B 2 51   ? 129.612 160.933 68.833  1.00 101.01 ? 51   ILE   A O   1 
ATOM   2792  C  CB  . ILE   B 2 51   ? 129.957 158.198 70.241  1.00 97.06  ? 51   ILE   A CB  1 
ATOM   2793  C  CG1 . ILE   B 2 51   ? 130.195 157.198 71.370  1.00 100.12 ? 51   ILE   A CG1 1 
ATOM   2794  C  CG2 . ILE   B 2 51   ? 131.217 158.315 69.395  1.00 97.87  ? 51   ILE   A CG2 1 
ATOM   2795  C  CD1 . ILE   B 2 51   ? 130.503 155.803 70.875  1.00 99.87  ? 51   ILE   A CD1 1 
ATOM   2796  N  N   . ASN   B 2 52   ? 131.099 161.399 70.478  1.00 111.62 ? 52   ASN   A N   1 
ATOM   2797  C  CA  . ASN   B 2 52   ? 131.788 162.473 69.760  1.00 110.85 ? 52   ASN   A CA  1 
ATOM   2798  C  C   . ASN   B 2 52   ? 130.802 163.528 69.264  1.00 109.77 ? 52   ASN   A C   1 
ATOM   2799  O  O   . ASN   B 2 52   ? 130.975 164.117 68.196  1.00 111.01 ? 52   ASN   A O   1 
ATOM   2800  C  CB  . ASN   B 2 52   ? 132.624 161.917 68.605  1.00 112.37 ? 52   ASN   A CB  1 
ATOM   2801  C  CG  . ASN   B 2 52   ? 133.685 162.890 68.129  1.00 113.71 ? 52   ASN   A CG  1 
ATOM   2802  O  OD1 . ASN   B 2 52   ? 134.067 163.811 68.852  1.00 112.30 ? 52   ASN   A OD1 1 
ATOM   2803  N  ND2 . ASN   B 2 52   ? 134.167 162.691 66.908  1.00 113.15 ? 52   ASN   A ND2 1 
ATOM   2804  N  N   . GLU   B 2 53   ? 129.753 163.766 70.048  1.00 123.83 ? 53   GLU   A N   1 
ATOM   2805  C  CA  . GLU   B 2 53   ? 128.720 164.725 69.708  1.00 127.15 ? 53   GLU   A CA  1 
ATOM   2806  C  C   . GLU   B 2 53   ? 128.402 165.549 70.947  1.00 129.48 ? 53   GLU   A C   1 
ATOM   2807  O  O   . GLU   B 2 53   ? 128.269 164.988 72.046  1.00 127.40 ? 53   GLU   A O   1 
ATOM   2808  C  CB  . GLU   B 2 53   ? 127.453 164.024 69.192  1.00 126.04 ? 53   GLU   A CB  1 
ATOM   2809  C  CG  . GLU   B 2 53   ? 126.425 164.950 68.563  1.00 127.44 ? 53   GLU   A CG  1 
ATOM   2810  C  CD  . GLU   B 2 53   ? 125.273 165.262 69.495  1.00 127.64 ? 53   GLU   A CD  1 
ATOM   2811  O  OE1 . GLU   B 2 53   ? 125.142 164.575 70.531  1.00 127.05 ? 53   GLU   A OE1 1 
ATOM   2812  O  OE2 . GLU   B 2 53   ? 124.498 166.193 69.193  1.00 127.46 ? 53   GLU   A OE2 1 
ATOM   2813  N  N   . PRO   B 2 54   ? 128.294 166.871 70.811  1.00 140.20 ? 54   PRO   A N   1 
ATOM   2814  C  CA  . PRO   B 2 54   ? 128.010 167.711 71.981  1.00 138.21 ? 54   PRO   A CA  1 
ATOM   2815  C  C   . PRO   B 2 54   ? 126.682 167.343 72.626  1.00 139.63 ? 54   PRO   A C   1 
ATOM   2816  O  O   . PRO   B 2 54   ? 125.719 166.980 71.947  1.00 139.90 ? 54   PRO   A O   1 
ATOM   2817  C  CB  . PRO   B 2 54   ? 127.979 169.129 71.399  1.00 137.53 ? 54   PRO   A CB  1 
ATOM   2818  C  CG  . PRO   B 2 54   ? 128.801 169.044 70.155  1.00 137.98 ? 54   PRO   A CG  1 
ATOM   2819  C  CD  . PRO   B 2 54   ? 128.549 167.672 69.602  1.00 138.12 ? 54   PRO   A CD  1 
ATOM   2820  N  N   . LEU   B 2 55   ? 126.643 167.439 73.950  1.00 143.87 ? 55   LEU   A N   1 
ATOM   2821  C  CA  . LEU   B 2 55   ? 125.445 167.064 74.685  1.00 143.68 ? 55   LEU   A CA  1 
ATOM   2822  C  C   . LEU   B 2 55   ? 124.293 167.997 74.318  1.00 144.38 ? 55   LEU   A C   1 
ATOM   2823  O  O   . LEU   B 2 55   ? 124.498 169.206 74.155  1.00 143.19 ? 55   LEU   A O   1 
ATOM   2824  C  CB  . LEU   B 2 55   ? 125.697 167.110 76.194  1.00 142.24 ? 55   LEU   A CB  1 
ATOM   2825  C  CG  . LEU   B 2 55   ? 126.533 165.993 76.829  1.00 142.44 ? 55   LEU   A CG  1 
ATOM   2826  C  CD1 . LEU   B 2 55   ? 128.021 166.163 76.545  1.00 141.95 ? 55   LEU   A CD1 1 
ATOM   2827  C  CD2 . LEU   B 2 55   ? 126.277 165.922 78.328  1.00 141.44 ? 55   LEU   A CD2 1 
ATOM   2828  N  N   . PRO   B 2 56   ? 123.073 167.475 74.178  1.00 147.02 ? 56   PRO   A N   1 
ATOM   2829  C  CA  . PRO   B 2 56   ? 121.938 168.333 73.812  1.00 146.78 ? 56   PRO   A CA  1 
ATOM   2830  C  C   . PRO   B 2 56   ? 121.515 169.259 74.940  1.00 147.39 ? 56   PRO   A C   1 
ATOM   2831  O  O   . PRO   B 2 56   ? 122.140 169.282 76.006  1.00 146.67 ? 56   PRO   A O   1 
ATOM   2832  C  CB  . PRO   B 2 56   ? 120.836 167.323 73.469  1.00 144.84 ? 56   PRO   A CB  1 
ATOM   2833  C  CG  . PRO   B 2 56   ? 121.178 166.118 74.276  1.00 144.06 ? 56   PRO   A CG  1 
ATOM   2834  C  CD  . PRO   B 2 56   ? 122.681 166.062 74.315  1.00 144.35 ? 56   PRO   A CD  1 
ATOM   2835  N  N   . SER   B 2 57   ? 120.453 170.027 74.714  1.00 157.15 ? 57   SER   A N   1 
ATOM   2836  C  CA  . SER   B 2 57   ? 119.968 170.963 75.715  1.00 157.08 ? 57   SER   A CA  1 
ATOM   2837  C  C   . SER   B 2 57   ? 119.409 170.213 76.925  1.00 156.94 ? 57   SER   A C   1 
ATOM   2838  O  O   . SER   B 2 57   ? 119.253 168.988 76.919  1.00 155.36 ? 57   SER   A O   1 
ATOM   2839  C  CB  . SER   B 2 57   ? 118.903 171.882 75.119  1.00 156.18 ? 57   SER   A CB  1 
ATOM   2840  O  OG  . SER   B 2 57   ? 118.423 172.801 76.084  1.00 155.50 ? 57   SER   A OG  1 
ATOM   2841  N  N   . GLU   B 2 58   ? 119.122 170.976 77.980  1.00 168.15 ? 58   GLU   A N   1 
ATOM   2842  C  CA  . GLU   B 2 58   ? 118.586 170.514 79.259  1.00 168.39 ? 58   GLU   A CA  1 
ATOM   2843  C  C   . GLU   B 2 58   ? 119.583 169.662 80.037  1.00 168.85 ? 58   GLU   A C   1 
ATOM   2844  O  O   . GLU   B 2 58   ? 119.253 169.207 81.140  1.00 169.27 ? 58   GLU   A O   1 
ATOM   2845  C  CB  . GLU   B 2 58   ? 117.271 169.734 79.094  1.00 167.62 ? 58   GLU   A CB  1 
ATOM   2846  C  CG  . GLU   B 2 58   ? 116.333 169.808 80.290  1.00 168.49 ? 58   GLU   A CG  1 
ATOM   2847  C  CD  . GLU   B 2 58   ? 115.060 169.012 80.080  1.00 168.33 ? 58   GLU   A CD  1 
ATOM   2848  O  OE1 . GLU   B 2 58   ? 114.912 168.397 79.003  1.00 167.64 ? 58   GLU   A OE1 1 
ATOM   2849  O  OE2 . GLU   B 2 58   ? 114.207 169.000 80.992  1.00 168.29 ? 58   GLU   A OE2 1 
ATOM   2850  N  N   . TYR   B 2 59   ? 120.793 169.455 79.515  1.00 168.83 ? 59   TYR   A N   1 
ATOM   2851  C  CA  . TYR   B 2 59   ? 121.845 168.641 80.138  1.00 168.73 ? 59   TYR   A CA  1 
ATOM   2852  C  C   . TYR   B 2 59   ? 121.323 167.377 80.820  1.00 168.72 ? 59   TYR   A C   1 
ATOM   2853  O  O   . TYR   B 2 59   ? 121.876 166.291 80.642  1.00 168.24 ? 59   TYR   A O   1 
ATOM   2854  C  CB  . TYR   B 2 59   ? 122.653 169.479 81.141  1.00 168.57 ? 59   TYR   A CB  1 
ATOM   2855  C  CG  . TYR   B 2 59   ? 121.850 170.107 82.261  1.00 169.01 ? 59   TYR   A CG  1 
ATOM   2856  C  CD1 . TYR   B 2 59   ? 121.555 169.394 83.417  1.00 168.55 ? 59   TYR   A CD1 1 
ATOM   2857  C  CD2 . TYR   B 2 59   ? 121.399 171.418 82.167  1.00 168.74 ? 59   TYR   A CD2 1 
ATOM   2858  C  CE1 . TYR   B 2 59   ? 120.825 169.966 84.442  1.00 168.63 ? 59   TYR   A CE1 1 
ATOM   2859  C  CE2 . TYR   B 2 59   ? 120.668 171.997 83.187  1.00 168.85 ? 59   TYR   A CE2 1 
ATOM   2860  C  CZ  . TYR   B 2 59   ? 120.385 171.267 84.322  1.00 169.34 ? 59   TYR   A CZ  1 
ATOM   2861  O  OH  . TYR   B 2 59   ? 119.658 171.840 85.340  1.00 169.08 ? 59   TYR   A OH  1 
ATOM   2862  N  N   . HIS   B 2 70   ? 125.700 163.173 87.199  1.00 115.47 ? 70   HIS   A N   1 
ATOM   2863  C  CA  . HIS   B 2 70   ? 124.736 162.247 86.618  1.00 115.53 ? 70   HIS   A CA  1 
ATOM   2864  C  C   . HIS   B 2 70   ? 125.330 161.449 85.459  1.00 116.23 ? 70   HIS   A C   1 
ATOM   2865  O  O   . HIS   B 2 70   ? 125.874 162.019 84.514  1.00 117.25 ? 70   HIS   A O   1 
ATOM   2866  C  CB  . HIS   B 2 70   ? 123.499 163.002 86.134  1.00 115.37 ? 70   HIS   A CB  1 
ATOM   2867  C  CG  . HIS   B 2 70   ? 122.621 162.195 85.231  1.00 117.69 ? 70   HIS   A CG  1 
ATOM   2868  N  ND1 . HIS   B 2 70   ? 122.041 161.008 85.624  1.00 116.74 ? 70   HIS   A ND1 1 
ATOM   2869  C  CD2 . HIS   B 2 70   ? 122.229 162.400 83.952  1.00 116.72 ? 70   HIS   A CD2 1 
ATOM   2870  C  CE1 . HIS   B 2 70   ? 121.329 160.517 84.625  1.00 115.13 ? 70   HIS   A CE1 1 
ATOM   2871  N  NE2 . HIS   B 2 70   ? 121.427 161.343 83.599  1.00 114.94 ? 70   HIS   A NE2 1 
ATOM   2872  N  N   . HIS   B 2 71   ? 125.213 160.123 85.528  1.00 111.34 ? 71   HIS   A N   1 
ATOM   2873  C  CA  . HIS   B 2 71   ? 125.682 159.247 84.460  1.00 112.40 ? 71   HIS   A CA  1 
ATOM   2874  C  C   . HIS   B 2 71   ? 124.645 158.157 84.238  1.00 111.67 ? 71   HIS   A C   1 
ATOM   2875  O  O   . HIS   B 2 71   ? 123.555 158.174 84.820  1.00 111.57 ? 71   HIS   A O   1 
ATOM   2876  C  CB  . HIS   B 2 71   ? 127.062 158.661 84.785  1.00 112.20 ? 71   HIS   A CB  1 
ATOM   2877  C  CG  . HIS   B 2 71   ? 128.176 159.655 84.703  1.00 114.17 ? 71   HIS   A CG  1 
ATOM   2878  N  ND1 . HIS   B 2 71   ? 128.747 160.036 83.508  1.00 112.84 ? 71   HIS   A ND1 1 
ATOM   2879  C  CD2 . HIS   B 2 71   ? 128.827 160.344 85.669  1.00 111.88 ? 71   HIS   A CD2 1 
ATOM   2880  C  CE1 . HIS   B 2 71   ? 129.700 160.921 83.742  1.00 111.06 ? 71   HIS   A CE1 1 
ATOM   2881  N  NE2 . HIS   B 2 71   ? 129.769 161.126 85.045  1.00 112.23 ? 71   HIS   A NE2 1 
ATOM   2882  N  N   . PHE   B 2 72   ? 124.992 157.179 83.400  1.00 100.37 ? 72   PHE   A N   1 
ATOM   2883  C  CA  . PHE   B 2 72   ? 124.010 156.170 83.004  1.00 99.64  ? 72   PHE   A CA  1 
ATOM   2884  C  C   . PHE   B 2 72   ? 123.868 155.100 84.086  1.00 99.96  ? 72   PHE   A C   1 
ATOM   2885  O  O   . PHE   B 2 72   ? 122.794 154.933 84.671  1.00 98.86  ? 72   PHE   A O   1 
ATOM   2886  C  CB  . PHE   B 2 72   ? 124.408 155.576 81.648  1.00 96.92  ? 72   PHE   A CB  1 
ATOM   2887  C  CG  . PHE   B 2 72   ? 124.352 156.561 80.500  1.00 96.45  ? 72   PHE   A CG  1 
ATOM   2888  C  CD1 . PHE   B 2 72   ? 123.157 156.818 79.841  1.00 97.05  ? 72   PHE   A CD1 1 
ATOM   2889  C  CD2 . PHE   B 2 72   ? 125.498 157.213 80.066  1.00 98.51  ? 72   PHE   A CD2 1 
ATOM   2890  C  CE1 . PHE   B 2 72   ? 123.105 157.720 78.780  1.00 99.82  ? 72   PHE   A CE1 1 
ATOM   2891  C  CE2 . PHE   B 2 72   ? 125.451 158.116 79.005  1.00 99.53  ? 72   PHE   A CE2 1 
ATOM   2892  C  CZ  . PHE   B 2 72   ? 124.252 158.367 78.364  1.00 100.17 ? 72   PHE   A CZ  1 
ATOM   2893  N  N   . ALA   B 2 73   ? 124.952 154.378 84.389  1.00 91.79  ? 73   ALA   A N   1 
ATOM   2894  C  CA  . ALA   B 2 73   ? 124.878 153.353 85.425  1.00 90.12  ? 73   ALA   A CA  1 
ATOM   2895  C  C   . ALA   B 2 73   ? 126.202 153.099 86.138  1.00 89.95  ? 73   ALA   A C   1 
ATOM   2896  O  O   . ALA   B 2 73   ? 126.312 152.096 86.855  1.00 90.40  ? 73   ALA   A O   1 
ATOM   2897  C  CB  . ALA   B 2 73   ? 124.354 152.038 84.843  1.00 88.56  ? 73   ALA   A CB  1 
ATOM   2898  N  N   . THR   B 2 74   ? 127.193 153.971 85.980  1.00 93.66  ? 74   THR   A N   1 
ATOM   2899  C  CA  . THR   B 2 74   ? 128.538 153.816 86.560  1.00 94.56  ? 74   THR   A CA  1 
ATOM   2900  C  C   . THR   B 2 74   ? 129.104 152.482 86.075  1.00 92.25  ? 74   THR   A C   1 
ATOM   2901  O  O   . THR   B 2 74   ? 129.009 152.182 84.874  1.00 93.24  ? 74   THR   A O   1 
ATOM   2902  C  CB  . THR   B 2 74   ? 128.487 153.993 88.077  1.00 94.07  ? 74   THR   A CB  1 
ATOM   2903  O  OG1 . THR   B 2 74   ? 127.808 152.881 88.677  1.00 94.32  ? 74   THR   A OG1 1 
ATOM   2904  C  CG2 . THR   B 2 74   ? 127.764 155.284 88.440  1.00 93.08  ? 74   THR   A CG2 1 
ATOM   2905  N  N   . ASN   B 2 75   ? 129.679 151.661 86.945  1.00 89.01  ? 75   ASN   A N   1 
ATOM   2906  C  CA  . ASN   B 2 75   ? 130.358 150.431 86.559  1.00 84.91  ? 75   ASN   A CA  1 
ATOM   2907  C  C   . ASN   B 2 75   ? 130.488 149.566 87.808  1.00 88.92  ? 75   ASN   A C   1 
ATOM   2908  O  O   . ASN   B 2 75   ? 129.819 149.812 88.818  1.00 94.61  ? 75   ASN   A O   1 
ATOM   2909  C  CB  . ASN   B 2 75   ? 131.716 150.737 85.923  1.00 91.40  ? 75   ASN   A CB  1 
ATOM   2910  C  CG  . ASN   B 2 75   ? 132.424 151.886 86.607  1.00 95.93  ? 75   ASN   A CG  1 
ATOM   2911  O  OD1 . ASN   B 2 75   ? 132.850 151.772 87.756  1.00 93.99  ? 75   ASN   A OD1 1 
ATOM   2912  N  ND2 . ASN   B 2 75   ? 132.544 153.007 85.907  1.00 93.01  ? 75   ASN   A ND2 1 
ATOM   2913  N  N   . GLN   B 2 76   ? 131.339 148.540 87.728  1.00 82.85  ? 76   GLN   A N   1 
ATOM   2914  C  CA  . GLN   B 2 76   ? 131.662 147.647 88.841  1.00 85.58  ? 76   GLN   A CA  1 
ATOM   2915  C  C   . GLN   B 2 76   ? 130.505 146.714 89.172  1.00 85.18  ? 76   GLN   A C   1 
ATOM   2916  O  O   . GLN   B 2 76   ? 129.339 147.116 89.135  1.00 90.38  ? 76   GLN   A O   1 
ATOM   2917  C  CB  . GLN   B 2 76   ? 132.066 148.438 90.092  1.00 89.24  ? 76   GLN   A CB  1 
ATOM   2918  C  CG  . GLN   B 2 76   ? 133.297 149.311 89.925  1.00 89.65  ? 76   GLN   A CG  1 
ATOM   2919  C  CD  . GLN   B 2 76   ? 133.595 150.146 91.156  1.00 90.67  ? 76   GLN   A CD  1 
ATOM   2920  O  OE1 . GLN   B 2 76   ? 132.814 150.170 92.108  1.00 91.98  ? 76   GLN   A OE1 1 
ATOM   2921  N  NE2 . GLN   B 2 76   ? 134.731 150.835 91.144  1.00 88.82  ? 76   GLN   A NE2 1 
ATOM   2922  N  N   . ASN   B 2 77   ? 130.819 145.458 89.496  1.00 81.26  ? 77   ASN   A N   1 
ATOM   2923  C  CA  . ASN   B 2 77   ? 129.770 144.530 89.897  1.00 83.80  ? 77   ASN   A CA  1 
ATOM   2924  C  C   . ASN   B 2 77   ? 129.199 144.890 91.262  1.00 89.88  ? 77   ASN   A C   1 
ATOM   2925  O  O   . ASN   B 2 77   ? 127.993 144.737 91.485  1.00 92.77  ? 77   ASN   A O   1 
ATOM   2926  C  CB  . ASN   B 2 77   ? 130.300 143.097 89.907  1.00 84.88  ? 77   ASN   A CB  1 
ATOM   2927  C  CG  . ASN   B 2 77   ? 129.190 142.070 90.012  1.00 89.49  ? 77   ASN   A CG  1 
ATOM   2928  O  OD1 . ASN   B 2 77   ? 128.770 141.699 91.108  1.00 89.05  ? 77   ASN   A OD1 1 
ATOM   2929  N  ND2 . ASN   B 2 77   ? 128.705 141.607 88.866  1.00 89.04  ? 77   ASN   A ND2 1 
ATOM   2930  N  N   . VAL   B 2 78   ? 130.046 145.373 92.174  1.00 88.70  ? 78   VAL   A N   1 
ATOM   2931  C  CA  . VAL   B 2 78   ? 129.654 145.773 93.524  1.00 85.24  ? 78   VAL   A CA  1 
ATOM   2932  C  C   . VAL   B 2 78   ? 128.940 144.618 94.215  1.00 82.51  ? 78   VAL   A C   1 
ATOM   2933  O  O   . VAL   B 2 78   ? 127.748 144.705 94.528  1.00 84.43  ? 78   VAL   A O   1 
ATOM   2934  C  CB  . VAL   B 2 78   ? 128.778 147.040 93.506  1.00 87.52  ? 78   VAL   A CB  1 
ATOM   2935  C  CG1 . VAL   B 2 78   ? 128.703 147.655 94.896  1.00 85.59  ? 78   VAL   A CG1 1 
ATOM   2936  C  CG2 . VAL   B 2 78   ? 129.321 148.049 92.509  1.00 87.26  ? 78   VAL   A CG2 1 
ATOM   2937  N  N   . THR   B 2 79   ? 129.662 143.526 94.447  1.00 79.18  ? 79   THR   A N   1 
ATOM   2938  C  CA  . THR   B 2 79   ? 129.134 142.392 95.189  1.00 85.14  ? 79   THR   A CA  1 
ATOM   2939  C  C   . THR   B 2 79   ? 129.424 142.487 96.679  1.00 89.09  ? 79   THR   A C   1 
ATOM   2940  O  O   . THR   B 2 79   ? 129.085 141.564 97.425  1.00 89.42  ? 79   THR   A O   1 
ATOM   2941  C  CB  . THR   B 2 79   ? 129.703 141.080 94.640  1.00 86.56  ? 79   THR   A CB  1 
ATOM   2942  O  OG1 . THR   B 2 79   ? 129.065 139.974 95.289  1.00 87.10  ? 79   THR   A OG1 1 
ATOM   2943  C  CG2 . THR   B 2 79   ? 131.198 141.006 94.891  1.00 86.46  ? 79   THR   A CG2 1 
ATOM   2944  N  N   . SER   B 2 80   ? 130.046 143.575 97.125  1.00 91.53  ? 80   SER   A N   1 
ATOM   2945  C  CA  . SER   B 2 80   ? 130.359 143.755 98.535  1.00 90.36  ? 80   SER   A CA  1 
ATOM   2946  C  C   . SER   B 2 80   ? 129.096 144.095 99.313  1.00 90.45  ? 80   SER   A C   1 
ATOM   2947  O  O   . SER   B 2 80   ? 128.306 144.945 98.891  1.00 91.52  ? 80   SER   A O   1 
ATOM   2948  C  CB  . SER   B 2 80   ? 131.399 144.858 98.709  1.00 90.38  ? 80   SER   A CB  1 
ATOM   2949  O  OG  . SER   B 2 80   ? 130.925 146.089 98.191  1.00 89.73  ? 80   SER   A OG  1 
ATOM   2950  N  N   . LYS   B 2 81   ? 128.907 143.426 100.451 1.00 81.62  ? 81   LYS   A N   1 
ATOM   2951  C  CA  . LYS   B 2 81   ? 127.717 143.671 101.258 1.00 79.32  ? 81   LYS   A CA  1 
ATOM   2952  C  C   . LYS   B 2 81   ? 127.799 145.013 101.974 1.00 82.17  ? 81   LYS   A C   1 
ATOM   2953  O  O   . LYS   B 2 81   ? 126.806 145.747 102.042 1.00 86.07  ? 81   LYS   A O   1 
ATOM   2954  C  CB  . LYS   B 2 81   ? 127.525 142.536 102.262 1.00 82.06  ? 81   LYS   A CB  1 
ATOM   2955  C  CG  . LYS   B 2 81   ? 126.219 142.605 103.031 1.00 83.00  ? 81   LYS   A CG  1 
ATOM   2956  C  CD  . LYS   B 2 81   ? 126.095 141.445 104.002 1.00 84.43  ? 81   LYS   A CD  1 
ATOM   2957  C  CE  . LYS   B 2 81   ? 126.151 140.111 103.277 1.00 84.69  ? 81   LYS   A CE  1 
ATOM   2958  N  NZ  . LYS   B 2 81   ? 126.040 138.964 104.220 1.00 84.59  ? 81   LYS   A NZ  1 
ATOM   2959  N  N   . TYR   B 2 82   ? 128.968 145.352 102.507 1.00 77.52  ? 82   TYR   A N   1 
ATOM   2960  C  CA  . TYR   B 2 82   ? 129.166 146.578 103.264 1.00 73.12  ? 82   TYR   A CA  1 
ATOM   2961  C  C   . TYR   B 2 82   ? 129.928 147.601 102.434 1.00 72.67  ? 82   TYR   A C   1 
ATOM   2962  O  O   . TYR   B 2 82   ? 130.417 147.314 101.338 1.00 79.65  ? 82   TYR   A O   1 
ATOM   2963  C  CB  . TYR   B 2 82   ? 129.928 146.307 104.566 1.00 74.63  ? 82   TYR   A CB  1 
ATOM   2964  C  CG  . TYR   B 2 82   ? 129.390 145.151 105.375 1.00 75.75  ? 82   TYR   A CG  1 
ATOM   2965  C  CD1 . TYR   B 2 82   ? 128.218 145.275 106.103 1.00 76.47  ? 82   TYR   A CD1 1 
ATOM   2966  C  CD2 . TYR   B 2 82   ? 130.062 143.940 105.420 1.00 76.15  ? 82   TYR   A CD2 1 
ATOM   2967  C  CE1 . TYR   B 2 82   ? 127.725 144.225 106.844 1.00 78.79  ? 82   TYR   A CE1 1 
ATOM   2968  C  CE2 . TYR   B 2 82   ? 129.577 142.883 106.158 1.00 77.90  ? 82   TYR   A CE2 1 
ATOM   2969  C  CZ  . TYR   B 2 82   ? 128.407 143.032 106.869 1.00 80.15  ? 82   TYR   A CZ  1 
ATOM   2970  O  OH  . TYR   B 2 82   ? 127.916 141.982 107.609 1.00 83.18  ? 82   TYR   A OH  1 
ATOM   2971  N  N   . THR   B 2 83   ? 130.018 148.809 102.979 1.00 73.62  ? 83   THR   A N   1 
ATOM   2972  C  CA  . THR   B 2 83   ? 130.798 149.888 102.396 1.00 74.94  ? 83   THR   A CA  1 
ATOM   2973  C  C   . THR   B 2 83   ? 131.589 150.563 103.508 1.00 77.72  ? 83   THR   A C   1 
ATOM   2974  O  O   . THR   B 2 83   ? 131.208 150.516 104.680 1.00 84.26  ? 83   THR   A O   1 
ATOM   2975  C  CB  . THR   B 2 83   ? 129.901 150.908 101.677 1.00 78.05  ? 83   THR   A CB  1 
ATOM   2976  O  OG1 . THR   B 2 83   ? 128.897 150.215 100.925 1.00 80.64  ? 83   THR   A OG1 1 
ATOM   2977  C  CG2 . THR   B 2 83   ? 130.716 151.770 100.725 1.00 75.82  ? 83   THR   A CG2 1 
ATOM   2978  N  N   . VAL   B 2 84   ? 132.707 151.185 103.132 1.00 75.56  ? 84   VAL   A N   1 
ATOM   2979  C  CA  . VAL   B 2 84   ? 133.551 151.851 104.119 1.00 74.44  ? 84   VAL   A CA  1 
ATOM   2980  C  C   . VAL   B 2 84   ? 132.778 152.962 104.819 1.00 77.79  ? 84   VAL   A C   1 
ATOM   2981  O  O   . VAL   B 2 84   ? 132.935 153.184 106.026 1.00 78.79  ? 84   VAL   A O   1 
ATOM   2982  C  CB  . VAL   B 2 84   ? 134.838 152.377 103.454 1.00 76.77  ? 84   VAL   A CB  1 
ATOM   2983  C  CG1 . VAL   B 2 84   ? 134.510 153.193 102.212 1.00 79.26  ? 84   VAL   A CG1 1 
ATOM   2984  C  CG2 . VAL   B 2 84   ? 135.656 153.196 104.438 1.00 76.81  ? 84   VAL   A CG2 1 
ATOM   2985  N  N   . ILE   B 2 85   ? 131.923 153.668 104.079 1.00 89.26  ? 85   ILE   A N   1 
ATOM   2986  C  CA  . ILE   B 2 85   ? 131.128 154.737 104.674 1.00 88.50  ? 85   ILE   A CA  1 
ATOM   2987  C  C   . ILE   B 2 85   ? 130.094 154.164 105.635 1.00 84.54  ? 85   ILE   A C   1 
ATOM   2988  O  O   . ILE   B 2 85   ? 129.935 154.647 106.762 1.00 87.18  ? 85   ILE   A O   1 
ATOM   2989  C  CB  . ILE   B 2 85   ? 130.464 155.585 103.575 1.00 89.48  ? 85   ILE   A CB  1 
ATOM   2990  C  CG1 . ILE   B 2 85   ? 131.523 156.162 102.631 1.00 90.10  ? 85   ILE   A CG1 1 
ATOM   2991  C  CG2 . ILE   B 2 85   ? 129.633 156.698 104.192 1.00 86.25  ? 85   ILE   A CG2 1 
ATOM   2992  C  CD1 . ILE   B 2 85   ? 132.541 157.048 103.318 1.00 88.31  ? 85   ILE   A CD1 1 
ATOM   2993  N  N   . THR   B 2 86   ? 129.381 153.124 105.210 1.00 75.57  ? 86   THR   A N   1 
ATOM   2994  C  CA  . THR   B 2 86   ? 128.291 152.538 105.990 1.00 76.46  ? 86   THR   A CA  1 
ATOM   2995  C  C   . THR   B 2 86   ? 128.583 151.056 106.207 1.00 75.28  ? 86   THR   A C   1 
ATOM   2996  O  O   . THR   B 2 86   ? 128.097 150.198 105.469 1.00 76.28  ? 86   THR   A O   1 
ATOM   2997  C  CB  . THR   B 2 86   ? 126.940 152.745 105.288 1.00 81.23  ? 86   THR   A CB  1 
ATOM   2998  O  OG1 . THR   B 2 86   ? 126.921 152.005 104.062 1.00 81.88  ? 86   THR   A OG1 1 
ATOM   2999  C  CG2 . THR   B 2 86   ? 126.710 154.221 104.987 1.00 80.73  ? 86   THR   A CG2 1 
ATOM   3000  N  N   . PHE   B 2 87   ? 129.380 150.762 107.230 1.00 67.86  ? 87   PHE   A N   1 
ATOM   3001  C  CA  . PHE   B 2 87   ? 129.620 149.398 107.683 1.00 63.39  ? 87   PHE   A CA  1 
ATOM   3002  C  C   . PHE   B 2 87   ? 129.168 149.190 109.117 1.00 71.53  ? 87   PHE   A C   1 
ATOM   3003  O  O   . PHE   B 2 87   ? 128.488 148.197 109.416 1.00 75.02  ? 87   PHE   A O   1 
ATOM   3004  C  CB  . PHE   B 2 87   ? 131.109 149.051 107.550 1.00 64.92  ? 87   PHE   A CB  1 
ATOM   3005  C  CG  . PHE   B 2 87   ? 131.512 147.810 108.286 1.00 66.53  ? 87   PHE   A CG  1 
ATOM   3006  C  CD1 . PHE   B 2 87   ? 131.089 146.568 107.856 1.00 70.95  ? 87   PHE   A CD1 1 
ATOM   3007  C  CD2 . PHE   B 2 87   ? 132.329 147.883 109.398 1.00 67.59  ? 87   PHE   A CD2 1 
ATOM   3008  C  CE1 . PHE   B 2 87   ? 131.463 145.425 108.526 1.00 69.16  ? 87   PHE   A CE1 1 
ATOM   3009  C  CE2 . PHE   B 2 87   ? 132.707 146.741 110.070 1.00 67.06  ? 87   PHE   A CE2 1 
ATOM   3010  C  CZ  . PHE   B 2 87   ? 132.273 145.512 109.633 1.00 66.12  ? 87   PHE   A CZ  1 
ATOM   3011  N  N   . ILE   B 2 88   ? 129.529 150.112 110.012 1.00 73.01  ? 88   ILE   A N   1 
ATOM   3012  C  CA  . ILE   B 2 88   ? 129.110 150.000 111.408 1.00 67.53  ? 88   ILE   A CA  1 
ATOM   3013  C  C   . ILE   B 2 88   ? 127.593 149.963 111.557 1.00 69.08  ? 88   ILE   A C   1 
ATOM   3014  O  O   . ILE   B 2 88   ? 127.090 149.083 112.271 1.00 75.73  ? 88   ILE   A O   1 
ATOM   3015  C  CB  . ILE   B 2 88   ? 129.758 151.118 112.244 1.00 64.56  ? 88   ILE   A CB  1 
ATOM   3016  C  CG1 . ILE   B 2 88   ? 131.280 151.064 112.119 1.00 67.53  ? 88   ILE   A CG1 1 
ATOM   3017  C  CG2 . ILE   B 2 88   ? 129.343 151.005 113.701 1.00 69.62  ? 88   ILE   A CG2 1 
ATOM   3018  C  CD1 . ILE   B 2 88   ? 131.886 149.768 112.603 1.00 70.58  ? 88   ILE   A CD1 1 
ATOM   3019  N  N   . PRO   B 2 89   ? 126.813 150.858 110.933 1.00 58.53  ? 89   PRO   A N   1 
ATOM   3020  C  CA  . PRO   B 2 89   ? 125.356 150.803 111.156 1.00 60.06  ? 89   PRO   A CA  1 
ATOM   3021  C  C   . PRO   B 2 89   ? 124.709 149.506 110.698 1.00 63.36  ? 89   PRO   A C   1 
ATOM   3022  O  O   . PRO   B 2 89   ? 123.948 148.895 111.463 1.00 73.07  ? 89   PRO   A O   1 
ATOM   3023  C  CB  . PRO   B 2 89   ? 124.838 152.016 110.370 1.00 64.28  ? 89   PRO   A CB  1 
ATOM   3024  C  CG  . PRO   B 2 89   ? 125.898 152.323 109.388 1.00 70.28  ? 89   PRO   A CG  1 
ATOM   3025  C  CD  . PRO   B 2 89   ? 127.177 152.006 110.084 1.00 66.88  ? 89   PRO   A CD  1 
ATOM   3026  N  N   . LYS   B 2 90   ? 124.982 149.063 109.470 1.00 65.70  ? 90   LYS   A N   1 
ATOM   3027  C  CA  . LYS   B 2 90   ? 124.330 147.852 108.982 1.00 71.12  ? 90   LYS   A CA  1 
ATOM   3028  C  C   . LYS   B 2 90   ? 124.831 146.614 109.715 1.00 73.86  ? 90   LYS   A C   1 
ATOM   3029  O  O   . LYS   B 2 90   ? 124.051 145.692 109.989 1.00 77.38  ? 90   LYS   A O   1 
ATOM   3030  C  CB  . LYS   B 2 90   ? 124.521 147.714 107.471 1.00 74.64  ? 90   LYS   A CB  1 
ATOM   3031  C  CG  . LYS   B 2 90   ? 125.941 147.892 106.976 1.00 77.43  ? 90   LYS   A CG  1 
ATOM   3032  C  CD  . LYS   B 2 90   ? 125.987 147.820 105.456 1.00 78.18  ? 90   LYS   A CD  1 
ATOM   3033  C  CE  . LYS   B 2 90   ? 125.115 148.893 104.823 1.00 77.29  ? 90   LYS   A CE  1 
ATOM   3034  N  NZ  . LYS   B 2 90   ? 125.169 148.848 103.335 1.00 76.24  ? 90   LYS   A NZ  1 
ATOM   3035  N  N   . ASN   B 2 91   ? 126.123 146.572 110.055 1.00 69.06  ? 91   ASN   A N   1 
ATOM   3036  C  CA  . ASN   B 2 91   ? 126.623 145.448 110.838 1.00 67.61  ? 91   ASN   A CA  1 
ATOM   3037  C  C   . ASN   B 2 91   ? 125.974 145.407 112.216 1.00 73.70  ? 91   ASN   A C   1 
ATOM   3038  O  O   . ASN   B 2 91   ? 125.593 144.334 112.697 1.00 75.24  ? 91   ASN   A O   1 
ATOM   3039  C  CB  . ASN   B 2 91   ? 128.143 145.517 110.959 1.00 66.28  ? 91   ASN   A CB  1 
ATOM   3040  C  CG  . ASN   B 2 91   ? 128.725 144.295 111.636 1.00 71.34  ? 91   ASN   A CG  1 
ATOM   3041  O  OD1 . ASN   B 2 91   ? 129.042 144.321 112.824 1.00 75.29  ? 91   ASN   A OD1 1 
ATOM   3042  N  ND2 . ASN   B 2 91   ? 128.862 143.211 110.884 1.00 71.82  ? 91   ASN   A ND2 1 
ATOM   3043  N  N   . LEU   B 2 92   ? 125.824 146.566 112.862 1.00 66.51  ? 92   LEU   A N   1 
ATOM   3044  C  CA  . LEU   B 2 92   ? 125.174 146.603 114.166 1.00 64.50  ? 92   LEU   A CA  1 
ATOM   3045  C  C   . LEU   B 2 92   ? 123.715 146.181 114.069 1.00 67.78  ? 92   LEU   A C   1 
ATOM   3046  O  O   . LEU   B 2 92   ? 123.206 145.486 114.952 1.00 75.11  ? 92   LEU   A O   1 
ATOM   3047  C  CB  . LEU   B 2 92   ? 125.295 147.997 114.777 1.00 64.76  ? 92   LEU   A CB  1 
ATOM   3048  C  CG  . LEU   B 2 92   ? 126.676 148.366 115.319 1.00 68.56  ? 92   LEU   A CG  1 
ATOM   3049  C  CD1 . LEU   B 2 92   ? 126.640 149.725 115.992 1.00 70.87  ? 92   LEU   A CD1 1 
ATOM   3050  C  CD2 . LEU   B 2 92   ? 127.181 147.303 116.278 1.00 68.62  ? 92   LEU   A CD2 1 
ATOM   3051  N  N   . PHE   B 2 93   ? 123.024 146.589 113.004 1.00 65.95  ? 93   PHE   A N   1 
ATOM   3052  C  CA  . PHE   B 2 93   ? 121.639 146.162 112.823 1.00 68.09  ? 93   PHE   A CA  1 
ATOM   3053  C  C   . PHE   B 2 93   ? 121.545 144.649 112.656 1.00 70.42  ? 93   PHE   A C   1 
ATOM   3054  O  O   . PHE   B 2 93   ? 120.723 143.987 113.309 1.00 75.59  ? 93   PHE   A O   1 
ATOM   3055  C  CB  . PHE   B 2 93   ? 121.022 146.878 111.623 1.00 69.12  ? 93   PHE   A CB  1 
ATOM   3056  C  CG  . PHE   B 2 93   ? 120.287 148.136 111.983 1.00 73.28  ? 93   PHE   A CG  1 
ATOM   3057  C  CD1 . PHE   B 2 93   ? 120.970 149.248 112.444 1.00 73.49  ? 93   PHE   A CD1 1 
ATOM   3058  C  CD2 . PHE   B 2 93   ? 118.911 148.207 111.855 1.00 74.89  ? 93   PHE   A CD2 1 
ATOM   3059  C  CE1 . PHE   B 2 93   ? 120.295 150.406 112.774 1.00 73.63  ? 93   PHE   A CE1 1 
ATOM   3060  C  CE2 . PHE   B 2 93   ? 118.229 149.363 112.184 1.00 77.92  ? 93   PHE   A CE2 1 
ATOM   3061  C  CZ  . PHE   B 2 93   ? 118.922 150.464 112.644 1.00 74.68  ? 93   PHE   A CZ  1 
ATOM   3062  N  N   . GLU   B 2 94   ? 122.393 144.076 111.797 1.00 66.16  ? 94   GLU   A N   1 
ATOM   3063  C  CA  . GLU   B 2 94   ? 122.321 142.637 111.575 1.00 68.35  ? 94   GLU   A CA  1 
ATOM   3064  C  C   . GLU   B 2 94   ? 122.769 141.855 112.804 1.00 73.59  ? 94   GLU   A C   1 
ATOM   3065  O  O   . GLU   B 2 94   ? 122.380 140.694 112.971 1.00 76.38  ? 94   GLU   A O   1 
ATOM   3066  C  CB  . GLU   B 2 94   ? 123.151 142.242 110.350 1.00 70.71  ? 94   GLU   A CB  1 
ATOM   3067  C  CG  . GLU   B 2 94   ? 124.648 142.205 110.572 1.00 74.39  ? 94   GLU   A CG  1 
ATOM   3068  C  CD  . GLU   B 2 94   ? 125.395 141.660 109.373 1.00 77.50  ? 94   GLU   A CD  1 
ATOM   3069  O  OE1 . GLU   B 2 94   ? 124.742 141.355 108.353 1.00 74.38  ? 94   GLU   A OE1 1 
ATOM   3070  O  OE2 . GLU   B 2 94   ? 126.634 141.534 109.449 1.00 81.14  ? 94   GLU   A OE2 1 
ATOM   3071  N  N   . GLN   B 2 95   ? 123.581 142.466 113.671 1.00 64.98  ? 95   GLN   A N   1 
ATOM   3072  C  CA  . GLN   B 2 95   ? 123.919 141.821 114.935 1.00 60.32  ? 95   GLN   A CA  1 
ATOM   3073  C  C   . GLN   B 2 95   ? 122.785 141.934 115.946 1.00 63.55  ? 95   GLN   A C   1 
ATOM   3074  O  O   . GLN   B 2 95   ? 122.557 141.009 116.732 1.00 72.74  ? 95   GLN   A O   1 
ATOM   3075  C  CB  . GLN   B 2 95   ? 125.201 142.418 115.510 1.00 61.72  ? 95   GLN   A CB  1 
ATOM   3076  C  CG  . GLN   B 2 95   ? 126.440 142.100 114.708 1.00 62.70  ? 95   GLN   A CG  1 
ATOM   3077  C  CD  . GLN   B 2 95   ? 127.706 142.419 115.460 1.00 65.76  ? 95   GLN   A CD  1 
ATOM   3078  O  OE1 . GLN   B 2 95   ? 127.877 142.005 116.604 1.00 65.94  ? 95   GLN   A OE1 1 
ATOM   3079  N  NE2 . GLN   B 2 95   ? 128.605 143.158 114.824 1.00 65.32  ? 95   GLN   A NE2 1 
ATOM   3080  N  N   . PHE   B 2 96   ? 122.066 143.054 115.941 1.00 59.00  ? 96   PHE   A N   1 
ATOM   3081  C  CA  . PHE   B 2 96   ? 120.956 143.256 116.861 1.00 58.37  ? 96   PHE   A CA  1 
ATOM   3082  C  C   . PHE   B 2 96   ? 119.672 142.603 116.378 1.00 62.29  ? 96   PHE   A C   1 
ATOM   3083  O  O   . PHE   B 2 96   ? 118.648 142.702 117.061 1.00 66.52  ? 96   PHE   A O   1 
ATOM   3084  C  CB  . PHE   B 2 96   ? 120.730 144.750 117.104 1.00 55.37  ? 96   PHE   A CB  1 
ATOM   3085  C  CG  . PHE   B 2 96   ? 121.568 145.310 118.217 1.00 54.48  ? 96   PHE   A CG  1 
ATOM   3086  C  CD1 . PHE   B 2 96   ? 121.141 145.227 119.528 1.00 56.38  ? 96   PHE   A CD1 1 
ATOM   3087  C  CD2 . PHE   B 2 96   ? 122.784 145.907 117.955 1.00 58.45  ? 96   PHE   A CD2 1 
ATOM   3088  C  CE1 . PHE   B 2 96   ? 121.909 145.733 120.553 1.00 58.52  ? 96   PHE   A CE1 1 
ATOM   3089  C  CE2 . PHE   B 2 96   ? 123.556 146.416 118.977 1.00 60.91  ? 96   PHE   A CE2 1 
ATOM   3090  C  CZ  . PHE   B 2 96   ? 123.118 146.329 120.277 1.00 60.22  ? 96   PHE   A CZ  1 
ATOM   3091  N  N   . ARG   B 2 97   ? 119.702 141.947 115.224 1.00 69.61  ? 97   ARG   A N   1 
ATOM   3092  C  CA  . ARG   B 2 97   ? 118.613 141.066 114.824 1.00 71.03  ? 97   ARG   A CA  1 
ATOM   3093  C  C   . ARG   B 2 97   ? 118.596 139.747 115.601 1.00 70.51  ? 97   ARG   A C   1 
ATOM   3094  O  O   . ARG   B 2 97   ? 117.882 138.823 115.199 1.00 73.51  ? 97   ARG   A O   1 
ATOM   3095  C  CB  . ARG   B 2 97   ? 118.696 140.779 113.321 1.00 74.39  ? 97   ARG   A CB  1 
ATOM   3096  C  CG  . ARG   B 2 97   ? 118.354 141.971 112.442 1.00 71.84  ? 97   ARG   A CG  1 
ATOM   3097  C  CD  . ARG   B 2 97   ? 118.777 141.755 110.993 1.00 70.96  ? 97   ARG   A CD  1 
ATOM   3098  N  NE  . ARG   B 2 97   ? 118.154 140.582 110.391 1.00 75.95  ? 97   ARG   A NE  1 
ATOM   3099  C  CZ  . ARG   B 2 97   ? 118.770 139.426 110.185 1.00 74.84  ? 97   ARG   A CZ  1 
ATOM   3100  N  NH1 . ARG   B 2 97   ? 120.037 139.248 110.524 1.00 71.29  ? 97   ARG   A NH1 1 
ATOM   3101  N  NH2 . ARG   B 2 97   ? 118.100 138.424 109.623 1.00 73.67  ? 97   ARG   A NH2 1 
ATOM   3102  N  N   . ARG   B 2 98   ? 119.362 139.634 116.689 1.00 68.09  ? 98   ARG   A N   1 
ATOM   3103  C  CA  . ARG   B 2 98   ? 119.475 138.397 117.452 1.00 64.34  ? 98   ARG   A CA  1 
ATOM   3104  C  C   . ARG   B 2 98   ? 118.760 138.433 118.798 1.00 68.62  ? 98   ARG   A C   1 
ATOM   3105  O  O   . ARG   B 2 98   ? 118.894 137.479 119.571 1.00 71.45  ? 98   ARG   A O   1 
ATOM   3106  C  CB  . ARG   B 2 98   ? 120.949 138.048 117.681 1.00 64.39  ? 98   ARG   A CB  1 
ATOM   3107  C  CG  . ARG   B 2 98   ? 121.674 137.535 116.453 1.00 66.97  ? 98   ARG   A CG  1 
ATOM   3108  C  CD  . ARG   B 2 98   ? 123.071 137.050 116.806 1.00 68.39  ? 98   ARG   A CD  1 
ATOM   3109  N  NE  . ARG   B 2 98   ? 123.764 136.496 115.649 1.00 70.65  ? 98   ARG   A NE  1 
ATOM   3110  C  CZ  . ARG   B 2 98   ? 124.989 135.990 115.681 1.00 71.99  ? 98   ARG   A CZ  1 
ATOM   3111  N  NH1 . ARG   B 2 98   ? 125.691 135.950 116.802 1.00 69.25  ? 98   ARG   A NH1 1 
ATOM   3112  N  NH2 . ARG   B 2 98   ? 125.523 135.511 114.561 1.00 69.14  ? 98   ARG   A NH2 1 
ATOM   3113  N  N   . VAL   B 2 99   ? 118.030 139.507 119.109 1.00 64.27  ? 99   VAL   A N   1 
ATOM   3114  C  CA  . VAL   B 2 99   ? 117.233 139.623 120.333 1.00 55.63  ? 99   VAL   A CA  1 
ATOM   3115  C  C   . VAL   B 2 99   ? 118.110 139.597 121.581 1.00 56.85  ? 99   VAL   A C   1 
ATOM   3116  O  O   . VAL   B 2 99   ? 118.011 140.483 122.442 1.00 63.65  ? 99   VAL   A O   1 
ATOM   3117  C  CB  . VAL   B 2 99   ? 116.160 138.521 120.407 1.00 49.01  ? 99   VAL   A CB  1 
ATOM   3118  C  CG1 . VAL   B 2 99   ? 115.338 138.673 121.672 1.00 52.43  ? 99   VAL   A CG1 1 
ATOM   3119  C  CG2 . VAL   B 2 99   ? 115.269 138.566 119.180 1.00 55.22  ? 99   VAL   A CG2 1 
ATOM   3120  N  N   . ALA   B 2 100  ? 118.956 138.572 121.699 1.00 48.06  ? 100  ALA   A N   1 
ATOM   3121  C  CA  . ALA   B 2 100  ? 119.848 138.474 122.847 1.00 45.35  ? 100  ALA   A CA  1 
ATOM   3122  C  C   . ALA   B 2 100  ? 120.766 139.684 122.937 1.00 48.58  ? 100  ALA   A C   1 
ATOM   3123  O  O   . ALA   B 2 100  ? 121.101 140.137 124.037 1.00 56.06  ? 100  ALA   A O   1 
ATOM   3124  C  CB  . ALA   B 2 100  ? 120.665 137.187 122.771 1.00 45.77  ? 100  ALA   A CB  1 
ATOM   3125  N  N   . ASN   B 2 101  ? 121.184 140.223 121.790 1.00 52.64  ? 101  ASN   A N   1 
ATOM   3126  C  CA  . ASN   B 2 101  ? 121.995 141.435 121.804 1.00 47.94  ? 101  ASN   A CA  1 
ATOM   3127  C  C   . ASN   B 2 101  ? 121.211 142.611 122.370 1.00 50.98  ? 101  ASN   A C   1 
ATOM   3128  O  O   . ASN   B 2 101  ? 121.760 143.434 123.112 1.00 54.11  ? 101  ASN   A O   1 
ATOM   3129  C  CB  . ASN   B 2 101  ? 122.498 141.747 120.397 1.00 47.81  ? 101  ASN   A CB  1 
ATOM   3130  C  CG  . ASN   B 2 101  ? 123.542 140.761 119.920 1.00 50.83  ? 101  ASN   A CG  1 
ATOM   3131  O  OD1 . ASN   B 2 101  ? 123.651 139.654 120.444 1.00 50.74  ? 101  ASN   A OD1 1 
ATOM   3132  N  ND2 . ASN   B 2 101  ? 124.317 141.159 118.922 1.00 53.41  ? 101  ASN   A ND2 1 
ATOM   3133  N  N   . CYS   B 2 102  ? 119.923 142.706 122.031 1.00 53.21  ? 102  CYS   A N   1 
ATOM   3134  C  CA  . CYS   B 2 102  ? 119.084 143.751 122.606 1.00 49.30  ? 102  CYS   A CA  1 
ATOM   3135  C  C   . CYS   B 2 102  ? 118.970 143.591 124.115 1.00 52.36  ? 102  CYS   A C   1 
ATOM   3136  O  O   . CYS   B 2 102  ? 119.029 144.577 124.860 1.00 57.79  ? 102  CYS   A O   1 
ATOM   3137  C  CB  . CYS   B 2 102  ? 117.702 143.731 121.957 1.00 49.61  ? 102  CYS   A CB  1 
ATOM   3138  S  SG  . CYS   B 2 102  ? 117.718 143.926 120.162 1.00 69.91  ? 102  CYS   A SG  1 
ATOM   3139  N  N   . PHE   B 2 103  ? 118.812 142.352 124.585 1.00 45.17  ? 103  PHE   A N   1 
ATOM   3140  C  CA  . PHE   B 2 103  ? 118.748 142.117 126.025 1.00 41.28  ? 103  PHE   A CA  1 
ATOM   3141  C  C   . PHE   B 2 103  ? 120.054 142.499 126.711 1.00 42.05  ? 103  PHE   A C   1 
ATOM   3142  O  O   . PHE   B 2 103  ? 120.044 143.094 127.796 1.00 52.57  ? 103  PHE   A O   1 
ATOM   3143  C  CB  . PHE   B 2 103  ? 118.403 140.656 126.304 1.00 38.34  ? 103  PHE   A CB  1 
ATOM   3144  C  CG  . PHE   B 2 103  ? 118.479 140.283 127.753 1.00 45.06  ? 103  PHE   A CG  1 
ATOM   3145  C  CD1 . PHE   B 2 103  ? 117.539 140.751 128.654 1.00 48.28  ? 103  PHE   A CD1 1 
ATOM   3146  C  CD2 . PHE   B 2 103  ? 119.486 139.458 128.215 1.00 44.38  ? 103  PHE   A CD2 1 
ATOM   3147  C  CE1 . PHE   B 2 103  ? 117.609 140.406 129.988 1.00 46.74  ? 103  PHE   A CE1 1 
ATOM   3148  C  CE2 . PHE   B 2 103  ? 119.557 139.107 129.544 1.00 45.84  ? 103  PHE   A CE2 1 
ATOM   3149  C  CZ  . PHE   B 2 103  ? 118.621 139.584 130.432 1.00 47.12  ? 103  PHE   A CZ  1 
ATOM   3150  N  N   . PHE   B 2 104  ? 121.189 142.157 126.099 1.00 36.97  ? 104  PHE   A N   1 
ATOM   3151  C  CA  . PHE   B 2 104  ? 122.482 142.510 126.679 1.00 37.12  ? 104  PHE   A CA  1 
ATOM   3152  C  C   . PHE   B 2 104  ? 122.664 144.019 126.738 1.00 39.56  ? 104  PHE   A C   1 
ATOM   3153  O  O   . PHE   B 2 104  ? 123.169 144.553 127.733 1.00 53.32  ? 104  PHE   A O   1 
ATOM   3154  C  CB  . PHE   B 2 104  ? 123.615 141.870 125.879 1.00 41.09  ? 104  PHE   A CB  1 
ATOM   3155  C  CG  . PHE   B 2 104  ? 123.534 140.376 125.797 1.00 45.12  ? 104  PHE   A CG  1 
ATOM   3156  C  CD1 . PHE   B 2 104  ? 122.914 139.645 126.794 1.00 49.83  ? 104  PHE   A CD1 1 
ATOM   3157  C  CD2 . PHE   B 2 104  ? 124.075 139.700 124.719 1.00 42.30  ? 104  PHE   A CD2 1 
ATOM   3158  C  CE1 . PHE   B 2 104  ? 122.835 138.273 126.715 1.00 47.91  ? 104  PHE   A CE1 1 
ATOM   3159  C  CE2 . PHE   B 2 104  ? 123.997 138.328 124.636 1.00 45.96  ? 104  PHE   A CE2 1 
ATOM   3160  C  CZ  . PHE   B 2 104  ? 123.376 137.614 125.635 1.00 47.55  ? 104  PHE   A CZ  1 
ATOM   3161  N  N   . LEU   B 2 105  ? 122.264 144.721 125.676 1.00 40.14  ? 105  LEU   A N   1 
ATOM   3162  C  CA  . LEU   B 2 105  ? 122.350 146.176 125.676 1.00 43.76  ? 105  LEU   A CA  1 
ATOM   3163  C  C   . LEU   B 2 105  ? 121.465 146.779 126.757 1.00 48.38  ? 105  LEU   A C   1 
ATOM   3164  O  O   . LEU   B 2 105  ? 121.868 147.725 127.443 1.00 55.74  ? 105  LEU   A O   1 
ATOM   3165  C  CB  . LEU   B 2 105  ? 121.967 146.722 124.303 1.00 44.51  ? 105  LEU   A CB  1 
ATOM   3166  C  CG  . LEU   B 2 105  ? 122.136 148.225 124.094 1.00 38.17  ? 105  LEU   A CG  1 
ATOM   3167  C  CD1 . LEU   B 2 105  ? 123.595 148.613 124.206 1.00 44.23  ? 105  LEU   A CD1 1 
ATOM   3168  C  CD2 . LEU   B 2 105  ? 121.573 148.638 122.750 1.00 48.03  ? 105  LEU   A CD2 1 
ATOM   3169  N  N   . ALA   B 2 106  ? 120.252 146.245 126.921 1.00 37.16  ? 106  ALA   A N   1 
ATOM   3170  C  CA  . ALA   B 2 106  ? 119.361 146.744 127.963 1.00 34.73  ? 106  ALA   A CA  1 
ATOM   3171  C  C   . ALA   B 2 106  ? 119.957 146.530 129.348 1.00 41.72  ? 106  ALA   A C   1 
ATOM   3172  O  O   . ALA   B 2 106  ? 119.916 147.429 130.196 1.00 53.37  ? 106  ALA   A O   1 
ATOM   3173  C  CB  . ALA   B 2 106  ? 117.997 146.066 127.854 1.00 37.01  ? 106  ALA   A CB  1 
ATOM   3174  N  N   . ILE   B 2 107  ? 120.531 145.350 129.587 1.00 37.71  ? 107  ILE   A N   1 
ATOM   3175  C  CA  . ILE   B 2 107  ? 121.146 145.066 130.881 1.00 34.24  ? 107  ILE   A CA  1 
ATOM   3176  C  C   . ILE   B 2 107  ? 122.320 146.002 131.138 1.00 48.10  ? 107  ILE   A C   1 
ATOM   3177  O  O   . ILE   B 2 107  ? 122.480 146.531 132.245 1.00 54.95  ? 107  ILE   A O   1 
ATOM   3178  C  CB  . ILE   B 2 107  ? 121.569 143.587 130.955 1.00 40.00  ? 107  ILE   A CB  1 
ATOM   3179  C  CG1 . ILE   B 2 107  ? 120.348 142.698 131.179 1.00 43.79  ? 107  ILE   A CG1 1 
ATOM   3180  C  CG2 . ILE   B 2 107  ? 122.581 143.374 132.062 1.00 46.66  ? 107  ILE   A CG2 1 
ATOM   3181  C  CD1 . ILE   B 2 107  ? 119.650 142.953 132.491 1.00 48.84  ? 107  ILE   A CD1 1 
ATOM   3182  N  N   . SER   B 2 108  ? 123.160 146.223 130.124 1.00 42.65  ? 108  SER   A N   1 
ATOM   3183  C  CA  . SER   B 2 108  ? 124.311 147.104 130.299 1.00 44.43  ? 108  SER   A CA  1 
ATOM   3184  C  C   . SER   B 2 108  ? 123.878 148.539 130.576 1.00 49.01  ? 108  SER   A C   1 
ATOM   3185  O  O   . SER   B 2 108  ? 124.439 149.209 131.455 1.00 56.52  ? 108  SER   A O   1 
ATOM   3186  C  CB  . SER   B 2 108  ? 125.208 147.038 129.065 1.00 53.69  ? 108  SER   A CB  1 
ATOM   3187  O  OG  . SER   B 2 108  ? 125.651 145.713 128.833 1.00 54.66  ? 108  SER   A OG  1 
ATOM   3188  N  N   . ILE   B 2 109  ? 122.877 149.028 129.840 1.00 39.65  ? 109  ILE   A N   1 
ATOM   3189  C  CA  . ILE   B 2 109  ? 122.372 150.378 130.071 1.00 42.45  ? 109  ILE   A CA  1 
ATOM   3190  C  C   . ILE   B 2 109  ? 121.797 150.495 131.475 1.00 51.11  ? 109  ILE   A C   1 
ATOM   3191  O  O   . ILE   B 2 109  ? 121.986 151.509 132.158 1.00 54.51  ? 109  ILE   A O   1 
ATOM   3192  C  CB  . ILE   B 2 109  ? 121.335 150.752 128.996 1.00 46.94  ? 109  ILE   A CB  1 
ATOM   3193  C  CG1 . ILE   B 2 109  ? 122.017 150.937 127.641 1.00 50.83  ? 109  ILE   A CG1 1 
ATOM   3194  C  CG2 . ILE   B 2 109  ? 120.583 152.010 129.385 1.00 48.42  ? 109  ILE   A CG2 1 
ATOM   3195  C  CD1 . ILE   B 2 109  ? 121.070 151.312 126.526 1.00 50.79  ? 109  ILE   A CD1 1 
ATOM   3196  N  N   . LEU   B 2 110  ? 121.092 149.457 131.933 1.00 49.04  ? 110  LEU   A N   1 
ATOM   3197  C  CA  . LEU   B 2 110  ? 120.565 149.467 133.293 1.00 41.21  ? 110  LEU   A CA  1 
ATOM   3198  C  C   . LEU   B 2 110  ? 121.689 149.517 134.319 1.00 48.64  ? 110  LEU   A C   1 
ATOM   3199  O  O   . LEU   B 2 110  ? 121.598 150.241 135.316 1.00 56.26  ? 110  LEU   A O   1 
ATOM   3200  C  CB  . LEU   B 2 110  ? 119.687 148.239 133.521 1.00 38.46  ? 110  LEU   A CB  1 
ATOM   3201  C  CG  . LEU   B 2 110  ? 119.011 148.132 134.885 1.00 44.29  ? 110  LEU   A CG  1 
ATOM   3202  C  CD1 . LEU   B 2 110  ? 118.079 149.307 135.102 1.00 49.49  ? 110  LEU   A CD1 1 
ATOM   3203  C  CD2 . LEU   B 2 110  ? 118.259 146.820 134.998 1.00 48.70  ? 110  LEU   A CD2 1 
ATOM   3204  N  N   . GLN   B 2 111  ? 122.757 148.755 134.093 1.00 52.34  ? 111  GLN   A N   1 
ATOM   3205  C  CA  . GLN   B 2 111  ? 123.875 148.732 135.025 1.00 47.50  ? 111  GLN   A CA  1 
ATOM   3206  C  C   . GLN   B 2 111  ? 124.716 149.998 134.976 1.00 50.74  ? 111  GLN   A C   1 
ATOM   3207  O  O   . GLN   B 2 111  ? 125.509 150.225 135.895 1.00 57.05  ? 111  GLN   A O   1 
ATOM   3208  C  CB  . GLN   B 2 111  ? 124.769 147.520 134.760 1.00 47.55  ? 111  GLN   A CB  1 
ATOM   3209  C  CG  . GLN   B 2 111  ? 124.077 146.190 134.965 1.00 52.04  ? 111  GLN   A CG  1 
ATOM   3210  C  CD  . GLN   B 2 111  ? 125.044 145.029 134.967 1.00 59.23  ? 111  GLN   A CD  1 
ATOM   3211  O  OE1 . GLN   B 2 111  ? 124.859 144.048 134.250 1.00 55.29  ? 111  GLN   A OE1 1 
ATOM   3212  N  NE2 . GLN   B 2 111  ? 126.082 145.132 135.783 1.00 61.50  ? 111  GLN   A NE2 1 
ATOM   3213  N  N   . PHE   B 2 112  ? 124.578 150.816 133.929 1.00 56.28  ? 112  PHE   A N   1 
ATOM   3214  C  CA  . PHE   B 2 112  ? 125.258 152.109 133.922 1.00 57.91  ? 112  PHE   A CA  1 
ATOM   3215  C  C   . PHE   B 2 112  ? 124.805 152.989 135.080 1.00 60.99  ? 112  PHE   A C   1 
ATOM   3216  O  O   . PHE   B 2 112  ? 125.583 153.814 135.571 1.00 60.47  ? 112  PHE   A O   1 
ATOM   3217  C  CB  . PHE   B 2 112  ? 125.022 152.830 132.595 1.00 60.06  ? 112  PHE   A CB  1 
ATOM   3218  C  CG  . PHE   B 2 112  ? 125.912 152.360 131.483 1.00 60.43  ? 112  PHE   A CG  1 
ATOM   3219  C  CD1 . PHE   B 2 112  ? 127.051 151.625 131.754 1.00 59.95  ? 112  PHE   A CD1 1 
ATOM   3220  C  CD2 . PHE   B 2 112  ? 125.613 152.660 130.165 1.00 61.16  ? 112  PHE   A CD2 1 
ATOM   3221  C  CE1 . PHE   B 2 112  ? 127.871 151.193 130.736 1.00 59.44  ? 112  PHE   A CE1 1 
ATOM   3222  C  CE2 . PHE   B 2 112  ? 126.431 152.231 129.140 1.00 64.36  ? 112  PHE   A CE2 1 
ATOM   3223  C  CZ  . PHE   B 2 112  ? 127.562 151.497 129.427 1.00 62.17  ? 112  PHE   A CZ  1 
ATOM   3224  N  N   . PHE   B 2 113  ? 123.559 152.836 135.522 1.00 61.97  ? 113  PHE   A N   1 
ATOM   3225  C  CA  . PHE   B 2 113  ? 123.047 153.639 136.621 1.00 57.19  ? 113  PHE   A CA  1 
ATOM   3226  C  C   . PHE   B 2 113  ? 123.791 153.316 137.916 1.00 58.63  ? 113  PHE   A C   1 
ATOM   3227  O  O   . PHE   B 2 113  ? 124.182 152.168 138.148 1.00 64.17  ? 113  PHE   A O   1 
ATOM   3228  C  CB  . PHE   B 2 113  ? 121.554 153.400 136.806 1.00 53.49  ? 113  PHE   A CB  1 
ATOM   3229  C  CG  . PHE   B 2 113  ? 120.716 153.904 135.670 1.00 51.98  ? 113  PHE   A CG  1 
ATOM   3230  C  CD1 . PHE   B 2 113  ? 120.461 153.103 134.571 1.00 59.20  ? 113  PHE   A CD1 1 
ATOM   3231  C  CD2 . PHE   B 2 113  ? 120.183 155.179 135.700 1.00 54.94  ? 113  PHE   A CD2 1 
ATOM   3232  C  CE1 . PHE   B 2 113  ? 119.690 153.566 133.524 1.00 59.00  ? 113  PHE   A CE1 1 
ATOM   3233  C  CE2 . PHE   B 2 113  ? 119.411 155.647 134.655 1.00 58.38  ? 113  PHE   A CE2 1 
ATOM   3234  C  CZ  . PHE   B 2 113  ? 119.165 154.839 133.566 1.00 59.23  ? 113  PHE   A CZ  1 
ATOM   3235  N  N   . PRO   B 2 114  ? 124.008 154.318 138.773 1.00 60.06  ? 114  PRO   A N   1 
ATOM   3236  C  CA  . PRO   B 2 114  ? 124.786 154.081 140.000 1.00 57.67  ? 114  PRO   A CA  1 
ATOM   3237  C  C   . PRO   B 2 114  ? 124.164 153.062 140.935 1.00 56.62  ? 114  PRO   A C   1 
ATOM   3238  O  O   . PRO   B 2 114  ? 124.894 152.363 141.648 1.00 61.41  ? 114  PRO   A O   1 
ATOM   3239  C  CB  . PRO   B 2 114  ? 124.846 155.471 140.649 1.00 61.31  ? 114  PRO   A CB  1 
ATOM   3240  C  CG  . PRO   B 2 114  ? 124.570 156.431 139.537 1.00 62.98  ? 114  PRO   A CG  1 
ATOM   3241  C  CD  . PRO   B 2 114  ? 123.603 155.727 138.641 1.00 61.34  ? 114  PRO   A CD  1 
ATOM   3242  N  N   . LYS   B 2 115  ? 122.834 152.962 140.962 1.00 53.79  ? 115  LYS   A N   1 
ATOM   3243  C  CA  . LYS   B 2 115  ? 122.181 152.076 141.918 1.00 54.78  ? 115  LYS   A CA  1 
ATOM   3244  C  C   . LYS   B 2 115  ? 122.449 150.609 141.613 1.00 57.21  ? 115  LYS   A C   1 
ATOM   3245  O  O   . LYS   B 2 115  ? 122.608 149.806 142.539 1.00 60.74  ? 115  LYS   A O   1 
ATOM   3246  C  CB  . LYS   B 2 115  ? 120.677 152.346 141.939 1.00 54.10  ? 115  LYS   A CB  1 
ATOM   3247  C  CG  . LYS   B 2 115  ? 119.986 151.843 143.191 1.00 53.71  ? 115  LYS   A CG  1 
ATOM   3248  C  CD  . LYS   B 2 115  ? 118.560 152.348 143.277 1.00 51.80  ? 115  LYS   A CD  1 
ATOM   3249  C  CE  . LYS   B 2 115  ? 118.028 152.234 144.694 1.00 54.76  ? 115  LYS   A CE  1 
ATOM   3250  N  NZ  . LYS   B 2 115  ? 118.109 150.841 145.208 1.00 58.43  ? 115  LYS   A NZ  1 
ATOM   3251  N  N   . PHE   B 2 116  ? 122.507 150.239 140.336 1.00 52.49  ? 116  PHE   A N   1 
ATOM   3252  C  CA  . PHE   B 2 116  ? 122.634 148.846 139.936 1.00 48.45  ? 116  PHE   A CA  1 
ATOM   3253  C  C   . PHE   B 2 116  ? 124.055 148.451 139.559 1.00 52.29  ? 116  PHE   A C   1 
ATOM   3254  O  O   . PHE   B 2 116  ? 124.262 147.328 139.089 1.00 56.78  ? 116  PHE   A O   1 
ATOM   3255  C  CB  . PHE   B 2 116  ? 121.696 148.553 138.763 1.00 52.54  ? 116  PHE   A CB  1 
ATOM   3256  C  CG  . PHE   B 2 116  ? 120.294 149.032 138.977 1.00 49.29  ? 116  PHE   A CG  1 
ATOM   3257  C  CD1 . PHE   B 2 116  ? 119.457 148.388 139.867 1.00 48.81  ? 116  PHE   A CD1 1 
ATOM   3258  C  CD2 . PHE   B 2 116  ? 119.809 150.122 138.281 1.00 49.19  ? 116  PHE   A CD2 1 
ATOM   3259  C  CE1 . PHE   B 2 116  ? 118.169 148.829 140.066 1.00 50.13  ? 116  PHE   A CE1 1 
ATOM   3260  C  CE2 . PHE   B 2 116  ? 118.520 150.565 138.475 1.00 53.18  ? 116  PHE   A CE2 1 
ATOM   3261  C  CZ  . PHE   B 2 116  ? 117.699 149.917 139.367 1.00 51.58  ? 116  PHE   A CZ  1 
ATOM   3262  N  N   . SER   B 2 117  ? 125.032 149.332 139.750 1.00 61.58  ? 117  SER   A N   1 
ATOM   3263  C  CA  . SER   B 2 117  ? 126.405 149.019 139.375 1.00 62.24  ? 117  SER   A CA  1 
ATOM   3264  C  C   . SER   B 2 117  ? 126.983 147.963 140.309 1.00 64.94  ? 117  SER   A C   1 
ATOM   3265  O  O   . SER   B 2 117  ? 126.820 148.044 141.530 1.00 68.06  ? 117  SER   A O   1 
ATOM   3266  C  CB  . SER   B 2 117  ? 127.266 150.279 139.410 1.00 63.28  ? 117  SER   A CB  1 
ATOM   3267  O  OG  . SER   B 2 117  ? 127.386 150.776 140.731 1.00 68.39  ? 117  SER   A OG  1 
ATOM   3268  N  N   . THR   B 2 118  ? 127.662 146.972 139.733 1.00 76.94  ? 118  THR   A N   1 
ATOM   3269  C  CA  . THR   B 2 118  ? 128.280 145.898 140.499 1.00 79.48  ? 118  THR   A CA  1 
ATOM   3270  C  C   . THR   B 2 118  ? 129.800 145.940 140.462 1.00 80.41  ? 118  THR   A C   1 
ATOM   3271  O  O   . THR   B 2 118  ? 130.444 145.820 141.509 1.00 78.71  ? 118  THR   A O   1 
ATOM   3272  C  CB  . THR   B 2 118  ? 127.780 144.530 140.002 1.00 80.91  ? 118  THR   A CB  1 
ATOM   3273  O  OG1 . THR   B 2 118  ? 128.601 143.489 140.546 1.00 80.89  ? 118  THR   A OG1 1 
ATOM   3274  C  CG2 . THR   B 2 118  ? 127.803 144.457 138.482 1.00 76.65  ? 118  THR   A CG2 1 
ATOM   3275  N  N   . ILE   B 2 119  ? 130.401 146.106 139.284 1.00 81.51  ? 119  ILE   A N   1 
ATOM   3276  C  CA  . ILE   B 2 119  ? 131.854 146.188 139.184 1.00 81.10  ? 119  ILE   A CA  1 
ATOM   3277  C  C   . ILE   B 2 119  ? 132.251 147.568 138.683 1.00 79.43  ? 119  ILE   A C   1 
ATOM   3278  O  O   . ILE   B 2 119  ? 132.883 148.348 139.405 1.00 80.20  ? 119  ILE   A O   1 
ATOM   3279  C  CB  . ILE   B 2 119  ? 132.416 145.099 138.253 1.00 82.31  ? 119  ILE   A CB  1 
ATOM   3280  C  CG1 . ILE   B 2 119  ? 131.723 143.759 138.497 1.00 80.86  ? 119  ILE   A CG1 1 
ATOM   3281  C  CG2 . ILE   B 2 119  ? 133.918 144.963 138.445 1.00 81.61  ? 119  ILE   A CG2 1 
ATOM   3282  C  CD1 . ILE   B 2 119  ? 132.133 142.687 137.508 1.00 79.37  ? 119  ILE   A CD1 1 
ATOM   3283  N  N   . SER   B 2 120  ? 131.866 147.879 137.447 1.00 79.35  ? 120  SER   A N   1 
ATOM   3284  C  CA  . SER   B 2 120  ? 132.184 149.137 136.786 1.00 81.19  ? 120  SER   A CA  1 
ATOM   3285  C  C   . SER   B 2 120  ? 131.458 149.189 135.449 1.00 84.36  ? 120  SER   A C   1 
ATOM   3286  O  O   . SER   B 2 120  ? 131.241 148.143 134.825 1.00 84.04  ? 120  SER   A O   1 
ATOM   3287  C  CB  . SER   B 2 120  ? 133.694 149.283 136.580 1.00 79.53  ? 120  SER   A CB  1 
ATOM   3288  O  OG  . SER   B 2 120  ? 134.206 148.215 135.804 1.00 81.31  ? 120  SER   A OG  1 
ATOM   3289  N  N   . PRO   B 2 121  ? 131.064 150.374 134.974 1.00 82.12  ? 121  PRO   A N   1 
ATOM   3290  C  CA  . PRO   B 2 121  ? 130.390 150.439 133.667 1.00 82.17  ? 121  PRO   A CA  1 
ATOM   3291  C  C   . PRO   B 2 121  ? 131.245 149.920 132.525 1.00 80.31  ? 121  PRO   A C   1 
ATOM   3292  O  O   . PRO   B 2 121  ? 130.728 149.268 131.607 1.00 80.04  ? 121  PRO   A O   1 
ATOM   3293  C  CB  . PRO   B 2 121  ? 130.074 151.934 133.515 1.00 77.88  ? 121  PRO   A CB  1 
ATOM   3294  C  CG  . PRO   B 2 121  ? 131.065 152.622 134.393 1.00 76.78  ? 121  PRO   A CG  1 
ATOM   3295  C  CD  . PRO   B 2 121  ? 131.267 151.708 135.562 1.00 75.41  ? 121  PRO   A CD  1 
ATOM   3296  N  N   . GLY   B 2 122  ? 132.553 150.180 132.568 1.00 66.66  ? 122  GLY   A N   1 
ATOM   3297  C  CA  . GLY   B 2 122  ? 133.419 149.737 131.490 1.00 66.70  ? 122  GLY   A CA  1 
ATOM   3298  C  C   . GLY   B 2 122  ? 133.502 148.228 131.394 1.00 71.71  ? 122  GLY   A C   1 
ATOM   3299  O  O   . GLY   B 2 122  ? 133.410 147.655 130.306 1.00 75.68  ? 122  GLY   A O   1 
ATOM   3300  N  N   . LEU   B 2 123  ? 133.668 147.559 132.535 1.00 67.34  ? 123  LEU   A N   1 
ATOM   3301  C  CA  . LEU   B 2 123  ? 133.776 146.105 132.515 1.00 69.36  ? 123  LEU   A CA  1 
ATOM   3302  C  C   . LEU   B 2 123  ? 132.432 145.450 132.226 1.00 73.87  ? 123  LEU   A C   1 
ATOM   3303  O  O   . LEU   B 2 123  ? 132.390 144.319 131.732 1.00 76.24  ? 123  LEU   A O   1 
ATOM   3304  C  CB  . LEU   B 2 123  ? 134.348 145.601 133.839 1.00 71.49  ? 123  LEU   A CB  1 
ATOM   3305  C  CG  . LEU   B 2 123  ? 134.819 144.146 133.868 1.00 73.83  ? 123  LEU   A CG  1 
ATOM   3306  C  CD1 . LEU   B 2 123  ? 135.881 143.911 132.807 1.00 69.87  ? 123  LEU   A CD1 1 
ATOM   3307  C  CD2 . LEU   B 2 123  ? 135.345 143.778 135.244 1.00 72.66  ? 123  LEU   A CD2 1 
ATOM   3308  N  N   . VAL   B 2 124  ? 131.330 146.135 132.534 1.00 68.98  ? 124  VAL   A N   1 
ATOM   3309  C  CA  . VAL   B 2 124  ? 130.014 145.626 132.165 1.00 65.91  ? 124  VAL   A CA  1 
ATOM   3310  C  C   . VAL   B 2 124  ? 129.809 145.720 130.658 1.00 71.19  ? 124  VAL   A C   1 
ATOM   3311  O  O   . VAL   B 2 124  ? 129.262 144.804 130.033 1.00 71.03  ? 124  VAL   A O   1 
ATOM   3312  C  CB  . VAL   B 2 124  ? 128.915 146.377 132.937 1.00 65.02  ? 124  VAL   A CB  1 
ATOM   3313  C  CG1 . VAL   B 2 124  ? 127.548 146.062 132.359 1.00 67.85  ? 124  VAL   A CG1 1 
ATOM   3314  C  CG2 . VAL   B 2 124  ? 128.961 146.004 134.408 1.00 67.32  ? 124  VAL   A CG2 1 
ATOM   3315  N  N   . ILE   B 2 125  ? 130.245 146.825 130.050 1.00 64.83  ? 125  ILE   A N   1 
ATOM   3316  C  CA  . ILE   B 2 125  ? 130.075 146.994 128.610 1.00 57.65  ? 125  ILE   A CA  1 
ATOM   3317  C  C   . ILE   B 2 125  ? 131.112 146.210 127.810 1.00 58.85  ? 125  ILE   A C   1 
ATOM   3318  O  O   . ILE   B 2 125  ? 130.896 145.948 126.619 1.00 64.71  ? 125  ILE   A O   1 
ATOM   3319  C  CB  . ILE   B 2 125  ? 130.106 148.493 128.258 1.00 57.10  ? 125  ILE   A CB  1 
ATOM   3320  C  CG1 . ILE   B 2 125  ? 128.862 148.887 127.458 1.00 57.66  ? 125  ILE   A CG1 1 
ATOM   3321  C  CG2 . ILE   B 2 125  ? 131.388 148.870 127.519 1.00 62.09  ? 125  ILE   A CG2 1 
ATOM   3322  C  CD1 . ILE   B 2 125  ? 128.736 148.202 126.120 1.00 60.32  ? 125  ILE   A CD1 1 
ATOM   3323  N  N   . LEU   B 2 126  ? 132.218 145.809 128.437 1.00 58.43  ? 126  LEU   A N   1 
ATOM   3324  C  CA  . LEU   B 2 126  ? 133.279 145.108 127.715 1.00 58.85  ? 126  LEU   A CA  1 
ATOM   3325  C  C   . LEU   B 2 126  ? 132.817 143.827 127.029 1.00 58.74  ? 126  LEU   A C   1 
ATOM   3326  O  O   . LEU   B 2 126  ? 133.196 143.615 125.865 1.00 65.68  ? 126  LEU   A O   1 
ATOM   3327  C  CB  . LEU   B 2 126  ? 134.449 144.840 128.670 1.00 61.07  ? 126  LEU   A CB  1 
ATOM   3328  C  CG  . LEU   B 2 126  ? 135.802 144.415 128.087 1.00 63.43  ? 126  LEU   A CG  1 
ATOM   3329  C  CD1 . LEU   B 2 126  ? 135.895 142.905 127.902 1.00 62.55  ? 126  LEU   A CD1 1 
ATOM   3330  C  CD2 . LEU   B 2 126  ? 136.077 145.136 126.773 1.00 60.48  ? 126  LEU   A CD2 1 
ATOM   3331  N  N   . PRO   B 2 127  ? 132.057 142.926 127.666 1.00 58.02  ? 127  PRO   A N   1 
ATOM   3332  C  CA  . PRO   B 2 127  ? 131.648 141.708 126.942 1.00 60.78  ? 127  PRO   A CA  1 
ATOM   3333  C  C   . PRO   B 2 127  ? 130.821 141.991 125.701 1.00 64.77  ? 127  PRO   A C   1 
ATOM   3334  O  O   . PRO   B 2 127  ? 131.039 141.363 124.656 1.00 69.42  ? 127  PRO   A O   1 
ATOM   3335  C  CB  . PRO   B 2 127  ? 130.843 140.931 127.993 1.00 59.40  ? 127  PRO   A CB  1 
ATOM   3336  C  CG  . PRO   B 2 127  ? 131.301 141.460 129.294 1.00 64.70  ? 127  PRO   A CG  1 
ATOM   3337  C  CD  . PRO   B 2 127  ? 131.598 142.899 129.064 1.00 61.41  ? 127  PRO   A CD  1 
ATOM   3338  N  N   . LEU   B 2 128  ? 129.875 142.929 125.786 1.00 59.62  ? 128  LEU   A N   1 
ATOM   3339  C  CA  . LEU   B 2 128  ? 129.060 143.261 124.623 1.00 54.69  ? 128  LEU   A CA  1 
ATOM   3340  C  C   . LEU   B 2 128  ? 129.908 143.874 123.518 1.00 58.51  ? 128  LEU   A C   1 
ATOM   3341  O  O   . LEU   B 2 128  ? 129.724 143.556 122.336 1.00 64.07  ? 128  LEU   A O   1 
ATOM   3342  C  CB  . LEU   B 2 128  ? 127.931 144.206 125.029 1.00 53.09  ? 128  LEU   A CB  1 
ATOM   3343  C  CG  . LEU   B 2 128  ? 126.911 144.545 123.945 1.00 57.77  ? 128  LEU   A CG  1 
ATOM   3344  C  CD1 . LEU   B 2 128  ? 126.295 143.280 123.380 1.00 57.41  ? 128  LEU   A CD1 1 
ATOM   3345  C  CD2 . LEU   B 2 128  ? 125.838 145.463 124.497 1.00 58.80  ? 128  LEU   A CD2 1 
ATOM   3346  N  N   . ILE   B 2 129  ? 130.846 144.749 123.884 1.00 52.08  ? 129  ILE   A N   1 
ATOM   3347  C  CA  . ILE   B 2 129  ? 131.741 145.340 122.894 1.00 47.46  ? 129  ILE   A CA  1 
ATOM   3348  C  C   . ILE   B 2 129  ? 132.590 144.262 122.236 1.00 51.14  ? 129  ILE   A C   1 
ATOM   3349  O  O   . ILE   B 2 129  ? 132.841 144.306 121.029 1.00 59.64  ? 129  ILE   A O   1 
ATOM   3350  C  CB  . ILE   B 2 129  ? 132.609 146.435 123.540 1.00 47.64  ? 129  ILE   A CB  1 
ATOM   3351  C  CG1 . ILE   B 2 129  ? 131.745 147.629 123.938 1.00 47.15  ? 129  ILE   A CG1 1 
ATOM   3352  C  CG2 . ILE   B 2 129  ? 133.713 146.878 122.594 1.00 52.24  ? 129  ILE   A CG2 1 
ATOM   3353  C  CD1 . ILE   B 2 129  ? 131.061 148.298 122.772 1.00 52.35  ? 129  ILE   A CD1 1 
ATOM   3354  N  N   . ILE   B 2 130  ? 133.037 143.275 123.013 1.00 52.09  ? 130  ILE   A N   1 
ATOM   3355  C  CA  . ILE   B 2 130  ? 133.838 142.192 122.449 1.00 51.91  ? 130  ILE   A CA  1 
ATOM   3356  C  C   . ILE   B 2 130  ? 133.014 141.364 121.470 1.00 50.92  ? 130  ILE   A C   1 
ATOM   3357  O  O   . ILE   B 2 130  ? 133.491 141.013 120.385 1.00 61.59  ? 130  ILE   A O   1 
ATOM   3358  C  CB  . ILE   B 2 130  ? 134.433 141.323 123.571 1.00 56.97  ? 130  ILE   A CB  1 
ATOM   3359  C  CG1 . ILE   B 2 130  ? 135.544 142.081 124.298 1.00 58.27  ? 130  ILE   A CG1 1 
ATOM   3360  C  CG2 . ILE   B 2 130  ? 134.971 140.018 123.011 1.00 58.28  ? 130  ILE   A CG2 1 
ATOM   3361  C  CD1 . ILE   B 2 130  ? 136.689 142.493 123.400 1.00 55.77  ? 130  ILE   A CD1 1 
ATOM   3362  N  N   . VAL   B 2 131  ? 131.771 141.041 121.831 1.00 43.62  ? 131  VAL   A N   1 
ATOM   3363  C  CA  . VAL   B 2 131  ? 130.908 140.285 120.923 1.00 52.78  ? 131  VAL   A CA  1 
ATOM   3364  C  C   . VAL   B 2 131  ? 130.700 141.055 119.626 1.00 56.26  ? 131  VAL   A C   1 
ATOM   3365  O  O   . VAL   B 2 131  ? 130.852 140.511 118.520 1.00 60.64  ? 131  VAL   A O   1 
ATOM   3366  C  CB  . VAL   B 2 131  ? 129.561 139.964 121.596 1.00 49.66  ? 131  VAL   A CB  1 
ATOM   3367  C  CG1 . VAL   B 2 131  ? 128.661 139.205 120.638 1.00 51.60  ? 131  VAL   A CG1 1 
ATOM   3368  C  CG2 . VAL   B 2 131  ? 129.771 139.171 122.857 1.00 51.65  ? 131  VAL   A CG2 1 
ATOM   3369  N  N   . LEU   B 2 132  ? 130.349 142.339 119.746 1.00 54.70  ? 132  LEU   A N   1 
ATOM   3370  C  CA  . LEU   B 2 132  ? 130.104 143.155 118.564 1.00 50.71  ? 132  LEU   A CA  1 
ATOM   3371  C  C   . LEU   B 2 132  ? 131.355 143.265 117.705 1.00 56.19  ? 132  LEU   A C   1 
ATOM   3372  O  O   . LEU   B 2 132  ? 131.282 143.154 116.478 1.00 60.07  ? 132  LEU   A O   1 
ATOM   3373  C  CB  . LEU   B 2 132  ? 129.610 144.542 118.974 1.00 56.20  ? 132  LEU   A CB  1 
ATOM   3374  C  CG  . LEU   B 2 132  ? 128.289 144.634 119.741 1.00 58.60  ? 132  LEU   A CG  1 
ATOM   3375  C  CD1 . LEU   B 2 132  ? 128.000 146.073 120.128 1.00 57.93  ? 132  LEU   A CD1 1 
ATOM   3376  C  CD2 . LEU   B 2 132  ? 127.142 144.063 118.935 1.00 55.94  ? 132  LEU   A CD2 1 
ATOM   3377  N  N   . ALA   B 2 133  ? 132.515 143.465 118.333 1.00 53.89  ? 133  ALA   A N   1 
ATOM   3378  C  CA  . ALA   B 2 133  ? 133.754 143.621 117.584 1.00 50.79  ? 133  ALA   A CA  1 
ATOM   3379  C  C   . ALA   B 2 133  ? 134.142 142.332 116.877 1.00 55.88  ? 133  ALA   A C   1 
ATOM   3380  O  O   . ALA   B 2 133  ? 134.620 142.365 115.741 1.00 61.69  ? 133  ALA   A O   1 
ATOM   3381  C  CB  . ALA   B 2 133  ? 134.875 144.081 118.514 1.00 52.62  ? 133  ALA   A CB  1 
ATOM   3382  N  N   . ILE   B 2 134  ? 133.949 141.185 117.530 1.00 58.55  ? 134  ILE   A N   1 
ATOM   3383  C  CA  . ILE   B 2 134  ? 134.306 139.915 116.905 1.00 60.90  ? 134  ILE   A CA  1 
ATOM   3384  C  C   . ILE   B 2 134  ? 133.403 139.631 115.714 1.00 59.69  ? 134  ILE   A C   1 
ATOM   3385  O  O   . ILE   B 2 134  ? 133.873 139.238 114.637 1.00 66.28  ? 134  ILE   A O   1 
ATOM   3386  C  CB  . ILE   B 2 134  ? 134.260 138.775 117.936 1.00 62.50  ? 134  ILE   A CB  1 
ATOM   3387  C  CG1 . ILE   B 2 134  ? 135.452 138.883 118.885 1.00 63.27  ? 134  ILE   A CG1 1 
ATOM   3388  C  CG2 . ILE   B 2 134  ? 134.245 137.422 117.241 1.00 61.29  ? 134  ILE   A CG2 1 
ATOM   3389  C  CD1 . ILE   B 2 134  ? 135.586 137.711 119.809 1.00 64.84  ? 134  ILE   A CD1 1 
ATOM   3390  N  N   . THR   B 2 135  ? 132.093 139.828 115.880 1.00 50.39  ? 135  THR   A N   1 
ATOM   3391  C  CA  . THR   B 2 135  ? 131.191 139.609 114.754 1.00 53.46  ? 135  THR   A CA  1 
ATOM   3392  C  C   . THR   B 2 135  ? 131.473 140.598 113.626 1.00 62.41  ? 135  THR   A C   1 
ATOM   3393  O  O   . THR   B 2 135  ? 131.424 140.236 112.442 1.00 68.33  ? 135  THR   A O   1 
ATOM   3394  C  CB  . THR   B 2 135  ? 129.738 139.707 115.212 1.00 58.94  ? 135  THR   A CB  1 
ATOM   3395  O  OG1 . THR   B 2 135  ? 129.541 138.864 116.354 1.00 60.72  ? 135  THR   A OG1 1 
ATOM   3396  C  CG2 . THR   B 2 135  ? 128.802 139.261 114.101 1.00 59.79  ? 135  THR   A CG2 1 
ATOM   3397  N  N   . ALA   B 2 136  ? 131.784 141.849 113.976 1.00 59.70  ? 136  ALA   A N   1 
ATOM   3398  C  CA  . ALA   B 2 136  ? 132.109 142.847 112.966 1.00 55.35  ? 136  ALA   A CA  1 
ATOM   3399  C  C   . ALA   B 2 136  ? 133.385 142.488 112.222 1.00 57.52  ? 136  ALA   A C   1 
ATOM   3400  O  O   . ALA   B 2 136  ? 133.467 142.672 111.007 1.00 67.35  ? 136  ALA   A O   1 
ATOM   3401  C  CB  . ALA   B 2 136  ? 132.235 144.226 113.614 1.00 59.79  ? 136  ALA   A CB  1 
ATOM   3402  N  N   . LEU   B 2 137  ? 134.398 141.988 112.933 1.00 54.88  ? 137  LEU   A N   1 
ATOM   3403  C  CA  . LEU   B 2 137  ? 135.633 141.578 112.273 1.00 51.98  ? 137  LEU   A CA  1 
ATOM   3404  C  C   . LEU   B 2 137  ? 135.401 140.380 111.365 1.00 60.69  ? 137  LEU   A C   1 
ATOM   3405  O  O   . LEU   B 2 137  ? 135.979 140.300 110.276 1.00 66.11  ? 137  LEU   A O   1 
ATOM   3406  C  CB  . LEU   B 2 137  ? 136.710 141.266 113.310 1.00 54.62  ? 137  LEU   A CB  1 
ATOM   3407  C  CG  . LEU   B 2 137  ? 137.362 142.466 113.997 1.00 63.72  ? 137  LEU   A CG  1 
ATOM   3408  C  CD1 . LEU   B 2 137  ? 138.441 142.008 114.966 1.00 64.68  ? 137  LEU   A CD1 1 
ATOM   3409  C  CD2 . LEU   B 2 137  ? 137.934 143.427 112.967 1.00 63.94  ? 137  LEU   A CD2 1 
ATOM   3410  N  N   . LYS   B 2 138  ? 134.561 139.437 111.796 1.00 64.99  ? 138  LYS   A N   1 
ATOM   3411  C  CA  . LYS   B 2 138  ? 134.204 138.314 110.935 1.00 60.00  ? 138  LYS   A CA  1 
ATOM   3412  C  C   . LYS   B 2 138  ? 133.555 138.800 109.644 1.00 61.13  ? 138  LYS   A C   1 
ATOM   3413  O  O   . LYS   B 2 138  ? 133.982 138.437 108.538 1.00 67.40  ? 138  LYS   A O   1 
ATOM   3414  C  CB  . LYS   B 2 138  ? 133.264 137.369 111.682 1.00 59.02  ? 138  LYS   A CB  1 
ATOM   3415  C  CG  . LYS   B 2 138  ? 133.811 135.977 111.905 1.00 59.27  ? 138  LYS   A CG  1 
ATOM   3416  C  CD  . LYS   B 2 138  ? 132.762 135.082 112.536 1.00 60.69  ? 138  LYS   A CD  1 
ATOM   3417  C  CE  . LYS   B 2 138  ? 131.465 135.127 111.751 1.00 57.58  ? 138  LYS   A CE  1 
ATOM   3418  N  NZ  . LYS   B 2 138  ? 131.659 134.753 110.325 1.00 59.67  ? 138  LYS   A NZ  1 
ATOM   3419  N  N   . ASP   B 2 139  ? 132.523 139.638 109.771 1.00 62.39  ? 139  ASP   A N   1 
ATOM   3420  C  CA  . ASP   B 2 139  ? 131.832 140.146 108.591 1.00 63.98  ? 139  ASP   A CA  1 
ATOM   3421  C  C   . ASP   B 2 139  ? 132.758 140.995 107.730 1.00 69.09  ? 139  ASP   A C   1 
ATOM   3422  O  O   . ASP   B 2 139  ? 132.665 140.976 106.498 1.00 71.69  ? 139  ASP   A O   1 
ATOM   3423  C  CB  . ASP   B 2 139  ? 130.601 140.946 109.012 1.00 67.46  ? 139  ASP   A CB  1 
ATOM   3424  C  CG  . ASP   B 2 139  ? 129.603 140.110 109.786 1.00 72.91  ? 139  ASP   A CG  1 
ATOM   3425  O  OD1 . ASP   B 2 139  ? 129.434 138.919 109.448 1.00 77.34  ? 139  ASP   A OD1 1 
ATOM   3426  O  OD2 . ASP   B 2 139  ? 128.991 140.641 110.736 1.00 69.90  ? 139  ASP   A OD2 1 
ATOM   3427  N  N   . GLY   B 2 140  ? 133.664 141.741 108.361 1.00 70.49  ? 140  GLY   A N   1 
ATOM   3428  C  CA  . GLY   B 2 140  ? 134.603 142.550 107.608 1.00 69.09  ? 140  GLY   A CA  1 
ATOM   3429  C  C   . GLY   B 2 140  ? 135.591 141.716 106.821 1.00 74.16  ? 140  GLY   A C   1 
ATOM   3430  O  O   . GLY   B 2 140  ? 135.930 142.056 105.689 1.00 78.16  ? 140  GLY   A O   1 
ATOM   3431  N  N   . TYR   B 2 141  ? 136.073 140.619 107.407 1.00 76.81  ? 141  TYR   A N   1 
ATOM   3432  C  CA  . TYR   B 2 141  ? 136.953 139.724 106.664 1.00 73.99  ? 141  TYR   A CA  1 
ATOM   3433  C  C   . TYR   B 2 141  ? 136.213 139.079 105.499 1.00 74.46  ? 141  TYR   A C   1 
ATOM   3434  O  O   . TYR   B 2 141  ? 136.758 138.962 104.391 1.00 80.63  ? 141  TYR   A O   1 
ATOM   3435  C  CB  . TYR   B 2 141  ? 137.530 138.659 107.594 1.00 76.06  ? 141  TYR   A CB  1 
ATOM   3436  C  CG  . TYR   B 2 141  ? 138.960 138.281 107.279 1.00 81.74  ? 141  TYR   A CG  1 
ATOM   3437  C  CD1 . TYR   B 2 141  ? 139.562 138.684 106.095 1.00 80.33  ? 141  TYR   A CD1 1 
ATOM   3438  C  CD2 . TYR   B 2 141  ? 139.709 137.523 108.169 1.00 80.46  ? 141  TYR   A CD2 1 
ATOM   3439  C  CE1 . TYR   B 2 141  ? 140.869 138.342 105.806 1.00 80.28  ? 141  TYR   A CE1 1 
ATOM   3440  C  CE2 . TYR   B 2 141  ? 141.016 137.175 107.888 1.00 79.52  ? 141  TYR   A CE2 1 
ATOM   3441  C  CZ  . TYR   B 2 141  ? 141.591 137.587 106.705 1.00 82.49  ? 141  TYR   A CZ  1 
ATOM   3442  O  OH  . TYR   B 2 141  ? 142.893 137.245 106.419 1.00 81.59  ? 141  TYR   A OH  1 
ATOM   3443  N  N   . GLU   B 2 142  ? 134.963 138.668 105.727 1.00 67.18  ? 142  GLU   A N   1 
ATOM   3444  C  CA  . GLU   B 2 142  ? 134.166 138.107 104.639 1.00 68.50  ? 142  GLU   A CA  1 
ATOM   3445  C  C   . GLU   B 2 142  ? 133.994 139.117 103.511 1.00 68.80  ? 142  GLU   A C   1 
ATOM   3446  O  O   . GLU   B 2 142  ? 134.176 138.793 102.329 1.00 73.72  ? 142  GLU   A O   1 
ATOM   3447  C  CB  . GLU   B 2 142  ? 132.803 137.653 105.164 1.00 70.27  ? 142  GLU   A CB  1 
ATOM   3448  C  CG  . GLU   B 2 142  ? 132.851 136.635 106.295 1.00 70.45  ? 142  GLU   A CG  1 
ATOM   3449  C  CD  . GLU   B 2 142  ? 133.124 135.222 105.820 1.00 71.80  ? 142  GLU   A CD  1 
ATOM   3450  O  OE1 . GLU   B 2 142  ? 134.146 134.999 105.137 1.00 73.09  ? 142  GLU   A OE1 1 
ATOM   3451  O  OE2 . GLU   B 2 142  ? 132.305 134.331 106.127 1.00 73.43  ? 142  GLU   A OE2 1 
ATOM   3452  N  N   . ASP   B 2 143  ? 133.665 140.359 103.857 1.00 72.27  ? 143  ASP   A N   1 
ATOM   3453  C  CA  . ASP   B 2 143  ? 133.460 141.372 102.834 1.00 74.92  ? 143  ASP   A CA  1 
ATOM   3454  C  C   . ASP   B 2 143  ? 134.761 141.834 102.195 1.00 77.53  ? 143  ASP   A C   1 
ATOM   3455  O  O   . ASP   B 2 143  ? 134.738 142.294 101.055 1.00 82.79  ? 143  ASP   A O   1 
ATOM   3456  C  CB  . ASP   B 2 143  ? 132.712 142.571 103.412 1.00 77.20  ? 143  ASP   A CB  1 
ATOM   3457  C  CG  . ASP   B 2 143  ? 131.754 143.185 102.415 1.00 83.83  ? 143  ASP   A CG  1 
ATOM   3458  O  OD1 . ASP   B 2 143  ? 131.332 142.472 101.481 1.00 85.41  ? 143  ASP   A OD1 1 
ATOM   3459  O  OD2 . ASP   B 2 143  ? 131.431 144.382 102.555 1.00 85.06  ? 143  ASP   A OD2 1 
ATOM   3460  N  N   . ILE   B 2 144  ? 135.895 141.710 102.886 1.00 71.93  ? 144  ILE   A N   1 
ATOM   3461  C  CA  . ILE   B 2 144  ? 137.179 141.999 102.256 1.00 70.16  ? 144  ILE   A CA  1 
ATOM   3462  C  C   . ILE   B 2 144  ? 137.516 140.924 101.232 1.00 76.37  ? 144  ILE   A C   1 
ATOM   3463  O  O   . ILE   B 2 144  ? 138.038 141.219 100.150 1.00 79.48  ? 144  ILE   A O   1 
ATOM   3464  C  CB  . ILE   B 2 144  ? 138.280 142.144 103.322 1.00 71.30  ? 144  ILE   A CB  1 
ATOM   3465  C  CG1 . ILE   B 2 144  ? 138.175 143.502 104.014 1.00 71.20  ? 144  ILE   A CG1 1 
ATOM   3466  C  CG2 . ILE   B 2 144  ? 139.659 141.976 102.706 1.00 75.55  ? 144  ILE   A CG2 1 
ATOM   3467  C  CD1 . ILE   B 2 144  ? 139.249 143.741 105.050 1.00 72.94  ? 144  ILE   A CD1 1 
ATOM   3468  N  N   . LYS   B 2 145  ? 137.219 139.662 101.551 1.00 80.50  ? 145  LYS   A N   1 
ATOM   3469  C  CA  . LYS   B 2 145  ? 137.352 138.610 100.546 1.00 79.11  ? 145  LYS   A CA  1 
ATOM   3470  C  C   . LYS   B 2 145  ? 136.440 138.879 99.355  1.00 79.78  ? 145  LYS   A C   1 
ATOM   3471  O  O   . LYS   B 2 145  ? 136.837 138.686 98.198  1.00 84.96  ? 145  LYS   A O   1 
ATOM   3472  C  CB  . LYS   B 2 145  ? 137.043 137.247 101.162 1.00 79.81  ? 145  LYS   A CB  1 
ATOM   3473  C  CG  . LYS   B 2 145  ? 138.272 136.442 101.546 1.00 80.58  ? 145  LYS   A CG  1 
ATOM   3474  C  CD  . LYS   B 2 145  ? 139.116 137.165 102.577 1.00 78.07  ? 145  LYS   A CD  1 
ATOM   3475  C  CE  . LYS   B 2 145  ? 140.333 136.342 102.956 1.00 79.01  ? 145  LYS   A CE  1 
ATOM   3476  N  NZ  . LYS   B 2 145  ? 139.950 135.040 103.565 1.00 79.45  ? 145  LYS   A NZ  1 
ATOM   3477  N  N   . ARG   B 2 146  ? 135.214 139.333 99.622  1.00 75.35  ? 146  ARG   A N   1 
ATOM   3478  C  CA  . ARG   B 2 146  ? 134.303 139.690 98.538  1.00 77.24  ? 146  ARG   A CA  1 
ATOM   3479  C  C   . ARG   B 2 146  ? 134.849 140.848 97.710  1.00 80.58  ? 146  ARG   A C   1 
ATOM   3480  O  O   . ARG   B 2 146  ? 134.728 140.852 96.480  1.00 86.50  ? 146  ARG   A O   1 
ATOM   3481  C  CB  . ARG   B 2 146  ? 132.927 140.035 99.106  1.00 79.67  ? 146  ARG   A CB  1 
ATOM   3482  C  CG  . ARG   B 2 146  ? 131.793 139.218 98.513  1.00 81.93  ? 146  ARG   A CG  1 
ATOM   3483  C  CD  . ARG   B 2 146  ? 130.527 139.352 99.341  1.00 81.25  ? 146  ARG   A CD  1 
ATOM   3484  N  NE  . ARG   B 2 146  ? 130.735 138.930 100.721 1.00 84.05  ? 146  ARG   A NE  1 
ATOM   3485  C  CZ  . ARG   B 2 146  ? 130.639 137.677 101.145 1.00 84.60  ? 146  ARG   A CZ  1 
ATOM   3486  N  NH1 . ARG   B 2 146  ? 130.345 136.688 100.318 1.00 82.84  ? 146  ARG   A NH1 1 
ATOM   3487  N  NH2 . ARG   B 2 146  ? 130.842 137.411 102.433 1.00 79.78  ? 146  ARG   A NH2 1 
ATOM   3488  N  N   . HIS   B 2 147  ? 135.444 141.846 98.368  1.00 79.34  ? 147  HIS   A N   1 
ATOM   3489  C  CA  . HIS   B 2 147  ? 136.049 142.968 97.657  1.00 77.40  ? 147  HIS   A CA  1 
ATOM   3490  C  C   . HIS   B 2 147  ? 137.196 142.505 96.772  1.00 80.12  ? 147  HIS   A C   1 
ATOM   3491  O  O   . HIS   B 2 147  ? 137.339 142.971 95.639  1.00 85.73  ? 147  HIS   A O   1 
ATOM   3492  C  CB  . HIS   B 2 147  ? 136.548 144.019 98.649  1.00 77.45  ? 147  HIS   A CB  1 
ATOM   3493  C  CG  . HIS   B 2 147  ? 135.514 145.025 99.049  1.00 83.76  ? 147  HIS   A CG  1 
ATOM   3494  N  ND1 . HIS   B 2 147  ? 135.129 146.062 98.228  1.00 84.75  ? 147  HIS   A ND1 1 
ATOM   3495  C  CD2 . HIS   B 2 147  ? 134.805 145.168 100.193 1.00 82.93  ? 147  HIS   A CD2 1 
ATOM   3496  C  CE1 . HIS   B 2 147  ? 134.217 146.793 98.844  1.00 82.53  ? 147  HIS   A CE1 1 
ATOM   3497  N  NE2 . HIS   B 2 147  ? 134.003 146.272 100.039 1.00 79.04  ? 147  HIS   A NE2 1 
ATOM   3498  N  N   . GLN   B 2 148  ? 138.035 141.601 97.280  1.00 79.06  ? 148  GLN   A N   1 
ATOM   3499  C  CA  . GLN   B 2 148  ? 139.130 141.073 96.472  1.00 80.38  ? 148  GLN   A CA  1 
ATOM   3500  C  C   . GLN   B 2 148  ? 138.601 140.313 95.263  1.00 86.45  ? 148  GLN   A C   1 
ATOM   3501  O  O   . GLN   B 2 148  ? 139.105 140.476 94.142  1.00 87.74  ? 148  GLN   A O   1 
ATOM   3502  C  CB  . GLN   B 2 148  ? 140.021 140.168 97.322  1.00 78.98  ? 148  GLN   A CB  1 
ATOM   3503  C  CG  . GLN   B 2 148  ? 140.737 140.878 98.452  1.00 81.11  ? 148  GLN   A CG  1 
ATOM   3504  C  CD  . GLN   B 2 148  ? 141.567 139.933 99.295  1.00 85.62  ? 148  GLN   A CD  1 
ATOM   3505  O  OE1 . GLN   B 2 148  ? 141.657 138.741 99.003  1.00 86.88  ? 148  GLN   A OE1 1 
ATOM   3506  N  NE2 . GLN   B 2 148  ? 142.178 140.460 100.349 1.00 86.12  ? 148  GLN   A NE2 1 
ATOM   3507  N  N   . ALA   B 2 149  ? 137.577 139.482 95.470  1.00 85.31  ? 149  ALA   A N   1 
ATOM   3508  C  CA  . ALA   B 2 149  ? 136.996 138.736 94.360  1.00 79.80  ? 149  ALA   A CA  1 
ATOM   3509  C  C   . ALA   B 2 149  ? 136.394 139.674 93.321  1.00 78.39  ? 149  ALA   A C   1 
ATOM   3510  O  O   . ALA   B 2 149  ? 136.542 139.453 92.113  1.00 80.90  ? 149  ALA   A O   1 
ATOM   3511  C  CB  . ALA   B 2 149  ? 135.942 137.760 94.880  1.00 76.67  ? 149  ALA   A CB  1 
ATOM   3512  N  N   . ASP   B 2 150  ? 135.708 140.726 93.772  1.00 78.57  ? 150  ASP   A N   1 
ATOM   3513  C  CA  . ASP   B 2 150  ? 135.121 141.685 92.844  1.00 81.61  ? 150  ASP   A CA  1 
ATOM   3514  C  C   . ASP   B 2 150  ? 136.198 142.463 92.101  1.00 84.68  ? 150  ASP   A C   1 
ATOM   3515  O  O   . ASP   B 2 150  ? 136.051 142.751 90.908  1.00 86.42  ? 150  ASP   A O   1 
ATOM   3516  C  CB  . ASP   B 2 150  ? 134.194 142.639 93.596  1.00 87.71  ? 150  ASP   A CB  1 
ATOM   3517  C  CG  . ASP   B 2 150  ? 133.170 143.299 92.691  1.00 91.52  ? 150  ASP   A CG  1 
ATOM   3518  O  OD1 . ASP   B 2 150  ? 133.429 143.429 91.476  1.00 92.19  ? 150  ASP   A OD1 1 
ATOM   3519  O  OD2 . ASP   B 2 150  ? 132.099 143.689 93.198  1.00 90.82  ? 150  ASP   A OD2 1 
ATOM   3520  N  N   . HIS   B 2 151  ? 137.281 142.826 92.791  1.00 87.18  ? 151  HIS   A N   1 
ATOM   3521  C  CA  . HIS   B 2 151  ? 138.352 143.579 92.154  1.00 87.22  ? 151  HIS   A CA  1 
ATOM   3522  C  C   . HIS   B 2 151  ? 139.100 142.732 91.136  1.00 88.65  ? 151  HIS   A C   1 
ATOM   3523  O  O   . HIS   B 2 151  ? 139.638 143.269 90.162  1.00 89.04  ? 151  HIS   A O   1 
ATOM   3524  C  CB  . HIS   B 2 151  ? 139.312 144.117 93.214  1.00 85.52  ? 151  HIS   A CB  1 
ATOM   3525  C  CG  . HIS   B 2 151  ? 140.365 145.027 92.668  1.00 86.61  ? 151  HIS   A CG  1 
ATOM   3526  N  ND1 . HIS   B 2 151  ? 141.582 144.569 92.212  1.00 90.18  ? 151  HIS   A ND1 1 
ATOM   3527  C  CD2 . HIS   B 2 151  ? 140.384 146.371 92.504  1.00 84.62  ? 151  HIS   A CD2 1 
ATOM   3528  C  CE1 . HIS   B 2 151  ? 142.305 145.590 91.792  1.00 89.03  ? 151  HIS   A CE1 1 
ATOM   3529  N  NE2 . HIS   B 2 151  ? 141.601 146.695 91.959  1.00 88.50  ? 151  HIS   A NE2 1 
ATOM   3530  N  N   . ARG   B 2 152  ? 139.148 141.414 91.343  1.00 89.95  ? 152  ARG   A N   1 
ATOM   3531  C  CA  . ARG   B 2 152  ? 139.691 140.538 90.310  1.00 87.71  ? 152  ARG   A CA  1 
ATOM   3532  C  C   . ARG   B 2 152  ? 138.852 140.590 89.040  1.00 88.67  ? 152  ARG   A C   1 
ATOM   3533  O  O   . ARG   B 2 152  ? 139.339 140.240 87.959  1.00 89.23  ? 152  ARG   A O   1 
ATOM   3534  C  CB  . ARG   B 2 152  ? 139.788 139.102 90.825  1.00 88.11  ? 152  ARG   A CB  1 
ATOM   3535  C  CG  . ARG   B 2 152  ? 140.899 138.871 91.841  1.00 89.87  ? 152  ARG   A CG  1 
ATOM   3536  C  CD  . ARG   B 2 152  ? 142.211 138.452 91.181  1.00 92.53  ? 152  ARG   A CD  1 
ATOM   3537  N  NE  . ARG   B 2 152  ? 142.812 139.511 90.378  1.00 93.47  ? 152  ARG   A NE  1 
ATOM   3538  C  CZ  . ARG   B 2 152  ? 142.753 139.575 89.055  1.00 93.71  ? 152  ARG   A CZ  1 
ATOM   3539  N  NH1 . ARG   B 2 152  ? 142.121 138.654 88.345  1.00 92.39  ? 152  ARG   A NH1 1 
ATOM   3540  N  NH2 . ARG   B 2 152  ? 143.342 140.590 88.427  1.00 91.79  ? 152  ARG   A NH2 1 
ATOM   3541  N  N   . THR   B 2 153  ? 137.595 141.022 89.148  1.00 81.33  ? 153  THR   A N   1 
ATOM   3542  C  CA  . THR   B 2 153  ? 136.705 141.149 88.001  1.00 79.04  ? 153  THR   A CA  1 
ATOM   3543  C  C   . THR   B 2 153  ? 136.743 142.544 87.391  1.00 80.43  ? 153  THR   A C   1 
ATOM   3544  O  O   . THR   B 2 153  ? 136.822 142.682 86.165  1.00 81.76  ? 153  THR   A O   1 
ATOM   3545  C  CB  . THR   B 2 153  ? 135.269 140.805 88.410  1.00 80.40  ? 153  THR   A CB  1 
ATOM   3546  O  OG1 . THR   B 2 153  ? 135.197 139.429 88.802  1.00 81.12  ? 153  THR   A OG1 1 
ATOM   3547  C  CG2 . THR   B 2 153  ? 134.307 141.052 87.260  1.00 77.69  ? 153  THR   A CG2 1 
ATOM   3548  N  N   . ASN   B 2 154  ? 136.703 143.585 88.223  1.00 84.01  ? 154  ASN   A N   1 
ATOM   3549  C  CA  . ASN   B 2 154  ? 136.665 144.965 87.754  1.00 84.08  ? 154  ASN   A CA  1 
ATOM   3550  C  C   . ASN   B 2 154  ? 138.055 145.564 87.570  1.00 86.25  ? 154  ASN   A C   1 
ATOM   3551  O  O   . ASN   B 2 154  ? 138.223 146.782 87.695  1.00 87.16  ? 154  ASN   A O   1 
ATOM   3552  C  CB  . ASN   B 2 154  ? 135.831 145.828 88.702  1.00 83.23  ? 154  ASN   A CB  1 
ATOM   3553  C  CG  . ASN   B 2 154  ? 136.331 145.785 90.130  1.00 87.56  ? 154  ASN   A CG  1 
ATOM   3554  O  OD1 . ASN   B 2 154  ? 137.403 146.302 90.444  1.00 88.14  ? 154  ASN   A OD1 1 
ATOM   3555  N  ND2 . ASN   B 2 154  ? 135.543 145.183 91.012  1.00 86.22  ? 154  ASN   A ND2 1 
ATOM   3556  N  N   . HIS   B 2 155  ? 139.065 144.737 87.307  1.00 85.58  ? 155  HIS   A N   1 
ATOM   3557  C  CA  . HIS   B 2 155  ? 140.380 145.252 86.949  1.00 85.82  ? 155  HIS   A CA  1 
ATOM   3558  C  C   . HIS   B 2 155  ? 141.015 144.431 85.836  1.00 85.22  ? 155  HIS   A C   1 
ATOM   3559  O  O   . HIS   B 2 155  ? 142.241 144.290 85.785  1.00 86.26  ? 155  HIS   A O   1 
ATOM   3560  C  CB  . HIS   B 2 155  ? 141.306 145.309 88.164  1.00 88.21  ? 155  HIS   A CB  1 
ATOM   3561  C  CG  . HIS   B 2 155  ? 141.396 146.669 88.784  1.00 85.11  ? 155  HIS   A CG  1 
ATOM   3562  N  ND1 . HIS   B 2 155  ? 140.282 147.393 89.151  1.00 84.83  ? 155  HIS   A ND1 1 
ATOM   3563  C  CD2 . HIS   B 2 155  ? 142.464 147.444 89.086  1.00 83.12  ? 155  HIS   A CD2 1 
ATOM   3564  C  CE1 . HIS   B 2 155  ? 140.661 148.552 89.659  1.00 84.79  ? 155  HIS   A CE1 1 
ATOM   3565  N  NE2 . HIS   B 2 155  ? 141.980 148.607 89.632  1.00 83.90  ? 155  HIS   A NE2 1 
ATOM   3566  N  N   . ALA   B 2 156  ? 140.199 143.886 84.938  1.00 85.55  ? 156  ALA   A N   1 
ATOM   3567  C  CA  . ALA   B 2 156  ? 140.707 143.134 83.800  1.00 85.01  ? 156  ALA   A CA  1 
ATOM   3568  C  C   . ALA   B 2 156  ? 141.147 144.110 82.709  1.00 85.61  ? 156  ALA   A C   1 
ATOM   3569  O  O   . ALA   B 2 156  ? 141.126 145.331 82.886  1.00 88.67  ? 156  ALA   A O   1 
ATOM   3570  C  CB  . ALA   B 2 156  ? 139.654 142.146 83.307  1.00 83.27  ? 156  ALA   A CB  1 
ATOM   3571  N  N   . ILE   B 2 157  ? 141.548 143.578 81.560  1.00 77.84  ? 157  ILE   A N   1 
ATOM   3572  C  CA  . ILE   B 2 157  ? 142.081 144.373 80.460  1.00 78.04  ? 157  ILE   A CA  1 
ATOM   3573  C  C   . ILE   B 2 157  ? 141.038 144.423 79.351  1.00 82.37  ? 157  ILE   A C   1 
ATOM   3574  O  O   . ILE   B 2 157  ? 140.618 143.381 78.832  1.00 86.69  ? 157  ILE   A O   1 
ATOM   3575  C  CB  . ILE   B 2 157  ? 143.412 143.800 79.946  1.00 81.06  ? 157  ILE   A CB  1 
ATOM   3576  C  CG1 . ILE   B 2 157  ? 143.715 144.305 78.533  1.00 83.25  ? 157  ILE   A CG1 1 
ATOM   3577  C  CG2 . ILE   B 2 157  ? 143.396 142.276 79.990  1.00 79.38  ? 157  ILE   A CG2 1 
ATOM   3578  C  CD1 . ILE   B 2 157  ? 143.997 145.787 78.457  1.00 81.23  ? 157  ILE   A CD1 1 
ATOM   3579  N  N   . VAL   B 2 158  ? 140.617 145.634 78.995  1.00 68.43  ? 158  VAL   A N   1 
ATOM   3580  C  CA  . VAL   B 2 158  ? 139.764 145.869 77.835  1.00 68.03  ? 158  VAL   A CA  1 
ATOM   3581  C  C   . VAL   B 2 158  ? 140.303 147.085 77.096  1.00 71.55  ? 158  VAL   A C   1 
ATOM   3582  O  O   . VAL   B 2 158  ? 140.577 148.121 77.712  1.00 77.21  ? 158  VAL   A O   1 
ATOM   3583  C  CB  . VAL   B 2 158  ? 138.287 146.069 78.231  1.00 65.21  ? 158  VAL   A CB  1 
ATOM   3584  C  CG1 . VAL   B 2 158  ? 137.596 147.010 77.269  1.00 67.28  ? 158  VAL   A CG1 1 
ATOM   3585  C  CG2 . VAL   B 2 158  ? 137.570 144.735 78.235  1.00 71.98  ? 158  VAL   A CG2 1 
ATOM   3586  N  N   . HIS   B 2 159  ? 140.470 146.956 75.783  1.00 66.41  ? 159  HIS   A N   1 
ATOM   3587  C  CA  . HIS   B 2 159  ? 141.026 148.022 74.962  1.00 64.83  ? 159  HIS   A CA  1 
ATOM   3588  C  C   . HIS   B 2 159  ? 139.904 148.958 74.529  1.00 69.09  ? 159  HIS   A C   1 
ATOM   3589  O  O   . HIS   B 2 159  ? 138.965 148.534 73.849  1.00 73.45  ? 159  HIS   A O   1 
ATOM   3590  C  CB  . HIS   B 2 159  ? 141.749 147.444 73.747  1.00 64.65  ? 159  HIS   A CB  1 
ATOM   3591  C  CG  . HIS   B 2 159  ? 142.935 146.599 74.092  1.00 68.55  ? 159  HIS   A CG  1 
ATOM   3592  N  ND1 . HIS   B 2 159  ? 142.858 145.515 74.940  1.00 70.90  ? 159  HIS   A ND1 1 
ATOM   3593  C  CD2 . HIS   B 2 159  ? 144.228 146.675 73.698  1.00 70.70  ? 159  HIS   A CD2 1 
ATOM   3594  C  CE1 . HIS   B 2 159  ? 144.052 144.962 75.055  1.00 71.65  ? 159  HIS   A CE1 1 
ATOM   3595  N  NE2 . HIS   B 2 159  ? 144.901 145.647 74.312  1.00 71.42  ? 159  HIS   A NE2 1 
ATOM   3596  N  N   . VAL   B 2 160  ? 140.004 150.226 74.921  1.00 68.97  ? 160  VAL   A N   1 
ATOM   3597  C  CA  . VAL   B 2 160  ? 138.998 151.233 74.609  1.00 65.07  ? 160  VAL   A CA  1 
ATOM   3598  C  C   . VAL   B 2 160  ? 139.669 152.388 73.881  1.00 67.87  ? 160  VAL   A C   1 
ATOM   3599  O  O   . VAL   B 2 160  ? 140.796 152.772 74.210  1.00 76.76  ? 160  VAL   A O   1 
ATOM   3600  C  CB  . VAL   B 2 160  ? 138.277 151.734 75.876  1.00 70.54  ? 160  VAL   A CB  1 
ATOM   3601  C  CG1 . VAL   B 2 160  ? 137.190 152.732 75.518  1.00 73.68  ? 160  VAL   A CG1 1 
ATOM   3602  C  CG2 . VAL   B 2 160  ? 137.689 150.568 76.634  1.00 71.78  ? 160  VAL   A CG2 1 
ATOM   3603  N  N   . LEU   B 2 161  ? 138.976 152.931 72.884  1.00 81.99  ? 161  LEU   A N   1 
ATOM   3604  C  CA  . LEU   B 2 161  ? 139.507 154.050 72.120  1.00 87.23  ? 161  LEU   A CA  1 
ATOM   3605  C  C   . LEU   B 2 161  ? 139.697 155.269 73.013  1.00 93.20  ? 161  LEU   A C   1 
ATOM   3606  O  O   . LEU   B 2 161  ? 138.859 155.574 73.866  1.00 95.69  ? 161  LEU   A O   1 
ATOM   3607  C  CB  . LEU   B 2 161  ? 138.564 154.383 70.966  1.00 85.96  ? 161  LEU   A CB  1 
ATOM   3608  C  CG  . LEU   B 2 161  ? 138.986 155.500 70.019  1.00 88.88  ? 161  LEU   A CG  1 
ATOM   3609  C  CD1 . LEU   B 2 161  ? 140.313 155.160 69.365  1.00 90.36  ? 161  LEU   A CD1 1 
ATOM   3610  C  CD2 . LEU   B 2 161  ? 137.906 155.723 68.976  1.00 90.02  ? 161  LEU   A CD2 1 
ATOM   3611  N  N   . GLY   B 2 162  ? 140.814 155.970 72.812  1.00 103.73 ? 162  GLY   A N   1 
ATOM   3612  C  CA  . GLY   B 2 162  ? 141.124 157.140 73.599  1.00 103.02 ? 162  GLY   A CA  1 
ATOM   3613  C  C   . GLY   B 2 162  ? 141.529 158.304 72.716  1.00 104.55 ? 162  GLY   A C   1 
ATOM   3614  O  O   . GLY   B 2 162  ? 142.006 158.133 71.594  1.00 104.19 ? 162  GLY   A O   1 
ATOM   3615  N  N   . GLY   B 2 163  ? 141.329 159.506 73.253  1.00 115.26 ? 163  GLY   A N   1 
ATOM   3616  C  CA  . GLY   B 2 163  ? 141.658 160.734 72.563  1.00 114.27 ? 163  GLY   A CA  1 
ATOM   3617  C  C   . GLY   B 2 163  ? 140.500 161.393 71.846  1.00 115.20 ? 163  GLY   A C   1 
ATOM   3618  O  O   . GLY   B 2 163  ? 140.580 162.591 71.548  1.00 114.40 ? 163  GLY   A O   1 
ATOM   3619  N  N   . GLN   B 2 164  ? 139.428 160.657 71.571  1.00 121.29 ? 164  GLN   A N   1 
ATOM   3620  C  CA  . GLN   B 2 164  ? 138.274 161.218 70.878  1.00 121.00 ? 164  GLN   A CA  1 
ATOM   3621  C  C   . GLN   B 2 164  ? 137.469 162.128 71.800  1.00 121.07 ? 164  GLN   A C   1 
ATOM   3622  O  O   . GLN   B 2 164  ? 137.777 163.311 71.943  1.00 121.38 ? 164  GLN   A O   1 
ATOM   3623  C  CB  . GLN   B 2 164  ? 137.388 160.099 70.323  1.00 121.25 ? 164  GLN   A CB  1 
ATOM   3624  C  CG  . GLN   B 2 164  ? 137.103 158.968 71.303  1.00 121.92 ? 164  GLN   A CG  1 
ATOM   3625  C  CD  . GLN   B 2 164  ? 136.008 159.306 72.297  1.00 123.03 ? 164  GLN   A CD  1 
ATOM   3626  O  OE1 . GLN   B 2 164  ? 135.157 160.156 72.037  1.00 122.10 ? 164  GLN   A OE1 1 
ATOM   3627  N  NE2 . GLN   B 2 164  ? 136.026 158.638 73.445  1.00 122.18 ? 164  GLN   A NE2 1 
ATOM   3628  N  N   . GLY   B 2 251  ? 149.297 160.085 73.599  1.00 109.06 ? 251  GLY   A N   1 
ATOM   3629  C  CA  . GLY   B 2 251  ? 148.650 159.139 72.709  1.00 110.04 ? 251  GLY   A CA  1 
ATOM   3630  C  C   . GLY   B 2 251  ? 147.385 159.687 72.076  1.00 110.01 ? 251  GLY   A C   1 
ATOM   3631  O  O   . GLY   B 2 251  ? 146.632 160.424 72.712  1.00 108.54 ? 251  GLY   A O   1 
ATOM   3632  N  N   . GLU   B 2 252  ? 147.153 159.325 70.816  1.00 112.42 ? 252  GLU   A N   1 
ATOM   3633  C  CA  . GLU   B 2 252  ? 145.980 159.792 70.093  1.00 112.03 ? 252  GLU   A CA  1 
ATOM   3634  C  C   . GLU   B 2 252  ? 145.680 158.814 68.965  1.00 111.76 ? 252  GLU   A C   1 
ATOM   3635  O  O   . GLU   B 2 252  ? 146.599 158.214 68.401  1.00 112.11 ? 252  GLU   A O   1 
ATOM   3636  C  CB  . GLU   B 2 252  ? 146.197 161.206 69.541  1.00 111.87 ? 252  GLU   A CB  1 
ATOM   3637  C  CG  . GLU   B 2 252  ? 144.919 161.945 69.175  1.00 113.13 ? 252  GLU   A CG  1 
ATOM   3638  C  CD  . GLU   B 2 252  ? 144.158 162.447 70.387  1.00 114.44 ? 252  GLU   A CD  1 
ATOM   3639  O  OE1 . GLU   B 2 252  ? 144.697 162.364 71.511  1.00 112.76 ? 252  GLU   A OE1 1 
ATOM   3640  O  OE2 . GLU   B 2 252  ? 143.020 162.929 70.214  1.00 114.80 ? 252  GLU   A OE2 1 
ATOM   3641  N  N   . LEU   B 2 253  ? 144.392 158.666 68.645  1.00 106.30 ? 253  LEU   A N   1 
ATOM   3642  C  CA  . LEU   B 2 253  ? 143.929 157.756 67.593  1.00 105.11 ? 253  LEU   A CA  1 
ATOM   3643  C  C   . LEU   B 2 253  ? 144.435 156.333 67.821  1.00 104.99 ? 253  LEU   A C   1 
ATOM   3644  O  O   . LEU   B 2 253  ? 144.867 155.653 66.888  1.00 106.02 ? 253  LEU   A O   1 
ATOM   3645  C  CB  . LEU   B 2 253  ? 144.335 158.250 66.201  1.00 106.85 ? 253  LEU   A CB  1 
ATOM   3646  C  CG  . LEU   B 2 253  ? 143.834 159.598 65.671  1.00 106.89 ? 253  LEU   A CG  1 
ATOM   3647  C  CD1 . LEU   B 2 253  ? 142.503 159.999 66.298  1.00 106.84 ? 253  LEU   A CD1 1 
ATOM   3648  C  CD2 . LEU   B 2 253  ? 144.882 160.687 65.855  1.00 106.47 ? 253  LEU   A CD2 1 
ATOM   3649  N  N   . GLY   B 2 254  ? 144.386 155.876 69.071  1.00 97.14  ? 254  GLY   A N   1 
ATOM   3650  C  CA  . GLY   B 2 254  ? 144.862 154.551 69.404  1.00 97.22  ? 254  GLY   A CA  1 
ATOM   3651  C  C   . GLY   B 2 254  ? 143.970 153.892 70.436  1.00 96.16  ? 254  GLY   A C   1 
ATOM   3652  O  O   . GLY   B 2 254  ? 143.192 154.548 71.133  1.00 98.05  ? 254  GLY   A O   1 
ATOM   3653  N  N   . TRP   B 2 255  ? 144.096 152.570 70.521  1.00 79.15  ? 255  TRP   A N   1 
ATOM   3654  C  CA  . TRP   B 2 255  ? 143.334 151.775 71.478  1.00 78.70  ? 255  TRP   A CA  1 
ATOM   3655  C  C   . TRP   B 2 255  ? 144.174 151.586 72.735  1.00 79.59  ? 255  TRP   A C   1 
ATOM   3656  O  O   . TRP   B 2 255  ? 145.125 150.798 72.744  1.00 81.41  ? 255  TRP   A O   1 
ATOM   3657  C  CB  . TRP   B 2 255  ? 142.930 150.432 70.874  1.00 81.02  ? 255  TRP   A CB  1 
ATOM   3658  C  CG  . TRP   B 2 255  ? 141.495 150.390 70.452  1.00 81.79  ? 255  TRP   A CG  1 
ATOM   3659  C  CD1 . TRP   B 2 255  ? 140.403 150.459 71.265  1.00 82.67  ? 255  TRP   A CD1 1 
ATOM   3660  C  CD2 . TRP   B 2 255  ? 140.993 150.266 69.117  1.00 77.17  ? 255  TRP   A CD2 1 
ATOM   3661  N  NE1 . TRP   B 2 255  ? 139.252 150.391 70.521  1.00 84.00  ? 255  TRP   A NE1 1 
ATOM   3662  C  CE2 . TRP   B 2 255  ? 139.587 150.272 69.198  1.00 76.66  ? 255  TRP   A CE2 1 
ATOM   3663  C  CE3 . TRP   B 2 255  ? 141.594 150.154 67.862  1.00 79.63  ? 255  TRP   A CE3 1 
ATOM   3664  C  CZ2 . TRP   B 2 255  ? 138.776 150.170 68.075  1.00 73.32  ? 255  TRP   A CZ2 1 
ATOM   3665  C  CZ3 . TRP   B 2 255  ? 140.785 150.051 66.749  1.00 80.01  ? 255  TRP   A CZ3 1 
ATOM   3666  C  CH2 . TRP   B 2 255  ? 139.392 150.061 66.862  1.00 75.58  ? 255  TRP   A CH2 1 
ATOM   3667  N  N   . HIS   B 2 256  ? 143.818 152.303 73.794  1.00 85.19  ? 256  HIS   A N   1 
ATOM   3668  C  CA  . HIS   B 2 256  ? 144.544 152.265 75.053  1.00 83.09  ? 256  HIS   A CA  1 
ATOM   3669  C  C   . HIS   B 2 256  ? 143.884 151.284 76.013  1.00 80.77  ? 256  HIS   A C   1 
ATOM   3670  O  O   . HIS   B 2 256  ? 142.679 151.033 75.945  1.00 84.32  ? 256  HIS   A O   1 
ATOM   3671  C  CB  . HIS   B 2 256  ? 144.604 153.654 75.690  1.00 83.45  ? 256  HIS   A CB  1 
ATOM   3672  C  CG  . HIS   B 2 256  ? 145.113 154.720 74.771  1.00 86.16  ? 256  HIS   A CG  1 
ATOM   3673  N  ND1 . HIS   B 2 256  ? 144.354 155.247 73.749  1.00 86.58  ? 256  HIS   A ND1 1 
ATOM   3674  C  CD2 . HIS   B 2 256  ? 146.305 155.361 74.722  1.00 85.77  ? 256  HIS   A CD2 1 
ATOM   3675  C  CE1 . HIS   B 2 256  ? 145.056 156.165 73.109  1.00 86.65  ? 256  HIS   A CE1 1 
ATOM   3676  N  NE2 . HIS   B 2 256  ? 146.243 156.253 73.679  1.00 87.47  ? 256  HIS   A NE2 1 
ATOM   3677  N  N   . ARG   B 2 257  ? 144.692 150.729 76.910  1.00 68.34  ? 257  ARG   A N   1 
ATOM   3678  C  CA  . ARG   B 2 257  ? 144.187 149.775 77.885  1.00 66.26  ? 257  ARG   A CA  1 
ATOM   3679  C  C   . ARG   B 2 257  ? 143.281 150.468 78.894  1.00 73.73  ? 257  ARG   A C   1 
ATOM   3680  O  O   . ARG   B 2 257  ? 143.503 151.624 79.263  1.00 79.87  ? 257  ARG   A O   1 
ATOM   3681  C  CB  . ARG   B 2 257  ? 145.350 149.094 78.606  1.00 65.79  ? 257  ARG   A CB  1 
ATOM   3682  C  CG  . ARG   B 2 257  ? 146.403 148.528 77.674  1.00 70.77  ? 257  ARG   A CG  1 
ATOM   3683  C  CD  . ARG   B 2 257  ? 147.600 148.005 78.445  1.00 71.91  ? 257  ARG   A CD  1 
ATOM   3684  N  NE  . ARG   B 2 257  ? 147.274 146.827 79.238  1.00 70.99  ? 257  ARG   A NE  1 
ATOM   3685  C  CZ  . ARG   B 2 257  ? 147.426 145.579 78.818  1.00 74.12  ? 257  ARG   A CZ  1 
ATOM   3686  N  NH1 . ARG   B 2 257  ? 147.891 145.307 77.610  1.00 74.02  ? 257  ARG   A NH1 1 
ATOM   3687  N  NH2 . ARG   B 2 257  ? 147.103 144.577 79.631  1.00 72.93  ? 257  ARG   A NH2 1 
ATOM   3688  N  N   . THR   B 2 258  ? 142.250 149.753 79.340  1.00 67.88  ? 258  THR   A N   1 
ATOM   3689  C  CA  . THR   B 2 258  ? 141.381 150.251 80.399  1.00 69.65  ? 258  THR   A CA  1 
ATOM   3690  C  C   . THR   B 2 258  ? 141.256 149.219 81.511  1.00 69.11  ? 258  THR   A C   1 
ATOM   3691  O  O   . THR   B 2 258  ? 141.986 148.222 81.525  1.00 70.63  ? 258  THR   A O   1 
ATOM   3692  C  CB  . THR   B 2 258  ? 140.001 150.616 79.857  1.00 68.07  ? 258  THR   A CB  1 
ATOM   3693  O  OG1 . THR   B 2 258  ? 139.512 149.549 79.036  1.00 72.18  ? 258  THR   A OG1 1 
ATOM   3694  C  CG2 . THR   B 2 258  ? 140.073 151.898 79.046  1.00 70.85  ? 258  THR   A CG2 1 
ATOM   3695  N  N   . ILE   B 2 259  ? 140.334 149.446 82.443  1.00 75.93  ? 259  ILE   A N   1 
ATOM   3696  C  CA  . ILE   B 2 259  ? 140.308 148.678 83.681  1.00 77.77  ? 259  ILE   A CA  1 
ATOM   3697  C  C   . ILE   B 2 259  ? 138.890 148.200 83.981  1.00 82.17  ? 259  ILE   A C   1 
ATOM   3698  O  O   . ILE   B 2 259  ? 138.575 147.830 85.118  1.00 83.78  ? 259  ILE   A O   1 
ATOM   3699  C  CB  . ILE   B 2 259  ? 140.893 149.521 84.833  1.00 81.68  ? 259  ILE   A CB  1 
ATOM   3700  C  CG1 . ILE   B 2 259  ? 141.398 148.628 85.969  1.00 80.78  ? 259  ILE   A CG1 1 
ATOM   3701  C  CG2 . ILE   B 2 259  ? 139.897 150.576 85.309  1.00 82.80  ? 259  ILE   A CG2 1 
ATOM   3702  C  CD1 . ILE   B 2 259  ? 142.615 147.806 85.598  1.00 79.11  ? 259  ILE   A CD1 1 
ATOM   3703  N  N   . TRP   B 2 260  ? 138.033 148.193 82.959  1.00 81.22  ? 260  TRP   A N   1 
ATOM   3704  C  CA  . TRP   B 2 260  ? 136.623 147.804 83.009  1.00 77.09  ? 260  TRP   A CA  1 
ATOM   3705  C  C   . TRP   B 2 260  ? 135.751 148.813 83.739  1.00 78.16  ? 260  TRP   A C   1 
ATOM   3706  O  O   . TRP   B 2 260  ? 134.553 148.561 83.904  1.00 81.90  ? 260  TRP   A O   1 
ATOM   3707  C  CB  . TRP   B 2 260  ? 136.392 146.432 83.660  1.00 73.04  ? 260  TRP   A CB  1 
ATOM   3708  C  CG  . TRP   B 2 260  ? 136.708 145.261 82.795  1.00 74.03  ? 260  TRP   A CG  1 
ATOM   3709  C  CD1 . TRP   B 2 260  ? 137.728 145.152 81.900  1.00 78.05  ? 260  TRP   A CD1 1 
ATOM   3710  C  CD2 . TRP   B 2 260  ? 135.991 144.022 82.739  1.00 77.32  ? 260  TRP   A CD2 1 
ATOM   3711  N  NE1 . TRP   B 2 260  ? 137.696 143.920 81.295  1.00 79.12  ? 260  TRP   A NE1 1 
ATOM   3712  C  CE2 . TRP   B 2 260  ? 136.635 143.209 81.791  1.00 76.51  ? 260  TRP   A CE2 1 
ATOM   3713  C  CE3 . TRP   B 2 260  ? 134.867 143.522 83.402  1.00 80.30  ? 260  TRP   A CE3 1 
ATOM   3714  C  CZ2 . TRP   B 2 260  ? 136.195 141.925 81.488  1.00 73.14  ? 260  TRP   A CZ2 1 
ATOM   3715  C  CZ3 . TRP   B 2 260  ? 134.432 142.247 83.100  1.00 77.16  ? 260  TRP   A CZ3 1 
ATOM   3716  C  CH2 . TRP   B 2 260  ? 135.093 141.463 82.152  1.00 71.71  ? 260  TRP   A CH2 1 
ATOM   3717  N  N   . GLU   B 2 261  ? 136.300 149.935 84.194  1.00 81.26  ? 261  GLU   A N   1 
ATOM   3718  C  CA  . GLU   B 2 261  ? 135.539 150.927 84.943  1.00 79.33  ? 261  GLU   A CA  1 
ATOM   3719  C  C   . GLU   B 2 261  ? 135.375 152.246 84.210  1.00 81.29  ? 261  GLU   A C   1 
ATOM   3720  O  O   . GLU   B 2 261  ? 134.309 152.858 84.288  1.00 83.16  ? 261  GLU   A O   1 
ATOM   3721  C  CB  . GLU   B 2 261  ? 136.198 151.180 86.302  1.00 79.06  ? 261  GLU   A CB  1 
ATOM   3722  C  CG  . GLU   B 2 261  ? 135.629 150.327 87.418  1.00 82.04  ? 261  GLU   A CG  1 
ATOM   3723  C  CD  . GLU   B 2 261  ? 135.324 148.914 86.970  1.00 86.03  ? 261  GLU   A CD  1 
ATOM   3724  O  OE1 . GLU   B 2 261  ? 136.268 148.195 86.591  1.00 86.40  ? 261  GLU   A OE1 1 
ATOM   3725  O  OE2 . GLU   B 2 261  ? 134.139 148.524 86.978  1.00 88.88  ? 261  GLU   A OE2 1 
ATOM   3726  N  N   . ASP   B 2 262  ? 136.399 152.698 83.490  1.00 87.64  ? 262  ASP   A N   1 
ATOM   3727  C  CA  . ASP   B 2 262  ? 136.281 153.918 82.703  1.00 90.90  ? 262  ASP   A CA  1 
ATOM   3728  C  C   . ASP   B 2 262  ? 135.604 153.623 81.371  1.00 93.97  ? 262  ASP   A C   1 
ATOM   3729  O  O   . ASP   B 2 262  ? 136.107 154.013 80.312  1.00 95.87  ? 262  ASP   A O   1 
ATOM   3730  C  CB  . ASP   B 2 262  ? 137.658 154.546 82.471  1.00 92.36  ? 262  ASP   A CB  1 
ATOM   3731  C  CG  . ASP   B 2 262  ? 138.347 154.936 83.763  1.00 93.45  ? 262  ASP   A CG  1 
ATOM   3732  O  OD1 . ASP   B 2 262  ? 137.641 155.243 84.745  1.00 94.03  ? 262  ASP   A OD1 1 
ATOM   3733  O  OD2 . ASP   B 2 262  ? 139.596 154.937 83.796  1.00 91.91  ? 262  ASP   A OD2 1 
ATOM   3734  N  N   . VAL   B 2 263  ? 134.461 152.939 81.413  1.00 72.76  ? 263  VAL   A N   1 
ATOM   3735  C  CA  . VAL   B 2 263  ? 133.732 152.537 80.212  1.00 69.20  ? 263  VAL   A CA  1 
ATOM   3736  C  C   . VAL   B 2 263  ? 132.269 152.914 80.430  1.00 72.74  ? 263  VAL   A C   1 
ATOM   3737  O  O   . VAL   B 2 263  ? 131.488 152.147 81.004  1.00 77.25  ? 263  VAL   A O   1 
ATOM   3738  C  CB  . VAL   B 2 263  ? 133.883 151.045 79.901  1.00 68.71  ? 263  VAL   A CB  1 
ATOM   3739  C  CG1 . VAL   B 2 263  ? 135.152 150.804 79.116  1.00 72.86  ? 263  VAL   A CG1 1 
ATOM   3740  C  CG2 . VAL   B 2 263  ? 133.912 150.235 81.180  1.00 66.86  ? 263  VAL   A CG2 1 
ATOM   3741  N  N   . LYS   B 2 264  ? 131.887 154.100 79.970  1.00 75.10  ? 264  LYS   A N   1 
ATOM   3742  C  CA  . LYS   B 2 264  ? 130.501 154.529 80.021  1.00 78.64  ? 264  LYS   A CA  1 
ATOM   3743  C  C   . LYS   B 2 264  ? 129.761 154.010 78.792  1.00 70.75  ? 264  LYS   A C   1 
ATOM   3744  O  O   . LYS   B 2 264  ? 130.334 153.348 77.925  1.00 74.10  ? 264  LYS   A O   1 
ATOM   3745  C  CB  . LYS   B 2 264  ? 130.413 156.051 80.121  1.00 79.52  ? 264  LYS   A CB  1 
ATOM   3746  C  CG  . LYS   B 2 264  ? 130.198 156.578 81.531  1.00 80.16  ? 264  LYS   A CG  1 
ATOM   3747  C  CD  . LYS   B 2 264  ? 131.328 156.177 82.461  1.00 80.48  ? 264  LYS   A CD  1 
ATOM   3748  C  CE  . LYS   B 2 264  ? 131.078 156.684 83.871  1.00 78.32  ? 264  LYS   A CE  1 
ATOM   3749  N  NZ  . LYS   B 2 264  ? 129.788 156.177 84.415  1.00 78.44  ? 264  LYS   A NZ  1 
ATOM   3750  N  N   . VAL   B 2 265  ? 128.465 154.308 78.717  1.00 60.81  ? 265  VAL   A N   1 
ATOM   3751  C  CA  . VAL   B 2 265  ? 127.701 153.956 77.528  1.00 63.51  ? 265  VAL   A CA  1 
ATOM   3752  C  C   . VAL   B 2 265  ? 128.272 154.724 76.348  1.00 67.66  ? 265  VAL   A C   1 
ATOM   3753  O  O   . VAL   B 2 265  ? 128.498 155.938 76.426  1.00 75.37  ? 265  VAL   A O   1 
ATOM   3754  C  CB  . VAL   B 2 265  ? 126.214 154.249 77.732  1.00 71.47  ? 265  VAL   A CB  1 
ATOM   3755  C  CG1 . VAL   B 2 265  ? 125.409 153.718 76.561  1.00 72.89  ? 265  VAL   A CG1 1 
ATOM   3756  C  CG2 . VAL   B 2 265  ? 125.735 153.627 79.024  1.00 69.69  ? 265  VAL   A CG2 1 
ATOM   3757  N  N   . GLY   B 2 266  ? 128.525 154.014 75.247  1.00 71.28  ? 266  GLY   A N   1 
ATOM   3758  C  CA  . GLY   B 2 266  ? 129.224 154.567 74.106  1.00 69.55  ? 266  GLY   A CA  1 
ATOM   3759  C  C   . GLY   B 2 266  ? 130.577 153.896 73.925  1.00 71.91  ? 266  GLY   A C   1 
ATOM   3760  O  O   . GLY   B 2 266  ? 130.678 152.664 73.953  1.00 78.85  ? 266  GLY   A O   1 
ATOM   3761  N  N   . ASP   B 2 267  ? 131.609 154.719 73.740  1.00 75.66  ? 267  ASP   A N   1 
ATOM   3762  C  CA  . ASP   B 2 267  ? 132.985 154.252 73.604  1.00 77.88  ? 267  ASP   A CA  1 
ATOM   3763  C  C   . ASP   B 2 267  ? 133.154 153.279 72.442  1.00 81.71  ? 267  ASP   A C   1 
ATOM   3764  O  O   . ASP   B 2 267  ? 132.221 153.045 71.668  1.00 85.12  ? 267  ASP   A O   1 
ATOM   3765  C  CB  . ASP   B 2 267  ? 133.459 153.600 74.905  1.00 74.05  ? 267  ASP   A CB  1 
ATOM   3766  C  CG  . ASP   B 2 267  ? 133.576 154.592 76.042  1.00 82.20  ? 267  ASP   A CG  1 
ATOM   3767  O  OD1 . ASP   B 2 267  ? 133.842 155.782 75.771  1.00 83.71  ? 267  ASP   A OD1 1 
ATOM   3768  O  OD2 . ASP   B 2 267  ? 133.402 154.182 77.209  1.00 83.63  ? 267  ASP   A OD2 1 
ATOM   3769  N  N   . PHE   B 2 268  ? 134.354 152.724 72.305  1.00 70.69  ? 268  PHE   A N   1 
ATOM   3770  C  CA  . PHE   B 2 268  ? 134.635 151.711 71.300  1.00 64.17  ? 268  PHE   A CA  1 
ATOM   3771  C  C   . PHE   B 2 268  ? 135.608 150.709 71.896  1.00 70.88  ? 268  PHE   A C   1 
ATOM   3772  O  O   . PHE   B 2 268  ? 136.710 151.082 72.309  1.00 80.60  ? 268  PHE   A O   1 
ATOM   3773  C  CB  . PHE   B 2 268  ? 135.209 152.332 70.023  1.00 68.40  ? 268  PHE   A CB  1 
ATOM   3774  C  CG  . PHE   B 2 268  ? 134.206 153.117 69.229  1.00 69.91  ? 268  PHE   A CG  1 
ATOM   3775  C  CD1 . PHE   B 2 268  ? 133.334 152.477 68.366  1.00 68.19  ? 268  PHE   A CD1 1 
ATOM   3776  C  CD2 . PHE   B 2 268  ? 134.138 154.493 69.340  1.00 75.93  ? 268  PHE   A CD2 1 
ATOM   3777  C  CE1 . PHE   B 2 268  ? 132.410 153.193 67.633  1.00 67.89  ? 268  PHE   A CE1 1 
ATOM   3778  C  CE2 . PHE   B 2 268  ? 133.216 155.215 68.607  1.00 78.85  ? 268  PHE   A CE2 1 
ATOM   3779  C  CZ  . PHE   B 2 268  ? 132.351 154.562 67.753  1.00 75.23  ? 268  PHE   A CZ  1 
ATOM   3780  N  N   . VAL   B 2 269  ? 135.203 149.444 71.935  1.00 58.99  ? 269  VAL   A N   1 
ATOM   3781  C  CA  . VAL   B 2 269  ? 135.953 148.394 72.610  1.00 56.77  ? 269  VAL   A CA  1 
ATOM   3782  C  C   . VAL   B 2 269  ? 136.372 147.349 71.587  1.00 61.47  ? 269  VAL   A C   1 
ATOM   3783  O  O   . VAL   B 2 269  ? 135.543 146.867 70.807  1.00 69.87  ? 269  VAL   A O   1 
ATOM   3784  C  CB  . VAL   B 2 269  ? 135.133 147.753 73.743  1.00 65.39  ? 269  VAL   A CB  1 
ATOM   3785  C  CG1 . VAL   B 2 269  ? 135.112 148.658 74.954  1.00 67.11  ? 269  VAL   A CG1 1 
ATOM   3786  C  CG2 . VAL   B 2 269  ? 133.716 147.465 73.280  1.00 66.34  ? 269  VAL   A CG2 1 
ATOM   3787  N  N   . LYS   B 2 270  ? 137.656 147.010 71.589  1.00 58.41  ? 270  LYS   A N   1 
ATOM   3788  C  CA  . LYS   B 2 270  ? 138.200 145.911 70.803  1.00 52.43  ? 270  LYS   A CA  1 
ATOM   3789  C  C   . LYS   B 2 270  ? 138.518 144.775 71.765  1.00 58.15  ? 270  LYS   A C   1 
ATOM   3790  O  O   . LYS   B 2 270  ? 139.310 144.955 72.696  1.00 64.50  ? 270  LYS   A O   1 
ATOM   3791  C  CB  . LYS   B 2 270  ? 139.450 146.355 70.045  1.00 59.85  ? 270  LYS   A CB  1 
ATOM   3792  C  CG  . LYS   B 2 270  ? 140.007 145.338 69.067  1.00 65.67  ? 270  LYS   A CG  1 
ATOM   3793  C  CD  . LYS   B 2 270  ? 141.368 145.783 68.560  1.00 61.63  ? 270  LYS   A CD  1 
ATOM   3794  C  CE  . LYS   B 2 270  ? 141.826 144.954 67.380  1.00 61.02  ? 270  LYS   A CE  1 
ATOM   3795  N  NZ  . LYS   B 2 270  ? 140.996 145.222 66.177  1.00 61.63  ? 270  LYS   A NZ  1 
ATOM   3796  N  N   . ILE   B 2 271  ? 137.909 143.611 71.544  1.00 58.41  ? 271  ILE   A N   1 
ATOM   3797  C  CA  . ILE   B 2 271  ? 137.927 142.539 72.534  1.00 59.89  ? 271  ILE   A CA  1 
ATOM   3798  C  C   . ILE   B 2 271  ? 138.788 141.360 72.116  1.00 65.81  ? 271  ILE   A C   1 
ATOM   3799  O  O   . ILE   B 2 271  ? 139.003 140.452 72.930  1.00 71.83  ? 271  ILE   A O   1 
ATOM   3800  C  CB  . ILE   B 2 271  ? 136.501 142.070 72.871  1.00 61.75  ? 271  ILE   A CB  1 
ATOM   3801  C  CG1 . ILE   B 2 271  ? 135.548 143.261 72.872  1.00 69.16  ? 271  ILE   A CG1 1 
ATOM   3802  C  CG2 . ILE   B 2 271  ? 136.470 141.416 74.243  1.00 64.05  ? 271  ILE   A CG2 1 
ATOM   3803  C  CD1 . ILE   B 2 271  ? 135.763 144.206 74.031  1.00 69.57  ? 271  ILE   A CD1 1 
ATOM   3804  N  N   . TYR   B 2 272  ? 139.292 141.340 70.889  1.00 70.99  ? 272  TYR   A N   1 
ATOM   3805  C  CA  . TYR   B 2 272  ? 140.217 140.287 70.450  1.00 71.70  ? 272  TYR   A CA  1 
ATOM   3806  C  C   . TYR   B 2 272  ? 139.527 138.926 70.595  1.00 74.70  ? 272  TYR   A C   1 
ATOM   3807  O  O   . TYR   B 2 272  ? 138.326 138.793 70.325  1.00 79.30  ? 272  TYR   A O   1 
ATOM   3808  C  CB  . TYR   B 2 272  ? 141.532 140.415 71.197  1.00 69.61  ? 272  TYR   A CB  1 
ATOM   3809  C  CG  . TYR   B 2 272  ? 142.315 141.654 70.834  1.00 69.15  ? 272  TYR   A CG  1 
ATOM   3810  C  CD1 . TYR   B 2 272  ? 143.186 141.654 69.755  1.00 68.59  ? 272  TYR   A CD1 1 
ATOM   3811  C  CD2 . TYR   B 2 272  ? 142.180 142.822 71.565  1.00 70.44  ? 272  TYR   A CD2 1 
ATOM   3812  C  CE1 . TYR   B 2 272  ? 143.901 142.781 69.416  1.00 69.27  ? 272  TYR   A CE1 1 
ATOM   3813  C  CE2 . TYR   B 2 272  ? 142.891 143.956 71.235  1.00 74.49  ? 272  TYR   A CE2 1 
ATOM   3814  C  CZ  . TYR   B 2 272  ? 143.751 143.930 70.159  1.00 75.00  ? 272  TYR   A CZ  1 
ATOM   3815  O  OH  . TYR   B 2 272  ? 144.464 145.058 69.824  1.00 76.23  ? 272  TYR   A OH  1 
ATOM   3816  N  N   . GLU   B 2 273  ? 140.271 137.910 71.025  1.00 73.11  ? 273  GLU   A N   1 
ATOM   3817  C  CA  . GLU   B 2 273  ? 139.798 136.533 71.039  1.00 70.90  ? 273  GLU   A CA  1 
ATOM   3818  C  C   . GLU   B 2 273  ? 139.998 135.911 72.414  1.00 74.14  ? 273  GLU   A C   1 
ATOM   3819  O  O   . GLU   B 2 273  ? 141.017 136.147 73.070  1.00 79.61  ? 273  GLU   A O   1 
ATOM   3820  C  CB  . GLU   B 2 273  ? 140.529 135.700 69.981  1.00 73.89  ? 273  GLU   A CB  1 
ATOM   3821  C  CG  . GLU   B 2 273  ? 140.152 134.229 69.966  1.00 75.17  ? 273  GLU   A CG  1 
ATOM   3822  C  CD  . GLU   B 2 273  ? 140.896 133.449 68.900  1.00 80.99  ? 273  GLU   A CD  1 
ATOM   3823  O  OE1 . GLU   B 2 273  ? 141.680 134.066 68.150  1.00 83.18  ? 273  GLU   A OE1 1 
ATOM   3824  O  OE2 . GLU   B 2 273  ? 140.696 132.219 68.812  1.00 78.99  ? 273  GLU   A OE2 1 
ATOM   3825  N  N   . ASN   B 2 274  ? 139.010 135.122 72.841  1.00 69.27  ? 274  ASN   A N   1 
ATOM   3826  C  CA  . ASN   B 2 274  ? 139.099 134.304 74.051  1.00 69.69  ? 274  ASN   A CA  1 
ATOM   3827  C  C   . ASN   B 2 274  ? 139.270 135.159 75.306  1.00 76.06  ? 274  ASN   A C   1 
ATOM   3828  O  O   . ASN   B 2 274  ? 140.165 134.933 76.124  1.00 79.39  ? 274  ASN   A O   1 
ATOM   3829  C  CB  . ASN   B 2 274  ? 140.225 133.273 73.934  1.00 72.26  ? 274  ASN   A CB  1 
ATOM   3830  C  CG  . ASN   B 2 274  ? 139.923 132.195 72.916  1.00 73.40  ? 274  ASN   A CG  1 
ATOM   3831  O  OD1 . ASN   B 2 274  ? 138.779 131.767 72.768  1.00 76.68  ? 274  ASN   A OD1 1 
ATOM   3832  N  ND2 . ASN   B 2 274  ? 140.951 131.748 72.205  1.00 73.35  ? 274  ASN   A ND2 1 
ATOM   3833  N  N   . GLU   B 2 275  ? 138.395 136.150 75.460  1.00 71.27  ? 275  GLU   A N   1 
ATOM   3834  C  CA  . GLU   B 2 275  ? 138.335 136.917 76.695  1.00 69.35  ? 275  GLU   A CA  1 
ATOM   3835  C  C   . GLU   B 2 275  ? 136.953 137.534 76.837  1.00 69.70  ? 275  GLU   A C   1 
ATOM   3836  O  O   . GLU   B 2 275  ? 136.276 137.816 75.846  1.00 69.86  ? 275  GLU   A O   1 
ATOM   3837  C  CB  . GLU   B 2 275  ? 139.420 138.000 76.758  1.00 72.54  ? 275  GLU   A CB  1 
ATOM   3838  C  CG  . GLU   B 2 275  ? 139.530 138.869 75.526  1.00 73.26  ? 275  GLU   A CG  1 
ATOM   3839  C  CD  . GLU   B 2 275  ? 140.578 139.955 75.680  1.00 77.20  ? 275  GLU   A CD  1 
ATOM   3840  O  OE1 . GLU   B 2 275  ? 140.813 140.395 76.825  1.00 74.62  ? 275  GLU   A OE1 1 
ATOM   3841  O  OE2 . GLU   B 2 275  ? 141.173 140.364 74.662  1.00 75.09  ? 275  GLU   A OE2 1 
ATOM   3842  N  N   . GLN   B 2 276  ? 136.551 137.751 78.086  1.00 68.27  ? 276  GLN   A N   1 
ATOM   3843  C  CA  . GLN   B 2 276  ? 135.193 138.162 78.398  1.00 63.44  ? 276  GLN   A CA  1 
ATOM   3844  C  C   . GLN   B 2 276  ? 134.949 139.609 77.980  1.00 68.04  ? 276  GLN   A C   1 
ATOM   3845  O  O   . GLN   B 2 276  ? 135.864 140.348 77.605  1.00 72.87  ? 276  GLN   A O   1 
ATOM   3846  C  CB  . GLN   B 2 276  ? 134.910 137.983 79.887  1.00 65.67  ? 276  GLN   A CB  1 
ATOM   3847  C  CG  . GLN   B 2 276  ? 135.053 136.554 80.368  1.00 65.33  ? 276  GLN   A CG  1 
ATOM   3848  C  CD  . GLN   B 2 276  ? 134.535 136.361 81.776  1.00 71.38  ? 276  GLN   A CD  1 
ATOM   3849  O  OE1 . GLN   B 2 276  ? 133.906 137.252 82.344  1.00 71.68  ? 276  GLN   A OE1 1 
ATOM   3850  N  NE2 . GLN   B 2 276  ? 134.797 135.193 82.348  1.00 69.19  ? 276  GLN   A NE2 1 
ATOM   3851  N  N   . PHE   B 2 277  ? 133.682 140.009 78.045  1.00 69.08  ? 277  PHE   A N   1 
ATOM   3852  C  CA  . PHE   B 2 277  ? 133.198 141.334 77.691  1.00 71.18  ? 277  PHE   A CA  1 
ATOM   3853  C  C   . PHE   B 2 277  ? 133.080 142.221 78.922  1.00 75.02  ? 277  PHE   A C   1 
ATOM   3854  O  O   . PHE   B 2 277  ? 132.759 141.734 80.012  1.00 76.09  ? 277  PHE   A O   1 
ATOM   3855  C  CB  . PHE   B 2 277  ? 131.835 141.245 77.009  1.00 65.88  ? 277  PHE   A CB  1 
ATOM   3856  C  CG  . PHE   B 2 277  ? 131.910 140.916 75.556  1.00 67.32  ? 277  PHE   A CG  1 
ATOM   3857  C  CD1 . PHE   B 2 277  ? 133.072 141.136 74.846  1.00 68.51  ? 277  PHE   A CD1 1 
ATOM   3858  C  CD2 . PHE   B 2 277  ? 130.818 140.397 74.893  1.00 72.54  ? 277  PHE   A CD2 1 
ATOM   3859  C  CE1 . PHE   B 2 277  ? 133.144 140.836 73.505  1.00 68.19  ? 277  PHE   A CE1 1 
ATOM   3860  C  CE2 . PHE   B 2 277  ? 130.891 140.098 73.554  1.00 70.68  ? 277  PHE   A CE2 1 
ATOM   3861  C  CZ  . PHE   B 2 277  ? 132.055 140.319 72.862  1.00 67.20  ? 277  PHE   A CZ  1 
ATOM   3862  N  N   . PRO   B 2 278  ? 133.335 143.520 78.768  1.00 56.48  ? 278  PRO   A N   1 
ATOM   3863  C  CA  . PRO   B 2 278  ? 133.189 144.439 79.902  1.00 57.57  ? 278  PRO   A CA  1 
ATOM   3864  C  C   . PRO   B 2 278  ? 131.738 144.810 80.160  1.00 59.20  ? 278  PRO   A C   1 
ATOM   3865  O  O   . PRO   B 2 278  ? 131.335 145.020 81.307  1.00 70.24  ? 278  PRO   A O   1 
ATOM   3866  C  CB  . PRO   B 2 278  ? 134.015 145.654 79.470  1.00 67.24  ? 278  PRO   A CB  1 
ATOM   3867  C  CG  . PRO   B 2 278  ? 133.931 145.638 77.982  1.00 67.17  ? 278  PRO   A CG  1 
ATOM   3868  C  CD  . PRO   B 2 278  ? 133.874 144.191 77.573  1.00 58.85  ? 278  PRO   A CD  1 
ATOM   3869  N  N   . ALA   B 2 279  ? 130.953 144.896 79.091  1.00 49.85  ? 279  ALA   A N   1 
ATOM   3870  C  CA  . ALA   B 2 279  ? 129.535 145.221 79.169  1.00 52.55  ? 279  ALA   A CA  1 
ATOM   3871  C  C   . ALA   B 2 279  ? 128.892 144.800 77.855  1.00 57.15  ? 279  ALA   A C   1 
ATOM   3872  O  O   . ALA   B 2 279  ? 129.532 144.184 76.999  1.00 70.75  ? 279  ALA   A O   1 
ATOM   3873  C  CB  . ALA   B 2 279  ? 129.316 146.708 79.454  1.00 61.58  ? 279  ALA   A CB  1 
ATOM   3874  N  N   . ASP   B 2 280  ? 127.614 145.130 77.700  1.00 55.81  ? 280  ASP   A N   1 
ATOM   3875  C  CA  . ASP   B 2 280  ? 126.929 144.833 76.451  1.00 59.98  ? 280  ASP   A CA  1 
ATOM   3876  C  C   . ASP   B 2 280  ? 127.436 145.745 75.341  1.00 65.26  ? 280  ASP   A C   1 
ATOM   3877  O  O   . ASP   B 2 280  ? 127.562 146.959 75.521  1.00 74.16  ? 280  ASP   A O   1 
ATOM   3878  C  CB  . ASP   B 2 280  ? 125.422 144.991 76.618  1.00 55.93  ? 280  ASP   A CB  1 
ATOM   3879  C  CG  . ASP   B 2 280  ? 124.871 144.139 77.739  1.00 70.00  ? 280  ASP   A CG  1 
ATOM   3880  O  OD1 . ASP   B 2 280  ? 125.678 143.526 78.468  1.00 73.72  ? 280  ASP   A OD1 1 
ATOM   3881  O  OD2 . ASP   B 2 280  ? 123.633 144.081 77.893  1.00 73.50  ? 280  ASP   A OD2 1 
ATOM   3882  N  N   . ILE   B 2 281  ? 127.740 145.152 74.187  1.00 60.23  ? 281  ILE   A N   1 
ATOM   3883  C  CA  . ILE   B 2 281  ? 128.259 145.897 73.051  1.00 60.12  ? 281  ILE   A CA  1 
ATOM   3884  C  C   . ILE   B 2 281  ? 127.373 145.632 71.843  1.00 62.91  ? 281  ILE   A C   1 
ATOM   3885  O  O   . ILE   B 2 281  ? 126.616 144.660 71.797  1.00 71.64  ? 281  ILE   A O   1 
ATOM   3886  C  CB  . ILE   B 2 281  ? 129.730 145.543 72.728  1.00 55.83  ? 281  ILE   A CB  1 
ATOM   3887  C  CG1 . ILE   B 2 281  ? 129.806 144.426 71.687  1.00 62.15  ? 281  ILE   A CG1 1 
ATOM   3888  C  CG2 . ILE   B 2 281  ? 130.467 145.121 73.979  1.00 62.07  ? 281  ILE   A CG2 1 
ATOM   3889  C  CD1 . ILE   B 2 281  ? 131.219 144.049 71.296  1.00 67.44  ? 281  ILE   A CD1 1 
ATOM   3890  N  N   . VAL   B 2 282  ? 127.467 146.524 70.862  1.00 57.00  ? 282  VAL   A N   1 
ATOM   3891  C  CA  . VAL   B 2 282  ? 126.803 146.365 69.576  1.00 54.80  ? 282  VAL   A CA  1 
ATOM   3892  C  C   . VAL   B 2 282  ? 127.881 146.122 68.531  1.00 63.05  ? 282  VAL   A C   1 
ATOM   3893  O  O   . VAL   B 2 282  ? 128.817 146.920 68.398  1.00 69.09  ? 282  VAL   A O   1 
ATOM   3894  C  CB  . VAL   B 2 282  ? 125.945 147.588 69.221  1.00 57.25  ? 282  VAL   A CB  1 
ATOM   3895  C  CG1 . VAL   B 2 282  ? 125.549 147.548 67.757  1.00 63.51  ? 282  VAL   A CG1 1 
ATOM   3896  C  CG2 . VAL   B 2 282  ? 124.710 147.628 70.098  1.00 61.43  ? 282  VAL   A CG2 1 
ATOM   3897  N  N   . ILE   B 2 283  ? 127.750 145.015 67.797  1.00 66.91  ? 283  ILE   A N   1 
ATOM   3898  C  CA  . ILE   B 2 283  ? 128.770 144.614 66.837  1.00 64.78  ? 283  ILE   A CA  1 
ATOM   3899  C  C   . ILE   B 2 283  ? 128.974 145.713 65.808  1.00 68.12  ? 283  ILE   A C   1 
ATOM   3900  O  O   . ILE   B 2 283  ? 128.012 146.307 65.309  1.00 75.98  ? 283  ILE   A O   1 
ATOM   3901  C  CB  . ILE   B 2 283  ? 128.375 143.286 66.175  1.00 74.75  ? 283  ILE   A CB  1 
ATOM   3902  C  CG1 . ILE   B 2 283  ? 128.881 142.109 67.006  1.00 69.24  ? 283  ILE   A CG1 1 
ATOM   3903  C  CG2 . ILE   B 2 283  ? 128.896 143.201 64.742  1.00 79.05  ? 283  ILE   A CG2 1 
ATOM   3904  C  CD1 . ILE   B 2 283  ? 130.357 141.876 66.869  1.00 68.28  ? 283  ILE   A CD1 1 
ATOM   3905  N  N   . CYS   B 2 284  ? 130.231 146.000 65.500  1.00 70.95  ? 284  CYS   A N   1 
ATOM   3906  C  CA  . CYS   B 2 284  ? 130.566 146.975 64.474  1.00 77.61  ? 284  CYS   A CA  1 
ATOM   3907  C  C   . CYS   B 2 284  ? 131.413 146.399 63.352  1.00 81.77  ? 284  CYS   A C   1 
ATOM   3908  O  O   . CYS   B 2 284  ? 131.172 146.715 62.184  1.00 87.26  ? 284  CYS   A O   1 
ATOM   3909  C  CB  . CYS   B 2 284  ? 131.289 148.172 65.106  1.00 79.56  ? 284  CYS   A CB  1 
ATOM   3910  S  SG  . CYS   B 2 284  ? 131.576 149.550 63.976  1.00 96.73  ? 284  CYS   A SG  1 
ATOM   3911  N  N   . ALA   B 2 285  ? 132.395 145.555 63.665  1.00 69.78  ? 285  ALA   A N   1 
ATOM   3912  C  CA  . ALA   B 2 285  ? 133.237 144.961 62.638  1.00 68.98  ? 285  ALA   A CA  1 
ATOM   3913  C  C   . ALA   B 2 285  ? 133.926 143.726 63.197  1.00 70.33  ? 285  ALA   A C   1 
ATOM   3914  O  O   . ALA   B 2 285  ? 134.173 143.627 64.401  1.00 75.19  ? 285  ALA   A O   1 
ATOM   3915  C  CB  . ALA   B 2 285  ? 134.280 145.957 62.117  1.00 75.24  ? 285  ALA   A CB  1 
ATOM   3916  N  N   . THR   B 2 286  ? 134.229 142.787 62.304  1.00 70.64  ? 286  THR   A N   1 
ATOM   3917  C  CA  . THR   B 2 286  ? 134.963 141.578 62.645  1.00 66.62  ? 286  THR   A CA  1 
ATOM   3918  C  C   . THR   B 2 286  ? 135.836 141.202 61.456  1.00 71.11  ? 286  THR   A C   1 
ATOM   3919  O  O   . THR   B 2 286  ? 135.594 141.631 60.325  1.00 77.64  ? 286  THR   A O   1 
ATOM   3920  C  CB  . THR   B 2 286  ? 134.021 140.425 63.020  1.00 71.55  ? 286  THR   A CB  1 
ATOM   3921  O  OG1 . THR   B 2 286  ? 132.972 140.921 63.859  1.00 74.24  ? 286  THR   A OG1 1 
ATOM   3922  C  CG2 . THR   B 2 286  ? 134.775 139.338 63.775  1.00 75.07  ? 286  THR   A CG2 1 
ATOM   3923  N  N   . SER   B 2 287  ? 136.859 140.394 61.718  1.00 71.62  ? 287  SER   A N   1 
ATOM   3924  C  CA  . SER   B 2 287  ? 137.920 140.159 60.749  1.00 78.26  ? 287  SER   A CA  1 
ATOM   3925  C  C   . SER   B 2 287  ? 137.697 138.944 59.856  1.00 81.06  ? 287  SER   A C   1 
ATOM   3926  O  O   . SER   B 2 287  ? 138.545 138.673 59.000  1.00 82.80  ? 287  SER   A O   1 
ATOM   3927  C  CB  . SER   B 2 287  ? 139.261 140.009 61.472  1.00 77.37  ? 287  SER   A CB  1 
ATOM   3928  O  OG  . SER   B 2 287  ? 140.307 139.736 60.556  1.00 78.63  ? 287  SER   A OG  1 
ATOM   3929  N  N   . GLU   B 2 288  ? 136.600 138.203 60.014  1.00 84.14  ? 288  GLU   A N   1 
ATOM   3930  C  CA  . GLU   B 2 288  ? 136.444 136.957 59.250  1.00 80.79  ? 288  GLU   A CA  1 
ATOM   3931  C  C   . GLU   B 2 288  ? 135.664 137.170 57.956  1.00 85.50  ? 288  GLU   A C   1 
ATOM   3932  O  O   . GLU   B 2 288  ? 136.220 137.050 56.861  1.00 89.73  ? 288  GLU   A O   1 
ATOM   3933  C  CB  . GLU   B 2 288  ? 135.774 135.894 60.122  1.00 82.69  ? 288  GLU   A CB  1 
ATOM   3934  C  CG  . GLU   B 2 288  ? 136.588 135.491 61.334  1.00 86.46  ? 288  GLU   A CG  1 
ATOM   3935  C  CD  . GLU   B 2 288  ? 137.854 134.737 60.974  1.00 87.85  ? 288  GLU   A CD  1 
ATOM   3936  O  OE1 . GLU   B 2 288  ? 137.916 134.162 59.867  1.00 87.36  ? 288  GLU   A OE1 1 
ATOM   3937  O  OE2 . GLU   B 2 288  ? 138.788 134.718 61.803  1.00 89.09  ? 288  GLU   A OE2 1 
ATOM   3938  N  N   . GLU   B 2 289  ? 134.381 137.514 58.075  1.00 89.68  ? 289  GLU   A N   1 
ATOM   3939  C  CA  . GLU   B 2 289  ? 133.525 137.792 56.927  1.00 89.84  ? 289  GLU   A CA  1 
ATOM   3940  C  C   . GLU   B 2 289  ? 132.155 138.236 57.413  1.00 91.10  ? 289  GLU   A C   1 
ATOM   3941  O  O   . GLU   B 2 289  ? 131.666 137.731 58.428  1.00 92.36  ? 289  GLU   A O   1 
ATOM   3942  C  CB  . GLU   B 2 289  ? 133.387 136.562 56.024  1.00 92.30  ? 289  GLU   A CB  1 
ATOM   3943  C  CG  . GLU   B 2 289  ? 132.744 136.846 54.674  1.00 94.93  ? 289  GLU   A CG  1 
ATOM   3944  C  CD  . GLU   B 2 289  ? 133.640 137.661 53.760  1.00 96.77  ? 289  GLU   A CD  1 
ATOM   3945  O  OE1 . GLU   B 2 289  ? 134.863 137.712 54.009  1.00 94.58  ? 289  GLU   A OE1 1 
ATOM   3946  O  OE2 . GLU   B 2 289  ? 133.120 138.251 52.790  1.00 96.85  ? 289  GLU   A OE2 1 
ATOM   3947  N  N   . GLU   B 2 290  ? 131.523 139.164 56.695  1.00 92.28  ? 290  GLU   A N   1 
ATOM   3948  C  CA  . GLU   B 2 290  ? 130.192 139.674 57.036  1.00 94.16  ? 290  GLU   A CA  1 
ATOM   3949  C  C   . GLU   B 2 290  ? 130.108 140.157 58.483  1.00 93.30  ? 290  GLU   A C   1 
ATOM   3950  O  O   . GLU   B 2 290  ? 129.012 140.290 59.035  1.00 90.06  ? 290  GLU   A O   1 
ATOM   3951  C  CB  . GLU   B 2 290  ? 129.111 138.623 56.762  1.00 91.32  ? 290  GLU   A CB  1 
ATOM   3952  C  CG  . GLU   B 2 290  ? 129.010 138.213 55.303  1.00 93.21  ? 290  GLU   A CG  1 
ATOM   3953  C  CD  . GLU   B 2 290  ? 127.895 137.218 55.053  1.00 96.18  ? 290  GLU   A CD  1 
ATOM   3954  O  OE1 . GLU   B 2 290  ? 127.157 136.899 56.008  1.00 93.49  ? 290  GLU   A OE1 1 
ATOM   3955  O  OE2 . GLU   B 2 290  ? 127.757 136.754 53.902  1.00 99.30  ? 290  GLU   A OE2 1 
ATOM   3956  N  N   . ASP   B 2 291  ? 131.262 140.421 59.101  1.00 85.36  ? 291  ASP   A N   1 
ATOM   3957  C  CA  . ASP   B 2 291  ? 131.351 140.894 60.482  1.00 80.93  ? 291  ASP   A CA  1 
ATOM   3958  C  C   . ASP   B 2 291  ? 130.662 139.948 61.462  1.00 83.91  ? 291  ASP   A C   1 
ATOM   3959  O  O   . ASP   B 2 291  ? 130.056 140.388 62.441  1.00 89.49  ? 291  ASP   A O   1 
ATOM   3960  C  CB  . ASP   B 2 291  ? 130.789 142.310 60.616  1.00 84.59  ? 291  ASP   A CB  1 
ATOM   3961  C  CG  . ASP   B 2 291  ? 131.455 143.290 59.672  1.00 88.63  ? 291  ASP   A CG  1 
ATOM   3962  O  OD1 . ASP   B 2 291  ? 132.658 143.117 59.387  1.00 88.53  ? 291  ASP   A OD1 1 
ATOM   3963  O  OD2 . ASP   B 2 291  ? 130.776 144.233 59.213  1.00 90.42  ? 291  ASP   A OD2 1 
ATOM   3964  N  N   . VAL   B 2 292  ? 130.756 138.643 61.218  1.00 74.57  ? 292  VAL   A N   1 
ATOM   3965  C  CA  . VAL   B 2 292  ? 130.147 137.654 62.101  1.00 68.59  ? 292  VAL   A CA  1 
ATOM   3966  C  C   . VAL   B 2 292  ? 131.095 137.347 63.251  1.00 67.91  ? 292  VAL   A C   1 
ATOM   3967  O  O   . VAL   B 2 292  ? 132.318 137.456 63.117  1.00 74.45  ? 292  VAL   A O   1 
ATOM   3968  C  CB  . VAL   B 2 292  ? 129.783 136.379 61.320  1.00 71.59  ? 292  VAL   A CB  1 
ATOM   3969  C  CG1 . VAL   B 2 292  ? 128.865 136.716 60.160  1.00 77.35  ? 292  VAL   A CG1 1 
ATOM   3970  C  CG2 . VAL   B 2 292  ? 131.035 135.673 60.830  1.00 78.26  ? 292  VAL   A CG2 1 
ATOM   3971  N  N   . ALA   B 2 293  ? 130.531 136.963 64.393  1.00 58.13  ? 293  ALA   A N   1 
ATOM   3972  C  CA  . ALA   B 2 293  ? 131.310 136.658 65.585  1.00 57.91  ? 293  ALA   A CA  1 
ATOM   3973  C  C   . ALA   B 2 293  ? 130.683 135.449 66.268  1.00 68.76  ? 293  ALA   A C   1 
ATOM   3974  O  O   . ALA   B 2 293  ? 129.686 134.894 65.797  1.00 78.58  ? 293  ALA   A O   1 
ATOM   3975  C  CB  . ALA   B 2 293  ? 131.387 137.877 66.512  1.00 67.97  ? 293  ALA   A CB  1 
ATOM   3976  N  N   . TYR   B 2 294  ? 131.266 135.035 67.392  1.00 62.71  ? 294  TYR   A N   1 
ATOM   3977  C  CA  . TYR   B 2 294  ? 130.816 133.835 68.080  1.00 56.18  ? 294  TYR   A CA  1 
ATOM   3978  C  C   . TYR   B 2 294  ? 130.882 134.045 69.588  1.00 60.12  ? 294  TYR   A C   1 
ATOM   3979  O  O   . TYR   B 2 294  ? 131.701 134.821 70.086  1.00 70.18  ? 294  TYR   A O   1 
ATOM   3980  C  CB  . TYR   B 2 294  ? 131.652 132.626 67.653  1.00 58.13  ? 294  TYR   A CB  1 
ATOM   3981  C  CG  . TYR   B 2 294  ? 131.578 132.346 66.168  1.00 58.47  ? 294  TYR   A CG  1 
ATOM   3982  C  CD1 . TYR   B 2 294  ? 130.459 131.744 65.612  1.00 61.41  ? 294  TYR   A CD1 1 
ATOM   3983  C  CD2 . TYR   B 2 294  ? 132.624 132.685 65.323  1.00 58.04  ? 294  TYR   A CD2 1 
ATOM   3984  C  CE1 . TYR   B 2 294  ? 130.383 131.490 64.257  1.00 63.94  ? 294  TYR   A CE1 1 
ATOM   3985  C  CE2 . TYR   B 2 294  ? 132.557 132.434 63.967  1.00 56.86  ? 294  TYR   A CE2 1 
ATOM   3986  C  CZ  . TYR   B 2 294  ? 131.435 131.836 63.440  1.00 62.23  ? 294  TYR   A CZ  1 
ATOM   3987  O  OH  . TYR   B 2 294  ? 131.364 131.584 62.090  1.00 70.33  ? 294  TYR   A OH  1 
ATOM   3988  N  N   . ILE   B 2 295  ? 130.009 133.336 70.307  1.00 53.67  ? 295  ILE   A N   1 
ATOM   3989  C  CA  . ILE   B 2 295  ? 129.831 133.462 71.748  1.00 53.25  ? 295  ILE   A CA  1 
ATOM   3990  C  C   . ILE   B 2 295  ? 129.945 132.070 72.369  1.00 59.11  ? 295  ILE   A C   1 
ATOM   3991  O  O   . ILE   B 2 295  ? 130.005 131.063 71.666  1.00 66.74  ? 295  ILE   A O   1 
ATOM   3992  C  CB  . ILE   B 2 295  ? 128.484 134.128 72.105  1.00 59.59  ? 295  ILE   A CB  1 
ATOM   3993  C  CG1 . ILE   B 2 295  ? 128.249 135.342 71.215  1.00 56.11  ? 295  ILE   A CG1 1 
ATOM   3994  C  CG2 . ILE   B 2 295  ? 128.444 134.593 73.555  1.00 62.73  ? 295  ILE   A CG2 1 
ATOM   3995  C  CD1 . ILE   B 2 295  ? 129.220 136.460 71.474  1.00 58.68  ? 295  ILE   A CD1 1 
ATOM   3996  N  N   . GLU   B 2 296  ? 129.997 132.020 73.699  1.00 58.42  ? 296  GLU   A N   1 
ATOM   3997  C  CA  . GLU   B 2 296  ? 130.105 130.764 74.430  1.00 57.98  ? 296  GLU   A CA  1 
ATOM   3998  C  C   . GLU   B 2 296  ? 129.021 130.712 75.505  1.00 65.81  ? 296  GLU   A C   1 
ATOM   3999  O  O   . GLU   B 2 296  ? 128.093 131.525 75.525  1.00 51.61  ? 296  GLU   A O   1 
ATOM   4000  C  CB  . GLU   B 2 296  ? 131.501 130.595 75.039  1.00 58.45  ? 296  GLU   A CB  1 
ATOM   4001  C  CG  . GLU   B 2 296  ? 132.274 129.405 74.495  1.00 68.77  ? 296  GLU   A CG  1 
ATOM   4002  C  CD  . GLU   B 2 296  ? 133.009 128.638 75.576  1.00 69.48  ? 296  GLU   A CD  1 
ATOM   4003  O  OE1 . GLU   B 2 296  ? 132.637 128.769 76.761  1.00 72.55  ? 296  GLU   A OE1 1 
ATOM   4004  O  OE2 . GLU   B 2 296  ? 133.960 127.903 75.240  1.00 63.76  ? 296  GLU   A OE2 1 
ATOM   4005  N  N   . THR   B 2 297  ? 129.156 129.739 76.407  1.00 82.04  ? 297  THR   A N   1 
ATOM   4006  C  CA  . THR   B 2 297  ? 128.159 129.439 77.430  1.00 75.05  ? 297  THR   A CA  1 
ATOM   4007  C  C   . THR   B 2 297  ? 128.251 130.445 78.579  1.00 68.51  ? 297  THR   A C   1 
ATOM   4008  O  O   . THR   B 2 297  ? 128.610 131.610 78.390  1.00 76.55  ? 297  THR   A O   1 
ATOM   4009  C  CB  . THR   B 2 297  ? 128.325 128.008 77.932  1.00 71.12  ? 297  THR   A CB  1 
ATOM   4010  O  OG1 . THR   B 2 297  ? 127.633 127.857 79.176  1.00 69.62  ? 297  THR   A OG1 1 
ATOM   4011  C  CG2 . THR   B 2 297  ? 129.796 127.690 78.145  1.00 66.88  ? 297  THR   A CG2 1 
ATOM   4012  N  N   . LYS   B 2 298  ? 127.860 130.006 79.778  1.00 56.91  ? 298  LYS   A N   1 
ATOM   4013  C  CA  . LYS   B 2 298  ? 127.747 130.756 81.030  1.00 63.89  ? 298  LYS   A CA  1 
ATOM   4014  C  C   . LYS   B 2 298  ? 126.497 131.632 81.035  1.00 66.56  ? 298  LYS   A C   1 
ATOM   4015  O  O   . LYS   B 2 298  ? 126.197 132.250 82.053  1.00 64.75  ? 298  LYS   A O   1 
ATOM   4016  C  CB  . LYS   B 2 298  ? 128.981 131.625 81.336  1.00 62.56  ? 298  LYS   A CB  1 
ATOM   4017  C  CG  . LYS   B 2 298  ? 129.154 131.977 82.792  1.00 64.31  ? 298  LYS   A CG  1 
ATOM   4018  C  CD  . LYS   B 2 298  ? 130.049 133.178 82.975  1.00 68.23  ? 298  LYS   A CD  1 
ATOM   4019  C  CE  . LYS   B 2 298  ? 129.808 133.833 84.322  1.00 71.04  ? 298  LYS   A CE  1 
ATOM   4020  N  NZ  . LYS   B 2 298  ? 130.159 132.940 85.462  1.00 71.02  ? 298  LYS   A NZ  1 
ATOM   4021  N  N   . ASN   B 2 299  ? 125.753 131.682 79.934  1.00 71.16  ? 299  ASN   A N   1 
ATOM   4022  C  CA  . ASN   B 2 299  ? 124.458 132.347 79.816  1.00 63.17  ? 299  ASN   A CA  1 
ATOM   4023  C  C   . ASN   B 2 299  ? 123.444 131.375 79.238  1.00 64.20  ? 299  ASN   A C   1 
ATOM   4024  O  O   . ASN   B 2 299  ? 122.769 131.659 78.246  1.00 67.78  ? 299  ASN   A O   1 
ATOM   4025  C  CB  . ASN   B 2 299  ? 124.528 133.601 78.947  1.00 63.27  ? 299  ASN   A CB  1 
ATOM   4026  C  CG  . ASN   B 2 299  ? 125.006 134.818 79.705  1.00 61.59  ? 299  ASN   A CG  1 
ATOM   4027  O  OD1 . ASN   B 2 299  ? 125.681 134.699 80.722  1.00 65.75  ? 299  ASN   A OD1 1 
ATOM   4028  N  ND2 . ASN   B 2 299  ? 124.654 136.002 79.210  1.00 62.41  ? 299  ASN   A ND2 1 
ATOM   4029  N  N   . LEU   B 2 300  ? 123.373 130.183 79.837  1.00 60.88  ? 300  LEU   A N   1 
ATOM   4030  C  CA  . LEU   B 2 300  ? 122.524 129.083 79.385  1.00 65.48  ? 300  LEU   A CA  1 
ATOM   4031  C  C   . LEU   B 2 300  ? 123.071 128.490 78.092  1.00 72.31  ? 300  LEU   A C   1 
ATOM   4032  O  O   . LEU   B 2 300  ? 124.025 129.023 77.515  1.00 74.27  ? 300  LEU   A O   1 
ATOM   4033  C  CB  . LEU   B 2 300  ? 121.069 129.528 79.191  1.00 69.52  ? 300  LEU   A CB  1 
ATOM   4034  C  CG  . LEU   B 2 300  ? 120.390 130.356 80.285  1.00 73.34  ? 300  LEU   A CG  1 
ATOM   4035  C  CD1 . LEU   B 2 300  ? 118.916 130.579 79.961  1.00 69.89  ? 300  LEU   A CD1 1 
ATOM   4036  C  CD2 . LEU   B 2 300  ? 120.554 129.693 81.636  1.00 69.73  ? 300  LEU   A CD2 1 
ATOM   4037  N  N   . ASP   B 2 301  ? 122.481 127.378 77.647  1.00 75.84  ? 301  ASP   A N   1 
ATOM   4038  C  CA  . ASP   B 2 301  ? 122.906 126.654 76.450  1.00 68.77  ? 301  ASP   A CA  1 
ATOM   4039  C  C   . ASP   B 2 301  ? 124.328 126.126 76.606  1.00 64.54  ? 301  ASP   A C   1 
ATOM   4040  O  O   . ASP   B 2 301  ? 124.982 126.378 77.621  1.00 67.88  ? 301  ASP   A O   1 
ATOM   4041  C  CB  . ASP   B 2 301  ? 122.788 127.539 75.205  1.00 64.50  ? 301  ASP   A CB  1 
ATOM   4042  C  CG  . ASP   B 2 301  ? 122.623 126.735 73.930  1.00 69.88  ? 301  ASP   A CG  1 
ATOM   4043  O  OD1 . ASP   B 2 301  ? 123.084 125.574 73.890  1.00 72.40  ? 301  ASP   A OD1 1 
ATOM   4044  O  OD2 . ASP   B 2 301  ? 122.030 127.265 72.966  1.00 71.93  ? 301  ASP   A OD2 1 
ATOM   4045  N  N   . GLY   B 2 302  ? 124.807 125.371 75.620  1.00 67.46  ? 302  GLY   A N   1 
ATOM   4046  C  CA  . GLY   B 2 302  ? 126.133 124.789 75.699  1.00 68.35  ? 302  GLY   A CA  1 
ATOM   4047  C  C   . GLY   B 2 302  ? 126.882 124.754 74.383  1.00 65.01  ? 302  GLY   A C   1 
ATOM   4048  O  O   . GLY   B 2 302  ? 127.879 124.039 74.248  1.00 63.12  ? 302  GLY   A O   1 
ATOM   4049  N  N   . GLU   B 2 303  ? 126.418 125.528 73.410  1.00 73.35  ? 303  GLU   A N   1 
ATOM   4050  C  CA  . GLU   B 2 303  ? 127.006 125.585 72.080  1.00 69.92  ? 303  GLU   A CA  1 
ATOM   4051  C  C   . GLU   B 2 303  ? 127.442 127.010 71.768  1.00 74.35  ? 303  GLU   A C   1 
ATOM   4052  O  O   . GLU   B 2 303  ? 127.040 127.969 72.432  1.00 73.78  ? 303  GLU   A O   1 
ATOM   4053  C  CB  . GLU   B 2 303  ? 126.015 125.091 71.022  1.00 66.51  ? 303  GLU   A CB  1 
ATOM   4054  C  CG  . GLU   B 2 303  ? 124.711 125.861 71.016  1.00 72.14  ? 303  GLU   A CG  1 
ATOM   4055  C  CD  . GLU   B 2 303  ? 123.686 125.270 70.076  1.00 75.15  ? 303  GLU   A CD  1 
ATOM   4056  O  OE1 . GLU   B 2 303  ? 124.023 124.311 69.351  1.00 76.44  ? 303  GLU   A OE1 1 
ATOM   4057  O  OE2 . GLU   B 2 303  ? 122.538 125.763 70.064  1.00 75.70  ? 303  GLU   A OE2 1 
ATOM   4058  N  N   . THR   B 2 304  ? 128.276 127.142 70.741  1.00 63.87  ? 304  THR   A N   1 
ATOM   4059  C  CA  . THR   B 2 304  ? 128.788 128.438 70.311  1.00 58.96  ? 304  THR   A CA  1 
ATOM   4060  C  C   . THR   B 2 304  ? 127.743 129.106 69.427  1.00 57.44  ? 304  THR   A C   1 
ATOM   4061  O  O   . THR   B 2 304  ? 127.403 128.592 68.358  1.00 65.03  ? 304  THR   A O   1 
ATOM   4062  C  CB  . THR   B 2 304  ? 130.117 128.282 69.575  1.00 58.42  ? 304  THR   A CB  1 
ATOM   4063  O  OG1 . THR   B 2 304  ? 131.168 128.062 70.522  1.00 57.06  ? 304  THR   A OG1 1 
ATOM   4064  C  CG2 . THR   B 2 304  ? 130.431 129.522 68.770  1.00 58.72  ? 304  THR   A CG2 1 
ATOM   4065  N  N   . ASN   B 2 305  ? 127.223 130.243 69.879  1.00 60.95  ? 305  ASN   A N   1 
ATOM   4066  C  CA  . ASN   B 2 305  ? 126.233 130.981 69.114  1.00 58.76  ? 305  ASN   A CA  1 
ATOM   4067  C  C   . ASN   B 2 305  ? 126.921 131.880 68.092  1.00 63.85  ? 305  ASN   A C   1 
ATOM   4068  O  O   . ASN   B 2 305  ? 128.148 131.905 67.969  1.00 71.47  ? 305  ASN   A O   1 
ATOM   4069  C  CB  . ASN   B 2 305  ? 125.338 131.791 70.047  1.00 56.88  ? 305  ASN   A CB  1 
ATOM   4070  C  CG  . ASN   B 2 305  ? 124.477 130.915 70.932  1.00 65.30  ? 305  ASN   A CG  1 
ATOM   4071  O  OD1 . ASN   B 2 305  ? 124.717 129.715 71.059  1.00 70.22  ? 305  ASN   A OD1 1 
ATOM   4072  N  ND2 . ASN   B 2 305  ? 123.468 131.512 71.551  1.00 63.18  ? 305  ASN   A ND2 1 
ATOM   4073  N  N   . LEU   B 2 306  ? 126.119 132.633 67.347  1.00 71.35  ? 306  LEU   A N   1 
ATOM   4074  C  CA  . LEU   B 2 306  ? 126.621 133.509 66.301  1.00 68.26  ? 306  LEU   A CA  1 
ATOM   4075  C  C   . LEU   B 2 306  ? 125.924 134.858 66.380  1.00 73.98  ? 306  LEU   A C   1 
ATOM   4076  O  O   . LEU   B 2 306  ? 124.735 134.942 66.699  1.00 84.24  ? 306  LEU   A O   1 
ATOM   4077  C  CB  . LEU   B 2 306  ? 126.412 132.890 64.913  1.00 69.84  ? 306  LEU   A CB  1 
ATOM   4078  C  CG  . LEU   B 2 306  ? 124.976 132.534 64.512  1.00 75.16  ? 306  LEU   A CG  1 
ATOM   4079  C  CD1 . LEU   B 2 306  ? 124.294 133.685 63.783  1.00 76.88  ? 306  LEU   A CD1 1 
ATOM   4080  C  CD2 . LEU   B 2 306  ? 124.945 131.270 63.668  1.00 77.15  ? 306  LEU   A CD2 1 
ATOM   4081  N  N   . LYS   B 2 307  ? 126.675 135.915 66.083  1.00 53.56  ? 307  LYS   A N   1 
ATOM   4082  C  CA  . LYS   B 2 307  ? 126.133 137.264 66.003  1.00 55.62  ? 307  LYS   A CA  1 
ATOM   4083  C  C   . LYS   B 2 307  ? 126.510 137.848 64.652  1.00 60.56  ? 307  LYS   A C   1 
ATOM   4084  O  O   . LYS   B 2 307  ? 127.692 137.879 64.296  1.00 67.10  ? 307  LYS   A O   1 
ATOM   4085  C  CB  . LYS   B 2 307  ? 126.645 138.136 67.149  1.00 64.30  ? 307  LYS   A CB  1 
ATOM   4086  C  CG  . LYS   B 2 307  ? 126.345 137.559 68.523  1.00 62.56  ? 307  LYS   A CG  1 
ATOM   4087  C  CD  . LYS   B 2 307  ? 124.858 137.325 68.717  1.00 56.64  ? 307  LYS   A CD  1 
ATOM   4088  C  CE  . LYS   B 2 307  ? 124.585 136.612 70.026  1.00 52.41  ? 307  LYS   A CE  1 
ATOM   4089  N  NZ  . LYS   B 2 307  ? 123.176 136.159 70.142  1.00 51.03  ? 307  LYS   A NZ  1 
ATOM   4090  N  N   . SER   B 2 308  ? 125.509 138.318 63.908  1.00 79.41  ? 308  SER   A N   1 
ATOM   4091  C  CA  . SER   B 2 308  ? 125.681 138.506 62.467  1.00 82.42  ? 308  SER   A CA  1 
ATOM   4092  C  C   . SER   B 2 308  ? 126.437 139.785 62.124  1.00 79.21  ? 308  SER   A C   1 
ATOM   4093  O  O   . SER   B 2 308  ? 127.542 139.736 61.577  1.00 82.50  ? 308  SER   A O   1 
ATOM   4094  C  CB  . SER   B 2 308  ? 124.308 138.495 61.782  1.00 80.41  ? 308  SER   A CB  1 
ATOM   4095  O  OG  . SER   B 2 308  ? 124.423 138.847 60.415  1.00 82.35  ? 308  SER   A OG  1 
ATOM   4096  N  N   . ARG   B 2 309  ? 125.855 140.937 62.442  1.00 85.78  ? 309  ARG   A N   1 
ATOM   4097  C  CA  . ARG   B 2 309  ? 126.376 142.227 62.003  1.00 90.00  ? 309  ARG   A CA  1 
ATOM   4098  C  C   . ARG   B 2 309  ? 125.450 143.300 62.559  1.00 91.78  ? 309  ARG   A C   1 
ATOM   4099  O  O   . ARG   B 2 309  ? 124.421 143.001 63.173  1.00 95.28  ? 309  ARG   A O   1 
ATOM   4100  C  CB  . ARG   B 2 309  ? 126.459 142.336 60.472  1.00 95.58  ? 309  ARG   A CB  1 
ATOM   4101  C  CG  . ARG   B 2 309  ? 127.452 143.374 59.958  1.00 96.77  ? 309  ARG   A CG  1 
ATOM   4102  C  CD  . ARG   B 2 309  ? 127.257 143.670 58.477  1.00 93.14  ? 309  ARG   A CD  1 
ATOM   4103  N  NE  . ARG   B 2 309  ? 127.442 142.490 57.641  1.00 93.01  ? 309  ARG   A NE  1 
ATOM   4104  C  CZ  . ARG   B 2 309  ? 127.342 142.487 56.318  1.00 93.16  ? 309  ARG   A CZ  1 
ATOM   4105  N  NH1 . ARG   B 2 309  ? 127.066 143.592 55.644  1.00 92.69  ? 309  ARG   A NH1 1 
ATOM   4106  N  NH2 . ARG   B 2 309  ? 127.523 141.349 55.656  1.00 90.38  ? 309  ARG   A NH2 1 
ATOM   4107  N  N   . ASN   B 2 310  ? 125.827 144.554 62.337  1.00 78.77  ? 310  ASN   A N   1 
ATOM   4108  C  CA  . ASN   B 2 310  ? 124.955 145.681 62.623  1.00 78.83  ? 310  ASN   A CA  1 
ATOM   4109  C  C   . ASN   B 2 310  ? 124.217 146.185 61.390  1.00 82.17  ? 310  ASN   A C   1 
ATOM   4110  O  O   . ASN   B 2 310  ? 123.465 147.159 61.491  1.00 87.23  ? 310  ASN   A O   1 
ATOM   4111  C  CB  . ASN   B 2 310  ? 125.758 146.823 63.241  1.00 79.26  ? 310  ASN   A CB  1 
ATOM   4112  C  CG  . ASN   B 2 310  ? 124.918 147.702 64.128  1.00 81.87  ? 310  ASN   A CG  1 
ATOM   4113  O  OD1 . ASN   B 2 310  ? 123.775 147.373 64.440  1.00 81.20  ? 310  ASN   A OD1 1 
ATOM   4114  N  ND2 . ASN   B 2 310  ? 125.480 148.827 64.552  1.00 83.79  ? 310  ASN   A ND2 1 
ATOM   4115  N  N   . GLY   B 2 311  ? 124.407 145.555 60.248  1.00 84.70  ? 311  GLY   A N   1 
ATOM   4116  C  CA  . GLY   B 2 311  ? 123.771 146.000 59.012  1.00 84.81  ? 311  GLY   A CA  1 
ATOM   4117  C  C   . GLY   B 2 311  ? 124.638 147.018 58.283  1.00 88.01  ? 311  GLY   A C   1 
ATOM   4118  O  O   . GLY   B 2 311  ? 125.788 146.734 57.967  1.00 91.12  ? 311  GLY   A O   1 
ATOM   4119  N  N   . VAL   B 2 312  ? 124.069 148.194 58.014  1.00 91.68  ? 312  VAL   A N   1 
ATOM   4120  C  CA  . VAL   B 2 312  ? 124.840 149.263 57.374  1.00 94.39  ? 312  VAL   A CA  1 
ATOM   4121  C  C   . VAL   B 2 312  ? 126.045 149.688 58.206  1.00 94.94  ? 312  VAL   A C   1 
ATOM   4122  O  O   . VAL   B 2 312  ? 127.133 149.861 57.631  1.00 96.17  ? 312  VAL   A O   1 
ATOM   4123  C  CB  . VAL   B 2 312  ? 123.916 150.443 57.022  1.00 97.21  ? 312  VAL   A CB  1 
ATOM   4124  C  CG1 . VAL   B 2 312  ? 124.700 151.545 56.322  1.00 95.87  ? 312  VAL   A CG1 1 
ATOM   4125  C  CG2 . VAL   B 2 312  ? 122.759 149.970 56.157  1.00 95.69  ? 312  VAL   A CG2 1 
ATOM   4126  N  N   . PRO   B 2 313  ? 125.941 149.881 59.528  1.00 95.06  ? 313  PRO   A N   1 
ATOM   4127  C  CA  . PRO   B 2 313  ? 127.142 150.246 60.299  1.00 94.73  ? 313  PRO   A CA  1 
ATOM   4128  C  C   . PRO   B 2 313  ? 128.237 149.199 60.247  1.00 96.93  ? 313  PRO   A C   1 
ATOM   4129  O  O   . PRO   B 2 313  ? 129.390 149.520 60.559  1.00 94.87  ? 313  PRO   A O   1 
ATOM   4130  C  CB  . PRO   B 2 313  ? 126.607 150.425 61.725  1.00 95.36  ? 313  PRO   A CB  1 
ATOM   4131  C  CG  . PRO   B 2 313  ? 125.178 150.752 61.547  1.00 96.77  ? 313  PRO   A CG  1 
ATOM   4132  C  CD  . PRO   B 2 313  ? 124.733 149.940 60.371  1.00 95.03  ? 313  PRO   A CD  1 
ATOM   4133  N  N   . GLY   B 2 314  ? 127.914 147.960 59.880  1.00 96.93  ? 314  GLY   A N   1 
ATOM   4134  C  CA  . GLY   B 2 314  ? 128.953 146.974 59.655  1.00 93.38  ? 314  GLY   A CA  1 
ATOM   4135  C  C   . GLY   B 2 314  ? 129.924 147.432 58.585  1.00 90.36  ? 314  GLY   A C   1 
ATOM   4136  O  O   . GLY   B 2 314  ? 129.567 148.170 57.665  1.00 91.59  ? 314  GLY   A O   1 
ATOM   4137  N  N   . LEU   B 2 315  ? 131.177 146.996 58.728  1.00 91.44  ? 315  LEU   A N   1 
ATOM   4138  C  CA  . LEU   B 2 315  ? 132.284 147.508 57.928  1.00 94.52  ? 315  LEU   A CA  1 
ATOM   4139  C  C   . LEU   B 2 315  ? 132.415 149.011 58.138  1.00 94.86  ? 315  LEU   A C   1 
ATOM   4140  O  O   . LEU   B 2 315  ? 131.826 149.564 59.073  1.00 90.46  ? 315  LEU   A O   1 
ATOM   4141  C  CB  . LEU   B 2 315  ? 132.103 147.174 56.444  1.00 95.47  ? 315  LEU   A CB  1 
ATOM   4142  C  CG  . LEU   B 2 315  ? 132.066 145.688 56.082  1.00 95.42  ? 315  LEU   A CG  1 
ATOM   4143  C  CD1 . LEU   B 2 315  ? 131.870 145.507 54.585  1.00 95.42  ? 315  LEU   A CD1 1 
ATOM   4144  C  CD2 . LEU   B 2 315  ? 133.335 144.992 56.549  1.00 93.52  ? 315  LEU   A CD2 1 
ATOM   4145  N  N   . SER   B 2 316  ? 133.208 149.675 57.298  1.00 97.34  ? 316  SER   A N   1 
ATOM   4146  C  CA  . SER   B 2 316  ? 133.466 151.110 57.372  1.00 94.00  ? 316  SER   A CA  1 
ATOM   4147  C  C   . SER   B 2 316  ? 134.173 151.516 58.659  1.00 95.87  ? 316  SER   A C   1 
ATOM   4148  O  O   . SER   B 2 316  ? 134.361 152.713 58.906  1.00 99.62  ? 316  SER   A O   1 
ATOM   4149  C  CB  . SER   B 2 316  ? 132.174 151.924 57.210  1.00 90.07  ? 316  SER   A CB  1 
ATOM   4150  O  OG  . SER   B 2 316  ? 132.397 153.296 57.479  1.00 91.57  ? 316  SER   A OG  1 
ATOM   4151  N  N   . HIS   B 2 317  ? 134.565 150.549 59.494  1.00 95.44  ? 317  HIS   A N   1 
ATOM   4152  C  CA  . HIS   B 2 317  ? 135.221 150.828 60.765  1.00 92.58  ? 317  HIS   A CA  1 
ATOM   4153  C  C   . HIS   B 2 317  ? 136.344 149.835 61.040  1.00 88.33  ? 317  HIS   A C   1 
ATOM   4154  O  O   . HIS   B 2 317  ? 136.597 149.486 62.196  1.00 88.57  ? 317  HIS   A O   1 
ATOM   4155  C  CB  . HIS   B 2 317  ? 134.214 150.808 61.915  1.00 94.77  ? 317  HIS   A CB  1 
ATOM   4156  C  CG  . HIS   B 2 317  ? 132.989 151.628 61.656  1.00 98.22  ? 317  HIS   A CG  1 
ATOM   4157  N  ND1 . HIS   B 2 317  ? 131.974 151.207 60.824  1.00 98.52  ? 317  HIS   A ND1 1 
ATOM   4158  C  CD2 . HIS   B 2 317  ? 132.619 152.848 62.113  1.00 99.37  ? 317  HIS   A CD2 1 
ATOM   4159  C  CE1 . HIS   B 2 317  ? 131.030 152.131 60.781  1.00 97.19  ? 317  HIS   A CE1 1 
ATOM   4160  N  NE2 . HIS   B 2 317  ? 131.397 153.136 61.555  1.00 100.50 ? 317  HIS   A NE2 1 
ATOM   4161  N  N   . LEU   B 2 318  ? 137.025 149.372 59.990  1.00 90.31  ? 318  LEU   A N   1 
ATOM   4162  C  CA  . LEU   B 2 318  ? 138.045 148.343 60.159  1.00 93.77  ? 318  LEU   A CA  1 
ATOM   4163  C  C   . LEU   B 2 318  ? 139.186 148.833 61.043  1.00 94.63  ? 318  LEU   A C   1 
ATOM   4164  O  O   . LEU   B 2 318  ? 139.692 148.091 61.893  1.00 95.20  ? 318  LEU   A O   1 
ATOM   4165  C  CB  . LEU   B 2 318  ? 138.575 147.896 58.794  1.00 97.10  ? 318  LEU   A CB  1 
ATOM   4166  C  CG  . LEU   B 2 318  ? 137.630 147.133 57.858  1.00 98.25  ? 318  LEU   A CG  1 
ATOM   4167  C  CD1 . LEU   B 2 318  ? 136.805 146.112 58.631  1.00 96.82  ? 318  LEU   A CD1 1 
ATOM   4168  C  CD2 . LEU   B 2 318  ? 136.734 148.073 57.057  1.00 96.51  ? 318  LEU   A CD2 1 
ATOM   4169  N  N   . ASN   B 2 319  ? 139.605 150.079 60.858  1.00 99.19  ? 319  ASN   A N   1 
ATOM   4170  C  CA  . ASN   B 2 319  ? 140.714 150.646 61.608  1.00 98.91  ? 319  ASN   A CA  1 
ATOM   4171  C  C   . ASN   B 2 319  ? 140.198 151.609 62.673  1.00 97.62  ? 319  ASN   A C   1 
ATOM   4172  O  O   . ASN   B 2 319  ? 139.011 151.931 62.740  1.00 100.38 ? 319  ASN   A O   1 
ATOM   4173  C  CB  . ASN   B 2 319  ? 141.691 151.354 60.664  1.00 100.25 ? 319  ASN   A CB  1 
ATOM   4174  C  CG  . ASN   B 2 319  ? 143.110 151.374 61.199  1.00 103.48 ? 319  ASN   A CG  1 
ATOM   4175  O  OD1 . ASN   B 2 319  ? 143.332 151.307 62.408  1.00 104.15 ? 319  ASN   A OD1 1 
ATOM   4176  N  ND2 . ASN   B 2 319  ? 144.080 151.467 60.297  1.00 101.59 ? 319  ASN   A ND2 1 
ATOM   4177  N  N   . THR   B 2 320  ? 141.121 152.065 63.522  1.00 97.26  ? 320  THR   A N   1 
ATOM   4178  C  CA  . THR   B 2 320  ? 140.764 152.988 64.593  1.00 98.77  ? 320  THR   A CA  1 
ATOM   4179  C  C   . THR   B 2 320  ? 140.391 154.371 64.076  1.00 98.85  ? 320  THR   A C   1 
ATOM   4180  O  O   . THR   B 2 320  ? 139.550 155.037 64.688  1.00 99.40  ? 320  THR   A O   1 
ATOM   4181  C  CB  . THR   B 2 320  ? 141.916 153.109 65.595  1.00 100.83 ? 320  THR   A CB  1 
ATOM   4182  O  OG1 . THR   B 2 320  ? 141.625 154.148 66.538  1.00 101.24 ? 320  THR   A OG1 1 
ATOM   4183  C  CG2 . THR   B 2 320  ? 143.225 153.425 64.883  1.00 99.43  ? 320  THR   A CG2 1 
ATOM   4184  N  N   . ALA   B 2 321  ? 140.994 154.816 62.971  1.00 100.00 ? 321  ALA   A N   1 
ATOM   4185  C  CA  . ALA   B 2 321  ? 140.740 156.167 62.480  1.00 99.47  ? 321  ALA   A CA  1 
ATOM   4186  C  C   . ALA   B 2 321  ? 139.281 156.345 62.084  1.00 100.58 ? 321  ALA   A C   1 
ATOM   4187  O  O   . ALA   B 2 321  ? 138.696 157.413 62.303  1.00 100.29 ? 321  ALA   A O   1 
ATOM   4188  C  CB  . ALA   B 2 321  ? 141.661 156.481 61.302  1.00 98.81  ? 321  ALA   A CB  1 
ATOM   4189  N  N   . GLU   B 2 322  ? 138.679 155.314 61.488  1.00 106.24 ? 322  GLU   A N   1 
ATOM   4190  C  CA  . GLU   B 2 322  ? 137.268 155.391 61.131  1.00 106.04 ? 322  GLU   A CA  1 
ATOM   4191  C  C   . GLU   B 2 322  ? 136.385 155.513 62.364  1.00 104.27 ? 322  GLU   A C   1 
ATOM   4192  O  O   . GLU   B 2 322  ? 135.375 156.223 62.332  1.00 106.13 ? 322  GLU   A O   1 
ATOM   4193  C  CB  . GLU   B 2 322  ? 136.863 154.170 60.304  1.00 106.75 ? 322  GLU   A CB  1 
ATOM   4194  C  CG  . GLU   B 2 322  ? 137.362 154.185 58.863  1.00 105.61 ? 322  GLU   A CG  1 
ATOM   4195  C  CD  . GLU   B 2 322  ? 138.846 153.895 58.743  1.00 107.70 ? 322  GLU   A CD  1 
ATOM   4196  O  OE1 . GLU   B 2 322  ? 139.460 153.489 59.752  1.00 109.24 ? 322  GLU   A OE1 1 
ATOM   4197  O  OE2 . GLU   B 2 322  ? 139.400 154.071 57.638  1.00 106.97 ? 322  GLU   A OE2 1 
ATOM   4198  N  N   . ALA   B 2 323  ? 136.740 154.826 63.452  1.00 98.27  ? 323  ALA   A N   1 
ATOM   4199  C  CA  . ALA   B 2 323  ? 135.970 154.947 64.685  1.00 100.25 ? 323  ALA   A CA  1 
ATOM   4200  C  C   . ALA   B 2 323  ? 136.046 156.361 65.248  1.00 104.50 ? 323  ALA   A C   1 
ATOM   4201  O  O   . ALA   B 2 323  ? 135.043 156.899 65.731  1.00 105.08 ? 323  ALA   A O   1 
ATOM   4202  C  CB  . ALA   B 2 323  ? 136.463 153.931 65.713  1.00 98.22  ? 323  ALA   A CB  1 
ATOM   4203  N  N   . CYS   B 2 324  ? 137.230 156.976 65.201  1.00 103.74 ? 324  CYS   A N   1 
ATOM   4204  C  CA  . CYS   B 2 324  ? 137.377 158.335 65.714  1.00 97.97  ? 324  CYS   A CA  1 
ATOM   4205  C  C   . CYS   B 2 324  ? 136.634 159.341 64.845  1.00 96.22  ? 324  CYS   A C   1 
ATOM   4206  O  O   . CYS   B 2 324  ? 135.885 160.180 65.359  1.00 96.81  ? 324  CYS   A O   1 
ATOM   4207  C  CB  . CYS   B 2 324  ? 138.857 158.708 65.798  1.00 99.95  ? 324  CYS   A CB  1 
ATOM   4208  S  SG  . CYS   B 2 324  ? 139.892 157.537 66.701  1.00 108.12 ? 324  CYS   A SG  1 
ATOM   4209  N  N   . ALA   B 2 325  ? 136.822 159.270 63.528  1.00 99.66  ? 325  ALA   A N   1 
ATOM   4210  C  CA  . ALA   B 2 325  ? 136.273 160.267 62.618  1.00 99.96  ? 325  ALA   A CA  1 
ATOM   4211  C  C   . ALA   B 2 325  ? 134.767 160.153 62.434  1.00 98.39  ? 325  ALA   A C   1 
ATOM   4212  O  O   . ALA   B 2 325  ? 134.165 161.057 61.846  1.00 100.04 ? 325  ALA   A O   1 
ATOM   4213  C  CB  . ALA   B 2 325  ? 136.960 160.167 61.254  1.00 100.09 ? 325  ALA   A CB  1 
ATOM   4214  N  N   . LYS   B 2 326  ? 134.147 159.079 62.910  1.00 98.31  ? 326  LYS   A N   1 
ATOM   4215  C  CA  . LYS   B 2 326  ? 132.715 158.866 62.760  1.00 101.51 ? 326  LYS   A CA  1 
ATOM   4216  C  C   . LYS   B 2 326  ? 132.039 159.027 64.110  1.00 102.86 ? 326  LYS   A C   1 
ATOM   4217  O  O   . LYS   B 2 326  ? 132.523 158.502 65.118  1.00 104.52 ? 326  LYS   A O   1 
ATOM   4218  C  CB  . LYS   B 2 326  ? 132.419 157.480 62.178  1.00 106.55 ? 326  LYS   A CB  1 
ATOM   4219  C  CG  . LYS   B 2 326  ? 132.832 157.314 60.724  1.00 107.14 ? 326  LYS   A CG  1 
ATOM   4220  C  CD  . LYS   B 2 326  ? 131.997 158.192 59.809  1.00 106.88 ? 326  LYS   A CD  1 
ATOM   4221  C  CE  . LYS   B 2 326  ? 130.527 157.810 59.873  1.00 104.98 ? 326  LYS   A CE  1 
ATOM   4222  N  NZ  . LYS   B 2 326  ? 130.306 156.391 59.479  1.00 102.75 ? 326  LYS   A NZ  1 
ATOM   4223  N  N   . ALA   B 2 327  ? 130.925 159.754 64.126  1.00 108.75 ? 327  ALA   A N   1 
ATOM   4224  C  CA  . ALA   B 2 327  ? 130.119 159.960 65.324  1.00 112.27 ? 327  ALA   A CA  1 
ATOM   4225  C  C   . ALA   B 2 327  ? 128.737 159.332 65.169  1.00 109.82 ? 327  ALA   A C   1 
ATOM   4226  O  O   . ALA   B 2 327  ? 127.716 159.943 65.487  1.00 107.05 ? 327  ALA   A O   1 
ATOM   4227  C  CB  . ALA   B 2 327  ? 130.002 161.445 65.652  1.00 110.65 ? 327  ALA   A CB  1 
ATOM   4228  N  N   . HIS   B 2 328  ? 128.699 158.101 64.664  1.00 114.81 ? 328  HIS   A N   1 
ATOM   4229  C  CA  . HIS   B 2 328  ? 127.447 157.382 64.440  1.00 115.34 ? 328  HIS   A CA  1 
ATOM   4230  C  C   . HIS   B 2 328  ? 126.906 156.885 65.774  1.00 113.07 ? 328  HIS   A C   1 
ATOM   4231  O  O   . HIS   B 2 328  ? 127.317 155.839 66.277  1.00 114.02 ? 328  HIS   A O   1 
ATOM   4232  C  CB  . HIS   B 2 328  ? 127.666 156.230 63.464  1.00 115.95 ? 328  HIS   A CB  1 
ATOM   4233  C  CG  . HIS   B 2 328  ? 128.776 155.303 63.855  1.00 115.82 ? 328  HIS   A CG  1 
ATOM   4234  N  ND1 . HIS   B 2 328  ? 130.102 155.678 63.835  1.00 115.11 ? 328  HIS   A ND1 1 
ATOM   4235  C  CD2 . HIS   B 2 328  ? 128.755 154.015 64.272  1.00 114.60 ? 328  HIS   A CD2 1 
ATOM   4236  C  CE1 . HIS   B 2 328  ? 130.850 154.662 64.227  1.00 114.88 ? 328  HIS   A CE1 1 
ATOM   4237  N  NE2 . HIS   B 2 328  ? 130.058 153.641 64.497  1.00 115.16 ? 328  HIS   A NE2 1 
ATOM   4238  N  N   . LEU   B 2 329  ? 125.973 157.635 66.349  1.00 101.63 ? 329  LEU   A N   1 
ATOM   4239  C  CA  . LEU   B 2 329  ? 125.332 157.277 67.610  1.00 102.94 ? 329  LEU   A CA  1 
ATOM   4240  C  C   . LEU   B 2 329  ? 123.985 157.996 67.663  1.00 101.56 ? 329  LEU   A C   1 
ATOM   4241  O  O   . LEU   B 2 329  ? 123.432 158.354 66.617  1.00 101.03 ? 329  LEU   A O   1 
ATOM   4242  C  CB  . LEU   B 2 329  ? 126.245 157.573 68.812  1.00 106.16 ? 329  LEU   A CB  1 
ATOM   4243  C  CG  . LEU   B 2 329  ? 126.169 156.397 69.802  1.00 109.45 ? 329  LEU   A CG  1 
ATOM   4244  C  CD1 . LEU   B 2 329  ? 126.824 155.151 69.224  1.00 106.78 ? 329  LEU   A CD1 1 
ATOM   4245  C  CD2 . LEU   B 2 329  ? 126.765 156.708 71.155  1.00 107.86 ? 329  LEU   A CD2 1 
ATOM   4246  N  N   . CYS   B 2 330  ? 123.456 158.186 68.880  1.00 108.95 ? 330  CYS   A N   1 
ATOM   4247  C  CA  . CYS   B 2 330  ? 122.038 158.475 69.141  1.00 110.22 ? 330  CYS   A CA  1 
ATOM   4248  C  C   . CYS   B 2 330  ? 121.200 157.209 68.956  1.00 110.66 ? 330  CYS   A C   1 
ATOM   4249  O  O   . CYS   B 2 330  ? 120.153 157.211 68.308  1.00 110.73 ? 330  CYS   A O   1 
ATOM   4250  C  CB  . CYS   B 2 330  ? 121.502 159.630 68.285  1.00 109.72 ? 330  CYS   A CB  1 
ATOM   4251  S  SG  . CYS   B 2 330  ? 119.875 160.255 68.770  1.00 115.46 ? 330  CYS   A SG  1 
ATOM   4252  N  N   . ILE   B 2 331  ? 121.700 156.110 69.530  1.00 93.32  ? 331  ILE   A N   1 
ATOM   4253  C  CA  . ILE   B 2 331  ? 120.981 154.848 69.520  1.00 91.51  ? 331  ILE   A CA  1 
ATOM   4254  C  C   . ILE   B 2 331  ? 119.642 154.989 70.246  1.00 91.18  ? 331  ILE   A C   1 
ATOM   4255  O  O   . ILE   B 2 331  ? 119.458 155.843 71.121  1.00 91.25  ? 331  ILE   A O   1 
ATOM   4256  C  CB  . ILE   B 2 331  ? 121.839 153.746 70.160  1.00 93.12  ? 331  ILE   A CB  1 
ATOM   4257  C  CG1 . ILE   B 2 331  ? 123.318 154.001 69.872  1.00 91.04  ? 331  ILE   A CG1 1 
ATOM   4258  C  CG2 . ILE   B 2 331  ? 121.433 152.376 69.635  1.00 96.64  ? 331  ILE   A CG2 1 
ATOM   4259  C  CD1 . ILE   B 2 331  ? 124.241 152.955 70.450  1.00 92.42  ? 331  ILE   A CD1 1 
ATOM   4260  N  N   . ASP   B 2 332  ? 118.699 154.125 69.873  1.00 96.35  ? 332  ASP   A N   1 
ATOM   4261  C  CA  . ASP   B 2 332  ? 117.343 154.112 70.421  1.00 97.43  ? 332  ASP   A CA  1 
ATOM   4262  C  C   . ASP   B 2 332  ? 117.145 152.977 71.416  1.00 99.24  ? 332  ASP   A C   1 
ATOM   4263  O  O   . ASP   B 2 332  ? 116.086 152.342 71.436  1.00 100.70 ? 332  ASP   A O   1 
ATOM   4264  C  CB  . ASP   B 2 332  ? 116.316 154.012 69.297  1.00 97.83  ? 332  ASP   A CB  1 
ATOM   4265  C  CG  . ASP   B 2 332  ? 116.370 155.191 68.346  1.00 99.55  ? 332  ASP   A CG  1 
ATOM   4266  O  OD1 . ASP   B 2 332  ? 116.794 156.286 68.769  1.00 97.29  ? 332  ASP   A OD1 1 
ATOM   4267  O  OD2 . ASP   B 2 332  ? 115.983 155.020 67.170  1.00 99.32  ? 332  ASP   A OD2 1 
ATOM   4268  N  N   . LEU   B 2 333  ? 118.158 152.688 72.233  1.00 83.24  ? 333  LEU   A N   1 
ATOM   4269  C  CA  . LEU   B 2 333  ? 118.112 151.547 73.141  1.00 79.82  ? 333  LEU   A CA  1 
ATOM   4270  C  C   . LEU   B 2 333  ? 116.904 151.621 74.066  1.00 81.90  ? 333  LEU   A C   1 
ATOM   4271  O  O   . LEU   B 2 333  ? 116.612 152.670 74.645  1.00 87.32  ? 333  LEU   A O   1 
ATOM   4272  C  CB  . LEU   B 2 333  ? 119.392 151.491 73.970  1.00 79.90  ? 333  LEU   A CB  1 
ATOM   4273  C  CG  . LEU   B 2 333  ? 120.717 151.517 73.216  1.00 80.91  ? 333  LEU   A CG  1 
ATOM   4274  C  CD1 . LEU   B 2 333  ? 121.816 151.973 74.151  1.00 83.86  ? 333  LEU   A CD1 1 
ATOM   4275  C  CD2 . LEU   B 2 333  ? 121.032 150.150 72.637  1.00 79.90  ? 333  LEU   A CD2 1 
ATOM   4276  N  N   . ASP   B 2 334  ? 116.214 150.494 74.216  1.00 73.86  ? 334  ASP   A N   1 
ATOM   4277  C  CA  . ASP   B 2 334  ? 115.039 150.418 75.068  1.00 74.43  ? 334  ASP   A CA  1 
ATOM   4278  C  C   . ASP   B 2 334  ? 115.455 150.331 76.535  1.00 75.31  ? 334  ASP   A C   1 
ATOM   4279  O  O   . ASP   B 2 334  ? 116.629 150.463 76.888  1.00 77.82  ? 334  ASP   A O   1 
ATOM   4280  C  CB  . ASP   B 2 334  ? 114.172 149.226 74.671  1.00 76.19  ? 334  ASP   A CB  1 
ATOM   4281  C  CG  . ASP   B 2 334  ? 113.622 149.349 73.265  1.00 80.04  ? 334  ASP   A CG  1 
ATOM   4282  O  OD1 . ASP   B 2 334  ? 113.913 150.364 72.599  1.00 77.25  ? 334  ASP   A OD1 1 
ATOM   4283  O  OD2 . ASP   B 2 334  ? 112.897 148.432 72.825  1.00 82.19  ? 334  ASP   A OD2 1 
ATOM   4284  N  N   . ALA   B 2 335  ? 114.475 150.113 77.404  1.00 79.28  ? 335  ALA   A N   1 
ATOM   4285  C  CA  . ALA   B 2 335  ? 114.760 150.013 78.826  1.00 76.75  ? 335  ALA   A CA  1 
ATOM   4286  C  C   . ALA   B 2 335  ? 115.544 148.736 79.117  1.00 75.10  ? 335  ALA   A C   1 
ATOM   4287  O  O   . ALA   B 2 335  ? 115.326 147.710 78.464  1.00 80.34  ? 335  ALA   A O   1 
ATOM   4288  C  CB  . ALA   B 2 335  ? 113.465 150.023 79.636  1.00 78.85  ? 335  ALA   A CB  1 
ATOM   4289  N  N   . PRO   B 2 336  ? 116.466 148.768 80.077  1.00 65.80  ? 336  PRO   A N   1 
ATOM   4290  C  CA  . PRO   B 2 336  ? 117.175 147.540 80.462  1.00 71.27  ? 336  PRO   A CA  1 
ATOM   4291  C  C   . PRO   B 2 336  ? 116.216 146.517 81.050  1.00 76.06  ? 336  PRO   A C   1 
ATOM   4292  O  O   . PRO   B 2 336  ? 115.507 146.789 82.021  1.00 78.60  ? 336  PRO   A O   1 
ATOM   4293  C  CB  . PRO   B 2 336  ? 118.189 148.032 81.500  1.00 70.50  ? 336  PRO   A CB  1 
ATOM   4294  C  CG  . PRO   B 2 336  ? 118.373 149.474 81.190  1.00 72.16  ? 336  PRO   A CG  1 
ATOM   4295  C  CD  . PRO   B 2 336  ? 117.038 149.960 80.719  1.00 72.86  ? 336  PRO   A CD  1 
ATOM   4296  N  N   . GLU   B 2 337  ? 116.197 145.332 80.450  1.00 76.12  ? 337  GLU   A N   1 
ATOM   4297  C  CA  . GLU   B 2 337  ? 115.321 144.250 80.867  1.00 75.50  ? 337  GLU   A CA  1 
ATOM   4298  C  C   . GLU   B 2 337  ? 116.138 143.031 81.270  1.00 78.47  ? 337  GLU   A C   1 
ATOM   4299  O  O   . GLU   B 2 337  ? 117.271 142.836 80.824  1.00 81.74  ? 337  GLU   A O   1 
ATOM   4300  C  CB  . GLU   B 2 337  ? 114.343 143.874 79.750  1.00 76.96  ? 337  GLU   A CB  1 
ATOM   4301  C  CG  . GLU   B 2 337  ? 113.442 145.010 79.303  1.00 79.04  ? 337  GLU   A CG  1 
ATOM   4302  C  CD  . GLU   B 2 337  ? 112.528 144.611 78.163  1.00 83.89  ? 337  GLU   A CD  1 
ATOM   4303  O  OE1 . GLU   B 2 337  ? 112.644 143.464 77.682  1.00 84.11  ? 337  GLU   A OE1 1 
ATOM   4304  O  OE2 . GLU   B 2 337  ? 111.694 145.444 77.748  1.00 82.88  ? 337  GLU   A OE2 1 
ATOM   4305  N  N   . SER   B 2 338  ? 115.543 142.207 82.133  1.00 70.14  ? 338  SER   A N   1 
ATOM   4306  C  CA  . SER   B 2 338  ? 116.186 140.975 82.569  1.00 68.27  ? 338  SER   A CA  1 
ATOM   4307  C  C   . SER   B 2 338  ? 116.152 139.884 81.508  1.00 74.67  ? 338  SER   A C   1 
ATOM   4308  O  O   . SER   B 2 338  ? 116.997 138.984 81.540  1.00 79.41  ? 338  SER   A O   1 
ATOM   4309  C  CB  . SER   B 2 338  ? 115.522 140.462 83.847  1.00 73.21  ? 338  SER   A CB  1 
ATOM   4310  O  OG  . SER   B 2 338  ? 115.563 141.440 84.869  1.00 75.21  ? 338  SER   A OG  1 
ATOM   4311  N  N   . ASN   B 2 339  ? 115.199 139.941 80.581  1.00 83.28  ? 339  ASN   A N   1 
ATOM   4312  C  CA  . ASN   B 2 339  ? 115.090 138.919 79.550  1.00 80.46  ? 339  ASN   A CA  1 
ATOM   4313  C  C   . ASN   B 2 339  ? 116.315 138.942 78.646  1.00 83.36  ? 339  ASN   A C   1 
ATOM   4314  O  O   . ASN   B 2 339  ? 116.809 140.007 78.268  1.00 88.83  ? 339  ASN   A O   1 
ATOM   4315  C  CB  . ASN   B 2 339  ? 113.821 139.137 78.725  1.00 80.94  ? 339  ASN   A CB  1 
ATOM   4316  C  CG  . ASN   B 2 339  ? 113.442 137.926 77.895  1.00 87.12  ? 339  ASN   A CG  1 
ATOM   4317  O  OD1 . ASN   B 2 339  ? 114.290 137.111 77.533  1.00 89.34  ? 339  ASN   A OD1 1 
ATOM   4318  N  ND2 . ASN   B 2 339  ? 112.157 137.804 77.587  1.00 89.61  ? 339  ASN   A ND2 1 
ATOM   4319  N  N   . MET   B 2 340  ? 116.804 137.752 78.296  1.00 78.84  ? 340  MET   A N   1 
ATOM   4320  C  CA  . MET   B 2 340  ? 117.982 137.603 77.451  1.00 80.25  ? 340  MET   A CA  1 
ATOM   4321  C  C   . MET   B 2 340  ? 117.622 137.284 76.005  1.00 81.91  ? 340  MET   A C   1 
ATOM   4322  O  O   . MET   B 2 340  ? 118.335 136.526 75.340  1.00 84.16  ? 340  MET   A O   1 
ATOM   4323  C  CB  . MET   B 2 340  ? 118.911 136.531 78.019  1.00 78.95  ? 340  MET   A CB  1 
ATOM   4324  C  CG  . MET   B 2 340  ? 119.539 136.899 79.350  1.00 78.68  ? 340  MET   A CG  1 
ATOM   4325  S  SD  . MET   B 2 340  ? 120.816 135.737 79.862  1.00 89.55  ? 340  MET   A SD  1 
ATOM   4326  C  CE  . MET   B 2 340  ? 121.384 136.505 81.376  1.00 79.96  ? 340  MET   A CE  1 
ATOM   4327  N  N   . PHE   B 2 341  ? 116.520 137.847 75.502  1.00 85.23  ? 341  PHE   A N   1 
ATOM   4328  C  CA  . PHE   B 2 341  ? 116.122 137.607 74.122  1.00 84.85  ? 341  PHE   A CA  1 
ATOM   4329  C  C   . PHE   B 2 341  ? 115.596 138.852 73.417  1.00 86.40  ? 341  PHE   A C   1 
ATOM   4330  O  O   . PHE   B 2 341  ? 115.026 138.725 72.326  1.00 88.14  ? 341  PHE   A O   1 
ATOM   4331  C  CB  . PHE   B 2 341  ? 115.063 136.502 74.049  1.00 85.66  ? 341  PHE   A CB  1 
ATOM   4332  C  CG  . PHE   B 2 341  ? 115.578 135.142 74.414  1.00 84.27  ? 341  PHE   A CG  1 
ATOM   4333  C  CD1 . PHE   B 2 341  ? 116.425 134.457 73.561  1.00 85.98  ? 341  PHE   A CD1 1 
ATOM   4334  C  CD2 . PHE   B 2 341  ? 115.202 134.541 75.601  1.00 82.42  ? 341  PHE   A CD2 1 
ATOM   4335  C  CE1 . PHE   B 2 341  ? 116.898 133.204 73.892  1.00 87.96  ? 341  PHE   A CE1 1 
ATOM   4336  C  CE2 . PHE   B 2 341  ? 115.671 133.288 75.938  1.00 85.14  ? 341  PHE   A CE2 1 
ATOM   4337  C  CZ  . PHE   B 2 341  ? 116.520 132.618 75.082  1.00 87.49  ? 341  PHE   A CZ  1 
ATOM   4338  N  N   . ARG   B 2 342  ? 115.760 140.045 73.988  1.00 80.92  ? 342  ARG   A N   1 
ATOM   4339  C  CA  . ARG   B 2 342  ? 115.206 141.257 73.393  1.00 81.88  ? 342  ARG   A CA  1 
ATOM   4340  C  C   . ARG   B 2 342  ? 116.162 142.422 73.593  1.00 83.02  ? 342  ARG   A C   1 
ATOM   4341  O  O   . ARG   B 2 342  ? 116.491 142.769 74.730  1.00 83.11  ? 342  ARG   A O   1 
ATOM   4342  C  CB  . ARG   B 2 342  ? 113.837 141.592 73.993  1.00 82.49  ? 342  ARG   A CB  1 
ATOM   4343  C  CG  . ARG   B 2 342  ? 112.721 140.640 73.600  1.00 81.17  ? 342  ARG   A CG  1 
ATOM   4344  C  CD  . ARG   B 2 342  ? 111.400 141.062 74.219  1.00 83.12  ? 342  ARG   A CD  1 
ATOM   4345  N  NE  . ARG   B 2 342  ? 111.482 141.139 75.672  1.00 85.06  ? 342  ARG   A NE  1 
ATOM   4346  C  CZ  . ARG   B 2 342  ? 110.461 141.434 76.465  1.00 86.31  ? 342  ARG   A CZ  1 
ATOM   4347  N  NH1 . ARG   B 2 342  ? 109.258 141.685 75.978  1.00 84.99  ? 342  ARG   A NH1 1 
ATOM   4348  N  NH2 . ARG   B 2 342  ? 110.653 141.476 77.781  1.00 84.89  ? 342  ARG   A NH2 1 
ATOM   4349  N  N   . LEU   B 2 343  ? 116.597 143.024 72.486  1.00 74.42  ? 343  LEU   A N   1 
ATOM   4350  C  CA  . LEU   B 2 343  ? 117.261 144.320 72.490  1.00 73.14  ? 343  LEU   A CA  1 
ATOM   4351  C  C   . LEU   B 2 343  ? 116.837 145.080 71.241  1.00 69.38  ? 343  LEU   A C   1 
ATOM   4352  O  O   . LEU   B 2 343  ? 116.540 144.485 70.202  1.00 68.73  ? 343  LEU   A O   1 
ATOM   4353  C  CB  . LEU   B 2 343  ? 118.792 144.195 72.543  1.00 69.53  ? 343  LEU   A CB  1 
ATOM   4354  C  CG  . LEU   B 2 343  ? 119.431 143.827 73.883  1.00 67.34  ? 343  LEU   A CG  1 
ATOM   4355  C  CD1 . LEU   B 2 343  ? 119.595 142.320 74.015  1.00 71.47  ? 343  LEU   A CD1 1 
ATOM   4356  C  CD2 . LEU   B 2 343  ? 120.762 144.536 74.064  1.00 66.24  ? 343  LEU   A CD2 1 
ATOM   4357  N  N   . ASN   B 2 344  ? 116.807 146.407 71.349  1.00 76.25  ? 344  ASN   A N   1 
ATOM   4358  C  CA  . ASN   B 2 344  ? 116.369 147.243 70.241  1.00 78.36  ? 344  ASN   A CA  1 
ATOM   4359  C  C   . ASN   B 2 344  ? 117.173 148.535 70.226  1.00 80.36  ? 344  ASN   A C   1 
ATOM   4360  O  O   . ASN   B 2 344  ? 117.724 148.958 71.245  1.00 82.76  ? 344  ASN   A O   1 
ATOM   4361  C  CB  . ASN   B 2 344  ? 114.867 147.537 70.323  1.00 82.83  ? 344  ASN   A CB  1 
ATOM   4362  C  CG  . ASN   B 2 344  ? 114.019 146.295 70.112  1.00 84.96  ? 344  ASN   A CG  1 
ATOM   4363  O  OD1 . ASN   B 2 344  ? 113.596 146.003 68.994  1.00 84.95  ? 344  ASN   A OD1 1 
ATOM   4364  N  ND2 . ASN   B 2 344  ? 113.770 145.557 71.187  1.00 84.17  ? 344  ASN   A ND2 1 
ATOM   4365  N  N   . GLY   B 2 345  ? 117.237 149.153 69.056  1.00 80.69  ? 345  GLY   A N   1 
ATOM   4366  C  CA  . GLY   B 2 345  ? 117.980 150.386 68.891  1.00 81.71  ? 345  GLY   A CA  1 
ATOM   4367  C  C   . GLY   B 2 345  ? 118.089 150.761 67.428  1.00 82.85  ? 345  GLY   A C   1 
ATOM   4368  O  O   . GLY   B 2 345  ? 117.515 150.117 66.550  1.00 89.70  ? 345  GLY   A O   1 
ATOM   4369  N  N   . ALA   B 2 346  ? 118.846 151.832 67.186  1.00 90.68  ? 346  ALA   A N   1 
ATOM   4370  C  CA  . ALA   B 2 346  ? 119.080 152.317 65.826  1.00 95.09  ? 346  ALA   A CA  1 
ATOM   4371  C  C   . ALA   B 2 346  ? 120.281 153.249 65.835  1.00 95.90  ? 346  ALA   A C   1 
ATOM   4372  O  O   . ALA   B 2 346  ? 120.276 154.250 66.556  1.00 100.06 ? 346  ALA   A O   1 
ATOM   4373  C  CB  . ALA   B 2 346  ? 117.846 153.033 65.278  1.00 97.81  ? 346  ALA   A CB  1 
ATOM   4374  N  N   . VAL   B 2 347  ? 121.293 152.937 65.022  1.00 98.03  ? 347  VAL   A N   1 
ATOM   4375  C  CA  . VAL   B 2 347  ? 122.514 153.740 65.005  1.00 102.74 ? 347  VAL   A CA  1 
ATOM   4376  C  C   . VAL   B 2 347  ? 122.268 155.122 64.406  1.00 105.11 ? 347  VAL   A C   1 
ATOM   4377  O  O   . VAL   B 2 347  ? 122.847 156.113 64.869  1.00 104.78 ? 347  VAL   A O   1 
ATOM   4378  C  CB  . VAL   B 2 347  ? 123.626 152.987 64.252  1.00 104.83 ? 347  VAL   A CB  1 
ATOM   4379  C  CG1 . VAL   B 2 347  ? 124.922 153.787 64.264  1.00 103.89 ? 347  VAL   A CG1 1 
ATOM   4380  C  CG2 . VAL   B 2 347  ? 123.836 151.620 64.870  1.00 104.90 ? 347  VAL   A CG2 1 
ATOM   4381  N  N   . ILE   B 2 348  ? 121.443 155.208 63.359  1.00 107.29 ? 348  ILE   A N   1 
ATOM   4382  C  CA  . ILE   B 2 348  ? 121.043 156.463 62.719  1.00 106.11 ? 348  ILE   A CA  1 
ATOM   4383  C  C   . ILE   B 2 348  ? 122.204 157.110 61.971  1.00 106.30 ? 348  ILE   A C   1 
ATOM   4384  O  O   . ILE   B 2 348  ? 122.064 157.469 60.796  1.00 110.51 ? 348  ILE   A O   1 
ATOM   4385  C  CB  . ILE   B 2 348  ? 120.434 157.447 63.736  1.00 107.70 ? 348  ILE   A CB  1 
ATOM   4386  C  CG1 . ILE   B 2 348  ? 119.129 156.885 64.301  1.00 107.46 ? 348  ILE   A CG1 1 
ATOM   4387  C  CG2 . ILE   B 2 348  ? 120.199 158.805 63.093  1.00 108.43 ? 348  ILE   A CG2 1 
ATOM   4388  C  CD1 . ILE   B 2 348  ? 118.088 156.598 63.245  1.00 106.61 ? 348  ILE   A CD1 1 
ATOM   4389  N  N   . ASN   B 2 349  ? 123.341 157.287 62.653  1.00 107.86 ? 349  ASN   A N   1 
ATOM   4390  C  CA  . ASN   B 2 349  ? 124.562 157.865 62.091  1.00 111.29 ? 349  ASN   A CA  1 
ATOM   4391  C  C   . ASN   B 2 349  ? 124.414 159.364 61.850  1.00 111.81 ? 349  ASN   A C   1 
ATOM   4392  O  O   . ASN   B 2 349  ? 123.356 159.835 61.419  1.00 111.62 ? 349  ASN   A O   1 
ATOM   4393  C  CB  . ASN   B 2 349  ? 124.966 157.153 60.795  1.00 112.88 ? 349  ASN   A CB  1 
ATOM   4394  C  CG  . ASN   B 2 349  ? 126.359 157.533 60.325  1.00 111.42 ? 349  ASN   A CG  1 
ATOM   4395  O  OD1 . ASN   B 2 349  ? 126.619 158.684 59.977  1.00 111.71 ? 349  ASN   A OD1 1 
ATOM   4396  N  ND2 . ASN   B 2 349  ? 127.257 156.557 60.292  1.00 110.81 ? 349  ASN   A ND2 1 
ATOM   4397  N  N   . LEU   B 2 350  ? 125.478 160.123 62.125  1.00 116.90 ? 350  LEU   A N   1 
ATOM   4398  C  CA  . LEU   B 2 350  ? 125.425 161.572 61.966  1.00 116.17 ? 350  LEU   A CA  1 
ATOM   4399  C  C   . LEU   B 2 350  ? 125.541 162.002 60.508  1.00 116.15 ? 350  LEU   A C   1 
ATOM   4400  O  O   . LEU   B 2 350  ? 125.028 163.065 60.142  1.00 116.17 ? 350  LEU   A O   1 
ATOM   4401  C  CB  . LEU   B 2 350  ? 126.527 162.239 62.794  1.00 115.05 ? 350  LEU   A CB  1 
ATOM   4402  C  CG  . LEU   B 2 350  ? 127.914 162.367 62.158  1.00 116.93 ? 350  LEU   A CG  1 
ATOM   4403  C  CD1 . LEU   B 2 350  ? 128.767 163.374 62.916  1.00 116.69 ? 350  LEU   A CD1 1 
ATOM   4404  C  CD2 . LEU   B 2 350  ? 128.613 161.018 62.079  1.00 115.57 ? 350  LEU   A CD2 1 
ATOM   4405  N  N   . GLU   B 2 351  ? 126.213 161.212 59.670  1.00 117.41 ? 351  GLU   A N   1 
ATOM   4406  C  CA  . GLU   B 2 351  ? 126.438 161.554 58.264  1.00 116.96 ? 351  GLU   A CA  1 
ATOM   4407  C  C   . GLU   B 2 351  ? 126.022 160.366 57.402  1.00 117.01 ? 351  GLU   A C   1 
ATOM   4408  O  O   . GLU   B 2 351  ? 126.852 159.523 57.052  1.00 117.98 ? 351  GLU   A O   1 
ATOM   4409  C  CB  . GLU   B 2 351  ? 127.895 161.941 58.020  1.00 117.55 ? 351  GLU   A CB  1 
ATOM   4410  C  CG  . GLU   B 2 351  ? 128.305 163.261 58.651  1.00 118.71 ? 351  GLU   A CG  1 
ATOM   4411  C  CD  . GLU   B 2 351  ? 129.741 163.635 58.340  1.00 119.14 ? 351  GLU   A CD  1 
ATOM   4412  O  OE1 . GLU   B 2 351  ? 130.420 162.859 57.634  1.00 119.65 ? 351  GLU   A OE1 1 
ATOM   4413  O  OE2 . GLU   B 2 351  ? 130.191 164.704 58.801  1.00 119.39 ? 351  GLU   A OE2 1 
ATOM   4414  N  N   . GLU   B 2 352  ? 124.738 160.311 57.057  1.00 123.82 ? 352  GLU   A N   1 
ATOM   4415  C  CA  . GLU   B 2 352  ? 124.221 159.280 56.160  1.00 126.27 ? 352  GLU   A CA  1 
ATOM   4416  C  C   . GLU   B 2 352  ? 122.850 159.726 55.683  1.00 127.71 ? 352  GLU   A C   1 
ATOM   4417  O  O   . GLU   B 2 352  ? 121.986 160.045 56.506  1.00 127.10 ? 352  GLU   A O   1 
ATOM   4418  C  CB  . GLU   B 2 352  ? 124.140 157.923 56.863  1.00 126.76 ? 352  GLU   A CB  1 
ATOM   4419  C  CG  . GLU   B 2 352  ? 123.813 156.760 55.937  1.00 126.40 ? 352  GLU   A CG  1 
ATOM   4420  C  CD  . GLU   B 2 352  ? 124.925 156.464 54.948  1.00 127.51 ? 352  GLU   A CD  1 
ATOM   4421  O  OE1 . GLU   B 2 352  ? 126.087 156.826 55.227  1.00 126.56 ? 352  GLU   A OE1 1 
ATOM   4422  O  OE2 . GLU   B 2 352  ? 124.636 155.868 53.889  1.00 128.89 ? 352  GLU   A OE2 1 
ATOM   4423  N  N   . TYR   B 2 353  ? 122.649 159.756 54.368  1.00 130.54 ? 353  TYR   A N   1 
ATOM   4424  C  CA  . TYR   B 2 353  ? 121.410 160.245 53.784  1.00 130.01 ? 353  TYR   A CA  1 
ATOM   4425  C  C   . TYR   B 2 353  ? 120.920 159.279 52.717  1.00 131.20 ? 353  TYR   A C   1 
ATOM   4426  O  O   . TYR   B 2 353  ? 121.708 158.775 51.912  1.00 131.63 ? 353  TYR   A O   1 
ATOM   4427  C  CB  . TYR   B 2 353  ? 121.599 161.639 53.178  1.00 131.21 ? 353  TYR   A CB  1 
ATOM   4428  C  CG  . TYR   B 2 353  ? 122.177 162.649 54.142  1.00 131.83 ? 353  TYR   A CG  1 
ATOM   4429  C  CD1 . TYR   B 2 353  ? 121.351 163.410 54.958  1.00 132.07 ? 353  TYR   A CD1 1 
ATOM   4430  C  CD2 . TYR   B 2 353  ? 123.548 162.841 54.236  1.00 131.74 ? 353  TYR   A CD2 1 
ATOM   4431  C  CE1 . TYR   B 2 353  ? 121.875 164.335 55.842  1.00 132.19 ? 353  TYR   A CE1 1 
ATOM   4432  C  CE2 . TYR   B 2 353  ? 124.082 163.763 55.116  1.00 132.32 ? 353  TYR   A CE2 1 
ATOM   4433  C  CZ  . TYR   B 2 353  ? 123.241 164.507 55.916  1.00 132.91 ? 353  TYR   A CZ  1 
ATOM   4434  O  OH  . TYR   B 2 353  ? 123.769 165.426 56.794  1.00 132.56 ? 353  TYR   A OH  1 
ATOM   4435  N  N   . ASP   B 2 354  ? 119.614 159.028 52.717  1.00 146.58 ? 354  ASP   A N   1 
ATOM   4436  C  CA  . ASP   B 2 354  ? 118.982 158.184 51.717  1.00 147.30 ? 354  ASP   A CA  1 
ATOM   4437  C  C   . ASP   B 2 354  ? 118.502 159.051 50.552  1.00 148.27 ? 354  ASP   A C   1 
ATOM   4438  O  O   . ASP   B 2 354  ? 118.866 160.223 50.429  1.00 147.89 ? 354  ASP   A O   1 
ATOM   4439  C  CB  . ASP   B 2 354  ? 117.844 157.379 52.344  1.00 147.66 ? 354  ASP   A CB  1 
ATOM   4440  C  CG  . ASP   B 2 354  ? 116.785 158.258 52.985  1.00 148.94 ? 354  ASP   A CG  1 
ATOM   4441  O  OD1 . ASP   B 2 354  ? 116.958 159.495 53.008  1.00 148.51 ? 354  ASP   A OD1 1 
ATOM   4442  O  OD2 . ASP   B 2 354  ? 115.773 157.708 53.468  1.00 148.83 ? 354  ASP   A OD2 1 
ATOM   4443  N  N   . GLU   B 2 355  ? 117.674 158.474 49.677  1.00 156.85 ? 355  GLU   A N   1 
ATOM   4444  C  CA  . GLU   B 2 355  ? 117.116 159.237 48.567  1.00 157.29 ? 355  GLU   A CA  1 
ATOM   4445  C  C   . GLU   B 2 355  ? 116.191 160.350 49.041  1.00 156.81 ? 355  GLU   A C   1 
ATOM   4446  O  O   . GLU   B 2 355  ? 115.919 161.283 48.277  1.00 156.00 ? 355  GLU   A O   1 
ATOM   4447  C  CB  . GLU   B 2 355  ? 116.365 158.310 47.607  1.00 156.29 ? 355  GLU   A CB  1 
ATOM   4448  C  CG  . GLU   B 2 355  ? 115.070 157.728 48.164  1.00 156.85 ? 355  GLU   A CG  1 
ATOM   4449  C  CD  . GLU   B 2 355  ? 115.302 156.613 49.167  1.00 157.34 ? 355  GLU   A CD  1 
ATOM   4450  O  OE1 . GLU   B 2 355  ? 116.447 156.122 49.261  1.00 157.27 ? 355  GLU   A OE1 1 
ATOM   4451  O  OE2 . GLU   B 2 355  ? 114.339 156.228 49.862  1.00 156.80 ? 355  GLU   A OE2 1 
ATOM   4452  N  N   . ASP   B 2 356  ? 115.702 160.275 50.277  1.00 153.47 ? 356  ASP   A N   1 
ATOM   4453  C  CA  . ASP   B 2 356  ? 114.844 161.301 50.852  1.00 152.47 ? 356  ASP   A CA  1 
ATOM   4454  C  C   . ASP   B 2 356  ? 115.596 162.231 51.796  1.00 151.77 ? 356  ASP   A C   1 
ATOM   4455  O  O   . ASP   B 2 356  ? 114.961 162.951 52.573  1.00 151.83 ? 356  ASP   A O   1 
ATOM   4456  C  CB  . ASP   B 2 356  ? 113.666 160.655 51.584  1.00 152.38 ? 356  ASP   A CB  1 
ATOM   4457  C  CG  . ASP   B 2 356  ? 112.796 159.821 50.665  1.00 153.08 ? 356  ASP   A CG  1 
ATOM   4458  O  OD1 . ASP   B 2 356  ? 112.713 160.151 49.463  1.00 152.99 ? 356  ASP   A OD1 1 
ATOM   4459  O  OD2 . ASP   B 2 356  ? 112.195 158.837 51.144  1.00 152.69 ? 356  ASP   A OD2 1 
ATOM   4460  N  N   . GLU   B 2 357  ? 116.930 162.219 51.754  1.00 143.42 ? 357  GLU   A N   1 
ATOM   4461  C  CA  . GLU   B 2 357  ? 117.783 163.048 52.606  1.00 142.92 ? 357  GLU   A CA  1 
ATOM   4462  C  C   . GLU   B 2 357  ? 117.562 162.773 54.089  1.00 141.42 ? 357  GLU   A C   1 
ATOM   4463  O  O   . GLU   B 2 357  ? 117.794 163.649 54.928  1.00 141.14 ? 357  GLU   A O   1 
ATOM   4464  C  CB  . GLU   B 2 357  ? 117.591 164.542 52.311  1.00 143.11 ? 357  GLU   A CB  1 
ATOM   4465  C  CG  . GLU   B 2 357  ? 117.997 164.959 50.905  1.00 142.27 ? 357  GLU   A CG  1 
ATOM   4466  C  CD  . GLU   B 2 357  ? 119.496 164.883 50.677  1.00 142.73 ? 357  GLU   A CD  1 
ATOM   4467  O  OE1 . GLU   B 2 357  ? 120.255 164.891 51.669  1.00 142.69 ? 357  GLU   A OE1 1 
ATOM   4468  O  OE2 . GLU   B 2 357  ? 119.916 164.815 49.502  1.00 142.60 ? 357  GLU   A OE2 1 
ATOM   4469  N  N   . GLN   B 2 358  ? 117.114 161.570 54.427  1.00 137.11 ? 358  GLN   A N   1 
ATOM   4470  C  CA  . GLN   B 2 358  ? 116.892 161.172 55.807  1.00 138.70 ? 358  GLN   A CA  1 
ATOM   4471  C  C   . GLN   B 2 358  ? 117.936 160.148 56.234  1.00 138.76 ? 358  GLN   A C   1 
ATOM   4472  O  O   . GLN   B 2 358  ? 118.426 159.359 55.423  1.00 139.34 ? 358  GLN   A O   1 
ATOM   4473  C  CB  . GLN   B 2 358  ? 115.488 160.591 55.987  1.00 137.82 ? 358  GLN   A CB  1 
ATOM   4474  C  CG  . GLN   B 2 358  ? 114.368 161.536 55.587  1.00 137.63 ? 358  GLN   A CG  1 
ATOM   4475  C  CD  . GLN   B 2 358  ? 112.993 160.938 55.811  1.00 138.29 ? 358  GLN   A CD  1 
ATOM   4476  O  OE1 . GLN   B 2 358  ? 112.865 159.798 56.258  1.00 138.72 ? 358  GLN   A OE1 1 
ATOM   4477  N  NE2 . GLN   B 2 358  ? 111.955 161.706 55.502  1.00 137.94 ? 358  GLN   A NE2 1 
ATOM   4478  N  N   . HIS   B 2 359  ? 118.275 160.172 57.514  1.00 124.09 ? 359  HIS   A N   1 
ATOM   4479  C  CA  . HIS   B 2 359  ? 119.223 159.202 58.047  1.00 122.02 ? 359  HIS   A CA  1 
ATOM   4480  C  C   . HIS   B 2 359  ? 118.560 157.835 58.140  1.00 123.69 ? 359  HIS   A C   1 
ATOM   4481  O  O   . HIS   B 2 359  ? 117.524 157.705 58.805  1.00 122.44 ? 359  HIS   A O   1 
ATOM   4482  C  CB  . HIS   B 2 359  ? 119.729 159.644 59.414  1.00 121.43 ? 359  HIS   A CB  1 
ATOM   4483  C  CG  . HIS   B 2 359  ? 120.637 160.831 59.365  1.00 123.15 ? 359  HIS   A CG  1 
ATOM   4484  N  ND1 . HIS   B 2 359  ? 121.935 160.756 58.909  1.00 123.44 ? 359  HIS   A ND1 1 
ATOM   4485  C  CD2 . HIS   B 2 359  ? 120.436 162.123 59.717  1.00 123.93 ? 359  HIS   A CD2 1 
ATOM   4486  C  CE1 . HIS   B 2 359  ? 122.494 161.950 58.981  1.00 123.34 ? 359  HIS   A CE1 1 
ATOM   4487  N  NE2 . HIS   B 2 359  ? 121.606 162.797 59.469  1.00 124.50 ? 359  HIS   A NE2 1 
ATOM   4488  N  N   . PRO   B 2 360  ? 119.100 156.804 57.493  1.00 116.46 ? 360  PRO   A N   1 
ATOM   4489  C  CA  . PRO   B 2 360  ? 118.471 155.481 57.560  1.00 113.38 ? 360  PRO   A CA  1 
ATOM   4490  C  C   . PRO   B 2 360  ? 118.499 154.921 58.973  1.00 113.30 ? 360  PRO   A C   1 
ATOM   4491  O  O   . PRO   B 2 360  ? 119.415 155.186 59.754  1.00 112.73 ? 360  PRO   A O   1 
ATOM   4492  C  CB  . PRO   B 2 360  ? 119.321 154.632 56.606  1.00 111.30 ? 360  PRO   A CB  1 
ATOM   4493  C  CG  . PRO   B 2 360  ? 120.025 155.620 55.729  1.00 112.31 ? 360  PRO   A CG  1 
ATOM   4494  C  CD  . PRO   B 2 360  ? 120.262 156.819 56.590  1.00 115.72 ? 360  PRO   A CD  1 
ATOM   4495  N  N   . ILE   B 2 361  ? 117.474 154.143 59.295  1.00 108.87 ? 361  ILE   A N   1 
ATOM   4496  C  CA  . ILE   B 2 361  ? 117.384 153.468 60.583  1.00 107.13 ? 361  ILE   A CA  1 
ATOM   4497  C  C   . ILE   B 2 361  ? 118.023 152.092 60.456  1.00 104.80 ? 361  ILE   A C   1 
ATOM   4498  O  O   . ILE   B 2 361  ? 117.722 151.336 59.525  1.00 104.63 ? 361  ILE   A O   1 
ATOM   4499  C  CB  . ILE   B 2 361  ? 115.923 153.366 61.060  1.00 107.88 ? 361  ILE   A CB  1 
ATOM   4500  C  CG1 . ILE   B 2 361  ? 115.019 152.755 59.979  1.00 107.57 ? 361  ILE   A CG1 1 
ATOM   4501  C  CG2 . ILE   B 2 361  ? 115.410 154.731 61.502  1.00 108.04 ? 361  ILE   A CG2 1 
ATOM   4502  C  CD1 . ILE   B 2 361  ? 114.314 153.768 59.088  1.00 105.66 ? 361  ILE   A CD1 1 
ATOM   4503  N  N   . HIS   B 2 362  ? 118.923 151.776 61.380  1.00 90.00  ? 362  HIS   A N   1 
ATOM   4504  C  CA  . HIS   B 2 362  ? 119.619 150.497 61.370  1.00 88.02  ? 362  HIS   A CA  1 
ATOM   4505  C  C   . HIS   B 2 362  ? 119.244 149.708 62.615  1.00 88.67  ? 362  HIS   A C   1 
ATOM   4506  O  O   . HIS   B 2 362  ? 119.782 149.982 63.699  1.00 91.51  ? 362  HIS   A O   1 
ATOM   4507  C  CB  . HIS   B 2 362  ? 121.130 150.716 61.304  1.00 87.98  ? 362  HIS   A CB  1 
ATOM   4508  C  CG  . HIS   B 2 362  ? 121.558 151.577 60.158  1.00 88.76  ? 362  HIS   A CG  1 
ATOM   4509  N  ND1 . HIS   B 2 362  ? 122.646 152.420 60.224  1.00 92.02  ? 362  HIS   A ND1 1 
ATOM   4510  C  CD2 . HIS   B 2 362  ? 121.039 151.730 58.917  1.00 90.89  ? 362  HIS   A CD2 1 
ATOM   4511  C  CE1 . HIS   B 2 362  ? 122.781 153.052 59.072  1.00 93.64  ? 362  HIS   A CE1 1 
ATOM   4512  N  NE2 . HIS   B 2 362  ? 121.818 152.653 58.262  1.00 94.70  ? 362  HIS   A NE2 1 
ATOM   4513  N  N   . PRO   B 2 363  ? 118.338 148.738 62.517  1.00 73.04  ? 363  PRO   A N   1 
ATOM   4514  C  CA  . PRO   B 2 363  ? 117.855 148.054 63.722  1.00 75.40  ? 363  PRO   A CA  1 
ATOM   4515  C  C   . PRO   B 2 363  ? 118.962 147.289 64.432  1.00 76.36  ? 363  PRO   A C   1 
ATOM   4516  O  O   . PRO   B 2 363  ? 119.861 146.727 63.805  1.00 76.69  ? 363  PRO   A O   1 
ATOM   4517  C  CB  . PRO   B 2 363  ? 116.776 147.110 63.182  1.00 77.81  ? 363  PRO   A CB  1 
ATOM   4518  C  CG  . PRO   B 2 363  ? 117.129 146.910 61.752  1.00 76.10  ? 363  PRO   A CG  1 
ATOM   4519  C  CD  . PRO   B 2 363  ? 117.717 148.207 61.293  1.00 76.71  ? 363  PRO   A CD  1 
ATOM   4520  N  N   . ILE   B 2 364  ? 118.877 147.270 65.758  1.00 71.24  ? 364  ILE   A N   1 
ATOM   4521  C  CA  . ILE   B 2 364  ? 119.798 146.531 66.611  1.00 64.35  ? 364  ILE   A CA  1 
ATOM   4522  C  C   . ILE   B 2 364  ? 118.981 145.467 67.327  1.00 74.18  ? 364  ILE   A C   1 
ATOM   4523  O  O   . ILE   B 2 364  ? 118.001 145.786 68.011  1.00 78.51  ? 364  ILE   A O   1 
ATOM   4524  C  CB  . ILE   B 2 364  ? 120.518 147.444 67.610  1.00 65.29  ? 364  ILE   A CB  1 
ATOM   4525  C  CG1 . ILE   B 2 364  ? 121.442 148.412 66.870  1.00 73.72  ? 364  ILE   A CG1 1 
ATOM   4526  C  CG2 . ILE   B 2 364  ? 121.296 146.625 68.618  1.00 70.94  ? 364  ILE   A CG2 1 
ATOM   4527  C  CD1 . ILE   B 2 364  ? 122.257 149.301 67.780  1.00 76.05  ? 364  ILE   A CD1 1 
ATOM   4528  N  N   . THR   B 2 365  ? 119.369 144.210 67.168  1.00 75.88  ? 365  THR   A N   1 
ATOM   4529  C  CA  . THR   B 2 365  ? 118.675 143.085 67.778  1.00 71.24  ? 365  THR   A CA  1 
ATOM   4530  C  C   . THR   B 2 365  ? 119.666 142.242 68.573  1.00 70.05  ? 365  THR   A C   1 
ATOM   4531  O  O   . THR   B 2 365  ? 120.842 142.587 68.708  1.00 73.20  ? 365  THR   A O   1 
ATOM   4532  C  CB  . THR   B 2 365  ? 117.967 142.241 66.714  1.00 74.59  ? 365  THR   A CB  1 
ATOM   4533  O  OG1 . THR   B 2 365  ? 118.917 141.822 65.727  1.00 74.07  ? 365  THR   A OG1 1 
ATOM   4534  C  CG2 . THR   B 2 365  ? 116.865 143.045 66.042  1.00 74.29  ? 365  THR   A CG2 1 
ATOM   4535  N  N   . LEU   B 2 366  ? 119.174 141.123 69.110  1.00 69.72  ? 366  LEU   A N   1 
ATOM   4536  C  CA  . LEU   B 2 366  ? 120.052 140.207 69.830  1.00 67.17  ? 366  LEU   A CA  1 
ATOM   4537  C  C   . LEU   B 2 366  ? 121.095 139.600 68.905  1.00 71.90  ? 366  LEU   A C   1 
ATOM   4538  O  O   . LEU   B 2 366  ? 122.207 139.285 69.343  1.00 75.11  ? 366  LEU   A O   1 
ATOM   4539  C  CB  . LEU   B 2 366  ? 119.232 139.104 70.498  1.00 69.91  ? 366  LEU   A CB  1 
ATOM   4540  C  CG  . LEU   B 2 366  ? 119.563 138.720 71.943  1.00 72.74  ? 366  LEU   A CG  1 
ATOM   4541  C  CD1 . LEU   B 2 366  ? 119.175 137.273 72.201  1.00 73.73  ? 366  LEU   A CD1 1 
ATOM   4542  C  CD2 . LEU   B 2 366  ? 121.025 138.952 72.286  1.00 73.23  ? 366  LEU   A CD2 1 
ATOM   4543  N  N   . GLU   B 2 367  ? 120.761 139.432 67.625  1.00 76.43  ? 367  GLU   A N   1 
ATOM   4544  C  CA  . GLU   B 2 367  ? 121.715 138.914 66.655  1.00 75.58  ? 367  GLU   A CA  1 
ATOM   4545  C  C   . GLU   B 2 367  ? 122.863 139.878 66.391  1.00 80.88  ? 367  GLU   A C   1 
ATOM   4546  O  O   . GLU   B 2 367  ? 123.846 139.482 65.757  1.00 86.82  ? 367  GLU   A O   1 
ATOM   4547  C  CB  . GLU   B 2 367  ? 121.005 138.586 65.339  1.00 78.46  ? 367  GLU   A CB  1 
ATOM   4548  C  CG  . GLU   B 2 367  ? 120.081 137.376 65.400  1.00 82.43  ? 367  GLU   A CG  1 
ATOM   4549  C  CD  . GLU   B 2 367  ? 118.756 137.675 66.077  1.00 87.75  ? 367  GLU   A CD  1 
ATOM   4550  O  OE1 . GLU   B 2 367  ? 118.469 138.864 66.332  1.00 86.34  ? 367  GLU   A OE1 1 
ATOM   4551  O  OE2 . GLU   B 2 367  ? 118.000 136.720 66.352  1.00 88.55  ? 367  GLU   A OE2 1 
ATOM   4552  N  N   . THR   B 2 368  ? 122.759 141.124 66.849  1.00 72.06  ? 368  THR   A N   1 
ATOM   4553  C  CA  . THR   B 2 368  ? 123.814 142.117 66.695  1.00 67.50  ? 368  THR   A CA  1 
ATOM   4554  C  C   . THR   B 2 368  ? 124.568 142.367 67.995  1.00 69.01  ? 368  THR   A C   1 
ATOM   4555  O  O   . THR   B 2 368  ? 125.793 142.502 67.988  1.00 73.72  ? 368  THR   A O   1 
ATOM   4556  C  CB  . THR   B 2 368  ? 123.222 143.431 66.174  1.00 72.00  ? 368  THR   A CB  1 
ATOM   4557  O  OG1 . THR   B 2 368  ? 122.631 143.212 64.888  1.00 75.54  ? 368  THR   A OG1 1 
ATOM   4558  C  CG2 . THR   B 2 368  ? 124.299 144.497 66.056  1.00 74.15  ? 368  THR   A CG2 1 
ATOM   4559  N  N   . THR   B 2 369  ? 123.859 142.418 69.117  1.00 70.07  ? 369  THR   A N   1 
ATOM   4560  C  CA  . THR   B 2 369  ? 124.495 142.685 70.394  1.00 69.33  ? 369  THR   A CA  1 
ATOM   4561  C  C   . THR   B 2 369  ? 125.083 141.406 70.984  1.00 67.41  ? 369  THR   A C   1 
ATOM   4562  O  O   . THR   B 2 369  ? 124.777 140.289 70.560  1.00 76.32  ? 369  THR   A O   1 
ATOM   4563  C  CB  . THR   B 2 369  ? 123.500 143.302 71.373  1.00 76.45  ? 369  THR   A CB  1 
ATOM   4564  O  OG1 . THR   B 2 369  ? 124.173 143.636 72.594  1.00 77.77  ? 369  THR   A OG1 1 
ATOM   4565  C  CG2 . THR   B 2 369  ? 122.385 142.323 71.676  1.00 77.73  ? 369  THR   A CG2 1 
ATOM   4566  N  N   . MET   B 2 370  ? 125.942 141.586 71.984  1.00 59.83  ? 370  MET   A N   1 
ATOM   4567  C  CA  . MET   B 2 370  ? 126.570 140.469 72.681  1.00 64.42  ? 370  MET   A CA  1 
ATOM   4568  C  C   . MET   B 2 370  ? 126.747 140.861 74.139  1.00 63.89  ? 370  MET   A C   1 
ATOM   4569  O  O   . MET   B 2 370  ? 127.353 141.894 74.435  1.00 66.07  ? 370  MET   A O   1 
ATOM   4570  C  CB  . MET   B 2 370  ? 127.905 140.101 72.038  1.00 63.38  ? 370  MET   A CB  1 
ATOM   4571  C  CG  . MET   B 2 370  ? 128.468 141.185 71.135  1.00 65.21  ? 370  MET   A CG  1 
ATOM   4572  S  SD  . MET   B 2 370  ? 129.975 140.709 70.267  1.00 79.79  ? 370  MET   A SD  1 
ATOM   4573  C  CE  . MET   B 2 370  ? 129.400 139.312 69.310  1.00 69.13  ? 370  MET   A CE  1 
ATOM   4574  N  N   . LEU   B 2 371  ? 126.228 140.030 75.041  1.00 60.40  ? 371  LEU   A N   1 
ATOM   4575  C  CA  . LEU   B 2 371  ? 126.008 140.440 76.419  1.00 56.20  ? 371  LEU   A CA  1 
ATOM   4576  C  C   . LEU   B 2 371  ? 127.303 140.391 77.231  1.00 62.61  ? 371  LEU   A C   1 
ATOM   4577  O  O   . LEU   B 2 371  ? 128.352 139.942 76.765  1.00 72.85  ? 371  LEU   A O   1 
ATOM   4578  C  CB  . LEU   B 2 371  ? 124.943 139.557 77.066  1.00 61.36  ? 371  LEU   A CB  1 
ATOM   4579  C  CG  . LEU   B 2 371  ? 123.642 139.424 76.276  1.00 65.42  ? 371  LEU   A CG  1 
ATOM   4580  C  CD1 . LEU   B 2 371  ? 122.631 138.592 77.044  1.00 66.38  ? 371  LEU   A CD1 1 
ATOM   4581  C  CD2 . LEU   B 2 371  ? 123.071 140.791 75.948  1.00 65.87  ? 371  LEU   A CD2 1 
ATOM   4582  N  N   . ARG   B 2 372  ? 127.209 140.863 78.473  1.00 58.18  ? 372  ARG   A N   1 
ATOM   4583  C  CA  . ARG   B 2 372  ? 128.365 140.958 79.355  1.00 60.92  ? 372  ARG   A CA  1 
ATOM   4584  C  C   . ARG   B 2 372  ? 128.594 139.657 80.115  1.00 62.63  ? 372  ARG   A C   1 
ATOM   4585  O  O   . ARG   B 2 372  ? 127.645 138.957 80.481  1.00 67.85  ? 372  ARG   A O   1 
ATOM   4586  C  CB  . ARG   B 2 372  ? 128.185 142.104 80.353  1.00 63.76  ? 372  ARG   A CB  1 
ATOM   4587  C  CG  . ARG   B 2 372  ? 129.273 142.160 81.421  1.00 60.66  ? 372  ARG   A CG  1 
ATOM   4588  C  CD  . ARG   B 2 372  ? 129.018 143.198 82.487  1.00 59.71  ? 372  ARG   A CD  1 
ATOM   4589  N  NE  . ARG   B 2 372  ? 129.996 143.071 83.560  1.00 57.33  ? 372  ARG   A NE  1 
ATOM   4590  C  CZ  . ARG   B 2 372  ? 130.254 144.004 84.465  1.00 58.82  ? 372  ARG   A CZ  1 
ATOM   4591  N  NH1 . ARG   B 2 372  ? 129.632 145.171 84.454  1.00 59.97  ? 372  ARG   A NH1 1 
ATOM   4592  N  NH2 . ARG   B 2 372  ? 131.162 143.759 85.403  1.00 60.93  ? 372  ARG   A NH2 1 
ATOM   4593  N  N   . GLY   B 2 373  ? 129.868 139.344 80.357  1.00 68.67  ? 373  GLY   A N   1 
ATOM   4594  C  CA  . GLY   B 2 373  ? 130.257 138.221 81.179  1.00 69.00  ? 373  GLY   A CA  1 
ATOM   4595  C  C   . GLY   B 2 373  ? 130.180 136.886 80.490  1.00 69.66  ? 373  GLY   A C   1 
ATOM   4596  O  O   . GLY   B 2 373  ? 130.601 135.882 81.074  1.00 74.37  ? 373  GLY   A O   1 
ATOM   4597  N  N   . CYS   B 2 374  ? 129.659 136.840 79.267  1.00 69.33  ? 374  CYS   A N   1 
ATOM   4598  C  CA  . CYS   B 2 374  ? 129.543 135.614 78.484  1.00 72.43  ? 374  CYS   A CA  1 
ATOM   4599  C  C   . CYS   B 2 374  ? 129.858 135.974 77.037  1.00 67.71  ? 374  CYS   A C   1 
ATOM   4600  O  O   . CYS   B 2 374  ? 129.018 136.508 76.308  1.00 64.99  ? 374  CYS   A O   1 
ATOM   4601  C  CB  . CYS   B 2 374  ? 128.156 134.991 78.653  1.00 74.82  ? 374  CYS   A CB  1 
ATOM   4602  S  SG  . CYS   B 2 374  ? 127.480 134.184 77.190  1.00 90.70  ? 374  CYS   A SG  1 
ATOM   4603  N  N   . VAL   B 2 375  ? 131.114 135.786 76.652  1.00 70.32  ? 375  VAL   A N   1 
ATOM   4604  C  CA  . VAL   B 2 375  ? 131.449 135.754 75.236  1.00 75.21  ? 375  VAL   A CA  1 
ATOM   4605  C  C   . VAL   B 2 375  ? 132.410 134.604 74.961  1.00 70.26  ? 375  VAL   A C   1 
ATOM   4606  O  O   . VAL   B 2 375  ? 132.082 133.689 74.199  1.00 77.76  ? 375  VAL   A O   1 
ATOM   4607  C  CB  . VAL   B 2 375  ? 132.006 137.106 74.753  1.00 79.60  ? 375  VAL   A CB  1 
ATOM   4608  C  CG1 . VAL   B 2 375  ? 133.026 137.666 75.719  1.00 77.75  ? 375  VAL   A CG1 1 
ATOM   4609  C  CG2 . VAL   B 2 375  ? 132.597 136.968 73.368  1.00 74.36  ? 375  VAL   A CG2 1 
ATOM   4610  N  N   . LEU   B 2 376  ? 133.568 134.616 75.617  1.00 63.66  ? 376  LEU   A N   1 
ATOM   4611  C  CA  . LEU   B 2 376  ? 134.669 133.705 75.307  1.00 74.45  ? 376  LEU   A CA  1 
ATOM   4612  C  C   . LEU   B 2 376  ? 134.798 133.545 73.794  1.00 78.10  ? 376  LEU   A C   1 
ATOM   4613  O  O   . LEU   B 2 376  ? 134.672 132.456 73.233  1.00 78.10  ? 376  LEU   A O   1 
ATOM   4614  C  CB  . LEU   B 2 376  ? 134.490 132.359 76.006  1.00 74.49  ? 376  LEU   A CB  1 
ATOM   4615  C  CG  . LEU   B 2 376  ? 134.563 132.420 77.532  1.00 74.21  ? 376  LEU   A CG  1 
ATOM   4616  C  CD1 . LEU   B 2 376  ? 134.478 131.025 78.139  1.00 72.20  ? 376  LEU   A CD1 1 
ATOM   4617  C  CD2 . LEU   B 2 376  ? 135.835 133.132 77.969  1.00 72.68  ? 376  LEU   A CD2 1 
ATOM   4618  N  N   . LYS   B 2 377  ? 135.021 134.685 73.141  1.00 65.27  ? 377  LYS   A N   1 
ATOM   4619  C  CA  . LYS   B 2 377  ? 134.896 134.777 71.694  1.00 64.48  ? 377  LYS   A CA  1 
ATOM   4620  C  C   . LYS   B 2 377  ? 135.811 133.778 70.997  1.00 68.13  ? 377  LYS   A C   1 
ATOM   4621  O  O   . LYS   B 2 377  ? 136.984 133.632 71.349  1.00 72.75  ? 377  LYS   A O   1 
ATOM   4622  C  CB  . LYS   B 2 377  ? 135.216 136.200 71.239  1.00 57.52  ? 377  LYS   A CB  1 
ATOM   4623  C  CG  . LYS   B 2 377  ? 134.794 136.505 69.829  1.00 61.24  ? 377  LYS   A CG  1 
ATOM   4624  C  CD  . LYS   B 2 377  ? 135.011 137.964 69.502  1.00 62.17  ? 377  LYS   A CD  1 
ATOM   4625  C  CE  . LYS   B 2 377  ? 134.194 138.850 70.419  1.00 70.31  ? 377  LYS   A CE  1 
ATOM   4626  N  NZ  . LYS   B 2 377  ? 132.736 138.588 70.273  1.00 71.74  ? 377  LYS   A NZ  1 
ATOM   4627  N  N   . ASN   B 2 378  ? 135.262 133.087 69.998  1.00 57.36  ? 378  ASN   A N   1 
ATOM   4628  C  CA  . ASN   B 2 378  ? 135.971 132.034 69.284  1.00 60.09  ? 378  ASN   A CA  1 
ATOM   4629  C  C   . ASN   B 2 378  ? 136.299 132.436 67.847  1.00 60.82  ? 378  ASN   A C   1 
ATOM   4630  O  O   . ASN   B 2 378  ? 136.453 131.581 66.973  1.00 51.40  ? 378  ASN   A O   1 
ATOM   4631  C  CB  . ASN   B 2 378  ? 135.159 130.741 69.314  1.00 64.13  ? 378  ASN   A CB  1 
ATOM   4632  C  CG  . ASN   B 2 378  ? 134.537 130.477 70.676  1.00 68.22  ? 378  ASN   A CG  1 
ATOM   4633  O  OD1 . ASN   B 2 378  ? 133.375 130.084 70.772  1.00 60.42  ? 378  ASN   A OD1 1 
ATOM   4634  N  ND2 . ASN   B 2 378  ? 135.307 130.704 71.735  1.00 71.07  ? 378  ASN   A ND2 1 
ATOM   4635  N  N   . THR   B 2 379  ? 136.417 133.737 67.597  1.00 69.78  ? 379  THR   A N   1 
ATOM   4636  C  CA  . THR   B 2 379  ? 136.785 134.265 66.290  1.00 62.60  ? 379  THR   A CA  1 
ATOM   4637  C  C   . THR   B 2 379  ? 137.849 135.336 66.501  1.00 67.79  ? 379  THR   A C   1 
ATOM   4638  O  O   . THR   B 2 379  ? 138.456 135.431 67.571  1.00 71.50  ? 379  THR   A O   1 
ATOM   4639  C  CB  . THR   B 2 379  ? 135.561 134.812 65.545  1.00 65.88  ? 379  THR   A CB  1 
ATOM   4640  O  OG1 . THR   B 2 379  ? 135.982 135.399 64.311  1.00 66.48  ? 379  THR   A OG1 1 
ATOM   4641  C  CG2 . THR   B 2 379  ? 134.860 135.868 66.372  1.00 70.93  ? 379  THR   A CG2 1 
ATOM   4642  N  N   . ALA   B 2 380  ? 138.076 136.150 65.478  1.00 67.68  ? 380  ALA   A N   1 
ATOM   4643  C  CA  . ALA   B 2 380  ? 139.115 137.170 65.526  1.00 67.85  ? 380  ALA   A CA  1 
ATOM   4644  C  C   . ALA   B 2 380  ? 138.637 138.357 66.362  1.00 70.17  ? 380  ALA   A C   1 
ATOM   4645  O  O   . ALA   B 2 380  ? 137.678 138.263 67.134  1.00 74.05  ? 380  ALA   A O   1 
ATOM   4646  C  CB  . ALA   B 2 380  ? 139.513 137.583 64.113  1.00 67.02  ? 380  ALA   A CB  1 
ATOM   4647  N  N   . TRP   B 2 381  ? 139.323 139.489 66.231  1.00 59.93  ? 381  TRP   A N   1 
ATOM   4648  C  CA  . TRP   B 2 381  ? 138.974 140.681 66.987  1.00 57.07  ? 381  TRP   A CA  1 
ATOM   4649  C  C   . TRP   B 2 381  ? 137.584 141.186 66.612  1.00 61.01  ? 381  TRP   A C   1 
ATOM   4650  O  O   . TRP   B 2 381  ? 137.104 141.009 65.489  1.00 66.80  ? 381  TRP   A O   1 
ATOM   4651  C  CB  . TRP   B 2 381  ? 140.002 141.784 66.751  1.00 61.94  ? 381  TRP   A CB  1 
ATOM   4652  C  CG  . TRP   B 2 381  ? 140.193 142.132 65.309  1.00 55.36  ? 381  TRP   A CG  1 
ATOM   4653  C  CD1 . TRP   B 2 381  ? 141.137 141.627 64.468  1.00 57.36  ? 381  TRP   A CD1 1 
ATOM   4654  C  CD2 . TRP   B 2 381  ? 139.431 143.069 64.542  1.00 54.41  ? 381  TRP   A CD2 1 
ATOM   4655  N  NE1 . TRP   B 2 381  ? 141.010 142.189 63.223  1.00 57.95  ? 381  TRP   A NE1 1 
ATOM   4656  C  CE2 . TRP   B 2 381  ? 139.969 143.078 63.243  1.00 59.07  ? 381  TRP   A CE2 1 
ATOM   4657  C  CE3 . TRP   B 2 381  ? 138.347 143.902 64.828  1.00 60.52  ? 381  TRP   A CE3 1 
ATOM   4658  C  CZ2 . TRP   B 2 381  ? 139.459 143.883 62.231  1.00 64.27  ? 381  TRP   A CZ2 1 
ATOM   4659  C  CZ3 . TRP   B 2 381  ? 137.843 144.700 63.822  1.00 66.29  ? 381  TRP   A CZ3 1 
ATOM   4660  C  CH2 . TRP   B 2 381  ? 138.398 144.686 62.540  1.00 67.60  ? 381  TRP   A CH2 1 
ATOM   4661  N  N   . VAL   B 2 382  ? 136.936 141.825 67.581  1.00 60.44  ? 382  VAL   A N   1 
ATOM   4662  C  CA  . VAL   B 2 382  ? 135.615 142.419 67.406  1.00 57.81  ? 382  VAL   A CA  1 
ATOM   4663  C  C   . VAL   B 2 382  ? 135.634 143.813 68.016  1.00 66.05  ? 382  VAL   A C   1 
ATOM   4664  O  O   . VAL   B 2 382  ? 136.108 143.995 69.142  1.00 73.26  ? 382  VAL   A O   1 
ATOM   4665  C  CB  . VAL   B 2 382  ? 134.514 141.557 68.054  1.00 57.33  ? 382  VAL   A CB  1 
ATOM   4666  C  CG1 . VAL   B 2 382  ? 133.394 142.425 68.590  1.00 59.30  ? 382  VAL   A CG1 1 
ATOM   4667  C  CG2 . VAL   B 2 382  ? 133.973 140.552 67.058  1.00 62.09  ? 382  VAL   A CG2 1 
ATOM   4668  N  N   . ILE   B 2 383  ? 135.132 144.796 67.275  1.00 56.88  ? 383  ILE   A N   1 
ATOM   4669  C  CA  . ILE   B 2 383  ? 134.963 146.146 67.795  1.00 50.96  ? 383  ILE   A CA  1 
ATOM   4670  C  C   . ILE   B 2 383  ? 133.478 146.394 68.008  1.00 57.61  ? 383  ILE   A C   1 
ATOM   4671  O  O   . ILE   B 2 383  ? 132.626 145.829 67.313  1.00 67.77  ? 383  ILE   A O   1 
ATOM   4672  C  CB  . ILE   B 2 383  ? 135.570 147.220 66.873  1.00 50.47  ? 383  ILE   A CB  1 
ATOM   4673  C  CG1 . ILE   B 2 383  ? 134.794 147.299 65.561  1.00 59.70  ? 383  ILE   A CG1 1 
ATOM   4674  C  CG2 . ILE   B 2 383  ? 137.035 146.925 66.610  1.00 59.78  ? 383  ILE   A CG2 1 
ATOM   4675  C  CD1 . ILE   B 2 383  ? 135.053 148.561 64.782  1.00 63.35  ? 383  ILE   A CD1 1 
ATOM   4676  N  N   . GLY   B 2 384  ? 133.168 147.238 68.984  1.00 59.64  ? 384  GLY   A N   1 
ATOM   4677  C  CA  . GLY   B 2 384  ? 131.777 147.474 69.317  1.00 62.18  ? 384  GLY   A CA  1 
ATOM   4678  C  C   . GLY   B 2 384  ? 131.617 148.727 70.146  1.00 65.94  ? 384  GLY   A C   1 
ATOM   4679  O  O   . GLY   B 2 384  ? 132.590 149.390 70.510  1.00 69.82  ? 384  GLY   A O   1 
ATOM   4680  N  N   . ILE   B 2 385  ? 130.359 149.040 70.440  1.00 66.06  ? 385  ILE   A N   1 
ATOM   4681  C  CA  . ILE   B 2 385  ? 129.983 150.221 71.208  1.00 58.00  ? 385  ILE   A CA  1 
ATOM   4682  C  C   . ILE   B 2 385  ? 129.352 149.750 72.509  1.00 66.42  ? 385  ILE   A C   1 
ATOM   4683  O  O   . ILE   B 2 385  ? 128.358 149.014 72.490  1.00 73.16  ? 385  ILE   A O   1 
ATOM   4684  C  CB  . ILE   B 2 385  ? 129.013 151.124 70.431  1.00 59.76  ? 385  ILE   A CB  1 
ATOM   4685  C  CG1 . ILE   B 2 385  ? 129.698 151.735 69.207  1.00 65.46  ? 385  ILE   A CG1 1 
ATOM   4686  C  CG2 . ILE   B 2 385  ? 128.458 152.209 71.335  1.00 67.74  ? 385  ILE   A CG2 1 
ATOM   4687  C  CD1 . ILE   B 2 385  ? 129.578 150.905 67.945  1.00 65.74  ? 385  ILE   A CD1 1 
ATOM   4688  N  N   . ILE   B 2 386  ? 129.919 150.179 73.634  1.00 64.15  ? 386  ILE   A N   1 
ATOM   4689  C  CA  . ILE   B 2 386  ? 129.438 149.749 74.944  1.00 56.37  ? 386  ILE   A CA  1 
ATOM   4690  C  C   . ILE   B 2 386  ? 128.085 150.405 75.199  1.00 62.52  ? 386  ILE   A C   1 
ATOM   4691  O  O   . ILE   B 2 386  ? 127.973 151.634 75.228  1.00 75.97  ? 386  ILE   A O   1 
ATOM   4692  C  CB  . ILE   B 2 386  ? 130.437 150.090 76.054  1.00 58.20  ? 386  ILE   A CB  1 
ATOM   4693  C  CG1 . ILE   B 2 386  ? 131.685 149.216 75.944  1.00 62.36  ? 386  ILE   A CG1 1 
ATOM   4694  C  CG2 . ILE   B 2 386  ? 129.799 149.906 77.415  1.00 63.25  ? 386  ILE   A CG2 1 
ATOM   4695  C  CD1 . ILE   B 2 386  ? 131.440 147.761 76.259  1.00 66.59  ? 386  ILE   A CD1 1 
ATOM   4696  N  N   . VAL   B 2 387  ? 127.055 149.584 75.382  1.00 56.88  ? 387  VAL   A N   1 
ATOM   4697  C  CA  . VAL   B 2 387  ? 125.720 150.043 75.735  1.00 52.93  ? 387  VAL   A CA  1 
ATOM   4698  C  C   . VAL   B 2 387  ? 125.232 149.218 76.916  1.00 64.77  ? 387  VAL   A C   1 
ATOM   4699  O  O   . VAL   B 2 387  ? 125.730 148.118 77.174  1.00 73.94  ? 387  VAL   A O   1 
ATOM   4700  C  CB  . VAL   B 2 387  ? 124.737 149.933 74.552  1.00 45.92  ? 387  VAL   A CB  1 
ATOM   4701  C  CG1 . VAL   B 2 387  ? 125.213 150.772 73.388  1.00 53.81  ? 387  VAL   A CG1 1 
ATOM   4702  C  CG2 . VAL   B 2 387  ? 124.571 148.485 74.132  1.00 63.01  ? 387  VAL   A CG2 1 
ATOM   4703  N  N   . TYR   B 2 388  ? 124.256 149.763 77.643  1.00 60.11  ? 388  TYR   A N   1 
ATOM   4704  C  CA  . TYR   B 2 388  ? 123.651 149.092 78.794  1.00 52.54  ? 388  TYR   A CA  1 
ATOM   4705  C  C   . TYR   B 2 388  ? 124.708 148.693 79.827  1.00 61.82  ? 388  TYR   A C   1 
ATOM   4706  O  O   . TYR   B 2 388  ? 124.618 147.649 80.470  1.00 70.02  ? 388  TYR   A O   1 
ATOM   4707  C  CB  . TYR   B 2 388  ? 122.847 147.865 78.354  1.00 57.42  ? 388  TYR   A CB  1 
ATOM   4708  C  CG  . TYR   B 2 388  ? 121.571 148.159 77.608  1.00 57.53  ? 388  TYR   A CG  1 
ATOM   4709  C  CD1 . TYR   B 2 388  ? 120.735 149.189 78.000  1.00 63.11  ? 388  TYR   A CD1 1 
ATOM   4710  C  CD2 . TYR   B 2 388  ? 121.196 147.391 76.517  1.00 63.41  ? 388  TYR   A CD2 1 
ATOM   4711  C  CE1 . TYR   B 2 388  ? 119.565 149.453 77.322  1.00 70.10  ? 388  TYR   A CE1 1 
ATOM   4712  C  CE2 . TYR   B 2 388  ? 120.029 147.646 75.831  1.00 65.73  ? 388  TYR   A CE2 1 
ATOM   4713  C  CZ  . TYR   B 2 388  ? 119.216 148.678 76.239  1.00 68.36  ? 388  TYR   A CZ  1 
ATOM   4714  O  OH  . TYR   B 2 388  ? 118.050 148.938 75.558  1.00 71.10  ? 388  TYR   A OH  1 
ATOM   4715  N  N   . THR   B 2 389  ? 125.714 149.548 79.984  1.00 64.89  ? 389  THR   A N   1 
ATOM   4716  C  CA  . THR   B 2 389  ? 126.838 149.232 80.852  1.00 63.17  ? 389  THR   A CA  1 
ATOM   4717  C  C   . THR   B 2 389  ? 126.431 149.313 82.322  1.00 61.10  ? 389  THR   A C   1 
ATOM   4718  O  O   . THR   B 2 389  ? 125.398 149.880 82.682  1.00 70.74  ? 389  THR   A O   1 
ATOM   4719  C  CB  . THR   B 2 389  ? 128.014 150.164 80.574  1.00 65.09  ? 389  THR   A CB  1 
ATOM   4720  O  OG1 . THR   B 2 389  ? 129.201 149.620 81.166  1.00 67.17  ? 389  THR   A OG1 1 
ATOM   4721  C  CG2 . THR   B 2 389  ? 127.755 151.538 81.168  1.00 66.90  ? 389  THR   A CG2 1 
ATOM   4722  N  N   . GLY   B 2 390  ? 127.262 148.732 83.184  1.00 54.57  ? 390  GLY   A N   1 
ATOM   4723  C  CA  . GLY   B 2 390  ? 127.030 148.839 84.615  1.00 60.04  ? 390  GLY   A CA  1 
ATOM   4724  C  C   . GLY   B 2 390  ? 126.026 147.819 85.118  1.00 60.78  ? 390  GLY   A C   1 
ATOM   4725  O  O   . GLY   B 2 390  ? 126.014 146.658 84.698  1.00 61.41  ? 390  GLY   A O   1 
ATOM   4726  N  N   . GLU   B 2 391  ? 125.171 148.259 86.041  1.00 66.83  ? 391  GLU   A N   1 
ATOM   4727  C  CA  . GLU   B 2 391  ? 124.177 147.385 86.650  1.00 60.86  ? 391  GLU   A CA  1 
ATOM   4728  C  C   . GLU   B 2 391  ? 122.966 147.157 85.761  1.00 60.61  ? 391  GLU   A C   1 
ATOM   4729  O  O   . GLU   B 2 391  ? 122.088 146.374 86.135  1.00 64.69  ? 391  GLU   A O   1 
ATOM   4730  C  CB  . GLU   B 2 391  ? 123.736 147.953 88.001  1.00 66.64  ? 391  GLU   A CB  1 
ATOM   4731  C  CG  . GLU   B 2 391  ? 123.132 149.347 87.937  1.00 72.61  ? 391  GLU   A CG  1 
ATOM   4732  C  CD  . GLU   B 2 391  ? 121.621 149.327 87.811  1.00 74.54  ? 391  GLU   A CD  1 
ATOM   4733  O  OE1 . GLU   B 2 391  ? 121.021 148.247 87.990  1.00 71.41  ? 391  GLU   A OE1 1 
ATOM   4734  O  OE2 . GLU   B 2 391  ? 121.033 150.394 87.535  1.00 74.34  ? 391  GLU   A OE2 1 
ATOM   4735  N  N   . ASP   B 2 392  ? 122.892 147.813 84.607  1.00 61.68  ? 392  ASP   A N   1 
ATOM   4736  C  CA  . ASP   B 2 392  ? 121.815 147.604 83.653  1.00 64.78  ? 392  ASP   A CA  1 
ATOM   4737  C  C   . ASP   B 2 392  ? 122.109 146.475 82.674  1.00 72.05  ? 392  ASP   A C   1 
ATOM   4738  O  O   . ASP   B 2 392  ? 121.290 146.209 81.789  1.00 75.73  ? 392  ASP   A O   1 
ATOM   4739  C  CB  . ASP   B 2 392  ? 121.533 148.895 82.891  1.00 68.40  ? 392  ASP   A CB  1 
ATOM   4740  C  CG  . ASP   B 2 392  ? 121.050 150.009 83.796  1.00 75.56  ? 392  ASP   A CG  1 
ATOM   4741  O  OD1 . ASP   B 2 392  ? 120.373 149.708 84.801  1.00 75.07  ? 392  ASP   A OD1 1 
ATOM   4742  O  OD2 . ASP   B 2 392  ? 121.347 151.186 83.503  1.00 76.78  ? 392  ASP   A OD2 1 
ATOM   4743  N  N   . THR   B 2 393  ? 123.256 145.813 82.807  1.00 68.11  ? 393  THR   A N   1 
ATOM   4744  C  CA  . THR   B 2 393  ? 123.559 144.659 81.979  1.00 56.75  ? 393  THR   A CA  1 
ATOM   4745  C  C   . THR   B 2 393  ? 122.574 143.530 82.261  1.00 66.77  ? 393  THR   A C   1 
ATOM   4746  O  O   . THR   B 2 393  ? 121.941 143.470 83.317  1.00 74.92  ? 393  THR   A O   1 
ATOM   4747  C  CB  . THR   B 2 393  ? 124.983 144.164 82.232  1.00 61.16  ? 393  THR   A CB  1 
ATOM   4748  O  OG1 . THR   B 2 393  ? 125.160 143.920 83.632  1.00 71.22  ? 393  THR   A OG1 1 
ATOM   4749  C  CG2 . THR   B 2 393  ? 126.000 145.187 81.771  1.00 65.11  ? 393  THR   A CG2 1 
ATOM   4750  N  N   . LYS   B 2 394  ? 122.448 142.626 81.289  1.00 69.26  ? 394  LYS   A N   1 
ATOM   4751  C  CA  . LYS   B 2 394  ? 121.572 141.472 81.466  1.00 66.65  ? 394  LYS   A CA  1 
ATOM   4752  C  C   . LYS   B 2 394  ? 122.044 140.594 82.616  1.00 67.15  ? 394  LYS   A C   1 
ATOM   4753  O  O   . LYS   B 2 394  ? 121.234 140.113 83.416  1.00 75.10  ? 394  LYS   A O   1 
ATOM   4754  C  CB  . LYS   B 2 394  ? 121.508 140.661 80.174  1.00 64.60  ? 394  LYS   A CB  1 
ATOM   4755  C  CG  . LYS   B 2 394  ? 121.068 141.447 78.958  1.00 64.00  ? 394  LYS   A CG  1 
ATOM   4756  C  CD  . LYS   B 2 394  ? 119.566 141.621 78.930  1.00 67.51  ? 394  LYS   A CD  1 
ATOM   4757  C  CE  . LYS   B 2 394  ? 119.117 142.293 77.647  1.00 72.00  ? 394  LYS   A CE  1 
ATOM   4758  N  NZ  . LYS   B 2 394  ? 117.639 142.465 77.601  1.00 75.20  ? 394  LYS   A NZ  1 
ATOM   4759  N  N   . ILE   B 2 395  ? 123.355 140.382 82.719  1.00 59.92  ? 395  ILE   A N   1 
ATOM   4760  C  CA  . ILE   B 2 395  ? 123.892 139.434 83.689  1.00 61.64  ? 395  ILE   A CA  1 
ATOM   4761  C  C   . ILE   B 2 395  ? 123.708 139.948 85.114  1.00 65.83  ? 395  ILE   A C   1 
ATOM   4762  O  O   . ILE   B 2 395  ? 123.229 139.223 85.995  1.00 67.31  ? 395  ILE   A O   1 
ATOM   4763  C  CB  . ILE   B 2 395  ? 125.368 139.137 83.365  1.00 62.35  ? 395  ILE   A CB  1 
ATOM   4764  C  CG1 . ILE   B 2 395  ? 126.044 138.391 84.508  1.00 62.51  ? 395  ILE   A CG1 1 
ATOM   4765  C  CG2 . ILE   B 2 395  ? 126.118 140.417 83.025  1.00 64.85  ? 395  ILE   A CG2 1 
ATOM   4766  C  CD1 . ILE   B 2 395  ? 127.391 137.845 84.126  1.00 66.30  ? 395  ILE   A CD1 1 
ATOM   4767  N  N   . ILE   B 2 396  ? 124.069 141.210 85.359  1.00 62.70  ? 396  ILE   A N   1 
ATOM   4768  C  CA  . ILE   B 2 396  ? 123.941 141.768 86.703  1.00 59.60  ? 396  ILE   A CA  1 
ATOM   4769  C  C   . ILE   B 2 396  ? 122.475 141.899 87.091  1.00 60.04  ? 396  ILE   A C   1 
ATOM   4770  O  O   . ILE   B 2 396  ? 122.095 141.618 88.234  1.00 61.34  ? 396  ILE   A O   1 
ATOM   4771  C  CB  . ILE   B 2 396  ? 124.678 143.116 86.797  1.00 60.37  ? 396  ILE   A CB  1 
ATOM   4772  C  CG1 . ILE   B 2 396  ? 126.175 142.921 86.564  1.00 62.22  ? 396  ILE   A CG1 1 
ATOM   4773  C  CG2 . ILE   B 2 396  ? 124.439 143.764 88.149  1.00 64.99  ? 396  ILE   A CG2 1 
ATOM   4774  C  CD1 . ILE   B 2 396  ? 126.979 144.196 86.657  1.00 64.70  ? 396  ILE   A CD1 1 
ATOM   4775  N  N   . ARG   B 2 397  ? 121.629 142.325 86.152  1.00 59.18  ? 397  ARG   A N   1 
ATOM   4776  C  CA  . ARG   B 2 397  ? 120.206 142.443 86.448  1.00 59.61  ? 397  ARG   A CA  1 
ATOM   4777  C  C   . ARG   B 2 397  ? 119.584 141.088 86.756  1.00 62.55  ? 397  ARG   A C   1 
ATOM   4778  O  O   . ARG   B 2 397  ? 118.745 140.983 87.657  1.00 63.25  ? 397  ARG   A O   1 
ATOM   4779  C  CB  . ARG   B 2 397  ? 119.483 143.116 85.284  1.00 57.82  ? 397  ARG   A CB  1 
ATOM   4780  C  CG  . ARG   B 2 397  ? 118.023 143.407 85.548  1.00 63.99  ? 397  ARG   A CG  1 
ATOM   4781  C  CD  . ARG   B 2 397  ? 117.470 144.369 84.516  1.00 64.25  ? 397  ARG   A CD  1 
ATOM   4782  N  NE  . ARG   B 2 397  ? 118.166 145.649 84.554  1.00 65.13  ? 397  ARG   A NE  1 
ATOM   4783  C  CZ  . ARG   B 2 397  ? 117.797 146.679 85.301  1.00 66.25  ? 397  ARG   A CZ  1 
ATOM   4784  N  NH1 . ARG   B 2 397  ? 116.728 146.621 86.076  1.00 61.93  ? 397  ARG   A NH1 1 
ATOM   4785  N  NH2 . ARG   B 2 397  ? 118.516 147.797 85.266  1.00 66.98  ? 397  ARG   A NH2 1 
ATOM   4786  N  N   . ASN   B 2 398  ? 119.976 140.042 86.025  1.00 61.45  ? 398  ASN   A N   1 
ATOM   4787  C  CA  . ASN   B 2 398  ? 119.506 138.702 86.350  1.00 57.33  ? 398  ASN   A CA  1 
ATOM   4788  C  C   . ASN   B 2 398  ? 120.091 138.199 87.662  1.00 59.83  ? 398  ASN   A C   1 
ATOM   4789  O  O   . ASN   B 2 398  ? 119.505 137.316 88.297  1.00 63.17  ? 398  ASN   A O   1 
ATOM   4790  C  CB  . ASN   B 2 398  ? 119.837 137.735 85.215  1.00 55.25  ? 398  ASN   A CB  1 
ATOM   4791  C  CG  . ASN   B 2 398  ? 118.946 137.931 84.009  1.00 61.02  ? 398  ASN   A CG  1 
ATOM   4792  O  OD1 . ASN   B 2 398  ? 117.872 137.341 83.917  1.00 62.51  ? 398  ASN   A OD1 1 
ATOM   4793  N  ND2 . ASN   B 2 398  ? 119.385 138.766 83.077  1.00 63.82  ? 398  ASN   A ND2 1 
ATOM   4794  N  N   . ALA   B 2 399  ? 121.234 138.736 88.078  1.00 61.06  ? 399  ALA   A N   1 
ATOM   4795  C  CA  . ALA   B 2 399  ? 121.733 138.474 89.418  1.00 58.77  ? 399  ALA   A CA  1 
ATOM   4796  C  C   . ALA   B 2 399  ? 120.939 139.296 90.432  1.00 61.61  ? 399  ALA   A C   1 
ATOM   4797  O  O   . ALA   B 2 399  ? 119.978 139.993 90.097  1.00 68.61  ? 399  ALA   A O   1 
ATOM   4798  C  CB  . ALA   B 2 399  ? 123.225 138.784 89.501  1.00 63.39  ? 399  ALA   A CB  1 
ATOM   4799  N  N   . GLY   B 2 400  ? 121.349 139.217 91.695  1.00 62.18  ? 400  GLY   A N   1 
ATOM   4800  C  CA  . GLY   B 2 400  ? 120.652 139.923 92.749  1.00 60.41  ? 400  GLY   A CA  1 
ATOM   4801  C  C   . GLY   B 2 400  ? 121.612 140.419 93.808  1.00 66.17  ? 400  GLY   A C   1 
ATOM   4802  O  O   . GLY   B 2 400  ? 122.812 140.140 93.771  1.00 68.87  ? 400  GLY   A O   1 
ATOM   4803  N  N   . ALA   B 2 401  ? 121.063 141.170 94.758  1.00 68.34  ? 401  ALA   A N   1 
ATOM   4804  C  CA  . ALA   B 2 401  ? 121.856 141.684 95.864  1.00 73.76  ? 401  ALA   A CA  1 
ATOM   4805  C  C   . ALA   B 2 401  ? 122.287 140.552 96.788  1.00 69.49  ? 401  ALA   A C   1 
ATOM   4806  O  O   . ALA   B 2 401  ? 121.576 139.560 96.967  1.00 68.31  ? 401  ALA   A O   1 
ATOM   4807  C  CB  . ALA   B 2 401  ? 121.063 142.728 96.649  1.00 70.28  ? 401  ALA   A CB  1 
ATOM   4808  N  N   . THR   B 2 402  ? 123.464 140.708 97.376  1.00 64.69  ? 402  THR   A N   1 
ATOM   4809  C  CA  . THR   B 2 402  ? 124.009 139.674 98.248  1.00 66.39  ? 402  THR   A CA  1 
ATOM   4810  C  C   . THR   B 2 402  ? 123.208 139.607 99.540  1.00 70.04  ? 402  THR   A C   1 
ATOM   4811  O  O   . THR   B 2 402  ? 123.121 140.612 100.257 1.00 75.37  ? 402  THR   A O   1 
ATOM   4812  C  CB  . THR   B 2 402  ? 125.477 139.947 98.552  1.00 65.66  ? 402  THR   A CB  1 
ATOM   4813  O  OG1 . THR   B 2 402  ? 125.608 141.235 99.167  1.00 71.93  ? 402  THR   A OG1 1 
ATOM   4814  C  CG2 . THR   B 2 402  ? 126.296 139.913 97.273  1.00 67.57  ? 402  THR   A CG2 1 
ATOM   4815  N  N   . PRO   B 2 403  ? 122.616 138.468 99.878  1.00 62.12  ? 403  PRO   A N   1 
ATOM   4816  C  CA  . PRO   B 2 403  ? 121.808 138.379 101.095 1.00 64.94  ? 403  PRO   A CA  1 
ATOM   4817  C  C   . PRO   B 2 403  ? 122.676 138.188 102.331 1.00 65.61  ? 403  PRO   A C   1 
ATOM   4818  O  O   . PRO   B 2 403  ? 123.877 137.930 102.256 1.00 68.11  ? 403  PRO   A O   1 
ATOM   4819  C  CB  . PRO   B 2 403  ? 120.934 137.151 100.837 1.00 61.68  ? 403  PRO   A CB  1 
ATOM   4820  C  CG  . PRO   B 2 403  ? 121.790 136.283 99.987  1.00 62.50  ? 403  PRO   A CG  1 
ATOM   4821  C  CD  . PRO   B 2 403  ? 122.597 137.210 99.112  1.00 64.01  ? 403  PRO   A CD  1 
ATOM   4822  N  N   . SER   B 2 404  ? 122.034 138.322 103.487 1.00 61.52  ? 404  SER   A N   1 
ATOM   4823  C  CA  . SER   B 2 404  ? 122.669 138.072 104.779 1.00 60.18  ? 404  SER   A CA  1 
ATOM   4824  C  C   . SER   B 2 404  ? 122.060 136.791 105.336 1.00 62.41  ? 404  SER   A C   1 
ATOM   4825  O  O   . SER   B 2 404  ? 121.088 136.817 106.090 1.00 69.78  ? 404  SER   A O   1 
ATOM   4826  C  CB  . SER   B 2 404  ? 122.477 139.254 105.721 1.00 67.41  ? 404  SER   A CB  1 
ATOM   4827  O  OG  . SER   B 2 404  ? 123.057 140.429 105.184 1.00 72.70  ? 404  SER   A OG  1 
ATOM   4828  N  N   . LYS   B 2 405  ? 122.644 135.659 104.956 1.00 53.58  ? 405  LYS   A N   1 
ATOM   4829  C  CA  . LYS   B 2 405  ? 122.099 134.363 105.327 1.00 53.28  ? 405  LYS   A CA  1 
ATOM   4830  C  C   . LYS   B 2 405  ? 122.458 134.011 106.763 1.00 54.76  ? 405  LYS   A C   1 
ATOM   4831  O  O   . LYS   B 2 405  ? 123.545 134.335 107.248 1.00 59.67  ? 405  LYS   A O   1 
ATOM   4832  C  CB  . LYS   B 2 405  ? 122.615 133.278 104.383 1.00 55.63  ? 405  LYS   A CB  1 
ATOM   4833  C  CG  . LYS   B 2 405  ? 122.158 133.429 102.946 1.00 57.03  ? 405  LYS   A CG  1 
ATOM   4834  C  CD  . LYS   B 2 405  ? 122.662 132.281 102.098 1.00 50.33  ? 405  LYS   A CD  1 
ATOM   4835  C  CE  . LYS   B 2 405  ? 122.322 132.479 100.637 1.00 47.18  ? 405  LYS   A CE  1 
ATOM   4836  N  NZ  . LYS   B 2 405  ? 122.842 131.360 99.807  1.00 48.39  ? 405  LYS   A NZ  1 
ATOM   4837  N  N   . ARG   B 2 406  ? 121.532 133.338 107.441 1.00 58.29  ? 406  ARG   A N   1 
ATOM   4838  C  CA  . ARG   B 2 406  ? 121.741 132.840 108.790 1.00 59.52  ? 406  ARG   A CA  1 
ATOM   4839  C  C   . ARG   B 2 406  ? 121.332 131.378 108.847 1.00 60.51  ? 406  ARG   A C   1 
ATOM   4840  O  O   . ARG   B 2 406  ? 120.417 130.953 108.135 1.00 62.87  ? 406  ARG   A O   1 
ATOM   4841  C  CB  . ARG   B 2 406  ? 120.948 133.653 109.820 1.00 59.17  ? 406  ARG   A CB  1 
ATOM   4842  C  CG  . ARG   B 2 406  ? 121.434 135.081 109.980 1.00 61.32  ? 406  ARG   A CG  1 
ATOM   4843  C  CD  . ARG   B 2 406  ? 120.714 135.806 111.105 1.00 64.95  ? 406  ARG   A CD  1 
ATOM   4844  N  NE  . ARG   B 2 406  ? 119.285 135.946 110.853 1.00 67.71  ? 406  ARG   A NE  1 
ATOM   4845  C  CZ  . ARG   B 2 406  ? 118.342 135.251 111.473 1.00 66.83  ? 406  ARG   A CZ  1 
ATOM   4846  N  NH1 . ARG   B 2 406  ? 118.639 134.357 112.401 1.00 64.06  ? 406  ARG   A NH1 1 
ATOM   4847  N  NH2 . ARG   B 2 406  ? 117.067 135.462 111.158 1.00 64.59  ? 406  ARG   A NH2 1 
ATOM   4848  N  N   . SER   B 2 407  ? 122.013 130.613 109.693 1.00 57.41  ? 407  SER   A N   1 
ATOM   4849  C  CA  . SER   B 2 407  ? 121.736 129.190 109.803 1.00 55.59  ? 407  SER   A CA  1 
ATOM   4850  C  C   . SER   B 2 407  ? 120.383 128.950 110.461 1.00 59.22  ? 407  SER   A C   1 
ATOM   4851  O  O   . SER   B 2 407  ? 119.863 129.796 111.194 1.00 64.72  ? 407  SER   A O   1 
ATOM   4852  C  CB  . SER   B 2 407  ? 122.835 128.494 110.602 1.00 57.39  ? 407  SER   A CB  1 
ATOM   4853  O  OG  . SER   B 2 407  ? 122.943 129.042 111.903 1.00 64.93  ? 407  SER   A OG  1 
ATOM   4854  N  N   . LYS   B 2 408  ? 119.809 127.778 110.184 1.00 52.71  ? 408  LYS   A N   1 
ATOM   4855  C  CA  . LYS   B 2 408  ? 118.548 127.407 110.816 1.00 52.91  ? 408  LYS   A CA  1 
ATOM   4856  C  C   . LYS   B 2 408  ? 118.708 127.242 112.320 1.00 57.39  ? 408  LYS   A C   1 
ATOM   4857  O  O   . LYS   B 2 408  ? 117.746 127.432 113.073 1.00 63.24  ? 408  LYS   A O   1 
ATOM   4858  C  CB  . LYS   B 2 408  ? 118.009 126.120 110.193 1.00 46.64  ? 408  LYS   A CB  1 
ATOM   4859  C  CG  . LYS   B 2 408  ? 116.653 125.685 110.715 1.00 50.44  ? 408  LYS   A CG  1 
ATOM   4860  C  CD  . LYS   B 2 408  ? 116.228 124.367 110.103 1.00 53.23  ? 408  LYS   A CD  1 
ATOM   4861  C  CE  . LYS   B 2 408  ? 114.854 123.951 110.579 1.00 58.02  ? 408  LYS   A CE  1 
ATOM   4862  N  NZ  . LYS   B 2 408  ? 114.441 122.649 109.990 1.00 57.29  ? 408  LYS   A NZ  1 
ATOM   4863  N  N   . VAL   B 2 409  ? 119.913 126.898 112.773 1.00 56.50  ? 409  VAL   A N   1 
ATOM   4864  C  CA  . VAL   B 2 409  ? 120.149 126.721 114.200 1.00 54.11  ? 409  VAL   A CA  1 
ATOM   4865  C  C   . VAL   B 2 409  ? 119.982 128.041 114.943 1.00 55.50  ? 409  VAL   A C   1 
ATOM   4866  O  O   . VAL   B 2 409  ? 119.431 128.077 116.047 1.00 62.31  ? 409  VAL   A O   1 
ATOM   4867  C  CB  . VAL   B 2 409  ? 121.536 126.097 114.433 1.00 53.13  ? 409  VAL   A CB  1 
ATOM   4868  C  CG1 . VAL   B 2 409  ? 121.817 125.972 115.910 1.00 57.85  ? 409  VAL   A CG1 1 
ATOM   4869  C  CG2 . VAL   B 2 409  ? 121.606 124.735 113.774 1.00 54.62  ? 409  VAL   A CG2 1 
ATOM   4870  N  N   . GLU   B 2 410  ? 120.438 129.149 114.353 1.00 55.82  ? 410  GLU   A N   1 
ATOM   4871  C  CA  . GLU   B 2 410  ? 120.236 130.454 114.981 1.00 60.82  ? 410  GLU   A CA  1 
ATOM   4872  C  C   . GLU   B 2 410  ? 118.761 130.847 114.995 1.00 64.74  ? 410  GLU   A C   1 
ATOM   4873  O  O   . GLU   B 2 410  ? 118.256 131.390 115.993 1.00 69.29  ? 410  GLU   A O   1 
ATOM   4874  C  CB  . GLU   B 2 410  ? 121.070 131.507 114.256 1.00 58.47  ? 410  GLU   A CB  1 
ATOM   4875  C  CG  . GLU   B 2 410  ? 120.931 132.913 114.808 1.00 66.19  ? 410  GLU   A CG  1 
ATOM   4876  C  CD  . GLU   B 2 410  ? 121.808 133.908 114.075 1.00 71.72  ? 410  GLU   A CD  1 
ATOM   4877  O  OE1 . GLU   B 2 410  ? 122.669 133.470 113.283 1.00 72.03  ? 410  GLU   A OE1 1 
ATOM   4878  O  OE2 . GLU   B 2 410  ? 121.634 135.126 114.287 1.00 65.78  ? 410  GLU   A OE2 1 
ATOM   4879  N  N   . LYS   B 2 411  ? 118.056 130.587 113.892 1.00 45.09  ? 411  LYS   A N   1 
ATOM   4880  C  CA  . LYS   B 2 411  ? 116.635 130.899 113.827 1.00 46.49  ? 411  LYS   A CA  1 
ATOM   4881  C  C   . LYS   B 2 411  ? 115.839 130.077 114.830 1.00 51.02  ? 411  LYS   A C   1 
ATOM   4882  O  O   . LYS   B 2 411  ? 114.796 130.530 115.311 1.00 56.30  ? 411  LYS   A O   1 
ATOM   4883  C  CB  . LYS   B 2 411  ? 116.112 130.670 112.411 1.00 53.75  ? 411  LYS   A CB  1 
ATOM   4884  C  CG  . LYS   B 2 411  ? 116.847 131.460 111.343 1.00 55.50  ? 411  LYS   A CG  1 
ATOM   4885  C  CD  . LYS   B 2 411  ? 116.319 131.129 109.958 1.00 55.81  ? 411  LYS   A CD  1 
ATOM   4886  C  CE  . LYS   B 2 411  ? 117.132 131.815 108.876 1.00 55.47  ? 411  LYS   A CE  1 
ATOM   4887  N  NZ  . LYS   B 2 411  ? 117.073 133.297 108.992 1.00 58.08  ? 411  LYS   A NZ  1 
ATOM   4888  N  N   . GLN   B 2 412  ? 116.300 128.866 115.143 1.00 47.66  ? 412  GLN   A N   1 
ATOM   4889  C  CA  . GLN   B 2 412  ? 115.687 128.078 116.203 1.00 47.23  ? 412  GLN   A CA  1 
ATOM   4890  C  C   . GLN   B 2 412  ? 116.161 128.496 117.587 1.00 50.21  ? 412  GLN   A C   1 
ATOM   4891  O  O   . GLN   B 2 412  ? 115.448 128.266 118.570 1.00 54.68  ? 412  GLN   A O   1 
ATOM   4892  C  CB  . GLN   B 2 412  ? 115.973 126.591 115.990 1.00 48.54  ? 412  GLN   A CB  1 
ATOM   4893  C  CG  . GLN   B 2 412  ? 115.232 125.978 114.818 1.00 48.94  ? 412  GLN   A CG  1 
ATOM   4894  C  CD  . GLN   B 2 412  ? 115.601 124.528 114.592 1.00 50.93  ? 412  GLN   A CD  1 
ATOM   4895  O  OE1 . GLN   B 2 412  ? 116.764 124.200 114.365 1.00 56.86  ? 412  GLN   A OE1 1 
ATOM   4896  N  NE2 . GLN   B 2 412  ? 114.609 123.649 114.655 1.00 57.42  ? 412  GLN   A NE2 1 
ATOM   4897  N  N   . MET   B 2 413  ? 117.349 129.092 117.684 1.00 47.43  ? 413  MET   A N   1 
ATOM   4898  C  CA  . MET   B 2 413  ? 117.843 129.577 118.965 1.00 40.38  ? 413  MET   A CA  1 
ATOM   4899  C  C   . MET   B 2 413  ? 117.067 130.794 119.435 1.00 47.63  ? 413  MET   A C   1 
ATOM   4900  O  O   . MET   B 2 413  ? 116.916 131.000 120.644 1.00 59.33  ? 413  MET   A O   1 
ATOM   4901  C  CB  . MET   B 2 413  ? 119.328 129.915 118.859 1.00 46.56  ? 413  MET   A CB  1 
ATOM   4902  C  CG  . MET   B 2 413  ? 120.179 129.386 119.993 1.00 54.70  ? 413  MET   A CG  1 
ATOM   4903  S  SD  . MET   B 2 413  ? 121.841 130.073 119.949 1.00 65.65  ? 413  MET   A SD  1 
ATOM   4904  C  CE  . MET   B 2 413  ? 122.181 130.010 118.193 1.00 56.73  ? 413  MET   A CE  1 
ATOM   4905  N  N   . ASN   B 2 414  ? 116.591 131.615 118.501 1.00 49.99  ? 414  ASN   A N   1 
ATOM   4906  C  CA  . ASN   B 2 414  ? 115.830 132.801 118.897 1.00 47.20  ? 414  ASN   A CA  1 
ATOM   4907  C  C   . ASN   B 2 414  ? 114.620 132.476 119.773 1.00 44.39  ? 414  ASN   A C   1 
ATOM   4908  O  O   . ASN   B 2 414  ? 114.463 133.118 120.828 1.00 49.80  ? 414  ASN   A O   1 
ATOM   4909  C  CB  . ASN   B 2 414  ? 115.423 133.601 117.655 1.00 44.79  ? 414  ASN   A CB  1 
ATOM   4910  C  CG  . ASN   B 2 414  ? 116.494 134.574 117.214 1.00 51.18  ? 414  ASN   A CG  1 
ATOM   4911  O  OD1 . ASN   B 2 414  ? 117.671 134.408 117.533 1.00 55.81  ? 414  ASN   A OD1 1 
ATOM   4912  N  ND2 . ASN   B 2 414  ? 116.090 135.601 116.479 1.00 52.76  ? 414  ASN   A ND2 1 
ATOM   4913  N  N   . PRO   B 2 415  ? 113.743 131.523 119.425 1.00 32.23  ? 415  PRO   A N   1 
ATOM   4914  C  CA  . PRO   B 2 415  ? 112.653 131.178 120.353 1.00 35.98  ? 415  PRO   A CA  1 
ATOM   4915  C  C   . PRO   B 2 415  ? 113.135 130.666 121.697 1.00 41.68  ? 415  PRO   A C   1 
ATOM   4916  O  O   . PRO   B 2 415  ? 112.480 130.916 122.715 1.00 48.97  ? 415  PRO   A O   1 
ATOM   4917  C  CB  . PRO   B 2 415  ? 111.872 130.100 119.590 1.00 37.71  ? 415  PRO   A CB  1 
ATOM   4918  C  CG  . PRO   B 2 415  ? 112.171 130.357 118.174 1.00 37.28  ? 415  PRO   A CG  1 
ATOM   4919  C  CD  . PRO   B 2 415  ? 113.593 130.808 118.146 1.00 38.44  ? 415  PRO   A CD  1 
ATOM   4920  N  N   . GLN   B 2 416  ? 114.255 129.945 121.734 1.00 40.17  ? 416  GLN   A N   1 
ATOM   4921  C  CA  . GLN   B 2 416  ? 114.790 129.479 123.007 1.00 37.39  ? 416  GLN   A CA  1 
ATOM   4922  C  C   . GLN   B 2 416  ? 115.226 130.648 123.882 1.00 41.23  ? 416  GLN   A C   1 
ATOM   4923  O  O   . GLN   B 2 416  ? 114.972 130.657 125.095 1.00 50.92  ? 416  GLN   A O   1 
ATOM   4924  C  CB  . GLN   B 2 416  ? 115.951 128.522 122.756 1.00 40.92  ? 416  GLN   A CB  1 
ATOM   4925  C  CG  . GLN   B 2 416  ? 115.590 127.371 121.837 1.00 47.75  ? 416  GLN   A CG  1 
ATOM   4926  C  CD  . GLN   B 2 416  ? 116.772 126.486 121.520 1.00 54.75  ? 416  GLN   A CD  1 
ATOM   4927  O  OE1 . GLN   B 2 416  ? 117.888 126.736 121.972 1.00 56.54  ? 416  GLN   A OE1 1 
ATOM   4928  N  NE2 . GLN   B 2 416  ? 116.534 125.442 120.737 1.00 51.29  ? 416  GLN   A NE2 1 
ATOM   4929  N  N   . VAL   B 2 417  ? 115.874 131.646 123.282 1.00 34.36  ? 417  VAL   A N   1 
ATOM   4930  C  CA  . VAL   B 2 417  ? 116.248 132.846 124.024 1.00 30.64  ? 417  VAL   A CA  1 
ATOM   4931  C  C   . VAL   B 2 417  ? 115.006 133.578 124.512 1.00 33.87  ? 417  VAL   A C   1 
ATOM   4932  O  O   . VAL   B 2 417  ? 114.983 134.114 125.625 1.00 40.80  ? 417  VAL   A O   1 
ATOM   4933  C  CB  . VAL   B 2 417  ? 117.142 133.750 123.155 1.00 31.43  ? 417  VAL   A CB  1 
ATOM   4934  C  CG1 . VAL   B 2 417  ? 117.400 135.075 123.846 1.00 39.02  ? 417  VAL   A CG1 1 
ATOM   4935  C  CG2 . VAL   B 2 417  ? 118.449 133.049 122.847 1.00 39.27  ? 417  VAL   A CG2 1 
ATOM   4936  N  N   . ILE   B 2 418  ? 113.952 133.607 123.695 1.00 33.15  ? 418  ILE   A N   1 
ATOM   4937  C  CA  . ILE   B 2 418  ? 112.715 134.260 124.120 1.00 31.72  ? 418  ILE   A CA  1 
ATOM   4938  C  C   . ILE   B 2 418  ? 112.097 133.523 125.305 1.00 35.43  ? 418  ILE   A C   1 
ATOM   4939  O  O   . ILE   B 2 418  ? 111.596 134.145 126.249 1.00 48.82  ? 418  ILE   A O   1 
ATOM   4940  C  CB  . ILE   B 2 418  ? 111.734 134.371 122.938 1.00 36.78  ? 418  ILE   A CB  1 
ATOM   4941  C  CG1 . ILE   B 2 418  ? 112.305 135.296 121.863 1.00 40.61  ? 418  ILE   A CG1 1 
ATOM   4942  C  CG2 . ILE   B 2 418  ? 110.387 134.887 123.405 1.00 36.29  ? 418  ILE   A CG2 1 
ATOM   4943  C  CD1 . ILE   B 2 418  ? 111.376 135.517 120.692 1.00 38.24  ? 418  ILE   A CD1 1 
ATOM   4944  N  N   . ILE   B 2 419  ? 112.122 132.190 125.274 1.00 33.64  ? 419  ILE   A N   1 
ATOM   4945  C  CA  . ILE   B 2 419  ? 111.595 131.403 126.388 1.00 27.19  ? 419  ILE   A CA  1 
ATOM   4946  C  C   . ILE   B 2 419  ? 112.394 131.670 127.656 1.00 36.35  ? 419  ILE   A C   1 
ATOM   4947  O  O   . ILE   B 2 419  ? 111.829 131.828 128.747 1.00 45.61  ? 419  ILE   A O   1 
ATOM   4948  C  CB  . ILE   B 2 419  ? 111.586 129.905 126.027 1.00 30.38  ? 419  ILE   A CB  1 
ATOM   4949  C  CG1 . ILE   B 2 419  ? 110.531 129.618 124.959 1.00 33.82  ? 419  ILE   A CG1 1 
ATOM   4950  C  CG2 . ILE   B 2 419  ? 111.331 129.061 127.257 1.00 36.52  ? 419  ILE   A CG2 1 
ATOM   4951  C  CD1 . ILE   B 2 419  ? 110.462 128.169 124.541 1.00 36.74  ? 419  ILE   A CD1 1 
ATOM   4952  N  N   . ASN   B 2 420  ? 113.722 131.723 127.535 1.00 39.56  ? 420  ASN   A N   1 
ATOM   4953  C  CA  . ASN   B 2 420  ? 114.555 132.024 128.696 1.00 29.36  ? 420  ASN   A CA  1 
ATOM   4954  C  C   . ASN   B 2 420  ? 114.270 133.420 129.237 1.00 40.76  ? 420  ASN   A C   1 
ATOM   4955  O  O   . ASN   B 2 420  ? 114.235 133.625 130.455 1.00 53.73  ? 420  ASN   A O   1 
ATOM   4956  C  CB  . ASN   B 2 420  ? 116.031 131.875 128.339 1.00 33.97  ? 420  ASN   A CB  1 
ATOM   4957  C  CG  . ASN   B 2 420  ? 116.485 130.433 128.338 1.00 46.40  ? 420  ASN   A CG  1 
ATOM   4958  O  OD1 . ASN   B 2 420  ? 115.669 129.515 128.334 1.00 47.76  ? 420  ASN   A OD1 1 
ATOM   4959  N  ND2 . ASN   B 2 420  ? 117.794 130.225 128.342 1.00 50.44  ? 420  ASN   A ND2 1 
ATOM   4960  N  N   . LEU   B 2 421  ? 114.065 134.395 128.349 1.00 36.50  ? 421  LEU   A N   1 
ATOM   4961  C  CA  . LEU   B 2 421  ? 113.741 135.745 128.798 1.00 25.94  ? 421  LEU   A CA  1 
ATOM   4962  C  C   . LEU   B 2 421  ? 112.386 135.790 129.491 1.00 30.00  ? 421  LEU   A C   1 
ATOM   4963  O  O   . LEU   B 2 421  ? 112.206 136.532 130.461 1.00 45.76  ? 421  LEU   A O   1 
ATOM   4964  C  CB  . LEU   B 2 421  ? 113.782 136.721 127.623 1.00 32.57  ? 421  LEU   A CB  1 
ATOM   4965  C  CG  . LEU   B 2 421  ? 115.168 137.026 127.056 1.00 31.42  ? 421  LEU   A CG  1 
ATOM   4966  C  CD1 . LEU   B 2 421  ? 115.091 138.093 125.984 1.00 34.23  ? 421  LEU   A CD1 1 
ATOM   4967  C  CD2 . LEU   B 2 421  ? 116.114 137.449 128.158 1.00 30.61  ? 421  LEU   A CD2 1 
ATOM   4968  N  N   . VAL   B 2 422  ? 111.419 135.009 129.009 1.00 23.60  ? 422  VAL   A N   1 
ATOM   4969  C  CA  . VAL   B 2 422  ? 110.119 134.946 129.672 1.00 23.46  ? 422  VAL   A CA  1 
ATOM   4970  C  C   . VAL   B 2 422  ? 110.254 134.332 131.060 1.00 33.27  ? 422  VAL   A C   1 
ATOM   4971  O  O   . VAL   B 2 422  ? 109.636 134.799 132.025 1.00 42.82  ? 422  VAL   A O   1 
ATOM   4972  C  CB  . VAL   B 2 422  ? 109.111 134.173 128.803 1.00 31.05  ? 422  VAL   A CB  1 
ATOM   4973  C  CG1 . VAL   B 2 422  ? 107.847 133.883 129.586 1.00 35.96  ? 422  VAL   A CG1 1 
ATOM   4974  C  CG2 . VAL   B 2 422  ? 108.778 134.965 127.555 1.00 36.01  ? 422  VAL   A CG2 1 
ATOM   4975  N  N   . ILE   B 2 423  ? 111.061 133.275 131.183 1.00 35.58  ? 423  ILE   A N   1 
ATOM   4976  C  CA  . ILE   B 2 423  ? 111.303 132.672 132.493 1.00 31.84  ? 423  ILE   A CA  1 
ATOM   4977  C  C   . ILE   B 2 423  ? 111.954 133.682 133.430 1.00 35.08  ? 423  ILE   A C   1 
ATOM   4978  O  O   . ILE   B 2 423  ? 111.582 133.795 134.606 1.00 50.00  ? 423  ILE   A O   1 
ATOM   4979  C  CB  . ILE   B 2 423  ? 112.158 131.400 132.346 1.00 36.79  ? 423  ILE   A CB  1 
ATOM   4980  C  CG1 . ILE   B 2 423  ? 111.377 130.313 131.607 1.00 41.26  ? 423  ILE   A CG1 1 
ATOM   4981  C  CG2 . ILE   B 2 423  ? 112.616 130.899 133.703 1.00 39.23  ? 423  ILE   A CG2 1 
ATOM   4982  C  CD1 . ILE   B 2 423  ? 112.161 129.042 131.387 1.00 45.29  ? 423  ILE   A CD1 1 
ATOM   4983  N  N   . LEU   B 2 424  ? 112.932 134.432 132.921 1.00 29.71  ? 424  LEU   A N   1 
ATOM   4984  C  CA  . LEU   B 2 424  ? 113.594 135.451 133.728 1.00 24.98  ? 424  LEU   A CA  1 
ATOM   4985  C  C   . LEU   B 2 424  ? 112.619 136.540 134.154 1.00 31.17  ? 424  LEU   A C   1 
ATOM   4986  O  O   . LEU   B 2 424  ? 112.667 137.015 135.293 1.00 38.81  ? 424  LEU   A O   1 
ATOM   4987  C  CB  . LEU   B 2 424  ? 114.765 136.043 132.947 1.00 27.76  ? 424  LEU   A CB  1 
ATOM   4988  C  CG  . LEU   B 2 424  ? 115.517 137.238 133.527 1.00 36.70  ? 424  LEU   A CG  1 
ATOM   4989  C  CD1 . LEU   B 2 424  ? 115.925 136.975 134.958 1.00 35.10  ? 424  LEU   A CD1 1 
ATOM   4990  C  CD2 . LEU   B 2 424  ? 116.734 137.537 132.680 1.00 40.22  ? 424  LEU   A CD2 1 
ATOM   4991  N  N   . ALA   B 2 425  ? 111.728 136.951 133.252 1.00 35.32  ? 425  ALA   A N   1 
ATOM   4992  C  CA  . ALA   B 2 425  ? 110.736 137.962 133.595 1.00 28.01  ? 425  ALA   A CA  1 
ATOM   4993  C  C   . ALA   B 2 425  ? 109.780 137.457 134.667 1.00 35.58  ? 425  ALA   A C   1 
ATOM   4994  O  O   . ALA   B 2 425  ? 109.402 138.207 135.573 1.00 48.02  ? 425  ALA   A O   1 
ATOM   4995  C  CB  . ALA   B 2 425  ? 109.967 138.387 132.347 1.00 35.19  ? 425  ALA   A CB  1 
ATOM   4996  N  N   . ALA   B 2 426  ? 109.367 136.191 134.574 1.00 33.99  ? 426  ALA   A N   1 
ATOM   4997  C  CA  . ALA   B 2 426  ? 108.501 135.622 135.604 1.00 28.03  ? 426  ALA   A CA  1 
ATOM   4998  C  C   . ALA   B 2 426  ? 109.209 135.573 136.952 1.00 36.86  ? 426  ALA   A C   1 
ATOM   4999  O  O   . ALA   B 2 426  ? 108.615 135.901 137.989 1.00 49.15  ? 426  ALA   A O   1 
ATOM   5000  C  CB  . ALA   B 2 426  ? 108.037 134.228 135.188 1.00 31.16  ? 426  ALA   A CB  1 
ATOM   5001  N  N   . ILE   B 2 427  ? 110.483 135.170 136.955 1.00 36.37  ? 427  ILE   A N   1 
ATOM   5002  C  CA  . ILE   B 2 427  ? 111.266 135.175 138.188 1.00 32.70  ? 427  ILE   A CA  1 
ATOM   5003  C  C   . ILE   B 2 427  ? 111.340 136.580 138.765 1.00 41.99  ? 427  ILE   A C   1 
ATOM   5004  O  O   . ILE   B 2 427  ? 111.173 136.782 139.973 1.00 49.87  ? 427  ILE   A O   1 
ATOM   5005  C  CB  . ILE   B 2 427  ? 112.673 134.602 137.933 1.00 35.78  ? 427  ILE   A CB  1 
ATOM   5006  C  CG1 . ILE   B 2 427  ? 112.598 133.119 137.572 1.00 41.58  ? 427  ILE   A CG1 1 
ATOM   5007  C  CG2 . ILE   B 2 427  ? 113.562 134.812 139.143 1.00 43.71  ? 427  ILE   A CG2 1 
ATOM   5008  C  CD1 . ILE   B 2 427  ? 113.948 132.492 137.319 1.00 40.42  ? 427  ILE   A CD1 1 
ATOM   5009  N  N   . ALA   B 2 428  ? 111.590 137.574 137.909 1.00 35.79  ? 428  ALA   A N   1 
ATOM   5010  C  CA  . ALA   B 2 428  ? 111.689 138.953 138.371 1.00 33.29  ? 428  ALA   A CA  1 
ATOM   5011  C  C   . ALA   B 2 428  ? 110.369 139.446 138.949 1.00 34.18  ? 428  ALA   A C   1 
ATOM   5012  O  O   . ALA   B 2 428  ? 110.354 140.142 139.968 1.00 45.34  ? 428  ALA   A O   1 
ATOM   5013  C  CB  . ALA   B 2 428  ? 112.144 139.856 137.227 1.00 40.83  ? 428  ALA   A CB  1 
ATOM   5014  N  N   . VAL   B 2 429  ? 109.251 139.103 138.308 1.00 35.13  ? 429  VAL   A N   1 
ATOM   5015  C  CA  . VAL   B 2 429  ? 107.944 139.541 138.798 1.00 34.24  ? 429  VAL   A CA  1 
ATOM   5016  C  C   . VAL   B 2 429  ? 107.652 138.924 140.160 1.00 34.93  ? 429  VAL   A C   1 
ATOM   5017  O  O   . VAL   B 2 429  ? 107.200 139.608 141.090 1.00 48.70  ? 429  VAL   A O   1 
ATOM   5018  C  CB  . VAL   B 2 429  ? 106.846 139.203 137.775 1.00 36.29  ? 429  VAL   A CB  1 
ATOM   5019  C  CG1 . VAL   B 2 429  ? 105.475 139.386 138.391 1.00 36.23  ? 429  VAL   A CG1 1 
ATOM   5020  C  CG2 . VAL   B 2 429  ? 106.987 140.078 136.544 1.00 40.88  ? 429  VAL   A CG2 1 
ATOM   5021  N  N   . VAL   B 2 430  ? 107.911 137.622 140.301 1.00 30.57  ? 430  VAL   A N   1 
ATOM   5022  C  CA  . VAL   B 2 430  ? 107.680 136.959 141.583 1.00 32.97  ? 430  VAL   A CA  1 
ATOM   5023  C  C   . VAL   B 2 430  ? 108.572 137.561 142.661 1.00 41.35  ? 430  VAL   A C   1 
ATOM   5024  O  O   . VAL   B 2 430  ? 108.119 137.837 143.782 1.00 52.71  ? 430  VAL   A O   1 
ATOM   5025  C  CB  . VAL   B 2 430  ? 107.896 135.442 141.448 1.00 34.21  ? 430  VAL   A CB  1 
ATOM   5026  C  CG1 . VAL   B 2 430  ? 107.825 134.774 142.807 1.00 36.48  ? 430  VAL   A CG1 1 
ATOM   5027  C  CG2 . VAL   B 2 430  ? 106.862 134.846 140.510 1.00 37.11  ? 430  VAL   A CG2 1 
ATOM   5028  N  N   . CYS   B 2 431  ? 109.849 137.784 142.338 1.00 38.19  ? 431  CYS   A N   1 
ATOM   5029  C  CA  . CYS   B 2 431  ? 110.766 138.381 143.300 1.00 32.80  ? 431  CYS   A CA  1 
ATOM   5030  C  C   . CYS   B 2 431  ? 110.298 139.765 143.719 1.00 34.68  ? 431  CYS   A C   1 
ATOM   5031  O  O   . CYS   B 2 431  ? 110.302 140.090 144.908 1.00 51.61  ? 431  CYS   A O   1 
ATOM   5032  C  CB  . CYS   B 2 431  ? 112.177 138.454 142.716 1.00 35.75  ? 431  CYS   A CB  1 
ATOM   5033  S  SG  . CYS   B 2 431  ? 113.029 136.871 142.571 1.00 59.64  ? 431  CYS   A SG  1 
ATOM   5034  N  N   . ALA   B 2 432  ? 109.878 140.588 142.758 1.00 30.88  ? 432  ALA   A N   1 
ATOM   5035  C  CA  . ALA   B 2 432  ? 109.440 141.941 143.078 1.00 26.02  ? 432  ALA   A CA  1 
ATOM   5036  C  C   . ALA   B 2 432  ? 108.214 141.924 143.978 1.00 29.18  ? 432  ALA   A C   1 
ATOM   5037  O  O   . ALA   B 2 432  ? 108.161 142.643 144.981 1.00 45.42  ? 432  ALA   A O   1 
ATOM   5038  C  CB  . ALA   B 2 432  ? 109.157 142.715 141.793 1.00 32.35  ? 432  ALA   A CB  1 
ATOM   5039  N  N   . ILE   B 2 433  ? 107.227 141.086 143.654 1.00 24.31  ? 433  ILE   A N   1 
ATOM   5040  C  CA  . ILE   B 2 433  ? 106.001 141.054 144.451 1.00 24.78  ? 433  ILE   A CA  1 
ATOM   5041  C  C   . ILE   B 2 433  ? 106.299 140.589 145.872 1.00 35.35  ? 433  ILE   A C   1 
ATOM   5042  O  O   . ILE   B 2 433  ? 105.897 141.233 146.855 1.00 49.30  ? 433  ILE   A O   1 
ATOM   5043  C  CB  . ILE   B 2 433  ? 104.944 140.162 143.775 1.00 31.67  ? 433  ILE   A CB  1 
ATOM   5044  C  CG1 . ILE   B 2 433  ? 104.440 140.810 142.485 1.00 39.92  ? 433  ILE   A CG1 1 
ATOM   5045  C  CG2 . ILE   B 2 433  ? 103.788 139.898 144.722 1.00 35.81  ? 433  ILE   A CG2 1 
ATOM   5046  C  CD1 . ILE   B 2 433  ? 103.417 139.981 141.747 1.00 37.32  ? 433  ILE   A CD1 1 
ATOM   5047  N  N   . VAL   B 2 434  ? 107.015 139.469 146.005 1.00 35.14  ? 434  VAL   A N   1 
ATOM   5048  C  CA  . VAL   B 2 434  ? 107.267 138.920 147.333 1.00 31.67  ? 434  VAL   A CA  1 
ATOM   5049  C  C   . VAL   B 2 434  ? 108.156 139.854 148.141 1.00 37.26  ? 434  VAL   A C   1 
ATOM   5050  O  O   . VAL   B 2 434  ? 107.926 140.066 149.338 1.00 51.44  ? 434  VAL   A O   1 
ATOM   5051  C  CB  . VAL   B 2 434  ? 107.868 137.508 147.228 1.00 32.41  ? 434  VAL   A CB  1 
ATOM   5052  C  CG1 . VAL   B 2 434  ? 108.164 136.962 148.609 1.00 38.47  ? 434  VAL   A CG1 1 
ATOM   5053  C  CG2 . VAL   B 2 434  ? 106.914 136.588 146.494 1.00 32.86  ? 434  VAL   A CG2 1 
ATOM   5054  N  N   . ASP   B 2 435  ? 109.179 140.433 147.508 1.00 35.24  ? 435  ASP   A N   1 
ATOM   5055  C  CA  . ASP   B 2 435  ? 110.061 141.352 148.212 1.00 36.03  ? 435  ASP   A CA  1 
ATOM   5056  C  C   . ASP   B 2 435  ? 109.316 142.600 148.655 1.00 40.05  ? 435  ASP   A C   1 
ATOM   5057  O  O   . ASP   B 2 435  ? 109.547 143.101 149.757 1.00 49.51  ? 435  ASP   A O   1 
ATOM   5058  C  CB  . ASP   B 2 435  ? 111.248 141.720 147.326 1.00 41.71  ? 435  ASP   A CB  1 
ATOM   5059  C  CG  . ASP   B 2 435  ? 112.185 142.704 147.990 1.00 55.87  ? 435  ASP   A CG  1 
ATOM   5060  O  OD1 . ASP   B 2 435  ? 112.825 142.332 148.996 1.00 56.37  ? 435  ASP   A OD1 1 
ATOM   5061  O  OD2 . ASP   B 2 435  ? 112.284 143.851 147.507 1.00 56.09  ? 435  ASP   A OD2 1 
ATOM   5062  N  N   . HIS   B 2 436  ? 108.416 143.118 147.818 1.00 36.90  ? 436  HIS   A N   1 
ATOM   5063  C  CA  . HIS   B 2 436  ? 107.642 144.287 148.213 1.00 31.62  ? 436  HIS   A CA  1 
ATOM   5064  C  C   . HIS   B 2 436  ? 106.749 143.983 149.407 1.00 43.73  ? 436  HIS   A C   1 
ATOM   5065  O  O   . HIS   B 2 436  ? 106.683 144.773 150.358 1.00 52.12  ? 436  HIS   A O   1 
ATOM   5066  C  CB  . HIS   B 2 436  ? 106.808 144.784 147.035 1.00 29.95  ? 436  HIS   A CB  1 
ATOM   5067  C  CG  . HIS   B 2 436  ? 105.716 145.726 147.427 1.00 27.29  ? 436  HIS   A CG  1 
ATOM   5068  N  ND1 . HIS   B 2 436  ? 105.937 147.063 147.666 1.00 34.55  ? 436  HIS   A ND1 1 
ATOM   5069  C  CD2 . HIS   B 2 436  ? 104.395 145.520 147.632 1.00 33.17  ? 436  HIS   A CD2 1 
ATOM   5070  C  CE1 . HIS   B 2 436  ? 104.798 147.642 147.998 1.00 31.83  ? 436  HIS   A CE1 1 
ATOM   5071  N  NE2 . HIS   B 2 436  ? 103.846 146.727 147.986 1.00 38.23  ? 436  HIS   A NE2 1 
ATOM   5072  N  N   . VAL   B 2 437  ? 106.056 142.842 149.383 1.00 34.94  ? 437  VAL   A N   1 
ATOM   5073  C  CA  . VAL   B 2 437  ? 105.183 142.494 150.504 1.00 27.16  ? 437  VAL   A CA  1 
ATOM   5074  C  C   . VAL   B 2 437  ? 106.002 142.319 151.778 1.00 37.29  ? 437  VAL   A C   1 
ATOM   5075  O  O   . VAL   B 2 437  ? 105.655 142.846 152.846 1.00 50.03  ? 437  VAL   A O   1 
ATOM   5076  C  CB  . VAL   B 2 437  ? 104.367 141.233 150.177 1.00 28.04  ? 437  VAL   A CB  1 
ATOM   5077  C  CG1 . VAL   B 2 437  ? 103.567 140.798 151.387 1.00 38.22  ? 437  VAL   A CG1 1 
ATOM   5078  C  CG2 . VAL   B 2 437  ? 103.449 141.496 149.002 1.00 34.22  ? 437  VAL   A CG2 1 
ATOM   5079  N  N   . ASN   B 2 438  ? 107.121 141.597 151.674 1.00 30.85  ? 438  ASN   A N   1 
ATOM   5080  C  CA  . ASN   B 2 438  ? 107.971 141.369 152.835 1.00 28.15  ? 438  ASN   A CA  1 
ATOM   5081  C  C   . ASN   B 2 438  ? 108.540 142.673 153.372 1.00 41.83  ? 438  ASN   A C   1 
ATOM   5082  O  O   . ASN   B 2 438  ? 108.635 142.858 154.588 1.00 52.76  ? 438  ASN   A O   1 
ATOM   5083  C  CB  . ASN   B 2 438  ? 109.100 140.403 152.479 1.00 37.18  ? 438  ASN   A CB  1 
ATOM   5084  C  CG  . ASN   B 2 438  ? 108.612 138.989 152.271 1.00 44.04  ? 438  ASN   A CG  1 
ATOM   5085  O  OD1 . ASN   B 2 438  ? 107.571 138.594 152.794 1.00 50.60  ? 438  ASN   A OD1 1 
ATOM   5086  N  ND2 . ASN   B 2 438  ? 109.367 138.212 151.507 1.00 42.18  ? 438  ASN   A ND2 1 
ATOM   5087  N  N   . GLU   B 2 439  ? 108.935 143.588 152.484 1.00 47.47  ? 439  GLU   A N   1 
ATOM   5088  C  CA  . GLU   B 2 439  ? 109.531 144.840 152.932 1.00 37.78  ? 439  GLU   A CA  1 
ATOM   5089  C  C   . GLU   B 2 439  ? 108.495 145.751 153.570 1.00 40.38  ? 439  GLU   A C   1 
ATOM   5090  O  O   . GLU   B 2 439  ? 108.798 146.451 154.539 1.00 51.85  ? 439  GLU   A O   1 
ATOM   5091  C  CB  . GLU   B 2 439  ? 110.228 145.543 151.771 1.00 41.10  ? 439  GLU   A CB  1 
ATOM   5092  C  CG  . GLU   B 2 439  ? 111.535 144.893 151.363 1.00 46.07  ? 439  GLU   A CG  1 
ATOM   5093  C  CD  . GLU   B 2 439  ? 112.422 145.823 150.566 1.00 54.11  ? 439  GLU   A CD  1 
ATOM   5094  O  OE1 . GLU   B 2 439  ? 112.271 147.052 150.711 1.00 57.88  ? 439  GLU   A OE1 1 
ATOM   5095  O  OE2 . GLU   B 2 439  ? 113.270 145.326 149.796 1.00 51.96  ? 439  GLU   A OE2 1 
ATOM   5096  N  N   . VAL   B 2 440  ? 107.267 145.757 153.052 1.00 33.41  ? 440  VAL   A N   1 
ATOM   5097  C  CA  . VAL   B 2 440  ? 106.213 146.521 153.712 1.00 36.06  ? 440  VAL   A CA  1 
ATOM   5098  C  C   . VAL   B 2 440  ? 105.966 145.972 155.109 1.00 46.56  ? 440  VAL   A C   1 
ATOM   5099  O  O   . VAL   B 2 440  ? 105.856 146.731 156.083 1.00 55.15  ? 440  VAL   A O   1 
ATOM   5100  C  CB  . VAL   B 2 440  ? 104.930 146.519 152.863 1.00 36.64  ? 440  VAL   A CB  1 
ATOM   5101  C  CG1 . VAL   B 2 440  ? 103.776 147.097 153.656 1.00 43.24  ? 440  VAL   A CG1 1 
ATOM   5102  C  CG2 . VAL   B 2 440  ? 105.143 147.316 151.593 1.00 45.25  ? 440  VAL   A CG2 1 
ATOM   5103  N  N   . GLU   B 2 441  ? 105.896 144.643 155.236 1.00 53.31  ? 441  GLU   A N   1 
ATOM   5104  C  CA  . GLU   B 2 441  ? 105.682 144.047 156.553 1.00 48.53  ? 441  GLU   A CA  1 
ATOM   5105  C  C   . GLU   B 2 441  ? 106.840 144.349 157.499 1.00 51.39  ? 441  GLU   A C   1 
ATOM   5106  O  O   . GLU   B 2 441  ? 106.623 144.691 158.666 1.00 56.28  ? 441  GLU   A O   1 
ATOM   5107  C  CB  . GLU   B 2 441  ? 105.474 142.541 156.419 1.00 46.43  ? 441  GLU   A CB  1 
ATOM   5108  C  CG  . GLU   B 2 441  ? 105.060 141.857 157.707 1.00 51.40  ? 441  GLU   A CG  1 
ATOM   5109  C  CD  . GLU   B 2 441  ? 103.657 142.230 158.142 1.00 63.44  ? 441  GLU   A CD  1 
ATOM   5110  O  OE1 . GLU   B 2 441  ? 102.859 142.658 157.282 1.00 63.66  ? 441  GLU   A OE1 1 
ATOM   5111  O  OE2 . GLU   B 2 441  ? 103.350 142.094 159.345 1.00 64.50  ? 441  GLU   A OE2 1 
ATOM   5112  N  N   . TRP   B 2 442  ? 108.077 144.241 157.013 1.00 45.56  ? 442  TRP   A N   1 
ATOM   5113  C  CA  . TRP   B 2 442  ? 109.270 144.487 157.812 1.00 36.96  ? 442  TRP   A CA  1 
ATOM   5114  C  C   . TRP   B 2 442  ? 109.536 145.966 158.055 1.00 43.10  ? 442  TRP   A C   1 
ATOM   5115  O  O   . TRP   B 2 442  ? 110.429 146.296 158.839 1.00 57.39  ? 442  TRP   A O   1 
ATOM   5116  C  CB  . TRP   B 2 442  ? 110.490 143.866 157.130 1.00 43.93  ? 442  TRP   A CB  1 
ATOM   5117  C  CG  . TRP   B 2 442  ? 110.533 142.374 157.176 1.00 39.49  ? 442  TRP   A CG  1 
ATOM   5118  C  CD1 . TRP   B 2 442  ? 110.023 141.570 158.146 1.00 42.89  ? 442  TRP   A CD1 1 
ATOM   5119  C  CD2 . TRP   B 2 442  ? 111.124 141.506 156.205 1.00 35.35  ? 442  TRP   A CD2 1 
ATOM   5120  N  NE1 . TRP   B 2 442  ? 110.259 140.254 157.842 1.00 38.56  ? 442  TRP   A NE1 1 
ATOM   5121  C  CE2 . TRP   B 2 442  ? 110.936 140.189 156.654 1.00 35.33  ? 442  TRP   A CE2 1 
ATOM   5122  C  CE3 . TRP   B 2 442  ? 111.796 141.716 154.998 1.00 42.80  ? 442  TRP   A CE3 1 
ATOM   5123  C  CZ2 . TRP   B 2 442  ? 111.390 139.088 155.941 1.00 41.42  ? 442  TRP   A CZ2 1 
ATOM   5124  C  CZ3 . TRP   B 2 442  ? 112.250 140.622 154.295 1.00 42.16  ? 442  TRP   A CZ3 1 
ATOM   5125  C  CH2 . TRP   B 2 442  ? 112.044 139.325 154.766 1.00 43.39  ? 442  TRP   A CH2 1 
ATOM   5126  N  N   . ASP   B 2 443  ? 108.831 146.857 157.365 1.00 48.07  ? 443  ASP   A N   1 
ATOM   5127  C  CA  . ASP   B 2 443  ? 108.905 148.277 157.670 1.00 48.44  ? 443  ASP   A CA  1 
ATOM   5128  C  C   . ASP   B 2 443  ? 107.814 148.707 158.635 1.00 53.25  ? 443  ASP   A C   1 
ATOM   5129  O  O   . ASP   B 2 443  ? 108.018 149.646 159.412 1.00 61.44  ? 443  ASP   A O   1 
ATOM   5130  C  CB  . ASP   B 2 443  ? 108.815 149.097 156.382 1.00 49.97  ? 443  ASP   A CB  1 
ATOM   5131  C  CG  . ASP   B 2 443  ? 109.311 150.514 156.557 1.00 58.64  ? 443  ASP   A CG  1 
ATOM   5132  O  OD1 . ASP   B 2 443  ? 109.898 150.815 157.618 1.00 63.79  ? 443  ASP   A OD1 1 
ATOM   5133  O  OD2 . ASP   B 2 443  ? 109.116 151.330 155.632 1.00 61.49  ? 443  ASP   A OD2 1 
ATOM   5134  N  N   . ARG   B 2 444  ? 106.658 148.039 158.605 1.00 55.75  ? 444  ARG   A N   1 
ATOM   5135  C  CA  . ARG   B 2 444  ? 105.649 148.289 159.628 1.00 57.03  ? 444  ARG   A CA  1 
ATOM   5136  C  C   . ARG   B 2 444  ? 106.179 147.938 161.014 1.00 59.36  ? 444  ARG   A C   1 
ATOM   5137  O  O   . ARG   B 2 444  ? 106.002 148.708 161.966 1.00 64.02  ? 444  ARG   A O   1 
ATOM   5138  C  CB  . ARG   B 2 444  ? 104.381 147.498 159.317 1.00 57.64  ? 444  ARG   A CB  1 
ATOM   5139  C  CG  . ARG   B 2 444  ? 103.277 147.676 160.338 1.00 58.58  ? 444  ARG   A CG  1 
ATOM   5140  C  CD  . ARG   B 2 444  ? 102.104 146.760 160.055 1.00 61.38  ? 444  ARG   A CD  1 
ATOM   5141  N  NE  . ARG   B 2 444  ? 102.478 145.357 160.169 1.00 65.48  ? 444  ARG   A NE  1 
ATOM   5142  C  CZ  . ARG   B 2 444  ? 102.442 144.663 161.298 1.00 69.41  ? 444  ARG   A CZ  1 
ATOM   5143  N  NH1 . ARG   B 2 444  ? 102.054 145.214 162.436 1.00 65.42  ? 444  ARG   A NH1 1 
ATOM   5144  N  NH2 . ARG   B 2 444  ? 102.803 143.383 161.284 1.00 64.84  ? 444  ARG   A NH2 1 
ATOM   5145  N  N   . GLN   B 2 445  ? 106.832 146.781 161.142 1.00 57.83  ? 445  GLN   A N   1 
ATOM   5146  C  CA  . GLN   B 2 445  ? 107.516 146.353 162.361 1.00 53.72  ? 445  GLN   A CA  1 
ATOM   5147  C  C   . GLN   B 2 445  ? 109.010 146.445 162.077 1.00 52.87  ? 445  GLN   A C   1 
ATOM   5148  O  O   . GLN   B 2 445  ? 109.527 145.725 161.217 1.00 62.53  ? 445  GLN   A O   1 
ATOM   5149  C  CB  . GLN   B 2 445  ? 107.100 144.937 162.762 1.00 54.54  ? 445  GLN   A CB  1 
ATOM   5150  C  CG  . GLN   B 2 445  ? 107.141 143.923 161.635 1.00 56.78  ? 445  GLN   A CG  1 
ATOM   5151  C  CD  . GLN   B 2 445  ? 106.375 142.663 161.949 1.00 59.55  ? 445  GLN   A CD  1 
ATOM   5152  O  OE1 . GLN   B 2 445  ? 105.527 142.644 162.837 1.00 64.54  ? 445  GLN   A OE1 1 
ATOM   5153  N  NE2 . GLN   B 2 445  ? 106.668 141.597 161.218 1.00 56.06  ? 445  GLN   A NE2 1 
ATOM   5154  N  N   . GLN   B 2 446  ? 109.701 147.321 162.799 1.00 48.30  ? 446  GLN   A N   1 
ATOM   5155  C  CA  . GLN   B 2 446  ? 111.003 147.779 162.337 1.00 49.46  ? 446  GLN   A CA  1 
ATOM   5156  C  C   . GLN   B 2 446  ? 112.055 146.688 162.480 1.00 51.34  ? 446  GLN   A C   1 
ATOM   5157  O  O   . GLN   B 2 446  ? 112.646 146.530 163.553 1.00 59.08  ? 446  GLN   A O   1 
ATOM   5158  C  CB  . GLN   B 2 446  ? 111.442 149.030 163.108 1.00 54.02  ? 446  GLN   A CB  1 
ATOM   5159  C  CG  . GLN   B 2 446  ? 110.651 150.288 162.801 1.00 52.07  ? 446  GLN   A CG  1 
ATOM   5160  C  CD  . GLN   B 2 446  ? 110.958 150.844 161.434 1.00 55.35  ? 446  GLN   A CD  1 
ATOM   5161  O  OE1 . GLN   B 2 446  ? 111.991 150.530 160.846 1.00 57.43  ? 446  GLN   A OE1 1 
ATOM   5162  N  NE2 . GLN   B 2 446  ? 110.058 151.666 160.912 1.00 53.99  ? 446  GLN   A NE2 1 
ATOM   5163  N  N   . ALA   B 2 447  ? 112.285 145.935 161.412 1.00 44.39  ? 447  ALA   A N   1 
ATOM   5164  C  CA  . ALA   B 2 447  ? 113.347 144.947 161.393 1.00 38.08  ? 447  ALA   A CA  1 
ATOM   5165  C  C   . ALA   B 2 447  ? 114.692 145.627 161.181 1.00 46.34  ? 447  ALA   A C   1 
ATOM   5166  O  O   . ALA   B 2 447  ? 114.776 146.762 160.704 1.00 57.46  ? 447  ALA   A O   1 
ATOM   5167  C  CB  . ALA   B 2 447  ? 113.105 143.907 160.302 1.00 40.24  ? 447  ALA   A CB  1 
ATOM   5168  N  N   . TYR   B 2 448  ? 115.755 144.914 161.544 1.00 40.35  ? 448  TYR   A N   1 
ATOM   5169  C  CA  . TYR   B 2 448  ? 117.096 145.479 161.479 1.00 36.02  ? 448  TYR   A CA  1 
ATOM   5170  C  C   . TYR   B 2 448  ? 117.630 145.576 160.058 1.00 41.99  ? 448  TYR   A C   1 
ATOM   5171  O  O   . TYR   B 2 448  ? 118.537 146.375 159.806 1.00 49.80  ? 448  TYR   A O   1 
ATOM   5172  C  CB  . TYR   B 2 448  ? 118.045 144.656 162.345 1.00 44.99  ? 448  TYR   A CB  1 
ATOM   5173  C  CG  . TYR   B 2 448  ? 117.604 144.562 163.785 1.00 40.90  ? 448  TYR   A CG  1 
ATOM   5174  C  CD1 . TYR   B 2 448  ? 117.971 145.529 164.706 1.00 36.66  ? 448  TYR   A CD1 1 
ATOM   5175  C  CD2 . TYR   B 2 448  ? 116.811 143.512 164.221 1.00 44.20  ? 448  TYR   A CD2 1 
ATOM   5176  C  CE1 . TYR   B 2 448  ? 117.567 145.450 166.018 1.00 40.86  ? 448  TYR   A CE1 1 
ATOM   5177  C  CE2 . TYR   B 2 448  ? 116.402 143.425 165.532 1.00 43.54  ? 448  TYR   A CE2 1 
ATOM   5178  C  CZ  . TYR   B 2 448  ? 116.781 144.396 166.427 1.00 45.29  ? 448  TYR   A CZ  1 
ATOM   5179  O  OH  . TYR   B 2 448  ? 116.373 144.309 167.738 1.00 55.00  ? 448  TYR   A OH  1 
ATOM   5180  N  N   . TRP   B 2 449  ? 117.102 144.783 159.132 1.00 43.58  ? 449  TRP   A N   1 
ATOM   5181  C  CA  . TRP   B 2 449  ? 117.506 144.847 157.736 1.00 42.96  ? 449  TRP   A CA  1 
ATOM   5182  C  C   . TRP   B 2 449  ? 116.640 145.789 156.914 1.00 37.51  ? 449  TRP   A C   1 
ATOM   5183  O  O   . TRP   B 2 449  ? 116.897 145.957 155.718 1.00 46.86  ? 449  TRP   A O   1 
ATOM   5184  C  CB  . TRP   B 2 449  ? 117.493 143.448 157.115 1.00 46.72  ? 449  TRP   A CB  1 
ATOM   5185  C  CG  . TRP   B 2 449  ? 116.230 142.677 157.342 1.00 40.05  ? 449  TRP   A CG  1 
ATOM   5186  C  CD1 . TRP   B 2 449  ? 115.185 142.550 156.482 1.00 37.69  ? 449  TRP   A CD1 1 
ATOM   5187  C  CD2 . TRP   B 2 449  ? 115.889 141.913 158.504 1.00 39.54  ? 449  TRP   A CD2 1 
ATOM   5188  N  NE1 . TRP   B 2 449  ? 114.211 141.761 157.035 1.00 41.07  ? 449  TRP   A NE1 1 
ATOM   5189  C  CE2 . TRP   B 2 449  ? 114.619 141.359 158.278 1.00 34.35  ? 449  TRP   A CE2 1 
ATOM   5190  C  CE3 . TRP   B 2 449  ? 116.532 141.649 159.715 1.00 43.73  ? 449  TRP   A CE3 1 
ATOM   5191  C  CZ2 . TRP   B 2 449  ? 113.981 140.556 159.213 1.00 36.11  ? 449  TRP   A CZ2 1 
ATOM   5192  C  CZ3 . TRP   B 2 449  ? 115.895 140.852 160.642 1.00 42.11  ? 449  TRP   A CZ3 1 
ATOM   5193  C  CH2 . TRP   B 2 449  ? 114.634 140.315 160.387 1.00 39.42  ? 449  TRP   A CH2 1 
ATOM   5194  N  N   . MET   B 2 450  ? 115.627 146.409 157.521 1.00 51.49  ? 450  MET   A N   1 
ATOM   5195  C  CA  . MET   B 2 450  ? 114.761 147.360 156.834 1.00 49.98  ? 450  MET   A CA  1 
ATOM   5196  C  C   . MET   B 2 450  ? 114.761 148.728 157.507 1.00 51.83  ? 450  MET   A C   1 
ATOM   5197  O  O   . MET   B 2 450  ? 113.852 149.530 157.272 1.00 57.82  ? 450  MET   A O   1 
ATOM   5198  C  CB  . MET   B 2 450  ? 113.334 146.820 156.737 1.00 43.52  ? 450  MET   A CB  1 
ATOM   5199  C  CG  . MET   B 2 450  ? 113.124 145.831 155.610 1.00 53.14  ? 450  MET   A CG  1 
ATOM   5200  S  SD  . MET   B 2 450  ? 113.434 146.555 153.992 1.00 72.30  ? 450  MET   A SD  1 
ATOM   5201  C  CE  . MET   B 2 450  ? 112.238 147.885 153.984 1.00 52.97  ? 450  MET   A CE  1 
ATOM   5202  N  N   . LEU   B 2 451  ? 115.755 149.008 158.342 1.00 49.11  ? 451  LEU   A N   1 
ATOM   5203  C  CA  . LEU   B 2 451  ? 115.865 150.321 158.956 1.00 42.03  ? 451  LEU   A CA  1 
ATOM   5204  C  C   . LEU   B 2 451  ? 116.226 151.368 157.911 1.00 51.10  ? 451  LEU   A C   1 
ATOM   5205  O  O   . LEU   B 2 451  ? 116.935 151.092 156.939 1.00 58.51  ? 451  LEU   A O   1 
ATOM   5206  C  CB  . LEU   B 2 451  ? 116.912 150.309 160.068 1.00 46.11  ? 451  LEU   A CB  1 
ATOM   5207  C  CG  . LEU   B 2 451  ? 116.610 149.436 161.286 1.00 44.88  ? 451  LEU   A CG  1 
ATOM   5208  C  CD1 . LEU   B 2 451  ? 117.731 149.531 162.303 1.00 46.85  ? 451  LEU   A CD1 1 
ATOM   5209  C  CD2 . LEU   B 2 451  ? 115.288 149.831 161.912 1.00 51.27  ? 451  LEU   A CD2 1 
ATOM   5210  N  N   . PHE   B 2 452  ? 115.720 152.584 158.121 1.00 55.48  ? 452  PHE   A N   1 
ATOM   5211  C  CA  . PHE   B 2 452  ? 115.958 153.721 157.232 1.00 47.59  ? 452  PHE   A CA  1 
ATOM   5212  C  C   . PHE   B 2 452  ? 115.491 153.414 155.807 1.00 52.31  ? 452  PHE   A C   1 
ATOM   5213  O  O   . PHE   B 2 452  ? 116.273 153.380 154.856 1.00 57.90  ? 452  PHE   A O   1 
ATOM   5214  C  CB  . PHE   B 2 452  ? 117.431 154.136 157.255 1.00 46.65  ? 452  PHE   A CB  1 
ATOM   5215  C  CG  . PHE   B 2 452  ? 117.935 154.503 158.617 1.00 51.47  ? 452  PHE   A CG  1 
ATOM   5216  C  CD1 . PHE   B 2 452  ? 117.740 155.773 159.122 1.00 55.61  ? 452  PHE   A CD1 1 
ATOM   5217  C  CD2 . PHE   B 2 452  ? 118.610 153.579 159.391 1.00 55.26  ? 452  PHE   A CD2 1 
ATOM   5218  C  CE1 . PHE   B 2 452  ? 118.206 156.113 160.375 1.00 56.33  ? 452  PHE   A CE1 1 
ATOM   5219  C  CE2 . PHE   B 2 452  ? 119.078 153.914 160.643 1.00 51.17  ? 452  PHE   A CE2 1 
ATOM   5220  C  CZ  . PHE   B 2 452  ? 118.874 155.182 161.135 1.00 50.97  ? 452  PHE   A CZ  1 
ATOM   5221  N  N   . ALA   B 2 453  ? 114.188 153.191 155.679 1.00 53.34  ? 453  ALA   A N   1 
ATOM   5222  C  CA  . ALA   B 2 453  ? 113.542 152.928 154.401 1.00 53.58  ? 453  ALA   A CA  1 
ATOM   5223  C  C   . ALA   B 2 453  ? 112.484 153.982 154.103 1.00 62.53  ? 453  ALA   A C   1 
ATOM   5224  O  O   . ALA   B 2 453  ? 111.370 153.671 153.679 1.00 65.88  ? 453  ALA   A O   1 
ATOM   5225  C  CB  . ALA   B 2 453  ? 112.929 151.531 154.376 1.00 50.11  ? 453  ALA   A CB  1 
ATOM   5226  N  N   . ASP   B 2 454  ? 112.824 155.250 154.331 1.00 63.54  ? 454  ASP   A N   1 
ATOM   5227  C  CA  . ASP   B 2 454  ? 111.897 156.353 154.135 1.00 57.87  ? 454  ASP   A CA  1 
ATOM   5228  C  C   . ASP   B 2 454  ? 112.331 157.318 153.041 1.00 60.74  ? 454  ASP   A C   1 
ATOM   5229  O  O   . ASP   B 2 454  ? 111.581 158.247 152.723 1.00 64.51  ? 454  ASP   A O   1 
ATOM   5230  C  CB  . ASP   B 2 454  ? 111.705 157.115 155.450 1.00 60.72  ? 454  ASP   A CB  1 
ATOM   5231  C  CG  . ASP   B 2 454  ? 113.019 157.453 156.122 1.00 66.14  ? 454  ASP   A CG  1 
ATOM   5232  O  OD1 . ASP   B 2 454  ? 114.079 157.080 155.579 1.00 67.08  ? 454  ASP   A OD1 1 
ATOM   5233  O  OD2 . ASP   B 2 454  ? 112.992 158.092 157.194 1.00 69.91  ? 454  ASP   A OD2 1 
ATOM   5234  N  N   . THR   B 2 455  ? 113.510 157.129 152.458 1.00 64.20  ? 455  THR   A N   1 
ATOM   5235  C  CA  . THR   B 2 455  ? 113.976 158.010 151.401 1.00 64.95  ? 455  THR   A CA  1 
ATOM   5236  C  C   . THR   B 2 455  ? 113.287 157.670 150.081 1.00 66.10  ? 455  THR   A C   1 
ATOM   5237  O  O   . THR   B 2 455  ? 112.576 156.670 149.954 1.00 69.19  ? 455  THR   A O   1 
ATOM   5238  C  CB  . THR   B 2 455  ? 115.492 157.916 151.247 1.00 67.66  ? 455  THR   A CB  1 
ATOM   5239  O  OG1 . THR   B 2 455  ? 115.852 156.595 150.827 1.00 67.03  ? 455  THR   A OG1 1 
ATOM   5240  C  CG2 . THR   B 2 455  ? 116.179 158.227 152.566 1.00 66.36  ? 455  THR   A CG2 1 
ATOM   5241  N  N   . SER   B 2 456  ? 113.510 158.526 149.083 1.00 61.19  ? 456  SER   A N   1 
ATOM   5242  C  CA  . SER   B 2 456  ? 112.881 158.352 147.781 1.00 58.37  ? 456  SER   A CA  1 
ATOM   5243  C  C   . SER   B 2 456  ? 113.460 157.187 146.989 1.00 56.19  ? 456  SER   A C   1 
ATOM   5244  O  O   . SER   B 2 456  ? 112.885 156.819 145.960 1.00 58.09  ? 456  SER   A O   1 
ATOM   5245  C  CB  . SER   B 2 456  ? 113.005 159.639 146.966 1.00 55.55  ? 456  SER   A CB  1 
ATOM   5246  O  OG  . SER   B 2 456  ? 112.406 160.729 147.644 1.00 58.78  ? 456  SER   A OG  1 
ATOM   5247  N  N   . GLY   B 2 457  ? 114.568 156.603 147.432 1.00 58.10  ? 457  GLY   A N   1 
ATOM   5248  C  CA  . GLY   B 2 457  ? 115.187 155.522 146.693 1.00 57.41  ? 457  GLY   A CA  1 
ATOM   5249  C  C   . GLY   B 2 457  ? 115.352 154.235 147.475 1.00 63.80  ? 457  GLY   A C   1 
ATOM   5250  O  O   . GLY   B 2 457  ? 115.804 153.227 146.924 1.00 66.36  ? 457  GLY   A O   1 
ATOM   5251  N  N   . ASP   B 2 458  ? 114.994 154.249 148.760 1.00 65.92  ? 458  ASP   A N   1 
ATOM   5252  C  CA  . ASP   B 2 458  ? 115.141 153.078 149.610 1.00 60.54  ? 458  ASP   A CA  1 
ATOM   5253  C  C   . ASP   B 2 458  ? 113.832 152.567 150.192 1.00 62.86  ? 458  ASP   A C   1 
ATOM   5254  O  O   . ASP   B 2 458  ? 113.829 151.497 150.810 1.00 71.55  ? 458  ASP   A O   1 
ATOM   5255  C  CB  . ASP   B 2 458  ? 116.116 153.371 150.761 1.00 63.01  ? 458  ASP   A CB  1 
ATOM   5256  C  CG  . ASP   B 2 458  ? 116.958 152.165 151.135 1.00 66.85  ? 458  ASP   A CG  1 
ATOM   5257  O  OD1 . ASP   B 2 458  ? 116.554 151.027 150.813 1.00 68.42  ? 458  ASP   A OD1 1 
ATOM   5258  O  OD2 . ASP   B 2 458  ? 118.027 152.354 151.752 1.00 70.77  ? 458  ASP   A OD2 1 
ATOM   5259  N  N   . ASN   B 2 459  ? 112.728 153.287 150.019 1.00 51.52  ? 459  ASN   A N   1 
ATOM   5260  C  CA  . ASN   B 2 459  ? 111.449 152.828 150.525 1.00 50.62  ? 459  ASN   A CA  1 
ATOM   5261  C  C   . ASN   B 2 459  ? 110.924 151.682 149.665 1.00 54.00  ? 459  ASN   A C   1 
ATOM   5262  O  O   . ASN   B 2 459  ? 111.378 151.485 148.535 1.00 58.90  ? 459  ASN   A O   1 
ATOM   5263  C  CB  . ASN   B 2 459  ? 110.444 153.976 150.544 1.00 51.18  ? 459  ASN   A CB  1 
ATOM   5264  C  CG  . ASN   B 2 459  ? 110.177 154.539 149.166 1.00 51.91  ? 459  ASN   A CG  1 
ATOM   5265  O  OD1 . ASN   B 2 459  ? 111.050 154.532 148.301 1.00 55.73  ? 459  ASN   A OD1 1 
ATOM   5266  N  ND2 . ASN   B 2 459  ? 108.964 155.033 148.955 1.00 57.52  ? 459  ASN   A ND2 1 
ATOM   5267  N  N   . PRO   B 2 460  ? 109.964 150.898 150.183 1.00 52.70  ? 460  PRO   A N   1 
ATOM   5268  C  CA  . PRO   B 2 460  ? 109.293 149.905 149.331 1.00 55.12  ? 460  PRO   A CA  1 
ATOM   5269  C  C   . PRO   B 2 460  ? 108.583 150.549 148.147 1.00 60.51  ? 460  PRO   A C   1 
ATOM   5270  O  O   . PRO   B 2 460  ? 108.617 151.775 147.996 1.00 64.33  ? 460  PRO   A O   1 
ATOM   5271  C  CB  . PRO   B 2 460  ? 108.307 149.220 150.289 1.00 47.00  ? 460  PRO   A CB  1 
ATOM   5272  C  CG  . PRO   B 2 460  ? 108.268 150.077 151.518 1.00 48.35  ? 460  PRO   A CG  1 
ATOM   5273  C  CD  . PRO   B 2 460  ? 109.593 150.746 151.597 1.00 49.82  ? 460  PRO   A CD  1 
ATOM   5274  N  N   . ASN   B 2 461  ? 107.952 149.729 147.301 1.00 54.41  ? 461  ASN   A N   1 
ATOM   5275  C  CA  . ASN   B 2 461  ? 107.445 150.134 145.990 1.00 51.36  ? 461  ASN   A CA  1 
ATOM   5276  C  C   . ASN   B 2 461  ? 108.623 150.441 145.074 1.00 51.30  ? 461  ASN   A C   1 
ATOM   5277  O  O   . ASN   B 2 461  ? 108.867 149.727 144.090 1.00 60.90  ? 461  ASN   A O   1 
ATOM   5278  C  CB  . ASN   B 2 461  ? 106.505 151.343 146.083 1.00 47.99  ? 461  ASN   A CB  1 
ATOM   5279  C  CG  . ASN   B 2 461  ? 105.470 151.197 147.179 1.00 50.64  ? 461  ASN   A CG  1 
ATOM   5280  O  OD1 . ASN   B 2 461  ? 104.425 150.577 146.983 1.00 58.78  ? 461  ASN   A OD1 1 
ATOM   5281  N  ND2 . ASN   B 2 461  ? 105.751 151.777 148.338 1.00 42.70  ? 461  ASN   A ND2 1 
ATOM   5282  N  N   . ILE   B 2 462  ? 109.369 151.499 145.397 1.00 36.60  ? 462  ILE   A N   1 
ATOM   5283  C  CA  . ILE   B 2 462  ? 110.631 151.730 144.708 1.00 47.65  ? 462  ILE   A CA  1 
ATOM   5284  C  C   . ILE   B 2 462  ? 111.572 150.561 144.946 1.00 58.01  ? 462  ILE   A C   1 
ATOM   5285  O  O   . ILE   B 2 462  ? 112.300 150.145 144.037 1.00 62.53  ? 462  ILE   A O   1 
ATOM   5286  C  CB  . ILE   B 2 462  ? 111.248 153.075 145.144 1.00 46.38  ? 462  ILE   A CB  1 
ATOM   5287  C  CG1 . ILE   B 2 462  ? 111.047 154.127 144.053 1.00 52.01  ? 462  ILE   A CG1 1 
ATOM   5288  C  CG2 . ILE   B 2 462  ? 112.729 152.928 145.455 1.00 50.55  ? 462  ILE   A CG2 1 
ATOM   5289  C  CD1 . ILE   B 2 462  ? 109.600 154.350 143.664 1.00 54.82  ? 462  ILE   A CD1 1 
ATOM   5290  N  N   . ASN   B 2 463  ? 111.553 149.988 146.152 1.00 51.08  ? 463  ASN   A N   1 
ATOM   5291  C  CA  . ASN   B 2 463  ? 112.357 148.799 146.407 1.00 47.80  ? 463  ASN   A CA  1 
ATOM   5292  C  C   . ASN   B 2 463  ? 111.839 147.592 145.639 1.00 51.64  ? 463  ASN   A C   1 
ATOM   5293  O  O   . ASN   B 2 463  ? 112.630 146.730 145.251 1.00 57.27  ? 463  ASN   A O   1 
ATOM   5294  C  CB  . ASN   B 2 463  ? 112.405 148.499 147.901 1.00 45.12  ? 463  ASN   A CB  1 
ATOM   5295  C  CG  . ASN   B 2 463  ? 113.535 149.223 148.600 1.00 52.35  ? 463  ASN   A CG  1 
ATOM   5296  O  OD1 . ASN   B 2 463  ? 114.110 150.167 148.061 1.00 52.27  ? 463  ASN   A OD1 1 
ATOM   5297  N  ND2 . ASN   B 2 463  ? 113.862 148.782 149.808 1.00 53.92  ? 463  ASN   A ND2 1 
ATOM   5298  N  N   . GLY   B 2 464  ? 110.530 147.511 145.398 1.00 45.76  ? 464  GLY   A N   1 
ATOM   5299  C  CA  . GLY   B 2 464  ? 110.020 146.450 144.543 1.00 45.39  ? 464  GLY   A CA  1 
ATOM   5300  C  C   . GLY   B 2 464  ? 110.521 146.567 143.116 1.00 50.86  ? 464  GLY   A C   1 
ATOM   5301  O  O   . GLY   B 2 464  ? 110.921 145.574 142.501 1.00 54.81  ? 464  GLY   A O   1 
ATOM   5302  N  N   . LEU   B 2 465  ? 110.516 147.786 142.575 1.00 47.80  ? 465  LEU   A N   1 
ATOM   5303  C  CA  . LEU   B 2 465  ? 111.079 148.004 141.242 1.00 39.21  ? 465  LEU   A CA  1 
ATOM   5304  C  C   . LEU   B 2 465  ? 112.575 147.704 141.216 1.00 36.83  ? 465  LEU   A C   1 
ATOM   5305  O  O   . LEU   B 2 465  ? 113.090 147.131 140.245 1.00 48.09  ? 465  LEU   A O   1 
ATOM   5306  C  CB  . LEU   B 2 465  ? 110.814 149.436 140.782 1.00 43.15  ? 465  LEU   A CB  1 
ATOM   5307  C  CG  . LEU   B 2 465  ? 109.371 149.797 140.438 1.00 47.08  ? 465  LEU   A CG  1 
ATOM   5308  C  CD1 . LEU   B 2 465  ? 109.292 151.226 139.939 1.00 48.10  ? 465  LEU   A CD1 1 
ATOM   5309  C  CD2 . LEU   B 2 465  ? 108.812 148.838 139.404 1.00 47.94  ? 465  LEU   A CD2 1 
ATOM   5310  N  N   . VAL   B 2 466  ? 113.291 148.093 142.272 1.00 36.44  ? 466  VAL   A N   1 
ATOM   5311  C  CA  . VAL   B 2 466  ? 114.723 147.821 142.343 1.00 40.31  ? 466  VAL   A CA  1 
ATOM   5312  C  C   . VAL   B 2 466  ? 114.977 146.321 142.408 1.00 49.08  ? 466  VAL   A C   1 
ATOM   5313  O  O   . VAL   B 2 466  ? 115.938 145.817 141.821 1.00 57.72  ? 466  VAL   A O   1 
ATOM   5314  C  CB  . VAL   B 2 466  ? 115.347 148.565 143.537 1.00 41.37  ? 466  VAL   A CB  1 
ATOM   5315  C  CG1 . VAL   B 2 466  ? 116.765 148.094 143.782 1.00 44.55  ? 466  VAL   A CG1 1 
ATOM   5316  C  CG2 . VAL   B 2 466  ? 115.336 150.057 143.283 1.00 44.82  ? 466  VAL   A CG2 1 
ATOM   5317  N  N   . THR   B 2 467  ? 114.123 145.586 143.122 1.00 45.36  ? 467  THR   A N   1 
ATOM   5318  C  CA  . THR   B 2 467  ? 114.233 144.132 143.157 1.00 40.41  ? 467  THR   A CA  1 
ATOM   5319  C  C   . THR   B 2 467  ? 113.948 143.525 141.790 1.00 49.40  ? 467  THR   A C   1 
ATOM   5320  O  O   . THR   B 2 467  ? 114.596 142.554 141.393 1.00 58.71  ? 467  THR   A O   1 
ATOM   5321  C  CB  . THR   B 2 467  ? 113.285 143.560 144.210 1.00 44.52  ? 467  THR   A CB  1 
ATOM   5322  O  OG1 . THR   B 2 467  ? 113.604 144.113 145.492 1.00 52.23  ? 467  THR   A OG1 1 
ATOM   5323  C  CG2 . THR   B 2 467  ? 113.410 142.052 144.280 1.00 46.23  ? 467  THR   A CG2 1 
ATOM   5324  N  N   . PHE   B 2 468  ? 112.979 144.079 141.061 1.00 45.77  ? 468  PHE   A N   1 
ATOM   5325  C  CA  . PHE   B 2 468  ? 112.730 143.651 139.685 1.00 35.07  ? 468  PHE   A CA  1 
ATOM   5326  C  C   . PHE   B 2 468  ? 113.987 143.798 138.831 1.00 36.42  ? 468  PHE   A C   1 
ATOM   5327  O  O   . PHE   B 2 468  ? 114.422 142.852 138.154 1.00 44.58  ? 468  PHE   A O   1 
ATOM   5328  C  CB  . PHE   B 2 468  ? 111.574 144.478 139.114 1.00 39.64  ? 468  PHE   A CB  1 
ATOM   5329  C  CG  . PHE   B 2 468  ? 111.068 144.008 137.782 1.00 44.15  ? 468  PHE   A CG  1 
ATOM   5330  C  CD1 . PHE   B 2 468  ? 110.101 143.022 137.703 1.00 47.36  ? 468  PHE   A CD1 1 
ATOM   5331  C  CD2 . PHE   B 2 468  ? 111.527 144.579 136.611 1.00 45.28  ? 468  PHE   A CD2 1 
ATOM   5332  C  CE1 . PHE   B 2 468  ? 109.622 142.600 136.481 1.00 46.33  ? 468  PHE   A CE1 1 
ATOM   5333  C  CE2 . PHE   B 2 468  ? 111.051 144.160 135.387 1.00 41.82  ? 468  PHE   A CE2 1 
ATOM   5334  C  CZ  . PHE   B 2 468  ? 110.098 143.169 135.323 1.00 44.52  ? 468  PHE   A CZ  1 
ATOM   5335  N  N   . ALA   B 2 469  ? 114.602 144.981 138.878 1.00 38.43  ? 469  ALA   A N   1 
ATOM   5336  C  CA  . ALA   B 2 469  ? 115.808 145.226 138.091 1.00 37.35  ? 469  ALA   A CA  1 
ATOM   5337  C  C   . ALA   B 2 469  ? 116.967 144.340 138.541 1.00 45.41  ? 469  ALA   A C   1 
ATOM   5338  O  O   . ALA   B 2 469  ? 117.707 143.799 137.710 1.00 48.95  ? 469  ALA   A O   1 
ATOM   5339  C  CB  . ALA   B 2 469  ? 116.194 146.700 138.176 1.00 43.15  ? 469  ALA   A CB  1 
ATOM   5340  N  N   . ASN   B 2 470  ? 117.144 144.180 139.853 1.00 43.07  ? 470  ASN   A N   1 
ATOM   5341  C  CA  . ASN   B 2 470  ? 118.229 143.353 140.364 1.00 36.90  ? 470  ASN   A CA  1 
ATOM   5342  C  C   . ASN   B 2 470  ? 118.000 141.881 140.066 1.00 46.52  ? 470  ASN   A C   1 
ATOM   5343  O  O   . ASN   B 2 470  ? 118.961 141.115 139.979 1.00 57.89  ? 470  ASN   A O   1 
ATOM   5344  C  CB  . ASN   B 2 470  ? 118.396 143.566 141.867 1.00 41.66  ? 470  ASN   A CB  1 
ATOM   5345  C  CG  . ASN   B 2 470  ? 118.948 144.931 142.205 1.00 55.13  ? 470  ASN   A CG  1 
ATOM   5346  O  OD1 . ASN   B 2 470  ? 119.624 145.559 141.391 1.00 61.90  ? 470  ASN   A OD1 1 
ATOM   5347  N  ND2 . ASN   B 2 470  ? 118.670 145.398 143.414 1.00 51.39  ? 470  ASN   A ND2 1 
ATOM   5348  N  N   . ALA   B 2 471  ? 116.743 141.461 139.931 1.00 39.45  ? 471  ALA   A N   1 
ATOM   5349  C  CA  . ALA   B 2 471  ? 116.464 140.099 139.498 1.00 38.13  ? 471  ALA   A CA  1 
ATOM   5350  C  C   . ALA   B 2 471  ? 116.836 139.915 138.039 1.00 38.84  ? 471  ALA   A C   1 
ATOM   5351  O  O   . ALA   B 2 471  ? 117.382 138.874 137.657 1.00 44.24  ? 471  ALA   A O   1 
ATOM   5352  C  CB  . ALA   B 2 471  ? 114.992 139.764 139.722 1.00 41.53  ? 471  ALA   A CB  1 
ATOM   5353  N  N   . PHE   B 2 472  ? 116.545 140.915 137.206 1.00 41.29  ? 472  PHE   A N   1 
ATOM   5354  C  CA  . PHE   B 2 472  ? 116.981 140.829 135.815 1.00 37.21  ? 472  PHE   A CA  1 
ATOM   5355  C  C   . PHE   B 2 472  ? 118.501 140.820 135.713 1.00 36.24  ? 472  PHE   A C   1 
ATOM   5356  O  O   . PHE   B 2 472  ? 119.066 140.183 134.817 1.00 38.58  ? 472  PHE   A O   1 
ATOM   5357  C  CB  . PHE   B 2 472  ? 116.389 141.974 134.998 1.00 38.00  ? 472  PHE   A CB  1 
ATOM   5358  C  CG  . PHE   B 2 472  ? 115.173 141.582 134.216 1.00 35.78  ? 472  PHE   A CG  1 
ATOM   5359  C  CD1 . PHE   B 2 472  ? 115.292 140.811 133.075 1.00 39.51  ? 472  PHE   A CD1 1 
ATOM   5360  C  CD2 . PHE   B 2 472  ? 113.915 141.973 134.621 1.00 35.46  ? 472  PHE   A CD2 1 
ATOM   5361  C  CE1 . PHE   B 2 472  ? 114.180 140.442 132.354 1.00 41.00  ? 472  PHE   A CE1 1 
ATOM   5362  C  CE2 . PHE   B 2 472  ? 112.800 141.607 133.903 1.00 41.90  ? 472  PHE   A CE2 1 
ATOM   5363  C  CZ  . PHE   B 2 472  ? 112.933 140.841 132.768 1.00 45.04  ? 472  PHE   A CZ  1 
ATOM   5364  N  N   . ILE   B 2 473  ? 119.182 141.520 136.622 1.00 46.39  ? 473  ILE   A N   1 
ATOM   5365  C  CA  . ILE   B 2 473  ? 120.643 141.566 136.580 1.00 41.16  ? 473  ILE   A CA  1 
ATOM   5366  C  C   . ILE   B 2 473  ? 121.250 140.269 137.105 1.00 42.72  ? 473  ILE   A C   1 
ATOM   5367  O  O   . ILE   B 2 473  ? 122.192 139.728 136.515 1.00 50.89  ? 473  ILE   A O   1 
ATOM   5368  C  CB  . ILE   B 2 473  ? 121.164 142.784 137.361 1.00 40.06  ? 473  ILE   A CB  1 
ATOM   5369  C  CG1 . ILE   B 2 473  ? 120.811 144.076 136.629 1.00 45.98  ? 473  ILE   A CG1 1 
ATOM   5370  C  CG2 . ILE   B 2 473  ? 122.663 142.686 137.559 1.00 40.00  ? 473  ILE   A CG2 1 
ATOM   5371  C  CD1 . ILE   B 2 473  ? 121.328 145.310 137.310 1.00 45.13  ? 473  ILE   A CD1 1 
ATOM   5372  N  N   . THR   B 2 474  ? 120.735 139.757 138.225 1.00 42.91  ? 474  THR   A N   1 
ATOM   5373  C  CA  . THR   B 2 474  ? 121.336 138.593 138.872 1.00 35.99  ? 474  THR   A CA  1 
ATOM   5374  C  C   . THR   B 2 474  ? 121.262 137.357 137.987 1.00 42.23  ? 474  THR   A C   1 
ATOM   5375  O  O   . THR   B 2 474  ? 122.246 136.620 137.858 1.00 47.54  ? 474  THR   A O   1 
ATOM   5376  C  CB  . THR   B 2 474  ? 120.648 138.327 140.211 1.00 35.87  ? 474  THR   A CB  1 
ATOM   5377  O  OG1 . THR   B 2 474  ? 120.810 139.463 141.067 1.00 45.42  ? 474  THR   A OG1 1 
ATOM   5378  C  CG2 . THR   B 2 474  ? 121.242 137.102 140.887 1.00 43.57  ? 474  THR   A CG2 1 
ATOM   5379  N  N   . PHE   B 2 475  ? 120.109 137.116 137.365 1.00 38.71  ? 475  PHE   A N   1 
ATOM   5380  C  CA  . PHE   B 2 475  ? 119.906 135.943 136.528 1.00 38.14  ? 475  PHE   A CA  1 
ATOM   5381  C  C   . PHE   B 2 475  ? 120.106 136.248 135.048 1.00 44.65  ? 475  PHE   A C   1 
ATOM   5382  O  O   . PHE   B 2 475  ? 119.426 135.668 134.197 1.00 51.89  ? 475  PHE   A O   1 
ATOM   5383  C  CB  . PHE   B 2 475  ? 118.516 135.355 136.764 1.00 42.04  ? 475  PHE   A CB  1 
ATOM   5384  C  CG  . PHE   B 2 475  ? 118.161 135.197 138.212 1.00 39.70  ? 475  PHE   A CG  1 
ATOM   5385  C  CD1 . PHE   B 2 475  ? 118.733 134.199 138.976 1.00 40.56  ? 475  PHE   A CD1 1 
ATOM   5386  C  CD2 . PHE   B 2 475  ? 117.239 136.037 138.805 1.00 43.37  ? 475  PHE   A CD2 1 
ATOM   5387  C  CE1 . PHE   B 2 475  ? 118.402 134.053 140.303 1.00 40.93  ? 475  PHE   A CE1 1 
ATOM   5388  C  CE2 . PHE   B 2 475  ? 116.905 135.893 140.132 1.00 42.50  ? 475  PHE   A CE2 1 
ATOM   5389  C  CZ  . PHE   B 2 475  ? 117.485 134.901 140.880 1.00 38.71  ? 475  PHE   A CZ  1 
ATOM   5390  N  N   . GLN   B 2 476  ? 121.029 137.155 134.725 1.00 38.64  ? 476  GLN   A N   1 
ATOM   5391  C  CA  . GLN   B 2 476  ? 121.297 137.482 133.331 1.00 40.75  ? 476  GLN   A CA  1 
ATOM   5392  C  C   . GLN   B 2 476  ? 121.970 136.339 132.586 1.00 51.12  ? 476  GLN   A C   1 
ATOM   5393  O  O   . GLN   B 2 476  ? 121.964 136.335 131.350 1.00 60.12  ? 476  GLN   A O   1 
ATOM   5394  C  CB  . GLN   B 2 476  ? 122.160 138.738 133.242 1.00 40.35  ? 476  GLN   A CB  1 
ATOM   5395  C  CG  . GLN   B 2 476  ? 123.510 138.615 133.916 1.00 41.65  ? 476  GLN   A CG  1 
ATOM   5396  C  CD  . GLN   B 2 476  ? 124.331 139.877 133.802 1.00 49.04  ? 476  GLN   A CD  1 
ATOM   5397  O  OE1 . GLN   B 2 476  ? 124.154 140.662 132.874 1.00 46.41  ? 476  GLN   A OE1 1 
ATOM   5398  N  NE2 . GLN   B 2 476  ? 125.238 140.081 134.749 1.00 52.60  ? 476  GLN   A NE2 1 
ATOM   5399  N  N   . ASN   B 2 477  ? 122.547 135.373 133.301 1.00 39.26  ? 477  ASN   A N   1 
ATOM   5400  C  CA  . ASN   B 2 477  ? 123.199 134.246 132.649 1.00 31.59  ? 477  ASN   A CA  1 
ATOM   5401  C  C   . ASN   B 2 477  ? 122.213 133.231 132.095 1.00 41.18  ? 477  ASN   A C   1 
ATOM   5402  O  O   . ASN   B 2 477  ? 122.640 132.296 131.413 1.00 46.95  ? 477  ASN   A O   1 
ATOM   5403  C  CB  . ASN   B 2 477  ? 124.158 133.555 133.615 1.00 40.21  ? 477  ASN   A CB  1 
ATOM   5404  C  CG  . ASN   B 2 477  ? 125.415 134.358 133.857 1.00 47.92  ? 477  ASN   A CG  1 
ATOM   5405  O  OD1 . ASN   B 2 477  ? 125.484 135.540 133.524 1.00 50.22  ? 477  ASN   A OD1 1 
ATOM   5406  N  ND2 . ASN   B 2 477  ? 126.421 133.720 134.441 1.00 49.59  ? 477  ASN   A ND2 1 
ATOM   5407  N  N   . ILE   B 2 478  ? 120.914 133.381 132.367 1.00 40.38  ? 478  ILE   A N   1 
ATOM   5408  C  CA  . ILE   B 2 478  ? 119.931 132.502 131.749 1.00 36.51  ? 478  ILE   A CA  1 
ATOM   5409  C  C   . ILE   B 2 478  ? 119.962 132.649 130.235 1.00 49.54  ? 478  ILE   A C   1 
ATOM   5410  O  O   . ILE   B 2 478  ? 119.578 131.724 129.511 1.00 60.83  ? 478  ILE   A O   1 
ATOM   5411  C  CB  . ILE   B 2 478  ? 118.524 132.771 132.326 1.00 37.81  ? 478  ILE   A CB  1 
ATOM   5412  C  CG1 . ILE   B 2 478  ? 117.590 131.600 132.023 1.00 47.00  ? 478  ILE   A CG1 1 
ATOM   5413  C  CG2 . ILE   B 2 478  ? 117.948 134.061 131.778 1.00 44.25  ? 478  ILE   A CG2 1 
ATOM   5414  C  CD1 . ILE   B 2 478  ? 116.223 131.734 132.644 1.00 47.88  ? 478  ILE   A CD1 1 
ATOM   5415  N  N   . VAL   B 2 479  ? 120.414 133.798 129.739 1.00 46.34  ? 479  VAL   A N   1 
ATOM   5416  C  CA  . VAL   B 2 479  ? 120.793 133.980 128.340 1.00 39.79  ? 479  VAL   A CA  1 
ATOM   5417  C  C   . VAL   B 2 479  ? 122.233 134.479 128.338 1.00 43.06  ? 479  VAL   A C   1 
ATOM   5418  O  O   . VAL   B 2 479  ? 122.466 135.695 128.358 1.00 51.86  ? 479  VAL   A O   1 
ATOM   5419  C  CB  . VAL   B 2 479  ? 119.857 134.958 127.615 1.00 43.10  ? 479  VAL   A CB  1 
ATOM   5420  C  CG1 . VAL   B 2 479  ? 120.234 135.058 126.149 1.00 47.96  ? 479  VAL   A CG1 1 
ATOM   5421  C  CG2 . VAL   B 2 479  ? 118.415 134.521 127.763 1.00 46.30  ? 479  VAL   A CG2 1 
ATOM   5422  N  N   . PRO   B 2 480  ? 123.222 133.590 128.346 1.00 44.63  ? 480  PRO   A N   1 
ATOM   5423  C  CA  . PRO   B 2 480  ? 124.612 134.038 128.468 1.00 45.70  ? 480  PRO   A CA  1 
ATOM   5424  C  C   . PRO   B 2 480  ? 125.079 134.798 127.239 1.00 50.33  ? 480  PRO   A C   1 
ATOM   5425  O  O   . PRO   B 2 480  ? 124.624 134.560 126.118 1.00 54.83  ? 480  PRO   A O   1 
ATOM   5426  C  CB  . PRO   B 2 480  ? 125.389 132.731 128.641 1.00 42.49  ? 480  PRO   A CB  1 
ATOM   5427  C  CG  . PRO   B 2 480  ? 124.540 131.711 127.970 1.00 49.47  ? 480  PRO   A CG  1 
ATOM   5428  C  CD  . PRO   B 2 480  ? 123.123 132.125 128.234 1.00 45.38  ? 480  PRO   A CD  1 
ATOM   5429  N  N   . ILE   B 2 481  ? 126.006 135.728 127.468 1.00 47.46  ? 481  ILE   A N   1 
ATOM   5430  C  CA  . ILE   B 2 481  ? 126.609 136.462 126.364 1.00 47.60  ? 481  ILE   A CA  1 
ATOM   5431  C  C   . ILE   B 2 481  ? 127.792 135.709 125.771 1.00 48.33  ? 481  ILE   A C   1 
ATOM   5432  O  O   . ILE   B 2 481  ? 128.101 135.886 124.586 1.00 59.29  ? 481  ILE   A O   1 
ATOM   5433  C  CB  . ILE   B 2 481  ? 127.014 137.875 126.821 1.00 50.55  ? 481  ILE   A CB  1 
ATOM   5434  C  CG1 . ILE   B 2 481  ? 127.469 138.726 125.635 1.00 52.39  ? 481  ILE   A CG1 1 
ATOM   5435  C  CG2 . ILE   B 2 481  ? 128.090 137.811 127.878 1.00 49.45  ? 481  ILE   A CG2 1 
ATOM   5436  C  CD1 . ILE   B 2 481  ? 127.775 140.156 126.001 1.00 51.07  ? 481  ILE   A CD1 1 
ATOM   5437  N  N   . SER   B 2 482  ? 128.451 134.857 126.555 1.00 51.71  ? 482  SER   A N   1 
ATOM   5438  C  CA  . SER   B 2 482  ? 129.544 134.038 126.049 1.00 51.38  ? 482  SER   A CA  1 
ATOM   5439  C  C   . SER   B 2 482  ? 129.078 132.963 125.080 1.00 52.79  ? 482  SER   A C   1 
ATOM   5440  O  O   . SER   B 2 482  ? 129.915 132.368 124.393 1.00 64.06  ? 482  SER   A O   1 
ATOM   5441  C  CB  . SER   B 2 482  ? 130.291 133.384 127.212 1.00 58.23  ? 482  SER   A CB  1 
ATOM   5442  O  OG  . SER   B 2 482  ? 129.406 132.637 128.026 1.00 58.85  ? 482  SER   A OG  1 
ATOM   5443  N  N   . LEU   B 2 483  ? 127.773 132.694 125.020 1.00 43.22  ? 483  LEU   A N   1 
ATOM   5444  C  CA  . LEU   B 2 483  ? 127.264 131.680 124.105 1.00 49.00  ? 483  LEU   A CA  1 
ATOM   5445  C  C   . LEU   B 2 483  ? 127.541 132.053 122.656 1.00 57.52  ? 483  LEU   A C   1 
ATOM   5446  O  O   . LEU   B 2 483  ? 128.002 131.218 121.868 1.00 64.36  ? 483  LEU   A O   1 
ATOM   5447  C  CB  . LEU   B 2 483  ? 125.766 131.482 124.337 1.00 48.75  ? 483  LEU   A CB  1 
ATOM   5448  C  CG  . LEU   B 2 483  ? 124.978 130.598 123.372 1.00 51.21  ? 483  LEU   A CG  1 
ATOM   5449  C  CD1 . LEU   B 2 483  ? 124.078 129.663 124.147 1.00 49.95  ? 483  LEU   A CD1 1 
ATOM   5450  C  CD2 . LEU   B 2 483  ? 124.153 131.451 122.429 1.00 51.84  ? 483  LEU   A CD2 1 
ATOM   5451  N  N   . TYR   B 2 484  ? 127.293 133.310 122.290 1.00 48.95  ? 484  TYR   A N   1 
ATOM   5452  C  CA  . TYR   B 2 484  ? 127.403 133.700 120.890 1.00 50.27  ? 484  TYR   A CA  1 
ATOM   5453  C  C   . TYR   B 2 484  ? 128.856 133.825 120.453 1.00 52.84  ? 484  TYR   A C   1 
ATOM   5454  O  O   . TYR   B 2 484  ? 129.191 133.490 119.312 1.00 62.18  ? 484  TYR   A O   1 
ATOM   5455  C  CB  . TYR   B 2 484  ? 126.633 134.995 120.650 1.00 53.78  ? 484  TYR   A CB  1 
ATOM   5456  C  CG  . TYR   B 2 484  ? 125.140 134.776 120.612 1.00 58.11  ? 484  TYR   A CG  1 
ATOM   5457  C  CD1 . TYR   B 2 484  ? 124.518 134.326 119.456 1.00 58.12  ? 484  TYR   A CD1 1 
ATOM   5458  C  CD2 . TYR   B 2 484  ? 124.356 134.998 121.732 1.00 59.18  ? 484  TYR   A CD2 1 
ATOM   5459  C  CE1 . TYR   B 2 484  ? 123.157 134.114 119.414 1.00 55.36  ? 484  TYR   A CE1 1 
ATOM   5460  C  CE2 . TYR   B 2 484  ? 122.992 134.788 121.698 1.00 61.08  ? 484  TYR   A CE2 1 
ATOM   5461  C  CZ  . TYR   B 2 484  ? 122.399 134.347 120.537 1.00 57.34  ? 484  TYR   A CZ  1 
ATOM   5462  O  OH  . TYR   B 2 484  ? 121.041 134.136 120.499 1.00 54.47  ? 484  TYR   A OH  1 
ATOM   5463  N  N   . ILE   B 2 485  ? 129.738 134.282 121.344 1.00 38.12  ? 485  ILE   A N   1 
ATOM   5464  C  CA  . ILE   B 2 485  ? 131.160 134.320 121.013 1.00 44.76  ? 485  ILE   A CA  1 
ATOM   5465  C  C   . ILE   B 2 485  ? 131.675 132.915 120.736 1.00 52.91  ? 485  ILE   A C   1 
ATOM   5466  O  O   . ILE   B 2 485  ? 132.383 132.674 119.748 1.00 61.03  ? 485  ILE   A O   1 
ATOM   5467  C  CB  . ILE   B 2 485  ? 131.957 134.988 122.147 1.00 50.48  ? 485  ILE   A CB  1 
ATOM   5468  C  CG1 . ILE   B 2 485  ? 131.051 135.882 122.985 1.00 50.06  ? 485  ILE   A CG1 1 
ATOM   5469  C  CG2 . ILE   B 2 485  ? 133.114 135.787 121.582 1.00 56.83  ? 485  ILE   A CG2 1 
ATOM   5470  C  CD1 . ILE   B 2 485  ? 131.754 136.518 124.154 1.00 51.51  ? 485  ILE   A CD1 1 
ATOM   5471  N  N   . SER   B 2 486  ? 131.325 131.966 121.608 1.00 45.55  ? 486  SER   A N   1 
ATOM   5472  C  CA  . SER   B 2 486  ? 131.751 130.586 121.421 1.00 47.77  ? 486  SER   A CA  1 
ATOM   5473  C  C   . SER   B 2 486  ? 131.175 130.001 120.141 1.00 54.15  ? 486  SER   A C   1 
ATOM   5474  O  O   . SER   B 2 486  ? 131.871 129.290 119.408 1.00 61.96  ? 486  SER   A O   1 
ATOM   5475  C  CB  . SER   B 2 486  ? 131.339 129.748 122.629 1.00 52.57  ? 486  SER   A CB  1 
ATOM   5476  O  OG  . SER   B 2 486  ? 131.819 130.324 123.828 1.00 61.47  ? 486  SER   A OG  1 
ATOM   5477  N  N   . ILE   B 2 487  ? 129.905 130.293 119.854 1.00 44.50  ? 487  ILE   A N   1 
ATOM   5478  C  CA  . ILE   B 2 487  ? 129.284 129.790 118.632 1.00 45.48  ? 487  ILE   A CA  1 
ATOM   5479  C  C   . ILE   B 2 487  ? 130.008 130.328 117.403 1.00 55.57  ? 487  ILE   A C   1 
ATOM   5480  O  O   . ILE   B 2 487  ? 130.303 129.583 116.460 1.00 58.42  ? 487  ILE   A O   1 
ATOM   5481  C  CB  . ILE   B 2 487  ? 127.788 130.144 118.606 1.00 43.95  ? 487  ILE   A CB  1 
ATOM   5482  C  CG1 . ILE   B 2 487  ? 127.014 129.259 119.580 1.00 49.62  ? 487  ILE   A CG1 1 
ATOM   5483  C  CG2 . ILE   B 2 487  ? 127.229 130.000 117.209 1.00 52.28  ? 487  ILE   A CG2 1 
ATOM   5484  C  CD1 . ILE   B 2 487  ? 125.543 129.578 119.640 1.00 55.65  ? 487  ILE   A CD1 1 
ATOM   5485  N  N   . GLU   B 2 488  ? 130.305 131.629 117.394 1.00 53.27  ? 488  GLU   A N   1 
ATOM   5486  C  CA  . GLU   B 2 488  ? 130.978 132.224 116.243 1.00 51.58  ? 488  GLU   A CA  1 
ATOM   5487  C  C   . GLU   B 2 488  ? 132.368 131.633 116.054 1.00 56.32  ? 488  GLU   A C   1 
ATOM   5488  O  O   . GLU   B 2 488  ? 132.769 131.305 114.930 1.00 66.27  ? 488  GLU   A O   1 
ATOM   5489  C  CB  . GLU   B 2 488  ? 131.054 133.743 116.400 1.00 50.19  ? 488  GLU   A CB  1 
ATOM   5490  C  CG  . GLU   B 2 488  ? 129.709 134.455 116.390 1.00 60.18  ? 488  GLU   A CG  1 
ATOM   5491  C  CD  . GLU   B 2 488  ? 129.006 134.394 115.044 1.00 68.04  ? 488  GLU   A CD  1 
ATOM   5492  O  OE1 . GLU   B 2 488  ? 129.639 133.988 114.048 1.00 67.41  ? 488  GLU   A OE1 1 
ATOM   5493  O  OE2 . GLU   B 2 488  ? 127.813 134.758 114.983 1.00 64.96  ? 488  GLU   A OE2 1 
ATOM   5494  N  N   . ALA   B 2 489  ? 133.118 131.483 117.148 1.00 44.72  ? 489  ALA   A N   1 
ATOM   5495  C  CA  . ALA   B 2 489  ? 134.457 130.911 117.043 1.00 47.20  ? 489  ALA   A CA  1 
ATOM   5496  C  C   . ALA   B 2 489  ? 134.407 129.471 116.549 1.00 52.56  ? 489  ALA   A C   1 
ATOM   5497  O  O   . ALA   B 2 489  ? 135.209 129.069 115.695 1.00 55.51  ? 489  ALA   A O   1 
ATOM   5498  C  CB  . ALA   B 2 489  ? 135.168 130.994 118.390 1.00 46.39  ? 489  ALA   A CB  1 
ATOM   5499  N  N   . VAL   B 2 490  ? 133.466 128.682 117.068 1.00 46.64  ? 490  VAL   A N   1 
ATOM   5500  C  CA  . VAL   B 2 490  ? 133.347 127.290 116.655 1.00 45.00  ? 490  VAL   A CA  1 
ATOM   5501  C  C   . VAL   B 2 490  ? 132.971 127.195 115.183 1.00 48.55  ? 490  VAL   A C   1 
ATOM   5502  O  O   . VAL   B 2 490  ? 133.506 126.359 114.450 1.00 55.45  ? 490  VAL   A O   1 
ATOM   5503  C  CB  . VAL   B 2 490  ? 132.339 126.557 117.557 1.00 42.51  ? 490  VAL   A CB  1 
ATOM   5504  C  CG1 . VAL   B 2 490  ? 131.887 125.261 116.914 1.00 52.30  ? 490  VAL   A CG1 1 
ATOM   5505  C  CG2 . VAL   B 2 490  ? 132.966 126.284 118.907 1.00 40.85  ? 490  VAL   A CG2 1 
ATOM   5506  N  N   . ARG   B 2 491  ? 132.054 128.048 114.722 1.00 43.03  ? 491  ARG   A N   1 
ATOM   5507  C  CA  . ARG   B 2 491  ? 131.672 128.012 113.314 1.00 43.27  ? 491  ARG   A CA  1 
ATOM   5508  C  C   . ARG   B 2 491  ? 132.826 128.441 112.413 1.00 45.81  ? 491  ARG   A C   1 
ATOM   5509  O  O   . ARG   B 2 491  ? 133.018 127.874 111.330 1.00 57.33  ? 491  ARG   A O   1 
ATOM   5510  C  CB  . ARG   B 2 491  ? 130.437 128.879 113.080 1.00 41.19  ? 491  ARG   A CB  1 
ATOM   5511  C  CG  . ARG   B 2 491  ? 129.180 128.335 113.739 1.00 41.69  ? 491  ARG   A CG  1 
ATOM   5512  C  CD  . ARG   B 2 491  ? 127.954 128.556 112.877 1.00 45.81  ? 491  ARG   A CD  1 
ATOM   5513  N  NE  . ARG   B 2 491  ? 127.033 129.526 113.456 1.00 54.24  ? 491  ARG   A NE  1 
ATOM   5514  C  CZ  . ARG   B 2 491  ? 125.953 129.208 114.155 1.00 48.03  ? 491  ARG   A CZ  1 
ATOM   5515  N  NH1 . ARG   B 2 491  ? 125.631 127.948 114.394 1.00 46.59  ? 491  ARG   A NH1 1 
ATOM   5516  N  NH2 . ARG   B 2 491  ? 125.175 130.179 114.624 1.00 47.33  ? 491  ARG   A NH2 1 
ATOM   5517  N  N   . THR   B 2 492  ? 133.613 129.429 112.844 1.00 37.93  ? 492  THR   A N   1 
ATOM   5518  C  CA  . THR   B 2 492  ? 134.785 129.823 112.068 1.00 37.62  ? 492  THR   A CA  1 
ATOM   5519  C  C   . THR   B 2 492  ? 135.790 128.680 111.970 1.00 50.02  ? 492  THR   A C   1 
ATOM   5520  O  O   . THR   B 2 492  ? 136.349 128.419 110.896 1.00 58.69  ? 492  THR   A O   1 
ATOM   5521  C  CB  . THR   B 2 492  ? 135.437 131.057 112.689 1.00 42.94  ? 492  THR   A CB  1 
ATOM   5522  O  OG1 . THR   B 2 492  ? 134.459 132.093 112.833 1.00 49.81  ? 492  THR   A OG1 1 
ATOM   5523  C  CG2 . THR   B 2 492  ? 136.568 131.561 111.812 1.00 46.63  ? 492  THR   A CG2 1 
ATOM   5524  N  N   . ILE   B 2 493  ? 136.026 127.977 113.079 1.00 41.35  ? 493  ILE   A N   1 
ATOM   5525  C  CA  . ILE   B 2 493  ? 136.969 126.865 113.042 1.00 36.64  ? 493  ILE   A CA  1 
ATOM   5526  C  C   . ILE   B 2 493  ? 136.414 125.703 112.223 1.00 42.65  ? 493  ILE   A C   1 
ATOM   5527  O  O   . ILE   B 2 493  ? 137.174 124.966 111.587 1.00 50.89  ? 493  ILE   A O   1 
ATOM   5528  C  CB  . ILE   B 2 493  ? 137.348 126.441 114.471 1.00 37.72  ? 493  ILE   A CB  1 
ATOM   5529  C  CG1 . ILE   B 2 493  ? 138.005 127.610 115.201 1.00 40.78  ? 493  ILE   A CG1 1 
ATOM   5530  C  CG2 . ILE   B 2 493  ? 138.296 125.260 114.452 1.00 48.07  ? 493  ILE   A CG2 1 
ATOM   5531  C  CD1 . ILE   B 2 493  ? 138.456 127.280 116.598 1.00 45.25  ? 493  ILE   A CD1 1 
ATOM   5532  N  N   . GLN   B 2 494  ? 135.093 125.517 112.212 1.00 34.19  ? 494  GLN   A N   1 
ATOM   5533  C  CA  . GLN   B 2 494  ? 134.500 124.503 111.344 1.00 37.62  ? 494  GLN   A CA  1 
ATOM   5534  C  C   . GLN   B 2 494  ? 134.689 124.859 109.874 1.00 45.57  ? 494  GLN   A C   1 
ATOM   5535  O  O   . GLN   B 2 494  ? 134.961 123.982 109.042 1.00 48.30  ? 494  GLN   A O   1 
ATOM   5536  C  CB  . GLN   B 2 494  ? 133.021 124.329 111.676 1.00 35.67  ? 494  GLN   A CB  1 
ATOM   5537  C  CG  . GLN   B 2 494  ? 132.765 123.663 113.012 1.00 37.34  ? 494  GLN   A CG  1 
ATOM   5538  C  CD  . GLN   B 2 494  ? 131.313 123.721 113.421 1.00 42.82  ? 494  GLN   A CD  1 
ATOM   5539  O  OE1 . GLN   B 2 494  ? 130.499 124.372 112.769 1.00 49.82  ? 494  GLN   A OE1 1 
ATOM   5540  N  NE2 . GLN   B 2 494  ? 130.977 123.040 114.507 1.00 45.43  ? 494  GLN   A NE2 1 
ATOM   5541  N  N   . ALA   B 2 495  ? 134.550 126.142 109.535 1.00 44.61  ? 495  ALA   A N   1 
ATOM   5542  C  CA  . ALA   B 2 495  ? 134.857 126.579 108.177 1.00 36.02  ? 495  ALA   A CA  1 
ATOM   5543  C  C   . ALA   B 2 495  ? 136.319 126.319 107.839 1.00 33.27  ? 495  ALA   A C   1 
ATOM   5544  O  O   . ALA   B 2 495  ? 136.645 125.912 106.718 1.00 45.09  ? 495  ALA   A O   1 
ATOM   5545  C  CB  . ALA   B 2 495  ? 134.520 128.060 108.012 1.00 41.60  ? 495  ALA   A CB  1 
ATOM   5546  N  N   . ALA   B 2 496  ? 137.212 126.546 108.803 1.00 37.73  ? 496  ALA   A N   1 
ATOM   5547  C  CA  . ALA   B 2 496  ? 138.626 126.243 108.591 1.00 41.44  ? 496  ALA   A CA  1 
ATOM   5548  C  C   . ALA   B 2 496  ? 138.846 124.752 108.359 1.00 40.74  ? 496  ALA   A C   1 
ATOM   5549  O  O   . ALA   B 2 496  ? 139.663 124.362 107.517 1.00 48.93  ? 496  ALA   A O   1 
ATOM   5550  C  CB  . ALA   B 2 496  ? 139.450 126.729 109.781 1.00 41.05  ? 496  ALA   A CB  1 
ATOM   5551  N  N   . PHE   B 2 497  ? 138.136 123.906 109.108 1.00 41.50  ? 497  PHE   A N   1 
ATOM   5552  C  CA  . PHE   B 2 497  ? 138.212 122.464 108.887 1.00 35.86  ? 497  PHE   A CA  1 
ATOM   5553  C  C   . PHE   B 2 497  ? 137.765 122.104 107.479 1.00 42.02  ? 497  PHE   A C   1 
ATOM   5554  O  O   . PHE   B 2 497  ? 138.378 121.257 106.820 1.00 50.18  ? 497  PHE   A O   1 
ATOM   5555  C  CB  . PHE   B 2 497  ? 137.349 121.721 109.906 1.00 39.55  ? 497  PHE   A CB  1 
ATOM   5556  C  CG  . PHE   B 2 497  ? 137.879 121.760 111.307 1.00 36.20  ? 497  PHE   A CG  1 
ATOM   5557  C  CD1 . PHE   B 2 497  ? 139.207 122.047 111.558 1.00 43.64  ? 497  PHE   A CD1 1 
ATOM   5558  C  CD2 . PHE   B 2 497  ? 137.043 121.500 112.375 1.00 33.54  ? 497  PHE   A CD2 1 
ATOM   5559  C  CE1 . PHE   B 2 497  ? 139.686 122.078 112.850 1.00 46.50  ? 497  PHE   A CE1 1 
ATOM   5560  C  CE2 . PHE   B 2 497  ? 137.516 121.529 113.664 1.00 40.71  ? 497  PHE   A CE2 1 
ATOM   5561  C  CZ  . PHE   B 2 497  ? 138.838 121.817 113.903 1.00 46.02  ? 497  PHE   A CZ  1 
ATOM   5562  N  N   . ILE   B 2 498  ? 136.681 122.727 107.011 1.00 45.23  ? 498  ILE   A N   1 
ATOM   5563  C  CA  . ILE   B 2 498  ? 136.240 122.526 105.633 1.00 39.04  ? 498  ILE   A CA  1 
ATOM   5564  C  C   . ILE   B 2 498  ? 137.338 122.934 104.660 1.00 41.26  ? 498  ILE   A C   1 
ATOM   5565  O  O   . ILE   B 2 498  ? 137.589 122.251 103.659 1.00 46.73  ? 498  ILE   A O   1 
ATOM   5566  C  CB  . ILE   B 2 498  ? 134.934 123.299 105.371 1.00 39.14  ? 498  ILE   A CB  1 
ATOM   5567  C  CG1 . ILE   B 2 498  ? 133.782 122.675 106.158 1.00 46.18  ? 498  ILE   A CG1 1 
ATOM   5568  C  CG2 . ILE   B 2 498  ? 134.613 123.325 103.893 1.00 39.87  ? 498  ILE   A CG2 1 
ATOM   5569  C  CD1 . ILE   B 2 498  ? 132.461 123.375 105.969 1.00 46.13  ? 498  ILE   A CD1 1 
ATOM   5570  N  N   . TYR   B 2 499  ? 138.015 124.047 104.942 1.00 42.50  ? 499  TYR   A N   1 
ATOM   5571  C  CA  . TYR   B 2 499  ? 139.082 124.512 104.061 1.00 40.19  ? 499  TYR   A CA  1 
ATOM   5572  C  C   . TYR   B 2 499  ? 140.275 123.564 104.073 1.00 42.35  ? 499  TYR   A C   1 
ATOM   5573  O  O   . TYR   B 2 499  ? 140.891 123.320 103.029 1.00 49.18  ? 499  TYR   A O   1 
ATOM   5574  C  CB  . TYR   B 2 499  ? 139.510 125.921 104.466 1.00 45.53  ? 499  TYR   A CB  1 
ATOM   5575  C  CG  . TYR   B 2 499  ? 140.613 126.509 103.619 1.00 41.39  ? 499  TYR   A CG  1 
ATOM   5576  C  CD1 . TYR   B 2 499  ? 140.357 126.972 102.339 1.00 44.42  ? 499  TYR   A CD1 1 
ATOM   5577  C  CD2 . TYR   B 2 499  ? 141.906 126.617 104.107 1.00 44.25  ? 499  TYR   A CD2 1 
ATOM   5578  C  CE1 . TYR   B 2 499  ? 141.360 127.514 101.565 1.00 46.59  ? 499  TYR   A CE1 1 
ATOM   5579  C  CE2 . TYR   B 2 499  ? 142.914 127.158 103.341 1.00 45.93  ? 499  TYR   A CE2 1 
ATOM   5580  C  CZ  . TYR   B 2 499  ? 142.636 127.605 102.072 1.00 48.20  ? 499  TYR   A CZ  1 
ATOM   5581  O  OH  . TYR   B 2 499  ? 143.640 128.147 101.305 1.00 52.36  ? 499  TYR   A OH  1 
ATOM   5582  N  N   . TRP   B 2 500  ? 140.615 123.019 105.238 1.00 52.08  ? 500  TRP   A N   1 
ATOM   5583  C  CA  . TRP   B 2 500  ? 141.819 122.210 105.387 1.00 43.99  ? 500  TRP   A CA  1 
ATOM   5584  C  C   . TRP   B 2 500  ? 141.613 120.743 105.037 1.00 45.22  ? 500  TRP   A C   1 
ATOM   5585  O  O   . TRP   B 2 500  ? 142.578 119.975 105.096 1.00 49.07  ? 500  TRP   A O   1 
ATOM   5586  C  CB  . TRP   B 2 500  ? 142.350 122.319 106.818 1.00 41.86  ? 500  TRP   A CB  1 
ATOM   5587  C  CG  . TRP   B 2 500  ? 143.083 123.592 107.094 1.00 43.89  ? 500  TRP   A CG  1 
ATOM   5588  C  CD1 . TRP   B 2 500  ? 143.851 124.300 106.220 1.00 43.36  ? 500  TRP   A CD1 1 
ATOM   5589  C  CD2 . TRP   B 2 500  ? 143.112 124.313 108.329 1.00 51.67  ? 500  TRP   A CD2 1 
ATOM   5590  N  NE1 . TRP   B 2 500  ? 144.360 125.416 106.833 1.00 47.99  ? 500  TRP   A NE1 1 
ATOM   5591  C  CE2 . TRP   B 2 500  ? 143.920 125.448 108.130 1.00 52.30  ? 500  TRP   A CE2 1 
ATOM   5592  C  CE3 . TRP   B 2 500  ? 142.533 124.109 109.586 1.00 52.98  ? 500  TRP   A CE3 1 
ATOM   5593  C  CZ2 . TRP   B 2 500  ? 144.165 126.375 109.140 1.00 54.22  ? 500  TRP   A CZ2 1 
ATOM   5594  C  CZ3 . TRP   B 2 500  ? 142.777 125.030 110.587 1.00 51.45  ? 500  TRP   A CZ3 1 
ATOM   5595  C  CH2 . TRP   B 2 500  ? 143.586 126.149 110.358 1.00 55.30  ? 500  TRP   A CH2 1 
ATOM   5596  N  N   . ASP   B 2 501  ? 140.400 120.332 104.679 1.00 55.61  ? 501  ASP   A N   1 
ATOM   5597  C  CA  . ASP   B 2 501  ? 140.163 118.940 104.325 1.00 49.80  ? 501  ASP   A CA  1 
ATOM   5598  C  C   . ASP   B 2 501  ? 140.839 118.621 102.998 1.00 54.40  ? 501  ASP   A C   1 
ATOM   5599  O  O   . ASP   B 2 501  ? 140.602 119.293 101.991 1.00 64.13  ? 501  ASP   A O   1 
ATOM   5600  C  CB  . ASP   B 2 501  ? 138.664 118.663 104.241 1.00 45.25  ? 501  ASP   A CB  1 
ATOM   5601  C  CG  . ASP   B 2 501  ? 138.335 117.184 104.287 1.00 56.82  ? 501  ASP   A CG  1 
ATOM   5602  O  OD1 . ASP   B 2 501  ? 139.211 116.357 103.955 1.00 62.03  ? 501  ASP   A OD1 1 
ATOM   5603  O  OD2 . ASP   B 2 501  ? 137.192 116.844 104.655 1.00 63.41  ? 501  ASP   A OD2 1 
ATOM   5604  N  N   . ARG   B 2 502  ? 141.684 117.592 102.999 1.00 56.79  ? 502  ARG   A N   1 
ATOM   5605  C  CA  . ARG   B 2 502  ? 142.432 117.215 101.809 1.00 52.91  ? 502  ARG   A CA  1 
ATOM   5606  C  C   . ARG   B 2 502  ? 141.654 116.297 100.877 1.00 58.18  ? 502  ARG   A C   1 
ATOM   5607  O  O   . ARG   B 2 502  ? 142.103 116.063 99.750  1.00 61.12  ? 502  ARG   A O   1 
ATOM   5608  C  CB  . ARG   B 2 502  ? 143.749 116.540 102.201 1.00 55.34  ? 502  ARG   A CB  1 
ATOM   5609  C  CG  . ARG   B 2 502  ? 143.586 115.165 102.819 1.00 62.41  ? 502  ARG   A CG  1 
ATOM   5610  C  CD  . ARG   B 2 502  ? 144.935 114.516 103.081 1.00 61.63  ? 502  ARG   A CD  1 
ATOM   5611  N  NE  . ARG   B 2 502  ? 144.796 113.150 103.572 1.00 66.53  ? 502  ARG   A NE  1 
ATOM   5612  C  CZ  . ARG   B 2 502  ? 144.770 112.075 102.796 1.00 67.83  ? 502  ARG   A CZ  1 
ATOM   5613  N  NH1 . ARG   B 2 502  ? 144.874 112.168 101.481 1.00 63.90  ? 502  ARG   A NH1 1 
ATOM   5614  N  NH2 . ARG   B 2 502  ? 144.636 110.875 103.355 1.00 64.29  ? 502  ARG   A NH2 1 
ATOM   5615  N  N   . ASP   B 2 503  ? 140.514 115.770 101.312 1.00 58.05  ? 503  ASP   A N   1 
ATOM   5616  C  CA  . ASP   B 2 503  ? 139.679 114.938 100.459 1.00 53.19  ? 503  ASP   A CA  1 
ATOM   5617  C  C   . ASP   B 2 503  ? 138.725 115.746 99.593  1.00 55.24  ? 503  ASP   A C   1 
ATOM   5618  O  O   . ASP   B 2 503  ? 138.095 115.177 98.696  1.00 61.34  ? 503  ASP   A O   1 
ATOM   5619  C  CB  . ASP   B 2 503  ? 138.879 113.946 101.307 1.00 55.32  ? 503  ASP   A CB  1 
ATOM   5620  C  CG  . ASP   B 2 503  ? 139.764 112.968 102.052 1.00 66.88  ? 503  ASP   A CG  1 
ATOM   5621  O  OD1 . ASP   B 2 503  ? 141.000 113.029 101.876 1.00 68.00  ? 503  ASP   A OD1 1 
ATOM   5622  O  OD2 . ASP   B 2 503  ? 139.225 112.139 102.813 1.00 68.72  ? 503  ASP   A OD2 1 
ATOM   5623  N  N   . ILE   B 2 504  ? 138.601 117.047 99.839  1.00 45.12  ? 504  ILE   A N   1 
ATOM   5624  C  CA  . ILE   B 2 504  ? 137.788 117.919 99.002  1.00 43.44  ? 504  ILE   A CA  1 
ATOM   5625  C  C   . ILE   B 2 504  ? 138.692 118.991 98.411  1.00 46.94  ? 504  ILE   A C   1 
ATOM   5626  O  O   . ILE   B 2 504  ? 138.273 120.134 98.200  1.00 58.22  ? 504  ILE   A O   1 
ATOM   5627  C  CB  . ILE   B 2 504  ? 136.612 118.530 99.786  1.00 42.10  ? 504  ILE   A CB  1 
ATOM   5628  C  CG1 . ILE   B 2 504  ? 137.104 119.277 101.023 1.00 49.05  ? 504  ILE   A CG1 1 
ATOM   5629  C  CG2 . ILE   B 2 504  ? 135.628 117.450 100.186 1.00 47.24  ? 504  ILE   A CG2 1 
ATOM   5630  C  CD1 . ILE   B 2 504  ? 135.986 119.845 101.862 1.00 54.20  ? 504  ILE   A CD1 1 
ATOM   5631  N  N   . LYS   B 2 505  ? 139.939 118.620 98.144  1.00 42.46  ? 505  LYS   A N   1 
ATOM   5632  C  CA  . LYS   B 2 505  ? 140.923 119.492 97.520  1.00 42.15  ? 505  LYS   A CA  1 
ATOM   5633  C  C   . LYS   B 2 505  ? 141.254 118.954 96.135  1.00 53.00  ? 505  LYS   A C   1 
ATOM   5634  O  O   . LYS   B 2 505  ? 141.583 117.773 95.987  1.00 58.06  ? 505  LYS   A O   1 
ATOM   5635  C  CB  . LYS   B 2 505  ? 142.187 119.579 98.377  1.00 44.54  ? 505  LYS   A CB  1 
ATOM   5636  C  CG  . LYS   B 2 505  ? 143.230 120.539 97.856  1.00 48.74  ? 505  LYS   A CG  1 
ATOM   5637  C  CD  . LYS   B 2 505  ? 144.441 120.609 98.775  1.00 53.13  ? 505  LYS   A CD  1 
ATOM   5638  C  CE  . LYS   B 2 505  ? 145.400 119.447 98.556  1.00 53.35  ? 505  LYS   A CE  1 
ATOM   5639  N  NZ  . LYS   B 2 505  ? 144.933 118.165 99.157  1.00 54.37  ? 505  LYS   A NZ  1 
ATOM   5640  N  N   . TYR   B 2 506  ? 141.167 119.817 95.129  1.00 52.73  ? 506  TYR   A N   1 
ATOM   5641  C  CA  . TYR   B 2 506  ? 141.329 119.428 93.734  1.00 49.42  ? 506  TYR   A CA  1 
ATOM   5642  C  C   . TYR   B 2 506  ? 142.659 119.946 93.207  1.00 55.21  ? 506  TYR   A C   1 
ATOM   5643  O  O   . TYR   B 2 506  ? 143.021 121.101 93.452  1.00 61.65  ? 506  TYR   A O   1 
ATOM   5644  C  CB  . TYR   B 2 506  ? 140.174 119.966 92.888  1.00 54.93  ? 506  TYR   A CB  1 
ATOM   5645  C  CG  . TYR   B 2 506  ? 140.128 119.420 91.482  1.00 52.36  ? 506  TYR   A CG  1 
ATOM   5646  C  CD1 . TYR   B 2 506  ? 139.996 118.060 91.250  1.00 53.07  ? 506  TYR   A CD1 1 
ATOM   5647  C  CD2 . TYR   B 2 506  ? 140.194 120.267 90.386  1.00 51.66  ? 506  TYR   A CD2 1 
ATOM   5648  C  CE1 . TYR   B 2 506  ? 139.947 117.557 89.969  1.00 53.96  ? 506  TYR   A CE1 1 
ATOM   5649  C  CE2 . TYR   B 2 506  ? 140.145 119.772 89.100  1.00 53.55  ? 506  TYR   A CE2 1 
ATOM   5650  C  CZ  . TYR   B 2 506  ? 140.022 118.417 88.897  1.00 55.05  ? 506  TYR   A CZ  1 
ATOM   5651  O  OH  . TYR   B 2 506  ? 139.972 117.916 87.617  1.00 58.44  ? 506  TYR   A OH  1 
ATOM   5652  N  N   . LYS   B 2 507  ? 143.380 119.093 92.483  1.00 61.56  ? 507  LYS   A N   1 
ATOM   5653  C  CA  . LYS   B 2 507  ? 144.690 119.430 91.927  1.00 59.22  ? 507  LYS   A CA  1 
ATOM   5654  C  C   . LYS   B 2 507  ? 144.775 118.865 90.513  1.00 62.83  ? 507  LYS   A C   1 
ATOM   5655  O  O   . LYS   B 2 507  ? 145.017 117.669 90.332  1.00 68.77  ? 507  LYS   A O   1 
ATOM   5656  C  CB  . LYS   B 2 507  ? 145.812 118.890 92.808  1.00 64.44  ? 507  LYS   A CB  1 
ATOM   5657  C  CG  . LYS   B 2 507  ? 147.208 119.262 92.337  1.00 66.86  ? 507  LYS   A CG  1 
ATOM   5658  C  CD  . LYS   B 2 507  ? 148.269 118.714 93.277  1.00 67.25  ? 507  LYS   A CD  1 
ATOM   5659  C  CE  . LYS   B 2 507  ? 149.665 119.137 92.847  1.00 69.14  ? 507  LYS   A CE  1 
ATOM   5660  N  NZ  . LYS   B 2 507  ? 149.997 118.652 91.478  1.00 68.43  ? 507  LYS   A NZ  1 
ATOM   5661  N  N   . LYS   B 2 508  ? 144.576 119.723 89.516  1.00 67.97  ? 508  LYS   A N   1 
ATOM   5662  C  CA  . LYS   B 2 508  ? 144.672 119.330 88.116  1.00 66.11  ? 508  LYS   A CA  1 
ATOM   5663  C  C   . LYS   B 2 508  ? 145.522 120.343 87.367  1.00 65.84  ? 508  LYS   A C   1 
ATOM   5664  O  O   . LYS   B 2 508  ? 145.345 121.551 87.544  1.00 69.42  ? 508  LYS   A O   1 
ATOM   5665  C  CB  . LYS   B 2 508  ? 143.289 119.229 87.466  1.00 68.20  ? 508  LYS   A CB  1 
ATOM   5666  C  CG  . LYS   B 2 508  ? 143.328 118.896 85.983  1.00 70.65  ? 508  LYS   A CG  1 
ATOM   5667  C  CD  . LYS   B 2 508  ? 141.959 119.042 85.343  1.00 71.09  ? 508  LYS   A CD  1 
ATOM   5668  C  CE  . LYS   B 2 508  ? 141.453 120.471 85.446  1.00 69.93  ? 508  LYS   A CE  1 
ATOM   5669  N  NZ  . LYS   B 2 508  ? 142.367 121.433 84.771  1.00 69.45  ? 508  LYS   A NZ  1 
ATOM   5670  N  N   . ASP   B 2 509  ? 146.437 119.846 86.534  1.00 71.36  ? 509  ASP   A N   1 
ATOM   5671  C  CA  . ASP   B 2 509  ? 147.289 120.684 85.689  1.00 75.71  ? 509  ASP   A CA  1 
ATOM   5672  C  C   . ASP   B 2 509  ? 148.103 121.685 86.505  1.00 76.32  ? 509  ASP   A C   1 
ATOM   5673  O  O   . ASP   B 2 509  ? 148.345 122.810 86.064  1.00 79.68  ? 509  ASP   A O   1 
ATOM   5674  C  CB  . ASP   B 2 509  ? 146.469 121.411 84.619  1.00 79.31  ? 509  ASP   A CB  1 
ATOM   5675  C  CG  . ASP   B 2 509  ? 145.815 120.458 83.638  1.00 82.43  ? 509  ASP   A CG  1 
ATOM   5676  O  OD1 . ASP   B 2 509  ? 146.003 119.232 83.784  1.00 82.30  ? 509  ASP   A OD1 1 
ATOM   5677  O  OD2 . ASP   B 2 509  ? 145.115 120.934 82.720  1.00 81.59  ? 509  ASP   A OD2 1 
ATOM   5678  N  N   . GLY   B 2 510  ? 148.529 121.285 87.700  1.00 70.04  ? 510  GLY   A N   1 
ATOM   5679  C  CA  . GLY   B 2 510  ? 149.442 122.091 88.483  1.00 67.76  ? 510  GLY   A CA  1 
ATOM   5680  C  C   . GLY   B 2 510  ? 148.820 123.198 89.302  1.00 69.97  ? 510  GLY   A C   1 
ATOM   5681  O  O   . GLY   B 2 510  ? 149.560 123.967 89.926  1.00 74.98  ? 510  GLY   A O   1 
ATOM   5682  N  N   . VAL   B 2 511  ? 147.495 123.313 89.327  1.00 67.75  ? 511  VAL   A N   1 
ATOM   5683  C  CA  . VAL   B 2 511  ? 146.810 124.317 90.133  1.00 66.17  ? 511  VAL   A CA  1 
ATOM   5684  C  C   . VAL   B 2 511  ? 145.921 123.601 91.139  1.00 64.83  ? 511  VAL   A C   1 
ATOM   5685  O  O   . VAL   B 2 511  ? 145.214 122.648 90.789  1.00 71.95  ? 511  VAL   A O   1 
ATOM   5686  C  CB  . VAL   B 2 511  ? 145.999 125.300 89.266  1.00 69.38  ? 511  VAL   A CB  1 
ATOM   5687  C  CG1 . VAL   B 2 511  ? 146.936 126.171 88.442  1.00 68.86  ? 511  VAL   A CG1 1 
ATOM   5688  C  CG2 . VAL   B 2 511  ? 145.030 124.564 88.359  1.00 68.61  ? 511  VAL   A CG2 1 
ATOM   5689  N  N   . THR   B 2 512  ? 145.973 124.048 92.390  1.00 54.99  ? 512  THR   A N   1 
ATOM   5690  C  CA  . THR   B 2 512  ? 145.255 123.423 93.491  1.00 49.64  ? 512  THR   A CA  1 
ATOM   5691  C  C   . THR   B 2 512  ? 144.108 124.323 93.926  1.00 55.44  ? 512  THR   A C   1 
ATOM   5692  O  O   . THR   B 2 512  ? 144.303 125.525 94.135  1.00 65.99  ? 512  THR   A O   1 
ATOM   5693  C  CB  . THR   B 2 512  ? 146.192 123.153 94.668  1.00 55.78  ? 512  THR   A CB  1 
ATOM   5694  O  OG1 . THR   B 2 512  ? 147.227 122.252 94.258  1.00 64.93  ? 512  THR   A OG1 1 
ATOM   5695  C  CG2 . THR   B 2 512  ? 145.430 122.541 95.822  1.00 57.26  ? 512  THR   A CG2 1 
ATOM   5696  N  N   . THR   B 2 513  ? 142.919 123.743 94.059  1.00 45.52  ? 513  THR   A N   1 
ATOM   5697  C  CA  . THR   B 2 513  ? 141.707 124.485 94.400  1.00 45.93  ? 513  THR   A CA  1 
ATOM   5698  C  C   . THR   B 2 513  ? 141.078 123.855 95.638  1.00 48.32  ? 513  THR   A C   1 
ATOM   5699  O  O   . THR   B 2 513  ? 140.347 122.865 95.537  1.00 57.24  ? 513  THR   A O   1 
ATOM   5700  C  CB  . THR   B 2 513  ? 140.729 124.498 93.229  1.00 47.00  ? 513  THR   A CB  1 
ATOM   5701  O  OG1 . THR   B 2 513  ? 141.373 125.047 92.074  1.00 48.13  ? 513  THR   A OG1 1 
ATOM   5702  C  CG2 . THR   B 2 513  ? 139.514 125.341 93.565  1.00 48.97  ? 513  THR   A CG2 1 
ATOM   5703  N  N   . ARG   B 2 514  ? 141.360 124.428 96.802  1.00 41.01  ? 514  ARG   A N   1 
ATOM   5704  C  CA  . ARG   B 2 514  ? 140.750 123.967 98.036  1.00 41.83  ? 514  ARG   A CA  1 
ATOM   5705  C  C   . ARG   B 2 514  ? 139.291 124.401 98.107  1.00 47.68  ? 514  ARG   A C   1 
ATOM   5706  O  O   . ARG   B 2 514  ? 138.863 125.349 97.444  1.00 58.65  ? 514  ARG   A O   1 
ATOM   5707  C  CB  . ARG   B 2 514  ? 141.510 124.501 99.249  1.00 48.60  ? 514  ARG   A CB  1 
ATOM   5708  C  CG  . ARG   B 2 514  ? 142.901 123.924 99.419  1.00 52.38  ? 514  ARG   A CG  1 
ATOM   5709  C  CD  . ARG   B 2 514  ? 143.595 124.514 100.632 1.00 48.59  ? 514  ARG   A CD  1 
ATOM   5710  N  NE  . ARG   B 2 514  ? 144.837 123.818 100.942 1.00 48.02  ? 514  ARG   A NE  1 
ATOM   5711  C  CZ  . ARG   B 2 514  ? 144.930 122.793 101.778 1.00 53.71  ? 514  ARG   A CZ  1 
ATOM   5712  N  NH1 . ARG   B 2 514  ? 143.870 122.322 102.413 1.00 53.76  ? 514  ARG   A NH1 1 
ATOM   5713  N  NH2 . ARG   B 2 514  ? 146.115 122.226 101.980 1.00 54.64  ? 514  ARG   A NH2 1 
ATOM   5714  N  N   . THR   B 2 515  ? 138.524 123.692 98.927  1.00 37.76  ? 515  THR   A N   1 
ATOM   5715  C  CA  . THR   B 2 515  ? 137.132 124.048 99.161  1.00 34.86  ? 515  THR   A CA  1 
ATOM   5716  C  C   . THR   B 2 515  ? 137.074 125.187 100.169 1.00 48.20  ? 515  THR   A C   1 
ATOM   5717  O  O   . THR   B 2 515  ? 137.457 125.017 101.331 1.00 54.34  ? 515  THR   A O   1 
ATOM   5718  C  CB  . THR   B 2 515  ? 136.342 122.843 99.661  1.00 37.17  ? 515  THR   A CB  1 
ATOM   5719  O  OG1 . THR   B 2 515  ? 136.267 121.857 98.625  1.00 43.17  ? 515  THR   A OG1 1 
ATOM   5720  C  CG2 . THR   B 2 515  ? 134.940 123.256 100.062 1.00 46.49  ? 515  THR   A CG2 1 
ATOM   5721  N  N   . THR   B 2 516  ? 136.599 126.345 99.725  1.00 44.82  ? 516  THR   A N   1 
ATOM   5722  C  CA  . THR   B 2 516  ? 136.603 127.557 100.526 1.00 44.36  ? 516  THR   A CA  1 
ATOM   5723  C  C   . THR   B 2 516  ? 135.193 127.882 100.992 1.00 47.62  ? 516  THR   A C   1 
ATOM   5724  O  O   . THR   B 2 516  ? 134.247 127.866 100.199 1.00 58.23  ? 516  THR   A O   1 
ATOM   5725  C  CB  . THR   B 2 516  ? 137.170 128.736 99.732  1.00 44.65  ? 516  THR   A CB  1 
ATOM   5726  O  OG1 . THR   B 2 516  ? 136.278 129.068 98.664  1.00 49.84  ? 516  THR   A OG1 1 
ATOM   5727  C  CG2 . THR   B 2 516  ? 138.526 128.377 99.152  1.00 47.23  ? 516  THR   A CG2 1 
ATOM   5728  N  N   . ALA   B 2 517  ? 135.059 128.179 102.280 1.00 41.51  ? 517  ALA   A N   1 
ATOM   5729  C  CA  . ALA   B 2 517  ? 133.782 128.555 102.876 1.00 40.75  ? 517  ALA   A CA  1 
ATOM   5730  C  C   . ALA   B 2 517  ? 133.667 130.073 102.818 1.00 44.67  ? 517  ALA   A C   1 
ATOM   5731  O  O   . ALA   B 2 517  ? 134.261 130.784 103.632 1.00 56.91  ? 517  ALA   A O   1 
ATOM   5732  C  CB  . ALA   B 2 517  ? 133.674 128.036 104.306 1.00 46.94  ? 517  ALA   A CB  1 
ATOM   5733  N  N   . ARG   B 2 518  ? 132.906 130.568 101.841 1.00 44.46  ? 518  ARG   A N   1 
ATOM   5734  C  CA  . ARG   B 2 518  ? 132.706 132.006 101.709 1.00 43.74  ? 518  ARG   A CA  1 
ATOM   5735  C  C   . ARG   B 2 518  ? 131.955 132.569 102.907 1.00 47.38  ? 518  ARG   A C   1 
ATOM   5736  O  O   . ARG   B 2 518  ? 132.267 133.665 103.383 1.00 56.22  ? 518  ARG   A O   1 
ATOM   5737  C  CB  . ARG   B 2 518  ? 131.950 132.312 100.418 1.00 54.11  ? 518  ARG   A CB  1 
ATOM   5738  C  CG  . ARG   B 2 518  ? 132.434 131.532 99.207  1.00 54.94  ? 518  ARG   A CG  1 
ATOM   5739  C  CD  . ARG   B 2 518  ? 133.669 132.161 98.593  1.00 51.41  ? 518  ARG   A CD  1 
ATOM   5740  N  NE  . ARG   B 2 518  ? 133.404 133.508 98.108  1.00 49.81  ? 518  ARG   A NE  1 
ATOM   5741  C  CZ  . ARG   B 2 518  ? 134.261 134.229 97.400  1.00 56.06  ? 518  ARG   A CZ  1 
ATOM   5742  N  NH1 . ARG   B 2 518  ? 135.451 133.756 97.067  1.00 57.16  ? 518  ARG   A NH1 1 
ATOM   5743  N  NH2 . ARG   B 2 518  ? 133.916 135.454 97.015  1.00 58.82  ? 518  ARG   A NH2 1 
ATOM   5744  N  N   . SER   B 2 519  ? 130.954 131.844 103.395 1.00 46.47  ? 519  SER   A N   1 
ATOM   5745  C  CA  . SER   B 2 519  ? 130.207 132.224 104.586 1.00 50.93  ? 519  SER   A CA  1 
ATOM   5746  C  C   . SER   B 2 519  ? 130.684 131.367 105.750 1.00 50.26  ? 519  SER   A C   1 
ATOM   5747  O  O   . SER   B 2 519  ? 130.552 130.140 105.714 1.00 50.95  ? 519  SER   A O   1 
ATOM   5748  C  CB  . SER   B 2 519  ? 128.705 132.051 104.365 1.00 51.91  ? 519  SER   A CB  1 
ATOM   5749  O  OG  . SER   B 2 519  ? 127.977 132.384 105.533 1.00 54.91  ? 519  SER   A OG  1 
ATOM   5750  N  N   . TRP   B 2 520  ? 131.235 132.011 106.778 1.00 46.91  ? 520  TRP   A N   1 
ATOM   5751  C  CA  . TRP   B 2 520  ? 131.828 131.272 107.884 1.00 42.68  ? 520  TRP   A CA  1 
ATOM   5752  C  C   . TRP   B 2 520  ? 130.789 130.693 108.832 1.00 49.95  ? 520  TRP   A C   1 
ATOM   5753  O  O   . TRP   B 2 520  ? 131.119 129.800 109.619 1.00 59.76  ? 520  TRP   A O   1 
ATOM   5754  C  CB  . TRP   B 2 520  ? 132.806 132.164 108.642 1.00 45.85  ? 520  TRP   A CB  1 
ATOM   5755  C  CG  . TRP   B 2 520  ? 134.013 132.480 107.829 1.00 45.45  ? 520  TRP   A CG  1 
ATOM   5756  C  CD1 . TRP   B 2 520  ? 134.338 131.953 106.618 1.00 43.00  ? 520  TRP   A CD1 1 
ATOM   5757  C  CD2 . TRP   B 2 520  ? 135.054 133.405 108.156 1.00 45.64  ? 520  TRP   A CD2 1 
ATOM   5758  N  NE1 . TRP   B 2 520  ? 135.518 132.486 106.170 1.00 44.67  ? 520  TRP   A NE1 1 
ATOM   5759  C  CE2 . TRP   B 2 520  ? 135.979 133.381 107.098 1.00 46.73  ? 520  TRP   A CE2 1 
ATOM   5760  C  CE3 . TRP   B 2 520  ? 135.296 134.248 109.243 1.00 50.96  ? 520  TRP   A CE3 1 
ATOM   5761  C  CZ2 . TRP   B 2 520  ? 137.126 134.165 107.093 1.00 50.39  ? 520  TRP   A CZ2 1 
ATOM   5762  C  CZ3 . TRP   B 2 520  ? 136.434 135.027 109.235 1.00 54.88  ? 520  TRP   A CZ3 1 
ATOM   5763  C  CH2 . TRP   B 2 520  ? 137.335 134.980 108.168 1.00 52.87  ? 520  TRP   A CH2 1 
ATOM   5764  N  N   . ASN   B 2 521  ? 129.553 131.172 108.776 1.00 49.16  ? 521  ASN   A N   1 
ATOM   5765  C  CA  . ASN   B 2 521  ? 128.441 130.470 109.399 1.00 43.16  ? 521  ASN   A CA  1 
ATOM   5766  C  C   . ASN   B 2 521  ? 127.913 129.439 108.402 1.00 52.10  ? 521  ASN   A C   1 
ATOM   5767  O  O   . ASN   B 2 521  ? 128.609 129.039 107.465 1.00 55.20  ? 521  ASN   A O   1 
ATOM   5768  C  CB  . ASN   B 2 521  ? 127.374 131.457 109.861 1.00 44.65  ? 521  ASN   A CB  1 
ATOM   5769  C  CG  . ASN   B 2 521  ? 127.052 132.503 108.818 1.00 53.87  ? 521  ASN   A CG  1 
ATOM   5770  O  OD1 . ASN   B 2 521  ? 126.187 132.303 107.967 1.00 55.36  ? 521  ASN   A OD1 1 
ATOM   5771  N  ND2 . ASN   B 2 521  ? 127.744 133.633 108.882 1.00 52.22  ? 521  ASN   A ND2 1 
ATOM   5772  N  N   . LEU   B 2 522  ? 126.687 128.965 108.616 1.00 50.58  ? 522  LEU   A N   1 
ATOM   5773  C  CA  . LEU   B 2 522  ? 125.992 128.034 107.731 1.00 47.29  ? 522  LEU   A CA  1 
ATOM   5774  C  C   . LEU   B 2 522  ? 126.668 126.674 107.640 1.00 47.59  ? 522  LEU   A C   1 
ATOM   5775  O  O   . LEU   B 2 522  ? 126.287 125.862 106.788 1.00 55.24  ? 522  LEU   A O   1 
ATOM   5776  C  CB  . LEU   B 2 522  ? 125.829 128.604 106.317 1.00 47.19  ? 522  LEU   A CB  1 
ATOM   5777  C  CG  . LEU   B 2 522  ? 124.979 129.861 106.152 1.00 51.50  ? 522  LEU   A CG  1 
ATOM   5778  C  CD1 . LEU   B 2 522  ? 125.011 130.335 104.714 1.00 50.75  ? 522  LEU   A CD1 1 
ATOM   5779  C  CD2 . LEU   B 2 522  ? 123.554 129.599 106.595 1.00 51.93  ? 522  LEU   A CD2 1 
ATOM   5780  N  N   . SER   B 2 523  ? 127.665 126.398 108.482 1.00 45.11  ? 523  SER   A N   1 
ATOM   5781  C  CA  . SER   B 2 523  ? 128.291 125.080 108.471 1.00 38.17  ? 523  SER   A CA  1 
ATOM   5782  C  C   . SER   B 2 523  ? 127.313 124.005 108.918 1.00 45.25  ? 523  SER   A C   1 
ATOM   5783  O  O   . SER   B 2 523  ? 127.242 122.930 108.312 1.00 57.92  ? 523  SER   A O   1 
ATOM   5784  C  CB  . SER   B 2 523  ? 129.534 125.081 109.358 1.00 47.45  ? 523  SER   A CB  1 
ATOM   5785  O  OG  . SER   B 2 523  ? 129.204 125.393 110.699 1.00 50.58  ? 523  SER   A OG  1 
ATOM   5786  N  N   . ASP   B 2 524  ? 126.545 124.279 109.972 1.00 49.34  ? 524  ASP   A N   1 
ATOM   5787  C  CA  . ASP   B 2 524  ? 125.523 123.349 110.431 1.00 49.23  ? 524  ASP   A CA  1 
ATOM   5788  C  C   . ASP   B 2 524  ? 124.344 123.260 109.477 1.00 54.69  ? 524  ASP   A C   1 
ATOM   5789  O  O   . ASP   B 2 524  ? 123.584 122.289 109.546 1.00 61.33  ? 524  ASP   A O   1 
ATOM   5790  C  CB  . ASP   B 2 524  ? 125.042 123.758 111.823 1.00 54.10  ? 524  ASP   A CB  1 
ATOM   5791  C  CG  . ASP   B 2 524  ? 124.816 125.251 111.944 1.00 63.00  ? 524  ASP   A CG  1 
ATOM   5792  O  OD1 . ASP   B 2 524  ? 124.871 125.947 110.908 1.00 64.27  ? 524  ASP   A OD1 1 
ATOM   5793  O  OD2 . ASP   B 2 524  ? 124.595 125.731 113.074 1.00 61.20  ? 524  ASP   A OD2 1 
ATOM   5794  N  N   . ASP   B 2 525  ? 124.174 124.245 108.595 1.00 55.71  ? 525  ASP   A N   1 
ATOM   5795  C  CA  . ASP   B 2 525  ? 123.113 124.190 107.600 1.00 49.28  ? 525  ASP   A CA  1 
ATOM   5796  C  C   . ASP   B 2 525  ? 123.342 123.080 106.584 1.00 47.89  ? 525  ASP   A C   1 
ATOM   5797  O  O   . ASP   B 2 525  ? 122.372 122.533 106.052 1.00 54.69  ? 525  ASP   A O   1 
ATOM   5798  C  CB  . ASP   B 2 525  ? 122.999 125.546 106.902 1.00 58.40  ? 525  ASP   A CB  1 
ATOM   5799  C  CG  . ASP   B 2 525  ? 121.666 125.746 106.214 1.00 64.23  ? 525  ASP   A CG  1 
ATOM   5800  O  OD1 . ASP   B 2 525  ? 121.304 124.919 105.353 1.00 68.17  ? 525  ASP   A OD1 1 
ATOM   5801  O  OD2 . ASP   B 2 525  ? 120.979 126.738 106.533 1.00 61.45  ? 525  ASP   A OD2 1 
ATOM   5802  N  N   . LEU   B 2 526  ? 124.601 122.729 106.313 1.00 48.19  ? 526  LEU   A N   1 
ATOM   5803  C  CA  . LEU   B 2 526  ? 124.904 121.666 105.363 1.00 42.56  ? 526  LEU   A CA  1 
ATOM   5804  C  C   . LEU   B 2 526  ? 124.379 120.312 105.813 1.00 41.71  ? 526  LEU   A C   1 
ATOM   5805  O  O   . LEU   B 2 526  ? 124.219 119.416 104.979 1.00 47.88  ? 526  LEU   A O   1 
ATOM   5806  C  CB  . LEU   B 2 526  ? 126.412 121.577 105.139 1.00 43.76  ? 526  LEU   A CB  1 
ATOM   5807  C  CG  . LEU   B 2 526  ? 127.073 122.708 104.360 1.00 41.79  ? 526  LEU   A CG  1 
ATOM   5808  C  CD1 . LEU   B 2 526  ? 128.578 122.545 104.377 1.00 48.28  ? 526  LEU   A CD1 1 
ATOM   5809  C  CD2 . LEU   B 2 526  ? 126.557 122.730 102.940 1.00 46.31  ? 526  LEU   A CD2 1 
ATOM   5810  N  N   . GLY   B 2 527  ? 124.109 120.143 107.100 1.00 45.32  ? 527  GLY   A N   1 
ATOM   5811  C  CA  . GLY   B 2 527  ? 123.622 118.889 107.624 1.00 42.31  ? 527  GLY   A CA  1 
ATOM   5812  C  C   . GLY   B 2 527  ? 122.126 118.711 107.628 1.00 44.78  ? 527  GLY   A C   1 
ATOM   5813  O  O   . GLY   B 2 527  ? 121.638 117.723 108.179 1.00 56.28  ? 527  GLY   A O   1 
ATOM   5814  N  N   . GLN   B 2 528  ? 121.369 119.631 107.036 1.00 45.16  ? 528  GLN   A N   1 
ATOM   5815  C  CA  . GLN   B 2 528  ? 119.913 119.559 107.046 1.00 42.24  ? 528  GLN   A CA  1 
ATOM   5816  C  C   . GLN   B 2 528  ? 119.330 119.693 105.645 1.00 44.51  ? 528  GLN   A C   1 
ATOM   5817  O  O   . GLN   B 2 528  ? 118.182 120.107 105.483 1.00 54.85  ? 528  GLN   A O   1 
ATOM   5818  C  CB  . GLN   B 2 528  ? 119.331 120.626 107.969 1.00 48.51  ? 528  GLN   A CB  1 
ATOM   5819  C  CG  . GLN   B 2 528  ? 120.030 120.728 109.309 1.00 46.11  ? 528  GLN   A CG  1 
ATOM   5820  C  CD  . GLN   B 2 528  ? 119.371 121.722 110.230 1.00 51.75  ? 528  GLN   A CD  1 
ATOM   5821  O  OE1 . GLN   B 2 528  ? 118.150 121.742 110.366 1.00 53.66  ? 528  GLN   A OE1 1 
ATOM   5822  N  NE2 . GLN   B 2 528  ? 120.176 122.560 110.867 1.00 56.05  ? 528  GLN   A NE2 1 
ATOM   5823  N  N   . ILE   B 2 529  ? 120.104 119.334 104.624 1.00 37.84  ? 529  ILE   A N   1 
ATOM   5824  C  CA  . ILE   B 2 529  ? 119.674 119.556 103.250 1.00 34.61  ? 529  ILE   A CA  1 
ATOM   5825  C  C   . ILE   B 2 529  ? 118.673 118.484 102.845 1.00 40.44  ? 529  ILE   A C   1 
ATOM   5826  O  O   . ILE   B 2 529  ? 118.924 117.282 103.002 1.00 53.84  ? 529  ILE   A O   1 
ATOM   5827  C  CB  . ILE   B 2 529  ? 120.881 119.581 102.303 1.00 34.05  ? 529  ILE   A CB  1 
ATOM   5828  C  CG1 . ILE   B 2 529  ? 121.834 120.709 102.692 1.00 39.36  ? 529  ILE   A CG1 1 
ATOM   5829  C  CG2 . ILE   B 2 529  ? 120.427 119.746 100.867 1.00 46.42  ? 529  ILE   A CG2 1 
ATOM   5830  C  CD1 . ILE   B 2 529  ? 121.179 122.065 102.752 1.00 48.76  ? 529  ILE   A CD1 1 
ATOM   5831  N  N   . GLU   B 2 530  ? 117.528 118.919 102.324 1.00 45.11  ? 530  GLU   A N   1 
ATOM   5832  C  CA  . GLU   B 2 530  ? 116.514 118.020 101.803 1.00 45.03  ? 530  GLU   A CA  1 
ATOM   5833  C  C   . GLU   B 2 530  ? 116.313 118.131 100.302 1.00 53.09  ? 530  GLU   A C   1 
ATOM   5834  O  O   . GLU   B 2 530  ? 115.851 117.162 99.689  1.00 59.71  ? 530  GLU   A O   1 
ATOM   5835  C  CB  . GLU   B 2 530  ? 115.166 118.268 102.497 1.00 53.93  ? 530  GLU   A CB  1 
ATOM   5836  C  CG  . GLU   B 2 530  ? 115.228 118.194 104.010 1.00 61.56  ? 530  GLU   A CG  1 
ATOM   5837  C  CD  . GLU   B 2 530  ? 113.855 118.222 104.648 1.00 69.78  ? 530  GLU   A CD  1 
ATOM   5838  O  OE1 . GLU   B 2 530  ? 112.864 117.950 103.940 1.00 65.31  ? 530  GLU   A OE1 1 
ATOM   5839  O  OE2 . GLU   B 2 530  ? 113.767 118.516 105.859 1.00 67.42  ? 530  GLU   A OE2 1 
ATOM   5840  N  N   . TYR   B 2 531  ? 116.641 119.268 99.696  1.00 43.17  ? 531  TYR   A N   1 
ATOM   5841  C  CA  . TYR   B 2 531  ? 116.539 119.461 98.258  1.00 35.02  ? 531  TYR   A CA  1 
ATOM   5842  C  C   . TYR   B 2 531  ? 117.832 120.060 97.732  1.00 37.49  ? 531  TYR   A C   1 
ATOM   5843  O  O   . TYR   B 2 531  ? 118.380 120.992 98.328  1.00 48.36  ? 531  TYR   A O   1 
ATOM   5844  C  CB  . TYR   B 2 531  ? 115.366 120.373 97.898  1.00 35.08  ? 531  TYR   A CB  1 
ATOM   5845  C  CG  . TYR   B 2 531  ? 114.029 119.676 97.854  1.00 30.63  ? 531  TYR   A CG  1 
ATOM   5846  C  CD1 . TYR   B 2 531  ? 113.316 119.428 99.012  1.00 35.09  ? 531  TYR   A CD1 1 
ATOM   5847  C  CD2 . TYR   B 2 531  ? 113.479 119.273 96.649  1.00 41.32  ? 531  TYR   A CD2 1 
ATOM   5848  C  CE1 . TYR   B 2 531  ? 112.096 118.797 98.975  1.00 33.17  ? 531  TYR   A CE1 1 
ATOM   5849  C  CE2 . TYR   B 2 531  ? 112.259 118.641 96.602  1.00 44.75  ? 531  TYR   A CE2 1 
ATOM   5850  C  CZ  . TYR   B 2 531  ? 111.573 118.404 97.767  1.00 39.90  ? 531  TYR   A CZ  1 
ATOM   5851  O  OH  . TYR   B 2 531  ? 110.354 117.772 97.725  1.00 51.41  ? 531  TYR   A OH  1 
ATOM   5852  N  N   . ILE   B 2 532  ? 118.319 119.522 96.619  1.00 39.33  ? 532  ILE   A N   1 
ATOM   5853  C  CA  . ILE   B 2 532  ? 119.494 120.041 95.930  1.00 35.04  ? 532  ILE   A CA  1 
ATOM   5854  C  C   . ILE   B 2 532  ? 119.083 120.418 94.515  1.00 41.52  ? 532  ILE   A C   1 
ATOM   5855  O  O   . ILE   B 2 532  ? 118.587 119.572 93.761  1.00 48.60  ? 532  ILE   A O   1 
ATOM   5856  C  CB  . ILE   B 2 532  ? 120.647 119.027 95.912  1.00 37.78  ? 532  ILE   A CB  1 
ATOM   5857  C  CG1 . ILE   B 2 532  ? 121.253 118.882 97.306  1.00 46.82  ? 532  ILE   A CG1 1 
ATOM   5858  C  CG2 . ILE   B 2 532  ? 121.712 119.448 94.923  1.00 48.31  ? 532  ILE   A CG2 1 
ATOM   5859  C  CD1 . ILE   B 2 532  ? 122.423 117.936 97.363  1.00 48.74  ? 532  ILE   A CD1 1 
ATOM   5860  N  N   . PHE   B 2 533  ? 119.286 121.682 94.159  1.00 37.57  ? 533  PHE   A N   1 
ATOM   5861  C  CA  . PHE   B 2 533  ? 119.020 122.182 92.818  1.00 30.41  ? 533  PHE   A CA  1 
ATOM   5862  C  C   . PHE   B 2 533  ? 120.357 122.384 92.120  1.00 39.42  ? 533  PHE   A C   1 
ATOM   5863  O  O   . PHE   B 2 533  ? 121.184 123.179 92.576  1.00 51.96  ? 533  PHE   A O   1 
ATOM   5864  C  CB  . PHE   B 2 533  ? 118.231 123.489 92.864  1.00 33.20  ? 533  PHE   A CB  1 
ATOM   5865  C  CG  . PHE   B 2 533  ? 116.943 123.398 93.630  1.00 32.81  ? 533  PHE   A CG  1 
ATOM   5866  C  CD1 . PHE   B 2 533  ? 116.935 123.466 95.010  1.00 37.31  ? 533  PHE   A CD1 1 
ATOM   5867  C  CD2 . PHE   B 2 533  ? 115.739 123.263 92.970  1.00 41.91  ? 533  PHE   A CD2 1 
ATOM   5868  C  CE1 . PHE   B 2 533  ? 115.758 123.386 95.713  1.00 39.77  ? 533  PHE   A CE1 1 
ATOM   5869  C  CE2 . PHE   B 2 533  ? 114.558 123.186 93.672  1.00 44.94  ? 533  PHE   A CE2 1 
ATOM   5870  C  CZ  . PHE   B 2 533  ? 114.569 123.249 95.045  1.00 39.88  ? 533  PHE   A CZ  1 
ATOM   5871  N  N   . SER   B 2 534  ? 120.570 121.665 91.023  1.00 35.87  ? 534  SER   A N   1 
ATOM   5872  C  CA  . SER   B 2 534  ? 121.864 121.619 90.361  1.00 34.08  ? 534  SER   A CA  1 
ATOM   5873  C  C   . SER   B 2 534  ? 121.740 122.083 88.920  1.00 37.63  ? 534  SER   A C   1 
ATOM   5874  O  O   . SER   B 2 534  ? 120.812 121.682 88.210  1.00 50.78  ? 534  SER   A O   1 
ATOM   5875  C  CB  . SER   B 2 534  ? 122.452 120.207 90.407  1.00 42.04  ? 534  SER   A CB  1 
ATOM   5876  O  OG  . SER   B 2 534  ? 121.582 119.271 89.795  1.00 50.80  ? 534  SER   A OG  1 
ATOM   5877  N  N   . ASP   B 2 535  ? 122.674 122.927 88.498  1.00 39.70  ? 535  ASP   A N   1 
ATOM   5878  C  CA  . ASP   B 2 535  ? 122.841 123.230 87.088  1.00 44.41  ? 535  ASP   A CA  1 
ATOM   5879  C  C   . ASP   B 2 535  ? 123.436 122.019 86.374  1.00 46.65  ? 535  ASP   A C   1 
ATOM   5880  O  O   . ASP   B 2 535  ? 124.059 121.149 86.987  1.00 54.97  ? 535  ASP   A O   1 
ATOM   5881  C  CB  . ASP   B 2 535  ? 123.733 124.461 86.918  1.00 45.23  ? 535  ASP   A CB  1 
ATOM   5882  C  CG  . ASP   B 2 535  ? 123.932 124.851 85.467  1.00 48.82  ? 535  ASP   A CG  1 
ATOM   5883  O  OD1 . ASP   B 2 535  ? 122.946 125.238 84.808  1.00 48.73  ? 535  ASP   A OD1 1 
ATOM   5884  O  OD2 . ASP   B 2 535  ? 125.081 124.782 84.988  1.00 53.20  ? 535  ASP   A OD2 1 
ATOM   5885  N  N   . LYS   B 2 536  ? 123.218 121.952 85.063  1.00 36.55  ? 536  LYS   A N   1 
ATOM   5886  C  CA  . LYS   B 2 536  ? 123.725 120.829 84.282  1.00 38.28  ? 536  LYS   A CA  1 
ATOM   5887  C  C   . LYS   B 2 536  ? 125.079 121.140 83.650  1.00 42.03  ? 536  LYS   A C   1 
ATOM   5888  O  O   . LYS   B 2 536  ? 126.065 120.444 83.907  1.00 55.02  ? 536  LYS   A O   1 
ATOM   5889  C  CB  . LYS   B 2 536  ? 122.712 120.439 83.203  1.00 45.59  ? 536  LYS   A CB  1 
ATOM   5890  C  CG  . LYS   B 2 536  ? 123.125 119.233 82.386  1.00 39.82  ? 536  LYS   A CG  1 
ATOM   5891  C  CD  . LYS   B 2 536  ? 122.164 118.995 81.245  1.00 42.78  ? 536  LYS   A CD  1 
ATOM   5892  C  CE  . LYS   B 2 536  ? 122.239 120.114 80.230  1.00 47.35  ? 536  LYS   A CE  1 
ATOM   5893  N  NZ  . LYS   B 2 536  ? 123.586 120.202 79.608  1.00 51.12  ? 536  LYS   A NZ  1 
ATOM   5894  N  N   . THR   B 2 537  ? 125.139 122.180 82.824  1.00 41.97  ? 537  THR   A N   1 
ATOM   5895  C  CA  . THR   B 2 537  ? 126.355 122.478 82.079  1.00 38.86  ? 537  THR   A CA  1 
ATOM   5896  C  C   . THR   B 2 537  ? 127.397 123.097 82.999  1.00 45.42  ? 537  THR   A C   1 
ATOM   5897  O  O   . THR   B 2 537  ? 127.151 124.134 83.622  1.00 55.94  ? 537  THR   A O   1 
ATOM   5898  C  CB  . THR   B 2 537  ? 126.043 123.415 80.916  1.00 46.53  ? 537  THR   A CB  1 
ATOM   5899  O  OG1 . THR   B 2 537  ? 125.080 122.801 80.052  1.00 56.61  ? 537  THR   A OG1 1 
ATOM   5900  C  CG2 . THR   B 2 537  ? 127.300 123.713 80.126  1.00 46.76  ? 537  THR   A CG2 1 
ATOM   5901  N  N   . GLY   B 2 538  ? 128.563 122.462 83.082  1.00 42.19  ? 538  GLY   A N   1 
ATOM   5902  C  CA  . GLY   B 2 538  ? 129.641 122.936 83.917  1.00 39.54  ? 538  GLY   A CA  1 
ATOM   5903  C  C   . GLY   B 2 538  ? 129.594 122.456 85.348  1.00 42.10  ? 538  GLY   A C   1 
ATOM   5904  O  O   . GLY   B 2 538  ? 130.604 122.565 86.054  1.00 48.91  ? 538  GLY   A O   1 
ATOM   5905  N  N   . THR   B 2 539  ? 128.460 121.925 85.796  1.00 42.65  ? 539  THR   A N   1 
ATOM   5906  C  CA  . THR   B 2 539  ? 128.308 121.373 87.134  1.00 45.51  ? 539  THR   A CA  1 
ATOM   5907  C  C   . THR   B 2 539  ? 128.259 119.855 87.128  1.00 47.11  ? 539  THR   A C   1 
ATOM   5908  O  O   . THR   B 2 539  ? 129.036 119.205 87.833  1.00 53.70  ? 539  THR   A O   1 
ATOM   5909  C  CB  . THR   B 2 539  ? 127.039 121.936 87.789  1.00 46.05  ? 539  THR   A CB  1 
ATOM   5910  O  OG1 . THR   B 2 539  ? 127.231 123.321 88.094  1.00 54.51  ? 539  THR   A OG1 1 
ATOM   5911  C  CG2 . THR   B 2 539  ? 126.709 121.183 89.060  1.00 42.23  ? 539  THR   A CG2 1 
ATOM   5912  N  N   . LEU   B 2 540  ? 127.358 119.271 86.342  1.00 44.90  ? 540  LEU   A N   1 
ATOM   5913  C  CA  . LEU   B 2 540  ? 127.321 117.833 86.136  1.00 34.10  ? 540  LEU   A CA  1 
ATOM   5914  C  C   . LEU   B 2 540  ? 128.093 117.394 84.901  1.00 38.09  ? 540  LEU   A C   1 
ATOM   5915  O  O   . LEU   B 2 540  ? 128.228 116.187 84.675  1.00 51.93  ? 540  LEU   A O   1 
ATOM   5916  C  CB  . LEU   B 2 540  ? 125.871 117.351 86.021  1.00 35.48  ? 540  LEU   A CB  1 
ATOM   5917  C  CG  . LEU   B 2 540  ? 124.964 117.576 87.228  1.00 32.84  ? 540  LEU   A CG  1 
ATOM   5918  C  CD1 . LEU   B 2 540  ? 123.554 117.126 86.924  1.00 36.55  ? 540  LEU   A CD1 1 
ATOM   5919  C  CD2 . LEU   B 2 540  ? 125.506 116.839 88.434  1.00 45.10  ? 540  LEU   A CD2 1 
ATOM   5920  N  N   . THR   B 2 541  ? 128.607 118.337 84.100  1.00 36.03  ? 541  THR   A N   1 
ATOM   5921  C  CA  . THR   B 2 541  ? 129.304 118.021 82.865  1.00 35.10  ? 541  THR   A CA  1 
ATOM   5922  C  C   . THR   B 2 541  ? 130.647 118.737 82.828  1.00 39.76  ? 541  THR   A C   1 
ATOM   5923  O  O   . THR   B 2 541  ? 130.841 119.773 83.468  1.00 49.59  ? 541  THR   A O   1 
ATOM   5924  C  CB  . THR   B 2 541  ? 128.481 118.412 81.631  1.00 41.26  ? 541  THR   A CB  1 
ATOM   5925  O  OG1 . THR   B 2 541  ? 128.283 119.830 81.618  1.00 47.52  ? 541  THR   A OG1 1 
ATOM   5926  C  CG2 . THR   B 2 541  ? 127.133 117.722 81.646  1.00 41.52  ? 541  THR   A CG2 1 
ATOM   5927  N  N   . GLN   B 2 542  ? 131.579 118.164 82.072  1.00 45.45  ? 542  GLN   A N   1 
ATOM   5928  C  CA  . GLN   B 2 542  ? 132.896 118.747 81.864  1.00 43.68  ? 542  GLN   A CA  1 
ATOM   5929  C  C   . GLN   B 2 542  ? 132.981 119.579 80.594  1.00 49.99  ? 542  GLN   A C   1 
ATOM   5930  O  O   . GLN   B 2 542  ? 134.048 120.129 80.304  1.00 57.87  ? 542  GLN   A O   1 
ATOM   5931  C  CB  . GLN   B 2 542  ? 133.962 117.650 81.818  1.00 50.74  ? 542  GLN   A CB  1 
ATOM   5932  C  CG  . GLN   B 2 542  ? 134.091 116.841 83.085  1.00 52.56  ? 542  GLN   A CG  1 
ATOM   5933  C  CD  . GLN   B 2 542  ? 135.210 115.827 83.007  1.00 55.79  ? 542  GLN   A CD  1 
ATOM   5934  O  OE1 . GLN   B 2 542  ? 135.353 114.973 83.882  1.00 53.55  ? 542  GLN   A OE1 1 
ATOM   5935  N  NE2 . GLN   B 2 542  ? 136.014 115.916 81.957  1.00 56.20  ? 542  GLN   A NE2 1 
ATOM   5936  N  N   . ASN   B 2 543  ? 131.889 119.682 79.835  1.00 53.10  ? 543  ASN   A N   1 
ATOM   5937  C  CA  . ASN   B 2 543  ? 131.874 120.387 78.553  1.00 51.99  ? 543  ASN   A CA  1 
ATOM   5938  C  C   . ASN   B 2 543  ? 132.912 119.811 77.593  1.00 58.85  ? 543  ASN   A C   1 
ATOM   5939  O  O   . ASN   B 2 543  ? 133.677 120.544 76.962  1.00 63.44  ? 543  ASN   A O   1 
ATOM   5940  C  CB  . ASN   B 2 543  ? 132.082 121.890 78.743  1.00 56.27  ? 543  ASN   A CB  1 
ATOM   5941  C  CG  . ASN   B 2 543  ? 131.090 122.492 79.710  1.00 61.05  ? 543  ASN   A CG  1 
ATOM   5942  O  OD1 . ASN   B 2 543  ? 129.984 121.981 79.876  1.00 60.72  ? 543  ASN   A OD1 1 
ATOM   5943  N  ND2 . ASN   B 2 543  ? 131.480 123.583 80.357  1.00 59.17  ? 543  ASN   A ND2 1 
ATOM   5944  N  N   . ALA   B 2 544  ? 132.941 118.485 77.483  1.00 62.74  ? 544  ALA   A N   1 
ATOM   5945  C  CA  . ALA   B 2 544  ? 133.870 117.797 76.595  1.00 63.72  ? 544  ALA   A CA  1 
ATOM   5946  C  C   . ALA   B 2 544  ? 133.137 116.659 75.905  1.00 68.14  ? 544  ALA   A C   1 
ATOM   5947  O  O   . ALA   B 2 544  ? 132.644 115.744 76.571  1.00 72.28  ? 544  ALA   A O   1 
ATOM   5948  C  CB  . ALA   B 2 544  ? 135.083 117.268 77.365  1.00 65.23  ? 544  ALA   A CB  1 
ATOM   5949  N  N   . MET   B 2 545  ? 133.070 116.715 74.579  1.00 70.25  ? 545  MET   A N   1 
ATOM   5950  C  CA  . MET   B 2 545  ? 132.465 115.663 73.775  1.00 68.40  ? 545  MET   A CA  1 
ATOM   5951  C  C   . MET   B 2 545  ? 133.561 114.777 73.201  1.00 74.58  ? 545  MET   A C   1 
ATOM   5952  O  O   . MET   B 2 545  ? 134.456 115.264 72.502  1.00 77.36  ? 545  MET   A O   1 
ATOM   5953  C  CB  . MET   B 2 545  ? 131.623 116.254 72.644  1.00 72.63  ? 545  MET   A CB  1 
ATOM   5954  C  CG  . MET   B 2 545  ? 130.355 116.952 73.097  1.00 74.65  ? 545  MET   A CG  1 
ATOM   5955  S  SD  . MET   B 2 545  ? 129.106 115.807 73.700  1.00 81.72  ? 545  MET   A SD  1 
ATOM   5956  C  CE  . MET   B 2 545  ? 127.693 116.897 73.847  1.00 74.84  ? 545  MET   A CE  1 
ATOM   5957  N  N   . ILE   B 2 546  ? 133.490 113.482 73.494  1.00 71.12  ? 546  ILE   A N   1 
ATOM   5958  C  CA  . ILE   B 2 546  ? 134.488 112.518 73.048  1.00 72.93  ? 546  ILE   A CA  1 
ATOM   5959  C  C   . ILE   B 2 546  ? 133.787 111.419 72.264  1.00 72.20  ? 546  ILE   A C   1 
ATOM   5960  O  O   . ILE   B 2 546  ? 132.832 110.811 72.759  1.00 70.96  ? 546  ILE   A O   1 
ATOM   5961  C  CB  . ILE   B 2 546  ? 135.280 111.922 74.228  1.00 75.03  ? 546  ILE   A CB  1 
ATOM   5962  C  CG1 . ILE   B 2 546  ? 136.320 112.920 74.747  1.00 76.79  ? 546  ILE   A CG1 1 
ATOM   5963  C  CG2 . ILE   B 2 546  ? 135.959 110.626 73.817  1.00 73.72  ? 546  ILE   A CG2 1 
ATOM   5964  C  CD1 . ILE   B 2 546  ? 135.774 113.956 75.708  1.00 73.65  ? 546  ILE   A CD1 1 
ATOM   5965  N  N   . PHE   B 2 547  ? 134.258 111.171 71.045  1.00 75.66  ? 547  PHE   A N   1 
ATOM   5966  C  CA  . PHE   B 2 547  ? 133.733 110.072 70.248  1.00 72.42  ? 547  PHE   A CA  1 
ATOM   5967  C  C   . PHE   B 2 547  ? 134.152 108.741 70.857  1.00 78.68  ? 547  PHE   A C   1 
ATOM   5968  O  O   . PHE   B 2 547  ? 135.326 108.525 71.169  1.00 84.49  ? 547  PHE   A O   1 
ATOM   5969  C  CB  . PHE   B 2 547  ? 134.240 110.170 68.811  1.00 71.86  ? 547  PHE   A CB  1 
ATOM   5970  C  CG  . PHE   B 2 547  ? 133.416 109.402 67.822  1.00 70.34  ? 547  PHE   A CG  1 
ATOM   5971  C  CD1 . PHE   B 2 547  ? 132.091 109.116 68.080  1.00 75.45  ? 547  PHE   A CD1 1 
ATOM   5972  C  CD2 . PHE   B 2 547  ? 133.969 108.962 66.636  1.00 71.16  ? 547  PHE   A CD2 1 
ATOM   5973  C  CE1 . PHE   B 2 547  ? 131.333 108.412 67.171  1.00 77.41  ? 547  PHE   A CE1 1 
ATOM   5974  C  CE2 . PHE   B 2 547  ? 133.217 108.257 65.725  1.00 75.32  ? 547  PHE   A CE2 1 
ATOM   5975  C  CZ  . PHE   B 2 547  ? 131.898 107.981 65.992  1.00 77.17  ? 547  PHE   A CZ  1 
ATOM   5976  N  N   . ARG   B 2 548  ? 133.186 107.839 71.023  1.00 78.84  ? 548  ARG   A N   1 
ATOM   5977  C  CA  . ARG   B 2 548  ? 133.442 106.565 71.686  1.00 77.39  ? 548  ARG   A CA  1 
ATOM   5978  C  C   . ARG   B 2 548  ? 133.309 105.380 70.740  1.00 77.91  ? 548  ARG   A C   1 
ATOM   5979  O  O   . ARG   B 2 548  ? 134.245 104.582 70.632  1.00 81.26  ? 548  ARG   A O   1 
ATOM   5980  C  CB  . ARG   B 2 548  ? 132.507 106.410 72.889  1.00 79.28  ? 548  ARG   A CB  1 
ATOM   5981  C  CG  . ARG   B 2 548  ? 132.963 107.168 74.123  1.00 80.12  ? 548  ARG   A CG  1 
ATOM   5982  C  CD  . ARG   B 2 548  ? 133.977 106.362 74.916  1.00 78.35  ? 548  ARG   A CD  1 
ATOM   5983  N  NE  . ARG   B 2 548  ? 134.557 107.131 76.010  1.00 83.37  ? 548  ARG   A NE  1 
ATOM   5984  C  CZ  . ARG   B 2 548  ? 135.759 107.688 75.978  1.00 84.57  ? 548  ARG   A CZ  1 
ATOM   5985  N  NH1 . ARG   B 2 548  ? 136.549 107.566 74.923  1.00 82.85  ? 548  ARG   A NH1 1 
ATOM   5986  N  NH2 . ARG   B 2 548  ? 136.181 108.383 77.030  1.00 83.40  ? 548  ARG   A NH2 1 
ATOM   5987  N  N   . GLN   B 2 549  ? 132.179 105.232 70.056  1.00 80.18  ? 549  GLN   A N   1 
ATOM   5988  C  CA  . GLN   B 2 549  ? 131.933 104.074 69.211  1.00 79.02  ? 549  GLN   A CA  1 
ATOM   5989  C  C   . GLN   B 2 549  ? 131.291 104.503 67.900  1.00 83.01  ? 549  GLN   A C   1 
ATOM   5990  O  O   . GLN   B 2 549  ? 130.561 105.496 67.842  1.00 87.68  ? 549  GLN   A O   1 
ATOM   5991  C  CB  . GLN   B 2 549  ? 131.041 103.051 69.923  1.00 79.68  ? 549  GLN   A CB  1 
ATOM   5992  C  CG  . GLN   B 2 549  ? 131.693 102.413 71.138  1.00 83.54  ? 549  GLN   A CG  1 
ATOM   5993  C  CD  . GLN   B 2 549  ? 130.745 101.526 71.913  1.00 86.77  ? 549  GLN   A CD  1 
ATOM   5994  O  OE1 . GLN   B 2 549  ? 129.529 101.613 71.755  1.00 88.26  ? 549  GLN   A OE1 1 
ATOM   5995  N  NE2 . GLN   B 2 549  ? 131.297 100.663 72.757  1.00 86.42  ? 549  GLN   A NE2 1 
ATOM   5996  N  N   . CYS   B 2 550  ? 131.573 103.741 66.846  1.00 89.63  ? 550  CYS   A N   1 
ATOM   5997  C  CA  . CYS   B 2 550  ? 131.014 103.984 65.523  1.00 87.75  ? 550  CYS   A CA  1 
ATOM   5998  C  C   . CYS   B 2 550  ? 130.503 102.673 64.947  1.00 89.06  ? 550  CYS   A C   1 
ATOM   5999  O  O   . CYS   B 2 550  ? 131.173 101.640 65.057  1.00 95.51  ? 550  CYS   A O   1 
ATOM   6000  C  CB  . CYS   B 2 550  ? 132.056 104.606 64.589  1.00 88.31  ? 550  CYS   A CB  1 
ATOM   6001  S  SG  . CYS   B 2 550  ? 133.577 103.646 64.416  1.00 96.12  ? 550  CYS   A SG  1 
ATOM   6002  N  N   . SER   B 2 551  ? 129.322 102.714 64.340  1.00 86.62  ? 551  SER   A N   1 
ATOM   6003  C  CA  . SER   B 2 551  ? 128.744 101.560 63.666  1.00 85.98  ? 551  SER   A CA  1 
ATOM   6004  C  C   . SER   B 2 551  ? 128.724 101.819 62.167  1.00 89.63  ? 551  SER   A C   1 
ATOM   6005  O  O   . SER   B 2 551  ? 128.223 102.855 61.719  1.00 94.75  ? 551  SER   A O   1 
ATOM   6006  C  CB  . SER   B 2 551  ? 127.330 101.279 64.173  1.00 87.80  ? 551  SER   A CB  1 
ATOM   6007  O  OG  . SER   B 2 551  ? 126.458 102.355 63.877  1.00 92.43  ? 551  SER   A OG  1 
ATOM   6008  N  N   . VAL   B 2 552  ? 129.273 100.887 61.400  1.00 96.29  ? 552  VAL   A N   1 
ATOM   6009  C  CA  . VAL   B 2 552  ? 129.374 101.022 59.950  1.00 97.49  ? 552  VAL   A CA  1 
ATOM   6010  C  C   . VAL   B 2 552  ? 128.575 99.873  59.347  1.00 99.81  ? 552  VAL   A C   1 
ATOM   6011  O  O   . VAL   B 2 552  ? 129.098 98.783  59.097  1.00 103.47 ? 552  VAL   A O   1 
ATOM   6012  C  CB  . VAL   B 2 552  ? 130.825 101.019 59.463  1.00 99.80  ? 552  VAL   A CB  1 
ATOM   6013  C  CG1 . VAL   B 2 552  ? 130.878 101.232 57.961  1.00 98.62  ? 552  VAL   A CG1 1 
ATOM   6014  C  CG2 . VAL   B 2 552  ? 131.624 102.098 60.183  1.00 99.94  ? 552  VAL   A CG2 1 
ATOM   6015  N  N   . GLY   B 2 553  ? 127.291 100.114 59.112  1.00 105.74 ? 553  GLY   A N   1 
ATOM   6016  C  CA  . GLY   B 2 553  ? 126.433 99.134  58.482  1.00 106.91 ? 553  GLY   A CA  1 
ATOM   6017  C  C   . GLY   B 2 553  ? 125.948 98.070  59.442  1.00 111.38 ? 553  GLY   A C   1 
ATOM   6018  O  O   . GLY   B 2 553  ? 124.803 98.114  59.901  1.00 111.43 ? 553  GLY   A O   1 
ATOM   6019  N  N   . GLY   B 2 554  ? 126.813 97.109  59.759  1.00 111.85 ? 554  GLY   A N   1 
ATOM   6020  C  CA  . GLY   B 2 554  ? 126.450 96.056  60.686  1.00 110.17 ? 554  GLY   A CA  1 
ATOM   6021  C  C   . GLY   B 2 554  ? 127.424 95.865  61.829  1.00 107.90 ? 554  GLY   A C   1 
ATOM   6022  O  O   . GLY   B 2 554  ? 127.045 95.384  62.901  1.00 109.58 ? 554  GLY   A O   1 
ATOM   6023  N  N   . LYS   B 2 555  ? 128.678 96.248  61.620  1.00 99.86  ? 555  LYS   A N   1 
ATOM   6024  C  CA  . LYS   B 2 555  ? 129.753 95.944  62.553  1.00 103.92 ? 555  LYS   A CA  1 
ATOM   6025  C  C   . LYS   B 2 555  ? 129.997 97.126  63.481  1.00 105.19 ? 555  LYS   A C   1 
ATOM   6026  O  O   . LYS   B 2 555  ? 130.083 98.272  63.028  1.00 106.94 ? 555  LYS   A O   1 
ATOM   6027  C  CB  . LYS   B 2 555  ? 131.037 95.589  61.802  1.00 106.06 ? 555  LYS   A CB  1 
ATOM   6028  C  CG  . LYS   B 2 555  ? 132.170 95.114  62.697  1.00 106.64 ? 555  LYS   A CG  1 
ATOM   6029  C  CD  . LYS   B 2 555  ? 133.396 94.740  61.884  1.00 105.58 ? 555  LYS   A CD  1 
ATOM   6030  C  CE  . LYS   B 2 555  ? 134.505 94.201  62.773  1.00 106.02 ? 555  LYS   A CE  1 
ATOM   6031  N  NZ  . LYS   B 2 555  ? 134.895 95.175  63.827  1.00 107.17 ? 555  LYS   A NZ  1 
ATOM   6032  N  N   . ILE   B 2 556  ? 130.107 96.841  64.774  1.00 101.26 ? 556  ILE   A N   1 
ATOM   6033  C  CA  . ILE   B 2 556  ? 130.428 97.844  65.781  1.00 99.00  ? 556  ILE   A CA  1 
ATOM   6034  C  C   . ILE   B 2 556  ? 131.939 97.962  65.887  1.00 100.93 ? 556  ILE   A C   1 
ATOM   6035  O  O   . ILE   B 2 556  ? 132.683 97.033  65.555  1.00 104.38 ? 556  ILE   A O   1 
ATOM   6036  C  CB  . ILE   B 2 556  ? 129.803 97.497  67.150  1.00 100.50 ? 556  ILE   A CB  1 
ATOM   6037  C  CG1 . ILE   B 2 556  ? 129.216 96.080  67.146  1.00 100.71 ? 556  ILE   A CG1 1 
ATOM   6038  C  CG2 . ILE   B 2 556  ? 128.770 98.536  67.545  1.00 98.02  ? 556  ILE   A CG2 1 
ATOM   6039  C  CD1 . ILE   B 2 556  ? 127.745 96.006  66.773  1.00 101.33 ? 556  ILE   A CD1 1 
ATOM   6040  N  N   . TYR   B 2 557  ? 132.400 99.118  66.351  1.00 92.54  ? 557  TYR   A N   1 
ATOM   6041  C  CA  . TYR   B 2 557  ? 133.816 99.363  66.569  1.00 92.47  ? 557  TYR   A CA  1 
ATOM   6042  C  C   . TYR   B 2 557  ? 134.003 100.092 67.891  1.00 93.28  ? 557  TYR   A C   1 
ATOM   6043  O  O   . TYR   B 2 557  ? 133.129 100.841 68.334  1.00 96.82  ? 557  TYR   A O   1 
ATOM   6044  C  CB  . TYR   B 2 557  ? 134.427 100.173 65.420  1.00 90.95  ? 557  TYR   A CB  1 
ATOM   6045  C  CG  . TYR   B 2 557  ? 134.371 99.463  64.088  1.00 92.88  ? 557  TYR   A CG  1 
ATOM   6046  C  CD1 . TYR   B 2 557  ? 133.248 99.552  63.280  1.00 94.18  ? 557  TYR   A CD1 1 
ATOM   6047  C  CD2 . TYR   B 2 557  ? 135.441 98.701  63.642  1.00 95.65  ? 557  TYR   A CD2 1 
ATOM   6048  C  CE1 . TYR   B 2 557  ? 133.191 98.903  62.065  1.00 95.23  ? 557  TYR   A CE1 1 
ATOM   6049  C  CE2 . TYR   B 2 557  ? 135.394 98.050  62.426  1.00 96.54  ? 557  TYR   A CE2 1 
ATOM   6050  C  CZ  . TYR   B 2 557  ? 134.266 98.154  61.643  1.00 96.34  ? 557  TYR   A CZ  1 
ATOM   6051  O  OH  . TYR   B 2 557  ? 134.212 97.507  60.433  1.00 96.29  ? 557  TYR   A OH  1 
ATOM   6052  N  N   . THR   B 2 558  ? 135.148 99.859  68.522  1.00 77.66  ? 558  THR   A N   1 
ATOM   6053  C  CA  . THR   B 2 558  ? 135.437 100.454 69.820  1.00 78.82  ? 558  THR   A CA  1 
ATOM   6054  C  C   . THR   B 2 558  ? 136.939 100.584 70.045  1.00 80.38  ? 558  THR   A C   1 
ATOM   6055  O  O   . THR   B 2 558  ? 137.434 101.655 70.395  1.00 81.01  ? 558  THR   A O   1 
ATOM   6056  C  CB  . THR   B 2 558  ? 134.825 99.627  70.965  1.00 82.08  ? 558  THR   A CB  1 
ATOM   6057  O  OG1 . THR   B 2 558  ? 133.403 99.555  70.803  1.00 82.15  ? 558  THR   A OG1 1 
ATOM   6058  C  CG2 . THR   B 2 558  ? 135.145 100.259 72.312  1.00 82.29  ? 558  THR   A CG2 1 
ATOM   6059  N  N   . LEU   B 2 628  ? 141.755 98.096  63.895  1.00 109.85 ? 628  LEU   A N   1 
ATOM   6060  C  CA  . LEU   B 2 628  ? 140.875 97.157  63.211  1.00 111.22 ? 628  LEU   A CA  1 
ATOM   6061  C  C   . LEU   B 2 628  ? 140.408 97.746  61.885  1.00 112.36 ? 628  LEU   A C   1 
ATOM   6062  O  O   . LEU   B 2 628  ? 140.232 97.024  60.904  1.00 114.55 ? 628  LEU   A O   1 
ATOM   6063  C  CB  . LEU   B 2 628  ? 139.677 96.802  64.097  1.00 111.00 ? 628  LEU   A CB  1 
ATOM   6064  C  CG  . LEU   B 2 628  ? 138.979 95.455  63.880  1.00 111.49 ? 628  LEU   A CG  1 
ATOM   6065  C  CD1 . LEU   B 2 628  ? 138.201 95.067  65.125  1.00 112.13 ? 628  LEU   A CD1 1 
ATOM   6066  C  CD2 . LEU   B 2 628  ? 138.055 95.483  62.674  1.00 110.88 ? 628  LEU   A CD2 1 
ATOM   6067  N  N   . ASP   B 2 629  ? 140.209 99.066  61.865  1.00 112.22 ? 629  ASP   A N   1 
ATOM   6068  C  CA  . ASP   B 2 629  ? 139.769 99.727  60.641  1.00 113.95 ? 629  ASP   A CA  1 
ATOM   6069  C  C   . ASP   B 2 629  ? 140.806 99.588  59.534  1.00 115.64 ? 629  ASP   A C   1 
ATOM   6070  O  O   . ASP   B 2 629  ? 140.456 99.354  58.371  1.00 116.69 ? 629  ASP   A O   1 
ATOM   6071  C  CB  . ASP   B 2 629  ? 139.469 101.200 60.917  1.00 114.07 ? 629  ASP   A CB  1 
ATOM   6072  C  CG  . ASP   B 2 629  ? 138.332 101.387 61.901  1.00 113.74 ? 629  ASP   A CG  1 
ATOM   6073  O  OD1 . ASP   B 2 629  ? 137.440 100.515 61.951  1.00 112.67 ? 629  ASP   A OD1 1 
ATOM   6074  O  OD2 . ASP   B 2 629  ? 138.330 102.405 62.624  1.00 114.90 ? 629  ASP   A OD2 1 
ATOM   6075  N  N   . LYS   B 2 630  ? 142.089 99.735  59.874  1.00 118.80 ? 630  LYS   A N   1 
ATOM   6076  C  CA  . LYS   B 2 630  ? 143.139 99.555  58.878  1.00 119.81 ? 630  LYS   A CA  1 
ATOM   6077  C  C   . LYS   B 2 630  ? 143.156 98.125  58.353  1.00 119.43 ? 630  LYS   A C   1 
ATOM   6078  O  O   . LYS   B 2 630  ? 143.318 97.900  57.148  1.00 118.13 ? 630  LYS   A O   1 
ATOM   6079  C  CB  . LYS   B 2 630  ? 144.497 99.927  59.472  1.00 118.76 ? 630  LYS   A CB  1 
ATOM   6080  C  CG  . LYS   B 2 630  ? 145.648 99.849  58.483  1.00 119.03 ? 630  LYS   A CG  1 
ATOM   6081  C  CD  . LYS   B 2 630  ? 146.963 100.250 59.131  1.00 119.41 ? 630  LYS   A CD  1 
ATOM   6082  C  CE  . LYS   B 2 630  ? 148.109 100.203 58.132  1.00 119.73 ? 630  LYS   A CE  1 
ATOM   6083  N  NZ  . LYS   B 2 630  ? 147.889 101.132 56.989  1.00 120.04 ? 630  LYS   A NZ  1 
ATOM   6084  N  N   . ASP   B 2 631  ? 142.995 97.145  59.245  1.00 124.00 ? 631  ASP   A N   1 
ATOM   6085  C  CA  . ASP   B 2 631  ? 142.897 95.757  58.807  1.00 124.99 ? 631  ASP   A CA  1 
ATOM   6086  C  C   . ASP   B 2 631  ? 141.635 95.529  57.983  1.00 125.30 ? 631  ASP   A C   1 
ATOM   6087  O  O   . ASP   B 2 631  ? 141.658 94.787  56.993  1.00 127.00 ? 631  ASP   A O   1 
ATOM   6088  C  CB  . ASP   B 2 631  ? 142.928 94.822  60.017  1.00 124.50 ? 631  ASP   A CB  1 
ATOM   6089  C  CG  . ASP   B 2 631  ? 143.116 93.368  59.628  1.00 124.70 ? 631  ASP   A CG  1 
ATOM   6090  O  OD1 . ASP   B 2 631  ? 143.429 93.099  58.449  1.00 124.74 ? 631  ASP   A OD1 1 
ATOM   6091  O  OD2 . ASP   B 2 631  ? 142.951 92.492  60.502  1.00 124.92 ? 631  ASP   A OD2 1 
ATOM   6092  N  N   . LEU   B 2 632  ? 140.524 96.157  58.378  1.00 118.43 ? 632  LEU   A N   1 
ATOM   6093  C  CA  . LEU   B 2 632  ? 139.279 96.006  57.633  1.00 118.91 ? 632  LEU   A CA  1 
ATOM   6094  C  C   . LEU   B 2 632  ? 139.385 96.582  56.228  1.00 119.97 ? 632  LEU   A C   1 
ATOM   6095  O  O   . LEU   B 2 632  ? 138.860 95.991  55.277  1.00 120.12 ? 632  LEU   A O   1 
ATOM   6096  C  CB  . LEU   B 2 632  ? 138.131 96.679  58.383  1.00 117.51 ? 632  LEU   A CB  1 
ATOM   6097  C  CG  . LEU   B 2 632  ? 136.775 96.618  57.675  1.00 119.61 ? 632  LEU   A CG  1 
ATOM   6098  C  CD1 . LEU   B 2 632  ? 135.959 95.426  58.158  1.00 119.75 ? 632  LEU   A CD1 1 
ATOM   6099  C  CD2 . LEU   B 2 632  ? 136.005 97.919  57.847  1.00 118.47 ? 632  LEU   A CD2 1 
ATOM   6100  N  N   . GLU   B 2 633  ? 140.059 97.721  56.073  1.00 120.72 ? 633  GLU   A N   1 
ATOM   6101  C  CA  . GLU   B 2 633  ? 140.120 98.422  54.792  1.00 121.36 ? 633  GLU   A CA  1 
ATOM   6102  C  C   . GLU   B 2 633  ? 141.037 97.643  53.852  1.00 121.45 ? 633  GLU   A C   1 
ATOM   6103  O  O   . GLU   B 2 633  ? 142.243 97.880  53.759  1.00 121.01 ? 633  GLU   A O   1 
ATOM   6104  C  CB  . GLU   B 2 633  ? 140.599 99.855  54.988  1.00 120.26 ? 633  GLU   A CB  1 
ATOM   6105  C  CG  . GLU   B 2 633  ? 140.089 100.837 53.943  1.00 121.33 ? 633  GLU   A CG  1 
ATOM   6106  C  CD  . GLU   B 2 633  ? 140.741 100.658 52.585  1.00 123.26 ? 633  GLU   A CD  1 
ATOM   6107  O  OE1 . GLU   B 2 633  ? 141.952 100.355 52.538  1.00 123.11 ? 633  GLU   A OE1 1 
ATOM   6108  O  OE2 . GLU   B 2 633  ? 140.042 100.822 51.564  1.00 122.92 ? 633  GLU   A OE2 1 
ATOM   6109  N  N   . ALA   B 2 634  ? 140.443 96.681  53.150  1.00 122.09 ? 634  ALA   A N   1 
ATOM   6110  C  CA  . ALA   B 2 634  ? 141.140 95.899  52.141  1.00 122.47 ? 634  ALA   A CA  1 
ATOM   6111  C  C   . ALA   B 2 634  ? 140.956 96.453  50.736  1.00 123.95 ? 634  ALA   A C   1 
ATOM   6112  O  O   . ALA   B 2 634  ? 141.467 95.862  49.780  1.00 124.77 ? 634  ALA   A O   1 
ATOM   6113  C  CB  . ALA   B 2 634  ? 140.673 94.441  52.186  1.00 122.36 ? 634  ALA   A CB  1 
ATOM   6114  N  N   . HIS   B 2 635  ? 140.228 97.560  50.591  1.00 124.50 ? 635  HIS   A N   1 
ATOM   6115  C  CA  . HIS   B 2 635  ? 139.964 98.232  49.321  1.00 124.01 ? 635  HIS   A CA  1 
ATOM   6116  C  C   . HIS   B 2 635  ? 139.181 97.363  48.343  1.00 123.32 ? 635  HIS   A C   1 
ATOM   6117  O  O   . HIS   B 2 635  ? 139.007 97.747  47.180  1.00 124.51 ? 635  HIS   A O   1 
ATOM   6118  C  CB  . HIS   B 2 635  ? 141.265 98.721  48.666  1.00 124.48 ? 635  HIS   A CB  1 
ATOM   6119  C  CG  . HIS   B 2 635  ? 141.061 99.783  47.629  1.00 125.69 ? 635  HIS   A CG  1 
ATOM   6120  N  ND1 . HIS   B 2 635  ? 140.843 99.493  46.300  1.00 126.45 ? 635  HIS   A ND1 1 
ATOM   6121  C  CD2 . HIS   B 2 635  ? 141.041 101.133 47.728  1.00 125.06 ? 635  HIS   A CD2 1 
ATOM   6122  C  CE1 . HIS   B 2 635  ? 140.699 100.619 45.624  1.00 125.63 ? 635  HIS   A CE1 1 
ATOM   6123  N  NE2 . HIS   B 2 635  ? 140.814 101.629 46.467  1.00 124.98 ? 635  HIS   A NE2 1 
ATOM   6124  N  N   . ASP   B 2 636  ? 138.694 96.204  48.782  1.00 122.31 ? 636  ASP   A N   1 
ATOM   6125  C  CA  . ASP   B 2 636  ? 137.927 95.324  47.910  1.00 125.51 ? 636  ASP   A CA  1 
ATOM   6126  C  C   . ASP   B 2 636  ? 136.634 94.897  48.592  1.00 125.68 ? 636  ASP   A C   1 
ATOM   6127  O  O   . ASP   B 2 636  ? 135.641 94.592  47.923  1.00 125.80 ? 636  ASP   A O   1 
ATOM   6128  C  CB  . ASP   B 2 636  ? 138.758 94.099  47.519  1.00 126.59 ? 636  ASP   A CB  1 
ATOM   6129  C  CG  . ASP   B 2 636  ? 138.013 93.160  46.590  1.00 125.60 ? 636  ASP   A CG  1 
ATOM   6130  O  OD1 . ASP   B 2 636  ? 137.790 93.532  45.419  1.00 123.66 ? 636  ASP   A OD1 1 
ATOM   6131  O  OD2 . ASP   B 2 636  ? 137.651 92.049  47.031  1.00 124.28 ? 636  ASP   A OD2 1 
ATOM   6132  N  N   . SER   B 2 637  ? 136.638 94.875  49.922  1.00 116.63 ? 637  SER   A N   1 
ATOM   6133  C  CA  . SER   B 2 637  ? 135.451 94.480  50.665  1.00 115.97 ? 637  SER   A CA  1 
ATOM   6134  C  C   . SER   B 2 637  ? 134.377 95.554  50.564  1.00 113.60 ? 637  SER   A C   1 
ATOM   6135  O  O   . SER   B 2 637  ? 134.671 96.752  50.573  1.00 113.80 ? 637  SER   A O   1 
ATOM   6136  C  CB  . SER   B 2 637  ? 135.802 94.224  52.130  1.00 115.56 ? 637  SER   A CB  1 
ATOM   6137  O  OG  . SER   B 2 637  ? 136.755 93.182  52.252  1.00 117.24 ? 637  SER   A OG  1 
ATOM   6138  N  N   . GLU   B 2 638  ? 133.121 95.115  50.461  1.00 112.83 ? 638  GLU   A N   1 
ATOM   6139  C  CA  . GLU   B 2 638  ? 132.011 96.061  50.453  1.00 113.78 ? 638  GLU   A CA  1 
ATOM   6140  C  C   . GLU   B 2 638  ? 131.926 96.816  51.772  1.00 117.03 ? 638  GLU   A C   1 
ATOM   6141  O  O   . GLU   B 2 638  ? 131.537 97.992  51.795  1.00 118.64 ? 638  GLU   A O   1 
ATOM   6142  C  CB  . GLU   B 2 638  ? 130.701 95.328  50.162  1.00 114.50 ? 638  GLU   A CB  1 
ATOM   6143  C  CG  . GLU   B 2 638  ? 129.536 96.234  49.797  1.00 116.09 ? 638  GLU   A CG  1 
ATOM   6144  C  CD  . GLU   B 2 638  ? 128.725 96.670  51.001  1.00 118.09 ? 638  GLU   A CD  1 
ATOM   6145  O  OE1 . GLU   B 2 638  ? 128.989 96.168  52.114  1.00 117.66 ? 638  GLU   A OE1 1 
ATOM   6146  O  OE2 . GLU   B 2 638  ? 127.818 97.512  50.833  1.00 118.10 ? 638  GLU   A OE2 1 
ATOM   6147  N  N   . GLN   B 2 639  ? 132.287 96.159  52.877  1.00 113.37 ? 639  GLN   A N   1 
ATOM   6148  C  CA  . GLN   B 2 639  ? 132.342 96.844  54.163  1.00 113.89 ? 639  GLN   A CA  1 
ATOM   6149  C  C   . GLN   B 2 639  ? 133.364 97.972  54.135  1.00 113.09 ? 639  GLN   A C   1 
ATOM   6150  O  O   . GLN   B 2 639  ? 133.151 99.028  54.740  1.00 115.47 ? 639  GLN   A O   1 
ATOM   6151  C  CB  . GLN   B 2 639  ? 132.667 95.845  55.273  1.00 113.53 ? 639  GLN   A CB  1 
ATOM   6152  C  CG  . GLN   B 2 639  ? 132.591 96.422  56.677  1.00 113.89 ? 639  GLN   A CG  1 
ATOM   6153  C  CD  . GLN   B 2 639  ? 131.168 96.714  57.114  1.00 113.95 ? 639  GLN   A CD  1 
ATOM   6154  O  OE1 . GLN   B 2 639  ? 130.210 96.209  56.529  1.00 114.93 ? 639  GLN   A OE1 1 
ATOM   6155  N  NE2 . GLN   B 2 639  ? 131.025 97.533  58.149  1.00 112.99 ? 639  GLN   A NE2 1 
ATOM   6156  N  N   . SER   B 2 640  ? 134.481 97.769  53.434  1.00 109.20 ? 640  SER   A N   1 
ATOM   6157  C  CA  . SER   B 2 640  ? 135.463 98.837  53.282  1.00 111.71 ? 640  SER   A CA  1 
ATOM   6158  C  C   . SER   B 2 640  ? 134.880 100.017 52.514  1.00 110.23 ? 640  SER   A C   1 
ATOM   6159  O  O   . SER   B 2 640  ? 135.130 101.178 52.860  1.00 112.19 ? 640  SER   A O   1 
ATOM   6160  C  CB  . SER   B 2 640  ? 136.713 98.304  52.584  1.00 115.06 ? 640  SER   A CB  1 
ATOM   6161  O  OG  . SER   B 2 640  ? 137.662 99.336  52.379  1.00 115.89 ? 640  SER   A OG  1 
ATOM   6162  N  N   . ARG   B 2 641  ? 134.107 99.740  51.463  1.00 106.39 ? 641  ARG   A N   1 
ATOM   6163  C  CA  . ARG   B 2 641  ? 133.467 100.817 50.714  1.00 107.20 ? 641  ARG   A CA  1 
ATOM   6164  C  C   . ARG   B 2 641  ? 132.481 101.579 51.589  1.00 107.54 ? 641  ARG   A C   1 
ATOM   6165  O  O   . ARG   B 2 641  ? 132.412 102.815 51.538  1.00 111.53 ? 641  ARG   A O   1 
ATOM   6166  C  CB  . ARG   B 2 641  ? 132.762 100.247 49.483  1.00 111.30 ? 641  ARG   A CB  1 
ATOM   6167  C  CG  . ARG   B 2 641  ? 133.576 99.210  48.725  1.00 113.53 ? 641  ARG   A CG  1 
ATOM   6168  C  CD  . ARG   B 2 641  ? 132.748 98.550  47.633  1.00 113.09 ? 641  ARG   A CD  1 
ATOM   6169  N  NE  . ARG   B 2 641  ? 133.418 97.390  47.058  1.00 113.50 ? 641  ARG   A NE  1 
ATOM   6170  C  CZ  . ARG   B 2 641  ? 134.211 97.430  45.997  1.00 113.79 ? 641  ARG   A CZ  1 
ATOM   6171  N  NH1 . ARG   B 2 641  ? 134.460 98.564  45.362  1.00 113.05 ? 641  ARG   A NH1 1 
ATOM   6172  N  NH2 . ARG   B 2 641  ? 134.769 96.304  45.560  1.00 113.55 ? 641  ARG   A NH2 1 
ATOM   6173  N  N   . ILE   B 2 642  ? 131.708 100.856 52.400  1.00 100.10 ? 642  ILE   A N   1 
ATOM   6174  C  CA  . ILE   B 2 642  ? 130.759 101.513 53.293  1.00 102.31 ? 642  ILE   A CA  1 
ATOM   6175  C  C   . ILE   B 2 642  ? 131.495 102.350 54.330  1.00 101.65 ? 642  ILE   A C   1 
ATOM   6176  O  O   . ILE   B 2 642  ? 131.045 103.438 54.700  1.00 104.92 ? 642  ILE   A O   1 
ATOM   6177  C  CB  . ILE   B 2 642  ? 129.831 100.474 53.948  1.00 104.13 ? 642  ILE   A CB  1 
ATOM   6178  C  CG1 . ILE   B 2 642  ? 129.043 99.724  52.876  1.00 103.30 ? 642  ILE   A CG1 1 
ATOM   6179  C  CG2 . ILE   B 2 642  ? 128.870 101.147 54.910  1.00 104.65 ? 642  ILE   A CG2 1 
ATOM   6180  C  CD1 . ILE   B 2 642  ? 128.193 100.626 52.007  1.00 102.60 ? 642  ILE   A CD1 1 
ATOM   6181  N  N   . LEU   B 2 643  ? 132.637 101.858 54.815  1.00 96.83  ? 643  LEU   A N   1 
ATOM   6182  C  CA  . LEU   B 2 643  ? 133.443 102.637 55.751  1.00 97.07  ? 643  LEU   A CA  1 
ATOM   6183  C  C   . LEU   B 2 643  ? 133.963 103.914 55.103  1.00 98.16  ? 643  LEU   A C   1 
ATOM   6184  O  O   . LEU   B 2 643  ? 133.953 104.986 55.724  1.00 100.88 ? 643  LEU   A O   1 
ATOM   6185  C  CB  . LEU   B 2 643  ? 134.603 101.788 56.270  1.00 98.97  ? 643  LEU   A CB  1 
ATOM   6186  C  CG  . LEU   B 2 643  ? 135.589 102.475 57.216  1.00 100.00 ? 643  LEU   A CG  1 
ATOM   6187  C  CD1 . LEU   B 2 643  ? 134.902 102.867 58.514  1.00 100.50 ? 643  LEU   A CD1 1 
ATOM   6188  C  CD2 . LEU   B 2 643  ? 136.787 101.578 57.488  1.00 100.70 ? 643  LEU   A CD2 1 
ATOM   6189  N  N   . HIS   B 2 644  ? 134.431 103.814 53.857  1.00 95.87  ? 644  HIS   A N   1 
ATOM   6190  C  CA  . HIS   B 2 644  ? 134.878 104.997 53.130  1.00 94.67  ? 644  HIS   A CA  1 
ATOM   6191  C  C   . HIS   B 2 644  ? 133.755 106.016 53.009  1.00 94.98  ? 644  HIS   A C   1 
ATOM   6192  O  O   . HIS   B 2 644  ? 133.947 107.207 53.279  1.00 99.74  ? 644  HIS   A O   1 
ATOM   6193  C  CB  . HIS   B 2 644  ? 135.390 104.599 51.745  1.00 95.01  ? 644  HIS   A CB  1 
ATOM   6194  C  CG  . HIS   B 2 644  ? 136.824 104.169 51.727  1.00 97.84  ? 644  HIS   A CG  1 
ATOM   6195  N  ND1 . HIS   B 2 644  ? 137.811 104.901 51.102  1.00 100.79 ? 644  HIS   A ND1 1 
ATOM   6196  C  CD2 . HIS   B 2 644  ? 137.439 103.084 52.254  1.00 98.21  ? 644  HIS   A CD2 1 
ATOM   6197  C  CE1 . HIS   B 2 644  ? 138.971 104.286 51.246  1.00 99.25  ? 644  HIS   A CE1 1 
ATOM   6198  N  NE2 . HIS   B 2 644  ? 138.773 103.181 51.941  1.00 97.38  ? 644  HIS   A NE2 1 
ATOM   6199  N  N   . GLY   B 2 645  ? 132.566 105.558 52.615  1.00 88.43  ? 645  GLY   A N   1 
ATOM   6200  C  CA  . GLY   B 2 645  ? 131.439 106.470 52.495  1.00 89.51  ? 645  GLY   A CA  1 
ATOM   6201  C  C   . GLY   B 2 645  ? 131.043 107.089 53.822  1.00 89.23  ? 645  GLY   A C   1 
ATOM   6202  O  O   . GLY   B 2 645  ? 130.742 108.283 53.898  1.00 93.32  ? 645  GLY   A O   1 
ATOM   6203  N  N   . PHE   B 2 646  ? 131.044 106.284 54.885  1.00 82.42  ? 646  PHE   A N   1 
ATOM   6204  C  CA  . PHE   B 2 646  ? 130.689 106.772 56.212  1.00 82.50  ? 646  PHE   A CA  1 
ATOM   6205  C  C   . PHE   B 2 646  ? 131.642 107.869 56.663  1.00 83.79  ? 646  PHE   A C   1 
ATOM   6206  O  O   . PHE   B 2 646  ? 131.212 108.933 57.127  1.00 89.68  ? 646  PHE   A O   1 
ATOM   6207  C  CB  . PHE   B 2 646  ? 130.698 105.599 57.195  1.00 83.76  ? 646  PHE   A CB  1 
ATOM   6208  C  CG  . PHE   B 2 646  ? 130.463 105.987 58.626  1.00 81.67  ? 646  PHE   A CG  1 
ATOM   6209  C  CD1 . PHE   B 2 646  ? 131.521 106.340 59.447  1.00 84.30  ? 646  PHE   A CD1 1 
ATOM   6210  C  CD2 . PHE   B 2 646  ? 129.190 105.963 59.162  1.00 81.76  ? 646  PHE   A CD2 1 
ATOM   6211  C  CE1 . PHE   B 2 646  ? 131.310 106.686 60.762  1.00 86.50  ? 646  PHE   A CE1 1 
ATOM   6212  C  CE2 . PHE   B 2 646  ? 128.973 106.304 60.479  1.00 85.08  ? 646  PHE   A CE2 1 
ATOM   6213  C  CZ  . PHE   B 2 646  ? 130.034 106.667 61.279  1.00 87.40  ? 646  PHE   A CZ  1 
ATOM   6214  N  N   . PHE   B 2 647  ? 132.946 107.630 56.531  1.00 80.24  ? 647  PHE   A N   1 
ATOM   6215  C  CA  . PHE   B 2 647  ? 133.909 108.634 56.966  1.00 81.27  ? 647  PHE   A CA  1 
ATOM   6216  C  C   . PHE   B 2 647  ? 133.885 109.864 56.069  1.00 81.47  ? 647  PHE   A C   1 
ATOM   6217  O  O   . PHE   B 2 647  ? 134.102 110.980 56.552  1.00 85.20  ? 647  PHE   A O   1 
ATOM   6218  C  CB  . PHE   B 2 647  ? 135.308 108.029 57.032  1.00 82.57  ? 647  PHE   A CB  1 
ATOM   6219  C  CG  . PHE   B 2 647  ? 135.674 107.512 58.393  1.00 82.96  ? 647  PHE   A CG  1 
ATOM   6220  C  CD1 . PHE   B 2 647  ? 134.960 106.478 58.971  1.00 79.76  ? 647  PHE   A CD1 1 
ATOM   6221  C  CD2 . PHE   B 2 647  ? 136.732 108.061 59.095  1.00 86.64  ? 647  PHE   A CD2 1 
ATOM   6222  C  CE1 . PHE   B 2 647  ? 135.293 106.003 60.223  1.00 80.04  ? 647  PHE   A CE1 1 
ATOM   6223  C  CE2 . PHE   B 2 647  ? 137.071 107.588 60.348  1.00 86.86  ? 647  PHE   A CE2 1 
ATOM   6224  C  CZ  . PHE   B 2 647  ? 136.350 106.558 60.911  1.00 81.97  ? 647  PHE   A CZ  1 
ATOM   6225  N  N   . ALA   B 2 648  ? 133.610 109.691 54.774  1.00 81.75  ? 648  ALA   A N   1 
ATOM   6226  C  CA  . ALA   B 2 648  ? 133.461 110.851 53.903  1.00 83.17  ? 648  ALA   A CA  1 
ATOM   6227  C  C   . ALA   B 2 648  ? 132.277 111.707 54.331  1.00 78.03  ? 648  ALA   A C   1 
ATOM   6228  O  O   . ALA   B 2 648  ? 132.373 112.939 54.369  1.00 84.07  ? 648  ALA   A O   1 
ATOM   6229  C  CB  . ALA   B 2 648  ? 133.307 110.403 52.450  1.00 85.17  ? 648  ALA   A CB  1 
ATOM   6230  N  N   . VAL   B 2 649  ? 131.150 111.073 54.659  1.00 71.94  ? 649  VAL   A N   1 
ATOM   6231  C  CA  . VAL   B 2 649  ? 129.990 111.826 55.128  1.00 76.78  ? 649  VAL   A CA  1 
ATOM   6232  C  C   . VAL   B 2 649  ? 130.312 112.531 56.437  1.00 81.17  ? 649  VAL   A C   1 
ATOM   6233  O  O   . VAL   B 2 649  ? 129.931 113.689 56.649  1.00 88.14  ? 649  VAL   A O   1 
ATOM   6234  C  CB  . VAL   B 2 649  ? 128.768 110.901 55.269  1.00 81.90  ? 649  VAL   A CB  1 
ATOM   6235  C  CG1 . VAL   B 2 649  ? 127.620 111.636 55.942  1.00 80.48  ? 649  VAL   A CG1 1 
ATOM   6236  C  CG2 . VAL   B 2 649  ? 128.340 110.384 53.910  1.00 83.29  ? 649  VAL   A CG2 1 
ATOM   6237  N  N   . LEU   B 2 650  ? 131.020 111.844 57.336  1.00 81.58  ? 650  LEU   A N   1 
ATOM   6238  C  CA  . LEU   B 2 650  ? 131.365 112.444 58.619  1.00 77.69  ? 650  LEU   A CA  1 
ATOM   6239  C  C   . LEU   B 2 650  ? 132.268 113.658 58.439  1.00 79.50  ? 650  LEU   A C   1 
ATOM   6240  O  O   . LEU   B 2 650  ? 132.100 114.672 59.126  1.00 83.72  ? 650  LEU   A O   1 
ATOM   6241  C  CB  . LEU   B 2 650  ? 132.036 111.403 59.515  1.00 77.04  ? 650  LEU   A CB  1 
ATOM   6242  C  CG  . LEU   B 2 650  ? 132.083 111.715 61.008  1.00 78.72  ? 650  LEU   A CG  1 
ATOM   6243  C  CD1 . LEU   B 2 650  ? 130.676 111.798 61.565  1.00 80.88  ? 650  LEU   A CD1 1 
ATOM   6244  C  CD2 . LEU   B 2 650  ? 132.892 110.662 61.744  1.00 81.28  ? 650  LEU   A CD2 1 
ATOM   6245  N  N   . GLY   B 2 651  ? 133.230 113.575 57.522  1.00 80.43  ? 651  GLY   A N   1 
ATOM   6246  C  CA  . GLY   B 2 651  ? 134.193 114.641 57.339  1.00 80.61  ? 651  GLY   A CA  1 
ATOM   6247  C  C   . GLY   B 2 651  ? 133.816 115.734 56.366  1.00 80.10  ? 651  GLY   A C   1 
ATOM   6248  O  O   . GLY   B 2 651  ? 134.497 116.762 56.321  1.00 83.14  ? 651  GLY   A O   1 
ATOM   6249  N  N   . LEU   B 2 652  ? 132.758 115.552 55.582  1.00 79.05  ? 652  LEU   A N   1 
ATOM   6250  C  CA  . LEU   B 2 652  ? 132.354 116.553 54.606  1.00 80.46  ? 652  LEU   A CA  1 
ATOM   6251  C  C   . LEU   B 2 652  ? 131.041 117.245 54.933  1.00 82.28  ? 652  LEU   A C   1 
ATOM   6252  O  O   . LEU   B 2 652  ? 130.883 118.419 54.592  1.00 86.86  ? 652  LEU   A O   1 
ATOM   6253  C  CB  . LEU   B 2 652  ? 132.249 115.929 53.206  1.00 83.92  ? 652  LEU   A CB  1 
ATOM   6254  C  CG  . LEU   B 2 652  ? 133.531 115.884 52.372  1.00 85.36  ? 652  LEU   A CG  1 
ATOM   6255  C  CD1 . LEU   B 2 652  ? 134.178 117.261 52.309  1.00 86.27  ? 652  LEU   A CD1 1 
ATOM   6256  C  CD2 . LEU   B 2 652  ? 134.509 114.851 52.903  1.00 84.69  ? 652  LEU   A CD2 1 
ATOM   6257  N  N   . CYS   B 2 653  ? 130.098 116.559 55.578  1.00 84.65  ? 653  CYS   A N   1 
ATOM   6258  C  CA  . CYS   B 2 653  ? 128.825 117.165 55.964  1.00 86.54  ? 653  CYS   A CA  1 
ATOM   6259  C  C   . CYS   B 2 653  ? 129.020 117.877 57.300  1.00 91.33  ? 653  CYS   A C   1 
ATOM   6260  O  O   . CYS   B 2 653  ? 128.594 117.417 58.362  1.00 92.18  ? 653  CYS   A O   1 
ATOM   6261  C  CB  . CYS   B 2 653  ? 127.728 116.111 56.041  1.00 88.65  ? 653  CYS   A CB  1 
ATOM   6262  S  SG  . CYS   B 2 653  ? 126.098 116.747 56.495  1.00 93.17  ? 653  CYS   A SG  1 
ATOM   6263  N  N   . HIS   B 2 654  ? 129.687 119.027 57.240  1.00 88.76  ? 654  HIS   A N   1 
ATOM   6264  C  CA  . HIS   B 2 654  ? 130.005 119.779 58.445  1.00 81.87  ? 654  HIS   A CA  1 
ATOM   6265  C  C   . HIS   B 2 654  ? 130.215 121.242 58.088  1.00 85.63  ? 654  HIS   A C   1 
ATOM   6266  O  O   . HIS   B 2 654  ? 130.792 121.556 57.044  1.00 91.29  ? 654  HIS   A O   1 
ATOM   6267  C  CB  . HIS   B 2 654  ? 131.257 119.225 59.133  1.00 79.85  ? 654  HIS   A CB  1 
ATOM   6268  C  CG  . HIS   B 2 654  ? 132.505 119.366 58.319  1.00 81.53  ? 654  HIS   A CG  1 
ATOM   6269  N  ND1 . HIS   B 2 654  ? 133.722 119.693 58.876  1.00 85.51  ? 654  HIS   A ND1 1 
ATOM   6270  C  CD2 . HIS   B 2 654  ? 132.727 119.221 56.992  1.00 85.94  ? 654  HIS   A CD2 1 
ATOM   6271  C  CE1 . HIS   B 2 654  ? 134.639 119.747 57.927  1.00 85.97  ? 654  HIS   A CE1 1 
ATOM   6272  N  NE2 . HIS   B 2 654  ? 134.061 119.464 56.774  1.00 87.31  ? 654  HIS   A NE2 1 
ATOM   6273  N  N   . THR   B 2 655  ? 129.734 122.128 58.956  1.00 80.88  ? 655  THR   A N   1 
ATOM   6274  C  CA  . THR   B 2 655  ? 129.996 123.560 58.827  1.00 77.56  ? 655  THR   A CA  1 
ATOM   6275  C  C   . THR   B 2 655  ? 131.128 123.953 59.777  1.00 79.47  ? 655  THR   A C   1 
ATOM   6276  O  O   . THR   B 2 655  ? 130.954 124.698 60.742  1.00 82.33  ? 655  THR   A O   1 
ATOM   6277  C  CB  . THR   B 2 655  ? 128.726 124.359 59.099  1.00 78.86  ? 655  THR   A CB  1 
ATOM   6278  O  OG1 . THR   B 2 655  ? 127.621 123.737 58.433  1.00 82.98  ? 655  THR   A OG1 1 
ATOM   6279  C  CG2 . THR   B 2 655  ? 128.874 125.783 58.583  1.00 81.19  ? 655  THR   A CG2 1 
ATOM   6280  N  N   . VAL   B 2 656  ? 132.312 123.421 59.485  1.00 81.32  ? 656  VAL   A N   1 
ATOM   6281  C  CA  . VAL   B 2 656  ? 133.491 123.592 60.326  1.00 78.73  ? 656  VAL   A CA  1 
ATOM   6282  C  C   . VAL   B 2 656  ? 134.603 124.201 59.486  1.00 81.85  ? 656  VAL   A C   1 
ATOM   6283  O  O   . VAL   B 2 656  ? 134.823 123.785 58.343  1.00 86.62  ? 656  VAL   A O   1 
ATOM   6284  C  CB  . VAL   B 2 656  ? 133.947 122.258 60.944  1.00 83.74  ? 656  VAL   A CB  1 
ATOM   6285  C  CG1 . VAL   B 2 656  ? 135.126 122.476 61.878  1.00 83.82  ? 656  VAL   A CG1 1 
ATOM   6286  C  CG2 . VAL   B 2 656  ? 132.795 121.586 61.673  1.00 85.88  ? 656  VAL   A CG2 1 
ATOM   6287  N  N   . LEU   B 2 657  ? 135.298 125.184 60.051  1.00 88.99  ? 657  LEU   A N   1 
ATOM   6288  C  CA  . LEU   B 2 657  ? 136.423 125.825 59.386  1.00 90.30  ? 657  LEU   A CA  1 
ATOM   6289  C  C   . LEU   B 2 657  ? 137.728 125.237 59.906  1.00 89.38  ? 657  LEU   A C   1 
ATOM   6290  O  O   . LEU   B 2 657  ? 137.894 125.051 61.115  1.00 90.55  ? 657  LEU   A O   1 
ATOM   6291  C  CB  . LEU   B 2 657  ? 136.402 127.339 59.610  1.00 92.79  ? 657  LEU   A CB  1 
ATOM   6292  C  CG  . LEU   B 2 657  ? 135.382 128.175 58.828  1.00 93.78  ? 657  LEU   A CG  1 
ATOM   6293  C  CD1 . LEU   B 2 657  ? 133.979 128.047 59.409  1.00 90.95  ? 657  LEU   A CD1 1 
ATOM   6294  C  CD2 . LEU   B 2 657  ? 135.814 129.634 58.778  1.00 90.88  ? 657  LEU   A CD2 1 
ATOM   6295  N  N   . ALA   B 2 658  ? 138.647 124.946 58.991  1.00 98.51  ? 658  ALA   A N   1 
ATOM   6296  C  CA  . ALA   B 2 658  ? 139.946 124.379 59.325  1.00 100.64 ? 658  ALA   A CA  1 
ATOM   6297  C  C   . ALA   B 2 658  ? 141.023 125.439 59.151  1.00 99.34  ? 658  ALA   A C   1 
ATOM   6298  O  O   . ALA   B 2 658  ? 141.083 126.106 58.112  1.00 98.28  ? 658  ALA   A O   1 
ATOM   6299  C  CB  . ALA   B 2 658  ? 140.253 123.160 58.454  1.00 101.23 ? 658  ALA   A CB  1 
ATOM   6300  N  N   . ALA   B 2 659  ? 141.871 125.588 60.164  1.00 117.35 ? 659  ALA   A N   1 
ATOM   6301  C  CA  . ALA   B 2 659  ? 142.934 126.583 60.162  1.00 120.17 ? 659  ALA   A CA  1 
ATOM   6302  C  C   . ALA   B 2 659  ? 144.272 125.911 59.885  1.00 120.77 ? 659  ALA   A C   1 
ATOM   6303  O  O   . ALA   B 2 659  ? 144.588 124.877 60.483  1.00 120.12 ? 659  ALA   A O   1 
ATOM   6304  C  CB  . ALA   B 2 659  ? 142.983 127.330 61.495  1.00 119.80 ? 659  ALA   A CB  1 
ATOM   6305  N  N   . GLU   B 2 660  ? 145.053 126.502 58.980  1.00 138.33 ? 660  GLU   A N   1 
ATOM   6306  C  CA  . GLU   B 2 660  ? 146.364 125.988 58.604  1.00 138.06 ? 660  GLU   A CA  1 
ATOM   6307  C  C   . GLU   B 2 660  ? 147.498 126.725 59.309  1.00 138.13 ? 660  GLU   A C   1 
ATOM   6308  O  O   . GLU   B 2 660  ? 148.574 126.908 58.728  1.00 137.77 ? 660  GLU   A O   1 
ATOM   6309  C  CB  . GLU   B 2 660  ? 146.546 126.063 57.088  1.00 138.62 ? 660  GLU   A CB  1 
ATOM   6310  C  CG  . GLU   B 2 660  ? 145.641 125.129 56.300  1.00 138.58 ? 660  GLU   A CG  1 
ATOM   6311  C  CD  . GLU   B 2 660  ? 146.080 123.680 56.384  1.00 139.07 ? 660  GLU   A CD  1 
ATOM   6312  O  OE1 . GLU   B 2 660  ? 147.235 123.429 56.789  1.00 139.41 ? 660  GLU   A OE1 1 
ATOM   6313  O  OE2 . GLU   B 2 660  ? 145.271 122.792 56.042  1.00 138.55 ? 660  GLU   A OE2 1 
ATOM   6314  N  N   . THR   B 2 661  ? 147.275 127.159 60.552  1.00 142.99 ? 661  THR   A N   1 
ATOM   6315  C  CA  . THR   B 2 661  ? 148.317 127.871 61.286  1.00 143.39 ? 661  THR   A CA  1 
ATOM   6316  C  C   . THR   B 2 661  ? 149.528 126.980 61.538  1.00 143.88 ? 661  THR   A C   1 
ATOM   6317  O  O   . THR   B 2 661  ? 150.674 127.431 61.424  1.00 143.66 ? 661  THR   A O   1 
ATOM   6318  C  CB  . THR   B 2 661  ? 147.759 128.413 62.604  1.00 143.05 ? 661  THR   A CB  1 
ATOM   6319  O  OG1 . THR   B 2 661  ? 148.839 128.808 63.459  1.00 143.53 ? 661  THR   A OG1 1 
ATOM   6320  C  CG2 . THR   B 2 661  ? 146.909 127.361 63.307  1.00 142.36 ? 661  THR   A CG2 1 
ATOM   6321  N  N   . GLU   B 2 662  ? 149.297 125.715 61.882  1.00 143.64 ? 662  GLU   A N   1 
ATOM   6322  C  CA  . GLU   B 2 662  ? 150.371 124.757 62.120  1.00 143.29 ? 662  GLU   A CA  1 
ATOM   6323  C  C   . GLU   B 2 662  ? 150.143 123.555 61.214  1.00 142.84 ? 662  GLU   A C   1 
ATOM   6324  O  O   . GLU   B 2 662  ? 149.071 122.920 61.291  1.00 141.71 ? 662  GLU   A O   1 
ATOM   6325  C  CB  . GLU   B 2 662  ? 150.425 124.335 63.590  1.00 142.92 ? 662  GLU   A CB  1 
ATOM   6326  C  CG  . GLU   B 2 662  ? 150.718 125.475 64.552  1.00 142.53 ? 662  GLU   A CG  1 
ATOM   6327  C  CD  . GLU   B 2 662  ? 150.806 125.013 65.993  1.00 142.98 ? 662  GLU   A CD  1 
ATOM   6328  O  OE1 . GLU   B 2 662  ? 150.637 123.801 66.242  1.00 143.00 ? 662  GLU   A OE1 1 
ATOM   6329  O  OE2 . GLU   B 2 662  ? 151.044 125.863 66.878  1.00 143.50 ? 662  GLU   A OE2 1 
ATOM   6330  N  N   . PRO   B 2 663  ? 151.091 123.214 60.341  1.00 140.23 ? 663  PRO   A N   1 
ATOM   6331  C  CA  . PRO   B 2 663  ? 150.905 122.046 59.471  1.00 139.32 ? 663  PRO   A CA  1 
ATOM   6332  C  C   . PRO   B 2 663  ? 150.748 120.769 60.283  1.00 139.09 ? 663  PRO   A C   1 
ATOM   6333  O  O   . PRO   B 2 663  ? 151.390 120.584 61.319  1.00 138.83 ? 663  PRO   A O   1 
ATOM   6334  C  CB  . PRO   B 2 663  ? 152.185 122.024 58.628  1.00 138.38 ? 663  PRO   A CB  1 
ATOM   6335  C  CG  . PRO   B 2 663  ? 152.708 123.425 58.689  1.00 138.33 ? 663  PRO   A CG  1 
ATOM   6336  C  CD  . PRO   B 2 663  ? 152.346 123.927 60.053  1.00 139.23 ? 663  PRO   A CD  1 
ATOM   6337  N  N   . GLY   B 2 664  ? 149.873 119.890 59.802  1.00 134.11 ? 664  GLY   A N   1 
ATOM   6338  C  CA  . GLY   B 2 664  ? 149.599 118.625 60.475  1.00 133.55 ? 664  GLY   A CA  1 
ATOM   6339  C  C   . GLY   B 2 664  ? 148.520 118.671 61.536  1.00 133.85 ? 664  GLY   A C   1 
ATOM   6340  O  O   . GLY   B 2 664  ? 147.661 117.791 61.587  1.00 132.77 ? 664  GLY   A O   1 
ATOM   6341  N  N   . VAL   B 2 665  ? 148.528 119.738 62.342  1.00 129.69 ? 665  VAL   A N   1 
ATOM   6342  C  CA  . VAL   B 2 665  ? 147.483 119.916 63.394  1.00 129.63 ? 665  VAL   A CA  1 
ATOM   6343  C  C   . VAL   B 2 665  ? 146.122 120.109 62.716  1.00 127.35 ? 665  VAL   A C   1 
ATOM   6344  O  O   . VAL   B 2 665  ? 145.159 119.435 63.131  1.00 125.82 ? 665  VAL   A O   1 
ATOM   6345  C  CB  . VAL   B 2 665  ? 147.818 121.110 64.309  1.00 127.57 ? 665  VAL   A CB  1 
ATOM   6346  C  CG1 . VAL   B 2 665  ? 146.712 121.378 65.318  1.00 126.34 ? 665  VAL   A CG1 1 
ATOM   6347  C  CG2 . VAL   B 2 665  ? 149.156 120.928 65.008  1.00 127.16 ? 665  VAL   A CG2 1 
ATOM   6348  N  N   . ILE   B 2 666  ? 146.052 120.993 61.715  1.00 115.94 ? 666  ILE   A N   1 
ATOM   6349  C  CA  . ILE   B 2 666  ? 144.766 121.276 61.006  1.00 115.41 ? 666  ILE   A CA  1 
ATOM   6350  C  C   . ILE   B 2 666  ? 143.708 121.664 62.046  1.00 116.09 ? 666  ILE   A C   1 
ATOM   6351  O  O   . ILE   B 2 666  ? 142.657 120.993 62.099  1.00 116.64 ? 666  ILE   A O   1 
ATOM   6352  C  CB  . ILE   B 2 666  ? 144.327 120.070 60.151  1.00 115.93 ? 666  ILE   A CB  1 
ATOM   6353  C  CG1 . ILE   B 2 666  ? 145.516 119.411 59.447  1.00 117.36 ? 666  ILE   A CG1 1 
ATOM   6354  C  CG2 . ILE   B 2 666  ? 143.243 120.476 59.166  1.00 114.36 ? 666  ILE   A CG2 1 
ATOM   6355  C  CD1 . ILE   B 2 666  ? 146.275 120.338 58.526  1.00 116.64 ? 666  ILE   A CD1 1 
ATOM   6356  N  N   . GLU   B 2 667  ? 143.984 122.700 62.843  1.00 114.47 ? 667  GLU   A N   1 
ATOM   6357  C  CA  . GLU   B 2 667  ? 143.031 123.163 63.888  1.00 113.64 ? 667  GLU   A CA  1 
ATOM   6358  C  C   . GLU   B 2 667  ? 141.611 123.195 63.312  1.00 113.03 ? 667  GLU   A C   1 
ATOM   6359  O  O   . GLU   B 2 667  ? 141.432 123.787 62.229  1.00 113.47 ? 667  GLU   A O   1 
ATOM   6360  C  CB  . GLU   B 2 667  ? 143.446 124.552 64.378  1.00 113.60 ? 667  GLU   A CB  1 
ATOM   6361  C  CG  . GLU   B 2 667  ? 143.174 124.801 65.852  1.00 114.99 ? 667  GLU   A CG  1 
ATOM   6362  C  CD  . GLU   B 2 667  ? 141.721 125.029 66.229  1.00 115.59 ? 667  GLU   A CD  1 
ATOM   6363  O  OE1 . GLU   B 2 667  ? 140.915 124.094 66.071  1.00 116.08 ? 667  GLU   A OE1 1 
ATOM   6364  O  OE2 . GLU   B 2 667  ? 141.400 126.146 66.680  1.00 114.20 ? 667  GLU   A OE2 1 
ATOM   6365  N  N   . TYR   B 2 668  ? 140.644 122.587 64.008  1.00 94.36  ? 668  TYR   A N   1 
ATOM   6366  C  CA  . TYR   B 2 668  ? 139.257 122.623 63.555  1.00 93.20  ? 668  TYR   A CA  1 
ATOM   6367  C  C   . TYR   B 2 668  ? 138.454 123.524 64.486  1.00 93.75  ? 668  TYR   A C   1 
ATOM   6368  O  O   . TYR   B 2 668  ? 138.283 123.213 65.669  1.00 95.28  ? 668  TYR   A O   1 
ATOM   6369  C  CB  . TYR   B 2 668  ? 138.670 121.215 63.516  1.00 95.74  ? 668  TYR   A CB  1 
ATOM   6370  C  CG  . TYR   B 2 668  ? 139.272 120.320 62.459  1.00 94.42  ? 668  TYR   A CG  1 
ATOM   6371  C  CD1 . TYR   B 2 668  ? 139.388 120.745 61.145  1.00 93.19  ? 668  TYR   A CD1 1 
ATOM   6372  C  CD2 . TYR   B 2 668  ? 139.730 119.051 62.779  1.00 94.99  ? 668  TYR   A CD2 1 
ATOM   6373  C  CE1 . TYR   B 2 668  ? 139.938 119.929 60.177  1.00 94.88  ? 668  TYR   A CE1 1 
ATOM   6374  C  CE2 . TYR   B 2 668  ? 140.283 118.229 61.820  1.00 94.36  ? 668  TYR   A CE2 1 
ATOM   6375  C  CZ  . TYR   B 2 668  ? 140.384 118.673 60.521  1.00 95.32  ? 668  TYR   A CZ  1 
ATOM   6376  O  OH  . TYR   B 2 668  ? 140.935 117.856 59.561  1.00 95.96  ? 668  TYR   A OH  1 
ATOM   6377  N  N   . LYS   B 2 669  ? 137.954 124.637 63.951  1.00 88.99  ? 669  LYS   A N   1 
ATOM   6378  C  CA  . LYS   B 2 669  ? 137.134 125.573 64.718  1.00 87.71  ? 669  LYS   A CA  1 
ATOM   6379  C  C   . LYS   B 2 669  ? 135.678 125.334 64.347  1.00 86.44  ? 669  LYS   A C   1 
ATOM   6380  O  O   . LYS   B 2 669  ? 135.184 125.818 63.328  1.00 84.50  ? 669  LYS   A O   1 
ATOM   6381  C  CB  . LYS   B 2 669  ? 137.561 127.011 64.451  1.00 89.19  ? 669  LYS   A CB  1 
ATOM   6382  C  CG  . LYS   B 2 669  ? 138.970 127.335 64.917  1.00 91.43  ? 669  LYS   A CG  1 
ATOM   6383  C  CD  . LYS   B 2 669  ? 139.327 128.784 64.629  1.00 88.70  ? 669  LYS   A CD  1 
ATOM   6384  C  CE  . LYS   B 2 669  ? 140.713 129.125 65.152  1.00 89.41  ? 669  LYS   A CE  1 
ATOM   6385  N  NZ  . LYS   B 2 669  ? 141.766 128.265 64.543  1.00 91.75  ? 669  LYS   A NZ  1 
ATOM   6386  N  N   . ALA   B 2 670  ? 135.000 124.579 65.167  1.00 81.91  ? 670  ALA   A N   1 
ATOM   6387  C  CA  . ALA   B 2 670  ? 133.623 124.202 64.896  1.00 78.41  ? 670  ALA   A CA  1 
ATOM   6388  C  C   . ALA   B 2 670  ? 132.662 124.974 65.788  1.00 79.26  ? 670  ALA   A C   1 
ATOM   6389  O  O   . ALA   B 2 670  ? 133.001 125.376 66.904  1.00 83.33  ? 670  ALA   A O   1 
ATOM   6390  C  CB  . ALA   B 2 670  ? 133.421 122.702 65.100  1.00 80.32  ? 670  ALA   A CB  1 
ATOM   6391  N  N   . GLN   B 2 671  ? 131.448 125.174 65.279  1.00 73.64  ? 671  GLN   A N   1 
ATOM   6392  C  CA  . GLN   B 2 671  ? 130.411 125.882 66.013  1.00 73.22  ? 671  GLN   A CA  1 
ATOM   6393  C  C   . GLN   B 2 671  ? 129.691 124.998 67.021  1.00 74.11  ? 671  GLN   A C   1 
ATOM   6394  O  O   . GLN   B 2 671  ? 128.969 125.522 67.876  1.00 81.42  ? 671  GLN   A O   1 
ATOM   6395  C  CB  . GLN   B 2 671  ? 129.402 126.477 65.029  1.00 71.58  ? 671  GLN   A CB  1 
ATOM   6396  C  CG  . GLN   B 2 671  ? 128.632 127.665 65.561  1.00 72.33  ? 671  GLN   A CG  1 
ATOM   6397  C  CD  . GLN   B 2 671  ? 127.935 128.441 64.466  1.00 78.75  ? 671  GLN   A CD  1 
ATOM   6398  O  OE1 . GLN   B 2 671  ? 127.381 129.513 64.707  1.00 83.26  ? 671  GLN   A OE1 1 
ATOM   6399  N  NE2 . GLN   B 2 671  ? 127.961 127.907 63.251  1.00 74.73  ? 671  GLN   A NE2 1 
ATOM   6400  N  N   . SER   B 2 672  ? 129.871 123.682 66.947  1.00 81.02  ? 672  SER   A N   1 
ATOM   6401  C  CA  . SER   B 2 672  ? 129.237 122.747 67.859  1.00 83.69  ? 672  SER   A CA  1 
ATOM   6402  C  C   . SER   B 2 672  ? 130.262 121.742 68.361  1.00 82.40  ? 672  SER   A C   1 
ATOM   6403  O  O   . SER   B 2 672  ? 131.129 121.303 67.595  1.00 85.84  ? 672  SER   A O   1 
ATOM   6404  C  CB  . SER   B 2 672  ? 128.080 122.009 67.172  1.00 84.37  ? 672  SER   A CB  1 
ATOM   6405  O  OG  . SER   B 2 672  ? 127.568 120.979 67.999  1.00 86.03  ? 672  SER   A OG  1 
ATOM   6406  N  N   . PRO   B 2 673  ? 130.199 121.367 69.640  1.00 70.36  ? 673  PRO   A N   1 
ATOM   6407  C  CA  . PRO   B 2 673  ? 131.137 120.352 70.147  1.00 71.94  ? 673  PRO   A CA  1 
ATOM   6408  C  C   . PRO   B 2 673  ? 131.003 119.011 69.449  1.00 74.86  ? 673  PRO   A C   1 
ATOM   6409  O  O   . PRO   B 2 673  ? 132.011 118.319 69.251  1.00 76.24  ? 673  PRO   A O   1 
ATOM   6410  C  CB  . PRO   B 2 673  ? 130.776 120.259 71.635  1.00 72.95  ? 673  PRO   A CB  1 
ATOM   6411  C  CG  . PRO   B 2 673  ? 129.363 120.734 71.712  1.00 70.99  ? 673  PRO   A CG  1 
ATOM   6412  C  CD  . PRO   B 2 673  ? 129.242 121.801 70.670  1.00 73.25  ? 673  PRO   A CD  1 
ATOM   6413  N  N   . ASP   B 2 674  ? 129.784 118.629 69.063  1.00 80.59  ? 674  ASP   A N   1 
ATOM   6414  C  CA  . ASP   B 2 674  ? 129.582 117.358 68.377  1.00 77.49  ? 674  ASP   A CA  1 
ATOM   6415  C  C   . ASP   B 2 674  ? 130.315 117.334 67.044  1.00 79.41  ? 674  ASP   A C   1 
ATOM   6416  O  O   . ASP   B 2 674  ? 131.005 116.361 66.718  1.00 87.80  ? 674  ASP   A O   1 
ATOM   6417  C  CB  . ASP   B 2 674  ? 128.089 117.109 68.170  1.00 79.34  ? 674  ASP   A CB  1 
ATOM   6418  C  CG  . ASP   B 2 674  ? 127.279 117.371 69.419  1.00 84.67  ? 674  ASP   A CG  1 
ATOM   6419  O  OD1 . ASP   B 2 674  ? 127.820 117.185 70.529  1.00 87.01  ? 674  ASP   A OD1 1 
ATOM   6420  O  OD2 . ASP   B 2 674  ? 126.100 117.762 69.293  1.00 86.06  ? 674  ASP   A OD2 1 
ATOM   6421  N  N   . GLU   B 2 675  ? 130.176 118.404 66.258  1.00 74.31  ? 675  GLU   A N   1 
ATOM   6422  C  CA  . GLU   B 2 675  ? 130.843 118.458 64.962  1.00 75.79  ? 675  GLU   A CA  1 
ATOM   6423  C  C   . GLU   B 2 675  ? 132.356 118.465 65.120  1.00 73.85  ? 675  GLU   A C   1 
ATOM   6424  O  O   . GLU   B 2 675  ? 133.069 117.803 64.356  1.00 80.56  ? 675  GLU   A O   1 
ATOM   6425  C  CB  . GLU   B 2 675  ? 130.378 119.687 64.182  1.00 80.66  ? 675  GLU   A CB  1 
ATOM   6426  C  CG  . GLU   B 2 675  ? 128.932 119.620 63.720  1.00 82.27  ? 675  GLU   A CG  1 
ATOM   6427  C  CD  . GLU   B 2 675  ? 128.711 118.586 62.631  1.00 83.30  ? 675  GLU   A CD  1 
ATOM   6428  O  OE1 . GLU   B 2 675  ? 129.695 118.189 61.972  1.00 82.45  ? 675  GLU   A OE1 1 
ATOM   6429  O  OE2 . GLU   B 2 675  ? 127.550 118.168 62.434  1.00 81.95  ? 675  GLU   A OE2 1 
ATOM   6430  N  N   . ALA   B 2 676  ? 132.865 119.212 66.102  1.00 66.38  ? 676  ALA   A N   1 
ATOM   6431  C  CA  . ALA   B 2 676  ? 134.305 119.245 66.332  1.00 70.97  ? 676  ALA   A CA  1 
ATOM   6432  C  C   . ALA   B 2 676  ? 134.829 117.862 66.689  1.00 72.93  ? 676  ALA   A C   1 
ATOM   6433  O  O   . ALA   B 2 676  ? 135.842 117.407 66.142  1.00 77.17  ? 676  ALA   A O   1 
ATOM   6434  C  CB  . ALA   B 2 676  ? 134.636 120.247 67.436  1.00 73.11  ? 676  ALA   A CB  1 
ATOM   6435  N  N   . ALA   B 2 677  ? 134.136 117.170 67.596  1.00 77.68  ? 677  ALA   A N   1 
ATOM   6436  C  CA  . ALA   B 2 677  ? 134.561 115.829 67.981  1.00 75.59  ? 677  ALA   A CA  1 
ATOM   6437  C  C   . ALA   B 2 677  ? 134.508 114.872 66.799  1.00 71.92  ? 677  ALA   A C   1 
ATOM   6438  O  O   . ALA   B 2 677  ? 135.431 114.075 66.597  1.00 76.37  ? 677  ALA   A O   1 
ATOM   6439  C  CB  . ALA   B 2 677  ? 133.694 115.314 69.130  1.00 74.96  ? 677  ALA   A CB  1 
ATOM   6440  N  N   . LEU   B 2 678  ? 133.441 114.941 66.000  1.00 63.38  ? 678  LEU   A N   1 
ATOM   6441  C  CA  . LEU   B 2 678  ? 133.308 114.032 64.867  1.00 62.74  ? 678  LEU   A CA  1 
ATOM   6442  C  C   . LEU   B 2 678  ? 134.402 114.267 63.833  1.00 70.17  ? 678  LEU   A C   1 
ATOM   6443  O  O   . LEU   B 2 678  ? 134.998 113.314 63.317  1.00 75.89  ? 678  LEU   A O   1 
ATOM   6444  C  CB  . LEU   B 2 678  ? 131.926 114.183 64.235  1.00 60.99  ? 678  LEU   A CB  1 
ATOM   6445  C  CG  . LEU   B 2 678  ? 130.763 113.620 65.047  1.00 64.00  ? 678  LEU   A CG  1 
ATOM   6446  C  CD1 . LEU   B 2 678  ? 129.448 113.887 64.345  1.00 68.70  ? 678  LEU   A CD1 1 
ATOM   6447  C  CD2 . LEU   B 2 678  ? 130.950 112.134 65.289  1.00 72.58  ? 678  LEU   A CD2 1 
ATOM   6448  N  N   . VAL   B 2 679  ? 134.687 115.533 63.521  1.00 73.72  ? 679  VAL   A N   1 
ATOM   6449  C  CA  . VAL   B 2 679  ? 135.711 115.828 62.524  1.00 71.09  ? 679  VAL   A CA  1 
ATOM   6450  C  C   . VAL   B 2 679  ? 137.090 115.434 63.035  1.00 74.04  ? 679  VAL   A C   1 
ATOM   6451  O  O   . VAL   B 2 679  ? 137.908 114.882 62.287  1.00 78.09  ? 679  VAL   A O   1 
ATOM   6452  C  CB  . VAL   B 2 679  ? 135.651 117.311 62.116  1.00 73.28  ? 679  VAL   A CB  1 
ATOM   6453  C  CG1 . VAL   B 2 679  ? 136.820 117.664 61.214  1.00 78.21  ? 679  VAL   A CG1 1 
ATOM   6454  C  CG2 . VAL   B 2 679  ? 134.342 117.603 61.410  1.00 72.39  ? 679  VAL   A CG2 1 
ATOM   6455  N  N   . GLN   B 2 680  ? 137.375 115.701 64.314  1.00 80.27  ? 680  GLN   A N   1 
ATOM   6456  C  CA  . GLN   B 2 680  ? 138.662 115.302 64.872  1.00 81.78  ? 680  GLN   A CA  1 
ATOM   6457  C  C   . GLN   B 2 680  ? 138.823 113.788 64.861  1.00 82.79  ? 680  GLN   A C   1 
ATOM   6458  O  O   . GLN   B 2 680  ? 139.902 113.274 64.542  1.00 84.66  ? 680  GLN   A O   1 
ATOM   6459  C  CB  . GLN   B 2 680  ? 138.816 115.849 66.290  1.00 84.33  ? 680  GLN   A CB  1 
ATOM   6460  C  CG  . GLN   B 2 680  ? 140.150 115.516 66.938  1.00 84.35  ? 680  GLN   A CG  1 
ATOM   6461  C  CD  . GLN   B 2 680  ? 141.325 116.158 66.225  1.00 84.27  ? 680  GLN   A CD  1 
ATOM   6462  O  OE1 . GLN   B 2 680  ? 141.179 117.181 65.556  1.00 82.98  ? 680  GLN   A OE1 1 
ATOM   6463  N  NE2 . GLN   B 2 680  ? 142.501 115.558 66.366  1.00 83.84  ? 680  GLN   A NE2 1 
ATOM   6464  N  N   . SER   B 2 681  ? 137.761 113.054 65.203  1.00 78.25  ? 681  SER   A N   1 
ATOM   6465  C  CA  . SER   B 2 681  ? 137.832 111.599 65.168  1.00 78.30  ? 681  SER   A CA  1 
ATOM   6466  C  C   . SER   B 2 681  ? 138.035 111.088 63.748  1.00 77.72  ? 681  SER   A C   1 
ATOM   6467  O  O   . SER   B 2 681  ? 138.829 110.168 63.522  1.00 80.00  ? 681  SER   A O   1 
ATOM   6468  C  CB  . SER   B 2 681  ? 136.568 110.999 65.777  1.00 79.66  ? 681  SER   A CB  1 
ATOM   6469  O  OG  . SER   B 2 681  ? 135.422 111.359 65.026  1.00 79.91  ? 681  SER   A OG  1 
ATOM   6470  N  N   . ALA   B 2 682  ? 137.332 111.675 62.777  1.00 74.71  ? 682  ALA   A N   1 
ATOM   6471  C  CA  . ALA   B 2 682  ? 137.510 111.261 61.390  1.00 74.68  ? 682  ALA   A CA  1 
ATOM   6472  C  C   . ALA   B 2 682  ? 138.937 111.508 60.923  1.00 77.70  ? 682  ALA   A C   1 
ATOM   6473  O  O   . ALA   B 2 682  ? 139.525 110.672 60.228  1.00 84.61  ? 682  ALA   A O   1 
ATOM   6474  C  CB  . ALA   B 2 682  ? 136.515 111.991 60.490  1.00 76.53  ? 682  ALA   A CB  1 
ATOM   6475  N  N   . ALA   B 2 683  ? 139.511 112.653 61.297  1.00 80.47  ? 683  ALA   A N   1 
ATOM   6476  C  CA  . ALA   B 2 683  ? 140.894 112.938 60.932  1.00 79.90  ? 683  ALA   A CA  1 
ATOM   6477  C  C   . ALA   B 2 683  ? 141.858 111.968 61.602  1.00 78.89  ? 683  ALA   A C   1 
ATOM   6478  O  O   . ALA   B 2 683  ? 142.823 111.512 60.978  1.00 82.75  ? 683  ALA   A O   1 
ATOM   6479  C  CB  . ALA   B 2 683  ? 141.246 114.380 61.293  1.00 83.68  ? 683  ALA   A CB  1 
ATOM   6480  N  N   . ASP   B 2 684  ? 141.616 111.640 62.872  1.00 82.04  ? 684  ASP   A N   1 
ATOM   6481  C  CA  . ASP   B 2 684  ? 142.545 110.784 63.602  1.00 86.31  ? 684  ASP   A CA  1 
ATOM   6482  C  C   . ASP   B 2 684  ? 142.464 109.333 63.147  1.00 86.11  ? 684  ASP   A C   1 
ATOM   6483  O  O   . ASP   B 2 684  ? 143.458 108.603 63.235  1.00 85.79  ? 684  ASP   A O   1 
ATOM   6484  C  CB  . ASP   B 2 684  ? 142.276 110.882 65.104  1.00 90.21  ? 684  ASP   A CB  1 
ATOM   6485  C  CG  . ASP   B 2 684  ? 143.227 110.033 65.925  1.00 92.28  ? 684  ASP   A CG  1 
ATOM   6486  O  OD1 . ASP   B 2 684  ? 144.423 110.385 66.005  1.00 90.81  ? 684  ASP   A OD1 1 
ATOM   6487  O  OD2 . ASP   B 2 684  ? 142.779 109.013 66.490  1.00 89.44  ? 684  ASP   A OD2 1 
ATOM   6488  N  N   . VAL   B 2 685  ? 141.306 108.897 62.656  1.00 79.35  ? 685  VAL   A N   1 
ATOM   6489  C  CA  . VAL   B 2 685  ? 141.110 107.496 62.301  1.00 78.49  ? 685  VAL   A CA  1 
ATOM   6490  C  C   . VAL   B 2 685  ? 140.904 107.392 60.795  1.00 76.30  ? 685  VAL   A C   1 
ATOM   6491  O  O   . VAL   B 2 685  ? 140.128 106.559 60.315  1.00 77.34  ? 685  VAL   A O   1 
ATOM   6492  C  CB  . VAL   B 2 685  ? 139.935 106.875 63.081  1.00 84.36  ? 685  VAL   A CB  1 
ATOM   6493  C  CG1 . VAL   B 2 685  ? 140.036 105.351 63.093  1.00 85.05  ? 685  VAL   A CG1 1 
ATOM   6494  C  CG2 . VAL   B 2 685  ? 139.907 107.400 64.507  1.00 81.54  ? 685  VAL   A CG2 1 
ATOM   6495  N  N   . GLY   B 2 686  ? 141.583 108.250 60.040  1.00 82.58  ? 686  GLY   A N   1 
ATOM   6496  C  CA  . GLY   B 2 686  ? 141.494 108.178 58.597  1.00 84.18  ? 686  GLY   A CA  1 
ATOM   6497  C  C   . GLY   B 2 686  ? 141.339 109.509 57.895  1.00 86.53  ? 686  GLY   A C   1 
ATOM   6498  O  O   . GLY   B 2 686  ? 142.228 110.362 57.956  1.00 85.29  ? 686  GLY   A O   1 
ATOM   6499  N  N   . PHE   B 2 687  ? 140.211 109.681 57.208  1.00 96.69  ? 687  PHE   A N   1 
ATOM   6500  C  CA  . PHE   B 2 687  ? 139.989 110.841 56.354  1.00 96.55  ? 687  PHE   A CA  1 
ATOM   6501  C  C   . PHE   B 2 687  ? 140.141 112.139 57.139  1.00 99.08  ? 687  PHE   A C   1 
ATOM   6502  O  O   . PHE   B 2 687  ? 139.328 112.444 58.017  1.00 99.35  ? 687  PHE   A O   1 
ATOM   6503  C  CB  . PHE   B 2 687  ? 138.597 110.759 55.730  1.00 96.61  ? 687  PHE   A CB  1 
ATOM   6504  C  CG  . PHE   B 2 687  ? 138.419 109.605 54.781  1.00 100.47 ? 687  PHE   A CG  1 
ATOM   6505  C  CD1 . PHE   B 2 687  ? 138.248 108.315 55.256  1.00 96.85  ? 687  PHE   A CD1 1 
ATOM   6506  C  CD2 . PHE   B 2 687  ? 138.407 109.815 53.412  1.00 100.93 ? 687  PHE   A CD2 1 
ATOM   6507  C  CE1 . PHE   B 2 687  ? 138.080 107.257 54.388  1.00 96.85  ? 687  PHE   A CE1 1 
ATOM   6508  C  CE2 . PHE   B 2 687  ? 138.237 108.759 52.536  1.00 98.70  ? 687  PHE   A CE2 1 
ATOM   6509  C  CZ  . PHE   B 2 687  ? 138.075 107.479 53.025  1.00 98.08  ? 687  PHE   A CZ  1 
ATOM   6510  N  N   . VAL   B 2 688  ? 141.177 112.906 56.809  1.00 100.52 ? 688  VAL   A N   1 
ATOM   6511  C  CA  . VAL   B 2 688  ? 141.460 114.190 57.441  1.00 99.65  ? 688  VAL   A CA  1 
ATOM   6512  C  C   . VAL   B 2 688  ? 140.846 115.285 56.583  1.00 99.29  ? 688  VAL   A C   1 
ATOM   6513  O  O   . VAL   B 2 688  ? 140.933 115.239 55.351  1.00 99.10  ? 688  VAL   A O   1 
ATOM   6514  C  CB  . VAL   B 2 688  ? 142.973 114.415 57.615  1.00 98.92  ? 688  VAL   A CB  1 
ATOM   6515  C  CG1 . VAL   B 2 688  ? 143.238 115.717 58.357  1.00 100.12 ? 688  VAL   A CG1 1 
ATOM   6516  C  CG2 . VAL   B 2 688  ? 143.608 113.245 58.342  1.00 98.22  ? 688  VAL   A CG2 1 
ATOM   6517  N  N   . PHE   B 2 689  ? 140.212 116.259 57.230  1.00 101.70 ? 689  PHE   A N   1 
ATOM   6518  C  CA  . PHE   B 2 689  ? 139.634 117.391 56.518  1.00 101.93 ? 689  PHE   A CA  1 
ATOM   6519  C  C   . PHE   B 2 689  ? 140.703 118.453 56.300  1.00 104.10 ? 689  PHE   A C   1 
ATOM   6520  O  O   . PHE   B 2 689  ? 141.335 118.913 57.258  1.00 105.99 ? 689  PHE   A O   1 
ATOM   6521  C  CB  . PHE   B 2 689  ? 138.450 117.965 57.291  1.00 101.11 ? 689  PHE   A CB  1 
ATOM   6522  C  CG  . PHE   B 2 689  ? 137.813 119.147 56.624  1.00 100.49 ? 689  PHE   A CG  1 
ATOM   6523  C  CD1 . PHE   B 2 689  ? 137.167 119.006 55.410  1.00 99.38  ? 689  PHE   A CD1 1 
ATOM   6524  C  CD2 . PHE   B 2 689  ? 137.857 120.398 57.212  1.00 102.32 ? 689  PHE   A CD2 1 
ATOM   6525  C  CE1 . PHE   B 2 689  ? 136.579 120.092 54.791  1.00 100.38 ? 689  PHE   A CE1 1 
ATOM   6526  C  CE2 . PHE   B 2 689  ? 137.269 121.487 56.600  1.00 102.95 ? 689  PHE   A CE2 1 
ATOM   6527  C  CZ  . PHE   B 2 689  ? 136.631 121.334 55.387  1.00 101.34 ? 689  PHE   A CZ  1 
ATOM   6528  N  N   . ARG   B 2 690  ? 140.905 118.844 55.041  1.00 103.26 ? 690  ARG   A N   1 
ATOM   6529  C  CA  . ARG   B 2 690  ? 141.927 119.835 54.723  1.00 104.56 ? 690  ARG   A CA  1 
ATOM   6530  C  C   . ARG   B 2 690  ? 141.470 121.237 55.103  1.00 106.20 ? 690  ARG   A C   1 
ATOM   6531  O  O   . ARG   B 2 690  ? 142.101 121.907 55.927  1.00 108.73 ? 690  ARG   A O   1 
ATOM   6532  C  CB  . ARG   B 2 690  ? 142.280 119.768 53.235  1.00 103.85 ? 690  ARG   A CB  1 
ATOM   6533  C  CG  . ARG   B 2 690  ? 143.261 120.843 52.780  1.00 106.85 ? 690  ARG   A CG  1 
ATOM   6534  C  CD  . ARG   B 2 690  ? 144.700 120.339 52.732  1.00 106.79 ? 690  ARG   A CD  1 
ATOM   6535  N  NE  . ARG   B 2 690  ? 145.092 119.623 53.941  1.00 106.06 ? 690  ARG   A NE  1 
ATOM   6536  C  CZ  . ARG   B 2 690  ? 145.199 118.305 54.025  1.00 105.86 ? 690  ARG   A CZ  1 
ATOM   6537  N  NH1 . ARG   B 2 690  ? 144.964 117.525 52.983  1.00 105.65 ? 690  ARG   A NH1 1 
ATOM   6538  N  NH2 . ARG   B 2 690  ? 145.551 117.755 55.183  1.00 106.01 ? 690  ARG   A NH2 1 
ATOM   6539  N  N   . GLY   B 2 691  ? 140.377 121.696 54.513  1.00 98.62  ? 691  GLY   A N   1 
ATOM   6540  C  CA  . GLY   B 2 691  ? 139.867 123.016 54.815  1.00 100.38 ? 691  GLY   A CA  1 
ATOM   6541  C  C   . GLY   B 2 691  ? 138.983 123.525 53.694  1.00 100.24 ? 691  GLY   A C   1 
ATOM   6542  O  O   . GLY   B 2 691  ? 138.636 122.796 52.766  1.00 100.71 ? 691  GLY   A O   1 
ATOM   6543  N  N   . ARG   B 2 692  ? 138.630 124.801 53.812  1.00 105.93 ? 692  ARG   A N   1 
ATOM   6544  C  CA  . ARG   B 2 692  ? 137.802 125.510 52.841  1.00 106.72 ? 692  ARG   A CA  1 
ATOM   6545  C  C   . ARG   B 2 692  ? 138.505 126.787 52.394  1.00 109.07 ? 692  ARG   A C   1 
ATOM   6546  O  O   . ARG   B 2 692  ? 137.963 127.892 52.473  1.00 108.81 ? 692  ARG   A O   1 
ATOM   6547  C  CB  . ARG   B 2 692  ? 136.421 125.809 53.417  1.00 105.58 ? 692  ARG   A CB  1 
ATOM   6548  C  CG  . ARG   B 2 692  ? 135.377 126.188 52.374  1.00 102.18 ? 692  ARG   A CG  1 
ATOM   6549  C  CD  . ARG   B 2 692  ? 134.057 126.593 53.009  1.00 102.17 ? 692  ARG   A CD  1 
ATOM   6550  N  NE  . ARG   B 2 692  ? 133.388 125.472 53.658  1.00 104.56 ? 692  ARG   A NE  1 
ATOM   6551  C  CZ  . ARG   B 2 692  ? 133.440 125.216 54.957  1.00 105.81 ? 692  ARG   A CZ  1 
ATOM   6552  N  NH1 . ARG   B 2 692  ? 134.125 125.986 55.786  1.00 104.90 ? 692  ARG   A NH1 1 
ATOM   6553  N  NH2 . ARG   B 2 692  ? 132.788 124.161 55.437  1.00 104.90 ? 692  ARG   A NH2 1 
ATOM   6554  N  N   . ASP   B 2 693  ? 139.756 126.646 51.943  1.00 115.44 ? 693  ASP   A N   1 
ATOM   6555  C  CA  . ASP   B 2 693  ? 140.520 127.803 51.482  1.00 113.89 ? 693  ASP   A CA  1 
ATOM   6556  C  C   . ASP   B 2 693  ? 139.822 128.520 50.332  1.00 113.38 ? 693  ASP   A C   1 
ATOM   6557  O  O   . ASP   B 2 693  ? 140.020 129.725 50.138  1.00 114.45 ? 693  ASP   A O   1 
ATOM   6558  C  CB  . ASP   B 2 693  ? 141.925 127.369 51.062  1.00 113.65 ? 693  ASP   A CB  1 
ATOM   6559  C  CG  . ASP   B 2 693  ? 142.793 128.536 50.634  1.00 114.72 ? 693  ASP   A CG  1 
ATOM   6560  O  OD1 . ASP   B 2 693  ? 143.148 129.363 51.500  1.00 114.67 ? 693  ASP   A OD1 1 
ATOM   6561  O  OD2 . ASP   B 2 693  ? 143.119 128.626 49.431  1.00 114.51 ? 693  ASP   A OD2 1 
ATOM   6562  N  N   . HIS   B 2 694  ? 139.000 127.803 49.568  1.00 109.82 ? 694  HIS   A N   1 
ATOM   6563  C  CA  . HIS   B 2 694  ? 138.197 128.412 48.517  1.00 109.17 ? 694  HIS   A CA  1 
ATOM   6564  C  C   . HIS   B 2 694  ? 136.777 127.866 48.590  1.00 109.05 ? 694  HIS   A C   1 
ATOM   6565  O  O   . HIS   B 2 694  ? 136.392 127.265 49.597  1.00 111.58 ? 694  HIS   A O   1 
ATOM   6566  C  CB  . HIS   B 2 694  ? 138.814 128.147 47.144  1.00 109.52 ? 694  HIS   A CB  1 
ATOM   6567  C  CG  . HIS   B 2 694  ? 138.444 129.163 46.109  1.00 111.22 ? 694  HIS   A CG  1 
ATOM   6568  N  ND1 . HIS   B 2 694  ? 137.726 130.302 46.406  1.00 111.86 ? 694  HIS   A ND1 1 
ATOM   6569  C  CD2 . HIS   B 2 694  ? 138.695 129.212 44.780  1.00 111.37 ? 694  HIS   A CD2 1 
ATOM   6570  C  CE1 . HIS   B 2 694  ? 137.550 131.008 45.303  1.00 110.41 ? 694  HIS   A CE1 1 
ATOM   6571  N  NE2 . HIS   B 2 694  ? 138.128 130.369 44.302  1.00 111.55 ? 694  HIS   A NE2 1 
ATOM   6572  N  N   . ASN   B 2 695  ? 135.991 128.071 47.543  1.00 107.34 ? 695  ASN   A N   1 
ATOM   6573  C  CA  . ASN   B 2 695  ? 134.638 127.522 47.522  1.00 107.85 ? 695  ASN   A CA  1 
ATOM   6574  C  C   . ASN   B 2 695  ? 134.610 126.007 47.255  1.00 111.28 ? 695  ASN   A C   1 
ATOM   6575  O  O   . ASN   B 2 695  ? 133.525 125.420 47.156  1.00 110.07 ? 695  ASN   A O   1 
ATOM   6576  C  CB  . ASN   B 2 695  ? 133.799 128.259 46.478  1.00 106.15 ? 695  ASN   A CB  1 
ATOM   6577  C  CG  . ASN   B 2 695  ? 132.313 128.035 46.659  1.00 106.80 ? 695  ASN   A CG  1 
ATOM   6578  O  OD1 . ASN   B 2 695  ? 131.866 127.596 47.718  1.00 105.77 ? 695  ASN   A OD1 1 
ATOM   6579  N  ND2 . ASN   B 2 695  ? 131.538 128.337 45.625  1.00 108.60 ? 695  ASN   A ND2 1 
ATOM   6580  N  N   . ILE   B 2 696  ? 135.760 125.348 47.140  1.00 110.40 ? 696  ILE   A N   1 
ATOM   6581  C  CA  . ILE   B 2 696  ? 135.837 123.918 46.868  1.00 106.13 ? 696  ILE   A CA  1 
ATOM   6582  C  C   . ILE   B 2 696  ? 136.491 123.241 48.063  1.00 108.51 ? 696  ILE   A C   1 
ATOM   6583  O  O   . ILE   B 2 696  ? 137.599 123.616 48.465  1.00 107.61 ? 696  ILE   A O   1 
ATOM   6584  C  CB  . ILE   B 2 696  ? 136.621 123.624 45.575  1.00 108.27 ? 696  ILE   A CB  1 
ATOM   6585  C  CG1 . ILE   B 2 696  ? 135.776 123.944 44.337  1.00 110.12 ? 696  ILE   A CG1 1 
ATOM   6586  C  CG2 . ILE   B 2 696  ? 137.087 122.178 45.545  1.00 109.31 ? 696  ILE   A CG2 1 
ATOM   6587  C  CD1 . ILE   B 2 696  ? 135.781 125.406 43.934  1.00 108.64 ? 696  ILE   A CD1 1 
ATOM   6588  N  N   . LEU   B 2 697  ? 135.808 122.248 48.626  1.00 112.07 ? 697  LEU   A N   1 
ATOM   6589  C  CA  . LEU   B 2 697  ? 136.307 121.535 49.791  1.00 111.16 ? 697  LEU   A CA  1 
ATOM   6590  C  C   . LEU   B 2 697  ? 137.414 120.562 49.398  1.00 109.83 ? 697  LEU   A C   1 
ATOM   6591  O  O   . LEU   B 2 697  ? 137.558 120.174 48.236  1.00 111.74 ? 697  LEU   A O   1 
ATOM   6592  C  CB  . LEU   B 2 697  ? 135.174 120.779 50.483  1.00 108.95 ? 697  LEU   A CB  1 
ATOM   6593  C  CG  . LEU   B 2 697  ? 133.995 121.623 50.964  1.00 110.37 ? 697  LEU   A CG  1 
ATOM   6594  C  CD1 . LEU   B 2 697  ? 132.918 120.739 51.569  1.00 110.29 ? 697  LEU   A CD1 1 
ATOM   6595  C  CD2 . LEU   B 2 697  ? 134.462 122.664 51.965  1.00 111.39 ? 697  LEU   A CD2 1 
ATOM   6596  N  N   . ARG   B 2 698  ? 138.208 120.171 50.392  1.00 107.73 ? 698  ARG   A N   1 
ATOM   6597  C  CA  . ARG   B 2 698  ? 139.285 119.213 50.192  1.00 108.90 ? 698  ARG   A CA  1 
ATOM   6598  C  C   . ARG   B 2 698  ? 139.283 118.207 51.334  1.00 111.49 ? 698  ARG   A C   1 
ATOM   6599  O  O   . ARG   B 2 698  ? 138.865 118.515 52.453  1.00 113.93 ? 698  ARG   A O   1 
ATOM   6600  C  CB  . ARG   B 2 698  ? 140.653 119.903 50.101  1.00 108.19 ? 698  ARG   A CB  1 
ATOM   6601  C  CG  . ARG   B 2 698  ? 140.807 120.839 48.916  1.00 108.98 ? 698  ARG   A CG  1 
ATOM   6602  C  CD  . ARG   B 2 698  ? 142.185 121.475 48.892  1.00 111.19 ? 698  ARG   A CD  1 
ATOM   6603  N  NE  . ARG   B 2 698  ? 142.342 122.391 47.769  1.00 112.03 ? 698  ARG   A NE  1 
ATOM   6604  C  CZ  . ARG   B 2 698  ? 142.058 123.686 47.813  1.00 113.05 ? 698  ARG   A CZ  1 
ATOM   6605  N  NH1 . ARG   B 2 698  ? 141.599 124.256 48.914  1.00 112.88 ? 698  ARG   A NH1 1 
ATOM   6606  N  NH2 . ARG   B 2 698  ? 142.240 124.427 46.723  1.00 110.52 ? 698  ARG   A NH2 1 
ATOM   6607  N  N   . MET   B 2 699  ? 139.758 116.999 51.039  1.00 110.49 ? 699  MET   A N   1 
ATOM   6608  C  CA  . MET   B 2 699  ? 139.812 115.925 52.020  1.00 106.79 ? 699  MET   A CA  1 
ATOM   6609  C  C   . MET   B 2 699  ? 141.161 115.229 51.922  1.00 107.94 ? 699  MET   A C   1 
ATOM   6610  O  O   . MET   B 2 699  ? 141.813 115.253 50.875  1.00 109.72 ? 699  MET   A O   1 
ATOM   6611  C  CB  . MET   B 2 699  ? 138.678 114.916 51.813  1.00 106.09 ? 699  MET   A CB  1 
ATOM   6612  C  CG  . MET   B 2 699  ? 138.282 114.174 53.073  1.00 107.95 ? 699  MET   A CG  1 
ATOM   6613  S  SD  . MET   B 2 699  ? 137.745 115.310 54.361  1.00 114.52 ? 699  MET   A SD  1 
ATOM   6614  C  CE  . MET   B 2 699  ? 137.443 114.180 55.715  1.00 108.03 ? 699  MET   A CE  1 
ATOM   6615  N  N   . SER   B 2 700  ? 141.578 114.608 53.022  1.00 108.58 ? 700  SER   A N   1 
ATOM   6616  C  CA  . SER   B 2 700  ? 142.880 113.950 53.106  1.00 110.87 ? 700  SER   A CA  1 
ATOM   6617  C  C   . SER   B 2 700  ? 142.687 112.500 53.541  1.00 111.74 ? 700  SER   A C   1 
ATOM   6618  O  O   . SER   B 2 700  ? 142.800 112.172 54.724  1.00 112.05 ? 700  SER   A O   1 
ATOM   6619  C  CB  . SER   B 2 700  ? 143.800 114.695 54.067  1.00 110.99 ? 700  SER   A CB  1 
ATOM   6620  O  OG  . SER   B 2 700  ? 145.072 114.077 54.134  1.00 110.31 ? 700  SER   A OG  1 
ATOM   6621  N  N   . THR   B 2 701  ? 142.404 111.632 52.577  1.00 106.20 ? 701  THR   A N   1 
ATOM   6622  C  CA  . THR   B 2 701  ? 142.394 110.207 52.837  1.00 103.34 ? 701  THR   A CA  1 
ATOM   6623  C  C   . THR   B 2 701  ? 143.836 109.706 52.921  1.00 104.08 ? 701  THR   A C   1 
ATOM   6624  O  O   . THR   B 2 701  ? 144.735 110.268 52.289  1.00 104.92 ? 701  THR   A O   1 
ATOM   6625  C  CB  . THR   B 2 701  ? 141.617 109.488 51.732  1.00 102.45 ? 701  THR   A CB  1 
ATOM   6626  O  OG1 . THR   B 2 701  ? 141.513 108.089 52.015  1.00 102.02 ? 701  THR   A OG1 1 
ATOM   6627  C  CG2 . THR   B 2 701  ? 142.299 109.674 50.384  1.00 103.11 ? 701  THR   A CG2 1 
ATOM   6628  N  N   . PRO   B 2 702  ? 144.098 108.648 53.718  1.00 105.64 ? 702  PRO   A N   1 
ATOM   6629  C  CA  . PRO   B 2 702  ? 145.474 108.160 53.880  1.00 106.68 ? 702  PRO   A CA  1 
ATOM   6630  C  C   . PRO   B 2 702  ? 145.982 107.374 52.672  1.00 106.90 ? 702  PRO   A C   1 
ATOM   6631  O  O   . PRO   B 2 702  ? 146.700 106.380 52.807  1.00 105.72 ? 702  PRO   A O   1 
ATOM   6632  C  CB  . PRO   B 2 702  ? 145.377 107.288 55.136  1.00 106.54 ? 702  PRO   A CB  1 
ATOM   6633  C  CG  . PRO   B 2 702  ? 144.013 106.754 55.078  1.00 106.03 ? 702  PRO   A CG  1 
ATOM   6634  C  CD  . PRO   B 2 702  ? 143.156 107.879 54.554  1.00 105.71 ? 702  PRO   A CD  1 
ATOM   6635  N  N   . PHE   B 2 703  ? 145.639 107.851 51.479  1.00 108.54 ? 703  PHE   A N   1 
ATOM   6636  C  CA  . PHE   B 2 703  ? 146.160 107.290 50.242  1.00 106.81 ? 703  PHE   A CA  1 
ATOM   6637  C  C   . PHE   B 2 703  ? 146.817 108.378 49.399  1.00 105.73 ? 703  PHE   A C   1 
ATOM   6638  O  O   . PHE   B 2 703  ? 147.809 108.113 48.713  1.00 105.43 ? 703  PHE   A O   1 
ATOM   6639  C  CB  . PHE   B 2 703  ? 145.043 106.601 49.457  1.00 104.80 ? 703  PHE   A CB  1 
ATOM   6640  C  CG  . PHE   B 2 703  ? 144.374 105.481 50.207  1.00 106.96 ? 703  PHE   A CG  1 
ATOM   6641  C  CD1 . PHE   B 2 703  ? 144.889 104.199 50.160  1.00 106.94 ? 703  PHE   A CD1 1 
ATOM   6642  C  CD2 . PHE   B 2 703  ? 143.225 105.706 50.948  1.00 106.43 ? 703  PHE   A CD2 1 
ATOM   6643  C  CE1 . PHE   B 2 703  ? 144.283 103.164 50.836  1.00 108.40 ? 703  PHE   A CE1 1 
ATOM   6644  C  CE2 . PHE   B 2 703  ? 142.606 104.668 51.633  1.00 105.74 ? 703  PHE   A CE2 1 
ATOM   6645  C  CZ  . PHE   B 2 703  ? 143.139 103.394 51.575  1.00 109.16 ? 703  PHE   A CZ  1 
ATOM   6646  N  N   . SER   B 2 704  ? 146.273 109.586 49.429  1.00 112.58 ? 704  SER   A N   1 
ATOM   6647  C  CA  . SER   B 2 704  ? 146.775 110.713 48.640  1.00 112.78 ? 704  SER   A CA  1 
ATOM   6648  C  C   . SER   B 2 704  ? 146.039 111.961 49.111  1.00 114.39 ? 704  SER   A C   1 
ATOM   6649  O  O   . SER   B 2 704  ? 145.335 111.937 50.128  1.00 115.97 ? 704  SER   A O   1 
ATOM   6650  C  CB  . SER   B 2 704  ? 146.594 110.475 47.140  1.00 112.89 ? 704  SER   A CB  1 
ATOM   6651  O  OG  . SER   B 2 704  ? 145.233 110.252 46.817  1.00 112.17 ? 704  SER   A OG  1 
ATOM   6652  N  N   . ASP   B 2 705  ? 146.195 113.053 48.368  1.00 115.64 ? 705  ASP   A N   1 
ATOM   6653  C  CA  . ASP   B 2 705  ? 145.509 114.313 48.657  1.00 116.34 ? 705  ASP   A CA  1 
ATOM   6654  C  C   . ASP   B 2 705  ? 144.375 114.466 47.648  1.00 115.91 ? 705  ASP   A C   1 
ATOM   6655  O  O   . ASP   B 2 705  ? 144.564 114.989 46.550  1.00 117.92 ? 705  ASP   A O   1 
ATOM   6656  C  CB  . ASP   B 2 705  ? 146.475 115.488 48.591  1.00 118.68 ? 705  ASP   A CB  1 
ATOM   6657  C  CG  . ASP   B 2 705  ? 147.644 115.337 49.536  1.00 119.33 ? 705  ASP   A CG  1 
ATOM   6658  O  OD1 . ASP   B 2 705  ? 147.482 114.709 50.602  1.00 119.63 ? 705  ASP   A OD1 1 
ATOM   6659  O  OD2 . ASP   B 2 705  ? 148.730 115.858 49.212  1.00 118.23 ? 705  ASP   A OD2 1 
ATOM   6660  N  N   . VAL   B 2 706  ? 143.186 113.999 48.026  1.00 115.32 ? 706  VAL   A N   1 
ATOM   6661  C  CA  . VAL   B 2 706  ? 142.015 114.063 47.155  1.00 116.14 ? 706  VAL   A CA  1 
ATOM   6662  C  C   . VAL   B 2 706  ? 141.296 115.391 47.347  1.00 112.69 ? 706  VAL   A C   1 
ATOM   6663  O  O   . VAL   B 2 706  ? 141.597 116.146 48.278  1.00 112.38 ? 706  VAL   A O   1 
ATOM   6664  C  CB  . VAL   B 2 706  ? 141.064 112.879 47.410  1.00 116.96 ? 706  VAL   A CB  1 
ATOM   6665  C  CG1 . VAL   B 2 706  ? 141.778 111.565 47.135  1.00 115.46 ? 706  VAL   A CG1 1 
ATOM   6666  C  CG2 . VAL   B 2 706  ? 140.528 112.918 48.838  1.00 115.80 ? 706  VAL   A CG2 1 
ATOM   6667  N  N   . SER   B 2 707  ? 140.357 115.694 46.455  1.00 118.05 ? 707  SER   A N   1 
ATOM   6668  C  CA  . SER   B 2 707  ? 139.563 116.909 46.558  1.00 121.42 ? 707  SER   A CA  1 
ATOM   6669  C  C   . SER   B 2 707  ? 138.272 116.716 45.779  1.00 121.21 ? 707  SER   A C   1 
ATOM   6670  O  O   . SER   B 2 707  ? 138.239 116.000 44.775  1.00 123.28 ? 707  SER   A O   1 
ATOM   6671  C  CB  . SER   B 2 707  ? 140.330 118.129 46.035  1.00 122.06 ? 707  SER   A CB  1 
ATOM   6672  O  OG  . SER   B 2 707  ? 140.724 117.948 44.686  1.00 120.74 ? 707  SER   A OG  1 
ATOM   6673  N  N   . ASP   B 2 708  ? 137.211 117.366 46.251  1.00 112.52 ? 708  ASP   A N   1 
ATOM   6674  C  CA  . ASP   B 2 708  ? 135.908 117.279 45.611  1.00 113.17 ? 708  ASP   A CA  1 
ATOM   6675  C  C   . ASP   B 2 708  ? 135.239 118.644 45.639  1.00 115.29 ? 708  ASP   A C   1 
ATOM   6676  O  O   . ASP   B 2 708  ? 135.468 119.446 46.546  1.00 115.46 ? 708  ASP   A O   1 
ATOM   6677  C  CB  . ASP   B 2 708  ? 135.011 116.236 46.292  1.00 115.04 ? 708  ASP   A CB  1 
ATOM   6678  C  CG  . ASP   B 2 708  ? 134.746 116.557 47.749  1.00 115.60 ? 708  ASP   A CG  1 
ATOM   6679  O  OD1 . ASP   B 2 708  ? 135.624 117.167 48.395  1.00 117.38 ? 708  ASP   A OD1 1 
ATOM   6680  O  OD2 . ASP   B 2 708  ? 133.660 116.198 48.247  1.00 114.35 ? 708  ASP   A OD2 1 
ATOM   6681  N  N   . GLU   B 2 709  ? 134.405 118.895 44.634  1.00 119.18 ? 709  GLU   A N   1 
ATOM   6682  C  CA  . GLU   B 2 709  ? 133.727 120.178 44.520  1.00 119.42 ? 709  GLU   A CA  1 
ATOM   6683  C  C   . GLU   B 2 709  ? 132.660 120.316 45.600  1.00 116.52 ? 709  GLU   A C   1 
ATOM   6684  O  O   . GLU   B 2 709  ? 132.122 119.327 46.105  1.00 114.66 ? 709  GLU   A O   1 
ATOM   6685  C  CB  . GLU   B 2 709  ? 133.102 120.324 43.131  1.00 118.33 ? 709  GLU   A CB  1 
ATOM   6686  C  CG  . GLU   B 2 709  ? 132.825 121.760 42.701  1.00 117.41 ? 709  GLU   A CG  1 
ATOM   6687  C  CD  . GLU   B 2 709  ? 131.433 122.233 43.076  1.00 118.50 ? 709  GLU   A CD  1 
ATOM   6688  O  OE1 . GLU   B 2 709  ? 130.619 121.401 43.527  1.00 118.30 ? 709  GLU   A OE1 1 
ATOM   6689  O  OE2 . GLU   B 2 709  ? 131.152 123.440 42.916  1.00 117.58 ? 709  GLU   A OE2 1 
ATOM   6690  N  N   . TYR   B 2 710  ? 132.364 121.560 45.962  1.00 111.33 ? 710  TYR   A N   1 
ATOM   6691  C  CA  . TYR   B 2 710  ? 131.349 121.874 46.960  1.00 111.16 ? 710  TYR   A CA  1 
ATOM   6692  C  C   . TYR   B 2 710  ? 130.165 122.544 46.276  1.00 108.54 ? 710  TYR   A C   1 
ATOM   6693  O  O   . TYR   B 2 710  ? 130.311 123.618 45.684  1.00 110.65 ? 710  TYR   A O   1 
ATOM   6694  C  CB  . TYR   B 2 710  ? 131.917 122.774 48.056  1.00 112.48 ? 710  TYR   A CB  1 
ATOM   6695  C  CG  . TYR   B 2 710  ? 130.862 123.450 48.900  1.00 113.39 ? 710  TYR   A CG  1 
ATOM   6696  C  CD1 . TYR   B 2 710  ? 130.125 122.734 49.833  1.00 109.94 ? 710  TYR   A CD1 1 
ATOM   6697  C  CD2 . TYR   B 2 710  ? 130.606 124.808 48.766  1.00 113.43 ? 710  TYR   A CD2 1 
ATOM   6698  C  CE1 . TYR   B 2 710  ? 129.162 123.349 50.606  1.00 108.34 ? 710  TYR   A CE1 1 
ATOM   6699  C  CE2 . TYR   B 2 710  ? 129.645 125.431 49.535  1.00 111.85 ? 710  TYR   A CE2 1 
ATOM   6700  C  CZ  . TYR   B 2 710  ? 128.926 124.698 50.453  1.00 110.42 ? 710  TYR   A CZ  1 
ATOM   6701  O  OH  . TYR   B 2 710  ? 127.969 125.319 51.220  1.00 110.74 ? 710  TYR   A OH  1 
ATOM   6702  N  N   . GLU   B 2 711  ? 129.002 121.913 46.364  1.00 99.96  ? 711  GLU   A N   1 
ATOM   6703  C  CA  . GLU   B 2 711  ? 127.779 122.430 45.780  1.00 101.30 ? 711  GLU   A CA  1 
ATOM   6704  C  C   . GLU   B 2 711  ? 127.007 123.212 46.838  1.00 100.33 ? 711  GLU   A C   1 
ATOM   6705  O  O   . GLU   B 2 711  ? 127.517 123.498 47.925  1.00 99.80  ? 711  GLU   A O   1 
ATOM   6706  C  CB  . GLU   B 2 711  ? 126.953 121.289 45.188  1.00 105.34 ? 711  GLU   A CB  1 
ATOM   6707  C  CG  . GLU   B 2 711  ? 126.683 121.427 43.698  1.00 105.03 ? 711  GLU   A CG  1 
ATOM   6708  C  CD  . GLU   B 2 711  ? 125.803 122.618 43.370  1.00 106.54 ? 711  GLU   A CD  1 
ATOM   6709  O  OE1 . GLU   B 2 711  ? 125.033 123.055 44.251  1.00 107.11 ? 711  GLU   A OE1 1 
ATOM   6710  O  OE2 . GLU   B 2 711  ? 125.882 123.118 42.228  1.00 106.07 ? 711  GLU   A OE2 1 
ATOM   6711  N  N   . LEU   B 2 712  ? 125.765 123.570 46.521  1.00 95.46  ? 712  LEU   A N   1 
ATOM   6712  C  CA  . LEU   B 2 712  ? 124.984 124.410 47.418  1.00 96.25  ? 712  LEU   A CA  1 
ATOM   6713  C  C   . LEU   B 2 712  ? 124.677 123.674 48.716  1.00 95.52  ? 712  LEU   A C   1 
ATOM   6714  O  O   . LEU   B 2 712  ? 124.325 122.492 48.711  1.00 91.77  ? 712  LEU   A O   1 
ATOM   6715  C  CB  . LEU   B 2 712  ? 123.690 124.858 46.735  1.00 94.42  ? 712  LEU   A CB  1 
ATOM   6716  C  CG  . LEU   B 2 712  ? 122.621 123.827 46.371  1.00 94.24  ? 712  LEU   A CG  1 
ATOM   6717  C  CD1 . LEU   B 2 712  ? 121.555 123.748 47.450  1.00 97.29  ? 712  LEU   A CD1 1 
ATOM   6718  C  CD2 . LEU   B 2 712  ? 121.997 124.162 45.028  1.00 98.16  ? 712  LEU   A CD2 1 
ATOM   6719  N  N   . LEU   B 2 713  ? 124.826 124.382 49.832  1.00 104.83 ? 713  LEU   A N   1 
ATOM   6720  C  CA  . LEU   B 2 713  ? 124.510 123.817 51.133  1.00 100.66 ? 713  LEU   A CA  1 
ATOM   6721  C  C   . LEU   B 2 713  ? 123.007 123.614 51.266  1.00 98.09  ? 713  LEU   A C   1 
ATOM   6722  O  O   . LEU   B 2 713  ? 122.204 124.319 50.648  1.00 103.59 ? 713  LEU   A O   1 
ATOM   6723  C  CB  . LEU   B 2 713  ? 125.022 124.732 52.246  1.00 102.81 ? 713  LEU   A CB  1 
ATOM   6724  C  CG  . LEU   B 2 713  ? 124.920 124.258 53.695  1.00 102.12 ? 713  LEU   A CG  1 
ATOM   6725  C  CD1 . LEU   B 2 713  ? 125.532 122.883 53.844  1.00 101.48 ? 713  LEU   A CD1 1 
ATOM   6726  C  CD2 . LEU   B 2 713  ? 125.612 125.250 54.614  1.00 103.45 ? 713  LEU   A CD2 1 
ATOM   6727  N  N   . HIS   B 2 714  ? 122.628 122.628 52.069  1.00 90.95  ? 714  HIS   A N   1 
ATOM   6728  C  CA  . HIS   B 2 714  ? 121.224 122.307 52.295  1.00 94.40  ? 714  HIS   A CA  1 
ATOM   6729  C  C   . HIS   B 2 714  ? 120.994 122.042 53.778  1.00 91.61  ? 714  HIS   A C   1 
ATOM   6730  O  O   . HIS   B 2 714  ? 120.262 121.132 54.170  1.00 95.57  ? 714  HIS   A O   1 
ATOM   6731  C  CB  . HIS   B 2 714  ? 120.809 121.118 51.430  1.00 98.24  ? 714  HIS   A CB  1 
ATOM   6732  C  CG  . HIS   B 2 714  ? 119.340 120.835 51.452  1.00 99.47  ? 714  HIS   A CG  1 
ATOM   6733  N  ND1 . HIS   B 2 714  ? 118.801 119.765 52.133  1.00 101.10 ? 714  HIS   A ND1 1 
ATOM   6734  C  CD2 . HIS   B 2 714  ? 118.297 121.484 50.883  1.00 98.80  ? 714  HIS   A CD2 1 
ATOM   6735  C  CE1 . HIS   B 2 714  ? 117.489 119.765 51.979  1.00 99.85  ? 714  HIS   A CE1 1 
ATOM   6736  N  NE2 . HIS   B 2 714  ? 117.158 120.798 51.225  1.00 100.23 ? 714  HIS   A NE2 1 
ATOM   6737  N  N   . VAL   B 2 715  ? 121.624 122.845 54.626  1.00 106.13 ? 715  VAL   A N   1 
ATOM   6738  C  CA  . VAL   B 2 715  ? 121.595 122.593 56.061  1.00 112.78 ? 715  VAL   A CA  1 
ATOM   6739  C  C   . VAL   B 2 715  ? 120.209 122.918 56.601  1.00 111.49 ? 715  VAL   A C   1 
ATOM   6740  O  O   . VAL   B 2 715  ? 119.664 124.001 56.355  1.00 112.98 ? 715  VAL   A O   1 
ATOM   6741  C  CB  . VAL   B 2 715  ? 122.691 123.396 56.782  1.00 113.20 ? 715  VAL   A CB  1 
ATOM   6742  C  CG1 . VAL   B 2 715  ? 122.552 124.889 56.516  1.00 112.51 ? 715  VAL   A CG1 1 
ATOM   6743  C  CG2 . VAL   B 2 715  ? 122.664 123.111 58.275  1.00 110.19 ? 715  VAL   A CG2 1 
ATOM   6744  N  N   . LEU   B 2 716  ? 119.616 121.958 57.311  1.00 113.42 ? 716  LEU   A N   1 
ATOM   6745  C  CA  . LEU   B 2 716  ? 118.350 122.194 57.990  1.00 117.88 ? 716  LEU   A CA  1 
ATOM   6746  C  C   . LEU   B 2 716  ? 118.539 122.817 59.364  1.00 117.61 ? 716  LEU   A C   1 
ATOM   6747  O  O   . LEU   B 2 716  ? 117.554 123.259 59.966  1.00 116.62 ? 716  LEU   A O   1 
ATOM   6748  C  CB  . LEU   B 2 716  ? 117.558 120.888 58.119  1.00 119.83 ? 716  LEU   A CB  1 
ATOM   6749  C  CG  . LEU   B 2 716  ? 116.792 120.382 56.891  1.00 116.68 ? 716  LEU   A CG  1 
ATOM   6750  C  CD1 . LEU   B 2 716  ? 115.923 121.485 56.306  1.00 117.39 ? 716  LEU   A CD1 1 
ATOM   6751  C  CD2 . LEU   B 2 716  ? 117.723 119.808 55.833  1.00 114.69 ? 716  LEU   A CD2 1 
ATOM   6752  N  N   . GLU   B 2 717  ? 119.772 122.851 59.869  1.00 121.75 ? 717  GLU   A N   1 
ATOM   6753  C  CA  . GLU   B 2 717  ? 120.127 123.530 61.111  1.00 124.68 ? 717  GLU   A CA  1 
ATOM   6754  C  C   . GLU   B 2 717  ? 119.389 122.968 62.319  1.00 123.59 ? 717  GLU   A C   1 
ATOM   6755  O  O   . GLU   B 2 717  ? 119.266 123.653 63.340  1.00 125.51 ? 717  GLU   A O   1 
ATOM   6756  C  CB  . GLU   B 2 717  ? 119.880 125.040 61.001  1.00 124.64 ? 717  GLU   A CB  1 
ATOM   6757  C  CG  . GLU   B 2 717  ? 120.571 125.692 59.818  1.00 124.20 ? 717  GLU   A CG  1 
ATOM   6758  C  CD  . GLU   B 2 717  ? 119.910 126.990 59.400  1.00 123.85 ? 717  GLU   A CD  1 
ATOM   6759  O  OE1 . GLU   B 2 717  ? 118.810 127.289 59.911  1.00 123.81 ? 717  GLU   A OE1 1 
ATOM   6760  O  OE2 . GLU   B 2 717  ? 120.488 127.707 58.558  1.00 123.78 ? 717  GLU   A OE2 1 
ATOM   6761  N  N   . PHE   B 2 718  ? 118.891 121.733 62.220  1.00 114.88 ? 718  PHE   A N   1 
ATOM   6762  C  CA  . PHE   B 2 718  ? 118.140 121.095 63.302  1.00 118.61 ? 718  PHE   A CA  1 
ATOM   6763  C  C   . PHE   B 2 718  ? 116.933 121.938 63.712  1.00 119.50 ? 718  PHE   A C   1 
ATOM   6764  O  O   . PHE   B 2 718  ? 116.545 121.973 64.881  1.00 119.05 ? 718  PHE   A O   1 
ATOM   6765  C  CB  . PHE   B 2 718  ? 119.051 120.810 64.504  1.00 119.38 ? 718  PHE   A CB  1 
ATOM   6766  C  CG  . PHE   B 2 718  ? 118.464 119.863 65.512  1.00 120.87 ? 718  PHE   A CG  1 
ATOM   6767  C  CD1 . PHE   B 2 718  ? 118.216 118.544 65.179  1.00 119.01 ? 718  PHE   A CD1 1 
ATOM   6768  C  CD2 . PHE   B 2 718  ? 118.181 120.288 66.801  1.00 121.25 ? 718  PHE   A CD2 1 
ATOM   6769  C  CE1 . PHE   B 2 718  ? 117.682 117.671 66.106  1.00 119.33 ? 718  PHE   A CE1 1 
ATOM   6770  C  CE2 . PHE   B 2 718  ? 117.646 119.419 67.732  1.00 119.32 ? 718  PHE   A CE2 1 
ATOM   6771  C  CZ  . PHE   B 2 718  ? 117.397 118.109 67.384  1.00 118.21 ? 718  PHE   A CZ  1 
ATOM   6772  N  N   . ASN   B 2 719  ? 116.326 122.623 62.746  1.00 121.72 ? 719  ASN   A N   1 
ATOM   6773  C  CA  . ASN   B 2 719  ? 115.260 123.576 63.005  1.00 122.65 ? 719  ASN   A CA  1 
ATOM   6774  C  C   . ASN   B 2 719  ? 113.996 123.164 62.261  1.00 123.38 ? 719  ASN   A C   1 
ATOM   6775  O  O   . ASN   B 2 719  ? 114.043 122.406 61.289  1.00 122.72 ? 719  ASN   A O   1 
ATOM   6776  C  CB  . ASN   B 2 719  ? 115.680 124.995 62.591  1.00 124.44 ? 719  ASN   A CB  1 
ATOM   6777  C  CG  . ASN   B 2 719  ? 114.732 126.061 63.107  1.00 124.81 ? 719  ASN   A CG  1 
ATOM   6778  O  OD1 . ASN   B 2 719  ? 114.831 126.493 64.255  1.00 123.25 ? 719  ASN   A OD1 1 
ATOM   6779  N  ND2 . ASN   B 2 719  ? 113.810 126.495 62.255  1.00 124.92 ? 719  ASN   A ND2 1 
ATOM   6780  N  N   . SER   B 2 720  ? 112.860 123.682 62.737  1.00 126.77 ? 720  SER   A N   1 
ATOM   6781  C  CA  . SER   B 2 720  ? 111.546 123.398 62.156  1.00 126.27 ? 720  SER   A CA  1 
ATOM   6782  C  C   . SER   B 2 720  ? 111.260 121.898 62.143  1.00 127.12 ? 720  SER   A C   1 
ATOM   6783  O  O   . SER   B 2 720  ? 110.739 121.356 61.166  1.00 126.55 ? 720  SER   A O   1 
ATOM   6784  C  CB  . SER   B 2 720  ? 111.421 123.989 60.749  1.00 126.05 ? 720  SER   A CB  1 
ATOM   6785  O  OG  . SER   B 2 720  ? 110.152 123.701 60.187  1.00 126.34 ? 720  SER   A OG  1 
ATOM   6786  N  N   . ALA   B 2 721  ? 111.620 121.225 63.237  1.00 126.90 ? 721  ALA   A N   1 
ATOM   6787  C  CA  . ALA   B 2 721  ? 111.435 119.785 63.411  1.00 125.94 ? 721  ALA   A CA  1 
ATOM   6788  C  C   . ALA   B 2 721  ? 112.177 118.970 62.359  1.00 125.74 ? 721  ALA   A C   1 
ATOM   6789  O  O   . ALA   B 2 721  ? 111.871 117.792 62.153  1.00 125.11 ? 721  ALA   A O   1 
ATOM   6790  C  CB  . ALA   B 2 721  ? 109.948 119.408 63.420  1.00 124.14 ? 721  ALA   A CB  1 
ATOM   6791  N  N   . ARG   B 2 722  ? 113.151 119.577 61.682  1.00 121.14 ? 722  ARG   A N   1 
ATOM   6792  C  CA  . ARG   B 2 722  ? 113.964 118.878 60.689  1.00 119.54 ? 722  ARG   A CA  1 
ATOM   6793  C  C   . ARG   B 2 722  ? 115.231 118.401 61.382  1.00 120.73 ? 722  ARG   A C   1 
ATOM   6794  O  O   . ARG   B 2 722  ? 116.271 119.061 61.355  1.00 121.30 ? 722  ARG   A O   1 
ATOM   6795  C  CB  . ARG   B 2 722  ? 114.272 119.781 59.501  1.00 118.01 ? 722  ARG   A CB  1 
ATOM   6796  C  CG  . ARG   B 2 722  ? 113.052 120.185 58.682  1.00 120.70 ? 722  ARG   A CG  1 
ATOM   6797  C  CD  . ARG   B 2 722  ? 112.713 119.156 57.607  1.00 122.07 ? 722  ARG   A CD  1 
ATOM   6798  N  NE  . ARG   B 2 722  ? 112.237 117.894 58.161  1.00 122.42 ? 722  ARG   A NE  1 
ATOM   6799  C  CZ  . ARG   B 2 722  ? 110.963 117.612 58.397  1.00 121.15 ? 722  ARG   A CZ  1 
ATOM   6800  N  NH1 . ARG   B 2 722  ? 110.002 118.484 58.138  1.00 120.13 ? 722  ARG   A NH1 1 
ATOM   6801  N  NH2 . ARG   B 2 722  ? 110.644 116.425 58.905  1.00 119.47 ? 722  ARG   A NH2 1 
ATOM   6802  N  N   . LYS   B 2 723  ? 115.142 117.230 62.014  1.00 110.28 ? 723  LYS   A N   1 
ATOM   6803  C  CA  . LYS   B 2 723  ? 116.265 116.656 62.753  1.00 106.52 ? 723  LYS   A CA  1 
ATOM   6804  C  C   . LYS   B 2 723  ? 117.239 116.014 61.764  1.00 107.20 ? 723  LYS   A C   1 
ATOM   6805  O  O   . LYS   B 2 723  ? 117.468 114.803 61.750  1.00 111.29 ? 723  LYS   A O   1 
ATOM   6806  C  CB  . LYS   B 2 723  ? 115.765 115.647 63.778  1.00 107.88 ? 723  LYS   A CB  1 
ATOM   6807  C  CG  . LYS   B 2 723  ? 114.384 115.948 64.344  1.00 109.60 ? 723  LYS   A CG  1 
ATOM   6808  C  CD  . LYS   B 2 723  ? 114.375 117.216 65.181  1.00 112.47 ? 723  LYS   A CD  1 
ATOM   6809  C  CE  . LYS   B 2 723  ? 113.013 117.446 65.815  1.00 110.88 ? 723  LYS   A CE  1 
ATOM   6810  N  NZ  . LYS   B 2 723  ? 112.612 116.312 66.692  1.00 110.73 ? 723  LYS   A NZ  1 
ATOM   6811  N  N   . ARG   B 2 724  ? 117.821 116.862 60.920  1.00 101.78 ? 724  ARG   A N   1 
ATOM   6812  C  CA  . ARG   B 2 724  ? 118.691 116.388 59.854  1.00 102.09 ? 724  ARG   A CA  1 
ATOM   6813  C  C   . ARG   B 2 724  ? 119.560 117.538 59.366  1.00 100.93 ? 724  ARG   A C   1 
ATOM   6814  O  O   . ARG   B 2 724  ? 119.341 118.701 59.711  1.00 103.40 ? 724  ARG   A O   1 
ATOM   6815  C  CB  . ARG   B 2 724  ? 117.877 115.787 58.704  1.00 105.10 ? 724  ARG   A CB  1 
ATOM   6816  C  CG  . ARG   B 2 724  ? 116.975 116.783 57.992  1.00 107.48 ? 724  ARG   A CG  1 
ATOM   6817  C  CD  . ARG   B 2 724  ? 115.869 116.076 57.225  1.00 108.09 ? 724  ARG   A CD  1 
ATOM   6818  N  NE  . ARG   B 2 724  ? 116.381 114.987 56.402  1.00 108.26 ? 724  ARG   A NE  1 
ATOM   6819  C  CZ  . ARG   B 2 724  ? 115.627 114.206 55.641  1.00 106.31 ? 724  ARG   A CZ  1 
ATOM   6820  N  NH1 . ARG   B 2 724  ? 114.317 114.372 55.565  1.00 104.39 ? 724  ARG   A NH1 1 
ATOM   6821  N  NH2 . ARG   B 2 724  ? 116.202 113.232 54.941  1.00 106.85 ? 724  ARG   A NH2 1 
ATOM   6822  N  N   . MET   B 2 725  ? 120.558 117.188 58.559  1.00 88.57  ? 725  MET   A N   1 
ATOM   6823  C  CA  . MET   B 2 725  ? 121.440 118.169 57.931  1.00 85.41  ? 725  MET   A CA  1 
ATOM   6824  C  C   . MET   B 2 725  ? 122.074 117.515 56.716  1.00 87.63  ? 725  MET   A C   1 
ATOM   6825  O  O   . MET   B 2 725  ? 122.684 116.448 56.839  1.00 92.63  ? 725  MET   A O   1 
ATOM   6826  C  CB  . MET   B 2 725  ? 122.510 118.654 58.904  1.00 88.91  ? 725  MET   A CB  1 
ATOM   6827  C  CG  . MET   B 2 725  ? 123.596 119.489 58.250  1.00 90.93  ? 725  MET   A CG  1 
ATOM   6828  S  SD  . MET   B 2 725  ? 124.817 120.098 59.425  1.00 89.93  ? 725  MET   A SD  1 
ATOM   6829  C  CE  . MET   B 2 725  ? 125.955 120.925 58.320  1.00 87.02  ? 725  MET   A CE  1 
ATOM   6830  N  N   . SER   B 2 726  ? 121.938 118.144 55.552  1.00 81.28  ? 726  SER   A N   1 
ATOM   6831  C  CA  . SER   B 2 726  ? 122.402 117.574 54.297  1.00 79.17  ? 726  SER   A CA  1 
ATOM   6832  C  C   . SER   B 2 726  ? 123.276 118.571 53.551  1.00 80.17  ? 726  SER   A C   1 
ATOM   6833  O  O   . SER   B 2 726  ? 123.092 119.786 53.658  1.00 92.13  ? 726  SER   A O   1 
ATOM   6834  C  CB  . SER   B 2 726  ? 121.221 117.155 53.416  1.00 85.40  ? 726  SER   A CB  1 
ATOM   6835  O  OG  . SER   B 2 726  ? 120.370 118.256 53.149  1.00 85.62  ? 726  SER   A OG  1 
ATOM   6836  N  N   . VAL   B 2 727  ? 124.238 118.046 52.794  1.00 74.74  ? 727  VAL   A N   1 
ATOM   6837  C  CA  . VAL   B 2 727  ? 125.170 118.853 52.013  1.00 84.32  ? 727  VAL   A CA  1 
ATOM   6838  C  C   . VAL   B 2 727  ? 125.266 118.250 50.618  1.00 90.01  ? 727  VAL   A C   1 
ATOM   6839  O  O   . VAL   B 2 727  ? 125.855 117.176 50.442  1.00 95.79  ? 727  VAL   A O   1 
ATOM   6840  C  CB  . VAL   B 2 727  ? 126.559 118.931 52.661  1.00 87.08  ? 727  VAL   A CB  1 
ATOM   6841  C  CG1 . VAL   B 2 727  ? 127.469 119.838 51.850  1.00 87.16  ? 727  VAL   A CG1 1 
ATOM   6842  C  CG2 . VAL   B 2 727  ? 126.463 119.416 54.097  1.00 88.33  ? 727  VAL   A CG2 1 
ATOM   6843  N  N   . ILE   B 2 728  ? 124.697 118.936 49.626  1.00 86.31  ? 728  ILE   A N   1 
ATOM   6844  C  CA  . ILE   B 2 728  ? 124.878 118.538 48.235  1.00 86.01  ? 728  ILE   A CA  1 
ATOM   6845  C  C   . ILE   B 2 728  ? 126.305 118.854 47.812  1.00 86.68  ? 728  ILE   A C   1 
ATOM   6846  O  O   . ILE   B 2 728  ? 126.825 119.940 48.096  1.00 95.06  ? 728  ILE   A O   1 
ATOM   6847  C  CB  . ILE   B 2 728  ? 123.858 119.250 47.335  1.00 89.88  ? 728  ILE   A CB  1 
ATOM   6848  C  CG1 . ILE   B 2 728  ? 122.438 118.761 47.631  1.00 91.14  ? 728  ILE   A CG1 1 
ATOM   6849  C  CG2 . ILE   B 2 728  ? 124.194 119.039 45.865  1.00 88.84  ? 728  ILE   A CG2 1 
ATOM   6850  C  CD1 . ILE   B 2 728  ? 122.096 117.437 46.977  1.00 91.29  ? 728  ILE   A CD1 1 
ATOM   6851  N  N   . LEU   B 2 729  ? 126.953 117.904 47.140  1.00 91.50  ? 729  LEU   A N   1 
ATOM   6852  C  CA  . LEU   B 2 729  ? 128.349 118.055 46.758  1.00 94.12  ? 729  LEU   A CA  1 
ATOM   6853  C  C   . LEU   B 2 729  ? 128.548 117.576 45.326  1.00 96.44  ? 729  LEU   A C   1 
ATOM   6854  O  O   . LEU   B 2 729  ? 127.605 117.166 44.643  1.00 96.58  ? 729  LEU   A O   1 
ATOM   6855  C  CB  . LEU   B 2 729  ? 129.269 117.295 47.721  1.00 98.30  ? 729  LEU   A CB  1 
ATOM   6856  C  CG  . LEU   B 2 729  ? 129.352 117.833 49.149  1.00 100.19 ? 729  LEU   A CG  1 
ATOM   6857  C  CD1 . LEU   B 2 729  ? 130.216 116.927 50.011  1.00 99.87  ? 729  LEU   A CD1 1 
ATOM   6858  C  CD2 . LEU   B 2 729  ? 129.900 119.247 49.147  1.00 98.73  ? 729  LEU   A CD2 1 
ATOM   6859  N  N   . ARG   B 2 730  ? 129.799 117.638 44.875  1.00 114.10 ? 730  ARG   A N   1 
ATOM   6860  C  CA  . ARG   B 2 730  ? 130.187 117.217 43.537  1.00 113.61 ? 730  ARG   A CA  1 
ATOM   6861  C  C   . ARG   B 2 730  ? 131.627 116.726 43.596  1.00 115.45 ? 730  ARG   A C   1 
ATOM   6862  O  O   . ARG   B 2 730  ? 132.391 117.097 44.490  1.00 116.70 ? 730  ARG   A O   1 
ATOM   6863  C  CB  . ARG   B 2 730  ? 130.043 118.364 42.525  1.00 115.56 ? 730  ARG   A CB  1 
ATOM   6864  C  CG  . ARG   B 2 730  ? 130.283 117.976 41.072  1.00 117.48 ? 730  ARG   A CG  1 
ATOM   6865  C  CD  . ARG   B 2 730  ? 130.992 119.087 40.312  1.00 117.38 ? 730  ARG   A CD  1 
ATOM   6866  N  NE  . ARG   B 2 730  ? 130.263 120.348 40.368  1.00 118.25 ? 730  ARG   A NE  1 
ATOM   6867  C  CZ  . ARG   B 2 730  ? 129.386 120.748 39.457  1.00 117.43 ? 730  ARG   A CZ  1 
ATOM   6868  N  NH1 . ARG   B 2 730  ? 129.100 120.005 38.400  1.00 115.63 ? 730  ARG   A NH1 1 
ATOM   6869  N  NH2 . ARG   B 2 730  ? 128.783 121.923 39.609  1.00 116.96 ? 730  ARG   A NH2 1 
ATOM   6870  N  N   . LYS   B 2 731  ? 131.994 115.884 42.635  1.00 127.97 ? 731  LYS   A N   1 
ATOM   6871  C  CA  . LYS   B 2 731  ? 133.341 115.338 42.555  1.00 131.02 ? 731  LYS   A CA  1 
ATOM   6872  C  C   . LYS   B 2 731  ? 134.122 116.055 41.461  1.00 131.59 ? 731  LYS   A C   1 
ATOM   6873  O  O   . LYS   B 2 731  ? 133.627 116.214 40.341  1.00 132.10 ? 731  LYS   A O   1 
ATOM   6874  C  CB  . LYS   B 2 731  ? 133.308 113.834 42.282  1.00 131.88 ? 731  LYS   A CB  1 
ATOM   6875  C  CG  . LYS   B 2 731  ? 134.638 113.139 42.517  1.00 131.67 ? 731  LYS   A CG  1 
ATOM   6876  C  CD  . LYS   B 2 731  ? 135.032 113.200 43.984  1.00 130.01 ? 731  LYS   A CD  1 
ATOM   6877  C  CE  . LYS   B 2 731  ? 136.417 112.617 44.216  1.00 130.38 ? 731  LYS   A CE  1 
ATOM   6878  N  NZ  . LYS   B 2 731  ? 137.477 113.432 43.562  1.00 130.53 ? 731  LYS   A NZ  1 
ATOM   6879  N  N   . LEU   B 2 732  ? 135.341 116.487 41.792  1.00 134.05 ? 732  LEU   A N   1 
ATOM   6880  C  CA  . LEU   B 2 732  ? 136.191 117.181 40.832  1.00 134.75 ? 732  LEU   A CA  1 
ATOM   6881  C  C   . LEU   B 2 732  ? 136.742 116.264 39.748  1.00 135.61 ? 732  LEU   A C   1 
ATOM   6882  O  O   . LEU   B 2 732  ? 137.246 116.767 38.738  1.00 135.90 ? 732  LEU   A O   1 
ATOM   6883  C  CB  . LEU   B 2 732  ? 137.351 117.867 41.557  1.00 134.30 ? 732  LEU   A CB  1 
ATOM   6884  C  CG  . LEU   B 2 732  ? 137.007 119.089 42.408  1.00 134.61 ? 732  LEU   A CG  1 
ATOM   6885  C  CD1 . LEU   B 2 732  ? 138.243 119.599 43.129  1.00 133.31 ? 732  LEU   A CD1 1 
ATOM   6886  C  CD2 . LEU   B 2 732  ? 136.400 120.183 41.544  1.00 133.69 ? 732  LEU   A CD2 1 
ATOM   6887  N  N   . ASP   B 2 733  ? 136.664 114.948 39.927  1.00 145.19 ? 733  ASP   A N   1 
ATOM   6888  C  CA  . ASP   B 2 733  ? 137.202 114.021 38.944  1.00 146.64 ? 733  ASP   A CA  1 
ATOM   6889  C  C   . ASP   B 2 733  ? 136.317 113.997 37.698  1.00 147.25 ? 733  ASP   A C   1 
ATOM   6890  O  O   . ASP   B 2 733  ? 135.258 114.628 37.634  1.00 146.06 ? 733  ASP   A O   1 
ATOM   6891  C  CB  . ASP   B 2 733  ? 137.334 112.624 39.548  1.00 146.05 ? 733  ASP   A CB  1 
ATOM   6892  C  CG  . ASP   B 2 733  ? 138.358 112.567 40.663  1.00 145.66 ? 733  ASP   A CG  1 
ATOM   6893  O  OD1 . ASP   B 2 733  ? 138.966 113.614 40.969  1.00 145.68 ? 733  ASP   A OD1 1 
ATOM   6894  O  OD2 . ASP   B 2 733  ? 138.556 111.474 41.235  1.00 145.64 ? 733  ASP   A OD2 1 
ATOM   6895  N  N   . GLU   B 2 734  ? 136.769 113.251 36.687  1.00 155.89 ? 734  GLU   A N   1 
ATOM   6896  C  CA  . GLU   B 2 734  ? 136.030 113.157 35.433  1.00 154.97 ? 734  GLU   A CA  1 
ATOM   6897  C  C   . GLU   B 2 734  ? 134.682 112.469 35.599  1.00 155.30 ? 734  GLU   A C   1 
ATOM   6898  O  O   . GLU   B 2 734  ? 133.815 112.619 34.731  1.00 154.36 ? 734  GLU   A O   1 
ATOM   6899  C  CB  . GLU   B 2 734  ? 136.862 112.419 34.380  1.00 154.54 ? 734  GLU   A CB  1 
ATOM   6900  C  CG  . GLU   B 2 734  ? 137.120 110.948 34.688  1.00 154.51 ? 734  GLU   A CG  1 
ATOM   6901  C  CD  . GLU   B 2 734  ? 138.222 110.742 35.711  1.00 155.32 ? 734  GLU   A CD  1 
ATOM   6902  O  OE1 . GLU   B 2 734  ? 138.910 111.726 36.055  1.00 155.43 ? 734  GLU   A OE1 1 
ATOM   6903  O  OE2 . GLU   B 2 734  ? 138.400 109.594 36.171  1.00 154.90 ? 734  GLU   A OE2 1 
ATOM   6904  N  N   . ASP   B 2 735  ? 134.489 111.712 36.683  1.00 154.66 ? 735  ASP   A N   1 
ATOM   6905  C  CA  . ASP   B 2 735  ? 133.203 111.061 36.908  1.00 153.44 ? 735  ASP   A CA  1 
ATOM   6906  C  C   . ASP   B 2 735  ? 132.089 112.084 37.088  1.00 152.15 ? 735  ASP   A C   1 
ATOM   6907  O  O   . ASP   B 2 735  ? 131.006 111.942 36.509  1.00 151.46 ? 735  ASP   A O   1 
ATOM   6908  C  CB  . ASP   B 2 735  ? 133.288 110.139 38.125  1.00 152.89 ? 735  ASP   A CB  1 
ATOM   6909  C  CG  . ASP   B 2 735  ? 134.346 109.065 37.969  1.00 152.93 ? 735  ASP   A CG  1 
ATOM   6910  O  OD1 . ASP   B 2 735  ? 135.011 109.033 36.912  1.00 153.62 ? 735  ASP   A OD1 1 
ATOM   6911  O  OD2 . ASP   B 2 735  ? 134.512 108.252 38.903  1.00 151.95 ? 735  ASP   A OD2 1 
ATOM   6912  N  N   . GLY   B 2 736  ? 132.340 113.125 37.877  1.00 136.56 ? 736  GLY   A N   1 
ATOM   6913  C  CA  . GLY   B 2 736  ? 131.347 114.169 38.079  1.00 134.74 ? 736  GLY   A CA  1 
ATOM   6914  C  C   . GLY   B 2 736  ? 130.058 113.678 38.701  1.00 134.67 ? 736  GLY   A C   1 
ATOM   6915  O  O   . GLY   B 2 736  ? 128.971 114.104 38.292  1.00 133.80 ? 736  GLY   A O   1 
ATOM   6916  N  N   . ARG   B 2 737  ? 130.154 112.789 39.684  1.00 129.32 ? 737  ARG   A N   1 
ATOM   6917  C  CA  . ARG   B 2 737  ? 128.969 112.228 40.316  1.00 129.84 ? 737  ARG   A CA  1 
ATOM   6918  C  C   . ARG   B 2 737  ? 128.450 113.165 41.399  1.00 129.46 ? 737  ARG   A C   1 
ATOM   6919  O  O   . ARG   B 2 737  ? 129.202 113.588 42.283  1.00 127.38 ? 737  ARG   A O   1 
ATOM   6920  C  CB  . ARG   B 2 737  ? 129.284 110.852 40.903  1.00 129.64 ? 737  ARG   A CB  1 
ATOM   6921  C  CG  . ARG   B 2 737  ? 130.606 110.783 41.650  1.00 130.04 ? 737  ARG   A CG  1 
ATOM   6922  C  CD  . ARG   B 2 737  ? 130.882 109.378 42.159  1.00 130.18 ? 737  ARG   A CD  1 
ATOM   6923  N  NE  . ARG   B 2 737  ? 132.197 109.271 42.780  1.00 130.08 ? 737  ARG   A NE  1 
ATOM   6924  C  CZ  . ARG   B 2 737  ? 132.440 109.495 44.064  1.00 130.43 ? 737  ARG   A CZ  1 
ATOM   6925  N  NH1 . ARG   B 2 737  ? 131.475 109.841 44.900  1.00 131.31 ? 737  ARG   A NH1 1 
ATOM   6926  N  NH2 . ARG   B 2 737  ? 133.682 109.368 44.521  1.00 129.85 ? 737  ARG   A NH2 1 
ATOM   6927  N  N   . ILE   B 2 738  ? 127.163 113.492 41.325  1.00 121.72 ? 738  ILE   A N   1 
ATOM   6928  C  CA  . ILE   B 2 738  ? 126.523 114.327 42.335  1.00 119.05 ? 738  ILE   A CA  1 
ATOM   6929  C  C   . ILE   B 2 738  ? 126.025 113.424 43.455  1.00 120.32 ? 738  ILE   A C   1 
ATOM   6930  O  O   . ILE   B 2 738  ? 125.149 112.580 43.242  1.00 120.51 ? 738  ILE   A O   1 
ATOM   6931  C  CB  . ILE   B 2 738  ? 125.371 115.142 41.734  1.00 118.35 ? 738  ILE   A CB  1 
ATOM   6932  C  CG1 . ILE   B 2 738  ? 125.842 115.908 40.496  1.00 119.36 ? 738  ILE   A CG1 1 
ATOM   6933  C  CG2 . ILE   B 2 738  ? 124.806 116.104 42.767  1.00 118.42 ? 738  ILE   A CG2 1 
ATOM   6934  C  CD1 . ILE   B 2 738  ? 126.841 116.998 40.797  1.00 118.14 ? 738  ILE   A CD1 1 
ATOM   6935  N  N   . PHE   B 2 739  ? 126.579 113.600 44.653  1.00 112.17 ? 739  PHE   A N   1 
ATOM   6936  C  CA  . PHE   B 2 739  ? 126.206 112.790 45.803  1.00 108.72 ? 739  PHE   A CA  1 
ATOM   6937  C  C   . PHE   B 2 739  ? 125.744 113.686 46.940  1.00 103.15 ? 739  PHE   A C   1 
ATOM   6938  O  O   . PHE   B 2 739  ? 126.357 114.719 47.220  1.00 104.50 ? 739  PHE   A O   1 
ATOM   6939  C  CB  . PHE   B 2 739  ? 127.369 111.898 46.269  1.00 105.08 ? 739  PHE   A CB  1 
ATOM   6940  C  CG  . PHE   B 2 739  ? 128.677 112.620 46.409  1.00 107.12 ? 739  PHE   A CG  1 
ATOM   6941  C  CD1 . PHE   B 2 739  ? 129.550 112.710 45.339  1.00 108.39 ? 739  PHE   A CD1 1 
ATOM   6942  C  CD2 . PHE   B 2 739  ? 129.043 113.195 47.614  1.00 107.76 ? 739  PHE   A CD2 1 
ATOM   6943  C  CE1 . PHE   B 2 739  ? 130.758 113.370 45.463  1.00 109.94 ? 739  PHE   A CE1 1 
ATOM   6944  C  CE2 . PHE   B 2 739  ? 130.250 113.856 47.746  1.00 109.49 ? 739  PHE   A CE2 1 
ATOM   6945  C  CZ  . PHE   B 2 739  ? 131.108 113.943 46.669  1.00 109.35 ? 739  PHE   A CZ  1 
ATOM   6946  N  N   . LEU   B 2 740  ? 124.655 113.285 47.587  1.00 95.41  ? 740  LEU   A N   1 
ATOM   6947  C  CA  . LEU   B 2 740  ? 124.098 114.004 48.724  1.00 97.35  ? 740  LEU   A CA  1 
ATOM   6948  C  C   . LEU   B 2 740  ? 124.504 113.284 50.003  1.00 102.28 ? 740  LEU   A C   1 
ATOM   6949  O  O   . LEU   B 2 740  ? 124.253 112.083 50.151  1.00 105.36 ? 740  LEU   A O   1 
ATOM   6950  C  CB  . LEU   B 2 740  ? 122.577 114.103 48.611  1.00 99.11  ? 740  LEU   A CB  1 
ATOM   6951  C  CG  . LEU   B 2 740  ? 121.769 114.828 49.695  1.00 98.77  ? 740  LEU   A CG  1 
ATOM   6952  C  CD1 . LEU   B 2 740  ? 121.360 113.886 50.821  1.00 100.04 ? 740  LEU   A CD1 1 
ATOM   6953  C  CD2 . LEU   B 2 740  ? 122.529 116.028 50.245  1.00 96.91  ? 740  LEU   A CD2 1 
ATOM   6954  N  N   . LEU   B 2 741  ? 125.127 114.016 50.921  1.00 86.60  ? 741  LEU   A N   1 
ATOM   6955  C  CA  . LEU   B 2 741  ? 125.532 113.481 52.213  1.00 79.37  ? 741  LEU   A CA  1 
ATOM   6956  C  C   . LEU   B 2 741  ? 124.642 114.092 53.286  1.00 80.94  ? 741  LEU   A C   1 
ATOM   6957  O  O   . LEU   B 2 741  ? 124.590 115.317 53.428  1.00 87.70  ? 741  LEU   A O   1 
ATOM   6958  C  CB  . LEU   B 2 741  ? 127.003 113.784 52.490  1.00 81.07  ? 741  LEU   A CB  1 
ATOM   6959  C  CG  . LEU   B 2 741  ? 127.978 113.517 51.343  1.00 87.60  ? 741  LEU   A CG  1 
ATOM   6960  C  CD1 . LEU   B 2 741  ? 129.413 113.746 51.793  1.00 87.41  ? 741  LEU   A CD1 1 
ATOM   6961  C  CD2 . LEU   B 2 741  ? 127.805 112.113 50.792  1.00 89.26  ? 741  LEU   A CD2 1 
ATOM   6962  N  N   . CYS   B 2 742  ? 123.946 113.242 54.037  1.00 83.11  ? 742  CYS   A N   1 
ATOM   6963  C  CA  . CYS   B 2 742  ? 122.985 113.692 55.031  1.00 83.16  ? 742  CYS   A CA  1 
ATOM   6964  C  C   . CYS   B 2 742  ? 123.236 113.003 56.364  1.00 86.59  ? 742  CYS   A C   1 
ATOM   6965  O  O   . CYS   B 2 742  ? 123.553 111.811 56.410  1.00 90.65  ? 742  CYS   A O   1 
ATOM   6966  C  CB  . CYS   B 2 742  ? 121.549 113.423 54.574  1.00 87.22  ? 742  CYS   A CB  1 
ATOM   6967  S  SG  . CYS   B 2 742  ? 120.283 113.942 55.756  1.00 100.86 ? 742  CYS   A SG  1 
ATOM   6968  N  N   . LYS   B 2 743  ? 123.092 113.766 57.445  1.00 85.78  ? 743  LYS   A N   1 
ATOM   6969  C  CA  . LYS   B 2 743  ? 123.173 113.254 58.804  1.00 83.96  ? 743  LYS   A CA  1 
ATOM   6970  C  C   . LYS   B 2 743  ? 121.996 113.796 59.598  1.00 81.17  ? 743  LYS   A C   1 
ATOM   6971  O  O   . LYS   B 2 743  ? 121.465 114.866 59.291  1.00 85.70  ? 743  LYS   A O   1 
ATOM   6972  C  CB  . LYS   B 2 743  ? 124.486 113.652 59.488  1.00 84.01  ? 743  LYS   A CB  1 
ATOM   6973  C  CG  . LYS   B 2 743  ? 124.618 115.141 59.748  1.00 83.18  ? 743  LYS   A CG  1 
ATOM   6974  C  CD  . LYS   B 2 743  ? 125.835 115.459 60.599  1.00 85.70  ? 743  LYS   A CD  1 
ATOM   6975  C  CE  . LYS   B 2 743  ? 127.123 115.060 59.904  1.00 86.09  ? 743  LYS   A CE  1 
ATOM   6976  N  NZ  . LYS   B 2 743  ? 128.318 115.600 60.613  1.00 86.94  ? 743  LYS   A NZ  1 
ATOM   6977  N  N   . GLY   B 2 744  ? 121.586 113.054 60.617  1.00 74.84  ? 744  GLY   A N   1 
ATOM   6978  C  CA  . GLY   B 2 744  ? 120.457 113.491 61.412  1.00 78.28  ? 744  GLY   A CA  1 
ATOM   6979  C  C   . GLY   B 2 744  ? 120.116 112.488 62.489  1.00 77.41  ? 744  GLY   A C   1 
ATOM   6980  O  O   . GLY   B 2 744  ? 120.938 111.655 62.877  1.00 82.62  ? 744  GLY   A O   1 
ATOM   6981  N  N   . ALA   B 2 745  ? 118.878 112.582 62.964  1.00 89.24  ? 745  ALA   A N   1 
ATOM   6982  C  CA  . ALA   B 2 745  ? 118.412 111.752 64.061  1.00 91.98  ? 745  ALA   A CA  1 
ATOM   6983  C  C   . ALA   B 2 745  ? 118.161 110.323 63.586  1.00 93.54  ? 745  ALA   A C   1 
ATOM   6984  O  O   . ALA   B 2 745  ? 118.424 109.957 62.438  1.00 96.04  ? 745  ALA   A O   1 
ATOM   6985  C  CB  . ALA   B 2 745  ? 117.148 112.346 64.677  1.00 94.99  ? 745  ALA   A CB  1 
ATOM   6986  N  N   . ASP   B 2 746  ? 117.642 109.502 64.498  1.00 106.60 ? 746  ASP   A N   1 
ATOM   6987  C  CA  . ASP   B 2 746  ? 117.387 108.102 64.180  1.00 108.14 ? 746  ASP   A CA  1 
ATOM   6988  C  C   . ASP   B 2 746  ? 116.072 107.939 63.429  1.00 109.49 ? 746  ASP   A C   1 
ATOM   6989  O  O   . ASP   B 2 746  ? 116.033 107.363 62.335  1.00 110.61 ? 746  ASP   A O   1 
ATOM   6990  C  CB  . ASP   B 2 746  ? 117.380 107.270 65.462  1.00 108.97 ? 746  ASP   A CB  1 
ATOM   6991  C  CG  . ASP   B 2 746  ? 116.864 105.864 65.240  1.00 111.90 ? 746  ASP   A CG  1 
ATOM   6992  O  OD1 . ASP   B 2 746  ? 117.505 105.105 64.483  1.00 111.98 ? 746  ASP   A OD1 1 
ATOM   6993  O  OD2 . ASP   B 2 746  ? 115.816 105.515 65.823  1.00 113.71 ? 746  ASP   A OD2 1 
ATOM   6994  N  N   . ASN   B 2 747  ? 114.980 108.441 64.009  1.00 111.13 ? 747  ASN   A N   1 
ATOM   6995  C  CA  . ASN   B 2 747  ? 113.661 108.234 63.422  1.00 111.93 ? 747  ASN   A CA  1 
ATOM   6996  C  C   . ASN   B 2 747  ? 113.560 108.878 62.045  1.00 113.81 ? 747  ASN   A C   1 
ATOM   6997  O  O   . ASN   B 2 747  ? 113.075 108.257 61.091  1.00 114.46 ? 747  ASN   A O   1 
ATOM   6998  C  CB  . ASN   B 2 747  ? 112.585 108.789 64.355  1.00 110.68 ? 747  ASN   A CB  1 
ATOM   6999  C  CG  . ASN   B 2 747  ? 112.616 108.147 65.727  1.00 112.04 ? 747  ASN   A CG  1 
ATOM   7000  O  OD1 . ASN   B 2 747  ? 113.627 107.575 66.135  1.00 112.07 ? 747  ASN   A OD1 1 
ATOM   7001  N  ND2 . ASN   B 2 747  ? 111.504 108.238 66.447  1.00 112.82 ? 747  ASN   A ND2 1 
ATOM   7002  N  N   . VAL   B 2 748  ? 114.026 110.122 61.922  1.00 107.29 ? 748  VAL   A N   1 
ATOM   7003  C  CA  . VAL   B 2 748  ? 113.880 110.854 60.666  1.00 105.38 ? 748  VAL   A CA  1 
ATOM   7004  C  C   . VAL   B 2 748  ? 114.648 110.159 59.551  1.00 105.94 ? 748  VAL   A C   1 
ATOM   7005  O  O   . VAL   B 2 748  ? 114.106 109.886 58.474  1.00 110.54 ? 748  VAL   A O   1 
ATOM   7006  C  CB  . VAL   B 2 748  ? 114.337 112.313 60.841  1.00 108.16 ? 748  VAL   A CB  1 
ATOM   7007  C  CG1 . VAL   B 2 748  ? 114.193 113.074 59.532  1.00 109.33 ? 748  VAL   A CG1 1 
ATOM   7008  C  CG2 . VAL   B 2 748  ? 113.543 112.988 61.948  1.00 108.98 ? 748  VAL   A CG2 1 
ATOM   7009  N  N   . ILE   B 2 749  ? 115.919 109.844 59.801  1.00 101.89 ? 749  ILE   A N   1 
ATOM   7010  C  CA  . ILE   B 2 749  ? 116.736 109.217 58.769  1.00 105.79 ? 749  ILE   A CA  1 
ATOM   7011  C  C   . ILE   B 2 749  ? 116.205 107.829 58.432  1.00 108.93 ? 749  ILE   A C   1 
ATOM   7012  O  O   . ILE   B 2 749  ? 116.115 107.459 57.256  1.00 109.96 ? 749  ILE   A O   1 
ATOM   7013  C  CB  . ILE   B 2 749  ? 118.212 109.178 59.200  1.00 106.10 ? 749  ILE   A CB  1 
ATOM   7014  C  CG1 . ILE   B 2 749  ? 118.761 110.600 59.323  1.00 107.63 ? 749  ILE   A CG1 1 
ATOM   7015  C  CG2 . ILE   B 2 749  ? 119.039 108.387 58.202  1.00 105.53 ? 749  ILE   A CG2 1 
ATOM   7016  C  CD1 . ILE   B 2 749  ? 118.692 111.392 58.036  1.00 107.19 ? 749  ILE   A CD1 1 
ATOM   7017  N  N   . PHE   B 2 750  ? 115.833 107.045 59.448  1.00 113.56 ? 750  PHE   A N   1 
ATOM   7018  C  CA  . PHE   B 2 750  ? 115.350 105.690 59.193  1.00 112.09 ? 750  PHE   A CA  1 
ATOM   7019  C  C   . PHE   B 2 750  ? 114.072 105.703 58.363  1.00 111.55 ? 750  PHE   A C   1 
ATOM   7020  O  O   . PHE   B 2 750  ? 113.935 104.935 57.403  1.00 112.88 ? 750  PHE   A O   1 
ATOM   7021  C  CB  . PHE   B 2 750  ? 115.131 104.949 60.511  1.00 112.05 ? 750  PHE   A CB  1 
ATOM   7022  C  CG  . PHE   B 2 750  ? 116.332 104.182 60.978  1.00 111.48 ? 750  PHE   A CG  1 
ATOM   7023  C  CD1 . PHE   B 2 750  ? 117.523 104.244 60.278  1.00 110.72 ? 750  PHE   A CD1 1 
ATOM   7024  C  CD2 . PHE   B 2 750  ? 116.266 103.385 62.108  1.00 112.22 ? 750  PHE   A CD2 1 
ATOM   7025  C  CE1 . PHE   B 2 750  ? 118.630 103.536 60.702  1.00 112.06 ? 750  PHE   A CE1 1 
ATOM   7026  C  CE2 . PHE   B 2 750  ? 117.369 102.673 62.536  1.00 112.67 ? 750  PHE   A CE2 1 
ATOM   7027  C  CZ  . PHE   B 2 750  ? 118.553 102.749 61.831  1.00 112.95 ? 750  PHE   A CZ  1 
ATOM   7028  N  N   . GLU   B 2 751  ? 113.121 106.574 58.711  1.00 110.80 ? 751  GLU   A N   1 
ATOM   7029  C  CA  . GLU   B 2 751  ? 111.923 106.716 57.893  1.00 113.91 ? 751  GLU   A CA  1 
ATOM   7030  C  C   . GLU   B 2 751  ? 112.240 107.316 56.531  1.00 114.26 ? 751  GLU   A C   1 
ATOM   7031  O  O   . GLU   B 2 751  ? 111.443 107.171 55.598  1.00 113.86 ? 751  GLU   A O   1 
ATOM   7032  C  CB  . GLU   B 2 751  ? 110.889 107.571 58.632  1.00 112.49 ? 751  GLU   A CB  1 
ATOM   7033  C  CG  . GLU   B 2 751  ? 109.480 107.524 58.051  1.00 113.94 ? 751  GLU   A CG  1 
ATOM   7034  C  CD  . GLU   B 2 751  ? 109.231 108.607 57.018  1.00 115.99 ? 751  GLU   A CD  1 
ATOM   7035  O  OE1 . GLU   B 2 751  ? 110.087 109.505 56.876  1.00 114.99 ? 751  GLU   A OE1 1 
ATOM   7036  O  OE2 . GLU   B 2 751  ? 108.178 108.559 56.347  1.00 114.81 ? 751  GLU   A OE2 1 
ATOM   7037  N  N   . ARG   B 2 752  ? 113.394 107.964 56.393  1.00 109.57 ? 752  ARG   A N   1 
ATOM   7038  C  CA  . ARG   B 2 752  ? 113.793 108.640 55.161  1.00 108.19 ? 752  ARG   A CA  1 
ATOM   7039  C  C   . ARG   B 2 752  ? 114.741 107.799 54.316  1.00 109.37 ? 752  ARG   A C   1 
ATOM   7040  O  O   . ARG   B 2 752  ? 115.668 108.332 53.701  1.00 111.25 ? 752  ARG   A O   1 
ATOM   7041  C  CB  . ARG   B 2 752  ? 114.423 109.988 55.493  1.00 109.20 ? 752  ARG   A CB  1 
ATOM   7042  C  CG  . ARG   B 2 752  ? 113.441 111.147 55.519  1.00 109.04 ? 752  ARG   A CG  1 
ATOM   7043  C  CD  . ARG   B 2 752  ? 112.967 111.495 54.117  1.00 108.98 ? 752  ARG   A CD  1 
ATOM   7044  N  NE  . ARG   B 2 752  ? 114.073 111.502 53.169  1.00 110.50 ? 752  ARG   A NE  1 
ATOM   7045  C  CZ  . ARG   B 2 752  ? 114.279 110.570 52.248  1.00 111.45 ? 752  ARG   A CZ  1 
ATOM   7046  N  NH1 . ARG   B 2 752  ? 113.434 109.566 52.080  1.00 112.22 ? 752  ARG   A NH1 1 
ATOM   7047  N  NH2 . ARG   B 2 752  ? 115.362 110.645 51.481  1.00 110.89 ? 752  ARG   A NH2 1 
ATOM   7048  N  N   . LEU   B 2 753  ? 114.544 106.486 54.266  1.00 112.64 ? 753  LEU   A N   1 
ATOM   7049  C  CA  . LEU   B 2 753  ? 115.378 105.604 53.463  1.00 113.43 ? 753  LEU   A CA  1 
ATOM   7050  C  C   . LEU   B 2 753  ? 114.534 104.892 52.412  1.00 116.72 ? 753  LEU   A C   1 
ATOM   7051  O  O   . LEU   B 2 753  ? 113.302 104.956 52.417  1.00 117.58 ? 753  LEU   A O   1 
ATOM   7052  C  CB  . LEU   B 2 753  ? 116.103 104.574 54.338  1.00 114.92 ? 753  LEU   A CB  1 
ATOM   7053  C  CG  . LEU   B 2 753  ? 117.037 105.104 55.426  1.00 117.44 ? 753  LEU   A CG  1 
ATOM   7054  C  CD1 . LEU   B 2 753  ? 117.778 103.966 56.100  1.00 118.03 ? 753  LEU   A CD1 1 
ATOM   7055  C  CD2 . LEU   B 2 753  ? 118.016 106.117 54.862  1.00 115.61 ? 753  LEU   A CD2 1 
ATOM   7056  N  N   . THR   B 2 754  ? 115.221 104.207 51.497  1.00 125.58 ? 754  THR   A N   1 
ATOM   7057  C  CA  . THR   B 2 754  ? 114.582 103.388 50.466  1.00 125.51 ? 754  THR   A CA  1 
ATOM   7058  C  C   . THR   B 2 754  ? 114.803 101.926 50.843  1.00 126.72 ? 754  THR   A C   1 
ATOM   7059  O  O   . THR   B 2 754  ? 115.824 101.323 50.512  1.00 128.86 ? 754  THR   A O   1 
ATOM   7060  C  CB  . THR   B 2 754  ? 115.136 103.710 49.082  1.00 126.10 ? 754  THR   A CB  1 
ATOM   7061  O  OG1 . THR   B 2 754  ? 114.919 102.596 48.206  1.00 126.27 ? 754  THR   A OG1 1 
ATOM   7062  C  CG2 . THR   B 2 754  ? 116.626 104.028 49.149  1.00 124.72 ? 754  THR   A CG2 1 
ATOM   7063  N  N   . LYS   B 2 755  ? 113.825 101.352 51.540  1.00 129.04 ? 755  LYS   A N   1 
ATOM   7064  C  CA  . LYS   B 2 755  ? 113.953 100.021 52.134  1.00 130.73 ? 755  LYS   A CA  1 
ATOM   7065  C  C   . LYS   B 2 755  ? 113.080 99.045  51.352  1.00 129.14 ? 755  LYS   A C   1 
ATOM   7066  O  O   . LYS   B 2 755  ? 111.857 99.030  51.492  1.00 128.30 ? 755  LYS   A O   1 
ATOM   7067  C  CB  . LYS   B 2 755  ? 113.562 100.052 53.608  1.00 130.21 ? 755  LYS   A CB  1 
ATOM   7068  C  CG  . LYS   B 2 755  ? 114.146 101.209 54.404  1.00 129.49 ? 755  LYS   A CG  1 
ATOM   7069  C  CD  . LYS   B 2 755  ? 113.194 102.402 54.486  1.00 129.50 ? 755  LYS   A CD  1 
ATOM   7070  C  CE  . LYS   B 2 755  ? 111.901 102.062 55.216  1.00 128.02 ? 755  LYS   A CE  1 
ATOM   7071  N  NZ  . LYS   B 2 755  ? 110.827 101.585 54.299  1.00 126.99 ? 755  LYS   A NZ  1 
ATOM   7072  N  N   . ASP   B 2 756  ? 113.714 98.219  50.517  1.00 134.74 ? 756  ASP   A N   1 
ATOM   7073  C  CA  . ASP   B 2 756  ? 112.958 97.168  49.848  1.00 136.60 ? 756  ASP   A CA  1 
ATOM   7074  C  C   . ASP   B 2 756  ? 113.050 95.843  50.601  1.00 137.58 ? 756  ASP   A C   1 
ATOM   7075  O  O   . ASP   B 2 756  ? 112.044 95.367  51.136  1.00 137.04 ? 756  ASP   A O   1 
ATOM   7076  C  CB  . ASP   B 2 756  ? 113.449 97.004  48.408  1.00 136.66 ? 756  ASP   A CB  1 
ATOM   7077  C  CG  . ASP   B 2 756  ? 114.957 97.096  48.293  1.00 136.40 ? 756  ASP   A CG  1 
ATOM   7078  O  OD1 . ASP   B 2 756  ? 115.644 96.125  48.672  1.00 136.77 ? 756  ASP   A OD1 1 
ATOM   7079  O  OD2 . ASP   B 2 756  ? 115.456 98.143  47.829  1.00 136.30 ? 756  ASP   A OD2 1 
ATOM   7080  N  N   . SER   B 2 757  ? 114.235 95.230  50.644  1.00 137.96 ? 757  SER   A N   1 
ATOM   7081  C  CA  . SER   B 2 757  ? 114.492 94.145  51.587  1.00 136.72 ? 757  SER   A CA  1 
ATOM   7082  C  C   . SER   B 2 757  ? 115.859 94.291  52.246  1.00 136.02 ? 757  SER   A C   1 
ATOM   7083  O  O   . SER   B 2 757  ? 116.010 94.106  53.461  1.00 134.48 ? 757  SER   A O   1 
ATOM   7084  C  CB  . SER   B 2 757  ? 114.387 92.791  50.881  1.00 135.47 ? 757  SER   A CB  1 
ATOM   7085  O  OG  . SER   B 2 757  ? 115.312 92.700  49.812  1.00 135.53 ? 757  SER   A OG  1 
ATOM   7086  N  N   . ASN   B 2 758  ? 116.859 94.657  51.440  1.00 133.15 ? 758  ASN   A N   1 
ATOM   7087  C  CA  . ASN   B 2 758  ? 118.228 94.723  51.938  1.00 133.02 ? 758  ASN   A CA  1 
ATOM   7088  C  C   . ASN   B 2 758  ? 118.414 95.920  52.856  1.00 132.85 ? 758  ASN   A C   1 
ATOM   7089  O  O   . ASN   B 2 758  ? 119.048 95.812  53.913  1.00 132.75 ? 758  ASN   A O   1 
ATOM   7090  C  CB  . ASN   B 2 758  ? 119.210 94.777  50.768  1.00 131.92 ? 758  ASN   A CB  1 
ATOM   7091  C  CG  . ASN   B 2 758  ? 118.823 95.808  49.724  1.00 132.22 ? 758  ASN   A CG  1 
ATOM   7092  O  OD1 . ASN   B 2 758  ? 118.078 96.747  50.006  1.00 132.61 ? 758  ASN   A OD1 1 
ATOM   7093  N  ND2 . ASN   B 2 758  ? 119.329 95.637  48.509  1.00 131.77 ? 758  ASN   A ND2 1 
ATOM   7094  N  N   . GLN   B 2 759  ? 117.862 97.069  52.470  1.00 129.01 ? 759  GLN   A N   1 
ATOM   7095  C  CA  . GLN   B 2 759  ? 117.886 98.216  53.364  1.00 130.11 ? 759  GLN   A CA  1 
ATOM   7096  C  C   . GLN   B 2 759  ? 117.031 97.968  54.599  1.00 132.15 ? 759  GLN   A C   1 
ATOM   7097  O  O   . GLN   B 2 759  ? 117.318 98.522  55.660  1.00 131.98 ? 759  GLN   A O   1 
ATOM   7098  C  CB  . GLN   B 2 759  ? 117.432 99.473  52.626  1.00 129.61 ? 759  GLN   A CB  1 
ATOM   7099  C  CG  . GLN   B 2 759  ? 117.629 100.751 53.420  1.00 129.30 ? 759  GLN   A CG  1 
ATOM   7100  C  CD  . GLN   B 2 759  ? 118.139 101.894 52.569  1.00 129.65 ? 759  GLN   A CD  1 
ATOM   7101  O  OE1 . GLN   B 2 759  ? 118.609 102.904 53.088  1.00 129.36 ? 759  GLN   A OE1 1 
ATOM   7102  N  NE2 . GLN   B 2 759  ? 118.053 101.738 51.253  1.00 130.06 ? 759  GLN   A NE2 1 
ATOM   7103  N  N   . ARG   B 2 760  ? 115.999 97.126  54.494  1.00 136.58 ? 760  ARG   A N   1 
ATOM   7104  C  CA  . ARG   B 2 760  ? 115.241 96.745  55.684  1.00 135.72 ? 760  ARG   A CA  1 
ATOM   7105  C  C   . ARG   B 2 760  ? 116.110 95.961  56.661  1.00 135.84 ? 760  ARG   A C   1 
ATOM   7106  O  O   . ARG   B 2 760  ? 116.094 96.220  57.872  1.00 136.50 ? 760  ARG   A O   1 
ATOM   7107  C  CB  . ARG   B 2 760  ? 114.009 95.928  55.289  1.00 135.51 ? 760  ARG   A CB  1 
ATOM   7108  C  CG  . ARG   B 2 760  ? 113.001 96.681  54.442  1.00 135.93 ? 760  ARG   A CG  1 
ATOM   7109  C  CD  . ARG   B 2 760  ? 111.720 95.884  54.261  1.00 135.69 ? 760  ARG   A CD  1 
ATOM   7110  N  NE  . ARG   B 2 760  ? 110.767 96.578  53.403  1.00 136.99 ? 760  ARG   A NE  1 
ATOM   7111  C  CZ  . ARG   B 2 760  ? 109.574 96.105  53.070  1.00 136.04 ? 760  ARG   A CZ  1 
ATOM   7112  N  NH1 . ARG   B 2 760  ? 109.148 94.932  53.509  1.00 135.26 ? 760  ARG   A NH1 1 
ATOM   7113  N  NH2 . ARG   B 2 760  ? 108.788 96.828  52.277  1.00 135.31 ? 760  ARG   A NH2 1 
ATOM   7114  N  N   . GLU   B 2 761  ? 116.874 94.991  56.151  1.00 128.86 ? 761  GLU   A N   1 
ATOM   7115  C  CA  . GLU   B 2 761  ? 117.782 94.239  57.015  1.00 129.05 ? 761  GLU   A CA  1 
ATOM   7116  C  C   . GLU   B 2 761  ? 118.849 95.149  57.616  1.00 130.94 ? 761  GLU   A C   1 
ATOM   7117  O  O   . GLU   B 2 761  ? 119.165 95.055  58.812  1.00 131.63 ? 761  GLU   A O   1 
ATOM   7118  C  CB  . GLU   B 2 761  ? 118.421 93.096  56.226  1.00 127.95 ? 761  GLU   A CB  1 
ATOM   7119  C  CG  . GLU   B 2 761  ? 119.499 92.328  56.974  1.00 129.29 ? 761  GLU   A CG  1 
ATOM   7120  C  CD  . GLU   B 2 761  ? 120.893 92.862  56.704  1.00 129.62 ? 761  GLU   A CD  1 
ATOM   7121  O  OE1 . GLU   B 2 761  ? 121.022 93.804  55.894  1.00 130.20 ? 761  GLU   A OE1 1 
ATOM   7122  O  OE2 . GLU   B 2 761  ? 121.858 92.339  57.300  1.00 129.70 ? 761  GLU   A OE2 1 
ATOM   7123  N  N   . MET   B 2 762  ? 119.411 96.043  56.800  1.00 128.50 ? 762  MET   A N   1 
ATOM   7124  C  CA  . MET   B 2 762  ? 120.407 96.979  57.307  1.00 126.87 ? 762  MET   A CA  1 
ATOM   7125  C  C   . MET   B 2 762  ? 119.810 97.887  58.374  1.00 124.58 ? 762  MET   A C   1 
ATOM   7126  O  O   . MET   B 2 762  ? 120.459 98.183  59.382  1.00 123.63 ? 762  MET   A O   1 
ATOM   7127  C  CB  . MET   B 2 762  ? 120.984 97.804  56.158  1.00 127.63 ? 762  MET   A CB  1 
ATOM   7128  C  CG  . MET   B 2 762  ? 122.246 98.563  56.518  1.00 127.45 ? 762  MET   A CG  1 
ATOM   7129  S  SD  . MET   B 2 762  ? 123.592 97.456  56.978  1.00 131.93 ? 762  MET   A SD  1 
ATOM   7130  C  CE  . MET   B 2 762  ? 123.771 96.497  55.475  1.00 126.11 ? 762  MET   A CE  1 
ATOM   7131  N  N   . ARG   B 2 763  ? 118.567 98.329  58.171  1.00 124.30 ? 763  ARG   A N   1 
ATOM   7132  C  CA  . ARG   B 2 763  ? 117.908 99.198  59.137  1.00 125.64 ? 763  ARG   A CA  1 
ATOM   7133  C  C   . ARG   B 2 763  ? 117.650 98.478  60.450  1.00 125.97 ? 763  ARG   A C   1 
ATOM   7134  O  O   . ARG   B 2 763  ? 117.819 99.067  61.520  1.00 126.90 ? 763  ARG   A O   1 
ATOM   7135  C  CB  . ARG   B 2 763  ? 116.598 99.734  58.563  1.00 126.24 ? 763  ARG   A CB  1 
ATOM   7136  C  CG  . ARG   B 2 763  ? 116.708 101.124 57.969  1.00 125.36 ? 763  ARG   A CG  1 
ATOM   7137  C  CD  . ARG   B 2 763  ? 115.338 101.739 57.719  1.00 125.47 ? 763  ARG   A CD  1 
ATOM   7138  N  NE  . ARG   B 2 763  ? 114.583 101.940 58.950  1.00 126.43 ? 763  ARG   A NE  1 
ATOM   7139  C  CZ  . ARG   B 2 763  ? 113.610 101.144 59.373  1.00 126.20 ? 763  ARG   A CZ  1 
ATOM   7140  N  NH1 . ARG   B 2 763  ? 113.240 100.078 58.682  1.00 125.77 ? 763  ARG   A NH1 1 
ATOM   7141  N  NH2 . ARG   B 2 763  ? 112.992 101.425 60.516  1.00 124.17 ? 763  ARG   A NH2 1 
ATOM   7142  N  N   . GLU   B 2 764  ? 117.221 97.215  60.400  1.00 126.36 ? 764  GLU   A N   1 
ATOM   7143  C  CA  . GLU   B 2 764  ? 116.985 96.503  61.653  1.00 126.27 ? 764  GLU   A CA  1 
ATOM   7144  C  C   . GLU   B 2 764  ? 118.295 96.255  62.397  1.00 124.65 ? 764  GLU   A C   1 
ATOM   7145  O  O   . GLU   B 2 764  ? 118.355 96.400  63.627  1.00 124.95 ? 764  GLU   A O   1 
ATOM   7146  C  CB  . GLU   B 2 764  ? 116.217 95.199  61.401  1.00 127.70 ? 764  GLU   A CB  1 
ATOM   7147  C  CG  . GLU   B 2 764  ? 116.972 94.090  60.686  1.00 127.86 ? 764  GLU   A CG  1 
ATOM   7148  C  CD  . GLU   B 2 764  ? 117.709 93.169  61.641  1.00 127.92 ? 764  GLU   A CD  1 
ATOM   7149  O  OE1 . GLU   B 2 764  ? 117.499 93.288  62.866  1.00 126.76 ? 764  GLU   A OE1 1 
ATOM   7150  O  OE2 . GLU   B 2 764  ? 118.497 92.325  61.165  1.00 126.87 ? 764  GLU   A OE2 1 
ATOM   7151  N  N   . LYS   B 2 765  ? 119.365 95.917  61.669  1.00 118.02 ? 765  LYS   A N   1 
ATOM   7152  C  CA  . LYS   B 2 765  ? 120.660 95.747  62.324  1.00 118.69 ? 765  LYS   A CA  1 
ATOM   7153  C  C   . LYS   B 2 765  ? 121.144 97.055  62.943  1.00 120.99 ? 765  LYS   A C   1 
ATOM   7154  O  O   . LYS   B 2 765  ? 121.632 97.072  64.081  1.00 121.60 ? 765  LYS   A O   1 
ATOM   7155  C  CB  . LYS   B 2 765  ? 121.689 95.213  61.330  1.00 120.01 ? 765  LYS   A CB  1 
ATOM   7156  C  CG  . LYS   B 2 765  ? 123.065 94.989  61.936  1.00 118.78 ? 765  LYS   A CG  1 
ATOM   7157  C  CD  . LYS   B 2 765  ? 122.988 94.049  63.129  1.00 118.73 ? 765  LYS   A CD  1 
ATOM   7158  C  CE  . LYS   B 2 765  ? 124.358 93.817  63.742  1.00 119.31 ? 765  LYS   A CE  1 
ATOM   7159  N  NZ  . LYS   B 2 765  ? 124.296 92.892  64.907  1.00 119.07 ? 765  LYS   A NZ  1 
ATOM   7160  N  N   . THR   B 2 766  ? 121.002 98.165  62.216  1.00 118.79 ? 766  THR   A N   1 
ATOM   7161  C  CA  . THR   B 2 766  ? 121.430 99.455  62.742  1.00 115.86 ? 766  THR   A CA  1 
ATOM   7162  C  C   . THR   B 2 766  ? 120.552 99.906  63.901  1.00 115.26 ? 766  THR   A C   1 
ATOM   7163  O  O   . THR   B 2 766  ? 121.034 100.583 64.811  1.00 115.91 ? 766  THR   A O   1 
ATOM   7164  C  CB  . THR   B 2 766  ? 121.427 100.502 61.629  1.00 117.23 ? 766  THR   A CB  1 
ATOM   7165  O  OG1 . THR   B 2 766  ? 122.151 99.997  60.500  1.00 118.88 ? 766  THR   A OG1 1 
ATOM   7166  C  CG2 . THR   B 2 766  ? 122.084 101.789 62.100  1.00 115.83 ? 766  THR   A CG2 1 
ATOM   7167  N  N   . ASP   B 2 767  ? 119.269 99.543  63.891  1.00 114.18 ? 767  ASP   A N   1 
ATOM   7168  C  CA  . ASP   B 2 767  ? 118.398 99.857  65.018  1.00 113.23 ? 767  ASP   A CA  1 
ATOM   7169  C  C   . ASP   B 2 767  ? 118.829 99.100  66.264  1.00 114.43 ? 767  ASP   A C   1 
ATOM   7170  O  O   . ASP   B 2 767  ? 118.852 99.666  67.363  1.00 115.36 ? 767  ASP   A O   1 
ATOM   7171  C  CB  . ASP   B 2 767  ? 116.947 99.534  64.664  1.00 114.94 ? 767  ASP   A CB  1 
ATOM   7172  C  CG  . ASP   B 2 767  ? 115.963 100.067 65.688  1.00 115.23 ? 767  ASP   A CG  1 
ATOM   7173  O  OD1 . ASP   B 2 767  ? 116.378 100.851 66.568  1.00 113.10 ? 767  ASP   A OD1 1 
ATOM   7174  O  OD2 . ASP   B 2 767  ? 114.772 99.701  65.612  1.00 115.79 ? 767  ASP   A OD2 1 
ATOM   7175  N  N   . GLN   B 2 768  ? 119.178 97.820  66.115  1.00 118.37 ? 768  GLN   A N   1 
ATOM   7176  C  CA  . GLN   B 2 768  ? 119.722 97.079  67.250  1.00 117.36 ? 768  GLN   A CA  1 
ATOM   7177  C  C   . GLN   B 2 768  ? 121.017 97.715  67.744  1.00 116.71 ? 768  GLN   A C   1 
ATOM   7178  O  O   . GLN   B 2 768  ? 121.234 97.855  68.956  1.00 117.87 ? 768  GLN   A O   1 
ATOM   7179  C  CB  . GLN   B 2 768  ? 119.949 95.617  66.866  1.00 116.70 ? 768  GLN   A CB  1 
ATOM   7180  C  CG  . GLN   B 2 768  ? 118.680 94.870  66.490  1.00 117.70 ? 768  GLN   A CG  1 
ATOM   7181  C  CD  . GLN   B 2 768  ? 118.945 93.427  66.107  1.00 120.09 ? 768  GLN   A CD  1 
ATOM   7182  O  OE1 . GLN   B 2 768  ? 120.088 92.970  66.113  1.00 119.66 ? 768  GLN   A OE1 1 
ATOM   7183  N  NE2 . GLN   B 2 768  ? 117.885 92.700  65.771  1.00 119.84 ? 768  GLN   A NE2 1 
ATOM   7184  N  N   . ASP   B 2 769  ? 121.883 98.122  66.813  1.00 104.81 ? 769  ASP   A N   1 
ATOM   7185  C  CA  . ASP   B 2 769  ? 123.139 98.761  67.191  1.00 102.59 ? 769  ASP   A CA  1 
ATOM   7186  C  C   . ASP   B 2 769  ? 122.893 100.069 67.938  1.00 105.00 ? 769  ASP   A C   1 
ATOM   7187  O  O   . ASP   B 2 769  ? 123.583 100.377 68.917  1.00 105.69 ? 769  ASP   A O   1 
ATOM   7188  C  CB  . ASP   B 2 769  ? 123.989 99.001  65.944  1.00 104.83 ? 769  ASP   A CB  1 
ATOM   7189  C  CG  . ASP   B 2 769  ? 125.465 99.128  66.256  1.00 107.09 ? 769  ASP   A CG  1 
ATOM   7190  O  OD1 . ASP   B 2 769  ? 125.813 99.766  67.271  1.00 108.32 ? 769  ASP   A OD1 1 
ATOM   7191  O  OD2 . ASP   B 2 769  ? 126.279 98.582  65.483  1.00 107.98 ? 769  ASP   A OD2 1 
ATOM   7192  N  N   . LEU   B 2 770  ? 121.910 100.851 67.492  1.00 102.95 ? 770  LEU   A N   1 
ATOM   7193  C  CA  . LEU   B 2 770  ? 121.628 102.132 68.129  1.00 98.62  ? 770  LEU   A CA  1 
ATOM   7194  C  C   . LEU   B 2 770  ? 120.976 101.940 69.492  1.00 100.82 ? 770  LEU   A C   1 
ATOM   7195  O  O   . LEU   B 2 770  ? 121.205 102.732 70.412  1.00 102.07 ? 770  LEU   A O   1 
ATOM   7196  C  CB  . LEU   B 2 770  ? 120.743 102.981 67.222  1.00 99.89  ? 770  LEU   A CB  1 
ATOM   7197  C  CG  . LEU   B 2 770  ? 121.130 104.455 67.165  1.00 99.50  ? 770  LEU   A CG  1 
ATOM   7198  C  CD1 . LEU   B 2 770  ? 122.583 104.584 66.752  1.00 100.13 ? 770  LEU   A CD1 1 
ATOM   7199  C  CD2 . LEU   B 2 770  ? 120.233 105.201 66.205  1.00 99.78  ? 770  LEU   A CD2 1 
ATOM   7200  N  N   . GLN   B 2 771  ? 120.156 100.897 69.641  1.00 107.86 ? 771  GLN   A N   1 
ATOM   7201  C  CA  . GLN   B 2 771  ? 119.639 100.557 70.961  1.00 106.49 ? 771  GLN   A CA  1 
ATOM   7202  C  C   . GLN   B 2 771  ? 120.774 100.181 71.903  1.00 106.64 ? 771  GLN   A C   1 
ATOM   7203  O  O   . GLN   B 2 771  ? 120.765 100.558 73.081  1.00 108.18 ? 771  GLN   A O   1 
ATOM   7204  C  CB  . GLN   B 2 771  ? 118.625 99.417  70.859  1.00 105.74 ? 771  GLN   A CB  1 
ATOM   7205  C  CG  . GLN   B 2 771  ? 117.340 99.776  70.127  1.00 105.97 ? 771  GLN   A CG  1 
ATOM   7206  C  CD  . GLN   B 2 771  ? 116.458 100.726 70.911  1.00 109.50 ? 771  GLN   A CD  1 
ATOM   7207  O  OE1 . GLN   B 2 771  ? 116.663 100.943 72.106  1.00 109.46 ? 771  GLN   A OE1 1 
ATOM   7208  N  NE2 . GLN   B 2 771  ? 115.465 101.297 70.241  1.00 109.66 ? 771  GLN   A NE2 1 
ATOM   7209  N  N   . TYR   B 2 772  ? 121.762 99.438  71.399  1.00 99.85  ? 772  TYR   A N   1 
ATOM   7210  C  CA  . TYR   B 2 772  ? 122.945 99.150  72.205  1.00 98.15  ? 772  TYR   A CA  1 
ATOM   7211  C  C   . TYR   B 2 772  ? 123.684 100.429 72.582  1.00 98.68  ? 772  TYR   A C   1 
ATOM   7212  O  O   . TYR   B 2 772  ? 124.134 100.581 73.723  1.00 101.27 ? 772  TYR   A O   1 
ATOM   7213  C  CB  . TYR   B 2 772  ? 123.881 98.202  71.458  1.00 99.69  ? 772  TYR   A CB  1 
ATOM   7214  C  CG  . TYR   B 2 772  ? 125.304 98.255  71.964  1.00 97.17  ? 772  TYR   A CG  1 
ATOM   7215  C  CD1 . TYR   B 2 772  ? 125.638 97.740  73.208  1.00 96.65  ? 772  TYR   A CD1 1 
ATOM   7216  C  CD2 . TYR   B 2 772  ? 126.312 98.823  71.198  1.00 98.41  ? 772  TYR   A CD2 1 
ATOM   7217  C  CE1 . TYR   B 2 772  ? 126.935 97.788  73.675  1.00 97.36  ? 772  TYR   A CE1 1 
ATOM   7218  C  CE2 . TYR   B 2 772  ? 127.613 98.875  71.657  1.00 98.24  ? 772  TYR   A CE2 1 
ATOM   7219  C  CZ  . TYR   B 2 772  ? 127.918 98.357  72.897  1.00 98.05  ? 772  TYR   A CZ  1 
ATOM   7220  O  OH  . TYR   B 2 772  ? 129.213 98.406  73.359  1.00 99.10  ? 772  TYR   A OH  1 
ATOM   7221  N  N   . PHE   B 2 773  ? 123.829 101.353 71.629  1.00 93.68  ? 773  PHE   A N   1 
ATOM   7222  C  CA  . PHE   B 2 773  ? 124.514 102.614 71.905  1.00 92.18  ? 773  PHE   A CA  1 
ATOM   7223  C  C   . PHE   B 2 773  ? 123.797 103.403 72.993  1.00 92.06  ? 773  PHE   A C   1 
ATOM   7224  O  O   . PHE   B 2 773  ? 124.430 103.939 73.910  1.00 91.06  ? 773  PHE   A O   1 
ATOM   7225  C  CB  . PHE   B 2 773  ? 124.618 103.450 70.630  1.00 88.88  ? 773  PHE   A CB  1 
ATOM   7226  C  CG  . PHE   B 2 773  ? 125.702 103.007 69.696  1.00 86.60  ? 773  PHE   A CG  1 
ATOM   7227  C  CD1 . PHE   B 2 773  ? 126.767 102.255 70.152  1.00 88.77  ? 773  PHE   A CD1 1 
ATOM   7228  C  CD2 . PHE   B 2 773  ? 125.660 103.353 68.358  1.00 88.27  ? 773  PHE   A CD2 1 
ATOM   7229  C  CE1 . PHE   B 2 773  ? 127.764 101.851 69.290  1.00 93.30  ? 773  PHE   A CE1 1 
ATOM   7230  C  CE2 . PHE   B 2 773  ? 126.655 102.953 67.493  1.00 88.42  ? 773  PHE   A CE2 1 
ATOM   7231  C  CZ  . PHE   B 2 773  ? 127.709 102.202 67.960  1.00 92.17  ? 773  PHE   A CZ  1 
ATOM   7232  N  N   . ALA   B 2 774  ? 122.470 103.486 72.903  1.00 95.97  ? 774  ALA   A N   1 
ATOM   7233  C  CA  . ALA   B 2 774  ? 121.704 104.233 73.894  1.00 94.11  ? 774  ALA   A CA  1 
ATOM   7234  C  C   . ALA   B 2 774  ? 121.687 103.528 75.244  1.00 94.39  ? 774  ALA   A C   1 
ATOM   7235  O  O   . ALA   B 2 774  ? 121.569 104.188 76.282  1.00 96.51  ? 774  ALA   A O   1 
ATOM   7236  C  CB  . ALA   B 2 774  ? 120.277 104.458 73.397  1.00 95.09  ? 774  ALA   A CB  1 
ATOM   7237  N  N   . SER   B 2 775  ? 121.793 102.196 75.252  1.00 101.07 ? 775  SER   A N   1 
ATOM   7238  C  CA  . SER   B 2 775  ? 121.783 101.462 76.514  1.00 101.67 ? 775  SER   A CA  1 
ATOM   7239  C  C   . SER   B 2 775  ? 122.976 101.838 77.382  1.00 100.50 ? 775  SER   A C   1 
ATOM   7240  O  O   . SER   B 2 775  ? 122.832 102.043 78.593  1.00 102.87 ? 775  SER   A O   1 
ATOM   7241  C  CB  . SER   B 2 775  ? 121.768 99.957  76.245  1.00 102.26 ? 775  SER   A CB  1 
ATOM   7242  O  OG  . SER   B 2 775  ? 122.922 99.555  75.529  1.00 103.95 ? 775  SER   A OG  1 
ATOM   7243  N  N   . GLU   B 2 776  ? 124.165 101.934 76.783  1.00 98.55  ? 776  GLU   A N   1 
ATOM   7244  C  CA  . GLU   B 2 776  ? 125.335 102.364 77.540  1.00 99.62  ? 776  GLU   A CA  1 
ATOM   7245  C  C   . GLU   B 2 776  ? 125.275 103.853 77.852  1.00 101.19 ? 776  GLU   A C   1 
ATOM   7246  O  O   . GLU   B 2 776  ? 125.843 104.302 78.855  1.00 100.21 ? 776  GLU   A O   1 
ATOM   7247  C  CB  . GLU   B 2 776  ? 126.611 102.023 76.767  1.00 98.99  ? 776  GLU   A CB  1 
ATOM   7248  C  CG  . GLU   B 2 776  ? 127.900 102.162 77.566  1.00 102.50 ? 776  GLU   A CG  1 
ATOM   7249  C  CD  . GLU   B 2 776  ? 128.501 103.552 77.479  1.00 103.02 ? 776  GLU   A CD  1 
ATOM   7250  O  OE1 . GLU   B 2 776  ? 128.043 104.347 76.632  1.00 102.77 ? 776  GLU   A OE1 1 
ATOM   7251  O  OE2 . GLU   B 2 776  ? 129.431 103.849 78.258  1.00 100.56 ? 776  GLU   A OE2 1 
ATOM   7252  N  N   . GLY   B 2 777  ? 124.594 104.626 77.011  1.00 92.89  ? 777  GLY   A N   1 
ATOM   7253  C  CA  . GLY   B 2 777  ? 124.437 106.053 77.208  1.00 90.07  ? 777  GLY   A CA  1 
ATOM   7254  C  C   . GLY   B 2 777  ? 125.372 106.843 76.321  1.00 88.82  ? 777  GLY   A C   1 
ATOM   7255  O  O   . GLY   B 2 777  ? 126.535 107.061 76.671  1.00 92.20  ? 777  GLY   A O   1 
ATOM   7256  N  N   . LEU   B 2 778  ? 124.860 107.305 75.182  1.00 77.95  ? 778  LEU   A N   1 
ATOM   7257  C  CA  . LEU   B 2 778  ? 125.668 107.970 74.171  1.00 78.16  ? 778  LEU   A CA  1 
ATOM   7258  C  C   . LEU   B 2 778  ? 124.746 108.814 73.305  1.00 81.12  ? 778  LEU   A C   1 
ATOM   7259  O  O   . LEU   B 2 778  ? 123.538 108.573 73.263  1.00 83.46  ? 778  LEU   A O   1 
ATOM   7260  C  CB  . LEU   B 2 778  ? 126.432 106.957 73.304  1.00 81.62  ? 778  LEU   A CB  1 
ATOM   7261  C  CG  . LEU   B 2 778  ? 127.612 106.192 73.912  1.00 80.26  ? 778  LEU   A CG  1 
ATOM   7262  C  CD1 . LEU   B 2 778  ? 127.916 104.924 73.131  1.00 81.09  ? 778  LEU   A CD1 1 
ATOM   7263  C  CD2 . LEU   B 2 778  ? 128.841 107.076 73.993  1.00 79.34  ? 778  LEU   A CD2 1 
ATOM   7264  N  N   . ARG   B 2 779  ? 125.321 109.799 72.622  1.00 85.71  ? 779  ARG   A N   1 
ATOM   7265  C  CA  . ARG   B 2 779  ? 124.579 110.631 71.684  1.00 85.40  ? 779  ARG   A CA  1 
ATOM   7266  C  C   . ARG   B 2 779  ? 124.889 110.163 70.268  1.00 89.15  ? 779  ARG   A C   1 
ATOM   7267  O  O   . ARG   B 2 779  ? 126.057 110.114 69.867  1.00 92.29  ? 779  ARG   A O   1 
ATOM   7268  C  CB  . ARG   B 2 779  ? 124.939 112.102 71.875  1.00 84.92  ? 779  ARG   A CB  1 
ATOM   7269  C  CG  . ARG   B 2 779  ? 124.602 112.626 73.264  1.00 88.48  ? 779  ARG   A CG  1 
ATOM   7270  C  CD  . ARG   B 2 779  ? 125.269 113.961 73.558  1.00 87.56  ? 779  ARG   A CD  1 
ATOM   7271  N  NE  . ARG   B 2 779  ? 124.727 115.049 72.753  1.00 89.21  ? 779  ARG   A NE  1 
ATOM   7272  C  CZ  . ARG   B 2 779  ? 125.282 115.503 71.638  1.00 90.37  ? 779  ARG   A CZ  1 
ATOM   7273  N  NH1 . ARG   B 2 779  ? 126.396 114.977 71.157  1.00 89.29  ? 779  ARG   A NH1 1 
ATOM   7274  N  NH2 . ARG   B 2 779  ? 124.706 116.513 70.992  1.00 89.57  ? 779  ARG   A NH2 1 
ATOM   7275  N  N   . THR   B 2 780  ? 123.847 109.824 69.513  1.00 85.81  ? 780  THR   A N   1 
ATOM   7276  C  CA  . THR   B 2 780  ? 123.984 109.110 68.253  1.00 82.47  ? 780  THR   A CA  1 
ATOM   7277  C  C   . THR   B 2 780  ? 123.460 109.935 67.085  1.00 83.58  ? 780  THR   A C   1 
ATOM   7278  O  O   . THR   B 2 780  ? 122.378 110.525 67.163  1.00 86.62  ? 780  THR   A O   1 
ATOM   7279  C  CB  . THR   B 2 780  ? 123.236 107.779 68.307  1.00 86.85  ? 780  THR   A CB  1 
ATOM   7280  O  OG1 . THR   B 2 780  ? 121.843 108.026 68.530  1.00 91.24  ? 780  THR   A OG1 1 
ATOM   7281  C  CG2 . THR   B 2 780  ? 123.776 106.912 69.430  1.00 87.06  ? 780  THR   A CG2 1 
ATOM   7282  N  N   . LEU   B 2 781  ? 124.230 109.959 66.000  1.00 82.45  ? 781  LEU   A N   1 
ATOM   7283  C  CA  . LEU   B 2 781  ? 123.825 110.567 64.741  1.00 78.94  ? 781  LEU   A CA  1 
ATOM   7284  C  C   . LEU   B 2 781  ? 123.854 109.502 63.655  1.00 84.86  ? 781  LEU   A C   1 
ATOM   7285  O  O   . LEU   B 2 781  ? 124.807 108.720 63.575  1.00 88.03  ? 781  LEU   A O   1 
ATOM   7286  C  CB  . LEU   B 2 781  ? 124.744 111.729 64.357  1.00 80.51  ? 781  LEU   A CB  1 
ATOM   7287  C  CG  . LEU   B 2 781  ? 124.859 112.903 65.325  1.00 83.82  ? 781  LEU   A CG  1 
ATOM   7288  C  CD1 . LEU   B 2 781  ? 125.796 113.955 64.760  1.00 85.31  ? 781  LEU   A CD1 1 
ATOM   7289  C  CD2 . LEU   B 2 781  ? 123.496 113.497 65.606  1.00 86.75  ? 781  LEU   A CD2 1 
ATOM   7290  N  N   . CYS   B 2 782  ? 122.817 109.474 62.822  1.00 90.86  ? 782  CYS   A N   1 
ATOM   7291  C  CA  . CYS   B 2 782  ? 122.708 108.493 61.747  1.00 86.28  ? 782  CYS   A CA  1 
ATOM   7292  C  C   . CYS   B 2 782  ? 123.114 109.150 60.434  1.00 87.76  ? 782  CYS   A C   1 
ATOM   7293  O  O   . CYS   B 2 782  ? 122.457 110.090 59.973  1.00 93.42  ? 782  CYS   A O   1 
ATOM   7294  C  CB  . CYS   B 2 782  ? 121.289 107.939 61.665  1.00 86.23  ? 782  CYS   A CB  1 
ATOM   7295  S  SG  . CYS   B 2 782  ? 120.740 107.070 63.146  1.00 96.88  ? 782  CYS   A SG  1 
ATOM   7296  N  N   . LEU   B 2 783  ? 124.189 108.656 59.829  1.00 77.28  ? 783  LEU   A N   1 
ATOM   7297  C  CA  . LEU   B 2 783  ? 124.633 109.169 58.543  1.00 80.94  ? 783  LEU   A CA  1 
ATOM   7298  C  C   . LEU   B 2 783  ? 123.848 108.521 57.408  1.00 86.51  ? 783  LEU   A C   1 
ATOM   7299  O  O   . LEU   B 2 783  ? 123.257 107.449 57.565  1.00 90.90  ? 783  LEU   A O   1 
ATOM   7300  C  CB  . LEU   B 2 783  ? 126.129 108.926 58.353  1.00 82.61  ? 783  LEU   A CB  1 
ATOM   7301  C  CG  . LEU   B 2 783  ? 127.066 109.430 59.454  1.00 85.40  ? 783  LEU   A CG  1 
ATOM   7302  C  CD1 . LEU   B 2 783  ? 128.505 109.437 58.963  1.00 87.21  ? 783  LEU   A CD1 1 
ATOM   7303  C  CD2 . LEU   B 2 783  ? 126.661 110.812 59.929  1.00 86.90  ? 783  LEU   A CD2 1 
ATOM   7304  N  N   . ALA   B 2 784  ? 123.845 109.184 56.253  1.00 91.16  ? 784  ALA   A N   1 
ATOM   7305  C  CA  . ALA   B 2 784  ? 123.102 108.730 55.088  1.00 88.60  ? 784  ALA   A CA  1 
ATOM   7306  C  C   . ALA   B 2 784  ? 123.925 108.952 53.826  1.00 90.35  ? 784  ALA   A C   1 
ATOM   7307  O  O   . ALA   B 2 784  ? 125.017 109.524 53.859  1.00 94.69  ? 784  ALA   A O   1 
ATOM   7308  C  CB  . ALA   B 2 784  ? 121.750 109.445 54.975  1.00 90.41  ? 784  ALA   A CB  1 
ATOM   7309  N  N   . TYR   B 2 785  ? 123.381 108.489 52.702  1.00 93.52  ? 785  TYR   A N   1 
ATOM   7310  C  CA  . TYR   B 2 785  ? 124.056 108.584 51.416  1.00 92.69  ? 785  TYR   A CA  1 
ATOM   7311  C  C   . TYR   B 2 785  ? 123.006 108.647 50.318  1.00 92.10  ? 785  TYR   A C   1 
ATOM   7312  O  O   . TYR   B 2 785  ? 121.856 108.244 50.509  1.00 91.98  ? 785  TYR   A O   1 
ATOM   7313  C  CB  . TYR   B 2 785  ? 125.000 107.395 51.195  1.00 95.31  ? 785  TYR   A CB  1 
ATOM   7314  C  CG  . TYR   B 2 785  ? 126.169 107.653 50.271  1.00 96.48  ? 785  TYR   A CG  1 
ATOM   7315  C  CD1 . TYR   B 2 785  ? 126.413 108.916 49.754  1.00 97.78  ? 785  TYR   A CD1 1 
ATOM   7316  C  CD2 . TYR   B 2 785  ? 127.033 106.625 49.918  1.00 97.00  ? 785  TYR   A CD2 1 
ATOM   7317  C  CE1 . TYR   B 2 785  ? 127.483 109.148 48.908  1.00 99.62  ? 785  TYR   A CE1 1 
ATOM   7318  C  CE2 . TYR   B 2 785  ? 128.104 106.846 49.075  1.00 97.52  ? 785  TYR   A CE2 1 
ATOM   7319  C  CZ  . TYR   B 2 785  ? 128.325 108.109 48.574  1.00 100.31 ? 785  TYR   A CZ  1 
ATOM   7320  O  OH  . TYR   B 2 785  ? 129.391 108.336 47.734  1.00 101.57 ? 785  TYR   A OH  1 
ATOM   7321  N  N   . ARG   B 2 786  ? 123.417 109.161 49.161  1.00 105.97 ? 786  ARG   A N   1 
ATOM   7322  C  CA  . ARG   B 2 786  ? 122.574 109.256 47.976  1.00 108.83 ? 786  ARG   A CA  1 
ATOM   7323  C  C   . ARG   B 2 786  ? 123.440 109.686 46.802  1.00 111.53 ? 786  ARG   A C   1 
ATOM   7324  O  O   . ARG   B 2 786  ? 124.344 110.511 46.959  1.00 113.74 ? 786  ARG   A O   1 
ATOM   7325  C  CB  . ARG   B 2 786  ? 121.421 110.247 48.179  1.00 105.47 ? 786  ARG   A CB  1 
ATOM   7326  C  CG  . ARG   B 2 786  ? 120.717 110.664 46.902  1.00 104.18 ? 786  ARG   A CG  1 
ATOM   7327  C  CD  . ARG   B 2 786  ? 119.935 109.522 46.283  1.00 108.69 ? 786  ARG   A CD  1 
ATOM   7328  N  NE  . ARG   B 2 786  ? 119.930 109.593 44.826  1.00 112.92 ? 786  ARG   A NE  1 
ATOM   7329  C  CZ  . ARG   B 2 786  ? 119.164 110.407 44.111  1.00 113.84 ? 786  ARG   A CZ  1 
ATOM   7330  N  NH1 . ARG   B 2 786  ? 118.333 111.260 44.686  1.00 112.13 ? 786  ARG   A NH1 1 
ATOM   7331  N  NH2 . ARG   B 2 786  ? 119.240 110.369 42.784  1.00 112.57 ? 786  ARG   A NH2 1 
ATOM   7332  N  N   . ILE   B 2 787  ? 123.159 109.118 45.632  1.00 109.27 ? 787  ILE   A N   1 
ATOM   7333  C  CA  . ILE   B 2 787  ? 123.820 109.498 44.389  1.00 106.35 ? 787  ILE   A CA  1 
ATOM   7334  C  C   . ILE   B 2 787  ? 122.784 110.172 43.502  1.00 105.28 ? 787  ILE   A C   1 
ATOM   7335  O  O   . ILE   B 2 787  ? 121.803 109.539 43.094  1.00 104.84 ? 787  ILE   A O   1 
ATOM   7336  C  CB  . ILE   B 2 787  ? 124.448 108.290 43.678  1.00 109.05 ? 787  ILE   A CB  1 
ATOM   7337  C  CG1 . ILE   B 2 787  ? 125.486 107.622 44.582  1.00 109.44 ? 787  ILE   A CG1 1 
ATOM   7338  C  CG2 . ILE   B 2 787  ? 125.081 108.719 42.363  1.00 108.54 ? 787  ILE   A CG2 1 
ATOM   7339  C  CD1 . ILE   B 2 787  ? 126.621 108.535 44.983  1.00 108.12 ? 787  ILE   A CD1 1 
ATOM   7340  N  N   . LEU   B 2 788  ? 123.008 111.446 43.194  1.00 115.19 ? 788  LEU   A N   1 
ATOM   7341  C  CA  . LEU   B 2 788  ? 122.061 112.255 42.440  1.00 116.26 ? 788  LEU   A CA  1 
ATOM   7342  C  C   . LEU   B 2 788  ? 122.422 112.240 40.961  1.00 119.49 ? 788  LEU   A C   1 
ATOM   7343  O  O   . LEU   B 2 788  ? 123.573 112.497 40.595  1.00 117.12 ? 788  LEU   A O   1 
ATOM   7344  C  CB  . LEU   B 2 788  ? 122.048 113.695 42.957  1.00 114.24 ? 788  LEU   A CB  1 
ATOM   7345  C  CG  . LEU   B 2 788  ? 120.770 114.211 43.622  1.00 113.54 ? 788  LEU   A CG  1 
ATOM   7346  C  CD1 . LEU   B 2 788  ? 119.545 113.849 42.796  1.00 116.00 ? 788  LEU   A CD1 1 
ATOM   7347  C  CD2 . LEU   B 2 788  ? 120.645 113.691 45.041  1.00 114.56 ? 788  LEU   A CD2 1 
ATOM   7348  N  N   . ASP   B 2 789  ? 121.438 111.938 40.117  1.00 129.95 ? 789  ASP   A N   1 
ATOM   7349  C  CA  . ASP   B 2 789  ? 121.645 112.020 38.682  1.00 128.12 ? 789  ASP   A CA  1 
ATOM   7350  C  C   . ASP   B 2 789  ? 121.650 113.482 38.237  1.00 126.49 ? 789  ASP   A C   1 
ATOM   7351  O  O   . ASP   B 2 789  ? 120.974 114.322 38.838  1.00 125.04 ? 789  ASP   A O   1 
ATOM   7352  C  CB  . ASP   B 2 789  ? 120.559 111.246 37.938  1.00 126.05 ? 789  ASP   A CB  1 
ATOM   7353  C  CG  . ASP   B 2 789  ? 119.181 111.835 38.141  1.00 127.18 ? 789  ASP   A CG  1 
ATOM   7354  O  OD1 . ASP   B 2 789  ? 118.837 112.806 37.435  1.00 126.83 ? 789  ASP   A OD1 1 
ATOM   7355  O  OD2 . ASP   B 2 789  ? 118.442 111.324 39.008  1.00 127.29 ? 789  ASP   A OD2 1 
ATOM   7356  N  N   . PRO   B 2 790  ? 122.407 113.812 37.186  1.00 125.75 ? 790  PRO   A N   1 
ATOM   7357  C  CA  . PRO   B 2 790  ? 122.530 115.228 36.795  1.00 126.40 ? 790  PRO   A CA  1 
ATOM   7358  C  C   . PRO   B 2 790  ? 121.210 115.892 36.442  1.00 125.72 ? 790  PRO   A C   1 
ATOM   7359  O  O   . PRO   B 2 790  ? 121.032 117.082 36.727  1.00 127.05 ? 790  PRO   A O   1 
ATOM   7360  C  CB  . PRO   B 2 790  ? 123.481 115.173 35.589  1.00 126.24 ? 790  PRO   A CB  1 
ATOM   7361  C  CG  . PRO   B 2 790  ? 123.391 113.768 35.089  1.00 125.95 ? 790  PRO   A CG  1 
ATOM   7362  C  CD  . PRO   B 2 790  ? 123.190 112.928 36.308  1.00 125.60 ? 790  PRO   A CD  1 
ATOM   7363  N  N   . GLN   B 2 791  ? 120.274 115.162 35.833  1.00 127.94 ? 791  GLN   A N   1 
ATOM   7364  C  CA  . GLN   B 2 791  ? 119.005 115.770 35.446  1.00 129.41 ? 791  GLN   A CA  1 
ATOM   7365  C  C   . GLN   B 2 791  ? 118.194 116.180 36.669  1.00 127.67 ? 791  GLN   A C   1 
ATOM   7366  O  O   . GLN   B 2 791  ? 117.735 117.326 36.771  1.00 127.71 ? 791  GLN   A O   1 
ATOM   7367  C  CB  . GLN   B 2 791  ? 118.209 114.804 34.568  1.00 130.44 ? 791  GLN   A CB  1 
ATOM   7368  C  CG  . GLN   B 2 791  ? 118.945 114.347 33.317  1.00 130.94 ? 791  GLN   A CG  1 
ATOM   7369  C  CD  . GLN   B 2 791  ? 119.167 115.470 32.321  1.00 131.09 ? 791  GLN   A CD  1 
ATOM   7370  O  OE1 . GLN   B 2 791  ? 118.466 116.482 32.341  1.00 130.49 ? 791  GLN   A OE1 1 
ATOM   7371  N  NE2 . GLN   B 2 791  ? 120.147 115.296 31.443  1.00 130.01 ? 791  GLN   A NE2 1 
ATOM   7372  N  N   . VAL   B 2 792  ? 118.012 115.255 37.614  1.00 124.96 ? 792  VAL   A N   1 
ATOM   7373  C  CA  . VAL   B 2 792  ? 117.285 115.580 38.836  1.00 127.02 ? 792  VAL   A CA  1 
ATOM   7374  C  C   . VAL   B 2 792  ? 118.054 116.610 39.650  1.00 128.98 ? 792  VAL   A C   1 
ATOM   7375  O  O   . VAL   B 2 792  ? 117.459 117.474 40.303  1.00 129.01 ? 792  VAL   A O   1 
ATOM   7376  C  CB  . VAL   B 2 792  ? 116.996 114.301 39.643  1.00 128.14 ? 792  VAL   A CB  1 
ATOM   7377  C  CG1 . VAL   B 2 792  ? 116.427 114.643 41.011  1.00 128.81 ? 792  VAL   A CG1 1 
ATOM   7378  C  CG2 . VAL   B 2 792  ? 116.025 113.413 38.883  1.00 127.89 ? 792  VAL   A CG2 1 
ATOM   7379  N  N   . TYR   B 2 793  ? 119.387 116.542 39.622  1.00 129.10 ? 793  TYR   A N   1 
ATOM   7380  C  CA  . TYR   B 2 793  ? 120.197 117.540 40.313  1.00 129.96 ? 793  TYR   A CA  1 
ATOM   7381  C  C   . TYR   B 2 793  ? 119.909 118.941 39.786  1.00 128.84 ? 793  TYR   A C   1 
ATOM   7382  O  O   . TYR   B 2 793  ? 119.671 119.871 40.564  1.00 128.09 ? 793  TYR   A O   1 
ATOM   7383  C  CB  . TYR   B 2 793  ? 121.681 117.201 40.167  1.00 130.00 ? 793  TYR   A CB  1 
ATOM   7384  C  CG  . TYR   B 2 793  ? 122.601 118.398 40.257  1.00 130.55 ? 793  TYR   A CG  1 
ATOM   7385  C  CD1 . TYR   B 2 793  ? 122.894 118.984 41.482  1.00 128.92 ? 793  TYR   A CD1 1 
ATOM   7386  C  CD2 . TYR   B 2 793  ? 123.183 118.937 39.117  1.00 129.85 ? 793  TYR   A CD2 1 
ATOM   7387  C  CE1 . TYR   B 2 793  ? 123.737 120.078 41.566  1.00 127.81 ? 793  TYR   A CE1 1 
ATOM   7388  C  CE2 . TYR   B 2 793  ? 124.026 120.029 39.192  1.00 128.54 ? 793  TYR   A CE2 1 
ATOM   7389  C  CZ  . TYR   B 2 793  ? 124.300 120.595 40.418  1.00 128.77 ? 793  TYR   A CZ  1 
ATOM   7390  O  OH  . TYR   B 2 793  ? 125.139 121.683 40.495  1.00 129.58 ? 793  TYR   A OH  1 
ATOM   7391  N  N   . GLU   B 2 794  ? 119.918 119.109 38.462  1.00 129.04 ? 794  GLU   A N   1 
ATOM   7392  C  CA  . GLU   B 2 794  ? 119.637 120.417 37.878  1.00 128.72 ? 794  GLU   A CA  1 
ATOM   7393  C  C   . GLU   B 2 794  ? 118.204 120.855 38.154  1.00 128.61 ? 794  GLU   A C   1 
ATOM   7394  O  O   . GLU   B 2 794  ? 117.954 122.031 38.453  1.00 128.83 ? 794  GLU   A O   1 
ATOM   7395  C  CB  . GLU   B 2 794  ? 119.910 120.392 36.375  1.00 129.59 ? 794  GLU   A CB  1 
ATOM   7396  C  CG  . GLU   B 2 794  ? 121.374 120.209 36.011  1.00 129.95 ? 794  GLU   A CG  1 
ATOM   7397  C  CD  . GLU   B 2 794  ? 121.604 120.190 34.513  1.00 131.59 ? 794  GLU   A CD  1 
ATOM   7398  O  OE1 . GLU   B 2 794  ? 120.619 120.329 33.757  1.00 132.32 ? 794  GLU   A OE1 1 
ATOM   7399  O  OE2 . GLU   B 2 794  ? 122.769 120.036 34.090  1.00 131.67 ? 794  GLU   A OE2 1 
ATOM   7400  N  N   . GLN   B 2 795  ? 117.248 119.927 38.053  1.00 127.24 ? 795  GLN   A N   1 
ATOM   7401  C  CA  . GLN   B 2 795  ? 115.856 120.279 38.313  1.00 128.28 ? 795  GLN   A CA  1 
ATOM   7402  C  C   . GLN   B 2 795  ? 115.668 120.759 39.747  1.00 129.38 ? 795  GLN   A C   1 
ATOM   7403  O  O   . GLN   B 2 795  ? 115.018 121.785 39.990  1.00 130.31 ? 795  GLN   A O   1 
ATOM   7404  C  CB  . GLN   B 2 795  ? 114.950 119.084 38.024  1.00 129.84 ? 795  GLN   A CB  1 
ATOM   7405  C  CG  . GLN   B 2 795  ? 113.476 119.343 38.294  1.00 130.78 ? 795  GLN   A CG  1 
ATOM   7406  C  CD  . GLN   B 2 795  ? 112.608 118.135 38.001  1.00 130.50 ? 795  GLN   A CD  1 
ATOM   7407  O  OE1 . GLN   B 2 795  ? 113.102 117.086 37.588  1.00 130.82 ? 795  GLN   A OE1 1 
ATOM   7408  N  NE2 . GLN   B 2 795  ? 111.305 118.278 38.213  1.00 129.29 ? 795  GLN   A NE2 1 
ATOM   7409  N  N   . TRP   B 2 796  ? 116.250 120.044 40.711  1.00 125.69 ? 796  TRP   A N   1 
ATOM   7410  C  CA  . TRP   B 2 796  ? 116.108 120.450 42.101  1.00 127.70 ? 796  TRP   A CA  1 
ATOM   7411  C  C   . TRP   B 2 796  ? 116.893 121.719 42.400  1.00 129.56 ? 796  TRP   A C   1 
ATOM   7412  O  O   . TRP   B 2 796  ? 116.482 122.503 43.258  1.00 128.42 ? 796  TRP   A O   1 
ATOM   7413  C  CB  . TRP   B 2 796  ? 116.546 119.331 43.041  1.00 126.52 ? 796  TRP   A CB  1 
ATOM   7414  C  CG  . TRP   B 2 796  ? 116.404 119.729 44.471  1.00 127.66 ? 796  TRP   A CG  1 
ATOM   7415  C  CD1 . TRP   B 2 796  ? 115.270 119.676 45.225  1.00 127.13 ? 796  TRP   A CD1 1 
ATOM   7416  C  CD2 . TRP   B 2 796  ? 117.424 120.275 45.315  1.00 127.60 ? 796  TRP   A CD2 1 
ATOM   7417  N  NE1 . TRP   B 2 796  ? 115.522 120.144 46.489  1.00 125.66 ? 796  TRP   A NE1 1 
ATOM   7418  C  CE2 . TRP   B 2 796  ? 116.837 120.518 46.571  1.00 126.46 ? 796  TRP   A CE2 1 
ATOM   7419  C  CE3 . TRP   B 2 796  ? 118.776 120.575 45.132  1.00 127.40 ? 796  TRP   A CE3 1 
ATOM   7420  C  CZ2 . TRP   B 2 796  ? 117.557 121.044 47.640  1.00 126.56 ? 796  TRP   A CZ2 1 
ATOM   7421  C  CZ3 . TRP   B 2 796  ? 119.488 121.099 46.194  1.00 126.62 ? 796  TRP   A CZ3 1 
ATOM   7422  C  CH2 . TRP   B 2 796  ? 118.878 121.328 47.432  1.00 126.67 ? 796  TRP   A CH2 1 
ATOM   7423  N  N   . ALA   B 2 797  ? 118.020 121.940 41.718  1.00 131.11 ? 797  ALA   A N   1 
ATOM   7424  C  CA  . ALA   B 2 797  ? 118.731 123.203 41.881  1.00 128.61 ? 797  ALA   A CA  1 
ATOM   7425  C  C   . ALA   B 2 797  ? 117.876 124.370 41.408  1.00 128.06 ? 797  ALA   A C   1 
ATOM   7426  O  O   . ALA   B 2 797  ? 117.818 125.417 42.065  1.00 128.89 ? 797  ALA   A O   1 
ATOM   7427  C  CB  . ALA   B 2 797  ? 120.057 123.163 41.123  1.00 127.02 ? 797  ALA   A CB  1 
ATOM   7428  N  N   . LYS   B 2 798  ? 117.196 124.203 40.272  1.00 131.54 ? 798  LYS   A N   1 
ATOM   7429  C  CA  . LYS   B 2 798  ? 116.283 125.239 39.799  1.00 133.51 ? 798  LYS   A CA  1 
ATOM   7430  C  C   . LYS   B 2 798  ? 115.143 125.459 40.787  1.00 133.04 ? 798  LYS   A C   1 
ATOM   7431  O  O   . LYS   B 2 798  ? 114.771 126.605 41.075  1.00 131.64 ? 798  LYS   A O   1 
ATOM   7432  C  CB  . LYS   B 2 798  ? 115.743 124.866 38.418  1.00 133.83 ? 798  LYS   A CB  1 
ATOM   7433  C  CG  . LYS   B 2 798  ? 114.730 125.847 37.846  1.00 133.67 ? 798  LYS   A CG  1 
ATOM   7434  C  CD  . LYS   B 2 798  ? 113.317 125.286 37.908  1.00 134.87 ? 798  LYS   A CD  1 
ATOM   7435  C  CE  . LYS   B 2 798  ? 113.202 123.988 37.125  1.00 133.78 ? 798  LYS   A CE  1 
ATOM   7436  N  NZ  . LYS   B 2 798  ? 113.535 124.178 35.686  1.00 131.99 ? 798  LYS   A NZ  1 
ATOM   7437  N  N   . GLU   B 2 799  ? 114.579 124.372 41.320  1.00 127.31 ? 799  GLU   A N   1 
ATOM   7438  C  CA  . GLU   B 2 799  ? 113.495 124.504 42.290  1.00 126.70 ? 799  GLU   A CA  1 
ATOM   7439  C  C   . GLU   B 2 799  ? 113.961 125.225 43.550  1.00 128.53 ? 799  GLU   A C   1 
ATOM   7440  O  O   . GLU   B 2 799  ? 113.246 126.078 44.089  1.00 128.39 ? 799  GLU   A O   1 
ATOM   7441  C  CB  . GLU   B 2 799  ? 112.929 123.127 42.639  1.00 128.52 ? 799  GLU   A CB  1 
ATOM   7442  C  CG  . GLU   B 2 799  ? 112.237 122.428 41.481  1.00 130.57 ? 799  GLU   A CG  1 
ATOM   7443  C  CD  . GLU   B 2 799  ? 111.681 121.071 41.868  1.00 130.78 ? 799  GLU   A CD  1 
ATOM   7444  O  OE1 . GLU   B 2 799  ? 111.851 120.668 43.038  1.00 129.04 ? 799  GLU   A OE1 1 
ATOM   7445  O  OE2 . GLU   B 2 799  ? 111.075 120.407 41.001  1.00 131.19 ? 799  GLU   A OE2 1 
ATOM   7446  N  N   . TYR   B 2 800  ? 115.158 124.890 44.035  1.00 128.83 ? 800  TYR   A N   1 
ATOM   7447  C  CA  . TYR   B 2 800  ? 115.707 125.545 45.218  1.00 128.65 ? 800  TYR   A CA  1 
ATOM   7448  C  C   . TYR   B 2 800  ? 115.963 127.023 44.961  1.00 127.28 ? 800  TYR   A C   1 
ATOM   7449  O  O   . TYR   B 2 800  ? 115.689 127.867 45.822  1.00 126.87 ? 800  TYR   A O   1 
ATOM   7450  C  CB  . TYR   B 2 800  ? 116.993 124.836 45.648  1.00 127.06 ? 800  TYR   A CB  1 
ATOM   7451  C  CG  . TYR   B 2 800  ? 117.728 125.493 46.796  1.00 127.52 ? 800  TYR   A CG  1 
ATOM   7452  C  CD1 . TYR   B 2 800  ? 117.403 125.200 48.113  1.00 126.10 ? 800  TYR   A CD1 1 
ATOM   7453  C  CD2 . TYR   B 2 800  ? 118.760 126.395 46.562  1.00 128.30 ? 800  TYR   A CD2 1 
ATOM   7454  C  CE1 . TYR   B 2 800  ? 118.077 125.794 49.165  1.00 126.53 ? 800  TYR   A CE1 1 
ATOM   7455  C  CE2 . TYR   B 2 800  ? 119.438 126.994 47.607  1.00 129.11 ? 800  TYR   A CE2 1 
ATOM   7456  C  CZ  . TYR   B 2 800  ? 119.092 126.690 48.906  1.00 128.63 ? 800  TYR   A CZ  1 
ATOM   7457  O  OH  . TYR   B 2 800  ? 119.765 127.283 49.950  1.00 127.92 ? 800  TYR   A OH  1 
ATOM   7458  N  N   . HIS   B 2 801  ? 116.495 127.357 43.783  1.00 125.22 ? 801  HIS   A N   1 
ATOM   7459  C  CA  . HIS   B 2 801  ? 116.723 128.759 43.453  1.00 123.84 ? 801  HIS   A CA  1 
ATOM   7460  C  C   . HIS   B 2 801  ? 115.409 129.526 43.399  1.00 125.50 ? 801  HIS   A C   1 
ATOM   7461  O  O   . HIS   B 2 801  ? 115.330 130.669 43.863  1.00 124.42 ? 801  HIS   A O   1 
ATOM   7462  C  CB  . HIS   B 2 801  ? 117.469 128.871 42.125  1.00 123.71 ? 801  HIS   A CB  1 
ATOM   7463  C  CG  . HIS   B 2 801  ? 118.019 130.237 41.856  1.00 124.20 ? 801  HIS   A CG  1 
ATOM   7464  N  ND1 . HIS   B 2 801  ? 118.612 130.578 40.660  1.00 124.80 ? 801  HIS   A ND1 1 
ATOM   7465  C  CD2 . HIS   B 2 801  ? 118.072 131.345 42.631  1.00 124.54 ? 801  HIS   A CD2 1 
ATOM   7466  C  CE1 . HIS   B 2 801  ? 119.003 131.839 40.708  1.00 124.76 ? 801  HIS   A CE1 1 
ATOM   7467  N  NE2 . HIS   B 2 801  ? 118.687 132.327 41.893  1.00 125.33 ? 801  HIS   A NE2 1 
ATOM   7468  N  N   . ASN   B 2 802  ? 114.367 128.914 42.831  1.00 131.38 ? 802  ASN   A N   1 
ATOM   7469  C  CA  . ASN   B 2 802  ? 113.060 129.564 42.797  1.00 131.47 ? 802  ASN   A CA  1 
ATOM   7470  C  C   . ASN   B 2 802  ? 112.497 129.755 44.200  1.00 129.37 ? 802  ASN   A C   1 
ATOM   7471  O  O   . ASN   B 2 802  ? 111.954 130.819 44.520  1.00 129.45 ? 802  ASN   A O   1 
ATOM   7472  C  CB  . ASN   B 2 802  ? 112.090 128.756 41.936  1.00 131.14 ? 802  ASN   A CB  1 
ATOM   7473  C  CG  . ASN   B 2 802  ? 112.419 128.833 40.459  1.00 131.93 ? 802  ASN   A CG  1 
ATOM   7474  O  OD1 . ASN   B 2 802  ? 112.543 127.812 39.784  1.00 132.40 ? 802  ASN   A OD1 1 
ATOM   7475  N  ND2 . ASN   B 2 802  ? 112.563 130.051 39.948  1.00 131.04 ? 802  ASN   A ND2 1 
ATOM   7476  N  N   . ALA   B 2 803  ? 112.618 128.737 45.053  1.00 123.85 ? 803  ALA   A N   1 
ATOM   7477  C  CA  . ALA   B 2 803  ? 112.093 128.829 46.409  1.00 124.85 ? 803  ALA   A CA  1 
ATOM   7478  C  C   . ALA   B 2 803  ? 112.951 129.699 47.317  1.00 126.26 ? 803  ALA   A C   1 
ATOM   7479  O  O   . ALA   B 2 803  ? 112.519 130.014 48.431  1.00 125.67 ? 803  ALA   A O   1 
ATOM   7480  C  CB  . ALA   B 2 803  ? 111.952 127.433 47.016  1.00 125.02 ? 803  ALA   A CB  1 
ATOM   7481  N  N   . THR   B 2 804  ? 114.153 130.081 46.877  1.00 131.28 ? 804  THR   A N   1 
ATOM   7482  C  CA  . THR   B 2 804  ? 114.987 130.965 47.683  1.00 132.00 ? 804  THR   A CA  1 
ATOM   7483  C  C   . THR   B 2 804  ? 114.310 132.312 47.898  1.00 131.09 ? 804  THR   A C   1 
ATOM   7484  O  O   . THR   B 2 804  ? 114.324 132.853 49.010  1.00 130.52 ? 804  THR   A O   1 
ATOM   7485  C  CB  . THR   B 2 804  ? 116.352 131.150 47.018  1.00 132.22 ? 804  THR   A CB  1 
ATOM   7486  O  OG1 . THR   B 2 804  ? 116.971 129.871 46.832  1.00 132.30 ? 804  THR   A OG1 1 
ATOM   7487  C  CG2 . THR   B 2 804  ? 117.253 132.022 47.879  1.00 131.86 ? 804  THR   A CG2 1 
ATOM   7488  N  N   . VAL   B 2 805  ? 113.707 132.864 46.849  1.00 128.13 ? 805  VAL   A N   1 
ATOM   7489  C  CA  . VAL   B 2 805  ? 112.962 134.113 46.957  1.00 128.67 ? 805  VAL   A CA  1 
ATOM   7490  C  C   . VAL   B 2 805  ? 111.478 133.801 46.832  1.00 129.44 ? 805  VAL   A C   1 
ATOM   7491  O  O   . VAL   B 2 805  ? 110.932 133.751 45.724  1.00 129.06 ? 805  VAL   A O   1 
ATOM   7492  C  CB  . VAL   B 2 805  ? 113.412 135.128 45.891  1.00 128.44 ? 805  VAL   A CB  1 
ATOM   7493  C  CG1 . VAL   B 2 805  ? 112.720 136.467 46.106  1.00 127.73 ? 805  VAL   A CG1 1 
ATOM   7494  C  CG2 . VAL   B 2 805  ? 114.924 135.290 45.917  1.00 127.27 ? 805  VAL   A CG2 1 
ATOM   7495  N  N   . ALA   B 2 806  ? 110.815 133.587 47.969  1.00 130.91 ? 806  ALA   A N   1 
ATOM   7496  C  CA  . ALA   B 2 806  ? 109.404 133.235 47.982  1.00 131.10 ? 806  ALA   A CA  1 
ATOM   7497  C  C   . ALA   B 2 806  ? 108.560 134.147 48.859  1.00 128.84 ? 806  ALA   A C   1 
ATOM   7498  O  O   . ALA   B 2 806  ? 107.336 133.977 48.895  1.00 128.56 ? 806  ALA   A O   1 
ATOM   7499  C  CB  . ALA   B 2 806  ? 109.217 131.781 48.440  1.00 129.66 ? 806  ALA   A CB  1 
ATOM   7500  N  N   . LEU   B 2 807  ? 109.173 135.100 49.565  1.00 124.83 ? 807  LEU   A N   1 
ATOM   7501  C  CA  . LEU   B 2 807  ? 108.459 136.041 50.421  1.00 126.45 ? 807  LEU   A CA  1 
ATOM   7502  C  C   . LEU   B 2 807  ? 107.636 135.313 51.477  1.00 127.37 ? 807  LEU   A C   1 
ATOM   7503  O  O   . LEU   B 2 807  ? 108.158 134.944 52.534  1.00 126.86 ? 807  LEU   A O   1 
ATOM   7504  C  CB  . LEU   B 2 807  ? 107.561 136.965 49.590  1.00 127.38 ? 807  LEU   A CB  1 
ATOM   7505  C  CG  . LEU   B 2 807  ? 108.224 138.035 48.716  1.00 127.18 ? 807  LEU   A CG  1 
ATOM   7506  C  CD1 . LEU   B 2 807  ? 108.779 137.449 47.423  1.00 126.31 ? 807  LEU   A CD1 1 
ATOM   7507  C  CD2 . LEU   B 2 807  ? 107.247 139.163 48.419  1.00 126.77 ? 807  LEU   A CD2 1 
ATOM   7508  N  N   . GLN   B 2 808  ? 106.353 135.105 51.198  1.00 130.23 ? 808  GLN   A N   1 
ATOM   7509  C  CA  . GLN   B 2 808  ? 105.466 134.477 52.167  1.00 129.60 ? 808  GLN   A CA  1 
ATOM   7510  C  C   . GLN   B 2 808  ? 105.796 132.999 52.334  1.00 130.21 ? 808  GLN   A C   1 
ATOM   7511  O  O   . GLN   B 2 808  ? 106.000 132.276 51.354  1.00 128.65 ? 808  GLN   A O   1 
ATOM   7512  C  CB  . GLN   B 2 808  ? 104.010 134.642 51.734  1.00 127.51 ? 808  GLN   A CB  1 
ATOM   7513  C  CG  . GLN   B 2 808  ? 103.003 134.019 52.686  1.00 128.79 ? 808  GLN   A CG  1 
ATOM   7514  C  CD  . GLN   B 2 808  ? 101.573 134.178 52.208  1.00 129.20 ? 808  GLN   A CD  1 
ATOM   7515  O  OE1 . GLN   B 2 808  ? 101.320 134.761 51.154  1.00 129.12 ? 808  GLN   A OE1 1 
ATOM   7516  N  NE2 . GLN   B 2 808  ? 100.629 133.659 52.984  1.00 128.63 ? 808  GLN   A NE2 1 
ATOM   7517  N  N   . ASP   B 2 809  ? 105.842 132.555 53.592  1.00 133.06 ? 809  ASP   A N   1 
ATOM   7518  C  CA  . ASP   B 2 809  ? 106.053 131.149 53.943  1.00 131.79 ? 809  ASP   A CA  1 
ATOM   7519  C  C   . ASP   B 2 809  ? 107.337 130.599 53.320  1.00 130.44 ? 809  ASP   A C   1 
ATOM   7520  O  O   . ASP   B 2 809  ? 107.363 129.501 52.761  1.00 129.57 ? 809  ASP   A O   1 
ATOM   7521  C  CB  . ASP   B 2 809  ? 104.844 130.299 53.544  1.00 130.81 ? 809  ASP   A CB  1 
ATOM   7522  C  CG  . ASP   B 2 809  ? 103.575 130.721 54.258  1.00 131.29 ? 809  ASP   A CG  1 
ATOM   7523  O  OD1 . ASP   B 2 809  ? 103.633 131.675 55.062  1.00 132.28 ? 809  ASP   A OD1 1 
ATOM   7524  O  OD2 . ASP   B 2 809  ? 102.519 130.099 54.016  1.00 130.19 ? 809  ASP   A OD2 1 
ATOM   7525  N  N   . ARG   B 2 810  ? 108.415 131.379 53.427  1.00 125.53 ? 810  ARG   A N   1 
ATOM   7526  C  CA  . ARG   B 2 810  ? 109.703 130.933 52.903  1.00 124.17 ? 810  ARG   A CA  1 
ATOM   7527  C  C   . ARG   B 2 810  ? 110.180 129.676 53.618  1.00 123.80 ? 810  ARG   A C   1 
ATOM   7528  O  O   . ARG   B 2 810  ? 110.757 128.776 52.993  1.00 123.57 ? 810  ARG   A O   1 
ATOM   7529  C  CB  . ARG   B 2 810  ? 110.737 132.051 53.029  1.00 124.13 ? 810  ARG   A CB  1 
ATOM   7530  C  CG  . ARG   B 2 810  ? 112.093 131.712 52.435  1.00 124.53 ? 810  ARG   A CG  1 
ATOM   7531  C  CD  . ARG   B 2 810  ? 113.066 132.870 52.588  1.00 125.54 ? 810  ARG   A CD  1 
ATOM   7532  N  NE  . ARG   B 2 810  ? 114.372 132.566 52.014  1.00 125.89 ? 810  ARG   A NE  1 
ATOM   7533  C  CZ  . ARG   B 2 810  ? 115.400 133.403 52.006  1.00 125.39 ? 810  ARG   A CZ  1 
ATOM   7534  N  NH1 . ARG   B 2 810  ? 115.312 134.613 52.534  1.00 124.86 ? 810  ARG   A NH1 1 
ATOM   7535  N  NH2 . ARG   B 2 810  ? 116.547 133.017 51.453  1.00 124.69 ? 810  ARG   A NH2 1 
ATOM   7536  N  N   . GLU   B 2 811  ? 109.953 129.597 54.931  1.00 131.86 ? 811  GLU   A N   1 
ATOM   7537  C  CA  . GLU   B 2 811  ? 110.310 128.392 55.672  1.00 132.94 ? 811  GLU   A CA  1 
ATOM   7538  C  C   . GLU   B 2 811  ? 109.519 127.188 55.176  1.00 133.00 ? 811  GLU   A C   1 
ATOM   7539  O  O   . GLU   B 2 811  ? 110.066 126.088 55.045  1.00 132.87 ? 811  GLU   A O   1 
ATOM   7540  C  CB  . GLU   B 2 811  ? 110.094 128.606 57.173  1.00 132.53 ? 811  GLU   A CB  1 
ATOM   7541  C  CG  . GLU   B 2 811  ? 108.704 129.094 57.568  1.00 133.29 ? 811  GLU   A CG  1 
ATOM   7542  C  CD  . GLU   B 2 811  ? 108.543 130.597 57.431  1.00 133.69 ? 811  GLU   A CD  1 
ATOM   7543  O  OE1 . GLU   B 2 811  ? 109.540 131.278 57.109  1.00 133.41 ? 811  GLU   A OE1 1 
ATOM   7544  O  OE2 . GLU   B 2 811  ? 107.418 131.097 57.644  1.00 133.11 ? 811  GLU   A OE2 1 
ATOM   7545  N  N   . GLU   B 2 812  ? 108.230 127.376 54.885  1.00 127.64 ? 812  GLU   A N   1 
ATOM   7546  C  CA  . GLU   B 2 812  ? 107.436 126.283 54.333  1.00 126.31 ? 812  GLU   A CA  1 
ATOM   7547  C  C   . GLU   B 2 812  ? 107.965 125.855 52.970  1.00 126.28 ? 812  GLU   A C   1 
ATOM   7548  O  O   . GLU   B 2 812  ? 108.030 124.657 52.667  1.00 125.48 ? 812  GLU   A O   1 
ATOM   7549  C  CB  . GLU   B 2 812  ? 105.968 126.698 54.236  1.00 127.21 ? 812  GLU   A CB  1 
ATOM   7550  C  CG  . GLU   B 2 812  ? 105.045 125.614 53.701  1.00 128.21 ? 812  GLU   A CG  1 
ATOM   7551  C  CD  . GLU   B 2 812  ? 104.899 124.443 54.654  1.00 128.48 ? 812  GLU   A CD  1 
ATOM   7552  O  OE1 . GLU   B 2 812  ? 105.133 124.624 55.867  1.00 129.21 ? 812  GLU   A OE1 1 
ATOM   7553  O  OE2 . GLU   B 2 812  ? 104.549 123.338 54.188  1.00 128.46 ? 812  GLU   A OE2 1 
ATOM   7554  N  N   . ARG   B 2 813  ? 108.349 126.822 52.134  1.00 128.16 ? 813  ARG   A N   1 
ATOM   7555  C  CA  . ARG   B 2 813  ? 108.874 126.490 50.814  1.00 128.65 ? 813  ARG   A CA  1 
ATOM   7556  C  C   . ARG   B 2 813  ? 110.179 125.711 50.917  1.00 128.77 ? 813  ARG   A C   1 
ATOM   7557  O  O   . ARG   B 2 813  ? 110.377 124.722 50.201  1.00 130.10 ? 813  ARG   A O   1 
ATOM   7558  C  CB  . ARG   B 2 813  ? 109.072 127.762 49.989  1.00 128.80 ? 813  ARG   A CB  1 
ATOM   7559  C  CG  . ARG   B 2 813  ? 107.795 128.548 49.743  1.00 128.88 ? 813  ARG   A CG  1 
ATOM   7560  C  CD  . ARG   B 2 813  ? 106.730 127.687 49.083  1.00 129.36 ? 813  ARG   A CD  1 
ATOM   7561  N  NE  . ARG   B 2 813  ? 105.481 128.415 48.895  1.00 130.60 ? 813  ARG   A NE  1 
ATOM   7562  C  CZ  . ARG   B 2 813  ? 104.378 127.890 48.378  1.00 129.39 ? 813  ARG   A CZ  1 
ATOM   7563  N  NH1 . ARG   B 2 813  ? 104.333 126.627 47.985  1.00 128.89 ? 813  ARG   A NH1 1 
ATOM   7564  N  NH2 . ARG   B 2 813  ? 103.294 128.650 48.254  1.00 127.72 ? 813  ARG   A NH2 1 
ATOM   7565  N  N   . ILE   B 2 814  ? 111.081 126.134 51.806  1.00 123.35 ? 814  ILE   A N   1 
ATOM   7566  C  CA  . ILE   B 2 814  ? 112.343 125.413 51.931  1.00 122.83 ? 814  ILE   A CA  1 
ATOM   7567  C  C   . ILE   B 2 814  ? 112.121 124.047 52.569  1.00 122.98 ? 814  ILE   A C   1 
ATOM   7568  O  O   . ILE   B 2 814  ? 112.837 123.090 52.257  1.00 123.36 ? 814  ILE   A O   1 
ATOM   7569  C  CB  . ILE   B 2 814  ? 113.388 126.249 52.697  1.00 124.76 ? 814  ILE   A CB  1 
ATOM   7570  C  CG1 . ILE   B 2 814  ? 114.771 125.609 52.567  1.00 123.84 ? 814  ILE   A CG1 1 
ATOM   7571  C  CG2 . ILE   B 2 814  ? 113.020 126.394 54.160  1.00 123.71 ? 814  ILE   A CG2 1 
ATOM   7572  C  CD1 . ILE   B 2 814  ? 115.174 125.317 51.138  1.00 121.47 ? 814  ILE   A CD1 1 
ATOM   7573  N  N   . GLU   B 2 815  ? 111.125 123.917 53.451  1.00 124.21 ? 815  GLU   A N   1 
ATOM   7574  C  CA  . GLU   B 2 815  ? 110.794 122.603 53.995  1.00 126.22 ? 815  GLU   A CA  1 
ATOM   7575  C  C   . GLU   B 2 815  ? 110.287 121.671 52.901  1.00 126.76 ? 815  GLU   A C   1 
ATOM   7576  O  O   . GLU   B 2 815  ? 110.666 120.494 52.849  1.00 125.66 ? 815  GLU   A O   1 
ATOM   7577  C  CB  . GLU   B 2 815  ? 109.758 122.746 55.111  1.00 125.85 ? 815  GLU   A CB  1 
ATOM   7578  C  CG  . GLU   B 2 815  ? 109.398 121.446 55.817  1.00 126.56 ? 815  GLU   A CG  1 
ATOM   7579  C  CD  . GLU   B 2 815  ? 108.237 120.721 55.164  1.00 127.21 ? 815  GLU   A CD  1 
ATOM   7580  O  OE1 . GLU   B 2 815  ? 107.568 121.324 54.298  1.00 127.92 ? 815  GLU   A OE1 1 
ATOM   7581  O  OE2 . GLU   B 2 815  ? 107.993 119.547 55.516  1.00 126.82 ? 815  GLU   A OE2 1 
ATOM   7582  N  N   . SER   B 2 816  ? 109.427 122.182 52.018  1.00 123.33 ? 816  SER   A N   1 
ATOM   7583  C  CA  . SER   B 2 816  ? 108.954 121.377 50.895  1.00 122.27 ? 816  SER   A CA  1 
ATOM   7584  C  C   . SER   B 2 816  ? 110.104 120.994 49.973  1.00 121.77 ? 816  SER   A C   1 
ATOM   7585  O  O   . SER   B 2 816  ? 110.167 119.861 49.482  1.00 122.11 ? 816  SER   A O   1 
ATOM   7586  C  CB  . SER   B 2 816  ? 107.875 122.136 50.124  1.00 123.20 ? 816  SER   A CB  1 
ATOM   7587  O  OG  . SER   B 2 816  ? 108.376 123.362 49.620  1.00 124.44 ? 816  SER   A OG  1 
ATOM   7588  N  N   . VAL   B 2 817  ? 111.025 121.927 49.727  1.00 118.70 ? 817  VAL   A N   1 
ATOM   7589  C  CA  . VAL   B 2 817  ? 112.188 121.638 48.890  1.00 119.64 ? 817  VAL   A CA  1 
ATOM   7590  C  C   . VAL   B 2 817  ? 113.046 120.548 49.523  1.00 118.75 ? 817  VAL   A C   1 
ATOM   7591  O  O   . VAL   B 2 817  ? 113.513 119.624 48.840  1.00 118.67 ? 817  VAL   A O   1 
ATOM   7592  C  CB  . VAL   B 2 817  ? 112.988 122.931 48.646  1.00 121.37 ? 817  VAL   A CB  1 
ATOM   7593  C  CG1 . VAL   B 2 817  ? 114.387 122.620 48.151  1.00 121.07 ? 817  VAL   A CG1 1 
ATOM   7594  C  CG2 . VAL   B 2 817  ? 112.257 123.822 47.654  1.00 121.57 ? 817  VAL   A CG2 1 
ATOM   7595  N  N   . SER   B 2 818  ? 113.264 120.637 50.837  1.00 116.80 ? 818  SER   A N   1 
ATOM   7596  C  CA  . SER   B 2 818  ? 114.045 119.626 51.540  1.00 117.48 ? 818  SER   A CA  1 
ATOM   7597  C  C   . SER   B 2 818  ? 113.370 118.264 51.476  1.00 118.90 ? 818  SER   A C   1 
ATOM   7598  O  O   . SER   B 2 818  ? 114.037 117.240 51.294  1.00 120.39 ? 818  SER   A O   1 
ATOM   7599  C  CB  . SER   B 2 818  ? 114.258 120.049 52.993  1.00 118.49 ? 818  SER   A CB  1 
ATOM   7600  O  OG  . SER   B 2 818  ? 113.021 120.187 53.669  1.00 117.82 ? 818  SER   A OG  1 
ATOM   7601  N  N   . SER   B 2 819  ? 112.047 118.231 51.636  1.00 115.90 ? 819  SER   A N   1 
ATOM   7602  C  CA  . SER   B 2 819  ? 111.327 116.969 51.500  1.00 114.52 ? 819  SER   A CA  1 
ATOM   7603  C  C   . SER   B 2 819  ? 111.455 116.418 50.086  1.00 113.88 ? 819  SER   A C   1 
ATOM   7604  O  O   . SER   B 2 819  ? 111.568 115.202 49.892  1.00 111.38 ? 819  SER   A O   1 
ATOM   7605  C  CB  . SER   B 2 819  ? 109.857 117.160 51.873  1.00 115.65 ? 819  SER   A CB  1 
ATOM   7606  O  OG  . SER   B 2 819  ? 109.136 115.949 51.734  1.00 115.89 ? 819  SER   A OG  1 
ATOM   7607  N  N   . SER   B 2 820  ? 111.439 117.300 49.085  1.00 122.34 ? 820  SER   A N   1 
ATOM   7608  C  CA  . SER   B 2 820  ? 111.535 116.856 47.698  1.00 122.75 ? 820  SER   A CA  1 
ATOM   7609  C  C   . SER   B 2 820  ? 112.897 116.237 47.406  1.00 123.16 ? 820  SER   A C   1 
ATOM   7610  O  O   . SER   B 2 820  ? 112.981 115.160 46.805  1.00 123.44 ? 820  SER   A O   1 
ATOM   7611  C  CB  . SER   B 2 820  ? 111.261 118.026 46.753  1.00 122.18 ? 820  SER   A CB  1 
ATOM   7612  O  OG  . SER   B 2 820  ? 112.248 119.033 46.888  1.00 121.92 ? 820  SER   A OG  1 
ATOM   7613  N  N   . ILE   B 2 821  ? 113.979 116.903 47.819  1.00 116.83 ? 821  ILE   A N   1 
ATOM   7614  C  CA  . ILE   B 2 821  ? 115.307 116.353 47.553  1.00 113.03 ? 821  ILE   A CA  1 
ATOM   7615  C  C   . ILE   B 2 821  ? 115.536 115.092 48.374  1.00 112.46 ? 821  ILE   A C   1 
ATOM   7616  O  O   . ILE   B 2 821  ? 116.159 114.134 47.904  1.00 114.09 ? 821  ILE   A O   1 
ATOM   7617  C  CB  . ILE   B 2 821  ? 116.403 117.405 47.807  1.00 114.63 ? 821  ILE   A CB  1 
ATOM   7618  C  CG1 . ILE   B 2 821  ? 117.788 116.818 47.522  1.00 114.45 ? 821  ILE   A CG1 1 
ATOM   7619  C  CG2 . ILE   B 2 821  ? 116.330 117.949 49.223  1.00 115.76 ? 821  ILE   A CG2 1 
ATOM   7620  C  CD1 . ILE   B 2 821  ? 117.955 116.308 46.107  1.00 112.45 ? 821  ILE   A CD1 1 
ATOM   7621  N  N   . GLU   B 2 822  ? 115.034 115.066 49.608  1.00 109.76 ? 822  GLU   A N   1 
ATOM   7622  C  CA  . GLU   B 2 822  ? 115.152 113.889 50.465  1.00 112.01 ? 822  GLU   A CA  1 
ATOM   7623  C  C   . GLU   B 2 822  ? 113.947 112.989 50.208  1.00 114.26 ? 822  GLU   A C   1 
ATOM   7624  O  O   . GLU   B 2 822  ? 112.943 113.007 50.924  1.00 114.29 ? 822  GLU   A O   1 
ATOM   7625  C  CB  . GLU   B 2 822  ? 115.252 114.295 51.930  1.00 112.04 ? 822  GLU   A CB  1 
ATOM   7626  C  CG  . GLU   B 2 822  ? 116.370 115.281 52.234  1.00 112.58 ? 822  GLU   A CG  1 
ATOM   7627  C  CD  . GLU   B 2 822  ? 117.752 114.688 52.046  1.00 113.51 ? 822  GLU   A CD  1 
ATOM   7628  O  OE1 . GLU   B 2 822  ? 117.879 113.445 52.057  1.00 115.30 ? 822  GLU   A OE1 1 
ATOM   7629  O  OE2 . GLU   B 2 822  ? 118.715 115.467 51.887  1.00 112.44 ? 822  GLU   A OE2 1 
ATOM   7630  N  N   . ARG   B 2 823  ? 114.060 112.178 49.157  1.00 119.02 ? 823  ARG   A N   1 
ATOM   7631  C  CA  . ARG   B 2 823  ? 113.028 111.208 48.813  1.00 117.72 ? 823  ARG   A CA  1 
ATOM   7632  C  C   . ARG   B 2 823  ? 113.452 109.766 49.041  1.00 116.85 ? 823  ARG   A C   1 
ATOM   7633  O  O   . ARG   B 2 823  ? 112.596 108.927 49.326  1.00 116.81 ? 823  ARG   A O   1 
ATOM   7634  C  CB  . ARG   B 2 823  ? 112.593 111.380 47.349  1.00 117.63 ? 823  ARG   A CB  1 
ATOM   7635  C  CG  . ARG   B 2 823  ? 113.446 110.646 46.317  1.00 118.58 ? 823  ARG   A CG  1 
ATOM   7636  C  CD  . ARG   B 2 823  ? 114.532 111.529 45.713  1.00 118.10 ? 823  ARG   A CD  1 
ATOM   7637  N  NE  . ARG   B 2 823  ? 115.513 111.969 46.696  1.00 119.28 ? 823  ARG   A NE  1 
ATOM   7638  C  CZ  . ARG   B 2 823  ? 116.510 111.221 47.149  1.00 116.58 ? 823  ARG   A CZ  1 
ATOM   7639  N  NH1 . ARG   B 2 823  ? 116.683 109.977 46.735  1.00 114.49 ? 823  ARG   A NH1 1 
ATOM   7640  N  NH2 . ARG   B 2 823  ? 117.350 111.732 48.044  1.00 115.96 ? 823  ARG   A NH2 1 
ATOM   7641  N  N   . ASP   B 2 824  ? 114.747 109.466 48.947  1.00 111.65 ? 824  ASP   A N   1 
ATOM   7642  C  CA  . ASP   B 2 824  ? 115.266 108.117 49.166  1.00 112.37 ? 824  ASP   A CA  1 
ATOM   7643  C  C   . ASP   B 2 824  ? 116.737 108.233 49.527  1.00 110.91 ? 824  ASP   A C   1 
ATOM   7644  O  O   . ASP   B 2 824  ? 117.487 108.925 48.832  1.00 110.30 ? 824  ASP   A O   1 
ATOM   7645  C  CB  . ASP   B 2 824  ? 115.085 107.243 47.920  1.00 115.62 ? 824  ASP   A CB  1 
ATOM   7646  C  CG  . ASP   B 2 824  ? 113.692 106.653 47.811  1.00 116.05 ? 824  ASP   A CG  1 
ATOM   7647  O  OD1 . ASP   B 2 824  ? 113.127 106.257 48.853  1.00 114.78 ? 824  ASP   A OD1 1 
ATOM   7648  O  OD2 . ASP   B 2 824  ? 113.163 106.583 46.682  1.00 114.88 ? 824  ASP   A OD2 1 
ATOM   7649  N  N   . LEU   B 2 825  ? 117.150 107.565 50.601  1.00 111.38 ? 825  LEU   A N   1 
ATOM   7650  C  CA  . LEU   B 2 825  ? 118.541 107.560 51.028  1.00 112.79 ? 825  LEU   A CA  1 
ATOM   7651  C  C   . LEU   B 2 825  ? 118.975 106.136 51.338  1.00 111.45 ? 825  LEU   A C   1 
ATOM   7652  O  O   . LEU   B 2 825  ? 118.161 105.291 51.717  1.00 112.23 ? 825  LEU   A O   1 
ATOM   7653  C  CB  . LEU   B 2 825  ? 118.761 108.444 52.264  1.00 113.09 ? 825  LEU   A CB  1 
ATOM   7654  C  CG  . LEU   B 2 825  ? 118.472 109.940 52.141  1.00 114.64 ? 825  LEU   A CG  1 
ATOM   7655  C  CD1 . LEU   B 2 825  ? 118.573 110.615 53.500  1.00 112.46 ? 825  LEU   A CD1 1 
ATOM   7656  C  CD2 . LEU   B 2 825  ? 119.416 110.591 51.148  1.00 113.59 ? 825  LEU   A CD2 1 
ATOM   7657  N  N   . ILE   B 2 826  ? 120.270 105.877 51.170  1.00 106.21 ? 826  ILE   A N   1 
ATOM   7658  C  CA  . ILE   B 2 826  ? 120.875 104.594 51.505  1.00 104.14 ? 826  ILE   A CA  1 
ATOM   7659  C  C   . ILE   B 2 826  ? 121.677 104.768 52.786  1.00 106.76 ? 826  ILE   A C   1 
ATOM   7660  O  O   . ILE   B 2 826  ? 122.515 105.673 52.887  1.00 109.37 ? 826  ILE   A O   1 
ATOM   7661  C  CB  . ILE   B 2 826  ? 121.755 104.060 50.361  1.00 103.27 ? 826  ILE   A CB  1 
ATOM   7662  C  CG1 . ILE   B 2 826  ? 122.659 105.161 49.811  1.00 104.22 ? 826  ILE   A CG1 1 
ATOM   7663  C  CG2 . ILE   B 2 826  ? 120.891 103.476 49.254  1.00 106.42 ? 826  ILE   A CG2 1 
ATOM   7664  C  CD1 . ILE   B 2 826  ? 123.637 104.683 48.763  1.00 105.24 ? 826  ILE   A CD1 1 
ATOM   7665  N  N   . LEU   B 2 827  ? 121.411 103.910 53.767  1.00 103.57 ? 827  LEU   A N   1 
ATOM   7666  C  CA  . LEU   B 2 827  ? 122.036 104.027 55.076  1.00 101.31 ? 827  LEU   A CA  1 
ATOM   7667  C  C   . LEU   B 2 827  ? 123.512 103.659 55.013  1.00 100.24 ? 827  LEU   A C   1 
ATOM   7668  O  O   . LEU   B 2 827  ? 123.915 102.764 54.266  1.00 102.87 ? 827  LEU   A O   1 
ATOM   7669  C  CB  . LEU   B 2 827  ? 121.318 103.132 56.084  1.00 101.11 ? 827  LEU   A CB  1 
ATOM   7670  C  CG  . LEU   B 2 827  ? 121.778 103.214 57.539  1.00 101.00 ? 827  LEU   A CG  1 
ATOM   7671  C  CD1 . LEU   B 2 827  ? 121.608 104.625 58.074  1.00 100.65 ? 827  LEU   A CD1 1 
ATOM   7672  C  CD2 . LEU   B 2 827  ? 121.008 102.220 58.387  1.00 104.04 ? 827  LEU   A CD2 1 
ATOM   7673  N  N   . LEU   B 2 828  ? 124.318 104.363 55.804  1.00 82.99  ? 828  LEU   A N   1 
ATOM   7674  C  CA  . LEU   B 2 828  ? 125.741 104.083 55.925  1.00 82.67  ? 828  LEU   A CA  1 
ATOM   7675  C  C   . LEU   B 2 828  ? 126.157 103.615 57.309  1.00 90.94  ? 828  LEU   A C   1 
ATOM   7676  O  O   . LEU   B 2 828  ? 127.106 102.835 57.418  1.00 93.77  ? 828  LEU   A O   1 
ATOM   7677  C  CB  . LEU   B 2 828  ? 126.566 105.324 55.561  1.00 85.11  ? 828  LEU   A CB  1 
ATOM   7678  C  CG  . LEU   B 2 828  ? 126.500 105.752 54.099  1.00 86.46  ? 828  LEU   A CG  1 
ATOM   7679  C  CD1 . LEU   B 2 828  ? 127.500 106.860 53.830  1.00 90.07  ? 828  LEU   A CD1 1 
ATOM   7680  C  CD2 . LEU   B 2 828  ? 126.751 104.563 53.186  1.00 88.33  ? 828  LEU   A CD2 1 
ATOM   7681  N  N   . GLY   B 2 829  ? 125.484 104.062 58.358  1.00 96.63  ? 829  GLY   A N   1 
ATOM   7682  C  CA  . GLY   B 2 829  ? 125.851 103.665 59.708  1.00 96.30  ? 829  GLY   A CA  1 
ATOM   7683  C  C   . GLY   B 2 829  ? 125.358 104.687 60.718  1.00 93.44  ? 829  GLY   A C   1 
ATOM   7684  O  O   . GLY   B 2 829  ? 124.391 105.408 60.468  1.00 94.91  ? 829  GLY   A O   1 
ATOM   7685  N  N   . ALA   B 2 830  ? 126.045 104.728 61.857  1.00 83.63  ? 830  ALA   A N   1 
ATOM   7686  C  CA  . ALA   B 2 830  ? 125.684 105.646 62.927  1.00 81.57  ? 830  ALA   A CA  1 
ATOM   7687  C  C   . ALA   B 2 830  ? 126.905 105.907 63.795  1.00 82.39  ? 830  ALA   A C   1 
ATOM   7688  O  O   . ALA   B 2 830  ? 127.879 105.150 63.775  1.00 88.34  ? 830  ALA   A O   1 
ATOM   7689  C  CB  . ALA   B 2 830  ? 124.530 105.098 63.768  1.00 82.80  ? 830  ALA   A CB  1 
ATOM   7690  N  N   . THR   B 2 831  ? 126.838 106.995 64.555  1.00 76.71  ? 831  THR   A N   1 
ATOM   7691  C  CA  . THR   B 2 831  ? 127.893 107.408 65.468  1.00 76.40  ? 831  THR   A CA  1 
ATOM   7692  C  C   . THR   B 2 831  ? 127.400 107.324 66.907  1.00 80.64  ? 831  THR   A C   1 
ATOM   7693  O  O   . THR   B 2 831  ? 126.243 106.993 67.176  1.00 84.23  ? 831  THR   A O   1 
ATOM   7694  C  CB  . THR   B 2 831  ? 128.360 108.832 65.152  1.00 76.93  ? 831  THR   A CB  1 
ATOM   7695  O  OG1 . THR   B 2 831  ? 127.278 109.746 65.363  1.00 81.43  ? 831  THR   A OG1 1 
ATOM   7696  C  CG2 . THR   B 2 831  ? 128.822 108.931 63.710  1.00 78.24  ? 831  THR   A CG2 1 
ATOM   7697  N  N   . ALA   B 2 832  ? 128.302 107.626 67.842  1.00 75.85  ? 832  ALA   A N   1 
ATOM   7698  C  CA  . ALA   B 2 832  ? 127.973 107.577 69.266  1.00 70.51  ? 832  ALA   A CA  1 
ATOM   7699  C  C   . ALA   B 2 832  ? 128.943 108.493 70.008  1.00 69.38  ? 832  ALA   A C   1 
ATOM   7700  O  O   . ALA   B 2 832  ? 130.104 108.131 70.216  1.00 70.84  ? 832  ALA   A O   1 
ATOM   7701  C  CB  . ALA   B 2 832  ? 128.038 106.151 69.792  1.00 75.03  ? 832  ALA   A CB  1 
ATOM   7702  N  N   . ILE   B 2 833  ? 128.456 109.660 70.417  1.00 73.60  ? 833  ILE   A N   1 
ATOM   7703  C  CA  . ILE   B 2 833  ? 129.265 110.666 71.097  1.00 74.44  ? 833  ILE   A CA  1 
ATOM   7704  C  C   . ILE   B 2 833  ? 128.887 110.688 72.570  1.00 80.35  ? 833  ILE   A C   1 
ATOM   7705  O  O   . ILE   B 2 833  ? 127.700 110.647 72.919  1.00 87.57  ? 833  ILE   A O   1 
ATOM   7706  C  CB  . ILE   B 2 833  ? 129.076 112.056 70.463  1.00 76.33  ? 833  ILE   A CB  1 
ATOM   7707  C  CG1 . ILE   B 2 833  ? 129.197 111.976 68.944  1.00 79.34  ? 833  ILE   A CG1 1 
ATOM   7708  C  CG2 . ILE   B 2 833  ? 130.094 113.036 71.016  1.00 79.66  ? 833  ILE   A CG2 1 
ATOM   7709  C  CD1 . ILE   B 2 833  ? 128.964 113.297 68.251  1.00 78.08  ? 833  ILE   A CD1 1 
ATOM   7710  N  N   . GLU   B 2 834  ? 129.893 110.749 73.436  1.00 76.99  ? 834  GLU   A N   1 
ATOM   7711  C  CA  . GLU   B 2 834  ? 129.685 110.785 74.878  1.00 74.90  ? 834  GLU   A CA  1 
ATOM   7712  C  C   . GLU   B 2 834  ? 129.905 112.198 75.400  1.00 78.65  ? 834  GLU   A C   1 
ATOM   7713  O  O   . GLU   B 2 834  ? 130.948 112.806 75.139  1.00 82.13  ? 834  GLU   A O   1 
ATOM   7714  C  CB  . GLU   B 2 834  ? 130.629 109.816 75.590  1.00 77.33  ? 834  GLU   A CB  1 
ATOM   7715  C  CG  . GLU   B 2 834  ? 130.544 109.880 77.106  1.00 81.06  ? 834  GLU   A CG  1 
ATOM   7716  C  CD  . GLU   B 2 834  ? 131.531 108.953 77.787  1.00 83.27  ? 834  GLU   A CD  1 
ATOM   7717  O  OE1 . GLU   B 2 834  ? 132.292 108.264 77.077  1.00 83.33  ? 834  GLU   A OE1 1 
ATOM   7718  O  OE2 . GLU   B 2 834  ? 131.547 108.914 79.035  1.00 82.25  ? 834  GLU   A OE2 1 
ATOM   7719  N  N   . ASP   B 2 835  ? 128.922 112.715 76.134  1.00 72.50  ? 835  ASP   A N   1 
ATOM   7720  C  CA  . ASP   B 2 835  ? 129.058 113.993 76.831  1.00 70.92  ? 835  ASP   A CA  1 
ATOM   7721  C  C   . ASP   B 2 835  ? 129.648 113.695 78.202  1.00 67.83  ? 835  ASP   A C   1 
ATOM   7722  O  O   . ASP   B 2 835  ? 128.949 113.229 79.104  1.00 72.28  ? 835  ASP   A O   1 
ATOM   7723  C  CB  . ASP   B 2 835  ? 127.717 114.707 76.936  1.00 72.14  ? 835  ASP   A CB  1 
ATOM   7724  C  CG  . ASP   B 2 835  ? 127.837 116.076 77.578  1.00 78.70  ? 835  ASP   A CG  1 
ATOM   7725  O  OD1 . ASP   B 2 835  ? 128.478 116.963 76.976  1.00 80.91  ? 835  ASP   A OD1 1 
ATOM   7726  O  OD2 . ASP   B 2 835  ? 127.294 116.265 78.685  1.00 78.14  ? 835  ASP   A OD2 1 
ATOM   7727  N  N   . LYS   B 2 836  ? 130.940 113.966 78.359  1.00 54.23  ? 836  LYS   A N   1 
ATOM   7728  C  CA  . LYS   B 2 836  ? 131.671 113.489 79.524  1.00 54.58  ? 836  LYS   A CA  1 
ATOM   7729  C  C   . LYS   B 2 836  ? 131.263 114.270 80.765  1.00 59.04  ? 836  LYS   A C   1 
ATOM   7730  O  O   . LYS   B 2 836  ? 131.446 115.490 80.831  1.00 63.26  ? 836  LYS   A O   1 
ATOM   7731  C  CB  . LYS   B 2 836  ? 133.174 113.601 79.285  1.00 55.58  ? 836  LYS   A CB  1 
ATOM   7732  C  CG  . LYS   B 2 836  ? 134.020 113.038 80.410  1.00 62.38  ? 836  LYS   A CG  1 
ATOM   7733  C  CD  . LYS   B 2 836  ? 135.491 113.015 80.037  1.00 63.20  ? 836  LYS   A CD  1 
ATOM   7734  C  CE  . LYS   B 2 836  ? 135.745 112.093 78.856  1.00 63.98  ? 836  LYS   A CE  1 
ATOM   7735  N  NZ  . LYS   B 2 836  ? 135.332 110.691 79.143  1.00 66.71  ? 836  LYS   A NZ  1 
ATOM   7736  N  N   . LEU   B 2 837  ? 130.709 113.563 81.744  1.00 47.45  ? 837  LEU   A N   1 
ATOM   7737  C  CA  . LEU   B 2 837  ? 130.374 114.149 83.028  1.00 41.89  ? 837  LEU   A CA  1 
ATOM   7738  C  C   . LEU   B 2 837  ? 131.623 114.277 83.890  1.00 46.47  ? 837  LEU   A C   1 
ATOM   7739  O  O   . LEU   B 2 837  ? 132.669 113.685 83.608  1.00 53.28  ? 837  LEU   A O   1 
ATOM   7740  C  CB  . LEU   B 2 837  ? 129.337 113.295 83.753  1.00 31.78  ? 837  LEU   A CB  1 
ATOM   7741  C  CG  . LEU   B 2 837  ? 128.158 112.781 82.935  1.00 39.26  ? 837  LEU   A CG  1 
ATOM   7742  C  CD1 . LEU   B 2 837  ? 127.446 111.685 83.696  1.00 47.33  ? 837  LEU   A CD1 1 
ATOM   7743  C  CD2 . LEU   B 2 837  ? 127.202 113.907 82.605  1.00 47.22  ? 837  LEU   A CD2 1 
ATOM   7744  N  N   . GLN   B 2 838  ? 131.508 115.068 84.951  1.00 42.17  ? 838  GLN   A N   1 
ATOM   7745  C  CA  . GLN   B 2 838  ? 132.583 115.137 85.927  1.00 39.66  ? 838  GLN   A CA  1 
ATOM   7746  C  C   . GLN   B 2 838  ? 132.713 113.801 86.645  1.00 47.15  ? 838  GLN   A C   1 
ATOM   7747  O  O   . GLN   B 2 838  ? 131.735 113.073 86.833  1.00 56.63  ? 838  GLN   A O   1 
ATOM   7748  C  CB  . GLN   B 2 838  ? 132.331 116.260 86.930  1.00 49.70  ? 838  GLN   A CB  1 
ATOM   7749  C  CG  . GLN   B 2 838  ? 132.486 117.652 86.347  1.00 50.77  ? 838  GLN   A CG  1 
ATOM   7750  C  CD  . GLN   B 2 838  ? 132.347 118.738 87.389  1.00 48.97  ? 838  GLN   A CD  1 
ATOM   7751  O  OE1 . GLN   B 2 838  ? 132.102 118.460 88.561  1.00 54.38  ? 838  GLN   A OE1 1 
ATOM   7752  N  NE2 . GLN   B 2 838  ? 132.501 119.984 86.967  1.00 48.95  ? 838  GLN   A NE2 1 
ATOM   7753  N  N   . ASP   B 2 839  ? 133.942 113.470 87.027  1.00 49.44  ? 839  ASP   A N   1 
ATOM   7754  C  CA  . ASP   B 2 839  ? 134.204 112.184 87.652  1.00 50.49  ? 839  ASP   A CA  1 
ATOM   7755  C  C   . ASP   B 2 839  ? 133.441 112.058 88.963  1.00 52.88  ? 839  ASP   A C   1 
ATOM   7756  O  O   . ASP   B 2 839  ? 133.441 112.976 89.789  1.00 60.57  ? 839  ASP   A O   1 
ATOM   7757  C  CB  . ASP   B 2 839  ? 135.703 112.012 87.888  1.00 57.95  ? 839  ASP   A CB  1 
ATOM   7758  C  CG  . ASP   B 2 839  ? 136.504 112.063 86.602  1.00 65.65  ? 839  ASP   A CG  1 
ATOM   7759  O  OD1 . ASP   B 2 839  ? 135.973 111.646 85.551  1.00 64.44  ? 839  ASP   A OD1 1 
ATOM   7760  O  OD2 . ASP   B 2 839  ? 137.666 112.519 86.641  1.00 67.36  ? 839  ASP   A OD2 1 
ATOM   7761  N  N   . GLY   B 2 840  ? 132.787 110.916 89.150  1.00 49.82  ? 840  GLY   A N   1 
ATOM   7762  C  CA  . GLY   B 2 840  ? 132.077 110.626 90.374  1.00 49.43  ? 840  GLY   A CA  1 
ATOM   7763  C  C   . GLY   B 2 840  ? 130.671 111.172 90.463  1.00 50.50  ? 840  GLY   A C   1 
ATOM   7764  O  O   . GLY   B 2 840  ? 130.030 111.000 91.506  1.00 63.70  ? 840  GLY   A O   1 
ATOM   7765  N  N   . VAL   B 2 841  ? 130.167 111.821 89.413  1.00 41.83  ? 841  VAL   A N   1 
ATOM   7766  C  CA  . VAL   B 2 841  ? 128.817 112.383 89.468  1.00 40.65  ? 841  VAL   A CA  1 
ATOM   7767  C  C   . VAL   B 2 841  ? 127.744 111.315 89.656  1.00 52.62  ? 841  VAL   A C   1 
ATOM   7768  O  O   . VAL   B 2 841  ? 126.877 111.492 90.528  1.00 57.54  ? 841  VAL   A O   1 
ATOM   7769  C  CB  . VAL   B 2 841  ? 128.562 113.270 88.237  1.00 42.22  ? 841  VAL   A CB  1 
ATOM   7770  C  CG1 . VAL   B 2 841  ? 127.079 113.533 88.075  1.00 50.75  ? 841  VAL   A CG1 1 
ATOM   7771  C  CG2 . VAL   B 2 841  ? 129.312 114.575 88.376  1.00 43.17  ? 841  VAL   A CG2 1 
ATOM   7772  N  N   . PRO   B 2 842  ? 127.718 110.215 88.888  1.00 45.78  ? 842  PRO   A N   1 
ATOM   7773  C  CA  . PRO   B 2 842  ? 126.664 109.212 89.129  1.00 45.29  ? 842  PRO   A CA  1 
ATOM   7774  C  C   . PRO   B 2 842  ? 126.724 108.591 90.515  1.00 51.27  ? 842  PRO   A C   1 
ATOM   7775  O  O   . PRO   B 2 842  ? 125.680 108.412 91.155  1.00 57.02  ? 842  PRO   A O   1 
ATOM   7776  C  CB  . PRO   B 2 842  ? 126.910 108.176 88.024  1.00 44.78  ? 842  PRO   A CB  1 
ATOM   7777  C  CG  . PRO   B 2 842  ? 128.317 108.381 87.609  1.00 46.45  ? 842  PRO   A CG  1 
ATOM   7778  C  CD  . PRO   B 2 842  ? 128.555 109.844 87.735  1.00 40.80  ? 842  PRO   A CD  1 
ATOM   7779  N  N   . ASP   B 2 843  ? 127.924 108.276 91.005  1.00 54.56  ? 843  ASP   A N   1 
ATOM   7780  C  CA  . ASP   B 2 843  ? 128.053 107.726 92.350  1.00 50.59  ? 843  ASP   A CA  1 
ATOM   7781  C  C   . ASP   B 2 843  ? 127.621 108.741 93.399  1.00 53.11  ? 843  ASP   A C   1 
ATOM   7782  O  O   . ASP   B 2 843  ? 126.957 108.389 94.381  1.00 61.38  ? 843  ASP   A O   1 
ATOM   7783  C  CB  . ASP   B 2 843  ? 129.492 107.280 92.596  1.00 52.96  ? 843  ASP   A CB  1 
ATOM   7784  C  CG  . ASP   B 2 843  ? 129.997 106.328 91.531  1.00 64.11  ? 843  ASP   A CG  1 
ATOM   7785  O  OD1 . ASP   B 2 843  ? 129.180 105.562 90.978  1.00 66.40  ? 843  ASP   A OD1 1 
ATOM   7786  O  OD2 . ASP   B 2 843  ? 131.212 106.347 91.244  1.00 60.84  ? 843  ASP   A OD2 1 
ATOM   7787  N  N   . THR   B 2 844  ? 127.994 110.007 93.206  1.00 39.33  ? 844  THR   A N   1 
ATOM   7788  C  CA  . THR   B 2 844  ? 127.589 111.056 94.134  1.00 39.12  ? 844  THR   A CA  1 
ATOM   7789  C  C   . THR   B 2 844  ? 126.075 111.202 94.178  1.00 47.13  ? 844  THR   A C   1 
ATOM   7790  O  O   . THR   B 2 844  ? 125.489 111.341 95.257  1.00 54.28  ? 844  THR   A O   1 
ATOM   7791  C  CB  . THR   B 2 844  ? 128.241 112.378 93.736  1.00 44.42  ? 844  THR   A CB  1 
ATOM   7792  O  OG1 . THR   B 2 844  ? 129.643 112.319 94.017  1.00 50.24  ? 844  THR   A OG1 1 
ATOM   7793  C  CG2 . THR   B 2 844  ? 127.620 113.535 94.487  1.00 45.12  ? 844  THR   A CG2 1 
ATOM   7794  N  N   . ILE   B 2 845  ? 125.423 111.171 93.016  1.00 42.94  ? 845  ILE   A N   1 
ATOM   7795  C  CA  . ILE   B 2 845  ? 123.972 111.311 92.978  1.00 41.18  ? 845  ILE   A CA  1 
ATOM   7796  C  C   . ILE   B 2 845  ? 123.300 110.098 93.608  1.00 46.59  ? 845  ILE   A C   1 
ATOM   7797  O  O   . ILE   B 2 845  ? 122.292 110.228 94.314  1.00 54.31  ? 845  ILE   A O   1 
ATOM   7798  C  CB  . ILE   B 2 845  ? 123.500 111.555 91.534  1.00 37.74  ? 845  ILE   A CB  1 
ATOM   7799  C  CG1 . ILE   B 2 845  ? 123.911 112.957 91.084  1.00 37.85  ? 845  ILE   A CG1 1 
ATOM   7800  C  CG2 . ILE   B 2 845  ? 122.000 111.385 91.421  1.00 45.93  ? 845  ILE   A CG2 1 
ATOM   7801  C  CD1 . ILE   B 2 845  ? 123.512 113.296 89.677  1.00 46.19  ? 845  ILE   A CD1 1 
ATOM   7802  N  N   . SER   B 2 846  ? 123.851 108.903 93.382  1.00 41.04  ? 846  SER   A N   1 
ATOM   7803  C  CA  . SER   B 2 846  ? 123.315 107.714 94.038  1.00 34.71  ? 846  SER   A CA  1 
ATOM   7804  C  C   . SER   B 2 846  ? 123.426 107.825 95.553  1.00 39.34  ? 846  SER   A C   1 
ATOM   7805  O  O   . SER   B 2 846  ? 122.476 107.507 96.279  1.00 48.86  ? 846  SER   A O   1 
ATOM   7806  C  CB  . SER   B 2 846  ? 124.040 106.468 93.538  1.00 42.54  ? 846  SER   A CB  1 
ATOM   7807  O  OG  . SER   B 2 846  ? 123.525 105.300 94.151  1.00 51.83  ? 846  SER   A OG  1 
ATOM   7808  N  N   . ASP   B 2 847  ? 124.575 108.290 96.046  1.00 45.21  ? 847  ASP   A N   1 
ATOM   7809  C  CA  . ASP   B 2 847  ? 124.758 108.447 97.485  1.00 36.62  ? 847  ASP   A CA  1 
ATOM   7810  C  C   . ASP   B 2 847  ? 123.826 109.509 98.054  1.00 43.83  ? 847  ASP   A C   1 
ATOM   7811  O  O   . ASP   B 2 847  ? 123.283 109.341 99.152  1.00 53.88  ? 847  ASP   A O   1 
ATOM   7812  C  CB  . ASP   B 2 847  ? 126.214 108.788 97.791  1.00 41.67  ? 847  ASP   A CB  1 
ATOM   7813  C  CG  . ASP   B 2 847  ? 127.169 107.687 97.374  1.00 57.34  ? 847  ASP   A CG  1 
ATOM   7814  O  OD1 . ASP   B 2 847  ? 126.780 106.502 97.443  1.00 60.19  ? 847  ASP   A OD1 1 
ATOM   7815  O  OD2 . ASP   B 2 847  ? 128.308 108.006 96.973  1.00 56.82  ? 847  ASP   A OD2 1 
ATOM   7816  N  N   . LEU   B 2 848  ? 123.632 110.611 97.328  1.00 40.56  ? 848  LEU   A N   1 
ATOM   7817  C  CA  . LEU   B 2 848  ? 122.722 111.655 97.788  1.00 31.26  ? 848  LEU   A CA  1 
ATOM   7818  C  C   . LEU   B 2 848  ? 121.285 111.153 97.843  1.00 32.20  ? 848  LEU   A C   1 
ATOM   7819  O  O   . LEU   B 2 848  ? 120.551 111.461 98.788  1.00 47.07  ? 848  LEU   A O   1 
ATOM   7820  C  CB  . LEU   B 2 848  ? 122.827 112.884 96.887  1.00 37.64  ? 848  LEU   A CB  1 
ATOM   7821  C  CG  . LEU   B 2 848  ? 124.118 113.699 96.952  1.00 38.43  ? 848  LEU   A CG  1 
ATOM   7822  C  CD1 . LEU   B 2 848  ? 124.052 114.877 96.002  1.00 42.24  ? 848  LEU   A CD1 1 
ATOM   7823  C  CD2 . LEU   B 2 848  ? 124.387 114.172 98.365  1.00 42.94  ? 848  LEU   A CD2 1 
ATOM   7824  N  N   . LYS   B 2 849  ? 120.861 110.383 96.838  1.00 31.33  ? 849  LYS   A N   1 
ATOM   7825  C  CA  . LYS   B 2 849  ? 119.514 109.826 96.863  1.00 31.10  ? 849  LYS   A CA  1 
ATOM   7826  C  C   . LYS   B 2 849  ? 119.356 108.792 97.969  1.00 38.10  ? 849  LYS   A C   1 
ATOM   7827  O  O   . LYS   B 2 849  ? 118.268 108.660 98.539  1.00 44.01  ? 849  LYS   A O   1 
ATOM   7828  C  CB  . LYS   B 2 849  ? 119.163 109.216 95.507  1.00 36.52  ? 849  LYS   A CB  1 
ATOM   7829  C  CG  . LYS   B 2 849  ? 119.039 110.232 94.384  1.00 45.14  ? 849  LYS   A CG  1 
ATOM   7830  C  CD  . LYS   B 2 849  ? 118.218 109.691 93.223  1.00 45.91  ? 849  LYS   A CD  1 
ATOM   7831  C  CE  . LYS   B 2 849  ? 118.807 108.406 92.665  1.00 43.18  ? 849  LYS   A CE  1 
ATOM   7832  N  NZ  . LYS   B 2 849  ? 120.173 108.612 92.111  1.00 39.39  ? 849  LYS   A NZ  1 
ATOM   7833  N  N   . ARG   B 2 850  ? 120.420 108.048 98.280  1.00 43.04  ? 850  ARG   A N   1 
ATOM   7834  C  CA  . ARG   B 2 850  ? 120.374 107.146 99.426  1.00 32.64  ? 850  ARG   A CA  1 
ATOM   7835  C  C   . ARG   B 2 850  ? 120.210 107.921 100.725 1.00 36.16  ? 850  ARG   A C   1 
ATOM   7836  O  O   . ARG   B 2 850  ? 119.505 107.478 101.638 1.00 43.12  ? 850  ARG   A O   1 
ATOM   7837  C  CB  . ARG   B 2 850  ? 121.635 106.284 99.472  1.00 35.63  ? 850  ARG   A CB  1 
ATOM   7838  C  CG  . ARG   B 2 850  ? 121.705 105.217 98.398  1.00 39.13  ? 850  ARG   A CG  1 
ATOM   7839  C  CD  . ARG   B 2 850  ? 123.073 104.567 98.369  1.00 39.37  ? 850  ARG   A CD  1 
ATOM   7840  N  NE  . ARG   B 2 850  ? 123.413 103.962 99.649  1.00 43.33  ? 850  ARG   A NE  1 
ATOM   7841  C  CZ  . ARG   B 2 850  ? 124.593 103.431 99.935  1.00 43.90  ? 850  ARG   A CZ  1 
ATOM   7842  N  NH1 . ARG   B 2 850  ? 125.578 103.422 99.053  1.00 39.77  ? 850  ARG   A NH1 1 
ATOM   7843  N  NH2 . ARG   B 2 850  ? 124.789 102.896 101.135 1.00 42.58  ? 850  ARG   A NH2 1 
ATOM   7844  N  N   . ALA   B 2 851  ? 120.854 109.085 100.826 1.00 35.66  ? 851  ALA   A N   1 
ATOM   7845  C  CA  . ALA   B 2 851  ? 120.753 109.918 102.016 1.00 33.07  ? 851  ALA   A CA  1 
ATOM   7846  C  C   . ALA   B 2 851  ? 119.382 110.556 102.180 1.00 42.88  ? 851  ALA   A C   1 
ATOM   7847  O  O   . ALA   B 2 851  ? 119.112 111.135 103.237 1.00 49.50  ? 851  ALA   A O   1 
ATOM   7848  C  CB  . ALA   B 2 851  ? 121.824 111.007 101.984 1.00 29.99  ? 851  ALA   A CB  1 
ATOM   7849  N  N   . GLY   B 2 852  ? 118.518 110.472 101.174 1.00 46.00  ? 852  GLY   A N   1 
ATOM   7850  C  CA  . GLY   B 2 852  ? 117.196 111.050 101.254 1.00 37.21  ? 852  GLY   A CA  1 
ATOM   7851  C  C   . GLY   B 2 852  ? 117.071 112.446 100.696 1.00 47.21  ? 852  GLY   A C   1 
ATOM   7852  O  O   . GLY   B 2 852  ? 116.051 113.101 100.937 1.00 55.31  ? 852  GLY   A O   1 
ATOM   7853  N  N   . ILE   B 2 853  ? 118.070 112.926 99.967  1.00 34.13  ? 853  ILE   A N   1 
ATOM   7854  C  CA  . ILE   B 2 853  ? 118.045 114.266 99.399  1.00 25.27  ? 853  ILE   A CA  1 
ATOM   7855  C  C   . ILE   B 2 853  ? 117.489 114.187 97.986  1.00 42.90  ? 853  ILE   A C   1 
ATOM   7856  O  O   . ILE   B 2 853  ? 117.957 113.388 97.166  1.00 51.99  ? 853  ILE   A O   1 
ATOM   7857  C  CB  . ILE   B 2 853  ? 119.447 114.892 99.407  1.00 28.76  ? 853  ILE   A CB  1 
ATOM   7858  C  CG1 . ILE   B 2 853  ? 120.042 114.831 100.812 1.00 38.49  ? 853  ILE   A CG1 1 
ATOM   7859  C  CG2 . ILE   B 2 853  ? 119.381 116.326 98.933  1.00 41.15  ? 853  ILE   A CG2 1 
ATOM   7860  C  CD1 . ILE   B 2 853  ? 121.481 115.251 100.884 1.00 38.07  ? 853  ILE   A CD1 1 
ATOM   7861  N  N   . LYS   B 2 854  ? 116.489 115.016 97.699  1.00 40.65  ? 854  LYS   A N   1 
ATOM   7862  C  CA  . LYS   B 2 854  ? 115.858 115.047 96.386  1.00 37.24  ? 854  LYS   A CA  1 
ATOM   7863  C  C   . LYS   B 2 854  ? 116.626 116.024 95.505  1.00 43.33  ? 854  LYS   A C   1 
ATOM   7864  O  O   . LYS   B 2 854  ? 116.684 117.221 95.798  1.00 47.15  ? 854  LYS   A O   1 
ATOM   7865  C  CB  . LYS   B 2 854  ? 114.389 115.437 96.508  1.00 38.41  ? 854  LYS   A CB  1 
ATOM   7866  C  CG  . LYS   B 2 854  ? 113.610 114.575 97.484  1.00 44.20  ? 854  LYS   A CG  1 
ATOM   7867  C  CD  . LYS   B 2 854  ? 112.118 114.831 97.386  1.00 51.06  ? 854  LYS   A CD  1 
ATOM   7868  C  CE  . LYS   B 2 854  ? 111.589 114.480 96.005  1.00 51.02  ? 854  LYS   A CE  1 
ATOM   7869  N  NZ  . LYS   B 2 854  ? 111.827 113.049 95.669  1.00 50.02  ? 854  LYS   A NZ  1 
ATOM   7870  N  N   . VAL   B 2 855  ? 117.213 115.514 94.428  1.00 40.41  ? 855  VAL   A N   1 
ATOM   7871  C  CA  . VAL   B 2 855  ? 118.077 116.295 93.554  1.00 35.81  ? 855  VAL   A CA  1 
ATOM   7872  C  C   . VAL   B 2 855  ? 117.287 116.694 92.317  1.00 46.52  ? 855  VAL   A C   1 
ATOM   7873  O  O   . VAL   B 2 855  ? 116.734 115.837 91.618  1.00 51.33  ? 855  VAL   A O   1 
ATOM   7874  C  CB  . VAL   B 2 855  ? 119.341 115.511 93.172  1.00 36.61  ? 855  VAL   A CB  1 
ATOM   7875  C  CG1 . VAL   B 2 855  ? 120.237 116.353 92.284  1.00 45.38  ? 855  VAL   A CG1 1 
ATOM   7876  C  CG2 . VAL   B 2 855  ? 120.085 115.072 94.417  1.00 45.00  ? 855  VAL   A CG2 1 
ATOM   7877  N  N   . TRP   B 2 856  ? 117.233 117.994 92.047  1.00 43.49  ? 856  TRP   A N   1 
ATOM   7878  C  CA  . TRP   B 2 856  ? 116.612 118.536 90.850  1.00 29.65  ? 856  TRP   A CA  1 
ATOM   7879  C  C   . TRP   B 2 856  ? 117.679 119.119 89.935  1.00 39.64  ? 856  TRP   A C   1 
ATOM   7880  O  O   . TRP   B 2 856  ? 118.792 119.436 90.363  1.00 54.76  ? 856  TRP   A O   1 
ATOM   7881  C  CB  . TRP   B 2 856  ? 115.590 119.624 91.189  1.00 37.41  ? 856  TRP   A CB  1 
ATOM   7882  C  CG  . TRP   B 2 856  ? 114.393 119.160 91.955  1.00 44.37  ? 856  TRP   A CG  1 
ATOM   7883  C  CD1 . TRP   B 2 856  ? 114.248 117.985 92.630  1.00 50.33  ? 856  TRP   A CD1 1 
ATOM   7884  C  CD2 . TRP   B 2 856  ? 113.163 119.871 92.122  1.00 41.30  ? 856  TRP   A CD2 1 
ATOM   7885  N  NE1 . TRP   B 2 856  ? 113.006 117.922 93.210  1.00 49.01  ? 856  TRP   A NE1 1 
ATOM   7886  C  CE2 . TRP   B 2 856  ? 112.321 119.069 92.911  1.00 42.75  ? 856  TRP   A CE2 1 
ATOM   7887  C  CE3 . TRP   B 2 856  ? 112.694 121.110 91.680  1.00 44.92  ? 856  TRP   A CE3 1 
ATOM   7888  C  CZ2 . TRP   B 2 856  ? 111.037 119.466 93.268  1.00 42.96  ? 856  TRP   A CZ2 1 
ATOM   7889  C  CZ3 . TRP   B 2 856  ? 111.421 121.500 92.035  1.00 44.64  ? 856  TRP   A CZ3 1 
ATOM   7890  C  CH2 . TRP   B 2 856  ? 110.608 120.683 92.821  1.00 43.74  ? 856  TRP   A CH2 1 
ATOM   7891  N  N   . VAL   B 2 857  ? 117.326 119.259 88.662  1.00 35.69  ? 857  VAL   A N   1 
ATOM   7892  C  CA  . VAL   B 2 857  ? 118.191 119.878 87.666  1.00 30.02  ? 857  VAL   A CA  1 
ATOM   7893  C  C   . VAL   B 2 857  ? 117.461 121.081 87.094  1.00 37.72  ? 857  VAL   A C   1 
ATOM   7894  O  O   . VAL   B 2 857  ? 116.344 120.951 86.580  1.00 50.85  ? 857  VAL   A O   1 
ATOM   7895  C  CB  . VAL   B 2 857  ? 118.585 118.898 86.552  1.00 32.91  ? 857  VAL   A CB  1 
ATOM   7896  C  CG1 . VAL   B 2 857  ? 119.417 119.604 85.505  1.00 37.53  ? 857  VAL   A CG1 1 
ATOM   7897  C  CG2 . VAL   B 2 857  ? 119.351 117.734 87.128  1.00 42.16  ? 857  VAL   A CG2 1 
ATOM   7898  N  N   . ALA   B 2 858  ? 118.091 122.247 87.183  1.00 43.34  ? 858  ALA   A N   1 
ATOM   7899  C  CA  . ALA   B 2 858  ? 117.572 123.484 86.610  1.00 43.36  ? 858  ALA   A CA  1 
ATOM   7900  C  C   . ALA   B 2 858  ? 118.635 124.004 85.653  1.00 42.51  ? 858  ALA   A C   1 
ATOM   7901  O  O   . ALA   B 2 858  ? 119.660 124.537 86.086  1.00 51.67  ? 858  ALA   A O   1 
ATOM   7902  C  CB  . ALA   B 2 858  ? 117.240 124.501 87.696  1.00 46.03  ? 858  ALA   A CB  1 
ATOM   7903  N  N   . THR   B 2 859  ? 118.401 123.841 84.355  1.00 45.71  ? 859  THR   A N   1 
ATOM   7904  C  CA  . THR   B 2 859  ? 119.385 124.178 83.339  1.00 48.64  ? 859  THR   A CA  1 
ATOM   7905  C  C   . THR   B 2 859  ? 118.748 125.003 82.232  1.00 48.91  ? 859  THR   A C   1 
ATOM   7906  O  O   . THR   B 2 859  ? 117.553 124.869 81.949  1.00 58.76  ? 859  THR   A O   1 
ATOM   7907  C  CB  . THR   B 2 859  ? 120.018 122.917 82.745  1.00 50.26  ? 859  THR   A CB  1 
ATOM   7908  O  OG1 . THR   B 2 859  ? 120.943 123.285 81.715  1.00 56.87  ? 859  THR   A OG1 1 
ATOM   7909  C  CG2 . THR   B 2 859  ? 118.953 122.007 82.159  1.00 47.52  ? 859  THR   A CG2 1 
ATOM   7910  N  N   . GLY   B 2 860  ? 119.553 125.860 81.614  1.00 48.39  ? 860  GLY   A N   1 
ATOM   7911  C  CA  . GLY   B 2 860  ? 119.135 126.626 80.463  1.00 49.41  ? 860  GLY   A CA  1 
ATOM   7912  C  C   . GLY   B 2 860  ? 119.272 125.921 79.137  1.00 57.29  ? 860  GLY   A C   1 
ATOM   7913  O  O   . GLY   B 2 860  ? 118.926 126.496 78.102  1.00 59.67  ? 860  GLY   A O   1 
ATOM   7914  N  N   . ASP   B 2 861  ? 119.774 124.689 79.133  1.00 58.50  ? 861  ASP   A N   1 
ATOM   7915  C  CA  . ASP   B 2 861  ? 119.943 123.927 77.907  1.00 54.37  ? 861  ASP   A CA  1 
ATOM   7916  C  C   . ASP   B 2 861  ? 118.612 123.304 77.492  1.00 61.15  ? 861  ASP   A C   1 
ATOM   7917  O  O   . ASP   B 2 861  ? 117.614 123.358 78.215  1.00 67.80  ? 861  ASP   A O   1 
ATOM   7918  C  CB  . ASP   B 2 861  ? 121.023 122.866 78.094  1.00 58.27  ? 861  ASP   A CB  1 
ATOM   7919  C  CG  . ASP   B 2 861  ? 121.716 122.506 76.798  1.00 64.67  ? 861  ASP   A CG  1 
ATOM   7920  O  OD1 . ASP   B 2 861  ? 121.100 122.669 75.725  1.00 70.53  ? 861  ASP   A OD1 1 
ATOM   7921  O  OD2 . ASP   B 2 861  ? 122.880 122.059 76.853  1.00 64.55  ? 861  ASP   A OD2 1 
ATOM   7922  N  N   . LYS   B 2 862  ? 118.597 122.695 76.310  1.00 62.91  ? 862  LYS   A N   1 
ATOM   7923  C  CA  . LYS   B 2 862  ? 117.371 122.166 75.734  1.00 60.14  ? 862  LYS   A CA  1 
ATOM   7924  C  C   . LYS   B 2 862  ? 116.928 120.902 76.467  1.00 62.43  ? 862  LYS   A C   1 
ATOM   7925  O  O   . LYS   B 2 862  ? 117.648 120.339 77.296  1.00 73.83  ? 862  LYS   A O   1 
ATOM   7926  C  CB  . LYS   B 2 862  ? 117.558 121.910 74.241  1.00 64.71  ? 862  LYS   A CB  1 
ATOM   7927  C  CG  . LYS   B 2 862  ? 118.849 121.200 73.882  1.00 67.33  ? 862  LYS   A CG  1 
ATOM   7928  C  CD  . LYS   B 2 862  ? 118.991 121.054 72.375  1.00 69.06  ? 862  LYS   A CD  1 
ATOM   7929  C  CE  . LYS   B 2 862  ? 120.369 120.540 71.998  1.00 70.10  ? 862  LYS   A CE  1 
ATOM   7930  N  NZ  . LYS   B 2 862  ? 121.439 121.478 72.437  1.00 68.84  ? 862  LYS   A NZ  1 
ATOM   7931  N  N   . LEU   B 2 863  ? 115.708 120.458 76.156  1.00 57.83  ? 863  LEU   A N   1 
ATOM   7932  C  CA  . LEU   B 2 863  ? 115.110 119.328 76.861  1.00 57.59  ? 863  LEU   A CA  1 
ATOM   7933  C  C   . LEU   B 2 863  ? 115.850 118.026 76.577  1.00 61.81  ? 863  LEU   A C   1 
ATOM   7934  O  O   . LEU   B 2 863  ? 116.048 117.211 77.487  1.00 65.75  ? 863  LEU   A O   1 
ATOM   7935  C  CB  . LEU   B 2 863  ? 113.635 119.208 76.477  1.00 58.07  ? 863  LEU   A CB  1 
ATOM   7936  C  CG  . LEU   B 2 863  ? 112.778 118.130 77.139  1.00 65.07  ? 863  LEU   A CG  1 
ATOM   7937  C  CD1 . LEU   B 2 863  ? 111.395 118.677 77.432  1.00 62.62  ? 863  LEU   A CD1 1 
ATOM   7938  C  CD2 . LEU   B 2 863  ? 112.677 116.899 76.253  1.00 64.72  ? 863  LEU   A CD2 1 
ATOM   7939  N  N   . GLU   B 2 864  ? 116.254 117.805 75.324  1.00 56.27  ? 864  GLU   A N   1 
ATOM   7940  C  CA  . GLU   B 2 864  ? 116.880 116.538 74.957  1.00 53.46  ? 864  GLU   A CA  1 
ATOM   7941  C  C   . GLU   B 2 864  ? 118.194 116.332 75.702  1.00 58.06  ? 864  GLU   A C   1 
ATOM   7942  O  O   . GLU   B 2 864  ? 118.448 115.254 76.254  1.00 66.41  ? 864  GLU   A O   1 
ATOM   7943  C  CB  . GLU   B 2 864  ? 117.107 116.480 73.446  1.00 58.62  ? 864  GLU   A CB  1 
ATOM   7944  C  CG  . GLU   B 2 864  ? 115.837 116.502 72.611  1.00 68.92  ? 864  GLU   A CG  1 
ATOM   7945  C  CD  . GLU   B 2 864  ? 115.337 117.908 72.339  1.00 70.22  ? 864  GLU   A CD  1 
ATOM   7946  O  OE1 . GLU   B 2 864  ? 116.025 118.872 72.734  1.00 69.84  ? 864  GLU   A OE1 1 
ATOM   7947  O  OE2 . GLU   B 2 864  ? 114.257 118.048 71.727  1.00 67.62  ? 864  GLU   A OE2 1 
ATOM   7948  N  N   . THR   B 2 865  ? 119.042 117.361 75.731  1.00 47.90  ? 865  THR   A N   1 
ATOM   7949  C  CA  . THR   B 2 865  ? 120.311 117.246 76.439  1.00 46.90  ? 865  THR   A CA  1 
ATOM   7950  C  C   . THR   B 2 865  ? 120.089 117.013 77.927  1.00 50.07  ? 865  THR   A C   1 
ATOM   7951  O  O   . THR   B 2 865  ? 120.774 116.188 78.545  1.00 59.19  ? 865  THR   A O   1 
ATOM   7952  C  CB  . THR   B 2 865  ? 121.154 118.499 76.212  1.00 52.78  ? 865  THR   A CB  1 
ATOM   7953  O  OG1 . THR   B 2 865  ? 121.339 118.702 74.807  1.00 59.42  ? 865  THR   A OG1 1 
ATOM   7954  C  CG2 . THR   B 2 865  ? 122.511 118.356 76.879  1.00 51.28  ? 865  THR   A CG2 1 
ATOM   7955  N  N   . ALA   B 2 866  ? 119.129 117.727 78.515  1.00 41.68  ? 866  ALA   A N   1 
ATOM   7956  C  CA  . ALA   B 2 866  ? 118.865 117.589 79.942  1.00 38.82  ? 866  ALA   A CA  1 
ATOM   7957  C  C   . ALA   B 2 866  ? 118.395 116.182 80.285  1.00 42.35  ? 866  ALA   A C   1 
ATOM   7958  O  O   . ALA   B 2 866  ? 118.860 115.582 81.260  1.00 47.46  ? 866  ALA   A O   1 
ATOM   7959  C  CB  . ALA   B 2 866  ? 117.834 118.626 80.385  1.00 48.66  ? 866  ALA   A CB  1 
ATOM   7960  N  N   . VAL   B 2 867  ? 117.473 115.633 79.489  1.00 45.18  ? 867  VAL   A N   1 
ATOM   7961  C  CA  . VAL   B 2 867  ? 116.960 114.300 79.788  1.00 37.43  ? 867  VAL   A CA  1 
ATOM   7962  C  C   . VAL   B 2 867  ? 118.036 113.244 79.550  1.00 40.21  ? 867  VAL   A C   1 
ATOM   7963  O  O   . VAL   B 2 867  ? 118.140 112.266 80.304  1.00 46.68  ? 867  VAL   A O   1 
ATOM   7964  C  CB  . VAL   B 2 867  ? 115.672 114.018 78.990  1.00 35.91  ? 867  VAL   A CB  1 
ATOM   7965  C  CG1 . VAL   B 2 867  ? 115.936 113.958 77.495  1.00 46.13  ? 867  VAL   A CG1 1 
ATOM   7966  C  CG2 . VAL   B 2 867  ? 115.030 112.734 79.469  1.00 43.28  ? 867  VAL   A CG2 1 
ATOM   7967  N  N   . ALA   B 2 868  ? 118.871 113.429 78.522  1.00 39.98  ? 868  ALA   A N   1 
ATOM   7968  C  CA  . ALA   B 2 868  ? 119.969 112.493 78.301  1.00 35.20  ? 868  ALA   A CA  1 
ATOM   7969  C  C   . ALA   B 2 868  ? 120.945 112.501 79.470  1.00 37.02  ? 868  ALA   A C   1 
ATOM   7970  O  O   . ALA   B 2 868  ? 121.381 111.439 79.934  1.00 44.13  ? 868  ALA   A O   1 
ATOM   7971  C  CB  . ALA   B 2 868  ? 120.690 112.829 76.997  1.00 36.85  ? 868  ALA   A CB  1 
ATOM   7972  N  N   . ILE   B 2 869  ? 121.294 113.689 79.967  1.00 35.48  ? 869  ILE   A N   1 
ATOM   7973  C  CA  . ILE   B 2 869  ? 122.208 113.774 81.102  1.00 30.69  ? 869  ILE   A CA  1 
ATOM   7974  C  C   . ILE   B 2 869  ? 121.574 113.160 82.342  1.00 42.55  ? 869  ILE   A C   1 
ATOM   7975  O  O   . ILE   B 2 869  ? 122.236 112.446 83.105  1.00 52.82  ? 869  ILE   A O   1 
ATOM   7976  C  CB  . ILE   B 2 869  ? 122.638 115.232 81.340  1.00 33.71  ? 869  ILE   A CB  1 
ATOM   7977  C  CG1 . ILE   B 2 869  ? 123.521 115.708 80.191  1.00 41.94  ? 869  ILE   A CG1 1 
ATOM   7978  C  CG2 . ILE   B 2 869  ? 123.380 115.364 82.657  1.00 44.14  ? 869  ILE   A CG2 1 
ATOM   7979  C  CD1 . ILE   B 2 869  ? 124.721 114.829 79.953  1.00 45.03  ? 869  ILE   A CD1 1 
ATOM   7980  N  N   . GLY   B 2 870  ? 120.284 113.418 82.560  1.00 49.87  ? 870  GLY   A N   1 
ATOM   7981  C  CA  . GLY   B 2 870  ? 119.600 112.804 83.685  1.00 49.06  ? 870  GLY   A CA  1 
ATOM   7982  C  C   . GLY   B 2 870  ? 119.627 111.290 83.622  1.00 50.48  ? 870  GLY   A C   1 
ATOM   7983  O  O   . GLY   B 2 870  ? 119.758 110.618 84.648  1.00 55.37  ? 870  GLY   A O   1 
ATOM   7984  N  N   . TYR   B 2 871  ? 119.497 110.732 82.417  1.00 44.05  ? 871  TYR   A N   1 
ATOM   7985  C  CA  . TYR   B 2 871  ? 119.645 109.289 82.260  1.00 32.66  ? 871  TYR   A CA  1 
ATOM   7986  C  C   . TYR   B 2 871  ? 121.065 108.838 82.573  1.00 39.55  ? 871  TYR   A C   1 
ATOM   7987  O  O   . TYR   B 2 871  ? 121.263 107.809 83.229  1.00 49.43  ? 871  TYR   A O   1 
ATOM   7988  C  CB  . TYR   B 2 871  ? 119.251 108.868 80.847  1.00 38.62  ? 871  TYR   A CB  1 
ATOM   7989  C  CG  . TYR   B 2 871  ? 117.767 108.689 80.649  1.00 37.87  ? 871  TYR   A CG  1 
ATOM   7990  C  CD1 . TYR   B 2 871  ? 117.024 107.905 81.513  1.00 40.87  ? 871  TYR   A CD1 1 
ATOM   7991  C  CD2 . TYR   B 2 871  ? 117.109 109.309 79.598  1.00 43.56  ? 871  TYR   A CD2 1 
ATOM   7992  C  CE1 . TYR   B 2 871  ? 115.670 107.737 81.337  1.00 45.34  ? 871  TYR   A CE1 1 
ATOM   7993  C  CE2 . TYR   B 2 871  ? 115.755 109.148 79.415  1.00 44.69  ? 871  TYR   A CE2 1 
ATOM   7994  C  CZ  . TYR   B 2 871  ? 115.040 108.362 80.288  1.00 46.93  ? 871  TYR   A CZ  1 
ATOM   7995  O  OH  . TYR   B 2 871  ? 113.688 108.195 80.111  1.00 50.30  ? 871  TYR   A OH  1 
ATOM   7996  N  N   . THR   B 2 872  ? 122.069 109.589 82.116  1.00 34.10  ? 872  THR   A N   1 
ATOM   7997  C  CA  . THR   B 2 872  ? 123.453 109.173 82.317  1.00 31.31  ? 872  THR   A CA  1 
ATOM   7998  C  C   . THR   B 2 872  ? 123.955 109.406 83.737  1.00 40.95  ? 872  THR   A C   1 
ATOM   7999  O  O   . THR   B 2 872  ? 124.949 108.790 84.132  1.00 48.31  ? 872  THR   A O   1 
ATOM   8000  C  CB  . THR   B 2 872  ? 124.376 109.896 81.334  1.00 32.36  ? 872  THR   A CB  1 
ATOM   8001  O  OG1 . THR   B 2 872  ? 124.231 111.311 81.490  1.00 47.05  ? 872  THR   A OG1 1 
ATOM   8002  C  CG2 . THR   B 2 872  ? 124.039 109.509 79.906  1.00 42.11  ? 872  THR   A CG2 1 
ATOM   8003  N  N   . THR   B 2 873  ? 123.301 110.272 84.508  1.00 44.60  ? 873  THR   A N   1 
ATOM   8004  C  CA  . THR   B 2 873  ? 123.723 110.590 85.867  1.00 40.62  ? 873  THR   A CA  1 
ATOM   8005  C  C   . THR   B 2 873  ? 122.992 109.773 86.923  1.00 43.80  ? 873  THR   A C   1 
ATOM   8006  O  O   . THR   B 2 873  ? 123.150 110.049 88.116  1.00 54.46  ? 873  THR   A O   1 
ATOM   8007  C  CB  . THR   B 2 873  ? 123.523 112.081 86.154  1.00 42.67  ? 873  THR   A CB  1 
ATOM   8008  O  OG1 . THR   B 2 873  ? 122.175 112.454 85.845  1.00 49.09  ? 873  THR   A OG1 1 
ATOM   8009  C  CG2 . THR   B 2 873  ? 124.481 112.923 85.335  1.00 45.26  ? 873  THR   A CG2 1 
ATOM   8010  N  N   . ASN   B 2 874  ? 122.189 108.794 86.511  1.00 44.73  ? 874  ASN   A N   1 
ATOM   8011  C  CA  . ASN   B 2 874  ? 121.346 107.969 87.372  1.00 46.42  ? 874  ASN   A CA  1 
ATOM   8012  C  C   . ASN   B 2 874  ? 120.260 108.768 88.079  1.00 52.61  ? 874  ASN   A C   1 
ATOM   8013  O  O   . ASN   B 2 874  ? 119.562 108.221 88.941  1.00 60.20  ? 874  ASN   A O   1 
ATOM   8014  C  CB  . ASN   B 2 874  ? 122.164 107.190 88.409  1.00 52.09  ? 874  ASN   A CB  1 
ATOM   8015  C  CG  . ASN   B 2 874  ? 122.886 106.003 87.808  1.00 57.11  ? 874  ASN   A CG  1 
ATOM   8016  O  OD1 . ASN   B 2 874  ? 122.432 105.421 86.823  1.00 55.15  ? 874  ASN   A OD1 1 
ATOM   8017  N  ND2 . ASN   B 2 874  ? 124.015 105.635 88.400  1.00 57.86  ? 874  ASN   A ND2 1 
ATOM   8018  N  N   . LEU   B 2 875  ? 120.099 110.051 87.746  1.00 50.52  ? 875  LEU   A N   1 
ATOM   8019  C  CA  . LEU   B 2 875  ? 118.956 110.804 88.249  1.00 46.85  ? 875  LEU   A CA  1 
ATOM   8020  C  C   . LEU   B 2 875  ? 117.653 110.221 87.725  1.00 52.58  ? 875  LEU   A C   1 
ATOM   8021  O  O   . LEU   B 2 875  ? 116.670 110.105 88.465  1.00 60.34  ? 875  LEU   A O   1 
ATOM   8022  C  CB  . LEU   B 2 875  ? 119.080 112.273 87.854  1.00 42.69  ? 875  LEU   A CB  1 
ATOM   8023  C  CG  . LEU   B 2 875  ? 119.964 113.139 88.745  1.00 51.60  ? 875  LEU   A CG  1 
ATOM   8024  C  CD1 . LEU   B 2 875  ? 120.340 114.416 88.033  1.00 55.44  ? 875  LEU   A CD1 1 
ATOM   8025  C  CD2 . LEU   B 2 875  ? 119.245 113.447 90.041  1.00 55.19  ? 875  LEU   A CD2 1 
ATOM   8026  N  N   . LEU   B 2 876  ? 117.632 109.848 86.454  1.00 49.53  ? 876  LEU   A N   1 
ATOM   8027  C  CA  . LEU   B 2 876  ? 116.475 109.235 85.813  1.00 44.30  ? 876  LEU   A CA  1 
ATOM   8028  C  C   . LEU   B 2 876  ? 116.845 107.785 85.526  1.00 51.58  ? 876  LEU   A C   1 
ATOM   8029  O  O   . LEU   B 2 876  ? 117.508 107.491 84.528  1.00 63.51  ? 876  LEU   A O   1 
ATOM   8030  C  CB  . LEU   B 2 876  ? 116.094 109.979 84.536  1.00 45.30  ? 876  LEU   A CB  1 
ATOM   8031  C  CG  . LEU   B 2 876  ? 115.260 111.259 84.600  1.00 40.76  ? 876  LEU   A CG  1 
ATOM   8032  C  CD1 . LEU   B 2 876  ? 115.884 112.295 85.512  1.00 50.45  ? 876  LEU   A CD1 1 
ATOM   8033  C  CD2 . LEU   B 2 876  ? 115.094 111.828 83.208  1.00 44.46  ? 876  LEU   A CD2 1 
ATOM   8034  N  N   . THR   B 2 877  ? 116.427 106.882 86.405  1.00 57.23  ? 877  THR   A N   1 
ATOM   8035  C  CA  . THR   B 2 877  ? 116.721 105.474 86.205  1.00 60.87  ? 877  THR   A CA  1 
ATOM   8036  C  C   . THR   B 2 877  ? 115.869 104.911 85.071  1.00 66.09  ? 877  THR   A C   1 
ATOM   8037  O  O   . THR   B 2 877  ? 114.896 105.523 84.623  1.00 71.31  ? 877  THR   A O   1 
ATOM   8038  C  CB  . THR   B 2 877  ? 116.479 104.685 87.490  1.00 63.78  ? 877  THR   A CB  1 
ATOM   8039  O  OG1 . THR   B 2 877  ? 115.131 104.885 87.931  1.00 64.07  ? 877  THR   A OG1 1 
ATOM   8040  C  CG2 . THR   B 2 877  ? 117.436 105.141 88.581  1.00 64.84  ? 877  THR   A CG2 1 
ATOM   8041  N  N   . LYS   B 2 878  ? 116.251 103.722 84.605  1.00 69.54  ? 878  LYS   A N   1 
ATOM   8042  C  CA  . LYS   B 2 878  ? 115.540 103.080 83.508  1.00 68.75  ? 878  LYS   A CA  1 
ATOM   8043  C  C   . LYS   B 2 878  ? 114.124 102.667 83.882  1.00 73.17  ? 878  LYS   A C   1 
ATOM   8044  O  O   . LYS   B 2 878  ? 113.338 102.336 82.989  1.00 78.48  ? 878  LYS   A O   1 
ATOM   8045  C  CB  . LYS   B 2 878  ? 116.319 101.857 83.023  1.00 72.88  ? 878  LYS   A CB  1 
ATOM   8046  C  CG  . LYS   B 2 878  ? 117.763 102.148 82.647  1.00 76.03  ? 878  LYS   A CG  1 
ATOM   8047  C  CD  . LYS   B 2 878  ? 117.850 103.169 81.526  1.00 77.68  ? 878  LYS   A CD  1 
ATOM   8048  C  CE  . LYS   B 2 878  ? 119.296 103.460 81.158  1.00 75.16  ? 878  LYS   A CE  1 
ATOM   8049  N  NZ  . LYS   B 2 878  ? 119.402 104.475 80.074  1.00 75.12  ? 878  LYS   A NZ  1 
ATOM   8050  N  N   . ASP   B 2 879  ? 113.782 102.675 85.170  1.00 75.44  ? 879  ASP   A N   1 
ATOM   8051  C  CA  . ASP   B 2 879  ? 112.464 102.275 85.643  1.00 75.49  ? 879  ASP   A CA  1 
ATOM   8052  C  C   . ASP   B 2 879  ? 111.605 103.472 86.041  1.00 79.90  ? 879  ASP   A C   1 
ATOM   8053  O  O   . ASP   B 2 879  ? 110.798 103.378 86.972  1.00 83.53  ? 879  ASP   A O   1 
ATOM   8054  C  CB  . ASP   B 2 879  ? 112.607 101.303 86.816  1.00 80.35  ? 879  ASP   A CB  1 
ATOM   8055  C  CG  . ASP   B 2 879  ? 111.365 100.462 87.036  1.00 84.22  ? 879  ASP   A CG  1 
ATOM   8056  O  OD1 . ASP   B 2 879  ? 110.394 100.620 86.268  1.00 86.83  ? 879  ASP   A OD1 1 
ATOM   8057  O  OD2 . ASP   B 2 879  ? 111.360 99.641  87.977  1.00 81.40  ? 879  ASP   A OD2 1 
ATOM   8058  N  N   . THR   B 2 880  ? 111.763 104.602 85.356  1.00 69.18  ? 880  THR   A N   1 
ATOM   8059  C  CA  . THR   B 2 880  ? 111.002 105.809 85.647  1.00 65.12  ? 880  THR   A CA  1 
ATOM   8060  C  C   . THR   B 2 880  ? 110.172 106.202 84.438  1.00 64.38  ? 880  THR   A C   1 
ATOM   8061  O  O   . THR   B 2 880  ? 110.597 106.019 83.293  1.00 71.46  ? 880  THR   A O   1 
ATOM   8062  C  CB  . THR   B 2 880  ? 111.913 106.975 86.038  1.00 62.49  ? 880  THR   A CB  1 
ATOM   8063  O  OG1 . THR   B 2 880  ? 112.911 107.165 85.029  1.00 63.73  ? 880  THR   A OG1 1 
ATOM   8064  C  CG2 . THR   B 2 880  ? 112.582 106.706 87.371  1.00 67.85  ? 880  THR   A CG2 1 
ATOM   8065  N  N   . ASN   B 2 881  ? 108.988 106.742 84.700  1.00 62.74  ? 881  ASN   A N   1 
ATOM   8066  C  CA  . ASN   B 2 881  ? 108.098 107.228 83.659  1.00 64.55  ? 881  ASN   A CA  1 
ATOM   8067  C  C   . ASN   B 2 881  ? 108.167 108.747 83.620  1.00 68.84  ? 881  ASN   A C   1 
ATOM   8068  O  O   . ASN   B 2 881  ? 107.967 109.408 84.645  1.00 71.21  ? 881  ASN   A O   1 
ATOM   8069  C  CB  . ASN   B 2 881  ? 106.664 106.764 83.907  1.00 66.53  ? 881  ASN   A CB  1 
ATOM   8070  C  CG  . ASN   B 2 881  ? 106.564 105.266 84.095  1.00 68.12  ? 881  ASN   A CG  1 
ATOM   8071  O  OD1 . ASN   B 2 881  ? 106.665 104.764 85.211  1.00 70.52  ? 881  ASN   A OD1 1 
ATOM   8072  N  ND2 . ASN   B 2 881  ? 106.363 104.544 83.000  1.00 69.45  ? 881  ASN   A ND2 1 
ATOM   8073  N  N   . LEU   B 2 882  ? 108.444 109.294 82.443  1.00 63.79  ? 882  LEU   A N   1 
ATOM   8074  C  CA  . LEU   B 2 882  ? 108.667 110.724 82.289  1.00 57.90  ? 882  LEU   A CA  1 
ATOM   8075  C  C   . LEU   B 2 882  ? 107.347 111.434 82.028  1.00 62.25  ? 882  LEU   A C   1 
ATOM   8076  O  O   . LEU   B 2 882  ? 106.584 111.038 81.141  1.00 71.47  ? 882  LEU   A O   1 
ATOM   8077  C  CB  . LEU   B 2 882  ? 109.649 110.995 81.153  1.00 58.04  ? 882  LEU   A CB  1 
ATOM   8078  C  CG  . LEU   B 2 882  ? 111.106 110.667 81.449  1.00 57.33  ? 882  LEU   A CG  1 
ATOM   8079  C  CD1 . LEU   B 2 882  ? 111.971 110.978 80.245  1.00 61.64  ? 882  LEU   A CD1 1 
ATOM   8080  C  CD2 . LEU   B 2 882  ? 111.562 111.452 82.656  1.00 63.64  ? 882  LEU   A CD2 1 
ATOM   8081  N  N   . ILE   B 2 883  ? 107.082 112.479 82.802  1.00 49.10  ? 883  ILE   A N   1 
ATOM   8082  C  CA  . ILE   B 2 883  ? 105.972 113.388 82.557  1.00 45.46  ? 883  ILE   A CA  1 
ATOM   8083  C  C   . ILE   B 2 883  ? 106.580 114.649 81.958  1.00 56.80  ? 883  ILE   A C   1 
ATOM   8084  O  O   . ILE   B 2 883  ? 107.161 115.472 82.670  1.00 65.27  ? 883  ILE   A O   1 
ATOM   8085  C  CB  . ILE   B 2 883  ? 105.188 113.687 83.836  1.00 49.12  ? 883  ILE   A CB  1 
ATOM   8086  C  CG1 . ILE   B 2 883  ? 104.717 112.391 84.490  1.00 50.47  ? 883  ILE   A CG1 1 
ATOM   8087  C  CG2 . ILE   B 2 883  ? 104.003 114.584 83.533  1.00 58.27  ? 883  ILE   A CG2 1 
ATOM   8088  C  CD1 . ILE   B 2 883  ? 104.059 112.602 85.827  1.00 56.36  ? 883  ILE   A CD1 1 
ATOM   8089  N  N   . VAL   B 2 884  ? 106.453 114.808 80.645  1.00 51.18  ? 884  VAL   A N   1 
ATOM   8090  C  CA  . VAL   B 2 884  ? 107.039 115.936 79.932  1.00 46.93  ? 884  VAL   A CA  1 
ATOM   8091  C  C   . VAL   B 2 884  ? 105.971 117.005 79.767  1.00 56.01  ? 884  VAL   A C   1 
ATOM   8092  O  O   . VAL   B 2 884  ? 104.969 116.793 79.075  1.00 66.04  ? 884  VAL   A O   1 
ATOM   8093  C  CB  . VAL   B 2 884  ? 107.610 115.507 78.573  1.00 50.98  ? 884  VAL   A CB  1 
ATOM   8094  C  CG1 . VAL   B 2 884  ? 108.198 116.703 77.850  1.00 56.01  ? 884  VAL   A CG1 1 
ATOM   8095  C  CG2 . VAL   B 2 884  ? 108.660 114.431 78.761  1.00 55.21  ? 884  VAL   A CG2 1 
ATOM   8096  N  N   . VAL   B 2 885  ? 106.187 118.155 80.397  1.00 53.14  ? 885  VAL   A N   1 
ATOM   8097  C  CA  . VAL   B 2 885  ? 105.264 119.282 80.341  1.00 47.27  ? 885  VAL   A CA  1 
ATOM   8098  C  C   . VAL   B 2 885  ? 105.940 120.399 79.561  1.00 57.88  ? 885  VAL   A C   1 
ATOM   8099  O  O   . VAL   B 2 885  ? 107.002 120.889 79.964  1.00 67.24  ? 885  VAL   A O   1 
ATOM   8100  C  CB  . VAL   B 2 885  ? 104.861 119.761 81.743  1.00 52.29  ? 885  VAL   A CB  1 
ATOM   8101  C  CG1 . VAL   B 2 885  ? 103.998 121.004 81.648  1.00 63.15  ? 885  VAL   A CG1 1 
ATOM   8102  C  CG2 . VAL   B 2 885  ? 104.128 118.663 82.485  1.00 57.08  ? 885  VAL   A CG2 1 
ATOM   8103  N  N   . ARG   B 2 886  ? 105.329 120.797 78.450  1.00 74.56  ? 886  ARG   A N   1 
ATOM   8104  C  CA  . ARG   B 2 886  ? 105.849 121.889 77.642  1.00 76.24  ? 886  ARG   A CA  1 
ATOM   8105  C  C   . ARG   B 2 886  ? 104.679 122.645 77.036  1.00 79.26  ? 886  ARG   A C   1 
ATOM   8106  O  O   . ARG   B 2 886  ? 103.581 122.105 76.880  1.00 81.33  ? 886  ARG   A O   1 
ATOM   8107  C  CB  . ARG   B 2 886  ? 106.794 121.385 76.545  1.00 73.17  ? 886  ARG   A CB  1 
ATOM   8108  C  CG  . ARG   B 2 886  ? 106.137 120.482 75.521  1.00 78.02  ? 886  ARG   A CG  1 
ATOM   8109  C  CD  . ARG   B 2 886  ? 107.000 120.345 74.278  1.00 80.88  ? 886  ARG   A CD  1 
ATOM   8110  N  NE  . ARG   B 2 886  ? 108.266 119.676 74.552  1.00 82.96  ? 886  ARG   A NE  1 
ATOM   8111  C  CZ  . ARG   B 2 886  ? 108.493 118.388 74.335  1.00 83.06  ? 886  ARG   A CZ  1 
ATOM   8112  N  NH1 . ARG   B 2 886  ? 107.558 117.595 73.838  1.00 80.50  ? 886  ARG   A NH1 1 
ATOM   8113  N  NH2 . ARG   B 2 886  ? 109.690 117.883 74.620  1.00 79.79  ? 886  ARG   A NH2 1 
ATOM   8114  N  N   . GLU   B 2 887  ? 104.924 123.908 76.700  1.00 80.53  ? 887  GLU   A N   1 
ATOM   8115  C  CA  . GLU   B 2 887  ? 103.879 124.738 76.118  1.00 79.70  ? 887  GLU   A CA  1 
ATOM   8116  C  C   . GLU   B 2 887  ? 103.499 124.213 74.740  1.00 82.01  ? 887  GLU   A C   1 
ATOM   8117  O  O   . GLU   B 2 887  ? 104.368 123.889 73.925  1.00 82.48  ? 887  GLU   A O   1 
ATOM   8118  C  CB  . GLU   B 2 887  ? 104.338 126.191 76.025  1.00 79.03  ? 887  GLU   A CB  1 
ATOM   8119  C  CG  . GLU   B 2 887  ? 103.335 127.113 75.350  1.00 83.55  ? 887  GLU   A CG  1 
ATOM   8120  C  CD  . GLU   B 2 887  ? 103.698 128.578 75.489  1.00 84.58  ? 887  GLU   A CD  1 
ATOM   8121  O  OE1 . GLU   B 2 887  ? 104.360 128.936 76.484  1.00 82.10  ? 887  GLU   A OE1 1 
ATOM   8122  O  OE2 . GLU   B 2 887  ? 103.321 129.372 74.602  1.00 84.59  ? 887  GLU   A OE2 1 
ATOM   8123  N  N   . GLY   B 2 888  ? 102.198 124.129 74.484  1.00 90.17  ? 888  GLY   A N   1 
ATOM   8124  C  CA  . GLY   B 2 888  ? 101.712 123.632 73.213  1.00 90.05  ? 888  GLY   A CA  1 
ATOM   8125  C  C   . GLY   B 2 888  ? 100.411 122.872 73.348  1.00 90.99  ? 888  GLY   A C   1 
ATOM   8126  O  O   . GLY   B 2 888  ? 100.249 122.073 74.275  1.00 93.53  ? 888  GLY   A O   1 
ATOM   8127  N  N   . ARG   B 2 889  ? 99.480  123.117 72.425  1.00 99.17  ? 889  ARG   A N   1 
ATOM   8128  C  CA  . ARG   B 2 889  ? 98.170  122.477 72.435  1.00 99.87  ? 889  ARG   A CA  1 
ATOM   8129  C  C   . ARG   B 2 889  ? 97.457  122.717 73.760  1.00 99.33  ? 889  ARG   A C   1 
ATOM   8130  O  O   . ARG   B 2 889  ? 96.909  123.799 73.988  1.00 101.78 ? 889  ARG   A O   1 
ATOM   8131  C  CB  . ARG   B 2 889  ? 98.298  120.976 72.157  1.00 101.58 ? 889  ARG   A CB  1 
ATOM   8132  C  CG  . ARG   B 2 889  ? 99.051  120.625 70.876  1.00 103.20 ? 889  ARG   A CG  1 
ATOM   8133  C  CD  . ARG   B 2 889  ? 98.307  121.074 69.623  1.00 103.11 ? 889  ARG   A CD  1 
ATOM   8134  N  NE  . ARG   B 2 889  ? 98.662  122.429 69.217  1.00 102.79 ? 889  ARG   A NE  1 
ATOM   8135  C  CZ  . ARG   B 2 889  ? 98.211  123.025 68.122  1.00 102.63 ? 889  ARG   A CZ  1 
ATOM   8136  N  NH1 . ARG   B 2 889  ? 97.380  122.414 67.294  1.00 101.80 ? 889  ARG   A NH1 1 
ATOM   8137  N  NH2 . ARG   B 2 889  ? 98.604  124.267 67.851  1.00 102.82 ? 889  ARG   A NH2 1 
ATOM   8138  N  N   . HIS   B 2 890  ? 97.463  121.717 74.636  1.00 91.91  ? 890  HIS   A N   1 
ATOM   8139  C  CA  . HIS   B 2 890  ? 96.774  121.836 75.912  1.00 92.73  ? 890  HIS   A CA  1 
ATOM   8140  C  C   . HIS   B 2 890  ? 97.505  122.800 76.839  1.00 91.67  ? 890  HIS   A C   1 
ATOM   8141  O  O   . HIS   B 2 890  ? 98.714  123.017 76.724  1.00 92.26  ? 890  HIS   A O   1 
ATOM   8142  C  CB  . HIS   B 2 890  ? 96.644  120.466 76.574  1.00 92.21  ? 890  HIS   A CB  1 
ATOM   8143  C  CG  . HIS   B 2 890  ? 95.942  119.452 75.726  1.00 95.94  ? 890  HIS   A CG  1 
ATOM   8144  N  ND1 . HIS   B 2 890  ? 94.569  119.339 75.687  1.00 97.67  ? 890  HIS   A ND1 1 
ATOM   8145  C  CD2 . HIS   B 2 890  ? 96.422  118.506 74.885  1.00 98.08  ? 890  HIS   A CD2 1 
ATOM   8146  C  CE1 . HIS   B 2 890  ? 94.233  118.366 74.858  1.00 97.62  ? 890  HIS   A CE1 1 
ATOM   8147  N  NE2 . HIS   B 2 890  ? 95.339  117.845 74.358  1.00 99.19  ? 890  HIS   A NE2 1 
ATOM   8148  N  N   . SER   B 2 891  ? 96.751  123.383 77.767  1.00 82.17  ? 891  SER   A N   1 
ATOM   8149  C  CA  . SER   B 2 891  ? 97.313  124.352 78.695  1.00 80.97  ? 891  SER   A CA  1 
ATOM   8150  C  C   . SER   B 2 891  ? 98.200  123.662 79.725  1.00 85.65  ? 891  SER   A C   1 
ATOM   8151  O  O   . SER   B 2 891  ? 98.070  122.464 79.989  1.00 89.77  ? 891  SER   A O   1 
ATOM   8152  C  CB  . SER   B 2 891  ? 96.200  125.126 79.399  1.00 83.02  ? 891  SER   A CB  1 
ATOM   8153  O  OG  . SER   B 2 891  ? 96.735  126.089 80.287  1.00 83.06  ? 891  SER   A OG  1 
ATOM   8154  N  N   . ILE   B 2 892  ? 99.113  124.441 80.309  1.00 74.01  ? 892  ILE   A N   1 
ATOM   8155  C  CA  . ILE   B 2 892  ? 100.084 123.879 81.246  1.00 71.29  ? 892  ILE   A CA  1 
ATOM   8156  C  C   . ILE   B 2 892  ? 99.389  123.382 82.507  1.00 71.79  ? 892  ILE   A C   1 
ATOM   8157  O  O   . ILE   B 2 892  ? 99.669  122.278 82.996  1.00 75.86  ? 892  ILE   A O   1 
ATOM   8158  C  CB  . ILE   B 2 892  ? 101.178 124.913 81.569  1.00 64.09  ? 892  ILE   A CB  1 
ATOM   8159  C  CG1 . ILE   B 2 892  ? 102.096 125.124 80.363  1.00 75.18  ? 892  ILE   A CG1 1 
ATOM   8160  C  CG2 . ILE   B 2 892  ? 101.993 124.464 82.762  1.00 65.29  ? 892  ILE   A CG2 1 
ATOM   8161  C  CD1 . ILE   B 2 892  ? 101.600 126.143 79.355  1.00 77.33  ? 892  ILE   A CD1 1 
ATOM   8162  N  N   . GLY   B 2 893  ? 98.474  124.183 83.054  1.00 72.22  ? 893  GLY   A N   1 
ATOM   8163  C  CA  . GLY   B 2 893  ? 97.737  123.749 84.228  1.00 74.17  ? 893  GLY   A CA  1 
ATOM   8164  C  C   . GLY   B 2 893  ? 96.895  122.519 83.961  1.00 71.93  ? 893  GLY   A C   1 
ATOM   8165  O  O   . GLY   B 2 893  ? 96.818  121.611 84.794  1.00 78.49  ? 893  GLY   A O   1 
ATOM   8166  N  N   . ASP   B 2 894  ? 96.255  122.469 82.791  1.00 67.97  ? 894  ASP   A N   1 
ATOM   8167  C  CA  . ASP   B 2 894  ? 95.496  121.283 82.416  1.00 69.94  ? 894  ASP   A CA  1 
ATOM   8168  C  C   . ASP   B 2 894  ? 96.407  120.071 82.284  1.00 75.60  ? 894  ASP   A C   1 
ATOM   8169  O  O   . ASP   B 2 894  ? 96.033  118.961 82.678  1.00 83.04  ? 894  ASP   A O   1 
ATOM   8170  C  CB  . ASP   B 2 894  ? 94.739  121.533 81.114  1.00 73.14  ? 894  ASP   A CB  1 
ATOM   8171  C  CG  . ASP   B 2 894  ? 93.734  122.658 81.234  1.00 78.60  ? 894  ASP   A CG  1 
ATOM   8172  O  OD1 . ASP   B 2 894  ? 93.211  122.870 82.347  1.00 79.48  ? 894  ASP   A OD1 1 
ATOM   8173  O  OD2 . ASP   B 2 894  ? 93.466  123.330 80.215  1.00 78.70  ? 894  ASP   A OD2 1 
ATOM   8174  N  N   . GLN   B 2 895  ? 97.608  120.262 81.730  1.00 73.74  ? 895  GLN   A N   1 
ATOM   8175  C  CA  . GLN   B 2 895  ? 98.551  119.153 81.622  1.00 72.52  ? 895  GLN   A CA  1 
ATOM   8176  C  C   . GLN   B 2 895  ? 98.949  118.630 82.995  1.00 74.99  ? 895  GLN   A C   1 
ATOM   8177  O  O   . GLN   B 2 895  ? 98.974  117.415 83.220  1.00 78.24  ? 895  GLN   A O   1 
ATOM   8178  C  CB  . GLN   B 2 895  ? 99.789  119.584 80.836  1.00 70.13  ? 895  GLN   A CB  1 
ATOM   8179  C  CG  . GLN   B 2 895  ? 99.566  119.720 79.342  1.00 75.72  ? 895  GLN   A CG  1 
ATOM   8180  C  CD  . GLN   B 2 895  ? 100.806 120.187 78.609  1.00 77.51  ? 895  GLN   A CD  1 
ATOM   8181  O  OE1 . GLN   B 2 895  ? 101.809 120.538 79.226  1.00 72.23  ? 895  GLN   A OE1 1 
ATOM   8182  N  NE2 . GLN   B 2 895  ? 100.743 120.192 77.283  1.00 79.58  ? 895  GLN   A NE2 1 
ATOM   8183  N  N   . LEU   B 2 896  ? 99.253  119.533 83.931  1.00 64.84  ? 896  LEU   A N   1 
ATOM   8184  C  CA  . LEU   B 2 896  ? 99.619  119.100 85.277  1.00 59.77  ? 896  LEU   A CA  1 
ATOM   8185  C  C   . LEU   B 2 896  ? 98.464  118.379 85.959  1.00 64.64  ? 896  LEU   A C   1 
ATOM   8186  O  O   . LEU   B 2 896  ? 98.663  117.342 86.604  1.00 73.04  ? 896  LEU   A O   1 
ATOM   8187  C  CB  . LEU   B 2 896  ? 100.068 120.296 86.114  1.00 60.71  ? 896  LEU   A CB  1 
ATOM   8188  C  CG  . LEU   B 2 896  ? 101.340 121.015 85.670  1.00 63.47  ? 896  LEU   A CG  1 
ATOM   8189  C  CD1 . LEU   B 2 896  ? 101.642 122.181 86.591  1.00 65.88  ? 896  LEU   A CD1 1 
ATOM   8190  C  CD2 . LEU   B 2 896  ? 102.509 120.054 85.625  1.00 66.53  ? 896  LEU   A CD2 1 
ATOM   8191  N  N   . ARG   B 2 897  ? 97.248  118.913 85.828  1.00 69.08  ? 897  ARG   A N   1 
ATOM   8192  C  CA  . ARG   B 2 897  ? 96.095  118.289 86.467  1.00 66.16  ? 897  ARG   A CA  1 
ATOM   8193  C  C   . ARG   B 2 897  ? 95.817  116.911 85.882  1.00 68.63  ? 897  ARG   A C   1 
ATOM   8194  O  O   . ARG   B 2 897  ? 95.534  115.960 86.621  1.00 77.37  ? 897  ARG   A O   1 
ATOM   8195  C  CB  . ARG   B 2 897  ? 94.873  119.195 86.332  1.00 68.38  ? 897  ARG   A CB  1 
ATOM   8196  C  CG  . ARG   B 2 897  ? 93.618  118.656 86.983  1.00 72.56  ? 897  ARG   A CG  1 
ATOM   8197  C  CD  . ARG   B 2 897  ? 92.728  119.793 87.459  1.00 76.53  ? 897  ARG   A CD  1 
ATOM   8198  N  NE  . ARG   B 2 897  ? 92.580  120.834 86.449  1.00 78.78  ? 897  ARG   A NE  1 
ATOM   8199  C  CZ  . ARG   B 2 897  ? 91.603  120.878 85.554  1.00 78.17  ? 897  ARG   A CZ  1 
ATOM   8200  N  NH1 . ARG   B 2 897  ? 90.660  119.951 85.513  1.00 75.25  ? 897  ARG   A NH1 1 
ATOM   8201  N  NH2 . ARG   B 2 897  ? 91.570  121.879 84.679  1.00 75.38  ? 897  ARG   A NH2 1 
ATOM   8202  N  N   . GLU   B 2 898  ? 95.901  116.780 84.557  1.00 76.37  ? 898  GLU   A N   1 
ATOM   8203  C  CA  . GLU   B 2 898  ? 95.691  115.483 83.926  1.00 79.29  ? 898  GLU   A CA  1 
ATOM   8204  C  C   . GLU   B 2 898  ? 96.770  114.491 84.336  1.00 82.36  ? 898  GLU   A C   1 
ATOM   8205  O  O   . GLU   B 2 898  ? 96.476  113.315 84.576  1.00 87.16  ? 898  GLU   A O   1 
ATOM   8206  C  CB  . GLU   B 2 898  ? 95.648  115.638 82.407  1.00 83.55  ? 898  GLU   A CB  1 
ATOM   8207  C  CG  . GLU   B 2 898  ? 95.302  114.361 81.661  1.00 84.57  ? 898  GLU   A CG  1 
ATOM   8208  C  CD  . GLU   B 2 898  ? 95.170  114.578 80.166  1.00 87.21  ? 898  GLU   A CD  1 
ATOM   8209  O  OE1 . GLU   B 2 898  ? 95.376  115.722 79.710  1.00 85.84  ? 898  GLU   A OE1 1 
ATOM   8210  O  OE2 . GLU   B 2 898  ? 94.860  113.605 79.447  1.00 87.05  ? 898  GLU   A OE2 1 
ATOM   8211  N  N   . ALA   B 2 899  ? 98.023  114.944 84.421  1.00 76.98  ? 899  ALA   A N   1 
ATOM   8212  C  CA  . ALA   B 2 899  ? 99.098  114.062 84.862  1.00 73.24  ? 899  ALA   A CA  1 
ATOM   8213  C  C   . ALA   B 2 899  ? 98.852  113.572 86.282  1.00 71.24  ? 899  ALA   A C   1 
ATOM   8214  O  O   . ALA   B 2 899  ? 99.007  112.381 86.576  1.00 76.93  ? 899  ALA   A O   1 
ATOM   8215  C  CB  . ALA   B 2 899  ? 100.442 114.782 84.763  1.00 72.75  ? 899  ALA   A CB  1 
ATOM   8216  N  N   . LEU   B 2 900  ? 98.455  114.480 87.176  1.00 68.64  ? 900  LEU   A N   1 
ATOM   8217  C  CA  . LEU   B 2 900  ? 98.160  114.085 88.549  1.00 68.23  ? 900  LEU   A CA  1 
ATOM   8218  C  C   . LEU   B 2 900  ? 97.019  113.078 88.595  1.00 74.73  ? 900  LEU   A C   1 
ATOM   8219  O  O   . LEU   B 2 900  ? 97.116  112.045 89.266  1.00 79.99  ? 900  LEU   A O   1 
ATOM   8220  C  CB  . LEU   B 2 900  ? 97.824  115.313 89.393  1.00 68.10  ? 900  LEU   A CB  1 
ATOM   8221  C  CG  . LEU   B 2 900  ? 98.990  116.066 90.028  1.00 69.99  ? 900  LEU   A CG  1 
ATOM   8222  C  CD1 . LEU   B 2 900  ? 98.488  117.302 90.746  1.00 69.75  ? 900  LEU   A CD1 1 
ATOM   8223  C  CD2 . LEU   B 2 900  ? 99.740  115.160 90.985  1.00 73.49  ? 900  LEU   A CD2 1 
ATOM   8224  N  N   . GLU   B 2 901  ? 95.937  113.349 87.862  1.00 79.68  ? 901  GLU   A N   1 
ATOM   8225  C  CA  . GLU   B 2 901  ? 94.784  112.456 87.893  1.00 76.03  ? 901  GLU   A CA  1 
ATOM   8226  C  C   . GLU   B 2 901  ? 95.120  111.082 87.324  1.00 80.54  ? 901  GLU   A C   1 
ATOM   8227  O  O   . GLU   B 2 901  ? 94.654  110.062 87.843  1.00 84.82  ? 901  GLU   A O   1 
ATOM   8228  C  CB  . GLU   B 2 901  ? 93.614  113.077 87.131  1.00 79.52  ? 901  GLU   A CB  1 
ATOM   8229  C  CG  . GLU   B 2 901  ? 93.051  114.339 87.763  1.00 84.94  ? 901  GLU   A CG  1 
ATOM   8230  C  CD  . GLU   B 2 901  ? 92.327  114.071 89.068  1.00 86.97  ? 901  GLU   A CD  1 
ATOM   8231  O  OE1 . GLU   B 2 901  ? 91.962  112.904 89.324  1.00 85.89  ? 901  GLU   A OE1 1 
ATOM   8232  O  OE2 . GLU   B 2 901  ? 92.120  115.031 89.839  1.00 87.96  ? 901  GLU   A OE2 1 
ATOM   8233  N  N   . GLU   B 2 902  ? 95.925  111.031 86.264  1.00 78.96  ? 902  GLU   A N   1 
ATOM   8234  C  CA  . GLU   B 2 902  ? 96.188  109.778 85.573  1.00 79.48  ? 902  GLU   A CA  1 
ATOM   8235  C  C   . GLU   B 2 902  ? 97.358  108.991 86.147  1.00 78.00  ? 902  GLU   A C   1 
ATOM   8236  O  O   . GLU   B 2 902  ? 97.488  107.803 85.836  1.00 81.35  ? 902  GLU   A O   1 
ATOM   8237  C  CB  . GLU   B 2 902  ? 96.443  110.039 84.084  1.00 82.64  ? 902  GLU   A CB  1 
ATOM   8238  C  CG  . GLU   B 2 902  ? 95.249  110.609 83.333  1.00 86.19  ? 902  GLU   A CG  1 
ATOM   8239  C  CD  . GLU   B 2 902  ? 94.112  109.615 83.192  1.00 87.58  ? 902  GLU   A CD  1 
ATOM   8240  O  OE1 . GLU   B 2 902  ? 94.363  108.396 83.301  1.00 85.51  ? 902  GLU   A OE1 1 
ATOM   8241  O  OE2 . GLU   B 2 902  ? 92.964  110.055 82.973  1.00 85.64  ? 902  GLU   A OE2 1 
ATOM   8242  N  N   . PHE   B 2 903  ? 98.210  109.601 86.974  1.00 69.10  ? 903  PHE   A N   1 
ATOM   8243  C  CA  . PHE   B 2 903  ? 99.363  108.893 87.506  1.00 67.73  ? 903  PHE   A CA  1 
ATOM   8244  C  C   . PHE   B 2 903  ? 99.411  108.805 89.025  1.00 70.56  ? 903  PHE   A C   1 
ATOM   8245  O  O   . PHE   B 2 903  ? 100.125 107.942 89.545  1.00 72.93  ? 903  PHE   A O   1 
ATOM   8246  C  CB  . PHE   B 2 903  ? 100.664 109.543 87.011  1.00 69.87  ? 903  PHE   A CB  1 
ATOM   8247  C  CG  . PHE   B 2 903  ? 100.895 109.384 85.535  1.00 69.60  ? 903  PHE   A CG  1 
ATOM   8248  C  CD1 . PHE   B 2 903  ? 100.425 108.273 84.861  1.00 69.98  ? 903  PHE   A CD1 1 
ATOM   8249  C  CD2 . PHE   B 2 903  ? 101.581 110.350 84.822  1.00 73.92  ? 903  PHE   A CD2 1 
ATOM   8250  C  CE1 . PHE   B 2 903  ? 100.637 108.128 83.504  1.00 69.46  ? 903  PHE   A CE1 1 
ATOM   8251  C  CE2 . PHE   B 2 903  ? 101.796 110.209 83.467  1.00 74.20  ? 903  PHE   A CE2 1 
ATOM   8252  C  CZ  . PHE   B 2 903  ? 101.323 109.098 82.808  1.00 70.54  ? 903  PHE   A CZ  1 
ATOM   8253  N  N   . PHE   B 2 904  ? 98.681  109.656 89.749  1.00 69.46  ? 904  PHE   A N   1 
ATOM   8254  C  CA  . PHE   B 2 904  ? 98.669  109.603 91.205  1.00 69.71  ? 904  PHE   A CA  1 
ATOM   8255  C  C   . PHE   B 2 904  ? 97.246  109.636 91.744  1.00 73.66  ? 904  PHE   A C   1 
ATOM   8256  O  O   . PHE   B 2 904  ? 97.020  110.065 92.880  1.00 75.74  ? 904  PHE   A O   1 
ATOM   8257  C  CB  . PHE   B 2 904  ? 99.471  110.756 91.811  1.00 71.36  ? 904  PHE   A CB  1 
ATOM   8258  C  CG  . PHE   B 2 904  ? 100.903 110.803 91.369  1.00 66.85  ? 904  PHE   A CG  1 
ATOM   8259  C  CD1 . PHE   B 2 904  ? 101.877 110.109 92.061  1.00 68.22  ? 904  PHE   A CD1 1 
ATOM   8260  C  CD2 . PHE   B 2 904  ? 101.277 111.550 90.268  1.00 69.43  ? 904  PHE   A CD2 1 
ATOM   8261  C  CE1 . PHE   B 2 904  ? 103.194 110.154 91.659  1.00 70.10  ? 904  PHE   A CE1 1 
ATOM   8262  C  CE2 . PHE   B 2 904  ? 102.593 111.597 89.863  1.00 69.42  ? 904  PHE   A CE2 1 
ATOM   8263  C  CZ  . PHE   B 2 904  ? 103.552 110.899 90.559  1.00 72.46  ? 904  PHE   A CZ  1 
ATOM   8264  N  N   . GLY   B 2 905  ? 96.276  109.191 90.942  1.00 84.92  ? 905  GLY   A N   1 
ATOM   8265  C  CA  . GLY   B 2 905  ? 94.887  109.272 91.356  1.00 83.75  ? 905  GLY   A CA  1 
ATOM   8266  C  C   . GLY   B 2 905  ? 94.577  108.456 92.593  1.00 85.94  ? 905  GLY   A C   1 
ATOM   8267  O  O   . GLY   B 2 905  ? 93.755  108.862 93.419  1.00 85.61  ? 905  GLY   A O   1 
ATOM   8268  N  N   . GLU   B 2 906  ? 95.226  107.306 92.745  1.00 104.32 ? 906  GLU   A N   1 
ATOM   8269  C  CA  . GLU   B 2 906  ? 95.007  106.436 93.901  1.00 105.45 ? 906  GLU   A CA  1 
ATOM   8270  C  C   . GLU   B 2 906  ? 95.810  106.903 95.113  1.00 105.66 ? 906  GLU   A C   1 
ATOM   8271  O  O   . GLU   B 2 906  ? 96.545  106.139 95.738  1.00 104.39 ? 906  GLU   A O   1 
ATOM   8272  C  CB  . GLU   B 2 906  ? 95.345  104.993 93.539  1.00 104.58 ? 906  GLU   A CB  1 
ATOM   8273  C  CG  . GLU   B 2 906  ? 96.711  104.793 92.888  1.00 104.14 ? 906  GLU   A CG  1 
ATOM   8274  C  CD  . GLU   B 2 906  ? 96.691  105.021 91.388  1.00 104.92 ? 906  GLU   A CD  1 
ATOM   8275  O  OE1 . GLU   B 2 906  ? 95.599  105.276 90.837  1.00 104.33 ? 906  GLU   A OE1 1 
ATOM   8276  O  OE2 . GLU   B 2 906  ? 97.768  104.944 90.759  1.00 104.59 ? 906  GLU   A OE2 1 
ATOM   8277  N  N   . ASP   B 2 907  ? 95.660  108.180 95.458  1.00 115.27 ? 907  ASP   A N   1 
ATOM   8278  C  CA  . ASP   B 2 907  ? 96.335  108.773 96.604  1.00 115.73 ? 907  ASP   A CA  1 
ATOM   8279  C  C   . ASP   B 2 907  ? 95.300  109.449 97.489  1.00 115.12 ? 907  ASP   A C   1 
ATOM   8280  O  O   . ASP   B 2 907  ? 94.533  110.294 97.017  1.00 113.60 ? 907  ASP   A O   1 
ATOM   8281  C  CB  . ASP   B 2 907  ? 97.400  109.782 96.162  1.00 115.28 ? 907  ASP   A CB  1 
ATOM   8282  C  CG  . ASP   B 2 907  ? 98.139  110.400 97.332  1.00 115.41 ? 907  ASP   A CG  1 
ATOM   8283  O  OD1 . ASP   B 2 907  ? 98.928  109.684 97.984  1.00 114.39 ? 907  ASP   A OD1 1 
ATOM   8284  O  OD2 . ASP   B 2 907  ? 97.932  111.602 97.600  1.00 115.45 ? 907  ASP   A OD2 1 
ATOM   8285  N  N   . ALA   B 2 908  ? 95.280  109.073 98.770  1.00 123.66 ? 908  ALA   A N   1 
ATOM   8286  C  CA  . ALA   B 2 908  ? 94.324  109.665 99.699  1.00 123.87 ? 908  ALA   A CA  1 
ATOM   8287  C  C   . ALA   B 2 908  ? 94.602  111.148 99.912  1.00 124.33 ? 908  ALA   A C   1 
ATOM   8288  O  O   . ALA   B 2 908  ? 93.669  111.957 99.974  1.00 124.64 ? 908  ALA   A O   1 
ATOM   8289  C  CB  . ALA   B 2 908  ? 94.354  108.915 101.031 1.00 123.40 ? 908  ALA   A CB  1 
ATOM   8290  N  N   . GLY   B 2 909  ? 95.875  111.523 100.025 1.00 125.65 ? 909  GLY   A N   1 
ATOM   8291  C  CA  . GLY   B 2 909  ? 96.232  112.907 100.269 1.00 126.40 ? 909  GLY   A CA  1 
ATOM   8292  C  C   . GLY   B 2 909  ? 96.149  113.820 99.067  1.00 127.52 ? 909  GLY   A C   1 
ATOM   8293  O  O   . GLY   B 2 909  ? 96.236  115.041 99.230  1.00 126.17 ? 909  GLY   A O   1 
ATOM   8294  N  N   . LEU   B 2 910  ? 95.988  113.263 97.864  1.00 124.33 ? 910  LEU   A N   1 
ATOM   8295  C  CA  . LEU   B 2 910  ? 95.892  114.100 96.673  1.00 123.27 ? 910  LEU   A CA  1 
ATOM   8296  C  C   . LEU   B 2 910  ? 94.612  114.925 96.677  1.00 123.32 ? 910  LEU   A C   1 
ATOM   8297  O  O   . LEU   B 2 910  ? 94.616  116.087 96.252  1.00 123.78 ? 910  LEU   A O   1 
ATOM   8298  C  CB  . LEU   B 2 910  ? 95.970  113.240 95.413  1.00 122.43 ? 910  LEU   A CB  1 
ATOM   8299  C  CG  . LEU   B 2 910  ? 95.972  114.026 94.100  1.00 123.37 ? 910  LEU   A CG  1 
ATOM   8300  C  CD1 . LEU   B 2 910  ? 97.201  114.916 94.018  1.00 121.67 ? 910  LEU   A CD1 1 
ATOM   8301  C  CD2 . LEU   B 2 910  ? 95.897  113.093 92.902  1.00 120.93 ? 910  LEU   A CD2 1 
ATOM   8302  N  N   . ARG   B 2 911  ? 93.508  114.345 97.157  1.00 124.39 ? 911  ARG   A N   1 
ATOM   8303  C  CA  . ARG   B 2 911  ? 92.232  115.053 97.151  1.00 124.97 ? 911  ARG   A CA  1 
ATOM   8304  C  C   . ARG   B 2 911  ? 92.285  116.324 97.987  1.00 123.67 ? 911  ARG   A C   1 
ATOM   8305  O  O   . ARG   B 2 911  ? 91.530  117.268 97.728  1.00 122.11 ? 911  ARG   A O   1 
ATOM   8306  C  CB  . ARG   B 2 911  ? 91.119  114.134 97.656  1.00 125.49 ? 911  ARG   A CB  1 
ATOM   8307  C  CG  . ARG   B 2 911  ? 90.883  112.909 96.789  1.00 125.68 ? 911  ARG   A CG  1 
ATOM   8308  C  CD  . ARG   B 2 911  ? 89.736  112.068 97.326  1.00 126.01 ? 911  ARG   A CD  1 
ATOM   8309  N  NE  . ARG   B 2 911  ? 89.478  110.900 96.492  1.00 127.30 ? 911  ARG   A NE  1 
ATOM   8310  C  CZ  . ARG   B 2 911  ? 88.524  110.008 96.726  1.00 126.51 ? 911  ARG   A CZ  1 
ATOM   8311  N  NH1 . ARG   B 2 911  ? 87.714  110.120 97.766  1.00 125.01 ? 911  ARG   A NH1 1 
ATOM   8312  N  NH2 . ARG   B 2 911  ? 88.380  108.980 95.896  1.00 126.25 ? 911  ARG   A NH2 1 
ATOM   8313  N  N   . THR   B 2 912  ? 93.160  116.367 98.994  1.00 125.01 ? 912  THR   A N   1 
ATOM   8314  C  CA  . THR   B 2 912  ? 93.328  117.591 99.769  1.00 127.09 ? 912  THR   A CA  1 
ATOM   8315  C  C   . THR   B 2 912  ? 93.850  118.724 98.894  1.00 127.29 ? 912  THR   A C   1 
ATOM   8316  O  O   . THR   B 2 912  ? 93.391  119.867 99.004  1.00 127.40 ? 912  THR   A O   1 
ATOM   8317  C  CB  . THR   B 2 912  ? 94.273  117.343 100.946 1.00 127.10 ? 912  THR   A CB  1 
ATOM   8318  O  OG1 . THR   B 2 912  ? 93.765  116.270 101.749 1.00 126.64 ? 912  THR   A OG1 1 
ATOM   8319  C  CG2 . THR   B 2 912  ? 94.400  118.593 101.804 1.00 125.66 ? 912  THR   A CG2 1 
ATOM   8320  N  N   . THR   B 2 913  ? 94.803  118.424 98.013  1.00 124.75 ? 913  THR   A N   1 
ATOM   8321  C  CA  . THR   B 2 913  ? 95.344  119.423 97.102  1.00 124.28 ? 913  THR   A CA  1 
ATOM   8322  C  C   . THR   B 2 913  ? 94.460  119.657 95.884  1.00 124.39 ? 913  THR   A C   1 
ATOM   8323  O  O   . THR   B 2 913  ? 94.666  120.646 95.172  1.00 124.91 ? 913  THR   A O   1 
ATOM   8324  C  CB  . THR   B 2 913  ? 96.745  119.016 96.640  1.00 125.03 ? 913  THR   A CB  1 
ATOM   8325  O  OG1 . THR   B 2 913  ? 96.680  117.753 95.965  1.00 125.54 ? 913  THR   A OG1 1 
ATOM   8326  C  CG2 . THR   B 2 913  ? 97.687  118.903 97.829  1.00 123.10 ? 913  THR   A CG2 1 
ATOM   8327  N  N   . LEU   B 2 914  ? 93.488  118.782 95.626  1.00 117.96 ? 914  LEU   A N   1 
ATOM   8328  C  CA  . LEU   B 2 914  ? 92.609  118.940 94.476  1.00 117.32 ? 914  LEU   A CA  1 
ATOM   8329  C  C   . LEU   B 2 914  ? 91.447  119.887 94.740  1.00 117.82 ? 914  LEU   A C   1 
ATOM   8330  O  O   . LEU   B 2 914  ? 90.680  120.171 93.814  1.00 117.45 ? 914  LEU   A O   1 
ATOM   8331  C  CB  . LEU   B 2 914  ? 92.069  117.578 94.035  1.00 118.76 ? 914  LEU   A CB  1 
ATOM   8332  C  CG  . LEU   B 2 914  ? 93.100  116.595 93.478  1.00 118.64 ? 914  LEU   A CG  1 
ATOM   8333  C  CD1 . LEU   B 2 914  ? 92.437  115.284 93.086  1.00 117.36 ? 914  LEU   A CD1 1 
ATOM   8334  C  CD2 . LEU   B 2 914  ? 93.839  117.204 92.297  1.00 117.02 ? 914  LEU   A CD2 1 
ATOM   8335  N  N   . SER   B 2 915  ? 91.297  120.380 95.968  1.00 117.15 ? 915  SER   A N   1 
ATOM   8336  C  CA  . SER   B 2 915  ? 90.225  121.314 96.287  1.00 116.90 ? 915  SER   A CA  1 
ATOM   8337  C  C   . SER   B 2 915  ? 90.526  122.687 95.701  1.00 116.37 ? 915  SER   A C   1 
ATOM   8338  O  O   . SER   B 2 915  ? 91.227  123.494 96.320  1.00 115.90 ? 915  SER   A O   1 
ATOM   8339  C  CB  . SER   B 2 915  ? 90.030  121.410 97.801  1.00 116.00 ? 915  SER   A CB  1 
ATOM   8340  O  OG  . SER   B 2 915  ? 91.213  121.857 98.440  1.00 116.35 ? 915  SER   A OG  1 
ATOM   8341  N  N   . ARG   B 2 916  ? 90.000  122.961 94.510  1.00 109.90 ? 916  ARG   A N   1 
ATOM   8342  C  CA  . ARG   B 2 916  ? 90.242  124.215 93.814  1.00 111.16 ? 916  ARG   A CA  1 
ATOM   8343  C  C   . ARG   B 2 916  ? 88.915  124.872 93.466  1.00 111.19 ? 916  ARG   A C   1 
ATOM   8344  O  O   . ARG   B 2 916  ? 87.903  124.197 93.261  1.00 110.30 ? 916  ARG   A O   1 
ATOM   8345  C  CB  . ARG   B 2 916  ? 91.067  124.000 92.537  1.00 109.93 ? 916  ARG   A CB  1 
ATOM   8346  C  CG  . ARG   B 2 916  ? 92.327  123.175 92.743  1.00 109.83 ? 916  ARG   A CG  1 
ATOM   8347  C  CD  . ARG   B 2 916  ? 93.259  123.823 93.752  1.00 109.67 ? 916  ARG   A CD  1 
ATOM   8348  N  NE  . ARG   B 2 916  ? 94.397  122.968 94.064  1.00 110.25 ? 916  ARG   A NE  1 
ATOM   8349  C  CZ  . ARG   B 2 916  ? 95.549  122.983 93.408  1.00 109.75 ? 916  ARG   A CZ  1 
ATOM   8350  N  NH1 . ARG   B 2 916  ? 95.757  123.807 92.395  1.00 108.62 ? 916  ARG   A NH1 1 
ATOM   8351  N  NH2 . ARG   B 2 916  ? 96.517  122.149 93.778  1.00 109.77 ? 916  ARG   A NH2 1 
ATOM   8352  N  N   . ILE   B 2 917  ? 88.931  126.199 93.402  1.00 114.90 ? 917  ILE   A N   1 
ATOM   8353  C  CA  . ILE   B 2 917  ? 87.733  126.963 93.080  1.00 114.79 ? 917  ILE   A CA  1 
ATOM   8354  C  C   . ILE   B 2 917  ? 88.038  127.998 92.005  1.00 114.36 ? 917  ILE   A C   1 
ATOM   8355  O  O   . ILE   B 2 917  ? 89.200  128.309 91.741  1.00 114.05 ? 917  ILE   A O   1 
ATOM   8356  C  CB  . ILE   B 2 917  ? 87.150  127.635 94.334  1.00 114.58 ? 917  ILE   A CB  1 
ATOM   8357  C  CG1 . ILE   B 2 917  ? 85.907  128.452 93.973  1.00 113.81 ? 917  ILE   A CG1 1 
ATOM   8358  C  CG2 . ILE   B 2 917  ? 88.197  128.514 95.003  1.00 112.31 ? 917  ILE   A CG2 1 
ATOM   8359  C  CD1 . ILE   B 2 917  ? 85.257  129.132 95.158  1.00 112.45 ? 917  ILE   A CD1 1 
ATOM   8360  N  N   . LEU   B 2 939  ? 100.028 117.349 70.412  1.00 116.78 ? 939  LEU   A N   1 
ATOM   8361  C  CA  . LEU   B 2 939  ? 99.467  116.988 71.709  1.00 117.45 ? 939  LEU   A CA  1 
ATOM   8362  C  C   . LEU   B 2 939  ? 100.507 116.281 72.572  1.00 116.73 ? 939  LEU   A C   1 
ATOM   8363  O  O   . LEU   B 2 939  ? 100.514 115.054 72.669  1.00 116.00 ? 939  LEU   A O   1 
ATOM   8364  C  CB  . LEU   B 2 939  ? 98.230  116.098 71.539  1.00 117.96 ? 939  LEU   A CB  1 
ATOM   8365  C  CG  . LEU   B 2 939  ? 96.929  116.738 71.041  1.00 117.05 ? 939  LEU   A CG  1 
ATOM   8366  C  CD1 . LEU   B 2 939  ? 96.963  117.006 69.541  1.00 115.38 ? 939  LEU   A CD1 1 
ATOM   8367  C  CD2 . LEU   B 2 939  ? 95.735  115.867 71.404  1.00 115.95 ? 939  LEU   A CD2 1 
ATOM   8368  N  N   . VAL   B 2 940  ? 101.387 117.064 73.193  1.00 111.28 ? 940  VAL   A N   1 
ATOM   8369  C  CA  . VAL   B 2 940  ? 102.433 116.523 74.055  1.00 112.47 ? 940  VAL   A CA  1 
ATOM   8370  C  C   . VAL   B 2 940  ? 101.800 115.973 75.326  1.00 112.40 ? 940  VAL   A C   1 
ATOM   8371  O  O   . VAL   B 2 940  ? 101.913 114.778 75.622  1.00 112.55 ? 940  VAL   A O   1 
ATOM   8372  C  CB  . VAL   B 2 940  ? 103.496 117.587 74.378  1.00 111.19 ? 940  VAL   A CB  1 
ATOM   8373  C  CG1 . VAL   B 2 940  ? 104.561 117.011 75.299  1.00 107.59 ? 940  VAL   A CG1 1 
ATOM   8374  C  CG2 . VAL   B 2 940  ? 104.118 118.120 73.095  1.00 109.19 ? 940  VAL   A CG2 1 
ATOM   8375  N  N   . GLY   B 2 941  ? 101.128 116.840 76.081  1.00 100.89 ? 941  GLY   A N   1 
ATOM   8376  C  CA  . GLY   B 2 941  ? 100.404 116.423 77.266  1.00 99.49  ? 941  GLY   A CA  1 
ATOM   8377  C  C   . GLY   B 2 941  ? 101.260 115.799 78.350  1.00 99.69  ? 941  GLY   A C   1 
ATOM   8378  O  O   . GLY   B 2 941  ? 102.217 116.413 78.830  1.00 98.23  ? 941  GLY   A O   1 
ATOM   8379  N  N   . ARG   B 2 942  ? 100.914 114.572 78.747  1.00 99.17  ? 942  ARG   A N   1 
ATOM   8380  C  CA  . ARG   B 2 942  ? 101.613 113.883 79.825  1.00 98.70  ? 942  ARG   A CA  1 
ATOM   8381  C  C   . ARG   B 2 942  ? 102.027 112.469 79.423  1.00 99.43  ? 942  ARG   A C   1 
ATOM   8382  O  O   . ARG   B 2 942  ? 102.278 111.632 80.300  1.00 96.15  ? 942  ARG   A O   1 
ATOM   8383  C  CB  . ARG   B 2 942  ? 100.747 113.844 81.102  1.00 97.11  ? 942  ARG   A CB  1 
ATOM   8384  C  CG  . ARG   B 2 942  ? 99.576  112.839 81.116  1.00 97.83  ? 942  ARG   A CG  1 
ATOM   8385  C  CD  . ARG   B 2 942  ? 98.478  113.154 80.102  1.00 98.20  ? 942  ARG   A CD  1 
ATOM   8386  N  NE  . ARG   B 2 942  ? 98.774  112.580 78.794  1.00 98.98  ? 942  ARG   A NE  1 
ATOM   8387  C  CZ  . ARG   B 2 942  ? 98.015  112.729 77.718  1.00 98.80  ? 942  ARG   A CZ  1 
ATOM   8388  N  NH1 . ARG   B 2 942  ? 96.892  113.426 77.755  1.00 98.28  ? 942  ARG   A NH1 1 
ATOM   8389  N  NH2 . ARG   B 2 942  ? 98.392  112.163 76.575  1.00 96.43  ? 942  ARG   A NH2 1 
ATOM   8390  N  N   . ASP   B 2 943  ? 102.133 112.194 78.123  1.00 102.34 ? 943  ASP   A N   1 
ATOM   8391  C  CA  . ASP   B 2 943  ? 102.408 110.851 77.622  1.00 102.01 ? 943  ASP   A CA  1 
ATOM   8392  C  C   . ASP   B 2 943  ? 103.895 110.513 77.703  1.00 100.65 ? 943  ASP   A C   1 
ATOM   8393  O  O   . ASP   B 2 943  ? 104.667 111.235 78.344  1.00 99.71  ? 943  ASP   A O   1 
ATOM   8394  C  CB  . ASP   B 2 943  ? 101.906 110.718 76.181  1.00 103.24 ? 943  ASP   A CB  1 
ATOM   8395  C  CG  . ASP   B 2 943  ? 101.561 109.289 75.809  1.00 103.65 ? 943  ASP   A CG  1 
ATOM   8396  O  OD1 . ASP   B 2 943  ? 100.537 108.774 76.304  1.00 102.29 ? 943  ASP   A OD1 1 
ATOM   8397  O  OD2 . ASP   B 2 943  ? 102.312 108.679 75.019  1.00 103.44 ? 943  ASP   A OD2 1 
ATOM   8398  N  N   . ASN   B 2 944  ? 104.283 109.396 77.077  1.00 99.00  ? 944  ASN   A N   1 
ATOM   8399  C  CA  . ASN   B 2 944  ? 105.652 108.888 76.995  1.00 100.20 ? 944  ASN   A CA  1 
ATOM   8400  C  C   . ASN   B 2 944  ? 106.133 108.314 78.323  1.00 100.91 ? 944  ASN   A C   1 
ATOM   8401  O  O   . ASN   B 2 944  ? 105.860 108.869 79.393  1.00 99.58  ? 944  ASN   A O   1 
ATOM   8402  C  CB  . ASN   B 2 944  ? 106.626 109.967 76.510  1.00 98.83  ? 944  ASN   A CB  1 
ATOM   8403  C  CG  . ASN   B 2 944  ? 108.057 109.460 76.418  1.00 99.16  ? 944  ASN   A CG  1 
ATOM   8404  O  OD1 . ASN   B 2 944  ? 108.295 108.272 76.187  1.00 98.93  ? 944  ASN   A OD1 1 
ATOM   8405  N  ND2 . ASN   B 2 944  ? 109.015 110.358 76.608  1.00 97.32  ? 944  ASN   A ND2 1 
ATOM   8406  N  N   . GLY   B 2 945  ? 106.871 107.214 78.249  1.00 93.11  ? 945  GLY   A N   1 
ATOM   8407  C  CA  . GLY   B 2 945  ? 107.361 106.533 79.431  1.00 90.77  ? 945  GLY   A CA  1 
ATOM   8408  C  C   . GLY   B 2 945  ? 107.989 105.217 79.039  1.00 91.74  ? 945  GLY   A C   1 
ATOM   8409  O  O   . GLY   B 2 945  ? 107.918 104.782 77.885  1.00 92.37  ? 945  GLY   A O   1 
ATOM   8410  N  N   . THR   B 2 946  ? 108.613 104.577 80.027  1.00 99.06  ? 946  THR   A N   1 
ATOM   8411  C  CA  . THR   B 2 946  ? 109.327 103.325 79.794  1.00 102.53 ? 946  THR   A CA  1 
ATOM   8412  C  C   . THR   B 2 946  ? 108.668 102.144 80.493  1.00 102.13 ? 946  THR   A C   1 
ATOM   8413  O  O   . THR   B 2 946  ? 108.306 101.167 79.828  1.00 100.80 ? 946  THR   A O   1 
ATOM   8414  C  CB  . THR   B 2 946  ? 110.789 103.468 80.237  1.00 101.16 ? 946  THR   A CB  1 
ATOM   8415  O  OG1 . THR   B 2 946  ? 111.417 104.514 79.484  1.00 99.74  ? 946  THR   A OG1 1 
ATOM   8416  C  CG2 . THR   B 2 946  ? 111.543 102.167 80.015  1.00 99.04  ? 946  THR   A CG2 1 
ATOM   8417  N  N   . ARG   B 2 947  ? 108.492 102.203 81.813  1.00 100.05 ? 947  ARG   A N   1 
ATOM   8418  C  CA  . ARG   B 2 947  ? 107.891 101.109 82.567  1.00 101.42 ? 947  ARG   A CA  1 
ATOM   8419  C  C   . ARG   B 2 947  ? 107.492 101.591 83.958  1.00 99.79  ? 947  ARG   A C   1 
ATOM   8420  O  O   . ARG   B 2 947  ? 108.164 102.458 84.530  1.00 95.29  ? 947  ARG   A O   1 
ATOM   8421  C  CB  . ARG   B 2 947  ? 108.855 99.923  82.661  1.00 98.62  ? 947  ARG   A CB  1 
ATOM   8422  C  CG  . ARG   B 2 947  ? 110.267 100.291 83.086  1.00 97.14  ? 947  ARG   A CG  1 
ATOM   8423  C  CD  . ARG   B 2 947  ? 111.172 99.067  83.133  1.00 98.30  ? 947  ARG   A CD  1 
ATOM   8424  N  NE  . ARG   B 2 947  ? 112.542 99.414  83.493  1.00 99.87  ? 947  ARG   A NE  1 
ATOM   8425  C  CZ  . ARG   B 2 947  ? 113.535 98.542  83.601  1.00 99.35  ? 947  ARG   A CZ  1 
ATOM   8426  N  NH1 . ARG   B 2 947  ? 113.347 97.250  83.385  1.00 99.20  ? 947  ARG   A NH1 1 
ATOM   8427  N  NH2 . ARG   B 2 947  ? 114.747 98.976  83.934  1.00 98.02  ? 947  ARG   A NH2 1 
ATOM   8428  N  N   . PRO   B 2 948  ? 106.411 101.059 84.531  1.00 105.29 ? 948  PRO   A N   1 
ATOM   8429  C  CA  . PRO   B 2 948  ? 105.971 101.529 85.850  1.00 103.01 ? 948  PRO   A CA  1 
ATOM   8430  C  C   . PRO   B 2 948  ? 106.977 101.184 86.938  1.00 103.05 ? 948  PRO   A C   1 
ATOM   8431  O  O   . PRO   B 2 948  ? 107.700 100.189 86.858  1.00 103.44 ? 948  PRO   A O   1 
ATOM   8432  C  CB  . PRO   B 2 948  ? 104.641 100.796 86.062  1.00 101.97 ? 948  PRO   A CB  1 
ATOM   8433  C  CG  . PRO   B 2 948  ? 104.739 99.582  85.197  1.00 101.16 ? 948  PRO   A CG  1 
ATOM   8434  C  CD  . PRO   B 2 948  ? 105.530 100.008 83.994  1.00 101.64 ? 948  PRO   A CD  1 
ATOM   8435  N  N   . GLY   B 2 949  ? 107.007 102.022 87.972  1.00 90.39  ? 949  GLY   A N   1 
ATOM   8436  C  CA  . GLY   B 2 949  ? 107.941 101.853 89.068  1.00 87.96  ? 949  GLY   A CA  1 
ATOM   8437  C  C   . GLY   B 2 949  ? 108.431 103.169 89.638  1.00 88.01  ? 949  GLY   A C   1 
ATOM   8438  O  O   . GLY   B 2 949  ? 109.101 103.195 90.674  1.00 89.88  ? 949  GLY   A O   1 
ATOM   8439  N  N   . GLY   B 2 950  ? 108.099 104.268 88.966  1.00 72.19  ? 950  GLY   A N   1 
ATOM   8440  C  CA  . GLY   B 2 950  ? 108.466 105.594 89.423  1.00 69.59  ? 950  GLY   A CA  1 
ATOM   8441  C  C   . GLY   B 2 950  ? 108.104 106.656 88.406  1.00 74.47  ? 950  GLY   A C   1 
ATOM   8442  O  O   . GLY   B 2 950  ? 107.896 106.343 87.231  1.00 79.93  ? 950  GLY   A O   1 
ATOM   8443  N  N   . PHE   B 2 951  ? 108.028 107.913 88.834  1.00 62.19  ? 951  PHE   A N   1 
ATOM   8444  C  CA  . PHE   B 2 951  ? 107.684 109.011 87.944  1.00 55.79  ? 951  PHE   A CA  1 
ATOM   8445  C  C   . PHE   B 2 951  ? 108.682 110.146 88.100  1.00 60.05  ? 951  PHE   A C   1 
ATOM   8446  O  O   . PHE   B 2 951  ? 109.107 110.465 89.214  1.00 67.78  ? 951  PHE   A O   1 
ATOM   8447  C  CB  . PHE   B 2 951  ? 106.271 109.526 88.211  1.00 55.56  ? 951  PHE   A CB  1 
ATOM   8448  C  CG  . PHE   B 2 951  ? 105.192 108.581 87.780  1.00 56.38  ? 951  PHE   A CG  1 
ATOM   8449  C  CD1 . PHE   B 2 951  ? 104.775 108.543 86.465  1.00 58.24  ? 951  PHE   A CD1 1 
ATOM   8450  C  CD2 . PHE   B 2 951  ? 104.595 107.730 88.691  1.00 61.96  ? 951  PHE   A CD2 1 
ATOM   8451  C  CE1 . PHE   B 2 951  ? 103.784 107.674 86.063  1.00 65.32  ? 951  PHE   A CE1 1 
ATOM   8452  C  CE2 . PHE   B 2 951  ? 103.602 106.860 88.296  1.00 65.22  ? 951  PHE   A CE2 1 
ATOM   8453  C  CZ  . PHE   B 2 951  ? 103.196 106.831 86.980  1.00 66.99  ? 951  PHE   A CZ  1 
ATOM   8454  N  N   . SER   B 2 952  ? 109.052 110.750 86.974  1.00 52.94  ? 952  SER   A N   1 
ATOM   8455  C  CA  . SER   B 2 952  ? 109.929 111.909 86.942  1.00 44.00  ? 952  SER   A CA  1 
ATOM   8456  C  C   . SER   B 2 952  ? 109.297 112.983 86.072  1.00 50.56  ? 952  SER   A C   1 
ATOM   8457  O  O   . SER   B 2 952  ? 108.578 112.685 85.115  1.00 61.76  ? 952  SER   A O   1 
ATOM   8458  C  CB  . SER   B 2 952  ? 111.317 111.553 86.409  1.00 48.98  ? 952  SER   A CB  1 
ATOM   8459  O  OG  . SER   B 2 952  ? 111.947 110.590 87.235  1.00 56.57  ? 952  SER   A OG  1 
ATOM   8460  N  N   . LEU   B 2 953  ? 109.575 114.237 86.407  1.00 43.10  ? 953  LEU   A N   1 
ATOM   8461  C  CA  . LEU   B 2 953  ? 108.954 115.382 85.757  1.00 40.47  ? 953  LEU   A CA  1 
ATOM   8462  C  C   . LEU   B 2 953  ? 110.002 116.146 84.961  1.00 46.95  ? 953  LEU   A C   1 
ATOM   8463  O  O   . LEU   B 2 953  ? 111.070 116.473 85.488  1.00 51.64  ? 953  LEU   A O   1 
ATOM   8464  C  CB  . LEU   B 2 953  ? 108.292 116.295 86.787  1.00 41.62  ? 953  LEU   A CB  1 
ATOM   8465  C  CG  . LEU   B 2 953  ? 107.562 117.526 86.255  1.00 39.87  ? 953  LEU   A CG  1 
ATOM   8466  C  CD1 . LEU   B 2 953  ? 106.363 117.110 85.433  1.00 50.64  ? 953  LEU   A CD1 1 
ATOM   8467  C  CD2 . LEU   B 2 953  ? 107.140 118.427 87.397  1.00 42.80  ? 953  LEU   A CD2 1 
ATOM   8468  N  N   . VAL   B 2 954  ? 109.697 116.421 83.698  1.00 47.95  ? 954  VAL   A N   1 
ATOM   8469  C  CA  . VAL   B 2 954  ? 110.515 117.276 82.847  1.00 35.80  ? 954  VAL   A CA  1 
ATOM   8470  C  C   . VAL   B 2 954  ? 109.642 118.434 82.388  1.00 43.74  ? 954  VAL   A C   1 
ATOM   8471  O  O   . VAL   B 2 954  ? 108.631 118.224 81.708  1.00 54.84  ? 954  VAL   A O   1 
ATOM   8472  C  CB  . VAL   B 2 954  ? 111.090 116.506 81.651  1.00 37.87  ? 954  VAL   A CB  1 
ATOM   8473  C  CG1 . VAL   B 2 954  ? 112.002 117.401 80.841  1.00 44.84  ? 954  VAL   A CG1 1 
ATOM   8474  C  CG2 . VAL   B 2 954  ? 111.838 115.278 82.125  1.00 45.73  ? 954  VAL   A CG2 1 
ATOM   8475  N  N   . ILE   B 2 955  ? 110.029 119.653 82.753  1.00 48.01  ? 955  ILE   A N   1 
ATOM   8476  C  CA  . ILE   B 2 955  ? 109.228 120.837 82.478  1.00 43.97  ? 955  ILE   A CA  1 
ATOM   8477  C  C   . ILE   B 2 955  ? 110.122 121.922 81.894  1.00 51.69  ? 955  ILE   A C   1 
ATOM   8478  O  O   . ILE   B 2 955  ? 111.269 122.103 82.315  1.00 63.10  ? 955  ILE   A O   1 
ATOM   8479  C  CB  . ILE   B 2 955  ? 108.496 121.327 83.750  1.00 48.30  ? 955  ILE   A CB  1 
ATOM   8480  C  CG1 . ILE   B 2 955  ? 107.572 122.500 83.434  1.00 55.29  ? 955  ILE   A CG1 1 
ATOM   8481  C  CG2 . ILE   B 2 955  ? 109.484 121.693 84.845  1.00 54.03  ? 955  ILE   A CG2 1 
ATOM   8482  C  CD1 . ILE   B 2 955  ? 106.688 122.899 84.591  1.00 56.75  ? 955  ILE   A CD1 1 
ATOM   8483  N  N   . GLU   B 2 956  ? 109.596 122.634 80.903  1.00 58.63  ? 956  GLU   A N   1 
ATOM   8484  C  CA  . GLU   B 2 956  ? 110.325 123.692 80.220  1.00 54.44  ? 956  GLU   A CA  1 
ATOM   8485  C  C   . GLU   B 2 956  ? 110.119 125.036 80.914  1.00 65.02  ? 956  GLU   A C   1 
ATOM   8486  O  O   . GLU   B 2 956  ? 109.355 125.164 81.872  1.00 68.00  ? 956  GLU   A O   1 
ATOM   8487  C  CB  . GLU   B 2 956  ? 109.895 123.783 78.753  1.00 54.65  ? 956  GLU   A CB  1 
ATOM   8488  C  CG  . GLU   B 2 956  ? 110.269 122.574 77.915  1.00 65.67  ? 956  GLU   A CG  1 
ATOM   8489  C  CD  . GLU   B 2 956  ? 109.974 122.772 76.441  1.00 74.07  ? 956  GLU   A CD  1 
ATOM   8490  O  OE1 . GLU   B 2 956  ? 109.472 123.854 76.072  1.00 73.61  ? 956  GLU   A OE1 1 
ATOM   8491  O  OE2 . GLU   B 2 956  ? 110.245 121.843 75.650  1.00 74.69  ? 956  GLU   A OE2 1 
ATOM   8492  N  N   . GLY   B 2 957  ? 110.831 126.047 80.412  1.00 60.31  ? 957  GLY   A N   1 
ATOM   8493  C  CA  . GLY   B 2 957  ? 110.780 127.363 81.031  1.00 54.18  ? 957  GLY   A CA  1 
ATOM   8494  C  C   . GLY   B 2 957  ? 109.446 128.067 80.866  1.00 60.28  ? 957  GLY   A C   1 
ATOM   8495  O  O   . GLY   B 2 957  ? 108.966 128.724 81.794  1.00 66.17  ? 957  GLY   A O   1 
ATOM   8496  N  N   . HIS   B 2 958  ? 108.839 127.964 79.681  1.00 60.46  ? 958  HIS   A N   1 
ATOM   8497  C  CA  . HIS   B 2 958  ? 107.559 128.630 79.448  1.00 59.77  ? 958  HIS   A CA  1 
ATOM   8498  C  C   . HIS   B 2 958  ? 106.460 128.050 80.328  1.00 64.07  ? 958  HIS   A C   1 
ATOM   8499  O  O   . HIS   B 2 958  ? 105.621 128.791 80.861  1.00 70.93  ? 958  HIS   A O   1 
ATOM   8500  C  CB  . HIS   B 2 958  ? 107.176 128.533 77.973  1.00 59.66  ? 958  HIS   A CB  1 
ATOM   8501  C  CG  . HIS   B 2 958  ? 107.968 129.438 77.083  1.00 68.18  ? 958  HIS   A CG  1 
ATOM   8502  N  ND1 . HIS   B 2 958  ? 109.256 129.151 76.684  1.00 70.55  ? 958  HIS   A ND1 1 
ATOM   8503  C  CD2 . HIS   B 2 958  ? 107.658 130.629 76.520  1.00 67.66  ? 958  HIS   A CD2 1 
ATOM   8504  C  CE1 . HIS   B 2 958  ? 109.703 130.124 75.911  1.00 67.54  ? 958  HIS   A CE1 1 
ATOM   8505  N  NE2 . HIS   B 2 958  ? 108.753 131.034 75.796  1.00 69.35  ? 958  HIS   A NE2 1 
ATOM   8506  N  N   . ALA   B 2 959  ? 106.443 126.726 80.487  1.00 56.91  ? 959  ALA   A N   1 
ATOM   8507  C  CA  . ALA   B 2 959  ? 105.474 126.108 81.382  1.00 59.03  ? 959  ALA   A CA  1 
ATOM   8508  C  C   . ALA   B 2 959  ? 105.679 126.582 82.814  1.00 61.10  ? 959  ALA   A C   1 
ATOM   8509  O  O   . ALA   B 2 959  ? 104.708 126.840 83.534  1.00 65.45  ? 959  ALA   A O   1 
ATOM   8510  C  CB  . ALA   B 2 959  ? 105.573 124.587 81.294  1.00 62.93  ? 959  ALA   A CB  1 
ATOM   8511  N  N   . LEU   B 2 960  ? 106.936 126.710 83.243  1.00 59.59  ? 960  LEU   A N   1 
ATOM   8512  C  CA  . LEU   B 2 960  ? 107.212 127.230 84.577  1.00 60.41  ? 960  LEU   A CA  1 
ATOM   8513  C  C   . LEU   B 2 960  ? 106.732 128.668 84.722  1.00 64.34  ? 960  LEU   A C   1 
ATOM   8514  O  O   . LEU   B 2 960  ? 106.223 129.055 85.780  1.00 69.17  ? 960  LEU   A O   1 
ATOM   8515  C  CB  . LEU   B 2 960  ? 108.705 127.134 84.882  1.00 59.39  ? 960  LEU   A CB  1 
ATOM   8516  C  CG  . LEU   B 2 960  ? 109.229 125.756 85.273  1.00 59.04  ? 960  LEU   A CG  1 
ATOM   8517  C  CD1 . LEU   B 2 960  ? 110.738 125.772 85.338  1.00 62.53  ? 960  LEU   A CD1 1 
ATOM   8518  C  CD2 . LEU   B 2 960  ? 108.645 125.332 86.603  1.00 60.06  ? 960  LEU   A CD2 1 
ATOM   8519  N  N   . ALA   B 2 961  ? 106.906 129.480 83.679  1.00 55.16  ? 961  ALA   A N   1 
ATOM   8520  C  CA  . ALA   B 2 961  ? 106.428 130.857 83.732  1.00 55.58  ? 961  ALA   A CA  1 
ATOM   8521  C  C   . ALA   B 2 961  ? 104.916 130.898 83.892  1.00 58.33  ? 961  ALA   A C   1 
ATOM   8522  O  O   . ALA   B 2 961  ? 104.383 131.658 84.710  1.00 65.80  ? 961  ALA   A O   1 
ATOM   8523  C  CB  . ALA   B 2 961  ? 106.859 131.614 82.477  1.00 56.47  ? 961  ALA   A CB  1 
ATOM   8524  N  N   . HIS   B 2 962  ? 104.206 130.071 83.123  1.00 58.67  ? 962  HIS   A N   1 
ATOM   8525  C  CA  . HIS   B 2 962  ? 102.752 130.029 83.248  1.00 54.48  ? 962  HIS   A CA  1 
ATOM   8526  C  C   . HIS   B 2 962  ? 102.332 129.512 84.618  1.00 59.76  ? 962  HIS   A C   1 
ATOM   8527  O  O   . HIS   B 2 962  ? 101.311 129.942 85.164  1.00 67.28  ? 962  HIS   A O   1 
ATOM   8528  C  CB  . HIS   B 2 962  ? 102.145 129.176 82.136  1.00 57.99  ? 962  HIS   A CB  1 
ATOM   8529  C  CG  . HIS   B 2 962  ? 102.240 129.798 80.778  1.00 64.29  ? 962  HIS   A CG  1 
ATOM   8530  N  ND1 . HIS   B 2 962  ? 101.409 129.444 79.738  1.00 65.17  ? 962  HIS   A ND1 1 
ATOM   8531  C  CD2 . HIS   B 2 962  ? 103.070 130.749 80.288  1.00 67.21  ? 962  HIS   A CD2 1 
ATOM   8532  C  CE1 . HIS   B 2 962  ? 101.723 130.149 78.666  1.00 65.50  ? 962  HIS   A CE1 1 
ATOM   8533  N  NE2 . HIS   B 2 962  ? 102.728 130.948 78.973  1.00 61.56  ? 962  HIS   A NE2 1 
ATOM   8534  N  N   . CYS   B 2 963  ? 103.103 128.582 85.187  1.00 66.44  ? 963  CYS   A N   1 
ATOM   8535  C  CA  . CYS   B 2 963  ? 102.804 128.087 86.529  1.00 63.89  ? 963  CYS   A CA  1 
ATOM   8536  C  C   . CYS   B 2 963  ? 102.964 129.187 87.569  1.00 66.90  ? 963  CYS   A C   1 
ATOM   8537  O  O   . CYS   B 2 963  ? 102.101 129.371 88.436  1.00 72.49  ? 963  CYS   A O   1 
ATOM   8538  C  CB  . CYS   B 2 963  ? 103.708 126.902 86.869  1.00 65.36  ? 963  CYS   A CB  1 
ATOM   8539  S  SG  . CYS   B 2 963  ? 103.375 125.388 85.949  1.00 80.89  ? 963  CYS   A SG  1 
ATOM   8540  N  N   . PHE   B 2 964  ? 104.066 129.931 87.499  1.00 60.54  ? 964  PHE   A N   1 
ATOM   8541  C  CA  . PHE   B 2 964  ? 104.351 130.975 88.474  1.00 61.78  ? 964  PHE   A CA  1 
ATOM   8542  C  C   . PHE   B 2 964  ? 103.484 132.214 88.299  1.00 63.78  ? 964  PHE   A C   1 
ATOM   8543  O  O   . PHE   B 2 964  ? 103.358 132.994 89.248  1.00 65.01  ? 964  PHE   A O   1 
ATOM   8544  C  CB  . PHE   B 2 964  ? 105.826 131.372 88.401  1.00 57.76  ? 964  PHE   A CB  1 
ATOM   8545  C  CG  . PHE   B 2 964  ? 106.765 130.288 88.835  1.00 57.13  ? 964  PHE   A CG  1 
ATOM   8546  C  CD1 . PHE   B 2 964  ? 106.463 129.488 89.920  1.00 59.91  ? 964  PHE   A CD1 1 
ATOM   8547  C  CD2 . PHE   B 2 964  ? 107.945 130.063 88.153  1.00 60.22  ? 964  PHE   A CD2 1 
ATOM   8548  C  CE1 . PHE   B 2 964  ? 107.324 128.488 90.319  1.00 61.35  ? 964  PHE   A CE1 1 
ATOM   8549  C  CE2 . PHE   B 2 964  ? 108.806 129.064 88.548  1.00 62.00  ? 964  PHE   A CE2 1 
ATOM   8550  C  CZ  . PHE   B 2 964  ? 108.495 128.276 89.632  1.00 60.89  ? 964  PHE   A CZ  1 
ATOM   8551  N  N   . ASP   B 2 965  ? 102.894 132.420 87.118  1.00 72.76  ? 965  ASP   A N   1 
ATOM   8552  C  CA  . ASP   B 2 965  ? 102.037 133.585 86.921  1.00 72.12  ? 965  ASP   A CA  1 
ATOM   8553  C  C   . ASP   B 2 965  ? 100.816 133.542 87.833  1.00 74.01  ? 965  ASP   A C   1 
ATOM   8554  O  O   . ASP   B 2 965  ? 100.433 134.563 88.415  1.00 76.22  ? 965  ASP   A O   1 
ATOM   8555  C  CB  . ASP   B 2 965  ? 101.609 133.685 85.457  1.00 72.61  ? 965  ASP   A CB  1 
ATOM   8556  C  CG  . ASP   B 2 965  ? 102.722 134.180 84.557  1.00 75.35  ? 965  ASP   A CG  1 
ATOM   8557  O  OD1 . ASP   B 2 965  ? 103.810 134.500 85.078  1.00 76.79  ? 965  ASP   A OD1 1 
ATOM   8558  O  OD2 . ASP   B 2 965  ? 102.510 134.248 83.328  1.00 75.01  ? 965  ASP   A OD2 1 
ATOM   8559  N  N   . ASP   B 2 966  ? 100.194 132.376 87.972  1.00 74.49  ? 966  ASP   A N   1 
ATOM   8560  C  CA  . ASP   B 2 966  ? 99.007  132.209 88.796  1.00 72.49  ? 966  ASP   A CA  1 
ATOM   8561  C  C   . ASP   B 2 966  ? 99.332  131.333 90.006  1.00 74.41  ? 966  ASP   A C   1 
ATOM   8562  O  O   . ASP   B 2 966  ? 100.487 130.961 90.240  1.00 75.19  ? 966  ASP   A O   1 
ATOM   8563  C  CB  . ASP   B 2 966  ? 97.865  131.630 87.960  1.00 73.82  ? 966  ASP   A CB  1 
ATOM   8564  C  CG  . ASP   B 2 966  ? 98.215  130.296 87.343  1.00 79.46  ? 966  ASP   A CG  1 
ATOM   8565  O  OD1 . ASP   B 2 966  ? 99.420  130.023 87.170  1.00 82.14  ? 966  ASP   A OD1 1 
ATOM   8566  O  OD2 . ASP   B 2 966  ? 97.288  129.521 87.029  1.00 79.16  ? 966  ASP   A OD2 1 
ATOM   8567  N  N   . GLU   B 2 967  ? 98.300  131.003 90.783  1.00 78.85  ? 967  GLU   A N   1 
ATOM   8568  C  CA  . GLU   B 2 967  ? 98.467  130.265 92.030  1.00 80.67  ? 967  GLU   A CA  1 
ATOM   8569  C  C   . GLU   B 2 967  ? 97.968  128.828 91.960  1.00 80.15  ? 967  GLU   A C   1 
ATOM   8570  O  O   . GLU   B 2 967  ? 98.594  127.937 92.539  1.00 83.48  ? 967  GLU   A O   1 
ATOM   8571  C  CB  . GLU   B 2 967  ? 97.752  130.991 93.172  1.00 80.14  ? 967  GLU   A CB  1 
ATOM   8572  C  CG  . GLU   B 2 967  ? 98.341  132.351 93.504  1.00 82.22  ? 967  GLU   A CG  1 
ATOM   8573  C  CD  . GLU   B 2 967  ? 99.744  132.259 94.074  1.00 84.02  ? 967  GLU   A CD  1 
ATOM   8574  O  OE1 . GLU   B 2 967  ? 100.093 131.201 94.639  1.00 82.61  ? 967  GLU   A OE1 1 
ATOM   8575  O  OE2 . GLU   B 2 967  ? 100.500 133.247 93.957  1.00 83.97  ? 967  GLU   A OE2 1 
ATOM   8576  N  N   . GLU   B 2 968  ? 96.847  128.581 91.280  1.00 79.47  ? 968  GLU   A N   1 
ATOM   8577  C  CA  . GLU   B 2 968  ? 96.345  127.215 91.161  1.00 77.79  ? 968  GLU   A CA  1 
ATOM   8578  C  C   . GLU   B 2 968  ? 97.326  126.330 90.402  1.00 81.75  ? 968  GLU   A C   1 
ATOM   8579  O  O   . GLU   B 2 968  ? 97.605  125.195 90.816  1.00 86.78  ? 968  GLU   A O   1 
ATOM   8580  C  CB  . GLU   B 2 968  ? 94.978  127.225 90.478  1.00 77.11  ? 968  GLU   A CB  1 
ATOM   8581  C  CG  . GLU   B 2 968  ? 94.413  125.850 90.164  1.00 84.23  ? 968  GLU   A CG  1 
ATOM   8582  C  CD  . GLU   B 2 968  ? 94.668  125.425 88.730  1.00 87.48  ? 968  GLU   A CD  1 
ATOM   8583  O  OE1 . GLU   B 2 968  ? 95.377  126.155 88.006  1.00 87.23  ? 968  GLU   A OE1 1 
ATOM   8584  O  OE2 . GLU   B 2 968  ? 94.153  124.361 88.325  1.00 85.81  ? 968  GLU   A OE2 1 
ATOM   8585  N  N   . THR   B 2 969  ? 97.866  126.837 89.293  1.00 69.79  ? 969  THR   A N   1 
ATOM   8586  C  CA  . THR   B 2 969  ? 98.860  126.079 88.545  1.00 67.42  ? 969  THR   A CA  1 
ATOM   8587  C  C   . THR   B 2 969  ? 100.125 125.880 89.368  1.00 71.71  ? 969  THR   A C   1 
ATOM   8588  O  O   . THR   B 2 969  ? 100.774 124.833 89.276  1.00 79.88  ? 969  THR   A O   1 
ATOM   8589  C  CB  . THR   B 2 969  ? 99.179  126.784 87.229  1.00 66.73  ? 969  THR   A CB  1 
ATOM   8590  O  OG1 . THR   B 2 969  ? 97.961  127.232 86.623  1.00 69.92  ? 969  THR   A OG1 1 
ATOM   8591  C  CG2 . THR   B 2 969  ? 99.877  125.835 86.278  1.00 68.53  ? 969  THR   A CG2 1 
ATOM   8592  N  N   . GLU   B 2 970  ? 100.487 126.872 90.184  1.00 66.97  ? 970  GLU   A N   1 
ATOM   8593  C  CA  . GLU   B 2 970  ? 101.649 126.726 91.054  1.00 63.17  ? 970  GLU   A CA  1 
ATOM   8594  C  C   . GLU   B 2 970  ? 101.433 125.624 92.083  1.00 67.39  ? 970  GLU   A C   1 
ATOM   8595  O  O   . GLU   B 2 970  ? 102.345 124.836 92.360  1.00 74.71  ? 970  GLU   A O   1 
ATOM   8596  C  CB  . GLU   B 2 970  ? 101.959 128.051 91.745  1.00 66.41  ? 970  GLU   A CB  1 
ATOM   8597  C  CG  . GLU   B 2 970  ? 103.151 127.996 92.680  1.00 70.25  ? 970  GLU   A CG  1 
ATOM   8598  C  CD  . GLU   B 2 970  ? 103.506 129.354 93.250  1.00 75.04  ? 970  GLU   A CD  1 
ATOM   8599  O  OE1 . GLU   B 2 970  ? 102.779 130.329 92.964  1.00 75.15  ? 970  GLU   A OE1 1 
ATOM   8600  O  OE2 . GLU   B 2 970  ? 104.512 129.448 93.983  1.00 76.01  ? 970  GLU   A OE2 1 
ATOM   8601  N  N   . ALA   B 2 971  ? 100.233 125.553 92.662  1.00 69.79  ? 971  ALA   A N   1 
ATOM   8602  C  CA  . ALA   B 2 971  ? 99.938  124.490 93.617  1.00 71.11  ? 971  ALA   A CA  1 
ATOM   8603  C  C   . ALA   B 2 971  ? 99.961  123.123 92.947  1.00 71.64  ? 971  ALA   A C   1 
ATOM   8604  O  O   . ALA   B 2 971  ? 100.480 122.153 93.514  1.00 76.94  ? 971  ALA   A O   1 
ATOM   8605  C  CB  . ALA   B 2 971  ? 98.585  124.741 94.281  1.00 69.02  ? 971  ALA   A CB  1 
ATOM   8606  N  N   . LEU   B 2 972  ? 99.400  123.026 91.739  1.00 60.83  ? 972  LEU   A N   1 
ATOM   8607  C  CA  . LEU   B 2 972  ? 99.453  121.762 91.009  1.00 58.78  ? 972  LEU   A CA  1 
ATOM   8608  C  C   . LEU   B 2 972  ? 100.892 121.358 90.711  1.00 61.89  ? 972  LEU   A C   1 
ATOM   8609  O  O   . LEU   B 2 972  ? 101.261 120.184 90.853  1.00 71.32  ? 972  LEU   A O   1 
ATOM   8610  C  CB  . LEU   B 2 972  ? 98.648  121.864 89.716  1.00 60.38  ? 972  LEU   A CB  1 
ATOM   8611  C  CG  . LEU   B 2 972  ? 97.131  121.977 89.851  1.00 65.32  ? 972  LEU   A CG  1 
ATOM   8612  C  CD1 . LEU   B 2 972  ? 96.484  122.066 88.481  1.00 68.06  ? 972  LEU   A CD1 1 
ATOM   8613  C  CD2 . LEU   B 2 972  ? 96.581  120.798 90.625  1.00 67.52  ? 972  LEU   A CD2 1 
ATOM   8614  N  N   . LEU   B 2 973  ? 101.720 122.320 90.298  1.00 50.71  ? 973  LEU   A N   1 
ATOM   8615  C  CA  . LEU   B 2 973  ? 103.124 122.034 90.033  1.00 52.11  ? 973  LEU   A CA  1 
ATOM   8616  C  C   . LEU   B 2 973  ? 103.836 121.569 91.292  1.00 53.41  ? 973  LEU   A C   1 
ATOM   8617  O  O   . LEU   B 2 973  ? 104.638 120.630 91.247  1.00 65.85  ? 973  LEU   A O   1 
ATOM   8618  C  CB  . LEU   B 2 973  ? 103.815 123.269 89.461  1.00 55.36  ? 973  LEU   A CB  1 
ATOM   8619  C  CG  . LEU   B 2 973  ? 105.330 123.169 89.293  1.00 52.29  ? 973  LEU   A CG  1 
ATOM   8620  C  CD1 . LEU   B 2 973  ? 105.679 122.141 88.238  1.00 56.22  ? 973  LEU   A CD1 1 
ATOM   8621  C  CD2 . LEU   B 2 973  ? 105.922 124.518 88.944  1.00 56.95  ? 973  LEU   A CD2 1 
ATOM   8622  N  N   . LEU   B 2 974  ? 103.562 122.217 92.424  1.00 47.74  ? 974  LEU   A N   1 
ATOM   8623  C  CA  . LEU   B 2 974  ? 104.187 121.808 93.675  1.00 44.87  ? 974  LEU   A CA  1 
ATOM   8624  C  C   . LEU   B 2 974  ? 103.788 120.390 94.052  1.00 52.78  ? 974  LEU   A C   1 
ATOM   8625  O  O   . LEU   B 2 974  ? 104.637 119.586 94.454  1.00 63.57  ? 974  LEU   A O   1 
ATOM   8626  C  CB  . LEU   B 2 974  ? 103.813 122.779 94.791  1.00 48.32  ? 974  LEU   A CB  1 
ATOM   8627  C  CG  . LEU   B 2 974  ? 104.276 122.362 96.185  1.00 54.68  ? 974  LEU   A CG  1 
ATOM   8628  C  CD1 . LEU   B 2 974  ? 105.743 122.690 96.387  1.00 59.90  ? 974  LEU   A CD1 1 
ATOM   8629  C  CD2 . LEU   B 2 974  ? 103.412 123.010 97.252  1.00 56.90  ? 974  LEU   A CD2 1 
ATOM   8630  N  N   . ALA   B 2 975  ? 102.501 120.063 93.922  1.00 55.28  ? 975  ALA   A N   1 
ATOM   8631  C  CA  . ALA   B 2 975  ? 102.045 118.715 94.249  1.00 53.78  ? 975  ALA   A CA  1 
ATOM   8632  C  C   . ALA   B 2 975  ? 102.714 117.677 93.355  1.00 53.27  ? 975  ALA   A C   1 
ATOM   8633  O  O   . ALA   B 2 975  ? 103.226 116.659 93.840  1.00 62.25  ? 975  ALA   A O   1 
ATOM   8634  C  CB  . ALA   B 2 975  ? 100.525 118.634 94.129  1.00 57.08  ? 975  ALA   A CB  1 
ATOM   8635  N  N   . LEU   B 2 976  ? 102.743 117.931 92.045  1.00 44.59  ? 976  LEU   A N   1 
ATOM   8636  C  CA  . LEU   B 2 976  ? 103.344 116.970 91.126  1.00 46.41  ? 976  LEU   A CA  1 
ATOM   8637  C  C   . LEU   B 2 976  ? 104.841 116.821 91.373  1.00 50.27  ? 976  LEU   A C   1 
ATOM   8638  O  O   . LEU   B 2 976  ? 105.373 115.706 91.329  1.00 61.85  ? 976  LEU   A O   1 
ATOM   8639  C  CB  . LEU   B 2 976  ? 103.076 117.381 89.681  1.00 43.89  ? 976  LEU   A CB  1 
ATOM   8640  C  CG  . LEU   B 2 976  ? 103.502 116.364 88.625  1.00 45.02  ? 976  LEU   A CG  1 
ATOM   8641  C  CD1 . LEU   B 2 976  ? 102.856 115.023 88.897  1.00 51.51  ? 976  LEU   A CD1 1 
ATOM   8642  C  CD2 . LEU   B 2 976  ? 103.143 116.851 87.237  1.00 52.03  ? 976  LEU   A CD2 1 
ATOM   8643  N  N   . SER   B 2 977  ? 105.538 117.928 91.637  1.00 36.25  ? 977  SER   A N   1 
ATOM   8644  C  CA  . SER   B 2 977  ? 106.979 117.867 91.848  1.00 37.15  ? 977  SER   A CA  1 
ATOM   8645  C  C   . SER   B 2 977  ? 107.323 117.165 93.153  1.00 44.34  ? 977  SER   A C   1 
ATOM   8646  O  O   . SER   B 2 977  ? 108.296 116.405 93.216  1.00 52.06  ? 977  SER   A O   1 
ATOM   8647  C  CB  . SER   B 2 977  ? 107.569 119.274 91.824  1.00 44.92  ? 977  SER   A CB  1 
ATOM   8648  O  OG  . SER   B 2 977  ? 107.013 120.075 92.851  1.00 53.12  ? 977  SER   A OG  1 
ATOM   8649  N  N   . THR   B 2 978  ? 106.545 117.410 94.209  1.00 47.46  ? 978  THR   A N   1 
ATOM   8650  C  CA  . THR   B 2 978  ? 106.783 116.723 95.471  1.00 50.42  ? 978  THR   A CA  1 
ATOM   8651  C  C   . THR   B 2 978  ? 106.456 115.240 95.367  1.00 53.04  ? 978  THR   A C   1 
ATOM   8652  O  O   . THR   B 2 978  ? 107.109 114.415 96.016  1.00 50.79  ? 978  THR   A O   1 
ATOM   8653  C  CB  . THR   B 2 978  ? 105.962 117.375 96.583  1.00 51.29  ? 978  THR   A CB  1 
ATOM   8654  O  OG1 . THR   B 2 978  ? 106.210 118.786 96.591  1.00 53.68  ? 978  THR   A OG1 1 
ATOM   8655  C  CG2 . THR   B 2 978  ? 106.339 116.799 97.941  1.00 54.64  ? 978  THR   A CG2 1 
ATOM   8656  N  N   . ARG   B 2 979  ? 105.469 114.878 94.551  1.00 57.30  ? 979  ARG   A N   1 
ATOM   8657  C  CA  . ARG   B 2 979  ? 105.096 113.479 94.401  1.00 54.74  ? 979  ARG   A CA  1 
ATOM   8658  C  C   . ARG   B 2 979  ? 105.978 112.725 93.413  1.00 56.22  ? 979  ARG   A C   1 
ATOM   8659  O  O   . ARG   B 2 979  ? 105.804 111.513 93.258  1.00 57.63  ? 979  ARG   A O   1 
ATOM   8660  C  CB  . ARG   B 2 979  ? 103.632 113.381 93.971  1.00 60.70  ? 979  ARG   A CB  1 
ATOM   8661  C  CG  . ARG   B 2 979  ? 102.848 112.311 94.701  1.00 62.87  ? 979  ARG   A CG  1 
ATOM   8662  C  CD  . ARG   B 2 979  ? 101.360 112.584 94.618  1.00 62.38  ? 979  ARG   A CD  1 
ATOM   8663  N  NE  . ARG   B 2 979  ? 101.040 113.932 95.068  1.00 56.72  ? 979  ARG   A NE  1 
ATOM   8664  C  CZ  . ARG   B 2 979  ? 100.841 114.271 96.334  1.00 58.44  ? 979  ARG   A CZ  1 
ATOM   8665  N  NH1 . ARG   B 2 979  ? 100.917 113.379 97.308  1.00 62.05  ? 979  ARG   A NH1 1 
ATOM   8666  N  NH2 . ARG   B 2 979  ? 100.558 115.536 96.630  1.00 63.59  ? 979  ARG   A NH2 1 
ATOM   8667  N  N   . CYS   B 2 980  ? 106.911 113.398 92.751  1.00 57.81  ? 980  CYS   A N   1 
ATOM   8668  C  CA  . CYS   B 2 980  ? 107.802 112.769 91.788  1.00 50.41  ? 980  CYS   A CA  1 
ATOM   8669  C  C   . CYS   B 2 980  ? 109.192 112.567 92.381  1.00 57.43  ? 980  CYS   A C   1 
ATOM   8670  O  O   . CYS   B 2 980  ? 109.573 113.198 93.369  1.00 63.32  ? 980  CYS   A O   1 
ATOM   8671  C  CB  . CYS   B 2 980  ? 107.897 113.605 90.510  1.00 48.99  ? 980  CYS   A CB  1 
ATOM   8672  S  SG  . CYS   B 2 980  ? 106.467 113.461 89.418  1.00 76.10  ? 980  CYS   A SG  1 
ATOM   8673  N  N   . ASN   B 2 981  ? 109.949 111.667 91.756  1.00 59.31  ? 981  ASN   A N   1 
ATOM   8674  C  CA  . ASN   B 2 981  ? 111.297 111.348 92.209  1.00 55.02  ? 981  ASN   A CA  1 
ATOM   8675  C  C   . ASN   B 2 981  ? 112.236 112.525 91.992  1.00 60.40  ? 981  ASN   A C   1 
ATOM   8676  O  O   . ASN   B 2 981  ? 112.805 113.060 92.949  1.00 67.85  ? 981  ASN   A O   1 
ATOM   8677  C  CB  . ASN   B 2 981  ? 111.829 110.113 91.480  1.00 57.04  ? 981  ASN   A CB  1 
ATOM   8678  C  CG  . ASN   B 2 981  ? 110.977 108.883 91.718  1.00 66.16  ? 981  ASN   A CG  1 
ATOM   8679  O  OD1 . ASN   B 2 981  ? 110.349 108.741 92.767  1.00 67.05  ? 981  ASN   A OD1 1 
ATOM   8680  N  ND2 . ASN   B 2 981  ? 110.951 107.984 90.741  1.00 66.64  ? 981  ASN   A ND2 1 
ATOM   8681  N  N   . THR   B 2 982  ? 112.402 112.934 90.739  1.00 52.91  ? 982  THR   A N   1 
ATOM   8682  C  CA  . THR   B 2 982  ? 113.254 114.057 90.388  1.00 53.56  ? 982  THR   A CA  1 
ATOM   8683  C  C   . THR   B 2 982  ? 112.558 114.914 89.343  1.00 53.63  ? 982  THR   A C   1 
ATOM   8684  O  O   . THR   B 2 982  ? 111.743 114.425 88.557  1.00 55.42  ? 982  THR   A O   1 
ATOM   8685  C  CB  . THR   B 2 982  ? 114.611 113.588 89.859  1.00 47.59  ? 982  THR   A CB  1 
ATOM   8686  O  OG1 . THR   B 2 982  ? 115.335 114.706 89.333  1.00 57.28  ? 982  THR   A OG1 1 
ATOM   8687  C  CG2 . THR   B 2 982  ? 114.422 112.552 88.768  1.00 45.03  ? 982  THR   A CG2 1 
ATOM   8688  N  N   . VAL   B 2 983  ? 112.887 116.202 89.344  1.00 45.20  ? 983  VAL   A N   1 
ATOM   8689  C  CA  . VAL   B 2 983  ? 112.327 117.166 88.406  1.00 34.36  ? 983  VAL   A CA  1 
ATOM   8690  C  C   . VAL   B 2 983  ? 113.469 117.773 87.607  1.00 44.14  ? 983  VAL   A C   1 
ATOM   8691  O  O   . VAL   B 2 983  ? 114.438 118.277 88.186  1.00 59.52  ? 983  VAL   A O   1 
ATOM   8692  C  CB  . VAL   B 2 983  ? 111.524 118.263 89.127  1.00 40.24  ? 983  VAL   A CB  1 
ATOM   8693  C  CG1 . VAL   B 2 983  ? 110.938 119.235 88.122  1.00 45.82  ? 983  VAL   A CG1 1 
ATOM   8694  C  CG2 . VAL   B 2 983  ? 110.429 117.644 89.972  1.00 49.93  ? 983  VAL   A CG2 1 
ATOM   8695  N  N   . ILE   B 2 984  ? 113.356 117.724 86.284  1.00 38.62  ? 984  ILE   A N   1 
ATOM   8696  C  CA  . ILE   B 2 984  ? 114.329 118.327 85.383  1.00 27.85  ? 984  ILE   A CA  1 
ATOM   8697  C  C   . ILE   B 2 984  ? 113.684 119.546 84.747  1.00 35.73  ? 984  ILE   A C   1 
ATOM   8698  O  O   . ILE   B 2 984  ? 112.675 119.429 84.040  1.00 48.38  ? 984  ILE   A O   1 
ATOM   8699  C  CB  . ILE   B 2 984  ? 114.810 117.335 84.313  1.00 35.02  ? 984  ILE   A CB  1 
ATOM   8700  C  CG1 . ILE   B 2 984  ? 115.743 116.294 84.929  1.00 39.25  ? 984  ILE   A CG1 1 
ATOM   8701  C  CG2 . ILE   B 2 984  ? 115.503 118.070 83.182  1.00 44.39  ? 984  ILE   A CG2 1 
ATOM   8702  C  CD1 . ILE   B 2 984  ? 116.467 115.453 83.909  1.00 38.60  ? 984  ILE   A CD1 1 
ATOM   8703  N  N   . CYS   B 2 985  ? 114.264 120.714 84.994  1.00 45.10  ? 985  CYS   A N   1 
ATOM   8704  C  CA  . CYS   B 2 985  ? 113.781 121.965 84.428  1.00 42.97  ? 985  CYS   A CA  1 
ATOM   8705  C  C   . CYS   B 2 985  ? 114.755 122.417 83.349  1.00 50.31  ? 985  CYS   A C   1 
ATOM   8706  O  O   . CYS   B 2 985  ? 115.936 122.646 83.631  1.00 60.36  ? 985  CYS   A O   1 
ATOM   8707  C  CB  . CYS   B 2 985  ? 113.632 123.029 85.513  1.00 50.72  ? 985  CYS   A CB  1 
ATOM   8708  S  SG  . CYS   B 2 985  ? 112.578 122.534 86.889  1.00 64.99  ? 985  CYS   A SG  1 
ATOM   8709  N  N   . CYS   B 2 986  ? 114.261 122.543 82.123  1.00 52.55  ? 986  CYS   A N   1 
ATOM   8710  C  CA  . CYS   B 2 986  ? 115.092 122.844 80.970  1.00 58.99  ? 986  CYS   A CA  1 
ATOM   8711  C  C   . CYS   B 2 986  ? 114.695 124.184 80.368  1.00 61.04  ? 986  CYS   A C   1 
ATOM   8712  O  O   . CYS   B 2 986  ? 113.515 124.548 80.346  1.00 65.21  ? 986  CYS   A O   1 
ATOM   8713  C  CB  . CYS   B 2 986  ? 114.984 121.743 79.913  1.00 63.16  ? 986  CYS   A CB  1 
ATOM   8714  S  SG  . CYS   B 2 986  ? 113.297 121.381 79.389  1.00 83.21  ? 986  CYS   A SG  1 
ATOM   8715  N  N   . ARG   B 2 987  ? 115.700 124.913 79.881  1.00 61.67  ? 987  ARG   A N   1 
ATOM   8716  C  CA  . ARG   B 2 987  ? 115.525 126.240 79.293  1.00 58.97  ? 987  ARG   A CA  1 
ATOM   8717  C  C   . ARG   B 2 987  ? 114.867 127.199 80.288  1.00 65.56  ? 987  ARG   A C   1 
ATOM   8718  O  O   . ARG   B 2 987  ? 113.770 127.713 80.069  1.00 70.65  ? 987  ARG   A O   1 
ATOM   8719  C  CB  . ARG   B 2 987  ? 114.731 126.166 77.986  1.00 56.35  ? 987  ARG   A CB  1 
ATOM   8720  C  CG  . ARG   B 2 987  ? 115.368 125.293 76.927  1.00 62.64  ? 987  ARG   A CG  1 
ATOM   8721  C  CD  . ARG   B 2 987  ? 114.960 125.729 75.533  1.00 63.85  ? 987  ARG   A CD  1 
ATOM   8722  N  NE  . ARG   B 2 987  ? 115.449 127.067 75.222  1.00 67.82  ? 987  ARG   A NE  1 
ATOM   8723  C  CZ  . ARG   B 2 987  ? 116.650 127.329 74.726  1.00 68.38  ? 987  ARG   A CZ  1 
ATOM   8724  N  NH1 . ARG   B 2 987  ? 117.519 126.365 74.475  1.00 64.43  ? 987  ARG   A NH1 1 
ATOM   8725  N  NH2 . ARG   B 2 987  ? 116.987 128.591 74.476  1.00 68.25  ? 987  ARG   A NH2 1 
ATOM   8726  N  N   . VAL   B 2 988  ? 115.569 127.437 81.392  1.00 53.50  ? 988  VAL   A N   1 
ATOM   8727  C  CA  . VAL   B 2 988  ? 115.083 128.285 82.472  1.00 43.00  ? 988  VAL   A CA  1 
ATOM   8728  C  C   . VAL   B 2 988  ? 116.017 129.478 82.620  1.00 53.14  ? 988  VAL   A C   1 
ATOM   8729  O  O   . VAL   B 2 988  ? 117.243 129.329 82.548  1.00 62.91  ? 988  VAL   A O   1 
ATOM   8730  C  CB  . VAL   B 2 988  ? 114.965 127.509 83.797  1.00 52.92  ? 988  VAL   A CB  1 
ATOM   8731  C  CG1 . VAL   B 2 988  ? 113.894 126.450 83.686  1.00 57.76  ? 988  VAL   A CG1 1 
ATOM   8732  C  CG2 . VAL   B 2 988  ? 116.291 126.871 84.171  1.00 54.77  ? 988  VAL   A CG2 1 
ATOM   8733  N  N   . SER   B 2 989  ? 115.435 130.658 82.801  1.00 52.92  ? 989  SER   A N   1 
ATOM   8734  C  CA  . SER   B 2 989  ? 116.195 131.861 83.086  1.00 44.72  ? 989  SER   A CA  1 
ATOM   8735  C  C   . SER   B 2 989  ? 116.675 131.853 84.534  1.00 51.04  ? 989  SER   A C   1 
ATOM   8736  O  O   . SER   B 2 989  ? 116.170 131.087 85.359  1.00 64.29  ? 989  SER   A O   1 
ATOM   8737  C  CB  . SER   B 2 989  ? 115.339 133.093 82.818  1.00 49.55  ? 989  SER   A CB  1 
ATOM   8738  O  OG  . SER   B 2 989  ? 114.181 133.098 83.633  1.00 56.06  ? 989  SER   A OG  1 
ATOM   8739  N  N   . PRO   B 2 990  ? 117.679 132.674 84.862  1.00 32.66  ? 990  PRO   A N   1 
ATOM   8740  C  CA  . PRO   B 2 990  ? 118.115 132.768 86.267  1.00 42.73  ? 990  PRO   A CA  1 
ATOM   8741  C  C   . PRO   B 2 990  ? 116.981 133.050 87.237  1.00 50.15  ? 990  PRO   A C   1 
ATOM   8742  O  O   . PRO   B 2 990  ? 116.896 132.434 88.314  1.00 57.79  ? 990  PRO   A O   1 
ATOM   8743  C  CB  . PRO   B 2 990  ? 119.118 133.928 86.237  1.00 43.97  ? 990  PRO   A CB  1 
ATOM   8744  C  CG  . PRO   B 2 990  ? 119.503 134.116 84.801  1.00 40.45  ? 990  PRO   A CG  1 
ATOM   8745  C  CD  . PRO   B 2 990  ? 118.666 133.244 83.933  1.00 36.03  ? 990  PRO   A CD  1 
ATOM   8746  N  N   . LEU   B 2 991  ? 116.091 133.970 86.867  1.00 49.31  ? 991  LEU   A N   1 
ATOM   8747  C  CA  . LEU   B 2 991  ? 114.962 134.291 87.726  1.00 48.37  ? 991  LEU   A CA  1 
ATOM   8748  C  C   . LEU   B 2 991  ? 114.054 133.088 87.913  1.00 50.92  ? 991  LEU   A C   1 
ATOM   8749  O  O   . LEU   B 2 991  ? 113.476 132.913 88.988  1.00 54.76  ? 991  LEU   A O   1 
ATOM   8750  C  CB  . LEU   B 2 991  ? 114.183 135.469 87.144  1.00 49.75  ? 991  LEU   A CB  1 
ATOM   8751  C  CG  . LEU   B 2 991  ? 115.022 136.705 86.815  1.00 49.47  ? 991  LEU   A CG  1 
ATOM   8752  C  CD1 . LEU   B 2 991  ? 114.142 137.820 86.280  1.00 52.24  ? 991  LEU   A CD1 1 
ATOM   8753  C  CD2 . LEU   B 2 991  ? 115.800 137.170 88.030  1.00 49.25  ? 991  LEU   A CD2 1 
ATOM   8754  N  N   . GLN   B 2 992  ? 113.931 132.237 86.894  1.00 41.73  ? 992  GLN   A N   1 
ATOM   8755  C  CA  . GLN   B 2 992  ? 113.106 131.044 87.039  1.00 38.73  ? 992  GLN   A CA  1 
ATOM   8756  C  C   . GLN   B 2 992  ? 113.755 130.027 87.971  1.00 49.84  ? 992  GLN   A C   1 
ATOM   8757  O  O   . GLN   B 2 992  ? 113.057 129.330 88.715  1.00 57.80  ? 992  GLN   A O   1 
ATOM   8758  C  CB  . GLN   B 2 992  ? 112.818 130.433 85.671  1.00 38.95  ? 992  GLN   A CB  1 
ATOM   8759  C  CG  . GLN   B 2 992  ? 111.763 131.191 84.890  1.00 37.32  ? 992  GLN   A CG  1 
ATOM   8760  C  CD  . GLN   B 2 992  ? 111.513 130.607 83.522  1.00 47.71  ? 992  GLN   A CD  1 
ATOM   8761  O  OE1 . GLN   B 2 992  ? 112.424 130.089 82.879  1.00 49.34  ? 992  GLN   A OE1 1 
ATOM   8762  N  NE2 . GLN   B 2 992  ? 110.271 130.685 83.066  1.00 53.93  ? 992  GLN   A NE2 1 
ATOM   8763  N  N   . LYS   B 2 993  ? 115.087 129.930 87.958  1.00 39.26  ? 993  LYS   A N   1 
ATOM   8764  C  CA  . LYS   B 2 993  ? 115.768 129.082 88.931  1.00 33.60  ? 993  LYS   A CA  1 
ATOM   8765  C  C   . LYS   B 2 993  ? 115.520 129.580 90.349  1.00 43.82  ? 993  LYS   A C   1 
ATOM   8766  O  O   . LYS   B 2 993  ? 115.209 128.795 91.260  1.00 52.62  ? 993  LYS   A O   1 
ATOM   8767  C  CB  . LYS   B 2 993  ? 117.267 129.039 88.637  1.00 43.39  ? 993  LYS   A CB  1 
ATOM   8768  C  CG  . LYS   B 2 993  ? 117.648 128.410 87.308  1.00 47.56  ? 993  LYS   A CG  1 
ATOM   8769  C  CD  . LYS   B 2 993  ? 119.159 128.340 87.169  1.00 37.19  ? 993  LYS   A CD  1 
ATOM   8770  C  CE  . LYS   B 2 993  ? 119.579 127.736 85.850  1.00 35.75  ? 993  LYS   A CE  1 
ATOM   8771  N  NZ  . LYS   B 2 993  ? 119.169 128.583 84.700  1.00 49.57  ? 993  LYS   A NZ  1 
ATOM   8772  N  N   . ALA   B 2 994  ? 115.645 130.894 90.551  1.00 48.22  ? 994  ALA   A N   1 
ATOM   8773  C  CA  . ALA   B 2 994  ? 115.349 131.468 91.858  1.00 43.06  ? 994  ALA   A CA  1 
ATOM   8774  C  C   . ALA   B 2 994  ? 113.901 131.215 92.249  1.00 47.47  ? 994  ALA   A C   1 
ATOM   8775  O  O   . ALA   B 2 994  ? 113.602 130.953 93.418  1.00 55.45  ? 994  ALA   A O   1 
ATOM   8776  C  CB  . ALA   B 2 994  ? 115.652 132.964 91.857  1.00 46.03  ? 994  ALA   A CB  1 
ATOM   8777  N  N   . GLN   B 2 995  ? 112.988 131.287 91.280  1.00 43.65  ? 995  GLN   A N   1 
ATOM   8778  C  CA  . GLN   B 2 995  ? 111.577 131.054 91.561  1.00 33.72  ? 995  GLN   A CA  1 
ATOM   8779  C  C   . GLN   B 2 995  ? 111.316 129.609 91.961  1.00 41.71  ? 995  GLN   A C   1 
ATOM   8780  O  O   . GLN   B 2 995  ? 110.500 129.351 92.847  1.00 53.87  ? 995  GLN   A O   1 
ATOM   8781  C  CB  . GLN   B 2 995  ? 110.733 131.443 90.351  1.00 37.04  ? 995  GLN   A CB  1 
ATOM   8782  C  CG  . GLN   B 2 995  ? 110.538 132.937 90.202  1.00 42.62  ? 995  GLN   A CG  1 
ATOM   8783  C  CD  . GLN   B 2 995  ? 109.791 133.305 88.941  1.00 46.34  ? 995  GLN   A CD  1 
ATOM   8784  O  OE1 . GLN   B 2 995  ? 109.786 132.553 87.968  1.00 46.75  ? 995  GLN   A OE1 1 
ATOM   8785  N  NE2 . GLN   B 2 995  ? 109.153 134.467 88.949  1.00 48.73  ? 995  GLN   A NE2 1 
ATOM   8786  N  N   . ILE   B 2 996  ? 111.991 128.653 91.322  1.00 46.84  ? 996  ILE   A N   1 
ATOM   8787  C  CA  . ILE   B 2 996  ? 111.846 127.249 91.712  1.00 46.99  ? 996  ILE   A CA  1 
ATOM   8788  C  C   . ILE   B 2 996  ? 112.337 127.043 93.140  1.00 52.56  ? 996  ILE   A C   1 
ATOM   8789  O  O   . ILE   B 2 996  ? 111.670 126.400 93.971  1.00 55.96  ? 996  ILE   A O   1 
ATOM   8790  C  CB  . ILE   B 2 996  ? 112.602 126.340 90.727  1.00 40.94  ? 996  ILE   A CB  1 
ATOM   8791  C  CG1 . ILE   B 2 996  ? 112.002 126.443 89.329  1.00 48.60  ? 996  ILE   A CG1 1 
ATOM   8792  C  CG2 . ILE   B 2 996  ? 112.580 124.902 91.206  1.00 48.82  ? 996  ILE   A CG2 1 
ATOM   8793  C  CD1 . ILE   B 2 996  ? 112.872 125.834 88.261  1.00 52.57  ? 996  ILE   A CD1 1 
ATOM   8794  N  N   . VAL   B 2 997  ? 113.519 127.588 93.443  1.00 44.53  ? 997  VAL   A N   1 
ATOM   8795  C  CA  . VAL   B 2 997  ? 114.076 127.442 94.784  1.00 39.88  ? 997  VAL   A CA  1 
ATOM   8796  C  C   . VAL   B 2 997  ? 113.143 128.058 95.817  1.00 48.95  ? 997  VAL   A C   1 
ATOM   8797  O  O   . VAL   B 2 997  ? 112.869 127.459 96.864  1.00 56.77  ? 997  VAL   A O   1 
ATOM   8798  C  CB  . VAL   B 2 997  ? 115.482 128.062 94.851  1.00 42.90  ? 997  VAL   A CB  1 
ATOM   8799  C  CG1 . VAL   B 2 997  ? 116.000 128.037 96.273  1.00 46.76  ? 997  VAL   A CG1 1 
ATOM   8800  C  CG2 . VAL   B 2 997  ? 116.427 127.320 93.929  1.00 44.88  ? 997  VAL   A CG2 1 
ATOM   8801  N  N   . HIS   B 2 998  ? 112.632 129.259 95.534  1.00 51.08  ? 998  HIS   A N   1 
ATOM   8802  C  CA  . HIS   B 2 998  ? 111.720 129.920 96.460  1.00 47.16  ? 998  HIS   A CA  1 
ATOM   8803  C  C   . HIS   B 2 998  ? 110.412 129.155 96.594  1.00 45.73  ? 998  HIS   A C   1 
ATOM   8804  O  O   . HIS   B 2 998  ? 109.852 129.075 97.690  1.00 56.67  ? 998  HIS   A O   1 
ATOM   8805  C  CB  . HIS   B 2 998  ? 111.463 131.357 96.011  1.00 47.60  ? 998  HIS   A CB  1 
ATOM   8806  C  CG  . HIS   B 2 998  ? 112.551 132.310 96.392  1.00 49.93  ? 998  HIS   A CG  1 
ATOM   8807  N  ND1 . HIS   B 2 998  ? 113.294 132.167 97.544  1.00 52.31  ? 998  HIS   A ND1 1 
ATOM   8808  C  CD2 . HIS   B 2 998  ? 113.025 133.417 95.774  1.00 52.02  ? 998  HIS   A CD2 1 
ATOM   8809  C  CE1 . HIS   B 2 998  ? 114.177 133.146 97.621  1.00 57.63  ? 998  HIS   A CE1 1 
ATOM   8810  N  NE2 . HIS   B 2 998  ? 114.036 133.918 96.558  1.00 56.64  ? 998  HIS   A NE2 1 
ATOM   8811  N  N   . LEU   B 2 999  ? 109.910 128.588 95.496  1.00 35.88  ? 999  LEU   A N   1 
ATOM   8812  C  CA  . LEU   B 2 999  ? 108.696 127.786 95.561  1.00 42.03  ? 999  LEU   A CA  1 
ATOM   8813  C  C   . LEU   B 2 999  ? 108.853 126.653 96.559  1.00 45.82  ? 999  LEU   A C   1 
ATOM   8814  O  O   . LEU   B 2 999  ? 108.035 126.498 97.476  1.00 57.54  ? 999  LEU   A O   1 
ATOM   8815  C  CB  . LEU   B 2 999  ? 108.360 127.231 94.178  1.00 47.22  ? 999  LEU   A CB  1 
ATOM   8816  C  CG  . LEU   B 2 999  ? 107.409 126.033 94.149  1.00 47.16  ? 999  LEU   A CG  1 
ATOM   8817  C  CD1 . LEU   B 2 999  ? 105.997 126.459 94.500  1.00 46.79  ? 999  LEU   A CD1 1 
ATOM   8818  C  CD2 . LEU   B 2 999  ? 107.443 125.343 92.798  1.00 45.64  ? 999  LEU   A CD2 1 
ATOM   8819  N  N   . ILE   B 2 1000 ? 109.921 125.867 96.416  1.00 47.18  ? 1000 ILE   A N   1 
ATOM   8820  C  CA  . ILE   B 2 1000 ? 110.124 124.753 97.341  1.00 44.29  ? 1000 ILE   A CA  1 
ATOM   8821  C  C   . ILE   B 2 1000 ? 110.323 125.271 98.762  1.00 43.29  ? 1000 ILE   A C   1 
ATOM   8822  O  O   . ILE   B 2 1000 ? 109.635 124.845 99.698  1.00 50.61  ? 1000 ILE   A O   1 
ATOM   8823  C  CB  . ILE   B 2 1000 ? 111.302 123.875 96.888  1.00 46.24  ? 1000 ILE   A CB  1 
ATOM   8824  C  CG1 . ILE   B 2 1000 ? 110.877 122.996 95.714  1.00 48.08  ? 1000 ILE   A CG1 1 
ATOM   8825  C  CG2 . ILE   B 2 1000 ? 111.789 123.012 98.033  1.00 43.44  ? 1000 ILE   A CG2 1 
ATOM   8826  C  CD1 . ILE   B 2 1000 ? 109.703 122.102 96.029  1.00 48.73  ? 1000 ILE   A CD1 1 
ATOM   8827  N  N   . LYS   B 2 1001 ? 111.231 126.236 98.932  1.00 48.46  ? 1001 LYS   A N   1 
ATOM   8828  C  CA  . LYS   B 2 1001 ? 111.614 126.707 100.257 1.00 45.50  ? 1001 LYS   A CA  1 
ATOM   8829  C  C   . LYS   B 2 1001 ? 110.468 127.374 101.005 1.00 50.98  ? 1001 LYS   A C   1 
ATOM   8830  O  O   . LYS   B 2 1001 ? 110.460 127.356 102.240 1.00 59.50  ? 1001 LYS   A O   1 
ATOM   8831  C  CB  . LYS   B 2 1001 ? 112.794 127.672 100.133 1.00 45.06  ? 1001 LYS   A CB  1 
ATOM   8832  C  CG  . LYS   B 2 1001 ? 113.445 128.058 101.446 1.00 50.72  ? 1001 LYS   A CG  1 
ATOM   8833  C  CD  . LYS   B 2 1001 ? 114.655 128.945 101.214 1.00 53.70  ? 1001 LYS   A CD  1 
ATOM   8834  C  CE  . LYS   B 2 1001 ? 114.270 130.229 100.505 1.00 55.15  ? 1001 LYS   A CE  1 
ATOM   8835  N  NZ  . LYS   B 2 1001 ? 115.450 131.103 100.263 1.00 52.85  ? 1001 LYS   A NZ  1 
ATOM   8836  N  N   . ASP   B 2 1002 ? 109.503 127.955 100.297 1.00 46.89  ? 1002 ASP   A N   1 
ATOM   8837  C  CA  . ASP   B 2 1002 ? 108.379 128.629 100.928 1.00 42.86  ? 1002 ASP   A CA  1 
ATOM   8838  C  C   . ASP   B 2 1002 ? 107.169 127.728 101.114 1.00 49.16  ? 1002 ASP   A C   1 
ATOM   8839  O  O   . ASP   B 2 1002 ? 106.567 127.733 102.192 1.00 57.91  ? 1002 ASP   A O   1 
ATOM   8840  C  CB  . ASP   B 2 1002 ? 107.975 129.856 100.106 1.00 52.62  ? 1002 ASP   A CB  1 
ATOM   8841  C  CG  . ASP   B 2 1002 ? 109.096 130.866 99.979  1.00 61.78  ? 1002 ASP   A CG  1 
ATOM   8842  O  OD1 . ASP   B 2 1002 ? 110.169 130.644 100.577 1.00 60.16  ? 1002 ASP   A OD1 1 
ATOM   8843  O  OD2 . ASP   B 2 1002 ? 108.906 131.882 99.278  1.00 62.47  ? 1002 ASP   A OD2 1 
ATOM   8844  N  N   . ASN   B 2 1003 ? 106.786 126.953 100.096 1.00 42.15  ? 1003 ASN   A N   1 
ATOM   8845  C  CA  . ASN   B 2 1003 ? 105.608 126.108 100.237 1.00 42.08  ? 1003 ASN   A CA  1 
ATOM   8846  C  C   . ASN   B 2 1003 ? 105.882 124.914 101.143 1.00 53.75  ? 1003 ASN   A C   1 
ATOM   8847  O  O   . ASN   B 2 1003 ? 105.021 124.531 101.944 1.00 61.20  ? 1003 ASN   A O   1 
ATOM   8848  C  CB  . ASN   B 2 1003 ? 105.128 125.651 98.864  1.00 47.96  ? 1003 ASN   A CB  1 
ATOM   8849  C  CG  . ASN   B 2 1003 ? 104.538 126.783 98.051  1.00 55.72  ? 1003 ASN   A CG  1 
ATOM   8850  O  OD1 . ASN   B 2 1003 ? 105.263 127.574 97.452  1.00 57.07  ? 1003 ASN   A OD1 1 
ATOM   8851  N  ND2 . ASN   B 2 1003 ? 103.213 126.865 98.024  1.00 53.82  ? 1003 ASN   A ND2 1 
ATOM   8852  N  N   . LEU   B 2 1004 ? 107.066 124.311 101.039 1.00 48.67  ? 1004 LEU   A N   1 
ATOM   8853  C  CA  . LEU   B 2 1004 ? 107.392 123.162 101.874 1.00 40.12  ? 1004 LEU   A CA  1 
ATOM   8854  C  C   . LEU   B 2 1004 ? 108.097 123.538 103.166 1.00 40.81  ? 1004 LEU   A C   1 
ATOM   8855  O  O   . LEU   B 2 1004 ? 108.000 122.797 104.148 1.00 48.93  ? 1004 LEU   A O   1 
ATOM   8856  C  CB  . LEU   B 2 1004 ? 108.265 122.170 101.100 1.00 43.65  ? 1004 LEU   A CB  1 
ATOM   8857  C  CG  . LEU   B 2 1004 ? 107.621 121.495 99.889  1.00 43.08  ? 1004 LEU   A CG  1 
ATOM   8858  C  CD1 . LEU   B 2 1004 ? 108.594 120.532 99.233  1.00 48.82  ? 1004 LEU   A CD1 1 
ATOM   8859  C  CD2 . LEU   B 2 1004 ? 106.349 120.778 100.293 1.00 44.51  ? 1004 LEU   A CD2 1 
ATOM   8860  N  N   . GLY   B 2 1005 ? 108.802 124.666 103.192 1.00 45.42  ? 1005 GLY   A N   1 
ATOM   8861  C  CA  . GLY   B 2 1005 ? 109.541 125.050 104.376 1.00 44.58  ? 1005 GLY   A CA  1 
ATOM   8862  C  C   . GLY   B 2 1005 ? 110.793 124.247 104.627 1.00 45.81  ? 1005 GLY   A C   1 
ATOM   8863  O  O   . GLY   B 2 1005 ? 111.357 124.333 105.721 1.00 50.35  ? 1005 GLY   A O   1 
ATOM   8864  N  N   . VAL   B 2 1006 ? 111.246 123.471 103.648 1.00 52.49  ? 1006 VAL   A N   1 
ATOM   8865  C  CA  . VAL   B 2 1006 ? 112.407 122.614 103.836 1.00 50.11  ? 1006 VAL   A CA  1 
ATOM   8866  C  C   . VAL   B 2 1006 ? 113.680 123.372 103.472 1.00 50.66  ? 1006 VAL   A C   1 
ATOM   8867  O  O   . VAL   B 2 1006 ? 113.657 124.399 102.791 1.00 56.72  ? 1006 VAL   A O   1 
ATOM   8868  C  CB  . VAL   B 2 1006 ? 112.268 121.326 103.010 1.00 50.81  ? 1006 VAL   A CB  1 
ATOM   8869  C  CG1 . VAL   B 2 1006 ? 111.011 120.576 103.412 1.00 49.75  ? 1006 VAL   A CG1 1 
ATOM   8870  C  CG2 . VAL   B 2 1006 ? 112.237 121.656 101.531 1.00 50.06  ? 1006 VAL   A CG2 1 
ATOM   8871  N  N   . MET   B 2 1007 ? 114.809 122.854 103.945 1.00 53.07  ? 1007 MET   A N   1 
ATOM   8872  C  CA  . MET   B 2 1007 ? 116.100 123.436 103.616 1.00 56.28  ? 1007 MET   A CA  1 
ATOM   8873  C  C   . MET   B 2 1007 ? 116.486 123.085 102.186 1.00 57.98  ? 1007 MET   A C   1 
ATOM   8874  O  O   . MET   B 2 1007 ? 116.166 122.002 101.690 1.00 60.53  ? 1007 MET   A O   1 
ATOM   8875  C  CB  . MET   B 2 1007 ? 117.173 122.942 104.581 1.00 51.39  ? 1007 MET   A CB  1 
ATOM   8876  C  CG  . MET   B 2 1007 ? 118.402 123.818 104.618 1.00 52.81  ? 1007 MET   A CG  1 
ATOM   8877  S  SD  . MET   B 2 1007 ? 118.259 125.092 105.877 1.00 61.63  ? 1007 MET   A SD  1 
ATOM   8878  C  CE  . MET   B 2 1007 ? 118.513 124.100 107.339 1.00 56.47  ? 1007 MET   A CE  1 
ATOM   8879  N  N   . CYS   B 2 1008 ? 117.176 124.008 101.523 1.00 49.82  ? 1008 CYS   A N   1 
ATOM   8880  C  CA  . CYS   B 2 1008 ? 117.523 123.857 100.121 1.00 41.15  ? 1008 CYS   A CA  1 
ATOM   8881  C  C   . CYS   B 2 1008 ? 118.988 124.197 99.887  1.00 42.24  ? 1008 CYS   A C   1 
ATOM   8882  O  O   . CYS   B 2 1008 ? 119.560 125.061 100.557 1.00 51.36  ? 1008 CYS   A O   1 
ATOM   8883  C  CB  . CYS   B 2 1008 ? 116.641 124.743 99.238  1.00 49.32  ? 1008 CYS   A CB  1 
ATOM   8884  S  SG  . CYS   B 2 1008 ? 114.884 124.371 99.345  1.00 69.33  ? 1008 CYS   A SG  1 
ATOM   8885  N  N   . LEU   B 2 1009 ? 119.586 123.506 98.920  1.00 38.94  ? 1009 LEU   A N   1 
ATOM   8886  C  CA  . LEU   B 2 1009 ? 120.953 123.756 98.486  1.00 33.93  ? 1009 LEU   A CA  1 
ATOM   8887  C  C   . LEU   B 2 1009 ? 120.949 123.949 96.979  1.00 39.86  ? 1009 LEU   A C   1 
ATOM   8888  O  O   . LEU   B 2 1009 ? 120.268 123.212 96.260  1.00 49.16  ? 1009 LEU   A O   1 
ATOM   8889  C  CB  . LEU   B 2 1009 ? 121.885 122.603 98.880  1.00 37.62  ? 1009 LEU   A CB  1 
ATOM   8890  C  CG  . LEU   B 2 1009 ? 123.371 122.716 98.528  1.00 39.46  ? 1009 LEU   A CG  1 
ATOM   8891  C  CD1 . LEU   B 2 1009 ? 124.219 122.173 99.653  1.00 42.13  ? 1009 LEU   A CD1 1 
ATOM   8892  C  CD2 . LEU   B 2 1009 ? 123.691 121.982 97.239  1.00 44.09  ? 1009 LEU   A CD2 1 
ATOM   8893  N  N   . ALA   B 2 1010 ? 121.702 124.937 96.506  1.00 37.04  ? 1010 ALA   A N   1 
ATOM   8894  C  CA  . ALA   B 2 1010 ? 121.808 125.241 95.087  1.00 26.80  ? 1010 ALA   A CA  1 
ATOM   8895  C  C   . ALA   B 2 1010 ? 123.272 125.220 94.682  1.00 39.26  ? 1010 ALA   A C   1 
ATOM   8896  O  O   . ALA   B 2 1010 ? 124.110 125.844 95.341  1.00 51.94  ? 1010 ALA   A O   1 
ATOM   8897  C  CB  . ALA   B 2 1010 ? 121.189 126.600 94.769  1.00 41.18  ? 1010 ALA   A CB  1 
ATOM   8898  N  N   . ILE   B 2 1011 ? 123.579 124.510 93.599  1.00 35.30  ? 1011 ILE   A N   1 
ATOM   8899  C  CA  . ILE   B 2 1011 ? 124.949 124.350 93.129  1.00 33.42  ? 1011 ILE   A CA  1 
ATOM   8900  C  C   . ILE   B 2 1011 ? 124.997 124.666 91.639  1.00 38.53  ? 1011 ILE   A C   1 
ATOM   8901  O  O   . ILE   B 2 1011 ? 124.130 124.225 90.878  1.00 50.87  ? 1011 ILE   A O   1 
ATOM   8902  C  CB  . ILE   B 2 1011 ? 125.489 122.935 93.423  1.00 33.84  ? 1011 ILE   A CB  1 
ATOM   8903  C  CG1 . ILE   B 2 1011 ? 126.890 122.754 92.840  1.00 42.87  ? 1011 ILE   A CG1 1 
ATOM   8904  C  CG2 . ILE   B 2 1011 ? 124.535 121.870 92.916  1.00 43.01  ? 1011 ILE   A CG2 1 
ATOM   8905  C  CD1 . ILE   B 2 1011 ? 127.565 121.479 93.271  1.00 48.18  ? 1011 ILE   A CD1 1 
ATOM   8906  N  N   . GLY   B 2 1012 ? 125.995 125.442 91.231  1.00 42.88  ? 1012 GLY   A N   1 
ATOM   8907  C  CA  . GLY   B 2 1012 ? 126.128 125.822 89.836  1.00 40.61  ? 1012 GLY   A CA  1 
ATOM   8908  C  C   . GLY   B 2 1012 ? 127.373 126.654 89.621  1.00 42.67  ? 1012 GLY   A C   1 
ATOM   8909  O  O   . GLY   B 2 1012 ? 128.121 126.950 90.558  1.00 55.23  ? 1012 GLY   A O   1 
ATOM   8910  N  N   . ASP   B 2 1013 ? 127.591 127.028 88.360  1.00 45.15  ? 1013 ASP   A N   1 
ATOM   8911  C  CA  . ASP   B 2 1013 ? 128.803 127.740 87.956  1.00 41.99  ? 1013 ASP   A CA  1 
ATOM   8912  C  C   . ASP   B 2 1013 ? 128.500 128.821 86.918  1.00 48.44  ? 1013 ASP   A C   1 
ATOM   8913  O  O   . ASP   B 2 1013 ? 129.160 128.924 85.884  1.00 49.79  ? 1013 ASP   A O   1 
ATOM   8914  C  CB  . ASP   B 2 1013 ? 129.845 126.758 87.427  1.00 44.46  ? 1013 ASP   A CB  1 
ATOM   8915  C  CG  . ASP   B 2 1013 ? 129.405 126.069 86.156  1.00 54.13  ? 1013 ASP   A CG  1 
ATOM   8916  O  OD1 . ASP   B 2 1013 ? 128.368 126.472 85.588  1.00 57.74  ? 1013 ASP   A OD1 1 
ATOM   8917  O  OD2 . ASP   B 2 1013 ? 130.101 125.130 85.719  1.00 58.20  ? 1013 ASP   A OD2 1 
ATOM   8918  N  N   . GLY   B 2 1014 ? 127.495 129.654 87.180  1.00 54.47  ? 1014 GLY   A N   1 
ATOM   8919  C  CA  . GLY   B 2 1014 ? 127.184 130.723 86.249  1.00 48.61  ? 1014 GLY   A CA  1 
ATOM   8920  C  C   . GLY   B 2 1014 ? 126.343 131.803 86.896  1.00 56.04  ? 1014 GLY   A C   1 
ATOM   8921  O  O   . GLY   B 2 1014 ? 125.993 131.727 88.076  1.00 61.42  ? 1014 GLY   A O   1 
ATOM   8922  N  N   . ALA   B 2 1015 ? 126.023 132.826 86.097  1.00 45.99  ? 1015 ALA   A N   1 
ATOM   8923  C  CA  . ALA   B 2 1015 ? 125.190 133.925 86.580  1.00 53.86  ? 1015 ALA   A CA  1 
ATOM   8924  C  C   . ALA   B 2 1015 ? 123.782 133.452 86.926  1.00 63.16  ? 1015 ALA   A C   1 
ATOM   8925  O  O   . ALA   B 2 1015 ? 123.204 133.871 87.942  1.00 70.76  ? 1015 ALA   A O   1 
ATOM   8926  C  CB  . ALA   B 2 1015 ? 125.140 135.040 85.538  1.00 56.00  ? 1015 ALA   A CB  1 
ATOM   8927  N  N   . ASN   B 2 1016 ? 123.202 132.595 86.085  1.00 42.12  ? 1016 ASN   A N   1 
ATOM   8928  C  CA  . ASN   B 2 1016 ? 121.941 131.961 86.446  1.00 50.96  ? 1016 ASN   A CA  1 
ATOM   8929  C  C   . ASN   B 2 1016 ? 122.097 131.198 87.750  1.00 49.85  ? 1016 ASN   A C   1 
ATOM   8930  O  O   . ASN   B 2 1016 ? 121.255 131.283 88.657  1.00 53.41  ? 1016 ASN   A O   1 
ATOM   8931  C  CB  . ASN   B 2 1016 ? 121.490 131.035 85.318  1.00 54.14  ? 1016 ASN   A CB  1 
ATOM   8932  C  CG  . ASN   B 2 1016 ? 122.654 130.504 84.507  1.00 48.26  ? 1016 ASN   A CG  1 
ATOM   8933  O  OD1 . ASN   B 2 1016 ? 123.594 131.235 84.208  1.00 51.95  ? 1016 ASN   A OD1 1 
ATOM   8934  N  ND2 . ASN   B 2 1016 ? 122.603 129.226 84.159  1.00 48.56  ? 1016 ASN   A ND2 1 
ATOM   8935  N  N   . ASP   B 2 1017 ? 123.204 130.470 87.868  1.00 46.46  ? 1017 ASP   A N   1 
ATOM   8936  C  CA  . ASP   B 2 1017 ? 123.532 129.826 89.125  1.00 50.60  ? 1017 ASP   A CA  1 
ATOM   8937  C  C   . ASP   B 2 1017 ? 123.789 130.849 90.220  1.00 58.72  ? 1017 ASP   A C   1 
ATOM   8938  O  O   . ASP   B 2 1017 ? 123.571 130.550 91.392  1.00 69.57  ? 1017 ASP   A O   1 
ATOM   8939  C  CB  . ASP   B 2 1017 ? 124.740 128.916 88.935  1.00 59.09  ? 1017 ASP   A CB  1 
ATOM   8940  C  CG  . ASP   B 2 1017 ? 124.578 127.981 87.755  1.00 65.07  ? 1017 ASP   A CG  1 
ATOM   8941  O  OD1 . ASP   B 2 1017 ? 123.425 127.624 87.437  1.00 63.28  ? 1017 ASP   A OD1 1 
ATOM   8942  O  OD2 . ASP   B 2 1017 ? 125.600 127.602 87.146  1.00 65.14  ? 1017 ASP   A OD2 1 
ATOM   8943  N  N   . VAL   B 2 1018 ? 124.229 132.060 89.869  1.00 48.61  ? 1018 VAL   A N   1 
ATOM   8944  C  CA  . VAL   B 2 1018 ? 124.409 133.099 90.883  1.00 42.34  ? 1018 VAL   A CA  1 
ATOM   8945  C  C   . VAL   B 2 1018 ? 123.074 133.440 91.532  1.00 39.23  ? 1018 VAL   A C   1 
ATOM   8946  O  O   . VAL   B 2 1018 ? 122.943 133.458 92.764  1.00 48.78  ? 1018 VAL   A O   1 
ATOM   8947  C  CB  . VAL   B 2 1018 ? 125.065 134.350 90.272  1.00 41.16  ? 1018 VAL   A CB  1 
ATOM   8948  C  CG1 . VAL   B 2 1018 ? 124.857 135.545 91.175  1.00 43.96  ? 1018 VAL   A CG1 1 
ATOM   8949  C  CG2 . VAL   B 2 1018 ? 126.540 134.122 90.032  1.00 47.87  ? 1018 VAL   A CG2 1 
ATOM   8950  N  N   . SER   B 2 1019 ? 122.061 133.709 90.708  1.00 40.65  ? 1019 SER   A N   1 
ATOM   8951  C  CA  . SER   B 2 1019 ? 120.745 134.031 91.254  1.00 41.40  ? 1019 SER   A CA  1 
ATOM   8952  C  C   . SER   B 2 1019 ? 120.161 132.850 92.021  1.00 46.31  ? 1019 SER   A C   1 
ATOM   8953  O  O   . SER   B 2 1019 ? 119.596 133.021 93.111  1.00 40.89  ? 1019 SER   A O   1 
ATOM   8954  C  CB  . SER   B 2 1019 ? 119.800 134.465 90.136  1.00 42.95  ? 1019 SER   A CB  1 
ATOM   8955  O  OG  . SER   B 2 1019 ? 118.544 134.848 90.662  1.00 48.16  ? 1019 SER   A OG  1 
ATOM   8956  N  N   . MET   B 2 1020 ? 120.303 131.637 91.475  1.00 57.66  ? 1020 MET   A N   1 
ATOM   8957  C  CA  . MET   B 2 1020 ? 119.787 130.455 92.162  1.00 44.76  ? 1020 MET   A CA  1 
ATOM   8958  C  C   . MET   B 2 1020 ? 120.479 130.245 93.504  1.00 38.59  ? 1020 MET   A C   1 
ATOM   8959  O  O   . MET   B 2 1020 ? 119.837 129.875 94.493  1.00 45.42  ? 1020 MET   A O   1 
ATOM   8960  C  CB  . MET   B 2 1020 ? 119.953 129.227 91.269  1.00 48.43  ? 1020 MET   A CB  1 
ATOM   8961  C  CG  . MET   B 2 1020 ? 119.467 127.932 91.884  1.00 49.90  ? 1020 MET   A CG  1 
ATOM   8962  S  SD  . MET   B 2 1020 ? 119.683 126.531 90.772  1.00 63.23  ? 1020 MET   A SD  1 
ATOM   8963  C  CE  . MET   B 2 1020 ? 121.413 126.695 90.354  1.00 51.69  ? 1020 MET   A CE  1 
ATOM   8964  N  N   . ILE   B 2 1021 ? 121.791 130.477 93.553  1.00 41.31  ? 1021 ILE   A N   1 
ATOM   8965  C  CA  . ILE   B 2 1021 ? 122.561 130.324 94.780  1.00 40.40  ? 1021 ILE   A CA  1 
ATOM   8966  C  C   . ILE   B 2 1021 ? 122.112 131.335 95.823  1.00 52.81  ? 1021 ILE   A C   1 
ATOM   8967  O  O   . ILE   B 2 1021 ? 121.920 130.998 96.997  1.00 60.10  ? 1021 ILE   A O   1 
ATOM   8968  C  CB  . ILE   B 2 1021 ? 124.062 130.463 94.467  1.00 38.58  ? 1021 ILE   A CB  1 
ATOM   8969  C  CG1 . ILE   B 2 1021 ? 124.629 129.147 93.934  1.00 51.66  ? 1021 ILE   A CG1 1 
ATOM   8970  C  CG2 . ILE   B 2 1021 ? 124.828 130.957 95.678  1.00 45.23  ? 1021 ILE   A CG2 1 
ATOM   8971  C  CD1 . ILE   B 2 1021 ? 125.996 129.287 93.314  1.00 48.49  ? 1021 ILE   A CD1 1 
ATOM   8972  N  N   . GLN   B 2 1022 ? 121.937 132.592 95.411  1.00 54.35  ? 1022 GLN   A N   1 
ATOM   8973  C  CA  . GLN   B 2 1022 ? 121.483 133.605 96.358  1.00 49.15  ? 1022 GLN   A CA  1 
ATOM   8974  C  C   . GLN   B 2 1022 ? 120.072 133.321 96.851  1.00 49.62  ? 1022 GLN   A C   1 
ATOM   8975  O  O   . GLN   B 2 1022 ? 119.725 133.690 97.977  1.00 51.79  ? 1022 GLN   A O   1 
ATOM   8976  C  CB  . GLN   B 2 1022 ? 121.562 134.993 95.728  1.00 51.17  ? 1022 GLN   A CB  1 
ATOM   8977  C  CG  . GLN   B 2 1022 ? 122.975 135.518 95.586  1.00 49.50  ? 1022 GLN   A CG  1 
ATOM   8978  C  CD  . GLN   B 2 1022 ? 123.028 136.873 94.923  1.00 55.47  ? 1022 GLN   A CD  1 
ATOM   8979  O  OE1 . GLN   B 2 1022 ? 122.023 137.370 94.420  1.00 57.76  ? 1022 GLN   A OE1 1 
ATOM   8980  N  NE2 . GLN   B 2 1022 ? 124.206 137.482 94.917  1.00 57.59  ? 1022 GLN   A NE2 1 
ATOM   8981  N  N   . ALA   B 2 1023 ? 119.250 132.662 96.038  1.00 48.03  ? 1023 ALA   A N   1 
ATOM   8982  C  CA  . ALA   B 2 1023 ? 117.871 132.382 96.417  1.00 42.72  ? 1023 ALA   A CA  1 
ATOM   8983  C  C   . ALA   B 2 1023 ? 117.723 131.198 97.366  1.00 44.35  ? 1023 ALA   A C   1 
ATOM   8984  O  O   . ALA   B 2 1023 ? 116.614 130.955 97.851  1.00 56.31  ? 1023 ALA   A O   1 
ATOM   8985  C  CB  . ALA   B 2 1023 ? 117.022 132.137 95.166  1.00 52.59  ? 1023 ALA   A CB  1 
ATOM   8986  N  N   . ALA   B 2 1024 ? 118.793 130.461 97.647  1.00 42.46  ? 1024 ALA   A N   1 
ATOM   8987  C  CA  . ALA   B 2 1024 ? 118.720 129.229 98.420  1.00 39.01  ? 1024 ALA   A CA  1 
ATOM   8988  C  C   . ALA   B 2 1024 ? 119.302 129.413 99.815  1.00 47.64  ? 1024 ALA   A C   1 
ATOM   8989  O  O   . ALA   B 2 1024 ? 119.901 130.443 100.135 1.00 60.11  ? 1024 ALA   A O   1 
ATOM   8990  C  CB  . ALA   B 2 1024 ? 119.452 128.091 97.704  1.00 41.77  ? 1024 ALA   A CB  1 
ATOM   8991  N  N   . ASP   B 2 1025 ? 119.110 128.389 100.651 1.00 49.67  ? 1025 ASP   A N   1 
ATOM   8992  C  CA  . ASP   B 2 1025 ? 119.630 128.433 102.014 1.00 49.39  ? 1025 ASP   A CA  1 
ATOM   8993  C  C   . ASP   B 2 1025 ? 121.147 128.310 102.028 1.00 50.20  ? 1025 ASP   A C   1 
ATOM   8994  O  O   . ASP   B 2 1025 ? 121.836 129.067 102.721 1.00 60.64  ? 1025 ASP   A O   1 
ATOM   8995  C  CB  . ASP   B 2 1025 ? 118.991 127.332 102.858 1.00 51.71  ? 1025 ASP   A CB  1 
ATOM   8996  C  CG  . ASP   B 2 1025 ? 117.542 127.620 103.190 1.00 59.18  ? 1025 ASP   A CG  1 
ATOM   8997  O  OD1 . ASP   B 2 1025 ? 117.182 128.811 103.301 1.00 61.18  ? 1025 ASP   A OD1 1 
ATOM   8998  O  OD2 . ASP   B 2 1025 ? 116.763 126.657 103.341 1.00 60.19  ? 1025 ASP   A OD2 1 
ATOM   8999  N  N   . VAL   B 2 1026 ? 121.686 127.356 101.276 1.00 42.43  ? 1026 VAL   A N   1 
ATOM   9000  C  CA  . VAL   B 2 1026 ? 123.124 127.206 101.096 1.00 37.52  ? 1026 VAL   A CA  1 
ATOM   9001  C  C   . VAL   B 2 1026 ? 123.405 127.222 99.604  1.00 38.93  ? 1026 VAL   A C   1 
ATOM   9002  O  O   . VAL   B 2 1026 ? 122.820 126.438 98.848  1.00 51.47  ? 1026 VAL   A O   1 
ATOM   9003  C  CB  . VAL   B 2 1026 ? 123.658 125.917 101.737 1.00 47.27  ? 1026 VAL   A CB  1 
ATOM   9004  C  CG1 . VAL   B 2 1026 ? 125.128 125.745 101.414 1.00 53.44  ? 1026 VAL   A CG1 1 
ATOM   9005  C  CG2 . VAL   B 2 1026 ? 123.451 125.950 103.231 1.00 46.23  ? 1026 VAL   A CG2 1 
ATOM   9006  N  N   . GLY   B 2 1027 ? 124.297 128.108 99.183  1.00 38.44  ? 1027 GLY   A N   1 
ATOM   9007  C  CA  . GLY   B 2 1027 ? 124.693 128.158 97.794  1.00 40.74  ? 1027 GLY   A CA  1 
ATOM   9008  C  C   . GLY   B 2 1027 ? 126.111 127.679 97.588  1.00 41.55  ? 1027 GLY   A C   1 
ATOM   9009  O  O   . GLY   B 2 1027 ? 127.033 128.136 98.270  1.00 55.97  ? 1027 GLY   A O   1 
ATOM   9010  N  N   . VAL   B 2 1028 ? 126.301 126.759 96.650  1.00 30.33  ? 1028 VAL   A N   1 
ATOM   9011  C  CA  . VAL   B 2 1028 ? 127.605 126.178 96.361  1.00 29.74  ? 1028 VAL   A CA  1 
ATOM   9012  C  C   . VAL   B 2 1028 ? 127.980 126.527 94.929  1.00 34.21  ? 1028 VAL   A C   1 
ATOM   9013  O  O   . VAL   B 2 1028 ? 127.182 126.333 94.006  1.00 44.89  ? 1028 VAL   A O   1 
ATOM   9014  C  CB  . VAL   B 2 1028 ? 127.603 124.656 96.575  1.00 32.07  ? 1028 VAL   A CB  1 
ATOM   9015  C  CG1 . VAL   B 2 1028 ? 129.009 124.123 96.500  1.00 35.81  ? 1028 VAL   A CG1 1 
ATOM   9016  C  CG2 . VAL   B 2 1028 ? 126.973 124.310 97.908  1.00 45.65  ? 1028 VAL   A CG2 1 
ATOM   9017  N  N   . GLY   B 2 1029 ? 129.188 127.047 94.746  1.00 31.46  ? 1029 GLY   A N   1 
ATOM   9018  C  CA  . GLY   B 2 1029 ? 129.694 127.402 93.435  1.00 34.65  ? 1029 GLY   A CA  1 
ATOM   9019  C  C   . GLY   B 2 1029 ? 130.805 126.458 93.021  1.00 43.56  ? 1029 GLY   A C   1 
ATOM   9020  O  O   . GLY   B 2 1029 ? 131.551 125.952 93.862  1.00 48.75  ? 1029 GLY   A O   1 
ATOM   9021  N  N   . ILE   B 2 1030 ? 130.909 126.215 91.720  1.00 45.68  ? 1030 ILE   A N   1 
ATOM   9022  C  CA  . ILE   B 2 1030 ? 131.923 125.328 91.166  1.00 41.01  ? 1030 ILE   A CA  1 
ATOM   9023  C  C   . ILE   B 2 1030 ? 132.943 126.173 90.418  1.00 45.53  ? 1030 ILE   A C   1 
ATOM   9024  O  O   . ILE   B 2 1030 ? 132.584 126.956 89.531  1.00 53.08  ? 1030 ILE   A O   1 
ATOM   9025  C  CB  . ILE   B 2 1030 ? 131.300 124.262 90.253  1.00 39.42  ? 1030 ILE   A CB  1 
ATOM   9026  C  CG1 . ILE   B 2 1030 ? 130.405 123.334 91.071  1.00 44.11  ? 1030 ILE   A CG1 1 
ATOM   9027  C  CG2 . ILE   B 2 1030 ? 132.382 123.469 89.545  1.00 43.57  ? 1030 ILE   A CG2 1 
ATOM   9028  C  CD1 . ILE   B 2 1030 ? 129.983 122.092 90.338  1.00 50.16  ? 1030 ILE   A CD1 1 
ATOM   9029  N  N   . SER   B 2 1031 ? 134.215 126.018 90.777  1.00 52.55  ? 1031 SER   A N   1 
ATOM   9030  C  CA  . SER   B 2 1031 ? 135.295 126.771 90.149  1.00 55.17  ? 1031 SER   A CA  1 
ATOM   9031  C  C   . SER   B 2 1031 ? 135.706 126.070 88.861  1.00 62.83  ? 1031 SER   A C   1 
ATOM   9032  O  O   . SER   B 2 1031 ? 136.255 124.964 88.895  1.00 69.44  ? 1031 SER   A O   1 
ATOM   9033  C  CB  . SER   B 2 1031 ? 136.475 126.901 91.105  1.00 59.20  ? 1031 SER   A CB  1 
ATOM   9034  O  OG  . SER   B 2 1031 ? 136.080 127.516 92.318  1.00 67.68  ? 1031 SER   A OG  1 
ATOM   9035  N  N   . GLY   B 2 1032 ? 135.444 126.711 87.725  1.00 70.32  ? 1032 GLY   A N   1 
ATOM   9036  C  CA  . GLY   B 2 1032 ? 135.786 126.137 86.440  1.00 69.02  ? 1032 GLY   A CA  1 
ATOM   9037  C  C   . GLY   B 2 1032 ? 136.361 127.144 85.468  1.00 74.97  ? 1032 GLY   A C   1 
ATOM   9038  O  O   . GLY   B 2 1032 ? 136.215 126.991 84.251  1.00 74.74  ? 1032 GLY   A O   1 
ATOM   9039  N  N   . GLU   B 2 1033 ? 137.022 128.176 85.998  1.00 97.32  ? 1033 GLU   A N   1 
ATOM   9040  C  CA  . GLU   B 2 1033 ? 137.608 129.245 85.187  1.00 98.16  ? 1033 GLU   A CA  1 
ATOM   9041  C  C   . GLU   B 2 1033 ? 136.559 129.880 84.276  1.00 96.54  ? 1033 GLU   A C   1 
ATOM   9042  O  O   . GLU   B 2 1033 ? 136.815 130.178 83.107  1.00 96.73  ? 1033 GLU   A O   1 
ATOM   9043  C  CB  . GLU   B 2 1033 ? 138.799 128.730 84.374  1.00 97.03  ? 1033 GLU   A CB  1 
ATOM   9044  C  CG  . GLU   B 2 1033 ? 139.925 128.150 85.216  1.00 97.66  ? 1033 GLU   A CG  1 
ATOM   9045  C  CD  . GLU   B 2 1033 ? 140.643 129.200 86.044  1.00 100.72 ? 1033 GLU   A CD  1 
ATOM   9046  O  OE1 . GLU   B 2 1033 ? 140.589 130.393 85.677  1.00 100.73 ? 1033 GLU   A OE1 1 
ATOM   9047  O  OE2 . GLU   B 2 1033 ? 141.261 128.831 87.064  1.00 99.38  ? 1033 GLU   A OE2 1 
ATOM   9048  N  N   . GLU   B 2 1034 ? 135.364 130.090 84.821  1.00 83.33  ? 1034 GLU   A N   1 
ATOM   9049  C  CA  . GLU   B 2 1034 ? 134.224 130.608 84.074  1.00 83.02  ? 1034 GLU   A CA  1 
ATOM   9050  C  C   . GLU   B 2 1034 ? 133.766 131.957 84.622  1.00 84.88  ? 1034 GLU   A C   1 
ATOM   9051  O  O   . GLU   B 2 1034 ? 132.570 132.208 84.780  1.00 84.08  ? 1034 GLU   A O   1 
ATOM   9052  C  CB  . GLU   B 2 1034 ? 133.074 129.604 84.088  1.00 82.86  ? 1034 GLU   A CB  1 
ATOM   9053  C  CG  . GLU   B 2 1034 ? 132.120 129.715 82.906  1.00 84.14  ? 1034 GLU   A CG  1 
ATOM   9054  C  CD  . GLU   B 2 1034 ? 132.738 129.241 81.604  1.00 86.00  ? 1034 GLU   A CD  1 
ATOM   9055  O  OE1 . GLU   B 2 1034 ? 133.754 128.516 81.652  1.00 83.92  ? 1034 GLU   A OE1 1 
ATOM   9056  O  OE2 . GLU   B 2 1034 ? 132.205 129.594 80.531  1.00 85.62  ? 1034 GLU   A OE2 1 
ATOM   9057  N  N   . GLY   B 2 1035 ? 134.717 132.838 84.930  1.00 82.12  ? 1035 GLY   A N   1 
ATOM   9058  C  CA  . GLY   B 2 1035 ? 134.404 134.137 85.484  1.00 78.93  ? 1035 GLY   A CA  1 
ATOM   9059  C  C   . GLY   B 2 1035 ? 134.250 134.174 86.987  1.00 75.10  ? 1035 GLY   A C   1 
ATOM   9060  O  O   . GLY   B 2 1035 ? 134.201 135.270 87.560  1.00 77.07  ? 1035 GLY   A O   1 
ATOM   9061  N  N   . LEU   B 2 1036 ? 134.156 133.016 87.642  1.00 59.09  ? 1036 LEU   A N   1 
ATOM   9062  C  CA  . LEU   B 2 1036 ? 134.136 132.895 89.097  1.00 60.63  ? 1036 LEU   A CA  1 
ATOM   9063  C  C   . LEU   B 2 1036 ? 132.946 133.603 89.734  1.00 63.57  ? 1036 LEU   A C   1 
ATOM   9064  O  O   . LEU   B 2 1036 ? 132.969 133.897 90.932  1.00 70.75  ? 1036 LEU   A O   1 
ATOM   9065  C  CB  . LEU   B 2 1036 ? 135.441 133.412 89.711  1.00 65.44  ? 1036 LEU   A CB  1 
ATOM   9066  C  CG  . LEU   B 2 1036 ? 136.735 132.773 89.208  1.00 68.50  ? 1036 LEU   A CG  1 
ATOM   9067  C  CD1 . LEU   B 2 1036 ? 137.940 133.431 89.859  1.00 63.83  ? 1036 LEU   A CD1 1 
ATOM   9068  C  CD2 . LEU   B 2 1036 ? 136.732 131.274 89.468  1.00 69.84  ? 1036 LEU   A CD2 1 
ATOM   9069  N  N   . GLN   B 2 1037 ? 131.892 133.875 88.965  1.00 50.34  ? 1037 GLN   A N   1 
ATOM   9070  C  CA  . GLN   B 2 1037 ? 130.771 134.639 89.501  1.00 51.80  ? 1037 GLN   A CA  1 
ATOM   9071  C  C   . GLN   B 2 1037 ? 129.956 133.814 90.489  1.00 58.65  ? 1037 GLN   A C   1 
ATOM   9072  O  O   . GLN   B 2 1037 ? 129.588 134.302 91.566  1.00 61.26  ? 1037 GLN   A O   1 
ATOM   9073  C  CB  . GLN   B 2 1037 ? 129.898 135.142 88.357  1.00 44.90  ? 1037 GLN   A CB  1 
ATOM   9074  C  CG  . GLN   B 2 1037 ? 130.702 135.774 87.244  1.00 49.17  ? 1037 GLN   A CG  1 
ATOM   9075  C  CD  . GLN   B 2 1037 ? 129.883 136.717 86.409  1.00 57.08  ? 1037 GLN   A CD  1 
ATOM   9076  O  OE1 . GLN   B 2 1037 ? 128.806 137.146 86.818  1.00 57.13  ? 1037 GLN   A OE1 1 
ATOM   9077  N  NE2 . GLN   B 2 1037 ? 130.387 137.053 85.228  1.00 58.66  ? 1037 GLN   A NE2 1 
ATOM   9078  N  N   . ALA   B 2 1038 ? 129.665 132.559 90.142  1.00 49.92  ? 1038 ALA   A N   1 
ATOM   9079  C  CA  . ALA   B 2 1038 ? 128.973 131.683 91.080  1.00 38.81  ? 1038 ALA   A CA  1 
ATOM   9080  C  C   . ALA   B 2 1038 ? 129.813 131.452 92.325  1.00 43.84  ? 1038 ALA   A C   1 
ATOM   9081  O  O   . ALA   B 2 1038 ? 129.281 131.380 93.437  1.00 53.46  ? 1038 ALA   A O   1 
ATOM   9082  C  CB  . ALA   B 2 1038 ? 128.628 130.357 90.409  1.00 43.21  ? 1038 ALA   A CB  1 
ATOM   9083  N  N   . VAL   B 2 1039 ? 131.131 131.339 92.157  1.00 40.99  ? 1039 VAL   A N   1 
ATOM   9084  C  CA  . VAL   B 2 1039 ? 132.028 131.209 93.300  1.00 34.10  ? 1039 VAL   A CA  1 
ATOM   9085  C  C   . VAL   B 2 1039 ? 131.955 132.451 94.178  1.00 45.34  ? 1039 VAL   A C   1 
ATOM   9086  O  O   . VAL   B 2 1039 ? 131.916 132.359 95.411  1.00 52.13  ? 1039 VAL   A O   1 
ATOM   9087  C  CB  . VAL   B 2 1039 ? 133.463 130.940 92.814  1.00 37.50  ? 1039 VAL   A CB  1 
ATOM   9088  C  CG1 . VAL   B 2 1039 ? 134.433 130.930 93.981  1.00 46.35  ? 1039 VAL   A CG1 1 
ATOM   9089  C  CG2 . VAL   B 2 1039 ? 133.522 129.630 92.055  1.00 47.59  ? 1039 VAL   A CG2 1 
ATOM   9090  N  N   . ASN   B 2 1040 ? 131.932 133.634 93.558  1.00 48.22  ? 1040 ASN   A N   1 
ATOM   9091  C  CA  . ASN   B 2 1040 ? 131.903 134.873 94.325  1.00 35.11  ? 1040 ASN   A CA  1 
ATOM   9092  C  C   . ASN   B 2 1040 ? 130.582 135.063 95.057  1.00 40.52  ? 1040 ASN   A C   1 
ATOM   9093  O  O   . ASN   B 2 1040 ? 130.561 135.638 96.151  1.00 54.03  ? 1040 ASN   A O   1 
ATOM   9094  C  CB  . ASN   B 2 1040 ? 132.172 136.065 93.410  1.00 39.28  ? 1040 ASN   A CB  1 
ATOM   9095  C  CG  . ASN   B 2 1040 ? 133.566 136.049 92.829  1.00 44.83  ? 1040 ASN   A CG  1 
ATOM   9096  O  OD1 . ASN   B 2 1040 ? 134.452 135.363 93.334  1.00 48.63  ? 1040 ASN   A OD1 1 
ATOM   9097  N  ND2 . ASN   B 2 1040 ? 133.770 136.808 91.761  1.00 47.28  ? 1040 ASN   A ND2 1 
ATOM   9098  N  N   . SER   B 2 1041 ? 129.478 134.600 94.480  1.00 33.58  ? 1041 SER   A N   1 
ATOM   9099  C  CA  . SER   B 2 1041 ? 128.162 134.789 95.075  1.00 34.47  ? 1041 SER   A CA  1 
ATOM   9100  C  C   . SER   B 2 1041 ? 127.723 133.628 95.955  1.00 39.56  ? 1041 SER   A C   1 
ATOM   9101  O  O   . SER   B 2 1041 ? 126.594 133.644 96.454  1.00 50.30  ? 1041 SER   A O   1 
ATOM   9102  C  CB  . SER   B 2 1041 ? 127.120 135.015 93.980  1.00 44.68  ? 1041 SER   A CB  1 
ATOM   9103  O  OG  . SER   B 2 1041 ? 126.945 133.844 93.204  1.00 53.16  ? 1041 SER   A OG  1 
ATOM   9104  N  N   . SER   B 2 1042 ? 128.573 132.627 96.159  1.00 42.87  ? 1042 SER   A N   1 
ATOM   9105  C  CA  . SER   B 2 1042 ? 128.194 131.428 96.886  1.00 38.23  ? 1042 SER   A CA  1 
ATOM   9106  C  C   . SER   B 2 1042 ? 128.619 131.519 98.347  1.00 41.01  ? 1042 SER   A C   1 
ATOM   9107  O  O   . SER   B 2 1042 ? 129.268 132.471 98.783  1.00 49.78  ? 1042 SER   A O   1 
ATOM   9108  C  CB  . SER   B 2 1042 ? 128.801 130.188 96.230  1.00 37.42  ? 1042 SER   A CB  1 
ATOM   9109  O  OG  . SER   B 2 1042 ? 130.212 130.284 96.174  1.00 43.45  ? 1042 SER   A OG  1 
ATOM   9110  N  N   . ASP   B 2 1043 ? 128.232 130.502 99.113  1.00 43.90  ? 1043 ASP   A N   1 
ATOM   9111  C  CA  . ASP   B 2 1043 ? 128.676 130.315 100.486 1.00 41.72  ? 1043 ASP   A CA  1 
ATOM   9112  C  C   . ASP   B 2 1043 ? 129.802 129.300 100.595 1.00 51.85  ? 1043 ASP   A C   1 
ATOM   9113  O  O   . ASP   B 2 1043 ? 130.607 129.367 101.528 1.00 57.99  ? 1043 ASP   A O   1 
ATOM   9114  C  CB  . ASP   B 2 1043 ? 127.505 129.870 101.363 1.00 44.50  ? 1043 ASP   A CB  1 
ATOM   9115  C  CG  . ASP   B 2 1043 ? 126.297 130.767 101.219 1.00 53.19  ? 1043 ASP   A CG  1 
ATOM   9116  O  OD1 . ASP   B 2 1043 ? 126.479 131.985 101.014 1.00 62.52  ? 1043 ASP   A OD1 1 
ATOM   9117  O  OD2 . ASP   B 2 1043 ? 125.164 130.254 101.309 1.00 55.77  ? 1043 ASP   A OD2 1 
ATOM   9118  N  N   . TYR   B 2 1044 ? 129.869 128.360 99.658  1.00 47.31  ? 1044 TYR   A N   1 
ATOM   9119  C  CA  . TYR   B 2 1044 ? 130.941 127.383 99.579  1.00 37.84  ? 1044 TYR   A CA  1 
ATOM   9120  C  C   . TYR   B 2 1044 ? 131.381 127.253 98.131  1.00 42.52  ? 1044 TYR   A C   1 
ATOM   9121  O  O   . TYR   B 2 1044 ? 130.550 127.272 97.219  1.00 57.84  ? 1044 TYR   A O   1 
ATOM   9122  C  CB  . TYR   B 2 1044 ? 130.498 126.024 100.123 1.00 42.35  ? 1044 TYR   A CB  1 
ATOM   9123  C  CG  . TYR   B 2 1044 ? 130.130 126.055 101.585 1.00 44.29  ? 1044 TYR   A CG  1 
ATOM   9124  C  CD1 . TYR   B 2 1044 ? 131.089 125.847 102.563 1.00 48.26  ? 1044 TYR   A CD1 1 
ATOM   9125  C  CD2 . TYR   B 2 1044 ? 128.828 126.303 101.987 1.00 48.37  ? 1044 TYR   A CD2 1 
ATOM   9126  C  CE1 . TYR   B 2 1044 ? 130.760 125.879 103.897 1.00 49.25  ? 1044 TYR   A CE1 1 
ATOM   9127  C  CE2 . TYR   B 2 1044 ? 128.491 126.337 103.320 1.00 49.30  ? 1044 TYR   A CE2 1 
ATOM   9128  C  CZ  . TYR   B 2 1044 ? 129.461 126.125 104.270 1.00 49.44  ? 1044 TYR   A CZ  1 
ATOM   9129  O  OH  . TYR   B 2 1044 ? 129.129 126.159 105.602 1.00 56.46  ? 1044 TYR   A OH  1 
ATOM   9130  N  N   . ALA   B 2 1045 ? 132.684 127.126 97.923  1.00 40.44  ? 1045 ALA   A N   1 
ATOM   9131  C  CA  . ALA   B 2 1045 ? 133.262 127.006 96.591  1.00 41.95  ? 1045 ALA   A CA  1 
ATOM   9132  C  C   . ALA   B 2 1045 ? 133.972 125.664 96.492  1.00 45.41  ? 1045 ALA   A C   1 
ATOM   9133  O  O   . ALA   B 2 1045 ? 135.025 125.463 97.107  1.00 48.00  ? 1045 ALA   A O   1 
ATOM   9134  C  CB  . ALA   B 2 1045 ? 134.221 128.157 96.303  1.00 46.21  ? 1045 ALA   A CB  1 
ATOM   9135  N  N   . ILE   B 2 1046 ? 133.398 124.752 95.717  1.00 36.93  ? 1046 ILE   A N   1 
ATOM   9136  C  CA  . ILE   B 2 1046 ? 133.989 123.448 95.474  1.00 34.08  ? 1046 ILE   A CA  1 
ATOM   9137  C  C   . ILE   B 2 1046 ? 134.425 123.378 94.016  1.00 42.57  ? 1046 ILE   A C   1 
ATOM   9138  O  O   . ILE   B 2 1046 ? 134.100 124.242 93.203  1.00 53.39  ? 1046 ILE   A O   1 
ATOM   9139  C  CB  . ILE   B 2 1046 ? 133.023 122.302 95.822  1.00 38.63  ? 1046 ILE   A CB  1 
ATOM   9140  C  CG1 . ILE   B 2 1046 ? 131.794 122.354 94.920  1.00 39.44  ? 1046 ILE   A CG1 1 
ATOM   9141  C  CG2 . ILE   B 2 1046 ? 132.608 122.381 97.277  1.00 50.75  ? 1046 ILE   A CG2 1 
ATOM   9142  C  CD1 . ILE   B 2 1046 ? 130.775 121.297 95.232  1.00 39.66  ? 1046 ILE   A CD1 1 
ATOM   9143  N  N   . ALA   B 2 1047 ? 135.183 122.335 93.691  1.00 40.05  ? 1047 ALA   A N   1 
ATOM   9144  C  CA  . ALA   B 2 1047 ? 135.613 122.097 92.324  1.00 39.26  ? 1047 ALA   A CA  1 
ATOM   9145  C  C   . ALA   B 2 1047 ? 134.994 120.854 91.702  1.00 45.80  ? 1047 ALA   A C   1 
ATOM   9146  O  O   . ALA   B 2 1047 ? 135.068 120.695 90.480  1.00 47.51  ? 1047 ALA   A O   1 
ATOM   9147  C  CB  . ALA   B 2 1047 ? 137.143 121.991 92.259  1.00 43.24  ? 1047 ALA   A CB  1 
ATOM   9148  N  N   . GLN   B 2 1048 ? 134.390 119.975 92.500  1.00 43.31  ? 1048 GLN   A N   1 
ATOM   9149  C  CA  . GLN   B 2 1048 ? 133.797 118.747 91.992  1.00 37.59  ? 1048 GLN   A CA  1 
ATOM   9150  C  C   . GLN   B 2 1048 ? 132.501 118.465 92.739  1.00 45.12  ? 1048 GLN   A C   1 
ATOM   9151  O  O   . GLN   B 2 1048 ? 132.292 118.931 93.860  1.00 54.41  ? 1048 GLN   A O   1 
ATOM   9152  C  CB  . GLN   B 2 1048 ? 134.753 117.553 92.136  1.00 45.49  ? 1048 GLN   A CB  1 
ATOM   9153  C  CG  . GLN   B 2 1048 ? 136.097 117.717 91.442  1.00 43.17  ? 1048 GLN   A CG  1 
ATOM   9154  C  CD  . GLN   B 2 1048 ? 135.988 117.670 89.938  1.00 44.13  ? 1048 GLN   A CD  1 
ATOM   9155  O  OE1 . GLN   B 2 1048 ? 135.122 116.991 89.388  1.00 48.84  ? 1048 GLN   A OE1 1 
ATOM   9156  N  NE2 . GLN   B 2 1048 ? 136.864 118.396 89.260  1.00 43.14  ? 1048 GLN   A NE2 1 
ATOM   9157  N  N   . PHE   B 2 1049 ? 131.634 117.676 92.100  1.00 36.48  ? 1049 PHE   A N   1 
ATOM   9158  C  CA  . PHE   B 2 1049 ? 130.372 117.275 92.718  1.00 43.86  ? 1049 PHE   A CA  1 
ATOM   9159  C  C   . PHE   B 2 1049 ? 130.595 116.296 93.871  1.00 48.16  ? 1049 PHE   A C   1 
ATOM   9160  O  O   . PHE   B 2 1049 ? 129.904 116.359 94.900  1.00 49.16  ? 1049 PHE   A O   1 
ATOM   9161  C  CB  . PHE   B 2 1049 ? 129.469 116.659 91.650  1.00 50.72  ? 1049 PHE   A CB  1 
ATOM   9162  C  CG  . PHE   B 2 1049 ? 128.031 117.063 91.757  1.00 43.22  ? 1049 PHE   A CG  1 
ATOM   9163  C  CD1 . PHE   B 2 1049 ? 127.618 118.312 91.341  1.00 43.53  ? 1049 PHE   A CD1 1 
ATOM   9164  C  CD2 . PHE   B 2 1049 ? 127.087 116.183 92.248  1.00 43.62  ? 1049 PHE   A CD2 1 
ATOM   9165  C  CE1 . PHE   B 2 1049 ? 126.295 118.679 91.432  1.00 48.49  ? 1049 PHE   A CE1 1 
ATOM   9166  C  CE2 . PHE   B 2 1049 ? 125.765 116.546 92.339  1.00 44.81  ? 1049 PHE   A CE2 1 
ATOM   9167  C  CZ  . PHE   B 2 1049 ? 125.368 117.795 91.930  1.00 42.89  ? 1049 PHE   A CZ  1 
ATOM   9168  N  N   . ARG   B 2 1050 ? 131.545 115.371 93.713  1.00 38.65  ? 1050 ARG   A N   1 
ATOM   9169  C  CA  . ARG   B 2 1050 ? 131.851 114.435 94.789  1.00 47.02  ? 1050 ARG   A CA  1 
ATOM   9170  C  C   . ARG   B 2 1050 ? 132.332 115.163 96.035  1.00 53.66  ? 1050 ARG   A C   1 
ATOM   9171  O  O   . ARG   B 2 1050 ? 132.130 114.686 97.164  1.00 60.55  ? 1050 ARG   A O   1 
ATOM   9172  C  CB  . ARG   B 2 1050 ? 132.892 113.423 94.312  1.00 53.03  ? 1050 ARG   A CB  1 
ATOM   9173  C  CG  . ARG   B 2 1050 ? 134.063 114.038 93.568  1.00 47.44  ? 1050 ARG   A CG  1 
ATOM   9174  C  CD  . ARG   B 2 1050 ? 134.947 112.963 92.962  1.00 49.35  ? 1050 ARG   A CD  1 
ATOM   9175  N  NE  . ARG   B 2 1050 ? 136.223 113.491 92.495  1.00 52.71  ? 1050 ARG   A NE  1 
ATOM   9176  C  CZ  . ARG   B 2 1050 ? 136.413 114.063 91.315  1.00 56.42  ? 1050 ARG   A CZ  1 
ATOM   9177  N  NH1 . ARG   B 2 1050 ? 135.421 114.219 90.454  1.00 59.49  ? 1050 ARG   A NH1 1 
ATOM   9178  N  NH2 . ARG   B 2 1050 ? 137.629 114.489 90.989  1.00 54.84  ? 1050 ARG   A NH2 1 
ATOM   9179  N  N   . TYR   B 2 1051 ? 132.968 116.318 95.849  1.00 41.89  ? 1051 TYR   A N   1 
ATOM   9180  C  CA  . TYR   B 2 1051 ? 133.326 117.145 96.990  1.00 41.63  ? 1051 TYR   A CA  1 
ATOM   9181  C  C   . TYR   B 2 1051 ? 132.078 117.618 97.715  1.00 48.14  ? 1051 TYR   A C   1 
ATOM   9182  O  O   . TYR   B 2 1051 ? 132.065 117.696 98.944  1.00 55.59  ? 1051 TYR   A O   1 
ATOM   9183  C  CB  . TYR   B 2 1051 ? 134.185 118.326 96.541  1.00 41.77  ? 1051 TYR   A CB  1 
ATOM   9184  C  CG  . TYR   B 2 1051 ? 135.488 117.919 95.893  1.00 44.31  ? 1051 TYR   A CG  1 
ATOM   9185  C  CD1 . TYR   B 2 1051 ? 135.957 116.618 95.987  1.00 43.37  ? 1051 TYR   A CD1 1 
ATOM   9186  C  CD2 . TYR   B 2 1051 ? 136.250 118.837 95.192  1.00 49.37  ? 1051 TYR   A CD2 1 
ATOM   9187  C  CE1 . TYR   B 2 1051 ? 137.139 116.243 95.395  1.00 42.90  ? 1051 TYR   A CE1 1 
ATOM   9188  C  CE2 . TYR   B 2 1051 ? 137.438 118.470 94.600  1.00 48.30  ? 1051 TYR   A CE2 1 
ATOM   9189  C  CZ  . TYR   B 2 1051 ? 137.877 117.171 94.704  1.00 46.78  ? 1051 TYR   A CZ  1 
ATOM   9190  O  OH  . TYR   B 2 1051 ? 139.061 116.796 94.116  1.00 56.78  ? 1051 TYR   A OH  1 
ATOM   9191  N  N   . LEU   B 2 1052 ? 131.015 117.930 96.970  1.00 44.75  ? 1052 LEU   A N   1 
ATOM   9192  C  CA  . LEU   B 2 1052 ? 129.737 118.237 97.603  1.00 41.61  ? 1052 LEU   A CA  1 
ATOM   9193  C  C   . LEU   B 2 1052 ? 129.214 117.043 98.384  1.00 36.31  ? 1052 LEU   A C   1 
ATOM   9194  O  O   . LEU   B 2 1052 ? 128.689 117.198 99.495  1.00 49.12  ? 1052 LEU   A O   1 
ATOM   9195  C  CB  . LEU   B 2 1052 ? 128.713 118.667 96.554  1.00 45.10  ? 1052 LEU   A CB  1 
ATOM   9196  C  CG  . LEU   B 2 1052 ? 127.251 118.664 97.005  1.00 44.96  ? 1052 LEU   A CG  1 
ATOM   9197  C  CD1 . LEU   B 2 1052 ? 126.933 119.919 97.797  1.00 47.49  ? 1052 LEU   A CD1 1 
ATOM   9198  C  CD2 . LEU   B 2 1052 ? 126.315 118.517 95.825  1.00 46.89  ? 1052 LEU   A CD2 1 
ATOM   9199  N  N   . LYS   B 2 1053 ? 129.331 115.844 97.810  1.00 45.04  ? 1053 LYS   A N   1 
ATOM   9200  C  CA  . LYS   B 2 1053 ? 128.860 114.650 98.509  1.00 49.55  ? 1053 LYS   A CA  1 
ATOM   9201  C  C   . LYS   B 2 1053 ? 129.537 114.504 99.865  1.00 41.26  ? 1053 LYS   A C   1 
ATOM   9202  O  O   . LYS   B 2 1053 ? 128.867 114.365 100.898 1.00 47.74  ? 1053 LYS   A O   1 
ATOM   9203  C  CB  . LYS   B 2 1053 ? 129.107 113.405 97.661  1.00 51.91  ? 1053 LYS   A CB  1 
ATOM   9204  C  CG  . LYS   B 2 1053 ? 128.653 112.120 98.326  1.00 45.86  ? 1053 LYS   A CG  1 
ATOM   9205  C  CD  . LYS   B 2 1053 ? 129.821 111.203 98.628  1.00 49.87  ? 1053 LYS   A CD  1 
ATOM   9206  C  CE  . LYS   B 2 1053 ? 129.354 109.952 99.346  1.00 48.42  ? 1053 LYS   A CE  1 
ATOM   9207  N  NZ  . LYS   B 2 1053 ? 130.414 108.913 99.403  1.00 45.92  ? 1053 LYS   A NZ  1 
ATOM   9208  N  N   . ARG   B 2 1054 ? 130.870 114.545 99.881  1.00 41.69  ? 1054 ARG   A N   1 
ATOM   9209  C  CA  . ARG   B 2 1054 ? 131.580 114.433 101.153 1.00 40.33  ? 1054 ARG   A CA  1 
ATOM   9210  C  C   . ARG   B 2 1054 ? 131.261 115.609 102.067 1.00 42.61  ? 1054 ARG   A C   1 
ATOM   9211  O  O   . ARG   B 2 1054 ? 130.979 115.425 103.257 1.00 45.69  ? 1054 ARG   A O   1 
ATOM   9212  C  CB  . ARG   B 2 1054 ? 133.087 114.334 100.938 1.00 46.00  ? 1054 ARG   A CB  1 
ATOM   9213  C  CG  . ARG   B 2 1054 ? 133.848 114.515 102.242 1.00 46.81  ? 1054 ARG   A CG  1 
ATOM   9214  C  CD  . ARG   B 2 1054 ? 135.310 114.159 102.140 1.00 45.87  ? 1054 ARG   A CD  1 
ATOM   9215  N  NE  . ARG   B 2 1054 ? 135.982 114.344 103.420 1.00 42.58  ? 1054 ARG   A NE  1 
ATOM   9216  C  CZ  . ARG   B 2 1054 ? 136.053 113.423 104.370 1.00 44.05  ? 1054 ARG   A CZ  1 
ATOM   9217  N  NH1 . ARG   B 2 1054 ? 135.506 112.230 104.218 1.00 41.72  ? 1054 ARG   A NH1 1 
ATOM   9218  N  NH2 . ARG   B 2 1054 ? 136.688 113.707 105.503 1.00 43.47  ? 1054 ARG   A NH2 1 
ATOM   9219  N  N   . LEU   B 2 1055 ? 131.311 116.831 101.526 1.00 45.80  ? 1055 LEU   A N   1 
ATOM   9220  C  CA  . LEU   B 2 1055 ? 130.999 118.034 102.287 1.00 40.12  ? 1055 LEU   A CA  1 
ATOM   9221  C  C   . LEU   B 2 1055 ? 129.724 117.851 103.088 1.00 36.50  ? 1055 LEU   A C   1 
ATOM   9222  O  O   . LEU   B 2 1055 ? 129.746 117.872 104.321 1.00 48.83  ? 1055 LEU   A O   1 
ATOM   9223  C  CB  . LEU   B 2 1055 ? 130.877 119.224 101.334 1.00 39.35  ? 1055 LEU   A CB  1 
ATOM   9224  C  CG  . LEU   B 2 1055 ? 130.658 120.609 101.938 1.00 38.22  ? 1055 LEU   A CG  1 
ATOM   9225  C  CD1 . LEU   B 2 1055 ? 131.859 121.021 102.767 1.00 47.33  ? 1055 LEU   A CD1 1 
ATOM   9226  C  CD2 . LEU   B 2 1055 ? 130.381 121.624 100.846 1.00 38.35  ? 1055 LEU   A CD2 1 
ATOM   9227  N  N   . LEU   B 2 1056 ? 128.615 117.590 102.401 1.00 39.05  ? 1056 LEU   A N   1 
ATOM   9228  C  CA  . LEU   B 2 1056 ? 127.364 117.334 103.099 1.00 41.08  ? 1056 LEU   A CA  1 
ATOM   9229  C  C   . LEU   B 2 1056 ? 127.540 116.198 104.098 1.00 43.87  ? 1056 LEU   A C   1 
ATOM   9230  O  O   . LEU   B 2 1056 ? 127.581 116.459 105.305 1.00 40.89  ? 1056 LEU   A O   1 
ATOM   9231  C  CB  . LEU   B 2 1056 ? 126.246 117.009 102.107 1.00 38.48  ? 1056 LEU   A CB  1 
ATOM   9232  C  CG  . LEU   B 2 1056 ? 125.282 118.148 101.775 1.00 38.14  ? 1056 LEU   A CG  1 
ATOM   9233  C  CD1 . LEU   B 2 1056 ? 126.036 119.368 101.288 1.00 42.83  ? 1056 LEU   A CD1 1 
ATOM   9234  C  CD2 . LEU   B 2 1056 ? 124.272 117.699 100.743 1.00 36.62  ? 1056 LEU   A CD2 1 
ATOM   9235  N  N   . LEU   B 2 1057 ? 127.799 114.981 103.602 1.00 43.96  ? 1057 LEU   A N   1 
ATOM   9236  C  CA  . LEU   B 2 1057 ? 127.622 113.786 104.423 1.00 39.50  ? 1057 LEU   A CA  1 
ATOM   9237  C  C   . LEU   B 2 1057 ? 128.447 113.828 105.704 1.00 41.72  ? 1057 LEU   A C   1 
ATOM   9238  O  O   . LEU   B 2 1057 ? 127.966 113.410 106.762 1.00 47.74  ? 1057 LEU   A O   1 
ATOM   9239  C  CB  . LEU   B 2 1057 ? 127.954 112.534 103.615 1.00 42.01  ? 1057 LEU   A CB  1 
ATOM   9240  C  CG  . LEU   B 2 1057 ? 126.859 112.073 102.654 1.00 43.25  ? 1057 LEU   A CG  1 
ATOM   9241  C  CD1 . LEU   B 2 1057 ? 127.144 110.668 102.164 1.00 48.01  ? 1057 LEU   A CD1 1 
ATOM   9242  C  CD2 . LEU   B 2 1057 ? 125.500 112.148 103.318 1.00 40.10  ? 1057 LEU   A CD2 1 
ATOM   9243  N  N   . VAL   B 2 1058 ? 129.685 114.313 105.646 1.00 41.11  ? 1058 VAL   A N   1 
ATOM   9244  C  CA  . VAL   B 2 1058 ? 130.488 114.347 106.866 1.00 34.18  ? 1058 VAL   A CA  1 
ATOM   9245  C  C   . VAL   B 2 1058 ? 130.461 115.724 107.523 1.00 37.58  ? 1058 VAL   A C   1 
ATOM   9246  O  O   . VAL   B 2 1058 ? 130.129 115.839 108.706 1.00 43.76  ? 1058 VAL   A O   1 
ATOM   9247  C  CB  . VAL   B 2 1058 ? 131.934 113.853 106.603 1.00 33.47  ? 1058 VAL   A CB  1 
ATOM   9248  C  CG1 . VAL   B 2 1058 ? 131.914 112.433 106.065 1.00 42.91  ? 1058 VAL   A CG1 1 
ATOM   9249  C  CG2 . VAL   B 2 1058 ? 132.706 114.761 105.663 1.00 40.09  ? 1058 VAL   A CG2 1 
ATOM   9250  N  N   . HIS   B 2 1059 ? 130.795 116.795 106.794 1.00 35.18  ? 1059 HIS   A N   1 
ATOM   9251  C  CA  . HIS   B 2 1059 ? 130.960 118.085 107.447 1.00 29.55  ? 1059 HIS   A CA  1 
ATOM   9252  C  C   . HIS   B 2 1059 ? 129.633 118.628 107.955 1.00 35.73  ? 1059 HIS   A C   1 
ATOM   9253  O  O   . HIS   B 2 1059 ? 129.568 119.138 109.076 1.00 42.78  ? 1059 HIS   A O   1 
ATOM   9254  C  CB  . HIS   B 2 1059 ? 131.619 119.079 106.494 1.00 28.73  ? 1059 HIS   A CB  1 
ATOM   9255  C  CG  . HIS   B 2 1059 ? 133.077 118.826 106.275 1.00 30.27  ? 1059 HIS   A CG  1 
ATOM   9256  N  ND1 . HIS   B 2 1059 ? 134.025 119.051 107.248 1.00 38.73  ? 1059 HIS   A ND1 1 
ATOM   9257  C  CD2 . HIS   B 2 1059 ? 133.750 118.368 105.194 1.00 30.31  ? 1059 HIS   A CD2 1 
ATOM   9258  C  CE1 . HIS   B 2 1059 ? 135.218 118.739 106.779 1.00 42.70  ? 1059 HIS   A CE1 1 
ATOM   9259  N  NE2 . HIS   B 2 1059 ? 135.080 118.324 105.533 1.00 38.69  ? 1059 HIS   A NE2 1 
ATOM   9260  N  N   . GLY   B 2 1060 ? 128.563 118.540 107.161 1.00 37.17  ? 1060 GLY   A N   1 
ATOM   9261  C  CA  . GLY   B 2 1060 ? 127.296 119.076 107.621 1.00 40.68  ? 1060 GLY   A CA  1 
ATOM   9262  C  C   . GLY   B 2 1060 ? 126.743 118.309 108.804 1.00 43.89  ? 1060 GLY   A C   1 
ATOM   9263  O  O   . GLY   B 2 1060 ? 126.258 118.906 109.769 1.00 53.63  ? 1060 GLY   A O   1 
ATOM   9264  N  N   . HIS   B 2 1061 ? 126.818 116.978 108.753 1.00 35.12  ? 1061 HIS   A N   1 
ATOM   9265  C  CA  . HIS   B 2 1061 ? 126.334 116.161 109.859 1.00 30.51  ? 1061 HIS   A CA  1 
ATOM   9266  C  C   . HIS   B 2 1061 ? 127.121 116.448 111.129 1.00 34.26  ? 1061 HIS   A C   1 
ATOM   9267  O  O   . HIS   B 2 1061 ? 126.539 116.671 112.200 1.00 44.87  ? 1061 HIS   A O   1 
ATOM   9268  C  CB  . HIS   B 2 1061 ? 126.423 114.681 109.483 1.00 28.73  ? 1061 HIS   A CB  1 
ATOM   9269  C  CG  . HIS   B 2 1061 ? 125.601 113.781 110.351 1.00 33.48  ? 1061 HIS   A CG  1 
ATOM   9270  N  ND1 . HIS   B 2 1061 ? 125.063 112.598 109.894 1.00 34.20  ? 1061 HIS   A ND1 1 
ATOM   9271  C  CD2 . HIS   B 2 1061 ? 125.228 113.885 111.648 1.00 38.67  ? 1061 HIS   A CD2 1 
ATOM   9272  C  CE1 . HIS   B 2 1061 ? 124.392 112.014 110.869 1.00 35.81  ? 1061 HIS   A CE1 1 
ATOM   9273  N  NE2 . HIS   B 2 1061 ? 124.476 112.774 111.945 1.00 39.41  ? 1061 HIS   A NE2 1 
ATOM   9274  N  N   . TRP   B 2 1062 ? 128.453 116.473 111.024 1.00 36.73  ? 1062 TRP   A N   1 
ATOM   9275  C  CA  . TRP   B 2 1062 ? 129.279 116.745 112.193 1.00 28.76  ? 1062 TRP   A CA  1 
ATOM   9276  C  C   . TRP   B 2 1062 ? 129.034 118.145 112.735 1.00 35.71  ? 1062 TRP   A C   1 
ATOM   9277  O  O   . TRP   B 2 1062 ? 128.944 118.335 113.950 1.00 56.67  ? 1062 TRP   A O   1 
ATOM   9278  C  CB  . TRP   B 2 1062 ? 130.752 116.553 111.848 1.00 39.23  ? 1062 TRP   A CB  1 
ATOM   9279  C  CG  . TRP   B 2 1062 ? 131.216 115.144 111.999 1.00 37.77  ? 1062 TRP   A CG  1 
ATOM   9280  C  CD1 . TRP   B 2 1062 ? 130.527 114.114 112.558 1.00 37.99  ? 1062 TRP   A CD1 1 
ATOM   9281  C  CD2 . TRP   B 2 1062 ? 132.477 114.609 111.590 1.00 31.48  ? 1062 TRP   A CD2 1 
ATOM   9282  N  NE1 . TRP   B 2 1062 ? 131.278 112.969 112.522 1.00 34.18  ? 1062 TRP   A NE1 1 
ATOM   9283  C  CE2 . TRP   B 2 1062 ? 132.481 113.246 111.931 1.00 28.99  ? 1062 TRP   A CE2 1 
ATOM   9284  C  CE3 . TRP   B 2 1062 ? 133.604 115.149 110.965 1.00 41.70  ? 1062 TRP   A CE3 1 
ATOM   9285  C  CZ2 . TRP   B 2 1062 ? 133.564 112.417 111.672 1.00 38.46  ? 1062 TRP   A CZ2 1 
ATOM   9286  C  CZ3 . TRP   B 2 1062 ? 134.678 114.324 110.710 1.00 39.25  ? 1062 TRP   A CZ3 1 
ATOM   9287  C  CH2 . TRP   B 2 1062 ? 134.651 112.974 111.061 1.00 40.89  ? 1062 TRP   A CH2 1 
ATOM   9288  N  N   . SER   B 2 1063 ? 128.926 119.141 111.853 1.00 31.21  ? 1063 SER   A N   1 
ATOM   9289  C  CA  . SER   B 2 1063 ? 128.716 120.509 112.305 1.00 34.72  ? 1063 SER   A CA  1 
ATOM   9290  C  C   . SER   B 2 1063 ? 127.365 120.666 112.986 1.00 33.78  ? 1063 SER   A C   1 
ATOM   9291  O  O   . SER   B 2 1063 ? 127.262 121.326 114.025 1.00 47.20  ? 1063 SER   A O   1 
ATOM   9292  C  CB  . SER   B 2 1063 ? 128.844 121.471 111.127 1.00 38.43  ? 1063 SER   A CB  1 
ATOM   9293  O  OG  . SER   B 2 1063 ? 130.131 121.384 110.543 1.00 43.15  ? 1063 SER   A OG  1 
ATOM   9294  N  N   . TYR   B 2 1064 ? 126.318 120.059 112.425 1.00 27.63  ? 1064 TYR   A N   1 
ATOM   9295  C  CA  . TYR   B 2 1064 ? 125.002 120.122 113.048 1.00 28.45  ? 1064 TYR   A CA  1 
ATOM   9296  C  C   . TYR   B 2 1064 ? 125.021 119.465 114.421 1.00 38.70  ? 1064 TYR   A C   1 
ATOM   9297  O  O   . TYR   B 2 1064 ? 124.525 120.033 115.404 1.00 51.94  ? 1064 TYR   A O   1 
ATOM   9298  C  CB  . TYR   B 2 1064 ? 123.971 119.460 112.135 1.00 33.16  ? 1064 TYR   A CB  1 
ATOM   9299  C  CG  . TYR   B 2 1064 ? 122.552 119.548 112.631 1.00 34.34  ? 1064 TYR   A CG  1 
ATOM   9300  C  CD1 . TYR   B 2 1064 ? 122.041 120.741 113.109 1.00 47.68  ? 1064 TYR   A CD1 1 
ATOM   9301  C  CD2 . TYR   B 2 1064 ? 121.720 118.442 112.609 1.00 30.18  ? 1064 TYR   A CD2 1 
ATOM   9302  C  CE1 . TYR   B 2 1064 ? 120.745 120.828 113.563 1.00 44.07  ? 1064 TYR   A CE1 1 
ATOM   9303  C  CE2 . TYR   B 2 1064 ? 120.422 118.520 113.060 1.00 33.52  ? 1064 TYR   A CE2 1 
ATOM   9304  C  CZ  . TYR   B 2 1064 ? 119.940 119.716 113.534 1.00 38.95  ? 1064 TYR   A CZ  1 
ATOM   9305  O  OH  . TYR   B 2 1064 ? 118.647 119.803 113.986 1.00 44.07  ? 1064 TYR   A OH  1 
ATOM   9306  N  N   . PHE   B 2 1065 ? 125.620 118.275 114.512 1.00 34.97  ? 1065 PHE   A N   1 
ATOM   9307  C  CA  . PHE   B 2 1065 ? 125.701 117.572 115.787 1.00 32.68  ? 1065 PHE   A CA  1 
ATOM   9308  C  C   . PHE   B 2 1065 ? 126.458 118.396 116.821 1.00 41.33  ? 1065 PHE   A C   1 
ATOM   9309  O  O   . PHE   B 2 1065 ? 125.984 118.595 117.949 1.00 49.21  ? 1065 PHE   A O   1 
ATOM   9310  C  CB  . PHE   B 2 1065 ? 126.369 116.214 115.564 1.00 32.28  ? 1065 PHE   A CB  1 
ATOM   9311  C  CG  . PHE   B 2 1065 ? 126.617 115.438 116.819 1.00 40.47  ? 1065 PHE   A CG  1 
ATOM   9312  C  CD1 . PHE   B 2 1065 ? 125.586 114.772 117.451 1.00 44.39  ? 1065 PHE   A CD1 1 
ATOM   9313  C  CD2 . PHE   B 2 1065 ? 127.889 115.350 117.352 1.00 42.83  ? 1065 PHE   A CD2 1 
ATOM   9314  C  CE1 . PHE   B 2 1065 ? 125.814 114.051 118.601 1.00 46.51  ? 1065 PHE   A CE1 1 
ATOM   9315  C  CE2 . PHE   B 2 1065 ? 128.122 114.630 118.501 1.00 47.69  ? 1065 PHE   A CE2 1 
ATOM   9316  C  CZ  . PHE   B 2 1065 ? 127.084 113.979 119.126 1.00 46.57  ? 1065 PHE   A CZ  1 
ATOM   9317  N  N   . ARG   B 2 1066 ? 127.634 118.901 116.442 1.00 35.78  ? 1066 ARG   A N   1 
ATOM   9318  C  CA  . ARG   B 2 1066 ? 128.466 119.652 117.371 1.00 32.40  ? 1066 ARG   A CA  1 
ATOM   9319  C  C   . ARG   B 2 1066 ? 127.783 120.933 117.823 1.00 38.80  ? 1066 ARG   A C   1 
ATOM   9320  O  O   . ARG   B 2 1066 ? 127.796 121.260 119.013 1.00 53.26  ? 1066 ARG   A O   1 
ATOM   9321  C  CB  . ARG   B 2 1066 ? 129.811 119.969 116.724 1.00 31.89  ? 1066 ARG   A CB  1 
ATOM   9322  C  CG  . ARG   B 2 1066 ? 130.683 118.761 116.461 1.00 33.41  ? 1066 ARG   A CG  1 
ATOM   9323  C  CD  . ARG   B 2 1066 ? 131.799 119.116 115.500 1.00 36.20  ? 1066 ARG   A CD  1 
ATOM   9324  N  NE  . ARG   B 2 1066 ? 132.684 117.989 115.241 1.00 36.88  ? 1066 ARG   A NE  1 
ATOM   9325  C  CZ  . ARG   B 2 1066 ? 133.649 117.992 114.333 1.00 35.95  ? 1066 ARG   A CZ  1 
ATOM   9326  N  NH1 . ARG   B 2 1066 ? 133.868 119.043 113.563 1.00 38.41  ? 1066 ARG   A NH1 1 
ATOM   9327  N  NH2 . ARG   B 2 1066 ? 134.413 116.913 114.195 1.00 38.17  ? 1066 ARG   A NH2 1 
ATOM   9328  N  N   . ASN   B 2 1067 ? 127.185 121.678 116.890 1.00 28.63  ? 1067 ASN   A N   1 
ATOM   9329  C  CA  . ASN   B 2 1067 ? 126.535 122.929 117.258 1.00 30.89  ? 1067 ASN   A CA  1 
ATOM   9330  C  C   . ASN   B 2 1067 ? 125.341 122.688 118.170 1.00 34.74  ? 1067 ASN   A C   1 
ATOM   9331  O  O   . ASN   B 2 1067 ? 125.163 123.403 119.165 1.00 55.92  ? 1067 ASN   A O   1 
ATOM   9332  C  CB  . ASN   B 2 1067 ? 126.116 123.689 116.001 1.00 37.59  ? 1067 ASN   A CB  1 
ATOM   9333  C  CG  . ASN   B 2 1067 ? 127.299 124.233 115.228 1.00 40.41  ? 1067 ASN   A CG  1 
ATOM   9334  O  OD1 . ASN   B 2 1067 ? 128.435 123.804 115.425 1.00 41.52  ? 1067 ASN   A OD1 1 
ATOM   9335  N  ND2 . ASN   B 2 1067 ? 127.039 125.186 114.345 1.00 44.78  ? 1067 ASN   A ND2 1 
ATOM   9336  N  N   . SER   B 2 1068 ? 124.519 121.681 117.860 1.00 28.87  ? 1068 SER   A N   1 
ATOM   9337  C  CA  . SER   B 2 1068 ? 123.378 121.381 118.716 1.00 33.63  ? 1068 SER   A CA  1 
ATOM   9338  C  C   . SER   B 2 1068 ? 123.834 121.019 120.123 1.00 41.06  ? 1068 SER   A C   1 
ATOM   9339  O  O   . SER   B 2 1068 ? 123.331 121.567 121.114 1.00 53.87  ? 1068 SER   A O   1 
ATOM   9340  C  CB  . SER   B 2 1068 ? 122.553 120.249 118.107 1.00 38.91  ? 1068 SER   A CB  1 
ATOM   9341  O  OG  . SER   B 2 1068 ? 122.155 120.565 116.786 1.00 42.87  ? 1068 SER   A OG  1 
ATOM   9342  N  N   . SER   B 2 1069 ? 124.808 120.110 120.228 1.00 32.16  ? 1069 SER   A N   1 
ATOM   9343  C  CA  . SER   B 2 1069 ? 125.279 119.693 121.542 1.00 34.38  ? 1069 SER   A CA  1 
ATOM   9344  C  C   . SER   B 2 1069 ? 125.895 120.857 122.306 1.00 38.04  ? 1069 SER   A C   1 
ATOM   9345  O  O   . SER   B 2 1069 ? 125.661 121.011 123.511 1.00 51.21  ? 1069 SER   A O   1 
ATOM   9346  C  CB  . SER   B 2 1069 ? 126.281 118.549 121.400 1.00 42.41  ? 1069 SER   A CB  1 
ATOM   9347  O  OG  . SER   B 2 1069 ? 125.689 117.421 120.782 1.00 49.13  ? 1069 SER   A OG  1 
ATOM   9348  N  N   . MET   B 2 1070 ? 126.675 121.696 121.620 1.00 31.62  ? 1070 MET   A N   1 
ATOM   9349  C  CA  . MET   B 2 1070 ? 127.332 122.816 122.282 1.00 35.37  ? 1070 MET   A CA  1 
ATOM   9350  C  C   . MET   B 2 1070 ? 126.319 123.817 122.819 1.00 37.59  ? 1070 MET   A C   1 
ATOM   9351  O  O   . MET   B 2 1070 ? 126.437 124.284 123.958 1.00 49.28  ? 1070 MET   A O   1 
ATOM   9352  C  CB  . MET   B 2 1070 ? 128.298 123.496 121.315 1.00 37.07  ? 1070 MET   A CB  1 
ATOM   9353  C  CG  . MET   B 2 1070 ? 128.908 124.764 121.864 1.00 44.66  ? 1070 MET   A CG  1 
ATOM   9354  S  SD  . MET   B 2 1070 ? 129.996 125.593 120.704 1.00 55.50  ? 1070 MET   A SD  1 
ATOM   9355  C  CE  . MET   B 2 1070 ? 128.846 125.984 119.390 1.00 46.49  ? 1070 MET   A CE  1 
ATOM   9356  N  N   . ILE   B 2 1071 ? 125.312 124.161 122.014 1.00 27.82  ? 1071 ILE   A N   1 
ATOM   9357  C  CA  . ILE   B 2 1071 ? 124.310 125.121 122.469 1.00 38.42  ? 1071 ILE   A CA  1 
ATOM   9358  C  C   . ILE   B 2 1071 ? 123.520 124.555 123.641 1.00 42.65  ? 1071 ILE   A C   1 
ATOM   9359  O  O   . ILE   B 2 1071 ? 123.261 125.254 124.634 1.00 51.46  ? 1071 ILE   A O   1 
ATOM   9360  C  CB  . ILE   B 2 1071 ? 123.391 125.528 121.304 1.00 37.05  ? 1071 ILE   A CB  1 
ATOM   9361  C  CG1 . ILE   B 2 1071 ? 124.198 126.243 120.225 1.00 34.06  ? 1071 ILE   A CG1 1 
ATOM   9362  C  CG2 . ILE   B 2 1071 ? 122.270 126.422 121.797 1.00 45.87  ? 1071 ILE   A CG2 1 
ATOM   9363  C  CD1 . ILE   B 2 1071 ? 123.376 126.678 119.050 1.00 41.33  ? 1071 ILE   A CD1 1 
ATOM   9364  N  N   . LEU   B 2 1072 ? 123.129 123.280 123.553 1.00 35.10  ? 1072 LEU   A N   1 
ATOM   9365  C  CA  . LEU   B 2 1072 ? 122.373 122.680 124.646 1.00 25.32  ? 1072 LEU   A CA  1 
ATOM   9366  C  C   . LEU   B 2 1072 ? 123.192 122.639 125.930 1.00 35.95  ? 1072 LEU   A C   1 
ATOM   9367  O  O   . LEU   B 2 1072 ? 122.671 122.927 127.013 1.00 50.12  ? 1072 LEU   A O   1 
ATOM   9368  C  CB  . LEU   B 2 1072 ? 121.898 121.284 124.251 1.00 39.31  ? 1072 LEU   A CB  1 
ATOM   9369  C  CG  . LEU   B 2 1072 ? 120.887 121.262 123.103 1.00 35.98  ? 1072 LEU   A CG  1 
ATOM   9370  C  CD1 . LEU   B 2 1072 ? 120.429 119.848 122.810 1.00 40.89  ? 1072 LEU   A CD1 1 
ATOM   9371  C  CD2 . LEU   B 2 1072 ? 119.705 122.150 123.414 1.00 33.53  ? 1072 LEU   A CD2 1 
ATOM   9372  N  N   . ASN   B 2 1073 ? 124.483 122.312 125.831 1.00 29.45  ? 1073 ASN   A N   1 
ATOM   9373  C  CA  . ASN   B 2 1073 ? 125.322 122.263 127.025 1.00 32.98  ? 1073 ASN   A CA  1 
ATOM   9374  C  C   . ASN   B 2 1073 ? 125.561 123.653 127.605 1.00 42.69  ? 1073 ASN   A C   1 
ATOM   9375  O  O   . ASN   B 2 1073 ? 125.626 123.816 128.831 1.00 50.16  ? 1073 ASN   A O   1 
ATOM   9376  C  CB  . ASN   B 2 1073 ? 126.646 121.573 126.702 1.00 33.30  ? 1073 ASN   A CB  1 
ATOM   9377  C  CG  . ASN   B 2 1073 ? 126.498 120.073 126.565 1.00 48.49  ? 1073 ASN   A CG  1 
ATOM   9378  O  OD1 . ASN   B 2 1073 ? 126.696 119.329 127.523 1.00 55.83  ? 1073 ASN   A OD1 1 
ATOM   9379  N  ND2 . ASN   B 2 1073 ? 126.138 119.620 125.372 1.00 48.45  ? 1073 ASN   A ND2 1 
ATOM   9380  N  N   . PHE   B 2 1074 ? 125.703 124.664 126.745 1.00 35.54  ? 1074 PHE   A N   1 
ATOM   9381  C  CA  . PHE   B 2 1074 ? 125.841 126.036 127.227 1.00 29.45  ? 1074 PHE   A CA  1 
ATOM   9382  C  C   . PHE   B 2 1074 ? 124.615 126.453 128.027 1.00 35.00  ? 1074 PHE   A C   1 
ATOM   9383  O  O   . PHE   B 2 1074 ? 124.727 126.964 129.156 1.00 49.86  ? 1074 PHE   A O   1 
ATOM   9384  C  CB  . PHE   B 2 1074 ? 126.051 126.977 126.041 1.00 35.79  ? 1074 PHE   A CB  1 
ATOM   9385  C  CG  . PHE   B 2 1074 ? 127.179 127.942 126.222 1.00 39.38  ? 1074 PHE   A CG  1 
ATOM   9386  C  CD1 . PHE   B 2 1074 ? 127.047 129.032 127.058 1.00 37.89  ? 1074 PHE   A CD1 1 
ATOM   9387  C  CD2 . PHE   B 2 1074 ? 128.368 127.767 125.545 1.00 46.02  ? 1074 PHE   A CD2 1 
ATOM   9388  C  CE1 . PHE   B 2 1074 ? 128.084 129.921 127.225 1.00 43.10  ? 1074 PHE   A CE1 1 
ATOM   9389  C  CE2 . PHE   B 2 1074 ? 129.409 128.654 125.707 1.00 43.13  ? 1074 PHE   A CE2 1 
ATOM   9390  C  CZ  . PHE   B 2 1074 ? 129.267 129.732 126.547 1.00 41.31  ? 1074 PHE   A CZ  1 
ATOM   9391  N  N   . PHE   B 2 1075 ? 123.430 126.224 127.456 1.00 36.84  ? 1075 PHE   A N   1 
ATOM   9392  C  CA  . PHE   B 2 1075 ? 122.196 126.521 128.173 1.00 35.74  ? 1075 PHE   A CA  1 
ATOM   9393  C  C   . PHE   B 2 1075 ? 122.123 125.742 129.477 1.00 41.05  ? 1075 PHE   A C   1 
ATOM   9394  O  O   . PHE   B 2 1075 ? 121.715 126.285 130.509 1.00 49.90  ? 1075 PHE   A O   1 
ATOM   9395  C  CB  . PHE   B 2 1075 ? 120.988 126.208 127.293 1.00 35.02  ? 1075 PHE   A CB  1 
ATOM   9396  C  CG  . PHE   B 2 1075 ? 120.661 127.286 126.303 1.00 42.17  ? 1075 PHE   A CG  1 
ATOM   9397  C  CD1 . PHE   B 2 1075 ? 120.737 128.619 126.662 1.00 43.90  ? 1075 PHE   A CD1 1 
ATOM   9398  C  CD2 . PHE   B 2 1075 ? 120.279 126.968 125.014 1.00 41.68  ? 1075 PHE   A CD2 1 
ATOM   9399  C  CE1 . PHE   B 2 1075 ? 120.434 129.611 125.754 1.00 43.16  ? 1075 PHE   A CE1 1 
ATOM   9400  C  CE2 . PHE   B 2 1075 ? 119.979 127.959 124.103 1.00 38.44  ? 1075 PHE   A CE2 1 
ATOM   9401  C  CZ  . PHE   B 2 1075 ? 120.057 129.279 124.474 1.00 41.68  ? 1075 PHE   A CZ  1 
ATOM   9402  N  N   . TYR   B 2 1076 ? 122.537 124.474 129.455 1.00 36.63  ? 1076 TYR   A N   1 
ATOM   9403  C  CA  . TYR   B 2 1076 ? 122.465 123.642 130.650 1.00 33.27  ? 1076 TYR   A CA  1 
ATOM   9404  C  C   . TYR   B 2 1076 ? 123.336 124.194 131.772 1.00 36.05  ? 1076 TYR   A C   1 
ATOM   9405  O  O   . TYR   B 2 1076 ? 122.897 124.285 132.923 1.00 48.62  ? 1076 TYR   A O   1 
ATOM   9406  C  CB  . TYR   B 2 1076 ? 122.875 122.211 130.309 1.00 37.16  ? 1076 TYR   A CB  1 
ATOM   9407  C  CG  . TYR   B 2 1076 ? 123.426 121.445 131.485 1.00 29.85  ? 1076 TYR   A CG  1 
ATOM   9408  C  CD1 . TYR   B 2 1076 ? 122.582 120.796 132.368 1.00 34.12  ? 1076 TYR   A CD1 1 
ATOM   9409  C  CD2 . TYR   B 2 1076 ? 124.794 121.372 131.710 1.00 38.93  ? 1076 TYR   A CD2 1 
ATOM   9410  C  CE1 . TYR   B 2 1076 ? 123.080 120.102 133.440 1.00 41.09  ? 1076 TYR   A CE1 1 
ATOM   9411  C  CE2 . TYR   B 2 1076 ? 125.299 120.685 132.783 1.00 41.29  ? 1076 TYR   A CE2 1 
ATOM   9412  C  CZ  . TYR   B 2 1076 ? 124.439 120.050 133.645 1.00 40.70  ? 1076 TYR   A CZ  1 
ATOM   9413  O  OH  . TYR   B 2 1076 ? 124.943 119.355 134.718 1.00 41.71  ? 1076 TYR   A OH  1 
ATOM   9414  N  N   . LYS   B 2 1077 ? 124.584 124.549 131.465 1.00 17.52  ? 1077 LYS   A N   1 
ATOM   9415  C  CA  . LYS   B 2 1077 ? 125.483 124.997 132.526 1.00 31.42  ? 1077 LYS   A CA  1 
ATOM   9416  C  C   . LYS   B 2 1077 ? 125.055 126.352 133.079 1.00 40.28  ? 1077 LYS   A C   1 
ATOM   9417  O  O   . LYS   B 2 1077 ? 125.091 126.582 134.304 1.00 47.59  ? 1077 LYS   A O   1 
ATOM   9418  C  CB  . LYS   B 2 1077 ? 126.928 125.028 132.023 1.00 35.35  ? 1077 LYS   A CB  1 
ATOM   9419  C  CG  . LYS   B 2 1077 ? 127.198 125.914 130.826 1.00 38.26  ? 1077 LYS   A CG  1 
ATOM   9420  C  CD  . LYS   B 2 1077 ? 128.577 125.626 130.256 1.00 34.86  ? 1077 LYS   A CD  1 
ATOM   9421  C  CE  . LYS   B 2 1077 ? 129.018 126.684 129.262 1.00 32.22  ? 1077 LYS   A CE  1 
ATOM   9422  N  NZ  . LYS   B 2 1077 ? 129.237 127.996 129.919 1.00 42.16  ? 1077 LYS   A NZ  1 
ATOM   9423  N  N   . ASN   B 2 1078 ? 124.621 127.257 132.200 1.00 34.38  ? 1078 ASN   A N   1 
ATOM   9424  C  CA  . ASN   B 2 1078 ? 124.131 128.535 132.698 1.00 32.82  ? 1078 ASN   A CA  1 
ATOM   9425  C  C   . ASN   B 2 1078 ? 122.871 128.350 133.535 1.00 32.79  ? 1078 ASN   A C   1 
ATOM   9426  O  O   . ASN   B 2 1078 ? 122.679 129.047 134.540 1.00 39.89  ? 1078 ASN   A O   1 
ATOM   9427  C  CB  . ASN   B 2 1078 ? 123.899 129.485 131.533 1.00 39.74  ? 1078 ASN   A CB  1 
ATOM   9428  C  CG  . ASN   B 2 1078 ? 125.187 129.858 130.838 1.00 43.48  ? 1078 ASN   A CG  1 
ATOM   9429  O  OD1 . ASN   B 2 1078 ? 125.884 130.781 131.253 1.00 49.28  ? 1078 ASN   A OD1 1 
ATOM   9430  N  ND2 . ASN   B 2 1078 ? 125.519 129.128 129.783 1.00 42.42  ? 1078 ASN   A ND2 1 
ATOM   9431  N  N   . ILE   B 2 1079 ? 122.016 127.400 133.154 1.00 25.61  ? 1079 ILE   A N   1 
ATOM   9432  C  CA  . ILE   B 2 1079 ? 120.841 127.092 133.957 1.00 21.68  ? 1079 ILE   A CA  1 
ATOM   9433  C  C   . ILE   B 2 1079 ? 121.249 126.510 135.301 1.00 24.61  ? 1079 ILE   A C   1 
ATOM   9434  O  O   . ILE   B 2 1079 ? 120.597 126.763 136.313 1.00 31.15  ? 1079 ILE   A O   1 
ATOM   9435  C  CB  . ILE   B 2 1079 ? 119.898 126.154 133.184 1.00 27.25  ? 1079 ILE   A CB  1 
ATOM   9436  C  CG1 . ILE   B 2 1079 ? 119.076 126.958 132.180 1.00 34.66  ? 1079 ILE   A CG1 1 
ATOM   9437  C  CG2 . ILE   B 2 1079 ? 118.981 125.398 134.124 1.00 31.83  ? 1079 ILE   A CG2 1 
ATOM   9438  C  CD1 . ILE   B 2 1079 ? 118.169 127.983 132.816 1.00 37.75  ? 1079 ILE   A CD1 1 
ATOM   9439  N  N   . ILE   B 2 1080 ? 122.328 125.730 135.341 1.00 37.17  ? 1080 ILE   A N   1 
ATOM   9440  C  CA  . ILE   B 2 1080 ? 122.814 125.205 136.617 1.00 34.96  ? 1080 ILE   A CA  1 
ATOM   9441  C  C   . ILE   B 2 1080 ? 123.150 126.350 137.564 1.00 40.74  ? 1080 ILE   A C   1 
ATOM   9442  O  O   . ILE   B 2 1080 ? 122.683 126.397 138.714 1.00 52.64  ? 1080 ILE   A O   1 
ATOM   9443  C  CB  . ILE   B 2 1080 ? 124.033 124.291 136.394 1.00 35.40  ? 1080 ILE   A CB  1 
ATOM   9444  C  CG1 . ILE   B 2 1080 ? 123.605 122.955 135.792 1.00 42.15  ? 1080 ILE   A CG1 1 
ATOM   9445  C  CG2 . ILE   B 2 1080 ? 124.777 124.063 137.696 1.00 34.69  ? 1080 ILE   A CG2 1 
ATOM   9446  C  CD1 . ILE   B 2 1080 ? 122.869 122.075 136.758 1.00 44.46  ? 1080 ILE   A CD1 1 
ATOM   9447  N  N   . GLY   B 2 1081 ? 123.949 127.305 137.083 1.00 38.70  ? 1081 GLY   A N   1 
ATOM   9448  C  CA  . GLY   B 2 1081 ? 124.315 128.432 137.936 1.00 38.80  ? 1081 GLY   A CA  1 
ATOM   9449  C  C   . GLY   B 2 1081 ? 123.113 129.256 138.368 1.00 36.33  ? 1081 GLY   A C   1 
ATOM   9450  O  O   . GLY   B 2 1081 ? 122.920 129.542 139.562 1.00 43.56  ? 1081 GLY   A O   1 
ATOM   9451  N  N   . ILE   B 2 1082 ? 122.266 129.623 137.402 1.00 33.06  ? 1082 ILE   A N   1 
ATOM   9452  C  CA  . ILE   B 2 1082 ? 121.091 130.433 137.701 1.00 35.53  ? 1082 ILE   A CA  1 
ATOM   9453  C  C   . ILE   B 2 1082 ? 120.147 129.690 138.633 1.00 37.00  ? 1082 ILE   A C   1 
ATOM   9454  O  O   . ILE   B 2 1082 ? 119.506 130.300 139.494 1.00 46.70  ? 1082 ILE   A O   1 
ATOM   9455  C  CB  . ILE   B 2 1082 ? 120.394 130.847 136.390 1.00 40.76  ? 1082 ILE   A CB  1 
ATOM   9456  C  CG1 . ILE   B 2 1082 ? 121.315 131.752 135.574 1.00 45.80  ? 1082 ILE   A CG1 1 
ATOM   9457  C  CG2 . ILE   B 2 1082 ? 119.072 131.540 136.663 1.00 44.72  ? 1082 ILE   A CG2 1 
ATOM   9458  C  CD1 . ILE   B 2 1082 ? 121.894 132.896 136.370 1.00 40.02  ? 1082 ILE   A CD1 1 
ATOM   9459  N  N   . GLY   B 2 1083 ? 120.046 128.370 138.485 1.00 34.34  ? 1083 GLY   A N   1 
ATOM   9460  C  CA  . GLY   B 2 1083 ? 119.163 127.596 139.333 1.00 41.07  ? 1083 GLY   A CA  1 
ATOM   9461  C  C   . GLY   B 2 1083 ? 119.640 127.532 140.765 1.00 38.85  ? 1083 GLY   A C   1 
ATOM   9462  O  O   . GLY   B 2 1083 ? 118.833 127.599 141.693 1.00 47.86  ? 1083 GLY   A O   1 
ATOM   9463  N  N   . VAL   B 2 1084 ? 120.949 127.386 140.974 1.00 27.20  ? 1084 VAL   A N   1 
ATOM   9464  C  CA  . VAL   B 2 1084 ? 121.446 127.441 142.347 1.00 28.36  ? 1084 VAL   A CA  1 
ATOM   9465  C  C   . VAL   B 2 1084 ? 121.133 128.800 142.960 1.00 33.32  ? 1084 VAL   A C   1 
ATOM   9466  O  O   . VAL   B 2 1084 ? 120.656 128.894 144.105 1.00 42.21  ? 1084 VAL   A O   1 
ATOM   9467  C  CB  . VAL   B 2 1084 ? 122.949 127.122 142.405 1.00 35.23  ? 1084 VAL   A CB  1 
ATOM   9468  C  CG1 . VAL   B 2 1084 ? 123.416 127.135 143.841 1.00 34.38  ? 1084 VAL   A CG1 1 
ATOM   9469  C  CG2 . VAL   B 2 1084 ? 123.226 125.769 141.782 1.00 41.23  ? 1084 VAL   A CG2 1 
ATOM   9470  N  N   . LEU   B 2 1085 ? 121.354 129.875 142.193 1.00 33.23  ? 1085 LEU   A N   1 
ATOM   9471  C  CA  . LEU   B 2 1085 ? 121.000 131.204 142.688 1.00 29.05  ? 1085 LEU   A CA  1 
ATOM   9472  C  C   . LEU   B 2 1085 ? 119.516 131.295 143.039 1.00 27.58  ? 1085 LEU   A C   1 
ATOM   9473  O  O   . LEU   B 2 1085 ? 119.148 131.823 144.093 1.00 39.23  ? 1085 LEU   A O   1 
ATOM   9474  C  CB  . LEU   B 2 1085 ? 121.368 132.267 141.655 1.00 29.45  ? 1085 LEU   A CB  1 
ATOM   9475  C  CG  . LEU   B 2 1085 ? 122.850 132.504 141.368 1.00 33.32  ? 1085 LEU   A CG  1 
ATOM   9476  C  CD1 . LEU   B 2 1085 ? 123.006 133.399 140.157 1.00 40.09  ? 1085 LEU   A CD1 1 
ATOM   9477  C  CD2 . LEU   B 2 1085 ? 123.532 133.122 142.566 1.00 37.12  ? 1085 LEU   A CD2 1 
ATOM   9478  N  N   . PHE   B 2 1086 ? 118.651 130.769 142.172 1.00 26.69  ? 1086 PHE   A N   1 
ATOM   9479  C  CA  . PHE   B 2 1086 ? 117.207 130.856 142.378 1.00 27.35  ? 1086 PHE   A CA  1 
ATOM   9480  C  C   . PHE   B 2 1086 ? 116.767 130.062 143.603 1.00 33.09  ? 1086 PHE   A C   1 
ATOM   9481  O  O   . PHE   B 2 1086 ? 115.972 130.543 144.427 1.00 45.34  ? 1086 PHE   A O   1 
ATOM   9482  C  CB  . PHE   B 2 1086 ? 116.495 130.358 141.119 1.00 33.14  ? 1086 PHE   A CB  1 
ATOM   9483  C  CG  . PHE   B 2 1086 ? 115.003 130.319 141.232 1.00 35.73  ? 1086 PHE   A CG  1 
ATOM   9484  C  CD1 . PHE   B 2 1086 ? 114.254 131.464 141.048 1.00 42.22  ? 1086 PHE   A CD1 1 
ATOM   9485  C  CD2 . PHE   B 2 1086 ? 114.347 129.133 141.501 1.00 31.09  ? 1086 PHE   A CD2 1 
ATOM   9486  C  CE1 . PHE   B 2 1086 ? 112.882 131.430 141.144 1.00 42.67  ? 1086 PHE   A CE1 1 
ATOM   9487  C  CE2 . PHE   B 2 1086 ? 112.975 129.095 141.596 1.00 34.33  ? 1086 PHE   A CE2 1 
ATOM   9488  C  CZ  . PHE   B 2 1086 ? 112.242 130.245 141.419 1.00 36.96  ? 1086 PHE   A CZ  1 
ATOM   9489  N  N   . TRP   B 2 1087 ? 117.271 128.836 143.737 1.00 40.74  ? 1087 TRP   A N   1 
ATOM   9490  C  CA  . TRP   B 2 1087 ? 116.909 128.017 144.883 1.00 31.94  ? 1087 TRP   A CA  1 
ATOM   9491  C  C   . TRP   B 2 1087 ? 117.375 128.655 146.179 1.00 33.60  ? 1087 TRP   A C   1 
ATOM   9492  O  O   . TRP   B 2 1087 ? 116.724 128.488 147.216 1.00 39.65  ? 1087 TRP   A O   1 
ATOM   9493  C  CB  . TRP   B 2 1087 ? 117.482 126.607 144.735 1.00 37.75  ? 1087 TRP   A CB  1 
ATOM   9494  C  CG  . TRP   B 2 1087 ? 116.930 125.834 143.569 1.00 25.47  ? 1087 TRP   A CG  1 
ATOM   9495  C  CD1 . TRP   B 2 1087 ? 117.646 125.204 142.600 1.00 27.71  ? 1087 TRP   A CD1 1 
ATOM   9496  C  CD2 . TRP   B 2 1087 ? 115.550 125.607 143.255 1.00 24.11  ? 1087 TRP   A CD2 1 
ATOM   9497  N  NE1 . TRP   B 2 1087 ? 116.805 124.606 141.700 1.00 34.30  ? 1087 TRP   A NE1 1 
ATOM   9498  C  CE2 . TRP   B 2 1087 ? 115.512 124.836 142.082 1.00 29.88  ? 1087 TRP   A CE2 1 
ATOM   9499  C  CE3 . TRP   B 2 1087 ? 114.345 125.981 143.853 1.00 38.80  ? 1087 TRP   A CE3 1 
ATOM   9500  C  CZ2 . TRP   B 2 1087 ? 114.320 124.431 141.496 1.00 36.25  ? 1087 TRP   A CZ2 1 
ATOM   9501  C  CZ3 . TRP   B 2 1087 ? 113.165 125.581 143.268 1.00 36.89  ? 1087 TRP   A CZ3 1 
ATOM   9502  C  CH2 . TRP   B 2 1087 ? 113.160 124.814 142.103 1.00 38.44  ? 1087 TRP   A CH2 1 
ATOM   9503  N  N   . PHE   B 2 1088 ? 118.487 129.394 146.152 1.00 36.38  ? 1088 PHE   A N   1 
ATOM   9504  C  CA  . PHE   B 2 1088 ? 118.797 130.202 147.328 1.00 30.74  ? 1088 PHE   A CA  1 
ATOM   9505  C  C   . PHE   B 2 1088 ? 117.800 131.339 147.489 1.00 34.92  ? 1088 PHE   A C   1 
ATOM   9506  O  O   . PHE   B 2 1088 ? 117.416 131.679 148.614 1.00 42.88  ? 1088 PHE   A O   1 
ATOM   9507  C  CB  . PHE   B 2 1088 ? 120.208 130.766 147.269 1.00 37.34  ? 1088 PHE   A CB  1 
ATOM   9508  C  CG  . PHE   B 2 1088 ? 120.525 131.661 148.429 1.00 37.05  ? 1088 PHE   A CG  1 
ATOM   9509  C  CD1 . PHE   B 2 1088 ? 120.684 131.133 149.696 1.00 33.51  ? 1088 PHE   A CD1 1 
ATOM   9510  C  CD2 . PHE   B 2 1088 ? 120.637 133.027 148.262 1.00 37.64  ? 1088 PHE   A CD2 1 
ATOM   9511  C  CE1 . PHE   B 2 1088 ? 120.963 131.948 150.769 1.00 35.36  ? 1088 PHE   A CE1 1 
ATOM   9512  C  CE2 . PHE   B 2 1088 ? 120.920 133.844 149.333 1.00 36.29  ? 1088 PHE   A CE2 1 
ATOM   9513  C  CZ  . PHE   B 2 1088 ? 121.082 133.304 150.586 1.00 43.25  ? 1088 PHE   A CZ  1 
ATOM   9514  N  N   . MET   B 2 1089 ? 117.377 131.946 146.377 1.00 50.81  ? 1089 MET   A N   1 
ATOM   9515  C  CA  . MET   B 2 1089 ? 116.412 133.037 146.447 1.00 44.55  ? 1089 MET   A CA  1 
ATOM   9516  C  C   . MET   B 2 1089 ? 115.109 132.599 147.096 1.00 34.55  ? 1089 MET   A C   1 
ATOM   9517  O  O   . MET   B 2 1089 ? 114.351 133.448 147.576 1.00 41.40  ? 1089 MET   A O   1 
ATOM   9518  C  CB  . MET   B 2 1089 ? 116.139 133.603 145.051 1.00 40.38  ? 1089 MET   A CB  1 
ATOM   9519  C  CG  . MET   B 2 1089 ? 116.440 135.080 144.922 1.00 38.75  ? 1089 MET   A CG  1 
ATOM   9520  S  SD  . MET   B 2 1089 ? 118.122 135.474 145.429 1.00 60.78  ? 1089 MET   A SD  1 
ATOM   9521  C  CE  . MET   B 2 1089 ? 119.044 134.985 143.977 1.00 49.02  ? 1089 MET   A CE  1 
ATOM   9522  N  N   . ILE   B 2 1090 ? 114.829 131.296 147.114 1.00 42.88  ? 1090 ILE   A N   1 
ATOM   9523  C  CA  . ILE   B 2 1090 ? 113.685 130.807 147.883 1.00 45.47  ? 1090 ILE   A CA  1 
ATOM   9524  C  C   . ILE   B 2 1090 ? 113.864 131.104 149.370 1.00 39.11  ? 1090 ILE   A C   1 
ATOM   9525  O  O   . ILE   B 2 1090 ? 112.910 131.477 150.062 1.00 41.86  ? 1090 ILE   A O   1 
ATOM   9526  C  CB  . ILE   B 2 1090 ? 113.462 129.304 147.626 1.00 49.55  ? 1090 ILE   A CB  1 
ATOM   9527  C  CG1 . ILE   B 2 1090 ? 112.817 129.086 146.256 1.00 49.54  ? 1090 ILE   A CG1 1 
ATOM   9528  C  CG2 . ILE   B 2 1090 ? 112.607 128.688 148.722 1.00 33.58  ? 1090 ILE   A CG2 1 
ATOM   9529  C  CD1 . ILE   B 2 1090 ? 112.262 127.692 146.062 1.00 47.98  ? 1090 ILE   A CD1 1 
ATOM   9530  N  N   . TYR   B 2 1091 ? 115.086 130.953 149.886 1.00 51.34  ? 1091 TYR   A N   1 
ATOM   9531  C  CA  . TYR   B 2 1091 ? 115.339 131.061 151.320 1.00 46.39  ? 1091 TYR   A CA  1 
ATOM   9532  C  C   . TYR   B 2 1091 ? 115.747 132.455 151.781 1.00 46.33  ? 1091 TYR   A C   1 
ATOM   9533  O  O   . TYR   B 2 1091 ? 115.919 132.658 152.987 1.00 48.14  ? 1091 TYR   A O   1 
ATOM   9534  C  CB  . TYR   B 2 1091 ? 116.429 130.068 151.743 1.00 46.48  ? 1091 TYR   A CB  1 
ATOM   9535  C  CG  . TYR   B 2 1091 ? 115.977 128.627 151.769 1.00 47.29  ? 1091 TYR   A CG  1 
ATOM   9536  C  CD1 . TYR   B 2 1091 ? 116.005 127.849 150.621 1.00 46.97  ? 1091 TYR   A CD1 1 
ATOM   9537  C  CD2 . TYR   B 2 1091 ? 115.526 128.045 152.944 1.00 48.62  ? 1091 TYR   A CD2 1 
ATOM   9538  C  CE1 . TYR   B 2 1091 ? 115.592 126.532 150.643 1.00 49.55  ? 1091 TYR   A CE1 1 
ATOM   9539  C  CE2 . TYR   B 2 1091 ? 115.111 126.731 152.974 1.00 49.86  ? 1091 TYR   A CE2 1 
ATOM   9540  C  CZ  . TYR   B 2 1091 ? 115.146 125.979 151.823 1.00 51.48  ? 1091 TYR   A CZ  1 
ATOM   9541  O  OH  . TYR   B 2 1091 ? 114.734 124.666 151.850 1.00 55.35  ? 1091 TYR   A OH  1 
ATOM   9542  N  N   . CYS   B 2 1092 ? 115.909 133.417 150.876 1.00 52.22  ? 1092 CYS   A N   1 
ATOM   9543  C  CA  . CYS   B 2 1092 ? 116.405 134.738 151.238 1.00 41.34  ? 1092 CYS   A CA  1 
ATOM   9544  C  C   . CYS   B 2 1092 ? 115.308 135.790 151.313 1.00 38.29  ? 1092 CYS   A C   1 
ATOM   9545  O  O   . CYS   B 2 1092 ? 115.612 136.969 151.513 1.00 42.90  ? 1092 CYS   A O   1 
ATOM   9546  C  CB  . CYS   B 2 1092 ? 117.472 135.191 150.243 1.00 40.74  ? 1092 CYS   A CB  1 
ATOM   9547  S  SG  . CYS   B 2 1092 ? 116.797 135.783 148.683 1.00 61.52  ? 1092 CYS   A SG  1 
ATOM   9548  N  N   . GLY   B 2 1093 ? 114.047 135.399 151.166 1.00 40.88  ? 1093 GLY   A N   1 
ATOM   9549  C  CA  . GLY   B 2 1093 ? 112.988 136.379 151.062 1.00 37.51  ? 1093 GLY   A CA  1 
ATOM   9550  C  C   . GLY   B 2 1093 ? 112.792 136.941 149.676 1.00 41.48  ? 1093 GLY   A C   1 
ATOM   9551  O  O   . GLY   B 2 1093 ? 112.127 137.970 149.528 1.00 52.26  ? 1093 GLY   A O   1 
ATOM   9552  N  N   . TRP   B 2 1094 ? 113.358 136.295 148.655 1.00 35.16  ? 1094 TRP   A N   1 
ATOM   9553  C  CA  . TRP   B 2 1094 ? 113.245 136.736 147.264 1.00 30.17  ? 1094 TRP   A CA  1 
ATOM   9554  C  C   . TRP   B 2 1094 ? 113.790 138.150 147.081 1.00 41.16  ? 1094 TRP   A C   1 
ATOM   9555  O  O   . TRP   B 2 1094 ? 113.182 138.989 146.415 1.00 49.43  ? 1094 TRP   A O   1 
ATOM   9556  C  CB  . TRP   B 2 1094 ? 111.800 136.638 146.770 1.00 36.28  ? 1094 TRP   A CB  1 
ATOM   9557  C  CG  . TRP   B 2 1094 ? 111.219 135.263 146.872 1.00 37.60  ? 1094 TRP   A CG  1 
ATOM   9558  C  CD1 . TRP   B 2 1094 ? 110.602 134.714 147.954 1.00 38.95  ? 1094 TRP   A CD1 1 
ATOM   9559  C  CD2 . TRP   B 2 1094 ? 111.200 134.263 145.850 1.00 37.29  ? 1094 TRP   A CD2 1 
ATOM   9560  N  NE1 . TRP   B 2 1094 ? 110.199 133.434 147.671 1.00 35.97  ? 1094 TRP   A NE1 1 
ATOM   9561  C  CE2 . TRP   B 2 1094 ? 110.556 133.133 146.385 1.00 30.60  ? 1094 TRP   A CE2 1 
ATOM   9562  C  CE3 . TRP   B 2 1094 ? 111.668 134.213 144.535 1.00 43.96  ? 1094 TRP   A CE3 1 
ATOM   9563  C  CZ2 . TRP   B 2 1094 ? 110.366 131.968 145.652 1.00 39.90  ? 1094 TRP   A CZ2 1 
ATOM   9564  C  CZ3 . TRP   B 2 1094 ? 111.478 133.058 143.810 1.00 39.95  ? 1094 TRP   A CZ3 1 
ATOM   9565  C  CH2 . TRP   B 2 1094 ? 110.834 131.950 144.368 1.00 41.51  ? 1094 TRP   A CH2 1 
ATOM   9566  N  N   . SER   B 2 1095 ? 114.951 138.412 147.673 1.00 37.15  ? 1095 SER   A N   1 
ATOM   9567  C  CA  . SER   B 2 1095 ? 115.579 139.725 147.636 1.00 36.60  ? 1095 SER   A CA  1 
ATOM   9568  C  C   . SER   B 2 1095 ? 116.643 139.854 146.555 1.00 43.53  ? 1095 SER   A C   1 
ATOM   9569  O  O   . SER   B 2 1095 ? 117.303 140.896 146.483 1.00 52.33  ? 1095 SER   A O   1 
ATOM   9570  C  CB  . SER   B 2 1095 ? 116.194 140.048 148.999 1.00 47.66  ? 1095 SER   A CB  1 
ATOM   9571  O  OG  . SER   B 2 1095 ? 117.118 139.048 149.386 1.00 48.75  ? 1095 SER   A OG  1 
ATOM   9572  N  N   . THR   B 2 1096 ? 116.825 138.828 145.724 1.00 37.19  ? 1096 THR   A N   1 
ATOM   9573  C  CA  . THR   B 2 1096 ? 117.779 138.838 144.612 1.00 33.94  ? 1096 THR   A CA  1 
ATOM   9574  C  C   . THR   B 2 1096 ? 119.205 139.086 145.107 1.00 45.47  ? 1096 THR   A C   1 
ATOM   9575  O  O   . THR   B 2 1096 ? 119.894 140.012 144.676 1.00 56.20  ? 1096 THR   A O   1 
ATOM   9576  C  CB  . THR   B 2 1096 ? 117.380 139.862 143.547 1.00 42.20  ? 1096 THR   A CB  1 
ATOM   9577  O  OG1 . THR   B 2 1096 ? 117.554 141.187 144.062 1.00 55.66  ? 1096 THR   A OG1 1 
ATOM   9578  C  CG2 . THR   B 2 1096 ? 115.932 139.666 143.156 1.00 45.37  ? 1096 THR   A CG2 1 
ATOM   9579  N  N   . THR   B 2 1097 ? 119.642 138.223 146.016 1.00 32.70  ? 1097 THR   A N   1 
ATOM   9580  C  CA  . THR   B 2 1097 ? 120.972 138.293 146.604 1.00 32.76  ? 1097 THR   A CA  1 
ATOM   9581  C  C   . THR   B 2 1097 ? 121.811 137.126 146.108 1.00 43.21  ? 1097 THR   A C   1 
ATOM   9582  O  O   . THR   B 2 1097 ? 121.307 136.007 145.969 1.00 57.39  ? 1097 THR   A O   1 
ATOM   9583  C  CB  . THR   B 2 1097 ? 120.898 138.276 148.131 1.00 38.58  ? 1097 THR   A CB  1 
ATOM   9584  O  OG1 . THR   B 2 1097 ? 122.212 138.110 148.673 1.00 43.79  ? 1097 THR   A OG1 1 
ATOM   9585  C  CG2 . THR   B 2 1097 ? 120.020 137.144 148.600 1.00 41.24  ? 1097 THR   A CG2 1 
ATOM   9586  N  N   . TYR   B 2 1098 ? 123.085 137.390 145.836 1.00 42.91  ? 1098 TYR   A N   1 
ATOM   9587  C  CA  . TYR   B 2 1098 ? 123.990 136.353 145.355 1.00 38.60  ? 1098 TYR   A CA  1 
ATOM   9588  C  C   . TYR   B 2 1098 ? 124.388 135.451 146.514 1.00 40.80  ? 1098 TYR   A C   1 
ATOM   9589  O  O   . TYR   B 2 1098 ? 125.023 135.905 147.471 1.00 43.29  ? 1098 TYR   A O   1 
ATOM   9590  C  CB  . TYR   B 2 1098 ? 125.223 136.981 144.713 1.00 37.93  ? 1098 TYR   A CB  1 
ATOM   9591  C  CG  . TYR   B 2 1098 ? 124.930 137.848 143.513 1.00 40.89  ? 1098 TYR   A CG  1 
ATOM   9592  C  CD1 . TYR   B 2 1098 ? 124.674 139.203 143.658 1.00 45.78  ? 1098 TYR   A CD1 1 
ATOM   9593  C  CD2 . TYR   B 2 1098 ? 124.919 137.315 142.235 1.00 44.49  ? 1098 TYR   A CD2 1 
ATOM   9594  C  CE1 . TYR   B 2 1098 ? 124.409 139.999 142.564 1.00 45.16  ? 1098 TYR   A CE1 1 
ATOM   9595  C  CE2 . TYR   B 2 1098 ? 124.656 138.103 141.137 1.00 44.14  ? 1098 TYR   A CE2 1 
ATOM   9596  C  CZ  . TYR   B 2 1098 ? 124.401 139.443 141.306 1.00 46.80  ? 1098 TYR   A CZ  1 
ATOM   9597  O  OH  . TYR   B 2 1098 ? 124.138 140.231 140.211 1.00 52.99  ? 1098 TYR   A OH  1 
ATOM   9598  N  N   . VAL   B 2 1099 ? 124.016 134.173 146.439 1.00 44.21  ? 1099 VAL   A N   1 
ATOM   9599  C  CA  . VAL   B 2 1099 ? 124.509 133.209 147.419 1.00 34.96  ? 1099 VAL   A CA  1 
ATOM   9600  C  C   . VAL   B 2 1099 ? 126.017 133.050 147.279 1.00 44.17  ? 1099 VAL   A C   1 
ATOM   9601  O  O   . VAL   B 2 1099 ? 126.762 133.130 148.261 1.00 50.26  ? 1099 VAL   A O   1 
ATOM   9602  C  CB  . VAL   B 2 1099 ? 123.773 131.863 147.275 1.00 42.66  ? 1099 VAL   A CB  1 
ATOM   9603  C  CG1 . VAL   B 2 1099 ? 123.648 131.461 145.816 1.00 41.52  ? 1099 VAL   A CG1 1 
ATOM   9604  C  CG2 . VAL   B 2 1099 ? 124.478 130.780 148.071 1.00 48.88  ? 1099 VAL   A CG2 1 
ATOM   9605  N  N   . PHE   B 2 1100 ? 126.488 132.864 146.049 1.00 43.28  ? 1100 PHE   A N   1 
ATOM   9606  C  CA  . PHE   B 2 1100 ? 127.914 132.744 145.789 1.00 41.30  ? 1100 PHE   A CA  1 
ATOM   9607  C  C   . PHE   B 2 1100 ? 128.623 134.069 146.021 1.00 42.62  ? 1100 PHE   A C   1 
ATOM   9608  O  O   . PHE   B 2 1100 ? 128.030 135.146 145.917 1.00 44.31  ? 1100 PHE   A O   1 
ATOM   9609  C  CB  . PHE   B 2 1100 ? 128.164 132.305 144.348 1.00 41.12  ? 1100 PHE   A CB  1 
ATOM   9610  C  CG  . PHE   B 2 1100 ? 127.568 130.979 143.999 1.00 39.04  ? 1100 PHE   A CG  1 
ATOM   9611  C  CD1 . PHE   B 2 1100 ? 127.558 129.944 144.912 1.00 43.99  ? 1100 PHE   A CD1 1 
ATOM   9612  C  CD2 . PHE   B 2 1100 ? 127.024 130.767 142.748 1.00 35.52  ? 1100 PHE   A CD2 1 
ATOM   9613  C  CE1 . PHE   B 2 1100 ? 127.012 128.724 144.582 1.00 46.43  ? 1100 PHE   A CE1 1 
ATOM   9614  C  CE2 . PHE   B 2 1100 ? 126.479 129.553 142.414 1.00 39.45  ? 1100 PHE   A CE2 1 
ATOM   9615  C  CZ  . PHE   B 2 1100 ? 126.475 128.529 143.330 1.00 45.15  ? 1100 PHE   A CZ  1 
ATOM   9616  N  N   . ALA   B 2 1101 ? 129.910 133.982 146.339 1.00 37.99  ? 1101 ALA   A N   1 
ATOM   9617  C  CA  . ALA   B 2 1101 ? 130.770 135.141 146.186 1.00 38.43  ? 1101 ALA   A CA  1 
ATOM   9618  C  C   . ALA   B 2 1101 ? 130.815 135.519 144.713 1.00 50.24  ? 1101 ALA   A C   1 
ATOM   9619  O  O   . ALA   B 2 1101 ? 130.842 134.651 143.837 1.00 48.59  ? 1101 ALA   A O   1 
ATOM   9620  C  CB  . ALA   B 2 1101 ? 132.173 134.846 146.712 1.00 37.58  ? 1101 ALA   A CB  1 
ATOM   9621  N  N   . TYR   B 2 1102 ? 130.812 136.824 144.438 1.00 51.15  ? 1102 TYR   A N   1 
ATOM   9622  C  CA  . TYR   B 2 1102 ? 130.614 137.284 143.070 1.00 43.88  ? 1102 TYR   A CA  1 
ATOM   9623  C  C   . TYR   B 2 1102 ? 131.719 136.823 142.129 1.00 55.51  ? 1102 TYR   A C   1 
ATOM   9624  O  O   . TYR   B 2 1102 ? 131.502 136.788 140.914 1.00 62.91  ? 1102 TYR   A O   1 
ATOM   9625  C  CB  . TYR   B 2 1102 ? 130.498 138.806 143.038 1.00 48.75  ? 1102 TYR   A CB  1 
ATOM   9626  C  CG  . TYR   B 2 1102 ? 130.037 139.344 141.706 1.00 54.58  ? 1102 TYR   A CG  1 
ATOM   9627  C  CD1 . TYR   B 2 1102 ? 128.735 139.149 141.272 1.00 56.85  ? 1102 TYR   A CD1 1 
ATOM   9628  C  CD2 . TYR   B 2 1102 ? 130.903 140.047 140.883 1.00 52.01  ? 1102 TYR   A CD2 1 
ATOM   9629  C  CE1 . TYR   B 2 1102 ? 128.308 139.636 140.054 1.00 57.65  ? 1102 TYR   A CE1 1 
ATOM   9630  C  CE2 . TYR   B 2 1102 ? 130.485 140.539 139.667 1.00 55.25  ? 1102 TYR   A CE2 1 
ATOM   9631  C  CZ  . TYR   B 2 1102 ? 129.188 140.331 139.256 1.00 56.94  ? 1102 TYR   A CZ  1 
ATOM   9632  O  OH  . TYR   B 2 1102 ? 128.769 140.822 138.041 1.00 61.89  ? 1102 TYR   A OH  1 
ATOM   9633  N  N   . VAL   B 2 1103 ? 132.891 136.465 142.654 1.00 44.72  ? 1103 VAL   A N   1 
ATOM   9634  C  CA  . VAL   B 2 1103 ? 133.964 135.974 141.795 1.00 31.88  ? 1103 VAL   A CA  1 
ATOM   9635  C  C   . VAL   B 2 1103 ? 133.595 134.627 141.186 1.00 39.88  ? 1103 VAL   A C   1 
ATOM   9636  O  O   . VAL   B 2 1103 ? 133.958 134.330 140.042 1.00 51.58  ? 1103 VAL   A O   1 
ATOM   9637  C  CB  . VAL   B 2 1103 ? 135.287 135.903 142.576 1.00 37.59  ? 1103 VAL   A CB  1 
ATOM   9638  C  CG1 . VAL   B 2 1103 ? 135.836 137.297 142.804 1.00 40.62  ? 1103 VAL   A CG1 1 
ATOM   9639  C  CG2 . VAL   B 2 1103 ? 135.087 135.187 143.900 1.00 38.02  ? 1103 VAL   A CG2 1 
ATOM   9640  N  N   . TYR   B 2 1104 ? 132.877 133.788 141.935 1.00 43.15  ? 1104 TYR   A N   1 
ATOM   9641  C  CA  . TYR   B 2 1104 ? 132.514 132.469 141.432 1.00 39.25  ? 1104 TYR   A CA  1 
ATOM   9642  C  C   . TYR   B 2 1104 ? 131.467 132.532 140.330 1.00 44.79  ? 1104 TYR   A C   1 
ATOM   9643  O  O   . TYR   B 2 1104 ? 131.437 131.645 139.471 1.00 56.81  ? 1104 TYR   A O   1 
ATOM   9644  C  CB  . TYR   B 2 1104 ? 132.019 131.587 142.579 1.00 38.63  ? 1104 TYR   A CB  1 
ATOM   9645  C  CG  . TYR   B 2 1104 ? 133.100 131.243 143.572 1.00 40.70  ? 1104 TYR   A CG  1 
ATOM   9646  C  CD1 . TYR   B 2 1104 ? 133.959 130.180 143.347 1.00 40.95  ? 1104 TYR   A CD1 1 
ATOM   9647  C  CD2 . TYR   B 2 1104 ? 133.267 131.985 144.729 1.00 48.18  ? 1104 TYR   A CD2 1 
ATOM   9648  C  CE1 . TYR   B 2 1104 ? 134.952 129.867 144.247 1.00 42.26  ? 1104 TYR   A CE1 1 
ATOM   9649  C  CE2 . TYR   B 2 1104 ? 134.257 131.677 145.635 1.00 48.39  ? 1104 TYR   A CE2 1 
ATOM   9650  C  CZ  . TYR   B 2 1104 ? 135.095 130.617 145.389 1.00 39.83  ? 1104 TYR   A CZ  1 
ATOM   9651  O  OH  . TYR   B 2 1104 ? 136.084 130.304 146.290 1.00 50.42  ? 1104 TYR   A OH  1 
ATOM   9652  N  N   . LEU   B 2 1105 ? 130.614 133.552 140.332 1.00 46.75  ? 1105 LEU   A N   1 
ATOM   9653  C  CA  . LEU   B 2 1105 ? 129.641 133.732 139.264 1.00 41.90  ? 1105 LEU   A CA  1 
ATOM   9654  C  C   . LEU   B 2 1105 ? 130.194 134.556 138.111 1.00 46.90  ? 1105 LEU   A C   1 
ATOM   9655  O  O   . LEU   B 2 1105 ? 129.748 134.394 136.970 1.00 56.30  ? 1105 LEU   A O   1 
ATOM   9656  C  CB  . LEU   B 2 1105 ? 128.376 134.395 139.816 1.00 42.81  ? 1105 LEU   A CB  1 
ATOM   9657  C  CG  . LEU   B 2 1105 ? 127.180 134.488 138.870 1.00 50.98  ? 1105 LEU   A CG  1 
ATOM   9658  C  CD1 . LEU   B 2 1105 ? 126.681 133.101 138.500 1.00 51.44  ? 1105 LEU   A CD1 1 
ATOM   9659  C  CD2 . LEU   B 2 1105 ? 126.073 135.312 139.494 1.00 48.80  ? 1105 LEU   A CD2 1 
ATOM   9660  N  N   . LEU   B 2 1106 ? 131.163 135.430 138.388 1.00 40.63  ? 1106 LEU   A N   1 
ATOM   9661  C  CA  . LEU   B 2 1106 ? 131.778 136.231 137.338 1.00 41.18  ? 1106 LEU   A CA  1 
ATOM   9662  C  C   . LEU   B 2 1106 ? 132.584 135.365 136.379 1.00 48.25  ? 1106 LEU   A C   1 
ATOM   9663  O  O   . LEU   B 2 1106 ? 132.604 135.620 135.170 1.00 58.31  ? 1106 LEU   A O   1 
ATOM   9664  C  CB  . LEU   B 2 1106 ? 132.662 137.307 137.964 1.00 46.66  ? 1106 LEU   A CB  1 
ATOM   9665  C  CG  . LEU   B 2 1106 ? 133.377 138.279 137.031 1.00 47.33  ? 1106 LEU   A CG  1 
ATOM   9666  C  CD1 . LEU   B 2 1106 ? 132.376 139.092 136.231 1.00 51.07  ? 1106 LEU   A CD1 1 
ATOM   9667  C  CD2 . LEU   B 2 1106 ? 134.291 139.184 137.830 1.00 40.10  ? 1106 LEU   A CD2 1 
ATOM   9668  N  N   . PHE   B 2 1107 ? 133.254 134.338 136.899 1.00 39.22  ? 1107 PHE   A N   1 
ATOM   9669  C  CA  . PHE   B 2 1107 ? 134.112 133.469 136.108 1.00 35.12  ? 1107 PHE   A CA  1 
ATOM   9670  C  C   . PHE   B 2 1107 ? 133.436 132.156 135.738 1.00 40.11  ? 1107 PHE   A C   1 
ATOM   9671  O  O   . PHE   B 2 1107 ? 134.124 131.180 135.423 1.00 48.97  ? 1107 PHE   A O   1 
ATOM   9672  C  CB  . PHE   B 2 1107 ? 135.412 133.197 136.861 1.00 35.46  ? 1107 PHE   A CB  1 
ATOM   9673  C  CG  . PHE   B 2 1107 ? 136.239 134.422 137.100 1.00 39.76  ? 1107 PHE   A CG  1 
ATOM   9674  C  CD1 . PHE   B 2 1107 ? 136.225 135.467 136.196 1.00 43.57  ? 1107 PHE   A CD1 1 
ATOM   9675  C  CD2 . PHE   B 2 1107 ? 137.029 134.532 138.227 1.00 43.41  ? 1107 PHE   A CD2 1 
ATOM   9676  C  CE1 . PHE   B 2 1107 ? 136.985 136.596 136.412 1.00 43.68  ? 1107 PHE   A CE1 1 
ATOM   9677  C  CE2 . PHE   B 2 1107 ? 137.788 135.658 138.446 1.00 40.76  ? 1107 PHE   A CE2 1 
ATOM   9678  C  CZ  . PHE   B 2 1107 ? 137.766 136.691 137.539 1.00 42.38  ? 1107 PHE   A CZ  1 
ATOM   9679  N  N   . TRP   B 2 1108 ? 132.102 132.110 135.771 1.00 40.94  ? 1108 TRP   A N   1 
ATOM   9680  C  CA  . TRP   B 2 1108 ? 131.398 130.865 135.485 1.00 38.61  ? 1108 TRP   A CA  1 
ATOM   9681  C  C   . TRP   B 2 1108 ? 131.618 130.414 134.047 1.00 44.40  ? 1108 TRP   A C   1 
ATOM   9682  O  O   . TRP   B 2 1108 ? 131.843 129.226 133.791 1.00 50.11  ? 1108 TRP   A O   1 
ATOM   9683  C  CB  . TRP   B 2 1108 ? 129.908 131.028 135.773 1.00 40.41  ? 1108 TRP   A CB  1 
ATOM   9684  C  CG  . TRP   B 2 1108 ? 129.131 129.775 135.576 1.00 39.41  ? 1108 TRP   A CG  1 
ATOM   9685  C  CD1 . TRP   B 2 1108 ? 128.428 129.414 134.467 1.00 41.31  ? 1108 TRP   A CD1 1 
ATOM   9686  C  CD2 . TRP   B 2 1108 ? 128.979 128.706 136.512 1.00 45.38  ? 1108 TRP   A CD2 1 
ATOM   9687  N  NE1 . TRP   B 2 1108 ? 127.846 128.188 134.655 1.00 41.27  ? 1108 TRP   A NE1 1 
ATOM   9688  C  CE2 . TRP   B 2 1108 ? 128.169 127.731 135.904 1.00 44.68  ? 1108 TRP   A CE2 1 
ATOM   9689  C  CE3 . TRP   B 2 1108 ? 129.447 128.480 137.808 1.00 47.46  ? 1108 TRP   A CE3 1 
ATOM   9690  C  CZ2 . TRP   B 2 1108 ? 127.818 126.550 136.545 1.00 49.68  ? 1108 TRP   A CZ2 1 
ATOM   9691  C  CZ3 . TRP   B 2 1108 ? 129.098 127.309 138.442 1.00 45.47  ? 1108 TRP   A CZ3 1 
ATOM   9692  C  CH2 . TRP   B 2 1108 ? 128.292 126.357 137.811 1.00 46.75  ? 1108 TRP   A CH2 1 
ATOM   9693  N  N   . ASN   B 2 1109 ? 131.560 131.343 133.096 1.00 44.37  ? 1109 ASN   A N   1 
ATOM   9694  C  CA  . ASN   B 2 1109 ? 131.759 131.014 131.691 1.00 37.21  ? 1109 ASN   A CA  1 
ATOM   9695  C  C   . ASN   B 2 1109 ? 133.171 131.291 131.206 1.00 37.36  ? 1109 ASN   A C   1 
ATOM   9696  O  O   . ASN   B 2 1109 ? 133.620 130.653 130.251 1.00 47.12  ? 1109 ASN   A O   1 
ATOM   9697  C  CB  . ASN   B 2 1109 ? 130.769 131.793 130.822 1.00 37.39  ? 1109 ASN   A CB  1 
ATOM   9698  C  CG  . ASN   B 2 1109 ? 129.333 131.553 131.223 1.00 46.22  ? 1109 ASN   A CG  1 
ATOM   9699  O  OD1 . ASN   B 2 1109 ? 128.709 130.589 130.788 1.00 47.51  ? 1109 ASN   A OD1 1 
ATOM   9700  N  ND2 . ASN   B 2 1109 ? 128.800 132.431 132.061 1.00 47.98  ? 1109 ASN   A ND2 1 
ATOM   9701  N  N   . VAL   B 2 1110 ? 133.879 132.225 131.841 1.00 35.60  ? 1110 VAL   A N   1 
ATOM   9702  C  CA  . VAL   B 2 1110 ? 135.237 132.541 131.416 1.00 31.19  ? 1110 VAL   A CA  1 
ATOM   9703  C  C   . VAL   B 2 1110 ? 136.180 131.385 131.719 1.00 42.82  ? 1110 VAL   A C   1 
ATOM   9704  O  O   . VAL   B 2 1110 ? 136.984 130.985 130.869 1.00 52.83  ? 1110 VAL   A O   1 
ATOM   9705  C  CB  . VAL   B 2 1110 ? 135.714 133.843 132.081 1.00 38.84  ? 1110 VAL   A CB  1 
ATOM   9706  C  CG1 . VAL   B 2 1110 ? 136.941 134.378 131.371 1.00 44.05  ? 1110 VAL   A CG1 1 
ATOM   9707  C  CG2 . VAL   B 2 1110 ? 134.603 134.872 132.092 1.00 42.90  ? 1110 VAL   A CG2 1 
ATOM   9708  N  N   . PHE   B 2 1111 ? 136.101 130.831 132.926 1.00 38.63  ? 1111 PHE   A N   1 
ATOM   9709  C  CA  . PHE   B 2 1111 ? 137.072 129.847 133.387 1.00 32.86  ? 1111 PHE   A CA  1 
ATOM   9710  C  C   . PHE   B 2 1111 ? 136.462 128.493 133.710 1.00 37.63  ? 1111 PHE   A C   1 
ATOM   9711  O  O   . PHE   B 2 1111 ? 136.945 127.472 133.209 1.00 46.91  ? 1111 PHE   A O   1 
ATOM   9712  C  CB  . PHE   B 2 1111 ? 137.812 130.384 134.620 1.00 32.85  ? 1111 PHE   A CB  1 
ATOM   9713  C  CG  . PHE   B 2 1111 ? 138.758 131.503 134.317 1.00 38.22  ? 1111 PHE   A CG  1 
ATOM   9714  C  CD1 . PHE   B 2 1111 ? 139.404 131.570 133.098 1.00 39.32  ? 1111 PHE   A CD1 1 
ATOM   9715  C  CD2 . PHE   B 2 1111 ? 139.003 132.489 135.253 1.00 41.96  ? 1111 PHE   A CD2 1 
ATOM   9716  C  CE1 . PHE   B 2 1111 ? 140.277 132.598 132.819 1.00 44.25  ? 1111 PHE   A CE1 1 
ATOM   9717  C  CE2 . PHE   B 2 1111 ? 139.874 133.520 134.978 1.00 43.42  ? 1111 PHE   A CE2 1 
ATOM   9718  C  CZ  . PHE   B 2 1111 ? 140.511 133.574 133.760 1.00 45.55  ? 1111 PHE   A CZ  1 
ATOM   9719  N  N   . TRP   B 2 1112 ? 135.418 128.450 134.543 1.00 32.77  ? 1112 TRP   A N   1 
ATOM   9720  C  CA  . TRP   B 2 1112 ? 134.964 127.173 135.087 1.00 29.96  ? 1112 TRP   A CA  1 
ATOM   9721  C  C   . TRP   B 2 1112 ? 134.424 126.256 133.997 1.00 40.24  ? 1112 TRP   A C   1 
ATOM   9722  O  O   . TRP   B 2 1112 ? 134.805 125.083 133.918 1.00 53.50  ? 1112 TRP   A O   1 
ATOM   9723  C  CB  . TRP   B 2 1112 ? 133.902 127.394 136.167 1.00 42.56  ? 1112 TRP   A CB  1 
ATOM   9724  C  CG  . TRP   B 2 1112 ? 134.208 128.439 137.223 1.00 42.33  ? 1112 TRP   A CG  1 
ATOM   9725  C  CD1 . TRP   B 2 1112 ? 133.294 129.214 137.872 1.00 37.73  ? 1112 TRP   A CD1 1 
ATOM   9726  C  CD2 . TRP   B 2 1112 ? 135.493 128.817 137.749 1.00 40.07  ? 1112 TRP   A CD2 1 
ATOM   9727  N  NE1 . TRP   B 2 1112 ? 133.920 130.047 138.761 1.00 41.76  ? 1112 TRP   A NE1 1 
ATOM   9728  C  CE2 . TRP   B 2 1112 ? 135.269 129.824 138.705 1.00 37.15  ? 1112 TRP   A CE2 1 
ATOM   9729  C  CE3 . TRP   B 2 1112 ? 136.807 128.404 137.506 1.00 45.62  ? 1112 TRP   A CE3 1 
ATOM   9730  C  CZ2 . TRP   B 2 1112 ? 136.304 130.422 139.412 1.00 34.95  ? 1112 TRP   A CZ2 1 
ATOM   9731  C  CZ3 . TRP   B 2 1112 ? 137.831 129.003 138.210 1.00 44.75  ? 1112 TRP   A CZ3 1 
ATOM   9732  C  CH2 . TRP   B 2 1112 ? 137.574 129.997 139.152 1.00 37.20  ? 1112 TRP   A CH2 1 
ATOM   9733  N  N   . THR   B 2 1113 ? 133.532 126.767 133.145 1.00 42.55  ? 1113 THR   A N   1 
ATOM   9734  C  CA  . THR   B 2 1113 ? 132.883 125.956 132.113 1.00 39.99  ? 1113 THR   A CA  1 
ATOM   9735  C  C   . THR   B 2 1113 ? 133.002 126.666 130.764 1.00 46.86  ? 1113 THR   A C   1 
ATOM   9736  O  O   . THR   B 2 1113 ? 132.083 127.364 130.335 1.00 58.39  ? 1113 THR   A O   1 
ATOM   9737  C  CB  . THR   B 2 1113 ? 131.424 125.691 132.477 1.00 44.99  ? 1113 THR   A CB  1 
ATOM   9738  O  OG1 . THR   B 2 1113 ? 130.731 126.936 132.615 1.00 47.99  ? 1113 THR   A OG1 1 
ATOM   9739  C  CG2 . THR   B 2 1113 ? 131.326 124.921 133.783 1.00 47.46  ? 1113 THR   A CG2 1 
ATOM   9740  N  N   . LEU   B 2 1114 ? 134.136 126.489 130.102 1.00 45.39  ? 1114 LEU   A N   1 
ATOM   9741  C  CA  . LEU   B 2 1114 ? 134.297 126.917 128.716 1.00 46.38  ? 1114 LEU   A CA  1 
ATOM   9742  C  C   . LEU   B 2 1114 ? 134.873 125.831 127.819 1.00 54.25  ? 1114 LEU   A C   1 
ATOM   9743  O  O   . LEU   B 2 1114 ? 134.430 125.671 126.671 1.00 59.16  ? 1114 LEU   A O   1 
ATOM   9744  C  CB  . LEU   B 2 1114 ? 135.196 128.161 128.670 1.00 47.24  ? 1114 LEU   A CB  1 
ATOM   9745  C  CG  . LEU   B 2 1114 ? 135.626 128.676 127.298 1.00 53.99  ? 1114 LEU   A CG  1 
ATOM   9746  C  CD1 . LEU   B 2 1114 ? 134.427 129.197 126.517 1.00 53.98  ? 1114 LEU   A CD1 1 
ATOM   9747  C  CD2 . LEU   B 2 1114 ? 136.695 129.747 127.450 1.00 45.57  ? 1114 LEU   A CD2 1 
ATOM   9748  N  N   . VAL   B 2 1115 ? 135.825 125.057 128.326 1.00 53.61  ? 1115 VAL   A N   1 
ATOM   9749  C  CA  . VAL   B 2 1115 ? 136.597 124.122 127.515 1.00 48.73  ? 1115 VAL   A CA  1 
ATOM   9750  C  C   . VAL   B 2 1115 ? 135.781 122.883 127.162 1.00 54.21  ? 1115 VAL   A C   1 
ATOM   9751  O  O   . VAL   B 2 1115 ? 135.923 122.381 126.042 1.00 64.75  ? 1115 VAL   A O   1 
ATOM   9752  C  CB  . VAL   B 2 1115 ? 137.909 123.739 128.214 1.00 51.35  ? 1115 VAL   A CB  1 
ATOM   9753  C  CG1 . VAL   B 2 1115 ? 138.945 123.324 127.187 1.00 54.30  ? 1115 VAL   A CG1 1 
ATOM   9754  C  CG2 . VAL   B 2 1115 ? 138.417 124.898 129.045 1.00 58.94  ? 1115 VAL   A CG2 1 
ATOM   9755  N  N   . PRO   B 2 1116 ? 134.959 122.319 128.059 1.00 48.19  ? 1116 PRO   A N   1 
ATOM   9756  C  CA  . PRO   B 2 1116 ? 134.083 121.221 127.616 1.00 47.53  ? 1116 PRO   A CA  1 
ATOM   9757  C  C   . PRO   B 2 1116 ? 133.167 121.608 126.469 1.00 45.67  ? 1116 PRO   A C   1 
ATOM   9758  O  O   . PRO   B 2 1116 ? 132.996 120.831 125.520 1.00 49.75  ? 1116 PRO   A O   1 
ATOM   9759  C  CB  . PRO   B 2 1116 ? 133.292 120.881 128.883 1.00 45.80  ? 1116 PRO   A CB  1 
ATOM   9760  C  CG  . PRO   B 2 1116 ? 134.195 121.241 129.984 1.00 54.36  ? 1116 PRO   A CG  1 
ATOM   9761  C  CD  . PRO   B 2 1116 ? 134.928 122.465 129.527 1.00 50.30  ? 1116 PRO   A CD  1 
ATOM   9762  N  N   . VAL   B 2 1117 ? 132.596 122.810 126.518 1.00 42.82  ? 1117 VAL   A N   1 
ATOM   9763  C  CA  . VAL   B 2 1117 ? 131.719 123.267 125.447 1.00 44.99  ? 1117 VAL   A CA  1 
ATOM   9764  C  C   . VAL   B 2 1117 ? 132.504 123.463 124.156 1.00 47.08  ? 1117 VAL   A C   1 
ATOM   9765  O  O   . VAL   B 2 1117 ? 132.051 123.067 123.074 1.00 56.04  ? 1117 VAL   A O   1 
ATOM   9766  C  CB  . VAL   B 2 1117 ? 130.986 124.549 125.880 1.00 49.51  ? 1117 VAL   A CB  1 
ATOM   9767  C  CG1 . VAL   B 2 1117 ? 130.850 125.515 124.719 1.00 47.08  ? 1117 VAL   A CG1 1 
ATOM   9768  C  CG2 . VAL   B 2 1117 ? 129.623 124.201 126.445 1.00 48.59  ? 1117 VAL   A CG2 1 
ATOM   9769  N  N   . ILE   B 2 1118 ? 133.695 124.064 124.244 1.00 45.91  ? 1118 ILE   A N   1 
ATOM   9770  C  CA  . ILE   B 2 1118 ? 134.503 124.253 123.041 1.00 46.11  ? 1118 ILE   A CA  1 
ATOM   9771  C  C   . ILE   B 2 1118 ? 134.905 122.907 122.445 1.00 48.58  ? 1118 ILE   A C   1 
ATOM   9772  O  O   . ILE   B 2 1118 ? 134.876 122.718 121.221 1.00 57.74  ? 1118 ILE   A O   1 
ATOM   9773  C  CB  . ILE   B 2 1118 ? 135.726 125.134 123.351 1.00 51.45  ? 1118 ILE   A CB  1 
ATOM   9774  C  CG1 . ILE   B 2 1118 ? 135.274 126.544 123.729 1.00 51.22  ? 1118 ILE   A CG1 1 
ATOM   9775  C  CG2 . ILE   B 2 1118 ? 136.671 125.180 122.168 1.00 52.67  ? 1118 ILE   A CG2 1 
ATOM   9776  C  CD1 . ILE   B 2 1118 ? 134.267 127.137 122.773 1.00 51.63  ? 1118 ILE   A CD1 1 
ATOM   9777  N  N   . ALA   B 2 1119 ? 135.277 121.949 123.297 1.00 40.02  ? 1119 ALA   A N   1 
ATOM   9778  C  CA  . ALA   B 2 1119 ? 135.660 120.626 122.819 1.00 40.91  ? 1119 ALA   A CA  1 
ATOM   9779  C  C   . ALA   B 2 1119 ? 134.491 119.910 122.160 1.00 44.71  ? 1119 ALA   A C   1 
ATOM   9780  O  O   . ALA   B 2 1119 ? 134.668 119.235 121.142 1.00 49.00  ? 1119 ALA   A O   1 
ATOM   9781  C  CB  . ALA   B 2 1119 ? 136.215 119.794 123.973 1.00 44.84  ? 1119 ALA   A CB  1 
ATOM   9782  N  N   . ILE   B 2 1120 ? 133.291 120.029 122.730 1.00 40.06  ? 1120 ILE   A N   1 
ATOM   9783  C  CA  . ILE   B 2 1120 ? 132.116 119.439 122.097 1.00 34.65  ? 1120 ILE   A CA  1 
ATOM   9784  C  C   . ILE   B 2 1120 ? 131.865 120.081 120.740 1.00 41.55  ? 1120 ILE   A C   1 
ATOM   9785  O  O   . ILE   B 2 1120 ? 131.570 119.394 119.754 1.00 43.91  ? 1120 ILE   A O   1 
ATOM   9786  C  CB  . ILE   B 2 1120 ? 130.888 119.570 123.015 1.00 38.65  ? 1120 ILE   A CB  1 
ATOM   9787  C  CG1 . ILE   B 2 1120 ? 131.025 118.660 124.232 1.00 48.09  ? 1120 ILE   A CG1 1 
ATOM   9788  C  CG2 . ILE   B 2 1120 ? 129.628 119.242 122.256 1.00 41.43  ? 1120 ILE   A CG2 1 
ATOM   9789  C  CD1 . ILE   B 2 1120 ? 129.865 118.753 125.192 1.00 44.17  ? 1120 ILE   A CD1 1 
ATOM   9790  N  N   . GLY   B 2 1121 ? 131.987 121.406 120.663 1.00 39.74  ? 1121 GLY   A N   1 
ATOM   9791  C  CA  . GLY   B 2 1121 ? 131.684 122.093 119.421 1.00 38.18  ? 1121 GLY   A CA  1 
ATOM   9792  C  C   . GLY   B 2 1121 ? 132.716 121.879 118.333 1.00 42.77  ? 1121 GLY   A C   1 
ATOM   9793  O  O   . GLY   B 2 1121 ? 132.409 122.033 117.148 1.00 50.78  ? 1121 GLY   A O   1 
ATOM   9794  N  N   . LEU   B 2 1122 ? 133.945 121.528 118.707 1.00 39.41  ? 1122 LEU   A N   1 
ATOM   9795  C  CA  . LEU   B 2 1122 ? 135.016 121.401 117.725 1.00 36.55  ? 1122 LEU   A CA  1 
ATOM   9796  C  C   . LEU   B 2 1122 ? 135.386 119.957 117.399 1.00 43.48  ? 1122 LEU   A C   1 
ATOM   9797  O  O   . LEU   B 2 1122 ? 135.554 119.618 116.225 1.00 46.89  ? 1122 LEU   A O   1 
ATOM   9798  C  CB  . LEU   B 2 1122 ? 136.263 122.149 118.210 1.00 42.70  ? 1122 LEU   A CB  1 
ATOM   9799  C  CG  . LEU   B 2 1122 ? 136.173 123.673 118.267 1.00 45.61  ? 1122 LEU   A CG  1 
ATOM   9800  C  CD1 . LEU   B 2 1122 ? 137.523 124.265 118.597 1.00 44.95  ? 1122 LEU   A CD1 1 
ATOM   9801  C  CD2 . LEU   B 2 1122 ? 135.656 124.224 116.955 1.00 47.47  ? 1122 LEU   A CD2 1 
ATOM   9802  N  N   . PHE   B 2 1123 ? 135.524 119.095 118.406 1.00 44.57  ? 1123 PHE   A N   1 
ATOM   9803  C  CA  . PHE   B 2 1123 ? 136.132 117.786 118.221 1.00 44.27  ? 1123 PHE   A CA  1 
ATOM   9804  C  C   . PHE   B 2 1123 ? 135.174 116.616 118.403 1.00 45.82  ? 1123 PHE   A C   1 
ATOM   9805  O  O   . PHE   B 2 1123 ? 135.569 115.475 118.146 1.00 51.42  ? 1123 PHE   A O   1 
ATOM   9806  C  CB  . PHE   B 2 1123 ? 137.313 117.620 119.181 1.00 42.05  ? 1123 PHE   A CB  1 
ATOM   9807  C  CG  . PHE   B 2 1123 ? 138.298 118.747 119.130 1.00 45.00  ? 1123 PHE   A CG  1 
ATOM   9808  C  CD1 . PHE   B 2 1123 ? 139.218 118.832 118.104 1.00 46.19  ? 1123 PHE   A CD1 1 
ATOM   9809  C  CD2 . PHE   B 2 1123 ? 138.312 119.716 120.116 1.00 50.65  ? 1123 PHE   A CD2 1 
ATOM   9810  C  CE1 . PHE   B 2 1123 ? 140.129 119.867 118.056 1.00 48.24  ? 1123 PHE   A CE1 1 
ATOM   9811  C  CE2 . PHE   B 2 1123 ? 139.221 120.752 120.073 1.00 53.66  ? 1123 PHE   A CE2 1 
ATOM   9812  C  CZ  . PHE   B 2 1123 ? 140.131 120.827 119.042 1.00 50.78  ? 1123 PHE   A CZ  1 
ATOM   9813  N  N   . ASP   B 2 1124 ? 133.941 116.852 118.837 1.00 44.32  ? 1124 ASP   A N   1 
ATOM   9814  C  CA  . ASP   B 2 1124 ? 133.032 115.745 119.105 1.00 44.00  ? 1124 ASP   A CA  1 
ATOM   9815  C  C   . ASP   B 2 1124 ? 132.566 115.105 117.803 1.00 53.39  ? 1124 ASP   A C   1 
ATOM   9816  O  O   . ASP   B 2 1124 ? 132.143 115.798 116.873 1.00 60.86  ? 1124 ASP   A O   1 
ATOM   9817  C  CB  . ASP   B 2 1124 ? 131.832 116.223 119.918 1.00 56.04  ? 1124 ASP   A CB  1 
ATOM   9818  C  CG  . ASP   B 2 1124 ? 131.037 115.077 120.512 1.00 60.90  ? 1124 ASP   A CG  1 
ATOM   9819  O  OD1 . ASP   B 2 1124 ? 131.490 113.917 120.407 1.00 62.47  ? 1124 ASP   A OD1 1 
ATOM   9820  O  OD2 . ASP   B 2 1124 ? 129.960 115.335 121.088 1.00 60.16  ? 1124 ASP   A OD2 1 
ATOM   9821  N  N   . ARG   B 2 1125 ? 132.639 113.777 117.741 1.00 55.64  ? 1125 ARG   A N   1 
ATOM   9822  C  CA  . ARG   B 2 1125 ? 132.226 113.011 116.572 1.00 50.94  ? 1125 ARG   A CA  1 
ATOM   9823  C  C   . ARG   B 2 1125 ? 131.257 111.927 117.018 1.00 54.10  ? 1125 ARG   A C   1 
ATOM   9824  O  O   . ARG   B 2 1125 ? 131.588 111.121 117.893 1.00 61.68  ? 1125 ARG   A O   1 
ATOM   9825  C  CB  . ARG   B 2 1125 ? 133.432 112.389 115.863 1.00 48.37  ? 1125 ARG   A CB  1 
ATOM   9826  C  CG  . ARG   B 2 1125 ? 134.430 113.397 115.328 1.00 52.00  ? 1125 ARG   A CG  1 
ATOM   9827  C  CD  . ARG   B 2 1125 ? 135.610 112.717 114.649 1.00 54.20  ? 1125 ARG   A CD  1 
ATOM   9828  N  NE  . ARG   B 2 1125 ? 136.429 111.956 115.585 1.00 60.63  ? 1125 ARG   A NE  1 
ATOM   9829  C  CZ  . ARG   B 2 1125 ? 136.371 110.640 115.737 1.00 66.65  ? 1125 ARG   A CZ  1 
ATOM   9830  N  NH1 . ARG   B 2 1125 ? 135.541 109.897 115.023 1.00 60.45  ? 1125 ARG   A NH1 1 
ATOM   9831  N  NH2 . ARG   B 2 1125 ? 137.167 110.054 116.627 1.00 64.30  ? 1125 ARG   A NH2 1 
ATOM   9832  N  N   . ASN   B 2 1126 ? 130.065 111.908 116.419 1.00 44.92  ? 1126 ASN   A N   1 
ATOM   9833  C  CA  . ASN   B 2 1126 ? 129.098 110.866 116.744 1.00 46.78  ? 1126 ASN   A CA  1 
ATOM   9834  C  C   . ASN   B 2 1126 ? 129.462 109.537 116.096 1.00 52.05  ? 1126 ASN   A C   1 
ATOM   9835  O  O   . ASN   B 2 1126 ? 129.196 108.477 116.670 1.00 56.54  ? 1126 ASN   A O   1 
ATOM   9836  C  CB  . ASN   B 2 1126 ? 127.696 111.300 116.324 1.00 51.20  ? 1126 ASN   A CB  1 
ATOM   9837  C  CG  . ASN   B 2 1126 ? 127.643 111.791 114.896 1.00 53.78  ? 1126 ASN   A CG  1 
ATOM   9838  O  OD1 . ASN   B 2 1126 ? 128.635 112.284 114.360 1.00 55.27  ? 1126 ASN   A OD1 1 
ATOM   9839  N  ND2 . ASN   B 2 1126 ? 126.481 111.667 114.271 1.00 56.57  ? 1126 ASN   A ND2 1 
ATOM   9840  N  N   . ILE   B 2 1127 ? 130.066 109.574 114.909 1.00 49.09  ? 1127 ILE   A N   1 
ATOM   9841  C  CA  . ILE   B 2 1127 ? 130.499 108.369 114.215 1.00 45.01  ? 1127 ILE   A CA  1 
ATOM   9842  C  C   . ILE   B 2 1127 ? 131.600 108.777 113.249 1.00 50.20  ? 1127 ILE   A C   1 
ATOM   9843  O  O   . ILE   B 2 1127 ? 131.641 109.917 112.782 1.00 57.36  ? 1127 ILE   A O   1 
ATOM   9844  C  CB  . ILE   B 2 1127 ? 129.309 107.678 113.500 1.00 42.91  ? 1127 ILE   A CB  1 
ATOM   9845  C  CG1 . ILE   B 2 1127 ? 129.731 106.344 112.880 1.00 49.30  ? 1127 ILE   A CG1 1 
ATOM   9846  C  CG2 . ILE   B 2 1127 ? 128.707 108.595 112.460 1.00 49.81  ? 1127 ILE   A CG2 1 
ATOM   9847  C  CD1 . ILE   B 2 1127 ? 130.237 105.338 113.884 1.00 55.37  ? 1127 ILE   A CD1 1 
ATOM   9848  N  N   . ASP   B 2 1128 ? 132.508 107.846 112.964 1.00 40.40  ? 1128 ASP   A N   1 
ATOM   9849  C  CA  . ASP   B 2 1128 ? 133.661 108.156 112.132 1.00 39.24  ? 1128 ASP   A CA  1 
ATOM   9850  C  C   . ASP   B 2 1128 ? 133.234 108.468 110.700 1.00 47.59  ? 1128 ASP   A C   1 
ATOM   9851  O  O   . ASP   B 2 1128 ? 132.182 108.033 110.223 1.00 54.70  ? 1128 ASP   A O   1 
ATOM   9852  C  CB  . ASP   B 2 1128 ? 134.659 106.999 112.145 1.00 48.73  ? 1128 ASP   A CB  1 
ATOM   9853  C  CG  . ASP   B 2 1128 ? 134.064 105.709 111.627 1.00 54.90  ? 1128 ASP   A CG  1 
ATOM   9854  O  OD1 . ASP   B 2 1128 ? 132.856 105.479 111.846 1.00 59.87  ? 1128 ASP   A OD1 1 
ATOM   9855  O  OD2 . ASP   B 2 1128 ? 134.804 104.924 111.000 1.00 56.15  ? 1128 ASP   A OD2 1 
ATOM   9856  N  N   . ASP   B 2 1129 ? 134.076 109.243 110.011 1.00 52.79  ? 1129 ASP   A N   1 
ATOM   9857  C  CA  . ASP   B 2 1129 ? 133.737 109.714 108.672 1.00 45.11  ? 1129 ASP   A CA  1 
ATOM   9858  C  C   . ASP   B 2 1129 ? 133.688 108.582 107.655 1.00 52.25  ? 1129 ASP   A C   1 
ATOM   9859  O  O   . ASP   B 2 1129 ? 132.962 108.683 106.659 1.00 58.77  ? 1129 ASP   A O   1 
ATOM   9860  C  CB  . ASP   B 2 1129 ? 134.733 110.783 108.226 1.00 45.44  ? 1129 ASP   A CB  1 
ATOM   9861  C  CG  . ASP   B 2 1129 ? 136.167 110.375 108.464 1.00 52.30  ? 1129 ASP   A CG  1 
ATOM   9862  O  OD1 . ASP   B 2 1129 ? 136.389 109.354 109.144 1.00 56.34  ? 1129 ASP   A OD1 1 
ATOM   9863  O  OD2 . ASP   B 2 1129 ? 137.075 111.077 107.973 1.00 53.88  ? 1129 ASP   A OD2 1 
ATOM   9864  N  N   . GLU   B 2 1130 ? 134.447 107.506 107.877 1.00 57.46  ? 1130 GLU   A N   1 
ATOM   9865  C  CA  . GLU   B 2 1130 ? 134.397 106.373 106.960 1.00 47.84  ? 1130 GLU   A CA  1 
ATOM   9866  C  C   . GLU   B 2 1130 ? 133.001 105.769 106.913 1.00 51.16  ? 1130 GLU   A C   1 
ATOM   9867  O  O   . GLU   B 2 1130 ? 132.506 105.415 105.837 1.00 59.34  ? 1130 GLU   A O   1 
ATOM   9868  C  CB  . GLU   B 2 1130 ? 135.423 105.314 107.362 1.00 51.01  ? 1130 GLU   A CB  1 
ATOM   9869  C  CG  . GLU   B 2 1130 ? 136.872 105.721 107.146 1.00 59.19  ? 1130 GLU   A CG  1 
ATOM   9870  C  CD  . GLU   B 2 1130 ? 137.420 106.566 108.277 1.00 64.61  ? 1130 GLU   A CD  1 
ATOM   9871  O  OE1 . GLU   B 2 1130 ? 136.830 106.542 109.378 1.00 63.80  ? 1130 GLU   A OE1 1 
ATOM   9872  O  OE2 . GLU   B 2 1130 ? 138.441 107.254 108.067 1.00 62.54  ? 1130 GLU   A OE2 1 
ATOM   9873  N  N   . THR   B 2 1131 ? 132.350 105.639 108.070 1.00 47.68  ? 1131 THR   A N   1 
ATOM   9874  C  CA  . THR   B 2 1131 ? 130.999 105.093 108.104 1.00 44.66  ? 1131 THR   A CA  1 
ATOM   9875  C  C   . THR   B 2 1131 ? 130.004 106.031 107.432 1.00 46.22  ? 1131 THR   A C   1 
ATOM   9876  O  O   . THR   B 2 1131 ? 129.098 105.579 106.722 1.00 57.71  ? 1131 THR   A O   1 
ATOM   9877  C  CB  . THR   B 2 1131 ? 130.581 104.812 109.546 1.00 46.99  ? 1131 THR   A CB  1 
ATOM   9878  O  OG1 . THR   B 2 1131 ? 131.607 104.059 110.202 1.00 56.37  ? 1131 THR   A OG1 1 
ATOM   9879  C  CG2 . THR   B 2 1131 ? 129.294 104.018 109.580 1.00 47.35  ? 1131 THR   A CG2 1 
ATOM   9880  N  N   . LEU   B 2 1132 ? 130.151 107.340 107.650 1.00 44.66  ? 1132 LEU   A N   1 
ATOM   9881  C  CA  . LEU   B 2 1132 ? 129.242 108.301 107.033 1.00 45.15  ? 1132 LEU   A CA  1 
ATOM   9882  C  C   . LEU   B 2 1132 ? 129.375 108.294 105.517 1.00 41.92  ? 1132 LEU   A C   1 
ATOM   9883  O  O   . LEU   B 2 1132 ? 128.372 108.370 104.798 1.00 46.32  ? 1132 LEU   A O   1 
ATOM   9884  C  CB  . LEU   B 2 1132 ? 129.503 109.699 107.590 1.00 44.55  ? 1132 LEU   A CB  1 
ATOM   9885  C  CG  . LEU   B 2 1132 ? 129.119 109.929 109.050 1.00 35.45  ? 1132 LEU   A CG  1 
ATOM   9886  C  CD1 . LEU   B 2 1132 ? 129.518 111.316 109.493 1.00 40.54  ? 1132 LEU   A CD1 1 
ATOM   9887  C  CD2 . LEU   B 2 1132 ? 127.632 109.722 109.229 1.00 42.07  ? 1132 LEU   A CD2 1 
ATOM   9888  N  N   . MET   B 2 1133 ? 130.606 108.214 105.012 1.00 44.09  ? 1133 MET   A N   1 
ATOM   9889  C  CA  . MET   B 2 1133 ? 130.807 108.108 103.572 1.00 44.95  ? 1133 MET   A CA  1 
ATOM   9890  C  C   . MET   B 2 1133 ? 130.295 106.776 103.039 1.00 49.25  ? 1133 MET   A C   1 
ATOM   9891  O  O   . MET   B 2 1133 ? 129.716 106.719 101.948 1.00 56.73  ? 1133 MET   A O   1 
ATOM   9892  C  CB  . MET   B 2 1133 ? 132.285 108.290 103.236 1.00 45.04  ? 1133 MET   A CB  1 
ATOM   9893  C  CG  . MET   B 2 1133 ? 132.827 109.662 103.570 1.00 50.63  ? 1133 MET   A CG  1 
ATOM   9894  S  SD  . MET   B 2 1133 ? 132.191 110.952 102.490 1.00 63.23  ? 1133 MET   A SD  1 
ATOM   9895  C  CE  . MET   B 2 1133 ? 133.024 110.550 100.960 1.00 53.70  ? 1133 MET   A CE  1 
ATOM   9896  N  N   . ALA   B 2 1134 ? 130.497 105.696 103.793 1.00 41.38  ? 1134 ALA   A N   1 
ATOM   9897  C  CA  . ALA   B 2 1134 ? 130.089 104.372 103.342 1.00 37.33  ? 1134 ALA   A CA  1 
ATOM   9898  C  C   . ALA   B 2 1134 ? 128.589 104.152 103.462 1.00 41.93  ? 1134 ALA   A C   1 
ATOM   9899  O  O   . ALA   B 2 1134 ? 128.008 103.435 102.642 1.00 52.22  ? 1134 ALA   A O   1 
ATOM   9900  C  CB  . ALA   B 2 1134 ? 130.836 103.297 104.131 1.00 43.06  ? 1134 ALA   A CB  1 
ATOM   9901  N  N   . LEU   B 2 1135 ? 127.947 104.748 104.467 1.00 38.51  ? 1135 LEU   A N   1 
ATOM   9902  C  CA  . LEU   B 2 1135 ? 126.518 104.570 104.717 1.00 37.32  ? 1135 LEU   A CA  1 
ATOM   9903  C  C   . LEU   B 2 1135 ? 125.842 105.933 104.711 1.00 43.93  ? 1135 LEU   A C   1 
ATOM   9904  O  O   . LEU   B 2 1135 ? 125.695 106.569 105.767 1.00 49.54  ? 1135 LEU   A O   1 
ATOM   9905  C  CB  . LEU   B 2 1135 ? 126.278 103.843 106.038 1.00 39.37  ? 1135 LEU   A CB  1 
ATOM   9906  C  CG  . LEU   B 2 1135 ? 126.685 102.372 106.074 1.00 41.53  ? 1135 LEU   A CG  1 
ATOM   9907  C  CD1 . LEU   B 2 1135 ? 126.554 101.821 107.477 1.00 46.51  ? 1135 LEU   A CD1 1 
ATOM   9908  C  CD2 . LEU   B 2 1135 ? 125.835 101.569 105.107 1.00 47.35  ? 1135 LEU   A CD2 1 
ATOM   9909  N  N   . PRO   B 2 1136 ? 125.421 106.424 103.545 1.00 37.73  ? 1136 PRO   A N   1 
ATOM   9910  C  CA  . PRO   B 2 1136 ? 124.710 107.709 103.503 1.00 33.57  ? 1136 PRO   A CA  1 
ATOM   9911  C  C   . PRO   B 2 1136 ? 123.378 107.692 104.226 1.00 41.67  ? 1136 PRO   A C   1 
ATOM   9912  O  O   . PRO   B 2 1136 ? 122.846 108.765 104.532 1.00 50.15  ? 1136 PRO   A O   1 
ATOM   9913  C  CB  . PRO   B 2 1136 ? 124.529 107.958 102.001 1.00 34.49  ? 1136 PRO   A CB  1 
ATOM   9914  C  CG  . PRO   B 2 1136 ? 125.586 107.141 101.352 1.00 35.67  ? 1136 PRO   A CG  1 
ATOM   9915  C  CD  . PRO   B 2 1136 ? 125.715 105.917 102.196 1.00 42.96  ? 1136 PRO   A CD  1 
ATOM   9916  N  N   . GLU   B 2 1137 ? 122.817 106.514 104.504 1.00 42.19  ? 1137 GLU   A N   1 
ATOM   9917  C  CA  . GLU   B 2 1137 ? 121.533 106.439 105.189 1.00 36.91  ? 1137 GLU   A CA  1 
ATOM   9918  C  C   . GLU   B 2 1137 ? 121.598 106.985 106.608 1.00 38.73  ? 1137 GLU   A C   1 
ATOM   9919  O  O   . GLU   B 2 1137 ? 120.551 107.280 107.192 1.00 48.93  ? 1137 GLU   A O   1 
ATOM   9920  C  CB  . GLU   B 2 1137 ? 121.027 104.997 105.213 1.00 40.08  ? 1137 GLU   A CB  1 
ATOM   9921  C  CG  . GLU   B 2 1137 ? 120.569 104.462 103.867 1.00 42.31  ? 1137 GLU   A CG  1 
ATOM   9922  C  CD  . GLU   B 2 1137 ? 121.717 104.085 102.958 1.00 50.05  ? 1137 GLU   A CD  1 
ATOM   9923  O  OE1 . GLU   B 2 1137 ? 122.871 104.059 103.434 1.00 57.62  ? 1137 GLU   A OE1 1 
ATOM   9924  O  OE2 . GLU   B 2 1137 ? 121.466 103.812 101.766 1.00 54.63  ? 1137 GLU   A OE2 1 
ATOM   9925  N  N   . LEU   B 2 1138 ? 122.797 107.128 107.175 1.00 38.17  ? 1138 LEU   A N   1 
ATOM   9926  C  CA  . LEU   B 2 1138 ? 122.943 107.700 108.506 1.00 38.82  ? 1138 LEU   A CA  1 
ATOM   9927  C  C   . LEU   B 2 1138 ? 122.640 109.191 108.540 1.00 45.12  ? 1138 LEU   A C   1 
ATOM   9928  O  O   . LEU   B 2 1138 ? 122.549 109.763 109.631 1.00 53.47  ? 1138 LEU   A O   1 
ATOM   9929  C  CB  . LEU   B 2 1138 ? 124.355 107.451 109.034 1.00 39.42  ? 1138 LEU   A CB  1 
ATOM   9930  C  CG  . LEU   B 2 1138 ? 124.795 106.000 109.229 1.00 42.81  ? 1138 LEU   A CG  1 
ATOM   9931  C  CD1 . LEU   B 2 1138 ? 126.204 105.958 109.769 1.00 42.00  ? 1138 LEU   A CD1 1 
ATOM   9932  C  CD2 . LEU   B 2 1138 ? 123.849 105.268 110.155 1.00 45.99  ? 1138 LEU   A CD2 1 
ATOM   9933  N  N   . TYR   B 2 1139 ? 122.480 109.825 107.379 1.00 37.90  ? 1139 TYR   A N   1 
ATOM   9934  C  CA  . TYR   B 2 1139 ? 122.186 111.248 107.261 1.00 22.26  ? 1139 TYR   A CA  1 
ATOM   9935  C  C   . TYR   B 2 1139 ? 120.754 111.595 107.646 1.00 37.95  ? 1139 TYR   A C   1 
ATOM   9936  O  O   . TYR   B 2 1139 ? 120.423 112.782 107.692 1.00 57.16  ? 1139 TYR   A O   1 
ATOM   9937  C  CB  . TYR   B 2 1139 ? 122.478 111.698 105.828 1.00 34.05  ? 1139 TYR   A CB  1 
ATOM   9938  C  CG  . TYR   B 2 1139 ? 122.521 113.191 105.604 1.00 35.59  ? 1139 TYR   A CG  1 
ATOM   9939  C  CD1 . TYR   B 2 1139 ? 123.631 113.936 105.968 1.00 42.58  ? 1139 TYR   A CD1 1 
ATOM   9940  C  CD2 . TYR   B 2 1139 ? 121.464 113.849 104.998 1.00 37.31  ? 1139 TYR   A CD2 1 
ATOM   9941  C  CE1 . TYR   B 2 1139 ? 123.676 115.296 105.752 1.00 42.33  ? 1139 TYR   A CE1 1 
ATOM   9942  C  CE2 . TYR   B 2 1139 ? 121.501 115.205 104.779 1.00 33.09  ? 1139 TYR   A CE2 1 
ATOM   9943  C  CZ  . TYR   B 2 1139 ? 122.607 115.923 105.155 1.00 38.32  ? 1139 TYR   A CZ  1 
ATOM   9944  O  OH  . TYR   B 2 1139 ? 122.645 117.278 104.938 1.00 53.15  ? 1139 TYR   A OH  1 
ATOM   9945  N  N   . ARG   B 2 1140 ? 119.903 110.601 107.917 1.00 36.45  ? 1140 ARG   A N   1 
ATOM   9946  C  CA  . ARG   B 2 1140 ? 118.507 110.875 108.248 1.00 33.50  ? 1140 ARG   A CA  1 
ATOM   9947  C  C   . ARG   B 2 1140 ? 118.384 111.712 109.513 1.00 41.27  ? 1140 ARG   A C   1 
ATOM   9948  O  O   . ARG   B 2 1140 ? 117.593 112.660 109.568 1.00 52.69  ? 1140 ARG   A O   1 
ATOM   9949  C  CB  . ARG   B 2 1140 ? 117.739 109.565 108.415 1.00 42.91  ? 1140 ARG   A CB  1 
ATOM   9950  C  CG  . ARG   B 2 1140 ? 117.369 108.877 107.122 1.00 47.14  ? 1140 ARG   A CG  1 
ATOM   9951  C  CD  . ARG   B 2 1140 ? 115.865 108.704 107.030 1.00 47.03  ? 1140 ARG   A CD  1 
ATOM   9952  N  NE  . ARG   B 2 1140 ? 115.303 108.156 108.258 1.00 49.68  ? 1140 ARG   A NE  1 
ATOM   9953  C  CZ  . ARG   B 2 1140 ? 115.092 106.866 108.475 1.00 54.16  ? 1140 ARG   A CZ  1 
ATOM   9954  N  NH1 . ARG   B 2 1140 ? 115.389 105.954 107.563 1.00 48.69  ? 1140 ARG   A NH1 1 
ATOM   9955  N  NH2 . ARG   B 2 1140 ? 114.569 106.480 109.635 1.00 51.61  ? 1140 ARG   A NH2 1 
ATOM   9956  N  N   . ALA   B 2 1141 ? 119.152 111.368 110.549 1.00 36.97  ? 1141 ALA   A N   1 
ATOM   9957  C  CA  . ALA   B 2 1141 ? 119.027 112.070 111.822 1.00 34.51  ? 1141 ALA   A CA  1 
ATOM   9958  C  C   . ALA   B 2 1141 ? 119.365 113.545 111.671 1.00 42.13  ? 1141 ALA   A C   1 
ATOM   9959  O  O   . ALA   B 2 1141 ? 118.695 114.407 112.252 1.00 53.07  ? 1141 ALA   A O   1 
ATOM   9960  C  CB  . ALA   B 2 1141 ? 119.924 111.416 112.872 1.00 47.53  ? 1141 ALA   A CB  1 
ATOM   9961  N  N   . SER   B 2 1142 ? 120.403 113.855 110.896 1.00 36.39  ? 1142 SER   A N   1 
ATOM   9962  C  CA  . SER   B 2 1142 ? 120.766 115.248 110.671 1.00 37.88  ? 1142 SER   A CA  1 
ATOM   9963  C  C   . SER   B 2 1142 ? 119.777 115.934 109.738 1.00 41.40  ? 1142 SER   A C   1 
ATOM   9964  O  O   . SER   B 2 1142 ? 119.456 117.114 109.922 1.00 50.60  ? 1142 SER   A O   1 
ATOM   9965  C  CB  . SER   B 2 1142 ? 122.184 115.326 110.111 1.00 42.19  ? 1142 SER   A CB  1 
ATOM   9966  O  OG  . SER   B 2 1142 ? 122.601 116.670 109.960 1.00 51.23  ? 1142 SER   A OG  1 
ATOM   9967  N  N   . ARG   B 2 1143 ? 119.279 115.210 108.736 1.00 35.49  ? 1143 ARG   A N   1 
ATOM   9968  C  CA  . ARG   B 2 1143 ? 118.379 115.803 107.755 1.00 31.35  ? 1143 ARG   A CA  1 
ATOM   9969  C  C   . ARG   B 2 1143 ? 116.994 116.057 108.334 1.00 38.32  ? 1143 ARG   A C   1 
ATOM   9970  O  O   . ARG   B 2 1143 ? 116.343 117.041 107.967 1.00 43.80  ? 1143 ARG   A O   1 
ATOM   9971  C  CB  . ARG   B 2 1143 ? 118.292 114.897 106.530 1.00 42.21  ? 1143 ARG   A CB  1 
ATOM   9972  C  CG  . ARG   B 2 1143 ? 117.353 115.375 105.446 1.00 44.68  ? 1143 ARG   A CG  1 
ATOM   9973  C  CD  . ARG   B 2 1143 ? 117.321 114.392 104.294 1.00 39.58  ? 1143 ARG   A CD  1 
ATOM   9974  N  NE  . ARG   B 2 1143 ? 116.921 113.058 104.721 1.00 35.76  ? 1143 ARG   A NE  1 
ATOM   9975  C  CZ  . ARG   B 2 1143 ? 115.668 112.631 104.764 1.00 41.42  ? 1143 ARG   A CZ  1 
ATOM   9976  N  NH1 . ARG   B 2 1143 ? 114.659 113.416 104.428 1.00 46.83  ? 1143 ARG   A NH1 1 
ATOM   9977  N  NH2 . ARG   B 2 1143 ? 115.420 111.384 105.153 1.00 44.83  ? 1143 ARG   A NH2 1 
ATOM   9978  N  N   . GLU   B 2 1144 ? 116.530 115.197 109.234 1.00 42.52  ? 1144 GLU   A N   1 
ATOM   9979  C  CA  . GLU   B 2 1144 ? 115.208 115.338 109.825 1.00 35.54  ? 1144 GLU   A CA  1 
ATOM   9980  C  C   . GLU   B 2 1144 ? 115.198 116.247 111.046 1.00 43.11  ? 1144 GLU   A C   1 
ATOM   9981  O  O   . GLU   B 2 1144 ? 114.146 116.403 111.673 1.00 50.86  ? 1144 GLU   A O   1 
ATOM   9982  C  CB  . GLU   B 2 1144 ? 114.648 113.963 110.194 1.00 42.01  ? 1144 GLU   A CB  1 
ATOM   9983  C  CG  . GLU   B 2 1144 ? 114.341 113.088 108.994 1.00 45.78  ? 1144 GLU   A CG  1 
ATOM   9984  C  CD  . GLU   B 2 1144 ? 113.697 111.773 109.374 1.00 56.64  ? 1144 GLU   A CD  1 
ATOM   9985  O  OE1 . GLU   B 2 1144 ? 113.585 111.491 110.585 1.00 60.67  ? 1144 GLU   A OE1 1 
ATOM   9986  O  OE2 . GLU   B 2 1144 ? 113.301 111.019 108.461 1.00 57.63  ? 1144 GLU   A OE2 1 
ATOM   9987  N  N   . GLY   B 2 1145 ? 116.333 116.846 111.394 1.00 45.85  ? 1145 GLY   A N   1 
ATOM   9988  C  CA  . GLY   B 2 1145 ? 116.399 117.791 112.490 1.00 43.79  ? 1145 GLY   A CA  1 
ATOM   9989  C  C   . GLY   B 2 1145 ? 116.126 117.185 113.850 1.00 47.31  ? 1145 GLY   A C   1 
ATOM   9990  O  O   . GLY   B 2 1145 ? 115.386 117.758 114.654 1.00 55.24  ? 1145 GLY   A O   1 
ATOM   9991  N  N   . LYS   B 2 1146 ? 116.719 116.025 114.118 1.00 42.47  ? 1146 LYS   A N   1 
ATOM   9992  C  CA  . LYS   B 2 1146 ? 116.534 115.329 115.381 1.00 41.26  ? 1146 LYS   A CA  1 
ATOM   9993  C  C   . LYS   B 2 1146 ? 117.623 115.648 116.395 1.00 39.77  ? 1146 LYS   A C   1 
ATOM   9994  O  O   . LYS   B 2 1146 ? 117.641 115.052 117.476 1.00 46.55  ? 1146 LYS   A O   1 
ATOM   9995  C  CB  . LYS   B 2 1146 ? 116.461 113.820 115.144 1.00 44.47  ? 1146 LYS   A CB  1 
ATOM   9996  C  CG  . LYS   B 2 1146 ? 115.143 113.363 114.547 1.00 46.37  ? 1146 LYS   A CG  1 
ATOM   9997  C  CD  . LYS   B 2 1146 ? 115.121 111.864 114.328 1.00 47.74  ? 1146 LYS   A CD  1 
ATOM   9998  C  CE  . LYS   B 2 1146 ? 113.726 111.386 113.964 1.00 53.57  ? 1146 LYS   A CE  1 
ATOM   9999  N  NZ  . LYS   B 2 1146 ? 113.188 112.092 112.769 1.00 52.74  ? 1146 LYS   A NZ  1 
ATOM   10000 N  N   . TYR   B 2 1147 ? 118.529 116.567 116.074 1.00 35.45  ? 1147 TYR   A N   1 
ATOM   10001 C  CA  . TYR   B 2 1147 ? 119.586 116.955 116.997 1.00 30.30  ? 1147 TYR   A CA  1 
ATOM   10002 C  C   . TYR   B 2 1147 ? 119.319 118.277 117.697 1.00 42.22  ? 1147 TYR   A C   1 
ATOM   10003 O  O   . TYR   B 2 1147 ? 119.820 118.486 118.806 1.00 54.94  ? 1147 TYR   A O   1 
ATOM   10004 C  CB  . TYR   B 2 1147 ? 120.927 117.041 116.264 1.00 39.66  ? 1147 TYR   A CB  1 
ATOM   10005 C  CG  . TYR   B 2 1147 ? 121.444 115.713 115.768 1.00 42.06  ? 1147 TYR   A CG  1 
ATOM   10006 C  CD1 . TYR   B 2 1147 ? 121.030 114.525 116.347 1.00 44.61  ? 1147 TYR   A CD1 1 
ATOM   10007 C  CD2 . TYR   B 2 1147 ? 122.348 115.650 114.721 1.00 41.75  ? 1147 TYR   A CD2 1 
ATOM   10008 C  CE1 . TYR   B 2 1147 ? 121.501 113.312 115.895 1.00 42.26  ? 1147 TYR   A CE1 1 
ATOM   10009 C  CE2 . TYR   B 2 1147 ? 122.822 114.445 114.264 1.00 38.05  ? 1147 TYR   A CE2 1 
ATOM   10010 C  CZ  . TYR   B 2 1147 ? 122.398 113.279 114.854 1.00 39.70  ? 1147 TYR   A CZ  1 
ATOM   10011 O  OH  . TYR   B 2 1147 ? 122.871 112.072 114.399 1.00 49.28  ? 1147 TYR   A OH  1 
ATOM   10012 N  N   . PHE   B 2 1148 ? 118.546 119.170 117.087 1.00 42.67  ? 1148 PHE   A N   1 
ATOM   10013 C  CA  . PHE   B 2 1148 ? 118.253 120.475 117.662 1.00 32.59  ? 1148 PHE   A CA  1 
ATOM   10014 C  C   . PHE   B 2 1148 ? 116.758 120.728 117.576 1.00 35.77  ? 1148 PHE   A C   1 
ATOM   10015 O  O   . PHE   B 2 1148 ? 116.144 120.486 116.534 1.00 43.92  ? 1148 PHE   A O   1 
ATOM   10016 C  CB  . PHE   B 2 1148 ? 119.023 121.579 116.937 1.00 36.54  ? 1148 PHE   A CB  1 
ATOM   10017 C  CG  . PHE   B 2 1148 ? 119.128 122.856 117.712 1.00 40.52  ? 1148 PHE   A CG  1 
ATOM   10018 C  CD1 . PHE   B 2 1148 ? 120.016 122.969 118.764 1.00 44.82  ? 1148 PHE   A CD1 1 
ATOM   10019 C  CD2 . PHE   B 2 1148 ? 118.352 123.948 117.380 1.00 41.67  ? 1148 PHE   A CD2 1 
ATOM   10020 C  CE1 . PHE   B 2 1148 ? 120.119 124.142 119.474 1.00 41.53  ? 1148 PHE   A CE1 1 
ATOM   10021 C  CE2 . PHE   B 2 1148 ? 118.455 125.124 118.089 1.00 44.65  ? 1148 PHE   A CE2 1 
ATOM   10022 C  CZ  . PHE   B 2 1148 ? 119.339 125.219 119.136 1.00 40.96  ? 1148 PHE   A CZ  1 
ATOM   10023 N  N   . GLY   B 2 1149 ? 116.179 121.212 118.666 1.00 40.26  ? 1149 GLY   A N   1 
ATOM   10024 C  CA  . GLY   B 2 1149 ? 114.753 121.467 118.698 1.00 37.52  ? 1149 GLY   A CA  1 
ATOM   10025 C  C   . GLY   B 2 1149 ? 114.332 121.910 120.079 1.00 45.72  ? 1149 GLY   A C   1 
ATOM   10026 O  O   . GLY   B 2 1149 ? 115.154 122.066 120.987 1.00 58.12  ? 1149 GLY   A O   1 
ATOM   10027 N  N   . LEU   B 2 1150 ? 113.022 122.114 120.227 1.00 39.47  ? 1150 LEU   A N   1 
ATOM   10028 C  CA  . LEU   B 2 1150 ? 112.483 122.566 121.503 1.00 42.33  ? 1150 LEU   A CA  1 
ATOM   10029 C  C   . LEU   B 2 1150 ? 112.453 121.459 122.548 1.00 46.79  ? 1150 LEU   A C   1 
ATOM   10030 O  O   . LEU   B 2 1150 ? 112.597 121.743 123.741 1.00 52.66  ? 1150 LEU   A O   1 
ATOM   10031 C  CB  . LEU   B 2 1150 ? 111.080 123.141 121.313 1.00 40.62  ? 1150 LEU   A CB  1 
ATOM   10032 C  CG  . LEU   B 2 1150 ? 111.003 124.567 120.765 1.00 46.18  ? 1150 LEU   A CG  1 
ATOM   10033 C  CD1 . LEU   B 2 1150 ? 109.560 124.999 120.589 1.00 46.82  ? 1150 LEU   A CD1 1 
ATOM   10034 C  CD2 . LEU   B 2 1150 ? 111.741 125.526 121.679 1.00 47.00  ? 1150 LEU   A CD2 1 
ATOM   10035 N  N   . MET   B 2 1151 ? 112.258 120.206 122.136 1.00 42.79  ? 1151 MET   A N   1 
ATOM   10036 C  CA  . MET   B 2 1151 ? 112.183 119.116 123.105 1.00 36.55  ? 1151 MET   A CA  1 
ATOM   10037 C  C   . MET   B 2 1151 ? 113.537 118.858 123.755 1.00 38.75  ? 1151 MET   A C   1 
ATOM   10038 O  O   . MET   B 2 1151 ? 113.626 118.681 124.976 1.00 52.21  ? 1151 MET   A O   1 
ATOM   10039 C  CB  . MET   B 2 1151 ? 111.653 117.852 122.431 1.00 41.80  ? 1151 MET   A CB  1 
ATOM   10040 C  CG  . MET   B 2 1151 ? 110.198 117.942 122.020 1.00 47.46  ? 1151 MET   A CG  1 
ATOM   10041 S  SD  . MET   B 2 1151 ? 109.093 118.145 123.430 1.00 73.38  ? 1151 MET   A SD  1 
ATOM   10042 C  CE  . MET   B 2 1151 ? 109.346 116.593 124.285 1.00 54.05  ? 1151 MET   A CE  1 
ATOM   10043 N  N   . ARG   B 2 1152 ? 114.606 118.831 122.957 1.00 34.36  ? 1152 ARG   A N   1 
ATOM   10044 C  CA  . ARG   B 2 1152 ? 115.943 118.682 123.522 1.00 39.29  ? 1152 ARG   A CA  1 
ATOM   10045 C  C   . ARG   B 2 1152 ? 116.297 119.867 124.408 1.00 41.13  ? 1152 ARG   A C   1 
ATOM   10046 O  O   . ARG   B 2 1152 ? 116.910 119.703 125.472 1.00 49.17  ? 1152 ARG   A O   1 
ATOM   10047 C  CB  . ARG   B 2 1152 ? 116.972 118.522 122.404 1.00 38.12  ? 1152 ARG   A CB  1 
ATOM   10048 C  CG  . ARG   B 2 1152 ? 116.890 117.208 121.661 1.00 33.54  ? 1152 ARG   A CG  1 
ATOM   10049 C  CD  . ARG   B 2 1152 ? 118.152 116.390 121.860 1.00 38.56  ? 1152 ARG   A CD  1 
ATOM   10050 N  NE  . ARG   B 2 1152 ? 119.327 117.058 121.315 1.00 49.95  ? 1152 ARG   A NE  1 
ATOM   10051 C  CZ  . ARG   B 2 1152 ? 120.562 116.584 121.392 1.00 51.63  ? 1152 ARG   A CZ  1 
ATOM   10052 N  NH1 . ARG   B 2 1152 ? 120.825 115.435 121.993 1.00 45.25  ? 1152 ARG   A NH1 1 
ATOM   10053 N  NH2 . ARG   B 2 1152 ? 121.559 117.278 120.853 1.00 47.05  ? 1152 ARG   A NH2 1 
ATOM   10054 N  N   . PHE   B 2 1153 ? 115.920 121.072 123.982 1.00 28.93  ? 1153 PHE   A N   1 
ATOM   10055 C  CA  . PHE   B 2 1153 ? 116.163 122.263 124.785 1.00 28.69  ? 1153 PHE   A CA  1 
ATOM   10056 C  C   . PHE   B 2 1153 ? 115.461 122.162 126.132 1.00 36.17  ? 1153 PHE   A C   1 
ATOM   10057 O  O   . PHE   B 2 1153 ? 116.052 122.456 127.177 1.00 44.15  ? 1153 PHE   A O   1 
ATOM   10058 C  CB  . PHE   B 2 1153 ? 115.703 123.498 124.009 1.00 30.36  ? 1153 PHE   A CB  1 
ATOM   10059 C  CG  . PHE   B 2 1153 ? 115.695 124.764 124.812 1.00 39.56  ? 1153 PHE   A CG  1 
ATOM   10060 C  CD1 . PHE   B 2 1153 ? 116.870 125.438 125.079 1.00 35.80  ? 1153 PHE   A CD1 1 
ATOM   10061 C  CD2 . PHE   B 2 1153 ? 114.504 125.298 125.270 1.00 37.85  ? 1153 PHE   A CD2 1 
ATOM   10062 C  CE1 . PHE   B 2 1153 ? 116.860 126.607 125.807 1.00 38.17  ? 1153 PHE   A CE1 1 
ATOM   10063 C  CE2 . PHE   B 2 1153 ? 114.489 126.466 125.997 1.00 36.14  ? 1153 PHE   A CE2 1 
ATOM   10064 C  CZ  . PHE   B 2 1153 ? 115.669 127.121 126.265 1.00 39.25  ? 1153 PHE   A CZ  1 
ATOM   10065 N  N   . ALA   B 2 1154 ? 114.202 121.719 126.127 1.00 34.14  ? 1154 ALA   A N   1 
ATOM   10066 C  CA  . ALA   B 2 1154 ? 113.463 121.561 127.373 1.00 32.49  ? 1154 ALA   A CA  1 
ATOM   10067 C  C   . ALA   B 2 1154 ? 114.088 120.490 128.252 1.00 35.25  ? 1154 ALA   A C   1 
ATOM   10068 O  O   . ALA   B 2 1154 ? 114.161 120.647 129.476 1.00 36.65  ? 1154 ALA   A O   1 
ATOM   10069 C  CB  . ALA   B 2 1154 ? 112.002 121.225 127.079 1.00 37.24  ? 1154 ALA   A CB  1 
ATOM   10070 N  N   . TYR   B 2 1155 ? 114.537 119.388 127.649 1.00 37.78  ? 1155 TYR   A N   1 
ATOM   10071 C  CA  . TYR   B 2 1155 ? 115.176 118.333 128.427 1.00 30.59  ? 1155 TYR   A CA  1 
ATOM   10072 C  C   . TYR   B 2 1155 ? 116.427 118.851 129.121 1.00 39.89  ? 1155 TYR   A C   1 
ATOM   10073 O  O   . TYR   B 2 1155 ? 116.645 118.590 130.307 1.00 54.11  ? 1155 TYR   A O   1 
ATOM   10074 C  CB  . TYR   B 2 1155 ? 115.516 117.144 127.531 1.00 30.16  ? 1155 TYR   A CB  1 
ATOM   10075 C  CG  . TYR   B 2 1155 ? 116.429 116.132 128.188 1.00 34.03  ? 1155 TYR   A CG  1 
ATOM   10076 C  CD1 . TYR   B 2 1155 ? 115.941 115.230 129.120 1.00 39.38  ? 1155 TYR   A CD1 1 
ATOM   10077 C  CD2 . TYR   B 2 1155 ? 117.778 116.078 127.873 1.00 40.57  ? 1155 TYR   A CD2 1 
ATOM   10078 C  CE1 . TYR   B 2 1155 ? 116.770 114.307 129.722 1.00 41.26  ? 1155 TYR   A CE1 1 
ATOM   10079 C  CE2 . TYR   B 2 1155 ? 118.614 115.158 128.470 1.00 44.98  ? 1155 TYR   A CE2 1 
ATOM   10080 C  CZ  . TYR   B 2 1155 ? 118.104 114.275 129.394 1.00 44.22  ? 1155 TYR   A CZ  1 
ATOM   10081 O  OH  . TYR   B 2 1155 ? 118.933 113.355 129.992 1.00 44.55  ? 1155 TYR   A OH  1 
ATOM   10082 N  N   . TYR   B 2 1156 ? 117.260 119.597 128.396 1.00 31.54  ? 1156 TYR   A N   1 
ATOM   10083 C  CA  . TYR   B 2 1156 ? 118.482 120.112 129.003 1.00 24.85  ? 1156 TYR   A CA  1 
ATOM   10084 C  C   . TYR   B 2 1156 ? 118.179 121.155 130.074 1.00 35.79  ? 1156 TYR   A C   1 
ATOM   10085 O  O   . TYR   B 2 1156 ? 118.821 121.168 131.134 1.00 47.41  ? 1156 TYR   A O   1 
ATOM   10086 C  CB  . TYR   B 2 1156 ? 119.403 120.673 127.925 1.00 29.90  ? 1156 TYR   A CB  1 
ATOM   10087 C  CG  . TYR   B 2 1156 ? 120.243 119.608 127.257 1.00 35.72  ? 1156 TYR   A CG  1 
ATOM   10088 C  CD1 . TYR   B 2 1156 ? 119.691 118.749 126.321 1.00 36.25  ? 1156 TYR   A CD1 1 
ATOM   10089 C  CD2 . TYR   B 2 1156 ? 121.584 119.459 127.569 1.00 40.39  ? 1156 TYR   A CD2 1 
ATOM   10090 C  CE1 . TYR   B 2 1156 ? 120.450 117.775 125.713 1.00 37.06  ? 1156 TYR   A CE1 1 
ATOM   10091 C  CE2 . TYR   B 2 1156 ? 122.352 118.487 126.964 1.00 39.47  ? 1156 TYR   A CE2 1 
ATOM   10092 C  CZ  . TYR   B 2 1156 ? 121.779 117.648 126.036 1.00 38.23  ? 1156 TYR   A CZ  1 
ATOM   10093 O  OH  . TYR   B 2 1156 ? 122.539 116.677 125.428 1.00 42.47  ? 1156 TYR   A OH  1 
ATOM   10094 N  N   . ILE   B 2 1157 ? 117.189 122.020 129.833 1.00 38.41  ? 1157 ILE   A N   1 
ATOM   10095 C  CA  . ILE   B 2 1157 ? 116.824 123.027 130.828 1.00 33.69  ? 1157 ILE   A CA  1 
ATOM   10096 C  C   . ILE   B 2 1157 ? 116.328 122.359 132.106 1.00 32.34  ? 1157 ILE   A C   1 
ATOM   10097 O  O   . ILE   B 2 1157 ? 116.712 122.743 133.217 1.00 42.84  ? 1157 ILE   A O   1 
ATOM   10098 C  CB  . ILE   B 2 1157 ? 115.774 123.999 130.258 1.00 35.67  ? 1157 ILE   A CB  1 
ATOM   10099 C  CG1 . ILE   B 2 1157 ? 116.343 124.798 129.085 1.00 32.58  ? 1157 ILE   A CG1 1 
ATOM   10100 C  CG2 . ILE   B 2 1157 ? 115.270 124.940 131.339 1.00 32.65  ? 1157 ILE   A CG2 1 
ATOM   10101 C  CD1 . ILE   B 2 1157 ? 117.676 125.431 129.347 1.00 39.46  ? 1157 ILE   A CD1 1 
ATOM   10102 N  N   . PHE   B 2 1158 ? 115.476 121.341 131.970 1.00 29.27  ? 1158 PHE   A N   1 
ATOM   10103 C  CA  . PHE   B 2 1158 ? 114.920 120.700 133.156 1.00 32.96  ? 1158 PHE   A CA  1 
ATOM   10104 C  C   . PHE   B 2 1158 ? 115.951 119.822 133.855 1.00 38.66  ? 1158 PHE   A C   1 
ATOM   10105 O  O   . PHE   B 2 1158 ? 115.915 119.694 135.085 1.00 52.04  ? 1158 PHE   A O   1 
ATOM   10106 C  CB  . PHE   B 2 1158 ? 113.658 119.916 132.781 1.00 33.16  ? 1158 PHE   A CB  1 
ATOM   10107 C  CG  . PHE   B 2 1158 ? 113.788 118.427 132.915 1.00 44.26  ? 1158 PHE   A CG  1 
ATOM   10108 C  CD1 . PHE   B 2 1158 ? 114.226 117.659 131.850 1.00 51.32  ? 1158 PHE   A CD1 1 
ATOM   10109 C  CD2 . PHE   B 2 1158 ? 113.437 117.787 134.094 1.00 48.00  ? 1158 PHE   A CD2 1 
ATOM   10110 C  CE1 . PHE   B 2 1158 ? 114.337 116.287 131.963 1.00 49.47  ? 1158 PHE   A CE1 1 
ATOM   10111 C  CE2 . PHE   B 2 1158 ? 113.547 116.415 134.213 1.00 48.64  ? 1158 PHE   A CE2 1 
ATOM   10112 C  CZ  . PHE   B 2 1158 ? 113.996 115.665 133.146 1.00 46.70  ? 1158 PHE   A CZ  1 
ATOM   10113 N  N   . GLU   B 2 1159 ? 116.895 119.244 133.108 1.00 33.27  ? 1159 GLU   A N   1 
ATOM   10114 C  CA  . GLU   B 2 1159 ? 118.024 118.572 133.743 1.00 34.01  ? 1159 GLU   A CA  1 
ATOM   10115 C  C   . GLU   B 2 1159 ? 118.835 119.548 134.582 1.00 33.88  ? 1159 GLU   A C   1 
ATOM   10116 O  O   . GLU   B 2 1159 ? 119.208 119.239 135.720 1.00 44.03  ? 1159 GLU   A O   1 
ATOM   10117 C  CB  . GLU   B 2 1159 ? 118.914 117.919 132.684 1.00 37.96  ? 1159 GLU   A CB  1 
ATOM   10118 C  CG  . GLU   B 2 1159 ? 118.394 116.598 132.146 1.00 45.31  ? 1159 GLU   A CG  1 
ATOM   10119 C  CD  . GLU   B 2 1159 ? 118.680 115.437 133.076 1.00 51.44  ? 1159 GLU   A CD  1 
ATOM   10120 O  OE1 . GLU   B 2 1159 ? 119.487 115.609 134.013 1.00 50.52  ? 1159 GLU   A OE1 1 
ATOM   10121 O  OE2 . GLU   B 2 1159 ? 118.098 114.351 132.870 1.00 53.38  ? 1159 GLU   A OE2 1 
ATOM   10122 N  N   . GLY   B 2 1160 ? 119.114 120.733 134.038 1.00 39.78  ? 1160 GLY   A N   1 
ATOM   10123 C  CA  . GLY   B 2 1160 ? 119.825 121.738 134.810 1.00 34.04  ? 1160 GLY   A CA  1 
ATOM   10124 C  C   . GLY   B 2 1160 ? 119.063 122.167 136.048 1.00 36.73  ? 1160 GLY   A C   1 
ATOM   10125 O  O   . GLY   B 2 1160 ? 119.647 122.329 137.123 1.00 46.55  ? 1160 GLY   A O   1 
ATOM   10126 N  N   . VAL   B 2 1161 ? 117.748 122.344 135.918 1.00 25.19  ? 1161 VAL   A N   1 
ATOM   10127 C  CA  . VAL   B 2 1161 ? 116.927 122.739 137.062 1.00 25.60  ? 1161 VAL   A CA  1 
ATOM   10128 C  C   . VAL   B 2 1161 ? 116.981 121.674 138.151 1.00 29.98  ? 1161 VAL   A C   1 
ATOM   10129 O  O   . VAL   B 2 1161 ? 117.199 121.977 139.331 1.00 39.26  ? 1161 VAL   A O   1 
ATOM   10130 C  CB  . VAL   B 2 1161 ? 115.480 123.013 136.613 1.00 21.40  ? 1161 VAL   A CB  1 
ATOM   10131 C  CG1 . VAL   B 2 1161 ? 114.567 123.139 137.812 1.00 28.56  ? 1161 VAL   A CG1 1 
ATOM   10132 C  CG2 . VAL   B 2 1161 ? 115.419 124.273 135.771 1.00 34.77  ? 1161 VAL   A CG2 1 
ATOM   10133 N  N   . TYR   B 2 1162 ? 116.804 120.408 137.766 1.00 19.98  ? 1162 TYR   A N   1 
ATOM   10134 C  CA  . TYR   B 2 1162 ? 116.838 119.324 138.742 1.00 17.74  ? 1162 TYR   A CA  1 
ATOM   10135 C  C   . TYR   B 2 1162 ? 118.197 119.227 139.422 1.00 31.48  ? 1162 TYR   A C   1 
ATOM   10136 O  O   . TYR   B 2 1162 ? 118.278 119.061 140.646 1.00 40.35  ? 1162 TYR   A O   1 
ATOM   10137 C  CB  . TYR   B 2 1162 ? 116.489 117.999 138.067 1.00 26.35  ? 1162 TYR   A CB  1 
ATOM   10138 C  CG  . TYR   B 2 1162 ? 117.040 116.794 138.789 1.00 25.44  ? 1162 TYR   A CG  1 
ATOM   10139 C  CD1 . TYR   B 2 1162 ? 116.395 116.274 139.898 1.00 29.97  ? 1162 TYR   A CD1 1 
ATOM   10140 C  CD2 . TYR   B 2 1162 ? 118.208 116.180 138.363 1.00 33.71  ? 1162 TYR   A CD2 1 
ATOM   10141 C  CE1 . TYR   B 2 1162 ? 116.898 115.178 140.562 1.00 34.03  ? 1162 TYR   A CE1 1 
ATOM   10142 C  CE2 . TYR   B 2 1162 ? 118.719 115.090 139.023 1.00 31.93  ? 1162 TYR   A CE2 1 
ATOM   10143 C  CZ  . TYR   B 2 1162 ? 118.061 114.591 140.121 1.00 33.64  ? 1162 TYR   A CZ  1 
ATOM   10144 O  OH  . TYR   B 2 1162 ? 118.565 113.497 140.780 1.00 33.53  ? 1162 TYR   A OH  1 
ATOM   10145 N  N   . GLN   B 2 1163 ? 119.277 119.310 138.645 1.00 30.84  ? 1163 GLN   A N   1 
ATOM   10146 C  CA  . GLN   B 2 1163 ? 120.604 119.167 139.229 1.00 25.78  ? 1163 GLN   A CA  1 
ATOM   10147 C  C   . GLN   B 2 1163 ? 120.930 120.329 140.159 1.00 33.95  ? 1163 GLN   A C   1 
ATOM   10148 O  O   . GLN   B 2 1163 ? 121.507 120.123 141.233 1.00 42.15  ? 1163 GLN   A O   1 
ATOM   10149 C  CB  . GLN   B 2 1163 ? 121.647 119.030 138.124 1.00 33.31  ? 1163 GLN   A CB  1 
ATOM   10150 C  CG  . GLN   B 2 1163 ? 121.495 117.753 137.319 1.00 34.50  ? 1163 GLN   A CG  1 
ATOM   10151 C  CD  . GLN   B 2 1163 ? 122.503 117.637 136.201 1.00 40.28  ? 1163 GLN   A CD  1 
ATOM   10152 O  OE1 . GLN   B 2 1163 ? 123.365 118.495 136.040 1.00 42.97  ? 1163 GLN   A OE1 1 
ATOM   10153 N  NE2 . GLN   B 2 1163 ? 122.399 116.571 135.418 1.00 44.62  ? 1163 GLN   A NE2 1 
ATOM   10154 N  N   . SER   B 2 1164 ? 120.559 121.553 139.774 1.00 30.63  ? 1164 SER   A N   1 
ATOM   10155 C  CA  . SER   B 2 1164 ? 120.767 122.694 140.657 1.00 25.24  ? 1164 SER   A CA  1 
ATOM   10156 C  C   . SER   B 2 1164 ? 119.965 122.546 141.941 1.00 30.70  ? 1164 SER   A C   1 
ATOM   10157 O  O   . SER   B 2 1164 ? 120.449 122.887 143.029 1.00 37.64  ? 1164 SER   A O   1 
ATOM   10158 C  CB  . SER   B 2 1164 ? 120.396 123.988 139.935 1.00 29.11  ? 1164 SER   A CB  1 
ATOM   10159 O  OG  . SER   B 2 1164 ? 119.054 123.956 139.485 1.00 37.02  ? 1164 SER   A OG  1 
ATOM   10160 N  N   . ALA   B 2 1165 ? 118.733 122.041 141.836 1.00 34.61  ? 1165 ALA   A N   1 
ATOM   10161 C  CA  . ALA   B 2 1165 ? 117.930 121.804 143.029 1.00 32.43  ? 1165 ALA   A CA  1 
ATOM   10162 C  C   . ALA   B 2 1165 ? 118.610 120.804 143.949 1.00 30.80  ? 1165 ALA   A C   1 
ATOM   10163 O  O   . ALA   B 2 1165 ? 118.698 121.020 145.163 1.00 43.22  ? 1165 ALA   A O   1 
ATOM   10164 C  CB  . ALA   B 2 1165 ? 116.537 121.316 142.634 1.00 35.60  ? 1165 ALA   A CB  1 
ATOM   10165 N  N   . VAL   B 2 1166 ? 119.117 119.708 143.382 1.00 33.38  ? 1166 VAL   A N   1 
ATOM   10166 C  CA  . VAL   B 2 1166 ? 119.804 118.704 144.190 1.00 31.03  ? 1166 VAL   A CA  1 
ATOM   10167 C  C   . VAL   B 2 1166 ? 120.992 119.330 144.908 1.00 31.07  ? 1166 VAL   A C   1 
ATOM   10168 O  O   . VAL   B 2 1166 ? 121.112 119.247 146.140 1.00 41.19  ? 1166 VAL   A O   1 
ATOM   10169 C  CB  . VAL   B 2 1166 ? 120.237 117.515 143.314 1.00 28.14  ? 1166 VAL   A CB  1 
ATOM   10170 C  CG1 . VAL   B 2 1166 ? 121.265 116.674 144.036 1.00 37.42  ? 1166 VAL   A CG1 1 
ATOM   10171 C  CG2 . VAL   B 2 1166 ? 119.038 116.671 142.946 1.00 31.41  ? 1166 VAL   A CG2 1 
ATOM   10172 N  N   . ILE   B 2 1167 ? 121.849 120.021 144.151 1.00 31.27  ? 1167 ILE   A N   1 
ATOM   10173 C  CA  . ILE   B 2 1167 ? 123.026 120.674 144.725 1.00 27.56  ? 1167 ILE   A CA  1 
ATOM   10174 C  C   . ILE   B 2 1167 ? 122.622 121.546 145.904 1.00 32.88  ? 1167 ILE   A C   1 
ATOM   10175 O  O   . ILE   B 2 1167 ? 123.020 121.304 147.057 1.00 48.45  ? 1167 ILE   A O   1 
ATOM   10176 C  CB  . ILE   B 2 1167 ? 123.753 121.509 143.656 1.00 30.91  ? 1167 ILE   A CB  1 
ATOM   10177 C  CG1 . ILE   B 2 1167 ? 124.205 120.633 142.491 1.00 37.27  ? 1167 ILE   A CG1 1 
ATOM   10178 C  CG2 . ILE   B 2 1167 ? 124.928 122.247 144.265 1.00 34.93  ? 1167 ILE   A CG2 1 
ATOM   10179 C  CD1 . ILE   B 2 1167 ? 124.733 121.407 141.316 1.00 35.55  ? 1167 ILE   A CD1 1 
ATOM   10180 N  N   . TYR   B 2 1168 ? 121.803 122.563 145.626 1.00 30.24  ? 1168 TYR   A N   1 
ATOM   10181 C  CA  . TYR   B 2 1168 ? 121.506 123.563 146.642 1.00 35.83  ? 1168 TYR   A CA  1 
ATOM   10182 C  C   . TYR   B 2 1168 ? 120.824 122.943 147.848 1.00 36.23  ? 1168 TYR   A C   1 
ATOM   10183 O  O   . TYR   B 2 1168 ? 121.231 123.186 148.986 1.00 51.78  ? 1168 TYR   A O   1 
ATOM   10184 C  CB  . TYR   B 2 1168 ? 120.637 124.685 146.077 1.00 38.80  ? 1168 TYR   A CB  1 
ATOM   10185 C  CG  . TYR   B 2 1168 ? 120.235 125.658 147.160 1.00 37.46  ? 1168 TYR   A CG  1 
ATOM   10186 C  CD1 . TYR   B 2 1168 ? 121.110 126.643 147.588 1.00 36.08  ? 1168 TYR   A CD1 1 
ATOM   10187 C  CD2 . TYR   B 2 1168 ? 119.002 125.562 147.786 1.00 37.03  ? 1168 TYR   A CD2 1 
ATOM   10188 C  CE1 . TYR   B 2 1168 ? 120.763 127.515 148.591 1.00 32.87  ? 1168 TYR   A CE1 1 
ATOM   10189 C  CE2 . TYR   B 2 1168 ? 118.647 126.431 148.790 1.00 34.15  ? 1168 TYR   A CE2 1 
ATOM   10190 C  CZ  . TYR   B 2 1168 ? 119.529 127.406 149.188 1.00 37.28  ? 1168 TYR   A CZ  1 
ATOM   10191 O  OH  . TYR   B 2 1168 ? 119.172 128.279 150.189 1.00 54.04  ? 1168 TYR   A OH  1 
ATOM   10192 N  N   . PHE   B 2 1169 ? 119.765 122.162 147.628 1.00 27.69  ? 1169 PHE   A N   1 
ATOM   10193 C  CA  . PHE   B 2 1169 ? 118.972 121.690 148.755 1.00 32.24  ? 1169 PHE   A CA  1 
ATOM   10194 C  C   . PHE   B 2 1169 ? 119.759 120.725 149.632 1.00 29.33  ? 1169 PHE   A C   1 
ATOM   10195 O  O   . PHE   B 2 1169 ? 119.732 120.842 150.867 1.00 39.86  ? 1169 PHE   A O   1 
ATOM   10196 C  CB  . PHE   B 2 1169 ? 117.681 121.054 148.248 1.00 29.11  ? 1169 PHE   A CB  1 
ATOM   10197 C  CG  . PHE   B 2 1169 ? 116.681 122.055 147.750 1.00 34.96  ? 1169 PHE   A CG  1 
ATOM   10198 C  CD1 . PHE   B 2 1169 ? 116.376 123.174 148.501 1.00 34.47  ? 1169 PHE   A CD1 1 
ATOM   10199 C  CD2 . PHE   B 2 1169 ? 116.061 121.892 146.526 1.00 33.31  ? 1169 PHE   A CD2 1 
ATOM   10200 C  CE1 . PHE   B 2 1169 ? 115.465 124.101 148.050 1.00 36.62  ? 1169 PHE   A CE1 1 
ATOM   10201 C  CE2 . PHE   B 2 1169 ? 115.149 122.820 146.069 1.00 32.11  ? 1169 PHE   A CE2 1 
ATOM   10202 C  CZ  . PHE   B 2 1169 ? 114.853 123.925 146.833 1.00 33.31  ? 1169 PHE   A CZ  1 
ATOM   10203 N  N   . PHE   B 2 1170 ? 120.477 119.773 149.026 1.00 28.97  ? 1170 PHE   A N   1 
ATOM   10204 C  CA  . PHE   B 2 1170 ? 121.233 118.836 149.846 1.00 27.43  ? 1170 PHE   A CA  1 
ATOM   10205 C  C   . PHE   B 2 1170 ? 122.339 119.542 150.620 1.00 33.77  ? 1170 PHE   A C   1 
ATOM   10206 O  O   . PHE   B 2 1170 ? 122.502 119.305 151.823 1.00 44.74  ? 1170 PHE   A O   1 
ATOM   10207 C  CB  . PHE   B 2 1170 ? 121.790 117.708 148.983 1.00 32.27  ? 1170 PHE   A CB  1 
ATOM   10208 C  CG  . PHE   B 2 1170 ? 120.773 116.660 148.639 1.00 27.08  ? 1170 PHE   A CG  1 
ATOM   10209 C  CD1 . PHE   B 2 1170 ? 120.458 115.664 149.541 1.00 30.09  ? 1170 PHE   A CD1 1 
ATOM   10210 C  CD2 . PHE   B 2 1170 ? 120.119 116.681 147.424 1.00 35.56  ? 1170 PHE   A CD2 1 
ATOM   10211 C  CE1 . PHE   B 2 1170 ? 119.519 114.705 149.233 1.00 35.70  ? 1170 PHE   A CE1 1 
ATOM   10212 C  CE2 . PHE   B 2 1170 ? 119.179 115.723 147.111 1.00 34.81  ? 1170 PHE   A CE2 1 
ATOM   10213 C  CZ  . PHE   B 2 1170 ? 118.880 114.735 148.017 1.00 37.30  ? 1170 PHE   A CZ  1 
ATOM   10214 N  N   . LEU   B 2 1171 ? 123.087 120.441 149.971 1.00 36.42  ? 1171 LEU   A N   1 
ATOM   10215 C  CA  . LEU   B 2 1171 ? 124.153 121.116 150.705 1.00 34.73  ? 1171 LEU   A CA  1 
ATOM   10216 C  C   . LEU   B 2 1171 ? 123.602 122.079 151.753 1.00 42.63  ? 1171 LEU   A C   1 
ATOM   10217 O  O   . LEU   B 2 1171 ? 124.212 122.253 152.815 1.00 54.14  ? 1171 LEU   A O   1 
ATOM   10218 C  CB  . LEU   B 2 1171 ? 125.085 121.828 149.732 1.00 40.32  ? 1171 LEU   A CB  1 
ATOM   10219 C  CG  . LEU   B 2 1171 ? 125.941 120.827 148.957 1.00 41.16  ? 1171 LEU   A CG  1 
ATOM   10220 C  CD1 . LEU   B 2 1171 ? 126.787 121.508 147.908 1.00 44.33  ? 1171 LEU   A CD1 1 
ATOM   10221 C  CD2 . LEU   B 2 1171 ? 126.814 120.041 149.915 1.00 43.35  ? 1171 LEU   A CD2 1 
ATOM   10222 N  N   . ASN   B 2 1172 ? 122.443 122.685 151.494 1.00 40.63  ? 1172 ASN   A N   1 
ATOM   10223 C  CA  . ASN   B 2 1172 ? 121.819 123.566 152.473 1.00 39.25  ? 1172 ASN   A CA  1 
ATOM   10224 C  C   . ASN   B 2 1172 ? 121.423 122.800 153.726 1.00 48.20  ? 1172 ASN   A C   1 
ATOM   10225 O  O   . ASN   B 2 1172 ? 121.789 123.182 154.844 1.00 51.01  ? 1172 ASN   A O   1 
ATOM   10226 C  CB  . ASN   B 2 1172 ? 120.600 124.243 151.846 1.00 39.04  ? 1172 ASN   A CB  1 
ATOM   10227 C  CG  . ASN   B 2 1172 ? 119.767 125.003 152.853 1.00 45.80  ? 1172 ASN   A CG  1 
ATOM   10228 O  OD1 . ASN   B 2 1172 ? 120.284 125.524 153.839 1.00 53.35  ? 1172 ASN   A OD1 1 
ATOM   10229 N  ND2 . ASN   B 2 1172 ? 118.466 125.068 152.610 1.00 42.33  ? 1172 ASN   A ND2 1 
ATOM   10230 N  N   . TYR   B 2 1173 ? 120.680 121.705 153.559 1.00 42.76  ? 1173 TYR   A N   1 
ATOM   10231 C  CA  . TYR   B 2 1173 ? 120.295 120.918 154.722 1.00 32.39  ? 1173 TYR   A CA  1 
ATOM   10232 C  C   . TYR   B 2 1173 ? 121.494 120.253 155.382 1.00 37.71  ? 1173 TYR   A C   1 
ATOM   10233 O  O   . TYR   B 2 1173 ? 121.419 119.901 156.564 1.00 40.19  ? 1173 TYR   A O   1 
ATOM   10234 C  CB  . TYR   B 2 1173 ? 119.249 119.879 154.331 1.00 34.39  ? 1173 TYR   A CB  1 
ATOM   10235 C  CG  . TYR   B 2 1173 ? 117.938 120.484 153.892 1.00 39.20  ? 1173 TYR   A CG  1 
ATOM   10236 C  CD1 . TYR   B 2 1173 ? 117.444 121.629 154.497 1.00 36.49  ? 1173 TYR   A CD1 1 
ATOM   10237 C  CD2 . TYR   B 2 1173 ? 117.200 119.915 152.864 1.00 48.92  ? 1173 TYR   A CD2 1 
ATOM   10238 C  CE1 . TYR   B 2 1173 ? 116.249 122.188 154.098 1.00 38.52  ? 1173 TYR   A CE1 1 
ATOM   10239 C  CE2 . TYR   B 2 1173 ? 116.003 120.467 152.457 1.00 50.87  ? 1173 TYR   A CE2 1 
ATOM   10240 C  CZ  . TYR   B 2 1173 ? 115.532 121.605 153.078 1.00 47.89  ? 1173 TYR   A CZ  1 
ATOM   10241 O  OH  . TYR   B 2 1173 ? 114.339 122.161 152.678 1.00 45.57  ? 1173 TYR   A OH  1 
ATOM   10242 N  N   . THR   B 2 1174 ? 122.597 120.075 154.651 1.00 42.35  ? 1174 THR   A N   1 
ATOM   10243 C  CA  . THR   B 2 1174 ? 123.833 119.633 155.286 1.00 39.18  ? 1174 THR   A CA  1 
ATOM   10244 C  C   . THR   B 2 1174 ? 124.407 120.717 156.190 1.00 40.02  ? 1174 THR   A C   1 
ATOM   10245 O  O   . THR   B 2 1174 ? 124.833 120.434 157.315 1.00 42.96  ? 1174 THR   A O   1 
ATOM   10246 C  CB  . THR   B 2 1174 ? 124.853 119.234 154.220 1.00 43.37  ? 1174 THR   A CB  1 
ATOM   10247 O  OG1 . THR   B 2 1174 ? 124.356 118.114 153.478 1.00 49.98  ? 1174 THR   A OG1 1 
ATOM   10248 C  CG2 . THR   B 2 1174 ? 126.177 118.866 154.859 1.00 40.17  ? 1174 THR   A CG2 1 
ATOM   10249 N  N   . TYR   B 2 1175 ? 124.418 121.961 155.720 1.00 49.90  ? 1175 TYR   A N   1 
ATOM   10250 C  CA  . TYR   B 2 1175 ? 125.003 123.063 156.472 1.00 37.63  ? 1175 TYR   A CA  1 
ATOM   10251 C  C   . TYR   B 2 1175 ? 124.044 123.688 157.474 1.00 45.15  ? 1175 TYR   A C   1 
ATOM   10252 O  O   . TYR   B 2 1175 ? 124.423 124.652 158.146 1.00 51.73  ? 1175 TYR   A O   1 
ATOM   10253 C  CB  . TYR   B 2 1175 ? 125.522 124.141 155.518 1.00 41.15  ? 1175 TYR   A CB  1 
ATOM   10254 C  CG  . TYR   B 2 1175 ? 126.903 123.858 154.980 1.00 44.18  ? 1175 TYR   A CG  1 
ATOM   10255 C  CD1 . TYR   B 2 1175 ? 128.031 124.158 155.725 1.00 44.61  ? 1175 TYR   A CD1 1 
ATOM   10256 C  CD2 . TYR   B 2 1175 ? 127.079 123.297 153.725 1.00 47.14  ? 1175 TYR   A CD2 1 
ATOM   10257 C  CE1 . TYR   B 2 1175 ? 129.290 123.905 155.241 1.00 48.73  ? 1175 TYR   A CE1 1 
ATOM   10258 C  CE2 . TYR   B 2 1175 ? 128.336 123.041 153.232 1.00 46.25  ? 1175 TYR   A CE2 1 
ATOM   10259 C  CZ  . TYR   B 2 1175 ? 129.437 123.348 153.993 1.00 50.91  ? 1175 TYR   A CZ  1 
ATOM   10260 O  OH  . TYR   B 2 1175 ? 130.695 123.093 153.503 1.00 58.42  ? 1175 TYR   A OH  1 
ATOM   10261 N  N   . VAL   B 2 1176 ? 122.821 123.176 157.600 1.00 48.97  ? 1176 VAL   A N   1 
ATOM   10262 C  CA  . VAL   B 2 1176 ? 121.961 123.617 158.693 1.00 33.19  ? 1176 VAL   A CA  1 
ATOM   10263 C  C   . VAL   B 2 1176 ? 122.457 122.933 159.957 1.00 40.75  ? 1176 VAL   A C   1 
ATOM   10264 O  O   . VAL   B 2 1176 ? 121.999 121.843 160.316 1.00 51.02  ? 1176 VAL   A O   1 
ATOM   10265 C  CB  . VAL   B 2 1176 ? 120.476 123.306 158.431 1.00 36.50  ? 1176 VAL   A CB  1 
ATOM   10266 C  CG1 . VAL   B 2 1176 ? 119.633 123.677 159.635 1.00 36.25  ? 1176 VAL   A CG1 1 
ATOM   10267 C  CG2 . VAL   B 2 1176 ? 119.987 124.063 157.218 1.00 45.70  ? 1176 VAL   A CG2 1 
ATOM   10268 N  N   . THR   B 2 1177 ? 123.411 123.566 160.629 1.00 44.17  ? 1177 THR   A N   1 
ATOM   10269 C  CA  . THR   B 2 1177 ? 124.056 122.997 161.802 1.00 44.37  ? 1177 THR   A CA  1 
ATOM   10270 C  C   . THR   B 2 1177 ? 124.675 124.142 162.597 1.00 44.70  ? 1177 THR   A C   1 
ATOM   10271 O  O   . THR   B 2 1177 ? 124.410 125.317 162.320 1.00 53.12  ? 1177 THR   A O   1 
ATOM   10272 C  CB  . THR   B 2 1177 ? 125.088 121.935 161.389 1.00 47.12  ? 1177 THR   A CB  1 
ATOM   10273 O  OG1 . THR   B 2 1177 ? 125.714 121.392 162.557 1.00 54.25  ? 1177 THR   A OG1 1 
ATOM   10274 C  CG2 . THR   B 2 1177 ? 126.148 122.544 160.492 1.00 46.60  ? 1177 THR   A CG2 1 
ATOM   10275 N  N   . THR   B 2 1178 ? 125.504 123.801 163.580 1.00 37.36  ? 1178 THR   A N   1 
ATOM   10276 C  CA  . THR   B 2 1178 ? 126.152 124.787 164.432 1.00 32.70  ? 1178 THR   A CA  1 
ATOM   10277 C  C   . THR   B 2 1178 ? 127.545 125.163 163.945 1.00 49.73  ? 1178 THR   A C   1 
ATOM   10278 O  O   . THR   B 2 1178 ? 127.872 126.351 163.872 1.00 52.91  ? 1178 THR   A O   1 
ATOM   10279 C  CB  . THR   B 2 1178 ? 126.227 124.268 165.872 1.00 37.33  ? 1178 THR   A CB  1 
ATOM   10280 O  OG1 . THR   B 2 1178 ? 126.803 122.957 165.880 1.00 51.38  ? 1178 THR   A OG1 1 
ATOM   10281 C  CG2 . THR   B 2 1178 ? 124.846 124.208 166.484 1.00 37.38  ? 1178 THR   A CG2 1 
ATOM   10282 N  N   . THR   B 2 1179 ? 128.373 124.184 163.609 1.00 43.93  ? 1179 THR   A N   1 
ATOM   10283 C  CA  . THR   B 2 1179 ? 129.764 124.504 163.315 1.00 33.06  ? 1179 THR   A CA  1 
ATOM   10284 C  C   . THR   B 2 1179 ? 130.280 123.928 162.005 1.00 41.60  ? 1179 THR   A C   1 
ATOM   10285 O  O   . THR   B 2 1179 ? 131.064 124.595 161.325 1.00 50.49  ? 1179 THR   A O   1 
ATOM   10286 C  CB  . THR   B 2 1179 ? 130.654 124.029 164.468 1.00 37.90  ? 1179 THR   A CB  1 
ATOM   10287 O  OG1 . THR   B 2 1179 ? 131.993 123.843 163.995 1.00 52.45  ? 1179 THR   A OG1 1 
ATOM   10288 C  CG2 . THR   B 2 1179 ? 130.132 122.726 165.043 1.00 41.04  ? 1179 THR   A CG2 1 
ATOM   10289 N  N   . ALA   B 2 1180 ? 129.881 122.708 161.646 1.00 39.82  ? 1180 ALA   A N   1 
ATOM   10290 C  CA  . ALA   B 2 1180 ? 130.346 121.956 160.481 1.00 41.31  ? 1180 ALA   A CA  1 
ATOM   10291 C  C   . ALA   B 2 1180 ? 131.808 121.532 160.585 1.00 43.21  ? 1180 ALA   A C   1 
ATOM   10292 O  O   . ALA   B 2 1180 ? 132.313 120.884 159.664 1.00 49.59  ? 1180 ALA   A O   1 
ATOM   10293 C  CB  . ALA   B 2 1180 ? 130.145 122.716 159.161 1.00 38.03  ? 1180 ALA   A CB  1 
ATOM   10294 N  N   . ARG   B 2 1181 ? 132.501 121.871 161.669 1.00 40.79  ? 1181 ARG   A N   1 
ATOM   10295 C  CA  . ARG   B 2 1181 ? 133.843 121.375 161.936 1.00 35.78  ? 1181 ARG   A CA  1 
ATOM   10296 C  C   . ARG   B 2 1181 ? 134.002 121.207 163.438 1.00 41.78  ? 1181 ARG   A C   1 
ATOM   10297 O  O   . ARG   B 2 1181 ? 133.125 121.576 164.222 1.00 56.32  ? 1181 ARG   A O   1 
ATOM   10298 C  CB  . ARG   B 2 1181 ? 134.927 122.311 161.399 1.00 45.04  ? 1181 ARG   A CB  1 
ATOM   10299 C  CG  . ARG   B 2 1181 ? 135.129 122.281 159.901 1.00 46.45  ? 1181 ARG   A CG  1 
ATOM   10300 C  CD  . ARG   B 2 1181 ? 136.010 123.436 159.475 1.00 40.19  ? 1181 ARG   A CD  1 
ATOM   10301 N  NE  . ARG   B 2 1181 ? 135.643 124.657 160.179 1.00 40.81  ? 1181 ARG   A NE  1 
ATOM   10302 C  CZ  . ARG   B 2 1181 ? 134.588 125.403 159.884 1.00 43.99  ? 1181 ARG   A CZ  1 
ATOM   10303 N  NH1 . ARG   B 2 1181 ? 133.776 125.089 158.890 1.00 49.04  ? 1181 ARG   A NH1 1 
ATOM   10304 N  NH2 . ARG   B 2 1181 ? 134.340 126.490 160.609 1.00 47.55  ? 1181 ARG   A NH2 1 
ATOM   10305 N  N   . GLY   B 2 1182 ? 135.142 120.650 163.835 1.00 42.25  ? 1182 GLY   A N   1 
ATOM   10306 C  CA  . GLY   B 2 1182 ? 135.428 120.476 165.245 1.00 39.50  ? 1182 GLY   A CA  1 
ATOM   10307 C  C   . GLY   B 2 1182 ? 135.947 121.706 165.952 1.00 46.04  ? 1182 GLY   A C   1 
ATOM   10308 O  O   . GLY   B 2 1182 ? 136.142 121.666 167.170 1.00 50.59  ? 1182 GLY   A O   1 
ATOM   10309 N  N   . ASP   B 2 1183 ? 136.179 122.796 165.223 1.00 44.86  ? 1183 ASP   A N   1 
ATOM   10310 C  CA  . ASP   B 2 1183 ? 136.677 124.029 165.814 1.00 41.94  ? 1183 ASP   A CA  1 
ATOM   10311 C  C   . ASP   B 2 1183 ? 135.572 124.923 166.362 1.00 50.02  ? 1183 ASP   A C   1 
ATOM   10312 O  O   . ASP   B 2 1183 ? 135.875 125.895 167.062 1.00 59.50  ? 1183 ASP   A O   1 
ATOM   10313 C  CB  . ASP   B 2 1183 ? 137.510 124.804 164.788 1.00 46.00  ? 1183 ASP   A CB  1 
ATOM   10314 C  CG  . ASP   B 2 1183 ? 136.808 124.951 163.453 1.00 59.71  ? 1183 ASP   A CG  1 
ATOM   10315 O  OD1 . ASP   B 2 1183 ? 135.589 124.690 163.384 1.00 60.40  ? 1183 ASP   A OD1 1 
ATOM   10316 O  OD2 . ASP   B 2 1183 ? 137.480 125.321 162.468 1.00 61.30  ? 1183 ASP   A OD2 1 
ATOM   10317 N  N   . GLY   B 2 1184 ? 134.311 124.626 166.064 1.00 38.29  ? 1184 GLY   A N   1 
ATOM   10318 C  CA  . GLY   B 2 1184 ? 133.197 125.358 166.624 1.00 34.89  ? 1184 GLY   A CA  1 
ATOM   10319 C  C   . GLY   B 2 1184 ? 132.803 126.618 165.889 1.00 36.63  ? 1184 GLY   A C   1 
ATOM   10320 O  O   . GLY   B 2 1184 ? 131.809 127.248 166.270 1.00 50.50  ? 1184 GLY   A O   1 
ATOM   10321 N  N   . TYR   B 2 1185 ? 133.537 127.006 164.853 1.00 37.86  ? 1185 TYR   A N   1 
ATOM   10322 C  CA  . TYR   B 2 1185 ? 133.240 128.241 164.147 1.00 39.95  ? 1185 TYR   A CA  1 
ATOM   10323 C  C   . TYR   B 2 1185 ? 131.932 128.118 163.378 1.00 42.79  ? 1185 TYR   A C   1 
ATOM   10324 O  O   . TYR   B 2 1185 ? 131.597 127.062 162.838 1.00 52.18  ? 1185 TYR   A O   1 
ATOM   10325 C  CB  . TYR   B 2 1185 ? 134.385 128.597 163.203 1.00 41.35  ? 1185 TYR   A CB  1 
ATOM   10326 C  CG  . TYR   B 2 1185 ? 135.716 128.725 163.902 1.00 43.46  ? 1185 TYR   A CG  1 
ATOM   10327 C  CD1 . TYR   B 2 1185 ? 135.797 129.228 165.190 1.00 42.84  ? 1185 TYR   A CD1 1 
ATOM   10328 C  CD2 . TYR   B 2 1185 ? 136.890 128.332 163.280 1.00 46.28  ? 1185 TYR   A CD2 1 
ATOM   10329 C  CE1 . TYR   B 2 1185 ? 137.006 129.343 165.835 1.00 40.71  ? 1185 TYR   A CE1 1 
ATOM   10330 C  CE2 . TYR   B 2 1185 ? 138.106 128.442 163.920 1.00 45.33  ? 1185 TYR   A CE2 1 
ATOM   10331 C  CZ  . TYR   B 2 1185 ? 138.157 128.950 165.197 1.00 41.93  ? 1185 TYR   A CZ  1 
ATOM   10332 O  OH  . TYR   B 2 1185 ? 139.365 129.065 165.841 1.00 48.36  ? 1185 TYR   A OH  1 
ATOM   10333 N  N   . ASP   B 2 1186 ? 131.194 129.221 163.328 1.00 46.18  ? 1186 ASP   A N   1 
ATOM   10334 C  CA  . ASP   B 2 1186 ? 129.851 129.218 162.777 1.00 43.99  ? 1186 ASP   A CA  1 
ATOM   10335 C  C   . ASP   B 2 1186 ? 129.881 129.024 161.265 1.00 51.57  ? 1186 ASP   A C   1 
ATOM   10336 O  O   . ASP   B 2 1186 ? 130.899 129.226 160.597 1.00 55.12  ? 1186 ASP   A O   1 
ATOM   10337 C  CB  . ASP   B 2 1186 ? 129.137 130.521 163.120 1.00 51.63  ? 1186 ASP   A CB  1 
ATOM   10338 C  CG  . ASP   B 2 1186 ? 129.236 130.862 164.586 1.00 59.66  ? 1186 ASP   A CG  1 
ATOM   10339 O  OD1 . ASP   B 2 1186 ? 129.005 129.963 165.421 1.00 63.48  ? 1186 ASP   A OD1 1 
ATOM   10340 O  OD2 . ASP   B 2 1186 ? 129.553 132.026 164.908 1.00 54.92  ? 1186 ASP   A OD2 1 
ATOM   10341 N  N   . VAL   B 2 1187 ? 128.735 128.624 160.729 1.00 50.82  ? 1187 VAL   A N   1 
ATOM   10342 C  CA  . VAL   B 2 1187 ? 128.551 128.429 159.298 1.00 47.22  ? 1187 VAL   A CA  1 
ATOM   10343 C  C   . VAL   B 2 1187 ? 127.976 129.710 158.718 1.00 52.38  ? 1187 VAL   A C   1 
ATOM   10344 O  O   . VAL   B 2 1187 ? 126.794 130.015 158.917 1.00 57.22  ? 1187 VAL   A O   1 
ATOM   10345 C  CB  . VAL   B 2 1187 ? 127.631 127.234 159.008 1.00 49.35  ? 1187 VAL   A CB  1 
ATOM   10346 C  CG1 . VAL   B 2 1187 ? 127.381 127.113 157.518 1.00 49.89  ? 1187 VAL   A CG1 1 
ATOM   10347 C  CG2 . VAL   B 2 1187 ? 128.234 125.956 159.557 1.00 55.18  ? 1187 VAL   A CG2 1 
ATOM   10348 N  N   . TYR   B 2 1188 ? 128.802 130.465 158.006 1.00 52.33  ? 1188 TYR   A N   1 
ATOM   10349 C  CA  . TYR   B 2 1188 ? 128.345 131.659 157.315 1.00 45.34  ? 1188 TYR   A CA  1 
ATOM   10350 C  C   . TYR   B 2 1188 ? 128.043 131.315 155.860 1.00 51.17  ? 1188 TYR   A C   1 
ATOM   10351 O  O   . TYR   B 2 1188 ? 128.278 130.196 155.399 1.00 56.85  ? 1188 TYR   A O   1 
ATOM   10352 C  CB  . TYR   B 2 1188 ? 129.365 132.794 157.450 1.00 45.58  ? 1188 TYR   A CB  1 
ATOM   10353 C  CG  . TYR   B 2 1188 ? 130.656 132.630 156.687 1.00 48.02  ? 1188 TYR   A CG  1 
ATOM   10354 C  CD1 . TYR   B 2 1188 ? 131.591 131.676 157.055 1.00 50.57  ? 1188 TYR   A CD1 1 
ATOM   10355 C  CD2 . TYR   B 2 1188 ? 130.960 133.466 155.625 1.00 50.47  ? 1188 TYR   A CD2 1 
ATOM   10356 C  CE1 . TYR   B 2 1188 ? 132.778 131.544 156.369 1.00 51.12  ? 1188 TYR   A CE1 1 
ATOM   10357 C  CE2 . TYR   B 2 1188 ? 132.143 133.340 154.936 1.00 49.49  ? 1188 TYR   A CE2 1 
ATOM   10358 C  CZ  . TYR   B 2 1188 ? 133.047 132.376 155.308 1.00 52.32  ? 1188 TYR   A CZ  1 
ATOM   10359 O  OH  . TYR   B 2 1188 ? 134.229 132.249 154.618 1.00 61.53  ? 1188 TYR   A OH  1 
ATOM   10360 N  N   . MET   B 2 1189 ? 127.508 132.300 155.138 1.00 52.89  ? 1189 MET   A N   1 
ATOM   10361 C  CA  . MET   B 2 1189 ? 126.900 132.026 153.840 1.00 47.31  ? 1189 MET   A CA  1 
ATOM   10362 C  C   . MET   B 2 1189 ? 127.915 131.489 152.840 1.00 51.47  ? 1189 MET   A C   1 
ATOM   10363 O  O   . MET   B 2 1189 ? 127.602 130.588 152.052 1.00 59.26  ? 1189 MET   A O   1 
ATOM   10364 C  CB  . MET   B 2 1189 ? 126.232 133.291 153.300 1.00 52.13  ? 1189 MET   A CB  1 
ATOM   10365 C  CG  . MET   B 2 1189 ? 125.458 133.087 152.010 1.00 53.35  ? 1189 MET   A CG  1 
ATOM   10366 S  SD  . MET   B 2 1189 ? 124.507 134.541 151.531 1.00 64.18  ? 1189 MET   A SD  1 
ATOM   10367 C  CE  . MET   B 2 1189 ? 125.809 135.759 151.377 1.00 57.80  ? 1189 MET   A CE  1 
ATOM   10368 N  N   . TYR   B 2 1190 ? 129.136 132.020 152.856 1.00 49.35  ? 1190 TYR   A N   1 
ATOM   10369 C  CA  . TYR   B 2 1190 ? 130.078 131.714 151.789 1.00 47.37  ? 1190 TYR   A CA  1 
ATOM   10370 C  C   . TYR   B 2 1190 ? 130.692 130.323 151.894 1.00 49.47  ? 1190 TYR   A C   1 
ATOM   10371 O  O   . TYR   B 2 1190 ? 131.137 129.798 150.874 1.00 58.15  ? 1190 TYR   A O   1 
ATOM   10372 C  CB  . TYR   B 2 1190 ? 131.176 132.776 151.735 1.00 49.25  ? 1190 TYR   A CB  1 
ATOM   10373 C  CG  . TYR   B 2 1190 ? 130.695 134.093 151.169 1.00 48.38  ? 1190 TYR   A CG  1 
ATOM   10374 C  CD1 . TYR   B 2 1190 ? 129.547 134.156 150.395 1.00 44.73  ? 1190 TYR   A CD1 1 
ATOM   10375 C  CD2 . TYR   B 2 1190 ? 131.387 135.270 151.408 1.00 50.96  ? 1190 TYR   A CD2 1 
ATOM   10376 C  CE1 . TYR   B 2 1190 ? 129.101 135.350 149.873 1.00 42.94  ? 1190 TYR   A CE1 1 
ATOM   10377 C  CE2 . TYR   B 2 1190 ? 130.947 136.471 150.888 1.00 54.47  ? 1190 TYR   A CE2 1 
ATOM   10378 C  CZ  . TYR   B 2 1190 ? 129.802 136.503 150.122 1.00 50.64  ? 1190 TYR   A CZ  1 
ATOM   10379 O  OH  . TYR   B 2 1190 ? 129.355 137.694 149.601 1.00 54.66  ? 1190 TYR   A OH  1 
ATOM   10380 N  N   . GLU   B 2 1191 ? 130.701 129.694 153.072 1.00 46.71  ? 1191 GLU   A N   1 
ATOM   10381 C  CA  . GLU   B 2 1191 ? 131.114 128.292 153.138 1.00 51.92  ? 1191 GLU   A CA  1 
ATOM   10382 C  C   . GLU   B 2 1191 ? 130.189 127.414 152.304 1.00 58.68  ? 1191 GLU   A C   1 
ATOM   10383 O  O   . GLU   B 2 1191 ? 130.634 126.679 151.408 1.00 65.00  ? 1191 GLU   A O   1 
ATOM   10384 C  CB  . GLU   B 2 1191 ? 131.123 127.807 154.585 1.00 51.30  ? 1191 GLU   A CB  1 
ATOM   10385 C  CG  . GLU   B 2 1191 ? 132.266 128.315 155.427 1.00 60.98  ? 1191 GLU   A CG  1 
ATOM   10386 C  CD  . GLU   B 2 1191 ? 132.205 127.787 156.845 1.00 65.33  ? 1191 GLU   A CD  1 
ATOM   10387 O  OE1 . GLU   B 2 1191 ? 131.572 126.733 157.058 1.00 62.52  ? 1191 GLU   A OE1 1 
ATOM   10388 O  OE2 . GLU   B 2 1191 ? 132.784 128.428 157.748 1.00 64.66  ? 1191 GLU   A OE2 1 
ATOM   10389 N  N   . MET   B 2 1192 ? 128.887 127.498 152.582 1.00 42.65  ? 1192 MET   A N   1 
ATOM   10390 C  CA  . MET   B 2 1192 ? 127.905 126.747 151.814 1.00 41.10  ? 1192 MET   A CA  1 
ATOM   10391 C  C   . MET   B 2 1192 ? 127.920 127.176 150.357 1.00 50.06  ? 1192 MET   A C   1 
ATOM   10392 O  O   . MET   B 2 1192 ? 127.787 126.343 149.454 1.00 60.59  ? 1192 MET   A O   1 
ATOM   10393 C  CB  . MET   B 2 1192 ? 126.519 126.948 152.423 1.00 46.55  ? 1192 MET   A CB  1 
ATOM   10394 C  CG  . MET   B 2 1192 ? 125.429 126.099 151.811 1.00 55.34  ? 1192 MET   A CG  1 
ATOM   10395 S  SD  . MET   B 2 1192 ? 123.796 126.624 152.359 1.00 63.51  ? 1192 MET   A SD  1 
ATOM   10396 C  CE  . MET   B 2 1192 ? 123.687 128.239 151.597 1.00 52.66  ? 1192 MET   A CE  1 
ATOM   10397 N  N   . SER   B 2 1193 ? 128.092 128.475 150.111 1.00 44.55  ? 1193 SER   A N   1 
ATOM   10398 C  CA  . SER   B 2 1193 ? 128.120 128.979 148.745 1.00 44.80  ? 1193 SER   A CA  1 
ATOM   10399 C  C   . SER   B 2 1193 ? 129.272 128.379 147.952 1.00 50.83  ? 1193 SER   A C   1 
ATOM   10400 O  O   . SER   B 2 1193 ? 129.094 127.972 146.802 1.00 59.33  ? 1193 SER   A O   1 
ATOM   10401 C  CB  . SER   B 2 1193 ? 128.225 130.500 148.759 1.00 52.30  ? 1193 SER   A CB  1 
ATOM   10402 O  OG  . SER   B 2 1193 ? 127.268 131.069 149.634 1.00 62.42  ? 1193 SER   A OG  1 
ATOM   10403 N  N   . THR   B 2 1194 ? 130.464 128.318 148.547 1.00 43.96  ? 1194 THR   A N   1 
ATOM   10404 C  CA  . THR   B 2 1194 ? 131.619 127.793 147.832 1.00 41.75  ? 1194 THR   A CA  1 
ATOM   10405 C  C   . THR   B 2 1194 ? 131.507 126.288 147.640 1.00 47.63  ? 1194 THR   A C   1 
ATOM   10406 O  O   . THR   B 2 1194 ? 131.889 125.763 146.586 1.00 59.47  ? 1194 THR   A O   1 
ATOM   10407 C  CB  . THR   B 2 1194 ? 132.903 128.153 148.573 1.00 43.55  ? 1194 THR   A CB  1 
ATOM   10408 O  OG1 . THR   B 2 1194 ? 132.857 129.529 148.964 1.00 49.49  ? 1194 THR   A OG1 1 
ATOM   10409 C  CG2 . THR   B 2 1194 ? 134.108 127.937 147.675 1.00 47.41  ? 1194 THR   A CG2 1 
ATOM   10410 N  N   . THR   B 2 1195 ? 130.975 125.575 148.638 1.00 40.81  ? 1195 THR   A N   1 
ATOM   10411 C  CA  . THR   B 2 1195 ? 130.737 124.147 148.450 1.00 41.69  ? 1195 THR   A CA  1 
ATOM   10412 C  C   . THR   B 2 1195 ? 129.763 123.904 147.303 1.00 43.40  ? 1195 THR   A C   1 
ATOM   10413 O  O   . THR   B 2 1195 ? 130.001 123.045 146.442 1.00 54.74  ? 1195 THR   A O   1 
ATOM   10414 C  CB  . THR   B 2 1195 ? 130.216 123.522 149.743 1.00 42.83  ? 1195 THR   A CB  1 
ATOM   10415 O  OG1 . THR   B 2 1195 ? 131.171 123.723 150.791 1.00 49.86  ? 1195 THR   A OG1 1 
ATOM   10416 C  CG2 . THR   B 2 1195 ? 129.996 122.036 149.561 1.00 45.58  ? 1195 THR   A CG2 1 
ATOM   10417 N  N   . GLN   B 2 1196 ? 128.676 124.678 147.255 1.00 38.65  ? 1196 GLN   A N   1 
ATOM   10418 C  CA  . GLN   B 2 1196 ? 127.703 124.538 146.178 1.00 38.76  ? 1196 GLN   A CA  1 
ATOM   10419 C  C   . GLN   B 2 1196 ? 128.302 124.914 144.830 1.00 45.71  ? 1196 GLN   A C   1 
ATOM   10420 O  O   . GLN   B 2 1196 ? 128.001 124.280 143.816 1.00 54.25  ? 1196 GLN   A O   1 
ATOM   10421 C  CB  . GLN   B 2 1196 ? 126.471 125.390 146.476 1.00 39.45  ? 1196 GLN   A CB  1 
ATOM   10422 C  CG  . GLN   B 2 1196 ? 125.660 124.894 147.654 1.00 35.43  ? 1196 GLN   A CG  1 
ATOM   10423 C  CD  . GLN   B 2 1196 ? 124.577 125.857 148.071 1.00 42.06  ? 1196 GLN   A CD  1 
ATOM   10424 O  OE1 . GLN   B 2 1196 ? 124.478 126.963 147.545 1.00 48.84  ? 1196 GLN   A OE1 1 
ATOM   10425 N  NE2 . GLN   B 2 1196 ? 123.755 125.443 149.024 1.00 42.84  ? 1196 GLN   A NE2 1 
ATOM   10426 N  N   . ALA   B 2 1197 ? 129.142 125.949 144.794 1.00 34.28  ? 1197 ALA   A N   1 
ATOM   10427 C  CA  . ALA   B 2 1197 ? 129.756 126.362 143.536 1.00 33.65  ? 1197 ALA   A CA  1 
ATOM   10428 C  C   . ALA   B 2 1197 ? 130.699 125.294 143.003 1.00 44.37  ? 1197 ALA   A C   1 
ATOM   10429 O  O   . ALA   B 2 1197 ? 130.696 124.994 141.802 1.00 51.00  ? 1197 ALA   A O   1 
ATOM   10430 C  CB  . ALA   B 2 1197 ? 130.494 127.685 143.723 1.00 36.46  ? 1197 ALA   A CB  1 
ATOM   10431 N  N   . ILE   B 2 1198 ? 131.516 124.708 143.880 1.00 33.10  ? 1198 ILE   A N   1 
ATOM   10432 C  CA  . ILE   B 2 1198 ? 132.417 123.644 143.449 1.00 23.45  ? 1198 ILE   A CA  1 
ATOM   10433 C  C   . ILE   B 2 1198 ? 131.623 122.435 142.976 1.00 32.17  ? 1198 ILE   A C   1 
ATOM   10434 O  O   . ILE   B 2 1198 ? 131.939 121.831 141.940 1.00 43.97  ? 1198 ILE   A O   1 
ATOM   10435 C  CB  . ILE   B 2 1198 ? 133.397 123.284 144.579 1.00 33.93  ? 1198 ILE   A CB  1 
ATOM   10436 C  CG1 . ILE   B 2 1198 ? 134.347 124.455 144.834 1.00 40.43  ? 1198 ILE   A CG1 1 
ATOM   10437 C  CG2 . ILE   B 2 1198 ? 134.174 122.032 144.230 1.00 39.76  ? 1198 ILE   A CG2 1 
ATOM   10438 C  CD1 . ILE   B 2 1198 ? 135.372 124.198 145.900 1.00 41.31  ? 1198 ILE   A CD1 1 
ATOM   10439 N  N   . GLY   B 2 1199 ? 130.571 122.073 143.714 1.00 33.99  ? 1199 GLY   A N   1 
ATOM   10440 C  CA  . GLY   B 2 1199 ? 129.724 120.978 143.276 1.00 36.04  ? 1199 GLY   A CA  1 
ATOM   10441 C  C   . GLY   B 2 1199 ? 129.080 121.242 141.929 1.00 39.08  ? 1199 GLY   A C   1 
ATOM   10442 O  O   . GLY   B 2 1199 ? 129.018 120.355 141.079 1.00 51.96  ? 1199 GLY   A O   1 
ATOM   10443 N  N   . ALA   B 2 1200 ? 128.601 122.468 141.715 1.00 29.95  ? 1200 ALA   A N   1 
ATOM   10444 C  CA  . ALA   B 2 1200 ? 127.962 122.817 140.452 1.00 34.72  ? 1200 ALA   A CA  1 
ATOM   10445 C  C   . ALA   B 2 1200 ? 128.948 122.769 139.294 1.00 37.91  ? 1200 ALA   A C   1 
ATOM   10446 O  O   . ALA   B 2 1200 ? 128.610 122.286 138.208 1.00 46.46  ? 1200 ALA   A O   1 
ATOM   10447 C  CB  . ALA   B 2 1200 ? 127.323 124.200 140.557 1.00 33.37  ? 1200 ALA   A CB  1 
ATOM   10448 N  N   . VAL   B 2 1201 ? 130.167 123.272 139.500 1.00 33.20  ? 1201 VAL   A N   1 
ATOM   10449 C  CA  . VAL   B 2 1201 ? 131.175 123.218 138.444 1.00 32.94  ? 1201 VAL   A CA  1 
ATOM   10450 C  C   . VAL   B 2 1201 ? 131.512 121.773 138.104 1.00 38.29  ? 1201 VAL   A C   1 
ATOM   10451 O  O   . VAL   B 2 1201 ? 131.580 121.394 136.924 1.00 49.63  ? 1201 VAL   A O   1 
ATOM   10452 C  CB  . VAL   B 2 1201 ? 132.424 124.018 138.857 1.00 35.74  ? 1201 VAL   A CB  1 
ATOM   10453 C  CG1 . VAL   B 2 1201 ? 133.590 123.697 137.948 1.00 45.16  ? 1201 VAL   A CG1 1 
ATOM   10454 C  CG2 . VAL   B 2 1201 ? 132.125 125.497 138.814 1.00 37.52  ? 1201 VAL   A CG2 1 
ATOM   10455 N  N   . MET   B 2 1202 ? 131.706 120.937 139.129 1.00 35.84  ? 1202 MET   A N   1 
ATOM   10456 C  CA  . MET   B 2 1202 ? 131.978 119.523 138.891 1.00 32.23  ? 1202 MET   A CA  1 
ATOM   10457 C  C   . MET   B 2 1202 ? 130.837 118.864 138.127 1.00 39.46  ? 1202 MET   A C   1 
ATOM   10458 O  O   . MET   B 2 1202 ? 131.065 118.126 137.159 1.00 47.61  ? 1202 MET   A O   1 
ATOM   10459 C  CB  . MET   B 2 1202 ? 132.216 118.807 140.220 1.00 36.24  ? 1202 MET   A CB  1 
ATOM   10460 C  CG  . MET   B 2 1202 ? 133.593 119.012 140.816 1.00 46.05  ? 1202 MET   A CG  1 
ATOM   10461 S  SD  . MET   B 2 1202 ? 134.840 118.016 139.987 1.00 64.42  ? 1202 MET   A SD  1 
ATOM   10462 C  CE  . MET   B 2 1202 ? 134.044 116.413 139.999 1.00 47.04  ? 1202 MET   A CE  1 
ATOM   10463 N  N   . VAL   B 2 1203 ? 129.596 119.132 138.541 1.00 31.72  ? 1203 VAL   A N   1 
ATOM   10464 C  CA  . VAL   B 2 1203 ? 128.438 118.508 137.907 1.00 27.37  ? 1203 VAL   A CA  1 
ATOM   10465 C  C   . VAL   B 2 1203 ? 128.326 118.937 136.453 1.00 35.83  ? 1203 VAL   A C   1 
ATOM   10466 O  O   . VAL   B 2 1203 ? 128.094 118.109 135.567 1.00 47.82  ? 1203 VAL   A O   1 
ATOM   10467 C  CB  . VAL   B 2 1203 ? 127.155 118.836 138.693 1.00 36.70  ? 1203 VAL   A CB  1 
ATOM   10468 C  CG1 . VAL   B 2 1203 ? 125.932 118.461 137.890 1.00 39.60  ? 1203 VAL   A CG1 1 
ATOM   10469 C  CG2 . VAL   B 2 1203 ? 127.145 118.103 140.013 1.00 41.57  ? 1203 VAL   A CG2 1 
ATOM   10470 N  N   . ALA   B 2 1204 ? 128.491 120.233 136.181 1.00 31.96  ? 1204 ALA   A N   1 
ATOM   10471 C  CA  . ALA   B 2 1204 ? 128.364 120.724 134.813 1.00 33.37  ? 1204 ALA   A CA  1 
ATOM   10472 C  C   . ALA   B 2 1204 ? 129.441 120.132 133.912 1.00 36.92  ? 1204 ALA   A C   1 
ATOM   10473 O  O   . ALA   B 2 1204 ? 129.154 119.674 132.797 1.00 41.63  ? 1204 ALA   A O   1 
ATOM   10474 C  CB  . ALA   B 2 1204 ? 128.426 122.250 134.801 1.00 34.23  ? 1204 ALA   A CB  1 
ATOM   10475 N  N   . ASN   B 2 1205 ? 130.690 120.122 134.384 1.00 39.41  ? 1205 ASN   A N   1 
ATOM   10476 C  CA  . ASN   B 2 1205 ? 131.772 119.596 133.558 1.00 32.53  ? 1205 ASN   A CA  1 
ATOM   10477 C  C   . ASN   B 2 1205 ? 131.608 118.102 133.310 1.00 35.49  ? 1205 ASN   A C   1 
ATOM   10478 O  O   . ASN   B 2 1205 ? 131.821 117.627 132.189 1.00 44.00  ? 1205 ASN   A O   1 
ATOM   10479 C  CB  . ASN   B 2 1205 ? 133.118 119.901 134.205 1.00 36.03  ? 1205 ASN   A CB  1 
ATOM   10480 C  CG  . ASN   B 2 1205 ? 133.461 121.373 134.153 1.00 44.06  ? 1205 ASN   A CG  1 
ATOM   10481 O  OD1 . ASN   B 2 1205 ? 134.168 121.826 133.257 1.00 48.37  ? 1205 ASN   A OD1 1 
ATOM   10482 N  ND2 . ASN   B 2 1205 ? 132.954 122.130 135.114 1.00 45.02  ? 1205 ASN   A ND2 1 
ATOM   10483 N  N   . LEU   B 2 1206 ? 131.210 117.341 134.333 1.00 26.67  ? 1206 LEU   A N   1 
ATOM   10484 C  CA  . LEU   B 2 1206 ? 131.035 115.908 134.134 1.00 29.24  ? 1206 LEU   A CA  1 
ATOM   10485 C  C   . LEU   B 2 1206 ? 129.805 115.597 133.288 1.00 35.55  ? 1206 LEU   A C   1 
ATOM   10486 O  O   . LEU   B 2 1206 ? 129.798 114.602 132.557 1.00 45.42  ? 1206 LEU   A O   1 
ATOM   10487 C  CB  . LEU   B 2 1206 ? 130.966 115.194 135.480 1.00 32.00  ? 1206 LEU   A CB  1 
ATOM   10488 C  CG  . LEU   B 2 1206 ? 132.274 115.139 136.268 1.00 38.73  ? 1206 LEU   A CG  1 
ATOM   10489 C  CD1 . LEU   B 2 1206 ? 132.082 114.393 137.573 1.00 38.98  ? 1206 LEU   A CD1 1 
ATOM   10490 C  CD2 . LEU   B 2 1206 ? 133.363 114.488 135.440 1.00 40.17  ? 1206 LEU   A CD2 1 
ATOM   10491 N  N   . PHE   B 2 1207 ? 128.767 116.431 133.356 1.00 33.54  ? 1207 PHE   A N   1 
ATOM   10492 C  CA  . PHE   B 2 1207 ? 127.633 116.278 132.451 1.00 33.80  ? 1207 PHE   A CA  1 
ATOM   10493 C  C   . PHE   B 2 1207 ? 128.063 116.485 131.007 1.00 36.35  ? 1207 PHE   A C   1 
ATOM   10494 O  O   . PHE   B 2 1207 ? 127.720 115.686 130.122 1.00 42.37  ? 1207 PHE   A O   1 
ATOM   10495 C  CB  . PHE   B 2 1207 ? 126.539 117.271 132.838 1.00 32.41  ? 1207 PHE   A CB  1 
ATOM   10496 C  CG  . PHE   B 2 1207 ? 125.269 117.127 132.056 1.00 33.68  ? 1207 PHE   A CG  1 
ATOM   10497 C  CD1 . PHE   B 2 1207 ? 124.256 116.306 132.507 1.00 39.40  ? 1207 PHE   A CD1 1 
ATOM   10498 C  CD2 . PHE   B 2 1207 ? 125.073 117.837 130.886 1.00 41.32  ? 1207 PHE   A CD2 1 
ATOM   10499 C  CE1 . PHE   B 2 1207 ? 123.083 116.184 131.800 1.00 42.81  ? 1207 PHE   A CE1 1 
ATOM   10500 C  CE2 . PHE   B 2 1207 ? 123.901 117.715 130.175 1.00 38.43  ? 1207 PHE   A CE2 1 
ATOM   10501 C  CZ  . PHE   B 2 1207 ? 122.907 116.888 130.633 1.00 39.86  ? 1207 PHE   A CZ  1 
ATOM   10502 N  N   . SER   B 2 1208 ? 128.837 117.542 130.753 1.00 38.37  ? 1208 SER   A N   1 
ATOM   10503 C  CA  . SER   B 2 1208 ? 129.348 117.766 129.407 1.00 36.73  ? 1208 SER   A CA  1 
ATOM   10504 C  C   . SER   B 2 1208 ? 130.227 116.608 128.958 1.00 41.77  ? 1208 SER   A C   1 
ATOM   10505 O  O   . SER   B 2 1208 ? 130.175 116.195 127.795 1.00 51.11  ? 1208 SER   A O   1 
ATOM   10506 C  CB  . SER   B 2 1208 ? 130.117 119.084 129.347 1.00 44.90  ? 1208 SER   A CB  1 
ATOM   10507 O  OG  . SER   B 2 1208 ? 129.256 120.182 129.590 1.00 56.74  ? 1208 SER   A OG  1 
ATOM   10508 N  N   . GLY   B 2 1209 ? 131.037 116.066 129.869 1.00 35.32  ? 1209 GLY   A N   1 
ATOM   10509 C  CA  . GLY   B 2 1209 ? 131.858 114.916 129.525 1.00 38.22  ? 1209 GLY   A CA  1 
ATOM   10510 C  C   . GLY   B 2 1209 ? 131.038 113.690 129.171 1.00 34.50  ? 1209 GLY   A C   1 
ATOM   10511 O  O   . GLY   B 2 1209 ? 131.363 112.967 128.227 1.00 43.91  ? 1209 GLY   A O   1 
ATOM   10512 N  N   . LEU   B 2 1210 ? 129.969 113.436 129.927 1.00 31.93  ? 1210 LEU   A N   1 
ATOM   10513 C  CA  . LEU   B 2 1210 ? 129.076 112.330 129.599 1.00 33.24  ? 1210 LEU   A CA  1 
ATOM   10514 C  C   . LEU   B 2 1210 ? 128.403 112.549 128.253 1.00 43.25  ? 1210 LEU   A C   1 
ATOM   10515 O  O   . LEU   B 2 1210 ? 128.072 111.587 127.552 1.00 44.70  ? 1210 LEU   A O   1 
ATOM   10516 C  CB  . LEU   B 2 1210 ? 128.022 112.151 130.691 1.00 35.10  ? 1210 LEU   A CB  1 
ATOM   10517 C  CG  . LEU   B 2 1210 ? 128.396 111.335 131.926 1.00 39.32  ? 1210 LEU   A CG  1 
ATOM   10518 C  CD1 . LEU   B 2 1210 ? 127.218 111.262 132.875 1.00 42.60  ? 1210 LEU   A CD1 1 
ATOM   10519 C  CD2 . LEU   B 2 1210 ? 128.852 109.942 131.531 1.00 45.81  ? 1210 LEU   A CD2 1 
ATOM   10520 N  N   . ASN   B 2 1211 ? 128.195 113.807 127.872 1.00 48.33  ? 1211 ASN   A N   1 
ATOM   10521 C  CA  . ASN   B 2 1211 ? 127.543 114.113 126.605 1.00 40.51  ? 1211 ASN   A CA  1 
ATOM   10522 C  C   . ASN   B 2 1211 ? 128.500 114.116 125.416 1.00 46.84  ? 1211 ASN   A C   1 
ATOM   10523 O  O   . ASN   B 2 1211 ? 128.178 114.727 124.392 1.00 60.04  ? 1211 ASN   A O   1 
ATOM   10524 C  CB  . ASN   B 2 1211 ? 126.829 115.462 126.694 1.00 41.84  ? 1211 ASN   A CB  1 
ATOM   10525 C  CG  . ASN   B 2 1211 ? 125.563 115.395 127.515 1.00 49.90  ? 1211 ASN   A CG  1 
ATOM   10526 O  OD1 . ASN   B 2 1211 ? 124.458 115.439 126.975 1.00 47.84  ? 1211 ASN   A OD1 1 
ATOM   10527 N  ND2 . ASN   B 2 1211 ? 125.715 115.283 128.828 1.00 54.36  ? 1211 ASN   A ND2 1 
ATOM   10528 N  N   . ILE   B 2 1212 ? 129.654 113.461 125.514 1.00 41.52  ? 1212 ILE   A N   1 
ATOM   10529 C  CA  . ILE   B 2 1212 ? 130.605 113.369 124.410 1.00 47.22  ? 1212 ILE   A CA  1 
ATOM   10530 C  C   . ILE   B 2 1212 ? 130.706 111.909 123.995 1.00 52.50  ? 1212 ILE   A C   1 
ATOM   10531 O  O   . ILE   B 2 1212 ? 131.014 111.041 124.820 1.00 53.87  ? 1212 ILE   A O   1 
ATOM   10532 C  CB  . ILE   B 2 1212 ? 131.984 113.928 124.789 1.00 43.52  ? 1212 ILE   A CB  1 
ATOM   10533 C  CG1 . ILE   B 2 1212 ? 131.857 115.344 125.338 1.00 48.86  ? 1212 ILE   A CG1 1 
ATOM   10534 C  CG2 . ILE   B 2 1212 ? 132.883 113.964 123.577 1.00 50.94  ? 1212 ILE   A CG2 1 
ATOM   10535 C  CD1 . ILE   B 2 1212 ? 133.181 116.005 125.634 1.00 51.53  ? 1212 ILE   A CD1 1 
ATOM   10536 N  N   . ASP   B 2 1213 ? 130.446 111.640 122.714 1.00 62.62  ? 1213 ASP   A N   1 
ATOM   10537 C  CA  . ASP   B 2 1213 ? 130.534 110.272 122.211 1.00 63.38  ? 1213 ASP   A CA  1 
ATOM   10538 C  C   . ASP   B 2 1213 ? 131.985 109.820 122.092 1.00 62.77  ? 1213 ASP   A C   1 
ATOM   10539 O  O   . ASP   B 2 1213 ? 132.334 108.708 122.504 1.00 64.59  ? 1213 ASP   A O   1 
ATOM   10540 C  CB  . ASP   B 2 1213 ? 129.822 110.165 120.863 1.00 64.14  ? 1213 ASP   A CB  1 
ATOM   10541 C  CG  . ASP   B 2 1213 ? 128.353 110.529 120.951 1.00 67.37  ? 1213 ASP   A CG  1 
ATOM   10542 O  OD1 . ASP   B 2 1213 ? 128.047 111.717 121.181 1.00 67.83  ? 1213 ASP   A OD1 1 
ATOM   10543 O  OD2 . ASP   B 2 1213 ? 127.504 109.627 120.790 1.00 67.35  ? 1213 ASP   A OD2 1 
ATOM   10544 N  N   . ALA   B 2 1214 ? 132.844 110.667 121.534 1.00 53.61  ? 1214 ALA   A N   1 
ATOM   10545 C  CA  . ALA   B 2 1214 ? 134.253 110.338 121.400 1.00 59.56  ? 1214 ALA   A CA  1 
ATOM   10546 C  C   . ALA   B 2 1214 ? 134.991 110.606 122.708 1.00 65.28  ? 1214 ALA   A C   1 
ATOM   10547 O  O   . ALA   B 2 1214 ? 134.536 111.367 123.564 1.00 69.07  ? 1214 ALA   A O   1 
ATOM   10548 C  CB  . ALA   B 2 1214 ? 134.888 111.141 120.266 1.00 59.51  ? 1214 ALA   A CB  1 
ATOM   10549 N  N   . TRP   B 2 1215 ? 136.148 109.966 122.860 1.00 72.39  ? 1215 TRP   A N   1 
ATOM   10550 C  CA  . TRP   B 2 1215 ? 136.946 110.152 124.062 1.00 74.59  ? 1215 TRP   A CA  1 
ATOM   10551 C  C   . TRP   B 2 1215 ? 138.426 110.030 123.734 1.00 72.30  ? 1215 TRP   A C   1 
ATOM   10552 O  O   . TRP   B 2 1215 ? 138.830 109.168 122.949 1.00 72.80  ? 1215 TRP   A O   1 
ATOM   10553 C  CB  . TRP   B 2 1215 ? 136.557 109.147 125.152 1.00 70.65  ? 1215 TRP   A CB  1 
ATOM   10554 C  CG  . TRP   B 2 1215 ? 135.436 109.634 126.017 1.00 72.97  ? 1215 TRP   A CG  1 
ATOM   10555 C  CD1 . TRP   B 2 1215 ? 134.101 109.448 125.813 1.00 76.03  ? 1215 TRP   A CD1 1 
ATOM   10556 C  CD2 . TRP   B 2 1215 ? 135.555 110.401 127.221 1.00 73.20  ? 1215 TRP   A CD2 1 
ATOM   10557 N  NE1 . TRP   B 2 1215 ? 133.381 110.048 126.816 1.00 77.38  ? 1215 TRP   A NE1 1 
ATOM   10558 C  CE2 . TRP   B 2 1215 ? 134.251 110.641 127.693 1.00 74.12  ? 1215 TRP   A CE2 1 
ATOM   10559 C  CE3 . TRP   B 2 1215 ? 136.637 110.905 127.947 1.00 75.84  ? 1215 TRP   A CE3 1 
ATOM   10560 C  CZ2 . TRP   B 2 1215 ? 134.001 111.360 128.857 1.00 73.06  ? 1215 TRP   A CZ2 1 
ATOM   10561 C  CZ3 . TRP   B 2 1215 ? 136.385 111.619 129.101 1.00 75.80  ? 1215 TRP   A CZ3 1 
ATOM   10562 C  CH2 . TRP   B 2 1215 ? 135.079 111.841 129.544 1.00 72.95  ? 1215 TRP   A CH2 1 
ATOM   10563 N  N   . THR   B 2 1216 ? 139.220 110.901 124.345 1.00 82.22  ? 1216 THR   A N   1 
ATOM   10564 C  CA  . THR   B 2 1216 ? 140.670 110.894 124.211 1.00 82.14  ? 1216 THR   A CA  1 
ATOM   10565 C  C   . THR   B 2 1216 ? 141.249 111.621 125.425 1.00 82.64  ? 1216 THR   A C   1 
ATOM   10566 O  O   . THR   B 2 1216 ? 140.531 111.896 126.393 1.00 84.39  ? 1216 THR   A O   1 
ATOM   10567 C  CB  . THR   B 2 1216 ? 141.094 111.525 122.874 1.00 83.53  ? 1216 THR   A CB  1 
ATOM   10568 O  OG1 . THR   B 2 1216 ? 142.524 111.567 122.793 1.00 85.08  ? 1216 THR   A OG1 1 
ATOM   10569 C  CG2 . THR   B 2 1216 ? 140.538 112.935 122.747 1.00 81.82  ? 1216 THR   A CG2 1 
ATOM   10570 N  N   . GLY   B 2 1217 ? 142.546 111.926 125.377 1.00 79.83  ? 1217 GLY   A N   1 
ATOM   10571 C  CA  . GLY   B 2 1217 ? 143.167 112.646 126.478 1.00 79.65  ? 1217 GLY   A CA  1 
ATOM   10572 C  C   . GLY   B 2 1217 ? 142.670 114.073 126.612 1.00 81.29  ? 1217 GLY   A C   1 
ATOM   10573 O  O   . GLY   B 2 1217 ? 142.536 114.591 127.725 1.00 82.58  ? 1217 GLY   A O   1 
ATOM   10574 N  N   . TRP   B 2 1218 ? 142.397 114.731 125.483 1.00 84.61  ? 1218 TRP   A N   1 
ATOM   10575 C  CA  . TRP   B 2 1218 ? 141.973 116.128 125.511 1.00 85.85  ? 1218 TRP   A CA  1 
ATOM   10576 C  C   . TRP   B 2 1218 ? 140.632 116.300 126.215 1.00 90.09  ? 1218 TRP   A C   1 
ATOM   10577 O  O   . TRP   B 2 1218 ? 140.401 117.326 126.872 1.00 91.17  ? 1218 TRP   A O   1 
ATOM   10578 C  CB  . TRP   B 2 1218 ? 141.904 116.675 124.086 1.00 83.37  ? 1218 TRP   A CB  1 
ATOM   10579 C  CG  . TRP   B 2 1218 ? 142.330 118.104 123.964 1.00 90.58  ? 1218 TRP   A CG  1 
ATOM   10580 C  CD1 . TRP   B 2 1218 ? 143.606 118.569 123.834 1.00 89.02  ? 1218 TRP   A CD1 1 
ATOM   10581 C  CD2 . TRP   B 2 1218 ? 141.480 119.256 123.950 1.00 93.38  ? 1218 TRP   A CD2 1 
ATOM   10582 N  NE1 . TRP   B 2 1218 ? 143.604 119.939 123.745 1.00 88.77  ? 1218 TRP   A NE1 1 
ATOM   10583 C  CE2 . TRP   B 2 1218 ? 142.311 120.386 123.813 1.00 93.34  ? 1218 TRP   A CE2 1 
ATOM   10584 C  CE3 . TRP   B 2 1218 ? 140.097 119.443 124.043 1.00 88.52  ? 1218 TRP   A CE3 1 
ATOM   10585 C  CZ2 . TRP   B 2 1218 ? 141.805 121.683 123.767 1.00 91.04  ? 1218 TRP   A CZ2 1 
ATOM   10586 C  CZ3 . TRP   B 2 1218 ? 139.598 120.732 123.996 1.00 89.22  ? 1218 TRP   A CZ3 1 
ATOM   10587 C  CH2 . TRP   B 2 1218 ? 140.449 121.835 123.859 1.00 89.05  ? 1218 TRP   A CH2 1 
ATOM   10588 N  N   . VAL   B 2 1219 ? 139.736 115.320 126.084 1.00 81.52  ? 1219 VAL   A N   1 
ATOM   10589 C  CA  . VAL   B 2 1219 ? 138.446 115.393 126.766 1.00 78.53  ? 1219 VAL   A CA  1 
ATOM   10590 C  C   . VAL   B 2 1219 ? 138.648 115.388 128.276 1.00 78.97  ? 1219 VAL   A C   1 
ATOM   10591 O  O   . VAL   B 2 1219 ? 138.062 116.203 129.002 1.00 85.10  ? 1219 VAL   A O   1 
ATOM   10592 C  CB  . VAL   B 2 1219 ? 137.534 114.242 126.310 1.00 76.71  ? 1219 VAL   A CB  1 
ATOM   10593 C  CG1 . VAL   B 2 1219 ? 136.161 114.375 126.941 1.00 79.47  ? 1219 VAL   A CG1 1 
ATOM   10594 C  CG2 . VAL   B 2 1219 ? 137.430 114.223 124.797 1.00 77.24  ? 1219 VAL   A CG2 1 
ATOM   10595 N  N   . TRP   B 2 1220 ? 139.485 114.471 128.769 1.00 68.21  ? 1220 TRP   A N   1 
ATOM   10596 C  CA  . TRP   B 2 1220 ? 139.826 114.473 130.187 1.00 70.77  ? 1220 TRP   A CA  1 
ATOM   10597 C  C   . TRP   B 2 1220 ? 140.456 115.798 130.586 1.00 72.64  ? 1220 TRP   A C   1 
ATOM   10598 O  O   . TRP   B 2 1220 ? 140.140 116.354 131.647 1.00 77.09  ? 1220 TRP   A O   1 
ATOM   10599 C  CB  . TRP   B 2 1220 ? 140.778 113.321 130.511 1.00 70.66  ? 1220 TRP   A CB  1 
ATOM   10600 C  CG  . TRP   B 2 1220 ? 140.161 111.963 130.450 1.00 73.97  ? 1220 TRP   A CG  1 
ATOM   10601 C  CD1 . TRP   B 2 1220 ? 140.105 111.137 129.367 1.00 74.82  ? 1220 TRP   A CD1 1 
ATOM   10602 C  CD2 . TRP   B 2 1220 ? 139.527 111.260 131.524 1.00 74.03  ? 1220 TRP   A CD2 1 
ATOM   10603 N  NE1 . TRP   B 2 1220 ? 139.467 109.967 129.697 1.00 74.82  ? 1220 TRP   A NE1 1 
ATOM   10604 C  CE2 . TRP   B 2 1220 ? 139.102 110.018 131.016 1.00 73.33  ? 1220 TRP   A CE2 1 
ATOM   10605 C  CE3 . TRP   B 2 1220 ? 139.271 111.563 132.863 1.00 75.06  ? 1220 TRP   A CE3 1 
ATOM   10606 C  CZ2 . TRP   B 2 1220 ? 138.437 109.080 131.800 1.00 75.21  ? 1220 TRP   A CZ2 1 
ATOM   10607 C  CZ3 . TRP   B 2 1220 ? 138.611 110.631 133.640 1.00 74.60  ? 1220 TRP   A CZ3 1 
ATOM   10608 C  CH2 . TRP   B 2 1220 ? 138.201 109.405 133.107 1.00 76.91  ? 1220 TRP   A CH2 1 
ATOM   10609 N  N   . PHE   B 2 1221 ? 141.339 116.323 129.734 1.00 67.09  ? 1221 PHE   A N   1 
ATOM   10610 C  CA  . PHE   B 2 1221 ? 142.004 117.586 130.029 1.00 65.50  ? 1221 PHE   A CA  1 
ATOM   10611 C  C   . PHE   B 2 1221 ? 140.992 118.697 130.263 1.00 70.34  ? 1221 PHE   A C   1 
ATOM   10612 O  O   . PHE   B 2 1221 ? 141.070 119.414 131.260 1.00 77.90  ? 1221 PHE   A O   1 
ATOM   10613 C  CB  . PHE   B 2 1221 ? 142.955 117.958 128.893 1.00 70.55  ? 1221 PHE   A CB  1 
ATOM   10614 C  CG  . PHE   B 2 1221 ? 143.516 119.347 129.005 1.00 76.41  ? 1221 PHE   A CG  1 
ATOM   10615 C  CD1 . PHE   B 2 1221 ? 144.582 119.611 129.848 1.00 76.50  ? 1221 PHE   A CD1 1 
ATOM   10616 C  CD2 . PHE   B 2 1221 ? 142.980 120.387 128.264 1.00 76.53  ? 1221 PHE   A CD2 1 
ATOM   10617 C  CE1 . PHE   B 2 1221 ? 145.100 120.888 129.953 1.00 74.59  ? 1221 PHE   A CE1 1 
ATOM   10618 C  CE2 . PHE   B 2 1221 ? 143.492 121.665 128.365 1.00 75.07  ? 1221 PHE   A CE2 1 
ATOM   10619 C  CZ  . PHE   B 2 1221 ? 144.554 121.916 129.210 1.00 75.65  ? 1221 PHE   A CZ  1 
ATOM   10620 N  N   . ALA   B 2 1222 ? 140.018 118.839 129.366 1.00 58.65  ? 1222 ALA   A N   1 
ATOM   10621 C  CA  . ALA   B 2 1222 ? 139.026 119.904 129.525 1.00 63.29  ? 1222 ALA   A CA  1 
ATOM   10622 C  C   . ALA   B 2 1222 ? 138.146 119.671 130.752 1.00 66.10  ? 1222 ALA   A C   1 
ATOM   10623 O  O   . ALA   B 2 1222 ? 137.966 120.573 131.600 1.00 69.78  ? 1222 ALA   A O   1 
ATOM   10624 C  CB  . ALA   B 2 1222 ? 138.172 120.005 128.264 1.00 59.09  ? 1222 ALA   A CB  1 
ATOM   10625 N  N   . ILE   B 2 1223 ? 137.593 118.456 130.862 1.00 51.08  ? 1223 ILE   A N   1 
ATOM   10626 C  CA  . ILE   B 2 1223 ? 136.611 118.151 131.896 1.00 50.26  ? 1223 ILE   A CA  1 
ATOM   10627 C  C   . ILE   B 2 1223 ? 137.214 118.311 133.280 1.00 56.70  ? 1223 ILE   A C   1 
ATOM   10628 O  O   . ILE   B 2 1223 ? 136.512 118.680 134.229 1.00 62.13  ? 1223 ILE   A O   1 
ATOM   10629 C  CB  . ILE   B 2 1223 ? 136.038 116.733 131.689 1.00 48.60  ? 1223 ILE   A CB  1 
ATOM   10630 C  CG1 . ILE   B 2 1223 ? 135.350 116.619 130.330 1.00 52.37  ? 1223 ILE   A CG1 1 
ATOM   10631 C  CG2 . ILE   B 2 1223 ? 135.051 116.382 132.784 1.00 53.03  ? 1223 ILE   A CG2 1 
ATOM   10632 C  CD1 . ILE   B 2 1223 ? 134.246 117.613 130.114 1.00 58.40  ? 1223 ILE   A CD1 1 
ATOM   10633 N  N   . TRP   B 2 1224 ? 138.510 118.043 133.432 1.00 54.97  ? 1224 TRP   A N   1 
ATOM   10634 C  CA  . TRP   B 2 1224 ? 139.167 118.212 134.719 1.00 52.02  ? 1224 TRP   A CA  1 
ATOM   10635 C  C   . TRP   B 2 1224 ? 140.031 119.463 134.776 1.00 55.84  ? 1224 TRP   A C   1 
ATOM   10636 O  O   . TRP   B 2 1224 ? 140.708 119.691 135.782 1.00 67.29  ? 1224 TRP   A O   1 
ATOM   10637 C  CB  . TRP   B 2 1224 ? 139.989 116.969 135.052 1.00 59.20  ? 1224 TRP   A CB  1 
ATOM   10638 C  CG  . TRP   B 2 1224 ? 139.132 115.767 135.252 1.00 61.98  ? 1224 TRP   A CG  1 
ATOM   10639 C  CD1 . TRP   B 2 1224 ? 138.976 114.718 134.398 1.00 61.52  ? 1224 TRP   A CD1 1 
ATOM   10640 C  CD2 . TRP   B 2 1224 ? 138.288 115.499 136.375 1.00 62.66  ? 1224 TRP   A CD2 1 
ATOM   10641 N  NE1 . TRP   B 2 1224 ? 138.096 113.806 134.924 1.00 60.71  ? 1224 TRP   A NE1 1 
ATOM   10642 C  CE2 . TRP   B 2 1224 ? 137.658 114.263 136.139 1.00 63.12  ? 1224 TRP   A CE2 1 
ATOM   10643 C  CE3 . TRP   B 2 1224 ? 138.009 116.182 137.562 1.00 61.43  ? 1224 TRP   A CE3 1 
ATOM   10644 C  CZ2 . TRP   B 2 1224 ? 136.767 113.695 137.044 1.00 63.93  ? 1224 TRP   A CZ2 1 
ATOM   10645 C  CZ3 . TRP   B 2 1224 ? 137.126 115.618 138.458 1.00 61.78  ? 1224 TRP   A CZ3 1 
ATOM   10646 C  CH2 . TRP   B 2 1224 ? 136.514 114.387 138.195 1.00 63.21  ? 1224 TRP   A CH2 1 
ATOM   10647 N  N   . PHE   B 2 1225 ? 140.032 120.270 133.719 1.00 48.46  ? 1225 PHE   A N   1 
ATOM   10648 C  CA  . PHE   B 2 1225 ? 140.662 121.579 133.743 1.00 51.75  ? 1225 PHE   A CA  1 
ATOM   10649 C  C   . PHE   B 2 1225 ? 139.735 122.637 134.298 1.00 56.63  ? 1225 PHE   A C   1 
ATOM   10650 O  O   . PHE   B 2 1225 ? 140.199 123.588 134.938 1.00 60.96  ? 1225 PHE   A O   1 
ATOM   10651 C  CB  . PHE   B 2 1225 ? 141.106 121.970 132.331 1.00 50.44  ? 1225 PHE   A CB  1 
ATOM   10652 C  CG  . PHE   B 2 1225 ? 141.574 123.390 132.207 1.00 52.05  ? 1225 PHE   A CG  1 
ATOM   10653 C  CD1 . PHE   B 2 1225 ? 142.854 123.744 132.583 1.00 52.43  ? 1225 PHE   A CD1 1 
ATOM   10654 C  CD2 . PHE   B 2 1225 ? 140.739 124.367 131.694 1.00 55.64  ? 1225 PHE   A CD2 1 
ATOM   10655 C  CE1 . PHE   B 2 1225 ? 143.289 125.045 132.465 1.00 53.61  ? 1225 PHE   A CE1 1 
ATOM   10656 C  CE2 . PHE   B 2 1225 ? 141.170 125.671 131.574 1.00 54.60  ? 1225 PHE   A CE2 1 
ATOM   10657 C  CZ  . PHE   B 2 1225 ? 142.446 126.009 131.958 1.00 55.54  ? 1225 PHE   A CZ  1 
ATOM   10658 N  N   . GLY   B 2 1226 ? 138.438 122.497 134.056 1.00 54.29  ? 1226 GLY   A N   1 
ATOM   10659 C  CA  . GLY   B 2 1226 ? 137.483 123.371 134.707 1.00 45.51  ? 1226 GLY   A CA  1 
ATOM   10660 C  C   . GLY   B 2 1226 ? 137.551 123.297 136.229 1.00 42.90  ? 1226 GLY   A C   1 
ATOM   10661 O  O   . GLY   B 2 1226 ? 137.889 124.268 136.929 1.00 50.01  ? 1226 GLY   A O   1 
ATOM   10662 N  N   . PRO   B 2 1227 ? 137.209 122.124 136.769 1.00 37.65  ? 1227 PRO   A N   1 
ATOM   10663 C  CA  . PRO   B 2 1227 ? 137.283 121.929 138.225 1.00 38.17  ? 1227 PRO   A CA  1 
ATOM   10664 C  C   . PRO   B 2 1227 ? 138.661 122.145 138.821 1.00 39.98  ? 1227 PRO   A C   1 
ATOM   10665 O  O   . PRO   B 2 1227 ? 138.755 122.598 139.967 1.00 46.00  ? 1227 PRO   A O   1 
ATOM   10666 C  CB  . PRO   B 2 1227 ? 136.818 120.480 138.394 1.00 43.26  ? 1227 PRO   A CB  1 
ATOM   10667 C  CG  . PRO   B 2 1227 ? 135.873 120.280 137.277 1.00 41.41  ? 1227 PRO   A CG  1 
ATOM   10668 C  CD  . PRO   B 2 1227 ? 136.438 121.054 136.119 1.00 44.05  ? 1227 PRO   A CD  1 
ATOM   10669 N  N   . PHE   B 2 1228 ? 139.737 121.825 138.101 1.00 38.15  ? 1228 PHE   A N   1 
ATOM   10670 C  CA  . PHE   B 2 1228 ? 141.064 122.139 138.618 1.00 38.82  ? 1228 PHE   A CA  1 
ATOM   10671 C  C   . PHE   B 2 1228 ? 141.219 123.636 138.825 1.00 41.87  ? 1228 PHE   A C   1 
ATOM   10672 O  O   . PHE   B 2 1228 ? 141.751 124.082 139.851 1.00 46.28  ? 1228 PHE   A O   1 
ATOM   10673 C  CB  . PHE   B 2 1228 ? 142.139 121.613 137.670 1.00 41.72  ? 1228 PHE   A CB  1 
ATOM   10674 C  CG  . PHE   B 2 1228 ? 143.531 122.041 138.027 1.00 44.25  ? 1228 PHE   A CG  1 
ATOM   10675 C  CD1 . PHE   B 2 1228 ? 144.251 121.365 138.994 1.00 45.66  ? 1228 PHE   A CD1 1 
ATOM   10676 C  CD2 . PHE   B 2 1228 ? 144.128 123.109 137.381 1.00 48.04  ? 1228 PHE   A CD2 1 
ATOM   10677 C  CE1 . PHE   B 2 1228 ? 145.533 121.753 139.318 1.00 47.39  ? 1228 PHE   A CE1 1 
ATOM   10678 C  CE2 . PHE   B 2 1228 ? 145.408 123.501 137.702 1.00 50.13  ? 1228 PHE   A CE2 1 
ATOM   10679 C  CZ  . PHE   B 2 1228 ? 146.112 122.822 138.671 1.00 48.82  ? 1228 PHE   A CZ  1 
ATOM   10680 N  N   . LEU   B 2 1229 ? 140.747 124.429 137.863 1.00 48.61  ? 1229 LEU   A N   1 
ATOM   10681 C  CA  . LEU   B 2 1229 ? 140.806 125.877 138.008 1.00 45.46  ? 1229 LEU   A CA  1 
ATOM   10682 C  C   . LEU   B 2 1229 ? 140.007 126.342 139.214 1.00 43.95  ? 1229 LEU   A C   1 
ATOM   10683 O  O   . LEU   B 2 1229 ? 140.486 127.175 139.991 1.00 49.45  ? 1229 LEU   A O   1 
ATOM   10684 C  CB  . LEU   B 2 1229 ? 140.302 126.563 136.740 1.00 48.15  ? 1229 LEU   A CB  1 
ATOM   10685 C  CG  . LEU   B 2 1229 ? 141.335 126.843 135.652 1.00 47.43  ? 1229 LEU   A CG  1 
ATOM   10686 C  CD1 . LEU   B 2 1229 ? 140.724 127.710 134.568 1.00 51.84  ? 1229 LEU   A CD1 1 
ATOM   10687 C  CD2 . LEU   B 2 1229 ? 142.559 127.508 136.244 1.00 49.65  ? 1229 LEU   A CD2 1 
ATOM   10688 N  N   . ILE   B 2 1230 ? 138.793 125.815 139.401 1.00 39.64  ? 1230 ILE   A N   1 
ATOM   10689 C  CA  . ILE   B 2 1230 ? 137.997 126.313 140.523 1.00 29.41  ? 1230 ILE   A CA  1 
ATOM   10690 C  C   . ILE   B 2 1230 ? 138.609 125.891 141.857 1.00 34.71  ? 1230 ILE   A C   1 
ATOM   10691 O  O   . ILE   B 2 1230 ? 138.600 126.662 142.823 1.00 45.06  ? 1230 ILE   A O   1 
ATOM   10692 C  CB  . ILE   B 2 1230 ? 136.518 125.895 140.411 1.00 33.97  ? 1230 ILE   A CB  1 
ATOM   10693 C  CG1 . ILE   B 2 1230 ? 135.693 126.693 141.422 1.00 35.78  ? 1230 ILE   A CG1 1 
ATOM   10694 C  CG2 . ILE   B 2 1230 ? 136.330 124.417 140.651 1.00 43.56  ? 1230 ILE   A CG2 1 
ATOM   10695 C  CD1 . ILE   B 2 1230 ? 134.271 126.241 141.561 1.00 45.52  ? 1230 ILE   A CD1 1 
ATOM   10696 N  N   . TRP   B 2 1231 ? 139.167 124.681 141.933 1.00 45.72  ? 1231 TRP   A N   1 
ATOM   10697 C  CA  . TRP   B 2 1231 ? 139.790 124.232 143.176 1.00 40.68  ? 1231 TRP   A CA  1 
ATOM   10698 C  C   . TRP   B 2 1231 ? 141.020 125.065 143.512 1.00 45.02  ? 1231 TRP   A C   1 
ATOM   10699 O  O   . TRP   B 2 1231 ? 141.201 125.485 144.661 1.00 53.26  ? 1231 TRP   A O   1 
ATOM   10700 C  CB  . TRP   B 2 1231 ? 140.154 122.752 143.081 1.00 43.24  ? 1231 TRP   A CB  1 
ATOM   10701 C  CG  . TRP   B 2 1231 ? 139.021 121.829 143.390 1.00 45.15  ? 1231 TRP   A CG  1 
ATOM   10702 C  CD1 . TRP   B 2 1231 ? 137.896 121.637 142.649 1.00 45.08  ? 1231 TRP   A CD1 1 
ATOM   10703 C  CD2 . TRP   B 2 1231 ? 138.909 120.961 144.521 1.00 46.50  ? 1231 TRP   A CD2 1 
ATOM   10704 N  NE1 . TRP   B 2 1231 ? 137.086 120.707 143.247 1.00 45.67  ? 1231 TRP   A NE1 1 
ATOM   10705 C  CE2 . TRP   B 2 1231 ? 137.685 120.276 144.400 1.00 50.52  ? 1231 TRP   A CE2 1 
ATOM   10706 C  CE3 . TRP   B 2 1231 ? 139.723 120.697 145.626 1.00 48.99  ? 1231 TRP   A CE3 1 
ATOM   10707 C  CZ2 . TRP   B 2 1231 ? 137.256 119.344 145.341 1.00 54.59  ? 1231 TRP   A CZ2 1 
ATOM   10708 C  CZ3 . TRP   B 2 1231 ? 139.296 119.773 146.558 1.00 52.37  ? 1231 TRP   A CZ3 1 
ATOM   10709 C  CH2 . TRP   B 2 1231 ? 138.073 119.106 146.410 1.00 53.55  ? 1231 TRP   A CH2 1 
ATOM   10710 N  N   . VAL   B 2 1232 ? 141.877 125.322 142.522 1.00 44.84  ? 1232 VAL   A N   1 
ATOM   10711 C  CA  . VAL   B 2 1232 ? 143.070 126.123 142.781 1.00 36.47  ? 1232 VAL   A CA  1 
ATOM   10712 C  C   . VAL   B 2 1232 ? 142.686 127.555 143.130 1.00 43.59  ? 1232 VAL   A C   1 
ATOM   10713 O  O   . VAL   B 2 1232 ? 143.314 128.189 143.987 1.00 51.94  ? 1232 VAL   A O   1 
ATOM   10714 C  CB  . VAL   B 2 1232 ? 144.028 126.062 141.578 1.00 37.00  ? 1232 VAL   A CB  1 
ATOM   10715 C  CG1 . VAL   B 2 1232 ? 145.212 126.981 141.793 1.00 42.93  ? 1232 VAL   A CG1 1 
ATOM   10716 C  CG2 . VAL   B 2 1232 ? 144.506 124.639 141.362 1.00 43.57  ? 1232 VAL   A CG2 1 
ATOM   10717 N  N   . PHE   B 2 1233 ? 141.650 128.091 142.478 1.00 42.19  ? 1233 PHE   A N   1 
ATOM   10718 C  CA  . PHE   B 2 1233 ? 141.199 129.439 142.797 1.00 31.66  ? 1233 PHE   A CA  1 
ATOM   10719 C  C   . PHE   B 2 1233 ? 140.652 129.521 144.214 1.00 44.22  ? 1233 PHE   A C   1 
ATOM   10720 O  O   . PHE   B 2 1233 ? 140.894 130.503 144.920 1.00 53.56  ? 1233 PHE   A O   1 
ATOM   10721 C  CB  . PHE   B 2 1233 ? 140.146 129.892 141.790 1.00 39.73  ? 1233 PHE   A CB  1 
ATOM   10722 C  CG  . PHE   B 2 1233 ? 139.634 131.279 142.035 1.00 44.45  ? 1233 PHE   A CG  1 
ATOM   10723 C  CD1 . PHE   B 2 1233 ? 140.353 132.379 141.607 1.00 44.34  ? 1233 PHE   A CD1 1 
ATOM   10724 C  CD2 . PHE   B 2 1233 ? 138.432 131.483 142.686 1.00 46.35  ? 1233 PHE   A CD2 1 
ATOM   10725 C  CE1 . PHE   B 2 1233 ? 139.885 133.653 141.830 1.00 46.79  ? 1233 PHE   A CE1 1 
ATOM   10726 C  CE2 . PHE   B 2 1233 ? 137.961 132.755 142.910 1.00 43.80  ? 1233 PHE   A CE2 1 
ATOM   10727 C  CZ  . PHE   B 2 1233 ? 138.687 133.841 142.481 1.00 45.95  ? 1233 PHE   A CZ  1 
ATOM   10728 N  N   . THR   B 2 1234 ? 139.897 128.510 144.647 1.00 42.24  ? 1234 THR   A N   1 
ATOM   10729 C  CA  . THR   B 2 1234 ? 139.417 128.500 146.024 1.00 29.97  ? 1234 THR   A CA  1 
ATOM   10730 C  C   . THR   B 2 1234 ? 140.576 128.367 147.004 1.00 43.51  ? 1234 THR   A C   1 
ATOM   10731 O  O   . THR   B 2 1234 ? 140.557 128.967 148.085 1.00 54.68  ? 1234 THR   A O   1 
ATOM   10732 C  CB  . THR   B 2 1234 ? 138.406 127.372 146.224 1.00 35.22  ? 1234 THR   A CB  1 
ATOM   10733 O  OG1 . THR   B 2 1234 ? 137.341 127.512 145.278 1.00 48.47  ? 1234 THR   A OG1 1 
ATOM   10734 C  CG2 . THR   B 2 1234 ? 137.827 127.418 147.626 1.00 41.05  ? 1234 THR   A CG2 1 
ATOM   10735 N  N   . ALA   B 2 1235 ? 141.597 127.591 146.641 1.00 41.85  ? 1235 ALA   A N   1 
ATOM   10736 C  CA  . ALA   B 2 1235 ? 142.734 127.403 147.535 1.00 42.07  ? 1235 ALA   A CA  1 
ATOM   10737 C  C   . ALA   B 2 1235 ? 143.561 128.676 147.679 1.00 46.37  ? 1235 ALA   A C   1 
ATOM   10738 O  O   . ALA   B 2 1235 ? 144.031 128.990 148.776 1.00 50.10  ? 1235 ALA   A O   1 
ATOM   10739 C  CB  . ALA   B 2 1235 ? 143.608 126.253 147.036 1.00 45.26  ? 1235 ALA   A CB  1 
ATOM   10740 N  N   . VAL   B 2 1236 ? 143.758 129.416 146.591 1.00 44.94  ? 1236 VAL   A N   1 
ATOM   10741 C  CA  . VAL   B 2 1236 ? 144.654 130.572 146.618 1.00 36.99  ? 1236 VAL   A CA  1 
ATOM   10742 C  C   . VAL   B 2 1236 ? 143.919 131.852 146.997 1.00 39.36  ? 1236 VAL   A C   1 
ATOM   10743 O  O   . VAL   B 2 1236 ? 144.426 132.653 147.785 1.00 52.86  ? 1236 VAL   A O   1 
ATOM   10744 C  CB  . VAL   B 2 1236 ? 145.366 130.716 145.259 1.00 39.29  ? 1236 VAL   A CB  1 
ATOM   10745 C  CG1 . VAL   B 2 1236 ? 146.274 131.929 145.263 1.00 42.76  ? 1236 VAL   A CG1 1 
ATOM   10746 C  CG2 . VAL   B 2 1236 ? 146.158 129.461 144.943 1.00 43.43  ? 1236 VAL   A CG2 1 
ATOM   10747 N  N   . TYR   B 2 1237 ? 142.725 132.063 146.445 1.00 42.72  ? 1237 TYR   A N   1 
ATOM   10748 C  CA  . TYR   B 2 1237 ? 141.944 133.268 146.695 1.00 41.08  ? 1237 TYR   A CA  1 
ATOM   10749 C  C   . TYR   B 2 1237 ? 141.549 133.416 148.157 1.00 51.01  ? 1237 TYR   A C   1 
ATOM   10750 O  O   . TYR   B 2 1237 ? 141.326 134.542 148.614 1.00 57.49  ? 1237 TYR   A O   1 
ATOM   10751 C  CB  . TYR   B 2 1237 ? 140.697 133.241 145.811 1.00 46.91  ? 1237 TYR   A CB  1 
ATOM   10752 C  CG  . TYR   B 2 1237 ? 139.937 134.541 145.702 1.00 45.31  ? 1237 TYR   A CG  1 
ATOM   10753 C  CD1 . TYR   B 2 1237 ? 140.442 135.603 144.968 1.00 39.96  ? 1237 TYR   A CD1 1 
ATOM   10754 C  CD2 . TYR   B 2 1237 ? 138.694 134.689 146.296 1.00 52.03  ? 1237 TYR   A CD2 1 
ATOM   10755 C  CE1 . TYR   B 2 1237 ? 139.742 136.784 144.853 1.00 42.99  ? 1237 TYR   A CE1 1 
ATOM   10756 C  CE2 . TYR   B 2 1237 ? 137.987 135.865 146.185 1.00 49.69  ? 1237 TYR   A CE2 1 
ATOM   10757 C  CZ  . TYR   B 2 1237 ? 138.514 136.908 145.460 1.00 47.79  ? 1237 TYR   A CZ  1 
ATOM   10758 O  OH  . TYR   B 2 1237 ? 137.813 138.085 145.350 1.00 51.88  ? 1237 TYR   A OH  1 
ATOM   10759 N  N   . SER   B 2 1238 ? 141.461 132.315 148.897 1.00 41.18  ? 1238 SER   A N   1 
ATOM   10760 C  CA  . SER   B 2 1238 ? 141.073 132.343 150.299 1.00 33.50  ? 1238 SER   A CA  1 
ATOM   10761 C  C   . SER   B 2 1238 ? 142.247 132.574 151.238 1.00 45.24  ? 1238 SER   A C   1 
ATOM   10762 O  O   . SER   B 2 1238 ? 142.048 132.603 152.456 1.00 53.65  ? 1238 SER   A O   1 
ATOM   10763 C  CB  . SER   B 2 1238 ? 140.364 131.039 150.671 1.00 41.11  ? 1238 SER   A CB  1 
ATOM   10764 O  OG  . SER   B 2 1238 ? 139.223 130.835 149.858 1.00 44.87  ? 1238 SER   A OG  1 
ATOM   10765 N  N   . VAL   B 2 1239 ? 143.461 132.724 150.712 1.00 45.05  ? 1239 VAL   A N   1 
ATOM   10766 C  CA  . VAL   B 2 1239 ? 144.623 133.065 151.527 1.00 36.09  ? 1239 VAL   A CA  1 
ATOM   10767 C  C   . VAL   B 2 1239 ? 145.126 134.475 151.261 1.00 46.47  ? 1239 VAL   A C   1 
ATOM   10768 O  O   . VAL   B 2 1239 ? 146.079 134.913 151.927 1.00 54.59  ? 1239 VAL   A O   1 
ATOM   10769 C  CB  . VAL   B 2 1239 ? 145.766 132.045 151.336 1.00 41.38  ? 1239 VAL   A CB  1 
ATOM   10770 C  CG1 . VAL   B 2 1239 ? 146.694 132.029 152.546 1.00 47.43  ? 1239 VAL   A CG1 1 
ATOM   10771 C  CG2 . VAL   B 2 1239 ? 145.200 130.666 151.112 1.00 46.41  ? 1239 VAL   A CG2 1 
ATOM   10772 N  N   . ILE   B 2 1240 ? 144.520 135.205 150.329 1.00 44.56  ? 1240 ILE   A N   1 
ATOM   10773 C  CA  . ILE   B 2 1240 ? 144.906 136.588 150.064 1.00 43.52  ? 1240 ILE   A CA  1 
ATOM   10774 C  C   . ILE   B 2 1240 ? 144.584 137.410 151.305 1.00 43.47  ? 1240 ILE   A C   1 
ATOM   10775 O  O   . ILE   B 2 1240 ? 143.424 137.441 151.741 1.00 47.62  ? 1240 ILE   A O   1 
ATOM   10776 C  CB  . ILE   B 2 1240 ? 144.194 137.144 148.822 1.00 41.44  ? 1240 ILE   A CB  1 
ATOM   10777 C  CG1 . ILE   B 2 1240 ? 144.562 136.321 147.588 1.00 43.09  ? 1240 ILE   A CG1 1 
ATOM   10778 C  CG2 . ILE   B 2 1240 ? 144.551 138.604 148.612 1.00 46.80  ? 1240 ILE   A CG2 1 
ATOM   10779 C  CD1 . ILE   B 2 1240 ? 143.838 136.742 146.334 1.00 47.41  ? 1240 ILE   A CD1 1 
ATOM   10780 N  N   . PRO   B 2 1241 ? 145.568 138.080 151.907 1.00 38.53  ? 1241 PRO   A N   1 
ATOM   10781 C  CA  . PRO   B 2 1241 ? 145.300 138.814 153.138 1.00 34.00  ? 1241 PRO   A CA  1 
ATOM   10782 C  C   . PRO   B 2 1241 ? 144.341 139.962 152.886 1.00 52.52  ? 1241 PRO   A C   1 
ATOM   10783 O  O   . PRO   B 2 1241 ? 144.280 140.504 151.769 1.00 58.68  ? 1241 PRO   A O   1 
ATOM   10784 C  CB  . PRO   B 2 1241 ? 146.691 139.325 153.555 1.00 45.40  ? 1241 PRO   A CB  1 
ATOM   10785 C  CG  . PRO   B 2 1241 ? 147.648 138.426 152.860 1.00 49.03  ? 1241 PRO   A CG  1 
ATOM   10786 C  CD  . PRO   B 2 1241 ? 146.996 138.089 151.559 1.00 47.38  ? 1241 PRO   A CD  1 
ATOM   10787 N  N   . PRO   B 2 1242 ? 143.556 140.356 153.890 1.00 52.02  ? 1242 PRO   A N   1 
ATOM   10788 C  CA  . PRO   B 2 1242 ? 142.628 141.479 153.692 1.00 45.52  ? 1242 PRO   A CA  1 
ATOM   10789 C  C   . PRO   B 2 1242 ? 143.322 142.777 153.332 1.00 50.41  ? 1242 PRO   A C   1 
ATOM   10790 O  O   . PRO   B 2 1242 ? 142.720 143.625 152.661 1.00 55.49  ? 1242 PRO   A O   1 
ATOM   10791 C  CB  . PRO   B 2 1242 ? 141.908 141.575 155.043 1.00 48.66  ? 1242 PRO   A CB  1 
ATOM   10792 C  CG  . PRO   B 2 1242 ? 142.065 140.225 155.652 1.00 51.89  ? 1242 PRO   A CG  1 
ATOM   10793 C  CD  . PRO   B 2 1242 ? 143.415 139.753 155.223 1.00 53.30  ? 1242 PRO   A CD  1 
ATOM   10794 N  N   . SER   B 2 1243 ? 144.573 142.960 153.759 1.00 47.22  ? 1243 SER   A N   1 
ATOM   10795 C  CA  . SER   B 2 1243 ? 145.308 144.170 153.406 1.00 45.58  ? 1243 SER   A CA  1 
ATOM   10796 C  C   . SER   B 2 1243 ? 145.496 144.285 151.899 1.00 55.25  ? 1243 SER   A C   1 
ATOM   10797 O  O   . SER   B 2 1243 ? 145.335 145.368 151.326 1.00 61.13  ? 1243 SER   A O   1 
ATOM   10798 C  CB  . SER   B 2 1243 ? 146.660 144.182 154.113 1.00 46.64  ? 1243 SER   A CB  1 
ATOM   10799 O  OG  . SER   B 2 1243 ? 146.499 144.094 155.516 1.00 58.09  ? 1243 SER   A OG  1 
ATOM   10800 N  N   . SER   B 2 1244 ? 145.841 143.177 151.240 1.00 53.87  ? 1244 SER   A N   1 
ATOM   10801 C  CA  . SER   B 2 1244 ? 146.053 143.210 149.798 1.00 51.79  ? 1244 SER   A CA  1 
ATOM   10802 C  C   . SER   B 2 1244 ? 144.739 143.366 149.045 1.00 55.77  ? 1244 SER   A C   1 
ATOM   10803 O  O   . SER   B 2 1244 ? 144.657 144.134 148.080 1.00 62.13  ? 1244 SER   A O   1 
ATOM   10804 C  CB  . SER   B 2 1244 ? 146.780 141.943 149.352 1.00 55.24  ? 1244 SER   A CB  1 
ATOM   10805 O  OG  . SER   B 2 1244 ? 147.989 141.773 150.068 1.00 57.91  ? 1244 SER   A OG  1 
ATOM   10806 N  N   . PHE   B 2 1245 ? 143.701 142.653 149.474 1.00 47.10  ? 1245 PHE   A N   1 
ATOM   10807 C  CA  . PHE   B 2 1245 ? 142.422 142.642 148.782 1.00 46.73  ? 1245 PHE   A CA  1 
ATOM   10808 C  C   . PHE   B 2 1245 ? 141.388 142.054 149.729 1.00 53.29  ? 1245 PHE   A C   1 
ATOM   10809 O  O   . PHE   B 2 1245 ? 141.679 141.092 150.443 1.00 62.03  ? 1245 PHE   A O   1 
ATOM   10810 C  CB  . PHE   B 2 1245 ? 142.514 141.829 147.484 1.00 49.25  ? 1245 PHE   A CB  1 
ATOM   10811 C  CG  . PHE   B 2 1245 ? 141.335 141.990 146.573 1.00 52.99  ? 1245 PHE   A CG  1 
ATOM   10812 C  CD1 . PHE   B 2 1245 ? 141.120 143.179 145.900 1.00 58.92  ? 1245 PHE   A CD1 1 
ATOM   10813 C  CD2 . PHE   B 2 1245 ? 140.452 140.945 146.373 1.00 55.33  ? 1245 PHE   A CD2 1 
ATOM   10814 C  CE1 . PHE   B 2 1245 ? 140.036 143.328 145.055 1.00 62.07  ? 1245 PHE   A CE1 1 
ATOM   10815 C  CE2 . PHE   B 2 1245 ? 139.367 141.086 145.530 1.00 56.67  ? 1245 PHE   A CE2 1 
ATOM   10816 C  CZ  . PHE   B 2 1245 ? 139.159 142.279 144.870 1.00 58.74  ? 1245 PHE   A CZ  1 
ATOM   10817 N  N   . TYR   B 2 1246 ? 140.189 142.643 149.744 1.00 48.85  ? 1246 TYR   A N   1 
ATOM   10818 C  CA  . TYR   B 2 1246 ? 139.175 142.220 150.706 1.00 53.46  ? 1246 TYR   A CA  1 
ATOM   10819 C  C   . TYR   B 2 1246 ? 138.788 140.761 150.495 1.00 60.99  ? 1246 TYR   A C   1 
ATOM   10820 O  O   . TYR   B 2 1246 ? 138.785 139.966 151.442 1.00 65.70  ? 1246 TYR   A O   1 
ATOM   10821 C  CB  . TYR   B 2 1246 ? 137.949 143.127 150.607 1.00 52.79  ? 1246 TYR   A CB  1 
ATOM   10822 C  CG  . TYR   B 2 1246 ? 136.756 142.626 151.385 1.00 53.50  ? 1246 TYR   A CG  1 
ATOM   10823 C  CD1 . TYR   B 2 1246 ? 136.832 142.426 152.755 1.00 56.59  ? 1246 TYR   A CD1 1 
ATOM   10824 C  CD2 . TYR   B 2 1246 ? 135.551 142.361 150.751 1.00 52.18  ? 1246 TYR   A CD2 1 
ATOM   10825 C  CE1 . TYR   B 2 1246 ? 135.747 141.967 153.469 1.00 58.43  ? 1246 TYR   A CE1 1 
ATOM   10826 C  CE2 . TYR   B 2 1246 ? 134.459 141.904 151.458 1.00 53.29  ? 1246 TYR   A CE2 1 
ATOM   10827 C  CZ  . TYR   B 2 1246 ? 134.563 141.708 152.817 1.00 58.47  ? 1246 TYR   A CZ  1 
ATOM   10828 O  OH  . TYR   B 2 1246 ? 133.478 141.253 153.528 1.00 59.09  ? 1246 TYR   A OH  1 
ATOM   10829 N  N   . THR   B 2 1247 ? 138.411 140.410 149.266 1.00 46.08  ? 1247 THR   A N   1 
ATOM   10830 C  CA  . THR   B 2 1247 ? 138.269 139.038 148.781 1.00 46.36  ? 1247 THR   A CA  1 
ATOM   10831 C  C   . THR   B 2 1247 ? 137.064 138.317 149.380 1.00 46.14  ? 1247 THR   A C   1 
ATOM   10832 O  O   . THR   B 2 1247 ? 136.621 137.295 148.845 1.00 59.85  ? 1247 THR   A O   1 
ATOM   10833 C  CB  . THR   B 2 1247 ? 139.564 138.253 149.053 1.00 53.93  ? 1247 THR   A CB  1 
ATOM   10834 O  OG1 . THR   B 2 1247 ? 140.023 137.633 147.847 1.00 58.51  ? 1247 THR   A OG1 1 
ATOM   10835 C  CG2 . THR   B 2 1247 ? 139.367 137.183 150.123 1.00 52.71  ? 1247 THR   A CG2 1 
ATOM   10836 N  N   . GLY   B 2 1248 ? 136.488 138.864 150.447 1.00 40.83  ? 1248 GLY   A N   1 
ATOM   10837 C  CA  . GLY   B 2 1248 ? 135.211 138.404 150.959 1.00 45.21  ? 1248 GLY   A CA  1 
ATOM   10838 C  C   . GLY   B 2 1248 ? 135.172 137.016 151.572 1.00 50.43  ? 1248 GLY   A C   1 
ATOM   10839 O  O   . GLY   B 2 1248 ? 134.274 136.714 152.362 1.00 50.99  ? 1248 GLY   A O   1 
ATOM   10840 N  N   . VAL   B 2 1249 ? 136.135 136.162 151.225 1.00 53.40  ? 1249 VAL   A N   1 
ATOM   10841 C  CA  . VAL   B 2 1249 ? 136.057 134.742 151.557 1.00 36.66  ? 1249 VAL   A CA  1 
ATOM   10842 C  C   . VAL   B 2 1249 ? 137.325 134.280 152.260 1.00 39.32  ? 1249 VAL   A C   1 
ATOM   10843 O  O   . VAL   B 2 1249 ? 137.719 133.114 152.145 1.00 49.38  ? 1249 VAL   A O   1 
ATOM   10844 C  CB  . VAL   B 2 1249 ? 135.794 133.896 150.299 1.00 39.27  ? 1249 VAL   A CB  1 
ATOM   10845 C  CG1 . VAL   B 2 1249 ? 134.431 134.216 149.719 1.00 46.30  ? 1249 VAL   A CG1 1 
ATOM   10846 C  CG2 . VAL   B 2 1249 ? 136.874 134.133 149.264 1.00 44.35  ? 1249 VAL   A CG2 1 
ATOM   10847 N  N   . TYR   B 2 1250 ? 137.971 135.186 152.987 1.00 41.20  ? 1250 TYR   A N   1 
ATOM   10848 C  CA  . TYR   B 2 1250 ? 139.207 134.857 153.682 1.00 38.07  ? 1250 TYR   A CA  1 
ATOM   10849 C  C   . TYR   B 2 1250 ? 138.978 133.722 154.670 1.00 47.84  ? 1250 TYR   A C   1 
ATOM   10850 O  O   . TYR   B 2 1250 ? 138.088 133.797 155.522 1.00 51.51  ? 1250 TYR   A O   1 
ATOM   10851 C  CB  . TYR   B 2 1250 ? 139.738 136.091 154.403 1.00 37.74  ? 1250 TYR   A CB  1 
ATOM   10852 C  CG  . TYR   B 2 1250 ? 141.134 135.942 154.952 1.00 35.39  ? 1250 TYR   A CG  1 
ATOM   10853 C  CD1 . TYR   B 2 1250 ? 142.051 135.099 154.349 1.00 41.93  ? 1250 TYR   A CD1 1 
ATOM   10854 C  CD2 . TYR   B 2 1250 ? 141.531 136.643 156.078 1.00 41.13  ? 1250 TYR   A CD2 1 
ATOM   10855 C  CE1 . TYR   B 2 1250 ? 143.327 134.963 154.850 1.00 43.22  ? 1250 TYR   A CE1 1 
ATOM   10856 C  CE2 . TYR   B 2 1250 ? 142.801 136.513 156.585 1.00 43.58  ? 1250 TYR   A CE2 1 
ATOM   10857 C  CZ  . TYR   B 2 1250 ? 143.696 135.673 155.969 1.00 43.37  ? 1250 TYR   A CZ  1 
ATOM   10858 O  OH  . TYR   B 2 1250 ? 144.966 135.540 156.474 1.00 49.47  ? 1250 TYR   A OH  1 
ATOM   10859 N  N   . GLY   B 2 1251 ? 139.779 132.668 154.550 1.00 55.43  ? 1251 GLY   A N   1 
ATOM   10860 C  CA  . GLY   B 2 1251 ? 139.716 131.543 155.457 1.00 49.34  ? 1251 GLY   A CA  1 
ATOM   10861 C  C   . GLY   B 2 1251 ? 138.910 130.353 154.986 1.00 43.13  ? 1251 GLY   A C   1 
ATOM   10862 O  O   . GLY   B 2 1251 ? 138.782 129.384 155.742 1.00 54.70  ? 1251 GLY   A O   1 
ATOM   10863 N  N   . ASN   B 2 1252 ? 138.359 130.387 153.771 1.00 41.01  ? 1252 ASN   A N   1 
ATOM   10864 C  CA  . ASN   B 2 1252 ? 137.591 129.251 153.277 1.00 43.12  ? 1252 ASN   A CA  1 
ATOM   10865 C  C   . ASN   B 2 1252 ? 138.453 128.015 153.064 1.00 48.86  ? 1252 ASN   A C   1 
ATOM   10866 O  O   . ASN   B 2 1252 ? 137.925 126.899 153.088 1.00 54.95  ? 1252 ASN   A O   1 
ATOM   10867 C  CB  . ASN   B 2 1252 ? 136.878 129.615 151.977 1.00 47.37  ? 1252 ASN   A CB  1 
ATOM   10868 C  CG  . ASN   B 2 1252 ? 135.525 130.240 152.215 1.00 49.06  ? 1252 ASN   A CG  1 
ATOM   10869 O  OD1 . ASN   B 2 1252 ? 135.235 130.718 153.309 1.00 53.45  ? 1252 ASN   A OD1 1 
ATOM   10870 N  ND2 . ASN   B 2 1252 ? 134.683 130.237 151.191 1.00 52.23  ? 1252 ASN   A ND2 1 
ATOM   10871 N  N   . ASP   B 2 1253 ? 139.761 128.185 152.860 1.00 50.20  ? 1253 ASP   A N   1 
ATOM   10872 C  CA  . ASP   B 2 1253 ? 140.644 127.029 152.760 1.00 50.64  ? 1253 ASP   A CA  1 
ATOM   10873 C  C   . ASP   B 2 1253 ? 140.696 126.256 154.070 1.00 53.75  ? 1253 ASP   A C   1 
ATOM   10874 O  O   . ASP   B 2 1253 ? 141.009 125.060 154.075 1.00 55.51  ? 1253 ASP   A O   1 
ATOM   10875 C  CB  . ASP   B 2 1253 ? 142.045 127.475 152.345 1.00 49.92  ? 1253 ASP   A CB  1 
ATOM   10876 C  CG  . ASP   B 2 1253 ? 142.675 128.417 153.347 1.00 58.52  ? 1253 ASP   A CG  1 
ATOM   10877 O  OD1 . ASP   B 2 1253 ? 141.927 129.144 154.033 1.00 55.68  ? 1253 ASP   A OD1 1 
ATOM   10878 O  OD2 . ASP   B 2 1253 ? 143.919 128.431 153.449 1.00 64.17  ? 1253 ASP   A OD2 1 
ATOM   10879 N  N   . VAL   B 2 1254 ? 140.397 126.916 155.185 1.00 47.41  ? 1254 VAL   A N   1 
ATOM   10880 C  CA  . VAL   B 2 1254 ? 140.314 126.235 156.470 1.00 36.90  ? 1254 VAL   A CA  1 
ATOM   10881 C  C   . VAL   B 2 1254 ? 138.899 125.739 156.752 1.00 40.56  ? 1254 VAL   A C   1 
ATOM   10882 O  O   . VAL   B 2 1254 ? 138.725 124.668 157.341 1.00 50.30  ? 1254 VAL   A O   1 
ATOM   10883 C  CB  . VAL   B 2 1254 ? 140.806 127.163 157.591 1.00 36.07  ? 1254 VAL   A CB  1 
ATOM   10884 C  CG1 . VAL   B 2 1254 ? 140.862 126.420 158.913 1.00 45.87  ? 1254 VAL   A CG1 1 
ATOM   10885 C  CG2 . VAL   B 2 1254 ? 142.165 127.731 157.243 1.00 44.51  ? 1254 VAL   A CG2 1 
ATOM   10886 N  N   . PHE   B 2 1255 ? 137.882 126.489 156.335 1.00 39.01  ? 1255 PHE   A N   1 
ATOM   10887 C  CA  . PHE   B 2 1255 ? 136.500 126.141 156.628 1.00 43.55  ? 1255 PHE   A CA  1 
ATOM   10888 C  C   . PHE   B 2 1255 ? 135.932 125.079 155.697 1.00 46.91  ? 1255 PHE   A C   1 
ATOM   10889 O  O   . PHE   B 2 1255 ? 134.891 124.496 156.018 1.00 50.94  ? 1255 PHE   A O   1 
ATOM   10890 C  CB  . PHE   B 2 1255 ? 135.622 127.391 156.558 1.00 45.01  ? 1255 PHE   A CB  1 
ATOM   10891 C  CG  . PHE   B 2 1255 ? 136.054 128.489 157.484 1.00 41.90  ? 1255 PHE   A CG  1 
ATOM   10892 C  CD1 . PHE   B 2 1255 ? 136.598 128.198 158.720 1.00 46.34  ? 1255 PHE   A CD1 1 
ATOM   10893 C  CD2 . PHE   B 2 1255 ? 135.924 129.814 157.114 1.00 45.92  ? 1255 PHE   A CD2 1 
ATOM   10894 C  CE1 . PHE   B 2 1255 ? 136.998 129.205 159.569 1.00 47.31  ? 1255 PHE   A CE1 1 
ATOM   10895 C  CE2 . PHE   B 2 1255 ? 136.324 130.825 157.960 1.00 49.56  ? 1255 PHE   A CE2 1 
ATOM   10896 C  CZ  . PHE   B 2 1255 ? 136.861 130.520 159.188 1.00 48.14  ? 1255 PHE   A CZ  1 
ATOM   10897 N  N   . LEU   B 2 1256 ? 136.576 124.811 154.565 1.00 45.63  ? 1256 LEU   A N   1 
ATOM   10898 C  CA  . LEU   B 2 1256 ? 136.057 123.860 153.591 1.00 47.08  ? 1256 LEU   A CA  1 
ATOM   10899 C  C   . LEU   B 2 1256 ? 136.925 122.622 153.459 1.00 50.32  ? 1256 LEU   A C   1 
ATOM   10900 O  O   . LEU   B 2 1256 ? 136.408 121.500 153.509 1.00 58.06  ? 1256 LEU   A O   1 
ATOM   10901 C  CB  . LEU   B 2 1256 ? 135.908 124.533 152.220 1.00 48.47  ? 1256 LEU   A CB  1 
ATOM   10902 C  CG  . LEU   B 2 1256 ? 134.614 125.293 151.936 1.00 51.24  ? 1256 LEU   A CG  1 
ATOM   10903 C  CD1 . LEU   B 2 1256 ? 134.541 126.590 152.723 1.00 47.42  ? 1256 LEU   A CD1 1 
ATOM   10904 C  CD2 . LEU   B 2 1256 ? 134.501 125.557 150.452 1.00 55.54  ? 1256 LEU   A CD2 1 
ATOM   10905 N  N   . PHE   B 2 1257 ? 138.234 122.791 153.289 1.00 45.28  ? 1257 PHE   A N   1 
ATOM   10906 C  CA  . PHE   B 2 1257 ? 139.116 121.652 153.081 1.00 38.07  ? 1257 PHE   A CA  1 
ATOM   10907 C  C   . PHE   B 2 1257 ? 139.341 120.843 154.350 1.00 40.93  ? 1257 PHE   A C   1 
ATOM   10908 O  O   . PHE   B 2 1257 ? 139.940 119.765 154.277 1.00 52.31  ? 1257 PHE   A O   1 
ATOM   10909 C  CB  . PHE   B 2 1257 ? 140.452 122.127 152.513 1.00 40.37  ? 1257 PHE   A CB  1 
ATOM   10910 C  CG  . PHE   B 2 1257 ? 140.328 122.877 151.215 1.00 39.10  ? 1257 PHE   A CG  1 
ATOM   10911 C  CD1 . PHE   B 2 1257 ? 139.237 122.684 150.386 1.00 43.78  ? 1257 PHE   A CD1 1 
ATOM   10912 C  CD2 . PHE   B 2 1257 ? 141.301 123.776 150.826 1.00 41.35  ? 1257 PHE   A CD2 1 
ATOM   10913 C  CE1 . PHE   B 2 1257 ? 139.121 123.373 149.201 1.00 42.78  ? 1257 PHE   A CE1 1 
ATOM   10914 C  CE2 . PHE   B 2 1257 ? 141.187 124.465 149.640 1.00 46.44  ? 1257 PHE   A CE2 1 
ATOM   10915 C  CZ  . PHE   B 2 1257 ? 140.096 124.262 148.828 1.00 42.25  ? 1257 PHE   A CZ  1 
ATOM   10916 N  N   . ARG   B 2 1258 ? 138.888 121.333 155.501 1.00 39.53  ? 1258 ARG   A N   1 
ATOM   10917 C  CA  . ARG   B 2 1258 ? 138.979 120.606 156.759 1.00 35.12  ? 1258 ARG   A CA  1 
ATOM   10918 C  C   . ARG   B 2 1258 ? 137.609 120.229 157.306 1.00 36.06  ? 1258 ARG   A C   1 
ATOM   10919 O  O   . ARG   B 2 1258 ? 137.486 119.937 158.500 1.00 39.47  ? 1258 ARG   A O   1 
ATOM   10920 C  CB  . ARG   B 2 1258 ? 139.751 121.435 157.786 1.00 31.95  ? 1258 ARG   A CB  1 
ATOM   10921 C  CG  . ARG   B 2 1258 ? 141.067 121.972 157.260 1.00 36.04  ? 1258 ARG   A CG  1 
ATOM   10922 C  CD  . ARG   B 2 1258 ? 141.793 122.810 158.292 1.00 39.20  ? 1258 ARG   A CD  1 
ATOM   10923 N  NE  . ARG   B 2 1258 ? 143.024 123.377 157.753 1.00 43.18  ? 1258 ARG   A NE  1 
ATOM   10924 C  CZ  . ARG   B 2 1258 ? 143.894 124.086 158.459 1.00 45.70  ? 1258 ARG   A CZ  1 
ATOM   10925 N  NH1 . ARG   B 2 1258 ? 143.702 124.334 159.744 1.00 46.46  ? 1258 ARG   A NH1 1 
ATOM   10926 N  NH2 . ARG   B 2 1258 ? 144.987 124.552 157.863 1.00 47.94  ? 1258 ARG   A NH2 1 
ATOM   10927 N  N   . SER   B 2 1259 ? 136.581 120.228 156.464 1.00 33.42  ? 1259 SER   A N   1 
ATOM   10928 C  CA  . SER   B 2 1259 ? 135.208 119.980 156.878 1.00 32.75  ? 1259 SER   A CA  1 
ATOM   10929 C  C   . SER   B 2 1259 ? 134.701 118.698 156.238 1.00 37.30  ? 1259 SER   A C   1 
ATOM   10930 O  O   . SER   B 2 1259 ? 134.881 118.486 155.035 1.00 43.23  ? 1259 SER   A O   1 
ATOM   10931 C  CB  . SER   B 2 1259 ? 134.302 121.149 156.492 1.00 38.94  ? 1259 SER   A CB  1 
ATOM   10932 O  OG  . SER   B 2 1259 ? 132.951 120.882 156.826 1.00 47.61  ? 1259 SER   A OG  1 
ATOM   10933 N  N   . ALA   B 2 1260 ? 134.067 117.845 157.045 1.00 42.55  ? 1260 ALA   A N   1 
ATOM   10934 C  CA  . ALA   B 2 1260 ? 133.444 116.646 156.501 1.00 37.57  ? 1260 ALA   A CA  1 
ATOM   10935 C  C   . ALA   B 2 1260 ? 132.261 116.988 155.610 1.00 38.94  ? 1260 ALA   A C   1 
ATOM   10936 O  O   . ALA   B 2 1260 ? 131.964 116.248 154.664 1.00 44.87  ? 1260 ALA   A O   1 
ATOM   10937 C  CB  . ALA   B 2 1260 ? 133.006 115.719 157.632 1.00 40.15  ? 1260 ALA   A CB  1 
ATOM   10938 N  N   . ALA   B 2 1261 ? 131.583 118.103 155.891 1.00 39.83  ? 1261 ALA   A N   1 
ATOM   10939 C  CA  . ALA   B 2 1261 ? 130.431 118.500 155.090 1.00 40.33  ? 1261 ALA   A CA  1 
ATOM   10940 C  C   . ALA   B 2 1261 ? 130.827 118.738 153.641 1.00 43.78  ? 1261 ALA   A C   1 
ATOM   10941 O  O   . ALA   B 2 1261 ? 130.170 118.250 152.721 1.00 49.19  ? 1261 ALA   A O   1 
ATOM   10942 C  CB  . ALA   B 2 1261 ? 129.784 119.749 155.685 1.00 42.97  ? 1261 ALA   A CB  1 
ATOM   10943 N  N   . TYR   B 2 1262 ? 131.922 119.462 153.420 1.00 46.14  ? 1262 TYR   A N   1 
ATOM   10944 C  CA  . TYR   B 2 1262 ? 132.390 119.732 152.064 1.00 46.64  ? 1262 TYR   A CA  1 
ATOM   10945 C  C   . TYR   B 2 1262 ? 132.770 118.441 151.342 1.00 47.68  ? 1262 TYR   A C   1 
ATOM   10946 O  O   . TYR   B 2 1262 ? 132.269 118.147 150.244 1.00 57.25  ? 1262 TYR   A O   1 
ATOM   10947 C  CB  . TYR   B 2 1262 ? 133.575 120.697 152.141 1.00 41.27  ? 1262 TYR   A CB  1 
ATOM   10948 C  CG  . TYR   B 2 1262 ? 134.339 120.920 150.860 1.00 43.75  ? 1262 TYR   A CG  1 
ATOM   10949 C  CD1 . TYR   B 2 1262 ? 133.896 121.829 149.913 1.00 48.12  ? 1262 TYR   A CD1 1 
ATOM   10950 C  CD2 . TYR   B 2 1262 ? 135.529 120.252 150.617 1.00 42.19  ? 1262 TYR   A CD2 1 
ATOM   10951 C  CE1 . TYR   B 2 1262 ? 134.601 122.047 148.752 1.00 44.62  ? 1262 TYR   A CE1 1 
ATOM   10952 C  CE2 . TYR   B 2 1262 ? 136.240 120.464 149.458 1.00 41.00  ? 1262 TYR   A CE2 1 
ATOM   10953 C  CZ  . TYR   B 2 1262 ? 135.772 121.362 148.530 1.00 45.90  ? 1262 TYR   A CZ  1 
ATOM   10954 O  OH  . TYR   B 2 1262 ? 136.477 121.579 147.371 1.00 51.50  ? 1262 TYR   A OH  1 
ATOM   10955 N  N   . TRP   B 2 1263 ? 133.630 117.637 151.978 1.00 37.73  ? 1263 TRP   A N   1 
ATOM   10956 C  CA  . TRP   B 2 1263 ? 134.203 116.451 151.353 1.00 30.48  ? 1263 TRP   A CA  1 
ATOM   10957 C  C   . TRP   B 2 1263 ? 133.191 115.335 151.158 1.00 42.61  ? 1263 TRP   A C   1 
ATOM   10958 O  O   . TRP   B 2 1263 ? 133.435 114.434 150.351 1.00 50.64  ? 1263 TRP   A O   1 
ATOM   10959 C  CB  . TRP   B 2 1263 ? 135.370 115.926 152.188 1.00 39.67  ? 1263 TRP   A CB  1 
ATOM   10960 C  CG  . TRP   B 2 1263 ? 136.604 116.751 152.075 1.00 42.43  ? 1263 TRP   A CG  1 
ATOM   10961 C  CD1 . TRP   B 2 1263 ? 137.134 117.566 153.026 1.00 44.64  ? 1263 TRP   A CD1 1 
ATOM   10962 C  CD2 . TRP   B 2 1263 ? 137.464 116.847 150.939 1.00 42.86  ? 1263 TRP   A CD2 1 
ATOM   10963 N  NE1 . TRP   B 2 1263 ? 138.275 118.163 152.554 1.00 47.69  ? 1263 TRP   A NE1 1 
ATOM   10964 C  CE2 . TRP   B 2 1263 ? 138.498 117.738 151.272 1.00 44.23  ? 1263 TRP   A CE2 1 
ATOM   10965 C  CE3 . TRP   B 2 1263 ? 137.460 116.265 149.669 1.00 45.87  ? 1263 TRP   A CE3 1 
ATOM   10966 C  CZ2 . TRP   B 2 1263 ? 139.517 118.060 150.386 1.00 44.44  ? 1263 TRP   A CZ2 1 
ATOM   10967 C  CZ3 . TRP   B 2 1263 ? 138.471 116.587 148.791 1.00 41.16  ? 1263 TRP   A CZ3 1 
ATOM   10968 C  CH2 . TRP   B 2 1263 ? 139.486 117.475 149.152 1.00 40.57  ? 1263 TRP   A CH2 1 
ATOM   10969 N  N   . PHE   B 2 1264 ? 132.081 115.354 151.888 1.00 43.47  ? 1264 PHE   A N   1 
ATOM   10970 C  CA  . PHE   B 2 1264 ? 131.030 114.372 151.688 1.00 35.49  ? 1264 PHE   A CA  1 
ATOM   10971 C  C   . PHE   B 2 1264 ? 129.790 114.961 151.037 1.00 42.67  ? 1264 PHE   A C   1 
ATOM   10972 O  O   . PHE   B 2 1264 ? 128.831 114.224 150.788 1.00 53.17  ? 1264 PHE   A O   1 
ATOM   10973 C  CB  . PHE   B 2 1264 ? 130.656 113.722 153.023 1.00 43.36  ? 1264 PHE   A CB  1 
ATOM   10974 C  CG  . PHE   B 2 1264 ? 131.724 112.830 153.577 1.00 41.83  ? 1264 PHE   A CG  1 
ATOM   10975 C  CD1 . PHE   B 2 1264 ? 132.496 112.053 152.736 1.00 41.06  ? 1264 PHE   A CD1 1 
ATOM   10976 C  CD2 . PHE   B 2 1264 ? 131.962 112.772 154.936 1.00 47.27  ? 1264 PHE   A CD2 1 
ATOM   10977 C  CE1 . PHE   B 2 1264 ? 133.480 111.231 153.241 1.00 42.82  ? 1264 PHE   A CE1 1 
ATOM   10978 C  CE2 . PHE   B 2 1264 ? 132.945 111.952 155.444 1.00 45.39  ? 1264 PHE   A CE2 1 
ATOM   10979 C  CZ  . PHE   B 2 1264 ? 133.704 111.181 154.595 1.00 42.97  ? 1264 PHE   A CZ  1 
ATOM   10980 N  N   . GLY   B 2 1265 ? 129.785 116.258 150.755 1.00 35.23  ? 1265 GLY   A N   1 
ATOM   10981 C  CA  . GLY   B 2 1265 ? 128.664 116.873 150.090 1.00 42.93  ? 1265 GLY   A CA  1 
ATOM   10982 C  C   . GLY   B 2 1265 ? 128.899 117.078 148.615 1.00 48.19  ? 1265 GLY   A C   1 
ATOM   10983 O  O   . GLY   B 2 1265 ? 128.019 116.762 147.811 1.00 53.91  ? 1265 GLY   A O   1 
ATOM   10984 N  N   . TRP   B 2 1266 ? 130.062 117.607 148.232 1.00 48.01  ? 1266 TRP   A N   1 
ATOM   10985 C  CA  . TRP   B 2 1266 ? 130.306 117.776 146.801 1.00 43.43  ? 1266 TRP   A CA  1 
ATOM   10986 C  C   . TRP   B 2 1266 ? 130.316 116.448 146.041 1.00 48.91  ? 1266 TRP   A C   1 
ATOM   10987 O  O   . TRP   B 2 1266 ? 129.718 116.397 144.951 1.00 52.78  ? 1266 TRP   A O   1 
ATOM   10988 C  CB  . TRP   B 2 1266 ? 131.573 118.618 146.559 1.00 44.41  ? 1266 TRP   A CB  1 
ATOM   10989 C  CG  . TRP   B 2 1266 ? 132.902 117.926 146.578 1.00 46.47  ? 1266 TRP   A CG  1 
ATOM   10990 C  CD1 . TRP   B 2 1266 ? 133.820 117.951 147.584 1.00 45.81  ? 1266 TRP   A CD1 1 
ATOM   10991 C  CD2 . TRP   B 2 1266 ? 133.480 117.138 145.529 1.00 48.22  ? 1266 TRP   A CD2 1 
ATOM   10992 N  NE1 . TRP   B 2 1266 ? 134.924 117.215 147.237 1.00 47.79  ? 1266 TRP   A NE1 1 
ATOM   10993 C  CE2 . TRP   B 2 1266 ? 134.740 116.704 145.980 1.00 47.13  ? 1266 TRP   A CE2 1 
ATOM   10994 C  CE3 . TRP   B 2 1266 ? 133.048 116.747 144.259 1.00 47.48  ? 1266 TRP   A CE3 1 
ATOM   10995 C  CZ2 . TRP   B 2 1266 ? 135.572 115.900 145.208 1.00 50.03  ? 1266 TRP   A CZ2 1 
ATOM   10996 C  CZ3 . TRP   B 2 1266 ? 133.875 115.949 143.496 1.00 46.42  ? 1266 TRP   A CZ3 1 
ATOM   10997 C  CH2 . TRP   B 2 1266 ? 135.122 115.535 143.971 1.00 50.77  ? 1266 TRP   A CH2 1 
ATOM   10998 N  N   . PRO   B 2 1267 ? 130.914 115.354 146.537 1.00 38.70  ? 1267 PRO   A N   1 
ATOM   10999 C  CA  . PRO   B 2 1267 ? 130.817 114.097 145.775 1.00 36.20  ? 1267 PRO   A CA  1 
ATOM   11000 C  C   . PRO   B 2 1267 ? 129.412 113.525 145.740 1.00 40.23  ? 1267 PRO   A C   1 
ATOM   11001 O  O   . PRO   B 2 1267 ? 128.976 113.031 144.692 1.00 43.07  ? 1267 PRO   A O   1 
ATOM   11002 C  CB  . PRO   B 2 1267 ? 131.788 113.162 146.513 1.00 35.32  ? 1267 PRO   A CB  1 
ATOM   11003 C  CG  . PRO   B 2 1267 ? 132.620 114.043 147.356 1.00 38.74  ? 1267 PRO   A CG  1 
ATOM   11004 C  CD  . PRO   B 2 1267 ? 131.728 115.162 147.747 1.00 36.53  ? 1267 PRO   A CD  1 
ATOM   11005 N  N   . PHE   B 2 1268 ? 128.696 113.563 146.864 1.00 42.82  ? 1268 PHE   A N   1 
ATOM   11006 C  CA  . PHE   B 2 1268 ? 127.321 113.078 146.882 1.00 41.80  ? 1268 PHE   A CA  1 
ATOM   11007 C  C   . PHE   B 2 1268 ? 126.446 113.894 145.947 1.00 36.51  ? 1268 PHE   A C   1 
ATOM   11008 O  O   . PHE   B 2 1268 ? 125.624 113.340 145.207 1.00 49.26  ? 1268 PHE   A O   1 
ATOM   11009 C  CB  . PHE   B 2 1268 ? 126.768 113.127 148.306 1.00 42.10  ? 1268 PHE   A CB  1 
ATOM   11010 C  CG  . PHE   B 2 1268 ? 125.318 112.756 148.409 1.00 40.26  ? 1268 PHE   A CG  1 
ATOM   11011 C  CD1 . PHE   B 2 1268 ? 124.937 111.434 148.527 1.00 44.17  ? 1268 PHE   A CD1 1 
ATOM   11012 C  CD2 . PHE   B 2 1268 ? 124.337 113.729 148.400 1.00 43.35  ? 1268 PHE   A CD2 1 
ATOM   11013 C  CE1 . PHE   B 2 1268 ? 123.607 111.090 148.625 1.00 42.49  ? 1268 PHE   A CE1 1 
ATOM   11014 C  CE2 . PHE   B 2 1268 ? 123.006 113.388 148.497 1.00 44.68  ? 1268 PHE   A CE2 1 
ATOM   11015 C  CZ  . PHE   B 2 1268 ? 122.642 112.068 148.611 1.00 42.82  ? 1268 PHE   A CZ  1 
ATOM   11016 N  N   . VAL   B 2 1269 ? 126.609 115.216 145.971 1.00 42.38  ? 1269 VAL   A N   1 
ATOM   11017 C  CA  . VAL   B 2 1269 ? 125.849 116.082 145.078 1.00 38.79  ? 1269 VAL   A CA  1 
ATOM   11018 C  C   . VAL   B 2 1269 ? 126.157 115.744 143.627 1.00 43.17  ? 1269 VAL   A C   1 
ATOM   11019 O  O   . VAL   B 2 1269 ? 125.249 115.635 142.795 1.00 51.61  ? 1269 VAL   A O   1 
ATOM   11020 C  CB  . VAL   B 2 1269 ? 126.141 117.558 145.407 1.00 40.79  ? 1269 VAL   A CB  1 
ATOM   11021 C  CG1 . VAL   B 2 1269 ? 126.206 118.393 144.152 1.00 44.17  ? 1269 VAL   A CG1 1 
ATOM   11022 C  CG2 . VAL   B 2 1269 ? 125.093 118.100 146.361 1.00 39.13  ? 1269 VAL   A CG2 1 
ATOM   11023 N  N   . THR   B 2 1270 ? 127.438 115.539 143.308 1.00 38.16  ? 1270 THR   A N   1 
ATOM   11024 C  CA  . THR   B 2 1270 ? 127.819 115.200 141.941 1.00 37.30  ? 1270 THR   A CA  1 
ATOM   11025 C  C   . THR   B 2 1270 ? 127.178 113.891 141.497 1.00 38.72  ? 1270 THR   A C   1 
ATOM   11026 O  O   . THR   B 2 1270 ? 126.575 113.812 140.417 1.00 42.35  ? 1270 THR   A O   1 
ATOM   11027 C  CB  . THR   B 2 1270 ? 129.341 115.118 141.840 1.00 36.39  ? 1270 THR   A CB  1 
ATOM   11028 O  OG1 . THR   B 2 1270 ? 129.920 116.300 142.404 1.00 50.58  ? 1270 THR   A OG1 1 
ATOM   11029 C  CG2 . THR   B 2 1270 ? 129.773 115.000 140.397 1.00 42.84  ? 1270 THR   A CG2 1 
ATOM   11030 N  N   . ILE   B 2 1271 ? 127.278 112.856 142.333 1.00 41.74  ? 1271 ILE   A N   1 
ATOM   11031 C  CA  . ILE   B 2 1271 ? 126.762 111.542 141.960 1.00 28.59  ? 1271 ILE   A CA  1 
ATOM   11032 C  C   . ILE   B 2 1271 ? 125.249 111.583 141.800 1.00 38.81  ? 1271 ILE   A C   1 
ATOM   11033 O  O   . ILE   B 2 1271 ? 124.701 111.039 140.835 1.00 46.85  ? 1271 ILE   A O   1 
ATOM   11034 C  CB  . ILE   B 2 1271 ? 127.195 110.484 142.990 1.00 34.79  ? 1271 ILE   A CB  1 
ATOM   11035 C  CG1 . ILE   B 2 1271 ? 128.710 110.296 142.957 1.00 41.08  ? 1271 ILE   A CG1 1 
ATOM   11036 C  CG2 . ILE   B 2 1271 ? 126.494 109.167 142.723 1.00 42.64  ? 1271 ILE   A CG2 1 
ATOM   11037 C  CD1 . ILE   B 2 1271 ? 129.237 109.827 141.623 1.00 47.09  ? 1271 ILE   A CD1 1 
ATOM   11038 N  N   . ILE   B 2 1272 ? 124.549 112.224 142.737 1.00 39.57  ? 1272 ILE   A N   1 
ATOM   11039 C  CA  . ILE   B 2 1272 ? 123.092 112.250 142.674 1.00 30.66  ? 1272 ILE   A CA  1 
ATOM   11040 C  C   . ILE   B 2 1272 ? 122.617 113.088 141.494 1.00 36.37  ? 1272 ILE   A C   1 
ATOM   11041 O  O   . ILE   B 2 1272 ? 121.620 112.754 140.843 1.00 46.18  ? 1272 ILE   A O   1 
ATOM   11042 C  CB  . ILE   B 2 1272 ? 122.509 112.747 144.008 1.00 34.02  ? 1272 ILE   A CB  1 
ATOM   11043 C  CG1 . ILE   B 2 1272 ? 122.857 111.765 145.124 1.00 38.21  ? 1272 ILE   A CG1 1 
ATOM   11044 C  CG2 . ILE   B 2 1272 ? 121.005 112.906 143.915 1.00 38.41  ? 1272 ILE   A CG2 1 
ATOM   11045 C  CD1 . ILE   B 2 1272 ? 122.377 110.360 144.866 1.00 38.10  ? 1272 ILE   A CD1 1 
ATOM   11046 N  N   . ALA   B 2 1273 ? 123.320 114.180 141.187 1.00 31.89  ? 1273 ALA   A N   1 
ATOM   11047 C  CA  . ALA   B 2 1273 ? 122.931 114.999 140.047 1.00 31.64  ? 1273 ALA   A CA  1 
ATOM   11048 C  C   . ALA   B 2 1273 ? 123.155 114.264 138.733 1.00 36.00  ? 1273 ALA   A C   1 
ATOM   11049 O  O   . ALA   B 2 1273 ? 122.345 114.384 137.807 1.00 37.47  ? 1273 ALA   A O   1 
ATOM   11050 C  CB  . ALA   B 2 1273 ? 123.699 116.318 140.065 1.00 37.91  ? 1273 ALA   A CB  1 
ATOM   11051 N  N   . LEU   B 2 1274 ? 124.240 113.497 138.628 1.00 41.49  ? 1274 LEU   A N   1 
ATOM   11052 C  CA  . LEU   B 2 1274 ? 124.578 112.877 137.355 1.00 29.36  ? 1274 LEU   A CA  1 
ATOM   11053 C  C   . LEU   B 2 1274 ? 124.024 111.469 137.183 1.00 30.62  ? 1274 LEU   A C   1 
ATOM   11054 O  O   . LEU   B 2 1274 ? 124.121 110.920 136.081 1.00 44.56  ? 1274 LEU   A O   1 
ATOM   11055 C  CB  . LEU   B 2 1274 ? 126.095 112.841 137.184 1.00 37.17  ? 1274 LEU   A CB  1 
ATOM   11056 C  CG  . LEU   B 2 1274 ? 126.761 114.211 137.189 1.00 39.01  ? 1274 LEU   A CG  1 
ATOM   11057 C  CD1 . LEU   B 2 1274 ? 128.247 114.034 137.307 1.00 40.67  ? 1274 LEU   A CD1 1 
ATOM   11058 C  CD2 . LEU   B 2 1274 ? 126.410 114.979 135.933 1.00 41.90  ? 1274 LEU   A CD2 1 
ATOM   11059 N  N   . LEU   B 2 1275 ? 123.461 110.870 138.229 1.00 26.06  ? 1275 LEU   A N   1 
ATOM   11060 C  CA  . LEU   B 2 1275 ? 122.929 109.515 138.093 1.00 27.84  ? 1275 LEU   A CA  1 
ATOM   11061 C  C   . LEU   B 2 1275 ? 121.777 109.422 137.099 1.00 41.16  ? 1275 LEU   A C   1 
ATOM   11062 O  O   . LEU   B 2 1275 ? 121.795 108.506 136.255 1.00 50.14  ? 1275 LEU   A O   1 
ATOM   11063 C  CB  . LEU   B 2 1275 ? 122.529 108.983 139.472 1.00 31.86  ? 1275 LEU   A CB  1 
ATOM   11064 C  CG  . LEU   B 2 1275 ? 122.282 107.481 139.556 1.00 38.04  ? 1275 LEU   A CG  1 
ATOM   11065 C  CD1 . LEU   B 2 1275 ? 123.560 106.732 139.236 1.00 45.14  ? 1275 LEU   A CD1 1 
ATOM   11066 C  CD2 . LEU   B 2 1275 ? 121.760 107.101 140.926 1.00 39.18  ? 1275 LEU   A CD2 1 
ATOM   11067 N  N   . PRO   B 2 1276 ? 120.753 110.288 137.140 1.00 37.27  ? 1276 PRO   A N   1 
ATOM   11068 C  CA  . PRO   B 2 1276 ? 119.688 110.179 136.131 1.00 30.87  ? 1276 PRO   A CA  1 
ATOM   11069 C  C   . PRO   B 2 1276 ? 120.188 110.304 134.705 1.00 34.60  ? 1276 PRO   A C   1 
ATOM   11070 O  O   . PRO   B 2 1276 ? 119.710 109.579 133.829 1.00 44.28  ? 1276 PRO   A O   1 
ATOM   11071 C  CB  . PRO   B 2 1276 ? 118.742 111.326 136.502 1.00 36.43  ? 1276 PRO   A CB  1 
ATOM   11072 C  CG  . PRO   B 2 1276 ? 118.975 111.548 137.938 1.00 38.17  ? 1276 PRO   A CG  1 
ATOM   11073 C  CD  . PRO   B 2 1276 ? 120.436 111.327 138.135 1.00 41.57  ? 1276 PRO   A CD  1 
ATOM   11074 N  N   . ARG   B 2 1277 ? 121.145 111.197 134.447 1.00 35.41  ? 1277 ARG   A N   1 
ATOM   11075 C  CA  . ARG   B 2 1277 ? 121.670 111.340 133.093 1.00 34.12  ? 1277 ARG   A CA  1 
ATOM   11076 C  C   . ARG   B 2 1277 ? 122.396 110.080 132.646 1.00 38.96  ? 1277 ARG   A C   1 
ATOM   11077 O  O   . ARG   B 2 1277 ? 122.224 109.625 131.510 1.00 51.16  ? 1277 ARG   A O   1 
ATOM   11078 C  CB  . ARG   B 2 1277 ? 122.601 112.548 133.015 1.00 39.97  ? 1277 ARG   A CB  1 
ATOM   11079 C  CG  . ARG   B 2 1277 ? 123.261 112.730 131.662 1.00 41.96  ? 1277 ARG   A CG  1 
ATOM   11080 C  CD  . ARG   B 2 1277 ? 122.226 112.845 130.561 1.00 42.78  ? 1277 ARG   A CD  1 
ATOM   11081 N  NE  . ARG   B 2 1277 ? 122.834 113.108 129.264 1.00 52.15  ? 1277 ARG   A NE  1 
ATOM   11082 C  CZ  . ARG   B 2 1277 ? 122.174 113.104 128.115 1.00 50.57  ? 1277 ARG   A CZ  1 
ATOM   11083 N  NH1 . ARG   B 2 1277 ? 120.880 112.840 128.063 1.00 41.82  ? 1277 ARG   A NH1 1 
ATOM   11084 N  NH2 . ARG   B 2 1277 ? 122.831 113.367 126.989 1.00 51.85  ? 1277 ARG   A NH2 1 
ATOM   11085 N  N   . TYR   B 2 1278 ? 123.207 109.502 133.531 1.00 33.71  ? 1278 TYR   A N   1 
ATOM   11086 C  CA  . TYR   B 2 1278 ? 123.926 108.275 133.207 1.00 30.88  ? 1278 TYR   A CA  1 
ATOM   11087 C  C   . TYR   B 2 1278 ? 122.956 107.144 132.887 1.00 33.91  ? 1278 TYR   A C   1 
ATOM   11088 O  O   . TYR   B 2 1278 ? 123.095 106.455 131.866 1.00 46.02  ? 1278 TYR   A O   1 
ATOM   11089 C  CB  . TYR   B 2 1278 ? 124.840 107.912 134.378 1.00 28.73  ? 1278 TYR   A CB  1 
ATOM   11090 C  CG  . TYR   B 2 1278 ? 125.770 106.746 134.157 1.00 30.02  ? 1278 TYR   A CG  1 
ATOM   11091 C  CD1 . TYR   B 2 1278 ? 126.727 106.774 133.154 1.00 41.56  ? 1278 TYR   A CD1 1 
ATOM   11092 C  CD2 . TYR   B 2 1278 ? 125.715 105.632 134.979 1.00 32.09  ? 1278 TYR   A CD2 1 
ATOM   11093 C  CE1 . TYR   B 2 1278 ? 127.586 105.711 132.962 1.00 48.19  ? 1278 TYR   A CE1 1 
ATOM   11094 C  CE2 . TYR   B 2 1278 ? 126.567 104.568 134.796 1.00 37.24  ? 1278 TYR   A CE2 1 
ATOM   11095 C  CZ  . TYR   B 2 1278 ? 127.502 104.611 133.787 1.00 48.08  ? 1278 TYR   A CZ  1 
ATOM   11096 O  OH  . TYR   B 2 1278 ? 128.355 103.547 133.603 1.00 50.28  ? 1278 TYR   A OH  1 
ATOM   11097 N  N   . LEU   B 2 1279 ? 121.944 106.960 133.738 1.00 32.80  ? 1279 LEU   A N   1 
ATOM   11098 C  CA  . LEU   B 2 1279 ? 120.980 105.888 133.514 1.00 33.67  ? 1279 LEU   A CA  1 
ATOM   11099 C  C   . LEU   B 2 1279 ? 120.166 106.125 132.248 1.00 45.10  ? 1279 LEU   A C   1 
ATOM   11100 O  O   . LEU   B 2 1279 ? 119.911 105.188 131.482 1.00 48.80  ? 1279 LEU   A O   1 
ATOM   11101 C  CB  . LEU   B 2 1279 ? 120.066 105.745 134.728 1.00 37.11  ? 1279 LEU   A CB  1 
ATOM   11102 C  CG  . LEU   B 2 1279 ? 120.743 105.269 136.013 1.00 35.90  ? 1279 LEU   A CG  1 
ATOM   11103 C  CD1 . LEU   B 2 1279 ? 119.730 105.146 137.131 1.00 40.21  ? 1279 LEU   A CD1 1 
ATOM   11104 C  CD2 . LEU   B 2 1279 ? 121.449 103.950 135.789 1.00 42.10  ? 1279 LEU   A CD2 1 
ATOM   11105 N  N   . ILE   B 2 1280 ? 119.750 107.372 132.009 1.00 46.61  ? 1280 ILE   A N   1 
ATOM   11106 C  CA  . ILE   B 2 1280 ? 118.976 107.691 130.814 1.00 36.27  ? 1280 ILE   A CA  1 
ATOM   11107 C  C   . ILE   B 2 1280 ? 119.793 107.415 129.563 1.00 42.16  ? 1280 ILE   A C   1 
ATOM   11108 O  O   . ILE   B 2 1280 ? 119.293 106.825 128.601 1.00 56.97  ? 1280 ILE   A O   1 
ATOM   11109 C  CB  . ILE   B 2 1280 ? 118.494 109.153 130.863 1.00 36.06  ? 1280 ILE   A CB  1 
ATOM   11110 C  CG1 . ILE   B 2 1280 ? 117.291 109.291 131.794 1.00 45.12  ? 1280 ILE   A CG1 1 
ATOM   11111 C  CG2 . ILE   B 2 1280 ? 118.151 109.652 129.475 1.00 41.64  ? 1280 ILE   A CG2 1 
ATOM   11112 C  CD1 . ILE   B 2 1280 ? 116.766 110.702 131.898 1.00 46.31  ? 1280 ILE   A CD1 1 
ATOM   11113 N  N   . LYS   B 2 1281 ? 121.059 107.831 129.554 1.00 36.52  ? 1281 LYS   A N   1 
ATOM   11114 C  CA  . LYS   B 2 1281 ? 121.901 107.607 128.386 1.00 42.67  ? 1281 LYS   A CA  1 
ATOM   11115 C  C   . LYS   B 2 1281 ? 122.097 106.118 128.134 1.00 49.59  ? 1281 LYS   A C   1 
ATOM   11116 O  O   . LYS   B 2 1281 ? 121.956 105.645 126.998 1.00 62.11  ? 1281 LYS   A O   1 
ATOM   11117 C  CB  . LYS   B 2 1281 ? 123.243 108.312 128.573 1.00 41.63  ? 1281 LYS   A CB  1 
ATOM   11118 C  CG  . LYS   B 2 1281 ? 124.043 108.459 127.302 1.00 46.84  ? 1281 LYS   A CG  1 
ATOM   11119 C  CD  . LYS   B 2 1281 ? 125.211 109.400 127.498 1.00 51.17  ? 1281 LYS   A CD  1 
ATOM   11120 C  CE  . LYS   B 2 1281 ? 125.925 109.653 126.182 1.00 56.82  ? 1281 LYS   A CE  1 
ATOM   11121 N  NZ  . LYS   B 2 1281 ? 126.430 108.391 125.574 1.00 53.29  ? 1281 LYS   A NZ  1 
ATOM   11122 N  N   . THR   B 2 1282 ? 122.394 105.355 129.190 1.00 48.81  ? 1282 THR   A N   1 
ATOM   11123 C  CA  . THR   B 2 1282 ? 122.601 103.920 129.024 1.00 49.34  ? 1282 THR   A CA  1 
ATOM   11124 C  C   . THR   B 2 1282 ? 121.344 103.234 128.499 1.00 53.10  ? 1282 THR   A C   1 
ATOM   11125 O  O   . THR   B 2 1282 ? 121.402 102.450 127.543 1.00 59.96  ? 1282 THR   A O   1 
ATOM   11126 C  CB  . THR   B 2 1282 ? 123.040 103.297 130.348 1.00 54.31  ? 1282 THR   A CB  1 
ATOM   11127 O  OG1 . THR   B 2 1282 ? 124.344 103.775 130.692 1.00 59.54  ? 1282 THR   A OG1 1 
ATOM   11128 C  CG2 . THR   B 2 1282 ? 123.072 101.781 130.238 1.00 60.12  ? 1282 THR   A CG2 1 
ATOM   11129 N  N   . PHE   B 2 1283 ? 120.191 103.530 129.100 1.00 54.31  ? 1283 PHE   A N   1 
ATOM   11130 C  CA  . PHE   B 2 1283 ? 118.965 102.853 128.697 1.00 55.78  ? 1283 PHE   A CA  1 
ATOM   11131 C  C   . PHE   B 2 1283 ? 118.491 103.301 127.322 1.00 55.28  ? 1283 PHE   A C   1 
ATOM   11132 O  O   . PHE   B 2 1283 ? 117.910 102.501 126.584 1.00 63.24  ? 1283 PHE   A O   1 
ATOM   11133 C  CB  . PHE   B 2 1283 ? 117.874 103.074 129.741 1.00 62.19  ? 1283 PHE   A CB  1 
ATOM   11134 C  CG  . PHE   B 2 1283 ? 118.123 102.350 131.032 1.00 63.55  ? 1283 PHE   A CG  1 
ATOM   11135 C  CD1 . PHE   B 2 1283 ? 119.032 101.305 131.090 1.00 58.39  ? 1283 PHE   A CD1 1 
ATOM   11136 C  CD2 . PHE   B 2 1283 ? 117.449 102.711 132.187 1.00 63.88  ? 1283 PHE   A CD2 1 
ATOM   11137 C  CE1 . PHE   B 2 1283 ? 119.265 100.637 132.272 1.00 59.90  ? 1283 PHE   A CE1 1 
ATOM   11138 C  CE2 . PHE   B 2 1283 ? 117.678 102.045 133.375 1.00 62.98  ? 1283 PHE   A CE2 1 
ATOM   11139 C  CZ  . PHE   B 2 1283 ? 118.588 101.006 133.417 1.00 61.94  ? 1283 PHE   A CZ  1 
ATOM   11140 N  N   . ARG   B 2 1284 ? 118.722 104.561 126.955 1.00 54.32  ? 1284 ARG   A N   1 
ATOM   11141 C  CA  . ARG   B 2 1284 ? 118.384 105.004 125.610 1.00 56.64  ? 1284 ARG   A CA  1 
ATOM   11142 C  C   . ARG   B 2 1284 ? 119.264 104.320 124.574 1.00 61.75  ? 1284 ARG   A C   1 
ATOM   11143 O  O   . ARG   B 2 1284 ? 118.782 103.931 123.505 1.00 63.45  ? 1284 ARG   A O   1 
ATOM   11144 C  CB  . ARG   B 2 1284 ? 118.515 106.523 125.507 1.00 57.87  ? 1284 ARG   A CB  1 
ATOM   11145 C  CG  . ARG   B 2 1284 ? 117.846 107.117 124.285 1.00 61.94  ? 1284 ARG   A CG  1 
ATOM   11146 C  CD  . ARG   B 2 1284 ? 118.277 108.554 124.059 1.00 63.66  ? 1284 ARG   A CD  1 
ATOM   11147 N  NE  . ARG   B 2 1284 ? 119.675 108.643 123.654 1.00 70.22  ? 1284 ARG   A NE  1 
ATOM   11148 C  CZ  . ARG   B 2 1284 ? 120.101 108.518 122.404 1.00 69.04  ? 1284 ARG   A CZ  1 
ATOM   11149 N  NH1 . ARG   B 2 1284 ? 119.261 108.295 121.407 1.00 64.69  ? 1284 ARG   A NH1 1 
ATOM   11150 N  NH2 . ARG   B 2 1284 ? 121.402 108.619 122.149 1.00 66.07  ? 1284 ARG   A NH2 1 
ATOM   11151 N  N   . GLN   B 2 1285 ? 120.555 104.155 124.872 1.00 62.37  ? 1285 GLN   A N   1 
ATOM   11152 C  CA  . GLN   B 2 1285 ? 121.438 103.493 123.921 1.00 59.62  ? 1285 GLN   A CA  1 
ATOM   11153 C  C   . GLN   B 2 1285 ? 121.201 101.991 123.847 1.00 61.68  ? 1285 GLN   A C   1 
ATOM   11154 O  O   . GLN   B 2 1285 ? 121.503 101.384 122.815 1.00 66.66  ? 1285 GLN   A O   1 
ATOM   11155 C  CB  . GLN   B 2 1285 ? 122.899 103.770 124.273 1.00 62.23  ? 1285 GLN   A CB  1 
ATOM   11156 C  CG  . GLN   B 2 1285 ? 123.314 105.218 124.079 1.00 68.16  ? 1285 GLN   A CG  1 
ATOM   11157 C  CD  . GLN   B 2 1285 ? 124.783 105.446 124.366 1.00 68.72  ? 1285 GLN   A CD  1 
ATOM   11158 O  OE1 . GLN   B 2 1285 ? 125.283 106.565 124.251 1.00 66.00  ? 1285 GLN   A OE1 1 
ATOM   11159 N  NE2 . GLN   B 2 1285 ? 125.485 104.383 124.742 1.00 66.27  ? 1285 GLN   A NE2 1 
ATOM   11160 N  N   . ASN   B 2 1286 ? 120.673 101.376 124.907 1.00 69.60  ? 1286 ASN   A N   1 
ATOM   11161 C  CA  . ASN   B 2 1286 ? 120.485 99.931  124.920 1.00 69.84  ? 1286 ASN   A CA  1 
ATOM   11162 C  C   . ASN   B 2 1286 ? 119.050 99.475  124.687 1.00 72.29  ? 1286 ASN   A C   1 
ATOM   11163 O  O   . ASN   B 2 1286 ? 118.825 98.268  124.548 1.00 75.10  ? 1286 ASN   A O   1 
ATOM   11164 C  CB  . ASN   B 2 1286 ? 120.984 99.346  126.247 1.00 67.41  ? 1286 ASN   A CB  1 
ATOM   11165 C  CG  . ASN   B 2 1286 ? 122.491 99.360  126.354 1.00 75.58  ? 1286 ASN   A CG  1 
ATOM   11166 O  OD1 . ASN   B 2 1286 ? 123.076 100.263 126.951 1.00 76.89  ? 1286 ASN   A OD1 1 
ATOM   11167 N  ND2 . ASN   B 2 1286 ? 123.134 98.356  125.769 1.00 78.18  ? 1286 ASN   A ND2 1 
ATOM   11168 N  N   . ILE   B 2 1287 ? 118.077 100.385 124.640 1.00 60.75  ? 1287 ILE   A N   1 
ATOM   11169 C  CA  . ILE   B 2 1287 ? 116.673 100.030 124.471 1.00 55.04  ? 1287 ILE   A CA  1 
ATOM   11170 C  C   . ILE   B 2 1287 ? 116.063 100.712 123.251 1.00 59.28  ? 1287 ILE   A C   1 
ATOM   11171 O  O   . ILE   B 2 1287 ? 115.404 100.066 122.430 1.00 66.28  ? 1287 ILE   A O   1 
ATOM   11172 C  CB  . ILE   B 2 1287 ? 115.853 100.345 125.743 1.00 65.37  ? 1287 ILE   A CB  1 
ATOM   11173 C  CG1 . ILE   B 2 1287 ? 116.105 99.290  126.825 1.00 66.10  ? 1287 ILE   A CG1 1 
ATOM   11174 C  CG2 . ILE   B 2 1287 ? 114.373 100.403 125.424 1.00 68.01  ? 1287 ILE   A CG2 1 
ATOM   11175 C  CD1 . ILE   B 2 1287 ? 117.332 99.536  127.677 1.00 64.80  ? 1287 ILE   A CD1 1 
ATOM   11176 N  N   . PHE   B 2 1288 ? 116.276 102.023 123.110 1.00 68.99  ? 1288 PHE   A N   1 
ATOM   11177 C  CA  . PHE   B 2 1288 ? 115.759 102.802 121.985 1.00 68.77  ? 1288 PHE   A CA  1 
ATOM   11178 C  C   . PHE   B 2 1288 ? 116.938 103.370 121.202 1.00 68.85  ? 1288 PHE   A C   1 
ATOM   11179 O  O   . PHE   B 2 1288 ? 117.198 104.582 121.247 1.00 66.13  ? 1288 PHE   A O   1 
ATOM   11180 C  CB  . PHE   B 2 1288 ? 114.831 103.920 122.456 1.00 65.76  ? 1288 PHE   A CB  1 
ATOM   11181 C  CG  . PHE   B 2 1288 ? 113.578 103.430 123.118 1.00 68.67  ? 1288 PHE   A CG  1 
ATOM   11182 C  CD1 . PHE   B 2 1288 ? 112.598 102.783 122.384 1.00 72.45  ? 1288 PHE   A CD1 1 
ATOM   11183 C  CD2 . PHE   B 2 1288 ? 113.371 103.628 124.472 1.00 68.99  ? 1288 PHE   A CD2 1 
ATOM   11184 C  CE1 . PHE   B 2 1288 ? 111.441 102.332 122.989 1.00 72.39  ? 1288 PHE   A CE1 1 
ATOM   11185 C  CE2 . PHE   B 2 1288 ? 112.216 103.182 125.083 1.00 72.44  ? 1288 PHE   A CE2 1 
ATOM   11186 C  CZ  . PHE   B 2 1288 ? 111.250 102.533 124.341 1.00 74.15  ? 1288 PHE   A CZ  1 
ATOM   11187 N  N   . PRO   B 2 1289 ? 117.662 102.534 120.465 1.00 71.19  ? 1289 PRO   A N   1 
ATOM   11188 C  CA  . PRO   B 2 1289 ? 118.896 102.984 119.823 1.00 70.64  ? 1289 PRO   A CA  1 
ATOM   11189 C  C   . PRO   B 2 1289 ? 118.681 103.533 118.423 1.00 74.98  ? 1289 PRO   A C   1 
ATOM   11190 O  O   . PRO   B 2 1289 ? 117.855 103.052 117.645 1.00 72.18  ? 1289 PRO   A O   1 
ATOM   11191 C  CB  . PRO   B 2 1289 ? 119.740 101.702 119.783 1.00 62.55  ? 1289 PRO   A CB  1 
ATOM   11192 C  CG  . PRO   B 2 1289 ? 118.733 100.563 119.816 1.00 69.07  ? 1289 PRO   A CG  1 
ATOM   11193 C  CD  . PRO   B 2 1289 ? 117.367 101.133 120.126 1.00 71.26  ? 1289 PRO   A CD  1 
ATOM   11194 N  N   . ASN   B 2 1290 ? 119.453 104.567 118.113 1.00 73.27  ? 1290 ASN   A N   1 
ATOM   11195 C  CA  . ASN   B 2 1290 ? 119.459 105.167 116.791 1.00 65.11  ? 1290 ASN   A CA  1 
ATOM   11196 C  C   . ASN   B 2 1290 ? 120.355 104.364 115.854 1.00 68.44  ? 1290 ASN   A C   1 
ATOM   11197 O  O   . ASN   B 2 1290 ? 121.069 103.447 116.264 1.00 75.57  ? 1290 ASN   A O   1 
ATOM   11198 C  CB  . ASN   B 2 1290 ? 119.933 106.617 116.865 1.00 63.63  ? 1290 ASN   A CB  1 
ATOM   11199 C  CG  . ASN   B 2 1290 ? 119.090 107.458 117.799 1.00 71.27  ? 1290 ASN   A CG  1 
ATOM   11200 O  OD1 . ASN   B 2 1290 ? 118.377 106.933 118.654 1.00 74.36  ? 1290 ASN   A OD1 1 
ATOM   11201 N  ND2 . ASN   B 2 1290 ? 119.168 108.773 117.641 1.00 69.57  ? 1290 ASN   A ND2 1 
ATOM   11202 N  N   . ASP   B 2 1291 ? 120.303 104.718 114.570 1.00 61.01  ? 1291 ASP   A N   1 
ATOM   11203 C  CA  . ASP   B 2 1291 ? 121.200 104.095 113.604 1.00 58.21  ? 1291 ASP   A CA  1 
ATOM   11204 C  C   . ASP   B 2 1291 ? 122.652 104.447 113.897 1.00 58.44  ? 1291 ASP   A C   1 
ATOM   11205 O  O   . ASP   B 2 1291 ? 123.539 103.595 113.776 1.00 61.81  ? 1291 ASP   A O   1 
ATOM   11206 C  CB  . ASP   B 2 1291 ? 120.819 104.516 112.187 1.00 62.44  ? 1291 ASP   A CB  1 
ATOM   11207 C  CG  . ASP   B 2 1291 ? 119.438 104.040 111.791 1.00 66.95  ? 1291 ASP   A CG  1 
ATOM   11208 O  OD1 . ASP   B 2 1291 ? 118.991 103.005 112.325 1.00 65.91  ? 1291 ASP   A OD1 1 
ATOM   11209 O  OD2 . ASP   B 2 1291 ? 118.800 104.699 110.944 1.00 68.36  ? 1291 ASP   A OD2 1 
ATOM   11210 N  N   . VAL   B 2 1292 ? 122.911 105.696 114.286 1.00 57.17  ? 1292 VAL   A N   1 
ATOM   11211 C  CA  . VAL   B 2 1292 ? 124.278 106.127 114.562 1.00 55.67  ? 1292 VAL   A CA  1 
ATOM   11212 C  C   . VAL   B 2 1292 ? 124.845 105.389 115.768 1.00 56.33  ? 1292 VAL   A C   1 
ATOM   11213 O  O   . VAL   B 2 1292 ? 125.995 104.938 115.750 1.00 65.01  ? 1292 VAL   A O   1 
ATOM   11214 C  CB  . VAL   B 2 1292 ? 124.328 107.653 114.753 1.00 58.10  ? 1292 VAL   A CB  1 
ATOM   11215 C  CG1 . VAL   B 2 1292 ? 125.744 108.101 115.058 1.00 57.40  ? 1292 VAL   A CG1 1 
ATOM   11216 C  CG2 . VAL   B 2 1292 ? 123.808 108.356 113.514 1.00 58.31  ? 1292 VAL   A CG2 1 
ATOM   11217 N  N   . ASP   B 2 1293 ? 124.054 105.258 116.835 1.00 62.15  ? 1293 ASP   A N   1 
ATOM   11218 C  CA  . ASP   B 2 1293 ? 124.528 104.555 118.025 1.00 63.18  ? 1293 ASP   A CA  1 
ATOM   11219 C  C   . ASP   B 2 1293 ? 124.784 103.082 117.735 1.00 64.29  ? 1293 ASP   A C   1 
ATOM   11220 O  O   . ASP   B 2 1293 ? 125.804 102.519 118.160 1.00 71.16  ? 1293 ASP   A O   1 
ATOM   11221 C  CB  . ASP   B 2 1293 ? 123.516 104.711 119.159 1.00 66.91  ? 1293 ASP   A CB  1 
ATOM   11222 C  CG  . ASP   B 2 1293 ? 123.918 103.952 120.407 1.00 75.12  ? 1293 ASP   A CG  1 
ATOM   11223 O  OD1 . ASP   B 2 1293 ? 124.906 104.354 121.057 1.00 75.04  ? 1293 ASP   A OD1 1 
ATOM   11224 O  OD2 . ASP   B 2 1293 ? 123.244 102.954 120.740 1.00 75.27  ? 1293 ASP   A OD2 1 
ATOM   11225 N  N   . THR   B 2 1294 ? 123.870 102.442 117.006 1.00 52.03  ? 1294 THR   A N   1 
ATOM   11226 C  CA  . THR   B 2 1294 ? 124.051 101.040 116.653 1.00 47.79  ? 1294 THR   A CA  1 
ATOM   11227 C  C   . THR   B 2 1294 ? 125.294 100.848 115.798 1.00 51.43  ? 1294 THR   A C   1 
ATOM   11228 O  O   . THR   B 2 1294 ? 126.067 99.907  116.014 1.00 62.84  ? 1294 THR   A O   1 
ATOM   11229 C  CB  . THR   B 2 1294 ? 122.813 100.523 115.925 1.00 53.95  ? 1294 THR   A CB  1 
ATOM   11230 O  OG1 . THR   B 2 1294 ? 121.676 100.605 116.792 1.00 61.68  ? 1294 THR   A OG1 1 
ATOM   11231 C  CG2 . THR   B 2 1294 ? 123.014 99.090  115.504 1.00 55.71  ? 1294 THR   A CG2 1 
ATOM   11232 N  N   . MET   B 2 1295 ? 125.513 101.738 114.828 1.00 57.35  ? 1295 MET   A N   1 
ATOM   11233 C  CA  . MET   B 2 1295 ? 126.699 101.626 113.990 1.00 51.73  ? 1295 MET   A CA  1 
ATOM   11234 C  C   . MET   B 2 1295 ? 127.973 101.900 114.772 1.00 52.56  ? 1295 MET   A C   1 
ATOM   11235 O  O   . MET   B 2 1295 ? 129.006 101.286 114.495 1.00 65.19  ? 1295 MET   A O   1 
ATOM   11236 C  CB  . MET   B 2 1295 ? 126.591 102.565 112.791 1.00 56.01  ? 1295 MET   A CB  1 
ATOM   11237 C  CG  . MET   B 2 1295 ? 125.852 101.963 111.608 1.00 58.36  ? 1295 MET   A CG  1 
ATOM   11238 S  SD  . MET   B 2 1295 ? 126.646 100.485 110.948 1.00 52.99  ? 1295 MET   A SD  1 
ATOM   11239 C  CE  . MET   B 2 1295 ? 125.653 99.191  111.689 1.00 59.95  ? 1295 MET   A CE  1 
ATOM   11240 N  N   . ARG   B 2 1296 ? 127.926 102.813 115.743 1.00 56.04  ? 1296 ARG   A N   1 
ATOM   11241 C  CA  . ARG   B 2 1296 ? 129.092 103.040 116.588 1.00 56.69  ? 1296 ARG   A CA  1 
ATOM   11242 C  C   . ARG   B 2 1296 ? 129.434 101.789 117.383 1.00 61.59  ? 1296 ARG   A C   1 
ATOM   11243 O  O   . ARG   B 2 1296 ? 130.606 101.407 117.483 1.00 68.41  ? 1296 ARG   A O   1 
ATOM   11244 C  CB  . ARG   B 2 1296 ? 128.844 104.228 117.516 1.00 55.34  ? 1296 ARG   A CB  1 
ATOM   11245 C  CG  . ARG   B 2 1296 ? 130.035 104.604 118.376 1.00 60.64  ? 1296 ARG   A CG  1 
ATOM   11246 C  CD  . ARG   B 2 1296 ? 129.889 105.997 118.971 1.00 63.62  ? 1296 ARG   A CD  1 
ATOM   11247 N  NE  . ARG   B 2 1296 ? 128.686 106.140 119.782 1.00 63.99  ? 1296 ARG   A NE  1 
ATOM   11248 C  CZ  . ARG   B 2 1296 ? 127.593 106.784 119.396 1.00 64.08  ? 1296 ARG   A CZ  1 
ATOM   11249 N  NH1 . ARG   B 2 1296 ? 127.515 107.362 118.209 1.00 63.85  ? 1296 ARG   A NH1 1 
ATOM   11250 N  NH2 . ARG   B 2 1296 ? 126.554 106.851 120.222 1.00 61.92  ? 1296 ARG   A NH2 1 
ATOM   11251 N  N   . LEU   B 2 1297 ? 128.417 101.122 117.933 1.00 60.57  ? 1297 LEU   A N   1 
ATOM   11252 C  CA  . LEU   B 2 1297 ? 128.662 99.865  118.637 1.00 57.72  ? 1297 LEU   A CA  1 
ATOM   11253 C  C   . LEU   B 2 1297 ? 129.219 98.801  117.697 1.00 56.82  ? 1297 LEU   A C   1 
ATOM   11254 O  O   . LEU   B 2 1297 ? 130.143 98.062  118.061 1.00 68.33  ? 1297 LEU   A O   1 
ATOM   11255 C  CB  . LEU   B 2 1297 ? 127.378 99.374  119.302 1.00 59.70  ? 1297 LEU   A CB  1 
ATOM   11256 C  CG  . LEU   B 2 1297 ? 126.833 100.227 120.447 1.00 59.63  ? 1297 LEU   A CG  1 
ATOM   11257 C  CD1 . LEU   B 2 1297 ? 125.565 99.615  121.012 1.00 59.76  ? 1297 LEU   A CD1 1 
ATOM   11258 C  CD2 . LEU   B 2 1297 ? 127.879 100.387 121.532 1.00 62.41  ? 1297 LEU   A CD2 1 
ATOM   11259 N  N   . VAL   B 2 1298 ? 128.673 98.711  116.482 1.00 53.56  ? 1298 VAL   A N   1 
ATOM   11260 C  CA  . VAL   B 2 1298 ? 129.137 97.708  115.523 1.00 55.55  ? 1298 VAL   A CA  1 
ATOM   11261 C  C   . VAL   B 2 1298 ? 130.598 97.948  115.164 1.00 62.10  ? 1298 VAL   A C   1 
ATOM   11262 O  O   . VAL   B 2 1298 ? 131.408 97.014  115.126 1.00 69.69  ? 1298 VAL   A O   1 
ATOM   11263 C  CB  . VAL   B 2 1298 ? 128.241 97.706  114.272 1.00 52.86  ? 1298 VAL   A CB  1 
ATOM   11264 C  CG1 . VAL   B 2 1298 ? 128.869 96.876  113.172 1.00 58.29  ? 1298 VAL   A CG1 1 
ATOM   11265 C  CG2 . VAL   B 2 1298 ? 126.868 97.169  114.610 1.00 59.85  ? 1298 VAL   A CG2 1 
ATOM   11266 N  N   . ARG   B 2 1299 ? 130.958 99.204  114.897 1.00 57.26  ? 1299 ARG   A N   1 
ATOM   11267 C  CA  . ARG   B 2 1299 ? 132.340 99.522  114.559 1.00 54.08  ? 1299 ARG   A CA  1 
ATOM   11268 C  C   . ARG   B 2 1299 ? 133.277 99.290  115.735 1.00 55.26  ? 1299 ARG   A C   1 
ATOM   11269 O  O   . ARG   B 2 1299 ? 134.414 98.848  115.539 1.00 60.17  ? 1299 ARG   A O   1 
ATOM   11270 C  CB  . ARG   B 2 1299 ? 132.449 100.967 114.075 1.00 54.53  ? 1299 ARG   A CB  1 
ATOM   11271 C  CG  . ARG   B 2 1299 ? 131.711 101.254 112.780 1.00 51.79  ? 1299 ARG   A CG  1 
ATOM   11272 C  CD  . ARG   B 2 1299 ? 132.234 100.402 111.640 1.00 56.32  ? 1299 ARG   A CD  1 
ATOM   11273 N  NE  . ARG   B 2 1299 ? 133.664 100.586 111.424 1.00 61.47  ? 1299 ARG   A NE  1 
ATOM   11274 C  CZ  . ARG   B 2 1299 ? 134.191 101.525 110.652 1.00 55.08  ? 1299 ARG   A CZ  1 
ATOM   11275 N  NH1 . ARG   B 2 1299 ? 133.433 102.398 110.011 1.00 59.75  ? 1299 ARG   A NH1 1 
ATOM   11276 N  NH2 . ARG   B 2 1299 ? 135.512 101.591 110.522 1.00 53.75  ? 1299 ARG   A NH2 1 
ATOM   11277 N  N   . LYS   B 2 1300 ? 132.828 99.583  116.958 1.00 62.25  ? 1300 LYS   A N   1 
ATOM   11278 C  CA  . LYS   B 2 1300 ? 133.695 99.400  118.117 1.00 66.25  ? 1300 LYS   A CA  1 
ATOM   11279 C  C   . LYS   B 2 1300 ? 133.936 97.925  118.410 1.00 68.29  ? 1300 LYS   A C   1 
ATOM   11280 O  O   . LYS   B 2 1300 ? 135.065 97.527  118.721 1.00 69.77  ? 1300 LYS   A O   1 
ATOM   11281 C  CB  . LYS   B 2 1300 ? 133.093 100.098 119.335 1.00 68.43  ? 1300 LYS   A CB  1 
ATOM   11282 C  CG  . LYS   B 2 1300 ? 133.960 100.037 120.579 1.00 70.90  ? 1300 LYS   A CG  1 
ATOM   11283 C  CD  . LYS   B 2 1300 ? 133.308 100.779 121.735 1.00 71.44  ? 1300 LYS   A CD  1 
ATOM   11284 C  CE  . LYS   B 2 1300 ? 134.180 100.741 122.979 1.00 70.32  ? 1300 LYS   A CE  1 
ATOM   11285 N  NZ  . LYS   B 2 1300 ? 133.554 101.473 124.115 1.00 69.04  ? 1300 LYS   A NZ  1 
ATOM   11286 N  N   . TYR   B 2 1301 ? 132.897 97.095  118.311 1.00 69.29  ? 1301 TYR   A N   1 
ATOM   11287 C  CA  . TYR   B 2 1301 ? 133.016 95.697  118.702 1.00 68.31  ? 1301 TYR   A CA  1 
ATOM   11288 C  C   . TYR   B 2 1301 ? 133.254 94.746  117.538 1.00 72.03  ? 1301 TYR   A C   1 
ATOM   11289 O  O   . TYR   B 2 1301 ? 133.780 93.650  117.759 1.00 78.87  ? 1301 TYR   A O   1 
ATOM   11290 C  CB  . TYR   B 2 1301 ? 131.766 95.250  119.467 1.00 66.14  ? 1301 TYR   A CB  1 
ATOM   11291 C  CG  . TYR   B 2 1301 ? 131.604 95.941  120.799 1.00 68.47  ? 1301 TYR   A CG  1 
ATOM   11292 C  CD1 . TYR   B 2 1301 ? 132.368 95.565  121.894 1.00 71.26  ? 1301 TYR   A CD1 1 
ATOM   11293 C  CD2 . TYR   B 2 1301 ? 130.691 96.971  120.961 1.00 70.89  ? 1301 TYR   A CD2 1 
ATOM   11294 C  CE1 . TYR   B 2 1301 ? 132.227 96.196  123.113 1.00 73.40  ? 1301 TYR   A CE1 1 
ATOM   11295 C  CE2 . TYR   B 2 1301 ? 130.542 97.607  122.176 1.00 72.28  ? 1301 TYR   A CE2 1 
ATOM   11296 C  CZ  . TYR   B 2 1301 ? 131.313 97.216  123.248 1.00 74.62  ? 1301 TYR   A CZ  1 
ATOM   11297 O  OH  . TYR   B 2 1301 ? 131.166 97.848  124.462 1.00 75.14  ? 1301 TYR   A OH  1 
ATOM   11298 N  N   . HIS   B 2 1302 ? 132.887 95.124  116.317 1.00 70.36  ? 1302 HIS   A N   1 
ATOM   11299 C  CA  . HIS   B 2 1302 ? 133.075 94.280  115.138 1.00 66.03  ? 1302 HIS   A CA  1 
ATOM   11300 C  C   . HIS   B 2 1302 ? 133.756 95.089  114.043 1.00 65.73  ? 1302 HIS   A C   1 
ATOM   11301 O  O   . HIS   B 2 1302 ? 133.134 95.444  113.036 1.00 69.47  ? 1302 HIS   A O   1 
ATOM   11302 C  CB  . HIS   B 2 1302 ? 131.741 93.718  114.645 1.00 67.89  ? 1302 HIS   A CB  1 
ATOM   11303 C  CG  . HIS   B 2 1302 ? 130.988 92.945  115.681 1.00 70.92  ? 1302 HIS   A CG  1 
ATOM   11304 N  ND1 . HIS   B 2 1302 ? 131.613 92.265  116.703 1.00 71.87  ? 1302 HIS   A ND1 1 
ATOM   11305 C  CD2 . HIS   B 2 1302 ? 129.660 92.746  115.853 1.00 72.63  ? 1302 HIS   A CD2 1 
ATOM   11306 C  CE1 . HIS   B 2 1302 ? 130.702 91.679  117.461 1.00 74.00  ? 1302 HIS   A CE1 1 
ATOM   11307 N  NE2 . HIS   B 2 1302 ? 129.509 91.956  116.966 1.00 74.11  ? 1302 HIS   A NE2 1 
ATOM   11308 N  N   . PRO   B 2 1303 ? 135.043 95.402  114.210 1.00 74.79  ? 1303 PRO   A N   1 
ATOM   11309 C  CA  . PRO   B 2 1303 ? 135.750 96.151  113.161 1.00 77.53  ? 1303 PRO   A CA  1 
ATOM   11310 C  C   . PRO   B 2 1303 ? 135.915 95.373  111.868 1.00 81.83  ? 1303 PRO   A C   1 
ATOM   11311 O  O   . PRO   B 2 1303 ? 136.157 95.990  110.822 1.00 82.43  ? 1303 PRO   A O   1 
ATOM   11312 C  CB  . PRO   B 2 1303 ? 137.107 96.460  113.804 1.00 78.66  ? 1303 PRO   A CB  1 
ATOM   11313 C  CG  . PRO   B 2 1303 ? 137.303 95.362  114.790 1.00 80.38  ? 1303 PRO   A CG  1 
ATOM   11314 C  CD  . PRO   B 2 1303 ? 135.935 95.038  115.325 1.00 79.30  ? 1303 PRO   A CD  1 
ATOM   11315 N  N   . GLU   B 2 1304 ? 135.792 94.045  111.902 1.00 85.83  ? 1304 GLU   A N   1 
ATOM   11316 C  CA  . GLU   B 2 1304 ? 135.986 93.232  110.709 1.00 82.80  ? 1304 GLU   A CA  1 
ATOM   11317 C  C   . GLU   B 2 1304 ? 134.826 93.326  109.729 1.00 83.63  ? 1304 GLU   A C   1 
ATOM   11318 O  O   . GLU   B 2 1304 ? 134.962 92.856  108.594 1.00 85.33  ? 1304 GLU   A O   1 
ATOM   11319 C  CB  . GLU   B 2 1304 ? 136.205 91.769  111.098 1.00 82.83  ? 1304 GLU   A CB  1 
ATOM   11320 C  CG  . GLU   B 2 1304 ? 134.968 91.065  111.640 1.00 86.97  ? 1304 GLU   A CG  1 
ATOM   11321 C  CD  . GLU   B 2 1304 ? 134.665 91.424  113.083 1.00 89.34  ? 1304 GLU   A CD  1 
ATOM   11322 O  OE1 . GLU   B 2 1304 ? 135.504 92.091  113.722 1.00 86.66  ? 1304 GLU   A OE1 1 
ATOM   11323 O  OE2 . GLU   B 2 1304 ? 133.585 91.036  113.578 1.00 90.30  ? 1304 GLU   A OE2 1 
ATOM   11324 N  N   . VAL   B 2 1305 ? 133.697 93.909  110.130 1.00 81.19  ? 1305 VAL   A N   1 
ATOM   11325 C  CA  . VAL   B 2 1305 ? 132.550 94.012  109.236 1.00 79.75  ? 1305 VAL   A CA  1 
ATOM   11326 C  C   . VAL   B 2 1305 ? 132.866 94.999  108.122 1.00 78.98  ? 1305 VAL   A C   1 
ATOM   11327 O  O   . VAL   B 2 1305 ? 133.304 96.129  108.375 1.00 81.53  ? 1305 VAL   A O   1 
ATOM   11328 C  CB  . VAL   B 2 1305 ? 131.294 94.430  110.015 1.00 79.25  ? 1305 VAL   A CB  1 
ATOM   11329 C  CG1 . VAL   B 2 1305 ? 130.142 94.684  109.064 1.00 77.14  ? 1305 VAL   A CG1 1 
ATOM   11330 C  CG2 . VAL   B 2 1305 ? 130.918 93.362  111.025 1.00 78.90  ? 1305 VAL   A CG2 1 
ATOM   11331 N  N   . ASP   B 2 1306 ? 132.649 94.574  106.881 1.00 79.11  ? 1306 ASP   A N   1 
ATOM   11332 C  CA  . ASP   B 2 1306 ? 132.873 95.422  105.719 1.00 77.06  ? 1306 ASP   A CA  1 
ATOM   11333 C  C   . ASP   B 2 1306 ? 131.599 96.201  105.421 1.00 76.67  ? 1306 ASP   A C   1 
ATOM   11334 O  O   . ASP   B 2 1306 ? 130.560 95.610  105.111 1.00 79.60  ? 1306 ASP   A O   1 
ATOM   11335 C  CB  . ASP   B 2 1306 ? 133.301 94.588  104.513 1.00 75.75  ? 1306 ASP   A CB  1 
ATOM   11336 C  CG  . ASP   B 2 1306 ? 132.577 93.261  104.435 1.00 78.71  ? 1306 ASP   A CG  1 
ATOM   11337 O  OD1 . ASP   B 2 1306 ? 131.712 92.998  105.297 1.00 79.87  ? 1306 ASP   A OD1 1 
ATOM   11338 O  OD2 . ASP   B 2 1306 ? 132.877 92.475  103.512 1.00 83.19  ? 1306 ASP   A OD2 1 
ATOM   11339 N  N   . LEU   B 2 1307 ? 131.685 97.528  105.519 1.00 66.49  ? 1307 LEU   A N   1 
ATOM   11340 C  CA  . LEU   B 2 1307 ? 130.505 98.368  105.351 1.00 68.53  ? 1307 LEU   A CA  1 
ATOM   11341 C  C   . LEU   B 2 1307 ? 129.959 98.290  103.933 1.00 72.15  ? 1307 LEU   A C   1 
ATOM   11342 O  O   . LEU   B 2 1307 ? 128.740 98.305  103.730 1.00 76.06  ? 1307 LEU   A O   1 
ATOM   11343 C  CB  . LEU   B 2 1307 ? 130.841 99.815  105.707 1.00 68.32  ? 1307 LEU   A CB  1 
ATOM   11344 C  CG  . LEU   B 2 1307 ? 131.430 100.090 107.088 1.00 63.28  ? 1307 LEU   A CG  1 
ATOM   11345 C  CD1 . LEU   B 2 1307 ? 131.987 101.495 107.142 1.00 62.05  ? 1307 LEU   A CD1 1 
ATOM   11346 C  CD2 . LEU   B 2 1307 ? 130.381 99.899  108.161 1.00 66.57  ? 1307 LEU   A CD2 1 
ATOM   11347 N  N   . TYR   B 2 1308 ? 130.844 98.210  102.938 1.00 69.20  ? 1308 TYR   A N   1 
ATOM   11348 C  CA  . TYR   B 2 1308 ? 130.407 98.344  101.553 1.00 71.56  ? 1308 TYR   A CA  1 
ATOM   11349 C  C   . TYR   B 2 1308 ? 129.715 97.082  101.052 1.00 73.39  ? 1308 TYR   A C   1 
ATOM   11350 O  O   . TYR   B 2 1308 ? 128.748 97.166  100.286 1.00 74.78  ? 1308 TYR   A O   1 
ATOM   11351 C  CB  . TYR   B 2 1308 ? 131.599 98.695  100.668 1.00 70.96  ? 1308 TYR   A CB  1 
ATOM   11352 C  CG  . TYR   B 2 1308 ? 132.234 100.021 101.012 1.00 68.48  ? 1308 TYR   A CG  1 
ATOM   11353 C  CD1 . TYR   B 2 1308 ? 131.737 101.205 100.488 1.00 70.30  ? 1308 TYR   A CD1 1 
ATOM   11354 C  CD2 . TYR   B 2 1308 ? 133.329 100.088 101.860 1.00 66.91  ? 1308 TYR   A CD2 1 
ATOM   11355 C  CE1 . TYR   B 2 1308 ? 132.313 102.418 100.799 1.00 73.19  ? 1308 TYR   A CE1 1 
ATOM   11356 C  CE2 . TYR   B 2 1308 ? 133.912 101.297 102.176 1.00 69.42  ? 1308 TYR   A CE2 1 
ATOM   11357 C  CZ  . TYR   B 2 1308 ? 133.401 102.458 101.644 1.00 73.64  ? 1308 TYR   A CZ  1 
ATOM   11358 O  OH  . TYR   B 2 1308 ? 133.980 103.666 101.959 1.00 71.67  ? 1308 TYR   A OH  1 
ATOM   11359 N  N   . ASN   B 2 1309 ? 130.193 95.909  101.457 1.00 74.32  ? 1309 ASN   A N   1 
ATOM   11360 C  CA  . ASN   B 2 1309 ? 129.621 94.638  101.013 1.00 73.27  ? 1309 ASN   A CA  1 
ATOM   11361 C  C   . ASN   B 2 1309 ? 129.367 93.752  102.228 1.00 72.86  ? 1309 ASN   A C   1 
ATOM   11362 O  O   . ASN   B 2 1309 ? 130.210 92.928  102.594 1.00 75.82  ? 1309 ASN   A O   1 
ATOM   11363 C  CB  . ASN   B 2 1309 ? 130.536 93.952  100.002 1.00 73.73  ? 1309 ASN   A CB  1 
ATOM   11364 C  CG  . ASN   B 2 1309 ? 132.001 94.089  100.350 1.00 75.82  ? 1309 ASN   A CG  1 
ATOM   11365 O  OD1 . ASN   B 2 1309 ? 132.353 94.505  101.452 1.00 76.29  ? 1309 ASN   A OD1 1 
ATOM   11366 N  ND2 . ASN   B 2 1309 ? 132.868 93.735  99.409  1.00 74.84  ? 1309 ASN   A ND2 1 
ATOM   11367 N  N   . HIS   B 2 1310 ? 128.196 93.915  102.844 1.00 65.43  ? 1310 HIS   A N   1 
ATOM   11368 C  CA  . HIS   B 2 1310 ? 127.757 93.085  103.951 1.00 63.56  ? 1310 HIS   A CA  1 
ATOM   11369 C  C   . HIS   B 2 1310 ? 126.283 92.803  103.715 1.00 66.11  ? 1310 HIS   A C   1 
ATOM   11370 O  O   . HIS   B 2 1310 ? 125.569 93.687  103.222 1.00 70.03  ? 1310 HIS   A O   1 
ATOM   11371 C  CB  . HIS   B 2 1310 ? 127.957 93.765  105.308 1.00 64.00  ? 1310 HIS   A CB  1 
ATOM   11372 C  CG  . HIS   B 2 1310 ? 127.699 92.869  106.479 1.00 69.39  ? 1310 HIS   A CG  1 
ATOM   11373 N  ND1 . HIS   B 2 1310 ? 126.446 92.703  107.027 1.00 71.58  ? 1310 HIS   A ND1 1 
ATOM   11374 C  CD2 . HIS   B 2 1310 ? 128.534 92.092  107.208 1.00 71.90  ? 1310 HIS   A CD2 1 
ATOM   11375 C  CE1 . HIS   B 2 1310 ? 126.520 91.861  108.042 1.00 67.49  ? 1310 HIS   A CE1 1 
ATOM   11376 N  NE2 . HIS   B 2 1310 ? 127.776 91.476  108.173 1.00 68.26  ? 1310 HIS   A NE2 1 
ATOM   11377 N  N   . PRO   B 2 1311 ? 125.802 91.600  104.042 1.00 69.50  ? 1311 PRO   A N   1 
ATOM   11378 C  CA  . PRO   B 2 1311 ? 124.397 91.276  103.741 1.00 71.20  ? 1311 PRO   A CA  1 
ATOM   11379 C  C   . PRO   B 2 1311 ? 123.395 92.229  104.367 1.00 72.05  ? 1311 PRO   A C   1 
ATOM   11380 O  O   . PRO   B 2 1311 ? 122.360 92.516  103.753 1.00 78.95  ? 1311 PRO   A O   1 
ATOM   11381 C  CB  . PRO   B 2 1311 ? 124.251 89.852  104.291 1.00 73.49  ? 1311 PRO   A CB  1 
ATOM   11382 C  CG  . PRO   B 2 1311 ? 125.622 89.284  104.211 1.00 73.86  ? 1311 PRO   A CG  1 
ATOM   11383 C  CD  . PRO   B 2 1311 ? 126.555 90.422  104.503 1.00 73.95  ? 1311 PRO   A CD  1 
ATOM   11384 N  N   . MET   B 2 1312 ? 123.666 92.732  105.571 1.00 67.06  ? 1312 MET   A N   1 
ATOM   11385 C  CA  . MET   B 2 1312 ? 122.745 93.634  106.248 1.00 65.97  ? 1312 MET   A CA  1 
ATOM   11386 C  C   . MET   B 2 1312 ? 123.207 95.084  106.255 1.00 69.64  ? 1312 MET   A C   1 
ATOM   11387 O  O   . MET   B 2 1312 ? 122.457 95.950  106.715 1.00 71.75  ? 1312 MET   A O   1 
ATOM   11388 C  CB  . MET   B 2 1312 ? 122.519 93.177  107.694 1.00 66.62  ? 1312 MET   A CB  1 
ATOM   11389 C  CG  . MET   B 2 1312 ? 121.787 91.858  107.831 1.00 72.82  ? 1312 MET   A CG  1 
ATOM   11390 S  SD  . MET   B 2 1312 ? 121.534 91.394  109.557 1.00 82.11  ? 1312 MET   A SD  1 
ATOM   11391 C  CE  . MET   B 2 1312 ? 123.228 91.221  110.115 1.00 73.59  ? 1312 MET   A CE  1 
ATOM   11392 N  N   . LEU   B 2 1313 ? 124.411 95.374  105.764 1.00 71.52  ? 1313 LEU   A N   1 
ATOM   11393 C  CA  . LEU   B 2 1313 ? 124.949 96.729  105.800 1.00 66.43  ? 1313 LEU   A CA  1 
ATOM   11394 C  C   . LEU   B 2 1313 ? 125.198 97.294  104.408 1.00 68.59  ? 1313 LEU   A C   1 
ATOM   11395 O  O   . LEU   B 2 1313 ? 124.764 98.413  104.119 1.00 69.78  ? 1313 LEU   A O   1 
ATOM   11396 C  CB  . LEU   B 2 1313 ? 126.233 96.751  106.632 1.00 67.14  ? 1313 LEU   A CB  1 
ATOM   11397 C  CG  . LEU   B 2 1313 ? 126.422 97.951  107.550 1.00 67.16  ? 1313 LEU   A CG  1 
ATOM   11398 C  CD1 . LEU   B 2 1313 ? 125.113 98.302  108.232 1.00 69.34  ? 1313 LEU   A CD1 1 
ATOM   11399 C  CD2 . LEU   B 2 1313 ? 127.484 97.630  108.573 1.00 70.19  ? 1313 LEU   A CD2 1 
ATOM   11400 N  N   . GLY   B 2 1314 ? 125.897 96.567  103.541 1.00 73.11  ? 1314 GLY   A N   1 
ATOM   11401 C  CA  . GLY   B 2 1314 ? 126.228 97.091  102.231 1.00 66.96  ? 1314 GLY   A CA  1 
ATOM   11402 C  C   . GLY   B 2 1314 ? 125.634 96.313  101.078 1.00 73.05  ? 1314 GLY   A C   1 
ATOM   11403 O  O   . GLY   B 2 1314 ? 125.289 96.896  100.046 1.00 76.11  ? 1314 GLY   A O   1 
ATOM   11404 N  N   . GLY   B 2 1315 ? 125.502 94.995  101.242 1.00 77.52  ? 1315 GLY   A N   1 
ATOM   11405 C  CA  . GLY   B 2 1315 ? 124.918 94.182  100.189 1.00 75.50  ? 1315 GLY   A CA  1 
ATOM   11406 C  C   . GLY   B 2 1315 ? 123.452 94.480  99.965  1.00 74.67  ? 1315 GLY   A C   1 
ATOM   11407 O  O   . GLY   B 2 1315 ? 122.917 94.206  98.887  1.00 78.96  ? 1315 GLY   A O   1 
ATOM   11408 N  N   . LYS   B 2 1316 ? 122.784 95.041  100.971 1.00 69.58  ? 1316 LYS   A N   1 
ATOM   11409 C  CA  . LYS   B 2 1316 ? 121.414 95.505  100.829 1.00 72.93  ? 1316 LYS   A CA  1 
ATOM   11410 C  C   . LYS   B 2 1316 ? 121.335 96.890  100.201 1.00 73.05  ? 1316 LYS   A C   1 
ATOM   11411 O  O   . LYS   B 2 1316 ? 120.233 97.346  99.878  1.00 74.70  ? 1316 LYS   A O   1 
ATOM   11412 C  CB  . LYS   B 2 1316 ? 120.733 95.499  102.203 1.00 74.20  ? 1316 LYS   A CB  1 
ATOM   11413 C  CG  . LYS   B 2 1316 ? 119.216 95.534  102.173 1.00 73.46  ? 1316 LYS   A CG  1 
ATOM   11414 C  CD  . LYS   B 2 1316 ? 118.634 95.325  103.559 1.00 69.93  ? 1316 LYS   A CD  1 
ATOM   11415 C  CE  . LYS   B 2 1316 ? 118.967 93.942  104.086 1.00 72.25  ? 1316 LYS   A CE  1 
ATOM   11416 N  NZ  . LYS   B 2 1316 ? 118.321 93.668  105.397 1.00 73.21  ? 1316 LYS   A NZ  1 
ATOM   11417 N  N   . LEU   B 2 1317 ? 122.477 97.554  100.010 1.00 72.15  ? 1317 LEU   A N   1 
ATOM   11418 C  CA  . LEU   B 2 1317 ? 122.543 98.902  99.444  1.00 73.93  ? 1317 LEU   A CA  1 
ATOM   11419 C  C   . LEU   B 2 1317 ? 121.661 99.866  100.230 1.00 74.97  ? 1317 LEU   A C   1 
ATOM   11420 O  O   . LEU   B 2 1317 ? 120.979 100.729 99.671  1.00 77.29  ? 1317 LEU   A O   1 
ATOM   11421 C  CB  . LEU   B 2 1317 ? 122.171 98.901  97.959  1.00 77.40  ? 1317 LEU   A CB  1 
ATOM   11422 C  CG  . LEU   B 2 1317 ? 123.282 98.564  96.961  1.00 77.31  ? 1317 LEU   A CG  1 
ATOM   11423 C  CD1 . LEU   B 2 1317 ? 124.519 99.400  97.245  1.00 71.91  ? 1317 LEU   A CD1 1 
ATOM   11424 C  CD2 . LEU   B 2 1317 ? 123.614 97.078  96.970  1.00 73.77  ? 1317 LEU   A CD2 1 
ATOM   11425 N  N   . ALA   B 2 1318 ? 121.683 99.714  101.548 1.00 65.05  ? 1318 ALA   A N   1 
ATOM   11426 C  CA  . ALA   B 2 1318 ? 120.876 100.554 102.420 1.00 63.03  ? 1318 ALA   A CA  1 
ATOM   11427 C  C   . ALA   B 2 1318 ? 121.546 100.728 103.775 1.00 64.47  ? 1318 ALA   A C   1 
ATOM   11428 O  O   . ALA   B 2 1318 ? 122.380 99.918  104.172 1.00 70.90  ? 1318 ALA   A O   1 
ATOM   11429 C  CB  . ALA   B 2 1318 ? 119.486 99.964  102.583 1.00 65.61  ? 1318 ALA   A CB  1 
ATOM   11430 N  N   . ARG   B 2 1411 ? 116.565 103.886 72.048  1.00 117.79 ? 1411 ARG   A N   1 
ATOM   11431 C  CA  . ARG   B 2 1411 ? 117.000 104.710 70.926  1.00 118.52 ? 1411 ARG   A CA  1 
ATOM   11432 C  C   . ARG   B 2 1411 ? 117.162 106.171 71.347  1.00 119.40 ? 1411 ARG   A C   1 
ATOM   11433 O  O   . ARG   B 2 1411 ? 116.185 106.908 71.477  1.00 118.06 ? 1411 ARG   A O   1 
ATOM   11434 C  CB  . ARG   B 2 1411 ? 116.014 104.585 69.760  1.00 118.32 ? 1411 ARG   A CB  1 
ATOM   11435 C  CG  . ARG   B 2 1411 ? 114.547 104.598 70.169  1.00 117.67 ? 1411 ARG   A CG  1 
ATOM   11436 C  CD  . ARG   B 2 1411 ? 113.668 103.945 69.113  1.00 117.72 ? 1411 ARG   A CD  1 
ATOM   11437 N  NE  . ARG   B 2 1411 ? 113.828 104.559 67.801  1.00 120.27 ? 1411 ARG   A NE  1 
ATOM   11438 C  CZ  . ARG   B 2 1411 ? 113.201 104.155 66.704  1.00 120.12 ? 1411 ARG   A CZ  1 
ATOM   11439 N  NH1 . ARG   B 2 1411 ? 112.357 103.136 66.726  1.00 117.54 ? 1411 ARG   A NH1 1 
ATOM   11440 N  NH2 . ARG   B 2 1411 ? 113.425 104.789 65.557  1.00 120.56 ? 1411 ARG   A NH2 1 
ATOM   11441 N  N   . GLY   B 2 1412 ? 118.410 106.579 71.564  1.00 114.70 ? 1412 GLY   A N   1 
ATOM   11442 C  CA  . GLY   B 2 1412 ? 118.730 107.923 72.005  1.00 112.51 ? 1412 GLY   A CA  1 
ATOM   11443 C  C   . GLY   B 2 1412 ? 119.374 108.726 70.892  1.00 112.11 ? 1412 GLY   A C   1 
ATOM   11444 O  O   . GLY   B 2 1412 ? 119.994 108.168 69.984  1.00 112.59 ? 1412 GLY   A O   1 
ATOM   11445 N  N   . PHE   B 2 1413 ? 119.222 110.047 70.965  1.00 104.75 ? 1413 PHE   A N   1 
ATOM   11446 C  CA  . PHE   B 2 1413 ? 119.745 110.938 69.942  1.00 103.69 ? 1413 PHE   A CA  1 
ATOM   11447 C  C   . PHE   B 2 1413 ? 120.029 112.301 70.554  1.00 103.89 ? 1413 PHE   A C   1 
ATOM   11448 O  O   . PHE   B 2 1413 ? 119.286 112.768 71.421  1.00 102.76 ? 1413 PHE   A O   1 
ATOM   11449 C  CB  . PHE   B 2 1413 ? 118.764 111.072 68.771  1.00 101.24 ? 1413 PHE   A CB  1 
ATOM   11450 C  CG  . PHE   B 2 1413 ? 118.919 112.346 67.994  1.00 101.94 ? 1413 PHE   A CG  1 
ATOM   11451 C  CD1 . PHE   B 2 1413 ? 119.988 112.524 67.135  1.00 104.19 ? 1413 PHE   A CD1 1 
ATOM   11452 C  CD2 . PHE   B 2 1413 ? 117.989 113.363 68.117  1.00 101.80 ? 1413 PHE   A CD2 1 
ATOM   11453 C  CE1 . PHE   B 2 1413 ? 120.131 113.695 66.420  1.00 103.96 ? 1413 PHE   A CE1 1 
ATOM   11454 C  CE2 . PHE   B 2 1413 ? 118.127 114.535 67.404  1.00 103.65 ? 1413 PHE   A CE2 1 
ATOM   11455 C  CZ  . PHE   B 2 1413 ? 119.200 114.700 66.553  1.00 104.83 ? 1413 PHE   A CZ  1 
ATOM   11456 N  N   . GLY   B 2 1414 ? 121.107 112.932 70.095  1.00 102.43 ? 1414 GLY   A N   1 
ATOM   11457 C  CA  . GLY   B 2 1414 ? 121.463 114.261 70.549  1.00 99.56  ? 1414 GLY   A CA  1 
ATOM   11458 C  C   . GLY   B 2 1414 ? 122.342 115.007 69.567  1.00 99.40  ? 1414 GLY   A C   1 
ATOM   11459 O  O   . GLY   B 2 1414 ? 123.359 114.479 69.108  1.00 98.35  ? 1414 GLY   A O   1 
ATOM   11460 N  N   . PHE   B 2 1415 ? 121.961 116.238 69.238  1.00 103.54 ? 1415 PHE   A N   1 
ATOM   11461 C  CA  . PHE   B 2 1415 ? 122.743 117.061 68.328  1.00 103.69 ? 1415 PHE   A CA  1 
ATOM   11462 C  C   . PHE   B 2 1415 ? 122.529 118.524 68.685  1.00 104.93 ? 1415 PHE   A C   1 
ATOM   11463 O  O   . PHE   B 2 1415 ? 121.442 118.919 69.115  1.00 103.71 ? 1415 PHE   A O   1 
ATOM   11464 C  CB  . PHE   B 2 1415 ? 122.364 116.803 66.866  1.00 103.47 ? 1415 PHE   A CB  1 
ATOM   11465 C  CG  . PHE   B 2 1415 ? 123.192 117.575 65.879  1.00 105.07 ? 1415 PHE   A CG  1 
ATOM   11466 C  CD1 . PHE   B 2 1415 ? 124.469 117.155 65.551  1.00 102.29 ? 1415 PHE   A CD1 1 
ATOM   11467 C  CD2 . PHE   B 2 1415 ? 122.691 118.714 65.273  1.00 106.01 ? 1415 PHE   A CD2 1 
ATOM   11468 C  CE1 . PHE   B 2 1415 ? 125.233 117.859 64.643  1.00 103.92 ? 1415 PHE   A CE1 1 
ATOM   11469 C  CE2 . PHE   B 2 1415 ? 123.451 119.423 64.363  1.00 103.92 ? 1415 PHE   A CE2 1 
ATOM   11470 C  CZ  . PHE   B 2 1415 ? 124.724 118.994 64.048  1.00 105.17 ? 1415 PHE   A CZ  1 
ATOM   11471 N  N   . THR   B 2 1416 ? 123.580 119.319 68.501  1.00 101.71 ? 1416 THR   A N   1 
ATOM   11472 C  CA  . THR   B 2 1416 ? 123.563 120.742 68.812  1.00 100.74 ? 1416 THR   A CA  1 
ATOM   11473 C  C   . THR   B 2 1416 ? 123.871 121.535 67.551  1.00 99.74  ? 1416 THR   A C   1 
ATOM   11474 O  O   . THR   B 2 1416 ? 124.803 121.196 66.813  1.00 99.32  ? 1416 THR   A O   1 
ATOM   11475 C  CB  . THR   B 2 1416 ? 124.576 121.078 69.910  1.00 99.00  ? 1416 THR   A CB  1 
ATOM   11476 O  OG1 . THR   B 2 1416 ? 125.896 120.746 69.463  1.00 98.88  ? 1416 THR   A OG1 1 
ATOM   11477 C  CG2 . THR   B 2 1416 ? 124.270 120.293 71.175  1.00 97.42  ? 1416 THR   A CG2 1 
ATOM   11478 N  N   . MET   B 2 1417 ? 123.091 122.585 67.307  1.00 110.60 ? 1417 MET   A N   1 
ATOM   11479 C  CA  . MET   B 2 1417 ? 123.276 123.421 66.131  1.00 113.38 ? 1417 MET   A CA  1 
ATOM   11480 C  C   . MET   B 2 1417 ? 122.856 124.844 66.468  1.00 115.52 ? 1417 MET   A C   1 
ATOM   11481 O  O   . MET   B 2 1417 ? 122.060 125.071 67.383  1.00 115.93 ? 1417 MET   A O   1 
ATOM   11482 C  CB  . MET   B 2 1417 ? 122.474 122.891 64.935  1.00 114.76 ? 1417 MET   A CB  1 
ATOM   11483 C  CG  . MET   B 2 1417 ? 122.918 123.420 63.573  1.00 114.17 ? 1417 MET   A CG  1 
ATOM   11484 S  SD  . MET   B 2 1417 ? 124.455 122.690 62.967  1.00 115.66 ? 1417 MET   A SD  1 
ATOM   11485 C  CE  . MET   B 2 1417 ? 125.670 123.880 63.533  1.00 111.13 ? 1417 MET   A CE  1 
ATOM   11486 N  N   . GLU   B 2 1418 ? 123.395 125.802 65.711  1.00 121.21 ? 1418 GLU   A N   1 
ATOM   11487 C  CA  . GLU   B 2 1418 ? 123.141 127.215 65.968  1.00 119.93 ? 1418 GLU   A CA  1 
ATOM   11488 C  C   . GLU   B 2 1418 ? 121.713 127.639 65.648  1.00 121.75 ? 1418 GLU   A C   1 
ATOM   11489 O  O   . GLU   B 2 1418 ? 121.303 128.724 66.077  1.00 122.32 ? 1418 GLU   A O   1 
ATOM   11490 C  CB  . GLU   B 2 1418 ? 124.129 128.071 65.173  1.00 119.66 ? 1418 GLU   A CB  1 
ATOM   11491 C  CG  . GLU   B 2 1418 ? 124.624 127.427 63.885  1.00 121.91 ? 1418 GLU   A CG  1 
ATOM   11492 C  CD  . GLU   B 2 1418 ? 123.541 127.299 62.831  1.00 122.46 ? 1418 GLU   A CD  1 
ATOM   11493 O  OE1 . GLU   B 2 1418 ? 122.625 128.147 62.809  1.00 123.15 ? 1418 GLU   A OE1 1 
ATOM   11494 O  OE2 . GLU   B 2 1418 ? 123.607 126.348 62.024  1.00 121.45 ? 1418 GLU   A OE2 1 
ATOM   11495 N  N   . GLU   B 2 1419 ? 120.957 126.825 64.907  1.00 123.50 ? 1419 GLU   A N   1 
ATOM   11496 C  CA  . GLU   B 2 1419 ? 119.550 127.087 64.600  1.00 122.90 ? 1419 GLU   A CA  1 
ATOM   11497 C  C   . GLU   B 2 1419 ? 119.379 128.406 63.840  1.00 124.32 ? 1419 GLU   A C   1 
ATOM   11498 O  O   . GLU   B 2 1419 ? 118.683 129.325 64.276  1.00 123.63 ? 1419 GLU   A O   1 
ATOM   11499 C  CB  . GLU   B 2 1419 ? 118.701 127.073 65.878  1.00 124.65 ? 1419 GLU   A CB  1 
ATOM   11500 C  CG  . GLU   B 2 1419 ? 118.906 125.849 66.758  1.00 123.38 ? 1419 GLU   A CG  1 
ATOM   11501 C  CD  . GLU   B 2 1419 ? 118.321 124.587 66.157  1.00 124.58 ? 1419 GLU   A CD  1 
ATOM   11502 O  OE1 . GLU   B 2 1419 ? 117.420 124.698 65.300  1.00 126.01 ? 1419 GLU   A OE1 1 
ATOM   11503 O  OE2 . GLU   B 2 1419 ? 118.762 123.484 66.543  1.00 124.34 ? 1419 GLU   A OE2 1 
ATOM   11504 N  N   . GLY   B 2 1420 ? 120.031 128.482 62.686  1.00 125.91 ? 1420 GLY   A N   1 
ATOM   11505 C  CA  . GLY   B 2 1420 ? 119.906 129.629 61.811  1.00 124.12 ? 1420 GLY   A CA  1 
ATOM   11506 C  C   . GLY   B 2 1420 ? 120.922 130.720 62.110  1.00 124.19 ? 1420 GLY   A C   1 
ATOM   11507 O  O   . GLY   B 2 1420 ? 121.519 130.785 63.184  1.00 123.28 ? 1420 GLY   A O   1 
ATOM   11508 N  N   . GLY   B 2 1421 ? 121.109 131.596 61.125  1.00 121.51 ? 1421 GLY   A N   1 
ATOM   11509 C  CA  . GLY   B 2 1421 ? 122.040 132.699 61.263  1.00 121.06 ? 1421 GLY   A CA  1 
ATOM   11510 C  C   . GLY   B 2 1421 ? 123.143 132.696 60.224  1.00 121.17 ? 1421 GLY   A C   1 
ATOM   11511 O  O   . GLY   B 2 1421 ? 122.891 132.944 59.041  1.00 119.20 ? 1421 GLY   A O   1 
ATOM   11512 N  N   . VAL   B 2 1422 ? 124.376 132.429 60.662  1.00 116.77 ? 1422 VAL   A N   1 
ATOM   11513 C  CA  . VAL   B 2 1422 ? 125.500 132.344 59.733  1.00 115.83 ? 1422 VAL   A CA  1 
ATOM   11514 C  C   . VAL   B 2 1422 ? 125.269 131.228 58.723  1.00 116.84 ? 1422 VAL   A C   1 
ATOM   11515 O  O   . VAL   B 2 1422 ? 125.617 131.356 57.542  1.00 117.37 ? 1422 VAL   A O   1 
ATOM   11516 C  CB  . VAL   B 2 1422 ? 126.819 132.153 60.504  1.00 114.17 ? 1422 VAL   A CB  1 
ATOM   11517 C  CG1 . VAL   B 2 1422 ? 127.975 131.896 59.545  1.00 114.21 ? 1422 VAL   A CG1 1 
ATOM   11518 C  CG2 . VAL   B 2 1422 ? 127.106 133.372 61.364  1.00 112.92 ? 1422 VAL   A CG2 1 
ATOM   11519 N  N   . ALA   B 2 1423 ? 124.674 130.119 59.168  1.00 122.82 ? 1423 ALA   A N   1 
ATOM   11520 C  CA  . ALA   B 2 1423 ? 124.302 129.058 58.237  1.00 123.02 ? 1423 ALA   A CA  1 
ATOM   11521 C  C   . ALA   B 2 1423 ? 123.309 129.567 57.200  1.00 124.74 ? 1423 ALA   A C   1 
ATOM   11522 O  O   . ALA   B 2 1423 ? 123.399 129.215 56.018  1.00 123.91 ? 1423 ALA   A O   1 
ATOM   11523 C  CB  . ALA   B 2 1423 ? 123.727 127.867 59.001  1.00 122.52 ? 1423 ALA   A CB  1 
ATOM   11524 N  N   . ILE   B 2 1424 ? 122.348 130.391 57.626  1.00 124.57 ? 1424 ILE   A N   1 
ATOM   11525 C  CA  . ILE   B 2 1424 ? 121.472 131.062 56.669  1.00 123.21 ? 1424 ILE   A CA  1 
ATOM   11526 C  C   . ILE   B 2 1424 ? 122.275 132.027 55.806  1.00 122.58 ? 1424 ILE   A C   1 
ATOM   11527 O  O   . ILE   B 2 1424 ? 122.093 132.092 54.585  1.00 123.65 ? 1424 ILE   A O   1 
ATOM   11528 C  CB  . ILE   B 2 1424 ? 120.322 131.778 57.403  1.00 122.39 ? 1424 ILE   A CB  1 
ATOM   11529 C  CG1 . ILE   B 2 1424 ? 119.484 130.771 58.192  1.00 122.87 ? 1424 ILE   A CG1 1 
ATOM   11530 C  CG2 . ILE   B 2 1424 ? 119.452 132.542 56.417  1.00 121.94 ? 1424 ILE   A CG2 1 
ATOM   11531 C  CD1 . ILE   B 2 1424 ? 118.313 131.391 58.924  1.00 121.48 ? 1424 ILE   A CD1 1 
ATOM   11532 N  N   . GLN   B 2 1425 ? 123.177 132.792 56.426  1.00 116.60 ? 1425 GLN   A N   1 
ATOM   11533 C  CA  . GLN   B 2 1425 ? 124.052 133.675 55.663  1.00 116.35 ? 1425 GLN   A CA  1 
ATOM   11534 C  C   . GLN   B 2 1425 ? 125.047 132.901 54.811  1.00 115.90 ? 1425 GLN   A C   1 
ATOM   11535 O  O   . GLN   B 2 1425 ? 125.551 133.444 53.822  1.00 115.00 ? 1425 GLN   A O   1 
ATOM   11536 C  CB  . GLN   B 2 1425 ? 124.794 134.627 56.600  1.00 116.99 ? 1425 GLN   A CB  1 
ATOM   11537 C  CG  . GLN   B 2 1425 ? 123.900 135.660 57.263  1.00 116.81 ? 1425 GLN   A CG  1 
ATOM   11538 C  CD  . GLN   B 2 1425 ? 124.679 136.652 58.102  1.00 116.03 ? 1425 GLN   A CD  1 
ATOM   11539 O  OE1 . GLN   B 2 1425 ? 124.142 137.670 58.537  1.00 115.18 ? 1425 GLN   A OE1 1 
ATOM   11540 N  NE2 . GLN   B 2 1425 ? 125.953 136.358 58.336  1.00 114.46 ? 1425 GLN   A NE2 1 
ATOM   11541 N  N   . ARG   B 2 1426 ? 125.348 131.654 55.177  1.00 121.26 ? 1426 ARG   A N   1 
ATOM   11542 C  CA  . ARG   B 2 1426 ? 126.153 130.806 54.306  1.00 122.56 ? 1426 ARG   A CA  1 
ATOM   11543 C  C   . ARG   B 2 1426 ? 125.416 130.506 53.008  1.00 123.33 ? 1426 ARG   A C   1 
ATOM   11544 O  O   . ARG   B 2 1426 ? 126.037 130.402 51.943  1.00 122.48 ? 1426 ARG   A O   1 
ATOM   11545 C  CB  . ARG   B 2 1426 ? 126.523 129.511 55.030  1.00 121.73 ? 1426 ARG   A CB  1 
ATOM   11546 C  CG  . ARG   B 2 1426 ? 127.406 128.573 54.223  1.00 122.25 ? 1426 ARG   A CG  1 
ATOM   11547 C  CD  . ARG   B 2 1426 ? 128.750 129.211 53.912  1.00 122.49 ? 1426 ARG   A CD  1 
ATOM   11548 N  NE  . ARG   B 2 1426 ? 129.500 129.518 55.124  1.00 125.39 ? 1426 ARG   A NE  1 
ATOM   11549 C  CZ  . ARG   B 2 1426 ? 130.350 128.686 55.710  1.00 123.95 ? 1426 ARG   A CZ  1 
ATOM   11550 N  NH1 . ARG   B 2 1426 ? 130.585 127.480 55.220  1.00 122.52 ? 1426 ARG   A NH1 1 
ATOM   11551 N  NH2 . ARG   B 2 1426 ? 130.979 129.073 56.816  1.00 122.17 ? 1426 ARG   A NH2 1 
ATOM   11552 N  N   . MET   B 2 1427 ? 124.090 130.362 53.078  1.00 121.17 ? 1427 MET   A N   1 
ATOM   11553 C  CA  . MET   B 2 1427 ? 123.303 130.122 51.872  1.00 121.01 ? 1427 MET   A CA  1 
ATOM   11554 C  C   . MET   B 2 1427 ? 123.411 131.289 50.900  1.00 121.11 ? 1427 MET   A C   1 
ATOM   11555 O  O   . MET   B 2 1427 ? 123.586 131.086 49.692  1.00 121.52 ? 1427 MET   A O   1 
ATOM   11556 C  CB  . MET   B 2 1427 ? 121.841 129.876 52.242  1.00 122.57 ? 1427 MET   A CB  1 
ATOM   11557 C  CG  . MET   B 2 1427 ? 121.606 128.646 53.098  1.00 123.39 ? 1427 MET   A CG  1 
ATOM   11558 S  SD  . MET   B 2 1427 ? 121.964 127.118 52.215  1.00 125.71 ? 1427 MET   A SD  1 
ATOM   11559 C  CE  . MET   B 2 1427 ? 121.222 125.919 53.316  1.00 122.41 ? 1427 MET   A CE  1 
ATOM   11560 N  N   . GLN   B 2 1428 ? 123.310 132.519 51.408  1.00 123.28 ? 1428 GLN   A N   1 
ATOM   11561 C  CA  . GLN   B 2 1428 ? 123.388 133.690 50.540  1.00 124.06 ? 1428 GLN   A CA  1 
ATOM   11562 C  C   . GLN   B 2 1428 ? 124.759 133.804 49.888  1.00 124.97 ? 1428 GLN   A C   1 
ATOM   11563 O  O   . GLN   B 2 1428 ? 124.865 134.152 48.706  1.00 126.15 ? 1428 GLN   A O   1 
ATOM   11564 C  CB  . GLN   B 2 1428 ? 123.064 134.954 51.336  1.00 123.98 ? 1428 GLN   A CB  1 
ATOM   11565 C  CG  . GLN   B 2 1428 ? 121.683 134.951 51.969  1.00 122.74 ? 1428 GLN   A CG  1 
ATOM   11566 C  CD  . GLN   B 2 1428 ? 121.406 136.209 52.769  1.00 124.02 ? 1428 GLN   A CD  1 
ATOM   11567 O  OE1 . GLN   B 2 1428 ? 122.254 137.096 52.865  1.00 124.15 ? 1428 GLN   A OE1 1 
ATOM   11568 N  NE2 . GLN   B 2 1428 ? 120.214 136.292 53.349  1.00 124.29 ? 1428 GLN   A NE2 1 
ATOM   11569 N  N   . SER   B 2 1429 ? 125.822 133.524 50.646  1.00 124.77 ? 1429 SER   A N   1 
ATOM   11570 C  CA  . SER   B 2 1429 ? 127.168 133.596 50.087  1.00 124.93 ? 1429 SER   A CA  1 
ATOM   11571 C  C   . SER   B 2 1429 ? 127.365 132.561 48.988  1.00 125.48 ? 1429 SER   A C   1 
ATOM   11572 O  O   . SER   B 2 1429 ? 127.975 132.851 47.953  1.00 125.03 ? 1429 SER   A O   1 
ATOM   11573 C  CB  . SER   B 2 1429 ? 128.205 133.409 51.194  1.00 124.02 ? 1429 SER   A CB  1 
ATOM   11574 O  OG  . SER   B 2 1429 ? 128.056 132.149 51.825  1.00 123.96 ? 1429 SER   A OG  1 
ATOM   11575 N  N   . ARG   B 2 1430 ? 126.851 131.351 49.191  1.00 126.85 ? 1430 ARG   A N   1 
ATOM   11576 C  CA  . ARG   B 2 1430 ? 127.004 130.269 48.228  1.00 126.62 ? 1430 ARG   A CA  1 
ATOM   11577 C  C   . ARG   B 2 1430 ? 125.885 130.226 47.196  1.00 126.60 ? 1430 ARG   A C   1 
ATOM   11578 O  O   . ARG   B 2 1430 ? 125.872 129.321 46.356  1.00 126.76 ? 1430 ARG   A O   1 
ATOM   11579 C  CB  . ARG   B 2 1430 ? 127.083 128.924 48.956  1.00 125.47 ? 1430 ARG   A CB  1 
ATOM   11580 C  CG  . ARG   B 2 1430 ? 128.131 128.861 50.062  1.00 126.28 ? 1430 ARG   A CG  1 
ATOM   11581 C  CD  . ARG   B 2 1430 ? 129.557 128.933 49.527  1.00 126.75 ? 1430 ARG   A CD  1 
ATOM   11582 N  NE  . ARG   B 2 1430 ? 130.096 130.289 49.526  1.00 127.71 ? 1430 ARG   A NE  1 
ATOM   11583 C  CZ  . ARG   B 2 1430 ? 130.369 130.988 48.433  1.00 125.84 ? 1430 ARG   A CZ  1 
ATOM   11584 N  NH1 . ARG   B 2 1430 ? 130.174 130.488 47.224  1.00 124.63 ? 1430 ARG   A NH1 1 
ATOM   11585 N  NH2 . ARG   B 2 1430 ? 130.854 132.221 48.556  1.00 125.20 ? 1430 ARG   A NH2 1 
ATOM   11586 N  N   . LEU   B 2 1431 ? 124.951 131.170 47.238  1.00 126.17 ? 1431 LEU   A N   1 
ATOM   11587 C  CA  . LEU   B 2 1431 ? 123.861 131.213 46.271  1.00 126.48 ? 1431 LEU   A CA  1 
ATOM   11588 C  C   . LEU   B 2 1431 ? 124.373 131.611 44.890  1.00 125.34 ? 1431 LEU   A C   1 
ATOM   11589 O  O   . LEU   B 2 1431 ? 125.423 132.240 44.765  1.00 123.86 ? 1431 LEU   A O   1 
ATOM   11590 C  CB  . LEU   B 2 1431 ? 122.773 132.186 46.729  1.00 126.53 ? 1431 LEU   A CB  1 
ATOM   11591 C  CG  . LEU   B 2 1431 ? 121.560 132.328 45.808  1.00 125.60 ? 1431 LEU   A CG  1 
ATOM   11592 C  CD1 . LEU   B 2 1431 ? 120.855 130.991 45.640  1.00 124.95 ? 1431 LEU   A CD1 1 
ATOM   11593 C  CD2 . LEU   B 2 1431 ? 120.601 133.382 46.340  1.00 124.43 ? 1431 LEU   A CD2 1 
HETATM 11594 C  C1  . NAG   C 3 .    ? 112.658 146.718 181.439 1.00 81.97  ? 1    NAG   D C1  1 
HETATM 11595 C  C2  . NAG   C 3 .    ? 112.126 146.406 180.041 1.00 81.63  ? 1    NAG   D C2  1 
HETATM 11596 C  C3  . NAG   C 3 .    ? 112.238 147.637 179.145 1.00 85.67  ? 1    NAG   D C3  1 
HETATM 11597 C  C4  . NAG   C 3 .    ? 111.576 148.841 179.800 1.00 85.54  ? 1    NAG   D C4  1 
HETATM 11598 C  C5  . NAG   C 3 .    ? 112.137 149.047 181.204 1.00 85.27  ? 1    NAG   D C5  1 
HETATM 11599 C  C6  . NAG   C 3 .    ? 111.445 150.150 181.970 1.00 86.97  ? 1    NAG   D C6  1 
HETATM 11600 C  C7  . NAG   C 3 .    ? 112.226 144.242 178.878 1.00 86.96  ? 1    NAG   D C7  1 
HETATM 11601 C  C8  . NAG   C 3 .    ? 110.726 144.282 178.867 1.00 86.40  ? 1    NAG   D C8  1 
HETATM 11602 N  N2  . NAG   C 3 .    ? 112.838 145.282 179.454 1.00 85.04  ? 1    NAG   D N2  1 
HETATM 11603 O  O3  . NAG   C 3 .    ? 111.624 147.367 177.890 1.00 90.26  ? 1    NAG   D O3  1 
HETATM 11604 O  O4  . NAG   C 3 .    ? 111.821 150.004 179.016 1.00 92.30  ? 1    NAG   D O4  1 
HETATM 11605 O  O5  . NAG   C 3 .    ? 111.970 147.848 181.972 1.00 84.84  ? 1    NAG   D O5  1 
HETATM 11606 O  O6  . NAG   C 3 .    ? 111.029 149.705 183.254 1.00 86.94  ? 1    NAG   D O6  1 
HETATM 11607 O  O7  . NAG   C 3 .    ? 112.854 143.309 178.389 1.00 83.65  ? 1    NAG   D O7  1 
HETATM 11608 C  C1  . NAG   C 3 .    ? 110.568 150.577 178.585 1.00 106.24 ? 2    NAG   D C1  1 
HETATM 11609 C  C2  . NAG   C 3 .    ? 110.861 151.957 177.993 1.00 103.74 ? 2    NAG   D C2  1 
HETATM 11610 C  C3  . NAG   C 3 .    ? 109.573 152.602 177.485 1.00 105.75 ? 2    NAG   D C3  1 
HETATM 11611 C  C4  . NAG   C 3 .    ? 108.852 151.664 176.526 1.00 107.49 ? 2    NAG   D C4  1 
HETATM 11612 C  C5  . NAG   C 3 .    ? 108.646 150.297 177.175 1.00 108.05 ? 2    NAG   D C5  1 
HETATM 11613 C  C6  . NAG   C 3 .    ? 108.039 149.282 176.235 1.00 105.42 ? 2    NAG   D C6  1 
HETATM 11614 C  C7  . NAG   C 3 .    ? 111.015 153.199 180.127 1.00 105.20 ? 2    NAG   D C7  1 
HETATM 11615 C  C8  . NAG   C 3 .    ? 111.879 154.093 180.964 1.00 105.01 ? 2    NAG   D C8  1 
HETATM 11616 N  N2  . NAG   C 3 .    ? 111.534 152.821 178.952 1.00 103.94 ? 2    NAG   D N2  1 
HETATM 11617 O  O3  . NAG   C 3 .    ? 109.884 153.826 176.828 1.00 105.73 ? 2    NAG   D O3  1 
HETATM 11618 O  O4  . NAG   C 3 .    ? 107.587 152.211 176.172 1.00 108.09 ? 2    NAG   D O4  1 
HETATM 11619 O  O5  . NAG   C 3 .    ? 109.908 149.764 177.604 1.00 108.78 ? 2    NAG   D O5  1 
HETATM 11620 O  O6  . NAG   C 3 .    ? 106.620 149.347 176.247 1.00 106.30 ? 2    NAG   D O6  1 
HETATM 11621 O  O7  . NAG   C 3 .    ? 109.902 152.840 180.501 1.00 103.64 ? 2    NAG   D O7  1 
HETATM 11622 C  C1  . NAG   D 4 .    ? 120.787 146.735 171.966 1.00 45.41  ? 1    NAG   E C1  1 
HETATM 11623 C  C2  . NAG   D 4 .    ? 120.615 148.120 172.582 1.00 40.29  ? 1    NAG   E C2  1 
HETATM 11624 C  C3  . NAG   D 4 .    ? 119.236 148.681 172.247 1.00 39.40  ? 1    NAG   E C3  1 
HETATM 11625 C  C4  . NAG   D 4 .    ? 118.995 148.648 170.744 1.00 38.86  ? 1    NAG   E C4  1 
HETATM 11626 C  C5  . NAG   D 4 .    ? 119.232 147.240 170.208 1.00 37.46  ? 1    NAG   E C5  1 
HETATM 11627 C  C6  . NAG   D 4 .    ? 119.140 147.154 168.704 1.00 42.01  ? 1    NAG   E C6  1 
HETATM 11628 C  C7  . NAG   D 4 .    ? 122.020 148.129 174.596 1.00 43.48  ? 1    NAG   E C7  1 
HETATM 11629 C  C8  . NAG   D 4 .    ? 122.038 148.075 176.092 1.00 42.54  ? 1    NAG   E C8  1 
HETATM 11630 N  N2  . NAG   D 4 .    ? 120.814 148.080 174.022 1.00 45.05  ? 1    NAG   E N2  1 
HETATM 11631 O  O3  . NAG   D 4 .    ? 119.139 150.018 172.723 1.00 52.59  ? 1    NAG   E O3  1 
HETATM 11632 O  O4  . NAG   D 4 .    ? 117.656 149.043 170.465 1.00 59.59  ? 1    NAG   E O4  1 
HETATM 11633 O  O5  . NAG   D 4 .    ? 120.551 146.801 170.561 1.00 47.52  ? 1    NAG   E O5  1 
HETATM 11634 O  O6  . NAG   D 4 .    ? 120.363 146.709 168.133 1.00 54.86  ? 1    NAG   E O6  1 
HETATM 11635 O  O7  . NAG   D 4 .    ? 123.049 148.208 173.937 1.00 46.58  ? 1    NAG   E O7  1 
HETATM 11636 C  C1  . NAG   D 4 .    ? 117.647 150.248 169.663 1.00 54.18  ? 2    NAG   E C1  1 
HETATM 11637 C  C2  . NAG   D 4 .    ? 116.215 150.507 169.210 1.00 42.13  ? 2    NAG   E C2  1 
HETATM 11638 C  C3  . NAG   D 4 .    ? 116.149 151.789 168.386 1.00 47.37  ? 2    NAG   E C3  1 
HETATM 11639 C  C4  . NAG   D 4 .    ? 116.780 152.954 169.138 1.00 48.59  ? 2    NAG   E C4  1 
HETATM 11640 C  C5  . NAG   D 4 .    ? 118.177 152.579 169.632 1.00 41.04  ? 2    NAG   E C5  1 
HETATM 11641 C  C6  . NAG   D 4 .    ? 118.799 153.629 170.522 1.00 49.26  ? 2    NAG   E C6  1 
HETATM 11642 C  C7  . NAG   D 4 .    ? 114.961 148.409 168.983 1.00 48.52  ? 2    NAG   E C7  1 
HETATM 11643 C  C8  . NAG   D 4 .    ? 114.511 147.333 168.043 1.00 48.88  ? 2    NAG   E C8  1 
HETATM 11644 N  N2  . NAG   D 4 .    ? 115.698 149.384 168.445 1.00 46.68  ? 2    NAG   E N2  1 
HETATM 11645 O  O3  . NAG   D 4 .    ? 114.791 152.085 168.082 1.00 56.72  ? 2    NAG   E O3  1 
HETATM 11646 O  O4  . NAG   D 4 .    ? 116.881 154.070 168.258 1.00 61.07  ? 2    NAG   E O4  1 
HETATM 11647 O  O5  . NAG   D 4 .    ? 118.124 151.369 170.402 1.00 51.79  ? 2    NAG   E O5  1 
HETATM 11648 O  O6  . NAG   D 4 .    ? 117.995 153.882 171.666 1.00 57.09  ? 2    NAG   E O6  1 
HETATM 11649 O  O7  . NAG   D 4 .    ? 114.669 148.396 170.173 1.00 46.53  ? 2    NAG   E O7  1 
HETATM 11650 C  C1  . BMA   D 4 .    ? 116.201 155.244 168.762 1.00 20.00  ? 3    BMA   E C1  1 
HETATM 11651 C  C2  . BMA   D 4 .    ? 116.857 156.466 168.072 1.00 20.00  ? 3    BMA   E C2  1 
HETATM 11652 C  C3  . BMA   D 4 .    ? 116.098 157.756 168.395 1.00 20.00  ? 3    BMA   E C3  1 
HETATM 11653 C  C4  . BMA   D 4 .    ? 114.592 157.577 168.208 1.00 20.00  ? 3    BMA   E C4  1 
HETATM 11654 C  C5  . BMA   D 4 .    ? 114.108 156.369 169.010 1.00 20.00  ? 3    BMA   E C5  1 
HETATM 11655 C  C6  . BMA   D 4 .    ? 112.611 156.143 168.889 1.00 20.00  ? 3    BMA   E C6  1 
HETATM 11656 O  O2  . BMA   D 4 .    ? 116.824 156.319 166.662 1.00 20.00  ? 3    BMA   E O2  1 
HETATM 11657 O  O3  . BMA   D 4 .    ? 116.549 158.838 167.588 1.00 20.00  ? 3    BMA   E O3  1 
HETATM 11658 O  O4  . BMA   D 4 .    ? 113.908 158.743 168.646 1.00 20.00  ? 3    BMA   E O4  1 
HETATM 11659 O  O5  . BMA   D 4 .    ? 114.797 155.208 168.518 1.00 20.00  ? 3    BMA   E O5  1 
HETATM 11660 O  O6  . BMA   D 4 .    ? 112.379 155.147 167.908 1.00 20.00  ? 3    BMA   E O6  1 
HETATM 11661 C  C1  . MAN   D 4 .    ? 111.491 155.665 166.894 1.00 20.00  ? 4    MAN   E C1  1 
HETATM 11662 C  C2  . MAN   D 4 .    ? 111.523 154.629 165.738 1.00 20.00  ? 4    MAN   E C2  1 
HETATM 11663 C  C3  . MAN   D 4 .    ? 111.028 155.204 164.406 1.00 20.00  ? 4    MAN   E C3  1 
HETATM 11664 C  C4  . MAN   D 4 .    ? 111.540 156.643 164.133 1.00 20.00  ? 4    MAN   E C4  1 
HETATM 11665 C  C5  . MAN   D 4 .    ? 111.292 157.551 165.348 1.00 20.00  ? 4    MAN   E C5  1 
HETATM 11666 C  C6  . MAN   D 4 .    ? 109.833 157.844 165.655 1.00 20.00  ? 4    MAN   E C6  1 
HETATM 11667 O  O2  . MAN   D 4 .    ? 110.659 153.524 166.016 1.00 20.00  ? 4    MAN   E O2  1 
HETATM 11668 O  O3  . MAN   D 4 .    ? 109.611 155.109 164.267 1.00 20.00  ? 4    MAN   E O3  1 
HETATM 11669 O  O4  . MAN   D 4 .    ? 112.953 156.644 163.879 1.00 20.00  ? 4    MAN   E O4  1 
HETATM 11670 O  O5  . MAN   D 4 .    ? 111.905 156.968 166.519 1.00 20.00  ? 4    MAN   E O5  1 
HETATM 11671 O  O6  . MAN   D 4 .    ? 109.789 158.812 166.695 1.00 20.00  ? 4    MAN   E O6  1 
HETATM 11672 C  C1  . MAN   D 4 .    ? 113.358 156.203 162.553 1.00 72.81  ? 5    MAN   E C1  1 
HETATM 11673 C  C2  . MAN   D 4 .    ? 112.379 156.756 161.472 1.00 69.83  ? 5    MAN   E C2  1 
HETATM 11674 C  C3  . MAN   D 4 .    ? 112.167 155.706 160.392 1.00 68.66  ? 5    MAN   E C3  1 
HETATM 11675 C  C4  . MAN   D 4 .    ? 113.475 154.976 160.077 1.00 64.93  ? 5    MAN   E C4  1 
HETATM 11676 C  C5  . MAN   D 4 .    ? 113.943 154.186 161.312 1.00 63.66  ? 5    MAN   E C5  1 
HETATM 11677 C  C6  . MAN   D 4 .    ? 115.445 154.125 161.467 1.00 66.68  ? 5    MAN   E C6  1 
HETATM 11678 O  O2  . MAN   D 4 .    ? 112.933 157.886 160.803 1.00 72.45  ? 5    MAN   E O2  1 
HETATM 11679 O  O3  . MAN   D 4 .    ? 111.623 156.275 159.206 1.00 75.60  ? 5    MAN   E O3  1 
HETATM 11680 O  O4  . MAN   D 4 .    ? 113.269 154.077 159.006 1.00 65.30  ? 5    MAN   E O4  1 
HETATM 11681 O  O5  . MAN   D 4 .    ? 113.416 154.777 162.516 1.00 68.84  ? 5    MAN   E O5  1 
HETATM 11682 O  O6  . MAN   D 4 .    ? 115.736 154.006 162.856 1.00 61.91  ? 5    MAN   E O6  1 
HETATM 11683 C  C1  . MAN   D 4 .    ? 117.562 159.589 168.289 1.00 76.92  ? 6    MAN   E C1  1 
HETATM 11684 C  C2  . MAN   D 4 .    ? 117.446 161.062 167.835 1.00 72.35  ? 6    MAN   E C2  1 
HETATM 11685 C  C3  . MAN   D 4 .    ? 117.872 161.186 166.377 1.00 75.00  ? 6    MAN   E C3  1 
HETATM 11686 C  C4  . MAN   D 4 .    ? 119.259 160.570 166.164 1.00 75.72  ? 6    MAN   E C4  1 
HETATM 11687 C  C5  . MAN   D 4 .    ? 119.252 159.112 166.633 1.00 75.94  ? 6    MAN   E C5  1 
HETATM 11688 C  C6  . MAN   D 4 .    ? 120.613 158.456 166.537 1.00 75.13  ? 6    MAN   E C6  1 
HETATM 11689 O  O2  . MAN   D 4 .    ? 118.339 161.903 168.566 1.00 70.95  ? 6    MAN   E O2  1 
HETATM 11690 O  O3  . MAN   D 4 .    ? 117.862 162.540 165.937 1.00 77.61  ? 6    MAN   E O3  1 
HETATM 11691 O  O4  . MAN   D 4 .    ? 119.605 160.621 164.789 1.00 75.99  ? 6    MAN   E O4  1 
HETATM 11692 O  O5  . MAN   D 4 .    ? 118.849 159.065 168.015 1.00 78.88  ? 6    MAN   E O5  1 
HETATM 11693 O  O6  . MAN   D 4 .    ? 121.123 158.681 165.227 1.00 77.79  ? 6    MAN   E O6  1 
HETATM 11694 C  C1  . NAG   E 3 .    ? 136.292 127.466 186.533 1.00 59.68  ? 1    NAG   G C1  1 
HETATM 11695 C  C2  . NAG   E 3 .    ? 136.335 126.047 187.076 1.00 61.29  ? 1    NAG   G C2  1 
HETATM 11696 C  C3  . NAG   E 3 .    ? 136.254 126.071 188.598 1.00 66.23  ? 1    NAG   G C3  1 
HETATM 11697 C  C4  . NAG   E 3 .    ? 137.315 126.997 189.180 1.00 64.54  ? 1    NAG   G C4  1 
HETATM 11698 C  C5  . NAG   E 3 .    ? 137.293 128.363 188.492 1.00 65.10  ? 1    NAG   G C5  1 
HETATM 11699 C  C6  . NAG   E 3 .    ? 138.448 129.247 188.899 1.00 68.34  ? 1    NAG   G C6  1 
HETATM 11700 C  C7  . NAG   E 3 .    ? 135.467 124.069 185.913 1.00 60.43  ? 1    NAG   G C7  1 
HETATM 11701 C  C8  . NAG   E 3 .    ? 134.245 123.371 185.399 1.00 62.33  ? 1    NAG   G C8  1 
HETATM 11702 N  N2  . NAG   E 3 .    ? 135.260 125.241 186.520 1.00 63.19  ? 1    NAG   G N2  1 
HETATM 11703 O  O3  . NAG   E 3 .    ? 136.428 124.751 189.100 1.00 70.44  ? 1    NAG   G O3  1 
HETATM 11704 O  O4  . NAG   E 3 .    ? 137.058 127.192 190.565 1.00 63.88  ? 1    NAG   G O4  1 
HETATM 11705 O  O5  . NAG   E 3 .    ? 137.373 128.210 187.067 1.00 66.72  ? 1    NAG   G O5  1 
HETATM 11706 O  O6  . NAG   E 3 .    ? 139.647 128.869 188.238 1.00 71.26  ? 1    NAG   G O6  1 
HETATM 11707 O  O7  . NAG   E 3 .    ? 136.589 123.594 185.783 1.00 61.99  ? 1    NAG   G O7  1 
HETATM 11708 C  C1  . NAG   E 3 .    ? 138.021 126.470 191.355 1.00 82.34  ? 2    NAG   G C1  1 
HETATM 11709 C  C2  . NAG   E 3 .    ? 138.023 127.075 192.755 1.00 84.52  ? 2    NAG   G C2  1 
HETATM 11710 C  C3  . NAG   E 3 .    ? 138.997 126.319 193.653 1.00 86.72  ? 2    NAG   G C3  1 
HETATM 11711 C  C4  . NAG   E 3 .    ? 138.682 124.829 193.639 1.00 87.39  ? 2    NAG   G C4  1 
HETATM 11712 C  C5  . NAG   E 3 .    ? 138.642 124.310 192.204 1.00 85.90  ? 2    NAG   G C5  1 
HETATM 11713 C  C6  . NAG   E 3 .    ? 138.208 122.866 192.110 1.00 87.21  ? 2    NAG   G C6  1 
HETATM 11714 C  C7  . NAG   E 3 .    ? 137.463 129.456 192.938 1.00 86.88  ? 2    NAG   G C7  1 
HETATM 11715 C  C8  . NAG   E 3 .    ? 137.979 130.861 192.852 1.00 85.40  ? 2    NAG   G C8  1 
HETATM 11716 N  N2  . NAG   E 3 .    ? 138.357 128.489 192.712 1.00 86.55  ? 2    NAG   G N2  1 
HETATM 11717 O  O3  . NAG   E 3 .    ? 138.907 126.824 194.980 1.00 86.37  ? 2    NAG   G O3  1 
HETATM 11718 O  O4  . NAG   E 3 .    ? 139.675 124.116 194.367 1.00 87.23  ? 2    NAG   G O4  1 
HETATM 11719 O  O5  . NAG   E 3 .    ? 137.703 125.075 191.433 1.00 85.60  ? 2    NAG   G O5  1 
HETATM 11720 O  O6  . NAG   E 3 .    ? 137.382 122.498 193.206 1.00 86.33  ? 2    NAG   G O6  1 
HETATM 11721 O  O7  . NAG   E 3 .    ? 136.290 129.209 193.202 1.00 86.36  ? 2    NAG   G O7  1 
HETATM 11722 C  C1  . NAG   F 5 .    ? 127.769 130.890 194.044 1.00 89.57  ? 501  NAG   B C1  1 
HETATM 11723 C  C2  . NAG   F 5 .    ? 126.654 131.920 193.889 1.00 87.43  ? 501  NAG   B C2  1 
HETATM 11724 C  C3  . NAG   F 5 .    ? 127.092 133.262 194.467 1.00 91.52  ? 501  NAG   B C3  1 
HETATM 11725 C  C4  . NAG   F 5 .    ? 127.569 133.092 195.903 1.00 91.80  ? 501  NAG   B C4  1 
HETATM 11726 C  C5  . NAG   F 5 .    ? 128.642 132.009 195.979 1.00 92.23  ? 501  NAG   B C5  1 
HETATM 11727 C  C6  . NAG   F 5 .    ? 129.070 131.698 197.394 1.00 91.48  ? 501  NAG   B C6  1 
HETATM 11728 C  C7  . NAG   F 5 .    ? 125.091 131.652 192.012 1.00 88.02  ? 501  NAG   B C7  1 
HETATM 11729 C  C8  . NAG   F 5 .    ? 124.160 131.014 193.001 1.00 87.59  ? 501  NAG   B C8  1 
HETATM 11730 N  N2  . NAG   F 5 .    ? 126.268 132.065 192.495 1.00 87.38  ? 501  NAG   B N2  1 
HETATM 11731 O  O3  . NAG   F 5 .    ? 126.003 134.177 194.421 1.00 93.25  ? 501  NAG   B O3  1 
HETATM 11732 O  O4  . NAG   F 5 .    ? 128.106 134.318 196.386 1.00 91.07  ? 501  NAG   B O4  1 
HETATM 11733 O  O5  . NAG   F 5 .    ? 128.139 130.785 195.422 1.00 93.01  ? 501  NAG   B O5  1 
HETATM 11734 O  O6  . NAG   F 5 .    ? 128.354 130.590 197.921 1.00 91.55  ? 501  NAG   B O6  1 
HETATM 11735 O  O7  . NAG   F 5 .    ? 124.790 131.787 190.831 1.00 89.20  ? 501  NAG   B O7  1 
HETATM 11736 BE BE  . BEF   G 6 .    ? 123.169 125.691 83.320  1.00 51.85  ? 1601 BEF   A BE  1 
HETATM 11737 F  F1  . BEF   G 6 .    ? 121.832 125.875 82.592  1.00 54.90  ? 1601 BEF   A F1  1 
HETATM 11738 F  F2  . BEF   G 6 .    ? 124.046 126.982 83.286  1.00 52.95  ? 1601 BEF   A F2  1 
HETATM 11739 F  F3  . BEF   G 6 .    ? 123.982 124.562 82.646  1.00 49.43  ? 1601 BEF   A F3  1 
HETATM 11740 MG MG  . MG    H 7 .    ? 126.656 126.015 84.377  1.00 45.20  ? 1602 MG    A MG  1 
HETATM 11741 C  C01 . A1BD6 I 8 .    ? 139.168 130.399 119.151 1.00 20.00  ? 1603 A1BD6 A C01 1 
HETATM 11742 C  C02 . A1BD6 I 8 .    ? 139.241 129.087 119.954 1.00 20.00  ? 1603 A1BD6 A C02 1 
HETATM 11743 C  C03 . A1BD6 I 8 .    ? 140.179 128.121 119.215 1.00 20.00  ? 1603 A1BD6 A C03 1 
HETATM 11744 C  C04 . A1BD6 I 8 .    ? 139.901 129.311 121.326 1.00 20.00  ? 1603 A1BD6 A C04 1 
HETATM 11745 C  C05 . A1BD6 I 8 .    ? 137.836 128.449 120.079 1.00 20.00  ? 1603 A1BD6 A C05 1 
HETATM 11746 C  C06 . A1BD6 I 8 .    ? 136.764 129.136 120.867 1.00 20.00  ? 1603 A1BD6 A C06 1 
HETATM 11747 C  C07 . A1BD6 I 8 .    ? 136.909 130.239 121.586 1.00 20.00  ? 1603 A1BD6 A C07 1 
HETATM 11748 C  C08 . A1BD6 I 8 .    ? 135.923 131.202 121.992 1.00 20.00  ? 1603 A1BD6 A C08 1 
HETATM 11749 C  C09 . A1BD6 I 8 .    ? 136.276 132.254 122.699 1.00 20.00  ? 1603 A1BD6 A C09 1 
HETATM 11750 C  C10 . A1BD6 I 8 .    ? 137.030 133.422 122.144 1.00 20.00  ? 1603 A1BD6 A C10 1 
HETATM 11751 C  C11 . A1BD6 I 8 .    ? 137.420 133.525 120.652 1.00 20.00  ? 1603 A1BD6 A C11 1 
HETATM 11752 C  C12 . A1BD6 I 8 .    ? 138.075 134.892 120.428 1.00 20.00  ? 1603 A1BD6 A C12 1 
HETATM 11753 C  C13 . A1BD6 I 8 .    ? 138.230 135.476 121.841 1.00 20.00  ? 1603 A1BD6 A C13 1 
HETATM 11754 C  C14 . A1BD6 I 8 .    ? 137.436 136.365 122.432 1.00 20.00  ? 1603 A1BD6 A C14 1 
HETATM 11755 C  C15 . A1BD6 I 8 .    ? 137.568 136.897 123.767 1.00 20.00  ? 1603 A1BD6 A C15 1 
HETATM 11756 C  C16 . A1BD6 I 8 .    ? 136.385 136.897 124.391 1.00 20.00  ? 1603 A1BD6 A C16 1 
HETATM 11757 C  C17 . A1BD6 I 8 .    ? 135.990 137.357 125.813 1.00 20.00  ? 1603 A1BD6 A C17 1 
HETATM 11758 C  C18 . A1BD6 I 8 .    ? 134.769 136.535 126.224 1.00 20.00  ? 1603 A1BD6 A C18 1 
HETATM 11759 C  C19 . A1BD6 I 8 .    ? 135.225 135.084 126.032 1.00 20.00  ? 1603 A1BD6 A C19 1 
HETATM 11760 C  C20 . A1BD6 I 8 .    ? 134.298 136.724 127.667 1.00 20.00  ? 1603 A1BD6 A C20 1 
HETATM 11761 C  C22 . A1BD6 I 8 .    ? 133.356 135.587 128.087 1.00 20.00  ? 1603 A1BD6 A C22 1 
HETATM 11762 C  C24 . A1BD6 I 8 .    ? 132.533 135.857 129.348 1.00 20.00  ? 1603 A1BD6 A C24 1 
HETATM 11763 C  C26 . A1BD6 I 8 .    ? 131.268 136.705 129.143 1.00 20.00  ? 1603 A1BD6 A C26 1 
HETATM 11764 C  C28 . A1BD6 I 8 .    ? 129.958 136.158 129.767 1.00 20.00  ? 1603 A1BD6 A C28 1 
HETATM 11765 O  O30 . A1BD6 I 8 .    ? 128.252 136.980 131.275 1.00 20.00  ? 1603 A1BD6 A O30 1 
HETATM 11766 O  O33 . A1BD6 I 8 .    ? 129.015 140.416 131.293 1.00 20.00  ? 1603 A1BD6 A O33 1 
HETATM 11767 O  O35 . A1BD6 I 8 .    ? 131.472 138.465 131.738 1.00 20.00  ? 1603 A1BD6 A O35 1 
HETATM 11768 O  O36 . A1BD6 I 8 .    ? 126.823 138.654 131.039 1.00 20.00  ? 1603 A1BD6 A O36 1 
HETATM 11769 O  O37 . A1BD6 I 8 .    ? 129.960 134.777 130.013 1.00 20.00  ? 1603 A1BD6 A O37 1 
HETATM 11770 O  O21 . A1BD6 I 8 .    ? 133.688 137.956 127.841 1.00 20.00  ? 1603 A1BD6 A O21 1 
HETATM 11771 O  O23 . A1BD6 I 8 .    ? 132.465 135.381 127.054 1.00 20.00  ? 1603 A1BD6 A O23 1 
HETATM 11772 O  O25 . A1BD6 I 8 .    ? 132.225 134.606 129.884 1.00 20.00  ? 1603 A1BD6 A O25 1 
HETATM 11773 O  O27 . A1BD6 I 8 .    ? 131.035 136.824 127.785 1.00 20.00  ? 1603 A1BD6 A O27 1 
HETATM 11774 C  C29 . A1BD6 I 8 .    ? 129.700 136.885 131.066 1.00 20.00  ? 1603 A1BD6 A C29 1 
HETATM 11775 C  C31 . A1BD6 I 8 .    ? 127.907 138.266 131.317 1.00 20.00  ? 1603 A1BD6 A C31 1 
HETATM 11776 C  C32 . A1BD6 I 8 .    ? 129.106 139.081 131.741 1.00 20.00  ? 1603 A1BD6 A C32 1 
HETATM 11777 C  C34 . A1BD6 I 8 .    ? 130.215 138.321 131.007 1.00 20.00  ? 1603 A1BD6 A C34 1 
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