data_9F2J
# 
_entry.id   9F2J 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9F2J         pdb_00009f2j 10.2210/pdb9f2j/pdb 
WWPDB D_1292138056 ?            ?                   
EMDB  EMD-50147    ?            ?                   
# 
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 2025-03-12 ? 
2 'EM metadata'     1 0 2025-03-12 ? 
3 'Additional map'  1 0 2025-03-12 1 
4 FSC               1 0 2025-03-12 ? 
5 'Half map'        1 0 2025-03-12 1 
6 'Half map'        1 0 2025-03-12 2 
7 Image             1 0 2025-03-12 ? 
8 Mask              1 0 2025-03-12 1 
9 'Primary map'     1 0 2025-03-12 ? 
# 
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 'Additional map'  repository 'Initial release' ? ? 
4 4 FSC               repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 'Half map'        repository 'Initial release' ? ? 
7 7 Image             repository 'Initial release' ? ? 
8 8 Mask              repository 'Initial release' ? ? 
9 9 'Primary map'     repository 'Initial release' ? ? 
# 
loop_
_database_PDB_caveat.id 
_database_PDB_caveat.text 
1 'FUC C 2 HAS WRONG CHIRALITY AT ATOM C1' 
2 'BMA D 3 HAS WRONG CHIRALITY AT ATOM C1' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9F2J 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB .                                           EMD-50146 'focused EM volume'    
PDB  'PDB model'                                 9F2B      unspecified            
EMDB 'Cryo-EM structure of SV2B-BoNT/A1 complex' EMD-50147 'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              volodymyr.korkhov@psi.ch 
_pdbx_contact_author.name_first         Volodymyr 
_pdbx_contact_author.name_last          Korkhov 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0962-9433 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Khanppnavar, B.' 1 0000-0002-6637-3550 
'Leka, O.'        2 ?                   
'Korkhov, V.'     3 0000-0002-0962-9433 
'Kammerer, R.'    4 0000-0003-4570-5197 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                1224 
_citation.page_last                 1224 
_citation.title                     
'Cryo-EM structure of the botulinum neurotoxin A/SV2B complex and its implications for translocation.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-56304-z 
_citation.pdbx_database_id_PubMed   39934119 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Khanppnavar, B.' 1 0000-0002-6637-3550 
primary 'Leka, O.'        2 ?                   
primary 'Pal, S.K.'       3 0000-0002-6193-9762 
primary 'Korkhov, V.M.'   4 0000-0002-0962-9433 
primary 'Kammerer, R.A.'  5 0000-0003-4570-5197 
# 
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 'Botulinum neurotoxin type A' 153083.734 1 ? ? ? ? 
2 polymer     man 'Synaptic vesicle glycoprotein 2B' 77515.016  1 ? ? ? ? 
3 branched    man 'alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose' 367.349    1 ? ? ? ? 
4 branched    man 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose
;
1056.964   1 ? ? ? ? 
5 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208    1 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'BoNT/A,Bontoxilysin-A,BOTOX,Botulinum neurotoxin type A1' 
# 
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 
;MRGSHHHHHHGSLVPRGSPFVNKQFNYKDPVNGVDIAYIKIPNAGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPP
EAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGS
YRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAH
QLIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSI
VGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNAKTFLNFDKAVFKINIVPKVN
YTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIITSKTKSLDKGYNKALNDLCIKVNNWDLF
FSPSEDNFTNDLNKGEEITSDTNIEAAEENISLDLIQQYYLTFNFDNEPENISIENLSSDIIGQLELMPNIERFPNGKKY
ELDKYTMFHYLRAQEFEHGKSRIALTNSVNEALLNPSRVYTFFSSDYVKKVNKATEAAMFLGWVEQLVYDFTDETSEVST
TDKIADITIIIPYIGPALNIGNMLYKDDFVGALIFSGAVILLEFIPEIAIPVLGTFALVSYIANKVLTVQTIDNALSKRN
EKWDEVYKYIVTNWLAKVNTQIDLIRKKMKEALENQAEATKAIINYQYNQYTEEEKNNINFNIDDLSSKLNESINKAMIN
INKFLNQCSVSYLMNSMIPYGVKRLEDFDASLKDALLKYIYDNRGTLIGQVDRLKDKVNNTLSTDIPFQLSKYVDNQRLL
STFTEYIKNIINTSILNLRYESNHLIDLSRYASKINIGSKVNFDPIDKNQIQLFNLESSKIEVILKNAIVYNSMYENFST
SFWIRIPKYFNSISLNNEYTIINCMENNSGWKVSLNYGEIIWTLQDTQEIKQRVVFKYSQMINISDYINRWIFVTITNNR
LNNSKIYINGRLIDQKPISNLGNIHASNNIMFKLDGCRDTHRYIWIKYFNLFDKELNEKEIKDLYDNQSNSGILKDFWGD
YLQYDKPYYMLNLYDPNKYVDVNNVGIRGYMYLKGPRGSVMTTNIYLNSSLYRGAKFIIKKYASGNKDNIVRNNDRVYIN
VVVKNKEYRLATNASQAGVEKILSALEIPDVGNLSQVVVMKSKNDQGITNKCKMNLQDNNGNDIGFIGFHQFNNIAKLVA
SNWYNRQIERSSRTLGCSWEFIPVDDGWGERPLVPPTPGSAWSHPQFEK
;
;MRGSHHHHHHGSLVPRGSPFVNKQFNYKDPVNGVDIAYIKIPNAGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPP
EAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGS
YRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAH
QLIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSI
VGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNAKTFLNFDKAVFKINIVPKVN
YTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIITSKTKSLDKGYNKALNDLCIKVNNWDLF
FSPSEDNFTNDLNKGEEITSDTNIEAAEENISLDLIQQYYLTFNFDNEPENISIENLSSDIIGQLELMPNIERFPNGKKY
ELDKYTMFHYLRAQEFEHGKSRIALTNSVNEALLNPSRVYTFFSSDYVKKVNKATEAAMFLGWVEQLVYDFTDETSEVST
TDKIADITIIIPYIGPALNIGNMLYKDDFVGALIFSGAVILLEFIPEIAIPVLGTFALVSYIANKVLTVQTIDNALSKRN
EKWDEVYKYIVTNWLAKVNTQIDLIRKKMKEALENQAEATKAIINYQYNQYTEEEKNNINFNIDDLSSKLNESINKAMIN
INKFLNQCSVSYLMNSMIPYGVKRLEDFDASLKDALLKYIYDNRGTLIGQVDRLKDKVNNTLSTDIPFQLSKYVDNQRLL
STFTEYIKNIINTSILNLRYESNHLIDLSRYASKINIGSKVNFDPIDKNQIQLFNLESSKIEVILKNAIVYNSMYENFST
SFWIRIPKYFNSISLNNEYTIINCMENNSGWKVSLNYGEIIWTLQDTQEIKQRVVFKYSQMINISDYINRWIFVTITNNR
LNNSKIYINGRLIDQKPISNLGNIHASNNIMFKLDGCRDTHRYIWIKYFNLFDKELNEKEIKDLYDNQSNSGILKDFWGD
YLQYDKPYYMLNLYDPNKYVDVNNVGIRGYMYLKGPRGSVMTTNIYLNSSLYRGAKFIIKKYASGNKDNIVRNNDRVYIN
VVVKNKEYRLATNASQAGVEKILSALEIPDVGNLSQVVVMKSKNDQGITNKCKMNLQDNNGNDIGFIGFHQFNNIAKLVA
SNWYNRQIERSSRTLGCSWEFIPVDDGWGERPLVPPTPGSAWSHPQFEK
;
B ? 
2 'polypeptide(L)' no no 
;MDDYKYQDNYGGYAPSDGYYRGNESNPEEDAQSDVTEGHDEEDEIYEGEYQGIPHPDDVKAKQAKMAPSRMDSLRGQTDL
MAERLEDEEQLAHQYETIMDECGHGRFQWILFFVLGLALMADGVEVFVVSFALPSAEKDMCLSSSKKGMLGMIVYLGMMA
GAFILGGLADKLGRKRVLSMSLAVNASFASLSSFVQGYGAFLFCRLISGIGIGGALPIVFAYFSEFLSREKRGEHLSWLG
IFWMTGGLYASAMAWSIIPHYGWGFSMGTNYHFHSWRVFVIVCALPCTVSMVALKFMPESPRFLLEMGKHDEAWMILKQV
HDTNMRAKGTPEKVFTVSNIKTPKQMDEFIEIQSSTGTWYQRWLVRFKTIFKQVWDNALYCVMGPYRMNTLILAVVWFAM
AFSYYGLTVWFPDMIRYFQDEEYKSKMKVFFGEHVYGATINFTMENQIHQHGKLVNDKFTRMYFKHVLFEDTFFDECYFE
DVTSTDTYFKNCTIESTIFYNTDLYEHKFINCRFINSTFLEQKEGCHMDLEQDNDFLIYLVSFLGSLSVLPGNIISALLM
DRIGRLKMIGGSMLISAVCCFFLFFGNSESAMIGWQCLFCGTSIAAWNALDVITVELYPTNQRATAFGILNGLCKFGAIL
GNTIFASFVGITKVVPILLAAASLVGGGLIALRLPETREQVLM
;
;MDDYKYQDNYGGYAPSDGYYRGNESNPEEDAQSDVTEGHDEEDEIYEGEYQGIPHPDDVKAKQAKMAPSRMDSLRGQTDL
MAERLEDEEQLAHQYETIMDECGHGRFQWILFFVLGLALMADGVEVFVVSFALPSAEKDMCLSSSKKGMLGMIVYLGMMA
GAFILGGLADKLGRKRVLSMSLAVNASFASLSSFVQGYGAFLFCRLISGIGIGGALPIVFAYFSEFLSREKRGEHLSWLG
IFWMTGGLYASAMAWSIIPHYGWGFSMGTNYHFHSWRVFVIVCALPCTVSMVALKFMPESPRFLLEMGKHDEAWMILKQV
HDTNMRAKGTPEKVFTVSNIKTPKQMDEFIEIQSSTGTWYQRWLVRFKTIFKQVWDNALYCVMGPYRMNTLILAVVWFAM
AFSYYGLTVWFPDMIRYFQDEEYKSKMKVFFGEHVYGATINFTMENQIHQHGKLVNDKFTRMYFKHVLFEDTFFDECYFE
DVTSTDTYFKNCTIESTIFYNTDLYEHKFINCRFINSTFLEQKEGCHMDLEQDNDFLIYLVSFLGSLSVLPGNIISALLM
DRIGRLKMIGGSMLISAVCCFFLFFGNSESAMIGWQCLFCGTSIAAWNALDVITVELYPTNQRATAFGILNGLCKFGAIL
GNTIFASFVGITKVVPILLAAASLVGGGLIALRLPETREQVLM
;
A ? 
# 
_pdbx_entity_nonpoly.entity_id   5 
_pdbx_entity_nonpoly.name        2-acetamido-2-deoxy-beta-D-glucopyranose 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
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    ARG n 
1 3    GLY n 
1 4    SER n 
1 5    HIS n 
1 6    HIS n 
1 7    HIS n 
1 8    HIS n 
1 9    HIS n 
1 10   HIS n 
1 11   GLY n 
1 12   SER n 
1 13   LEU n 
1 14   VAL n 
1 15   PRO n 
1 16   ARG n 
1 17   GLY n 
1 18   SER n 
1 19   PRO n 
1 20   PHE n 
1 21   VAL n 
1 22   ASN n 
1 23   LYS n 
1 24   GLN n 
1 25   PHE n 
1 26   ASN n 
1 27   TYR n 
1 28   LYS n 
1 29   ASP n 
1 30   PRO n 
1 31   VAL n 
1 32   ASN n 
1 33   GLY n 
1 34   VAL n 
1 35   ASP n 
1 36   ILE n 
1 37   ALA n 
1 38   TYR n 
1 39   ILE n 
1 40   LYS n 
1 41   ILE n 
1 42   PRO n 
1 43   ASN n 
1 44   ALA n 
1 45   GLY n 
1 46   GLN n 
1 47   MET n 
1 48   GLN n 
1 49   PRO n 
1 50   VAL n 
1 51   LYS n 
1 52   ALA n 
1 53   PHE n 
1 54   LYS n 
1 55   ILE n 
1 56   HIS n 
1 57   ASN n 
1 58   LYS n 
1 59   ILE n 
1 60   TRP n 
1 61   VAL n 
1 62   ILE n 
1 63   PRO n 
1 64   GLU n 
1 65   ARG n 
1 66   ASP n 
1 67   THR n 
1 68   PHE n 
1 69   THR n 
1 70   ASN n 
1 71   PRO n 
1 72   GLU n 
1 73   GLU n 
1 74   GLY n 
1 75   ASP n 
1 76   LEU n 
1 77   ASN n 
1 78   PRO n 
1 79   PRO n 
1 80   PRO n 
1 81   GLU n 
1 82   ALA n 
1 83   LYS n 
1 84   GLN n 
1 85   VAL n 
1 86   PRO n 
1 87   VAL n 
1 88   SER n 
1 89   TYR n 
1 90   TYR n 
1 91   ASP n 
1 92   SER n 
1 93   THR n 
1 94   TYR n 
1 95   LEU n 
1 96   SER n 
1 97   THR n 
1 98   ASP n 
1 99   ASN n 
1 100  GLU n 
1 101  LYS n 
1 102  ASP n 
1 103  ASN n 
1 104  TYR n 
1 105  LEU n 
1 106  LYS n 
1 107  GLY n 
1 108  VAL n 
1 109  THR n 
1 110  LYS n 
1 111  LEU n 
1 112  PHE n 
1 113  GLU n 
1 114  ARG n 
1 115  ILE n 
1 116  TYR n 
1 117  SER n 
1 118  THR n 
1 119  ASP n 
1 120  LEU n 
1 121  GLY n 
1 122  ARG n 
1 123  MET n 
1 124  LEU n 
1 125  LEU n 
1 126  THR n 
1 127  SER n 
1 128  ILE n 
1 129  VAL n 
1 130  ARG n 
1 131  GLY n 
1 132  ILE n 
1 133  PRO n 
1 134  PHE n 
1 135  TRP n 
1 136  GLY n 
1 137  GLY n 
1 138  SER n 
1 139  THR n 
1 140  ILE n 
1 141  ASP n 
1 142  THR n 
1 143  GLU n 
1 144  LEU n 
1 145  LYS n 
1 146  VAL n 
1 147  ILE n 
1 148  ASP n 
1 149  THR n 
1 150  ASN n 
1 151  CYS n 
1 152  ILE n 
1 153  ASN n 
1 154  VAL n 
1 155  ILE n 
1 156  GLN n 
1 157  PRO n 
1 158  ASP n 
1 159  GLY n 
1 160  SER n 
1 161  TYR n 
1 162  ARG n 
1 163  SER n 
1 164  GLU n 
1 165  GLU n 
1 166  LEU n 
1 167  ASN n 
1 168  LEU n 
1 169  VAL n 
1 170  ILE n 
1 171  ILE n 
1 172  GLY n 
1 173  PRO n 
1 174  SER n 
1 175  ALA n 
1 176  ASP n 
1 177  ILE n 
1 178  ILE n 
1 179  GLN n 
1 180  PHE n 
1 181  GLU n 
1 182  CYS n 
1 183  LYS n 
1 184  SER n 
1 185  PHE n 
1 186  GLY n 
1 187  HIS n 
1 188  GLU n 
1 189  VAL n 
1 190  LEU n 
1 191  ASN n 
1 192  LEU n 
1 193  THR n 
1 194  ARG n 
1 195  ASN n 
1 196  GLY n 
1 197  TYR n 
1 198  GLY n 
1 199  SER n 
1 200  THR n 
1 201  GLN n 
1 202  TYR n 
1 203  ILE n 
1 204  ARG n 
1 205  PHE n 
1 206  SER n 
1 207  PRO n 
1 208  ASP n 
1 209  PHE n 
1 210  THR n 
1 211  PHE n 
1 212  GLY n 
1 213  PHE n 
1 214  GLU n 
1 215  GLU n 
1 216  SER n 
1 217  LEU n 
1 218  GLU n 
1 219  VAL n 
1 220  ASP n 
1 221  THR n 
1 222  ASN n 
1 223  PRO n 
1 224  LEU n 
1 225  LEU n 
1 226  GLY n 
1 227  ALA n 
1 228  GLY n 
1 229  LYS n 
1 230  PHE n 
1 231  ALA n 
1 232  THR n 
1 233  ASP n 
1 234  PRO n 
1 235  ALA n 
1 236  VAL n 
1 237  THR n 
1 238  LEU n 
1 239  ALA n 
1 240  HIS n 
1 241  GLN n 
1 242  LEU n 
1 243  ILE n 
1 244  HIS n 
1 245  ALA n 
1 246  GLY n 
1 247  HIS n 
1 248  ARG n 
1 249  LEU n 
1 250  TYR n 
1 251  GLY n 
1 252  ILE n 
1 253  ALA n 
1 254  ILE n 
1 255  ASN n 
1 256  PRO n 
1 257  ASN n 
1 258  ARG n 
1 259  VAL n 
1 260  PHE n 
1 261  LYS n 
1 262  VAL n 
1 263  ASN n 
1 264  THR n 
1 265  ASN n 
1 266  ALA n 
1 267  TYR n 
1 268  TYR n 
1 269  GLU n 
1 270  MET n 
1 271  SER n 
1 272  GLY n 
1 273  LEU n 
1 274  GLU n 
1 275  VAL n 
1 276  SER n 
1 277  PHE n 
1 278  GLU n 
1 279  GLU n 
1 280  LEU n 
1 281  ARG n 
1 282  THR n 
1 283  PHE n 
1 284  GLY n 
1 285  GLY n 
1 286  HIS n 
1 287  ASP n 
1 288  ALA n 
1 289  LYS n 
1 290  PHE n 
1 291  ILE n 
1 292  ASP n 
1 293  SER n 
1 294  LEU n 
1 295  GLN n 
1 296  GLU n 
1 297  ASN n 
1 298  GLU n 
1 299  PHE n 
1 300  ARG n 
1 301  LEU n 
1 302  TYR n 
1 303  TYR n 
1 304  TYR n 
1 305  ASN n 
1 306  LYS n 
1 307  PHE n 
1 308  LYS n 
1 309  ASP n 
1 310  ILE n 
1 311  ALA n 
1 312  SER n 
1 313  THR n 
1 314  LEU n 
1 315  ASN n 
1 316  LYS n 
1 317  ALA n 
1 318  LYS n 
1 319  SER n 
1 320  ILE n 
1 321  VAL n 
1 322  GLY n 
1 323  THR n 
1 324  THR n 
1 325  ALA n 
1 326  SER n 
1 327  LEU n 
1 328  GLN n 
1 329  TYR n 
1 330  MET n 
1 331  LYS n 
1 332  ASN n 
1 333  VAL n 
1 334  PHE n 
1 335  LYS n 
1 336  GLU n 
1 337  LYS n 
1 338  TYR n 
1 339  LEU n 
1 340  LEU n 
1 341  SER n 
1 342  GLU n 
1 343  ASP n 
1 344  THR n 
1 345  SER n 
1 346  GLY n 
1 347  LYS n 
1 348  PHE n 
1 349  SER n 
1 350  VAL n 
1 351  ASP n 
1 352  LYS n 
1 353  LEU n 
1 354  LYS n 
1 355  PHE n 
1 356  ASP n 
1 357  LYS n 
1 358  LEU n 
1 359  TYR n 
1 360  LYS n 
1 361  MET n 
1 362  LEU n 
1 363  THR n 
1 364  GLU n 
1 365  ILE n 
1 366  TYR n 
1 367  THR n 
1 368  GLU n 
1 369  ASP n 
1 370  ASN n 
1 371  PHE n 
1 372  VAL n 
1 373  LYS n 
1 374  PHE n 
1 375  PHE n 
1 376  LYS n 
1 377  VAL n 
1 378  LEU n 
1 379  ASN n 
1 380  ALA n 
1 381  LYS n 
1 382  THR n 
1 383  PHE n 
1 384  LEU n 
1 385  ASN n 
1 386  PHE n 
1 387  ASP n 
1 388  LYS n 
1 389  ALA n 
1 390  VAL n 
1 391  PHE n 
1 392  LYS n 
1 393  ILE n 
1 394  ASN n 
1 395  ILE n 
1 396  VAL n 
1 397  PRO n 
1 398  LYS n 
1 399  VAL n 
1 400  ASN n 
1 401  TYR n 
1 402  THR n 
1 403  ILE n 
1 404  TYR n 
1 405  ASP n 
1 406  GLY n 
1 407  PHE n 
1 408  ASN n 
1 409  LEU n 
1 410  ARG n 
1 411  ASN n 
1 412  THR n 
1 413  ASN n 
1 414  LEU n 
1 415  ALA n 
1 416  ALA n 
1 417  ASN n 
1 418  PHE n 
1 419  ASN n 
1 420  GLY n 
1 421  GLN n 
1 422  ASN n 
1 423  THR n 
1 424  GLU n 
1 425  ILE n 
1 426  ASN n 
1 427  ASN n 
1 428  MET n 
1 429  ASN n 
1 430  PHE n 
1 431  THR n 
1 432  LYS n 
1 433  LEU n 
1 434  LYS n 
1 435  ASN n 
1 436  PHE n 
1 437  THR n 
1 438  GLY n 
1 439  LEU n 
1 440  PHE n 
1 441  GLU n 
1 442  PHE n 
1 443  TYR n 
1 444  LYS n 
1 445  LEU n 
1 446  LEU n 
1 447  CYS n 
1 448  VAL n 
1 449  ARG n 
1 450  GLY n 
1 451  ILE n 
1 452  ILE n 
1 453  THR n 
1 454  SER n 
1 455  LYS n 
1 456  THR n 
1 457  LYS n 
1 458  SER n 
1 459  LEU n 
1 460  ASP n 
1 461  LYS n 
1 462  GLY n 
1 463  TYR n 
1 464  ASN n 
1 465  LYS n 
1 466  ALA n 
1 467  LEU n 
1 468  ASN n 
1 469  ASP n 
1 470  LEU n 
1 471  CYS n 
1 472  ILE n 
1 473  LYS n 
1 474  VAL n 
1 475  ASN n 
1 476  ASN n 
1 477  TRP n 
1 478  ASP n 
1 479  LEU n 
1 480  PHE n 
1 481  PHE n 
1 482  SER n 
1 483  PRO n 
1 484  SER n 
1 485  GLU n 
1 486  ASP n 
1 487  ASN n 
1 488  PHE n 
1 489  THR n 
1 490  ASN n 
1 491  ASP n 
1 492  LEU n 
1 493  ASN n 
1 494  LYS n 
1 495  GLY n 
1 496  GLU n 
1 497  GLU n 
1 498  ILE n 
1 499  THR n 
1 500  SER n 
1 501  ASP n 
1 502  THR n 
1 503  ASN n 
1 504  ILE n 
1 505  GLU n 
1 506  ALA n 
1 507  ALA n 
1 508  GLU n 
1 509  GLU n 
1 510  ASN n 
1 511  ILE n 
1 512  SER n 
1 513  LEU n 
1 514  ASP n 
1 515  LEU n 
1 516  ILE n 
1 517  GLN n 
1 518  GLN n 
1 519  TYR n 
1 520  TYR n 
1 521  LEU n 
1 522  THR n 
1 523  PHE n 
1 524  ASN n 
1 525  PHE n 
1 526  ASP n 
1 527  ASN n 
1 528  GLU n 
1 529  PRO n 
1 530  GLU n 
1 531  ASN n 
1 532  ILE n 
1 533  SER n 
1 534  ILE n 
1 535  GLU n 
1 536  ASN n 
1 537  LEU n 
1 538  SER n 
1 539  SER n 
1 540  ASP n 
1 541  ILE n 
1 542  ILE n 
1 543  GLY n 
1 544  GLN n 
1 545  LEU n 
1 546  GLU n 
1 547  LEU n 
1 548  MET n 
1 549  PRO n 
1 550  ASN n 
1 551  ILE n 
1 552  GLU n 
1 553  ARG n 
1 554  PHE n 
1 555  PRO n 
1 556  ASN n 
1 557  GLY n 
1 558  LYS n 
1 559  LYS n 
1 560  TYR n 
1 561  GLU n 
1 562  LEU n 
1 563  ASP n 
1 564  LYS n 
1 565  TYR n 
1 566  THR n 
1 567  MET n 
1 568  PHE n 
1 569  HIS n 
1 570  TYR n 
1 571  LEU n 
1 572  ARG n 
1 573  ALA n 
1 574  GLN n 
1 575  GLU n 
1 576  PHE n 
1 577  GLU n 
1 578  HIS n 
1 579  GLY n 
1 580  LYS n 
1 581  SER n 
1 582  ARG n 
1 583  ILE n 
1 584  ALA n 
1 585  LEU n 
1 586  THR n 
1 587  ASN n 
1 588  SER n 
1 589  VAL n 
1 590  ASN n 
1 591  GLU n 
1 592  ALA n 
1 593  LEU n 
1 594  LEU n 
1 595  ASN n 
1 596  PRO n 
1 597  SER n 
1 598  ARG n 
1 599  VAL n 
1 600  TYR n 
1 601  THR n 
1 602  PHE n 
1 603  PHE n 
1 604  SER n 
1 605  SER n 
1 606  ASP n 
1 607  TYR n 
1 608  VAL n 
1 609  LYS n 
1 610  LYS n 
1 611  VAL n 
1 612  ASN n 
1 613  LYS n 
1 614  ALA n 
1 615  THR n 
1 616  GLU n 
1 617  ALA n 
1 618  ALA n 
1 619  MET n 
1 620  PHE n 
1 621  LEU n 
1 622  GLY n 
1 623  TRP n 
1 624  VAL n 
1 625  GLU n 
1 626  GLN n 
1 627  LEU n 
1 628  VAL n 
1 629  TYR n 
1 630  ASP n 
1 631  PHE n 
1 632  THR n 
1 633  ASP n 
1 634  GLU n 
1 635  THR n 
1 636  SER n 
1 637  GLU n 
1 638  VAL n 
1 639  SER n 
1 640  THR n 
1 641  THR n 
1 642  ASP n 
1 643  LYS n 
1 644  ILE n 
1 645  ALA n 
1 646  ASP n 
1 647  ILE n 
1 648  THR n 
1 649  ILE n 
1 650  ILE n 
1 651  ILE n 
1 652  PRO n 
1 653  TYR n 
1 654  ILE n 
1 655  GLY n 
1 656  PRO n 
1 657  ALA n 
1 658  LEU n 
1 659  ASN n 
1 660  ILE n 
1 661  GLY n 
1 662  ASN n 
1 663  MET n 
1 664  LEU n 
1 665  TYR n 
1 666  LYS n 
1 667  ASP n 
1 668  ASP n 
1 669  PHE n 
1 670  VAL n 
1 671  GLY n 
1 672  ALA n 
1 673  LEU n 
1 674  ILE n 
1 675  PHE n 
1 676  SER n 
1 677  GLY n 
1 678  ALA n 
1 679  VAL n 
1 680  ILE n 
1 681  LEU n 
1 682  LEU n 
1 683  GLU n 
1 684  PHE n 
1 685  ILE n 
1 686  PRO n 
1 687  GLU n 
1 688  ILE n 
1 689  ALA n 
1 690  ILE n 
1 691  PRO n 
1 692  VAL n 
1 693  LEU n 
1 694  GLY n 
1 695  THR n 
1 696  PHE n 
1 697  ALA n 
1 698  LEU n 
1 699  VAL n 
1 700  SER n 
1 701  TYR n 
1 702  ILE n 
1 703  ALA n 
1 704  ASN n 
1 705  LYS n 
1 706  VAL n 
1 707  LEU n 
1 708  THR n 
1 709  VAL n 
1 710  GLN n 
1 711  THR n 
1 712  ILE n 
1 713  ASP n 
1 714  ASN n 
1 715  ALA n 
1 716  LEU n 
1 717  SER n 
1 718  LYS n 
1 719  ARG n 
1 720  ASN n 
1 721  GLU n 
1 722  LYS n 
1 723  TRP n 
1 724  ASP n 
1 725  GLU n 
1 726  VAL n 
1 727  TYR n 
1 728  LYS n 
1 729  TYR n 
1 730  ILE n 
1 731  VAL n 
1 732  THR n 
1 733  ASN n 
1 734  TRP n 
1 735  LEU n 
1 736  ALA n 
1 737  LYS n 
1 738  VAL n 
1 739  ASN n 
1 740  THR n 
1 741  GLN n 
1 742  ILE n 
1 743  ASP n 
1 744  LEU n 
1 745  ILE n 
1 746  ARG n 
1 747  LYS n 
1 748  LYS n 
1 749  MET n 
1 750  LYS n 
1 751  GLU n 
1 752  ALA n 
1 753  LEU n 
1 754  GLU n 
1 755  ASN n 
1 756  GLN n 
1 757  ALA n 
1 758  GLU n 
1 759  ALA n 
1 760  THR n 
1 761  LYS n 
1 762  ALA n 
1 763  ILE n 
1 764  ILE n 
1 765  ASN n 
1 766  TYR n 
1 767  GLN n 
1 768  TYR n 
1 769  ASN n 
1 770  GLN n 
1 771  TYR n 
1 772  THR n 
1 773  GLU n 
1 774  GLU n 
1 775  GLU n 
1 776  LYS n 
1 777  ASN n 
1 778  ASN n 
1 779  ILE n 
1 780  ASN n 
1 781  PHE n 
1 782  ASN n 
1 783  ILE n 
1 784  ASP n 
1 785  ASP n 
1 786  LEU n 
1 787  SER n 
1 788  SER n 
1 789  LYS n 
1 790  LEU n 
1 791  ASN n 
1 792  GLU n 
1 793  SER n 
1 794  ILE n 
1 795  ASN n 
1 796  LYS n 
1 797  ALA n 
1 798  MET n 
1 799  ILE n 
1 800  ASN n 
1 801  ILE n 
1 802  ASN n 
1 803  LYS n 
1 804  PHE n 
1 805  LEU n 
1 806  ASN n 
1 807  GLN n 
1 808  CYS n 
1 809  SER n 
1 810  VAL n 
1 811  SER n 
1 812  TYR n 
1 813  LEU n 
1 814  MET n 
1 815  ASN n 
1 816  SER n 
1 817  MET n 
1 818  ILE n 
1 819  PRO n 
1 820  TYR n 
1 821  GLY n 
1 822  VAL n 
1 823  LYS n 
1 824  ARG n 
1 825  LEU n 
1 826  GLU n 
1 827  ASP n 
1 828  PHE n 
1 829  ASP n 
1 830  ALA n 
1 831  SER n 
1 832  LEU n 
1 833  LYS n 
1 834  ASP n 
1 835  ALA n 
1 836  LEU n 
1 837  LEU n 
1 838  LYS n 
1 839  TYR n 
1 840  ILE n 
1 841  TYR n 
1 842  ASP n 
1 843  ASN n 
1 844  ARG n 
1 845  GLY n 
1 846  THR n 
1 847  LEU n 
1 848  ILE n 
1 849  GLY n 
1 850  GLN n 
1 851  VAL n 
1 852  ASP n 
1 853  ARG n 
1 854  LEU n 
1 855  LYS n 
1 856  ASP n 
1 857  LYS n 
1 858  VAL n 
1 859  ASN n 
1 860  ASN n 
1 861  THR n 
1 862  LEU n 
1 863  SER n 
1 864  THR n 
1 865  ASP n 
1 866  ILE n 
1 867  PRO n 
1 868  PHE n 
1 869  GLN n 
1 870  LEU n 
1 871  SER n 
1 872  LYS n 
1 873  TYR n 
1 874  VAL n 
1 875  ASP n 
1 876  ASN n 
1 877  GLN n 
1 878  ARG n 
1 879  LEU n 
1 880  LEU n 
1 881  SER n 
1 882  THR n 
1 883  PHE n 
1 884  THR n 
1 885  GLU n 
1 886  TYR n 
1 887  ILE n 
1 888  LYS n 
1 889  ASN n 
1 890  ILE n 
1 891  ILE n 
1 892  ASN n 
1 893  THR n 
1 894  SER n 
1 895  ILE n 
1 896  LEU n 
1 897  ASN n 
1 898  LEU n 
1 899  ARG n 
1 900  TYR n 
1 901  GLU n 
1 902  SER n 
1 903  ASN n 
1 904  HIS n 
1 905  LEU n 
1 906  ILE n 
1 907  ASP n 
1 908  LEU n 
1 909  SER n 
1 910  ARG n 
1 911  TYR n 
1 912  ALA n 
1 913  SER n 
1 914  LYS n 
1 915  ILE n 
1 916  ASN n 
1 917  ILE n 
1 918  GLY n 
1 919  SER n 
1 920  LYS n 
1 921  VAL n 
1 922  ASN n 
1 923  PHE n 
1 924  ASP n 
1 925  PRO n 
1 926  ILE n 
1 927  ASP n 
1 928  LYS n 
1 929  ASN n 
1 930  GLN n 
1 931  ILE n 
1 932  GLN n 
1 933  LEU n 
1 934  PHE n 
1 935  ASN n 
1 936  LEU n 
1 937  GLU n 
1 938  SER n 
1 939  SER n 
1 940  LYS n 
1 941  ILE n 
1 942  GLU n 
1 943  VAL n 
1 944  ILE n 
1 945  LEU n 
1 946  LYS n 
1 947  ASN n 
1 948  ALA n 
1 949  ILE n 
1 950  VAL n 
1 951  TYR n 
1 952  ASN n 
1 953  SER n 
1 954  MET n 
1 955  TYR n 
1 956  GLU n 
1 957  ASN n 
1 958  PHE n 
1 959  SER n 
1 960  THR n 
1 961  SER n 
1 962  PHE n 
1 963  TRP n 
1 964  ILE n 
1 965  ARG n 
1 966  ILE n 
1 967  PRO n 
1 968  LYS n 
1 969  TYR n 
1 970  PHE n 
1 971  ASN n 
1 972  SER n 
1 973  ILE n 
1 974  SER n 
1 975  LEU n 
1 976  ASN n 
1 977  ASN n 
1 978  GLU n 
1 979  TYR n 
1 980  THR n 
1 981  ILE n 
1 982  ILE n 
1 983  ASN n 
1 984  CYS n 
1 985  MET n 
1 986  GLU n 
1 987  ASN n 
1 988  ASN n 
1 989  SER n 
1 990  GLY n 
1 991  TRP n 
1 992  LYS n 
1 993  VAL n 
1 994  SER n 
1 995  LEU n 
1 996  ASN n 
1 997  TYR n 
1 998  GLY n 
1 999  GLU n 
1 1000 ILE n 
1 1001 ILE n 
1 1002 TRP n 
1 1003 THR n 
1 1004 LEU n 
1 1005 GLN n 
1 1006 ASP n 
1 1007 THR n 
1 1008 GLN n 
1 1009 GLU n 
1 1010 ILE n 
1 1011 LYS n 
1 1012 GLN n 
1 1013 ARG n 
1 1014 VAL n 
1 1015 VAL n 
1 1016 PHE n 
1 1017 LYS n 
1 1018 TYR n 
1 1019 SER n 
1 1020 GLN n 
1 1021 MET n 
1 1022 ILE n 
1 1023 ASN n 
1 1024 ILE n 
1 1025 SER n 
1 1026 ASP n 
1 1027 TYR n 
1 1028 ILE n 
1 1029 ASN n 
1 1030 ARG n 
1 1031 TRP n 
1 1032 ILE n 
1 1033 PHE n 
1 1034 VAL n 
1 1035 THR n 
1 1036 ILE n 
1 1037 THR n 
1 1038 ASN n 
1 1039 ASN n 
1 1040 ARG n 
1 1041 LEU n 
1 1042 ASN n 
1 1043 ASN n 
1 1044 SER n 
1 1045 LYS n 
1 1046 ILE n 
1 1047 TYR n 
1 1048 ILE n 
1 1049 ASN n 
1 1050 GLY n 
1 1051 ARG n 
1 1052 LEU n 
1 1053 ILE n 
1 1054 ASP n 
1 1055 GLN n 
1 1056 LYS n 
1 1057 PRO n 
1 1058 ILE n 
1 1059 SER n 
1 1060 ASN n 
1 1061 LEU n 
1 1062 GLY n 
1 1063 ASN n 
1 1064 ILE n 
1 1065 HIS n 
1 1066 ALA n 
1 1067 SER n 
1 1068 ASN n 
1 1069 ASN n 
1 1070 ILE n 
1 1071 MET n 
1 1072 PHE n 
1 1073 LYS n 
1 1074 LEU n 
1 1075 ASP n 
1 1076 GLY n 
1 1077 CYS n 
1 1078 ARG n 
1 1079 ASP n 
1 1080 THR n 
1 1081 HIS n 
1 1082 ARG n 
1 1083 TYR n 
1 1084 ILE n 
1 1085 TRP n 
1 1086 ILE n 
1 1087 LYS n 
1 1088 TYR n 
1 1089 PHE n 
1 1090 ASN n 
1 1091 LEU n 
1 1092 PHE n 
1 1093 ASP n 
1 1094 LYS n 
1 1095 GLU n 
1 1096 LEU n 
1 1097 ASN n 
1 1098 GLU n 
1 1099 LYS n 
1 1100 GLU n 
1 1101 ILE n 
1 1102 LYS n 
1 1103 ASP n 
1 1104 LEU n 
1 1105 TYR n 
1 1106 ASP n 
1 1107 ASN n 
1 1108 GLN n 
1 1109 SER n 
1 1110 ASN n 
1 1111 SER n 
1 1112 GLY n 
1 1113 ILE n 
1 1114 LEU n 
1 1115 LYS n 
1 1116 ASP n 
1 1117 PHE n 
1 1118 TRP n 
1 1119 GLY n 
1 1120 ASP n 
1 1121 TYR n 
1 1122 LEU n 
1 1123 GLN n 
1 1124 TYR n 
1 1125 ASP n 
1 1126 LYS n 
1 1127 PRO n 
1 1128 TYR n 
1 1129 TYR n 
1 1130 MET n 
1 1131 LEU n 
1 1132 ASN n 
1 1133 LEU n 
1 1134 TYR n 
1 1135 ASP n 
1 1136 PRO n 
1 1137 ASN n 
1 1138 LYS n 
1 1139 TYR n 
1 1140 VAL n 
1 1141 ASP n 
1 1142 VAL n 
1 1143 ASN n 
1 1144 ASN n 
1 1145 VAL n 
1 1146 GLY n 
1 1147 ILE n 
1 1148 ARG n 
1 1149 GLY n 
1 1150 TYR n 
1 1151 MET n 
1 1152 TYR n 
1 1153 LEU n 
1 1154 LYS n 
1 1155 GLY n 
1 1156 PRO n 
1 1157 ARG n 
1 1158 GLY n 
1 1159 SER n 
1 1160 VAL n 
1 1161 MET n 
1 1162 THR n 
1 1163 THR n 
1 1164 ASN n 
1 1165 ILE n 
1 1166 TYR n 
1 1167 LEU n 
1 1168 ASN n 
1 1169 SER n 
1 1170 SER n 
1 1171 LEU n 
1 1172 TYR n 
1 1173 ARG n 
1 1174 GLY n 
1 1175 ALA n 
1 1176 LYS n 
1 1177 PHE n 
1 1178 ILE n 
1 1179 ILE n 
1 1180 LYS n 
1 1181 LYS n 
1 1182 TYR n 
1 1183 ALA n 
1 1184 SER n 
1 1185 GLY n 
1 1186 ASN n 
1 1187 LYS n 
1 1188 ASP n 
1 1189 ASN n 
1 1190 ILE n 
1 1191 VAL n 
1 1192 ARG n 
1 1193 ASN n 
1 1194 ASN n 
1 1195 ASP n 
1 1196 ARG n 
1 1197 VAL n 
1 1198 TYR n 
1 1199 ILE n 
1 1200 ASN n 
1 1201 VAL n 
1 1202 VAL n 
1 1203 VAL n 
1 1204 LYS n 
1 1205 ASN n 
1 1206 LYS n 
1 1207 GLU n 
1 1208 TYR n 
1 1209 ARG n 
1 1210 LEU n 
1 1211 ALA n 
1 1212 THR n 
1 1213 ASN n 
1 1214 ALA n 
1 1215 SER n 
1 1216 GLN n 
1 1217 ALA n 
1 1218 GLY n 
1 1219 VAL n 
1 1220 GLU n 
1 1221 LYS n 
1 1222 ILE n 
1 1223 LEU n 
1 1224 SER n 
1 1225 ALA n 
1 1226 LEU n 
1 1227 GLU n 
1 1228 ILE n 
1 1229 PRO n 
1 1230 ASP n 
1 1231 VAL n 
1 1232 GLY n 
1 1233 ASN n 
1 1234 LEU n 
1 1235 SER n 
1 1236 GLN n 
1 1237 VAL n 
1 1238 VAL n 
1 1239 VAL n 
1 1240 MET n 
1 1241 LYS n 
1 1242 SER n 
1 1243 LYS n 
1 1244 ASN n 
1 1245 ASP n 
1 1246 GLN n 
1 1247 GLY n 
1 1248 ILE n 
1 1249 THR n 
1 1250 ASN n 
1 1251 LYS n 
1 1252 CYS n 
1 1253 LYS n 
1 1254 MET n 
1 1255 ASN n 
1 1256 LEU n 
1 1257 GLN n 
1 1258 ASP n 
1 1259 ASN n 
1 1260 ASN n 
1 1261 GLY n 
1 1262 ASN n 
1 1263 ASP n 
1 1264 ILE n 
1 1265 GLY n 
1 1266 PHE n 
1 1267 ILE n 
1 1268 GLY n 
1 1269 PHE n 
1 1270 HIS n 
1 1271 GLN n 
1 1272 PHE n 
1 1273 ASN n 
1 1274 ASN n 
1 1275 ILE n 
1 1276 ALA n 
1 1277 LYS n 
1 1278 LEU n 
1 1279 VAL n 
1 1280 ALA n 
1 1281 SER n 
1 1282 ASN n 
1 1283 TRP n 
1 1284 TYR n 
1 1285 ASN n 
1 1286 ARG n 
1 1287 GLN n 
1 1288 ILE n 
1 1289 GLU n 
1 1290 ARG n 
1 1291 SER n 
1 1292 SER n 
1 1293 ARG n 
1 1294 THR n 
1 1295 LEU n 
1 1296 GLY n 
1 1297 CYS n 
1 1298 SER n 
1 1299 TRP n 
1 1300 GLU n 
1 1301 PHE n 
1 1302 ILE n 
1 1303 PRO n 
1 1304 VAL n 
1 1305 ASP n 
1 1306 ASP n 
1 1307 GLY n 
1 1308 TRP n 
1 1309 GLY n 
1 1310 GLU n 
1 1311 ARG n 
1 1312 PRO n 
1 1313 LEU n 
1 1314 VAL n 
1 1315 PRO n 
1 1316 PRO n 
1 1317 THR n 
1 1318 PRO n 
1 1319 GLY n 
1 1320 SER n 
1 1321 ALA n 
1 1322 TRP n 
1 1323 SER n 
1 1324 HIS n 
1 1325 PRO n 
1 1326 GLN n 
1 1327 PHE n 
1 1328 GLU n 
1 1329 LYS n 
2 1    MET n 
2 2    ASP n 
2 3    ASP n 
2 4    TYR n 
2 5    LYS n 
2 6    TYR n 
2 7    GLN n 
2 8    ASP n 
2 9    ASN n 
2 10   TYR n 
2 11   GLY n 
2 12   GLY n 
2 13   TYR n 
2 14   ALA n 
2 15   PRO n 
2 16   SER n 
2 17   ASP n 
2 18   GLY n 
2 19   TYR n 
2 20   TYR n 
2 21   ARG n 
2 22   GLY n 
2 23   ASN n 
2 24   GLU n 
2 25   SER n 
2 26   ASN n 
2 27   PRO n 
2 28   GLU n 
2 29   GLU n 
2 30   ASP n 
2 31   ALA n 
2 32   GLN n 
2 33   SER n 
2 34   ASP n 
2 35   VAL n 
2 36   THR n 
2 37   GLU n 
2 38   GLY n 
2 39   HIS n 
2 40   ASP n 
2 41   GLU n 
2 42   GLU n 
2 43   ASP n 
2 44   GLU n 
2 45   ILE n 
2 46   TYR n 
2 47   GLU n 
2 48   GLY n 
2 49   GLU n 
2 50   TYR n 
2 51   GLN n 
2 52   GLY n 
2 53   ILE n 
2 54   PRO n 
2 55   HIS n 
2 56   PRO n 
2 57   ASP n 
2 58   ASP n 
2 59   VAL n 
2 60   LYS n 
2 61   ALA n 
2 62   LYS n 
2 63   GLN n 
2 64   ALA n 
2 65   LYS n 
2 66   MET n 
2 67   ALA n 
2 68   PRO n 
2 69   SER n 
2 70   ARG n 
2 71   MET n 
2 72   ASP n 
2 73   SER n 
2 74   LEU n 
2 75   ARG n 
2 76   GLY n 
2 77   GLN n 
2 78   THR n 
2 79   ASP n 
2 80   LEU n 
2 81   MET n 
2 82   ALA n 
2 83   GLU n 
2 84   ARG n 
2 85   LEU n 
2 86   GLU n 
2 87   ASP n 
2 88   GLU n 
2 89   GLU n 
2 90   GLN n 
2 91   LEU n 
2 92   ALA n 
2 93   HIS n 
2 94   GLN n 
2 95   TYR n 
2 96   GLU n 
2 97   THR n 
2 98   ILE n 
2 99   MET n 
2 100  ASP n 
2 101  GLU n 
2 102  CYS n 
2 103  GLY n 
2 104  HIS n 
2 105  GLY n 
2 106  ARG n 
2 107  PHE n 
2 108  GLN n 
2 109  TRP n 
2 110  ILE n 
2 111  LEU n 
2 112  PHE n 
2 113  PHE n 
2 114  VAL n 
2 115  LEU n 
2 116  GLY n 
2 117  LEU n 
2 118  ALA n 
2 119  LEU n 
2 120  MET n 
2 121  ALA n 
2 122  ASP n 
2 123  GLY n 
2 124  VAL n 
2 125  GLU n 
2 126  VAL n 
2 127  PHE n 
2 128  VAL n 
2 129  VAL n 
2 130  SER n 
2 131  PHE n 
2 132  ALA n 
2 133  LEU n 
2 134  PRO n 
2 135  SER n 
2 136  ALA n 
2 137  GLU n 
2 138  LYS n 
2 139  ASP n 
2 140  MET n 
2 141  CYS n 
2 142  LEU n 
2 143  SER n 
2 144  SER n 
2 145  SER n 
2 146  LYS n 
2 147  LYS n 
2 148  GLY n 
2 149  MET n 
2 150  LEU n 
2 151  GLY n 
2 152  MET n 
2 153  ILE n 
2 154  VAL n 
2 155  TYR n 
2 156  LEU n 
2 157  GLY n 
2 158  MET n 
2 159  MET n 
2 160  ALA n 
2 161  GLY n 
2 162  ALA n 
2 163  PHE n 
2 164  ILE n 
2 165  LEU n 
2 166  GLY n 
2 167  GLY n 
2 168  LEU n 
2 169  ALA n 
2 170  ASP n 
2 171  LYS n 
2 172  LEU n 
2 173  GLY n 
2 174  ARG n 
2 175  LYS n 
2 176  ARG n 
2 177  VAL n 
2 178  LEU n 
2 179  SER n 
2 180  MET n 
2 181  SER n 
2 182  LEU n 
2 183  ALA n 
2 184  VAL n 
2 185  ASN n 
2 186  ALA n 
2 187  SER n 
2 188  PHE n 
2 189  ALA n 
2 190  SER n 
2 191  LEU n 
2 192  SER n 
2 193  SER n 
2 194  PHE n 
2 195  VAL n 
2 196  GLN n 
2 197  GLY n 
2 198  TYR n 
2 199  GLY n 
2 200  ALA n 
2 201  PHE n 
2 202  LEU n 
2 203  PHE n 
2 204  CYS n 
2 205  ARG n 
2 206  LEU n 
2 207  ILE n 
2 208  SER n 
2 209  GLY n 
2 210  ILE n 
2 211  GLY n 
2 212  ILE n 
2 213  GLY n 
2 214  GLY n 
2 215  ALA n 
2 216  LEU n 
2 217  PRO n 
2 218  ILE n 
2 219  VAL n 
2 220  PHE n 
2 221  ALA n 
2 222  TYR n 
2 223  PHE n 
2 224  SER n 
2 225  GLU n 
2 226  PHE n 
2 227  LEU n 
2 228  SER n 
2 229  ARG n 
2 230  GLU n 
2 231  LYS n 
2 232  ARG n 
2 233  GLY n 
2 234  GLU n 
2 235  HIS n 
2 236  LEU n 
2 237  SER n 
2 238  TRP n 
2 239  LEU n 
2 240  GLY n 
2 241  ILE n 
2 242  PHE n 
2 243  TRP n 
2 244  MET n 
2 245  THR n 
2 246  GLY n 
2 247  GLY n 
2 248  LEU n 
2 249  TYR n 
2 250  ALA n 
2 251  SER n 
2 252  ALA n 
2 253  MET n 
2 254  ALA n 
2 255  TRP n 
2 256  SER n 
2 257  ILE n 
2 258  ILE n 
2 259  PRO n 
2 260  HIS n 
2 261  TYR n 
2 262  GLY n 
2 263  TRP n 
2 264  GLY n 
2 265  PHE n 
2 266  SER n 
2 267  MET n 
2 268  GLY n 
2 269  THR n 
2 270  ASN n 
2 271  TYR n 
2 272  HIS n 
2 273  PHE n 
2 274  HIS n 
2 275  SER n 
2 276  TRP n 
2 277  ARG n 
2 278  VAL n 
2 279  PHE n 
2 280  VAL n 
2 281  ILE n 
2 282  VAL n 
2 283  CYS n 
2 284  ALA n 
2 285  LEU n 
2 286  PRO n 
2 287  CYS n 
2 288  THR n 
2 289  VAL n 
2 290  SER n 
2 291  MET n 
2 292  VAL n 
2 293  ALA n 
2 294  LEU n 
2 295  LYS n 
2 296  PHE n 
2 297  MET n 
2 298  PRO n 
2 299  GLU n 
2 300  SER n 
2 301  PRO n 
2 302  ARG n 
2 303  PHE n 
2 304  LEU n 
2 305  LEU n 
2 306  GLU n 
2 307  MET n 
2 308  GLY n 
2 309  LYS n 
2 310  HIS n 
2 311  ASP n 
2 312  GLU n 
2 313  ALA n 
2 314  TRP n 
2 315  MET n 
2 316  ILE n 
2 317  LEU n 
2 318  LYS n 
2 319  GLN n 
2 320  VAL n 
2 321  HIS n 
2 322  ASP n 
2 323  THR n 
2 324  ASN n 
2 325  MET n 
2 326  ARG n 
2 327  ALA n 
2 328  LYS n 
2 329  GLY n 
2 330  THR n 
2 331  PRO n 
2 332  GLU n 
2 333  LYS n 
2 334  VAL n 
2 335  PHE n 
2 336  THR n 
2 337  VAL n 
2 338  SER n 
2 339  ASN n 
2 340  ILE n 
2 341  LYS n 
2 342  THR n 
2 343  PRO n 
2 344  LYS n 
2 345  GLN n 
2 346  MET n 
2 347  ASP n 
2 348  GLU n 
2 349  PHE n 
2 350  ILE n 
2 351  GLU n 
2 352  ILE n 
2 353  GLN n 
2 354  SER n 
2 355  SER n 
2 356  THR n 
2 357  GLY n 
2 358  THR n 
2 359  TRP n 
2 360  TYR n 
2 361  GLN n 
2 362  ARG n 
2 363  TRP n 
2 364  LEU n 
2 365  VAL n 
2 366  ARG n 
2 367  PHE n 
2 368  LYS n 
2 369  THR n 
2 370  ILE n 
2 371  PHE n 
2 372  LYS n 
2 373  GLN n 
2 374  VAL n 
2 375  TRP n 
2 376  ASP n 
2 377  ASN n 
2 378  ALA n 
2 379  LEU n 
2 380  TYR n 
2 381  CYS n 
2 382  VAL n 
2 383  MET n 
2 384  GLY n 
2 385  PRO n 
2 386  TYR n 
2 387  ARG n 
2 388  MET n 
2 389  ASN n 
2 390  THR n 
2 391  LEU n 
2 392  ILE n 
2 393  LEU n 
2 394  ALA n 
2 395  VAL n 
2 396  VAL n 
2 397  TRP n 
2 398  PHE n 
2 399  ALA n 
2 400  MET n 
2 401  ALA n 
2 402  PHE n 
2 403  SER n 
2 404  TYR n 
2 405  TYR n 
2 406  GLY n 
2 407  LEU n 
2 408  THR n 
2 409  VAL n 
2 410  TRP n 
2 411  PHE n 
2 412  PRO n 
2 413  ASP n 
2 414  MET n 
2 415  ILE n 
2 416  ARG n 
2 417  TYR n 
2 418  PHE n 
2 419  GLN n 
2 420  ASP n 
2 421  GLU n 
2 422  GLU n 
2 423  TYR n 
2 424  LYS n 
2 425  SER n 
2 426  LYS n 
2 427  MET n 
2 428  LYS n 
2 429  VAL n 
2 430  PHE n 
2 431  PHE n 
2 432  GLY n 
2 433  GLU n 
2 434  HIS n 
2 435  VAL n 
2 436  TYR n 
2 437  GLY n 
2 438  ALA n 
2 439  THR n 
2 440  ILE n 
2 441  ASN n 
2 442  PHE n 
2 443  THR n 
2 444  MET n 
2 445  GLU n 
2 446  ASN n 
2 447  GLN n 
2 448  ILE n 
2 449  HIS n 
2 450  GLN n 
2 451  HIS n 
2 452  GLY n 
2 453  LYS n 
2 454  LEU n 
2 455  VAL n 
2 456  ASN n 
2 457  ASP n 
2 458  LYS n 
2 459  PHE n 
2 460  THR n 
2 461  ARG n 
2 462  MET n 
2 463  TYR n 
2 464  PHE n 
2 465  LYS n 
2 466  HIS n 
2 467  VAL n 
2 468  LEU n 
2 469  PHE n 
2 470  GLU n 
2 471  ASP n 
2 472  THR n 
2 473  PHE n 
2 474  PHE n 
2 475  ASP n 
2 476  GLU n 
2 477  CYS n 
2 478  TYR n 
2 479  PHE n 
2 480  GLU n 
2 481  ASP n 
2 482  VAL n 
2 483  THR n 
2 484  SER n 
2 485  THR n 
2 486  ASP n 
2 487  THR n 
2 488  TYR n 
2 489  PHE n 
2 490  LYS n 
2 491  ASN n 
2 492  CYS n 
2 493  THR n 
2 494  ILE n 
2 495  GLU n 
2 496  SER n 
2 497  THR n 
2 498  ILE n 
2 499  PHE n 
2 500  TYR n 
2 501  ASN n 
2 502  THR n 
2 503  ASP n 
2 504  LEU n 
2 505  TYR n 
2 506  GLU n 
2 507  HIS n 
2 508  LYS n 
2 509  PHE n 
2 510  ILE n 
2 511  ASN n 
2 512  CYS n 
2 513  ARG n 
2 514  PHE n 
2 515  ILE n 
2 516  ASN n 
2 517  SER n 
2 518  THR n 
2 519  PHE n 
2 520  LEU n 
2 521  GLU n 
2 522  GLN n 
2 523  LYS n 
2 524  GLU n 
2 525  GLY n 
2 526  CYS n 
2 527  HIS n 
2 528  MET n 
2 529  ASP n 
2 530  LEU n 
2 531  GLU n 
2 532  GLN n 
2 533  ASP n 
2 534  ASN n 
2 535  ASP n 
2 536  PHE n 
2 537  LEU n 
2 538  ILE n 
2 539  TYR n 
2 540  LEU n 
2 541  VAL n 
2 542  SER n 
2 543  PHE n 
2 544  LEU n 
2 545  GLY n 
2 546  SER n 
2 547  LEU n 
2 548  SER n 
2 549  VAL n 
2 550  LEU n 
2 551  PRO n 
2 552  GLY n 
2 553  ASN n 
2 554  ILE n 
2 555  ILE n 
2 556  SER n 
2 557  ALA n 
2 558  LEU n 
2 559  LEU n 
2 560  MET n 
2 561  ASP n 
2 562  ARG n 
2 563  ILE n 
2 564  GLY n 
2 565  ARG n 
2 566  LEU n 
2 567  LYS n 
2 568  MET n 
2 569  ILE n 
2 570  GLY n 
2 571  GLY n 
2 572  SER n 
2 573  MET n 
2 574  LEU n 
2 575  ILE n 
2 576  SER n 
2 577  ALA n 
2 578  VAL n 
2 579  CYS n 
2 580  CYS n 
2 581  PHE n 
2 582  PHE n 
2 583  LEU n 
2 584  PHE n 
2 585  PHE n 
2 586  GLY n 
2 587  ASN n 
2 588  SER n 
2 589  GLU n 
2 590  SER n 
2 591  ALA n 
2 592  MET n 
2 593  ILE n 
2 594  GLY n 
2 595  TRP n 
2 596  GLN n 
2 597  CYS n 
2 598  LEU n 
2 599  PHE n 
2 600  CYS n 
2 601  GLY n 
2 602  THR n 
2 603  SER n 
2 604  ILE n 
2 605  ALA n 
2 606  ALA n 
2 607  TRP n 
2 608  ASN n 
2 609  ALA n 
2 610  LEU n 
2 611  ASP n 
2 612  VAL n 
2 613  ILE n 
2 614  THR n 
2 615  VAL n 
2 616  GLU n 
2 617  LEU n 
2 618  TYR n 
2 619  PRO n 
2 620  THR n 
2 621  ASN n 
2 622  GLN n 
2 623  ARG n 
2 624  ALA n 
2 625  THR n 
2 626  ALA n 
2 627  PHE n 
2 628  GLY n 
2 629  ILE n 
2 630  LEU n 
2 631  ASN n 
2 632  GLY n 
2 633  LEU n 
2 634  CYS n 
2 635  LYS n 
2 636  PHE n 
2 637  GLY n 
2 638  ALA n 
2 639  ILE n 
2 640  LEU n 
2 641  GLY n 
2 642  ASN n 
2 643  THR n 
2 644  ILE n 
2 645  PHE n 
2 646  ALA n 
2 647  SER n 
2 648  PHE n 
2 649  VAL n 
2 650  GLY n 
2 651  ILE n 
2 652  THR n 
2 653  LYS n 
2 654  VAL n 
2 655  VAL n 
2 656  PRO n 
2 657  ILE n 
2 658  LEU n 
2 659  LEU n 
2 660  ALA n 
2 661  ALA n 
2 662  ALA n 
2 663  SER n 
2 664  LEU n 
2 665  VAL n 
2 666  GLY n 
2 667  GLY n 
2 668  GLY n 
2 669  LEU n 
2 670  ILE n 
2 671  ALA n 
2 672  LEU n 
2 673  ARG n 
2 674  LEU n 
2 675  PRO n 
2 676  GLU n 
2 677  THR n 
2 678  ARG n 
2 679  GLU n 
2 680  GLN n 
2 681  VAL n 
2 682  LEU n 
2 683  MET 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 1329 ?     ? 'botA, atx, bonT' ? ? ? ? ? ? 'Clostridium botulinum' 1491 ? ? ? ? ? ? ? ? 
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
866768 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 683  human ? 'SV2B, KIAA0735'  ? ? ? ? ? ? 'Homo sapiens'          9606 ? ? ? ? ? ? ? ? 
'Homo sapiens'                              9606   ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 LFucpa1-6DGlcpNAcb1-ROH 'Glycam Condensed Sequence' GMML       1.0   
2 3 'WURCS=2.0/2,2,1/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-2/a6-b1' WURCS                       PDB2Glycan 1.1.0 
3 3 '[][D-1-deoxy-GlcpNAc]{[(6+1)][b-L-Fucp]{}}' LINUCS                      PDB-CARE   ?     
4 4 'DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-ROH' 'Glycam Condensed Sequence' GMML       1.0   
5 4 
'WURCS=2.0/4,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5][a1221m-1a_1-5]/1-1-2-3-3-4/a4-b1_a6-f1_b4-c1_c3-d1_c6-e1' 
WURCS                       PDB2Glycan 1.1.0 
6 4 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}[(6+1)][a-L-Fucp]{}}' 
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 FUC C1 O1 1 NAG O6 HO6 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 O3 HO3 sing ? 
5 4 5 MAN C1 O1 3 BMA O6 HO6 sing ? 
6 4 6 FUC C1 O1 1 NAG O6 HO6 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 
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 
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 
FUC 'L-saccharide, alpha linking' . alpha-L-fucopyranose                     
'alpha-L-fucose; 6-deoxy-alpha-L-galactopyranose; L-fucose; fucose' 'C6 H12 O5'      164.156 
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 
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                            
FUC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 LFucpa                         
FUC 'COMMON NAME'                         GMML     1.0 a-L-fucopyranose               
FUC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-L-Fucp                       
FUC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Fuc                            
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    -16  ?    ?   ?   B . n 
A 1 2    ARG 2    -15  ?    ?   ?   B . n 
A 1 3    GLY 3    -14  ?    ?   ?   B . n 
A 1 4    SER 4    -13  ?    ?   ?   B . n 
A 1 5    HIS 5    -12  ?    ?   ?   B . n 
A 1 6    HIS 6    -11  ?    ?   ?   B . n 
A 1 7    HIS 7    -10  ?    ?   ?   B . n 
A 1 8    HIS 8    -9   ?    ?   ?   B . n 
A 1 9    HIS 9    -8   ?    ?   ?   B . n 
A 1 10   HIS 10   -7   ?    ?   ?   B . n 
A 1 11   GLY 11   -6   ?    ?   ?   B . n 
A 1 12   SER 12   -5   ?    ?   ?   B . n 
A 1 13   LEU 13   -4   ?    ?   ?   B . n 
A 1 14   VAL 14   -3   ?    ?   ?   B . n 
A 1 15   PRO 15   -2   ?    ?   ?   B . n 
A 1 16   ARG 16   -1   ?    ?   ?   B . n 
A 1 17   GLY 17   0    ?    ?   ?   B . n 
A 1 18   SER 18   1    1    SER SER B . n 
A 1 19   PRO 19   2    2    PRO PRO B . n 
A 1 20   PHE 20   3    3    PHE PHE B . n 
A 1 21   VAL 21   4    4    VAL VAL B . n 
A 1 22   ASN 22   5    5    ASN ASN B . n 
A 1 23   LYS 23   6    6    LYS LYS B . n 
A 1 24   GLN 24   7    7    GLN GLN B . n 
A 1 25   PHE 25   8    8    PHE PHE B . n 
A 1 26   ASN 26   9    9    ASN ASN B . n 
A 1 27   TYR 27   10   10   TYR TYR B . n 
A 1 28   LYS 28   11   11   LYS LYS B . n 
A 1 29   ASP 29   12   12   ASP ASP B . n 
A 1 30   PRO 30   13   13   PRO PRO B . n 
A 1 31   VAL 31   14   14   VAL VAL B . n 
A 1 32   ASN 32   15   15   ASN ASN B . n 
A 1 33   GLY 33   16   16   GLY GLY B . n 
A 1 34   VAL 34   17   17   VAL VAL B . n 
A 1 35   ASP 35   18   18   ASP ASP B . n 
A 1 36   ILE 36   19   19   ILE ILE B . n 
A 1 37   ALA 37   20   20   ALA ALA B . n 
A 1 38   TYR 38   21   21   TYR TYR B . n 
A 1 39   ILE 39   22   22   ILE ILE B . n 
A 1 40   LYS 40   23   23   LYS LYS B . n 
A 1 41   ILE 41   24   24   ILE ILE B . n 
A 1 42   PRO 42   25   25   PRO PRO B . n 
A 1 43   ASN 43   26   26   ASN ASN B . n 
A 1 44   ALA 44   27   27   ALA ALA B . n 
A 1 45   GLY 45   28   28   GLY GLY B . n 
A 1 46   GLN 46   29   29   GLN GLN B . n 
A 1 47   MET 47   30   30   MET MET B . n 
A 1 48   GLN 48   31   31   GLN GLN B . n 
A 1 49   PRO 49   32   32   PRO PRO B . n 
A 1 50   VAL 50   33   33   VAL VAL B . n 
A 1 51   LYS 51   34   34   LYS LYS B . n 
A 1 52   ALA 52   35   35   ALA ALA B . n 
A 1 53   PHE 53   36   36   PHE PHE B . n 
A 1 54   LYS 54   37   37   LYS LYS B . n 
A 1 55   ILE 55   38   38   ILE ILE B . n 
A 1 56   HIS 56   39   39   HIS HIS B . n 
A 1 57   ASN 57   40   40   ASN ASN B . n 
A 1 58   LYS 58   41   41   LYS LYS B . n 
A 1 59   ILE 59   42   42   ILE ILE B . n 
A 1 60   TRP 60   43   43   TRP TRP B . n 
A 1 61   VAL 61   44   44   VAL VAL B . n 
A 1 62   ILE 62   45   45   ILE ILE B . n 
A 1 63   PRO 63   46   46   PRO PRO B . n 
A 1 64   GLU 64   47   47   GLU GLU B . n 
A 1 65   ARG 65   48   48   ARG ARG B . n 
A 1 66   ASP 66   49   49   ASP ASP B . n 
A 1 67   THR 67   50   50   THR THR B . n 
A 1 68   PHE 68   51   51   PHE PHE B . n 
A 1 69   THR 69   52   52   THR THR B . n 
A 1 70   ASN 70   53   53   ASN ASN B . n 
A 1 71   PRO 71   54   54   PRO PRO B . n 
A 1 72   GLU 72   55   55   GLU GLU B . n 
A 1 73   GLU 73   56   56   GLU GLU B . n 
A 1 74   GLY 74   57   57   GLY GLY B . n 
A 1 75   ASP 75   58   58   ASP ASP B . n 
A 1 76   LEU 76   59   59   LEU LEU B . n 
A 1 77   ASN 77   60   60   ASN ASN B . n 
A 1 78   PRO 78   61   61   PRO PRO B . n 
A 1 79   PRO 79   62   62   PRO PRO B . n 
A 1 80   PRO 80   63   63   PRO PRO B . n 
A 1 81   GLU 81   64   64   GLU GLU B . n 
A 1 82   ALA 82   65   65   ALA ALA B . n 
A 1 83   LYS 83   66   66   LYS LYS B . n 
A 1 84   GLN 84   67   67   GLN GLN B . n 
A 1 85   VAL 85   68   68   VAL VAL B . n 
A 1 86   PRO 86   69   69   PRO PRO B . n 
A 1 87   VAL 87   70   70   VAL VAL B . n 
A 1 88   SER 88   71   71   SER SER B . n 
A 1 89   TYR 89   72   72   TYR TYR B . n 
A 1 90   TYR 90   73   73   TYR TYR B . n 
A 1 91   ASP 91   74   74   ASP ASP B . n 
A 1 92   SER 92   75   75   SER SER B . n 
A 1 93   THR 93   76   76   THR THR B . n 
A 1 94   TYR 94   77   77   TYR TYR B . n 
A 1 95   LEU 95   78   78   LEU LEU B . n 
A 1 96   SER 96   79   79   SER SER B . n 
A 1 97   THR 97   80   80   THR THR B . n 
A 1 98   ASP 98   81   81   ASP ASP B . n 
A 1 99   ASN 99   82   82   ASN ASN B . n 
A 1 100  GLU 100  83   83   GLU GLU B . n 
A 1 101  LYS 101  84   84   LYS LYS B . n 
A 1 102  ASP 102  85   85   ASP ASP B . n 
A 1 103  ASN 103  86   86   ASN ASN B . n 
A 1 104  TYR 104  87   87   TYR TYR B . n 
A 1 105  LEU 105  88   88   LEU LEU B . n 
A 1 106  LYS 106  89   89   LYS LYS B . n 
A 1 107  GLY 107  90   90   GLY GLY B . n 
A 1 108  VAL 108  91   91   VAL VAL B . n 
A 1 109  THR 109  92   92   THR THR B . n 
A 1 110  LYS 110  93   93   LYS LYS B . n 
A 1 111  LEU 111  94   94   LEU LEU B . n 
A 1 112  PHE 112  95   95   PHE PHE B . n 
A 1 113  GLU 113  96   96   GLU GLU B . n 
A 1 114  ARG 114  97   97   ARG ARG B . n 
A 1 115  ILE 115  98   98   ILE ILE B . n 
A 1 116  TYR 116  99   99   TYR TYR B . n 
A 1 117  SER 117  100  100  SER SER B . n 
A 1 118  THR 118  101  101  THR THR B . n 
A 1 119  ASP 119  102  102  ASP ASP B . n 
A 1 120  LEU 120  103  103  LEU LEU B . n 
A 1 121  GLY 121  104  104  GLY GLY B . n 
A 1 122  ARG 122  105  105  ARG ARG B . n 
A 1 123  MET 123  106  106  MET MET B . n 
A 1 124  LEU 124  107  107  LEU LEU B . n 
A 1 125  LEU 125  108  108  LEU LEU B . n 
A 1 126  THR 126  109  109  THR THR B . n 
A 1 127  SER 127  110  110  SER SER B . n 
A 1 128  ILE 128  111  111  ILE ILE B . n 
A 1 129  VAL 129  112  112  VAL VAL B . n 
A 1 130  ARG 130  113  113  ARG ARG B . n 
A 1 131  GLY 131  114  114  GLY GLY B . n 
A 1 132  ILE 132  115  115  ILE ILE B . n 
A 1 133  PRO 133  116  116  PRO PRO B . n 
A 1 134  PHE 134  117  117  PHE PHE B . n 
A 1 135  TRP 135  118  118  TRP TRP B . n 
A 1 136  GLY 136  119  119  GLY GLY B . n 
A 1 137  GLY 137  120  120  GLY GLY B . n 
A 1 138  SER 138  121  121  SER SER B . n 
A 1 139  THR 139  122  122  THR THR B . n 
A 1 140  ILE 140  123  123  ILE ILE B . n 
A 1 141  ASP 141  124  124  ASP ASP B . n 
A 1 142  THR 142  125  125  THR THR B . n 
A 1 143  GLU 143  126  126  GLU GLU B . n 
A 1 144  LEU 144  127  127  LEU LEU B . n 
A 1 145  LYS 145  128  128  LYS LYS B . n 
A 1 146  VAL 146  129  129  VAL VAL B . n 
A 1 147  ILE 147  130  130  ILE ILE B . n 
A 1 148  ASP 148  131  131  ASP ASP B . n 
A 1 149  THR 149  132  132  THR THR B . n 
A 1 150  ASN 150  133  133  ASN ASN B . n 
A 1 151  CYS 151  134  134  CYS CYS B . n 
A 1 152  ILE 152  135  135  ILE ILE B . n 
A 1 153  ASN 153  136  136  ASN ASN B . n 
A 1 154  VAL 154  137  137  VAL VAL B . n 
A 1 155  ILE 155  138  138  ILE ILE B . n 
A 1 156  GLN 156  139  139  GLN GLN B . n 
A 1 157  PRO 157  140  140  PRO PRO B . n 
A 1 158  ASP 158  141  141  ASP ASP B . n 
A 1 159  GLY 159  142  142  GLY GLY B . n 
A 1 160  SER 160  143  143  SER SER B . n 
A 1 161  TYR 161  144  144  TYR TYR B . n 
A 1 162  ARG 162  145  145  ARG ARG B . n 
A 1 163  SER 163  146  146  SER SER B . n 
A 1 164  GLU 164  147  147  GLU GLU B . n 
A 1 165  GLU 165  148  148  GLU GLU B . n 
A 1 166  LEU 166  149  149  LEU LEU B . n 
A 1 167  ASN 167  150  150  ASN ASN B . n 
A 1 168  LEU 168  151  151  LEU LEU B . n 
A 1 169  VAL 169  152  152  VAL VAL B . n 
A 1 170  ILE 170  153  153  ILE ILE B . n 
A 1 171  ILE 171  154  154  ILE ILE B . n 
A 1 172  GLY 172  155  155  GLY GLY B . n 
A 1 173  PRO 173  156  156  PRO PRO B . n 
A 1 174  SER 174  157  157  SER SER B . n 
A 1 175  ALA 175  158  158  ALA ALA B . n 
A 1 176  ASP 176  159  159  ASP ASP B . n 
A 1 177  ILE 177  160  160  ILE ILE B . n 
A 1 178  ILE 178  161  161  ILE ILE B . n 
A 1 179  GLN 179  162  162  GLN GLN B . n 
A 1 180  PHE 180  163  163  PHE PHE B . n 
A 1 181  GLU 181  164  164  GLU GLU B . n 
A 1 182  CYS 182  165  165  CYS CYS B . n 
A 1 183  LYS 183  166  166  LYS LYS B . n 
A 1 184  SER 184  167  167  SER SER B . n 
A 1 185  PHE 185  168  168  PHE PHE B . n 
A 1 186  GLY 186  169  169  GLY GLY B . n 
A 1 187  HIS 187  170  170  HIS HIS B . n 
A 1 188  GLU 188  171  171  GLU GLU B . n 
A 1 189  VAL 189  172  172  VAL VAL B . n 
A 1 190  LEU 190  173  173  LEU LEU B . n 
A 1 191  ASN 191  174  174  ASN ASN B . n 
A 1 192  LEU 192  175  175  LEU LEU B . n 
A 1 193  THR 193  176  176  THR THR B . n 
A 1 194  ARG 194  177  177  ARG ARG B . n 
A 1 195  ASN 195  178  178  ASN ASN B . n 
A 1 196  GLY 196  179  179  GLY GLY B . n 
A 1 197  TYR 197  180  180  TYR TYR B . n 
A 1 198  GLY 198  181  181  GLY GLY B . n 
A 1 199  SER 199  182  182  SER SER B . n 
A 1 200  THR 200  183  183  THR THR B . n 
A 1 201  GLN 201  184  184  GLN GLN B . n 
A 1 202  TYR 202  185  185  TYR TYR B . n 
A 1 203  ILE 203  186  186  ILE ILE B . n 
A 1 204  ARG 204  187  187  ARG ARG B . n 
A 1 205  PHE 205  188  188  PHE PHE B . n 
A 1 206  SER 206  189  189  SER SER B . n 
A 1 207  PRO 207  190  190  PRO PRO B . n 
A 1 208  ASP 208  191  191  ASP ASP B . n 
A 1 209  PHE 209  192  192  PHE PHE B . n 
A 1 210  THR 210  193  193  THR THR B . n 
A 1 211  PHE 211  194  194  PHE PHE B . n 
A 1 212  GLY 212  195  195  GLY GLY B . n 
A 1 213  PHE 213  196  196  PHE PHE B . n 
A 1 214  GLU 214  197  197  GLU GLU B . n 
A 1 215  GLU 215  198  198  GLU GLU B . n 
A 1 216  SER 216  199  199  SER SER B . n 
A 1 217  LEU 217  200  200  LEU LEU B . n 
A 1 218  GLU 218  201  201  GLU GLU B . n 
A 1 219  VAL 219  202  202  VAL VAL B . n 
A 1 220  ASP 220  203  203  ASP ASP B . n 
A 1 221  THR 221  204  204  THR THR B . n 
A 1 222  ASN 222  205  205  ASN ASN B . n 
A 1 223  PRO 223  206  206  PRO PRO B . n 
A 1 224  LEU 224  207  207  LEU LEU B . n 
A 1 225  LEU 225  208  208  LEU LEU B . n 
A 1 226  GLY 226  209  209  GLY GLY B . n 
A 1 227  ALA 227  210  210  ALA ALA B . n 
A 1 228  GLY 228  211  211  GLY GLY B . n 
A 1 229  LYS 229  212  212  LYS LYS B . n 
A 1 230  PHE 230  213  213  PHE PHE B . n 
A 1 231  ALA 231  214  214  ALA ALA B . n 
A 1 232  THR 232  215  215  THR THR B . n 
A 1 233  ASP 233  216  216  ASP ASP B . n 
A 1 234  PRO 234  217  217  PRO PRO B . n 
A 1 235  ALA 235  218  218  ALA ALA B . n 
A 1 236  VAL 236  219  219  VAL VAL B . n 
A 1 237  THR 237  220  220  THR THR B . n 
A 1 238  LEU 238  221  221  LEU LEU B . n 
A 1 239  ALA 239  222  222  ALA ALA B . n 
A 1 240  HIS 240  223  223  HIS HIS B . n 
A 1 241  GLN 241  224  224  GLN GLN B . n 
A 1 242  LEU 242  225  225  LEU LEU B . n 
A 1 243  ILE 243  226  226  ILE ILE B . n 
A 1 244  HIS 244  227  227  HIS HIS B . n 
A 1 245  ALA 245  228  228  ALA ALA B . n 
A 1 246  GLY 246  229  229  GLY GLY B . n 
A 1 247  HIS 247  230  230  HIS HIS B . n 
A 1 248  ARG 248  231  231  ARG ARG B . n 
A 1 249  LEU 249  232  232  LEU LEU B . n 
A 1 250  TYR 250  233  233  TYR TYR B . n 
A 1 251  GLY 251  234  234  GLY GLY B . n 
A 1 252  ILE 252  235  235  ILE ILE B . n 
A 1 253  ALA 253  236  236  ALA ALA B . n 
A 1 254  ILE 254  237  237  ILE ILE B . n 
A 1 255  ASN 255  238  238  ASN ASN B . n 
A 1 256  PRO 256  239  239  PRO PRO B . n 
A 1 257  ASN 257  240  240  ASN ASN B . n 
A 1 258  ARG 258  241  241  ARG ARG B . n 
A 1 259  VAL 259  242  242  VAL VAL B . n 
A 1 260  PHE 260  243  243  PHE PHE B . n 
A 1 261  LYS 261  244  244  LYS LYS B . n 
A 1 262  VAL 262  245  245  VAL VAL B . n 
A 1 263  ASN 263  246  246  ASN ASN B . n 
A 1 264  THR 264  247  247  THR THR B . n 
A 1 265  ASN 265  248  248  ASN ASN B . n 
A 1 266  ALA 266  249  249  ALA ALA B . n 
A 1 267  TYR 267  250  250  TYR TYR B . n 
A 1 268  TYR 268  251  251  TYR TYR B . n 
A 1 269  GLU 269  252  252  GLU GLU B . n 
A 1 270  MET 270  253  253  MET MET B . n 
A 1 271  SER 271  254  254  SER SER B . n 
A 1 272  GLY 272  255  255  GLY GLY B . n 
A 1 273  LEU 273  256  256  LEU LEU B . n 
A 1 274  GLU 274  257  257  GLU GLU B . n 
A 1 275  VAL 275  258  258  VAL VAL B . n 
A 1 276  SER 276  259  259  SER SER B . n 
A 1 277  PHE 277  260  260  PHE PHE B . n 
A 1 278  GLU 278  261  261  GLU GLU B . n 
A 1 279  GLU 279  262  262  GLU GLU B . n 
A 1 280  LEU 280  263  263  LEU LEU B . n 
A 1 281  ARG 281  264  264  ARG ARG B . n 
A 1 282  THR 282  265  265  THR THR B . n 
A 1 283  PHE 283  266  266  PHE PHE B . n 
A 1 284  GLY 284  267  267  GLY GLY B . n 
A 1 285  GLY 285  268  268  GLY GLY B . n 
A 1 286  HIS 286  269  269  HIS HIS B . n 
A 1 287  ASP 287  270  270  ASP ASP B . n 
A 1 288  ALA 288  271  271  ALA ALA B . n 
A 1 289  LYS 289  272  272  LYS LYS B . n 
A 1 290  PHE 290  273  273  PHE PHE B . n 
A 1 291  ILE 291  274  274  ILE ILE B . n 
A 1 292  ASP 292  275  275  ASP ASP B . n 
A 1 293  SER 293  276  276  SER SER B . n 
A 1 294  LEU 294  277  277  LEU LEU B . n 
A 1 295  GLN 295  278  278  GLN GLN B . n 
A 1 296  GLU 296  279  279  GLU GLU B . n 
A 1 297  ASN 297  280  280  ASN ASN B . n 
A 1 298  GLU 298  281  281  GLU GLU B . n 
A 1 299  PHE 299  282  282  PHE PHE B . n 
A 1 300  ARG 300  283  283  ARG ARG B . n 
A 1 301  LEU 301  284  284  LEU LEU B . n 
A 1 302  TYR 302  285  285  TYR TYR B . n 
A 1 303  TYR 303  286  286  TYR TYR B . n 
A 1 304  TYR 304  287  287  TYR TYR B . n 
A 1 305  ASN 305  288  288  ASN ASN B . n 
A 1 306  LYS 306  289  289  LYS LYS B . n 
A 1 307  PHE 307  290  290  PHE PHE B . n 
A 1 308  LYS 308  291  291  LYS LYS B . n 
A 1 309  ASP 309  292  292  ASP ASP B . n 
A 1 310  ILE 310  293  293  ILE ILE B . n 
A 1 311  ALA 311  294  294  ALA ALA B . n 
A 1 312  SER 312  295  295  SER SER B . n 
A 1 313  THR 313  296  296  THR THR B . n 
A 1 314  LEU 314  297  297  LEU LEU B . n 
A 1 315  ASN 315  298  298  ASN ASN B . n 
A 1 316  LYS 316  299  299  LYS LYS B . n 
A 1 317  ALA 317  300  300  ALA ALA B . n 
A 1 318  LYS 318  301  301  LYS LYS B . n 
A 1 319  SER 319  302  302  SER SER B . n 
A 1 320  ILE 320  303  303  ILE ILE B . n 
A 1 321  VAL 321  304  304  VAL VAL B . n 
A 1 322  GLY 322  305  305  GLY GLY B . n 
A 1 323  THR 323  306  306  THR THR B . n 
A 1 324  THR 324  307  307  THR THR B . n 
A 1 325  ALA 325  308  308  ALA ALA B . n 
A 1 326  SER 326  309  309  SER SER B . n 
A 1 327  LEU 327  310  310  LEU LEU B . n 
A 1 328  GLN 328  311  311  GLN GLN B . n 
A 1 329  TYR 329  312  312  TYR TYR B . n 
A 1 330  MET 330  313  313  MET MET B . n 
A 1 331  LYS 331  314  314  LYS LYS B . n 
A 1 332  ASN 332  315  315  ASN ASN B . n 
A 1 333  VAL 333  316  316  VAL VAL B . n 
A 1 334  PHE 334  317  317  PHE PHE B . n 
A 1 335  LYS 335  318  318  LYS LYS B . n 
A 1 336  GLU 336  319  319  GLU GLU B . n 
A 1 337  LYS 337  320  320  LYS LYS B . n 
A 1 338  TYR 338  321  321  TYR TYR B . n 
A 1 339  LEU 339  322  322  LEU LEU B . n 
A 1 340  LEU 340  323  323  LEU LEU B . n 
A 1 341  SER 341  324  324  SER SER B . n 
A 1 342  GLU 342  325  325  GLU GLU B . n 
A 1 343  ASP 343  326  326  ASP ASP B . n 
A 1 344  THR 344  327  327  THR THR B . n 
A 1 345  SER 345  328  328  SER SER B . n 
A 1 346  GLY 346  329  329  GLY GLY B . n 
A 1 347  LYS 347  330  330  LYS LYS B . n 
A 1 348  PHE 348  331  331  PHE PHE B . n 
A 1 349  SER 349  332  332  SER SER B . n 
A 1 350  VAL 350  333  333  VAL VAL B . n 
A 1 351  ASP 351  334  334  ASP ASP B . n 
A 1 352  LYS 352  335  335  LYS LYS B . n 
A 1 353  LEU 353  336  336  LEU LEU B . n 
A 1 354  LYS 354  337  337  LYS LYS B . n 
A 1 355  PHE 355  338  338  PHE PHE B . n 
A 1 356  ASP 356  339  339  ASP ASP B . n 
A 1 357  LYS 357  340  340  LYS LYS B . n 
A 1 358  LEU 358  341  341  LEU LEU B . n 
A 1 359  TYR 359  342  342  TYR TYR B . n 
A 1 360  LYS 360  343  343  LYS LYS B . n 
A 1 361  MET 361  344  344  MET MET B . n 
A 1 362  LEU 362  345  345  LEU LEU B . n 
A 1 363  THR 363  346  346  THR THR B . n 
A 1 364  GLU 364  347  347  GLU GLU B . n 
A 1 365  ILE 365  348  348  ILE ILE B . n 
A 1 366  TYR 366  349  349  TYR TYR B . n 
A 1 367  THR 367  350  350  THR THR B . n 
A 1 368  GLU 368  351  351  GLU GLU B . n 
A 1 369  ASP 369  352  352  ASP ASP B . n 
A 1 370  ASN 370  353  353  ASN ASN B . n 
A 1 371  PHE 371  354  354  PHE PHE B . n 
A 1 372  VAL 372  355  355  VAL VAL B . n 
A 1 373  LYS 373  356  356  LYS LYS B . n 
A 1 374  PHE 374  357  357  PHE PHE B . n 
A 1 375  PHE 375  358  358  PHE PHE B . n 
A 1 376  LYS 376  359  359  LYS LYS B . n 
A 1 377  VAL 377  360  360  VAL VAL B . n 
A 1 378  LEU 378  361  361  LEU LEU B . n 
A 1 379  ASN 379  362  362  ASN ASN B . n 
A 1 380  ALA 380  363  363  ALA ALA B . n 
A 1 381  LYS 381  364  364  LYS LYS B . n 
A 1 382  THR 382  365  365  THR THR B . n 
A 1 383  PHE 383  366  366  PHE PHE B . n 
A 1 384  LEU 384  367  367  LEU LEU B . n 
A 1 385  ASN 385  368  368  ASN ASN B . n 
A 1 386  PHE 386  369  369  PHE PHE B . n 
A 1 387  ASP 387  370  370  ASP ASP B . n 
A 1 388  LYS 388  371  371  LYS LYS B . n 
A 1 389  ALA 389  372  372  ALA ALA B . n 
A 1 390  VAL 390  373  373  VAL VAL B . n 
A 1 391  PHE 391  374  374  PHE PHE B . n 
A 1 392  LYS 392  375  375  LYS LYS B . n 
A 1 393  ILE 393  376  376  ILE ILE B . n 
A 1 394  ASN 394  377  377  ASN ASN B . n 
A 1 395  ILE 395  378  378  ILE ILE B . n 
A 1 396  VAL 396  379  379  VAL VAL B . n 
A 1 397  PRO 397  380  380  PRO PRO B . n 
A 1 398  LYS 398  381  381  LYS LYS B . n 
A 1 399  VAL 399  382  382  VAL VAL B . n 
A 1 400  ASN 400  383  383  ASN ASN B . n 
A 1 401  TYR 401  384  384  TYR TYR B . n 
A 1 402  THR 402  385  385  THR THR B . n 
A 1 403  ILE 403  386  386  ILE ILE B . n 
A 1 404  TYR 404  387  387  TYR TYR B . n 
A 1 405  ASP 405  388  388  ASP ASP B . n 
A 1 406  GLY 406  389  389  GLY GLY B . n 
A 1 407  PHE 407  390  390  PHE PHE B . n 
A 1 408  ASN 408  391  391  ASN ASN B . n 
A 1 409  LEU 409  392  392  LEU LEU B . n 
A 1 410  ARG 410  393  393  ARG ARG B . n 
A 1 411  ASN 411  394  394  ASN ASN B . n 
A 1 412  THR 412  395  395  THR THR B . n 
A 1 413  ASN 413  396  396  ASN ASN B . n 
A 1 414  LEU 414  397  397  LEU LEU B . n 
A 1 415  ALA 415  398  398  ALA ALA B . n 
A 1 416  ALA 416  399  399  ALA ALA B . n 
A 1 417  ASN 417  400  400  ASN ASN B . n 
A 1 418  PHE 418  401  401  PHE PHE B . n 
A 1 419  ASN 419  402  402  ASN ASN B . n 
A 1 420  GLY 420  403  403  GLY GLY B . n 
A 1 421  GLN 421  404  404  GLN GLN B . n 
A 1 422  ASN 422  405  405  ASN ASN B . n 
A 1 423  THR 423  406  406  THR THR B . n 
A 1 424  GLU 424  407  407  GLU GLU B . n 
A 1 425  ILE 425  408  408  ILE ILE B . n 
A 1 426  ASN 426  409  409  ASN ASN B . n 
A 1 427  ASN 427  410  410  ASN ASN B . n 
A 1 428  MET 428  411  411  MET MET B . n 
A 1 429  ASN 429  412  412  ASN ASN B . n 
A 1 430  PHE 430  413  413  PHE PHE B . n 
A 1 431  THR 431  414  414  THR THR B . n 
A 1 432  LYS 432  415  415  LYS LYS B . n 
A 1 433  LEU 433  416  416  LEU LEU B . n 
A 1 434  LYS 434  417  417  LYS LYS B . n 
A 1 435  ASN 435  418  418  ASN ASN B . n 
A 1 436  PHE 436  419  419  PHE PHE B . n 
A 1 437  THR 437  420  420  THR THR B . n 
A 1 438  GLY 438  421  421  GLY GLY B . n 
A 1 439  LEU 439  422  422  LEU LEU B . n 
A 1 440  PHE 440  423  423  PHE PHE B . n 
A 1 441  GLU 441  424  424  GLU GLU B . n 
A 1 442  PHE 442  425  425  PHE PHE B . n 
A 1 443  TYR 443  426  426  TYR TYR B . n 
A 1 444  LYS 444  427  427  LYS LYS B . n 
A 1 445  LEU 445  428  428  LEU LEU B . n 
A 1 446  LEU 446  429  429  LEU LEU B . n 
A 1 447  CYS 447  430  430  CYS CYS B . n 
A 1 448  VAL 448  431  431  VAL VAL B . n 
A 1 449  ARG 449  432  432  ARG ARG B . n 
A 1 450  GLY 450  433  ?    ?   ?   B . n 
A 1 451  ILE 451  434  ?    ?   ?   B . n 
A 1 452  ILE 452  435  ?    ?   ?   B . n 
A 1 453  THR 453  436  ?    ?   ?   B . n 
A 1 454  SER 454  437  ?    ?   ?   B . n 
A 1 455  LYS 455  438  ?    ?   ?   B . n 
A 1 456  THR 456  439  ?    ?   ?   B . n 
A 1 457  LYS 457  440  ?    ?   ?   B . n 
A 1 458  SER 458  441  ?    ?   ?   B . n 
A 1 459  LEU 459  442  ?    ?   ?   B . n 
A 1 460  ASP 460  443  ?    ?   ?   B . n 
A 1 461  LYS 461  444  ?    ?   ?   B . n 
A 1 462  GLY 462  445  ?    ?   ?   B . n 
A 1 463  TYR 463  446  ?    ?   ?   B . n 
A 1 464  ASN 464  447  ?    ?   ?   B . n 
A 1 465  LYS 465  448  ?    ?   ?   B . n 
A 1 466  ALA 466  449  ?    ?   ?   B . n 
A 1 467  LEU 467  450  ?    ?   ?   B . n 
A 1 468  ASN 468  451  ?    ?   ?   B . n 
A 1 469  ASP 469  452  452  ASP ASP B . n 
A 1 470  LEU 470  453  453  LEU LEU B . n 
A 1 471  CYS 471  454  454  CYS CYS B . n 
A 1 472  ILE 472  455  455  ILE ILE B . n 
A 1 473  LYS 473  456  456  LYS LYS B . n 
A 1 474  VAL 474  457  457  VAL VAL B . n 
A 1 475  ASN 475  458  458  ASN ASN B . n 
A 1 476  ASN 476  459  459  ASN ASN B . n 
A 1 477  TRP 477  460  460  TRP TRP B . n 
A 1 478  ASP 478  461  461  ASP ASP B . n 
A 1 479  LEU 479  462  462  LEU LEU B . n 
A 1 480  PHE 480  463  463  PHE PHE B . n 
A 1 481  PHE 481  464  464  PHE PHE B . n 
A 1 482  SER 482  465  465  SER SER B . n 
A 1 483  PRO 483  466  466  PRO PRO B . n 
A 1 484  SER 484  467  467  SER SER B . n 
A 1 485  GLU 485  468  468  GLU GLU B . n 
A 1 486  ASP 486  469  469  ASP ASP B . n 
A 1 487  ASN 487  470  470  ASN ASN B . n 
A 1 488  PHE 488  471  471  PHE PHE B . n 
A 1 489  THR 489  472  472  THR THR B . n 
A 1 490  ASN 490  473  473  ASN ASN B . n 
A 1 491  ASP 491  474  474  ASP ASP B . n 
A 1 492  LEU 492  475  475  LEU LEU B . n 
A 1 493  ASN 493  476  476  ASN ASN B . n 
A 1 494  LYS 494  477  477  LYS LYS B . n 
A 1 495  GLY 495  478  478  GLY GLY B . n 
A 1 496  GLU 496  479  479  GLU GLU B . n 
A 1 497  GLU 497  480  480  GLU GLU B . n 
A 1 498  ILE 498  481  481  ILE ILE B . n 
A 1 499  THR 499  482  482  THR THR B . n 
A 1 500  SER 500  483  483  SER SER B . n 
A 1 501  ASP 501  484  484  ASP ASP B . n 
A 1 502  THR 502  485  485  THR THR B . n 
A 1 503  ASN 503  486  486  ASN ASN B . n 
A 1 504  ILE 504  487  ?    ?   ?   B . n 
A 1 505  GLU 505  488  ?    ?   ?   B . n 
A 1 506  ALA 506  489  ?    ?   ?   B . n 
A 1 507  ALA 507  490  ?    ?   ?   B . n 
A 1 508  GLU 508  491  ?    ?   ?   B . n 
A 1 509  GLU 509  492  ?    ?   ?   B . n 
A 1 510  ASN 510  493  ?    ?   ?   B . n 
A 1 511  ILE 511  494  ?    ?   ?   B . n 
A 1 512  SER 512  495  495  SER SER B . n 
A 1 513  LEU 513  496  496  LEU LEU B . n 
A 1 514  ASP 514  497  497  ASP ASP B . n 
A 1 515  LEU 515  498  498  LEU LEU B . n 
A 1 516  ILE 516  499  499  ILE ILE B . n 
A 1 517  GLN 517  500  500  GLN GLN B . n 
A 1 518  GLN 518  501  501  GLN GLN B . n 
A 1 519  TYR 519  502  502  TYR TYR B . n 
A 1 520  TYR 520  503  503  TYR TYR B . n 
A 1 521  LEU 521  504  504  LEU LEU B . n 
A 1 522  THR 522  505  505  THR THR B . n 
A 1 523  PHE 523  506  506  PHE PHE B . n 
A 1 524  ASN 524  507  507  ASN ASN B . n 
A 1 525  PHE 525  508  508  PHE PHE B . n 
A 1 526  ASP 526  509  509  ASP ASP B . n 
A 1 527  ASN 527  510  510  ASN ASN B . n 
A 1 528  GLU 528  511  511  GLU GLU B . n 
A 1 529  PRO 529  512  512  PRO PRO B . n 
A 1 530  GLU 530  513  513  GLU GLU B . n 
A 1 531  ASN 531  514  514  ASN ASN B . n 
A 1 532  ILE 532  515  515  ILE ILE B . n 
A 1 533  SER 533  516  516  SER SER B . n 
A 1 534  ILE 534  517  517  ILE ILE B . n 
A 1 535  GLU 535  518  518  GLU GLU B . n 
A 1 536  ASN 536  519  519  ASN ASN B . n 
A 1 537  LEU 537  520  520  LEU LEU B . n 
A 1 538  SER 538  521  521  SER SER B . n 
A 1 539  SER 539  522  522  SER SER B . n 
A 1 540  ASP 540  523  523  ASP ASP B . n 
A 1 541  ILE 541  524  524  ILE ILE B . n 
A 1 542  ILE 542  525  525  ILE ILE B . n 
A 1 543  GLY 543  526  526  GLY GLY B . n 
A 1 544  GLN 544  527  527  GLN GLN B . n 
A 1 545  LEU 545  528  528  LEU LEU B . n 
A 1 546  GLU 546  529  529  GLU GLU B . n 
A 1 547  LEU 547  530  530  LEU LEU B . n 
A 1 548  MET 548  531  531  MET MET B . n 
A 1 549  PRO 549  532  532  PRO PRO B . n 
A 1 550  ASN 550  533  533  ASN ASN B . n 
A 1 551  ILE 551  534  534  ILE ILE B . n 
A 1 552  GLU 552  535  535  GLU GLU B . n 
A 1 553  ARG 553  536  536  ARG ARG B . n 
A 1 554  PHE 554  537  537  PHE PHE B . n 
A 1 555  PRO 555  538  538  PRO PRO B . n 
A 1 556  ASN 556  539  539  ASN ASN B . n 
A 1 557  GLY 557  540  540  GLY GLY B . n 
A 1 558  LYS 558  541  541  LYS LYS B . n 
A 1 559  LYS 559  542  542  LYS LYS B . n 
A 1 560  TYR 560  543  543  TYR TYR B . n 
A 1 561  GLU 561  544  544  GLU GLU B . n 
A 1 562  LEU 562  545  545  LEU LEU B . n 
A 1 563  ASP 563  546  546  ASP ASP B . n 
A 1 564  LYS 564  547  547  LYS LYS B . n 
A 1 565  TYR 565  548  548  TYR TYR B . n 
A 1 566  THR 566  549  549  THR THR B . n 
A 1 567  MET 567  550  550  MET MET B . n 
A 1 568  PHE 568  551  551  PHE PHE B . n 
A 1 569  HIS 569  552  552  HIS HIS B . n 
A 1 570  TYR 570  553  553  TYR TYR B . n 
A 1 571  LEU 571  554  554  LEU LEU B . n 
A 1 572  ARG 572  555  555  ARG ARG B . n 
A 1 573  ALA 573  556  556  ALA ALA B . n 
A 1 574  GLN 574  557  557  GLN GLN B . n 
A 1 575  GLU 575  558  558  GLU GLU B . n 
A 1 576  PHE 576  559  559  PHE PHE B . n 
A 1 577  GLU 577  560  560  GLU GLU B . n 
A 1 578  HIS 578  561  561  HIS HIS B . n 
A 1 579  GLY 579  562  562  GLY GLY B . n 
A 1 580  LYS 580  563  563  LYS LYS B . n 
A 1 581  SER 581  564  564  SER SER B . n 
A 1 582  ARG 582  565  565  ARG ARG B . n 
A 1 583  ILE 583  566  566  ILE ILE B . n 
A 1 584  ALA 584  567  567  ALA ALA B . n 
A 1 585  LEU 585  568  568  LEU LEU B . n 
A 1 586  THR 586  569  569  THR THR B . n 
A 1 587  ASN 587  570  570  ASN ASN B . n 
A 1 588  SER 588  571  571  SER SER B . n 
A 1 589  VAL 589  572  572  VAL VAL B . n 
A 1 590  ASN 590  573  573  ASN ASN B . n 
A 1 591  GLU 591  574  574  GLU GLU B . n 
A 1 592  ALA 592  575  575  ALA ALA B . n 
A 1 593  LEU 593  576  576  LEU LEU B . n 
A 1 594  LEU 594  577  577  LEU LEU B . n 
A 1 595  ASN 595  578  578  ASN ASN B . n 
A 1 596  PRO 596  579  579  PRO PRO B . n 
A 1 597  SER 597  580  580  SER SER B . n 
A 1 598  ARG 598  581  581  ARG ARG B . n 
A 1 599  VAL 599  582  582  VAL VAL B . n 
A 1 600  TYR 600  583  583  TYR TYR B . n 
A 1 601  THR 601  584  584  THR THR B . n 
A 1 602  PHE 602  585  585  PHE PHE B . n 
A 1 603  PHE 603  586  586  PHE PHE B . n 
A 1 604  SER 604  587  587  SER SER B . n 
A 1 605  SER 605  588  588  SER SER B . n 
A 1 606  ASP 606  589  589  ASP ASP B . n 
A 1 607  TYR 607  590  590  TYR TYR B . n 
A 1 608  VAL 608  591  591  VAL VAL B . n 
A 1 609  LYS 609  592  592  LYS LYS B . n 
A 1 610  LYS 610  593  593  LYS LYS B . n 
A 1 611  VAL 611  594  594  VAL VAL B . n 
A 1 612  ASN 612  595  595  ASN ASN B . n 
A 1 613  LYS 613  596  596  LYS LYS B . n 
A 1 614  ALA 614  597  597  ALA ALA B . n 
A 1 615  THR 615  598  598  THR THR B . n 
A 1 616  GLU 616  599  599  GLU GLU B . n 
A 1 617  ALA 617  600  600  ALA ALA B . n 
A 1 618  ALA 618  601  601  ALA ALA B . n 
A 1 619  MET 619  602  602  MET MET B . n 
A 1 620  PHE 620  603  603  PHE PHE B . n 
A 1 621  LEU 621  604  604  LEU LEU B . n 
A 1 622  GLY 622  605  605  GLY GLY B . n 
A 1 623  TRP 623  606  606  TRP TRP B . n 
A 1 624  VAL 624  607  607  VAL VAL B . n 
A 1 625  GLU 625  608  608  GLU GLU B . n 
A 1 626  GLN 626  609  609  GLN GLN B . n 
A 1 627  LEU 627  610  610  LEU LEU B . n 
A 1 628  VAL 628  611  611  VAL VAL B . n 
A 1 629  TYR 629  612  612  TYR TYR B . n 
A 1 630  ASP 630  613  613  ASP ASP B . n 
A 1 631  PHE 631  614  614  PHE PHE B . n 
A 1 632  THR 632  615  615  THR THR B . n 
A 1 633  ASP 633  616  616  ASP ASP B . n 
A 1 634  GLU 634  617  617  GLU GLU B . n 
A 1 635  THR 635  618  618  THR THR B . n 
A 1 636  SER 636  619  619  SER SER B . n 
A 1 637  GLU 637  620  620  GLU GLU B . n 
A 1 638  VAL 638  621  621  VAL VAL B . n 
A 1 639  SER 639  622  622  SER SER B . n 
A 1 640  THR 640  623  623  THR THR B . n 
A 1 641  THR 641  624  624  THR THR B . n 
A 1 642  ASP 642  625  625  ASP ASP B . n 
A 1 643  LYS 643  626  626  LYS LYS B . n 
A 1 644  ILE 644  627  627  ILE ILE B . n 
A 1 645  ALA 645  628  628  ALA ALA B . n 
A 1 646  ASP 646  629  629  ASP ASP B . n 
A 1 647  ILE 647  630  630  ILE ILE B . n 
A 1 648  THR 648  631  631  THR THR B . n 
A 1 649  ILE 649  632  632  ILE ILE B . n 
A 1 650  ILE 650  633  633  ILE ILE B . n 
A 1 651  ILE 651  634  634  ILE ILE B . n 
A 1 652  PRO 652  635  635  PRO PRO B . n 
A 1 653  TYR 653  636  636  TYR TYR B . n 
A 1 654  ILE 654  637  637  ILE ILE B . n 
A 1 655  GLY 655  638  638  GLY GLY B . n 
A 1 656  PRO 656  639  639  PRO PRO B . n 
A 1 657  ALA 657  640  640  ALA ALA B . n 
A 1 658  LEU 658  641  641  LEU LEU B . n 
A 1 659  ASN 659  642  642  ASN ASN B . n 
A 1 660  ILE 660  643  643  ILE ILE B . n 
A 1 661  GLY 661  644  644  GLY GLY B . n 
A 1 662  ASN 662  645  645  ASN ASN B . n 
A 1 663  MET 663  646  646  MET MET B . n 
A 1 664  LEU 664  647  647  LEU LEU B . n 
A 1 665  TYR 665  648  648  TYR TYR B . n 
A 1 666  LYS 666  649  649  LYS LYS B . n 
A 1 667  ASP 667  650  650  ASP ASP B . n 
A 1 668  ASP 668  651  651  ASP ASP B . n 
A 1 669  PHE 669  652  652  PHE PHE B . n 
A 1 670  VAL 670  653  653  VAL VAL B . n 
A 1 671  GLY 671  654  654  GLY GLY B . n 
A 1 672  ALA 672  655  655  ALA ALA B . n 
A 1 673  LEU 673  656  656  LEU LEU B . n 
A 1 674  ILE 674  657  657  ILE ILE B . n 
A 1 675  PHE 675  658  658  PHE PHE B . n 
A 1 676  SER 676  659  659  SER SER B . n 
A 1 677  GLY 677  660  660  GLY GLY B . n 
A 1 678  ALA 678  661  661  ALA ALA B . n 
A 1 679  VAL 679  662  662  VAL VAL B . n 
A 1 680  ILE 680  663  663  ILE ILE B . n 
A 1 681  LEU 681  664  664  LEU LEU B . n 
A 1 682  LEU 682  665  665  LEU LEU B . n 
A 1 683  GLU 683  666  666  GLU GLU B . n 
A 1 684  PHE 684  667  667  PHE PHE B . n 
A 1 685  ILE 685  668  668  ILE ILE B . n 
A 1 686  PRO 686  669  669  PRO PRO B . n 
A 1 687  GLU 687  670  670  GLU GLU B . n 
A 1 688  ILE 688  671  671  ILE ILE B . n 
A 1 689  ALA 689  672  672  ALA ALA B . n 
A 1 690  ILE 690  673  673  ILE ILE B . n 
A 1 691  PRO 691  674  674  PRO PRO B . n 
A 1 692  VAL 692  675  675  VAL VAL B . n 
A 1 693  LEU 693  676  676  LEU LEU B . n 
A 1 694  GLY 694  677  677  GLY GLY B . n 
A 1 695  THR 695  678  678  THR THR B . n 
A 1 696  PHE 696  679  679  PHE PHE B . n 
A 1 697  ALA 697  680  680  ALA ALA B . n 
A 1 698  LEU 698  681  681  LEU LEU B . n 
A 1 699  VAL 699  682  682  VAL VAL B . n 
A 1 700  SER 700  683  683  SER SER B . n 
A 1 701  TYR 701  684  684  TYR TYR B . n 
A 1 702  ILE 702  685  685  ILE ILE B . n 
A 1 703  ALA 703  686  686  ALA ALA B . n 
A 1 704  ASN 704  687  687  ASN ASN B . n 
A 1 705  LYS 705  688  688  LYS LYS B . n 
A 1 706  VAL 706  689  689  VAL VAL B . n 
A 1 707  LEU 707  690  690  LEU LEU B . n 
A 1 708  THR 708  691  691  THR THR B . n 
A 1 709  VAL 709  692  692  VAL VAL B . n 
A 1 710  GLN 710  693  693  GLN GLN B . n 
A 1 711  THR 711  694  694  THR THR B . n 
A 1 712  ILE 712  695  695  ILE ILE B . n 
A 1 713  ASP 713  696  696  ASP ASP B . n 
A 1 714  ASN 714  697  697  ASN ASN B . n 
A 1 715  ALA 715  698  698  ALA ALA B . n 
A 1 716  LEU 716  699  699  LEU LEU B . n 
A 1 717  SER 717  700  700  SER SER B . n 
A 1 718  LYS 718  701  701  LYS LYS B . n 
A 1 719  ARG 719  702  702  ARG ARG B . n 
A 1 720  ASN 720  703  703  ASN ASN B . n 
A 1 721  GLU 721  704  704  GLU GLU B . n 
A 1 722  LYS 722  705  705  LYS LYS B . n 
A 1 723  TRP 723  706  706  TRP TRP B . n 
A 1 724  ASP 724  707  707  ASP ASP B . n 
A 1 725  GLU 725  708  708  GLU GLU B . n 
A 1 726  VAL 726  709  709  VAL VAL B . n 
A 1 727  TYR 727  710  710  TYR TYR B . n 
A 1 728  LYS 728  711  711  LYS LYS B . n 
A 1 729  TYR 729  712  712  TYR TYR B . n 
A 1 730  ILE 730  713  713  ILE ILE B . n 
A 1 731  VAL 731  714  714  VAL VAL B . n 
A 1 732  THR 732  715  715  THR THR B . n 
A 1 733  ASN 733  716  716  ASN ASN B . n 
A 1 734  TRP 734  717  717  TRP TRP B . n 
A 1 735  LEU 735  718  718  LEU LEU B . n 
A 1 736  ALA 736  719  719  ALA ALA B . n 
A 1 737  LYS 737  720  720  LYS LYS B . n 
A 1 738  VAL 738  721  721  VAL VAL B . n 
A 1 739  ASN 739  722  722  ASN ASN B . n 
A 1 740  THR 740  723  723  THR THR B . n 
A 1 741  GLN 741  724  724  GLN GLN B . n 
A 1 742  ILE 742  725  725  ILE ILE B . n 
A 1 743  ASP 743  726  726  ASP ASP B . n 
A 1 744  LEU 744  727  727  LEU LEU B . n 
A 1 745  ILE 745  728  728  ILE ILE B . n 
A 1 746  ARG 746  729  729  ARG ARG B . n 
A 1 747  LYS 747  730  730  LYS LYS B . n 
A 1 748  LYS 748  731  731  LYS LYS B . n 
A 1 749  MET 749  732  732  MET MET B . n 
A 1 750  LYS 750  733  733  LYS LYS B . n 
A 1 751  GLU 751  734  734  GLU GLU B . n 
A 1 752  ALA 752  735  735  ALA ALA B . n 
A 1 753  LEU 753  736  736  LEU LEU B . n 
A 1 754  GLU 754  737  737  GLU GLU B . n 
A 1 755  ASN 755  738  738  ASN ASN B . n 
A 1 756  GLN 756  739  739  GLN GLN B . n 
A 1 757  ALA 757  740  740  ALA ALA B . n 
A 1 758  GLU 758  741  741  GLU GLU B . n 
A 1 759  ALA 759  742  742  ALA ALA B . n 
A 1 760  THR 760  743  743  THR THR B . n 
A 1 761  LYS 761  744  744  LYS LYS B . n 
A 1 762  ALA 762  745  745  ALA ALA B . n 
A 1 763  ILE 763  746  746  ILE ILE B . n 
A 1 764  ILE 764  747  747  ILE ILE B . n 
A 1 765  ASN 765  748  748  ASN ASN B . n 
A 1 766  TYR 766  749  749  TYR TYR B . n 
A 1 767  GLN 767  750  750  GLN GLN B . n 
A 1 768  TYR 768  751  751  TYR TYR B . n 
A 1 769  ASN 769  752  752  ASN ASN B . n 
A 1 770  GLN 770  753  753  GLN GLN B . n 
A 1 771  TYR 771  754  754  TYR TYR B . n 
A 1 772  THR 772  755  755  THR THR B . n 
A 1 773  GLU 773  756  756  GLU GLU B . n 
A 1 774  GLU 774  757  757  GLU GLU B . n 
A 1 775  GLU 775  758  758  GLU GLU B . n 
A 1 776  LYS 776  759  759  LYS LYS B . n 
A 1 777  ASN 777  760  760  ASN ASN B . n 
A 1 778  ASN 778  761  761  ASN ASN B . n 
A 1 779  ILE 779  762  762  ILE ILE B . n 
A 1 780  ASN 780  763  763  ASN ASN B . n 
A 1 781  PHE 781  764  764  PHE PHE B . n 
A 1 782  ASN 782  765  765  ASN ASN B . n 
A 1 783  ILE 783  766  766  ILE ILE B . n 
A 1 784  ASP 784  767  767  ASP ASP B . n 
A 1 785  ASP 785  768  768  ASP ASP B . n 
A 1 786  LEU 786  769  769  LEU LEU B . n 
A 1 787  SER 787  770  770  SER SER B . n 
A 1 788  SER 788  771  771  SER SER B . n 
A 1 789  LYS 789  772  772  LYS LYS B . n 
A 1 790  LEU 790  773  773  LEU LEU B . n 
A 1 791  ASN 791  774  774  ASN ASN B . n 
A 1 792  GLU 792  775  775  GLU GLU B . n 
A 1 793  SER 793  776  776  SER SER B . n 
A 1 794  ILE 794  777  777  ILE ILE B . n 
A 1 795  ASN 795  778  778  ASN ASN B . n 
A 1 796  LYS 796  779  779  LYS LYS B . n 
A 1 797  ALA 797  780  780  ALA ALA B . n 
A 1 798  MET 798  781  781  MET MET B . n 
A 1 799  ILE 799  782  782  ILE ILE B . n 
A 1 800  ASN 800  783  783  ASN ASN B . n 
A 1 801  ILE 801  784  784  ILE ILE B . n 
A 1 802  ASN 802  785  785  ASN ASN B . n 
A 1 803  LYS 803  786  786  LYS LYS B . n 
A 1 804  PHE 804  787  787  PHE PHE B . n 
A 1 805  LEU 805  788  788  LEU LEU B . n 
A 1 806  ASN 806  789  789  ASN ASN B . n 
A 1 807  GLN 807  790  790  GLN GLN B . n 
A 1 808  CYS 808  791  791  CYS CYS B . n 
A 1 809  SER 809  792  792  SER SER B . n 
A 1 810  VAL 810  793  793  VAL VAL B . n 
A 1 811  SER 811  794  794  SER SER B . n 
A 1 812  TYR 812  795  795  TYR TYR B . n 
A 1 813  LEU 813  796  796  LEU LEU B . n 
A 1 814  MET 814  797  797  MET MET B . n 
A 1 815  ASN 815  798  798  ASN ASN B . n 
A 1 816  SER 816  799  799  SER SER B . n 
A 1 817  MET 817  800  800  MET MET B . n 
A 1 818  ILE 818  801  801  ILE ILE B . n 
A 1 819  PRO 819  802  802  PRO PRO B . n 
A 1 820  TYR 820  803  803  TYR TYR B . n 
A 1 821  GLY 821  804  804  GLY GLY B . n 
A 1 822  VAL 822  805  805  VAL VAL B . n 
A 1 823  LYS 823  806  806  LYS LYS B . n 
A 1 824  ARG 824  807  807  ARG ARG B . n 
A 1 825  LEU 825  808  808  LEU LEU B . n 
A 1 826  GLU 826  809  809  GLU GLU B . n 
A 1 827  ASP 827  810  810  ASP ASP B . n 
A 1 828  PHE 828  811  811  PHE PHE B . n 
A 1 829  ASP 829  812  812  ASP ASP B . n 
A 1 830  ALA 830  813  813  ALA ALA B . n 
A 1 831  SER 831  814  814  SER SER B . n 
A 1 832  LEU 832  815  815  LEU LEU B . n 
A 1 833  LYS 833  816  816  LYS LYS B . n 
A 1 834  ASP 834  817  817  ASP ASP B . n 
A 1 835  ALA 835  818  818  ALA ALA B . n 
A 1 836  LEU 836  819  819  LEU LEU B . n 
A 1 837  LEU 837  820  820  LEU LEU B . n 
A 1 838  LYS 838  821  821  LYS LYS B . n 
A 1 839  TYR 839  822  822  TYR TYR B . n 
A 1 840  ILE 840  823  823  ILE ILE B . n 
A 1 841  TYR 841  824  824  TYR TYR B . n 
A 1 842  ASP 842  825  ?    ?   ?   B . n 
A 1 843  ASN 843  826  ?    ?   ?   B . n 
A 1 844  ARG 844  827  ?    ?   ?   B . n 
A 1 845  GLY 845  828  ?    ?   ?   B . n 
A 1 846  THR 846  829  ?    ?   ?   B . n 
A 1 847  LEU 847  830  ?    ?   ?   B . n 
A 1 848  ILE 848  831  831  ILE ILE B . n 
A 1 849  GLY 849  832  832  GLY GLY B . n 
A 1 850  GLN 850  833  833  GLN GLN B . n 
A 1 851  VAL 851  834  834  VAL VAL B . n 
A 1 852  ASP 852  835  835  ASP ASP B . n 
A 1 853  ARG 853  836  836  ARG ARG B . n 
A 1 854  LEU 854  837  837  LEU LEU B . n 
A 1 855  LYS 855  838  838  LYS LYS B . n 
A 1 856  ASP 856  839  839  ASP ASP B . n 
A 1 857  LYS 857  840  840  LYS LYS B . n 
A 1 858  VAL 858  841  841  VAL VAL B . n 
A 1 859  ASN 859  842  842  ASN ASN B . n 
A 1 860  ASN 860  843  843  ASN ASN B . n 
A 1 861  THR 861  844  844  THR THR B . n 
A 1 862  LEU 862  845  845  LEU LEU B . n 
A 1 863  SER 863  846  846  SER SER B . n 
A 1 864  THR 864  847  847  THR THR B . n 
A 1 865  ASP 865  848  848  ASP ASP B . n 
A 1 866  ILE 866  849  849  ILE ILE B . n 
A 1 867  PRO 867  850  850  PRO PRO B . n 
A 1 868  PHE 868  851  851  PHE PHE B . n 
A 1 869  GLN 869  852  852  GLN GLN B . n 
A 1 870  LEU 870  853  853  LEU LEU B . n 
A 1 871  SER 871  854  854  SER SER B . n 
A 1 872  LYS 872  855  855  LYS LYS B . n 
A 1 873  TYR 873  856  856  TYR TYR B . n 
A 1 874  VAL 874  857  857  VAL VAL B . n 
A 1 875  ASP 875  858  858  ASP ASP B . n 
A 1 876  ASN 876  859  859  ASN ASN B . n 
A 1 877  GLN 877  860  860  GLN GLN B . n 
A 1 878  ARG 878  861  861  ARG ARG B . n 
A 1 879  LEU 879  862  862  LEU LEU B . n 
A 1 880  LEU 880  863  863  LEU LEU B . n 
A 1 881  SER 881  864  864  SER SER B . n 
A 1 882  THR 882  865  865  THR THR B . n 
A 1 883  PHE 883  866  866  PHE PHE B . n 
A 1 884  THR 884  867  867  THR THR B . n 
A 1 885  GLU 885  868  868  GLU GLU B . n 
A 1 886  TYR 886  869  869  TYR TYR B . n 
A 1 887  ILE 887  870  870  ILE ILE B . n 
A 1 888  LYS 888  871  871  LYS LYS B . n 
A 1 889  ASN 889  872  872  ASN ASN B . n 
A 1 890  ILE 890  873  873  ILE ILE B . n 
A 1 891  ILE 891  874  874  ILE ILE B . n 
A 1 892  ASN 892  875  875  ASN ASN B . n 
A 1 893  THR 893  876  876  THR THR B . n 
A 1 894  SER 894  877  877  SER SER B . n 
A 1 895  ILE 895  878  878  ILE ILE B . n 
A 1 896  LEU 896  879  879  LEU LEU B . n 
A 1 897  ASN 897  880  880  ASN ASN B . n 
A 1 898  LEU 898  881  881  LEU LEU B . n 
A 1 899  ARG 899  882  882  ARG ARG B . n 
A 1 900  TYR 900  883  883  TYR TYR B . n 
A 1 901  GLU 901  884  884  GLU GLU B . n 
A 1 902  SER 902  885  885  SER SER B . n 
A 1 903  ASN 903  886  886  ASN ASN B . n 
A 1 904  HIS 904  887  887  HIS HIS B . n 
A 1 905  LEU 905  888  888  LEU LEU B . n 
A 1 906  ILE 906  889  889  ILE ILE B . n 
A 1 907  ASP 907  890  890  ASP ASP B . n 
A 1 908  LEU 908  891  891  LEU LEU B . n 
A 1 909  SER 909  892  892  SER SER B . n 
A 1 910  ARG 910  893  893  ARG ARG B . n 
A 1 911  TYR 911  894  894  TYR TYR B . n 
A 1 912  ALA 912  895  895  ALA ALA B . n 
A 1 913  SER 913  896  896  SER SER B . n 
A 1 914  LYS 914  897  897  LYS LYS B . n 
A 1 915  ILE 915  898  898  ILE ILE B . n 
A 1 916  ASN 916  899  899  ASN ASN B . n 
A 1 917  ILE 917  900  900  ILE ILE B . n 
A 1 918  GLY 918  901  901  GLY GLY B . n 
A 1 919  SER 919  902  902  SER SER B . n 
A 1 920  LYS 920  903  903  LYS LYS B . n 
A 1 921  VAL 921  904  904  VAL VAL B . n 
A 1 922  ASN 922  905  905  ASN ASN B . n 
A 1 923  PHE 923  906  906  PHE PHE B . n 
A 1 924  ASP 924  907  907  ASP ASP B . n 
A 1 925  PRO 925  908  908  PRO PRO B . n 
A 1 926  ILE 926  909  909  ILE ILE B . n 
A 1 927  ASP 927  910  910  ASP ASP B . n 
A 1 928  LYS 928  911  911  LYS LYS B . n 
A 1 929  ASN 929  912  912  ASN ASN B . n 
A 1 930  GLN 930  913  913  GLN GLN B . n 
A 1 931  ILE 931  914  914  ILE ILE B . n 
A 1 932  GLN 932  915  915  GLN GLN B . n 
A 1 933  LEU 933  916  916  LEU LEU B . n 
A 1 934  PHE 934  917  917  PHE PHE B . n 
A 1 935  ASN 935  918  918  ASN ASN B . n 
A 1 936  LEU 936  919  919  LEU LEU B . n 
A 1 937  GLU 937  920  920  GLU GLU B . n 
A 1 938  SER 938  921  921  SER SER B . n 
A 1 939  SER 939  922  922  SER SER B . n 
A 1 940  LYS 940  923  923  LYS LYS B . n 
A 1 941  ILE 941  924  924  ILE ILE B . n 
A 1 942  GLU 942  925  925  GLU GLU B . n 
A 1 943  VAL 943  926  926  VAL VAL B . n 
A 1 944  ILE 944  927  927  ILE ILE B . n 
A 1 945  LEU 945  928  928  LEU LEU B . n 
A 1 946  LYS 946  929  929  LYS LYS B . n 
A 1 947  ASN 947  930  930  ASN ASN B . n 
A 1 948  ALA 948  931  931  ALA ALA B . n 
A 1 949  ILE 949  932  932  ILE ILE B . n 
A 1 950  VAL 950  933  933  VAL VAL B . n 
A 1 951  TYR 951  934  934  TYR TYR B . n 
A 1 952  ASN 952  935  935  ASN ASN B . n 
A 1 953  SER 953  936  936  SER SER B . n 
A 1 954  MET 954  937  937  MET MET B . n 
A 1 955  TYR 955  938  938  TYR TYR B . n 
A 1 956  GLU 956  939  939  GLU GLU B . n 
A 1 957  ASN 957  940  940  ASN ASN B . n 
A 1 958  PHE 958  941  941  PHE PHE B . n 
A 1 959  SER 959  942  942  SER SER B . n 
A 1 960  THR 960  943  943  THR THR B . n 
A 1 961  SER 961  944  944  SER SER B . n 
A 1 962  PHE 962  945  945  PHE PHE B . n 
A 1 963  TRP 963  946  946  TRP TRP B . n 
A 1 964  ILE 964  947  947  ILE ILE B . n 
A 1 965  ARG 965  948  948  ARG ARG B . n 
A 1 966  ILE 966  949  949  ILE ILE B . n 
A 1 967  PRO 967  950  950  PRO PRO B . n 
A 1 968  LYS 968  951  951  LYS LYS B . n 
A 1 969  TYR 969  952  952  TYR TYR B . n 
A 1 970  PHE 970  953  953  PHE PHE B . n 
A 1 971  ASN 971  954  954  ASN ASN B . n 
A 1 972  SER 972  955  955  SER SER B . n 
A 1 973  ILE 973  956  956  ILE ILE B . n 
A 1 974  SER 974  957  957  SER SER B . n 
A 1 975  LEU 975  958  958  LEU LEU B . n 
A 1 976  ASN 976  959  959  ASN ASN B . n 
A 1 977  ASN 977  960  960  ASN ASN B . n 
A 1 978  GLU 978  961  961  GLU GLU B . n 
A 1 979  TYR 979  962  962  TYR TYR B . n 
A 1 980  THR 980  963  963  THR THR B . n 
A 1 981  ILE 981  964  964  ILE ILE B . n 
A 1 982  ILE 982  965  965  ILE ILE B . n 
A 1 983  ASN 983  966  966  ASN ASN B . n 
A 1 984  CYS 984  967  967  CYS CYS B . n 
A 1 985  MET 985  968  968  MET MET B . n 
A 1 986  GLU 986  969  969  GLU GLU B . n 
A 1 987  ASN 987  970  970  ASN ASN B . n 
A 1 988  ASN 988  971  971  ASN ASN B . n 
A 1 989  SER 989  972  972  SER SER B . n 
A 1 990  GLY 990  973  973  GLY GLY B . n 
A 1 991  TRP 991  974  974  TRP TRP B . n 
A 1 992  LYS 992  975  975  LYS LYS B . n 
A 1 993  VAL 993  976  976  VAL VAL B . n 
A 1 994  SER 994  977  977  SER SER B . n 
A 1 995  LEU 995  978  978  LEU LEU B . n 
A 1 996  ASN 996  979  979  ASN ASN B . n 
A 1 997  TYR 997  980  980  TYR TYR B . n 
A 1 998  GLY 998  981  981  GLY GLY B . n 
A 1 999  GLU 999  982  982  GLU GLU B . n 
A 1 1000 ILE 1000 983  983  ILE ILE B . n 
A 1 1001 ILE 1001 984  984  ILE ILE B . n 
A 1 1002 TRP 1002 985  985  TRP TRP B . n 
A 1 1003 THR 1003 986  986  THR THR B . n 
A 1 1004 LEU 1004 987  987  LEU LEU B . n 
A 1 1005 GLN 1005 988  988  GLN GLN B . n 
A 1 1006 ASP 1006 989  989  ASP ASP B . n 
A 1 1007 THR 1007 990  990  THR THR B . n 
A 1 1008 GLN 1008 991  991  GLN GLN B . n 
A 1 1009 GLU 1009 992  992  GLU GLU B . n 
A 1 1010 ILE 1010 993  993  ILE ILE B . n 
A 1 1011 LYS 1011 994  994  LYS LYS B . n 
A 1 1012 GLN 1012 995  995  GLN GLN B . n 
A 1 1013 ARG 1013 996  996  ARG ARG B . n 
A 1 1014 VAL 1014 997  997  VAL VAL B . n 
A 1 1015 VAL 1015 998  998  VAL VAL B . n 
A 1 1016 PHE 1016 999  999  PHE PHE B . n 
A 1 1017 LYS 1017 1000 1000 LYS LYS B . n 
A 1 1018 TYR 1018 1001 1001 TYR TYR B . n 
A 1 1019 SER 1019 1002 1002 SER SER B . n 
A 1 1020 GLN 1020 1003 1003 GLN GLN B . n 
A 1 1021 MET 1021 1004 1004 MET MET B . n 
A 1 1022 ILE 1022 1005 1005 ILE ILE B . n 
A 1 1023 ASN 1023 1006 1006 ASN ASN B . n 
A 1 1024 ILE 1024 1007 1007 ILE ILE B . n 
A 1 1025 SER 1025 1008 1008 SER SER B . n 
A 1 1026 ASP 1026 1009 1009 ASP ASP B . n 
A 1 1027 TYR 1027 1010 1010 TYR TYR B . n 
A 1 1028 ILE 1028 1011 1011 ILE ILE B . n 
A 1 1029 ASN 1029 1012 1012 ASN ASN B . n 
A 1 1030 ARG 1030 1013 1013 ARG ARG B . n 
A 1 1031 TRP 1031 1014 1014 TRP TRP B . n 
A 1 1032 ILE 1032 1015 1015 ILE ILE B . n 
A 1 1033 PHE 1033 1016 1016 PHE PHE B . n 
A 1 1034 VAL 1034 1017 1017 VAL VAL B . n 
A 1 1035 THR 1035 1018 1018 THR THR B . n 
A 1 1036 ILE 1036 1019 1019 ILE ILE B . n 
A 1 1037 THR 1037 1020 1020 THR THR B . n 
A 1 1038 ASN 1038 1021 1021 ASN ASN B . n 
A 1 1039 ASN 1039 1022 1022 ASN ASN B . n 
A 1 1040 ARG 1040 1023 1023 ARG ARG B . n 
A 1 1041 LEU 1041 1024 1024 LEU LEU B . n 
A 1 1042 ASN 1042 1025 1025 ASN ASN B . n 
A 1 1043 ASN 1043 1026 1026 ASN ASN B . n 
A 1 1044 SER 1044 1027 1027 SER SER B . n 
A 1 1045 LYS 1045 1028 1028 LYS LYS B . n 
A 1 1046 ILE 1046 1029 1029 ILE ILE B . n 
A 1 1047 TYR 1047 1030 1030 TYR TYR B . n 
A 1 1048 ILE 1048 1031 1031 ILE ILE B . n 
A 1 1049 ASN 1049 1032 1032 ASN ASN B . n 
A 1 1050 GLY 1050 1033 1033 GLY GLY B . n 
A 1 1051 ARG 1051 1034 1034 ARG ARG B . n 
A 1 1052 LEU 1052 1035 1035 LEU LEU B . n 
A 1 1053 ILE 1053 1036 1036 ILE ILE B . n 
A 1 1054 ASP 1054 1037 1037 ASP ASP B . n 
A 1 1055 GLN 1055 1038 1038 GLN GLN B . n 
A 1 1056 LYS 1056 1039 1039 LYS LYS B . n 
A 1 1057 PRO 1057 1040 1040 PRO PRO B . n 
A 1 1058 ILE 1058 1041 1041 ILE ILE B . n 
A 1 1059 SER 1059 1042 1042 SER SER B . n 
A 1 1060 ASN 1060 1043 1043 ASN ASN B . n 
A 1 1061 LEU 1061 1044 1044 LEU LEU B . n 
A 1 1062 GLY 1062 1045 1045 GLY GLY B . n 
A 1 1063 ASN 1063 1046 1046 ASN ASN B . n 
A 1 1064 ILE 1064 1047 1047 ILE ILE B . n 
A 1 1065 HIS 1065 1048 1048 HIS HIS B . n 
A 1 1066 ALA 1066 1049 1049 ALA ALA B . n 
A 1 1067 SER 1067 1050 1050 SER SER B . n 
A 1 1068 ASN 1068 1051 1051 ASN ASN B . n 
A 1 1069 ASN 1069 1052 1052 ASN ASN B . n 
A 1 1070 ILE 1070 1053 1053 ILE ILE B . n 
A 1 1071 MET 1071 1054 1054 MET MET B . n 
A 1 1072 PHE 1072 1055 1055 PHE PHE B . n 
A 1 1073 LYS 1073 1056 1056 LYS LYS B . n 
A 1 1074 LEU 1074 1057 1057 LEU LEU B . n 
A 1 1075 ASP 1075 1058 1058 ASP ASP B . n 
A 1 1076 GLY 1076 1059 1059 GLY GLY B . n 
A 1 1077 CYS 1077 1060 1060 CYS CYS B . n 
A 1 1078 ARG 1078 1061 1061 ARG ARG B . n 
A 1 1079 ASP 1079 1062 1062 ASP ASP B . n 
A 1 1080 THR 1080 1063 1063 THR THR B . n 
A 1 1081 HIS 1081 1064 1064 HIS HIS B . n 
A 1 1082 ARG 1082 1065 1065 ARG ARG B . n 
A 1 1083 TYR 1083 1066 1066 TYR TYR B . n 
A 1 1084 ILE 1084 1067 1067 ILE ILE B . n 
A 1 1085 TRP 1085 1068 1068 TRP TRP B . n 
A 1 1086 ILE 1086 1069 1069 ILE ILE B . n 
A 1 1087 LYS 1087 1070 1070 LYS LYS B . n 
A 1 1088 TYR 1088 1071 1071 TYR TYR B . n 
A 1 1089 PHE 1089 1072 1072 PHE PHE B . n 
A 1 1090 ASN 1090 1073 1073 ASN ASN B . n 
A 1 1091 LEU 1091 1074 1074 LEU LEU B . n 
A 1 1092 PHE 1092 1075 1075 PHE PHE B . n 
A 1 1093 ASP 1093 1076 1076 ASP ASP B . n 
A 1 1094 LYS 1094 1077 1077 LYS LYS B . n 
A 1 1095 GLU 1095 1078 1078 GLU GLU B . n 
A 1 1096 LEU 1096 1079 1079 LEU LEU B . n 
A 1 1097 ASN 1097 1080 1080 ASN ASN B . n 
A 1 1098 GLU 1098 1081 1081 GLU GLU B . n 
A 1 1099 LYS 1099 1082 1082 LYS LYS B . n 
A 1 1100 GLU 1100 1083 1083 GLU GLU B . n 
A 1 1101 ILE 1101 1084 1084 ILE ILE B . n 
A 1 1102 LYS 1102 1085 1085 LYS LYS B . n 
A 1 1103 ASP 1103 1086 1086 ASP ASP B . n 
A 1 1104 LEU 1104 1087 1087 LEU LEU B . n 
A 1 1105 TYR 1105 1088 1088 TYR TYR B . n 
A 1 1106 ASP 1106 1089 1089 ASP ASP B . n 
A 1 1107 ASN 1107 1090 1090 ASN ASN B . n 
A 1 1108 GLN 1108 1091 1091 GLN GLN B . n 
A 1 1109 SER 1109 1092 1092 SER SER B . n 
A 1 1110 ASN 1110 1093 1093 ASN ASN B . n 
A 1 1111 SER 1111 1094 1094 SER SER B . n 
A 1 1112 GLY 1112 1095 1095 GLY GLY B . n 
A 1 1113 ILE 1113 1096 1096 ILE ILE B . n 
A 1 1114 LEU 1114 1097 1097 LEU LEU B . n 
A 1 1115 LYS 1115 1098 1098 LYS LYS B . n 
A 1 1116 ASP 1116 1099 1099 ASP ASP B . n 
A 1 1117 PHE 1117 1100 1100 PHE PHE B . n 
A 1 1118 TRP 1118 1101 1101 TRP TRP B . n 
A 1 1119 GLY 1119 1102 1102 GLY GLY B . n 
A 1 1120 ASP 1120 1103 1103 ASP ASP B . n 
A 1 1121 TYR 1121 1104 1104 TYR TYR B . n 
A 1 1122 LEU 1122 1105 1105 LEU LEU B . n 
A 1 1123 GLN 1123 1106 1106 GLN GLN B . n 
A 1 1124 TYR 1124 1107 1107 TYR TYR B . n 
A 1 1125 ASP 1125 1108 1108 ASP ASP B . n 
A 1 1126 LYS 1126 1109 1109 LYS LYS B . n 
A 1 1127 PRO 1127 1110 1110 PRO PRO B . n 
A 1 1128 TYR 1128 1111 1111 TYR TYR B . n 
A 1 1129 TYR 1129 1112 1112 TYR TYR B . n 
A 1 1130 MET 1130 1113 1113 MET MET B . n 
A 1 1131 LEU 1131 1114 1114 LEU LEU B . n 
A 1 1132 ASN 1132 1115 1115 ASN ASN B . n 
A 1 1133 LEU 1133 1116 1116 LEU LEU B . n 
A 1 1134 TYR 1134 1117 1117 TYR TYR B . n 
A 1 1135 ASP 1135 1118 1118 ASP ASP B . n 
A 1 1136 PRO 1136 1119 1119 PRO PRO B . n 
A 1 1137 ASN 1137 1120 1120 ASN ASN B . n 
A 1 1138 LYS 1138 1121 1121 LYS LYS B . n 
A 1 1139 TYR 1139 1122 1122 TYR TYR B . n 
A 1 1140 VAL 1140 1123 1123 VAL VAL B . n 
A 1 1141 ASP 1141 1124 1124 ASP ASP B . n 
A 1 1142 VAL 1142 1125 1125 VAL VAL B . n 
A 1 1143 ASN 1143 1126 1126 ASN ASN B . n 
A 1 1144 ASN 1144 1127 1127 ASN ASN B . n 
A 1 1145 VAL 1145 1128 1128 VAL VAL B . n 
A 1 1146 GLY 1146 1129 1129 GLY GLY B . n 
A 1 1147 ILE 1147 1130 1130 ILE ILE B . n 
A 1 1148 ARG 1148 1131 1131 ARG ARG B . n 
A 1 1149 GLY 1149 1132 1132 GLY GLY B . n 
A 1 1150 TYR 1150 1133 1133 TYR TYR B . n 
A 1 1151 MET 1151 1134 1134 MET MET B . n 
A 1 1152 TYR 1152 1135 1135 TYR TYR B . n 
A 1 1153 LEU 1153 1136 1136 LEU LEU B . n 
A 1 1154 LYS 1154 1137 1137 LYS LYS B . n 
A 1 1155 GLY 1155 1138 1138 GLY GLY B . n 
A 1 1156 PRO 1156 1139 1139 PRO PRO B . n 
A 1 1157 ARG 1157 1140 1140 ARG ARG B . n 
A 1 1158 GLY 1158 1141 1141 GLY GLY B . n 
A 1 1159 SER 1159 1142 1142 SER SER B . n 
A 1 1160 VAL 1160 1143 1143 VAL VAL B . n 
A 1 1161 MET 1161 1144 1144 MET MET B . n 
A 1 1162 THR 1162 1145 1145 THR THR B . n 
A 1 1163 THR 1163 1146 1146 THR THR B . n 
A 1 1164 ASN 1164 1147 1147 ASN ASN B . n 
A 1 1165 ILE 1165 1148 1148 ILE ILE B . n 
A 1 1166 TYR 1166 1149 1149 TYR TYR B . n 
A 1 1167 LEU 1167 1150 1150 LEU LEU B . n 
A 1 1168 ASN 1168 1151 1151 ASN ASN B . n 
A 1 1169 SER 1169 1152 1152 SER SER B . n 
A 1 1170 SER 1170 1153 1153 SER SER B . n 
A 1 1171 LEU 1171 1154 1154 LEU LEU B . n 
A 1 1172 TYR 1172 1155 1155 TYR TYR B . n 
A 1 1173 ARG 1173 1156 1156 ARG ARG B . n 
A 1 1174 GLY 1174 1157 1157 GLY GLY B . n 
A 1 1175 ALA 1175 1158 1158 ALA ALA B . n 
A 1 1176 LYS 1176 1159 1159 LYS LYS B . n 
A 1 1177 PHE 1177 1160 1160 PHE PHE B . n 
A 1 1178 ILE 1178 1161 1161 ILE ILE B . n 
A 1 1179 ILE 1179 1162 1162 ILE ILE B . n 
A 1 1180 LYS 1180 1163 1163 LYS LYS B . n 
A 1 1181 LYS 1181 1164 1164 LYS LYS B . n 
A 1 1182 TYR 1182 1165 1165 TYR TYR B . n 
A 1 1183 ALA 1183 1166 1166 ALA ALA B . n 
A 1 1184 SER 1184 1167 1167 SER SER B . n 
A 1 1185 GLY 1185 1168 1168 GLY GLY B . n 
A 1 1186 ASN 1186 1169 1169 ASN ASN B . n 
A 1 1187 LYS 1187 1170 1170 LYS LYS B . n 
A 1 1188 ASP 1188 1171 1171 ASP ASP B . n 
A 1 1189 ASN 1189 1172 1172 ASN ASN B . n 
A 1 1190 ILE 1190 1173 1173 ILE ILE B . n 
A 1 1191 VAL 1191 1174 1174 VAL VAL B . n 
A 1 1192 ARG 1192 1175 1175 ARG ARG B . n 
A 1 1193 ASN 1193 1176 1176 ASN ASN B . n 
A 1 1194 ASN 1194 1177 1177 ASN ASN B . n 
A 1 1195 ASP 1195 1178 1178 ASP ASP B . n 
A 1 1196 ARG 1196 1179 1179 ARG ARG B . n 
A 1 1197 VAL 1197 1180 1180 VAL VAL B . n 
A 1 1198 TYR 1198 1181 1181 TYR TYR B . n 
A 1 1199 ILE 1199 1182 1182 ILE ILE B . n 
A 1 1200 ASN 1200 1183 1183 ASN ASN B . n 
A 1 1201 VAL 1201 1184 1184 VAL VAL B . n 
A 1 1202 VAL 1202 1185 1185 VAL VAL B . n 
A 1 1203 VAL 1203 1186 1186 VAL VAL B . n 
A 1 1204 LYS 1204 1187 1187 LYS LYS B . n 
A 1 1205 ASN 1205 1188 1188 ASN ASN B . n 
A 1 1206 LYS 1206 1189 1189 LYS LYS B . n 
A 1 1207 GLU 1207 1190 1190 GLU GLU B . n 
A 1 1208 TYR 1208 1191 1191 TYR TYR B . n 
A 1 1209 ARG 1209 1192 1192 ARG ARG B . n 
A 1 1210 LEU 1210 1193 1193 LEU LEU B . n 
A 1 1211 ALA 1211 1194 1194 ALA ALA B . n 
A 1 1212 THR 1212 1195 1195 THR THR B . n 
A 1 1213 ASN 1213 1196 1196 ASN ASN B . n 
A 1 1214 ALA 1214 1197 1197 ALA ALA B . n 
A 1 1215 SER 1215 1198 1198 SER SER B . n 
A 1 1216 GLN 1216 1199 1199 GLN GLN B . n 
A 1 1217 ALA 1217 1200 1200 ALA ALA B . n 
A 1 1218 GLY 1218 1201 1201 GLY GLY B . n 
A 1 1219 VAL 1219 1202 1202 VAL VAL B . n 
A 1 1220 GLU 1220 1203 1203 GLU GLU B . n 
A 1 1221 LYS 1221 1204 1204 LYS LYS B . n 
A 1 1222 ILE 1222 1205 1205 ILE ILE B . n 
A 1 1223 LEU 1223 1206 1206 LEU LEU B . n 
A 1 1224 SER 1224 1207 1207 SER SER B . n 
A 1 1225 ALA 1225 1208 1208 ALA ALA B . n 
A 1 1226 LEU 1226 1209 1209 LEU LEU B . n 
A 1 1227 GLU 1227 1210 1210 GLU GLU B . n 
A 1 1228 ILE 1228 1211 1211 ILE ILE B . n 
A 1 1229 PRO 1229 1212 1212 PRO PRO B . n 
A 1 1230 ASP 1230 1213 1213 ASP ASP B . n 
A 1 1231 VAL 1231 1214 1214 VAL VAL B . n 
A 1 1232 GLY 1232 1215 1215 GLY GLY B . n 
A 1 1233 ASN 1233 1216 1216 ASN ASN B . n 
A 1 1234 LEU 1234 1217 1217 LEU LEU B . n 
A 1 1235 SER 1235 1218 1218 SER SER B . n 
A 1 1236 GLN 1236 1219 1219 GLN GLN B . n 
A 1 1237 VAL 1237 1220 1220 VAL VAL B . n 
A 1 1238 VAL 1238 1221 1221 VAL VAL B . n 
A 1 1239 VAL 1239 1222 1222 VAL VAL B . n 
A 1 1240 MET 1240 1223 1223 MET MET B . n 
A 1 1241 LYS 1241 1224 1224 LYS LYS B . n 
A 1 1242 SER 1242 1225 1225 SER SER B . n 
A 1 1243 LYS 1243 1226 1226 LYS LYS B . n 
A 1 1244 ASN 1244 1227 1227 ASN ASN B . n 
A 1 1245 ASP 1245 1228 ?    ?   ?   B . n 
A 1 1246 GLN 1246 1229 ?    ?   ?   B . n 
A 1 1247 GLY 1247 1230 ?    ?   ?   B . n 
A 1 1248 ILE 1248 1231 1231 ILE ILE B . n 
A 1 1249 THR 1249 1232 1232 THR THR B . n 
A 1 1250 ASN 1250 1233 1233 ASN ASN B . n 
A 1 1251 LYS 1251 1234 1234 LYS LYS B . n 
A 1 1252 CYS 1252 1235 1235 CYS CYS B . n 
A 1 1253 LYS 1253 1236 1236 LYS LYS B . n 
A 1 1254 MET 1254 1237 1237 MET MET B . n 
A 1 1255 ASN 1255 1238 1238 ASN ASN B . n 
A 1 1256 LEU 1256 1239 1239 LEU LEU B . n 
A 1 1257 GLN 1257 1240 1240 GLN GLN B . n 
A 1 1258 ASP 1258 1241 1241 ASP ASP B . n 
A 1 1259 ASN 1259 1242 1242 ASN ASN B . n 
A 1 1260 ASN 1260 1243 1243 ASN ASN B . n 
A 1 1261 GLY 1261 1244 1244 GLY GLY B . n 
A 1 1262 ASN 1262 1245 1245 ASN ASN B . n 
A 1 1263 ASP 1263 1246 1246 ASP ASP B . n 
A 1 1264 ILE 1264 1247 1247 ILE ILE B . n 
A 1 1265 GLY 1265 1248 1248 GLY GLY B . n 
A 1 1266 PHE 1266 1249 1249 PHE PHE B . n 
A 1 1267 ILE 1267 1250 1250 ILE ILE B . n 
A 1 1268 GLY 1268 1251 1251 GLY GLY B . n 
A 1 1269 PHE 1269 1252 1252 PHE PHE B . n 
A 1 1270 HIS 1270 1253 1253 HIS HIS B . n 
A 1 1271 GLN 1271 1254 1254 GLN GLN B . n 
A 1 1272 PHE 1272 1255 1255 PHE PHE B . n 
A 1 1273 ASN 1273 1256 1256 ASN ASN B . n 
A 1 1274 ASN 1274 1257 1257 ASN ASN B . n 
A 1 1275 ILE 1275 1258 1258 ILE ILE B . n 
A 1 1276 ALA 1276 1259 1259 ALA ALA B . n 
A 1 1277 LYS 1277 1260 1260 LYS LYS B . n 
A 1 1278 LEU 1278 1261 1261 LEU LEU B . n 
A 1 1279 VAL 1279 1262 1262 VAL VAL B . n 
A 1 1280 ALA 1280 1263 1263 ALA ALA B . n 
A 1 1281 SER 1281 1264 1264 SER SER B . n 
A 1 1282 ASN 1282 1265 1265 ASN ASN B . n 
A 1 1283 TRP 1283 1266 1266 TRP TRP B . n 
A 1 1284 TYR 1284 1267 1267 TYR TYR B . n 
A 1 1285 ASN 1285 1268 1268 ASN ASN B . n 
A 1 1286 ARG 1286 1269 1269 ARG ARG B . n 
A 1 1287 GLN 1287 1270 1270 GLN GLN B . n 
A 1 1288 ILE 1288 1271 ?    ?   ?   B . n 
A 1 1289 GLU 1289 1272 ?    ?   ?   B . n 
A 1 1290 ARG 1290 1273 ?    ?   ?   B . n 
A 1 1291 SER 1291 1274 ?    ?   ?   B . n 
A 1 1292 SER 1292 1275 ?    ?   ?   B . n 
A 1 1293 ARG 1293 1276 ?    ?   ?   B . n 
A 1 1294 THR 1294 1277 ?    ?   ?   B . n 
A 1 1295 LEU 1295 1278 1278 LEU LEU B . n 
A 1 1296 GLY 1296 1279 1279 GLY GLY B . n 
A 1 1297 CYS 1297 1280 1280 CYS CYS B . n 
A 1 1298 SER 1298 1281 1281 SER SER B . n 
A 1 1299 TRP 1299 1282 1282 TRP TRP B . n 
A 1 1300 GLU 1300 1283 1283 GLU GLU B . n 
A 1 1301 PHE 1301 1284 1284 PHE PHE B . n 
A 1 1302 ILE 1302 1285 1285 ILE ILE B . n 
A 1 1303 PRO 1303 1286 1286 PRO PRO B . n 
A 1 1304 VAL 1304 1287 1287 VAL VAL B . n 
A 1 1305 ASP 1305 1288 1288 ASP ASP B . n 
A 1 1306 ASP 1306 1289 1289 ASP ASP B . n 
A 1 1307 GLY 1307 1290 1290 GLY GLY B . n 
A 1 1308 TRP 1308 1291 1291 TRP TRP B . n 
A 1 1309 GLY 1309 1292 1292 GLY GLY B . n 
A 1 1310 GLU 1310 1293 1293 GLU GLU B . n 
A 1 1311 ARG 1311 1294 1294 ARG ARG B . n 
A 1 1312 PRO 1312 1295 1295 PRO PRO B . n 
A 1 1313 LEU 1313 1296 1296 LEU LEU B . n 
A 1 1314 VAL 1314 1297 ?    ?   ?   B . n 
A 1 1315 PRO 1315 1298 ?    ?   ?   B . n 
A 1 1316 PRO 1316 1299 ?    ?   ?   B . n 
A 1 1317 THR 1317 1300 ?    ?   ?   B . n 
A 1 1318 PRO 1318 1301 ?    ?   ?   B . n 
A 1 1319 GLY 1319 1302 ?    ?   ?   B . n 
A 1 1320 SER 1320 1303 ?    ?   ?   B . n 
A 1 1321 ALA 1321 1304 ?    ?   ?   B . n 
A 1 1322 TRP 1322 1305 ?    ?   ?   B . n 
A 1 1323 SER 1323 1306 ?    ?   ?   B . n 
A 1 1324 HIS 1324 1307 ?    ?   ?   B . n 
A 1 1325 PRO 1325 1308 ?    ?   ?   B . n 
A 1 1326 GLN 1326 1309 ?    ?   ?   B . n 
A 1 1327 PHE 1327 1310 ?    ?   ?   B . n 
A 1 1328 GLU 1328 1311 ?    ?   ?   B . n 
A 1 1329 LYS 1329 1312 ?    ?   ?   B . n 
B 2 1    MET 1    1    ?    ?   ?   A . n 
B 2 2    ASP 2    2    ?    ?   ?   A . n 
B 2 3    ASP 3    3    ?    ?   ?   A . n 
B 2 4    TYR 4    4    ?    ?   ?   A . n 
B 2 5    LYS 5    5    ?    ?   ?   A . n 
B 2 6    TYR 6    6    ?    ?   ?   A . n 
B 2 7    GLN 7    7    ?    ?   ?   A . n 
B 2 8    ASP 8    8    ?    ?   ?   A . n 
B 2 9    ASN 9    9    ?    ?   ?   A . n 
B 2 10   TYR 10   10   ?    ?   ?   A . n 
B 2 11   GLY 11   11   ?    ?   ?   A . n 
B 2 12   GLY 12   12   ?    ?   ?   A . n 
B 2 13   TYR 13   13   ?    ?   ?   A . n 
B 2 14   ALA 14   14   ?    ?   ?   A . n 
B 2 15   PRO 15   15   ?    ?   ?   A . n 
B 2 16   SER 16   16   ?    ?   ?   A . n 
B 2 17   ASP 17   17   ?    ?   ?   A . n 
B 2 18   GLY 18   18   ?    ?   ?   A . n 
B 2 19   TYR 19   19   ?    ?   ?   A . n 
B 2 20   TYR 20   20   ?    ?   ?   A . n 
B 2 21   ARG 21   21   ?    ?   ?   A . n 
B 2 22   GLY 22   22   ?    ?   ?   A . n 
B 2 23   ASN 23   23   ?    ?   ?   A . n 
B 2 24   GLU 24   24   ?    ?   ?   A . n 
B 2 25   SER 25   25   ?    ?   ?   A . n 
B 2 26   ASN 26   26   ?    ?   ?   A . n 
B 2 27   PRO 27   27   ?    ?   ?   A . n 
B 2 28   GLU 28   28   ?    ?   ?   A . n 
B 2 29   GLU 29   29   ?    ?   ?   A . n 
B 2 30   ASP 30   30   ?    ?   ?   A . n 
B 2 31   ALA 31   31   ?    ?   ?   A . n 
B 2 32   GLN 32   32   ?    ?   ?   A . n 
B 2 33   SER 33   33   ?    ?   ?   A . n 
B 2 34   ASP 34   34   ?    ?   ?   A . n 
B 2 35   VAL 35   35   ?    ?   ?   A . n 
B 2 36   THR 36   36   ?    ?   ?   A . n 
B 2 37   GLU 37   37   ?    ?   ?   A . n 
B 2 38   GLY 38   38   ?    ?   ?   A . n 
B 2 39   HIS 39   39   ?    ?   ?   A . n 
B 2 40   ASP 40   40   ?    ?   ?   A . n 
B 2 41   GLU 41   41   ?    ?   ?   A . n 
B 2 42   GLU 42   42   ?    ?   ?   A . n 
B 2 43   ASP 43   43   ?    ?   ?   A . n 
B 2 44   GLU 44   44   ?    ?   ?   A . n 
B 2 45   ILE 45   45   ?    ?   ?   A . n 
B 2 46   TYR 46   46   ?    ?   ?   A . n 
B 2 47   GLU 47   47   ?    ?   ?   A . n 
B 2 48   GLY 48   48   ?    ?   ?   A . n 
B 2 49   GLU 49   49   ?    ?   ?   A . n 
B 2 50   TYR 50   50   ?    ?   ?   A . n 
B 2 51   GLN 51   51   ?    ?   ?   A . n 
B 2 52   GLY 52   52   ?    ?   ?   A . n 
B 2 53   ILE 53   53   ?    ?   ?   A . n 
B 2 54   PRO 54   54   ?    ?   ?   A . n 
B 2 55   HIS 55   55   ?    ?   ?   A . n 
B 2 56   PRO 56   56   ?    ?   ?   A . n 
B 2 57   ASP 57   57   ?    ?   ?   A . n 
B 2 58   ASP 58   58   ?    ?   ?   A . n 
B 2 59   VAL 59   59   ?    ?   ?   A . n 
B 2 60   LYS 60   60   ?    ?   ?   A . n 
B 2 61   ALA 61   61   ?    ?   ?   A . n 
B 2 62   LYS 62   62   ?    ?   ?   A . n 
B 2 63   GLN 63   63   ?    ?   ?   A . n 
B 2 64   ALA 64   64   ?    ?   ?   A . n 
B 2 65   LYS 65   65   ?    ?   ?   A . n 
B 2 66   MET 66   66   ?    ?   ?   A . n 
B 2 67   ALA 67   67   ?    ?   ?   A . n 
B 2 68   PRO 68   68   ?    ?   ?   A . n 
B 2 69   SER 69   69   ?    ?   ?   A . n 
B 2 70   ARG 70   70   ?    ?   ?   A . n 
B 2 71   MET 71   71   ?    ?   ?   A . n 
B 2 72   ASP 72   72   ?    ?   ?   A . n 
B 2 73   SER 73   73   ?    ?   ?   A . n 
B 2 74   LEU 74   74   ?    ?   ?   A . n 
B 2 75   ARG 75   75   ?    ?   ?   A . n 
B 2 76   GLY 76   76   ?    ?   ?   A . n 
B 2 77   GLN 77   77   ?    ?   ?   A . n 
B 2 78   THR 78   78   ?    ?   ?   A . n 
B 2 79   ASP 79   79   ?    ?   ?   A . n 
B 2 80   LEU 80   80   ?    ?   ?   A . n 
B 2 81   MET 81   81   ?    ?   ?   A . n 
B 2 82   ALA 82   82   ?    ?   ?   A . n 
B 2 83   GLU 83   83   ?    ?   ?   A . n 
B 2 84   ARG 84   84   ?    ?   ?   A . n 
B 2 85   LEU 85   85   ?    ?   ?   A . n 
B 2 86   GLU 86   86   ?    ?   ?   A . n 
B 2 87   ASP 87   87   ?    ?   ?   A . n 
B 2 88   GLU 88   88   ?    ?   ?   A . n 
B 2 89   GLU 89   89   ?    ?   ?   A . n 
B 2 90   GLN 90   90   ?    ?   ?   A . n 
B 2 91   LEU 91   91   ?    ?   ?   A . n 
B 2 92   ALA 92   92   92   ALA ALA A . n 
B 2 93   HIS 93   93   93   HIS HIS A . n 
B 2 94   GLN 94   94   94   GLN GLN A . n 
B 2 95   TYR 95   95   95   TYR TYR A . n 
B 2 96   GLU 96   96   96   GLU GLU A . n 
B 2 97   THR 97   97   97   THR THR A . n 
B 2 98   ILE 98   98   98   ILE ILE A . n 
B 2 99   MET 99   99   99   MET MET A . n 
B 2 100  ASP 100  100  100  ASP ASP A . n 
B 2 101  GLU 101  101  101  GLU GLU A . n 
B 2 102  CYS 102  102  102  CYS CYS A . n 
B 2 103  GLY 103  103  103  GLY GLY A . n 
B 2 104  HIS 104  104  104  HIS HIS A . n 
B 2 105  GLY 105  105  105  GLY GLY A . n 
B 2 106  ARG 106  106  106  ARG ARG A . n 
B 2 107  PHE 107  107  107  PHE PHE A . n 
B 2 108  GLN 108  108  108  GLN GLN A . n 
B 2 109  TRP 109  109  109  TRP TRP A . n 
B 2 110  ILE 110  110  110  ILE ILE A . n 
B 2 111  LEU 111  111  111  LEU LEU 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  VAL 114  114  114  VAL VAL A . n 
B 2 115  LEU 115  115  115  LEU LEU A . n 
B 2 116  GLY 116  116  116  GLY GLY A . n 
B 2 117  LEU 117  117  117  LEU LEU A . n 
B 2 118  ALA 118  118  118  ALA ALA A . n 
B 2 119  LEU 119  119  119  LEU LEU A . n 
B 2 120  MET 120  120  120  MET MET A . n 
B 2 121  ALA 121  121  121  ALA ALA A . n 
B 2 122  ASP 122  122  122  ASP ASP A . n 
B 2 123  GLY 123  123  123  GLY GLY A . n 
B 2 124  VAL 124  124  124  VAL VAL A . n 
B 2 125  GLU 125  125  125  GLU GLU A . n 
B 2 126  VAL 126  126  126  VAL VAL A . n 
B 2 127  PHE 127  127  127  PHE PHE A . n 
B 2 128  VAL 128  128  128  VAL VAL A . n 
B 2 129  VAL 129  129  129  VAL VAL A . n 
B 2 130  SER 130  130  130  SER SER A . n 
B 2 131  PHE 131  131  131  PHE PHE A . n 
B 2 132  ALA 132  132  132  ALA ALA A . n 
B 2 133  LEU 133  133  133  LEU LEU A . n 
B 2 134  PRO 134  134  134  PRO PRO A . n 
B 2 135  SER 135  135  135  SER SER A . n 
B 2 136  ALA 136  136  136  ALA ALA A . n 
B 2 137  GLU 137  137  137  GLU GLU 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  MET 140  140  140  MET MET A . n 
B 2 141  CYS 141  141  141  CYS CYS A . n 
B 2 142  LEU 142  142  142  LEU LEU A . n 
B 2 143  SER 143  143  143  SER SER A . n 
B 2 144  SER 144  144  144  SER SER A . n 
B 2 145  SER 145  145  145  SER SER A . n 
B 2 146  LYS 146  146  146  LYS LYS A . n 
B 2 147  LYS 147  147  147  LYS LYS A . n 
B 2 148  GLY 148  148  148  GLY GLY A . n 
B 2 149  MET 149  149  149  MET MET A . n 
B 2 150  LEU 150  150  150  LEU LEU A . n 
B 2 151  GLY 151  151  151  GLY GLY A . n 
B 2 152  MET 152  152  152  MET MET A . n 
B 2 153  ILE 153  153  153  ILE ILE A . n 
B 2 154  VAL 154  154  154  VAL VAL A . n 
B 2 155  TYR 155  155  155  TYR TYR A . n 
B 2 156  LEU 156  156  156  LEU LEU A . n 
B 2 157  GLY 157  157  157  GLY GLY A . n 
B 2 158  MET 158  158  158  MET MET A . n 
B 2 159  MET 159  159  159  MET MET A . n 
B 2 160  ALA 160  160  160  ALA ALA A . n 
B 2 161  GLY 161  161  161  GLY GLY A . n 
B 2 162  ALA 162  162  162  ALA ALA A . n 
B 2 163  PHE 163  163  163  PHE PHE A . n 
B 2 164  ILE 164  164  164  ILE ILE A . n 
B 2 165  LEU 165  165  165  LEU LEU A . n 
B 2 166  GLY 166  166  166  GLY GLY A . n 
B 2 167  GLY 167  167  167  GLY GLY A . n 
B 2 168  LEU 168  168  168  LEU LEU A . n 
B 2 169  ALA 169  169  169  ALA ALA A . n 
B 2 170  ASP 170  170  170  ASP ASP A . n 
B 2 171  LYS 171  171  171  LYS LYS A . n 
B 2 172  LEU 172  172  172  LEU LEU A . n 
B 2 173  GLY 173  173  173  GLY GLY A . n 
B 2 174  ARG 174  174  174  ARG ARG A . n 
B 2 175  LYS 175  175  175  LYS LYS A . n 
B 2 176  ARG 176  176  176  ARG ARG A . n 
B 2 177  VAL 177  177  177  VAL VAL A . n 
B 2 178  LEU 178  178  178  LEU LEU A . n 
B 2 179  SER 179  179  179  SER SER A . n 
B 2 180  MET 180  180  180  MET MET A . n 
B 2 181  SER 181  181  181  SER SER A . n 
B 2 182  LEU 182  182  182  LEU LEU A . n 
B 2 183  ALA 183  183  183  ALA ALA A . n 
B 2 184  VAL 184  184  184  VAL VAL A . n 
B 2 185  ASN 185  185  185  ASN ASN A . n 
B 2 186  ALA 186  186  186  ALA ALA A . n 
B 2 187  SER 187  187  187  SER SER A . n 
B 2 188  PHE 188  188  188  PHE PHE A . n 
B 2 189  ALA 189  189  189  ALA ALA A . n 
B 2 190  SER 190  190  190  SER SER A . n 
B 2 191  LEU 191  191  191  LEU LEU A . n 
B 2 192  SER 192  192  192  SER SER A . n 
B 2 193  SER 193  193  193  SER SER A . n 
B 2 194  PHE 194  194  194  PHE PHE A . n 
B 2 195  VAL 195  195  195  VAL VAL A . n 
B 2 196  GLN 196  196  196  GLN GLN A . n 
B 2 197  GLY 197  197  197  GLY GLY A . n 
B 2 198  TYR 198  198  198  TYR TYR A . n 
B 2 199  GLY 199  199  199  GLY GLY A . n 
B 2 200  ALA 200  200  200  ALA ALA A . n 
B 2 201  PHE 201  201  201  PHE PHE A . n 
B 2 202  LEU 202  202  202  LEU LEU A . n 
B 2 203  PHE 203  203  203  PHE PHE A . n 
B 2 204  CYS 204  204  204  CYS CYS A . n 
B 2 205  ARG 205  205  205  ARG ARG A . n 
B 2 206  LEU 206  206  206  LEU LEU A . n 
B 2 207  ILE 207  207  207  ILE ILE A . n 
B 2 208  SER 208  208  208  SER SER A . n 
B 2 209  GLY 209  209  209  GLY GLY A . n 
B 2 210  ILE 210  210  210  ILE ILE A . n 
B 2 211  GLY 211  211  211  GLY GLY A . n 
B 2 212  ILE 212  212  212  ILE ILE A . n 
B 2 213  GLY 213  213  213  GLY GLY A . n 
B 2 214  GLY 214  214  214  GLY GLY A . n 
B 2 215  ALA 215  215  215  ALA ALA A . n 
B 2 216  LEU 216  216  216  LEU LEU A . n 
B 2 217  PRO 217  217  217  PRO PRO A . n 
B 2 218  ILE 218  218  218  ILE ILE A . n 
B 2 219  VAL 219  219  219  VAL VAL A . n 
B 2 220  PHE 220  220  220  PHE PHE A . n 
B 2 221  ALA 221  221  221  ALA ALA A . n 
B 2 222  TYR 222  222  222  TYR TYR A . n 
B 2 223  PHE 223  223  223  PHE PHE A . n 
B 2 224  SER 224  224  224  SER SER A . n 
B 2 225  GLU 225  225  225  GLU GLU A . n 
B 2 226  PHE 226  226  226  PHE PHE A . n 
B 2 227  LEU 227  227  227  LEU LEU A . n 
B 2 228  SER 228  228  228  SER SER A . n 
B 2 229  ARG 229  229  229  ARG ARG A . n 
B 2 230  GLU 230  230  230  GLU GLU A . n 
B 2 231  LYS 231  231  231  LYS LYS A . n 
B 2 232  ARG 232  232  232  ARG ARG A . n 
B 2 233  GLY 233  233  233  GLY GLY A . n 
B 2 234  GLU 234  234  234  GLU GLU A . n 
B 2 235  HIS 235  235  235  HIS HIS A . n 
B 2 236  LEU 236  236  236  LEU LEU A . n 
B 2 237  SER 237  237  237  SER SER A . n 
B 2 238  TRP 238  238  238  TRP TRP A . n 
B 2 239  LEU 239  239  239  LEU LEU A . n 
B 2 240  GLY 240  240  240  GLY GLY A . n 
B 2 241  ILE 241  241  241  ILE ILE A . n 
B 2 242  PHE 242  242  242  PHE PHE A . n 
B 2 243  TRP 243  243  243  TRP TRP A . n 
B 2 244  MET 244  244  244  MET MET A . n 
B 2 245  THR 245  245  245  THR THR A . n 
B 2 246  GLY 246  246  246  GLY GLY A . n 
B 2 247  GLY 247  247  247  GLY GLY A . n 
B 2 248  LEU 248  248  248  LEU LEU A . n 
B 2 249  TYR 249  249  249  TYR TYR A . n 
B 2 250  ALA 250  250  250  ALA ALA A . n 
B 2 251  SER 251  251  251  SER SER A . n 
B 2 252  ALA 252  252  252  ALA ALA A . n 
B 2 253  MET 253  253  253  MET MET A . n 
B 2 254  ALA 254  254  254  ALA ALA A . n 
B 2 255  TRP 255  255  255  TRP TRP A . n 
B 2 256  SER 256  256  256  SER SER A . n 
B 2 257  ILE 257  257  257  ILE ILE A . n 
B 2 258  ILE 258  258  258  ILE ILE A . n 
B 2 259  PRO 259  259  259  PRO PRO A . n 
B 2 260  HIS 260  260  260  HIS HIS A . n 
B 2 261  TYR 261  261  261  TYR TYR A . n 
B 2 262  GLY 262  262  262  GLY GLY A . n 
B 2 263  TRP 263  263  263  TRP TRP A . n 
B 2 264  GLY 264  264  264  GLY GLY A . n 
B 2 265  PHE 265  265  265  PHE PHE A . n 
B 2 266  SER 266  266  266  SER SER A . n 
B 2 267  MET 267  267  267  MET MET A . n 
B 2 268  GLY 268  268  268  GLY GLY A . n 
B 2 269  THR 269  269  269  THR THR A . n 
B 2 270  ASN 270  270  270  ASN ASN A . n 
B 2 271  TYR 271  271  271  TYR TYR A . n 
B 2 272  HIS 272  272  272  HIS HIS A . n 
B 2 273  PHE 273  273  273  PHE PHE A . n 
B 2 274  HIS 274  274  274  HIS HIS A . n 
B 2 275  SER 275  275  275  SER SER A . n 
B 2 276  TRP 276  276  276  TRP TRP A . n 
B 2 277  ARG 277  277  277  ARG ARG A . n 
B 2 278  VAL 278  278  278  VAL VAL A . n 
B 2 279  PHE 279  279  279  PHE PHE A . n 
B 2 280  VAL 280  280  280  VAL VAL 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  CYS 283  283  283  CYS CYS A . n 
B 2 284  ALA 284  284  284  ALA ALA A . n 
B 2 285  LEU 285  285  285  LEU LEU A . n 
B 2 286  PRO 286  286  286  PRO PRO A . n 
B 2 287  CYS 287  287  287  CYS CYS A . n 
B 2 288  THR 288  288  288  THR THR A . n 
B 2 289  VAL 289  289  289  VAL VAL A . n 
B 2 290  SER 290  290  290  SER SER A . n 
B 2 291  MET 291  291  291  MET MET 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  LEU 294  294  294  LEU LEU A . n 
B 2 295  LYS 295  295  295  LYS LYS A . n 
B 2 296  PHE 296  296  296  PHE PHE A . n 
B 2 297  MET 297  297  297  MET MET A . n 
B 2 298  PRO 298  298  298  PRO PRO A . n 
B 2 299  GLU 299  299  299  GLU GLU A . n 
B 2 300  SER 300  300  300  SER SER A . n 
B 2 301  PRO 301  301  301  PRO PRO A . n 
B 2 302  ARG 302  302  302  ARG ARG A . n 
B 2 303  PHE 303  303  303  PHE PHE A . n 
B 2 304  LEU 304  304  304  LEU LEU A . n 
B 2 305  LEU 305  305  305  LEU LEU A . n 
B 2 306  GLU 306  306  306  GLU GLU A . n 
B 2 307  MET 307  307  307  MET MET A . n 
B 2 308  GLY 308  308  308  GLY GLY A . n 
B 2 309  LYS 309  309  309  LYS LYS A . n 
B 2 310  HIS 310  310  310  HIS HIS A . n 
B 2 311  ASP 311  311  311  ASP ASP A . n 
B 2 312  GLU 312  312  312  GLU GLU A . n 
B 2 313  ALA 313  313  313  ALA ALA A . n 
B 2 314  TRP 314  314  314  TRP TRP A . n 
B 2 315  MET 315  315  315  MET MET A . n 
B 2 316  ILE 316  316  316  ILE ILE A . n 
B 2 317  LEU 317  317  317  LEU LEU A . n 
B 2 318  LYS 318  318  318  LYS LYS A . n 
B 2 319  GLN 319  319  319  GLN GLN A . n 
B 2 320  VAL 320  320  320  VAL VAL A . n 
B 2 321  HIS 321  321  321  HIS HIS A . n 
B 2 322  ASP 322  322  322  ASP ASP A . n 
B 2 323  THR 323  323  323  THR THR A . n 
B 2 324  ASN 324  324  324  ASN ASN A . n 
B 2 325  MET 325  325  325  MET MET A . n 
B 2 326  ARG 326  326  326  ARG ARG A . n 
B 2 327  ALA 327  327  327  ALA ALA A . n 
B 2 328  LYS 328  328  328  LYS LYS A . n 
B 2 329  GLY 329  329  329  GLY GLY A . n 
B 2 330  THR 330  330  ?    ?   ?   A . n 
B 2 331  PRO 331  331  ?    ?   ?   A . n 
B 2 332  GLU 332  332  ?    ?   ?   A . n 
B 2 333  LYS 333  333  ?    ?   ?   A . n 
B 2 334  VAL 334  334  ?    ?   ?   A . n 
B 2 335  PHE 335  335  ?    ?   ?   A . n 
B 2 336  THR 336  336  ?    ?   ?   A . n 
B 2 337  VAL 337  337  ?    ?   ?   A . n 
B 2 338  SER 338  338  ?    ?   ?   A . n 
B 2 339  ASN 339  339  ?    ?   ?   A . n 
B 2 340  ILE 340  340  ?    ?   ?   A . n 
B 2 341  LYS 341  341  ?    ?   ?   A . n 
B 2 342  THR 342  342  ?    ?   ?   A . n 
B 2 343  PRO 343  343  ?    ?   ?   A . n 
B 2 344  LYS 344  344  ?    ?   ?   A . n 
B 2 345  GLN 345  345  ?    ?   ?   A . n 
B 2 346  MET 346  346  ?    ?   ?   A . n 
B 2 347  ASP 347  347  ?    ?   ?   A . n 
B 2 348  GLU 348  348  ?    ?   ?   A . n 
B 2 349  PHE 349  349  ?    ?   ?   A . n 
B 2 350  ILE 350  350  ?    ?   ?   A . n 
B 2 351  GLU 351  351  ?    ?   ?   A . n 
B 2 352  ILE 352  352  ?    ?   ?   A . n 
B 2 353  GLN 353  353  ?    ?   ?   A . n 
B 2 354  SER 354  354  ?    ?   ?   A . n 
B 2 355  SER 355  355  ?    ?   ?   A . n 
B 2 356  THR 356  356  ?    ?   ?   A . n 
B 2 357  GLY 357  357  ?    ?   ?   A . n 
B 2 358  THR 358  358  ?    ?   ?   A . n 
B 2 359  TRP 359  359  ?    ?   ?   A . n 
B 2 360  TYR 360  360  ?    ?   ?   A . n 
B 2 361  GLN 361  361  ?    ?   ?   A . n 
B 2 362  ARG 362  362  ?    ?   ?   A . n 
B 2 363  TRP 363  363  ?    ?   ?   A . n 
B 2 364  LEU 364  364  ?    ?   ?   A . n 
B 2 365  VAL 365  365  ?    ?   ?   A . n 
B 2 366  ARG 366  366  ?    ?   ?   A . n 
B 2 367  PHE 367  367  ?    ?   ?   A . n 
B 2 368  LYS 368  368  ?    ?   ?   A . n 
B 2 369  THR 369  369  ?    ?   ?   A . n 
B 2 370  ILE 370  370  370  ILE ILE A . n 
B 2 371  PHE 371  371  371  PHE PHE A . n 
B 2 372  LYS 372  372  372  LYS LYS A . n 
B 2 373  GLN 373  373  373  GLN GLN A . n 
B 2 374  VAL 374  374  374  VAL VAL A . n 
B 2 375  TRP 375  375  375  TRP TRP A . n 
B 2 376  ASP 376  376  376  ASP ASP A . n 
B 2 377  ASN 377  377  377  ASN ASN A . n 
B 2 378  ALA 378  378  378  ALA ALA A . n 
B 2 379  LEU 379  379  379  LEU LEU A . n 
B 2 380  TYR 380  380  380  TYR TYR A . n 
B 2 381  CYS 381  381  381  CYS CYS A . n 
B 2 382  VAL 382  382  382  VAL VAL A . n 
B 2 383  MET 383  383  383  MET MET A . n 
B 2 384  GLY 384  384  384  GLY GLY A . n 
B 2 385  PRO 385  385  385  PRO PRO A . n 
B 2 386  TYR 386  386  386  TYR TYR A . n 
B 2 387  ARG 387  387  387  ARG ARG A . n 
B 2 388  MET 388  388  388  MET MET A . n 
B 2 389  ASN 389  389  389  ASN ASN A . n 
B 2 390  THR 390  390  390  THR THR A . n 
B 2 391  LEU 391  391  391  LEU LEU A . n 
B 2 392  ILE 392  392  392  ILE ILE A . n 
B 2 393  LEU 393  393  393  LEU LEU A . n 
B 2 394  ALA 394  394  394  ALA ALA A . n 
B 2 395  VAL 395  395  395  VAL VAL A . n 
B 2 396  VAL 396  396  396  VAL VAL A . n 
B 2 397  TRP 397  397  397  TRP TRP A . n 
B 2 398  PHE 398  398  398  PHE PHE A . n 
B 2 399  ALA 399  399  399  ALA ALA A . n 
B 2 400  MET 400  400  400  MET MET A . n 
B 2 401  ALA 401  401  401  ALA ALA A . n 
B 2 402  PHE 402  402  402  PHE PHE A . n 
B 2 403  SER 403  403  403  SER SER A . n 
B 2 404  TYR 404  404  404  TYR TYR A . n 
B 2 405  TYR 405  405  405  TYR TYR A . n 
B 2 406  GLY 406  406  406  GLY GLY A . n 
B 2 407  LEU 407  407  407  LEU LEU A . n 
B 2 408  THR 408  408  408  THR THR A . n 
B 2 409  VAL 409  409  409  VAL VAL A . n 
B 2 410  TRP 410  410  410  TRP TRP A . n 
B 2 411  PHE 411  411  411  PHE PHE A . n 
B 2 412  PRO 412  412  412  PRO PRO A . n 
B 2 413  ASP 413  413  413  ASP ASP A . n 
B 2 414  MET 414  414  414  MET MET A . n 
B 2 415  ILE 415  415  415  ILE ILE A . n 
B 2 416  ARG 416  416  416  ARG ARG A . n 
B 2 417  TYR 417  417  417  TYR TYR A . n 
B 2 418  PHE 418  418  418  PHE PHE A . n 
B 2 419  GLN 419  419  419  GLN GLN A . n 
B 2 420  ASP 420  420  420  ASP ASP A . n 
B 2 421  GLU 421  421  421  GLU GLU A . n 
B 2 422  GLU 422  422  422  GLU GLU A . n 
B 2 423  TYR 423  423  423  TYR TYR A . n 
B 2 424  LYS 424  424  424  LYS LYS A . n 
B 2 425  SER 425  425  425  SER SER A . n 
B 2 426  LYS 426  426  426  LYS LYS A . n 
B 2 427  MET 427  427  427  MET MET A . n 
B 2 428  LYS 428  428  428  LYS LYS A . n 
B 2 429  VAL 429  429  429  VAL VAL A . n 
B 2 430  PHE 430  430  430  PHE PHE A . n 
B 2 431  PHE 431  431  431  PHE PHE A . n 
B 2 432  GLY 432  432  432  GLY GLY A . n 
B 2 433  GLU 433  433  433  GLU GLU A . n 
B 2 434  HIS 434  434  434  HIS HIS A . n 
B 2 435  VAL 435  435  435  VAL VAL A . n 
B 2 436  TYR 436  436  436  TYR TYR A . n 
B 2 437  GLY 437  437  437  GLY GLY A . n 
B 2 438  ALA 438  438  438  ALA ALA A . n 
B 2 439  THR 439  439  439  THR THR A . n 
B 2 440  ILE 440  440  440  ILE ILE A . n 
B 2 441  ASN 441  441  441  ASN ASN A . n 
B 2 442  PHE 442  442  442  PHE PHE A . n 
B 2 443  THR 443  443  443  THR THR A . n 
B 2 444  MET 444  444  444  MET MET A . n 
B 2 445  GLU 445  445  445  GLU GLU A . n 
B 2 446  ASN 446  446  446  ASN ASN A . n 
B 2 447  GLN 447  447  447  GLN GLN A . n 
B 2 448  ILE 448  448  448  ILE ILE A . n 
B 2 449  HIS 449  449  449  HIS HIS A . n 
B 2 450  GLN 450  450  450  GLN GLN A . n 
B 2 451  HIS 451  451  451  HIS HIS A . n 
B 2 452  GLY 452  452  452  GLY GLY A . n 
B 2 453  LYS 453  453  453  LYS LYS A . n 
B 2 454  LEU 454  454  454  LEU LEU A . n 
B 2 455  VAL 455  455  455  VAL VAL A . n 
B 2 456  ASN 456  456  456  ASN ASN A . n 
B 2 457  ASP 457  457  457  ASP ASP A . n 
B 2 458  LYS 458  458  458  LYS LYS A . n 
B 2 459  PHE 459  459  459  PHE PHE A . n 
B 2 460  THR 460  460  460  THR THR A . n 
B 2 461  ARG 461  461  461  ARG ARG A . n 
B 2 462  MET 462  462  462  MET MET A . n 
B 2 463  TYR 463  463  463  TYR TYR A . n 
B 2 464  PHE 464  464  464  PHE PHE A . n 
B 2 465  LYS 465  465  465  LYS LYS A . n 
B 2 466  HIS 466  466  466  HIS HIS A . n 
B 2 467  VAL 467  467  467  VAL VAL A . n 
B 2 468  LEU 468  468  468  LEU LEU A . n 
B 2 469  PHE 469  469  469  PHE PHE A . n 
B 2 470  GLU 470  470  470  GLU GLU A . n 
B 2 471  ASP 471  471  471  ASP ASP A . n 
B 2 472  THR 472  472  472  THR THR A . n 
B 2 473  PHE 473  473  473  PHE PHE A . n 
B 2 474  PHE 474  474  474  PHE PHE A . n 
B 2 475  ASP 475  475  475  ASP ASP A . n 
B 2 476  GLU 476  476  476  GLU GLU A . n 
B 2 477  CYS 477  477  477  CYS CYS A . n 
B 2 478  TYR 478  478  478  TYR TYR A . n 
B 2 479  PHE 479  479  479  PHE PHE A . n 
B 2 480  GLU 480  480  480  GLU GLU A . n 
B 2 481  ASP 481  481  481  ASP ASP A . n 
B 2 482  VAL 482  482  482  VAL VAL A . n 
B 2 483  THR 483  483  483  THR THR A . n 
B 2 484  SER 484  484  484  SER SER A . n 
B 2 485  THR 485  485  485  THR THR A . n 
B 2 486  ASP 486  486  486  ASP ASP A . n 
B 2 487  THR 487  487  487  THR THR A . n 
B 2 488  TYR 488  488  488  TYR TYR A . n 
B 2 489  PHE 489  489  489  PHE PHE A . n 
B 2 490  LYS 490  490  490  LYS LYS A . n 
B 2 491  ASN 491  491  491  ASN ASN A . n 
B 2 492  CYS 492  492  492  CYS CYS A . n 
B 2 493  THR 493  493  493  THR THR A . n 
B 2 494  ILE 494  494  494  ILE ILE A . n 
B 2 495  GLU 495  495  495  GLU GLU A . n 
B 2 496  SER 496  496  496  SER SER A . n 
B 2 497  THR 497  497  497  THR THR A . n 
B 2 498  ILE 498  498  498  ILE ILE A . n 
B 2 499  PHE 499  499  499  PHE PHE A . n 
B 2 500  TYR 500  500  500  TYR TYR A . n 
B 2 501  ASN 501  501  501  ASN ASN A . n 
B 2 502  THR 502  502  502  THR THR A . n 
B 2 503  ASP 503  503  503  ASP ASP A . n 
B 2 504  LEU 504  504  504  LEU LEU A . n 
B 2 505  TYR 505  505  505  TYR TYR A . n 
B 2 506  GLU 506  506  506  GLU GLU A . n 
B 2 507  HIS 507  507  507  HIS HIS A . n 
B 2 508  LYS 508  508  508  LYS LYS A . n 
B 2 509  PHE 509  509  509  PHE PHE A . n 
B 2 510  ILE 510  510  510  ILE ILE A . n 
B 2 511  ASN 511  511  511  ASN ASN A . n 
B 2 512  CYS 512  512  512  CYS CYS A . n 
B 2 513  ARG 513  513  513  ARG ARG A . n 
B 2 514  PHE 514  514  514  PHE PHE A . n 
B 2 515  ILE 515  515  515  ILE ILE A . n 
B 2 516  ASN 516  516  516  ASN ASN A . n 
B 2 517  SER 517  517  517  SER SER A . n 
B 2 518  THR 518  518  518  THR THR A . n 
B 2 519  PHE 519  519  519  PHE PHE A . n 
B 2 520  LEU 520  520  520  LEU LEU A . n 
B 2 521  GLU 521  521  521  GLU GLU A . n 
B 2 522  GLN 522  522  522  GLN GLN A . n 
B 2 523  LYS 523  523  523  LYS LYS A . n 
B 2 524  GLU 524  524  524  GLU GLU A . n 
B 2 525  GLY 525  525  525  GLY GLY A . n 
B 2 526  CYS 526  526  526  CYS CYS A . n 
B 2 527  HIS 527  527  527  HIS HIS A . n 
B 2 528  MET 528  528  528  MET MET A . n 
B 2 529  ASP 529  529  529  ASP ASP A . n 
B 2 530  LEU 530  530  530  LEU LEU A . n 
B 2 531  GLU 531  531  531  GLU GLU A . n 
B 2 532  GLN 532  532  532  GLN GLN A . n 
B 2 533  ASP 533  533  533  ASP ASP A . n 
B 2 534  ASN 534  534  534  ASN ASN A . n 
B 2 535  ASP 535  535  535  ASP ASP A . n 
B 2 536  PHE 536  536  536  PHE PHE A . n 
B 2 537  LEU 537  537  537  LEU LEU A . n 
B 2 538  ILE 538  538  538  ILE ILE A . n 
B 2 539  TYR 539  539  539  TYR TYR A . n 
B 2 540  LEU 540  540  540  LEU LEU A . n 
B 2 541  VAL 541  541  541  VAL VAL A . n 
B 2 542  SER 542  542  542  SER SER A . n 
B 2 543  PHE 543  543  543  PHE PHE A . n 
B 2 544  LEU 544  544  544  LEU LEU A . n 
B 2 545  GLY 545  545  545  GLY GLY A . n 
B 2 546  SER 546  546  546  SER SER A . n 
B 2 547  LEU 547  547  547  LEU LEU A . n 
B 2 548  SER 548  548  548  SER SER A . n 
B 2 549  VAL 549  549  549  VAL VAL A . n 
B 2 550  LEU 550  550  550  LEU LEU A . n 
B 2 551  PRO 551  551  551  PRO PRO A . n 
B 2 552  GLY 552  552  552  GLY GLY A . n 
B 2 553  ASN 553  553  553  ASN ASN A . n 
B 2 554  ILE 554  554  554  ILE ILE A . n 
B 2 555  ILE 555  555  555  ILE ILE A . n 
B 2 556  SER 556  556  556  SER SER A . n 
B 2 557  ALA 557  557  557  ALA ALA A . n 
B 2 558  LEU 558  558  558  LEU LEU A . n 
B 2 559  LEU 559  559  559  LEU LEU A . n 
B 2 560  MET 560  560  560  MET MET A . n 
B 2 561  ASP 561  561  561  ASP ASP A . n 
B 2 562  ARG 562  562  562  ARG ARG A . n 
B 2 563  ILE 563  563  563  ILE ILE A . n 
B 2 564  GLY 564  564  564  GLY GLY A . n 
B 2 565  ARG 565  565  565  ARG ARG A . n 
B 2 566  LEU 566  566  566  LEU LEU A . n 
B 2 567  LYS 567  567  567  LYS LYS A . n 
B 2 568  MET 568  568  568  MET MET A . n 
B 2 569  ILE 569  569  569  ILE ILE A . n 
B 2 570  GLY 570  570  570  GLY GLY A . n 
B 2 571  GLY 571  571  571  GLY GLY A . n 
B 2 572  SER 572  572  572  SER SER A . n 
B 2 573  MET 573  573  573  MET MET A . n 
B 2 574  LEU 574  574  574  LEU LEU A . n 
B 2 575  ILE 575  575  575  ILE ILE A . n 
B 2 576  SER 576  576  576  SER SER A . n 
B 2 577  ALA 577  577  577  ALA ALA A . n 
B 2 578  VAL 578  578  578  VAL VAL A . n 
B 2 579  CYS 579  579  579  CYS CYS A . n 
B 2 580  CYS 580  580  580  CYS CYS A . n 
B 2 581  PHE 581  581  581  PHE PHE A . n 
B 2 582  PHE 582  582  582  PHE PHE A . n 
B 2 583  LEU 583  583  583  LEU LEU A . n 
B 2 584  PHE 584  584  584  PHE PHE A . n 
B 2 585  PHE 585  585  585  PHE PHE A . n 
B 2 586  GLY 586  586  586  GLY GLY A . n 
B 2 587  ASN 587  587  587  ASN ASN A . n 
B 2 588  SER 588  588  588  SER SER A . n 
B 2 589  GLU 589  589  589  GLU GLU A . n 
B 2 590  SER 590  590  590  SER SER A . n 
B 2 591  ALA 591  591  591  ALA ALA A . n 
B 2 592  MET 592  592  592  MET MET A . n 
B 2 593  ILE 593  593  593  ILE ILE A . n 
B 2 594  GLY 594  594  594  GLY GLY A . n 
B 2 595  TRP 595  595  595  TRP TRP A . n 
B 2 596  GLN 596  596  596  GLN GLN A . n 
B 2 597  CYS 597  597  597  CYS CYS A . n 
B 2 598  LEU 598  598  598  LEU LEU A . n 
B 2 599  PHE 599  599  599  PHE PHE A . n 
B 2 600  CYS 600  600  600  CYS CYS A . n 
B 2 601  GLY 601  601  601  GLY GLY A . n 
B 2 602  THR 602  602  602  THR THR A . n 
B 2 603  SER 603  603  603  SER SER A . n 
B 2 604  ILE 604  604  604  ILE ILE A . n 
B 2 605  ALA 605  605  605  ALA ALA A . n 
B 2 606  ALA 606  606  606  ALA ALA A . n 
B 2 607  TRP 607  607  607  TRP TRP A . n 
B 2 608  ASN 608  608  608  ASN ASN A . n 
B 2 609  ALA 609  609  609  ALA ALA A . n 
B 2 610  LEU 610  610  610  LEU LEU A . n 
B 2 611  ASP 611  611  611  ASP ASP A . n 
B 2 612  VAL 612  612  612  VAL VAL A . n 
B 2 613  ILE 613  613  613  ILE ILE A . n 
B 2 614  THR 614  614  614  THR THR A . n 
B 2 615  VAL 615  615  615  VAL VAL A . n 
B 2 616  GLU 616  616  616  GLU GLU A . n 
B 2 617  LEU 617  617  617  LEU LEU A . n 
B 2 618  TYR 618  618  618  TYR TYR A . n 
B 2 619  PRO 619  619  619  PRO PRO A . n 
B 2 620  THR 620  620  620  THR THR A . n 
B 2 621  ASN 621  621  621  ASN ASN A . n 
B 2 622  GLN 622  622  622  GLN GLN A . n 
B 2 623  ARG 623  623  623  ARG ARG A . n 
B 2 624  ALA 624  624  624  ALA ALA A . n 
B 2 625  THR 625  625  625  THR THR A . n 
B 2 626  ALA 626  626  626  ALA ALA A . n 
B 2 627  PHE 627  627  627  PHE PHE A . n 
B 2 628  GLY 628  628  628  GLY GLY A . n 
B 2 629  ILE 629  629  629  ILE ILE A . n 
B 2 630  LEU 630  630  630  LEU LEU A . n 
B 2 631  ASN 631  631  631  ASN ASN A . n 
B 2 632  GLY 632  632  632  GLY GLY A . n 
B 2 633  LEU 633  633  633  LEU LEU A . n 
B 2 634  CYS 634  634  634  CYS CYS A . n 
B 2 635  LYS 635  635  635  LYS LYS A . n 
B 2 636  PHE 636  636  636  PHE PHE A . n 
B 2 637  GLY 637  637  637  GLY GLY A . n 
B 2 638  ALA 638  638  638  ALA ALA A . n 
B 2 639  ILE 639  639  639  ILE ILE A . n 
B 2 640  LEU 640  640  640  LEU LEU A . n 
B 2 641  GLY 641  641  641  GLY GLY A . n 
B 2 642  ASN 642  642  642  ASN ASN A . n 
B 2 643  THR 643  643  643  THR THR A . n 
B 2 644  ILE 644  644  644  ILE ILE A . n 
B 2 645  PHE 645  645  645  PHE PHE A . n 
B 2 646  ALA 646  646  646  ALA ALA A . n 
B 2 647  SER 647  647  647  SER SER A . n 
B 2 648  PHE 648  648  648  PHE PHE A . n 
B 2 649  VAL 649  649  649  VAL VAL A . n 
B 2 650  GLY 650  650  650  GLY GLY A . n 
B 2 651  ILE 651  651  651  ILE ILE A . n 
B 2 652  THR 652  652  652  THR THR A . n 
B 2 653  LYS 653  653  653  LYS LYS A . n 
B 2 654  VAL 654  654  654  VAL VAL A . n 
B 2 655  VAL 655  655  655  VAL VAL A . n 
B 2 656  PRO 656  656  656  PRO PRO A . n 
B 2 657  ILE 657  657  657  ILE ILE A . n 
B 2 658  LEU 658  658  658  LEU LEU A . n 
B 2 659  LEU 659  659  659  LEU LEU A . n 
B 2 660  ALA 660  660  660  ALA ALA A . n 
B 2 661  ALA 661  661  661  ALA ALA A . n 
B 2 662  ALA 662  662  662  ALA ALA A . n 
B 2 663  SER 663  663  663  SER SER A . n 
B 2 664  LEU 664  664  664  LEU LEU A . n 
B 2 665  VAL 665  665  665  VAL VAL A . n 
B 2 666  GLY 666  666  666  GLY GLY A . n 
B 2 667  GLY 667  667  667  GLY GLY A . n 
B 2 668  GLY 668  668  668  GLY GLY A . n 
B 2 669  LEU 669  669  669  LEU LEU A . n 
B 2 670  ILE 670  670  670  ILE ILE A . n 
B 2 671  ALA 671  671  671  ALA ALA A . n 
B 2 672  LEU 672  672  672  LEU LEU A . n 
B 2 673  ARG 673  673  673  ARG ARG A . n 
B 2 674  LEU 674  674  674  LEU LEU A . n 
B 2 675  PRO 675  675  675  PRO PRO A . n 
B 2 676  GLU 676  676  676  GLU GLU A . n 
B 2 677  THR 677  677  677  THR THR A . n 
B 2 678  ARG 678  678  678  ARG ARG A . n 
B 2 679  GLU 679  679  ?    ?   ?   A . n 
B 2 680  GLN 680  680  ?    ?   ?   A . n 
B 2 681  VAL 681  681  ?    ?   ?   A . n 
B 2 682  LEU 682  682  ?    ?   ?   A . n 
B 2 683  MET 683  683  ?    ?   ?   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 C NAG 1 A NAG 745 n 
C 3 FUC 2 C FUC 2 A FUC 746 n 
D 4 NAG 1 D NAG 1 A NAG 748 n 
D 4 NAG 2 D NAG 2 A NAG 761 n 
D 4 BMA 3 D BMA 3 A BMA 762 n 
D 4 MAN 4 D MAN 4 A MAN 766 n 
D 4 MAN 5 D MAN 5 A MAN 765 n 
D 4 FUC 6 D FUC 6 A FUC 749 n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 FUC ? ? FUC ? ? 'SUBJECT OF INVESTIGATION' ? 
2 BMA ? ? BMA ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MAN ? ? MAN ? ? 'SUBJECT OF INVESTIGATION' ? 
4 NAG ? ? NAG ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
_pdbx_nonpoly_scheme.asym_id         E 
_pdbx_nonpoly_scheme.entity_id       5 
_pdbx_nonpoly_scheme.mon_id          NAG 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     701 
_pdbx_nonpoly_scheme.auth_seq_num    756 
_pdbx_nonpoly_scheme.pdb_mon_id      NAG 
_pdbx_nonpoly_scheme.auth_mon_id     NAG 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 B LEU 647 ? CG  ? A LEU 664 CG  
2 1 Y 1 B LEU 647 ? CD1 ? A LEU 664 CD1 
3 1 Y 1 B LEU 647 ? CD2 ? A LEU 664 CD2 
4 1 Y 1 B ILE 831 ? CG1 ? A ILE 848 CG1 
5 1 Y 1 B ILE 831 ? CG2 ? A ILE 848 CG2 
6 1 Y 1 B ILE 831 ? CD1 ? A ILE 848 CD1 
7 1 N 1 D NAG 1   ? O1  ? D NAG 1   O1  
# 
_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                     9F2J 
_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                         9F2J 
_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                   9F2J 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9F2J 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.98 
_refine.ls_d_res_low                             ? 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_struct.entry_id                     9F2J 
_struct.title                        'Cryo-EM structure of SV2B-BoNT/A1 complex' 
_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        9F2J 
_struct_keywords.text            'transporter, botulinum neurotoxin, synaptic vesicle glycoprotein, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
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 BXA1_CLOBO P0DPI0 ? 1 
;PFVNKQFNYKDPVNGVDIAYIKIPNVGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTD
NEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADII
QFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNR
VFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEKY
LLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANF
NGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIITSKTKSLDKGYNKALNDLCIKVNNWDLFFSPSEDNFTNDLNKGEEI
TSDTNIEAAEENISLDLIQQYYLTFNFDNEPENISIENLSSDIIGQLELMPNIERFPNGKKYELDKYTMFHYLRAQEFEH
GKSRIALTNSVNEALLNPSRVYTFFSSDYVKKVNKATEAAMFLGWVEQLVYDFTDETSEVSTTDKIADITIIIPYIGPAL
NIGNMLYKDDFVGALIFSGAVILLEFIPEIAIPVLGTFALVSYIANKVLTVQTIDNALSKRNEKWDEVYKYIVTNWLAKV
NTQIDLIRKKMKEALENQAEATKAIINYQYNQYTEEEKNNINFNIDDLSSKLNESINKAMININKFLNQCSVSYLMNSMI
PYGVKRLEDFDASLKDALLKYIYDNRGTLIGQVDRLKDKVNNTLSTDIPFQLSKYVDNQRLLSTFTEYIKNIINTSILNL
RYESNHLIDLSRYASKINIGSKVNFDPIDKNQIQLFNLESSKIEVILKNAIVYNSMYENFSTSFWIRIPKYFNSISLNNE
YTIINCMENNSGWKVSLNYGEIIWTLQDTQEIKQRVVFKYSQMINISDYINRWIFVTITNNRLNNSKIYINGRLIDQKPI
SNLGNIHASNNIMFKLDGCRDTHRYIWIKYFNLFDKELNEKEIKDLYDNQSNSGILKDFWGDYLQYDKPYYMLNLYDPNK
YVDVNNVGIRGYMYLKGPRGSVMTTNIYLNSSLYRGTKFIIKKYASGNKDNIVRNNDRVYINVVVKNKEYRLATNASQAG
VEKILSALEIPDVGNLSQVVVMKSKNDQGITNKCKMNLQDNNGNDIGFIGFHQFNNIAKLVASNWYNRQIERSSRTLGCS
WEFIPVDDGWGERPL
;
2 
2 UNP SV2B_HUMAN Q7L1I2 ? 2 
;MDDYKYQDNYGGYAPSDGYYRGNESNPEEDAQSDVTEGHDEEDEIYEGEYQGIPHPDDVKAKQAKMAPSRMDSLRGQTDL
MAERLEDEEQLAHQYETIMDECGHGRFQWILFFVLGLALMADGVEVFVVSFALPSAEKDMCLSSSKKGMLGMIVYLGMMA
GAFILGGLADKLGRKRVLSMSLAVNASFASLSSFVQGYGAFLFCRLISGIGIGGALPIVFAYFSEFLSREKRGEHLSWLG
IFWMTGGLYASAMAWSIIPHYGWGFSMGTNYHFHSWRVFVIVCALPCTVSMVALKFMPESPRFLLEMGKHDEAWMILKQV
HDTNMRAKGTPEKVFTVSNIKTPKQMDEFIEIQSSTGTWYQRWLVRFKTIFKQVWDNALYCVMGPYRMNTLILAVVWFAM
AFSYYGLTVWFPDMIRYFQDEEYKSKMKVFFGEHVYGATINFTMENQIHQHGKLVNDKFTRMYFKHVLFEDTFFDECYFE
DVTSTDTYFKNCTIESTIFYNTDLYEHKFINCRFINSTFLEQKEGCHMDLEQDNDFLIYLVSFLGSLSVLPGNIISALLM
DRIGRLKMIGGSMLISAVCCFFLFFGNSESAMIGWQCLFCGTSIAAWNALDVITVELYPTNQRATAFGILNGLCKFGAIL
GNTIFASFVGITKVVPILLAAASLVGGGLIALRLPETREQVLM
;
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 9F2J B 19 ? 1313 ? P0DPI0 2 ? 1296 ? 2 1296 
2 2 9F2J A 1  ? 683  ? Q7L1I2 1 ? 683  ? 1 683  
# 
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 9F2J MET B 1    ? UNP P0DPI0 ?   ?    'initiating methionine' -16  1  
1 9F2J ARG B 2    ? UNP P0DPI0 ?   ?    'expression tag'        -15  2  
1 9F2J GLY B 3    ? UNP P0DPI0 ?   ?    'expression tag'        -14  3  
1 9F2J SER B 4    ? UNP P0DPI0 ?   ?    'expression tag'        -13  4  
1 9F2J HIS B 5    ? UNP P0DPI0 ?   ?    'expression tag'        -12  5  
1 9F2J HIS B 6    ? UNP P0DPI0 ?   ?    'expression tag'        -11  6  
1 9F2J HIS B 7    ? UNP P0DPI0 ?   ?    'expression tag'        -10  7  
1 9F2J HIS B 8    ? UNP P0DPI0 ?   ?    'expression tag'        -9   8  
1 9F2J HIS B 9    ? UNP P0DPI0 ?   ?    'expression tag'        -8   9  
1 9F2J HIS B 10   ? UNP P0DPI0 ?   ?    'expression tag'        -7   10 
1 9F2J GLY B 11   ? UNP P0DPI0 ?   ?    'expression tag'        -6   11 
1 9F2J SER B 12   ? UNP P0DPI0 ?   ?    'expression tag'        -5   12 
1 9F2J LEU B 13   ? UNP P0DPI0 ?   ?    'expression tag'        -4   13 
1 9F2J VAL B 14   ? UNP P0DPI0 ?   ?    'expression tag'        -3   14 
1 9F2J PRO B 15   ? UNP P0DPI0 ?   ?    'expression tag'        -2   15 
1 9F2J ARG B 16   ? UNP P0DPI0 ?   ?    'expression tag'        -1   16 
1 9F2J GLY B 17   ? UNP P0DPI0 ?   ?    'expression tag'        0    17 
1 9F2J SER B 18   ? UNP P0DPI0 ?   ?    'expression tag'        1    18 
1 9F2J ALA B 44   ? UNP P0DPI0 VAL 27   variant                 27   19 
1 9F2J GLN B 241  ? UNP P0DPI0 GLU 224  'engineered mutation'   224  20 
1 9F2J ALA B 380  ? UNP P0DPI0 ARG 363  'engineered mutation'   363  21 
1 9F2J PHE B 383  ? UNP P0DPI0 TYR 366  'engineered mutation'   366  22 
1 9F2J ALA B 1175 ? UNP P0DPI0 THR 1158 conflict                1158 23 
1 9F2J VAL B 1314 ? UNP P0DPI0 ?   ?    'expression tag'        1297 24 
1 9F2J PRO B 1315 ? UNP P0DPI0 ?   ?    'expression tag'        1298 25 
1 9F2J PRO B 1316 ? UNP P0DPI0 ?   ?    'expression tag'        1299 26 
1 9F2J THR B 1317 ? UNP P0DPI0 ?   ?    'expression tag'        1300 27 
1 9F2J PRO B 1318 ? UNP P0DPI0 ?   ?    'expression tag'        1301 28 
1 9F2J GLY B 1319 ? UNP P0DPI0 ?   ?    'expression tag'        1302 29 
1 9F2J SER B 1320 ? UNP P0DPI0 ?   ?    'expression tag'        1303 30 
1 9F2J ALA B 1321 ? UNP P0DPI0 ?   ?    'expression tag'        1304 31 
1 9F2J TRP B 1322 ? UNP P0DPI0 ?   ?    'expression tag'        1305 32 
1 9F2J SER B 1323 ? UNP P0DPI0 ?   ?    'expression tag'        1306 33 
1 9F2J HIS B 1324 ? UNP P0DPI0 ?   ?    'expression tag'        1307 34 
1 9F2J PRO B 1325 ? UNP P0DPI0 ?   ?    'expression tag'        1308 35 
1 9F2J GLN B 1326 ? UNP P0DPI0 ?   ?    'expression tag'        1309 36 
1 9F2J PHE B 1327 ? UNP P0DPI0 ?   ?    'expression tag'        1310 37 
1 9F2J GLU B 1328 ? UNP P0DPI0 ?   ?    'expression tag'        1311 38 
1 9F2J LYS B 1329 ? UNP P0DPI0 ?   ?    'expression tag'        1312 39 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_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 
# 
_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   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 97   ? THR A 118  ? THR B 80   THR B 101  1 ? 22 
HELX_P HELX_P2  AA2 THR A 118  ? GLY A 131  ? THR B 101  GLY B 114  1 ? 14 
HELX_P HELX_P3  AA3 ASP A 233  ? TYR A 250  ? ASP B 216  TYR B 233  1 ? 18 
HELX_P HELX_P4  AA4 SER A 276  ? GLY A 284  ? SER B 259  GLY B 267  1 ? 9  
HELX_P HELX_P5  AA5 HIS A 286  ? ILE A 291  ? HIS B 269  ILE B 274  5 ? 6  
HELX_P HELX_P6  AA6 ASP A 292  ? ALA A 317  ? ASP B 275  ALA B 300  1 ? 26 
HELX_P HELX_P7  AA7 SER A 326  ? LEU A 339  ? SER B 309  LEU B 322  1 ? 14 
HELX_P HELX_P8  AA8 ASP A 351  ? GLU A 364  ? ASP B 334  GLU B 347  1 ? 14 
HELX_P HELX_P9  AA9 THR A 367  ? LYS A 376  ? THR B 350  LYS B 359  1 ? 10 
HELX_P HELX_P10 AB1 ASN A 426  ? MET A 428  ? ASN B 409  MET B 411  5 ? 3  
HELX_P HELX_P11 AB2 SER A 484  ? PHE A 488  ? SER B 467  PHE B 471  5 ? 5  
HELX_P HELX_P12 AB3 LEU A 513  ? PHE A 523  ? LEU B 496  PHE B 506  1 ? 11 
HELX_P HELX_P13 AB4 THR A 566  ? GLN A 574  ? THR B 549  GLN B 557  1 ? 9  
HELX_P HELX_P14 AB5 SER A 588  ? LEU A 593  ? SER B 571  LEU B 576  1 ? 6  
HELX_P HELX_P15 AB6 SER A 604  ? ASN A 612  ? SER B 587  ASN B 595  1 ? 9  
HELX_P HELX_P16 AB7 MET A 619  ? SER A 636  ? MET B 602  SER B 619  1 ? 18 
HELX_P HELX_P17 AB8 TYR A 653  ? ASN A 659  ? TYR B 636  ASN B 642  1 ? 7  
HELX_P HELX_P18 AB9 ILE A 660  ? MET A 663  ? ILE B 643  MET B 646  5 ? 4  
HELX_P HELX_P19 AC1 TYR A 665  ? GLY A 677  ? TYR B 648  GLY B 660  1 ? 13 
HELX_P HELX_P20 AC2 VAL A 706  ? VAL A 738  ? VAL B 689  VAL B 721  1 ? 33 
HELX_P HELX_P21 AC3 VAL A 738  ? GLN A 770  ? VAL B 721  GLN B 753  1 ? 33 
HELX_P HELX_P22 AC4 THR A 772  ? ILE A 779  ? THR B 755  ILE B 762  1 ? 8  
HELX_P HELX_P23 AC5 ASN A 782  ? MET A 817  ? ASN B 765  MET B 800  1 ? 36 
HELX_P HELX_P24 AC6 MET A 817  ? TYR A 841  ? MET B 800  TYR B 824  1 ? 25 
HELX_P HELX_P25 AC7 GLN A 850  ? THR A 864  ? GLN B 833  THR B 847  1 ? 15 
HELX_P HELX_P26 AC8 GLN A 869  ? TYR A 873  ? GLN B 852  TYR B 856  5 ? 5  
HELX_P HELX_P27 AC9 ASN A 876  ? ASN A 889  ? ASN B 859  ASN B 872  1 ? 14 
HELX_P HELX_P28 AD1 ILE A 890  ? SER A 894  ? ILE B 873  SER B 877  5 ? 5  
HELX_P HELX_P29 AD2 ASN A 971  ? LEU A 975  ? ASN B 954  LEU B 958  5 ? 5  
HELX_P HELX_P30 AD3 ASN A 1097 ? SER A 1109 ? ASN B 1080 SER B 1092 1 ? 13 
HELX_P HELX_P31 AD4 TRP A 1283 ? GLN A 1287 ? TRP B 1266 GLN B 1270 5 ? 5  
HELX_P HELX_P32 AD5 HIS B 93   ? GLY B 103  ? HIS A 93   GLY A 103  1 ? 11 
HELX_P HELX_P33 AD6 GLY B 105  ? PHE B 131  ? GLY A 105  PHE A 131  1 ? 27 
HELX_P HELX_P34 AD7 ALA B 132  ? GLU B 137  ? ALA A 132  GLU A 137  1 ? 6  
HELX_P HELX_P35 AD8 MET B 149  ? GLY B 151  ? MET A 149  GLY A 151  5 ? 3  
HELX_P HELX_P36 AD9 MET B 152  ? LEU B 168  ? MET A 152  LEU A 168  1 ? 17 
HELX_P HELX_P37 AE1 LEU B 168  ? GLY B 173  ? LEU A 168  GLY A 173  1 ? 6  
HELX_P HELX_P38 AE2 ARG B 174  ? PHE B 194  ? ARG A 174  PHE A 194  1 ? 21 
HELX_P HELX_P39 AE3 GLY B 197  ? GLY B 213  ? GLY A 197  GLY A 213  1 ? 17 
HELX_P HELX_P40 AE4 ALA B 215  ? GLU B 225  ? ALA A 215  GLU A 225  1 ? 11 
HELX_P HELX_P41 AE5 ARG B 229  ? LYS B 231  ? ARG A 229  LYS A 231  5 ? 3  
HELX_P HELX_P42 AE6 ARG B 232  ? ILE B 258  ? ARG A 232  ILE A 258  1 ? 27 
HELX_P HELX_P43 AE7 HIS B 274  ? CYS B 283  ? HIS A 274  CYS A 283  1 ? 10 
HELX_P HELX_P44 AE8 ALA B 284  ? LEU B 294  ? ALA A 284  LEU A 294  1 ? 11 
HELX_P HELX_P45 AE9 SER B 300  ? GLY B 308  ? SER A 300  GLY A 308  1 ? 9  
HELX_P HELX_P46 AF1 LYS B 309  ? GLY B 329  ? LYS A 309  GLY A 329  1 ? 21 
HELX_P HELX_P47 AF2 PHE B 371  ? CYS B 381  ? PHE A 371  CYS A 381  1 ? 11 
HELX_P HELX_P48 AF3 ARG B 387  ? LYS B 426  ? ARG A 387  LYS A 426  1 ? 40 
HELX_P HELX_P49 AF4 TYR B 505  ? HIS B 507  ? TYR A 505  HIS A 507  5 ? 3  
HELX_P HELX_P50 AF5 ASP B 529  ? ASP B 533  ? ASP A 529  ASP A 533  5 ? 5  
HELX_P HELX_P51 AF6 ASP B 535  ? SER B 548  ? ASP A 535  SER A 548  1 ? 14 
HELX_P HELX_P52 AF7 SER B 548  ? LEU B 558  ? SER A 548  LEU A 558  1 ? 11 
HELX_P HELX_P53 AF8 LEU B 566  ? PHE B 581  ? LEU A 566  PHE A 581  1 ? 16 
HELX_P HELX_P54 AF9 PHE B 582  ? GLY B 586  ? PHE A 582  GLY A 586  5 ? 5  
HELX_P HELX_P55 AG1 SER B 588  ? SER B 603  ? SER A 588  SER A 603  1 ? 16 
HELX_P HELX_P56 AG2 ILE B 604  ? LEU B 617  ? ILE A 604  LEU A 617  1 ? 14 
HELX_P HELX_P57 AG3 GLN B 622  ? PHE B 648  ? GLN A 622  PHE A 648  1 ? 27 
HELX_P HELX_P58 AG4 LYS B 653  ? ALA B 671  ? LYS A 653  ALA A 671  1 ? 19 
# 
_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 447 SG  ? ? ? 1_555 A CYS 471 SG ? ? B CYS 430 B CYS 454 1_555 ? ? ? ? ? ? ? 2.036 ? ?               
disulf2 disulf ?    ? B CYS 141 SG  ? ? ? 1_555 B CYS 526 SG ? ? A CYS 141 A CYS 526 1_555 ? ? ? ? ? ? ? 2.027 ? ?               
covale1 covale one  ? B ASN 441 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 441 A NAG 701 1_555 ? ? ? ? ? ? ? 1.485 ? N-Glycosylation 
covale2 covale one  ? B ASN 491 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 491 C NAG 1   1_555 ? ? ? ? ? ? ? 1.529 ? N-Glycosylation 
covale3 covale both ? C NAG .   O6  ? ? ? 1_555 C FUC .   C1 ? ? C NAG 1   C FUC 2   1_555 ? ? ? ? ? ? ? 1.402 ? ?               
covale4 covale both ? D NAG .   O4  ? ? ? 1_555 D NAG .   C1 ? ? D NAG 1   D NAG 2   1_555 ? ? ? ? ? ? ? 1.456 ? ?               
covale5 covale both ? D NAG .   O6  ? ? ? 1_555 D FUC .   C1 ? ? D NAG 1   D FUC 6   1_555 ? ? ? ? ? ? ? 1.433 ? ?               
covale6 covale both ? D NAG .   O4  ? ? ? 1_555 D BMA .   C1 ? ? D NAG 2   D BMA 3   1_555 ? ? ? ? ? ? ? 1.404 ? ?               
covale7 covale both ? D BMA .   O3  ? ? ? 1_555 D MAN .   C1 ? ? D BMA 3   D MAN 4   1_555 ? ? ? ? ? ? ? 1.399 ? ?               
covale8 covale both ? D BMA .   O6  ? ? ? 1_555 D MAN .   C1 ? ? D BMA 3   D MAN 5   1_555 ? ? ? ? ? ? ? 1.400 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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 B 491 ? NAG C 1   ? 1_555 ASN A 491 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG E .   ? ASN B 441 ? NAG A 701 ? 1_555 ASN A 441 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 CYS A 447 ? CYS A 471 ? CYS B 430 ? 1_555 CYS B 454 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
4 CYS B 141 ? CYS B 526 ? CYS A 141 ? 1_555 CYS A 526 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLY 
_struct_mon_prot_cis.label_seq_id           1155 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLY 
_struct_mon_prot_cis.auth_seq_id            1138 
_struct_mon_prot_cis.auth_asym_id           B 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    1156 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     1139 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    B 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -3.43 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
AA8 ? 7 ? 
AA9 ? 7 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
AB3 ? 7 ? 
AB4 ? 4 ? 
AB5 ? 6 ? 
AB6 ? 4 ? 
AB7 ? 5 ? 
AB8 ? 2 ? 
# 
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 
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA5 1 2 ? parallel      
AA6 1 2 ? parallel      
AA7 1 2 ? anti-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 
AA9 6 7 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? parallel      
AB3 4 5 ? parallel      
AB3 5 6 ? parallel      
AB3 6 7 ? parallel      
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB5 4 5 ? anti-parallel 
AB5 5 6 ? anti-parallel 
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB6 3 4 ? parallel      
AB7 1 2 ? parallel      
AB7 2 3 ? parallel      
AB7 3 4 ? parallel      
AB7 4 5 ? parallel      
AB8 1 2 ? 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 161  ? GLU A 165  ? TYR B 144  GLU B 148  
AA1 2 CYS A 151  ? ILE A 155  ? CYS B 134  ILE B 138  
AA1 3 ILE A 36   ? LYS A 40   ? ILE B 19   LYS B 23   
AA1 4 VAL A 50   ? HIS A 56   ? VAL B 33   HIS B 39   
AA1 5 ILE A 59   ? ARG A 65   ? ILE B 42   ARG B 48   
AA1 6 LEU A 168  ? GLY A 172  ? LEU B 151  GLY B 155  
AA1 7 GLN A 201  ? ARG A 204  ? GLN B 184  ARG B 187  
AA1 8 GLU A 181  ? SER A 184  ? GLU B 164  SER B 167  
AA2 1 GLU A 143  ? LEU A 144  ? GLU B 126  LEU B 127  
AA2 2 SER A 319  ? ILE A 320  ? SER B 302  ILE B 303  
AA3 1 PHE A 230  ? ALA A 231  ? PHE B 213  ALA B 214  
AA3 2 PHE A 209  ? PHE A 213  ? PHE B 192  PHE B 196  
AA3 3 ALA A 389  ? ILE A 393  ? ALA B 372  ILE B 376  
AA3 4 PHE A 430  ? LEU A 433  ? PHE B 413  LEU B 416  
AA4 1 ILE A 472  ? ASN A 475  ? ILE B 455  ASN B 458  
AA4 2 TYR A 443  ? VAL A 448  ? TYR B 426  VAL B 431  
AA4 3 LYS A 558  ? LEU A 562  ? LYS B 541  LEU B 545  
AA5 1 GLU A 496  ? ILE A 498  ? GLU B 479  ILE B 481  
AA5 2 PHE A 696  ? LEU A 698  ? PHE B 679  LEU B 681  
AA6 1 ALA A 584  ? THR A 586  ? ALA B 567  THR B 569  
AA6 2 ARG A 598  ? TYR A 600  ? ARG B 581  TYR B 583  
AA7 1 LEU A 898  ? TYR A 900  ? LEU B 881  TYR B 883  
AA7 2 LEU A 905  ? ASP A 907  ? LEU B 888  ASP B 890  
AA8 1 ALA A 912  ? ILE A 917  ? ALA B 895  ILE B 900  
AA8 2 ILE A 941  ? LEU A 945  ? ILE B 924  LEU B 928  
AA8 3 ASN A 1069 ? ASP A 1075 ? ASN B 1052 ASP B 1058 
AA8 4 TYR A 979  ? ASN A 983  ? TYR B 962  ASN B 966  
AA8 5 GLY A 990  ? ASN A 996  ? GLY B 973  ASN B 979  
AA8 6 GLU A 999  ? GLN A 1005 ? GLU B 982  GLN B 988  
AA8 7 LYS A 1011 ? LYS A 1017 ? LYS B 994  LYS B 1000 
AA9 1 VAL A 921  ? PHE A 923  ? VAL B 904  PHE B 906  
AA9 2 ILE A 931  ? PHE A 934  ? ILE B 914  PHE B 917  
AA9 3 TYR A 1083 ? PHE A 1092 ? TYR B 1066 PHE B 1075 
AA9 4 ASN A 957  ? ARG A 965  ? ASN B 940  ARG B 948  
AA9 5 ILE A 1032 ? ASN A 1039 ? ILE B 1015 ASN B 1022 
AA9 6 SER A 1044 ? ILE A 1048 ? SER B 1027 ILE B 1031 
AA9 7 ARG A 1051 ? LYS A 1056 ? ARG B 1034 LYS B 1039 
AB1 1 TYR A 1129 ? ASN A 1132 ? TYR B 1112 ASN B 1115 
AB1 2 TRP A 1299 ? ILE A 1302 ? TRP B 1282 ILE B 1285 
AB2 1 TYR A 1139 ? ASN A 1143 ? TYR B 1122 ASN B 1126 
AB2 2 TYR A 1150 ? LYS A 1154 ? TYR B 1133 LYS B 1137 
AB3 1 TYR A 1166 ? ASN A 1168 ? TYR B 1149 ASN B 1151 
AB3 2 SER A 1159 ? THR A 1162 ? SER B 1142 THR B 1145 
AB3 3 SER B 517  ? PHE B 519  ? SER A 517  PHE A 519  
AB3 4 ILE B 498  ? TYR B 500  ? ILE A 498  TYR A 500  
AB3 5 TYR B 478  ? GLU B 480  ? TYR A 478  GLU A 480  
AB3 6 LYS B 458  ? THR B 460  ? LYS A 458  THR A 460  
AB3 7 THR B 439  ? ILE B 440  ? THR A 439  ILE A 440  
AB4 1 PHE A 1177 ? LYS A 1181 ? PHE B 1160 LYS B 1164 
AB4 2 ASP A 1195 ? VAL A 1203 ? ASP B 1178 VAL B 1186 
AB4 3 LYS A 1206 ? ALA A 1211 ? LYS B 1189 ALA B 1194 
AB4 4 SER A 1224 ? GLU A 1227 ? SER B 1207 GLU B 1210 
AB5 1 PHE A 1177 ? LYS A 1181 ? PHE B 1160 LYS B 1164 
AB5 2 ASP A 1195 ? VAL A 1203 ? ASP B 1178 VAL B 1186 
AB5 3 VAL A 1238 ? LYS A 1241 ? VAL B 1221 LYS B 1224 
AB5 4 LYS A 1253 ? GLN A 1257 ? LYS B 1236 GLN B 1240 
AB5 5 ASP A 1263 ? HIS A 1270 ? ASP B 1246 HIS B 1253 
AB5 6 LYS A 1277 ? SER A 1281 ? LYS B 1260 SER B 1264 
AB6 1 LYS B 428  ? PHE B 431  ? LYS A 428  PHE A 431  
AB6 2 MET B 444  ? GLN B 450  ? MET A 444  GLN A 450  
AB6 3 TYR B 463  ? GLU B 470  ? TYR A 463  GLU A 470  
AB6 4 THR B 483  ? THR B 485  ? THR A 483  THR A 485  
AB7 1 LYS B 428  ? PHE B 431  ? LYS A 428  PHE A 431  
AB7 2 MET B 444  ? GLN B 450  ? MET A 444  GLN A 450  
AB7 3 TYR B 463  ? GLU B 470  ? TYR A 463  GLU A 470  
AB7 4 TYR B 488  ? LYS B 490  ? TYR A 488  LYS A 490  
AB7 5 PHE B 509  ? ILE B 510  ? PHE A 509  ILE A 510  
AB8 1 THR B 493  ? GLU B 495  ? THR A 493  GLU A 495  
AB8 2 ARG B 513  ? ILE B 515  ? ARG A 513  ILE A 515  
# 
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 GLU A 164  ? O GLU B 147  N ILE A 152  ? N ILE B 135  
AA1 2 3 O ILE A 155  ? O ILE B 138  N TYR A 38   ? N TYR B 21   
AA1 3 4 N ALA A 37   ? N ALA B 20   O ALA A 52   ? O ALA B 35   
AA1 4 5 N PHE A 53   ? N PHE B 36   O VAL A 61   ? O VAL B 44   
AA1 5 6 N ILE A 62   ? N ILE B 45   O ILE A 170  ? O ILE B 153  
AA1 6 7 N VAL A 169  ? N VAL B 152  O ILE A 203  ? O ILE B 186  
AA1 7 8 O TYR A 202  ? O TYR B 185  N LYS A 183  ? N LYS B 166  
AA2 1 2 N LEU A 144  ? N LEU B 127  O SER A 319  ? O SER B 302  
AA3 1 2 O PHE A 230  ? O PHE B 213  N PHE A 213  ? N PHE B 196  
AA3 2 3 N THR A 210  ? N THR B 193  O PHE A 391  ? O PHE B 374  
AA3 3 4 N LYS A 392  ? N LYS B 375  O THR A 431  ? O THR B 414  
AA4 1 2 O VAL A 474  ? O VAL B 457  N LYS A 444  ? N LYS B 427  
AA4 2 3 N LEU A 445  ? N LEU B 428  O TYR A 560  ? O TYR B 543  
AA5 1 2 N ILE A 498  ? N ILE B 481  O ALA A 697  ? O ALA B 680  
AA6 1 2 N ALA A 584  ? N ALA B 567  O VAL A 599  ? O VAL B 582  
AA7 1 2 N ARG A 899  ? N ARG B 882  O ILE A 906  ? O ILE B 889  
AA8 1 2 N ASN A 916  ? N ASN B 899  O GLU A 942  ? O GLU B 925  
AA8 2 3 N ILE A 941  ? N ILE B 924  O PHE A 1072 ? O PHE B 1055 
AA8 3 4 O MET A 1071 ? O MET B 1054 N ASN A 983  ? N ASN B 966  
AA8 4 5 N ILE A 981  ? N ILE B 964  O VAL A 993  ? O VAL B 976  
AA8 5 6 N LYS A 992  ? N LYS B 975  O THR A 1003 ? O THR B 986  
AA8 6 7 N TRP A 1002 ? N TRP B 985  O VAL A 1014 ? O VAL B 997  
AA9 1 2 N ASN A 922  ? N ASN B 905  O GLN A 932  ? O GLN B 915  
AA9 2 3 N ILE A 931  ? N ILE B 914  O ILE A 1086 ? O ILE B 1069 
AA9 3 4 O LYS A 1087 ? O LYS B 1070 N TRP A 963  ? N TRP B 946  
AA9 4 5 N PHE A 958  ? N PHE B 941  O ASN A 1038 ? O ASN B 1021 
AA9 5 6 N THR A 1037 ? N THR B 1020 O LYS A 1045 ? O LYS B 1028 
AA9 6 7 N ILE A 1046 ? N ILE B 1029 O ASP A 1054 ? O ASP B 1037 
AB1 1 2 N TYR A 1129 ? N TYR B 1112 O ILE A 1302 ? O ILE B 1285 
AB2 1 2 N ASP A 1141 ? N ASP B 1124 O TYR A 1152 ? O TYR B 1135 
AB3 1 2 O TYR A 1166 ? O TYR B 1149 N THR A 1162 ? N THR B 1145 
AB3 2 3 N SER A 1159 ? N SER B 1142 O PHE B 519  ? O PHE A 519  
AB3 3 4 O THR B 518  ? O THR A 518  N PHE B 499  ? N PHE A 499  
AB3 4 5 O ILE B 498  ? O ILE A 498  N PHE B 479  ? N PHE A 479  
AB3 5 6 O GLU B 480  ? O GLU A 480  N PHE B 459  ? N PHE A 459  
AB3 6 7 O LYS B 458  ? O LYS A 458  N ILE B 440  ? N ILE A 440  
AB4 1 2 N LYS A 1180 ? N LYS B 1163 O TYR A 1198 ? O TYR B 1181 
AB4 2 3 N VAL A 1203 ? N VAL B 1186 O LYS A 1206 ? O LYS B 1189 
AB4 3 4 N ARG A 1209 ? N ARG B 1192 O LEU A 1226 ? O LEU B 1209 
AB5 1 2 N LYS A 1180 ? N LYS B 1163 O TYR A 1198 ? O TYR B 1181 
AB5 2 3 N VAL A 1197 ? N VAL B 1180 O VAL A 1238 ? O VAL B 1221 
AB5 3 4 N VAL A 1239 ? N VAL B 1222 O ASN A 1255 ? O ASN B 1238 
AB5 4 5 N MET A 1254 ? N MET B 1237 O ILE A 1267 ? O ILE B 1250 
AB5 5 6 N GLY A 1268 ? N GLY B 1251 O VAL A 1279 ? O VAL B 1262 
AB6 1 2 N LYS B 428  ? N LYS A 428  O ILE B 448  ? O ILE A 448  
AB6 2 3 N ASN B 446  ? N ASN A 446  O LYS B 465  ? O LYS A 465  
AB6 3 4 N PHE B 464  ? N PHE A 464  O THR B 483  ? O THR A 483  
AB7 1 2 N LYS B 428  ? N LYS A 428  O ILE B 448  ? O ILE A 448  
AB7 2 3 N ASN B 446  ? N ASN A 446  O LYS B 465  ? O LYS A 465  
AB7 3 4 N PHE B 469  ? N PHE A 469  O LYS B 490  ? O LYS A 490  
AB7 4 5 N PHE B 489  ? N PHE A 489  O ILE B 510  ? O ILE A 510  
AB8 1 2 N ILE B 494  ? N ILE A 494  O ARG B 513  ? O ARG A 513  
# 
_pdbx_entry_details.entry_id                   9F2J 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 ND2 A ASN 516 ? ? C1 D NAG 1   ? ? 1.74 
2 1 OH  A TYR 222 ? ? O  A PRO 298 ? ? 2.04 
3 1 OD1 B ASP 461 ? ? NZ B LYS 731 ? ? 2.17 
4 1 OG  A SER 181 ? ? O  A GLY 211 ? ? 2.18 
# 
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 LYS B 6    ? ? 59.38   71.39   
2  1 ASN B 9    ? ? 51.24   -140.52 
3  1 TYR B 10   ? ? -131.74 -39.52  
4  1 PRO B 13   ? ? -65.28  -175.32 
5  1 VAL B 14   ? ? -99.63  31.31   
6  1 SER B 157  ? ? -77.58  -161.50 
7  1 THR B 327  ? ? 59.28   10.37   
8  1 THR B 482  ? ? -124.45 -168.50 
9  1 ASP B 509  ? ? 68.66   -1.06   
10 1 SER B 580  ? ? -95.11  35.81   
11 1 TYR B 1133 ? ? -165.33 -168.71 
12 1 ILE B 1148 ? ? -122.81 -60.17  
13 1 TYR B 1165 ? ? -134.55 -50.42  
14 1 ALA B 1166 ? ? -140.58 20.45   
15 1 LYS B 1234 ? ? 49.42   -138.71 
16 1 ASN B 1256 ? ? 50.89   -160.21 
17 1 ARG B 1269 ? ? -105.77 40.98   
18 1 LYS A 146  ? ? -92.60  -148.40 
19 1 LYS A 231  ? ? -90.63  52.52   
20 1 HIS A 272  ? ? -77.58  -168.16 
21 1 HIS A 274  ? ? -79.42  26.88   
22 1 VAL A 382  ? ? -122.89 -62.32  
23 1 MET A 383  ? ? -97.01  54.11   
24 1 LYS A 458  ? ? -160.35 116.09  
25 1 GLU A 476  ? ? 47.63   29.41   
26 1 ASN A 491  ? ? 47.75   27.00   
27 1 LEU A 520  ? ? -94.28  -149.66 
28 1 ASP A 535  ? ? -82.66  30.16   
29 1 LEU A 558  ? ? -89.45  45.27   
30 1 LEU A 559  ? ? -141.10 -16.59  
# 
loop_
_pdbx_validate_chiral.id 
_pdbx_validate_chiral.PDB_model_num 
_pdbx_validate_chiral.auth_atom_id 
_pdbx_validate_chiral.label_alt_id 
_pdbx_validate_chiral.auth_asym_id 
_pdbx_validate_chiral.auth_comp_id 
_pdbx_validate_chiral.auth_seq_id 
_pdbx_validate_chiral.PDB_ins_code 
_pdbx_validate_chiral.details 
_pdbx_validate_chiral.omega 
1 1 C1 ? C FUC 2 ? 'WRONG HAND' . 
2 1 C1 ? D BMA 3 ? PLANAR       . 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     1179 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.105 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9F2J 
_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      'RIGID BODY FIT' 
# 
loop_
_em_3d_fitting_list.id 
_em_3d_fitting_list.3d_fitting_id 
_em_3d_fitting_list.pdb_entry_id 
_em_3d_fitting_list.pdb_chain_id 
_em_3d_fitting_list.pdb_chain_residue_range 
_em_3d_fitting_list.details 
_em_3d_fitting_list.chain_id 
_em_3d_fitting_list.chain_residue_range 
_em_3d_fitting_list.source_name 
_em_3d_fitting_list.type 
_em_3d_fitting_list.accession_code 
_em_3d_fitting_list.initial_refinement_model_id 
1 1 9F1R ? ? ? ? ? PDB 'experimental model' 9F1R 1 
2 1 9F2B ? ? ? ? ? PDB 'experimental model' 9F2B 2 
# 
_em_3d_reconstruction.entry_id                    9F2J 
_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                  3.98 
_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               149718 
_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            8.0 
# 
_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                 'Cryo-EM structure of SV2B-BoNT/A1 complex' 
_em_entity_assembly.details              'Cryo-EM structure of SV2B-BoNT/A1 complex' 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2' 
# 
_em_imaging.entry_id                        9F2J 
_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             600 
_em_imaging.nominal_defocus_max             2400 
_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              9F2J 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277.15 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9F2J 
_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 -16  ? A MET 1    
2   1 Y 1 B ARG -15  ? A ARG 2    
3   1 Y 1 B GLY -14  ? A GLY 3    
4   1 Y 1 B SER -13  ? A SER 4    
5   1 Y 1 B HIS -12  ? A HIS 5    
6   1 Y 1 B HIS -11  ? A HIS 6    
7   1 Y 1 B HIS -10  ? A HIS 7    
8   1 Y 1 B HIS -9   ? A HIS 8    
9   1 Y 1 B HIS -8   ? A HIS 9    
10  1 Y 1 B HIS -7   ? A HIS 10   
11  1 Y 1 B GLY -6   ? A GLY 11   
12  1 Y 1 B SER -5   ? A SER 12   
13  1 Y 1 B LEU -4   ? A LEU 13   
14  1 Y 1 B VAL -3   ? A VAL 14   
15  1 Y 1 B PRO -2   ? A PRO 15   
16  1 Y 1 B ARG -1   ? A ARG 16   
17  1 Y 1 B GLY 0    ? A GLY 17   
18  1 Y 1 B GLY 433  ? A GLY 450  
19  1 Y 1 B ILE 434  ? A ILE 451  
20  1 Y 1 B ILE 435  ? A ILE 452  
21  1 Y 1 B THR 436  ? A THR 453  
22  1 Y 1 B SER 437  ? A SER 454  
23  1 Y 1 B LYS 438  ? A LYS 455  
24  1 Y 1 B THR 439  ? A THR 456  
25  1 Y 1 B LYS 440  ? A LYS 457  
26  1 Y 1 B SER 441  ? A SER 458  
27  1 Y 1 B LEU 442  ? A LEU 459  
28  1 Y 1 B ASP 443  ? A ASP 460  
29  1 Y 1 B LYS 444  ? A LYS 461  
30  1 Y 1 B GLY 445  ? A GLY 462  
31  1 Y 1 B TYR 446  ? A TYR 463  
32  1 Y 1 B ASN 447  ? A ASN 464  
33  1 Y 1 B LYS 448  ? A LYS 465  
34  1 Y 1 B ALA 449  ? A ALA 466  
35  1 Y 1 B LEU 450  ? A LEU 467  
36  1 Y 1 B ASN 451  ? A ASN 468  
37  1 Y 1 B ILE 487  ? A ILE 504  
38  1 Y 1 B GLU 488  ? A GLU 505  
39  1 Y 1 B ALA 489  ? A ALA 506  
40  1 Y 1 B ALA 490  ? A ALA 507  
41  1 Y 1 B GLU 491  ? A GLU 508  
42  1 Y 1 B GLU 492  ? A GLU 509  
43  1 Y 1 B ASN 493  ? A ASN 510  
44  1 Y 1 B ILE 494  ? A ILE 511  
45  1 Y 1 B ASP 825  ? A ASP 842  
46  1 Y 1 B ASN 826  ? A ASN 843  
47  1 Y 1 B ARG 827  ? A ARG 844  
48  1 Y 1 B GLY 828  ? A GLY 845  
49  1 Y 1 B THR 829  ? A THR 846  
50  1 Y 1 B LEU 830  ? A LEU 847  
51  1 Y 1 B ASP 1228 ? A ASP 1245 
52  1 Y 1 B GLN 1229 ? A GLN 1246 
53  1 Y 1 B GLY 1230 ? A GLY 1247 
54  1 Y 1 B ILE 1271 ? A ILE 1288 
55  1 Y 1 B GLU 1272 ? A GLU 1289 
56  1 Y 1 B ARG 1273 ? A ARG 1290 
57  1 Y 1 B SER 1274 ? A SER 1291 
58  1 Y 1 B SER 1275 ? A SER 1292 
59  1 Y 1 B ARG 1276 ? A ARG 1293 
60  1 Y 1 B THR 1277 ? A THR 1294 
61  1 Y 1 B VAL 1297 ? A VAL 1314 
62  1 Y 1 B PRO 1298 ? A PRO 1315 
63  1 Y 1 B PRO 1299 ? A PRO 1316 
64  1 Y 1 B THR 1300 ? A THR 1317 
65  1 Y 1 B PRO 1301 ? A PRO 1318 
66  1 Y 1 B GLY 1302 ? A GLY 1319 
67  1 Y 1 B SER 1303 ? A SER 1320 
68  1 Y 1 B ALA 1304 ? A ALA 1321 
69  1 Y 1 B TRP 1305 ? A TRP 1322 
70  1 Y 1 B SER 1306 ? A SER 1323 
71  1 Y 1 B HIS 1307 ? A HIS 1324 
72  1 Y 1 B PRO 1308 ? A PRO 1325 
73  1 Y 1 B GLN 1309 ? A GLN 1326 
74  1 Y 1 B PHE 1310 ? A PHE 1327 
75  1 Y 1 B GLU 1311 ? A GLU 1328 
76  1 Y 1 B LYS 1312 ? A LYS 1329 
77  1 Y 1 A MET 1    ? B MET 1    
78  1 Y 1 A ASP 2    ? B ASP 2    
79  1 Y 1 A ASP 3    ? B ASP 3    
80  1 Y 1 A TYR 4    ? B TYR 4    
81  1 Y 1 A LYS 5    ? B LYS 5    
82  1 Y 1 A TYR 6    ? B TYR 6    
83  1 Y 1 A GLN 7    ? B GLN 7    
84  1 Y 1 A ASP 8    ? B ASP 8    
85  1 Y 1 A ASN 9    ? B ASN 9    
86  1 Y 1 A TYR 10   ? B TYR 10   
87  1 Y 1 A GLY 11   ? B GLY 11   
88  1 Y 1 A GLY 12   ? B GLY 12   
89  1 Y 1 A TYR 13   ? B TYR 13   
90  1 Y 1 A ALA 14   ? B ALA 14   
91  1 Y 1 A PRO 15   ? B PRO 15   
92  1 Y 1 A SER 16   ? B SER 16   
93  1 Y 1 A ASP 17   ? B ASP 17   
94  1 Y 1 A GLY 18   ? B GLY 18   
95  1 Y 1 A TYR 19   ? B TYR 19   
96  1 Y 1 A TYR 20   ? B TYR 20   
97  1 Y 1 A ARG 21   ? B ARG 21   
98  1 Y 1 A GLY 22   ? B GLY 22   
99  1 Y 1 A ASN 23   ? B ASN 23   
100 1 Y 1 A GLU 24   ? B GLU 24   
101 1 Y 1 A SER 25   ? B SER 25   
102 1 Y 1 A ASN 26   ? B ASN 26   
103 1 Y 1 A PRO 27   ? B PRO 27   
104 1 Y 1 A GLU 28   ? B GLU 28   
105 1 Y 1 A GLU 29   ? B GLU 29   
106 1 Y 1 A ASP 30   ? B ASP 30   
107 1 Y 1 A ALA 31   ? B ALA 31   
108 1 Y 1 A GLN 32   ? B GLN 32   
109 1 Y 1 A SER 33   ? B SER 33   
110 1 Y 1 A ASP 34   ? B ASP 34   
111 1 Y 1 A VAL 35   ? B VAL 35   
112 1 Y 1 A THR 36   ? B THR 36   
113 1 Y 1 A GLU 37   ? B GLU 37   
114 1 Y 1 A GLY 38   ? B GLY 38   
115 1 Y 1 A HIS 39   ? B HIS 39   
116 1 Y 1 A ASP 40   ? B ASP 40   
117 1 Y 1 A GLU 41   ? B GLU 41   
118 1 Y 1 A GLU 42   ? B GLU 42   
119 1 Y 1 A ASP 43   ? B ASP 43   
120 1 Y 1 A GLU 44   ? B GLU 44   
121 1 Y 1 A ILE 45   ? B ILE 45   
122 1 Y 1 A TYR 46   ? B TYR 46   
123 1 Y 1 A GLU 47   ? B GLU 47   
124 1 Y 1 A GLY 48   ? B GLY 48   
125 1 Y 1 A GLU 49   ? B GLU 49   
126 1 Y 1 A TYR 50   ? B TYR 50   
127 1 Y 1 A GLN 51   ? B GLN 51   
128 1 Y 1 A GLY 52   ? B GLY 52   
129 1 Y 1 A ILE 53   ? B ILE 53   
130 1 Y 1 A PRO 54   ? B PRO 54   
131 1 Y 1 A HIS 55   ? B HIS 55   
132 1 Y 1 A PRO 56   ? B PRO 56   
133 1 Y 1 A ASP 57   ? B ASP 57   
134 1 Y 1 A ASP 58   ? B ASP 58   
135 1 Y 1 A VAL 59   ? B VAL 59   
136 1 Y 1 A LYS 60   ? B LYS 60   
137 1 Y 1 A ALA 61   ? B ALA 61   
138 1 Y 1 A LYS 62   ? B LYS 62   
139 1 Y 1 A GLN 63   ? B GLN 63   
140 1 Y 1 A ALA 64   ? B ALA 64   
141 1 Y 1 A LYS 65   ? B LYS 65   
142 1 Y 1 A MET 66   ? B MET 66   
143 1 Y 1 A ALA 67   ? B ALA 67   
144 1 Y 1 A PRO 68   ? B PRO 68   
145 1 Y 1 A SER 69   ? B SER 69   
146 1 Y 1 A ARG 70   ? B ARG 70   
147 1 Y 1 A MET 71   ? B MET 71   
148 1 Y 1 A ASP 72   ? B ASP 72   
149 1 Y 1 A SER 73   ? B SER 73   
150 1 Y 1 A LEU 74   ? B LEU 74   
151 1 Y 1 A ARG 75   ? B ARG 75   
152 1 Y 1 A GLY 76   ? B GLY 76   
153 1 Y 1 A GLN 77   ? B GLN 77   
154 1 Y 1 A THR 78   ? B THR 78   
155 1 Y 1 A ASP 79   ? B ASP 79   
156 1 Y 1 A LEU 80   ? B LEU 80   
157 1 Y 1 A MET 81   ? B MET 81   
158 1 Y 1 A ALA 82   ? B ALA 82   
159 1 Y 1 A GLU 83   ? B GLU 83   
160 1 Y 1 A ARG 84   ? B ARG 84   
161 1 Y 1 A LEU 85   ? B LEU 85   
162 1 Y 1 A GLU 86   ? B GLU 86   
163 1 Y 1 A ASP 87   ? B ASP 87   
164 1 Y 1 A GLU 88   ? B GLU 88   
165 1 Y 1 A GLU 89   ? B GLU 89   
166 1 Y 1 A GLN 90   ? B GLN 90   
167 1 Y 1 A LEU 91   ? B LEU 91   
168 1 Y 1 A THR 330  ? B THR 330  
169 1 Y 1 A PRO 331  ? B PRO 331  
170 1 Y 1 A GLU 332  ? B GLU 332  
171 1 Y 1 A LYS 333  ? B LYS 333  
172 1 Y 1 A VAL 334  ? B VAL 334  
173 1 Y 1 A PHE 335  ? B PHE 335  
174 1 Y 1 A THR 336  ? B THR 336  
175 1 Y 1 A VAL 337  ? B VAL 337  
176 1 Y 1 A SER 338  ? B SER 338  
177 1 Y 1 A ASN 339  ? B ASN 339  
178 1 Y 1 A ILE 340  ? B ILE 340  
179 1 Y 1 A LYS 341  ? B LYS 341  
180 1 Y 1 A THR 342  ? B THR 342  
181 1 Y 1 A PRO 343  ? B PRO 343  
182 1 Y 1 A LYS 344  ? B LYS 344  
183 1 Y 1 A GLN 345  ? B GLN 345  
184 1 Y 1 A MET 346  ? B MET 346  
185 1 Y 1 A ASP 347  ? B ASP 347  
186 1 Y 1 A GLU 348  ? B GLU 348  
187 1 Y 1 A PHE 349  ? B PHE 349  
188 1 Y 1 A ILE 350  ? B ILE 350  
189 1 Y 1 A GLU 351  ? B GLU 351  
190 1 Y 1 A ILE 352  ? B ILE 352  
191 1 Y 1 A GLN 353  ? B GLN 353  
192 1 Y 1 A SER 354  ? B SER 354  
193 1 Y 1 A SER 355  ? B SER 355  
194 1 Y 1 A THR 356  ? B THR 356  
195 1 Y 1 A GLY 357  ? B GLY 357  
196 1 Y 1 A THR 358  ? B THR 358  
197 1 Y 1 A TRP 359  ? B TRP 359  
198 1 Y 1 A TYR 360  ? B TYR 360  
199 1 Y 1 A GLN 361  ? B GLN 361  
200 1 Y 1 A ARG 362  ? B ARG 362  
201 1 Y 1 A TRP 363  ? B TRP 363  
202 1 Y 1 A LEU 364  ? B LEU 364  
203 1 Y 1 A VAL 365  ? B VAL 365  
204 1 Y 1 A ARG 366  ? B ARG 366  
205 1 Y 1 A PHE 367  ? B PHE 367  
206 1 Y 1 A LYS 368  ? B LYS 368  
207 1 Y 1 A THR 369  ? B THR 369  
208 1 Y 1 A GLU 679  ? B GLU 679  
209 1 Y 1 A GLN 680  ? B GLN 680  
210 1 Y 1 A VAL 681  ? B VAL 681  
211 1 Y 1 A LEU 682  ? B LEU 682  
212 1 Y 1 A MET 683  ? B MET 683  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
BMA C1   C N R 74  
BMA C2   C N S 75  
BMA C3   C N S 76  
BMA C4   C N S 77  
BMA C5   C N R 78  
BMA C6   C N N 79  
BMA O1   O N N 80  
BMA O2   O N N 81  
BMA O3   O N N 82  
BMA O4   O N N 83  
BMA O5   O N N 84  
BMA O6   O N N 85  
BMA H1   H N N 86  
BMA H2   H N N 87  
BMA H3   H N N 88  
BMA H4   H N N 89  
BMA H5   H N N 90  
BMA H61  H N N 91  
BMA H62  H N N 92  
BMA HO1  H N N 93  
BMA HO2  H N N 94  
BMA HO3  H N N 95  
BMA HO4  H N N 96  
BMA HO6  H N N 97  
CYS N    N N N 98  
CYS CA   C N R 99  
CYS C    C N N 100 
CYS O    O N N 101 
CYS CB   C N N 102 
CYS SG   S N N 103 
CYS OXT  O N N 104 
CYS H    H N N 105 
CYS H2   H N N 106 
CYS HA   H N N 107 
CYS HB2  H N N 108 
CYS HB3  H N N 109 
CYS HG   H N N 110 
CYS HXT  H N N 111 
FUC C1   C N R 112 
FUC C2   C N S 113 
FUC C3   C N R 114 
FUC C4   C N S 115 
FUC C5   C N S 116 
FUC C6   C N N 117 
FUC O1   O N N 118 
FUC O2   O N N 119 
FUC O3   O N N 120 
FUC O4   O N N 121 
FUC O5   O N N 122 
FUC H1   H N N 123 
FUC H2   H N N 124 
FUC H3   H N N 125 
FUC H4   H N N 126 
FUC H5   H N N 127 
FUC H61  H N N 128 
FUC H62  H N N 129 
FUC H63  H N N 130 
FUC HO1  H N N 131 
FUC HO2  H N N 132 
FUC HO3  H N N 133 
FUC HO4  H N N 134 
GLN N    N N N 135 
GLN CA   C N S 136 
GLN C    C N N 137 
GLN O    O N N 138 
GLN CB   C N N 139 
GLN CG   C N N 140 
GLN CD   C N N 141 
GLN OE1  O N N 142 
GLN NE2  N N N 143 
GLN OXT  O N N 144 
GLN H    H N N 145 
GLN H2   H N N 146 
GLN HA   H N N 147 
GLN HB2  H N N 148 
GLN HB3  H N N 149 
GLN HG2  H N N 150 
GLN HG3  H N N 151 
GLN HE21 H N N 152 
GLN HE22 H N N 153 
GLN HXT  H N N 154 
GLU N    N N N 155 
GLU CA   C N S 156 
GLU C    C N N 157 
GLU O    O N N 158 
GLU CB   C N N 159 
GLU CG   C N N 160 
GLU CD   C N N 161 
GLU OE1  O N N 162 
GLU OE2  O N N 163 
GLU OXT  O N N 164 
GLU H    H N N 165 
GLU H2   H N N 166 
GLU HA   H N N 167 
GLU HB2  H N N 168 
GLU HB3  H N N 169 
GLU HG2  H N N 170 
GLU HG3  H N N 171 
GLU HE2  H N N 172 
GLU HXT  H N N 173 
GLY N    N N N 174 
GLY CA   C N N 175 
GLY C    C N N 176 
GLY O    O N N 177 
GLY OXT  O N N 178 
GLY H    H N N 179 
GLY H2   H N N 180 
GLY HA2  H N N 181 
GLY HA3  H N N 182 
GLY HXT  H N N 183 
HIS N    N N N 184 
HIS CA   C N S 185 
HIS C    C N N 186 
HIS O    O N N 187 
HIS CB   C N N 188 
HIS CG   C Y N 189 
HIS ND1  N Y N 190 
HIS CD2  C Y N 191 
HIS CE1  C Y N 192 
HIS NE2  N Y N 193 
HIS OXT  O N N 194 
HIS H    H N N 195 
HIS H2   H N N 196 
HIS HA   H N N 197 
HIS HB2  H N N 198 
HIS HB3  H N N 199 
HIS HD1  H N N 200 
HIS HD2  H N N 201 
HIS HE1  H N N 202 
HIS HE2  H N N 203 
HIS HXT  H N N 204 
ILE N    N N N 205 
ILE CA   C N S 206 
ILE C    C N N 207 
ILE O    O N N 208 
ILE CB   C N S 209 
ILE CG1  C N N 210 
ILE CG2  C N N 211 
ILE CD1  C N N 212 
ILE OXT  O N N 213 
ILE H    H N N 214 
ILE H2   H N N 215 
ILE HA   H N N 216 
ILE HB   H N N 217 
ILE HG12 H N N 218 
ILE HG13 H N N 219 
ILE HG21 H N N 220 
ILE HG22 H N N 221 
ILE HG23 H N N 222 
ILE HD11 H N N 223 
ILE HD12 H N N 224 
ILE HD13 H N N 225 
ILE HXT  H N N 226 
LEU N    N N N 227 
LEU CA   C N S 228 
LEU C    C N N 229 
LEU O    O N N 230 
LEU CB   C N N 231 
LEU CG   C N N 232 
LEU CD1  C N N 233 
LEU CD2  C N N 234 
LEU OXT  O N N 235 
LEU H    H N N 236 
LEU H2   H N N 237 
LEU HA   H N N 238 
LEU HB2  H N N 239 
LEU HB3  H N N 240 
LEU HG   H N N 241 
LEU HD11 H N N 242 
LEU HD12 H N N 243 
LEU HD13 H N N 244 
LEU HD21 H N N 245 
LEU HD22 H N N 246 
LEU HD23 H N N 247 
LEU HXT  H N N 248 
LYS N    N N N 249 
LYS CA   C N S 250 
LYS C    C N N 251 
LYS O    O N N 252 
LYS CB   C N N 253 
LYS CG   C N N 254 
LYS CD   C N N 255 
LYS CE   C N N 256 
LYS NZ   N N N 257 
LYS OXT  O N N 258 
LYS H    H N N 259 
LYS H2   H N N 260 
LYS HA   H N N 261 
LYS HB2  H N N 262 
LYS HB3  H N N 263 
LYS HG2  H N N 264 
LYS HG3  H N N 265 
LYS HD2  H N N 266 
LYS HD3  H N N 267 
LYS HE2  H N N 268 
LYS HE3  H N N 269 
LYS HZ1  H N N 270 
LYS HZ2  H N N 271 
LYS HZ3  H N N 272 
LYS HXT  H N N 273 
MAN C1   C N S 274 
MAN C2   C N S 275 
MAN C3   C N S 276 
MAN C4   C N S 277 
MAN C5   C N R 278 
MAN C6   C N N 279 
MAN O1   O N N 280 
MAN O2   O N N 281 
MAN O3   O N N 282 
MAN O4   O N N 283 
MAN O5   O N N 284 
MAN O6   O N N 285 
MAN H1   H N N 286 
MAN H2   H N N 287 
MAN H3   H N N 288 
MAN H4   H N N 289 
MAN H5   H N N 290 
MAN H61  H N N 291 
MAN H62  H N N 292 
MAN HO1  H N N 293 
MAN HO2  H N N 294 
MAN HO3  H N N 295 
MAN HO4  H N N 296 
MAN HO6  H N N 297 
MET N    N N N 298 
MET CA   C N S 299 
MET C    C N N 300 
MET O    O N N 301 
MET CB   C N N 302 
MET CG   C N N 303 
MET SD   S N N 304 
MET CE   C N N 305 
MET OXT  O N N 306 
MET H    H N N 307 
MET H2   H N N 308 
MET HA   H N N 309 
MET HB2  H N N 310 
MET HB3  H N N 311 
MET HG2  H N N 312 
MET HG3  H N N 313 
MET HE1  H N N 314 
MET HE2  H N N 315 
MET HE3  H N N 316 
MET HXT  H N N 317 
NAG C1   C N R 318 
NAG C2   C N R 319 
NAG C3   C N R 320 
NAG C4   C N S 321 
NAG C5   C N R 322 
NAG C6   C N N 323 
NAG C7   C N N 324 
NAG C8   C N N 325 
NAG N2   N N N 326 
NAG O1   O N N 327 
NAG O3   O N N 328 
NAG O4   O N N 329 
NAG O5   O N N 330 
NAG O6   O N N 331 
NAG O7   O N N 332 
NAG H1   H N N 333 
NAG H2   H N N 334 
NAG H3   H N N 335 
NAG H4   H N N 336 
NAG H5   H N N 337 
NAG H61  H N N 338 
NAG H62  H N N 339 
NAG H81  H N N 340 
NAG H82  H N N 341 
NAG H83  H N N 342 
NAG HN2  H N N 343 
NAG HO1  H N N 344 
NAG HO3  H N N 345 
NAG HO4  H N N 346 
NAG HO6  H N N 347 
PHE N    N N N 348 
PHE CA   C N S 349 
PHE C    C N N 350 
PHE O    O N N 351 
PHE CB   C N N 352 
PHE CG   C Y N 353 
PHE CD1  C Y N 354 
PHE CD2  C Y N 355 
PHE CE1  C Y N 356 
PHE CE2  C Y N 357 
PHE CZ   C Y N 358 
PHE OXT  O N N 359 
PHE H    H N N 360 
PHE H2   H N N 361 
PHE HA   H N N 362 
PHE HB2  H N N 363 
PHE HB3  H N N 364 
PHE HD1  H N N 365 
PHE HD2  H N N 366 
PHE HE1  H N N 367 
PHE HE2  H N N 368 
PHE HZ   H N N 369 
PHE HXT  H N N 370 
PRO N    N N N 371 
PRO CA   C N S 372 
PRO C    C N N 373 
PRO O    O N N 374 
PRO CB   C N N 375 
PRO CG   C N N 376 
PRO CD   C N N 377 
PRO OXT  O N N 378 
PRO H    H N N 379 
PRO HA   H N N 380 
PRO HB2  H N N 381 
PRO HB3  H N N 382 
PRO HG2  H N N 383 
PRO HG3  H N N 384 
PRO HD2  H N N 385 
PRO HD3  H N N 386 
PRO HXT  H N N 387 
SER N    N N N 388 
SER CA   C N S 389 
SER C    C N N 390 
SER O    O N N 391 
SER CB   C N N 392 
SER OG   O N N 393 
SER OXT  O N N 394 
SER H    H N N 395 
SER H2   H N N 396 
SER HA   H N N 397 
SER HB2  H N N 398 
SER HB3  H N N 399 
SER HG   H N N 400 
SER HXT  H N N 401 
THR N    N N N 402 
THR CA   C N S 403 
THR C    C N N 404 
THR O    O N N 405 
THR CB   C N R 406 
THR OG1  O N N 407 
THR CG2  C N N 408 
THR OXT  O N N 409 
THR H    H N N 410 
THR H2   H N N 411 
THR HA   H N N 412 
THR HB   H N N 413 
THR HG1  H N N 414 
THR HG21 H N N 415 
THR HG22 H N N 416 
THR HG23 H N N 417 
THR HXT  H N N 418 
TRP N    N N N 419 
TRP CA   C N S 420 
TRP C    C N N 421 
TRP O    O N N 422 
TRP CB   C N N 423 
TRP CG   C Y N 424 
TRP CD1  C Y N 425 
TRP CD2  C Y N 426 
TRP NE1  N Y N 427 
TRP CE2  C Y N 428 
TRP CE3  C Y N 429 
TRP CZ2  C Y N 430 
TRP CZ3  C Y N 431 
TRP CH2  C Y N 432 
TRP OXT  O N N 433 
TRP H    H N N 434 
TRP H2   H N N 435 
TRP HA   H N N 436 
TRP HB2  H N N 437 
TRP HB3  H N N 438 
TRP HD1  H N N 439 
TRP HE1  H N N 440 
TRP HE3  H N N 441 
TRP HZ2  H N N 442 
TRP HZ3  H N N 443 
TRP HH2  H N N 444 
TRP HXT  H N N 445 
TYR N    N N N 446 
TYR CA   C N S 447 
TYR C    C N N 448 
TYR O    O N N 449 
TYR CB   C N N 450 
TYR CG   C Y N 451 
TYR CD1  C Y N 452 
TYR CD2  C Y N 453 
TYR CE1  C Y N 454 
TYR CE2  C Y N 455 
TYR CZ   C Y N 456 
TYR OH   O N N 457 
TYR OXT  O N N 458 
TYR H    H N N 459 
TYR H2   H N N 460 
TYR HA   H N N 461 
TYR HB2  H N N 462 
TYR HB3  H N N 463 
TYR HD1  H N N 464 
TYR HD2  H N N 465 
TYR HE1  H N N 466 
TYR HE2  H N N 467 
TYR HH   H N N 468 
TYR HXT  H N N 469 
VAL N    N N N 470 
VAL CA   C N S 471 
VAL C    C N N 472 
VAL O    O N N 473 
VAL CB   C N N 474 
VAL CG1  C N N 475 
VAL CG2  C N N 476 
VAL OXT  O N N 477 
VAL H    H N N 478 
VAL H2   H N N 479 
VAL HA   H N N 480 
VAL HB   H N N 481 
VAL HG11 H N N 482 
VAL HG12 H N N 483 
VAL HG13 H N N 484 
VAL HG21 H N N 485 
VAL HG22 H N N 486 
VAL HG23 H N N 487 
VAL HXT  H N N 488 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BMA C1  C2   sing N N 70  
BMA C1  O1   sing N N 71  
BMA C1  O5   sing N N 72  
BMA C1  H1   sing N N 73  
BMA C2  C3   sing N N 74  
BMA C2  O2   sing N N 75  
BMA C2  H2   sing N N 76  
BMA C3  C4   sing N N 77  
BMA C3  O3   sing N N 78  
BMA C3  H3   sing N N 79  
BMA C4  C5   sing N N 80  
BMA C4  O4   sing N N 81  
BMA C4  H4   sing N N 82  
BMA C5  C6   sing N N 83  
BMA C5  O5   sing N N 84  
BMA C5  H5   sing N N 85  
BMA C6  O6   sing N N 86  
BMA C6  H61  sing N N 87  
BMA C6  H62  sing N N 88  
BMA O1  HO1  sing N N 89  
BMA O2  HO2  sing N N 90  
BMA O3  HO3  sing N N 91  
BMA O4  HO4  sing N N 92  
BMA O6  HO6  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
FUC C1  C2   sing N N 107 
FUC C1  O1   sing N N 108 
FUC C1  O5   sing N N 109 
FUC C1  H1   sing N N 110 
FUC C2  C3   sing N N 111 
FUC C2  O2   sing N N 112 
FUC C2  H2   sing N N 113 
FUC C3  C4   sing N N 114 
FUC C3  O3   sing N N 115 
FUC C3  H3   sing N N 116 
FUC C4  C5   sing N N 117 
FUC C4  O4   sing N N 118 
FUC C4  H4   sing N N 119 
FUC C5  C6   sing N N 120 
FUC C5  O5   sing N N 121 
FUC C5  H5   sing N N 122 
FUC C6  H61  sing N N 123 
FUC C6  H62  sing N N 124 
FUC C6  H63  sing N N 125 
FUC O1  HO1  sing N N 126 
FUC O2  HO2  sing N N 127 
FUC O3  HO3  sing N N 128 
FUC O4  HO4  sing N N 129 
GLN N   CA   sing N N 130 
GLN N   H    sing N N 131 
GLN N   H2   sing N N 132 
GLN CA  C    sing N N 133 
GLN CA  CB   sing N N 134 
GLN CA  HA   sing N N 135 
GLN C   O    doub N N 136 
GLN C   OXT  sing N N 137 
GLN CB  CG   sing N N 138 
GLN CB  HB2  sing N N 139 
GLN CB  HB3  sing N N 140 
GLN CG  CD   sing N N 141 
GLN CG  HG2  sing N N 142 
GLN CG  HG3  sing N N 143 
GLN CD  OE1  doub N N 144 
GLN CD  NE2  sing N N 145 
GLN NE2 HE21 sing N N 146 
GLN NE2 HE22 sing N N 147 
GLN OXT HXT  sing N N 148 
GLU N   CA   sing N N 149 
GLU N   H    sing N N 150 
GLU N   H2   sing N N 151 
GLU CA  C    sing N N 152 
GLU CA  CB   sing N N 153 
GLU CA  HA   sing N N 154 
GLU C   O    doub N N 155 
GLU C   OXT  sing N N 156 
GLU CB  CG   sing N N 157 
GLU CB  HB2  sing N N 158 
GLU CB  HB3  sing N N 159 
GLU CG  CD   sing N N 160 
GLU CG  HG2  sing N N 161 
GLU CG  HG3  sing N N 162 
GLU CD  OE1  doub N N 163 
GLU CD  OE2  sing N N 164 
GLU OE2 HE2  sing N N 165 
GLU OXT HXT  sing N N 166 
GLY N   CA   sing N N 167 
GLY N   H    sing N N 168 
GLY N   H2   sing N N 169 
GLY CA  C    sing N N 170 
GLY CA  HA2  sing N N 171 
GLY CA  HA3  sing N N 172 
GLY C   O    doub N N 173 
GLY C   OXT  sing N N 174 
GLY OXT HXT  sing N N 175 
HIS N   CA   sing N N 176 
HIS N   H    sing N N 177 
HIS N   H2   sing N N 178 
HIS CA  C    sing N N 179 
HIS CA  CB   sing N N 180 
HIS CA  HA   sing N N 181 
HIS C   O    doub N N 182 
HIS C   OXT  sing N N 183 
HIS CB  CG   sing N N 184 
HIS CB  HB2  sing N N 185 
HIS CB  HB3  sing N N 186 
HIS CG  ND1  sing Y N 187 
HIS CG  CD2  doub Y N 188 
HIS ND1 CE1  doub Y N 189 
HIS ND1 HD1  sing N N 190 
HIS CD2 NE2  sing Y N 191 
HIS CD2 HD2  sing N N 192 
HIS CE1 NE2  sing Y N 193 
HIS CE1 HE1  sing N N 194 
HIS NE2 HE2  sing N N 195 
HIS OXT HXT  sing N N 196 
ILE N   CA   sing N N 197 
ILE N   H    sing N N 198 
ILE N   H2   sing N N 199 
ILE CA  C    sing N N 200 
ILE CA  CB   sing N N 201 
ILE CA  HA   sing N N 202 
ILE C   O    doub N N 203 
ILE C   OXT  sing N N 204 
ILE CB  CG1  sing N N 205 
ILE CB  CG2  sing N N 206 
ILE CB  HB   sing N N 207 
ILE CG1 CD1  sing N N 208 
ILE CG1 HG12 sing N N 209 
ILE CG1 HG13 sing N N 210 
ILE CG2 HG21 sing N N 211 
ILE CG2 HG22 sing N N 212 
ILE CG2 HG23 sing N N 213 
ILE CD1 HD11 sing N N 214 
ILE CD1 HD12 sing N N 215 
ILE CD1 HD13 sing N N 216 
ILE OXT HXT  sing N N 217 
LEU N   CA   sing N N 218 
LEU N   H    sing N N 219 
LEU N   H2   sing N N 220 
LEU CA  C    sing N N 221 
LEU CA  CB   sing N N 222 
LEU CA  HA   sing N N 223 
LEU C   O    doub N N 224 
LEU C   OXT  sing N N 225 
LEU CB  CG   sing N N 226 
LEU CB  HB2  sing N N 227 
LEU CB  HB3  sing N N 228 
LEU CG  CD1  sing N N 229 
LEU CG  CD2  sing N N 230 
LEU CG  HG   sing N N 231 
LEU CD1 HD11 sing N N 232 
LEU CD1 HD12 sing N N 233 
LEU CD1 HD13 sing N N 234 
LEU CD2 HD21 sing N N 235 
LEU CD2 HD22 sing N N 236 
LEU CD2 HD23 sing N N 237 
LEU OXT HXT  sing N N 238 
LYS N   CA   sing N N 239 
LYS N   H    sing N N 240 
LYS N   H2   sing N N 241 
LYS CA  C    sing N N 242 
LYS CA  CB   sing N N 243 
LYS CA  HA   sing N N 244 
LYS C   O    doub N N 245 
LYS C   OXT  sing N N 246 
LYS CB  CG   sing N N 247 
LYS CB  HB2  sing N N 248 
LYS CB  HB3  sing N N 249 
LYS CG  CD   sing N N 250 
LYS CG  HG2  sing N N 251 
LYS CG  HG3  sing N N 252 
LYS CD  CE   sing N N 253 
LYS CD  HD2  sing N N 254 
LYS CD  HD3  sing N N 255 
LYS CE  NZ   sing N N 256 
LYS CE  HE2  sing N N 257 
LYS CE  HE3  sing N N 258 
LYS NZ  HZ1  sing N N 259 
LYS NZ  HZ2  sing N N 260 
LYS NZ  HZ3  sing N N 261 
LYS OXT HXT  sing N N 262 
MAN C1  C2   sing N N 263 
MAN C1  O1   sing N N 264 
MAN C1  O5   sing N N 265 
MAN C1  H1   sing N N 266 
MAN C2  C3   sing N N 267 
MAN C2  O2   sing N N 268 
MAN C2  H2   sing N N 269 
MAN C3  C4   sing N N 270 
MAN C3  O3   sing N N 271 
MAN C3  H3   sing N N 272 
MAN C4  C5   sing N N 273 
MAN C4  O4   sing N N 274 
MAN C4  H4   sing N N 275 
MAN C5  C6   sing N N 276 
MAN C5  O5   sing N N 277 
MAN C5  H5   sing N N 278 
MAN C6  O6   sing N N 279 
MAN C6  H61  sing N N 280 
MAN C6  H62  sing N N 281 
MAN O1  HO1  sing N N 282 
MAN O2  HO2  sing N N 283 
MAN O3  HO3  sing N N 284 
MAN O4  HO4  sing N N 285 
MAN O6  HO6  sing N N 286 
MET N   CA   sing N N 287 
MET N   H    sing N N 288 
MET N   H2   sing N N 289 
MET CA  C    sing N N 290 
MET CA  CB   sing N N 291 
MET CA  HA   sing N N 292 
MET C   O    doub N N 293 
MET C   OXT  sing N N 294 
MET CB  CG   sing N N 295 
MET CB  HB2  sing N N 296 
MET CB  HB3  sing N N 297 
MET CG  SD   sing N N 298 
MET CG  HG2  sing N N 299 
MET CG  HG3  sing N N 300 
MET SD  CE   sing N N 301 
MET CE  HE1  sing N N 302 
MET CE  HE2  sing N N 303 
MET CE  HE3  sing N N 304 
MET OXT HXT  sing N N 305 
NAG C1  C2   sing N N 306 
NAG C1  O1   sing N N 307 
NAG C1  O5   sing N N 308 
NAG C1  H1   sing N N 309 
NAG C2  C3   sing N N 310 
NAG C2  N2   sing N N 311 
NAG C2  H2   sing N N 312 
NAG C3  C4   sing N N 313 
NAG C3  O3   sing N N 314 
NAG C3  H3   sing N N 315 
NAG C4  C5   sing N N 316 
NAG C4  O4   sing N N 317 
NAG C4  H4   sing N N 318 
NAG C5  C6   sing N N 319 
NAG C5  O5   sing N N 320 
NAG C5  H5   sing N N 321 
NAG C6  O6   sing N N 322 
NAG C6  H61  sing N N 323 
NAG C6  H62  sing N N 324 
NAG C7  C8   sing N N 325 
NAG C7  N2   sing N N 326 
NAG C7  O7   doub N N 327 
NAG C8  H81  sing N N 328 
NAG C8  H82  sing N N 329 
NAG C8  H83  sing N N 330 
NAG N2  HN2  sing N N 331 
NAG O1  HO1  sing N N 332 
NAG O3  HO3  sing N N 333 
NAG O4  HO4  sing N N 334 
NAG O6  HO6  sing N N 335 
PHE N   CA   sing N N 336 
PHE N   H    sing N N 337 
PHE N   H2   sing N N 338 
PHE CA  C    sing N N 339 
PHE CA  CB   sing N N 340 
PHE CA  HA   sing N N 341 
PHE C   O    doub N N 342 
PHE C   OXT  sing N N 343 
PHE CB  CG   sing N N 344 
PHE CB  HB2  sing N N 345 
PHE CB  HB3  sing N N 346 
PHE CG  CD1  doub Y N 347 
PHE CG  CD2  sing Y N 348 
PHE CD1 CE1  sing Y N 349 
PHE CD1 HD1  sing N N 350 
PHE CD2 CE2  doub Y N 351 
PHE CD2 HD2  sing N N 352 
PHE CE1 CZ   doub Y N 353 
PHE CE1 HE1  sing N N 354 
PHE CE2 CZ   sing Y N 355 
PHE CE2 HE2  sing N N 356 
PHE CZ  HZ   sing N N 357 
PHE OXT HXT  sing N N 358 
PRO N   CA   sing N N 359 
PRO N   CD   sing N N 360 
PRO N   H    sing N N 361 
PRO CA  C    sing N N 362 
PRO CA  CB   sing N N 363 
PRO CA  HA   sing N N 364 
PRO C   O    doub N N 365 
PRO C   OXT  sing N N 366 
PRO CB  CG   sing N N 367 
PRO CB  HB2  sing N N 368 
PRO CB  HB3  sing N N 369 
PRO CG  CD   sing N N 370 
PRO CG  HG2  sing N N 371 
PRO CG  HG3  sing N N 372 
PRO CD  HD2  sing N N 373 
PRO CD  HD3  sing N N 374 
PRO OXT HXT  sing N N 375 
SER N   CA   sing N N 376 
SER N   H    sing N N 377 
SER N   H2   sing N N 378 
SER CA  C    sing N N 379 
SER CA  CB   sing N N 380 
SER CA  HA   sing N N 381 
SER C   O    doub N N 382 
SER C   OXT  sing N N 383 
SER CB  OG   sing N N 384 
SER CB  HB2  sing N N 385 
SER CB  HB3  sing N N 386 
SER OG  HG   sing N N 387 
SER OXT HXT  sing N N 388 
THR N   CA   sing N N 389 
THR N   H    sing N N 390 
THR N   H2   sing N N 391 
THR CA  C    sing N N 392 
THR CA  CB   sing N N 393 
THR CA  HA   sing N N 394 
THR C   O    doub N N 395 
THR C   OXT  sing N N 396 
THR CB  OG1  sing N N 397 
THR CB  CG2  sing N N 398 
THR CB  HB   sing N N 399 
THR OG1 HG1  sing N N 400 
THR CG2 HG21 sing N N 401 
THR CG2 HG22 sing N N 402 
THR CG2 HG23 sing N N 403 
THR OXT HXT  sing N N 404 
TRP N   CA   sing N N 405 
TRP N   H    sing N N 406 
TRP N   H2   sing N N 407 
TRP CA  C    sing N N 408 
TRP CA  CB   sing N N 409 
TRP CA  HA   sing N N 410 
TRP C   O    doub N N 411 
TRP C   OXT  sing N N 412 
TRP CB  CG   sing N N 413 
TRP CB  HB2  sing N N 414 
TRP CB  HB3  sing N N 415 
TRP CG  CD1  doub Y N 416 
TRP CG  CD2  sing Y N 417 
TRP CD1 NE1  sing Y N 418 
TRP CD1 HD1  sing N N 419 
TRP CD2 CE2  doub Y N 420 
TRP CD2 CE3  sing Y N 421 
TRP NE1 CE2  sing Y N 422 
TRP NE1 HE1  sing N N 423 
TRP CE2 CZ2  sing Y N 424 
TRP CE3 CZ3  doub Y N 425 
TRP CE3 HE3  sing N N 426 
TRP CZ2 CH2  doub Y N 427 
TRP CZ2 HZ2  sing N N 428 
TRP CZ3 CH2  sing Y N 429 
TRP CZ3 HZ3  sing N N 430 
TRP CH2 HH2  sing N N 431 
TRP OXT HXT  sing N N 432 
TYR N   CA   sing N N 433 
TYR N   H    sing N N 434 
TYR N   H2   sing N N 435 
TYR CA  C    sing N N 436 
TYR CA  CB   sing N N 437 
TYR CA  HA   sing N N 438 
TYR C   O    doub N N 439 
TYR C   OXT  sing N N 440 
TYR CB  CG   sing N N 441 
TYR CB  HB2  sing N N 442 
TYR CB  HB3  sing N N 443 
TYR CG  CD1  doub Y N 444 
TYR CG  CD2  sing Y N 445 
TYR CD1 CE1  sing Y N 446 
TYR CD1 HD1  sing N N 447 
TYR CD2 CE2  doub Y N 448 
TYR CD2 HD2  sing N N 449 
TYR CE1 CZ   doub Y N 450 
TYR CE1 HE1  sing N N 451 
TYR CE2 CZ   sing Y N 452 
TYR CE2 HE2  sing N N 453 
TYR CZ  OH   sing N N 454 
TYR OH  HH   sing N N 455 
TYR OXT HXT  sing N N 456 
VAL N   CA   sing N N 457 
VAL N   H    sing N N 458 
VAL N   H2   sing N N 459 
VAL CA  C    sing N N 460 
VAL CA  CB   sing N N 461 
VAL CA  HA   sing N N 462 
VAL C   O    doub N N 463 
VAL C   OXT  sing N N 464 
VAL CB  CG1  sing N N 465 
VAL CB  CG2  sing N N 466 
VAL CB  HB   sing N N 467 
VAL CG1 HG11 sing N N 468 
VAL CG1 HG12 sing N N 469 
VAL CG1 HG13 sing N N 470 
VAL CG2 HG21 sing N N 471 
VAL CG2 HG22 sing N N 472 
VAL CG2 HG23 sing N N 473 
VAL OXT HXT  sing N N 474 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-04-23 
_em_admin.deposition_site    PDBE 
_em_admin.entry_id           9F2J 
_em_admin.last_update        2025-03-12 
_em_admin.map_release_date   2025-03-12 
_em_admin.title              'Cryo-EM structure of SV2B-BoNT/A1 complex' 
# 
_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                0.22 
# 
_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          1491 
_em_entity_assembly_naturalsource.organism             'Clostridium botulinum' 
_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          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_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         54 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (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                     28457 
# 
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 
'PARTICLE SELECTION'            ? 1  1 ? ? RELION    5.0-beta 
'IMAGE ACQUISITION'             ? 2  ? ? 1 ?         ?        
MASKING                         ? 3  ? ? ? ?         ?        
'CTF CORRECTION'                ? 4  1 ? ? CTFFIND   4.1      
'LAYERLINE INDEXING'            ? 5  ? ? ? ?         ?        
'DIFFRACTION INDEXING'          ? 6  ? ? ? ?         ?        
'MODEL FITTING'                 ? 7  ? 1 ? Coot      ?        
OTHER                           ? 8  ? ? ? ?         ?        
'INITIAL EULER ASSIGNMENT'      ? 9  1 ? ? ?         ?        
'FINAL EULER ASSIGNMENT'        ? 10 1 ? ? ?         ?        
CLASSIFICATION                  ? 11 1 ? ? ?         ?        
RECONSTRUCTION                  ? 12 1 ? ? cryoSPARC ?        
'MODEL REFINEMENT'              ? 13 ? 1 ? PHENIX    ?        
'VOLUME SELECTION'              ? 14 1 1 1 ?         ?        
'SERIES ALIGNMENT'              ? 15 1 1 1 ?         ?        
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ?         ?        
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ?         ?        
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ?         ?        
'CRYSTALLOGRAPHY MERGING'       ? 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 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Swiss National Science Foundation' Switzerland 310030_212253 1 
'Swiss National Science Foundation' Switzerland 198545        2 
# 
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 FUC 2 n 
4 NAG 1 n 
4 NAG 2 n 
4 BMA 3 n 
4 MAN 4 n 
4 MAN 5 n 
4 FUC 6 n 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB 9F1R ? 
2 ? 'experimental model' PDB 9F2B ? 
# 
_atom_sites.entry_id                    9F2J 
_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 
C 
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   . SER A 1 18   ? 226.800 190.365 290.699 1.00 78.42  ? 1    SER B N   1 
ATOM   2     C CA  . SER A 1 18   ? 226.455 190.895 292.012 1.00 78.42  ? 1    SER B CA  1 
ATOM   3     C C   . SER A 1 18   ? 224.946 190.873 292.228 1.00 78.42  ? 1    SER B C   1 
ATOM   4     O O   . SER A 1 18   ? 224.209 191.587 291.550 1.00 78.42  ? 1    SER B O   1 
ATOM   5     C CB  . SER A 1 18   ? 226.990 192.319 292.173 1.00 78.42  ? 1    SER B CB  1 
ATOM   6     O OG  . SER A 1 18   ? 227.215 192.627 293.537 1.00 78.42  ? 1    SER B OG  1 
ATOM   7     N N   . PRO A 1 19   ? 224.488 190.055 293.169 1.00 79.89  ? 2    PRO B N   1 
ATOM   8     C CA  . PRO A 1 19   ? 223.052 189.975 293.444 1.00 79.89  ? 2    PRO B CA  1 
ATOM   9     C C   . PRO A 1 19   ? 222.537 191.222 294.143 1.00 79.89  ? 2    PRO B C   1 
ATOM   10    O O   . PRO A 1 19   ? 223.279 191.947 294.809 1.00 79.89  ? 2    PRO B O   1 
ATOM   11    C CB  . PRO A 1 19   ? 222.944 188.747 294.353 1.00 79.89  ? 2    PRO B CB  1 
ATOM   12    C CG  . PRO A 1 19   ? 224.235 188.744 295.095 1.00 79.89  ? 2    PRO B CG  1 
ATOM   13    C CD  . PRO A 1 19   ? 225.276 189.258 294.125 1.00 79.89  ? 2    PRO B CD  1 
ATOM   14    N N   . PHE A 1 20   ? 221.239 191.466 293.972 1.00 74.79  ? 3    PHE B N   1 
ATOM   15    C CA  . PHE A 1 20   ? 220.596 192.610 294.605 1.00 74.79  ? 3    PHE B CA  1 
ATOM   16    C C   . PHE A 1 20   ? 220.652 192.500 296.121 1.00 74.79  ? 3    PHE B C   1 
ATOM   17    O O   . PHE A 1 20   ? 221.327 193.293 296.784 1.00 74.79  ? 3    PHE B O   1 
ATOM   18    C CB  . PHE A 1 20   ? 219.143 192.730 294.149 1.00 74.79  ? 3    PHE B CB  1 
ATOM   19    C CG  . PHE A 1 20   ? 218.505 194.034 294.510 1.00 74.79  ? 3    PHE B CG  1 
ATOM   20    C CD1 . PHE A 1 20   ? 219.252 195.196 294.547 1.00 74.79  ? 3    PHE B CD1 1 
ATOM   21    C CD2 . PHE A 1 20   ? 217.163 194.099 294.827 1.00 74.79  ? 3    PHE B CD2 1 
ATOM   22    C CE1 . PHE A 1 20   ? 218.673 196.398 294.880 1.00 74.79  ? 3    PHE B CE1 1 
ATOM   23    C CE2 . PHE A 1 20   ? 216.581 195.299 295.163 1.00 74.79  ? 3    PHE B CE2 1 
ATOM   24    C CZ  . PHE A 1 20   ? 217.338 196.450 295.191 1.00 74.79  ? 3    PHE B CZ  1 
ATOM   25    N N   . VAL A 1 21   ? 219.962 191.510 296.674 1.00 77.07  ? 4    VAL B N   1 
ATOM   26    C CA  . VAL A 1 21   ? 219.907 191.308 298.116 1.00 77.07  ? 4    VAL B CA  1 
ATOM   27    C C   . VAL A 1 21   ? 221.050 190.387 298.515 1.00 77.07  ? 4    VAL B C   1 
ATOM   28    O O   . VAL A 1 21   ? 221.170 189.271 297.998 1.00 77.07  ? 4    VAL B O   1 
ATOM   29    C CB  . VAL A 1 21   ? 218.555 190.724 298.545 1.00 77.07  ? 4    VAL B CB  1 
ATOM   30    C CG1 . VAL A 1 21   ? 218.487 190.617 300.057 1.00 77.07  ? 4    VAL B CG1 1 
ATOM   31    C CG2 . VAL A 1 21   ? 217.419 191.577 298.014 1.00 77.07  ? 4    VAL B CG2 1 
ATOM   32    N N   . ASN A 1 22   ? 221.887 190.852 299.434 1.00 86.48  ? 5    ASN B N   1 
ATOM   33    C CA  . ASN A 1 22   ? 223.049 190.097 299.875 1.00 86.48  ? 5    ASN B CA  1 
ATOM   34    C C   . ASN A 1 22   ? 222.736 189.370 301.175 1.00 86.48  ? 5    ASN B C   1 
ATOM   35    O O   . ASN A 1 22   ? 222.001 189.885 302.022 1.00 86.48  ? 5    ASN B O   1 
ATOM   36    C CB  . ASN A 1 22   ? 224.243 191.032 300.077 1.00 86.48  ? 5    ASN B CB  1 
ATOM   37    C CG  . ASN A 1 22   ? 225.024 191.274 298.798 1.00 86.48  ? 5    ASN B CG  1 
ATOM   38    O OD1 . ASN A 1 22   ? 224.492 191.802 297.822 1.00 86.48  ? 5    ASN B OD1 1 
ATOM   39    N ND2 . ASN A 1 22   ? 226.296 190.896 298.801 1.00 86.48  ? 5    ASN B ND2 1 
ATOM   40    N N   . LYS A 1 23   ? 223.301 188.169 301.328 1.00 90.90  ? 6    LYS B N   1 
ATOM   41    C CA  . LYS A 1 23   ? 223.287 187.446 302.601 1.00 90.90  ? 6    LYS B CA  1 
ATOM   42    C C   . LYS A 1 23   ? 221.855 187.177 303.078 1.00 90.90  ? 6    LYS B C   1 
ATOM   43    O O   . LYS A 1 23   ? 221.353 187.799 304.016 1.00 90.90  ? 6    LYS B O   1 
ATOM   44    C CB  . LYS A 1 23   ? 224.101 188.200 303.658 1.00 90.90  ? 6    LYS B CB  1 
ATOM   45    C CG  . LYS A 1 23   ? 225.530 188.471 303.226 1.00 90.90  ? 6    LYS B CG  1 
ATOM   46    C CD  . LYS A 1 23   ? 226.310 187.174 303.089 1.00 90.90  ? 6    LYS B CD  1 
ATOM   47    C CE  . LYS A 1 23   ? 227.209 187.196 301.864 1.00 90.90  ? 6    LYS B CE  1 
ATOM   48    N NZ  . LYS A 1 23   ? 226.419 187.204 300.603 1.00 90.90  ? 6    LYS B NZ  1 
ATOM   49    N N   . GLN A 1 24   ? 221.203 186.255 302.361 1.00 91.19  ? 7    GLN B N   1 
ATOM   50    C CA  . GLN A 1 24   ? 219.827 185.847 302.636 1.00 91.19  ? 7    GLN B CA  1 
ATOM   51    C C   . GLN A 1 24   ? 219.569 185.724 304.132 1.00 91.19  ? 7    GLN B C   1 
ATOM   52    O O   . GLN A 1 24   ? 220.436 185.292 304.895 1.00 91.19  ? 7    GLN B O   1 
ATOM   53    C CB  . GLN A 1 24   ? 219.541 184.507 301.956 1.00 91.19  ? 7    GLN B CB  1 
ATOM   54    C CG  . GLN A 1 24   ? 220.079 184.391 300.542 1.00 91.19  ? 7    GLN B CG  1 
ATOM   55    C CD  . GLN A 1 24   ? 219.211 183.517 299.662 1.00 91.19  ? 7    GLN B CD  1 
ATOM   56    O OE1 . GLN A 1 24   ? 218.773 182.443 300.075 1.00 91.19  ? 7    GLN B OE1 1 
ATOM   57    N NE2 . GLN A 1 24   ? 218.959 183.971 298.440 1.00 91.19  ? 7    GLN B NE2 1 
ATOM   58    N N   . PHE A 1 25   ? 218.355 186.096 304.543 1.00 84.71  ? 8    PHE B N   1 
ATOM   59    C CA  . PHE A 1 25   ? 218.080 186.434 305.932 1.00 84.71  ? 8    PHE B CA  1 
ATOM   60    C C   . PHE A 1 25   ? 217.324 185.371 306.717 1.00 84.71  ? 8    PHE B C   1 
ATOM   61    O O   . PHE A 1 25   ? 217.159 185.539 307.929 1.00 84.71  ? 8    PHE B O   1 
ATOM   62    C CB  . PHE A 1 25   ? 217.290 187.750 305.997 1.00 84.71  ? 8    PHE B CB  1 
ATOM   63    C CG  . PHE A 1 25   ? 218.071 188.939 305.528 1.00 84.71  ? 8    PHE B CG  1 
ATOM   64    C CD1 . PHE A 1 25   ? 219.061 189.489 306.319 1.00 84.71  ? 8    PHE B CD1 1 
ATOM   65    C CD2 . PHE A 1 25   ? 217.830 189.492 304.284 1.00 84.71  ? 8    PHE B CD2 1 
ATOM   66    C CE1 . PHE A 1 25   ? 219.789 190.576 305.885 1.00 84.71  ? 8    PHE B CE1 1 
ATOM   67    C CE2 . PHE A 1 25   ? 218.556 190.578 303.845 1.00 84.71  ? 8    PHE B CE2 1 
ATOM   68    C CZ  . PHE A 1 25   ? 219.536 191.119 304.647 1.00 84.71  ? 8    PHE B CZ  1 
ATOM   69    N N   . ASN A 1 26   ? 216.871 184.289 306.078 1.00 83.97  ? 9    ASN B N   1 
ATOM   70    C CA  . ASN A 1 26   ? 215.997 183.317 306.731 1.00 83.97  ? 9    ASN B CA  1 
ATOM   71    C C   . ASN A 1 26   ? 214.825 184.053 307.369 1.00 83.97  ? 9    ASN B C   1 
ATOM   72    O O   . ASN A 1 26   ? 214.304 184.996 306.771 1.00 83.97  ? 9    ASN B O   1 
ATOM   73    C CB  . ASN A 1 26   ? 216.767 182.497 307.769 1.00 83.97  ? 9    ASN B CB  1 
ATOM   74    C CG  . ASN A 1 26   ? 217.299 181.194 307.204 1.00 83.97  ? 9    ASN B CG  1 
ATOM   75    O OD1 . ASN A 1 26   ? 216.655 180.150 307.307 1.00 83.97  ? 9    ASN B OD1 1 
ATOM   76    N ND2 . ASN A 1 26   ? 218.479 181.250 306.599 1.00 83.97  ? 9    ASN B ND2 1 
ATOM   77    N N   . TYR A 1 27   ? 214.388 183.651 308.564 1.00 80.03  ? 10   TYR B N   1 
ATOM   78    C CA  . TYR A 1 27   ? 213.462 184.509 309.296 1.00 80.03  ? 10   TYR B CA  1 
ATOM   79    C C   . TYR A 1 27   ? 213.850 184.733 310.752 1.00 80.03  ? 10   TYR B C   1 
ATOM   80    O O   . TYR A 1 27   ? 213.702 185.843 311.271 1.00 80.03  ? 10   TYR B O   1 
ATOM   81    C CB  . TYR A 1 27   ? 212.041 183.950 309.255 1.00 80.03  ? 10   TYR B CB  1 
ATOM   82    C CG  . TYR A 1 27   ? 211.052 184.862 309.948 1.00 80.03  ? 10   TYR B CG  1 
ATOM   83    C CD1 . TYR A 1 27   ? 210.563 185.994 309.315 1.00 80.03  ? 10   TYR B CD1 1 
ATOM   84    C CD2 . TYR A 1 27   ? 210.636 184.610 311.246 1.00 80.03  ? 10   TYR B CD2 1 
ATOM   85    C CE1 . TYR A 1 27   ? 209.669 186.835 309.948 1.00 80.03  ? 10   TYR B CE1 1 
ATOM   86    C CE2 . TYR A 1 27   ? 209.743 185.444 311.887 1.00 80.03  ? 10   TYR B CE2 1 
ATOM   87    C CZ  . TYR A 1 27   ? 209.264 186.555 311.234 1.00 80.03  ? 10   TYR B CZ  1 
ATOM   88    O OH  . TYR A 1 27   ? 208.375 187.389 311.868 1.00 80.03  ? 10   TYR B OH  1 
ATOM   89    N N   . LYS A 1 28   ? 214.340 183.693 311.424 1.00 83.28  ? 11   LYS B N   1 
ATOM   90    C CA  . LYS A 1 28   ? 214.505 183.723 312.871 1.00 83.28  ? 11   LYS B CA  1 
ATOM   91    C C   . LYS A 1 28   ? 215.903 184.143 313.300 1.00 83.28  ? 11   LYS B C   1 
ATOM   92    O O   . LYS A 1 28   ? 216.334 183.798 314.406 1.00 83.28  ? 11   LYS B O   1 
ATOM   93    C CB  . LYS A 1 28   ? 214.146 182.362 313.469 1.00 83.28  ? 11   LYS B CB  1 
ATOM   94    C CG  . LYS A 1 28   ? 214.500 181.179 312.592 1.00 83.28  ? 11   LYS B CG  1 
ATOM   95    C CD  . LYS A 1 28   ? 213.843 179.918 313.117 1.00 83.28  ? 11   LYS B CD  1 
ATOM   96    C CE  . LYS A 1 28   ? 212.341 179.956 312.885 1.00 83.28  ? 11   LYS B CE  1 
ATOM   97    N NZ  . LYS A 1 28   ? 211.689 178.666 313.234 1.00 83.28  ? 11   LYS B NZ  1 
ATOM   98    N N   . ASP A 1 29   ? 216.613 184.881 312.454 1.00 83.86  ? 12   ASP B N   1 
ATOM   99    C CA  . ASP A 1 29   ? 217.891 185.447 312.837 1.00 83.86  ? 12   ASP B CA  1 
ATOM   100   C C   . ASP A 1 29   ? 217.672 186.535 313.888 1.00 83.86  ? 12   ASP B C   1 
ATOM   101   O O   . ASP A 1 29   ? 216.561 187.051 314.034 1.00 83.86  ? 12   ASP B O   1 
ATOM   102   C CB  . ASP A 1 29   ? 218.599 185.995 311.600 1.00 83.86  ? 12   ASP B CB  1 
ATOM   103   C CG  . ASP A 1 29   ? 218.672 184.978 310.480 1.00 83.86  ? 12   ASP B CG  1 
ATOM   104   O OD1 . ASP A 1 29   ? 217.678 184.253 310.276 1.00 83.86  ? 12   ASP B OD1 1 
ATOM   105   O OD2 . ASP A 1 29   ? 219.718 184.907 309.802 1.00 83.86  ? 12   ASP B OD2 1 
ATOM   106   N N   . PRO A 1 30   ? 218.718 186.897 314.648 1.00 85.21  ? 13   PRO B N   1 
ATOM   107   C CA  . PRO A 1 30   ? 218.515 187.797 315.793 1.00 85.21  ? 13   PRO B CA  1 
ATOM   108   C C   . PRO A 1 30   ? 218.060 189.198 315.416 1.00 85.21  ? 13   PRO B C   1 
ATOM   109   O O   . PRO A 1 30   ? 217.811 189.503 314.246 1.00 85.21  ? 13   PRO B O   1 
ATOM   110   C CB  . PRO A 1 30   ? 219.894 187.828 316.464 1.00 85.21  ? 13   PRO B CB  1 
ATOM   111   C CG  . PRO A 1 30   ? 220.846 187.468 315.393 1.00 85.21  ? 13   PRO B CG  1 
ATOM   112   C CD  . PRO A 1 30   ? 220.126 186.481 314.530 1.00 85.21  ? 13   PRO B CD  1 
ATOM   113   N N   . VAL A 1 31   ? 217.963 190.059 316.426 1.00 84.32  ? 14   VAL B N   1 
ATOM   114   C CA  . VAL A 1 31   ? 217.349 191.378 316.327 1.00 84.32  ? 14   VAL B CA  1 
ATOM   115   C C   . VAL A 1 31   ? 218.432 192.439 316.170 1.00 84.32  ? 14   VAL B C   1 
ATOM   116   O O   . VAL A 1 31   ? 218.270 193.575 316.627 1.00 84.32  ? 14   VAL B O   1 
ATOM   117   C CB  . VAL A 1 31   ? 216.460 191.664 317.549 1.00 84.32  ? 14   VAL B CB  1 
ATOM   118   C CG1 . VAL A 1 31   ? 215.119 190.971 317.394 1.00 84.32  ? 14   VAL B CG1 1 
ATOM   119   C CG2 . VAL A 1 31   ? 217.149 191.203 318.819 1.00 84.32  ? 14   VAL B CG2 1 
ATOM   120   N N   . ASN A 1 32   ? 219.541 192.059 315.525 1.00 86.63  ? 15   ASN B N   1 
ATOM   121   C CA  . ASN A 1 32   ? 220.808 192.788 315.491 1.00 86.63  ? 15   ASN B CA  1 
ATOM   122   C C   . ASN A 1 32   ? 220.673 194.305 315.505 1.00 86.63  ? 15   ASN B C   1 
ATOM   123   O O   . ASN A 1 32   ? 221.244 194.968 316.377 1.00 86.63  ? 15   ASN B O   1 
ATOM   124   C CB  . ASN A 1 32   ? 221.592 192.379 314.242 1.00 86.63  ? 15   ASN B CB  1 
ATOM   125   C CG  . ASN A 1 32   ? 223.019 191.992 314.550 1.00 86.63  ? 15   ASN B CG  1 
ATOM   126   O OD1 . ASN A 1 32   ? 223.529 192.268 315.635 1.00 86.63  ? 15   ASN B OD1 1 
ATOM   127   N ND2 . ASN A 1 32   ? 223.676 191.353 313.592 1.00 86.63  ? 15   ASN B ND2 1 
ATOM   128   N N   . GLY A 1 33   ? 219.928 194.869 314.563 1.00 83.28  ? 16   GLY B N   1 
ATOM   129   C CA  . GLY A 1 33   ? 219.711 196.301 314.585 1.00 83.28  ? 16   GLY B CA  1 
ATOM   130   C C   . GLY A 1 33   ? 220.057 197.028 313.304 1.00 83.28  ? 16   GLY B C   1 
ATOM   131   O O   . GLY A 1 33   ? 219.736 198.210 313.159 1.00 83.28  ? 16   GLY B O   1 
ATOM   132   N N   . VAL A 1 34   ? 220.712 196.345 312.364 1.00 80.66  ? 17   VAL B N   1 
ATOM   133   C CA  . VAL A 1 34   ? 221.110 196.947 311.101 1.00 80.66  ? 17   VAL B CA  1 
ATOM   134   C C   . VAL A 1 34   ? 220.419 196.294 309.910 1.00 80.66  ? 17   VAL B C   1 
ATOM   135   O O   . VAL A 1 34   ? 220.020 196.986 308.968 1.00 80.66  ? 17   VAL B O   1 
ATOM   136   C CB  . VAL A 1 34   ? 222.648 196.929 310.926 1.00 80.66  ? 17   VAL B CB  1 
ATOM   137   C CG1 . VAL A 1 34   ? 223.320 197.547 312.139 1.00 80.66  ? 17   VAL B CG1 1 
ATOM   138   C CG2 . VAL A 1 34   ? 223.172 195.519 310.709 1.00 80.66  ? 17   VAL B CG2 1 
ATOM   139   N N   . ASP A 1 35   ? 220.252 194.972 309.929 1.00 79.78  ? 18   ASP B N   1 
ATOM   140   C CA  . ASP A 1 35   ? 219.653 194.253 308.813 1.00 79.78  ? 18   ASP B CA  1 
ATOM   141   C C   . ASP A 1 35   ? 218.387 193.501 309.181 1.00 79.78  ? 18   ASP B C   1 
ATOM   142   O O   . ASP A 1 35   ? 217.568 193.233 308.301 1.00 79.78  ? 18   ASP B O   1 
ATOM   143   C CB  . ASP A 1 35   ? 220.660 193.263 308.216 1.00 79.78  ? 18   ASP B CB  1 
ATOM   144   C CG  . ASP A 1 35   ? 221.413 192.486 309.276 1.00 79.78  ? 18   ASP B CG  1 
ATOM   145   O OD1 . ASP A 1 35   ? 220.877 192.324 310.393 1.00 79.78  ? 18   ASP B OD1 1 
ATOM   146   O OD2 . ASP A 1 35   ? 222.542 192.034 308.994 1.00 79.78  ? 18   ASP B OD2 1 
ATOM   147   N N   . ILE A 1 36   ? 218.219 193.144 310.452 1.00 75.61  ? 19   ILE B N   1 
ATOM   148   C CA  . ILE A 1 36   ? 217.048 192.434 310.956 1.00 75.61  ? 19   ILE B CA  1 
ATOM   149   C C   . ILE A 1 36   ? 216.745 193.014 312.328 1.00 75.61  ? 19   ILE B C   1 
ATOM   150   O O   . ILE A 1 36   ? 217.496 192.771 313.278 1.00 75.61  ? 19   ILE B O   1 
ATOM   151   C CB  . ILE A 1 36   ? 217.280 190.918 311.057 1.00 75.61  ? 19   ILE B CB  1 
ATOM   152   C CG1 . ILE A 1 36   ? 217.650 190.321 309.696 1.00 75.61  ? 19   ILE B CG1 1 
ATOM   153   C CG2 . ILE A 1 36   ? 216.086 190.229 311.677 1.00 75.61  ? 19   ILE B CG2 1 
ATOM   154   C CD1 . ILE A 1 36   ? 217.537 188.818 309.636 1.00 75.61  ? 19   ILE B CD1 1 
ATOM   155   N N   . ALA A 1 37   ? 215.659 193.773 312.448 1.00 73.98  ? 20   ALA B N   1 
ATOM   156   C CA  . ALA A 1 37   ? 215.419 194.399 313.740 1.00 73.98  ? 20   ALA B CA  1 
ATOM   157   C C   . ALA A 1 37   ? 213.948 194.741 313.895 1.00 73.98  ? 20   ALA B C   1 
ATOM   158   O O   . ALA A 1 37   ? 213.192 194.781 312.924 1.00 73.98  ? 20   ALA B O   1 
ATOM   159   C CB  . ALA A 1 37   ? 216.272 195.655 313.917 1.00 73.98  ? 20   ALA B CB  1 
ATOM   160   N N   . TYR A 1 38   ? 213.554 194.982 315.139 1.00 79.38  ? 21   TYR B N   1 
ATOM   161   C CA  . TYR A 1 38   ? 212.211 195.461 315.419 1.00 79.38  ? 21   TYR B CA  1 
ATOM   162   C C   . TYR A 1 38   ? 212.127 196.930 315.037 1.00 79.38  ? 21   TYR B C   1 
ATOM   163   O O   . TYR A 1 38   ? 212.989 197.727 315.419 1.00 79.38  ? 21   TYR B O   1 
ATOM   164   C CB  . TYR A 1 38   ? 211.864 195.267 316.893 1.00 79.38  ? 21   TYR B CB  1 
ATOM   165   C CG  . TYR A 1 38   ? 211.397 193.871 317.246 1.00 79.38  ? 21   TYR B CG  1 
ATOM   166   C CD1 . TYR A 1 38   ? 211.917 192.757 316.600 1.00 79.38  ? 21   TYR B CD1 1 
ATOM   167   C CD2 . TYR A 1 38   ? 210.433 193.668 318.223 1.00 79.38  ? 21   TYR B CD2 1 
ATOM   168   C CE1 . TYR A 1 38   ? 211.495 191.486 316.918 1.00 79.38  ? 21   TYR B CE1 1 
ATOM   169   C CE2 . TYR A 1 38   ? 210.004 192.399 318.548 1.00 79.38  ? 21   TYR B CE2 1 
ATOM   170   C CZ  . TYR A 1 38   ? 210.539 191.312 317.892 1.00 79.38  ? 21   TYR B CZ  1 
ATOM   171   O OH  . TYR A 1 38   ? 210.115 190.043 318.211 1.00 79.38  ? 21   TYR B OH  1 
ATOM   172   N N   . ILE A 1 39   ? 211.111 197.281 314.254 1.00 74.66  ? 22   ILE B N   1 
ATOM   173   C CA  . ILE A 1 39   ? 210.943 198.634 313.751 1.00 74.66  ? 22   ILE B CA  1 
ATOM   174   C C   . ILE A 1 39   ? 209.540 199.108 314.093 1.00 74.66  ? 22   ILE B C   1 
ATOM   175   O O   . ILE A 1 39   ? 208.630 198.315 314.353 1.00 74.66  ? 22   ILE B O   1 
ATOM   176   C CB  . ILE A 1 39   ? 211.195 198.728 312.232 1.00 74.66  ? 22   ILE B CB  1 
ATOM   177   C CG1 . ILE A 1 39   ? 209.911 198.461 311.452 1.00 74.66  ? 22   ILE B CG1 1 
ATOM   178   C CG2 . ILE A 1 39   ? 212.255 197.742 311.808 1.00 74.66  ? 22   ILE B CG2 1 
ATOM   179   C CD1 . ILE A 1 39   ? 209.991 198.882 310.010 1.00 74.66  ? 22   ILE B CD1 1 
ATOM   180   N N   . LYS A 1 40   ? 209.381 200.429 314.111 1.00 76.06  ? 23   LYS B N   1 
ATOM   181   C CA  . LYS A 1 40   ? 208.089 201.064 314.364 1.00 76.06  ? 23   LYS B CA  1 
ATOM   182   C C   . LYS A 1 40   ? 207.801 202.042 313.229 1.00 76.06  ? 23   LYS B C   1 
ATOM   183   O O   . LYS A 1 40   ? 208.290 203.175 313.243 1.00 76.06  ? 23   LYS B O   1 
ATOM   184   C CB  . LYS A 1 40   ? 208.074 201.776 315.711 1.00 76.06  ? 23   LYS B CB  1 
ATOM   185   C CG  . LYS A 1 40   ? 208.759 201.028 316.836 1.00 76.06  ? 23   LYS B CG  1 
ATOM   186   C CD  . LYS A 1 40   ? 208.238 201.503 318.183 1.00 76.06  ? 23   LYS B CD  1 
ATOM   187   C CE  . LYS A 1 40   ? 208.932 202.778 318.632 1.00 76.06  ? 23   LYS B CE  1 
ATOM   188   N NZ  . LYS A 1 40   ? 209.143 202.817 320.105 1.00 76.06  ? 23   LYS B NZ  1 
ATOM   189   N N   . ILE A 1 41   ? 206.999 201.616 312.259 1.00 78.19  ? 24   ILE B N   1 
ATOM   190   C CA  . ILE A 1 41   ? 206.621 202.476 311.140 1.00 78.19  ? 24   ILE B CA  1 
ATOM   191   C C   . ILE A 1 41   ? 205.680 203.559 311.652 1.00 78.19  ? 24   ILE B C   1 
ATOM   192   O O   . ILE A 1 41   ? 205.075 203.392 312.720 1.00 78.19  ? 24   ILE B O   1 
ATOM   193   C CB  . ILE A 1 41   ? 205.966 201.671 310.006 1.00 78.19  ? 24   ILE B CB  1 
ATOM   194   C CG1 . ILE A 1 41   ? 204.804 200.839 310.543 1.00 78.19  ? 24   ILE B CG1 1 
ATOM   195   C CG2 . ILE A 1 41   ? 206.989 200.786 309.325 1.00 78.19  ? 24   ILE B CG2 1 
ATOM   196   C CD1 . ILE A 1 41   ? 203.805 200.444 309.483 1.00 78.19  ? 24   ILE B CD1 1 
ATOM   197   N N   . PRO A 1 42   ? 205.540 204.683 310.952 1.00 80.80  ? 25   PRO B N   1 
ATOM   198   C CA  . PRO A 1 42   ? 204.565 205.692 311.378 1.00 80.80  ? 25   PRO B CA  1 
ATOM   199   C C   . PRO A 1 42   ? 203.153 205.130 311.359 1.00 80.80  ? 25   PRO B C   1 
ATOM   200   O O   . PRO A 1 42   ? 202.810 204.280 310.536 1.00 80.80  ? 25   PRO B O   1 
ATOM   201   C CB  . PRO A 1 42   ? 204.728 206.818 310.349 1.00 80.80  ? 25   PRO B CB  1 
ATOM   202   C CG  . PRO A 1 42   ? 205.633 206.298 309.293 1.00 80.80  ? 25   PRO B CG  1 
ATOM   203   C CD  . PRO A 1 42   ? 206.386 205.146 309.842 1.00 80.80  ? 25   PRO B CD  1 
ATOM   204   N N   . ASN A 1 43   ? 202.332 205.612 312.287 1.00 88.36  ? 26   ASN B N   1 
ATOM   205   C CA  . ASN A 1 43   ? 200.960 205.143 312.408 1.00 88.36  ? 26   ASN B CA  1 
ATOM   206   C C   . ASN A 1 43   ? 200.132 206.222 313.090 1.00 88.36  ? 26   ASN B C   1 
ATOM   207   O O   . ASN A 1 43   ? 200.666 207.181 313.651 1.00 88.36  ? 26   ASN B O   1 
ATOM   208   C CB  . ASN A 1 43   ? 200.887 203.825 313.180 1.00 88.36  ? 26   ASN B CB  1 
ATOM   209   C CG  . ASN A 1 43   ? 201.474 203.936 314.566 1.00 88.36  ? 26   ASN B CG  1 
ATOM   210   O OD1 . ASN A 1 43   ? 202.566 204.470 314.747 1.00 88.36  ? 26   ASN B OD1 1 
ATOM   211   N ND2 . ASN A 1 43   ? 200.747 203.440 315.558 1.00 88.36  ? 26   ASN B ND2 1 
ATOM   212   N N   . ALA A 1 44   ? 198.809 206.053 313.022 1.00 97.16  ? 27   ALA B N   1 
ATOM   213   C CA  . ALA A 1 44   ? 197.903 207.047 313.587 1.00 97.16  ? 27   ALA B CA  1 
ATOM   214   C C   . ALA A 1 44   ? 198.037 207.134 315.103 1.00 97.16  ? 27   ALA B C   1 
ATOM   215   O O   . ALA A 1 44   ? 198.063 208.233 315.668 1.00 97.16  ? 27   ALA B O   1 
ATOM   216   C CB  . ALA A 1 44   ? 196.462 206.725 313.194 1.00 97.16  ? 27   ALA B CB  1 
ATOM   217   N N   . GLY A 1 45   ? 198.122 205.991 315.777 1.00 95.84  ? 28   GLY B N   1 
ATOM   218   C CA  . GLY A 1 45   ? 198.202 205.982 317.225 1.00 95.84  ? 28   GLY B CA  1 
ATOM   219   C C   . GLY A 1 45   ? 199.470 205.348 317.757 1.00 95.84  ? 28   GLY B C   1 
ATOM   220   O O   . GLY A 1 45   ? 200.575 205.818 317.470 1.00 95.84  ? 28   GLY B O   1 
ATOM   221   N N   . GLN A 1 46   ? 199.322 204.281 318.538 1.00 95.37  ? 29   GLN B N   1 
ATOM   222   C CA  . GLN A 1 46   ? 200.445 203.541 319.095 1.00 95.37  ? 29   GLN B CA  1 
ATOM   223   C C   . GLN A 1 46   ? 200.412 202.116 318.564 1.00 95.37  ? 29   GLN B C   1 
ATOM   224   O O   . GLN A 1 46   ? 199.364 201.463 318.594 1.00 95.37  ? 29   GLN B O   1 
ATOM   225   C CB  . GLN A 1 46   ? 200.405 203.539 320.625 1.00 95.37  ? 29   GLN B CB  1 
ATOM   226   C CG  . GLN A 1 46   ? 201.652 202.966 321.280 1.00 95.37  ? 29   GLN B CG  1 
ATOM   227   C CD  . GLN A 1 46   ? 201.422 201.589 321.871 1.00 95.37  ? 29   GLN B CD  1 
ATOM   228   O OE1 . GLN A 1 46   ? 200.738 200.753 321.282 1.00 95.37  ? 29   GLN B OE1 1 
ATOM   229   N NE2 . GLN A 1 46   ? 201.996 201.347 323.043 1.00 95.37  ? 29   GLN B NE2 1 
ATOM   230   N N   . MET A 1 47   ? 201.556 201.639 318.081 1.00 88.00  ? 30   MET B N   1 
ATOM   231   C CA  . MET A 1 47   ? 201.661 200.309 317.498 1.00 88.00  ? 30   MET B CA  1 
ATOM   232   C C   . MET A 1 47   ? 202.829 199.557 318.118 1.00 88.00  ? 30   MET B C   1 
ATOM   233   O O   . MET A 1 47   ? 203.885 200.136 318.387 1.00 88.00  ? 30   MET B O   1 
ATOM   234   C CB  . MET A 1 47   ? 201.812 200.391 315.970 1.00 88.00  ? 30   MET B CB  1 
ATOM   235   C CG  . MET A 1 47   ? 203.153 200.912 315.479 1.00 88.00  ? 30   MET B CG  1 
ATOM   236   S SD  . MET A 1 47   ? 203.552 200.347 313.815 1.00 88.00  ? 30   MET B SD  1 
ATOM   237   C CE  . MET A 1 47   ? 204.729 199.048 314.157 1.00 88.00  ? 30   MET B CE  1 
ATOM   238   N N   . GLN A 1 48   ? 202.618 198.269 318.363 1.00 86.91  ? 31   GLN B N   1 
ATOM   239   C CA  . GLN A 1 48   ? 203.682 197.429 318.885 1.00 86.91  ? 31   GLN B CA  1 
ATOM   240   C C   . GLN A 1 48   ? 204.779 197.271 317.835 1.00 86.91  ? 31   GLN B C   1 
ATOM   241   O O   . GLN A 1 48   ? 204.482 197.116 316.648 1.00 86.91  ? 31   GLN B O   1 
ATOM   242   C CB  . GLN A 1 48   ? 203.130 196.059 319.281 1.00 86.91  ? 31   GLN B CB  1 
ATOM   243   C CG  . GLN A 1 48   ? 204.185 195.042 319.680 1.00 86.91  ? 31   GLN B CG  1 
ATOM   244   C CD  . GLN A 1 48   ? 203.601 193.864 320.430 1.00 86.91  ? 31   GLN B CD  1 
ATOM   245   O OE1 . GLN A 1 48   ? 204.332 193.042 320.983 1.00 86.91  ? 31   GLN B OE1 1 
ATOM   246   N NE2 . GLN A 1 48   ? 202.277 193.773 320.451 1.00 86.91  ? 31   GLN B NE2 1 
ATOM   247   N N   . PRO A 1 49   ? 206.049 197.318 318.235 1.00 81.83  ? 32   PRO B N   1 
ATOM   248   C CA  . PRO A 1 49   ? 207.134 197.142 317.263 1.00 81.83  ? 32   PRO B CA  1 
ATOM   249   C C   . PRO A 1 49   ? 207.017 195.814 316.531 1.00 81.83  ? 32   PRO B C   1 
ATOM   250   O O   . PRO A 1 49   ? 206.680 194.785 317.119 1.00 81.83  ? 32   PRO B O   1 
ATOM   251   C CB  . PRO A 1 49   ? 208.394 197.194 318.131 1.00 81.83  ? 32   PRO B CB  1 
ATOM   252   C CG  . PRO A 1 49   ? 207.996 198.000 319.314 1.00 81.83  ? 32   PRO B CG  1 
ATOM   253   C CD  . PRO A 1 49   ? 206.555 197.677 319.571 1.00 81.83  ? 32   PRO B CD  1 
ATOM   254   N N   . VAL A 1 50   ? 207.308 195.844 315.235 1.00 75.99  ? 33   VAL B N   1 
ATOM   255   C CA  . VAL A 1 50   ? 207.155 194.685 314.367 1.00 75.99  ? 33   VAL B CA  1 
ATOM   256   C C   . VAL A 1 50   ? 208.508 194.358 313.754 1.00 75.99  ? 33   VAL B C   1 
ATOM   257   O O   . VAL A 1 50   ? 209.268 195.260 313.394 1.00 75.99  ? 33   VAL B O   1 
ATOM   258   C CB  . VAL A 1 50   ? 206.094 194.939 313.276 1.00 75.99  ? 33   VAL B CB  1 
ATOM   259   C CG1 . VAL A 1 50   ? 206.417 196.198 312.493 1.00 75.99  ? 33   VAL B CG1 1 
ATOM   260   C CG2 . VAL A 1 50   ? 205.980 193.745 312.358 1.00 75.99  ? 33   VAL B CG2 1 
ATOM   261   N N   . LYS A 1 51   ? 208.824 193.069 313.666 1.00 71.58  ? 34   LYS B N   1 
ATOM   262   C CA  . LYS A 1 51   ? 210.120 192.651 313.148 1.00 71.58  ? 34   LYS B CA  1 
ATOM   263   C C   . LYS A 1 51   ? 210.183 192.888 311.644 1.00 71.58  ? 34   LYS B C   1 
ATOM   264   O O   . LYS A 1 51   ? 209.374 192.339 310.891 1.00 71.58  ? 34   LYS B O   1 
ATOM   265   C CB  . LYS A 1 51   ? 210.357 191.180 313.468 1.00 71.58  ? 34   LYS B CB  1 
ATOM   266   C CG  . LYS A 1 51   ? 211.812 190.771 313.459 1.00 71.58  ? 34   LYS B CG  1 
ATOM   267   C CD  . LYS A 1 51   ? 211.985 189.388 314.047 1.00 71.58  ? 34   LYS B CD  1 
ATOM   268   C CE  . LYS A 1 51   ? 213.406 188.894 313.886 1.00 71.58  ? 34   LYS B CE  1 
ATOM   269   N NZ  . LYS A 1 51   ? 213.561 187.512 314.413 1.00 71.58  ? 34   LYS B NZ  1 
ATOM   270   N N   . ALA A 1 52   ? 211.145 193.699 311.203 1.00 70.36  ? 35   ALA B N   1 
ATOM   271   C CA  . ALA A 1 52   ? 211.324 194.020 309.796 1.00 70.36  ? 35   ALA B CA  1 
ATOM   272   C C   . ALA A 1 52   ? 212.780 193.826 309.406 1.00 70.36  ? 35   ALA B C   1 
ATOM   273   O O   . ALA A 1 52   ? 213.691 194.082 310.205 1.00 70.36  ? 35   ALA B O   1 
ATOM   274   C CB  . ALA A 1 52   ? 210.898 195.450 309.492 1.00 70.36  ? 35   ALA B CB  1 
ATOM   275   N N   . PHE A 1 53   ? 212.994 193.344 308.183 1.00 69.60  ? 36   PHE B N   1 
ATOM   276   C CA  . PHE A 1 53   ? 214.328 193.015 307.701 1.00 69.60  ? 36   PHE B CA  1 
ATOM   277   C C   . PHE A 1 53   ? 214.656 193.896 306.508 1.00 69.60  ? 36   PHE B C   1 
ATOM   278   O O   . PHE A 1 53   ? 213.860 193.998 305.572 1.00 69.60  ? 36   PHE B O   1 
ATOM   279   C CB  . PHE A 1 53   ? 214.472 191.538 307.293 1.00 69.60  ? 36   PHE B CB  1 
ATOM   280   C CG  . PHE A 1 53   ? 213.890 190.533 308.268 1.00 69.60  ? 36   PHE B CG  1 
ATOM   281   C CD1 . PHE A 1 53   ? 213.485 190.879 309.541 1.00 69.60  ? 36   PHE B CD1 1 
ATOM   282   C CD2 . PHE A 1 53   ? 213.796 189.212 307.901 1.00 69.60  ? 36   PHE B CD2 1 
ATOM   283   C CE1 . PHE A 1 53   ? 212.960 189.943 310.399 1.00 69.60  ? 36   PHE B CE1 1 
ATOM   284   C CE2 . PHE A 1 53   ? 213.279 188.267 308.761 1.00 69.60  ? 36   PHE B CE2 1 
ATOM   285   C CZ  . PHE A 1 53   ? 212.863 188.635 310.012 1.00 69.60  ? 36   PHE B CZ  1 
ATOM   286   N N   . LYS A 1 54   ? 215.825 194.525 306.540 1.00 69.60  ? 37   LYS B N   1 
ATOM   287   C CA  . LYS A 1 54   ? 216.269 195.349 305.425 1.00 69.60  ? 37   LYS B CA  1 
ATOM   288   C C   . LYS A 1 54   ? 216.930 194.465 304.379 1.00 69.60  ? 37   LYS B C   1 
ATOM   289   O O   . LYS A 1 54   ? 217.805 193.659 304.703 1.00 69.60  ? 37   LYS B O   1 
ATOM   290   C CB  . LYS A 1 54   ? 217.240 196.424 305.909 1.00 69.60  ? 37   LYS B CB  1 
ATOM   291   C CG  . LYS A 1 54   ? 218.386 196.713 304.957 1.00 69.60  ? 37   LYS B CG  1 
ATOM   292   C CD  . LYS A 1 54   ? 219.207 197.896 305.434 1.00 69.60  ? 37   LYS B CD  1 
ATOM   293   C CE  . LYS A 1 54   ? 218.426 199.189 305.316 1.00 69.60  ? 37   LYS B CE  1 
ATOM   294   N NZ  . LYS A 1 54   ? 219.274 200.370 305.620 1.00 69.60  ? 37   LYS B NZ  1 
ATOM   295   N N   . ILE A 1 55   ? 216.506 194.603 303.124 1.00 69.60  ? 38   ILE B N   1 
ATOM   296   C CA  . ILE A 1 55   ? 217.045 193.754 302.069 1.00 69.60  ? 38   ILE B CA  1 
ATOM   297   C C   . ILE A 1 55   ? 218.075 194.467 301.203 1.00 69.60  ? 38   ILE B C   1 
ATOM   298   O O   . ILE A 1 55   ? 218.842 193.795 300.496 1.00 69.60  ? 38   ILE B O   1 
ATOM   299   C CB  . ILE A 1 55   ? 215.921 193.181 301.184 1.00 69.60  ? 38   ILE B CB  1 
ATOM   300   C CG1 . ILE A 1 55   ? 215.366 194.255 300.255 1.00 69.60  ? 38   ILE B CG1 1 
ATOM   301   C CG2 . ILE A 1 55   ? 214.816 192.615 302.040 1.00 69.60  ? 38   ILE B CG2 1 
ATOM   302   C CD1 . ILE A 1 55   ? 214.522 193.700 299.135 1.00 69.60  ? 38   ILE B CD1 1 
ATOM   303   N N   . HIS A 1 56   ? 218.125 195.787 301.238 1.00 69.60  ? 39   HIS B N   1 
ATOM   304   C CA  . HIS A 1 56   ? 219.060 196.571 300.439 1.00 69.60  ? 39   HIS B CA  1 
ATOM   305   C C   . HIS A 1 56   ? 219.060 197.983 301.014 1.00 69.60  ? 39   HIS B C   1 
ATOM   306   O O   . HIS A 1 56   ? 218.490 198.232 302.083 1.00 69.60  ? 39   HIS B O   1 
ATOM   307   C CB  . HIS A 1 56   ? 218.682 196.540 298.958 1.00 69.60  ? 39   HIS B CB  1 
ATOM   308   C CG  . HIS A 1 56   ? 219.820 196.842 298.037 1.00 69.60  ? 39   HIS B CG  1 
ATOM   309   N ND1 . HIS A 1 56   ? 220.822 195.935 297.772 1.00 69.60  ? 39   HIS B ND1 1 
ATOM   310   C CD2 . HIS A 1 56   ? 220.117 197.951 297.321 1.00 69.60  ? 39   HIS B CD2 1 
ATOM   311   C CE1 . HIS A 1 56   ? 221.687 196.471 296.930 1.00 69.60  ? 39   HIS B CE1 1 
ATOM   312   N NE2 . HIS A 1 56   ? 221.281 197.694 296.639 1.00 69.60  ? 39   HIS B NE2 1 
ATOM   313   N N   . ASN A 1 57   ? 219.707 198.907 300.316 1.00 69.60  ? 40   ASN B N   1 
ATOM   314   C CA  . ASN A 1 57   ? 219.706 200.293 300.755 1.00 69.60  ? 40   ASN B CA  1 
ATOM   315   C C   . ASN A 1 57   ? 218.297 200.862 300.677 1.00 69.60  ? 40   ASN B C   1 
ATOM   316   O O   . ASN A 1 57   ? 217.660 200.821 299.621 1.00 69.60  ? 40   ASN B O   1 
ATOM   317   C CB  . ASN A 1 57   ? 220.662 201.114 299.897 1.00 69.60  ? 40   ASN B CB  1 
ATOM   318   C CG  . ASN A 1 57   ? 222.093 201.015 300.369 1.00 69.60  ? 40   ASN B CG  1 
ATOM   319   O OD1 . ASN A 1 57   ? 222.959 200.502 299.662 1.00 69.60  ? 40   ASN B OD1 1 
ATOM   320   N ND2 . ASN A 1 57   ? 222.350 201.508 301.574 1.00 69.60  ? 40   ASN B ND2 1 
ATOM   321   N N   . LYS A 1 58   ? 217.811 201.381 301.803 1.00 69.60  ? 41   LYS B N   1 
ATOM   322   C CA  . LYS A 1 58   ? 216.520 202.058 301.895 1.00 69.60  ? 41   LYS B CA  1 
ATOM   323   C C   . LYS A 1 58   ? 215.350 201.170 301.480 1.00 69.60  ? 41   LYS B C   1 
ATOM   324   O O   . LYS A 1 58   ? 214.304 201.679 301.070 1.00 69.60  ? 41   LYS B O   1 
ATOM   325   C CB  . LYS A 1 58   ? 216.512 203.347 301.064 1.00 69.60  ? 41   LYS B CB  1 
ATOM   326   C CG  . LYS A 1 58   ? 217.773 204.191 301.179 1.00 69.60  ? 41   LYS B CG  1 
ATOM   327   C CD  . LYS A 1 58   ? 217.897 204.816 302.555 1.00 69.60  ? 41   LYS B CD  1 
ATOM   328   C CE  . LYS A 1 58   ? 219.208 205.565 302.708 1.00 69.60  ? 41   LYS B CE  1 
ATOM   329   N NZ  . LYS A 1 58   ? 220.367 204.643 302.853 1.00 69.60  ? 41   LYS B NZ  1 
ATOM   330   N N   . ILE A 1 59   ? 215.490 199.850 301.572 1.00 69.60  ? 42   ILE B N   1 
ATOM   331   C CA  . ILE A 1 59   ? 214.409 198.927 301.243 1.00 69.60  ? 42   ILE B CA  1 
ATOM   332   C C   . ILE A 1 59   ? 214.233 197.958 302.403 1.00 69.60  ? 42   ILE B C   1 
ATOM   333   O O   . ILE A 1 59   ? 215.144 197.177 302.710 1.00 69.60  ? 42   ILE B O   1 
ATOM   334   C CB  . ILE A 1 59   ? 214.672 198.158 299.938 1.00 69.60  ? 42   ILE B CB  1 
ATOM   335   C CG1 . ILE A 1 59   ? 214.913 199.126 298.781 1.00 69.60  ? 42   ILE B CG1 1 
ATOM   336   C CG2 . ILE A 1 59   ? 213.502 197.254 299.618 1.00 69.60  ? 42   ILE B CG2 1 
ATOM   337   C CD1 . ILE A 1 59   ? 214.982 198.453 297.431 1.00 69.60  ? 42   ILE B CD1 1 
ATOM   338   N N   . TRP A 1 60   ? 213.062 197.993 303.030 1.00 69.60  ? 43   TRP B N   1 
ATOM   339   C CA  . TRP A 1 60   ? 212.719 197.100 304.124 1.00 69.60  ? 43   TRP B CA  1 
ATOM   340   C C   . TRP A 1 60   ? 211.543 196.225 303.719 1.00 69.60  ? 43   TRP B C   1 
ATOM   341   O O   . TRP A 1 60   ? 210.710 196.619 302.899 1.00 69.60  ? 43   TRP B O   1 
ATOM   342   C CB  . TRP A 1 60   ? 212.359 197.878 305.390 1.00 69.60  ? 43   TRP B CB  1 
ATOM   343   C CG  . TRP A 1 60   ? 213.519 198.541 306.051 1.00 69.60  ? 43   TRP B CG  1 
ATOM   344   C CD1 . TRP A 1 60   ? 214.067 199.741 305.725 1.00 69.60  ? 43   TRP B CD1 1 
ATOM   345   C CD2 . TRP A 1 60   ? 214.267 198.048 307.167 1.00 69.60  ? 43   TRP B CD2 1 
ATOM   346   N NE1 . TRP A 1 60   ? 215.114 200.027 306.564 1.00 69.60  ? 43   TRP B NE1 1 
ATOM   347   C CE2 . TRP A 1 60   ? 215.257 199.001 307.459 1.00 69.60  ? 43   TRP B CE2 1 
ATOM   348   C CE3 . TRP A 1 60   ? 214.197 196.892 307.947 1.00 69.60  ? 43   TRP B CE3 1 
ATOM   349   C CZ2 . TRP A 1 60   ? 216.170 198.834 308.493 1.00 69.60  ? 43   TRP B CZ2 1 
ATOM   350   C CZ3 . TRP A 1 60   ? 215.104 196.728 308.972 1.00 69.60  ? 43   TRP B CZ3 1 
ATOM   351   C CH2 . TRP A 1 60   ? 216.077 197.692 309.237 1.00 69.60  ? 43   TRP B CH2 1 
ATOM   352   N N   . VAL A 1 61   ? 211.482 195.028 304.294 1.00 69.60  ? 44   VAL B N   1 
ATOM   353   C CA  . VAL A 1 61   ? 210.344 194.136 304.136 1.00 69.60  ? 44   VAL B CA  1 
ATOM   354   C C   . VAL A 1 61   ? 209.835 193.768 305.521 1.00 69.60  ? 44   VAL B C   1 
ATOM   355   O O   . VAL A 1 61   ? 210.625 193.470 306.425 1.00 69.60  ? 44   VAL B O   1 
ATOM   356   C CB  . VAL A 1 61   ? 210.694 192.875 303.322 1.00 69.60  ? 44   VAL B CB  1 
ATOM   357   C CG1 . VAL A 1 61   ? 211.098 193.252 301.914 1.00 69.60  ? 44   VAL B CG1 1 
ATOM   358   C CG2 . VAL A 1 61   ? 211.816 192.123 303.977 1.00 69.60  ? 44   VAL B CG2 1 
ATOM   359   N N   . ILE A 1 62   ? 208.522 193.826 305.692 1.00 69.60  ? 45   ILE B N   1 
ATOM   360   C CA  . ILE A 1 62   ? 207.862 193.501 306.946 1.00 69.60  ? 45   ILE B CA  1 
ATOM   361   C C   . ILE A 1 62   ? 206.914 192.339 306.689 1.00 69.60  ? 45   ILE B C   1 
ATOM   362   O O   . ILE A 1 62   ? 205.786 192.533 306.239 1.00 69.60  ? 45   ILE B O   1 
ATOM   363   C CB  . ILE A 1 62   ? 207.105 194.714 307.514 1.00 69.60  ? 45   ILE B CB  1 
ATOM   364   C CG1 . ILE A 1 62   ? 208.003 195.947 307.538 1.00 69.60  ? 45   ILE B CG1 1 
ATOM   365   C CG2 . ILE A 1 62   ? 206.606 194.418 308.905 1.00 69.60  ? 45   ILE B CG2 1 
ATOM   366   C CD1 . ILE A 1 62   ? 207.314 197.184 308.052 1.00 69.60  ? 45   ILE B CD1 1 
ATOM   367   N N   . PRO A 1 63   ? 207.336 191.110 306.965 1.00 69.60  ? 46   PRO B N   1 
ATOM   368   C CA  . PRO A 1 63   ? 206.470 189.960 306.680 1.00 69.60  ? 46   PRO B CA  1 
ATOM   369   C C   . PRO A 1 63   ? 205.294 189.877 307.638 1.00 69.60  ? 46   PRO B C   1 
ATOM   370   O O   . PRO A 1 63   ? 205.183 188.926 308.415 1.00 69.60  ? 46   PRO B O   1 
ATOM   371   C CB  . PRO A 1 63   ? 207.409 188.756 306.839 1.00 69.60  ? 46   PRO B CB  1 
ATOM   372   C CG  . PRO A 1 63   ? 208.790 189.325 307.004 1.00 69.60  ? 46   PRO B CG  1 
ATOM   373   C CD  . PRO A 1 63   ? 208.623 190.700 307.541 1.00 69.60  ? 46   PRO B CD  1 
ATOM   374   N N   . GLU A 1 64   ? 204.412 190.872 307.591 1.00 70.68  ? 47   GLU B N   1 
ATOM   375   C CA  . GLU A 1 64   ? 203.221 190.895 308.425 1.00 70.68  ? 47   GLU B CA  1 
ATOM   376   C C   . GLU A 1 64   ? 202.070 191.495 307.634 1.00 70.68  ? 47   GLU B C   1 
ATOM   377   O O   . GLU A 1 64   ? 202.272 192.232 306.665 1.00 70.68  ? 47   GLU B O   1 
ATOM   378   C CB  . GLU A 1 64   ? 203.440 191.692 309.717 1.00 70.68  ? 47   GLU B CB  1 
ATOM   379   C CG  . GLU A 1 64   ? 204.325 191.000 310.734 1.00 70.68  ? 47   GLU B CG  1 
ATOM   380   C CD  . GLU A 1 64   ? 203.598 189.908 311.490 1.00 70.68  ? 47   GLU B CD  1 
ATOM   381   O OE1 . GLU A 1 64   ? 202.350 189.887 311.456 1.00 70.68  ? 47   GLU B OE1 1 
ATOM   382   O OE2 . GLU A 1 64   ? 204.274 189.069 312.122 1.00 70.68  ? 47   GLU B OE2 1 
ATOM   383   N N   . ARG A 1 65   ? 200.855 191.154 308.054 1.00 74.15  ? 48   ARG B N   1 
ATOM   384   C CA  . ARG A 1 65   ? 199.662 191.721 307.445 1.00 74.15  ? 48   ARG B CA  1 
ATOM   385   C C   . ARG A 1 65   ? 199.574 193.208 307.751 1.00 74.15  ? 48   ARG B C   1 
ATOM   386   O O   . ARG A 1 65   ? 199.896 193.650 308.856 1.00 74.15  ? 48   ARG B O   1 
ATOM   387   C CB  . ARG A 1 65   ? 198.414 191.006 307.956 1.00 74.15  ? 48   ARG B CB  1 
ATOM   388   C CG  . ARG A 1 65   ? 198.471 189.501 307.820 1.00 74.15  ? 48   ARG B CG  1 
ATOM   389   C CD  . ARG A 1 65   ? 198.598 189.096 306.367 1.00 74.15  ? 48   ARG B CD  1 
ATOM   390   N NE  . ARG A 1 65   ? 197.517 189.628 305.549 1.00 74.15  ? 48   ARG B NE  1 
ATOM   391   C CZ  . ARG A 1 65   ? 196.296 189.117 305.500 1.00 74.15  ? 48   ARG B CZ  1 
ATOM   392   N NH1 . ARG A 1 65   ? 195.961 188.057 306.216 1.00 74.15  ? 48   ARG B NH1 1 
ATOM   393   N NH2 . ARG A 1 65   ? 195.388 189.680 304.709 1.00 74.15  ? 48   ARG B NH2 1 
ATOM   394   N N   . ASP A 1 66   ? 199.131 193.984 306.767 1.00 80.05  ? 49   ASP B N   1 
ATOM   395   C CA  . ASP A 1 66   ? 199.062 195.435 306.918 1.00 80.05  ? 49   ASP B CA  1 
ATOM   396   C C   . ASP A 1 66   ? 197.799 195.776 307.696 1.00 80.05  ? 49   ASP B C   1 
ATOM   397   O O   . ASP A 1 66   ? 196.724 195.975 307.131 1.00 80.05  ? 49   ASP B O   1 
ATOM   398   C CB  . ASP A 1 66   ? 199.092 196.123 305.560 1.00 80.05  ? 49   ASP B CB  1 
ATOM   399   C CG  . ASP A 1 66   ? 198.930 197.634 305.661 1.00 80.05  ? 49   ASP B CG  1 
ATOM   400   O OD1 . ASP A 1 66   ? 199.008 198.184 306.780 1.00 80.05  ? 49   ASP B OD1 1 
ATOM   401   O OD2 . ASP A 1 66   ? 198.741 198.279 304.610 1.00 80.05  ? 49   ASP B OD2 1 
ATOM   402   N N   . THR A 1 67   ? 197.935 195.842 309.020 1.00 87.14  ? 50   THR B N   1 
ATOM   403   C CA  . THR A 1 67   ? 196.873 196.318 309.898 1.00 87.14  ? 50   THR B CA  1 
ATOM   404   C C   . THR A 1 67   ? 197.321 197.525 310.714 1.00 87.14  ? 50   THR B C   1 
ATOM   405   O O   . THR A 1 67   ? 196.667 197.884 311.697 1.00 87.14  ? 50   THR B O   1 
ATOM   406   C CB  . THR A 1 67   ? 196.394 195.203 310.830 1.00 87.14  ? 50   THR B CB  1 
ATOM   407   O OG1 . THR A 1 67   ? 197.234 195.153 311.989 1.00 87.14  ? 50   THR B OG1 1 
ATOM   408   C CG2 . THR A 1 67   ? 196.433 193.856 310.127 1.00 87.14  ? 50   THR B CG2 1 
ATOM   409   N N   . PHE A 1 68   ? 198.427 198.158 310.324 1.00 89.06  ? 51   PHE B N   1 
ATOM   410   C CA  . PHE A 1 68   ? 199.013 199.265 311.068 1.00 89.06  ? 51   PHE B CA  1 
ATOM   411   C C   . PHE A 1 68   ? 198.769 200.616 310.417 1.00 89.06  ? 51   PHE B C   1 
ATOM   412   O O   . PHE A 1 68   ? 198.281 201.540 311.075 1.00 89.06  ? 51   PHE B O   1 
ATOM   413   C CB  . PHE A 1 68   ? 200.525 199.051 311.231 1.00 89.06  ? 51   PHE B CB  1 
ATOM   414   C CG  . PHE A 1 68   ? 200.922 197.616 311.397 1.00 89.06  ? 51   PHE B CG  1 
ATOM   415   C CD1 . PHE A 1 68   ? 200.466 196.876 312.471 1.00 89.06  ? 51   PHE B CD1 1 
ATOM   416   C CD2 . PHE A 1 68   ? 201.755 197.008 310.476 1.00 89.06  ? 51   PHE B CD2 1 
ATOM   417   C CE1 . PHE A 1 68   ? 200.834 195.557 312.625 1.00 89.06  ? 51   PHE B CE1 1 
ATOM   418   C CE2 . PHE A 1 68   ? 202.125 195.691 310.623 1.00 89.06  ? 51   PHE B CE2 1 
ATOM   419   C CZ  . PHE A 1 68   ? 201.664 194.964 311.699 1.00 89.06  ? 51   PHE B CZ  1 
ATOM   420   N N   . THR A 1 69   ? 199.107 200.755 309.133 1.00 93.26  ? 52   THR B N   1 
ATOM   421   C CA  . THR A 1 69   ? 199.066 202.065 308.490 1.00 93.26  ? 52   THR B CA  1 
ATOM   422   C C   . THR A 1 69   ? 197.653 202.633 308.464 1.00 93.26  ? 52   THR B C   1 
ATOM   423   O O   . THR A 1 69   ? 197.448 203.818 308.750 1.00 93.26  ? 52   THR B O   1 
ATOM   424   C CB  . THR A 1 69   ? 199.628 201.972 307.072 1.00 93.26  ? 52   THR B CB  1 
ATOM   425   O OG1 . THR A 1 69   ? 198.577 201.631 306.161 1.00 93.26  ? 52   THR B OG1 1 
ATOM   426   C CG2 . THR A 1 69   ? 200.713 200.912 306.999 1.00 93.26  ? 52   THR B CG2 1 
ATOM   427   N N   . ASN A 1 70   ? 196.664 201.804 308.137 1.00 102.09 ? 53   ASN B N   1 
ATOM   428   C CA  . ASN A 1 70   ? 195.292 202.270 308.025 1.00 102.09 ? 53   ASN B CA  1 
ATOM   429   C C   . ASN A 1 70   ? 194.515 201.853 309.263 1.00 102.09 ? 53   ASN B C   1 
ATOM   430   O O   . ASN A 1 70   ? 194.329 200.647 309.486 1.00 102.09 ? 53   ASN B O   1 
ATOM   431   C CB  . ASN A 1 70   ? 194.637 201.705 306.768 1.00 102.09 ? 53   ASN B CB  1 
ATOM   432   C CG  . ASN A 1 70   ? 193.597 202.636 306.186 1.00 102.09 ? 53   ASN B CG  1 
ATOM   433   O OD1 . ASN A 1 70   ? 193.419 203.756 306.660 1.00 102.09 ? 53   ASN B OD1 1 
ATOM   434   N ND2 . ASN A 1 70   ? 192.908 202.179 305.147 1.00 102.09 ? 53   ASN B ND2 1 
ATOM   435   N N   . PRO A 1 71   ? 194.050 202.790 310.093 1.00 106.84 ? 54   PRO B N   1 
ATOM   436   C CA  . PRO A 1 71   ? 193.303 202.386 311.293 1.00 106.84 ? 54   PRO B CA  1 
ATOM   437   C C   . PRO A 1 71   ? 191.951 201.777 310.978 1.00 106.84 ? 54   PRO B C   1 
ATOM   438   O O   . PRO A 1 71   ? 191.449 200.971 311.770 1.00 106.84 ? 54   PRO B O   1 
ATOM   439   C CB  . PRO A 1 71   ? 193.168 203.693 312.082 1.00 106.84 ? 54   PRO B CB  1 
ATOM   440   C CG  . PRO A 1 71   ? 193.255 204.772 311.059 1.00 106.84 ? 54   PRO B CG  1 
ATOM   441   C CD  . PRO A 1 71   ? 194.014 204.245 309.868 1.00 106.84 ? 54   PRO B CD  1 
ATOM   442   N N   . GLU A 1 72   ? 191.342 202.142 309.848 1.00 110.08 ? 55   GLU B N   1 
ATOM   443   C CA  . GLU A 1 72   ? 190.078 201.528 309.457 1.00 110.08 ? 55   GLU B CA  1 
ATOM   444   C C   . GLU A 1 72   ? 190.256 200.045 309.154 1.00 110.08 ? 55   GLU B C   1 
ATOM   445   O O   . GLU A 1 72   ? 189.399 199.226 309.505 1.00 110.08 ? 55   GLU B O   1 
ATOM   446   C CB  . GLU A 1 72   ? 189.493 202.259 308.250 1.00 110.08 ? 55   GLU B CB  1 
ATOM   447   C CG  . GLU A 1 72   ? 189.027 203.675 308.549 1.00 110.08 ? 55   GLU B CG  1 
ATOM   448   C CD  . GLU A 1 72   ? 188.418 204.357 307.340 1.00 110.08 ? 55   GLU B CD  1 
ATOM   449   O OE1 . GLU A 1 72   ? 189.171 204.685 306.399 1.00 110.08 ? 55   GLU B OE1 1 
ATOM   450   O OE2 . GLU A 1 72   ? 187.187 204.565 307.329 1.00 110.08 ? 55   GLU B OE2 1 
ATOM   451   N N   . GLU A 1 73   ? 191.362 199.681 308.504 1.00 105.48 ? 56   GLU B N   1 
ATOM   452   C CA  . GLU A 1 73   ? 191.644 198.289 308.154 1.00 105.48 ? 56   GLU B CA  1 
ATOM   453   C C   . GLU A 1 73   ? 192.270 197.582 309.357 1.00 105.48 ? 56   GLU B C   1 
ATOM   454   O O   . GLU A 1 73   ? 193.457 197.252 309.389 1.00 105.48 ? 56   GLU B O   1 
ATOM   455   C CB  . GLU A 1 73   ? 192.548 198.219 306.932 1.00 105.48 ? 56   GLU B CB  1 
ATOM   456   C CG  . GLU A 1 73   ? 192.578 196.859 306.249 1.00 105.48 ? 56   GLU B CG  1 
ATOM   457   C CD  . GLU A 1 73   ? 191.785 196.837 304.956 1.00 105.48 ? 56   GLU B CD  1 
ATOM   458   O OE1 . GLU A 1 73   ? 191.579 197.916 304.363 1.00 105.48 ? 56   GLU B OE1 1 
ATOM   459   O OE2 . GLU A 1 73   ? 191.368 195.741 304.531 1.00 105.48 ? 56   GLU B OE2 1 
ATOM   460   N N   . GLY A 1 74   ? 191.437 197.356 310.369 1.00 111.64 ? 57   GLY B N   1 
ATOM   461   C CA  . GLY A 1 74   ? 191.878 196.659 311.561 1.00 111.64 ? 57   GLY B CA  1 
ATOM   462   C C   . GLY A 1 74   ? 191.400 195.223 311.635 1.00 111.64 ? 57   GLY B C   1 
ATOM   463   O O   . GLY A 1 74   ? 191.806 194.473 312.529 1.00 111.64 ? 57   GLY B O   1 
ATOM   464   N N   . ASP A 1 75   ? 190.542 194.826 310.700 1.00 106.64 ? 58   ASP B N   1 
ATOM   465   C CA  . ASP A 1 75   ? 189.947 193.500 310.686 1.00 106.64 ? 58   ASP B CA  1 
ATOM   466   C C   . ASP A 1 75   ? 190.361 192.753 309.426 1.00 106.64 ? 58   ASP B C   1 
ATOM   467   O O   . ASP A 1 75   ? 190.696 193.353 308.402 1.00 106.64 ? 58   ASP B O   1 
ATOM   468   C CB  . ASP A 1 75   ? 188.418 193.577 310.766 1.00 106.64 ? 58   ASP B CB  1 
ATOM   469   C CG  . ASP A 1 75   ? 187.790 194.015 309.459 1.00 106.64 ? 58   ASP B CG  1 
ATOM   470   O OD1 . ASP A 1 75   ? 187.758 195.235 309.195 1.00 106.64 ? 58   ASP B OD1 1 
ATOM   471   O OD2 . ASP A 1 75   ? 187.331 193.140 308.695 1.00 106.64 ? 58   ASP B OD2 1 
ATOM   472   N N   . LEU A 1 76   ? 190.332 191.425 309.515 1.00 97.01  ? 59   LEU B N   1 
ATOM   473   C CA  . LEU A 1 76   ? 190.738 190.559 308.417 1.00 97.01  ? 59   LEU B CA  1 
ATOM   474   C C   . LEU A 1 76   ? 189.583 189.762 307.827 1.00 97.01  ? 59   LEU B C   1 
ATOM   475   O O   . LEU A 1 76   ? 189.814 188.907 306.966 1.00 97.01  ? 59   LEU B O   1 
ATOM   476   C CB  . LEU A 1 76   ? 191.841 189.600 308.882 1.00 97.01  ? 59   LEU B CB  1 
ATOM   477   C CG  . LEU A 1 76   ? 193.290 190.094 308.810 1.00 97.01  ? 59   LEU B CG  1 
ATOM   478   C CD1 . LEU A 1 76   ? 193.651 190.490 307.394 1.00 97.01  ? 59   LEU B CD1 1 
ATOM   479   C CD2 . LEU A 1 76   ? 193.546 191.244 309.771 1.00 97.01  ? 59   LEU B CD2 1 
ATOM   480   N N   . ASN A 1 77   ? 188.352 190.010 308.268 1.00 101.93 ? 60   ASN B N   1 
ATOM   481   C CA  . ASN A 1 77   ? 187.192 189.298 307.759 1.00 101.93 ? 60   ASN B CA  1 
ATOM   482   C C   . ASN A 1 77   ? 186.632 189.995 306.520 1.00 101.93 ? 60   ASN B C   1 
ATOM   483   O O   . ASN A 1 77   ? 186.799 191.206 306.352 1.00 101.93 ? 60   ASN B O   1 
ATOM   484   C CB  . ASN A 1 77   ? 186.114 189.211 308.832 1.00 101.93 ? 60   ASN B CB  1 
ATOM   485   C CG  . ASN A 1 77   ? 186.549 188.386 310.022 1.00 101.93 ? 60   ASN B CG  1 
ATOM   486   O OD1 . ASN A 1 77   ? 186.884 187.210 309.887 1.00 101.93 ? 60   ASN B OD1 1 
ATOM   487   N ND2 . ASN A 1 77   ? 186.551 189.001 311.199 1.00 101.93 ? 60   ASN B ND2 1 
ATOM   488   N N   . PRO A 1 78   ? 185.975 189.251 305.634 1.00 98.84  ? 61   PRO B N   1 
ATOM   489   C CA  . PRO A 1 78   ? 185.377 189.864 304.441 1.00 98.84  ? 61   PRO B CA  1 
ATOM   490   C C   . PRO A 1 78   ? 184.322 190.888 304.820 1.00 98.84  ? 61   PRO B C   1 
ATOM   491   O O   . PRO A 1 78   ? 183.524 190.659 305.740 1.00 98.84  ? 61   PRO B O   1 
ATOM   492   C CB  . PRO A 1 78   ? 184.754 188.670 303.705 1.00 98.84  ? 61   PRO B CB  1 
ATOM   493   C CG  . PRO A 1 78   ? 185.499 187.485 304.205 1.00 98.84  ? 61   PRO B CG  1 
ATOM   494   C CD  . PRO A 1 78   ? 185.842 187.786 305.628 1.00 98.84  ? 61   PRO B CD  1 
ATOM   495   N N   . PRO A 1 79   ? 184.281 192.025 304.131 1.00 104.75 ? 62   PRO B N   1 
ATOM   496   C CA  . PRO A 1 79   ? 183.274 193.044 304.432 1.00 104.75 ? 62   PRO B CA  1 
ATOM   497   C C   . PRO A 1 79   ? 181.906 192.620 303.931 1.00 104.75 ? 62   PRO B C   1 
ATOM   498   O O   . PRO A 1 79   ? 181.803 191.801 303.005 1.00 104.75 ? 62   PRO B O   1 
ATOM   499   C CB  . PRO A 1 79   ? 183.788 194.277 303.678 1.00 104.75 ? 62   PRO B CB  1 
ATOM   500   C CG  . PRO A 1 79   ? 184.546 193.711 302.535 1.00 104.75 ? 62   PRO B CG  1 
ATOM   501   C CD  . PRO A 1 79   ? 185.171 192.436 303.033 1.00 104.75 ? 62   PRO B CD  1 
ATOM   502   N N   . PRO A 1 80   ? 180.830 193.144 304.525 1.00 112.33 ? 63   PRO B N   1 
ATOM   503   C CA  . PRO A 1 80   ? 179.486 192.791 304.033 1.00 112.33 ? 63   PRO B CA  1 
ATOM   504   C C   . PRO A 1 80   ? 179.246 193.190 302.587 1.00 112.33 ? 63   PRO B C   1 
ATOM   505   O O   . PRO A 1 80   ? 178.560 192.467 301.854 1.00 112.33 ? 63   PRO B O   1 
ATOM   506   C CB  . PRO A 1 80   ? 178.553 193.544 304.993 1.00 112.33 ? 63   PRO B CB  1 
ATOM   507   C CG  . PRO A 1 80   ? 179.390 193.859 306.192 1.00 112.33 ? 63   PRO B CG  1 
ATOM   508   C CD  . PRO A 1 80   ? 180.779 194.053 305.681 1.00 112.33 ? 63   PRO B CD  1 
ATOM   509   N N   . GLU A 1 81   ? 179.799 194.321 302.153 1.00 113.00 ? 64   GLU B N   1 
ATOM   510   C CA  . GLU A 1 81   ? 179.607 194.825 300.797 1.00 113.00 ? 64   GLU B CA  1 
ATOM   511   C C   . GLU A 1 81   ? 180.865 194.531 299.990 1.00 113.00 ? 64   GLU B C   1 
ATOM   512   O O   . GLU A 1 81   ? 181.917 195.134 300.227 1.00 113.00 ? 64   GLU B O   1 
ATOM   513   C CB  . GLU A 1 81   ? 179.307 196.322 300.810 1.00 113.00 ? 64   GLU B CB  1 
ATOM   514   C CG  . GLU A 1 81   ? 177.896 196.677 301.245 1.00 113.00 ? 64   GLU B CG  1 
ATOM   515   C CD  . GLU A 1 81   ? 177.785 196.891 302.742 1.00 113.00 ? 64   GLU B CD  1 
ATOM   516   O OE1 . GLU A 1 81   ? 178.799 196.704 303.447 1.00 113.00 ? 64   GLU B OE1 1 
ATOM   517   O OE2 . GLU A 1 81   ? 176.685 197.249 303.214 1.00 113.00 ? 64   GLU B OE2 1 
ATOM   518   N N   . ALA A 1 82   ? 180.757 193.610 299.036 1.00 100.41 ? 65   ALA B N   1 
ATOM   519   C CA  . ALA A 1 82   ? 181.901 193.263 298.208 1.00 100.41 ? 65   ALA B CA  1 
ATOM   520   C C   . ALA A 1 82   ? 182.289 194.433 297.312 1.00 100.41 ? 65   ALA B C   1 
ATOM   521   O O   . ALA A 1 82   ? 181.457 195.260 296.931 1.00 100.41 ? 65   ALA B O   1 
ATOM   522   C CB  . ALA A 1 82   ? 181.600 192.028 297.361 1.00 100.41 ? 65   ALA B CB  1 
ATOM   523   N N   . LYS A 1 83   ? 183.575 194.498 296.983 1.00 89.20  ? 66   LYS B N   1 
ATOM   524   C CA  . LYS A 1 83   ? 184.114 195.596 296.201 1.00 89.20  ? 66   LYS B CA  1 
ATOM   525   C C   . LYS A 1 83   ? 183.777 195.429 294.722 1.00 89.20  ? 66   LYS B C   1 
ATOM   526   O O   . LYS A 1 83   ? 183.439 194.341 294.249 1.00 89.20  ? 66   LYS B O   1 
ATOM   527   C CB  . LYS A 1 83   ? 185.627 195.684 296.388 1.00 89.20  ? 66   LYS B CB  1 
ATOM   528   C CG  . LYS A 1 83   ? 186.066 195.655 297.843 1.00 89.20  ? 66   LYS B CG  1 
ATOM   529   C CD  . LYS A 1 83   ? 187.450 195.048 298.008 1.00 89.20  ? 66   LYS B CD  1 
ATOM   530   C CE  . LYS A 1 83   ? 188.326 195.300 296.794 1.00 89.20  ? 66   LYS B CE  1 
ATOM   531   N NZ  . LYS A 1 83   ? 189.717 194.820 297.008 1.00 89.20  ? 66   LYS B NZ  1 
ATOM   532   N N   . GLN A 1 84   ? 183.878 196.538 293.987 1.00 90.46  ? 67   GLN B N   1 
ATOM   533   C CA  . GLN A 1 84   ? 183.678 196.541 292.537 1.00 90.46  ? 67   GLN B CA  1 
ATOM   534   C C   . GLN A 1 84   ? 184.926 195.967 291.865 1.00 90.46  ? 67   GLN B C   1 
ATOM   535   O O   . GLN A 1 84   ? 185.691 196.656 291.188 1.00 90.46  ? 67   GLN B O   1 
ATOM   536   C CB  . GLN A 1 84   ? 183.383 197.950 292.044 1.00 90.46  ? 67   GLN B CB  1 
ATOM   537   C CG  . GLN A 1 84   ? 182.600 198.811 293.019 1.00 90.46  ? 67   GLN B CG  1 
ATOM   538   C CD  . GLN A 1 84   ? 181.138 198.429 293.095 1.00 90.46  ? 67   GLN B CD  1 
ATOM   539   O OE1 . GLN A 1 84   ? 180.555 197.965 292.115 1.00 90.46  ? 67   GLN B OE1 1 
ATOM   540   N NE2 . GLN A 1 84   ? 180.532 198.638 294.257 1.00 90.46  ? 67   GLN B NE2 1 
ATOM   541   N N   . VAL A 1 85   ? 185.123 194.669 292.066 1.00 79.92  ? 68   VAL B N   1 
ATOM   542   C CA  . VAL A 1 85   ? 186.370 194.019 291.675 1.00 79.92  ? 68   VAL B CA  1 
ATOM   543   C C   . VAL A 1 85   ? 186.059 192.704 290.968 1.00 79.92  ? 68   VAL B C   1 
ATOM   544   O O   . VAL A 1 85   ? 185.177 191.958 291.414 1.00 79.92  ? 68   VAL B O   1 
ATOM   545   C CB  . VAL A 1 85   ? 187.272 193.816 292.902 1.00 79.92  ? 68   VAL B CB  1 
ATOM   546   C CG1 . VAL A 1 85   ? 188.192 192.634 292.717 1.00 79.92  ? 68   VAL B CG1 1 
ATOM   547   C CG2 . VAL A 1 85   ? 188.076 195.078 293.170 1.00 79.92  ? 68   VAL B CG2 1 
ATOM   548   N N   . PRO A 1 86   ? 186.746 192.379 289.868 1.00 76.58  ? 69   PRO B N   1 
ATOM   549   C CA  . PRO A 1 86   ? 186.402 191.149 289.139 1.00 76.58  ? 69   PRO B CA  1 
ATOM   550   C C   . PRO A 1 86   ? 186.819 189.880 289.857 1.00 76.58  ? 69   PRO B C   1 
ATOM   551   O O   . PRO A 1 86   ? 186.168 188.845 289.674 1.00 76.58  ? 69   PRO B O   1 
ATOM   552   C CB  . PRO A 1 86   ? 187.137 191.302 287.799 1.00 76.58  ? 69   PRO B CB  1 
ATOM   553   C CG  . PRO A 1 86   ? 187.939 192.556 287.885 1.00 76.58  ? 69   PRO B CG  1 
ATOM   554   C CD  . PRO A 1 86   ? 187.888 193.087 289.271 1.00 76.58  ? 69   PRO B CD  1 
ATOM   555   N N   . VAL A 1 87   ? 187.877 189.917 290.661 1.00 73.80  ? 70   VAL B N   1 
ATOM   556   C CA  . VAL A 1 87   ? 188.347 188.723 291.357 1.00 73.80  ? 70   VAL B CA  1 
ATOM   557   C C   . VAL A 1 87   ? 189.057 189.150 292.635 1.00 73.80  ? 70   VAL B C   1 
ATOM   558   O O   . VAL A 1 87   ? 189.890 190.060 292.622 1.00 73.80  ? 70   VAL B O   1 
ATOM   559   C CB  . VAL A 1 87   ? 189.257 187.862 290.454 1.00 73.80  ? 70   VAL B CB  1 
ATOM   560   C CG1 . VAL A 1 87   ? 190.563 188.574 290.127 1.00 73.80  ? 70   VAL B CG1 1 
ATOM   561   C CG2 . VAL A 1 87   ? 189.526 186.525 291.095 1.00 73.80  ? 70   VAL B CG2 1 
ATOM   562   N N   . SER A 1 88   ? 188.712 188.504 293.745 1.00 72.10  ? 71   SER B N   1 
ATOM   563   C CA  . SER A 1 88   ? 189.300 188.848 295.030 1.00 72.10  ? 71   SER B CA  1 
ATOM   564   C C   . SER A 1 88   ? 189.148 187.667 295.974 1.00 72.10  ? 71   SER B C   1 
ATOM   565   O O   . SER A 1 88   ? 188.099 187.022 296.003 1.00 72.10  ? 71   SER B O   1 
ATOM   566   C CB  . SER A 1 88   ? 188.645 190.095 295.627 1.00 72.10  ? 71   SER B CB  1 
ATOM   567   O OG  . SER A 1 88   ? 187.322 189.821 296.047 1.00 72.10  ? 71   SER B OG  1 
ATOM   568   N N   . TYR A 1 89   ? 190.197 187.399 296.744 1.00 74.13  ? 72   TYR B N   1 
ATOM   569   C CA  . TYR A 1 89   ? 190.230 186.296 297.694 1.00 74.13  ? 72   TYR B CA  1 
ATOM   570   C C   . TYR A 1 89   ? 190.420 186.861 299.091 1.00 74.13  ? 72   TYR B C   1 
ATOM   571   O O   . TYR A 1 89   ? 191.291 187.708 299.305 1.00 74.13  ? 72   TYR B O   1 
ATOM   572   C CB  . TYR A 1 89   ? 191.356 185.319 297.356 1.00 74.13  ? 72   TYR B CB  1 
ATOM   573   C CG  . TYR A 1 89   ? 191.477 184.155 298.308 1.00 74.13  ? 72   TYR B CG  1 
ATOM   574   C CD1 . TYR A 1 89   ? 190.467 183.215 298.419 1.00 74.13  ? 72   TYR B CD1 1 
ATOM   575   C CD2 . TYR A 1 89   ? 192.604 183.998 299.098 1.00 74.13  ? 72   TYR B CD2 1 
ATOM   576   C CE1 . TYR A 1 89   ? 190.577 182.150 299.289 1.00 74.13  ? 72   TYR B CE1 1 
ATOM   577   C CE2 . TYR A 1 89   ? 192.723 182.938 299.972 1.00 74.13  ? 72   TYR B CE2 1 
ATOM   578   C CZ  . TYR A 1 89   ? 191.707 182.018 300.064 1.00 74.13  ? 72   TYR B CZ  1 
ATOM   579   O OH  . TYR A 1 89   ? 191.823 180.960 300.933 1.00 74.13  ? 72   TYR B OH  1 
ATOM   580   N N   . TYR A 1 90   ? 189.609 186.398 300.035 1.00 79.12  ? 73   TYR B N   1 
ATOM   581   C CA  . TYR A 1 90   ? 189.644 186.885 301.405 1.00 79.12  ? 73   TYR B CA  1 
ATOM   582   C C   . TYR A 1 90   ? 190.085 185.768 302.336 1.00 79.12  ? 73   TYR B C   1 
ATOM   583   O O   . TYR A 1 90   ? 189.666 184.618 302.183 1.00 79.12  ? 73   TYR B O   1 
ATOM   584   C CB  . TYR A 1 90   ? 188.281 187.413 301.838 1.00 79.12  ? 73   TYR B CB  1 
ATOM   585   C CG  . TYR A 1 90   ? 188.050 188.854 301.466 1.00 79.12  ? 73   TYR B CG  1 
ATOM   586   C CD1 . TYR A 1 90   ? 188.457 189.876 302.304 1.00 79.12  ? 73   TYR B CD1 1 
ATOM   587   C CD2 . TYR A 1 90   ? 187.420 189.192 300.279 1.00 79.12  ? 73   TYR B CD2 1 
ATOM   588   C CE1 . TYR A 1 90   ? 188.251 191.195 301.970 1.00 79.12  ? 73   TYR B CE1 1 
ATOM   589   C CE2 . TYR A 1 90   ? 187.206 190.507 299.936 1.00 79.12  ? 73   TYR B CE2 1 
ATOM   590   C CZ  . TYR A 1 90   ? 187.624 191.505 300.786 1.00 79.12  ? 73   TYR B CZ  1 
ATOM   591   O OH  . TYR A 1 90   ? 187.416 192.822 300.455 1.00 79.12  ? 73   TYR B OH  1 
ATOM   592   N N   . ASP A 1 91   ? 190.927 186.115 303.306 1.00 76.45  ? 74   ASP B N   1 
ATOM   593   C CA  . ASP A 1 91   ? 191.482 185.128 304.218 1.00 76.45  ? 74   ASP B CA  1 
ATOM   594   C C   . ASP A 1 91   ? 191.813 185.809 305.538 1.00 76.45  ? 74   ASP B C   1 
ATOM   595   O O   . ASP A 1 91   ? 191.913 187.036 305.619 1.00 76.45  ? 74   ASP B O   1 
ATOM   596   C CB  . ASP A 1 91   ? 192.723 184.457 303.619 1.00 76.45  ? 74   ASP B CB  1 
ATOM   597   C CG  . ASP A 1 91   ? 193.142 183.223 304.379 1.00 76.45  ? 74   ASP B CG  1 
ATOM   598   O OD1 . ASP A 1 91   ? 193.410 183.332 305.592 1.00 76.45  ? 74   ASP B OD1 1 
ATOM   599   O OD2 . ASP A 1 91   ? 193.198 182.140 303.761 1.00 76.45  ? 74   ASP B OD2 1 
ATOM   600   N N   . SER A 1 92   ? 191.974 184.994 306.579 1.00 77.51  ? 75   SER B N   1 
ATOM   601   C CA  . SER A 1 92   ? 192.254 185.515 307.911 1.00 77.51  ? 75   SER B CA  1 
ATOM   602   C C   . SER A 1 92   ? 193.466 184.837 308.535 1.00 77.51  ? 75   SER B C   1 
ATOM   603   O O   . SER A 1 92   ? 194.173 185.444 309.345 1.00 77.51  ? 75   SER B O   1 
ATOM   604   C CB  . SER A 1 92   ? 191.031 185.344 308.813 1.00 77.51  ? 75   SER B CB  1 
ATOM   605   O OG  . SER A 1 92   ? 190.595 183.995 308.825 1.00 77.51  ? 75   SER B OG  1 
ATOM   606   N N   . THR A 1 93   ? 193.715 183.583 308.172 1.00 77.86  ? 76   THR B N   1 
ATOM   607   C CA  . THR A 1 93   ? 194.831 182.831 308.728 1.00 77.86  ? 76   THR B CA  1 
ATOM   608   C C   . THR A 1 93   ? 196.117 182.998 307.930 1.00 77.86  ? 76   THR B C   1 
ATOM   609   O O   . THR A 1 93   ? 197.145 182.431 308.316 1.00 77.86  ? 76   THR B O   1 
ATOM   610   C CB  . THR A 1 93   ? 194.476 181.342 308.822 1.00 77.86  ? 76   THR B CB  1 
ATOM   611   O OG1 . THR A 1 93   ? 195.638 180.595 309.204 1.00 77.86  ? 76   THR B OG1 1 
ATOM   612   C CG2 . THR A 1 93   ? 193.968 180.825 307.487 1.00 77.86  ? 76   THR B CG2 1 
ATOM   613   N N   . TYR A 1 94   ? 196.087 183.756 306.838 1.00 75.12  ? 77   TYR B N   1 
ATOM   614   C CA  . TYR A 1 94   ? 197.271 183.926 306.008 1.00 75.12  ? 77   TYR B CA  1 
ATOM   615   C C   . TYR A 1 94   ? 198.343 184.715 306.746 1.00 75.12  ? 77   TYR B C   1 
ATOM   616   O O   . TYR A 1 94   ? 198.046 185.666 307.472 1.00 75.12  ? 77   TYR B O   1 
ATOM   617   C CB  . TYR A 1 94   ? 196.901 184.635 304.707 1.00 75.12  ? 77   TYR B CB  1 
ATOM   618   C CG  . TYR A 1 94   ? 198.071 184.894 303.789 1.00 75.12  ? 77   TYR B CG  1 
ATOM   619   C CD1 . TYR A 1 94   ? 198.609 183.877 303.019 1.00 75.12  ? 77   TYR B CD1 1 
ATOM   620   C CD2 . TYR A 1 94   ? 198.628 186.158 303.684 1.00 75.12  ? 77   TYR B CD2 1 
ATOM   621   C CE1 . TYR A 1 94   ? 199.675 184.110 302.177 1.00 75.12  ? 77   TYR B CE1 1 
ATOM   622   C CE2 . TYR A 1 94   ? 199.692 186.400 302.841 1.00 75.12  ? 77   TYR B CE2 1 
ATOM   623   C CZ  . TYR A 1 94   ? 200.211 185.373 302.091 1.00 75.12  ? 77   TYR B CZ  1 
ATOM   624   O OH  . TYR A 1 94   ? 201.273 185.606 301.252 1.00 75.12  ? 77   TYR B OH  1 
ATOM   625   N N   . LEU A 1 95   ? 199.598 184.306 306.557 1.00 73.59  ? 78   LEU B N   1 
ATOM   626   C CA  . LEU A 1 95   ? 200.756 185.002 307.120 1.00 73.59  ? 78   LEU B CA  1 
ATOM   627   C C   . LEU A 1 95   ? 200.664 185.113 308.639 1.00 73.59  ? 78   LEU B C   1 
ATOM   628   O O   . LEU A 1 95   ? 201.065 186.117 309.230 1.00 73.59  ? 78   LEU B O   1 
ATOM   629   C CB  . LEU A 1 95   ? 200.927 186.386 306.491 1.00 73.59  ? 78   LEU B CB  1 
ATOM   630   C CG  . LEU A 1 95   ? 202.038 186.572 305.462 1.00 73.59  ? 78   LEU B CG  1 
ATOM   631   C CD1 . LEU A 1 95   ? 202.146 188.030 305.069 1.00 73.59  ? 78   LEU B CD1 1 
ATOM   632   C CD2 . LEU A 1 95   ? 203.350 186.074 306.010 1.00 73.59  ? 78   LEU B CD2 1 
ATOM   633   N N   . SER A 1 96   ? 200.131 184.076 309.280 1.00 78.14  ? 79   SER B N   1 
ATOM   634   C CA  . SER A 1 96   ? 200.033 184.045 310.731 1.00 78.14  ? 79   SER B CA  1 
ATOM   635   C C   . SER A 1 96   ? 201.006 183.075 311.379 1.00 78.14  ? 79   SER B C   1 
ATOM   636   O O   . SER A 1 96   ? 201.193 183.136 312.599 1.00 78.14  ? 79   SER B O   1 
ATOM   637   C CB  . SER A 1 96   ? 198.604 183.688 311.162 1.00 78.14  ? 79   SER B CB  1 
ATOM   638   O OG  . SER A 1 96   ? 198.461 183.787 312.567 1.00 78.14  ? 79   SER B OG  1 
ATOM   639   N N   . THR A 1 97   ? 201.628 182.191 310.606 1.00 78.64  ? 80   THR B N   1 
ATOM   640   C CA  . THR A 1 97   ? 202.558 181.199 311.118 1.00 78.64  ? 80   THR B CA  1 
ATOM   641   C C   . THR A 1 97   ? 203.974 181.517 310.658 1.00 78.64  ? 80   THR B C   1 
ATOM   642   O O   . THR A 1 97   ? 204.187 182.232 309.676 1.00 78.64  ? 80   THR B O   1 
ATOM   643   C CB  . THR A 1 97   ? 202.166 179.792 310.658 1.00 78.64  ? 80   THR B CB  1 
ATOM   644   O OG1 . THR A 1 97   ? 202.629 179.583 309.319 1.00 78.64  ? 80   THR B OG1 1 
ATOM   645   C CG2 . THR A 1 97   ? 200.657 179.623 310.695 1.00 78.64  ? 80   THR B CG2 1 
ATOM   646   N N   . ASP A 1 98   ? 204.947 180.968 311.388 1.00 79.45  ? 81   ASP B N   1 
ATOM   647   C CA  . ASP A 1 98   ? 206.348 181.251 311.093 1.00 79.45  ? 81   ASP B CA  1 
ATOM   648   C C   . ASP A 1 98   ? 206.733 180.768 309.700 1.00 79.45  ? 81   ASP B C   1 
ATOM   649   O O   . ASP A 1 98   ? 207.452 181.461 308.968 1.00 79.45  ? 81   ASP B O   1 
ATOM   650   C CB  . ASP A 1 98   ? 207.239 180.601 312.149 1.00 79.45  ? 81   ASP B CB  1 
ATOM   651   C CG  . ASP A 1 98   ? 208.418 181.465 312.522 1.00 79.45  ? 81   ASP B CG  1 
ATOM   652   O OD1 . ASP A 1 98   ? 208.671 182.448 311.800 1.00 79.45  ? 81   ASP B OD1 1 
ATOM   653   O OD2 . ASP A 1 98   ? 209.088 181.165 313.531 1.00 79.45  ? 81   ASP B OD2 1 
ATOM   654   N N   . ASN A 1 99   ? 206.265 179.578 309.320 1.00 79.34  ? 82   ASN B N   1 
ATOM   655   C CA  . ASN A 1 99   ? 206.571 179.049 307.997 1.00 79.34  ? 82   ASN B CA  1 
ATOM   656   C C   . ASN A 1 99   ? 206.033 179.964 306.906 1.00 79.34  ? 82   ASN B C   1 
ATOM   657   O O   . ASN A 1 99   ? 206.703 180.194 305.892 1.00 79.34  ? 82   ASN B O   1 
ATOM   658   C CB  . ASN A 1 99   ? 205.991 177.644 307.852 1.00 79.34  ? 82   ASN B CB  1 
ATOM   659   C CG  . ASN A 1 99   ? 206.419 176.720 308.974 1.00 79.34  ? 82   ASN B CG  1 
ATOM   660   O OD1 . ASN A 1 99   ? 206.271 177.047 310.152 1.00 79.34  ? 82   ASN B OD1 1 
ATOM   661   N ND2 . ASN A 1 99   ? 206.945 175.555 308.615 1.00 79.34  ? 82   ASN B ND2 1 
ATOM   662   N N   . GLU A 1 100  ? 204.824 180.495 307.098 1.00 76.94  ? 83   GLU B N   1 
ATOM   663   C CA  . GLU A 1 100  ? 204.250 181.402 306.111 1.00 76.94  ? 83   GLU B CA  1 
ATOM   664   C C   . GLU A 1 100  ? 205.093 182.659 305.963 1.00 76.94  ? 83   GLU B C   1 
ATOM   665   O O   . GLU A 1 100  ? 205.323 183.130 304.844 1.00 76.94  ? 83   GLU B O   1 
ATOM   666   C CB  . GLU A 1 100  ? 202.816 181.763 306.497 1.00 76.94  ? 83   GLU B CB  1 
ATOM   667   C CG  . GLU A 1 100  ? 201.820 180.631 306.333 1.00 76.94  ? 83   GLU B CG  1 
ATOM   668   C CD  . GLU A 1 100  ? 200.939 180.805 305.116 1.00 76.94  ? 83   GLU B CD  1 
ATOM   669   O OE1 . GLU A 1 100  ? 201.411 181.393 304.121 1.00 76.94  ? 83   GLU B OE1 1 
ATOM   670   O OE2 . GLU A 1 100  ? 199.774 180.357 305.152 1.00 76.94  ? 83   GLU B OE2 1 
ATOM   671   N N   . LYS A 1 101  ? 205.562 183.220 307.079 1.00 74.57  ? 84   LYS B N   1 
ATOM   672   C CA  . LYS A 1 101  ? 206.378 184.427 307.009 1.00 74.57  ? 84   LYS B CA  1 
ATOM   673   C C   . LYS A 1 101  ? 207.709 184.159 306.318 1.00 74.57  ? 84   LYS B C   1 
ATOM   674   O O   . LYS A 1 101  ? 208.163 184.967 305.498 1.00 74.57  ? 84   LYS B O   1 
ATOM   675   C CB  . LYS A 1 101  ? 206.598 184.995 308.409 1.00 74.57  ? 84   LYS B CB  1 
ATOM   676   C CG  . LYS A 1 101  ? 205.365 185.652 308.997 1.00 74.57  ? 84   LYS B CG  1 
ATOM   677   C CD  . LYS A 1 101  ? 205.618 186.139 310.408 1.00 74.57  ? 84   LYS B CD  1 
ATOM   678   C CE  . LYS A 1 101  ? 204.395 185.949 311.282 1.00 74.57  ? 84   LYS B CE  1 
ATOM   679   N NZ  . LYS A 1 101  ? 204.139 184.512 311.558 1.00 74.57  ? 84   LYS B NZ  1 
ATOM   680   N N   . ASP A 1 102  ? 208.351 183.032 306.632 1.00 75.25  ? 85   ASP B N   1 
ATOM   681   C CA  . ASP A 1 102  ? 209.609 182.708 305.965 1.00 75.25  ? 85   ASP B CA  1 
ATOM   682   C C   . ASP A 1 102  ? 209.401 182.499 304.469 1.00 75.25  ? 85   ASP B C   1 
ATOM   683   O O   . ASP A 1 102  ? 210.213 182.952 303.653 1.00 75.25  ? 85   ASP B O   1 
ATOM   684   C CB  . ASP A 1 102  ? 210.241 181.471 306.599 1.00 75.25  ? 85   ASP B CB  1 
ATOM   685   C CG  . ASP A 1 102  ? 211.707 181.323 306.246 1.00 75.25  ? 85   ASP B CG  1 
ATOM   686   O OD1 . ASP A 1 102  ? 212.278 182.270 305.668 1.00 75.25  ? 85   ASP B OD1 1 
ATOM   687   O OD2 . ASP A 1 102  ? 212.291 180.261 306.546 1.00 75.25  ? 85   ASP B OD2 1 
ATOM   688   N N   . ASN A 1 103  ? 208.320 181.815 304.090 1.00 71.98  ? 86   ASN B N   1 
ATOM   689   C CA  . ASN A 1 103  ? 208.029 181.617 302.674 1.00 71.98  ? 86   ASN B CA  1 
ATOM   690   C C   . ASN A 1 103  ? 207.764 182.945 301.977 1.00 71.98  ? 86   ASN B C   1 
ATOM   691   O O   . ASN A 1 103  ? 208.209 183.162 300.844 1.00 71.98  ? 86   ASN B O   1 
ATOM   692   C CB  . ASN A 1 103  ? 206.836 180.678 302.515 1.00 71.98  ? 86   ASN B CB  1 
ATOM   693   C CG  . ASN A 1 103  ? 207.005 179.718 301.362 1.00 71.98  ? 86   ASN B CG  1 
ATOM   694   O OD1 . ASN A 1 103  ? 207.698 178.709 301.477 1.00 71.98  ? 86   ASN B OD1 1 
ATOM   695   N ND2 . ASN A 1 103  ? 206.374 180.030 300.236 1.00 71.98  ? 86   ASN B ND2 1 
ATOM   696   N N   . TYR A 1 104  ? 207.037 183.846 302.644 1.00 69.60  ? 87   TYR B N   1 
ATOM   697   C CA  . TYR A 1 104  ? 206.814 185.183 302.107 1.00 69.60  ? 87   TYR B CA  1 
ATOM   698   C C   . TYR A 1 104  ? 208.130 185.903 301.872 1.00 69.60  ? 87   TYR B C   1 
ATOM   699   O O   . TYR A 1 104  ? 208.328 186.536 300.828 1.00 69.60  ? 87   TYR B O   1 
ATOM   700   C CB  . TYR A 1 104  ? 205.943 185.985 303.072 1.00 69.60  ? 87   TYR B CB  1 
ATOM   701   C CG  . TYR A 1 104  ? 205.778 187.431 302.690 1.00 69.60  ? 87   TYR B CG  1 
ATOM   702   C CD1 . TYR A 1 104  ? 204.868 187.811 301.722 1.00 69.60  ? 87   TYR B CD1 1 
ATOM   703   C CD2 . TYR A 1 104  ? 206.536 188.419 303.298 1.00 69.60  ? 87   TYR B CD2 1 
ATOM   704   C CE1 . TYR A 1 104  ? 204.714 189.129 301.367 1.00 69.60  ? 87   TYR B CE1 1 
ATOM   705   C CE2 . TYR A 1 104  ? 206.390 189.742 302.949 1.00 69.60  ? 87   TYR B CE2 1 
ATOM   706   C CZ  . TYR A 1 104  ? 205.477 190.090 301.984 1.00 69.60  ? 87   TYR B CZ  1 
ATOM   707   O OH  . TYR A 1 104  ? 205.324 191.408 301.632 1.00 69.60  ? 87   TYR B OH  1 
ATOM   708   N N   . LEU A 1 105  ? 209.039 185.821 302.841 1.00 69.60  ? 88   LEU B N   1 
ATOM   709   C CA  . LEU A 1 105  ? 210.331 186.480 302.709 1.00 69.60  ? 88   LEU B CA  1 
ATOM   710   C C   . LEU A 1 105  ? 211.115 185.934 301.526 1.00 69.60  ? 88   LEU B C   1 
ATOM   711   O O   . LEU A 1 105  ? 211.670 186.697 300.727 1.00 69.60  ? 88   LEU B O   1 
ATOM   712   C CB  . LEU A 1 105  ? 211.131 186.302 303.988 1.00 69.60  ? 88   LEU B CB  1 
ATOM   713   C CG  . LEU A 1 105  ? 212.043 187.479 304.244 1.00 69.60  ? 88   LEU B CG  1 
ATOM   714   C CD1 . LEU A 1 105  ? 211.220 188.730 304.276 1.00 69.60  ? 88   LEU B CD1 1 
ATOM   715   C CD2 . LEU A 1 105  ? 212.703 187.255 305.542 1.00 69.60  ? 88   LEU B CD2 1 
ATOM   716   N N   . LYS A 1 106  ? 211.193 184.606 301.415 1.00 70.77  ? 89   LYS B N   1 
ATOM   717   C CA  . LYS A 1 106  ? 211.944 184.011 300.316 1.00 70.77  ? 89   LYS B CA  1 
ATOM   718   C C   . LYS A 1 106  ? 211.332 184.380 298.973 1.00 70.77  ? 89   LYS B C   1 
ATOM   719   O O   . LYS A 1 106  ? 212.054 184.684 298.018 1.00 70.77  ? 89   LYS B O   1 
ATOM   720   C CB  . LYS A 1 106  ? 212.015 182.496 300.477 1.00 70.77  ? 89   LYS B CB  1 
ATOM   721   C CG  . LYS A 1 106  ? 212.491 182.033 301.836 1.00 70.77  ? 89   LYS B CG  1 
ATOM   722   C CD  . LYS A 1 106  ? 213.981 181.780 301.854 1.00 70.77  ? 89   LYS B CD  1 
ATOM   723   C CE  . LYS A 1 106  ? 214.419 181.283 303.218 1.00 70.77  ? 89   LYS B CE  1 
ATOM   724   N NZ  . LYS A 1 106  ? 213.556 180.168 303.695 1.00 70.77  ? 89   LYS B NZ  1 
ATOM   725   N N   . GLY A 1 107  ? 210.001 184.375 298.883 1.00 73.41  ? 90   GLY B N   1 
ATOM   726   C CA  . GLY A 1 107  ? 209.358 184.762 297.639 1.00 73.41  ? 90   GLY B CA  1 
ATOM   727   C C   . GLY A 1 107  ? 209.645 186.201 297.258 1.00 73.41  ? 90   GLY B C   1 
ATOM   728   O O   . GLY A 1 107  ? 209.962 186.500 296.103 1.00 73.41  ? 90   GLY B O   1 
ATOM   729   N N   . VAL A 1 108  ? 209.547 187.115 298.228 1.00 69.66  ? 91   VAL B N   1 
ATOM   730   C CA  . VAL A 1 108  ? 209.802 188.525 297.939 1.00 69.66  ? 91   VAL B CA  1 
ATOM   731   C C   . VAL A 1 108  ? 211.246 188.728 297.502 1.00 69.66  ? 91   VAL B C   1 
ATOM   732   O O   . VAL A 1 108  ? 211.519 189.437 296.525 1.00 69.66  ? 91   VAL B O   1 
ATOM   733   C CB  . VAL A 1 108  ? 209.450 189.397 299.157 1.00 69.66  ? 91   VAL B CB  1 
ATOM   734   C CG1 . VAL A 1 108  ? 210.234 190.697 299.126 1.00 69.66  ? 91   VAL B CG1 1 
ATOM   735   C CG2 . VAL A 1 108  ? 207.964 189.686 299.183 1.00 69.66  ? 91   VAL B CG2 1 
ATOM   736   N N   . THR A 1 109  ? 212.192 188.110 298.213 1.00 69.88  ? 92   THR B N   1 
ATOM   737   C CA  . THR A 1 109  ? 213.598 188.271 297.855 1.00 69.88  ? 92   THR B CA  1 
ATOM   738   C C   . THR A 1 109  ? 213.883 187.702 296.471 1.00 69.88  ? 92   THR B C   1 
ATOM   739   O O   . THR A 1 109  ? 214.596 188.323 295.671 1.00 69.88  ? 92   THR B O   1 
ATOM   740   C CB  . THR A 1 109  ? 214.486 187.612 298.910 1.00 69.88  ? 92   THR B CB  1 
ATOM   741   O OG1 . THR A 1 109  ? 214.503 188.422 300.092 1.00 69.88  ? 92   THR B OG1 1 
ATOM   742   C CG2 . THR A 1 109  ? 215.904 187.455 298.399 1.00 69.88  ? 92   THR B CG2 1 
ATOM   743   N N   . LYS A 1 110  ? 213.325 186.530 296.162 1.00 70.63  ? 93   LYS B N   1 
ATOM   744   C CA  . LYS A 1 110  ? 213.539 185.938 294.847 1.00 70.63  ? 93   LYS B CA  1 
ATOM   745   C C   . LYS A 1 110  ? 212.958 186.813 293.747 1.00 70.63  ? 93   LYS B C   1 
ATOM   746   O O   . LYS A 1 110  ? 213.570 186.976 292.686 1.00 70.63  ? 93   LYS B O   1 
ATOM   747   C CB  . LYS A 1 110  ? 212.929 184.541 294.797 1.00 70.63  ? 93   LYS B CB  1 
ATOM   748   C CG  . LYS A 1 110  ? 213.501 183.664 293.709 1.00 70.63  ? 93   LYS B CG  1 
ATOM   749   C CD  . LYS A 1 110  ? 213.297 182.201 294.037 1.00 70.63  ? 93   LYS B CD  1 
ATOM   750   C CE  . LYS A 1 110  ? 213.633 181.331 292.850 1.00 70.63  ? 93   LYS B CE  1 
ATOM   751   N NZ  . LYS A 1 110  ? 213.270 179.911 293.086 1.00 70.63  ? 93   LYS B NZ  1 
ATOM   752   N N   . LEU A 1 111  ? 211.774 187.383 293.976 1.00 70.89  ? 94   LEU B N   1 
ATOM   753   C CA  . LEU A 1 111  ? 211.185 188.262 292.972 1.00 70.89  ? 94   LEU B CA  1 
ATOM   754   C C   . LEU A 1 111  ? 212.023 189.521 292.783 1.00 70.89  ? 94   LEU B C   1 
ATOM   755   O O   . LEU A 1 111  ? 212.189 190.000 291.653 1.00 70.89  ? 94   LEU B O   1 
ATOM   756   C CB  . LEU A 1 111  ? 209.751 188.612 293.360 1.00 70.89  ? 94   LEU B CB  1 
ATOM   757   C CG  . LEU A 1 111  ? 208.748 187.467 293.214 1.00 70.89  ? 94   LEU B CG  1 
ATOM   758   C CD1 . LEU A 1 111  ? 207.352 188.005 293.016 1.00 70.89  ? 94   LEU B CD1 1 
ATOM   759   C CD2 . LEU A 1 111  ? 209.128 186.550 292.064 1.00 70.89  ? 94   LEU B CD2 1 
ATOM   760   N N   . PHE A 1 112  ? 212.563 190.069 293.873 1.00 69.60  ? 95   PHE B N   1 
ATOM   761   C CA  . PHE A 1 112  ? 213.429 191.236 293.747 1.00 69.60  ? 95   PHE B CA  1 
ATOM   762   C C   . PHE A 1 112  ? 214.676 190.909 292.937 1.00 69.60  ? 95   PHE B C   1 
ATOM   763   O O   . PHE A 1 112  ? 215.091 191.698 292.081 1.00 69.60  ? 95   PHE B O   1 
ATOM   764   C CB  . PHE A 1 112  ? 213.813 191.769 295.124 1.00 69.60  ? 95   PHE B CB  1 
ATOM   765   C CG  . PHE A 1 112  ? 212.997 192.945 295.562 1.00 69.60  ? 95   PHE B CG  1 
ATOM   766   C CD1 . PHE A 1 112  ? 213.328 194.221 295.151 1.00 69.60  ? 95   PHE B CD1 1 
ATOM   767   C CD2 . PHE A 1 112  ? 211.902 192.776 296.387 1.00 69.60  ? 95   PHE B CD2 1 
ATOM   768   C CE1 . PHE A 1 112  ? 212.580 195.306 295.549 1.00 69.60  ? 95   PHE B CE1 1 
ATOM   769   C CE2 . PHE A 1 112  ? 211.151 193.857 296.789 1.00 69.60  ? 95   PHE B CE2 1 
ATOM   770   C CZ  . PHE A 1 112  ? 211.491 195.125 296.370 1.00 69.60  ? 95   PHE B CZ  1 
ATOM   771   N N   . GLU A 1 113  ? 215.286 189.748 293.188 1.00 73.12  ? 96   GLU B N   1 
ATOM   772   C CA  . GLU A 1 113  ? 216.455 189.355 292.403 1.00 73.12  ? 96   GLU B CA  1 
ATOM   773   C C   . GLU A 1 113  ? 216.093 189.161 290.936 1.00 73.12  ? 96   GLU B C   1 
ATOM   774   O O   . GLU A 1 113  ? 216.857 189.551 290.042 1.00 73.12  ? 96   GLU B O   1 
ATOM   775   C CB  . GLU A 1 113  ? 217.076 188.082 292.974 1.00 73.12  ? 96   GLU B CB  1 
ATOM   776   C CG  . GLU A 1 113  ? 217.440 188.171 294.439 1.00 73.12  ? 96   GLU B CG  1 
ATOM   777   C CD  . GLU A 1 113  ? 218.930 188.276 294.660 1.00 73.12  ? 96   GLU B CD  1 
ATOM   778   O OE1 . GLU A 1 113  ? 219.660 188.500 293.672 1.00 73.12  ? 96   GLU B OE1 1 
ATOM   779   O OE2 . GLU A 1 113  ? 219.373 188.131 295.818 1.00 73.12  ? 96   GLU B OE2 1 
ATOM   780   N N   . ARG A 1 114  ? 214.931 188.563 290.667 1.00 71.72  ? 97   ARG B N   1 
ATOM   781   C CA  . ARG A 1 114  ? 214.510 188.356 289.286 1.00 71.72  ? 97   ARG B CA  1 
ATOM   782   C C   . ARG A 1 114  ? 214.321 189.681 288.565 1.00 71.72  ? 97   ARG B C   1 
ATOM   783   O O   . ARG A 1 114  ? 214.695 189.818 287.395 1.00 71.72  ? 97   ARG B O   1 
ATOM   784   C CB  . ARG A 1 114  ? 213.220 187.543 289.240 1.00 71.72  ? 97   ARG B CB  1 
ATOM   785   C CG  . ARG A 1 114  ? 212.550 187.560 287.882 1.00 71.72  ? 97   ARG B CG  1 
ATOM   786   C CD  . ARG A 1 114  ? 211.802 186.276 287.622 1.00 71.72  ? 97   ARG B CD  1 
ATOM   787   N NE  . ARG A 1 114  ? 210.929 186.387 286.462 1.00 71.72  ? 97   ARG B NE  1 
ATOM   788   C CZ  . ARG A 1 114  ? 211.326 186.201 285.211 1.00 71.72  ? 97   ARG B CZ  1 
ATOM   789   N NH1 . ARG A 1 114  ? 212.580 185.898 284.922 1.00 71.72  ? 97   ARG B NH1 1 
ATOM   790   N NH2 . ARG A 1 114  ? 210.443 186.321 284.226 1.00 71.72  ? 97   ARG B NH2 1 
ATOM   791   N N   . ILE A 1 115  ? 213.731 190.666 289.240 1.00 69.60  ? 98   ILE B N   1 
ATOM   792   C CA  . ILE A 1 115  ? 213.608 191.984 288.628 1.00 69.60  ? 98   ILE B CA  1 
ATOM   793   C C   . ILE A 1 115  ? 214.984 192.607 288.429 1.00 69.60  ? 98   ILE B C   1 
ATOM   794   O O   . ILE A 1 115  ? 215.260 193.213 287.389 1.00 69.60  ? 98   ILE B O   1 
ATOM   795   C CB  . ILE A 1 115  ? 212.689 192.891 289.466 1.00 69.60  ? 98   ILE B CB  1 
ATOM   796   C CG1 . ILE A 1 115  ? 211.264 192.349 289.465 1.00 69.60  ? 98   ILE B CG1 1 
ATOM   797   C CG2 . ILE A 1 115  ? 212.673 194.290 288.897 1.00 69.60  ? 98   ILE B CG2 1 
ATOM   798   C CD1 . ILE A 1 115  ? 210.528 192.596 290.751 1.00 69.60  ? 98   ILE B CD1 1 
ATOM   799   N N   . TYR A 1 116  ? 215.876 192.448 289.409 1.00 70.07  ? 99   TYR B N   1 
ATOM   800   C CA  . TYR A 1 116  ? 217.177 193.104 289.337 1.00 70.07  ? 99   TYR B CA  1 
ATOM   801   C C   . TYR A 1 116  ? 218.040 192.552 288.213 1.00 70.07  ? 99   TYR B C   1 
ATOM   802   O O   . TYR A 1 116  ? 218.876 193.280 287.669 1.00 70.07  ? 99   TYR B O   1 
ATOM   803   C CB  . TYR A 1 116  ? 217.914 192.968 290.664 1.00 70.07  ? 99   TYR B CB  1 
ATOM   804   C CG  . TYR A 1 116  ? 219.210 193.741 290.715 1.00 70.07  ? 99   TYR B CG  1 
ATOM   805   C CD1 . TYR A 1 116  ? 219.219 195.095 291.009 1.00 70.07  ? 99   TYR B CD1 1 
ATOM   806   C CD2 . TYR A 1 116  ? 220.422 193.118 290.467 1.00 70.07  ? 99   TYR B CD2 1 
ATOM   807   C CE1 . TYR A 1 116  ? 220.397 195.806 291.059 1.00 70.07  ? 99   TYR B CE1 1 
ATOM   808   C CE2 . TYR A 1 116  ? 221.606 193.821 290.513 1.00 70.07  ? 99   TYR B CE2 1 
ATOM   809   C CZ  . TYR A 1 116  ? 221.588 195.165 290.809 1.00 70.07  ? 99   TYR B CZ  1 
ATOM   810   O OH  . TYR A 1 116  ? 222.766 195.871 290.858 1.00 70.07  ? 99   TYR B OH  1 
ATOM   811   N N   . SER A 1 117  ? 217.877 191.274 287.864 1.00 71.56  ? 100  SER B N   1 
ATOM   812   C CA  . SER A 1 117  ? 218.695 190.700 286.801 1.00 71.56  ? 100  SER B CA  1 
ATOM   813   C C   . SER A 1 117  ? 218.444 191.397 285.470 1.00 71.56  ? 100  SER B C   1 
ATOM   814   O O   . SER A 1 117  ? 219.385 191.670 284.716 1.00 71.56  ? 100  SER B O   1 
ATOM   815   C CB  . SER A 1 117  ? 218.423 189.203 286.678 1.00 71.56  ? 100  SER B CB  1 
ATOM   816   O OG  . SER A 1 117  ? 217.421 188.951 285.710 1.00 71.56  ? 100  SER B OG  1 
ATOM   817   N N   . THR A 1 118  ? 217.185 191.692 285.165 1.00 75.59  ? 101  THR B N   1 
ATOM   818   C CA  . THR A 1 118  ? 216.845 192.353 283.913 1.00 75.59  ? 101  THR B CA  1 
ATOM   819   C C   . THR A 1 118  ? 217.426 193.762 283.879 1.00 75.59  ? 101  THR B C   1 
ATOM   820   O O   . THR A 1 118  ? 217.404 194.483 284.880 1.00 75.59  ? 101  THR B O   1 
ATOM   821   C CB  . THR A 1 118  ? 215.324 192.393 283.740 1.00 75.59  ? 101  THR B CB  1 
ATOM   822   O OG1 . THR A 1 118  ? 214.869 191.126 283.253 1.00 75.59  ? 101  THR B OG1 1 
ATOM   823   C CG2 . THR A 1 118  ? 214.906 193.477 282.763 1.00 75.59  ? 101  THR B CG2 1 
ATOM   824   N N   . ASP A 1 119  ? 217.957 194.148 282.714 1.00 80.40  ? 102  ASP B N   1 
ATOM   825   C CA  . ASP A 1 119  ? 218.577 195.462 282.569 1.00 80.40  ? 102  ASP B CA  1 
ATOM   826   C C   . ASP A 1 119  ? 217.599 196.572 282.931 1.00 80.40  ? 102  ASP B C   1 
ATOM   827   O O   . ASP A 1 119  ? 217.937 197.497 283.681 1.00 80.40  ? 102  ASP B O   1 
ATOM   828   C CB  . ASP A 1 119  ? 219.084 195.640 281.139 1.00 80.40  ? 102  ASP B CB  1 
ATOM   829   C CG  . ASP A 1 119  ? 220.520 195.188 280.969 1.00 80.40  ? 102  ASP B CG  1 
ATOM   830   O OD1 . ASP A 1 119  ? 221.069 194.577 281.909 1.00 80.40  ? 102  ASP B OD1 1 
ATOM   831   O OD2 . ASP A 1 119  ? 221.099 195.441 279.892 1.00 80.40  ? 102  ASP B OD2 1 
ATOM   832   N N   . LEU A 1 120  ? 216.373 196.489 282.412 1.00 74.01  ? 103  LEU B N   1 
ATOM   833   C CA  . LEU A 1 120  ? 215.346 197.454 282.788 1.00 74.01  ? 103  LEU B CA  1 
ATOM   834   C C   . LEU A 1 120  ? 215.062 197.394 284.281 1.00 74.01  ? 103  LEU B C   1 
ATOM   835   O O   . LEU A 1 120  ? 214.914 198.432 284.936 1.00 74.01  ? 103  LEU B O   1 
ATOM   836   C CB  . LEU A 1 120  ? 214.070 197.197 281.995 1.00 74.01  ? 103  LEU B CB  1 
ATOM   837   C CG  . LEU A 1 120  ? 213.054 198.334 282.008 1.00 74.01  ? 103  LEU B CG  1 
ATOM   838   C CD1 . LEU A 1 120  ? 213.752 199.678 281.991 1.00 74.01  ? 103  LEU B CD1 1 
ATOM   839   C CD2 . LEU A 1 120  ? 212.129 198.205 280.828 1.00 74.01  ? 103  LEU B CD2 1 
ATOM   840   N N   . GLY A 1 121  ? 214.981 196.186 284.836 1.00 72.72  ? 104  GLY B N   1 
ATOM   841   C CA  . GLY A 1 121  ? 214.800 196.060 286.270 1.00 72.72  ? 104  GLY B CA  1 
ATOM   842   C C   . GLY A 1 121  ? 215.967 196.627 287.053 1.00 72.72  ? 104  GLY B C   1 
ATOM   843   O O   . GLY A 1 121  ? 215.782 197.234 288.109 1.00 72.72  ? 104  GLY B O   1 
ATOM   844   N N   . ARG A 1 122  ? 217.187 196.428 286.552 1.00 75.53  ? 105  ARG B N   1 
ATOM   845   C CA  . ARG A 1 122  ? 218.351 196.998 287.219 1.00 75.53  ? 105  ARG B CA  1 
ATOM   846   C C   . ARG A 1 122  ? 218.262 198.517 287.258 1.00 75.53  ? 105  ARG B C   1 
ATOM   847   O O   . ARG A 1 122  ? 218.508 199.137 288.302 1.00 75.53  ? 105  ARG B O   1 
ATOM   848   C CB  . ARG A 1 122  ? 219.628 196.544 286.514 1.00 75.53  ? 105  ARG B CB  1 
ATOM   849   C CG  . ARG A 1 122  ? 220.906 196.955 287.215 1.00 75.53  ? 105  ARG B CG  1 
ATOM   850   C CD  . ARG A 1 122  ? 222.121 196.691 286.343 1.00 75.53  ? 105  ARG B CD  1 
ATOM   851   N NE  . ARG A 1 122  ? 223.360 197.089 287.000 1.00 75.53  ? 105  ARG B NE  1 
ATOM   852   C CZ  . ARG A 1 122  ? 224.199 196.249 287.590 1.00 75.53  ? 105  ARG B CZ  1 
ATOM   853   N NH1 . ARG A 1 122  ? 223.960 194.950 287.632 1.00 75.53  ? 105  ARG B NH1 1 
ATOM   854   N NH2 . ARG A 1 122  ? 225.305 196.726 288.154 1.00 75.53  ? 105  ARG B NH2 1 
ATOM   855   N N   . MET A 1 123  ? 217.883 199.130 286.134 1.00 75.53  ? 106  MET B N   1 
ATOM   856   C CA  . MET A 1 123  ? 217.711 200.579 286.105 1.00 75.53  ? 106  MET B CA  1 
ATOM   857   C C   . MET A 1 123  ? 216.612 201.021 287.062 1.00 75.53  ? 106  MET B C   1 
ATOM   858   O O   . MET A 1 123  ? 216.761 202.024 287.769 1.00 75.53  ? 106  MET B O   1 
ATOM   859   C CB  . MET A 1 123  ? 217.396 201.044 284.685 1.00 75.53  ? 106  MET B CB  1 
ATOM   860   C CG  . MET A 1 123  ? 218.557 201.701 283.971 1.00 75.53  ? 106  MET B CG  1 
ATOM   861   S SD  . MET A 1 123  ? 218.202 201.952 282.225 1.00 75.53  ? 106  MET B SD  1 
ATOM   862   C CE  . MET A 1 123  ? 217.597 200.330 281.778 1.00 75.53  ? 106  MET B CE  1 
ATOM   863   N N   . LEU A 1 124  ? 215.500 200.285 287.095 1.00 69.60  ? 107  LEU B N   1 
ATOM   864   C CA  . LEU A 1 124  ? 214.391 200.658 287.968 1.00 69.60  ? 107  LEU B CA  1 
ATOM   865   C C   . LEU A 1 124  ? 214.808 200.619 289.432 1.00 69.60  ? 107  LEU B C   1 
ATOM   866   O O   . LEU A 1 124  ? 214.529 201.552 290.195 1.00 69.60  ? 107  LEU B O   1 
ATOM   867   C CB  . LEU A 1 124  ? 213.199 199.733 287.725 1.00 69.60  ? 107  LEU B CB  1 
ATOM   868   C CG  . LEU A 1 124  ? 211.990 199.934 288.637 1.00 69.60  ? 107  LEU B CG  1 
ATOM   869   C CD1 . LEU A 1 124  ? 211.620 201.402 288.740 1.00 69.60  ? 107  LEU B CD1 1 
ATOM   870   C CD2 . LEU A 1 124  ? 210.817 199.130 288.135 1.00 69.60  ? 107  LEU B CD2 1 
ATOM   871   N N   . LEU A 1 125  ? 215.475 199.539 289.845 1.00 69.60  ? 108  LEU B N   1 
ATOM   872   C CA  . LEU A 1 125  ? 215.897 199.426 291.237 1.00 69.60  ? 108  LEU B CA  1 
ATOM   873   C C   . LEU A 1 125  ? 216.933 200.484 291.590 1.00 69.60  ? 108  LEU B C   1 
ATOM   874   O O   . LEU A 1 125  ? 216.892 201.056 292.686 1.00 69.60  ? 108  LEU B O   1 
ATOM   875   C CB  . LEU A 1 125  ? 216.432 198.025 291.525 1.00 69.60  ? 108  LEU B CB  1 
ATOM   876   C CG  . LEU A 1 125  ? 215.396 196.998 291.986 1.00 69.60  ? 108  LEU B CG  1 
ATOM   877   C CD1 . LEU A 1 125  ? 214.602 197.547 293.153 1.00 69.60  ? 108  LEU B CD1 1 
ATOM   878   C CD2 . LEU A 1 125  ? 214.468 196.609 290.870 1.00 69.60  ? 108  LEU B CD2 1 
ATOM   879   N N   . THR A 1 126  ? 217.867 200.766 290.678 1.00 71.05  ? 109  THR B N   1 
ATOM   880   C CA  . THR A 1 126  ? 218.847 201.809 290.957 1.00 71.05  ? 109  THR B CA  1 
ATOM   881   C C   . THR A 1 126  ? 218.170 203.164 291.120 1.00 71.05  ? 109  THR B C   1 
ATOM   882   O O   . THR A 1 126  ? 218.506 203.927 292.033 1.00 71.05  ? 109  THR B O   1 
ATOM   883   C CB  . THR A 1 126  ? 219.896 201.857 289.849 1.00 71.05  ? 109  THR B CB  1 
ATOM   884   O OG1 . THR A 1 126  ? 220.664 200.649 289.867 1.00 71.05  ? 109  THR B OG1 1 
ATOM   885   C CG2 . THR A 1 126  ? 220.830 203.034 290.062 1.00 71.05  ? 109  THR B CG2 1 
ATOM   886   N N   . SER A 1 127  ? 217.201 203.475 290.255 1.00 69.92  ? 110  SER B N   1 
ATOM   887   C CA  . SER A 1 127  ? 216.500 204.752 290.359 1.00 69.92  ? 110  SER B CA  1 
ATOM   888   C C   . SER A 1 127  ? 215.689 204.839 291.644 1.00 69.92  ? 110  SER B C   1 
ATOM   889   O O   . SER A 1 127  ? 215.629 205.899 292.277 1.00 69.92  ? 110  SER B O   1 
ATOM   890   C CB  . SER A 1 127  ? 215.599 204.960 289.143 1.00 69.92  ? 110  SER B CB  1 
ATOM   891   O OG  . SER A 1 127  ? 216.333 205.477 288.049 1.00 69.92  ? 110  SER B OG  1 
ATOM   892   N N   . ILE A 1 128  ? 215.044 203.740 292.040 1.00 69.60  ? 111  ILE B N   1 
ATOM   893   C CA  . ILE A 1 128  ? 214.255 203.745 293.269 1.00 69.60  ? 111  ILE B CA  1 
ATOM   894   C C   . ILE A 1 128  ? 215.156 203.942 294.480 1.00 69.60  ? 111  ILE B C   1 
ATOM   895   O O   . ILE A 1 128  ? 214.818 204.685 295.410 1.00 69.60  ? 111  ILE B O   1 
ATOM   896   C CB  . ILE A 1 128  ? 213.426 202.454 293.380 1.00 69.60  ? 111  ILE B CB  1 
ATOM   897   C CG1 . ILE A 1 128  ? 212.114 202.603 292.617 1.00 69.60  ? 111  ILE B CG1 1 
ATOM   898   C CG2 . ILE A 1 128  ? 213.148 202.114 294.828 1.00 69.60  ? 111  ILE B CG2 1 
ATOM   899   C CD1 . ILE A 1 128  ? 211.258 201.370 292.649 1.00 69.60  ? 111  ILE B CD1 1 
ATOM   900   N N   . VAL A 1 129  ? 216.317 203.283 294.491 1.00 69.77  ? 112  VAL B N   1 
ATOM   901   C CA  . VAL A 1 129  ? 217.241 203.430 295.610 1.00 69.77  ? 112  VAL B CA  1 
ATOM   902   C C   . VAL A 1 129  ? 217.804 204.846 295.662 1.00 69.77  ? 112  VAL B C   1 
ATOM   903   O O   . VAL A 1 129  ? 217.951 205.431 296.741 1.00 69.77  ? 112  VAL B O   1 
ATOM   904   C CB  . VAL A 1 129  ? 218.359 202.377 295.517 1.00 69.77  ? 112  VAL B CB  1 
ATOM   905   C CG1 . VAL A 1 129  ? 219.509 202.742 296.430 1.00 69.77  ? 112  VAL B CG1 1 
ATOM   906   C CG2 . VAL A 1 129  ? 217.819 201.003 295.864 1.00 69.77  ? 112  VAL B CG2 1 
ATOM   907   N N   . ARG A 1 130  ? 218.128 205.419 294.500 1.00 75.38  ? 113  ARG B N   1 
ATOM   908   C CA  . ARG A 1 130  ? 218.722 206.752 294.469 1.00 75.38  ? 113  ARG B CA  1 
ATOM   909   C C   . ARG A 1 130  ? 217.735 207.821 294.920 1.00 75.38  ? 113  ARG B C   1 
ATOM   910   O O   . ARG A 1 130  ? 218.108 208.746 295.649 1.00 75.38  ? 113  ARG B O   1 
ATOM   911   C CB  . ARG A 1 130  ? 219.232 207.066 293.064 1.00 75.38  ? 113  ARG B CB  1 
ATOM   912   C CG  . ARG A 1 130  ? 220.647 206.588 292.797 1.00 75.38  ? 113  ARG B CG  1 
ATOM   913   C CD  . ARG A 1 130  ? 221.430 207.613 292.003 1.00 75.38  ? 113  ARG B CD  1 
ATOM   914   N NE  . ARG A 1 130  ? 220.608 208.249 290.982 1.00 75.38  ? 113  ARG B NE  1 
ATOM   915   C CZ  . ARG A 1 130  ? 220.623 207.920 289.698 1.00 75.38  ? 113  ARG B CZ  1 
ATOM   916   N NH1 . ARG A 1 130  ? 221.412 206.963 289.240 1.00 75.38  ? 113  ARG B NH1 1 
ATOM   917   N NH2 . ARG A 1 130  ? 219.826 208.568 288.853 1.00 75.38  ? 113  ARG B NH2 1 
ATOM   918   N N   . GLY A 1 131  ? 216.476 207.707 294.512 1.00 69.60  ? 114  GLY B N   1 
ATOM   919   C CA  . GLY A 1 131  ? 215.523 208.783 294.696 1.00 69.60  ? 114  GLY B CA  1 
ATOM   920   C C   . GLY A 1 131  ? 214.953 208.922 296.092 1.00 69.60  ? 114  GLY B C   1 
ATOM   921   O O   . GLY A 1 131  ? 213.794 208.574 296.325 1.00 69.60  ? 114  GLY B O   1 
ATOM   922   N N   . ILE A 1 132  ? 215.746 209.432 297.028 1.00 69.75  ? 115  ILE B N   1 
ATOM   923   C CA  . ILE A 1 132  ? 215.281 209.632 298.398 1.00 69.75  ? 115  ILE B CA  1 
ATOM   924   C C   . ILE A 1 132  ? 214.286 210.789 298.424 1.00 69.75  ? 115  ILE B C   1 
ATOM   925   O O   . ILE A 1 132  ? 214.326 211.658 297.541 1.00 69.75  ? 115  ILE B O   1 
ATOM   926   C CB  . ILE A 1 132  ? 216.454 209.887 299.357 1.00 69.75  ? 115  ILE B CB  1 
ATOM   927   C CG1 . ILE A 1 132  ? 217.028 211.284 299.150 1.00 69.75  ? 115  ILE B CG1 1 
ATOM   928   C CG2 . ILE A 1 132  ? 217.543 208.854 299.148 1.00 69.75  ? 115  ILE B CG2 1 
ATOM   929   C CD1 . ILE A 1 132  ? 218.191 211.589 300.056 1.00 69.75  ? 115  ILE B CD1 1 
ATOM   930   N N   . PRO A 1 133  ? 213.367 210.829 299.385 1.00 70.57  ? 116  PRO B N   1 
ATOM   931   C CA  . PRO A 1 133  ? 212.447 211.967 299.478 1.00 70.57  ? 116  PRO B CA  1 
ATOM   932   C C   . PRO A 1 133  ? 213.163 213.257 299.842 1.00 70.57  ? 116  PRO B C   1 
ATOM   933   O O   . PRO A 1 133  ? 214.156 213.262 300.571 1.00 70.57  ? 116  PRO B O   1 
ATOM   934   C CB  . PRO A 1 133  ? 211.475 211.546 300.585 1.00 70.57  ? 116  PRO B CB  1 
ATOM   935   C CG  . PRO A 1 133  ? 211.581 210.060 300.636 1.00 70.57  ? 116  PRO B CG  1 
ATOM   936   C CD  . PRO A 1 133  ? 213.005 209.754 300.321 1.00 70.57  ? 116  PRO B CD  1 
ATOM   937   N N   . PHE A 1 134  ? 212.627 214.363 299.332 1.00 78.42  ? 117  PHE B N   1 
ATOM   938   C CA  . PHE A 1 134  ? 213.213 215.676 299.562 1.00 78.42  ? 117  PHE B CA  1 
ATOM   939   C C   . PHE A 1 134  ? 213.012 216.118 301.007 1.00 78.42  ? 117  PHE B C   1 
ATOM   940   O O   . PHE A 1 134  ? 212.028 215.762 301.659 1.00 78.42  ? 117  PHE B O   1 
ATOM   941   C CB  . PHE A 1 134  ? 212.600 216.700 298.605 1.00 78.42  ? 117  PHE B CB  1 
ATOM   942   C CG  . PHE A 1 134  ? 213.188 218.081 298.718 1.00 78.42  ? 117  PHE B CG  1 
ATOM   943   C CD1 . PHE A 1 134  ? 214.357 218.407 298.061 1.00 78.42  ? 117  PHE B CD1 1 
ATOM   944   C CD2 . PHE A 1 134  ? 212.555 219.058 299.463 1.00 78.42  ? 117  PHE B CD2 1 
ATOM   945   C CE1 . PHE A 1 134  ? 214.888 219.676 298.155 1.00 78.42  ? 117  PHE B CE1 1 
ATOM   946   C CE2 . PHE A 1 134  ? 213.086 220.326 299.561 1.00 78.42  ? 117  PHE B CE2 1 
ATOM   947   C CZ  . PHE A 1 134  ? 214.253 220.633 298.906 1.00 78.42  ? 117  PHE B CZ  1 
ATOM   948   N N   . TRP A 1 135  ? 213.963 216.907 301.503 1.00 87.58  ? 118  TRP B N   1 
ATOM   949   C CA  . TRP A 1 135  ? 213.928 217.420 302.872 1.00 87.58  ? 118  TRP B CA  1 
ATOM   950   C C   . TRP A 1 135  ? 213.240 218.777 302.859 1.00 87.58  ? 118  TRP B C   1 
ATOM   951   O O   . TRP A 1 135  ? 213.865 219.814 302.640 1.00 87.58  ? 118  TRP B O   1 
ATOM   952   C CB  . TRP A 1 135  ? 215.336 217.516 303.445 1.00 87.58  ? 118  TRP B CB  1 
ATOM   953   C CG  . TRP A 1 135  ? 215.931 216.204 303.835 1.00 87.58  ? 118  TRP B CG  1 
ATOM   954   C CD1 . TRP A 1 135  ? 215.859 215.033 303.143 1.00 87.58  ? 118  TRP B CD1 1 
ATOM   955   C CD2 . TRP A 1 135  ? 216.703 215.931 305.008 1.00 87.58  ? 118  TRP B CD2 1 
ATOM   956   N NE1 . TRP A 1 135  ? 216.535 214.043 303.815 1.00 87.58  ? 118  TRP B NE1 1 
ATOM   957   C CE2 . TRP A 1 135  ? 217.063 214.571 304.964 1.00 87.58  ? 118  TRP B CE2 1 
ATOM   958   C CE3 . TRP A 1 135  ? 217.124 216.704 306.093 1.00 87.58  ? 118  TRP B CE3 1 
ATOM   959   C CZ2 . TRP A 1 135  ? 217.821 213.968 305.962 1.00 87.58  ? 118  TRP B CZ2 1 
ATOM   960   C CZ3 . TRP A 1 135  ? 217.877 216.105 307.081 1.00 87.58  ? 118  TRP B CZ3 1 
ATOM   961   C CH2 . TRP A 1 135  ? 218.217 214.751 307.010 1.00 87.58  ? 118  TRP B CH2 1 
ATOM   962   N N   . GLY A 1 136  ? 211.934 218.774 303.104 1.00 91.28  ? 119  GLY B N   1 
ATOM   963   C CA  . GLY A 1 136  ? 211.173 220.008 303.103 1.00 91.28  ? 119  GLY B CA  1 
ATOM   964   C C   . GLY A 1 136  ? 210.298 220.185 304.326 1.00 91.28  ? 119  GLY B C   1 
ATOM   965   O O   . GLY A 1 136  ? 209.188 220.715 304.229 1.00 91.28  ? 119  GLY B O   1 
ATOM   966   N N   . GLY A 1 137  ? 210.781 219.745 305.481 1.00 98.66  ? 120  GLY B N   1 
ATOM   967   C CA  . GLY A 1 137  ? 210.031 219.836 306.715 1.00 98.66  ? 120  GLY B CA  1 
ATOM   968   C C   . GLY A 1 137  ? 210.242 221.096 307.522 1.00 98.66  ? 120  GLY B C   1 
ATOM   969   O O   . GLY A 1 137  ? 209.707 221.197 308.631 1.00 98.66  ? 120  GLY B O   1 
ATOM   970   N N   . SER A 1 138  ? 210.999 222.060 307.011 1.00 105.46 ? 121  SER B N   1 
ATOM   971   C CA  . SER A 1 138  ? 211.301 223.283 307.740 1.00 105.46 ? 121  SER B CA  1 
ATOM   972   C C   . SER A 1 138  ? 210.334 224.383 307.330 1.00 105.46 ? 121  SER B C   1 
ATOM   973   O O   . SER A 1 138  ? 210.144 224.637 306.136 1.00 105.46 ? 121  SER B O   1 
ATOM   974   C CB  . SER A 1 138  ? 212.741 223.729 307.489 1.00 105.46 ? 121  SER B CB  1 
ATOM   975   O OG  . SER A 1 138  ? 213.002 224.967 308.126 1.00 105.46 ? 121  SER B OG  1 
ATOM   976   N N   . THR A 1 139  ? 209.721 225.029 308.324 1.00 112.10 ? 122  THR B N   1 
ATOM   977   C CA  . THR A 1 139  ? 208.823 226.143 308.038 1.00 112.10 ? 122  THR B CA  1 
ATOM   978   C C   . THR A 1 139  ? 209.580 227.329 307.452 1.00 112.10 ? 122  THR B C   1 
ATOM   979   O O   . THR A 1 139  ? 209.098 227.980 306.517 1.00 112.10 ? 122  THR B O   1 
ATOM   980   C CB  . THR A 1 139  ? 208.080 226.558 309.308 1.00 112.10 ? 122  THR B CB  1 
ATOM   981   O OG1 . THR A 1 139  ? 208.975 227.266 310.175 1.00 112.10 ? 122  THR B OG1 1 
ATOM   982   C CG2 . THR A 1 139  ? 207.541 225.333 310.033 1.00 112.10 ? 122  THR B CG2 1 
ATOM   983   N N   . ILE A 1 140  ? 210.760 227.624 307.984 1.00 109.64 ? 123  ILE B N   1 
ATOM   984   C CA  . ILE A 1 140  ? 211.574 228.725 307.482 1.00 109.64 ? 123  ILE B CA  1 
ATOM   985   C C   . ILE A 1 140  ? 212.174 228.320 306.141 1.00 109.64 ? 123  ILE B C   1 
ATOM   986   O O   . ILE A 1 140  ? 212.673 227.199 305.983 1.00 109.64 ? 123  ILE B O   1 
ATOM   987   C CB  . ILE A 1 140  ? 212.660 229.105 308.502 1.00 109.64 ? 123  ILE B CB  1 
ATOM   988   C CG1 . ILE A 1 140  ? 212.074 230.004 309.593 1.00 109.64 ? 123  ILE B CG1 1 
ATOM   989   C CG2 . ILE A 1 140  ? 213.825 229.794 307.823 1.00 109.64 ? 123  ILE B CG2 1 
ATOM   990   C CD1 . ILE A 1 140  ? 212.053 231.473 309.234 1.00 109.64 ? 123  ILE B CD1 1 
ATOM   991   N N   . ASP A 1 141  ? 212.125 229.234 305.170 1.00 107.67 ? 124  ASP B N   1 
ATOM   992   C CA  . ASP A 1 141  ? 212.422 228.903 303.781 1.00 107.67 ? 124  ASP B CA  1 
ATOM   993   C C   . ASP A 1 141  ? 213.900 228.646 303.506 1.00 107.67 ? 124  ASP B C   1 
ATOM   994   O O   . ASP A 1 141  ? 214.220 228.113 302.439 1.00 107.67 ? 124  ASP B O   1 
ATOM   995   C CB  . ASP A 1 141  ? 211.922 230.022 302.868 1.00 107.67 ? 124  ASP B CB  1 
ATOM   996   C CG  . ASP A 1 141  ? 212.556 231.360 303.187 1.00 107.67 ? 124  ASP B CG  1 
ATOM   997   O OD1 . ASP A 1 141  ? 213.219 231.471 304.240 1.00 107.67 ? 124  ASP B OD1 1 
ATOM   998   O OD2 . ASP A 1 141  ? 212.392 232.303 302.385 1.00 107.67 ? 124  ASP B OD2 1 
ATOM   999   N N   . THR A 1 142  ? 214.805 229.006 304.415 1.00 105.27 ? 125  THR B N   1 
ATOM   1000  C CA  . THR A 1 142  ? 216.234 228.827 304.183 1.00 105.27 ? 125  THR B CA  1 
ATOM   1001  C C   . THR A 1 142  ? 216.815 227.679 305.002 1.00 105.27 ? 125  THR B C   1 
ATOM   1002  O O   . THR A 1 142  ? 217.985 227.716 305.386 1.00 105.27 ? 125  THR B O   1 
ATOM   1003  C CB  . THR A 1 142  ? 217.002 230.115 304.473 1.00 105.27 ? 125  THR B CB  1 
ATOM   1004  O OG1 . THR A 1 142  ? 218.403 229.825 304.556 1.00 105.27 ? 125  THR B OG1 1 
ATOM   1005  C CG2 . THR A 1 142  ? 216.548 230.728 305.780 1.00 105.27 ? 125  THR B CG2 1 
ATOM   1006  N N   . GLU A 1 143  ? 216.009 226.656 305.284 1.00 103.92 ? 126  GLU B N   1 
ATOM   1007  C CA  . GLU A 1 143  ? 216.477 225.476 305.995 1.00 103.92 ? 126  GLU B CA  1 
ATOM   1008  C C   . GLU A 1 143  ? 215.907 224.229 305.338 1.00 103.92 ? 126  GLU B C   1 
ATOM   1009  O O   . GLU A 1 143  ? 214.865 224.277 304.680 1.00 103.92 ? 126  GLU B O   1 
ATOM   1010  C CB  . GLU A 1 143  ? 216.083 225.504 307.478 1.00 103.92 ? 126  GLU B CB  1 
ATOM   1011  C CG  . GLU A 1 143  ? 216.316 226.835 308.170 1.00 103.92 ? 126  GLU B CG  1 
ATOM   1012  C CD  . GLU A 1 143  ? 215.642 226.909 309.522 1.00 103.92 ? 126  GLU B CD  1 
ATOM   1013  O OE1 . GLU A 1 143  ? 214.428 226.631 309.596 1.00 103.92 ? 126  GLU B OE1 1 
ATOM   1014  O OE2 . GLU A 1 143  ? 216.325 227.252 310.510 1.00 103.92 ? 126  GLU B OE2 1 
ATOM   1015  N N   . LEU A 1 144  ? 216.605 223.112 305.519 1.00 95.01  ? 127  LEU B N   1 
ATOM   1016  C CA  . LEU A 1 144  ? 216.148 221.806 305.066 1.00 95.01  ? 127  LEU B CA  1 
ATOM   1017  C C   . LEU A 1 144  ? 215.964 220.904 306.276 1.00 95.01  ? 127  LEU B C   1 
ATOM   1018  O O   . LEU A 1 144  ? 216.873 220.778 307.102 1.00 95.01  ? 127  LEU B O   1 
ATOM   1019  C CB  . LEU A 1 144  ? 217.141 221.174 304.086 1.00 95.01  ? 127  LEU B CB  1 
ATOM   1020  C CG  . LEU A 1 144  ? 217.490 221.948 302.814 1.00 95.01  ? 127  LEU B CG  1 
ATOM   1021  C CD1 . LEU A 1 144  ? 218.912 221.640 302.384 1.00 95.01  ? 127  LEU B CD1 1 
ATOM   1022  C CD2 . LEU A 1 144  ? 216.519 221.618 301.699 1.00 95.01  ? 127  LEU B CD2 1 
ATOM   1023  N N   . LYS A 1 145  ? 214.792 220.286 306.383 1.00 93.93  ? 128  LYS B N   1 
ATOM   1024  C CA  . LYS A 1 145  ? 214.497 219.375 307.478 1.00 93.93  ? 128  LYS B CA  1 
ATOM   1025  C C   . LYS A 1 145  ? 213.725 218.179 306.942 1.00 93.93  ? 128  LYS B C   1 
ATOM   1026  O O   . LYS A 1 145  ? 212.857 218.329 306.078 1.00 93.93  ? 128  LYS B O   1 
ATOM   1027  C CB  . LYS A 1 145  ? 213.694 220.071 308.584 1.00 93.93  ? 128  LYS B CB  1 
ATOM   1028  C CG  . LYS A 1 145  ? 213.316 219.168 309.744 1.00 93.93  ? 128  LYS B CG  1 
ATOM   1029  C CD  . LYS A 1 145  ? 213.047 219.973 311.001 1.00 93.93  ? 128  LYS B CD  1 
ATOM   1030  C CE  . LYS A 1 145  ? 211.560 220.217 311.190 1.00 93.93  ? 128  LYS B CE  1 
ATOM   1031  N NZ  . LYS A 1 145  ? 210.897 219.092 311.902 1.00 93.93  ? 128  LYS B NZ  1 
ATOM   1032  N N   . VAL A 1 146  ? 214.049 216.993 307.458 1.00 90.13  ? 129  VAL B N   1 
ATOM   1033  C CA  . VAL A 1 146  ? 213.403 215.771 306.996 1.00 90.13  ? 129  VAL B CA  1 
ATOM   1034  C C   . VAL A 1 146  ? 211.933 215.768 307.400 1.00 90.13  ? 129  VAL B C   1 
ATOM   1035  O O   . VAL A 1 146  ? 211.543 216.318 308.438 1.00 90.13  ? 129  VAL B O   1 
ATOM   1036  C CB  . VAL A 1 146  ? 214.137 214.537 307.551 1.00 90.13  ? 129  VAL B CB  1 
ATOM   1037  C CG1 . VAL A 1 146  ? 213.947 214.430 309.055 1.00 90.13  ? 129  VAL B CG1 1 
ATOM   1038  C CG2 . VAL A 1 146  ? 213.658 213.271 306.858 1.00 90.13  ? 129  VAL B CG2 1 
ATOM   1039  N N   . ILE A 1 147  ? 211.100 215.158 306.556 1.00 86.45  ? 130  ILE B N   1 
ATOM   1040  C CA  . ILE A 1 147  ? 209.701 214.952 306.904 1.00 86.45  ? 130  ILE B CA  1 
ATOM   1041  C C   . ILE A 1 147  ? 209.622 213.903 308.003 1.00 86.45  ? 130  ILE B C   1 
ATOM   1042  O O   . ILE A 1 147  ? 210.196 212.814 307.883 1.00 86.45  ? 130  ILE B O   1 
ATOM   1043  C CB  . ILE A 1 147  ? 208.896 214.519 305.670 1.00 86.45  ? 130  ILE B CB  1 
ATOM   1044  C CG1 . ILE A 1 147  ? 208.895 215.612 304.602 1.00 86.45  ? 130  ILE B CG1 1 
ATOM   1045  C CG2 . ILE A 1 147  ? 207.467 214.195 306.064 1.00 86.45  ? 130  ILE B CG2 1 
ATOM   1046  C CD1 . ILE A 1 147  ? 208.690 216.997 305.142 1.00 86.45  ? 130  ILE B CD1 1 
ATOM   1047  N N   . ASP A 1 148  ? 208.911 214.225 309.085 1.00 85.94  ? 131  ASP B N   1 
ATOM   1048  C CA  . ASP A 1 148  ? 208.840 213.304 310.214 1.00 85.94  ? 131  ASP B CA  1 
ATOM   1049  C C   . ASP A 1 148  ? 208.138 211.999 309.864 1.00 85.94  ? 131  ASP B C   1 
ATOM   1050  O O   . ASP A 1 148  ? 208.363 210.992 310.542 1.00 85.94  ? 131  ASP B O   1 
ATOM   1051  C CB  . ASP A 1 148  ? 208.134 213.967 311.394 1.00 85.94  ? 131  ASP B CB  1 
ATOM   1052  C CG  . ASP A 1 148  ? 208.955 215.076 312.011 1.00 85.94  ? 131  ASP B CG  1 
ATOM   1053  O OD1 . ASP A 1 148  ? 209.862 215.591 311.325 1.00 85.94  ? 131  ASP B OD1 1 
ATOM   1054  O OD2 . ASP A 1 148  ? 208.700 215.428 313.181 1.00 85.94  ? 131  ASP B OD2 1 
ATOM   1055  N N   . THR A 1 149  ? 207.307 211.988 308.827 1.00 83.37  ? 132  THR B N   1 
ATOM   1056  C CA  . THR A 1 149  ? 206.557 210.800 308.445 1.00 83.37  ? 132  THR B CA  1 
ATOM   1057  C C   . THR A 1 149  ? 207.263 209.964 307.390 1.00 83.37  ? 132  THR B C   1 
ATOM   1058  O O   . THR A 1 149  ? 206.692 208.972 306.928 1.00 83.37  ? 132  THR B O   1 
ATOM   1059  C CB  . THR A 1 149  ? 205.172 211.192 307.928 1.00 83.37  ? 132  THR B CB  1 
ATOM   1060  O OG1 . THR A 1 149  ? 205.245 211.435 306.519 1.00 83.37  ? 132  THR B OG1 1 
ATOM   1061  C CG2 . THR A 1 149  ? 204.679 212.450 308.627 1.00 83.37  ? 132  THR B CG2 1 
ATOM   1062  N N   . ASN A 1 150  ? 208.475 210.339 306.991 1.00 78.60  ? 133  ASN B N   1 
ATOM   1063  C CA  . ASN A 1 150  ? 209.237 209.615 305.980 1.00 78.60  ? 133  ASN B CA  1 
ATOM   1064  C C   . ASN A 1 150  ? 210.424 208.881 306.593 1.00 78.60  ? 133  ASN B C   1 
ATOM   1065  O O   . ASN A 1 150  ? 211.511 208.839 306.016 1.00 78.60  ? 133  ASN B O   1 
ATOM   1066  C CB  . ASN A 1 150  ? 209.715 210.557 304.880 1.00 78.60  ? 133  ASN B CB  1 
ATOM   1067  C CG  . ASN A 1 150  ? 208.574 211.242 304.165 1.00 78.60  ? 133  ASN B CG  1 
ATOM   1068  O OD1 . ASN A 1 150  ? 207.415 211.111 304.555 1.00 78.60  ? 133  ASN B OD1 1 
ATOM   1069  N ND2 . ASN A 1 150  ? 208.895 211.975 303.107 1.00 78.60  ? 133  ASN B ND2 1 
ATOM   1070  N N   . CYS A 1 151  ? 210.230 208.294 307.771 1.00 78.43  ? 134  CYS B N   1 
ATOM   1071  C CA  . CYS A 1 151  ? 211.322 207.630 308.465 1.00 78.43  ? 134  CYS B CA  1 
ATOM   1072  C C   . CYS A 1 151  ? 210.763 206.643 309.480 1.00 78.43  ? 134  CYS B C   1 
ATOM   1073  O O   . CYS A 1 151  ? 209.620 206.767 309.923 1.00 78.43  ? 134  CYS B O   1 
ATOM   1074  C CB  . CYS A 1 151  ? 212.233 208.656 309.143 1.00 78.43  ? 134  CYS B CB  1 
ATOM   1075  S SG  . CYS A 1 151  ? 211.339 209.983 309.952 1.00 78.43  ? 134  CYS B SG  1 
ATOM   1076  N N   . ILE A 1 152  ? 211.592 205.667 309.842 1.00 73.54  ? 135  ILE B N   1 
ATOM   1077  C CA  . ILE A 1 152  ? 211.221 204.608 310.769 1.00 73.54  ? 135  ILE B CA  1 
ATOM   1078  C C   . ILE A 1 152  ? 212.156 204.658 311.969 1.00 73.54  ? 135  ILE B C   1 
ATOM   1079  O O   . ILE A 1 152  ? 213.149 205.384 311.983 1.00 73.54  ? 135  ILE B O   1 
ATOM   1080  C CB  . ILE A 1 152  ? 211.263 203.217 310.115 1.00 73.54  ? 135  ILE B CB  1 
ATOM   1081  C CG1 . ILE A 1 152  ? 212.714 202.776 309.921 1.00 73.54  ? 135  ILE B CG1 1 
ATOM   1082  C CG2 . ILE A 1 152  ? 210.514 203.226 308.803 1.00 73.54  ? 135  ILE B CG2 1 
ATOM   1083  C CD1 . ILE A 1 152  ? 212.888 201.624 308.964 1.00 73.54  ? 135  ILE B CD1 1 
ATOM   1084  N N   . ASN A 1 153  ? 211.817 203.875 312.990 1.00 79.02  ? 136  ASN B N   1 
ATOM   1085  C CA  . ASN A 1 153  ? 212.632 203.735 314.195 1.00 79.02  ? 136  ASN B CA  1 
ATOM   1086  C C   . ASN A 1 153  ? 212.954 202.256 314.364 1.00 79.02  ? 136  ASN B C   1 
ATOM   1087  O O   . ASN A 1 153  ? 212.061 201.461 314.669 1.00 79.02  ? 136  ASN B O   1 
ATOM   1088  C CB  . ASN A 1 153  ? 211.912 204.271 315.429 1.00 79.02  ? 136  ASN B CB  1 
ATOM   1089  C CG  . ASN A 1 153  ? 211.324 205.647 315.217 1.00 79.02  ? 136  ASN B CG  1 
ATOM   1090  O OD1 . ASN A 1 153  ? 211.664 206.345 314.266 1.00 79.02  ? 136  ASN B OD1 1 
ATOM   1091  N ND2 . ASN A 1 153  ? 210.424 206.045 316.109 1.00 79.02  ? 136  ASN B ND2 1 
ATOM   1092  N N   . VAL A 1 154  ? 214.213 201.886 314.149 1.00 79.94  ? 137  VAL B N   1 
ATOM   1093  C CA  . VAL A 1 154  ? 214.684 200.548 314.489 1.00 79.94  ? 137  VAL B CA  1 
ATOM   1094  C C   . VAL A 1 154  ? 215.186 200.577 315.926 1.00 79.94  ? 137  VAL B C   1 
ATOM   1095  O O   . VAL A 1 154  ? 216.069 201.370 316.268 1.00 79.94  ? 137  VAL B O   1 
ATOM   1096  C CB  . VAL A 1 154  ? 215.783 200.073 313.526 1.00 79.94  ? 137  VAL B CB  1 
ATOM   1097  C CG1 . VAL A 1 154  ? 215.187 199.676 312.199 1.00 79.94  ? 137  VAL B CG1 1 
ATOM   1098  C CG2 . VAL A 1 154  ? 216.824 201.154 313.314 1.00 79.94  ? 137  VAL B CG2 1 
ATOM   1099  N N   . ILE A 1 155  ? 214.612 199.737 316.778 1.00 84.28  ? 138  ILE B N   1 
ATOM   1100  C CA  . ILE A 1 155  ? 215.009 199.694 318.180 1.00 84.28  ? 138  ILE B CA  1 
ATOM   1101  C C   . ILE A 1 155  ? 216.144 198.690 318.334 1.00 84.28  ? 138  ILE B C   1 
ATOM   1102  O O   . ILE A 1 155  ? 216.008 197.518 317.969 1.00 84.28  ? 138  ILE B O   1 
ATOM   1103  C CB  . ILE A 1 155  ? 213.827 199.348 319.097 1.00 84.28  ? 138  ILE B CB  1 
ATOM   1104  C CG1 . ILE A 1 155  ? 213.055 198.142 318.574 1.00 84.28  ? 138  ILE B CG1 1 
ATOM   1105  C CG2 . ILE A 1 155  ? 212.896 200.540 319.226 1.00 84.28  ? 138  ILE B CG2 1 
ATOM   1106  C CD1 . ILE A 1 155  ? 211.719 197.955 319.247 1.00 84.28  ? 138  ILE B CD1 1 
ATOM   1107  N N   . GLN A 1 156  ? 217.270 199.158 318.859 1.00 91.88  ? 139  GLN B N   1 
ATOM   1108  C CA  . GLN A 1 156  ? 218.416 198.298 319.066 1.00 91.88  ? 139  GLN B CA  1 
ATOM   1109  C C   . GLN A 1 156  ? 218.172 197.380 320.261 1.00 91.88  ? 139  GLN B C   1 
ATOM   1110  O O   . GLN A 1 156  ? 217.355 197.684 321.132 1.00 91.88  ? 139  GLN B O   1 
ATOM   1111  C CB  . GLN A 1 156  ? 219.671 199.139 319.290 1.00 91.88  ? 139  GLN B CB  1 
ATOM   1112  C CG  . GLN A 1 156  ? 219.782 200.374 318.401 1.00 91.88  ? 139  GLN B CG  1 
ATOM   1113  C CD  . GLN A 1 156  ? 220.092 200.057 316.946 1.00 91.88  ? 139  GLN B CD  1 
ATOM   1114  O OE1 . GLN A 1 156  ? 219.899 198.935 316.479 1.00 91.88  ? 139  GLN B OE1 1 
ATOM   1115  N NE2 . GLN A 1 156  ? 220.579 201.058 316.221 1.00 91.88  ? 139  GLN B NE2 1 
ATOM   1116  N N   . PRO A 1 157  ? 218.868 196.241 320.318 1.00 94.35  ? 140  PRO B N   1 
ATOM   1117  C CA  . PRO A 1 157  ? 218.726 195.355 321.484 1.00 94.35  ? 140  PRO B CA  1 
ATOM   1118  C C   . PRO A 1 157  ? 219.089 196.018 322.801 1.00 94.35  ? 140  PRO B C   1 
ATOM   1119  O O   . PRO A 1 157  ? 218.594 195.585 323.849 1.00 94.35  ? 140  PRO B O   1 
ATOM   1120  C CB  . PRO A 1 157  ? 219.678 194.197 321.160 1.00 94.35  ? 140  PRO B CB  1 
ATOM   1121  C CG  . PRO A 1 157  ? 219.752 194.186 319.675 1.00 94.35  ? 140  PRO B CG  1 
ATOM   1122  C CD  . PRO A 1 157  ? 219.677 195.623 319.254 1.00 94.35  ? 140  PRO B CD  1 
ATOM   1123  N N   . ASP A 1 158  ? 219.938 197.049 322.785 1.00 97.88  ? 141  ASP B N   1 
ATOM   1124  C CA  . ASP A 1 158  ? 220.272 197.751 324.020 1.00 97.88  ? 141  ASP B CA  1 
ATOM   1125  C C   . ASP A 1 158  ? 219.061 198.460 324.615 1.00 97.88  ? 141  ASP B C   1 
ATOM   1126  O O   . ASP A 1 158  ? 218.972 198.604 325.839 1.00 97.88  ? 141  ASP B O   1 
ATOM   1127  C CB  . ASP A 1 158  ? 221.403 198.747 323.768 1.00 97.88  ? 141  ASP B CB  1 
ATOM   1128  C CG  . ASP A 1 158  ? 221.243 199.489 322.457 1.00 97.88  ? 141  ASP B CG  1 
ATOM   1129  O OD1 . ASP A 1 158  ? 220.224 200.192 322.295 1.00 97.88  ? 141  ASP B OD1 1 
ATOM   1130  O OD2 . ASP A 1 158  ? 222.134 199.367 321.590 1.00 97.88  ? 141  ASP B OD2 1 
ATOM   1131  N N   . GLY A 1 159  ? 218.128 198.909 323.777 1.00 97.57  ? 142  GLY B N   1 
ATOM   1132  C CA  . GLY A 1 159  ? 216.902 199.499 324.278 1.00 97.57  ? 142  GLY B CA  1 
ATOM   1133  C C   . GLY A 1 159  ? 216.453 200.755 323.560 1.00 97.57  ? 142  GLY B C   1 
ATOM   1134  O O   . GLY A 1 159  ? 215.250 201.011 323.448 1.00 97.57  ? 142  GLY B O   1 
ATOM   1135  N N   . SER A 1 160  ? 217.399 201.548 323.073 1.00 94.27  ? 143  SER B N   1 
ATOM   1136  C CA  . SER A 1 160  ? 217.073 202.785 322.383 1.00 94.27  ? 143  SER B CA  1 
ATOM   1137  C C   . SER A 1 160  ? 216.859 202.533 320.894 1.00 94.27  ? 143  SER B C   1 
ATOM   1138  O O   . SER A 1 160  ? 217.306 201.529 320.336 1.00 94.27  ? 143  SER B O   1 
ATOM   1139  C CB  . SER A 1 160  ? 218.178 203.823 322.583 1.00 94.27  ? 143  SER B CB  1 
ATOM   1140  O OG  . SER A 1 160  ? 217.880 204.682 323.669 1.00 94.27  ? 143  SER B OG  1 
ATOM   1141  N N   . TYR A 1 161  ? 216.166 203.466 320.255 1.00 91.38  ? 144  TYR B N   1 
ATOM   1142  C CA  . TYR A 1 161  ? 215.909 203.410 318.825 1.00 91.38  ? 144  TYR B CA  1 
ATOM   1143  C C   . TYR A 1 161  ? 216.871 204.325 318.082 1.00 91.38  ? 144  TYR B C   1 
ATOM   1144  O O   . TYR A 1 161  ? 217.446 205.253 318.656 1.00 91.38  ? 144  TYR B O   1 
ATOM   1145  C CB  . TYR A 1 161  ? 214.466 203.808 318.511 1.00 91.38  ? 144  TYR B CB  1 
ATOM   1146  C CG  . TYR A 1 161  ? 213.928 204.923 319.377 1.00 91.38  ? 144  TYR B CG  1 
ATOM   1147  C CD1 . TYR A 1 161  ? 214.549 206.164 319.416 1.00 91.38  ? 144  TYR B CD1 1 
ATOM   1148  C CD2 . TYR A 1 161  ? 212.802 204.732 320.163 1.00 91.38  ? 144  TYR B CD2 1 
ATOM   1149  C CE1 . TYR A 1 161  ? 214.065 207.180 320.207 1.00 91.38  ? 144  TYR B CE1 1 
ATOM   1150  C CE2 . TYR A 1 161  ? 212.310 205.743 320.958 1.00 91.38  ? 144  TYR B CE2 1 
ATOM   1151  C CZ  . TYR A 1 161  ? 212.945 206.965 320.977 1.00 91.38  ? 144  TYR B CZ  1 
ATOM   1152  O OH  . TYR A 1 161  ? 212.456 207.978 321.769 1.00 91.38  ? 144  TYR B OH  1 
ATOM   1153  N N   . ARG A 1 162  ? 217.046 204.050 316.795 1.00 85.71  ? 145  ARG B N   1 
ATOM   1154  C CA  . ARG A 1 162  ? 217.897 204.854 315.922 1.00 85.71  ? 145  ARG B CA  1 
ATOM   1155  C C   . ARG A 1 162  ? 217.076 205.220 314.691 1.00 85.71  ? 145  ARG B C   1 
ATOM   1156  O O   . ARG A 1 162  ? 216.938 204.409 313.770 1.00 85.71  ? 145  ARG B O   1 
ATOM   1157  C CB  . ARG A 1 162  ? 219.167 204.098 315.549 1.00 85.71  ? 145  ARG B CB  1 
ATOM   1158  C CG  . ARG A 1 162  ? 220.098 204.857 314.622 1.00 85.71  ? 145  ARG B CG  1 
ATOM   1159  C CD  . ARG A 1 162  ? 221.097 203.918 313.970 1.00 85.71  ? 145  ARG B CD  1 
ATOM   1160  N NE  . ARG A 1 162  ? 220.439 202.801 313.305 1.00 85.71  ? 145  ARG B NE  1 
ATOM   1161  C CZ  . ARG A 1 162  ? 221.077 201.782 312.745 1.00 85.71  ? 145  ARG B CZ  1 
ATOM   1162  N NH1 . ARG A 1 162  ? 222.396 201.694 312.772 1.00 85.71  ? 145  ARG B NH1 1 
ATOM   1163  N NH2 . ARG A 1 162  ? 220.374 200.828 312.144 1.00 85.71  ? 145  ARG B NH2 1 
ATOM   1164  N N   . SER A 1 163  ? 216.531 206.435 314.677 1.00 81.29  ? 146  SER B N   1 
ATOM   1165  C CA  . SER A 1 163  ? 215.684 206.864 313.572 1.00 81.29  ? 146  SER B CA  1 
ATOM   1166  C C   . SER A 1 163  ? 216.451 206.805 312.260 1.00 81.29  ? 146  SER B C   1 
ATOM   1167  O O   . SER A 1 163  ? 217.595 207.258 312.173 1.00 81.29  ? 146  SER B O   1 
ATOM   1168  C CB  . SER A 1 163  ? 215.168 208.279 313.817 1.00 81.29  ? 146  SER B CB  1 
ATOM   1169  O OG  . SER A 1 163  ? 214.213 208.300 314.861 1.00 81.29  ? 146  SER B OG  1 
ATOM   1170  N N   . GLU A 1 164  ? 215.819 206.237 311.238 1.00 79.11  ? 147  GLU B N   1 
ATOM   1171  C CA  . GLU A 1 164  ? 216.457 206.060 309.945 1.00 79.11  ? 147  GLU B CA  1 
ATOM   1172  C C   . GLU A 1 164  ? 215.495 206.451 308.835 1.00 79.11  ? 147  GLU B C   1 
ATOM   1173  O O   . GLU A 1 164  ? 214.279 206.299 308.959 1.00 79.11  ? 147  GLU B O   1 
ATOM   1174  C CB  . GLU A 1 164  ? 216.926 204.614 309.746 1.00 79.11  ? 147  GLU B CB  1 
ATOM   1175  C CG  . GLU A 1 164  ? 218.101 204.469 308.796 1.00 79.11  ? 147  GLU B CG  1 
ATOM   1176  C CD  . GLU A 1 164  ? 219.416 204.912 309.410 1.00 79.11  ? 147  GLU B CD  1 
ATOM   1177  O OE1 . GLU A 1 164  ? 219.433 205.268 310.607 1.00 79.11  ? 147  GLU B OE1 1 
ATOM   1178  O OE2 . GLU A 1 164  ? 220.437 204.904 308.691 1.00 79.11  ? 147  GLU B OE2 1 
ATOM   1179  N N   . GLU A 1 165  ? 216.057 206.950 307.742 1.00 76.65  ? 148  GLU B N   1 
ATOM   1180  C CA  . GLU A 1 165  ? 215.292 207.320 306.563 1.00 76.65  ? 148  GLU B CA  1 
ATOM   1181  C C   . GLU A 1 165  ? 215.317 206.167 305.571 1.00 76.65  ? 148  GLU B C   1 
ATOM   1182  O O   . GLU A 1 165  ? 216.348 205.513 305.393 1.00 76.65  ? 148  GLU B O   1 
ATOM   1183  C CB  . GLU A 1 165  ? 215.866 208.588 305.925 1.00 76.65  ? 148  GLU B CB  1 
ATOM   1184  C CG  . GLU A 1 165  ? 215.483 208.804 304.470 1.00 76.65  ? 148  GLU B CG  1 
ATOM   1185  C CD  . GLU A 1 165  ? 214.129 209.465 304.311 1.00 76.65  ? 148  GLU B CD  1 
ATOM   1186  O OE1 . GLU A 1 165  ? 213.955 210.592 304.820 1.00 76.65  ? 148  GLU B OE1 1 
ATOM   1187  O OE2 . GLU A 1 165  ? 213.242 208.866 303.671 1.00 76.65  ? 148  GLU B OE2 1 
ATOM   1188  N N   . LEU A 1 166  ? 214.176 205.911 304.936 1.00 69.60  ? 149  LEU B N   1 
ATOM   1189  C CA  . LEU A 1 166  ? 214.047 204.796 304.010 1.00 69.60  ? 149  LEU B CA  1 
ATOM   1190  C C   . LEU A 1 166  ? 213.197 205.218 302.820 1.00 69.60  ? 149  LEU B C   1 
ATOM   1191  O O   . LEU A 1 166  ? 212.592 206.291 302.811 1.00 69.60  ? 149  LEU B O   1 
ATOM   1192  C CB  . LEU A 1 166  ? 213.457 203.565 304.704 1.00 69.60  ? 149  LEU B CB  1 
ATOM   1193  C CG  . LEU A 1 166  ? 211.942 203.432 304.833 1.00 69.60  ? 149  LEU B CG  1 
ATOM   1194  C CD1 . LEU A 1 166  ? 211.634 202.160 305.580 1.00 69.60  ? 149  LEU B CD1 1 
ATOM   1195  C CD2 . LEU A 1 166  ? 211.324 204.621 305.543 1.00 69.60  ? 149  LEU B CD2 1 
ATOM   1196  N N   . ASN A 1 167  ? 213.164 204.360 301.803 1.00 69.60  ? 150  ASN B N   1 
ATOM   1197  C CA  . ASN A 1 167  ? 212.465 204.639 300.555 1.00 69.60  ? 150  ASN B CA  1 
ATOM   1198  C C   . ASN A 1 167  ? 211.269 203.729 300.324 1.00 69.60  ? 150  ASN B C   1 
ATOM   1199  O O   . ASN A 1 167  ? 210.158 204.215 300.099 1.00 69.60  ? 150  ASN B O   1 
ATOM   1200  C CB  . ASN A 1 167  ? 213.439 204.512 299.378 1.00 69.60  ? 150  ASN B CB  1 
ATOM   1201  C CG  . ASN A 1 167  ? 214.261 205.757 299.171 1.00 69.60  ? 150  ASN B CG  1 
ATOM   1202  O OD1 . ASN A 1 167  ? 214.228 206.364 298.104 1.00 69.60  ? 150  ASN B OD1 1 
ATOM   1203  N ND2 . ASN A 1 167  ? 214.996 206.157 300.197 1.00 69.60  ? 150  ASN B ND2 1 
ATOM   1204  N N   . LEU A 1 168  ? 211.468 202.415 300.375 1.00 69.60  ? 151  LEU B N   1 
ATOM   1205  C CA  . LEU A 1 168  ? 210.429 201.442 300.081 1.00 69.60  ? 151  LEU B CA  1 
ATOM   1206  C C   . LEU A 1 168  ? 210.183 200.547 301.285 1.00 69.60  ? 151  LEU B C   1 
ATOM   1207  O O   . LEU A 1 168  ? 211.097 200.260 302.061 1.00 69.60  ? 151  LEU B O   1 
ATOM   1208  C CB  . LEU A 1 168  ? 210.811 200.577 298.882 1.00 69.60  ? 151  LEU B CB  1 
ATOM   1209  C CG  . LEU A 1 168  ? 210.269 201.002 297.525 1.00 69.60  ? 151  LEU B CG  1 
ATOM   1210  C CD1 . LEU A 1 168  ? 210.629 199.973 296.486 1.00 69.60  ? 151  LEU B CD1 1 
ATOM   1211  C CD2 . LEU A 1 168  ? 208.772 201.163 297.605 1.00 69.60  ? 151  LEU B CD2 1 
ATOM   1212  N N   . VAL A 1 169  ? 208.934 200.121 301.444 1.00 69.60  ? 152  VAL B N   1 
ATOM   1213  C CA  . VAL A 1 169  ? 208.559 199.115 302.430 1.00 69.60  ? 152  VAL B CA  1 
ATOM   1214  C C   . VAL A 1 169  ? 207.619 198.128 301.759 1.00 69.60  ? 152  VAL B C   1 
ATOM   1215  O O   . VAL A 1 169  ? 206.726 198.526 301.004 1.00 69.60  ? 152  VAL B O   1 
ATOM   1216  C CB  . VAL A 1 169  ? 207.883 199.730 303.670 1.00 69.60  ? 152  VAL B CB  1 
ATOM   1217  C CG1 . VAL A 1 169  ? 207.733 198.690 304.754 1.00 69.60  ? 152  VAL B CG1 1 
ATOM   1218  C CG2 . VAL A 1 169  ? 208.667 200.913 304.180 1.00 69.60  ? 152  VAL B CG2 1 
ATOM   1219  N N   . ILE A 1 170  ? 207.815 196.841 302.028 1.00 69.60  ? 153  ILE B N   1 
ATOM   1220  C CA  . ILE A 1 170  ? 206.957 195.787 301.498 1.00 69.60  ? 153  ILE B CA  1 
ATOM   1221  C C   . ILE A 1 170  ? 206.248 195.124 302.670 1.00 69.60  ? 153  ILE B C   1 
ATOM   1222  O O   . ILE A 1 170  ? 206.898 194.620 303.593 1.00 69.60  ? 153  ILE B O   1 
ATOM   1223  C CB  . ILE A 1 170  ? 207.750 194.758 300.682 1.00 69.60  ? 153  ILE B CB  1 
ATOM   1224  C CG1 . ILE A 1 170  ? 208.833 195.451 299.862 1.00 69.60  ? 153  ILE B CG1 1 
ATOM   1225  C CG2 . ILE A 1 170  ? 206.825 194.000 299.760 1.00 69.60  ? 153  ILE B CG2 1 
ATOM   1226  C CD1 . ILE A 1 170  ? 208.294 196.241 298.709 1.00 69.60  ? 153  ILE B CD1 1 
ATOM   1227  N N   . ILE A 1 171  ? 204.920 195.124 302.632 1.00 69.60  ? 154  ILE B N   1 
ATOM   1228  C CA  . ILE A 1 171  ? 204.090 194.567 303.689 1.00 69.60  ? 154  ILE B CA  1 
ATOM   1229  C C   . ILE A 1 171  ? 203.152 193.551 303.056 1.00 69.60  ? 154  ILE B C   1 
ATOM   1230  O O   . ILE A 1 171  ? 202.750 193.701 301.899 1.00 69.60  ? 154  ILE B O   1 
ATOM   1231  C CB  . ILE A 1 171  ? 203.287 195.668 304.418 1.00 69.60  ? 154  ILE B CB  1 
ATOM   1232  C CG1 . ILE A 1 171  ? 204.192 196.825 304.819 1.00 69.60  ? 154  ILE B CG1 1 
ATOM   1233  C CG2 . ILE A 1 171  ? 202.626 195.129 305.658 1.00 69.60  ? 154  ILE B CG2 1 
ATOM   1234  C CD1 . ILE A 1 171  ? 203.477 197.890 305.614 1.00 69.60  ? 154  ILE B CD1 1 
ATOM   1235  N N   . GLY A 1 172  ? 202.813 192.499 303.803 1.00 69.60  ? 155  GLY B N   1 
ATOM   1236  C CA  . GLY A 1 172  ? 201.820 191.567 303.337 1.00 69.60  ? 155  GLY B CA  1 
ATOM   1237  C C   . GLY A 1 172  ? 200.493 192.273 303.160 1.00 69.60  ? 155  GLY B C   1 
ATOM   1238  O O   . GLY A 1 172  ? 200.262 193.353 303.712 1.00 69.60  ? 155  GLY B O   1 
ATOM   1239  N N   . PRO A 1 173  ? 199.592 191.677 302.391 1.00 71.83  ? 156  PRO B N   1 
ATOM   1240  C CA  . PRO A 1 173  ? 198.372 192.385 301.996 1.00 71.83  ? 156  PRO B CA  1 
ATOM   1241  C C   . PRO A 1 173  ? 197.434 192.607 303.172 1.00 71.83  ? 156  PRO B C   1 
ATOM   1242  O O   . PRO A 1 173  ? 197.561 192.011 304.242 1.00 71.83  ? 156  PRO B O   1 
ATOM   1243  C CB  . PRO A 1 173  ? 197.750 191.453 300.958 1.00 71.83  ? 156  PRO B CB  1 
ATOM   1244  C CG  . PRO A 1 173  ? 198.228 190.103 301.352 1.00 71.83  ? 156  PRO B CG  1 
ATOM   1245  C CD  . PRO A 1 173  ? 199.611 190.290 301.898 1.00 71.83  ? 156  PRO B CD  1 
ATOM   1246  N N   . SER A 1 174  ? 196.463 193.486 302.942 1.00 80.65  ? 157  SER B N   1 
ATOM   1247  C CA  . SER A 1 174  ? 195.410 193.777 303.906 1.00 80.65  ? 157  SER B CA  1 
ATOM   1248  C C   . SER A 1 174  ? 194.375 192.662 303.888 1.00 80.65  ? 157  SER B C   1 
ATOM   1249  O O   . SER A 1 174  ? 194.671 191.548 303.444 1.00 80.65  ? 157  SER B O   1 
ATOM   1250  C CB  . SER A 1 174  ? 194.751 195.122 303.602 1.00 80.65  ? 157  SER B CB  1 
ATOM   1251  O OG  . SER A 1 174  ? 195.607 196.197 303.942 1.00 80.65  ? 157  SER B OG  1 
ATOM   1252  N N   . ALA A 1 175  ? 193.177 192.934 304.411 1.00 80.74  ? 158  ALA B N   1 
ATOM   1253  C CA  . ALA A 1 175  ? 192.117 191.932 304.401 1.00 80.74  ? 158  ALA B CA  1 
ATOM   1254  C C   . ALA A 1 175  ? 191.944 191.328 303.014 1.00 80.74  ? 158  ALA B C   1 
ATOM   1255  O O   . ALA A 1 175  ? 191.900 190.103 302.859 1.00 80.74  ? 158  ALA B O   1 
ATOM   1256  C CB  . ALA A 1 175  ? 190.806 192.551 304.885 1.00 80.74  ? 158  ALA B CB  1 
ATOM   1257  N N   . ASP A 1 176  ? 191.871 192.170 301.988 1.00 75.02  ? 159  ASP B N   1 
ATOM   1258  C CA  . ASP A 1 176  ? 191.838 191.676 300.616 1.00 75.02  ? 159  ASP B CA  1 
ATOM   1259  C C   . ASP A 1 176  ? 193.209 191.124 300.262 1.00 75.02  ? 159  ASP B C   1 
ATOM   1260  O O   . ASP A 1 176  ? 194.158 191.887 300.058 1.00 75.02  ? 159  ASP B O   1 
ATOM   1261  C CB  . ASP A 1 176  ? 191.433 192.785 299.653 1.00 75.02  ? 159  ASP B CB  1 
ATOM   1262  C CG  . ASP A 1 176  ? 190.895 192.247 298.347 1.00 75.02  ? 159  ASP B CG  1 
ATOM   1263  O OD1 . ASP A 1 176  ? 191.668 191.607 297.606 1.00 75.02  ? 159  ASP B OD1 1 
ATOM   1264  O OD2 . ASP A 1 176  ? 189.703 192.472 298.053 1.00 75.02  ? 159  ASP B OD2 1 
ATOM   1265  N N   . ILE A 1 177  ? 193.313 189.798 300.181 1.00 70.52  ? 160  ILE B N   1 
ATOM   1266  C CA  . ILE A 1 177  ? 194.613 189.150 300.031 1.00 70.52  ? 160  ILE B CA  1 
ATOM   1267  C C   . ILE A 1 177  ? 195.262 189.528 298.707 1.00 70.52  ? 160  ILE B C   1 
ATOM   1268  O O   . ILE A 1 177  ? 196.469 189.786 298.642 1.00 70.52  ? 160  ILE B O   1 
ATOM   1269  C CB  . ILE A 1 177  ? 194.462 187.625 300.168 1.00 70.52  ? 160  ILE B CB  1 
ATOM   1270  C CG1 . ILE A 1 177  ? 194.223 187.242 301.626 1.00 70.52  ? 160  ILE B CG1 1 
ATOM   1271  C CG2 . ILE A 1 177  ? 195.679 186.921 299.627 1.00 70.52  ? 160  ILE B CG2 1 
ATOM   1272  C CD1 . ILE A 1 177  ? 195.477 187.174 302.449 1.00 70.52  ? 160  ILE B CD1 1 
ATOM   1273  N N   . ILE A 1 178  ? 194.480 189.576 297.634 1.00 71.99  ? 161  ILE B N   1 
ATOM   1274  C CA  . ILE A 1 178  ? 195.057 189.636 296.298 1.00 71.99  ? 161  ILE B CA  1 
ATOM   1275  C C   . ILE A 1 178  ? 194.740 191.017 295.725 1.00 71.99  ? 161  ILE B C   1 
ATOM   1276  O O   . ILE A 1 178  ? 194.516 191.188 294.522 1.00 71.99  ? 161  ILE B O   1 
ATOM   1277  C CB  . ILE A 1 178  ? 194.540 188.458 295.443 1.00 71.99  ? 161  ILE B CB  1 
ATOM   1278  C CG1 . ILE A 1 178  ? 195.074 188.478 294.011 1.00 71.99  ? 161  ILE B CG1 1 
ATOM   1279  C CG2 . ILE A 1 178  ? 193.025 188.454 295.414 1.00 71.99  ? 161  ILE B CG2 1 
ATOM   1280  C CD1 . ILE A 1 178  ? 194.412 187.475 293.115 1.00 71.99  ? 161  ILE B CD1 1 
ATOM   1281  N N   . GLN A 1 179  ? 194.691 192.017 296.599 1.00 73.55  ? 162  GLN B N   1 
ATOM   1282  C CA  . GLN A 1 179  ? 194.616 193.417 296.194 1.00 73.55  ? 162  GLN B CA  1 
ATOM   1283  C C   . GLN A 1 179  ? 195.943 194.078 296.543 1.00 73.55  ? 162  GLN B C   1 
ATOM   1284  O O   . GLN A 1 179  ? 196.256 194.271 297.722 1.00 73.55  ? 162  GLN B O   1 
ATOM   1285  C CB  . GLN A 1 179  ? 193.456 194.133 296.877 1.00 73.55  ? 162  GLN B CB  1 
ATOM   1286  C CG  . GLN A 1 179  ? 193.501 195.642 296.749 1.00 73.55  ? 162  GLN B CG  1 
ATOM   1287  C CD  . GLN A 1 179  ? 192.896 196.333 297.948 1.00 73.55  ? 162  GLN B CD  1 
ATOM   1288  O OE1 . GLN A 1 179  ? 191.676 196.384 298.100 1.00 73.55  ? 162  GLN B OE1 1 
ATOM   1289  N NE2 . GLN A 1 179  ? 193.747 196.861 298.816 1.00 73.55  ? 162  GLN B NE2 1 
ATOM   1290  N N   . PHE A 1 180  ? 196.714 194.429 295.519 1.00 69.60  ? 163  PHE B N   1 
ATOM   1291  C CA  . PHE A 1 180  ? 198.039 195.007 295.683 1.00 69.60  ? 163  PHE B CA  1 
ATOM   1292  C C   . PHE A 1 180  ? 197.978 196.495 295.375 1.00 69.60  ? 163  PHE B C   1 
ATOM   1293  O O   . PHE A 1 180  ? 197.454 196.892 294.330 1.00 69.60  ? 163  PHE B O   1 
ATOM   1294  C CB  . PHE A 1 180  ? 199.047 194.315 294.766 1.00 69.60  ? 163  PHE B CB  1 
ATOM   1295  C CG  . PHE A 1 180  ? 199.062 192.820 294.903 1.00 69.60  ? 163  PHE B CG  1 
ATOM   1296  C CD1 . PHE A 1 180  ? 199.196 192.227 296.143 1.00 69.60  ? 163  PHE B CD1 1 
ATOM   1297  C CD2 . PHE A 1 180  ? 198.933 192.010 293.791 1.00 69.60  ? 163  PHE B CD2 1 
ATOM   1298  C CE1 . PHE A 1 180  ? 199.209 190.854 296.270 1.00 69.60  ? 163  PHE B CE1 1 
ATOM   1299  C CE2 . PHE A 1 180  ? 198.943 190.638 293.914 1.00 69.60  ? 163  PHE B CE2 1 
ATOM   1300  C CZ  . PHE A 1 180  ? 199.081 190.061 295.154 1.00 69.60  ? 163  PHE B CZ  1 
ATOM   1301  N N   . GLU A 1 181  ? 198.511 197.312 296.279 1.00 69.60  ? 164  GLU B N   1 
ATOM   1302  C CA  . GLU A 1 181  ? 198.475 198.755 296.098 1.00 69.60  ? 164  GLU B CA  1 
ATOM   1303  C C   . GLU A 1 181  ? 199.651 199.387 296.824 1.00 69.60  ? 164  GLU B C   1 
ATOM   1304  O O   . GLU A 1 181  ? 200.227 198.804 297.745 1.00 69.60  ? 164  GLU B O   1 
ATOM   1305  C CB  . GLU A 1 181  ? 197.154 199.350 296.595 1.00 69.60  ? 164  GLU B CB  1 
ATOM   1306  C CG  . GLU A 1 181  ? 196.922 199.197 298.086 1.00 69.60  ? 164  GLU B CG  1 
ATOM   1307  C CD  . GLU A 1 181  ? 195.623 199.835 298.540 1.00 69.60  ? 164  GLU B CD  1 
ATOM   1308  O OE1 . GLU A 1 181  ? 194.717 200.006 297.698 1.00 69.60  ? 164  GLU B OE1 1 
ATOM   1309  O OE2 . GLU A 1 181  ? 195.506 200.161 299.739 1.00 69.60  ? 164  GLU B OE2 1 
ATOM   1310  N N   . CYS A 1 182  ? 199.992 200.601 296.405 1.00 69.60  ? 165  CYS B N   1 
ATOM   1311  C CA  . CYS A 1 182  ? 201.123 201.340 296.951 1.00 69.60  ? 165  CYS B CA  1 
ATOM   1312  C C   . CYS A 1 182  ? 200.603 202.558 297.701 1.00 69.60  ? 165  CYS B C   1 
ATOM   1313  O O   . CYS A 1 182  ? 200.106 203.504 297.083 1.00 69.60  ? 165  CYS B O   1 
ATOM   1314  C CB  . CYS A 1 182  ? 202.084 201.755 295.839 1.00 69.60  ? 165  CYS B CB  1 
ATOM   1315  S SG  . CYS A 1 182  ? 203.116 203.170 296.234 1.00 69.60  ? 165  CYS B SG  1 
ATOM   1316  N N   . LYS A 1 183  ? 200.719 202.533 299.023 1.00 69.60  ? 166  LYS B N   1 
ATOM   1317  C CA  . LYS A 1 183  ? 200.243 203.606 299.880 1.00 69.60  ? 166  LYS B CA  1 
ATOM   1318  C C   . LYS A 1 183  ? 201.390 204.531 300.264 1.00 69.60  ? 166  LYS B C   1 
ATOM   1319  O O   . LYS A 1 183  ? 202.566 204.189 300.137 1.00 69.60  ? 166  LYS B O   1 
ATOM   1320  C CB  . LYS A 1 183  ? 199.587 203.037 301.138 1.00 69.60  ? 166  LYS B CB  1 
ATOM   1321  C CG  . LYS A 1 183  ? 198.263 202.344 300.881 1.00 69.60  ? 166  LYS B CG  1 
ATOM   1322  C CD  . LYS A 1 183  ? 197.252 203.312 300.298 1.00 69.60  ? 166  LYS B CD  1 
ATOM   1323  C CE  . LYS A 1 183  ? 195.907 203.194 300.987 1.00 69.60  ? 166  LYS B CE  1 
ATOM   1324  N NZ  . LYS A 1 183  ? 194.813 203.748 300.144 1.00 69.60  ? 166  LYS B NZ  1 
ATOM   1325  N N   . SER A 1 184  ? 201.030 205.716 300.746 1.00 76.16  ? 167  SER B N   1 
ATOM   1326  C CA  . SER A 1 184  ? 202.014 206.713 301.136 1.00 76.16  ? 167  SER B CA  1 
ATOM   1327  C C   . SER A 1 184  ? 201.474 207.507 302.312 1.00 76.16  ? 167  SER B C   1 
ATOM   1328  O O   . SER A 1 184  ? 200.265 207.568 302.541 1.00 76.16  ? 167  SER B O   1 
ATOM   1329  C CB  . SER A 1 184  ? 202.355 207.650 299.974 1.00 76.16  ? 167  SER B CB  1 
ATOM   1330  O OG  . SER A 1 184  ? 202.946 208.848 300.447 1.00 76.16  ? 167  SER B OG  1 
ATOM   1331  N N   . PHE A 1 185  ? 202.386 208.125 303.056 1.00 80.24  ? 168  PHE B N   1 
ATOM   1332  C CA  . PHE A 1 185  ? 202.030 208.930 304.215 1.00 80.24  ? 168  PHE B CA  1 
ATOM   1333  C C   . PHE A 1 185  ? 202.061 210.400 303.826 1.00 80.24  ? 168  PHE B C   1 
ATOM   1334  O O   . PHE A 1 185  ? 203.107 210.919 303.428 1.00 80.24  ? 168  PHE B O   1 
ATOM   1335  C CB  . PHE A 1 185  ? 202.976 208.655 305.380 1.00 80.24  ? 168  PHE B CB  1 
ATOM   1336  C CG  . PHE A 1 185  ? 202.476 207.603 306.317 1.00 80.24  ? 168  PHE B CG  1 
ATOM   1337  C CD1 . PHE A 1 185  ? 202.669 206.265 306.039 1.00 80.24  ? 168  PHE B CD1 1 
ATOM   1338  C CD2 . PHE A 1 185  ? 201.810 207.951 307.475 1.00 80.24  ? 168  PHE B CD2 1 
ATOM   1339  C CE1 . PHE A 1 185  ? 202.208 205.294 306.897 1.00 80.24  ? 168  PHE B CE1 1 
ATOM   1340  C CE2 . PHE A 1 185  ? 201.349 206.985 308.337 1.00 80.24  ? 168  PHE B CE2 1 
ATOM   1341  C CZ  . PHE A 1 185  ? 201.549 205.655 308.047 1.00 80.24  ? 168  PHE B CZ  1 
ATOM   1342  N N   . GLY A 1 186  ? 200.917 211.066 303.946 1.00 88.87  ? 169  GLY B N   1 
ATOM   1343  C CA  . GLY A 1 186  ? 200.781 212.426 303.481 1.00 88.87  ? 169  GLY B CA  1 
ATOM   1344  C C   . GLY A 1 186  ? 201.253 213.455 304.487 1.00 88.87  ? 169  GLY B C   1 
ATOM   1345  O O   . GLY A 1 186  ? 201.716 213.146 305.585 1.00 88.87  ? 169  GLY B O   1 
ATOM   1346  N N   . HIS A 1 187  ? 201.123 214.715 304.088 1.00 93.86  ? 170  HIS B N   1 
ATOM   1347  C CA  . HIS A 1 187  ? 201.500 215.859 304.899 1.00 93.86  ? 170  HIS B CA  1 
ATOM   1348  C C   . HIS A 1 187  ? 200.282 216.743 305.121 1.00 93.86  ? 170  HIS B C   1 
ATOM   1349  O O   . HIS A 1 187  ? 199.220 216.542 304.524 1.00 93.86  ? 170  HIS B O   1 
ATOM   1350  C CB  . HIS A 1 187  ? 202.633 216.649 304.235 1.00 93.86  ? 170  HIS B CB  1 
ATOM   1351  C CG  . HIS A 1 187  ? 203.366 217.562 305.168 1.00 93.86  ? 170  HIS B CG  1 
ATOM   1352  N ND1 . HIS A 1 187  ? 203.117 218.915 305.231 1.00 93.86  ? 170  HIS B ND1 1 
ATOM   1353  C CD2 . HIS A 1 187  ? 204.340 217.315 306.075 1.00 93.86  ? 170  HIS B CD2 1 
ATOM   1354  C CE1 . HIS A 1 187  ? 203.907 219.464 306.136 1.00 93.86  ? 170  HIS B CE1 1 
ATOM   1355  N NE2 . HIS A 1 187  ? 204.659 218.515 306.663 1.00 93.86  ? 170  HIS B NE2 1 
ATOM   1356  N N   . GLU A 1 188  ? 200.442 217.733 306.001 1.00 98.03  ? 171  GLU B N   1 
ATOM   1357  C CA  . GLU A 1 188  ? 199.318 218.593 306.357 1.00 98.03  ? 171  GLU B CA  1 
ATOM   1358  C C   . GLU A 1 188  ? 198.967 219.560 305.232 1.00 98.03  ? 171  GLU B C   1 
ATOM   1359  O O   . GLU A 1 188  ? 197.785 219.824 304.982 1.00 98.03  ? 171  GLU B O   1 
ATOM   1360  C CB  . GLU A 1 188  ? 199.633 219.359 307.642 1.00 98.03  ? 171  GLU B CB  1 
ATOM   1361  C CG  . GLU A 1 188  ? 200.298 218.519 308.725 1.00 98.03  ? 171  GLU B CG  1 
ATOM   1362  C CD  . GLU A 1 188  ? 199.409 217.398 309.237 1.00 98.03  ? 171  GLU B CD  1 
ATOM   1363  O OE1 . GLU A 1 188  ? 198.169 217.535 309.172 1.00 98.03  ? 171  GLU B OE1 1 
ATOM   1364  O OE2 . GLU A 1 188  ? 199.952 216.378 309.707 1.00 98.03  ? 171  GLU B OE2 1 
ATOM   1365  N N   . VAL A 1 189  ? 199.971 220.102 304.544 1.00 94.92  ? 172  VAL B N   1 
ATOM   1366  C CA  . VAL A 1 189  ? 199.730 221.146 303.555 1.00 94.92  ? 172  VAL B CA  1 
ATOM   1367  C C   . VAL A 1 189  ? 200.314 220.749 302.203 1.00 94.92  ? 172  VAL B C   1 
ATOM   1368  O O   . VAL A 1 189  ? 199.809 221.157 301.151 1.00 94.92  ? 172  VAL B O   1 
ATOM   1369  C CB  . VAL A 1 189  ? 200.309 222.488 304.047 1.00 94.92  ? 172  VAL B CB  1 
ATOM   1370  C CG1 . VAL A 1 189  ? 201.716 222.291 304.588 1.00 94.92  ? 172  VAL B CG1 1 
ATOM   1371  C CG2 . VAL A 1 189  ? 200.286 223.544 302.950 1.00 94.92  ? 172  VAL B CG2 1 
ATOM   1372  N N   . LEU A 1 190  ? 201.351 219.917 302.215 1.00 87.04  ? 173  LEU B N   1 
ATOM   1373  C CA  . LEU A 1 190  ? 202.094 219.576 301.008 1.00 87.04  ? 173  LEU B CA  1 
ATOM   1374  C C   . LEU A 1 190  ? 201.610 218.246 300.443 1.00 87.04  ? 173  LEU B C   1 
ATOM   1375  O O   . LEU A 1 190  ? 201.420 217.281 301.190 1.00 87.04  ? 173  LEU B O   1 
ATOM   1376  C CB  . LEU A 1 190  ? 203.593 219.503 301.299 1.00 87.04  ? 173  LEU B CB  1 
ATOM   1377  C CG  . LEU A 1 190  ? 204.250 220.765 301.856 1.00 87.04  ? 173  LEU B CG  1 
ATOM   1378  C CD1 . LEU A 1 190  ? 205.528 220.412 302.594 1.00 87.04  ? 173  LEU B CD1 1 
ATOM   1379  C CD2 . LEU A 1 190  ? 204.529 221.762 300.745 1.00 87.04  ? 173  LEU B CD2 1 
ATOM   1380  N N   . ASN A 1 191  ? 201.412 218.201 299.126 1.00 78.54  ? 174  ASN B N   1 
ATOM   1381  C CA  . ASN A 1 191  ? 201.121 216.954 298.422 1.00 78.54  ? 174  ASN B CA  1 
ATOM   1382  C C   . ASN A 1 191  ? 202.456 216.367 297.987 1.00 78.54  ? 174  ASN B C   1 
ATOM   1383  O O   . ASN A 1 191  ? 202.947 216.630 296.890 1.00 78.54  ? 174  ASN B O   1 
ATOM   1384  C CB  . ASN A 1 191  ? 200.200 217.195 297.234 1.00 78.54  ? 174  ASN B CB  1 
ATOM   1385  C CG  . ASN A 1 191  ? 199.171 218.268 297.504 1.00 78.54  ? 174  ASN B CG  1 
ATOM   1386  O OD1 . ASN A 1 191  ? 198.320 218.122 298.381 1.00 78.54  ? 174  ASN B OD1 1 
ATOM   1387  N ND2 . ASN A 1 191  ? 199.240 219.356 296.749 1.00 78.54  ? 174  ASN B ND2 1 
ATOM   1388  N N   . LEU A 1 192  ? 203.052 215.559 298.865 1.00 71.87  ? 175  LEU B N   1 
ATOM   1389  C CA  . LEU A 1 192  ? 204.409 215.081 298.628 1.00 71.87  ? 175  LEU B CA  1 
ATOM   1390  C C   . LEU A 1 192  ? 204.504 214.205 297.387 1.00 71.87  ? 175  LEU B C   1 
ATOM   1391  O O   . LEU A 1 192  ? 205.566 214.137 296.761 1.00 71.87  ? 175  LEU B O   1 
ATOM   1392  C CB  . LEU A 1 192  ? 204.916 214.318 299.850 1.00 71.87  ? 175  LEU B CB  1 
ATOM   1393  C CG  . LEU A 1 192  ? 204.966 215.079 301.173 1.00 71.87  ? 175  LEU B CG  1 
ATOM   1394  C CD1 . LEU A 1 192  ? 205.258 214.127 302.317 1.00 71.87  ? 175  LEU B CD1 1 
ATOM   1395  C CD2 . LEU A 1 192  ? 206.012 216.174 301.113 1.00 71.87  ? 175  LEU B CD2 1 
ATOM   1396  N N   . THR A 1 193  ? 203.423 213.532 297.011 1.00 70.93  ? 176  THR B N   1 
ATOM   1397  C CA  . THR A 1 193  ? 203.481 212.564 295.925 1.00 70.93  ? 176  THR B CA  1 
ATOM   1398  C C   . THR A 1 193  ? 203.193 213.168 294.559 1.00 70.93  ? 176  THR B C   1 
ATOM   1399  O O   . THR A 1 193  ? 203.213 212.438 293.565 1.00 70.93  ? 176  THR B O   1 
ATOM   1400  C CB  . THR A 1 193  ? 202.503 211.416 296.180 1.00 70.93  ? 176  THR B CB  1 
ATOM   1401  O OG1 . THR A 1 193  ? 201.216 211.759 295.658 1.00 70.93  ? 176  THR B OG1 1 
ATOM   1402  C CG2 . THR A 1 193  ? 202.385 211.140 297.668 1.00 70.93  ? 176  THR B CG2 1 
ATOM   1403  N N   . ARG A 1 194  ? 202.917 214.471 294.475 1.00 74.64  ? 177  ARG B N   1 
ATOM   1404  C CA  . ARG A 1 194  ? 202.636 215.077 293.180 1.00 74.64  ? 177  ARG B CA  1 
ATOM   1405  C C   . ARG A 1 194  ? 203.248 216.463 293.012 1.00 74.64  ? 177  ARG B C   1 
ATOM   1406  O O   . ARG A 1 194  ? 202.931 217.143 292.030 1.00 74.64  ? 177  ARG B O   1 
ATOM   1407  C CB  . ARG A 1 194  ? 201.127 215.151 292.936 1.00 74.64  ? 177  ARG B CB  1 
ATOM   1408  C CG  . ARG A 1 194  ? 200.423 216.239 293.714 1.00 74.64  ? 177  ARG B CG  1 
ATOM   1409  C CD  . ARG A 1 194  ? 198.923 216.135 293.543 1.00 74.64  ? 177  ARG B CD  1 
ATOM   1410  N NE  . ARG A 1 194  ? 198.401 214.864 294.026 1.00 74.64  ? 177  ARG B NE  1 
ATOM   1411  C CZ  . ARG A 1 194  ? 197.593 214.737 295.069 1.00 74.64  ? 177  ARG B CZ  1 
ATOM   1412  N NH1 . ARG A 1 194  ? 197.178 215.790 295.754 1.00 74.64  ? 177  ARG B NH1 1 
ATOM   1413  N NH2 . ARG A 1 194  ? 197.188 213.523 295.432 1.00 74.64  ? 177  ARG B NH2 1 
ATOM   1414  N N   . ASN A 1 195  ? 204.111 216.905 293.924 1.00 70.56  ? 178  ASN B N   1 
ATOM   1415  C CA  . ASN A 1 195  ? 204.770 218.198 293.797 1.00 70.56  ? 178  ASN B CA  1 
ATOM   1416  C C   . ASN A 1 195  ? 206.281 218.074 293.657 1.00 70.56  ? 178  ASN B C   1 
ATOM   1417  O O   . ASN A 1 195  ? 206.986 219.083 293.746 1.00 70.56  ? 178  ASN B O   1 
ATOM   1418  C CB  . ASN A 1 195  ? 204.421 219.092 294.988 1.00 70.56  ? 178  ASN B CB  1 
ATOM   1419  C CG  . ASN A 1 195  ? 205.232 218.767 296.219 1.00 70.56  ? 178  ASN B CG  1 
ATOM   1420  O OD1 . ASN A 1 195  ? 205.546 217.609 296.483 1.00 70.56  ? 178  ASN B OD1 1 
ATOM   1421  N ND2 . ASN A 1 195  ? 205.576 219.793 296.984 1.00 70.56  ? 178  ASN B ND2 1 
ATOM   1422  N N   . GLY A 1 196  ? 206.794 216.865 293.442 1.00 69.60  ? 179  GLY B N   1 
ATOM   1423  C CA  . GLY A 1 196  ? 208.206 216.649 293.235 1.00 69.60  ? 179  GLY B CA  1 
ATOM   1424  C C   . GLY A 1 196  ? 209.003 216.364 294.489 1.00 69.60  ? 179  GLY B C   1 
ATOM   1425  O O   . GLY A 1 196  ? 210.131 215.873 294.387 1.00 69.60  ? 179  GLY B O   1 
ATOM   1426  N N   . TYR A 1 197  ? 208.456 216.661 295.668 1.00 70.39  ? 180  TYR B N   1 
ATOM   1427  C CA  . TYR A 1 197  ? 209.176 216.382 296.906 1.00 70.39  ? 180  TYR B CA  1 
ATOM   1428  C C   . TYR A 1 197  ? 209.364 214.885 297.111 1.00 70.39  ? 180  TYR B C   1 
ATOM   1429  O O   . TYR A 1 197  ? 210.449 214.439 297.498 1.00 70.39  ? 180  TYR B O   1 
ATOM   1430  C CB  . TYR A 1 197  ? 208.437 216.993 298.096 1.00 70.39  ? 180  TYR B CB  1 
ATOM   1431  C CG  . TYR A 1 197  ? 208.642 218.479 298.275 1.00 70.39  ? 180  TYR B CG  1 
ATOM   1432  C CD1 . TYR A 1 197  ? 208.924 219.298 297.195 1.00 70.39  ? 180  TYR B CD1 1 
ATOM   1433  C CD2 . TYR A 1 197  ? 208.550 219.062 299.528 1.00 70.39  ? 180  TYR B CD2 1 
ATOM   1434  C CE1 . TYR A 1 197  ? 209.109 220.653 297.358 1.00 70.39  ? 180  TYR B CE1 1 
ATOM   1435  C CE2 . TYR A 1 197  ? 208.735 220.416 299.701 1.00 70.39  ? 180  TYR B CE2 1 
ATOM   1436  C CZ  . TYR A 1 197  ? 209.015 221.207 298.613 1.00 70.39  ? 180  TYR B CZ  1 
ATOM   1437  O OH  . TYR A 1 197  ? 209.200 222.559 298.776 1.00 70.39  ? 180  TYR B OH  1 
ATOM   1438  N N   . GLY A 1 198  ? 208.326 214.099 296.862 1.00 69.60  ? 181  GLY B N   1 
ATOM   1439  C CA  . GLY A 1 198  ? 208.391 212.666 297.038 1.00 69.60  ? 181  GLY B CA  1 
ATOM   1440  C C   . GLY A 1 198  ? 208.190 212.247 298.484 1.00 69.60  ? 181  GLY B C   1 
ATOM   1441  O O   . GLY A 1 198  ? 208.339 213.028 299.421 1.00 69.60  ? 181  GLY B O   1 
ATOM   1442  N N   . SER A 1 199  ? 207.849 210.973 298.659 1.00 69.60  ? 182  SER B N   1 
ATOM   1443  C CA  . SER A 1 199  ? 207.630 210.424 299.989 1.00 69.60  ? 182  SER B CA  1 
ATOM   1444  C C   . SER A 1 199  ? 207.823 208.919 299.931 1.00 69.60  ? 182  SER B C   1 
ATOM   1445  O O   . SER A 1 199  ? 207.801 208.317 298.856 1.00 69.60  ? 182  SER B O   1 
ATOM   1446  C CB  . SER A 1 199  ? 206.235 210.759 300.515 1.00 69.60  ? 182  SER B CB  1 
ATOM   1447  O OG  . SER A 1 199  ? 205.238 210.198 299.681 1.00 69.60  ? 182  SER B OG  1 
ATOM   1448  N N   . THR A 1 200  ? 208.001 208.318 301.105 1.00 69.60  ? 183  THR B N   1 
ATOM   1449  C CA  . THR A 1 200  ? 208.174 206.875 301.191 1.00 69.60  ? 183  THR B CA  1 
ATOM   1450  C C   . THR A 1 200  ? 206.920 206.159 300.710 1.00 69.60  ? 183  THR B C   1 
ATOM   1451  O O   . THR A 1 200  ? 205.800 206.650 300.864 1.00 69.60  ? 183  THR B O   1 
ATOM   1452  C CB  . THR A 1 200  ? 208.485 206.457 302.623 1.00 69.60  ? 183  THR B CB  1 
ATOM   1453  O OG1 . THR A 1 200  ? 207.324 206.659 303.435 1.00 69.60  ? 183  THR B OG1 1 
ATOM   1454  C CG2 . THR A 1 200  ? 209.615 207.284 303.175 1.00 69.60  ? 183  THR B CG2 1 
ATOM   1455  N N   . GLN A 1 201  ? 207.115 204.987 300.113 1.00 69.60  ? 184  GLN B N   1 
ATOM   1456  C CA  . GLN A 1 201  ? 206.026 204.200 299.556 1.00 69.60  ? 184  GLN B CA  1 
ATOM   1457  C C   . GLN A 1 201  ? 205.980 202.836 300.227 1.00 69.60  ? 184  GLN B C   1 
ATOM   1458  O O   . GLN A 1 201  ? 206.979 202.112 300.236 1.00 69.60  ? 184  GLN B O   1 
ATOM   1459  C CB  . GLN A 1 201  ? 206.190 204.039 298.046 1.00 69.60  ? 184  GLN B CB  1 
ATOM   1460  C CG  . GLN A 1 201  ? 206.291 205.350 297.308 1.00 69.60  ? 184  GLN B CG  1 
ATOM   1461  C CD  . GLN A 1 201  ? 205.185 206.306 297.682 1.00 69.60  ? 184  GLN B CD  1 
ATOM   1462  O OE1 . GLN A 1 201  ? 204.007 206.009 297.505 1.00 69.60  ? 184  GLN B OE1 1 
ATOM   1463  N NE2 . GLN A 1 201  ? 205.558 207.464 298.208 1.00 69.60  ? 184  GLN B NE2 1 
ATOM   1464  N N   . TYR A 1 202  ? 204.821 202.488 300.777 1.00 69.60  ? 185  TYR B N   1 
ATOM   1465  C CA  . TYR A 1 202  ? 204.594 201.186 301.386 1.00 69.60  ? 185  TYR B CA  1 
ATOM   1466  C C   . TYR A 1 202  ? 203.770 200.347 300.420 1.00 69.60  ? 185  TYR B C   1 
ATOM   1467  O O   . TYR A 1 202  ? 202.617 200.679 300.137 1.00 69.60  ? 185  TYR B O   1 
ATOM   1468  C CB  . TYR A 1 202  ? 203.866 201.322 302.723 1.00 69.60  ? 185  TYR B CB  1 
ATOM   1469  C CG  . TYR A 1 202  ? 204.572 202.173 303.752 1.00 69.60  ? 185  TYR B CG  1 
ATOM   1470  C CD1 . TYR A 1 202  ? 204.652 203.546 303.610 1.00 69.60  ? 185  TYR B CD1 1 
ATOM   1471  C CD2 . TYR A 1 202  ? 205.141 201.602 304.876 1.00 69.60  ? 185  TYR B CD2 1 
ATOM   1472  C CE1 . TYR A 1 202  ? 205.289 204.321 304.547 1.00 69.60  ? 185  TYR B CE1 1 
ATOM   1473  C CE2 . TYR A 1 202  ? 205.781 202.371 305.819 1.00 69.60  ? 185  TYR B CE2 1 
ATOM   1474  C CZ  . TYR A 1 202  ? 205.852 203.730 305.650 1.00 69.60  ? 185  TYR B CZ  1 
ATOM   1475  O OH  . TYR A 1 202  ? 206.489 204.508 306.587 1.00 69.60  ? 185  TYR B OH  1 
ATOM   1476  N N   . ILE A 1 203  ? 204.350 199.267 299.918 1.00 69.60  ? 186  ILE B N   1 
ATOM   1477  C CA  . ILE A 1 203  ? 203.692 198.412 298.940 1.00 69.60  ? 186  ILE B CA  1 
ATOM   1478  C C   . ILE A 1 203  ? 203.054 197.241 299.669 1.00 69.60  ? 186  ILE B C   1 
ATOM   1479  O O   . ILE A 1 203  ? 203.690 196.614 300.523 1.00 69.60  ? 186  ILE B O   1 
ATOM   1480  C CB  . ILE A 1 203  ? 204.685 197.919 297.876 1.00 69.60  ? 186  ILE B CB  1 
ATOM   1481  C CG1 . ILE A 1 203  ? 205.327 199.099 297.158 1.00 69.60  ? 186  ILE B CG1 1 
ATOM   1482  C CG2 . ILE A 1 203  ? 203.991 197.027 296.877 1.00 69.60  ? 186  ILE B CG2 1 
ATOM   1483  C CD1 . ILE A 1 203  ? 206.421 198.694 296.212 1.00 69.60  ? 186  ILE B CD1 1 
ATOM   1484  N N   . ARG A 1 204  ? 201.797 196.947 299.345 1.00 69.60  ? 187  ARG B N   1 
ATOM   1485  C CA  . ARG A 1 204  ? 201.106 195.777 299.877 1.00 69.60  ? 187  ARG B CA  1 
ATOM   1486  C C   . ARG A 1 204  ? 201.177 194.685 298.818 1.00 69.60  ? 187  ARG B C   1 
ATOM   1487  O O   . ARG A 1 204  ? 200.365 194.651 297.892 1.00 69.60  ? 187  ARG B O   1 
ATOM   1488  C CB  . ARG A 1 204  ? 199.662 196.109 300.233 1.00 69.60  ? 187  ARG B CB  1 
ATOM   1489  C CG  . ARG A 1 204  ? 199.493 197.165 301.306 1.00 69.60  ? 187  ARG B CG  1 
ATOM   1490  C CD  . ARG A 1 204  ? 198.054 197.640 301.336 1.00 69.60  ? 187  ARG B CD  1 
ATOM   1491  N NE  . ARG A 1 204  ? 197.710 198.322 302.575 1.00 69.60  ? 187  ARG B NE  1 
ATOM   1492  C CZ  . ARG A 1 204  ? 196.553 198.930 302.794 1.00 69.60  ? 187  ARG B CZ  1 
ATOM   1493  N NH1 . ARG A 1 204  ? 195.610 198.973 301.869 1.00 69.60  ? 187  ARG B NH1 1 
ATOM   1494  N NH2 . ARG A 1 204  ? 196.336 199.505 303.973 1.00 69.60  ? 187  ARG B NH2 1 
ATOM   1495  N N   . PHE A 1 205  ? 202.147 193.787 298.954 1.00 69.60  ? 188  PHE B N   1 
ATOM   1496  C CA  . PHE A 1 205  ? 202.385 192.755 297.959 1.00 69.60  ? 188  PHE B CA  1 
ATOM   1497  C C   . PHE A 1 205  ? 202.494 191.394 298.628 1.00 69.60  ? 188  PHE B C   1 
ATOM   1498  O O   . PHE A 1 205  ? 202.999 191.272 299.746 1.00 69.60  ? 188  PHE B O   1 
ATOM   1499  C CB  . PHE A 1 205  ? 203.656 193.041 297.156 1.00 69.60  ? 188  PHE B CB  1 
ATOM   1500  C CG  . PHE A 1 205  ? 204.090 191.900 296.291 1.00 69.60  ? 188  PHE B CG  1 
ATOM   1501  C CD1 . PHE A 1 205  ? 203.323 191.505 295.212 1.00 69.60  ? 188  PHE B CD1 1 
ATOM   1502  C CD2 . PHE A 1 205  ? 205.256 191.214 296.562 1.00 69.60  ? 188  PHE B CD2 1 
ATOM   1503  C CE1 . PHE A 1 205  ? 203.715 190.453 294.417 1.00 69.60  ? 188  PHE B CE1 1 
ATOM   1504  C CE2 . PHE A 1 205  ? 205.651 190.161 295.769 1.00 69.60  ? 188  PHE B CE2 1 
ATOM   1505  C CZ  . PHE A 1 205  ? 204.878 189.781 294.696 1.00 69.60  ? 188  PHE B CZ  1 
ATOM   1506  N N   . SER A 1 206  ? 202.007 190.365 297.927 1.00 69.60  ? 189  SER B N   1 
ATOM   1507  C CA  . SER A 1 206  ? 202.083 188.986 298.385 1.00 69.60  ? 189  SER B CA  1 
ATOM   1508  C C   . SER A 1 206  ? 202.473 188.113 297.196 1.00 69.60  ? 189  SER B C   1 
ATOM   1509  O O   . SER A 1 206  ? 201.819 188.184 296.141 1.00 69.60  ? 189  SER B O   1 
ATOM   1510  C CB  . SER A 1 206  ? 200.756 188.518 298.980 1.00 69.60  ? 189  SER B CB  1 
ATOM   1511  O OG  . SER A 1 206  ? 200.830 187.163 299.382 1.00 69.60  ? 189  SER B OG  1 
ATOM   1512  N N   . PRO A 1 207  ? 203.518 187.290 297.321 1.00 69.60  ? 190  PRO B N   1 
ATOM   1513  C CA  . PRO A 1 207  ? 203.959 186.481 296.180 1.00 69.60  ? 190  PRO B CA  1 
ATOM   1514  C C   . PRO A 1 207  ? 203.259 185.137 296.080 1.00 69.60  ? 190  PRO B C   1 
ATOM   1515  O O   . PRO A 1 207  ? 203.276 184.508 295.018 1.00 69.60  ? 190  PRO B O   1 
ATOM   1516  C CB  . PRO A 1 207  ? 205.454 186.305 296.450 1.00 69.60  ? 190  PRO B CB  1 
ATOM   1517  C CG  . PRO A 1 207  ? 205.543 186.283 297.929 1.00 69.60  ? 190  PRO B CG  1 
ATOM   1518  C CD  . PRO A 1 207  ? 204.443 187.175 298.458 1.00 69.60  ? 190  PRO B CD  1 
ATOM   1519  N N   . ASP A 1 208  ? 202.644 184.681 297.172 1.00 72.33  ? 191  ASP B N   1 
ATOM   1520  C CA  . ASP A 1 208  ? 201.998 183.373 297.176 1.00 72.33  ? 191  ASP B CA  1 
ATOM   1521  C C   . ASP A 1 208  ? 200.731 183.328 296.335 1.00 72.33  ? 191  ASP B C   1 
ATOM   1522  O O   . ASP A 1 208  ? 200.234 182.230 296.063 1.00 72.33  ? 191  ASP B O   1 
ATOM   1523  C CB  . ASP A 1 208  ? 201.667 182.943 298.606 1.00 72.33  ? 191  ASP B CB  1 
ATOM   1524  C CG  . ASP A 1 208  ? 202.777 183.260 299.585 1.00 72.33  ? 191  ASP B CG  1 
ATOM   1525  O OD1 . ASP A 1 208  ? 203.952 182.995 299.258 1.00 72.33  ? 191  ASP B OD1 1 
ATOM   1526  O OD2 . ASP A 1 208  ? 202.475 183.765 300.686 1.00 72.33  ? 191  ASP B OD2 1 
ATOM   1527  N N   . PHE A 1 209  ? 200.204 184.473 295.913 1.00 69.60  ? 192  PHE B N   1 
ATOM   1528  C CA  . PHE A 1 209  ? 198.943 184.535 295.191 1.00 69.60  ? 192  PHE B CA  1 
ATOM   1529  C C   . PHE A 1 209  ? 199.143 185.256 293.868 1.00 69.60  ? 192  PHE B C   1 
ATOM   1530  O O   . PHE A 1 209  ? 199.999 186.135 293.746 1.00 69.60  ? 192  PHE B O   1 
ATOM   1531  C CB  . PHE A 1 209  ? 197.873 185.246 296.020 1.00 69.60  ? 192  PHE B CB  1 
ATOM   1532  C CG  . PHE A 1 209  ? 197.407 184.454 297.203 1.00 69.60  ? 192  PHE B CG  1 
ATOM   1533  C CD1 . PHE A 1 209  ? 196.417 183.501 297.069 1.00 69.60  ? 192  PHE B CD1 1 
ATOM   1534  C CD2 . PHE A 1 209  ? 197.980 184.643 298.443 1.00 69.60  ? 192  PHE B CD2 1 
ATOM   1535  C CE1 . PHE A 1 209  ? 195.994 182.768 298.156 1.00 69.60  ? 192  PHE B CE1 1 
ATOM   1536  C CE2 . PHE A 1 209  ? 197.559 183.910 299.532 1.00 69.60  ? 192  PHE B CE2 1 
ATOM   1537  C CZ  . PHE A 1 209  ? 196.566 182.971 299.387 1.00 69.60  ? 192  PHE B CZ  1 
ATOM   1538  N N   . THR A 1 210  ? 198.459 184.769 292.835 1.00 69.92  ? 193  THR B N   1 
ATOM   1539  C CA  . THR A 1 210  ? 198.598 185.366 291.486 1.00 69.92  ? 193  THR B CA  1 
ATOM   1540  C C   . THR A 1 210  ? 197.251 185.353 290.770 1.00 69.92  ? 193  THR B C   1 
ATOM   1541  O O   . THR A 1 210  ? 196.577 184.325 290.800 1.00 69.92  ? 193  THR B O   1 
ATOM   1542  C CB  . THR A 1 210  ? 199.616 184.639 290.608 1.00 69.92  ? 193  THR B CB  1 
ATOM   1543  O OG1 . THR A 1 210  ? 199.642 185.364 289.383 1.00 69.92  ? 193  THR B OG1 1 
ATOM   1544  C CG2 . THR A 1 210  ? 199.271 183.204 290.301 1.00 69.92  ? 193  THR B CG2 1 
ATOM   1545  N N   . PHE A 1 211  ? 196.860 186.478 290.184 1.00 73.34  ? 194  PHE B N   1 
ATOM   1546  C CA  . PHE A 1 211  ? 195.619 186.527 289.391 1.00 73.34  ? 194  PHE B CA  1 
ATOM   1547  C C   . PHE A 1 211  ? 195.804 185.617 288.184 1.00 73.34  ? 194  PHE B C   1 
ATOM   1548  O O   . PHE A 1 211  ? 196.949 185.408 287.783 1.00 73.34  ? 194  PHE B O   1 
ATOM   1549  C CB  . PHE A 1 211  ? 195.407 187.937 288.860 1.00 73.34  ? 194  PHE B CB  1 
ATOM   1550  C CG  . PHE A 1 211  ? 195.522 189.070 289.843 1.00 73.34  ? 194  PHE B CG  1 
ATOM   1551  C CD1 . PHE A 1 211  ? 196.751 189.632 290.134 1.00 73.34  ? 194  PHE B CD1 1 
ATOM   1552  C CD2 . PHE A 1 211  ? 194.392 189.619 290.419 1.00 73.34  ? 194  PHE B CD2 1 
ATOM   1553  C CE1 . PHE A 1 211  ? 196.852 190.692 291.018 1.00 73.34  ? 194  PHE B CE1 1 
ATOM   1554  C CE2 . PHE A 1 211  ? 194.491 190.683 291.299 1.00 73.34  ? 194  PHE B CE2 1 
ATOM   1555  C CZ  . PHE A 1 211  ? 195.722 191.216 291.597 1.00 73.34  ? 194  PHE B CZ  1 
ATOM   1556  N N   . GLY A 1 212  ? 194.720 185.129 287.596 1.00 80.39  ? 195  GLY B N   1 
ATOM   1557  C CA  . GLY A 1 212  ? 194.828 184.305 286.382 1.00 80.39  ? 195  GLY B CA  1 
ATOM   1558  C C   . GLY A 1 212  ? 193.974 184.863 285.265 1.00 80.39  ? 195  GLY B C   1 
ATOM   1559  O O   . GLY A 1 212  ? 192.816 185.184 285.537 1.00 80.39  ? 195  GLY B O   1 
ATOM   1560  N N   . PHE A 1 213  ? 194.518 184.975 284.056 1.00 80.99  ? 196  PHE B N   1 
ATOM   1561  C CA  . PHE A 1 213  ? 193.782 185.567 282.914 1.00 80.99  ? 196  PHE B CA  1 
ATOM   1562  C C   . PHE A 1 213  ? 193.532 184.493 281.865 1.00 80.99  ? 196  PHE B C   1 
ATOM   1563  O O   . PHE A 1 213  ? 193.772 183.319 282.158 1.00 80.99  ? 196  PHE B O   1 
ATOM   1564  C CB  . PHE A 1 213  ? 194.560 186.722 282.287 1.00 80.99  ? 196  PHE B CB  1 
ATOM   1565  C CG  . PHE A 1 213  ? 195.933 186.410 281.751 1.00 80.99  ? 196  PHE B CG  1 
ATOM   1566  C CD1 . PHE A 1 213  ? 196.986 186.130 282.603 1.00 80.99  ? 196  PHE B CD1 1 
ATOM   1567  C CD2 . PHE A 1 213  ? 196.184 186.453 280.392 1.00 80.99  ? 196  PHE B CD2 1 
ATOM   1568  C CE1 . PHE A 1 213  ? 198.249 185.856 282.108 1.00 80.99  ? 196  PHE B CE1 1 
ATOM   1569  C CE2 . PHE A 1 213  ? 197.448 186.185 279.897 1.00 80.99  ? 196  PHE B CE2 1 
ATOM   1570  C CZ  . PHE A 1 213  ? 198.478 185.888 280.756 1.00 80.99  ? 196  PHE B CZ  1 
ATOM   1571  N N   . GLU A 1 214  ? 193.048 184.892 280.693 1.00 97.09  ? 197  GLU B N   1 
ATOM   1572  C CA  . GLU A 1 214  ? 192.811 183.927 279.592 1.00 97.09  ? 197  GLU B CA  1 
ATOM   1573  C C   . GLU A 1 214  ? 193.242 184.597 278.295 1.00 97.09  ? 197  GLU B C   1 
ATOM   1574  O O   . GLU A 1 214  ? 192.733 185.692 278.019 1.00 97.09  ? 197  GLU B O   1 
ATOM   1575  C CB  . GLU A 1 214  ? 191.329 183.591 279.489 1.00 97.09  ? 197  GLU B CB  1 
ATOM   1576  C CG  . GLU A 1 214  ? 191.055 182.195 278.971 1.00 97.09  ? 197  GLU B CG  1 
ATOM   1577  C CD  . GLU A 1 214  ? 190.693 182.108 277.499 1.00 97.09  ? 197  GLU B CD  1 
ATOM   1578  O OE1 . GLU A 1 214  ? 189.580 181.641 277.197 1.00 97.09  ? 197  GLU B OE1 1 
ATOM   1579  O OE2 . GLU A 1 214  ? 191.527 182.497 276.659 1.00 97.09  ? 197  GLU B OE2 1 
ATOM   1580  N N   . GLU A 1 215  ? 194.139 183.978 277.533 1.00 109.23 ? 198  GLU B N   1 
ATOM   1581  C CA  . GLU A 1 215  ? 194.649 184.674 276.326 1.00 109.23 ? 198  GLU B CA  1 
ATOM   1582  C C   . GLU A 1 215  ? 194.157 183.959 275.073 1.00 109.23 ? 198  GLU B C   1 
ATOM   1583  O O   . GLU A 1 215  ? 194.298 182.730 275.000 1.00 109.23 ? 198  GLU B O   1 
ATOM   1584  C CB  . GLU A 1 215  ? 196.169 184.735 276.332 1.00 109.23 ? 198  GLU B CB  1 
ATOM   1585  C CG  . GLU A 1 215  ? 196.693 186.153 276.236 1.00 109.23 ? 198  GLU B CG  1 
ATOM   1586  C CD  . GLU A 1 215  ? 196.199 186.925 275.025 1.00 109.23 ? 198  GLU B CD  1 
ATOM   1587  O OE1 . GLU A 1 215  ? 196.194 186.348 273.920 1.00 109.23 ? 198  GLU B OE1 1 
ATOM   1588  O OE2 . GLU A 1 215  ? 195.825 188.102 275.189 1.00 109.23 ? 198  GLU B OE2 1 
ATOM   1589  N N   . SER A 1 216  ? 193.600 184.718 274.129 1.00 110.57 ? 199  SER B N   1 
ATOM   1590  C CA  . SER A 1 216  ? 193.078 184.127 272.901 1.00 110.57 ? 199  SER B CA  1 
ATOM   1591  C C   . SER A 1 216  ? 193.710 184.723 271.646 1.00 110.57 ? 199  SER B C   1 
ATOM   1592  O O   . SER A 1 216  ? 193.117 184.639 270.565 1.00 110.57 ? 199  SER B O   1 
ATOM   1593  C CB  . SER A 1 216  ? 191.556 184.280 272.839 1.00 110.57 ? 199  SER B CB  1 
ATOM   1594  O OG  . SER A 1 216  ? 191.181 185.646 272.836 1.00 110.57 ? 199  SER B OG  1 
ATOM   1595  N N   . LEU A 1 217  ? 194.893 185.320 271.756 1.00 119.97 ? 200  LEU B N   1 
ATOM   1596  C CA  . LEU A 1 217  ? 195.596 185.896 270.615 1.00 119.97 ? 200  LEU B CA  1 
ATOM   1597  C C   . LEU A 1 217  ? 197.039 185.410 270.577 1.00 119.97 ? 200  LEU B C   1 
ATOM   1598  O O   . LEU A 1 217  ? 197.957 186.153 270.219 1.00 119.97 ? 200  LEU B O   1 
ATOM   1599  C CB  . LEU A 1 217  ? 195.539 187.423 270.642 1.00 119.97 ? 200  LEU B CB  1 
ATOM   1600  C CG  . LEU A 1 217  ? 194.300 188.093 270.042 1.00 119.97 ? 200  LEU B CG  1 
ATOM   1601  C CD1 . LEU A 1 217  ? 193.124 188.049 271.005 1.00 119.97 ? 200  LEU B CD1 1 
ATOM   1602  C CD2 . LEU A 1 217  ? 194.610 189.523 269.639 1.00 119.97 ? 200  LEU B CD2 1 
ATOM   1603  N N   . GLU A 1 218  ? 197.257 184.148 270.950 1.00 139.71 ? 201  GLU B N   1 
ATOM   1604  C CA  . GLU A 1 218  ? 198.583 183.546 270.947 1.00 139.71 ? 201  GLU B CA  1 
ATOM   1605  C C   . GLU A 1 218  ? 198.730 182.482 269.865 1.00 139.71 ? 201  GLU B C   1 
ATOM   1606  O O   . GLU A 1 218  ? 199.858 182.132 269.506 1.00 139.71 ? 201  GLU B O   1 
ATOM   1607  C CB  . GLU A 1 218  ? 198.873 182.941 272.335 1.00 139.71 ? 201  GLU B CB  1 
ATOM   1608  C CG  . GLU A 1 218  ? 199.906 181.808 272.466 1.00 139.71 ? 201  GLU B CG  1 
ATOM   1609  C CD  . GLU A 1 218  ? 201.325 182.182 272.032 1.00 139.71 ? 201  GLU B CD  1 
ATOM   1610  O OE1 . GLU A 1 218  ? 202.264 181.474 272.453 1.00 139.71 ? 201  GLU B OE1 1 
ATOM   1611  O OE2 . GLU A 1 218  ? 201.527 183.185 271.315 1.00 139.71 ? 201  GLU B OE2 1 
ATOM   1612  N N   . VAL A 1 219  ? 197.617 182.018 269.289 1.00 146.35 ? 202  VAL B N   1 
ATOM   1613  C CA  . VAL A 1 219  ? 197.632 180.947 268.298 1.00 146.35 ? 202  VAL B CA  1 
ATOM   1614  C C   . VAL A 1 219  ? 198.485 181.295 267.084 1.00 146.35 ? 202  VAL B C   1 
ATOM   1615  O O   . VAL A 1 219  ? 198.918 180.396 266.353 1.00 146.35 ? 202  VAL B O   1 
ATOM   1616  C CB  . VAL A 1 219  ? 196.179 180.615 267.887 1.00 146.35 ? 202  VAL B CB  1 
ATOM   1617  C CG1 . VAL A 1 219  ? 195.542 181.793 267.161 1.00 146.35 ? 202  VAL B CG1 1 
ATOM   1618  C CG2 . VAL A 1 219  ? 196.117 179.347 267.045 1.00 146.35 ? 202  VAL B CG2 1 
ATOM   1619  N N   . ASP A 1 220  ? 198.757 182.584 266.855 1.00 151.89 ? 203  ASP B N   1 
ATOM   1620  C CA  . ASP A 1 220  ? 199.566 182.983 265.707 1.00 151.89 ? 203  ASP B CA  1 
ATOM   1621  C C   . ASP A 1 220  ? 200.977 182.411 265.760 1.00 151.89 ? 203  ASP B C   1 
ATOM   1622  O O   . ASP A 1 220  ? 201.642 182.336 264.722 1.00 151.89 ? 203  ASP B O   1 
ATOM   1623  C CB  . ASP A 1 220  ? 199.629 184.509 265.609 1.00 151.89 ? 203  ASP B CB  1 
ATOM   1624  C CG  . ASP A 1 220  ? 199.965 185.168 266.932 1.00 151.89 ? 203  ASP B CG  1 
ATOM   1625  O OD1 . ASP A 1 220  ? 200.133 184.445 267.935 1.00 151.89 ? 203  ASP B OD1 1 
ATOM   1626  O OD2 . ASP A 1 220  ? 200.066 186.412 266.968 1.00 151.89 ? 203  ASP B OD2 1 
ATOM   1627  N N   . THR A 1 221  ? 201.447 182.008 266.938 1.00 153.36 ? 204  THR B N   1 
ATOM   1628  C CA  . THR A 1 221  ? 202.760 181.393 267.091 1.00 153.36 ? 204  THR B CA  1 
ATOM   1629  C C   . THR A 1 221  ? 202.698 179.908 267.409 1.00 153.36 ? 204  THR B C   1 
ATOM   1630  O O   . THR A 1 221  ? 203.520 179.142 266.904 1.00 153.36 ? 204  THR B O   1 
ATOM   1631  C CB  . THR A 1 221  ? 203.556 182.108 268.191 1.00 153.36 ? 204  THR B CB  1 
ATOM   1632  O OG1 . THR A 1 221  ? 202.893 181.941 269.450 1.00 153.36 ? 204  THR B OG1 1 
ATOM   1633  C CG2 . THR A 1 221  ? 203.678 183.592 267.881 1.00 153.36 ? 204  THR B CG2 1 
ATOM   1634  N N   . ASN A 1 222  ? 201.741 179.478 268.233 1.00 146.13 ? 205  ASN B N   1 
ATOM   1635  C CA  . ASN A 1 222  ? 201.592 178.077 268.629 1.00 146.13 ? 205  ASN B CA  1 
ATOM   1636  C C   . ASN A 1 222  ? 200.177 177.619 268.310 1.00 146.13 ? 205  ASN B C   1 
ATOM   1637  O O   . ASN A 1 222  ? 199.286 177.669 269.173 1.00 146.13 ? 205  ASN B O   1 
ATOM   1638  C CB  . ASN A 1 222  ? 201.905 177.885 270.112 1.00 146.13 ? 205  ASN B CB  1 
ATOM   1639  C CG  . ASN A 1 222  ? 203.016 178.791 270.599 1.00 146.13 ? 205  ASN B CG  1 
ATOM   1640  O OD1 . ASN A 1 222  ? 204.031 178.967 269.925 1.00 146.13 ? 205  ASN B OD1 1 
ATOM   1641  N ND2 . ASN A 1 222  ? 202.831 179.372 271.777 1.00 146.13 ? 205  ASN B ND2 1 
ATOM   1642  N N   . PRO A 1 223  ? 199.918 177.172 267.078 1.00 148.12 ? 206  PRO B N   1 
ATOM   1643  C CA  . PRO A 1 223  ? 198.578 176.657 266.748 1.00 148.12 ? 206  PRO B CA  1 
ATOM   1644  C C   . PRO A 1 223  ? 198.188 175.422 267.541 1.00 148.12 ? 206  PRO B C   1 
ATOM   1645  O O   . PRO A 1 223  ? 196.991 175.132 267.652 1.00 148.12 ? 206  PRO B O   1 
ATOM   1646  C CB  . PRO A 1 223  ? 198.679 176.347 265.247 1.00 148.12 ? 206  PRO B CB  1 
ATOM   1647  C CG  . PRO A 1 223  ? 199.828 177.179 264.761 1.00 148.12 ? 206  PRO B CG  1 
ATOM   1648  C CD  . PRO A 1 223  ? 200.798 177.221 265.900 1.00 148.12 ? 206  PRO B CD  1 
ATOM   1649  N N   . LEU A 1 224  ? 199.153 174.690 268.095 1.00 143.50 ? 207  LEU B N   1 
ATOM   1650  C CA  . LEU A 1 224  ? 198.859 173.480 268.853 1.00 143.50 ? 207  LEU B CA  1 
ATOM   1651  C C   . LEU A 1 224  ? 198.370 173.766 270.266 1.00 143.50 ? 207  LEU B C   1 
ATOM   1652  O O   . LEU A 1 224  ? 197.991 172.825 270.974 1.00 143.50 ? 207  LEU B O   1 
ATOM   1653  C CB  . LEU A 1 224  ? 200.100 172.583 268.902 1.00 143.50 ? 207  LEU B CB  1 
ATOM   1654  C CG  . LEU A 1 224  ? 201.394 173.173 269.475 1.00 143.50 ? 207  LEU B CG  1 
ATOM   1655  C CD1 . LEU A 1 224  ? 201.520 172.905 270.971 1.00 143.50 ? 207  LEU B CD1 1 
ATOM   1656  C CD2 . LEU A 1 224  ? 202.607 172.642 268.725 1.00 143.50 ? 207  LEU B CD2 1 
ATOM   1657  N N   . LEU A 1 225  ? 198.372 175.027 270.692 1.00 140.19 ? 208  LEU B N   1 
ATOM   1658  C CA  . LEU A 1 225  ? 197.934 175.370 272.038 1.00 140.19 ? 208  LEU B CA  1 
ATOM   1659  C C   . LEU A 1 225  ? 196.449 175.070 272.210 1.00 140.19 ? 208  LEU B C   1 
ATOM   1660  O O   . LEU A 1 225  ? 195.655 175.176 271.271 1.00 140.19 ? 208  LEU B O   1 
ATOM   1661  C CB  . LEU A 1 225  ? 198.242 176.845 272.325 1.00 140.19 ? 208  LEU B CB  1 
ATOM   1662  C CG  . LEU A 1 225  ? 197.601 177.631 273.473 1.00 140.19 ? 208  LEU B CG  1 
ATOM   1663  C CD1 . LEU A 1 225  ? 198.528 178.758 273.878 1.00 140.19 ? 208  LEU B CD1 1 
ATOM   1664  C CD2 . LEU A 1 225  ? 196.260 178.219 273.067 1.00 140.19 ? 208  LEU B CD2 1 
ATOM   1665  N N   . GLY A 1 226  ? 196.075 174.685 273.429 1.00 138.10 ? 209  GLY B N   1 
ATOM   1666  C CA  . GLY A 1 226  ? 194.705 174.317 273.728 1.00 138.10 ? 209  GLY B CA  1 
ATOM   1667  C C   . GLY A 1 226  ? 193.852 175.491 274.161 1.00 138.10 ? 209  GLY B C   1 
ATOM   1668  O O   . GLY A 1 226  ? 193.678 176.450 273.405 1.00 138.10 ? 209  GLY B O   1 
ATOM   1669  N N   . ALA A 1 227  ? 193.301 175.421 275.368 1.00 123.39 ? 210  ALA B N   1 
ATOM   1670  C CA  . ALA A 1 227  ? 192.505 176.514 275.906 1.00 123.39 ? 210  ALA B CA  1 
ATOM   1671  C C   . ALA A 1 227  ? 193.437 177.608 276.427 1.00 123.39 ? 210  ALA B C   1 
ATOM   1672  O O   . ALA A 1 227  ? 194.656 177.561 276.245 1.00 123.39 ? 210  ALA B O   1 
ATOM   1673  C CB  . ALA A 1 227  ? 191.558 176.000 276.987 1.00 123.39 ? 210  ALA B CB  1 
ATOM   1674  N N   . GLY A 1 228  ? 192.868 178.613 277.086 1.00 105.28 ? 211  GLY B N   1 
ATOM   1675  C CA  . GLY A 1 228  ? 193.662 179.687 277.647 1.00 105.28 ? 211  GLY B CA  1 
ATOM   1676  C C   . GLY A 1 228  ? 194.025 179.443 279.098 1.00 105.28 ? 211  GLY B C   1 
ATOM   1677  O O   . GLY A 1 228  ? 194.782 178.517 279.406 1.00 105.28 ? 211  GLY B O   1 
ATOM   1678  N N   . LYS A 1 229  ? 193.490 180.273 279.994 1.00 94.80  ? 212  LYS B N   1 
ATOM   1679  C CA  . LYS A 1 229  ? 193.686 180.141 281.438 1.00 94.80  ? 212  LYS B CA  1 
ATOM   1680  C C   . LYS A 1 229  ? 195.176 180.179 281.793 1.00 94.80  ? 212  LYS B C   1 
ATOM   1681  O O   . LYS A 1 229  ? 195.764 179.212 282.275 1.00 94.80  ? 212  LYS B O   1 
ATOM   1682  C CB  . LYS A 1 229  ? 193.019 178.861 281.962 1.00 94.80  ? 212  LYS B CB  1 
ATOM   1683  C CG  . LYS A 1 229  ? 191.599 178.647 281.461 1.00 94.80  ? 212  LYS B CG  1 
ATOM   1684  C CD  . LYS A 1 229  ? 190.639 179.685 282.024 1.00 94.80  ? 212  LYS B CD  1 
ATOM   1685  C CE  . LYS A 1 229  ? 190.765 179.809 283.535 1.00 94.80  ? 212  LYS B CE  1 
ATOM   1686  N NZ  . LYS A 1 229  ? 190.287 178.586 284.235 1.00 94.80  ? 212  LYS B NZ  1 
ATOM   1687  N N   . PHE A 1 230  ? 195.772 181.334 281.525 1.00 92.03  ? 213  PHE B N   1 
ATOM   1688  C CA  . PHE A 1 230  ? 197.174 181.571 281.830 1.00 92.03  ? 213  PHE B CA  1 
ATOM   1689  C C   . PHE A 1 230  ? 197.310 182.293 283.164 1.00 92.03  ? 213  PHE B C   1 
ATOM   1690  O O   . PHE A 1 230  ? 196.465 183.107 283.540 1.00 92.03  ? 213  PHE B O   1 
ATOM   1691  C CB  . PHE A 1 230  ? 197.844 182.384 280.721 1.00 92.03  ? 213  PHE B CB  1 
ATOM   1692  C CG  . PHE A 1 230  ? 198.097 181.601 279.466 1.00 92.03  ? 213  PHE B CG  1 
ATOM   1693  C CD1 . PHE A 1 230  ? 197.060 181.307 278.597 1.00 92.03  ? 213  PHE B CD1 1 
ATOM   1694  C CD2 . PHE A 1 230  ? 199.368 181.153 279.160 1.00 92.03  ? 213  PHE B CD2 1 
ATOM   1695  C CE1 . PHE A 1 230  ? 197.289 180.585 277.444 1.00 92.03  ? 213  PHE B CE1 1 
ATOM   1696  C CE2 . PHE A 1 230  ? 199.604 180.430 278.008 1.00 92.03  ? 213  PHE B CE2 1 
ATOM   1697  C CZ  . PHE A 1 230  ? 198.562 180.146 277.150 1.00 92.03  ? 213  PHE B CZ  1 
ATOM   1698  N N   . ALA A 1 231  ? 198.427 182.003 283.844 1.00 83.02  ? 214  ALA B N   1 
ATOM   1699  C CA  . ALA A 1 231  ? 198.634 182.564 285.170 1.00 83.02  ? 214  ALA B CA  1 
ATOM   1700  C C   . ALA A 1 231  ? 199.614 183.724 285.079 1.00 83.02  ? 214  ALA B C   1 
ATOM   1701  O O   . ALA A 1 231  ? 200.667 183.604 284.445 1.00 83.02  ? 214  ALA B O   1 
ATOM   1702  C CB  . ALA A 1 231  ? 199.154 181.502 286.139 1.00 83.02  ? 214  ALA B CB  1 
ATOM   1703  N N   . THR A 1 232  ? 199.264 184.843 285.708 1.00 78.03  ? 215  THR B N   1 
ATOM   1704  C CA  . THR A 1 232  ? 200.117 186.023 285.670 1.00 78.03  ? 215  THR B CA  1 
ATOM   1705  C C   . THR A 1 232  ? 201.373 185.797 286.502 1.00 78.03  ? 215  THR B C   1 
ATOM   1706  O O   . THR A 1 232  ? 201.303 185.319 287.638 1.00 78.03  ? 215  THR B O   1 
ATOM   1707  C CB  . THR A 1 232  ? 199.355 187.244 286.182 1.00 78.03  ? 215  THR B CB  1 
ATOM   1708  O OG1 . THR A 1 232  ? 198.233 187.499 285.330 1.00 78.03  ? 215  THR B OG1 1 
ATOM   1709  C CG2 . THR A 1 232  ? 200.252 188.467 286.195 1.00 78.03  ? 215  THR B CG2 1 
ATOM   1710  N N   . ASP A 1 233  ? 202.519 186.139 285.933 1.00 76.67  ? 216  ASP B N   1 
ATOM   1711  C CA  . ASP A 1 233  ? 203.782 185.990 286.640 1.00 76.67  ? 216  ASP B CA  1 
ATOM   1712  C C   . ASP A 1 233  ? 203.888 187.050 287.730 1.00 76.67  ? 216  ASP B C   1 
ATOM   1713  O O   . ASP A 1 233  ? 203.748 188.243 287.439 1.00 76.67  ? 216  ASP B O   1 
ATOM   1714  C CB  . ASP A 1 233  ? 204.944 186.116 285.661 1.00 76.67  ? 216  ASP B CB  1 
ATOM   1715  C CG  . ASP A 1 233  ? 206.200 185.438 286.154 1.00 76.67  ? 216  ASP B CG  1 
ATOM   1716  O OD1 . ASP A 1 233  ? 206.550 185.612 287.338 1.00 76.67  ? 216  ASP B OD1 1 
ATOM   1717  O OD2 . ASP A 1 233  ? 206.840 184.727 285.353 1.00 76.67  ? 216  ASP B OD2 1 
ATOM   1718  N N   . PRO A 1 234  ? 204.129 186.666 288.986 1.00 72.07  ? 217  PRO B N   1 
ATOM   1719  C CA  . PRO A 1 234  ? 204.185 187.669 290.063 1.00 72.07  ? 217  PRO B CA  1 
ATOM   1720  C C   . PRO A 1 234  ? 205.282 188.702 289.884 1.00 72.07  ? 217  PRO B C   1 
ATOM   1721  O O   . PRO A 1 234  ? 205.173 189.802 290.444 1.00 72.07  ? 217  PRO B O   1 
ATOM   1722  C CB  . PRO A 1 234  ? 204.414 186.824 291.323 1.00 72.07  ? 217  PRO B CB  1 
ATOM   1723  C CG  . PRO A 1 234  ? 204.925 185.516 290.830 1.00 72.07  ? 217  PRO B CG  1 
ATOM   1724  C CD  . PRO A 1 234  ? 204.292 185.297 289.496 1.00 72.07  ? 217  PRO B CD  1 
ATOM   1725  N N   . ALA A 1 235  ? 206.332 188.388 289.123 1.00 69.66  ? 218  ALA B N   1 
ATOM   1726  C CA  . ALA A 1 235  ? 207.392 189.362 288.891 1.00 69.66  ? 218  ALA B CA  1 
ATOM   1727  C C   . ALA A 1 235  ? 206.853 190.597 288.184 1.00 69.66  ? 218  ALA B C   1 
ATOM   1728  O O   . ALA A 1 235  ? 207.239 191.725 288.509 1.00 69.66  ? 218  ALA B O   1 
ATOM   1729  C CB  . ALA A 1 235  ? 208.520 188.728 288.081 1.00 69.66  ? 218  ALA B CB  1 
ATOM   1730  N N   . VAL A 1 236  ? 205.949 190.406 287.223 1.00 69.60  ? 219  VAL B N   1 
ATOM   1731  C CA  . VAL A 1 236  ? 205.365 191.540 286.513 1.00 69.60  ? 219  VAL B CA  1 
ATOM   1732  C C   . VAL A 1 236  ? 204.540 192.399 287.463 1.00 69.60  ? 219  VAL B C   1 
ATOM   1733  O O   . VAL A 1 236  ? 204.574 193.633 287.394 1.00 69.60  ? 219  VAL B O   1 
ATOM   1734  C CB  . VAL A 1 236  ? 204.529 191.048 285.320 1.00 69.60  ? 219  VAL B CB  1 
ATOM   1735  C CG1 . VAL A 1 236  ? 203.769 192.197 284.706 1.00 69.60  ? 219  VAL B CG1 1 
ATOM   1736  C CG2 . VAL A 1 236  ? 205.424 190.394 284.289 1.00 69.60  ? 219  VAL B CG2 1 
ATOM   1737  N N   . THR A 1 237  ? 203.777 191.764 288.356 1.00 69.60  ? 220  THR B N   1 
ATOM   1738  C CA  . THR A 1 237  ? 202.984 192.521 289.320 1.00 69.60  ? 220  THR B CA  1 
ATOM   1739  C C   . THR A 1 237  ? 203.875 193.330 290.255 1.00 69.60  ? 220  THR B C   1 
ATOM   1740  O O   . THR A 1 237  ? 203.599 194.508 290.536 1.00 69.60  ? 220  THR B O   1 
ATOM   1741  C CB  . THR A 1 237  ? 202.095 191.570 290.118 1.00 69.60  ? 220  THR B CB  1 
ATOM   1742  O OG1 . THR A 1 237  ? 201.104 191.001 289.254 1.00 69.60  ? 220  THR B OG1 1 
ATOM   1743  C CG2 . THR A 1 237  ? 201.409 192.312 291.248 1.00 69.60  ? 220  THR B CG2 1 
ATOM   1744  N N   . LEU A 1 238  ? 204.954 192.718 290.745 1.00 69.60  ? 221  LEU B N   1 
ATOM   1745  C CA  . LEU A 1 238  ? 205.878 193.458 291.594 1.00 69.60  ? 221  LEU B CA  1 
ATOM   1746  C C   . LEU A 1 238  ? 206.523 194.602 290.827 1.00 69.60  ? 221  LEU B C   1 
ATOM   1747  O O   . LEU A 1 238  ? 206.759 195.676 291.387 1.00 69.60  ? 221  LEU B O   1 
ATOM   1748  C CB  . LEU A 1 238  ? 206.941 192.525 292.168 1.00 69.60  ? 221  LEU B CB  1 
ATOM   1749  C CG  . LEU A 1 238  ? 207.844 193.162 293.224 1.00 69.60  ? 221  LEU B CG  1 
ATOM   1750  C CD1 . LEU A 1 238  ? 207.028 193.979 294.206 1.00 69.60  ? 221  LEU B CD1 1 
ATOM   1751  C CD2 . LEU A 1 238  ? 208.639 192.099 293.951 1.00 69.60  ? 221  LEU B CD2 1 
ATOM   1752  N N   . ALA A 1 239  ? 206.810 194.393 289.540 1.00 69.60  ? 222  ALA B N   1 
ATOM   1753  C CA  . ALA A 1 239  ? 207.357 195.470 288.722 1.00 69.60  ? 222  ALA B CA  1 
ATOM   1754  C C   . ALA A 1 239  ? 206.362 196.612 288.578 1.00 69.60  ? 222  ALA B C   1 
ATOM   1755  O O   . ALA A 1 239  ? 206.747 197.783 288.588 1.00 69.60  ? 222  ALA B O   1 
ATOM   1756  C CB  . ALA A 1 239  ? 207.759 194.936 287.350 1.00 69.60  ? 222  ALA B CB  1 
ATOM   1757  N N   . HIS A 1 240  ? 205.080 196.287 288.425 1.00 69.60  ? 223  HIS B N   1 
ATOM   1758  C CA  . HIS A 1 240  ? 204.050 197.320 288.347 1.00 69.60  ? 223  HIS B CA  1 
ATOM   1759  C C   . HIS A 1 240  ? 204.019 198.148 289.626 1.00 69.60  ? 223  HIS B C   1 
ATOM   1760  O O   . HIS A 1 240  ? 203.973 199.387 289.588 1.00 69.60  ? 223  HIS B O   1 
ATOM   1761  C CB  . HIS A 1 240  ? 202.694 196.663 288.083 1.00 69.60  ? 223  HIS B CB  1 
ATOM   1762  C CG  . HIS A 1 240  ? 201.544 197.620 288.027 1.00 69.60  ? 223  HIS B CG  1 
ATOM   1763  N ND1 . HIS A 1 240  ? 200.884 197.918 286.855 1.00 69.60  ? 223  HIS B ND1 1 
ATOM   1764  C CD2 . HIS A 1 240  ? 200.913 198.319 289.000 1.00 69.60  ? 223  HIS B CD2 1 
ATOM   1765  C CE1 . HIS A 1 240  ? 199.908 198.772 287.105 1.00 69.60  ? 223  HIS B CE1 1 
ATOM   1766  N NE2 . HIS A 1 240  ? 199.904 199.032 288.399 1.00 69.60  ? 223  HIS B NE2 1 
ATOM   1767  N N   . GLN A 1 241  ? 204.062 197.476 290.776 1.00 69.60  ? 224  GLN B N   1 
ATOM   1768  C CA  . GLN A 1 241  ? 204.069 198.209 292.039 1.00 69.60  ? 224  GLN B CA  1 
ATOM   1769  C C   . GLN A 1 241  ? 205.337 199.043 292.189 1.00 69.60  ? 224  GLN B C   1 
ATOM   1770  O O   . GLN A 1 241  ? 205.294 200.170 292.698 1.00 69.60  ? 224  GLN B O   1 
ATOM   1771  C CB  . GLN A 1 241  ? 203.910 197.248 293.211 1.00 69.60  ? 224  GLN B CB  1 
ATOM   1772  C CG  . GLN A 1 241  ? 202.634 196.451 293.148 1.00 69.60  ? 224  GLN B CG  1 
ATOM   1773  C CD  . GLN A 1 241  ? 201.424 197.338 292.999 1.00 69.60  ? 224  GLN B CD  1 
ATOM   1774  O OE1 . GLN A 1 241  ? 201.229 198.272 293.772 1.00 69.60  ? 224  GLN B OE1 1 
ATOM   1775  N NE2 . GLN A 1 241  ? 200.604 197.055 291.998 1.00 69.60  ? 224  GLN B NE2 1 
ATOM   1776  N N   . LEU A 1 242  ? 206.477 198.508 291.751 1.00 69.60  ? 225  LEU B N   1 
ATOM   1777  C CA  . LEU A 1 242  ? 207.723 199.263 291.822 1.00 69.60  ? 225  LEU B CA  1 
ATOM   1778  C C   . LEU A 1 242  ? 207.671 200.491 290.924 1.00 69.60  ? 225  LEU B C   1 
ATOM   1779  O O   . LEU A 1 242  ? 208.224 201.536 291.269 1.00 69.60  ? 225  LEU B O   1 
ATOM   1780  C CB  . LEU A 1 242  ? 208.905 198.373 291.444 1.00 69.60  ? 225  LEU B CB  1 
ATOM   1781  C CG  . LEU A 1 242  ? 209.334 197.312 292.456 1.00 69.60  ? 225  LEU B CG  1 
ATOM   1782  C CD1 . LEU A 1 242  ? 210.751 196.861 292.178 1.00 69.60  ? 225  LEU B CD1 1 
ATOM   1783  C CD2 . LEU A 1 242  ? 209.212 197.828 293.870 1.00 69.60  ? 225  LEU B CD2 1 
ATOM   1784  N N   . ILE A 1 243  ? 207.025 200.380 289.763 1.00 69.60  ? 226  ILE B N   1 
ATOM   1785  C CA  . ILE A 1 243  ? 206.865 201.534 288.884 1.00 69.60  ? 226  ILE B CA  1 
ATOM   1786  C C   . ILE A 1 243  ? 206.002 202.594 289.550 1.00 69.60  ? 226  ILE B C   1 
ATOM   1787  O O   . ILE A 1 243  ? 206.294 203.794 289.471 1.00 69.60  ? 226  ILE B O   1 
ATOM   1788  C CB  . ILE A 1 243  ? 206.277 201.099 287.531 1.00 69.60  ? 226  ILE B CB  1 
ATOM   1789  C CG1 . ILE A 1 243  ? 207.292 200.278 286.747 1.00 69.60  ? 226  ILE B CG1 1 
ATOM   1790  C CG2 . ILE A 1 243  ? 205.870 202.305 286.721 1.00 69.60  ? 226  ILE B CG2 1 
ATOM   1791  C CD1 . ILE A 1 243  ? 206.742 199.721 285.465 1.00 69.60  ? 226  ILE B CD1 1 
ATOM   1792  N N   . HIS A 1 244  ? 204.917 202.172 290.205 1.00 69.60  ? 227  HIS B N   1 
ATOM   1793  C CA  . HIS A 1 244  ? 204.103 203.128 290.953 1.00 69.60  ? 227  HIS B CA  1 
ATOM   1794  C C   . HIS A 1 244  ? 204.934 203.833 292.019 1.00 69.60  ? 227  HIS B C   1 
ATOM   1795  O O   . HIS A 1 244  ? 204.860 205.061 292.175 1.00 69.60  ? 227  HIS B O   1 
ATOM   1796  C CB  . HIS A 1 244  ? 202.914 202.418 291.596 1.00 69.60  ? 227  HIS B CB  1 
ATOM   1797  C CG  . HIS A 1 244  ? 201.718 202.308 290.707 1.00 69.60  ? 227  HIS B CG  1 
ATOM   1798  N ND1 . HIS A 1 244  ? 201.300 203.336 289.892 1.00 69.60  ? 227  HIS B ND1 1 
ATOM   1799  C CD2 . HIS A 1 244  ? 200.847 201.292 290.509 1.00 69.60  ? 227  HIS B CD2 1 
ATOM   1800  C CE1 . HIS A 1 244  ? 200.224 202.956 289.227 1.00 69.60  ? 227  HIS B CE1 1 
ATOM   1801  N NE2 . HIS A 1 244  ? 199.928 201.720 289.584 1.00 69.60  ? 227  HIS B NE2 1 
ATOM   1802  N N   . ALA A 1 245  ? 205.739 203.066 292.757 1.00 69.60  ? 228  ALA B N   1 
ATOM   1803  C CA  . ALA A 1 245  ? 206.574 203.651 293.800 1.00 69.60  ? 228  ALA B CA  1 
ATOM   1804  C C   . ALA A 1 245  ? 207.611 204.597 293.212 1.00 69.60  ? 228  ALA B C   1 
ATOM   1805  O O   . ALA A 1 245  ? 207.935 205.623 293.815 1.00 69.60  ? 228  ALA B O   1 
ATOM   1806  C CB  . ALA A 1 245  ? 207.254 202.548 294.608 1.00 69.60  ? 228  ALA B CB  1 
ATOM   1807  N N   . GLY A 1 246  ? 208.157 204.258 292.046 1.00 69.60  ? 229  GLY B N   1 
ATOM   1808  C CA  . GLY A 1 246  ? 209.124 205.134 291.408 1.00 69.60  ? 229  GLY B CA  1 
ATOM   1809  C C   . GLY A 1 246  ? 208.508 206.440 290.954 1.00 69.60  ? 229  GLY B C   1 
ATOM   1810  O O   . GLY A 1 246  ? 209.129 207.500 291.065 1.00 69.60  ? 229  GLY B O   1 
ATOM   1811  N N   . HIS A 1 247  ? 207.284 206.385 290.429 1.00 69.60  ? 230  HIS B N   1 
ATOM   1812  C CA  . HIS A 1 247  ? 206.585 207.617 290.079 1.00 69.60  ? 230  HIS B CA  1 
ATOM   1813  C C   . HIS A 1 247  ? 206.348 208.473 291.314 1.00 69.60  ? 230  HIS B C   1 
ATOM   1814  O O   . HIS A 1 247  ? 206.611 209.679 291.308 1.00 69.60  ? 230  HIS B O   1 
ATOM   1815  C CB  . HIS A 1 247  ? 205.256 207.304 289.394 1.00 69.60  ? 230  HIS B CB  1 
ATOM   1816  C CG  . HIS A 1 247  ? 205.401 206.712 288.030 1.00 69.60  ? 230  HIS B CG  1 
ATOM   1817  N ND1 . HIS A 1 247  ? 204.326 206.249 287.304 1.00 69.60  ? 230  HIS B ND1 1 
ATOM   1818  C CD2 . HIS A 1 247  ? 206.493 206.501 287.261 1.00 69.60  ? 230  HIS B CD2 1 
ATOM   1819  C CE1 . HIS A 1 247  ? 204.750 205.781 286.144 1.00 69.60  ? 230  HIS B CE1 1 
ATOM   1820  N NE2 . HIS A 1 247  ? 206.061 205.922 286.093 1.00 69.60  ? 230  HIS B NE2 1 
ATOM   1821  N N   . ARG A 1 248  ? 205.863 207.860 292.395 1.00 69.60  ? 231  ARG B N   1 
ATOM   1822  C CA  . ARG A 1 248  ? 205.523 208.635 293.583 1.00 69.60  ? 231  ARG B CA  1 
ATOM   1823  C C   . ARG A 1 248  ? 206.743 209.088 294.373 1.00 69.60  ? 231  ARG B C   1 
ATOM   1824  O O   . ARG A 1 248  ? 206.631 210.017 295.176 1.00 69.60  ? 231  ARG B O   1 
ATOM   1825  C CB  . ARG A 1 248  ? 204.598 207.828 294.494 1.00 69.60  ? 231  ARG B CB  1 
ATOM   1826  C CG  . ARG A 1 248  ? 203.272 207.460 293.857 1.00 69.60  ? 231  ARG B CG  1 
ATOM   1827  C CD  . ARG A 1 248  ? 202.605 206.336 294.619 1.00 69.60  ? 231  ARG B CD  1 
ATOM   1828  N NE  . ARG A 1 248  ? 201.762 206.835 295.696 1.00 69.60  ? 231  ARG B NE  1 
ATOM   1829  C CZ  . ARG A 1 248  ? 200.437 206.821 295.674 1.00 69.60  ? 231  ARG B CZ  1 
ATOM   1830  N NH1 . ARG A 1 248  ? 199.770 206.318 294.649 1.00 69.60  ? 231  ARG B NH1 1 
ATOM   1831  N NH2 . ARG A 1 248  ? 199.765 207.321 296.706 1.00 69.60  ? 231  ARG B NH2 1 
ATOM   1832  N N   . LEU A 1 249  ? 207.899 208.454 294.170 1.00 69.60  ? 232  LEU B N   1 
ATOM   1833  C CA  . LEU A 1 249  ? 209.095 208.825 294.919 1.00 69.60  ? 232  LEU B CA  1 
ATOM   1834  C C   . LEU A 1 249  ? 209.693 210.128 294.409 1.00 69.60  ? 232  LEU B C   1 
ATOM   1835  O O   . LEU A 1 249  ? 210.307 210.871 295.181 1.00 69.60  ? 232  LEU B O   1 
ATOM   1836  C CB  . LEU A 1 249  ? 210.128 207.702 294.845 1.00 69.60  ? 232  LEU B CB  1 
ATOM   1837  C CG  . LEU A 1 249  ? 210.188 206.747 296.033 1.00 69.60  ? 232  LEU B CG  1 
ATOM   1838  C CD1 . LEU A 1 249  ? 211.226 205.681 295.790 1.00 69.60  ? 232  LEU B CD1 1 
ATOM   1839  C CD2 . LEU A 1 249  ? 210.507 207.511 297.293 1.00 69.60  ? 232  LEU B CD2 1 
ATOM   1840  N N   . TYR A 1 250  ? 209.540 210.412 293.122 1.00 69.60  ? 233  TYR B N   1 
ATOM   1841  C CA  . TYR A 1 250  ? 209.962 211.682 292.556 1.00 69.60  ? 233  TYR B CA  1 
ATOM   1842  C C   . TYR A 1 250  ? 208.839 212.706 292.537 1.00 69.60  ? 233  TYR B C   1 
ATOM   1843  O O   . TYR A 1 250  ? 209.030 213.808 292.014 1.00 69.60  ? 233  TYR B O   1 
ATOM   1844  C CB  . TYR A 1 250  ? 210.509 211.472 291.144 1.00 69.60  ? 233  TYR B CB  1 
ATOM   1845  C CG  . TYR A 1 250  ? 211.772 210.651 291.117 1.00 69.60  ? 233  TYR B CG  1 
ATOM   1846  C CD1 . TYR A 1 250  ? 213.016 211.250 291.222 1.00 69.60  ? 233  TYR B CD1 1 
ATOM   1847  C CD2 . TYR A 1 250  ? 211.718 209.272 291.000 1.00 69.60  ? 233  TYR B CD2 1 
ATOM   1848  C CE1 . TYR A 1 250  ? 214.170 210.499 291.204 1.00 69.60  ? 233  TYR B CE1 1 
ATOM   1849  C CE2 . TYR A 1 250  ? 212.864 208.513 290.982 1.00 69.60  ? 233  TYR B CE2 1 
ATOM   1850  C CZ  . TYR A 1 250  ? 214.087 209.129 291.084 1.00 69.60  ? 233  TYR B CZ  1 
ATOM   1851  O OH  . TYR A 1 250  ? 215.230 208.365 291.064 1.00 69.60  ? 233  TYR B OH  1 
ATOM   1852  N N   . GLY A 1 251  ? 207.678 212.368 293.087 1.00 69.60  ? 234  GLY B N   1 
ATOM   1853  C CA  . GLY A 1 251  ? 206.592 213.326 293.201 1.00 69.60  ? 234  GLY B CA  1 
ATOM   1854  C C   . GLY A 1 251  ? 206.043 213.798 291.875 1.00 69.60  ? 234  GLY B C   1 
ATOM   1855  O O   . GLY A 1 251  ? 205.656 214.966 291.748 1.00 69.60  ? 234  GLY B O   1 
ATOM   1856  N N   . ILE A 1 252  ? 205.998 212.918 290.880 1.00 69.60  ? 235  ILE B N   1 
ATOM   1857  C CA  . ILE A 1 252  ? 205.450 213.258 289.577 1.00 69.60  ? 235  ILE B CA  1 
ATOM   1858  C C   . ILE A 1 252  ? 204.225 212.406 289.248 1.00 69.60  ? 235  ILE B C   1 
ATOM   1859  O O   . ILE A 1 252  ? 203.888 212.222 288.085 1.00 69.60  ? 235  ILE B O   1 
ATOM   1860  C CB  . ILE A 1 252  ? 206.526 213.157 288.479 1.00 69.60  ? 235  ILE B CB  1 
ATOM   1861  C CG1 . ILE A 1 252  ? 206.934 211.707 288.235 1.00 69.60  ? 235  ILE B CG1 1 
ATOM   1862  C CG2 . ILE A 1 252  ? 207.745 213.974 288.854 1.00 69.60  ? 235  ILE B CG2 1 
ATOM   1863  C CD1 . ILE A 1 252  ? 207.876 211.541 287.068 1.00 69.60  ? 235  ILE B CD1 1 
ATOM   1864  N N   . ALA A 1 253  ? 203.544 211.894 290.269 1.00 69.60  ? 236  ALA B N   1 
ATOM   1865  C CA  . ALA A 1 253  ? 202.343 211.099 290.062 1.00 69.60  ? 236  ALA B CA  1 
ATOM   1866  C C   . ALA A 1 253  ? 201.148 211.996 289.768 1.00 69.60  ? 236  ALA B C   1 
ATOM   1867  O O   . ALA A 1 253  ? 201.009 213.079 290.343 1.00 69.60  ? 236  ALA B O   1 
ATOM   1868  C CB  . ALA A 1 253  ? 202.057 210.237 291.289 1.00 69.60  ? 236  ALA B CB  1 
ATOM   1869  N N   . ILE A 1 254  ? 200.280 211.538 288.864 1.00 72.79  ? 237  ILE B N   1 
ATOM   1870  C CA  . ILE A 1 254  ? 199.094 212.308 288.514 1.00 72.79  ? 237  ILE B CA  1 
ATOM   1871  C C   . ILE A 1 254  ? 198.115 212.296 289.682 1.00 72.79  ? 237  ILE B C   1 
ATOM   1872  O O   . ILE A 1 254  ? 198.022 211.319 290.438 1.00 72.79  ? 237  ILE B O   1 
ATOM   1873  C CB  . ILE A 1 254  ? 198.436 211.754 287.236 1.00 72.79  ? 237  ILE B CB  1 
ATOM   1874  C CG1 . ILE A 1 254  ? 199.417 211.773 286.069 1.00 72.79  ? 237  ILE B CG1 1 
ATOM   1875  C CG2 . ILE A 1 254  ? 197.209 212.559 286.856 1.00 72.79  ? 237  ILE B CG2 1 
ATOM   1876  C CD1 . ILE A 1 254  ? 200.077 210.452 285.832 1.00 72.79  ? 237  ILE B CD1 1 
ATOM   1877  N N   . ASN A 1 255  ? 197.380 213.392 289.833 1.00 80.69  ? 238  ASN B N   1 
ATOM   1878  C CA  . ASN A 1 255  ? 196.372 213.479 290.876 1.00 80.69  ? 238  ASN B CA  1 
ATOM   1879  C C   . ASN A 1 255  ? 195.332 212.375 290.689 1.00 80.69  ? 238  ASN B C   1 
ATOM   1880  O O   . ASN A 1 255  ? 194.961 212.057 289.554 1.00 80.69  ? 238  ASN B O   1 
ATOM   1881  C CB  . ASN A 1 255  ? 195.692 214.847 290.842 1.00 80.69  ? 238  ASN B CB  1 
ATOM   1882  C CG  . ASN A 1 255  ? 196.665 215.976 290.592 1.00 80.69  ? 238  ASN B CG  1 
ATOM   1883  O OD1 . ASN A 1 255  ? 197.382 215.983 289.594 1.00 80.69  ? 238  ASN B OD1 1 
ATOM   1884  N ND2 . ASN A 1 255  ? 196.674 216.956 291.487 1.00 80.69  ? 238  ASN B ND2 1 
ATOM   1885  N N   . PRO A 1 256  ? 194.855 211.761 291.773 1.00 82.45  ? 239  PRO B N   1 
ATOM   1886  C CA  . PRO A 1 256  ? 193.895 210.655 291.630 1.00 82.45  ? 239  PRO B CA  1 
ATOM   1887  C C   . PRO A 1 256  ? 192.564 211.055 291.019 1.00 82.45  ? 239  PRO B C   1 
ATOM   1888  O O   . PRO A 1 256  ? 191.882 210.190 290.458 1.00 82.45  ? 239  PRO B O   1 
ATOM   1889  C CB  . PRO A 1 256  ? 193.719 210.157 293.070 1.00 82.45  ? 239  PRO B CB  1 
ATOM   1890  C CG  . PRO A 1 256  ? 194.089 211.317 293.918 1.00 82.45  ? 239  PRO B CG  1 
ATOM   1891  C CD  . PRO A 1 256  ? 195.173 212.039 293.182 1.00 82.45  ? 239  PRO B CD  1 
ATOM   1892  N N   . ASN A 1 257  ? 192.158 212.325 291.111 1.00 82.30  ? 240  ASN B N   1 
ATOM   1893  C CA  . ASN A 1 257  ? 190.872 212.713 290.541 1.00 82.30  ? 240  ASN B CA  1 
ATOM   1894  C C   . ASN A 1 257  ? 190.910 212.780 289.020 1.00 82.30  ? 240  ASN B C   1 
ATOM   1895  O O   . ASN A 1 257  ? 189.849 212.770 288.388 1.00 82.30  ? 240  ASN B O   1 
ATOM   1896  C CB  . ASN A 1 257  ? 190.405 214.054 291.110 1.00 82.30  ? 240  ASN B CB  1 
ATOM   1897  C CG  . ASN A 1 257  ? 191.528 215.053 291.246 1.00 82.30  ? 240  ASN B CG  1 
ATOM   1898  O OD1 . ASN A 1 257  ? 192.697 214.685 291.261 1.00 82.30  ? 240  ASN B OD1 1 
ATOM   1899  N ND2 . ASN A 1 257  ? 191.176 216.330 291.344 1.00 82.30  ? 240  ASN B ND2 1 
ATOM   1900  N N   . ARG A 1 258  ? 192.096 212.853 288.420 1.00 79.68  ? 241  ARG B N   1 
ATOM   1901  C CA  . ARG A 1 258  ? 192.207 212.753 286.971 1.00 79.68  ? 241  ARG B CA  1 
ATOM   1902  C C   . ARG A 1 258  ? 191.947 211.316 286.547 1.00 79.68  ? 241  ARG B C   1 
ATOM   1903  O O   . ARG A 1 258  ? 192.862 210.488 286.540 1.00 79.68  ? 241  ARG B O   1 
ATOM   1904  C CB  . ARG A 1 258  ? 193.584 213.214 286.497 1.00 79.68  ? 241  ARG B CB  1 
ATOM   1905  C CG  . ARG A 1 258  ? 193.799 214.707 286.601 1.00 79.68  ? 241  ARG B CG  1 
ATOM   1906  C CD  . ARG A 1 258  ? 192.785 215.456 285.758 1.00 79.68  ? 241  ARG B CD  1 
ATOM   1907  N NE  . ARG A 1 258  ? 193.271 215.691 284.404 1.00 79.68  ? 241  ARG B NE  1 
ATOM   1908  C CZ  . ARG A 1 258  ? 194.110 216.661 284.070 1.00 79.68  ? 241  ARG B CZ  1 
ATOM   1909  N NH1 . ARG A 1 258  ? 194.582 217.507 284.970 1.00 79.68  ? 241  ARG B NH1 1 
ATOM   1910  N NH2 . ARG A 1 258  ? 194.484 216.786 282.800 1.00 79.68  ? 241  ARG B NH2 1 
ATOM   1911  N N   . VAL A 1 259  ? 190.703 211.014 286.190 1.00 79.34  ? 242  VAL B N   1 
ATOM   1912  C CA  . VAL A 1 259  ? 190.250 209.647 285.977 1.00 79.34  ? 242  VAL B CA  1 
ATOM   1913  C C   . VAL A 1 259  ? 189.642 209.534 284.586 1.00 79.34  ? 242  VAL B C   1 
ATOM   1914  O O   . VAL A 1 259  ? 188.975 210.458 284.109 1.00 79.34  ? 242  VAL B O   1 
ATOM   1915  C CB  . VAL A 1 259  ? 189.241 209.224 287.066 1.00 79.34  ? 242  VAL B CB  1 
ATOM   1916  C CG1 . VAL A 1 259  ? 188.095 210.220 287.148 1.00 79.34  ? 242  VAL B CG1 1 
ATOM   1917  C CG2 . VAL A 1 259  ? 188.725 207.817 286.819 1.00 79.34  ? 242  VAL B CG2 1 
ATOM   1918  N N   . PHE A 1 260  ? 189.893 208.402 283.932 1.00 78.18  ? 243  PHE B N   1 
ATOM   1919  C CA  . PHE A 1 260  ? 189.342 208.105 282.617 1.00 78.18  ? 243  PHE B CA  1 
ATOM   1920  C C   . PHE A 1 260  ? 187.851 207.808 282.725 1.00 78.18  ? 243  PHE B C   1 
ATOM   1921  O O   . PHE A 1 260  ? 187.461 206.666 282.983 1.00 78.18  ? 243  PHE B O   1 
ATOM   1922  C CB  . PHE A 1 260  ? 190.084 206.915 282.006 1.00 78.18  ? 243  PHE B CB  1 
ATOM   1923  C CG  . PHE A 1 260  ? 190.066 206.878 280.510 1.00 78.18  ? 243  PHE B CG  1 
ATOM   1924  C CD1 . PHE A 1 260  ? 190.462 207.974 279.770 1.00 78.18  ? 243  PHE B CD1 1 
ATOM   1925  C CD2 . PHE A 1 260  ? 189.666 205.735 279.843 1.00 78.18  ? 243  PHE B CD2 1 
ATOM   1926  C CE1 . PHE A 1 260  ? 190.451 207.931 278.392 1.00 78.18  ? 243  PHE B CE1 1 
ATOM   1927  C CE2 . PHE A 1 260  ? 189.652 205.689 278.468 1.00 78.18  ? 243  PHE B CE2 1 
ATOM   1928  C CZ  . PHE A 1 260  ? 190.044 206.788 277.742 1.00 78.18  ? 243  PHE B CZ  1 
ATOM   1929  N N   . LYS A 1 261  ? 187.013 208.823 282.531 1.00 79.68  ? 244  LYS B N   1 
ATOM   1930  C CA  . LYS A 1 261  ? 185.578 208.665 282.716 1.00 79.68  ? 244  LYS B CA  1 
ATOM   1931  C C   . LYS A 1 261  ? 184.937 207.999 281.505 1.00 79.68  ? 244  LYS B C   1 
ATOM   1932  O O   . LYS A 1 261  ? 185.374 208.176 280.365 1.00 79.68  ? 244  LYS B O   1 
ATOM   1933  C CB  . LYS A 1 261  ? 184.918 210.020 282.972 1.00 79.68  ? 244  LYS B CB  1 
ATOM   1934  C CG  . LYS A 1 261  ? 185.147 211.043 281.875 1.00 79.68  ? 244  LYS B CG  1 
ATOM   1935  C CD  . LYS A 1 261  ? 184.314 212.295 282.099 1.00 79.68  ? 244  LYS B CD  1 
ATOM   1936  C CE  . LYS A 1 261  ? 184.419 212.783 283.534 1.00 79.68  ? 244  LYS B CE  1 
ATOM   1937  N NZ  . LYS A 1 261  ? 185.832 213.032 283.930 1.00 79.68  ? 244  LYS B NZ  1 
ATOM   1938  N N   . VAL A 1 262  ? 183.886 207.225 281.766 1.00 80.09  ? 245  VAL B N   1 
ATOM   1939  C CA  . VAL A 1 262  ? 183.141 206.511 280.742 1.00 80.09  ? 245  VAL B CA  1 
ATOM   1940  C C   . VAL A 1 262  ? 181.662 206.860 280.880 1.00 80.09  ? 245  VAL B C   1 
ATOM   1941  O O   . VAL A 1 262  ? 181.266 207.647 281.739 1.00 80.09  ? 245  VAL B O   1 
ATOM   1942  C CB  . VAL A 1 262  ? 183.354 204.985 280.817 1.00 80.09  ? 245  VAL B CB  1 
ATOM   1943  C CG1 . VAL A 1 262  ? 184.832 204.655 280.849 1.00 80.09  ? 245  VAL B CG1 1 
ATOM   1944  C CG2 . VAL A 1 262  ? 182.652 204.407 282.033 1.00 80.09  ? 245  VAL B CG2 1 
ATOM   1945  N N   . ASN A 1 263  ? 180.848 206.268 280.011 1.00 78.89  ? 246  ASN B N   1 
ATOM   1946  C CA  . ASN A 1 263  ? 179.401 206.416 280.056 1.00 78.89  ? 246  ASN B CA  1 
ATOM   1947  C C   . ASN A 1 263  ? 178.772 205.137 280.590 1.00 78.89  ? 246  ASN B C   1 
ATOM   1948  O O   . ASN A 1 263  ? 179.221 204.033 280.269 1.00 78.89  ? 246  ASN B O   1 
ATOM   1949  C CB  . ASN A 1 263  ? 178.838 206.735 278.672 1.00 78.89  ? 246  ASN B CB  1 
ATOM   1950  C CG  . ASN A 1 263  ? 179.475 207.960 278.055 1.00 78.89  ? 246  ASN B CG  1 
ATOM   1951  O OD1 . ASN A 1 263  ? 179.840 208.902 278.756 1.00 78.89  ? 246  ASN B OD1 1 
ATOM   1952  N ND2 . ASN A 1 263  ? 179.606 207.957 276.735 1.00 78.89  ? 246  ASN B ND2 1 
ATOM   1953  N N   . THR A 1 264  ? 177.732 205.290 281.411 1.00 79.23  ? 247  THR B N   1 
ATOM   1954  C CA  . THR A 1 264  ? 177.085 204.153 282.048 1.00 79.23  ? 247  THR B CA  1 
ATOM   1955  C C   . THR A 1 264  ? 175.573 204.114 281.862 1.00 79.23  ? 247  THR B C   1 
ATOM   1956  O O   . THR A 1 264  ? 174.925 203.224 282.422 1.00 79.23  ? 247  THR B O   1 
ATOM   1957  C CB  . THR A 1 264  ? 177.392 204.133 283.554 1.00 79.23  ? 247  THR B CB  1 
ATOM   1958  O OG1 . THR A 1 264  ? 176.743 205.242 284.187 1.00 79.23  ? 247  THR B OG1 1 
ATOM   1959  C CG2 . THR A 1 264  ? 178.888 204.221 283.802 1.00 79.23  ? 247  THR B CG2 1 
ATOM   1960  N N   . ASN A 1 265  ? 174.992 205.042 281.100 1.00 80.69  ? 248  ASN B N   1 
ATOM   1961  C CA  . ASN A 1 265  ? 173.537 205.113 281.010 1.00 80.69  ? 248  ASN B CA  1 
ATOM   1962  C C   . ASN A 1 265  ? 172.964 203.995 280.145 1.00 80.69  ? 248  ASN B C   1 
ATOM   1963  O O   . ASN A 1 265  ? 171.929 203.410 280.486 1.00 80.69  ? 248  ASN B O   1 
ATOM   1964  C CB  . ASN A 1 265  ? 173.114 206.483 280.478 1.00 80.69  ? 248  ASN B CB  1 
ATOM   1965  C CG  . ASN A 1 265  ? 173.789 206.838 279.167 1.00 80.69  ? 248  ASN B CG  1 
ATOM   1966  O OD1 . ASN A 1 265  ? 173.731 206.082 278.197 1.00 80.69  ? 248  ASN B OD1 1 
ATOM   1967  N ND2 . ASN A 1 265  ? 174.436 207.997 279.132 1.00 80.69  ? 248  ASN B ND2 1 
ATOM   1968  N N   . ALA A 1 266  ? 173.615 203.680 279.028 1.00 77.33  ? 249  ALA B N   1 
ATOM   1969  C CA  . ALA A 1 266  ? 173.057 202.725 278.084 1.00 77.33  ? 249  ALA B CA  1 
ATOM   1970  C C   . ALA A 1 266  ? 173.139 201.303 278.636 1.00 77.33  ? 249  ALA B C   1 
ATOM   1971  O O   . ALA A 1 266  ? 173.806 201.026 279.635 1.00 77.33  ? 249  ALA B O   1 
ATOM   1972  C CB  . ALA A 1 266  ? 173.777 202.816 276.742 1.00 77.33  ? 249  ALA B CB  1 
ATOM   1973  N N   . TYR A 1 267  ? 172.437 200.389 277.962 1.00 76.69  ? 250  TYR B N   1 
ATOM   1974  C CA  . TYR A 1 267  ? 172.361 199.005 278.412 1.00 76.69  ? 250  TYR B CA  1 
ATOM   1975  C C   . TYR A 1 267  ? 173.595 198.188 278.055 1.00 76.69  ? 250  TYR B C   1 
ATOM   1976  O O   . TYR A 1 267  ? 173.792 197.112 278.627 1.00 76.69  ? 250  TYR B O   1 
ATOM   1977  C CB  . TYR A 1 267  ? 171.117 198.329 277.828 1.00 76.69  ? 250  TYR B CB  1 
ATOM   1978  C CG  . TYR A 1 267  ? 171.221 198.012 276.353 1.00 76.69  ? 250  TYR B CG  1 
ATOM   1979  C CD1 . TYR A 1 267  ? 170.947 198.977 275.395 1.00 76.69  ? 250  TYR B CD1 1 
ATOM   1980  C CD2 . TYR A 1 267  ? 171.585 196.747 275.918 1.00 76.69  ? 250  TYR B CD2 1 
ATOM   1981  C CE1 . TYR A 1 267  ? 171.039 198.691 274.048 1.00 76.69  ? 250  TYR B CE1 1 
ATOM   1982  C CE2 . TYR A 1 267  ? 171.681 196.454 274.576 1.00 76.69  ? 250  TYR B CE2 1 
ATOM   1983  C CZ  . TYR A 1 267  ? 171.407 197.428 273.645 1.00 76.69  ? 250  TYR B CZ  1 
ATOM   1984  O OH  . TYR A 1 267  ? 171.501 197.137 272.305 1.00 76.69  ? 250  TYR B OH  1 
ATOM   1985  N N   . TYR A 1 268  ? 174.422 198.665 277.127 1.00 75.98  ? 251  TYR B N   1 
ATOM   1986  C CA  . TYR A 1 268  ? 175.595 197.934 276.669 1.00 75.98  ? 251  TYR B CA  1 
ATOM   1987  C C   . TYR A 1 268  ? 176.884 198.452 277.291 1.00 75.98  ? 251  TYR B C   1 
ATOM   1988  O O   . TYR A 1 268  ? 177.971 198.144 276.795 1.00 75.98  ? 251  TYR B O   1 
ATOM   1989  C CB  . TYR A 1 268  ? 175.690 197.995 275.144 1.00 75.98  ? 251  TYR B CB  1 
ATOM   1990  C CG  . TYR A 1 268  ? 175.749 199.402 274.598 1.00 75.98  ? 251  TYR B CG  1 
ATOM   1991  C CD1 . TYR A 1 268  ? 176.955 200.075 274.486 1.00 75.98  ? 251  TYR B CD1 1 
ATOM   1992  C CD2 . TYR A 1 268  ? 174.597 200.057 274.196 1.00 75.98  ? 251  TYR B CD2 1 
ATOM   1993  C CE1 . TYR A 1 268  ? 177.011 201.358 273.992 1.00 75.98  ? 251  TYR B CE1 1 
ATOM   1994  C CE2 . TYR A 1 268  ? 174.643 201.339 273.699 1.00 75.98  ? 251  TYR B CE2 1 
ATOM   1995  C CZ  . TYR A 1 268  ? 175.852 201.986 273.600 1.00 75.98  ? 251  TYR B CZ  1 
ATOM   1996  O OH  . TYR A 1 268  ? 175.901 203.267 273.105 1.00 75.98  ? 251  TYR B OH  1 
ATOM   1997  N N   . GLU A 1 269  ? 176.787 199.232 278.360 1.00 78.01  ? 252  GLU B N   1 
ATOM   1998  C CA  . GLU A 1 269  ? 177.933 199.919 278.931 1.00 78.01  ? 252  GLU B CA  1 
ATOM   1999  C C   . GLU A 1 269  ? 178.249 199.370 280.315 1.00 78.01  ? 252  GLU B C   1 
ATOM   2000  O O   . GLU A 1 269  ? 177.355 198.951 281.055 1.00 78.01  ? 252  GLU B O   1 
ATOM   2001  C CB  . GLU A 1 269  ? 177.669 201.422 279.012 1.00 78.01  ? 252  GLU B CB  1 
ATOM   2002  C CG  . GLU A 1 269  ? 177.557 202.084 277.653 1.00 78.01  ? 252  GLU B CG  1 
ATOM   2003  C CD  . GLU A 1 269  ? 177.113 203.527 277.739 1.00 78.01  ? 252  GLU B CD  1 
ATOM   2004  O OE1 . GLU A 1 269  ? 176.662 203.945 278.824 1.00 78.01  ? 252  GLU B OE1 1 
ATOM   2005  O OE2 . GLU A 1 269  ? 177.214 204.242 276.720 1.00 78.01  ? 252  GLU B OE2 1 
ATOM   2006  N N   . MET A 1 270  ? 179.537 199.365 280.650 1.00 78.38  ? 253  MET B N   1 
ATOM   2007  C CA  . MET A 1 270  ? 179.962 198.919 281.969 1.00 78.38  ? 253  MET B CA  1 
ATOM   2008  C C   . MET A 1 270  ? 179.379 199.826 283.043 1.00 78.38  ? 253  MET B C   1 
ATOM   2009  O O   . MET A 1 270  ? 179.396 201.053 282.916 1.00 78.38  ? 253  MET B O   1 
ATOM   2010  C CB  . MET A 1 270  ? 181.486 198.909 282.058 1.00 78.38  ? 253  MET B CB  1 
ATOM   2011  C CG  . MET A 1 270  ? 182.102 197.528 282.023 1.00 78.38  ? 253  MET B CG  1 
ATOM   2012  S SD  . MET A 1 270  ? 183.898 197.594 282.005 1.00 78.38  ? 253  MET B SD  1 
ATOM   2013  C CE  . MET A 1 270  ? 184.260 196.422 280.705 1.00 78.38  ? 253  MET B CE  1 
ATOM   2014  N N   . SER A 1 271  ? 178.857 199.213 284.107 1.00 82.83  ? 254  SER B N   1 
ATOM   2015  C CA  . SER A 1 271  ? 178.225 199.994 285.165 1.00 82.83  ? 254  SER B CA  1 
ATOM   2016  C C   . SER A 1 271  ? 179.232 200.909 285.848 1.00 82.83  ? 254  SER B C   1 
ATOM   2017  O O   . SER A 1 271  ? 178.911 202.053 286.188 1.00 82.83  ? 254  SER B O   1 
ATOM   2018  C CB  . SER A 1 271  ? 177.562 199.068 286.184 1.00 82.83  ? 254  SER B CB  1 
ATOM   2019  O OG  . SER A 1 271  ? 178.522 198.287 286.869 1.00 82.83  ? 254  SER B OG  1 
ATOM   2020  N N   . GLY A 1 272  ? 180.451 200.425 286.060 1.00 85.35  ? 255  GLY B N   1 
ATOM   2021  C CA  . GLY A 1 272  ? 181.480 201.240 286.669 1.00 85.35  ? 255  GLY B CA  1 
ATOM   2022  C C   . GLY A 1 272  ? 182.872 200.668 286.516 1.00 85.35  ? 255  GLY B C   1 
ATOM   2023  O O   . GLY A 1 272  ? 183.107 199.492 286.808 1.00 85.35  ? 255  GLY B O   1 
ATOM   2024  N N   . LEU A 1 273  ? 183.806 201.498 286.058 1.00 80.91  ? 256  LEU B N   1 
ATOM   2025  C CA  . LEU A 1 273  ? 185.202 201.090 285.919 1.00 80.91  ? 256  LEU B CA  1 
ATOM   2026  C C   . LEU A 1 273  ? 186.056 202.347 286.048 1.00 80.91  ? 256  LEU B C   1 
ATOM   2027  O O   . LEU A 1 273  ? 186.198 203.102 285.082 1.00 80.91  ? 256  LEU B O   1 
ATOM   2028  C CB  . LEU A 1 273  ? 185.447 200.384 284.593 1.00 80.91  ? 256  LEU B CB  1 
ATOM   2029  C CG  . LEU A 1 273  ? 186.898 199.989 284.308 1.00 80.91  ? 256  LEU B CG  1 
ATOM   2030  C CD1 . LEU A 1 273  ? 187.519 199.286 285.505 1.00 80.91  ? 256  LEU B CD1 1 
ATOM   2031  C CD2 . LEU A 1 273  ? 186.992 199.119 283.069 1.00 80.91  ? 256  LEU B CD2 1 
ATOM   2032  N N   . GLU A 1 274  ? 186.614 202.564 287.233 1.00 87.93  ? 257  GLU B N   1 
ATOM   2033  C CA  . GLU A 1 274  ? 187.530 203.673 287.452 1.00 87.93  ? 257  GLU B CA  1 
ATOM   2034  C C   . GLU A 1 274  ? 188.933 203.254 287.033 1.00 87.93  ? 257  GLU B C   1 
ATOM   2035  O O   . GLU A 1 274  ? 189.392 202.155 287.366 1.00 87.93  ? 257  GLU B O   1 
ATOM   2036  C CB  . GLU A 1 274  ? 187.494 204.129 288.914 1.00 87.93  ? 257  GLU B CB  1 
ATOM   2037  C CG  . GLU A 1 274  ? 188.445 203.406 289.859 1.00 87.93  ? 257  GLU B CG  1 
ATOM   2038  C CD  . GLU A 1 274  ? 188.677 204.161 291.152 1.00 87.93  ? 257  GLU B CD  1 
ATOM   2039  O OE1 . GLU A 1 274  ? 189.386 205.188 291.122 1.00 87.93  ? 257  GLU B OE1 1 
ATOM   2040  O OE2 . GLU A 1 274  ? 188.151 203.727 292.198 1.00 87.93  ? 257  GLU B OE2 1 
ATOM   2041  N N   . VAL A 1 275  ? 189.585 204.102 286.244 1.00 74.16  ? 258  VAL B N   1 
ATOM   2042  C CA  . VAL A 1 275  ? 190.972 203.880 285.856 1.00 74.16  ? 258  VAL B CA  1 
ATOM   2043  C C   . VAL A 1 275  ? 191.678 205.226 285.747 1.00 74.16  ? 258  VAL B C   1 
ATOM   2044  O O   . VAL A 1 275  ? 191.441 206.001 284.815 1.00 74.16  ? 258  VAL B O   1 
ATOM   2045  C CB  . VAL A 1 275  ? 191.064 203.054 284.558 1.00 74.16  ? 258  VAL B CB  1 
ATOM   2046  C CG1 . VAL A 1 275  ? 190.219 203.657 283.452 1.00 74.16  ? 258  VAL B CG1 1 
ATOM   2047  C CG2 . VAL A 1 275  ? 192.505 202.939 284.112 1.00 74.16  ? 258  VAL B CG2 1 
ATOM   2048  N N   . SER A 1 276  ? 192.543 205.516 286.711 1.00 75.69  ? 259  SER B N   1 
ATOM   2049  C CA  . SER A 1 276  ? 193.178 206.819 286.767 1.00 75.69  ? 259  SER B CA  1 
ATOM   2050  C C   . SER A 1 276  ? 194.216 206.952 285.658 1.00 75.69  ? 259  SER B C   1 
ATOM   2051  O O   . SER A 1 276  ? 194.615 205.977 285.017 1.00 75.69  ? 259  SER B O   1 
ATOM   2052  C CB  . SER A 1 276  ? 193.827 207.042 288.130 1.00 75.69  ? 259  SER B CB  1 
ATOM   2053  O OG  . SER A 1 276  ? 194.852 208.015 288.048 1.00 75.69  ? 259  SER B OG  1 
ATOM   2054  N N   . PHE A 1 277  ? 194.647 208.191 285.424 1.00 72.95  ? 260  PHE B N   1 
ATOM   2055  C CA  . PHE A 1 277  ? 195.700 208.422 284.444 1.00 72.95  ? 260  PHE B CA  1 
ATOM   2056  C C   . PHE A 1 277  ? 197.014 207.802 284.892 1.00 72.95  ? 260  PHE B C   1 
ATOM   2057  O O   . PHE A 1 277  ? 197.853 207.455 284.053 1.00 72.95  ? 260  PHE B O   1 
ATOM   2058  C CB  . PHE A 1 277  ? 195.872 209.919 284.199 1.00 72.95  ? 260  PHE B CB  1 
ATOM   2059  C CG  . PHE A 1 277  ? 194.937 210.477 283.165 1.00 72.95  ? 260  PHE B CG  1 
ATOM   2060  C CD1 . PHE A 1 277  ? 193.611 210.088 283.126 1.00 72.95  ? 260  PHE B CD1 1 
ATOM   2061  C CD2 . PHE A 1 277  ? 195.382 211.399 282.238 1.00 72.95  ? 260  PHE B CD2 1 
ATOM   2062  C CE1 . PHE A 1 277  ? 192.751 210.601 282.179 1.00 72.95  ? 260  PHE B CE1 1 
ATOM   2063  C CE2 . PHE A 1 277  ? 194.524 211.915 281.290 1.00 72.95  ? 260  PHE B CE2 1 
ATOM   2064  C CZ  . PHE A 1 277  ? 193.209 211.516 281.262 1.00 72.95  ? 260  PHE B CZ  1 
ATOM   2065  N N   . GLU A 1 278  ? 197.211 207.657 286.204 1.00 70.94  ? 261  GLU B N   1 
ATOM   2066  C CA  . GLU A 1 278  ? 198.427 207.029 286.707 1.00 70.94  ? 261  GLU B CA  1 
ATOM   2067  C C   . GLU A 1 278  ? 198.520 205.574 286.269 1.00 70.94  ? 261  GLU B C   1 
ATOM   2068  O O   . GLU A 1 278  ? 199.593 205.105 285.872 1.00 70.94  ? 261  GLU B O   1 
ATOM   2069  C CB  . GLU A 1 278  ? 198.476 207.134 288.229 1.00 70.94  ? 261  GLU B CB  1 
ATOM   2070  C CG  . GLU A 1 278  ? 199.606 206.353 288.857 1.00 70.94  ? 261  GLU B CG  1 
ATOM   2071  C CD  . GLU A 1 278  ? 200.943 207.025 288.665 1.00 70.94  ? 261  GLU B CD  1 
ATOM   2072  O OE1 . GLU A 1 278  ? 201.065 208.210 289.031 1.00 70.94  ? 261  GLU B OE1 1 
ATOM   2073  O OE2 . GLU A 1 278  ? 201.872 206.371 288.147 1.00 70.94  ? 261  GLU B OE2 1 
ATOM   2074  N N   . GLU A 1 279  ? 197.408 204.841 286.337 1.00 69.60  ? 262  GLU B N   1 
ATOM   2075  C CA  . GLU A 1 279  ? 197.419 203.455 285.884 1.00 69.60  ? 262  GLU B CA  1 
ATOM   2076  C C   . GLU A 1 279  ? 197.675 203.373 284.386 1.00 69.60  ? 262  GLU B C   1 
ATOM   2077  O O   . GLU A 1 279  ? 198.367 202.462 283.916 1.00 69.60  ? 262  GLU B O   1 
ATOM   2078  C CB  . GLU A 1 279  ? 196.103 202.771 286.244 1.00 69.60  ? 262  GLU B CB  1 
ATOM   2079  C CG  . GLU A 1 279  ? 196.273 201.357 286.764 1.00 69.60  ? 262  GLU B CG  1 
ATOM   2080  C CD  . GLU A 1 279  ? 196.833 201.321 288.172 1.00 69.60  ? 262  GLU B CD  1 
ATOM   2081  O OE1 . GLU A 1 279  ? 196.411 202.158 288.996 1.00 69.60  ? 262  GLU B OE1 1 
ATOM   2082  O OE2 . GLU A 1 279  ? 197.691 200.456 288.457 1.00 69.60  ? 262  GLU B OE2 1 
ATOM   2083  N N   . LEU A 1 280  ? 197.125 204.314 283.618 1.00 69.70  ? 263  LEU B N   1 
ATOM   2084  C CA  . LEU A 1 280  ? 197.377 204.328 282.182 1.00 69.70  ? 263  LEU B CA  1 
ATOM   2085  C C   . LEU A 1 280  ? 198.847 204.592 281.883 1.00 69.70  ? 263  LEU B C   1 
ATOM   2086  O O   . LEU A 1 280  ? 199.425 203.968 280.987 1.00 69.70  ? 263  LEU B O   1 
ATOM   2087  C CB  . LEU A 1 280  ? 196.490 205.370 281.504 1.00 69.70  ? 263  LEU B CB  1 
ATOM   2088  C CG  . LEU A 1 280  ? 195.019 204.981 281.364 1.00 69.70  ? 263  LEU B CG  1 
ATOM   2089  C CD1 . LEU A 1 280  ? 194.254 206.053 280.617 1.00 69.70  ? 263  LEU B CD1 1 
ATOM   2090  C CD2 . LEU A 1 280  ? 194.888 203.643 280.665 1.00 69.70  ? 263  LEU B CD2 1 
ATOM   2091  N N   . ARG A 1 281  ? 199.468 205.516 282.619 1.00 69.60  ? 264  ARG B N   1 
ATOM   2092  C CA  . ARG A 1 281  ? 200.899 205.749 282.445 1.00 69.60  ? 264  ARG B CA  1 
ATOM   2093  C C   . ARG A 1 281  ? 201.704 204.511 282.805 1.00 69.60  ? 264  ARG B C   1 
ATOM   2094  O O   . ARG A 1 281  ? 202.645 204.143 282.092 1.00 69.60  ? 264  ARG B O   1 
ATOM   2095  C CB  . ARG A 1 281  ? 201.353 206.929 283.301 1.00 69.60  ? 264  ARG B CB  1 
ATOM   2096  C CG  . ARG A 1 281  ? 201.104 208.283 282.688 1.00 69.60  ? 264  ARG B CG  1 
ATOM   2097  C CD  . ARG A 1 281  ? 202.190 209.261 283.089 1.00 69.60  ? 264  ARG B CD  1 
ATOM   2098  N NE  . ARG A 1 281  ? 202.629 209.059 284.464 1.00 69.60  ? 264  ARG B NE  1 
ATOM   2099  C CZ  . ARG A 1 281  ? 203.349 209.931 285.154 1.00 69.60  ? 264  ARG B CZ  1 
ATOM   2100  N NH1 . ARG A 1 281  ? 203.728 211.083 284.629 1.00 69.60  ? 264  ARG B NH1 1 
ATOM   2101  N NH2 . ARG A 1 281  ? 203.689 209.644 286.406 1.00 69.60  ? 264  ARG B NH2 1 
ATOM   2102  N N   . THR A 1 282  ? 201.352 203.857 283.913 1.00 69.60  ? 265  THR B N   1 
ATOM   2103  C CA  . THR A 1 282  ? 202.125 202.712 284.376 1.00 69.60  ? 265  THR B CA  1 
ATOM   2104  C C   . THR A 1 282  ? 202.015 201.537 283.415 1.00 69.60  ? 265  THR B C   1 
ATOM   2105  O O   . THR A 1 282  ? 203.009 200.854 283.148 1.00 69.60  ? 265  THR B O   1 
ATOM   2106  C CB  . THR A 1 282  ? 201.665 202.306 285.771 1.00 69.60  ? 265  THR B CB  1 
ATOM   2107  O OG1 . THR A 1 282  ? 201.917 203.379 286.684 1.00 69.60  ? 265  THR B OG1 1 
ATOM   2108  C CG2 . THR A 1 282  ? 202.413 201.079 286.234 1.00 69.60  ? 265  THR B CG2 1 
ATOM   2109  N N   . PHE A 1 283  ? 200.818 201.284 282.884 1.00 69.60  ? 266  PHE B N   1 
ATOM   2110  C CA  . PHE A 1 283  ? 200.637 200.147 281.987 1.00 69.60  ? 266  PHE B CA  1 
ATOM   2111  C C   . PHE A 1 283  ? 201.481 200.300 280.729 1.00 69.60  ? 266  PHE B C   1 
ATOM   2112  O O   . PHE A 1 283  ? 202.147 199.354 280.296 1.00 69.60  ? 266  PHE B O   1 
ATOM   2113  C CB  . PHE A 1 283  ? 199.161 199.990 281.628 1.00 69.60  ? 266  PHE B CB  1 
ATOM   2114  C CG  . PHE A 1 283  ? 198.378 199.187 282.621 1.00 69.60  ? 266  PHE B CG  1 
ATOM   2115  C CD1 . PHE A 1 283  ? 198.822 197.943 283.025 1.00 69.60  ? 266  PHE B CD1 1 
ATOM   2116  C CD2 . PHE A 1 283  ? 197.196 199.673 283.147 1.00 69.60  ? 266  PHE B CD2 1 
ATOM   2117  C CE1 . PHE A 1 283  ? 198.105 197.201 283.938 1.00 69.60  ? 266  PHE B CE1 1 
ATOM   2118  C CE2 . PHE A 1 283  ? 196.474 198.936 284.060 1.00 69.60  ? 266  PHE B CE2 1 
ATOM   2119  C CZ  . PHE A 1 283  ? 196.929 197.698 284.456 1.00 69.60  ? 266  PHE B CZ  1 
ATOM   2120  N N   . GLY A 1 284  ? 201.467 201.483 280.131 1.00 72.60  ? 267  GLY B N   1 
ATOM   2121  C CA  . GLY A 1 284  ? 202.255 201.717 278.941 1.00 72.60  ? 267  GLY B CA  1 
ATOM   2122  C C   . GLY A 1 284  ? 201.768 200.900 277.755 1.00 72.60  ? 267  GLY B C   1 
ATOM   2123  O O   . GLY A 1 284  ? 200.727 200.246 277.786 1.00 72.60  ? 267  GLY B O   1 
ATOM   2124  N N   . GLY A 1 285  ? 202.566 200.942 276.697 1.00 75.79  ? 268  GLY B N   1 
ATOM   2125  C CA  . GLY A 1 285  ? 202.246 200.177 275.504 1.00 75.79  ? 268  GLY B CA  1 
ATOM   2126  C C   . GLY A 1 285  ? 200.944 200.643 274.886 1.00 75.79  ? 268  GLY B C   1 
ATOM   2127  O O   . GLY A 1 285  ? 200.767 201.826 274.572 1.00 75.79  ? 268  GLY B O   1 
ATOM   2128  N N   . HIS A 1 286  ? 200.017 199.702 274.697 1.00 79.54  ? 269  HIS B N   1 
ATOM   2129  C CA  . HIS A 1 286  ? 198.725 200.038 274.108 1.00 79.54  ? 269  HIS B CA  1 
ATOM   2130  C C   . HIS A 1 286  ? 197.926 200.963 275.016 1.00 79.54  ? 269  HIS B C   1 
ATOM   2131  O O   . HIS A 1 286  ? 197.233 201.868 274.538 1.00 79.54  ? 269  HIS B O   1 
ATOM   2132  C CB  . HIS A 1 286  ? 197.941 198.758 273.816 1.00 79.54  ? 269  HIS B CB  1 
ATOM   2133  C CG  . HIS A 1 286  ? 196.539 198.994 273.345 1.00 79.54  ? 269  HIS B CG  1 
ATOM   2134  N ND1 . HIS A 1 286  ? 195.520 199.370 274.194 1.00 79.54  ? 269  HIS B ND1 1 
ATOM   2135  C CD2 . HIS A 1 286  ? 195.985 198.895 272.114 1.00 79.54  ? 269  HIS B CD2 1 
ATOM   2136  C CE1 . HIS A 1 286  ? 194.401 199.499 273.505 1.00 79.54  ? 269  HIS B CE1 1 
ATOM   2137  N NE2 . HIS A 1 286  ? 194.655 199.216 272.240 1.00 79.54  ? 269  HIS B NE2 1 
ATOM   2138  N N   . ASP A 1 287  ? 198.004 200.744 276.330 1.00 78.76  ? 270  ASP B N   1 
ATOM   2139  C CA  . ASP A 1 287  ? 197.201 201.523 277.268 1.00 78.76  ? 270  ASP B CA  1 
ATOM   2140  C C   . ASP A 1 287  ? 197.587 202.996 277.252 1.00 78.76  ? 270  ASP B C   1 
ATOM   2141  O O   . ASP A 1 287  ? 196.716 203.872 277.266 1.00 78.76  ? 270  ASP B O   1 
ATOM   2142  C CB  . ASP A 1 287  ? 197.357 200.952 278.673 1.00 78.76  ? 270  ASP B CB  1 
ATOM   2143  C CG  . ASP A 1 287  ? 196.306 199.921 279.001 1.00 78.76  ? 270  ASP B CG  1 
ATOM   2144  O OD1 . ASP A 1 287  ? 195.598 199.477 278.073 1.00 78.76  ? 270  ASP B OD1 1 
ATOM   2145  O OD2 . ASP A 1 287  ? 196.197 199.543 280.185 1.00 78.76  ? 270  ASP B OD2 1 
ATOM   2146  N N   . ALA A 1 288  ? 198.888 203.288 277.218 1.00 76.33  ? 271  ALA B N   1 
ATOM   2147  C CA  . ALA A 1 288  ? 199.352 204.666 277.320 1.00 76.33  ? 271  ALA B CA  1 
ATOM   2148  C C   . ALA A 1 288  ? 198.886 205.527 276.156 1.00 76.33  ? 271  ALA B C   1 
ATOM   2149  O O   . ALA A 1 288  ? 198.901 206.756 276.267 1.00 76.33  ? 271  ALA B O   1 
ATOM   2150  C CB  . ALA A 1 288  ? 200.876 204.703 277.410 1.00 76.33  ? 271  ALA B CB  1 
ATOM   2151  N N   . LYS A 1 289  ? 198.479 204.916 275.044 1.00 77.36  ? 272  LYS B N   1 
ATOM   2152  C CA  . LYS A 1 289  ? 197.965 205.684 273.919 1.00 77.36  ? 272  LYS B CA  1 
ATOM   2153  C C   . LYS A 1 289  ? 196.562 206.219 274.165 1.00 77.36  ? 272  LYS B C   1 
ATOM   2154  O O   . LYS A 1 289  ? 196.078 207.025 273.365 1.00 77.36  ? 272  LYS B O   1 
ATOM   2155  C CB  . LYS A 1 289  ? 197.981 204.829 272.653 1.00 77.36  ? 272  LYS B CB  1 
ATOM   2156  C CG  . LYS A 1 289  ? 199.312 204.148 272.399 1.00 77.36  ? 272  LYS B CG  1 
ATOM   2157  C CD  . LYS A 1 289  ? 199.310 203.383 271.090 1.00 77.36  ? 272  LYS B CD  1 
ATOM   2158  C CE  . LYS A 1 289  ? 200.481 202.418 271.024 1.00 77.36  ? 272  LYS B CE  1 
ATOM   2159  N NZ  . LYS A 1 289  ? 201.785 203.118 271.187 1.00 77.36  ? 272  LYS B NZ  1 
ATOM   2160  N N   . PHE A 1 290  ? 195.902 205.798 275.244 1.00 74.73  ? 273  PHE B N   1 
ATOM   2161  C CA  . PHE A 1 290  ? 194.550 206.263 275.525 1.00 74.73  ? 273  PHE B CA  1 
ATOM   2162  C C   . PHE A 1 290  ? 194.505 207.708 275.996 1.00 74.73  ? 273  PHE B C   1 
ATOM   2163  O O   . PHE A 1 290  ? 193.414 208.280 276.069 1.00 74.73  ? 273  PHE B O   1 
ATOM   2164  C CB  . PHE A 1 290  ? 193.892 205.370 276.573 1.00 74.73  ? 273  PHE B CB  1 
ATOM   2165  C CG  . PHE A 1 290  ? 193.276 204.127 276.009 1.00 74.73  ? 273  PHE B CG  1 
ATOM   2166  C CD1 . PHE A 1 290  ? 193.585 203.705 274.733 1.00 74.73  ? 273  PHE B CD1 1 
ATOM   2167  C CD2 . PHE A 1 290  ? 192.388 203.382 276.759 1.00 74.73  ? 273  PHE B CD2 1 
ATOM   2168  C CE1 . PHE A 1 290  ? 193.021 202.564 274.216 1.00 74.73  ? 273  PHE B CE1 1 
ATOM   2169  C CE2 . PHE A 1 290  ? 191.822 202.240 276.247 1.00 74.73  ? 273  PHE B CE2 1 
ATOM   2170  C CZ  . PHE A 1 290  ? 192.139 201.830 274.973 1.00 74.73  ? 273  PHE B CZ  1 
ATOM   2171  N N   . ILE A 1 291  ? 195.646 208.308 276.322 1.00 78.44  ? 274  ILE B N   1 
ATOM   2172  C CA  . ILE A 1 291  ? 195.715 209.706 276.727 1.00 78.44  ? 274  ILE B CA  1 
ATOM   2173  C C   . ILE A 1 291  ? 196.351 210.500 275.594 1.00 78.44  ? 274  ILE B C   1 
ATOM   2174  O O   . ILE A 1 291  ? 197.429 210.146 275.103 1.00 78.44  ? 274  ILE B O   1 
ATOM   2175  C CB  . ILE A 1 291  ? 196.483 209.877 278.050 1.00 78.44  ? 274  ILE B CB  1 
ATOM   2176  C CG1 . ILE A 1 291  ? 197.883 209.273 277.967 1.00 78.44  ? 274  ILE B CG1 1 
ATOM   2177  C CG2 . ILE A 1 291  ? 195.717 209.233 279.188 1.00 78.44  ? 274  ILE B CG2 1 
ATOM   2178  C CD1 . ILE A 1 291  ? 198.629 209.297 279.280 1.00 78.44  ? 274  ILE B CD1 1 
ATOM   2179  N N   . ASP A 1 292  ? 195.670 211.560 275.166 1.00 85.20  ? 275  ASP B N   1 
ATOM   2180  C CA  . ASP A 1 292  ? 196.117 212.335 274.022 1.00 85.20  ? 275  ASP B CA  1 
ATOM   2181  C C   . ASP A 1 292  ? 197.396 213.099 274.356 1.00 85.20  ? 275  ASP B C   1 
ATOM   2182  O O   . ASP A 1 292  ? 197.835 213.169 275.507 1.00 85.20  ? 275  ASP B O   1 
ATOM   2183  C CB  . ASP A 1 292  ? 195.023 213.299 273.572 1.00 85.20  ? 275  ASP B CB  1 
ATOM   2184  C CG  . ASP A 1 292  ? 194.431 214.074 274.724 1.00 85.20  ? 275  ASP B CG  1 
ATOM   2185  O OD1 . ASP A 1 292  ? 194.685 213.689 275.883 1.00 85.20  ? 275  ASP B OD1 1 
ATOM   2186  O OD2 . ASP A 1 292  ? 193.713 215.064 274.473 1.00 85.20  ? 275  ASP B OD2 1 
ATOM   2187  N N   . SER A 1 293  ? 198.000 213.679 273.318 1.00 84.29  ? 276  SER B N   1 
ATOM   2188  C CA  . SER A 1 293  ? 199.285 214.345 273.490 1.00 84.29  ? 276  SER B CA  1 
ATOM   2189  C C   . SER A 1 293  ? 199.154 215.662 274.244 1.00 84.29  ? 276  SER B C   1 
ATOM   2190  O O   . SER A 1 293  ? 200.114 216.100 274.887 1.00 84.29  ? 276  SER B O   1 
ATOM   2191  C CB  . SER A 1 293  ? 199.940 214.577 272.131 1.00 84.29  ? 276  SER B CB  1 
ATOM   2192  O OG  . SER A 1 293  ? 201.324 214.841 272.276 1.00 84.29  ? 276  SER B OG  1 
ATOM   2193  N N   . LEU A 1 294  ? 197.990 216.313 274.173 1.00 84.30  ? 277  LEU B N   1 
ATOM   2194  C CA  . LEU A 1 294  ? 197.820 217.585 274.868 1.00 84.30  ? 277  LEU B CA  1 
ATOM   2195  C C   . LEU A 1 294  ? 197.936 217.412 276.378 1.00 84.30  ? 277  LEU B C   1 
ATOM   2196  O O   . LEU A 1 294  ? 198.579 218.222 277.058 1.00 84.30  ? 277  LEU B O   1 
ATOM   2197  C CB  . LEU A 1 294  ? 196.475 218.208 274.504 1.00 84.30  ? 277  LEU B CB  1 
ATOM   2198  C CG  . LEU A 1 294  ? 196.055 219.403 275.359 1.00 84.30  ? 277  LEU B CG  1 
ATOM   2199  C CD1 . LEU A 1 294  ? 197.038 220.546 275.189 1.00 84.30  ? 277  LEU B CD1 1 
ATOM   2200  C CD2 . LEU A 1 294  ? 194.648 219.848 275.010 1.00 84.30  ? 277  LEU B CD2 1 
ATOM   2201  N N   . GLN A 1 295  ? 197.323 216.361 276.922 1.00 82.98  ? 278  GLN B N   1 
ATOM   2202  C CA  . GLN A 1 295  ? 197.400 216.134 278.360 1.00 82.98  ? 278  GLN B CA  1 
ATOM   2203  C C   . GLN A 1 295  ? 198.807 215.729 278.780 1.00 82.98  ? 278  GLN B C   1 
ATOM   2204  O O   . GLN A 1 295  ? 199.270 216.108 279.862 1.00 82.98  ? 278  GLN B O   1 
ATOM   2205  C CB  . GLN A 1 295  ? 196.372 215.086 278.774 1.00 82.98  ? 278  GLN B CB  1 
ATOM   2206  C CG  . GLN A 1 295  ? 194.948 215.516 278.472 1.00 82.98  ? 278  GLN B CG  1 
ATOM   2207  C CD  . GLN A 1 295  ? 193.920 214.495 278.898 1.00 82.98  ? 278  GLN B CD  1 
ATOM   2208  O OE1 . GLN A 1 295  ? 193.389 214.559 280.006 1.00 82.98  ? 278  GLN B OE1 1 
ATOM   2209  N NE2 . GLN A 1 295  ? 193.633 213.544 278.019 1.00 82.98  ? 278  GLN B NE2 1 
ATOM   2210  N N   . GLU A 1 296  ? 199.507 214.968 277.936 1.00 80.69  ? 279  GLU B N   1 
ATOM   2211  C CA  . GLU A 1 296  ? 200.905 214.665 278.218 1.00 80.69  ? 279  GLU B CA  1 
ATOM   2212  C C   . GLU A 1 296  ? 201.737 215.938 278.267 1.00 80.69  ? 279  GLU B C   1 
ATOM   2213  O O   . GLU A 1 296  ? 202.589 216.098 279.147 1.00 80.69  ? 279  GLU B O   1 
ATOM   2214  C CB  . GLU A 1 296  ? 201.466 213.707 277.169 1.00 80.69  ? 279  GLU B CB  1 
ATOM   2215  C CG  . GLU A 1 296  ? 200.762 212.368 277.103 1.00 80.69  ? 279  GLU B CG  1 
ATOM   2216  C CD  . GLU A 1 296  ? 201.462 211.394 276.177 1.00 80.69  ? 279  GLU B CD  1 
ATOM   2217  O OE1 . GLU A 1 296  ? 202.698 211.495 276.031 1.00 80.69  ? 279  GLU B OE1 1 
ATOM   2218  O OE2 . GLU A 1 296  ? 200.779 210.526 275.595 1.00 80.69  ? 279  GLU B OE2 1 
ATOM   2219  N N   . ASN A 1 297  ? 201.501 216.856 277.328 1.00 82.13  ? 280  ASN B N   1 
ATOM   2220  C CA  . ASN A 1 297  ? 202.217 218.126 277.334 1.00 82.13  ? 280  ASN B CA  1 
ATOM   2221  C C   . ASN A 1 297  ? 201.911 218.924 278.593 1.00 82.13  ? 280  ASN B C   1 
ATOM   2222  O O   . ASN A 1 297  ? 202.812 219.520 279.197 1.00 82.13  ? 280  ASN B O   1 
ATOM   2223  C CB  . ASN A 1 297  ? 201.854 218.933 276.090 1.00 82.13  ? 280  ASN B CB  1 
ATOM   2224  C CG  . ASN A 1 297  ? 203.068 219.416 275.336 1.00 82.13  ? 280  ASN B CG  1 
ATOM   2225  O OD1 . ASN A 1 297  ? 204.005 219.952 275.926 1.00 82.13  ? 280  ASN B OD1 1 
ATOM   2226  N ND2 . ASN A 1 297  ? 203.063 219.227 274.022 1.00 82.13  ? 280  ASN B ND2 1 
ATOM   2227  N N   . GLU A 1 298  ? 200.641 218.949 279.001 1.00 82.15  ? 281  GLU B N   1 
ATOM   2228  C CA  . GLU A 1 298  ? 200.266 219.676 280.209 1.00 82.15  ? 281  GLU B CA  1 
ATOM   2229  C C   . GLU A 1 298  ? 200.955 219.094 281.437 1.00 82.15  ? 281  GLU B C   1 
ATOM   2230  O O   . GLU A 1 298  ? 201.486 219.837 282.273 1.00 82.15  ? 281  GLU B O   1 
ATOM   2231  C CB  . GLU A 1 298  ? 198.746 219.657 280.375 1.00 82.15  ? 281  GLU B CB  1 
ATOM   2232  C CG  . GLU A 1 298  ? 198.265 219.572 281.813 1.00 82.15  ? 281  GLU B CG  1 
ATOM   2233  C CD  . GLU A 1 298  ? 196.788 219.238 281.911 1.00 82.15  ? 281  GLU B CD  1 
ATOM   2234  O OE1 . GLU A 1 298  ? 196.042 219.546 280.958 1.00 82.15  ? 281  GLU B OE1 1 
ATOM   2235  O OE2 . GLU A 1 298  ? 196.372 218.665 282.941 1.00 82.15  ? 281  GLU B OE2 1 
ATOM   2236  N N   . PHE A 1 299  ? 200.974 217.764 281.553 1.00 75.66  ? 282  PHE B N   1 
ATOM   2237  C CA  . PHE A 1 299  ? 201.636 217.131 282.689 1.00 75.66  ? 282  PHE B CA  1 
ATOM   2238  C C   . PHE A 1 299  ? 203.134 217.400 282.677 1.00 75.66  ? 282  PHE B C   1 
ATOM   2239  O O   . PHE A 1 299  ? 203.732 217.674 283.725 1.00 75.66  ? 282  PHE B O   1 
ATOM   2240  C CB  . PHE A 1 299  ? 201.366 215.627 282.687 1.00 75.66  ? 282  PHE B CB  1 
ATOM   2241  C CG  . PHE A 1 299  ? 199.967 215.266 283.084 1.00 75.66  ? 282  PHE B CG  1 
ATOM   2242  C CD1 . PHE A 1 299  ? 199.258 216.062 283.964 1.00 75.66  ? 282  PHE B CD1 1 
ATOM   2243  C CD2 . PHE A 1 299  ? 199.363 214.130 282.578 1.00 75.66  ? 282  PHE B CD2 1 
ATOM   2244  C CE1 . PHE A 1 299  ? 197.972 215.733 284.330 1.00 75.66  ? 282  PHE B CE1 1 
ATOM   2245  C CE2 . PHE A 1 299  ? 198.077 213.796 282.941 1.00 75.66  ? 282  PHE B CE2 1 
ATOM   2246  C CZ  . PHE A 1 299  ? 197.381 214.599 283.818 1.00 75.66  ? 282  PHE B CZ  1 
ATOM   2247  N N   . ARG A 1 300  ? 203.760 217.316 281.503 1.00 72.93  ? 283  ARG B N   1 
ATOM   2248  C CA  . ARG A 1 300  ? 205.195 217.554 281.417 1.00 72.93  ? 283  ARG B CA  1 
ATOM   2249  C C   . ARG A 1 300  ? 205.537 218.980 281.821 1.00 72.93  ? 283  ARG B C   1 
ATOM   2250  O O   . ARG A 1 300  ? 206.503 219.207 282.556 1.00 72.93  ? 283  ARG B O   1 
ATOM   2251  C CB  . ARG A 1 300  ? 205.690 217.256 280.005 1.00 72.93  ? 283  ARG B CB  1 
ATOM   2252  C CG  . ARG A 1 300  ? 207.143 217.607 279.765 1.00 72.93  ? 283  ARG B CG  1 
ATOM   2253  C CD  . ARG A 1 300  ? 207.450 217.653 278.280 1.00 72.93  ? 283  ARG B CD  1 
ATOM   2254  N NE  . ARG A 1 300  ? 206.678 216.664 277.538 1.00 72.93  ? 283  ARG B NE  1 
ATOM   2255  C CZ  . ARG A 1 300  ? 206.987 215.378 277.454 1.00 72.93  ? 283  ARG B CZ  1 
ATOM   2256  N NH1 . ARG A 1 300  ? 208.060 214.884 278.049 1.00 72.93  ? 283  ARG B NH1 1 
ATOM   2257  N NH2 . ARG A 1 300  ? 206.200 214.566 276.754 1.00 72.93  ? 283  ARG B NH2 1 
ATOM   2258  N N   . LEU A 1 301  ? 204.747 219.954 281.365 1.00 73.59  ? 284  LEU B N   1 
ATOM   2259  C CA  . LEU A 1 301  ? 204.988 221.340 281.757 1.00 73.59  ? 284  LEU B CA  1 
ATOM   2260  C C   . LEU A 1 301  ? 204.779 221.537 283.253 1.00 73.59  ? 284  LEU B C   1 
ATOM   2261  O O   . LEU A 1 301  ? 205.561 222.237 283.910 1.00 73.59  ? 284  LEU B O   1 
ATOM   2262  C CB  . LEU A 1 301  ? 204.080 222.275 280.962 1.00 73.59  ? 284  LEU B CB  1 
ATOM   2263  C CG  . LEU A 1 301  ? 204.726 222.928 279.742 1.00 73.59  ? 284  LEU B CG  1 
ATOM   2264  C CD1 . LEU A 1 301  ? 203.686 223.674 278.930 1.00 73.59  ? 284  LEU B CD1 1 
ATOM   2265  C CD2 . LEU A 1 301  ? 205.844 223.859 280.170 1.00 73.59  ? 284  LEU B CD2 1 
ATOM   2266  N N   . TYR A 1 302  ? 203.733 220.922 283.812 1.00 73.34  ? 285  TYR B N   1 
ATOM   2267  C CA  . TYR A 1 302  ? 203.466 221.061 285.240 1.00 73.34  ? 285  TYR B CA  1 
ATOM   2268  C C   . TYR A 1 302  ? 204.619 220.509 286.070 1.00 73.34  ? 285  TYR B C   1 
ATOM   2269  O O   . TYR A 1 302  ? 205.086 221.152 287.020 1.00 73.34  ? 285  TYR B O   1 
ATOM   2270  C CB  . TYR A 1 302  ? 202.156 220.354 285.585 1.00 73.34  ? 285  TYR B CB  1 
ATOM   2271  C CG  . TYR A 1 302  ? 201.711 220.522 287.017 1.00 73.34  ? 285  TYR B CG  1 
ATOM   2272  C CD1 . TYR A 1 302  ? 201.149 221.712 287.452 1.00 73.34  ? 285  TYR B CD1 1 
ATOM   2273  C CD2 . TYR A 1 302  ? 201.832 219.485 287.927 1.00 73.34  ? 285  TYR B CD2 1 
ATOM   2274  C CE1 . TYR A 1 302  ? 200.734 221.868 288.757 1.00 73.34  ? 285  TYR B CE1 1 
ATOM   2275  C CE2 . TYR A 1 302  ? 201.419 219.632 289.233 1.00 73.34  ? 285  TYR B CE2 1 
ATOM   2276  C CZ  . TYR A 1 302  ? 200.871 220.826 289.642 1.00 73.34  ? 285  TYR B CZ  1 
ATOM   2277  O OH  . TYR A 1 302  ? 200.458 220.978 290.944 1.00 73.34  ? 285  TYR B OH  1 
ATOM   2278  N N   . TYR A 1 303  ? 205.116 219.328 285.707 1.00 69.60  ? 286  TYR B N   1 
ATOM   2279  C CA  . TYR A 1 303  ? 206.186 218.733 286.496 1.00 69.60  ? 286  TYR B CA  1 
ATOM   2280  C C   . TYR A 1 303  ? 207.522 219.421 286.247 1.00 69.60  ? 286  TYR B C   1 
ATOM   2281  O O   . TYR A 1 303  ? 208.363 219.471 287.150 1.00 69.60  ? 286  TYR B O   1 
ATOM   2282  C CB  . TYR A 1 303  ? 206.267 217.235 286.219 1.00 69.60  ? 286  TYR B CB  1 
ATOM   2283  C CG  . TYR A 1 303  ? 205.052 216.503 286.733 1.00 69.60  ? 286  TYR B CG  1 
ATOM   2284  C CD1 . TYR A 1 303  ? 204.567 216.744 288.009 1.00 69.60  ? 286  TYR B CD1 1 
ATOM   2285  C CD2 . TYR A 1 303  ? 204.375 215.592 285.939 1.00 69.60  ? 286  TYR B CD2 1 
ATOM   2286  C CE1 . TYR A 1 303  ? 203.450 216.091 288.482 1.00 69.60  ? 286  TYR B CE1 1 
ATOM   2287  C CE2 . TYR A 1 303  ? 203.257 214.933 286.404 1.00 69.60  ? 286  TYR B CE2 1 
ATOM   2288  C CZ  . TYR A 1 303  ? 202.800 215.187 287.676 1.00 69.60  ? 286  TYR B CZ  1 
ATOM   2289  O OH  . TYR A 1 303  ? 201.687 214.532 288.142 1.00 69.60  ? 286  TYR B OH  1 
ATOM   2290  N N   . TYR A 1 304  ? 207.734 219.982 285.053 1.00 73.82  ? 287  TYR B N   1 
ATOM   2291  C CA  . TYR A 1 304  ? 208.918 220.806 284.837 1.00 73.82  ? 287  TYR B CA  1 
ATOM   2292  C C   . TYR A 1 304  ? 208.892 222.039 285.728 1.00 73.82  ? 287  TYR B C   1 
ATOM   2293  O O   . TYR A 1 304  ? 209.916 222.418 286.310 1.00 73.82  ? 287  TYR B O   1 
ATOM   2294  C CB  . TYR A 1 304  ? 209.018 221.214 283.369 1.00 73.82  ? 287  TYR B CB  1 
ATOM   2295  C CG  . TYR A 1 304  ? 210.049 222.285 283.106 1.00 73.82  ? 287  TYR B CG  1 
ATOM   2296  C CD1 . TYR A 1 304  ? 211.391 222.063 283.372 1.00 73.82  ? 287  TYR B CD1 1 
ATOM   2297  C CD2 . TYR A 1 304  ? 209.679 223.520 282.593 1.00 73.82  ? 287  TYR B CD2 1 
ATOM   2298  C CE1 . TYR A 1 304  ? 212.336 223.039 283.135 1.00 73.82  ? 287  TYR B CE1 1 
ATOM   2299  C CE2 . TYR A 1 304  ? 210.616 224.503 282.352 1.00 73.82  ? 287  TYR B CE2 1 
ATOM   2300  C CZ  . TYR A 1 304  ? 211.944 224.257 282.625 1.00 73.82  ? 287  TYR B CZ  1 
ATOM   2301  O OH  . TYR A 1 304  ? 212.882 225.233 282.387 1.00 73.82  ? 287  TYR B OH  1 
ATOM   2302  N N   . ASN A 1 305  ? 207.728 222.680 285.846 1.00 73.45  ? 288  ASN B N   1 
ATOM   2303  C CA  . ASN A 1 305  ? 207.614 223.822 286.744 1.00 73.45  ? 288  ASN B CA  1 
ATOM   2304  C C   . ASN A 1 305  ? 207.849 223.407 288.190 1.00 73.45  ? 288  ASN B C   1 
ATOM   2305  O O   . ASN A 1 305  ? 208.483 224.139 288.958 1.00 73.45  ? 288  ASN B O   1 
ATOM   2306  C CB  . ASN A 1 305  ? 206.247 224.482 286.584 1.00 73.45  ? 288  ASN B CB  1 
ATOM   2307  C CG  . ASN A 1 305  ? 206.191 225.412 285.392 1.00 73.45  ? 288  ASN B CG  1 
ATOM   2308  O OD1 . ASN A 1 305  ? 206.122 224.968 284.247 1.00 73.45  ? 288  ASN B OD1 1 
ATOM   2309  N ND2 . ASN A 1 305  ? 206.223 226.713 285.654 1.00 73.45  ? 288  ASN B ND2 1 
ATOM   2310  N N   . LYS A 1 306  ? 207.348 222.233 288.581 1.00 71.72  ? 289  LYS B N   1 
ATOM   2311  C CA  . LYS A 1 306  ? 207.592 221.752 289.940 1.00 71.72  ? 289  LYS B CA  1 
ATOM   2312  C C   . LYS A 1 306  ? 209.079 221.523 290.190 1.00 71.72  ? 289  LYS B C   1 
ATOM   2313  O O   . LYS A 1 306  ? 209.601 221.879 291.256 1.00 71.72  ? 289  LYS B O   1 
ATOM   2314  C CB  . LYS A 1 306  ? 206.802 220.468 290.196 1.00 71.72  ? 289  LYS B CB  1 
ATOM   2315  C CG  . LYS A 1 306  ? 205.314 220.687 290.408 1.00 71.72  ? 289  LYS B CG  1 
ATOM   2316  C CD  . LYS A 1 306  ? 205.052 221.910 291.270 1.00 71.72  ? 289  LYS B CD  1 
ATOM   2317  C CE  . LYS A 1 306  ? 203.569 222.093 291.532 1.00 71.72  ? 289  LYS B CE  1 
ATOM   2318  N NZ  . LYS A 1 306  ? 202.937 220.847 292.039 1.00 71.72  ? 289  LYS B NZ  1 
ATOM   2319  N N   . PHE A 1 307  ? 209.775 220.921 289.223 1.00 70.03  ? 290  PHE B N   1 
ATOM   2320  C CA  . PHE A 1 307  ? 211.207 220.684 289.376 1.00 70.03  ? 290  PHE B CA  1 
ATOM   2321  C C   . PHE A 1 307  ? 211.978 221.995 289.445 1.00 70.03  ? 290  PHE B C   1 
ATOM   2322  O O   . PHE A 1 307  ? 212.927 222.126 290.226 1.00 70.03  ? 290  PHE B O   1 
ATOM   2323  C CB  . PHE A 1 307  ? 211.725 219.810 288.236 1.00 70.03  ? 290  PHE B CB  1 
ATOM   2324  C CG  . PHE A 1 307  ? 211.593 218.336 288.494 1.00 70.03  ? 290  PHE B CG  1 
ATOM   2325  C CD1 . PHE A 1 307  ? 210.480 217.829 289.137 1.00 70.03  ? 290  PHE B CD1 1 
ATOM   2326  C CD2 . PHE A 1 307  ? 212.583 217.459 288.096 1.00 70.03  ? 290  PHE B CD2 1 
ATOM   2327  C CE1 . PHE A 1 307  ? 210.358 216.478 289.375 1.00 70.03  ? 290  PHE B CE1 1 
ATOM   2328  C CE2 . PHE A 1 307  ? 212.464 216.106 288.333 1.00 70.03  ? 290  PHE B CE2 1 
ATOM   2329  C CZ  . PHE A 1 307  ? 211.351 215.617 288.973 1.00 70.03  ? 290  PHE B CZ  1 
ATOM   2330  N N   . LYS A 1 308  ? 211.582 222.982 288.640 1.00 76.96  ? 291  LYS B N   1 
ATOM   2331  C CA  . LYS A 1 308  ? 212.210 224.296 288.728 1.00 76.96  ? 291  LYS B CA  1 
ATOM   2332  C C   . LYS A 1 308  ? 211.973 224.923 290.096 1.00 76.96  ? 291  LYS B C   1 
ATOM   2333  O O   . LYS A 1 308  ? 212.878 225.538 290.673 1.00 76.96  ? 291  LYS B O   1 
ATOM   2334  C CB  . LYS A 1 308  ? 211.682 225.201 287.615 1.00 76.96  ? 291  LYS B CB  1 
ATOM   2335  C CG  . LYS A 1 308  ? 211.742 226.684 287.926 1.00 76.96  ? 291  LYS B CG  1 
ATOM   2336  C CD  . LYS A 1 308  ? 210.829 227.472 287.005 1.00 76.96  ? 291  LYS B CD  1 
ATOM   2337  C CE  . LYS A 1 308  ? 211.348 227.462 285.577 1.00 76.96  ? 291  LYS B CE  1 
ATOM   2338  N NZ  . LYS A 1 308  ? 210.859 228.632 284.797 1.00 76.96  ? 291  LYS B NZ  1 
ATOM   2339  N N   . ASP A 1 309  ? 210.760 224.771 290.632 1.00 77.46  ? 292  ASP B N   1 
ATOM   2340  C CA  . ASP A 1 309  ? 210.444 225.338 291.939 1.00 77.46  ? 292  ASP B CA  1 
ATOM   2341  C C   . ASP A 1 309  ? 211.299 224.711 293.032 1.00 77.46  ? 292  ASP B C   1 
ATOM   2342  O O   . ASP A 1 309  ? 211.842 225.413 293.895 1.00 77.46  ? 292  ASP B O   1 
ATOM   2343  C CB  . ASP A 1 309  ? 208.958 225.146 292.240 1.00 77.46  ? 292  ASP B CB  1 
ATOM   2344  C CG  . ASP A 1 309  ? 208.372 226.299 293.024 1.00 77.46  ? 292  ASP B CG  1 
ATOM   2345  O OD1 . ASP A 1 309  ? 209.038 226.778 293.965 1.00 77.46  ? 292  ASP B OD1 1 
ATOM   2346  O OD2 . ASP A 1 309  ? 207.245 226.727 292.700 1.00 77.46  ? 292  ASP B OD2 1 
ATOM   2347  N N   . ILE A 1 310  ? 211.436 223.383 293.012 1.00 75.57  ? 293  ILE B N   1 
ATOM   2348  C CA  . ILE A 1 310  ? 212.234 222.740 294.053 1.00 75.57  ? 293  ILE B CA  1 
ATOM   2349  C C   . ILE A 1 310  ? 213.711 223.068 293.870 1.00 75.57  ? 293  ILE B C   1 
ATOM   2350  O O   . ILE A 1 310  ? 214.447 223.201 294.854 1.00 75.57  ? 293  ILE B O   1 
ATOM   2351  C CB  . ILE A 1 310  ? 211.985 221.220 294.096 1.00 75.57  ? 293  ILE B CB  1 
ATOM   2352  C CG1 . ILE A 1 310  ? 212.998 220.531 295.000 1.00 75.57  ? 293  ILE B CG1 1 
ATOM   2353  C CG2 . ILE A 1 310  ? 212.115 220.610 292.740 1.00 75.57  ? 293  ILE B CG2 1 
ATOM   2354  C CD1 . ILE A 1 310  ? 212.753 219.066 295.131 1.00 75.57  ? 293  ILE B CD1 1 
ATOM   2355  N N   . ALA A 1 311  ? 214.170 223.224 292.625 1.00 80.71  ? 294  ALA B N   1 
ATOM   2356  C CA  . ALA A 1 311  ? 215.549 223.648 292.401 1.00 80.71  ? 294  ALA B CA  1 
ATOM   2357  C C   . ALA A 1 311  ? 215.800 225.039 292.970 1.00 80.71  ? 294  ALA B C   1 
ATOM   2358  O O   . ALA A 1 311  ? 216.841 225.288 293.588 1.00 80.71  ? 294  ALA B O   1 
ATOM   2359  C CB  . ALA A 1 311  ? 215.871 223.615 290.908 1.00 80.71  ? 294  ALA B CB  1 
ATOM   2360  N N   . SER A 1 312  ? 214.858 225.963 292.769 1.00 82.31  ? 295  SER B N   1 
ATOM   2361  C CA  . SER A 1 312  ? 214.996 227.294 293.352 1.00 82.31  ? 295  SER B CA  1 
ATOM   2362  C C   . SER A 1 312  ? 214.989 227.233 294.875 1.00 82.31  ? 295  SER B C   1 
ATOM   2363  O O   . SER A 1 312  ? 215.757 227.942 295.538 1.00 82.31  ? 295  SER B O   1 
ATOM   2364  C CB  . SER A 1 312  ? 213.881 228.207 292.848 1.00 82.31  ? 295  SER B CB  1 
ATOM   2365  O OG  . SER A 1 312  ? 213.940 229.472 293.482 1.00 82.31  ? 295  SER B OG  1 
ATOM   2366  N N   . THR A 1 313  ? 214.121 226.393 295.448 1.00 82.68  ? 296  THR B N   1 
ATOM   2367  C CA  . THR A 1 313  ? 214.089 226.229 296.899 1.00 82.68  ? 296  THR B CA  1 
ATOM   2368  C C   . THR A 1 313  ? 215.420 225.704 297.423 1.00 82.68  ? 296  THR B C   1 
ATOM   2369  O O   . THR A 1 313  ? 215.928 226.180 298.445 1.00 82.68  ? 296  THR B O   1 
ATOM   2370  C CB  . THR A 1 313  ? 212.951 225.287 297.292 1.00 82.68  ? 296  THR B CB  1 
ATOM   2371  O OG1 . THR A 1 313  ? 211.718 226.015 297.329 1.00 82.68  ? 296  THR B OG1 1 
ATOM   2372  C CG2 . THR A 1 313  ? 213.207 224.663 298.656 1.00 82.68  ? 296  THR B CG2 1 
ATOM   2373  N N   . LEU A 1 314  ? 216.000 224.726 296.729 1.00 83.54  ? 297  LEU B N   1 
ATOM   2374  C CA  . LEU A 1 314  ? 217.311 224.211 297.104 1.00 83.54  ? 297  LEU B CA  1 
ATOM   2375  C C   . LEU A 1 314  ? 218.374 225.295 297.005 1.00 83.54  ? 297  LEU B C   1 
ATOM   2376  O O   . LEU A 1 314  ? 219.251 225.399 297.870 1.00 83.54  ? 297  LEU B O   1 
ATOM   2377  C CB  . LEU A 1 314  ? 217.672 223.028 296.210 1.00 83.54  ? 297  LEU B CB  1 
ATOM   2378  C CG  . LEU A 1 314  ? 218.723 222.051 296.717 1.00 83.54  ? 297  LEU B CG  1 
ATOM   2379  C CD1 . LEU A 1 314  ? 218.407 221.620 298.133 1.00 83.54  ? 297  LEU B CD1 1 
ATOM   2380  C CD2 . LEU A 1 314  ? 218.788 220.859 295.790 1.00 83.54  ? 297  LEU B CD2 1 
ATOM   2381  N N   . ASN A 1 315  ? 218.311 226.108 295.950 1.00 89.36  ? 298  ASN B N   1 
ATOM   2382  C CA  . ASN A 1 315  ? 219.288 227.176 295.769 1.00 89.36  ? 298  ASN B CA  1 
ATOM   2383  C C   . ASN A 1 315  ? 219.220 228.188 296.904 1.00 89.36  ? 298  ASN B C   1 
ATOM   2384  O O   . ASN A 1 315  ? 220.253 228.609 297.435 1.00 89.36  ? 298  ASN B O   1 
ATOM   2385  C CB  . ASN A 1 315  ? 219.053 227.871 294.429 1.00 89.36  ? 298  ASN B CB  1 
ATOM   2386  C CG  . ASN A 1 315  ? 220.177 227.638 293.444 1.00 89.36  ? 298  ASN B CG  1 
ATOM   2387  O OD1 . ASN A 1 315  ? 221.172 226.984 293.758 1.00 89.36  ? 298  ASN B OD1 1 
ATOM   2388  N ND2 . ASN A 1 315  ? 220.024 228.175 292.240 1.00 89.36  ? 298  ASN B ND2 1 
ATOM   2389  N N   . LYS A 1 316  ? 218.008 228.591 297.288 1.00 94.08  ? 299  LYS B N   1 
ATOM   2390  C CA  . LYS A 1 316  ? 217.859 229.642 298.289 1.00 94.08  ? 299  LYS B CA  1 
ATOM   2391  C C   . LYS A 1 316  ? 218.402 229.210 299.646 1.00 94.08  ? 299  LYS B C   1 
ATOM   2392  O O   . LYS A 1 316  ? 219.065 229.995 300.333 1.00 94.08  ? 299  LYS B O   1 
ATOM   2393  C CB  . LYS A 1 316  ? 216.390 230.047 298.400 1.00 94.08  ? 299  LYS B CB  1 
ATOM   2394  C CG  . LYS A 1 316  ? 216.018 230.705 299.714 1.00 94.08  ? 299  LYS B CG  1 
ATOM   2395  C CD  . LYS A 1 316  ? 214.531 230.580 299.980 1.00 94.08  ? 299  LYS B CD  1 
ATOM   2396  C CE  . LYS A 1 316  ? 213.722 231.352 298.955 1.00 94.08  ? 299  LYS B CE  1 
ATOM   2397  N NZ  . LYS A 1 316  ? 212.290 231.453 299.348 1.00 94.08  ? 299  LYS B NZ  1 
ATOM   2398  N N   . ALA A 1 317  ? 218.139 227.969 300.045 1.00 95.44  ? 300  ALA B N   1 
ATOM   2399  C CA  . ALA A 1 317  ? 218.510 227.509 301.375 1.00 95.44  ? 300  ALA B CA  1 
ATOM   2400  C C   . ALA A 1 317  ? 220.024 227.434 301.529 1.00 95.44  ? 300  ALA B C   1 
ATOM   2401  O O   . ALA A 1 317  ? 220.757 227.148 300.579 1.00 95.44  ? 300  ALA B O   1 
ATOM   2402  C CB  . ALA A 1 317  ? 217.891 226.143 301.658 1.00 95.44  ? 300  ALA B CB  1 
ATOM   2403  N N   . LYS A 1 318  ? 220.490 227.702 302.751 1.00 97.49  ? 301  LYS B N   1 
ATOM   2404  C CA  . LYS A 1 318  ? 221.912 227.641 303.054 1.00 97.49  ? 301  LYS B CA  1 
ATOM   2405  C C   . LYS A 1 318  ? 222.224 227.001 304.400 1.00 97.49  ? 301  LYS B C   1 
ATOM   2406  O O   . LYS A 1 318  ? 223.401 226.932 304.768 1.00 97.49  ? 301  LYS B O   1 
ATOM   2407  C CB  . LYS A 1 318  ? 222.528 229.050 303.010 1.00 97.49  ? 301  LYS B CB  1 
ATOM   2408  C CG  . LYS A 1 318  ? 221.668 230.129 303.654 1.00 97.49  ? 301  LYS B CG  1 
ATOM   2409  C CD  . LYS A 1 318  ? 221.998 230.297 305.130 1.00 97.49  ? 301  LYS B CD  1 
ATOM   2410  C CE  . LYS A 1 318  ? 221.144 231.373 305.775 1.00 97.49  ? 301  LYS B CE  1 
ATOM   2411  N NZ  . LYS A 1 318  ? 221.313 231.394 307.253 1.00 97.49  ? 301  LYS B NZ  1 
ATOM   2412  N N   . SER A 1 319  ? 221.225 226.528 305.141 1.00 99.80  ? 302  SER B N   1 
ATOM   2413  C CA  . SER A 1 319  ? 221.447 225.917 306.442 1.00 99.80  ? 302  SER B CA  1 
ATOM   2414  C C   . SER A 1 319  ? 220.629 224.640 306.545 1.00 99.80  ? 302  SER B C   1 
ATOM   2415  O O   . SER A 1 319  ? 219.589 224.496 305.899 1.00 99.80  ? 302  SER B O   1 
ATOM   2416  C CB  . SER A 1 319  ? 221.079 226.867 307.589 1.00 99.80  ? 302  SER B CB  1 
ATOM   2417  O OG  . SER A 1 319  ? 219.676 226.923 307.771 1.00 99.80  ? 302  SER B OG  1 
ATOM   2418  N N   . ILE A 1 320  ? 221.113 223.712 307.365 1.00 94.15  ? 303  ILE B N   1 
ATOM   2419  C CA  . ILE A 1 320  ? 220.464 222.426 307.577 1.00 94.15  ? 303  ILE B CA  1 
ATOM   2420  C C   . ILE A 1 320  ? 220.416 222.159 309.074 1.00 94.15  ? 303  ILE B C   1 
ATOM   2421  O O   . ILE A 1 320  ? 221.395 222.398 309.789 1.00 94.15  ? 303  ILE B O   1 
ATOM   2422  C CB  . ILE A 1 320  ? 221.197 221.291 306.827 1.00 94.15  ? 303  ILE B CB  1 
ATOM   2423  C CG1 . ILE A 1 320  ? 220.525 219.943 307.084 1.00 94.15  ? 303  ILE B CG1 1 
ATOM   2424  C CG2 . ILE A 1 320  ? 222.670 221.241 307.212 1.00 94.15  ? 303  ILE B CG2 1 
ATOM   2425  C CD1 . ILE A 1 320  ? 220.640 218.985 305.921 1.00 94.15  ? 303  ILE B CD1 1 
ATOM   2426  N N   . VAL A 1 321  ? 219.266 221.691 309.553 1.00 96.97  ? 304  VAL B N   1 
ATOM   2427  C CA  . VAL A 1 321  ? 219.060 221.412 310.969 1.00 96.97  ? 304  VAL B CA  1 
ATOM   2428  C C   . VAL A 1 321  ? 218.504 220.002 311.117 1.00 96.97  ? 304  VAL B C   1 
ATOM   2429  O O   . VAL A 1 321  ? 217.578 219.614 310.397 1.00 96.97  ? 304  VAL B O   1 
ATOM   2430  C CB  . VAL A 1 321  ? 218.124 222.447 311.625 1.00 96.97  ? 304  VAL B CB  1 
ATOM   2431  C CG1 . VAL A 1 321  ? 216.813 222.559 310.862 1.00 96.97  ? 304  VAL B CG1 1 
ATOM   2432  C CG2 . VAL A 1 321  ? 217.869 222.085 313.079 1.00 96.97  ? 304  VAL B CG2 1 
ATOM   2433  N N   . GLY A 1 322  ? 219.082 219.232 312.036 1.00 95.52  ? 305  GLY B N   1 
ATOM   2434  C CA  . GLY A 1 322  ? 218.598 217.900 312.341 1.00 95.52  ? 305  GLY B CA  1 
ATOM   2435  C C   . GLY A 1 322  ? 219.520 216.765 311.954 1.00 95.52  ? 305  GLY B C   1 
ATOM   2436  O O   . GLY A 1 322  ? 219.149 215.603 312.156 1.00 95.52  ? 305  GLY B O   1 
ATOM   2437  N N   . THR A 1 323  ? 220.700 217.045 311.407 1.00 98.88  ? 306  THR B N   1 
ATOM   2438  C CA  . THR A 1 323  ? 221.603 215.972 311.019 1.00 98.88  ? 306  THR B CA  1 
ATOM   2439  C C   . THR A 1 323  ? 223.044 216.446 311.113 1.00 98.88  ? 306  THR B C   1 
ATOM   2440  O O   . THR A 1 323  ? 223.336 217.643 311.065 1.00 98.88  ? 306  THR B O   1 
ATOM   2441  C CB  . THR A 1 323  ? 221.308 215.469 309.603 1.00 98.88  ? 306  THR B CB  1 
ATOM   2442  O OG1 . THR A 1 323  ? 222.206 214.399 309.284 1.00 98.88  ? 306  THR B OG1 1 
ATOM   2443  C CG2 . THR A 1 323  ? 221.479 216.591 308.596 1.00 98.88  ? 306  THR B CG2 1 
ATOM   2444  N N   . THR A 1 324  ? 223.946 215.473 311.255 1.00 98.99  ? 307  THR B N   1 
ATOM   2445  C CA  . THR A 1 324  ? 225.373 215.756 311.336 1.00 98.99  ? 307  THR B CA  1 
ATOM   2446  C C   . THR A 1 324  ? 225.979 216.062 309.971 1.00 98.99  ? 307  THR B C   1 
ATOM   2447  O O   . THR A 1 324  ? 226.845 216.939 309.865 1.00 98.99  ? 307  THR B O   1 
ATOM   2448  C CB  . THR A 1 324  ? 226.091 214.571 311.992 1.00 98.99  ? 307  THR B CB  1 
ATOM   2449  O OG1 . THR A 1 324  ? 225.966 214.667 313.417 1.00 98.99  ? 307  THR B OG1 1 
ATOM   2450  C CG2 . THR A 1 324  ? 227.568 214.533 311.618 1.00 98.99  ? 307  THR B CG2 1 
ATOM   2451  N N   . ALA A 1 325  ? 225.515 215.384 308.922 1.00 98.20  ? 308  ALA B N   1 
ATOM   2452  C CA  . ALA A 1 325  ? 226.170 215.443 307.622 1.00 98.20  ? 308  ALA B CA  1 
ATOM   2453  C C   . ALA A 1 325  ? 226.183 216.863 307.069 1.00 98.20  ? 308  ALA B C   1 
ATOM   2454  O O   . ALA A 1 325  ? 225.267 217.655 307.299 1.00 98.20  ? 308  ALA B O   1 
ATOM   2455  C CB  . ALA A 1 325  ? 225.472 214.507 306.635 1.00 98.20  ? 308  ALA B CB  1 
ATOM   2456  N N   . SER A 1 326  ? 227.248 217.177 306.335 1.00 94.25  ? 309  SER B N   1 
ATOM   2457  C CA  . SER A 1 326  ? 227.430 218.513 305.790 1.00 94.25  ? 309  SER B CA  1 
ATOM   2458  C C   . SER A 1 326  ? 226.355 218.833 304.757 1.00 94.25  ? 309  SER B C   1 
ATOM   2459  O O   . SER A 1 326  ? 225.848 217.952 304.058 1.00 94.25  ? 309  SER B O   1 
ATOM   2460  C CB  . SER A 1 326  ? 228.816 218.647 305.160 1.00 94.25  ? 309  SER B CB  1 
ATOM   2461  O OG  . SER A 1 326  ? 228.934 217.830 304.009 1.00 94.25  ? 309  SER B OG  1 
ATOM   2462  N N   . LEU A 1 327  ? 226.010 220.119 304.671 1.00 88.66  ? 310  LEU B N   1 
ATOM   2463  C CA  . LEU A 1 327  ? 224.960 220.553 303.755 1.00 88.66  ? 310  LEU B CA  1 
ATOM   2464  C C   . LEU A 1 327  ? 225.339 220.292 302.304 1.00 88.66  ? 310  LEU B C   1 
ATOM   2465  O O   . LEU A 1 327  ? 224.488 219.903 301.496 1.00 88.66  ? 310  LEU B O   1 
ATOM   2466  C CB  . LEU A 1 327  ? 224.658 222.035 303.977 1.00 88.66  ? 310  LEU B CB  1 
ATOM   2467  C CG  . LEU A 1 327  ? 223.552 222.668 303.133 1.00 88.66  ? 310  LEU B CG  1 
ATOM   2468  C CD1 . LEU A 1 327  ? 222.774 223.661 303.960 1.00 88.66  ? 310  LEU B CD1 1 
ATOM   2469  C CD2 . LEU A 1 327  ? 224.138 223.365 301.921 1.00 88.66  ? 310  LEU B CD2 1 
ATOM   2470  N N   . GLN A 1 328  ? 226.607 220.518 301.952 1.00 89.66  ? 311  GLN B N   1 
ATOM   2471  C CA  . GLN A 1 328  ? 227.030 220.375 300.562 1.00 89.66  ? 311  GLN B CA  1 
ATOM   2472  C C   . GLN A 1 328  ? 226.781 218.963 300.055 1.00 89.66  ? 311  GLN B C   1 
ATOM   2473  O O   . GLN A 1 328  ? 226.411 218.768 298.892 1.00 89.66  ? 311  GLN B O   1 
ATOM   2474  C CB  . GLN A 1 328  ? 228.506 220.744 300.419 1.00 89.66  ? 311  GLN B CB  1 
ATOM   2475  C CG  . GLN A 1 328  ? 228.863 222.127 300.942 1.00 89.66  ? 311  GLN B CG  1 
ATOM   2476  C CD  . GLN A 1 328  ? 229.151 222.138 302.433 1.00 89.66  ? 311  GLN B CD  1 
ATOM   2477  O OE1 . GLN A 1 328  ? 228.599 221.341 303.191 1.00 89.66  ? 311  GLN B OE1 1 
ATOM   2478  N NE2 . GLN A 1 328  ? 230.022 223.045 302.859 1.00 89.66  ? 311  GLN B NE2 1 
ATOM   2479  N N   . TYR A 1 329  ? 226.973 217.965 300.918 1.00 92.48  ? 312  TYR B N   1 
ATOM   2480  C CA  . TYR A 1 329  ? 226.682 216.591 300.529 1.00 92.48  ? 312  TYR B CA  1 
ATOM   2481  C C   . TYR A 1 329  ? 225.199 216.410 300.226 1.00 92.48  ? 312  TYR B C   1 
ATOM   2482  O O   . TYR A 1 329  ? 224.834 215.721 299.267 1.00 92.48  ? 312  TYR B O   1 
ATOM   2483  C CB  . TYR A 1 329  ? 227.137 215.633 301.629 1.00 92.48  ? 312  TYR B CB  1 
ATOM   2484  C CG  . TYR A 1 329  ? 226.395 214.324 301.644 1.00 92.48  ? 312  TYR B CG  1 
ATOM   2485  C CD1 . TYR A 1 329  ? 226.611 213.373 300.661 1.00 92.48  ? 312  TYR B CD1 1 
ATOM   2486  C CD2 . TYR A 1 329  ? 225.480 214.037 302.643 1.00 92.48  ? 312  TYR B CD2 1 
ATOM   2487  C CE1 . TYR A 1 329  ? 225.937 212.174 300.671 1.00 92.48  ? 312  TYR B CE1 1 
ATOM   2488  C CE2 . TYR A 1 329  ? 224.800 212.840 302.661 1.00 92.48  ? 312  TYR B CE2 1 
ATOM   2489  C CZ  . TYR A 1 329  ? 225.031 211.912 301.672 1.00 92.48  ? 312  TYR B CZ  1 
ATOM   2490  O OH  . TYR A 1 329  ? 224.353 210.717 301.686 1.00 92.48  ? 312  TYR B OH  1 
ATOM   2491  N N   . MET A 1 330  ? 224.328 217.028 301.030 1.00 87.86  ? 313  MET B N   1 
ATOM   2492  C CA  . MET A 1 330  ? 222.893 216.946 300.769 1.00 87.86  ? 313  MET B CA  1 
ATOM   2493  C C   . MET A 1 330  ? 222.527 217.622 299.455 1.00 87.86  ? 313  MET B C   1 
ATOM   2494  O O   . MET A 1 330  ? 221.707 217.104 298.685 1.00 87.86  ? 313  MET B O   1 
ATOM   2495  C CB  . MET A 1 330  ? 222.112 217.573 301.924 1.00 87.86  ? 313  MET B CB  1 
ATOM   2496  C CG  . MET A 1 330  ? 220.755 216.940 302.169 1.00 87.86  ? 313  MET B CG  1 
ATOM   2497  S SD  . MET A 1 330  ? 220.855 215.228 302.717 1.00 87.86  ? 313  MET B SD  1 
ATOM   2498  C CE  . MET A 1 330  ? 222.292 215.293 303.781 1.00 87.86  ? 313  MET B CE  1 
ATOM   2499  N N   . LYS A 1 331  ? 223.114 218.789 299.190 1.00 85.91  ? 314  LYS B N   1 
ATOM   2500  C CA  . LYS A 1 331  ? 222.840 219.472 297.932 1.00 85.91  ? 314  LYS B CA  1 
ATOM   2501  C C   . LYS A 1 331  ? 223.317 218.642 296.749 1.00 85.91  ? 314  LYS B C   1 
ATOM   2502  O O   . LYS A 1 331  ? 222.640 218.575 295.720 1.00 85.91  ? 314  LYS B O   1 
ATOM   2503  C CB  . LYS A 1 331  ? 223.489 220.855 297.924 1.00 85.91  ? 314  LYS B CB  1 
ATOM   2504  C CG  . LYS A 1 331  ? 222.610 221.949 298.508 1.00 85.91  ? 314  LYS B CG  1 
ATOM   2505  C CD  . LYS A 1 331  ? 223.263 223.310 298.377 1.00 85.91  ? 314  LYS B CD  1 
ATOM   2506  C CE  . LYS A 1 331  ? 222.384 224.394 298.973 1.00 85.91  ? 314  LYS B CE  1 
ATOM   2507  N NZ  . LYS A 1 331  ? 222.724 225.745 298.442 1.00 85.91  ? 314  LYS B NZ  1 
ATOM   2508  N N   . ASN A 1 332  ? 224.474 217.992 296.880 1.00 81.93  ? 315  ASN B N   1 
ATOM   2509  C CA  . ASN A 1 332  ? 224.945 217.112 295.816 1.00 81.93  ? 315  ASN B CA  1 
ATOM   2510  C C   . ASN A 1 332  ? 224.011 215.923 295.629 1.00 81.93  ? 315  ASN B C   1 
ATOM   2511  O O   . ASN A 1 332  ? 223.758 215.494 294.495 1.00 81.93  ? 315  ASN B O   1 
ATOM   2512  C CB  . ASN A 1 332  ? 226.364 216.635 296.115 1.00 81.93  ? 315  ASN B CB  1 
ATOM   2513  C CG  . ASN A 1 332  ? 226.924 215.752 295.019 1.00 81.93  ? 315  ASN B CG  1 
ATOM   2514  O OD1 . ASN A 1 332  ? 226.679 214.547 294.991 1.00 81.93  ? 315  ASN B OD1 1 
ATOM   2515  N ND2 . ASN A 1 332  ? 227.680 216.350 294.106 1.00 81.93  ? 315  ASN B ND2 1 
ATOM   2516  N N   . VAL A 1 333  ? 223.492 215.373 296.729 1.00 82.01  ? 316  VAL B N   1 
ATOM   2517  C CA  . VAL A 1 333  ? 222.573 214.241 296.636 1.00 82.01  ? 316  VAL B CA  1 
ATOM   2518  C C   . VAL A 1 333  ? 221.314 214.642 295.880 1.00 82.01  ? 316  VAL B C   1 
ATOM   2519  O O   . VAL A 1 333  ? 220.853 213.933 294.977 1.00 82.01  ? 316  VAL B O   1 
ATOM   2520  C CB  . VAL A 1 333  ? 222.241 213.704 298.039 1.00 82.01  ? 316  VAL B CB  1 
ATOM   2521  C CG1 . VAL A 1 333  ? 220.894 213.013 298.035 1.00 82.01  ? 316  VAL B CG1 1 
ATOM   2522  C CG2 . VAL A 1 333  ? 223.316 212.746 298.500 1.00 82.01  ? 316  VAL B CG2 1 
ATOM   2523  N N   . PHE A 1 334  ? 220.748 215.796 296.225 1.00 78.65  ? 317  PHE B N   1 
ATOM   2524  C CA  . PHE A 1 334  ? 219.533 216.222 295.542 1.00 78.65  ? 317  PHE B CA  1 
ATOM   2525  C C   . PHE A 1 334  ? 219.816 216.629 294.101 1.00 78.65  ? 317  PHE B C   1 
ATOM   2526  O O   . PHE A 1 334  ? 218.963 216.437 293.226 1.00 78.65  ? 317  PHE B O   1 
ATOM   2527  C CB  . PHE A 1 334  ? 218.867 217.354 296.316 1.00 78.65  ? 317  PHE B CB  1 
ATOM   2528  C CG  . PHE A 1 334  ? 218.181 216.894 297.566 1.00 78.65  ? 317  PHE B CG  1 
ATOM   2529  C CD1 . PHE A 1 334  ? 217.287 215.842 297.529 1.00 78.65  ? 317  PHE B CD1 1 
ATOM   2530  C CD2 . PHE A 1 334  ? 218.442 217.500 298.780 1.00 78.65  ? 317  PHE B CD2 1 
ATOM   2531  C CE1 . PHE A 1 334  ? 216.662 215.411 298.674 1.00 78.65  ? 317  PHE B CE1 1 
ATOM   2532  C CE2 . PHE A 1 334  ? 217.817 217.070 299.929 1.00 78.65  ? 317  PHE B CE2 1 
ATOM   2533  C CZ  . PHE A 1 334  ? 216.926 216.026 299.875 1.00 78.65  ? 317  PHE B CZ  1 
ATOM   2534  N N   . LYS A 1 335  ? 221.007 217.168 293.830 1.00 76.45  ? 318  LYS B N   1 
ATOM   2535  C CA  . LYS A 1 335  ? 221.376 217.498 292.460 1.00 76.45  ? 318  LYS B CA  1 
ATOM   2536  C C   . LYS A 1 335  ? 221.475 216.248 291.600 1.00 76.45  ? 318  LYS B C   1 
ATOM   2537  O O   . LYS A 1 335  ? 221.011 216.237 290.455 1.00 76.45  ? 318  LYS B O   1 
ATOM   2538  C CB  . LYS A 1 335  ? 222.696 218.268 292.445 1.00 76.45  ? 318  LYS B CB  1 
ATOM   2539  C CG  . LYS A 1 335  ? 223.570 217.993 291.231 1.00 76.45  ? 318  LYS B CG  1 
ATOM   2540  C CD  . LYS A 1 335  ? 224.955 218.593 291.400 1.00 76.45  ? 318  LYS B CD  1 
ATOM   2541  C CE  . LYS A 1 335  ? 226.030 217.520 291.380 1.00 76.45  ? 318  LYS B CE  1 
ATOM   2542  N NZ  . LYS A 1 335  ? 226.084 216.807 290.076 1.00 76.45  ? 318  LYS B NZ  1 
ATOM   2543  N N   . GLU A 1 336  ? 222.078 215.181 292.128 1.00 77.85  ? 319  GLU B N   1 
ATOM   2544  C CA  . GLU A 1 336  ? 222.174 213.955 291.345 1.00 77.85  ? 319  GLU B CA  1 
ATOM   2545  C C   . GLU A 1 336  ? 220.851 213.206 291.285 1.00 77.85  ? 319  GLU B C   1 
ATOM   2546  O O   . GLU A 1 336  ? 220.657 212.394 290.376 1.00 77.85  ? 319  GLU B O   1 
ATOM   2547  C CB  . GLU A 1 336  ? 223.267 213.039 291.897 1.00 77.85  ? 319  GLU B CB  1 
ATOM   2548  C CG  . GLU A 1 336  ? 222.983 212.458 293.264 1.00 77.85  ? 319  GLU B CG  1 
ATOM   2549  C CD  . GLU A 1 336  ? 224.229 211.916 293.932 1.00 77.85  ? 319  GLU B CD  1 
ATOM   2550  O OE1 . GLU A 1 336  ? 224.751 210.883 293.464 1.00 77.85  ? 319  GLU B OE1 1 
ATOM   2551  O OE2 . GLU A 1 336  ? 224.689 212.521 294.922 1.00 77.85  ? 319  GLU B OE2 1 
ATOM   2552  N N   . LYS A 1 337  ? 219.943 213.447 292.232 1.00 71.52  ? 320  LYS B N   1 
ATOM   2553  C CA  . LYS A 1 337  ? 218.612 212.857 292.131 1.00 71.52  ? 320  LYS B CA  1 
ATOM   2554  C C   . LYS A 1 337  ? 217.778 213.548 291.059 1.00 71.52  ? 320  LYS B C   1 
ATOM   2555  O O   . LYS A 1 337  ? 217.119 212.886 290.251 1.00 71.52  ? 320  LYS B O   1 
ATOM   2556  C CB  . LYS A 1 337  ? 217.901 212.920 293.480 1.00 71.52  ? 320  LYS B CB  1 
ATOM   2557  C CG  . LYS A 1 337  ? 216.700 212.003 293.565 1.00 71.52  ? 320  LYS B CG  1 
ATOM   2558  C CD  . LYS A 1 337  ? 215.806 212.354 294.738 1.00 71.52  ? 320  LYS B CD  1 
ATOM   2559  C CE  . LYS A 1 337  ? 214.418 212.753 294.273 1.00 71.52  ? 320  LYS B CE  1 
ATOM   2560  N NZ  . LYS A 1 337  ? 213.668 213.471 295.336 1.00 71.52  ? 320  LYS B NZ  1 
ATOM   2561  N N   . TYR A 1 338  ? 217.792 214.880 291.036 1.00 70.88  ? 321  TYR B N   1 
ATOM   2562  C CA  . TYR A 1 338  ? 216.970 215.654 290.114 1.00 70.88  ? 321  TYR B CA  1 
ATOM   2563  C C   . TYR A 1 338  ? 217.701 216.049 288.840 1.00 70.88  ? 321  TYR B C   1 
ATOM   2564  O O   . TYR A 1 338  ? 217.100 216.701 287.979 1.00 70.88  ? 321  TYR B O   1 
ATOM   2565  C CB  . TYR A 1 338  ? 216.442 216.911 290.811 1.00 70.88  ? 321  TYR B CB  1 
ATOM   2566  C CG  . TYR A 1 338  ? 215.398 216.613 291.851 1.00 70.88  ? 321  TYR B CG  1 
ATOM   2567  C CD1 . TYR A 1 338  ? 214.119 216.227 291.484 1.00 70.88  ? 321  TYR B CD1 1 
ATOM   2568  C CD2 . TYR A 1 338  ? 215.695 216.695 293.202 1.00 70.88  ? 321  TYR B CD2 1 
ATOM   2569  C CE1 . TYR A 1 338  ? 213.164 215.942 292.432 1.00 70.88  ? 321  TYR B CE1 1 
ATOM   2570  C CE2 . TYR A 1 338  ? 214.748 216.410 294.155 1.00 70.88  ? 321  TYR B CE2 1 
ATOM   2571  C CZ  . TYR A 1 338  ? 213.484 216.036 293.764 1.00 70.88  ? 321  TYR B CZ  1 
ATOM   2572  O OH  . TYR A 1 338  ? 212.535 215.750 294.713 1.00 70.88  ? 321  TYR B OH  1 
ATOM   2573  N N   . LEU A 1 339  ? 218.973 215.673 288.700 1.00 74.89  ? 322  LEU B N   1 
ATOM   2574  C CA  . LEU A 1 339  ? 219.792 216.040 287.543 1.00 74.89  ? 322  LEU B CA  1 
ATOM   2575  C C   . LEU A 1 339  ? 219.828 217.554 287.341 1.00 74.89  ? 322  LEU B C   1 
ATOM   2576  O O   . LEU A 1 339  ? 219.751 218.050 286.217 1.00 74.89  ? 322  LEU B O   1 
ATOM   2577  C CB  . LEU A 1 339  ? 219.308 215.335 286.275 1.00 74.89  ? 322  LEU B CB  1 
ATOM   2578  C CG  . LEU A 1 339  ? 219.188 213.816 286.354 1.00 74.89  ? 322  LEU B CG  1 
ATOM   2579  C CD1 . LEU A 1 339  ? 218.589 213.266 285.075 1.00 74.89  ? 322  LEU B CD1 1 
ATOM   2580  C CD2 . LEU A 1 339  ? 220.538 213.187 286.626 1.00 74.89  ? 322  LEU B CD2 1 
ATOM   2581  N N   . LEU A 1 340  ? 219.936 218.297 288.439 1.00 78.48  ? 323  LEU B N   1 
ATOM   2582  C CA  . LEU A 1 340  ? 220.109 219.737 288.340 1.00 78.48  ? 323  LEU B CA  1 
ATOM   2583  C C   . LEU A 1 340  ? 221.506 220.064 287.824 1.00 78.48  ? 323  LEU B C   1 
ATOM   2584  O O   . LEU A 1 340  ? 222.430 219.251 287.893 1.00 78.48  ? 323  LEU B O   1 
ATOM   2585  C CB  . LEU A 1 340  ? 219.884 220.409 289.693 1.00 78.48  ? 323  LEU B CB  1 
ATOM   2586  C CG  . LEU A 1 340  ? 218.584 220.109 290.434 1.00 78.48  ? 323  LEU B CG  1 
ATOM   2587  C CD1 . LEU A 1 340  ? 218.412 221.069 291.596 1.00 78.48  ? 323  LEU B CD1 1 
ATOM   2588  C CD2 . LEU A 1 340  ? 217.408 220.198 289.491 1.00 78.48  ? 323  LEU B CD2 1 
ATOM   2589  N N   . SER A 1 341  ? 221.657 221.278 287.304 1.00 87.38  ? 324  SER B N   1 
ATOM   2590  C CA  . SER A 1 341  ? 222.919 221.728 286.722 1.00 87.38  ? 324  SER B CA  1 
ATOM   2591  C C   . SER A 1 341  ? 223.377 222.998 287.429 1.00 87.38  ? 324  SER B C   1 
ATOM   2592  O O   . SER A 1 341  ? 222.886 224.091 287.135 1.00 87.38  ? 324  SER B O   1 
ATOM   2593  C CB  . SER A 1 341  ? 222.771 221.957 285.224 1.00 87.38  ? 324  SER B CB  1 
ATOM   2594  O OG  . SER A 1 341  ? 222.414 220.756 284.569 1.00 87.38  ? 324  SER B OG  1 
ATOM   2595  N N   . GLU A 1 342  ? 224.318 222.854 288.357 1.00 98.84  ? 325  GLU B N   1 
ATOM   2596  C CA  . GLU A 1 342  ? 224.978 224.008 288.941 1.00 98.84  ? 325  GLU B CA  1 
ATOM   2597  C C   . GLU A 1 342  ? 226.037 224.539 287.979 1.00 98.84  ? 325  GLU B C   1 
ATOM   2598  O O   . GLU A 1 342  ? 226.459 223.856 287.043 1.00 98.84  ? 325  GLU B O   1 
ATOM   2599  C CB  . GLU A 1 342  ? 225.603 223.646 290.288 1.00 98.84  ? 325  GLU B CB  1 
ATOM   2600  C CG  . GLU A 1 342  ? 227.090 223.348 290.228 1.00 98.84  ? 325  GLU B CG  1 
ATOM   2601  C CD  . GLU A 1 342  ? 227.608 222.710 291.500 1.00 98.84  ? 325  GLU B CD  1 
ATOM   2602  O OE1 . GLU A 1 342  ? 226.833 222.604 292.474 1.00 98.84  ? 325  GLU B OE1 1 
ATOM   2603  O OE2 . GLU A 1 342  ? 228.792 222.312 291.523 1.00 98.84  ? 325  GLU B OE2 1 
ATOM   2604  N N   . ASP A 1 343  ? 226.464 225.776 288.213 1.00 108.49 ? 326  ASP B N   1 
ATOM   2605  C CA  . ASP A 1 343  ? 227.391 226.460 287.318 1.00 108.49 ? 326  ASP B CA  1 
ATOM   2606  C C   . ASP A 1 343  ? 228.576 227.020 288.092 1.00 108.49 ? 326  ASP B C   1 
ATOM   2607  O O   . ASP A 1 343  ? 228.950 228.186 287.953 1.00 108.49 ? 326  ASP B O   1 
ATOM   2608  C CB  . ASP A 1 343  ? 226.678 227.562 286.543 1.00 108.49 ? 326  ASP B CB  1 
ATOM   2609  C CG  . ASP A 1 343  ? 226.307 227.135 285.139 1.00 108.49 ? 326  ASP B CG  1 
ATOM   2610  O OD1 . ASP A 1 343  ? 227.226 226.870 284.336 1.00 108.49 ? 326  ASP B OD1 1 
ATOM   2611  O OD2 . ASP A 1 343  ? 225.097 227.059 284.839 1.00 108.49 ? 326  ASP B OD2 1 
ATOM   2612  N N   . THR A 1 344  ? 229.179 226.180 288.933 1.00 113.52 ? 327  THR B N   1 
ATOM   2613  C CA  . THR A 1 344  ? 230.393 226.481 289.690 1.00 113.52 ? 327  THR B CA  1 
ATOM   2614  C C   . THR A 1 344  ? 230.243 227.683 290.615 1.00 113.52 ? 327  THR B C   1 
ATOM   2615  O O   . THR A 1 344  ? 231.241 228.161 291.167 1.00 113.52 ? 327  THR B O   1 
ATOM   2616  C CB  . THR A 1 344  ? 231.601 226.696 288.766 1.00 113.52 ? 327  THR B CB  1 
ATOM   2617  O OG1 . THR A 1 344  ? 231.535 228.004 288.184 1.00 113.52 ? 327  THR B OG1 1 
ATOM   2618  C CG2 . THR A 1 344  ? 231.636 225.645 287.662 1.00 113.52 ? 327  THR B CG2 1 
ATOM   2619  N N   . SER A 1 345  ? 229.023 228.185 290.803 1.00 112.98 ? 328  SER B N   1 
ATOM   2620  C CA  . SER A 1 345  ? 228.764 229.304 291.701 1.00 112.98 ? 328  SER B CA  1 
ATOM   2621  C C   . SER A 1 345  ? 227.692 228.964 292.729 1.00 112.98 ? 328  SER B C   1 
ATOM   2622  O O   . SER A 1 345  ? 227.154 229.864 293.382 1.00 112.98 ? 328  SER B O   1 
ATOM   2623  C CB  . SER A 1 345  ? 228.365 230.549 290.906 1.00 112.98 ? 328  SER B CB  1 
ATOM   2624  O OG  . SER A 1 345  ? 228.358 231.700 291.732 1.00 112.98 ? 328  SER B OG  1 
ATOM   2625  N N   . GLY A 1 346  ? 227.374 227.684 292.887 1.00 107.37 ? 329  GLY B N   1 
ATOM   2626  C CA  . GLY A 1 346  ? 226.318 227.275 293.794 1.00 107.37 ? 329  GLY B CA  1 
ATOM   2627  C C   . GLY A 1 346  ? 224.946 227.757 293.380 1.00 107.37 ? 329  GLY B C   1 
ATOM   2628  O O   . GLY A 1 346  ? 224.128 228.104 294.242 1.00 107.37 ? 329  GLY B O   1 
ATOM   2629  N N   . LYS A 1 347  ? 224.670 227.789 292.080 1.00 102.01 ? 330  LYS B N   1 
ATOM   2630  C CA  . LYS A 1 347  ? 223.390 228.247 291.549 1.00 102.01 ? 330  LYS B CA  1 
ATOM   2631  C C   . LYS A 1 347  ? 222.771 227.099 290.760 1.00 102.01 ? 330  LYS B C   1 
ATOM   2632  O O   . LYS A 1 347  ? 222.960 226.991 289.546 1.00 102.01 ? 330  LYS B O   1 
ATOM   2633  C CB  . LYS A 1 347  ? 223.568 229.492 290.686 1.00 102.01 ? 330  LYS B CB  1 
ATOM   2634  C CG  . LYS A 1 347  ? 223.804 230.766 291.483 1.00 102.01 ? 330  LYS B CG  1 
ATOM   2635  C CD  . LYS A 1 347  ? 222.709 230.983 292.518 1.00 102.01 ? 330  LYS B CD  1 
ATOM   2636  C CE  . LYS A 1 347  ? 223.201 231.839 293.672 1.00 102.01 ? 330  LYS B CE  1 
ATOM   2637  N NZ  . LYS A 1 347  ? 224.277 231.159 294.443 1.00 102.01 ? 330  LYS B NZ  1 
ATOM   2638  N N   . PHE A 1 348  ? 222.030 226.244 291.458 1.00 90.82  ? 331  PHE B N   1 
ATOM   2639  C CA  . PHE A 1 348  ? 221.345 225.136 290.809 1.00 90.82  ? 331  PHE B CA  1 
ATOM   2640  C C   . PHE A 1 348  ? 220.250 225.649 289.883 1.00 90.82  ? 331  PHE B C   1 
ATOM   2641  O O   . PHE A 1 348  ? 219.542 226.608 290.200 1.00 90.82  ? 331  PHE B O   1 
ATOM   2642  C CB  . PHE A 1 348  ? 220.743 224.199 291.854 1.00 90.82  ? 331  PHE B CB  1 
ATOM   2643  C CG  . PHE A 1 348  ? 221.757 223.383 292.593 1.00 90.82  ? 331  PHE B CG  1 
ATOM   2644  C CD1 . PHE A 1 348  ? 222.575 222.499 291.920 1.00 90.82  ? 331  PHE B CD1 1 
ATOM   2645  C CD2 . PHE A 1 348  ? 221.889 223.500 293.963 1.00 90.82  ? 331  PHE B CD2 1 
ATOM   2646  C CE1 . PHE A 1 348  ? 223.508 221.747 292.599 1.00 90.82  ? 331  PHE B CE1 1 
ATOM   2647  C CE2 . PHE A 1 348  ? 222.820 222.750 294.648 1.00 90.82  ? 331  PHE B CE2 1 
ATOM   2648  C CZ  . PHE A 1 348  ? 223.631 221.873 293.965 1.00 90.82  ? 331  PHE B CZ  1 
ATOM   2649  N N   . SER A 1 349  ? 220.117 225.002 288.729 1.00 86.01  ? 332  SER B N   1 
ATOM   2650  C CA  . SER A 1 349  ? 219.062 225.323 287.782 1.00 86.01  ? 332  SER B CA  1 
ATOM   2651  C C   . SER A 1 349  ? 218.756 224.083 286.959 1.00 86.01  ? 332  SER B C   1 
ATOM   2652  O O   . SER A 1 349  ? 219.592 223.188 286.818 1.00 86.01  ? 332  SER B O   1 
ATOM   2653  C CB  . SER A 1 349  ? 219.454 226.489 286.869 1.00 86.01  ? 332  SER B CB  1 
ATOM   2654  O OG  . SER A 1 349  ? 219.907 227.601 287.620 1.00 86.01  ? 332  SER B OG  1 
ATOM   2655  N N   . VAL A 1 350  ? 217.553 224.041 286.415 1.00 78.06  ? 333  VAL B N   1 
ATOM   2656  C CA  . VAL A 1 350  ? 217.119 222.922 285.588 1.00 78.06  ? 333  VAL B CA  1 
ATOM   2657  C C   . VAL A 1 350  ? 217.452 223.217 284.136 1.00 78.06  ? 333  VAL B C   1 
ATOM   2658  O O   . VAL A 1 350  ? 217.501 224.373 283.705 1.00 78.06  ? 333  VAL B O   1 
ATOM   2659  C CB  . VAL A 1 350  ? 215.612 222.647 285.768 1.00 78.06  ? 333  VAL B CB  1 
ATOM   2660  C CG1 . VAL A 1 350  ? 215.348 222.001 287.112 1.00 78.06  ? 333  VAL B CG1 1 
ATOM   2661  C CG2 . VAL A 1 350  ? 214.822 223.936 285.627 1.00 78.06  ? 333  VAL B CG2 1 
ATOM   2662  N N   . ASP A 1 351  ? 217.693 222.158 283.372 1.00 77.84  ? 334  ASP B N   1 
ATOM   2663  C CA  . ASP A 1 351  ? 217.879 222.245 281.933 1.00 77.84  ? 334  ASP B CA  1 
ATOM   2664  C C   . ASP A 1 351  ? 216.843 221.359 281.260 1.00 77.84  ? 334  ASP B C   1 
ATOM   2665  O O   . ASP A 1 351  ? 216.558 220.256 281.734 1.00 77.84  ? 334  ASP B O   1 
ATOM   2666  C CB  . ASP A 1 351  ? 219.296 221.827 281.527 1.00 77.84  ? 334  ASP B CB  1 
ATOM   2667  C CG  . ASP A 1 351  ? 219.546 221.971 280.037 1.00 77.84  ? 334  ASP B CG  1 
ATOM   2668  O OD1 . ASP A 1 351  ? 219.139 221.071 279.274 1.00 77.84  ? 334  ASP B OD1 1 
ATOM   2669  O OD2 . ASP A 1 351  ? 220.158 222.981 279.630 1.00 77.84  ? 334  ASP B OD2 1 
ATOM   2670  N N   . LYS A 1 352  ? 216.275 221.850 280.160 1.00 71.77  ? 335  LYS B N   1 
ATOM   2671  C CA  . LYS A 1 352  ? 215.143 221.164 279.550 1.00 71.77  ? 335  LYS B CA  1 
ATOM   2672  C C   . LYS A 1 352  ? 215.536 219.796 279.007 1.00 71.77  ? 335  LYS B C   1 
ATOM   2673  O O   . LYS A 1 352  ? 214.739 218.854 279.061 1.00 71.77  ? 335  LYS B O   1 
ATOM   2674  C CB  . LYS A 1 352  ? 214.541 222.028 278.445 1.00 71.77  ? 335  LYS B CB  1 
ATOM   2675  C CG  . LYS A 1 352  ? 213.357 222.861 278.899 1.00 71.77  ? 335  LYS B CG  1 
ATOM   2676  C CD  . LYS A 1 352  ? 212.235 221.988 279.437 1.00 71.77  ? 335  LYS B CD  1 
ATOM   2677  C CE  . LYS A 1 352  ? 211.394 221.412 278.309 1.00 71.77  ? 335  LYS B CE  1 
ATOM   2678  N NZ  . LYS A 1 352  ? 210.111 220.840 278.801 1.00 71.77  ? 335  LYS B NZ  1 
ATOM   2679  N N   . LEU A 1 353  ? 216.753 219.660 278.479 1.00 75.70  ? 336  LEU B N   1 
ATOM   2680  C CA  . LEU A 1 353  ? 217.153 218.394 277.870 1.00 75.70  ? 336  LEU B CA  1 
ATOM   2681  C C   . LEU A 1 353  ? 217.260 217.281 278.907 1.00 75.70  ? 336  LEU B C   1 
ATOM   2682  O O   . LEU A 1 353  ? 216.697 216.194 278.727 1.00 75.70  ? 336  LEU B O   1 
ATOM   2683  C CB  . LEU A 1 353  ? 218.480 218.565 277.131 1.00 75.70  ? 336  LEU B CB  1 
ATOM   2684  C CG  . LEU A 1 353  ? 219.050 217.305 276.475 1.00 75.70  ? 336  LEU B CG  1 
ATOM   2685  C CD1 . LEU A 1 353  ? 218.010 216.639 275.587 1.00 75.70  ? 336  LEU B CD1 1 
ATOM   2686  C CD2 . LEU A 1 353  ? 220.310 217.626 275.685 1.00 75.70  ? 336  LEU B CD2 1 
ATOM   2687  N N   . LYS A 1 354  ? 217.983 217.531 280.002 1.00 72.36  ? 337  LYS B N   1 
ATOM   2688  C CA  . LYS A 1 354  ? 218.176 216.486 281.002 1.00 72.36  ? 337  LYS B CA  1 
ATOM   2689  C C   . LYS A 1 354  ? 216.869 216.134 281.697 1.00 72.36  ? 337  LYS B C   1 
ATOM   2690  O O   . LYS A 1 354  ? 216.601 214.956 281.961 1.00 72.36  ? 337  LYS B O   1 
ATOM   2691  C CB  . LYS A 1 354  ? 219.225 216.914 282.025 1.00 72.36  ? 337  LYS B CB  1 
ATOM   2692  C CG  . LYS A 1 354  ? 219.258 218.398 282.287 1.00 72.36  ? 337  LYS B CG  1 
ATOM   2693  C CD  . LYS A 1 354  ? 220.491 218.780 283.075 1.00 72.36  ? 337  LYS B CD  1 
ATOM   2694  C CE  . LYS A 1 354  ? 221.752 218.575 282.260 1.00 72.36  ? 337  LYS B CE  1 
ATOM   2695  N NZ  . LYS A 1 354  ? 222.958 218.489 283.128 1.00 72.36  ? 337  LYS B NZ  1 
ATOM   2696  N N   . PHE A 1 355  ? 216.044 217.134 282.009 1.00 70.21  ? 338  PHE B N   1 
ATOM   2697  C CA  . PHE A 1 355  ? 214.763 216.830 282.634 1.00 70.21  ? 338  PHE B CA  1 
ATOM   2698  C C   . PHE A 1 355  ? 213.842 216.098 281.672 1.00 70.21  ? 338  PHE B C   1 
ATOM   2699  O O   . PHE A 1 355  ? 213.067 215.236 282.090 1.00 70.21  ? 338  PHE B O   1 
ATOM   2700  C CB  . PHE A 1 355  ? 214.075 218.091 283.138 1.00 70.21  ? 338  PHE B CB  1 
ATOM   2701  C CG  . PHE A 1 355  ? 212.637 217.869 283.485 1.00 70.21  ? 338  PHE B CG  1 
ATOM   2702  C CD1 . PHE A 1 355  ? 212.295 217.158 284.620 1.00 70.21  ? 338  PHE B CD1 1 
ATOM   2703  C CD2 . PHE A 1 355  ? 211.629 218.328 282.661 1.00 70.21  ? 338  PHE B CD2 1 
ATOM   2704  C CE1 . PHE A 1 355  ? 210.974 216.933 284.942 1.00 70.21  ? 338  PHE B CE1 1 
ATOM   2705  C CE2 . PHE A 1 355  ? 210.307 218.101 282.977 1.00 70.21  ? 338  PHE B CE2 1 
ATOM   2706  C CZ  . PHE A 1 355  ? 209.979 217.406 284.120 1.00 70.21  ? 338  PHE B CZ  1 
ATOM   2707  N N   . ASP A 1 356  ? 213.890 216.442 280.385 1.00 74.14  ? 339  ASP B N   1 
ATOM   2708  C CA  . ASP A 1 356  ? 213.107 215.707 279.400 1.00 74.14  ? 339  ASP B CA  1 
ATOM   2709  C C   . ASP A 1 356  ? 213.543 214.248 279.380 1.00 74.14  ? 339  ASP B C   1 
ATOM   2710  O O   . ASP A 1 356  ? 212.704 213.340 279.378 1.00 74.14  ? 339  ASP B O   1 
ATOM   2711  C CB  . ASP A 1 356  ? 213.263 216.392 278.032 1.00 74.14  ? 339  ASP B CB  1 
ATOM   2712  C CG  . ASP A 1 356  ? 212.959 215.488 276.823 1.00 74.14  ? 339  ASP B CG  1 
ATOM   2713  O OD1 . ASP A 1 356  ? 212.527 214.326 276.942 1.00 74.14  ? 339  ASP B OD1 1 
ATOM   2714  O OD2 . ASP A 1 356  ? 213.172 215.978 275.694 1.00 74.14  ? 339  ASP B OD2 1 
ATOM   2715  N N   . LYS A 1 357  ? 214.855 214.006 279.401 1.00 73.73  ? 340  LYS B N   1 
ATOM   2716  C CA  . LYS A 1 357  ? 215.360 212.637 279.424 1.00 73.73  ? 340  LYS B CA  1 
ATOM   2717  C C   . LYS A 1 357  ? 214.890 211.894 280.669 1.00 73.73  ? 340  LYS B C   1 
ATOM   2718  O O   . LYS A 1 357  ? 214.427 210.750 280.588 1.00 73.73  ? 340  LYS B O   1 
ATOM   2719  C CB  . LYS A 1 357  ? 216.886 212.649 279.349 1.00 73.73  ? 340  LYS B CB  1 
ATOM   2720  C CG  . LYS A 1 357  ? 217.522 211.277 279.362 1.00 73.73  ? 340  LYS B CG  1 
ATOM   2721  C CD  . LYS A 1 357  ? 219.038 211.373 279.370 1.00 73.73  ? 340  LYS B CD  1 
ATOM   2722  C CE  . LYS A 1 357  ? 219.664 210.173 280.059 1.00 73.73  ? 340  LYS B CE  1 
ATOM   2723  N NZ  . LYS A 1 357  ? 219.946 210.451 281.494 1.00 73.73  ? 340  LYS B NZ  1 
ATOM   2724  N N   . LEU A 1 358  ? 214.992 212.539 281.834 1.00 69.60  ? 341  LEU B N   1 
ATOM   2725  C CA  . LEU A 1 358  ? 214.594 211.891 283.081 1.00 69.60  ? 341  LEU B CA  1 
ATOM   2726  C C   . LEU A 1 358  ? 213.098 211.602 283.109 1.00 69.60  ? 341  LEU B C   1 
ATOM   2727  O O   . LEU A 1 358  ? 212.675 210.527 283.547 1.00 69.60  ? 341  LEU B O   1 
ATOM   2728  C CB  . LEU A 1 358  ? 214.987 212.760 284.274 1.00 69.60  ? 341  LEU B CB  1 
ATOM   2729  C CG  . LEU A 1 358  ? 214.477 212.281 285.632 1.00 69.60  ? 341  LEU B CG  1 
ATOM   2730  C CD1 . LEU A 1 358  ? 215.121 210.963 286.008 1.00 69.60  ? 341  LEU B CD1 1 
ATOM   2731  C CD2 . LEU A 1 358  ? 214.733 213.323 286.698 1.00 69.60  ? 341  LEU B CD2 1 
ATOM   2732  N N   . TYR A 1 359  ? 212.284 212.555 282.658 1.00 69.60  ? 342  TYR B N   1 
ATOM   2733  C CA  . TYR A 1 359  ? 210.842 212.356 282.629 1.00 69.60  ? 342  TYR B CA  1 
ATOM   2734  C C   . TYR A 1 359  ? 210.462 211.237 281.672 1.00 69.60  ? 342  TYR B C   1 
ATOM   2735  O O   . TYR A 1 359  ? 209.605 210.406 281.988 1.00 69.60  ? 342  TYR B O   1 
ATOM   2736  C CB  . TYR A 1 359  ? 210.153 213.661 282.236 1.00 69.60  ? 342  TYR B CB  1 
ATOM   2737  C CG  . TYR A 1 359  ? 208.679 213.706 282.535 1.00 69.60  ? 342  TYR B CG  1 
ATOM   2738  C CD1 . TYR A 1 359  ? 207.757 213.187 281.640 1.00 69.60  ? 342  TYR B CD1 1 
ATOM   2739  C CD2 . TYR A 1 359  ? 208.207 214.276 283.703 1.00 69.60  ? 342  TYR B CD2 1 
ATOM   2740  C CE1 . TYR A 1 359  ? 206.407 213.225 281.905 1.00 69.60  ? 342  TYR B CE1 1 
ATOM   2741  C CE2 . TYR A 1 359  ? 206.860 214.319 283.977 1.00 69.60  ? 342  TYR B CE2 1 
ATOM   2742  C CZ  . TYR A 1 359  ? 205.964 213.793 283.073 1.00 69.60  ? 342  TYR B CZ  1 
ATOM   2743  O OH  . TYR A 1 359  ? 204.615 213.832 283.338 1.00 69.60  ? 342  TYR B OH  1 
ATOM   2744  N N   . LYS A 1 360  ? 211.092 211.198 280.496 1.00 69.60  ? 343  LYS B N   1 
ATOM   2745  C CA  . LYS A 1 360  ? 210.810 210.128 279.548 1.00 69.60  ? 343  LYS B CA  1 
ATOM   2746  C C   . LYS A 1 360  ? 211.209 208.775 280.116 1.00 69.60  ? 343  LYS B C   1 
ATOM   2747  O O   . LYS A 1 360  ? 210.510 207.777 279.911 1.00 69.60  ? 343  LYS B O   1 
ATOM   2748  C CB  . LYS A 1 360  ? 211.532 210.394 278.229 1.00 69.60  ? 343  LYS B CB  1 
ATOM   2749  C CG  . LYS A 1 360  ? 211.432 209.260 277.227 1.00 69.60  ? 343  LYS B CG  1 
ATOM   2750  C CD  . LYS A 1 360  ? 212.167 209.594 275.940 1.00 69.60  ? 343  LYS B CD  1 
ATOM   2751  C CE  . LYS A 1 360  ? 211.933 211.037 275.524 1.00 69.60  ? 343  LYS B CE  1 
ATOM   2752  N NZ  . LYS A 1 360  ? 212.780 211.431 274.366 1.00 69.60  ? 343  LYS B NZ  1 
ATOM   2753  N N   . MET A 1 361  ? 212.333 208.719 280.831 1.00 69.60  ? 344  MET B N   1 
ATOM   2754  C CA  . MET A 1 361  ? 212.737 207.463 281.450 1.00 69.60  ? 344  MET B CA  1 
ATOM   2755  C C   . MET A 1 361  ? 211.744 207.026 282.518 1.00 69.60  ? 344  MET B C   1 
ATOM   2756  O O   . MET A 1 361  ? 211.322 205.866 282.541 1.00 69.60  ? 344  MET B O   1 
ATOM   2757  C CB  . MET A 1 361  ? 214.138 207.594 282.042 1.00 69.60  ? 344  MET B CB  1 
ATOM   2758  C CG  . MET A 1 361  ? 214.619 206.350 282.757 1.00 69.60  ? 344  MET B CG  1 
ATOM   2759  S SD  . MET A 1 361  ? 216.130 206.601 283.704 1.00 69.60  ? 344  MET B SD  1 
ATOM   2760  C CE  . MET A 1 361  ? 216.460 208.334 283.401 1.00 69.60  ? 344  MET B CE  1 
ATOM   2761  N N   . LEU A 1 362  ? 211.346 207.943 283.401 1.00 69.60  ? 345  LEU B N   1 
ATOM   2762  C CA  . LEU A 1 362  ? 210.462 207.579 284.502 1.00 69.60  ? 345  LEU B CA  1 
ATOM   2763  C C   . LEU A 1 362  ? 209.032 207.327 284.050 1.00 69.60  ? 345  LEU B C   1 
ATOM   2764  O O   . LEU A 1 362  ? 208.269 206.692 284.784 1.00 69.60  ? 345  LEU B O   1 
ATOM   2765  C CB  . LEU A 1 362  ? 210.471 208.671 285.570 1.00 69.60  ? 345  LEU B CB  1 
ATOM   2766  C CG  . LEU A 1 362  ? 211.610 208.635 286.582 1.00 69.60  ? 345  LEU B CG  1 
ATOM   2767  C CD1 . LEU A 1 362  ? 211.540 209.850 287.479 1.00 69.60  ? 345  LEU B CD1 1 
ATOM   2768  C CD2 . LEU A 1 362  ? 211.549 207.365 287.398 1.00 69.60  ? 345  LEU B CD2 1 
ATOM   2769  N N   . THR A 1 363  ? 208.648 207.807 282.871 1.00 69.60  ? 346  THR B N   1 
ATOM   2770  C CA  . THR A 1 363  ? 207.278 207.690 282.393 1.00 69.60  ? 346  THR B CA  1 
ATOM   2771  C C   . THR A 1 363  ? 207.116 206.662 281.285 1.00 69.60  ? 346  THR B C   1 
ATOM   2772  O O   . THR A 1 363  ? 206.206 205.831 281.342 1.00 69.60  ? 346  THR B O   1 
ATOM   2773  C CB  . THR A 1 363  ? 206.783 209.058 281.906 1.00 69.60  ? 346  THR B CB  1 
ATOM   2774  O OG1 . THR A 1 363  ? 206.753 209.973 283.007 1.00 69.60  ? 346  THR B OG1 1 
ATOM   2775  C CG2 . THR A 1 363  ? 205.396 208.943 281.311 1.00 69.60  ? 346  THR B CG2 1 
ATOM   2776  N N   . GLU A 1 364  ? 207.981 206.689 280.274 1.00 70.19  ? 347  GLU B N   1 
ATOM   2777  C CA  . GLU A 1 364  ? 207.840 205.822 279.112 1.00 70.19  ? 347  GLU B CA  1 
ATOM   2778  C C   . GLU A 1 364  ? 208.732 204.590 279.166 1.00 70.19  ? 347  GLU B C   1 
ATOM   2779  O O   . GLU A 1 364  ? 208.304 203.509 278.754 1.00 70.19  ? 347  GLU B O   1 
ATOM   2780  C CB  . GLU A 1 364  ? 208.139 206.608 277.834 1.00 70.19  ? 347  GLU B CB  1 
ATOM   2781  C CG  . GLU A 1 364  ? 207.435 207.950 277.765 1.00 70.19  ? 347  GLU B CG  1 
ATOM   2782  C CD  . GLU A 1 364  ? 207.041 208.331 276.354 1.00 70.19  ? 347  GLU B CD  1 
ATOM   2783  O OE1 . GLU A 1 364  ? 207.840 208.087 275.425 1.00 70.19  ? 347  GLU B OE1 1 
ATOM   2784  O OE2 . GLU A 1 364  ? 205.934 208.877 276.172 1.00 70.19  ? 347  GLU B OE2 1 
ATOM   2785  N N   . ILE A 1 365  ? 209.966 204.724 279.653 1.00 70.98  ? 348  ILE B N   1 
ATOM   2786  C CA  . ILE A 1 365  ? 210.864 203.574 279.706 1.00 70.98  ? 348  ILE B CA  1 
ATOM   2787  C C   . ILE A 1 365  ? 210.406 202.581 280.767 1.00 70.98  ? 348  ILE B C   1 
ATOM   2788  O O   . ILE A 1 365  ? 210.378 201.368 280.528 1.00 70.98  ? 348  ILE B O   1 
ATOM   2789  C CB  . ILE A 1 365  ? 212.310 204.036 279.951 1.00 70.98  ? 348  ILE B CB  1 
ATOM   2790  C CG1 . ILE A 1 365  ? 212.761 204.977 278.836 1.00 70.98  ? 348  ILE B CG1 1 
ATOM   2791  C CG2 . ILE A 1 365  ? 213.239 202.842 280.044 1.00 70.98  ? 348  ILE B CG2 1 
ATOM   2792  C CD1 . ILE A 1 365  ? 212.546 204.431 277.451 1.00 70.98  ? 348  ILE B CD1 1 
ATOM   2793  N N   . TYR A 1 366  ? 210.040 203.071 281.950 1.00 69.60  ? 349  TYR B N   1 
ATOM   2794  C CA  . TYR A 1 366  ? 209.575 202.216 283.041 1.00 69.60  ? 349  TYR B CA  1 
ATOM   2795  C C   . TYR A 1 366  ? 208.085 201.978 282.848 1.00 69.60  ? 349  TYR B C   1 
ATOM   2796  O O   . TYR A 1 366  ? 207.245 202.737 283.329 1.00 69.60  ? 349  TYR B O   1 
ATOM   2797  C CB  . TYR A 1 366  ? 209.854 202.852 284.396 1.00 69.60  ? 349  TYR B CB  1 
ATOM   2798  C CG  . TYR A 1 366  ? 211.311 203.045 284.724 1.00 69.60  ? 349  TYR B CG  1 
ATOM   2799  C CD1 . TYR A 1 366  ? 212.304 202.473 283.948 1.00 69.60  ? 349  TYR B CD1 1 
ATOM   2800  C CD2 . TYR A 1 366  ? 211.693 203.803 285.818 1.00 69.60  ? 349  TYR B CD2 1 
ATOM   2801  C CE1 . TYR A 1 366  ? 213.635 202.655 284.251 1.00 69.60  ? 349  TYR B CE1 1 
ATOM   2802  C CE2 . TYR A 1 366  ? 213.019 203.988 286.128 1.00 69.60  ? 349  TYR B CE2 1 
ATOM   2803  C CZ  . TYR A 1 366  ? 213.985 203.412 285.342 1.00 69.60  ? 349  TYR B CZ  1 
ATOM   2804  O OH  . TYR A 1 366  ? 215.310 203.596 285.652 1.00 69.60  ? 349  TYR B OH  1 
ATOM   2805  N N   . THR A 1 367  ? 207.749 200.910 282.132 1.00 69.60  ? 350  THR B N   1 
ATOM   2806  C CA  . THR A 1 367  ? 206.360 200.551 281.907 1.00 69.60  ? 350  THR B CA  1 
ATOM   2807  C C   . THR A 1 367  ? 206.213 199.044 282.026 1.00 69.60  ? 350  THR B C   1 
ATOM   2808  O O   . THR A 1 367  ? 207.168 198.290 281.832 1.00 69.60  ? 350  THR B O   1 
ATOM   2809  C CB  . THR A 1 367  ? 205.865 201.028 280.539 1.00 69.60  ? 350  THR B CB  1 
ATOM   2810  O OG1 . THR A 1 367  ? 206.923 200.912 279.582 1.00 69.60  ? 350  THR B OG1 1 
ATOM   2811  C CG2 . THR A 1 367  ? 205.419 202.475 280.616 1.00 69.60  ? 350  THR B CG2 1 
ATOM   2812  N N   . GLU A 1 368  ? 204.997 198.610 282.357 1.00 70.33  ? 351  GLU B N   1 
ATOM   2813  C CA  . GLU A 1 368  ? 204.751 197.185 282.531 1.00 70.33  ? 351  GLU B CA  1 
ATOM   2814  C C   . GLU A 1 368  ? 204.922 196.420 281.225 1.00 70.33  ? 351  GLU B C   1 
ATOM   2815  O O   . GLU A 1 368  ? 205.365 195.267 281.240 1.00 70.33  ? 351  GLU B O   1 
ATOM   2816  C CB  . GLU A 1 368  ? 203.354 196.960 283.102 1.00 70.33  ? 351  GLU B CB  1 
ATOM   2817  C CG  . GLU A 1 368  ? 203.025 195.506 283.363 1.00 70.33  ? 351  GLU B CG  1 
ATOM   2818  C CD  . GLU A 1 368  ? 201.749 195.329 284.157 1.00 70.33  ? 351  GLU B CD  1 
ATOM   2819  O OE1 . GLU A 1 368  ? 201.539 196.089 285.124 1.00 70.33  ? 351  GLU B OE1 1 
ATOM   2820  O OE2 . GLU A 1 368  ? 200.957 194.426 283.816 1.00 70.33  ? 351  GLU B OE2 1 
ATOM   2821  N N   . ASP A 1 369  ? 204.579 197.036 280.091 1.00 72.76  ? 352  ASP B N   1 
ATOM   2822  C CA  . ASP A 1 369  ? 204.735 196.354 278.810 1.00 72.76  ? 352  ASP B CA  1 
ATOM   2823  C C   . ASP A 1 369  ? 206.202 196.087 278.497 1.00 72.76  ? 352  ASP B C   1 
ATOM   2824  O O   . ASP A 1 369  ? 206.551 195.017 277.984 1.00 72.76  ? 352  ASP B O   1 
ATOM   2825  C CB  . ASP A 1 369  ? 204.091 197.174 277.696 1.00 72.76  ? 352  ASP B CB  1 
ATOM   2826  C CG  . ASP A 1 369  ? 203.461 196.306 276.631 1.00 72.76  ? 352  ASP B CG  1 
ATOM   2827  O OD1 . ASP A 1 369  ? 202.806 195.306 276.992 1.00 72.76  ? 352  ASP B OD1 1 
ATOM   2828  O OD2 . ASP A 1 369  ? 203.621 196.619 275.434 1.00 72.76  ? 352  ASP B OD2 1 
ATOM   2829  N N   . ASN A 1 370  ? 207.074 197.053 278.786 1.00 69.77  ? 353  ASN B N   1 
ATOM   2830  C CA  . ASN A 1 370  ? 208.501 196.843 278.572 1.00 69.77  ? 353  ASN B CA  1 
ATOM   2831  C C   . ASN A 1 370  ? 209.030 195.728 279.463 1.00 69.77  ? 353  ASN B C   1 
ATOM   2832  O O   . ASN A 1 370  ? 209.853 194.914 279.031 1.00 69.77  ? 353  ASN B O   1 
ATOM   2833  C CB  . ASN A 1 370  ? 209.263 198.142 278.819 1.00 69.77  ? 353  ASN B CB  1 
ATOM   2834  C CG  . ASN A 1 370  ? 209.147 199.110 277.666 1.00 69.77  ? 353  ASN B CG  1 
ATOM   2835  O OD1 . ASN A 1 370  ? 208.944 198.707 276.523 1.00 69.77  ? 353  ASN B OD1 1 
ATOM   2836  N ND2 . ASN A 1 370  ? 209.274 200.397 277.959 1.00 69.77  ? 353  ASN B ND2 1 
ATOM   2837  N N   . PHE A 1 371  ? 208.571 195.677 280.713 1.00 69.60  ? 354  PHE B N   1 
ATOM   2838  C CA  . PHE A 1 371  ? 208.965 194.587 281.597 1.00 69.60  ? 354  PHE B CA  1 
ATOM   2839  C C   . PHE A 1 371  ? 208.480 193.248 281.065 1.00 69.60  ? 354  PHE B C   1 
ATOM   2840  O O   . PHE A 1 371  ? 209.187 192.241 281.165 1.00 69.60  ? 354  PHE B O   1 
ATOM   2841  C CB  . PHE A 1 371  ? 208.424 194.829 283.002 1.00 69.60  ? 354  PHE B CB  1 
ATOM   2842  C CG  . PHE A 1 371  ? 209.381 195.543 283.899 1.00 69.60  ? 354  PHE B CG  1 
ATOM   2843  C CD1 . PHE A 1 371  ? 210.467 194.882 284.433 1.00 69.60  ? 354  PHE B CD1 1 
ATOM   2844  C CD2 . PHE A 1 371  ? 209.199 196.876 284.203 1.00 69.60  ? 354  PHE B CD2 1 
ATOM   2845  C CE1 . PHE A 1 371  ? 211.348 195.534 285.257 1.00 69.60  ? 354  PHE B CE1 1 
ATOM   2846  C CE2 . PHE A 1 371  ? 210.078 197.533 285.026 1.00 69.60  ? 354  PHE B CE2 1 
ATOM   2847  C CZ  . PHE A 1 371  ? 211.155 196.861 285.553 1.00 69.60  ? 354  PHE B CZ  1 
ATOM   2848  N N   . VAL A 1 372  ? 207.269 193.214 280.506 1.00 71.76  ? 355  VAL B N   1 
ATOM   2849  C CA  . VAL A 1 372  ? 206.754 191.979 279.922 1.00 71.76  ? 355  VAL B CA  1 
ATOM   2850  C C   . VAL A 1 372  ? 207.625 191.543 278.753 1.00 71.76  ? 355  VAL B C   1 
ATOM   2851  O O   . VAL A 1 372  ? 207.957 190.360 278.611 1.00 71.76  ? 355  VAL B O   1 
ATOM   2852  C CB  . VAL A 1 372  ? 205.287 192.166 279.499 1.00 71.76  ? 355  VAL B CB  1 
ATOM   2853  C CG1 . VAL A 1 372  ? 204.904 191.150 278.438 1.00 71.76  ? 355  VAL B CG1 1 
ATOM   2854  C CG2 . VAL A 1 372  ? 204.376 192.057 280.703 1.00 71.76  ? 355  VAL B CG2 1 
ATOM   2855  N N   . LYS A 1 373  ? 208.011 192.493 277.898 1.00 74.80  ? 356  LYS B N   1 
ATOM   2856  C CA  . LYS A 1 373  ? 208.865 192.165 276.760 1.00 74.80  ? 356  LYS B CA  1 
ATOM   2857  C C   . LYS A 1 373  ? 210.227 191.657 277.214 1.00 74.80  ? 356  LYS B C   1 
ATOM   2858  O O   . LYS A 1 373  ? 210.766 190.704 276.639 1.00 74.80  ? 356  LYS B O   1 
ATOM   2859  C CB  . LYS A 1 373  ? 209.025 193.383 275.852 1.00 74.80  ? 356  LYS B CB  1 
ATOM   2860  C CG  . LYS A 1 373  ? 207.948 193.506 274.792 1.00 74.80  ? 356  LYS B CG  1 
ATOM   2861  C CD  . LYS A 1 373  ? 207.514 194.948 274.617 1.00 74.80  ? 356  LYS B CD  1 
ATOM   2862  C CE  . LYS A 1 373  ? 208.687 195.825 274.223 1.00 74.80  ? 356  LYS B CE  1 
ATOM   2863  N NZ  . LYS A 1 373  ? 208.952 195.763 272.760 1.00 74.80  ? 356  LYS B NZ  1 
ATOM   2864  N N   . PHE A 1 374  ? 210.806 192.286 278.238 1.00 75.51  ? 357  PHE B N   1 
ATOM   2865  C CA  . PHE A 1 374  ? 212.109 191.847 278.729 1.00 75.51  ? 357  PHE B CA  1 
ATOM   2866  C C   . PHE A 1 374  ? 212.027 190.471 279.378 1.00 75.51  ? 357  PHE B C   1 
ATOM   2867  O O   . PHE A 1 374  ? 212.916 189.635 279.184 1.00 75.51  ? 357  PHE B O   1 
ATOM   2868  C CB  . PHE A 1 374  ? 212.673 192.872 279.710 1.00 75.51  ? 357  PHE B CB  1 
ATOM   2869  C CG  . PHE A 1 374  ? 213.504 193.936 279.058 1.00 75.51  ? 357  PHE B CG  1 
ATOM   2870  C CD1 . PHE A 1 374  ? 214.860 193.751 278.863 1.00 75.51  ? 357  PHE B CD1 1 
ATOM   2871  C CD2 . PHE A 1 374  ? 212.930 195.121 278.636 1.00 75.51  ? 357  PHE B CD2 1 
ATOM   2872  C CE1 . PHE A 1 374  ? 215.627 194.727 278.263 1.00 75.51  ? 357  PHE B CE1 1 
ATOM   2873  C CE2 . PHE A 1 374  ? 213.691 196.101 278.035 1.00 75.51  ? 357  PHE B CE2 1 
ATOM   2874  C CZ  . PHE A 1 374  ? 215.040 195.905 277.849 1.00 75.51  ? 357  PHE B CZ  1 
ATOM   2875  N N   . PHE A 1 375  ? 210.973 190.217 280.155 1.00 73.21  ? 358  PHE B N   1 
ATOM   2876  C CA  . PHE A 1 375  ? 210.809 188.926 280.810 1.00 73.21  ? 358  PHE B CA  1 
ATOM   2877  C C   . PHE A 1 375  ? 210.356 187.834 279.854 1.00 73.21  ? 358  PHE B C   1 
ATOM   2878  O O   . PHE A 1 375  ? 210.532 186.651 280.164 1.00 73.21  ? 358  PHE B O   1 
ATOM   2879  C CB  . PHE A 1 375  ? 209.804 189.038 281.957 1.00 73.21  ? 358  PHE B CB  1 
ATOM   2880  C CG  . PHE A 1 375  ? 210.310 189.813 283.135 1.00 73.21  ? 358  PHE B CG  1 
ATOM   2881  C CD1 . PHE A 1 375  ? 211.656 189.836 283.440 1.00 73.21  ? 358  PHE B CD1 1 
ATOM   2882  C CD2 . PHE A 1 375  ? 209.437 190.518 283.941 1.00 73.21  ? 358  PHE B CD2 1 
ATOM   2883  C CE1 . PHE A 1 375  ? 212.121 190.547 284.526 1.00 73.21  ? 358  PHE B CE1 1 
ATOM   2884  C CE2 . PHE A 1 375  ? 209.897 191.231 285.026 1.00 73.21  ? 358  PHE B CE2 1 
ATOM   2885  C CZ  . PHE A 1 375  ? 211.240 191.245 285.318 1.00 73.21  ? 358  PHE B CZ  1 
ATOM   2886  N N   . LYS A 1 376  ? 209.788 188.201 278.707 1.00 78.93  ? 359  LYS B N   1 
ATOM   2887  C CA  . LYS A 1 376  ? 209.255 187.251 277.732 1.00 78.93  ? 359  LYS B CA  1 
ATOM   2888  C C   . LYS A 1 376  ? 208.229 186.320 278.380 1.00 78.93  ? 359  LYS B C   1 
ATOM   2889  O O   . LYS A 1 376  ? 208.377 185.097 278.405 1.00 78.93  ? 359  LYS B O   1 
ATOM   2890  C CB  . LYS A 1 376  ? 210.383 186.457 277.067 1.00 78.93  ? 359  LYS B CB  1 
ATOM   2891  C CG  . LYS A 1 376  ? 211.641 187.264 276.789 1.00 78.93  ? 359  LYS B CG  1 
ATOM   2892  C CD  . LYS A 1 376  ? 212.878 186.381 276.807 1.00 78.93  ? 359  LYS B CD  1 
ATOM   2893  C CE  . LYS A 1 376  ? 214.150 187.212 276.822 1.00 78.93  ? 359  LYS B CE  1 
ATOM   2894  N NZ  . LYS A 1 376  ? 214.335 187.968 275.554 1.00 78.93  ? 359  LYS B NZ  1 
ATOM   2895  N N   . VAL A 1 377  ? 207.174 186.932 278.918 1.00 78.15  ? 360  VAL B N   1 
ATOM   2896  C CA  . VAL A 1 377  ? 206.086 186.208 279.559 1.00 78.15  ? 360  VAL B CA  1 
ATOM   2897  C C   . VAL A 1 377  ? 204.761 186.771 279.064 1.00 78.15  ? 360  VAL B C   1 
ATOM   2898  O O   . VAL A 1 377  ? 204.692 187.873 278.518 1.00 78.15  ? 360  VAL B O   1 
ATOM   2899  C CB  . VAL A 1 377  ? 206.158 186.286 281.097 1.00 78.15  ? 360  VAL B CB  1 
ATOM   2900  C CG1 . VAL A 1 377  ? 207.385 185.556 281.609 1.00 78.15  ? 360  VAL B CG1 1 
ATOM   2901  C CG2 . VAL A 1 377  ? 206.165 187.730 281.548 1.00 78.15  ? 360  VAL B CG2 1 
ATOM   2902  N N   . LEU A 1 378  ? 203.704 185.989 279.256 1.00 83.81  ? 361  LEU B N   1 
ATOM   2903  C CA  . LEU A 1 378  ? 202.366 186.422 278.886 1.00 83.81  ? 361  LEU B CA  1 
ATOM   2904  C C   . LEU A 1 378  ? 201.815 187.435 279.878 1.00 83.81  ? 361  LEU B C   1 
ATOM   2905  O O   . LEU A 1 378  ? 202.111 187.398 281.075 1.00 83.81  ? 361  LEU B O   1 
ATOM   2906  C CB  . LEU A 1 378  ? 201.409 185.233 278.792 1.00 83.81  ? 361  LEU B CB  1 
ATOM   2907  C CG  . LEU A 1 378  ? 201.216 184.579 277.425 1.00 83.81  ? 361  LEU B CG  1 
ATOM   2908  C CD1 . LEU A 1 378  ? 200.283 185.428 276.585 1.00 83.81  ? 361  LEU B CD1 1 
ATOM   2909  C CD2 . LEU A 1 378  ? 202.532 184.413 276.714 1.00 83.81  ? 361  LEU B CD2 1 
ATOM   2910  N N   . ASN A 1 379  ? 201.007 188.351 279.356 1.00 83.32  ? 362  ASN B N   1 
ATOM   2911  C CA  . ASN A 1 379  ? 200.251 189.285 280.175 1.00 83.32  ? 362  ASN B CA  1 
ATOM   2912  C C   . ASN A 1 379  ? 199.115 189.834 279.329 1.00 83.32  ? 362  ASN B C   1 
ATOM   2913  O O   . ASN A 1 379  ? 199.139 189.754 278.099 1.00 83.32  ? 362  ASN B O   1 
ATOM   2914  C CB  . ASN A 1 379  ? 201.133 190.418 280.706 1.00 83.32  ? 362  ASN B CB  1 
ATOM   2915  C CG  . ASN A 1 379  ? 200.479 191.181 281.839 1.00 83.32  ? 362  ASN B CG  1 
ATOM   2916  O OD1 . ASN A 1 379  ? 199.321 191.586 281.743 1.00 83.32  ? 362  ASN B OD1 1 
ATOM   2917  N ND2 . ASN A 1 379  ? 201.215 191.376 282.922 1.00 83.32  ? 362  ASN B ND2 1 
ATOM   2918  N N   . ALA A 1 380  ? 198.113 190.385 280.006 1.00 82.78  ? 363  ALA B N   1 
ATOM   2919  C CA  . ALA A 1 380  ? 197.010 191.028 279.308 1.00 82.78  ? 363  ALA B CA  1 
ATOM   2920  C C   . ALA A 1 380  ? 197.528 192.263 278.583 1.00 82.78  ? 363  ALA B C   1 
ATOM   2921  O O   . ALA A 1 380  ? 198.033 193.195 279.217 1.00 82.78  ? 363  ALA B O   1 
ATOM   2922  C CB  . ALA A 1 380  ? 195.906 191.400 280.292 1.00 82.78  ? 363  ALA B CB  1 
ATOM   2923  N N   . LYS A 1 381  ? 197.409 192.268 277.253 1.00 83.07  ? 364  LYS B N   1 
ATOM   2924  C CA  . LYS A 1 381  ? 197.945 193.376 276.470 1.00 83.07  ? 364  LYS B CA  1 
ATOM   2925  C C   . LYS A 1 381  ? 197.252 194.688 276.804 1.00 83.07  ? 364  LYS B C   1 
ATOM   2926  O O   . LYS A 1 381  ? 197.833 195.763 276.615 1.00 83.07  ? 364  LYS B O   1 
ATOM   2927  C CB  . LYS A 1 381  ? 197.822 193.075 274.976 1.00 83.07  ? 364  LYS B CB  1 
ATOM   2928  C CG  . LYS A 1 381  ? 198.249 191.670 274.584 1.00 83.07  ? 364  LYS B CG  1 
ATOM   2929  C CD  . LYS A 1 381  ? 199.731 191.431 274.842 1.00 83.07  ? 364  LYS B CD  1 
ATOM   2930  C CE  . LYS A 1 381  ? 200.595 192.555 274.291 1.00 83.07  ? 364  LYS B CE  1 
ATOM   2931  N NZ  . LYS A 1 381  ? 201.949 192.559 274.910 1.00 83.07  ? 364  LYS B NZ  1 
ATOM   2932  N N   . THR A 1 382  ? 196.021 194.625 277.299 1.00 79.36  ? 365  THR B N   1 
ATOM   2933  C CA  . THR A 1 382  ? 195.293 195.812 277.714 1.00 79.36  ? 365  THR B CA  1 
ATOM   2934  C C   . THR A 1 382  ? 194.591 195.519 279.030 1.00 79.36  ? 365  THR B C   1 
ATOM   2935  O O   . THR A 1 382  ? 194.344 194.363 279.381 1.00 79.36  ? 365  THR B O   1 
ATOM   2936  C CB  . THR A 1 382  ? 194.283 196.258 276.649 1.00 79.36  ? 365  THR B CB  1 
ATOM   2937  O OG1 . THR A 1 382  ? 193.741 197.536 277.005 1.00 79.36  ? 365  THR B OG1 1 
ATOM   2938  C CG2 . THR A 1 382  ? 193.157 195.245 276.524 1.00 79.36  ? 365  THR B CG2 1 
ATOM   2939  N N   . PHE A 1 383  ? 194.278 196.585 279.767 1.00 76.29  ? 366  PHE B N   1 
ATOM   2940  C CA  . PHE A 1 383  ? 193.611 196.422 281.053 1.00 76.29  ? 366  PHE B CA  1 
ATOM   2941  C C   . PHE A 1 383  ? 192.199 195.874 280.908 1.00 76.29  ? 366  PHE B C   1 
ATOM   2942  O O   . PHE A 1 383  ? 191.622 195.418 281.899 1.00 76.29  ? 366  PHE B O   1 
ATOM   2943  C CB  . PHE A 1 383  ? 193.577 197.753 281.806 1.00 76.29  ? 366  PHE B CB  1 
ATOM   2944  C CG  . PHE A 1 383  ? 192.704 198.794 281.166 1.00 76.29  ? 366  PHE B CG  1 
ATOM   2945  C CD1 . PHE A 1 383  ? 193.150 199.519 280.077 1.00 76.29  ? 366  PHE B CD1 1 
ATOM   2946  C CD2 . PHE A 1 383  ? 191.442 199.055 281.661 1.00 76.29  ? 366  PHE B CD2 1 
ATOM   2947  C CE1 . PHE A 1 383  ? 192.355 200.477 279.492 1.00 76.29  ? 366  PHE B CE1 1 
ATOM   2948  C CE2 . PHE A 1 383  ? 190.642 200.014 281.079 1.00 76.29  ? 366  PHE B CE2 1 
ATOM   2949  C CZ  . PHE A 1 383  ? 191.100 200.724 279.993 1.00 76.29  ? 366  PHE B CZ  1 
ATOM   2950  N N   . LEU A 1 384  ? 191.632 195.910 279.701 1.00 78.30  ? 367  LEU B N   1 
ATOM   2951  C CA  . LEU A 1 384  ? 190.280 195.399 279.501 1.00 78.30  ? 367  LEU B CA  1 
ATOM   2952  C C   . LEU A 1 384  ? 190.218 193.887 279.651 1.00 78.30  ? 367  LEU B C   1 
ATOM   2953  O O   . LEU A 1 384  ? 189.180 193.350 280.050 1.00 78.30  ? 367  LEU B O   1 
ATOM   2954  C CB  . LEU A 1 384  ? 189.761 195.814 278.127 1.00 78.30  ? 367  LEU B CB  1 
ATOM   2955  C CG  . LEU A 1 384  ? 189.215 197.236 278.006 1.00 78.30  ? 367  LEU B CG  1 
ATOM   2956  C CD1 . LEU A 1 384  ? 188.181 197.304 276.902 1.00 78.30  ? 367  LEU B CD1 1 
ATOM   2957  C CD2 . LEU A 1 384  ? 188.621 197.699 279.323 1.00 78.30  ? 367  LEU B CD2 1 
ATOM   2958  N N   . ASN A 1 385  ? 191.308 193.184 279.344 1.00 78.36  ? 368  ASN B N   1 
ATOM   2959  C CA  . ASN A 1 385  ? 191.345 191.727 279.461 1.00 78.36  ? 368  ASN B CA  1 
ATOM   2960  C C   . ASN A 1 385  ? 191.403 191.382 280.946 1.00 78.36  ? 368  ASN B C   1 
ATOM   2961  O O   . ASN A 1 385  ? 192.463 191.138 281.527 1.00 78.36  ? 368  ASN B O   1 
ATOM   2962  C CB  . ASN A 1 385  ? 192.529 191.152 278.696 1.00 78.36  ? 368  ASN B CB  1 
ATOM   2963  C CG  . ASN A 1 385  ? 192.533 189.640 278.682 1.00 78.36  ? 368  ASN B CG  1 
ATOM   2964  O OD1 . ASN A 1 385  ? 191.491 189.004 278.824 1.00 78.36  ? 368  ASN B OD1 1 
ATOM   2965  N ND2 . ASN A 1 385  ? 193.709 189.054 278.502 1.00 78.36  ? 368  ASN B ND2 1 
ATOM   2966  N N   . PHE A 1 386  ? 190.227 191.363 281.565 1.00 78.10  ? 369  PHE B N   1 
ATOM   2967  C CA  . PHE A 1 386  ? 190.119 191.277 283.011 1.00 78.10  ? 369  PHE B CA  1 
ATOM   2968  C C   . PHE A 1 386  ? 190.595 189.924 283.526 1.00 78.10  ? 369  PHE B C   1 
ATOM   2969  O O   . PHE A 1 386  ? 190.611 188.919 282.811 1.00 78.10  ? 369  PHE B O   1 
ATOM   2970  C CB  . PHE A 1 386  ? 188.678 191.520 283.452 1.00 78.10  ? 369  PHE B CB  1 
ATOM   2971  C CG  . PHE A 1 386  ? 188.241 192.943 283.318 1.00 78.10  ? 369  PHE B CG  1 
ATOM   2972  C CD1 . PHE A 1 386  ? 188.929 193.953 283.961 1.00 78.10  ? 369  PHE B CD1 1 
ATOM   2973  C CD2 . PHE A 1 386  ? 187.148 193.274 282.544 1.00 78.10  ? 369  PHE B CD2 1 
ATOM   2974  C CE1 . PHE A 1 386  ? 188.531 195.265 283.838 1.00 78.10  ? 369  PHE B CE1 1 
ATOM   2975  C CE2 . PHE A 1 386  ? 186.746 194.584 282.417 1.00 78.10  ? 369  PHE B CE2 1 
ATOM   2976  C CZ  . PHE A 1 386  ? 187.438 195.580 283.065 1.00 78.10  ? 369  PHE B CZ  1 
ATOM   2977  N N   . ASP A 1 387  ? 190.994 189.917 284.793 1.00 77.79  ? 370  ASP B N   1 
ATOM   2978  C CA  . ASP A 1 387  ? 191.377 188.691 285.468 1.00 77.79  ? 370  ASP B CA  1 
ATOM   2979  C C   . ASP A 1 387  ? 190.143 187.848 285.772 1.00 77.79  ? 370  ASP B C   1 
ATOM   2980  O O   . ASP A 1 387  ? 189.019 188.349 285.855 1.00 77.79  ? 370  ASP B O   1 
ATOM   2981  C CB  . ASP A 1 387  ? 192.136 189.016 286.751 1.00 77.79  ? 370  ASP B CB  1 
ATOM   2982  C CG  . ASP A 1 387  ? 193.215 190.051 286.530 1.00 77.79  ? 370  ASP B CG  1 
ATOM   2983  O OD1 . ASP A 1 387  ? 193.479 190.387 285.358 1.00 77.79  ? 370  ASP B OD1 1 
ATOM   2984  O OD2 . ASP A 1 387  ? 193.793 190.539 287.521 1.00 77.79  ? 370  ASP B OD2 1 
ATOM   2985  N N   . LYS A 1 388  ? 190.362 186.556 285.934 1.00 75.10  ? 371  LYS B N   1 
ATOM   2986  C CA  . LYS A 1 388  ? 189.225 185.656 286.091 1.00 75.10  ? 371  LYS B CA  1 
ATOM   2987  C C   . LYS A 1 388  ? 189.287 184.803 287.347 1.00 75.10  ? 371  LYS B C   1 
ATOM   2988  O O   . LYS A 1 388  ? 188.243 184.540 287.947 1.00 75.10  ? 371  LYS B O   1 
ATOM   2989  C CB  . LYS A 1 388  ? 189.104 184.751 284.857 1.00 75.10  ? 371  LYS B CB  1 
ATOM   2990  C CG  . LYS A 1 388  ? 188.961 185.510 283.552 1.00 75.10  ? 371  LYS B CG  1 
ATOM   2991  C CD  . LYS A 1 388  ? 188.250 184.679 282.503 1.00 75.10  ? 371  LYS B CD  1 
ATOM   2992  C CE  . LYS A 1 388  ? 187.863 185.528 281.307 1.00 75.10  ? 371  LYS B CE  1 
ATOM   2993  N NZ  . LYS A 1 388  ? 189.025 186.288 280.774 1.00 75.10  ? 371  LYS B NZ  1 
ATOM   2994  N N   . ALA A 1 389  ? 190.472 184.362 287.764 1.00 76.33  ? 372  ALA B N   1 
ATOM   2995  C CA  . ALA A 1 389  ? 190.566 183.434 288.882 1.00 76.33  ? 372  ALA B CA  1 
ATOM   2996  C C   . ALA A 1 389  ? 191.691 183.847 289.819 1.00 76.33  ? 372  ALA B C   1 
ATOM   2997  O O   . ALA A 1 389  ? 192.526 184.691 289.492 1.00 76.33  ? 372  ALA B O   1 
ATOM   2998  C CB  . ALA A 1 389  ? 190.782 181.996 288.397 1.00 76.33  ? 372  ALA B CB  1 
ATOM   2999  N N   . VAL A 1 390  ? 191.704 183.229 290.997 1.00 74.22  ? 373  VAL B N   1 
ATOM   3000  C CA  . VAL A 1 390  ? 192.777 183.380 291.971 1.00 74.22  ? 373  VAL B CA  1 
ATOM   3001  C C   . VAL A 1 390  ? 193.560 182.079 292.004 1.00 74.22  ? 373  VAL B C   1 
ATOM   3002  O O   . VAL A 1 390  ? 192.973 181.000 292.153 1.00 74.22  ? 373  VAL B O   1 
ATOM   3003  C CB  . VAL A 1 390  ? 192.233 183.719 293.368 1.00 74.22  ? 373  VAL B CB  1 
ATOM   3004  C CG1 . VAL A 1 390  ? 193.295 183.469 294.421 1.00 74.22  ? 373  VAL B CG1 1 
ATOM   3005  C CG2 . VAL A 1 390  ? 191.764 185.149 293.422 1.00 74.22  ? 373  VAL B CG2 1 
ATOM   3006  N N   . PHE A 1 391  ? 194.878 182.171 291.859 1.00 75.70  ? 374  PHE B N   1 
ATOM   3007  C CA  . PHE A 1 391  ? 195.743 181.001 291.870 1.00 75.70  ? 374  PHE B CA  1 
ATOM   3008  C C   . PHE A 1 391  ? 196.729 181.128 293.019 1.00 75.70  ? 374  PHE B C   1 
ATOM   3009  O O   . PHE A 1 391  ? 197.489 182.099 293.087 1.00 75.70  ? 374  PHE B O   1 
ATOM   3010  C CB  . PHE A 1 391  ? 196.484 180.853 290.541 1.00 75.70  ? 374  PHE B CB  1 
ATOM   3011  C CG  . PHE A 1 391  ? 195.696 180.140 289.487 1.00 75.70  ? 374  PHE B CG  1 
ATOM   3012  C CD1 . PHE A 1 391  ? 195.042 178.958 289.775 1.00 75.70  ? 374  PHE B CD1 1 
ATOM   3013  C CD2 . PHE A 1 391  ? 195.610 180.652 288.207 1.00 75.70  ? 374  PHE B CD2 1 
ATOM   3014  C CE1 . PHE A 1 391  ? 194.317 178.299 288.806 1.00 75.70  ? 374  PHE B CE1 1 
ATOM   3015  C CE2 . PHE A 1 391  ? 194.886 179.999 287.235 1.00 75.70  ? 374  PHE B CE2 1 
ATOM   3016  C CZ  . PHE A 1 391  ? 194.239 178.820 287.534 1.00 75.70  ? 374  PHE B CZ  1 
ATOM   3017  N N   . LYS A 1 392  ? 196.711 180.153 293.919 1.00 75.09  ? 375  LYS B N   1 
ATOM   3018  C CA  . LYS A 1 392  ? 197.745 180.044 294.933 1.00 75.09  ? 375  LYS B CA  1 
ATOM   3019  C C   . LYS A 1 392  ? 198.951 179.342 294.327 1.00 75.09  ? 375  LYS B C   1 
ATOM   3020  O O   . LYS A 1 392  ? 198.814 178.277 293.712 1.00 75.09  ? 375  LYS B O   1 
ATOM   3021  C CB  . LYS A 1 392  ? 197.227 179.278 296.148 1.00 75.09  ? 375  LYS B CB  1 
ATOM   3022  C CG  . LYS A 1 392  ? 198.308 178.633 296.992 1.00 75.09  ? 375  LYS B CG  1 
ATOM   3023  C CD  . LYS A 1 392  ? 198.991 179.654 297.878 1.00 75.09  ? 375  LYS B CD  1 
ATOM   3024  C CE  . LYS A 1 392  ? 199.449 179.030 299.183 1.00 75.09  ? 375  LYS B CE  1 
ATOM   3025  N NZ  . LYS A 1 392  ? 200.489 179.854 299.856 1.00 75.09  ? 375  LYS B NZ  1 
ATOM   3026  N N   . ILE A 1 393  ? 200.127 179.956 294.477 1.00 73.15  ? 376  ILE B N   1 
ATOM   3027  C CA  . ILE A 1 393  ? 201.363 179.459 293.890 1.00 73.15  ? 376  ILE B CA  1 
ATOM   3028  C C   . ILE A 1 393  ? 202.439 179.404 294.964 1.00 73.15  ? 376  ILE B C   1 
ATOM   3029  O O   . ILE A 1 393  ? 202.346 180.050 296.010 1.00 73.15  ? 376  ILE B O   1 
ATOM   3030  C CB  . ILE A 1 393  ? 201.848 180.326 292.709 1.00 73.15  ? 376  ILE B CB  1 
ATOM   3031  C CG1 . ILE A 1 393  ? 202.455 181.629 293.221 1.00 73.15  ? 376  ILE B CG1 1 
ATOM   3032  C CG2 . ILE A 1 393  ? 200.715 180.619 291.753 1.00 73.15  ? 376  ILE B CG2 1 
ATOM   3033  C CD1 . ILE A 1 393  ? 202.931 182.543 292.121 1.00 73.15  ? 376  ILE B CD1 1 
ATOM   3034  N N   . ASN A 1 394  ? 203.473 178.613 294.688 1.00 78.47  ? 377  ASN B N   1 
ATOM   3035  C CA  . ASN A 1 394  ? 204.640 178.496 295.549 1.00 78.47  ? 377  ASN B CA  1 
ATOM   3036  C C   . ASN A 1 394  ? 205.868 178.934 294.766 1.00 78.47  ? 377  ASN B C   1 
ATOM   3037  O O   . ASN A 1 394  ? 206.135 178.409 293.680 1.00 78.47  ? 377  ASN B O   1 
ATOM   3038  C CB  . ASN A 1 394  ? 204.813 177.063 296.056 1.00 78.47  ? 377  ASN B CB  1 
ATOM   3039  C CG  . ASN A 1 394  ? 205.721 176.981 297.262 1.00 78.47  ? 377  ASN B CG  1 
ATOM   3040  O OD1 . ASN A 1 394  ? 206.087 178.000 297.846 1.00 78.47  ? 377  ASN B OD1 1 
ATOM   3041  N ND2 . ASN A 1 394  ? 206.089 175.765 297.645 1.00 78.47  ? 377  ASN B ND2 1 
ATOM   3042  N N   . ILE A 1 395  ? 206.612 179.888 295.320 1.00 74.57  ? 378  ILE B N   1 
ATOM   3043  C CA  . ILE A 1 395  ? 207.725 180.502 294.619 1.00 74.57  ? 378  ILE B CA  1 
ATOM   3044  C C   . ILE A 1 395  ? 209.079 180.065 295.171 1.00 74.57  ? 378  ILE B C   1 
ATOM   3045  O O   . ILE A 1 395  ? 210.052 180.001 294.410 1.00 74.57  ? 378  ILE B O   1 
ATOM   3046  C CB  . ILE A 1 395  ? 207.580 182.039 294.663 1.00 74.57  ? 378  ILE B CB  1 
ATOM   3047  C CG1 . ILE A 1 395  ? 206.528 182.495 293.655 1.00 74.57  ? 378  ILE B CG1 1 
ATOM   3048  C CG2 . ILE A 1 395  ? 208.898 182.743 294.397 1.00 74.57  ? 378  ILE B CG2 1 
ATOM   3049  C CD1 . ILE A 1 395  ? 207.001 182.455 292.234 1.00 74.57  ? 378  ILE B CD1 1 
ATOM   3050  N N   . VAL A 1 396  ? 209.158 179.717 296.457 1.00 75.96  ? 379  VAL B N   1 
ATOM   3051  C CA  . VAL A 1 396  ? 210.455 179.443 297.079 1.00 75.96  ? 379  VAL B CA  1 
ATOM   3052  C C   . VAL A 1 396  ? 211.217 178.317 296.389 1.00 75.96  ? 379  VAL B C   1 
ATOM   3053  O O   . VAL A 1 396  ? 212.402 178.511 296.072 1.00 75.96  ? 379  VAL B O   1 
ATOM   3054  C CB  . VAL A 1 396  ? 210.268 179.182 298.585 1.00 75.96  ? 379  VAL B CB  1 
ATOM   3055  C CG1 . VAL A 1 396  ? 211.609 178.936 299.252 1.00 75.96  ? 379  VAL B CG1 1 
ATOM   3056  C CG2 . VAL A 1 396  ? 209.539 180.337 299.225 1.00 75.96  ? 379  VAL B CG2 1 
ATOM   3057  N N   . PRO A 1 397  ? 210.637 177.139 296.141 1.00 81.48  ? 380  PRO B N   1 
ATOM   3058  C CA  . PRO A 1 397  ? 211.427 176.068 295.524 1.00 81.48  ? 380  PRO B CA  1 
ATOM   3059  C C   . PRO A 1 397  ? 211.879 176.446 294.122 1.00 81.48  ? 380  PRO B C   1 
ATOM   3060  O O   . PRO A 1 397  ? 211.142 177.067 293.356 1.00 81.48  ? 380  PRO B O   1 
ATOM   3061  C CB  . PRO A 1 397  ? 210.460 174.877 295.502 1.00 81.48  ? 380  PRO B CB  1 
ATOM   3062  C CG  . PRO A 1 397  ? 209.410 175.210 296.496 1.00 81.48  ? 380  PRO B CG  1 
ATOM   3063  C CD  . PRO A 1 397  ? 209.262 176.687 296.418 1.00 81.48  ? 380  PRO B CD  1 
ATOM   3064  N N   . LYS A 1 398  ? 213.111 176.060 293.792 1.00 83.97  ? 381  LYS B N   1 
ATOM   3065  C CA  . LYS A 1 398  ? 213.655 176.333 292.469 1.00 83.97  ? 381  LYS B CA  1 
ATOM   3066  C C   . LYS A 1 398  ? 213.073 175.418 291.401 1.00 83.97  ? 381  LYS B C   1 
ATOM   3067  O O   . LYS A 1 398  ? 213.144 175.748 290.212 1.00 83.97  ? 381  LYS B O   1 
ATOM   3068  C CB  . LYS A 1 398  ? 215.179 176.199 292.493 1.00 83.97  ? 381  LYS B CB  1 
ATOM   3069  C CG  . LYS A 1 398  ? 215.882 176.737 291.258 1.00 83.97  ? 381  LYS B CG  1 
ATOM   3070  C CD  . LYS A 1 398  ? 217.384 176.513 291.327 1.00 83.97  ? 381  LYS B CD  1 
ATOM   3071  C CE  . LYS A 1 398  ? 217.926 176.767 292.725 1.00 83.97  ? 381  LYS B CE  1 
ATOM   3072  N NZ  . LYS A 1 398  ? 217.846 178.203 293.104 1.00 83.97  ? 381  LYS B NZ  1 
ATOM   3073  N N   . VAL A 1 399  ? 212.488 174.285 291.795 1.00 85.53  ? 382  VAL B N   1 
ATOM   3074  C CA  . VAL A 1 399  ? 211.944 173.350 290.820 1.00 85.53  ? 382  VAL B CA  1 
ATOM   3075  C C   . VAL A 1 399  ? 210.655 173.863 290.193 1.00 85.53  ? 382  VAL B C   1 
ATOM   3076  O O   . VAL A 1 399  ? 210.230 173.345 289.154 1.00 85.53  ? 382  VAL B O   1 
ATOM   3077  C CB  . VAL A 1 399  ? 211.723 171.975 291.475 1.00 85.53  ? 382  VAL B CB  1 
ATOM   3078  C CG1 . VAL A 1 399  ? 212.951 171.572 292.271 1.00 85.53  ? 382  VAL B CG1 1 
ATOM   3079  C CG2 . VAL A 1 399  ? 210.495 172.003 292.368 1.00 85.53  ? 382  VAL B CG2 1 
ATOM   3080  N N   . ASN A 1 400  ? 210.015 174.871 290.793 1.00 85.76  ? 383  ASN B N   1 
ATOM   3081  C CA  . ASN A 1 400  ? 208.793 175.442 290.246 1.00 85.76  ? 383  ASN B CA  1 
ATOM   3082  C C   . ASN A 1 400  ? 208.970 176.838 289.673 1.00 85.76  ? 383  ASN B C   1 
ATOM   3083  O O   . ASN A 1 400  ? 208.147 177.258 288.855 1.00 85.76  ? 383  ASN B O   1 
ATOM   3084  C CB  . ASN A 1 400  ? 207.695 175.495 291.317 1.00 85.76  ? 383  ASN B CB  1 
ATOM   3085  C CG  . ASN A 1 400  ? 207.712 174.289 292.229 1.00 85.76  ? 383  ASN B CG  1 
ATOM   3086  O OD1 . ASN A 1 400  ? 208.206 174.355 293.352 1.00 85.76  ? 383  ASN B OD1 1 
ATOM   3087  N ND2 . ASN A 1 400  ? 207.160 173.180 291.753 1.00 85.76  ? 383  ASN B ND2 1 
ATOM   3088  N N   . TYR A 1 401  ? 210.011 177.563 290.076 1.00 82.41  ? 384  TYR B N   1 
ATOM   3089  C CA  . TYR A 1 401  ? 210.193 178.945 289.641 1.00 82.41  ? 384  TYR B CA  1 
ATOM   3090  C C   . TYR A 1 401  ? 211.684 179.257 289.713 1.00 82.41  ? 384  TYR B C   1 
ATOM   3091  O O   . TYR A 1 401  ? 212.211 179.518 290.797 1.00 82.41  ? 384  TYR B O   1 
ATOM   3092  C CB  . TYR A 1 401  ? 209.381 179.896 290.508 1.00 82.41  ? 384  TYR B CB  1 
ATOM   3093  C CG  . TYR A 1 401  ? 209.281 181.303 289.973 1.00 82.41  ? 384  TYR B CG  1 
ATOM   3094  C CD1 . TYR A 1 401  ? 208.284 181.655 289.078 1.00 82.41  ? 384  TYR B CD1 1 
ATOM   3095  C CD2 . TYR A 1 401  ? 210.169 182.284 290.380 1.00 82.41  ? 384  TYR B CD2 1 
ATOM   3096  C CE1 . TYR A 1 401  ? 208.182 182.939 288.595 1.00 82.41  ? 384  TYR B CE1 1 
ATOM   3097  C CE2 . TYR A 1 401  ? 210.074 183.572 289.900 1.00 82.41  ? 384  TYR B CE2 1 
ATOM   3098  C CZ  . TYR A 1 401  ? 209.079 183.892 289.008 1.00 82.41  ? 384  TYR B CZ  1 
ATOM   3099  O OH  . TYR A 1 401  ? 208.978 185.173 288.527 1.00 82.41  ? 384  TYR B OH  1 
ATOM   3100  N N   . THR A 1 402  ? 212.352 179.227 288.565 1.00 86.51  ? 385  THR B N   1 
ATOM   3101  C CA  . THR A 1 402  ? 213.762 179.570 288.535 1.00 86.51  ? 385  THR B CA  1 
ATOM   3102  C C   . THR A 1 402  ? 213.939 181.084 288.461 1.00 86.51  ? 385  THR B C   1 
ATOM   3103  O O   . THR A 1 402  ? 213.063 181.821 288.003 1.00 86.51  ? 385  THR B O   1 
ATOM   3104  C CB  . THR A 1 402  ? 214.467 178.890 287.362 1.00 86.51  ? 385  THR B CB  1 
ATOM   3105  O OG1 . THR A 1 402  ? 215.878 178.852 287.608 1.00 86.51  ? 385  THR B OG1 1 
ATOM   3106  C CG2 . THR A 1 402  ? 214.206 179.638 286.073 1.00 86.51  ? 385  THR B CG2 1 
ATOM   3107  N N   . ILE A 1 403  ? 215.099 181.540 288.930 1.00 79.53  ? 386  ILE B N   1 
ATOM   3108  C CA  . ILE A 1 403  ? 215.327 182.969 289.107 1.00 79.53  ? 386  ILE B CA  1 
ATOM   3109  C C   . ILE A 1 403  ? 215.400 183.682 287.762 1.00 79.53  ? 386  ILE B C   1 
ATOM   3110  O O   . ILE A 1 403  ? 214.931 184.818 287.621 1.00 79.53  ? 386  ILE B O   1 
ATOM   3111  C CB  . ILE A 1 403  ? 216.597 183.190 289.948 1.00 79.53  ? 386  ILE B CB  1 
ATOM   3112  C CG1 . ILE A 1 403  ? 216.879 184.680 290.112 1.00 79.53  ? 386  ILE B CG1 1 
ATOM   3113  C CG2 . ILE A 1 403  ? 217.785 182.458 289.341 1.00 79.53  ? 386  ILE B CG2 1 
ATOM   3114  C CD1 . ILE A 1 403  ? 215.892 185.364 291.001 1.00 79.53  ? 386  ILE B CD1 1 
ATOM   3115  N N   . TYR A 1 404  ? 215.979 183.034 286.752 1.00 85.47  ? 387  TYR B N   1 
ATOM   3116  C CA  . TYR A 1 404  ? 216.235 183.684 285.472 1.00 85.47  ? 387  TYR B CA  1 
ATOM   3117  C C   . TYR A 1 404  ? 215.051 183.606 284.516 1.00 85.47  ? 387  TYR B C   1 
ATOM   3118  O O   . TYR A 1 404  ? 214.759 184.582 283.817 1.00 85.47  ? 387  TYR B O   1 
ATOM   3119  C CB  . TYR A 1 404  ? 217.470 183.069 284.812 1.00 85.47  ? 387  TYR B CB  1 
ATOM   3120  C CG  . TYR A 1 404  ? 218.742 183.833 285.080 1.00 85.47  ? 387  TYR B CG  1 
ATOM   3121  C CD1 . TYR A 1 404  ? 219.426 183.682 286.278 1.00 85.47  ? 387  TYR B CD1 1 
ATOM   3122  C CD2 . TYR A 1 404  ? 219.258 184.708 284.137 1.00 85.47  ? 387  TYR B CD2 1 
ATOM   3123  C CE1 . TYR A 1 404  ? 220.588 184.381 286.528 1.00 85.47  ? 387  TYR B CE1 1 
ATOM   3124  C CE2 . TYR A 1 404  ? 220.419 185.412 284.377 1.00 85.47  ? 387  TYR B CE2 1 
ATOM   3125  C CZ  . TYR A 1 404  ? 221.081 185.245 285.573 1.00 85.47  ? 387  TYR B CZ  1 
ATOM   3126  O OH  . TYR A 1 404  ? 222.240 185.947 285.812 1.00 85.47  ? 387  TYR B OH  1 
ATOM   3127  N N   . ASP A 1 405  ? 214.364 182.466 284.464 1.00 90.42  ? 388  ASP B N   1 
ATOM   3128  C CA  . ASP A 1 405  ? 213.267 182.274 283.525 1.00 90.42  ? 388  ASP B CA  1 
ATOM   3129  C C   . ASP A 1 405  ? 211.890 182.386 284.162 1.00 90.42  ? 388  ASP B C   1 
ATOM   3130  O O   . ASP A 1 405  ? 210.958 182.870 283.512 1.00 90.42  ? 388  ASP B O   1 
ATOM   3131  C CB  . ASP A 1 405  ? 213.386 180.908 282.842 1.00 90.42  ? 388  ASP B CB  1 
ATOM   3132  C CG  . ASP A 1 405  ? 214.205 180.963 281.571 1.00 90.42  ? 388  ASP B CG  1 
ATOM   3133  O OD1 . ASP A 1 405  ? 213.792 181.666 280.625 1.00 90.42  ? 388  ASP B OD1 1 
ATOM   3134  O OD2 . ASP A 1 405  ? 215.263 180.300 281.516 1.00 90.42  ? 388  ASP B OD2 1 
ATOM   3135  N N   . GLY A 1 406  ? 211.733 181.960 285.411 1.00 87.34  ? 389  GLY B N   1 
ATOM   3136  C CA  . GLY A 1 406  ? 210.427 181.974 286.036 1.00 87.34  ? 389  GLY B CA  1 
ATOM   3137  C C   . GLY A 1 406  ? 209.688 180.671 285.827 1.00 87.34  ? 389  GLY B C   1 
ATOM   3138  O O   . GLY A 1 406  ? 210.290 179.597 285.908 1.00 87.34  ? 389  GLY B O   1 
ATOM   3139  N N   . PHE A 1 407  ? 208.384 180.743 285.556 1.00 90.95  ? 390  PHE B N   1 
ATOM   3140  C CA  . PHE A 1 407  ? 207.618 179.526 285.320 1.00 90.95  ? 390  PHE B CA  1 
ATOM   3141  C C   . PHE A 1 407  ? 207.996 178.848 284.012 1.00 90.95  ? 390  PHE B C   1 
ATOM   3142  O O   . PHE A 1 407  ? 207.765 177.644 283.865 1.00 90.95  ? 390  PHE B O   1 
ATOM   3143  C CB  . PHE A 1 407  ? 206.119 179.824 285.328 1.00 90.95  ? 390  PHE B CB  1 
ATOM   3144  C CG  . PHE A 1 407  ? 205.573 180.146 286.686 1.00 90.95  ? 390  PHE B CG  1 
ATOM   3145  C CD1 . PHE A 1 407  ? 205.722 179.257 287.733 1.00 90.95  ? 390  PHE B CD1 1 
ATOM   3146  C CD2 . PHE A 1 407  ? 204.891 181.326 286.910 1.00 90.95  ? 390  PHE B CD2 1 
ATOM   3147  C CE1 . PHE A 1 407  ? 205.217 179.549 288.982 1.00 90.95  ? 390  PHE B CE1 1 
ATOM   3148  C CE2 . PHE A 1 407  ? 204.383 181.620 288.156 1.00 90.95  ? 390  PHE B CE2 1 
ATOM   3149  C CZ  . PHE A 1 407  ? 204.547 180.731 289.192 1.00 90.95  ? 390  PHE B CZ  1 
ATOM   3150  N N   . ASN A 1 408  ? 208.567 179.586 283.063 1.00 97.24  ? 391  ASN B N   1 
ATOM   3151  C CA  . ASN A 1 408  ? 208.974 179.014 281.779 1.00 97.24  ? 391  ASN B CA  1 
ATOM   3152  C C   . ASN A 1 408  ? 210.384 178.438 281.904 1.00 97.24  ? 391  ASN B C   1 
ATOM   3153  O O   . ASN A 1 408  ? 211.357 178.934 281.333 1.00 97.24  ? 391  ASN B O   1 
ATOM   3154  C CB  . ASN A 1 408  ? 208.887 180.063 280.680 1.00 97.24  ? 391  ASN B CB  1 
ATOM   3155  C CG  . ASN A 1 408  ? 207.468 180.521 280.425 1.00 97.24  ? 391  ASN B CG  1 
ATOM   3156  O OD1 . ASN A 1 408  ? 206.519 179.758 280.597 1.00 97.24  ? 391  ASN B OD1 1 
ATOM   3157  N ND2 . ASN A 1 408  ? 207.315 181.772 280.011 1.00 97.24  ? 391  ASN B ND2 1 
ATOM   3158  N N   . LEU A 1 409  ? 210.475 177.360 282.679 1.00 103.72 ? 392  LEU B N   1 
ATOM   3159  C CA  . LEU A 1 409  ? 211.755 176.702 282.899 1.00 103.72 ? 392  LEU B CA  1 
ATOM   3160  C C   . LEU A 1 409  ? 212.297 176.134 281.593 1.00 103.72 ? 392  LEU B C   1 
ATOM   3161  O O   . LEU A 1 409  ? 211.557 175.567 280.785 1.00 103.72 ? 392  LEU B O   1 
ATOM   3162  C CB  . LEU A 1 409  ? 211.602 175.591 283.935 1.00 103.72 ? 392  LEU B CB  1 
ATOM   3163  C CG  . LEU A 1 409  ? 211.893 175.989 285.380 1.00 103.72 ? 392  LEU B CG  1 
ATOM   3164  C CD1 . LEU A 1 409  ? 211.091 175.129 286.339 1.00 103.72 ? 392  LEU B CD1 1 
ATOM   3165  C CD2 . LEU A 1 409  ? 213.377 175.868 285.665 1.00 103.72 ? 392  LEU B CD2 1 
ATOM   3166  N N   . ARG A 1 410  ? 213.601 176.290 281.391 1.00 111.31 ? 393  ARG B N   1 
ATOM   3167  C CA  . ARG A 1 410  ? 214.238 175.868 280.156 1.00 111.31 ? 393  ARG B CA  1 
ATOM   3168  C C   . ARG A 1 410  ? 214.497 174.364 280.157 1.00 111.31 ? 393  ARG B C   1 
ATOM   3169  O O   . ARG A 1 410  ? 214.517 173.708 281.202 1.00 111.31 ? 393  ARG B O   1 
ATOM   3170  C CB  . ARG A 1 410  ? 215.550 176.621 279.949 1.00 111.31 ? 393  ARG B CB  1 
ATOM   3171  C CG  . ARG A 1 410  ? 216.561 176.403 281.059 1.00 111.31 ? 393  ARG B CG  1 
ATOM   3172  C CD  . ARG A 1 410  ? 217.852 177.143 280.774 1.00 111.31 ? 393  ARG B CD  1 
ATOM   3173  N NE  . ARG A 1 410  ? 217.686 178.585 280.904 1.00 111.31 ? 393  ARG B NE  1 
ATOM   3174  C CZ  . ARG A 1 410  ? 218.619 179.407 281.363 1.00 111.31 ? 393  ARG B CZ  1 
ATOM   3175  N NH1 . ARG A 1 410  ? 219.802 178.962 281.754 1.00 111.31 ? 393  ARG B NH1 1 
ATOM   3176  N NH2 . ARG A 1 410  ? 218.359 180.710 281.430 1.00 111.31 ? 393  ARG B NH2 1 
ATOM   3177  N N   . ASN A 1 411  ? 214.690 173.824 278.952 1.00 118.21 ? 394  ASN B N   1 
ATOM   3178  C CA  . ASN A 1 411  ? 215.023 172.418 278.722 1.00 118.21 ? 394  ASN B CA  1 
ATOM   3179  C C   . ASN A 1 411  ? 213.948 171.468 279.240 1.00 118.21 ? 394  ASN B C   1 
ATOM   3180  O O   . ASN A 1 411  ? 214.234 170.304 279.535 1.00 118.21 ? 394  ASN B O   1 
ATOM   3181  C CB  . ASN A 1 411  ? 216.382 172.061 279.335 1.00 118.21 ? 394  ASN B CB  1 
ATOM   3182  C CG  . ASN A 1 411  ? 217.477 173.024 278.921 1.00 118.21 ? 394  ASN B CG  1 
ATOM   3183  O OD1 . ASN A 1 411  ? 217.494 173.515 277.793 1.00 118.21 ? 394  ASN B OD1 1 
ATOM   3184  N ND2 . ASN A 1 411  ? 218.400 173.299 279.835 1.00 118.21 ? 394  ASN B ND2 1 
ATOM   3185  N N   . THR A 1 412  ? 212.711 171.943 279.358 1.00 114.93 ? 395  THR B N   1 
ATOM   3186  C CA  . THR A 1 412  ? 211.578 171.128 279.773 1.00 114.93 ? 395  THR B CA  1 
ATOM   3187  C C   . THR A 1 412  ? 210.407 171.396 278.836 1.00 114.93 ? 395  THR B C   1 
ATOM   3188  O O   . THR A 1 412  ? 210.485 172.229 277.929 1.00 114.93 ? 395  THR B O   1 
ATOM   3189  C CB  . THR A 1 412  ? 211.179 171.411 281.228 1.00 114.93 ? 395  THR B CB  1 
ATOM   3190  O OG1 . THR A 1 412  ? 210.811 172.788 281.363 1.00 114.93 ? 395  THR B OG1 1 
ATOM   3191  C CG2 . THR A 1 412  ? 212.323 171.093 282.179 1.00 114.93 ? 395  THR B CG2 1 
ATOM   3192  N N   . ASN A 1 413  ? 209.306 170.677 279.064 1.00 114.76 ? 396  ASN B N   1 
ATOM   3193  C CA  . ASN A 1 413  ? 208.112 170.869 278.251 1.00 114.76 ? 396  ASN B CA  1 
ATOM   3194  C C   . ASN A 1 413  ? 207.478 172.237 278.466 1.00 114.76 ? 396  ASN B C   1 
ATOM   3195  O O   . ASN A 1 413  ? 206.667 172.667 277.638 1.00 114.76 ? 396  ASN B O   1 
ATOM   3196  C CB  . ASN A 1 413  ? 207.092 169.767 278.546 1.00 114.76 ? 396  ASN B CB  1 
ATOM   3197  C CG  . ASN A 1 413  ? 206.587 169.806 279.974 1.00 114.76 ? 396  ASN B CG  1 
ATOM   3198  O OD1 . ASN A 1 413  ? 207.332 169.534 280.916 1.00 114.76 ? 396  ASN B OD1 1 
ATOM   3199  N ND2 . ASN A 1 413  ? 205.315 170.147 280.142 1.00 114.76 ? 396  ASN B ND2 1 
ATOM   3200  N N   . LEU A 1 414  ? 207.824 172.925 279.550 1.00 110.18 ? 397  LEU B N   1 
ATOM   3201  C CA  . LEU A 1 414  ? 207.308 174.257 279.831 1.00 110.18 ? 397  LEU B CA  1 
ATOM   3202  C C   . LEU A 1 414  ? 208.109 175.357 279.149 1.00 110.18 ? 397  LEU B C   1 
ATOM   3203  O O   . LEU A 1 414  ? 207.719 176.526 279.229 1.00 110.18 ? 397  LEU B O   1 
ATOM   3204  C CB  . LEU A 1 414  ? 207.282 174.509 281.343 1.00 110.18 ? 397  LEU B CB  1 
ATOM   3205  C CG  . LEU A 1 414  ? 206.796 173.377 282.253 1.00 110.18 ? 397  LEU B CG  1 
ATOM   3206  C CD1 . LEU A 1 414  ? 207.955 172.536 282.761 1.00 110.18 ? 397  LEU B CD1 1 
ATOM   3207  C CD2 . LEU A 1 414  ? 205.996 173.933 283.418 1.00 110.18 ? 397  LEU B CD2 1 
ATOM   3208  N N   . ALA A 1 415  ? 209.214 175.015 278.486 1.00 112.81 ? 398  ALA B N   1 
ATOM   3209  C CA  . ALA A 1 415  ? 210.070 176.037 277.892 1.00 112.81 ? 398  ALA B CA  1 
ATOM   3210  C C   . ALA A 1 415  ? 209.401 176.715 276.703 1.00 112.81 ? 398  ALA B C   1 
ATOM   3211  O O   . ALA A 1 415  ? 209.517 177.934 276.532 1.00 112.81 ? 398  ALA B O   1 
ATOM   3212  C CB  . ALA A 1 415  ? 211.406 175.422 277.476 1.00 112.81 ? 398  ALA B CB  1 
ATOM   3213  N N   . ALA A 1 416  ? 208.701 175.949 275.873 1.00 108.40 ? 399  ALA B N   1 
ATOM   3214  C CA  . ALA A 1 416  ? 208.153 176.454 274.624 1.00 108.40 ? 399  ALA B CA  1 
ATOM   3215  C C   . ALA A 1 416  ? 206.660 176.729 274.748 1.00 108.40 ? 399  ALA B C   1 
ATOM   3216  O O   . ALA A 1 416  ? 205.952 176.086 275.528 1.00 108.40 ? 399  ALA B O   1 
ATOM   3217  C CB  . ALA A 1 416  ? 208.403 175.466 273.483 1.00 108.40 ? 399  ALA B CB  1 
ATOM   3218  N N   . ASN A 1 417  ? 206.194 177.705 273.967 1.00 105.64 ? 400  ASN B N   1 
ATOM   3219  C CA  . ASN A 1 417  ? 204.788 178.096 273.889 1.00 105.64 ? 400  ASN B CA  1 
ATOM   3220  C C   . ASN A 1 417  ? 204.241 178.583 275.226 1.00 105.64 ? 400  ASN B C   1 
ATOM   3221  O O   . ASN A 1 417  ? 203.025 178.554 275.445 1.00 105.64 ? 400  ASN B O   1 
ATOM   3222  C CB  . ASN A 1 417  ? 203.920 176.953 273.352 1.00 105.64 ? 400  ASN B CB  1 
ATOM   3223  C CG  . ASN A 1 417  ? 204.435 176.402 272.040 1.00 105.64 ? 400  ASN B CG  1 
ATOM   3224  O OD1 . ASN A 1 417  ? 205.517 176.767 271.582 1.00 105.64 ? 400  ASN B OD1 1 
ATOM   3225  N ND2 . ASN A 1 417  ? 203.659 175.518 271.424 1.00 105.64 ? 400  ASN B ND2 1 
ATOM   3226  N N   . PHE A 1 418  ? 205.122 179.037 276.119 1.00 96.49  ? 401  PHE B N   1 
ATOM   3227  C CA  . PHE A 1 418  ? 204.728 179.551 277.431 1.00 96.49  ? 401  PHE B CA  1 
ATOM   3228  C C   . PHE A 1 418  ? 203.890 178.534 278.197 1.00 96.49  ? 401  PHE B C   1 
ATOM   3229  O O   . PHE A 1 418  ? 202.914 178.877 278.866 1.00 96.49  ? 401  PHE B O   1 
ATOM   3230  C CB  . PHE A 1 418  ? 203.984 180.879 277.300 1.00 96.49  ? 401  PHE B CB  1 
ATOM   3231  C CG  . PHE A 1 418  ? 204.724 181.911 276.505 1.00 96.49  ? 401  PHE B CG  1 
ATOM   3232  C CD1 . PHE A 1 418  ? 205.656 182.732 277.113 1.00 96.49  ? 401  PHE B CD1 1 
ATOM   3233  C CD2 . PHE A 1 418  ? 204.486 182.064 275.151 1.00 96.49  ? 401  PHE B CD2 1 
ATOM   3234  C CE1 . PHE A 1 418  ? 206.336 183.686 276.387 1.00 96.49  ? 401  PHE B CE1 1 
ATOM   3235  C CE2 . PHE A 1 418  ? 205.164 183.018 274.420 1.00 96.49  ? 401  PHE B CE2 1 
ATOM   3236  C CZ  . PHE A 1 418  ? 206.090 183.829 275.039 1.00 96.49  ? 401  PHE B CZ  1 
ATOM   3237  N N   . ASN A 1 419  ? 204.273 177.261 278.094 1.00 103.35 ? 402  ASN B N   1 
ATOM   3238  C CA  . ASN A 1 419  ? 203.553 176.208 278.794 1.00 103.35 ? 402  ASN B CA  1 
ATOM   3239  C C   . ASN A 1 419  ? 203.766 176.251 280.300 1.00 103.35 ? 402  ASN B C   1 
ATOM   3240  O O   . ASN A 1 419  ? 203.039 175.570 281.029 1.00 103.35 ? 402  ASN B O   1 
ATOM   3241  C CB  . ASN A 1 419  ? 203.963 174.841 278.250 1.00 103.35 ? 402  ASN B CB  1 
ATOM   3242  C CG  . ASN A 1 419  ? 203.233 174.484 276.972 1.00 103.35 ? 402  ASN B CG  1 
ATOM   3243  O OD1 . ASN A 1 419  ? 202.227 175.103 276.626 1.00 103.35 ? 402  ASN B OD1 1 
ATOM   3244  N ND2 . ASN A 1 419  ? 203.738 173.483 276.262 1.00 103.35 ? 402  ASN B ND2 1 
ATOM   3245  N N   . GLY A 1 420  ? 204.739 177.026 280.780 1.00 98.36  ? 403  GLY B N   1 
ATOM   3246  C CA  . GLY A 1 420  ? 204.923 177.169 282.211 1.00 98.36  ? 403  GLY B CA  1 
ATOM   3247  C C   . GLY A 1 420  ? 203.857 178.003 282.884 1.00 98.36  ? 403  GLY B C   1 
ATOM   3248  O O   . GLY A 1 420  ? 203.640 177.857 284.091 1.00 98.36  ? 403  GLY B O   1 
ATOM   3249  N N   . GLN A 1 421  ? 203.188 178.873 282.134 1.00 91.71  ? 404  GLN B N   1 
ATOM   3250  C CA  . GLN A 1 421  ? 202.132 179.715 282.671 1.00 91.71  ? 404  GLN B CA  1 
ATOM   3251  C C   . GLN A 1 421  ? 200.740 179.177 282.385 1.00 91.71  ? 404  GLN B C   1 
ATOM   3252  O O   . GLN A 1 421  ? 199.756 179.811 282.776 1.00 91.71  ? 404  GLN B O   1 
ATOM   3253  C CB  . GLN A 1 421  ? 202.254 181.135 282.114 1.00 91.71  ? 404  GLN B CB  1 
ATOM   3254  C CG  . GLN A 1 421  ? 203.259 181.997 282.843 1.00 91.71  ? 404  GLN B CG  1 
ATOM   3255  C CD  . GLN A 1 421  ? 203.744 183.146 281.997 1.00 91.71  ? 404  GLN B CD  1 
ATOM   3256  O OE1 . GLN A 1 421  ? 204.940 183.293 281.758 1.00 91.71  ? 404  GLN B OE1 1 
ATOM   3257  N NE2 . GLN A 1 421  ? 202.814 183.966 281.527 1.00 91.71  ? 404  GLN B NE2 1 
ATOM   3258  N N   . ASN A 1 422  ? 200.628 178.034 281.718 1.00 92.88  ? 405  ASN B N   1 
ATOM   3259  C CA  . ASN A 1 422  ? 199.332 177.447 281.408 1.00 92.88  ? 405  ASN B CA  1 
ATOM   3260  C C   . ASN A 1 422  ? 198.914 176.537 282.555 1.00 92.88  ? 405  ASN B C   1 
ATOM   3261  O O   . ASN A 1 422  ? 199.614 175.570 282.872 1.00 92.88  ? 405  ASN B O   1 
ATOM   3262  C CB  . ASN A 1 422  ? 199.391 176.670 280.096 1.00 92.88  ? 405  ASN B CB  1 
ATOM   3263  C CG  . ASN A 1 422  ? 198.029 176.488 279.468 1.00 92.88  ? 405  ASN B CG  1 
ATOM   3264  O OD1 . ASN A 1 422  ? 197.027 176.339 280.166 1.00 92.88  ? 405  ASN B OD1 1 
ATOM   3265  N ND2 . ASN A 1 422  ? 197.982 176.496 278.142 1.00 92.88  ? 405  ASN B ND2 1 
ATOM   3266  N N   . THR A 1 423  ? 197.774 176.845 283.175 1.00 95.51  ? 406  THR B N   1 
ATOM   3267  C CA  . THR A 1 423  ? 197.335 176.065 284.325 1.00 95.51  ? 406  THR B CA  1 
ATOM   3268  C C   . THR A 1 423  ? 196.868 174.669 283.935 1.00 95.51  ? 406  THR B C   1 
ATOM   3269  O O   . THR A 1 423  ? 196.910 173.761 284.771 1.00 95.51  ? 406  THR B O   1 
ATOM   3270  C CB  . THR A 1 423  ? 196.217 176.793 285.074 1.00 95.51  ? 406  THR B CB  1 
ATOM   3271  O OG1 . THR A 1 423  ? 195.828 176.019 286.215 1.00 95.51  ? 406  THR B OG1 1 
ATOM   3272  C CG2 . THR A 1 423  ? 195.008 176.976 284.184 1.00 95.51  ? 406  THR B CG2 1 
ATOM   3273  N N   . GLU A 1 424  ? 196.428 174.472 282.691 1.00 100.14 ? 407  GLU B N   1 
ATOM   3274  C CA  . GLU A 1 424  ? 195.952 173.164 282.265 1.00 100.14 ? 407  GLU B CA  1 
ATOM   3275  C C   . GLU A 1 424  ? 197.078 172.230 281.837 1.00 100.14 ? 407  GLU B C   1 
ATOM   3276  O O   . GLU A 1 424  ? 196.836 171.027 281.690 1.00 100.14 ? 407  GLU B O   1 
ATOM   3277  C CB  . GLU A 1 424  ? 194.932 173.320 281.133 1.00 100.14 ? 407  GLU B CB  1 
ATOM   3278  C CG  . GLU A 1 424  ? 195.534 173.513 279.757 1.00 100.14 ? 407  GLU B CG  1 
ATOM   3279  C CD  . GLU A 1 424  ? 194.486 173.550 278.662 1.00 100.14 ? 407  GLU B CD  1 
ATOM   3280  O OE1 . GLU A 1 424  ? 193.282 173.503 278.987 1.00 100.14 ? 407  GLU B OE1 1 
ATOM   3281  O OE2 . GLU A 1 424  ? 194.867 173.628 277.475 1.00 100.14 ? 407  GLU B OE2 1 
ATOM   3282  N N   . ILE A 1 425  ? 198.293 172.741 281.638 1.00 98.42  ? 408  ILE B N   1 
ATOM   3283  C CA  . ILE A 1 425  ? 199.460 171.889 281.435 1.00 98.42  ? 408  ILE B CA  1 
ATOM   3284  C C   . ILE A 1 425  ? 200.202 171.783 282.758 1.00 98.42  ? 408  ILE B C   1 
ATOM   3285  O O   . ILE A 1 425  ? 200.435 170.681 283.268 1.00 98.42  ? 408  ILE B O   1 
ATOM   3286  C CB  . ILE A 1 425  ? 200.392 172.417 280.326 1.00 98.42  ? 408  ILE B CB  1 
ATOM   3287  C CG1 . ILE A 1 425  ? 199.849 172.089 278.933 1.00 98.42  ? 408  ILE B CG1 1 
ATOM   3288  C CG2 . ILE A 1 425  ? 201.786 171.834 280.480 1.00 98.42  ? 408  ILE B CG2 1 
ATOM   3289  C CD1 . ILE A 1 425  ? 198.729 172.977 278.467 1.00 98.42  ? 408  ILE B CD1 1 
ATOM   3290  N N   . ASN A 1 426  ? 200.576 172.931 283.323 1.00 96.18  ? 409  ASN B N   1 
ATOM   3291  C CA  . ASN A 1 426  ? 201.288 172.980 284.600 1.00 96.18  ? 409  ASN B CA  1 
ATOM   3292  C C   . ASN A 1 426  ? 200.274 173.093 285.739 1.00 96.18  ? 409  ASN B C   1 
ATOM   3293  O O   . ASN A 1 426  ? 200.142 174.116 286.411 1.00 96.18  ? 409  ASN B O   1 
ATOM   3294  C CB  . ASN A 1 426  ? 202.281 174.134 284.608 1.00 96.18  ? 409  ASN B CB  1 
ATOM   3295  C CG  . ASN A 1 426  ? 203.233 174.073 285.780 1.00 96.18  ? 409  ASN B CG  1 
ATOM   3296  O OD1 . ASN A 1 426  ? 203.231 173.109 286.544 1.00 96.18  ? 409  ASN B OD1 1 
ATOM   3297  N ND2 . ASN A 1 426  ? 204.052 175.106 285.931 1.00 96.18  ? 409  ASN B ND2 1 
ATOM   3298  N N   . ASN A 1 427  ? 199.540 171.998 285.941 1.00 98.47  ? 410  ASN B N   1 
ATOM   3299  C CA  . ASN A 1 427  ? 198.493 171.988 286.957 1.00 98.47  ? 410  ASN B CA  1 
ATOM   3300  C C   . ASN A 1 427  ? 199.064 171.989 288.369 1.00 98.47  ? 410  ASN B C   1 
ATOM   3301  O O   . ASN A 1 427  ? 198.485 172.608 289.268 1.00 98.47  ? 410  ASN B O   1 
ATOM   3302  C CB  . ASN A 1 427  ? 197.584 170.776 286.756 1.00 98.47  ? 410  ASN B CB  1 
ATOM   3303  C CG  . ASN A 1 427  ? 198.361 169.485 286.583 1.00 98.47  ? 410  ASN B CG  1 
ATOM   3304  O OD1 . ASN A 1 427  ? 199.323 169.222 287.306 1.00 98.47  ? 410  ASN B OD1 1 
ATOM   3305  N ND2 . ASN A 1 427  ? 197.949 168.673 285.617 1.00 98.47  ? 410  ASN B ND2 1 
ATOM   3306  N N   . MET A 1 428  ? 200.190 171.308 288.584 1.00 96.10  ? 411  MET B N   1 
ATOM   3307  C CA  . MET A 1 428  ? 200.721 171.127 289.929 1.00 96.10  ? 411  MET B CA  1 
ATOM   3308  C C   . MET A 1 428  ? 201.258 172.412 290.547 1.00 96.10  ? 411  MET B C   1 
ATOM   3309  O O   . MET A 1 428  ? 201.481 172.444 291.762 1.00 96.10  ? 411  MET B O   1 
ATOM   3310  C CB  . MET A 1 428  ? 201.824 170.068 289.911 1.00 96.10  ? 411  MET B CB  1 
ATOM   3311  C CG  . MET A 1 428  ? 202.526 169.936 288.571 1.00 96.10  ? 411  MET B CG  1 
ATOM   3312  S SD  . MET A 1 428  ? 203.910 168.784 288.616 1.00 96.10  ? 411  MET B SD  1 
ATOM   3313  C CE  . MET A 1 428  ? 204.587 169.005 286.972 1.00 96.10  ? 411  MET B CE  1 
ATOM   3314  N N   . ASN A 1 429  ? 201.466 173.466 289.758 1.00 91.90  ? 412  ASN B N   1 
ATOM   3315  C CA  . ASN A 1 429  ? 202.083 174.684 290.266 1.00 91.90  ? 412  ASN B CA  1 
ATOM   3316  C C   . ASN A 1 429  ? 201.081 175.742 290.705 1.00 91.90  ? 412  ASN B C   1 
ATOM   3317  O O   . ASN A 1 429  ? 201.439 176.612 291.505 1.00 91.90  ? 412  ASN B O   1 
ATOM   3318  C CB  . ASN A 1 429  ? 203.012 175.286 289.208 1.00 91.90  ? 412  ASN B CB  1 
ATOM   3319  C CG  . ASN A 1 429  ? 204.338 174.566 289.124 1.00 91.90  ? 412  ASN B CG  1 
ATOM   3320  O OD1 . ASN A 1 429  ? 205.206 174.931 288.332 1.00 91.90  ? 412  ASN B OD1 1 
ATOM   3321  N ND2 . ASN A 1 429  ? 204.505 173.536 289.944 1.00 91.90  ? 412  ASN B ND2 1 
ATOM   3322  N N   . PHE A 1 430  ? 199.847 175.693 290.211 1.00 87.20  ? 413  PHE B N   1 
ATOM   3323  C CA  . PHE A 1 430  ? 198.822 176.664 290.568 1.00 87.20  ? 413  PHE B CA  1 
ATOM   3324  C C   . PHE A 1 430  ? 197.611 175.928 291.115 1.00 87.20  ? 413  PHE B C   1 
ATOM   3325  O O   . PHE A 1 430  ? 197.157 174.949 290.515 1.00 87.20  ? 413  PHE B O   1 
ATOM   3326  C CB  . PHE A 1 430  ? 198.408 177.506 289.360 1.00 87.20  ? 413  PHE B CB  1 
ATOM   3327  C CG  . PHE A 1 430  ? 199.532 177.820 288.424 1.00 87.20  ? 413  PHE B CG  1 
ATOM   3328  C CD1 . PHE A 1 430  ? 200.564 178.648 288.814 1.00 87.20  ? 413  PHE B CD1 1 
ATOM   3329  C CD2 . PHE A 1 430  ? 199.551 177.293 287.148 1.00 87.20  ? 413  PHE B CD2 1 
ATOM   3330  C CE1 . PHE A 1 430  ? 201.595 178.941 287.951 1.00 87.20  ? 413  PHE B CE1 1 
ATOM   3331  C CE2 . PHE A 1 430  ? 200.580 177.582 286.282 1.00 87.20  ? 413  PHE B CE2 1 
ATOM   3332  C CZ  . PHE A 1 430  ? 201.604 178.407 286.683 1.00 87.20  ? 413  PHE B CZ  1 
ATOM   3333  N N   . THR A 1 431  ? 197.083 176.397 292.242 1.00 81.97  ? 414  THR B N   1 
ATOM   3334  C CA  . THR A 1 431  ? 195.863 175.839 292.813 1.00 81.97  ? 414  THR B CA  1 
ATOM   3335  C C   . THR A 1 431  ? 194.756 176.878 292.713 1.00 81.97  ? 414  THR B C   1 
ATOM   3336  O O   . THR A 1 431  ? 194.903 177.994 293.221 1.00 81.97  ? 414  THR B O   1 
ATOM   3337  C CB  . THR A 1 431  ? 196.072 175.415 294.266 1.00 81.97  ? 414  THR B CB  1 
ATOM   3338  O OG1 . THR A 1 431  ? 195.804 176.523 295.132 1.00 81.97  ? 414  THR B OG1 1 
ATOM   3339  C CG2 . THR A 1 431  ? 197.500 174.945 294.484 1.00 81.97  ? 414  THR B CG2 1 
ATOM   3340  N N   . LYS A 1 432  ? 193.659 176.515 292.055 1.00 77.02  ? 415  LYS B N   1 
ATOM   3341  C CA  . LYS A 1 432  ? 192.541 177.433 291.895 1.00 77.02  ? 415  LYS B CA  1 
ATOM   3342  C C   . LYS A 1 432  ? 191.838 177.650 293.227 1.00 77.02  ? 415  LYS B C   1 
ATOM   3343  O O   . LYS A 1 432  ? 191.648 176.712 294.006 1.00 77.02  ? 415  LYS B O   1 
ATOM   3344  C CB  . LYS A 1 432  ? 191.557 176.890 290.860 1.00 77.02  ? 415  LYS B CB  1 
ATOM   3345  C CG  . LYS A 1 432  ? 190.357 177.786 290.609 1.00 77.02  ? 415  LYS B CG  1 
ATOM   3346  C CD  . LYS A 1 432  ? 189.507 177.262 289.465 1.00 77.02  ? 415  LYS B CD  1 
ATOM   3347  C CE  . LYS A 1 432  ? 190.323 177.124 288.195 1.00 77.02  ? 415  LYS B CE  1 
ATOM   3348  N NZ  . LYS A 1 432  ? 191.039 178.385 287.865 1.00 77.02  ? 415  LYS B NZ  1 
ATOM   3349  N N   . LEU A 1 433  ? 191.447 178.894 293.489 1.00 74.58  ? 416  LEU B N   1 
ATOM   3350  C CA  . LEU A 1 433  ? 190.780 179.253 294.730 1.00 74.58  ? 416  LEU B CA  1 
ATOM   3351  C C   . LEU A 1 433  ? 189.428 179.887 294.434 1.00 74.58  ? 416  LEU B C   1 
ATOM   3352  O O   . LEU A 1 433  ? 189.162 180.348 293.322 1.00 74.58  ? 416  LEU B O   1 
ATOM   3353  C CB  . LEU A 1 433  ? 191.636 180.213 295.561 1.00 74.58  ? 416  LEU B CB  1 
ATOM   3354  C CG  . LEU A 1 433  ? 192.479 179.597 296.677 1.00 74.58  ? 416  LEU B CG  1 
ATOM   3355  C CD1 . LEU A 1 433  ? 193.396 178.512 296.144 1.00 74.58  ? 416  LEU B CD1 1 
ATOM   3356  C CD2 . LEU A 1 433  ? 193.287 180.674 297.359 1.00 74.58  ? 416  LEU B CD2 1 
ATOM   3357  N N   . LYS A 1 434  ? 188.572 179.904 295.452 1.00 77.51  ? 417  LYS B N   1 
ATOM   3358  C CA  . LYS A 1 434  ? 187.214 180.423 295.326 1.00 77.51  ? 417  LYS B CA  1 
ATOM   3359  C C   . LYS A 1 434  ? 187.229 181.918 295.620 1.00 77.51  ? 417  LYS B C   1 
ATOM   3360  O O   . LYS A 1 434  ? 187.403 182.331 296.771 1.00 77.51  ? 417  LYS B O   1 
ATOM   3361  C CB  . LYS A 1 434  ? 186.269 179.685 296.271 1.00 77.51  ? 417  LYS B CB  1 
ATOM   3362  C CG  . LYS A 1 434  ? 184.968 180.418 296.559 1.00 77.51  ? 417  LYS B CG  1 
ATOM   3363  C CD  . LYS A 1 434  ? 184.071 179.611 297.480 1.00 77.51  ? 417  LYS B CD  1 
ATOM   3364  C CE  . LYS A 1 434  ? 184.726 179.401 298.835 1.00 77.51  ? 417  LYS B CE  1 
ATOM   3365  N NZ  . LYS A 1 434  ? 183.738 179.475 299.945 1.00 77.51  ? 417  LYS B NZ  1 
ATOM   3366  N N   . ASN A 1 435  ? 187.052 182.729 294.582 1.00 74.74  ? 418  ASN B N   1 
ATOM   3367  C CA  . ASN A 1 435  ? 187.029 184.173 294.753 1.00 74.74  ? 418  ASN B CA  1 
ATOM   3368  C C   . ASN A 1 435  ? 185.675 184.613 295.288 1.00 74.74  ? 418  ASN B C   1 
ATOM   3369  O O   . ASN A 1 435  ? 184.639 184.036 294.949 1.00 74.74  ? 418  ASN B O   1 
ATOM   3370  C CB  . ASN A 1 435  ? 187.340 184.874 293.433 1.00 74.74  ? 418  ASN B CB  1 
ATOM   3371  C CG  . ASN A 1 435  ? 186.190 184.823 292.463 1.00 74.74  ? 418  ASN B CG  1 
ATOM   3372  O OD1 . ASN A 1 435  ? 185.347 185.715 292.438 1.00 74.74  ? 418  ASN B OD1 1 
ATOM   3373  N ND2 . ASN A 1 435  ? 186.145 183.772 291.654 1.00 74.74  ? 418  ASN B ND2 1 
ATOM   3374  N N   . PHE A 1 436  ? 185.689 185.642 296.136 1.00 79.70  ? 419  PHE B N   1 
ATOM   3375  C CA  . PHE A 1 436  ? 184.495 186.007 296.886 1.00 79.70  ? 419  PHE B CA  1 
ATOM   3376  C C   . PHE A 1 436  ? 183.519 186.865 296.096 1.00 79.70  ? 419  PHE B C   1 
ATOM   3377  O O   . PHE A 1 436  ? 182.372 187.019 296.526 1.00 79.70  ? 419  PHE B O   1 
ATOM   3378  C CB  . PHE A 1 436  ? 184.885 186.726 298.175 1.00 79.70  ? 419  PHE B CB  1 
ATOM   3379  C CG  . PHE A 1 436  ? 185.112 185.800 299.330 1.00 79.70  ? 419  PHE B CG  1 
ATOM   3380  C CD1 . PHE A 1 436  ? 185.922 184.686 299.189 1.00 79.70  ? 419  PHE B CD1 1 
ATOM   3381  C CD2 . PHE A 1 436  ? 184.506 186.033 300.551 1.00 79.70  ? 419  PHE B CD2 1 
ATOM   3382  C CE1 . PHE A 1 436  ? 186.131 183.826 300.246 1.00 79.70  ? 419  PHE B CE1 1 
ATOM   3383  C CE2 . PHE A 1 436  ? 184.710 185.174 301.614 1.00 79.70  ? 419  PHE B CE2 1 
ATOM   3384  C CZ  . PHE A 1 436  ? 185.524 184.070 301.461 1.00 79.70  ? 419  PHE B CZ  1 
ATOM   3385  N N   . THR A 1 437  ? 183.931 187.428 294.965 1.00 78.25  ? 420  THR B N   1 
ATOM   3386  C CA  . THR A 1 437  ? 183.015 188.206 294.139 1.00 78.25  ? 420  THR B CA  1 
ATOM   3387  C C   . THR A 1 437  ? 182.230 187.247 293.256 1.00 78.25  ? 420  THR B C   1 
ATOM   3388  O O   . THR A 1 437  ? 182.777 186.679 292.306 1.00 78.25  ? 420  THR B O   1 
ATOM   3389  C CB  . THR A 1 437  ? 183.770 189.227 293.295 1.00 78.25  ? 420  THR B CB  1 
ATOM   3390  O OG1 . THR A 1 437  ? 184.681 188.546 292.427 1.00 78.25  ? 420  THR B OG1 1 
ATOM   3391  C CG2 . THR A 1 437  ? 184.538 190.185 294.186 1.00 78.25  ? 420  THR B CG2 1 
ATOM   3392  N N   . GLY A 1 438  ? 180.948 187.071 293.563 1.00 80.31  ? 421  GLY B N   1 
ATOM   3393  C CA  . GLY A 1 438  ? 180.131 186.152 292.798 1.00 80.31  ? 421  GLY B CA  1 
ATOM   3394  C C   . GLY A 1 438  ? 180.034 186.552 291.340 1.00 80.31  ? 421  GLY B C   1 
ATOM   3395  O O   . GLY A 1 438  ? 180.228 187.708 290.962 1.00 80.31  ? 421  GLY B O   1 
ATOM   3396  N N   . LEU A 1 439  ? 179.738 185.557 290.503 1.00 80.19  ? 422  LEU B N   1 
ATOM   3397  C CA  . LEU A 1 439  ? 179.674 185.795 289.066 1.00 80.19  ? 422  LEU B CA  1 
ATOM   3398  C C   . LEU A 1 439  ? 178.564 186.774 288.706 1.00 80.19  ? 422  LEU B C   1 
ATOM   3399  O O   . LEU A 1 439  ? 178.646 187.451 287.676 1.00 80.19  ? 422  LEU B O   1 
ATOM   3400  C CB  . LEU A 1 439  ? 179.485 184.476 288.308 1.00 80.19  ? 422  LEU B CB  1 
ATOM   3401  C CG  . LEU A 1 439  ? 178.299 183.539 288.576 1.00 80.19  ? 422  LEU B CG  1 
ATOM   3402  C CD1 . LEU A 1 439  ? 178.246 182.472 287.495 1.00 80.19  ? 422  LEU B CD1 1 
ATOM   3403  C CD2 . LEU A 1 439  ? 178.359 182.874 289.946 1.00 80.19  ? 422  LEU B CD2 1 
ATOM   3404  N N   . PHE A 1 440  ? 177.531 186.874 289.542 1.00 76.05  ? 423  PHE B N   1 
ATOM   3405  C CA  . PHE A 1 440  ? 176.386 187.737 289.284 1.00 76.05  ? 423  PHE B CA  1 
ATOM   3406  C C   . PHE A 1 440  ? 176.167 188.731 290.420 1.00 76.05  ? 423  PHE B C   1 
ATOM   3407  O O   . PHE A 1 440  ? 175.034 189.120 290.702 1.00 76.05  ? 423  PHE B O   1 
ATOM   3408  C CB  . PHE A 1 440  ? 175.131 186.896 289.058 1.00 76.05  ? 423  PHE B CB  1 
ATOM   3409  C CG  . PHE A 1 440  ? 174.978 186.404 287.649 1.00 76.05  ? 423  PHE B CG  1 
ATOM   3410  C CD1 . PHE A 1 440  ? 175.829 186.843 286.653 1.00 76.05  ? 423  PHE B CD1 1 
ATOM   3411  C CD2 . PHE A 1 440  ? 174.006 185.475 287.330 1.00 76.05  ? 423  PHE B CD2 1 
ATOM   3412  C CE1 . PHE A 1 440  ? 175.696 186.386 285.360 1.00 76.05  ? 423  PHE B CE1 1 
ATOM   3413  C CE2 . PHE A 1 440  ? 173.871 185.010 286.039 1.00 76.05  ? 423  PHE B CE2 1 
ATOM   3414  C CZ  . PHE A 1 440  ? 174.718 185.466 285.053 1.00 76.05  ? 423  PHE B CZ  1 
ATOM   3415  N N   . GLU A 1 441  ? 177.245 189.135 291.094 1.00 84.01  ? 424  GLU B N   1 
ATOM   3416  C CA  . GLU A 1 441  ? 177.110 190.091 292.188 1.00 84.01  ? 424  GLU B CA  1 
ATOM   3417  C C   . GLU A 1 441  ? 176.868 191.502 291.669 1.00 84.01  ? 424  GLU B C   1 
ATOM   3418  O O   . GLU A 1 441  ? 176.026 192.231 292.207 1.00 84.01  ? 424  GLU B O   1 
ATOM   3419  C CB  . GLU A 1 441  ? 178.349 190.049 293.077 1.00 84.01  ? 424  GLU B CB  1 
ATOM   3420  C CG  . GLU A 1 441  ? 178.279 188.990 294.162 1.00 84.01  ? 424  GLU B CG  1 
ATOM   3421  C CD  . GLU A 1 441  ? 179.129 189.332 295.365 1.00 84.01  ? 424  GLU B CD  1 
ATOM   3422  O OE1 . GLU A 1 441  ? 179.408 190.531 295.568 1.00 84.01  ? 424  GLU B OE1 1 
ATOM   3423  O OE2 . GLU A 1 441  ? 179.516 188.404 296.106 1.00 84.01  ? 424  GLU B OE2 1 
ATOM   3424  N N   . PHE A 1 442  ? 177.595 191.908 290.632 1.00 83.83  ? 425  PHE B N   1 
ATOM   3425  C CA  . PHE A 1 442  ? 177.433 193.219 290.005 1.00 83.83  ? 425  PHE B CA  1 
ATOM   3426  C C   . PHE A 1 442  ? 176.987 192.973 288.569 1.00 83.83  ? 425  PHE B C   1 
ATOM   3427  O O   . PHE A 1 442  ? 177.792 192.574 287.723 1.00 83.83  ? 425  PHE B O   1 
ATOM   3428  C CB  . PHE A 1 442  ? 178.726 194.021 290.068 1.00 83.83  ? 425  PHE B CB  1 
ATOM   3429  C CG  . PHE A 1 442  ? 179.017 194.580 291.428 1.00 83.83  ? 425  PHE B CG  1 
ATOM   3430  C CD1 . PHE A 1 442  ? 178.017 195.187 292.166 1.00 83.83  ? 425  PHE B CD1 1 
ATOM   3431  C CD2 . PHE A 1 442  ? 180.281 194.481 291.978 1.00 83.83  ? 425  PHE B CD2 1 
ATOM   3432  C CE1 . PHE A 1 442  ? 178.276 195.697 293.421 1.00 83.83  ? 425  PHE B CE1 1 
ATOM   3433  C CE2 . PHE A 1 442  ? 180.545 194.987 293.233 1.00 83.83  ? 425  PHE B CE2 1 
ATOM   3434  C CZ  . PHE A 1 442  ? 179.541 195.595 293.955 1.00 83.83  ? 425  PHE B CZ  1 
ATOM   3435  N N   . TYR A 1 443  ? 175.708 193.212 288.294 1.00 76.13  ? 426  TYR B N   1 
ATOM   3436  C CA  . TYR A 1 443  ? 175.110 192.793 287.038 1.00 76.13  ? 426  TYR B CA  1 
ATOM   3437  C C   . TYR A 1 443  ? 174.153 193.858 286.529 1.00 76.13  ? 426  TYR B C   1 
ATOM   3438  O O   . TYR A 1 443  ? 173.804 194.809 287.232 1.00 76.13  ? 426  TYR B O   1 
ATOM   3439  C CB  . TYR A 1 443  ? 174.371 191.461 287.197 1.00 76.13  ? 426  TYR B CB  1 
ATOM   3440  C CG  . TYR A 1 443  ? 173.185 191.524 288.134 1.00 76.13  ? 426  TYR B CG  1 
ATOM   3441  C CD1 . TYR A 1 443  ? 173.352 191.405 289.503 1.00 76.13  ? 426  TYR B CD1 1 
ATOM   3442  C CD2 . TYR A 1 443  ? 171.899 191.695 287.646 1.00 76.13  ? 426  TYR B CD2 1 
ATOM   3443  C CE1 . TYR A 1 443  ? 172.275 191.458 290.360 1.00 76.13  ? 426  TYR B CE1 1 
ATOM   3444  C CE2 . TYR A 1 443  ? 170.816 191.749 288.496 1.00 76.13  ? 426  TYR B CE2 1 
ATOM   3445  C CZ  . TYR A 1 443  ? 171.010 191.631 289.851 1.00 76.13  ? 426  TYR B CZ  1 
ATOM   3446  O OH  . TYR A 1 443  ? 169.932 191.684 290.702 1.00 76.13  ? 426  TYR B OH  1 
ATOM   3447  N N   . LYS A 1 444  ? 173.740 193.685 285.279 1.00 73.23  ? 427  LYS B N   1 
ATOM   3448  C CA  . LYS A 1 444  ? 172.682 194.469 284.663 1.00 73.23  ? 427  LYS B CA  1 
ATOM   3449  C C   . LYS A 1 444  ? 171.590 193.518 284.199 1.00 73.23  ? 427  LYS B C   1 
ATOM   3450  O O   . LYS A 1 444  ? 171.878 192.465 283.625 1.00 73.23  ? 427  LYS B O   1 
ATOM   3451  C CB  . LYS A 1 444  ? 173.208 195.287 283.483 1.00 73.23  ? 427  LYS B CB  1 
ATOM   3452  C CG  . LYS A 1 444  ? 173.681 196.683 283.845 1.00 73.23  ? 427  LYS B CG  1 
ATOM   3453  C CD  . LYS A 1 444  ? 174.341 197.354 282.653 1.00 73.23  ? 427  LYS B CD  1 
ATOM   3454  C CE  . LYS A 1 444  ? 174.092 198.853 282.636 1.00 73.23  ? 427  LYS B CE  1 
ATOM   3455  N NZ  . LYS A 1 444  ? 174.389 199.489 283.946 1.00 73.23  ? 427  LYS B NZ  1 
ATOM   3456  N N   . LEU A 1 445  ? 170.340 193.887 284.450 1.00 72.25  ? 428  LEU B N   1 
ATOM   3457  C CA  . LEU A 1 445  ? 169.192 193.022 284.188 1.00 72.25  ? 428  LEU B CA  1 
ATOM   3458  C C   . LEU A 1 445  ? 168.532 193.468 282.889 1.00 72.25  ? 428  LEU B C   1 
ATOM   3459  O O   . LEU A 1 445  ? 167.776 194.441 282.870 1.00 72.25  ? 428  LEU B O   1 
ATOM   3460  C CB  . LEU A 1 445  ? 168.221 193.072 285.362 1.00 72.25  ? 428  LEU B CB  1 
ATOM   3461  C CG  . LEU A 1 445  ? 167.251 191.915 285.569 1.00 72.25  ? 428  LEU B CG  1 
ATOM   3462  C CD1 . LEU A 1 445  ? 166.949 191.755 287.043 1.00 72.25  ? 428  LEU B CD1 1 
ATOM   3463  C CD2 . LEU A 1 445  ? 165.977 192.179 284.806 1.00 72.25  ? 428  LEU B CD2 1 
ATOM   3464  N N   . LEU A 1 446  ? 168.807 192.751 281.803 1.00 73.55  ? 429  LEU B N   1 
ATOM   3465  C CA  . LEU A 1 446  ? 168.279 193.097 280.492 1.00 73.55  ? 429  LEU B CA  1 
ATOM   3466  C C   . LEU A 1 446  ? 167.153 192.149 280.112 1.00 73.55  ? 429  LEU B C   1 
ATOM   3467  O O   . LEU A 1 446  ? 167.203 190.957 280.429 1.00 73.55  ? 429  LEU B O   1 
ATOM   3468  C CB  . LEU A 1 446  ? 169.365 193.033 279.418 1.00 73.55  ? 429  LEU B CB  1 
ATOM   3469  C CG  . LEU A 1 446  ? 170.713 193.699 279.664 1.00 73.55  ? 429  LEU B CG  1 
ATOM   3470  C CD1 . LEU A 1 446  ? 171.692 192.699 280.223 1.00 73.55  ? 429  LEU B CD1 1 
ATOM   3471  C CD2 . LEU A 1 446  ? 171.243 194.280 278.373 1.00 73.55  ? 429  LEU B CD2 1 
ATOM   3472  N N   . CYS A 1 447  ? 166.143 192.681 279.429 1.00 83.67  ? 430  CYS B N   1 
ATOM   3473  C CA  . CYS A 1 447  ? 165.107 191.850 278.828 1.00 83.67  ? 430  CYS B CA  1 
ATOM   3474  C C   . CYS A 1 447  ? 164.287 192.670 277.846 1.00 83.67  ? 430  CYS B C   1 
ATOM   3475  O O   . CYS A 1 447  ? 164.397 193.896 277.775 1.00 83.67  ? 430  CYS B O   1 
ATOM   3476  C CB  . CYS A 1 447  ? 164.198 191.201 279.870 1.00 83.67  ? 430  CYS B CB  1 
ATOM   3477  S SG  . CYS A 1 447  ? 163.855 192.121 281.377 1.00 83.67  ? 430  CYS B SG  1 
ATOM   3478  N N   . VAL A 1 448  ? 163.454 191.962 277.096 1.00 87.22  ? 431  VAL B N   1 
ATOM   3479  C CA  . VAL A 1 448  ? 162.636 192.548 276.063 1.00 87.22  ? 431  VAL B CA  1 
ATOM   3480  C C   . VAL A 1 448  ? 161.208 192.666 276.584 1.00 87.22  ? 431  VAL B C   1 
ATOM   3481  O O   . VAL A 1 448  ? 160.859 192.126 277.630 1.00 87.22  ? 431  VAL B O   1 
ATOM   3482  C CB  . VAL A 1 448  ? 162.704 191.722 274.755 1.00 87.22  ? 431  VAL B CB  1 
ATOM   3483  C CG1 . VAL A 1 448  ? 161.701 190.585 274.793 1.00 87.22  ? 431  VAL B CG1 1 
ATOM   3484  C CG2 . VAL A 1 448  ? 162.484 192.604 273.541 1.00 87.22  ? 431  VAL B CG2 1 
ATOM   3485  N N   . ARG A 1 449  ? 160.371 193.398 275.853 1.00 89.96  ? 432  ARG B N   1 
ATOM   3486  C CA  . ARG A 1 449  ? 158.973 193.573 276.234 1.00 89.96  ? 432  ARG B CA  1 
ATOM   3487  C C   . ARG A 1 449  ? 158.241 192.238 276.268 1.00 89.96  ? 432  ARG B C   1 
ATOM   3488  O O   . ARG A 1 449  ? 158.194 191.522 275.268 1.00 89.96  ? 432  ARG B O   1 
ATOM   3489  C CB  . ARG A 1 449  ? 158.264 194.525 275.272 1.00 89.96  ? 432  ARG B CB  1 
ATOM   3490  C CG  . ARG A 1 449  ? 159.182 195.506 274.569 1.00 89.96  ? 432  ARG B CG  1 
ATOM   3491  C CD  . ARG A 1 449  ? 158.408 196.706 274.047 1.00 89.96  ? 432  ARG B CD  1 
ATOM   3492  N NE  . ARG A 1 449  ? 157.916 197.548 275.130 1.00 89.96  ? 432  ARG B NE  1 
ATOM   3493  C CZ  . ARG A 1 449  ? 158.647 198.452 275.766 1.00 89.96  ? 432  ARG B CZ  1 
ATOM   3494  N NH1 . ARG A 1 449  ? 159.911 198.669 275.445 1.00 89.96  ? 432  ARG B NH1 1 
ATOM   3495  N NH2 . ARG A 1 449  ? 158.095 199.156 276.751 1.00 89.96  ? 432  ARG B NH2 1 
ATOM   3496  N N   . ASP A 1 469  ? 157.804 187.355 281.039 1.00 102.17 ? 452  ASP B N   1 
ATOM   3497  C CA  . ASP A 1 469  ? 158.927 187.755 280.199 1.00 102.17 ? 452  ASP B CA  1 
ATOM   3498  C C   . ASP A 1 469  ? 160.155 186.889 280.468 1.00 102.17 ? 452  ASP B C   1 
ATOM   3499  O O   . ASP A 1 469  ? 160.104 185.949 281.261 1.00 102.17 ? 452  ASP B O   1 
ATOM   3500  C CB  . ASP A 1 469  ? 159.262 189.232 280.419 1.00 102.17 ? 452  ASP B CB  1 
ATOM   3501  C CG  . ASP A 1 469  ? 159.242 189.624 281.886 1.00 102.17 ? 452  ASP B CG  1 
ATOM   3502  O OD1 . ASP A 1 469  ? 159.434 188.740 282.746 1.00 102.17 ? 452  ASP B OD1 1 
ATOM   3503  O OD2 . ASP A 1 469  ? 159.034 190.821 282.178 1.00 102.17 ? 452  ASP B OD2 1 
ATOM   3504  N N   . LEU A 1 470  ? 161.260 187.215 279.800 1.00 89.51  ? 453  LEU B N   1 
ATOM   3505  C CA  . LEU A 1 470  ? 162.516 186.472 279.913 1.00 89.51  ? 453  LEU B CA  1 
ATOM   3506  C C   . LEU A 1 470  ? 163.635 187.476 280.192 1.00 89.51  ? 453  LEU B C   1 
ATOM   3507  O O   . LEU A 1 470  ? 164.260 188.022 279.280 1.00 89.51  ? 453  LEU B O   1 
ATOM   3508  C CB  . LEU A 1 470  ? 162.766 185.620 278.652 1.00 89.51  ? 453  LEU B CB  1 
ATOM   3509  C CG  . LEU A 1 470  ? 163.170 186.155 277.269 1.00 89.51  ? 453  LEU B CG  1 
ATOM   3510  C CD1 . LEU A 1 470  ? 163.153 185.030 276.247 1.00 89.51  ? 453  LEU B CD1 1 
ATOM   3511  C CD2 . LEU A 1 470  ? 162.287 187.305 276.804 1.00 89.51  ? 453  LEU B CD2 1 
ATOM   3512  N N   . CYS A 1 471  ? 163.884 187.729 281.473 1.00 85.67  ? 454  CYS B N   1 
ATOM   3513  C CA  . CYS A 1 471  ? 164.893 188.690 281.894 1.00 85.67  ? 454  CYS B CA  1 
ATOM   3514  C C   . CYS A 1 471  ? 166.158 187.960 282.317 1.00 85.67  ? 454  CYS B C   1 
ATOM   3515  O O   . CYS A 1 471  ? 166.107 187.047 283.147 1.00 85.67  ? 454  CYS B O   1 
ATOM   3516  C CB  . CYS A 1 471  ? 164.377 189.574 283.032 1.00 85.67  ? 454  CYS B CB  1 
ATOM   3517  S SG  . CYS A 1 471  ? 163.024 190.715 282.593 1.00 85.67  ? 454  CYS B SG  1 
ATOM   3518  N N   . ILE A 1 472  ? 167.287 188.364 281.742 1.00 73.24  ? 455  ILE B N   1 
ATOM   3519  C CA  . ILE A 1 472  ? 168.573 187.734 282.003 1.00 73.24  ? 455  ILE B CA  1 
ATOM   3520  C C   . ILE A 1 472  ? 169.500 188.754 282.647 1.00 73.24  ? 455  ILE B C   1 
ATOM   3521  O O   . ILE A 1 472  ? 169.484 189.941 282.299 1.00 73.24  ? 455  ILE B O   1 
ATOM   3522  C CB  . ILE A 1 472  ? 169.200 187.144 280.722 1.00 73.24  ? 455  ILE B CB  1 
ATOM   3523  C CG1 . ILE A 1 472  ? 169.700 188.245 279.789 1.00 73.24  ? 455  ILE B CG1 1 
ATOM   3524  C CG2 . ILE A 1 472  ? 168.202 186.259 280.002 1.00 73.24  ? 455  ILE B CG2 1 
ATOM   3525  C CD1 . ILE A 1 472  ? 170.743 187.776 278.806 1.00 73.24  ? 455  ILE B CD1 1 
ATOM   3526  N N   . LYS A 1 473  ? 170.290 188.288 283.607 1.00 72.78  ? 456  LYS B N   1 
ATOM   3527  C CA  . LYS A 1 473  ? 171.284 189.105 284.283 1.00 72.78  ? 456  LYS B CA  1 
ATOM   3528  C C   . LYS A 1 473  ? 172.635 188.881 283.622 1.00 72.78  ? 456  LYS B C   1 
ATOM   3529  O O   . LYS A 1 473  ? 173.073 187.737 283.467 1.00 72.78  ? 456  LYS B O   1 
ATOM   3530  C CB  . LYS A 1 473  ? 171.351 188.752 285.768 1.00 72.78  ? 456  LYS B CB  1 
ATOM   3531  C CG  . LYS A 1 473  ? 170.003 188.396 286.366 1.00 72.78  ? 456  LYS B CG  1 
ATOM   3532  C CD  . LYS A 1 473  ? 170.060 188.265 287.878 1.00 72.78  ? 456  LYS B CD  1 
ATOM   3533  C CE  . LYS A 1 473  ? 170.968 187.128 288.308 1.00 72.78  ? 456  LYS B CE  1 
ATOM   3534  N NZ  . LYS A 1 473  ? 171.100 187.058 289.789 1.00 72.78  ? 456  LYS B NZ  1 
ATOM   3535  N N   . VAL A 1 474  ? 173.289 189.969 283.229 1.00 72.10  ? 457  VAL B N   1 
ATOM   3536  C CA  . VAL A 1 474  ? 174.586 189.920 282.567 1.00 72.10  ? 457  VAL B CA  1 
ATOM   3537  C C   . VAL A 1 474  ? 175.612 190.573 283.478 1.00 72.10  ? 457  VAL B C   1 
ATOM   3538  O O   . VAL A 1 474  ? 175.389 191.682 283.979 1.00 72.10  ? 457  VAL B O   1 
ATOM   3539  C CB  . VAL A 1 474  ? 174.543 190.610 281.195 1.00 72.10  ? 457  VAL B CB  1 
ATOM   3540  C CG1 . VAL A 1 474  ? 175.944 190.919 280.715 1.00 72.10  ? 457  VAL B CG1 1 
ATOM   3541  C CG2 . VAL A 1 474  ? 173.824 189.729 280.196 1.00 72.10  ? 457  VAL B CG2 1 
ATOM   3542  N N   . ASN A 1 475  ? 176.729 189.883 283.695 1.00 77.85  ? 458  ASN B N   1 
ATOM   3543  C CA  . ASN A 1 475  ? 177.764 190.377 284.592 1.00 77.85  ? 458  ASN B CA  1 
ATOM   3544  C C   . ASN A 1 475  ? 178.309 191.711 284.098 1.00 77.85  ? 458  ASN B C   1 
ATOM   3545  O O   . ASN A 1 475  ? 178.437 191.940 282.893 1.00 77.85  ? 458  ASN B O   1 
ATOM   3546  C CB  . ASN A 1 475  ? 178.890 189.350 284.700 1.00 77.85  ? 458  ASN B CB  1 
ATOM   3547  C CG  . ASN A 1 475  ? 179.835 189.639 285.842 1.00 77.85  ? 458  ASN B CG  1 
ATOM   3548  O OD1 . ASN A 1 475  ? 179.675 190.623 286.561 1.00 77.85  ? 458  ASN B OD1 1 
ATOM   3549  N ND2 . ASN A 1 475  ? 180.828 188.777 286.019 1.00 77.85  ? 458  ASN B ND2 1 
ATOM   3550  N N   . ASN A 1 476  ? 178.623 192.600 285.041 1.00 76.68  ? 459  ASN B N   1 
ATOM   3551  C CA  . ASN A 1 476  ? 179.104 193.926 284.668 1.00 76.68  ? 459  ASN B CA  1 
ATOM   3552  C C   . ASN A 1 476  ? 180.427 193.858 283.920 1.00 76.68  ? 459  ASN B C   1 
ATOM   3553  O O   . ASN A 1 476  ? 180.701 194.710 283.069 1.00 76.68  ? 459  ASN B O   1 
ATOM   3554  C CB  . ASN A 1 476  ? 179.249 194.804 285.908 1.00 76.68  ? 459  ASN B CB  1 
ATOM   3555  C CG  . ASN A 1 476  ? 180.001 196.085 285.626 1.00 76.68  ? 459  ASN B CG  1 
ATOM   3556  O OD1 . ASN A 1 476  ? 179.655 196.833 284.715 1.00 76.68  ? 459  ASN B OD1 1 
ATOM   3557  N ND2 . ASN A 1 476  ? 181.037 196.347 286.412 1.00 76.68  ? 459  ASN B ND2 1 
ATOM   3558  N N   . TRP A 1 477  ? 181.254 192.858 284.212 1.00 75.75  ? 460  TRP B N   1 
ATOM   3559  C CA  . TRP A 1 477  ? 182.550 192.710 283.564 1.00 75.75  ? 460  TRP B CA  1 
ATOM   3560  C C   . TRP A 1 477  ? 182.455 192.030 282.214 1.00 75.75  ? 460  TRP B C   1 
ATOM   3561  O O   . TRP A 1 477  ? 183.463 191.525 281.706 1.00 75.75  ? 460  TRP B O   1 
ATOM   3562  C CB  . TRP A 1 477  ? 183.505 191.944 284.481 1.00 75.75  ? 460  TRP B CB  1 
ATOM   3563  C CG  . TRP A 1 477  ? 183.455 192.439 285.883 1.00 75.75  ? 460  TRP B CG  1 
ATOM   3564  C CD1 . TRP A 1 477  ? 183.037 191.752 286.980 1.00 75.75  ? 460  TRP B CD1 1 
ATOM   3565  C CD2 . TRP A 1 477  ? 183.822 193.743 286.340 1.00 75.75  ? 460  TRP B CD2 1 
ATOM   3566  N NE1 . TRP A 1 477  ? 183.125 192.545 288.096 1.00 75.75  ? 460  TRP B NE1 1 
ATOM   3567  C CE2 . TRP A 1 477  ? 183.604 193.774 287.728 1.00 75.75  ? 460  TRP B CE2 1 
ATOM   3568  C CE3 . TRP A 1 477  ? 184.316 194.887 285.710 1.00 75.75  ? 460  TRP B CE3 1 
ATOM   3569  C CZ2 . TRP A 1 477  ? 183.864 194.901 288.497 1.00 75.75  ? 460  TRP B CZ2 1 
ATOM   3570  C CZ3 . TRP A 1 477  ? 184.572 196.004 286.473 1.00 75.75  ? 460  TRP B CZ3 1 
ATOM   3571  C CH2 . TRP A 1 477  ? 184.347 196.005 287.852 1.00 75.75  ? 460  TRP B CH2 1 
ATOM   3572  N N   . ASP A 1 478  ? 181.266 192.006 281.625 1.00 73.72  ? 461  ASP B N   1 
ATOM   3573  C CA  . ASP A 1 478  ? 181.025 191.416 280.317 1.00 73.72  ? 461  ASP B CA  1 
ATOM   3574  C C   . ASP A 1 478  ? 180.171 192.385 279.502 1.00 73.72  ? 461  ASP B C   1 
ATOM   3575  O O   . ASP A 1 478  ? 179.115 192.048 278.965 1.00 73.72  ? 461  ASP B O   1 
ATOM   3576  C CB  . ASP A 1 478  ? 180.384 190.038 280.507 1.00 73.72  ? 461  ASP B CB  1 
ATOM   3577  C CG  . ASP A 1 478  ? 180.110 189.303 279.199 1.00 73.72  ? 461  ASP B CG  1 
ATOM   3578  O OD1 . ASP A 1 478  ? 180.118 189.908 278.111 1.00 73.72  ? 461  ASP B OD1 1 
ATOM   3579  O OD2 . ASP A 1 478  ? 179.876 188.079 279.272 1.00 73.72  ? 461  ASP B OD2 1 
ATOM   3580  N N   . LEU A 1 479  ? 180.594 193.646 279.470 1.00 70.13  ? 462  LEU B N   1 
ATOM   3581  C CA  . LEU A 1 479  ? 179.886 194.688 278.743 1.00 70.13  ? 462  LEU B CA  1 
ATOM   3582  C C   . LEU A 1 479  ? 180.899 195.594 278.061 1.00 70.13  ? 462  LEU B C   1 
ATOM   3583  O O   . LEU A 1 479  ? 182.077 195.627 278.423 1.00 70.13  ? 462  LEU B O   1 
ATOM   3584  C CB  . LEU A 1 479  ? 178.970 195.508 279.661 1.00 70.13  ? 462  LEU B CB  1 
ATOM   3585  C CG  . LEU A 1 479  ? 177.896 194.749 280.442 1.00 70.13  ? 462  LEU B CG  1 
ATOM   3586  C CD1 . LEU A 1 479  ? 177.355 195.596 281.575 1.00 70.13  ? 462  LEU B CD1 1 
ATOM   3587  C CD2 . LEU A 1 479  ? 176.777 194.322 279.520 1.00 70.13  ? 462  LEU B CD2 1 
ATOM   3588  N N   . PHE A 1 480  ? 180.425 196.332 277.064 1.00 72.04  ? 463  PHE B N   1 
ATOM   3589  C CA  . PHE A 1 480  ? 181.312 197.137 276.239 1.00 72.04  ? 463  PHE B CA  1 
ATOM   3590  C C   . PHE A 1 480  ? 181.858 198.330 277.016 1.00 72.04  ? 463  PHE B C   1 
ATOM   3591  O O   . PHE A 1 480  ? 181.197 198.887 277.895 1.00 72.04  ? 463  PHE B O   1 
ATOM   3592  C CB  . PHE A 1 480  ? 180.584 197.611 274.984 1.00 72.04  ? 463  PHE B CB  1 
ATOM   3593  C CG  . PHE A 1 480  ? 180.327 196.518 273.993 1.00 72.04  ? 463  PHE B CG  1 
ATOM   3594  C CD1 . PHE A 1 480  ? 179.312 195.602 274.201 1.00 72.04  ? 463  PHE B CD1 1 
ATOM   3595  C CD2 . PHE A 1 480  ? 181.103 196.399 272.858 1.00 72.04  ? 463  PHE B CD2 1 
ATOM   3596  C CE1 . PHE A 1 480  ? 179.076 194.593 273.295 1.00 72.04  ? 463  PHE B CE1 1 
ATOM   3597  C CE2 . PHE A 1 480  ? 180.869 195.391 271.948 1.00 72.04  ? 463  PHE B CE2 1 
ATOM   3598  C CZ  . PHE A 1 480  ? 179.855 194.488 272.168 1.00 72.04  ? 463  PHE B CZ  1 
ATOM   3599  N N   . PHE A 1 481  ? 183.083 198.717 276.676 1.00 71.76  ? 464  PHE B N   1 
ATOM   3600  C CA  . PHE A 1 481  ? 183.785 199.816 277.327 1.00 71.76  ? 464  PHE B CA  1 
ATOM   3601  C C   . PHE A 1 481  ? 183.705 201.033 276.414 1.00 71.76  ? 464  PHE B C   1 
ATOM   3602  O O   . PHE A 1 481  ? 184.348 201.067 275.361 1.00 71.76  ? 464  PHE B O   1 
ATOM   3603  C CB  . PHE A 1 481  ? 185.232 199.420 277.611 1.00 71.76  ? 464  PHE B CB  1 
ATOM   3604  C CG  . PHE A 1 481  ? 186.096 200.549 278.086 1.00 71.76  ? 464  PHE B CG  1 
ATOM   3605  C CD1 . PHE A 1 481  ? 186.072 200.947 279.410 1.00 71.76  ? 464  PHE B CD1 1 
ATOM   3606  C CD2 . PHE A 1 481  ? 186.949 201.200 277.213 1.00 71.76  ? 464  PHE B CD2 1 
ATOM   3607  C CE1 . PHE A 1 481  ? 186.871 201.979 279.850 1.00 71.76  ? 464  PHE B CE1 1 
ATOM   3608  C CE2 . PHE A 1 481  ? 187.750 202.234 277.649 1.00 71.76  ? 464  PHE B CE2 1 
ATOM   3609  C CZ  . PHE A 1 481  ? 187.711 202.624 278.969 1.00 71.76  ? 464  PHE B CZ  1 
ATOM   3610  N N   . SER A 1 482  ? 182.922 202.031 276.816 1.00 75.74  ? 465  SER B N   1 
ATOM   3611  C CA  . SER A 1 482  ? 182.654 203.200 275.978 1.00 75.74  ? 465  SER B CA  1 
ATOM   3612  C C   . SER A 1 482  ? 183.176 204.463 276.643 1.00 75.74  ? 465  SER B C   1 
ATOM   3613  O O   . SER A 1 482  ? 182.477 205.062 277.479 1.00 75.74  ? 465  SER B O   1 
ATOM   3614  C CB  . SER A 1 482  ? 181.159 203.330 275.708 1.00 75.74  ? 465  SER B CB  1 
ATOM   3615  O OG  . SER A 1 482  ? 180.421 203.039 276.878 1.00 75.74  ? 465  SER B OG  1 
ATOM   3616  N N   . PRO A 1 483  ? 184.382 204.911 276.310 1.00 75.21  ? 466  PRO B N   1 
ATOM   3617  C CA  . PRO A 1 483  ? 184.894 206.149 276.902 1.00 75.21  ? 466  PRO B CA  1 
ATOM   3618  C C   . PRO A 1 483  ? 184.102 207.357 276.434 1.00 75.21  ? 466  PRO B C   1 
ATOM   3619  O O   . PRO A 1 483  ? 183.586 207.398 275.316 1.00 75.21  ? 466  PRO B O   1 
ATOM   3620  C CB  . PRO A 1 483  ? 186.341 206.208 276.406 1.00 75.21  ? 466  PRO B CB  1 
ATOM   3621  C CG  . PRO A 1 483  ? 186.338 205.407 275.156 1.00 75.21  ? 466  PRO B CG  1 
ATOM   3622  C CD  . PRO A 1 483  ? 185.334 204.315 275.360 1.00 75.21  ? 466  PRO B CD  1 
ATOM   3623  N N   . SER A 1 484  ? 184.013 208.351 277.311 1.00 79.68  ? 467  SER B N   1 
ATOM   3624  C CA  . SER A 1 484  ? 183.308 209.579 276.991 1.00 79.68  ? 467  SER B CA  1 
ATOM   3625  C C   . SER A 1 484  ? 184.172 210.474 276.109 1.00 79.68  ? 467  SER B C   1 
ATOM   3626  O O   . SER A 1 484  ? 185.383 210.283 275.974 1.00 79.68  ? 467  SER B O   1 
ATOM   3627  C CB  . SER A 1 484  ? 182.910 210.315 278.268 1.00 79.68  ? 467  SER B CB  1 
ATOM   3628  O OG  . SER A 1 484  ? 182.165 211.483 277.971 1.00 79.68  ? 467  SER B OG  1 
ATOM   3629  N N   . GLU A 1 485  ? 183.531 211.470 275.500 1.00 82.30  ? 468  GLU B N   1 
ATOM   3630  C CA  . GLU A 1 485  ? 184.236 212.408 274.638 1.00 82.30  ? 468  GLU B CA  1 
ATOM   3631  C C   . GLU A 1 485  ? 185.027 213.451 275.414 1.00 82.30  ? 468  GLU B C   1 
ATOM   3632  O O   . GLU A 1 485  ? 185.793 214.202 274.802 1.00 82.30  ? 468  GLU B O   1 
ATOM   3633  C CB  . GLU A 1 485  ? 183.247 213.111 273.706 1.00 82.30  ? 468  GLU B CB  1 
ATOM   3634  C CG  . GLU A 1 485  ? 182.095 213.792 274.427 1.00 82.30  ? 468  GLU B CG  1 
ATOM   3635  C CD  . GLU A 1 485  ? 180.865 213.945 273.553 1.00 82.30  ? 468  GLU B CD  1 
ATOM   3636  O OE1 . GLU A 1 485  ? 180.828 214.891 272.737 1.00 82.30  ? 468  GLU B OE1 1 
ATOM   3637  O OE2 . GLU A 1 485  ? 179.936 213.121 273.680 1.00 82.30  ? 468  GLU B OE2 1 
ATOM   3638  N N   . ASP A 1 486  ? 184.859 213.521 276.736 1.00 82.68  ? 469  ASP B N   1 
ATOM   3639  C CA  . ASP A 1 486  ? 185.567 214.528 277.519 1.00 82.68  ? 469  ASP B CA  1 
ATOM   3640  C C   . ASP A 1 486  ? 187.055 214.222 277.628 1.00 82.68  ? 469  ASP B C   1 
ATOM   3641  O O   . ASP A 1 486  ? 187.869 215.147 277.725 1.00 82.68  ? 469  ASP B O   1 
ATOM   3642  C CB  . ASP A 1 486  ? 184.946 214.637 278.910 1.00 82.68  ? 469  ASP B CB  1 
ATOM   3643  C CG  . ASP A 1 486  ? 185.333 215.918 279.622 1.00 82.68  ? 469  ASP B CG  1 
ATOM   3644  O OD1 . ASP A 1 486  ? 185.986 216.776 278.994 1.00 82.68  ? 469  ASP B OD1 1 
ATOM   3645  O OD2 . ASP A 1 486  ? 184.982 216.068 280.812 1.00 82.68  ? 469  ASP B OD2 1 
ATOM   3646  N N   . ASN A 1 487  ? 187.433 212.942 277.613 1.00 81.06  ? 470  ASN B N   1 
ATOM   3647  C CA  . ASN A 1 487  ? 188.828 212.566 277.806 1.00 81.06  ? 470  ASN B CA  1 
ATOM   3648  C C   . ASN A 1 487  ? 189.729 212.973 276.647 1.00 81.06  ? 470  ASN B C   1 
ATOM   3649  O O   . ASN A 1 487  ? 190.953 212.964 276.811 1.00 81.06  ? 470  ASN B O   1 
ATOM   3650  C CB  . ASN A 1 487  ? 188.943 211.058 278.025 1.00 81.06  ? 470  ASN B CB  1 
ATOM   3651  C CG  . ASN A 1 487  ? 187.840 210.512 278.900 1.00 81.06  ? 470  ASN B CG  1 
ATOM   3652  O OD1 . ASN A 1 487  ? 186.850 209.975 278.406 1.00 81.06  ? 470  ASN B OD1 1 
ATOM   3653  N ND2 . ASN A 1 487  ? 188.005 210.643 280.208 1.00 81.06  ? 470  ASN B ND2 1 
ATOM   3654  N N   . PHE A 1 488  ? 189.170 213.320 275.493 1.00 78.43  ? 471  PHE B N   1 
ATOM   3655  C CA  . PHE A 1 488  ? 189.954 213.699 274.324 1.00 78.43  ? 471  PHE B CA  1 
ATOM   3656  C C   . PHE A 1 488  ? 189.791 215.193 274.083 1.00 78.43  ? 471  PHE B C   1 
ATOM   3657  O O   . PHE A 1 488  ? 188.666 215.681 273.932 1.00 78.43  ? 471  PHE B O   1 
ATOM   3658  C CB  . PHE A 1 488  ? 189.523 212.901 273.095 1.00 78.43  ? 471  PHE B CB  1 
ATOM   3659  C CG  . PHE A 1 488  ? 189.293 211.443 273.370 1.00 78.43  ? 471  PHE B CG  1 
ATOM   3660  C CD1 . PHE A 1 488  ? 190.358 210.589 273.590 1.00 78.43  ? 471  PHE B CD1 1 
ATOM   3661  C CD2 . PHE A 1 488  ? 188.011 210.925 273.405 1.00 78.43  ? 471  PHE B CD2 1 
ATOM   3662  C CE1 . PHE A 1 488  ? 190.147 209.248 273.842 1.00 78.43  ? 471  PHE B CE1 1 
ATOM   3663  C CE2 . PHE A 1 488  ? 187.797 209.585 273.656 1.00 78.43  ? 471  PHE B CE2 1 
ATOM   3664  C CZ  . PHE A 1 488  ? 188.866 208.748 273.875 1.00 78.43  ? 471  PHE B CZ  1 
ATOM   3665  N N   . THR A 1 489  ? 190.910 215.912 274.046 1.00 81.10  ? 472  THR B N   1 
ATOM   3666  C CA  . THR A 1 489  ? 190.911 217.351 273.830 1.00 81.10  ? 472  THR B CA  1 
ATOM   3667  C C   . THR A 1 489  ? 191.941 217.706 272.769 1.00 81.10  ? 472  THR B C   1 
ATOM   3668  O O   . THR A 1 489  ? 192.918 216.982 272.563 1.00 81.10  ? 472  THR B O   1 
ATOM   3669  C CB  . THR A 1 489  ? 191.216 218.118 275.120 1.00 81.10  ? 472  THR B CB  1 
ATOM   3670  O OG1 . THR A 1 489  ? 192.393 217.577 275.730 1.00 81.10  ? 472  THR B OG1 1 
ATOM   3671  C CG2 . THR A 1 489  ? 190.053 218.014 276.091 1.00 81.10  ? 472  THR B CG2 1 
ATOM   3672  N N   . ASN A 1 490  ? 191.713 218.830 272.095 1.00 81.03  ? 473  ASN B N   1 
ATOM   3673  C CA  . ASN A 1 490  ? 192.569 219.267 271.004 1.00 81.03  ? 473  ASN B CA  1 
ATOM   3674  C C   . ASN A 1 490  ? 192.918 220.739 271.144 1.00 81.03  ? 473  ASN B C   1 
ATOM   3675  O O   . ASN A 1 490  ? 192.079 221.555 271.535 1.00 81.03  ? 473  ASN B O   1 
ATOM   3676  C CB  . ASN A 1 490  ? 191.905 219.038 269.648 1.00 81.03  ? 473  ASN B CB  1 
ATOM   3677  C CG  . ASN A 1 490  ? 191.372 217.638 269.494 1.00 81.03  ? 473  ASN B CG  1 
ATOM   3678  O OD1 . ASN A 1 490  ? 190.372 217.267 270.105 1.00 81.03  ? 473  ASN B OD1 1 
ATOM   3679  N ND2 . ASN A 1 490  ? 192.047 216.844 268.677 1.00 81.03  ? 473  ASN B ND2 1 
ATOM   3680  N N   . ASP A 1 491  ? 194.167 221.065 270.815 1.00 84.58  ? 474  ASP B N   1 
ATOM   3681  C CA  . ASP A 1 491  ? 194.609 222.437 270.624 1.00 84.58  ? 474  ASP B CA  1 
ATOM   3682  C C   . ASP A 1 491  ? 194.744 222.784 269.147 1.00 84.58  ? 474  ASP B C   1 
ATOM   3683  O O   . ASP A 1 491  ? 195.429 223.752 268.801 1.00 84.58  ? 474  ASP B O   1 
ATOM   3684  C CB  . ASP A 1 491  ? 195.933 222.674 271.349 1.00 84.58  ? 474  ASP B CB  1 
ATOM   3685  C CG  . ASP A 1 491  ? 197.001 221.668 270.960 1.00 84.58  ? 474  ASP B CG  1 
ATOM   3686  O OD1 . ASP A 1 491  ? 196.732 220.810 270.094 1.00 84.58  ? 474  ASP B OD1 1 
ATOM   3687  O OD2 . ASP A 1 491  ? 198.115 221.737 271.521 1.00 84.58  ? 474  ASP B OD2 1 
ATOM   3688  N N   . LEU A 1 492  ? 194.108 222.000 268.273 1.00 79.23  ? 475  LEU B N   1 
ATOM   3689  C CA  . LEU A 1 492  ? 194.254 222.195 266.835 1.00 79.23  ? 475  LEU B CA  1 
ATOM   3690  C C   . LEU A 1 492  ? 193.717 223.550 266.398 1.00 79.23  ? 475  LEU B C   1 
ATOM   3691  O O   . LEU A 1 492  ? 194.305 224.207 265.532 1.00 79.23  ? 475  LEU B O   1 
ATOM   3692  C CB  . LEU A 1 492  ? 193.538 221.074 266.085 1.00 79.23  ? 475  LEU B CB  1 
ATOM   3693  C CG  . LEU A 1 492  ? 193.917 219.641 266.451 1.00 79.23  ? 475  LEU B CG  1 
ATOM   3694  C CD1 . LEU A 1 492  ? 192.857 218.674 265.968 1.00 79.23  ? 475  LEU B CD1 1 
ATOM   3695  C CD2 . LEU A 1 492  ? 195.256 219.289 265.852 1.00 79.23  ? 475  LEU B CD2 1 
ATOM   3696  N N   . ASN A 1 493  ? 192.597 223.981 266.980 1.00 83.28  ? 476  ASN B N   1 
ATOM   3697  C CA  . ASN A 1 493  ? 191.954 225.209 266.525 1.00 83.28  ? 476  ASN B CA  1 
ATOM   3698  C C   . ASN A 1 493  ? 192.837 226.427 266.765 1.00 83.28  ? 476  ASN B C   1 
ATOM   3699  O O   . ASN A 1 493  ? 192.839 227.367 265.963 1.00 83.28  ? 476  ASN B O   1 
ATOM   3700  C CB  . ASN A 1 493  ? 190.604 225.381 267.219 1.00 83.28  ? 476  ASN B CB  1 
ATOM   3701  C CG  . ASN A 1 493  ? 190.004 226.752 266.988 1.00 83.28  ? 476  ASN B CG  1 
ATOM   3702  O OD1 . ASN A 1 493  ? 189.796 227.166 265.848 1.00 83.28  ? 476  ASN B OD1 1 
ATOM   3703  N ND2 . ASN A 1 493  ? 189.725 227.467 268.071 1.00 83.28  ? 476  ASN B ND2 1 
ATOM   3704  N N   . LYS A 1 494  ? 193.593 226.431 267.861 1.00 85.21  ? 477  LYS B N   1 
ATOM   3705  C CA  . LYS A 1 494  ? 194.415 227.587 268.192 1.00 85.21  ? 477  LYS B CA  1 
ATOM   3706  C C   . LYS A 1 494  ? 195.500 227.800 267.143 1.00 85.21  ? 477  LYS B C   1 
ATOM   3707  O O   . LYS A 1 494  ? 196.147 226.853 266.690 1.00 85.21  ? 477  LYS B O   1 
ATOM   3708  C CB  . LYS A 1 494  ? 195.042 227.414 269.575 1.00 85.21  ? 477  LYS B CB  1 
ATOM   3709  C CG  . LYS A 1 494  ? 194.054 226.999 270.654 1.00 85.21  ? 477  LYS B CG  1 
ATOM   3710  C CD  . LYS A 1 494  ? 194.687 226.047 271.655 1.00 85.21  ? 477  LYS B CD  1 
ATOM   3711  C CE  . LYS A 1 494  ? 195.693 226.762 272.544 1.00 85.21  ? 477  LYS B CE  1 
ATOM   3712  N NZ  . LYS A 1 494  ? 196.189 225.882 273.638 1.00 85.21  ? 477  LYS B NZ  1 
ATOM   3713  N N   . GLY A 1 495  ? 195.697 229.061 266.763 1.00 87.20  ? 478  GLY B N   1 
ATOM   3714  C CA  . GLY A 1 495  ? 196.644 229.410 265.729 1.00 87.20  ? 478  GLY B CA  1 
ATOM   3715  C C   . GLY A 1 495  ? 198.081 229.382 266.209 1.00 87.20  ? 478  GLY B C   1 
ATOM   3716  O O   . GLY A 1 495  ? 198.382 229.171 267.384 1.00 87.20  ? 478  GLY B O   1 
ATOM   3717  N N   . GLU A 1 496  ? 198.991 229.604 265.263 1.00 83.78  ? 479  GLU B N   1 
ATOM   3718  C CA  . GLU A 1 496  ? 200.419 229.541 265.529 1.00 83.78  ? 479  GLU B CA  1 
ATOM   3719  C C   . GLU A 1 496  ? 201.141 230.601 264.712 1.00 83.78  ? 479  GLU B C   1 
ATOM   3720  O O   . GLU A 1 496  ? 200.811 230.826 263.544 1.00 83.78  ? 479  GLU B O   1 
ATOM   3721  C CB  . GLU A 1 496  ? 200.974 228.151 265.201 1.00 83.78  ? 479  GLU B CB  1 
ATOM   3722  C CG  . GLU A 1 496  ? 202.481 228.045 265.257 1.00 83.78  ? 479  GLU B CG  1 
ATOM   3723  C CD  . GLU A 1 496  ? 202.941 226.754 265.897 1.00 83.78  ? 479  GLU B CD  1 
ATOM   3724  O OE1 . GLU A 1 496  ? 202.510 225.676 265.436 1.00 83.78  ? 479  GLU B OE1 1 
ATOM   3725  O OE2 . GLU A 1 496  ? 203.734 226.814 266.860 1.00 83.78  ? 479  GLU B OE2 1 
ATOM   3726  N N   . GLU A 1 497  ? 202.124 231.248 265.331 1.00 85.15  ? 480  GLU B N   1 
ATOM   3727  C CA  . GLU A 1 497  ? 202.946 232.253 264.676 1.00 85.15  ? 480  GLU B CA  1 
ATOM   3728  C C   . GLU A 1 497  ? 204.358 231.718 264.490 1.00 85.15  ? 480  GLU B C   1 
ATOM   3729  O O   . GLU A 1 497  ? 204.924 231.104 265.400 1.00 85.15  ? 480  GLU B O   1 
ATOM   3730  C CB  . GLU A 1 497  ? 202.985 233.552 265.483 1.00 85.15  ? 480  GLU B CB  1 
ATOM   3731  C CG  . GLU A 1 497  ? 203.564 234.730 264.718 1.00 85.15  ? 480  GLU B CG  1 
ATOM   3732  C CD  . GLU A 1 497  ? 204.421 235.628 265.585 1.00 85.15  ? 480  GLU B CD  1 
ATOM   3733  O OE1 . GLU A 1 497  ? 204.569 235.328 266.788 1.00 85.15  ? 480  GLU B OE1 1 
ATOM   3734  O OE2 . GLU A 1 497  ? 204.947 236.633 265.065 1.00 85.15  ? 480  GLU B OE2 1 
ATOM   3735  N N   . ILE A 1 498  ? 204.924 231.956 263.311 1.00 79.53  ? 481  ILE B N   1 
ATOM   3736  C CA  . ILE A 1 498  ? 206.237 231.442 262.943 1.00 79.53  ? 481  ILE B CA  1 
ATOM   3737  C C   . ILE A 1 498  ? 207.223 232.597 262.854 1.00 79.53  ? 481  ILE B C   1 
ATOM   3738  O O   . ILE A 1 498  ? 206.926 233.639 262.261 1.00 79.53  ? 481  ILE B O   1 
ATOM   3739  C CB  . ILE A 1 498  ? 206.187 230.666 261.615 1.00 79.53  ? 481  ILE B CB  1 
ATOM   3740  C CG1 . ILE A 1 498  ? 205.638 229.265 261.849 1.00 79.53  ? 481  ILE B CG1 1 
ATOM   3741  C CG2 . ILE A 1 498  ? 207.561 230.590 260.982 1.00 79.53  ? 481  ILE B CG2 1 
ATOM   3742  C CD1 . ILE A 1 498  ? 205.837 228.361 260.682 1.00 79.53  ? 481  ILE B CD1 1 
ATOM   3743  N N   . THR A 1 499  ? 208.399 232.401 263.439 1.00 86.71  ? 482  THR B N   1 
ATOM   3744  C CA  . THR A 1 499  ? 209.487 233.366 263.438 1.00 86.71  ? 482  THR B CA  1 
ATOM   3745  C C   . THR A 1 499  ? 210.738 232.699 262.866 1.00 86.71  ? 482  THR B C   1 
ATOM   3746  O O   . THR A 1 499  ? 210.677 231.609 262.294 1.00 86.71  ? 482  THR B O   1 
ATOM   3747  C CB  . THR A 1 499  ? 209.730 233.919 264.844 1.00 86.71  ? 482  THR B CB  1 
ATOM   3748  O OG1 . THR A 1 499  ? 209.944 232.838 265.758 1.00 86.71  ? 482  THR B OG1 1 
ATOM   3749  C CG2 . THR A 1 499  ? 208.537 234.738 265.311 1.00 86.71  ? 482  THR B CG2 1 
ATOM   3750  N N   . SER A 1 500  ? 211.878 233.377 263.019 1.00 86.09  ? 483  SER B N   1 
ATOM   3751  C CA  . SER A 1 500  ? 213.113 232.916 262.392 1.00 86.09  ? 483  SER B CA  1 
ATOM   3752  C C   . SER A 1 500  ? 213.496 231.515 262.853 1.00 86.09  ? 483  SER B C   1 
ATOM   3753  O O   . SER A 1 500  ? 213.919 230.684 262.041 1.00 86.09  ? 483  SER B O   1 
ATOM   3754  C CB  . SER A 1 500  ? 214.245 233.898 262.688 1.00 86.09  ? 483  SER B CB  1 
ATOM   3755  O OG  . SER A 1 500  ? 214.366 234.860 261.657 1.00 86.09  ? 483  SER B OG  1 
ATOM   3756  N N   . ASP A 1 501  ? 213.363 231.231 264.148 1.00 93.82  ? 484  ASP B N   1 
ATOM   3757  C CA  . ASP A 1 501  ? 213.779 229.948 264.717 1.00 93.82  ? 484  ASP B CA  1 
ATOM   3758  C C   . ASP A 1 501  ? 212.662 229.407 265.605 1.00 93.82  ? 484  ASP B C   1 
ATOM   3759  O O   . ASP A 1 501  ? 212.563 229.762 266.782 1.00 93.82  ? 484  ASP B O   1 
ATOM   3760  C CB  . ASP A 1 501  ? 215.086 230.098 265.487 1.00 93.82  ? 484  ASP B CB  1 
ATOM   3761  C CG  . ASP A 1 501  ? 215.178 231.418 266.227 1.00 93.82  ? 484  ASP B CG  1 
ATOM   3762  O OD1 . ASP A 1 501  ? 214.133 232.077 266.407 1.00 93.82  ? 484  ASP B OD1 1 
ATOM   3763  O OD2 . ASP A 1 501  ? 216.299 231.797 266.627 1.00 93.82  ? 484  ASP B OD2 1 
ATOM   3764  N N   . THR A 1 502  ? 211.820 228.546 265.036 1.00 97.35  ? 485  THR B N   1 
ATOM   3765  C CA  . THR A 1 502  ? 210.781 227.837 265.778 1.00 97.35  ? 485  THR B CA  1 
ATOM   3766  C C   . THR A 1 502  ? 210.954 226.347 265.523 1.00 97.35  ? 485  THR B C   1 
ATOM   3767  O O   . THR A 1 502  ? 210.736 225.878 264.401 1.00 97.35  ? 485  THR B O   1 
ATOM   3768  C CB  . THR A 1 502  ? 209.381 228.288 265.364 1.00 97.35  ? 485  THR B CB  1 
ATOM   3769  O OG1 . THR A 1 502  ? 209.014 227.639 264.140 1.00 97.35  ? 485  THR B OG1 1 
ATOM   3770  C CG2 . THR A 1 502  ? 209.334 229.788 265.169 1.00 97.35  ? 485  THR B CG2 1 
ATOM   3771  N N   . ASN A 1 503  ? 211.340 225.606 266.556 1.00 104.99 ? 486  ASN B N   1 
ATOM   3772  C CA  . ASN A 1 503  ? 211.498 224.162 266.441 1.00 104.99 ? 486  ASN B CA  1 
ATOM   3773  C C   . ASN A 1 503  ? 210.831 223.477 267.624 1.00 104.99 ? 486  ASN B C   1 
ATOM   3774  O O   . ASN A 1 503  ? 209.754 223.884 268.060 1.00 104.99 ? 486  ASN B O   1 
ATOM   3775  C CB  . ASN A 1 503  ? 212.974 223.774 266.349 1.00 30.00  ? 486  ASN B CB  1 
ATOM   3776  C CG  . ASN A 1 503  ? 213.592 224.140 265.014 1.00 30.00  ? 486  ASN B CG  1 
ATOM   3777  O OD1 . ASN A 1 503  ? 212.892 224.289 264.013 1.00 30.00  ? 486  ASN B OD1 1 
ATOM   3778  N ND2 . ASN A 1 503  ? 214.912 224.287 264.993 1.00 30.00  ? 486  ASN B ND2 1 
ATOM   3779  N N   . SER A 1 512  ? 211.186 200.326 271.800 1.00 105.87 ? 495  SER B N   1 
ATOM   3780  C CA  . SER A 1 512  ? 212.244 199.617 271.090 1.00 105.87 ? 495  SER B CA  1 
ATOM   3781  C C   . SER A 1 512  ? 213.376 199.244 272.041 1.00 105.87 ? 495  SER B C   1 
ATOM   3782  O O   . SER A 1 512  ? 213.831 200.070 272.830 1.00 105.87 ? 495  SER B O   1 
ATOM   3783  C CB  . SER A 1 512  ? 212.778 200.466 269.938 1.00 105.87 ? 495  SER B CB  1 
ATOM   3784  O OG  . SER A 1 512  ? 213.728 201.408 270.402 1.00 105.87 ? 495  SER B OG  1 
ATOM   3785  N N   . LEU A 1 513  ? 213.832 197.992 271.954 1.00 104.32 ? 496  LEU B N   1 
ATOM   3786  C CA  . LEU A 1 513  ? 214.831 197.500 272.897 1.00 104.32 ? 496  LEU B CA  1 
ATOM   3787  C C   . LEU A 1 513  ? 216.177 198.191 272.719 1.00 104.32 ? 496  LEU B C   1 
ATOM   3788  O O   . LEU A 1 513  ? 216.937 198.315 273.687 1.00 104.32 ? 496  LEU B O   1 
ATOM   3789  C CB  . LEU A 1 513  ? 214.989 195.986 272.753 1.00 104.32 ? 496  LEU B CB  1 
ATOM   3790  C CG  . LEU A 1 513  ? 213.786 195.112 273.124 1.00 104.32 ? 496  LEU B CG  1 
ATOM   3791  C CD1 . LEU A 1 513  ? 214.243 193.726 273.546 1.00 104.32 ? 496  LEU B CD1 1 
ATOM   3792  C CD2 . LEU A 1 513  ? 212.950 195.754 274.219 1.00 104.32 ? 496  LEU B CD2 1 
ATOM   3793  N N   . ASP A 1 514  ? 216.497 198.637 271.502 1.00 106.48 ? 497  ASP B N   1 
ATOM   3794  C CA  . ASP A 1 514  ? 217.766 199.325 271.285 1.00 106.48 ? 497  ASP B CA  1 
ATOM   3795  C C   . ASP A 1 514  ? 217.815 200.644 272.045 1.00 106.48 ? 497  ASP B C   1 
ATOM   3796  O O   . ASP A 1 514  ? 218.866 201.032 272.568 1.00 106.48 ? 497  ASP B O   1 
ATOM   3797  C CB  . ASP A 1 514  ? 217.997 199.552 269.790 1.00 106.48 ? 497  ASP B CB  1 
ATOM   3798  C CG  . ASP A 1 514  ? 216.920 200.410 269.153 1.00 106.48 ? 497  ASP B CG  1 
ATOM   3799  O OD1 . ASP A 1 514  ? 215.905 200.693 269.822 1.00 106.48 ? 497  ASP B OD1 1 
ATOM   3800  O OD2 . ASP A 1 514  ? 217.090 200.806 267.981 1.00 106.48 ? 497  ASP B OD2 1 
ATOM   3801  N N   . LEU A 1 515  ? 216.687 201.353 272.109 1.00 100.73 ? 498  LEU B N   1 
ATOM   3802  C CA  . LEU A 1 515  ? 216.631 202.600 272.862 1.00 100.73 ? 498  LEU B CA  1 
ATOM   3803  C C   . LEU A 1 515  ? 216.837 202.342 274.352 1.00 100.73 ? 498  LEU B C   1 
ATOM   3804  O O   . LEU A 1 515  ? 217.556 203.091 275.028 1.00 100.73 ? 498  LEU B O   1 
ATOM   3805  C CB  . LEU A 1 515  ? 215.294 203.292 272.584 1.00 100.73 ? 498  LEU B CB  1 
ATOM   3806  C CG  . LEU A 1 515  ? 215.067 204.798 272.748 1.00 100.73 ? 498  LEU B CG  1 
ATOM   3807  C CD1 . LEU A 1 515  ? 213.625 205.135 272.404 1.00 100.73 ? 498  LEU B CD1 1 
ATOM   3808  C CD2 . LEU A 1 515  ? 215.388 205.293 274.134 1.00 100.73 ? 498  LEU B CD2 1 
ATOM   3809  N N   . ILE A 1 516  ? 216.231 201.272 274.874 1.00 98.62  ? 499  ILE B N   1 
ATOM   3810  C CA  . ILE A 1 516  ? 216.438 200.900 276.271 1.00 98.62  ? 499  ILE B CA  1 
ATOM   3811  C C   . ILE A 1 516  ? 217.901 200.563 276.516 1.00 98.62  ? 499  ILE B C   1 
ATOM   3812  O O   . ILE A 1 516  ? 218.475 200.926 277.549 1.00 98.62  ? 499  ILE B O   1 
ATOM   3813  C CB  . ILE A 1 516  ? 215.521 199.726 276.659 1.00 98.62  ? 499  ILE B CB  1 
ATOM   3814  C CG1 . ILE A 1 516  ? 214.139 199.881 276.026 1.00 98.62  ? 499  ILE B CG1 1 
ATOM   3815  C CG2 . ILE A 1 516  ? 215.403 199.623 278.168 1.00 98.62  ? 499  ILE B CG2 1 
ATOM   3816  C CD1 . ILE A 1 516  ? 213.370 201.066 276.529 1.00 98.62  ? 499  ILE B CD1 1 
ATOM   3817  N N   . GLN A 1 517  ? 218.525 199.852 275.576 1.00 101.19 ? 500  GLN B N   1 
ATOM   3818  C CA  . GLN A 1 517  ? 219.939 199.521 275.709 1.00 101.19 ? 500  GLN B CA  1 
ATOM   3819  C C   . GLN A 1 517  ? 220.800 200.779 275.720 1.00 101.19 ? 500  GLN B C   1 
ATOM   3820  O O   . GLN A 1 517  ? 221.747 200.890 276.511 1.00 101.19 ? 500  GLN B O   1 
ATOM   3821  C CB  . GLN A 1 517  ? 220.347 198.579 274.575 1.00 101.19 ? 500  GLN B CB  1 
ATOM   3822  C CG  . GLN A 1 517  ? 221.746 198.000 274.671 1.00 101.19 ? 500  GLN B CG  1 
ATOM   3823  C CD  . GLN A 1 517  ? 222.691 198.590 273.644 1.00 101.19 ? 500  GLN B CD  1 
ATOM   3824  O OE1 . GLN A 1 517  ? 222.298 199.424 272.829 1.00 101.19 ? 500  GLN B OE1 1 
ATOM   3825  N NE2 . GLN A 1 517  ? 223.938 198.136 273.660 1.00 101.19 ? 500  GLN B NE2 1 
ATOM   3826  N N   . GLN A 1 518  ? 220.484 201.739 274.851 1.00 98.34  ? 501  GLN B N   1 
ATOM   3827  C CA  . GLN A 1 518  ? 221.244 202.983 274.823 1.00 98.34  ? 501  GLN B CA  1 
ATOM   3828  C C   . GLN A 1 518  ? 221.102 203.716 276.148 1.00 98.34  ? 501  GLN B C   1 
ATOM   3829  O O   . GLN A 1 518  ? 222.077 204.274 276.668 1.00 98.34  ? 501  GLN B O   1 
ATOM   3830  C CB  . GLN A 1 518  ? 220.798 203.822 273.614 1.00 98.34  ? 501  GLN B CB  1 
ATOM   3831  C CG  . GLN A 1 518  ? 221.188 205.325 273.493 1.00 98.34  ? 501  GLN B CG  1 
ATOM   3832  C CD  . GLN A 1 518  ? 220.773 206.232 274.643 1.00 98.34  ? 501  GLN B CD  1 
ATOM   3833  O OE1 . GLN A 1 518  ? 219.760 206.004 275.302 1.00 98.34  ? 501  GLN B OE1 1 
ATOM   3834  N NE2 . GLN A 1 518  ? 221.561 207.274 274.881 1.00 98.34  ? 501  GLN B NE2 1 
ATOM   3835  N N   . TYR A 1 519  ? 219.893 203.719 276.713 1.00 92.28  ? 502  TYR B N   1 
ATOM   3836  C CA  . TYR A 1 519  ? 219.707 204.289 278.044 1.00 92.28  ? 502  TYR B CA  1 
ATOM   3837  C C   . TYR A 1 519  ? 220.536 203.545 279.080 1.00 92.28  ? 502  TYR B C   1 
ATOM   3838  O O   . TYR A 1 519  ? 221.074 204.156 280.010 1.00 92.28  ? 502  TYR B O   1 
ATOM   3839  C CB  . TYR A 1 519  ? 218.231 204.267 278.431 1.00 92.28  ? 502  TYR B CB  1 
ATOM   3840  C CG  . TYR A 1 519  ? 217.540 205.598 278.274 1.00 92.28  ? 502  TYR B CG  1 
ATOM   3841  C CD1 . TYR A 1 519  ? 217.574 206.549 279.285 1.00 92.28  ? 502  TYR B CD1 1 
ATOM   3842  C CD2 . TYR A 1 519  ? 216.859 205.906 277.112 1.00 92.28  ? 502  TYR B CD2 1 
ATOM   3843  C CE1 . TYR A 1 519  ? 216.940 207.768 279.138 1.00 92.28  ? 502  TYR B CE1 1 
ATOM   3844  C CE2 . TYR A 1 519  ? 216.226 207.118 276.956 1.00 92.28  ? 502  TYR B CE2 1 
ATOM   3845  C CZ  . TYR A 1 519  ? 216.268 208.045 277.968 1.00 92.28  ? 502  TYR B CZ  1 
ATOM   3846  O OH  . TYR A 1 519  ? 215.633 209.252 277.805 1.00 92.28  ? 502  TYR B OH  1 
ATOM   3847  N N   . TYR A 1 520  ? 220.637 202.220 278.944 1.00 90.92  ? 503  TYR B N   1 
ATOM   3848  C CA  . TYR A 1 520  ? 221.408 201.432 279.901 1.00 90.92  ? 503  TYR B CA  1 
ATOM   3849  C C   . TYR A 1 520  ? 222.881 201.816 279.877 1.00 90.92  ? 503  TYR B C   1 
ATOM   3850  O O   . TYR A 1 520  ? 223.506 201.961 280.935 1.00 90.92  ? 503  TYR B O   1 
ATOM   3851  C CB  . TYR A 1 520  ? 221.239 199.939 279.620 1.00 90.92  ? 503  TYR B CB  1 
ATOM   3852  C CG  . TYR A 1 520  ? 222.046 199.052 280.542 1.00 90.92  ? 503  TYR B CG  1 
ATOM   3853  C CD1 . TYR A 1 520  ? 221.865 199.097 281.916 1.00 90.92  ? 503  TYR B CD1 1 
ATOM   3854  C CD2 . TYR A 1 520  ? 222.988 198.169 280.036 1.00 90.92  ? 503  TYR B CD2 1 
ATOM   3855  C CE1 . TYR A 1 520  ? 222.601 198.291 282.759 1.00 90.92  ? 503  TYR B CE1 1 
ATOM   3856  C CE2 . TYR A 1 520  ? 223.729 197.358 280.871 1.00 90.92  ? 503  TYR B CE2 1 
ATOM   3857  C CZ  . TYR A 1 520  ? 223.532 197.423 282.231 1.00 90.92  ? 503  TYR B CZ  1 
ATOM   3858  O OH  . TYR A 1 520  ? 224.270 196.613 283.062 1.00 90.92  ? 503  TYR B OH  1 
ATOM   3859  N N   . LEU A 1 521  ? 223.461 201.975 278.684 1.00 95.32  ? 504  LEU B N   1 
ATOM   3860  C CA  . LEU A 1 521  ? 224.836 202.479 278.627 1.00 95.32  ? 504  LEU B CA  1 
ATOM   3861  C C   . LEU A 1 521  ? 224.931 203.900 279.171 1.00 95.32  ? 504  LEU B C   1 
ATOM   3862  O O   . LEU A 1 521  ? 225.887 204.237 279.878 1.00 95.32  ? 504  LEU B O   1 
ATOM   3863  C CB  . LEU A 1 521  ? 225.421 202.423 277.212 1.00 95.32  ? 504  LEU B CB  1 
ATOM   3864  C CG  . LEU A 1 521  ? 225.735 201.117 276.473 1.00 95.32  ? 504  LEU B CG  1 
ATOM   3865  C CD1 . LEU A 1 521  ? 226.355 200.094 277.422 1.00 95.32  ? 504  LEU B CD1 1 
ATOM   3866  C CD2 . LEU A 1 521  ? 224.566 200.543 275.720 1.00 95.32  ? 504  LEU B CD2 1 
ATOM   3867  N N   . THR A 1 522  ? 223.955 204.750 278.852 1.00 96.69  ? 505  THR B N   1 
ATOM   3868  C CA  . THR A 1 522  ? 224.023 206.136 279.300 1.00 96.69  ? 505  THR B CA  1 
ATOM   3869  C C   . THR A 1 522  ? 223.776 206.276 280.800 1.00 96.69  ? 505  THR B C   1 
ATOM   3870  O O   . THR A 1 522  ? 224.191 207.277 281.392 1.00 96.69  ? 505  THR B O   1 
ATOM   3871  C CB  . THR A 1 522  ? 223.020 206.985 278.514 1.00 96.69  ? 505  THR B CB  1 
ATOM   3872  O OG1 . THR A 1 522  ? 223.159 206.707 277.115 1.00 96.69  ? 505  THR B OG1 1 
ATOM   3873  C CG2 . THR A 1 522  ? 223.269 208.471 278.740 1.00 96.69  ? 505  THR B CG2 1 
ATOM   3874  N N   . PHE A 1 523  ? 223.142 205.289 281.429 1.00 89.28  ? 506  PHE B N   1 
ATOM   3875  C CA  . PHE A 1 523  ? 222.771 205.411 282.833 1.00 89.28  ? 506  PHE B CA  1 
ATOM   3876  C C   . PHE A 1 523  ? 224.004 205.483 283.729 1.00 89.28  ? 506  PHE B C   1 
ATOM   3877  O O   . PHE A 1 523  ? 225.081 204.986 283.390 1.00 89.28  ? 506  PHE B O   1 
ATOM   3878  C CB  . PHE A 1 523  ? 221.891 204.236 283.259 1.00 89.28  ? 506  PHE B CB  1 
ATOM   3879  C CG  . PHE A 1 523  ? 221.003 204.544 284.426 1.00 89.28  ? 506  PHE B CG  1 
ATOM   3880  C CD1 . PHE A 1 523  ? 219.830 205.254 284.253 1.00 89.28  ? 506  PHE B CD1 1 
ATOM   3881  C CD2 . PHE A 1 523  ? 221.346 204.131 285.700 1.00 89.28  ? 506  PHE B CD2 1 
ATOM   3882  C CE1 . PHE A 1 523  ? 219.015 205.542 285.327 1.00 89.28  ? 506  PHE B CE1 1 
ATOM   3883  C CE2 . PHE A 1 523  ? 220.534 204.418 286.776 1.00 89.28  ? 506  PHE B CE2 1 
ATOM   3884  C CZ  . PHE A 1 523  ? 219.368 205.123 286.589 1.00 89.28  ? 506  PHE B CZ  1 
ATOM   3885  N N   . ASN A 1 524  ? 223.831 206.114 284.887 1.00 95.10  ? 507  ASN B N   1 
ATOM   3886  C CA  . ASN A 1 524  ? 224.901 206.309 285.855 1.00 95.10  ? 507  ASN B CA  1 
ATOM   3887  C C   . ASN A 1 524  ? 224.714 205.365 287.035 1.00 95.10  ? 507  ASN B C   1 
ATOM   3888  O O   . ASN A 1 524  ? 223.619 205.277 287.599 1.00 95.10  ? 507  ASN B O   1 
ATOM   3889  C CB  . ASN A 1 524  ? 224.933 207.758 286.341 1.00 95.10  ? 507  ASN B CB  1 
ATOM   3890  C CG  . ASN A 1 524  ? 225.681 207.916 287.649 1.00 95.10  ? 507  ASN B CG  1 
ATOM   3891  O OD1 . ASN A 1 524  ? 225.091 208.244 288.679 1.00 95.10  ? 507  ASN B OD1 1 
ATOM   3892  N ND2 . ASN A 1 524  ? 226.987 207.684 287.616 1.00 95.10  ? 507  ASN B ND2 1 
ATOM   3893  N N   . PHE A 1 525  ? 225.782 204.670 287.405 1.00 95.25  ? 508  PHE B N   1 
ATOM   3894  C CA  . PHE A 1 525  ? 225.799 203.736 288.523 1.00 95.25  ? 508  PHE B CA  1 
ATOM   3895  C C   . PHE A 1 525  ? 226.852 204.175 289.538 1.00 95.25  ? 508  PHE B C   1 
ATOM   3896  O O   . PHE A 1 525  ? 227.394 205.281 289.468 1.00 95.25  ? 508  PHE B O   1 
ATOM   3897  C CB  . PHE A 1 525  ? 226.080 202.306 288.046 1.00 95.25  ? 508  PHE B CB  1 
ATOM   3898  C CG  . PHE A 1 525  ? 225.006 201.728 287.167 1.00 95.25  ? 508  PHE B CG  1 
ATOM   3899  C CD1 . PHE A 1 525  ? 224.910 202.089 285.834 1.00 95.25  ? 508  PHE B CD1 1 
ATOM   3900  C CD2 . PHE A 1 525  ? 224.104 200.810 287.670 1.00 95.25  ? 508  PHE B CD2 1 
ATOM   3901  C CE1 . PHE A 1 525  ? 223.927 201.553 285.026 1.00 95.25  ? 508  PHE B CE1 1 
ATOM   3902  C CE2 . PHE A 1 525  ? 223.120 200.272 286.865 1.00 95.25  ? 508  PHE B CE2 1 
ATOM   3903  C CZ  . PHE A 1 525  ? 223.032 200.643 285.543 1.00 95.25  ? 508  PHE B CZ  1 
ATOM   3904  N N   . ASP A 1 526  ? 227.104 203.297 290.512 1.00 105.27 ? 509  ASP B N   1 
ATOM   3905  C CA  . ASP A 1 526  ? 228.203 203.426 291.465 1.00 105.27 ? 509  ASP B CA  1 
ATOM   3906  C C   . ASP A 1 526  ? 228.017 204.586 292.437 1.00 105.27 ? 509  ASP B C   1 
ATOM   3907  O O   . ASP A 1 526  ? 228.858 204.799 293.316 1.00 105.27 ? 509  ASP B O   1 
ATOM   3908  C CB  . ASP A 1 526  ? 229.539 203.573 290.730 1.00 105.27 ? 509  ASP B CB  1 
ATOM   3909  C CG  . ASP A 1 526  ? 229.838 202.397 289.824 1.00 105.27 ? 509  ASP B CG  1 
ATOM   3910  O OD1 . ASP A 1 526  ? 229.259 202.329 288.719 1.00 105.27 ? 509  ASP B OD1 1 
ATOM   3911  O OD2 . ASP A 1 526  ? 230.657 201.540 290.215 1.00 105.27 ? 509  ASP B OD2 1 
ATOM   3912  N N   . ASN A 1 527  ? 226.929 205.336 292.301 1.00 98.55  ? 510  ASN B N   1 
ATOM   3913  C CA  . ASN A 1 527  ? 226.627 206.452 293.193 1.00 98.55  ? 510  ASN B CA  1 
ATOM   3914  C C   . ASN A 1 527  ? 225.252 206.210 293.805 1.00 98.55  ? 510  ASN B C   1 
ATOM   3915  O O   . ASN A 1 527  ? 224.227 206.524 293.192 1.00 98.55  ? 510  ASN B O   1 
ATOM   3916  C CB  . ASN A 1 527  ? 226.679 207.785 292.454 1.00 98.55  ? 510  ASN B CB  1 
ATOM   3917  C CG  . ASN A 1 527  ? 227.297 208.888 293.289 1.00 98.55  ? 510  ASN B CG  1 
ATOM   3918  O OD1 . ASN A 1 527  ? 227.253 208.848 294.518 1.00 98.55  ? 510  ASN B OD1 1 
ATOM   3919  N ND2 . ASN A 1 527  ? 227.872 209.882 292.624 1.00 98.55  ? 510  ASN B ND2 1 
ATOM   3920  N N   . GLU A 1 528  ? 225.233 205.653 295.011 1.00 94.15  ? 511  GLU B N   1 
ATOM   3921  C CA  . GLU A 1 528  ? 223.998 205.417 295.746 1.00 94.15  ? 511  GLU B CA  1 
ATOM   3922  C C   . GLU A 1 528  ? 224.063 206.189 297.054 1.00 94.15  ? 511  GLU B C   1 
ATOM   3923  O O   . GLU A 1 528  ? 225.031 206.017 297.816 1.00 94.15  ? 511  GLU B O   1 
ATOM   3924  C CB  . GLU A 1 528  ? 223.791 203.926 296.008 1.00 94.15  ? 511  GLU B CB  1 
ATOM   3925  C CG  . GLU A 1 528  ? 222.792 203.277 295.072 1.00 94.15  ? 511  GLU B CG  1 
ATOM   3926  C CD  . GLU A 1 528  ? 223.139 201.838 294.763 1.00 94.15  ? 511  GLU B CD  1 
ATOM   3927  O OE1 . GLU A 1 528  ? 223.973 201.260 295.488 1.00 94.15  ? 511  GLU B OE1 1 
ATOM   3928  O OE2 . GLU A 1 528  ? 222.581 201.287 293.792 1.00 94.15  ? 511  GLU B OE2 1 
ATOM   3929  N N   . PRO A 1 529  ? 223.094 207.070 297.336 1.00 90.32  ? 512  PRO B N   1 
ATOM   3930  C CA  . PRO A 1 529  ? 223.126 207.858 298.571 1.00 90.32  ? 512  PRO B CA  1 
ATOM   3931  C C   . PRO A 1 529  ? 223.482 207.055 299.809 1.00 90.32  ? 512  PRO B C   1 
ATOM   3932  O O   . PRO A 1 529  ? 222.741 206.157 300.219 1.00 90.32  ? 512  PRO B O   1 
ATOM   3933  C CB  . PRO A 1 529  ? 221.691 208.382 298.653 1.00 90.32  ? 512  PRO B CB  1 
ATOM   3934  C CG  . PRO A 1 529  ? 221.267 208.530 297.181 1.00 90.32  ? 512  PRO B CG  1 
ATOM   3935  C CD  . PRO A 1 529  ? 222.280 207.764 296.327 1.00 90.32  ? 512  PRO B CD  1 
ATOM   3936  N N   . GLU A 1 530  ? 224.621 207.385 300.409 1.00 92.43  ? 513  GLU B N   1 
ATOM   3937  C CA  . GLU A 1 530  ? 225.098 206.664 301.577 1.00 92.43  ? 513  GLU B CA  1 
ATOM   3938  C C   . GLU A 1 530  ? 224.180 206.910 302.766 1.00 92.43  ? 513  GLU B C   1 
ATOM   3939  O O   . GLU A 1 530  ? 223.517 207.945 302.864 1.00 92.43  ? 513  GLU B O   1 
ATOM   3940  C CB  . GLU A 1 530  ? 226.529 207.084 301.920 1.00 92.43  ? 513  GLU B CB  1 
ATOM   3941  C CG  . GLU A 1 530  ? 226.872 208.533 301.584 1.00 92.43  ? 513  GLU B CG  1 
ATOM   3942  C CD  . GLU A 1 530  ? 227.324 208.722 300.145 1.00 92.43  ? 513  GLU B CD  1 
ATOM   3943  O OE1 . GLU A 1 530  ? 226.541 208.407 299.224 1.00 92.43  ? 513  GLU B OE1 1 
ATOM   3944  O OE2 . GLU A 1 530  ? 228.464 209.185 299.933 1.00 92.43  ? 513  GLU B OE2 1 
ATOM   3945  N N   . ASN A 1 531  ? 224.140 205.936 303.671 1.00 90.93  ? 514  ASN B N   1 
ATOM   3946  C CA  . ASN A 1 531  ? 223.296 206.059 304.849 1.00 90.93  ? 514  ASN B CA  1 
ATOM   3947  C C   . ASN A 1 531  ? 223.748 207.234 305.705 1.00 90.93  ? 514  ASN B C   1 
ATOM   3948  O O   . ASN A 1 531  ? 224.944 207.441 305.930 1.00 90.93  ? 514  ASN B O   1 
ATOM   3949  C CB  . ASN A 1 531  ? 223.324 204.764 305.660 1.00 90.93  ? 514  ASN B CB  1 
ATOM   3950  C CG  . ASN A 1 531  ? 222.068 203.939 305.474 1.00 90.93  ? 514  ASN B CG  1 
ATOM   3951  O OD1 . ASN A 1 531  ? 220.981 204.344 305.880 1.00 90.93  ? 514  ASN B OD1 1 
ATOM   3952  N ND2 . ASN A 1 531  ? 222.211 202.778 304.848 1.00 90.93  ? 514  ASN B ND2 1 
ATOM   3953  N N   . ILE A 1 532  ? 222.779 208.008 306.179 1.00 92.09  ? 515  ILE B N   1 
ATOM   3954  C CA  . ILE A 1 532  ? 223.030 209.229 306.930 1.00 92.09  ? 515  ILE B CA  1 
ATOM   3955  C C   . ILE A 1 532  ? 222.468 209.074 308.334 1.00 92.09  ? 515  ILE B C   1 
ATOM   3956  O O   . ILE A 1 532  ? 221.380 208.519 308.524 1.00 92.09  ? 515  ILE B O   1 
ATOM   3957  C CB  . ILE A 1 532  ? 222.425 210.460 306.222 1.00 92.09  ? 515  ILE B CB  1 
ATOM   3958  C CG1 . ILE A 1 532  ? 222.848 211.748 306.933 1.00 92.09  ? 515  ILE B CG1 1 
ATOM   3959  C CG2 . ILE A 1 532  ? 220.910 210.337 306.100 1.00 92.09  ? 515  ILE B CG2 1 
ATOM   3960  C CD1 . ILE A 1 532  ? 222.148 212.976 306.422 1.00 92.09  ? 515  ILE B CD1 1 
ATOM   3961  N N   . SER A 1 533  ? 223.227 209.542 309.320 1.00 95.93  ? 516  SER B N   1 
ATOM   3962  C CA  . SER A 1 533  ? 222.771 209.518 310.701 1.00 95.93  ? 516  SER B CA  1 
ATOM   3963  C C   . SER A 1 533  ? 221.771 210.642 310.932 1.00 95.93  ? 516  SER B C   1 
ATOM   3964  O O   . SER A 1 533  ? 222.061 211.810 310.656 1.00 95.93  ? 516  SER B O   1 
ATOM   3965  C CB  . SER A 1 533  ? 223.954 209.656 311.657 1.00 95.93  ? 516  SER B CB  1 
ATOM   3966  O OG  . SER A 1 533  ? 224.238 211.019 311.915 1.00 95.93  ? 516  SER B OG  1 
ATOM   3967  N N   . ILE A 1 534  ? 220.596 210.288 311.442 1.00 92.88  ? 517  ILE B N   1 
ATOM   3968  C CA  . ILE A 1 534  ? 219.532 211.241 311.729 1.00 92.88  ? 517  ILE B CA  1 
ATOM   3969  C C   . ILE A 1 534  ? 219.276 211.215 313.228 1.00 92.88  ? 517  ILE B C   1 
ATOM   3970  O O   . ILE A 1 534  ? 219.167 210.137 313.822 1.00 92.88  ? 517  ILE B O   1 
ATOM   3971  C CB  . ILE A 1 534  ? 218.249 210.915 310.942 1.00 92.88  ? 517  ILE B CB  1 
ATOM   3972  C CG1 . ILE A 1 534  ? 218.320 211.501 309.533 1.00 92.88  ? 517  ILE B CG1 1 
ATOM   3973  C CG2 . ILE A 1 534  ? 217.022 211.453 311.656 1.00 92.88  ? 517  ILE B CG2 1 
ATOM   3974  C CD1 . ILE A 1 534  ? 217.244 210.982 308.607 1.00 92.88  ? 517  ILE B CD1 1 
ATOM   3975  N N   . GLU A 1 535  ? 219.207 212.397 313.840 1.00 95.72  ? 518  GLU B N   1 
ATOM   3976  C CA  . GLU A 1 535  ? 218.885 212.476 315.258 1.00 95.72  ? 518  GLU B CA  1 
ATOM   3977  C C   . GLU A 1 535  ? 217.527 211.835 315.516 1.00 95.72  ? 518  GLU B C   1 
ATOM   3978  O O   . GLU A 1 535  ? 216.563 212.077 314.784 1.00 95.72  ? 518  GLU B O   1 
ATOM   3979  C CB  . GLU A 1 535  ? 218.904 213.934 315.727 1.00 95.72  ? 518  GLU B CB  1 
ATOM   3980  C CG  . GLU A 1 535  ? 217.900 214.848 315.040 1.00 95.72  ? 518  GLU B CG  1 
ATOM   3981  C CD  . GLU A 1 535  ? 216.699 215.158 315.911 1.00 95.72  ? 518  GLU B CD  1 
ATOM   3982  O OE1 . GLU A 1 535  ? 216.673 214.709 317.076 1.00 95.72  ? 518  GLU B OE1 1 
ATOM   3983  O OE2 . GLU A 1 535  ? 215.780 215.855 315.431 1.00 95.72  ? 518  GLU B OE2 1 
ATOM   3984  N N   . ASN A 1 536  ? 217.462 210.997 316.548 1.00 94.54  ? 519  ASN B N   1 
ATOM   3985  C CA  . ASN A 1 536  ? 216.276 210.182 316.770 1.00 94.54  ? 519  ASN B CA  1 
ATOM   3986  C C   . ASN A 1 536  ? 215.061 211.049 317.073 1.00 94.54  ? 519  ASN B C   1 
ATOM   3987  O O   . ASN A 1 536  ? 215.161 212.089 317.730 1.00 94.54  ? 519  ASN B O   1 
ATOM   3988  C CB  . ASN A 1 536  ? 216.520 209.183 317.903 1.00 94.54  ? 519  ASN B CB  1 
ATOM   3989  C CG  . ASN A 1 536  ? 216.788 209.856 319.233 1.00 94.54  ? 519  ASN B CG  1 
ATOM   3990  O OD1 . ASN A 1 536  ? 217.110 211.042 319.292 1.00 94.54  ? 519  ASN B OD1 1 
ATOM   3991  N ND2 . ASN A 1 536  ? 216.656 209.097 320.313 1.00 94.54  ? 519  ASN B ND2 1 
ATOM   3992  N N   . LEU A 1 537  ? 213.911 210.622 316.569 1.00 89.81  ? 520  LEU B N   1 
ATOM   3993  C CA  . LEU A 1 537  ? 212.661 211.335 316.751 1.00 89.81  ? 520  LEU B CA  1 
ATOM   3994  C C   . LEU A 1 537  ? 211.886 210.740 317.923 1.00 89.81  ? 520  LEU B C   1 
ATOM   3995  O O   . LEU A 1 537  ? 212.397 209.916 318.687 1.00 89.81  ? 520  LEU B O   1 
ATOM   3996  C CB  . LEU A 1 537  ? 211.840 211.308 315.462 1.00 89.81  ? 520  LEU B CB  1 
ATOM   3997  C CG  . LEU A 1 537  ? 212.576 211.424 314.130 1.00 89.81  ? 520  LEU B CG  1 
ATOM   3998  C CD1 . LEU A 1 537  ? 211.563 211.495 313.016 1.00 89.81  ? 520  LEU B CD1 1 
ATOM   3999  C CD2 . LEU A 1 537  ? 213.466 212.652 314.105 1.00 89.81  ? 520  LEU B CD2 1 
ATOM   4000  N N   . SER A 1 538  ? 210.634 211.162 318.064 1.00 90.55  ? 521  SER B N   1 
ATOM   4001  C CA  . SER A 1 538  ? 209.797 210.688 319.152 1.00 90.55  ? 521  SER B CA  1 
ATOM   4002  C C   . SER A 1 538  ? 209.499 209.200 318.992 1.00 90.55  ? 521  SER B C   1 
ATOM   4003  O O   . SER A 1 538  ? 209.630 208.622 317.910 1.00 90.55  ? 521  SER B O   1 
ATOM   4004  C CB  . SER A 1 538  ? 208.491 211.481 319.207 1.00 90.55  ? 521  SER B CB  1 
ATOM   4005  O OG  . SER A 1 538  ? 208.719 212.805 319.656 1.00 90.55  ? 521  SER B OG  1 
ATOM   4006  N N   . SER A 1 539  ? 209.097 208.577 320.103 1.00 89.67  ? 522  SER B N   1 
ATOM   4007  C CA  . SER A 1 539  ? 208.791 207.151 320.083 1.00 89.67  ? 522  SER B CA  1 
ATOM   4008  C C   . SER A 1 539  ? 207.630 206.847 319.146 1.00 89.67  ? 522  SER B C   1 
ATOM   4009  O O   . SER A 1 539  ? 207.673 205.870 318.389 1.00 89.67  ? 522  SER B O   1 
ATOM   4010  C CB  . SER A 1 539  ? 208.483 206.664 321.497 1.00 89.67  ? 522  SER B CB  1 
ATOM   4011  O OG  . SER A 1 539  ? 207.837 207.673 322.251 1.00 89.67  ? 522  SER B OG  1 
ATOM   4012  N N   . ASP A 1 540  ? 206.587 207.670 319.176 1.00 92.66  ? 523  ASP B N   1 
ATOM   4013  C CA  . ASP A 1 540  ? 205.425 207.495 318.316 1.00 92.66  ? 523  ASP B CA  1 
ATOM   4014  C C   . ASP A 1 540  ? 205.477 208.523 317.193 1.00 92.66  ? 523  ASP B C   1 
ATOM   4015  O O   . ASP A 1 540  ? 205.459 209.731 317.450 1.00 92.66  ? 523  ASP B O   1 
ATOM   4016  C CB  . ASP A 1 540  ? 204.129 207.635 319.114 1.00 92.66  ? 523  ASP B CB  1 
ATOM   4017  C CG  . ASP A 1 540  ? 203.844 206.424 319.979 1.00 92.66  ? 523  ASP B CG  1 
ATOM   4018  O OD1 . ASP A 1 540  ? 204.795 205.682 320.297 1.00 92.66  ? 523  ASP B OD1 1 
ATOM   4019  O OD2 . ASP A 1 540  ? 202.668 206.214 320.341 1.00 92.66  ? 523  ASP B OD2 1 
ATOM   4020  N N   . ILE A 1 541  ? 205.539 208.041 315.956 1.00 89.27  ? 524  ILE B N   1 
ATOM   4021  C CA  . ILE A 1 541  ? 205.558 208.903 314.781 1.00 89.27  ? 524  ILE B CA  1 
ATOM   4022  C C   . ILE A 1 541  ? 204.115 209.115 314.342 1.00 89.27  ? 524  ILE B C   1 
ATOM   4023  O O   . ILE A 1 541  ? 203.488 208.213 313.782 1.00 89.27  ? 524  ILE B O   1 
ATOM   4024  C CB  . ILE A 1 541  ? 206.396 208.297 313.651 1.00 89.27  ? 524  ILE B CB  1 
ATOM   4025  C CG1 . ILE A 1 541  ? 207.807 207.972 314.142 1.00 89.27  ? 524  ILE B CG1 1 
ATOM   4026  C CG2 . ILE A 1 541  ? 206.443 209.238 312.464 1.00 89.27  ? 524  ILE B CG2 1 
ATOM   4027  C CD1 . ILE A 1 541  ? 208.735 209.160 314.156 1.00 89.27  ? 524  ILE B CD1 1 
ATOM   4028  N N   . ILE A 1 542  ? 203.588 210.308 314.593 1.00 93.48  ? 525  ILE B N   1 
ATOM   4029  C CA  . ILE A 1 542  ? 202.218 210.628 314.209 1.00 93.48  ? 525  ILE B CA  1 
ATOM   4030  C C   . ILE A 1 542  ? 202.183 210.934 312.716 1.00 93.48  ? 525  ILE B C   1 
ATOM   4031  O O   . ILE A 1 542  ? 203.053 211.635 312.189 1.00 93.48  ? 525  ILE B O   1 
ATOM   4032  C CB  . ILE A 1 542  ? 201.662 211.792 315.046 1.00 93.48  ? 525  ILE B CB  1 
ATOM   4033  C CG1 . ILE A 1 542  ? 202.234 213.139 314.597 1.00 93.48  ? 525  ILE B CG1 1 
ATOM   4034  C CG2 . ILE A 1 542  ? 201.945 211.562 316.524 1.00 93.48  ? 525  ILE B CG2 1 
ATOM   4035  C CD1 . ILE A 1 542  ? 201.502 214.333 315.165 1.00 93.48  ? 525  ILE B CD1 1 
ATOM   4036  N N   . GLY A 1 543  ? 201.208 210.357 312.020 1.00 91.91  ? 526  GLY B N   1 
ATOM   4037  C CA  . GLY A 1 543  ? 201.070 210.567 310.593 1.00 91.91  ? 526  GLY B CA  1 
ATOM   4038  C C   . GLY A 1 543  ? 199.888 209.827 310.005 1.00 91.91  ? 526  GLY B C   1 
ATOM   4039  O O   . GLY A 1 543  ? 199.628 208.674 310.360 1.00 91.91  ? 526  GLY B O   1 
ATOM   4040  N N   . GLN A 1 544  ? 199.169 210.477 309.097 1.00 92.66  ? 527  GLN B N   1 
ATOM   4041  C CA  . GLN A 1 544  ? 197.987 209.910 308.467 1.00 92.66  ? 527  GLN B CA  1 
ATOM   4042  C C   . GLN A 1 544  ? 198.274 209.673 306.992 1.00 92.66  ? 527  GLN B C   1 
ATOM   4043  O O   . GLN A 1 544  ? 198.990 210.456 306.360 1.00 92.66  ? 527  GLN B O   1 
ATOM   4044  C CB  . GLN A 1 544  ? 196.781 210.841 308.631 1.00 92.66  ? 527  GLN B CB  1 
ATOM   4045  C CG  . GLN A 1 544  ? 195.475 210.286 308.092 1.00 92.66  ? 527  GLN B CG  1 
ATOM   4046  C CD  . GLN A 1 544  ? 194.788 209.363 309.075 1.00 92.66  ? 527  GLN B CD  1 
ATOM   4047  O OE1 . GLN A 1 544  ? 195.176 209.279 310.240 1.00 92.66  ? 527  GLN B OE1 1 
ATOM   4048  N NE2 . GLN A 1 544  ? 193.758 208.665 308.610 1.00 92.66  ? 527  GLN B NE2 1 
ATOM   4049  N N   . LEU A 1 545  ? 197.714 208.593 306.449 1.00 87.82  ? 528  LEU B N   1 
ATOM   4050  C CA  . LEU A 1 545  ? 197.952 208.241 305.057 1.00 87.82  ? 528  LEU B CA  1 
ATOM   4051  C C   . LEU A 1 545  ? 197.512 209.365 304.124 1.00 87.82  ? 528  LEU B C   1 
ATOM   4052  O O   . LEU A 1 545  ? 196.777 210.279 304.505 1.00 87.82  ? 528  LEU B O   1 
ATOM   4053  C CB  . LEU A 1 545  ? 197.214 206.957 304.690 1.00 87.82  ? 528  LEU B CB  1 
ATOM   4054  C CG  . LEU A 1 545  ? 197.788 205.654 305.234 1.00 87.82  ? 528  LEU B CG  1 
ATOM   4055  C CD1 . LEU A 1 545  ? 196.675 204.790 305.775 1.00 87.82  ? 528  LEU B CD1 1 
ATOM   4056  C CD2 . LEU A 1 545  ? 198.553 204.923 304.151 1.00 87.82  ? 528  LEU B CD2 1 
ATOM   4057  N N   . GLU A 1 546  ? 197.984 209.290 302.882 1.00 95.52  ? 529  GLU B N   1 
ATOM   4058  C CA  . GLU A 1 546  ? 197.568 210.251 301.873 1.00 95.52  ? 529  GLU B CA  1 
ATOM   4059  C C   . GLU A 1 546  ? 196.072 210.122 301.628 1.00 95.52  ? 529  GLU B C   1 
ATOM   4060  O O   . GLU A 1 546  ? 195.563 209.026 301.382 1.00 95.52  ? 529  GLU B O   1 
ATOM   4061  C CB  . GLU A 1 546  ? 198.342 210.022 300.576 1.00 95.52  ? 529  GLU B CB  1 
ATOM   4062  C CG  . GLU A 1 546  ? 197.865 210.865 299.407 1.00 95.52  ? 529  GLU B CG  1 
ATOM   4063  C CD  . GLU A 1 546  ? 198.706 212.109 299.204 1.00 95.52  ? 529  GLU B CD  1 
ATOM   4064  O OE1 . GLU A 1 546  ? 199.841 212.152 299.722 1.00 95.52  ? 529  GLU B OE1 1 
ATOM   4065  O OE2 . GLU A 1 546  ? 198.232 213.044 298.526 1.00 95.52  ? 529  GLU B OE2 1 
ATOM   4066  N N   . LEU A 1 547  ? 195.367 211.248 301.700 1.00 111.72 ? 530  LEU B N   1 
ATOM   4067  C CA  . LEU A 1 547  ? 193.917 211.227 301.578 1.00 111.72 ? 530  LEU B CA  1 
ATOM   4068  C C   . LEU A 1 547  ? 193.510 210.850 300.161 1.00 111.72 ? 530  LEU B C   1 
ATOM   4069  O O   . LEU A 1 547  ? 194.034 211.395 299.185 1.00 111.72 ? 530  LEU B O   1 
ATOM   4070  C CB  . LEU A 1 547  ? 193.332 212.586 301.957 1.00 111.72 ? 530  LEU B CB  1 
ATOM   4071  C CG  . LEU A 1 547  ? 192.788 212.688 303.382 1.00 111.72 ? 530  LEU B CG  1 
ATOM   4072  C CD1 . LEU A 1 547  ? 192.164 214.052 303.626 1.00 111.72 ? 530  LEU B CD1 1 
ATOM   4073  C CD2 . LEU A 1 547  ? 191.781 211.579 303.646 1.00 111.72 ? 530  LEU B CD2 1 
ATOM   4074  N N   . MET A 1 548  ? 192.586 209.928 300.054 1.00 121.90 ? 531  MET B N   1 
ATOM   4075  C CA  . MET A 1 548  ? 192.115 209.483 298.757 1.00 121.90 ? 531  MET B CA  1 
ATOM   4076  C C   . MET A 1 548  ? 190.725 210.040 298.474 1.00 121.90 ? 531  MET B C   1 
ATOM   4077  O O   . MET A 1 548  ? 189.924 210.225 299.395 1.00 121.90 ? 531  MET B O   1 
ATOM   4078  C CB  . MET A 1 548  ? 192.071 207.953 298.700 1.00 121.90 ? 531  MET B CB  1 
ATOM   4079  C CG  . MET A 1 548  ? 193.182 207.278 299.484 1.00 121.90 ? 531  MET B CG  1 
ATOM   4080  S SD  . MET A 1 548  ? 192.898 207.329 301.265 1.00 121.90 ? 531  MET B SD  1 
ATOM   4081  C CE  . MET A 1 548  ? 191.614 206.094 301.443 1.00 121.90 ? 531  MET B CE  1 
ATOM   4082  N N   . PRO A 1 549  ? 190.416 210.329 297.213 1.00 128.34 ? 532  PRO B N   1 
ATOM   4083  C CA  . PRO A 1 549  ? 189.069 210.799 296.879 1.00 128.34 ? 532  PRO B CA  1 
ATOM   4084  C C   . PRO A 1 549  ? 188.032 209.712 297.109 1.00 128.34 ? 532  PRO B C   1 
ATOM   4085  O O   . PRO A 1 549  ? 188.308 208.517 296.981 1.00 128.34 ? 532  PRO B O   1 
ATOM   4086  C CB  . PRO A 1 549  ? 189.178 211.160 295.393 1.00 128.34 ? 532  PRO B CB  1 
ATOM   4087  C CG  . PRO A 1 549  ? 190.315 210.339 294.891 1.00 128.34 ? 532  PRO B CG  1 
ATOM   4088  C CD  . PRO A 1 549  ? 191.285 210.245 296.028 1.00 128.34 ? 532  PRO B CD  1 
ATOM   4089  N N   . ASN A 1 550  ? 186.824 210.145 297.460 1.00 136.43 ? 533  ASN B N   1 
ATOM   4090  C CA  . ASN A 1 550  ? 185.730 209.216 297.709 1.00 136.43 ? 533  ASN B CA  1 
ATOM   4091  C C   . ASN A 1 550  ? 185.135 208.745 296.389 1.00 136.43 ? 533  ASN B C   1 
ATOM   4092  O O   . ASN A 1 550  ? 184.831 209.556 295.509 1.00 136.43 ? 533  ASN B O   1 
ATOM   4093  C CB  . ASN A 1 550  ? 184.655 209.874 298.571 1.00 136.43 ? 533  ASN B CB  1 
ATOM   4094  C CG  . ASN A 1 550  ? 185.202 210.396 299.884 1.00 136.43 ? 533  ASN B CG  1 
ATOM   4095  O OD1 . ASN A 1 550  ? 184.717 211.393 300.418 1.00 136.43 ? 533  ASN B OD1 1 
ATOM   4096  N ND2 . ASN A 1 550  ? 186.216 209.722 300.413 1.00 136.43 ? 533  ASN B ND2 1 
ATOM   4097  N N   . ILE A 1 551  ? 184.969 207.432 296.253 1.00 131.37 ? 534  ILE B N   1 
ATOM   4098  C CA  . ILE A 1 551  ? 184.406 206.823 295.055 1.00 131.37 ? 534  ILE B CA  1 
ATOM   4099  C C   . ILE A 1 551  ? 182.989 206.376 295.381 1.00 131.37 ? 534  ILE B C   1 
ATOM   4100  O O   . ILE A 1 551  ? 182.783 205.524 296.255 1.00 131.37 ? 534  ILE B O   1 
ATOM   4101  C CB  . ILE A 1 551  ? 185.258 205.644 294.561 1.00 131.37 ? 534  ILE B CB  1 
ATOM   4102  C CG1 . ILE A 1 551  ? 186.587 206.147 293.993 1.00 131.37 ? 534  ILE B CG1 1 
ATOM   4103  C CG2 . ILE A 1 551  ? 184.503 204.844 293.512 1.00 131.37 ? 534  ILE B CG2 1 
ATOM   4104  C CD1 . ILE A 1 551  ? 187.752 206.008 294.949 1.00 131.37 ? 534  ILE B CD1 1 
ATOM   4105  N N   . GLU A 1 552  ? 182.014 206.952 294.684 1.00 129.20 ? 535  GLU B N   1 
ATOM   4106  C CA  . GLU A 1 552  ? 180.620 206.619 294.933 1.00 129.20 ? 535  GLU B CA  1 
ATOM   4107  C C   . GLU A 1 552  ? 180.296 205.231 294.396 1.00 129.20 ? 535  GLU B C   1 
ATOM   4108  O O   . GLU A 1 552  ? 180.774 204.829 293.332 1.00 129.20 ? 535  GLU B O   1 
ATOM   4109  C CB  . GLU A 1 552  ? 179.703 207.660 294.292 1.00 129.20 ? 535  GLU B CB  1 
ATOM   4110  C CG  . GLU A 1 552  ? 179.785 209.047 294.919 1.00 129.20 ? 535  GLU B CG  1 
ATOM   4111  C CD  . GLU A 1 552  ? 179.882 209.018 296.436 1.00 129.20 ? 535  GLU B CD  1 
ATOM   4112  O OE1 . GLU A 1 552  ? 179.101 208.283 297.078 1.00 129.20 ? 535  GLU B OE1 1 
ATOM   4113  O OE2 . GLU A 1 552  ? 180.744 209.735 296.989 1.00 129.20 ? 535  GLU B OE2 1 
ATOM   4114  N N   . ARG A 1 553  ? 179.473 204.499 295.141 1.00 114.70 ? 536  ARG B N   1 
ATOM   4115  C CA  . ARG A 1 553  ? 179.093 203.149 294.747 1.00 114.70 ? 536  ARG B CA  1 
ATOM   4116  C C   . ARG A 1 553  ? 178.126 203.202 293.572 1.00 114.70 ? 536  ARG B C   1 
ATOM   4117  O O   . ARG A 1 553  ? 177.073 203.844 293.653 1.00 114.70 ? 536  ARG B O   1 
ATOM   4118  C CB  . ARG A 1 553  ? 178.463 202.418 295.928 1.00 114.70 ? 536  ARG B CB  1 
ATOM   4119  C CG  . ARG A 1 553  ? 179.246 202.546 297.220 1.00 114.70 ? 536  ARG B CG  1 
ATOM   4120  C CD  . ARG A 1 553  ? 180.004 201.270 297.522 1.00 114.70 ? 536  ARG B CD  1 
ATOM   4121  N NE  . ARG A 1 553  ? 179.142 200.100 297.425 1.00 114.70 ? 536  ARG B NE  1 
ATOM   4122  C CZ  . ARG A 1 553  ? 179.580 198.855 297.304 1.00 114.70 ? 536  ARG B CZ  1 
ATOM   4123  N NH1 . ARG A 1 553  ? 180.873 198.579 297.267 1.00 114.70 ? 536  ARG B NH1 1 
ATOM   4124  N NH2 . ARG A 1 553  ? 178.699 197.863 297.219 1.00 114.70 ? 536  ARG B NH2 1 
ATOM   4125  N N   . PHE A 1 554  ? 178.483 202.533 292.483 1.00 105.68 ? 537  PHE B N   1 
ATOM   4126  C CA  . PHE A 1 554  ? 177.611 202.493 291.321 1.00 105.68 ? 537  PHE B CA  1 
ATOM   4127  C C   . PHE A 1 554  ? 176.365 201.664 291.626 1.00 105.68 ? 537  PHE B C   1 
ATOM   4128  O O   . PHE A 1 554  ? 176.448 200.654 292.332 1.00 105.68 ? 537  PHE B O   1 
ATOM   4129  C CB  . PHE A 1 554  ? 178.350 201.909 290.119 1.00 105.68 ? 537  PHE B CB  1 
ATOM   4130  C CG  . PHE A 1 554  ? 179.837 202.107 290.170 1.00 105.68 ? 537  PHE B CG  1 
ATOM   4131  C CD1 . PHE A 1 554  ? 180.397 203.331 289.847 1.00 105.68 ? 537  PHE B CD1 1 
ATOM   4132  C CD2 . PHE A 1 554  ? 180.676 201.070 290.542 1.00 105.68 ? 537  PHE B CD2 1 
ATOM   4133  C CE1 . PHE A 1 554  ? 181.765 203.518 289.893 1.00 105.68 ? 537  PHE B CE1 1 
ATOM   4134  C CE2 . PHE A 1 554  ? 182.045 201.253 290.590 1.00 105.68 ? 537  PHE B CE2 1 
ATOM   4135  C CZ  . PHE A 1 554  ? 182.589 202.478 290.265 1.00 105.68 ? 537  PHE B CZ  1 
ATOM   4136  N N   . PRO A 1 555  ? 175.201 202.062 291.113 1.00 99.35  ? 538  PRO B N   1 
ATOM   4137  C CA  . PRO A 1 555  ? 173.979 201.296 291.380 1.00 99.35  ? 538  PRO B CA  1 
ATOM   4138  C C   . PRO A 1 555  ? 174.050 199.905 290.772 1.00 99.35  ? 538  PRO B C   1 
ATOM   4139  O O   . PRO A 1 555  ? 174.707 199.677 289.754 1.00 99.35  ? 538  PRO B O   1 
ATOM   4140  C CB  . PRO A 1 555  ? 172.879 202.140 290.727 1.00 99.35  ? 538  PRO B CB  1 
ATOM   4141  C CG  . PRO A 1 555  ? 173.587 202.968 289.709 1.00 99.35  ? 538  PRO B CG  1 
ATOM   4142  C CD  . PRO A 1 555  ? 174.944 203.245 290.276 1.00 99.35  ? 538  PRO B CD  1 
ATOM   4143  N N   . ASN A 1 556  ? 173.357 198.969 291.412 1.00 86.66  ? 539  ASN B N   1 
ATOM   4144  C CA  . ASN A 1 556  ? 173.383 197.566 291.031 1.00 86.66  ? 539  ASN B CA  1 
ATOM   4145  C C   . ASN A 1 556  ? 172.002 197.116 290.579 1.00 86.66  ? 539  ASN B C   1 
ATOM   4146  O O   . ASN A 1 556  ? 170.979 197.611 291.061 1.00 86.66  ? 539  ASN B O   1 
ATOM   4147  C CB  . ASN A 1 556  ? 173.853 196.688 292.196 1.00 86.66  ? 539  ASN B CB  1 
ATOM   4148  C CG  . ASN A 1 556  ? 174.254 195.299 291.754 1.00 86.66  ? 539  ASN B CG  1 
ATOM   4149  O OD1 . ASN A 1 556  ? 173.956 194.880 290.638 1.00 86.66  ? 539  ASN B OD1 1 
ATOM   4150  N ND2 . ASN A 1 556  ? 174.927 194.570 292.635 1.00 86.66  ? 539  ASN B ND2 1 
ATOM   4151  N N   . GLY A 1 557  ? 171.985 196.167 289.650 1.00 81.51  ? 540  GLY B N   1 
ATOM   4152  C CA  . GLY A 1 557  ? 170.744 195.560 289.205 1.00 81.51  ? 540  GLY B CA  1 
ATOM   4153  C C   . GLY A 1 557  ? 169.800 196.484 288.468 1.00 81.51  ? 540  GLY B C   1 
ATOM   4154  O O   . GLY A 1 557  ? 168.586 196.436 288.704 1.00 81.51  ? 540  GLY B O   1 
ATOM   4155  N N   . LYS A 1 558  ? 170.322 197.327 287.583 1.00 80.23  ? 541  LYS B N   1 
ATOM   4156  C CA  . LYS A 1 558  ? 169.461 198.188 286.786 1.00 80.23  ? 541  LYS B CA  1 
ATOM   4157  C C   . LYS A 1 558  ? 168.670 197.364 285.781 1.00 80.23  ? 541  LYS B C   1 
ATOM   4158  O O   . LYS A 1 558  ? 169.215 196.490 285.103 1.00 80.23  ? 541  LYS B O   1 
ATOM   4159  C CB  . LYS A 1 558  ? 170.286 199.249 286.061 1.00 80.23  ? 541  LYS B CB  1 
ATOM   4160  C CG  . LYS A 1 558  ? 170.293 200.604 286.749 1.00 80.23  ? 541  LYS B CG  1 
ATOM   4161  C CD  . LYS A 1 558  ? 168.878 201.112 286.986 1.00 80.23  ? 541  LYS B CD  1 
ATOM   4162  C CE  . LYS A 1 558  ? 168.111 201.266 285.680 1.00 80.23  ? 541  LYS B CE  1 
ATOM   4163  N NZ  . LYS A 1 558  ? 166.717 201.739 285.902 1.00 80.23  ? 541  LYS B NZ  1 
ATOM   4164  N N   . LYS A 1 559  ? 167.377 197.652 285.682 1.00 76.60  ? 542  LYS B N   1 
ATOM   4165  C CA  . LYS A 1 559  ? 166.477 196.933 284.792 1.00 76.60  ? 542  LYS B CA  1 
ATOM   4166  C C   . LYS A 1 559  ? 166.322 197.706 283.490 1.00 76.60  ? 542  LYS B C   1 
ATOM   4167  O O   . LYS A 1 559  ? 166.026 198.905 283.506 1.00 76.60  ? 542  LYS B O   1 
ATOM   4168  C CB  . LYS A 1 559  ? 165.113 196.727 285.449 1.00 76.60  ? 542  LYS B CB  1 
ATOM   4169  C CG  . LYS A 1 559  ? 163.968 196.584 284.466 1.00 76.60  ? 542  LYS B CG  1 
ATOM   4170  C CD  . LYS A 1 559  ? 162.675 196.222 285.174 1.00 76.60  ? 542  LYS B CD  1 
ATOM   4171  C CE  . LYS A 1 559  ? 162.516 194.718 285.300 1.00 76.60  ? 542  LYS B CE  1 
ATOM   4172  N NZ  . LYS A 1 559  ? 161.216 194.351 285.926 1.00 76.60  ? 542  LYS B NZ  1 
ATOM   4173  N N   . TYR A 1 560  ? 166.519 197.019 282.370 1.00 79.12  ? 543  TYR B N   1 
ATOM   4174  C CA  . TYR A 1 560  ? 166.403 197.613 281.047 1.00 79.12  ? 543  TYR B CA  1 
ATOM   4175  C C   . TYR A 1 560  ? 165.336 196.874 280.257 1.00 79.12  ? 543  TYR B C   1 
ATOM   4176  O O   . TYR A 1 560  ? 165.298 195.640 280.264 1.00 79.12  ? 543  TYR B O   1 
ATOM   4177  C CB  . TYR A 1 560  ? 167.740 197.571 280.305 1.00 79.12  ? 543  TYR B CB  1 
ATOM   4178  C CG  . TYR A 1 560  ? 168.744 198.563 280.829 1.00 79.12  ? 543  TYR B CG  1 
ATOM   4179  C CD1 . TYR A 1 560  ? 169.589 198.237 281.878 1.00 79.12  ? 543  TYR B CD1 1 
ATOM   4180  C CD2 . TYR A 1 560  ? 168.838 199.834 280.283 1.00 79.12  ? 543  TYR B CD2 1 
ATOM   4181  C CE1 . TYR A 1 560  ? 170.504 199.146 282.363 1.00 79.12  ? 543  TYR B CE1 1 
ATOM   4182  C CE2 . TYR A 1 560  ? 169.748 200.751 280.762 1.00 79.12  ? 543  TYR B CE2 1 
ATOM   4183  C CZ  . TYR A 1 560  ? 170.578 200.403 281.800 1.00 79.12  ? 543  TYR B CZ  1 
ATOM   4184  O OH  . TYR A 1 560  ? 171.487 201.318 282.277 1.00 79.12  ? 543  TYR B OH  1 
ATOM   4185  N N   . GLU A 1 561  ? 164.469 197.626 279.590 1.00 84.44  ? 544  GLU B N   1 
ATOM   4186  C CA  . GLU A 1 561  ? 163.450 197.066 278.714 1.00 84.44  ? 544  GLU B CA  1 
ATOM   4187  C C   . GLU A 1 561  ? 163.744 197.510 277.289 1.00 84.44  ? 544  GLU B C   1 
ATOM   4188  O O   . GLU A 1 561  ? 163.749 198.711 276.999 1.00 84.44  ? 544  GLU B O   1 
ATOM   4189  C CB  . GLU A 1 561  ? 162.051 197.502 279.145 1.00 84.44  ? 544  GLU B CB  1 
ATOM   4190  C CG  . GLU A 1 561  ? 161.503 196.711 280.320 1.00 84.44  ? 544  GLU B CG  1 
ATOM   4191  C CD  . GLU A 1 561  ? 160.255 197.332 280.915 1.00 84.44  ? 544  GLU B CD  1 
ATOM   4192  O OE1 . GLU A 1 561  ? 159.390 197.790 280.140 1.00 84.44  ? 544  GLU B OE1 1 
ATOM   4193  O OE2 . GLU A 1 561  ? 160.140 197.361 282.158 1.00 84.44  ? 544  GLU B OE2 1 
ATOM   4194  N N   . LEU A 1 562  ? 163.986 196.547 276.410 1.00 83.96  ? 545  LEU B N   1 
ATOM   4195  C CA  . LEU A 1 562  ? 164.369 196.799 275.029 1.00 83.96  ? 545  LEU B CA  1 
ATOM   4196  C C   . LEU A 1 562  ? 163.327 196.201 274.090 1.00 83.96  ? 545  LEU B C   1 
ATOM   4197  O O   . LEU A 1 562  ? 162.316 195.646 274.520 1.00 83.96  ? 545  LEU B O   1 
ATOM   4198  C CB  . LEU A 1 562  ? 165.758 196.225 274.741 1.00 83.96  ? 545  LEU B CB  1 
ATOM   4199  C CG  . LEU A 1 562  ? 166.724 196.274 275.921 1.00 83.96  ? 545  LEU B CG  1 
ATOM   4200  C CD1 . LEU A 1 562  ? 167.968 195.471 275.618 1.00 83.96  ? 545  LEU B CD1 1 
ATOM   4201  C CD2 . LEU A 1 562  ? 167.081 197.711 276.250 1.00 83.96  ? 545  LEU B CD2 1 
ATOM   4202  N N   . ASP A 1 563  ? 163.586 196.325 272.789 1.00 88.94  ? 546  ASP B N   1 
ATOM   4203  C CA  . ASP A 1 563  ? 162.674 195.838 271.766 1.00 88.94  ? 546  ASP B CA  1 
ATOM   4204  C C   . ASP A 1 563  ? 163.292 194.782 270.861 1.00 88.94  ? 546  ASP B C   1 
ATOM   4205  O O   . ASP A 1 563  ? 162.647 194.368 269.891 1.00 88.94  ? 546  ASP B O   1 
ATOM   4206  C CB  . ASP A 1 563  ? 162.166 197.004 270.906 1.00 88.94  ? 546  ASP B CB  1 
ATOM   4207  C CG  . ASP A 1 563  ? 161.852 198.243 271.725 1.00 88.94  ? 546  ASP B CG  1 
ATOM   4208  O OD1 . ASP A 1 563  ? 161.411 198.101 272.884 1.00 88.94  ? 546  ASP B OD1 1 
ATOM   4209  O OD2 . ASP A 1 563  ? 162.049 199.363 271.207 1.00 88.94  ? 546  ASP B OD2 1 
ATOM   4210  N N   . LYS A 1 564  ? 164.513 194.336 271.142 1.00 85.24  ? 547  LYS B N   1 
ATOM   4211  C CA  . LYS A 1 564  ? 165.200 193.376 270.293 1.00 85.24  ? 547  LYS B CA  1 
ATOM   4212  C C   . LYS A 1 564  ? 166.008 192.428 271.162 1.00 85.24  ? 547  LYS B C   1 
ATOM   4213  O O   . LYS A 1 564  ? 166.246 192.687 272.343 1.00 85.24  ? 547  LYS B O   1 
ATOM   4214  C CB  . LYS A 1 564  ? 166.115 194.076 269.281 1.00 85.24  ? 547  LYS B CB  1 
ATOM   4215  C CG  . LYS A 1 564  ? 167.484 194.429 269.835 1.00 85.24  ? 547  LYS B CG  1 
ATOM   4216  C CD  . LYS A 1 564  ? 168.005 195.725 269.240 1.00 85.24  ? 547  LYS B CD  1 
ATOM   4217  C CE  . LYS A 1 564  ? 169.272 196.181 269.942 1.00 85.24  ? 547  LYS B CE  1 
ATOM   4218  N NZ  . LYS A 1 564  ? 170.383 195.207 269.764 1.00 85.24  ? 547  LYS B NZ  1 
ATOM   4219  N N   . TYR A 1 565  ? 166.430 191.317 270.562 1.00 79.04  ? 548  TYR B N   1 
ATOM   4220  C CA  . TYR A 1 565  ? 167.260 190.333 271.248 1.00 79.04  ? 548  TYR B CA  1 
ATOM   4221  C C   . TYR A 1 565  ? 168.721 190.712 271.057 1.00 79.04  ? 548  TYR B C   1 
ATOM   4222  O O   . TYR A 1 565  ? 169.268 190.580 269.958 1.00 79.04  ? 548  TYR B O   1 
ATOM   4223  C CB  . TYR A 1 565  ? 166.985 188.928 270.723 1.00 79.04  ? 548  TYR B CB  1 
ATOM   4224  C CG  . TYR A 1 565  ? 165.810 188.260 271.388 1.00 79.04  ? 548  TYR B CG  1 
ATOM   4225  C CD1 . TYR A 1 565  ? 164.892 188.998 272.117 1.00 79.04  ? 548  TYR B CD1 1 
ATOM   4226  C CD2 . TYR A 1 565  ? 165.619 186.892 271.292 1.00 79.04  ? 548  TYR B CD2 1 
ATOM   4227  C CE1 . TYR A 1 565  ? 163.816 188.395 272.727 1.00 79.04  ? 548  TYR B CE1 1 
ATOM   4228  C CE2 . TYR A 1 565  ? 164.547 186.280 271.901 1.00 79.04  ? 548  TYR B CE2 1 
ATOM   4229  C CZ  . TYR A 1 565  ? 163.648 187.036 272.617 1.00 79.04  ? 548  TYR B CZ  1 
ATOM   4230  O OH  . TYR A 1 565  ? 162.574 186.434 273.228 1.00 79.04  ? 548  TYR B OH  1 
ATOM   4231  N N   . THR A 1 566  ? 169.353 191.177 272.129 1.00 78.19  ? 549  THR B N   1 
ATOM   4232  C CA  . THR A 1 566  ? 170.728 191.638 272.065 1.00 78.19  ? 549  THR B CA  1 
ATOM   4233  C C   . THR A 1 566  ? 171.692 190.458 272.004 1.00 78.19  ? 549  THR B C   1 
ATOM   4234  O O   . THR A 1 566  ? 171.310 189.292 272.129 1.00 78.19  ? 549  THR B O   1 
ATOM   4235  C CB  . THR A 1 566  ? 171.049 192.521 273.265 1.00 78.19  ? 549  THR B CB  1 
ATOM   4236  O OG1 . THR A 1 566  ? 171.035 191.729 274.458 1.00 78.19  ? 549  THR B OG1 1 
ATOM   4237  C CG2 . THR A 1 566  ? 170.021 193.619 273.387 1.00 78.19  ? 549  THR B CG2 1 
ATOM   4238  N N   . MET A 1 567  ? 172.969 190.780 271.803 1.00 76.89  ? 550  MET B N   1 
ATOM   4239  C CA  . MET A 1 567  ? 173.987 189.743 271.692 1.00 76.89  ? 550  MET B CA  1 
ATOM   4240  C C   . MET A 1 567  ? 174.196 189.012 273.014 1.00 76.89  ? 550  MET B C   1 
ATOM   4241  O O   . MET A 1 567  ? 174.500 187.812 273.016 1.00 76.89  ? 550  MET B O   1 
ATOM   4242  C CB  . MET A 1 567  ? 175.281 190.367 271.170 1.00 76.89  ? 550  MET B CB  1 
ATOM   4243  C CG  . MET A 1 567  ? 176.378 190.575 272.187 1.00 76.89  ? 550  MET B CG  1 
ATOM   4244  S SD  . MET A 1 567  ? 177.879 191.135 271.367 1.00 76.89  ? 550  MET B SD  1 
ATOM   4245  C CE  . MET A 1 567  ? 177.225 192.453 270.348 1.00 76.89  ? 550  MET B CE  1 
ATOM   4246  N N   . PHE A 1 568  ? 174.015 189.701 274.144 1.00 71.86  ? 551  PHE B N   1 
ATOM   4247  C CA  . PHE A 1 568  ? 174.074 189.019 275.432 1.00 71.86  ? 551  PHE B CA  1 
ATOM   4248  C C   . PHE A 1 568  ? 172.950 188.001 275.563 1.00 71.86  ? 551  PHE B C   1 
ATOM   4249  O O   . PHE A 1 568  ? 173.131 186.943 276.176 1.00 71.86  ? 551  PHE B O   1 
ATOM   4250  C CB  . PHE A 1 568  ? 174.013 190.031 276.574 1.00 71.86  ? 551  PHE B CB  1 
ATOM   4251  C CG  . PHE A 1 568  ? 174.794 191.288 276.320 1.00 71.86  ? 551  PHE B CG  1 
ATOM   4252  C CD1 . PHE A 1 568  ? 176.175 191.267 276.298 1.00 71.86  ? 551  PHE B CD1 1 
ATOM   4253  C CD2 . PHE A 1 568  ? 174.145 192.492 276.117 1.00 71.86  ? 551  PHE B CD2 1 
ATOM   4254  C CE1 . PHE A 1 568  ? 176.893 192.421 276.069 1.00 71.86  ? 551  PHE B CE1 1 
ATOM   4255  C CE2 . PHE A 1 568  ? 174.860 193.648 275.887 1.00 71.86  ? 551  PHE B CE2 1 
ATOM   4256  C CZ  . PHE A 1 568  ? 176.234 193.612 275.864 1.00 71.86  ? 551  PHE B CZ  1 
ATOM   4257  N N   . HIS A 1 569  ? 171.782 188.303 274.994 1.00 74.17  ? 552  HIS B N   1 
ATOM   4258  C CA  . HIS A 1 569  ? 170.679 187.350 275.010 1.00 74.17  ? 552  HIS B CA  1 
ATOM   4259  C C   . HIS A 1 569  ? 171.042 186.080 274.255 1.00 74.17  ? 552  HIS B C   1 
ATOM   4260  O O   . HIS A 1 569  ? 170.771 184.969 274.724 1.00 74.17  ? 552  HIS B O   1 
ATOM   4261  C CB  . HIS A 1 569  ? 169.432 187.993 274.409 1.00 74.17  ? 552  HIS B CB  1 
ATOM   4262  C CG  . HIS A 1 569  ? 168.632 188.792 275.388 1.00 74.17  ? 552  HIS B CG  1 
ATOM   4263  N ND1 . HIS A 1 569  ? 168.184 190.065 275.115 1.00 74.17  ? 552  HIS B ND1 1 
ATOM   4264  C CD2 . HIS A 1 569  ? 168.187 188.494 276.630 1.00 74.17  ? 552  HIS B CD2 1 
ATOM   4265  C CE1 . HIS A 1 569  ? 167.507 190.523 276.152 1.00 74.17  ? 552  HIS B CE1 1 
ATOM   4266  N NE2 . HIS A 1 569  ? 167.493 189.588 277.084 1.00 74.17  ? 552  HIS B NE2 1 
ATOM   4267  N N   . TYR A 1 570  ? 171.665 186.224 273.083 1.00 74.99  ? 553  TYR B N   1 
ATOM   4268  C CA  . TYR A 1 570  ? 172.083 185.051 272.323 1.00 74.99  ? 553  TYR B CA  1 
ATOM   4269  C C   . TYR A 1 570  ? 173.164 184.269 273.057 1.00 74.99  ? 553  TYR B C   1 
ATOM   4270  O O   . TYR A 1 570  ? 173.153 183.034 273.054 1.00 74.99  ? 553  TYR B O   1 
ATOM   4271  C CB  . TYR A 1 570  ? 172.567 185.466 270.937 1.00 74.99  ? 553  TYR B CB  1 
ATOM   4272  C CG  . TYR A 1 570  ? 171.459 185.603 269.921 1.00 74.99  ? 553  TYR B CG  1 
ATOM   4273  C CD1 . TYR A 1 570  ? 170.375 186.433 270.156 1.00 74.99  ? 553  TYR B CD1 1 
ATOM   4274  C CD2 . TYR A 1 570  ? 171.496 184.897 268.729 1.00 74.99  ? 553  TYR B CD2 1 
ATOM   4275  C CE1 . TYR A 1 570  ? 169.361 186.559 269.232 1.00 74.99  ? 553  TYR B CE1 1 
ATOM   4276  C CE2 . TYR A 1 570  ? 170.487 185.016 267.799 1.00 74.99  ? 553  TYR B CE2 1 
ATOM   4277  C CZ  . TYR A 1 570  ? 169.422 185.849 268.055 1.00 74.99  ? 553  TYR B CZ  1 
ATOM   4278  O OH  . TYR A 1 570  ? 168.413 185.972 267.129 1.00 74.99  ? 553  TYR B OH  1 
ATOM   4279  N N   . LEU A 1 571  ? 174.114 184.968 273.687 1.00 69.60  ? 554  LEU B N   1 
ATOM   4280  C CA  . LEU A 1 571  ? 175.152 184.270 274.442 1.00 69.60  ? 554  LEU B CA  1 
ATOM   4281  C C   . LEU A 1 571  ? 174.568 183.489 275.612 1.00 69.60  ? 554  LEU B C   1 
ATOM   4282  O O   . LEU A 1 571  ? 174.970 182.349 275.866 1.00 69.60  ? 554  LEU B O   1 
ATOM   4283  C CB  . LEU A 1 571  ? 176.214 185.250 274.938 1.00 69.60  ? 554  LEU B CB  1 
ATOM   4284  C CG  . LEU A 1 571  ? 177.401 185.547 274.023 1.00 69.60  ? 554  LEU B CG  1 
ATOM   4285  C CD1 . LEU A 1 571  ? 178.375 184.388 274.077 1.00 69.60  ? 554  LEU B CD1 1 
ATOM   4286  C CD2 . LEU A 1 571  ? 176.964 185.794 272.600 1.00 69.60  ? 554  LEU B CD2 1 
ATOM   4287  N N   . ARG A 1 572  ? 173.625 184.082 276.340 1.00 69.60  ? 555  ARG B N   1 
ATOM   4288  C CA  . ARG A 1 572  ? 173.009 183.376 277.454 1.00 69.60  ? 555  ARG B CA  1 
ATOM   4289  C C   . ARG A 1 572  ? 171.963 182.370 277.005 1.00 69.60  ? 555  ARG B C   1 
ATOM   4290  O O   . ARG A 1 572  ? 171.468 181.605 277.838 1.00 69.60  ? 555  ARG B O   1 
ATOM   4291  C CB  . ARG A 1 572  ? 172.377 184.366 278.432 1.00 69.60  ? 555  ARG B CB  1 
ATOM   4292  C CG  . ARG A 1 572  ? 173.339 184.900 279.480 1.00 69.60  ? 555  ARG B CG  1 
ATOM   4293  C CD  . ARG A 1 572  ? 173.569 183.893 280.587 1.00 69.60  ? 555  ARG B CD  1 
ATOM   4294  N NE  . ARG A 1 572  ? 172.387 183.698 281.417 1.00 69.60  ? 555  ARG B NE  1 
ATOM   4295  C CZ  . ARG A 1 572  ? 171.524 182.703 281.266 1.00 69.60  ? 555  ARG B CZ  1 
ATOM   4296  N NH1 . ARG A 1 572  ? 171.667 181.802 280.310 1.00 69.60  ? 555  ARG B NH1 1 
ATOM   4297  N NH2 . ARG A 1 572  ? 170.489 182.610 282.097 1.00 69.60  ? 555  ARG B NH2 1 
ATOM   4298  N N   . ALA A 1 573  ? 171.602 182.363 275.721 1.00 69.60  ? 556  ALA B N   1 
ATOM   4299  C CA  . ALA A 1 573  ? 170.708 181.335 275.206 1.00 69.60  ? 556  ALA B CA  1 
ATOM   4300  C C   . ALA A 1 573  ? 171.416 180.001 275.020 1.00 69.60  ? 556  ALA B C   1 
ATOM   4301  O O   . ALA A 1 573  ? 170.769 178.951 275.085 1.00 69.60  ? 556  ALA B O   1 
ATOM   4302  C CB  . ALA A 1 573  ? 170.094 181.785 273.882 1.00 69.60  ? 556  ALA B CB  1 
ATOM   4303  N N   . GLN A 1 574  ? 172.726 180.018 274.793 1.00 69.60  ? 557  GLN B N   1 
ATOM   4304  C CA  . GLN A 1 574  ? 173.486 178.817 274.471 1.00 69.60  ? 557  GLN B CA  1 
ATOM   4305  C C   . GLN A 1 574  ? 173.994 178.073 275.697 1.00 69.60  ? 557  GLN B C   1 
ATOM   4306  O O   . GLN A 1 574  ? 174.607 177.012 275.545 1.00 69.60  ? 557  GLN B O   1 
ATOM   4307  C CB  . GLN A 1 574  ? 174.670 179.176 273.570 1.00 69.60  ? 557  GLN B CB  1 
ATOM   4308  C CG  . GLN A 1 574  ? 174.291 179.435 272.129 1.00 69.60  ? 557  GLN B CG  1 
ATOM   4309  C CD  . GLN A 1 574  ? 175.324 180.263 271.399 1.00 69.60  ? 557  GLN B CD  1 
ATOM   4310  O OE1 . GLN A 1 574  ? 176.519 179.995 271.483 1.00 69.60  ? 557  GLN B OE1 1 
ATOM   4311  N NE2 . GLN A 1 574  ? 174.866 181.274 270.674 1.00 69.60  ? 557  GLN B NE2 1 
ATOM   4312  N N   . GLU A 1 575  ? 173.762 178.589 276.897 1.00 70.40  ? 558  GLU B N   1 
ATOM   4313  C CA  . GLU A 1 575  ? 174.287 177.974 278.105 1.00 70.40  ? 558  GLU B CA  1 
ATOM   4314  C C   . GLU A 1 575  ? 173.342 176.897 278.628 1.00 70.40  ? 558  GLU B C   1 
ATOM   4315  O O   . GLU A 1 575  ? 172.169 176.825 278.256 1.00 70.40  ? 558  GLU B O   1 
ATOM   4316  C CB  . GLU A 1 575  ? 174.525 179.029 279.184 1.00 70.40  ? 558  GLU B CB  1 
ATOM   4317  C CG  . GLU A 1 575  ? 175.686 179.956 278.889 1.00 70.40  ? 558  GLU B CG  1 
ATOM   4318  C CD  . GLU A 1 575  ? 176.434 180.364 280.139 1.00 70.40  ? 558  GLU B CD  1 
ATOM   4319  O OE1 . GLU A 1 575  ? 175.919 180.113 281.248 1.00 70.40  ? 558  GLU B OE1 1 
ATOM   4320  O OE2 . GLU A 1 575  ? 177.539 180.933 280.014 1.00 70.40  ? 558  GLU B OE2 1 
ATOM   4321  N N   . PHE A 1 576  ? 173.876 176.053 279.506 1.00 76.11  ? 559  PHE B N   1 
ATOM   4322  C CA  . PHE A 1 576  ? 173.105 174.978 280.117 1.00 76.11  ? 559  PHE B CA  1 
ATOM   4323  C C   . PHE A 1 576  ? 173.771 174.585 281.428 1.00 76.11  ? 559  PHE B C   1 
ATOM   4324  O O   . PHE A 1 576  ? 174.847 175.077 281.776 1.00 76.11  ? 559  PHE B O   1 
ATOM   4325  C CB  . PHE A 1 576  ? 172.962 173.782 279.172 1.00 76.11  ? 559  PHE B CB  1 
ATOM   4326  C CG  . PHE A 1 576  ? 174.206 172.957 279.034 1.00 76.11  ? 559  PHE B CG  1 
ATOM   4327  C CD1 . PHE A 1 576  ? 175.399 173.534 278.641 1.00 76.11  ? 559  PHE B CD1 1 
ATOM   4328  C CD2 . PHE A 1 576  ? 174.175 171.598 279.275 1.00 76.11  ? 559  PHE B CD2 1 
ATOM   4329  C CE1 . PHE A 1 576  ? 176.538 172.776 278.506 1.00 76.11  ? 559  PHE B CE1 1 
ATOM   4330  C CE2 . PHE A 1 576  ? 175.313 170.834 279.140 1.00 76.11  ? 559  PHE B CE2 1 
ATOM   4331  C CZ  . PHE A 1 576  ? 176.496 171.424 278.756 1.00 76.11  ? 559  PHE B CZ  1 
ATOM   4332  N N   . GLU A 1 577  ? 173.110 173.683 282.154 1.00 81.10  ? 560  GLU B N   1 
ATOM   4333  C CA  . GLU A 1 577  ? 173.430 173.403 283.548 1.00 81.10  ? 560  GLU B CA  1 
ATOM   4334  C C   . GLU A 1 577  ? 174.130 172.067 283.757 1.00 81.10  ? 560  GLU B C   1 
ATOM   4335  O O   . GLU A 1 577  ? 174.344 171.672 284.908 1.00 81.10  ? 560  GLU B O   1 
ATOM   4336  C CB  . GLU A 1 577  ? 172.150 173.446 284.385 1.00 81.10  ? 560  GLU B CB  1 
ATOM   4337  C CG  . GLU A 1 577  ? 171.264 172.205 284.249 1.00 81.10  ? 560  GLU B CG  1 
ATOM   4338  C CD  . GLU A 1 577  ? 170.478 172.152 282.942 1.00 81.10  ? 560  GLU B CD  1 
ATOM   4339  O OE1 . GLU A 1 577  ? 170.840 172.860 281.980 1.00 81.10  ? 560  GLU B OE1 1 
ATOM   4340  O OE2 . GLU A 1 577  ? 169.489 171.392 282.880 1.00 81.10  ? 560  GLU B OE2 1 
ATOM   4341  N N   . HIS A 1 578  ? 174.499 171.367 282.682 1.00 82.56  ? 561  HIS B N   1 
ATOM   4342  C CA  . HIS A 1 578  ? 175.068 170.021 282.778 1.00 82.56  ? 561  HIS B CA  1 
ATOM   4343  C C   . HIS A 1 578  ? 174.141 169.091 283.557 1.00 82.56  ? 561  HIS B C   1 
ATOM   4344  O O   . HIS A 1 578  ? 174.579 168.302 284.396 1.00 82.56  ? 561  HIS B O   1 
ATOM   4345  C CB  . HIS A 1 578  ? 176.463 170.048 283.406 1.00 82.56  ? 561  HIS B CB  1 
ATOM   4346  C CG  . HIS A 1 578  ? 177.568 169.811 282.427 1.00 82.56  ? 561  HIS B CG  1 
ATOM   4347  N ND1 . HIS A 1 578  ? 177.709 168.627 281.737 1.00 82.56  ? 561  HIS B ND1 1 
ATOM   4348  C CD2 . HIS A 1 578  ? 178.584 170.608 282.020 1.00 82.56  ? 561  HIS B CD2 1 
ATOM   4349  C CE1 . HIS A 1 578  ? 178.765 168.704 280.947 1.00 82.56  ? 561  HIS B CE1 1 
ATOM   4350  N NE2 . HIS A 1 578  ? 179.313 169.896 281.100 1.00 82.56  ? 561  HIS B NE2 1 
ATOM   4351  N N   . GLY A 1 579  ? 172.847 169.184 283.272 1.00 81.18  ? 562  GLY B N   1 
ATOM   4352  C CA  . GLY A 1 579  ? 171.858 168.459 284.038 1.00 81.18  ? 562  GLY B CA  1 
ATOM   4353  C C   . GLY A 1 579  ? 171.824 166.981 283.707 1.00 81.18  ? 562  GLY B C   1 
ATOM   4354  O O   . GLY A 1 579  ? 172.520 166.480 282.824 1.00 81.18  ? 562  GLY B O   1 
ATOM   4355  N N   . LYS A 1 580  ? 170.981 166.268 284.455 1.00 82.34  ? 563  LYS B N   1 
ATOM   4356  C CA  . LYS A 1 580  ? 170.866 164.825 284.272 1.00 82.34  ? 563  LYS B CA  1 
ATOM   4357  C C   . LYS A 1 580  ? 170.087 164.484 283.006 1.00 82.34  ? 563  LYS B C   1 
ATOM   4358  O O   . LYS A 1 580  ? 170.412 163.510 282.316 1.00 82.34  ? 563  LYS B O   1 
ATOM   4359  C CB  . LYS A 1 580  ? 170.206 164.196 285.499 1.00 82.34  ? 563  LYS B CB  1 
ATOM   4360  C CG  . LYS A 1 580  ? 169.976 162.701 285.380 1.00 82.34  ? 563  LYS B CG  1 
ATOM   4361  C CD  . LYS A 1 580  ? 171.293 161.952 285.292 1.00 82.34  ? 563  LYS B CD  1 
ATOM   4362  C CE  . LYS A 1 580  ? 171.241 160.873 284.226 1.00 82.34  ? 563  LYS B CE  1 
ATOM   4363  N NZ  . LYS A 1 580  ? 171.462 161.441 282.869 1.00 82.34  ? 563  LYS B NZ  1 
ATOM   4364  N N   . SER A 1 581  ? 169.060 165.266 282.685 1.00 74.84  ? 564  SER B N   1 
ATOM   4365  C CA  . SER A 1 581  ? 168.233 164.970 281.527 1.00 74.84  ? 564  SER B CA  1 
ATOM   4366  C C   . SER A 1 581  ? 168.965 165.309 280.231 1.00 74.84  ? 564  SER B C   1 
ATOM   4367  O O   . SER A 1 581  ? 169.953 166.048 280.216 1.00 74.84  ? 564  SER B O   1 
ATOM   4368  C CB  . SER A 1 581  ? 166.916 165.741 281.594 1.00 74.84  ? 564  SER B CB  1 
ATOM   4369  O OG  . SER A 1 581  ? 166.254 165.715 280.342 1.00 74.84  ? 564  SER B OG  1 
ATOM   4370  N N   . ARG A 1 582  ? 168.459 164.754 279.132 1.00 72.51  ? 565  ARG B N   1 
ATOM   4371  C CA  . ARG A 1 582  ? 169.073 164.963 277.828 1.00 72.51  ? 565  ARG B CA  1 
ATOM   4372  C C   . ARG A 1 582  ? 168.974 166.423 277.412 1.00 72.51  ? 565  ARG B C   1 
ATOM   4373  O O   . ARG A 1 582  ? 167.987 167.104 277.699 1.00 72.51  ? 565  ARG B O   1 
ATOM   4374  C CB  . ARG A 1 582  ? 168.405 164.082 276.774 1.00 72.51  ? 565  ARG B CB  1 
ATOM   4375  C CG  . ARG A 1 582  ? 169.198 163.944 275.477 1.00 72.51  ? 565  ARG B CG  1 
ATOM   4376  C CD  . ARG A 1 582  ? 168.761 162.715 274.689 1.00 72.51  ? 565  ARG B CD  1 
ATOM   4377  N NE  . ARG A 1 582  ? 169.867 162.074 273.988 1.00 72.51  ? 565  ARG B NE  1 
ATOM   4378  C CZ  . ARG A 1 582  ? 170.445 162.555 272.897 1.00 72.51  ? 565  ARG B CZ  1 
ATOM   4379  N NH1 . ARG A 1 582  ? 170.033 163.678 272.334 1.00 72.51  ? 565  ARG B NH1 1 
ATOM   4380  N NH2 . ARG A 1 582  ? 171.457 161.888 272.351 1.00 72.51  ? 565  ARG B NH2 1 
ATOM   4381  N N   . ILE A 1 583  ? 170.007 166.900 276.728 1.00 69.60  ? 566  ILE B N   1 
ATOM   4382  C CA  . ILE A 1 583  ? 170.065 168.262 276.219 1.00 69.60  ? 566  ILE B CA  1 
ATOM   4383  C C   . ILE A 1 583  ? 170.003 168.199 274.703 1.00 69.60  ? 566  ILE B C   1 
ATOM   4384  O O   . ILE A 1 583  ? 170.816 167.518 274.071 1.00 69.60  ? 566  ILE B O   1 
ATOM   4385  C CB  . ILE A 1 583  ? 171.337 168.985 276.693 1.00 69.60  ? 566  ILE B CB  1 
ATOM   4386  C CG1 . ILE A 1 583  ? 171.336 169.125 278.214 1.00 69.60  ? 566  ILE B CG1 1 
ATOM   4387  C CG2 . ILE A 1 583  ? 171.444 170.343 276.049 1.00 69.60  ? 566  ILE B CG2 1 
ATOM   4388  C CD1 . ILE A 1 583  ? 172.108 168.041 278.932 1.00 69.60  ? 566  ILE B CD1 1 
ATOM   4389  N N   . ALA A 1 584  ? 169.041 168.901 274.119 1.00 69.60  ? 567  ALA B N   1 
ATOM   4390  C CA  . ALA A 1 584  ? 168.850 168.914 272.679 1.00 69.60  ? 567  ALA B CA  1 
ATOM   4391  C C   . ALA A 1 584  ? 169.159 170.295 272.120 1.00 69.60  ? 567  ALA B C   1 
ATOM   4392  O O   . ALA A 1 584  ? 168.810 171.319 272.720 1.00 69.60  ? 567  ALA B O   1 
ATOM   4393  C CB  . ALA A 1 584  ? 167.422 168.511 272.310 1.00 69.60  ? 567  ALA B CB  1 
ATOM   4394  N N   . LEU A 1 585  ? 169.837 170.317 270.980 1.00 69.60  ? 568  LEU B N   1 
ATOM   4395  C CA  . LEU A 1 585  ? 170.078 171.569 270.293 1.00 69.60  ? 568  LEU B CA  1 
ATOM   4396  C C   . LEU A 1 585  ? 168.797 172.046 269.621 1.00 69.60  ? 568  LEU B C   1 
ATOM   4397  O O   . LEU A 1 585  ? 167.877 171.272 269.351 1.00 69.60  ? 568  LEU B O   1 
ATOM   4398  C CB  . LEU A 1 585  ? 171.193 171.408 269.261 1.00 69.60  ? 568  LEU B CB  1 
ATOM   4399  C CG  . LEU A 1 585  ? 172.607 171.830 269.659 1.00 69.60  ? 568  LEU B CG  1 
ATOM   4400  C CD1 . LEU A 1 585  ? 173.029 171.162 270.940 1.00 69.60  ? 568  LEU B CD1 1 
ATOM   4401  C CD2 . LEU A 1 585  ? 173.584 171.496 268.549 1.00 69.60  ? 568  LEU B CD2 1 
ATOM   4402  N N   . THR A 1 586  ? 168.738 173.349 269.368 1.00 69.60  ? 569  THR B N   1 
ATOM   4403  C CA  . THR A 1 586  ? 167.592 173.951 268.703 1.00 69.60  ? 569  THR B CA  1 
ATOM   4404  C C   . THR A 1 586  ? 168.058 175.229 268.027 1.00 69.60  ? 569  THR B C   1 
ATOM   4405  O O   . THR A 1 586  ? 169.151 175.728 268.299 1.00 69.60  ? 569  THR B O   1 
ATOM   4406  C CB  . THR A 1 586  ? 166.452 174.235 269.684 1.00 69.60  ? 569  THR B CB  1 
ATOM   4407  O OG1 . THR A 1 586  ? 165.222 174.357 268.965 1.00 69.60  ? 569  THR B OG1 1 
ATOM   4408  C CG2 . THR A 1 586  ? 166.711 175.517 270.445 1.00 69.60  ? 569  THR B CG2 1 
ATOM   4409  N N   . ASN A 1 587  ? 167.224 175.744 267.127 1.00 69.60  ? 570  ASN B N   1 
ATOM   4410  C CA  . ASN A 1 587  ? 167.559 176.938 266.364 1.00 69.60  ? 570  ASN B CA  1 
ATOM   4411  C C   . ASN A 1 587  ? 166.675 178.129 266.705 1.00 69.60  ? 570  ASN B C   1 
ATOM   4412  O O   . ASN A 1 587  ? 166.747 179.155 266.022 1.00 69.60  ? 570  ASN B O   1 
ATOM   4413  C CB  . ASN A 1 587  ? 167.482 176.645 264.866 1.00 69.60  ? 570  ASN B CB  1 
ATOM   4414  C CG  . ASN A 1 587  ? 168.564 175.695 264.404 1.00 69.60  ? 570  ASN B CG  1 
ATOM   4415  O OD1 . ASN A 1 587  ? 168.337 174.850 263.539 1.00 69.60  ? 570  ASN B OD1 1 
ATOM   4416  N ND2 . ASN A 1 587  ? 169.751 175.825 264.981 1.00 69.60  ? 570  ASN B ND2 1 
ATOM   4417  N N   . SER A 1 588  ? 165.848 178.026 267.741 1.00 69.60  ? 571  SER B N   1 
ATOM   4418  C CA  . SER A 1 588  ? 164.916 179.084 268.120 1.00 69.60  ? 571  SER B CA  1 
ATOM   4419  C C   . SER A 1 588  ? 165.288 179.592 269.505 1.00 69.60  ? 571  SER B C   1 
ATOM   4420  O O   . SER A 1 588  ? 165.098 178.887 270.501 1.00 69.60  ? 571  SER B O   1 
ATOM   4421  C CB  . SER A 1 588  ? 163.477 178.574 268.093 1.00 69.60  ? 571  SER B CB  1 
ATOM   4422  O OG  . SER A 1 588  ? 162.634 179.380 268.895 1.00 69.60  ? 571  SER B OG  1 
ATOM   4423  N N   . VAL A 1 589  ? 165.806 180.821 269.571 1.00 69.60  ? 572  VAL B N   1 
ATOM   4424  C CA  . VAL A 1 589  ? 166.183 181.390 270.859 1.00 69.60  ? 572  VAL B CA  1 
ATOM   4425  C C   . VAL A 1 589  ? 164.962 181.588 271.745 1.00 69.60  ? 572  VAL B C   1 
ATOM   4426  O O   . VAL A 1 589  ? 165.047 181.433 272.968 1.00 69.60  ? 572  VAL B O   1 
ATOM   4427  C CB  . VAL A 1 589  ? 166.958 182.706 270.667 1.00 69.60  ? 572  VAL B CB  1 
ATOM   4428  C CG1 . VAL A 1 589  ? 168.331 182.427 270.101 1.00 69.60  ? 572  VAL B CG1 1 
ATOM   4429  C CG2 . VAL A 1 589  ? 166.196 183.638 269.750 1.00 69.60  ? 572  VAL B CG2 1 
ATOM   4430  N N   . ASN A 1 590  ? 163.811 181.924 271.154 1.00 73.36  ? 573  ASN B N   1 
ATOM   4431  C CA  . ASN A 1 590  ? 162.602 182.144 271.944 1.00 73.36  ? 573  ASN B CA  1 
ATOM   4432  C C   . ASN A 1 590  ? 162.236 180.919 272.767 1.00 73.36  ? 573  ASN B C   1 
ATOM   4433  O O   . ASN A 1 590  ? 161.558 181.042 273.793 1.00 73.36  ? 573  ASN B O   1 
ATOM   4434  C CB  . ASN A 1 590  ? 161.436 182.529 271.034 1.00 73.36  ? 573  ASN B CB  1 
ATOM   4435  C CG  . ASN A 1 590  ? 161.748 183.723 270.155 1.00 73.36  ? 573  ASN B CG  1 
ATOM   4436  O OD1 . ASN A 1 590  ? 162.275 184.730 270.621 1.00 73.36  ? 573  ASN B OD1 1 
ATOM   4437  N ND2 . ASN A 1 590  ? 161.418 183.616 268.874 1.00 73.36  ? 573  ASN B ND2 1 
ATOM   4438  N N   . GLU A 1 591  ? 162.661 179.732 272.334 1.00 71.35  ? 574  GLU B N   1 
ATOM   4439  C CA  . GLU A 1 591  ? 162.454 178.518 273.108 1.00 71.35  ? 574  GLU B CA  1 
ATOM   4440  C C   . GLU A 1 591  ? 163.683 178.093 273.897 1.00 71.35  ? 574  GLU B C   1 
ATOM   4441  O O   . GLU A 1 591  ? 163.541 177.376 274.892 1.00 71.35  ? 574  GLU B O   1 
ATOM   4442  C CB  . GLU A 1 591  ? 162.029 177.366 272.191 1.00 71.35  ? 574  GLU B CB  1 
ATOM   4443  C CG  . GLU A 1 591  ? 161.302 176.203 272.879 1.00 71.35  ? 574  GLU B CG  1 
ATOM   4444  C CD  . GLU A 1 591  ? 160.358 176.629 273.998 1.00 71.35  ? 574  GLU B CD  1 
ATOM   4445  O OE1 . GLU A 1 591  ? 159.130 176.587 273.778 1.00 71.35  ? 574  GLU B OE1 1 
ATOM   4446  O OE2 . GLU A 1 591  ? 160.826 176.956 275.110 1.00 71.35  ? 574  GLU B OE2 1 
ATOM   4447  N N   . ALA A 1 592  ? 164.879 178.512 273.482 1.00 69.60  ? 575  ALA B N   1 
ATOM   4448  C CA  . ALA A 1 592  ? 166.086 178.111 274.197 1.00 69.60  ? 575  ALA B CA  1 
ATOM   4449  C C   . ALA A 1 592  ? 166.183 178.805 275.549 1.00 69.60  ? 575  ALA B C   1 
ATOM   4450  O O   . ALA A 1 592  ? 166.532 178.176 276.554 1.00 69.60  ? 575  ALA B O   1 
ATOM   4451  C CB  . ALA A 1 592  ? 167.321 178.404 273.349 1.00 69.60  ? 575  ALA B CB  1 
ATOM   4452  N N   . LEU A 1 593  ? 165.886 180.105 275.596 1.00 69.75  ? 576  LEU B N   1 
ATOM   4453  C CA  . LEU A 1 593  ? 165.868 180.797 276.879 1.00 69.75  ? 576  LEU B CA  1 
ATOM   4454  C C   . LEU A 1 593  ? 164.746 180.289 277.773 1.00 69.75  ? 576  LEU B C   1 
ATOM   4455  O O   . LEU A 1 593  ? 164.918 180.207 278.994 1.00 69.75  ? 576  LEU B O   1 
ATOM   4456  C CB  . LEU A 1 593  ? 165.728 182.306 276.680 1.00 69.75  ? 576  LEU B CB  1 
ATOM   4457  C CG  . LEU A 1 593  ? 166.861 183.070 275.996 1.00 69.75  ? 576  LEU B CG  1 
ATOM   4458  C CD1 . LEU A 1 593  ? 166.371 183.744 274.731 1.00 69.75  ? 576  LEU B CD1 1 
ATOM   4459  C CD2 . LEU A 1 593  ? 167.453 184.093 276.947 1.00 69.75  ? 576  LEU B CD2 1 
ATOM   4460  N N   . LEU A 1 594  ? 163.597 179.949 277.188 1.00 72.22  ? 577  LEU B N   1 
ATOM   4461  C CA  . LEU A 1 594  ? 162.455 179.527 277.992 1.00 72.22  ? 577  LEU B CA  1 
ATOM   4462  C C   . LEU A 1 594  ? 162.669 178.142 278.587 1.00 72.22  ? 577  LEU B C   1 
ATOM   4463  O O   . LEU A 1 594  ? 162.363 177.913 279.763 1.00 72.22  ? 577  LEU B O   1 
ATOM   4464  C CB  . LEU A 1 594  ? 161.184 179.554 277.147 1.00 72.22  ? 577  LEU B CB  1 
ATOM   4465  C CG  . LEU A 1 594  ? 160.283 180.777 277.324 1.00 72.22  ? 577  LEU B CG  1 
ATOM   4466  C CD1 . LEU A 1 594  ? 159.491 180.668 278.616 1.00 72.22  ? 577  LEU B CD1 1 
ATOM   4467  C CD2 . LEU A 1 594  ? 161.093 182.063 277.295 1.00 72.22  ? 577  LEU B CD2 1 
ATOM   4468  N N   . ASN A 1 595  ? 163.191 177.205 277.797 1.00 71.17  ? 578  ASN B N   1 
ATOM   4469  C CA  . ASN A 1 595  ? 163.340 175.829 278.242 1.00 71.17  ? 578  ASN B CA  1 
ATOM   4470  C C   . ASN A 1 595  ? 164.763 175.592 278.715 1.00 71.17  ? 578  ASN B C   1 
ATOM   4471  O O   . ASN A 1 595  ? 165.701 175.745 277.918 1.00 71.17  ? 578  ASN B O   1 
ATOM   4472  C CB  . ASN A 1 595  ? 162.993 174.863 277.117 1.00 71.17  ? 578  ASN B CB  1 
ATOM   4473  C CG  . ASN A 1 595  ? 162.317 173.608 277.619 1.00 71.17  ? 578  ASN B CG  1 
ATOM   4474  O OD1 . ASN A 1 595  ? 162.432 173.256 278.792 1.00 71.17  ? 578  ASN B OD1 1 
ATOM   4475  N ND2 . ASN A 1 595  ? 161.608 172.923 276.732 1.00 71.17  ? 578  ASN B ND2 1 
ATOM   4476  N N   . PRO A 1 596  ? 164.977 175.239 279.984 1.00 69.60  ? 579  PRO B N   1 
ATOM   4477  C CA  . PRO A 1 596  ? 166.349 174.971 280.446 1.00 69.60  ? 579  PRO B CA  1 
ATOM   4478  C C   . PRO A 1 596  ? 167.025 173.810 279.735 1.00 69.60  ? 579  PRO B C   1 
ATOM   4479  O O   . PRO A 1 596  ? 168.246 173.845 279.546 1.00 69.60  ? 579  PRO B O   1 
ATOM   4480  C CB  . PRO A 1 596  ? 166.162 174.685 281.943 1.00 69.60  ? 579  PRO B CB  1 
ATOM   4481  C CG  . PRO A 1 596  ? 164.729 174.305 282.089 1.00 69.60  ? 579  PRO B CG  1 
ATOM   4482  C CD  . PRO A 1 596  ? 163.990 175.101 281.065 1.00 69.60  ? 579  PRO B CD  1 
ATOM   4483  N N   . SER A 1 597  ? 166.272 172.788 279.322 1.00 69.60  ? 580  SER B N   1 
ATOM   4484  C CA  . SER A 1 597  ? 166.843 171.567 278.762 1.00 69.60  ? 580  SER B CA  1 
ATOM   4485  C C   . SER A 1 597  ? 166.902 171.584 277.241 1.00 69.60  ? 580  SER B C   1 
ATOM   4486  O O   . SER A 1 597  ? 166.690 170.546 276.603 1.00 69.60  ? 580  SER B O   1 
ATOM   4487  C CB  . SER A 1 597  ? 166.058 170.348 279.245 1.00 69.60  ? 580  SER B CB  1 
ATOM   4488  O OG  . SER A 1 597  ? 164.682 170.475 278.938 1.00 69.60  ? 580  SER B OG  1 
ATOM   4489  N N   . ARG A 1 598  ? 167.164 172.741 276.642 1.00 69.60  ? 581  ARG B N   1 
ATOM   4490  C CA  . ARG A 1 598  ? 167.279 172.863 275.196 1.00 69.60  ? 581  ARG B CA  1 
ATOM   4491  C C   . ARG A 1 598  ? 168.146 174.076 274.906 1.00 69.60  ? 581  ARG B C   1 
ATOM   4492  O O   . ARG A 1 598  ? 167.852 175.173 275.391 1.00 69.60  ? 581  ARG B O   1 
ATOM   4493  C CB  . ARG A 1 598  ? 165.898 173.008 274.551 1.00 69.60  ? 581  ARG B CB  1 
ATOM   4494  C CG  . ARG A 1 598  ? 165.869 172.760 273.060 1.00 69.60  ? 581  ARG B CG  1 
ATOM   4495  C CD  . ARG A 1 598  ? 164.587 172.056 272.649 1.00 69.60  ? 581  ARG B CD  1 
ATOM   4496  N NE  . ARG A 1 598  ? 164.420 170.788 273.346 1.00 69.60  ? 581  ARG B NE  1 
ATOM   4497  C CZ  . ARG A 1 598  ? 163.363 170.472 274.081 1.00 69.60  ? 581  ARG B CZ  1 
ATOM   4498  N NH1 . ARG A 1 598  ? 162.350 171.309 274.230 1.00 69.60  ? 581  ARG B NH1 1 
ATOM   4499  N NH2 . ARG A 1 598  ? 163.321 169.287 274.682 1.00 69.60  ? 581  ARG B NH2 1 
ATOM   4500  N N   . VAL A 1 599  ? 169.206 173.887 274.124 1.00 69.60  ? 582  VAL B N   1 
ATOM   4501  C CA  . VAL A 1 599  ? 170.220 174.920 273.929 1.00 69.60  ? 582  VAL B CA  1 
ATOM   4502  C C   . VAL A 1 599  ? 170.181 175.403 272.487 1.00 69.60  ? 582  VAL B C   1 
ATOM   4503  O O   . VAL A 1 599  ? 170.126 174.592 271.557 1.00 69.60  ? 582  VAL B O   1 
ATOM   4504  C CB  . VAL A 1 599  ? 171.626 174.413 274.291 1.00 69.60  ? 582  VAL B CB  1 
ATOM   4505  C CG1 . VAL A 1 599  ? 171.807 174.407 275.789 1.00 69.60  ? 582  VAL B CG1 1 
ATOM   4506  C CG2 . VAL A 1 599  ? 171.844 173.036 273.736 1.00 69.60  ? 582  VAL B CG2 1 
ATOM   4507  N N   . TYR A 1 600  ? 170.206 176.719 272.304 1.00 69.60  ? 583  TYR B N   1 
ATOM   4508  C CA  . TYR A 1 600  ? 170.253 177.290 270.967 1.00 69.60  ? 583  TYR B CA  1 
ATOM   4509  C C   . TYR A 1 600  ? 171.585 176.978 270.297 1.00 69.60  ? 583  TYR B C   1 
ATOM   4510  O O   . TYR A 1 600  ? 172.621 176.850 270.953 1.00 69.60  ? 583  TYR B O   1 
ATOM   4511  C CB  . TYR A 1 600  ? 170.048 178.799 271.027 1.00 69.60  ? 583  TYR B CB  1 
ATOM   4512  C CG  . TYR A 1 600  ? 170.398 179.529 269.753 1.00 69.60  ? 583  TYR B CG  1 
ATOM   4513  C CD1 . TYR A 1 600  ? 169.570 179.468 268.647 1.00 69.60  ? 583  TYR B CD1 1 
ATOM   4514  C CD2 . TYR A 1 600  ? 171.555 180.283 269.660 1.00 69.60  ? 583  TYR B CD2 1 
ATOM   4515  C CE1 . TYR A 1 600  ? 169.882 180.138 267.485 1.00 69.60  ? 583  TYR B CE1 1 
ATOM   4516  C CE2 . TYR A 1 600  ? 171.875 180.956 268.503 1.00 69.60  ? 583  TYR B CE2 1 
ATOM   4517  C CZ  . TYR A 1 600  ? 171.036 180.881 267.419 1.00 69.60  ? 583  TYR B CZ  1 
ATOM   4518  O OH  . TYR A 1 600  ? 171.354 181.550 266.261 1.00 69.60  ? 583  TYR B OH  1 
ATOM   4519  N N   . THR A 1 601  ? 171.549 176.849 268.973 1.00 72.36  ? 584  THR B N   1 
ATOM   4520  C CA  . THR A 1 601  ? 172.749 176.626 268.182 1.00 72.36  ? 584  THR B CA  1 
ATOM   4521  C C   . THR A 1 601  ? 172.586 177.291 266.824 1.00 72.36  ? 584  THR B C   1 
ATOM   4522  O O   . THR A 1 601  ? 171.486 177.339 266.268 1.00 72.36  ? 584  THR B O   1 
ATOM   4523  C CB  . THR A 1 601  ? 173.042 175.136 268.003 1.00 72.36  ? 584  THR B CB  1 
ATOM   4524  O OG1 . THR A 1 601  ? 174.283 174.977 267.310 1.00 72.36  ? 584  THR B OG1 1 
ATOM   4525  C CG2 . THR A 1 601  ? 171.939 174.465 267.207 1.00 72.36  ? 584  THR B CG2 1 
ATOM   4526  N N   . PHE A 1 602  ? 173.689 177.811 266.294 1.00 73.96  ? 585  PHE B N   1 
ATOM   4527  C CA  . PHE A 1 602  ? 173.662 178.540 265.035 1.00 73.96  ? 585  PHE B CA  1 
ATOM   4528  C C   . PHE A 1 602  ? 174.149 177.707 263.858 1.00 73.96  ? 585  PHE B C   1 
ATOM   4529  O O   . PHE A 1 602  ? 174.398 178.260 262.783 1.00 73.96  ? 585  PHE B O   1 
ATOM   4530  C CB  . PHE A 1 602  ? 174.485 179.824 265.144 1.00 73.96  ? 585  PHE B CB  1 
ATOM   4531  C CG  . PHE A 1 602  ? 175.849 179.628 265.731 1.00 73.96  ? 585  PHE B CG  1 
ATOM   4532  C CD1 . PHE A 1 602  ? 176.925 179.324 264.923 1.00 73.96  ? 585  PHE B CD1 1 
ATOM   4533  C CD2 . PHE A 1 602  ? 176.058 179.768 267.088 1.00 73.96  ? 585  PHE B CD2 1 
ATOM   4534  C CE1 . PHE A 1 602  ? 178.182 179.149 265.460 1.00 73.96  ? 585  PHE B CE1 1 
ATOM   4535  C CE2 . PHE A 1 602  ? 177.313 179.595 267.629 1.00 73.96  ? 585  PHE B CE2 1 
ATOM   4536  C CZ  . PHE A 1 602  ? 178.375 179.285 266.815 1.00 73.96  ? 585  PHE B CZ  1 
ATOM   4537  N N   . PHE A 1 603  ? 174.284 176.396 264.029 1.00 78.92  ? 586  PHE B N   1 
ATOM   4538  C CA  . PHE A 1 603  ? 174.719 175.535 262.943 1.00 78.92  ? 586  PHE B CA  1 
ATOM   4539  C C   . PHE A 1 603  ? 173.534 175.184 262.046 1.00 78.92  ? 586  PHE B C   1 
ATOM   4540  O O   . PHE A 1 603  ? 172.399 175.610 262.273 1.00 78.92  ? 586  PHE B O   1 
ATOM   4541  C CB  . PHE A 1 603  ? 175.393 174.285 263.502 1.00 78.92  ? 586  PHE B CB  1 
ATOM   4542  C CG  . PHE A 1 603  ? 176.727 174.553 264.132 1.00 78.92  ? 586  PHE B CG  1 
ATOM   4543  C CD1 . PHE A 1 603  ? 177.502 175.617 263.709 1.00 78.92  ? 586  PHE B CD1 1 
ATOM   4544  C CD2 . PHE A 1 603  ? 177.201 173.751 265.153 1.00 78.92  ? 586  PHE B CD2 1 
ATOM   4545  C CE1 . PHE A 1 603  ? 178.726 175.870 264.287 1.00 78.92  ? 586  PHE B CE1 1 
ATOM   4546  C CE2 . PHE A 1 603  ? 178.424 173.999 265.733 1.00 78.92  ? 586  PHE B CE2 1 
ATOM   4547  C CZ  . PHE A 1 603  ? 179.187 175.060 265.300 1.00 78.92  ? 586  PHE B CZ  1 
ATOM   4548  N N   . SER A 1 604  ? 173.799 174.397 261.009 1.00 84.11  ? 587  SER B N   1 
ATOM   4549  C CA  . SER A 1 604  ? 172.758 174.045 260.057 1.00 84.11  ? 587  SER B CA  1 
ATOM   4550  C C   . SER A 1 604  ? 171.764 173.067 260.678 1.00 84.11  ? 587  SER B C   1 
ATOM   4551  O O   . SER A 1 604  ? 172.021 172.447 261.712 1.00 84.11  ? 587  SER B O   1 
ATOM   4552  C CB  . SER A 1 604  ? 173.364 173.443 258.791 1.00 84.11  ? 587  SER B CB  1 
ATOM   4553  O OG  . SER A 1 604  ? 172.371 172.810 258.005 1.00 84.11  ? 587  SER B OG  1 
ATOM   4554  N N   . SER A 1 605  ? 170.608 172.938 260.022 1.00 81.44  ? 588  SER B N   1 
ATOM   4555  C CA  . SER A 1 605  ? 169.557 172.065 260.534 1.00 81.44  ? 588  SER B CA  1 
ATOM   4556  C C   . SER A 1 605  ? 169.982 170.602 260.536 1.00 81.44  ? 588  SER B C   1 
ATOM   4557  O O   . SER A 1 605  ? 169.506 169.820 261.368 1.00 81.44  ? 588  SER B O   1 
ATOM   4558  C CB  . SER A 1 605  ? 168.282 172.243 259.713 1.00 81.44  ? 588  SER B CB  1 
ATOM   4559  O OG  . SER A 1 605  ? 168.382 171.569 258.472 1.00 81.44  ? 588  SER B OG  1 
ATOM   4560  N N   . ASP A 1 606  ? 170.868 170.209 259.618 1.00 84.70  ? 589  ASP B N   1 
ATOM   4561  C CA  . ASP A 1 606  ? 171.320 168.823 259.585 1.00 84.70  ? 589  ASP B CA  1 
ATOM   4562  C C   . ASP A 1 606  ? 172.059 168.452 260.865 1.00 84.70  ? 589  ASP B C   1 
ATOM   4563  O O   . ASP A 1 606  ? 171.866 167.359 261.407 1.00 84.70  ? 589  ASP B O   1 
ATOM   4564  C CB  . ASP A 1 606  ? 172.197 168.581 258.354 1.00 84.70  ? 589  ASP B CB  1 
ATOM   4565  C CG  . ASP A 1 606  ? 173.427 169.476 258.316 1.00 84.70  ? 589  ASP B CG  1 
ATOM   4566  O OD1 . ASP A 1 606  ? 173.662 170.233 259.281 1.00 84.70  ? 589  ASP B OD1 1 
ATOM   4567  O OD2 . ASP A 1 606  ? 174.167 169.419 257.310 1.00 84.70  ? 589  ASP B OD2 1 
ATOM   4568  N N   . TYR A 1 607  ? 172.900 169.356 261.370 1.00 81.95  ? 590  TYR B N   1 
ATOM   4569  C CA  . TYR A 1 607  ? 173.667 169.060 262.575 1.00 81.95  ? 590  TYR B CA  1 
ATOM   4570  C C   . TYR A 1 607  ? 172.756 168.886 263.784 1.00 81.95  ? 590  TYR B C   1 
ATOM   4571  O O   . TYR A 1 607  ? 172.911 167.932 264.557 1.00 81.95  ? 590  TYR B O   1 
ATOM   4572  C CB  . TYR A 1 607  ? 174.686 170.166 262.831 1.00 81.95  ? 590  TYR B CB  1 
ATOM   4573  C CG  . TYR A 1 607  ? 175.680 169.834 263.916 1.00 81.95  ? 590  TYR B CG  1 
ATOM   4574  C CD1 . TYR A 1 607  ? 176.391 168.645 263.892 1.00 81.95  ? 590  TYR B CD1 1 
ATOM   4575  C CD2 . TYR A 1 607  ? 175.896 170.703 264.971 1.00 81.95  ? 590  TYR B CD2 1 
ATOM   4576  C CE1 . TYR A 1 607  ? 177.299 168.340 264.883 1.00 81.95  ? 590  TYR B CE1 1 
ATOM   4577  C CE2 . TYR A 1 607  ? 176.800 170.407 265.965 1.00 81.95  ? 590  TYR B CE2 1 
ATOM   4578  C CZ  . TYR A 1 607  ? 177.499 169.224 265.917 1.00 81.95  ? 590  TYR B CZ  1 
ATOM   4579  O OH  . TYR A 1 607  ? 178.401 168.927 266.911 1.00 81.95  ? 590  TYR B OH  1 
ATOM   4580  N N   . VAL A 1 608  ? 171.805 169.804 263.971 1.00 75.58  ? 591  VAL B N   1 
ATOM   4581  C CA  . VAL A 1 608  ? 170.908 169.696 265.115 1.00 75.58  ? 591  VAL B CA  1 
ATOM   4582  C C   . VAL A 1 608  ? 170.018 168.470 264.979 1.00 75.58  ? 591  VAL B C   1 
ATOM   4583  O O   . VAL A 1 608  ? 169.668 167.835 265.982 1.00 75.58  ? 591  VAL B O   1 
ATOM   4584  C CB  . VAL A 1 608  ? 170.089 170.988 265.296 1.00 75.58  ? 591  VAL B CB  1 
ATOM   4585  C CG1 . VAL A 1 608  ? 169.408 171.379 264.015 1.00 75.58  ? 591  VAL B CG1 1 
ATOM   4586  C CG2 . VAL A 1 608  ? 169.061 170.814 266.390 1.00 75.58  ? 591  VAL B CG2 1 
ATOM   4587  N N   . LYS A 1 609  ? 169.644 168.103 263.751 1.00 77.93  ? 592  LYS B N   1 
ATOM   4588  C CA  . LYS A 1 609  ? 168.917 166.854 263.561 1.00 77.93  ? 592  LYS B CA  1 
ATOM   4589  C C   . LYS A 1 609  ? 169.773 165.658 263.962 1.00 77.93  ? 592  LYS B C   1 
ATOM   4590  O O   . LYS A 1 609  ? 169.278 164.710 264.581 1.00 77.93  ? 592  LYS B O   1 
ATOM   4591  C CB  . LYS A 1 609  ? 168.461 166.726 262.108 1.00 77.93  ? 592  LYS B CB  1 
ATOM   4592  C CG  . LYS A 1 609  ? 167.298 165.764 261.882 1.00 77.93  ? 592  LYS B CG  1 
ATOM   4593  C CD  . LYS A 1 609  ? 166.520 165.478 263.163 1.00 77.93  ? 592  LYS B CD  1 
ATOM   4594  C CE  . LYS A 1 609  ? 165.186 164.810 262.866 1.00 77.93  ? 592  LYS B CE  1 
ATOM   4595  N NZ  . LYS A 1 609  ? 164.441 164.474 264.110 1.00 77.93  ? 592  LYS B NZ  1 
ATOM   4596  N N   . LYS A 1 610  ? 171.060 165.687 263.618 1.00 77.13  ? 593  LYS B N   1 
ATOM   4597  C CA  . LYS A 1 610  ? 171.932 164.553 263.908 1.00 77.13  ? 593  LYS B CA  1 
ATOM   4598  C C   . LYS A 1 610  ? 172.161 164.388 265.405 1.00 77.13  ? 593  LYS B C   1 
ATOM   4599  O O   . LYS A 1 610  ? 171.984 163.294 265.952 1.00 77.13  ? 593  LYS B O   1 
ATOM   4600  C CB  . LYS A 1 610  ? 173.264 164.720 263.178 1.00 77.13  ? 593  LYS B CB  1 
ATOM   4601  C CG  . LYS A 1 610  ? 173.871 163.420 262.691 1.00 77.13  ? 593  LYS B CG  1 
ATOM   4602  C CD  . LYS A 1 610  ? 175.072 163.683 261.806 1.00 77.13  ? 593  LYS B CD  1 
ATOM   4603  C CE  . LYS A 1 610  ? 174.689 164.529 260.607 1.00 77.13  ? 593  LYS B CE  1 
ATOM   4604  N NZ  . LYS A 1 610  ? 173.467 164.008 259.937 1.00 77.13  ? 593  LYS B NZ  1 
ATOM   4605  N N   . VAL A 1 611  ? 172.546 165.468 266.092 1.00 69.60  ? 594  VAL B N   1 
ATOM   4606  C CA  . VAL A 1 611  ? 172.910 165.360 267.502 1.00 69.60  ? 594  VAL B CA  1 
ATOM   4607  C C   . VAL A 1 611  ? 171.723 165.054 268.399 1.00 69.60  ? 594  VAL B C   1 
ATOM   4608  O O   . VAL A 1 611  ? 171.917 164.744 269.579 1.00 69.60  ? 594  VAL B O   1 
ATOM   4609  C CB  . VAL A 1 611  ? 173.602 166.643 268.001 1.00 69.60  ? 594  VAL B CB  1 
ATOM   4610  C CG1 . VAL A 1 611  ? 174.703 167.055 267.049 1.00 69.60  ? 594  VAL B CG1 1 
ATOM   4611  C CG2 . VAL A 1 611  ? 172.596 167.756 268.166 1.00 69.60  ? 594  VAL B CG2 1 
ATOM   4612  N N   . ASN A 1 612  ? 170.503 165.136 267.877 1.00 69.60  ? 595  ASN B N   1 
ATOM   4613  C CA  . ASN A 1 612  ? 169.296 164.854 268.639 1.00 69.60  ? 595  ASN B CA  1 
ATOM   4614  C C   . ASN A 1 612  ? 168.802 163.426 268.457 1.00 69.60  ? 595  ASN B C   1 
ATOM   4615  O O   . ASN A 1 612  ? 167.753 163.075 269.003 1.00 69.60  ? 595  ASN B O   1 
ATOM   4616  C CB  . ASN A 1 612  ? 168.186 165.830 268.238 1.00 69.60  ? 595  ASN B CB  1 
ATOM   4617  C CG  . ASN A 1 612  ? 168.413 167.221 268.779 1.00 69.60  ? 595  ASN B CG  1 
ATOM   4618  O OD1 . ASN A 1 612  ? 169.138 167.408 269.752 1.00 69.60  ? 595  ASN B OD1 1 
ATOM   4619  N ND2 . ASN A 1 612  ? 167.804 168.211 268.140 1.00 69.60  ? 595  ASN B ND2 1 
ATOM   4620  N N   . LYS A 1 613  ? 169.527 162.601 267.711 1.00 74.16  ? 596  LYS B N   1 
ATOM   4621  C CA  . LYS A 1 613  ? 169.046 161.293 267.290 1.00 74.16  ? 596  LYS B CA  1 
ATOM   4622  C C   . LYS A 1 613  ? 169.572 160.211 268.221 1.00 74.16  ? 596  LYS B C   1 
ATOM   4623  O O   . LYS A 1 613  ? 170.771 160.165 268.511 1.00 74.16  ? 596  LYS B O   1 
ATOM   4624  C CB  . LYS A 1 613  ? 169.476 161.007 265.852 1.00 74.16  ? 596  LYS B CB  1 
ATOM   4625  C CG  . LYS A 1 613  ? 169.224 159.590 265.398 1.00 74.16  ? 596  LYS B CG  1 
ATOM   4626  C CD  . LYS A 1 613  ? 169.205 159.507 263.884 1.00 74.16  ? 596  LYS B CD  1 
ATOM   4627  C CE  . LYS A 1 613  ? 170.352 160.291 263.272 1.00 74.16  ? 596  LYS B CE  1 
ATOM   4628  N NZ  . LYS A 1 613  ? 171.672 159.741 263.678 1.00 74.16  ? 596  LYS B NZ  1 
ATOM   4629  N N   . ALA A 1 614  ? 168.677 159.340 268.679 1.00 75.22  ? 597  ALA B N   1 
ATOM   4630  C CA  . ALA A 1 614  ? 169.063 158.237 269.549 1.00 75.22  ? 597  ALA B CA  1 
ATOM   4631  C C   . ALA A 1 614  ? 169.731 157.148 268.718 1.00 75.22  ? 597  ALA B C   1 
ATOM   4632  O O   . ALA A 1 614  ? 169.104 156.570 267.824 1.00 75.22  ? 597  ALA B O   1 
ATOM   4633  C CB  . ALA A 1 614  ? 167.845 157.690 270.286 1.00 75.22  ? 597  ALA B CB  1 
ATOM   4634  N N   . THR A 1 615  ? 170.997 156.862 269.015 1.00 76.09  ? 598  THR B N   1 
ATOM   4635  C CA  . THR A 1 615  ? 171.798 155.912 268.256 1.00 76.09  ? 598  THR B CA  1 
ATOM   4636  C C   . THR A 1 615  ? 172.231 154.757 269.146 1.00 76.09  ? 598  THR B C   1 
ATOM   4637  O O   . THR A 1 615  ? 172.570 154.959 270.316 1.00 76.09  ? 598  THR B O   1 
ATOM   4638  C CB  . THR A 1 615  ? 173.033 156.589 267.661 1.00 76.09  ? 598  THR B CB  1 
ATOM   4639  O OG1 . THR A 1 615  ? 173.599 157.479 268.630 1.00 76.09  ? 598  THR B OG1 1 
ATOM   4640  C CG2 . THR A 1 615  ? 172.666 157.371 266.417 1.00 76.09  ? 598  THR B CG2 1 
ATOM   4641  N N   . GLU A 1 616  ? 172.225 153.548 268.588 1.00 80.32  ? 599  GLU B N   1 
ATOM   4642  C CA  . GLU A 1 616  ? 172.661 152.378 269.333 1.00 80.32  ? 599  GLU B CA  1 
ATOM   4643  C C   . GLU A 1 616  ? 174.173 152.418 269.540 1.00 80.32  ? 599  GLU B C   1 
ATOM   4644  O O   . GLU A 1 616  ? 174.875 153.314 269.064 1.00 80.32  ? 599  GLU B O   1 
ATOM   4645  C CB  . GLU A 1 616  ? 172.274 151.091 268.610 1.00 80.32  ? 599  GLU B CB  1 
ATOM   4646  C CG  . GLU A 1 616  ? 170.791 150.867 268.429 1.00 80.32  ? 599  GLU B CG  1 
ATOM   4647  C CD  . GLU A 1 616  ? 170.419 150.658 266.977 1.00 80.32  ? 599  GLU B CD  1 
ATOM   4648  O OE1 . GLU A 1 616  ? 171.076 151.260 266.103 1.00 80.32  ? 599  GLU B OE1 1 
ATOM   4649  O OE2 . GLU A 1 616  ? 169.478 149.883 266.708 1.00 80.32  ? 599  GLU B OE2 1 
ATOM   4650  N N   . ALA A 1 617  ? 174.680 151.417 270.259 1.00 83.06  ? 600  ALA B N   1 
ATOM   4651  C CA  . ALA A 1 617  ? 176.121 151.307 270.455 1.00 83.06  ? 600  ALA B CA  1 
ATOM   4652  C C   . ALA A 1 617  ? 176.831 150.931 269.160 1.00 83.06  ? 600  ALA B C   1 
ATOM   4653  O O   . ALA A 1 617  ? 177.959 151.373 268.913 1.00 83.06  ? 600  ALA B O   1 
ATOM   4654  C CB  . ALA A 1 617  ? 176.423 150.286 271.550 1.00 83.06  ? 600  ALA B CB  1 
ATOM   4655  N N   . ALA A 1 618  ? 176.185 150.117 268.321 1.00 82.42  ? 601  ALA B N   1 
ATOM   4656  C CA  . ALA A 1 618  ? 176.822 149.653 267.094 1.00 82.42  ? 601  ALA B CA  1 
ATOM   4657  C C   . ALA A 1 618  ? 177.143 150.801 266.147 1.00 82.42  ? 601  ALA B C   1 
ATOM   4658  O O   . ALA A 1 618  ? 178.068 150.693 265.335 1.00 82.42  ? 601  ALA B O   1 
ATOM   4659  C CB  . ALA A 1 618  ? 175.931 148.626 266.397 1.00 82.42  ? 601  ALA B CB  1 
ATOM   4660  N N   . MET A 1 619  ? 176.396 151.901 266.225 1.00 84.04  ? 602  MET B N   1 
ATOM   4661  C CA  . MET A 1 619  ? 176.641 153.060 265.380 1.00 84.04  ? 602  MET B CA  1 
ATOM   4662  C C   . MET A 1 619  ? 177.197 154.255 266.142 1.00 84.04  ? 602  MET B C   1 
ATOM   4663  O O   . MET A 1 619  ? 177.405 155.308 265.535 1.00 84.04  ? 602  MET B O   1 
ATOM   4664  C CB  . MET A 1 619  ? 175.351 153.474 264.663 1.00 84.04  ? 602  MET B CB  1 
ATOM   4665  C CG  . MET A 1 619  ? 174.485 152.306 264.226 1.00 84.04  ? 602  MET B CG  1 
ATOM   4666  S SD  . MET A 1 619  ? 173.240 152.778 263.011 1.00 84.04  ? 602  MET B SD  1 
ATOM   4667  C CE  . MET A 1 619  ? 174.133 154.009 262.065 1.00 84.04  ? 602  MET B CE  1 
ATOM   4668  N N   . PHE A 1 620  ? 177.439 154.114 267.447 1.00 82.19  ? 603  PHE B N   1 
ATOM   4669  C CA  . PHE A 1 620  ? 177.893 155.234 268.267 1.00 82.19  ? 603  PHE B CA  1 
ATOM   4670  C C   . PHE A 1 620  ? 179.250 155.761 267.808 1.00 82.19  ? 603  PHE B C   1 
ATOM   4671  O O   . PHE A 1 620  ? 179.464 156.978 267.714 1.00 82.19  ? 603  PHE B O   1 
ATOM   4672  C CB  . PHE A 1 620  ? 177.954 154.787 269.728 1.00 82.19  ? 603  PHE B CB  1 
ATOM   4673  C CG  . PHE A 1 620  ? 178.686 155.732 270.629 1.00 82.19  ? 603  PHE B CG  1 
ATOM   4674  C CD1 . PHE A 1 620  ? 178.338 157.067 270.692 1.00 82.19  ? 603  PHE B CD1 1 
ATOM   4675  C CD2 . PHE A 1 620  ? 179.731 155.282 271.411 1.00 82.19  ? 603  PHE B CD2 1 
ATOM   4676  C CE1 . PHE A 1 620  ? 179.014 157.930 271.527 1.00 82.19  ? 603  PHE B CE1 1 
ATOM   4677  C CE2 . PHE A 1 620  ? 180.411 156.142 272.242 1.00 82.19  ? 603  PHE B CE2 1 
ATOM   4678  C CZ  . PHE A 1 620  ? 180.054 157.468 272.299 1.00 82.19  ? 603  PHE B CZ  1 
ATOM   4679  N N   . LEU A 1 621  ? 180.189 154.850 267.539 1.00 84.29  ? 604  LEU B N   1 
ATOM   4680  C CA  . LEU A 1 621  ? 181.537 155.258 267.158 1.00 84.29  ? 604  LEU B CA  1 
ATOM   4681  C C   . LEU A 1 621  ? 181.532 156.012 265.837 1.00 84.29  ? 604  LEU B C   1 
ATOM   4682  O O   . LEU A 1 621  ? 182.227 157.024 265.689 1.00 84.29  ? 604  LEU B O   1 
ATOM   4683  C CB  . LEU A 1 621  ? 182.449 154.036 267.080 1.00 84.29  ? 604  LEU B CB  1 
ATOM   4684  C CG  . LEU A 1 621  ? 183.009 153.564 268.420 1.00 84.29  ? 604  LEU B CG  1 
ATOM   4685  C CD1 . LEU A 1 621  ? 184.014 152.443 268.224 1.00 84.29  ? 604  LEU B CD1 1 
ATOM   4686  C CD2 . LEU A 1 621  ? 183.641 154.730 269.157 1.00 84.29  ? 604  LEU B CD2 1 
ATOM   4687  N N   . GLY A 1 622  ? 180.760 155.532 264.862 1.00 83.88  ? 605  GLY B N   1 
ATOM   4688  C CA  . GLY A 1 622  ? 180.626 156.266 263.614 1.00 83.88  ? 605  GLY B CA  1 
ATOM   4689  C C   . GLY A 1 622  ? 179.912 157.590 263.804 1.00 83.88  ? 605  GLY B C   1 
ATOM   4690  O O   . GLY A 1 622  ? 180.255 158.592 263.170 1.00 83.88  ? 605  GLY B O   1 
ATOM   4691  N N   . TRP A 1 623  ? 178.909 157.608 264.684 1.00 80.58  ? 606  TRP B N   1 
ATOM   4692  C CA  . TRP A 1 623  ? 178.156 158.824 264.964 1.00 80.58  ? 606  TRP B CA  1 
ATOM   4693  C C   . TRP A 1 623  ? 179.067 159.931 265.473 1.00 80.58  ? 606  TRP B C   1 
ATOM   4694  O O   . TRP A 1 623  ? 178.967 161.085 265.045 1.00 80.58  ? 606  TRP B O   1 
ATOM   4695  C CB  . TRP A 1 623  ? 177.060 158.516 265.987 1.00 80.58  ? 606  TRP B CB  1 
ATOM   4696  C CG  . TRP A 1 623  ? 176.144 159.661 266.270 1.00 80.58  ? 606  TRP B CG  1 
ATOM   4697  C CD1 . TRP A 1 623  ? 175.589 160.512 265.365 1.00 80.58  ? 606  TRP B CD1 1 
ATOM   4698  C CD2 . TRP A 1 623  ? 175.708 160.105 267.559 1.00 80.58  ? 606  TRP B CD2 1 
ATOM   4699  N NE1 . TRP A 1 623  ? 174.818 161.447 266.008 1.00 80.58  ? 606  TRP B NE1 1 
ATOM   4700  C CE2 . TRP A 1 623  ? 174.878 161.218 267.357 1.00 80.58  ? 606  TRP B CE2 1 
ATOM   4701  C CE3 . TRP A 1 623  ? 175.936 159.663 268.863 1.00 80.58  ? 606  TRP B CE3 1 
ATOM   4702  C CZ2 . TRP A 1 623  ? 174.276 161.894 268.408 1.00 80.58  ? 606  TRP B CZ2 1 
ATOM   4703  C CZ3 . TRP A 1 623  ? 175.338 160.334 269.902 1.00 80.58  ? 606  TRP B CZ3 1 
ATOM   4704  C CH2 . TRP A 1 623  ? 174.518 161.436 269.671 1.00 80.58  ? 606  TRP B CH2 1 
ATOM   4705  N N   . VAL A 1 624  ? 179.963 159.592 266.402 1.00 81.53  ? 607  VAL B N   1 
ATOM   4706  C CA  . VAL A 1 624  ? 180.847 160.606 266.979 1.00 81.53  ? 607  VAL B CA  1 
ATOM   4707  C C   . VAL A 1 624  ? 181.763 161.193 265.911 1.00 81.53  ? 607  VAL B C   1 
ATOM   4708  O O   . VAL A 1 624  ? 181.989 162.410 265.854 1.00 81.53  ? 607  VAL B O   1 
ATOM   4709  C CB  . VAL A 1 624  ? 181.651 160.017 268.149 1.00 81.53  ? 607  VAL B CB  1 
ATOM   4710  C CG1 . VAL A 1 624  ? 182.825 160.918 268.491 1.00 81.53  ? 607  VAL B CG1 1 
ATOM   4711  C CG2 . VAL A 1 624  ? 180.754 159.850 269.349 1.00 81.53  ? 607  VAL B CG2 1 
ATOM   4712  N N   . GLU A 1 625  ? 182.317 160.333 265.055 1.00 89.45  ? 608  GLU B N   1 
ATOM   4713  C CA  . GLU A 1 625  ? 183.202 160.813 263.998 1.00 89.45  ? 608  GLU B CA  1 
ATOM   4714  C C   . GLU A 1 625  ? 182.449 161.704 263.018 1.00 89.45  ? 608  GLU B C   1 
ATOM   4715  O O   . GLU A 1 625  ? 182.961 162.745 262.586 1.00 89.45  ? 608  GLU B O   1 
ATOM   4716  C CB  . GLU A 1 625  ? 183.848 159.632 263.277 1.00 89.45  ? 608  GLU B CB  1 
ATOM   4717  C CG  . GLU A 1 625  ? 185.190 159.960 262.646 1.00 89.45  ? 608  GLU B CG  1 
ATOM   4718  C CD  . GLU A 1 625  ? 185.055 160.712 261.337 1.00 89.45  ? 608  GLU B CD  1 
ATOM   4719  O OE1 . GLU A 1 625  ? 184.042 160.510 260.636 1.00 89.45  ? 608  GLU B OE1 1 
ATOM   4720  O OE2 . GLU A 1 625  ? 185.962 161.505 261.009 1.00 89.45  ? 608  GLU B OE2 1 
ATOM   4721  N N   . GLN A 1 626  ? 181.224 161.315 262.652 1.00 86.51  ? 609  GLN B N   1 
ATOM   4722  C CA  . GLN A 1 626  ? 180.417 162.181 261.798 1.00 86.51  ? 609  GLN B CA  1 
ATOM   4723  C C   . GLN A 1 626  ? 180.169 163.523 262.471 1.00 86.51  ? 609  GLN B C   1 
ATOM   4724  O O   . GLN A 1 626  ? 180.221 164.573 261.824 1.00 86.51  ? 609  GLN B O   1 
ATOM   4725  C CB  . GLN A 1 626  ? 179.091 161.510 261.436 1.00 86.51  ? 609  GLN B CB  1 
ATOM   4726  C CG  . GLN A 1 626  ? 179.224 160.134 260.818 1.00 86.51  ? 609  GLN B CG  1 
ATOM   4727  C CD  . GLN A 1 626  ? 177.920 159.364 260.833 1.00 86.51  ? 609  GLN B CD  1 
ATOM   4728  O OE1 . GLN A 1 626  ? 177.732 158.455 261.641 1.00 86.51  ? 609  GLN B OE1 1 
ATOM   4729  N NE2 . GLN A 1 626  ? 177.010 159.724 259.936 1.00 86.51  ? 609  GLN B NE2 1 
ATOM   4730  N N   . LEU A 1 627  ? 179.899 163.505 263.776 1.00 82.31  ? 610  LEU B N   1 
ATOM   4731  C CA  . LEU A 1 627  ? 179.621 164.744 264.491 1.00 82.31  ? 610  LEU B CA  1 
ATOM   4732  C C   . LEU A 1 627  ? 180.826 165.674 264.471 1.00 82.31  ? 610  LEU B C   1 
ATOM   4733  O O   . LEU A 1 627  ? 180.689 166.881 264.240 1.00 82.31  ? 610  LEU B O   1 
ATOM   4734  C CB  . LEU A 1 627  ? 179.202 164.437 265.927 1.00 82.31  ? 610  LEU B CB  1 
ATOM   4735  C CG  . LEU A 1 627  ? 177.747 164.015 266.111 1.00 82.31  ? 610  LEU B CG  1 
ATOM   4736  C CD1 . LEU A 1 627  ? 177.281 164.378 267.498 1.00 82.31  ? 610  LEU B CD1 1 
ATOM   4737  C CD2 . LEU A 1 627  ? 176.860 164.657 265.067 1.00 82.31  ? 610  LEU B CD2 1 
ATOM   4738  N N   . VAL A 1 628  ? 182.021 165.130 264.708 1.00 86.71  ? 611  VAL B N   1 
ATOM   4739  C CA  . VAL A 1 628  ? 183.208 165.984 264.675 1.00 86.71  ? 611  VAL B CA  1 
ATOM   4740  C C   . VAL A 1 628  ? 183.465 166.483 263.259 1.00 86.71  ? 611  VAL B C   1 
ATOM   4741  O O   . VAL A 1 628  ? 183.919 167.621 263.065 1.00 86.71  ? 611  VAL B O   1 
ATOM   4742  C CB  . VAL A 1 628  ? 184.440 165.266 265.269 1.00 86.71  ? 611  VAL B CB  1 
ATOM   4743  C CG1 . VAL A 1 628  ? 184.104 164.662 266.621 1.00 86.71  ? 611  VAL B CG1 1 
ATOM   4744  C CG2 . VAL A 1 628  ? 184.984 164.214 264.326 1.00 86.71  ? 611  VAL B CG2 1 
ATOM   4745  N N   . TYR A 1 629  ? 183.170 165.662 262.247 1.00 93.04  ? 612  TYR B N   1 
ATOM   4746  C CA  . TYR A 1 629  ? 183.335 166.113 260.870 1.00 93.04  ? 612  TYR B CA  1 
ATOM   4747  C C   . TYR A 1 629  ? 182.410 167.284 260.563 1.00 93.04  ? 612  TYR B C   1 
ATOM   4748  O O   . TYR A 1 629  ? 182.831 168.279 259.963 1.00 93.04  ? 612  TYR B O   1 
ATOM   4749  C CB  . TYR A 1 629  ? 183.088 164.957 259.901 1.00 93.04  ? 612  TYR B CB  1 
ATOM   4750  C CG  . TYR A 1 629  ? 183.743 165.146 258.552 1.00 93.04  ? 612  TYR B CG  1 
ATOM   4751  C CD1 . TYR A 1 629  ? 183.275 166.098 257.657 1.00 93.04  ? 612  TYR B CD1 1 
ATOM   4752  C CD2 . TYR A 1 629  ? 184.838 164.380 258.179 1.00 93.04  ? 612  TYR B CD2 1 
ATOM   4753  C CE1 . TYR A 1 629  ? 183.872 166.276 256.427 1.00 93.04  ? 612  TYR B CE1 1 
ATOM   4754  C CE2 . TYR A 1 629  ? 185.442 164.552 256.951 1.00 93.04  ? 612  TYR B CE2 1 
ATOM   4755  C CZ  . TYR A 1 629  ? 184.956 165.501 256.078 1.00 93.04  ? 612  TYR B CZ  1 
ATOM   4756  O OH  . TYR A 1 629  ? 185.555 165.675 254.852 1.00 93.04  ? 612  TYR B OH  1 
ATOM   4757  N N   . ASP A 1 630  ? 181.140 167.185 260.967 1.00 92.01  ? 613  ASP B N   1 
ATOM   4758  C CA  . ASP A 1 630  ? 180.222 168.300 260.750 1.00 92.01  ? 613  ASP B CA  1 
ATOM   4759  C C   . ASP A 1 630  ? 180.633 169.526 261.554 1.00 92.01  ? 613  ASP B C   1 
ATOM   4760  O O   . ASP A 1 630  ? 180.454 170.658 261.097 1.00 92.01  ? 613  ASP B O   1 
ATOM   4761  C CB  . ASP A 1 630  ? 178.776 167.915 261.073 1.00 92.01  ? 613  ASP B CB  1 
ATOM   4762  C CG  . ASP A 1 630  ? 178.286 166.729 260.269 1.00 92.01  ? 613  ASP B CG  1 
ATOM   4763  O OD1 . ASP A 1 630  ? 178.061 166.898 259.052 1.00 92.01  ? 613  ASP B OD1 1 
ATOM   4764  O OD2 . ASP A 1 630  ? 178.125 165.633 260.837 1.00 92.01  ? 613  ASP B OD2 1 
ATOM   4765  N N   . PHE A 1 631  ? 181.171 169.327 262.758 1.00 89.89  ? 614  PHE B N   1 
ATOM   4766  C CA  . PHE A 1 631  ? 181.673 170.462 263.527 1.00 89.89  ? 614  PHE B CA  1 
ATOM   4767  C C   . PHE A 1 631  ? 182.762 171.200 262.759 1.00 89.89  ? 614  PHE B C   1 
ATOM   4768  O O   . PHE A 1 631  ? 182.716 172.429 262.610 1.00 89.89  ? 614  PHE B O   1 
ATOM   4769  C CB  . PHE A 1 631  ? 182.200 169.985 264.880 1.00 89.89  ? 614  PHE B CB  1 
ATOM   4770  C CG  . PHE A 1 631  ? 182.292 171.070 265.910 1.00 89.89  ? 614  PHE B CG  1 
ATOM   4771  C CD1 . PHE A 1 631  ? 181.675 172.288 265.710 1.00 89.89  ? 614  PHE B CD1 1 
ATOM   4772  C CD2 . PHE A 1 631  ? 183.008 170.873 267.074 1.00 89.89  ? 614  PHE B CD2 1 
ATOM   4773  C CE1 . PHE A 1 631  ? 181.764 173.283 266.656 1.00 89.89  ? 614  PHE B CE1 1 
ATOM   4774  C CE2 . PHE A 1 631  ? 183.101 171.865 268.021 1.00 89.89  ? 614  PHE B CE2 1 
ATOM   4775  C CZ  . PHE A 1 631  ? 182.478 173.071 267.812 1.00 89.89  ? 614  PHE B CZ  1 
ATOM   4776  N N   . THR A 1 632  ? 183.745 170.455 262.250 1.00 91.82  ? 615  THR B N   1 
ATOM   4777  C CA  . THR A 1 632  ? 184.813 171.073 261.469 1.00 91.82  ? 615  THR B CA  1 
ATOM   4778  C C   . THR A 1 632  ? 184.258 171.744 260.219 1.00 91.82  ? 615  THR B C   1 
ATOM   4779  O O   . THR A 1 632  ? 184.722 172.817 259.816 1.00 91.82  ? 615  THR B O   1 
ATOM   4780  C CB  . THR A 1 632  ? 185.864 170.031 261.094 1.00 91.82  ? 615  THR B CB  1 
ATOM   4781  O OG1 . THR A 1 632  ? 185.257 169.006 260.299 1.00 91.82  ? 615  THR B OG1 1 
ATOM   4782  C CG2 . THR A 1 632  ? 186.470 169.415 262.342 1.00 91.82  ? 615  THR B CG2 1 
ATOM   4783  N N   . ASP A 1 633  ? 183.300 171.090 259.572 1.00 96.19  ? 616  ASP B N   1 
ATOM   4784  C CA  . ASP A 1 633  ? 182.794 171.651 258.294 1.00 96.19  ? 616  ASP B CA  1 
ATOM   4785  C C   . ASP A 1 633  ? 182.128 172.994 258.580 1.00 96.19  ? 616  ASP B C   1 
ATOM   4786  O O   . ASP A 1 633  ? 182.499 173.982 257.927 1.00 96.19  ? 616  ASP B O   1 
ATOM   4787  C CB  . ASP A 1 633  ? 181.826 170.689 257.609 1.00 96.19  ? 616  ASP B CB  1 
ATOM   4788  C CG  . ASP A 1 633  ? 181.021 171.334 256.497 1.00 96.19  ? 616  ASP B CG  1 
ATOM   4789  O OD1 . ASP A 1 633  ? 181.628 172.048 255.676 1.00 96.19  ? 616  ASP B OD1 1 
ATOM   4790  O OD2 . ASP A 1 633  ? 179.796 171.113 256.460 1.00 96.19  ? 616  ASP B OD2 1 
ATOM   4791  N N   . GLU A 1 634  ? 181.204 173.026 259.538 1.00 92.86  ? 617  GLU B N   1 
ATOM   4792  C CA  . GLU A 1 634  ? 180.438 174.271 259.794 1.00 92.86  ? 617  GLU B CA  1 
ATOM   4793  C C   . GLU A 1 634  ? 181.370 175.379 260.285 1.00 92.86  ? 617  GLU B C   1 
ATOM   4794  O O   . GLU A 1 634  ? 181.216 176.514 259.818 1.00 92.86  ? 617  GLU B O   1 
ATOM   4795  C CB  . GLU A 1 634  ? 179.333 173.995 260.810 1.00 92.86  ? 617  GLU B CB  1 
ATOM   4796  C CG  . GLU A 1 634  ? 178.430 172.841 260.415 1.00 92.86  ? 617  GLU B CG  1 
ATOM   4797  C CD  . GLU A 1 634  ? 176.952 173.178 260.332 1.00 92.86  ? 617  GLU B CD  1 
ATOM   4798  O OE1 . GLU A 1 634  ? 176.134 172.239 260.278 1.00 92.86  ? 617  GLU B OE1 1 
ATOM   4799  O OE2 . GLU A 1 634  ? 176.622 174.380 260.320 1.00 92.86  ? 617  GLU B OE2 1 
ATOM   4800  N N   . THR A 1 635  ? 182.304 175.065 261.179 1.00 90.52  ? 618  THR B N   1 
ATOM   4801  C CA  . THR A 1 635  ? 183.140 176.142 261.769 1.00 90.52  ? 618  THR B CA  1 
ATOM   4802  C C   . THR A 1 635  ? 184.144 176.699 260.759 1.00 90.52  ? 618  THR B C   1 
ATOM   4803  O O   . THR A 1 635  ? 184.464 177.893 260.866 1.00 90.52  ? 618  THR B O   1 
ATOM   4804  C CB  . THR A 1 635  ? 183.895 175.634 262.996 1.00 90.52  ? 618  THR B CB  1 
ATOM   4805  O OG1 . THR A 1 635  ? 184.412 174.346 262.664 1.00 90.52  ? 618  THR B OG1 1 
ATOM   4806  C CG2 . THR A 1 635  ? 183.019 175.543 264.225 1.00 90.52  ? 618  THR B CG2 1 
ATOM   4807  N N   . SER A 1 636  ? 184.623 175.882 259.822 1.00 94.06  ? 619  SER B N   1 
ATOM   4808  C CA  . SER A 1 636  ? 185.702 176.350 258.912 1.00 94.06  ? 619  SER B CA  1 
ATOM   4809  C C   . SER A 1 636  ? 185.141 176.997 257.644 1.00 94.06  ? 619  SER B C   1 
ATOM   4810  O O   . SER A 1 636  ? 185.940 177.297 256.744 1.00 94.06  ? 619  SER B O   1 
ATOM   4811  C CB  . SER A 1 636  ? 186.612 175.211 258.564 1.00 94.06  ? 619  SER B CB  1 
ATOM   4812  O OG  . SER A 1 636  ? 185.902 174.209 257.852 1.00 94.06  ? 619  SER B OG  1 
ATOM   4813  N N   . GLU A 1 637  ? 183.830 177.210 257.572 1.00 98.31  ? 620  GLU B N   1 
ATOM   4814  C CA  . GLU A 1 637  ? 183.225 177.754 256.365 1.00 98.31  ? 620  GLU B CA  1 
ATOM   4815  C C   . GLU A 1 637  ? 183.677 179.192 256.130 1.00 98.31  ? 620  GLU B C   1 
ATOM   4816  O O   . GLU A 1 637  ? 183.950 179.946 257.068 1.00 98.31  ? 620  GLU B O   1 
ATOM   4817  C CB  . GLU A 1 637  ? 181.699 177.684 256.452 1.00 98.31  ? 620  GLU B CB  1 
ATOM   4818  C CG  . GLU A 1 637  ? 181.047 178.872 257.136 1.00 98.31  ? 620  GLU B CG  1 
ATOM   4819  C CD  . GLU A 1 637  ? 179.596 178.615 257.488 1.00 98.31  ? 620  GLU B CD  1 
ATOM   4820  O OE1 . GLU A 1 637  ? 179.309 177.567 258.104 1.00 98.31  ? 620  GLU B OE1 1 
ATOM   4821  O OE2 . GLU A 1 637  ? 178.743 179.460 257.148 1.00 98.31  ? 620  GLU B OE2 1 
ATOM   4822  N N   . VAL A 1 638  ? 183.765 179.612 254.868 1.00 102.66 ? 621  VAL B N   1 
ATOM   4823  C CA  . VAL A 1 638  ? 184.127 181.034 254.586 1.00 102.66 ? 621  VAL B CA  1 
ATOM   4824  C C   . VAL A 1 638  ? 183.244 181.589 253.461 1.00 102.66 ? 621  VAL B C   1 
ATOM   4825  O O   . VAL A 1 638  ? 182.477 180.806 252.874 1.00 102.66 ? 621  VAL B O   1 
ATOM   4826  C CB  . VAL A 1 638  ? 185.621 181.173 254.254 1.00 102.66 ? 621  VAL B CB  1 
ATOM   4827  C CG1 . VAL A 1 638  ? 186.428 181.588 255.471 1.00 102.66 ? 621  VAL B CG1 1 
ATOM   4828  C CG2 . VAL A 1 638  ? 186.181 179.894 253.654 1.00 102.66 ? 621  VAL B CG2 1 
ATOM   4829  N N   . SER A 1 639  ? 183.351 182.890 253.172 1.00 118.85 ? 622  SER B N   1 
ATOM   4830  C CA  . SER A 1 639  ? 182.480 183.526 252.146 1.00 118.85 ? 622  SER B CA  1 
ATOM   4831  C C   . SER A 1 639  ? 183.258 183.778 250.854 1.00 118.85 ? 622  SER B C   1 
ATOM   4832  O O   . SER A 1 639  ? 184.349 184.373 250.930 1.00 118.85 ? 622  SER B O   1 
ATOM   4833  C CB  . SER A 1 639  ? 181.883 184.796 252.654 1.00 118.85 ? 622  SER B CB  1 
ATOM   4834  O OG  . SER A 1 639  ? 180.659 185.073 251.992 1.00 118.85 ? 622  SER B OG  1 
ATOM   4835  N N   . THR A 1 640  ? 182.696 183.366 249.715 1.00 136.15 ? 623  THR B N   1 
ATOM   4836  C CA  . THR A 1 640  ? 183.395 183.490 248.408 1.00 136.15 ? 623  THR B CA  1 
ATOM   4837  C C   . THR A 1 640  ? 183.443 184.944 247.932 1.00 136.15 ? 623  THR B C   1 
ATOM   4838  O O   . THR A 1 640  ? 184.528 185.369 247.496 1.00 136.15 ? 623  THR B O   1 
ATOM   4839  C CB  . THR A 1 640  ? 182.702 182.617 247.357 1.00 136.15 ? 623  THR B CB  1 
ATOM   4840  O OG1 . THR A 1 640  ? 181.435 183.209 247.071 1.00 136.15 ? 623  THR B OG1 1 
ATOM   4841  C CG2 . THR A 1 640  ? 182.507 181.190 247.818 1.00 136.15 ? 623  THR B CG2 1 
ATOM   4842  N N   . THR A 1 641  ? 182.321 185.668 247.996 1.00 141.12 ? 624  THR B N   1 
ATOM   4843  C CA  . THR A 1 641  ? 182.280 187.059 247.461 1.00 141.12 ? 624  THR B CA  1 
ATOM   4844  C C   . THR A 1 641  ? 183.502 187.831 247.970 1.00 141.12 ? 624  THR B C   1 
ATOM   4845  O O   . THR A 1 641  ? 183.675 187.914 249.202 1.00 141.12 ? 624  THR B O   1 
ATOM   4846  C CB  . THR A 1 641  ? 180.957 187.746 247.814 1.00 141.12 ? 624  THR B CB  1 
ATOM   4847  O OG1 . THR A 1 641  ? 179.912 186.787 247.656 1.00 141.12 ? 624  THR B OG1 1 
ATOM   4848  C CG2 . THR A 1 641  ? 180.679 188.959 246.954 1.00 141.12 ? 624  THR B CG2 1 
ATOM   4849  N N   . ASP A 1 642  ? 184.309 188.383 247.061 1.00 140.99 ? 625  ASP B N   1 
ATOM   4850  C CA  . ASP A 1 642  ? 185.568 189.050 247.481 1.00 140.99 ? 625  ASP B CA  1 
ATOM   4851  C C   . ASP A 1 642  ? 185.644 190.454 246.888 1.00 140.99 ? 625  ASP B C   1 
ATOM   4852  O O   . ASP A 1 642  ? 186.573 191.192 247.255 1.00 140.99 ? 625  ASP B O   1 
ATOM   4853  C CB  . ASP A 1 642  ? 186.787 188.256 247.016 1.00 140.99 ? 625  ASP B CB  1 
ATOM   4854  C CG  . ASP A 1 642  ? 186.529 187.462 245.746 1.00 140.99 ? 625  ASP B CG  1 
ATOM   4855  O OD1 . ASP A 1 642  ? 185.814 187.981 244.867 1.00 140.99 ? 625  ASP B OD1 1 
ATOM   4856  O OD2 . ASP A 1 642  ? 187.041 186.330 245.647 1.00 140.99 ? 625  ASP B OD2 1 
ATOM   4857  N N   . LYS A 1 643  ? 184.698 190.804 246.016 1.00 125.37 ? 626  LYS B N   1 
ATOM   4858  C CA  . LYS A 1 643  ? 184.732 192.132 245.350 1.00 125.37 ? 626  LYS B CA  1 
ATOM   4859  C C   . LYS A 1 643  ? 184.776 193.213 246.429 1.00 125.37 ? 626  LYS B C   1 
ATOM   4860  O O   . LYS A 1 643  ? 185.093 194.365 246.094 1.00 125.37 ? 626  LYS B O   1 
ATOM   4861  C CB  . LYS A 1 643  ? 183.507 192.304 244.452 1.00 125.37 ? 626  LYS B CB  1 
ATOM   4862  C CG  . LYS A 1 643  ? 182.452 191.213 244.593 1.00 125.37 ? 626  LYS B CG  1 
ATOM   4863  C CD  . LYS A 1 643  ? 182.095 190.542 243.285 1.00 125.37 ? 626  LYS B CD  1 
ATOM   4864  C CE  . LYS A 1 643  ? 183.305 190.072 242.507 1.00 125.37 ? 626  LYS B CE  1 
ATOM   4865  N NZ  . LYS A 1 643  ? 184.113 189.103 243.284 1.00 125.37 ? 626  LYS B NZ  1 
ATOM   4866  N N   . ILE A 1 644  ? 184.477 192.842 247.672 1.00 115.74 ? 627  ILE B N   1 
ATOM   4867  C CA  . ILE A 1 644  ? 184.533 193.810 248.798 1.00 115.74 ? 627  ILE B CA  1 
ATOM   4868  C C   . ILE A 1 644  ? 185.971 194.319 248.934 1.00 115.74 ? 627  ILE B C   1 
ATOM   4869  O O   . ILE A 1 644  ? 186.891 193.662 248.414 1.00 115.74 ? 627  ILE B O   1 
ATOM   4870  C CB  . ILE A 1 644  ? 184.009 193.143 250.081 1.00 115.74 ? 627  ILE B CB  1 
ATOM   4871  C CG1 . ILE A 1 644  ? 183.790 194.157 251.206 1.00 115.74 ? 627  ILE B CG1 1 
ATOM   4872  C CG2 . ILE A 1 644  ? 184.926 192.008 250.504 1.00 115.74 ? 627  ILE B CG2 1 
ATOM   4873  C CD1 . ILE A 1 644  ? 182.936 195.337 250.813 1.00 115.74 ? 627  ILE B CD1 1 
ATOM   4874  N N   . ALA A 1 645  ? 186.151 195.462 249.598 1.00 105.94 ? 628  ALA B N   1 
ATOM   4875  C CA  . ALA A 1 645  ? 187.490 196.077 249.747 1.00 105.94 ? 628  ALA B CA  1 
ATOM   4876  C C   . ALA A 1 645  ? 188.198 195.570 251.009 1.00 105.94 ? 628  ALA B C   1 
ATOM   4877  O O   . ALA A 1 645  ? 187.983 196.159 252.086 1.00 105.94 ? 628  ALA B O   1 
ATOM   4878  C CB  . ALA A 1 645  ? 187.326 197.577 249.770 1.00 105.94 ? 628  ALA B CB  1 
ATOM   4879  N N   . ASP A 1 646  ? 188.973 194.496 250.885 1.00 96.21  ? 629  ASP B N   1 
ATOM   4880  C CA  . ASP A 1 646  ? 189.782 194.009 252.003 1.00 96.21  ? 629  ASP B CA  1 
ATOM   4881  C C   . ASP A 1 646  ? 188.940 193.409 253.127 1.00 96.21  ? 629  ASP B C   1 
ATOM   4882  O O   . ASP A 1 646  ? 189.393 193.324 254.273 1.00 96.21  ? 629  ASP B O   1 
ATOM   4883  C CB  . ASP A 1 646  ? 190.690 195.112 252.560 1.00 96.21  ? 629  ASP B CB  1 
ATOM   4884  C CG  . ASP A 1 646  ? 191.946 194.557 253.218 1.00 96.21  ? 629  ASP B CG  1 
ATOM   4885  O OD1 . ASP A 1 646  ? 191.970 193.359 253.569 1.00 96.21  ? 629  ASP B OD1 1 
ATOM   4886  O OD2 . ASP A 1 646  ? 192.915 195.322 253.388 1.00 96.21  ? 629  ASP B OD2 1 
ATOM   4887  N N   . ILE A 1 647  ? 187.714 192.993 252.828 1.00 93.53  ? 630  ILE B N   1 
ATOM   4888  C CA  . ILE A 1 647  ? 186.902 192.228 253.767 1.00 93.53  ? 630  ILE B CA  1 
ATOM   4889  C C   . ILE A 1 647  ? 186.786 190.840 253.148 1.00 93.53  ? 630  ILE B C   1 
ATOM   4890  O O   . ILE A 1 647  ? 185.744 190.182 253.237 1.00 93.53  ? 630  ILE B O   1 
ATOM   4891  C CB  . ILE A 1 647  ? 185.529 192.884 254.022 1.00 93.53  ? 630  ILE B CB  1 
ATOM   4892  C CG1 . ILE A 1 647  ? 185.678 194.362 254.387 1.00 93.53  ? 630  ILE B CG1 1 
ATOM   4893  C CG2 . ILE A 1 647  ? 184.833 192.232 255.205 1.00 93.53  ? 630  ILE B CG2 1 
ATOM   4894  C CD1 . ILE A 1 647  ? 186.757 194.655 255.407 1.00 93.53  ? 630  ILE B CD1 1 
ATOM   4895  N N   . THR A 1 648  ? 187.860 190.414 252.478 1.00 95.80  ? 631  THR B N   1 
ATOM   4896  C CA  . THR A 1 648  ? 187.852 189.195 251.673 1.00 95.80  ? 631  THR B CA  1 
ATOM   4897  C C   . THR A 1 648  ? 187.339 187.982 252.440 1.00 95.80  ? 631  THR B C   1 
ATOM   4898  O O   . THR A 1 648  ? 186.501 187.225 251.938 1.00 95.80  ? 631  THR B O   1 
ATOM   4899  C CB  . THR A 1 648  ? 189.264 188.926 251.147 1.00 95.80  ? 631  THR B CB  1 
ATOM   4900  O OG1 . THR A 1 648  ? 190.155 188.731 252.252 1.00 95.80  ? 631  THR B OG1 1 
ATOM   4901  C CG2 . THR A 1 648  ? 189.754 190.099 250.316 1.00 95.80  ? 631  THR B CG2 1 
ATOM   4902  N N   . ILE A 1 649  ? 187.829 187.794 253.667 1.00 92.58  ? 632  ILE B N   1 
ATOM   4903  C CA  . ILE A 1 649  ? 187.418 186.599 254.461 1.00 92.58  ? 632  ILE B CA  1 
ATOM   4904  C C   . ILE A 1 649  ? 186.220 186.978 255.331 1.00 92.58  ? 632  ILE B C   1 
ATOM   4905  O O   . ILE A 1 649  ? 186.449 187.497 256.428 1.00 92.58  ? 632  ILE B O   1 
ATOM   4906  C CB  . ILE A 1 649  ? 188.587 186.083 255.318 1.00 92.58  ? 632  ILE B CB  1 
ATOM   4907  C CG1 . ILE A 1 649  ? 189.873 185.955 254.499 1.00 92.58  ? 632  ILE B CG1 1 
ATOM   4908  C CG2 . ILE A 1 649  ? 188.221 184.775 255.999 1.00 92.58  ? 632  ILE B CG2 1 
ATOM   4909  C CD1 . ILE A 1 649  ? 190.628 184.672 254.749 1.00 92.58  ? 632  ILE B CD1 1 
ATOM   4910  N N   . ILE A 1 650  ? 185.001 186.759 254.836 1.00 87.28  ? 633  ILE B N   1 
ATOM   4911  C CA  . ILE A 1 650  ? 183.780 187.067 255.633 1.00 87.28  ? 633  ILE B CA  1 
ATOM   4912  C C   . ILE A 1 650  ? 183.280 185.764 256.254 1.00 87.28  ? 633  ILE B C   1 
ATOM   4913  O O   . ILE A 1 650  ? 183.035 184.818 255.495 1.00 87.28  ? 633  ILE B O   1 
ATOM   4914  C CB  . ILE A 1 650  ? 182.696 187.727 254.765 1.00 87.28  ? 633  ILE B CB  1 
ATOM   4915  C CG1 . ILE A 1 650  ? 183.055 189.168 254.402 1.00 87.28  ? 633  ILE B CG1 1 
ATOM   4916  C CG2 . ILE A 1 650  ? 181.340 187.644 255.446 1.00 87.28  ? 633  ILE B CG2 1 
ATOM   4917  C CD1 . ILE A 1 650  ? 182.196 189.754 253.308 1.00 87.28  ? 633  ILE B CD1 1 
ATOM   4918  N N   . ILE A 1 651  ? 183.162 185.720 257.581 1.00 87.28  ? 634  ILE B N   1 
ATOM   4919  C CA  . ILE A 1 651  ? 182.678 184.498 258.281 1.00 87.28  ? 634  ILE B CA  1 
ATOM   4920  C C   . ILE A 1 651  ? 181.168 184.628 258.441 1.00 87.28  ? 634  ILE B C   1 
ATOM   4921  O O   . ILE A 1 651  ? 180.728 185.509 259.185 1.00 87.28  ? 634  ILE B O   1 
ATOM   4922  C CB  . ILE A 1 651  ? 183.384 184.337 259.635 1.00 87.28  ? 634  ILE B CB  1 
ATOM   4923  C CG1 . ILE A 1 651  ? 184.879 184.063 259.461 1.00 87.28  ? 634  ILE B CG1 1 
ATOM   4924  C CG2 . ILE A 1 651  ? 182.708 183.260 260.462 1.00 87.28  ? 634  ILE B CG2 1 
ATOM   4925  C CD1 . ILE A 1 651  ? 185.179 182.796 258.701 1.00 87.28  ? 634  ILE B CD1 1 
ATOM   4926  N N   . PRO A 1 652  ? 180.358 183.791 257.770 1.00 94.22  ? 635  PRO B N   1 
ATOM   4927  C CA  . PRO A 1 652  ? 178.905 183.946 257.806 1.00 94.22  ? 635  PRO B CA  1 
ATOM   4928  C C   . PRO A 1 652  ? 178.228 183.678 259.156 1.00 94.22  ? 635  PRO B C   1 
ATOM   4929  O O   . PRO A 1 652  ? 177.397 184.468 259.540 1.00 94.22  ? 635  PRO B O   1 
ATOM   4930  C CB  . PRO A 1 652  ? 178.430 182.850 256.843 1.00 94.22  ? 635  PRO B CB  1 
ATOM   4931  C CG  . PRO A 1 652  ? 179.632 182.543 255.983 1.00 94.22  ? 635  PRO B CG  1 
ATOM   4932  C CD  . PRO A 1 652  ? 180.801 182.681 256.930 1.00 94.22  ? 635  PRO B CD  1 
ATOM   4933  N N   . TYR A 1 653  ? 178.589 182.596 259.842 1.00 85.53  ? 636  TYR B N   1 
ATOM   4934  C CA  . TYR A 1 653  ? 177.852 182.225 261.080 1.00 85.53  ? 636  TYR B CA  1 
ATOM   4935  C C   . TYR A 1 653  ? 177.880 183.353 262.096 1.00 85.53  ? 636  TYR B C   1 
ATOM   4936  O O   . TYR A 1 653  ? 177.099 183.289 263.054 1.00 85.53  ? 636  TYR B O   1 
ATOM   4937  C CB  . TYR A 1 653  ? 178.371 180.925 261.701 1.00 85.53  ? 636  TYR B CB  1 
ATOM   4938  C CG  . TYR A 1 653  ? 179.874 180.741 261.832 1.00 85.53  ? 636  TYR B CG  1 
ATOM   4939  C CD1 . TYR A 1 653  ? 180.567 181.239 262.927 1.00 85.53  ? 636  TYR B CD1 1 
ATOM   4940  C CD2 . TYR A 1 653  ? 180.588 180.024 260.882 1.00 85.53  ? 636  TYR B CD2 1 
ATOM   4941  C CE1 . TYR A 1 653  ? 181.932 181.055 263.058 1.00 85.53  ? 636  TYR B CE1 1 
ATOM   4942  C CE2 . TYR A 1 653  ? 181.953 179.835 261.001 1.00 85.53  ? 636  TYR B CE2 1 
ATOM   4943  C CZ  . TYR A 1 653  ? 182.626 180.351 262.092 1.00 85.53  ? 636  TYR B CZ  1 
ATOM   4944  O OH  . TYR A 1 653  ? 183.971 180.165 262.205 1.00 85.53  ? 636  TYR B OH  1 
ATOM   4945  N N   . ILE A 1 654  ? 178.721 184.366 261.910 1.00 84.64  ? 637  ILE B N   1 
ATOM   4946  C CA  . ILE A 1 654  ? 178.798 185.376 262.961 1.00 84.64  ? 637  ILE B CA  1 
ATOM   4947  C C   . ILE A 1 654  ? 177.443 186.048 263.152 1.00 84.64  ? 637  ILE B C   1 
ATOM   4948  O O   . ILE A 1 654  ? 177.052 186.380 264.277 1.00 84.64  ? 637  ILE B O   1 
ATOM   4949  C CB  . ILE A 1 654  ? 179.907 186.396 262.642 1.00 84.64  ? 637  ILE B CB  1 
ATOM   4950  C CG1 . ILE A 1 654  ? 181.266 185.849 263.075 1.00 84.64  ? 637  ILE B CG1 1 
ATOM   4951  C CG2 . ILE A 1 654  ? 179.645 187.729 263.322 1.00 84.64  ? 637  ILE B CG2 1 
ATOM   4952  C CD1 . ILE A 1 654  ? 182.415 186.769 262.764 1.00 84.64  ? 637  ILE B CD1 1 
ATOM   4953  N N   . GLY A 1 655  ? 176.705 186.246 262.062 1.00 86.42  ? 638  GLY B N   1 
ATOM   4954  C CA  . GLY A 1 655  ? 175.397 186.857 262.108 1.00 86.42  ? 638  GLY B CA  1 
ATOM   4955  C C   . GLY A 1 655  ? 174.468 186.225 263.125 1.00 86.42  ? 638  GLY B C   1 
ATOM   4956  O O   . GLY A 1 655  ? 174.085 186.853 264.116 1.00 86.42  ? 638  GLY B O   1 
ATOM   4957  N N   . PRO A 1 656  ? 174.085 184.966 262.904 1.00 81.93  ? 639  PRO B N   1 
ATOM   4958  C CA  . PRO A 1 656  ? 173.251 184.274 263.897 1.00 81.93  ? 639  PRO B CA  1 
ATOM   4959  C C   . PRO A 1 656  ? 173.947 184.047 265.227 1.00 81.93  ? 639  PRO B C   1 
ATOM   4960  O O   . PRO A 1 656  ? 173.268 183.758 266.220 1.00 81.93  ? 639  PRO B O   1 
ATOM   4961  C CB  . PRO A 1 656  ? 172.915 182.945 263.209 1.00 81.93  ? 639  PRO B CB  1 
ATOM   4962  C CG  . PRO A 1 656  ? 173.998 182.756 262.208 1.00 81.93  ? 639  PRO B CG  1 
ATOM   4963  C CD  . PRO A 1 656  ? 174.333 184.130 261.719 1.00 81.93  ? 639  PRO B CD  1 
ATOM   4964  N N   . ALA A 1 657  ? 175.277 184.155 265.278 1.00 78.28  ? 640  ALA B N   1 
ATOM   4965  C CA  . ALA A 1 657  ? 175.997 183.890 266.520 1.00 78.28  ? 640  ALA B CA  1 
ATOM   4966  C C   . ALA A 1 657  ? 175.696 184.939 267.581 1.00 78.28  ? 640  ALA B C   1 
ATOM   4967  O O   . ALA A 1 657  ? 175.551 184.607 268.762 1.00 78.28  ? 640  ALA B O   1 
ATOM   4968  C CB  . ALA A 1 657  ? 177.499 183.817 266.254 1.00 78.28  ? 640  ALA B CB  1 
ATOM   4969  N N   . LEU A 1 658  ? 175.609 186.210 267.188 1.00 80.29  ? 641  LEU B N   1 
ATOM   4970  C CA  . LEU A 1 658  ? 175.339 187.286 268.130 1.00 80.29  ? 641  LEU B CA  1 
ATOM   4971  C C   . LEU A 1 658  ? 174.132 188.131 267.762 1.00 80.29  ? 641  LEU B C   1 
ATOM   4972  O O   . LEU A 1 658  ? 173.832 189.089 268.482 1.00 80.29  ? 641  LEU B O   1 
ATOM   4973  C CB  . LEU A 1 658  ? 176.548 188.220 268.252 1.00 80.29  ? 641  LEU B CB  1 
ATOM   4974  C CG  . LEU A 1 658  ? 177.955 187.640 268.232 1.00 80.29  ? 641  LEU B CG  1 
ATOM   4975  C CD1 . LEU A 1 658  ? 178.959 188.771 268.098 1.00 80.29  ? 641  LEU B CD1 1 
ATOM   4976  C CD2 . LEU A 1 658  ? 178.225 186.822 269.473 1.00 80.29  ? 641  LEU B CD2 1 
ATOM   4977  N N   . ASN A 1 659  ? 173.435 187.815 266.670 1.00 86.38  ? 642  ASN B N   1 
ATOM   4978  C CA  . ASN A 1 659  ? 172.390 188.677 266.122 1.00 86.38  ? 642  ASN B CA  1 
ATOM   4979  C C   . ASN A 1 659  ? 173.001 190.054 265.824 1.00 86.38  ? 642  ASN B C   1 
ATOM   4980  O O   . ASN A 1 659  ? 172.798 191.054 266.506 1.00 86.38  ? 642  ASN B O   1 
ATOM   4981  C CB  . ASN A 1 659  ? 171.159 188.658 267.056 1.00 86.38  ? 642  ASN B CB  1 
ATOM   4982  C CG  . ASN A 1 659  ? 170.263 189.899 266.970 1.00 86.38  ? 642  ASN B CG  1 
ATOM   4983  O OD1 . ASN A 1 659  ? 170.599 190.986 267.431 1.00 86.38  ? 642  ASN B OD1 1 
ATOM   4984  N ND2 . ASN A 1 659  ? 169.093 189.716 266.373 1.00 86.38  ? 642  ASN B ND2 1 
ATOM   4985  N N   . ILE A 1 660  ? 173.888 190.028 264.837 1.00 89.83  ? 643  ILE B N   1 
ATOM   4986  C CA  . ILE A 1 660  ? 174.641 191.209 264.433 1.00 89.83  ? 643  ILE B CA  1 
ATOM   4987  C C   . ILE A 1 660  ? 173.773 192.013 263.477 1.00 89.83  ? 643  ILE B C   1 
ATOM   4988  O O   . ILE A 1 660  ? 173.421 191.535 262.394 1.00 89.83  ? 643  ILE B O   1 
ATOM   4989  C CB  . ILE A 1 660  ? 175.975 190.822 263.778 1.00 89.83  ? 643  ILE B CB  1 
ATOM   4990  C CG1 . ILE A 1 660  ? 177.003 190.437 264.840 1.00 89.83  ? 643  ILE B CG1 1 
ATOM   4991  C CG2 . ILE A 1 660  ? 176.510 191.971 262.946 1.00 89.83  ? 643  ILE B CG2 1 
ATOM   4992  C CD1 . ILE A 1 660  ? 177.284 191.530 265.838 1.00 89.83  ? 643  ILE B CD1 1 
ATOM   4993  N N   . GLY A 1 661  ? 173.417 193.229 263.881 1.00 97.74  ? 644  GLY B N   1 
ATOM   4994  C CA  . GLY A 1 661  ? 172.544 194.065 263.087 1.00 97.74  ? 644  GLY B CA  1 
ATOM   4995  C C   . GLY A 1 661  ? 171.082 193.684 263.137 1.00 97.74  ? 644  GLY B C   1 
ATOM   4996  O O   . GLY A 1 661  ? 170.282 194.279 262.404 1.00 97.74  ? 644  GLY B O   1 
ATOM   4997  N N   . ASN A 1 662  ? 170.716 192.700 263.961 1.00 98.62  ? 645  ASN B N   1 
ATOM   4998  C CA  . ASN A 1 662  ? 169.333 192.252 264.141 1.00 98.62  ? 645  ASN B CA  1 
ATOM   4999  C C   . ASN A 1 662  ? 168.778 191.563 262.892 1.00 98.62  ? 645  ASN B C   1 
ATOM   5000  O O   . ASN A 1 662  ? 167.621 191.765 262.522 1.00 98.62  ? 645  ASN B O   1 
ATOM   5001  C CB  . ASN A 1 662  ? 168.421 193.402 264.577 1.00 98.62  ? 645  ASN B CB  1 
ATOM   5002  C CG  . ASN A 1 662  ? 167.231 192.927 265.383 1.00 98.62  ? 645  ASN B CG  1 
ATOM   5003  O OD1 . ASN A 1 662  ? 167.161 191.764 265.778 1.00 98.62  ? 645  ASN B OD1 1 
ATOM   5004  N ND2 . ASN A 1 662  ? 166.288 193.827 265.635 1.00 98.62  ? 645  ASN B ND2 1 
ATOM   5005  N N   . MET A 1 663  ? 169.600 190.741 262.240 1.00 107.70 ? 646  MET B N   1 
ATOM   5006  C CA  . MET A 1 663  ? 169.108 189.740 261.304 1.00 107.70 ? 646  MET B CA  1 
ATOM   5007  C C   . MET A 1 663  ? 169.632 188.376 261.728 1.00 107.70 ? 646  MET B C   1 
ATOM   5008  O O   . MET A 1 663  ? 170.736 188.258 262.266 1.00 107.70 ? 646  MET B O   1 
ATOM   5009  C CB  . MET A 1 663  ? 169.512 190.003 259.839 1.00 107.70 ? 646  MET B CB  1 
ATOM   5010  C CG  . MET A 1 663  ? 170.916 190.529 259.606 1.00 107.70 ? 646  MET B CG  1 
ATOM   5011  S SD  . MET A 1 663  ? 171.199 192.165 260.283 1.00 107.70 ? 646  MET B SD  1 
ATOM   5012  C CE  . MET A 1 663  ? 170.203 193.158 259.175 1.00 107.70 ? 646  MET B CE  1 
ATOM   5013  N N   . LEU A 1 664  ? 168.824 187.344 261.487 1.00 118.21 ? 647  LEU B N   1 
ATOM   5014  C CA  . LEU A 1 664  ? 169.146 185.983 261.896 1.00 118.21 ? 647  LEU B CA  1 
ATOM   5015  C C   . LEU A 1 664  ? 169.414 185.068 260.704 1.00 118.21 ? 647  LEU B C   1 
ATOM   5016  O O   . LEU A 1 664  ? 169.161 183.863 260.771 1.00 118.21 ? 647  LEU B O   1 
ATOM   5017  C CB  . LEU A 1 664  ? 168.028 185.411 262.765 1.00 118.21 ? 647  LEU B CB  1 
ATOM   5018  N N   . TYR A 1 665  ? 169.916 185.623 259.603 1.00 117.55 ? 648  TYR B N   1 
ATOM   5019  C CA  . TYR A 1 665  ? 170.294 184.838 258.435 1.00 117.55 ? 648  TYR B CA  1 
ATOM   5020  C C   . TYR A 1 665  ? 171.726 185.175 258.051 1.00 117.55 ? 648  TYR B C   1 
ATOM   5021  O O   . TYR A 1 665  ? 172.089 186.353 257.973 1.00 117.55 ? 648  TYR B O   1 
ATOM   5022  C CB  . TYR A 1 665  ? 169.354 185.098 257.254 1.00 117.55 ? 648  TYR B CB  1 
ATOM   5023  C CG  . TYR A 1 665  ? 167.924 185.375 257.654 1.00 117.55 ? 648  TYR B CG  1 
ATOM   5024  C CD1 . TYR A 1 665  ? 167.156 184.400 258.276 1.00 117.55 ? 648  TYR B CD1 1 
ATOM   5025  C CD2 . TYR A 1 665  ? 167.341 186.611 257.407 1.00 117.55 ? 648  TYR B CD2 1 
ATOM   5026  C CE1 . TYR A 1 665  ? 165.846 184.648 258.642 1.00 117.55 ? 648  TYR B CE1 1 
ATOM   5027  C CE2 . TYR A 1 665  ? 166.033 186.869 257.769 1.00 117.55 ? 648  TYR B CE2 1 
ATOM   5028  C CZ  . TYR A 1 665  ? 165.290 185.885 258.386 1.00 117.55 ? 648  TYR B CZ  1 
ATOM   5029  O OH  . TYR A 1 665  ? 163.987 186.139 258.749 1.00 117.55 ? 648  TYR B OH  1 
ATOM   5030  N N   . LYS A 1 666  ? 172.534 184.139 257.815 1.00 110.43 ? 649  LYS B N   1 
ATOM   5031  C CA  . LYS A 1 666  ? 173.929 184.357 257.441 1.00 110.43 ? 649  LYS B CA  1 
ATOM   5032  C C   . LYS A 1 666  ? 174.039 185.082 256.105 1.00 110.43 ? 649  LYS B C   1 
ATOM   5033  O O   . LYS A 1 666  ? 174.878 185.977 255.943 1.00 110.43 ? 649  LYS B O   1 
ATOM   5034  C CB  . LYS A 1 666  ? 174.670 183.022 257.396 1.00 110.43 ? 649  LYS B CB  1 
ATOM   5035  C CG  . LYS A 1 666  ? 173.797 181.841 257.017 1.00 110.43 ? 649  LYS B CG  1 
ATOM   5036  C CD  . LYS A 1 666  ? 174.315 180.559 257.644 1.00 110.43 ? 649  LYS B CD  1 
ATOM   5037  C CE  . LYS A 1 666  ? 173.528 179.350 257.169 1.00 110.43 ? 649  LYS B CE  1 
ATOM   5038  N NZ  . LYS A 1 666  ? 173.897 178.121 257.924 1.00 110.43 ? 649  LYS B NZ  1 
ATOM   5039  N N   . ASP A 1 667  ? 173.205 184.705 255.134 1.00 111.84 ? 650  ASP B N   1 
ATOM   5040  C CA  . ASP A 1 667  ? 173.185 185.413 253.860 1.00 111.84 ? 650  ASP B CA  1 
ATOM   5041  C C   . ASP A 1 667  ? 172.797 186.869 254.082 1.00 111.84 ? 650  ASP B C   1 
ATOM   5042  O O   . ASP A 1 667  ? 173.413 187.782 253.516 1.00 111.84 ? 650  ASP B O   1 
ATOM   5043  C CB  . ASP A 1 667  ? 172.221 184.694 252.903 1.00 111.84 ? 650  ASP B CB  1 
ATOM   5044  C CG  . ASP A 1 667  ? 171.626 185.594 251.811 1.00 111.84 ? 650  ASP B CG  1 
ATOM   5045  O OD1 . ASP A 1 667  ? 172.182 186.658 251.467 1.00 111.84 ? 650  ASP B OD1 1 
ATOM   5046  O OD2 . ASP A 1 667  ? 170.559 185.218 251.283 1.00 111.84 ? 650  ASP B OD2 1 
ATOM   5047  N N   . ASP A 1 668  ? 171.791 187.105 254.928 1.00 108.17 ? 651  ASP B N   1 
ATOM   5048  C CA  . ASP A 1 668  ? 171.408 188.471 255.259 1.00 108.17 ? 651  ASP B CA  1 
ATOM   5049  C C   . ASP A 1 668  ? 172.546 189.205 255.955 1.00 108.17 ? 651  ASP B C   1 
ATOM   5050  O O   . ASP A 1 668  ? 172.753 190.402 255.726 1.00 108.17 ? 651  ASP B O   1 
ATOM   5051  C CB  . ASP A 1 668  ? 170.155 188.466 256.132 1.00 108.17 ? 651  ASP B CB  1 
ATOM   5052  C CG  . ASP A 1 668  ? 169.302 189.701 255.933 1.00 108.17 ? 651  ASP B CG  1 
ATOM   5053  O OD1 . ASP A 1 668  ? 169.829 190.714 255.428 1.00 108.17 ? 651  ASP B OD1 1 
ATOM   5054  O OD2 . ASP A 1 668  ? 168.103 189.659 256.280 1.00 108.17 ? 651  ASP B OD2 1 
ATOM   5055  N N   . PHE A 1 669  ? 173.298 188.504 256.808 1.00 98.64  ? 652  PHE B N   1 
ATOM   5056  C CA  . PHE A 1 669  ? 174.435 189.136 257.470 1.00 98.64  ? 652  PHE B CA  1 
ATOM   5057  C C   . PHE A 1 669  ? 175.494 189.564 256.464 1.00 98.64  ? 652  PHE B C   1 
ATOM   5058  O O   . PHE A 1 669  ? 176.028 190.672 256.554 1.00 98.64  ? 652  PHE B O   1 
ATOM   5059  C CB  . PHE A 1 669  ? 175.048 188.197 258.506 1.00 98.64  ? 652  PHE B CB  1 
ATOM   5060  C CG  . PHE A 1 669  ? 176.406 188.636 258.978 1.00 98.64  ? 652  PHE B CG  1 
ATOM   5061  C CD1 . PHE A 1 669  ? 176.569 189.848 259.626 1.00 98.64  ? 652  PHE B CD1 1 
ATOM   5062  C CD2 . PHE A 1 669  ? 177.519 187.846 258.760 1.00 98.64  ? 652  PHE B CD2 1 
ATOM   5063  C CE1 . PHE A 1 669  ? 177.814 190.259 260.054 1.00 98.64  ? 652  PHE B CE1 1 
ATOM   5064  C CE2 . PHE A 1 669  ? 178.766 188.254 259.187 1.00 98.64  ? 652  PHE B CE2 1 
ATOM   5065  C CZ  . PHE A 1 669  ? 178.912 189.461 259.835 1.00 98.64  ? 652  PHE B CZ  1 
ATOM   5066  N N   . VAL A 1 670  ? 175.818 188.696 255.503 1.00 97.42  ? 653  VAL B N   1 
ATOM   5067  C CA  . VAL A 1 670  ? 176.820 189.048 254.498 1.00 97.42  ? 653  VAL B CA  1 
ATOM   5068  C C   . VAL A 1 670  ? 176.333 190.213 253.647 1.00 97.42  ? 653  VAL B C   1 
ATOM   5069  O O   . VAL A 1 670  ? 177.100 191.128 253.316 1.00 97.42  ? 653  VAL B O   1 
ATOM   5070  C CB  . VAL A 1 670  ? 177.170 187.820 253.637 1.00 97.42  ? 653  VAL B CB  1 
ATOM   5071  C CG1 . VAL A 1 670  ? 178.183 188.192 252.571 1.00 97.42  ? 653  VAL B CG1 1 
ATOM   5072  C CG2 . VAL A 1 670  ? 177.707 186.700 254.508 1.00 97.42  ? 653  VAL B CG2 1 
ATOM   5073  N N   . GLY A 1 671  ? 175.052 190.196 253.277 1.00 95.00  ? 654  GLY B N   1 
ATOM   5074  C CA  . GLY A 1 671  ? 174.506 191.302 252.507 1.00 95.00  ? 654  GLY B CA  1 
ATOM   5075  C C   . GLY A 1 671  ? 174.582 192.618 253.254 1.00 95.00  ? 654  GLY B C   1 
ATOM   5076  O O   . GLY A 1 671  ? 174.993 193.640 252.699 1.00 95.00  ? 654  GLY B O   1 
ATOM   5077  N N   . ALA A 1 672  ? 174.201 192.607 254.534 1.00 90.34  ? 655  ALA B N   1 
ATOM   5078  C CA  . ALA A 1 672  ? 174.275 193.821 255.338 1.00 90.34  ? 655  ALA B CA  1 
ATOM   5079  C C   . ALA A 1 672  ? 175.716 194.272 255.516 1.00 90.34  ? 655  ALA B C   1 
ATOM   5080  O O   . ALA A 1 672  ? 176.001 195.474 255.518 1.00 90.34  ? 655  ALA B O   1 
ATOM   5081  C CB  . ALA A 1 672  ? 173.613 193.595 256.696 1.00 90.34  ? 655  ALA B CB  1 
ATOM   5082  N N   . LEU A 1 673  ? 176.638 193.322 255.674 1.00 87.03  ? 656  LEU B N   1 
ATOM   5083  C CA  . LEU A 1 673  ? 178.051 193.662 255.789 1.00 87.03  ? 656  LEU B CA  1 
ATOM   5084  C C   . LEU A 1 673  ? 178.530 194.403 254.552 1.00 87.03  ? 656  LEU B C   1 
ATOM   5085  O O   . LEU A 1 673  ? 179.113 195.487 254.649 1.00 87.03  ? 656  LEU B O   1 
ATOM   5086  C CB  . LEU A 1 673  ? 178.873 192.391 256.005 1.00 87.03  ? 656  LEU B CB  1 
ATOM   5087  C CG  . LEU A 1 673  ? 180.381 192.543 256.193 1.00 87.03  ? 656  LEU B CG  1 
ATOM   5088  C CD1 . LEU A 1 673  ? 180.697 193.679 257.145 1.00 87.03  ? 656  LEU B CD1 1 
ATOM   5089  C CD2 . LEU A 1 673  ? 180.985 191.244 256.689 1.00 87.03  ? 656  LEU B CD2 1 
ATOM   5090  N N   . ILE A 1 674  ? 178.267 193.841 253.372 1.00 83.21  ? 657  ILE B N   1 
ATOM   5091  C CA  . ILE A 1 674  ? 178.722 194.476 252.138 1.00 83.21  ? 657  ILE B CA  1 
ATOM   5092  C C   . ILE A 1 674  ? 178.034 195.822 251.947 1.00 83.21  ? 657  ILE B C   1 
ATOM   5093  O O   . ILE A 1 674  ? 178.642 196.786 251.468 1.00 83.21  ? 657  ILE B O   1 
ATOM   5094  C CB  . ILE A 1 674  ? 178.493 193.536 250.942 1.00 83.21  ? 657  ILE B CB  1 
ATOM   5095  C CG1 . ILE A 1 674  ? 179.562 192.446 250.918 1.00 83.21  ? 657  ILE B CG1 1 
ATOM   5096  C CG2 . ILE A 1 674  ? 178.522 194.304 249.641 1.00 83.21  ? 657  ILE B CG2 1 
ATOM   5097  C CD1 . ILE A 1 674  ? 179.269 191.330 249.948 1.00 83.21  ? 657  ILE B CD1 1 
ATOM   5098  N N   . PHE A 1 675  ? 176.763 195.919 252.343 1.00 79.74  ? 658  PHE B N   1 
ATOM   5099  C CA  . PHE A 1 675  ? 176.020 197.158 252.143 1.00 79.74  ? 658  PHE B CA  1 
ATOM   5100  C C   . PHE A 1 675  ? 176.524 198.277 253.048 1.00 79.74  ? 658  PHE B C   1 
ATOM   5101  O O   . PHE A 1 675  ? 176.669 199.420 252.601 1.00 79.74  ? 658  PHE B O   1 
ATOM   5102  C CB  . PHE A 1 675  ? 174.531 196.910 252.376 1.00 79.74  ? 658  PHE B CB  1 
ATOM   5103  C CG  . PHE A 1 675  ? 173.672 198.125 252.176 1.00 79.74  ? 658  PHE B CG  1 
ATOM   5104  C CD1 . PHE A 1 675  ? 173.919 199.005 251.139 1.00 79.74  ? 658  PHE B CD1 1 
ATOM   5105  C CD2 . PHE A 1 675  ? 172.616 198.388 253.030 1.00 79.74  ? 658  PHE B CD2 1 
ATOM   5106  C CE1 . PHE A 1 675  ? 173.129 200.123 250.957 1.00 79.74  ? 658  PHE B CE1 1 
ATOM   5107  C CE2 . PHE A 1 675  ? 171.824 199.505 252.853 1.00 79.74  ? 658  PHE B CE2 1 
ATOM   5108  C CZ  . PHE A 1 675  ? 172.082 200.373 251.815 1.00 79.74  ? 658  PHE B CZ  1 
ATOM   5109  N N   . SER A 1 676  ? 176.797 197.978 254.319 1.00 80.14  ? 659  SER B N   1 
ATOM   5110  C CA  . SER A 1 676  ? 177.017 199.016 255.318 1.00 80.14  ? 659  SER B CA  1 
ATOM   5111  C C   . SER A 1 676  ? 178.434 199.043 255.880 1.00 80.14  ? 659  SER B C   1 
ATOM   5112  O O   . SER A 1 676  ? 178.683 199.769 256.847 1.00 80.14  ? 659  SER B O   1 
ATOM   5113  C CB  . SER A 1 676  ? 176.017 198.860 256.465 1.00 80.14  ? 659  SER B CB  1 
ATOM   5114  O OG  . SER A 1 676  ? 174.688 199.044 256.012 1.00 80.14  ? 659  SER B OG  1 
ATOM   5115  N N   . GLY A 1 677  ? 179.370 198.291 255.307 1.00 80.43  ? 660  GLY B N   1 
ATOM   5116  C CA  . GLY A 1 677  ? 180.707 198.394 255.845 1.00 80.43  ? 660  GLY B CA  1 
ATOM   5117  C C   . GLY A 1 677  ? 180.824 197.672 257.178 1.00 80.43  ? 660  GLY B C   1 
ATOM   5118  O O   . GLY A 1 677  ? 180.066 196.756 257.497 1.00 80.43  ? 660  GLY B O   1 
ATOM   5119  N N   . ALA A 1 678  ? 181.797 198.114 257.969 1.00 74.80  ? 661  ALA B N   1 
ATOM   5120  C CA  . ALA A 1 678  ? 182.047 197.542 259.284 1.00 74.80  ? 661  ALA B CA  1 
ATOM   5121  C C   . ALA A 1 678  ? 181.249 198.225 260.384 1.00 74.80  ? 661  ALA B C   1 
ATOM   5122  O O   . ALA A 1 678  ? 181.495 197.962 261.564 1.00 74.80  ? 661  ALA B O   1 
ATOM   5123  C CB  . ALA A 1 678  ? 183.539 197.605 259.611 1.00 74.80  ? 661  ALA B CB  1 
ATOM   5124  N N   . VAL A 1 679  ? 180.305 199.096 260.025 1.00 74.65  ? 662  VAL B N   1 
ATOM   5125  C CA  . VAL A 1 679  ? 179.543 199.828 261.030 1.00 74.65  ? 662  VAL B CA  1 
ATOM   5126  C C   . VAL A 1 679  ? 178.641 198.886 261.821 1.00 74.65  ? 662  VAL B C   1 
ATOM   5127  O O   . VAL A 1 679  ? 178.470 199.048 263.035 1.00 74.65  ? 662  VAL B O   1 
ATOM   5128  C CB  . VAL A 1 679  ? 178.741 200.958 260.359 1.00 74.65  ? 662  VAL B CB  1 
ATOM   5129  C CG1 . VAL A 1 679  ? 177.498 201.294 261.163 1.00 74.65  ? 662  VAL B CG1 1 
ATOM   5130  C CG2 . VAL A 1 679  ? 179.611 202.186 260.190 1.00 74.65  ? 662  VAL B CG2 1 
ATOM   5131  N N   . ILE A 1 680  ? 178.067 197.881 261.156 1.00 79.99  ? 663  ILE B N   1 
ATOM   5132  C CA  . ILE A 1 680  ? 177.083 197.018 261.807 1.00 79.99  ? 663  ILE B CA  1 
ATOM   5133  C C   . ILE A 1 680  ? 177.695 196.246 262.969 1.00 79.99  ? 663  ILE B C   1 
ATOM   5134  O O   . ILE A 1 680  ? 176.993 195.892 263.923 1.00 79.99  ? 663  ILE B O   1 
ATOM   5135  C CB  . ILE A 1 680  ? 176.442 196.067 260.779 1.00 79.99  ? 663  ILE B CB  1 
ATOM   5136  C CG1 . ILE A 1 680  ? 177.486 195.114 260.203 1.00 79.99  ? 663  ILE B CG1 1 
ATOM   5137  C CG2 . ILE A 1 680  ? 175.782 196.861 259.668 1.00 79.99  ? 663  ILE B CG2 1 
ATOM   5138  C CD1 . ILE A 1 680  ? 176.932 194.178 259.171 1.00 79.99  ? 663  ILE B CD1 1 
ATOM   5139  N N   . LEU A 1 681  ? 178.996 195.959 262.909 1.00 74.30  ? 664  LEU B N   1 
ATOM   5140  C CA  . LEU A 1 681  ? 179.649 195.286 264.028 1.00 74.30  ? 664  LEU B CA  1 
ATOM   5141  C C   . LEU A 1 681  ? 179.666 196.167 265.270 1.00 74.30  ? 664  LEU B C   1 
ATOM   5142  O O   . LEU A 1 681  ? 179.482 195.675 266.389 1.00 74.30  ? 664  LEU B O   1 
ATOM   5143  C CB  . LEU A 1 681  ? 181.070 194.882 263.643 1.00 74.30  ? 664  LEU B CB  1 
ATOM   5144  C CG  . LEU A 1 681  ? 181.201 193.824 262.552 1.00 74.30  ? 664  LEU B CG  1 
ATOM   5145  C CD1 . LEU A 1 681  ? 182.656 193.447 262.357 1.00 74.30  ? 664  LEU B CD1 1 
ATOM   5146  C CD2 . LEU A 1 681  ? 180.378 192.605 262.907 1.00 74.30  ? 664  LEU B CD2 1 
ATOM   5147  N N   . LEU A 1 682  ? 179.889 197.465 265.095 1.00 70.78  ? 665  LEU B N   1 
ATOM   5148  C CA  . LEU A 1 682  ? 180.003 198.371 266.229 1.00 70.78  ? 665  LEU B CA  1 
ATOM   5149  C C   . LEU A 1 682  ? 178.669 198.491 266.955 1.00 70.78  ? 665  LEU B C   1 
ATOM   5150  O O   . LEU A 1 682  ? 177.618 198.637 266.326 1.00 70.78  ? 665  LEU B O   1 
ATOM   5151  C CB  . LEU A 1 682  ? 180.472 199.746 265.759 1.00 70.78  ? 665  LEU B CB  1 
ATOM   5152  C CG  . LEU A 1 682  ? 181.972 200.038 265.778 1.00 70.78  ? 665  LEU B CG  1 
ATOM   5153  C CD1 . LEU A 1 682  ? 182.768 198.910 265.146 1.00 70.78  ? 665  LEU B CD1 1 
ATOM   5154  C CD2 . LEU A 1 682  ? 182.250 201.348 265.073 1.00 70.78  ? 665  LEU B CD2 1 
ATOM   5155  N N   . GLU A 1 683  ? 178.714 198.426 268.287 1.00 75.03  ? 666  GLU B N   1 
ATOM   5156  C CA  . GLU A 1 683  ? 177.498 198.610 269.071 1.00 75.03  ? 666  GLU B CA  1 
ATOM   5157  C C   . GLU A 1 683  ? 177.098 200.078 269.128 1.00 75.03  ? 666  GLU B C   1 
ATOM   5158  O O   . GLU A 1 683  ? 175.907 200.403 269.098 1.00 75.03  ? 666  GLU B O   1 
ATOM   5159  C CB  . GLU A 1 683  ? 177.690 198.049 270.478 1.00 75.03  ? 666  GLU B CB  1 
ATOM   5160  C CG  . GLU A 1 683  ? 176.446 198.125 271.343 1.00 75.03  ? 666  GLU B CG  1 
ATOM   5161  C CD  . GLU A 1 683  ? 175.662 196.829 271.348 1.00 75.03  ? 666  GLU B CD  1 
ATOM   5162  O OE1 . GLU A 1 683  ? 176.180 195.818 270.830 1.00 75.03  ? 666  GLU B OE1 1 
ATOM   5163  O OE2 . GLU A 1 683  ? 174.528 196.820 271.870 1.00 75.03  ? 666  GLU B OE2 1 
ATOM   5164  N N   . PHE A 1 684  ? 178.076 200.975 269.215 1.00 71.47  ? 667  PHE B N   1 
ATOM   5165  C CA  . PHE A 1 684  ? 177.828 202.409 269.192 1.00 71.47  ? 667  PHE B CA  1 
ATOM   5166  C C   . PHE A 1 684  ? 178.806 203.069 268.234 1.00 71.47  ? 667  PHE B C   1 
ATOM   5167  O O   . PHE A 1 684  ? 179.971 202.673 268.152 1.00 71.47  ? 667  PHE B O   1 
ATOM   5168  C CB  . PHE A 1 684  ? 177.953 203.028 270.592 1.00 71.47  ? 667  PHE B CB  1 
ATOM   5169  C CG  . PHE A 1 684  ? 179.339 202.964 271.169 1.00 71.47  ? 667  PHE B CG  1 
ATOM   5170  C CD1 . PHE A 1 684  ? 179.796 201.813 271.785 1.00 71.47  ? 667  PHE B CD1 1 
ATOM   5171  C CD2 . PHE A 1 684  ? 180.179 204.061 271.111 1.00 71.47  ? 667  PHE B CD2 1 
ATOM   5172  C CE1 . PHE A 1 684  ? 181.064 201.755 272.320 1.00 71.47  ? 667  PHE B CE1 1 
ATOM   5173  C CE2 . PHE A 1 684  ? 181.449 204.007 271.644 1.00 71.47  ? 667  PHE B CE2 1 
ATOM   5174  C CZ  . PHE A 1 684  ? 181.891 202.853 272.249 1.00 71.47  ? 667  PHE B CZ  1 
ATOM   5175  N N   . ILE A 1 685  ? 178.326 204.071 267.506 1.00 72.77  ? 668  ILE B N   1 
ATOM   5176  C CA  . ILE A 1 685  ? 179.142 204.767 266.516 1.00 72.77  ? 668  ILE B CA  1 
ATOM   5177  C C   . ILE A 1 685  ? 179.947 205.864 267.201 1.00 72.77  ? 668  ILE B C   1 
ATOM   5178  O O   . ILE A 1 685  ? 179.363 206.764 267.820 1.00 72.77  ? 668  ILE B O   1 
ATOM   5179  C CB  . ILE A 1 685  ? 178.273 205.348 265.390 1.00 72.77  ? 668  ILE B CB  1 
ATOM   5180  C CG1 . ILE A 1 685  ? 177.497 204.233 264.688 1.00 72.77  ? 668  ILE B CG1 1 
ATOM   5181  C CG2 . ILE A 1 685  ? 179.130 206.115 264.400 1.00 72.77  ? 668  ILE B CG2 1 
ATOM   5182  C CD1 . ILE A 1 685  ? 178.351 203.054 264.294 1.00 72.77  ? 668  ILE B CD1 1 
ATOM   5183  N N   . PRO A 1 686  ? 181.275 205.831 267.127 1.00 71.01  ? 669  PRO B N   1 
ATOM   5184  C CA  . PRO A 1 686  ? 182.069 206.923 267.695 1.00 71.01  ? 669  PRO B CA  1 
ATOM   5185  C C   . PRO A 1 686  ? 181.830 208.224 266.950 1.00 71.01  ? 669  PRO B C   1 
ATOM   5186  O O   . PRO A 1 686  ? 181.584 208.242 265.742 1.00 71.01  ? 669  PRO B O   1 
ATOM   5187  C CB  . PRO A 1 686  ? 183.513 206.441 267.520 1.00 71.01  ? 669  PRO B CB  1 
ATOM   5188  C CG  . PRO A 1 686  ? 183.450 205.483 266.390 1.00 71.01  ? 669  PRO B CG  1 
ATOM   5189  C CD  . PRO A 1 686  ? 182.120 204.801 266.503 1.00 71.01  ? 669  PRO B CD  1 
ATOM   5190  N N   . GLU A 1 687  ? 181.906 209.325 267.691 1.00 75.89  ? 670  GLU B N   1 
ATOM   5191  C CA  . GLU A 1 687  ? 181.725 210.663 267.141 1.00 75.89  ? 670  GLU B CA  1 
ATOM   5192  C C   . GLU A 1 687  ? 183.086 211.345 267.098 1.00 75.89  ? 670  GLU B C   1 
ATOM   5193  O O   . GLU A 1 687  ? 183.640 211.703 268.142 1.00 75.89  ? 670  GLU B O   1 
ATOM   5194  C CB  . GLU A 1 687  ? 180.728 211.466 267.971 1.00 75.89  ? 670  GLU B CB  1 
ATOM   5195  C CG  . GLU A 1 687  ? 179.278 211.216 267.597 1.00 75.89  ? 670  GLU B CG  1 
ATOM   5196  C CD  . GLU A 1 687  ? 178.608 210.210 268.511 1.00 75.89  ? 670  GLU B CD  1 
ATOM   5197  O OE1 . GLU A 1 687  ? 179.324 209.374 269.100 1.00 75.89  ? 670  GLU B OE1 1 
ATOM   5198  O OE2 . GLU A 1 687  ? 177.366 210.254 268.639 1.00 75.89  ? 670  GLU B OE2 1 
ATOM   5199  N N   . ILE A 1 688  ? 183.617 211.527 265.893 1.00 73.31  ? 671  ILE B N   1 
ATOM   5200  C CA  . ILE A 1 688  ? 184.923 212.136 265.680 1.00 73.31  ? 671  ILE B CA  1 
ATOM   5201  C C   . ILE A 1 688  ? 184.717 213.451 264.942 1.00 73.31  ? 671  ILE B C   1 
ATOM   5202  O O   . ILE A 1 688  ? 184.062 213.485 263.894 1.00 73.31  ? 671  ILE B O   1 
ATOM   5203  C CB  . ILE A 1 688  ? 185.861 211.199 264.897 1.00 73.31  ? 671  ILE B CB  1 
ATOM   5204  C CG1 . ILE A 1 688  ? 187.077 211.964 264.381 1.00 73.31  ? 671  ILE B CG1 1 
ATOM   5205  C CG2 . ILE A 1 688  ? 185.115 210.522 263.758 1.00 73.31  ? 671  ILE B CG2 1 
ATOM   5206  C CD1 . ILE A 1 688  ? 188.018 212.391 265.474 1.00 73.31  ? 671  ILE B CD1 1 
ATOM   5207  N N   . ALA A 1 689  ? 185.265 214.532 265.493 1.00 73.49  ? 672  ALA B N   1 
ATOM   5208  C CA  . ALA A 1 689  ? 185.097 215.865 264.919 1.00 73.49  ? 672  ALA B CA  1 
ATOM   5209  C C   . ALA A 1 689  ? 186.398 216.633 265.087 1.00 73.49  ? 672  ALA B C   1 
ATOM   5210  O O   . ALA A 1 689  ? 186.786 216.962 266.212 1.00 73.49  ? 672  ALA B O   1 
ATOM   5211  C CB  . ALA A 1 689  ? 183.936 216.608 265.579 1.00 73.49  ? 672  ALA B CB  1 
ATOM   5212  N N   . ILE A 1 690  ? 187.066 216.919 263.975 1.00 69.60  ? 673  ILE B N   1 
ATOM   5213  C CA  . ILE A 1 690  ? 188.302 217.695 263.978 1.00 69.60  ? 673  ILE B CA  1 
ATOM   5214  C C   . ILE A 1 690  ? 187.932 219.164 263.802 1.00 69.60  ? 673  ILE B C   1 
ATOM   5215  O O   . ILE A 1 690  ? 187.246 219.502 262.825 1.00 69.60  ? 673  ILE B O   1 
ATOM   5216  C CB  . ILE A 1 690  ? 189.256 217.240 262.870 1.00 69.60  ? 673  ILE B CB  1 
ATOM   5217  C CG1 . ILE A 1 690  ? 189.453 215.729 262.915 1.00 69.60  ? 673  ILE B CG1 1 
ATOM   5218  C CG2 . ILE A 1 690  ? 190.592 217.934 263.017 1.00 69.60  ? 673  ILE B CG2 1 
ATOM   5219  C CD1 . ILE A 1 690  ? 189.904 215.227 264.246 1.00 69.60  ? 673  ILE B CD1 1 
ATOM   5220  N N   . PRO A 1 691  ? 188.348 220.052 264.698 1.00 74.70  ? 674  PRO B N   1 
ATOM   5221  C CA  . PRO A 1 691  ? 188.069 221.476 264.505 1.00 74.70  ? 674  PRO B CA  1 
ATOM   5222  C C   . PRO A 1 691  ? 188.870 222.034 263.341 1.00 74.70  ? 674  PRO B C   1 
ATOM   5223  O O   . PRO A 1 691  ? 189.844 221.440 262.876 1.00 74.70  ? 674  PRO B O   1 
ATOM   5224  C CB  . PRO A 1 691  ? 188.502 222.106 265.830 1.00 74.70  ? 674  PRO B CB  1 
ATOM   5225  C CG  . PRO A 1 691  ? 189.534 221.178 266.359 1.00 74.70  ? 674  PRO B CG  1 
ATOM   5226  C CD  . PRO A 1 691  ? 189.131 219.799 265.918 1.00 74.70  ? 674  PRO B CD  1 
ATOM   5227  N N   . VAL A 1 692  ? 188.430 223.197 262.860 1.00 74.20  ? 675  VAL B N   1 
ATOM   5228  C CA  . VAL A 1 692  ? 189.135 223.864 261.772 1.00 74.20  ? 675  VAL B CA  1 
ATOM   5229  C C   . VAL A 1 692  ? 190.539 224.211 262.240 1.00 74.20  ? 675  VAL B C   1 
ATOM   5230  O O   . VAL A 1 692  ? 190.718 224.990 263.183 1.00 74.20  ? 675  VAL B O   1 
ATOM   5231  C CB  . VAL A 1 692  ? 188.371 225.109 261.316 1.00 74.20  ? 675  VAL B CB  1 
ATOM   5232  C CG1 . VAL A 1 692  ? 188.874 225.568 259.960 1.00 74.20  ? 675  VAL B CG1 1 
ATOM   5233  C CG2 . VAL A 1 692  ? 186.881 224.826 261.267 1.00 74.20  ? 675  VAL B CG2 1 
ATOM   5234  N N   . LEU A 1 693  ? 191.542 223.631 261.585 1.00 70.09  ? 676  LEU B N   1 
ATOM   5235  C CA  . LEU A 1 693  ? 192.921 223.832 262.007 1.00 70.09  ? 676  LEU B CA  1 
ATOM   5236  C C   . LEU A 1 693  ? 193.304 225.301 261.897 1.00 70.09  ? 676  LEU B C   1 
ATOM   5237  O O   . LEU A 1 693  ? 192.856 226.012 260.994 1.00 70.09  ? 676  LEU B O   1 
ATOM   5238  C CB  . LEU A 1 693  ? 193.866 222.976 261.167 1.00 70.09  ? 676  LEU B CB  1 
ATOM   5239  C CG  . LEU A 1 693  ? 193.547 221.485 261.066 1.00 70.09  ? 676  LEU B CG  1 
ATOM   5240  C CD1 . LEU A 1 693  ? 194.664 220.755 260.347 1.00 70.09  ? 676  LEU B CD1 1 
ATOM   5241  C CD2 . LEU A 1 693  ? 193.319 220.889 262.434 1.00 70.09  ? 676  LEU B CD2 1 
ATOM   5242  N N   . GLY A 1 694  ? 194.133 225.756 262.830 1.00 73.46  ? 677  GLY B N   1 
ATOM   5243  C CA  . GLY A 1 694  ? 194.483 227.157 262.881 1.00 73.46  ? 677  GLY B CA  1 
ATOM   5244  C C   . GLY A 1 694  ? 195.358 227.585 261.721 1.00 73.46  ? 677  GLY B C   1 
ATOM   5245  O O   . GLY A 1 694  ? 195.955 226.776 261.012 1.00 73.46  ? 677  GLY B O   1 
ATOM   5246  N N   . THR A 1 695  ? 195.423 228.896 261.529 1.00 79.10  ? 678  THR B N   1 
ATOM   5247  C CA  . THR A 1 695  ? 196.223 229.495 260.474 1.00 79.10  ? 678  THR B CA  1 
ATOM   5248  C C   . THR A 1 695  ? 197.640 229.772 260.965 1.00 79.10  ? 678  THR B C   1 
ATOM   5249  O O   . THR A 1 695  ? 197.909 229.833 262.166 1.00 79.10  ? 678  THR B O   1 
ATOM   5250  C CB  . THR A 1 695  ? 195.579 230.791 259.982 1.00 79.10  ? 678  THR B CB  1 
ATOM   5251  O OG1 . THR A 1 695  ? 195.850 231.842 260.917 1.00 79.10  ? 678  THR B OG1 1 
ATOM   5252  C CG2 . THR A 1 695  ? 194.074 230.620 259.845 1.00 79.10  ? 678  THR B CG2 1 
ATOM   5253  N N   . PHE A 1 696  ? 198.549 229.945 260.010 1.00 72.50  ? 679  PHE B N   1 
ATOM   5254  C CA  . PHE A 1 696  ? 199.956 230.199 260.295 1.00 72.50  ? 679  PHE B CA  1 
ATOM   5255  C C   . PHE A 1 696  ? 200.265 231.666 260.033 1.00 72.50  ? 679  PHE B C   1 
ATOM   5256  O O   . PHE A 1 696  ? 200.184 232.126 258.890 1.00 72.50  ? 679  PHE B O   1 
ATOM   5257  C CB  . PHE A 1 696  ? 200.849 229.306 259.438 1.00 72.50  ? 679  PHE B CB  1 
ATOM   5258  C CG  . PHE A 1 696  ? 201.214 228.014 260.095 1.00 72.50  ? 679  PHE B CG  1 
ATOM   5259  C CD1 . PHE A 1 696  ? 200.287 227.001 260.219 1.00 72.50  ? 679  PHE B CD1 1 
ATOM   5260  C CD2 . PHE A 1 696  ? 202.482 227.813 260.587 1.00 72.50  ? 679  PHE B CD2 1 
ATOM   5261  C CE1 . PHE A 1 696  ? 200.623 225.812 260.825 1.00 72.50  ? 679  PHE B CE1 1 
ATOM   5262  C CE2 . PHE A 1 696  ? 202.822 226.627 261.192 1.00 72.50  ? 679  PHE B CE2 1 
ATOM   5263  C CZ  . PHE A 1 696  ? 201.892 225.625 261.310 1.00 72.50  ? 679  PHE B CZ  1 
ATOM   5264  N N   . ALA A 1 697  ? 200.627 232.393 261.086 1.00 78.44  ? 680  ALA B N   1 
ATOM   5265  C CA  . ALA A 1 697  ? 200.954 233.809 260.973 1.00 78.44  ? 680  ALA B CA  1 
ATOM   5266  C C   . ALA A 1 697  ? 202.453 233.959 260.752 1.00 78.44  ? 680  ALA B C   1 
ATOM   5267  O O   . ALA A 1 697  ? 203.252 233.617 261.630 1.00 78.44  ? 680  ALA B O   1 
ATOM   5268  C CB  . ALA A 1 697  ? 200.514 234.570 262.222 1.00 78.44  ? 680  ALA B CB  1 
ATOM   5269  N N   . LEU A 1 698  ? 202.832 234.482 259.591 1.00 73.21  ? 681  LEU B N   1 
ATOM   5270  C CA  . LEU A 1 698  ? 204.230 234.594 259.199 1.00 73.21  ? 681  LEU B CA  1 
ATOM   5271  C C   . LEU A 1 698  ? 204.723 236.012 259.438 1.00 73.21  ? 681  LEU B C   1 
ATOM   5272  O O   . LEU A 1 698  ? 204.105 236.974 258.975 1.00 73.21  ? 681  LEU B O   1 
ATOM   5273  C CB  . LEU A 1 698  ? 204.410 234.231 257.728 1.00 73.21  ? 681  LEU B CB  1 
ATOM   5274  C CG  . LEU A 1 698  ? 204.556 232.755 257.382 1.00 73.21  ? 681  LEU B CG  1 
ATOM   5275  C CD1 . LEU A 1 698  ? 205.121 232.646 255.999 1.00 73.21  ? 681  LEU B CD1 1 
ATOM   5276  C CD2 . LEU A 1 698  ? 205.449 232.056 258.370 1.00 73.21  ? 681  LEU B CD2 1 
ATOM   5277  N N   . VAL A 1 699  ? 205.830 236.137 260.148 1.00 77.09  ? 682  VAL B N   1 
ATOM   5278  C CA  . VAL A 1 699  ? 206.440 237.437 260.394 1.00 77.09  ? 682  VAL B CA  1 
ATOM   5279  C C   . VAL A 1 699  ? 207.404 237.743 259.259 1.00 77.09  ? 682  VAL B C   1 
ATOM   5280  O O   . VAL A 1 699  ? 208.052 236.843 258.713 1.00 77.09  ? 682  VAL B O   1 
ATOM   5281  C CB  . VAL A 1 699  ? 207.149 237.467 261.762 1.00 77.09  ? 682  VAL B CB  1 
ATOM   5282  C CG1 . VAL A 1 699  ? 208.285 236.464 261.801 1.00 77.09  ? 682  VAL B CG1 1 
ATOM   5283  C CG2 . VAL A 1 699  ? 207.654 238.867 262.073 1.00 77.09  ? 682  VAL B CG2 1 
ATOM   5284  N N   . SER A 1 700  ? 207.481 239.013 258.882 1.00 81.59  ? 683  SER B N   1 
ATOM   5285  C CA  . SER A 1 700  ? 208.369 239.469 257.824 1.00 81.59  ? 683  SER B CA  1 
ATOM   5286  C C   . SER A 1 700  ? 209.499 240.279 258.437 1.00 81.59  ? 683  SER B C   1 
ATOM   5287  O O   . SER A 1 700  ? 209.255 241.171 259.256 1.00 81.59  ? 683  SER B O   1 
ATOM   5288  C CB  . SER A 1 700  ? 207.611 240.307 256.794 1.00 81.59  ? 683  SER B CB  1 
ATOM   5289  O OG  . SER A 1 700  ? 207.042 241.457 257.394 1.00 81.59  ? 683  SER B OG  1 
ATOM   5290  N N   . TYR A 1 701  ? 210.728 239.964 258.047 1.00 83.21  ? 684  TYR B N   1 
ATOM   5291  C CA  . TYR A 1 701  ? 211.906 240.681 258.509 1.00 83.21  ? 684  TYR B CA  1 
ATOM   5292  C C   . TYR A 1 701  ? 212.347 241.663 257.436 1.00 83.21  ? 684  TYR B C   1 
ATOM   5293  O O   . TYR A 1 701  ? 212.351 241.336 256.247 1.00 83.21  ? 684  TYR B O   1 
ATOM   5294  C CB  . TYR A 1 701  ? 213.039 239.710 258.837 1.00 83.21  ? 684  TYR B CB  1 
ATOM   5295  C CG  . TYR A 1 701  ? 212.652 238.665 259.853 1.00 83.21  ? 684  TYR B CG  1 
ATOM   5296  C CD1 . TYR A 1 701  ? 212.619 238.966 261.205 1.00 83.21  ? 684  TYR B CD1 1 
ATOM   5297  C CD2 . TYR A 1 701  ? 212.310 237.381 259.457 1.00 83.21  ? 684  TYR B CD2 1 
ATOM   5298  C CE1 . TYR A 1 701  ? 212.260 238.016 262.137 1.00 83.21  ? 684  TYR B CE1 1 
ATOM   5299  C CE2 . TYR A 1 701  ? 211.951 236.424 260.381 1.00 83.21  ? 684  TYR B CE2 1 
ATOM   5300  C CZ  . TYR A 1 701  ? 211.927 236.747 261.720 1.00 83.21  ? 684  TYR B CZ  1 
ATOM   5301  O OH  . TYR A 1 701  ? 211.570 235.798 262.648 1.00 83.21  ? 684  TYR B OH  1 
ATOM   5302  N N   . ILE A 1 702  ? 212.711 242.867 257.856 1.00 87.81  ? 685  ILE B N   1 
ATOM   5303  C CA  . ILE A 1 702  ? 213.021 243.926 256.904 1.00 87.81  ? 685  ILE B CA  1 
ATOM   5304  C C   . ILE A 1 702  ? 214.425 243.716 256.346 1.00 87.81  ? 685  ILE B C   1 
ATOM   5305  O O   . ILE A 1 702  ? 215.388 243.514 257.096 1.00 87.81  ? 685  ILE B O   1 
ATOM   5306  C CB  . ILE A 1 702  ? 212.842 245.313 257.554 1.00 87.81  ? 685  ILE B CB  1 
ATOM   5307  C CG1 . ILE A 1 702  ? 212.484 246.360 256.496 1.00 87.81  ? 685  ILE B CG1 1 
ATOM   5308  C CG2 . ILE A 1 702  ? 214.052 245.743 258.382 1.00 87.81  ? 685  ILE B CG2 1 
ATOM   5309  C CD1 . ILE A 1 702  ? 211.060 246.258 255.997 1.00 87.81  ? 685  ILE B CD1 1 
ATOM   5310  N N   . ALA A 1 703  ? 214.526 243.697 255.017 1.00 86.30  ? 686  ALA B N   1 
ATOM   5311  C CA  . ALA A 1 703  ? 215.792 243.630 254.288 1.00 86.30  ? 686  ALA B CA  1 
ATOM   5312  C C   . ALA A 1 703  ? 216.690 242.497 254.794 1.00 86.30  ? 686  ALA B C   1 
ATOM   5313  O O   . ALA A 1 703  ? 217.833 242.705 255.204 1.00 86.30  ? 686  ALA B O   1 
ATOM   5314  C CB  . ALA A 1 703  ? 216.517 244.975 254.353 1.00 86.30  ? 686  ALA B CB  1 
ATOM   5315  N N   . ASN A 1 704  ? 216.155 241.279 254.751 1.00 84.25  ? 687  ASN B N   1 
ATOM   5316  C CA  . ASN A 1 704  ? 216.894 240.100 255.175 1.00 84.25  ? 687  ASN B CA  1 
ATOM   5317  C C   . ASN A 1 704  ? 216.779 239.011 254.119 1.00 84.25  ? 687  ASN B C   1 
ATOM   5318  O O   . ASN A 1 704  ? 215.747 238.875 253.458 1.00 84.25  ? 687  ASN B O   1 
ATOM   5319  C CB  . ASN A 1 704  ? 216.392 239.578 256.519 1.00 84.25  ? 687  ASN B CB  1 
ATOM   5320  C CG  . ASN A 1 704  ? 217.417 238.726 257.223 1.00 84.25  ? 687  ASN B CG  1 
ATOM   5321  O OD1 . ASN A 1 704  ? 217.662 237.584 256.840 1.00 84.25  ? 687  ASN B OD1 1 
ATOM   5322  N ND2 . ASN A 1 704  ? 218.033 239.282 258.258 1.00 84.25  ? 687  ASN B ND2 1 
ATOM   5323  N N   . LYS A 1 705  ? 217.848 238.226 253.972 1.00 75.06  ? 688  LYS B N   1 
ATOM   5324  C CA  . LYS A 1 705  ? 217.946 237.249 252.896 1.00 75.06  ? 688  LYS B CA  1 
ATOM   5325  C C   . LYS A 1 705  ? 218.016 235.802 253.360 1.00 75.06  ? 688  LYS B C   1 
ATOM   5326  O O   . LYS A 1 705  ? 217.565 234.919 252.628 1.00 75.06  ? 688  LYS B O   1 
ATOM   5327  C CB  . LYS A 1 705  ? 219.173 237.543 252.020 1.00 75.06  ? 688  LYS B CB  1 
ATOM   5328  C CG  . LYS A 1 705  ? 218.940 237.332 250.532 1.00 75.06  ? 688  LYS B CG  1 
ATOM   5329  C CD  . LYS A 1 705  ? 219.246 235.899 250.116 1.00 75.06  ? 688  LYS B CD  1 
ATOM   5330  C CE  . LYS A 1 705  ? 219.272 235.746 248.604 1.00 75.06  ? 688  LYS B CE  1 
ATOM   5331  N NZ  . LYS A 1 705  ? 219.461 234.328 248.196 1.00 75.06  ? 688  LYS B NZ  1 
ATOM   5332  N N   . VAL A 1 706  ? 218.568 235.527 254.537 1.00 78.21  ? 689  VAL B N   1 
ATOM   5333  C CA  . VAL A 1 706  ? 218.676 234.163 255.039 1.00 78.21  ? 689  VAL B CA  1 
ATOM   5334  C C   . VAL A 1 706  ? 217.506 233.798 255.942 1.00 78.21  ? 689  VAL B C   1 
ATOM   5335  O O   . VAL A 1 706  ? 217.005 232.675 255.885 1.00 78.21  ? 689  VAL B O   1 
ATOM   5336  C CB  . VAL A 1 706  ? 220.021 233.959 255.769 1.00 78.21  ? 689  VAL B CB  1 
ATOM   5337  C CG1 . VAL A 1 706  ? 221.136 233.713 254.768 1.00 78.21  ? 689  VAL B CG1 1 
ATOM   5338  C CG2 . VAL A 1 706  ? 220.339 235.158 256.646 1.00 78.21  ? 689  VAL B CG2 1 
ATOM   5339  N N   . LEU A 1 707  ? 217.057 234.733 256.782 1.00 76.71  ? 690  LEU B N   1 
ATOM   5340  C CA  . LEU A 1 707  ? 216.008 234.417 257.744 1.00 76.71  ? 690  LEU B CA  1 
ATOM   5341  C C   . LEU A 1 707  ? 214.689 234.081 257.062 1.00 76.71  ? 690  LEU B C   1 
ATOM   5342  O O   . LEU A 1 707  ? 213.924 233.258 257.574 1.00 76.71  ? 690  LEU B O   1 
ATOM   5343  C CB  . LEU A 1 707  ? 215.823 235.576 258.721 1.00 76.71  ? 690  LEU B CB  1 
ATOM   5344  C CG  . LEU A 1 707  ? 217.041 235.911 259.580 1.00 76.71  ? 690  LEU B CG  1 
ATOM   5345  C CD1 . LEU A 1 707  ? 216.735 237.046 260.539 1.00 76.71  ? 690  LEU B CD1 1 
ATOM   5346  C CD2 . LEU A 1 707  ? 217.498 234.685 260.336 1.00 76.71  ? 690  LEU B CD2 1 
ATOM   5347  N N   . THR A 1 708  ? 214.394 234.708 255.923 1.00 72.24  ? 691  THR B N   1 
ATOM   5348  C CA  . THR A 1 708  ? 213.133 234.430 255.241 1.00 72.24  ? 691  THR B CA  1 
ATOM   5349  C C   . THR A 1 708  ? 213.092 233.002 254.711 1.00 72.24  ? 691  THR B C   1 
ATOM   5350  O O   . THR A 1 708  ? 212.053 232.332 254.786 1.00 72.24  ? 691  THR B O   1 
ATOM   5351  C CB  . THR A 1 708  ? 212.915 235.432 254.114 1.00 72.24  ? 691  THR B CB  1 
ATOM   5352  O OG1 . THR A 1 708  ? 213.577 234.970 252.932 1.00 72.24  ? 691  THR B OG1 1 
ATOM   5353  C CG2 . THR A 1 708  ? 213.477 236.784 254.502 1.00 72.24  ? 691  THR B CG2 1 
ATOM   5354  N N   . VAL A 1 709  ? 214.210 232.518 254.170 1.00 73.90  ? 692  VAL B N   1 
ATOM   5355  C CA  . VAL A 1 709  ? 214.276 231.122 253.750 1.00 73.90  ? 692  VAL B CA  1 
ATOM   5356  C C   . VAL A 1 709  ? 214.085 230.208 254.951 1.00 73.90  ? 692  VAL B C   1 
ATOM   5357  O O   . VAL A 1 709  ? 213.457 229.144 254.853 1.00 73.90  ? 692  VAL B O   1 
ATOM   5358  C CB  . VAL A 1 709  ? 215.603 230.840 253.023 1.00 73.90  ? 692  VAL B CB  1 
ATOM   5359  C CG1 . VAL A 1 709  ? 215.568 229.469 252.373 1.00 73.90  ? 692  VAL B CG1 1 
ATOM   5360  C CG2 . VAL A 1 709  ? 215.880 231.920 251.991 1.00 73.90  ? 692  VAL B CG2 1 
ATOM   5361  N N   . GLN A 1 710  ? 214.616 230.612 256.107 1.00 77.50  ? 693  GLN B N   1 
ATOM   5362  C CA  . GLN A 1 710  ? 214.389 229.853 257.331 1.00 77.50  ? 693  GLN B CA  1 
ATOM   5363  C C   . GLN A 1 710  ? 212.912 229.833 257.697 1.00 77.50  ? 693  GLN B C   1 
ATOM   5364  O O   . GLN A 1 710  ? 212.401 228.814 258.165 1.00 77.50  ? 693  GLN B O   1 
ATOM   5365  C CB  . GLN A 1 710  ? 215.220 230.433 258.474 1.00 77.50  ? 693  GLN B CB  1 
ATOM   5366  C CG  . GLN A 1 710  ? 216.543 229.723 258.699 1.00 77.50  ? 693  GLN B CG  1 
ATOM   5367  C CD  . GLN A 1 710  ? 217.319 230.304 259.863 1.00 77.50  ? 693  GLN B CD  1 
ATOM   5368  O OE1 . GLN A 1 710  ? 216.736 230.776 260.838 1.00 77.50  ? 693  GLN B OE1 1 
ATOM   5369  N NE2 . GLN A 1 710  ? 218.642 230.279 259.762 1.00 77.50  ? 693  GLN B NE2 1 
ATOM   5370  N N   . THR A 1 711  ? 212.210 230.952 257.498 1.00 71.91  ? 694  THR B N   1 
ATOM   5371  C CA  . THR A 1 711  ? 210.778 230.976 257.784 1.00 71.91  ? 694  THR B CA  1 
ATOM   5372  C C   . THR A 1 711  ? 210.017 230.038 256.859 1.00 71.91  ? 694  THR B C   1 
ATOM   5373  O O   . THR A 1 711  ? 209.093 229.344 257.292 1.00 71.91  ? 694  THR B O   1 
ATOM   5374  C CB  . THR A 1 711  ? 210.225 232.395 257.665 1.00 71.91  ? 694  THR B CB  1 
ATOM   5375  O OG1 . THR A 1 711  ? 210.506 232.906 256.360 1.00 71.91  ? 694  THR B OG1 1 
ATOM   5376  C CG2 . THR A 1 711  ? 210.847 233.304 258.704 1.00 71.91  ? 694  THR B CG2 1 
ATOM   5377  N N   . ILE A 1 712  ? 210.388 230.006 255.578 1.00 71.02  ? 695  ILE B N   1 
ATOM   5378  C CA  . ILE A 1 712  ? 209.723 229.098 254.641 1.00 71.02  ? 695  ILE B CA  1 
ATOM   5379  C C   . ILE A 1 712  ? 209.969 227.644 255.041 1.00 71.02  ? 695  ILE B C   1 
ATOM   5380  O O   . ILE A 1 712  ? 209.047 226.813 255.058 1.00 71.02  ? 695  ILE B O   1 
ATOM   5381  C CB  . ILE A 1 712  ? 210.192 229.371 253.202 1.00 71.02  ? 695  ILE B CB  1 
ATOM   5382  C CG1 . ILE A 1 712  ? 210.033 230.849 252.851 1.00 71.02  ? 695  ILE B CG1 1 
ATOM   5383  C CG2 . ILE A 1 712  ? 209.409 228.519 252.223 1.00 71.02  ? 695  ILE B CG2 1 
ATOM   5384  C CD1 . ILE A 1 712  ? 208.634 231.360 253.003 1.00 71.02  ? 695  ILE B CD1 1 
ATOM   5385  N N   . ASP A 1 713  ? 211.223 227.318 255.365 1.00 78.59  ? 696  ASP B N   1 
ATOM   5386  C CA  . ASP A 1 713  ? 211.560 225.960 255.781 1.00 78.59  ? 696  ASP B CA  1 
ATOM   5387  C C   . ASP A 1 713  ? 210.798 225.593 257.050 1.00 78.59  ? 696  ASP B C   1 
ATOM   5388  O O   . ASP A 1 713  ? 210.251 224.488 257.159 1.00 78.59  ? 696  ASP B O   1 
ATOM   5389  C CB  . ASP A 1 713  ? 213.082 225.864 255.969 1.00 78.59  ? 696  ASP B CB  1 
ATOM   5390  C CG  . ASP A 1 713  ? 213.551 224.618 256.741 1.00 78.59  ? 696  ASP B CG  1 
ATOM   5391  O OD1 . ASP A 1 713  ? 212.755 223.758 257.167 1.00 78.59  ? 696  ASP B OD1 1 
ATOM   5392  O OD2 . ASP A 1 713  ? 214.784 224.470 256.867 1.00 78.59  ? 696  ASP B OD2 1 
ATOM   5393  N N   . ASN A 1 714  ? 210.732 226.519 258.008 1.00 77.21  ? 697  ASN B N   1 
ATOM   5394  C CA  . ASN A 1 714  ? 209.999 226.274 259.242 1.00 77.21  ? 697  ASN B CA  1 
ATOM   5395  C C   . ASN A 1 714  ? 208.520 226.052 258.968 1.00 77.21  ? 697  ASN B C   1 
ATOM   5396  O O   . ASN A 1 714  ? 207.890 225.199 259.597 1.00 77.21  ? 697  ASN B O   1 
ATOM   5397  C CB  . ASN A 1 714  ? 210.192 227.444 260.203 1.00 77.21  ? 697  ASN B CB  1 
ATOM   5398  C CG  . ASN A 1 714  ? 211.515 227.387 260.928 1.00 77.21  ? 697  ASN B CG  1 
ATOM   5399  O OD1 . ASN A 1 714  ? 212.553 227.114 260.329 1.00 77.21  ? 697  ASN B OD1 1 
ATOM   5400  N ND2 . ASN A 1 714  ? 211.487 227.644 262.228 1.00 77.21  ? 697  ASN B ND2 1 
ATOM   5401  N N   . ALA A 1 715  ? 207.945 226.824 258.045 1.00 72.89  ? 698  ALA B N   1 
ATOM   5402  C CA  . ALA A 1 715  ? 206.538 226.645 257.712 1.00 72.89  ? 698  ALA B CA  1 
ATOM   5403  C C   . ALA A 1 715  ? 206.281 225.257 257.152 1.00 72.89  ? 698  ALA B C   1 
ATOM   5404  O O   . ALA A 1 715  ? 205.320 224.588 257.548 1.00 72.89  ? 698  ALA B O   1 
ATOM   5405  C CB  . ALA A 1 715  ? 206.089 227.718 256.723 1.00 72.89  ? 698  ALA B CB  1 
ATOM   5406  N N   . LEU A 1 716  ? 207.138 224.796 256.241 1.00 70.98  ? 699  LEU B N   1 
ATOM   5407  C CA  . LEU A 1 716  ? 206.946 223.457 255.687 1.00 70.98  ? 699  LEU B CA  1 
ATOM   5408  C C   . LEU A 1 716  ? 207.117 222.381 256.760 1.00 70.98  ? 699  LEU B C   1 
ATOM   5409  O O   . LEU A 1 716  ? 206.345 221.409 256.817 1.00 70.98  ? 699  LEU B O   1 
ATOM   5410  C CB  . LEU A 1 716  ? 207.910 223.230 254.525 1.00 70.98  ? 699  LEU B CB  1 
ATOM   5411  C CG  . LEU A 1 716  ? 207.743 224.172 253.329 1.00 70.98  ? 699  LEU B CG  1 
ATOM   5412  C CD1 . LEU A 1 716  ? 208.390 223.579 252.092 1.00 70.98  ? 699  LEU B CD1 1 
ATOM   5413  C CD2 . LEU A 1 716  ? 206.278 224.477 253.069 1.00 70.98  ? 699  LEU B CD2 1 
ATOM   5414  N N   . SER A 1 717  ? 208.117 222.545 257.629 1.00 74.52  ? 700  SER B N   1 
ATOM   5415  C CA  . SER A 1 717  ? 208.338 221.570 258.692 1.00 74.52  ? 700  SER B CA  1 
ATOM   5416  C C   . SER A 1 717  ? 207.153 221.514 259.649 1.00 74.52  ? 700  SER B C   1 
ATOM   5417  O O   . SER A 1 717  ? 206.705 220.428 260.032 1.00 74.52  ? 700  SER B O   1 
ATOM   5418  C CB  . SER A 1 717  ? 209.620 221.905 259.449 1.00 74.52  ? 700  SER B CB  1 
ATOM   5419  O OG  . SER A 1 717  ? 209.395 222.950 260.378 1.00 74.52  ? 700  SER B OG  1 
ATOM   5420  N N   . LYS A 1 718  ? 206.625 222.676 260.039 1.00 74.89  ? 701  LYS B N   1 
ATOM   5421  C CA  . LYS A 1 718  ? 205.469 222.706 260.926 1.00 74.89  ? 701  LYS B CA  1 
ATOM   5422  C C   . LYS A 1 718  ? 204.224 222.169 260.238 1.00 74.89  ? 701  LYS B C   1 
ATOM   5423  O O   . LYS A 1 718  ? 203.347 221.612 260.902 1.00 74.89  ? 701  LYS B O   1 
ATOM   5424  C CB  . LYS A 1 718  ? 205.229 224.126 261.431 1.00 74.89  ? 701  LYS B CB  1 
ATOM   5425  C CG  . LYS A 1 718  ? 206.360 224.681 262.276 1.00 74.89  ? 701  LYS B CG  1 
ATOM   5426  C CD  . LYS A 1 718  ? 206.571 223.855 263.525 1.00 74.89  ? 701  LYS B CD  1 
ATOM   5427  C CE  . LYS A 1 718  ? 205.589 224.255 264.607 1.00 74.89  ? 701  LYS B CE  1 
ATOM   5428  N NZ  . LYS A 1 718  ? 205.680 225.710 264.898 1.00 74.89  ? 701  LYS B NZ  1 
ATOM   5429  N N   . ARG A 1 719  ? 204.125 222.327 258.917 1.00 70.93  ? 702  ARG B N   1 
ATOM   5430  C CA  . ARG A 1 719  ? 203.059 221.666 258.171 1.00 70.93  ? 702  ARG B CA  1 
ATOM   5431  C C   . ARG A 1 719  ? 203.137 220.154 258.340 1.00 70.93  ? 702  ARG B C   1 
ATOM   5432  O O   . ARG A 1 719  ? 202.128 219.486 258.614 1.00 70.93  ? 702  ARG B O   1 
ATOM   5433  C CB  . ARG A 1 719  ? 203.158 222.048 256.694 1.00 70.93  ? 702  ARG B CB  1 
ATOM   5434  C CG  . ARG A 1 719  ? 201.886 221.852 255.911 1.00 70.93  ? 702  ARG B CG  1 
ATOM   5435  C CD  . ARG A 1 719  ? 201.826 220.473 255.275 1.00 70.93  ? 702  ARG B CD  1 
ATOM   5436  N NE  . ARG A 1 719  ? 202.927 220.221 254.355 1.00 70.93  ? 702  ARG B NE  1 
ATOM   5437  C CZ  . ARG A 1 719  ? 202.926 219.263 253.439 1.00 70.93  ? 702  ARG B CZ  1 
ATOM   5438  N NH1 . ARG A 1 719  ? 201.885 218.465 253.276 1.00 70.93  ? 702  ARG B NH1 1 
ATOM   5439  N NH2 . ARG A 1 719  ? 203.995 219.101 252.668 1.00 70.93  ? 702  ARG B NH2 1 
ATOM   5440  N N   . ASN A 1 720  ? 204.338 219.598 258.181 1.00 72.19  ? 703  ASN B N   1 
ATOM   5441  C CA  . ASN A 1 720  ? 204.500 218.161 258.381 1.00 72.19  ? 703  ASN B CA  1 
ATOM   5442  C C   . ASN A 1 720  ? 204.166 217.765 259.816 1.00 72.19  ? 703  ASN B C   1 
ATOM   5443  O O   . ASN A 1 720  ? 203.548 216.718 260.057 1.00 72.19  ? 703  ASN B O   1 
ATOM   5444  C CB  . ASN A 1 720  ? 205.920 217.738 258.017 1.00 72.19  ? 703  ASN B CB  1 
ATOM   5445  C CG  . ASN A 1 720  ? 206.178 217.809 256.529 1.00 72.19  ? 703  ASN B CG  1 
ATOM   5446  O OD1 . ASN A 1 720  ? 205.553 218.594 255.819 1.00 72.19  ? 703  ASN B OD1 1 
ATOM   5447  N ND2 . ASN A 1 720  ? 207.100 216.985 256.047 1.00 72.19  ? 703  ASN B ND2 1 
ATOM   5448  N N   . GLU A 1 721  ? 204.567 218.594 260.782 1.00 77.23  ? 704  GLU B N   1 
ATOM   5449  C CA  . GLU A 1 721  ? 204.257 218.306 262.180 1.00 77.23  ? 704  GLU B CA  1 
ATOM   5450  C C   . GLU A 1 721  ? 202.753 218.299 262.424 1.00 77.23  ? 704  GLU B C   1 
ATOM   5451  O O   . GLU A 1 721  ? 202.243 217.448 263.161 1.00 77.23  ? 704  GLU B O   1 
ATOM   5452  C CB  . GLU A 1 721  ? 204.937 219.321 263.098 1.00 77.23  ? 704  GLU B CB  1 
ATOM   5453  C CG  . GLU A 1 721  ? 206.443 219.425 262.923 1.00 77.23  ? 704  GLU B CG  1 
ATOM   5454  C CD  . GLU A 1 721  ? 207.210 218.451 263.793 1.00 77.23  ? 704  GLU B CD  1 
ATOM   5455  O OE1 . GLU A 1 721  ? 206.767 217.291 263.927 1.00 77.23  ? 704  GLU B OE1 1 
ATOM   5456  O OE2 . GLU A 1 721  ? 208.259 218.847 264.343 1.00 77.23  ? 704  GLU B OE2 1 
ATOM   5457  N N   . LYS A 1 722  ? 202.029 219.249 261.828 1.00 69.60  ? 705  LYS B N   1 
ATOM   5458  C CA  . LYS A 1 722  ? 200.578 219.288 261.980 1.00 69.60  ? 705  LYS B CA  1 
ATOM   5459  C C   . LYS A 1 722  ? 199.929 218.050 261.383 1.00 69.60  ? 705  LYS B C   1 
ATOM   5460  O O   . LYS A 1 722  ? 199.001 217.478 261.972 1.00 69.60  ? 705  LYS B O   1 
ATOM   5461  C CB  . LYS A 1 722  ? 200.015 220.549 261.328 1.00 69.60  ? 705  LYS B CB  1 
ATOM   5462  C CG  . LYS A 1 722  ? 198.730 221.042 261.954 1.00 69.60  ? 705  LYS B CG  1 
ATOM   5463  C CD  . LYS A 1 722  ? 199.006 222.022 263.074 1.00 69.60  ? 705  LYS B CD  1 
ATOM   5464  C CE  . LYS A 1 722  ? 197.862 223.002 263.235 1.00 69.60  ? 705  LYS B CE  1 
ATOM   5465  N NZ  . LYS A 1 722  ? 198.159 224.026 264.270 1.00 69.60  ? 705  LYS B NZ  1 
ATOM   5466  N N   . TRP A 1 723  ? 200.397 217.624 260.207 1.00 69.60  ? 706  TRP B N   1 
ATOM   5467  C CA  . TRP A 1 723  ? 199.876 216.395 259.615 1.00 69.60  ? 706  TRP B CA  1 
ATOM   5468  C C   . TRP A 1 723  ? 200.081 215.211 260.551 1.00 69.60  ? 706  TRP B C   1 
ATOM   5469  O O   . TRP A 1 723  ? 199.150 214.436 260.816 1.00 69.60  ? 706  TRP B O   1 
ATOM   5470  C CB  . TRP A 1 723  ? 200.548 216.134 258.268 1.00 69.60  ? 706  TRP B CB  1 
ATOM   5471  C CG  . TRP A 1 723  ? 199.855 216.777 257.118 1.00 69.60  ? 706  TRP B CG  1 
ATOM   5472  C CD1 . TRP A 1 723  ? 199.898 218.090 256.768 1.00 69.60  ? 706  TRP B CD1 1 
ATOM   5473  C CD2 . TRP A 1 723  ? 199.011 216.133 256.158 1.00 69.60  ? 706  TRP B CD2 1 
ATOM   5474  N NE1 . TRP A 1 723  ? 199.133 218.308 255.650 1.00 69.60  ? 706  TRP B NE1 1 
ATOM   5475  C CE2 . TRP A 1 723  ? 198.577 217.120 255.257 1.00 69.60  ? 706  TRP B CE2 1 
ATOM   5476  C CE3 . TRP A 1 723  ? 198.579 214.818 255.977 1.00 69.60  ? 706  TRP B CE3 1 
ATOM   5477  C CZ2 . TRP A 1 723  ? 197.735 216.834 254.191 1.00 69.60  ? 706  TRP B CZ2 1 
ATOM   5478  C CZ3 . TRP A 1 723  ? 197.744 214.538 254.919 1.00 69.60  ? 706  TRP B CZ3 1 
ATOM   5479  C CH2 . TRP A 1 723  ? 197.330 215.540 254.040 1.00 69.60  ? 706  TRP B CH2 1 
ATOM   5480  N N   . ASP A 1 724  ? 201.297 215.072 261.084 1.00 71.17  ? 707  ASP B N   1 
ATOM   5481  C CA  . ASP A 1 724  ? 201.592 213.952 261.971 1.00 71.17  ? 707  ASP B CA  1 
ATOM   5482  C C   . ASP A 1 724  ? 200.734 214.006 263.229 1.00 71.17  ? 707  ASP B C   1 
ATOM   5483  O O   . ASP A 1 724  ? 200.230 212.977 263.694 1.00 71.17  ? 707  ASP B O   1 
ATOM   5484  C CB  . ASP A 1 724  ? 203.077 213.952 262.329 1.00 71.17  ? 707  ASP B CB  1 
ATOM   5485  C CG  . ASP A 1 724  ? 203.525 212.659 262.983 1.00 71.17  ? 707  ASP B CG  1 
ATOM   5486  O OD1 . ASP A 1 724  ? 202.681 211.763 263.183 1.00 71.17  ? 707  ASP B OD1 1 
ATOM   5487  O OD2 . ASP A 1 724  ? 204.730 212.531 263.283 1.00 71.17  ? 707  ASP B OD2 1 
ATOM   5488  N N   . GLU A 1 725  ? 200.550 215.201 263.790 1.00 70.15  ? 708  GLU B N   1 
ATOM   5489  C CA  . GLU A 1 725  ? 199.799 215.337 265.033 1.00 70.15  ? 708  GLU B CA  1 
ATOM   5490  C C   . GLU A 1 725  ? 198.323 215.008 264.837 1.00 70.15  ? 708  GLU B C   1 
ATOM   5491  O O   . GLU A 1 725  ? 197.719 214.328 265.677 1.00 70.15  ? 708  GLU B O   1 
ATOM   5492  C CB  . GLU A 1 725  ? 199.988 216.748 265.585 1.00 70.15  ? 708  GLU B CB  1 
ATOM   5493  C CG  . GLU A 1 725  ? 198.847 217.289 266.410 1.00 70.15  ? 708  GLU B CG  1 
ATOM   5494  C CD  . GLU A 1 725  ? 199.080 218.734 266.803 1.00 70.15  ? 708  GLU B CD  1 
ATOM   5495  O OE1 . GLU A 1 725  ? 198.104 219.430 267.146 1.00 70.15  ? 708  GLU B OE1 1 
ATOM   5496  O OE2 . GLU A 1 725  ? 200.247 219.176 266.765 1.00 70.15  ? 708  GLU B OE2 1 
ATOM   5497  N N   . VAL A 1 726  ? 197.725 215.467 263.734 1.00 69.60  ? 709  VAL B N   1 
ATOM   5498  C CA  . VAL A 1 726  ? 196.327 215.129 263.473 1.00 69.60  ? 709  VAL B CA  1 
ATOM   5499  C C   . VAL A 1 726  ? 196.174 213.631 263.247 1.00 69.60  ? 709  VAL B C   1 
ATOM   5500  O O   . VAL A 1 726  ? 195.221 213.007 263.738 1.00 69.60  ? 709  VAL B O   1 
ATOM   5501  C CB  . VAL A 1 726  ? 195.784 215.940 262.283 1.00 69.60  ? 709  VAL B CB  1 
ATOM   5502  C CG1 . VAL A 1 726  ? 194.573 215.254 261.687 1.00 69.60  ? 709  VAL B CG1 1 
ATOM   5503  C CG2 . VAL A 1 726  ? 195.423 217.340 262.727 1.00 69.60  ? 709  VAL B CG2 1 
ATOM   5504  N N   . TYR A 1 727  ? 197.108 213.025 262.507 1.00 69.70  ? 710  TYR B N   1 
ATOM   5505  C CA  . TYR A 1 727  ? 197.040 211.582 262.301 1.00 69.70  ? 710  TYR B CA  1 
ATOM   5506  C C   . TYR A 1 727  ? 197.124 210.835 263.625 1.00 69.70  ? 710  TYR B C   1 
ATOM   5507  O O   . TYR A 1 727  ? 196.385 209.868 263.851 1.00 69.70  ? 710  TYR B O   1 
ATOM   5508  C CB  . TYR A 1 727  ? 198.155 211.132 261.360 1.00 69.70  ? 710  TYR B CB  1 
ATOM   5509  C CG  . TYR A 1 727  ? 197.818 211.286 259.898 1.00 69.70  ? 710  TYR B CG  1 
ATOM   5510  C CD1 . TYR A 1 727  ? 196.589 211.787 259.500 1.00 69.70  ? 710  TYR B CD1 1 
ATOM   5511  C CD2 . TYR A 1 727  ? 198.729 210.931 258.916 1.00 69.70  ? 710  TYR B CD2 1 
ATOM   5512  C CE1 . TYR A 1 727  ? 196.277 211.930 258.168 1.00 69.70  ? 710  TYR B CE1 1 
ATOM   5513  C CE2 . TYR A 1 727  ? 198.425 211.071 257.581 1.00 69.70  ? 710  TYR B CE2 1 
ATOM   5514  C CZ  . TYR A 1 727  ? 197.197 211.572 257.213 1.00 69.70  ? 710  TYR B CZ  1 
ATOM   5515  O OH  . TYR A 1 727  ? 196.888 211.713 255.882 1.00 69.70  ? 710  TYR B OH  1 
ATOM   5516  N N   . LYS A 1 728  ? 198.015 211.272 264.516 1.00 69.60  ? 711  LYS B N   1 
ATOM   5517  C CA  . LYS A 1 728  ? 198.150 210.616 265.812 1.00 69.60  ? 711  LYS B CA  1 
ATOM   5518  C C   . LYS A 1 728  ? 196.882 210.764 266.642 1.00 69.60  ? 711  LYS B C   1 
ATOM   5519  O O   . LYS A 1 728  ? 196.456 209.815 267.311 1.00 69.60  ? 711  LYS B O   1 
ATOM   5520  C CB  . LYS A 1 728  ? 199.356 211.179 266.561 1.00 69.60  ? 711  LYS B CB  1 
ATOM   5521  C CG  . LYS A 1 728  ? 199.296 211.001 268.063 1.00 69.60  ? 711  LYS B CG  1 
ATOM   5522  C CD  . LYS A 1 728  ? 200.392 211.792 268.749 1.00 69.60  ? 711  LYS B CD  1 
ATOM   5523  C CE  . LYS A 1 728  ? 201.718 211.061 268.674 1.00 69.60  ? 711  LYS B CE  1 
ATOM   5524  N NZ  . LYS A 1 728  ? 201.689 209.799 269.461 1.00 69.60  ? 711  LYS B NZ  1 
ATOM   5525  N N   . TYR A 1 729  ? 196.263 211.947 266.617 1.00 69.60  ? 712  TYR B N   1 
ATOM   5526  C CA  . TYR A 1 729  ? 195.022 212.132 267.364 1.00 69.60  ? 712  TYR B CA  1 
ATOM   5527  C C   . TYR A 1 729  ? 193.922 211.215 266.847 1.00 69.60  ? 712  TYR B C   1 
ATOM   5528  O O   . TYR A 1 729  ? 193.184 210.608 267.635 1.00 69.60  ? 712  TYR B O   1 
ATOM   5529  C CB  . TYR A 1 729  ? 194.567 213.586 267.290 1.00 69.60  ? 712  TYR B CB  1 
ATOM   5530  C CG  . TYR A 1 729  ? 193.165 213.793 267.810 1.00 69.60  ? 712  TYR B CG  1 
ATOM   5531  C CD1 . TYR A 1 729  ? 192.875 213.644 269.156 1.00 69.60  ? 712  TYR B CD1 1 
ATOM   5532  C CD2 . TYR A 1 729  ? 192.130 214.125 266.953 1.00 69.60  ? 712  TYR B CD2 1 
ATOM   5533  C CE1 . TYR A 1 729  ? 191.595 213.829 269.636 1.00 69.60  ? 712  TYR B CE1 1 
ATOM   5534  C CE2 . TYR A 1 729  ? 190.847 214.310 267.424 1.00 69.60  ? 712  TYR B CE2 1 
ATOM   5535  C CZ  . TYR A 1 729  ? 190.586 214.163 268.764 1.00 69.60  ? 712  TYR B CZ  1 
ATOM   5536  O OH  . TYR A 1 729  ? 189.308 214.350 269.232 1.00 69.60  ? 712  TYR B OH  1 
ATOM   5537  N N   . ILE A 1 730  ? 193.794 211.102 265.524 1.00 69.60  ? 713  ILE B N   1 
ATOM   5538  C CA  . ILE A 1 730  ? 192.761 210.237 264.959 1.00 69.60  ? 713  ILE B CA  1 
ATOM   5539  C C   . ILE A 1 730  ? 193.035 208.779 265.308 1.00 69.60  ? 713  ILE B C   1 
ATOM   5540  O O   . ILE A 1 730  ? 192.112 208.016 265.619 1.00 69.60  ? 713  ILE B O   1 
ATOM   5541  C CB  . ILE A 1 730  ? 192.652 210.452 263.439 1.00 69.60  ? 713  ILE B CB  1 
ATOM   5542  C CG1 . ILE A 1 730  ? 191.767 211.659 263.143 1.00 69.60  ? 713  ILE B CG1 1 
ATOM   5543  C CG2 . ILE A 1 730  ? 192.100 209.218 262.758 1.00 69.60  ? 713  ILE B CG2 1 
ATOM   5544  C CD1 . ILE A 1 730  ? 191.746 212.045 261.692 1.00 69.60  ? 713  ILE B CD1 1 
ATOM   5545  N N   . VAL A 1 731  ? 194.304 208.369 265.270 1.00 69.60  ? 714  VAL B N   1 
ATOM   5546  C CA  . VAL A 1 731  ? 194.644 206.996 265.633 1.00 69.60  ? 714  VAL B CA  1 
ATOM   5547  C C   . VAL A 1 731  ? 194.299 206.729 267.092 1.00 69.60  ? 714  VAL B C   1 
ATOM   5548  O O   . VAL A 1 731  ? 193.777 205.662 267.435 1.00 69.60  ? 714  VAL B O   1 
ATOM   5549  C CB  . VAL A 1 731  ? 196.128 206.716 265.340 1.00 69.60  ? 714  VAL B CB  1 
ATOM   5550  C CG1 . VAL A 1 731  ? 196.588 205.467 266.066 1.00 69.60  ? 714  VAL B CG1 1 
ATOM   5551  C CG2 . VAL A 1 731  ? 196.346 206.567 263.849 1.00 69.60  ? 714  VAL B CG2 1 
ATOM   5552  N N   . THR A 1 732  ? 194.590 207.688 267.975 1.00 69.60  ? 715  THR B N   1 
ATOM   5553  C CA  . THR A 1 732  ? 194.244 207.527 269.385 1.00 69.60  ? 715  THR B CA  1 
ATOM   5554  C C   . THR A 1 732  ? 192.740 207.387 269.571 1.00 69.60  ? 715  THR B C   1 
ATOM   5555  O O   . THR A 1 732  ? 192.275 206.523 270.325 1.00 69.60  ? 715  THR B O   1 
ATOM   5556  C CB  . THR A 1 732  ? 194.772 208.712 270.192 1.00 69.60  ? 715  THR B CB  1 
ATOM   5557  O OG1 . THR A 1 732  ? 196.179 208.555 270.414 1.00 69.60  ? 715  THR B OG1 1 
ATOM   5558  C CG2 . THR A 1 732  ? 194.061 208.812 271.529 1.00 69.60  ? 715  THR B CG2 1 
ATOM   5559  N N   . ASN A 1 733  ? 191.962 208.227 268.885 1.00 69.60  ? 716  ASN B N   1 
ATOM   5560  C CA  . ASN A 1 733  ? 190.509 208.140 268.990 1.00 69.60  ? 716  ASN B CA  1 
ATOM   5561  C C   . ASN A 1 733  ? 189.999 206.789 268.504 1.00 69.60  ? 716  ASN B C   1 
ATOM   5562  O O   . ASN A 1 733  ? 189.133 206.176 269.139 1.00 69.60  ? 716  ASN B O   1 
ATOM   5563  C CB  . ASN A 1 733  ? 189.863 209.274 268.197 1.00 69.60  ? 716  ASN B CB  1 
ATOM   5564  C CG  . ASN A 1 733  ? 188.546 209.712 268.783 1.00 69.60  ? 716  ASN B CG  1 
ATOM   5565  O OD1 . ASN A 1 733  ? 187.752 208.890 269.230 1.00 69.60  ? 716  ASN B OD1 1 
ATOM   5566  N ND2 . ASN A 1 733  ? 188.306 211.016 268.788 1.00 69.60  ? 716  ASN B ND2 1 
ATOM   5567  N N   . TRP A 1 734  ? 190.534 206.306 267.381 1.00 69.60  ? 717  TRP B N   1 
ATOM   5568  C CA  . TRP A 1 734  ? 190.106 205.018 266.847 1.00 69.60  ? 717  TRP B CA  1 
ATOM   5569  C C   . TRP A 1 734  ? 190.463 203.879 267.791 1.00 69.60  ? 717  TRP B C   1 
ATOM   5570  O O   . TRP A 1 734  ? 189.663 202.960 267.995 1.00 69.60  ? 717  TRP B O   1 
ATOM   5571  C CB  . TRP A 1 734  ? 190.735 204.792 265.476 1.00 69.60  ? 717  TRP B CB  1 
ATOM   5572  C CG  . TRP A 1 734  ? 190.761 203.367 265.051 1.00 69.60  ? 717  TRP B CG  1 
ATOM   5573  C CD1 . TRP A 1 734  ? 189.700 202.610 264.665 1.00 69.60  ? 717  TRP B CD1 1 
ATOM   5574  C CD2 . TRP A 1 734  ? 191.912 202.526 264.951 1.00 69.60  ? 717  TRP B CD2 1 
ATOM   5575  N NE1 . TRP A 1 734  ? 190.116 201.344 264.335 1.00 69.60  ? 717  TRP B NE1 1 
ATOM   5576  C CE2 . TRP A 1 734  ? 191.472 201.269 264.503 1.00 69.60  ? 717  TRP B CE2 1 
ATOM   5577  C CE3 . TRP A 1 734  ? 193.272 202.713 265.200 1.00 69.60  ? 717  TRP B CE3 1 
ATOM   5578  C CZ2 . TRP A 1 734  ? 192.342 200.207 264.300 1.00 69.60  ? 717  TRP B CZ2 1 
ATOM   5579  C CZ3 . TRP A 1 734  ? 194.132 201.658 264.997 1.00 69.60  ? 717  TRP B CZ3 1 
ATOM   5580  C CH2 . TRP A 1 734  ? 193.666 200.423 264.551 1.00 69.60  ? 717  TRP B CH2 1 
ATOM   5581  N N   . LEU A 1 735  ? 191.663 203.918 268.372 1.00 69.60  ? 718  LEU B N   1 
ATOM   5582  C CA  . LEU A 1 735  ? 192.067 202.871 269.305 1.00 69.60  ? 718  LEU B CA  1 
ATOM   5583  C C   . LEU A 1 735  ? 191.196 202.879 270.551 1.00 69.60  ? 718  LEU B C   1 
ATOM   5584  O O   . LEU A 1 735  ? 190.843 201.818 271.077 1.00 69.60  ? 718  LEU B O   1 
ATOM   5585  C CB  . LEU A 1 735  ? 193.537 203.043 269.686 1.00 69.60  ? 718  LEU B CB  1 
ATOM   5586  C CG  . LEU A 1 735  ? 194.550 202.190 268.926 1.00 69.60  ? 718  LEU B CG  1 
ATOM   5587  C CD1 . LEU A 1 735  ? 195.961 202.568 269.330 1.00 69.60  ? 718  LEU B CD1 1 
ATOM   5588  C CD2 . LEU A 1 735  ? 194.298 200.717 269.176 1.00 69.60  ? 718  LEU B CD2 1 
ATOM   5589  N N   . ALA A 1 736  ? 190.846 204.067 271.044 1.00 69.60  ? 719  ALA B N   1 
ATOM   5590  C CA  . ALA A 1 736  ? 190.072 204.145 272.276 1.00 69.60  ? 719  ALA B CA  1 
ATOM   5591  C C   . ALA A 1 736  ? 188.622 203.731 272.061 1.00 69.60  ? 719  ALA B C   1 
ATOM   5592  O O   . ALA A 1 736  ? 188.031 203.068 272.920 1.00 69.60  ? 719  ALA B O   1 
ATOM   5593  C CB  . ALA A 1 736  ? 190.142 205.558 272.851 1.00 69.60  ? 719  ALA B CB  1 
ATOM   5594  N N   . LYS A 1 737  ? 188.027 204.103 270.924 1.00 69.60  ? 720  LYS B N   1 
ATOM   5595  C CA  . LYS A 1 737  ? 186.585 203.973 270.769 1.00 69.60  ? 720  LYS B CA  1 
ATOM   5596  C C   . LYS A 1 737  ? 186.124 202.828 269.878 1.00 69.60  ? 720  LYS B C   1 
ATOM   5597  O O   . LYS A 1 737  ? 184.960 202.434 269.980 1.00 69.60  ? 720  LYS B O   1 
ATOM   5598  C CB  . LYS A 1 737  ? 185.991 205.278 270.221 1.00 69.60  ? 720  LYS B CB  1 
ATOM   5599  C CG  . LYS A 1 737  ? 185.581 206.269 271.292 1.00 69.60  ? 720  LYS B CG  1 
ATOM   5600  C CD  . LYS A 1 737  ? 185.241 207.615 270.683 1.00 69.60  ? 720  LYS B CD  1 
ATOM   5601  C CE  . LYS A 1 737  ? 184.712 208.578 271.726 1.00 69.60  ? 720  LYS B CE  1 
ATOM   5602  N NZ  . LYS A 1 737  ? 184.430 209.917 271.146 1.00 69.60  ? 720  LYS B NZ  1 
ATOM   5603  N N   . VAL A 1 738  ? 186.976 202.284 269.015 1.00 69.60  ? 721  VAL B N   1 
ATOM   5604  C CA  . VAL A 1 738  ? 186.556 201.314 268.009 1.00 69.60  ? 721  VAL B CA  1 
ATOM   5605  C C   . VAL A 1 738  ? 187.143 199.932 268.271 1.00 69.60  ? 721  VAL B C   1 
ATOM   5606  O O   . VAL A 1 738  ? 186.418 198.937 268.288 1.00 69.60  ? 721  VAL B O   1 
ATOM   5607  C CB  . VAL A 1 738  ? 186.906 201.802 266.587 1.00 69.60  ? 721  VAL B CB  1 
ATOM   5608  C CG1 . VAL A 1 738  ? 186.944 200.633 265.622 1.00 69.60  ? 721  VAL B CG1 1 
ATOM   5609  C CG2 . VAL A 1 738  ? 185.900 202.835 266.130 1.00 69.60  ? 721  VAL B CG2 1 
ATOM   5610  N N   . ASN A 1 739  ? 188.459 199.846 268.469 1.00 69.60  ? 722  ASN B N   1 
ATOM   5611  C CA  . ASN A 1 739  ? 189.098 198.538 268.566 1.00 69.60  ? 722  ASN B CA  1 
ATOM   5612  C C   . ASN A 1 739  ? 188.628 197.758 269.788 1.00 69.60  ? 722  ASN B C   1 
ATOM   5613  O O   . ASN A 1 739  ? 188.649 196.521 269.775 1.00 69.60  ? 722  ASN B O   1 
ATOM   5614  C CB  . ASN A 1 739  ? 190.616 198.693 268.588 1.00 69.60  ? 722  ASN B CB  1 
ATOM   5615  C CG  . ASN A 1 739  ? 191.325 197.544 267.905 1.00 69.60  ? 722  ASN B CG  1 
ATOM   5616  O OD1 . ASN A 1 739  ? 191.085 197.262 266.733 1.00 69.60  ? 722  ASN B OD1 1 
ATOM   5617  N ND2 . ASN A 1 739  ? 192.202 196.870 268.636 1.00 69.60  ? 722  ASN B ND2 1 
ATOM   5618  N N   . THR A 1 740  ? 188.202 198.451 270.846 1.00 69.60  ? 723  THR B N   1 
ATOM   5619  C CA  . THR A 1 740  ? 187.730 197.760 272.041 1.00 69.60  ? 723  THR B CA  1 
ATOM   5620  C C   . THR A 1 740  ? 186.485 196.930 271.748 1.00 69.60  ? 723  THR B C   1 
ATOM   5621  O O   . THR A 1 740  ? 186.360 195.792 272.218 1.00 69.60  ? 723  THR B O   1 
ATOM   5622  C CB  . THR A 1 740  ? 187.448 198.770 273.150 1.00 69.60  ? 723  THR B CB  1 
ATOM   5623  O OG1 . THR A 1 740  ? 186.238 199.475 272.854 1.00 69.60  ? 723  THR B OG1 1 
ATOM   5624  C CG2 . THR A 1 740  ? 188.589 199.767 273.256 1.00 69.60  ? 723  THR B CG2 1 
ATOM   5625  N N   . GLN A 1 741  ? 185.550 197.486 270.975 1.00 69.60  ? 724  GLN B N   1 
ATOM   5626  C CA  . GLN A 1 741  ? 184.347 196.743 270.617 1.00 69.60  ? 724  GLN B CA  1 
ATOM   5627  C C   . GLN A 1 741  ? 184.683 195.519 269.778 1.00 69.60  ? 724  GLN B C   1 
ATOM   5628  O O   . GLN A 1 741  ? 184.092 194.448 269.960 1.00 69.60  ? 724  GLN B O   1 
ATOM   5629  C CB  . GLN A 1 741  ? 183.377 197.656 269.873 1.00 69.60  ? 724  GLN B CB  1 
ATOM   5630  C CG  . GLN A 1 741  ? 183.013 198.904 270.642 1.00 69.60  ? 724  GLN B CG  1 
ATOM   5631  C CD  . GLN A 1 741  ? 182.275 199.908 269.795 1.00 69.60  ? 724  GLN B CD  1 
ATOM   5632  O OE1 . GLN A 1 741  ? 181.225 199.609 269.233 1.00 69.60  ? 724  GLN B OE1 1 
ATOM   5633  N NE2 . GLN A 1 741  ? 182.821 201.111 269.698 1.00 69.60  ? 724  GLN B NE2 1 
ATOM   5634  N N   . ILE A 1 742  ? 185.626 195.659 268.846 1.00 69.60  ? 725  ILE B N   1 
ATOM   5635  C CA  . ILE A 1 742  ? 186.037 194.520 268.034 1.00 69.60  ? 725  ILE B CA  1 
ATOM   5636  C C   . ILE A 1 742  ? 186.660 193.442 268.910 1.00 69.60  ? 725  ILE B C   1 
ATOM   5637  O O   . ILE A 1 742  ? 186.407 192.245 268.722 1.00 69.60  ? 725  ILE B O   1 
ATOM   5638  C CB  . ILE A 1 742  ? 186.996 194.977 266.922 1.00 69.60  ? 725  ILE B CB  1 
ATOM   5639  C CG1 . ILE A 1 742  ? 186.336 196.052 266.061 1.00 69.60  ? 725  ILE B CG1 1 
ATOM   5640  C CG2 . ILE A 1 742  ? 187.407 193.803 266.064 1.00 69.60  ? 725  ILE B CG2 1 
ATOM   5641  C CD1 . ILE A 1 742  ? 185.151 195.558 265.272 1.00 69.60  ? 725  ILE B CD1 1 
ATOM   5642  N N   . ASP A 1 743  ? 187.481 193.845 269.883 1.00 70.05  ? 726  ASP B N   1 
ATOM   5643  C CA  . ASP A 1 743  ? 188.074 192.869 270.792 1.00 70.05  ? 726  ASP B CA  1 
ATOM   5644  C C   . ASP A 1 743  ? 187.003 192.143 271.598 1.00 70.05  ? 726  ASP B C   1 
ATOM   5645  O O   . ASP A 1 743  ? 187.077 190.921 271.791 1.00 70.05  ? 726  ASP B O   1 
ATOM   5646  C CB  . ASP A 1 743  ? 189.068 193.559 271.723 1.00 70.05  ? 726  ASP B CB  1 
ATOM   5647  C CG  . ASP A 1 743  ? 190.481 193.540 271.181 1.00 70.05  ? 726  ASP B CG  1 
ATOM   5648  O OD1 . ASP A 1 743  ? 190.666 193.111 270.024 1.00 70.05  ? 726  ASP B OD1 1 
ATOM   5649  O OD2 . ASP A 1 743  ? 191.405 193.956 271.911 1.00 70.05  ? 726  ASP B OD2 1 
ATOM   5650  N N   . LEU A 1 744  ? 186.005 192.879 272.084 1.00 69.60  ? 727  LEU B N   1 
ATOM   5651  C CA  . LEU A 1 744  ? 184.932 192.240 272.839 1.00 69.60  ? 727  LEU B CA  1 
ATOM   5652  C C   . LEU A 1 744  ? 184.156 191.258 271.971 1.00 69.60  ? 727  LEU B C   1 
ATOM   5653  O O   . LEU A 1 744  ? 183.799 190.165 272.425 1.00 69.60  ? 727  LEU B O   1 
ATOM   5654  C CB  . LEU A 1 744  ? 183.994 193.291 273.421 1.00 69.60  ? 727  LEU B CB  1 
ATOM   5655  C CG  . LEU A 1 744  ? 183.458 192.933 274.803 1.00 69.60  ? 727  LEU B CG  1 
ATOM   5656  C CD1 . LEU A 1 744  ? 184.556 193.049 275.844 1.00 69.60  ? 727  LEU B CD1 1 
ATOM   5657  C CD2 . LEU A 1 744  ? 182.282 193.814 275.155 1.00 69.60  ? 727  LEU B CD2 1 
ATOM   5658  N N   . ILE A 1 745  ? 183.882 191.632 270.720 1.00 69.60  ? 728  ILE B N   1 
ATOM   5659  C CA  . ILE A 1 745  ? 183.174 190.729 269.817 1.00 69.60  ? 728  ILE B CA  1 
ATOM   5660  C C   . ILE A 1 745  ? 184.003 189.477 269.563 1.00 69.60  ? 728  ILE B C   1 
ATOM   5661  O O   . ILE A 1 745  ? 183.468 188.366 269.475 1.00 69.60  ? 728  ILE B O   1 
ATOM   5662  C CB  . ILE A 1 745  ? 182.815 191.454 268.508 1.00 69.60  ? 728  ILE B CB  1 
ATOM   5663  C CG1 . ILE A 1 745  ? 181.679 192.444 268.751 1.00 69.60  ? 728  ILE B CG1 1 
ATOM   5664  C CG2 . ILE A 1 745  ? 182.414 190.463 267.437 1.00 69.60  ? 728  ILE B CG2 1 
ATOM   5665  C CD1 . ILE A 1 745  ? 181.483 193.426 267.628 1.00 69.60  ? 728  ILE B CD1 1 
ATOM   5666  N N   . ARG A 1 746  ? 185.321 189.636 269.442 1.00 71.88  ? 729  ARG B N   1 
ATOM   5667  C CA  . ARG A 1 746  ? 186.200 188.485 269.261 1.00 71.88  ? 729  ARG B CA  1 
ATOM   5668  C C   . ARG A 1 746  ? 186.125 187.541 270.457 1.00 71.88  ? 729  ARG B C   1 
ATOM   5669  O O   . ARG A 1 746  ? 185.988 186.316 270.301 1.00 71.88  ? 729  ARG B O   1 
ATOM   5670  C CB  . ARG A 1 746  ? 187.629 188.977 269.044 1.00 71.88  ? 729  ARG B CB  1 
ATOM   5671  C CG  . ARG A 1 746  ? 188.682 187.900 269.027 1.00 71.88  ? 729  ARG B CG  1 
ATOM   5672  C CD  . ARG A 1 746  ? 189.904 188.379 268.266 1.00 71.88  ? 729  ARG B CD  1 
ATOM   5673  N NE  . ARG A 1 746  ? 190.071 189.824 268.351 1.00 71.88  ? 729  ARG B NE  1 
ATOM   5674  C CZ  . ARG A 1 746  ? 190.298 190.614 267.310 1.00 71.88  ? 729  ARG B CZ  1 
ATOM   5675  N NH1 . ARG A 1 746  ? 190.380 190.133 266.082 1.00 71.88  ? 729  ARG B NH1 1 
ATOM   5676  N NH2 . ARG A 1 746  ? 190.450 191.920 267.508 1.00 71.88  ? 729  ARG B NH2 1 
ATOM   5677  N N   . LYS A 1 747  ? 186.201 188.101 271.666 1.00 69.60  ? 730  LYS B N   1 
ATOM   5678  C CA  . LYS A 1 747  ? 186.112 187.277 272.867 1.00 69.60  ? 730  LYS B CA  1 
ATOM   5679  C C   . LYS A 1 747  ? 184.767 186.565 272.945 1.00 69.60  ? 730  LYS B C   1 
ATOM   5680  O O   . LYS A 1 747  ? 184.690 185.398 273.349 1.00 69.60  ? 730  LYS B O   1 
ATOM   5681  C CB  . LYS A 1 747  ? 186.342 188.136 274.109 1.00 69.60  ? 730  LYS B CB  1 
ATOM   5682  C CG  . LYS A 1 747  ? 187.786 188.578 274.288 1.00 69.60  ? 730  LYS B CG  1 
ATOM   5683  C CD  . LYS A 1 747  ? 187.936 189.616 275.389 1.00 69.60  ? 730  LYS B CD  1 
ATOM   5684  C CE  . LYS A 1 747  ? 187.189 189.208 276.645 1.00 69.60  ? 730  LYS B CE  1 
ATOM   5685  N NZ  . LYS A 1 747  ? 186.727 190.390 277.423 1.00 69.60  ? 730  LYS B NZ  1 
ATOM   5686  N N   . LYS A 1 748  ? 183.694 187.251 272.550 1.00 70.37  ? 731  LYS B N   1 
ATOM   5687  C CA  . LYS A 1 748  ? 182.371 186.639 272.598 1.00 70.37  ? 731  LYS B CA  1 
ATOM   5688  C C   . LYS A 1 748  ? 182.226 185.535 271.558 1.00 70.37  ? 731  LYS B C   1 
ATOM   5689  O O   . LYS A 1 748  ? 181.552 184.530 271.808 1.00 70.37  ? 731  LYS B O   1 
ATOM   5690  C CB  . LYS A 1 748  ? 181.301 187.709 272.416 1.00 70.37  ? 731  LYS B CB  1 
ATOM   5691  C CG  . LYS A 1 748  ? 181.063 188.512 273.676 1.00 70.37  ? 731  LYS B CG  1 
ATOM   5692  C CD  . LYS A 1 748  ? 179.844 189.388 273.551 1.00 70.37  ? 731  LYS B CD  1 
ATOM   5693  C CE  . LYS A 1 748  ? 179.679 190.252 274.778 1.00 70.37  ? 731  LYS B CE  1 
ATOM   5694  N NZ  . LYS A 1 748  ? 179.887 189.445 276.002 1.00 70.37  ? 731  LYS B NZ  1 
ATOM   5695  N N   . MET A 1 749  ? 182.843 185.700 270.387 1.00 74.80  ? 732  MET B N   1 
ATOM   5696  C CA  . MET A 1 749  ? 182.883 184.612 269.413 1.00 74.80  ? 732  MET B CA  1 
ATOM   5697  C C   . MET A 1 749  ? 183.575 183.389 269.994 1.00 74.80  ? 732  MET B C   1 
ATOM   5698  O O   . MET A 1 749  ? 183.091 182.256 269.853 1.00 74.80  ? 732  MET B O   1 
ATOM   5699  C CB  . MET A 1 749  ? 183.597 185.066 268.139 1.00 74.80  ? 732  MET B CB  1 
ATOM   5700  C CG  . MET A 1 749  ? 183.107 184.406 266.852 1.00 74.80  ? 732  MET B CG  1 
ATOM   5701  S SD  . MET A 1 749  ? 181.330 184.277 266.596 1.00 74.80  ? 732  MET B SD  1 
ATOM   5702  C CE  . MET A 1 749  ? 180.806 185.938 266.984 1.00 74.80  ? 732  MET B CE  1 
ATOM   5703  N N   . LYS A 1 750  ? 184.716 183.601 270.652 1.00 73.86  ? 733  LYS B N   1 
ATOM   5704  C CA  . LYS A 1 750  ? 185.416 182.476 271.264 1.00 73.86  ? 733  LYS B CA  1 
ATOM   5705  C C   . LYS A 1 750  ? 184.542 181.797 272.311 1.00 73.86  ? 733  LYS B C   1 
ATOM   5706  O O   . LYS A 1 750  ? 184.466 180.561 272.370 1.00 73.86  ? 733  LYS B O   1 
ATOM   5707  C CB  . LYS A 1 750  ? 186.728 182.954 271.882 1.00 73.86  ? 733  LYS B CB  1 
ATOM   5708  C CG  . LYS A 1 750  ? 187.493 181.887 272.638 1.00 73.86  ? 733  LYS B CG  1 
ATOM   5709  C CD  . LYS A 1 750  ? 188.174 180.934 271.676 1.00 73.86  ? 733  LYS B CD  1 
ATOM   5710  C CE  . LYS A 1 750  ? 189.275 180.151 272.363 1.00 73.86  ? 733  LYS B CE  1 
ATOM   5711  N NZ  . LYS A 1 750  ? 190.360 181.049 272.841 1.00 73.86  ? 733  LYS B NZ  1 
ATOM   5712  N N   . GLU A 1 751  ? 183.856 182.595 273.133 1.00 76.11  ? 734  GLU B N   1 
ATOM   5713  C CA  . GLU A 1 751  ? 182.995 182.035 274.170 1.00 76.11  ? 734  GLU B CA  1 
ATOM   5714  C C   . GLU A 1 751  ? 181.843 181.236 273.569 1.00 76.11  ? 734  GLU B C   1 
ATOM   5715  O O   . GLU A 1 751  ? 181.500 180.157 274.066 1.00 76.11  ? 734  GLU B O   1 
ATOM   5716  C CB  . GLU A 1 751  ? 182.469 183.157 275.064 1.00 76.11  ? 734  GLU B CB  1 
ATOM   5717  C CG  . GLU A 1 751  ? 181.324 182.758 275.976 1.00 76.11  ? 734  GLU B CG  1 
ATOM   5718  C CD  . GLU A 1 751  ? 181.097 183.760 277.091 1.00 76.11  ? 734  GLU B CD  1 
ATOM   5719  O OE1 . GLU A 1 751  ? 181.776 184.807 277.095 1.00 76.11  ? 734  GLU B OE1 1 
ATOM   5720  O OE2 . GLU A 1 751  ? 180.244 183.500 277.964 1.00 76.11  ? 734  GLU B OE2 1 
ATOM   5721  N N   . ALA A 1 752  ? 181.231 181.750 272.499 1.00 71.97  ? 735  ALA B N   1 
ATOM   5722  C CA  . ALA A 1 752  ? 180.121 181.040 271.869 1.00 71.97  ? 735  ALA B CA  1 
ATOM   5723  C C   . ALA A 1 752  ? 180.579 179.719 271.269 1.00 71.97  ? 735  ALA B C   1 
ATOM   5724  O O   . ALA A 1 752  ? 179.882 178.701 271.380 1.00 71.97  ? 735  ALA B O   1 
ATOM   5725  C CB  . ALA A 1 752  ? 179.476 181.917 270.799 1.00 71.97  ? 735  ALA B CB  1 
ATOM   5726  N N   . LEU A 1 753  ? 181.746 179.716 270.621 1.00 72.85  ? 736  LEU B N   1 
ATOM   5727  C CA  . LEU A 1 753  ? 182.265 178.468 270.071 1.00 72.85  ? 736  LEU B CA  1 
ATOM   5728  C C   . LEU A 1 753  ? 182.545 177.456 271.176 1.00 72.85  ? 736  LEU B C   1 
ATOM   5729  O O   . LEU A 1 753  ? 182.230 176.265 271.037 1.00 72.85  ? 736  LEU B O   1 
ATOM   5730  C CB  . LEU A 1 753  ? 183.523 178.739 269.252 1.00 72.85  ? 736  LEU B CB  1 
ATOM   5731  C CG  . LEU A 1 753  ? 183.264 179.256 267.838 1.00 72.85  ? 736  LEU B CG  1 
ATOM   5732  C CD1 . LEU A 1 753  ? 184.567 179.615 267.153 1.00 72.85  ? 736  LEU B CD1 1 
ATOM   5733  C CD2 . LEU A 1 753  ? 182.497 178.226 267.034 1.00 72.85  ? 736  LEU B CD2 1 
ATOM   5734  N N   . GLU A 1 754  ? 183.123 177.915 272.291 1.00 77.30  ? 737  GLU B N   1 
ATOM   5735  C CA  . GLU A 1 754  ? 183.352 177.017 273.417 1.00 77.30  ? 737  GLU B CA  1 
ATOM   5736  C C   . GLU A 1 754  ? 182.040 176.452 273.947 1.00 77.30  ? 737  GLU B C   1 
ATOM   5737  O O   . GLU A 1 754  ? 181.956 175.265 274.283 1.00 77.30  ? 737  GLU B O   1 
ATOM   5738  C CB  . GLU A 1 754  ? 184.102 177.743 274.531 1.00 77.30  ? 737  GLU B CB  1 
ATOM   5739  C CG  . GLU A 1 754  ? 185.612 177.650 274.437 1.00 77.30  ? 737  GLU B CG  1 
ATOM   5740  C CD  . GLU A 1 754  ? 186.308 178.774 275.180 1.00 77.30  ? 737  GLU B CD  1 
ATOM   5741  O OE1 . GLU A 1 754  ? 185.841 179.145 276.277 1.00 77.30  ? 737  GLU B OE1 1 
ATOM   5742  O OE2 . GLU A 1 754  ? 187.326 179.285 274.671 1.00 77.30  ? 737  GLU B OE2 1 
ATOM   5743  N N   . ASN A 1 755  ? 181.006 177.293 274.036 1.00 74.41  ? 738  ASN B N   1 
ATOM   5744  C CA  . ASN A 1 755  ? 179.712 176.834 274.532 1.00 74.41  ? 738  ASN B CA  1 
ATOM   5745  C C   . ASN A 1 755  ? 179.122 175.766 273.622 1.00 74.41  ? 738  ASN B C   1 
ATOM   5746  O O   . ASN A 1 755  ? 178.582 174.759 274.098 1.00 74.41  ? 738  ASN B O   1 
ATOM   5747  C CB  . ASN A 1 755  ? 178.755 178.017 274.658 1.00 74.41  ? 738  ASN B CB  1 
ATOM   5748  C CG  . ASN A 1 755  ? 179.080 178.904 275.840 1.00 74.41  ? 738  ASN B CG  1 
ATOM   5749  O OD1 . ASN A 1 755  ? 179.974 178.601 276.629 1.00 74.41  ? 738  ASN B OD1 1 
ATOM   5750  N ND2 . ASN A 1 755  ? 178.363 180.014 275.962 1.00 74.41  ? 738  ASN B ND2 1 
ATOM   5751  N N   . GLN A 1 756  ? 179.213 175.969 272.306 1.00 71.40  ? 739  GLN B N   1 
ATOM   5752  C CA  . GLN A 1 756  ? 178.699 174.972 271.371 1.00 71.40  ? 739  GLN B CA  1 
ATOM   5753  C C   . GLN A 1 756  ? 179.452 173.652 271.499 1.00 71.40  ? 739  GLN B C   1 
ATOM   5754  O O   . GLN A 1 756  ? 178.842 172.570 271.507 1.00 71.40  ? 739  GLN B O   1 
ATOM   5755  C CB  . GLN A 1 756  ? 178.786 175.505 269.944 1.00 71.40  ? 739  GLN B CB  1 
ATOM   5756  C CG  . GLN A 1 756  ? 177.711 176.514 269.601 1.00 71.40  ? 739  GLN B CG  1 
ATOM   5757  C CD  . GLN A 1 756  ? 176.357 175.869 269.441 1.00 71.40  ? 739  GLN B CD  1 
ATOM   5758  O OE1 . GLN A 1 756  ? 175.392 176.249 270.099 1.00 71.40  ? 739  GLN B OE1 1 
ATOM   5759  N NE2 . GLN A 1 756  ? 176.278 174.877 268.567 1.00 71.40  ? 739  GLN B NE2 1 
ATOM   5760  N N   . ALA A 1 757  ? 180.782 173.722 271.609 1.00 74.72  ? 740  ALA B N   1 
ATOM   5761  C CA  . ALA A 1 757  ? 181.571 172.502 271.757 1.00 74.72  ? 740  ALA B CA  1 
ATOM   5762  C C   . ALA A 1 757  ? 181.211 171.765 273.041 1.00 74.72  ? 740  ALA B C   1 
ATOM   5763  O O   . ALA A 1 757  ? 181.077 170.534 273.045 1.00 74.72  ? 740  ALA B O   1 
ATOM   5764  C CB  . ALA A 1 757  ? 183.062 172.834 271.728 1.00 74.72  ? 740  ALA B CB  1 
ATOM   5765  N N   . GLU A 1 758  ? 181.043 172.503 274.141 1.00 76.11  ? 741  GLU B N   1 
ATOM   5766  C CA  . GLU A 1 758  ? 180.681 171.875 275.407 1.00 76.11  ? 741  GLU B CA  1 
ATOM   5767  C C   . GLU A 1 758  ? 179.298 171.241 275.337 1.00 76.11  ? 741  GLU B C   1 
ATOM   5768  O O   . GLU A 1 758  ? 179.076 170.168 275.908 1.00 76.11  ? 741  GLU B O   1 
ATOM   5769  C CB  . GLU A 1 758  ? 180.750 172.898 276.538 1.00 76.11  ? 741  GLU B CB  1 
ATOM   5770  C CG  . GLU A 1 758  ? 182.160 173.356 276.862 1.00 76.11  ? 741  GLU B CG  1 
ATOM   5771  C CD  . GLU A 1 758  ? 182.336 173.723 278.320 1.00 76.11  ? 741  GLU B CD  1 
ATOM   5772  O OE1 . GLU A 1 758  ? 181.503 173.296 279.147 1.00 76.11  ? 741  GLU B OE1 1 
ATOM   5773  O OE2 . GLU A 1 758  ? 183.309 174.438 278.641 1.00 76.11  ? 741  GLU B OE2 1 
ATOM   5774  N N   . ALA A 1 759  ? 178.354 171.889 274.651 1.00 73.11  ? 742  ALA B N   1 
ATOM   5775  C CA  . ALA A 1 759  ? 177.022 171.309 274.502 1.00 73.11  ? 742  ALA B CA  1 
ATOM   5776  C C   . ALA A 1 759  ? 177.078 169.992 273.738 1.00 73.11  ? 742  ALA B C   1 
ATOM   5777  O O   . ALA A 1 759  ? 176.459 168.995 274.141 1.00 73.11  ? 742  ALA B O   1 
ATOM   5778  C CB  . ALA A 1 759  ? 176.096 172.300 273.800 1.00 73.11  ? 742  ALA B CB  1 
ATOM   5779  N N   . THR A 1 760  ? 177.827 169.964 272.631 1.00 70.79  ? 743  THR B N   1 
ATOM   5780  C CA  . THR A 1 760  ? 177.950 168.719 271.875 1.00 70.79  ? 743  THR B CA  1 
ATOM   5781  C C   . THR A 1 760  ? 178.613 167.631 272.712 1.00 70.79  ? 743  THR B C   1 
ATOM   5782  O O   . THR A 1 760  ? 178.178 166.470 272.700 1.00 70.79  ? 743  THR B O   1 
ATOM   5783  C CB  . THR A 1 760  ? 178.730 168.954 270.583 1.00 70.79  ? 743  THR B CB  1 
ATOM   5784  O OG1 . THR A 1 760  ? 177.955 169.769 269.698 1.00 70.79  ? 743  THR B OG1 1 
ATOM   5785  C CG2 . THR A 1 760  ? 179.029 167.634 269.900 1.00 70.79  ? 743  THR B CG2 1 
ATOM   5786  N N   . LYS A 1 761  ? 179.662 167.990 273.457 1.00 74.86  ? 744  LYS B N   1 
ATOM   5787  C CA  . LYS A 1 761  ? 180.336 167.008 274.299 1.00 74.86  ? 744  LYS B CA  1 
ATOM   5788  C C   . LYS A 1 761  ? 179.396 166.452 275.359 1.00 74.86  ? 744  LYS B C   1 
ATOM   5789  O O   . LYS A 1 761  ? 179.409 165.249 275.642 1.00 74.86  ? 744  LYS B O   1 
ATOM   5790  C CB  . LYS A 1 761  ? 181.567 167.633 274.952 1.00 74.86  ? 744  LYS B CB  1 
ATOM   5791  C CG  . LYS A 1 761  ? 182.735 167.825 274.010 1.00 74.86  ? 744  LYS B CG  1 
ATOM   5792  C CD  . LYS A 1 761  ? 184.033 167.987 274.774 1.00 74.86  ? 744  LYS B CD  1 
ATOM   5793  C CE  . LYS A 1 761  ? 184.090 169.327 275.482 1.00 74.86  ? 744  LYS B CE  1 
ATOM   5794  N NZ  . LYS A 1 761  ? 185.419 169.569 276.105 1.00 74.86  ? 744  LYS B NZ  1 
ATOM   5795  N N   . ALA A 1 762  ? 178.578 167.315 275.964 1.00 73.27  ? 745  ALA B N   1 
ATOM   5796  C CA  . ALA A 1 762  ? 177.637 166.855 276.979 1.00 73.27  ? 745  ALA B CA  1 
ATOM   5797  C C   . ALA A 1 762  ? 176.607 165.907 276.384 1.00 73.27  ? 745  ALA B C   1 
ATOM   5798  O O   . ALA A 1 762  ? 176.244 164.903 277.009 1.00 73.27  ? 745  ALA B O   1 
ATOM   5799  C CB  . ALA A 1 762  ? 176.950 168.046 277.641 1.00 73.27  ? 745  ALA B CB  1 
ATOM   5800  N N   . ILE A 1 763  ? 176.119 166.209 275.178 1.00 69.83  ? 746  ILE B N   1 
ATOM   5801  C CA  . ILE A 1 763  ? 175.166 165.310 274.529 1.00 69.83  ? 746  ILE B CA  1 
ATOM   5802  C C   . ILE A 1 763  ? 175.804 163.949 274.288 1.00 69.83  ? 746  ILE B C   1 
ATOM   5803  O O   . ILE A 1 763  ? 175.198 162.900 274.550 1.00 69.83  ? 746  ILE B O   1 
ATOM   5804  C CB  . ILE A 1 763  ? 174.653 165.923 273.216 1.00 69.83  ? 746  ILE B CB  1 
ATOM   5805  C CG1 . ILE A 1 763  ? 173.878 167.203 273.499 1.00 69.83  ? 746  ILE B CG1 1 
ATOM   5806  C CG2 . ILE A 1 763  ? 173.774 164.932 272.483 1.00 69.83  ? 746  ILE B CG2 1 
ATOM   5807  C CD1 . ILE A 1 763  ? 173.451 167.920 272.258 1.00 69.83  ? 746  ILE B CD1 1 
ATOM   5808  N N   . ILE A 1 764  ? 177.042 163.947 273.786 1.00 73.52  ? 747  ILE B N   1 
ATOM   5809  C CA  . ILE A 1 764  ? 177.727 162.687 273.506 1.00 73.52  ? 747  ILE B CA  1 
ATOM   5810  C C   . ILE A 1 764  ? 177.921 161.887 274.787 1.00 73.52  ? 747  ILE B C   1 
ATOM   5811  O O   . ILE A 1 764  ? 177.683 160.673 274.821 1.00 73.52  ? 747  ILE B O   1 
ATOM   5812  C CB  . ILE A 1 764  ? 179.066 162.952 272.796 1.00 73.52  ? 747  ILE B CB  1 
ATOM   5813  C CG1 . ILE A 1 764  ? 178.825 163.520 271.401 1.00 73.52  ? 747  ILE B CG1 1 
ATOM   5814  C CG2 . ILE A 1 764  ? 179.876 161.676 272.699 1.00 73.52  ? 747  ILE B CG2 1 
ATOM   5815  C CD1 . ILE A 1 764  ? 177.807 162.745 270.615 1.00 73.52  ? 747  ILE B CD1 1 
ATOM   5816  N N   . ASN A 1 765  ? 178.356 162.552 275.857 1.00 73.46  ? 748  ASN B N   1 
ATOM   5817  C CA  . ASN A 1 765  ? 178.581 161.861 277.121 1.00 73.46  ? 748  ASN B CA  1 
ATOM   5818  C C   . ASN A 1 765  ? 177.284 161.286 277.674 1.00 73.46  ? 748  ASN B C   1 
ATOM   5819  O O   . ASN A 1 765  ? 177.264 160.161 278.190 1.00 73.46  ? 748  ASN B O   1 
ATOM   5820  C CB  . ASN A 1 765  ? 179.220 162.817 278.126 1.00 73.46  ? 748  ASN B CB  1 
ATOM   5821  C CG  . ASN A 1 765  ? 179.387 162.202 279.499 1.00 73.46  ? 748  ASN B CG  1 
ATOM   5822  O OD1 . ASN A 1 765  ? 179.482 160.984 279.642 1.00 73.46  ? 748  ASN B OD1 1 
ATOM   5823  N ND2 . ASN A 1 765  ? 179.432 163.049 280.521 1.00 73.46  ? 748  ASN B ND2 1 
ATOM   5824  N N   . TYR A 1 766  ? 176.188 162.042 277.579 1.00 78.04  ? 749  TYR B N   1 
ATOM   5825  C CA  . TYR A 1 766  ? 174.912 161.538 278.074 1.00 78.04  ? 749  TYR B CA  1 
ATOM   5826  C C   . TYR A 1 766  ? 174.454 160.329 277.274 1.00 78.04  ? 749  TYR B C   1 
ATOM   5827  O O   . TYR A 1 766  ? 173.908 159.375 277.839 1.00 78.04  ? 749  TYR B O   1 
ATOM   5828  C CB  . TYR A 1 766  ? 173.849 162.634 278.034 1.00 78.04  ? 749  TYR B CB  1 
ATOM   5829  C CG  . TYR A 1 766  ? 172.453 162.118 278.293 1.00 78.04  ? 749  TYR B CG  1 
ATOM   5830  C CD1 . TYR A 1 766  ? 172.007 161.891 279.587 1.00 78.04  ? 749  TYR B CD1 1 
ATOM   5831  C CD2 . TYR A 1 766  ? 171.583 161.848 277.246 1.00 78.04  ? 749  TYR B CD2 1 
ATOM   5832  C CE1 . TYR A 1 766  ? 170.733 161.418 279.828 1.00 78.04  ? 749  TYR B CE1 1 
ATOM   5833  C CE2 . TYR A 1 766  ? 170.313 161.368 277.480 1.00 78.04  ? 749  TYR B CE2 1 
ATOM   5834  C CZ  . TYR A 1 766  ? 169.890 161.160 278.771 1.00 78.04  ? 749  TYR B CZ  1 
ATOM   5835  O OH  . TYR A 1 766  ? 168.619 160.687 279.005 1.00 78.04  ? 749  TYR B OH  1 
ATOM   5836  N N   . GLN A 1 767  ? 174.646 160.355 275.953 1.00 77.20  ? 750  GLN B N   1 
ATOM   5837  C CA  . GLN A 1 767  ? 174.284 159.189 275.154 1.00 77.20  ? 750  GLN B CA  1 
ATOM   5838  C C   . GLN A 1 767  ? 175.146 157.988 275.514 1.00 77.20  ? 750  GLN B C   1 
ATOM   5839  O O   . GLN A 1 767  ? 174.650 156.858 275.586 1.00 77.20  ? 750  GLN B O   1 
ATOM   5840  C CB  . GLN A 1 767  ? 174.396 159.498 273.664 1.00 77.20  ? 750  GLN B CB  1 
ATOM   5841  C CG  . GLN A 1 767  ? 174.331 158.260 272.773 1.00 77.20  ? 750  GLN B CG  1 
ATOM   5842  C CD  . GLN A 1 767  ? 172.934 157.667 272.653 1.00 77.20  ? 750  GLN B CD  1 
ATOM   5843  O OE1 . GLN A 1 767  ? 172.108 157.781 273.558 1.00 77.20  ? 750  GLN B OE1 1 
ATOM   5844  N NE2 . GLN A 1 767  ? 172.669 157.020 271.525 1.00 77.20  ? 750  GLN B NE2 1 
ATOM   5845  N N   . TYR A 1 768  ? 176.438 158.213 275.747 1.00 82.34  ? 751  TYR B N   1 
ATOM   5846  C CA  . TYR A 1 768  ? 177.314 157.119 276.149 1.00 82.34  ? 751  TYR B CA  1 
ATOM   5847  C C   . TYR A 1 768  ? 176.845 156.514 277.466 1.00 82.34  ? 751  TYR B C   1 
ATOM   5848  O O   . TYR A 1 768  ? 176.809 155.288 277.619 1.00 82.34  ? 751  TYR B O   1 
ATOM   5849  C CB  . TYR A 1 768  ? 178.751 157.628 276.274 1.00 82.34  ? 751  TYR B CB  1 
ATOM   5850  C CG  . TYR A 1 768  ? 179.800 156.584 276.600 1.00 82.34  ? 751  TYR B CG  1 
ATOM   5851  C CD1 . TYR A 1 768  ? 179.529 155.228 276.492 1.00 82.34  ? 751  TYR B CD1 1 
ATOM   5852  C CD2 . TYR A 1 768  ? 181.086 156.962 276.946 1.00 82.34  ? 751  TYR B CD2 1 
ATOM   5853  C CE1 . TYR A 1 768  ? 180.490 154.286 276.772 1.00 82.34  ? 751  TYR B CE1 1 
ATOM   5854  C CE2 . TYR A 1 768  ? 182.056 156.025 277.231 1.00 82.34  ? 751  TYR B CE2 1 
ATOM   5855  C CZ  . TYR A 1 768  ? 181.752 154.686 277.139 1.00 82.34  ? 751  TYR B CZ  1 
ATOM   5856  O OH  . TYR A 1 768  ? 182.716 153.744 277.416 1.00 82.34  ? 751  TYR B OH  1 
ATOM   5857  N N   . ASN A 1 769  ? 176.445 157.361 278.416 1.00 76.49  ? 752  ASN B N   1 
ATOM   5858  C CA  . ASN A 1 769  ? 176.120 156.889 279.757 1.00 76.49  ? 752  ASN B CA  1 
ATOM   5859  C C   . ASN A 1 769  ? 174.966 155.896 279.770 1.00 76.49  ? 752  ASN B C   1 
ATOM   5860  O O   . ASN A 1 769  ? 174.815 155.155 280.747 1.00 76.49  ? 752  ASN B O   1 
ATOM   5861  C CB  . ASN A 1 769  ? 175.779 158.079 280.655 1.00 76.49  ? 752  ASN B CB  1 
ATOM   5862  C CG  . ASN A 1 769  ? 177.009 158.794 281.170 1.00 76.49  ? 752  ASN B CG  1 
ATOM   5863  O OD1 . ASN A 1 769  ? 178.114 158.588 280.673 1.00 76.49  ? 752  ASN B OD1 1 
ATOM   5864  N ND2 . ASN A 1 769  ? 176.822 159.649 282.169 1.00 76.49  ? 752  ASN B ND2 1 
ATOM   5865  N N   . GLN A 1 770  ? 174.154 155.857 278.712 1.00 77.43  ? 753  GLN B N   1 
ATOM   5866  C CA  . GLN A 1 770  ? 172.924 155.074 278.712 1.00 77.43  ? 753  GLN B CA  1 
ATOM   5867  C C   . GLN A 1 770  ? 173.142 153.591 278.435 1.00 77.43  ? 753  GLN B C   1 
ATOM   5868  O O   . GLN A 1 770  ? 172.227 152.798 278.680 1.00 77.43  ? 753  GLN B O   1 
ATOM   5869  C CB  . GLN A 1 770  ? 171.947 155.637 277.677 1.00 77.43  ? 753  GLN B CB  1 
ATOM   5870  C CG  . GLN A 1 770  ? 171.287 156.948 278.075 1.00 77.43  ? 753  GLN B CG  1 
ATOM   5871  C CD  . GLN A 1 770  ? 170.885 156.984 279.533 1.00 77.43  ? 753  GLN B CD  1 
ATOM   5872  O OE1 . GLN A 1 770  ? 170.072 156.180 279.984 1.00 77.43  ? 753  GLN B OE1 1 
ATOM   5873  N NE2 . GLN A 1 770  ? 171.451 157.924 280.279 1.00 77.43  ? 753  GLN B NE2 1 
ATOM   5874  N N   . TYR A 1 771  ? 174.312 153.195 277.943 1.00 82.90  ? 754  TYR B N   1 
ATOM   5875  C CA  . TYR A 1 771  ? 174.532 151.822 277.513 1.00 82.90  ? 754  TYR B CA  1 
ATOM   5876  C C   . TYR A 1 771  ? 174.654 150.878 278.709 1.00 82.90  ? 754  TYR B C   1 
ATOM   5877  O O   . TYR A 1 771  ? 174.613 151.285 279.872 1.00 82.90  ? 754  TYR B O   1 
ATOM   5878  C CB  . TYR A 1 771  ? 175.779 151.732 276.639 1.00 82.90  ? 754  TYR B CB  1 
ATOM   5879  C CG  . TYR A 1 771  ? 175.669 152.443 275.313 1.00 82.90  ? 754  TYR B CG  1 
ATOM   5880  C CD1 . TYR A 1 771  ? 174.432 152.741 274.763 1.00 82.90  ? 754  TYR B CD1 1 
ATOM   5881  C CD2 . TYR A 1 771  ? 176.805 152.808 274.608 1.00 82.90  ? 754  TYR B CD2 1 
ATOM   5882  C CE1 . TYR A 1 771  ? 174.333 153.386 273.551 1.00 82.90  ? 754  TYR B CE1 1 
ATOM   5883  C CE2 . TYR A 1 771  ? 176.716 153.452 273.398 1.00 82.90  ? 754  TYR B CE2 1 
ATOM   5884  C CZ  . TYR A 1 771  ? 175.480 153.740 272.875 1.00 82.90  ? 754  TYR B CZ  1 
ATOM   5885  O OH  . TYR A 1 771  ? 175.390 154.385 271.666 1.00 82.90  ? 754  TYR B OH  1 
ATOM   5886  N N   . THR A 1 772  ? 174.800 149.590 278.406 1.00 92.82  ? 755  THR B N   1 
ATOM   5887  C CA  . THR A 1 772  ? 175.061 148.561 279.399 1.00 92.82  ? 755  THR B CA  1 
ATOM   5888  C C   . THR A 1 772  ? 176.562 148.302 279.498 1.00 92.82  ? 755  THR B C   1 
ATOM   5889  O O   . THR A 1 772  ? 177.347 148.732 278.651 1.00 92.82  ? 755  THR B O   1 
ATOM   5890  C CB  . THR A 1 772  ? 174.323 147.270 279.048 1.00 92.82  ? 755  THR B CB  1 
ATOM   5891  O OG1 . THR A 1 772  ? 175.110 146.507 278.127 1.00 92.82  ? 755  THR B OG1 1 
ATOM   5892  C CG2 . THR A 1 772  ? 172.976 147.583 278.411 1.00 92.82  ? 755  THR B CG2 1 
ATOM   5893  N N   . GLU A 1 773  ? 176.959 147.583 280.552 1.00 95.02  ? 756  GLU B N   1 
ATOM   5894  C CA  . GLU A 1 773  ? 178.380 147.445 280.865 1.00 95.02  ? 756  GLU B CA  1 
ATOM   5895  C C   . GLU A 1 773  ? 179.147 146.771 279.734 1.00 95.02  ? 756  GLU B C   1 
ATOM   5896  O O   . GLU A 1 773  ? 180.241 147.219 279.361 1.00 95.02  ? 756  GLU B O   1 
ATOM   5897  C CB  . GLU A 1 773  ? 178.558 146.664 282.169 1.00 95.02  ? 756  GLU B CB  1 
ATOM   5898  C CG  . GLU A 1 773  ? 179.926 146.820 282.835 1.00 95.02  ? 756  GLU B CG  1 
ATOM   5899  C CD  . GLU A 1 773  ? 180.462 148.246 282.829 1.00 95.02  ? 756  GLU B CD  1 
ATOM   5900  O OE1 . GLU A 1 773  ? 181.699 148.409 282.778 1.00 95.02  ? 756  GLU B OE1 1 
ATOM   5901  O OE2 . GLU A 1 773  ? 179.666 149.203 282.934 1.00 95.02  ? 756  GLU B OE2 1 
ATOM   5902  N N   . GLU A 1 774  ? 178.593 145.692 279.178 1.00 95.57  ? 757  GLU B N   1 
ATOM   5903  C CA  . GLU A 1 774  ? 179.239 145.033 278.050 1.00 95.57  ? 757  GLU B CA  1 
ATOM   5904  C C   . GLU A 1 774  ? 179.352 145.977 276.860 1.00 95.57  ? 757  GLU B C   1 
ATOM   5905  O O   . GLU A 1 774  ? 180.348 145.950 276.128 1.00 95.57  ? 757  GLU B O   1 
ATOM   5906  C CB  . GLU A 1 774  ? 178.476 143.759 277.684 1.00 95.57  ? 757  GLU B CB  1 
ATOM   5907  C CG  . GLU A 1 774  ? 177.167 143.983 276.950 1.00 95.57  ? 757  GLU B CG  1 
ATOM   5908  C CD  . GLU A 1 774  ? 176.218 142.813 277.085 1.00 95.57  ? 757  GLU B CD  1 
ATOM   5909  O OE1 . GLU A 1 774  ? 176.636 141.766 277.621 1.00 95.57  ? 757  GLU B OE1 1 
ATOM   5910  O OE2 . GLU A 1 774  ? 175.051 142.942 276.660 1.00 95.57  ? 757  GLU B OE2 1 
ATOM   5911  N N   . GLU A 1 775  ? 178.352 146.840 276.667 1.00 92.21  ? 758  GLU B N   1 
ATOM   5912  C CA  . GLU A 1 775  ? 178.414 147.810 275.580 1.00 92.21  ? 758  GLU B CA  1 
ATOM   5913  C C   . GLU A 1 775  ? 179.510 148.842 275.816 1.00 92.21  ? 758  GLU B C   1 
ATOM   5914  O O   . GLU A 1 775  ? 180.216 149.224 274.877 1.00 92.21  ? 758  GLU B O   1 
ATOM   5915  C CB  . GLU A 1 775  ? 177.058 148.490 275.402 1.00 92.21  ? 758  GLU B CB  1 
ATOM   5916  C CG  . GLU A 1 775  ? 176.224 147.934 274.257 1.00 92.21  ? 758  GLU B CG  1 
ATOM   5917  C CD  . GLU A 1 775  ? 175.267 146.844 274.695 1.00 92.21  ? 758  GLU B CD  1 
ATOM   5918  O OE1 . GLU A 1 775  ? 175.072 146.677 275.915 1.00 92.21  ? 758  GLU B OE1 1 
ATOM   5919  O OE2 . GLU A 1 775  ? 174.700 146.160 273.819 1.00 92.21  ? 758  GLU B OE2 1 
ATOM   5920  N N   . LYS A 1 776  ? 179.668 149.317 277.055 1.00 91.65  ? 759  LYS B N   1 
ATOM   5921  C CA  . LYS A 1 776  ? 180.730 150.285 277.308 1.00 91.65  ? 759  LYS B CA  1 
ATOM   5922  C C   . LYS A 1 776  ? 182.110 149.662 277.144 1.00 91.65  ? 759  LYS B C   1 
ATOM   5923  O O   . LYS A 1 776  ? 183.007 150.288 276.568 1.00 91.65  ? 759  LYS B O   1 
ATOM   5924  C CB  . LYS A 1 776  ? 180.603 150.924 278.695 1.00 91.65  ? 759  LYS B CB  1 
ATOM   5925  C CG  . LYS A 1 776  ? 179.417 151.866 278.879 1.00 91.65  ? 759  LYS B CG  1 
ATOM   5926  C CD  . LYS A 1 776  ? 178.979 151.980 280.334 1.00 91.65  ? 759  LYS B CD  1 
ATOM   5927  C CE  . LYS A 1 776  ? 177.863 151.038 280.693 1.00 91.65  ? 759  LYS B CE  1 
ATOM   5928  N NZ  . LYS A 1 776  ? 177.997 150.532 282.084 1.00 91.65  ? 759  LYS B NZ  1 
ATOM   5929  N N   . ASN A 1 777  ? 182.313 148.436 277.637 1.00 96.16  ? 760  ASN B N   1 
ATOM   5930  C CA  . ASN A 1 777  ? 183.658 147.871 277.542 1.00 96.16  ? 760  ASN B CA  1 
ATOM   5931  C C   . ASN A 1 777  ? 183.990 147.386 276.135 1.00 96.16  ? 760  ASN B C   1 
ATOM   5932  O O   . ASN A 1 777  ? 185.150 147.470 275.721 1.00 96.16  ? 760  ASN B O   1 
ATOM   5933  C CB  . ASN A 1 777  ? 183.853 146.735 278.549 1.00 96.16  ? 760  ASN B CB  1 
ATOM   5934  C CG  . ASN A 1 777  ? 182.723 145.737 278.535 1.00 96.16  ? 760  ASN B CG  1 
ATOM   5935  O OD1 . ASN A 1 777  ? 182.532 145.009 277.562 1.00 96.16  ? 760  ASN B OD1 1 
ATOM   5936  N ND2 . ASN A 1 777  ? 181.982 145.675 279.633 1.00 96.16  ? 760  ASN B ND2 1 
ATOM   5937  N N   . ASN A 1 778  ? 183.008 146.876 275.388 1.00 93.08  ? 761  ASN B N   1 
ATOM   5938  C CA  . ASN A 1 778  ? 183.279 146.478 274.010 1.00 93.08  ? 761  ASN B CA  1 
ATOM   5939  C C   . ASN A 1 778  ? 183.454 147.687 273.101 1.00 93.08  ? 761  ASN B C   1 
ATOM   5940  O O   . ASN A 1 778  ? 184.334 147.693 272.235 1.00 93.08  ? 761  ASN B O   1 
ATOM   5941  C CB  . ASN A 1 778  ? 182.161 145.579 273.486 1.00 93.08  ? 761  ASN B CB  1 
ATOM   5942  C CG  . ASN A 1 778  ? 182.412 144.114 273.770 1.00 93.08  ? 761  ASN B CG  1 
ATOM   5943  O OD1 . ASN A 1 778  ? 182.693 143.334 272.863 1.00 93.08  ? 761  ASN B OD1 1 
ATOM   5944  N ND2 . ASN A 1 778  ? 182.312 143.733 275.037 1.00 93.08  ? 761  ASN B ND2 1 
ATOM   5945  N N   . ILE A 1 779  ? 182.629 148.712 273.278 1.00 95.61  ? 762  ILE B N   1 
ATOM   5946  C CA  . ILE A 1 779  ? 182.694 149.934 272.485 1.00 95.61  ? 762  ILE B CA  1 
ATOM   5947  C C   . ILE A 1 779  ? 183.256 151.017 273.398 1.00 95.61  ? 762  ILE B C   1 
ATOM   5948  O O   . ILE A 1 779  ? 182.515 151.657 274.153 1.00 95.61  ? 762  ILE B O   1 
ATOM   5949  C CB  . ILE A 1 779  ? 181.325 150.328 271.918 1.00 95.61  ? 762  ILE B CB  1 
ATOM   5950  C CG1 . ILE A 1 779  ? 180.769 149.232 271.000 1.00 95.61  ? 762  ILE B CG1 1 
ATOM   5951  C CG2 . ILE A 1 779  ? 181.420 151.641 271.163 1.00 95.61  ? 762  ILE B CG2 1 
ATOM   5952  C CD1 . ILE A 1 779  ? 181.815 148.446 270.226 1.00 95.61  ? 762  ILE B CD1 1 
ATOM   5953  N N   . ASN A 1 780  ? 184.567 151.227 273.333 1.00 97.82  ? 763  ASN B N   1 
ATOM   5954  C CA  . ASN A 1 780  ? 185.246 152.153 274.228 1.00 97.82  ? 763  ASN B CA  1 
ATOM   5955  C C   . ASN A 1 780  ? 185.331 153.536 273.597 1.00 97.82  ? 763  ASN B C   1 
ATOM   5956  O O   . ASN A 1 780  ? 185.770 153.680 272.452 1.00 97.82  ? 763  ASN B O   1 
ATOM   5957  C CB  . ASN A 1 780  ? 186.647 151.646 274.567 1.00 97.82  ? 763  ASN B CB  1 
ATOM   5958  C CG  . ASN A 1 780  ? 186.696 150.920 275.895 1.00 97.82  ? 763  ASN B CG  1 
ATOM   5959  O OD1 . ASN A 1 780  ? 185.820 150.116 276.208 1.00 97.82  ? 763  ASN B OD1 1 
ATOM   5960  N ND2 . ASN A 1 780  ? 187.726 151.202 276.684 1.00 97.82  ? 763  ASN B ND2 1 
ATOM   5961  N N   . PHE A 1 781  ? 184.911 154.548 274.352 1.00 95.16  ? 764  PHE B N   1 
ATOM   5962  C CA  . PHE A 1 781  ? 185.015 155.935 273.925 1.00 95.16  ? 764  PHE B CA  1 
ATOM   5963  C C   . PHE A 1 781  ? 185.556 156.753 275.085 1.00 95.16  ? 764  PHE B C   1 
ATOM   5964  O O   . PHE A 1 781  ? 185.090 156.609 276.218 1.00 95.16  ? 764  PHE B O   1 
ATOM   5965  C CB  . PHE A 1 781  ? 183.656 156.478 273.469 1.00 95.16  ? 764  PHE B CB  1 
ATOM   5966  C CG  . PHE A 1 781  ? 183.538 157.974 273.547 1.00 95.16  ? 764  PHE B CG  1 
ATOM   5967  C CD1 . PHE A 1 781  ? 184.047 158.775 272.541 1.00 95.16  ? 764  PHE B CD1 1 
ATOM   5968  C CD2 . PHE A 1 781  ? 182.902 158.580 274.618 1.00 95.16  ? 764  PHE B CD2 1 
ATOM   5969  C CE1 . PHE A 1 781  ? 183.933 160.147 272.607 1.00 95.16  ? 764  PHE B CE1 1 
ATOM   5970  C CE2 . PHE A 1 781  ? 182.788 159.952 274.690 1.00 95.16  ? 764  PHE B CE2 1 
ATOM   5971  C CZ  . PHE A 1 781  ? 183.302 160.736 273.684 1.00 95.16  ? 764  PHE B CZ  1 
ATOM   5972  N N   . ASN A 1 782  ? 186.538 157.602 274.802 1.00 102.81 ? 765  ASN B N   1 
ATOM   5973  C CA  . ASN A 1 782  ? 187.145 158.460 275.805 1.00 102.81 ? 765  ASN B CA  1 
ATOM   5974  C C   . ASN A 1 782  ? 186.875 159.917 275.458 1.00 102.81 ? 765  ASN B C   1 
ATOM   5975  O O   . ASN A 1 782  ? 186.654 160.271 274.298 1.00 102.81 ? 765  ASN B O   1 
ATOM   5976  C CB  . ASN A 1 782  ? 188.653 158.202 275.920 1.00 102.81 ? 765  ASN B CB  1 
ATOM   5977  C CG  . ASN A 1 782  ? 189.430 158.753 274.745 1.00 102.81 ? 765  ASN B CG  1 
ATOM   5978  O OD1 . ASN A 1 782  ? 189.457 158.155 273.669 1.00 102.81 ? 765  ASN B OD1 1 
ATOM   5979  N ND2 . ASN A 1 782  ? 190.076 159.895 274.946 1.00 102.81 ? 765  ASN B ND2 1 
ATOM   5980  N N   . ILE A 1 783  ? 186.888 160.762 276.485 1.00 103.70 ? 766  ILE B N   1 
ATOM   5981  C CA  . ILE A 1 783  ? 186.480 162.151 276.315 1.00 103.70 ? 766  ILE B CA  1 
ATOM   5982  C C   . ILE A 1 783  ? 187.655 163.071 275.981 1.00 103.70 ? 766  ILE B C   1 
ATOM   5983  O O   . ILE A 1 783  ? 187.479 164.053 275.250 1.00 103.70 ? 766  ILE B O   1 
ATOM   5984  C CB  . ILE A 1 783  ? 185.735 162.621 277.578 1.00 103.70 ? 766  ILE B CB  1 
ATOM   5985  C CG1 . ILE A 1 783  ? 184.288 162.122 277.552 1.00 103.70 ? 766  ILE B CG1 1 
ATOM   5986  C CG2 . ILE A 1 783  ? 185.773 164.134 277.726 1.00 103.70 ? 766  ILE B CG2 1 
ATOM   5987  C CD1 . ILE A 1 783  ? 183.387 162.906 276.621 1.00 103.70 ? 766  ILE B CD1 1 
ATOM   5988  N N   . ASP A 1 784  ? 188.856 162.759 276.474 1.00 106.35 ? 767  ASP B N   1 
ATOM   5989  C CA  . ASP A 1 784  ? 189.980 163.683 276.336 1.00 106.35 ? 767  ASP B CA  1 
ATOM   5990  C C   . ASP A 1 784  ? 190.338 163.927 274.874 1.00 106.35 ? 767  ASP B C   1 
ATOM   5991  O O   . ASP A 1 784  ? 190.572 165.073 274.471 1.00 106.35 ? 767  ASP B O   1 
ATOM   5992  C CB  . ASP A 1 784  ? 191.189 163.151 277.103 1.00 106.35 ? 767  ASP B CB  1 
ATOM   5993  C CG  . ASP A 1 784  ? 191.342 163.794 278.468 1.00 106.35 ? 767  ASP B CG  1 
ATOM   5994  O OD1 . ASP A 1 784  ? 190.314 163.997 279.148 1.00 106.35 ? 767  ASP B OD1 1 
ATOM   5995  O OD2 . ASP A 1 784  ? 192.488 164.098 278.861 1.00 106.35 ? 767  ASP B OD2 1 
ATOM   5996  N N   . ASP A 1 785  ? 190.392 162.867 274.064 1.00 105.12 ? 768  ASP B N   1 
ATOM   5997  C CA  . ASP A 1 785  ? 190.734 163.041 272.655 1.00 105.12 ? 768  ASP B CA  1 
ATOM   5998  C C   . ASP A 1 785  ? 189.665 163.842 271.919 1.00 105.12 ? 768  ASP B C   1 
ATOM   5999  O O   . ASP A 1 785  ? 189.985 164.690 271.075 1.00 105.12 ? 768  ASP B O   1 
ATOM   6000  C CB  . ASP A 1 785  ? 190.946 161.681 271.990 1.00 105.12 ? 768  ASP B CB  1 
ATOM   6001  C CG  . ASP A 1 785  ? 189.697 160.823 271.998 1.00 105.12 ? 768  ASP B CG  1 
ATOM   6002  O OD1 . ASP A 1 785  ? 188.754 161.151 272.747 1.00 105.12 ? 768  ASP B OD1 1 
ATOM   6003  O OD2 . ASP A 1 785  ? 189.659 159.820 271.255 1.00 105.12 ? 768  ASP B OD2 1 
ATOM   6004  N N   . LEU A 1 786  ? 188.389 163.579 272.221 1.00 96.90  ? 769  LEU B N   1 
ATOM   6005  C CA  . LEU A 1 786  ? 187.311 164.346 271.608 1.00 96.90  ? 769  LEU B CA  1 
ATOM   6006  C C   . LEU A 1 786  ? 187.428 165.822 271.959 1.00 96.90  ? 769  LEU B C   1 
ATOM   6007  O O   . LEU A 1 786  ? 187.294 166.690 271.088 1.00 96.90  ? 769  LEU B O   1 
ATOM   6008  C CB  . LEU A 1 786  ? 185.958 163.794 272.053 1.00 96.90  ? 769  LEU B CB  1 
ATOM   6009  C CG  . LEU A 1 786  ? 184.728 164.663 271.782 1.00 96.90  ? 769  LEU B CG  1 
ATOM   6010  C CD1 . LEU A 1 786  ? 184.549 164.898 270.296 1.00 96.90  ? 769  LEU B CD1 1 
ATOM   6011  C CD2 . LEU A 1 786  ? 183.482 164.033 272.374 1.00 96.90  ? 769  LEU B CD2 1 
ATOM   6012  N N   . SER A 1 787  ? 187.697 166.121 273.231 1.00 97.84  ? 770  SER B N   1 
ATOM   6013  C CA  . SER A 1 787  ? 187.865 167.509 273.643 1.00 97.84  ? 770  SER B CA  1 
ATOM   6014  C C   . SER A 1 787  ? 189.047 168.149 272.931 1.00 97.84  ? 770  SER B C   1 
ATOM   6015  O O   . SER A 1 787  ? 188.966 169.301 272.494 1.00 97.84  ? 770  SER B O   1 
ATOM   6016  C CB  . SER A 1 787  ? 188.044 167.588 275.158 1.00 97.84  ? 770  SER B CB  1 
ATOM   6017  O OG  . SER A 1 787  ? 186.919 167.056 275.833 1.00 97.84  ? 770  SER B OG  1 
ATOM   6018  N N   . SER A 1 788  ? 190.152 167.412 272.797 1.00 97.35  ? 771  SER B N   1 
ATOM   6019  C CA  . SER A 1 788  ? 191.332 167.963 272.140 1.00 97.35  ? 771  SER B CA  1 
ATOM   6020  C C   . SER A 1 788  ? 191.057 168.289 270.677 1.00 97.35  ? 771  SER B C   1 
ATOM   6021  O O   . SER A 1 788  ? 191.435 169.363 270.190 1.00 97.35  ? 771  SER B O   1 
ATOM   6022  C CB  . SER A 1 788  ? 192.502 166.988 272.261 1.00 97.35  ? 771  SER B CB  1 
ATOM   6023  O OG  . SER A 1 788  ? 192.980 166.930 273.593 1.00 97.35  ? 771  SER B OG  1 
ATOM   6024  N N   . LYS A 1 789  ? 190.394 167.381 269.956 1.00 97.33  ? 772  LYS B N   1 
ATOM   6025  C CA  . LYS A 1 789  ? 190.148 167.641 268.540 1.00 97.33  ? 772  LYS B CA  1 
ATOM   6026  C C   . LYS A 1 789  ? 189.114 168.745 268.350 1.00 97.33  ? 772  LYS B C   1 
ATOM   6027  O O   . LYS A 1 789  ? 189.232 169.563 267.426 1.00 97.33  ? 772  LYS B O   1 
ATOM   6028  C CB  . LYS A 1 789  ? 189.731 166.359 267.818 1.00 97.33  ? 772  LYS B CB  1 
ATOM   6029  C CG  . LYS A 1 789  ? 188.465 165.707 268.320 1.00 97.33  ? 772  LYS B CG  1 
ATOM   6030  C CD  . LYS A 1 789  ? 188.600 164.195 268.289 1.00 97.33  ? 772  LYS B CD  1 
ATOM   6031  C CE  . LYS A 1 789  ? 188.864 163.697 266.883 1.00 97.33  ? 772  LYS B CE  1 
ATOM   6032  N NZ  . LYS A 1 789  ? 187.708 163.953 265.989 1.00 97.33  ? 772  LYS B NZ  1 
ATOM   6033  N N   . LEU A 1 790  ? 188.106 168.811 269.224 1.00 92.19  ? 773  LEU B N   1 
ATOM   6034  C CA  . LEU A 1 790  ? 187.162 169.919 269.142 1.00 92.19  ? 773  LEU B CA  1 
ATOM   6035  C C   . LEU A 1 790  ? 187.852 171.247 269.429 1.00 92.19  ? 773  LEU B C   1 
ATOM   6036  O O   . LEU A 1 790  ? 187.561 172.258 268.781 1.00 92.19  ? 773  LEU B O   1 
ATOM   6037  C CB  . LEU A 1 790  ? 185.992 169.694 270.099 1.00 92.19  ? 773  LEU B CB  1 
ATOM   6038  C CG  . LEU A 1 790  ? 185.078 168.506 269.782 1.00 92.19  ? 773  LEU B CG  1 
ATOM   6039  C CD1 . LEU A 1 790  ? 183.712 168.687 270.415 1.00 92.19  ? 773  LEU B CD1 1 
ATOM   6040  C CD2 . LEU A 1 790  ? 184.952 168.288 268.285 1.00 92.19  ? 773  LEU B CD2 1 
ATOM   6041  N N   . ASN A 1 791  ? 188.783 171.262 270.387 1.00 93.15  ? 774  ASN B N   1 
ATOM   6042  C CA  . ASN A 1 791  ? 189.531 172.481 270.672 1.00 93.15  ? 774  ASN B CA  1 
ATOM   6043  C C   . ASN A 1 791  ? 190.399 172.888 269.489 1.00 93.15  ? 774  ASN B C   1 
ATOM   6044  O O   . ASN A 1 791  ? 190.530 174.080 269.187 1.00 93.15  ? 774  ASN B O   1 
ATOM   6045  C CB  . ASN A 1 791  ? 190.386 172.290 271.923 1.00 93.15  ? 774  ASN B CB  1 
ATOM   6046  C CG  . ASN A 1 791  ? 189.571 172.345 273.197 1.00 93.15  ? 774  ASN B CG  1 
ATOM   6047  O OD1 . ASN A 1 791  ? 188.607 173.102 273.297 1.00 93.15  ? 774  ASN B OD1 1 
ATOM   6048  N ND2 . ASN A 1 791  ? 189.954 171.540 274.180 1.00 93.15  ? 774  ASN B ND2 1 
ATOM   6049  N N   . GLU A 1 792  ? 191.015 171.915 268.814 1.00 91.68  ? 775  GLU B N   1 
ATOM   6050  C CA  . GLU A 1 792  ? 191.822 172.255 267.646 1.00 91.68  ? 775  GLU B CA  1 
ATOM   6051  C C   . GLU A 1 792  ? 190.953 172.820 266.526 1.00 91.68  ? 775  GLU B C   1 
ATOM   6052  O O   . GLU A 1 792  ? 191.351 173.773 265.844 1.00 91.68  ? 775  GLU B O   1 
ATOM   6053  C CB  . GLU A 1 792  ? 192.630 171.038 267.181 1.00 91.68  ? 775  GLU B CB  1 
ATOM   6054  C CG  . GLU A 1 792  ? 191.997 170.188 266.093 1.00 91.68  ? 775  GLU B CG  1 
ATOM   6055  C CD  . GLU A 1 792  ? 192.781 168.920 265.816 1.00 91.68  ? 775  GLU B CD  1 
ATOM   6056  O OE1 . GLU A 1 792  ? 194.028 168.977 265.828 1.00 91.68  ? 775  GLU B OE1 1 
ATOM   6057  O OE2 . GLU A 1 792  ? 192.149 167.868 265.587 1.00 91.68  ? 775  GLU B OE2 1 
ATOM   6058  N N   . SER A 1 793  ? 189.749 172.270 266.341 1.00 89.77  ? 776  SER B N   1 
ATOM   6059  C CA  . SER A 1 793  ? 188.834 172.836 265.352 1.00 89.77  ? 776  SER B CA  1 
ATOM   6060  C C   . SER A 1 793  ? 188.416 174.251 265.738 1.00 89.77  ? 776  SER B C   1 
ATOM   6061  O O   . SER A 1 793  ? 188.298 175.136 264.878 1.00 89.77  ? 776  SER B O   1 
ATOM   6062  C CB  . SER A 1 793  ? 187.611 171.935 265.194 1.00 89.77  ? 776  SER B CB  1 
ATOM   6063  O OG  . SER A 1 793  ? 187.999 170.602 264.917 1.00 89.77  ? 776  SER B OG  1 
ATOM   6064  N N   . ILE A 1 794  ? 188.187 174.479 267.033 1.00 87.95  ? 777  ILE B N   1 
ATOM   6065  C CA  . ILE A 1 794  ? 187.830 175.811 267.509 1.00 87.95  ? 777  ILE B CA  1 
ATOM   6066  C C   . ILE A 1 794  ? 188.953 176.796 267.217 1.00 87.95  ? 777  ILE B C   1 
ATOM   6067  O O   . ILE A 1 794  ? 188.707 177.924 266.783 1.00 87.95  ? 777  ILE B O   1 
ATOM   6068  C CB  . ILE A 1 794  ? 187.485 175.770 269.009 1.00 87.95  ? 777  ILE B CB  1 
ATOM   6069  C CG1 . ILE A 1 794  ? 186.129 175.099 269.229 1.00 87.95  ? 777  ILE B CG1 1 
ATOM   6070  C CG2 . ILE A 1 794  ? 187.477 177.167 269.598 1.00 87.95  ? 777  ILE B CG2 1 
ATOM   6071  C CD1 . ILE A 1 794  ? 185.133 175.358 268.126 1.00 87.95  ? 777  ILE B CD1 1 
ATOM   6072  N N   . ASN A 1 795  ? 190.201 176.387 267.451 1.00 88.18  ? 778  ASN B N   1 
ATOM   6073  C CA  . ASN A 1 795  ? 191.333 177.259 267.146 1.00 88.18  ? 778  ASN B CA  1 
ATOM   6074  C C   . ASN A 1 795  ? 191.424 177.546 265.651 1.00 88.18  ? 778  ASN B C   1 
ATOM   6075  O O   . ASN A 1 795  ? 191.706 178.683 265.239 1.00 88.18  ? 778  ASN B O   1 
ATOM   6076  C CB  . ASN A 1 795  ? 192.631 176.628 267.646 1.00 88.18  ? 778  ASN B CB  1 
ATOM   6077  C CG  . ASN A 1 795  ? 192.815 176.782 269.140 1.00 88.18  ? 778  ASN B CG  1 
ATOM   6078  O OD1 . ASN A 1 795  ? 193.794 176.298 269.709 1.00 88.18  ? 778  ASN B OD1 1 
ATOM   6079  N ND2 . ASN A 1 795  ? 191.874 177.458 269.786 1.00 88.18  ? 778  ASN B ND2 1 
ATOM   6080  N N   . LYS A 1 796  ? 191.194 176.524 264.823 1.00 87.86  ? 779  LYS B N   1 
ATOM   6081  C CA  . LYS A 1 796  ? 191.247 176.719 263.378 1.00 87.86  ? 779  LYS B CA  1 
ATOM   6082  C C   . LYS A 1 796  ? 190.207 177.734 262.922 1.00 87.86  ? 779  LYS B C   1 
ATOM   6083  O O   . LYS A 1 796  ? 190.490 178.582 262.068 1.00 87.86  ? 779  LYS B O   1 
ATOM   6084  C CB  . LYS A 1 796  ? 191.051 175.385 262.660 1.00 87.86  ? 779  LYS B CB  1 
ATOM   6085  C CG  . LYS A 1 796  ? 192.204 174.414 262.844 1.00 87.86  ? 779  LYS B CG  1 
ATOM   6086  C CD  . LYS A 1 796  ? 192.338 173.477 261.657 1.00 87.86  ? 779  LYS B CD  1 
ATOM   6087  C CE  . LYS A 1 796  ? 191.336 172.338 261.743 1.00 87.86  ? 779  LYS B CE  1 
ATOM   6088  N NZ  . LYS A 1 796  ? 191.888 171.072 261.191 1.00 87.86  ? 779  LYS B NZ  1 
ATOM   6089  N N   . ALA A 1 797  ? 188.996 177.664 263.478 1.00 85.42  ? 780  ALA B N   1 
ATOM   6090  C CA  . ALA A 1 797  ? 187.990 178.673 263.155 1.00 85.42  ? 780  ALA B CA  1 
ATOM   6091  C C   . ALA A 1 797  ? 188.350 180.037 263.737 1.00 85.42  ? 780  ALA B C   1 
ATOM   6092  O O   . ALA A 1 797  ? 188.067 181.076 263.122 1.00 85.42  ? 780  ALA B O   1 
ATOM   6093  C CB  . ALA A 1 797  ? 186.619 178.229 263.660 1.00 85.42  ? 780  ALA B CB  1 
ATOM   6094  N N   . MET A 1 798  ? 188.970 180.048 264.918 1.00 85.20  ? 781  MET B N   1 
ATOM   6095  C CA  . MET A 1 798  ? 189.278 181.296 265.599 1.00 85.20  ? 781  MET B CA  1 
ATOM   6096  C C   . MET A 1 798  ? 190.313 182.100 264.831 1.00 85.20  ? 781  MET B C   1 
ATOM   6097  O O   . MET A 1 798  ? 190.289 183.334 264.871 1.00 85.20  ? 781  MET B O   1 
ATOM   6098  C CB  . MET A 1 798  ? 189.766 180.993 267.014 1.00 85.20  ? 781  MET B CB  1 
ATOM   6099  C CG  . MET A 1 798  ? 188.682 181.083 268.076 1.00 85.20  ? 781  MET B CG  1 
ATOM   6100  S SD  . MET A 1 798  ? 187.809 182.656 268.146 1.00 85.20  ? 781  MET B SD  1 
ATOM   6101  C CE  . MET A 1 798  ? 189.141 183.750 268.614 1.00 85.20  ? 781  MET B CE  1 
ATOM   6102  N N   . ILE A 1 799  ? 191.219 181.424 264.123 1.00 83.67  ? 782  ILE B N   1 
ATOM   6103  C CA  . ILE A 1 799  ? 192.181 182.143 263.286 1.00 83.67  ? 782  ILE B CA  1 
ATOM   6104  C C   . ILE A 1 799  ? 191.456 182.961 262.220 1.00 83.67  ? 782  ILE B C   1 
ATOM   6105  O O   . ILE A 1 799  ? 191.737 184.153 262.021 1.00 83.67  ? 782  ILE B O   1 
ATOM   6106  C CB  . ILE A 1 799  ? 193.185 181.165 262.652 1.00 83.67  ? 782  ILE B CB  1 
ATOM   6107  C CG1 . ILE A 1 799  ? 193.930 180.382 263.731 1.00 83.67  ? 782  ILE B CG1 1 
ATOM   6108  C CG2 . ILE A 1 799  ? 194.161 181.913 261.765 1.00 83.67  ? 782  ILE B CG2 1 
ATOM   6109  C CD1 . ILE A 1 799  ? 194.729 179.220 263.191 1.00 83.67  ? 782  ILE B CD1 1 
ATOM   6110  N N   . ASN A 1 800  ? 190.507 182.333 261.522 1.00 84.48  ? 783  ASN B N   1 
ATOM   6111  C CA  . ASN A 1 800  ? 189.758 183.039 260.486 1.00 84.48  ? 783  ASN B CA  1 
ATOM   6112  C C   . ASN A 1 800  ? 188.924 184.166 261.079 1.00 84.48  ? 783  ASN B C   1 
ATOM   6113  O O   . ASN A 1 800  ? 188.827 185.252 260.492 1.00 84.48  ? 783  ASN B O   1 
ATOM   6114  C CB  . ASN A 1 800  ? 188.866 182.062 259.723 1.00 84.48  ? 783  ASN B CB  1 
ATOM   6115  C CG  . ASN A 1 800  ? 189.652 181.152 258.805 1.00 84.48  ? 783  ASN B CG  1 
ATOM   6116  O OD1 . ASN A 1 800  ? 190.835 181.377 258.556 1.00 84.48  ? 783  ASN B OD1 1 
ATOM   6117  N ND2 . ASN A 1 800  ? 188.997 180.117 258.294 1.00 84.48  ? 783  ASN B ND2 1 
ATOM   6118  N N   . ILE A 1 801  ? 188.304 183.923 262.235 1.00 82.25  ? 784  ILE B N   1 
ATOM   6119  C CA  . ILE A 1 801  ? 187.502 184.971 262.864 1.00 82.25  ? 784  ILE B CA  1 
ATOM   6120  C C   . ILE A 1 801  ? 188.375 186.165 263.231 1.00 82.25  ? 784  ILE B C   1 
ATOM   6121  O O   . ILE A 1 801  ? 187.989 187.324 263.025 1.00 82.25  ? 784  ILE B O   1 
ATOM   6122  C CB  . ILE A 1 801  ? 186.753 184.417 264.089 1.00 82.25  ? 784  ILE B CB  1 
ATOM   6123  C CG1 . ILE A 1 801  ? 185.769 183.331 263.660 1.00 82.25  ? 784  ILE B CG1 1 
ATOM   6124  C CG2 . ILE A 1 801  ? 186.018 185.531 264.806 1.00 82.25  ? 784  ILE B CG2 1 
ATOM   6125  C CD1 . ILE A 1 801  ? 185.465 182.325 264.739 1.00 82.25  ? 784  ILE B CD1 1 
ATOM   6126  N N   . ASN A 1 802  ? 189.565 185.903 263.779 1.00 79.79  ? 785  ASN B N   1 
ATOM   6127  C CA  . ASN A 1 802  ? 190.479 186.987 264.117 1.00 79.79  ? 785  ASN B CA  1 
ATOM   6128  C C   . ASN A 1 802  ? 190.887 187.771 262.882 1.00 79.79  ? 785  ASN B C   1 
ATOM   6129  O O   . ASN A 1 802  ? 190.933 189.006 262.910 1.00 79.79  ? 785  ASN B O   1 
ATOM   6130  C CB  . ASN A 1 802  ? 191.715 186.436 264.822 1.00 79.79  ? 785  ASN B CB  1 
ATOM   6131  C CG  . ASN A 1 802  ? 191.415 185.954 266.213 1.00 79.79  ? 785  ASN B CG  1 
ATOM   6132  O OD1 . ASN A 1 802  ? 190.260 185.737 266.562 1.00 79.79  ? 785  ASN B OD1 1 
ATOM   6133  N ND2 . ASN A 1 802  ? 192.453 185.788 267.023 1.00 79.79  ? 785  ASN B ND2 1 
ATOM   6134  N N   . LYS A 1 803  ? 191.197 187.072 261.787 1.00 84.13  ? 786  LYS B N   1 
ATOM   6135  C CA  . LYS A 1 803  ? 191.585 187.780 260.571 1.00 84.13  ? 786  LYS B CA  1 
ATOM   6136  C C   . LYS A 1 803  ? 190.448 188.658 260.064 1.00 84.13  ? 786  LYS B C   1 
ATOM   6137  O O   . LYS A 1 803  ? 190.666 189.820 259.695 1.00 84.13  ? 786  LYS B O   1 
ATOM   6138  C CB  . LYS A 1 803  ? 192.018 186.787 259.495 1.00 84.13  ? 786  LYS B CB  1 
ATOM   6139  C CG  . LYS A 1 803  ? 192.578 187.446 258.250 1.00 84.13  ? 786  LYS B CG  1 
ATOM   6140  C CD  . LYS A 1 803  ? 193.074 186.416 257.252 1.00 84.13  ? 786  LYS B CD  1 
ATOM   6141  C CE  . LYS A 1 803  ? 193.718 187.083 256.049 1.00 84.13  ? 786  LYS B CE  1 
ATOM   6142  N NZ  . LYS A 1 803  ? 193.795 186.160 254.884 1.00 84.13  ? 786  LYS B NZ  1 
ATOM   6143  N N   . PHE A 1 804  ? 189.224 188.128 260.064 1.00 80.63  ? 787  PHE B N   1 
ATOM   6144  C CA  . PHE A 1 804  ? 188.077 188.902 259.599 1.00 80.63  ? 787  PHE B CA  1 
ATOM   6145  C C   . PHE A 1 804  ? 187.861 190.142 260.456 1.00 80.63  ? 787  PHE B C   1 
ATOM   6146  O O   . PHE A 1 804  ? 187.612 191.236 259.932 1.00 80.63  ? 787  PHE B O   1 
ATOM   6147  C CB  . PHE A 1 804  ? 186.831 188.018 259.597 1.00 80.63  ? 787  PHE B CB  1 
ATOM   6148  C CG  . PHE A 1 804  ? 185.539 188.777 259.536 1.00 80.63  ? 787  PHE B CG  1 
ATOM   6149  C CD1 . PHE A 1 804  ? 185.242 189.582 258.456 1.00 80.63  ? 787  PHE B CD1 1 
ATOM   6150  C CD2 . PHE A 1 804  ? 184.615 188.672 260.556 1.00 80.63  ? 787  PHE B CD2 1 
ATOM   6151  C CE1 . PHE A 1 804  ? 184.050 190.268 258.395 1.00 80.63  ? 787  PHE B CE1 1 
ATOM   6152  C CE2 . PHE A 1 804  ? 183.424 189.361 260.502 1.00 80.63  ? 787  PHE B CE2 1 
ATOM   6153  C CZ  . PHE A 1 804  ? 183.143 190.161 259.422 1.00 80.63  ? 787  PHE B CZ  1 
ATOM   6154  N N   . LEU A 1 805  ? 187.966 189.999 261.778 1.00 75.54  ? 788  LEU B N   1 
ATOM   6155  C CA  . LEU A 1 805  ? 187.718 191.141 262.652 1.00 75.54  ? 788  LEU B CA  1 
ATOM   6156  C C   . LEU A 1 805  ? 188.825 192.184 262.539 1.00 75.54  ? 788  LEU B C   1 
ATOM   6157  O O   . LEU A 1 805  ? 188.553 193.391 262.585 1.00 75.54  ? 788  LEU B O   1 
ATOM   6158  C CB  . LEU A 1 805  ? 187.548 190.665 264.091 1.00 75.54  ? 788  LEU B CB  1 
ATOM   6159  C CG  . LEU A 1 805  ? 186.154 190.096 264.362 1.00 75.54  ? 788  LEU B CG  1 
ATOM   6160  C CD1 . LEU A 1 805  ? 186.039 189.582 265.778 1.00 75.54  ? 788  LEU B CD1 1 
ATOM   6161  C CD2 . LEU A 1 805  ? 185.098 191.148 264.094 1.00 75.54  ? 788  LEU B CD2 1 
ATOM   6162  N N   . ASN A 1 806  ? 190.077 191.746 262.383 1.00 78.39  ? 789  ASN B N   1 
ATOM   6163  C CA  . ASN A 1 806  ? 191.161 192.696 262.155 1.00 78.39  ? 789  ASN B CA  1 
ATOM   6164  C C   . ASN A 1 806  ? 190.941 193.473 260.865 1.00 78.39  ? 789  ASN B C   1 
ATOM   6165  O O   . ASN A 1 806  ? 191.140 194.696 260.821 1.00 78.39  ? 789  ASN B O   1 
ATOM   6166  C CB  . ASN A 1 806  ? 192.501 191.967 262.106 1.00 78.39  ? 789  ASN B CB  1 
ATOM   6167  C CG  . ASN A 1 806  ? 192.826 191.263 263.400 1.00 78.39  ? 789  ASN B CG  1 
ATOM   6168  O OD1 . ASN A 1 806  ? 192.430 191.704 264.478 1.00 78.39  ? 789  ASN B OD1 1 
ATOM   6169  N ND2 . ASN A 1 806  ? 193.542 190.150 263.301 1.00 78.39  ? 789  ASN B ND2 1 
ATOM   6170  N N   . GLN A 1 807  ? 190.533 192.775 259.802 1.00 81.25  ? 790  GLN B N   1 
ATOM   6171  C CA  . GLN A 1 807  ? 190.257 193.456 258.543 1.00 81.25  ? 790  GLN B CA  1 
ATOM   6172  C C   . GLN A 1 807  ? 189.130 194.465 258.702 1.00 81.25  ? 790  GLN B C   1 
ATOM   6173  O O   . GLN A 1 807  ? 189.209 195.577 258.171 1.00 81.25  ? 790  GLN B O   1 
ATOM   6174  C CB  . GLN A 1 807  ? 189.920 192.437 257.457 1.00 81.25  ? 790  GLN B CB  1 
ATOM   6175  C CG  . GLN A 1 807  ? 191.053 191.487 257.138 1.00 81.25  ? 790  GLN B CG  1 
ATOM   6176  C CD  . GLN A 1 807  ? 191.064 191.061 255.692 1.00 81.25  ? 790  GLN B CD  1 
ATOM   6177  O OE1 . GLN A 1 807  ? 190.100 190.480 255.197 1.00 81.25  ? 790  GLN B OE1 1 
ATOM   6178  N NE2 . GLN A 1 807  ? 192.161 191.344 255.002 1.00 81.25  ? 790  GLN B NE2 1 
ATOM   6179  N N   . CYS A 1 808  ? 188.077 194.101 259.439 1.00 78.43  ? 791  CYS B N   1 
ATOM   6180  C CA  . CYS A 1 808  ? 186.980 195.040 259.661 1.00 78.43  ? 791  CYS B CA  1 
ATOM   6181  C C   . CYS A 1 808  ? 187.445 196.279 260.416 1.00 78.43  ? 791  CYS B C   1 
ATOM   6182  O O   . CYS A 1 808  ? 187.081 197.406 260.057 1.00 78.43  ? 791  CYS B O   1 
ATOM   6183  C CB  . CYS A 1 808  ? 185.843 194.359 260.418 1.00 78.43  ? 791  CYS B CB  1 
ATOM   6184  S SG  . CYS A 1 808  ? 184.780 193.350 259.385 1.00 78.43  ? 791  CYS B SG  1 
ATOM   6185  N N   . SER A 1 809  ? 188.244 196.094 261.469 1.00 75.16  ? 792  SER B N   1 
ATOM   6186  C CA  . SER A 1 809  ? 188.697 197.238 262.255 1.00 75.16  ? 792  SER B CA  1 
ATOM   6187  C C   . SER A 1 809  ? 189.568 198.170 261.421 1.00 75.16  ? 792  SER B C   1 
ATOM   6188  O O   . SER A 1 809  ? 189.390 199.396 261.444 1.00 75.16  ? 792  SER B O   1 
ATOM   6189  C CB  . SER A 1 809  ? 189.453 196.758 263.492 1.00 75.16  ? 792  SER B CB  1 
ATOM   6190  O OG  . SER A 1 809  ? 190.330 195.697 263.168 1.00 75.16  ? 792  SER B OG  1 
ATOM   6191  N N   . VAL A 1 810  ? 190.510 197.605 260.662 1.00 70.76  ? 793  VAL B N   1 
ATOM   6192  C CA  . VAL A 1 810  ? 191.386 198.443 259.847 1.00 70.76  ? 793  VAL B CA  1 
ATOM   6193  C C   . VAL A 1 810  ? 190.594 199.131 258.741 1.00 70.76  ? 793  VAL B C   1 
ATOM   6194  O O   . VAL A 1 810  ? 190.841 200.301 258.415 1.00 70.76  ? 793  VAL B O   1 
ATOM   6195  C CB  . VAL A 1 810  ? 192.551 197.612 259.285 1.00 70.76  ? 793  VAL B CB  1 
ATOM   6196  C CG1 . VAL A 1 810  ? 193.438 198.472 258.413 1.00 70.76  ? 793  VAL B CG1 1 
ATOM   6197  C CG2 . VAL A 1 810  ? 193.352 197.018 260.420 1.00 70.76  ? 793  VAL B CG2 1 
ATOM   6198  N N   . SER A 1 811  ? 189.628 198.424 258.149 1.00 73.27  ? 794  SER B N   1 
ATOM   6199  C CA  . SER A 1 811  ? 188.795 199.028 257.120 1.00 73.27  ? 794  SER B CA  1 
ATOM   6200  C C   . SER A 1 811  ? 188.006 200.203 257.672 1.00 73.27  ? 794  SER B C   1 
ATOM   6201  O O   . SER A 1 811  ? 187.912 201.251 257.025 1.00 73.27  ? 794  SER B O   1 
ATOM   6202  C CB  . SER A 1 811  ? 187.851 197.982 256.532 1.00 73.27  ? 794  SER B CB  1 
ATOM   6203  O OG  . SER A 1 811  ? 186.798 198.597 255.813 1.00 73.27  ? 794  SER B OG  1 
ATOM   6204  N N   . TYR A 1 812  ? 187.431 200.052 258.866 1.00 70.01  ? 795  TYR B N   1 
ATOM   6205  C CA  . TYR A 1 812  ? 186.704 201.169 259.457 1.00 70.01  ? 795  TYR B CA  1 
ATOM   6206  C C   . TYR A 1 812  ? 187.633 202.340 259.737 1.00 70.01  ? 795  TYR B C   1 
ATOM   6207  O O   . TYR A 1 812  ? 187.277 203.496 259.476 1.00 70.01  ? 795  TYR B O   1 
ATOM   6208  C CB  . TYR A 1 812  ? 185.993 200.742 260.738 1.00 70.01  ? 795  TYR B CB  1 
ATOM   6209  C CG  . TYR A 1 812  ? 185.066 201.812 261.258 1.00 70.01  ? 795  TYR B CG  1 
ATOM   6210  C CD1 . TYR A 1 812  ? 183.788 201.956 260.745 1.00 70.01  ? 795  TYR B CD1 1 
ATOM   6211  C CD2 . TYR A 1 812  ? 185.476 202.694 262.244 1.00 70.01  ? 795  TYR B CD2 1 
ATOM   6212  C CE1 . TYR A 1 812  ? 182.940 202.937 261.207 1.00 70.01  ? 795  TYR B CE1 1 
ATOM   6213  C CE2 . TYR A 1 812  ? 184.633 203.680 262.713 1.00 70.01  ? 795  TYR B CE2 1 
ATOM   6214  C CZ  . TYR A 1 812  ? 183.366 203.795 262.190 1.00 70.01  ? 795  TYR B CZ  1 
ATOM   6215  O OH  . TYR A 1 812  ? 182.521 204.775 262.651 1.00 70.01  ? 795  TYR B OH  1 
ATOM   6216  N N   . LEU A 1 813  ? 188.833 202.061 260.253 1.00 69.60  ? 796  LEU B N   1 
ATOM   6217  C CA  . LEU A 1 813  ? 189.781 203.138 260.524 1.00 69.60  ? 796  LEU B CA  1 
ATOM   6218  C C   . LEU A 1 813  ? 190.103 203.914 259.256 1.00 69.60  ? 796  LEU B C   1 
ATOM   6219  O O   . LEU A 1 813  ? 190.084 205.150 259.250 1.00 69.60  ? 796  LEU B O   1 
ATOM   6220  C CB  . LEU A 1 813  ? 191.064 202.579 261.137 1.00 69.60  ? 796  LEU B CB  1 
ATOM   6221  C CG  . LEU A 1 813  ? 192.295 203.489 261.036 1.00 69.60  ? 796  LEU B CG  1 
ATOM   6222  C CD1 . LEU A 1 813  ? 192.097 204.796 261.792 1.00 69.60  ? 796  LEU B CD1 1 
ATOM   6223  C CD2 . LEU A 1 813  ? 193.543 202.774 261.518 1.00 69.60  ? 796  LEU B CD2 1 
ATOM   6224  N N   . MET A 1 814  ? 190.394 203.207 258.167 1.00 69.60  ? 797  MET B N   1 
ATOM   6225  C CA  . MET A 1 814  ? 190.816 203.884 256.948 1.00 69.60  ? 797  MET B CA  1 
ATOM   6226  C C   . MET A 1 814  ? 189.656 204.407 256.111 1.00 69.60  ? 797  MET B C   1 
ATOM   6227  O O   . MET A 1 814  ? 189.894 205.171 255.171 1.00 69.60  ? 797  MET B O   1 
ATOM   6228  C CB  . MET A 1 814  ? 191.679 202.950 256.101 1.00 69.60  ? 797  MET B CB  1 
ATOM   6229  C CG  . MET A 1 814  ? 192.918 202.454 256.816 1.00 69.60  ? 797  MET B CG  1 
ATOM   6230  S SD  . MET A 1 814  ? 194.273 203.636 256.734 1.00 69.60  ? 797  MET B SD  1 
ATOM   6231  C CE  . MET A 1 814  ? 194.143 204.176 255.033 1.00 69.60  ? 797  MET B CE  1 
ATOM   6232  N N   . ASN A 1 815  ? 188.418 204.029 256.423 1.00 69.87  ? 798  ASN B N   1 
ATOM   6233  C CA  . ASN A 1 815  ? 187.268 204.460 255.640 1.00 69.87  ? 798  ASN B CA  1 
ATOM   6234  C C   . ASN A 1 815  ? 186.483 205.585 256.300 1.00 69.87  ? 798  ASN B C   1 
ATOM   6235  O O   . ASN A 1 815  ? 186.154 206.574 255.640 1.00 69.87  ? 798  ASN B O   1 
ATOM   6236  C CB  . ASN A 1 815  ? 186.335 203.271 255.385 1.00 69.87  ? 798  ASN B CB  1 
ATOM   6237  C CG  . ASN A 1 815  ? 186.666 202.537 254.108 1.00 69.87  ? 798  ASN B CG  1 
ATOM   6238  O OD1 . ASN A 1 815  ? 187.656 202.839 253.444 1.00 69.87  ? 798  ASN B OD1 1 
ATOM   6239  N ND2 . ASN A 1 815  ? 185.839 201.562 253.756 1.00 69.87  ? 798  ASN B ND2 1 
ATOM   6240  N N   . SER A 1 816  ? 186.171 205.460 257.589 1.00 69.97  ? 799  SER B N   1 
ATOM   6241  C CA  . SER A 1 816  ? 185.240 206.374 258.234 1.00 69.97  ? 799  SER B CA  1 
ATOM   6242  C C   . SER A 1 816  ? 185.891 207.315 259.237 1.00 69.97  ? 799  SER B C   1 
ATOM   6243  O O   . SER A 1 816  ? 185.191 208.145 259.823 1.00 69.97  ? 799  SER B O   1 
ATOM   6244  C CB  . SER A 1 816  ? 184.128 205.580 258.925 1.00 69.97  ? 799  SER B CB  1 
ATOM   6245  O OG  . SER A 1 816  ? 183.489 204.708 258.010 1.00 69.97  ? 799  SER B OG  1 
ATOM   6246  N N   . MET A 1 817  ? 187.200 207.220 259.453 1.00 69.60  ? 800  MET B N   1 
ATOM   6247  C CA  . MET A 1 817  ? 187.878 208.094 260.402 1.00 69.60  ? 800  MET B CA  1 
ATOM   6248  C C   . MET A 1 817  ? 188.943 208.958 259.750 1.00 69.60  ? 800  MET B C   1 
ATOM   6249  O O   . MET A 1 817  ? 188.998 210.165 260.010 1.00 69.60  ? 800  MET B O   1 
ATOM   6250  C CB  . MET A 1 817  ? 188.497 207.262 261.534 1.00 69.60  ? 800  MET B CB  1 
ATOM   6251  C CG  . MET A 1 817  ? 187.542 206.257 262.150 1.00 69.60  ? 800  MET B CG  1 
ATOM   6252  S SD  . MET A 1 817  ? 187.796 206.044 263.918 1.00 69.60  ? 800  MET B SD  1 
ATOM   6253  C CE  . MET A 1 817  ? 187.283 207.646 264.522 1.00 69.60  ? 800  MET B CE  1 
ATOM   6254  N N   . ILE A 1 818  ? 189.799 208.370 258.914 1.00 69.60  ? 801  ILE B N   1 
ATOM   6255  C CA  . ILE A 1 818  ? 190.886 209.136 258.301 1.00 69.60  ? 801  ILE B CA  1 
ATOM   6256  C C   . ILE A 1 818  ? 190.384 210.272 257.414 1.00 69.60  ? 801  ILE B C   1 
ATOM   6257  O O   . ILE A 1 818  ? 190.908 211.392 257.533 1.00 69.60  ? 801  ILE B O   1 
ATOM   6258  C CB  . ILE A 1 818  ? 191.845 208.184 257.563 1.00 69.60  ? 801  ILE B CB  1 
ATOM   6259  C CG1 . ILE A 1 818  ? 192.833 207.570 258.551 1.00 69.60  ? 801  ILE B CG1 1 
ATOM   6260  C CG2 . ILE A 1 818  ? 192.590 208.910 256.466 1.00 69.60  ? 801  ILE B CG2 1 
ATOM   6261  C CD1 . ILE A 1 818  ? 193.794 208.567 259.139 1.00 69.60  ? 801  ILE B CD1 1 
ATOM   6262  N N   . PRO A 1 819  ? 189.405 210.073 256.521 1.00 69.60  ? 802  PRO B N   1 
ATOM   6263  C CA  . PRO A 1 819  ? 189.009 211.177 255.629 1.00 69.60  ? 802  PRO B CA  1 
ATOM   6264  C C   . PRO A 1 819  ? 188.563 212.431 256.354 1.00 69.60  ? 802  PRO B C   1 
ATOM   6265  O O   . PRO A 1 819  ? 188.815 213.540 255.863 1.00 69.60  ? 802  PRO B O   1 
ATOM   6266  C CB  . PRO A 1 819  ? 187.861 210.570 254.814 1.00 69.60  ? 802  PRO B CB  1 
ATOM   6267  C CG  . PRO A 1 819  ? 188.105 209.124 254.848 1.00 69.60  ? 802  PRO B CG  1 
ATOM   6268  C CD  . PRO A 1 819  ? 188.677 208.836 256.190 1.00 69.60  ? 802  PRO B CD  1 
ATOM   6269  N N   . TYR A 1 820  ? 187.906 212.295 257.507 1.00 69.60  ? 803  TYR B N   1 
ATOM   6270  C CA  . TYR A 1 820  ? 187.428 213.472 258.225 1.00 69.60  ? 803  TYR B CA  1 
ATOM   6271  C C   . TYR A 1 820  ? 188.581 214.335 258.715 1.00 69.60  ? 803  TYR B C   1 
ATOM   6272  O O   . TYR A 1 820  ? 188.390 215.523 258.995 1.00 69.60  ? 803  TYR B O   1 
ATOM   6273  C CB  . TYR A 1 820  ? 186.544 213.049 259.395 1.00 69.60  ? 803  TYR B CB  1 
ATOM   6274  C CG  . TYR A 1 820  ? 185.214 212.478 258.967 1.00 69.60  ? 803  TYR B CG  1 
ATOM   6275  C CD1 . TYR A 1 820  ? 185.074 211.127 258.696 1.00 69.60  ? 803  TYR B CD1 1 
ATOM   6276  C CD2 . TYR A 1 820  ? 184.101 213.292 258.830 1.00 69.60  ? 803  TYR B CD2 1 
ATOM   6277  C CE1 . TYR A 1 820  ? 183.864 210.601 258.304 1.00 69.60  ? 803  TYR B CE1 1 
ATOM   6278  C CE2 . TYR A 1 820  ? 182.886 212.775 258.438 1.00 69.60  ? 803  TYR B CE2 1 
ATOM   6279  C CZ  . TYR A 1 820  ? 182.773 211.429 258.176 1.00 69.60  ? 803  TYR B CZ  1 
ATOM   6280  O OH  . TYR A 1 820  ? 181.563 210.908 257.785 1.00 69.60  ? 803  TYR B OH  1 
ATOM   6281  N N   . GLY A 1 821  ? 189.774 213.761 258.830 1.00 69.60  ? 804  GLY B N   1 
ATOM   6282  C CA  . GLY A 1 821  ? 190.945 214.529 259.194 1.00 69.60  ? 804  GLY B CA  1 
ATOM   6283  C C   . GLY A 1 821  ? 191.736 214.966 257.981 1.00 69.60  ? 804  GLY B C   1 
ATOM   6284  O O   . GLY A 1 821  ? 192.339 216.044 257.978 1.00 69.60  ? 804  GLY B O   1 
ATOM   6285  N N   . VAL A 1 822  ? 191.742 214.129 256.941 1.00 69.60  ? 805  VAL B N   1 
ATOM   6286  C CA  . VAL A 1 822  ? 192.441 214.484 255.709 1.00 69.60  ? 805  VAL B CA  1 
ATOM   6287  C C   . VAL A 1 822  ? 191.820 215.725 255.086 1.00 69.60  ? 805  VAL B C   1 
ATOM   6288  O O   . VAL A 1 822  ? 192.527 216.588 254.550 1.00 69.60  ? 805  VAL B O   1 
ATOM   6289  C CB  . VAL A 1 822  ? 192.444 213.295 254.731 1.00 69.60  ? 805  VAL B CB  1 
ATOM   6290  C CG1 . VAL A 1 822  ? 192.869 213.743 253.350 1.00 69.60  ? 805  VAL B CG1 1 
ATOM   6291  C CG2 . VAL A 1 822  ? 193.373 212.214 255.232 1.00 69.60  ? 805  VAL B CG2 1 
ATOM   6292  N N   . LYS A 1 823  ? 190.492 215.840 255.149 1.00 69.60  ? 806  LYS B N   1 
ATOM   6293  C CA  . LYS A 1 823  ? 189.835 217.036 254.633 1.00 69.60  ? 806  LYS B CA  1 
ATOM   6294  C C   . LYS A 1 823  ? 190.343 218.287 255.336 1.00 69.60  ? 806  LYS B C   1 
ATOM   6295  O O   . LYS A 1 823  ? 190.704 219.277 254.687 1.00 69.60  ? 806  LYS B O   1 
ATOM   6296  C CB  . LYS A 1 823  ? 188.322 216.926 254.796 1.00 69.60  ? 806  LYS B CB  1 
ATOM   6297  C CG  . LYS A 1 823  ? 187.639 218.281 254.792 1.00 69.60  ? 806  LYS B CG  1 
ATOM   6298  C CD  . LYS A 1 823  ? 186.298 218.247 255.485 1.00 69.60  ? 806  LYS B CD  1 
ATOM   6299  C CE  . LYS A 1 823  ? 185.446 219.426 255.061 1.00 69.60  ? 806  LYS B CE  1 
ATOM   6300  N NZ  . LYS A 1 823  ? 186.284 220.548 254.561 1.00 69.60  ? 806  LYS B NZ  1 
ATOM   6301  N N   . ARG A 1 824  ? 190.378 218.258 256.670 1.00 69.60  ? 807  ARG B N   1 
ATOM   6302  C CA  . ARG A 1 824  ? 190.843 219.415 257.425 1.00 69.60  ? 807  ARG B CA  1 
ATOM   6303  C C   . ARG A 1 824  ? 192.296 219.728 257.108 1.00 69.60  ? 807  ARG B C   1 
ATOM   6304  O O   . ARG A 1 824  ? 192.661 220.893 256.911 1.00 69.60  ? 807  ARG B O   1 
ATOM   6305  C CB  . ARG A 1 824  ? 190.667 219.166 258.921 1.00 69.60  ? 807  ARG B CB  1 
ATOM   6306  C CG  . ARG A 1 824  ? 189.227 219.033 259.353 1.00 69.60  ? 807  ARG B CG  1 
ATOM   6307  C CD  . ARG A 1 824  ? 188.522 220.369 259.299 1.00 69.60  ? 807  ARG B CD  1 
ATOM   6308  N NE  . ARG A 1 824  ? 187.165 220.281 259.819 1.00 69.60  ? 807  ARG B NE  1 
ATOM   6309  C CZ  . ARG A 1 824  ? 186.170 221.069 259.440 1.00 69.60  ? 807  ARG B CZ  1 
ATOM   6310  N NH1 . ARG A 1 824  ? 186.353 222.035 258.555 1.00 69.60  ? 807  ARG B NH1 1 
ATOM   6311  N NH2 . ARG A 1 824  ? 184.962 220.887 259.965 1.00 69.60  ? 807  ARG B NH2 1 
ATOM   6312  N N   . LEU A 1 825  ? 193.138 218.695 257.040 1.00 69.60  ? 808  LEU B N   1 
ATOM   6313  C CA  . LEU A 1 825  ? 194.554 218.921 256.779 1.00 69.60  ? 808  LEU B CA  1 
ATOM   6314  C C   . LEU A 1 825  ? 194.773 219.545 255.410 1.00 69.60  ? 808  LEU B C   1 
ATOM   6315  O O   . LEU A 1 825  ? 195.569 220.478 255.269 1.00 69.60  ? 808  LEU B O   1 
ATOM   6316  C CB  . LEU A 1 825  ? 195.333 217.615 256.898 1.00 69.60  ? 808  LEU B CB  1 
ATOM   6317  C CG  . LEU A 1 825  ? 195.361 216.999 258.290 1.00 69.60  ? 808  LEU B CG  1 
ATOM   6318  C CD1 . LEU A 1 825  ? 195.515 215.496 258.189 1.00 69.60  ? 808  LEU B CD1 1 
ATOM   6319  C CD2 . LEU A 1 825  ? 196.472 217.611 259.111 1.00 69.60  ? 808  LEU B CD2 1 
ATOM   6320  N N   . GLU A 1 826  ? 194.072 219.058 254.387 1.00 69.60  ? 809  GLU B N   1 
ATOM   6321  C CA  . GLU A 1 826  ? 194.315 219.583 253.050 1.00 69.60  ? 809  GLU B CA  1 
ATOM   6322  C C   . GLU A 1 826  ? 193.672 220.949 252.844 1.00 69.60  ? 809  GLU B C   1 
ATOM   6323  O O   . GLU A 1 826  ? 194.211 221.773 252.095 1.00 69.60  ? 809  GLU B O   1 
ATOM   6324  C CB  . GLU A 1 826  ? 193.849 218.575 252.002 1.00 69.60  ? 809  GLU B CB  1 
ATOM   6325  C CG  . GLU A 1 826  ? 194.832 217.420 251.868 1.00 69.60  ? 809  GLU B CG  1 
ATOM   6326  C CD  . GLU A 1 826  ? 194.664 216.627 250.594 1.00 69.60  ? 809  GLU B CD  1 
ATOM   6327  O OE1 . GLU A 1 826  ? 193.575 216.687 249.997 1.00 69.60  ? 809  GLU B OE1 1 
ATOM   6328  O OE2 . GLU A 1 826  ? 195.625 215.941 250.188 1.00 69.60  ? 809  GLU B OE2 1 
ATOM   6329  N N   . ASP A 1 827  ? 192.554 221.229 253.516 1.00 69.60  ? 810  ASP B N   1 
ATOM   6330  C CA  . ASP A 1 827  ? 192.031 222.591 253.515 1.00 69.60  ? 810  ASP B CA  1 
ATOM   6331  C C   . ASP A 1 827  ? 193.016 223.551 254.171 1.00 69.60  ? 810  ASP B C   1 
ATOM   6332  O O   . ASP A 1 827  ? 193.251 224.660 253.670 1.00 69.60  ? 810  ASP B O   1 
ATOM   6333  C CB  . ASP A 1 827  ? 190.681 222.628 254.227 1.00 69.60  ? 810  ASP B CB  1 
ATOM   6334  C CG  . ASP A 1 827  ? 189.803 223.758 253.749 1.00 69.60  ? 810  ASP B CG  1 
ATOM   6335  O OD1 . ASP A 1 827  ? 190.342 224.721 253.165 1.00 69.60  ? 810  ASP B OD1 1 
ATOM   6336  O OD2 . ASP A 1 827  ? 188.574 223.683 253.953 1.00 69.60  ? 810  ASP B OD2 1 
ATOM   6337  N N   . PHE A 1 828  ? 193.618 223.131 255.287 1.00 69.60  ? 811  PHE B N   1 
ATOM   6338  C CA  . PHE A 1 828  ? 194.646 223.940 255.932 1.00 69.60  ? 811  PHE B CA  1 
ATOM   6339  C C   . PHE A 1 828  ? 195.850 224.128 255.018 1.00 69.60  ? 811  PHE B C   1 
ATOM   6340  O O   . PHE A 1 828  ? 196.448 225.209 254.979 1.00 69.60  ? 811  PHE B O   1 
ATOM   6341  C CB  . PHE A 1 828  ? 195.052 223.285 257.252 1.00 69.60  ? 811  PHE B CB  1 
ATOM   6342  C CG  . PHE A 1 828  ? 196.463 223.569 257.671 1.00 69.60  ? 811  PHE B CG  1 
ATOM   6343  C CD1 . PHE A 1 828  ? 196.853 224.844 258.035 1.00 69.60  ? 811  PHE B CD1 1 
ATOM   6344  C CD2 . PHE A 1 828  ? 197.397 222.551 257.716 1.00 69.60  ? 811  PHE B CD2 1 
ATOM   6345  C CE1 . PHE A 1 828  ? 198.147 225.096 258.423 1.00 69.60  ? 811  PHE B CE1 1 
ATOM   6346  C CE2 . PHE A 1 828  ? 198.691 222.800 258.106 1.00 69.60  ? 811  PHE B CE2 1 
ATOM   6347  C CZ  . PHE A 1 828  ? 199.066 224.073 258.458 1.00 69.60  ? 811  PHE B CZ  1 
ATOM   6348  N N   . ASP A 1 829  ? 196.225 223.081 254.283 1.00 69.60  ? 812  ASP B N   1 
ATOM   6349  C CA  . ASP A 1 829  ? 197.341 223.180 253.350 1.00 69.60  ? 812  ASP B CA  1 
ATOM   6350  C C   . ASP A 1 829  ? 197.059 224.213 252.271 1.00 69.60  ? 812  ASP B C   1 
ATOM   6351  O O   . ASP A 1 829  ? 197.925 225.030 251.936 1.00 69.60  ? 812  ASP B O   1 
ATOM   6352  C CB  . ASP A 1 829  ? 197.606 221.819 252.712 1.00 69.60  ? 812  ASP B CB  1 
ATOM   6353  C CG  . ASP A 1 829  ? 198.659 221.042 253.446 1.00 69.60  ? 812  ASP B CG  1 
ATOM   6354  O OD1 . ASP A 1 829  ? 199.154 221.574 254.454 1.00 69.60  ? 812  ASP B OD1 1 
ATOM   6355  O OD2 . ASP A 1 829  ? 198.964 219.900 253.045 1.00 69.60  ? 812  ASP B OD2 1 
ATOM   6356  N N   . ALA A 1 830  ? 195.851 224.183 251.711 1.00 69.60  ? 813  ALA B N   1 
ATOM   6357  C CA  . ALA A 1 830  ? 195.483 225.166 250.701 1.00 69.60  ? 813  ALA B CA  1 
ATOM   6358  C C   . ALA A 1 830  ? 195.495 226.574 251.277 1.00 69.60  ? 813  ALA B C   1 
ATOM   6359  O O   . ALA A 1 830  ? 195.931 227.520 250.612 1.00 69.60  ? 813  ALA B O   1 
ATOM   6360  C CB  . ALA A 1 830  ? 194.111 224.837 250.124 1.00 69.60  ? 813  ALA B CB  1 
ATOM   6361  N N   . SER A 1 831  ? 195.012 226.736 252.510 1.00 69.60  ? 814  SER B N   1 
ATOM   6362  C CA  . SER A 1 831  ? 195.027 228.058 253.128 1.00 69.60  ? 814  SER B CA  1 
ATOM   6363  C C   . SER A 1 831  ? 196.452 228.554 253.339 1.00 69.60  ? 814  SER B C   1 
ATOM   6364  O O   . SER A 1 831  ? 196.741 229.740 253.147 1.00 69.60  ? 814  SER B O   1 
ATOM   6365  C CB  . SER A 1 831  ? 194.271 228.031 254.455 1.00 69.60  ? 814  SER B CB  1 
ATOM   6366  O OG  . SER A 1 831  ? 195.155 227.784 255.534 1.00 69.60  ? 814  SER B OG  1 
ATOM   6367  N N   . LEU A 1 832  ? 197.357 227.659 253.738 1.00 69.60  ? 815  LEU B N   1 
ATOM   6368  C CA  . LEU A 1 832  ? 198.735 228.060 254.003 1.00 69.60  ? 815  LEU B CA  1 
ATOM   6369  C C   . LEU A 1 832  ? 199.501 228.347 252.717 1.00 69.60  ? 815  LEU B C   1 
ATOM   6370  O O   . LEU A 1 832  ? 200.407 229.188 252.714 1.00 69.60  ? 815  LEU B O   1 
ATOM   6371  C CB  . LEU A 1 832  ? 199.443 226.976 254.819 1.00 69.60  ? 815  LEU B CB  1 
ATOM   6372  C CG  . LEU A 1 832  ? 200.963 226.846 254.722 1.00 69.60  ? 815  LEU B CG  1 
ATOM   6373  C CD1 . LEU A 1 832  ? 201.644 227.933 255.524 1.00 69.60  ? 815  LEU B CD1 1 
ATOM   6374  C CD2 . LEU A 1 832  ? 201.409 225.481 255.197 1.00 69.60  ? 815  LEU B CD2 1 
ATOM   6375  N N   . LYS A 1 833  ? 199.163 227.657 251.624 1.00 69.60  ? 816  LYS B N   1 
ATOM   6376  C CA  . LYS A 1 833  ? 199.891 227.854 250.374 1.00 69.60  ? 816  LYS B CA  1 
ATOM   6377  C C   . LYS A 1 833  ? 199.740 229.278 249.857 1.00 69.60  ? 816  LYS B C   1 
ATOM   6378  O O   . LYS A 1 833  ? 200.712 229.882 249.391 1.00 69.60  ? 816  LYS B O   1 
ATOM   6379  C CB  . LYS A 1 833  ? 199.411 226.855 249.323 1.00 69.60  ? 816  LYS B CB  1 
ATOM   6380  C CG  . LYS A 1 833  ? 200.378 226.650 248.175 1.00 69.60  ? 816  LYS B CG  1 
ATOM   6381  C CD  . LYS A 1 833  ? 199.648 226.578 246.846 1.00 69.60  ? 816  LYS B CD  1 
ATOM   6382  C CE  . LYS A 1 833  ? 198.572 225.509 246.862 1.00 69.60  ? 816  LYS B CE  1 
ATOM   6383  N NZ  . LYS A 1 833  ? 199.151 224.144 246.937 1.00 69.60  ? 816  LYS B NZ  1 
ATOM   6384  N N   . ASP A 1 834  ? 198.526 229.827 249.919 1.00 69.60  ? 817  ASP B N   1 
ATOM   6385  C CA  . ASP A 1 834  ? 198.318 231.194 249.455 1.00 69.60  ? 817  ASP B CA  1 
ATOM   6386  C C   . ASP A 1 834  ? 199.090 232.188 250.310 1.00 69.60  ? 817  ASP B C   1 
ATOM   6387  O O   . ASP A 1 834  ? 199.678 233.142 249.787 1.00 69.60  ? 817  ASP B O   1 
ATOM   6388  C CB  . ASP A 1 834  ? 196.828 231.527 249.455 1.00 69.60  ? 817  ASP B CB  1 
ATOM   6389  C CG  . ASP A 1 834  ? 196.068 230.787 248.374 1.00 69.60  ? 817  ASP B CG  1 
ATOM   6390  O OD1 . ASP A 1 834  ? 196.638 229.844 247.788 1.00 69.60  ? 817  ASP B OD1 1 
ATOM   6391  O OD2 . ASP A 1 834  ? 194.902 231.147 248.110 1.00 69.60  ? 817  ASP B OD2 1 
ATOM   6392  N N   . ALA A 1 835  ? 199.104 231.978 251.628 1.00 69.60  ? 818  ALA B N   1 
ATOM   6393  C CA  . ALA A 1 835  ? 199.868 232.857 252.505 1.00 69.60  ? 818  ALA B CA  1 
ATOM   6394  C C   . ALA A 1 835  ? 201.356 232.786 252.192 1.00 69.60  ? 818  ALA B C   1 
ATOM   6395  O O   . ALA A 1 835  ? 202.041 233.813 252.161 1.00 69.60  ? 818  ALA B O   1 
ATOM   6396  C CB  . ALA A 1 835  ? 199.611 232.497 253.966 1.00 69.60  ? 818  ALA B CB  1 
ATOM   6397  N N   . LEU A 1 836  ? 201.872 231.581 251.947 1.00 69.60  ? 819  LEU B N   1 
ATOM   6398  C CA  . LEU A 1 836  ? 203.283 231.434 251.605 1.00 69.60  ? 819  LEU B CA  1 
ATOM   6399  C C   . LEU A 1 836  ? 203.612 232.134 250.291 1.00 69.60  ? 819  LEU B C   1 
ATOM   6400  O O   . LEU A 1 836  ? 204.626 232.837 250.188 1.00 69.60  ? 819  LEU B O   1 
ATOM   6401  C CB  . LEU A 1 836  ? 203.640 229.950 251.531 1.00 69.60  ? 819  LEU B CB  1 
ATOM   6402  C CG  . LEU A 1 836  ? 204.241 229.332 252.791 1.00 69.60  ? 819  LEU B CG  1 
ATOM   6403  C CD1 . LEU A 1 836  ? 205.033 228.086 252.466 1.00 69.60  ? 819  LEU B CD1 1 
ATOM   6404  C CD2 . LEU A 1 836  ? 205.132 230.335 253.457 1.00 69.60  ? 819  LEU B CD2 1 
ATOM   6405  N N   . LEU A 1 837  ? 202.762 231.955 249.277 1.00 69.60  ? 820  LEU B N   1 
ATOM   6406  C CA  . LEU A 1 837  ? 203.007 232.583 247.981 1.00 69.60  ? 820  LEU B CA  1 
ATOM   6407  C C   . LEU A 1 837  ? 202.943 234.100 248.083 1.00 69.60  ? 820  LEU B C   1 
ATOM   6408  O O   . LEU A 1 837  ? 203.703 234.808 247.414 1.00 69.60  ? 820  LEU B O   1 
ATOM   6409  C CB  . LEU A 1 837  ? 202.000 232.075 246.951 1.00 69.60  ? 820  LEU B CB  1 
ATOM   6410  C CG  . LEU A 1 837  ? 202.435 230.936 246.030 1.00 69.60  ? 820  LEU B CG  1 
ATOM   6411  C CD1 . LEU A 1 837  ? 203.438 231.433 245.010 1.00 69.60  ? 820  LEU B CD1 1 
ATOM   6412  C CD2 . LEU A 1 837  ? 203.004 229.783 246.825 1.00 69.60  ? 820  LEU B CD2 1 
ATOM   6413  N N   . LYS A 1 838  ? 202.027 234.620 248.901 1.00 69.60  ? 821  LYS B N   1 
ATOM   6414  C CA  . LYS A 1 838  ? 202.001 236.055 249.154 1.00 69.60  ? 821  LYS B CA  1 
ATOM   6415  C C   . LYS A 1 838  ? 203.258 236.500 249.890 1.00 69.60  ? 821  LYS B C   1 
ATOM   6416  O O   . LYS A 1 838  ? 203.763 237.606 249.665 1.00 69.60  ? 821  LYS B O   1 
ATOM   6417  C CB  . LYS A 1 838  ? 200.750 236.418 249.952 1.00 69.60  ? 821  LYS B CB  1 
ATOM   6418  C CG  . LYS A 1 838  ? 200.609 237.893 250.282 1.00 69.60  ? 821  LYS B CG  1 
ATOM   6419  C CD  . LYS A 1 838  ? 200.681 238.756 249.036 1.00 69.60  ? 821  LYS B CD  1 
ATOM   6420  C CE  . LYS A 1 838  ? 200.784 240.228 249.399 1.00 69.60  ? 821  LYS B CE  1 
ATOM   6421  N NZ  . LYS A 1 838  ? 200.946 241.092 248.198 1.00 69.60  ? 821  LYS B NZ  1 
ATOM   6422  N N   . TYR A 1 839  ? 203.776 235.649 250.779 1.00 69.60  ? 822  TYR B N   1 
ATOM   6423  C CA  . TYR A 1 839  ? 204.968 236.006 251.538 1.00 69.60  ? 822  TYR B CA  1 
ATOM   6424  C C   . TYR A 1 839  ? 206.195 236.094 250.642 1.00 69.60  ? 822  TYR B C   1 
ATOM   6425  O O   . TYR A 1 839  ? 207.052 236.961 250.844 1.00 69.60  ? 822  TYR B O   1 
ATOM   6426  C CB  . TYR A 1 839  ? 205.207 234.998 252.656 1.00 69.60  ? 822  TYR B CB  1 
ATOM   6427  C CG  . TYR A 1 839  ? 206.275 235.439 253.619 1.00 69.60  ? 822  TYR B CG  1 
ATOM   6428  C CD1 . TYR A 1 839  ? 206.192 236.671 254.245 1.00 69.60  ? 822  TYR B CD1 1 
ATOM   6429  C CD2 . TYR A 1 839  ? 207.364 234.635 253.898 1.00 69.60  ? 822  TYR B CD2 1 
ATOM   6430  C CE1 . TYR A 1 839  ? 207.157 237.087 255.124 1.00 69.60  ? 822  TYR B CE1 1 
ATOM   6431  C CE2 . TYR A 1 839  ? 208.336 235.043 254.776 1.00 69.60  ? 822  TYR B CE2 1 
ATOM   6432  C CZ  . TYR A 1 839  ? 208.227 236.271 255.388 1.00 69.60  ? 822  TYR B CZ  1 
ATOM   6433  O OH  . TYR A 1 839  ? 209.193 236.692 256.269 1.00 69.60  ? 822  TYR B OH  1 
ATOM   6434  N N   . ILE A 1 840  ? 206.310 235.193 249.663 1.00 69.60  ? 823  ILE B N   1 
ATOM   6435  C CA  . ILE A 1 840  ? 207.423 235.282 248.720 1.00 69.60  ? 823  ILE B CA  1 
ATOM   6436  C C   . ILE A 1 840  ? 207.392 236.625 248.002 1.00 69.60  ? 823  ILE B C   1 
ATOM   6437  O O   . ILE A 1 840  ? 208.434 237.247 247.765 1.00 69.60  ? 823  ILE B O   1 
ATOM   6438  C CB  . ILE A 1 840  ? 207.388 234.105 247.729 1.00 69.60  ? 823  ILE B CB  1 
ATOM   6439  C CG1 . ILE A 1 840  ? 207.362 232.775 248.473 1.00 69.60  ? 823  ILE B CG1 1 
ATOM   6440  C CG2 . ILE A 1 840  ? 208.600 234.141 246.830 1.00 69.60  ? 823  ILE B CG2 1 
ATOM   6441  C CD1 . ILE A 1 840  ? 208.575 232.541 249.319 1.00 69.60  ? 823  ILE B CD1 1 
ATOM   6442  N N   . TYR A 1 841  ? 206.200 237.092 247.652 1.00 69.60  ? 824  TYR B N   1 
ATOM   6443  C CA  . TYR A 1 841  ? 206.010 238.453 247.173 1.00 69.60  ? 824  TYR B CA  1 
ATOM   6444  C C   . TYR A 1 841  ? 206.378 239.431 248.287 1.00 69.60  ? 824  TYR B C   1 
ATOM   6445  O O   . TYR A 1 841  ? 205.519 239.869 249.053 1.00 69.60  ? 824  TYR B O   1 
ATOM   6446  C CB  . TYR A 1 841  ? 204.561 238.662 246.723 1.00 69.60  ? 824  TYR B CB  1 
ATOM   6447  C CG  . TYR A 1 841  ? 204.317 239.845 245.806 1.00 69.60  ? 824  TYR B CG  1 
ATOM   6448  C CD1 . TYR A 1 841  ? 205.123 240.976 245.855 1.00 69.60  ? 824  TYR B CD1 1 
ATOM   6449  C CD2 . TYR A 1 841  ? 203.263 239.834 244.904 1.00 69.60  ? 824  TYR B CD2 1 
ATOM   6450  C CE1 . TYR A 1 841  ? 204.893 242.052 245.026 1.00 69.60  ? 824  TYR B CE1 1 
ATOM   6451  C CE2 . TYR A 1 841  ? 203.024 240.907 244.071 1.00 69.60  ? 824  TYR B CE2 1 
ATOM   6452  C CZ  . TYR A 1 841  ? 203.842 242.013 244.136 1.00 69.60  ? 824  TYR B CZ  1 
ATOM   6453  O OH  . TYR A 1 841  ? 203.610 243.086 243.307 1.00 69.60  ? 824  TYR B OH  1 
ATOM   6454  N N   . ILE A 1 848  ? 214.428 237.333 248.397 1.00 69.60  ? 831  ILE B N   1 
ATOM   6455  C CA  . ILE A 1 848  ? 214.775 238.340 247.403 1.00 69.60  ? 831  ILE B CA  1 
ATOM   6456  C C   . ILE A 1 848  ? 215.779 237.774 246.404 1.00 69.60  ? 831  ILE B C   1 
ATOM   6457  O O   . ILE A 1 848  ? 216.902 237.433 246.766 1.00 69.60  ? 831  ILE B O   1 
ATOM   6458  C CB  . ILE A 1 848  ? 215.323 239.612 248.074 1.00 69.60  ? 831  ILE B CB  1 
ATOM   6459  N N   . GLY A 1 849  ? 215.369 237.681 245.142 1.00 70.13  ? 832  GLY B N   1 
ATOM   6460  C CA  . GLY A 1 849  ? 216.218 237.137 244.105 1.00 70.13  ? 832  GLY B CA  1 
ATOM   6461  C C   . GLY A 1 849  ? 216.224 235.629 244.003 1.00 70.13  ? 832  GLY B C   1 
ATOM   6462  O O   . GLY A 1 849  ? 216.953 235.085 243.163 1.00 70.13  ? 832  GLY B O   1 
ATOM   6463  N N   . GLN A 1 850  ? 215.438 234.934 244.827 1.00 72.87  ? 833  GLN B N   1 
ATOM   6464  C CA  . GLN A 1 850  ? 215.352 233.478 244.808 1.00 72.87  ? 833  GLN B CA  1 
ATOM   6465  C C   . GLN A 1 850  ? 213.903 233.019 244.721 1.00 72.87  ? 833  GLN B C   1 
ATOM   6466  O O   . GLN A 1 850  ? 213.542 231.976 245.270 1.00 72.87  ? 833  GLN B O   1 
ATOM   6467  C CB  . GLN A 1 850  ? 216.026 232.874 246.040 1.00 72.87  ? 833  GLN B CB  1 
ATOM   6468  C CG  . GLN A 1 850  ? 217.364 232.227 245.756 1.00 72.87  ? 833  GLN B CG  1 
ATOM   6469  C CD  . GLN A 1 850  ? 217.352 231.430 244.471 1.00 72.87  ? 833  GLN B CD  1 
ATOM   6470  O OE1 . GLN A 1 850  ? 216.630 230.443 244.348 1.00 72.87  ? 833  GLN B OE1 1 
ATOM   6471  N NE2 . GLN A 1 850  ? 218.153 231.857 243.503 1.00 72.87  ? 833  GLN B NE2 1 
ATOM   6472  N N   . VAL A 1 851  ? 213.060 233.788 244.033 1.00 71.81  ? 834  VAL B N   1 
ATOM   6473  C CA  . VAL A 1 851  ? 211.627 233.523 244.068 1.00 71.81  ? 834  VAL B CA  1 
ATOM   6474  C C   . VAL A 1 851  ? 211.291 232.221 243.351 1.00 71.81  ? 834  VAL B C   1 
ATOM   6475  O O   . VAL A 1 851  ? 210.383 231.495 243.766 1.00 71.81  ? 834  VAL B O   1 
ATOM   6476  C CB  . VAL A 1 851  ? 210.843 234.719 243.493 1.00 71.81  ? 834  VAL B CB  1 
ATOM   6477  C CG1 . VAL A 1 851  ? 211.237 235.999 244.210 1.00 71.81  ? 834  VAL B CG1 1 
ATOM   6478  C CG2 . VAL A 1 851  ? 211.080 234.862 241.999 1.00 71.81  ? 834  VAL B CG2 1 
ATOM   6479  N N   . ASP A 1 852  ? 212.007 231.896 242.274 1.00 77.20  ? 835  ASP B N   1 
ATOM   6480  C CA  . ASP A 1 852  ? 211.600 230.767 241.441 1.00 77.20  ? 835  ASP B CA  1 
ATOM   6481  C C   . ASP A 1 852  ? 211.781 229.441 242.169 1.00 77.20  ? 835  ASP B C   1 
ATOM   6482  O O   . ASP A 1 852  ? 210.868 228.603 242.193 1.00 77.20  ? 835  ASP B O   1 
ATOM   6483  C CB  . ASP A 1 852  ? 212.382 230.772 240.130 1.00 77.20  ? 835  ASP B CB  1 
ATOM   6484  C CG  . ASP A 1 852  ? 211.554 230.285 238.959 1.00 77.20  ? 835  ASP B CG  1 
ATOM   6485  O OD1 . ASP A 1 852  ? 210.822 229.287 239.124 1.00 77.20  ? 835  ASP B OD1 1 
ATOM   6486  O OD2 . ASP A 1 852  ? 211.631 230.904 237.877 1.00 77.20  ? 835  ASP B OD2 1 
ATOM   6487  N N   . ARG A 1 853  ? 212.955 229.230 242.767 1.00 75.55  ? 836  ARG B N   1 
ATOM   6488  C CA  . ARG A 1 853  ? 213.202 227.986 243.486 1.00 75.55  ? 836  ARG B CA  1 
ATOM   6489  C C   . ARG A 1 853  ? 212.249 227.836 244.663 1.00 75.55  ? 836  ARG B C   1 
ATOM   6490  O O   . ARG A 1 853  ? 211.713 226.748 244.901 1.00 75.55  ? 836  ARG B O   1 
ATOM   6491  C CB  . ARG A 1 853  ? 214.652 227.934 243.963 1.00 75.55  ? 836  ARG B CB  1 
ATOM   6492  C CG  . ARG A 1 853  ? 215.202 226.532 244.132 1.00 75.55  ? 836  ARG B CG  1 
ATOM   6493  C CD  . ARG A 1 853  ? 214.974 226.010 245.538 1.00 75.55  ? 836  ARG B CD  1 
ATOM   6494  N NE  . ARG A 1 853  ? 215.889 226.605 246.504 1.00 75.55  ? 836  ARG B NE  1 
ATOM   6495  C CZ  . ARG A 1 853  ? 215.977 226.238 247.775 1.00 75.55  ? 836  ARG B CZ  1 
ATOM   6496  N NH1 . ARG A 1 853  ? 215.227 225.266 248.266 1.00 75.55  ? 836  ARG B NH1 1 
ATOM   6497  N NH2 . ARG A 1 853  ? 216.840 226.859 248.572 1.00 75.55  ? 836  ARG B NH2 1 
ATOM   6498  N N   . LEU A 1 854  ? 212.026 228.919 245.409 1.00 70.65  ? 837  LEU B N   1 
ATOM   6499  C CA  . LEU A 1 854  ? 211.129 228.854 246.557 1.00 70.65  ? 837  LEU B CA  1 
ATOM   6500  C C   . LEU A 1 854  ? 209.699 228.556 246.128 1.00 70.65  ? 837  LEU B C   1 
ATOM   6501  O O   . LEU A 1 854  ? 209.005 227.764 246.773 1.00 70.65  ? 837  LEU B O   1 
ATOM   6502  C CB  . LEU A 1 854  ? 211.193 230.159 247.345 1.00 70.65  ? 837  LEU B CB  1 
ATOM   6503  C CG  . LEU A 1 854  ? 212.452 230.357 248.185 1.00 70.65  ? 837  LEU B CG  1 
ATOM   6504  C CD1 . LEU A 1 854  ? 212.439 231.720 248.850 1.00 70.65  ? 837  LEU B CD1 1 
ATOM   6505  C CD2 . LEU A 1 854  ? 212.568 229.257 249.216 1.00 70.65  ? 837  LEU B CD2 1 
ATOM   6506  N N   . LYS A 1 855  ? 209.236 229.193 245.049 1.00 70.33  ? 838  LYS B N   1 
ATOM   6507  C CA  . LYS A 1 855  ? 207.888 228.929 244.559 1.00 70.33  ? 838  LYS B CA  1 
ATOM   6508  C C   . LYS A 1 855  ? 207.740 227.482 244.119 1.00 70.33  ? 838  LYS B C   1 
ATOM   6509  O O   . LYS A 1 855  ? 206.727 226.835 244.414 1.00 70.33  ? 838  LYS B O   1 
ATOM   6510  C CB  . LYS A 1 855  ? 207.546 229.867 243.404 1.00 70.33  ? 838  LYS B CB  1 
ATOM   6511  C CG  . LYS A 1 855  ? 207.227 231.289 243.816 1.00 70.33  ? 838  LYS B CG  1 
ATOM   6512  C CD  . LYS A 1 855  ? 206.401 231.983 242.748 1.00 70.33  ? 838  LYS B CD  1 
ATOM   6513  C CE  . LYS A 1 855  ? 205.973 233.363 243.199 1.00 70.33  ? 838  LYS B CE  1 
ATOM   6514  N NZ  . LYS A 1 855  ? 207.066 234.037 243.943 1.00 70.33  ? 838  LYS B NZ  1 
ATOM   6515  N N   . ASP A 1 856  ? 208.739 226.955 243.408 1.00 75.66  ? 839  ASP B N   1 
ATOM   6516  C CA  . ASP A 1 856  ? 208.683 225.556 243.005 1.00 75.66  ? 839  ASP B CA  1 
ATOM   6517  C C   . ASP A 1 856  ? 208.647 224.653 244.231 1.00 75.66  ? 839  ASP B C   1 
ATOM   6518  O O   . ASP A 1 856  ? 207.863 223.697 244.287 1.00 75.66  ? 839  ASP B O   1 
ATOM   6519  C CB  . ASP A 1 856  ? 209.880 225.233 242.104 1.00 75.66  ? 839  ASP B CB  1 
ATOM   6520  C CG  . ASP A 1 856  ? 209.869 223.803 241.565 1.00 75.66  ? 839  ASP B CG  1 
ATOM   6521  O OD1 . ASP A 1 856  ? 209.216 222.910 242.140 1.00 75.66  ? 839  ASP B OD1 1 
ATOM   6522  O OD2 . ASP A 1 856  ? 210.526 223.574 240.528 1.00 75.66  ? 839  ASP B OD2 1 
ATOM   6523  N N   . LYS A 1 857  ? 209.464 224.965 245.240 1.00 71.57  ? 840  LYS B N   1 
ATOM   6524  C CA  . LYS A 1 857  ? 209.510 224.144 246.444 1.00 71.57  ? 840  LYS B CA  1 
ATOM   6525  C C   . LYS A 1 857  ? 208.166 224.136 247.159 1.00 71.57  ? 840  LYS B C   1 
ATOM   6526  O O   . LYS A 1 857  ? 207.663 223.075 247.538 1.00 71.57  ? 840  LYS B O   1 
ATOM   6527  C CB  . LYS A 1 857  ? 210.613 224.642 247.378 1.00 71.57  ? 840  LYS B CB  1 
ATOM   6528  C CG  . LYS A 1 857  ? 210.327 224.407 248.849 1.00 71.57  ? 840  LYS B CG  1 
ATOM   6529  C CD  . LYS A 1 857  ? 211.294 225.173 249.731 1.00 71.57  ? 840  LYS B CD  1 
ATOM   6530  C CE  . LYS A 1 857  ? 212.552 224.372 249.986 1.00 71.57  ? 840  LYS B CE  1 
ATOM   6531  N NZ  . LYS A 1 857  ? 212.238 223.081 250.650 1.00 71.57  ? 840  LYS B NZ  1 
ATOM   6532  N N   . VAL A 1 858  ? 207.557 225.310 247.337 1.00 71.68  ? 841  VAL B N   1 
ATOM   6533  C CA  . VAL A 1 858  ? 206.299 225.365 248.077 1.00 71.68  ? 841  VAL B CA  1 
ATOM   6534  C C   . VAL A 1 858  ? 205.181 224.694 247.287 1.00 71.68  ? 841  VAL B C   1 
ATOM   6535  O O   . VAL A 1 858  ? 204.378 223.939 247.851 1.00 71.68  ? 841  VAL B O   1 
ATOM   6536  C CB  . VAL A 1 858  ? 205.942 226.813 248.465 1.00 71.68  ? 841  VAL B CB  1 
ATOM   6537  C CG1 . VAL A 1 858  ? 205.918 227.712 247.267 1.00 71.68  ? 841  VAL B CG1 1 
ATOM   6538  C CG2 . VAL A 1 858  ? 204.597 226.852 249.147 1.00 71.68  ? 841  VAL B CG2 1 
ATOM   6539  N N   . ASN A 1 859  ? 205.114 224.938 245.974 1.00 72.74  ? 842  ASN B N   1 
ATOM   6540  C CA  . ASN A 1 859  ? 204.075 224.311 245.164 1.00 72.74  ? 842  ASN B CA  1 
ATOM   6541  C C   . ASN A 1 859  ? 204.194 222.794 245.199 1.00 72.74  ? 842  ASN B C   1 
ATOM   6542  O O   . ASN A 1 859  ? 203.205 222.087 245.420 1.00 72.74  ? 842  ASN B O   1 
ATOM   6543  C CB  . ASN A 1 859  ? 204.149 224.823 243.727 1.00 72.74  ? 842  ASN B CB  1 
ATOM   6544  C CG  . ASN A 1 859  ? 203.459 226.156 243.549 1.00 72.74  ? 842  ASN B CG  1 
ATOM   6545  O OD1 . ASN A 1 859  ? 204.072 227.133 243.124 1.00 72.74  ? 842  ASN B OD1 1 
ATOM   6546  N ND2 . ASN A 1 859  ? 202.173 226.202 243.868 1.00 72.74  ? 842  ASN B ND2 1 
ATOM   6547  N N   . ASN A 1 860  ? 205.408 222.274 245.007 1.00 76.45  ? 843  ASN B N   1 
ATOM   6548  C CA  . ASN A 1 860  ? 205.587 220.828 245.001 1.00 76.45  ? 843  ASN B CA  1 
ATOM   6549  C C   . ASN A 1 860  ? 205.374 220.228 246.385 1.00 76.45  ? 843  ASN B C   1 
ATOM   6550  O O   . ASN A 1 860  ? 204.895 219.094 246.498 1.00 76.45  ? 843  ASN B O   1 
ATOM   6551  C CB  . ASN A 1 860  ? 206.974 220.476 244.468 1.00 76.45  ? 843  ASN B CB  1 
ATOM   6552  C CG  . ASN A 1 860  ? 207.390 219.063 244.816 1.00 76.45  ? 843  ASN B CG  1 
ATOM   6553  O OD1 . ASN A 1 860  ? 208.059 218.828 245.822 1.00 76.45  ? 843  ASN B OD1 1 
ATOM   6554  N ND2 . ASN A 1 860  ? 206.988 218.108 243.985 1.00 76.45  ? 843  ASN B ND2 1 
ATOM   6555  N N   . THR A 1 861  ? 205.718 220.962 247.445 1.00 74.24  ? 844  THR B N   1 
ATOM   6556  C CA  . THR A 1 861  ? 205.560 220.432 248.793 1.00 74.24  ? 844  THR B CA  1 
ATOM   6557  C C   . THR A 1 861  ? 204.091 220.348 249.181 1.00 74.24  ? 844  THR B C   1 
ATOM   6558  O O   . THR A 1 861  ? 203.635 219.323 249.700 1.00 74.24  ? 844  THR B O   1 
ATOM   6559  C CB  . THR A 1 861  ? 206.324 221.301 249.791 1.00 74.24  ? 844  THR B CB  1 
ATOM   6560  O OG1 . THR A 1 861  ? 207.592 221.667 249.236 1.00 74.24  ? 844  THR B OG1 1 
ATOM   6561  C CG2 . THR A 1 861  ? 206.554 220.539 251.082 1.00 74.24  ? 844  THR B CG2 1 
ATOM   6562  N N   . LEU A 1 862  ? 203.331 221.412 248.932 1.00 71.21  ? 845  LEU B N   1 
ATOM   6563  C CA  . LEU A 1 862  ? 201.947 221.459 249.380 1.00 71.21  ? 845  LEU B CA  1 
ATOM   6564  C C   . LEU A 1 862  ? 200.961 220.909 248.360 1.00 71.21  ? 845  LEU B C   1 
ATOM   6565  O O   . LEU A 1 862  ? 199.774 220.788 248.679 1.00 71.21  ? 845  LEU B O   1 
ATOM   6566  C CB  . LEU A 1 862  ? 201.561 222.893 249.746 1.00 71.21  ? 845  LEU B CB  1 
ATOM   6567  C CG  . LEU A 1 862  ? 202.557 223.620 250.648 1.00 71.21  ? 845  LEU B CG  1 
ATOM   6568  C CD1 . LEU A 1 862  ? 202.036 224.989 251.005 1.00 71.21  ? 845  LEU B CD1 1 
ATOM   6569  C CD2 . LEU A 1 862  ? 202.831 222.817 251.901 1.00 71.21  ? 845  LEU B CD2 1 
ATOM   6570  N N   . SER A 1 863  ? 201.409 220.572 247.149 1.00 77.35  ? 846  SER B N   1 
ATOM   6571  C CA  . SER A 1 863  ? 200.497 219.969 246.182 1.00 77.35  ? 846  SER B CA  1 
ATOM   6572  C C   . SER A 1 863  ? 200.127 218.546 246.582 1.00 77.35  ? 846  SER B C   1 
ATOM   6573  O O   . SER A 1 863  ? 198.981 218.123 246.401 1.00 77.35  ? 846  SER B O   1 
ATOM   6574  C CB  . SER A 1 863  ? 201.121 219.987 244.789 1.00 77.35  ? 846  SER B CB  1 
ATOM   6575  O OG  . SER A 1 863  ? 202.499 219.668 244.848 1.00 77.35  ? 846  SER B OG  1 
ATOM   6576  N N   . THR A 1 864  ? 201.082 217.796 247.123 1.00 76.26  ? 847  THR B N   1 
ATOM   6577  C CA  . THR A 1 864  ? 200.860 216.410 247.500 1.00 76.26  ? 847  THR B CA  1 
ATOM   6578  C C   . THR A 1 864  ? 200.408 216.334 248.957 1.00 76.26  ? 847  THR B C   1 
ATOM   6579  O O   . THR A 1 864  ? 200.067 217.343 249.580 1.00 76.26  ? 847  THR B O   1 
ATOM   6580  C CB  . THR A 1 864  ? 202.124 215.589 247.263 1.00 76.26  ? 847  THR B CB  1 
ATOM   6581  O OG1 . THR A 1 864  ? 203.002 215.730 248.387 1.00 76.26  ? 847  THR B OG1 1 
ATOM   6582  C CG2 . THR A 1 864  ? 202.837 216.068 246.009 1.00 76.26  ? 847  THR B CG2 1 
ATOM   6583  N N   . ASP A 1 865  ? 200.395 215.126 249.514 1.00 78.83  ? 848  ASP B N   1 
ATOM   6584  C CA  . ASP A 1 865  ? 200.014 214.907 250.900 1.00 78.83  ? 848  ASP B CA  1 
ATOM   6585  C C   . ASP A 1 865  ? 200.962 213.906 251.546 1.00 78.83  ? 848  ASP B C   1 
ATOM   6586  O O   . ASP A 1 865  ? 201.594 213.089 250.873 1.00 78.83  ? 848  ASP B O   1 
ATOM   6587  C CB  . ASP A 1 865  ? 198.557 214.426 251.016 1.00 78.83  ? 848  ASP B CB  1 
ATOM   6588  C CG  . ASP A 1 865  ? 198.248 213.237 250.121 1.00 78.83  ? 848  ASP B CG  1 
ATOM   6589  O OD1 . ASP A 1 865  ? 199.149 212.415 249.855 1.00 78.83  ? 848  ASP B OD1 1 
ATOM   6590  O OD2 . ASP A 1 865  ? 197.086 213.124 249.678 1.00 78.83  ? 848  ASP B OD2 1 
ATOM   6591  N N   . ILE A 1 866  ? 201.063 213.989 252.869 1.00 73.96  ? 849  ILE B N   1 
ATOM   6592  C CA  . ILE A 1 866  ? 201.898 213.072 253.638 1.00 73.96  ? 849  ILE B CA  1 
ATOM   6593  C C   . ILE A 1 866  ? 201.174 211.737 253.757 1.00 73.96  ? 849  ILE B C   1 
ATOM   6594  O O   . ILE A 1 866  ? 200.019 211.699 254.203 1.00 73.96  ? 849  ILE B O   1 
ATOM   6595  C CB  . ILE A 1 866  ? 202.236 213.649 255.021 1.00 73.96  ? 849  ILE B CB  1 
ATOM   6596  C CG1 . ILE A 1 866  ? 203.340 214.697 254.897 1.00 73.96  ? 849  ILE B CG1 1 
ATOM   6597  C CG2 . ILE A 1 866  ? 202.653 212.541 255.971 1.00 73.96  ? 849  ILE B CG2 1 
ATOM   6598  C CD1 . ILE A 1 866  ? 204.022 215.027 256.203 1.00 73.96  ? 849  ILE B CD1 1 
ATOM   6599  N N   . PRO A 1 867  ? 201.796 210.629 253.365 1.00 76.22  ? 850  PRO B N   1 
ATOM   6600  C CA  . PRO A 1 867  ? 201.117 209.335 253.458 1.00 76.22  ? 850  PRO B CA  1 
ATOM   6601  C C   . PRO A 1 867  ? 200.871 208.940 254.903 1.00 76.22  ? 850  PRO B C   1 
ATOM   6602  O O   . PRO A 1 867  ? 201.629 209.294 255.808 1.00 76.22  ? 850  PRO B O   1 
ATOM   6603  C CB  . PRO A 1 867  ? 202.097 208.371 252.781 1.00 76.22  ? 850  PRO B CB  1 
ATOM   6604  C CG  . PRO A 1 867  ? 203.427 209.014 252.961 1.00 76.22  ? 850  PRO B CG  1 
ATOM   6605  C CD  . PRO A 1 867  ? 203.184 210.495 252.891 1.00 76.22  ? 850  PRO B CD  1 
ATOM   6606  N N   . PHE A 1 868  ? 199.788 208.198 255.113 1.00 74.37  ? 851  PHE B N   1 
ATOM   6607  C CA  . PHE A 1 868  ? 199.449 207.679 256.432 1.00 74.37  ? 851  PHE B CA  1 
ATOM   6608  C C   . PHE A 1 868  ? 200.033 206.280 256.570 1.00 74.37  ? 851  PHE B C   1 
ATOM   6609  O O   . PHE A 1 868  ? 199.546 205.333 255.945 1.00 74.37  ? 851  PHE B O   1 
ATOM   6610  C CB  . PHE A 1 868  ? 197.939 207.654 256.643 1.00 74.37  ? 851  PHE B CB  1 
ATOM   6611  C CG  . PHE A 1 868  ? 197.525 207.021 257.940 1.00 74.37  ? 851  PHE B CG  1 
ATOM   6612  C CD1 . PHE A 1 868  ? 198.075 207.441 259.136 1.00 74.37  ? 851  PHE B CD1 1 
ATOM   6613  C CD2 . PHE A 1 868  ? 196.604 205.992 257.960 1.00 74.37  ? 851  PHE B CD2 1 
ATOM   6614  C CE1 . PHE A 1 868  ? 197.701 206.857 260.328 1.00 74.37  ? 851  PHE B CE1 1 
ATOM   6615  C CE2 . PHE A 1 868  ? 196.229 205.405 259.150 1.00 74.37  ? 851  PHE B CE2 1 
ATOM   6616  C CZ  . PHE A 1 868  ? 196.779 205.839 260.334 1.00 74.37  ? 851  PHE B CZ  1 
ATOM   6617  N N   . GLN A 1 869  ? 201.073 206.148 257.385 1.00 80.08  ? 852  GLN B N   1 
ATOM   6618  C CA  . GLN A 1 869  ? 201.663 204.856 257.704 1.00 80.08  ? 852  GLN B CA  1 
ATOM   6619  C C   . GLN A 1 869  ? 201.383 204.545 259.167 1.00 80.08  ? 852  GLN B C   1 
ATOM   6620  O O   . GLN A 1 869  ? 201.774 205.311 260.054 1.00 80.08  ? 852  GLN B O   1 
ATOM   6621  C CB  . GLN A 1 869  ? 203.163 204.849 257.416 1.00 80.08  ? 852  GLN B CB  1 
ATOM   6622  C CG  . GLN A 1 869  ? 203.855 206.168 257.694 1.00 80.08  ? 852  GLN B CG  1 
ATOM   6623  C CD  . GLN A 1 869  ? 205.168 206.302 256.950 1.00 80.08  ? 852  GLN B CD  1 
ATOM   6624  O OE1 . GLN A 1 869  ? 206.021 205.418 257.011 1.00 80.08  ? 852  GLN B OE1 1 
ATOM   6625  N NE2 . GLN A 1 869  ? 205.337 207.412 256.242 1.00 80.08  ? 852  GLN B NE2 1 
ATOM   6626  N N   . LEU A 1 870  ? 200.706 203.424 259.414 1.00 77.54  ? 853  LEU B N   1 
ATOM   6627  C CA  . LEU A 1 870  ? 200.310 203.067 260.770 1.00 77.54  ? 853  LEU B CA  1 
ATOM   6628  C C   . LEU A 1 870  ? 201.492 202.651 261.630 1.00 77.54  ? 853  LEU B C   1 
ATOM   6629  O O   . LEU A 1 870  ? 201.373 202.640 262.859 1.00 77.54  ? 853  LEU B O   1 
ATOM   6630  C CB  . LEU A 1 870  ? 199.279 201.940 260.731 1.00 77.54  ? 853  LEU B CB  1 
ATOM   6631  C CG  . LEU A 1 870  ? 198.450 201.691 261.988 1.00 77.54  ? 853  LEU B CG  1 
ATOM   6632  C CD1 . LEU A 1 870  ? 197.579 202.894 262.285 1.00 77.54  ? 853  LEU B CD1 1 
ATOM   6633  C CD2 . LEU A 1 870  ? 197.606 200.441 261.828 1.00 77.54  ? 853  LEU B CD2 1 
ATOM   6634  N N   . SER A 1 871  ? 202.630 202.321 261.019 1.00 80.84  ? 854  SER B N   1 
ATOM   6635  C CA  . SER A 1 871  ? 203.766 201.818 261.781 1.00 80.84  ? 854  SER B CA  1 
ATOM   6636  C C   . SER A 1 871  ? 204.337 202.855 262.739 1.00 80.84  ? 854  SER B C   1 
ATOM   6637  O O   . SER A 1 871  ? 205.077 202.487 263.657 1.00 80.84  ? 854  SER B O   1 
ATOM   6638  C CB  . SER A 1 871  ? 204.860 201.333 260.830 1.00 80.84  ? 854  SER B CB  1 
ATOM   6639  O OG  . SER A 1 871  ? 206.143 201.490 261.408 1.00 80.84  ? 854  SER B OG  1 
ATOM   6640  N N   . LYS A 1 872  ? 204.014 204.131 262.555 1.00 81.15  ? 855  LYS B N   1 
ATOM   6641  C CA  . LYS A 1 872  ? 204.538 205.188 263.407 1.00 81.15  ? 855  LYS B CA  1 
ATOM   6642  C C   . LYS A 1 872  ? 203.627 205.526 264.578 1.00 81.15  ? 855  LYS B C   1 
ATOM   6643  O O   . LYS A 1 872  ? 203.942 206.446 265.339 1.00 81.15  ? 855  LYS B O   1 
ATOM   6644  C CB  . LYS A 1 872  ? 204.792 206.454 262.584 1.00 81.15  ? 855  LYS B CB  1 
ATOM   6645  C CG  . LYS A 1 872  ? 205.771 206.269 261.441 1.00 81.15  ? 855  LYS B CG  1 
ATOM   6646  C CD  . LYS A 1 872  ? 205.726 207.444 260.479 1.00 81.15  ? 855  LYS B CD  1 
ATOM   6647  C CE  . LYS A 1 872  ? 205.824 208.774 261.208 1.00 81.15  ? 855  LYS B CE  1 
ATOM   6648  N NZ  . LYS A 1 872  ? 206.988 208.827 262.135 1.00 81.15  ? 855  LYS B NZ  1 
ATOM   6649  N N   . TYR A 1 873  ? 202.512 204.818 264.746 1.00 76.49  ? 856  TYR B N   1 
ATOM   6650  C CA  . TYR A 1 873  ? 201.573 205.122 265.819 1.00 76.49  ? 856  TYR B CA  1 
ATOM   6651  C C   . TYR A 1 873  ? 201.174 203.927 266.667 1.00 76.49  ? 856  TYR B C   1 
ATOM   6652  O O   . TYR A 1 873  ? 200.830 204.122 267.838 1.00 76.49  ? 856  TYR B O   1 
ATOM   6653  C CB  . TYR A 1 873  ? 200.304 205.767 265.249 1.00 76.49  ? 856  TYR B CB  1 
ATOM   6654  C CG  . TYR A 1 873  ? 200.595 206.894 264.292 1.00 76.49  ? 856  TYR B CG  1 
ATOM   6655  C CD1 . TYR A 1 873  ? 200.954 208.146 264.759 1.00 76.49  ? 856  TYR B CD1 1 
ATOM   6656  C CD2 . TYR A 1 873  ? 200.524 206.703 262.923 1.00 76.49  ? 856  TYR B CD2 1 
ATOM   6657  C CE1 . TYR A 1 873  ? 201.226 209.177 263.891 1.00 76.49  ? 856  TYR B CE1 1 
ATOM   6658  C CE2 . TYR A 1 873  ? 200.794 207.729 262.046 1.00 76.49  ? 856  TYR B CE2 1 
ATOM   6659  C CZ  . TYR A 1 873  ? 201.146 208.964 262.535 1.00 76.49  ? 856  TYR B CZ  1 
ATOM   6660  O OH  . TYR A 1 873  ? 201.418 209.990 261.663 1.00 76.49  ? 856  TYR B OH  1 
ATOM   6661  N N   . VAL A 1 874  ? 201.203 202.709 266.134 1.00 82.22  ? 857  VAL B N   1 
ATOM   6662  C CA  . VAL A 1 874  ? 200.908 201.513 266.908 1.00 82.22  ? 857  VAL B CA  1 
ATOM   6663  C C   . VAL A 1 874  ? 202.059 200.536 266.732 1.00 82.22  ? 857  VAL B C   1 
ATOM   6664  O O   . VAL A 1 874  ? 202.814 200.603 265.757 1.00 82.22  ? 857  VAL B O   1 
ATOM   6665  C CB  . VAL A 1 874  ? 199.569 200.861 266.498 1.00 82.22  ? 857  VAL B CB  1 
ATOM   6666  C CG1 . VAL A 1 874  ? 198.498 201.916 266.309 1.00 82.22  ? 857  VAL B CG1 1 
ATOM   6667  C CG2 . VAL A 1 874  ? 199.738 200.043 265.234 1.00 82.22  ? 857  VAL B CG2 1 
ATOM   6668  N N   . ASP A 1 875  ? 202.203 199.632 267.695 1.00 91.18  ? 858  ASP B N   1 
ATOM   6669  C CA  . ASP A 1 875  ? 203.259 198.627 267.684 1.00 91.18  ? 858  ASP B CA  1 
ATOM   6670  C C   . ASP A 1 875  ? 202.675 197.218 267.758 1.00 91.18  ? 858  ASP B C   1 
ATOM   6671  O O   . ASP A 1 875  ? 203.248 196.317 268.371 1.00 91.18  ? 858  ASP B O   1 
ATOM   6672  C CB  . ASP A 1 875  ? 204.244 198.871 268.825 1.00 91.18  ? 858  ASP B CB  1 
ATOM   6673  C CG  . ASP A 1 875  ? 205.524 198.072 268.676 1.00 91.18  ? 858  ASP B CG  1 
ATOM   6674  O OD1 . ASP A 1 875  ? 205.865 197.705 267.532 1.00 91.18  ? 858  ASP B OD1 1 
ATOM   6675  O OD2 . ASP A 1 875  ? 206.188 197.809 269.700 1.00 91.18  ? 858  ASP B OD2 1 
ATOM   6676  N N   . ASN A 1 876  ? 201.519 197.014 267.133 1.00 89.78  ? 859  ASN B N   1 
ATOM   6677  C CA  . ASN A 1 876  ? 200.861 195.715 267.110 1.00 89.78  ? 859  ASN B CA  1 
ATOM   6678  C C   . ASN A 1 876  ? 201.133 195.052 265.766 1.00 89.78  ? 859  ASN B C   1 
ATOM   6679  O O   . ASN A 1 876  ? 200.680 195.539 264.725 1.00 89.78  ? 859  ASN B O   1 
ATOM   6680  C CB  . ASN A 1 876  ? 199.359 195.861 267.350 1.00 89.78  ? 859  ASN B CB  1 
ATOM   6681  C CG  . ASN A 1 876  ? 198.719 194.573 267.826 1.00 89.78  ? 859  ASN B CG  1 
ATOM   6682  O OD1 . ASN A 1 876  ? 197.526 194.346 267.626 1.00 89.78  ? 859  ASN B OD1 1 
ATOM   6683  N ND2 . ASN A 1 876  ? 199.512 193.721 268.462 1.00 89.78  ? 859  ASN B ND2 1 
ATOM   6684  N N   . GLN A 1 877  ? 201.873 193.942 265.795 1.00 90.45  ? 860  GLN B N   1 
ATOM   6685  C CA  . GLN A 1 877  ? 202.285 193.276 264.563 1.00 90.45  ? 860  GLN B CA  1 
ATOM   6686  C C   . GLN A 1 877  ? 201.075 192.759 263.792 1.00 90.45  ? 860  GLN B C   1 
ATOM   6687  O O   . GLN A 1 877  ? 200.974 192.939 262.570 1.00 90.45  ? 860  GLN B O   1 
ATOM   6688  C CB  . GLN A 1 877  ? 203.247 192.133 264.910 1.00 90.45  ? 860  GLN B CB  1 
ATOM   6689  C CG  . GLN A 1 877  ? 203.506 191.005 263.878 1.00 90.45  ? 860  GLN B CG  1 
ATOM   6690  C CD  . GLN A 1 877  ? 203.560 191.411 262.400 1.00 90.45  ? 860  GLN B CD  1 
ATOM   6691  O OE1 . GLN A 1 877  ? 203.580 192.589 262.044 1.00 90.45  ? 860  GLN B OE1 1 
ATOM   6692  N NE2 . GLN A 1 877  ? 203.585 190.407 261.531 1.00 90.45  ? 860  GLN B NE2 1 
ATOM   6693  N N   . ARG A 1 878  ? 200.131 192.137 264.503 1.00 86.88  ? 861  ARG B N   1 
ATOM   6694  C CA  . ARG A 1 878  ? 198.989 191.509 263.846 1.00 86.88  ? 861  ARG B CA  1 
ATOM   6695  C C   . ARG A 1 878  ? 198.163 192.533 263.081 1.00 86.88  ? 861  ARG B C   1 
ATOM   6696  O O   . ARG A 1 878  ? 197.700 192.262 261.968 1.00 86.88  ? 861  ARG B O   1 
ATOM   6697  C CB  . ARG A 1 878  ? 198.132 190.786 264.885 1.00 86.88  ? 861  ARG B CB  1 
ATOM   6698  C CG  . ARG A 1 878  ? 196.773 190.329 264.386 1.00 86.88  ? 861  ARG B CG  1 
ATOM   6699  C CD  . ARG A 1 878  ? 195.890 189.875 265.542 1.00 86.88  ? 861  ARG B CD  1 
ATOM   6700  N NE  . ARG A 1 878  ? 196.089 190.691 266.733 1.00 86.88  ? 861  ARG B NE  1 
ATOM   6701  C CZ  . ARG A 1 878  ? 195.437 191.817 266.987 1.00 86.88  ? 861  ARG B CZ  1 
ATOM   6702  N NH1 . ARG A 1 878  ? 194.519 192.287 266.158 1.00 86.88  ? 861  ARG B NH1 1 
ATOM   6703  N NH2 . ARG A 1 878  ? 195.712 192.489 268.101 1.00 86.88  ? 861  ARG B NH2 1 
ATOM   6704  N N   . LEU A 1 879  ? 197.976 193.717 263.657 1.00 83.85  ? 862  LEU B N   1 
ATOM   6705  C CA  . LEU A 1 879  ? 197.219 194.764 262.986 1.00 83.85  ? 862  LEU B CA  1 
ATOM   6706  C C   . LEU A 1 879  ? 198.030 195.445 261.891 1.00 83.85  ? 862  LEU B C   1 
ATOM   6707  O O   . LEU A 1 879  ? 197.471 195.831 260.856 1.00 83.85  ? 862  LEU B O   1 
ATOM   6708  C CB  . LEU A 1 879  ? 196.747 195.786 264.015 1.00 83.85  ? 862  LEU B CB  1 
ATOM   6709  C CG  . LEU A 1 879  ? 195.314 196.277 263.874 1.00 83.85  ? 862  LEU B CG  1 
ATOM   6710  C CD1 . LEU A 1 879  ? 194.358 195.133 264.122 1.00 83.85  ? 862  LEU B CD1 1 
ATOM   6711  C CD2 . LEU A 1 879  ? 195.082 197.372 264.880 1.00 83.85  ? 862  LEU B CD2 1 
ATOM   6712  N N   . LEU A 1 880  ? 199.340 195.599 262.095 1.00 84.87  ? 863  LEU B N   1 
ATOM   6713  C CA  . LEU A 1 880  ? 200.173 196.247 261.089 1.00 84.87  ? 863  LEU B CA  1 
ATOM   6714  C C   . LEU A 1 880  ? 200.243 195.422 259.811 1.00 84.87  ? 863  LEU B C   1 
ATOM   6715  O O   . LEU A 1 880  ? 200.288 195.982 258.709 1.00 84.87  ? 863  LEU B O   1 
ATOM   6716  C CB  . LEU A 1 880  ? 201.573 196.498 261.644 1.00 84.87  ? 863  LEU B CB  1 
ATOM   6717  C CG  . LEU A 1 880  ? 201.710 197.726 262.544 1.00 84.87  ? 863  LEU B CG  1 
ATOM   6718  C CD1 . LEU A 1 880  ? 203.089 197.783 263.181 1.00 84.87  ? 863  LEU B CD1 1 
ATOM   6719  C CD2 . LEU A 1 880  ? 201.428 198.990 261.757 1.00 84.87  ? 863  LEU B CD2 1 
ATOM   6720  N N   . SER A 1 881  ? 200.264 194.092 259.931 1.00 84.69  ? 864  SER B N   1 
ATOM   6721  C CA  . SER A 1 881  ? 200.271 193.258 258.731 1.00 84.69  ? 864  SER B CA  1 
ATOM   6722  C C   . SER A 1 881  ? 199.015 193.480 257.896 1.00 84.69  ? 864  SER B C   1 
ATOM   6723  O O   . SER A 1 881  ? 199.089 193.637 256.668 1.00 84.69  ? 864  SER B O   1 
ATOM   6724  C CB  . SER A 1 881  ? 200.404 191.787 259.115 1.00 84.69  ? 864  SER B CB  1 
ATOM   6725  O OG  . SER A 1 881  ? 199.135 191.160 259.147 1.00 84.69  ? 864  SER B OG  1 
ATOM   6726  N N   . THR A 1 882  ? 197.850 193.511 258.546 1.00 81.91  ? 865  THR B N   1 
ATOM   6727  C CA  . THR A 1 882  ? 196.611 193.741 257.812 1.00 81.91  ? 865  THR B CA  1 
ATOM   6728  C C   . THR A 1 882  ? 196.557 195.154 257.250 1.00 81.91  ? 865  THR B C   1 
ATOM   6729  O O   . THR A 1 882  ? 195.983 195.376 256.179 1.00 81.91  ? 865  THR B O   1 
ATOM   6730  C CB  . THR A 1 882  ? 195.405 193.472 258.706 1.00 81.91  ? 865  THR B CB  1 
ATOM   6731  O OG1 . THR A 1 882  ? 195.231 194.564 259.613 1.00 81.91  ? 865  THR B OG1 1 
ATOM   6732  C CG2 . THR A 1 882  ? 195.601 192.189 259.488 1.00 81.91  ? 865  THR B CG2 1 
ATOM   6733  N N   . PHE A 1 883  ? 197.150 196.127 257.945 1.00 77.67  ? 866  PHE B N   1 
ATOM   6734  C CA  . PHE A 1 883  ? 197.201 197.473 257.381 1.00 77.67  ? 866  PHE B CA  1 
ATOM   6735  C C   . PHE A 1 883  ? 198.067 197.516 256.128 1.00 77.67  ? 866  PHE B C   1 
ATOM   6736  O O   . PHE A 1 883  ? 197.735 198.208 255.159 1.00 77.67  ? 866  PHE B O   1 
ATOM   6737  C CB  . PHE A 1 883  ? 197.720 198.477 258.402 1.00 77.67  ? 866  PHE B CB  1 
ATOM   6738  C CG  . PHE A 1 883  ? 198.024 199.820 257.808 1.00 77.67  ? 866  PHE B CG  1 
ATOM   6739  C CD1 . PHE A 1 883  ? 197.001 200.657 257.405 1.00 77.67  ? 866  PHE B CD1 1 
ATOM   6740  C CD2 . PHE A 1 883  ? 199.329 200.237 257.632 1.00 77.67  ? 866  PHE B CD2 1 
ATOM   6741  C CE1 . PHE A 1 883  ? 197.274 201.888 256.854 1.00 77.67  ? 866  PHE B CE1 1 
ATOM   6742  C CE2 . PHE A 1 883  ? 199.606 201.468 257.080 1.00 77.67  ? 866  PHE B CE2 1 
ATOM   6743  C CZ  . PHE A 1 883  ? 198.577 202.294 256.693 1.00 77.67  ? 866  PHE B CZ  1 
ATOM   6744  N N   . THR A 1 884  ? 199.197 196.806 256.138 1.00 81.28  ? 867  THR B N   1 
ATOM   6745  C CA  . THR A 1 884  ? 200.027 196.741 254.939 1.00 81.28  ? 867  THR B CA  1 
ATOM   6746  C C   . THR A 1 884  ? 199.273 196.081 253.793 1.00 81.28  ? 867  THR B C   1 
ATOM   6747  O O   . THR A 1 884  ? 199.364 196.525 252.641 1.00 81.28  ? 867  THR B O   1 
ATOM   6748  C CB  . THR A 1 884  ? 201.328 195.991 255.222 1.00 81.28  ? 867  THR B CB  1 
ATOM   6749  O OG1 . THR A 1 884  ? 201.029 194.688 255.738 1.00 81.28  ? 867  THR B OG1 1 
ATOM   6750  C CG2 . THR A 1 884  ? 202.179 196.753 256.222 1.00 81.28  ? 867  THR B CG2 1 
ATOM   6751  N N   . GLU A 1 885  ? 198.517 195.022 254.090 1.00 84.08  ? 868  GLU B N   1 
ATOM   6752  C CA  . GLU A 1 885  ? 197.689 194.405 253.056 1.00 84.08  ? 868  GLU B CA  1 
ATOM   6753  C C   . GLU A 1 885  ? 196.640 195.381 252.530 1.00 84.08  ? 868  GLU B C   1 
ATOM   6754  O O   . GLU A 1 885  ? 196.343 195.397 251.330 1.00 84.08  ? 868  GLU B O   1 
ATOM   6755  C CB  . GLU A 1 885  ? 197.023 193.139 253.591 1.00 84.08  ? 868  GLU B CB  1 
ATOM   6756  C CG  . GLU A 1 885  ? 197.997 192.050 253.999 1.00 84.08  ? 868  GLU B CG  1 
ATOM   6757  C CD  . GLU A 1 885  ? 197.304 190.735 254.294 1.00 84.08  ? 868  GLU B CD  1 
ATOM   6758  O OE1 . GLU A 1 885  ? 196.219 190.493 253.725 1.00 84.08  ? 868  GLU B OE1 1 
ATOM   6759  O OE2 . GLU A 1 885  ? 197.843 189.942 255.094 1.00 84.08  ? 868  GLU B OE2 1 
ATOM   6760  N N   . TYR A 1 886  ? 196.059 196.191 253.417 1.00 77.29  ? 869  TYR B N   1 
ATOM   6761  C CA  . TYR A 1 886  ? 195.105 197.211 252.988 1.00 77.29  ? 869  TYR B CA  1 
ATOM   6762  C C   . TYR A 1 886  ? 195.754 198.217 252.050 1.00 77.29  ? 869  TYR B C   1 
ATOM   6763  O O   . TYR A 1 886  ? 195.172 198.591 251.026 1.00 77.29  ? 869  TYR B O   1 
ATOM   6764  C CB  . TYR A 1 886  ? 194.524 197.925 254.209 1.00 77.29  ? 869  TYR B CB  1 
ATOM   6765  C CG  . TYR A 1 886  ? 193.340 198.815 253.912 1.00 77.29  ? 869  TYR B CG  1 
ATOM   6766  C CD1 . TYR A 1 886  ? 193.519 200.140 253.547 1.00 77.29  ? 869  TYR B CD1 1 
ATOM   6767  C CD2 . TYR A 1 886  ? 192.045 198.334 254.006 1.00 77.29  ? 869  TYR B CD2 1 
ATOM   6768  C CE1 . TYR A 1 886  ? 192.443 200.956 253.279 1.00 77.29  ? 869  TYR B CE1 1 
ATOM   6769  C CE2 . TYR A 1 886  ? 190.963 199.143 253.739 1.00 77.29  ? 869  TYR B CE2 1 
ATOM   6770  C CZ  . TYR A 1 886  ? 191.167 200.453 253.376 1.00 77.29  ? 869  TYR B CZ  1 
ATOM   6771  O OH  . TYR A 1 886  ? 190.089 201.262 253.109 1.00 77.29  ? 869  TYR B OH  1 
ATOM   6772  N N   . ILE A 1 887  ? 196.957 198.675 252.391 1.00 78.84  ? 870  ILE B N   1 
ATOM   6773  C CA  . ILE A 1 887  ? 197.644 199.665 251.568 1.00 78.84  ? 870  ILE B CA  1 
ATOM   6774  C C   . ILE A 1 887  ? 198.062 199.066 250.230 1.00 78.84  ? 870  ILE B C   1 
ATOM   6775  O O   . ILE A 1 887  ? 198.120 199.775 249.217 1.00 78.84  ? 870  ILE B O   1 
ATOM   6776  C CB  . ILE A 1 887  ? 198.842 200.245 252.342 1.00 78.84  ? 870  ILE B CB  1 
ATOM   6777  C CG1 . ILE A 1 887  ? 198.345 201.168 253.450 1.00 78.84  ? 870  ILE B CG1 1 
ATOM   6778  C CG2 . ILE A 1 887  ? 199.783 201.003 251.426 1.00 78.84  ? 870  ILE B CG2 1 
ATOM   6779  C CD1 . ILE A 1 887  ? 197.449 202.276 252.954 1.00 78.84  ? 870  ILE B CD1 1 
ATOM   6780  N N   . LYS A 1 888  ? 198.335 197.759 250.196 1.00 78.32  ? 871  LYS B N   1 
ATOM   6781  C CA  . LYS A 1 888  ? 198.861 197.130 248.987 1.00 78.32  ? 871  LYS B CA  1 
ATOM   6782  C C   . LYS A 1 888  ? 197.942 197.347 247.790 1.00 78.32  ? 871  LYS B C   1 
ATOM   6783  O O   . LYS A 1 888  ? 198.389 197.781 246.723 1.00 78.32  ? 871  LYS B O   1 
ATOM   6784  C CB  . LYS A 1 888  ? 199.074 195.638 249.232 1.00 78.32  ? 871  LYS B CB  1 
ATOM   6785  C CG  . LYS A 1 888  ? 199.508 194.864 248.002 1.00 78.32  ? 871  LYS B CG  1 
ATOM   6786  C CD  . LYS A 1 888  ? 199.767 193.405 248.334 1.00 78.32  ? 871  LYS B CD  1 
ATOM   6787  C CE  . LYS A 1 888  ? 200.765 193.260 249.473 1.00 78.32  ? 871  LYS B CE  1 
ATOM   6788  N NZ  . LYS A 1 888  ? 201.950 194.148 249.311 1.00 78.32  ? 871  LYS B NZ  1 
ATOM   6789  N N   . ASN A 1 889  ? 196.655 197.052 247.946 1.00 79.37  ? 872  ASN B N   1 
ATOM   6790  C CA  . ASN A 1 889  ? 195.728 197.179 246.829 1.00 79.37  ? 872  ASN B CA  1 
ATOM   6791  C C   . ASN A 1 889  ? 195.443 198.645 246.526 1.00 79.37  ? 872  ASN B C   1 
ATOM   6792  O O   . ASN A 1 889  ? 195.237 199.457 247.431 1.00 79.37  ? 872  ASN B O   1 
ATOM   6793  C CB  . ASN A 1 889  ? 194.426 196.440 247.133 1.00 79.37  ? 872  ASN B CB  1 
ATOM   6794  C CG  . ASN A 1 889  ? 193.601 196.175 245.889 1.00 79.37  ? 872  ASN B CG  1 
ATOM   6795  O OD1 . ASN A 1 889  ? 193.309 197.087 245.117 1.00 79.37  ? 872  ASN B OD1 1 
ATOM   6796  N ND2 . ASN A 1 889  ? 193.224 194.919 245.687 1.00 79.37  ? 872  ASN B ND2 1 
ATOM   6797  N N   . ILE A 1 890  ? 195.432 198.979 245.235 1.00 74.50  ? 873  ILE B N   1 
ATOM   6798  C CA  . ILE A 1 890  ? 195.174 200.353 244.819 1.00 74.50  ? 873  ILE B CA  1 
ATOM   6799  C C   . ILE A 1 890  ? 193.707 200.728 245.003 1.00 74.50  ? 873  ILE B C   1 
ATOM   6800  O O   . ILE A 1 890  ? 193.397 201.872 245.353 1.00 74.50  ? 873  ILE B O   1 
ATOM   6801  C CB  . ILE A 1 890  ? 195.634 200.556 243.365 1.00 74.50  ? 873  ILE B CB  1 
ATOM   6802  C CG1 . ILE A 1 890  ? 195.299 201.968 242.885 1.00 74.50  ? 873  ILE B CG1 1 
ATOM   6803  C CG2 . ILE A 1 890  ? 195.022 199.508 242.453 1.00 74.50  ? 873  ILE B CG2 1 
ATOM   6804  C CD1 . ILE A 1 890  ? 196.028 203.048 243.635 1.00 74.50  ? 873  ILE B CD1 1 
ATOM   6805  N N   . ILE A 1 891  ? 192.789 199.784 244.786 1.00 73.13  ? 874  ILE B N   1 
ATOM   6806  C CA  . ILE A 1 891  ? 191.365 200.098 244.841 1.00 73.13  ? 874  ILE B CA  1 
ATOM   6807  C C   . ILE A 1 891  ? 190.959 200.526 246.247 1.00 73.13  ? 874  ILE B C   1 
ATOM   6808  O O   . ILE A 1 891  ? 190.104 201.403 246.420 1.00 73.13  ? 874  ILE B O   1 
ATOM   6809  C CB  . ILE A 1 891  ? 190.542 198.897 244.341 1.00 73.13  ? 874  ILE B CB  1 
ATOM   6810  C CG1 . ILE A 1 891  ? 190.490 198.893 242.813 1.00 73.13  ? 874  ILE B CG1 1 
ATOM   6811  C CG2 . ILE A 1 891  ? 189.138 198.913 244.914 1.00 73.13  ? 874  ILE B CG2 1 
ATOM   6812  C CD1 . ILE A 1 891  ? 190.381 197.514 242.209 1.00 73.13  ? 874  ILE B CD1 1 
ATOM   6813  N N   . ASN A 1 892  ? 191.575 199.932 247.272 1.00 76.67  ? 875  ASN B N   1 
ATOM   6814  C CA  . ASN A 1 892  ? 191.229 200.275 248.648 1.00 76.67  ? 875  ASN B CA  1 
ATOM   6815  C C   . ASN A 1 892  ? 191.455 201.753 248.941 1.00 76.67  ? 875  ASN B C   1 
ATOM   6816  O O   . ASN A 1 892  ? 190.773 202.324 249.799 1.00 76.67  ? 875  ASN B O   1 
ATOM   6817  C CB  . ASN A 1 892  ? 192.036 199.419 249.622 1.00 76.67  ? 875  ASN B CB  1 
ATOM   6818  C CG  . ASN A 1 892  ? 191.794 197.938 249.432 1.00 76.67  ? 875  ASN B CG  1 
ATOM   6819  O OD1 . ASN A 1 892  ? 192.652 197.114 249.742 1.00 76.67  ? 875  ASN B OD1 1 
ATOM   6820  N ND2 . ASN A 1 892  ? 190.621 197.592 248.921 1.00 76.67  ? 875  ASN B ND2 1 
ATOM   6821  N N   . THR A 1 893  ? 192.395 202.388 248.246 1.00 71.69  ? 876  THR B N   1 
ATOM   6822  C CA  . THR A 1 893  ? 192.690 203.799 248.449 1.00 71.69  ? 876  THR B CA  1 
ATOM   6823  C C   . THR A 1 893  ? 191.885 204.710 247.533 1.00 71.69  ? 876  THR B C   1 
ATOM   6824  O O   . THR A 1 893  ? 192.130 205.920 247.513 1.00 71.69  ? 876  THR B O   1 
ATOM   6825  C CB  . THR A 1 893  ? 194.183 204.064 248.249 1.00 71.69  ? 876  THR B CB  1 
ATOM   6826  O OG1 . THR A 1 893  ? 194.462 204.186 246.850 1.00 71.69  ? 876  THR B OG1 1 
ATOM   6827  C CG2 . THR A 1 893  ? 195.008 202.928 248.830 1.00 71.69  ? 876  THR B CG2 1 
ATOM   6828  N N   . SER A 1 894  ? 190.942 204.162 246.771 1.00 64.29  ? 877  SER B N   1 
ATOM   6829  C CA  . SER A 1 894  ? 190.120 204.977 245.894 1.00 64.29  ? 877  SER B CA  1 
ATOM   6830  C C   . SER A 1 894  ? 189.167 205.847 246.711 1.00 64.29  ? 877  SER B C   1 
ATOM   6831  O O   . SER A 1 894  ? 188.884 205.582 247.882 1.00 64.29  ? 877  SER B O   1 
ATOM   6832  C CB  . SER A 1 894  ? 189.333 204.097 244.926 1.00 64.29  ? 877  SER B CB  1 
ATOM   6833  O OG  . SER A 1 894  ? 188.141 203.630 245.525 1.00 64.29  ? 877  SER B OG  1 
ATOM   6834  N N   . ILE A 1 895  ? 188.670 206.902 246.075 1.00 60.48  ? 878  ILE B N   1 
ATOM   6835  C CA  . ILE A 1 895  ? 187.771 207.846 246.721 1.00 60.48  ? 878  ILE B CA  1 
ATOM   6836  C C   . ILE A 1 895  ? 186.312 207.558 246.385 1.00 60.48  ? 878  ILE B C   1 
ATOM   6837  O O   . ILE A 1 895  ? 185.436 207.726 247.232 1.00 60.48  ? 878  ILE B O   1 
ATOM   6838  C CB  . ILE A 1 895  ? 188.167 209.293 246.349 1.00 60.48  ? 878  ILE B CB  1 
ATOM   6839  C CG1 . ILE A 1 895  ? 187.213 210.307 246.966 1.00 60.48  ? 878  ILE B CG1 1 
ATOM   6840  C CG2 . ILE A 1 895  ? 188.207 209.482 244.861 1.00 60.48  ? 878  ILE B CG2 1 
ATOM   6841  C CD1 . ILE A 1 895  ? 187.637 211.731 246.744 1.00 60.48  ? 878  ILE B CD1 1 
ATOM   6842  N N   . LEU A 1 896  ? 186.029 207.112 245.164 1.00 59.25  ? 879  LEU B N   1 
ATOM   6843  C CA  . LEU A 1 896  ? 184.681 206.733 244.761 1.00 59.25  ? 879  LEU B CA  1 
ATOM   6844  C C   . LEU A 1 896  ? 184.748 205.399 244.033 1.00 59.25  ? 879  LEU B C   1 
ATOM   6845  O O   . LEU A 1 896  ? 185.513 205.253 243.075 1.00 59.25  ? 879  LEU B O   1 
ATOM   6846  C CB  . LEU A 1 896  ? 184.054 207.803 243.870 1.00 59.25  ? 879  LEU B CB  1 
ATOM   6847  C CG  . LEU A 1 896  ? 182.558 208.030 244.058 1.00 59.25  ? 879  LEU B CG  1 
ATOM   6848  C CD1 . LEU A 1 896  ? 182.284 208.537 245.457 1.00 59.25  ? 879  LEU B CD1 1 
ATOM   6849  C CD2 . LEU A 1 896  ? 182.043 209.012 243.029 1.00 59.25  ? 879  LEU B CD2 1 
ATOM   6850  N N   . ASN A 1 897  ? 183.951 204.435 244.480 1.00 61.33  ? 880  ASN B N   1 
ATOM   6851  C CA  . ASN A 1 897  ? 184.086 203.047 244.047 1.00 61.33  ? 880  ASN B CA  1 
ATOM   6852  C C   . ASN A 1 897  ? 182.725 202.438 243.723 1.00 61.33  ? 880  ASN B C   1 
ATOM   6853  O O   . ASN A 1 897  ? 182.375 201.360 244.203 1.00 61.33  ? 880  ASN B O   1 
ATOM   6854  C CB  . ASN A 1 897  ? 184.805 202.224 245.113 1.00 61.33  ? 880  ASN B CB  1 
ATOM   6855  C CG  . ASN A 1 897  ? 185.361 200.928 244.570 1.00 61.33  ? 880  ASN B CG  1 
ATOM   6856  O OD1 . ASN A 1 897  ? 185.122 200.572 243.419 1.00 61.33  ? 880  ASN B OD1 1 
ATOM   6857  N ND2 . ASN A 1 897  ? 186.101 200.209 245.402 1.00 61.33  ? 880  ASN B ND2 1 
ATOM   6858  N N   . LEU A 1 898  ? 181.930 203.136 242.911 1.00 62.41  ? 881  LEU B N   1 
ATOM   6859  C CA  . LEU A 1 898  ? 180.595 202.663 242.551 1.00 62.41  ? 881  LEU B CA  1 
ATOM   6860  C C   . LEU A 1 898  ? 180.607 201.248 241.988 1.00 62.41  ? 881  LEU B C   1 
ATOM   6861  O O   . LEU A 1 898  ? 181.168 201.008 240.916 1.00 62.41  ? 881  LEU B O   1 
ATOM   6862  C CB  . LEU A 1 898  ? 179.953 203.596 241.525 1.00 62.41  ? 881  LEU B CB  1 
ATOM   6863  C CG  . LEU A 1 898  ? 179.226 204.829 242.046 1.00 62.41  ? 881  LEU B CG  1 
ATOM   6864  C CD1 . LEU A 1 898  ? 180.207 205.951 242.274 1.00 62.41  ? 881  LEU B CD1 1 
ATOM   6865  C CD2 . LEU A 1 898  ? 178.152 205.243 241.066 1.00 62.41  ? 881  LEU B CD2 1 
ATOM   6866  N N   . ARG A 1 899  ? 179.988 200.306 242.699 1.00 66.53  ? 882  ARG B N   1 
ATOM   6867  C CA  . ARG A 1 899  ? 179.846 198.939 242.222 1.00 66.53  ? 882  ARG B CA  1 
ATOM   6868  C C   . ARG A 1 899  ? 178.470 198.418 242.609 1.00 66.53  ? 882  ARG B C   1 
ATOM   6869  O O   . ARG A 1 899  ? 177.861 198.879 243.576 1.00 66.53  ? 882  ARG B O   1 
ATOM   6870  C CB  . ARG A 1 899  ? 180.931 198.012 242.787 1.00 66.53  ? 882  ARG B CB  1 
ATOM   6871  C CG  . ARG A 1 899  ? 182.354 198.481 242.549 1.00 66.53  ? 882  ARG B CG  1 
ATOM   6872  C CD  . ARG A 1 899  ? 182.759 198.303 241.099 1.00 66.53  ? 882  ARG B CD  1 
ATOM   6873  N NE  . ARG A 1 899  ? 184.205 198.219 240.939 1.00 66.53  ? 882  ARG B NE  1 
ATOM   6874  C CZ  . ARG A 1 899  ? 184.929 197.148 241.231 1.00 66.53  ? 882  ARG B CZ  1 
ATOM   6875  N NH1 . ARG A 1 899  ? 184.373 196.047 241.708 1.00 66.53  ? 882  ARG B NH1 1 
ATOM   6876  N NH2 . ARG A 1 899  ? 186.243 197.181 241.037 1.00 66.53  ? 882  ARG B NH2 1 
ATOM   6877  N N   . TYR A 1 900  ? 177.985 197.444 241.845 1.00 73.79  ? 883  TYR B N   1 
ATOM   6878  C CA  . TYR A 1 900  ? 176.694 196.819 242.111 1.00 73.79  ? 883  TYR B CA  1 
ATOM   6879  C C   . TYR A 1 900  ? 176.918 195.584 242.974 1.00 73.79  ? 883  TYR B C   1 
ATOM   6880  O O   . TYR A 1 900  ? 177.539 194.613 242.531 1.00 73.79  ? 883  TYR B O   1 
ATOM   6881  C CB  . TYR A 1 900  ? 175.988 196.453 240.810 1.00 73.79  ? 883  TYR B CB  1 
ATOM   6882  C CG  . TYR A 1 900  ? 174.512 196.180 240.974 1.00 73.79  ? 883  TYR B CG  1 
ATOM   6883  C CD1 . TYR A 1 900  ? 173.592 197.218 240.990 1.00 73.79  ? 883  TYR B CD1 1 
ATOM   6884  C CD2 . TYR A 1 900  ? 174.038 194.886 241.118 1.00 73.79  ? 883  TYR B CD2 1 
ATOM   6885  C CE1 . TYR A 1 900  ? 172.241 196.973 241.138 1.00 73.79  ? 883  TYR B CE1 1 
ATOM   6886  C CE2 . TYR A 1 900  ? 172.690 194.632 241.265 1.00 73.79  ? 883  TYR B CE2 1 
ATOM   6887  C CZ  . TYR A 1 900  ? 171.797 195.679 241.275 1.00 73.79  ? 883  TYR B CZ  1 
ATOM   6888  O OH  . TYR A 1 900  ? 170.453 195.432 241.423 1.00 73.79  ? 883  TYR B OH  1 
ATOM   6889  N N   . GLU A 1 901  ? 176.399 195.642 244.196 1.00 83.70  ? 884  GLU B N   1 
ATOM   6890  C CA  . GLU A 1 901  ? 176.590 194.497 245.117 1.00 83.70  ? 884  GLU B CA  1 
ATOM   6891  C C   . GLU A 1 901  ? 175.316 194.229 245.916 1.00 83.70  ? 884  GLU B C   1 
ATOM   6892  O O   . GLU A 1 901  ? 174.782 195.177 246.515 1.00 83.70  ? 884  GLU B O   1 
ATOM   6893  C CB  . GLU A 1 901  ? 177.793 194.717 246.032 1.00 83.70  ? 884  GLU B CB  1 
ATOM   6894  C CG  . GLU A 1 901  ? 178.568 193.437 246.287 1.00 83.70  ? 884  GLU B CG  1 
ATOM   6895  C CD  . GLU A 1 901  ? 180.081 193.572 246.270 1.00 83.70  ? 884  GLU B CD  1 
ATOM   6896  O OE1 . GLU A 1 901  ? 180.581 194.511 245.622 1.00 83.70  ? 884  GLU B OE1 1 
ATOM   6897  O OE2 . GLU A 1 901  ? 180.754 192.737 246.905 1.00 83.70  ? 884  GLU B OE2 1 
ATOM   6898  N N   . SER A 1 902  ? 174.839 192.994 245.867 1.00 85.62  ? 885  SER B N   1 
ATOM   6899  C CA  . SER A 1 902  ? 173.671 192.550 246.627 1.00 85.62  ? 885  SER B CA  1 
ATOM   6900  C C   . SER A 1 902  ? 172.421 193.348 246.258 1.00 85.62  ? 885  SER B C   1 
ATOM   6901  O O   . SER A 1 902  ? 171.730 193.904 247.115 1.00 85.62  ? 885  SER B O   1 
ATOM   6902  C CB  . SER A 1 902  ? 173.944 192.626 248.129 1.00 85.62  ? 885  SER B CB  1 
ATOM   6903  O OG  . SER A 1 902  ? 175.146 191.952 248.458 1.00 85.62  ? 885  SER B OG  1 
ATOM   6904  N N   . ASN A 1 903  ? 172.132 193.395 244.957 1.00 84.91  ? 886  ASN B N   1 
ATOM   6905  C CA  . ASN A 1 903  ? 170.958 194.092 244.429 1.00 84.91  ? 886  ASN B CA  1 
ATOM   6906  C C   . ASN A 1 903  ? 170.931 195.551 244.882 1.00 84.91  ? 886  ASN B C   1 
ATOM   6907  O O   . ASN A 1 903  ? 169.879 196.100 245.216 1.00 84.91  ? 886  ASN B O   1 
ATOM   6908  C CB  . ASN A 1 903  ? 169.665 193.370 244.817 1.00 84.91  ? 886  ASN B CB  1 
ATOM   6909  C CG  . ASN A 1 903  ? 168.455 193.883 244.052 1.00 84.91  ? 886  ASN B CG  1 
ATOM   6910  O OD1 . ASN A 1 903  ? 168.258 193.550 242.884 1.00 84.91  ? 886  ASN B OD1 1 
ATOM   6911  N ND2 . ASN A 1 903  ? 167.639 194.698 244.711 1.00 84.91  ? 886  ASN B ND2 1 
ATOM   6912  N N   . HIS A 1 904  ? 172.101 196.185 244.898 1.00 80.96  ? 887  HIS B N   1 
ATOM   6913  C CA  . HIS A 1 904  ? 172.201 197.593 245.257 1.00 80.96  ? 887  HIS B CA  1 
ATOM   6914  C C   . HIS A 1 904  ? 173.450 198.180 244.622 1.00 80.96  ? 887  HIS B C   1 
ATOM   6915  O O   . HIS A 1 904  ? 174.520 197.567 244.676 1.00 80.96  ? 887  HIS B O   1 
ATOM   6916  C CB  . HIS A 1 904  ? 172.244 197.778 246.777 1.00 80.96  ? 887  HIS B CB  1 
ATOM   6917  C CG  . HIS A 1 904  ? 170.903 197.702 247.434 1.00 80.96  ? 887  HIS B CG  1 
ATOM   6918  N ND1 . HIS A 1 904  ? 169.797 198.360 246.942 1.00 80.96  ? 887  HIS B ND1 1 
ATOM   6919  C CD2 . HIS A 1 904  ? 170.488 197.046 248.543 1.00 80.96  ? 887  HIS B CD2 1 
ATOM   6920  C CE1 . HIS A 1 904  ? 168.758 198.114 247.720 1.00 80.96  ? 887  HIS B CE1 1 
ATOM   6921  N NE2 . HIS A 1 904  ? 169.151 197.319 248.699 1.00 80.96  ? 887  HIS B NE2 1 
ATOM   6922  N N   . LEU A 1 905  ? 173.310 199.360 244.025 1.00 71.73  ? 888  LEU B N   1 
ATOM   6923  C CA  . LEU A 1 905  ? 174.447 200.120 243.519 1.00 71.73  ? 888  LEU B CA  1 
ATOM   6924  C C   . LEU A 1 905  ? 174.985 200.965 244.665 1.00 71.73  ? 888  LEU B C   1 
ATOM   6925  O O   . LEU A 1 905  ? 174.331 201.917 245.101 1.00 71.73  ? 888  LEU B O   1 
ATOM   6926  C CB  . LEU A 1 905  ? 174.036 200.993 242.338 1.00 71.73  ? 888  LEU B CB  1 
ATOM   6927  C CG  . LEU A 1 905  ? 175.182 201.583 241.520 1.00 71.73  ? 888  LEU B CG  1 
ATOM   6928  C CD1 . LEU A 1 905  ? 176.121 200.486 241.067 1.00 71.73  ? 888  LEU B CD1 1 
ATOM   6929  C CD2 . LEU A 1 905  ? 174.650 202.359 240.334 1.00 71.73  ? 888  LEU B CD2 1 
ATOM   6930  N N   . ILE A 1 906  ? 176.175 200.622 245.158 1.00 71.62  ? 889  ILE B N   1 
ATOM   6931  C CA  . ILE A 1 906  ? 176.711 201.234 246.362 1.00 71.62  ? 889  ILE B CA  1 
ATOM   6932  C C   . ILE A 1 906  ? 178.145 201.681 246.125 1.00 71.62  ? 889  ILE B C   1 
ATOM   6933  O O   . ILE A 1 906  ? 178.855 201.166 245.258 1.00 71.62  ? 889  ILE B O   1 
ATOM   6934  C CB  . ILE A 1 906  ? 176.647 200.278 247.568 1.00 71.62  ? 889  ILE B CB  1 
ATOM   6935  C CG1 . ILE A 1 906  ? 177.045 198.866 247.143 1.00 71.62  ? 889  ILE B CG1 1 
ATOM   6936  C CG2 . ILE A 1 906  ? 175.257 200.281 248.161 1.00 71.62  ? 889  ILE B CG2 1 
ATOM   6937  C CD1 . ILE A 1 906  ? 177.553 198.012 248.274 1.00 71.62  ? 889  ILE B CD1 1 
ATOM   6938  N N   . ASP A 1 907  ? 178.563 202.654 246.928 1.00 67.48  ? 890  ASP B N   1 
ATOM   6939  C CA  . ASP A 1 907  ? 179.924 203.179 246.901 1.00 67.48  ? 890  ASP B CA  1 
ATOM   6940  C C   . ASP A 1 907  ? 180.732 202.408 247.933 1.00 67.48  ? 890  ASP B C   1 
ATOM   6941  O O   . ASP A 1 907  ? 180.638 202.670 249.133 1.00 67.48  ? 890  ASP B O   1 
ATOM   6942  C CB  . ASP A 1 907  ? 179.922 204.676 247.188 1.00 67.48  ? 890  ASP B CB  1 
ATOM   6943  C CG  . ASP A 1 907  ? 181.315 205.247 247.333 1.00 67.48  ? 890  ASP B CG  1 
ATOM   6944  O OD1 . ASP A 1 907  ? 182.285 204.599 246.894 1.00 67.48  ? 890  ASP B OD1 1 
ATOM   6945  O OD2 . ASP A 1 907  ? 181.441 206.353 247.896 1.00 67.48  ? 890  ASP B OD2 1 
ATOM   6946  N N   . LEU A 1 908  ? 181.538 201.455 247.465 1.00 65.94  ? 891  LEU B N   1 
ATOM   6947  C CA  . LEU A 1 908  ? 182.309 200.620 248.376 1.00 65.94  ? 891  LEU B CA  1 
ATOM   6948  C C   . LEU A 1 908  ? 183.369 201.407 249.133 1.00 65.94  ? 891  LEU B C   1 
ATOM   6949  O O   . LEU A 1 908  ? 183.859 200.929 250.161 1.00 65.94  ? 891  LEU B O   1 
ATOM   6950  C CB  . LEU A 1 908  ? 182.960 199.472 247.609 1.00 65.94  ? 891  LEU B CB  1 
ATOM   6951  C CG  . LEU A 1 908  ? 182.015 198.344 247.202 1.00 65.94  ? 891  LEU B CG  1 
ATOM   6952  C CD1 . LEU A 1 908  ? 182.785 197.218 246.544 1.00 65.94  ? 891  LEU B CD1 1 
ATOM   6953  C CD2 . LEU A 1 908  ? 181.256 197.836 248.407 1.00 65.94  ? 891  LEU B CD2 1 
ATOM   6954  N N   . SER A 1 909  ? 183.739 202.593 248.655 1.00 65.46  ? 892  SER B N   1 
ATOM   6955  C CA  . SER A 1 909  ? 184.706 203.417 249.366 1.00 65.46  ? 892  SER B CA  1 
ATOM   6956  C C   . SER A 1 909  ? 184.071 204.249 250.471 1.00 65.46  ? 892  SER B C   1 
ATOM   6957  O O   . SER A 1 909  ? 184.800 204.865 251.253 1.00 65.46  ? 892  SER B O   1 
ATOM   6958  C CB  . SER A 1 909  ? 185.436 204.334 248.387 1.00 65.46  ? 892  SER B CB  1 
ATOM   6959  O OG  . SER A 1 909  ? 185.801 205.548 249.012 1.00 65.46  ? 892  SER B OG  1 
ATOM   6960  N N   . ARG A 1 910  ? 182.740 204.287 250.539 1.00 67.75  ? 893  ARG B N   1 
ATOM   6961  C CA  . ARG A 1 910  ? 181.999 204.892 251.649 1.00 67.75  ? 893  ARG B CA  1 
ATOM   6962  C C   . ARG A 1 910  ? 182.239 206.395 251.754 1.00 67.75  ? 893  ARG B C   1 
ATOM   6963  O O   . ARG A 1 910  ? 182.185 206.965 252.845 1.00 67.75  ? 893  ARG B O   1 
ATOM   6964  C CB  . ARG A 1 910  ? 182.321 204.207 252.982 1.00 67.75  ? 893  ARG B CB  1 
ATOM   6965  C CG  . ARG A 1 910  ? 181.452 202.990 253.291 1.00 67.75  ? 893  ARG B CG  1 
ATOM   6966  C CD  . ARG A 1 910  ? 181.511 201.977 252.165 1.00 67.75  ? 893  ARG B CD  1 
ATOM   6967  N NE  . ARG A 1 910  ? 180.460 200.971 252.232 1.00 67.75  ? 893  ARG B NE  1 
ATOM   6968  C CZ  . ARG A 1 910  ? 180.667 199.693 252.510 1.00 67.75  ? 893  ARG B CZ  1 
ATOM   6969  N NH1 . ARG A 1 910  ? 181.875 199.233 252.790 1.00 67.75  ? 893  ARG B NH1 1 
ATOM   6970  N NH2 . ARG A 1 910  ? 179.638 198.852 252.494 1.00 67.75  ? 893  ARG B NH2 1 
ATOM   6971  N N   . TYR A 1 911  ? 182.502 207.050 250.625 1.00 63.92  ? 894  TYR B N   1 
ATOM   6972  C CA  . TYR A 1 911  ? 182.575 208.503 250.578 1.00 63.92  ? 894  TYR B CA  1 
ATOM   6973  C C   . TYR A 1 911  ? 181.283 209.148 250.099 1.00 63.92  ? 894  TYR B C   1 
ATOM   6974  O O   . TYR A 1 911  ? 181.127 210.364 250.247 1.00 63.92  ? 894  TYR B O   1 
ATOM   6975  C CB  . TYR A 1 911  ? 183.714 208.960 249.661 1.00 63.92  ? 894  TYR B CB  1 
ATOM   6976  C CG  . TYR A 1 911  ? 185.100 208.924 250.264 1.00 63.92  ? 894  TYR B CG  1 
ATOM   6977  C CD1 . TYR A 1 911  ? 185.540 207.834 250.998 1.00 63.92  ? 894  TYR B CD1 1 
ATOM   6978  C CD2 . TYR A 1 911  ? 185.976 209.980 250.080 1.00 63.92  ? 894  TYR B CD2 1 
ATOM   6979  C CE1 . TYR A 1 911  ? 186.813 207.803 251.534 1.00 63.92  ? 894  TYR B CE1 1 
ATOM   6980  C CE2 . TYR A 1 911  ? 187.245 209.959 250.610 1.00 63.92  ? 894  TYR B CE2 1 
ATOM   6981  C CZ  . TYR A 1 911  ? 187.660 208.870 251.336 1.00 63.92  ? 894  TYR B CZ  1 
ATOM   6982  O OH  . TYR A 1 911  ? 188.929 208.855 251.862 1.00 63.92  ? 894  TYR B OH  1 
ATOM   6983  N N   . ALA A 1 912  ? 180.360 208.375 249.539 1.00 65.29  ? 895  ALA B N   1 
ATOM   6984  C CA  . ALA A 1 912  ? 179.160 208.915 248.919 1.00 65.29  ? 895  ALA B CA  1 
ATOM   6985  C C   . ALA A 1 912  ? 177.990 208.869 249.889 1.00 65.29  ? 895  ALA B C   1 
ATOM   6986  O O   . ALA A 1 912  ? 177.774 207.866 250.574 1.00 65.29  ? 895  ALA B O   1 
ATOM   6987  C CB  . ALA A 1 912  ? 178.803 208.144 247.648 1.00 65.29  ? 895  ALA B CB  1 
ATOM   6988  N N   . SER A 1 913  ? 177.234 209.964 249.935 1.00 66.82  ? 896  SER B N   1 
ATOM   6989  C CA  . SER A 1 913  ? 176.076 210.066 250.811 1.00 66.82  ? 896  SER B CA  1 
ATOM   6990  C C   . SER A 1 913  ? 174.822 209.484 250.167 1.00 66.82  ? 896  SER B C   1 
ATOM   6991  O O   . SER A 1 913  ? 174.089 208.728 250.810 1.00 66.82  ? 896  SER B O   1 
ATOM   6992  C CB  . SER A 1 913  ? 175.841 211.528 251.198 1.00 66.82  ? 896  SER B CB  1 
ATOM   6993  O OG  . SER A 1 913  ? 174.523 211.726 251.675 1.00 66.82  ? 896  SER B OG  1 
ATOM   6994  N N   . LYS A 1 914  ? 174.567 209.817 248.903 1.00 64.73  ? 897  LYS B N   1 
ATOM   6995  C CA  . LYS A 1 914  ? 173.347 209.380 248.229 1.00 64.73  ? 897  LYS B CA  1 
ATOM   6996  C C   . LYS A 1 914  ? 173.670 208.911 246.821 1.00 64.73  ? 897  LYS B C   1 
ATOM   6997  O O   . LYS A 1 914  ? 174.178 209.689 246.011 1.00 64.73  ? 897  LYS B O   1 
ATOM   6998  C CB  . LYS A 1 914  ? 172.311 210.506 248.176 1.00 64.73  ? 897  LYS B CB  1 
ATOM   6999  C CG  . LYS A 1 914  ? 171.678 210.848 249.509 1.00 64.73  ? 897  LYS B CG  1 
ATOM   7000  C CD  . LYS A 1 914  ? 170.314 211.496 249.317 1.00 64.73  ? 897  LYS B CD  1 
ATOM   7001  C CE  . LYS A 1 914  ? 169.456 210.718 248.330 1.00 64.73  ? 897  LYS B CE  1 
ATOM   7002  N NZ  . LYS A 1 914  ? 169.260 209.303 248.752 1.00 64.73  ? 897  LYS B NZ  1 
ATOM   7003  N N   . ILE A 1 915  ? 173.366 207.655 246.522 1.00 61.33  ? 898  ILE B N   1 
ATOM   7004  C CA  . ILE A 1 915  ? 173.463 207.138 245.160 1.00 61.33  ? 898  ILE B CA  1 
ATOM   7005  C C   . ILE A 1 915  ? 172.032 207.103 244.634 1.00 61.33  ? 898  ILE B C   1 
ATOM   7006  O O   . ILE A 1 915  ? 171.263 206.175 244.894 1.00 61.33  ? 898  ILE B O   1 
ATOM   7007  C CB  . ILE A 1 915  ? 174.155 205.778 245.107 1.00 61.33  ? 898  ILE B CB  1 
ATOM   7008  C CG1 . ILE A 1 915  ? 175.667 205.976 245.134 1.00 61.33  ? 898  ILE B CG1 1 
ATOM   7009  C CG2 . ILE A 1 915  ? 173.825 205.053 243.818 1.00 61.33  ? 898  ILE B CG2 1 
ATOM   7010  C CD1 . ILE A 1 915  ? 176.436 204.732 245.458 1.00 61.33  ? 898  ILE B CD1 1 
ATOM   7011  N N   . ASN A 1 916  ? 171.652 208.163 243.929 1.00 62.08  ? 899  ASN B N   1 
ATOM   7012  C CA  . ASN A 1 916  ? 170.319 208.272 243.359 1.00 62.08  ? 899  ASN B CA  1 
ATOM   7013  C C   . ASN A 1 916  ? 170.296 207.598 241.994 1.00 62.08  ? 899  ASN B C   1 
ATOM   7014  O O   . ASN A 1 916  ? 171.193 207.814 241.177 1.00 62.08  ? 899  ASN B O   1 
ATOM   7015  C CB  . ASN A 1 916  ? 169.929 209.742 243.235 1.00 62.08  ? 899  ASN B CB  1 
ATOM   7016  C CG  . ASN A 1 916  ? 168.578 210.037 243.832 1.00 62.08  ? 899  ASN B CG  1 
ATOM   7017  O OD1 . ASN A 1 916  ? 168.332 209.751 245.002 1.00 62.08  ? 899  ASN B OD1 1 
ATOM   7018  N ND2 . ASN A 1 916  ? 167.692 210.618 243.035 1.00 62.08  ? 899  ASN B ND2 1 
ATOM   7019  N N   . ILE A 1 917  ? 169.276 206.786 241.738 1.00 58.63  ? 900  ILE B N   1 
ATOM   7020  C CA  . ILE A 1 917  ? 169.173 206.035 240.493 1.00 58.63  ? 900  ILE B CA  1 
ATOM   7021  C C   . ILE A 1 917  ? 167.863 206.396 239.810 1.00 58.63  ? 900  ILE B C   1 
ATOM   7022  O O   . ILE A 1 917  ? 166.804 206.388 240.446 1.00 58.63  ? 900  ILE B O   1 
ATOM   7023  C CB  . ILE A 1 917  ? 169.266 204.519 240.733 1.00 58.63  ? 900  ILE B CB  1 
ATOM   7024  C CG1 . ILE A 1 917  ? 170.623 204.161 241.334 1.00 58.63  ? 900  ILE B CG1 1 
ATOM   7025  C CG2 . ILE A 1 917  ? 169.046 203.759 239.440 1.00 58.63  ? 900  ILE B CG2 1 
ATOM   7026  C CD1 . ILE A 1 917  ? 170.533 203.266 242.545 1.00 58.63  ? 900  ILE B CD1 1 
ATOM   7027  N N   . GLY A 1 918  ? 167.938 206.714 238.522 1.00 57.44  ? 901  GLY B N   1 
ATOM   7028  C CA  . GLY A 1 918  ? 166.746 206.992 237.752 1.00 57.44  ? 901  GLY B CA  1 
ATOM   7029  C C   . GLY A 1 918  ? 165.954 205.734 237.453 1.00 57.44  ? 901  GLY B C   1 
ATOM   7030  O O   . GLY A 1 918  ? 166.415 204.606 237.624 1.00 57.44  ? 901  GLY B O   1 
ATOM   7031  N N   . SER A 1 919  ? 164.726 205.941 236.990 1.00 58.87  ? 902  SER B N   1 
ATOM   7032  C CA  . SER A 1 919  ? 163.801 204.846 236.734 1.00 58.87  ? 902  SER B CA  1 
ATOM   7033  C C   . SER A 1 919  ? 163.969 204.222 235.355 1.00 58.87  ? 902  SER B C   1 
ATOM   7034  O O   . SER A 1 919  ? 163.296 203.230 235.057 1.00 58.87  ? 902  SER B O   1 
ATOM   7035  C CB  . SER A 1 919  ? 162.358 205.331 236.905 1.00 58.87  ? 902  SER B CB  1 
ATOM   7036  O OG  . SER A 1 919  ? 162.073 206.402 236.024 1.00 58.87  ? 902  SER B OG  1 
ATOM   7037  N N   . LYS A 1 920  ? 164.839 204.766 234.512 1.00 56.98  ? 903  LYS B N   1 
ATOM   7038  C CA  . LYS A 1 920  ? 165.038 204.273 233.155 1.00 56.98  ? 903  LYS B CA  1 
ATOM   7039  C C   . LYS A 1 920  ? 166.497 203.906 232.914 1.00 56.98  ? 903  LYS B C   1 
ATOM   7040  O O   . LYS A 1 920  ? 167.036 204.104 231.825 1.00 56.98  ? 903  LYS B O   1 
ATOM   7041  C CB  . LYS A 1 920  ? 164.567 205.302 232.132 1.00 56.98  ? 903  LYS B CB  1 
ATOM   7042  C CG  . LYS A 1 920  ? 163.130 205.749 232.327 1.00 56.98  ? 903  LYS B CG  1 
ATOM   7043  C CD  . LYS A 1 920  ? 162.197 205.074 231.342 1.00 56.98  ? 903  LYS B CD  1 
ATOM   7044  C CE  . LYS A 1 920  ? 160.834 205.741 231.339 1.00 56.98  ? 903  LYS B CE  1 
ATOM   7045  N NZ  . LYS A 1 920  ? 160.249 205.798 229.972 1.00 56.98  ? 903  LYS B NZ  1 
ATOM   7046  N N   . VAL A 1 921  ? 167.151 203.360 233.933 1.00 54.23  ? 904  VAL B N   1 
ATOM   7047  C CA  . VAL A 1 921  ? 168.546 202.940 233.861 1.00 54.23  ? 904  VAL B CA  1 
ATOM   7048  C C   . VAL A 1 921  ? 168.569 201.422 233.921 1.00 54.23  ? 904  VAL B C   1 
ATOM   7049  O O   . VAL A 1 921  ? 168.053 200.830 234.876 1.00 54.23  ? 904  VAL B O   1 
ATOM   7050  C CB  . VAL A 1 921  ? 169.374 203.548 235.000 1.00 54.23  ? 904  VAL B CB  1 
ATOM   7051  C CG1 . VAL A 1 921  ? 170.703 202.845 235.119 1.00 54.23  ? 904  VAL B CG1 1 
ATOM   7052  C CG2 . VAL A 1 921  ? 169.568 205.036 234.774 1.00 54.23  ? 904  VAL B CG2 1 
ATOM   7053  N N   . ASN A 1 922  ? 169.160 200.785 232.915 1.00 58.14  ? 905  ASN B N   1 
ATOM   7054  C CA  . ASN A 1 922  ? 169.073 199.337 232.806 1.00 58.14  ? 905  ASN B CA  1 
ATOM   7055  C C   . ASN A 1 922  ? 170.325 198.674 233.364 1.00 58.14  ? 905  ASN B C   1 
ATOM   7056  O O   . ASN A 1 922  ? 171.418 199.238 233.326 1.00 58.14  ? 905  ASN B O   1 
ATOM   7057  C CB  . ASN A 1 922  ? 168.863 198.912 231.353 1.00 58.14  ? 905  ASN B CB  1 
ATOM   7058  C CG  . ASN A 1 922  ? 168.395 197.476 231.229 1.00 58.14  ? 905  ASN B CG  1 
ATOM   7059  O OD1 . ASN A 1 922  ? 167.475 197.051 231.924 1.00 58.14  ? 905  ASN B OD1 1 
ATOM   7060  N ND2 . ASN A 1 922  ? 169.023 196.722 230.334 1.00 58.14  ? 905  ASN B ND2 1 
ATOM   7061  N N   . PHE A 1 923  ? 170.151 197.469 233.896 1.00 60.80  ? 906  PHE B N   1 
ATOM   7062  C CA  . PHE A 1 923  ? 171.255 196.648 234.372 1.00 60.80  ? 906  PHE B CA  1 
ATOM   7063  C C   . PHE A 1 923  ? 171.214 195.315 233.642 1.00 60.80  ? 906  PHE B C   1 
ATOM   7064  O O   . PHE A 1 923  ? 170.145 194.710 233.513 1.00 60.80  ? 906  PHE B O   1 
ATOM   7065  C CB  . PHE A 1 923  ? 171.178 196.426 235.884 1.00 60.80  ? 906  PHE B CB  1 
ATOM   7066  C CG  . PHE A 1 923  ? 171.395 197.671 236.695 1.00 60.80  ? 906  PHE B CG  1 
ATOM   7067  C CD1 . PHE A 1 923  ? 170.368 198.574 236.893 1.00 60.80  ? 906  PHE B CD1 1 
ATOM   7068  C CD2 . PHE A 1 923  ? 172.626 197.935 237.264 1.00 60.80  ? 906  PHE B CD2 1 
ATOM   7069  C CE1 . PHE A 1 923  ? 170.566 199.716 237.641 1.00 60.80  ? 906  PHE B CE1 1 
ATOM   7070  C CE2 . PHE A 1 923  ? 172.829 199.075 238.011 1.00 60.80  ? 906  PHE B CE2 1 
ATOM   7071  C CZ  . PHE A 1 923  ? 171.798 199.966 238.199 1.00 60.80  ? 906  PHE B CZ  1 
ATOM   7072  N N   . ASP A 1 924  ? 172.364 194.862 233.168 1.00 69.30  ? 907  ASP B N   1 
ATOM   7073  C CA  . ASP A 1 924  ? 172.414 193.616 232.413 1.00 69.30  ? 907  ASP B CA  1 
ATOM   7074  C C   . ASP A 1 924  ? 172.116 192.441 233.334 1.00 69.30  ? 907  ASP B C   1 
ATOM   7075  O O   . ASP A 1 924  ? 172.805 192.271 234.347 1.00 69.30  ? 907  ASP B O   1 
ATOM   7076  C CB  . ASP A 1 924  ? 173.776 193.442 231.759 1.00 69.30  ? 907  ASP B CB  1 
ATOM   7077  C CG  . ASP A 1 924  ? 174.040 192.011 231.341 1.00 69.30  ? 907  ASP B CG  1 
ATOM   7078  O OD1 . ASP A 1 924  ? 173.229 191.457 230.570 1.00 69.30  ? 907  ASP B OD1 1 
ATOM   7079  O OD2 . ASP A 1 924  ? 175.054 191.436 231.786 1.00 69.30  ? 907  ASP B OD2 1 
ATOM   7080  N N   . PRO A 1 925  ? 171.110 191.617 233.035 1.00 70.56  ? 908  PRO B N   1 
ATOM   7081  C CA  . PRO A 1 925  ? 170.771 190.512 233.946 1.00 70.56  ? 908  PRO B CA  1 
ATOM   7082  C C   . PRO A 1 925  ? 171.894 189.509 234.154 1.00 70.56  ? 908  PRO B C   1 
ATOM   7083  O O   . PRO A 1 925  ? 172.023 188.967 235.258 1.00 70.56  ? 908  PRO B O   1 
ATOM   7084  C CB  . PRO A 1 925  ? 169.555 189.863 233.270 1.00 70.56  ? 908  PRO B CB  1 
ATOM   7085  C CG  . PRO A 1 925  ? 169.626 190.302 231.841 1.00 70.56  ? 908  PRO B CG  1 
ATOM   7086  C CD  . PRO A 1 925  ? 170.209 191.675 231.873 1.00 70.56  ? 908  PRO B CD  1 
ATOM   7087  N N   . ILE A 1 926  ? 172.705 189.237 233.132 1.00 71.54  ? 909  ILE B N   1 
ATOM   7088  C CA  . ILE A 1 926  ? 173.769 188.246 233.277 1.00 71.54  ? 909  ILE B CA  1 
ATOM   7089  C C   . ILE A 1 926  ? 174.864 188.772 234.197 1.00 71.54  ? 909  ILE B C   1 
ATOM   7090  O O   . ILE A 1 926  ? 175.346 188.062 235.087 1.00 71.54  ? 909  ILE B O   1 
ATOM   7091  C CB  . ILE A 1 926  ? 174.325 187.850 231.897 1.00 71.54  ? 909  ILE B CB  1 
ATOM   7092  C CG1 . ILE A 1 926  ? 173.539 186.667 231.328 1.00 71.54  ? 909  ILE B CG1 1 
ATOM   7093  C CG2 . ILE A 1 926  ? 175.802 187.501 231.988 1.00 71.54  ? 909  ILE B CG2 1 
ATOM   7094  C CD1 . ILE A 1 926  ? 173.820 185.351 232.023 1.00 71.54  ? 909  ILE B CD1 1 
ATOM   7095  N N   . ASP A 1 927  ? 175.269 190.025 234.000 1.00 71.30  ? 910  ASP B N   1 
ATOM   7096  C CA  . ASP A 1 927  ? 176.286 190.671 234.823 1.00 71.30  ? 910  ASP B CA  1 
ATOM   7097  C C   . ASP A 1 927  ? 175.723 192.041 235.170 1.00 71.30  ? 910  ASP B C   1 
ATOM   7098  O O   . ASP A 1 927  ? 175.686 192.933 234.317 1.00 71.30  ? 910  ASP B O   1 
ATOM   7099  C CB  . ASP A 1 927  ? 177.622 190.763 234.072 1.00 71.30  ? 910  ASP B CB  1 
ATOM   7100  C CG  . ASP A 1 927  ? 178.620 191.751 234.692 1.00 71.30  ? 910  ASP B CG  1 
ATOM   7101  O OD1 . ASP A 1 927  ? 178.280 192.548 235.589 1.00 71.30  ? 910  ASP B OD1 1 
ATOM   7102  O OD2 . ASP A 1 927  ? 179.790 191.726 234.255 1.00 71.30  ? 910  ASP B OD2 1 
ATOM   7103  N N   . LYS A 1 928  ? 175.292 192.211 236.418 1.00 68.06  ? 911  LYS B N   1 
ATOM   7104  C CA  . LYS A 1 928  ? 174.585 193.425 236.803 1.00 68.06  ? 911  LYS B CA  1 
ATOM   7105  C C   . LYS A 1 928  ? 175.493 194.639 236.929 1.00 68.06  ? 911  LYS B C   1 
ATOM   7106  O O   . LYS A 1 928  ? 174.981 195.748 237.106 1.00 68.06  ? 911  LYS B O   1 
ATOM   7107  C CB  . LYS A 1 928  ? 173.838 193.197 238.114 1.00 68.06  ? 911  LYS B CB  1 
ATOM   7108  C CG  . LYS A 1 928  ? 172.680 192.221 238.000 1.00 68.06  ? 911  LYS B CG  1 
ATOM   7109  C CD  . LYS A 1 928  ? 171.397 192.827 238.539 1.00 68.06  ? 911  LYS B CD  1 
ATOM   7110  C CE  . LYS A 1 928  ? 170.249 191.839 238.469 1.00 68.06  ? 911  LYS B CE  1 
ATOM   7111  N NZ  . LYS A 1 928  ? 170.017 191.365 237.080 1.00 68.06  ? 911  LYS B NZ  1 
ATOM   7112  N N   . ASN A 1 929  ? 176.814 194.467 236.856 1.00 63.33  ? 912  ASN B N   1 
ATOM   7113  C CA  . ASN A 1 929  ? 177.706 195.620 236.942 1.00 63.33  ? 912  ASN B CA  1 
ATOM   7114  C C   . ASN A 1 929  ? 177.549 196.540 235.738 1.00 63.33  ? 912  ASN B C   1 
ATOM   7115  O O   . ASN A 1 929  ? 177.595 197.767 235.881 1.00 63.33  ? 912  ASN B O   1 
ATOM   7116  C CB  . ASN A 1 929  ? 179.157 195.162 237.076 1.00 63.33  ? 912  ASN B CB  1 
ATOM   7117  C CG  . ASN A 1 929  ? 179.624 195.130 238.510 1.00 63.33  ? 912  ASN B CG  1 
ATOM   7118  O OD1 . ASN A 1 929  ? 179.680 196.160 239.176 1.00 63.33  ? 912  ASN B OD1 1 
ATOM   7119  N ND2 . ASN A 1 929  ? 179.966 193.944 238.996 1.00 63.33  ? 912  ASN B ND2 1 
ATOM   7120  N N   . GLN A 1 930  ? 177.368 195.971 234.549 1.00 61.11  ? 913  GLN B N   1 
ATOM   7121  C CA  . GLN A 1 930  ? 177.264 196.774 233.337 1.00 61.11  ? 913  GLN B CA  1 
ATOM   7122  C C   . GLN A 1 930  ? 175.967 197.570 233.350 1.00 61.11  ? 913  GLN B C   1 
ATOM   7123  O O   . GLN A 1 930  ? 174.875 196.995 233.360 1.00 61.11  ? 913  GLN B O   1 
ATOM   7124  C CB  . GLN A 1 930  ? 177.334 195.878 232.106 1.00 61.11  ? 913  GLN B CB  1 
ATOM   7125  C CG  . GLN A 1 930  ? 178.178 194.637 232.305 1.00 61.11  ? 913  GLN B CG  1 
ATOM   7126  C CD  . GLN A 1 930  ? 178.362 193.851 231.028 1.00 61.11  ? 913  GLN B CD  1 
ATOM   7127  O OE1 . GLN A 1 930  ? 179.037 192.822 231.011 1.00 61.11  ? 913  GLN B OE1 1 
ATOM   7128  N NE2 . GLN A 1 930  ? 177.765 194.333 229.946 1.00 61.11  ? 913  GLN B NE2 1 
ATOM   7129  N N   . ILE A 1 931  ? 176.088 198.893 233.333 1.00 51.60  ? 914  ILE B N   1 
ATOM   7130  C CA  . ILE A 1 931  ? 174.957 199.803 233.442 1.00 51.60  ? 914  ILE B CA  1 
ATOM   7131  C C   . ILE A 1 931  ? 174.690 200.397 232.070 1.00 51.60  ? 914  ILE B C   1 
ATOM   7132  O O   . ILE A 1 931  ? 175.616 200.862 231.401 1.00 51.60  ? 914  ILE B O   1 
ATOM   7133  C CB  . ILE A 1 931  ? 175.238 200.908 234.474 1.00 51.60  ? 914  ILE B CB  1 
ATOM   7134  C CG1 . ILE A 1 931  ? 175.548 200.292 235.837 1.00 51.60  ? 914  ILE B CG1 1 
ATOM   7135  C CG2 . ILE A 1 931  ? 174.075 201.865 234.567 1.00 51.60  ? 914  ILE B CG2 1 
ATOM   7136  C CD1 . ILE A 1 931  ? 176.328 201.206 236.749 1.00 51.60  ? 914  ILE B CD1 1 
ATOM   7137  N N   . GLN A 1 932  ? 173.433 200.381 231.645 1.00 51.79  ? 915  GLN B N   1 
ATOM   7138  C CA  . GLN A 1 932  ? 173.035 200.916 230.350 1.00 51.79  ? 915  GLN B CA  1 
ATOM   7139  C C   . GLN A 1 932  ? 172.241 202.196 230.566 1.00 51.79  ? 915  GLN B C   1 
ATOM   7140  O O   . GLN A 1 932  ? 171.217 202.187 231.263 1.00 51.79  ? 915  GLN B O   1 
ATOM   7141  C CB  . GLN A 1 932  ? 172.211 199.894 229.572 1.00 51.79  ? 915  GLN B CB  1 
ATOM   7142  C CG  . GLN A 1 932  ? 171.528 200.456 228.347 1.00 51.79  ? 915  GLN B CG  1 
ATOM   7143  C CD  . GLN A 1 932  ? 170.946 199.374 227.470 1.00 51.79  ? 915  GLN B CD  1 
ATOM   7144  O OE1 . GLN A 1 932  ? 170.650 198.276 227.936 1.00 51.79  ? 915  GLN B OE1 1 
ATOM   7145  N NE2 . GLN A 1 932  ? 170.777 199.676 226.192 1.00 51.79  ? 915  GLN B NE2 1 
ATOM   7146  N N   . LEU A 1 933  ? 172.714 203.288 229.965 1.00 50.69  ? 916  LEU B N   1 
ATOM   7147  C CA  . LEU A 1 933  ? 172.086 204.597 230.081 1.00 50.69  ? 916  LEU B CA  1 
ATOM   7148  C C   . LEU A 1 933  ? 171.580 205.036 228.716 1.00 50.69  ? 916  LEU B C   1 
ATOM   7149  O O   . LEU A 1 933  ? 172.325 204.986 227.731 1.00 50.69  ? 916  LEU B O   1 
ATOM   7150  C CB  . LEU A 1 933  ? 173.061 205.639 230.630 1.00 50.69  ? 916  LEU B CB  1 
ATOM   7151  C CG  . LEU A 1 933  ? 173.821 205.302 231.910 1.00 50.69  ? 916  LEU B CG  1 
ATOM   7152  C CD1 . LEU A 1 933  ? 174.794 206.412 232.251 1.00 50.69  ? 916  LEU B CD1 1 
ATOM   7153  C CD2 . LEU A 1 933  ? 172.858 205.075 233.050 1.00 50.69  ? 916  LEU B CD2 1 
ATOM   7154  N N   . PHE A 1 934  ? 170.325 205.477 228.667 1.00 53.34  ? 917  PHE B N   1 
ATOM   7155  C CA  . PHE A 1 934  ? 169.671 205.894 227.438 1.00 53.34  ? 917  PHE B CA  1 
ATOM   7156  C C   . PHE A 1 934  ? 169.650 207.415 227.339 1.00 53.34  ? 917  PHE B C   1 
ATOM   7157  O O   . PHE A 1 934  ? 170.093 208.131 228.238 1.00 53.34  ? 917  PHE B O   1 
ATOM   7158  C CB  . PHE A 1 934  ? 168.250 205.337 227.371 1.00 53.34  ? 917  PHE B CB  1 
ATOM   7159  C CG  . PHE A 1 934  ? 168.187 203.844 227.351 1.00 53.34  ? 917  PHE B CG  1 
ATOM   7160  C CD1 . PHE A 1 934  ? 168.209 203.156 226.155 1.00 53.34  ? 917  PHE B CD1 1 
ATOM   7161  C CD2 . PHE A 1 934  ? 168.103 203.128 228.528 1.00 53.34  ? 917  PHE B CD2 1 
ATOM   7162  C CE1 . PHE A 1 934  ? 168.151 201.783 226.134 1.00 53.34  ? 917  PHE B CE1 1 
ATOM   7163  C CE2 . PHE A 1 934  ? 168.045 201.753 228.512 1.00 53.34  ? 917  PHE B CE2 1 
ATOM   7164  C CZ  . PHE A 1 934  ? 168.068 201.081 227.315 1.00 53.34  ? 917  PHE B CZ  1 
ATOM   7165  N N   . ASN A 1 935  ? 169.118 207.913 226.225 1.00 54.33  ? 918  ASN B N   1 
ATOM   7166  C CA  . ASN A 1 935  ? 168.973 209.352 226.012 1.00 54.33  ? 918  ASN B CA  1 
ATOM   7167  C C   . ASN A 1 935  ? 167.561 209.785 226.404 1.00 54.33  ? 918  ASN B C   1 
ATOM   7168  O O   . ASN A 1 935  ? 166.731 210.162 225.578 1.00 54.33  ? 918  ASN B O   1 
ATOM   7169  C CB  . ASN A 1 935  ? 169.292 209.710 224.565 1.00 54.33  ? 918  ASN B CB  1 
ATOM   7170  C CG  . ASN A 1 935  ? 169.406 211.207 224.344 1.00 54.33  ? 918  ASN B CG  1 
ATOM   7171  O OD1 . ASN A 1 935  ? 169.068 212.003 225.216 1.00 54.33  ? 918  ASN B OD1 1 
ATOM   7172  N ND2 . ASN A 1 935  ? 169.891 211.595 223.174 1.00 54.33  ? 918  ASN B ND2 1 
ATOM   7173  N N   . LEU A 1 936  ? 167.308 209.726 227.707 1.00 57.40  ? 919  LEU B N   1 
ATOM   7174  C CA  . LEU A 1 936  ? 166.041 210.142 228.283 1.00 57.40  ? 919  LEU B CA  1 
ATOM   7175  C C   . LEU A 1 936  ? 166.310 211.037 229.484 1.00 57.40  ? 919  LEU B C   1 
ATOM   7176  O O   . LEU A 1 936  ? 167.371 210.972 230.107 1.00 57.40  ? 919  LEU B O   1 
ATOM   7177  C CB  . LEU A 1 936  ? 165.187 208.939 228.701 1.00 57.40  ? 919  LEU B CB  1 
ATOM   7178  C CG  . LEU A 1 936  ? 164.784 207.989 227.577 1.00 57.40  ? 919  LEU B CG  1 
ATOM   7179  C CD1 . LEU A 1 936  ? 164.200 206.708 228.140 1.00 57.40  ? 919  LEU B CD1 1 
ATOM   7180  C CD2 . LEU A 1 936  ? 163.795 208.667 226.651 1.00 57.40  ? 919  LEU B CD2 1 
ATOM   7181  N N   . GLU A 1 937  ? 165.331 211.887 229.798 1.00 63.49  ? 920  GLU B N   1 
ATOM   7182  C CA  . GLU A 1 937  ? 165.487 212.798 230.926 1.00 63.49  ? 920  GLU B CA  1 
ATOM   7183  C C   . GLU A 1 937  ? 165.540 212.051 232.250 1.00 63.49  ? 920  GLU B C   1 
ATOM   7184  O O   . GLU A 1 937  ? 166.102 212.562 233.225 1.00 63.49  ? 920  GLU B O   1 
ATOM   7185  C CB  . GLU A 1 937  ? 164.346 213.815 230.946 1.00 63.49  ? 920  GLU B CB  1 
ATOM   7186  C CG  . GLU A 1 937  ? 163.867 214.246 229.571 1.00 63.49  ? 920  GLU B CG  1 
ATOM   7187  C CD  . GLU A 1 937  ? 162.711 213.405 229.067 1.00 63.49  ? 920  GLU B CD  1 
ATOM   7188  O OE1 . GLU A 1 937  ? 162.510 212.292 229.597 1.00 63.49  ? 920  GLU B OE1 1 
ATOM   7189  O OE2 . GLU A 1 937  ? 162.004 213.856 228.142 1.00 63.49  ? 920  GLU B OE2 1 
ATOM   7190  N N   . SER A 1 938  ? 164.963 210.854 232.307 1.00 58.20  ? 921  SER B N   1 
ATOM   7191  C CA  . SER A 1 938  ? 164.877 210.085 233.538 1.00 58.20  ? 921  SER B CA  1 
ATOM   7192  C C   . SER A 1 938  ? 165.883 208.947 233.610 1.00 58.20  ? 921  SER B C   1 
ATOM   7193  O O   . SER A 1 938  ? 165.866 208.190 234.583 1.00 58.20  ? 921  SER B O   1 
ATOM   7194  C CB  . SER A 1 938  ? 163.464 209.524 233.706 1.00 58.20  ? 921  SER B CB  1 
ATOM   7195  O OG  . SER A 1 938  ? 163.496 208.283 234.384 1.00 58.20  ? 921  SER B OG  1 
ATOM   7196  N N   . SER A 1 939  ? 166.746 208.799 232.612 1.00 55.48  ? 922  SER B N   1 
ATOM   7197  C CA  . SER A 1 939  ? 167.740 207.726 232.601 1.00 55.48  ? 922  SER B CA  1 
ATOM   7198  C C   . SER A 1 939  ? 169.098 208.244 233.067 1.00 55.48  ? 922  SER B C   1 
ATOM   7199  O O   . SER A 1 939  ? 170.076 208.265 232.326 1.00 55.48  ? 922  SER B O   1 
ATOM   7200  C CB  . SER A 1 939  ? 167.835 207.113 231.210 1.00 55.48  ? 922  SER B CB  1 
ATOM   7201  O OG  . SER A 1 939  ? 168.393 205.815 231.271 1.00 55.48  ? 922  SER B OG  1 
ATOM   7202  N N   . LYS A 1 940  ? 169.146 208.658 234.330 1.00 56.03  ? 923  LYS B N   1 
ATOM   7203  C CA  . LYS A 1 940  ? 170.330 209.279 234.898 1.00 56.03  ? 923  LYS B CA  1 
ATOM   7204  C C   . LYS A 1 940  ? 170.688 208.617 236.218 1.00 56.03  ? 923  LYS B C   1 
ATOM   7205  O O   . LYS A 1 940  ? 169.856 207.981 236.866 1.00 56.03  ? 923  LYS B O   1 
ATOM   7206  C CB  . LYS A 1 940  ? 170.128 210.780 235.127 1.00 56.03  ? 923  LYS B CB  1 
ATOM   7207  C CG  . LYS A 1 940  ? 169.091 211.110 236.179 1.00 56.03  ? 923  LYS B CG  1 
ATOM   7208  C CD  . LYS A 1 940  ? 168.777 212.595 236.177 1.00 56.03  ? 923  LYS B CD  1 
ATOM   7209  C CE  . LYS A 1 940  ? 167.600 212.917 237.079 1.00 56.03  ? 923  LYS B CE  1 
ATOM   7210  N NZ  . LYS A 1 940  ? 167.352 214.383 237.153 1.00 56.03  ? 923  LYS B NZ  1 
ATOM   7211  N N   . ILE A 1 941  ? 171.950 208.774 236.605 1.00 56.60  ? 924  ILE B N   1 
ATOM   7212  C CA  . ILE A 1 941  ? 172.435 208.360 237.915 1.00 56.60  ? 924  ILE B CA  1 
ATOM   7213  C C   . ILE A 1 941  ? 173.085 209.568 238.569 1.00 56.60  ? 924  ILE B C   1 
ATOM   7214  O O   . ILE A 1 941  ? 173.801 210.325 237.907 1.00 56.60  ? 924  ILE B O   1 
ATOM   7215  C CB  . ILE A 1 941  ? 173.430 207.190 237.822 1.00 56.60  ? 924  ILE B CB  1 
ATOM   7216  C CG1 . ILE A 1 941  ? 172.752 205.961 237.228 1.00 56.60  ? 924  ILE B CG1 1 
ATOM   7217  C CG2 . ILE A 1 941  ? 173.992 206.855 239.187 1.00 56.60  ? 924  ILE B CG2 1 
ATOM   7218  C CD1 . ILE A 1 941  ? 173.680 204.784 237.067 1.00 56.60  ? 924  ILE B CD1 1 
ATOM   7219  N N   . GLU A 1 942  ? 172.820 209.767 239.851 1.00 61.31  ? 925  GLU B N   1 
ATOM   7220  C CA  . GLU A 1 942  ? 173.395 210.869 240.601 1.00 61.31  ? 925  GLU B CA  1 
ATOM   7221  C C   . GLU A 1 942  ? 174.218 210.316 241.750 1.00 61.31  ? 925  GLU B C   1 
ATOM   7222  O O   . GLU A 1 942  ? 173.794 209.382 242.434 1.00 61.31  ? 925  GLU B O   1 
ATOM   7223  C CB  . GLU A 1 942  ? 172.311 211.794 241.143 1.00 61.31  ? 925  GLU B CB  1 
ATOM   7224  C CG  . GLU A 1 942  ? 172.839 212.899 242.031 1.00 61.31  ? 925  GLU B CG  1 
ATOM   7225  C CD  . GLU A 1 942  ? 171.999 214.150 241.944 1.00 61.31  ? 925  GLU B CD  1 
ATOM   7226  O OE1 . GLU A 1 942  ? 170.781 214.030 241.703 1.00 61.31  ? 925  GLU B OE1 1 
ATOM   7227  O OE2 . GLU A 1 942  ? 172.555 215.255 242.105 1.00 61.31  ? 925  GLU B OE2 1 
ATOM   7228  N N   . VAL A 1 943  ? 175.397 210.886 241.957 1.00 59.26  ? 926  VAL B N   1 
ATOM   7229  C CA  . VAL A 1 943  ? 176.211 210.572 243.124 1.00 59.26  ? 926  VAL B CA  1 
ATOM   7230  C C   . VAL A 1 943  ? 176.378 211.850 243.928 1.00 59.26  ? 926  VAL B C   1 
ATOM   7231  O O   . VAL A 1 943  ? 176.905 212.845 243.417 1.00 59.26  ? 926  VAL B O   1 
ATOM   7232  C CB  . VAL A 1 943  ? 177.572 209.979 242.736 1.00 59.26  ? 926  VAL B CB  1 
ATOM   7233  C CG1 . VAL A 1 943  ? 178.336 209.573 243.979 1.00 59.26  ? 926  VAL B CG1 1 
ATOM   7234  C CG2 . VAL A 1 943  ? 177.380 208.789 241.821 1.00 59.26  ? 926  VAL B CG2 1 
ATOM   7235  N N   . ILE A 1 944  ? 175.916 211.826 245.175 1.00 63.71  ? 927  ILE B N   1 
ATOM   7236  C CA  . ILE A 1 944  ? 176.029 212.944 246.100 1.00 63.71  ? 927  ILE B CA  1 
ATOM   7237  C C   . ILE A 1 944  ? 177.008 212.520 247.181 1.00 63.71  ? 927  ILE B C   1 
ATOM   7238  O O   . ILE A 1 944  ? 176.729 211.587 247.947 1.00 63.71  ? 927  ILE B O   1 
ATOM   7239  C CB  . ILE A 1 944  ? 174.673 213.321 246.708 1.00 63.71  ? 927  ILE B CB  1 
ATOM   7240  C CG1 . ILE A 1 944  ? 173.669 213.686 245.616 1.00 63.71  ? 927  ILE B CG1 1 
ATOM   7241  C CG2 . ILE A 1 944  ? 174.840 214.463 247.695 1.00 63.71  ? 927  ILE B CG2 1 
ATOM   7242  C CD1 . ILE A 1 944  ? 173.678 215.140 245.239 1.00 63.71  ? 927  ILE B CD1 1 
ATOM   7243  N N   . LEU A 1 945  ? 178.147 213.204 247.247 1.00 65.18  ? 928  LEU B N   1 
ATOM   7244  C CA  . LEU A 1 945  ? 179.195 212.878 248.198 1.00 65.18  ? 928  LEU B CA  1 
ATOM   7245  C C   . LEU A 1 945  ? 178.901 213.496 249.561 1.00 65.18  ? 928  LEU B C   1 
ATOM   7246  O O   . LEU A 1 945  ? 178.108 214.432 249.693 1.00 65.18  ? 928  LEU B O   1 
ATOM   7247  C CB  . LEU A 1 945  ? 180.552 213.365 247.691 1.00 65.18  ? 928  LEU B CB  1 
ATOM   7248  C CG  . LEU A 1 945  ? 181.212 212.546 246.582 1.00 65.18  ? 928  LEU B CG  1 
ATOM   7249  C CD1 . LEU A 1 945  ? 180.825 213.084 245.222 1.00 65.18  ? 928  LEU B CD1 1 
ATOM   7250  C CD2 . LEU A 1 945  ? 182.719 212.550 246.746 1.00 65.18  ? 928  LEU B CD2 1 
ATOM   7251  N N   . LYS A 1 946  ? 179.556 212.955 250.584 1.00 67.28  ? 929  LYS B N   1 
ATOM   7252  C CA  . LYS A 1 946  ? 179.403 213.478 251.933 1.00 67.28  ? 929  LYS B CA  1 
ATOM   7253  C C   . LYS A 1 946  ? 180.006 214.873 252.019 1.00 67.28  ? 929  LYS B C   1 
ATOM   7254  O O   . LYS A 1 946  ? 181.136 215.100 251.579 1.00 67.28  ? 929  LYS B O   1 
ATOM   7255  C CB  . LYS A 1 946  ? 180.070 212.546 252.941 1.00 67.28  ? 929  LYS B CB  1 
ATOM   7256  C CG  . LYS A 1 946  ? 179.312 211.253 253.179 1.00 67.28  ? 929  LYS B CG  1 
ATOM   7257  C CD  . LYS A 1 946  ? 179.524 210.739 254.590 1.00 67.28  ? 929  LYS B CD  1 
ATOM   7258  C CE  . LYS A 1 946  ? 179.280 209.243 254.670 1.00 67.28  ? 929  LYS B CE  1 
ATOM   7259  N NZ  . LYS A 1 946  ? 180.387 208.536 255.370 1.00 67.28  ? 929  LYS B NZ  1 
ATOM   7260  N N   . ASN A 1 947  ? 179.249 215.810 252.590 1.00 69.52  ? 930  ASN B N   1 
ATOM   7261  C CA  . ASN A 1 947  ? 179.687 217.200 252.633 1.00 69.52  ? 930  ASN B CA  1 
ATOM   7262  C C   . ASN A 1 947  ? 180.878 217.415 253.556 1.00 69.52  ? 930  ASN B C   1 
ATOM   7263  O O   . ASN A 1 947  ? 181.614 218.391 253.376 1.00 69.52  ? 930  ASN B O   1 
ATOM   7264  C CB  . ASN A 1 947  ? 178.530 218.097 253.066 1.00 69.52  ? 930  ASN B CB  1 
ATOM   7265  C CG  . ASN A 1 947  ? 178.823 219.565 252.853 1.00 69.52  ? 930  ASN B CG  1 
ATOM   7266  O OD1 . ASN A 1 947  ? 179.339 219.960 251.809 1.00 69.52  ? 930  ASN B OD1 1 
ATOM   7267  N ND2 . ASN A 1 947  ? 178.497 220.384 253.846 1.00 69.52  ? 930  ASN B ND2 1 
ATOM   7268  N N   . ALA A 1 948  ? 181.088 216.536 254.530 1.00 69.07  ? 931  ALA B N   1 
ATOM   7269  C CA  . ALA A 1 948  ? 182.156 216.695 255.506 1.00 69.07  ? 931  ALA B CA  1 
ATOM   7270  C C   . ALA A 1 948  ? 183.420 215.936 255.130 1.00 69.07  ? 931  ALA B C   1 
ATOM   7271  O O   . ALA A 1 948  ? 184.332 215.830 255.955 1.00 69.07  ? 931  ALA B O   1 
ATOM   7272  C CB  . ALA A 1 948  ? 181.678 216.248 256.889 1.00 69.07  ? 931  ALA B CB  1 
ATOM   7273  N N   . ILE A 1 949  ? 183.490 215.397 253.916 1.00 66.63  ? 932  ILE B N   1 
ATOM   7274  C CA  . ILE A 1 949  ? 184.665 214.662 253.465 1.00 66.63  ? 932  ILE B CA  1 
ATOM   7275  C C   . ILE A 1 949  ? 185.288 215.394 252.283 1.00 66.63  ? 932  ILE B C   1 
ATOM   7276  O O   . ILE A 1 949  ? 186.508 215.364 252.087 1.00 66.63  ? 932  ILE B O   1 
ATOM   7277  C CB  . ILE A 1 949  ? 184.291 213.212 253.111 1.00 66.63  ? 932  ILE B CB  1 
ATOM   7278  C CG1 . ILE A 1 949  ? 184.392 212.325 254.350 1.00 66.63  ? 932  ILE B CG1 1 
ATOM   7279  C CG2 . ILE A 1 949  ? 185.160 212.673 251.997 1.00 66.63  ? 932  ILE B CG2 1 
ATOM   7280  C CD1 . ILE A 1 949  ? 183.951 210.902 254.116 1.00 66.63  ? 932  ILE B CD1 1 
ATOM   7281  N N   . VAL A 1 950  ? 184.458 216.089 251.512 1.00 66.58  ? 933  VAL B N   1 
ATOM   7282  C CA  . VAL A 1 950  ? 184.918 216.788 250.317 1.00 66.58  ? 933  VAL B CA  1 
ATOM   7283  C C   . VAL A 1 950  ? 185.565 218.105 250.726 1.00 66.58  ? 933  VAL B C   1 
ATOM   7284  O O   . VAL A 1 950  ? 184.947 218.930 251.405 1.00 66.58  ? 933  VAL B O   1 
ATOM   7285  C CB  . VAL A 1 950  ? 183.758 217.025 249.341 1.00 66.58  ? 933  VAL B CB  1 
ATOM   7286  C CG1 . VAL A 1 950  ? 184.093 218.149 248.376 1.00 66.58  ? 933  VAL B CG1 1 
ATOM   7287  C CG2 . VAL A 1 950  ? 183.439 215.748 248.586 1.00 66.58  ? 933  VAL B CG2 1 
ATOM   7288  N N   . TYR A 1 951  ? 186.810 218.305 250.308 1.00 67.31  ? 934  TYR B N   1 
ATOM   7289  C CA  . TYR A 1 951  ? 187.530 219.547 250.534 1.00 67.31  ? 934  TYR B CA  1 
ATOM   7290  C C   . TYR A 1 951  ? 187.493 220.417 249.285 1.00 67.31  ? 934  TYR B C   1 
ATOM   7291  O O   . TYR A 1 951  ? 187.270 219.940 248.170 1.00 67.31  ? 934  TYR B O   1 
ATOM   7292  C CB  . TYR A 1 951  ? 188.982 219.282 250.945 1.00 67.31  ? 934  TYR B CB  1 
ATOM   7293  C CG  . TYR A 1 951  ? 189.604 218.044 250.344 1.00 67.31  ? 934  TYR B CG  1 
ATOM   7294  C CD1 . TYR A 1 951  ? 189.361 216.788 250.882 1.00 67.31  ? 934  TYR B CD1 1 
ATOM   7295  C CD2 . TYR A 1 951  ? 190.431 218.128 249.240 1.00 67.31  ? 934  TYR B CD2 1 
ATOM   7296  C CE1 . TYR A 1 951  ? 189.927 215.655 250.340 1.00 67.31  ? 934  TYR B CE1 1 
ATOM   7297  C CE2 . TYR A 1 951  ? 190.997 217.000 248.688 1.00 67.31  ? 934  TYR B CE2 1 
ATOM   7298  C CZ  . TYR A 1 951  ? 190.745 215.766 249.245 1.00 67.31  ? 934  TYR B CZ  1 
ATOM   7299  O OH  . TYR A 1 951  ? 191.310 214.637 248.702 1.00 67.31  ? 934  TYR B OH  1 
ATOM   7300  N N   . ASN A 1 952  ? 187.716 221.716 249.489 1.00 70.18  ? 935  ASN B N   1 
ATOM   7301  C CA  . ASN A 1 952  ? 187.605 222.669 248.390 1.00 70.18  ? 935  ASN B CA  1 
ATOM   7302  C C   . ASN A 1 952  ? 188.685 222.445 247.341 1.00 70.18  ? 935  ASN B C   1 
ATOM   7303  O O   . ASN A 1 952  ? 188.430 222.588 246.140 1.00 70.18  ? 935  ASN B O   1 
ATOM   7304  C CB  . ASN A 1 952  ? 187.670 224.096 248.927 1.00 70.18  ? 935  ASN B CB  1 
ATOM   7305  C CG  . ASN A 1 952  ? 186.382 224.860 248.706 1.00 70.18  ? 935  ASN B CG  1 
ATOM   7306  O OD1 . ASN A 1 952  ? 185.561 224.481 247.872 1.00 70.18  ? 935  ASN B OD1 1 
ATOM   7307  N ND2 . ASN A 1 952  ? 186.199 225.943 249.452 1.00 70.18  ? 935  ASN B ND2 1 
ATOM   7308  N N   . SER A 1 953  ? 189.897 222.091 247.770 1.00 69.51  ? 936  SER B N   1 
ATOM   7309  C CA  . SER A 1 953  ? 191.044 221.993 246.876 1.00 69.51  ? 936  SER B CA  1 
ATOM   7310  C C   . SER A 1 953  ? 191.231 220.598 246.299 1.00 69.51  ? 936  SER B C   1 
ATOM   7311  O O   . SER A 1 953  ? 192.361 220.213 245.973 1.00 69.51  ? 936  SER B O   1 
ATOM   7312  C CB  . SER A 1 953  ? 192.310 222.445 247.600 1.00 69.51  ? 936  SER B CB  1 
ATOM   7313  O OG  . SER A 1 953  ? 192.235 223.825 247.902 1.00 69.51  ? 936  SER B OG  1 
ATOM   7314  N N   . MET A 1 954  ? 190.158 219.828 246.169 1.00 69.87  ? 937  MET B N   1 
ATOM   7315  C CA  . MET A 1 954  ? 190.235 218.553 245.478 1.00 69.87  ? 937  MET B CA  1 
ATOM   7316  C C   . MET A 1 954  ? 190.326 218.797 243.972 1.00 69.87  ? 937  MET B C   1 
ATOM   7317  O O   . MET A 1 954  ? 190.332 219.936 243.497 1.00 69.87  ? 937  MET B O   1 
ATOM   7318  C CB  . MET A 1 954  ? 189.028 217.691 245.839 1.00 69.87  ? 937  MET B CB  1 
ATOM   7319  C CG  . MET A 1 954  ? 189.255 216.194 245.730 1.00 69.87  ? 937  MET B CG  1 
ATOM   7320  S SD  . MET A 1 954  ? 187.867 215.247 246.379 1.00 69.87  ? 937  MET B SD  1 
ATOM   7321  C CE  . MET A 1 954  ? 186.536 216.434 246.233 1.00 69.87  ? 937  MET B CE  1 
ATOM   7322  N N   . TYR A 1 955  ? 190.410 217.708 243.210 1.00 68.43  ? 938  TYR B N   1 
ATOM   7323  C CA  . TYR A 1 955  ? 190.465 217.745 241.750 1.00 68.43  ? 938  TYR B CA  1 
ATOM   7324  C C   . TYR A 1 955  ? 191.687 218.493 241.229 1.00 68.43  ? 938  TYR B C   1 
ATOM   7325  O O   . TYR A 1 955  ? 191.688 218.968 240.090 1.00 68.43  ? 938  TYR B O   1 
ATOM   7326  C CB  . TYR A 1 955  ? 189.185 218.346 241.156 1.00 68.43  ? 938  TYR B CB  1 
ATOM   7327  C CG  . TYR A 1 955  ? 187.924 217.634 241.583 1.00 68.43  ? 938  TYR B CG  1 
ATOM   7328  C CD1 . TYR A 1 955  ? 187.920 216.266 241.808 1.00 68.43  ? 938  TYR B CD1 1 
ATOM   7329  C CD2 . TYR A 1 955  ? 186.740 218.329 241.766 1.00 68.43  ? 938  TYR B CD2 1 
ATOM   7330  C CE1 . TYR A 1 955  ? 186.775 215.612 242.201 1.00 68.43  ? 938  TYR B CE1 1 
ATOM   7331  C CE2 . TYR A 1 955  ? 185.590 217.683 242.159 1.00 68.43  ? 938  TYR B CE2 1 
ATOM   7332  C CZ  . TYR A 1 955  ? 185.613 216.325 242.375 1.00 68.43  ? 938  TYR B CZ  1 
ATOM   7333  O OH  . TYR A 1 955  ? 184.468 215.674 242.768 1.00 68.43  ? 938  TYR B OH  1 
ATOM   7334  N N   . GLU A 1 956  ? 192.733 218.613 242.045 1.00 69.09  ? 939  GLU B N   1 
ATOM   7335  C CA  . GLU A 1 956  ? 193.998 219.170 241.585 1.00 69.09  ? 939  GLU B CA  1 
ATOM   7336  C C   . GLU A 1 956  ? 194.924 218.075 241.072 1.00 69.09  ? 939  GLU B C   1 
ATOM   7337  O O   . GLU A 1 956  ? 195.554 218.230 240.022 1.00 69.09  ? 939  GLU B O   1 
ATOM   7338  C CB  . GLU A 1 956  ? 194.670 219.955 242.713 1.00 69.09  ? 939  GLU B CB  1 
ATOM   7339  C CG  . GLU A 1 956  ? 194.002 221.284 243.022 1.00 69.09  ? 939  GLU B CG  1 
ATOM   7340  C CD  . GLU A 1 956  ? 194.987 222.347 243.464 1.00 69.09  ? 939  GLU B CD  1 
ATOM   7341  O OE1 . GLU A 1 956  ? 196.178 222.020 243.641 1.00 69.09  ? 939  GLU B OE1 1 
ATOM   7342  O OE2 . GLU A 1 956  ? 194.568 223.511 243.635 1.00 69.09  ? 939  GLU B OE2 1 
ATOM   7343  N N   . ASN A 1 957  ? 195.016 216.968 241.804 1.00 65.53  ? 940  ASN B N   1 
ATOM   7344  C CA  . ASN A 1 957  ? 195.729 215.774 241.363 1.00 65.53  ? 940  ASN B CA  1 
ATOM   7345  C C   . ASN A 1 957  ? 194.799 214.593 241.580 1.00 65.53  ? 940  ASN B C   1 
ATOM   7346  O O   . ASN A 1 957  ? 194.568 214.188 242.724 1.00 65.53  ? 940  ASN B O   1 
ATOM   7347  C CB  . ASN A 1 957  ? 197.036 215.584 242.131 1.00 65.53  ? 940  ASN B CB  1 
ATOM   7348  C CG  . ASN A 1 957  ? 197.785 216.879 242.335 1.00 65.53  ? 940  ASN B CG  1 
ATOM   7349  O OD1 . ASN A 1 957  ? 197.280 217.809 242.962 1.00 65.53  ? 940  ASN B OD1 1 
ATOM   7350  N ND2 . ASN A 1 957  ? 199.002 216.948 241.810 1.00 65.53  ? 940  ASN B ND2 1 
ATOM   7351  N N   . PHE A 1 958  ? 194.262 214.040 240.497 1.00 63.07  ? 941  PHE B N   1 
ATOM   7352  C CA  . PHE A 1 958  ? 193.265 212.987 240.652 1.00 63.07  ? 941  PHE B CA  1 
ATOM   7353  C C   . PHE A 1 958  ? 193.167 212.156 239.385 1.00 63.07  ? 941  PHE B C   1 
ATOM   7354  O O   . PHE A 1 958  ? 193.541 212.597 238.298 1.00 63.07  ? 941  PHE B O   1 
ATOM   7355  C CB  . PHE A 1 958  ? 191.899 213.573 241.013 1.00 63.07  ? 941  PHE B CB  1 
ATOM   7356  C CG  . PHE A 1 958  ? 191.151 214.129 239.842 1.00 63.07  ? 941  PHE B CG  1 
ATOM   7357  C CD1 . PHE A 1 958  ? 191.410 215.406 239.390 1.00 63.07  ? 941  PHE B CD1 1 
ATOM   7358  C CD2 . PHE A 1 958  ? 190.182 213.381 239.202 1.00 63.07  ? 941  PHE B CD2 1 
ATOM   7359  C CE1 . PHE A 1 958  ? 190.724 215.926 238.320 1.00 63.07  ? 941  PHE B CE1 1 
ATOM   7360  C CE2 . PHE A 1 958  ? 189.494 213.896 238.128 1.00 63.07  ? 941  PHE B CE2 1 
ATOM   7361  C CZ  . PHE A 1 958  ? 189.765 215.170 237.688 1.00 63.07  ? 941  PHE B CZ  1 
ATOM   7362  N N   . SER A 1 959  ? 192.618 210.955 239.534 1.00 59.40  ? 942  SER B N   1 
ATOM   7363  C CA  . SER A 1 959  ? 192.475 210.031 238.422 1.00 59.40  ? 942  SER B CA  1 
ATOM   7364  C C   . SER A 1 959  ? 191.045 209.520 238.353 1.00 59.40  ? 942  SER B C   1 
ATOM   7365  O O   . SER A 1 959  ? 190.310 209.531 239.340 1.00 59.40  ? 942  SER B O   1 
ATOM   7366  C CB  . SER A 1 959  ? 193.445 208.853 238.543 1.00 59.40  ? 942  SER B CB  1 
ATOM   7367  O OG  . SER A 1 959  ? 194.744 209.304 238.875 1.00 59.40  ? 942  SER B OG  1 
ATOM   7368  N N   . THR A 1 960  ? 190.657 209.074 237.164 1.00 57.07  ? 943  THR B N   1 
ATOM   7369  C CA  . THR A 1 960  ? 189.343 208.498 236.930 1.00 57.07  ? 943  THR B CA  1 
ATOM   7370  C C   . THR A 1 960  ? 189.502 207.316 235.989 1.00 57.07  ? 943  THR B C   1 
ATOM   7371  O O   . THR A 1 960  ? 190.391 207.310 235.137 1.00 57.07  ? 943  THR B O   1 
ATOM   7372  C CB  . THR A 1 960  ? 188.378 209.524 236.327 1.00 57.07  ? 943  THR B CB  1 
ATOM   7373  O OG1 . THR A 1 960  ? 188.596 210.801 236.938 1.00 57.07  ? 943  THR B OG1 1 
ATOM   7374  C CG2 . THR A 1 960  ? 186.941 209.104 236.552 1.00 57.07  ? 943  THR B CG2 1 
ATOM   7375  N N   . SER A 1 961  ? 188.644 206.313 236.143 1.00 54.16  ? 944  SER B N   1 
ATOM   7376  C CA  . SER A 1 961  ? 188.734 205.147 235.277 1.00 54.16  ? 944  SER B CA  1 
ATOM   7377  C C   . SER A 1 961  ? 187.372 204.489 235.155 1.00 54.16  ? 944  SER B C   1 
ATOM   7378  O O   . SER A 1 961  ? 186.649 204.364 236.145 1.00 54.16  ? 944  SER B O   1 
ATOM   7379  C CB  . SER A 1 961  ? 189.753 204.135 235.805 1.00 54.16  ? 944  SER B CB  1 
ATOM   7380  O OG  . SER A 1 961  ? 189.246 203.454 236.937 1.00 54.16  ? 944  SER B OG  1 
ATOM   7381  N N   . PHE A 1 962  ? 187.033 204.058 233.943 1.00 56.69  ? 945  PHE B N   1 
ATOM   7382  C CA  . PHE A 1 962  ? 185.765 203.376 233.732 1.00 56.69  ? 945  PHE B CA  1 
ATOM   7383  C C   . PHE A 1 962  ? 185.819 202.595 232.431 1.00 56.69  ? 945  PHE B C   1 
ATOM   7384  O O   . PHE A 1 962  ? 186.555 202.952 231.509 1.00 56.69  ? 945  PHE B O   1 
ATOM   7385  C CB  . PHE A 1 962  ? 184.591 204.362 233.711 1.00 56.69  ? 945  PHE B CB  1 
ATOM   7386  C CG  . PHE A 1 962  ? 184.820 205.564 232.845 1.00 56.69  ? 945  PHE B CG  1 
ATOM   7387  C CD1 . PHE A 1 962  ? 185.424 206.696 233.355 1.00 56.69  ? 945  PHE B CD1 1 
ATOM   7388  C CD2 . PHE A 1 962  ? 184.419 205.568 231.525 1.00 56.69  ? 945  PHE B CD2 1 
ATOM   7389  C CE1 . PHE A 1 962  ? 185.632 207.804 232.562 1.00 56.69  ? 945  PHE B CE1 1 
ATOM   7390  C CE2 . PHE A 1 962  ? 184.625 206.673 230.729 1.00 56.69  ? 945  PHE B CE2 1 
ATOM   7391  C CZ  . PHE A 1 962  ? 185.232 207.792 231.249 1.00 56.69  ? 945  PHE B CZ  1 
ATOM   7392  N N   . TRP A 1 963  ? 185.029 201.529 232.364 1.00 63.49  ? 946  TRP B N   1 
ATOM   7393  C CA  . TRP A 1 963  ? 184.865 200.758 231.143 1.00 63.49  ? 946  TRP B CA  1 
ATOM   7394  C C   . TRP A 1 963  ? 183.617 201.249 230.431 1.00 63.49  ? 946  TRP B C   1 
ATOM   7395  O O   . TRP A 1 963  ? 182.543 201.321 231.035 1.00 63.49  ? 946  TRP B O   1 
ATOM   7396  C CB  . TRP A 1 963  ? 184.743 199.268 231.445 1.00 63.49  ? 946  TRP B CB  1 
ATOM   7397  C CG  . TRP A 1 963  ? 185.981 198.659 231.984 1.00 63.49  ? 946  TRP B CG  1 
ATOM   7398  C CD1 . TRP A 1 963  ? 186.577 198.935 233.173 1.00 63.49  ? 946  TRP B CD1 1 
ATOM   7399  C CD2 . TRP A 1 963  ? 186.781 197.659 231.353 1.00 63.49  ? 946  TRP B CD2 1 
ATOM   7400  N NE1 . TRP A 1 963  ? 187.704 198.168 233.325 1.00 63.49  ? 946  TRP B NE1 1 
ATOM   7401  C CE2 . TRP A 1 963  ? 187.851 197.376 232.217 1.00 63.49  ? 946  TRP B CE2 1 
ATOM   7402  C CE3 . TRP A 1 963  ? 186.697 196.976 230.140 1.00 63.49  ? 946  TRP B CE3 1 
ATOM   7403  C CZ2 . TRP A 1 963  ? 188.828 196.441 231.908 1.00 63.49  ? 946  TRP B CZ2 1 
ATOM   7404  C CZ3 . TRP A 1 963  ? 187.666 196.050 229.834 1.00 63.49  ? 946  TRP B CZ3 1 
ATOM   7405  C CH2 . TRP A 1 963  ? 188.718 195.790 230.713 1.00 63.49  ? 946  TRP B CH2 1 
ATOM   7406  N N   . ILE A 1 964  ? 183.755 201.586 229.154 1.00 48.84  ? 947  ILE B N   1 
ATOM   7407  C CA  . ILE A 1 964  ? 182.658 202.155 228.386 1.00 48.84  ? 947  ILE B CA  1 
ATOM   7408  C C   . ILE A 1 964  ? 182.522 201.406 227.069 1.00 48.84  ? 947  ILE B C   1 
ATOM   7409  O O   . ILE A 1 964  ? 183.521 201.027 226.447 1.00 48.84  ? 947  ILE B O   1 
ATOM   7410  C CB  . ILE A 1 964  ? 182.854 203.668 228.151 1.00 48.84  ? 947  ILE B CB  1 
ATOM   7411  C CG1 . ILE A 1 964  ? 181.682 204.249 227.367 1.00 48.84  ? 947  ILE B CG1 1 
ATOM   7412  C CG2 . ILE A 1 964  ? 184.157 203.944 227.447 1.00 48.84  ? 947  ILE B CG2 1 
ATOM   7413  C CD1 . ILE A 1 964  ? 181.749 205.740 227.217 1.00 48.84  ? 947  ILE B CD1 1 
ATOM   7414  N N   . ARG A 1 965  ? 181.275 201.157 226.676 1.00 49.49  ? 948  ARG B N   1 
ATOM   7415  C CA  . ARG A 1 965  ? 180.927 200.573 225.388 1.00 49.49  ? 948  ARG B CA  1 
ATOM   7416  C C   . ARG A 1 965  ? 179.998 201.533 224.665 1.00 49.49  ? 948  ARG B C   1 
ATOM   7417  O O   . ARG A 1 965  ? 178.932 201.887 225.188 1.00 49.49  ? 948  ARG B O   1 
ATOM   7418  C CB  . ARG A 1 965  ? 180.263 199.208 225.554 1.00 49.49  ? 948  ARG B CB  1 
ATOM   7419  C CG  . ARG A 1 965  ? 179.953 198.526 224.241 1.00 49.49  ? 948  ARG B CG  1 
ATOM   7420  C CD  . ARG A 1 965  ? 180.167 197.029 224.325 1.00 49.49  ? 948  ARG B CD  1 
ATOM   7421  N NE  . ARG A 1 965  ? 178.972 196.314 224.751 1.00 49.49  ? 948  ARG B NE  1 
ATOM   7422  C CZ  . ARG A 1 965  ? 177.952 196.022 223.956 1.00 49.49  ? 948  ARG B CZ  1 
ATOM   7423  N NH1 . ARG A 1 965  ? 177.932 196.401 222.690 1.00 49.49  ? 948  ARG B NH1 1 
ATOM   7424  N NH2 . ARG A 1 965  ? 176.927 195.332 224.445 1.00 49.49  ? 948  ARG B NH2 1 
ATOM   7425  N N   . ILE A 1 966  ? 180.403 201.943 223.467 1.00 51.09  ? 949  ILE B N   1 
ATOM   7426  C CA  . ILE A 1 966  ? 179.698 202.945 222.675 1.00 51.09  ? 949  ILE B CA  1 
ATOM   7427  C C   . ILE A 1 966  ? 179.243 202.308 221.368 1.00 51.09  ? 949  ILE B C   1 
ATOM   7428  O O   . ILE A 1 966  ? 180.086 201.928 220.544 1.00 51.09  ? 949  ILE B O   1 
ATOM   7429  C CB  . ILE A 1 966  ? 180.593 204.160 222.399 1.00 51.09  ? 949  ILE B CB  1 
ATOM   7430  C CG1 . ILE A 1 966  ? 181.348 204.563 223.662 1.00 51.09  ? 949  ILE B CG1 1 
ATOM   7431  C CG2 . ILE A 1 966  ? 179.763 205.320 221.893 1.00 51.09  ? 949  ILE B CG2 1 
ATOM   7432  C CD1 . ILE A 1 966  ? 182.313 205.703 223.454 1.00 51.09  ? 949  ILE B CD1 1 
ATOM   7433  N N   . PRO A 1 967  ? 177.943 202.177 221.131 1.00 49.38  ? 950  PRO B N   1 
ATOM   7434  C CA  . PRO A 1 967  ? 177.474 201.575 219.879 1.00 49.38  ? 950  PRO B CA  1 
ATOM   7435  C C   . PRO A 1 967  ? 177.845 202.429 218.677 1.00 49.38  ? 950  PRO B C   1 
ATOM   7436  O O   . PRO A 1 967  ? 178.269 203.579 218.792 1.00 49.38  ? 950  PRO B O   1 
ATOM   7437  C CB  . PRO A 1 967  ? 175.957 201.500 220.066 1.00 49.38  ? 950  PRO B CB  1 
ATOM   7438  C CG  . PRO A 1 967  ? 175.652 202.507 221.110 1.00 49.38  ? 950  PRO B CG  1 
ATOM   7439  C CD  . PRO A 1 967  ? 176.830 202.523 222.025 1.00 49.38  ? 950  PRO B CD  1 
ATOM   7440  N N   . LYS A 1 968  ? 177.686 201.832 217.500 1.00 51.92  ? 951  LYS B N   1 
ATOM   7441  C CA  . LYS A 1 968  ? 178.019 202.516 216.260 1.00 51.92  ? 951  LYS B CA  1 
ATOM   7442  C C   . LYS A 1 968  ? 177.092 203.703 216.032 1.00 51.92  ? 951  LYS B C   1 
ATOM   7443  O O   . LYS A 1 968  ? 175.923 203.691 216.421 1.00 51.92  ? 951  LYS B O   1 
ATOM   7444  C CB  . LYS A 1 968  ? 177.927 201.547 215.086 1.00 51.92  ? 951  LYS B CB  1 
ATOM   7445  C CG  . LYS A 1 968  ? 178.745 201.950 213.883 1.00 51.92  ? 951  LYS B CG  1 
ATOM   7446  C CD  . LYS A 1 968  ? 179.195 200.726 213.115 1.00 51.92  ? 951  LYS B CD  1 
ATOM   7447  C CE  . LYS A 1 968  ? 178.020 200.028 212.463 1.00 51.92  ? 951  LYS B CE  1 
ATOM   7448  N NZ  . LYS A 1 968  ? 178.431 198.753 211.818 1.00 51.92  ? 951  LYS B NZ  1 
ATOM   7449  N N   . TYR A 1 969  ? 177.627 204.742 215.398 1.00 52.33  ? 952  TYR B N   1 
ATOM   7450  C CA  . TYR A 1 969  ? 176.855 205.936 215.080 1.00 52.33  ? 952  TYR B CA  1 
ATOM   7451  C C   . TYR A 1 969  ? 176.159 205.729 213.742 1.00 52.33  ? 952  TYR B C   1 
ATOM   7452  O O   . TYR A 1 969  ? 176.819 205.511 212.723 1.00 52.33  ? 952  TYR B O   1 
ATOM   7453  C CB  . TYR A 1 969  ? 177.757 207.167 215.035 1.00 52.33  ? 952  TYR B CB  1 
ATOM   7454  C CG  . TYR A 1 969  ? 178.309 207.562 216.383 1.00 52.33  ? 952  TYR B CG  1 
ATOM   7455  C CD1 . TYR A 1 969  ? 179.442 206.950 216.893 1.00 52.33  ? 952  TYR B CD1 1 
ATOM   7456  C CD2 . TYR A 1 969  ? 177.704 208.551 217.140 1.00 52.33  ? 952  TYR B CD2 1 
ATOM   7457  C CE1 . TYR A 1 969  ? 179.951 207.305 218.120 1.00 52.33  ? 952  TYR B CE1 1 
ATOM   7458  C CE2 . TYR A 1 969  ? 178.208 208.914 218.370 1.00 52.33  ? 952  TYR B CE2 1 
ATOM   7459  C CZ  . TYR A 1 969  ? 179.333 208.287 218.854 1.00 52.33  ? 952  TYR B CZ  1 
ATOM   7460  O OH  . TYR A 1 969  ? 179.845 208.639 220.078 1.00 52.33  ? 952  TYR B OH  1 
ATOM   7461  N N   . PHE A 1 970  ? 174.830 205.803 213.746 1.00 55.12  ? 953  PHE B N   1 
ATOM   7462  C CA  . PHE A 1 970  ? 174.026 205.496 212.572 1.00 55.12  ? 953  PHE B CA  1 
ATOM   7463  C C   . PHE A 1 970  ? 173.453 206.731 211.897 1.00 55.12  ? 953  PHE B C   1 
ATOM   7464  O O   . PHE A 1 970  ? 173.650 206.923 210.695 1.00 55.12  ? 953  PHE B O   1 
ATOM   7465  C CB  . PHE A 1 970  ? 172.889 204.547 212.961 1.00 55.12  ? 953  PHE B CB  1 
ATOM   7466  C CG  . PHE A 1 970  ? 173.336 203.139 213.197 1.00 55.12  ? 953  PHE B CG  1 
ATOM   7467  C CD1 . PHE A 1 970  ? 173.783 202.357 212.152 1.00 55.12  ? 953  PHE B CD1 1 
ATOM   7468  C CD2 . PHE A 1 970  ? 173.312 202.597 214.467 1.00 55.12  ? 953  PHE B CD2 1 
ATOM   7469  C CE1 . PHE A 1 970  ? 174.193 201.064 212.370 1.00 55.12  ? 953  PHE B CE1 1 
ATOM   7470  C CE2 . PHE A 1 970  ? 173.721 201.304 214.687 1.00 55.12  ? 953  PHE B CE2 1 
ATOM   7471  C CZ  . PHE A 1 970  ? 174.163 200.538 213.638 1.00 55.12  ? 953  PHE B CZ  1 
ATOM   7472  N N   . ASN A 1 971  ? 172.737 207.573 212.633 1.00 60.88  ? 954  ASN B N   1 
ATOM   7473  C CA  . ASN A 1 971  ? 172.148 208.764 212.043 1.00 60.88  ? 954  ASN B CA  1 
ATOM   7474  C C   . ASN A 1 971  ? 173.212 209.820 211.775 1.00 60.88  ? 954  ASN B C   1 
ATOM   7475  O O   . ASN A 1 971  ? 174.173 209.974 212.532 1.00 60.88  ? 954  ASN B O   1 
ATOM   7476  C CB  . ASN A 1 971  ? 171.062 209.339 212.951 1.00 60.88  ? 954  ASN B CB  1 
ATOM   7477  C CG  . ASN A 1 971  ? 170.023 208.309 213.340 1.00 60.88  ? 954  ASN B CG  1 
ATOM   7478  O OD1 . ASN A 1 971  ? 169.580 208.258 214.486 1.00 60.88  ? 954  ASN B OD1 1 
ATOM   7479  N ND2 . ASN A 1 971  ? 169.629 207.479 212.382 1.00 60.88  ? 954  ASN B ND2 1 
ATOM   7480  N N   . SER A 1 972  ? 173.024 210.554 210.679 1.00 61.22  ? 955  SER B N   1 
ATOM   7481  C CA  . SER A 1 972  ? 173.945 211.616 210.299 1.00 61.22  ? 955  SER B CA  1 
ATOM   7482  C C   . SER A 1 972  ? 173.854 212.832 211.211 1.00 61.22  ? 955  SER B C   1 
ATOM   7483  O O   . SER A 1 972  ? 174.687 213.736 211.092 1.00 61.22  ? 955  SER B O   1 
ATOM   7484  C CB  . SER A 1 972  ? 173.688 212.031 208.851 1.00 61.22  ? 955  SER B CB  1 
ATOM   7485  O OG  . SER A 1 972  ? 172.395 212.592 208.708 1.00 61.22  ? 955  SER B OG  1 
ATOM   7486  N N   . ILE A 1 973  ? 172.861 212.883 212.100 1.00 60.60  ? 956  ILE B N   1 
ATOM   7487  C CA  . ILE A 1 973  ? 172.782 213.974 213.064 1.00 60.60  ? 956  ILE B CA  1 
ATOM   7488  C C   . ILE A 1 973  ? 173.938 213.902 214.054 1.00 60.60  ? 956  ILE B C   1 
ATOM   7489  O O   . ILE A 1 973  ? 174.400 214.933 214.557 1.00 60.60  ? 956  ILE B O   1 
ATOM   7490  C CB  . ILE A 1 973  ? 171.414 213.943 213.772 1.00 60.60  ? 956  ILE B CB  1 
ATOM   7491  C CG1 . ILE A 1 973  ? 170.303 214.301 212.782 1.00 60.60  ? 956  ILE B CG1 1 
ATOM   7492  C CG2 . ILE A 1 973  ? 171.394 214.887 214.959 1.00 60.60  ? 956  ILE B CG2 1 
ATOM   7493  C CD1 . ILE A 1 973  ? 169.048 214.858 213.426 1.00 60.60  ? 956  ILE B CD1 1 
ATOM   7494  N N   . SER A 1 974  ? 174.443 212.696 214.325 1.00 60.37  ? 957  SER B N   1 
ATOM   7495  C CA  . SER A 1 974  ? 175.490 212.516 215.326 1.00 60.37  ? 957  SER B CA  1 
ATOM   7496  C C   . SER A 1 974  ? 176.778 213.248 214.976 1.00 60.37  ? 957  SER B C   1 
ATOM   7497  O O   . SER A 1 974  ? 177.573 213.535 215.876 1.00 60.37  ? 957  SER B O   1 
ATOM   7498  C CB  . SER A 1 974  ? 175.785 211.028 215.510 1.00 60.37  ? 957  SER B CB  1 
ATOM   7499  O OG  . SER A 1 974  ? 174.733 210.379 216.198 1.00 60.37  ? 957  SER B OG  1 
ATOM   7500  N N   . LEU A 1 975  ? 177.009 213.549 213.702 1.00 59.92  ? 958  LEU B N   1 
ATOM   7501  C CA  . LEU A 1 975  ? 178.229 214.243 213.313 1.00 59.92  ? 958  LEU B CA  1 
ATOM   7502  C C   . LEU A 1 975  ? 178.258 215.647 213.904 1.00 59.92  ? 958  LEU B C   1 
ATOM   7503  O O   . LEU A 1 975  ? 177.257 216.368 213.882 1.00 59.92  ? 958  LEU B O   1 
ATOM   7504  C CB  . LEU A 1 975  ? 178.339 214.314 211.792 1.00 59.92  ? 958  LEU B CB  1 
ATOM   7505  C CG  . LEU A 1 975  ? 178.259 212.989 211.036 1.00 59.92  ? 958  LEU B CG  1 
ATOM   7506  C CD1 . LEU A 1 975  ? 178.189 213.236 209.542 1.00 59.92  ? 958  LEU B CD1 1 
ATOM   7507  C CD2 . LEU A 1 975  ? 179.438 212.104 211.378 1.00 59.92  ? 958  LEU B CD2 1 
ATOM   7508  N N   . ASN A 1 976  ? 179.421 216.031 214.430 1.00 61.48  ? 959  ASN B N   1 
ATOM   7509  C CA  . ASN A 1 976  ? 179.626 217.346 215.038 1.00 61.48  ? 959  ASN B CA  1 
ATOM   7510  C C   . ASN A 1 976  ? 178.599 217.613 216.136 1.00 61.48  ? 959  ASN B C   1 
ATOM   7511  O O   . ASN A 1 976  ? 177.945 218.657 216.174 1.00 61.48  ? 959  ASN B O   1 
ATOM   7512  C CB  . ASN A 1 976  ? 179.598 218.450 213.981 1.00 61.48  ? 959  ASN B CB  1 
ATOM   7513  C CG  . ASN A 1 976  ? 180.373 219.680 214.405 1.00 61.48  ? 959  ASN B CG  1 
ATOM   7514  O OD1 . ASN A 1 976  ? 180.300 220.107 215.556 1.00 61.48  ? 959  ASN B OD1 1 
ATOM   7515  N ND2 . ASN A 1 976  ? 181.121 220.257 213.474 1.00 61.48  ? 959  ASN B ND2 1 
ATOM   7516  N N   . ASN A 1 977  ? 178.457 216.645 217.038 1.00 62.34  ? 960  ASN B N   1 
ATOM   7517  C CA  . ASN A 1 977  ? 177.519 216.745 218.153 1.00 62.34  ? 960  ASN B CA  1 
ATOM   7518  C C   . ASN A 1 977  ? 178.199 216.189 219.395 1.00 62.34  ? 960  ASN B C   1 
ATOM   7519  O O   . ASN A 1 977  ? 178.444 214.983 219.480 1.00 62.34  ? 960  ASN B O   1 
ATOM   7520  C CB  . ASN A 1 977  ? 176.227 215.989 217.857 1.00 62.34  ? 960  ASN B CB  1 
ATOM   7521  C CG  . ASN A 1 977  ? 175.230 216.088 218.982 1.00 62.34  ? 960  ASN B CG  1 
ATOM   7522  O OD1 . ASN A 1 977  ? 174.565 215.114 219.323 1.00 62.34  ? 960  ASN B OD1 1 
ATOM   7523  N ND2 . ASN A 1 977  ? 175.116 217.272 219.567 1.00 62.34  ? 960  ASN B ND2 1 
ATOM   7524  N N   . GLU A 1 978  ? 178.498 217.059 220.353 1.00 63.09  ? 961  GLU B N   1 
ATOM   7525  C CA  . GLU A 1 978  ? 179.182 216.670 221.579 1.00 63.09  ? 961  GLU B CA  1 
ATOM   7526  C C   . GLU A 1 978  ? 178.179 216.649 222.724 1.00 63.09  ? 961  GLU B C   1 
ATOM   7527  O O   . GLU A 1 978  ? 177.534 217.664 223.005 1.00 63.09  ? 961  GLU B O   1 
ATOM   7528  C CB  . GLU A 1 978  ? 180.330 217.629 221.887 1.00 63.09  ? 961  GLU B CB  1 
ATOM   7529  C CG  . GLU A 1 978  ? 180.847 217.537 223.309 1.00 63.09  ? 961  GLU B CG  1 
ATOM   7530  C CD  . GLU A 1 978  ? 181.820 218.647 223.646 1.00 63.09  ? 961  GLU B CD  1 
ATOM   7531  O OE1 . GLU A 1 978  ? 182.153 219.440 222.741 1.00 63.09  ? 961  GLU B OE1 1 
ATOM   7532  O OE2 . GLU A 1 978  ? 182.253 218.727 224.815 1.00 63.09  ? 961  GLU B OE2 1 
ATOM   7533  N N   . TYR A 1 979  ? 178.052 215.502 223.384 1.00 59.11  ? 962  TYR B N   1 
ATOM   7534  C CA  . TYR A 1 979  ? 177.127 215.352 224.497 1.00 59.11  ? 962  TYR B CA  1 
ATOM   7535  C C   . TYR A 1 979  ? 177.874 214.840 225.717 1.00 59.11  ? 962  TYR B C   1 
ATOM   7536  O O   . TYR A 1 979  ? 178.660 213.895 225.617 1.00 59.11  ? 962  TYR B O   1 
ATOM   7537  C CB  . TYR A 1 979  ? 175.969 214.412 224.142 1.00 59.11  ? 962  TYR B CB  1 
ATOM   7538  C CG  . TYR A 1 979  ? 176.372 213.039 223.658 1.00 59.11  ? 962  TYR B CG  1 
ATOM   7539  C CD1 . TYR A 1 979  ? 176.584 212.791 222.313 1.00 59.11  ? 962  TYR B CD1 1 
ATOM   7540  C CD2 . TYR A 1 979  ? 176.511 211.985 224.544 1.00 59.11  ? 962  TYR B CD2 1 
ATOM   7541  C CE1 . TYR A 1 979  ? 176.941 211.540 221.868 1.00 59.11  ? 962  TYR B CE1 1 
ATOM   7542  C CE2 . TYR A 1 979  ? 176.869 210.731 224.109 1.00 59.11  ? 962  TYR B CE2 1 
ATOM   7543  C CZ  . TYR A 1 979  ? 177.082 210.513 222.771 1.00 59.11  ? 962  TYR B CZ  1 
ATOM   7544  O OH  . TYR A 1 979  ? 177.439 209.259 222.337 1.00 59.11  ? 962  TYR B OH  1 
ATOM   7545  N N   . THR A 1 980  ? 177.632 215.473 226.859 1.00 59.49  ? 963  THR B N   1 
ATOM   7546  C CA  . THR A 1 980  ? 178.260 215.057 228.104 1.00 59.49  ? 963  THR B CA  1 
ATOM   7547  C C   . THR A 1 980  ? 177.677 213.730 228.569 1.00 59.49  ? 963  THR B C   1 
ATOM   7548  O O   . THR A 1 980  ? 176.459 213.539 228.550 1.00 59.49  ? 963  THR B O   1 
ATOM   7549  C CB  . THR A 1 980  ? 178.048 216.125 229.173 1.00 59.49  ? 963  THR B CB  1 
ATOM   7550  O OG1 . THR A 1 980  ? 178.764 217.312 228.815 1.00 59.49  ? 963  THR B OG1 1 
ATOM   7551  C CG2 . THR A 1 980  ? 178.532 215.635 230.521 1.00 59.49  ? 963  THR B CG2 1 
ATOM   7552  N N   . ILE A 1 981  ? 178.542 212.809 228.985 1.00 69.60  ? 964  ILE B N   1 
ATOM   7553  C CA  . ILE A 1 981  ? 178.089 211.565 229.590 1.00 69.60  ? 964  ILE B CA  1 
ATOM   7554  C C   . ILE A 1 981  ? 178.428 211.472 231.070 1.00 69.60  ? 964  ILE B C   1 
ATOM   7555  O O   . ILE A 1 981  ? 177.787 210.684 231.782 1.00 69.60  ? 964  ILE B O   1 
ATOM   7556  C CB  . ILE A 1 981  ? 178.634 210.333 228.842 1.00 69.60  ? 964  ILE B CB  1 
ATOM   7557  C CG1 . ILE A 1 981  ? 180.119 210.138 229.129 1.00 69.60  ? 964  ILE B CG1 1 
ATOM   7558  C CG2 . ILE A 1 981  ? 178.389 210.466 227.359 1.00 69.60  ? 964  ILE B CG2 1 
ATOM   7559  C CD1 . ILE A 1 981  ? 180.575 208.711 228.995 1.00 69.60  ? 964  ILE B CD1 1 
ATOM   7560  N N   . ILE A 1 982  ? 179.409 212.228 231.558 1.00 69.60  ? 965  ILE B N   1 
ATOM   7561  C CA  . ILE A 1 982  ? 179.682 212.334 232.989 1.00 69.60  ? 965  ILE B CA  1 
ATOM   7562  C C   . ILE A 1 982  ? 179.957 213.795 233.305 1.00 69.60  ? 965  ILE B C   1 
ATOM   7563  O O   . ILE A 1 982  ? 180.793 214.424 232.650 1.00 69.60  ? 965  ILE B O   1 
ATOM   7564  C CB  . ILE A 1 982  ? 180.869 211.456 233.424 1.00 69.60  ? 965  ILE B CB  1 
ATOM   7565  C CG1 . ILE A 1 982  ? 180.508 209.977 233.318 1.00 69.60  ? 965  ILE B CG1 1 
ATOM   7566  C CG2 . ILE A 1 982  ? 181.283 211.793 234.837 1.00 69.60  ? 965  ILE B CG2 1 
ATOM   7567  C CD1 . ILE A 1 982  ? 181.564 209.060 233.857 1.00 69.60  ? 965  ILE B CD1 1 
ATOM   7568  N N   . ASN A 1 983  ? 179.272 214.333 234.307 1.00 65.08  ? 966  ASN B N   1 
ATOM   7569  C CA  . ASN A 1 983  ? 179.361 215.750 234.624 1.00 65.08  ? 966  ASN B CA  1 
ATOM   7570  C C   . ASN A 1 983  ? 179.642 215.939 236.106 1.00 65.08  ? 966  ASN B C   1 
ATOM   7571  O O   . ASN A 1 983  ? 179.021 215.294 236.953 1.00 65.08  ? 966  ASN B O   1 
ATOM   7572  C CB  . ASN A 1 983  ? 178.069 216.475 234.242 1.00 65.08  ? 966  ASN B CB  1 
ATOM   7573  C CG  . ASN A 1 983  ? 178.204 217.979 234.304 1.00 65.08  ? 966  ASN B CG  1 
ATOM   7574  O OD1 . ASN A 1 983  ? 179.209 218.505 234.779 1.00 65.08  ? 966  ASN B OD1 1 
ATOM   7575  N ND2 . ASN A 1 983  ? 177.187 218.682 233.827 1.00 65.08  ? 966  ASN B ND2 1 
ATOM   7576  N N   . CYS A 1 984  ? 180.587 216.825 236.412 1.00 68.88  ? 967  CYS B N   1 
ATOM   7577  C CA  . CYS A 1 984  ? 180.902 217.206 237.784 1.00 68.88  ? 967  CYS B CA  1 
ATOM   7578  C C   . CYS A 1 984  ? 181.158 218.701 237.868 1.00 68.88  ? 967  CYS B C   1 
ATOM   7579  O O   . CYS A 1 984  ? 182.073 219.155 238.561 1.00 68.88  ? 967  CYS B O   1 
ATOM   7580  C CB  . CYS A 1 984  ? 182.103 216.429 238.315 1.00 68.88  ? 967  CYS B CB  1 
ATOM   7581  S SG  . CYS A 1 984  ? 182.229 216.393 240.114 1.00 68.88  ? 967  CYS B SG  1 
ATOM   7582  N N   . MET A 1 985  ? 180.355 219.486 237.161 1.00 73.50  ? 968  MET B N   1 
ATOM   7583  C CA  . MET A 1 985  ? 180.559 220.922 237.046 1.00 73.50  ? 968  MET B CA  1 
ATOM   7584  C C   . MET A 1 985  ? 179.456 221.661 237.786 1.00 73.50  ? 968  MET B C   1 
ATOM   7585  O O   . MET A 1 985  ? 178.279 221.307 237.670 1.00 73.50  ? 968  MET B O   1 
ATOM   7586  C CB  . MET A 1 985  ? 180.582 221.355 235.579 1.00 73.50  ? 968  MET B CB  1 
ATOM   7587  C CG  . MET A 1 985  ? 181.852 220.987 234.836 1.00 73.50  ? 968  MET B CG  1 
ATOM   7588  S SD  . MET A 1 985  ? 181.882 221.622 233.150 1.00 73.50  ? 968  MET B SD  1 
ATOM   7589  C CE  . MET A 1 985  ? 180.709 222.967 233.272 1.00 73.50  ? 968  MET B CE  1 
ATOM   7590  N N   . GLU A 1 986  ? 179.838 222.681 238.547 1.00 82.40  ? 969  GLU B N   1 
ATOM   7591  C CA  . GLU A 1 986  ? 178.880 223.593 239.150 1.00 82.40  ? 969  GLU B CA  1 
ATOM   7592  C C   . GLU A 1 986  ? 179.399 225.014 238.992 1.00 82.40  ? 969  GLU B C   1 
ATOM   7593  O O   . GLU A 1 986  ? 180.603 225.259 239.109 1.00 82.40  ? 969  GLU B O   1 
ATOM   7594  C CB  . GLU A 1 986  ? 178.627 223.256 240.626 1.00 82.40  ? 969  GLU B CB  1 
ATOM   7595  C CG  . GLU A 1 986  ? 179.711 223.700 241.588 1.00 82.40  ? 969  GLU B CG  1 
ATOM   7596  C CD  . GLU A 1 986  ? 179.358 223.407 243.033 1.00 82.40  ? 969  GLU B CD  1 
ATOM   7597  O OE1 . GLU A 1 986  ? 179.020 222.245 243.341 1.00 82.40  ? 969  GLU B OE1 1 
ATOM   7598  O OE2 . GLU A 1 986  ? 179.416 224.340 243.861 1.00 82.40  ? 969  GLU B OE2 1 
ATOM   7599  N N   . ASN A 1 987  ? 178.482 225.939 238.705 1.00 83.50  ? 970  ASN B N   1 
ATOM   7600  C CA  . ASN A 1 987  ? 178.830 227.327 238.399 1.00 83.50  ? 970  ASN B CA  1 
ATOM   7601  C C   . ASN A 1 987  ? 179.832 227.401 237.248 1.00 83.50  ? 970  ASN B C   1 
ATOM   7602  O O   . ASN A 1 987  ? 180.771 228.199 237.262 1.00 83.50  ? 970  ASN B O   1 
ATOM   7603  C CB  . ASN A 1 987  ? 179.362 228.050 239.637 1.00 83.50  ? 970  ASN B CB  1 
ATOM   7604  C CG  . ASN A 1 987  ? 179.243 229.557 239.527 1.00 83.50  ? 970  ASN B CG  1 
ATOM   7605  O OD1 . ASN A 1 987  ? 178.801 230.084 238.507 1.00 83.50  ? 970  ASN B OD1 1 
ATOM   7606  N ND2 . ASN A 1 987  ? 179.639 230.260 240.582 1.00 83.50  ? 970  ASN B ND2 1 
ATOM   7607  N N   . ASN A 1 988  ? 179.614 226.564 236.234 1.00 83.03  ? 971  ASN B N   1 
ATOM   7608  C CA  . ASN A 1 988  ? 180.465 226.488 235.046 1.00 83.03  ? 971  ASN B CA  1 
ATOM   7609  C C   . ASN A 1 988  ? 181.933 226.290 235.426 1.00 83.03  ? 971  ASN B C   1 
ATOM   7610  O O   . ASN A 1 988  ? 182.805 227.092 235.090 1.00 83.03  ? 971  ASN B O   1 
ATOM   7611  C CB  . ASN A 1 988  ? 180.296 227.728 234.163 1.00 83.03  ? 971  ASN B CB  1 
ATOM   7612  C CG  . ASN A 1 988  ? 178.857 228.201 234.079 1.00 83.03  ? 971  ASN B CG  1 
ATOM   7613  O OD1 . ASN A 1 988  ? 178.166 228.325 235.088 1.00 83.03  ? 971  ASN B OD1 1 
ATOM   7614  N ND2 . ASN A 1 988  ? 178.401 228.476 232.862 1.00 83.03  ? 971  ASN B ND2 1 
ATOM   7615  N N   . SER A 1 989  ? 182.197 225.195 236.136 1.00 77.67  ? 972  SER B N   1 
ATOM   7616  C CA  . SER A 1 989  ? 183.554 224.895 236.575 1.00 77.67  ? 972  SER B CA  1 
ATOM   7617  C C   . SER A 1 989  ? 183.688 223.444 237.011 1.00 77.67  ? 972  SER B C   1 
ATOM   7618  O O   . SER A 1 989  ? 182.890 222.959 237.816 1.00 77.67  ? 972  SER B O   1 
ATOM   7619  C CB  . SER A 1 989  ? 183.958 225.818 237.722 1.00 77.67  ? 972  SER B CB  1 
ATOM   7620  O OG  . SER A 1 989  ? 184.601 226.976 237.230 1.00 77.67  ? 972  SER B OG  1 
ATOM   7621  N N   . GLY A 1 990  ? 184.690 222.751 236.498 1.00 69.57  ? 973  GLY B N   1 
ATOM   7622  C CA  . GLY A 1 990  ? 184.947 221.385 236.884 1.00 69.57  ? 973  GLY B CA  1 
ATOM   7623  C C   . GLY A 1 990  ? 185.366 220.564 235.689 1.00 69.57  ? 973  GLY B C   1 
ATOM   7624  O O   . GLY A 1 990  ? 185.804 221.095 234.671 1.00 69.57  ? 973  GLY B O   1 
ATOM   7625  N N   . TRP A 1 991  ? 185.223 219.252 235.825 1.00 66.87  ? 974  TRP B N   1 
ATOM   7626  C CA  . TRP A 1 991  ? 185.624 218.303 234.801 1.00 66.87  ? 974  TRP B CA  1 
ATOM   7627  C C   . TRP A 1 991  ? 184.405 217.557 234.287 1.00 66.87  ? 974  TRP B C   1 
ATOM   7628  O O   . TRP A 1 991  ? 183.500 217.227 235.056 1.00 66.87  ? 974  TRP B O   1 
ATOM   7629  C CB  . TRP A 1 991  ? 186.640 217.303 235.342 1.00 66.87  ? 974  TRP B CB  1 
ATOM   7630  C CG  . TRP A 1 991  ? 186.187 216.583 236.569 1.00 66.87  ? 974  TRP B CG  1 
ATOM   7631  C CD1 . TRP A 1 991  ? 186.401 216.958 237.858 1.00 66.87  ? 974  TRP B CD1 1 
ATOM   7632  C CD2 . TRP A 1 991  ? 185.450 215.356 236.624 1.00 66.87  ? 974  TRP B CD2 1 
ATOM   7633  N NE1 . TRP A 1 991  ? 185.841 216.045 238.716 1.00 66.87  ? 974  TRP B NE1 1 
ATOM   7634  C CE2 . TRP A 1 991  ? 185.251 215.051 237.981 1.00 66.87  ? 974  TRP B CE2 1 
ATOM   7635  C CE3 . TRP A 1 991  ? 184.940 214.488 235.659 1.00 66.87  ? 974  TRP B CE3 1 
ATOM   7636  C CZ2 . TRP A 1 991  ? 184.564 213.918 238.395 1.00 66.87  ? 974  TRP B CZ2 1 
ATOM   7637  C CZ3 . TRP A 1 991  ? 184.260 213.365 236.074 1.00 66.87  ? 974  TRP B CZ3 1 
ATOM   7638  C CH2 . TRP A 1 991  ? 184.077 213.089 237.428 1.00 66.87  ? 974  TRP B CH2 1 
ATOM   7639  N N   . LYS A 1 992  ? 184.389 217.287 232.987 1.00 69.60  ? 975  LYS B N   1 
ATOM   7640  C CA  . LYS A 1 992  ? 183.307 216.515 232.397 1.00 69.60  ? 975  LYS B CA  1 
ATOM   7641  C C   . LYS A 1 992  ? 183.840 215.617 231.293 1.00 69.60  ? 975  LYS B C   1 
ATOM   7642  O O   . LYS A 1 992  ? 184.712 216.016 230.516 1.00 69.60  ? 975  LYS B O   1 
ATOM   7643  C CB  . LYS A 1 992  ? 182.199 217.423 231.855 1.00 69.60  ? 975  LYS B CB  1 
ATOM   7644  C CG  . LYS A 1 992  ? 182.650 218.436 230.831 1.00 69.60  ? 975  LYS B CG  1 
ATOM   7645  C CD  . LYS A 1 992  ? 181.462 219.035 230.105 1.00 69.60  ? 975  LYS B CD  1 
ATOM   7646  C CE  . LYS A 1 992  ? 181.868 219.572 228.748 1.00 69.60  ? 975  LYS B CE  1 
ATOM   7647  N NZ  . LYS A 1 992  ? 180.689 219.861 227.892 1.00 69.60  ? 975  LYS B NZ  1 
ATOM   7648  N N   . VAL A 1 993  ? 183.311 214.402 231.237 1.00 69.60  ? 976  VAL B N   1 
ATOM   7649  C CA  . VAL A 1 993  ? 183.626 213.444 230.186 1.00 69.60  ? 976  VAL B CA  1 
ATOM   7650  C C   . VAL A 1 993  ? 182.484 213.467 229.186 1.00 69.60  ? 976  VAL B C   1 
ATOM   7651  O O   . VAL A 1 993  ? 181.338 213.161 229.536 1.00 69.60  ? 976  VAL B O   1 
ATOM   7652  C CB  . VAL A 1 993  ? 183.824 212.030 230.749 1.00 69.60  ? 976  VAL B CB  1 
ATOM   7653  C CG1 . VAL A 1 993  ? 184.238 211.079 229.645 1.00 69.60  ? 976  VAL B CG1 1 
ATOM   7654  C CG2 . VAL A 1 993  ? 184.843 212.042 231.860 1.00 69.60  ? 976  VAL B CG2 1 
ATOM   7655  N N   . SER A 1 994  ? 182.792 213.825 227.946 1.00 58.83  ? 977  SER B N   1 
ATOM   7656  C CA  . SER A 1 994  ? 181.802 213.920 226.890 1.00 58.83  ? 977  SER B CA  1 
ATOM   7657  C C   . SER A 1 994  ? 182.196 213.024 225.724 1.00 58.83  ? 977  SER B C   1 
ATOM   7658  O O   . SER A 1 994  ? 183.298 212.475 225.669 1.00 58.83  ? 977  SER B O   1 
ATOM   7659  C CB  . SER A 1 994  ? 181.635 215.370 226.424 1.00 58.83  ? 977  SER B CB  1 
ATOM   7660  O OG  . SER A 1 994  ? 182.891 215.980 226.204 1.00 58.83  ? 977  SER B OG  1 
ATOM   7661  N N   . LEU A 1 995  ? 181.273 212.887 224.782 1.00 54.39  ? 978  LEU B N   1 
ATOM   7662  C CA  . LEU A 1 995  ? 181.444 212.009 223.640 1.00 54.39  ? 978  LEU B CA  1 
ATOM   7663  C C   . LEU A 1 995  ? 181.155 212.779 222.362 1.00 54.39  ? 978  LEU B C   1 
ATOM   7664  O O   . LEU A 1 995  ? 180.555 213.854 222.382 1.00 54.39  ? 978  LEU B O   1 
ATOM   7665  C CB  . LEU A 1 995  ? 180.522 210.795 223.731 1.00 54.39  ? 978  LEU B CB  1 
ATOM   7666  C CG  . LEU A 1 995  ? 181.120 209.487 224.229 1.00 54.39  ? 978  LEU B CG  1 
ATOM   7667  C CD1 . LEU A 1 995  ? 181.605 209.643 225.645 1.00 54.39  ? 978  LEU B CD1 1 
ATOM   7668  C CD2 . LEU A 1 995  ? 180.068 208.405 224.150 1.00 54.39  ? 978  LEU B CD2 1 
ATOM   7669  N N   . ASN A 1 996  ? 181.595 212.214 221.246 1.00 56.25  ? 979  ASN B N   1 
ATOM   7670  C CA  . ASN A 1 996  ? 181.299 212.770 219.934 1.00 56.25  ? 979  ASN B CA  1 
ATOM   7671  C C   . ASN A 1 996  ? 181.517 211.672 218.904 1.00 56.25  ? 979  ASN B C   1 
ATOM   7672  O O   . ASN A 1 996  ? 181.903 210.549 219.239 1.00 56.25  ? 979  ASN B O   1 
ATOM   7673  C CB  . ASN A 1 996  ? 182.157 213.999 219.641 1.00 56.25  ? 979  ASN B CB  1 
ATOM   7674  C CG  . ASN A 1 996  ? 181.517 214.923 218.634 1.00 56.25  ? 979  ASN B CG  1 
ATOM   7675  O OD1 . ASN A 1 996  ? 180.703 214.497 217.820 1.00 56.25  ? 979  ASN B OD1 1 
ATOM   7676  N ND2 . ASN A 1 996  ? 181.886 216.195 218.679 1.00 56.25  ? 979  ASN B ND2 1 
ATOM   7677  N N   . TYR A 1 997  ? 181.297 212.015 217.636 1.00 54.99  ? 980  TYR B N   1 
ATOM   7678  C CA  . TYR A 1 997  ? 181.375 211.019 216.577 1.00 54.99  ? 980  TYR B CA  1 
ATOM   7679  C C   . TYR A 1 997  ? 182.785 210.453 216.510 1.00 54.99  ? 980  TYR B C   1 
ATOM   7680  O O   . TYR A 1 997  ? 183.707 211.109 216.017 1.00 54.99  ? 980  TYR B O   1 
ATOM   7681  C CB  . TYR A 1 997  ? 180.967 211.631 215.237 1.00 54.99  ? 980  TYR B CB  1 
ATOM   7682  C CG  . TYR A 1 997  ? 181.301 210.774 214.042 1.00 54.99  ? 980  TYR B CG  1 
ATOM   7683  C CD1 . TYR A 1 997  ? 180.559 209.644 213.746 1.00 54.99  ? 980  TYR B CD1 1 
ATOM   7684  C CD2 . TYR A 1 997  ? 182.354 211.102 213.203 1.00 54.99  ? 980  TYR B CD2 1 
ATOM   7685  C CE1 . TYR A 1 997  ? 180.861 208.860 212.656 1.00 54.99  ? 980  TYR B CE1 1 
ATOM   7686  C CE2 . TYR A 1 997  ? 182.661 210.324 212.111 1.00 54.99  ? 980  TYR B CE2 1 
ATOM   7687  C CZ  . TYR A 1 997  ? 181.913 209.205 211.843 1.00 54.99  ? 980  TYR B CZ  1 
ATOM   7688  O OH  . TYR A 1 997  ? 182.219 208.427 210.754 1.00 54.99  ? 980  TYR B OH  1 
ATOM   7689  N N   . GLY A 1 998  ? 182.953 209.234 217.013 1.00 55.31  ? 981  GLY B N   1 
ATOM   7690  C CA  . GLY A 1 998  ? 184.265 208.619 217.085 1.00 55.31  ? 981  GLY B CA  1 
ATOM   7691  C C   . GLY A 1 998  ? 185.248 209.349 217.971 1.00 55.31  ? 981  GLY B C   1 
ATOM   7692  O O   . GLY A 1 998  ? 186.447 209.348 217.678 1.00 55.31  ? 981  GLY B O   1 
ATOM   7693  N N   . GLU A 1 999  ? 184.780 209.968 219.057 1.00 57.63  ? 982  GLU B N   1 
ATOM   7694  C CA  . GLU A 1 999  ? 185.658 210.729 219.936 1.00 57.63  ? 982  GLU B CA  1 
ATOM   7695  C C   . GLU A 1 999  ? 185.218 210.600 221.384 1.00 57.63  ? 982  GLU B C   1 
ATOM   7696  O O   . GLU A 1 999  ? 184.023 210.661 221.683 1.00 57.63  ? 982  GLU B O   1 
ATOM   7697  C CB  . GLU A 1 999  ? 185.678 212.215 219.569 1.00 57.63  ? 982  GLU B CB  1 
ATOM   7698  C CG  . GLU A 1 999  ? 186.441 212.553 218.316 1.00 57.63  ? 982  GLU B CG  1 
ATOM   7699  C CD  . GLU A 1 999  ? 186.645 214.040 218.165 1.00 57.63  ? 982  GLU B CD  1 
ATOM   7700  O OE1 . GLU A 1 999  ? 186.045 214.802 218.950 1.00 57.63  ? 982  GLU B OE1 1 
ATOM   7701  O OE2 . GLU A 1 999  ? 187.403 214.450 217.263 1.00 57.63  ? 982  GLU B OE2 1 
ATOM   7702  N N   . ILE A 1 1000 ? 186.193 210.458 222.278 1.00 55.08  ? 983  ILE B N   1 
ATOM   7703  C CA  . ILE A 1 1000 ? 185.979 210.564 223.719 1.00 55.08  ? 983  ILE B CA  1 
ATOM   7704  C C   . ILE A 1 1000 ? 186.761 211.771 224.207 1.00 55.08  ? 983  ILE B C   1 
ATOM   7705  O O   . ILE A 1 1000 ? 187.985 211.827 224.040 1.00 55.08  ? 983  ILE B O   1 
ATOM   7706  C CB  . ILE A 1 1000 ? 186.420 209.297 224.465 1.00 55.08  ? 983  ILE B CB  1 
ATOM   7707  C CG1 . ILE A 1 1000 ? 185.638 208.083 223.971 1.00 55.08  ? 983  ILE B CG1 1 
ATOM   7708  C CG2 . ILE A 1 1000 ? 186.234 209.478 225.955 1.00 55.08  ? 983  ILE B CG2 1 
ATOM   7709  C CD1 . ILE A 1 1000 ? 185.908 206.832 224.763 1.00 55.08  ? 983  ILE B CD1 1 
ATOM   7710  N N   . ILE A 1 1001 ? 186.069 212.730 224.816 1.00 60.31  ? 984  ILE B N   1 
ATOM   7711  C CA  . ILE A 1 1001 ? 186.655 214.011 225.180 1.00 60.31  ? 984  ILE B CA  1 
ATOM   7712  C C   . ILE A 1 1001 ? 186.624 214.157 226.692 1.00 60.31  ? 984  ILE B C   1 
ATOM   7713  O O   . ILE A 1 1001 ? 185.621 213.834 227.335 1.00 60.31  ? 984  ILE B O   1 
ATOM   7714  C CB  . ILE A 1 1001 ? 185.905 215.179 224.509 1.00 60.31  ? 984  ILE B CB  1 
ATOM   7715  C CG1 . ILE A 1 1001 ? 185.913 215.019 222.993 1.00 60.31  ? 984  ILE B CG1 1 
ATOM   7716  C CG2 . ILE A 1 1001 ? 186.516 216.507 224.900 1.00 60.31  ? 984  ILE B CG2 1 
ATOM   7717  C CD1 . ILE A 1 1001 ? 184.755 215.703 222.313 1.00 60.31  ? 984  ILE B CD1 1 
ATOM   7718  N N   . TRP A 1 1002 ? 187.725 214.636 227.259 1.00 69.60  ? 985  TRP B N   1 
ATOM   7719  C CA  . TRP A 1 1002 ? 187.801 215.007 228.662 1.00 69.60  ? 985  TRP B CA  1 
ATOM   7720  C C   . TRP A 1 1002 ? 188.031 216.508 228.738 1.00 69.60  ? 985  TRP B C   1 
ATOM   7721  O O   . TRP A 1 1002 ? 188.977 217.020 228.130 1.00 69.60  ? 985  TRP B O   1 
ATOM   7722  C CB  . TRP A 1 1002 ? 188.929 214.249 229.363 1.00 69.60  ? 985  TRP B CB  1 
ATOM   7723  C CG  . TRP A 1 1002 ? 189.323 214.820 230.682 1.00 69.60  ? 985  TRP B CG  1 
ATOM   7724  C CD1 . TRP A 1 1002 ? 190.232 215.808 230.910 1.00 69.60  ? 985  TRP B CD1 1 
ATOM   7725  C CD2 . TRP A 1 1002 ? 188.824 214.430 231.962 1.00 69.60  ? 985  TRP B CD2 1 
ATOM   7726  N NE1 . TRP A 1 1002 ? 190.326 216.063 232.255 1.00 69.60  ? 985  TRP B NE1 1 
ATOM   7727  C CE2 . TRP A 1 1002 ? 189.470 215.228 232.922 1.00 69.60  ? 985  TRP B CE2 1 
ATOM   7728  C CE3 . TRP A 1 1002 ? 187.892 213.485 232.389 1.00 69.60  ? 985  TRP B CE3 1 
ATOM   7729  C CZ2 . TRP A 1 1002 ? 189.212 215.109 234.282 1.00 69.60  ? 985  TRP B CZ2 1 
ATOM   7730  C CZ3 . TRP A 1 1002 ? 187.637 213.368 233.736 1.00 69.60  ? 985  TRP B CZ3 1 
ATOM   7731  C CH2 . TRP A 1 1002 ? 188.294 214.174 234.668 1.00 69.60  ? 985  TRP B CH2 1 
ATOM   7732  N N   . THR A 1 1003 ? 187.177 217.210 229.478 1.00 73.11  ? 986  THR B N   1 
ATOM   7733  C CA  . THR A 1 1003 ? 187.194 218.664 229.519 1.00 73.11  ? 986  THR B CA  1 
ATOM   7734  C C   . THR A 1 1003 ? 187.392 219.136 230.948 1.00 73.11  ? 986  THR B C   1 
ATOM   7735  O O   . THR A 1 1003 ? 186.716 218.654 231.861 1.00 73.11  ? 986  THR B O   1 
ATOM   7736  C CB  . THR A 1 1003 ? 185.894 219.239 228.960 1.00 73.11  ? 986  THR B CB  1 
ATOM   7737  O OG1 . THR A 1 1003 ? 185.736 218.824 227.599 1.00 73.11  ? 986  THR B OG1 1 
ATOM   7738  C CG2 . THR A 1 1003 ? 185.911 220.750 229.024 1.00 73.11  ? 986  THR B CG2 1 
ATOM   7739  N N   . LEU A 1 1004 ? 188.310 220.082 231.134 1.00 73.08  ? 987  LEU B N   1 
ATOM   7740  C CA  . LEU A 1 1004 ? 188.569 220.714 232.422 1.00 73.08  ? 987  LEU B CA  1 
ATOM   7741  C C   . LEU A 1 1004 ? 188.394 222.214 232.249 1.00 73.08  ? 987  LEU B C   1 
ATOM   7742  O O   . LEU A 1 1004 ? 189.064 222.821 231.408 1.00 73.08  ? 987  LEU B O   1 
ATOM   7743  C CB  . LEU A 1 1004 ? 189.979 220.389 232.913 1.00 73.08  ? 987  LEU B CB  1 
ATOM   7744  C CG  . LEU A 1 1004 ? 190.207 220.232 234.411 1.00 73.08  ? 987  LEU B CG  1 
ATOM   7745  C CD1 . LEU A 1 1004 ? 189.777 218.858 234.853 1.00 73.08  ? 987  LEU B CD1 1 
ATOM   7746  C CD2 . LEU A 1 1004 ? 191.667 220.446 234.737 1.00 73.08  ? 987  LEU B CD2 1 
ATOM   7747  N N   . GLN A 1 1005 ? 187.508 222.815 233.040 1.00 75.21  ? 988  GLN B N   1 
ATOM   7748  C CA  . GLN A 1 1005 ? 187.181 224.223 232.879 1.00 75.21  ? 988  GLN B CA  1 
ATOM   7749  C C   . GLN A 1 1005 ? 187.192 224.917 234.231 1.00 75.21  ? 988  GLN B C   1 
ATOM   7750  O O   . GLN A 1 1005 ? 186.748 224.346 235.230 1.00 75.21  ? 988  GLN B O   1 
ATOM   7751  C CB  . GLN A 1 1005 ? 185.816 224.391 232.210 1.00 75.21  ? 988  GLN B CB  1 
ATOM   7752  C CG  . GLN A 1 1005 ? 185.356 225.827 232.090 1.00 75.21  ? 988  GLN B CG  1 
ATOM   7753  C CD  . GLN A 1 1005 ? 184.004 225.950 231.427 1.00 75.21  ? 988  GLN B CD  1 
ATOM   7754  O OE1 . GLN A 1 1005 ? 183.421 224.958 230.994 1.00 75.21  ? 988  GLN B OE1 1 
ATOM   7755  N NE2 . GLN A 1 1005 ? 183.496 227.173 231.343 1.00 75.21  ? 988  GLN B NE2 1 
ATOM   7756  N N   . ASP A 1 1006 ? 187.697 226.147 234.260 1.00 82.59  ? 989  ASP B N   1 
ATOM   7757  C CA  . ASP A 1 1006 ? 187.768 226.945 235.476 1.00 82.59  ? 989  ASP B CA  1 
ATOM   7758  C C   . ASP A 1 1006 ? 186.736 228.068 235.431 1.00 82.59  ? 989  ASP B C   1 
ATOM   7759  O O   . ASP A 1 1006 ? 185.994 228.230 234.458 1.00 82.59  ? 989  ASP B O   1 
ATOM   7760  C CB  . ASP A 1 1006 ? 189.179 227.502 235.678 1.00 82.59  ? 989  ASP B CB  1 
ATOM   7761  C CG  . ASP A 1 1006 ? 189.709 228.217 234.452 1.00 82.59  ? 989  ASP B CG  1 
ATOM   7762  O OD1 . ASP A 1 1006 ? 188.898 228.641 233.604 1.00 82.59  ? 989  ASP B OD1 1 
ATOM   7763  O OD2 . ASP A 1 1006 ? 190.944 228.364 234.341 1.00 82.59  ? 989  ASP B OD2 1 
ATOM   7764  N N   . THR A 1 1007 ? 186.702 228.859 236.507 1.00 87.64  ? 990  THR B N   1 
ATOM   7765  C CA  . THR A 1 1007 ? 185.717 229.930 236.620 1.00 87.64  ? 990  THR B CA  1 
ATOM   7766  C C   . THR A 1 1007 ? 185.916 231.005 235.561 1.00 87.64  ? 990  THR B C   1 
ATOM   7767  O O   . THR A 1 1007 ? 184.939 231.601 235.096 1.00 87.64  ? 990  THR B O   1 
ATOM   7768  C CB  . THR A 1 1007 ? 185.775 230.557 238.011 1.00 87.64  ? 990  THR B CB  1 
ATOM   7769  O OG1 . THR A 1 1007 ? 187.140 230.812 238.363 1.00 87.64  ? 990  THR B OG1 1 
ATOM   7770  C CG2 . THR A 1 1007 ? 185.154 229.630 239.040 1.00 87.64  ? 990  THR B CG2 1 
ATOM   7771  N N   . GLN A 1 1008 ? 187.159 231.263 235.163 1.00 89.16  ? 991  GLN B N   1 
ATOM   7772  C CA  . GLN A 1 1008 ? 187.464 232.306 234.193 1.00 89.16  ? 991  GLN B CA  1 
ATOM   7773  C C   . GLN A 1 1008 ? 187.155 231.893 232.761 1.00 89.16  ? 991  GLN B C   1 
ATOM   7774  O O   . GLN A 1 1008 ? 187.637 232.547 231.830 1.00 89.16  ? 991  GLN B O   1 
ATOM   7775  C CB  . GLN A 1 1008 ? 188.934 232.717 234.307 1.00 89.16  ? 991  GLN B CB  1 
ATOM   7776  C CG  . GLN A 1 1008 ? 189.278 233.486 235.574 1.00 89.16  ? 991  GLN B CG  1 
ATOM   7777  C CD  . GLN A 1 1008 ? 189.484 232.583 236.775 1.00 89.16  ? 991  GLN B CD  1 
ATOM   7778  O OE1 . GLN A 1 1008 ? 189.204 231.387 236.724 1.00 89.16  ? 991  GLN B OE1 1 
ATOM   7779  N NE2 . GLN A 1 1008 ? 189.979 233.155 237.866 1.00 89.16  ? 991  GLN B NE2 1 
ATOM   7780  N N   . GLU A 1 1009 ? 186.380 230.825 232.571 1.00 88.94  ? 992  GLU B N   1 
ATOM   7781  C CA  . GLU A 1 1009 ? 185.936 230.289 231.288 1.00 88.94  ? 992  GLU B CA  1 
ATOM   7782  C C   . GLU A 1 1009 ? 187.064 229.666 230.477 1.00 88.94  ? 992  GLU B C   1 
ATOM   7783  O O   . GLU A 1 1009 ? 186.831 229.273 229.328 1.00 88.94  ? 992  GLU B O   1 
ATOM   7784  C CB  . GLU A 1 1009 ? 185.227 231.341 230.422 1.00 88.94  ? 992  GLU B CB  1 
ATOM   7785  C CG  . GLU A 1 1009 ? 183.802 231.639 230.852 1.00 88.94  ? 992  GLU B CG  1 
ATOM   7786  C CD  . GLU A 1 1009 ? 182.888 231.920 229.677 1.00 88.94  ? 992  GLU B CD  1 
ATOM   7787  O OE1 . GLU A 1 1009 ? 183.254 232.755 228.824 1.00 88.94  ? 992  GLU B OE1 1 
ATOM   7788  O OE2 . GLU A 1 1009 ? 181.803 231.306 229.606 1.00 88.94  ? 992  GLU B OE2 1 
ATOM   7789  N N   . ILE A 1 1010 ? 188.276 229.563 231.023 1.00 82.82  ? 993  ILE B N   1 
ATOM   7790  C CA  . ILE A 1 1010 ? 189.336 228.844 230.328 1.00 82.82  ? 993  ILE B CA  1 
ATOM   7791  C C   . ILE A 1 1010 ? 188.991 227.362 230.291 1.00 82.82  ? 993  ILE B C   1 
ATOM   7792  O O   . ILE A 1 1010 ? 188.391 226.813 231.223 1.00 82.82  ? 993  ILE B O   1 
ATOM   7793  C CB  . ILE A 1 1010 ? 190.711 229.075 230.983 1.00 82.82  ? 993  ILE B CB  1 
ATOM   7794  C CG1 . ILE A 1 1010 ? 190.801 230.446 231.664 1.00 82.82  ? 993  ILE B CG1 1 
ATOM   7795  C CG2 . ILE A 1 1010 ? 191.820 228.924 229.954 1.00 82.82  ? 993  ILE B CG2 1 
ATOM   7796  C CD1 . ILE A 1 1010 ? 190.502 231.631 230.754 1.00 82.82  ? 993  ILE B CD1 1 
ATOM   7797  N N   . LYS A 1 1011 ? 189.372 226.705 229.203 1.00 69.92  ? 994  LYS B N   1 
ATOM   7798  C CA  . LYS A 1 1011 ? 188.976 225.330 228.952 1.00 69.92  ? 994  LYS B CA  1 
ATOM   7799  C C   . LYS A 1 1011 ? 190.157 224.565 228.382 1.00 69.92  ? 994  LYS B C   1 
ATOM   7800  O O   . LYS A 1 1011 ? 190.881 225.081 227.528 1.00 69.92  ? 994  LYS B O   1 
ATOM   7801  C CB  . LYS A 1 1011 ? 187.795 225.281 227.978 1.00 69.92  ? 994  LYS B CB  1 
ATOM   7802  C CG  . LYS A 1 1011 ? 187.334 223.890 227.600 1.00 69.92  ? 994  LYS B CG  1 
ATOM   7803  C CD  . LYS A 1 1011 ? 185.848 223.886 227.286 1.00 69.92  ? 994  LYS B CD  1 
ATOM   7804  C CE  . LYS A 1 1011 ? 185.483 225.020 226.343 1.00 69.92  ? 994  LYS B CE  1 
ATOM   7805  N NZ  . LYS A 1 1011 ? 184.047 225.389 226.453 1.00 69.92  ? 994  LYS B NZ  1 
ATOM   7806  N N   . GLN A 1 1012 ? 190.358 223.340 228.859 1.00 64.17  ? 995  GLN B N   1 
ATOM   7807  C CA  . GLN A 1 1012 ? 191.395 222.476 228.316 1.00 64.17  ? 995  GLN B CA  1 
ATOM   7808  C C   . GLN A 1 1012 ? 190.791 221.109 228.038 1.00 64.17  ? 995  GLN B C   1 
ATOM   7809  O O   . GLN A 1 1012 ? 190.157 220.516 228.916 1.00 64.17  ? 995  GLN B O   1 
ATOM   7810  C CB  . GLN A 1 1012 ? 192.579 222.352 229.276 1.00 64.17  ? 995  GLN B CB  1 
ATOM   7811  C CG  . GLN A 1 1012 ? 193.783 221.525 228.788 1.00 64.17  ? 995  GLN B CG  1 
ATOM   7812  C CD  . GLN A 1 1012 ? 194.369 221.949 227.438 1.00 64.17  ? 995  GLN B CD  1 
ATOM   7813  O OE1 . GLN A 1 1012 ? 193.682 222.453 226.552 1.00 64.17  ? 995  GLN B OE1 1 
ATOM   7814  N NE2 . GLN A 1 1012 ? 195.672 221.762 227.298 1.00 64.17  ? 995  GLN B NE2 1 
ATOM   7815  N N   . ARG A 1 1013 ? 190.997 220.610 226.823 1.00 59.38  ? 996  ARG B N   1 
ATOM   7816  C CA  . ARG A 1 1013 ? 190.372 219.384 226.356 1.00 59.38  ? 996  ARG B CA  1 
ATOM   7817  C C   . ARG A 1 1013 ? 191.437 218.398 225.917 1.00 59.38  ? 996  ARG B C   1 
ATOM   7818  O O   . ARG A 1 1013 ? 192.383 218.769 225.218 1.00 59.38  ? 996  ARG B O   1 
ATOM   7819  C CB  . ARG A 1 1013 ? 189.436 219.658 225.181 1.00 59.38  ? 996  ARG B CB  1 
ATOM   7820  C CG  . ARG A 1 1013 ? 188.238 220.518 225.518 1.00 59.38  ? 996  ARG B CG  1 
ATOM   7821  C CD  . ARG A 1 1013 ? 187.606 221.091 224.261 1.00 59.38  ? 996  ARG B CD  1 
ATOM   7822  N NE  . ARG A 1 1013 ? 188.057 220.396 223.061 1.00 59.38  ? 996  ARG B NE  1 
ATOM   7823  C CZ  . ARG A 1 1013 ? 187.340 219.499 222.401 1.00 59.38  ? 996  ARG B CZ  1 
ATOM   7824  N NH1 . ARG A 1 1013 ? 186.125 219.159 222.797 1.00 59.38  ? 996  ARG B NH1 1 
ATOM   7825  N NH2 . ARG A 1 1013 ? 187.855 218.927 221.317 1.00 59.38  ? 996  ARG B NH2 1 
ATOM   7826  N N   . VAL A 1 1014 ? 191.282 217.142 226.320 1.00 58.12  ? 997  VAL B N   1 
ATOM   7827  C CA  . VAL A 1 1014 ? 192.094 216.051 225.793 1.00 58.12  ? 997  VAL B CA  1 
ATOM   7828  C C   . VAL A 1 1014 ? 191.155 215.055 225.122 1.00 58.12  ? 997  VAL B C   1 
ATOM   7829  O O   . VAL A 1 1014 ? 190.156 214.630 225.715 1.00 58.12  ? 997  VAL B O   1 
ATOM   7830  C CB  . VAL A 1 1014 ? 192.973 215.401 226.878 1.00 58.12  ? 997  VAL B CB  1 
ATOM   7831  C CG1 . VAL A 1 1014 ? 193.634 216.473 227.713 1.00 58.12  ? 997  VAL B CG1 1 
ATOM   7832  C CG2 . VAL A 1 1014 ? 192.178 214.496 227.789 1.00 58.12  ? 997  VAL B CG2 1 
ATOM   7833  N N   . VAL A 1 1015 ? 191.438 214.729 223.867 1.00 53.25  ? 998  VAL B N   1 
ATOM   7834  C CA  . VAL A 1 1015 ? 190.520 213.933 223.068 1.00 53.25  ? 998  VAL B CA  1 
ATOM   7835  C C   . VAL A 1 1015 ? 191.215 212.662 222.611 1.00 53.25  ? 998  VAL B C   1 
ATOM   7836  O O   . VAL A 1 1015 ? 192.429 212.632 222.387 1.00 53.25  ? 998  VAL B O   1 
ATOM   7837  C CB  . VAL A 1 1015 ? 189.974 214.723 221.858 1.00 53.25  ? 998  VAL B CB  1 
ATOM   7838  C CG1 . VAL A 1 1015 ? 189.404 216.052 222.306 1.00 53.25  ? 998  VAL B CG1 1 
ATOM   7839  C CG2 . VAL A 1 1015 ? 191.059 214.946 220.830 1.00 53.25  ? 998  VAL B CG2 1 
ATOM   7840  N N   . PHE A 1 1016 ? 190.430 211.596 222.500 1.00 54.71  ? 999  PHE B N   1 
ATOM   7841  C CA  . PHE A 1 1016 ? 190.866 210.345 221.897 1.00 54.71  ? 999  PHE B CA  1 
ATOM   7842  C C   . PHE A 1 1016 ? 189.941 210.065 220.726 1.00 54.71  ? 999  PHE B C   1 
ATOM   7843  O O   . PHE A 1 1016 ? 188.729 209.911 220.915 1.00 54.71  ? 999  PHE B O   1 
ATOM   7844  C CB  . PHE A 1 1016 ? 190.833 209.200 222.908 1.00 54.71  ? 999  PHE B CB  1 
ATOM   7845  C CG  . PHE A 1 1016 ? 190.773 207.838 222.282 1.00 54.71  ? 999  PHE B CG  1 
ATOM   7846  C CD1 . PHE A 1 1016 ? 191.845 207.344 221.566 1.00 54.71  ? 999  PHE B CD1 1 
ATOM   7847  C CD2 . PHE A 1 1016 ? 189.646 207.051 222.414 1.00 54.71  ? 999  PHE B CD2 1 
ATOM   7848  C CE1 . PHE A 1 1016 ? 191.792 206.091 220.993 1.00 54.71  ? 999  PHE B CE1 1 
ATOM   7849  C CE2 . PHE A 1 1016 ? 189.588 205.800 221.842 1.00 54.71  ? 999  PHE B CE2 1 
ATOM   7850  C CZ  . PHE A 1 1016 ? 190.662 205.320 221.131 1.00 54.71  ? 999  PHE B CZ  1 
ATOM   7851  N N   . LYS A 1 1017 ? 190.507 210.013 219.524 1.00 54.83  ? 1000 LYS B N   1 
ATOM   7852  C CA  . LYS A 1 1017 ? 189.741 209.893 218.293 1.00 54.83  ? 1000 LYS B CA  1 
ATOM   7853  C C   . LYS A 1 1017 ? 189.995 208.537 217.656 1.00 54.83  ? 1000 LYS B C   1 
ATOM   7854  O O   . LYS A 1 1017 ? 191.149 208.161 217.427 1.00 54.83  ? 1000 LYS B O   1 
ATOM   7855  C CB  . LYS A 1 1017 ? 190.105 211.006 217.310 1.00 54.83  ? 1000 LYS B CB  1 
ATOM   7856  C CG  . LYS A 1 1017 ? 190.274 212.369 217.951 1.00 54.83  ? 1000 LYS B CG  1 
ATOM   7857  C CD  . LYS A 1 1017 ? 190.974 213.339 217.016 1.00 54.83  ? 1000 LYS B CD  1 
ATOM   7858  C CE  . LYS A 1 1017 ? 190.347 213.330 215.633 1.00 54.83  ? 1000 LYS B CE  1 
ATOM   7859  N NZ  . LYS A 1 1017 ? 188.904 213.679 215.673 1.00 54.83  ? 1000 LYS B NZ  1 
ATOM   7860  N N   . TYR A 1 1018 ? 188.920 207.813 217.369 1.00 57.14  ? 1001 TYR B N   1 
ATOM   7861  C CA  . TYR A 1 1018 ? 188.991 206.549 216.655 1.00 57.14  ? 1001 TYR B CA  1 
ATOM   7862  C C   . TYR A 1 1018 ? 188.050 206.612 215.463 1.00 57.14  ? 1001 TYR B C   1 
ATOM   7863  O O   . TYR A 1 1018 ? 186.933 207.125 215.570 1.00 57.14  ? 1001 TYR B O   1 
ATOM   7864  C CB  . TYR A 1 1018 ? 188.634 205.365 217.562 1.00 57.14  ? 1001 TYR B CB  1 
ATOM   7865  C CG  . TYR A 1 1018 ? 187.192 205.325 218.014 1.00 57.14  ? 1001 TYR B CG  1 
ATOM   7866  C CD1 . TYR A 1 1018 ? 186.699 206.250 218.923 1.00 57.14  ? 1001 TYR B CD1 1 
ATOM   7867  C CD2 . TYR A 1 1018 ? 186.325 204.355 217.537 1.00 57.14  ? 1001 TYR B CD2 1 
ATOM   7868  C CE1 . TYR A 1 1018 ? 185.384 206.210 219.338 1.00 57.14  ? 1001 TYR B CE1 1 
ATOM   7869  C CE2 . TYR A 1 1018 ? 185.010 204.309 217.947 1.00 57.14  ? 1001 TYR B CE2 1 
ATOM   7870  C CZ  . TYR A 1 1018 ? 184.545 205.238 218.845 1.00 57.14  ? 1001 TYR B CZ  1 
ATOM   7871  O OH  . TYR A 1 1018 ? 183.235 205.191 219.251 1.00 57.14  ? 1001 TYR B OH  1 
ATOM   7872  N N   . SER A 1 1019 ? 188.511 206.104 214.326 1.00 55.46  ? 1002 SER B N   1 
ATOM   7873  C CA  . SER A 1 1019 ? 187.757 206.191 213.087 1.00 55.46  ? 1002 SER B CA  1 
ATOM   7874  C C   . SER A 1 1019 ? 186.742 205.062 212.990 1.00 55.46  ? 1002 SER B C   1 
ATOM   7875  O O   . SER A 1 1019 ? 186.900 204.001 213.598 1.00 55.46  ? 1002 SER B O   1 
ATOM   7876  C CB  . SER A 1 1019 ? 188.694 206.149 211.881 1.00 55.46  ? 1002 SER B CB  1 
ATOM   7877  O OG  . SER A 1 1019 ? 189.663 205.128 212.028 1.00 55.46  ? 1002 SER B OG  1 
ATOM   7878  N N   . GLN A 1 1020 ? 185.687 205.307 212.217 1.00 55.58  ? 1003 GLN B N   1 
ATOM   7879  C CA  . GLN A 1 1020 ? 184.659 204.310 211.961 1.00 55.58  ? 1003 GLN B CA  1 
ATOM   7880  C C   . GLN A 1 1020 ? 184.799 203.647 210.601 1.00 55.58  ? 1003 GLN B C   1 
ATOM   7881  O O   . GLN A 1 1020 ? 184.128 202.642 210.350 1.00 55.58  ? 1003 GLN B O   1 
ATOM   7882  C CB  . GLN A 1 1020 ? 183.268 204.940 212.065 1.00 55.58  ? 1003 GLN B CB  1 
ATOM   7883  C CG  . GLN A 1 1020 ? 182.822 205.233 213.478 1.00 55.58  ? 1003 GLN B CG  1 
ATOM   7884  C CD  . GLN A 1 1020 ? 181.322 205.295 213.597 1.00 55.58  ? 1003 GLN B CD  1 
ATOM   7885  O OE1 . GLN A 1 1020 ? 180.767 205.120 214.678 1.00 55.58  ? 1003 GLN B OE1 1 
ATOM   7886  N NE2 . GLN A 1 1020 ? 180.652 205.545 212.482 1.00 55.58  ? 1003 GLN B NE2 1 
ATOM   7887  N N   . MET A 1 1021 ? 185.641 204.181 209.722 1.00 54.65  ? 1004 MET B N   1 
ATOM   7888  C CA  . MET A 1 1021 ? 185.815 203.630 208.382 1.00 54.65  ? 1004 MET B CA  1 
ATOM   7889  C C   . MET A 1 1021 ? 187.048 202.730 208.357 1.00 54.65  ? 1004 MET B C   1 
ATOM   7890  O O   . MET A 1 1021 ? 188.106 203.070 207.830 1.00 54.65  ? 1004 MET B O   1 
ATOM   7891  C CB  . MET A 1 1021 ? 185.912 204.756 207.361 1.00 54.65  ? 1004 MET B CB  1 
ATOM   7892  C CG  . MET A 1 1021 ? 184.572 205.375 207.019 1.00 54.65  ? 1004 MET B CG  1 
ATOM   7893  S SD  . MET A 1 1021 ? 184.646 207.159 206.795 1.00 54.65  ? 1004 MET B SD  1 
ATOM   7894  C CE  . MET A 1 1021 ? 182.905 207.543 206.644 1.00 54.65  ? 1004 MET B CE  1 
ATOM   7895  N N   . ILE A 1 1022 ? 186.883 201.549 208.953 1.00 53.00  ? 1005 ILE B N   1 
ATOM   7896  C CA  . ILE A 1 1022 ? 187.935 200.545 209.026 1.00 53.00  ? 1005 ILE B CA  1 
ATOM   7897  C C   . ILE A 1 1022 ? 187.299 199.173 208.865 1.00 53.00  ? 1005 ILE B C   1 
ATOM   7898  O O   . ILE A 1 1022 ? 186.108 198.981 209.118 1.00 53.00  ? 1005 ILE B O   1 
ATOM   7899  C CB  . ILE A 1 1022 ? 188.726 200.628 210.350 1.00 53.00  ? 1005 ILE B CB  1 
ATOM   7900  C CG1 . ILE A 1 1022 ? 190.109 199.996 210.194 1.00 53.00  ? 1005 ILE B CG1 1 
ATOM   7901  C CG2 . ILE A 1 1022 ? 187.962 199.961 211.469 1.00 53.00  ? 1005 ILE B CG2 1 
ATOM   7902  C CD1 . ILE A 1 1022 ? 191.006 200.198 211.392 1.00 53.00  ? 1005 ILE B CD1 1 
ATOM   7903  N N   . ASN A 1 1023 ? 188.110 198.211 208.424 1.00 56.19  ? 1006 ASN B N   1 
ATOM   7904  C CA  . ASN A 1 1023 ? 187.599 196.863 208.200 1.00 56.19  ? 1006 ASN B CA  1 
ATOM   7905  C C   . ASN A 1 1023 ? 187.157 196.218 209.506 1.00 56.19  ? 1006 ASN B C   1 
ATOM   7906  O O   . ASN A 1 1023 ? 186.041 195.695 209.606 1.00 56.19  ? 1006 ASN B O   1 
ATOM   7907  C CB  . ASN A 1 1023 ? 188.659 196.011 207.505 1.00 56.19  ? 1006 ASN B CB  1 
ATOM   7908  C CG  . ASN A 1 1023 ? 188.759 196.304 206.024 1.00 56.19  ? 1006 ASN B CG  1 
ATOM   7909  O OD1 . ASN A 1 1023 ? 188.126 197.231 205.522 1.00 56.19  ? 1006 ASN B OD1 1 
ATOM   7910  N ND2 . ASN A 1 1023 ? 189.557 195.517 205.316 1.00 56.19  ? 1006 ASN B ND2 1 
ATOM   7911  N N   . ILE A 1 1024 ? 188.016 196.243 210.520 1.00 57.29  ? 1007 ILE B N   1 
ATOM   7912  C CA  . ILE A 1 1024 ? 187.692 195.713 211.840 1.00 57.29  ? 1007 ILE B CA  1 
ATOM   7913  C C   . ILE A 1 1024 ? 188.189 196.701 212.882 1.00 57.29  ? 1007 ILE B C   1 
ATOM   7914  O O   . ILE A 1 1024 ? 189.364 197.083 212.870 1.00 57.29  ? 1007 ILE B O   1 
ATOM   7915  C CB  . ILE A 1 1024 ? 188.313 194.323 212.068 1.00 57.29  ? 1007 ILE B CB  1 
ATOM   7916  C CG1 . ILE A 1 1024 ? 187.499 193.258 211.334 1.00 57.29  ? 1007 ILE B CG1 1 
ATOM   7917  C CG2 . ILE A 1 1024 ? 188.390 194.011 213.551 1.00 57.29  ? 1007 ILE B CG2 1 
ATOM   7918  C CD1 . ILE A 1 1024 ? 187.824 191.853 211.754 1.00 57.29  ? 1007 ILE B CD1 1 
ATOM   7919  N N   . SER A 1 1025 ? 187.305 197.110 213.785 1.00 59.46  ? 1008 SER B N   1 
ATOM   7920  C CA  . SER A 1 1025 ? 187.608 198.141 214.765 1.00 59.46  ? 1008 SER B CA  1 
ATOM   7921  C C   . SER A 1 1025 ? 187.636 197.546 216.164 1.00 59.46  ? 1008 SER B C   1 
ATOM   7922  O O   . SER A 1 1025 ? 186.770 196.744 216.526 1.00 59.46  ? 1008 SER B O   1 
ATOM   7923  C CB  . SER A 1 1025 ? 186.582 199.273 214.703 1.00 59.46  ? 1008 SER B CB  1 
ATOM   7924  O OG  . SER A 1 1025 ? 187.077 200.440 215.333 1.00 59.46  ? 1008 SER B OG  1 
ATOM   7925  N N   . ASP A 1 1026 ? 188.634 197.944 216.946 1.00 60.32  ? 1009 ASP B N   1 
ATOM   7926  C CA  . ASP A 1 1026 ? 188.755 197.519 218.333 1.00 60.32  ? 1009 ASP B CA  1 
ATOM   7927  C C   . ASP A 1 1026 ? 188.075 198.471 219.304 1.00 60.32  ? 1009 ASP B C   1 
ATOM   7928  O O   . ASP A 1 1026 ? 188.142 198.247 220.516 1.00 60.32  ? 1009 ASP B O   1 
ATOM   7929  C CB  . ASP A 1 1026 ? 190.230 197.374 218.715 1.00 60.32  ? 1009 ASP B CB  1 
ATOM   7930  C CG  . ASP A 1 1026 ? 191.003 196.525 217.732 1.00 60.32  ? 1009 ASP B CG  1 
ATOM   7931  O OD1 . ASP A 1 1026 ? 190.411 196.108 216.716 1.00 60.32  ? 1009 ASP B OD1 1 
ATOM   7932  O OD2 . ASP A 1 1026 ? 192.201 196.272 217.976 1.00 60.32  ? 1009 ASP B OD2 1 
ATOM   7933  N N   . TYR A 1 1027 ? 187.426 199.523 218.807 1.00 59.39  ? 1010 TYR B N   1 
ATOM   7934  C CA  . TYR A 1 1027 ? 186.802 200.512 219.668 1.00 59.39  ? 1010 TYR B CA  1 
ATOM   7935  C C   . TYR A 1 1027 ? 185.351 200.806 219.316 1.00 59.39  ? 1010 TYR B C   1 
ATOM   7936  O O   . TYR A 1 1027 ? 184.742 201.663 219.964 1.00 59.39  ? 1010 TYR B O   1 
ATOM   7937  C CB  . TYR A 1 1027 ? 187.598 201.823 219.637 1.00 59.39  ? 1010 TYR B CB  1 
ATOM   7938  C CG  . TYR A 1 1027 ? 189.082 201.639 219.842 1.00 59.39  ? 1010 TYR B CG  1 
ATOM   7939  C CD1 . TYR A 1 1027 ? 189.604 201.417 221.105 1.00 59.39  ? 1010 TYR B CD1 1 
ATOM   7940  C CD2 . TYR A 1 1027 ? 189.959 201.685 218.770 1.00 59.39  ? 1010 TYR B CD2 1 
ATOM   7941  C CE1 . TYR A 1 1027 ? 190.957 201.249 221.296 1.00 59.39  ? 1010 TYR B CE1 1 
ATOM   7942  C CE2 . TYR A 1 1027 ? 191.313 201.518 218.952 1.00 59.39  ? 1010 TYR B CE2 1 
ATOM   7943  C CZ  . TYR A 1 1027 ? 191.807 201.300 220.216 1.00 59.39  ? 1010 TYR B CZ  1 
ATOM   7944  O OH  . TYR A 1 1027 ? 193.158 201.131 220.401 1.00 59.39  ? 1010 TYR B OH  1 
ATOM   7945  N N   . ILE A 1 1028 ? 184.781 200.136 218.320 1.00 53.78  ? 1011 ILE B N   1 
ATOM   7946  C CA  . ILE A 1 1028 ? 183.391 200.340 217.929 1.00 53.78  ? 1011 ILE B CA  1 
ATOM   7947  C C   . ILE A 1 1028 ? 182.555 199.235 218.553 1.00 53.78  ? 1011 ILE B C   1 
ATOM   7948  O O   . ILE A 1 1028 ? 182.740 198.054 218.237 1.00 53.78  ? 1011 ILE B O   1 
ATOM   7949  C CB  . ILE A 1 1028 ? 183.229 200.351 216.402 1.00 53.78  ? 1011 ILE B CB  1 
ATOM   7950  C CG1 . ILE A 1 1028 ? 183.801 201.634 215.812 1.00 53.78  ? 1011 ILE B CG1 1 
ATOM   7951  C CG2 . ILE A 1 1028 ? 181.772 200.220 216.026 1.00 53.78  ? 1011 ILE B CG2 1 
ATOM   7952  C CD1 . ILE A 1 1028 ? 183.770 201.660 214.310 1.00 53.78  ? 1011 ILE B CD1 1 
ATOM   7953  N N   . ASN A 1 1029 ? 181.635 199.618 219.438 1.00 53.61  ? 1012 ASN B N   1 
ATOM   7954  C CA  . ASN A 1 1029 ? 180.733 198.680 220.102 1.00 53.61  ? 1012 ASN B CA  1 
ATOM   7955  C C   . ASN A 1 1029 ? 181.494 197.599 220.862 1.00 53.61  ? 1012 ASN B C   1 
ATOM   7956  O O   . ASN A 1 1029 ? 181.025 196.467 220.986 1.00 53.61  ? 1012 ASN B O   1 
ATOM   7957  C CB  . ASN A 1 1029 ? 179.760 198.046 219.105 1.00 53.61  ? 1012 ASN B CB  1 
ATOM   7958  C CG  . ASN A 1 1029 ? 178.491 197.555 219.761 1.00 53.61  ? 1012 ASN B CG  1 
ATOM   7959  O OD1 . ASN A 1 1029 ? 178.108 198.026 220.828 1.00 53.61  ? 1012 ASN B OD1 1 
ATOM   7960  N ND2 . ASN A 1 1029 ? 177.825 196.606 219.120 1.00 53.61  ? 1012 ASN B ND2 1 
ATOM   7961  N N   . ARG A 1 1030 ? 182.674 197.933 221.373 1.00 59.29  ? 1013 ARG B N   1 
ATOM   7962  C CA  . ARG A 1 1030 ? 183.468 197.012 222.170 1.00 59.29  ? 1013 ARG B CA  1 
ATOM   7963  C C   . ARG A 1 1030 ? 183.925 197.715 223.436 1.00 59.29  ? 1013 ARG B C   1 
ATOM   7964  O O   . ARG A 1 1030 ? 184.201 198.917 223.429 1.00 59.29  ? 1013 ARG B O   1 
ATOM   7965  C CB  . ARG A 1 1030 ? 184.683 196.491 221.397 1.00 59.29  ? 1013 ARG B CB  1 
ATOM   7966  C CG  . ARG A 1 1030 ? 184.350 195.891 220.046 1.00 59.29  ? 1013 ARG B CG  1 
ATOM   7967  C CD  . ARG A 1 1030 ? 185.587 195.329 219.375 1.00 59.29  ? 1013 ARG B CD  1 
ATOM   7968  N NE  . ARG A 1 1030 ? 186.279 194.377 220.233 1.00 59.29  ? 1013 ARG B NE  1 
ATOM   7969  C CZ  . ARG A 1 1030 ? 187.273 193.597 219.835 1.00 59.29  ? 1013 ARG B CZ  1 
ATOM   7970  N NH1 . ARG A 1 1030 ? 187.717 193.626 218.590 1.00 59.29  ? 1013 ARG B NH1 1 
ATOM   7971  N NH2 . ARG A 1 1030 ? 187.836 192.767 220.707 1.00 59.29  ? 1013 ARG B NH2 1 
ATOM   7972  N N   . TRP A 1 1031 ? 183.999 196.955 224.526 1.00 49.22  ? 1014 TRP B N   1 
ATOM   7973  C CA  . TRP A 1 1031 ? 184.382 197.527 225.808 1.00 49.22  ? 1014 TRP B CA  1 
ATOM   7974  C C   . TRP A 1 1031 ? 185.784 198.111 225.731 1.00 49.22  ? 1014 TRP B C   1 
ATOM   7975  O O   . TRP A 1 1031 ? 186.722 197.443 225.290 1.00 49.22  ? 1014 TRP B O   1 
ATOM   7976  C CB  . TRP A 1 1031 ? 184.322 196.461 226.898 1.00 49.22  ? 1014 TRP B CB  1 
ATOM   7977  C CG  . TRP A 1 1031 ? 182.943 196.153 227.377 1.00 49.22  ? 1014 TRP B CG  1 
ATOM   7978  C CD1 . TRP A 1 1031 ? 182.236 195.011 227.153 1.00 49.22  ? 1014 TRP B CD1 1 
ATOM   7979  C CD2 . TRP A 1 1031 ? 182.104 196.994 228.172 1.00 49.22  ? 1014 TRP B CD2 1 
ATOM   7980  N NE1 . TRP A 1 1031 ? 181.007 195.090 227.757 1.00 49.22  ? 1014 TRP B NE1 1 
ATOM   7981  C CE2 . TRP A 1 1031 ? 180.902 196.299 228.389 1.00 49.22  ? 1014 TRP B CE2 1 
ATOM   7982  C CE3 . TRP A 1 1031 ? 182.252 198.269 228.719 1.00 49.22  ? 1014 TRP B CE3 1 
ATOM   7983  C CZ2 . TRP A 1 1031 ? 179.857 196.834 229.128 1.00 49.22  ? 1014 TRP B CZ2 1 
ATOM   7984  C CZ3 . TRP A 1 1031 ? 181.214 198.798 229.451 1.00 49.22  ? 1014 TRP B CZ3 1 
ATOM   7985  C CH2 . TRP A 1 1031 ? 180.032 198.083 229.650 1.00 49.22  ? 1014 TRP B CH2 1 
ATOM   7986  N N   . ILE A 1 1032 ? 185.929 199.363 226.160 1.00 61.01  ? 1015 ILE B N   1 
ATOM   7987  C CA  . ILE A 1 1032 ? 187.232 200.014 226.226 1.00 61.01  ? 1015 ILE B CA  1 
ATOM   7988  C C   . ILE A 1 1032 ? 187.412 200.611 227.614 1.00 61.01  ? 1015 ILE B C   1 
ATOM   7989  O O   . ILE A 1 1032 ? 186.467 201.152 228.199 1.00 61.01  ? 1015 ILE B O   1 
ATOM   7990  C CB  . ILE A 1 1032 ? 187.410 201.085 225.126 1.00 61.01  ? 1015 ILE B CB  1 
ATOM   7991  C CG1 . ILE A 1 1032 ? 186.551 202.315 225.396 1.00 61.01  ? 1015 ILE B CG1 1 
ATOM   7992  C CG2 . ILE A 1 1032 ? 187.083 200.513 223.761 1.00 61.01  ? 1015 ILE B CG2 1 
ATOM   7993  C CD1 . ILE A 1 1032 ? 186.533 203.290 224.250 1.00 61.01  ? 1015 ILE B CD1 1 
ATOM   7994  N N   . PHE A 1 1033 ? 188.621 200.487 228.149 1.00 57.32  ? 1016 PHE B N   1 
ATOM   7995  C CA  . PHE A 1 1033 ? 188.937 200.909 229.511 1.00 57.32  ? 1016 PHE B CA  1 
ATOM   7996  C C   . PHE A 1 1033 ? 189.601 202.279 229.445 1.00 57.32  ? 1016 PHE B C   1 
ATOM   7997  O O   . PHE A 1 1033 ? 190.793 202.388 229.153 1.00 57.32  ? 1016 PHE B O   1 
ATOM   7998  C CB  . PHE A 1 1033 ? 189.835 199.881 230.189 1.00 57.32  ? 1016 PHE B CB  1 
ATOM   7999  C CG  . PHE A 1 1033 ? 190.445 200.356 231.473 1.00 57.32  ? 1016 PHE B CG  1 
ATOM   8000  C CD1 . PHE A 1 1033 ? 189.665 200.545 232.595 1.00 57.32  ? 1016 PHE B CD1 1 
ATOM   8001  C CD2 . PHE A 1 1033 ? 191.800 200.602 231.560 1.00 57.32  ? 1016 PHE B CD2 1 
ATOM   8002  C CE1 . PHE A 1 1033 ? 190.223 200.977 233.774 1.00 57.32  ? 1016 PHE B CE1 1 
ATOM   8003  C CE2 . PHE A 1 1033 ? 192.362 201.034 232.737 1.00 57.32  ? 1016 PHE B CE2 1 
ATOM   8004  C CZ  . PHE A 1 1033 ? 191.572 201.222 233.845 1.00 57.32  ? 1016 PHE B CZ  1 
ATOM   8005  N N   . VAL A 1 1034 ? 188.829 203.326 229.723 1.00 69.60  ? 1017 VAL B N   1 
ATOM   8006  C CA  . VAL A 1 1034 ? 189.299 204.701 229.632 1.00 69.60  ? 1017 VAL B CA  1 
ATOM   8007  C C   . VAL A 1 1034 ? 189.746 205.155 231.010 1.00 69.60  ? 1017 VAL B C   1 
ATOM   8008  O O   . VAL A 1 1034 ? 188.985 205.046 231.980 1.00 69.60  ? 1017 VAL B O   1 
ATOM   8009  C CB  . VAL A 1 1034 ? 188.198 205.626 229.094 1.00 69.60  ? 1017 VAL B CB  1 
ATOM   8010  C CG1 . VAL A 1 1034 ? 188.710 207.046 228.990 1.00 69.60  ? 1017 VAL B CG1 1 
ATOM   8011  C CG2 . VAL A 1 1034 ? 187.698 205.129 227.756 1.00 69.60  ? 1017 VAL B CG2 1 
ATOM   8012  N N   . THR A 1 1035 ? 190.969 205.672 231.105 1.00 62.61  ? 1018 THR B N   1 
ATOM   8013  C CA  . THR A 1 1035 ? 191.449 206.258 232.346 1.00 62.61  ? 1018 THR B CA  1 
ATOM   8014  C C   . THR A 1 1035 ? 192.066 207.620 232.063 1.00 62.61  ? 1018 THR B C   1 
ATOM   8015  O O   . THR A 1 1035 ? 192.659 207.845 231.008 1.00 62.61  ? 1018 THR B O   1 
ATOM   8016  C CB  . THR A 1 1035 ? 192.457 205.348 233.051 1.00 62.61  ? 1018 THR B CB  1 
ATOM   8017  O OG1 . THR A 1 1035 ? 192.944 205.996 234.230 1.00 62.61  ? 1018 THR B OG1 1 
ATOM   8018  C CG2 . THR A 1 1035 ? 193.610 205.026 232.141 1.00 62.61  ? 1018 THR B CG2 1 
ATOM   8019  N N   . ILE A 1 1036 ? 191.887 208.540 233.004 1.00 55.84  ? 1019 ILE B N   1 
ATOM   8020  C CA  . ILE A 1 1036 ? 192.308 209.926 232.836 1.00 55.84  ? 1019 ILE B CA  1 
ATOM   8021  C C   . ILE A 1 1036 ? 192.968 210.391 234.123 1.00 55.84  ? 1019 ILE B C   1 
ATOM   8022  O O   . ILE A 1 1036 ? 192.361 210.312 235.194 1.00 55.84  ? 1019 ILE B O   1 
ATOM   8023  C CB  . ILE A 1 1036 ? 191.118 210.836 232.484 1.00 55.84  ? 1019 ILE B CB  1 
ATOM   8024  C CG1 . ILE A 1 1036 ? 190.598 210.508 231.087 1.00 55.84  ? 1019 ILE B CG1 1 
ATOM   8025  C CG2 . ILE A 1 1036 ? 191.527 212.285 232.561 1.00 55.84  ? 1019 ILE B CG2 1 
ATOM   8026  C CD1 . ILE A 1 1036 ? 189.097 210.451 230.994 1.00 55.84  ? 1019 ILE B CD1 1 
ATOM   8027  N N   . THR A 1 1037 ? 194.200 210.886 234.023 1.00 61.02  ? 1020 THR B N   1 
ATOM   8028  C CA  . THR A 1 1037 ? 194.966 211.323 235.185 1.00 61.02  ? 1020 THR B CA  1 
ATOM   8029  C C   . THR A 1 1037 ? 195.323 212.792 235.026 1.00 61.02  ? 1020 THR B C   1 
ATOM   8030  O O   . THR A 1 1037 ? 195.980 213.169 234.051 1.00 61.02  ? 1020 THR B O   1 
ATOM   8031  C CB  . THR A 1 1037 ? 196.238 210.491 235.355 1.00 61.02  ? 1020 THR B CB  1 
ATOM   8032  O OG1 . THR A 1 1037 ? 197.281 211.047 234.548 1.00 61.02  ? 1020 THR B OG1 1 
ATOM   8033  C CG2 . THR A 1 1037 ? 196.000 209.056 234.930 1.00 61.02  ? 1020 THR B CG2 1 
ATOM   8034  N N   . ASN A 1 1038 ? 194.913 213.614 235.986 1.00 64.73  ? 1021 ASN B N   1 
ATOM   8035  C CA  . ASN A 1 1038 ? 195.182 215.043 235.968 1.00 64.73  ? 1021 ASN B CA  1 
ATOM   8036  C C   . ASN A 1 1038 ? 196.135 215.402 237.095 1.00 64.73  ? 1021 ASN B C   1 
ATOM   8037  O O   . ASN A 1 1038 ? 195.895 215.048 238.255 1.00 64.73  ? 1021 ASN B O   1 
ATOM   8038  C CB  . ASN A 1 1038 ? 193.897 215.855 236.115 1.00 64.73  ? 1021 ASN B CB  1 
ATOM   8039  C CG  . ASN A 1 1038 ? 192.869 215.503 235.079 1.00 64.73  ? 1021 ASN B CG  1 
ATOM   8040  O OD1 . ASN A 1 1038 ? 192.861 214.395 234.551 1.00 64.73  ? 1021 ASN B OD1 1 
ATOM   8041  N ND2 . ASN A 1 1038 ? 191.997 216.450 234.769 1.00 64.73  ? 1021 ASN B ND2 1 
ATOM   8042  N N   . ASN A 1 1039 ? 197.213 216.095 236.742 1.00 67.73  ? 1022 ASN B N   1 
ATOM   8043  C CA  . ASN A 1 1039 ? 198.104 216.749 237.691 1.00 67.73  ? 1022 ASN B CA  1 
ATOM   8044  C C   . ASN A 1 1039 ? 198.080 218.237 237.386 1.00 67.73  ? 1022 ASN B C   1 
ATOM   8045  O O   . ASN A 1 1039 ? 198.374 218.643 236.258 1.00 67.73  ? 1022 ASN B O   1 
ATOM   8046  C CB  . ASN A 1 1039 ? 199.527 216.201 237.585 1.00 67.73  ? 1022 ASN B CB  1 
ATOM   8047  C CG  . ASN A 1 1039 ? 200.393 216.593 238.763 1.00 67.73  ? 1022 ASN B CG  1 
ATOM   8048  O OD1 . ASN A 1 1039 ? 200.288 217.701 239.285 1.00 67.73  ? 1022 ASN B OD1 1 
ATOM   8049  N ND2 . ASN A 1 1039 ? 201.265 215.685 239.181 1.00 67.73  ? 1022 ASN B ND2 1 
ATOM   8050  N N   . ARG A 1 1040 ? 197.735 219.046 238.386 1.00 71.97  ? 1023 ARG B N   1 
ATOM   8051  C CA  . ARG A 1 1040 ? 197.651 220.483 238.159 1.00 71.97  ? 1023 ARG B CA  1 
ATOM   8052  C C   . ARG A 1 1040 ? 199.010 221.075 237.815 1.00 71.97  ? 1023 ARG B C   1 
ATOM   8053  O O   . ARG A 1 1040 ? 199.091 222.065 237.080 1.00 71.97  ? 1023 ARG B O   1 
ATOM   8054  C CB  . ARG A 1 1040 ? 197.061 221.172 239.388 1.00 71.97  ? 1023 ARG B CB  1 
ATOM   8055  C CG  . ARG A 1 1040 ? 197.067 222.686 239.314 1.00 71.97  ? 1023 ARG B CG  1 
ATOM   8056  C CD  . ARG A 1 1040 ? 196.252 223.184 238.137 1.00 71.97  ? 1023 ARG B CD  1 
ATOM   8057  N NE  . ARG A 1 1040 ? 194.957 223.706 238.554 1.00 71.97  ? 1023 ARG B NE  1 
ATOM   8058  C CZ  . ARG A 1 1040 ? 194.667 224.997 238.634 1.00 71.97  ? 1023 ARG B CZ  1 
ATOM   8059  N NH1 . ARG A 1 1040 ? 195.556 225.926 238.323 1.00 71.97  ? 1023 ARG B NH1 1 
ATOM   8060  N NH2 . ARG A 1 1040 ? 193.456 225.366 239.037 1.00 71.97  ? 1023 ARG B NH2 1 
ATOM   8061  N N   . LEU A 1 1041 ? 200.089 220.478 238.321 1.00 72.61  ? 1024 LEU B N   1 
ATOM   8062  C CA  . LEU A 1 1041 ? 201.411 221.063 238.132 1.00 72.61  ? 1024 LEU B CA  1 
ATOM   8063  C C   . LEU A 1 1041 ? 201.879 220.952 236.685 1.00 72.61  ? 1024 LEU B C   1 
ATOM   8064  O O   . LEU A 1 1041 ? 202.327 221.941 236.093 1.00 72.61  ? 1024 LEU B O   1 
ATOM   8065  C CB  . LEU A 1 1041 ? 202.415 220.395 239.071 1.00 72.61  ? 1024 LEU B CB  1 
ATOM   8066  C CG  . LEU A 1 1041 ? 202.287 220.706 240.562 1.00 72.61  ? 1024 LEU B CG  1 
ATOM   8067  C CD1 . LEU A 1 1041 ? 203.602 220.431 241.265 1.00 72.61  ? 1024 LEU B CD1 1 
ATOM   8068  C CD2 . LEU A 1 1041 ? 201.850 222.145 240.780 1.00 72.61  ? 1024 LEU B CD2 1 
ATOM   8069  N N   . ASN A 1 1042 ? 201.780 219.763 236.090 1.00 71.39  ? 1025 ASN B N   1 
ATOM   8070  C CA  . ASN A 1 1042 ? 202.457 219.497 234.828 1.00 71.39  ? 1025 ASN B CA  1 
ATOM   8071  C C   . ASN A 1 1042 ? 201.505 219.261 233.662 1.00 71.39  ? 1025 ASN B C   1 
ATOM   8072  O O   . ASN A 1 1042 ? 201.535 220.013 232.685 1.00 71.39  ? 1025 ASN B O   1 
ATOM   8073  C CB  . ASN A 1 1042 ? 203.386 218.288 234.992 1.00 71.39  ? 1025 ASN B CB  1 
ATOM   8074  C CG  . ASN A 1 1042 ? 203.897 218.139 236.406 1.00 71.39  ? 1025 ASN B CG  1 
ATOM   8075  O OD1 . ASN A 1 1042 ? 204.468 219.070 236.972 1.00 71.39  ? 1025 ASN B OD1 1 
ATOM   8076  N ND2 . ASN A 1 1042 ? 203.693 216.964 236.988 1.00 71.39  ? 1025 ASN B ND2 1 
ATOM   8077  N N   . ASN A 1 1043 ? 200.646 218.249 233.739 1.00 67.21  ? 1026 ASN B N   1 
ATOM   8078  C CA  . ASN A 1 1043 ? 199.923 217.808 232.555 1.00 67.21  ? 1026 ASN B CA  1 
ATOM   8079  C C   . ASN A 1 1043 ? 198.675 217.046 232.966 1.00 67.21  ? 1026 ASN B C   1 
ATOM   8080  O O   . ASN A 1 1043 ? 198.541 216.602 234.107 1.00 67.21  ? 1026 ASN B O   1 
ATOM   8081  C CB  . ASN A 1 1043 ? 200.800 216.919 231.666 1.00 67.21  ? 1026 ASN B CB  1 
ATOM   8082  C CG  . ASN A 1 1043 ? 201.756 217.711 230.805 1.00 67.21  ? 1026 ASN B CG  1 
ATOM   8083  O OD1 . ASN A 1 1043 ? 202.972 217.626 230.967 1.00 67.21  ? 1026 ASN B OD1 1 
ATOM   8084  N ND2 . ASN A 1 1043 ? 201.211 218.483 229.874 1.00 67.21  ? 1026 ASN B ND2 1 
ATOM   8085  N N   . SER A 1 1044 ? 197.767 216.899 232.007 1.00 58.31  ? 1027 SER B N   1 
ATOM   8086  C CA  . SER A 1 1044 ? 196.620 216.011 232.120 1.00 58.31  ? 1027 SER B CA  1 
ATOM   8087  C C   . SER A 1 1044 ? 196.672 215.028 230.962 1.00 58.31  ? 1027 SER B C   1 
ATOM   8088  O O   . SER A 1 1044 ? 196.782 215.440 229.803 1.00 58.31  ? 1027 SER B O   1 
ATOM   8089  C CB  . SER A 1 1044 ? 195.307 216.793 232.104 1.00 58.31  ? 1027 SER B CB  1 
ATOM   8090  O OG  . SER A 1 1044 ? 194.758 216.835 230.801 1.00 58.31  ? 1027 SER B OG  1 
ATOM   8091  N N   . LYS A 1 1045 ? 196.606 213.737 231.274 1.00 57.52  ? 1028 LYS B N   1 
ATOM   8092  C CA  . LYS A 1 1045 ? 196.773 212.685 230.285 1.00 57.52  ? 1028 LYS B CA  1 
ATOM   8093  C C   . LYS A 1 1045 ? 195.565 211.761 230.274 1.00 57.52  ? 1028 LYS B C   1 
ATOM   8094  O O   . LYS A 1 1045 ? 194.860 211.618 231.277 1.00 57.52  ? 1028 LYS B O   1 
ATOM   8095  C CB  . LYS A 1 1045 ? 198.032 211.858 230.551 1.00 57.52  ? 1028 LYS B CB  1 
ATOM   8096  C CG  . LYS A 1 1045 ? 199.180 212.629 231.166 1.00 57.52  ? 1028 LYS B CG  1 
ATOM   8097  C CD  . LYS A 1 1045 ? 200.203 211.686 231.770 1.00 57.52  ? 1028 LYS B CD  1 
ATOM   8098  C CE  . LYS A 1 1045 ? 201.500 212.408 232.086 1.00 57.52  ? 1028 LYS B CE  1 
ATOM   8099  N NZ  . LYS A 1 1045 ? 201.978 213.214 230.931 1.00 57.52  ? 1028 LYS B NZ  1 
ATOM   8100  N N   . ILE A 1 1046 ? 195.336 211.138 229.122 1.00 49.76  ? 1029 ILE B N   1 
ATOM   8101  C CA  . ILE A 1 1046 ? 194.282 210.151 228.939 1.00 49.76  ? 1029 ILE B CA  1 
ATOM   8102  C C   . ILE A 1 1046 ? 194.887 208.909 228.304 1.00 49.76  ? 1029 ILE B C   1 
ATOM   8103  O O   . ILE A 1 1046 ? 195.571 209.000 227.273 1.00 49.76  ? 1029 ILE B O   1 
ATOM   8104  C CB  . ILE A 1 1046 ? 193.123 210.693 228.081 1.00 49.76  ? 1029 ILE B CB  1 
ATOM   8105  C CG1 . ILE A 1 1046 ? 192.187 209.560 227.671 1.00 49.76  ? 1029 ILE B CG1 1 
ATOM   8106  C CG2 . ILE A 1 1046 ? 193.647 211.402 226.856 1.00 49.76  ? 1029 ILE B CG2 1 
ATOM   8107  C CD1 . ILE A 1 1046 ? 190.946 210.031 226.964 1.00 49.76  ? 1029 ILE B CD1 1 
ATOM   8108  N N   . TYR A 1 1047 ? 194.643 207.759 228.933 1.00 63.47  ? 1030 TYR B N   1 
ATOM   8109  C CA  . TYR A 1 1047 ? 195.062 206.450 228.459 1.00 63.47  ? 1030 TYR B CA  1 
ATOM   8110  C C   . TYR A 1 1047 ? 193.832 205.641 228.071 1.00 63.47  ? 1030 TYR B C   1 
ATOM   8111  O O   . TYR A 1 1047 ? 192.815 205.658 228.776 1.00 63.47  ? 1030 TYR B O   1 
ATOM   8112  C CB  . TYR A 1 1047 ? 195.836 205.665 229.529 1.00 63.47  ? 1030 TYR B CB  1 
ATOM   8113  C CG  . TYR A 1 1047 ? 196.931 206.400 230.274 1.00 63.47  ? 1030 TYR B CG  1 
ATOM   8114  C CD1 . TYR A 1 1047 ? 196.640 207.441 231.141 1.00 63.47  ? 1030 TYR B CD1 1 
ATOM   8115  C CD2 . TYR A 1 1047 ? 198.255 206.014 230.146 1.00 63.47  ? 1030 TYR B CD2 1 
ATOM   8116  C CE1 . TYR A 1 1047 ? 197.636 208.098 231.827 1.00 63.47  ? 1030 TYR B CE1 1 
ATOM   8117  C CE2 . TYR A 1 1047 ? 199.256 206.666 230.828 1.00 63.47  ? 1030 TYR B CE2 1 
ATOM   8118  C CZ  . TYR A 1 1047 ? 198.941 207.706 231.667 1.00 63.47  ? 1030 TYR B CZ  1 
ATOM   8119  O OH  . TYR A 1 1047 ? 199.938 208.359 232.351 1.00 63.47  ? 1030 TYR B OH  1 
ATOM   8120  N N   . ILE A 1 1048 ? 193.933 204.923 226.957 1.00 51.80  ? 1031 ILE B N   1 
ATOM   8121  C CA  . ILE A 1 1048 ? 192.890 204.015 226.498 1.00 51.80  ? 1031 ILE B CA  1 
ATOM   8122  C C   . ILE A 1 1048 ? 193.465 202.608 226.514 1.00 51.80  ? 1031 ILE B C   1 
ATOM   8123  O O   . ILE A 1 1048 ? 194.487 202.346 225.869 1.00 51.80  ? 1031 ILE B O   1 
ATOM   8124  C CB  . ILE A 1 1048 ? 192.388 204.377 225.095 1.00 51.80  ? 1031 ILE B CB  1 
ATOM   8125  C CG1 . ILE A 1 1048 ? 191.813 205.790 225.076 1.00 51.80  ? 1031 ILE B CG1 1 
ATOM   8126  C CG2 . ILE A 1 1048 ? 191.337 203.386 224.649 1.00 51.80  ? 1031 ILE B CG2 1 
ATOM   8127  C CD1 . ILE A 1 1048 ? 190.817 206.048 226.160 1.00 51.80  ? 1031 ILE B CD1 1 
ATOM   8128  N N   . ASN A 1 1049 ? 192.806 201.706 227.239 1.00 60.14  ? 1032 ASN B N   1 
ATOM   8129  C CA  . ASN A 1 1049 ? 193.249 200.318 227.360 1.00 60.14  ? 1032 ASN B CA  1 
ATOM   8130  C C   . ASN A 1 1049 ? 194.674 200.227 227.903 1.00 60.14  ? 1032 ASN B C   1 
ATOM   8131  O O   . ASN A 1 1049 ? 195.480 199.414 227.449 1.00 60.14  ? 1032 ASN B O   1 
ATOM   8132  C CB  . ASN A 1 1049 ? 193.129 199.580 226.026 1.00 60.14  ? 1032 ASN B CB  1 
ATOM   8133  C CG  . ASN A 1 1049 ? 191.729 199.071 225.769 1.00 60.14  ? 1032 ASN B CG  1 
ATOM   8134  O OD1 . ASN A 1 1049 ? 190.948 198.879 226.698 1.00 60.14  ? 1032 ASN B OD1 1 
ATOM   8135  N ND2 . ASN A 1 1049 ? 191.404 198.847 224.503 1.00 60.14  ? 1032 ASN B ND2 1 
ATOM   8136  N N   . GLY A 1 1050 ? 194.989 201.071 228.882 1.00 55.11  ? 1033 GLY B N   1 
ATOM   8137  C CA  . GLY A 1 1050 ? 196.273 200.983 229.546 1.00 55.11  ? 1033 GLY B CA  1 
ATOM   8138  C C   . GLY A 1 1050 ? 197.459 201.429 228.725 1.00 55.11  ? 1033 GLY B C   1 
ATOM   8139  O O   . GLY A 1 1050 ? 198.592 201.067 229.049 1.00 55.11  ? 1033 GLY B O   1 
ATOM   8140  N N   . ARG A 1 1051 ? 197.235 202.204 227.669 1.00 57.15  ? 1034 ARG B N   1 
ATOM   8141  C CA  . ARG A 1 1051 ? 198.308 202.737 226.841 1.00 57.15  ? 1034 ARG B CA  1 
ATOM   8142  C C   . ARG A 1 1051 ? 198.116 204.237 226.705 1.00 57.15  ? 1034 ARG B C   1 
ATOM   8143  O O   . ARG A 1 1051 ? 197.006 204.695 226.420 1.00 57.15  ? 1034 ARG B O   1 
ATOM   8144  C CB  . ARG A 1 1051 ? 198.324 202.073 225.462 1.00 57.15  ? 1034 ARG B CB  1 
ATOM   8145  C CG  . ARG A 1 1051 ? 199.067 202.860 224.399 1.00 57.15  ? 1034 ARG B CG  1 
ATOM   8146  C CD  . ARG A 1 1051 ? 199.007 202.159 223.053 1.00 57.15  ? 1034 ARG B CD  1 
ATOM   8147  N NE  . ARG A 1 1051 ? 197.849 202.579 222.275 1.00 57.15  ? 1034 ARG B NE  1 
ATOM   8148  C CZ  . ARG A 1 1051 ? 196.690 201.935 222.248 1.00 57.15  ? 1034 ARG B CZ  1 
ATOM   8149  N NH1 . ARG A 1 1051 ? 196.497 200.830 222.949 1.00 57.15  ? 1034 ARG B NH1 1 
ATOM   8150  N NH2 . ARG A 1 1051 ? 195.699 202.413 221.502 1.00 57.15  ? 1034 ARG B NH2 1 
ATOM   8151  N N   . LEU A 1 1052 ? 199.188 204.998 226.914 1.00 55.23  ? 1035 LEU B N   1 
ATOM   8152  C CA  . LEU A 1 1052 ? 199.093 206.448 226.825 1.00 55.23  ? 1035 LEU B CA  1 
ATOM   8153  C C   . LEU A 1 1052 ? 198.615 206.857 225.441 1.00 55.23  ? 1035 LEU B C   1 
ATOM   8154  O O   . LEU A 1 1052 ? 199.161 206.419 224.426 1.00 55.23  ? 1035 LEU B O   1 
ATOM   8155  C CB  . LEU A 1 1052 ? 200.443 207.096 227.130 1.00 55.23  ? 1035 LEU B CB  1 
ATOM   8156  C CG  . LEU A 1 1052 ? 200.500 208.621 227.004 1.00 55.23  ? 1035 LEU B CG  1 
ATOM   8157  C CD1 . LEU A 1 1052 ? 199.354 209.279 227.745 1.00 55.23  ? 1035 LEU B CD1 1 
ATOM   8158  C CD2 . LEU A 1 1052 ? 201.827 209.151 227.507 1.00 55.23  ? 1035 LEU B CD2 1 
ATOM   8159  N N   . ILE A 1 1053 ? 197.590 207.700 225.407 1.00 53.01  ? 1036 ILE B N   1 
ATOM   8160  C CA  . ILE A 1 1053 ? 196.974 208.145 224.167 1.00 53.01  ? 1036 ILE B CA  1 
ATOM   8161  C C   . ILE A 1 1053 ? 197.182 209.636 223.950 1.00 53.01  ? 1036 ILE B C   1 
ATOM   8162  O O   . ILE A 1 1053 ? 197.606 210.058 222.875 1.00 53.01  ? 1036 ILE B O   1 
ATOM   8163  C CB  . ILE A 1 1053 ? 195.473 207.784 224.132 1.00 53.01  ? 1036 ILE B CB  1 
ATOM   8164  C CG1 . ILE A 1 1053 ? 195.293 206.313 223.762 1.00 53.01  ? 1036 ILE B CG1 1 
ATOM   8165  C CG2 . ILE A 1 1053 ? 194.739 208.669 223.146 1.00 53.01  ? 1036 ILE B CG2 1 
ATOM   8166  C CD1 . ILE A 1 1053 ? 195.743 205.980 222.363 1.00 53.01  ? 1036 ILE B CD1 1 
ATOM   8167  N N   . ASP A 1 1054 ? 196.898 210.453 224.961 1.00 58.08  ? 1037 ASP B N   1 
ATOM   8168  C CA  . ASP A 1 1054 ? 197.056 211.886 224.748 1.00 58.08  ? 1037 ASP B CA  1 
ATOM   8169  C C   . ASP A 1 1054 ? 197.412 212.579 226.052 1.00 58.08  ? 1037 ASP B C   1 
ATOM   8170  O O   . ASP A 1 1054 ? 197.196 212.045 227.139 1.00 58.08  ? 1037 ASP B O   1 
ATOM   8171  C CB  . ASP A 1 1054 ? 195.790 212.503 224.147 1.00 58.08  ? 1037 ASP B CB  1 
ATOM   8172  C CG  . ASP A 1 1054 ? 196.078 213.761 223.362 1.00 58.08  ? 1037 ASP B CG  1 
ATOM   8173  O OD1 . ASP A 1 1054 ? 197.099 214.417 223.652 1.00 58.08  ? 1037 ASP B OD1 1 
ATOM   8174  O OD2 . ASP A 1 1054 ? 195.289 214.090 222.452 1.00 58.08  ? 1037 ASP B OD2 1 
ATOM   8175  N N   . GLN A 1 1055 ? 197.971 213.780 225.927 1.00 58.26  ? 1038 GLN B N   1 
ATOM   8176  C CA  . GLN A 1 1055 ? 198.307 214.586 227.091 1.00 58.26  ? 1038 GLN B CA  1 
ATOM   8177  C C   . GLN A 1 1055 ? 198.377 216.046 226.677 1.00 58.26  ? 1038 GLN B C   1 
ATOM   8178  O O   . GLN A 1 1055 ? 198.735 216.364 225.541 1.00 58.26  ? 1038 GLN B O   1 
ATOM   8179  C CB  . GLN A 1 1055 ? 199.634 214.156 227.719 1.00 58.26  ? 1038 GLN B CB  1 
ATOM   8180  C CG  . GLN A 1 1055 ? 200.853 214.510 226.896 1.00 58.26  ? 1038 GLN B CG  1 
ATOM   8181  C CD  . GLN A 1 1055 ? 202.133 214.403 227.692 1.00 58.26  ? 1038 GLN B CD  1 
ATOM   8182  O OE1 . GLN A 1 1055 ? 202.349 213.433 228.416 1.00 58.26  ? 1038 GLN B OE1 1 
ATOM   8183  N NE2 . GLN A 1 1055 ? 202.989 215.408 227.568 1.00 58.26  ? 1038 GLN B NE2 1 
ATOM   8184  N N   . LYS A 1 1056 ? 198.037 216.930 227.617 1.00 59.30  ? 1039 LYS B N   1 
ATOM   8185  C CA  . LYS A 1 1056 ? 198.050 218.364 227.362 1.00 59.30  ? 1039 LYS B CA  1 
ATOM   8186  C C   . LYS A 1 1056 ? 198.263 219.123 228.663 1.00 59.30  ? 1039 LYS B C   1 
ATOM   8187  O O   . LYS A 1 1056 ? 197.795 218.670 229.716 1.00 59.30  ? 1039 LYS B O   1 
ATOM   8188  C CB  . LYS A 1 1056 ? 196.747 218.825 226.704 1.00 59.30  ? 1039 LYS B CB  1 
ATOM   8189  C CG  . LYS A 1 1056 ? 196.668 218.582 225.205 1.00 59.30  ? 1039 LYS B CG  1 
ATOM   8190  C CD  . LYS A 1 1056 ? 195.764 219.594 224.528 1.00 59.30  ? 1039 LYS B CD  1 
ATOM   8191  C CE  . LYS A 1 1056 ? 195.378 219.145 223.131 1.00 59.30  ? 1039 LYS B CE  1 
ATOM   8192  N NZ  . LYS A 1 1056 ? 195.171 217.675 223.059 1.00 59.30  ? 1039 LYS B NZ  1 
ATOM   8193  N N   . PRO A 1 1057 ? 198.964 220.256 228.631 1.00 66.11  ? 1040 PRO B N   1 
ATOM   8194  C CA  . PRO A 1 1057 ? 199.160 221.041 229.857 1.00 66.11  ? 1040 PRO B CA  1 
ATOM   8195  C C   . PRO A 1 1057 ? 197.869 221.674 230.350 1.00 66.11  ? 1040 PRO B C   1 
ATOM   8196  O O   . PRO A 1 1057 ? 196.991 222.045 229.567 1.00 66.11  ? 1040 PRO B O   1 
ATOM   8197  C CB  . PRO A 1 1057 ? 200.172 222.115 229.435 1.00 66.11  ? 1040 PRO B CB  1 
ATOM   8198  C CG  . PRO A 1 1057 ? 200.791 221.596 228.176 1.00 66.11  ? 1040 PRO B CG  1 
ATOM   8199  C CD  . PRO A 1 1057 ? 199.724 220.806 227.499 1.00 66.11  ? 1040 PRO B CD  1 
ATOM   8200  N N   . ILE A 1 1058 ? 197.767 221.808 231.673 1.00 70.07  ? 1041 ILE B N   1 
ATOM   8201  C CA  . ILE A 1 1058 ? 196.603 222.424 232.303 1.00 70.07  ? 1041 ILE B CA  1 
ATOM   8202  C C   . ILE A 1 1058 ? 197.053 223.485 233.296 1.00 70.07  ? 1041 ILE B C   1 
ATOM   8203  O O   . ILE A 1 1058 ? 196.232 224.057 234.021 1.00 70.07  ? 1041 ILE B O   1 
ATOM   8204  C CB  . ILE A 1 1058 ? 195.717 221.381 233.006 1.00 70.07  ? 1041 ILE B CB  1 
ATOM   8205  C CG1 . ILE A 1 1058 ? 196.561 220.471 233.894 1.00 70.07  ? 1041 ILE B CG1 1 
ATOM   8206  C CG2 . ILE A 1 1058 ? 194.958 220.550 231.995 1.00 70.07  ? 1041 ILE B CG2 1 
ATOM   8207  C CD1 . ILE A 1 1058 ? 195.741 219.457 234.648 1.00 70.07  ? 1041 ILE B CD1 1 
ATOM   8208  N N   . SER A 1 1059 ? 198.359 223.753 233.341 1.00 72.02  ? 1042 SER B N   1 
ATOM   8209  C CA  . SER A 1 1059 ? 198.897 224.673 234.337 1.00 72.02  ? 1042 SER B CA  1 
ATOM   8210  C C   . SER A 1 1059 ? 198.371 226.092 234.173 1.00 72.02  ? 1042 SER B C   1 
ATOM   8211  O O   . SER A 1 1059 ? 198.391 226.861 235.139 1.00 72.02  ? 1042 SER B O   1 
ATOM   8212  C CB  . SER A 1 1059 ? 200.424 224.680 234.273 1.00 72.02  ? 1042 SER B CB  1 
ATOM   8213  O OG  . SER A 1 1059 ? 200.891 225.762 233.487 1.00 72.02  ? 1042 SER B OG  1 
ATOM   8214  N N   . ASN A 1 1060 ? 197.904 226.461 232.979 1.00 75.72  ? 1043 ASN B N   1 
ATOM   8215  C CA  . ASN A 1 1060 ? 197.415 227.817 232.765 1.00 75.72  ? 1043 ASN B CA  1 
ATOM   8216  C C   . ASN A 1 1060 ? 196.061 228.060 233.419 1.00 75.72  ? 1043 ASN B C   1 
ATOM   8217  O O   . ASN A 1 1060 ? 195.670 229.220 233.587 1.00 75.72  ? 1043 ASN B O   1 
ATOM   8218  C CB  . ASN A 1 1060 ? 197.320 228.114 231.269 1.00 75.72  ? 1043 ASN B CB  1 
ATOM   8219  C CG  . ASN A 1 1060 ? 196.245 227.299 230.581 1.00 75.72  ? 1043 ASN B CG  1 
ATOM   8220  O OD1 . ASN A 1 1060 ? 196.202 226.076 230.707 1.00 75.72  ? 1043 ASN B OD1 1 
ATOM   8221  N ND2 . ASN A 1 1060 ? 195.366 227.974 229.851 1.00 75.72  ? 1043 ASN B ND2 1 
ATOM   8222  N N   . LEU A 1 1061 ? 195.341 227.003 233.788 1.00 77.46  ? 1044 LEU B N   1 
ATOM   8223  C CA  . LEU A 1 1061 ? 194.008 227.161 234.352 1.00 77.46  ? 1044 LEU B CA  1 
ATOM   8224  C C   . LEU A 1 1061 ? 194.069 227.844 235.713 1.00 77.46  ? 1044 LEU B C   1 
ATOM   8225  O O   . LEU A 1 1061 ? 195.059 227.745 236.443 1.00 77.46  ? 1044 LEU B O   1 
ATOM   8226  C CB  . LEU A 1 1061 ? 193.316 225.804 234.480 1.00 77.46  ? 1044 LEU B CB  1 
ATOM   8227  C CG  . LEU A 1 1061 ? 193.044 225.073 233.167 1.00 77.46  ? 1044 LEU B CG  1 
ATOM   8228  C CD1 . LEU A 1 1061 ? 192.463 223.707 233.435 1.00 77.46  ? 1044 LEU B CD1 1 
ATOM   8229  C CD2 . LEU A 1 1061 ? 192.115 225.882 232.288 1.00 77.46  ? 1044 LEU B CD2 1 
ATOM   8230  N N   . GLY A 1 1062 ? 192.990 228.542 236.052 1.00 82.86  ? 1045 GLY B N   1 
ATOM   8231  C CA  . GLY A 1 1062 ? 192.933 229.287 237.294 1.00 82.86  ? 1045 GLY B CA  1 
ATOM   8232  C C   . GLY A 1 1062 ? 192.251 228.548 238.427 1.00 82.86  ? 1045 GLY B C   1 
ATOM   8233  O O   . GLY A 1 1062 ? 192.829 227.630 239.017 1.00 82.86  ? 1045 GLY B O   1 
ATOM   8234  N N   . ASN A 1 1063 ? 191.021 228.943 238.742 1.00 87.53  ? 1046 ASN B N   1 
ATOM   8235  C CA  . ASN A 1 1063 ? 190.277 228.392 239.872 1.00 87.53  ? 1046 ASN B CA  1 
ATOM   8236  C C   . ASN A 1 1063 ? 189.284 227.384 239.301 1.00 87.53  ? 1046 ASN B C   1 
ATOM   8237  O O   . ASN A 1 1063 ? 188.258 227.762 238.730 1.00 87.53  ? 1046 ASN B O   1 
ATOM   8238  C CB  . ASN A 1 1063 ? 189.599 229.523 240.648 1.00 87.53  ? 1046 ASN B CB  1 
ATOM   8239  C CG  . ASN A 1 1063 ? 188.341 229.088 241.408 1.00 87.53  ? 1046 ASN B CG  1 
ATOM   8240  O OD1 . ASN A 1 1063 ? 188.093 227.904 241.642 1.00 87.53  ? 1046 ASN B OD1 1 
ATOM   8241  N ND2 . ASN A 1 1063 ? 187.533 230.071 241.790 1.00 87.53  ? 1046 ASN B ND2 1 
ATOM   8242  N N   . ILE A 1 1064 ? 189.590 226.101 239.455 1.00 82.77  ? 1047 ILE B N   1 
ATOM   8243  C CA  . ILE A 1 1064 ? 188.663 225.027 239.109 1.00 82.77  ? 1047 ILE B CA  1 
ATOM   8244  C C   . ILE A 1 1064 ? 187.951 224.663 240.407 1.00 82.77  ? 1047 ILE B C   1 
ATOM   8245  O O   . ILE A 1 1064 ? 188.392 223.800 241.168 1.00 82.77  ? 1047 ILE B O   1 
ATOM   8246  C CB  . ILE A 1 1064 ? 189.374 223.832 238.476 1.00 82.77  ? 1047 ILE B CB  1 
ATOM   8247  C CG1 . ILE A 1 1064 ? 190.733 223.601 239.137 1.00 82.77  ? 1047 ILE B CG1 1 
ATOM   8248  C CG2 . ILE A 1 1064 ? 189.546 224.047 236.987 1.00 82.77  ? 1047 ILE B CG2 1 
ATOM   8249  C CD1 . ILE A 1 1064 ? 191.495 222.423 238.572 1.00 82.77  ? 1047 ILE B CD1 1 
ATOM   8250  N N   . HIS A 1 1065 ? 186.832 225.332 240.665 1.00 84.03  ? 1048 HIS B N   1 
ATOM   8251  C CA  . HIS A 1 1065 ? 186.140 225.167 241.935 1.00 84.03  ? 1048 HIS B CA  1 
ATOM   8252  C C   . HIS A 1 1065 ? 185.438 223.814 241.977 1.00 84.03  ? 1048 HIS B C   1 
ATOM   8253  O O   . HIS A 1 1065 ? 184.689 223.462 241.062 1.00 84.03  ? 1048 HIS B O   1 
ATOM   8254  C CB  . HIS A 1 1065 ? 185.148 226.310 242.137 1.00 84.03  ? 1048 HIS B CB  1 
ATOM   8255  C CG  . HIS A 1 1065 ? 183.878 225.906 242.815 1.00 84.03  ? 1048 HIS B CG  1 
ATOM   8256  N ND1 . HIS A 1 1065 ? 183.762 225.830 244.186 1.00 84.03  ? 1048 HIS B ND1 1 
ATOM   8257  C CD2 . HIS A 1 1065 ? 182.663 225.579 242.316 1.00 84.03  ? 1048 HIS B CD2 1 
ATOM   8258  C CE1 . HIS A 1 1065 ? 182.533 225.465 244.503 1.00 84.03  ? 1048 HIS B CE1 1 
ATOM   8259  N NE2 . HIS A 1 1065 ? 181.846 225.306 243.386 1.00 84.03  ? 1048 HIS B NE2 1 
ATOM   8260  N N   . ALA A 1 1066 ? 185.684 223.059 243.044 1.00 78.67  ? 1049 ALA B N   1 
ATOM   8261  C CA  . ALA A 1 1066 ? 185.205 221.689 243.132 1.00 78.67  ? 1049 ALA B CA  1 
ATOM   8262  C C   . ALA A 1 1066 ? 183.686 221.648 243.265 1.00 78.67  ? 1049 ALA B C   1 
ATOM   8263  O O   . ALA A 1 1066 ? 183.043 222.610 243.691 1.00 78.67  ? 1049 ALA B O   1 
ATOM   8264  C CB  . ALA A 1 1066 ? 185.850 220.970 244.315 1.00 78.67  ? 1049 ALA B CB  1 
ATOM   8265  N N   . SER A 1 1067 ? 183.115 220.510 242.890 1.00 74.16  ? 1050 SER B N   1 
ATOM   8266  C CA  . SER A 1 1067 ? 181.679 220.283 242.941 1.00 74.16  ? 1050 SER B CA  1 
ATOM   8267  C C   . SER A 1 1067 ? 181.370 219.154 243.917 1.00 74.16  ? 1050 SER B C   1 
ATOM   8268  O O   . SER A 1 1067 ? 182.256 218.608 244.577 1.00 74.16  ? 1050 SER B O   1 
ATOM   8269  C CB  . SER A 1 1067 ? 181.127 219.965 241.550 1.00 74.16  ? 1050 SER B CB  1 
ATOM   8270  O OG  . SER A 1 1067 ? 181.829 218.885 240.960 1.00 74.16  ? 1050 SER B OG  1 
ATOM   8271  N N   . ASN A 1 1068 ? 180.089 218.803 243.996 1.00 71.41  ? 1051 ASN B N   1 
ATOM   8272  C CA  . ASN A 1 1068 ? 179.621 217.773 244.914 1.00 71.41  ? 1051 ASN B CA  1 
ATOM   8273  C C   . ASN A 1 1068 ? 178.769 216.697 244.262 1.00 71.41  ? 1051 ASN B C   1 
ATOM   8274  O O   . ASN A 1 1068 ? 178.740 215.573 244.776 1.00 71.41  ? 1051 ASN B O   1 
ATOM   8275  C CB  . ASN A 1 1068 ? 178.818 218.407 246.059 1.00 71.41  ? 1051 ASN B CB  1 
ATOM   8276  C CG  . ASN A 1 1068 ? 178.628 217.468 247.223 1.00 71.41  ? 1051 ASN B CG  1 
ATOM   8277  O OD1 . ASN A 1 1068 ? 179.358 216.490 247.369 1.00 71.41  ? 1051 ASN B OD1 1 
ATOM   8278  N ND2 . ASN A 1 1068 ? 177.642 217.759 248.062 1.00 71.41  ? 1051 ASN B ND2 1 
ATOM   8279  N N   . ASN A 1 1069 ? 178.086 216.988 243.162 1.00 64.51  ? 1052 ASN B N   1 
ATOM   8280  C CA  . ASN A 1 1069 ? 177.248 216.017 242.479 1.00 64.51  ? 1052 ASN B CA  1 
ATOM   8281  C C   . ASN A 1 1069 ? 177.971 215.466 241.260 1.00 64.51  ? 1052 ASN B C   1 
ATOM   8282  O O   . ASN A 1 1069 ? 178.742 216.168 240.604 1.00 64.51  ? 1052 ASN B O   1 
ATOM   8283  C CB  . ASN A 1 1069 ? 175.927 216.649 242.044 1.00 64.51  ? 1052 ASN B CB  1 
ATOM   8284  C CG  . ASN A 1 1069 ? 175.227 217.367 243.173 1.00 64.51  ? 1052 ASN B CG  1 
ATOM   8285  O OD1 . ASN A 1 1069 ? 175.833 217.665 244.200 1.00 64.51  ? 1052 ASN B OD1 1 
ATOM   8286  N ND2 . ASN A 1 1069 ? 173.945 217.652 242.989 1.00 64.51  ? 1052 ASN B ND2 1 
ATOM   8287  N N   . ILE A 1 1070 ? 177.717 214.196 240.964 1.00 60.08  ? 1053 ILE B N   1 
ATOM   8288  C CA  . ILE A 1 1070 ? 178.211 213.560 239.750 1.00 60.08  ? 1053 ILE B CA  1 
ATOM   8289  C C   . ILE A 1 1070 ? 177.015 213.048 238.961 1.00 60.08  ? 1053 ILE B C   1 
ATOM   8290  O O   . ILE A 1 1070 ? 176.175 212.320 239.502 1.00 60.08  ? 1053 ILE B O   1 
ATOM   8291  C CB  . ILE A 1 1070 ? 179.202 212.426 240.059 1.00 60.08  ? 1053 ILE B CB  1 
ATOM   8292  C CG1 . ILE A 1 1070 ? 180.472 213.001 240.681 1.00 60.08  ? 1053 ILE B CG1 1 
ATOM   8293  C CG2 . ILE A 1 1070 ? 179.548 211.672 238.798 1.00 60.08  ? 1053 ILE B CG2 1 
ATOM   8294  C CD1 . ILE A 1 1070 ? 181.501 211.961 241.034 1.00 60.08  ? 1053 ILE B CD1 1 
ATOM   8295  N N   . MET A 1 1071 ? 176.951 213.428 237.686 1.00 64.04  ? 1054 MET B N   1 
ATOM   8296  C CA  . MET A 1 1071 ? 175.813 213.194 236.802 1.00 64.04  ? 1054 MET B CA  1 
ATOM   8297  C C   . MET A 1 1071 ? 176.203 212.179 235.735 1.00 64.04  ? 1054 MET B C   1 
ATOM   8298  O O   . MET A 1 1071 ? 176.927 212.517 234.795 1.00 64.04  ? 1054 MET B O   1 
ATOM   8299  C CB  . MET A 1 1071 ? 175.391 214.502 236.136 1.00 64.04  ? 1054 MET B CB  1 
ATOM   8300  C CG  . MET A 1 1071 ? 174.173 215.215 236.691 1.00 64.04  ? 1054 MET B CG  1 
ATOM   8301  S SD  . MET A 1 1071 ? 172.701 214.194 236.797 1.00 64.04  ? 1054 MET B SD  1 
ATOM   8302  C CE  . MET A 1 1071 ? 172.595 213.997 238.560 1.00 64.04  ? 1054 MET B CE  1 
ATOM   8303  N N   . PHE A 1 1072 ? 175.718 210.946 235.863 1.00 54.17  ? 1055 PHE B N   1 
ATOM   8304  C CA  . PHE A 1 1072 ? 175.814 209.969 234.781 1.00 54.17  ? 1055 PHE B CA  1 
ATOM   8305  C C   . PHE A 1 1072 ? 174.548 210.109 233.950 1.00 54.17  ? 1055 PHE B C   1 
ATOM   8306  O O   . PHE A 1 1072 ? 173.524 209.485 234.233 1.00 54.17  ? 1055 PHE B O   1 
ATOM   8307  C CB  . PHE A 1 1072 ? 175.963 208.553 235.321 1.00 54.17  ? 1055 PHE B CB  1 
ATOM   8308  C CG  . PHE A 1 1072 ? 177.170 208.348 236.182 1.00 54.17  ? 1055 PHE B CG  1 
ATOM   8309  C CD1 . PHE A 1 1072 ? 177.151 208.688 237.518 1.00 54.17  ? 1055 PHE B CD1 1 
ATOM   8310  C CD2 . PHE A 1 1072 ? 178.317 207.790 235.660 1.00 54.17  ? 1055 PHE B CD2 1 
ATOM   8311  C CE1 . PHE A 1 1072 ? 178.254 208.489 238.311 1.00 54.17  ? 1055 PHE B CE1 1 
ATOM   8312  C CE2 . PHE A 1 1072 ? 179.423 207.591 236.451 1.00 54.17  ? 1055 PHE B CE2 1 
ATOM   8313  C CZ  . PHE A 1 1072 ? 179.391 207.943 237.778 1.00 54.17  ? 1055 PHE B CZ  1 
ATOM   8314  N N   . LYS A 1 1073 ? 174.608 210.947 232.918 1.00 57.52  ? 1056 LYS B N   1 
ATOM   8315  C CA  . LYS A 1 1073 ? 173.430 211.209 232.105 1.00 57.52  ? 1056 LYS B CA  1 
ATOM   8316  C C   . LYS A 1 1073 ? 173.859 211.791 230.769 1.00 57.52  ? 1056 LYS B C   1 
ATOM   8317  O O   . LYS A 1 1073 ? 174.728 212.662 230.719 1.00 57.52  ? 1056 LYS B O   1 
ATOM   8318  C CB  . LYS A 1 1073 ? 172.471 212.170 232.815 1.00 57.52  ? 1056 LYS B CB  1 
ATOM   8319  C CG  . LYS A 1 1073 ? 171.415 212.776 231.915 1.00 57.52  ? 1056 LYS B CG  1 
ATOM   8320  C CD  . LYS A 1 1073 ? 170.394 213.557 232.713 1.00 57.52  ? 1056 LYS B CD  1 
ATOM   8321  C CE  . LYS A 1 1073 ? 170.864 214.974 232.959 1.00 57.52  ? 1056 LYS B CE  1 
ATOM   8322  N NZ  . LYS A 1 1073 ? 169.752 215.951 232.825 1.00 57.52  ? 1056 LYS B NZ  1 
ATOM   8323  N N   . LEU A 1 1074 ? 173.237 211.313 229.694 1.00 51.66  ? 1057 LEU B N   1 
ATOM   8324  C CA  . LEU A 1 1074 ? 173.509 211.823 228.355 1.00 51.66  ? 1057 LEU B CA  1 
ATOM   8325  C C   . LEU A 1 1074 ? 172.764 213.138 228.170 1.00 51.66  ? 1057 LEU B C   1 
ATOM   8326  O O   . LEU A 1 1074 ? 171.533 213.154 228.079 1.00 51.66  ? 1057 LEU B O   1 
ATOM   8327  C CB  . LEU A 1 1074 ? 173.092 210.802 227.302 1.00 51.66  ? 1057 LEU B CB  1 
ATOM   8328  C CG  . LEU A 1 1074 ? 174.135 209.752 226.934 1.00 51.66  ? 1057 LEU B CG  1 
ATOM   8329  C CD1 . LEU A 1 1074 ? 174.105 208.619 227.928 1.00 51.66  ? 1057 LEU B CD1 1 
ATOM   8330  C CD2 . LEU A 1 1074 ? 173.884 209.239 225.537 1.00 51.66  ? 1057 LEU B CD2 1 
ATOM   8331  N N   . ASP A 1 1075 ? 173.505 214.239 228.108 1.00 55.76  ? 1058 ASP B N   1 
ATOM   8332  C CA  . ASP A 1 1075 ? 172.929 215.574 228.027 1.00 55.76  ? 1058 ASP B CA  1 
ATOM   8333  C C   . ASP A 1 1075 ? 173.372 216.246 226.737 1.00 55.76  ? 1058 ASP B C   1 
ATOM   8334  O O   . ASP A 1 1075 ? 174.559 216.224 226.398 1.00 55.76  ? 1058 ASP B O   1 
ATOM   8335  C CB  . ASP A 1 1075 ? 173.345 216.422 229.230 1.00 55.76  ? 1058 ASP B CB  1 
ATOM   8336  C CG  . ASP A 1 1075 ? 172.168 217.094 229.905 1.00 55.76  ? 1058 ASP B CG  1 
ATOM   8337  O OD1 . ASP A 1 1075 ? 171.154 217.346 229.223 1.00 55.76  ? 1058 ASP B OD1 1 
ATOM   8338  O OD2 . ASP A 1 1075 ? 172.257 217.371 231.118 1.00 55.76  ? 1058 ASP B OD2 1 
ATOM   8339  N N   . GLY A 1 1076 ? 172.423 216.850 226.029 1.00 60.86  ? 1059 GLY B N   1 
ATOM   8340  C CA  . GLY A 1 1076 ? 172.724 217.575 224.815 1.00 60.86  ? 1059 GLY B CA  1 
ATOM   8341  C C   . GLY A 1 1076 ? 172.839 216.733 223.565 1.00 60.86  ? 1059 GLY B C   1 
ATOM   8342  O O   . GLY A 1 1076 ? 173.175 217.277 222.506 1.00 60.86  ? 1059 GLY B O   1 
ATOM   8343  N N   . CYS A 1 1077 ? 172.571 215.433 223.644 1.00 61.23  ? 1060 CYS B N   1 
ATOM   8344  C CA  . CYS A 1 1077 ? 172.661 214.562 222.479 1.00 61.23  ? 1060 CYS B CA  1 
ATOM   8345  C C   . CYS A 1 1077 ? 171.414 214.725 221.620 1.00 61.23  ? 1060 CYS B C   1 
ATOM   8346  O O   . CYS A 1 1077 ? 170.297 214.481 222.087 1.00 61.23  ? 1060 CYS B O   1 
ATOM   8347  C CB  . CYS A 1 1077 ? 172.828 213.109 222.911 1.00 61.23  ? 1060 CYS B CB  1 
ATOM   8348  S SG  . CYS A 1 1077 ? 172.898 211.943 221.540 1.00 61.23  ? 1060 CYS B SG  1 
ATOM   8349  N N   . ARG A 1 1078 ? 171.605 215.133 220.365 1.00 61.16  ? 1061 ARG B N   1 
ATOM   8350  C CA  . ARG A 1 1078 ? 170.475 215.328 219.465 1.00 61.16  ? 1061 ARG B CA  1 
ATOM   8351  C C   . ARG A 1 1078 ? 169.926 214.012 218.931 1.00 61.16  ? 1061 ARG B C   1 
ATOM   8352  O O   . ARG A 1 1078 ? 168.737 213.934 218.604 1.00 61.16  ? 1061 ARG B O   1 
ATOM   8353  C CB  . ARG A 1 1078 ? 170.881 216.239 218.308 1.00 61.16  ? 1061 ARG B CB  1 
ATOM   8354  C CG  . ARG A 1 1078 ? 171.332 217.615 218.748 1.00 61.16  ? 1061 ARG B CG  1 
ATOM   8355  C CD  . ARG A 1 1078 ? 171.708 218.476 217.559 1.00 61.16  ? 1061 ARG B CD  1 
ATOM   8356  N NE  . ARG A 1 1078 ? 172.676 219.503 217.921 1.00 61.16  ? 1061 ARG B NE  1 
ATOM   8357  C CZ  . ARG A 1 1078 ? 173.694 219.874 217.158 1.00 61.16  ? 1061 ARG B CZ  1 
ATOM   8358  N NH1 . ARG A 1 1078 ? 173.908 219.323 215.975 1.00 61.16  ? 1061 ARG B NH1 1 
ATOM   8359  N NH2 . ARG A 1 1078 ? 174.517 220.823 217.592 1.00 61.16  ? 1061 ARG B NH2 1 
ATOM   8360  N N   . ASP A 1 1079 ? 170.762 212.983 218.819 1.00 62.42  ? 1062 ASP B N   1 
ATOM   8361  C CA  . ASP A 1 1079 ? 170.272 211.667 218.434 1.00 62.42  ? 1062 ASP B CA  1 
ATOM   8362  C C   . ASP A 1 1079 ? 169.337 211.132 219.510 1.00 62.42  ? 1062 ASP B C   1 
ATOM   8363  O O   . ASP A 1 1079 ? 169.647 211.191 220.703 1.00 62.42  ? 1062 ASP B O   1 
ATOM   8364  C CB  . ASP A 1 1079 ? 171.444 210.714 218.217 1.00 62.42  ? 1062 ASP B CB  1 
ATOM   8365  C CG  . ASP A 1 1079 ? 171.039 209.446 217.499 1.00 62.42  ? 1062 ASP B CG  1 
ATOM   8366  O OD1 . ASP A 1 1079 ? 169.864 209.343 217.093 1.00 62.42  ? 1062 ASP B OD1 1 
ATOM   8367  O OD2 . ASP A 1 1079 ? 171.898 208.555 217.332 1.00 62.42  ? 1062 ASP B OD2 1 
ATOM   8368  N N   . THR A 1 1080 ? 168.188 210.607 219.090 1.00 61.95  ? 1063 THR B N   1 
ATOM   8369  C CA  . THR A 1 1080 ? 167.136 210.262 220.039 1.00 61.95  ? 1063 THR B CA  1 
ATOM   8370  C C   . THR A 1 1080 ? 167.271 208.861 220.617 1.00 61.95  ? 1063 THR B C   1 
ATOM   8371  O O   . THR A 1 1080 ? 166.785 208.614 221.726 1.00 61.95  ? 1063 THR B O   1 
ATOM   8372  C CB  . THR A 1 1080 ? 165.763 210.404 219.379 1.00 61.95  ? 1063 THR B CB  1 
ATOM   8373  O OG1 . THR A 1 1080 ? 165.554 209.318 218.470 1.00 61.95  ? 1063 THR B OG1 1 
ATOM   8374  C CG2 . THR A 1 1080 ? 165.675 211.714 218.618 1.00 61.95  ? 1063 THR B CG2 1 
ATOM   8375  N N   . HIS A 1 1081 ? 167.904 207.935 219.903 1.00 64.17  ? 1064 HIS B N   1 
ATOM   8376  C CA  . HIS A 1 1081 ? 168.049 206.565 220.375 1.00 64.17  ? 1064 HIS B CA  1 
ATOM   8377  C C   . HIS A 1 1081 ? 169.444 206.266 220.905 1.00 64.17  ? 1064 HIS B C   1 
ATOM   8378  O O   . HIS A 1 1081 ? 169.766 205.099 221.148 1.00 64.17  ? 1064 HIS B O   1 
ATOM   8379  C CB  . HIS A 1 1081 ? 167.698 205.584 219.257 1.00 64.17  ? 1064 HIS B CB  1 
ATOM   8380  C CG  . HIS A 1 1081 ? 166.357 205.827 218.639 1.00 64.17  ? 1064 HIS B CG  1 
ATOM   8381  N ND1 . HIS A 1 1081 ? 165.194 205.298 219.153 1.00 64.17  ? 1064 HIS B ND1 1 
ATOM   8382  C CD2 . HIS A 1 1081 ? 165.996 206.537 217.545 1.00 64.17  ? 1064 HIS B CD2 1 
ATOM   8383  C CE1 . HIS A 1 1081 ? 164.173 205.676 218.405 1.00 64.17  ? 1064 HIS B CE1 1 
ATOM   8384  N NE2 . HIS A 1 1081 ? 164.633 206.429 217.423 1.00 64.17  ? 1064 HIS B NE2 1 
ATOM   8385  N N   . ARG A 1 1082 ? 170.275 207.285 221.086 1.00 56.62  ? 1065 ARG B N   1 
ATOM   8386  C CA  . ARG A 1 1082 ? 171.639 207.074 221.549 1.00 56.62  ? 1065 ARG B CA  1 
ATOM   8387  C C   . ARG A 1 1082 ? 171.644 206.522 222.969 1.00 56.62  ? 1065 ARG B C   1 
ATOM   8388  O O   . ARG A 1 1082 ? 170.802 206.879 223.795 1.00 56.62  ? 1065 ARG B O   1 
ATOM   8389  C CB  . ARG A 1 1082 ? 172.417 208.387 221.482 1.00 56.62  ? 1065 ARG B CB  1 
ATOM   8390  C CG  . ARG A 1 1082 ? 173.906 208.282 221.759 1.00 56.62  ? 1065 ARG B CG  1 
ATOM   8391  C CD  . ARG A 1 1082 ? 174.554 207.122 221.028 1.00 56.62  ? 1065 ARG B CD  1 
ATOM   8392  N NE  . ARG A 1 1082 ? 174.295 207.154 219.596 1.00 56.62  ? 1065 ARG B NE  1 
ATOM   8393  C CZ  . ARG A 1 1082 ? 174.641 206.188 218.758 1.00 56.62  ? 1065 ARG B CZ  1 
ATOM   8394  N NH1 . ARG A 1 1082 ? 175.296 205.117 219.172 1.00 56.62  ? 1065 ARG B NH1 1 
ATOM   8395  N NH2 . ARG A 1 1082 ? 174.323 206.300 217.473 1.00 56.62  ? 1065 ARG B NH2 1 
ATOM   8396  N N   . TYR A 1 1083 ? 172.592 205.631 223.244 1.00 54.44  ? 1066 TYR B N   1 
ATOM   8397  C CA  . TYR A 1 1083 ? 172.743 205.056 224.572 1.00 54.44  ? 1066 TYR B CA  1 
ATOM   8398  C C   . TYR A 1 1083 ? 174.172 204.561 224.722 1.00 54.44  ? 1066 TYR B C   1 
ATOM   8399  O O   . TYR A 1 1083 ? 174.885 204.372 223.735 1.00 54.44  ? 1066 TYR B O   1 
ATOM   8400  C CB  . TYR A 1 1083 ? 171.746 203.920 224.810 1.00 54.44  ? 1066 TYR B CB  1 
ATOM   8401  C CG  . TYR A 1 1083 ? 172.024 202.673 224.009 1.00 54.44  ? 1066 TYR B CG  1 
ATOM   8402  C CD1 . TYR A 1 1083 ? 171.585 202.554 222.702 1.00 54.44  ? 1066 TYR B CD1 1 
ATOM   8403  C CD2 . TYR A 1 1083 ? 172.714 201.610 224.566 1.00 54.44  ? 1066 TYR B CD2 1 
ATOM   8404  C CE1 . TYR A 1 1083 ? 171.832 201.416 221.971 1.00 54.44  ? 1066 TYR B CE1 1 
ATOM   8405  C CE2 . TYR A 1 1083 ? 172.965 200.469 223.842 1.00 54.44  ? 1066 TYR B CE2 1 
ATOM   8406  C CZ  . TYR A 1 1083 ? 172.522 200.376 222.546 1.00 54.44  ? 1066 TYR B CZ  1 
ATOM   8407  O OH  . TYR A 1 1083 ? 172.772 199.236 221.822 1.00 54.44  ? 1066 TYR B OH  1 
ATOM   8408  N N   . ILE A 1 1084 ? 174.589 204.362 225.972 1.00 49.00  ? 1067 ILE B N   1 
ATOM   8409  C CA  . ILE A 1 1084 ? 175.939 203.897 226.268 1.00 49.00  ? 1067 ILE B CA  1 
ATOM   8410  C C   . ILE A 1 1084 ? 175.891 202.833 227.353 1.00 49.00  ? 1067 ILE B C   1 
ATOM   8411  O O   . ILE A 1 1084 ? 174.916 202.714 228.099 1.00 49.00  ? 1067 ILE B O   1 
ATOM   8412  C CB  . ILE A 1 1084 ? 176.880 205.037 226.710 1.00 49.00  ? 1067 ILE B CB  1 
ATOM   8413  C CG1 . ILE A 1 1084 ? 176.388 205.655 228.014 1.00 49.00  ? 1067 ILE B CG1 1 
ATOM   8414  C CG2 . ILE A 1 1084 ? 177.003 206.088 225.628 1.00 49.00  ? 1067 ILE B CG2 1 
ATOM   8415  C CD1 . ILE A 1 1084 ? 177.365 206.615 228.629 1.00 49.00  ? 1067 ILE B CD1 1 
ATOM   8416  N N   . TRP A 1 1085 ? 176.968 202.053 227.434 1.00 64.42  ? 1068 TRP B N   1 
ATOM   8417  C CA  . TRP A 1 1085 ? 177.189 201.134 228.541 1.00 64.42  ? 1068 TRP B CA  1 
ATOM   8418  C C   . TRP A 1 1085 ? 178.392 201.616 229.335 1.00 64.42  ? 1068 TRP B C   1 
ATOM   8419  O O   . TRP A 1 1085 ? 179.440 201.909 228.756 1.00 64.42  ? 1068 TRP B O   1 
ATOM   8420  C CB  . TRP A 1 1085 ? 177.431 199.709 228.045 1.00 64.42  ? 1068 TRP B CB  1 
ATOM   8421  C CG  . TRP A 1 1085 ? 176.282 199.100 227.324 1.00 64.42  ? 1068 TRP B CG  1 
ATOM   8422  C CD1 . TRP A 1 1085 ? 175.956 199.274 226.016 1.00 64.42  ? 1068 TRP B CD1 1 
ATOM   8423  C CD2 . TRP A 1 1085 ? 175.316 198.194 227.862 1.00 64.42  ? 1068 TRP B CD2 1 
ATOM   8424  N NE1 . TRP A 1 1085 ? 174.838 198.542 225.705 1.00 64.42  ? 1068 TRP B NE1 1 
ATOM   8425  C CE2 . TRP A 1 1085 ? 174.426 197.870 226.824 1.00 64.42  ? 1068 TRP B CE2 1 
ATOM   8426  C CE3 . TRP A 1 1085 ? 175.112 197.632 229.123 1.00 64.42  ? 1068 TRP B CE3 1 
ATOM   8427  C CZ2 . TRP A 1 1085 ? 173.351 197.009 227.007 1.00 64.42  ? 1068 TRP B CZ2 1 
ATOM   8428  C CZ3 . TRP A 1 1085 ? 174.044 196.776 229.302 1.00 64.42  ? 1068 TRP B CZ3 1 
ATOM   8429  C CH2 . TRP A 1 1085 ? 173.178 196.474 228.252 1.00 64.42  ? 1068 TRP B CH2 1 
ATOM   8430  N N   . ILE A 1 1086 ? 178.244 201.697 230.651 1.00 47.47  ? 1069 ILE B N   1 
ATOM   8431  C CA  . ILE A 1 1086 ? 179.309 202.152 231.535 1.00 47.47  ? 1069 ILE B CA  1 
ATOM   8432  C C   . ILE A 1 1086 ? 179.383 201.202 232.720 1.00 47.47  ? 1069 ILE B C   1 
ATOM   8433  O O   . ILE A 1 1086 ? 178.353 200.729 233.212 1.00 47.47  ? 1069 ILE B O   1 
ATOM   8434  C CB  . ILE A 1 1086 ? 179.081 203.608 231.991 1.00 47.47  ? 1069 ILE B CB  1 
ATOM   8435  C CG1 . ILE A 1 1086 ? 180.221 204.082 232.888 1.00 47.47  ? 1069 ILE B CG1 1 
ATOM   8436  C CG2 . ILE A 1 1086 ? 177.750 203.751 232.699 1.00 47.47  ? 1069 ILE B CG2 1 
ATOM   8437  C CD1 . ILE A 1 1086 ? 180.349 205.583 232.955 1.00 47.47  ? 1069 ILE B CD1 1 
ATOM   8438  N N   . LYS A 1 1087 ? 180.600 200.896 233.160 1.00 58.65  ? 1070 LYS B N   1 
ATOM   8439  C CA  . LYS A 1 1087 ? 180.765 200.003 234.296 1.00 58.65  ? 1070 LYS B CA  1 
ATOM   8440  C C   . LYS A 1 1087 ? 182.114 200.248 234.953 1.00 58.65  ? 1070 LYS B C   1 
ATOM   8441  O O   . LYS A 1 1087 ? 183.004 200.884 234.379 1.00 58.65  ? 1070 LYS B O   1 
ATOM   8442  C CB  . LYS A 1 1087 ? 180.628 198.536 233.880 1.00 58.65  ? 1070 LYS B CB  1 
ATOM   8443  C CG  . LYS A 1 1087 ? 181.818 197.988 233.132 1.00 58.65  ? 1070 LYS B CG  1 
ATOM   8444  C CD  . LYS A 1 1087 ? 181.819 196.470 233.145 1.00 58.65  ? 1070 LYS B CD  1 
ATOM   8445  C CE  . LYS A 1 1087 ? 182.919 195.914 232.263 1.00 58.65  ? 1070 LYS B CE  1 
ATOM   8446  N NZ  . LYS A 1 1087 ? 183.144 194.466 232.504 1.00 58.65  ? 1070 LYS B NZ  1 
ATOM   8447  N N   . TYR A 1 1088 ? 182.238 199.743 236.181 1.00 60.00  ? 1071 TYR B N   1 
ATOM   8448  C CA  . TYR A 1 1088 ? 183.481 199.789 236.951 1.00 60.00  ? 1071 TYR B CA  1 
ATOM   8449  C C   . TYR A 1 1088 ? 184.029 201.207 237.071 1.00 60.00  ? 1071 TYR B C   1 
ATOM   8450  O O   . TYR A 1 1088 ? 185.228 201.443 236.919 1.00 60.00  ? 1071 TYR B O   1 
ATOM   8451  C CB  . TYR A 1 1088 ? 184.537 198.863 236.350 1.00 60.00  ? 1071 TYR B CB  1 
ATOM   8452  C CG  . TYR A 1 1088 ? 184.306 197.397 236.612 1.00 60.00  ? 1071 TYR B CG  1 
ATOM   8453  C CD1 . TYR A 1 1088 ? 184.157 196.919 237.901 1.00 60.00  ? 1071 TYR B CD1 1 
ATOM   8454  C CD2 . TYR A 1 1088 ? 184.275 196.486 235.570 1.00 60.00  ? 1071 TYR B CD2 1 
ATOM   8455  C CE1 . TYR A 1 1088 ? 183.956 195.579 238.142 1.00 60.00  ? 1071 TYR B CE1 1 
ATOM   8456  C CE2 . TYR A 1 1088 ? 184.076 195.145 235.801 1.00 60.00  ? 1071 TYR B CE2 1 
ATOM   8457  C CZ  . TYR A 1 1088 ? 183.919 194.696 237.089 1.00 60.00  ? 1071 TYR B CZ  1 
ATOM   8458  O OH  . TYR A 1 1088 ? 183.721 193.356 237.324 1.00 60.00  ? 1071 TYR B OH  1 
ATOM   8459  N N   . PHE A 1 1089 ? 183.150 202.164 237.344 1.00 57.53  ? 1072 PHE B N   1 
ATOM   8460  C CA  . PHE A 1 1089 ? 183.613 203.526 237.564 1.00 57.53  ? 1072 PHE B CA  1 
ATOM   8461  C C   . PHE A 1 1089 ? 184.438 203.596 238.841 1.00 57.53  ? 1072 PHE B C   1 
ATOM   8462  O O   . PHE A 1 1089 ? 184.123 202.946 239.839 1.00 57.53  ? 1072 PHE B O   1 
ATOM   8463  C CB  . PHE A 1 1089 ? 182.437 204.494 237.645 1.00 57.53  ? 1072 PHE B CB  1 
ATOM   8464  C CG  . PHE A 1 1089 ? 182.850 205.933 237.754 1.00 57.53  ? 1072 PHE B CG  1 
ATOM   8465  C CD1 . PHE A 1 1089 ? 183.160 206.664 236.625 1.00 57.53  ? 1072 PHE B CD1 1 
ATOM   8466  C CD2 . PHE A 1 1089 ? 182.932 206.553 238.986 1.00 57.53  ? 1072 PHE B CD2 1 
ATOM   8467  C CE1 . PHE A 1 1089 ? 183.541 207.984 236.722 1.00 57.53  ? 1072 PHE B CE1 1 
ATOM   8468  C CE2 . PHE A 1 1089 ? 183.312 207.874 239.086 1.00 57.53  ? 1072 PHE B CE2 1 
ATOM   8469  C CZ  . PHE A 1 1089 ? 183.617 208.588 237.952 1.00 57.53  ? 1072 PHE B CZ  1 
ATOM   8470  N N   . ASN A 1 1090 ? 185.507 204.385 238.799 1.00 59.38  ? 1073 ASN B N   1 
ATOM   8471  C CA  . ASN A 1 1090 ? 186.408 204.534 239.931 1.00 59.38  ? 1073 ASN B CA  1 
ATOM   8472  C C   . ASN A 1 1090 ? 187.049 205.909 239.871 1.00 59.38  ? 1073 ASN B C   1 
ATOM   8473  O O   . ASN A 1 1090 ? 187.396 206.392 238.790 1.00 59.38  ? 1073 ASN B O   1 
ATOM   8474  C CB  . ASN A 1 1090 ? 187.497 203.457 239.934 1.00 59.38  ? 1073 ASN B CB  1 
ATOM   8475  C CG  . ASN A 1 1090 ? 187.040 202.165 240.569 1.00 59.38  ? 1073 ASN B CG  1 
ATOM   8476  O OD1 . ASN A 1 1090 ? 186.459 201.307 239.909 1.00 59.38  ? 1073 ASN B OD1 1 
ATOM   8477  N ND2 . ASN A 1 1090 ? 187.311 202.014 241.858 1.00 59.38  ? 1073 ASN B ND2 1 
ATOM   8478  N N   . LEU A 1 1091 ? 187.211 206.525 241.035 1.00 53.34  ? 1074 LEU B N   1 
ATOM   8479  C CA  . LEU A 1 1091 ? 187.892 207.803 241.159 1.00 53.34  ? 1074 LEU B CA  1 
ATOM   8480  C C   . LEU A 1 1091 ? 189.011 207.664 242.180 1.00 53.34  ? 1074 LEU B C   1 
ATOM   8481  O O   . LEU A 1 1091 ? 188.897 206.906 243.146 1.00 53.34  ? 1074 LEU B O   1 
ATOM   8482  C CB  . LEU A 1 1091 ? 186.915 208.914 241.567 1.00 53.34  ? 1074 LEU B CB  1 
ATOM   8483  C CG  . LEU A 1 1091 ? 187.333 210.368 241.353 1.00 53.34  ? 1074 LEU B CG  1 
ATOM   8484  C CD1 . LEU A 1 1091 ? 187.193 210.744 239.899 1.00 53.34  ? 1074 LEU B CD1 1 
ATOM   8485  C CD2 . LEU A 1 1091 ? 186.488 211.289 242.206 1.00 53.34  ? 1074 LEU B CD2 1 
ATOM   8486  N N   . PHE A 1 1092 ? 190.099 208.391 241.954 1.00 62.39  ? 1075 PHE B N   1 
ATOM   8487  C CA  . PHE A 1 1092 ? 191.269 208.352 242.815 1.00 62.39  ? 1075 PHE B CA  1 
ATOM   8488  C C   . PHE A 1 1092 ? 191.721 209.772 243.114 1.00 62.39  ? 1075 PHE B C   1 
ATOM   8489  O O   . PHE A 1 1092 ? 191.603 210.666 242.272 1.00 62.39  ? 1075 PHE B O   1 
ATOM   8490  C CB  . PHE A 1 1092 ? 192.422 207.578 242.172 1.00 62.39  ? 1075 PHE B CB  1 
ATOM   8491  C CG  . PHE A 1 1092 ? 192.055 206.196 241.724 1.00 62.39  ? 1075 PHE B CG  1 
ATOM   8492  C CD1 . PHE A 1 1092 ? 191.915 205.171 242.638 1.00 62.39  ? 1075 PHE B CD1 1 
ATOM   8493  C CD2 . PHE A 1 1092 ? 191.852 205.920 240.386 1.00 62.39  ? 1075 PHE B CD2 1 
ATOM   8494  C CE1 . PHE A 1 1092 ? 191.583 203.899 242.226 1.00 62.39  ? 1075 PHE B CE1 1 
ATOM   8495  C CE2 . PHE A 1 1092 ? 191.518 204.650 239.970 1.00 62.39  ? 1075 PHE B CE2 1 
ATOM   8496  C CZ  . PHE A 1 1092 ? 191.383 203.640 240.892 1.00 62.39  ? 1075 PHE B CZ  1 
ATOM   8497  N N   . ASP A 1 1093 ? 192.264 209.964 244.312 1.00 66.41  ? 1076 ASP B N   1 
ATOM   8498  C CA  . ASP A 1 1093 ? 192.670 211.279 244.787 1.00 66.41  ? 1076 ASP B CA  1 
ATOM   8499  C C   . ASP A 1 1093 ? 194.134 211.590 244.505 1.00 66.41  ? 1076 ASP B C   1 
ATOM   8500  O O   . ASP A 1 1093 ? 194.666 212.553 245.065 1.00 66.41  ? 1076 ASP B O   1 
ATOM   8501  C CB  . ASP A 1 1093 ? 192.400 211.402 246.287 1.00 66.41  ? 1076 ASP B CB  1 
ATOM   8502  C CG  . ASP A 1 1093 ? 192.999 210.261 247.079 1.00 66.41  ? 1076 ASP B CG  1 
ATOM   8503  O OD1 . ASP A 1 1093 ? 193.440 209.274 246.456 1.00 66.41  ? 1076 ASP B OD1 1 
ATOM   8504  O OD2 . ASP A 1 1093 ? 193.029 210.351 248.324 1.00 66.41  ? 1076 ASP B OD2 1 
ATOM   8505  N N   . LYS A 1 1094 ? 194.796 210.801 243.664 1.00 65.86  ? 1077 LYS B N   1 
ATOM   8506  C CA  . LYS A 1 1094 ? 196.187 211.044 243.318 1.00 65.86  ? 1077 LYS B CA  1 
ATOM   8507  C C   . LYS A 1 1094 ? 196.427 210.648 241.870 1.00 65.86  ? 1077 LYS B C   1 
ATOM   8508  O O   . LYS A 1 1094 ? 195.695 209.840 241.295 1.00 65.86  ? 1077 LYS B O   1 
ATOM   8509  C CB  . LYS A 1 1094 ? 197.136 210.275 244.240 1.00 65.86  ? 1077 LYS B CB  1 
ATOM   8510  C CG  . LYS A 1 1094 ? 197.131 208.778 244.008 1.00 65.86  ? 1077 LYS B CG  1 
ATOM   8511  C CD  . LYS A 1 1094 ? 198.354 208.120 244.613 1.00 65.86  ? 1077 LYS B CD  1 
ATOM   8512  C CE  . LYS A 1 1094 ? 198.322 206.621 244.392 1.00 65.86  ? 1077 LYS B CE  1 
ATOM   8513  N NZ  . LYS A 1 1094 ? 196.937 206.093 244.511 1.00 65.86  ? 1077 LYS B NZ  1 
ATOM   8514  N N   . GLU A 1 1095 ? 197.466 211.235 241.283 1.00 66.16  ? 1078 GLU B N   1 
ATOM   8515  C CA  . GLU A 1 1095 ? 197.859 210.881 239.928 1.00 66.16  ? 1078 GLU B CA  1 
ATOM   8516  C C   . GLU A 1 1095 ? 198.336 209.435 239.875 1.00 66.16  ? 1078 GLU B C   1 
ATOM   8517  O O   . GLU A 1 1095 ? 198.993 208.946 240.796 1.00 66.16  ? 1078 GLU B O   1 
ATOM   8518  C CB  . GLU A 1 1095 ? 198.961 211.816 239.434 1.00 66.16  ? 1078 GLU B CB  1 
ATOM   8519  C CG  . GLU A 1 1095 ? 198.977 212.011 237.931 1.00 66.16  ? 1078 GLU B CG  1 
ATOM   8520  C CD  . GLU A 1 1095 ? 200.172 212.818 237.461 1.00 66.16  ? 1078 GLU B CD  1 
ATOM   8521  O OE1 . GLU A 1 1095 ? 201.138 212.964 238.239 1.00 66.16  ? 1078 GLU B OE1 1 
ATOM   8522  O OE2 . GLU A 1 1095 ? 200.151 213.299 236.308 1.00 66.16  ? 1078 GLU B OE2 1 
ATOM   8523  N N   . LEU A 1 1096 ? 198.003 208.752 238.786 1.00 64.01  ? 1079 LEU B N   1 
ATOM   8524  C CA  . LEU A 1 1096 ? 198.327 207.345 238.604 1.00 64.01  ? 1079 LEU B CA  1 
ATOM   8525  C C   . LEU A 1 1096 ? 199.388 207.204 237.523 1.00 64.01  ? 1079 LEU B C   1 
ATOM   8526  O O   . LEU A 1 1096 ? 199.224 207.728 236.417 1.00 64.01  ? 1079 LEU B O   1 
ATOM   8527  C CB  . LEU A 1 1096 ? 197.081 206.546 238.222 1.00 64.01  ? 1079 LEU B CB  1 
ATOM   8528  C CG  . LEU A 1 1096 ? 196.160 206.089 239.352 1.00 64.01  ? 1079 LEU B CG  1 
ATOM   8529  C CD1 . LEU A 1 1096 ? 195.222 205.009 238.858 1.00 64.01  ? 1079 LEU B CD1 1 
ATOM   8530  C CD2 . LEU A 1 1096 ? 196.972 205.586 240.526 1.00 64.01  ? 1079 LEU B CD2 1 
ATOM   8531  N N   . ASN A 1 1097 ? 200.470 206.499 237.842 1.00 70.76  ? 1080 ASN B N   1 
ATOM   8532  C CA  . ASN A 1 1097 ? 201.512 206.247 236.861 1.00 70.76  ? 1080 ASN B CA  1 
ATOM   8533  C C   . ASN A 1 1097 ? 201.104 205.090 235.951 1.00 70.76  ? 1080 ASN B C   1 
ATOM   8534  O O   . ASN A 1 1097 ? 200.057 204.463 236.129 1.00 70.76  ? 1080 ASN B O   1 
ATOM   8535  C CB  . ASN A 1 1097 ? 202.844 205.972 237.556 1.00 70.76  ? 1080 ASN B CB  1 
ATOM   8536  C CG  . ASN A 1 1097 ? 202.765 204.824 238.539 1.00 70.76  ? 1080 ASN B CG  1 
ATOM   8537  O OD1 . ASN A 1 1097 ? 202.500 203.684 238.162 1.00 70.76  ? 1080 ASN B OD1 1 
ATOM   8538  N ND2 . ASN A 1 1097 ? 203.002 205.120 239.810 1.00 70.76  ? 1080 ASN B ND2 1 
ATOM   8539  N N   . GLU A 1 1098 ? 201.948 204.800 234.960 1.00 73.54  ? 1081 GLU B N   1 
ATOM   8540  C CA  . GLU A 1 1098 ? 201.604 203.785 233.968 1.00 73.54  ? 1081 GLU B CA  1 
ATOM   8541  C C   . GLU A 1 1098 ? 201.500 202.400 234.594 1.00 73.54  ? 1081 GLU B C   1 
ATOM   8542  O O   . GLU A 1 1098 ? 200.655 201.594 234.188 1.00 73.54  ? 1081 GLU B O   1 
ATOM   8543  C CB  . GLU A 1 1098 ? 202.633 203.786 232.840 1.00 73.54  ? 1081 GLU B CB  1 
ATOM   8544  C CG  . GLU A 1 1098 ? 202.447 204.909 231.834 1.00 73.54  ? 1081 GLU B CG  1 
ATOM   8545  C CD  . GLU A 1 1098 ? 203.059 206.216 232.295 1.00 73.54  ? 1081 GLU B CD  1 
ATOM   8546  O OE1 . GLU A 1 1098 ? 203.568 206.268 233.434 1.00 73.54  ? 1081 GLU B OE1 1 
ATOM   8547  O OE2 . GLU A 1 1098 ? 203.033 207.193 231.518 1.00 73.54  ? 1081 GLU B OE2 1 
ATOM   8548  N N   . LYS A 1 1099 ? 202.358 202.098 235.571 1.00 71.13  ? 1082 LYS B N   1 
ATOM   8549  C CA  . LYS A 1 1099 ? 202.325 200.780 236.194 1.00 71.13  ? 1082 LYS B CA  1 
ATOM   8550  C C   . LYS A 1 1099 ? 201.002 200.535 236.908 1.00 71.13  ? 1082 LYS B C   1 
ATOM   8551  O O   . LYS A 1 1099 ? 200.414 199.454 236.786 1.00 71.13  ? 1082 LYS B O   1 
ATOM   8552  C CB  . LYS A 1 1099 ? 203.497 200.626 237.163 1.00 71.13  ? 1082 LYS B CB  1 
ATOM   8553  C CG  . LYS A 1 1099 ? 203.583 199.258 237.826 1.00 71.13  ? 1082 LYS B CG  1 
ATOM   8554  C CD  . LYS A 1 1099 ? 203.425 198.128 236.818 1.00 71.13  ? 1082 LYS B CD  1 
ATOM   8555  C CE  . LYS A 1 1099 ? 204.643 198.001 235.918 1.00 71.13  ? 1082 LYS B CE  1 
ATOM   8556  N NZ  . LYS A 1 1099 ? 204.647 196.712 235.173 1.00 71.13  ? 1082 LYS B NZ  1 
ATOM   8557  N N   . GLU A 1 1100 ? 200.513 201.528 237.653 1.00 72.68  ? 1083 GLU B N   1 
ATOM   8558  C CA  . GLU A 1 1100 ? 199.236 201.362 238.338 1.00 72.68  ? 1083 GLU B CA  1 
ATOM   8559  C C   . GLU A 1 1100 ? 198.089 201.248 237.345 1.00 72.68  ? 1083 GLU B C   1 
ATOM   8560  O O   . GLU A 1 1100 ? 197.134 200.500 237.578 1.00 72.68  ? 1083 GLU B O   1 
ATOM   8561  C CB  . GLU A 1 1100 ? 198.999 202.517 239.308 1.00 72.68  ? 1083 GLU B CB  1 
ATOM   8562  C CG  . GLU A 1 1100 ? 199.953 202.532 240.490 1.00 72.68  ? 1083 GLU B CG  1 
ATOM   8563  C CD  . GLU A 1 1100 ? 200.315 203.934 240.932 1.00 72.68  ? 1083 GLU B CD  1 
ATOM   8564  O OE1 . GLU A 1 1100 ? 200.204 204.865 240.109 1.00 72.68  ? 1083 GLU B OE1 1 
ATOM   8565  O OE2 . GLU A 1 1100 ? 200.711 204.105 242.104 1.00 72.68  ? 1083 GLU B OE2 1 
ATOM   8566  N N   . ILE A 1 1101 ? 198.166 201.975 236.229 1.00 66.83  ? 1084 ILE B N   1 
ATOM   8567  C CA  . ILE A 1 1101 ? 197.127 201.878 235.207 1.00 66.83  ? 1084 ILE B CA  1 
ATOM   8568  C C   . ILE A 1 1101 ? 197.096 200.480 234.606 1.00 66.83  ? 1084 ILE B C   1 
ATOM   8569  O O   . ILE A 1 1101 ? 196.024 199.889 234.420 1.00 66.83  ? 1084 ILE B O   1 
ATOM   8570  C CB  . ILE A 1 1101 ? 197.342 202.951 234.128 1.00 66.83  ? 1084 ILE B CB  1 
ATOM   8571  C CG1 . ILE A 1 1101 ? 197.188 204.345 234.731 1.00 66.83  ? 1084 ILE B CG1 1 
ATOM   8572  C CG2 . ILE A 1 1101 ? 196.375 202.749 232.982 1.00 66.83  ? 1084 ILE B CG2 1 
ATOM   8573  C CD1 . ILE A 1 1101 ? 195.773 204.690 235.100 1.00 66.83  ? 1084 ILE B CD1 1 
ATOM   8574  N N   . LYS A 1 1102 ? 198.268 199.928 234.289 1.00 68.51  ? 1085 LYS B N   1 
ATOM   8575  C CA  . LYS A 1 1102 ? 198.318 198.578 233.739 1.00 68.51  ? 1085 LYS B CA  1 
ATOM   8576  C C   . LYS A 1 1102 ? 197.834 197.550 234.754 1.00 68.51  ? 1085 LYS B C   1 
ATOM   8577  O O   . LYS A 1 1102 ? 197.149 196.588 234.391 1.00 68.51  ? 1085 LYS B O   1 
ATOM   8578  C CB  . LYS A 1 1102 ? 199.735 198.252 233.272 1.00 68.51  ? 1085 LYS B CB  1 
ATOM   8579  C CG  . LYS A 1 1102 ? 199.915 196.821 232.799 1.00 68.51  ? 1085 LYS B CG  1 
ATOM   8580  C CD  . LYS A 1 1102 ? 198.992 196.500 231.634 1.00 68.51  ? 1085 LYS B CD  1 
ATOM   8581  C CE  . LYS A 1 1102 ? 199.325 197.337 230.412 1.00 68.51  ? 1085 LYS B CE  1 
ATOM   8582  N NZ  . LYS A 1 1102 ? 200.673 197.013 229.874 1.00 68.51  ? 1085 LYS B NZ  1 
ATOM   8583  N N   . ASP A 1 1103 ? 198.181 197.732 236.030 1.00 71.58  ? 1086 ASP B N   1 
ATOM   8584  C CA  . ASP A 1 1103 ? 197.692 196.821 237.060 1.00 71.58  ? 1086 ASP B CA  1 
ATOM   8585  C C   . ASP A 1 1103 ? 196.175 196.889 237.181 1.00 71.58  ? 1086 ASP B C   1 
ATOM   8586  O O   . ASP A 1 1103 ? 195.511 195.858 237.342 1.00 71.58  ? 1086 ASP B O   1 
ATOM   8587  C CB  . ASP A 1 1103 ? 198.354 197.139 238.399 1.00 71.58  ? 1086 ASP B CB  1 
ATOM   8588  C CG  . ASP A 1 1103 ? 199.782 196.639 238.474 1.00 71.58  ? 1086 ASP B CG  1 
ATOM   8589  O OD1 . ASP A 1 1103 ? 200.140 195.743 237.683 1.00 71.58  ? 1086 ASP B OD1 1 
ATOM   8590  O OD2 . ASP A 1 1103 ? 200.545 197.141 239.325 1.00 71.58  ? 1086 ASP B OD2 1 
ATOM   8591  N N   . LEU A 1 1104 ? 195.609 198.096 237.113 1.00 66.29  ? 1087 LEU B N   1 
ATOM   8592  C CA  . LEU A 1 1104 ? 194.158 198.243 237.133 1.00 66.29  ? 1087 LEU B CA  1 
ATOM   8593  C C   . LEU A 1 1104 ? 193.520 197.544 235.943 1.00 66.29  ? 1087 LEU B C   1 
ATOM   8594  O O   . LEU A 1 1104 ? 192.502 196.856 236.086 1.00 66.29  ? 1087 LEU B O   1 
ATOM   8595  C CB  . LEU A 1 1104 ? 193.786 199.725 237.138 1.00 66.29  ? 1087 LEU B CB  1 
ATOM   8596  C CG  . LEU A 1 1104 ? 192.657 200.167 238.061 1.00 66.29  ? 1087 LEU B CG  1 
ATOM   8597  C CD1 . LEU A 1 1104 ? 192.849 199.596 239.448 1.00 66.29  ? 1087 LEU B CD1 1 
ATOM   8598  C CD2 . LEU A 1 1104 ? 192.594 201.679 238.109 1.00 66.29  ? 1087 LEU B CD2 1 
ATOM   8599  N N   . TYR A 1 1105 ? 194.108 197.710 234.757 1.00 64.34  ? 1088 TYR B N   1 
ATOM   8600  C CA  . TYR A 1 1105 ? 193.585 197.046 233.569 1.00 64.34  ? 1088 TYR B CA  1 
ATOM   8601  C C   . TYR A 1 1105 ? 193.623 195.532 233.725 1.00 64.34  ? 1088 TYR B C   1 
ATOM   8602  O O   . TYR A 1 1105 ? 192.666 194.838 233.365 1.00 64.34  ? 1088 TYR B O   1 
ATOM   8603  C CB  . TYR A 1 1105 ? 194.382 197.480 232.341 1.00 64.34  ? 1088 TYR B CB  1 
ATOM   8604  C CG  . TYR A 1 1105 ? 193.853 196.950 231.032 1.00 64.34  ? 1088 TYR B CG  1 
ATOM   8605  C CD1 . TYR A 1 1105 ? 192.499 196.726 230.848 1.00 64.34  ? 1088 TYR B CD1 1 
ATOM   8606  C CD2 . TYR A 1 1105 ? 194.710 196.676 229.979 1.00 64.34  ? 1088 TYR B CD2 1 
ATOM   8607  C CE1 . TYR A 1 1105 ? 192.015 196.242 229.653 1.00 64.34  ? 1088 TYR B CE1 1 
ATOM   8608  C CE2 . TYR A 1 1105 ? 194.235 196.192 228.781 1.00 64.34  ? 1088 TYR B CE2 1 
ATOM   8609  C CZ  . TYR A 1 1105 ? 192.886 195.977 228.624 1.00 64.34  ? 1088 TYR B CZ  1 
ATOM   8610  O OH  . TYR A 1 1105 ? 192.405 195.494 227.430 1.00 64.34  ? 1088 TYR B OH  1 
ATOM   8611  N N   . ASP A 1 1106 ? 194.723 195.004 234.262 1.00 70.79  ? 1089 ASP B N   1 
ATOM   8612  C CA  . ASP A 1 1106 ? 194.838 193.562 234.451 1.00 70.79  ? 1089 ASP B CA  1 
ATOM   8613  C C   . ASP A 1 1106 ? 193.826 193.048 235.469 1.00 70.79  ? 1089 ASP B C   1 
ATOM   8614  O O   . ASP A 1 1106 ? 193.216 191.992 235.266 1.00 70.79  ? 1089 ASP B O   1 
ATOM   8615  C CB  . ASP A 1 1106 ? 196.259 193.203 234.881 1.00 70.79  ? 1089 ASP B CB  1 
ATOM   8616  C CG  . ASP A 1 1106 ? 197.220 193.137 233.713 1.00 70.79  ? 1089 ASP B CG  1 
ATOM   8617  O OD1 . ASP A 1 1106 ? 196.750 193.088 232.558 1.00 70.79  ? 1089 ASP B OD1 1 
ATOM   8618  O OD2 . ASP A 1 1106 ? 198.446 193.136 233.950 1.00 70.79  ? 1089 ASP B OD2 1 
ATOM   8619  N N   . ASN A 1 1107 ? 193.641 193.774 236.573 1.00 71.38  ? 1090 ASN B N   1 
ATOM   8620  C CA  . ASN A 1 1107 ? 192.731 193.312 237.617 1.00 71.38  ? 1090 ASN B CA  1 
ATOM   8621  C C   . ASN A 1 1107 ? 191.280 193.365 237.155 1.00 71.38  ? 1090 ASN B C   1 
ATOM   8622  O O   . ASN A 1 1107 ? 190.534 192.392 237.309 1.00 71.38  ? 1090 ASN B O   1 
ATOM   8623  C CB  . ASN A 1 1107 ? 192.919 194.145 238.884 1.00 71.38  ? 1090 ASN B CB  1 
ATOM   8624  C CG  . ASN A 1 1107 ? 194.319 194.040 239.446 1.00 71.38  ? 1090 ASN B CG  1 
ATOM   8625  O OD1 . ASN A 1 1107 ? 195.173 193.349 238.891 1.00 71.38  ? 1090 ASN B OD1 1 
ATOM   8626  N ND2 . ASN A 1 1107 ? 194.566 194.730 240.553 1.00 71.38  ? 1090 ASN B ND2 1 
ATOM   8627  N N   . GLN A 1 1108 ? 190.862 194.493 236.581 1.00 66.99  ? 1091 GLN B N   1 
ATOM   8628  C CA  . GLN A 1 1108 ? 189.465 194.672 236.210 1.00 66.99  ? 1091 GLN B CA  1 
ATOM   8629  C C   . GLN A 1 1108 ? 189.069 193.892 234.965 1.00 66.99  ? 1091 GLN B C   1 
ATOM   8630  O O   . GLN A 1 1108 ? 187.873 193.792 234.675 1.00 66.99  ? 1091 GLN B O   1 
ATOM   8631  C CB  . GLN A 1 1108 ? 189.163 196.156 235.999 1.00 66.99  ? 1091 GLN B CB  1 
ATOM   8632  C CG  . GLN A 1 1108 ? 189.415 197.015 237.223 1.00 66.99  ? 1091 GLN B CG  1 
ATOM   8633  C CD  . GLN A 1 1108 ? 188.687 198.340 237.163 1.00 66.99  ? 1091 GLN B CD  1 
ATOM   8634  O OE1 . GLN A 1 1108 ? 188.300 198.798 236.090 1.00 66.99  ? 1091 GLN B OE1 1 
ATOM   8635  N NE2 . GLN A 1 1108 ? 188.500 198.965 238.316 1.00 66.99  ? 1091 GLN B NE2 1 
ATOM   8636  N N   . SER A 1 1109 ? 190.031 193.337 234.226 1.00 70.24  ? 1092 SER B N   1 
ATOM   8637  C CA  . SER A 1 1109 ? 189.697 192.616 233.004 1.00 70.24  ? 1092 SER B CA  1 
ATOM   8638  C C   . SER A 1 1109 ? 188.969 191.306 233.276 1.00 70.24  ? 1092 SER B C   1 
ATOM   8639  O O   . SER A 1 1109 ? 188.253 190.824 232.394 1.00 70.24  ? 1092 SER B O   1 
ATOM   8640  C CB  . SER A 1 1109 ? 190.961 192.345 232.188 1.00 70.24  ? 1092 SER B CB  1 
ATOM   8641  O OG  . SER A 1 1109 ? 192.072 192.118 233.034 1.00 70.24  ? 1092 SER B OG  1 
ATOM   8642  N N   . ASN A 1 1110 ? 189.130 190.727 234.467 1.00 75.01  ? 1093 ASN B N   1 
ATOM   8643  C CA  . ASN A 1 1110 ? 188.485 189.467 234.840 1.00 75.01  ? 1093 ASN B CA  1 
ATOM   8644  C C   . ASN A 1 1110 ? 188.875 188.352 233.865 1.00 75.01  ? 1093 ASN B C   1 
ATOM   8645  O O   . ASN A 1 1110 ? 188.061 187.820 233.109 1.00 75.01  ? 1093 ASN B O   1 
ATOM   8646  C CB  . ASN A 1 1110 ? 186.963 189.635 234.920 1.00 75.01  ? 1093 ASN B CB  1 
ATOM   8647  C CG  . ASN A 1 1110 ? 186.355 188.854 236.061 1.00 75.01  ? 1093 ASN B CG  1 
ATOM   8648  O OD1 . ASN A 1 1110 ? 186.994 187.972 236.634 1.00 75.01  ? 1093 ASN B OD1 1 
ATOM   8649  N ND2 . ASN A 1 1110 ? 185.113 189.176 236.403 1.00 75.01  ? 1093 ASN B ND2 1 
ATOM   8650  N N   . SER A 1 1111 ? 190.166 188.019 233.909 1.00 78.72  ? 1094 SER B N   1 
ATOM   8651  C CA  . SER A 1 1111 ? 190.727 187.044 232.981 1.00 78.72  ? 1094 SER B CA  1 
ATOM   8652  C C   . SER A 1 1111 ? 190.170 185.642 233.188 1.00 78.72  ? 1094 SER B C   1 
ATOM   8653  O O   . SER A 1 1111 ? 190.344 184.785 232.315 1.00 78.72  ? 1094 SER B O   1 
ATOM   8654  C CB  . SER A 1 1111 ? 192.248 187.016 233.112 1.00 78.72  ? 1094 SER B CB  1 
ATOM   8655  O OG  . SER A 1 1111 ? 192.641 187.114 234.468 1.00 78.72  ? 1094 SER B OG  1 
ATOM   8656  N N   . GLY A 1 1112 ? 189.513 185.382 234.315 1.00 78.12  ? 1095 GLY B N   1 
ATOM   8657  C CA  . GLY A 1 1112 ? 188.998 184.047 234.561 1.00 78.12  ? 1095 GLY B CA  1 
ATOM   8658  C C   . GLY A 1 1112 ? 187.847 183.634 233.668 1.00 78.12  ? 1095 GLY B C   1 
ATOM   8659  O O   . GLY A 1 1112 ? 187.511 182.446 233.636 1.00 78.12  ? 1095 GLY B O   1 
ATOM   8660  N N   . ILE A 1 1113 ? 187.243 184.572 232.944 1.00 74.88  ? 1096 ILE B N   1 
ATOM   8661  C CA  . ILE A 1 1113 ? 186.059 184.311 232.135 1.00 74.88  ? 1096 ILE B CA  1 
ATOM   8662  C C   . ILE A 1 1113 ? 186.369 184.651 230.686 1.00 74.88  ? 1096 ILE B C   1 
ATOM   8663  O O   . ILE A 1 1113 ? 186.824 185.762 230.389 1.00 74.88  ? 1096 ILE B O   1 
ATOM   8664  C CB  . ILE A 1 1113 ? 184.848 185.118 232.636 1.00 74.88  ? 1096 ILE B CB  1 
ATOM   8665  C CG1 . ILE A 1 1113 ? 184.436 184.645 234.029 1.00 74.88  ? 1096 ILE B CG1 1 
ATOM   8666  C CG2 . ILE A 1 1113 ? 183.694 185.001 231.665 1.00 74.88  ? 1096 ILE B CG2 1 
ATOM   8667  C CD1 . ILE A 1 1113 ? 183.832 185.730 234.881 1.00 74.88  ? 1096 ILE B CD1 1 
ATOM   8668  N N   . LEU A 1 1114 ? 186.120 183.702 229.788 1.00 74.40  ? 1097 LEU B N   1 
ATOM   8669  C CA  . LEU A 1 1114 ? 186.293 183.952 228.366 1.00 74.40  ? 1097 LEU B CA  1 
ATOM   8670  C C   . LEU A 1 1114 ? 185.274 184.975 227.880 1.00 74.40  ? 1097 LEU B C   1 
ATOM   8671  O O   . LEU A 1 1114 ? 184.156 185.065 228.393 1.00 74.40  ? 1097 LEU B O   1 
ATOM   8672  C CB  . LEU A 1 1114 ? 186.154 182.654 227.577 1.00 74.40  ? 1097 LEU B CB  1 
ATOM   8673  C CG  . LEU A 1 1114 ? 187.234 181.614 227.862 1.00 74.40  ? 1097 LEU B CG  1 
ATOM   8674  C CD1 . LEU A 1 1114 ? 186.662 180.486 228.678 1.00 74.40  ? 1097 LEU B CD1 1 
ATOM   8675  C CD2 . LEU A 1 1114 ? 187.816 181.081 226.572 1.00 74.40  ? 1097 LEU B CD2 1 
ATOM   8676  N N   . LYS A 1 1115 ? 185.671 185.758 226.879 1.00 68.47  ? 1098 LYS B N   1 
ATOM   8677  C CA  . LYS A 1 1115 ? 184.877 186.883 226.413 1.00 68.47  ? 1098 LYS B CA  1 
ATOM   8678  C C   . LYS A 1 1115 ? 184.653 186.796 224.911 1.00 68.47  ? 1098 LYS B C   1 
ATOM   8679  O O   . LYS A 1 1115 ? 185.515 186.331 224.162 1.00 68.47  ? 1098 LYS B O   1 
ATOM   8680  C CB  . LYS A 1 1115 ? 185.552 188.211 226.759 1.00 68.47  ? 1098 LYS B CB  1 
ATOM   8681  C CG  . LYS A 1 1115 ? 186.556 188.099 227.883 1.00 68.47  ? 1098 LYS B CG  1 
ATOM   8682  C CD  . LYS A 1 1115 ? 187.079 189.453 228.298 1.00 68.47  ? 1098 LYS B CD  1 
ATOM   8683  C CE  . LYS A 1 1115 ? 187.728 189.372 229.660 1.00 68.47  ? 1098 LYS B CE  1 
ATOM   8684  N NZ  . LYS A 1 1115 ? 186.769 188.872 230.679 1.00 68.47  ? 1098 LYS B NZ  1 
ATOM   8685  N N   . ASP A 1 1116 ? 183.487 187.263 224.477 1.00 64.52  ? 1099 ASP B N   1 
ATOM   8686  C CA  . ASP A 1 1116 ? 183.136 187.264 223.065 1.00 64.52  ? 1099 ASP B CA  1 
ATOM   8687  C C   . ASP A 1 1116 ? 183.795 188.457 222.373 1.00 64.52  ? 1099 ASP B C   1 
ATOM   8688  O O   . ASP A 1 1116 ? 184.691 189.106 222.916 1.00 64.52  ? 1099 ASP B O   1 
ATOM   8689  C CB  . ASP A 1 1116 ? 181.620 187.255 222.897 1.00 64.52  ? 1099 ASP B CB  1 
ATOM   8690  C CG  . ASP A 1 1116 ? 180.936 188.367 223.663 1.00 64.52  ? 1099 ASP B CG  1 
ATOM   8691  O OD1 . ASP A 1 1116 ? 181.588 189.386 223.967 1.00 64.52  ? 1099 ASP B OD1 1 
ATOM   8692  O OD2 . ASP A 1 1116 ? 179.732 188.223 223.959 1.00 64.52  ? 1099 ASP B OD2 1 
ATOM   8693  N N   . PHE A 1 1117 ? 183.358 188.750 221.148 1.00 57.41  ? 1100 PHE B N   1 
ATOM   8694  C CA  . PHE A 1 1117 ? 183.965 189.835 220.385 1.00 57.41  ? 1100 PHE B CA  1 
ATOM   8695  C C   . PHE A 1 1117 ? 183.746 191.181 221.064 1.00 57.41  ? 1100 PHE B C   1 
ATOM   8696  O O   . PHE A 1 1117 ? 184.684 191.971 221.216 1.00 57.41  ? 1100 PHE B O   1 
ATOM   8697  C CB  . PHE A 1 1117 ? 183.398 189.853 218.968 1.00 57.41  ? 1100 PHE B CB  1 
ATOM   8698  C CG  . PHE A 1 1117 ? 184.032 190.873 218.076 1.00 57.41  ? 1100 PHE B CG  1 
ATOM   8699  C CD1 . PHE A 1 1117 ? 185.334 190.721 217.649 1.00 57.41  ? 1100 PHE B CD1 1 
ATOM   8700  C CD2 . PHE A 1 1117 ? 183.325 191.987 217.669 1.00 57.41  ? 1100 PHE B CD2 1 
ATOM   8701  C CE1 . PHE A 1 1117 ? 185.918 191.656 216.829 1.00 57.41  ? 1100 PHE B CE1 1 
ATOM   8702  C CE2 . PHE A 1 1117 ? 183.905 192.926 216.851 1.00 57.41  ? 1100 PHE B CE2 1 
ATOM   8703  C CZ  . PHE A 1 1117 ? 185.203 192.761 216.430 1.00 57.41  ? 1100 PHE B CZ  1 
ATOM   8704  N N   . TRP A 1 1118 ? 182.512 191.457 221.487 1.00 58.31  ? 1101 TRP B N   1 
ATOM   8705  C CA  . TRP A 1 1118 ? 182.186 192.764 222.043 1.00 58.31  ? 1101 TRP B CA  1 
ATOM   8706  C C   . TRP A 1 1118 ? 182.796 192.998 223.416 1.00 58.31  ? 1101 TRP B C   1 
ATOM   8707  O O   . TRP A 1 1118 ? 182.783 194.137 223.891 1.00 58.31  ? 1101 TRP B O   1 
ATOM   8708  C CB  . TRP A 1 1118 ? 180.672 192.941 222.127 1.00 58.31  ? 1101 TRP B CB  1 
ATOM   8709  C CG  . TRP A 1 1118 ? 179.947 192.468 220.918 1.00 58.31  ? 1101 TRP B CG  1 
ATOM   8710  C CD1 . TRP A 1 1118 ? 179.050 191.449 220.853 1.00 58.31  ? 1101 TRP B CD1 1 
ATOM   8711  C CD2 . TRP A 1 1118 ? 180.048 192.999 219.594 1.00 58.31  ? 1101 TRP B CD2 1 
ATOM   8712  N NE1 . TRP A 1 1118 ? 178.588 191.307 219.570 1.00 58.31  ? 1101 TRP B NE1 1 
ATOM   8713  C CE2 . TRP A 1 1118 ? 179.187 192.249 218.778 1.00 58.31  ? 1101 TRP B CE2 1 
ATOM   8714  C CE3 . TRP A 1 1118 ? 180.786 194.035 219.020 1.00 58.31  ? 1101 TRP B CE3 1 
ATOM   8715  C CZ2 . TRP A 1 1118 ? 179.043 192.499 217.422 1.00 58.31  ? 1101 TRP B CZ2 1 
ATOM   8716  C CZ3 . TRP A 1 1118 ? 180.641 194.282 217.675 1.00 58.31  ? 1101 TRP B CZ3 1 
ATOM   8717  C CH2 . TRP A 1 1118 ? 179.777 193.519 216.890 1.00 58.31  ? 1101 TRP B CH2 1 
ATOM   8718  N N   . GLY A 1 1119 ? 183.324 191.965 224.061 1.00 61.08  ? 1102 GLY B N   1 
ATOM   8719  C CA  . GLY A 1 1119 ? 183.883 192.102 225.386 1.00 61.08  ? 1102 GLY B CA  1 
ATOM   8720  C C   . GLY A 1 1119 ? 182.976 191.687 226.520 1.00 61.08  ? 1102 GLY B C   1 
ATOM   8721  O O   . GLY A 1 1119 ? 183.319 191.933 227.681 1.00 61.08  ? 1102 GLY B O   1 
ATOM   8722  N N   . ASP A 1 1120 ? 181.834 191.073 226.227 1.00 66.01  ? 1103 ASP B N   1 
ATOM   8723  C CA  . ASP A 1 1120 ? 180.928 190.590 227.259 1.00 66.01  ? 1103 ASP B CA  1 
ATOM   8724  C C   . ASP A 1 1120 ? 181.424 189.239 227.772 1.00 66.01  ? 1103 ASP B C   1 
ATOM   8725  O O   . ASP A 1 1120 ? 182.533 188.799 227.463 1.00 66.01  ? 1103 ASP B O   1 
ATOM   8726  C CB  . ASP A 1 1120 ? 179.505 190.512 226.715 1.00 66.01  ? 1103 ASP B CB  1 
ATOM   8727  C CG  . ASP A 1 1120 ? 178.764 191.826 226.833 1.00 66.01  ? 1103 ASP B CG  1 
ATOM   8728  O OD1 . ASP A 1 1120 ? 178.897 192.494 227.879 1.00 66.01  ? 1103 ASP B OD1 1 
ATOM   8729  O OD2 . ASP A 1 1120 ? 178.045 192.193 225.882 1.00 66.01  ? 1103 ASP B OD2 1 
ATOM   8730  N N   . TYR A 1 1121 ? 180.605 188.560 228.569 1.00 70.16  ? 1104 TYR B N   1 
ATOM   8731  C CA  . TYR A 1 1121 ? 180.948 187.241 229.083 1.00 70.16  ? 1104 TYR B CA  1 
ATOM   8732  C C   . TYR A 1 1121 ? 180.469 186.174 228.109 1.00 70.16  ? 1104 TYR B C   1 
ATOM   8733  O O   . TYR A 1 1121 ? 179.308 186.185 227.692 1.00 70.16  ? 1104 TYR B O   1 
ATOM   8734  C CB  . TYR A 1 1121 ? 180.319 187.008 230.457 1.00 70.16  ? 1104 TYR B CB  1 
ATOM   8735  C CG  . TYR A 1 1121 ? 180.937 187.806 231.581 1.00 70.16  ? 1104 TYR B CG  1 
ATOM   8736  C CD1 . TYR A 1 1121 ? 182.085 188.557 231.380 1.00 70.16  ? 1104 TYR B CD1 1 
ATOM   8737  C CD2 . TYR A 1 1121 ? 180.369 187.806 232.847 1.00 70.16  ? 1104 TYR B CD2 1 
ATOM   8738  C CE1 . TYR A 1 1121 ? 182.649 189.287 232.406 1.00 70.16  ? 1104 TYR B CE1 1 
ATOM   8739  C CE2 . TYR A 1 1121 ? 180.926 188.531 233.879 1.00 70.16  ? 1104 TYR B CE2 1 
ATOM   8740  C CZ  . TYR A 1 1121 ? 182.065 189.270 233.653 1.00 70.16  ? 1104 TYR B CZ  1 
ATOM   8741  O OH  . TYR A 1 1121 ? 182.626 189.996 234.678 1.00 70.16  ? 1104 TYR B OH  1 
ATOM   8742  N N   . LEU A 1 1122 ? 181.363 185.259 227.746 1.00 68.99  ? 1105 LEU B N   1 
ATOM   8743  C CA  . LEU A 1 1122 ? 180.970 184.145 226.896 1.00 68.99  ? 1105 LEU B CA  1 
ATOM   8744  C C   . LEU A 1 1122 ? 179.969 183.266 227.632 1.00 68.99  ? 1105 LEU B C   1 
ATOM   8745  O O   . LEU A 1 1122 ? 180.060 183.081 228.847 1.00 68.99  ? 1105 LEU B O   1 
ATOM   8746  C CB  . LEU A 1 1122 ? 182.195 183.331 226.486 1.00 68.99  ? 1105 LEU B CB  1 
ATOM   8747  C CG  . LEU A 1 1122 ? 182.077 182.550 225.180 1.00 68.99  ? 1105 LEU B CG  1 
ATOM   8748  C CD1 . LEU A 1 1122 ? 181.751 183.490 224.039 1.00 68.99  ? 1105 LEU B CD1 1 
ATOM   8749  C CD2 . LEU A 1 1122 ? 183.354 181.787 224.900 1.00 68.99  ? 1105 LEU B CD2 1 
ATOM   8750  N N   . GLN A 1 1123 ? 179.004 182.725 226.893 1.00 67.68  ? 1106 GLN B N   1 
ATOM   8751  C CA  . GLN A 1 1123 ? 177.882 182.028 227.500 1.00 67.68  ? 1106 GLN B CA  1 
ATOM   8752  C C   . GLN A 1 1123 ? 177.634 180.698 226.805 1.00 67.68  ? 1106 GLN B C   1 
ATOM   8753  O O   . GLN A 1 1123 ? 177.981 180.503 225.639 1.00 67.68  ? 1106 GLN B O   1 
ATOM   8754  C CB  . GLN A 1 1123 ? 176.612 182.884 227.458 1.00 67.68  ? 1106 GLN B CB  1 
ATOM   8755  C CG  . GLN A 1 1123 ? 176.695 184.133 228.310 1.00 67.68  ? 1106 GLN B CG  1 
ATOM   8756  C CD  . GLN A 1 1123 ? 175.387 184.885 228.369 1.00 67.68  ? 1106 GLN B CD  1 
ATOM   8757  O OE1 . GLN A 1 1123 ? 174.334 184.300 228.616 1.00 67.68  ? 1106 GLN B OE1 1 
ATOM   8758  N NE2 . GLN A 1 1123 ? 175.444 186.190 228.143 1.00 67.68  ? 1106 GLN B NE2 1 
ATOM   8759  N N   . TYR A 1 1124 ? 177.028 179.781 227.552 1.00 71.20  ? 1107 TYR B N   1 
ATOM   8760  C CA  . TYR A 1 1124 ? 176.654 178.477 227.029 1.00 71.20  ? 1107 TYR B CA  1 
ATOM   8761  C C   . TYR A 1 1124 ? 175.356 178.567 226.240 1.00 71.20  ? 1107 TYR B C   1 
ATOM   8762  O O   . TYR A 1 1124 ? 174.520 179.443 226.479 1.00 71.20  ? 1107 TYR B O   1 
ATOM   8763  C CB  . TYR A 1 1124 ? 176.482 177.473 228.168 1.00 71.20  ? 1107 TYR B CB  1 
ATOM   8764  C CG  . TYR A 1 1124 ? 177.772 176.920 228.722 1.00 71.20  ? 1107 TYR B CG  1 
ATOM   8765  C CD1 . TYR A 1 1124 ? 178.619 176.161 227.934 1.00 71.20  ? 1107 TYR B CD1 1 
ATOM   8766  C CD2 . TYR A 1 1124 ? 178.140 177.157 230.037 1.00 71.20  ? 1107 TYR B CD2 1 
ATOM   8767  C CE1 . TYR A 1 1124 ? 179.792 175.654 228.439 1.00 71.20  ? 1107 TYR B CE1 1 
ATOM   8768  C CE2 . TYR A 1 1124 ? 179.312 176.655 230.549 1.00 71.20  ? 1107 TYR B CE2 1 
ATOM   8769  C CZ  . TYR A 1 1124 ? 180.135 175.904 229.746 1.00 71.20  ? 1107 TYR B CZ  1 
ATOM   8770  O OH  . TYR A 1 1124 ? 181.307 175.401 230.257 1.00 71.20  ? 1107 TYR B OH  1 
ATOM   8771  N N   . ASP A 1 1125 ? 175.190 177.636 225.301 1.00 70.34  ? 1108 ASP B N   1 
ATOM   8772  C CA  . ASP A 1 1125 ? 173.954 177.503 224.531 1.00 70.34  ? 1108 ASP B CA  1 
ATOM   8773  C C   . ASP A 1 1125 ? 173.567 178.815 223.855 1.00 70.34  ? 1108 ASP B C   1 
ATOM   8774  O O   . ASP A 1 1125 ? 172.409 179.235 223.877 1.00 70.34  ? 1108 ASP B O   1 
ATOM   8775  C CB  . ASP A 1 1125 ? 172.815 176.989 225.411 1.00 70.34  ? 1108 ASP B CB  1 
ATOM   8776  C CG  . ASP A 1 1125 ? 172.743 175.478 225.443 1.00 70.34  ? 1108 ASP B CG  1 
ATOM   8777  O OD1 . ASP A 1 1125 ? 172.547 174.872 224.369 1.00 70.34  ? 1108 ASP B OD1 1 
ATOM   8778  O OD2 . ASP A 1 1125 ? 172.884 174.896 226.538 1.00 70.34  ? 1108 ASP B OD2 1 
ATOM   8779  N N   . LYS A 1 1126 ? 174.554 179.476 223.256 1.00 61.19  ? 1109 LYS B N   1 
ATOM   8780  C CA  . LYS A 1 1126 ? 174.331 180.692 222.493 1.00 61.19  ? 1109 LYS B CA  1 
ATOM   8781  C C   . LYS A 1 1126 ? 175.091 180.567 221.180 1.00 61.19  ? 1109 LYS B C   1 
ATOM   8782  O O   . LYS A 1 1126 ? 176.251 180.122 221.179 1.00 61.19  ? 1109 LYS B O   1 
ATOM   8783  C CB  . LYS A 1 1126 ? 174.792 181.928 223.272 1.00 61.19  ? 1109 LYS B CB  1 
ATOM   8784  C CG  . LYS A 1 1126 ? 174.342 183.245 222.678 1.00 61.19  ? 1109 LYS B CG  1 
ATOM   8785  C CD  . LYS A 1 1126 ? 174.716 184.407 223.580 1.00 61.19  ? 1109 LYS B CD  1 
ATOM   8786  C CE  . LYS A 1 1126 ? 174.409 185.738 222.915 1.00 61.19  ? 1109 LYS B CE  1 
ATOM   8787  N NZ  . LYS A 1 1126 ? 174.652 186.888 223.827 1.00 61.19  ? 1109 LYS B NZ  1 
ATOM   8788  N N   . PRO A 1 1127 ? 174.483 180.921 220.047 1.00 58.19  ? 1110 PRO B N   1 
ATOM   8789  C CA  . PRO A 1 1127 ? 175.175 180.795 218.756 1.00 58.19  ? 1110 PRO B CA  1 
ATOM   8790  C C   . PRO A 1 1127 ? 176.045 182.013 218.474 1.00 58.19  ? 1110 PRO B C   1 
ATOM   8791  O O   . PRO A 1 1127 ? 175.549 183.136 218.365 1.00 58.19  ? 1110 PRO B O   1 
ATOM   8792  C CB  . PRO A 1 1127 ? 174.024 180.678 217.752 1.00 58.19  ? 1110 PRO B CB  1 
ATOM   8793  C CG  . PRO A 1 1127 ? 172.906 181.417 218.390 1.00 58.19  ? 1110 PRO B CG  1 
ATOM   8794  C CD  . PRO A 1 1127 ? 173.065 181.280 219.882 1.00 58.19  ? 1110 PRO B CD  1 
ATOM   8795  N N   . TYR A 1 1128 ? 177.349 181.784 218.353 1.00 57.05  ? 1111 TYR B N   1 
ATOM   8796  C CA  . TYR A 1 1128 ? 178.313 182.819 218.014 1.00 57.05  ? 1111 TYR B CA  1 
ATOM   8797  C C   . TYR A 1 1128 ? 178.895 182.551 216.636 1.00 57.05  ? 1111 TYR B C   1 
ATOM   8798  O O   . TYR A 1 1128 ? 179.234 181.411 216.310 1.00 57.05  ? 1111 TYR B O   1 
ATOM   8799  C CB  . TYR A 1 1128 ? 179.463 182.876 219.020 1.00 57.05  ? 1111 TYR B CB  1 
ATOM   8800  C CG  . TYR A 1 1128 ? 179.067 183.084 220.457 1.00 57.05  ? 1111 TYR B CG  1 
ATOM   8801  C CD1 . TYR A 1 1128 ? 178.713 182.016 221.260 1.00 57.05  ? 1111 TYR B CD1 1 
ATOM   8802  C CD2 . TYR A 1 1128 ? 179.072 184.349 221.018 1.00 57.05  ? 1111 TYR B CD2 1 
ATOM   8803  C CE1 . TYR A 1 1128 ? 178.362 182.204 222.573 1.00 57.05  ? 1111 TYR B CE1 1 
ATOM   8804  C CE2 . TYR A 1 1128 ? 178.723 184.547 222.329 1.00 57.05  ? 1111 TYR B CE2 1 
ATOM   8805  C CZ  . TYR A 1 1128 ? 178.368 183.472 223.102 1.00 57.05  ? 1111 TYR B CZ  1 
ATOM   8806  O OH  . TYR A 1 1128 ? 178.017 183.667 224.415 1.00 57.05  ? 1111 TYR B OH  1 
ATOM   8807  N N   . TYR A 1 1129 ? 179.018 183.601 215.832 1.00 61.86  ? 1112 TYR B N   1 
ATOM   8808  C CA  . TYR A 1 1129 ? 179.791 183.488 214.607 1.00 61.86  ? 1112 TYR B CA  1 
ATOM   8809  C C   . TYR A 1 1129 ? 181.277 183.489 214.942 1.00 61.86  ? 1112 TYR B C   1 
ATOM   8810  O O   . TYR A 1 1129 ? 181.712 184.095 215.921 1.00 61.86  ? 1112 TYR B O   1 
ATOM   8811  C CB  . TYR A 1 1129 ? 179.458 184.632 213.655 1.00 61.86  ? 1112 TYR B CB  1 
ATOM   8812  C CG  . TYR A 1 1129 ? 177.994 184.720 213.299 1.00 61.86  ? 1112 TYR B CG  1 
ATOM   8813  C CD1 . TYR A 1 1129 ? 177.108 185.424 214.098 1.00 61.86  ? 1112 TYR B CD1 1 
ATOM   8814  C CD2 . TYR A 1 1129 ? 177.499 184.098 212.166 1.00 61.86  ? 1112 TYR B CD2 1 
ATOM   8815  C CE1 . TYR A 1 1129 ? 175.771 185.505 213.777 1.00 61.86  ? 1112 TYR B CE1 1 
ATOM   8816  C CE2 . TYR A 1 1129 ? 176.163 184.177 211.836 1.00 61.86  ? 1112 TYR B CE2 1 
ATOM   8817  C CZ  . TYR A 1 1129 ? 175.304 184.879 212.646 1.00 61.86  ? 1112 TYR B CZ  1 
ATOM   8818  O OH  . TYR A 1 1129 ? 173.971 184.957 212.320 1.00 61.86  ? 1112 TYR B OH  1 
ATOM   8819  N N   . MET A 1 1130 ? 182.061 182.796 214.126 1.00 64.85  ? 1113 MET B N   1 
ATOM   8820  C CA  . MET A 1 1130 ? 183.486 182.642 214.379 1.00 64.85  ? 1113 MET B CA  1 
ATOM   8821  C C   . MET A 1 1130 ? 184.292 183.591 213.508 1.00 64.85  ? 1113 MET B C   1 
ATOM   8822  O O   . MET A 1 1130 ? 183.984 183.779 212.328 1.00 64.85  ? 1113 MET B O   1 
ATOM   8823  C CB  . MET A 1 1130 ? 183.937 181.205 214.121 1.00 64.85  ? 1113 MET B CB  1 
ATOM   8824  C CG  . MET A 1 1130 ? 183.420 180.158 215.101 1.00 64.85  ? 1113 MET B CG  1 
ATOM   8825  S SD  . MET A 1 1130 ? 183.439 180.448 216.887 1.00 64.85  ? 1113 MET B SD  1 
ATOM   8826  C CE  . MET A 1 1130 ? 184.890 181.463 217.151 1.00 64.85  ? 1113 MET B CE  1 
ATOM   8827  N N   . LEU A 1 1131 ? 185.326 184.189 214.096 1.00 63.44  ? 1114 LEU B N   1 
ATOM   8828  C CA  . LEU A 1 1131 ? 186.264 185.012 213.345 1.00 63.44  ? 1114 LEU B CA  1 
ATOM   8829  C C   . LEU A 1 1131 ? 187.676 184.650 213.769 1.00 63.44  ? 1114 LEU B C   1 
ATOM   8830  O O   . LEU A 1 1131 ? 187.944 184.492 214.961 1.00 63.44  ? 1114 LEU B O   1 
ATOM   8831  C CB  . LEU A 1 1131 ? 185.998 186.503 213.574 1.00 63.44  ? 1114 LEU B CB  1 
ATOM   8832  C CG  . LEU A 1 1131 ? 187.042 187.503 213.084 1.00 63.44  ? 1114 LEU B CG  1 
ATOM   8833  C CD1 . LEU A 1 1131 ? 186.338 188.694 212.481 1.00 63.44  ? 1114 LEU B CD1 1 
ATOM   8834  C CD2 . LEU A 1 1131 ? 187.943 187.950 214.216 1.00 63.44  ? 1114 LEU B CD2 1 
ATOM   8835  N N   . ASN A 1 1132 ? 188.575 184.513 212.802 1.00 69.65  ? 1115 ASN B N   1 
ATOM   8836  C CA  . ASN A 1 1132 ? 189.965 184.180 213.080 1.00 69.65  ? 1115 ASN B CA  1 
ATOM   8837  C C   . ASN A 1 1132 ? 190.808 185.447 213.034 1.00 69.65  ? 1115 ASN B C   1 
ATOM   8838  O O   . ASN A 1 1132 ? 190.744 186.203 212.061 1.00 69.65  ? 1115 ASN B O   1 
ATOM   8839  C CB  . ASN A 1 1132 ? 190.493 183.159 212.076 1.00 69.65  ? 1115 ASN B CB  1 
ATOM   8840  C CG  . ASN A 1 1132 ? 191.784 182.518 212.529 1.00 69.65  ? 1115 ASN B CG  1 
ATOM   8841  O OD1 . ASN A 1 1132 ? 192.581 183.131 213.236 1.00 69.65  ? 1115 ASN B OD1 1 
ATOM   8842  N ND2 . ASN A 1 1132 ? 192.000 181.275 212.120 1.00 69.65  ? 1115 ASN B ND2 1 
ATOM   8843  N N   . LEU A 1 1133 ? 191.600 185.672 214.083 1.00 69.05  ? 1116 LEU B N   1 
ATOM   8844  C CA  . LEU A 1 1133 ? 192.420 186.877 214.133 1.00 69.05  ? 1116 LEU B CA  1 
ATOM   8845  C C   . LEU A 1 1133 ? 193.559 186.831 213.124 1.00 69.05  ? 1116 LEU B C   1 
ATOM   8846  O O   . LEU A 1 1133 ? 193.970 187.877 212.612 1.00 69.05  ? 1116 LEU B O   1 
ATOM   8847  C CB  . LEU A 1 1133 ? 192.969 187.080 215.542 1.00 69.05  ? 1116 LEU B CB  1 
ATOM   8848  C CG  . LEU A 1 1133 ? 192.037 187.772 216.535 1.00 69.05  ? 1116 LEU B CG  1 
ATOM   8849  C CD1 . LEU A 1 1133 ? 192.843 188.450 217.627 1.00 69.05  ? 1116 LEU B CD1 1 
ATOM   8850  C CD2 . LEU A 1 1133 ? 191.147 188.775 215.827 1.00 69.05  ? 1116 LEU B CD2 1 
ATOM   8851  N N   . TYR A 1 1134 ? 194.087 185.639 212.835 1.00 73.44  ? 1117 TYR B N   1 
ATOM   8852  C CA  . TYR A 1 1134 ? 195.165 185.527 211.859 1.00 73.44  ? 1117 TYR B CA  1 
ATOM   8853  C C   . TYR A 1 1134 ? 194.702 185.953 210.473 1.00 73.44  ? 1117 TYR B C   1 
ATOM   8854  O O   . TYR A 1 1134 ? 195.425 186.654 209.757 1.00 73.44  ? 1117 TYR B O   1 
ATOM   8855  C CB  . TYR A 1 1134 ? 195.693 184.095 211.827 1.00 73.44  ? 1117 TYR B CB  1 
ATOM   8856  C CG  . TYR A 1 1134 ? 197.045 183.949 211.168 1.00 73.44  ? 1117 TYR B CG  1 
ATOM   8857  C CD1 . TYR A 1 1134 ? 198.109 184.760 211.536 1.00 73.44  ? 1117 TYR B CD1 1 
ATOM   8858  C CD2 . TYR A 1 1134 ? 197.259 182.998 210.183 1.00 73.44  ? 1117 TYR B CD2 1 
ATOM   8859  C CE1 . TYR A 1 1134 ? 199.347 184.626 210.939 1.00 73.44  ? 1117 TYR B CE1 1 
ATOM   8860  C CE2 . TYR A 1 1134 ? 198.491 182.857 209.581 1.00 73.44  ? 1117 TYR B CE2 1 
ATOM   8861  C CZ  . TYR A 1 1134 ? 199.531 183.673 209.962 1.00 73.44  ? 1117 TYR B CZ  1 
ATOM   8862  O OH  . TYR A 1 1134 ? 200.761 183.534 209.363 1.00 73.44  ? 1117 TYR B OH  1 
ATOM   8863  N N   . ASP A 1 1135 ? 193.500 185.539 210.079 1.00 71.44  ? 1118 ASP B N   1 
ATOM   8864  C CA  . ASP A 1 1135 ? 192.922 185.873 208.778 1.00 71.44  ? 1118 ASP B CA  1 
ATOM   8865  C C   . ASP A 1 1135 ? 191.526 186.433 209.006 1.00 71.44  ? 1118 ASP B C   1 
ATOM   8866  O O   . ASP A 1 1135 ? 190.523 185.730 208.829 1.00 71.44  ? 1118 ASP B O   1 
ATOM   8867  C CB  . ASP A 1 1135 ? 192.889 184.653 207.857 1.00 71.44  ? 1118 ASP B CB  1 
ATOM   8868  C CG  . ASP A 1 1135 ? 193.337 184.977 206.450 1.00 71.44  ? 1118 ASP B CG  1 
ATOM   8869  O OD1 . ASP A 1 1135 ? 193.536 186.172 206.151 1.00 71.44  ? 1118 ASP B OD1 1 
ATOM   8870  O OD2 . ASP A 1 1135 ? 193.500 184.039 205.643 1.00 71.44  ? 1118 ASP B OD2 1 
ATOM   8871  N N   . PRO A 1 1136 ? 191.422 187.704 209.401 1.00 65.83  ? 1119 PRO B N   1 
ATOM   8872  C CA  . PRO A 1 1136 ? 190.112 188.286 209.709 1.00 65.83  ? 1119 PRO B CA  1 
ATOM   8873  C C   . PRO A 1 1136 ? 189.269 188.617 208.490 1.00 65.83  ? 1119 PRO B C   1 
ATOM   8874  O O   . PRO A 1 1136 ? 188.144 189.101 208.656 1.00 65.83  ? 1119 PRO B O   1 
ATOM   8875  C CB  . PRO A 1 1136 ? 190.487 189.560 210.474 1.00 65.83  ? 1119 PRO B CB  1 
ATOM   8876  C CG  . PRO A 1 1136 ? 191.786 189.957 209.885 1.00 65.83  ? 1119 PRO B CG  1 
ATOM   8877  C CD  . PRO A 1 1136 ? 192.515 188.672 209.597 1.00 65.83  ? 1119 PRO B CD  1 
ATOM   8878  N N   . ASN A 1 1137 ? 189.764 188.378 207.280 1.00 67.41  ? 1120 ASN B N   1 
ATOM   8879  C CA  . ASN A 1 1137 ? 189.035 188.697 206.062 1.00 67.41  ? 1120 ASN B CA  1 
ATOM   8880  C C   . ASN A 1 1137 ? 188.286 187.502 205.493 1.00 67.41  ? 1120 ASN B C   1 
ATOM   8881  O O   . ASN A 1 1137 ? 187.770 187.585 204.375 1.00 67.41  ? 1120 ASN B O   1 
ATOM   8882  C CB  . ASN A 1 1137 ? 189.988 189.260 205.008 1.00 67.41  ? 1120 ASN B CB  1 
ATOM   8883  C CG  . ASN A 1 1137 ? 189.293 190.183 204.033 1.00 67.41  ? 1120 ASN B CG  1 
ATOM   8884  O OD1 . ASN A 1 1137 ? 188.132 190.541 204.221 1.00 67.41  ? 1120 ASN B OD1 1 
ATOM   8885  N ND2 . ASN A 1 1137 ? 189.999 190.572 202.980 1.00 67.41  ? 1120 ASN B ND2 1 
ATOM   8886  N N   . LYS A 1 1138 ? 188.216 186.395 206.226 1.00 66.61  ? 1121 LYS B N   1 
ATOM   8887  C CA  . LYS A 1 1138 ? 187.536 185.202 205.749 1.00 66.61  ? 1121 LYS B CA  1 
ATOM   8888  C C   . LYS A 1 1138 ? 186.753 184.573 206.890 1.00 66.61  ? 1121 LYS B C   1 
ATOM   8889  O O   . LYS A 1 1138 ? 187.107 184.720 208.061 1.00 66.61  ? 1121 LYS B O   1 
ATOM   8890  C CB  . LYS A 1 1138 ? 188.535 184.208 205.151 1.00 66.61  ? 1121 LYS B CB  1 
ATOM   8891  C CG  . LYS A 1 1138 ? 189.802 184.055 205.969 1.00 66.61  ? 1121 LYS B CG  1 
ATOM   8892  C CD  . LYS A 1 1138 ? 190.565 182.801 205.591 1.00 66.61  ? 1121 LYS B CD  1 
ATOM   8893  C CE  . LYS A 1 1138 ? 190.776 182.712 204.090 1.00 66.61  ? 1121 LYS B CE  1 
ATOM   8894  N NZ  . LYS A 1 1138 ? 191.609 183.838 203.581 1.00 66.61  ? 1121 LYS B NZ  1 
ATOM   8895  N N   . TYR A 1 1139 ? 185.681 183.872 206.534 1.00 65.54  ? 1122 TYR B N   1 
ATOM   8896  C CA  . TYR A 1 1139 ? 184.760 183.295 207.498 1.00 65.54  ? 1122 TYR B CA  1 
ATOM   8897  C C   . TYR A 1 1139 ? 184.729 181.780 207.359 1.00 65.54  ? 1122 TYR B C   1 
ATOM   8898  O O   . TYR A 1 1139 ? 185.101 181.219 206.326 1.00 65.54  ? 1122 TYR B O   1 
ATOM   8899  C CB  . TYR A 1 1139 ? 183.345 183.859 207.325 1.00 65.54  ? 1122 TYR B CB  1 
ATOM   8900  C CG  . TYR A 1 1139 ? 182.785 183.685 205.935 1.00 65.54  ? 1122 TYR B CG  1 
ATOM   8901  C CD1 . TYR A 1 1139 ? 182.162 182.505 205.558 1.00 65.54  ? 1122 TYR B CD1 1 
ATOM   8902  C CD2 . TYR A 1 1139 ? 182.877 184.702 205.001 1.00 65.54  ? 1122 TYR B CD2 1 
ATOM   8903  C CE1 . TYR A 1 1139 ? 181.652 182.342 204.291 1.00 65.54  ? 1122 TYR B CE1 1 
ATOM   8904  C CE2 . TYR A 1 1139 ? 182.369 184.548 203.732 1.00 65.54  ? 1122 TYR B CE2 1 
ATOM   8905  C CZ  . TYR A 1 1139 ? 181.757 183.367 203.382 1.00 65.54  ? 1122 TYR B CZ  1 
ATOM   8906  O OH  . TYR A 1 1139 ? 181.248 183.210 202.115 1.00 65.54  ? 1122 TYR B OH  1 
ATOM   8907  N N   . VAL A 1 1140 ? 184.255 181.129 208.416 1.00 62.56  ? 1123 VAL B N   1 
ATOM   8908  C CA  . VAL A 1 1140 ? 184.217 179.674 208.479 1.00 62.56  ? 1123 VAL B CA  1 
ATOM   8909  C C   . VAL A 1 1140 ? 182.961 179.170 207.783 1.00 62.56  ? 1123 VAL B C   1 
ATOM   8910  O O   . VAL A 1 1140 ? 181.853 179.638 208.062 1.00 62.56  ? 1123 VAL B O   1 
ATOM   8911  C CB  . VAL A 1 1140 ? 184.269 179.199 209.939 1.00 62.56  ? 1123 VAL B CB  1 
ATOM   8912  C CG1 . VAL A 1 1140 ? 183.799 177.765 210.047 1.00 62.56  ? 1123 VAL B CG1 1 
ATOM   8913  C CG2 . VAL A 1 1140 ? 185.674 179.347 210.494 1.00 62.56  ? 1123 VAL B CG2 1 
ATOM   8914  N N   . ASP A 1 1141 ? 183.131 178.212 206.877 1.00 68.95  ? 1124 ASP B N   1 
ATOM   8915  C CA  . ASP A 1 1141 ? 182.021 177.582 206.180 1.00 68.95  ? 1124 ASP B CA  1 
ATOM   8916  C C   . ASP A 1 1141 ? 182.197 176.072 206.212 1.00 68.95  ? 1124 ASP B C   1 
ATOM   8917  O O   . ASP A 1 1141 ? 183.308 175.563 206.379 1.00 68.95  ? 1124 ASP B O   1 
ATOM   8918  C CB  . ASP A 1 1141 ? 181.913 178.059 204.732 1.00 68.95  ? 1124 ASP B CB  1 
ATOM   8919  C CG  . ASP A 1 1141 ? 180.488 178.378 204.328 1.00 68.95  ? 1124 ASP B CG  1 
ATOM   8920  O OD1 . ASP A 1 1141 ? 179.556 177.830 204.952 1.00 68.95  ? 1124 ASP B OD1 1 
ATOM   8921  O OD2 . ASP A 1 1141 ? 180.298 179.174 203.385 1.00 68.95  ? 1124 ASP B OD2 1 
ATOM   8922  N N   . VAL A 1 1142 ? 181.088 175.363 206.051 1.00 61.17  ? 1125 VAL B N   1 
ATOM   8923  C CA  . VAL A 1 1142 ? 181.066 173.922 206.169 1.00 61.17  ? 1125 VAL B CA  1 
ATOM   8924  C C   . VAL A 1 1142 ? 180.992 173.320 204.770 1.00 61.17  ? 1125 VAL B C   1 
ATOM   8925  O O   . VAL A 1 1142 ? 180.644 173.989 203.801 1.00 61.17  ? 1125 VAL B O   1 
ATOM   8926  C CB  . VAL A 1 1142 ? 179.896 173.451 207.065 1.00 61.17  ? 1125 VAL B CB  1 
ATOM   8927  C CG1 . VAL A 1 1142 ? 180.035 171.984 207.432 1.00 61.17  ? 1125 VAL B CG1 1 
ATOM   8928  C CG2 . VAL A 1 1142 ? 179.816 174.313 208.312 1.00 61.17  ? 1125 VAL B CG2 1 
ATOM   8929  N N   . ASN A 1 1143 ? 181.327 172.034 204.656 1.00 63.18  ? 1126 ASN B N   1 
ATOM   8930  C CA  . ASN A 1 1143 ? 181.388 171.372 203.356 1.00 63.18  ? 1126 ASN B CA  1 
ATOM   8931  C C   . ASN A 1 1143 ? 180.970 169.917 203.555 1.00 63.18  ? 1126 ASN B C   1 
ATOM   8932  O O   . ASN A 1 1143 ? 181.768 169.102 204.031 1.00 63.18  ? 1126 ASN B O   1 
ATOM   8933  C CB  . ASN A 1 1143 ? 182.791 171.482 202.774 1.00 63.18  ? 1126 ASN B CB  1 
ATOM   8934  C CG  . ASN A 1 1143 ? 182.911 170.859 201.403 1.00 63.18  ? 1126 ASN B CG  1 
ATOM   8935  O OD1 . ASN A 1 1143 ? 181.949 170.325 200.863 1.00 63.18  ? 1126 ASN B OD1 1 
ATOM   8936  N ND2 . ASN A 1 1143 ? 184.107 170.919 200.833 1.00 63.18  ? 1126 ASN B ND2 1 
ATOM   8937  N N   . ASN A 1 1144 ? 179.723 169.606 203.190 1.00 68.04  ? 1127 ASN B N   1 
ATOM   8938  C CA  . ASN A 1 1144 ? 179.201 168.238 203.170 1.00 68.04  ? 1127 ASN B CA  1 
ATOM   8939  C C   . ASN A 1 1144 ? 179.316 167.577 204.547 1.00 68.04  ? 1127 ASN B C   1 
ATOM   8940  O O   . ASN A 1 1144 ? 180.099 166.652 204.758 1.00 68.04  ? 1127 ASN B O   1 
ATOM   8941  C CB  . ASN A 1 1144 ? 179.901 167.389 202.103 1.00 68.04  ? 1127 ASN B CB  1 
ATOM   8942  C CG  . ASN A 1 1144 ? 179.873 168.030 200.733 1.00 68.04  ? 1127 ASN B CG  1 
ATOM   8943  O OD1 . ASN A 1 1144 ? 180.862 167.998 200.000 1.00 68.04  ? 1127 ASN B OD1 1 
ATOM   8944  N ND2 . ASN A 1 1144 ? 178.737 168.619 200.378 1.00 68.04  ? 1127 ASN B ND2 1 
ATOM   8945  N N   . VAL A 1 1145 ? 178.519 168.095 205.484 1.00 65.45  ? 1128 VAL B N   1 
ATOM   8946  C CA  . VAL A 1 1145 ? 178.484 167.604 206.861 1.00 65.45  ? 1128 VAL B CA  1 
ATOM   8947  C C   . VAL A 1 1145 ? 178.484 166.079 206.902 1.00 65.45  ? 1128 VAL B C   1 
ATOM   8948  O O   . VAL A 1 1145 ? 177.770 165.419 206.138 1.00 65.45  ? 1128 VAL B O   1 
ATOM   8949  C CB  . VAL A 1 1145 ? 177.266 168.174 207.612 1.00 65.45  ? 1128 VAL B CB  1 
ATOM   8950  C CG1 . VAL A 1 1145 ? 177.324 169.684 207.624 1.00 65.45  ? 1128 VAL B CG1 1 
ATOM   8951  C CG2 . VAL A 1 1145 ? 175.971 167.713 206.968 1.00 65.45  ? 1128 VAL B CG2 1 
ATOM   8952  N N   . GLY A 1 1146 ? 179.303 165.515 207.775 1.00 64.86  ? 1129 GLY B N   1 
ATOM   8953  C CA  . GLY A 1 1146 ? 179.524 164.090 207.852 1.00 64.86  ? 1129 GLY B CA  1 
ATOM   8954  C C   . GLY A 1 1146 ? 181.001 163.805 208.000 1.00 64.86  ? 1129 GLY B C   1 
ATOM   8955  O O   . GLY A 1 1146 ? 181.811 164.710 208.187 1.00 64.86  ? 1129 GLY B O   1 
ATOM   8956  N N   . ILE A 1 1147 ? 181.357 162.522 207.918 1.00 65.43  ? 1130 ILE B N   1 
ATOM   8957  C CA  . ILE A 1 1147 ? 182.762 162.139 208.036 1.00 65.43  ? 1130 ILE B CA  1 
ATOM   8958  C C   . ILE A 1 1147 ? 183.560 162.651 206.843 1.00 65.43  ? 1130 ILE B C   1 
ATOM   8959  O O   . ILE A 1 1147 ? 184.684 163.144 206.995 1.00 65.43  ? 1130 ILE B O   1 
ATOM   8960  C CB  . ILE A 1 1147 ? 182.891 160.612 208.187 1.00 65.43  ? 1130 ILE B CB  1 
ATOM   8961  C CG1 . ILE A 1 1147 ? 182.682 160.193 209.640 1.00 65.43  ? 1130 ILE B CG1 1 
ATOM   8962  C CG2 . ILE A 1 1147 ? 184.249 160.136 207.716 1.00 65.43  ? 1130 ILE B CG2 1 
ATOM   8963  C CD1 . ILE A 1 1147 ? 182.685 158.699 209.841 1.00 65.43  ? 1130 ILE B CD1 1 
ATOM   8964  N N   . ARG A 1 1148 ? 182.991 162.560 205.643 1.00 70.14  ? 1131 ARG B N   1 
ATOM   8965  C CA  . ARG A 1 1148 ? 183.727 162.870 204.425 1.00 70.14  ? 1131 ARG B CA  1 
ATOM   8966  C C   . ARG A 1 1148 ? 183.767 164.359 204.104 1.00 70.14  ? 1131 ARG B C   1 
ATOM   8967  O O   . ARG A 1 1148 ? 184.459 164.750 203.158 1.00 70.14  ? 1131 ARG B O   1 
ATOM   8968  C CB  . ARG A 1 1148 ? 183.130 162.100 203.246 1.00 70.14  ? 1131 ARG B CB  1 
ATOM   8969  C CG  . ARG A 1 1148 ? 183.987 160.928 202.790 1.00 70.14  ? 1131 ARG B CG  1 
ATOM   8970  C CD  . ARG A 1 1148 ? 184.359 160.032 203.963 1.00 70.14  ? 1131 ARG B CD  1 
ATOM   8971  N NE  . ARG A 1 1148 ? 184.798 158.709 203.535 1.00 70.14  ? 1131 ARG B NE  1 
ATOM   8972  C CZ  . ARG A 1 1148 ? 184.787 157.630 204.305 1.00 70.14  ? 1131 ARG B CZ  1 
ATOM   8973  N NH1 . ARG A 1 1148 ? 184.345 157.673 205.551 1.00 70.14  ? 1131 ARG B NH1 1 
ATOM   8974  N NH2 . ARG A 1 1148 ? 185.228 156.476 203.812 1.00 70.14  ? 1131 ARG B NH2 1 
ATOM   8975  N N   . GLY A 1 1149 ? 183.056 165.196 204.855 1.00 63.58  ? 1132 GLY B N   1 
ATOM   8976  C CA  . GLY A 1 1149 ? 183.134 166.631 204.692 1.00 63.58  ? 1132 GLY B CA  1 
ATOM   8977  C C   . GLY A 1 1149 ? 184.196 167.240 205.582 1.00 63.58  ? 1132 GLY B C   1 
ATOM   8978  O O   . GLY A 1 1149 ? 185.024 166.550 206.179 1.00 63.58  ? 1132 GLY B O   1 
ATOM   8979  N N   . TYR A 1 1150 ? 184.168 168.562 205.670 1.00 63.12  ? 1133 TYR B N   1 
ATOM   8980  C CA  . TYR A 1 1150 ? 185.096 169.284 206.539 1.00 63.12  ? 1133 TYR B CA  1 
ATOM   8981  C C   . TYR A 1 1150 ? 184.583 170.707 206.700 1.00 63.12  ? 1133 TYR B C   1 
ATOM   8982  O O   . TYR A 1 1150 ? 183.435 171.014 206.358 1.00 63.12  ? 1133 TYR B O   1 
ATOM   8983  C CB  . TYR A 1 1150 ? 186.526 169.242 205.998 1.00 63.12  ? 1133 TYR B CB  1 
ATOM   8984  C CG  . TYR A 1 1150 ? 186.701 169.707 204.570 1.00 63.12  ? 1133 TYR B CG  1 
ATOM   8985  C CD1 . TYR A 1 1150 ? 186.561 171.042 204.224 1.00 63.12  ? 1133 TYR B CD1 1 
ATOM   8986  C CD2 . TYR A 1 1150 ? 187.006 168.803 203.565 1.00 63.12  ? 1133 TYR B CD2 1 
ATOM   8987  C CE1 . TYR A 1 1150 ? 186.727 171.460 202.921 1.00 63.12  ? 1133 TYR B CE1 1 
ATOM   8988  C CE2 . TYR A 1 1150 ? 187.170 169.214 202.260 1.00 63.12  ? 1133 TYR B CE2 1 
ATOM   8989  C CZ  . TYR A 1 1150 ? 187.031 170.541 201.945 1.00 63.12  ? 1133 TYR B CZ  1 
ATOM   8990  O OH  . TYR A 1 1150 ? 187.194 170.946 200.644 1.00 63.12  ? 1133 TYR B OH  1 
ATOM   8991  N N   . MET A 1 1151 ? 185.417 171.570 207.265 1.00 64.20  ? 1134 MET B N   1 
ATOM   8992  C CA  . MET A 1 1151 ? 185.123 172.991 207.349 1.00 64.20  ? 1134 MET B CA  1 
ATOM   8993  C C   . MET A 1 1151 ? 186.354 173.775 206.937 1.00 64.20  ? 1134 MET B C   1 
ATOM   8994  O O   . MET A 1 1151 ? 187.479 173.409 207.286 1.00 64.20  ? 1134 MET B O   1 
ATOM   8995  C CB  . MET A 1 1151 ? 184.696 173.403 208.752 1.00 64.20  ? 1134 MET B CB  1 
ATOM   8996  C CG  . MET A 1 1151 ? 183.954 172.337 209.507 1.00 64.20  ? 1134 MET B CG  1 
ATOM   8997  S SD  . MET A 1 1151 ? 183.949 172.703 211.257 1.00 64.20  ? 1134 MET B SD  1 
ATOM   8998  C CE  . MET A 1 1151 ? 183.290 174.360 211.225 1.00 64.20  ? 1134 MET B CE  1 
ATOM   8999  N N   . TYR A 1 1152 ? 186.138 174.856 206.200 1.00 68.04  ? 1135 TYR B N   1 
ATOM   9000  C CA  . TYR A 1 1152 ? 187.232 175.663 205.687 1.00 68.04  ? 1135 TYR B CA  1 
ATOM   9001  C C   . TYR A 1 1152 ? 186.917 177.134 205.908 1.00 68.04  ? 1135 TYR B C   1 
ATOM   9002  O O   . TYR A 1 1152 ? 185.897 177.491 206.499 1.00 68.04  ? 1135 TYR B O   1 
ATOM   9003  C CB  . TYR A 1 1152 ? 187.511 175.374 204.205 1.00 68.04  ? 1135 TYR B CB  1 
ATOM   9004  C CG  . TYR A 1 1152 ? 186.330 175.494 203.267 1.00 68.04  ? 1135 TYR B CG  1 
ATOM   9005  C CD1 . TYR A 1 1152 ? 185.207 174.695 203.411 1.00 68.04  ? 1135 TYR B CD1 1 
ATOM   9006  C CD2 . TYR A 1 1152 ? 186.353 176.400 202.220 1.00 68.04  ? 1135 TYR B CD2 1 
ATOM   9007  C CE1 . TYR A 1 1152 ? 184.140 174.804 202.552 1.00 68.04  ? 1135 TYR B CE1 1 
ATOM   9008  C CE2 . TYR A 1 1152 ? 185.290 176.515 201.353 1.00 68.04  ? 1135 TYR B CE2 1 
ATOM   9009  C CZ  . TYR A 1 1152 ? 184.185 175.716 201.524 1.00 68.04  ? 1135 TYR B CZ  1 
ATOM   9010  O OH  . TYR A 1 1152 ? 183.121 175.831 200.660 1.00 68.04  ? 1135 TYR B OH  1 
ATOM   9011  N N   . LEU A 1 1153 ? 187.818 177.992 205.446 1.00 66.57  ? 1136 LEU B N   1 
ATOM   9012  C CA  . LEU A 1 1153 ? 187.673 179.432 205.588 1.00 66.57  ? 1136 LEU B CA  1 
ATOM   9013  C C   . LEU A 1 1153 ? 187.705 180.077 204.212 1.00 66.57  ? 1136 LEU B C   1 
ATOM   9014  O O   . LEU A 1 1153 ? 188.680 179.924 203.471 1.00 66.57  ? 1136 LEU B O   1 
ATOM   9015  C CB  . LEU A 1 1153 ? 188.777 180.009 206.469 1.00 66.57  ? 1136 LEU B CB  1 
ATOM   9016  C CG  . LEU A 1 1153 ? 188.794 179.533 207.915 1.00 66.57  ? 1136 LEU B CG  1 
ATOM   9017  C CD1 . LEU A 1 1153 ? 189.847 178.476 208.062 1.00 66.57  ? 1136 LEU B CD1 1 
ATOM   9018  C CD2 . LEU A 1 1153 ? 189.070 180.690 208.852 1.00 66.57  ? 1136 LEU B CD2 1 
ATOM   9019  N N   . LYS A 1 1154 ? 186.646 180.805 203.884 1.00 67.40  ? 1137 LYS B N   1 
ATOM   9020  C CA  . LYS A 1 1154 ? 186.536 181.462 202.593 1.00 67.40  ? 1137 LYS B CA  1 
ATOM   9021  C C   . LYS A 1 1154 ? 186.140 182.915 202.793 1.00 67.40  ? 1137 LYS B C   1 
ATOM   9022  O O   . LYS A 1 1154 ? 185.405 183.252 203.724 1.00 67.40  ? 1137 LYS B O   1 
ATOM   9023  C CB  . LYS A 1 1154 ? 185.520 180.754 201.695 1.00 67.40  ? 1137 LYS B CB  1 
ATOM   9024  C CG  . LYS A 1 1154 ? 184.129 180.670 202.283 1.00 67.40  ? 1137 LYS B CG  1 
ATOM   9025  C CD  . LYS A 1 1154 ? 183.411 179.426 201.803 1.00 67.40  ? 1137 LYS B CD  1 
ATOM   9026  C CE  . LYS A 1 1154 ? 183.187 179.454 200.304 1.00 67.40  ? 1137 LYS B CE  1 
ATOM   9027  N NZ  . LYS A 1 1154 ? 182.218 178.407 199.881 1.00 67.40  ? 1137 LYS B NZ  1 
ATOM   9028  N N   . GLY A 1 1155 ? 186.640 183.775 201.912 1.00 64.53  ? 1138 GLY B N   1 
ATOM   9029  C CA  . GLY A 1 1155 ? 186.340 185.184 201.972 1.00 64.53  ? 1138 GLY B CA  1 
ATOM   9030  C C   . GLY A 1 1155 ? 186.036 185.753 200.603 1.00 64.53  ? 1138 GLY B C   1 
ATOM   9031  O O   . GLY A 1 1155 ? 185.880 185.019 199.624 1.00 64.53  ? 1138 GLY B O   1 
ATOM   9032  N N   . PRO A 1 1156 ? 185.944 187.082 200.506 1.00 65.27  ? 1139 PRO B N   1 
ATOM   9033  C CA  . PRO A 1 1156 ? 186.036 188.064 201.595 1.00 65.27  ? 1139 PRO B CA  1 
ATOM   9034  C C   . PRO A 1 1156 ? 184.755 188.112 202.417 1.00 65.27  ? 1139 PRO B C   1 
ATOM   9035  O O   . PRO A 1 1156 ? 183.729 187.588 201.999 1.00 65.27  ? 1139 PRO B O   1 
ATOM   9036  C CB  . PRO A 1 1156 ? 186.290 189.395 200.868 1.00 65.27  ? 1139 PRO B CB  1 
ATOM   9037  C CG  . PRO A 1 1156 ? 186.508 189.074 199.418 1.00 65.27  ? 1139 PRO B CG  1 
ATOM   9038  C CD  . PRO A 1 1156 ? 185.933 187.713 199.178 1.00 65.27  ? 1139 PRO B CD  1 
ATOM   9039  N N   . ARG A 1 1157 ? 184.796 188.732 203.598 1.00 62.83  ? 1140 ARG B N   1 
ATOM   9040  C CA  . ARG A 1 1157 ? 183.613 188.779 204.451 1.00 62.83  ? 1140 ARG B CA  1 
ATOM   9041  C C   . ARG A 1 1157 ? 182.488 189.574 203.802 1.00 62.83  ? 1140 ARG B C   1 
ATOM   9042  O O   . ARG A 1 1157 ? 181.324 189.163 203.844 1.00 62.83  ? 1140 ARG B O   1 
ATOM   9043  C CB  . ARG A 1 1157 ? 183.970 189.374 205.811 1.00 62.83  ? 1140 ARG B CB  1 
ATOM   9044  C CG  . ARG A 1 1157 ? 184.598 188.381 206.766 1.00 62.83  ? 1140 ARG B CG  1 
ATOM   9045  C CD  . ARG A 1 1157 ? 184.628 188.912 208.184 1.00 62.83  ? 1140 ARG B CD  1 
ATOM   9046  N NE  . ARG A 1 1157 ? 184.949 187.862 209.141 1.00 62.83  ? 1140 ARG B NE  1 
ATOM   9047  C CZ  . ARG A 1 1157 ? 184.081 186.967 209.587 1.00 62.83  ? 1140 ARG B CZ  1 
ATOM   9048  N NH1 . ARG A 1 1157 ? 182.821 186.969 209.187 1.00 62.83  ? 1140 ARG B NH1 1 
ATOM   9049  N NH2 . ARG A 1 1157 ? 184.486 186.049 210.458 1.00 62.83  ? 1140 ARG B NH2 1 
ATOM   9050  N N   . GLY A 1 1158 ? 182.813 190.711 203.197 1.00 59.67  ? 1141 GLY B N   1 
ATOM   9051  C CA  . GLY A 1 1158 ? 181.822 191.569 202.594 1.00 59.67  ? 1141 GLY B CA  1 
ATOM   9052  C C   . GLY A 1 1158 ? 182.019 192.996 203.047 1.00 59.67  ? 1141 GLY B C   1 
ATOM   9053  O O   . GLY A 1 1158 ? 183.121 193.402 203.431 1.00 59.67  ? 1141 GLY B O   1 
ATOM   9054  N N   . SER A 1 1159 ? 180.938 193.770 203.005 1.00 52.72  ? 1142 SER B N   1 
ATOM   9055  C CA  . SER A 1 1159 ? 181.004 195.174 203.373 1.00 52.72  ? 1142 SER B CA  1 
ATOM   9056  C C   . SER A 1 1159 ? 179.638 195.648 203.835 1.00 52.72  ? 1142 SER B C   1 
ATOM   9057  O O   . SER A 1 1159 ? 178.619 195.319 203.225 1.00 52.72  ? 1142 SER B O   1 
ATOM   9058  C CB  . SER A 1 1159 ? 181.485 196.034 202.203 1.00 52.72  ? 1142 SER B CB  1 
ATOM   9059  O OG  . SER A 1 1159 ? 182.897 196.022 202.115 1.00 52.72  ? 1142 SER B OG  1 
ATOM   9060  N N   . VAL A 1 1160 ? 179.630 196.417 204.918 1.00 49.79  ? 1143 VAL B N   1 
ATOM   9061  C CA  . VAL A 1 1160 ? 178.436 197.067 205.439 1.00 49.79  ? 1143 VAL B CA  1 
ATOM   9062  C C   . VAL A 1 1160 ? 178.733 198.555 205.492 1.00 49.79  ? 1143 VAL B C   1 
ATOM   9063  O O   . VAL A 1 1160 ? 179.669 198.980 206.179 1.00 49.79  ? 1143 VAL B O   1 
ATOM   9064  C CB  . VAL A 1 1160 ? 178.049 196.527 206.823 1.00 49.79  ? 1143 VAL B CB  1 
ATOM   9065  C CG1 . VAL A 1 1160 ? 177.259 197.560 207.598 1.00 49.79  ? 1143 VAL B CG1 1 
ATOM   9066  C CG2 . VAL A 1 1160 ? 177.251 195.247 206.679 1.00 49.79  ? 1143 VAL B CG2 1 
ATOM   9067  N N   . MET A 1 1161 ? 177.948 199.346 204.766 1.00 49.11  ? 1144 MET B N   1 
ATOM   9068  C CA  . MET A 1 1161 ? 178.280 200.742 204.545 1.00 49.11  ? 1144 MET B CA  1 
ATOM   9069  C C   . MET A 1 1161 ? 177.072 201.638 204.750 1.00 49.11  ? 1144 MET B C   1 
ATOM   9070  O O   . MET A 1 1161 ? 175.928 201.233 204.539 1.00 49.11  ? 1144 MET B O   1 
ATOM   9071  C CB  . MET A 1 1161 ? 178.828 200.969 203.137 1.00 49.11  ? 1144 MET B CB  1 
ATOM   9072  C CG  . MET A 1 1161 ? 178.102 200.194 202.063 1.00 49.11  ? 1144 MET B CG  1 
ATOM   9073  S SD  . MET A 1 1161 ? 179.010 200.181 200.509 1.00 49.11  ? 1144 MET B SD  1 
ATOM   9074  C CE  . MET A 1 1161 ? 180.569 199.480 201.033 1.00 49.11  ? 1144 MET B CE  1 
ATOM   9075  N N   . THR A 1 1162 ? 177.356 202.867 205.172 1.00 50.96  ? 1145 THR B N   1 
ATOM   9076  C CA  . THR A 1 1162 ? 176.405 203.973 205.170 1.00 50.96  ? 1145 THR B CA  1 
ATOM   9077  C C   . THR A 1 1162 ? 177.199 205.195 204.742 1.00 50.96  ? 1145 THR B C   1 
ATOM   9078  O O   . THR A 1 1162 ? 178.094 205.636 205.472 1.00 50.96  ? 1145 THR B O   1 
ATOM   9079  C CB  . THR A 1 1162 ? 175.768 204.189 206.540 1.00 50.96  ? 1145 THR B CB  1 
ATOM   9080  O OG1 . THR A 1 1162 ? 174.911 203.087 206.853 1.00 50.96  ? 1145 THR B OG1 1 
ATOM   9081  C CG2 . THR A 1 1162 ? 174.963 205.469 206.548 1.00 50.96  ? 1145 THR B CG2 1 
ATOM   9082  N N   . THR A 1 1163 ? 176.883 205.721 203.562 1.00 51.17  ? 1146 THR B N   1 
ATOM   9083  C CA  . THR A 1 1163 ? 177.708 206.747 202.941 1.00 51.17  ? 1146 THR B CA  1 
ATOM   9084  C C   . THR A 1 1163 ? 177.856 207.951 203.858 1.00 51.17  ? 1146 THR B C   1 
ATOM   9085  O O   . THR A 1 1163 ? 176.877 208.424 204.442 1.00 51.17  ? 1146 THR B O   1 
ATOM   9086  C CB  . THR A 1 1163 ? 177.100 207.168 201.604 1.00 51.17  ? 1146 THR B CB  1 
ATOM   9087  O OG1 . THR A 1 1163 ? 177.302 206.128 200.642 1.00 51.17  ? 1146 THR B OG1 1 
ATOM   9088  C CG2 . THR A 1 1163 ? 177.744 208.444 201.096 1.00 51.17  ? 1146 THR B CG2 1 
ATOM   9089  N N   . ASN A 1 1164 ? 179.095 208.425 203.996 1.00 55.73  ? 1147 ASN B N   1 
ATOM   9090  C CA  . ASN A 1 1164 ? 179.486 209.567 204.816 1.00 55.73  ? 1147 ASN B CA  1 
ATOM   9091  C C   . ASN A 1 1164 ? 179.411 209.269 206.308 1.00 55.73  ? 1147 ASN B C   1 
ATOM   9092  O O   . ASN A 1 1164 ? 179.626 210.172 207.123 1.00 55.73  ? 1147 ASN B O   1 
ATOM   9093  C CB  . ASN A 1 1164 ? 178.647 210.810 204.486 1.00 55.73  ? 1147 ASN B CB  1 
ATOM   9094  C CG  . ASN A 1 1164 ? 179.285 212.096 204.966 1.00 55.73  ? 1147 ASN B CG  1 
ATOM   9095  O OD1 . ASN A 1 1164 ? 178.597 213.015 205.409 1.00 55.73  ? 1147 ASN B OD1 1 
ATOM   9096  N ND2 . ASN A 1 1164 ? 180.607 212.168 204.881 1.00 55.73  ? 1147 ASN B ND2 1 
ATOM   9097  N N   . ILE A 1 1165 ? 179.126 208.027 206.697 1.00 53.07  ? 1148 ILE B N   1 
ATOM   9098  C CA  . ILE A 1 1165 ? 179.049 207.688 208.114 1.00 53.07  ? 1148 ILE B CA  1 
ATOM   9099  C C   . ILE A 1 1165 ? 180.019 206.564 208.455 1.00 53.07  ? 1148 ILE B C   1 
ATOM   9100  O O   . ILE A 1 1165 ? 180.910 206.745 209.291 1.00 53.07  ? 1148 ILE B O   1 
ATOM   9101  C CB  . ILE A 1 1165 ? 177.617 207.316 208.528 1.00 53.07  ? 1148 ILE B CB  1 
ATOM   9102  C CG1 . ILE A 1 1165 ? 176.686 208.506 208.323 1.00 53.07  ? 1148 ILE B CG1 1 
ATOM   9103  C CG2 . ILE A 1 1165 ? 177.591 206.917 209.979 1.00 53.07  ? 1148 ILE B CG2 1 
ATOM   9104  C CD1 . ILE A 1 1165 ? 177.029 209.692 209.182 1.00 53.07  ? 1148 ILE B CD1 1 
ATOM   9105  N N   . TYR A 1 1166 ? 179.864 205.396 207.831 1.00 47.54  ? 1149 TYR B N   1 
ATOM   9106  C CA  . TYR A 1 1166 ? 180.744 204.289 208.183 1.00 47.54  ? 1149 TYR B CA  1 
ATOM   9107  C C   . TYR A 1 1166 ? 180.867 203.301 207.035 1.00 47.54  ? 1149 TYR B C   1 
ATOM   9108  O O   . TYR A 1 1166 ? 180.050 203.275 206.114 1.00 47.54  ? 1149 TYR B O   1 
ATOM   9109  C CB  . TYR A 1 1166 ? 180.271 203.561 209.450 1.00 47.54  ? 1149 TYR B CB  1 
ATOM   9110  C CG  . TYR A 1 1166 ? 178.940 202.851 209.336 1.00 47.54  ? 1149 TYR B CG  1 
ATOM   9111  C CD1 . TYR A 1 1166 ? 178.860 201.551 208.866 1.00 47.54  ? 1149 TYR B CD1 1 
ATOM   9112  C CD2 . TYR A 1 1166 ? 177.769 203.469 209.734 1.00 47.54  ? 1149 TYR B CD2 1 
ATOM   9113  C CE1 . TYR A 1 1166 ? 177.649 200.904 208.773 1.00 47.54  ? 1149 TYR B CE1 1 
ATOM   9114  C CE2 . TYR A 1 1166 ? 176.556 202.827 209.647 1.00 47.54  ? 1149 TYR B CE2 1 
ATOM   9115  C CZ  . TYR A 1 1166 ? 176.502 201.548 209.166 1.00 47.54  ? 1149 TYR B CZ  1 
ATOM   9116  O OH  . TYR A 1 1166 ? 175.291 200.911 209.078 1.00 47.54  ? 1149 TYR B OH  1 
ATOM   9117  N N   . LEU A 1 1167 ? 181.915 202.479 207.114 1.00 52.33  ? 1150 LEU B N   1 
ATOM   9118  C CA  . LEU A 1 1167 ? 182.139 201.412 206.142 1.00 52.33  ? 1150 LEU B CA  1 
ATOM   9119  C C   . LEU A 1 1167 ? 182.984 200.354 206.851 1.00 52.33  ? 1150 LEU B C   1 
ATOM   9120  O O   . LEU A 1 1167 ? 184.205 200.500 206.938 1.00 52.33  ? 1150 LEU B O   1 
ATOM   9121  C CB  . LEU A 1 1167 ? 182.830 201.942 204.897 1.00 52.33  ? 1150 LEU B CB  1 
ATOM   9122  C CG  . LEU A 1 1167 ? 182.833 201.120 203.606 1.00 52.33  ? 1150 LEU B CG  1 
ATOM   9123  C CD1 . LEU A 1 1167 ? 183.356 201.980 202.470 1.00 52.33  ? 1150 LEU B CD1 1 
ATOM   9124  C CD2 . LEU A 1 1167 ? 183.654 199.845 203.716 1.00 52.33  ? 1150 LEU B CD2 1 
ATOM   9125  N N   . ASN A 1 1168 ? 182.335 199.301 207.337 1.00 51.68  ? 1151 ASN B N   1 
ATOM   9126  C CA  . ASN A 1 1168 ? 183.016 198.263 208.093 1.00 51.68  ? 1151 ASN B CA  1 
ATOM   9127  C C   . ASN A 1 1168 ? 182.679 196.904 207.508 1.00 51.68  ? 1151 ASN B C   1 
ATOM   9128  O O   . ASN A 1 1168 ? 181.563 196.676 207.038 1.00 51.68  ? 1151 ASN B O   1 
ATOM   9129  C CB  . ASN A 1 1168 ? 182.625 198.289 209.570 1.00 51.68  ? 1151 ASN B CB  1 
ATOM   9130  C CG  . ASN A 1 1168 ? 182.343 199.684 210.069 1.00 51.68  ? 1151 ASN B CG  1 
ATOM   9131  O OD1 . ASN A 1 1168 ? 181.214 200.009 210.427 1.00 51.68  ? 1151 ASN B OD1 1 
ATOM   9132  N ND2 . ASN A 1 1168 ? 183.369 200.519 210.097 1.00 51.68  ? 1151 ASN B ND2 1 
ATOM   9133  N N   . SER A 1 1169 ? 183.651 195.999 207.545 1.00 54.39  ? 1152 SER B N   1 
ATOM   9134  C CA  . SER A 1 1169 ? 183.435 194.660 207.021 1.00 54.39  ? 1152 SER B CA  1 
ATOM   9135  C C   . SER A 1 1169 ? 182.380 193.934 207.843 1.00 54.39  ? 1152 SER B C   1 
ATOM   9136  O O   . SER A 1 1169 ? 182.350 194.033 209.072 1.00 54.39  ? 1152 SER B O   1 
ATOM   9137  C CB  . SER A 1 1169 ? 184.740 193.869 207.023 1.00 54.39  ? 1152 SER B CB  1 
ATOM   9138  O OG  . SER A 1 1169 ? 185.325 193.866 208.311 1.00 54.39  ? 1152 SER B OG  1 
ATOM   9139  N N   . SER A 1 1170 ? 181.505 193.209 207.154 1.00 58.39  ? 1153 SER B N   1 
ATOM   9140  C CA  . SER A 1 1170 ? 180.435 192.486 207.822 1.00 58.39  ? 1153 SER B CA  1 
ATOM   9141  C C   . SER A 1 1170 ? 181.002 191.359 208.674 1.00 58.39  ? 1153 SER B C   1 
ATOM   9142  O O   . SER A 1 1170 ? 181.999 190.730 208.314 1.00 58.39  ? 1153 SER B O   1 
ATOM   9143  C CB  . SER A 1 1170 ? 179.460 191.924 206.794 1.00 58.39  ? 1153 SER B CB  1 
ATOM   9144  O OG  . SER A 1 1170 ? 179.954 190.721 206.234 1.00 58.39  ? 1153 SER B OG  1 
ATOM   9145  N N   . LEU A 1 1171 ? 180.357 191.101 209.810 1.00 57.50  ? 1154 LEU B N   1 
ATOM   9146  C CA  . LEU A 1 1171 ? 180.810 190.073 210.737 1.00 57.50  ? 1154 LEU B CA  1 
ATOM   9147  C C   . LEU A 1 1171 ? 179.864 188.892 210.862 1.00 57.50  ? 1154 LEU B C   1 
ATOM   9148  O O   . LEU A 1 1171 ? 180.328 187.771 211.070 1.00 57.50  ? 1154 LEU B O   1 
ATOM   9149  C CB  . LEU A 1 1171 ? 181.033 190.673 212.128 1.00 57.50  ? 1154 LEU B CB  1 
ATOM   9150  C CG  . LEU A 1 1171 ? 181.887 191.937 212.163 1.00 57.50  ? 1154 LEU B CG  1 
ATOM   9151  C CD1 . LEU A 1 1171 ? 181.719 192.646 213.487 1.00 57.50  ? 1154 LEU B CD1 1 
ATOM   9152  C CD2 . LEU A 1 1171 ? 183.342 191.601 211.918 1.00 57.50  ? 1154 LEU B CD2 1 
ATOM   9153  N N   . TYR A 1 1172 ? 178.554 189.106 210.736 1.00 59.93  ? 1155 TYR B N   1 
ATOM   9154  C CA  . TYR A 1 1172 ? 177.574 188.032 210.899 1.00 59.93  ? 1155 TYR B CA  1 
ATOM   9155  C C   . TYR A 1 1172 ? 177.585 187.133 209.662 1.00 59.93  ? 1155 TYR B C   1 
ATOM   9156  O O   . TYR A 1 1172 ? 176.627 187.057 208.891 1.00 59.93  ? 1155 TYR B O   1 
ATOM   9157  C CB  . TYR A 1 1172 ? 176.186 188.605 211.146 1.00 59.93  ? 1155 TYR B CB  1 
ATOM   9158  C CG  . TYR A 1 1172 ? 176.066 189.444 212.392 1.00 59.93  ? 1155 TYR B CG  1 
ATOM   9159  C CD1 . TYR A 1 1172 ? 176.901 189.238 213.475 1.00 59.93  ? 1155 TYR B CD1 1 
ATOM   9160  C CD2 . TYR A 1 1172 ? 175.104 190.435 212.489 1.00 59.93  ? 1155 TYR B CD2 1 
ATOM   9161  C CE1 . TYR A 1 1172 ? 176.788 190.002 214.614 1.00 59.93  ? 1155 TYR B CE1 1 
ATOM   9162  C CE2 . TYR A 1 1172 ? 174.982 191.202 213.623 1.00 59.93  ? 1155 TYR B CE2 1 
ATOM   9163  C CZ  . TYR A 1 1172 ? 175.826 190.981 214.682 1.00 59.93  ? 1155 TYR B CZ  1 
ATOM   9164  O OH  . TYR A 1 1172 ? 175.707 191.744 215.817 1.00 59.93  ? 1155 TYR B OH  1 
ATOM   9165  N N   . ARG A 1 1173 ? 178.698 186.427 209.490 1.00 59.48  ? 1156 ARG B N   1 
ATOM   9166  C CA  . ARG A 1 1173 ? 178.896 185.566 208.337 1.00 59.48  ? 1156 ARG B CA  1 
ATOM   9167  C C   . ARG A 1 1173 ? 179.382 184.194 208.781 1.00 59.48  ? 1156 ARG B C   1 
ATOM   9168  O O   . ARG A 1 1173 ? 180.049 184.055 209.808 1.00 59.48  ? 1156 ARG B O   1 
ATOM   9169  C CB  . ARG A 1 1173 ? 179.901 186.173 207.356 1.00 59.48  ? 1156 ARG B CB  1 
ATOM   9170  C CG  . ARG A 1 1173 ? 179.440 187.467 206.714 1.00 59.48  ? 1156 ARG B CG  1 
ATOM   9171  C CD  . ARG A 1 1173 ? 178.044 187.329 206.136 1.00 59.48  ? 1156 ARG B CD  1 
ATOM   9172  N NE  . ARG A 1 1173 ? 177.931 186.191 205.231 1.00 59.48  ? 1156 ARG B NE  1 
ATOM   9173  C CZ  . ARG A 1 1173 ? 178.516 186.115 204.044 1.00 59.48  ? 1156 ARG B CZ  1 
ATOM   9174  N NH1 . ARG A 1 1173 ? 179.250 187.107 203.571 1.00 59.48  ? 1156 ARG B NH1 1 
ATOM   9175  N NH2 . ARG A 1 1173 ? 178.357 185.017 203.313 1.00 59.48  ? 1156 ARG B NH2 1 
ATOM   9176  N N   . GLY A 1 1174 ? 179.039 183.183 207.995 1.00 57.76  ? 1157 GLY B N   1 
ATOM   9177  C CA  . GLY A 1 1174 ? 179.523 181.843 208.242 1.00 57.76  ? 1157 GLY B CA  1 
ATOM   9178  C C   . GLY A 1 1174 ? 178.583 181.008 209.083 1.00 57.76  ? 1157 GLY B C   1 
ATOM   9179  O O   . GLY A 1 1174 ? 177.437 181.369 209.364 1.00 57.76  ? 1157 GLY B O   1 
ATOM   9180  N N   . ALA A 1 1175 ? 179.096 179.847 209.486 1.00 60.25  ? 1158 ALA B N   1 
ATOM   9181  C CA  . ALA A 1 1175 ? 178.345 178.897 210.295 1.00 60.25  ? 1158 ALA B CA  1 
ATOM   9182  C C   . ALA A 1 1175 ? 178.531 179.218 211.771 1.00 60.25  ? 1158 ALA B C   1 
ATOM   9183  O O   . ALA A 1 1175 ? 179.660 179.389 212.238 1.00 60.25  ? 1158 ALA B O   1 
ATOM   9184  C CB  . ALA A 1 1175 ? 178.793 177.466 210.002 1.00 60.25  ? 1158 ALA B CB  1 
ATOM   9185  N N   . LYS A 1 1176 ? 177.421 179.291 212.499 1.00 61.37  ? 1159 LYS B N   1 
ATOM   9186  C CA  . LYS A 1 1176 ? 177.449 179.712 213.891 1.00 61.37  ? 1159 LYS B CA  1 
ATOM   9187  C C   . LYS A 1 1176 ? 177.855 178.564 214.804 1.00 61.37  ? 1159 LYS B C   1 
ATOM   9188  O O   . LYS A 1 1176 ? 177.419 177.424 214.629 1.00 61.37  ? 1159 LYS B O   1 
ATOM   9189  C CB  . LYS A 1 1176 ? 176.081 180.254 214.303 1.00 61.37  ? 1159 LYS B CB  1 
ATOM   9190  C CG  . LYS A 1 1176 ? 175.438 181.121 213.238 1.00 61.37  ? 1159 LYS B CG  1 
ATOM   9191  C CD  . LYS A 1 1176 ? 174.067 181.625 213.650 1.00 61.37  ? 1159 LYS B CD  1 
ATOM   9192  C CE  . LYS A 1 1176 ? 173.224 180.528 214.264 1.00 61.37  ? 1159 LYS B CE  1 
ATOM   9193  N NZ  . LYS A 1 1176 ? 171.773 180.754 214.025 1.00 61.37  ? 1159 LYS B NZ  1 
ATOM   9194  N N   . PHE A 1 1177 ? 178.694 178.877 215.786 1.00 59.31  ? 1160 PHE B N   1 
ATOM   9195  C CA  . PHE A 1 1177 ? 179.163 177.912 216.768 1.00 59.31  ? 1160 PHE B CA  1 
ATOM   9196  C C   . PHE A 1 1177 ? 178.413 178.113 218.075 1.00 59.31  ? 1160 PHE B C   1 
ATOM   9197  O O   . PHE A 1 1177 ? 178.236 179.245 218.530 1.00 59.31  ? 1160 PHE B O   1 
ATOM   9198  C CB  . PHE A 1 1177 ? 180.661 178.069 217.026 1.00 59.31  ? 1160 PHE B CB  1 
ATOM   9199  C CG  . PHE A 1 1177 ? 181.538 177.443 215.982 1.00 59.31  ? 1160 PHE B CG  1 
ATOM   9200  C CD1 . PHE A 1 1177 ? 181.248 177.571 214.637 1.00 59.31  ? 1160 PHE B CD1 1 
ATOM   9201  C CD2 . PHE A 1 1177 ? 182.674 176.751 216.350 1.00 59.31  ? 1160 PHE B CD2 1 
ATOM   9202  C CE1 . PHE A 1 1177 ? 182.070 177.011 213.686 1.00 59.31  ? 1160 PHE B CE1 1 
ATOM   9203  C CE2 . PHE A 1 1177 ? 183.493 176.186 215.403 1.00 59.31  ? 1160 PHE B CE2 1 
ATOM   9204  C CZ  . PHE A 1 1177 ? 183.191 176.315 214.072 1.00 59.31  ? 1160 PHE B CZ  1 
ATOM   9205  N N   . ILE A 1 1178 ? 177.977 177.014 218.678 1.00 60.96  ? 1161 ILE B N   1 
ATOM   9206  C CA  . ILE A 1 1178 ? 177.355 177.057 219.993 1.00 60.96  ? 1161 ILE B CA  1 
ATOM   9207  C C   . ILE A 1 1178 ? 178.131 176.130 220.915 1.00 60.96  ? 1161 ILE B C   1 
ATOM   9208  O O   . ILE A 1 1178 ? 178.745 175.152 220.476 1.00 60.96  ? 1161 ILE B O   1 
ATOM   9209  C CB  . ILE A 1 1178 ? 175.860 176.677 219.959 1.00 60.96  ? 1161 ILE B CB  1 
ATOM   9210  C CG1 . ILE A 1 1178 ? 175.673 175.176 220.131 1.00 60.96  ? 1161 ILE B CG1 1 
ATOM   9211  C CG2 . ILE A 1 1178 ? 175.223 177.116 218.655 1.00 60.96  ? 1161 ILE B CG2 1 
ATOM   9212  C CD1 . ILE A 1 1178 ? 174.234 174.777 220.277 1.00 60.96  ? 1161 ILE B CD1 1 
ATOM   9213  N N   . ILE A 1 1179 ? 178.110 176.452 222.204 1.00 63.89  ? 1162 ILE B N   1 
ATOM   9214  C CA  . ILE A 1 1179 ? 178.908 175.759 223.206 1.00 63.89  ? 1162 ILE B CA  1 
ATOM   9215  C C   . ILE A 1 1179 ? 177.963 175.060 224.172 1.00 63.89  ? 1162 ILE B C   1 
ATOM   9216  O O   . ILE A 1 1179 ? 177.153 175.714 224.841 1.00 63.89  ? 1162 ILE B O   1 
ATOM   9217  C CB  . ILE A 1 1179 ? 179.838 176.727 223.949 1.00 63.89  ? 1162 ILE B CB  1 
ATOM   9218  C CG1 . ILE A 1 1179 ? 180.520 177.666 222.958 1.00 63.89  ? 1162 ILE B CG1 1 
ATOM   9219  C CG2 . ILE A 1 1179 ? 180.869 175.965 224.736 1.00 63.89  ? 1162 ILE B CG2 1 
ATOM   9220  C CD1 . ILE A 1 1179 ? 181.365 178.724 223.612 1.00 63.89  ? 1162 ILE B CD1 1 
ATOM   9221  N N   . LYS A 1 1180 ? 177.973 173.730 224.139 1.00 68.02  ? 1163 LYS B N   1 
ATOM   9222  C CA  . LYS A 1 1180 ? 177.064 172.953 225.007 1.00 68.02  ? 1163 LYS B CA  1 
ATOM   9223  C C   . LYS A 1 1180 ? 177.894 172.476 226.194 1.00 68.02  ? 1163 LYS B C   1 
ATOM   9224  O O   . LYS A 1 1180 ? 179.054 172.114 225.957 1.00 68.02  ? 1163 LYS B O   1 
ATOM   9225  C CB  . LYS A 1 1180 ? 176.520 171.763 224.226 1.00 68.02  ? 1163 LYS B CB  1 
ATOM   9226  C CG  . LYS A 1 1180 ? 175.876 172.097 222.894 1.00 68.02  ? 1163 LYS B CG  1 
ATOM   9227  C CD  . LYS A 1 1180 ? 174.547 172.762 223.088 1.00 68.02  ? 1163 LYS B CD  1 
ATOM   9228  C CE  . LYS A 1 1180 ? 173.379 171.846 222.807 1.00 68.02  ? 1163 LYS B CE  1 
ATOM   9229  N NZ  . LYS A 1 1180 ? 172.095 172.500 223.150 1.00 68.02  ? 1163 LYS B NZ  1 
ATOM   9230  N N   . LYS A 1 1181 ? 177.346 172.468 227.411 1.00 75.77  ? 1164 LYS B N   1 
ATOM   9231  C CA  . LYS A 1 1181 ? 178.171 172.108 228.593 1.00 75.77  ? 1164 LYS B CA  1 
ATOM   9232  C C   . LYS A 1 1181 ? 178.579 170.640 228.509 1.00 75.77  ? 1164 LYS B C   1 
ATOM   9233  O O   . LYS A 1 1181 ? 177.929 169.898 227.762 1.00 75.77  ? 1164 LYS B O   1 
ATOM   9234  C CB  . LYS A 1 1181 ? 177.381 172.303 229.883 1.00 75.77  ? 1164 LYS B CB  1 
ATOM   9235  C CG  . LYS A 1 1181 ? 176.944 173.725 230.192 1.00 75.77  ? 1164 LYS B CG  1 
ATOM   9236  C CD  . LYS A 1 1181 ? 176.888 174.005 231.677 1.00 75.77  ? 1164 LYS B CD  1 
ATOM   9237  C CE  . LYS A 1 1181 ? 175.768 174.944 232.069 1.00 75.77  ? 1164 LYS B CE  1 
ATOM   9238  N NZ  . LYS A 1 1181 ? 175.933 175.438 233.455 1.00 75.77  ? 1164 LYS B NZ  1 
ATOM   9239  N N   . TYR A 1 1182 ? 179.598 170.230 229.263 1.00 97.10  ? 1165 TYR B N   1 
ATOM   9240  C CA  . TYR A 1 1182 ? 179.971 168.793 229.308 1.00 97.10  ? 1165 TYR B CA  1 
ATOM   9241  C C   . TYR A 1 1182 ? 180.196 168.403 230.741 1.00 97.10  ? 1165 TYR B C   1 
ATOM   9242  O O   . TYR A 1 1182 ? 179.575 167.423 231.191 1.00 97.10  ? 1165 TYR B O   1 
ATOM   9243  C CB  . TYR A 1 1182 ? 181.273 168.502 228.570 1.00 97.10  ? 1165 TYR B CB  1 
ATOM   9244  C CG  . TYR A 1 1182 ? 181.873 167.121 228.769 1.00 97.10  ? 1165 TYR B CG  1 
ATOM   9245  C CD1 . TYR A 1 1182 ? 181.141 165.975 228.500 1.00 97.10  ? 1165 TYR B CD1 1 
ATOM   9246  C CD2 . TYR A 1 1182 ? 183.179 166.972 229.209 1.00 97.10  ? 1165 TYR B CD2 1 
ATOM   9247  C CE1 . TYR A 1 1182 ? 181.686 164.716 228.678 1.00 97.10  ? 1165 TYR B CE1 1 
ATOM   9248  C CE2 . TYR A 1 1182 ? 183.737 165.719 229.389 1.00 97.10  ? 1165 TYR B CE2 1 
ATOM   9249  C CZ  . TYR A 1 1182 ? 182.988 164.588 229.122 1.00 97.10  ? 1165 TYR B CZ  1 
ATOM   9250  O OH  . TYR A 1 1182 ? 183.534 163.351 229.297 1.00 97.10  ? 1165 TYR B OH  1 
ATOM   9251  N N   . ALA A 1 1183 ? 181.006 169.173 231.467 1.00 111.54 ? 1166 ALA B N   1 
ATOM   9252  C CA  . ALA A 1 1183 ? 181.380 168.788 232.822 1.00 111.54 ? 1166 ALA B CA  1 
ATOM   9253  C C   . ALA A 1 1183 ? 181.424 169.980 233.773 1.00 111.54 ? 1166 ALA B C   1 
ATOM   9254  O O   . ALA A 1 1183 ? 182.077 169.901 234.821 1.00 111.54 ? 1166 ALA B O   1 
ATOM   9255  C CB  . ALA A 1 1183 ? 182.736 168.074 232.831 1.00 111.54 ? 1166 ALA B CB  1 
ATOM   9256  N N   . SER A 1 1184 ? 180.757 171.081 233.438 1.00 117.59 ? 1167 SER B N   1 
ATOM   9257  C CA  . SER A 1 1184 ? 180.736 172.252 234.302 1.00 117.59 ? 1167 SER B CA  1 
ATOM   9258  C C   . SER A 1 1184 ? 179.681 172.066 235.386 1.00 117.59 ? 1167 SER B C   1 
ATOM   9259  O O   . SER A 1 1184 ? 178.486 171.971 235.089 1.00 117.59 ? 1167 SER B O   1 
ATOM   9260  C CB  . SER A 1 1184 ? 180.456 173.513 233.486 1.00 117.59 ? 1167 SER B CB  1 
ATOM   9261  O OG  . SER A 1 1184 ? 180.563 174.674 234.291 1.00 117.59 ? 1167 SER B OG  1 
ATOM   9262  N N   . GLY A 1 1185 ? 180.125 172.015 236.645 1.00 125.46 ? 1168 GLY B N   1 
ATOM   9263  C CA  . GLY A 1 1185 ? 179.195 171.858 237.749 1.00 125.46 ? 1168 GLY B CA  1 
ATOM   9264  C C   . GLY A 1 1185 ? 178.445 173.117 238.121 1.00 125.46 ? 1168 GLY B C   1 
ATOM   9265  O O   . GLY A 1 1185 ? 177.430 173.035 238.820 1.00 125.46 ? 1168 GLY B O   1 
ATOM   9266  N N   . ASN A 1 1186 ? 178.922 174.275 237.673 1.00 116.94 ? 1169 ASN B N   1 
ATOM   9267  C CA  . ASN A 1 1186 ? 178.229 175.527 237.946 1.00 116.94 ? 1169 ASN B CA  1 
ATOM   9268  C C   . ASN A 1 1186 ? 176.894 175.561 237.213 1.00 116.94 ? 1169 ASN B C   1 
ATOM   9269  O O   . ASN A 1 1186 ? 176.810 175.206 236.034 1.00 116.94 ? 1169 ASN B O   1 
ATOM   9270  C CB  . ASN A 1 1186 ? 179.099 176.710 237.528 1.00 116.94 ? 1169 ASN B CB  1 
ATOM   9271  C CG  . ASN A 1 1186 ? 179.919 177.263 238.675 1.00 116.94 ? 1169 ASN B CG  1 
ATOM   9272  O OD1 . ASN A 1 1186 ? 179.508 178.209 239.348 1.00 116.94 ? 1169 ASN B OD1 1 
ATOM   9273  N ND2 . ASN A 1 1186 ? 181.087 176.674 238.906 1.00 116.94 ? 1169 ASN B ND2 1 
ATOM   9274  N N   . LYS A 1 1187 ? 175.847 175.992 237.916 1.00 113.97 ? 1170 LYS B N   1 
ATOM   9275  C CA  . LYS A 1 1187 ? 174.509 175.991 237.341 1.00 113.97 ? 1170 LYS B CA  1 
ATOM   9276  C C   . LYS A 1 1187 ? 174.272 177.150 236.382 1.00 113.97 ? 1170 LYS B C   1 
ATOM   9277  O O   . LYS A 1 1187 ? 173.332 177.088 235.583 1.00 113.97 ? 1170 LYS B O   1 
ATOM   9278  C CB  . LYS A 1 1187 ? 173.458 176.016 238.452 1.00 113.97 ? 1170 LYS B CB  1 
ATOM   9279  C CG  . LYS A 1 1187 ? 173.372 174.719 239.239 1.00 113.97 ? 1170 LYS B CG  1 
ATOM   9280  C CD  . LYS A 1 1187 ? 171.971 174.489 239.782 1.00 113.97 ? 1170 LYS B CD  1 
ATOM   9281  C CE  . LYS A 1 1187 ? 171.774 173.039 240.193 1.00 113.97 ? 1170 LYS B CE  1 
ATOM   9282  N NZ  . LYS A 1 1187 ? 170.413 172.797 240.746 1.00 113.97 ? 1170 LYS B NZ  1 
ATOM   9283  N N   . ASP A 1 1188 ? 175.091 178.197 236.440 1.00 105.07 ? 1171 ASP B N   1 
ATOM   9284  C CA  . ASP A 1 1188 ? 174.953 179.291 235.494 1.00 105.07 ? 1171 ASP B CA  1 
ATOM   9285  C C   . ASP A 1 1188 ? 175.571 178.914 234.152 1.00 105.07 ? 1171 ASP B C   1 
ATOM   9286  O O   . ASP A 1 1188 ? 176.416 178.018 234.053 1.00 105.07 ? 1171 ASP B O   1 
ATOM   9287  C CB  . ASP A 1 1188 ? 175.599 180.567 236.040 1.00 105.07 ? 1171 ASP B CB  1 
ATOM   9288  C CG  . ASP A 1 1188 ? 176.965 180.317 236.644 1.00 105.07 ? 1171 ASP B CG  1 
ATOM   9289  O OD1 . ASP A 1 1188 ? 177.518 179.217 236.439 1.00 105.07 ? 1171 ASP B OD1 1 
ATOM   9290  O OD2 . ASP A 1 1188 ? 177.486 181.222 237.328 1.00 105.07 ? 1171 ASP B OD2 1 
ATOM   9291  N N   . ASN A 1 1189 ? 175.137 179.615 233.105 1.00 92.29  ? 1172 ASN B N   1 
ATOM   9292  C CA  . ASN A 1 1189 ? 175.571 179.336 231.746 1.00 92.29  ? 1172 ASN B CA  1 
ATOM   9293  C C   . ASN A 1 1189 ? 176.837 180.094 231.361 1.00 92.29  ? 1172 ASN B C   1 
ATOM   9294  O O   . ASN A 1 1189 ? 177.174 180.158 230.174 1.00 92.29  ? 1172 ASN B O   1 
ATOM   9295  C CB  . ASN A 1 1189 ? 174.448 179.656 230.758 1.00 92.29  ? 1172 ASN B CB  1 
ATOM   9296  C CG  . ASN A 1 1189 ? 173.927 181.069 230.910 1.00 92.29  ? 1172 ASN B CG  1 
ATOM   9297  O OD1 . ASN A 1 1189 ? 174.190 181.735 231.912 1.00 92.29  ? 1172 ASN B OD1 1 
ATOM   9298  N ND2 . ASN A 1 1189 ? 173.184 181.536 229.914 1.00 92.29  ? 1172 ASN B ND2 1 
ATOM   9299  N N   . ILE A 1 1190 ? 177.540 180.667 232.331 1.00 89.81  ? 1173 ILE B N   1 
ATOM   9300  C CA  . ILE A 1 1190 ? 178.777 181.395 232.071 1.00 89.81  ? 1173 ILE B CA  1 
ATOM   9301  C C   . ILE A 1 1190 ? 179.925 180.400 232.009 1.00 89.81  ? 1173 ILE B C   1 
ATOM   9302  O O   . ILE A 1 1190 ? 180.108 179.588 232.924 1.00 89.81  ? 1173 ILE B O   1 
ATOM   9303  C CB  . ILE A 1 1190 ? 179.030 182.457 233.154 1.00 89.81  ? 1173 ILE B CB  1 
ATOM   9304  C CG1 . ILE A 1 1190 ? 177.892 183.477 233.183 1.00 89.81  ? 1173 ILE B CG1 1 
ATOM   9305  C CG2 . ILE A 1 1190 ? 180.357 183.154 232.915 1.00 89.81  ? 1173 ILE B CG2 1 
ATOM   9306  C CD1 . ILE A 1 1190 ? 177.620 184.125 231.849 1.00 89.81  ? 1173 ILE B CD1 1 
ATOM   9307  N N   . VAL A 1 1191 ? 180.700 180.459 230.932 1.00 82.06  ? 1174 VAL B N   1 
ATOM   9308  C CA  . VAL A 1 1191 ? 181.867 179.602 230.766 1.00 82.06  ? 1174 VAL B CA  1 
ATOM   9309  C C   . VAL A 1 1191 ? 183.067 180.282 231.409 1.00 82.06  ? 1174 VAL B C   1 
ATOM   9310  O O   . VAL A 1 1191 ? 183.136 181.515 231.484 1.00 82.06  ? 1174 VAL B O   1 
ATOM   9311  C CB  . VAL A 1 1191 ? 182.117 179.292 229.277 1.00 82.06  ? 1174 VAL B CB  1 
ATOM   9312  C CG1 . VAL A 1 1191 ? 182.904 180.403 228.616 1.00 82.06  ? 1174 VAL B CG1 1 
ATOM   9313  C CG2 . VAL A 1 1191 ? 182.845 177.970 229.126 1.00 82.06  ? 1174 VAL B CG2 1 
ATOM   9314  N N   . ARG A 1 1192 ? 184.002 179.479 231.908 1.00 90.32  ? 1175 ARG B N   1 
ATOM   9315  C CA  . ARG A 1 1192 ? 185.189 179.981 232.587 1.00 90.32  ? 1175 ARG B CA  1 
ATOM   9316  C C   . ARG A 1 1192 ? 186.422 179.266 232.046 1.00 90.32  ? 1175 ARG B C   1 
ATOM   9317  O O   . ARG A 1 1192 ? 186.332 178.370 231.202 1.00 90.32  ? 1175 ARG B O   1 
ATOM   9318  C CB  . ARG A 1 1192 ? 185.081 179.806 234.107 1.00 90.32  ? 1175 ARG B CB  1 
ATOM   9319  C CG  . ARG A 1 1192 ? 183.878 180.497 234.723 1.00 90.32  ? 1175 ARG B CG  1 
ATOM   9320  C CD  . ARG A 1 1192 ? 183.649 180.045 236.152 1.00 90.32  ? 1175 ARG B CD  1 
ATOM   9321  N NE  . ARG A 1 1192 ? 182.486 180.695 236.744 1.00 90.32  ? 1175 ARG B NE  1 
ATOM   9322  C CZ  . ARG A 1 1192 ? 181.229 180.345 236.504 1.00 90.32  ? 1175 ARG B CZ  1 
ATOM   9323  N NH1 . ARG A 1 1192 ? 180.933 179.342 235.694 1.00 90.32  ? 1175 ARG B NH1 1 
ATOM   9324  N NH2 . ARG A 1 1192 ? 180.245 181.017 237.095 1.00 90.32  ? 1175 ARG B NH2 1 
ATOM   9325  N N   . ASN A 1 1193 ? 187.585 179.676 232.547 1.00 91.15  ? 1176 ASN B N   1 
ATOM   9326  C CA  . ASN A 1 1193 ? 188.849 179.130 232.078 1.00 91.15  ? 1176 ASN B CA  1 
ATOM   9327  C C   . ASN A 1 1193 ? 188.947 177.640 232.391 1.00 91.15  ? 1176 ASN B C   1 
ATOM   9328  O O   . ASN A 1 1193 ? 188.460 177.166 233.421 1.00 91.15  ? 1176 ASN B O   1 
ATOM   9329  C CB  . ASN A 1 1193 ? 190.015 179.879 232.725 1.00 91.15  ? 1176 ASN B CB  1 
ATOM   9330  C CG  . ASN A 1 1193 ? 191.256 179.882 231.859 1.00 91.15  ? 1176 ASN B CG  1 
ATOM   9331  O OD1 . ASN A 1 1193 ? 191.182 179.690 230.646 1.00 91.15  ? 1176 ASN B OD1 1 
ATOM   9332  N ND2 . ASN A 1 1193 ? 192.408 180.104 232.479 1.00 91.15  ? 1176 ASN B ND2 1 
ATOM   9333  N N   . ASN A 1 1194 ? 189.618 176.937 231.471 1.00 92.60  ? 1177 ASN B N   1 
ATOM   9334  C CA  . ASN A 1 1194 ? 189.874 175.479 231.609 1.00 92.60  ? 1177 ASN B CA  1 
ATOM   9335  C C   . ASN A 1 1194 ? 188.576 174.672 231.696 1.00 92.60  ? 1177 ASN B C   1 
ATOM   9336  O O   . ASN A 1 1194 ? 188.653 173.505 232.095 1.00 92.60  ? 1177 ASN B O   1 
ATOM   9337  C CB  . ASN A 1 1194 ? 190.853 175.207 232.746 1.00 92.60  ? 1177 ASN B CB  1 
ATOM   9338  C CG  . ASN A 1 1194 ? 192.002 176.191 232.746 1.00 92.60  ? 1177 ASN B CG  1 
ATOM   9339  O OD1 . ASN A 1 1194 ? 192.241 176.866 231.749 1.00 92.60  ? 1177 ASN B OD1 1 
ATOM   9340  N ND2 . ASN A 1 1194 ? 192.713 176.283 233.858 1.00 92.60  ? 1177 ASN B ND2 1 
ATOM   9341  N N   . ASP A 1 1195 ? 187.439 175.246 231.305 1.00 94.94  ? 1178 ASP B N   1 
ATOM   9342  C CA  . ASP A 1 1195 ? 186.192 174.443 231.275 1.00 94.94  ? 1178 ASP B CA  1 
ATOM   9343  C C   . ASP A 1 1195 ? 186.321 173.404 230.172 1.00 94.94  ? 1178 ASP B C   1 
ATOM   9344  O O   . ASP A 1 1195 ? 187.100 173.646 229.249 1.00 94.94  ? 1178 ASP B O   1 
ATOM   9345  C CB  . ASP A 1 1195 ? 184.969 175.301 230.979 1.00 94.94  ? 1178 ASP B CB  1 
ATOM   9346  C CG  . ASP A 1 1195 ? 184.422 176.010 232.201 1.00 94.94  ? 1178 ASP B CG  1 
ATOM   9347  O OD1 . ASP A 1 1195 ? 185.224 176.322 233.097 1.00 94.94  ? 1178 ASP B OD1 1 
ATOM   9348  O OD2 . ASP A 1 1195 ? 183.200 176.244 232.242 1.00 94.94  ? 1178 ASP B OD2 1 
ATOM   9349  N N   . ARG A 1 1196 ? 185.601 172.291 230.267 1.00 94.70  ? 1179 ARG B N   1 
ATOM   9350  C CA  . ARG A 1 1196 ? 185.595 171.316 229.150 1.00 94.70  ? 1179 ARG B CA  1 
ATOM   9351  C C   . ARG A 1 1196 ? 184.236 171.485 228.484 1.00 94.70  ? 1179 ARG B C   1 
ATOM   9352  O O   . ARG A 1 1196 ? 183.256 171.546 229.226 1.00 94.70  ? 1179 ARG B O   1 
ATOM   9353  C CB  . ARG A 1 1196 ? 185.838 169.899 229.664 1.00 94.70  ? 1179 ARG B CB  1 
ATOM   9354  C CG  . ARG A 1 1196 ? 187.310 169.551 229.812 1.00 94.70  ? 1179 ARG B CG  1 
ATOM   9355  C CD  . ARG A 1 1196 ? 187.501 168.114 230.248 1.00 94.70  ? 1179 ARG B CD  1 
ATOM   9356  N NE  . ARG A 1 1196 ? 188.248 167.337 229.272 1.00 94.70  ? 1179 ARG B NE  1 
ATOM   9357  C CZ  . ARG A 1 1196 ? 188.229 166.011 229.201 1.00 94.70  ? 1179 ARG B CZ  1 
ATOM   9358  N NH1 . ARG A 1 1196 ? 187.225 165.338 229.732 1.00 94.70  ? 1179 ARG B NH1 1 
ATOM   9359  N NH2 . ARG A 1 1196 ? 189.215 165.364 228.603 1.00 94.70  ? 1179 ARG B NH2 1 
ATOM   9360  N N   . VAL A 1 1197 ? 184.172 171.603 227.159 1.00 69.41  ? 1180 VAL B N   1 
ATOM   9361  C CA  . VAL A 1 1197 ? 182.860 171.913 226.536 1.00 69.41  ? 1180 VAL B CA  1 
ATOM   9362  C C   . VAL A 1 1197 ? 182.686 171.171 225.227 1.00 69.41  ? 1180 VAL B C   1 
ATOM   9363  O O   . VAL A 1 1197 ? 183.686 170.687 224.704 1.00 69.41  ? 1180 VAL B O   1 
ATOM   9364  C CB  . VAL A 1 1197 ? 182.766 173.410 226.231 1.00 69.41  ? 1180 VAL B CB  1 
ATOM   9365  C CG1 . VAL A 1 1197 ? 182.962 174.281 227.459 1.00 69.41  ? 1180 VAL B CG1 1 
ATOM   9366  C CG2 . VAL A 1 1197 ? 183.725 173.814 225.128 1.00 69.41  ? 1180 VAL B CG2 1 
ATOM   9367  N N   . TYR A 1 1198 ? 181.447 171.008 224.780 1.00 67.90  ? 1181 TYR B N   1 
ATOM   9368  C CA  . TYR A 1 1198 ? 181.226 170.502 223.436 1.00 67.90  ? 1181 TYR B CA  1 
ATOM   9369  C C   . TYR A 1 1198 ? 180.939 171.670 222.504 1.00 67.90  ? 1181 TYR B C   1 
ATOM   9370  O O   . TYR A 1 1198 ? 180.396 172.695 222.922 1.00 67.90  ? 1181 TYR B O   1 
ATOM   9371  C CB  . TYR A 1 1198 ? 180.054 169.519 223.394 1.00 67.90  ? 1181 TYR B CB  1 
ATOM   9372  C CG  . TYR A 1 1198 ? 180.362 168.155 223.953 1.00 67.90  ? 1181 TYR B CG  1 
ATOM   9373  C CD1 . TYR A 1 1198 ? 181.583 167.550 223.721 1.00 67.90  ? 1181 TYR B CD1 1 
ATOM   9374  C CD2 . TYR A 1 1198 ? 179.422 167.466 224.703 1.00 67.90  ? 1181 TYR B CD2 1 
ATOM   9375  C CE1 . TYR A 1 1198 ? 181.866 166.301 224.228 1.00 67.90  ? 1181 TYR B CE1 1 
ATOM   9376  C CE2 . TYR A 1 1198 ? 179.694 166.216 225.213 1.00 67.90  ? 1181 TYR B CE2 1 
ATOM   9377  C CZ  . TYR A 1 1198 ? 180.919 165.638 224.972 1.00 67.90  ? 1181 TYR B CZ  1 
ATOM   9378  O OH  . TYR A 1 1198 ? 181.202 164.392 225.477 1.00 67.90  ? 1181 TYR B OH  1 
ATOM   9379  N N   . ILE A 1 1199 ? 181.294 171.511 221.234 1.00 62.90  ? 1182 ILE B N   1 
ATOM   9380  C CA  . ILE A 1 1199 ? 181.079 172.539 220.225 1.00 62.90  ? 1182 ILE B CA  1 
ATOM   9381  C C   . ILE A 1 1199 ? 180.124 171.991 219.176 1.00 62.90  ? 1182 ILE B C   1 
ATOM   9382  O O   . ILE A 1 1199 ? 180.341 170.895 218.648 1.00 62.90  ? 1182 ILE B O   1 
ATOM   9383  C CB  . ILE A 1 1199 ? 182.401 172.983 219.576 1.00 62.90  ? 1182 ILE B CB  1 
ATOM   9384  C CG1 . ILE A 1 1199 ? 183.446 173.290 220.646 1.00 62.90  ? 1182 ILE B CG1 1 
ATOM   9385  C CG2 . ILE A 1 1199 ? 182.175 174.196 218.704 1.00 62.90  ? 1182 ILE B CG2 1 
ATOM   9386  C CD1 . ILE A 1 1199 ? 183.327 174.668 221.239 1.00 62.90  ? 1182 ILE B CD1 1 
ATOM   9387  N N   . ASN A 1 1200 ? 179.071 172.747 218.879 1.00 63.16  ? 1183 ASN B N   1 
ATOM   9388  C CA  . ASN A 1 1200 ? 178.127 172.401 217.827 1.00 63.16  ? 1183 ASN B CA  1 
ATOM   9389  C C   . ASN A 1 1200 ? 178.168 173.462 216.740 1.00 63.16  ? 1183 ASN B C   1 
ATOM   9390  O O   . ASN A 1 1200 ? 178.247 174.657 217.032 1.00 63.16  ? 1183 ASN B O   1 
ATOM   9391  C CB  . ASN A 1 1200 ? 176.702 172.278 218.366 1.00 63.16  ? 1183 ASN B CB  1 
ATOM   9392  C CG  . ASN A 1 1200 ? 176.475 170.996 219.130 1.00 63.16  ? 1183 ASN B CG  1 
ATOM   9393  O OD1 . ASN A 1 1200 ? 177.415 170.259 219.418 1.00 63.16  ? 1183 ASN B OD1 1 
ATOM   9394  N ND2 . ASN A 1 1200 ? 175.220 170.719 219.459 1.00 63.16  ? 1183 ASN B ND2 1 
ATOM   9395  N N   . VAL A 1 1201 ? 178.116 173.025 215.489 1.00 63.87  ? 1184 VAL B N   1 
ATOM   9396  C CA  . VAL A 1 1201 ? 178.062 173.919 214.341 1.00 63.87  ? 1184 VAL B CA  1 
ATOM   9397  C C   . VAL A 1 1201 ? 176.691 173.784 213.702 1.00 63.87  ? 1184 VAL B C   1 
ATOM   9398  O O   . VAL A 1 1201 ? 176.165 172.674 213.571 1.00 63.87  ? 1184 VAL B O   1 
ATOM   9399  C CB  . VAL A 1 1201 ? 179.177 173.609 213.326 1.00 63.87  ? 1184 VAL B CB  1 
ATOM   9400  C CG1 . VAL A 1 1201 ? 180.512 174.004 213.895 1.00 63.87  ? 1184 VAL B CG1 1 
ATOM   9401  C CG2 . VAL A 1 1201 ? 179.176 172.140 212.971 1.00 63.87  ? 1184 VAL B CG2 1 
ATOM   9402  N N   . VAL A 1 1202 ? 176.099 174.909 213.322 1.00 67.40  ? 1185 VAL B N   1 
ATOM   9403  C CA  . VAL A 1 1202 ? 174.768 174.914 212.732 1.00 67.40  ? 1185 VAL B CA  1 
ATOM   9404  C C   . VAL A 1 1202 ? 174.895 174.965 211.215 1.00 67.40  ? 1185 VAL B C   1 
ATOM   9405  O O   . VAL A 1 1202 ? 175.598 175.820 210.662 1.00 67.40  ? 1185 VAL B O   1 
ATOM   9406  C CB  . VAL A 1 1202 ? 173.913 176.070 213.283 1.00 67.40  ? 1185 VAL B CB  1 
ATOM   9407  C CG1 . VAL A 1 1202 ? 173.879 176.011 214.798 1.00 67.40  ? 1185 VAL B CG1 1 
ATOM   9408  C CG2 . VAL A 1 1202 ? 174.443 177.416 212.840 1.00 67.40  ? 1185 VAL B CG2 1 
ATOM   9409  N N   . VAL A 1 1203 ? 174.264 174.005 210.547 1.00 72.83  ? 1186 VAL B N   1 
ATOM   9410  C CA  . VAL A 1 1203 ? 174.153 173.967 209.096 1.00 72.83  ? 1186 VAL B CA  1 
ATOM   9411  C C   . VAL A 1 1203 ? 172.690 173.717 208.767 1.00 72.83  ? 1186 VAL B C   1 
ATOM   9412  O O   . VAL A 1 1203 ? 172.109 172.728 209.232 1.00 72.83  ? 1186 VAL B O   1 
ATOM   9413  C CB  . VAL A 1 1203 ? 175.040 172.879 208.469 1.00 72.83  ? 1186 VAL B CB  1 
ATOM   9414  C CG1 . VAL A 1 1203 ? 175.065 173.026 206.959 1.00 72.83  ? 1186 VAL B CG1 1 
ATOM   9415  C CG2 . VAL A 1 1203 ? 176.446 172.947 209.032 1.00 72.83  ? 1186 VAL B CG2 1 
ATOM   9416  N N   . LYS A 1 1204 ? 172.096 174.613 207.978 1.00 80.30  ? 1187 LYS B N   1 
ATOM   9417  C CA  . LYS A 1 1204 ? 170.686 174.516 207.598 1.00 80.30  ? 1187 LYS B CA  1 
ATOM   9418  C C   . LYS A 1 1204 ? 169.793 174.381 208.828 1.00 80.30  ? 1187 LYS B C   1 
ATOM   9419  O O   . LYS A 1 1204 ? 168.873 173.563 208.870 1.00 80.30  ? 1187 LYS B O   1 
ATOM   9420  C CB  . LYS A 1 1204 ? 170.460 173.358 206.625 1.00 80.30  ? 1187 LYS B CB  1 
ATOM   9421  C CG  . LYS A 1 1204 ? 171.417 173.351 205.444 1.00 80.30  ? 1187 LYS B CG  1 
ATOM   9422  C CD  . LYS A 1 1204 ? 171.492 174.717 204.781 1.00 80.30  ? 1187 LYS B CD  1 
ATOM   9423  C CE  . LYS A 1 1204 ? 172.170 174.632 203.425 1.00 80.30  ? 1187 LYS B CE  1 
ATOM   9424  N NZ  . LYS A 1 1204 ? 172.092 173.261 202.850 1.00 80.30  ? 1187 LYS B NZ  1 
ATOM   9425  N N   . ASN A 1 1205 ? 170.074 175.205 209.841 1.00 80.17  ? 1188 ASN B N   1 
ATOM   9426  C CA  . ASN A 1 1205 ? 169.340 175.199 211.109 1.00 80.17  ? 1188 ASN B CA  1 
ATOM   9427  C C   . ASN A 1 1205 ? 169.321 173.815 211.752 1.00 80.17  ? 1188 ASN B C   1 
ATOM   9428  O O   . ASN A 1 1205 ? 168.350 173.435 212.409 1.00 80.17  ? 1188 ASN B O   1 
ATOM   9429  C CB  . ASN A 1 1205 ? 167.913 175.732 210.941 1.00 80.17  ? 1188 ASN B CB  1 
ATOM   9430  C CG  . ASN A 1 1205 ? 167.822 176.880 209.950 1.00 80.17  ? 1188 ASN B CG  1 
ATOM   9431  O OD1 . ASN A 1 1205 ? 168.265 176.778 208.809 1.00 80.17  ? 1188 ASN B OD1 1 
ATOM   9432  N ND2 . ASN A 1 1205 ? 167.238 177.988 210.392 1.00 80.17  ? 1188 ASN B ND2 1 
ATOM   9433  N N   . LYS A 1 1206 ? 170.395 173.049 211.571 1.00 74.18  ? 1189 LYS B N   1 
ATOM   9434  C CA  . LYS A 1 1206 ? 170.544 171.752 212.215 1.00 74.18  ? 1189 LYS B CA  1 
ATOM   9435  C C   . LYS A 1 1206 ? 171.933 171.661 212.825 1.00 74.18  ? 1189 LYS B C   1 
ATOM   9436  O O   . LYS A 1 1206 ? 172.911 172.112 212.227 1.00 74.18  ? 1189 LYS B O   1 
ATOM   9437  C CB  . LYS A 1 1206 ? 170.316 170.604 211.227 1.00 74.18  ? 1189 LYS B CB  1 
ATOM   9438  C CG  . LYS A 1 1206 ? 170.369 169.222 211.856 1.00 74.18  ? 1189 LYS B CG  1 
ATOM   9439  C CD  . LYS A 1 1206 ? 169.496 168.241 211.093 1.00 74.18  ? 1189 LYS B CD  1 
ATOM   9440  C CE  . LYS A 1 1206 ? 170.151 166.877 210.987 1.00 74.18  ? 1189 LYS B CE  1 
ATOM   9441  N NZ  . LYS A 1 1206 ? 171.152 166.826 209.888 1.00 74.18  ? 1189 LYS B NZ  1 
ATOM   9442  N N   . GLU A 1 1207 ? 172.016 171.074 214.013 1.00 72.73  ? 1190 GLU B N   1 
ATOM   9443  C CA  . GLU A 1 1207 ? 173.249 171.074 214.785 1.00 72.73  ? 1190 GLU B CA  1 
ATOM   9444  C C   . GLU A 1 1207 ? 174.072 169.824 214.504 1.00 72.73  ? 1190 GLU B C   1 
ATOM   9445  O O   . GLU A 1 1207 ? 173.537 168.714 214.435 1.00 72.73  ? 1190 GLU B O   1 
ATOM   9446  C CB  . GLU A 1 1207 ? 172.933 171.166 216.275 1.00 72.73  ? 1190 GLU B CB  1 
ATOM   9447  C CG  . GLU A 1 1207 ? 172.115 172.386 216.647 1.00 72.73  ? 1190 GLU B CG  1 
ATOM   9448  C CD  . GLU A 1 1207 ? 172.344 172.820 218.075 1.00 72.73  ? 1190 GLU B CD  1 
ATOM   9449  O OE1 . GLU A 1 1207 ? 173.159 172.174 218.767 1.00 72.73  ? 1190 GLU B OE1 1 
ATOM   9450  O OE2 . GLU A 1 1207 ? 171.707 173.801 218.508 1.00 72.73  ? 1190 GLU B OE2 1 
ATOM   9451  N N   . TYR A 1 1208 ? 175.379 170.014 214.345 1.00 66.72  ? 1191 TYR B N   1 
ATOM   9452  C CA  . TYR A 1 1208 ? 176.319 168.924 214.131 1.00 66.72  ? 1191 TYR B CA  1 
ATOM   9453  C C   . TYR A 1 1208 ? 177.463 169.055 215.123 1.00 66.72  ? 1191 TYR B C   1 
ATOM   9454  O O   . TYR A 1 1208 ? 178.028 170.141 215.281 1.00 66.72  ? 1191 TYR B O   1 
ATOM   9455  C CB  . TYR A 1 1208 ? 176.859 168.929 212.701 1.00 66.72  ? 1191 TYR B CB  1 
ATOM   9456  C CG  . TYR A 1 1208 ? 175.808 168.704 211.645 1.00 66.72  ? 1191 TYR B CG  1 
ATOM   9457  C CD1 . TYR A 1 1208 ? 175.435 167.422 211.275 1.00 66.72  ? 1191 TYR B CD1 1 
ATOM   9458  C CD2 . TYR A 1 1208 ? 175.202 169.770 211.005 1.00 66.72  ? 1191 TYR B CD2 1 
ATOM   9459  C CE1 . TYR A 1 1208 ? 174.481 167.208 210.309 1.00 66.72  ? 1191 TYR B CE1 1 
ATOM   9460  C CE2 . TYR A 1 1208 ? 174.246 169.566 210.034 1.00 66.72  ? 1191 TYR B CE2 1 
ATOM   9461  C CZ  . TYR A 1 1208 ? 173.890 168.283 209.690 1.00 66.72  ? 1191 TYR B CZ  1 
ATOM   9462  O OH  . TYR A 1 1208 ? 172.935 168.072 208.722 1.00 66.72  ? 1191 TYR B OH  1 
ATOM   9463  N N   . ARG A 1 1209 ? 177.797 167.954 215.788 1.00 63.83  ? 1192 ARG B N   1 
ATOM   9464  C CA  . ARG A 1 1209 ? 178.894 167.960 216.740 1.00 63.83  ? 1192 ARG B CA  1 
ATOM   9465  C C   . ARG A 1 1209 ? 180.221 168.126 216.017 1.00 63.83  ? 1192 ARG B C   1 
ATOM   9466  O O   . ARG A 1 1209 ? 180.438 167.557 214.942 1.00 63.83  ? 1192 ARG B O   1 
ATOM   9467  C CB  . ARG A 1 1209 ? 178.897 166.672 217.556 1.00 63.83  ? 1192 ARG B CB  1 
ATOM   9468  C CG  . ARG A 1 1209 ? 179.791 166.721 218.776 1.00 63.83  ? 1192 ARG B CG  1 
ATOM   9469  C CD  . ARG A 1 1209 ? 179.166 167.551 219.877 1.00 63.83  ? 1192 ARG B CD  1 
ATOM   9470  N NE  . ARG A 1 1209 ? 177.912 166.975 220.346 1.00 63.83  ? 1192 ARG B NE  1 
ATOM   9471  C CZ  . ARG A 1 1209 ? 177.019 167.623 221.080 1.00 63.83  ? 1192 ARG B CZ  1 
ATOM   9472  N NH1 . ARG A 1 1209 ? 177.202 168.883 221.436 1.00 63.83  ? 1192 ARG B NH1 1 
ATOM   9473  N NH2 . ARG A 1 1209 ? 175.915 166.991 221.466 1.00 63.83  ? 1192 ARG B NH2 1 
ATOM   9474  N N   . LEU A 1 1210 ? 181.111 168.909 216.623 1.00 56.07  ? 1193 LEU B N   1 
ATOM   9475  C CA  . LEU A 1 1210 ? 182.407 169.262 216.047 1.00 56.07  ? 1193 LEU B CA  1 
ATOM   9476  C C   . LEU A 1 1210 ? 183.436 168.219 216.460 1.00 56.07  ? 1193 LEU B C   1 
ATOM   9477  O O   . LEU A 1 1210 ? 184.028 168.311 217.537 1.00 56.07  ? 1193 LEU B O   1 
ATOM   9478  C CB  . LEU A 1 1210 ? 182.823 170.649 216.518 1.00 56.07  ? 1193 LEU B CB  1 
ATOM   9479  C CG  . LEU A 1 1210 ? 184.043 171.234 215.830 1.00 56.07  ? 1193 LEU B CG  1 
ATOM   9480  C CD1 . LEU A 1 1210 ? 183.677 171.560 214.416 1.00 56.07  ? 1193 LEU B CD1 1 
ATOM   9481  C CD2 . LEU A 1 1210 ? 184.524 172.467 216.558 1.00 56.07  ? 1193 LEU B CD2 1 
ATOM   9482  N N   . ALA A 1 1211 ? 183.675 167.234 215.601 1.00 54.61  ? 1194 ALA B N   1 
ATOM   9483  C CA  . ALA A 1 1211 ? 184.513 166.109 215.982 1.00 54.61  ? 1194 ALA B CA  1 
ATOM   9484  C C   . ALA A 1 1211 ? 185.479 165.773 214.860 1.00 54.61  ? 1194 ALA B C   1 
ATOM   9485  O O   . ALA A 1 1211 ? 185.373 166.282 213.743 1.00 54.61  ? 1194 ALA B O   1 
ATOM   9486  C CB  . ALA A 1 1211 ? 183.670 164.885 216.344 1.00 54.61  ? 1194 ALA B CB  1 
ATOM   9487  N N   . THR A 1 1212 ? 186.428 164.896 215.173 1.00 64.72  ? 1195 THR B N   1 
ATOM   9488  C CA  . THR A 1 1212 ? 187.427 164.467 214.206 1.00 64.72  ? 1195 THR B CA  1 
ATOM   9489  C C   . THR A 1 1212 ? 187.939 163.091 214.600 1.00 64.72  ? 1195 THR B C   1 
ATOM   9490  O O   . THR A 1 1212 ? 187.774 162.649 215.739 1.00 64.72  ? 1195 THR B O   1 
ATOM   9491  C CB  . THR A 1 1212 ? 188.584 165.466 214.116 1.00 64.72  ? 1195 THR B CB  1 
ATOM   9492  O OG1 . THR A 1 1212 ? 189.187 165.386 212.820 1.00 64.72  ? 1195 THR B OG1 1 
ATOM   9493  C CG2 . THR A 1 1212 ? 189.630 165.176 215.178 1.00 64.72  ? 1195 THR B CG2 1 
ATOM   9494  N N   . ASN A 1 1213 ? 188.554 162.416 213.636 1.00 73.27  ? 1196 ASN B N   1 
ATOM   9495  C CA  . ASN A 1 1213 ? 189.220 161.142 213.869 1.00 73.27  ? 1196 ASN B CA  1 
ATOM   9496  C C   . ASN A 1 1213 ? 190.720 161.392 213.927 1.00 73.27  ? 1196 ASN B C   1 
ATOM   9497  O O   . ASN A 1 1213 ? 191.302 161.902 212.965 1.00 73.27  ? 1196 ASN B O   1 
ATOM   9498  C CB  . ASN A 1 1213 ? 188.886 160.138 212.768 1.00 73.27  ? 1196 ASN B CB  1 
ATOM   9499  C CG  . ASN A 1 1213 ? 189.952 159.077 212.608 1.00 73.27  ? 1196 ASN B CG  1 
ATOM   9500  O OD1 . ASN A 1 1213 ? 190.834 159.189 211.759 1.00 73.27  ? 1196 ASN B OD1 1 
ATOM   9501  N ND2 . ASN A 1 1213 ? 189.877 158.038 213.428 1.00 73.27  ? 1196 ASN B ND2 1 
ATOM   9502  N N   . ALA A 1 1214 ? 191.344 161.025 215.040 1.00 74.77  ? 1197 ALA B N   1 
ATOM   9503  C CA  . ALA A 1 1214 ? 192.736 161.379 215.283 1.00 74.77  ? 1197 ALA B CA  1 
ATOM   9504  C C   . ALA A 1 1214 ? 193.726 160.355 214.747 1.00 74.77  ? 1197 ALA B C   1 
ATOM   9505  O O   . ALA A 1 1214 ? 194.933 160.527 214.939 1.00 74.77  ? 1197 ALA B O   1 
ATOM   9506  C CB  . ALA A 1 1214 ? 192.972 161.580 216.782 1.00 74.77  ? 1197 ALA B CB  1 
ATOM   9507  N N   . SER A 1 1215 ? 193.257 159.301 214.083 1.00 76.67  ? 1198 SER B N   1 
ATOM   9508  C CA  . SER A 1 1215 ? 194.146 158.255 213.599 1.00 76.67  ? 1198 SER B CA  1 
ATOM   9509  C C   . SER A 1 1215 ? 194.697 158.522 212.204 1.00 76.67  ? 1198 SER B C   1 
ATOM   9510  O O   . SER A 1 1215 ? 195.565 157.771 211.748 1.00 76.67  ? 1198 SER B O   1 
ATOM   9511  C CB  . SER A 1 1215 ? 193.424 156.905 213.611 1.00 76.67  ? 1198 SER B CB  1 
ATOM   9512  O OG  . SER A 1 1215 ? 192.969 156.586 214.914 1.00 76.67  ? 1198 SER B OG  1 
ATOM   9513  N N   . GLN A 1 1216 ? 194.224 159.561 211.522 1.00 73.21  ? 1199 GLN B N   1 
ATOM   9514  C CA  . GLN A 1 1216 ? 194.706 159.855 210.180 1.00 73.21  ? 1199 GLN B CA  1 
ATOM   9515  C C   . GLN A 1 1216 ? 196.169 160.277 210.217 1.00 73.21  ? 1199 GLN B C   1 
ATOM   9516  O O   . GLN A 1 1216 ? 196.639 160.892 211.178 1.00 73.21  ? 1199 GLN B O   1 
ATOM   9517  C CB  . GLN A 1 1216 ? 193.859 160.949 209.534 1.00 73.21  ? 1199 GLN B CB  1 
ATOM   9518  C CG  . GLN A 1 1216 ? 193.285 161.944 210.520 1.00 73.21  ? 1199 GLN B CG  1 
ATOM   9519  C CD  . GLN A 1 1216 ? 192.405 162.979 209.857 1.00 73.21  ? 1199 GLN B CD  1 
ATOM   9520  O OE1 . GLN A 1 1216 ? 191.765 162.706 208.843 1.00 73.21  ? 1199 GLN B OE1 1 
ATOM   9521  N NE2 . GLN A 1 1216 ? 192.360 164.172 210.430 1.00 73.21  ? 1199 GLN B NE2 1 
ATOM   9522  N N   . ALA A 1 1217 ? 196.891 159.939 209.152 1.00 82.99  ? 1200 ALA B N   1 
ATOM   9523  C CA  . ALA A 1 1217 ? 198.324 160.186 209.103 1.00 82.99  ? 1200 ALA B CA  1 
ATOM   9524  C C   . ALA A 1 1217 ? 198.624 161.681 209.095 1.00 82.99  ? 1200 ALA B C   1 
ATOM   9525  O O   . ALA A 1 1217 ? 197.814 162.501 208.653 1.00 82.99  ? 1200 ALA B O   1 
ATOM   9526  C CB  . ALA A 1 1217 ? 198.939 159.523 207.871 1.00 82.99  ? 1200 ALA B CB  1 
ATOM   9527  N N   . GLY A 1 1218 ? 199.801 162.030 209.597 1.00 80.67  ? 1201 GLY B N   1 
ATOM   9528  C CA  . GLY A 1 1218 ? 200.215 163.413 209.677 1.00 80.67  ? 1201 GLY B CA  1 
ATOM   9529  C C   . GLY A 1 1218 ? 199.796 164.070 210.980 1.00 80.67  ? 1201 GLY B C   1 
ATOM   9530  O O   . GLY A 1 1218 ? 198.865 163.643 211.661 1.00 80.67  ? 1201 GLY B O   1 
ATOM   9531  N N   . VAL A 1 1219 ? 200.517 165.137 211.329 1.00 81.85  ? 1202 VAL B N   1 
ATOM   9532  C CA  . VAL A 1 1219 ? 200.218 165.862 212.559 1.00 81.85  ? 1202 VAL B CA  1 
ATOM   9533  C C   . VAL A 1 1219 ? 198.860 166.545 212.458 1.00 81.85  ? 1202 VAL B C   1 
ATOM   9534  O O   . VAL A 1 1219 ? 198.123 166.642 213.447 1.00 81.85  ? 1202 VAL B O   1 
ATOM   9535  C CB  . VAL A 1 1219 ? 201.345 166.862 212.879 1.00 81.85  ? 1202 VAL B CB  1 
ATOM   9536  C CG1 . VAL A 1 1219 ? 201.582 167.806 211.710 1.00 81.85  ? 1202 VAL B CG1 1 
ATOM   9537  C CG2 . VAL A 1 1219 ? 201.032 167.639 214.149 1.00 81.85  ? 1202 VAL B CG2 1 
ATOM   9538  N N   . GLU A 1 1220 ? 198.502 167.016 211.267 1.00 80.88  ? 1203 GLU B N   1 
ATOM   9539  C CA  . GLU A 1 1220 ? 197.252 167.740 211.091 1.00 80.88  ? 1203 GLU B CA  1 
ATOM   9540  C C   . GLU A 1 1220 ? 196.063 166.799 211.224 1.00 80.88  ? 1203 GLU B C   1 
ATOM   9541  O O   . GLU A 1 1220 ? 196.039 165.720 210.626 1.00 80.88  ? 1203 GLU B O   1 
ATOM   9542  C CB  . GLU A 1 1220 ? 197.231 168.430 209.728 1.00 80.88  ? 1203 GLU B CB  1 
ATOM   9543  C CG  . GLU A 1 1220 ? 198.149 169.652 209.561 1.00 80.88  ? 1203 GLU B CG  1 
ATOM   9544  C CD  . GLU A 1 1220 ? 198.522 170.375 210.854 1.00 80.88  ? 1203 GLU B CD  1 
ATOM   9545  O OE1 . GLU A 1 1220 ? 197.687 170.489 211.775 1.00 80.88  ? 1203 GLU B OE1 1 
ATOM   9546  O OE2 . GLU A 1 1220 ? 199.679 170.834 210.947 1.00 80.88  ? 1203 GLU B OE2 1 
ATOM   9547  N N   . LYS A 1 1221 ? 195.073 167.217 212.007 1.00 78.50  ? 1204 LYS B N   1 
ATOM   9548  C CA  . LYS A 1 1221 ? 193.839 166.466 212.213 1.00 78.50  ? 1204 LYS B CA  1 
ATOM   9549  C C   . LYS A 1 1221 ? 192.687 167.355 211.759 1.00 78.50  ? 1204 LYS B C   1 
ATOM   9550  O O   . LYS A 1 1221 ? 192.228 168.216 212.513 1.00 78.50  ? 1204 LYS B O   1 
ATOM   9551  C CB  . LYS A 1 1221 ? 193.687 166.055 213.672 1.00 78.50  ? 1204 LYS B CB  1 
ATOM   9552  C CG  . LYS A 1 1221 ? 194.884 165.314 214.225 1.00 78.50  ? 1204 LYS B CG  1 
ATOM   9553  C CD  . LYS A 1 1221 ? 195.180 164.064 213.421 1.00 78.50  ? 1204 LYS B CD  1 
ATOM   9554  C CE  . LYS A 1 1221 ? 196.378 163.323 213.990 1.00 78.50  ? 1204 LYS B CE  1 
ATOM   9555  N NZ  . LYS A 1 1221 ? 196.509 161.956 213.417 1.00 78.50  ? 1204 LYS B NZ  1 
ATOM   9556  N N   . ILE A 1 1222 ? 192.223 167.148 210.527 1.00 68.18  ? 1205 ILE B N   1 
ATOM   9557  C CA  . ILE A 1 1222 ? 191.191 168.004 209.958 1.00 68.18  ? 1205 ILE B CA  1 
ATOM   9558  C C   . ILE A 1 1222 ? 189.884 167.805 210.713 1.00 68.18  ? 1205 ILE B C   1 
ATOM   9559  O O   . ILE A 1 1222 ? 189.457 166.670 210.961 1.00 68.18  ? 1205 ILE B O   1 
ATOM   9560  C CB  . ILE A 1 1222 ? 191.021 167.710 208.462 1.00 68.18  ? 1205 ILE B CB  1 
ATOM   9561  C CG1 . ILE A 1 1222 ? 192.373 167.773 207.758 1.00 68.18  ? 1205 ILE B CG1 1 
ATOM   9562  C CG2 . ILE A 1 1222 ? 190.056 168.691 207.835 1.00 68.18  ? 1205 ILE B CG2 1 
ATOM   9563  C CD1 . ILE A 1 1222 ? 192.394 167.052 206.436 1.00 68.18  ? 1205 ILE B CD1 1 
ATOM   9564  N N   . LEU A 1 1223 ? 189.245 168.910 211.085 1.00 60.20  ? 1206 LEU B N   1 
ATOM   9565  C CA  . LEU A 1 1223 ? 187.994 168.851 211.822 1.00 60.20  ? 1206 LEU B CA  1 
ATOM   9566  C C   . LEU A 1 1223 ? 186.827 168.563 210.885 1.00 60.20  ? 1206 LEU B C   1 
ATOM   9567  O O   . LEU A 1 1223 ? 186.893 168.792 209.676 1.00 60.20  ? 1206 LEU B O   1 
ATOM   9568  C CB  . LEU A 1 1223 ? 187.744 170.156 212.574 1.00 60.20  ? 1206 LEU B CB  1 
ATOM   9569  C CG  . LEU A 1 1223 ? 188.553 170.360 213.851 1.00 60.20  ? 1206 LEU B CG  1 
ATOM   9570  C CD1 . LEU A 1 1223 ? 187.816 171.282 214.783 1.00 60.20  ? 1206 LEU B CD1 1 
ATOM   9571  C CD2 . LEU A 1 1223 ? 188.823 169.042 214.528 1.00 60.20  ? 1206 LEU B CD2 1 
ATOM   9572  N N   . SER A 1 1224 ? 185.741 168.061 211.469 1.00 59.11  ? 1207 SER B N   1 
ATOM   9573  C CA  . SER A 1 1224 ? 184.557 167.695 210.708 1.00 59.11  ? 1207 SER B CA  1 
ATOM   9574  C C   . SER A 1 1224 ? 183.323 167.912 211.568 1.00 59.11  ? 1207 SER B C   1 
ATOM   9575  O O   . SER A 1 1224 ? 183.408 168.057 212.792 1.00 59.11  ? 1207 SER B O   1 
ATOM   9576  C CB  . SER A 1 1224 ? 184.621 166.240 210.233 1.00 59.11  ? 1207 SER B CB  1 
ATOM   9577  O OG  . SER A 1 1224 ? 185.719 166.036 209.364 1.00 59.11  ? 1207 SER B OG  1 
ATOM   9578  N N   . ALA A 1 1225 ? 182.172 167.938 210.909 1.00 58.35  ? 1208 ALA B N   1 
ATOM   9579  C CA  . ALA A 1 1225 ? 180.881 168.053 211.570 1.00 58.35  ? 1208 ALA B CA  1 
ATOM   9580  C C   . ALA A 1 1225 ? 180.105 166.760 211.370 1.00 58.35  ? 1208 ALA B C   1 
ATOM   9581  O O   . ALA A 1 1225 ? 179.921 166.316 210.233 1.00 58.35  ? 1208 ALA B O   1 
ATOM   9582  C CB  . ALA A 1 1225 ? 180.094 169.240 211.019 1.00 58.35  ? 1208 ALA B CB  1 
ATOM   9583  N N   . LEU A 1 1226 ? 179.657 166.155 212.468 1.00 62.14  ? 1209 LEU B N   1 
ATOM   9584  C CA  . LEU A 1 1226 ? 178.971 164.874 212.404 1.00 62.14  ? 1209 LEU B CA  1 
ATOM   9585  C C   . LEU A 1 1226 ? 177.630 164.957 213.113 1.00 62.14  ? 1209 LEU B C   1 
ATOM   9586  O O   . LEU A 1 1226 ? 177.477 165.688 214.091 1.00 62.14  ? 1209 LEU B O   1 
ATOM   9587  C CB  . LEU A 1 1226 ? 179.800 163.761 213.032 1.00 62.14  ? 1209 LEU B CB  1 
ATOM   9588  C CG  . LEU A 1 1226 ? 181.280 163.760 212.674 1.00 62.14  ? 1209 LEU B CG  1 
ATOM   9589  C CD1 . LEU A 1 1226 ? 182.081 163.068 213.752 1.00 62.14  ? 1209 LEU B CD1 1 
ATOM   9590  C CD2 . LEU A 1 1226 ? 181.487 163.091 211.337 1.00 62.14  ? 1209 LEU B CD2 1 
ATOM   9591  N N   . GLU A 1 1227 ? 176.663 164.187 212.618 1.00 71.51  ? 1210 GLU B N   1 
ATOM   9592  C CA  . GLU A 1 1227 ? 175.347 164.153 213.242 1.00 71.51  ? 1210 GLU B CA  1 
ATOM   9593  C C   . GLU A 1 1227 ? 175.470 163.728 214.698 1.00 71.51  ? 1210 GLU B C   1 
ATOM   9594  O O   . GLU A 1 1227 ? 176.197 162.789 215.024 1.00 71.51  ? 1210 GLU B O   1 
ATOM   9595  C CB  . GLU A 1 1227 ? 174.425 163.196 212.490 1.00 71.51  ? 1210 GLU B CB  1 
ATOM   9596  C CG  . GLU A 1 1227 ? 174.484 163.337 210.978 1.00 71.51  ? 1210 GLU B CG  1 
ATOM   9597  C CD  . GLU A 1 1227 ? 175.343 162.272 210.323 1.00 71.51  ? 1210 GLU B CD  1 
ATOM   9598  O OE1 . GLU A 1 1227 ? 176.204 161.689 211.015 1.00 71.51  ? 1210 GLU B OE1 1 
ATOM   9599  O OE2 . GLU A 1 1227 ? 175.156 162.016 209.115 1.00 71.51  ? 1210 GLU B OE2 1 
ATOM   9600  N N   . ILE A 1 1228 ? 174.746 164.423 215.571 1.00 69.79  ? 1211 ILE B N   1 
ATOM   9601  C CA  . ILE A 1 1228 ? 174.892 164.294 217.021 1.00 69.79  ? 1211 ILE B CA  1 
ATOM   9602  C C   . ILE A 1 1228 ? 174.802 162.834 217.460 1.00 69.79  ? 1211 ILE B C   1 
ATOM   9603  O O   . ILE A 1 1228 ? 175.556 162.427 218.355 1.00 69.79  ? 1211 ILE B O   1 
ATOM   9604  C CB  . ILE A 1 1228 ? 173.866 165.167 217.761 1.00 69.79  ? 1211 ILE B CB  1 
ATOM   9605  C CG1 . ILE A 1 1228 ? 173.856 166.577 217.173 1.00 69.79  ? 1211 ILE B CG1 1 
ATOM   9606  C CG2 . ILE A 1 1228 ? 174.189 165.222 219.237 1.00 69.79  ? 1211 ILE B CG2 1 
ATOM   9607  C CD1 . ILE A 1 1228 ? 172.854 167.497 217.819 1.00 69.79  ? 1211 ILE B CD1 1 
ATOM   9608  N N   . PRO A 1 1229 ? 173.909 162.005 216.891 1.00 75.32  ? 1212 PRO B N   1 
ATOM   9609  C CA  . PRO A 1 1229 ? 174.044 160.558 217.109 1.00 75.32  ? 1212 PRO B CA  1 
ATOM   9610  C C   . PRO A 1 1229 ? 175.221 159.973 216.342 1.00 75.32  ? 1212 PRO B C   1 
ATOM   9611  O O   . PRO A 1 1229 ? 175.036 159.132 215.456 1.00 75.32  ? 1212 PRO B O   1 
ATOM   9612  C CB  . PRO A 1 1229 ? 172.710 159.996 216.603 1.00 75.32  ? 1212 PRO B CB  1 
ATOM   9613  C CG  . PRO A 1 1229 ? 171.775 161.147 216.635 1.00 75.32  ? 1212 PRO B CG  1 
ATOM   9614  C CD  . PRO A 1 1229 ? 172.612 162.325 216.270 1.00 75.32  ? 1212 PRO B CD  1 
ATOM   9615  N N   . ASP A 1 1230 ? 176.433 160.415 216.673 1.00 74.21  ? 1213 ASP B N   1 
ATOM   9616  C CA  . ASP A 1 1230 ? 177.659 159.943 216.054 1.00 74.21  ? 1213 ASP B CA  1 
ATOM   9617  C C   . ASP A 1 1230 ? 178.282 158.845 216.908 1.00 74.21  ? 1213 ASP B C   1 
ATOM   9618  O O   . ASP A 1 1230 ? 177.674 158.335 217.854 1.00 74.21  ? 1213 ASP B O   1 
ATOM   9619  C CB  . ASP A 1 1230 ? 178.636 161.101 215.852 1.00 74.21  ? 1213 ASP B CB  1 
ATOM   9620  C CG  . ASP A 1 1230 ? 179.176 161.642 217.159 1.00 74.21  ? 1213 ASP B CG  1 
ATOM   9621  O OD1 . ASP A 1 1230 ? 178.371 162.123 217.980 1.00 74.21  ? 1213 ASP B OD1 1 
ATOM   9622  O OD2 . ASP A 1 1230 ? 180.404 161.589 217.368 1.00 74.21  ? 1213 ASP B OD2 1 
ATOM   9623  N N   . VAL A 1 1231 ? 179.511 158.475 216.572 1.00 82.50  ? 1214 VAL B N   1 
ATOM   9624  C CA  . VAL A 1 1231 ? 180.275 157.504 217.344 1.00 82.50  ? 1214 VAL B CA  1 
ATOM   9625  C C   . VAL A 1 1231 ? 181.087 158.248 218.394 1.00 82.50  ? 1214 VAL B C   1 
ATOM   9626  O O   . VAL A 1 1231 ? 181.853 159.163 218.068 1.00 82.50  ? 1214 VAL B O   1 
ATOM   9627  C CB  . VAL A 1 1231 ? 181.185 156.669 216.429 1.00 82.50  ? 1214 VAL B CB  1 
ATOM   9628  C CG1 . VAL A 1 1231 ? 182.020 155.704 217.253 1.00 82.50  ? 1214 VAL B CG1 1 
ATOM   9629  C CG2 . VAL A 1 1231 ? 180.355 155.923 215.398 1.00 82.50  ? 1214 VAL B CG2 1 
ATOM   9630  N N   . GLY A 1 1232 ? 180.923 157.857 219.656 1.00 84.02  ? 1215 GLY B N   1 
ATOM   9631  C CA  . GLY A 1 1232 ? 181.653 158.497 220.732 1.00 84.02  ? 1215 GLY B CA  1 
ATOM   9632  C C   . GLY A 1 1232 ? 183.146 158.256 220.707 1.00 84.02  ? 1215 GLY B C   1 
ATOM   9633  O O   . GLY A 1 1232 ? 183.875 158.921 221.450 1.00 84.02  ? 1215 GLY B O   1 
ATOM   9634  N N   . ASN A 1 1233 ? 183.617 157.324 219.876 1.00 86.13  ? 1216 ASN B N   1 
ATOM   9635  C CA  . ASN A 1 1233 ? 185.047 157.058 219.782 1.00 86.13  ? 1216 ASN B CA  1 
ATOM   9636  C C   . ASN A 1 1233 ? 185.821 158.232 219.197 1.00 86.13  ? 1216 ASN B C   1 
ATOM   9637  O O   . ASN A 1 1233 ? 187.036 158.316 219.397 1.00 86.13  ? 1216 ASN B O   1 
ATOM   9638  C CB  . ASN A 1 1233 ? 185.289 155.803 218.945 1.00 86.13  ? 1216 ASN B CB  1 
ATOM   9639  C CG  . ASN A 1 1233 ? 184.641 154.573 219.545 1.00 86.13  ? 1216 ASN B CG  1 
ATOM   9640  O OD1 . ASN A 1 1233 ? 184.203 153.673 218.828 1.00 86.13  ? 1216 ASN B OD1 1 
ATOM   9641  N ND2 . ASN A 1 1233 ? 184.574 154.529 220.871 1.00 86.13  ? 1216 ASN B ND2 1 
ATOM   9642  N N   . LEU A 1 1234 ? 185.154 159.131 218.483 1.00 75.32  ? 1217 LEU B N   1 
ATOM   9643  C CA  . LEU A 1 1234 ? 185.833 160.258 217.863 1.00 75.32  ? 1217 LEU B CA  1 
ATOM   9644  C C   . LEU A 1 1234 ? 186.054 161.376 218.874 1.00 75.32  ? 1217 LEU B C   1 
ATOM   9645  O O   . LEU A 1 1234 ? 185.179 161.680 219.689 1.00 75.32  ? 1217 LEU B O   1 
ATOM   9646  C CB  . LEU A 1 1234 ? 185.027 160.767 216.669 1.00 75.32  ? 1217 LEU B CB  1 
ATOM   9647  C CG  . LEU A 1 1234 ? 184.744 159.691 215.616 1.00 75.32  ? 1217 LEU B CG  1 
ATOM   9648  C CD1 . LEU A 1 1234 ? 183.485 159.995 214.826 1.00 75.32  ? 1217 LEU B CD1 1 
ATOM   9649  C CD2 . LEU A 1 1234 ? 185.930 159.522 214.686 1.00 75.32  ? 1217 LEU B CD2 1 
ATOM   9650  N N   . SER A 1 1235 ? 187.236 161.985 218.813 1.00 75.25  ? 1218 SER B N   1 
ATOM   9651  C CA  . SER A 1 1235 ? 187.607 163.034 219.755 1.00 75.25  ? 1218 SER B CA  1 
ATOM   9652  C C   . SER A 1 1235 ? 186.724 164.255 219.548 1.00 75.25  ? 1218 SER B C   1 
ATOM   9653  O O   . SER A 1 1235 ? 186.707 164.837 218.460 1.00 75.25  ? 1218 SER B O   1 
ATOM   9654  C CB  . SER A 1 1235 ? 189.075 163.404 219.574 1.00 75.25  ? 1218 SER B CB  1 
ATOM   9655  O OG  . SER A 1 1235 ? 189.896 162.252 219.618 1.00 75.25  ? 1218 SER B OG  1 
ATOM   9656  N N   . GLN A 1 1236 ? 185.992 164.646 220.587 1.00 68.46  ? 1219 GLN B N   1 
ATOM   9657  C CA  . GLN A 1 1236 ? 185.078 165.773 220.486 1.00 68.46  ? 1219 GLN B CA  1 
ATOM   9658  C C   . GLN A 1 1236 ? 185.142 166.750 221.648 1.00 68.46  ? 1219 GLN B C   1 
ATOM   9659  O O   . GLN A 1 1236 ? 184.756 167.910 221.464 1.00 68.46  ? 1219 GLN B O   1 
ATOM   9660  C CB  . GLN A 1 1236 ? 183.634 165.272 220.344 1.00 68.46  ? 1219 GLN B CB  1 
ATOM   9661  C CG  . GLN A 1 1236 ? 183.347 164.003 221.122 1.00 68.46  ? 1219 GLN B CG  1 
ATOM   9662  C CD  . GLN A 1 1236 ? 181.893 163.589 221.043 1.00 68.46  ? 1219 GLN B CD  1 
ATOM   9663  O OE1 . GLN A 1 1236 ? 181.090 164.226 220.361 1.00 68.46  ? 1219 GLN B OE1 1 
ATOM   9664  N NE2 . GLN A 1 1236 ? 181.544 162.518 221.746 1.00 68.46  ? 1219 GLN B NE2 1 
ATOM   9665  N N   . VAL A 1 1237 ? 185.613 166.340 222.825 1.00 73.17  ? 1220 VAL B N   1 
ATOM   9666  C CA  . VAL A 1 1237 ? 185.597 167.222 223.985 1.00 73.17  ? 1220 VAL B CA  1 
ATOM   9667  C C   . VAL A 1 1237 ? 186.650 168.307 223.819 1.00 73.17  ? 1220 VAL B C   1 
ATOM   9668  O O   . VAL A 1 1237 ? 187.820 168.025 223.532 1.00 73.17  ? 1220 VAL B O   1 
ATOM   9669  C CB  . VAL A 1 1237 ? 185.806 166.420 225.277 1.00 73.17  ? 1220 VAL B CB  1 
ATOM   9670  C CG1 . VAL A 1 1237 ? 187.059 165.567 225.188 1.00 73.17  ? 1220 VAL B CG1 1 
ATOM   9671  C CG2 . VAL A 1 1237 ? 185.892 167.358 226.464 1.00 73.17  ? 1220 VAL B CG2 1 
ATOM   9672  N N   . VAL A 1 1238 ? 186.238 169.558 223.996 1.00 74.53  ? 1221 VAL B N   1 
ATOM   9673  C CA  . VAL A 1 1238 ? 187.096 170.715 223.771 1.00 74.53  ? 1221 VAL B CA  1 
ATOM   9674  C C   . VAL A 1 1238 ? 187.280 171.438 225.093 1.00 74.53  ? 1221 VAL B C   1 
ATOM   9675  O O   . VAL A 1 1238 ? 186.296 171.810 225.738 1.00 74.53  ? 1221 VAL B O   1 
ATOM   9676  C CB  . VAL A 1 1238 ? 186.497 171.672 222.725 1.00 74.53  ? 1221 VAL B CB  1 
ATOM   9677  C CG1 . VAL A 1 1238 ? 187.415 172.843 222.509 1.00 74.53  ? 1221 VAL B CG1 1 
ATOM   9678  C CG2 . VAL A 1 1238 ? 186.237 170.951 221.426 1.00 74.53  ? 1221 VAL B CG2 1 
ATOM   9679  N N   . VAL A 1 1239 ? 188.527 171.653 225.492 1.00 76.90  ? 1222 VAL B N   1 
ATOM   9680  C CA  . VAL A 1 1239 ? 188.820 172.432 226.686 1.00 76.90  ? 1222 VAL B CA  1 
ATOM   9681  C C   . VAL A 1 1239 ? 189.123 173.862 226.258 1.00 76.90  ? 1222 VAL B C   1 
ATOM   9682  O O   . VAL A 1 1239 ? 189.986 174.102 225.405 1.00 76.90  ? 1222 VAL B O   1 
ATOM   9683  C CB  . VAL A 1 1239 ? 189.965 171.814 227.504 1.00 76.90  ? 1222 VAL B CB  1 
ATOM   9684  C CG1 . VAL A 1 1239 ? 191.199 171.616 226.663 1.00 76.90  ? 1222 VAL B CG1 1 
ATOM   9685  C CG2 . VAL A 1 1239 ? 190.278 172.686 228.703 1.00 76.90  ? 1222 VAL B CG2 1 
ATOM   9686  N N   . MET A 1 1240 ? 188.374 174.805 226.815 1.00 80.24  ? 1223 MET B N   1 
ATOM   9687  C CA  . MET A 1 1240 ? 188.515 176.214 226.491 1.00 80.24  ? 1223 MET B CA  1 
ATOM   9688  C C   . MET A 1 1240 ? 189.455 176.871 227.488 1.00 80.24  ? 1223 MET B C   1 
ATOM   9689  O O   . MET A 1 1240 ? 189.326 176.662 228.702 1.00 80.24  ? 1223 MET B O   1 
ATOM   9690  C CB  . MET A 1 1240 ? 187.156 176.911 226.512 1.00 80.24  ? 1223 MET B CB  1 
ATOM   9691  C CG  . MET A 1 1240 ? 186.089 176.217 225.692 1.00 80.24  ? 1223 MET B CG  1 
ATOM   9692  S SD  . MET A 1 1240 ? 186.045 176.800 223.990 1.00 80.24  ? 1223 MET B SD  1 
ATOM   9693  C CE  . MET A 1 1240 ? 185.938 178.566 224.251 1.00 80.24  ? 1223 MET B CE  1 
ATOM   9694  N N   . LYS A 1 1241 ? 190.401 177.658 226.969 1.00 80.18  ? 1224 LYS B N   1 
ATOM   9695  C CA  . LYS A 1 1241 ? 191.383 178.361 227.777 1.00 80.18  ? 1224 LYS B CA  1 
ATOM   9696  C C   . LYS A 1 1241 ? 191.436 179.824 227.366 1.00 80.18  ? 1224 LYS B C   1 
ATOM   9697  O O   . LYS A 1 1241 ? 191.195 180.172 226.205 1.00 80.18  ? 1224 LYS B O   1 
ATOM   9698  C CB  . LYS A 1 1241 ? 192.782 177.750 227.638 1.00 80.18  ? 1224 LYS B CB  1 
ATOM   9699  C CG  . LYS A 1 1241 ? 192.800 176.248 227.461 1.00 80.18  ? 1224 LYS B CG  1 
ATOM   9700  C CD  . LYS A 1 1241 ? 194.200 175.756 227.158 1.00 80.18  ? 1224 LYS B CD  1 
ATOM   9701  C CE  . LYS A 1 1241 ? 194.939 175.406 228.435 1.00 80.18  ? 1224 LYS B CE  1 
ATOM   9702  N NZ  . LYS A 1 1241 ? 194.420 174.152 229.043 1.00 80.18  ? 1224 LYS B NZ  1 
ATOM   9703  N N   . SER A 1 1242 ? 191.765 180.679 228.335 1.00 85.66  ? 1225 SER B N   1 
ATOM   9704  C CA  . SER A 1 1242 ? 191.939 182.103 228.091 1.00 85.66  ? 1225 SER B CA  1 
ATOM   9705  C C   . SER A 1 1242 ? 193.212 182.651 228.724 1.00 85.66  ? 1225 SER B C   1 
ATOM   9706  O O   . SER A 1 1242 ? 193.418 183.870 228.713 1.00 85.66  ? 1225 SER B O   1 
ATOM   9707  C CB  . SER A 1 1242 ? 190.729 182.890 228.606 1.00 85.66  ? 1225 SER B CB  1 
ATOM   9708  O OG  . SER A 1 1242 ? 191.068 184.247 228.825 1.00 85.66  ? 1225 SER B OG  1 
ATOM   9709  N N   . LYS A 1 1243 ? 194.065 181.792 229.277 1.00 92.88  ? 1226 LYS B N   1 
ATOM   9710  C CA  . LYS A 1 1243 ? 195.310 182.211 229.904 1.00 92.88  ? 1226 LYS B CA  1 
ATOM   9711  C C   . LYS A 1 1243 ? 196.440 181.293 229.464 1.00 92.88  ? 1226 LYS B C   1 
ATOM   9712  O O   . LYS A 1 1243 ? 196.216 180.138 229.094 1.00 92.88  ? 1226 LYS B O   1 
ATOM   9713  C CB  . LYS A 1 1243 ? 195.203 182.203 231.434 1.00 92.88  ? 1226 LYS B CB  1 
ATOM   9714  C CG  . LYS A 1 1243 ? 194.240 183.232 231.997 1.00 92.88  ? 1226 LYS B CG  1 
ATOM   9715  C CD  . LYS A 1 1243 ? 194.552 183.545 233.451 1.00 92.88  ? 1226 LYS B CD  1 
ATOM   9716  C CE  . LYS A 1 1243 ? 194.757 182.277 234.263 1.00 92.88  ? 1226 LYS B CE  1 
ATOM   9717  N NZ  . LYS A 1 1243 ? 193.495 181.817 234.901 1.00 92.88  ? 1226 LYS B NZ  1 
ATOM   9718  N N   . ASN A 1 1244 ? 197.660 181.819 229.512 1.00 98.08  ? 1227 ASN B N   1 
ATOM   9719  C CA  . ASN A 1 1244 ? 198.840 181.048 229.136 1.00 98.08  ? 1227 ASN B CA  1 
ATOM   9720  C C   . ASN A 1 1244 ? 199.426 180.319 230.339 1.00 98.08  ? 1227 ASN B C   1 
ATOM   9721  O O   . ASN A 1 1244 ? 198.947 180.472 231.463 1.00 98.08  ? 1227 ASN B O   1 
ATOM   9722  C CB  . ASN A 1 1244 ? 199.898 181.956 228.508 1.00 98.08  ? 1227 ASN B CB  1 
ATOM   9723  C CG  . ASN A 1 1244 ? 199.623 182.247 227.046 1.00 98.08  ? 1227 ASN B CG  1 
ATOM   9724  O OD1 . ASN A 1 1244 ? 198.519 182.016 226.553 1.00 98.08  ? 1227 ASN B OD1 1 
ATOM   9725  N ND2 . ASN A 1 1244 ? 200.629 182.756 226.344 1.00 98.08  ? 1227 ASN B ND2 1 
ATOM   9726  N N   . ILE A 1 1248 ? 199.387 185.952 231.709 1.00 103.50 ? 1231 ILE B N   1 
ATOM   9727  C CA  . ILE A 1 1248 ? 199.211 186.578 230.405 1.00 103.50 ? 1231 ILE B CA  1 
ATOM   9728  C C   . ILE A 1 1248 ? 198.069 185.891 229.661 1.00 103.50 ? 1231 ILE B C   1 
ATOM   9729  O O   . ILE A 1 1248 ? 198.000 184.663 229.606 1.00 103.50 ? 1231 ILE B O   1 
ATOM   9730  C CB  . ILE A 1 1248 ? 200.521 186.544 229.593 1.00 103.50 ? 1231 ILE B CB  1 
ATOM   9731  C CG1 . ILE A 1 1248 ? 200.271 186.943 228.136 1.00 103.50 ? 1231 ILE B CG1 1 
ATOM   9732  C CG2 . ILE A 1 1248 ? 201.175 185.174 229.683 1.00 103.50 ? 1231 ILE B CG2 1 
ATOM   9733  C CD1 . ILE A 1 1248 ? 199.843 188.385 227.962 1.00 103.50 ? 1231 ILE B CD1 1 
ATOM   9734  N N   . THR A 1 1249 ? 197.171 186.692 229.096 1.00 97.74  ? 1232 THR B N   1 
ATOM   9735  C CA  . THR A 1 1249 ? 195.969 186.200 228.438 1.00 97.74  ? 1232 THR B CA  1 
ATOM   9736  C C   . THR A 1 1249 ? 196.084 186.404 226.934 1.00 97.74  ? 1232 THR B C   1 
ATOM   9737  O O   . THR A 1 1249 ? 196.476 187.483 226.479 1.00 97.74  ? 1232 THR B O   1 
ATOM   9738  C CB  . THR A 1 1249 ? 194.728 186.918 228.967 1.00 97.74  ? 1232 THR B CB  1 
ATOM   9739  O OG1 . THR A 1 1249 ? 194.801 188.308 228.627 1.00 97.74  ? 1232 THR B OG1 1 
ATOM   9740  C CG2 . THR A 1 1249 ? 194.660 186.786 230.470 1.00 97.74  ? 1232 THR B CG2 1 
ATOM   9741  N N   . ASN A 1 1250 ? 195.740 185.368 226.168 1.00 91.03  ? 1233 ASN B N   1 
ATOM   9742  C CA  . ASN A 1 1250 ? 195.777 185.416 224.706 1.00 91.03  ? 1233 ASN B CA  1 
ATOM   9743  C C   . ASN A 1 1250 ? 194.405 185.013 224.176 1.00 91.03  ? 1233 ASN B C   1 
ATOM   9744  O O   . ASN A 1 1250 ? 194.182 183.845 223.847 1.00 91.03  ? 1233 ASN B O   1 
ATOM   9745  C CB  . ASN A 1 1250 ? 196.879 184.517 224.158 1.00 91.03  ? 1233 ASN B CB  1 
ATOM   9746  C CG  . ASN A 1 1250 ? 196.927 184.514 222.643 1.00 91.03  ? 1233 ASN B CG  1 
ATOM   9747  O OD1 . ASN A 1 1250 ? 197.052 185.564 222.013 1.00 91.03  ? 1233 ASN B OD1 1 
ATOM   9748  N ND2 . ASN A 1 1250 ? 196.826 183.331 222.049 1.00 91.03  ? 1233 ASN B ND2 1 
ATOM   9749  N N   . LYS A 1 1251 ? 193.500 185.990 224.085 1.00 83.81  ? 1234 LYS B N   1 
ATOM   9750  C CA  . LYS A 1 1251 ? 192.170 185.808 223.509 1.00 83.81  ? 1234 LYS B CA  1 
ATOM   9751  C C   . LYS A 1 1251 ? 191.448 184.593 224.076 1.00 83.81  ? 1234 LYS B C   1 
ATOM   9752  O O   . LYS A 1 1251 ? 191.503 184.337 225.282 1.00 83.81  ? 1234 LYS B O   1 
ATOM   9753  C CB  . LYS A 1 1251 ? 192.263 185.700 221.985 1.00 83.81  ? 1234 LYS B CB  1 
ATOM   9754  C CG  . LYS A 1 1251 ? 192.992 186.860 221.327 1.00 83.81  ? 1234 LYS B CG  1 
ATOM   9755  C CD  . LYS A 1 1251 ? 192.433 188.202 221.780 1.00 83.81  ? 1234 LYS B CD  1 
ATOM   9756  C CE  . LYS A 1 1251 ? 190.976 188.365 221.382 1.00 83.81  ? 1234 LYS B CE  1 
ATOM   9757  N NZ  . LYS A 1 1251 ? 190.350 189.542 222.042 1.00 83.81  ? 1234 LYS B NZ  1 
ATOM   9758  N N   . CYS A 1 1252 ? 190.766 183.844 223.212 1.00 79.76  ? 1235 CYS B N   1 
ATOM   9759  C CA  . CYS A 1 1252 ? 190.008 182.664 223.611 1.00 79.76  ? 1235 CYS B CA  1 
ATOM   9760  C C   . CYS A 1 1252 ? 190.402 181.508 222.710 1.00 79.76  ? 1235 CYS B C   1 
ATOM   9761  O O   . CYS A 1 1252 ? 190.145 181.546 221.503 1.00 79.76  ? 1235 CYS B O   1 
ATOM   9762  C CB  . CYS A 1 1252 ? 188.503 182.924 223.525 1.00 79.76  ? 1235 CYS B CB  1 
ATOM   9763  S SG  . CYS A 1 1252 ? 188.009 184.533 224.162 1.00 79.76  ? 1235 CYS B SG  1 
ATOM   9764  N N   . LYS A 1 1253 ? 191.015 180.481 223.288 1.00 80.18  ? 1236 LYS B N   1 
ATOM   9765  C CA  . LYS A 1 1253 ? 191.534 179.367 222.513 1.00 80.18  ? 1236 LYS B CA  1 
ATOM   9766  C C   . LYS A 1 1253 ? 190.833 178.073 222.897 1.00 80.18  ? 1236 LYS B C   1 
ATOM   9767  O O   . LYS A 1 1253 ? 190.438 177.874 224.051 1.00 80.18  ? 1236 LYS B O   1 
ATOM   9768  C CB  . LYS A 1 1253 ? 193.046 179.221 222.702 1.00 80.18  ? 1236 LYS B CB  1 
ATOM   9769  C CG  . LYS A 1 1253 ? 193.812 180.507 222.471 1.00 80.18  ? 1236 LYS B CG  1 
ATOM   9770  C CD  . LYS A 1 1253 ? 195.308 180.281 222.525 1.00 80.18  ? 1236 LYS B CD  1 
ATOM   9771  C CE  . LYS A 1 1253 ? 195.773 180.067 223.952 1.00 80.18  ? 1236 LYS B CE  1 
ATOM   9772  N NZ  . LYS A 1 1253 ? 195.805 181.347 224.713 1.00 80.18  ? 1236 LYS B NZ  1 
ATOM   9773  N N   . MET A 1 1254 ? 190.684 177.195 221.911 1.00 79.83  ? 1237 MET B N   1 
ATOM   9774  C CA  . MET A 1 1254 ? 190.066 175.893 222.091 1.00 79.83  ? 1237 MET B CA  1 
ATOM   9775  C C   . MET A 1 1254 ? 191.120 174.816 221.898 1.00 79.83  ? 1237 MET B C   1 
ATOM   9776  O O   . MET A 1 1254 ? 191.955 174.912 220.995 1.00 79.83  ? 1237 MET B O   1 
ATOM   9777  C CB  . MET A 1 1254 ? 188.928 175.669 221.098 1.00 79.83  ? 1237 MET B CB  1 
ATOM   9778  C CG  . MET A 1 1254 ? 188.101 176.892 220.784 1.00 79.83  ? 1237 MET B CG  1 
ATOM   9779  S SD  . MET A 1 1254 ? 187.276 176.701 219.195 1.00 79.83  ? 1237 MET B SD  1 
ATOM   9780  C CE  . MET A 1 1254 ? 186.584 178.330 218.970 1.00 79.83  ? 1237 MET B CE  1 
ATOM   9781  N N   . ASN A 1 1255 ? 191.074 173.784 222.734 1.00 82.60  ? 1238 ASN B N   1 
ATOM   9782  C CA  . ASN A 1 1255 ? 192.033 172.688 222.672 1.00 82.60  ? 1238 ASN B CA  1 
ATOM   9783  C C   . ASN A 1 1255 ? 191.252 171.384 222.583 1.00 82.60  ? 1238 ASN B C   1 
ATOM   9784  O O   . ASN A 1 1255 ? 190.580 170.992 223.542 1.00 82.60  ? 1238 ASN B O   1 
ATOM   9785  C CB  . ASN A 1 1255 ? 192.952 172.710 223.893 1.00 82.60  ? 1238 ASN B CB  1 
ATOM   9786  C CG  . ASN A 1 1255 ? 193.998 171.617 223.868 1.00 82.60  ? 1238 ASN B CG  1 
ATOM   9787  O OD1 . ASN A 1 1255 ? 194.072 170.824 222.930 1.00 82.60  ? 1238 ASN B OD1 1 
ATOM   9788  N ND2 . ASN A 1 1255 ? 194.820 171.572 224.909 1.00 82.60  ? 1238 ASN B ND2 1 
ATOM   9789  N N   . LEU A 1 1256 ? 191.319 170.734 221.425 1.00 79.06  ? 1239 LEU B N   1 
ATOM   9790  C CA  . LEU A 1 1256 ? 190.722 169.419 221.259 1.00 79.06  ? 1239 LEU B CA  1 
ATOM   9791  C C   . LEU A 1 1256 ? 191.496 168.397 222.074 1.00 79.06  ? 1239 LEU B C   1 
ATOM   9792  O O   . LEU A 1 1256 ? 192.729 168.329 221.993 1.00 79.06  ? 1239 LEU B O   1 
ATOM   9793  C CB  . LEU A 1 1256 ? 190.730 169.015 219.788 1.00 79.06  ? 1239 LEU B CB  1 
ATOM   9794  C CG  . LEU A 1 1256 ? 189.601 168.108 219.313 1.00 79.06  ? 1239 LEU B CG  1 
ATOM   9795  C CD1 . LEU A 1 1256 ? 188.272 168.751 219.592 1.00 79.06  ? 1239 LEU B CD1 1 
ATOM   9796  C CD2 . LEU A 1 1256 ? 189.746 167.784 217.842 1.00 79.06  ? 1239 LEU B CD2 1 
ATOM   9797  N N   . GLN A 1 1257 ? 190.767 167.593 222.844 1.00 84.57  ? 1240 GLN B N   1 
ATOM   9798  C CA  . GLN A 1 1257 ? 191.338 166.534 223.658 1.00 84.57  ? 1240 GLN B CA  1 
ATOM   9799  C C   . GLN A 1 1257 ? 190.753 165.193 223.245 1.00 84.57  ? 1240 GLN B C   1 
ATOM   9800  O O   . GLN A 1 1257 ? 189.589 165.101 222.846 1.00 84.57  ? 1240 GLN B O   1 
ATOM   9801  C CB  . GLN A 1 1257 ? 191.070 166.760 225.148 1.00 84.57  ? 1240 GLN B CB  1 
ATOM   9802  C CG  . GLN A 1 1257 ? 191.798 167.943 225.746 1.00 84.57  ? 1240 GLN B CG  1 
ATOM   9803  C CD  . GLN A 1 1257 ? 191.844 167.882 227.257 1.00 84.57  ? 1240 GLN B CD  1 
ATOM   9804  O OE1 . GLN A 1 1257 ? 190.916 167.391 227.898 1.00 84.57  ? 1240 GLN B OE1 1 
ATOM   9805  N NE2 . GLN A 1 1257 ? 192.929 168.380 227.836 1.00 84.57  ? 1240 GLN B NE2 1 
ATOM   9806  N N   . ASP A 1 1258 ? 191.570 164.151 223.345 1.00 97.74  ? 1241 ASP B N   1 
ATOM   9807  C CA  . ASP A 1 1258 ? 191.076 162.806 223.117 1.00 97.74  ? 1241 ASP B CA  1 
ATOM   9808  C C   . ASP A 1 1258 ? 190.200 162.369 224.290 1.00 97.74  ? 1241 ASP B C   1 
ATOM   9809  O O   . ASP A 1 1258 ? 190.149 163.014 225.340 1.00 97.74  ? 1241 ASP B O   1 
ATOM   9810  C CB  . ASP A 1 1258 ? 192.241 161.836 222.917 1.00 97.74  ? 1241 ASP B CB  1 
ATOM   9811  C CG  . ASP A 1 1258 ? 191.835 160.579 222.168 1.00 97.74  ? 1241 ASP B CG  1 
ATOM   9812  O OD1 . ASP A 1 1258 ? 190.624 160.276 222.119 1.00 97.74  ? 1241 ASP B OD1 1 
ATOM   9813  O OD2 . ASP A 1 1258 ? 192.727 159.894 221.626 1.00 97.74  ? 1241 ASP B OD2 1 
ATOM   9814  N N   . ASN A 1 1259 ? 189.492 161.256 224.097 1.00 100.27 ? 1242 ASN B N   1 
ATOM   9815  C CA  . ASN A 1 1259 ? 188.647 160.730 225.161 1.00 100.27 ? 1242 ASN B CA  1 
ATOM   9816  C C   . ASN A 1 1259 ? 189.455 160.196 226.337 1.00 100.27 ? 1242 ASN B C   1 
ATOM   9817  O O   . ASN A 1 1259 ? 188.905 160.051 227.433 1.00 100.27 ? 1242 ASN B O   1 
ATOM   9818  C CB  . ASN A 1 1259 ? 187.738 159.631 224.611 1.00 100.27 ? 1242 ASN B CB  1 
ATOM   9819  C CG  . ASN A 1 1259 ? 186.560 160.183 223.839 1.00 100.27 ? 1242 ASN B CG  1 
ATOM   9820  O OD1 . ASN A 1 1259 ? 186.125 161.310 224.073 1.00 100.27 ? 1242 ASN B OD1 1 
ATOM   9821  N ND2 . ASN A 1 1259 ? 186.033 159.392 222.913 1.00 100.27 ? 1242 ASN B ND2 1 
ATOM   9822  N N   . ASN A 1 1260 ? 190.740 159.908 226.139 1.00 108.62 ? 1243 ASN B N   1 
ATOM   9823  C CA  . ASN A 1 1260 ? 191.589 159.339 227.177 1.00 108.62 ? 1243 ASN B CA  1 
ATOM   9824  C C   . ASN A 1 1260 ? 192.435 160.385 227.890 1.00 108.62 ? 1243 ASN B C   1 
ATOM   9825  O O   . ASN A 1 1260 ? 193.304 160.023 228.690 1.00 108.62 ? 1243 ASN B O   1 
ATOM   9826  C CB  . ASN A 1 1260 ? 192.493 158.258 226.582 1.00 108.62 ? 1243 ASN B CB  1 
ATOM   9827  C CG  . ASN A 1 1260 ? 191.710 157.119 225.966 1.00 108.62 ? 1243 ASN B CG  1 
ATOM   9828  O OD1 . ASN A 1 1260 ? 190.726 156.648 226.535 1.00 108.62 ? 1243 ASN B OD1 1 
ATOM   9829  N ND2 . ASN A 1 1260 ? 192.145 156.668 224.796 1.00 108.62 ? 1243 ASN B ND2 1 
ATOM   9830  N N   . GLY A 1 1261 ? 192.207 161.667 227.621 1.00 106.96 ? 1244 GLY B N   1 
ATOM   9831  C CA  . GLY A 1 1261 ? 192.963 162.727 228.247 1.00 106.96 ? 1244 GLY B CA  1 
ATOM   9832  C C   . GLY A 1 1261 ? 194.163 163.211 227.464 1.00 106.96 ? 1244 GLY B C   1 
ATOM   9833  O O   . GLY A 1 1261 ? 194.732 164.253 227.816 1.00 106.96 ? 1244 GLY B O   1 
ATOM   9834  N N   . ASN A 1 1262 ? 194.569 162.495 226.419 1.00 101.56 ? 1245 ASN B N   1 
ATOM   9835  C CA  . ASN A 1 1262 ? 195.652 162.970 225.571 1.00 101.56 ? 1245 ASN B CA  1 
ATOM   9836  C C   . ASN A 1 1262 ? 195.213 164.210 224.804 1.00 101.56 ? 1245 ASN B C   1 
ATOM   9837  O O   . ASN A 1 1262 ? 194.060 164.322 224.377 1.00 101.56 ? 1245 ASN B O   1 
ATOM   9838  C CB  . ASN A 1 1262 ? 196.094 161.876 224.601 1.00 101.56 ? 1245 ASN B CB  1 
ATOM   9839  C CG  . ASN A 1 1262 ? 196.425 160.576 225.302 1.00 101.56 ? 1245 ASN B CG  1 
ATOM   9840  O OD1 . ASN A 1 1262 ? 196.090 159.495 224.822 1.00 101.56 ? 1245 ASN B OD1 1 
ATOM   9841  N ND2 . ASN A 1 1262 ? 197.085 160.676 226.450 1.00 101.56 ? 1245 ASN B ND2 1 
ATOM   9842  N N   . ASP A 1 1263 ? 196.140 165.145 224.630 1.00 91.40  ? 1246 ASP B N   1 
ATOM   9843  C CA  . ASP A 1 1263 ? 195.849 166.420 223.986 1.00 91.40  ? 1246 ASP B CA  1 
ATOM   9844  C C   . ASP A 1 1263 ? 196.005 166.266 222.480 1.00 91.40  ? 1246 ASP B C   1 
ATOM   9845  O O   . ASP A 1 1263 ? 197.123 166.111 221.979 1.00 91.40  ? 1246 ASP B O   1 
ATOM   9846  C CB  . ASP A 1 1263 ? 196.772 167.511 224.520 1.00 91.40  ? 1246 ASP B CB  1 
ATOM   9847  C CG  . ASP A 1 1263 ? 196.049 168.816 224.760 1.00 91.40  ? 1246 ASP B CG  1 
ATOM   9848  O OD1 . ASP A 1 1263 ? 194.802 168.806 224.799 1.00 91.40  ? 1246 ASP B OD1 1 
ATOM   9849  O OD2 . ASP A 1 1263 ? 196.724 169.856 224.909 1.00 91.40  ? 1246 ASP B OD2 1 
ATOM   9850  N N   . ILE A 1 1264 ? 194.885 166.301 221.756 1.00 84.68  ? 1247 ILE B N   1 
ATOM   9851  C CA  . ILE A 1 1264 ? 194.959 166.336 220.299 1.00 84.68  ? 1247 ILE B CA  1 
ATOM   9852  C C   . ILE A 1 1264 ? 195.600 167.634 219.834 1.00 84.68  ? 1247 ILE B C   1 
ATOM   9853  O O   . ILE A 1 1264 ? 196.442 167.638 218.928 1.00 84.68  ? 1247 ILE B O   1 
ATOM   9854  C CB  . ILE A 1 1264 ? 193.566 166.136 219.680 1.00 84.68  ? 1247 ILE B CB  1 
ATOM   9855  C CG1 . ILE A 1 1264 ? 193.025 164.755 220.038 1.00 84.68  ? 1247 ILE B CG1 1 
ATOM   9856  C CG2 . ILE A 1 1264 ? 193.632 166.289 218.178 1.00 84.68  ? 1247 ILE B CG2 1 
ATOM   9857  C CD1 . ILE A 1 1264 ? 193.924 163.631 219.592 1.00 84.68  ? 1247 ILE B CD1 1 
ATOM   9858  N N   . GLY A 1 1265 ? 195.222 168.753 220.444 1.00 84.20  ? 1248 GLY B N   1 
ATOM   9859  C CA  . GLY A 1 1265 ? 195.922 169.994 220.170 1.00 84.20  ? 1248 GLY B CA  1 
ATOM   9860  C C   . GLY A 1 1265 ? 195.028 171.202 220.009 1.00 84.20  ? 1248 GLY B C   1 
ATOM   9861  O O   . GLY A 1 1265 ? 193.805 171.090 220.080 1.00 84.20  ? 1248 GLY B O   1 
ATOM   9862  N N   . PHE A 1 1266 ? 195.625 172.366 219.779 1.00 81.78  ? 1249 PHE B N   1 
ATOM   9863  C CA  . PHE A 1 1266 ? 194.832 173.580 219.664 1.00 81.78  ? 1249 PHE B CA  1 
ATOM   9864  C C   . PHE A 1 1266 ? 194.091 173.608 218.336 1.00 81.78  ? 1249 PHE B C   1 
ATOM   9865  O O   . PHE A 1 1266 ? 194.609 173.171 217.305 1.00 81.78  ? 1249 PHE B O   1 
ATOM   9866  C CB  . PHE A 1 1266 ? 195.720 174.815 219.790 1.00 81.78  ? 1249 PHE B CB  1 
ATOM   9867  C CG  . PHE A 1 1266 ? 195.955 175.250 221.204 1.00 81.78  ? 1249 PHE B CG  1 
ATOM   9868  C CD1 . PHE A 1 1266 ? 195.048 174.937 222.196 1.00 81.78  ? 1249 PHE B CD1 1 
ATOM   9869  C CD2 . PHE A 1 1266 ? 197.077 175.981 221.538 1.00 81.78  ? 1249 PHE B CD2 1 
ATOM   9870  C CE1 . PHE A 1 1266 ? 195.261 175.338 223.496 1.00 81.78  ? 1249 PHE B CE1 1 
ATOM   9871  C CE2 . PHE A 1 1266 ? 197.294 176.384 222.836 1.00 81.78  ? 1249 PHE B CE2 1 
ATOM   9872  C CZ  . PHE A 1 1266 ? 196.385 176.062 223.816 1.00 81.78  ? 1249 PHE B CZ  1 
ATOM   9873  N N   . ILE A 1 1267 ? 192.861 174.120 218.368 1.00 75.89  ? 1250 ILE B N   1 
ATOM   9874  C CA  . ILE A 1 1267 ? 192.121 174.334 217.136 1.00 75.89  ? 1250 ILE B CA  1 
ATOM   9875  C C   . ILE A 1 1267 ? 192.762 175.465 216.337 1.00 75.89  ? 1250 ILE B C   1 
ATOM   9876  O O   . ILE A 1 1267 ? 193.398 176.376 216.881 1.00 75.89  ? 1250 ILE B O   1 
ATOM   9877  C CB  . ILE A 1 1267 ? 190.643 174.628 217.439 1.00 75.89  ? 1250 ILE B CB  1 
ATOM   9878  C CG1 . ILE A 1 1267 ? 189.737 174.020 216.374 1.00 75.89  ? 1250 ILE B CG1 1 
ATOM   9879  C CG2 . ILE A 1 1267 ? 190.399 176.117 217.546 1.00 75.89  ? 1250 ILE B CG2 1 
ATOM   9880  C CD1 . ILE A 1 1267 ? 188.272 174.276 216.631 1.00 75.89  ? 1250 ILE B CD1 1 
ATOM   9881  N N   . GLY A 1 1268 ? 192.602 175.395 215.021 1.00 75.06  ? 1251 GLY B N   1 
ATOM   9882  C CA  . GLY A 1 1268 ? 193.196 176.390 214.149 1.00 75.06  ? 1251 GLY B CA  1 
ATOM   9883  C C   . GLY A 1 1268 ? 192.946 176.004 212.709 1.00 75.06  ? 1251 GLY B C   1 
ATOM   9884  O O   . GLY A 1 1268 ? 192.123 175.136 212.434 1.00 75.06  ? 1251 GLY B O   1 
ATOM   9885  N N   . PHE A 1 1269 ? 193.668 176.644 211.797 1.00 74.35  ? 1252 PHE B N   1 
ATOM   9886  C CA  . PHE A 1 1269 ? 193.471 176.376 210.381 1.00 74.35  ? 1252 PHE B CA  1 
ATOM   9887  C C   . PHE A 1 1269 ? 194.799 176.069 209.709 1.00 74.35  ? 1252 PHE B C   1 
ATOM   9888  O O   . PHE A 1 1269 ? 195.827 176.668 210.036 1.00 74.35  ? 1252 PHE B O   1 
ATOM   9889  C CB  . PHE A 1 1269 ? 192.773 177.550 209.686 1.00 74.35  ? 1252 PHE B CB  1 
ATOM   9890  C CG  . PHE A 1 1269 ? 193.700 178.635 209.231 1.00 74.35  ? 1252 PHE B CG  1 
ATOM   9891  C CD1 . PHE A 1 1269 ? 194.065 179.653 210.090 1.00 74.35  ? 1252 PHE B CD1 1 
ATOM   9892  C CD2 . PHE A 1 1269 ? 194.179 178.658 207.932 1.00 74.35  ? 1252 PHE B CD2 1 
ATOM   9893  C CE1 . PHE A 1 1269 ? 194.909 180.657 209.672 1.00 74.35  ? 1252 PHE B CE1 1 
ATOM   9894  C CE2 . PHE A 1 1269 ? 195.025 179.660 207.510 1.00 74.35  ? 1252 PHE B CE2 1 
ATOM   9895  C CZ  . PHE A 1 1269 ? 195.389 180.661 208.380 1.00 74.35  ? 1252 PHE B CZ  1 
ATOM   9896  N N   . HIS A 1 1270 ? 194.805 175.078 208.817 1.00 69.31  ? 1253 HIS B N   1 
ATOM   9897  C CA  . HIS A 1 1270 ? 195.969 174.732 208.016 1.00 69.31  ? 1253 HIS B CA  1 
ATOM   9898  C C   . HIS A 1 1270 ? 195.576 174.804 206.552 1.00 69.31  ? 1253 HIS B C   1 
ATOM   9899  O O   . HIS A 1 1270 ? 194.480 174.373 206.178 1.00 69.31  ? 1253 HIS B O   1 
ATOM   9900  C CB  . HIS A 1 1270 ? 196.498 173.337 208.355 1.00 69.31  ? 1253 HIS B CB  1 
ATOM   9901  C CG  . HIS A 1 1270 ? 197.823 173.023 207.732 1.00 69.31  ? 1253 HIS B CG  1 
ATOM   9902  N ND1 . HIS A 1 1270 ? 197.969 172.102 206.717 1.00 69.31  ? 1253 HIS B ND1 1 
ATOM   9903  C CD2 . HIS A 1 1270 ? 199.062 173.508 207.981 1.00 69.31  ? 1253 HIS B CD2 1 
ATOM   9904  C CE1 . HIS A 1 1270 ? 199.241 172.033 206.368 1.00 69.31  ? 1253 HIS B CE1 1 
ATOM   9905  N NE2 . HIS A 1 1270 ? 199.925 172.876 207.120 1.00 69.31  ? 1253 HIS B NE2 1 
ATOM   9906  N N   . GLN A 1 1271 ? 196.468 175.347 205.729 1.00 72.28  ? 1254 GLN B N   1 
ATOM   9907  C CA  . GLN A 1 1271 ? 196.216 175.449 204.299 1.00 72.28  ? 1254 GLN B CA  1 
ATOM   9908  C C   . GLN A 1 1271 ? 196.425 174.101 203.624 1.00 72.28  ? 1254 GLN B C   1 
ATOM   9909  O O   . GLN A 1 1271 ? 197.230 173.977 202.698 1.00 72.28  ? 1254 GLN B O   1 
ATOM   9910  C CB  . GLN A 1 1271 ? 197.102 176.539 203.685 1.00 72.28  ? 1254 GLN B CB  1 
ATOM   9911  C CG  . GLN A 1 1271 ? 198.523 176.610 204.247 1.00 72.28  ? 1254 GLN B CG  1 
ATOM   9912  C CD  . GLN A 1 1271 ? 199.476 175.594 203.645 1.00 72.28  ? 1254 GLN B CD  1 
ATOM   9913  O OE1 . GLN A 1 1271 ? 199.499 175.387 202.432 1.00 72.28  ? 1254 GLN B OE1 1 
ATOM   9914  N NE2 . GLN A 1 1271 ? 200.268 174.952 204.495 1.00 72.28  ? 1254 GLN B NE2 1 
ATOM   9915  N N   . PHE A 1 1272 ? 195.688 173.086 204.076 1.00 73.00  ? 1255 PHE B N   1 
ATOM   9916  C CA  . PHE A 1 1272 ? 195.804 171.752 203.505 1.00 73.00  ? 1255 PHE B CA  1 
ATOM   9917  C C   . PHE A 1 1272 ? 195.423 171.815 202.035 1.00 73.00  ? 1255 PHE B C   1 
ATOM   9918  O O   . PHE A 1 1272 ? 194.238 171.902 201.700 1.00 73.00  ? 1255 PHE B O   1 
ATOM   9919  C CB  . PHE A 1 1272 ? 194.898 170.781 204.267 1.00 73.00  ? 1255 PHE B CB  1 
ATOM   9920  C CG  . PHE A 1 1272 ? 195.242 169.337 204.068 1.00 73.00  ? 1255 PHE B CG  1 
ATOM   9921  C CD1 . PHE A 1 1272 ? 194.742 168.635 202.984 1.00 73.00  ? 1255 PHE B CD1 1 
ATOM   9922  C CD2 . PHE A 1 1272 ? 196.046 168.673 204.976 1.00 73.00  ? 1255 PHE B CD2 1 
ATOM   9923  C CE1 . PHE A 1 1272 ? 195.052 167.302 202.802 1.00 73.00  ? 1255 PHE B CE1 1 
ATOM   9924  C CE2 . PHE A 1 1272 ? 196.358 167.340 204.800 1.00 73.00  ? 1255 PHE B CE2 1 
ATOM   9925  C CZ  . PHE A 1 1272 ? 195.860 166.654 203.711 1.00 73.00  ? 1255 PHE B CZ  1 
ATOM   9926  N N   . ASN A 1 1273 ? 196.421 171.737 201.153 1.00 70.12  ? 1256 ASN B N   1 
ATOM   9927  C CA  . ASN A 1 1273 ? 196.226 172.023 199.736 1.00 70.12  ? 1256 ASN B CA  1 
ATOM   9928  C C   . ASN A 1 1273 ? 195.527 173.368 199.560 1.00 70.12  ? 1256 ASN B C   1 
ATOM   9929  O O   . ASN A 1 1273 ? 195.558 174.214 200.459 1.00 70.12  ? 1256 ASN B O   1 
ATOM   9930  C CB  . ASN A 1 1273 ? 195.446 170.904 199.045 1.00 70.12  ? 1256 ASN B CB  1 
ATOM   9931  C CG  . ASN A 1 1273 ? 195.840 170.739 197.589 1.00 70.12  ? 1256 ASN B CG  1 
ATOM   9932  O OD1 . ASN A 1 1273 ? 196.670 171.486 197.072 1.00 70.12  ? 1256 ASN B OD1 1 
ATOM   9933  N ND2 . ASN A 1 1273 ? 195.248 169.756 196.922 1.00 70.12  ? 1256 ASN B ND2 1 
ATOM   9934  N N   . ASN A 1 1274 ? 194.924 173.582 198.391 1.00 73.19  ? 1257 ASN B N   1 
ATOM   9935  C CA  . ASN A 1 1274 ? 194.239 174.828 198.063 1.00 73.19  ? 1257 ASN B CA  1 
ATOM   9936  C C   . ASN A 1 1274 ? 193.241 175.259 199.134 1.00 73.19  ? 1257 ASN B C   1 
ATOM   9937  O O   . ASN A 1 1274 ? 193.234 176.423 199.547 1.00 73.19  ? 1257 ASN B O   1 
ATOM   9938  C CB  . ASN A 1 1274 ? 193.524 174.681 196.720 1.00 73.19  ? 1257 ASN B CB  1 
ATOM   9939  C CG  . ASN A 1 1274 ? 194.346 173.910 195.708 1.00 73.19  ? 1257 ASN B CG  1 
ATOM   9940  O OD1 . ASN A 1 1274 ? 193.874 172.937 195.120 1.00 73.19  ? 1257 ASN B OD1 1 
ATOM   9941  N ND2 . ASN A 1 1274 ? 195.584 174.342 195.500 1.00 73.19  ? 1257 ASN B ND2 1 
ATOM   9942  N N   . ILE A 1 1275 ? 192.397 174.337 199.588 1.00 70.78  ? 1258 ILE B N   1 
ATOM   9943  C CA  . ILE A 1 1275 ? 191.330 174.661 200.531 1.00 70.78  ? 1258 ILE B CA  1 
ATOM   9944  C C   . ILE A 1 1275 ? 191.935 174.787 201.926 1.00 70.78  ? 1258 ILE B C   1 
ATOM   9945  O O   . ILE A 1 1275 ? 192.563 173.853 202.425 1.00 70.78  ? 1258 ILE B O   1 
ATOM   9946  C CB  . ILE A 1 1275 ? 190.220 173.605 200.504 1.00 70.78  ? 1258 ILE B CB  1 
ATOM   9947  C CG1 . ILE A 1 1275 ? 189.936 173.163 199.068 1.00 70.78  ? 1258 ILE B CG1 1 
ATOM   9948  C CG2 . ILE A 1 1275 ? 188.958 174.150 201.141 1.00 70.78  ? 1258 ILE B CG2 1 
ATOM   9949  C CD1 . ILE A 1 1275 ? 189.326 174.242 198.202 1.00 70.78  ? 1258 ILE B CD1 1 
ATOM   9950  N N   . ALA A 1 1276 ? 191.744 175.919 202.608 1.00 68.74  ? 1259 ALA B N   1 
ATOM   9951  C CA  . ALA A 1 1276 ? 192.285 176.153 203.945 1.00 68.74  ? 1259 ALA B CA  1 
ATOM   9952  C C   . ALA A 1 1276 ? 191.337 175.539 204.965 1.00 68.74  ? 1259 ALA B C   1 
ATOM   9953  O O   . ALA A 1 1276 ? 190.366 176.168 205.386 1.00 68.74  ? 1259 ALA B O   1 
ATOM   9954  C CB  . ALA A 1 1276 ? 192.479 177.643 204.195 1.00 68.74  ? 1259 ALA B CB  1 
ATOM   9955  N N   . LYS A 1 1277 ? 191.630 174.309 205.379 1.00 70.42  ? 1260 LYS B N   1 
ATOM   9956  C CA  . LYS A 1 1277 ? 190.747 173.564 206.261 1.00 70.42  ? 1260 LYS B CA  1 
ATOM   9957  C C   . LYS A 1 1277 ? 191.007 173.925 207.720 1.00 70.42  ? 1260 LYS B C   1 
ATOM   9958  O O   . LYS A 1 1277 ? 191.997 174.575 208.064 1.00 70.42  ? 1260 LYS B O   1 
ATOM   9959  C CB  . LYS A 1 1277 ? 190.938 172.066 206.062 1.00 70.42  ? 1260 LYS B CB  1 
ATOM   9960  C CG  . LYS A 1 1277 ? 191.058 171.649 204.619 1.00 70.42  ? 1260 LYS B CG  1 
ATOM   9961  C CD  . LYS A 1 1277 ? 191.386 170.177 204.515 1.00 70.42  ? 1260 LYS B CD  1 
ATOM   9962  C CE  . LYS A 1 1277 ? 190.356 169.439 203.694 1.00 70.42  ? 1260 LYS B CE  1 
ATOM   9963  N NZ  . LYS A 1 1277 ? 190.153 170.089 202.373 1.00 70.42  ? 1260 LYS B NZ  1 
ATOM   9964  N N   . LEU A 1 1278 ? 190.096 173.490 208.585 1.00 69.60  ? 1261 LEU B N   1 
ATOM   9965  C CA  . LEU A 1 1278 ? 190.274 173.621 210.023 1.00 69.60  ? 1261 LEU B CA  1 
ATOM   9966  C C   . LEU A 1 1278 ? 190.862 172.336 210.584 1.00 69.60  ? 1261 LEU B C   1 
ATOM   9967  O O   . LEU A 1 1278 ? 190.431 171.236 210.231 1.00 69.60  ? 1261 LEU B O   1 
ATOM   9968  C CB  . LEU A 1 1278 ? 188.948 173.932 210.713 1.00 69.60  ? 1261 LEU B CB  1 
ATOM   9969  C CG  . LEU A 1 1278 ? 188.548 175.401 210.802 1.00 69.60  ? 1261 LEU B CG  1 
ATOM   9970  C CD1 . LEU A 1 1278 ? 187.625 175.758 209.661 1.00 69.60  ? 1261 LEU B CD1 1 
ATOM   9971  C CD2 . LEU A 1 1278 ? 187.887 175.683 212.131 1.00 69.60  ? 1261 LEU B CD2 1 
ATOM   9972  N N   . VAL A 1 1279 ? 191.852 172.481 211.459 1.00 73.96  ? 1262 VAL B N   1 
ATOM   9973  C CA  . VAL A 1 1279 ? 192.583 171.350 212.007 1.00 73.96  ? 1262 VAL B CA  1 
ATOM   9974  C C   . VAL A 1 1279 ? 192.813 171.563 213.495 1.00 73.96  ? 1262 VAL B C   1 
ATOM   9975  O O   . VAL A 1 1279 ? 192.918 172.695 213.976 1.00 73.96  ? 1262 VAL B O   1 
ATOM   9976  C CB  . VAL A 1 1279 ? 193.935 171.150 211.300 1.00 73.96  ? 1262 VAL B CB  1 
ATOM   9977  C CG1 . VAL A 1 1279 ? 193.737 170.531 209.934 1.00 73.96  ? 1262 VAL B CG1 1 
ATOM   9978  C CG2 . VAL A 1 1279 ? 194.663 172.471 211.201 1.00 73.96  ? 1262 VAL B CG2 1 
ATOM   9979  N N   . ALA A 1 1280 ? 192.910 170.456 214.220 1.00 76.49  ? 1263 ALA B N   1 
ATOM   9980  C CA  . ALA A 1 1280 ? 193.385 170.453 215.597 1.00 76.49  ? 1263 ALA B CA  1 
ATOM   9981  C C   . ALA A 1 1280 ? 194.856 170.066 215.542 1.00 76.49  ? 1263 ALA B C   1 
ATOM   9982  O O   . ALA A 1 1280 ? 195.194 168.891 215.389 1.00 76.49  ? 1263 ALA B O   1 
ATOM   9983  C CB  . ALA A 1 1280 ? 192.579 169.491 216.458 1.00 76.49  ? 1263 ALA B CB  1 
ATOM   9984  N N   . SER A 1 1281 ? 195.728 171.060 215.663 1.00 86.27  ? 1264 SER B N   1 
ATOM   9985  C CA  . SER A 1 1281 ? 197.157 170.882 215.463 1.00 86.27  ? 1264 SER B CA  1 
ATOM   9986  C C   . SER A 1 1281 ? 197.897 170.985 216.788 1.00 86.27  ? 1264 SER B C   1 
ATOM   9987  O O   . SER A 1 1281 ? 197.528 171.781 217.657 1.00 86.27  ? 1264 SER B O   1 
ATOM   9988  C CB  . SER A 1 1281 ? 197.703 171.926 214.490 1.00 86.27  ? 1264 SER B CB  1 
ATOM   9989  O OG  . SER A 1 1281 ? 199.075 171.701 214.228 1.00 86.27  ? 1264 SER B OG  1 
ATOM   9990  N N   . ASN A 1 1282 ? 198.933 170.164 216.942 1.00 90.36  ? 1265 ASN B N   1 
ATOM   9991  C CA  . ASN A 1 1282 ? 199.801 170.245 218.106 1.00 90.36  ? 1265 ASN B CA  1 
ATOM   9992  C C   . ASN A 1 1282 ? 200.962 171.205 217.906 1.00 90.36  ? 1265 ASN B C   1 
ATOM   9993  O O   . ASN A 1 1282 ? 201.697 171.472 218.862 1.00 90.36  ? 1265 ASN B O   1 
ATOM   9994  C CB  . ASN A 1 1282 ? 200.335 168.856 218.469 1.00 90.36  ? 1265 ASN B CB  1 
ATOM   9995  C CG  . ASN A 1 1282 ? 199.544 168.204 219.585 1.00 90.36  ? 1265 ASN B CG  1 
ATOM   9996  O OD1 . ASN A 1 1282 ? 199.269 168.826 220.610 1.00 90.36  ? 1265 ASN B OD1 1 
ATOM   9997  N ND2 . ASN A 1 1282 ? 199.172 166.945 219.391 1.00 90.36  ? 1265 ASN B ND2 1 
ATOM   9998  N N   . TRP A 1 1283 ? 201.148 171.722 216.690 1.00 92.25  ? 1266 TRP B N   1 
ATOM   9999  C CA  . TRP A 1 1283 ? 202.127 172.782 216.481 1.00 92.25  ? 1266 TRP B CA  1 
ATOM   10000 C C   . TRP A 1 1283 ? 201.745 174.029 217.268 1.00 92.25  ? 1266 TRP B C   1 
ATOM   10001 O O   . TRP A 1 1283 ? 202.601 174.668 217.891 1.00 92.25  ? 1266 TRP B O   1 
ATOM   10002 C CB  . TRP A 1 1283 ? 202.243 173.096 214.987 1.00 92.25  ? 1266 TRP B CB  1 
ATOM   10003 C CG  . TRP A 1 1283 ? 202.867 174.430 214.659 1.00 92.25  ? 1266 TRP B CG  1 
ATOM   10004 C CD1 . TRP A 1 1283 ? 202.410 175.336 213.747 1.00 92.25  ? 1266 TRP B CD1 1 
ATOM   10005 C CD2 . TRP A 1 1283 ? 204.085 174.980 215.189 1.00 92.25  ? 1266 TRP B CD2 1 
ATOM   10006 N NE1 . TRP A 1 1283 ? 203.242 176.428 213.701 1.00 92.25  ? 1266 TRP B NE1 1 
ATOM   10007 C CE2 . TRP A 1 1283 ? 204.279 176.232 214.573 1.00 92.25  ? 1266 TRP B CE2 1 
ATOM   10008 C CE3 . TRP A 1 1283 ? 205.022 174.541 216.130 1.00 92.25  ? 1266 TRP B CE3 1 
ATOM   10009 C CZ2 . TRP A 1 1283 ? 205.367 177.049 214.869 1.00 92.25  ? 1266 TRP B CZ2 1 
ATOM   10010 C CZ3 . TRP A 1 1283 ? 206.099 175.356 216.425 1.00 92.25  ? 1266 TRP B CZ3 1 
ATOM   10011 C CH2 . TRP A 1 1283 ? 206.263 176.594 215.796 1.00 92.25  ? 1266 TRP B CH2 1 
ATOM   10012 N N   . TYR A 1 1284 ? 200.458 174.380 217.267 1.00 88.80  ? 1267 TYR B N   1 
ATOM   10013 C CA  . TYR A 1 1284 ? 200.000 175.540 218.020 1.00 88.80  ? 1267 TYR B CA  1 
ATOM   10014 C C   . TYR A 1 1284 ? 200.215 175.373 219.515 1.00 88.80  ? 1267 TYR B C   1 
ATOM   10015 O O   . TYR A 1 1284 ? 200.288 176.373 220.235 1.00 88.80  ? 1267 TYR B O   1 
ATOM   10016 C CB  . TYR A 1 1284 ? 198.521 175.801 217.733 1.00 88.80  ? 1267 TYR B CB  1 
ATOM   10017 C CG  . TYR A 1 1284 ? 198.233 176.148 216.295 1.00 88.80  ? 1267 TYR B CG  1 
ATOM   10018 C CD1 . TYR A 1 1284 ? 199.180 176.789 215.515 1.00 88.80  ? 1267 TYR B CD1 1 
ATOM   10019 C CD2 . TYR A 1 1284 ? 197.020 175.821 215.713 1.00 88.80  ? 1267 TYR B CD2 1 
ATOM   10020 C CE1 . TYR A 1 1284 ? 198.925 177.103 214.201 1.00 88.80  ? 1267 TYR B CE1 1 
ATOM   10021 C CE2 . TYR A 1 1284 ? 196.756 176.130 214.399 1.00 88.80  ? 1267 TYR B CE2 1 
ATOM   10022 C CZ  . TYR A 1 1284 ? 197.712 176.772 213.647 1.00 88.80  ? 1267 TYR B CZ  1 
ATOM   10023 O OH  . TYR A 1 1284 ? 197.457 177.086 212.333 1.00 88.80  ? 1267 TYR B OH  1 
ATOM   10024 N N   . ASN A 1 1285 ? 200.315 174.135 220.000 1.00 91.29  ? 1268 ASN B N   1 
ATOM   10025 C CA  . ASN A 1 1285 ? 200.607 173.898 221.407 1.00 91.29  ? 1268 ASN B CA  1 
ATOM   10026 C C   . ASN A 1 1285 ? 202.055 174.199 221.765 1.00 91.29  ? 1268 ASN B C   1 
ATOM   10027 O O   . ASN A 1 1285 ? 202.393 174.201 222.953 1.00 91.29  ? 1268 ASN B O   1 
ATOM   10028 C CB  . ASN A 1 1285 ? 200.280 172.449 221.770 1.00 91.29  ? 1268 ASN B CB  1 
ATOM   10029 C CG  . ASN A 1 1285 ? 198.952 172.314 222.479 1.00 91.29  ? 1268 ASN B CG  1 
ATOM   10030 O OD1 . ASN A 1 1285 ? 198.156 173.251 222.514 1.00 91.29  ? 1268 ASN B OD1 1 
ATOM   10031 N ND2 . ASN A 1 1285 ? 198.703 171.141 223.049 1.00 91.29  ? 1268 ASN B ND2 1 
ATOM   10032 N N   . ARG A 1 1286 ? 202.910 174.445 220.777 1.00 96.64  ? 1269 ARG B N   1 
ATOM   10033 C CA  . ARG A 1 1286 ? 204.336 174.672 220.984 1.00 96.64  ? 1269 ARG B CA  1 
ATOM   10034 C C   . ARG A 1 1286 ? 204.705 176.144 220.817 1.00 96.64  ? 1269 ARG B C   1 
ATOM   10035 O O   . ARG A 1 1286 ? 205.726 176.478 220.212 1.00 96.64  ? 1269 ARG B O   1 
ATOM   10036 C CB  . ARG A 1 1286 ? 205.159 173.801 220.040 1.00 96.64  ? 1269 ARG B CB  1 
ATOM   10037 C CG  . ARG A 1 1286 ? 205.915 172.689 220.742 1.00 96.64  ? 1269 ARG B CG  1 
ATOM   10038 C CD  . ARG A 1 1286 ? 206.418 171.651 219.757 1.00 96.64  ? 1269 ARG B CD  1 
ATOM   10039 N NE  . ARG A 1 1286 ? 205.324 170.863 219.201 1.00 96.64  ? 1269 ARG B NE  1 
ATOM   10040 C CZ  . ARG A 1 1286 ? 204.775 169.816 219.799 1.00 96.64  ? 1269 ARG B CZ  1 
ATOM   10041 N NH1 . ARG A 1 1286 ? 205.188 169.402 220.986 1.00 96.64  ? 1269 ARG B NH1 1 
ATOM   10042 N NH2 . ARG A 1 1286 ? 203.784 169.168 219.194 1.00 96.64  ? 1269 ARG B NH2 1 
ATOM   10043 N N   . GLN A 1 1287 ? 203.864 177.035 221.334 1.00 99.79  ? 1270 GLN B N   1 
ATOM   10044 C CA  . GLN A 1 1287 ? 204.114 178.473 221.280 1.00 99.79  ? 1270 GLN B CA  1 
ATOM   10045 C C   . GLN A 1 1287 ? 205.480 178.838 221.856 1.00 99.79  ? 1270 GLN B C   1 
ATOM   10046 O O   . GLN A 1 1287 ? 205.971 178.186 222.778 1.00 99.79  ? 1270 GLN B O   1 
ATOM   10047 C CB  . GLN A 1 1287 ? 203.021 179.233 222.033 1.00 99.79  ? 1270 GLN B CB  1 
ATOM   10048 C CG  . GLN A 1 1287 ? 201.616 178.736 221.753 1.00 99.79  ? 1270 GLN B CG  1 
ATOM   10049 C CD  . GLN A 1 1287 ? 200.556 179.779 222.039 1.00 99.79  ? 1270 GLN B CD  1 
ATOM   10050 O OE1 . GLN A 1 1287 ? 199.637 179.546 222.824 1.00 99.79  ? 1270 GLN B OE1 1 
ATOM   10051 N NE2 . GLN A 1 1287 ? 200.678 180.937 221.402 1.00 99.79  ? 1270 GLN B NE2 1 
ATOM   10052 N N   . LEU A 1 1295 ? 200.571 182.172 215.297 1.00 80.50  ? 1278 LEU B N   1 
ATOM   10053 C CA  . LEU A 1 1295 ? 199.167 182.486 215.531 1.00 80.50  ? 1278 LEU B CA  1 
ATOM   10054 C C   . LEU A 1 1295 ? 198.260 181.528 214.774 1.00 80.50  ? 1278 LEU B C   1 
ATOM   10055 O O   . LEU A 1 1295 ? 198.690 180.460 214.344 1.00 80.50  ? 1278 LEU B O   1 
ATOM   10056 C CB  . LEU A 1 1295 ? 198.861 183.928 215.125 1.00 80.50  ? 1278 LEU B CB  1 
ATOM   10057 C CG  . LEU A 1 1295 ? 198.711 184.930 216.270 1.00 80.50  ? 1278 LEU B CG  1 
ATOM   10058 C CD1 . LEU A 1 1295 ? 200.012 185.051 217.046 1.00 80.50  ? 1278 LEU B CD1 1 
ATOM   10059 C CD2 . LEU A 1 1295 ? 198.265 186.285 215.744 1.00 80.50  ? 1278 LEU B CD2 1 
ATOM   10060 N N   . GLY A 1 1296 ? 197.001 181.924 214.605 1.00 78.29  ? 1279 GLY B N   1 
ATOM   10061 C CA  . GLY A 1 1296 ? 196.000 181.068 214.012 1.00 78.29  ? 1279 GLY B CA  1 
ATOM   10062 C C   . GLY A 1 1296 ? 195.230 180.222 215.000 1.00 78.29  ? 1279 GLY B C   1 
ATOM   10063 O O   . GLY A 1 1296 ? 194.254 179.573 214.606 1.00 78.29  ? 1279 GLY B O   1 
ATOM   10064 N N   . CYS A 1 1297 ? 195.638 180.203 216.266 1.00 79.59  ? 1280 CYS B N   1 
ATOM   10065 C CA  . CYS A 1 1297 ? 194.927 179.487 217.313 1.00 79.59  ? 1280 CYS B CA  1 
ATOM   10066 C C   . CYS A 1 1297 ? 194.113 180.417 218.200 1.00 79.59  ? 1280 CYS B C   1 
ATOM   10067 O O   . CYS A 1 1297 ? 193.631 179.988 219.253 1.00 79.59  ? 1280 CYS B O   1 
ATOM   10068 C CB  . CYS A 1 1297 ? 195.909 178.680 218.164 1.00 79.59  ? 1280 CYS B CB  1 
ATOM   10069 S SG  . CYS A 1 1297 ? 197.250 179.648 218.882 1.00 79.59  ? 1280 CYS B SG  1 
ATOM   10070 N N   . SER A 1 1298 ? 193.958 181.677 217.806 1.00 74.52  ? 1281 SER B N   1 
ATOM   10071 C CA  . SER A 1 1298 ? 193.171 182.651 218.547 1.00 74.52  ? 1281 SER B CA  1 
ATOM   10072 C C   . SER A 1 1298 ? 191.904 182.962 217.766 1.00 74.52  ? 1281 SER B C   1 
ATOM   10073 O O   . SER A 1 1298 ? 191.967 183.249 216.567 1.00 74.52  ? 1281 SER B O   1 
ATOM   10074 C CB  . SER A 1 1298 ? 193.970 183.930 218.792 1.00 74.52  ? 1281 SER B CB  1 
ATOM   10075 O OG  . SER A 1 1298 ? 193.894 184.791 217.672 1.00 74.52  ? 1281 SER B OG  1 
ATOM   10076 N N   . TRP A 1 1299 ? 190.761 182.911 218.446 1.00 68.50  ? 1282 TRP B N   1 
ATOM   10077 C CA  . TRP A 1 1299 ? 189.466 183.056 217.804 1.00 68.50  ? 1282 TRP B CA  1 
ATOM   10078 C C   . TRP A 1 1299 ? 188.659 184.138 218.504 1.00 68.50  ? 1282 TRP B C   1 
ATOM   10079 O O   . TRP A 1 1299 ? 188.954 184.530 219.634 1.00 68.50  ? 1282 TRP B O   1 
ATOM   10080 C CB  . TRP A 1 1299 ? 188.689 181.736 217.818 1.00 68.50  ? 1282 TRP B CB  1 
ATOM   10081 C CG  . TRP A 1 1299 ? 189.307 180.688 216.967 1.00 68.50  ? 1282 TRP B CG  1 
ATOM   10082 C CD1 . TRP A 1 1299 ? 190.404 179.942 217.262 1.00 68.50  ? 1282 TRP B CD1 1 
ATOM   10083 C CD2 . TRP A 1 1299 ? 188.868 180.263 215.675 1.00 68.50  ? 1282 TRP B CD2 1 
ATOM   10084 N NE1 . TRP A 1 1299 ? 190.680 179.080 216.234 1.00 68.50  ? 1282 TRP B NE1 1 
ATOM   10085 C CE2 . TRP A 1 1299 ? 189.749 179.257 215.246 1.00 68.50  ? 1282 TRP B CE2 1 
ATOM   10086 C CE3 . TRP A 1 1299 ? 187.816 180.636 214.839 1.00 68.50  ? 1282 TRP B CE3 1 
ATOM   10087 C CZ2 . TRP A 1 1299 ? 189.611 178.620 214.020 1.00 68.50  ? 1282 TRP B CZ2 1 
ATOM   10088 C CZ3 . TRP A 1 1299 ? 187.681 180.002 213.623 1.00 68.50  ? 1282 TRP B CZ3 1 
ATOM   10089 C CH2 . TRP A 1 1299 ? 188.572 179.006 213.224 1.00 68.50  ? 1282 TRP B CH2 1 
ATOM   10090 N N   . GLU A 1 1300 ? 187.634 184.623 217.809 1.00 64.30  ? 1283 GLU B N   1 
ATOM   10091 C CA  . GLU A 1 1300 ? 186.720 185.621 218.339 1.00 64.30  ? 1283 GLU B CA  1 
ATOM   10092 C C   . GLU A 1 1300 ? 185.296 185.162 218.080 1.00 64.30  ? 1283 GLU B C   1 
ATOM   10093 O O   . GLU A 1 1300 ? 184.967 184.743 216.965 1.00 64.30  ? 1283 GLU B O   1 
ATOM   10094 C CB  . GLU A 1 1300 ? 186.953 186.991 217.701 1.00 64.30  ? 1283 GLU B CB  1 
ATOM   10095 C CG  . GLU A 1 1300 ? 188.360 187.526 217.865 1.00 64.30  ? 1283 GLU B CG  1 
ATOM   10096 C CD  . GLU A 1 1300 ? 188.477 188.513 219.002 1.00 64.30  ? 1283 GLU B CD  1 
ATOM   10097 O OE1 . GLU A 1 1300 ? 187.887 188.262 220.073 1.00 64.30  ? 1283 GLU B OE1 1 
ATOM   10098 O OE2 . GLU A 1 1300 ? 189.159 189.543 218.825 1.00 64.30  ? 1283 GLU B OE2 1 
ATOM   10099 N N   . PHE A 1 1301 ? 184.461 185.246 219.109 1.00 60.03  ? 1284 PHE B N   1 
ATOM   10100 C CA  . PHE A 1 1301 ? 183.056 184.877 219.025 1.00 60.03  ? 1284 PHE B CA  1 
ATOM   10101 C C   . PHE A 1 1301 ? 182.230 186.147 218.892 1.00 60.03  ? 1284 PHE B C   1 
ATOM   10102 O O   . PHE A 1 1301 ? 182.259 187.005 219.780 1.00 60.03  ? 1284 PHE B O   1 
ATOM   10103 C CB  . PHE A 1 1301 ? 182.628 184.092 220.262 1.00 60.03  ? 1284 PHE B CB  1 
ATOM   10104 C CG  . PHE A 1 1301 ? 183.411 182.837 220.488 1.00 60.03  ? 1284 PHE B CG  1 
ATOM   10105 C CD1 . PHE A 1 1301 ? 184.646 182.880 221.103 1.00 60.03  ? 1284 PHE B CD1 1 
ATOM   10106 C CD2 . PHE A 1 1301 ? 182.904 181.612 220.103 1.00 60.03  ? 1284 PHE B CD2 1 
ATOM   10107 C CE1 . PHE A 1 1301 ? 185.365 181.728 221.317 1.00 60.03  ? 1284 PHE B CE1 1 
ATOM   10108 C CE2 . PHE A 1 1301 ? 183.618 180.456 220.318 1.00 60.03  ? 1284 PHE B CE2 1 
ATOM   10109 C CZ  . PHE A 1 1301 ? 184.849 180.516 220.926 1.00 60.03  ? 1284 PHE B CZ  1 
ATOM   10110 N N   . ILE A 1 1302 ? 181.495 186.266 217.794 1.00 55.23  ? 1285 ILE B N   1 
ATOM   10111 C CA  . ILE A 1 1302 ? 180.689 187.444 217.504 1.00 55.23  ? 1285 ILE B CA  1 
ATOM   10112 C C   . ILE A 1 1302 ? 179.221 187.048 217.641 1.00 55.23  ? 1285 ILE B C   1 
ATOM   10113 O O   . ILE A 1 1302 ? 178.686 186.347 216.770 1.00 55.23  ? 1285 ILE B O   1 
ATOM   10114 C CB  . ILE A 1 1302 ? 180.986 187.999 216.107 1.00 55.23  ? 1285 ILE B CB  1 
ATOM   10115 C CG1 . ILE A 1 1302 ? 182.492 188.057 215.873 1.00 55.23  ? 1285 ILE B CG1 1 
ATOM   10116 C CG2 . ILE A 1 1302 ? 180.375 189.373 215.945 1.00 55.23  ? 1285 ILE B CG2 1 
ATOM   10117 C CD1 . ILE A 1 1302 ? 182.869 188.466 214.479 1.00 55.23  ? 1285 ILE B CD1 1 
ATOM   10118 N N   . PRO A 1 1303 ? 178.541 187.446 218.710 1.00 54.44  ? 1286 PRO B N   1 
ATOM   10119 C CA  . PRO A 1 1303 ? 177.100 187.224 218.809 1.00 54.44  ? 1286 PRO B CA  1 
ATOM   10120 C C   . PRO A 1 1303 ? 176.315 188.380 218.206 1.00 54.44  ? 1286 PRO B C   1 
ATOM   10121 O O   . PRO A 1 1303 ? 176.814 189.494 218.043 1.00 54.44  ? 1286 PRO B O   1 
ATOM   10122 C CB  . PRO A 1 1303 ? 176.873 187.143 220.322 1.00 54.44  ? 1286 PRO B CB  1 
ATOM   10123 C CG  . PRO A 1 1303 ? 177.902 188.056 220.877 1.00 54.44  ? 1286 PRO B CG  1 
ATOM   10124 C CD  . PRO A 1 1303 ? 179.095 188.002 219.954 1.00 54.44  ? 1286 PRO B CD  1 
ATOM   10125 N N   . VAL A 1 1304 ? 175.059 188.089 217.875 1.00 56.93  ? 1287 VAL B N   1 
ATOM   10126 C CA  . VAL A 1 1304 ? 174.180 189.103 217.305 1.00 56.93  ? 1287 VAL B CA  1 
ATOM   10127 C C   . VAL A 1 1304 ? 173.900 190.159 218.364 1.00 56.93  ? 1287 VAL B C   1 
ATOM   10128 O O   . VAL A 1 1304 ? 173.343 189.861 219.427 1.00 56.93  ? 1287 VAL B O   1 
ATOM   10129 C CB  . VAL A 1 1304 ? 172.881 188.475 216.790 1.00 56.93  ? 1287 VAL B CB  1 
ATOM   10130 C CG1 . VAL A 1 1304 ? 172.211 189.394 215.785 1.00 56.93  ? 1287 VAL B CG1 1 
ATOM   10131 C CG2 . VAL A 1 1304 ? 173.160 187.113 216.175 1.00 56.93  ? 1287 VAL B CG2 1 
ATOM   10132 N N   . ASP A 1 1305 ? 174.279 191.399 218.079 1.00 56.10  ? 1288 ASP B N   1 
ATOM   10133 C CA  . ASP A 1 1305 ? 174.118 192.497 219.016 1.00 56.10  ? 1288 ASP B CA  1 
ATOM   10134 C C   . ASP A 1 1305 ? 173.331 193.626 218.368 1.00 56.10  ? 1288 ASP B C   1 
ATOM   10135 O O   . ASP A 1 1305 ? 173.401 193.838 217.154 1.00 56.10  ? 1288 ASP B O   1 
ATOM   10136 C CB  . ASP A 1 1305 ? 175.470 193.018 219.498 1.00 56.10  ? 1288 ASP B CB  1 
ATOM   10137 C CG  . ASP A 1 1305 ? 175.353 193.871 220.738 1.00 56.10  ? 1288 ASP B CG  1 
ATOM   10138 O OD1 . ASP A 1 1305 ? 175.051 195.074 220.602 1.00 56.10  ? 1288 ASP B OD1 1 
ATOM   10139 O OD2 . ASP A 1 1305 ? 175.560 193.341 221.848 1.00 56.10  ? 1288 ASP B OD2 1 
ATOM   10140 N N   . ASP A 1 1306 ? 172.581 194.351 219.191 1.00 59.38  ? 1289 ASP B N   1 
ATOM   10141 C CA  . ASP A 1 1306 ? 171.734 195.438 218.724 1.00 59.38  ? 1289 ASP B CA  1 
ATOM   10142 C C   . ASP A 1 1306 ? 172.478 196.760 218.606 1.00 59.38  ? 1289 ASP B C   1 
ATOM   10143 O O   . ASP A 1 1306 ? 171.865 197.769 218.244 1.00 59.38  ? 1289 ASP B O   1 
ATOM   10144 C CB  . ASP A 1 1306 ? 170.530 195.604 219.656 1.00 59.38  ? 1289 ASP B CB  1 
ATOM   10145 C CG  . ASP A 1 1306 ? 169.908 194.277 220.047 1.00 59.38  ? 1289 ASP B CG  1 
ATOM   10146 O OD1 . ASP A 1 1306 ? 169.366 193.586 219.159 1.00 59.38  ? 1289 ASP B OD1 1 
ATOM   10147 O OD2 . ASP A 1 1306 ? 169.962 193.923 221.244 1.00 59.38  ? 1289 ASP B OD2 1 
ATOM   10148 N N   . GLY A 1 1307 ? 173.770 196.784 218.914 1.00 52.52  ? 1290 GLY B N   1 
ATOM   10149 C CA  . GLY A 1 1307 ? 174.561 197.985 218.746 1.00 52.52  ? 1290 GLY B CA  1 
ATOM   10150 C C   . GLY A 1 1307 ? 175.371 197.981 217.467 1.00 52.52  ? 1290 GLY B C   1 
ATOM   10151 O O   . GLY A 1 1307 ? 175.946 199.004 217.087 1.00 52.52  ? 1290 GLY B O   1 
ATOM   10152 N N   . TRP A 1 1308 ? 175.424 196.835 216.791 1.00 53.21  ? 1291 TRP B N   1 
ATOM   10153 C CA  . TRP A 1 1308 ? 176.173 196.728 215.546 1.00 53.21  ? 1291 TRP B CA  1 
ATOM   10154 C C   . TRP A 1 1308 ? 175.335 197.129 214.339 1.00 53.21  ? 1291 TRP B C   1 
ATOM   10155 O O   . TRP A 1 1308 ? 175.845 197.782 213.423 1.00 53.21  ? 1291 TRP B O   1 
ATOM   10156 C CB  . TRP A 1 1308 ? 176.708 195.304 215.374 1.00 53.21  ? 1291 TRP B CB  1 
ATOM   10157 C CG  . TRP A 1 1308 ? 177.648 195.133 214.217 1.00 53.21  ? 1291 TRP B CG  1 
ATOM   10158 C CD1 . TRP A 1 1308 ? 177.516 194.259 213.182 1.00 53.21  ? 1291 TRP B CD1 1 
ATOM   10159 C CD2 . TRP A 1 1308 ? 178.865 195.851 213.978 1.00 53.21  ? 1291 TRP B CD2 1 
ATOM   10160 N NE1 . TRP A 1 1308 ? 178.569 194.387 212.313 1.00 53.21  ? 1291 TRP B NE1 1 
ATOM   10161 C CE2 . TRP A 1 1308 ? 179.411 195.359 212.780 1.00 53.21  ? 1291 TRP B CE2 1 
ATOM   10162 C CE3 . TRP A 1 1308 ? 179.542 196.864 214.661 1.00 53.21  ? 1291 TRP B CE3 1 
ATOM   10163 C CZ2 . TRP A 1 1308 ? 180.600 195.844 212.251 1.00 53.21  ? 1291 TRP B CZ2 1 
ATOM   10164 C CZ3 . TRP A 1 1308 ? 180.722 197.342 214.133 1.00 53.21  ? 1291 TRP B CZ3 1 
ATOM   10165 C CH2 . TRP A 1 1308 ? 181.240 196.833 212.941 1.00 53.21  ? 1291 TRP B CH2 1 
ATOM   10166 N N   . GLY A 1 1309 ? 174.058 196.759 214.316 1.00 60.88  ? 1292 GLY B N   1 
ATOM   10167 C CA  . GLY A 1 1309 ? 173.152 197.231 213.292 1.00 60.88  ? 1292 GLY B CA  1 
ATOM   10168 C C   . GLY A 1 1309 ? 173.180 196.476 211.982 1.00 60.88  ? 1292 GLY B C   1 
ATOM   10169 O O   . GLY A 1 1309 ? 172.471 196.870 211.049 1.00 60.88  ? 1292 GLY B O   1 
ATOM   10170 N N   . GLU A 1 1310 ? 173.977 195.421 211.870 1.00 64.04  ? 1293 GLU B N   1 
ATOM   10171 C CA  . GLU A 1 1310 ? 173.968 194.596 210.672 1.00 64.04  ? 1293 GLU B CA  1 
ATOM   10172 C C   . GLU A 1 1310 ? 172.824 193.593 210.735 1.00 64.04  ? 1293 GLU B C   1 
ATOM   10173 O O   . GLU A 1 1310 ? 172.562 192.997 211.783 1.00 64.04  ? 1293 GLU B O   1 
ATOM   10174 C CB  . GLU A 1 1310 ? 175.300 193.865 210.517 1.00 64.04  ? 1293 GLU B CB  1 
ATOM   10175 C CG  . GLU A 1 1310 ? 175.237 192.662 209.607 1.00 64.04  ? 1293 GLU B CG  1 
ATOM   10176 C CD  . GLU A 1 1310 ? 176.576 192.317 209.010 1.00 64.04  ? 1293 GLU B CD  1 
ATOM   10177 O OE1 . GLU A 1 1310 ? 177.592 192.882 209.461 1.00 64.04  ? 1293 GLU B OE1 1 
ATOM   10178 O OE2 . GLU A 1 1310 ? 176.612 191.475 208.091 1.00 64.04  ? 1293 GLU B OE2 1 
ATOM   10179 N N   . ARG A 1 1311 ? 172.139 193.412 209.609 1.00 73.40  ? 1294 ARG B N   1 
ATOM   10180 C CA  . ARG A 1 1311 ? 171.023 192.478 209.547 1.00 73.40  ? 1294 ARG B CA  1 
ATOM   10181 C C   . ARG A 1 1311 ? 171.526 191.102 209.139 1.00 73.40  ? 1294 ARG B C   1 
ATOM   10182 O O   . ARG A 1 1311 ? 172.078 190.959 208.040 1.00 73.40  ? 1294 ARG B O   1 
ATOM   10183 C CB  . ARG A 1 1311 ? 169.971 192.952 208.562 1.00 73.40  ? 1294 ARG B CB  1 
ATOM   10184 C CG  . ARG A 1 1311 ? 169.267 194.235 208.964 1.00 73.40  ? 1294 ARG B CG  1 
ATOM   10185 C CD  . ARG A 1 1311 ? 169.982 195.446 208.400 1.00 73.40  ? 1294 ARG B CD  1 
ATOM   10186 N NE  . ARG A 1 1311 ? 170.014 195.402 206.945 1.00 73.40  ? 1294 ARG B NE  1 
ATOM   10187 C CZ  . ARG A 1 1311 ? 169.005 195.761 206.165 1.00 73.40  ? 1294 ARG B CZ  1 
ATOM   10188 N NH1 . ARG A 1 1311 ? 167.873 196.224 206.669 1.00 73.40  ? 1294 ARG B NH1 1 
ATOM   10189 N NH2 . ARG A 1 1311 ? 169.132 195.646 204.847 1.00 73.40  ? 1294 ARG B NH2 1 
ATOM   10190 N N   . PRO A 1 1312 ? 171.355 190.078 209.965 1.00 75.15  ? 1295 PRO B N   1 
ATOM   10191 C CA  . PRO A 1 1312 ? 171.812 188.716 209.617 1.00 75.15  ? 1295 PRO B CA  1 
ATOM   10192 C C   . PRO A 1 1312 ? 170.913 188.056 208.575 1.00 75.15  ? 1295 PRO B C   1 
ATOM   10193 O O   . PRO A 1 1312 ? 169.943 187.360 208.870 1.00 75.15  ? 1295 PRO B O   1 
ATOM   10194 C CB  . PRO A 1 1312 ? 171.761 187.987 210.964 1.00 75.15  ? 1295 PRO B CB  1 
ATOM   10195 C CG  . PRO A 1 1312 ? 171.545 189.052 212.007 1.00 75.15  ? 1295 PRO B CG  1 
ATOM   10196 C CD  . PRO A 1 1312 ? 170.799 190.135 211.322 1.00 75.15  ? 1295 PRO B CD  1 
ATOM   10197 N N   . LEU A 1 1313 ? 171.238 188.297 207.310 1.00 83.45  ? 1296 LEU B N   1 
ATOM   10198 C CA  . LEU A 1 1313 ? 170.482 187.735 206.197 1.00 83.45  ? 1296 LEU B CA  1 
ATOM   10199 C C   . LEU A 1 1313 ? 170.492 186.210 206.225 1.00 83.45  ? 1296 LEU B C   1 
ATOM   10200 O O   . LEU A 1 1313 ? 171.548 185.588 206.332 1.00 83.45  ? 1296 LEU B O   1 
ATOM   10201 C CB  . LEU A 1 1313 ? 171.046 188.234 204.868 1.00 83.45  ? 1296 LEU B CB  1 
ATOM   10202 C CG  . LEU A 1 1313 ? 170.641 187.439 203.629 1.00 83.45  ? 1296 LEU B CG  1 
ATOM   10203 C CD1 . LEU A 1 1313 ? 169.162 187.628 203.330 1.00 83.45  ? 1296 LEU B CD1 1 
ATOM   10204 C CD2 . LEU A 1 1313 ? 171.490 187.845 202.440 1.00 83.45  ? 1296 LEU B CD2 1 
ATOM   10205 N N   . ALA B 2 92   ? 220.329 194.449 126.804 1.00 64.11  ? 92   ALA A N   1 
ATOM   10206 C CA  . ALA B 2 92   ? 218.977 194.136 127.246 1.00 64.11  ? 92   ALA A CA  1 
ATOM   10207 C C   . ALA B 2 92   ? 218.207 193.391 126.168 1.00 64.11  ? 92   ALA A C   1 
ATOM   10208 O O   . ALA B 2 92   ? 217.285 192.635 126.465 1.00 64.11  ? 92   ALA A O   1 
ATOM   10209 C CB  . ALA B 2 92   ? 218.239 195.409 127.636 1.00 64.11  ? 92   ALA A CB  1 
ATOM   10210 N N   . HIS B 2 93   ? 218.590 193.612 124.908 1.00 67.51  ? 93   HIS A N   1 
ATOM   10211 C CA  . HIS B 2 93   ? 217.903 192.955 123.799 1.00 67.51  ? 93   HIS A CA  1 
ATOM   10212 C C   . HIS B 2 93   ? 218.120 191.446 123.826 1.00 67.51  ? 93   HIS A C   1 
ATOM   10213 O O   . HIS B 2 93   ? 217.173 190.673 123.644 1.00 67.51  ? 93   HIS A O   1 
ATOM   10214 C CB  . HIS B 2 93   ? 218.368 193.546 122.469 1.00 67.51  ? 93   HIS A CB  1 
ATOM   10215 C CG  . HIS B 2 93   ? 218.027 194.995 122.300 1.00 67.51  ? 93   HIS A CG  1 
ATOM   10216 N ND1 . HIS B 2 93   ? 216.729 195.441 122.170 1.00 67.51  ? 93   HIS A ND1 1 
ATOM   10217 C CD2 . HIS B 2 93   ? 218.812 196.095 122.241 1.00 67.51  ? 93   HIS A CD2 1 
ATOM   10218 C CE1 . HIS B 2 93   ? 216.731 196.755 122.037 1.00 67.51  ? 93   HIS A CE1 1 
ATOM   10219 N NE2 . HIS B 2 93   ? 217.982 197.177 122.078 1.00 67.51  ? 93   HIS A NE2 1 
ATOM   10220 N N   . GLN B 2 94   ? 219.360 191.006 124.055 1.00 63.32  ? 94   GLN A N   1 
ATOM   10221 C CA  . GLN B 2 94   ? 219.631 189.571 124.083 1.00 63.32  ? 94   GLN A CA  1 
ATOM   10222 C C   . GLN B 2 94   ? 218.961 188.903 125.278 1.00 63.32  ? 94   GLN A C   1 
ATOM   10223 O O   . GLN B 2 94   ? 218.425 187.793 125.156 1.00 63.32  ? 94   GLN A O   1 
ATOM   10224 C CB  . GLN B 2 94   ? 221.140 189.320 124.090 1.00 63.32  ? 94   GLN A CB  1 
ATOM   10225 C CG  . GLN B 2 94   ? 221.919 190.140 125.104 1.00 63.32  ? 94   GLN A CG  1 
ATOM   10226 C CD  . GLN B 2 94   ? 223.366 189.699 125.212 1.00 63.32  ? 94   GLN A CD  1 
ATOM   10227 O OE1 . GLN B 2 94   ? 223.833 188.862 124.438 1.00 63.32  ? 94   GLN A OE1 1 
ATOM   10228 N NE2 . GLN B 2 94   ? 224.083 190.260 126.177 1.00 63.32  ? 94   GLN A NE2 1 
ATOM   10229 N N   . TYR B 2 95   ? 218.983 189.559 126.441 1.00 56.96  ? 95   TYR A N   1 
ATOM   10230 C CA  . TYR B 2 95   ? 218.292 189.020 127.608 1.00 56.96  ? 95   TYR A CA  1 
ATOM   10231 C C   . TYR B 2 95   ? 216.792 188.935 127.364 1.00 56.96  ? 95   TYR A C   1 
ATOM   10232 O O   . TYR B 2 95   ? 216.150 187.938 127.720 1.00 56.96  ? 95   TYR A O   1 
ATOM   10233 C CB  . TYR B 2 95   ? 218.600 189.877 128.836 1.00 56.96  ? 95   TYR A CB  1 
ATOM   10234 C CG  . TYR B 2 95   ? 217.609 189.758 129.977 1.00 56.96  ? 95   TYR A CG  1 
ATOM   10235 C CD1 . TYR B 2 95   ? 216.483 190.571 130.036 1.00 56.96  ? 95   TYR A CD1 1 
ATOM   10236 C CD2 . TYR B 2 95   ? 217.821 188.862 131.011 1.00 56.96  ? 95   TYR A CD2 1 
ATOM   10237 C CE1 . TYR B 2 95   ? 215.585 190.469 131.079 1.00 56.96  ? 95   TYR A CE1 1 
ATOM   10238 C CE2 . TYR B 2 95   ? 216.930 188.756 132.059 1.00 56.96  ? 95   TYR A CE2 1 
ATOM   10239 C CZ  . TYR B 2 95   ? 215.814 189.563 132.086 1.00 56.96  ? 95   TYR A CZ  1 
ATOM   10240 O OH  . TYR B 2 95   ? 214.923 189.463 133.129 1.00 56.96  ? 95   TYR A OH  1 
ATOM   10241 N N   . GLU B 2 96   ? 216.212 189.970 126.755 1.00 59.74  ? 96   GLU A N   1 
ATOM   10242 C CA  . GLU B 2 96   ? 214.788 189.943 126.449 1.00 59.74  ? 96   GLU A CA  1 
ATOM   10243 C C   . GLU B 2 96   ? 214.462 188.824 125.468 1.00 59.74  ? 96   GLU A C   1 
ATOM   10244 O O   . GLU B 2 96   ? 213.454 188.127 125.621 1.00 59.74  ? 96   GLU A O   1 
ATOM   10245 C CB  . GLU B 2 96   ? 214.347 191.299 125.898 1.00 59.74  ? 96   GLU A CB  1 
ATOM   10246 C CG  . GLU B 2 96   ? 213.254 191.228 124.844 1.00 59.74  ? 96   GLU A CG  1 
ATOM   10247 C CD  . GLU B 2 96   ? 211.883 190.998 125.445 1.00 59.74  ? 96   GLU A CD  1 
ATOM   10248 O OE1 . GLU B 2 96   ? 211.764 191.033 126.688 1.00 59.74  ? 96   GLU A OE1 1 
ATOM   10249 O OE2 . GLU B 2 96   ? 210.924 190.782 124.675 1.00 59.74  ? 96   GLU A OE2 1 
ATOM   10250 N N   . THR B 2 97   ? 215.313 188.629 124.460 1.00 61.07  ? 97   THR A N   1 
ATOM   10251 C CA  . THR B 2 97   ? 215.076 187.576 123.479 1.00 61.07  ? 97   THR A CA  1 
ATOM   10252 C C   . THR B 2 97   ? 215.157 186.194 124.112 1.00 61.07  ? 97   THR A C   1 
ATOM   10253 O O   . THR B 2 97   ? 214.322 185.326 123.830 1.00 61.07  ? 97   THR A O   1 
ATOM   10254 C CB  . THR B 2 97   ? 216.075 187.696 122.328 1.00 61.07  ? 97   THR A CB  1 
ATOM   10255 O OG1 . THR B 2 97   ? 216.113 189.053 121.866 1.00 61.07  ? 97   THR A OG1 1 
ATOM   10256 C CG2 . THR B 2 97   ? 215.672 186.788 121.178 1.00 61.07  ? 97   THR A CG2 1 
ATOM   10257 N N   . ILE B 2 98   ? 216.157 185.960 124.968 1.00 59.76  ? 98   ILE A N   1 
ATOM   10258 C CA  . ILE B 2 98   ? 216.274 184.647 125.593 1.00 59.76  ? 98   ILE A CA  1 
ATOM   10259 C C   . ILE B 2 98   ? 215.131 184.416 126.577 1.00 59.76  ? 98   ILE A C   1 
ATOM   10260 O O   . ILE B 2 98   ? 214.637 183.288 126.708 1.00 59.76  ? 98   ILE A O   1 
ATOM   10261 C CB  . ILE B 2 98   ? 217.655 184.464 126.252 1.00 59.76  ? 98   ILE A CB  1 
ATOM   10262 C CG1 . ILE B 2 98   ? 217.860 183.006 126.671 1.00 59.76  ? 98   ILE A CG1 1 
ATOM   10263 C CG2 . ILE B 2 98   ? 217.828 185.376 127.446 1.00 59.76  ? 98   ILE A CG2 1 
ATOM   10264 C CD1 . ILE B 2 98   ? 217.473 181.998 125.611 1.00 59.76  ? 98   ILE A CD1 1 
ATOM   10265 N N   . MET B 2 99   ? 214.678 185.464 127.271 1.00 57.46  ? 99   MET A N   1 
ATOM   10266 C CA  . MET B 2 99   ? 213.523 185.313 128.151 1.00 57.46  ? 99   MET A CA  1 
ATOM   10267 C C   . MET B 2 99   ? 212.260 185.022 127.354 1.00 57.46  ? 99   MET A C   1 
ATOM   10268 O O   . MET B 2 99   ? 211.407 184.242 127.791 1.00 57.46  ? 99   MET A O   1 
ATOM   10269 C CB  . MET B 2 99   ? 213.347 186.566 129.008 1.00 57.46  ? 99   MET A CB  1 
ATOM   10270 C CG  . MET B 2 99   ? 212.254 186.446 130.055 1.00 57.46  ? 99   MET A CG  1 
ATOM   10271 S SD  . MET B 2 99   ? 212.687 185.301 131.377 1.00 57.46  ? 99   MET A SD  1 
ATOM   10272 C CE  . MET B 2 99   ? 214.378 185.782 131.710 1.00 57.46  ? 99   MET A CE  1 
ATOM   10273 N N   . ASP B 2 100  ? 212.119 185.645 126.181 1.00 59.99  ? 100  ASP A N   1 
ATOM   10274 C CA  . ASP B 2 100  ? 210.988 185.348 125.310 1.00 59.99  ? 100  ASP A CA  1 
ATOM   10275 C C   . ASP B 2 100  ? 211.029 183.904 124.830 1.00 59.99  ? 100  ASP A C   1 
ATOM   10276 O O   . ASP B 2 100  ? 209.997 183.223 124.792 1.00 59.99  ? 100  ASP A O   1 
ATOM   10277 C CB  . ASP B 2 100  ? 210.982 186.311 124.121 1.00 59.99  ? 100  ASP A CB  1 
ATOM   10278 C CG  . ASP B 2 100  ? 209.649 186.346 123.408 1.00 59.99  ? 100  ASP A CG  1 
ATOM   10279 O OD1 . ASP B 2 100  ? 208.653 186.767 124.031 1.00 59.99  ? 100  ASP A OD1 1 
ATOM   10280 O OD2 . ASP B 2 100  ? 209.597 185.950 122.225 1.00 59.99  ? 100  ASP A OD2 1 
ATOM   10281 N N   . GLU B 2 101  ? 212.214 183.420 124.452 1.00 61.60  ? 101  GLU A N   1 
ATOM   10282 C CA  . GLU B 2 101  ? 212.341 182.031 124.026 1.00 61.60  ? 101  GLU A CA  1 
ATOM   10283 C C   . GLU B 2 101  ? 212.059 181.066 125.168 1.00 61.60  ? 101  GLU A C   1 
ATOM   10284 O O   . GLU B 2 101  ? 211.549 179.964 124.934 1.00 61.60  ? 101  GLU A O   1 
ATOM   10285 C CB  . GLU B 2 101  ? 213.731 181.774 123.448 1.00 61.60  ? 101  GLU A CB  1 
ATOM   10286 C CG  . GLU B 2 101  ? 213.769 180.669 122.403 1.00 61.60  ? 101  GLU A CG  1 
ATOM   10287 C CD  . GLU B 2 101  ? 214.182 179.324 122.971 1.00 61.60  ? 101  GLU A CD  1 
ATOM   10288 O OE1 . GLU B 2 101  ? 214.168 179.165 124.209 1.00 61.60  ? 101  GLU A OE1 1 
ATOM   10289 O OE2 . GLU B 2 101  ? 214.521 178.421 122.176 1.00 61.60  ? 101  GLU A OE2 1 
ATOM   10290 N N   . CYS B 2 102  ? 212.388 181.454 126.403 1.00 57.39  ? 102  CYS A N   1 
ATOM   10291 C CA  . CYS B 2 102  ? 212.114 180.588 127.546 1.00 57.39  ? 102  CYS A CA  1 
ATOM   10292 C C   . CYS B 2 102  ? 210.621 180.321 127.693 1.00 57.39  ? 102  CYS A C   1 
ATOM   10293 O O   . CYS B 2 102  ? 210.208 179.187 127.964 1.00 57.39  ? 102  CYS A O   1 
ATOM   10294 C CB  . CYS B 2 102  ? 212.679 181.207 128.824 1.00 57.39  ? 102  CYS A CB  1 
ATOM   10295 S SG  . CYS B 2 102  ? 214.469 181.044 129.005 1.00 57.39  ? 102  CYS A SG  1 
ATOM   10296 N N   . GLY B 2 103  ? 209.796 181.349 127.515 1.00 52.07  ? 103  GLY A N   1 
ATOM   10297 C CA  . GLY B 2 103  ? 208.361 181.175 127.560 1.00 52.07  ? 103  GLY A CA  1 
ATOM   10298 C C   . GLY B 2 103  ? 207.825 181.013 128.971 1.00 52.07  ? 103  GLY A C   1 
ATOM   10299 O O   . GLY B 2 103  ? 208.526 181.192 129.970 1.00 52.07  ? 103  GLY A O   1 
ATOM   10300 N N   . HIS B 2 104  ? 206.546 180.659 129.040 1.00 43.48  ? 104  HIS A N   1 
ATOM   10301 C CA  . HIS B 2 104  ? 205.833 180.501 130.298 1.00 43.48  ? 104  HIS A CA  1 
ATOM   10302 C C   . HIS B 2 104  ? 205.519 179.030 130.529 1.00 43.48  ? 104  HIS A C   1 
ATOM   10303 O O   . HIS B 2 104  ? 204.970 178.362 129.646 1.00 43.48  ? 104  HIS A O   1 
ATOM   10304 C CB  . HIS B 2 104  ? 204.544 181.322 130.304 1.00 43.48  ? 104  HIS A CB  1 
ATOM   10305 C CG  . HIS B 2 104  ? 203.963 181.516 131.669 1.00 43.48  ? 104  HIS A CG  1 
ATOM   10306 N ND1 . HIS B 2 104  ? 204.665 182.106 132.698 1.00 43.48  ? 104  HIS A ND1 1 
ATOM   10307 C CD2 . HIS B 2 104  ? 202.751 181.190 132.176 1.00 43.48  ? 104  HIS A CD2 1 
ATOM   10308 C CE1 . HIS B 2 104  ? 203.907 182.138 133.779 1.00 43.48  ? 104  HIS A CE1 1 
ATOM   10309 N NE2 . HIS B 2 104  ? 202.743 181.587 133.491 1.00 43.48  ? 104  HIS A NE2 1 
ATOM   10310 N N   . GLY B 2 105  ? 205.858 178.529 131.717 1.00 42.92  ? 105  GLY A N   1 
ATOM   10311 C CA  . GLY B 2 105  ? 205.650 177.129 132.024 1.00 42.92  ? 105  GLY A CA  1 
ATOM   10312 C C   . GLY B 2 105  ? 205.593 176.801 133.502 1.00 42.92  ? 105  GLY A C   1 
ATOM   10313 O O   . GLY B 2 105  ? 205.001 177.545 134.288 1.00 42.92  ? 105  GLY A O   1 
ATOM   10314 N N   . ARG B 2 106  ? 206.204 175.677 133.882 1.00 43.98  ? 106  ARG A N   1 
ATOM   10315 C CA  . ARG B 2 106  ? 206.127 175.200 135.260 1.00 43.98  ? 106  ARG A CA  1 
ATOM   10316 C C   . ARG B 2 106  ? 206.813 176.158 136.227 1.00 43.98  ? 106  ARG A C   1 
ATOM   10317 O O   . ARG B 2 106  ? 206.266 176.487 137.290 1.00 43.98  ? 106  ARG A O   1 
ATOM   10318 C CB  . ARG B 2 106  ? 206.760 173.809 135.361 1.00 43.98  ? 106  ARG A CB  1 
ATOM   10319 C CG  . ARG B 2 106  ? 206.128 172.899 136.397 1.00 43.98  ? 106  ARG A CG  1 
ATOM   10320 C CD  . ARG B 2 106  ? 207.065 171.757 136.757 1.00 43.98  ? 106  ARG A CD  1 
ATOM   10321 N NE  . ARG B 2 106  ? 206.869 170.577 135.923 1.00 43.98  ? 106  ARG A NE  1 
ATOM   10322 C CZ  . ARG B 2 106  ? 207.268 169.356 136.251 1.00 43.98  ? 106  ARG A CZ  1 
ATOM   10323 N NH1 . ARG B 2 106  ? 207.890 169.115 137.394 1.00 43.98  ? 106  ARG A NH1 1 
ATOM   10324 N NH2 . ARG B 2 106  ? 207.042 168.351 135.409 1.00 43.98  ? 106  ARG A NH2 1 
ATOM   10325 N N   . PHE B 2 107  ? 208.013 176.618 135.871 1.00 39.88  ? 107  PHE A N   1 
ATOM   10326 C CA  . PHE B 2 107  ? 208.837 177.349 136.828 1.00 39.88  ? 107  PHE A CA  1 
ATOM   10327 C C   . PHE B 2 107  ? 208.204 178.673 137.227 1.00 39.88  ? 107  PHE A C   1 
ATOM   10328 O O   . PHE B 2 107  ? 208.177 179.025 138.414 1.00 39.88  ? 107  PHE A O   1 
ATOM   10329 C CB  . PHE B 2 107  ? 210.228 177.590 136.256 1.00 39.88  ? 107  PHE A CB  1 
ATOM   10330 C CG  . PHE B 2 107  ? 211.080 178.444 137.132 1.00 39.88  ? 107  PHE A CG  1 
ATOM   10331 C CD1 . PHE B 2 107  ? 211.303 178.094 138.449 1.00 39.88  ? 107  PHE A CD1 1 
ATOM   10332 C CD2 . PHE B 2 107  ? 211.624 179.616 136.650 1.00 39.88  ? 107  PHE A CD2 1 
ATOM   10333 C CE1 . PHE B 2 107  ? 212.074 178.887 139.258 1.00 39.88  ? 107  PHE A CE1 1 
ATOM   10334 C CE2 . PHE B 2 107  ? 212.393 180.412 137.458 1.00 39.88  ? 107  PHE A CE2 1 
ATOM   10335 C CZ  . PHE B 2 107  ? 212.618 180.046 138.763 1.00 39.88  ? 107  PHE A CZ  1 
ATOM   10336 N N   . GLN B 2 108  ? 207.715 179.435 136.249 1.00 38.49  ? 108  GLN A N   1 
ATOM   10337 C CA  . GLN B 2 108  ? 207.119 180.721 136.579 1.00 38.49  ? 108  GLN A CA  1 
ATOM   10338 C C   . GLN B 2 108  ? 205.853 180.555 137.403 1.00 38.49  ? 108  GLN A C   1 
ATOM   10339 O O   . GLN B 2 108  ? 205.573 181.386 138.270 1.00 38.49  ? 108  GLN A O   1 
ATOM   10340 C CB  . GLN B 2 108  ? 206.847 181.512 135.304 1.00 38.49  ? 108  GLN A CB  1 
ATOM   10341 C CG  . GLN B 2 108  ? 208.039 182.322 134.837 1.00 38.49  ? 108  GLN A CG  1 
ATOM   10342 C CD  . GLN B 2 108  ? 208.449 181.989 133.421 1.00 38.49  ? 108  GLN A CD  1 
ATOM   10343 O OE1 . GLN B 2 108  ? 207.682 181.396 132.667 1.00 38.49  ? 108  GLN A OE1 1 
ATOM   10344 N NE2 . GLN B 2 108  ? 209.665 182.368 133.052 1.00 38.49  ? 108  GLN A NE2 1 
ATOM   10345 N N   . TRP B 2 109  ? 205.097 179.474 137.187 1.00 38.92  ? 109  TRP A N   1 
ATOM   10346 C CA  . TRP B 2 109  ? 203.917 179.228 138.011 1.00 38.92  ? 109  TRP A CA  1 
ATOM   10347 C C   . TRP B 2 109  ? 204.303 178.893 139.446 1.00 38.92  ? 109  TRP A C   1 
ATOM   10348 O O   . TRP B 2 109  ? 203.680 179.387 140.396 1.00 38.92  ? 109  TRP A O   1 
ATOM   10349 C CB  . TRP B 2 109  ? 203.075 178.103 137.415 1.00 38.92  ? 109  TRP A CB  1 
ATOM   10350 C CG  . TRP B 2 109  ? 202.191 178.510 136.271 1.00 38.92  ? 109  TRP A CG  1 
ATOM   10351 C CD1 . TRP B 2 109  ? 201.957 177.795 135.137 1.00 38.92  ? 109  TRP A CD1 1 
ATOM   10352 C CD2 . TRP B 2 109  ? 201.411 179.711 136.155 1.00 38.92  ? 109  TRP A CD2 1 
ATOM   10353 N NE1 . TRP B 2 109  ? 201.091 178.470 134.316 1.00 38.92  ? 109  TRP A NE1 1 
ATOM   10354 C CE2 . TRP B 2 109  ? 200.739 179.650 134.919 1.00 38.92  ? 109  TRP A CE2 1 
ATOM   10355 C CE3 . TRP B 2 109  ? 201.214 180.829 136.972 1.00 38.92  ? 109  TRP A CE3 1 
ATOM   10356 C CZ2 . TRP B 2 109  ? 199.889 180.662 134.482 1.00 38.92  ? 109  TRP A CZ2 1 
ATOM   10357 C CZ3 . TRP B 2 109  ? 200.373 181.832 136.533 1.00 38.92  ? 109  TRP A CZ3 1 
ATOM   10358 C CH2 . TRP B 2 109  ? 199.723 181.741 135.301 1.00 38.92  ? 109  TRP A CH2 1 
ATOM   10359 N N   . ILE B 2 110  ? 205.317 178.046 139.627 1.00 34.51  ? 110  ILE A N   1 
ATOM   10360 C CA  . ILE B 2 110  ? 205.749 177.710 140.981 1.00 34.51  ? 110  ILE A CA  1 
ATOM   10361 C C   . ILE B 2 110  ? 206.234 178.959 141.705 1.00 34.51  ? 110  ILE A C   1 
ATOM   10362 O O   . ILE B 2 110  ? 205.888 179.201 142.873 1.00 34.51  ? 110  ILE A O   1 
ATOM   10363 C CB  . ILE B 2 110  ? 206.829 176.616 140.940 1.00 34.51  ? 110  ILE A CB  1 
ATOM   10364 C CG1 . ILE B 2 110  ? 206.272 175.348 140.289 1.00 34.51  ? 110  ILE A CG1 1 
ATOM   10365 C CG2 . ILE B 2 110  ? 207.326 176.306 142.337 1.00 34.51  ? 110  ILE A CG2 1 
ATOM   10366 C CD1 . ILE B 2 110  ? 207.319 174.494 139.618 1.00 34.51  ? 110  ILE A CD1 1 
ATOM   10367 N N   . LEU B 2 111  ? 207.025 179.785 141.017 1.00 33.32  ? 111  LEU A N   1 
ATOM   10368 C CA  . LEU B 2 111  ? 207.476 181.038 141.611 1.00 33.32  ? 111  LEU A CA  1 
ATOM   10369 C C   . LEU B 2 111  ? 206.302 181.957 141.918 1.00 33.32  ? 111  LEU A C   1 
ATOM   10370 O O   . LEU B 2 111  ? 206.292 182.645 142.946 1.00 33.32  ? 111  LEU A O   1 
ATOM   10371 C CB  . LEU B 2 111  ? 208.467 181.732 140.680 1.00 33.32  ? 111  LEU A CB  1 
ATOM   10372 C CG  . LEU B 2 111  ? 209.145 182.966 141.261 1.00 33.32  ? 111  LEU A CG  1 
ATOM   10373 C CD1 . LEU B 2 111  ? 210.269 182.557 142.185 1.00 33.32  ? 111  LEU A CD1 1 
ATOM   10374 C CD2 . LEU B 2 111  ? 209.659 183.847 140.150 1.00 33.32  ? 111  LEU A CD2 1 
ATOM   10375 N N   . PHE B 2 112  ? 205.302 181.983 141.037 1.00 33.00  ? 112  PHE A N   1 
ATOM   10376 C CA  . PHE B 2 112  ? 204.129 182.818 141.259 1.00 33.00  ? 112  PHE A CA  1 
ATOM   10377 C C   . PHE B 2 112  ? 203.408 182.407 142.530 1.00 33.00  ? 112  PHE A C   1 
ATOM   10378 O O   . PHE B 2 112  ? 202.940 183.260 143.288 1.00 33.00  ? 112  PHE A O   1 
ATOM   10379 C CB  . PHE B 2 112  ? 203.202 182.737 140.053 1.00 33.00  ? 112  PHE A CB  1 
ATOM   10380 C CG  . PHE B 2 112  ? 201.778 183.077 140.359 1.00 33.00  ? 112  PHE A CG  1 
ATOM   10381 C CD1 . PHE B 2 112  ? 201.377 184.395 140.456 1.00 33.00  ? 112  PHE A CD1 1 
ATOM   10382 C CD2 . PHE B 2 112  ? 200.835 182.080 140.528 1.00 33.00  ? 112  PHE A CD2 1 
ATOM   10383 C CE1 . PHE B 2 112  ? 200.063 184.710 140.729 1.00 33.00  ? 112  PHE A CE1 1 
ATOM   10384 C CE2 . PHE B 2 112  ? 199.520 182.391 140.802 1.00 33.00  ? 112  PHE A CE2 1 
ATOM   10385 C CZ  . PHE B 2 112  ? 199.135 183.709 140.902 1.00 33.00  ? 112  PHE A CZ  1 
ATOM   10386 N N   . PHE B 2 113  ? 203.311 181.104 142.786 1.00 33.95  ? 113  PHE A N   1 
ATOM   10387 C CA  . PHE B 2 113  ? 202.692 180.650 144.029 1.00 33.95  ? 113  PHE A CA  1 
ATOM   10388 C C   . PHE B 2 113  ? 203.531 181.043 145.244 1.00 33.95  ? 113  PHE A C   1 
ATOM   10389 O O   . PHE B 2 113  ? 203.007 181.581 146.232 1.00 33.95  ? 113  PHE A O   1 
ATOM   10390 C CB  . PHE B 2 113  ? 202.466 179.140 143.991 1.00 33.95  ? 113  PHE A CB  1 
ATOM   10391 C CG  . PHE B 2 113  ? 201.100 178.746 143.514 1.00 33.95  ? 113  PHE A CG  1 
ATOM   10392 C CD1 . PHE B 2 113  ? 200.680 179.069 142.234 1.00 33.95  ? 113  PHE A CD1 1 
ATOM   10393 C CD2 . PHE B 2 113  ? 200.231 178.067 144.347 1.00 33.95  ? 113  PHE A CD2 1 
ATOM   10394 C CE1 . PHE B 2 113  ? 199.423 178.714 141.795 1.00 33.95  ? 113  PHE A CE1 1 
ATOM   10395 C CE2 . PHE B 2 113  ? 198.972 177.710 143.913 1.00 33.95  ? 113  PHE A CE2 1 
ATOM   10396 C CZ  . PHE B 2 113  ? 198.568 178.033 142.636 1.00 33.95  ? 113  PHE A CZ  1 
ATOM   10397 N N   . VAL B 2 114  ? 204.842 180.785 145.192 1.00 31.52  ? 114  VAL A N   1 
ATOM   10398 C CA  . VAL B 2 114  ? 205.685 181.090 146.348 1.00 31.52  ? 114  VAL A CA  1 
ATOM   10399 C C   . VAL B 2 114  ? 205.850 182.584 146.581 1.00 31.52  ? 114  VAL A C   1 
ATOM   10400 O O   . VAL B 2 114  ? 206.371 182.982 147.629 1.00 31.52  ? 114  VAL A O   1 
ATOM   10401 C CB  . VAL B 2 114  ? 207.077 180.440 146.233 1.00 31.52  ? 114  VAL A CB  1 
ATOM   10402 C CG1 . VAL B 2 114  ? 206.957 179.006 145.764 1.00 31.52  ? 114  VAL A CG1 1 
ATOM   10403 C CG2 . VAL B 2 114  ? 207.964 181.240 145.308 1.00 31.52  ? 114  VAL A CG2 1 
ATOM   10404 N N   . LEU B 2 115  ? 205.432 183.422 145.633 1.00 31.08  ? 115  LEU A N   1 
ATOM   10405 C CA  . LEU B 2 115  ? 205.393 184.865 145.850 1.00 31.08  ? 115  LEU A CA  1 
ATOM   10406 C C   . LEU B 2 115  ? 204.010 185.357 146.265 1.00 31.08  ? 115  LEU A C   1 
ATOM   10407 O O   . LEU B 2 115  ? 203.895 186.297 147.067 1.00 31.08  ? 115  LEU A O   1 
ATOM   10408 C CB  . LEU B 2 115  ? 205.849 185.591 144.583 1.00 31.08  ? 115  LEU A CB  1 
ATOM   10409 C CG  . LEU B 2 115  ? 207.298 185.359 144.162 1.00 31.08  ? 115  LEU A CG  1 
ATOM   10410 C CD1 . LEU B 2 115  ? 207.559 185.971 142.805 1.00 31.08  ? 115  LEU A CD1 1 
ATOM   10411 C CD2 . LEU B 2 115  ? 208.262 185.913 145.196 1.00 31.08  ? 115  LEU A CD2 1 
ATOM   10412 N N   . GLY B 2 116  ? 202.955 184.740 145.734 1.00 34.01  ? 116  GLY A N   1 
ATOM   10413 C CA  . GLY B 2 116  ? 201.627 185.014 146.235 1.00 34.01  ? 116  GLY A CA  1 
ATOM   10414 C C   . GLY B 2 116  ? 201.493 184.677 147.702 1.00 34.01  ? 116  GLY A C   1 
ATOM   10415 O O   . GLY B 2 116  ? 200.652 185.246 148.396 1.00 34.01  ? 116  GLY A O   1 
ATOM   10416 N N   . LEU B 2 117  ? 202.326 183.760 148.197 1.00 34.89  ? 117  LEU A N   1 
ATOM   10417 C CA  . LEU B 2 117  ? 202.376 183.537 149.640 1.00 34.89  ? 117  LEU A CA  1 
ATOM   10418 C C   . LEU B 2 117  ? 202.783 184.809 150.384 1.00 34.89  ? 117  LEU A C   1 
ATOM   10419 O O   . LEU B 2 117  ? 202.153 185.189 151.380 1.00 34.89  ? 117  LEU A O   1 
ATOM   10420 C CB  . LEU B 2 117  ? 203.346 182.402 149.958 1.00 34.89  ? 117  LEU A CB  1 
ATOM   10421 C CG  . LEU B 2 117  ? 202.831 180.982 149.737 1.00 34.89  ? 117  LEU A CG  1 
ATOM   10422 C CD1 . LEU B 2 117  ? 203.626 180.008 150.573 1.00 34.89  ? 117  LEU A CD1 1 
ATOM   10423 C CD2 . LEU B 2 117  ? 201.354 180.876 150.046 1.00 34.89  ? 117  LEU A CD2 1 
ATOM   10424 N N   . ALA B 2 118  ? 203.829 185.488 149.910 1.00 35.00  ? 118  ALA A N   1 
ATOM   10425 C CA  . ALA B 2 118  ? 204.261 186.723 150.559 1.00 35.00  ? 118  ALA A CA  1 
ATOM   10426 C C   . ALA B 2 118  ? 203.214 187.819 150.412 1.00 35.00  ? 118  ALA A C   1 
ATOM   10427 O O   . ALA B 2 118  ? 203.006 188.620 151.334 1.00 35.00  ? 118  ALA A O   1 
ATOM   10428 C CB  . ALA B 2 118  ? 205.600 187.178 149.983 1.00 35.00  ? 118  ALA A CB  1 
ATOM   10429 N N   . LEU B 2 119  ? 202.554 187.883 149.257 1.00 35.07  ? 119  LEU A N   1 
ATOM   10430 C CA  . LEU B 2 119  ? 201.482 188.863 149.098 1.00 35.07  ? 119  LEU A CA  1 
ATOM   10431 C C   . LEU B 2 119  ? 200.323 188.574 150.056 1.00 35.07  ? 119  LEU A C   1 
ATOM   10432 O O   . LEU B 2 119  ? 199.712 189.501 150.606 1.00 35.07  ? 119  LEU A O   1 
ATOM   10433 C CB  . LEU B 2 119  ? 201.001 188.902 147.649 1.00 35.07  ? 119  LEU A CB  1 
ATOM   10434 C CG  . LEU B 2 119  ? 201.732 189.951 146.815 1.00 35.07  ? 119  LEU A CG  1 
ATOM   10435 C CD1 . LEU B 2 119  ? 201.393 189.812 145.347 1.00 35.07  ? 119  LEU A CD1 1 
ATOM   10436 C CD2 . LEU B 2 119  ? 201.391 191.341 147.308 1.00 35.07  ? 119  LEU A CD2 1 
ATOM   10437 N N   . MET B 2 120  ? 200.016 187.294 150.272 1.00 35.14  ? 120  MET A N   1 
ATOM   10438 C CA  . MET B 2 120  ? 199.059 186.918 151.304 1.00 35.14  ? 120  MET A CA  1 
ATOM   10439 C C   . MET B 2 120  ? 199.509 187.396 152.673 1.00 35.14  ? 120  MET A C   1 
ATOM   10440 O O   . MET B 2 120  ? 198.685 187.856 153.470 1.00 35.14  ? 120  MET A O   1 
ATOM   10441 C CB  . MET B 2 120  ? 198.863 185.401 151.318 1.00 35.14  ? 120  MET A CB  1 
ATOM   10442 C CG  . MET B 2 120  ? 197.570 184.957 151.967 1.00 35.14  ? 120  MET A CG  1 
ATOM   10443 S SD  . MET B 2 120  ? 196.935 183.359 151.440 1.00 35.14  ? 120  MET A SD  1 
ATOM   10444 C CE  . MET B 2 120  ? 198.451 182.441 151.266 1.00 35.14  ? 120  MET A CE  1 
ATOM   10445 N N   . ALA B 2 121  ? 200.803 187.276 152.968 1.00 38.33  ? 121  ALA A N   1 
ATOM   10446 C CA  . ALA B 2 121  ? 201.308 187.765 154.247 1.00 38.33  ? 121  ALA A CA  1 
ATOM   10447 C C   . ALA B 2 121  ? 201.083 189.266 154.385 1.00 38.33  ? 121  ALA A C   1 
ATOM   10448 O O   . ALA B 2 121  ? 200.690 189.748 155.456 1.00 38.33  ? 121  ALA A O   1 
ATOM   10449 C CB  . ALA B 2 121  ? 202.788 187.424 154.398 1.00 38.33  ? 121  ALA A CB  1 
ATOM   10450 N N   . ASP B 2 122  ? 201.319 190.017 153.309 1.00 37.00  ? 122  ASP A N   1 
ATOM   10451 C CA  . ASP B 2 122  ? 201.059 191.456 153.345 1.00 37.00  ? 122  ASP A CA  1 
ATOM   10452 C C   . ASP B 2 122  ? 199.581 191.740 153.604 1.00 37.00  ? 122  ASP A C   1 
ATOM   10453 O O   . ASP B 2 122  ? 199.231 192.626 154.396 1.00 37.00  ? 122  ASP A O   1 
ATOM   10454 C CB  . ASP B 2 122  ? 201.511 192.105 152.035 1.00 37.00  ? 122  ASP A CB  1 
ATOM   10455 C CG  . ASP B 2 122  ? 201.644 193.610 152.147 1.00 37.00  ? 122  ASP A CG  1 
ATOM   10456 O OD1 . ASP B 2 122  ? 200.622 194.285 152.386 1.00 37.00  ? 122  ASP A OD1 1 
ATOM   10457 O OD2 . ASP B 2 122  ? 202.772 194.123 151.993 1.00 37.00  ? 122  ASP A OD2 1 
ATOM   10458 N N   . GLY B 2 123  ? 198.700 190.995 152.938 1.00 37.41  ? 123  GLY A N   1 
ATOM   10459 C CA  . GLY B 2 123  ? 197.273 191.196 153.141 1.00 37.41  ? 123  GLY A CA  1 
ATOM   10460 C C   . GLY B 2 123  ? 196.848 190.929 154.573 1.00 37.41  ? 123  GLY A C   1 
ATOM   10461 O O   . GLY B 2 123  ? 196.100 191.711 155.172 1.00 37.41  ? 123  GLY A O   1 
ATOM   10462 N N   . VAL B 2 124  ? 197.315 189.815 155.144 1.00 38.25  ? 124  VAL A N   1 
ATOM   10463 C CA  . VAL B 2 124  ? 196.956 189.499 156.520 1.00 38.25  ? 124  VAL A CA  1 
ATOM   10464 C C   . VAL B 2 124  ? 197.566 190.494 157.494 1.00 38.25  ? 124  VAL A C   1 
ATOM   10465 O O   . VAL B 2 124  ? 196.982 190.757 158.547 1.00 38.25  ? 124  VAL A O   1 
ATOM   10466 C CB  . VAL B 2 124  ? 197.336 188.047 156.899 1.00 38.25  ? 124  VAL A CB  1 
ATOM   10467 C CG1 . VAL B 2 124  ? 196.898 187.080 155.819 1.00 38.25  ? 124  VAL A CG1 1 
ATOM   10468 C CG2 . VAL B 2 124  ? 198.823 187.918 157.168 1.00 38.25  ? 124  VAL A CG2 1 
ATOM   10469 N N   . GLU B 2 125  ? 198.718 191.083 157.163 1.00 40.54  ? 125  GLU A N   1 
ATOM   10470 C CA  . GLU B 2 125  ? 199.244 192.147 158.008 1.00 40.54  ? 125  GLU A CA  1 
ATOM   10471 C C   . GLU B 2 125  ? 198.341 193.373 157.982 1.00 40.54  ? 125  GLU A C   1 
ATOM   10472 O O   . GLU B 2 125  ? 198.053 193.958 159.033 1.00 40.54  ? 125  GLU A O   1 
ATOM   10473 C CB  . GLU B 2 125  ? 200.659 192.517 157.567 1.00 40.54  ? 125  GLU A CB  1 
ATOM   10474 C CG  . GLU B 2 125  ? 201.771 191.850 158.362 1.00 40.54  ? 125  GLU A CG  1 
ATOM   10475 C CD  . GLU B 2 125  ? 201.452 191.649 159.833 1.00 40.54  ? 125  GLU A CD  1 
ATOM   10476 O OE1 . GLU B 2 125  ? 201.813 190.583 160.371 1.00 40.54  ? 125  GLU A OE1 1 
ATOM   10477 O OE2 . GLU B 2 125  ? 200.915 192.579 160.473 1.00 40.54  ? 125  GLU A OE2 1 
ATOM   10478 N N   . VAL B 2 126  ? 197.872 193.758 156.793 1.00 38.94  ? 126  VAL A N   1 
ATOM   10479 C CA  . VAL B 2 126  ? 196.964 194.899 156.713 1.00 38.94  ? 126  VAL A CA  1 
ATOM   10480 C C   . VAL B 2 126  ? 195.698 194.626 157.515 1.00 38.94  ? 126  VAL A C   1 
ATOM   10481 O O   . VAL B 2 126  ? 195.222 195.497 158.257 1.00 38.94  ? 126  VAL A O   1 
ATOM   10482 C CB  . VAL B 2 126  ? 196.645 195.235 155.247 1.00 38.94  ? 126  VAL A CB  1 
ATOM   10483 C CG1 . VAL B 2 126  ? 195.440 196.150 155.162 1.00 38.94  ? 126  VAL A CG1 1 
ATOM   10484 C CG2 . VAL B 2 126  ? 197.846 195.885 154.586 1.00 38.94  ? 126  VAL A CG2 1 
ATOM   10485 N N   . PHE B 2 127  ? 195.146 193.415 157.404 1.00 38.12  ? 127  PHE A N   1 
ATOM   10486 C CA  . PHE B 2 127  ? 193.963 193.074 158.192 1.00 38.12  ? 127  PHE A CA  1 
ATOM   10487 C C   . PHE B 2 127  ? 194.247 193.140 159.688 1.00 38.12  ? 127  PHE A C   1 
ATOM   10488 O O   . PHE B 2 127  ? 193.509 193.782 160.441 1.00 38.12  ? 127  PHE A O   1 
ATOM   10489 C CB  . PHE B 2 127  ? 193.451 191.684 157.825 1.00 38.12  ? 127  PHE A CB  1 
ATOM   10490 C CG  . PHE B 2 127  ? 192.219 191.286 158.590 1.00 38.12  ? 127  PHE A CG  1 
ATOM   10491 C CD1 . PHE B 2 127  ? 191.005 191.909 158.354 1.00 38.12  ? 127  PHE A CD1 1 
ATOM   10492 C CD2 . PHE B 2 127  ? 192.286 190.311 159.568 1.00 38.12  ? 127  PHE A CD2 1 
ATOM   10493 C CE1 . PHE B 2 127  ? 189.879 191.546 159.065 1.00 38.12  ? 127  PHE A CE1 1 
ATOM   10494 C CE2 . PHE B 2 127  ? 191.164 189.947 160.281 1.00 38.12  ? 127  PHE A CE2 1 
ATOM   10495 C CZ  . PHE B 2 127  ? 189.960 190.565 160.031 1.00 38.12  ? 127  PHE A CZ  1 
ATOM   10496 N N   . VAL B 2 128  ? 195.307 192.470 160.141 1.00 39.97  ? 128  VAL A N   1 
ATOM   10497 C CA  . VAL B 2 128  ? 195.575 192.390 161.571 1.00 39.97  ? 128  VAL A CA  1 
ATOM   10498 C C   . VAL B 2 128  ? 195.932 193.748 162.151 1.00 39.97  ? 128  VAL A C   1 
ATOM   10499 O O   . VAL B 2 128  ? 195.858 193.937 163.367 1.00 39.97  ? 128  VAL A O   1 
ATOM   10500 C CB  . VAL B 2 128  ? 196.686 191.360 161.854 1.00 39.97  ? 128  VAL A CB  1 
ATOM   10501 C CG1 . VAL B 2 128  ? 198.045 192.000 161.705 1.00 39.97  ? 128  VAL A CG1 1 
ATOM   10502 C CG2 . VAL B 2 128  ? 196.519 190.771 163.242 1.00 39.97  ? 128  VAL A CG2 1 
ATOM   10503 N N   . VAL B 2 129  ? 196.322 194.708 161.310 1.00 40.23  ? 129  VAL A N   1 
ATOM   10504 C CA  . VAL B 2 129  ? 196.574 196.058 161.799 1.00 40.23  ? 129  VAL A CA  1 
ATOM   10505 C C   . VAL B 2 129  ? 195.328 196.933 161.767 1.00 40.23  ? 129  VAL A C   1 
ATOM   10506 O O   . VAL B 2 129  ? 195.169 197.797 162.644 1.00 40.23  ? 129  VAL A O   1 
ATOM   10507 C CB  . VAL B 2 129  ? 197.710 196.733 161.003 1.00 40.23  ? 129  VAL A CB  1 
ATOM   10508 C CG1 . VAL B 2 129  ? 197.811 198.200 161.359 1.00 40.23  ? 129  VAL A CG1 1 
ATOM   10509 C CG2 . VAL B 2 129  ? 199.024 196.029 161.264 1.00 40.23  ? 129  VAL A CG2 1 
ATOM   10510 N N   . SER B 2 130  ? 194.414 196.708 160.822 1.00 40.82  ? 130  SER A N   1 
ATOM   10511 C CA  . SER B 2 130  ? 193.291 197.616 160.650 1.00 40.82  ? 130  SER A CA  1 
ATOM   10512 C C   . SER B 2 130  ? 191.985 197.141 161.269 1.00 40.82  ? 130  SER A C   1 
ATOM   10513 O O   . SER B 2 130  ? 191.102 197.974 161.499 1.00 40.82  ? 130  SER A O   1 
ATOM   10514 C CB  . SER B 2 130  ? 193.058 197.887 159.157 1.00 40.82  ? 130  SER A CB  1 
ATOM   10515 O OG  . SER B 2 130  ? 192.167 198.970 158.976 1.00 40.82  ? 130  SER A OG  1 
ATOM   10516 N N   . PHE B 2 131  ? 191.827 195.843 161.549 1.00 41.96  ? 131  PHE A N   1 
ATOM   10517 C CA  . PHE B 2 131  ? 190.577 195.342 162.108 1.00 41.96  ? 131  PHE A CA  1 
ATOM   10518 C C   . PHE B 2 131  ? 190.777 194.405 163.295 1.00 41.96  ? 131  PHE A C   1 
ATOM   10519 O O   . PHE B 2 131  ? 189.784 193.904 163.835 1.00 41.96  ? 131  PHE A O   1 
ATOM   10520 C CB  . PHE B 2 131  ? 189.747 194.607 161.045 1.00 41.96  ? 131  PHE A CB  1 
ATOM   10521 C CG  . PHE B 2 131  ? 189.244 195.487 159.940 1.00 41.96  ? 131  PHE A CG  1 
ATOM   10522 C CD1 . PHE B 2 131  ? 190.094 195.943 158.948 1.00 41.96  ? 131  PHE A CD1 1 
ATOM   10523 C CD2 . PHE B 2 131  ? 187.905 195.828 159.872 1.00 41.96  ? 131  PHE A CD2 1 
ATOM   10524 C CE1 . PHE B 2 131  ? 189.629 196.743 157.931 1.00 41.96  ? 131  PHE A CE1 1 
ATOM   10525 C CE2 . PHE B 2 131  ? 187.432 196.627 158.856 1.00 41.96  ? 131  PHE A CE2 1 
ATOM   10526 C CZ  . PHE B 2 131  ? 188.293 197.084 157.882 1.00 41.96  ? 131  PHE A CZ  1 
ATOM   10527 N N   . ALA B 2 132  ? 192.013 194.142 163.714 1.00 45.81  ? 132  ALA A N   1 
ATOM   10528 C CA  . ALA B 2 132  ? 192.257 193.249 164.846 1.00 45.81  ? 132  ALA A CA  1 
ATOM   10529 C C   . ALA B 2 132  ? 192.798 194.032 166.034 1.00 45.81  ? 132  ALA A C   1 
ATOM   10530 O O   . ALA B 2 132  ? 192.212 193.968 167.118 1.00 45.81  ? 132  ALA A O   1 
ATOM   10531 C CB  . ALA B 2 132  ? 193.203 192.122 164.438 1.00 45.81  ? 132  ALA A CB  1 
ATOM   10532 N N   . LEU B 2 133  ? 193.893 194.762 165.871 1.00 48.81  ? 133  LEU A N   1 
ATOM   10533 C CA  . LEU B 2 133  ? 194.405 195.631 166.923 1.00 48.81  ? 133  LEU A CA  1 
ATOM   10534 C C   . LEU B 2 133  ? 193.384 196.700 167.314 1.00 48.81  ? 133  LEU A C   1 
ATOM   10535 O O   . LEU B 2 133  ? 193.150 196.898 168.512 1.00 48.81  ? 133  LEU A O   1 
ATOM   10536 C CB  . LEU B 2 133  ? 195.726 196.273 166.493 1.00 48.81  ? 133  LEU A CB  1 
ATOM   10537 C CG  . LEU B 2 133  ? 196.935 195.343 166.412 1.00 48.81  ? 133  LEU A CG  1 
ATOM   10538 C CD1 . LEU B 2 133  ? 198.227 196.141 166.440 1.00 48.81  ? 133  LEU A CD1 1 
ATOM   10539 C CD2 . LEU B 2 133  ? 196.906 194.329 167.540 1.00 48.81  ? 133  LEU A CD2 1 
ATOM   10540 N N   . PRO B 2 134  ? 192.757 197.411 166.365 1.00 49.90  ? 134  PRO A N   1 
ATOM   10541 C CA  . PRO B 2 134  ? 191.782 198.437 166.769 1.00 49.90  ? 134  PRO A CA  1 
ATOM   10542 C C   . PRO B 2 134  ? 190.580 197.888 167.510 1.00 49.90  ? 134  PRO A C   1 
ATOM   10543 O O   . PRO B 2 134  ? 189.917 198.647 168.229 1.00 49.90  ? 134  PRO A O   1 
ATOM   10544 C CB  . PRO B 2 134  ? 191.370 199.073 165.434 1.00 49.90  ? 134  PRO A CB  1 
ATOM   10545 C CG  . PRO B 2 134  ? 192.515 198.822 164.538 1.00 49.90  ? 134  PRO A CG  1 
ATOM   10546 C CD  . PRO B 2 134  ? 192.976 197.449 164.910 1.00 49.90  ? 134  PRO A CD  1 
ATOM   10547 N N   . SER B 2 135  ? 190.328 196.582 167.396 1.00 51.82  ? 135  SER A N   1 
ATOM   10548 C CA  . SER B 2 135  ? 189.224 195.950 168.165 1.00 51.82  ? 135  SER A CA  1 
ATOM   10549 C C   . SER B 2 135  ? 189.806 195.219 169.380 1.00 51.82  ? 135  SER A C   1 
ATOM   10550 O O   . SER B 2 135  ? 189.016 194.759 170.226 1.00 51.82  ? 135  SER A O   1 
ATOM   10551 C CB  . SER B 2 135  ? 188.427 195.018 167.297 1.00 51.82  ? 135  SER A CB  1 
ATOM   10552 O OG  . SER B 2 135  ? 189.255 193.990 166.775 1.00 51.82  ? 135  SER A OG  1 
ATOM   10553 N N   . ALA B 2 136  ? 191.136 195.111 169.454 1.00 55.92  ? 136  ALA A N   1 
ATOM   10554 C CA  . ALA B 2 136  ? 191.797 194.456 170.604 1.00 55.92  ? 136  ALA A CA  1 
ATOM   10555 C C   . ALA B 2 136  ? 191.830 195.415 171.795 1.00 55.92  ? 136  ALA A C   1 
ATOM   10556 O O   . ALA B 2 136  ? 191.711 194.940 172.940 1.00 55.92  ? 136  ALA A O   1 
ATOM   10557 C CB  . ALA B 2 136  ? 193.191 194.064 170.214 1.00 55.92  ? 136  ALA A CB  1 
ATOM   10558 N N   . GLU B 2 137  ? 191.986 196.714 171.530 1.00 61.55  ? 137  GLU A N   1 
ATOM   10559 C CA  . GLU B 2 137  ? 192.103 197.715 172.623 1.00 61.55  ? 137  GLU A CA  1 
ATOM   10560 C C   . GLU B 2 137  ? 190.719 197.992 173.214 1.00 61.55  ? 137  GLU A C   1 
ATOM   10561 O O   . GLU B 2 137  ? 190.623 198.877 174.082 1.00 61.55  ? 137  GLU A O   1 
ATOM   10562 C CB  . GLU B 2 137  ? 192.725 198.996 172.071 1.00 61.55  ? 137  GLU A CB  1 
ATOM   10563 C CG  . GLU B 2 137  ? 193.928 198.725 171.187 1.00 61.55  ? 137  GLU A CG  1 
ATOM   10564 C CD  . GLU B 2 137  ? 194.330 199.860 170.263 1.00 61.55  ? 137  GLU A CD  1 
ATOM   10565 O OE1 . GLU B 2 137  ? 193.689 200.927 170.324 1.00 61.55  ? 137  GLU A OE1 1 
ATOM   10566 O OE2 . GLU B 2 137  ? 195.279 199.669 169.476 1.00 61.55  ? 137  GLU A OE2 1 
ATOM   10567 N N   . LYS B 2 138  ? 189.696 197.266 172.761 1.00 64.55  ? 138  LYS A N   1 
ATOM   10568 C CA  . LYS B 2 138  ? 188.307 197.504 173.235 1.00 64.55  ? 138  LYS A CA  1 
ATOM   10569 C C   . LYS B 2 138  ? 188.156 197.008 174.677 1.00 64.55  ? 138  LYS A C   1 
ATOM   10570 O O   . LYS B 2 138  ? 189.063 196.305 175.157 1.00 64.55  ? 138  LYS A O   1 
ATOM   10571 C CB  . LYS B 2 138  ? 187.311 196.828 172.291 1.00 64.55  ? 138  LYS A CB  1 
ATOM   10572 C CG  . LYS B 2 138  ? 187.127 197.523 170.949 1.00 64.55  ? 138  LYS A CG  1 
ATOM   10573 C CD  . LYS B 2 138  ? 186.122 196.839 170.050 1.00 64.55  ? 138  LYS A CD  1 
ATOM   10574 C CE  . LYS B 2 138  ? 185.976 197.509 168.701 1.00 64.55  ? 138  LYS A CE  1 
ATOM   10575 N NZ  . LYS B 2 138  ? 185.142 196.704 167.779 1.00 64.55  ? 138  LYS A NZ  1 
ATOM   10576 N N   . ASP B 2 139  ? 187.065 197.389 175.348 1.00 72.41  ? 139  ASP A N   1 
ATOM   10577 C CA  . ASP B 2 139  ? 186.846 196.993 176.765 1.00 72.41  ? 139  ASP A CA  1 
ATOM   10578 C C   . ASP B 2 139  ? 185.832 195.851 176.813 1.00 72.41  ? 139  ASP A C   1 
ATOM   10579 O O   . ASP B 2 139  ? 184.622 196.135 176.782 1.00 72.41  ? 139  ASP A O   1 
ATOM   10580 C CB  . ASP B 2 139  ? 186.390 198.177 177.616 1.00 72.41  ? 139  ASP A CB  1 
ATOM   10581 C CG  . ASP B 2 139  ? 186.187 197.815 179.077 1.00 72.41  ? 139  ASP A CG  1 
ATOM   10582 O OD1 . ASP B 2 139  ? 187.162 197.364 179.709 1.00 72.41  ? 139  ASP A OD1 1 
ATOM   10583 O OD2 . ASP B 2 139  ? 185.056 197.986 179.571 1.00 72.41  ? 139  ASP A OD2 1 
ATOM   10584 N N   . MET B 2 140  ? 186.315 194.613 176.895 1.00 76.63  ? 140  MET A N   1 
ATOM   10585 C CA  . MET B 2 140  ? 185.416 193.432 176.891 1.00 76.63  ? 140  MET A CA  1 
ATOM   10586 C C   . MET B 2 140  ? 184.332 193.656 177.944 1.00 76.63  ? 140  MET A C   1 
ATOM   10587 O O   . MET B 2 140  ? 183.174 193.278 177.689 1.00 76.63  ? 140  MET A O   1 
ATOM   10588 C CB  . MET B 2 140  ? 186.194 192.161 177.243 1.00 76.63  ? 140  MET A CB  1 
ATOM   10589 C CG  . MET B 2 140  ? 187.408 192.422 178.111 1.00 76.63  ? 140  MET A CG  1 
ATOM   10590 S SD  . MET B 2 140  ? 188.287 190.901 178.540 1.00 76.63  ? 140  MET A SD  1 
ATOM   10591 C CE  . MET B 2 140  ? 186.937 189.722 178.508 1.00 76.63  ? 140  MET A CE  1 
ATOM   10592 N N   . CYS B 2 141  ? 184.699 194.270 179.070 1.00 75.21  ? 141  CYS A N   1 
ATOM   10593 C CA  . CYS B 2 141  ? 183.730 194.496 180.173 1.00 75.21  ? 141  CYS A CA  1 
ATOM   10594 C C   . CYS B 2 141  ? 182.540 195.315 179.670 1.00 75.21  ? 141  CYS A C   1 
ATOM   10595 O O   . CYS B 2 141  ? 181.392 194.900 179.917 1.00 75.21  ? 141  CYS A O   1 
ATOM   10596 C CB  . CYS B 2 141  ? 184.424 195.201 181.329 1.00 75.21  ? 141  CYS A CB  1 
ATOM   10597 S SG  . CYS B 2 141  ? 185.158 193.997 182.460 1.00 75.21  ? 141  CYS A SG  1 
ATOM   10598 N N   . LEU B 2 142  ? 182.808 196.419 178.974 1.00 69.32  ? 142  LEU A N   1 
ATOM   10599 C CA  . LEU B 2 142  ? 181.692 197.204 178.390 1.00 69.32  ? 142  LEU A CA  1 
ATOM   10600 C C   . LEU B 2 142  ? 181.079 196.389 177.250 1.00 69.32  ? 142  LEU A C   1 
ATOM   10601 O O   . LEU B 2 142  ? 181.747 196.232 176.212 1.00 69.32  ? 142  LEU A O   1 
ATOM   10602 C CB  . LEU B 2 142  ? 182.225 198.551 177.895 1.00 69.32  ? 142  LEU A CB  1 
ATOM   10603 C CG  . LEU B 2 142  ? 182.248 199.665 178.937 1.00 69.32  ? 142  LEU A CG  1 
ATOM   10604 C CD1 . LEU B 2 142  ? 182.533 201.007 178.282 1.00 69.32  ? 142  LEU A CD1 1 
ATOM   10605 C CD2 . LEU B 2 142  ? 180.932 199.715 179.698 1.00 69.32  ? 142  LEU A CD2 1 
ATOM   10606 N N   . SER B 2 143  ? 179.847 195.913 177.434 1.00 64.17  ? 143  SER A N   1 
ATOM   10607 C CA  . SER B 2 143  ? 179.151 195.152 176.367 1.00 64.17  ? 143  SER A CA  1 
ATOM   10608 C C   . SER B 2 143  ? 179.074 196.001 175.096 1.00 64.17  ? 143  SER A C   1 
ATOM   10609 O O   . SER B 2 143  ? 178.810 195.425 174.026 1.00 64.17  ? 143  SER A O   1 
ATOM   10610 C CB  . SER B 2 143  ? 177.787 194.735 176.827 1.00 64.17  ? 143  SER A CB  1 
ATOM   10611 O OG  . SER B 2 143  ? 176.957 195.870 177.022 1.00 64.17  ? 143  SER A OG  1 
ATOM   10612 N N   . SER B 2 144  ? 179.266 197.318 175.210 1.00 65.70  ? 144  SER A N   1 
ATOM   10613 C CA  . SER B 2 144  ? 179.295 198.203 174.015 1.00 65.70  ? 144  SER A CA  1 
ATOM   10614 C C   . SER B 2 144  ? 180.524 199.110 174.106 1.00 65.70  ? 144  SER A C   1 
ATOM   10615 O O   . SER B 2 144  ? 180.695 199.747 175.160 1.00 65.70  ? 144  SER A O   1 
ATOM   10616 C CB  . SER B 2 144  ? 178.027 198.998 173.909 1.00 65.70  ? 144  SER A CB  1 
ATOM   10617 O OG  . SER B 2 144  ? 177.788 199.708 175.114 1.00 65.70  ? 144  SER A OG  1 
ATOM   10618 N N   . SER B 2 145  ? 181.345 199.169 173.052 1.00 65.48  ? 145  SER A N   1 
ATOM   10619 C CA  . SER B 2 145  ? 182.611 199.947 173.125 1.00 65.48  ? 145  SER A CA  1 
ATOM   10620 C C   . SER B 2 145  ? 182.870 200.703 171.817 1.00 65.48  ? 145  SER A C   1 
ATOM   10621 O O   . SER B 2 145  ? 182.203 200.389 170.815 1.00 65.48  ? 145  SER A O   1 
ATOM   10622 C CB  . SER B 2 145  ? 183.769 199.044 173.463 1.00 65.48  ? 145  SER A CB  1 
ATOM   10623 O OG  . SER B 2 145  ? 183.536 198.352 174.680 1.00 65.48  ? 145  SER A OG  1 
ATOM   10624 N N   . LYS B 2 146  ? 183.804 201.661 171.840 1.00 62.87  ? 146  LYS A N   1 
ATOM   10625 C CA  . LYS B 2 146  ? 184.135 202.463 170.632 1.00 62.87  ? 146  LYS A CA  1 
ATOM   10626 C C   . LYS B 2 146  ? 185.296 201.805 169.881 1.00 62.87  ? 146  LYS A C   1 
ATOM   10627 O O   . LYS B 2 146  ? 185.399 200.566 169.925 1.00 62.87  ? 146  LYS A O   1 
ATOM   10628 C CB  . LYS B 2 146  ? 184.503 203.895 171.027 1.00 62.87  ? 146  LYS A CB  1 
ATOM   10629 C CG  . LYS B 2 146  ? 183.322 204.801 171.342 1.00 62.87  ? 146  LYS A CG  1 
ATOM   10630 C CD  . LYS B 2 146  ? 182.341 204.919 170.194 1.00 62.87  ? 146  LYS A CD  1 
ATOM   10631 C CE  . LYS B 2 146  ? 182.964 205.469 168.928 1.00 62.87  ? 146  LYS A CE  1 
ATOM   10632 N NZ  . LYS B 2 146  ? 183.485 206.843 169.120 1.00 62.87  ? 146  LYS A NZ  1 
ATOM   10633 N N   . LYS B 2 147  ? 186.132 202.610 169.218 1.00 56.05  ? 147  LYS A N   1 
ATOM   10634 C CA  . LYS B 2 147  ? 187.258 202.050 168.425 1.00 56.05  ? 147  LYS A CA  1 
ATOM   10635 C C   . LYS B 2 147  ? 188.487 202.956 168.546 1.00 56.05  ? 147  LYS A C   1 
ATOM   10636 O O   . LYS B 2 147  ? 188.403 204.113 168.094 1.00 56.05  ? 147  LYS A O   1 
ATOM   10637 C CB  . LYS B 2 147  ? 186.849 201.911 166.957 1.00 56.05  ? 147  LYS A CB  1 
ATOM   10638 C CG  . LYS B 2 147  ? 187.836 201.144 166.089 1.00 56.05  ? 147  LYS A CG  1 
ATOM   10639 C CD  . LYS B 2 147  ? 187.556 201.296 164.614 1.00 56.05  ? 147  LYS A CD  1 
ATOM   10640 C CE  . LYS B 2 147  ? 187.494 202.749 164.195 1.00 56.05  ? 147  LYS A CE  1 
ATOM   10641 N NZ  . LYS B 2 147  ? 187.375 202.890 162.725 1.00 56.05  ? 147  LYS A NZ  1 
ATOM   10642 N N   . GLY B 2 148  ? 189.582 202.449 169.122 1.00 56.78  ? 148  GLY A N   1 
ATOM   10643 C CA  . GLY B 2 148  ? 190.836 203.227 169.206 1.00 56.78  ? 148  GLY A CA  1 
ATOM   10644 C C   . GLY B 2 148  ? 191.813 202.793 168.126 1.00 56.78  ? 148  GLY A C   1 
ATOM   10645 O O   . GLY B 2 148  ? 191.589 201.716 167.540 1.00 56.78  ? 148  GLY A O   1 
ATOM   10646 N N   . MET B 2 149  ? 192.858 203.584 167.866 1.00 55.14  ? 149  MET A N   1 
ATOM   10647 C CA  . MET B 2 149  ? 193.794 203.257 166.756 1.00 55.14  ? 149  MET A CA  1 
ATOM   10648 C C   . MET B 2 149  ? 195.238 203.237 167.267 1.00 55.14  ? 149  MET A C   1 
ATOM   10649 O O   . MET B 2 149  ? 196.139 203.584 166.485 1.00 55.14  ? 149  MET A O   1 
ATOM   10650 C CB  . MET B 2 149  ? 193.671 204.293 165.635 1.00 55.14  ? 149  MET A CB  1 
ATOM   10651 C CG  . MET B 2 149  ? 192.326 204.260 164.936 1.00 55.14  ? 149  MET A CG  1 
ATOM   10652 S SD  . MET B 2 149  ? 191.839 202.581 164.473 1.00 55.14  ? 149  MET A SD  1 
ATOM   10653 C CE  . MET B 2 149  ? 190.648 202.927 163.181 1.00 55.14  ? 149  MET A CE  1 
ATOM   10654 N N   . LEU B 2 150  ? 195.453 202.842 168.524 1.00 54.29  ? 150  LEU A N   1 
ATOM   10655 C CA  . LEU B 2 150  ? 196.823 202.876 169.108 1.00 54.29  ? 150  LEU A CA  1 
ATOM   10656 C C   . LEU B 2 150  ? 197.752 202.012 168.249 1.00 54.29  ? 150  LEU A C   1 
ATOM   10657 O O   . LEU B 2 150  ? 198.834 202.503 167.874 1.00 54.29  ? 150  LEU A O   1 
ATOM   10658 C CB  . LEU B 2 150  ? 196.758 202.345 170.544 1.00 54.29  ? 150  LEU A CB  1 
ATOM   10659 C CG  . LEU B 2 150  ? 197.732 202.954 171.552 1.00 54.29  ? 150  LEU A CG  1 
ATOM   10660 C CD1 . LEU B 2 150  ? 197.819 202.090 172.800 1.00 54.29  ? 150  LEU A CD1 1 
ATOM   10661 C CD2 . LEU B 2 150  ? 199.114 203.156 170.952 1.00 54.29  ? 150  LEU A CD2 1 
ATOM   10662 N N   . GLY B 2 151  ? 197.334 200.787 167.930 1.00 51.04  ? 151  GLY A N   1 
ATOM   10663 C CA  . GLY B 2 151  ? 198.203 199.869 167.170 1.00 51.04  ? 151  GLY A CA  1 
ATOM   10664 C C   . GLY B 2 151  ? 198.616 200.454 165.834 1.00 51.04  ? 151  GLY A C   1 
ATOM   10665 O O   . GLY B 2 151  ? 199.719 200.120 165.379 1.00 51.04  ? 151  GLY A O   1 
ATOM   10666 N N   . MET B 2 152  ? 197.798 201.333 165.249 1.00 48.67  ? 152  MET A N   1 
ATOM   10667 C CA  . MET B 2 152  ? 198.081 201.884 163.895 1.00 48.67  ? 152  MET A CA  1 
ATOM   10668 C C   . MET B 2 152  ? 199.571 202.213 163.740 1.00 48.67  ? 152  MET A C   1 
ATOM   10669 O O   . MET B 2 152  ? 200.081 202.028 162.635 1.00 48.67  ? 152  MET A O   1 
ATOM   10670 C CB  . MET B 2 152  ? 197.275 203.162 163.655 1.00 48.67  ? 152  MET A CB  1 
ATOM   10671 C CG  . MET B 2 152  ? 195.867 202.909 163.154 1.00 48.67  ? 152  MET A CG  1 
ATOM   10672 S SD  . MET B 2 152  ? 195.764 202.801 161.351 1.00 48.67  ? 152  MET A SD  1 
ATOM   10673 C CE  . MET B 2 152  ? 195.051 204.403 160.983 1.00 48.67  ? 152  MET A CE  1 
ATOM   10674 N N   . ILE B 2 153  ? 200.229 202.708 164.790 1.00 50.19  ? 153  ILE A N   1 
ATOM   10675 C CA  . ILE B 2 153  ? 201.660 203.134 164.684 1.00 50.19  ? 153  ILE A CA  1 
ATOM   10676 C C   . ILE B 2 153  ? 202.478 202.095 163.904 1.00 50.19  ? 153  ILE A C   1 
ATOM   10677 O O   . ILE B 2 153  ? 203.426 202.496 163.219 1.00 50.19  ? 153  ILE A O   1 
ATOM   10678 C CB  . ILE B 2 153  ? 202.252 203.402 166.083 1.00 50.19  ? 153  ILE A CB  1 
ATOM   10679 C CG1 . ILE B 2 153  ? 202.160 202.168 166.984 1.00 50.19  ? 153  ILE A CG1 1 
ATOM   10680 C CG2 . ILE B 2 153  ? 201.594 204.616 166.721 1.00 50.19  ? 153  ILE A CG2 1 
ATOM   10681 C CD1 . ILE B 2 153  ? 202.754 202.366 168.358 1.00 50.19  ? 153  ILE A CD1 1 
ATOM   10682 N N   . VAL B 2 154  ? 202.153 200.810 164.025 1.00 46.57  ? 154  VAL A N   1 
ATOM   10683 C CA  . VAL B 2 154  ? 202.855 199.774 163.272 1.00 46.57  ? 154  VAL A CA  1 
ATOM   10684 C C   . VAL B 2 154  ? 202.833 200.097 161.783 1.00 46.57  ? 154  VAL A C   1 
ATOM   10685 O O   . VAL B 2 154  ? 203.806 199.839 161.062 1.00 46.57  ? 154  VAL A O   1 
ATOM   10686 C CB  . VAL B 2 154  ? 202.261 198.381 163.564 1.00 46.57  ? 154  VAL A CB  1 
ATOM   10687 C CG1 . VAL B 2 154  ? 200.784 198.360 163.289 1.00 46.57  ? 154  VAL A CG1 1 
ATOM   10688 C CG2 . VAL B 2 154  ? 202.957 197.325 162.726 1.00 46.57  ? 154  VAL A CG2 1 
ATOM   10689 N N   . TYR B 2 155  ? 201.731 200.678 161.302 1.00 44.40  ? 155  TYR A N   1 
ATOM   10690 C CA  . TYR B 2 155  ? 201.690 201.206 159.941 1.00 44.40  ? 155  TYR A CA  1 
ATOM   10691 C C   . TYR B 2 155  ? 202.871 202.128 159.678 1.00 44.40  ? 155  TYR A C   1 
ATOM   10692 O O   . TYR B 2 155  ? 203.563 201.997 158.662 1.00 44.40  ? 155  TYR A O   1 
ATOM   10693 C CB  . TYR B 2 155  ? 200.374 201.941 159.713 1.00 44.40  ? 155  TYR A CB  1 
ATOM   10694 C CG  . TYR B 2 155  ? 199.332 201.175 158.938 1.00 44.40  ? 155  TYR A CG  1 
ATOM   10695 C CD1 . TYR B 2 155  ? 199.396 199.798 158.818 1.00 44.40  ? 155  TYR A CD1 1 
ATOM   10696 C CD2 . TYR B 2 155  ? 198.263 201.834 158.352 1.00 44.40  ? 155  TYR A CD2 1 
ATOM   10697 C CE1 . TYR B 2 155  ? 198.436 199.100 158.108 1.00 44.40  ? 155  TYR A CE1 1 
ATOM   10698 C CE2 . TYR B 2 155  ? 197.296 201.148 157.650 1.00 44.40  ? 155  TYR A CE2 1 
ATOM   10699 C CZ  . TYR B 2 155  ? 197.387 199.782 157.530 1.00 44.40  ? 155  TYR A CZ  1 
ATOM   10700 O OH  . TYR B 2 155  ? 196.423 199.099 156.828 1.00 44.40  ? 155  TYR A OH  1 
ATOM   10701 N N   . LEU B 2 156  ? 203.129 203.059 160.602 1.00 47.62  ? 156  LEU A N   1 
ATOM   10702 C CA  . LEU B 2 156  ? 204.299 203.919 160.468 1.00 47.62  ? 156  LEU A CA  1 
ATOM   10703 C C   . LEU B 2 156  ? 205.562 203.087 160.319 1.00 47.62  ? 156  LEU A C   1 
ATOM   10704 O O   . LEU B 2 156  ? 206.396 203.358 159.445 1.00 47.62  ? 156  LEU A O   1 
ATOM   10705 C CB  . LEU B 2 156  ? 204.411 204.851 161.671 1.00 47.62  ? 156  LEU A CB  1 
ATOM   10706 C CG  . LEU B 2 156  ? 203.354 205.948 161.786 1.00 47.62  ? 156  LEU A CG  1 
ATOM   10707 C CD1 . LEU B 2 156  ? 203.169 206.364 163.237 1.00 47.62  ? 156  LEU A CD1 1 
ATOM   10708 C CD2 . LEU B 2 156  ? 203.736 207.138 160.920 1.00 47.62  ? 156  LEU A CD2 1 
ATOM   10709 N N   . GLY B 2 157  ? 205.703 202.047 161.143 1.00 46.98  ? 157  GLY A N   1 
ATOM   10710 C CA  . GLY B 2 157  ? 206.832 201.147 160.995 1.00 46.98  ? 157  GLY A CA  1 
ATOM   10711 C C   . GLY B 2 157  ? 206.910 200.548 159.605 1.00 46.98  ? 157  GLY A C   1 
ATOM   10712 O O   . GLY B 2 157  ? 207.981 200.520 158.993 1.00 46.98  ? 157  GLY A O   1 
ATOM   10713 N N   . MET B 2 158  ? 205.769 200.099 159.073 1.00 45.36  ? 158  MET A N   1 
ATOM   10714 C CA  . MET B 2 158  ? 205.752 199.580 157.711 1.00 45.36  ? 158  MET A CA  1 
ATOM   10715 C C   . MET B 2 158  ? 206.396 200.572 156.761 1.00 45.36  ? 158  MET A C   1 
ATOM   10716 O O   . MET B 2 158  ? 207.211 200.195 155.907 1.00 45.36  ? 158  MET A O   1 
ATOM   10717 C CB  . MET B 2 158  ? 204.317 199.281 157.280 1.00 45.36  ? 158  MET A CB  1 
ATOM   10718 C CG  . MET B 2 158  ? 203.877 197.848 157.514 1.00 45.36  ? 158  MET A CG  1 
ATOM   10719 S SD  . MET B 2 158  ? 202.299 197.482 156.723 1.00 45.36  ? 158  MET A SD  1 
ATOM   10720 C CE  . MET B 2 158  ? 201.729 196.108 157.715 1.00 45.36  ? 158  MET A CE  1 
ATOM   10721 N N   . MET B 2 159  ? 206.086 201.860 156.942 1.00 45.47  ? 159  MET A N   1 
ATOM   10722 C CA  . MET B 2 159  ? 206.685 202.910 156.131 1.00 45.47  ? 159  MET A CA  1 
ATOM   10723 C C   . MET B 2 159  ? 208.195 202.748 156.075 1.00 45.47  ? 159  MET A C   1 
ATOM   10724 O O   . MET B 2 159  ? 208.779 202.589 154.994 1.00 45.47  ? 159  MET A O   1 
ATOM   10725 C CB  . MET B 2 159  ? 206.330 204.274 156.714 1.00 45.47  ? 159  MET A CB  1 
ATOM   10726 C CG  . MET B 2 159  ? 206.651 205.450 155.825 1.00 45.47  ? 159  MET A CG  1 
ATOM   10727 S SD  . MET B 2 159  ? 205.805 206.907 156.455 1.00 45.47  ? 159  MET A SD  1 
ATOM   10728 C CE  . MET B 2 159  ? 204.147 206.267 156.581 1.00 45.47  ? 159  MET A CE  1 
ATOM   10729 N N   . ALA B 2 160  ? 208.836 202.722 157.245 1.00 44.58  ? 160  ALA A N   1 
ATOM   10730 C CA  . ALA B 2 160  ? 210.287 202.605 157.283 1.00 44.58  ? 160  ALA A CA  1 
ATOM   10731 C C   . ALA B 2 160  ? 210.741 201.345 156.570 1.00 44.58  ? 160  ALA A C   1 
ATOM   10732 O O   . ALA B 2 160  ? 211.680 201.384 155.765 1.00 44.58  ? 160  ALA A O   1 
ATOM   10733 C CB  . ALA B 2 160  ? 210.776 202.616 158.730 1.00 44.58  ? 160  ALA A CB  1 
ATOM   10734 N N   . GLY B 2 161  ? 210.050 200.227 156.809 1.00 44.14  ? 161  GLY A N   1 
ATOM   10735 C CA  . GLY B 2 161  ? 210.413 199.005 156.118 1.00 44.14  ? 161  GLY A CA  1 
ATOM   10736 C C   . GLY B 2 161  ? 210.369 199.189 154.618 1.00 44.14  ? 161  GLY A C   1 
ATOM   10737 O O   . GLY B 2 161  ? 211.332 198.874 153.910 1.00 44.14  ? 161  GLY A O   1 
ATOM   10738 N N   . ALA B 2 162  ? 209.287 199.798 154.125 1.00 41.85  ? 162  ALA A N   1 
ATOM   10739 C CA  . ALA B 2 162  ? 209.132 199.964 152.690 1.00 41.85  ? 162  ALA A CA  1 
ATOM   10740 C C   . ALA B 2 162  ? 210.219 200.844 152.100 1.00 41.85  ? 162  ALA A C   1 
ATOM   10741 O O   . ALA B 2 162  ? 210.431 200.816 150.886 1.00 41.85  ? 162  ALA A O   1 
ATOM   10742 C CB  . ALA B 2 162  ? 207.756 200.547 152.369 1.00 41.85  ? 162  ALA A CB  1 
ATOM   10743 N N   . PHE B 2 163  ? 210.922 201.614 152.928 1.00 43.23  ? 163  PHE A N   1 
ATOM   10744 C CA  . PHE B 2 163  ? 212.054 202.383 152.440 1.00 43.23  ? 163  PHE A CA  1 
ATOM   10745 C C   . PHE B 2 163  ? 213.381 201.744 152.828 1.00 43.23  ? 163  PHE A C   1 
ATOM   10746 O O   . PHE B 2 163  ? 214.373 201.899 152.106 1.00 43.23  ? 163  PHE A O   1 
ATOM   10747 C CB  . PHE B 2 163  ? 211.985 203.817 152.985 1.00 43.23  ? 163  PHE A CB  1 
ATOM   10748 C CG  . PHE B 2 163  ? 212.900 204.795 152.285 1.00 43.23  ? 163  PHE A CG  1 
ATOM   10749 C CD1 . PHE B 2 163  ? 213.556 204.456 151.114 1.00 43.23  ? 163  PHE A CD1 1 
ATOM   10750 C CD2 . PHE B 2 163  ? 213.102 206.058 152.811 1.00 43.23  ? 163  PHE A CD2 1 
ATOM   10751 C CE1 . PHE B 2 163  ? 214.392 205.352 150.481 1.00 43.23  ? 163  PHE A CE1 1 
ATOM   10752 C CE2 . PHE B 2 163  ? 213.937 206.962 152.182 1.00 43.23  ? 163  PHE A CE2 1 
ATOM   10753 C CZ  . PHE B 2 163  ? 214.581 206.609 151.017 1.00 43.23  ? 163  PHE A CZ  1 
ATOM   10754 N N   . ILE B 2 164  ? 213.418 200.989 153.921 1.00 43.10  ? 164  ILE A N   1 
ATOM   10755 C CA  . ILE B 2 164  ? 214.673 200.402 154.380 1.00 43.10  ? 164  ILE A CA  1 
ATOM   10756 C C   . ILE B 2 164  ? 214.937 199.070 153.699 1.00 43.10  ? 164  ILE A C   1 
ATOM   10757 O O   . ILE B 2 164  ? 216.018 198.845 153.150 1.00 43.10  ? 164  ILE A O   1 
ATOM   10758 C CB  . ILE B 2 164  ? 214.666 200.267 155.917 1.00 43.10  ? 164  ILE A CB  1 
ATOM   10759 C CG1 . ILE B 2 164  ? 215.069 201.593 156.562 1.00 43.10  ? 164  ILE A CG1 1 
ATOM   10760 C CG2 . ILE B 2 164  ? 215.597 199.156 156.369 1.00 43.10  ? 164  ILE A CG2 1 
ATOM   10761 C CD1 . ILE B 2 164  ? 216.404 202.120 156.090 1.00 43.10  ? 164  ILE A CD1 1 
ATOM   10762 N N   . LEU B 2 165  ? 213.959 198.172 153.716 1.00 43.17  ? 165  LEU A N   1 
ATOM   10763 C CA  . LEU B 2 165  ? 214.054 196.902 153.013 1.00 43.17  ? 165  LEU A CA  1 
ATOM   10764 C C   . LEU B 2 165  ? 213.524 196.981 151.589 1.00 43.17  ? 165  LEU A C   1 
ATOM   10765 O O   . LEU B 2 165  ? 213.533 195.969 150.884 1.00 43.17  ? 165  LEU A O   1 
ATOM   10766 C CB  . LEU B 2 165  ? 213.300 195.817 153.784 1.00 43.17  ? 165  LEU A CB  1 
ATOM   10767 C CG  . LEU B 2 165  ? 213.693 195.647 155.251 1.00 43.17  ? 165  LEU A CG  1 
ATOM   10768 C CD1 . LEU B 2 165  ? 212.643 194.840 155.995 1.00 43.17  ? 165  LEU A CD1 1 
ATOM   10769 C CD2 . LEU B 2 165  ? 215.058 194.990 155.366 1.00 43.17  ? 165  LEU A CD2 1 
ATOM   10770 N N   . GLY B 2 166  ? 213.055 198.148 151.160 1.00 41.18  ? 166  GLY A N   1 
ATOM   10771 C CA  . GLY B 2 166  ? 212.551 198.307 149.810 1.00 41.18  ? 166  GLY A CA  1 
ATOM   10772 C C   . GLY B 2 166  ? 213.591 198.859 148.862 1.00 41.18  ? 166  GLY A C   1 
ATOM   10773 O O   . GLY B 2 166  ? 213.779 198.334 147.760 1.00 41.18  ? 166  GLY A O   1 
ATOM   10774 N N   . GLY B 2 167  ? 214.274 199.927 149.277 1.00 41.77  ? 167  GLY A N   1 
ATOM   10775 C CA  . GLY B 2 167  ? 215.329 200.491 148.459 1.00 41.77  ? 167  GLY A CA  1 
ATOM   10776 C C   . GLY B 2 167  ? 216.648 199.758 148.550 1.00 41.77  ? 167  GLY A C   1 
ATOM   10777 O O   . GLY B 2 167  ? 217.447 199.823 147.611 1.00 41.77  ? 167  GLY A O   1 
ATOM   10778 N N   . LEU B 2 168  ? 216.892 199.062 149.661 1.00 42.01  ? 168  LEU A N   1 
ATOM   10779 C CA  . LEU B 2 168  ? 218.154 198.353 149.833 1.00 42.01  ? 168  LEU A CA  1 
ATOM   10780 C C   . LEU B 2 168  ? 218.318 197.233 148.818 1.00 42.01  ? 168  LEU A C   1 
ATOM   10781 O O   . LEU B 2 168  ? 219.437 196.970 148.362 1.00 42.01  ? 168  LEU A O   1 
ATOM   10782 C CB  . LEU B 2 168  ? 218.248 197.798 151.253 1.00 42.01  ? 168  LEU A CB  1 
ATOM   10783 C CG  . LEU B 2 168  ? 219.383 196.822 151.554 1.00 42.01  ? 168  LEU A CG  1 
ATOM   10784 C CD1 . LEU B 2 168  ? 220.707 197.552 151.558 1.00 42.01  ? 168  LEU A CD1 1 
ATOM   10785 C CD2 . LEU B 2 168  ? 219.150 196.127 152.883 1.00 42.01  ? 168  LEU A CD2 1 
ATOM   10786 N N   . ALA B 2 169  ? 217.221 196.576 148.440 1.00 42.35  ? 169  ALA A N   1 
ATOM   10787 C CA  . ALA B 2 169  ? 217.317 195.384 147.606 1.00 42.35  ? 169  ALA A CA  1 
ATOM   10788 C C   . ALA B 2 169  ? 217.934 195.690 146.252 1.00 42.35  ? 169  ALA A C   1 
ATOM   10789 O O   . ALA B 2 169  ? 218.630 194.848 145.674 1.00 42.35  ? 169  ALA A O   1 
ATOM   10790 C CB  . ALA B 2 169  ? 215.940 194.754 147.432 1.00 42.35  ? 169  ALA A CB  1 
ATOM   10791 N N   . ASP B 2 170  ? 217.683 196.887 145.719 1.00 41.35  ? 170  ASP A N   1 
ATOM   10792 C CA  . ASP B 2 170  ? 218.252 197.238 144.426 1.00 41.35  ? 170  ASP A CA  1 
ATOM   10793 C C   . ASP B 2 170  ? 219.769 197.346 144.477 1.00 41.35  ? 170  ASP A C   1 
ATOM   10794 O O   . ASP B 2 170  ? 220.421 197.239 143.433 1.00 41.35  ? 170  ASP A O   1 
ATOM   10795 C CB  . ASP B 2 170  ? 217.646 198.546 143.923 1.00 41.35  ? 170  ASP A CB  1 
ATOM   10796 C CG  . ASP B 2 170  ? 217.539 198.588 142.416 1.00 41.35  ? 170  ASP A CG  1 
ATOM   10797 O OD1 . ASP B 2 170  ? 218.535 198.271 141.737 1.00 41.35  ? 170  ASP A OD1 1 
ATOM   10798 O OD2 . ASP B 2 170  ? 216.450 198.929 141.910 1.00 41.35  ? 170  ASP A OD2 1 
ATOM   10799 N N   . LYS B 2 171  ? 220.347 197.548 145.660 1.00 39.87  ? 171  LYS A N   1 
ATOM   10800 C CA  . LYS B 2 171  ? 221.791 197.622 145.817 1.00 39.87  ? 171  LYS A CA  1 
ATOM   10801 C C   . LYS B 2 171  ? 222.404 196.334 146.349 1.00 39.87  ? 171  LYS A C   1 
ATOM   10802 O O   . LYS B 2 171  ? 223.625 196.174 146.274 1.00 39.87  ? 171  LYS A O   1 
ATOM   10803 C CB  . LYS B 2 171  ? 222.156 198.785 146.751 1.00 39.87  ? 171  LYS A CB  1 
ATOM   10804 C CG  . LYS B 2 171  ? 223.540 199.377 146.528 1.00 39.87  ? 171  LYS A CG  1 
ATOM   10805 C CD  . LYS B 2 171  ? 223.899 199.434 145.054 1.00 39.87  ? 171  LYS A CD  1 
ATOM   10806 C CE  . LYS B 2 171  ? 223.278 200.644 144.386 1.00 39.87  ? 171  LYS A CE  1 
ATOM   10807 N NZ  . LYS B 2 171  ? 223.481 200.623 142.912 1.00 39.87  ? 171  LYS A NZ  1 
ATOM   10808 N N   . LEU B 2 172  ? 221.597 195.415 146.872 1.00 43.97  ? 172  LEU A N   1 
ATOM   10809 C CA  . LEU B 2 172  ? 222.107 194.203 147.503 1.00 43.97  ? 172  LEU A CA  1 
ATOM   10810 C C   . LEU B 2 172  ? 221.575 192.920 146.883 1.00 43.97  ? 172  LEU A C   1 
ATOM   10811 O O   . LEU B 2 172  ? 222.335 191.964 146.714 1.00 43.97  ? 172  LEU A O   1 
ATOM   10812 C CB  . LEU B 2 172  ? 221.776 194.217 149.000 1.00 43.97  ? 172  LEU A CB  1 
ATOM   10813 C CG  . LEU B 2 172  ? 222.110 192.953 149.790 1.00 43.97  ? 172  LEU A CG  1 
ATOM   10814 C CD1 . LEU B 2 172  ? 223.614 192.747 149.857 1.00 43.97  ? 172  LEU A CD1 1 
ATOM   10815 C CD2 . LEU B 2 172  ? 221.514 193.032 151.184 1.00 43.97  ? 172  LEU A CD2 1 
ATOM   10816 N N   . GLY B 2 173  ? 220.300 192.866 146.548 1.00 45.40  ? 173  GLY A N   1 
ATOM   10817 C CA  . GLY B 2 173  ? 219.719 191.672 145.966 1.00 45.40  ? 173  GLY A CA  1 
ATOM   10818 C C   . GLY B 2 173  ? 218.248 191.567 146.300 1.00 45.40  ? 173  GLY A C   1 
ATOM   10819 O O   . GLY B 2 173  ? 217.743 192.182 147.238 1.00 45.40  ? 173  GLY A O   1 
ATOM   10820 N N   . ARG B 2 174  ? 217.543 190.755 145.517 1.00 40.70  ? 174  ARG A N   1 
ATOM   10821 C CA  . ARG B 2 174  ? 216.101 190.604 145.659 1.00 40.70  ? 174  ARG A CA  1 
ATOM   10822 C C   . ARG B 2 174  ? 215.714 189.353 146.435 1.00 40.70  ? 174  ARG A C   1 
ATOM   10823 O O   . ARG B 2 174  ? 214.763 189.390 147.221 1.00 40.70  ? 174  ARG A O   1 
ATOM   10824 C CB  . ARG B 2 174  ? 215.438 190.570 144.281 1.00 40.70  ? 174  ARG A CB  1 
ATOM   10825 C CG  . ARG B 2 174  ? 215.645 191.836 143.475 1.00 40.70  ? 174  ARG A CG  1 
ATOM   10826 C CD  . ARG B 2 174  ? 214.397 192.256 142.716 1.00 40.70  ? 174  ARG A CD  1 
ATOM   10827 N NE  . ARG B 2 174  ? 214.622 193.301 141.714 1.00 40.70  ? 174  ARG A NE  1 
ATOM   10828 C CZ  . ARG B 2 174  ? 215.305 194.427 141.885 1.00 40.70  ? 174  ARG A CZ  1 
ATOM   10829 N NH1 . ARG B 2 174  ? 215.808 194.773 143.059 1.00 40.70  ? 174  ARG A NH1 1 
ATOM   10830 N NH2 . ARG B 2 174  ? 215.469 195.244 140.850 1.00 40.70  ? 174  ARG A NH2 1 
ATOM   10831 N N   . LYS B 2 175  ? 216.422 188.241 146.232 1.00 42.48  ? 175  LYS A N   1 
ATOM   10832 C CA  . LYS B 2 175  ? 216.121 187.040 147.001 1.00 42.48  ? 175  LYS A CA  1 
ATOM   10833 C C   . LYS B 2 175  ? 216.619 187.168 148.434 1.00 42.48  ? 175  LYS A C   1 
ATOM   10834 O O   . LYS B 2 175  ? 215.915 186.781 149.374 1.00 42.48  ? 175  LYS A O   1 
ATOM   10835 C CB  . LYS B 2 175  ? 216.732 185.808 146.333 1.00 42.48  ? 175  LYS A CB  1 
ATOM   10836 C CG  . LYS B 2 175  ? 216.318 184.492 146.980 1.00 42.48  ? 175  LYS A CG  1 
ATOM   10837 C CD  . LYS B 2 175  ? 217.322 183.385 146.700 1.00 42.48  ? 175  LYS A CD  1 
ATOM   10838 C CE  . LYS B 2 175  ? 216.980 182.123 147.477 1.00 42.48  ? 175  LYS A CE  1 
ATOM   10839 N NZ  . LYS B 2 175  ? 218.100 181.144 147.464 1.00 42.48  ? 175  LYS A NZ  1 
ATOM   10840 N N   . ARG B 2 176  ? 217.825 187.708 148.622 1.00 44.87  ? 176  ARG A N   1 
ATOM   10841 C CA  . ARG B 2 176  ? 218.367 187.853 149.971 1.00 44.87  ? 176  ARG A CA  1 
ATOM   10842 C C   . ARG B 2 176  ? 217.533 188.816 150.806 1.00 44.87  ? 176  ARG A C   1 
ATOM   10843 O O   . ARG B 2 176  ? 217.236 188.539 151.974 1.00 44.87  ? 176  ARG A O   1 
ATOM   10844 C CB  . ARG B 2 176  ? 219.820 188.319 149.903 1.00 44.87  ? 176  ARG A CB  1 
ATOM   10845 C CG  . ARG B 2 176  ? 220.315 188.973 151.182 1.00 44.87  ? 176  ARG A CG  1 
ATOM   10846 C CD  . ARG B 2 176  ? 221.802 189.272 151.119 1.00 44.87  ? 176  ARG A CD  1 
ATOM   10847 N NE  . ARG B 2 176  ? 222.612 188.062 151.150 1.00 44.87  ? 176  ARG A NE  1 
ATOM   10848 C CZ  . ARG B 2 176  ? 223.323 187.607 150.129 1.00 44.87  ? 176  ARG A CZ  1 
ATOM   10849 N NH1 . ARG B 2 176  ? 223.344 188.237 148.966 1.00 44.87  ? 176  ARG A NH1 1 
ATOM   10850 N NH2 . ARG B 2 176  ? 224.030 186.490 150.275 1.00 44.87  ? 176  ARG A NH2 1 
ATOM   10851 N N   . VAL B 2 177  ? 217.146 189.955 150.224 1.00 41.53  ? 177  VAL A N   1 
ATOM   10852 C CA  . VAL B 2 177  ? 216.391 190.952 150.975 1.00 41.53  ? 177  VAL A CA  1 
ATOM   10853 C C   . VAL B 2 177  ? 215.011 190.423 151.341 1.00 41.53  ? 177  VAL A C   1 
ATOM   10854 O O   . VAL B 2 177  ? 214.552 190.587 152.478 1.00 41.53  ? 177  VAL A O   1 
ATOM   10855 C CB  . VAL B 2 177  ? 216.305 192.265 150.179 1.00 41.53  ? 177  VAL A CB  1 
ATOM   10856 C CG1 . VAL B 2 177  ? 215.054 193.035 150.558 1.00 41.53  ? 177  VAL A CG1 1 
ATOM   10857 C CG2 . VAL B 2 177  ? 217.544 193.101 150.419 1.00 41.53  ? 177  VAL A CG2 1 
ATOM   10858 N N   . LEU B 2 178  ? 214.327 189.778 150.392 1.00 42.95  ? 178  LEU A N   1 
ATOM   10859 C CA  . LEU B 2 178  ? 213.026 189.189 150.695 1.00 42.95  ? 178  LEU A CA  1 
ATOM   10860 C C   . LEU B 2 178  ? 213.153 188.094 151.742 1.00 42.95  ? 178  LEU A C   1 
ATOM   10861 O O   . LEU B 2 178  ? 212.312 187.984 152.644 1.00 42.95  ? 178  LEU A O   1 
ATOM   10862 C CB  . LEU B 2 178  ? 212.386 188.633 149.423 1.00 42.95  ? 178  LEU A CB  1 
ATOM   10863 C CG  . LEU B 2 178  ? 210.959 188.110 149.586 1.00 42.95  ? 178  LEU A CG  1 
ATOM   10864 C CD1 . LEU B 2 178  ? 210.021 189.223 150.016 1.00 42.95  ? 178  LEU A CD1 1 
ATOM   10865 C CD2 . LEU B 2 178  ? 210.466 187.458 148.307 1.00 42.95  ? 178  LEU A CD2 1 
ATOM   10866 N N   . SER B 2 179  ? 214.198 187.272 151.637 1.00 44.59  ? 179  SER A N   1 
ATOM   10867 C CA  . SER B 2 179  ? 214.421 186.222 152.619 1.00 44.59  ? 179  SER A CA  1 
ATOM   10868 C C   . SER B 2 179  ? 214.572 186.808 154.014 1.00 44.59  ? 179  SER A C   1 
ATOM   10869 O O   . SER B 2 179  ? 213.891 186.387 154.954 1.00 44.59  ? 179  SER A O   1 
ATOM   10870 C CB  . SER B 2 179  ? 215.654 185.401 152.242 1.00 44.59  ? 179  SER A CB  1 
ATOM   10871 O OG  . SER B 2 179  ? 216.838 186.043 152.677 1.00 44.59  ? 179  SER A OG  1 
ATOM   10872 N N   . MET B 2 180  ? 215.438 187.815 154.155 1.00 45.75  ? 180  MET A N   1 
ATOM   10873 C CA  . MET B 2 180  ? 215.649 188.433 155.460 1.00 45.75  ? 180  MET A CA  1 
ATOM   10874 C C   . MET B 2 180  ? 214.373 189.085 155.979 1.00 45.75  ? 180  MET A C   1 
ATOM   10875 O O   . MET B 2 180  ? 214.029 188.941 157.159 1.00 45.75  ? 180  MET A O   1 
ATOM   10876 C CB  . MET B 2 180  ? 216.780 189.457 155.375 1.00 45.75  ? 180  MET A CB  1 
ATOM   10877 C CG  . MET B 2 180  ? 218.163 188.844 155.216 1.00 45.75  ? 180  MET A CG  1 
ATOM   10878 S SD  . MET B 2 180  ? 219.501 190.052 155.272 1.00 45.75  ? 180  MET A SD  1 
ATOM   10879 C CE  . MET B 2 180  ? 218.599 191.577 155.541 1.00 45.75  ? 180  MET A CE  1 
ATOM   10880 N N   . SER B 2 181  ? 213.654 189.801 155.111 1.00 46.63  ? 181  SER A N   1 
ATOM   10881 C CA  . SER B 2 181  ? 212.460 190.519 155.543 1.00 46.63  ? 181  SER A CA  1 
ATOM   10882 C C   . SER B 2 181  ? 211.388 189.561 156.041 1.00 46.63  ? 181  SER A C   1 
ATOM   10883 O O   . SER B 2 181  ? 210.855 189.721 157.148 1.00 46.63  ? 181  SER A O   1 
ATOM   10884 C CB  . SER B 2 181  ? 211.924 191.369 154.393 1.00 46.63  ? 181  SER A CB  1 
ATOM   10885 O OG  . SER B 2 181  ? 210.609 191.816 154.665 1.00 46.63  ? 181  SER A OG  1 
ATOM   10886 N N   . LEU B 2 182  ? 211.047 188.556 155.236 1.00 48.34  ? 182  LEU A N   1 
ATOM   10887 C CA  . LEU B 2 182  ? 210.007 187.633 155.668 1.00 48.34  ? 182  LEU A CA  1 
ATOM   10888 C C   . LEU B 2 182  ? 210.468 186.787 156.848 1.00 48.34  ? 182  LEU A C   1 
ATOM   10889 O O   . LEU B 2 182  ? 209.651 186.432 157.704 1.00 48.34  ? 182  LEU A O   1 
ATOM   10890 C CB  . LEU B 2 182  ? 209.560 186.753 154.505 1.00 48.34  ? 182  LEU A CB  1 
ATOM   10891 C CG  . LEU B 2 182  ? 208.280 187.217 153.814 1.00 48.34  ? 182  LEU A CG  1 
ATOM   10892 C CD1 . LEU B 2 182  ? 207.849 186.213 152.758 1.00 48.34  ? 182  LEU A CD1 1 
ATOM   10893 C CD2 . LEU B 2 182  ? 207.182 187.446 154.835 1.00 48.34  ? 182  LEU A CD2 1 
ATOM   10894 N N   . ALA B 2 183  ? 211.766 186.475 156.929 1.00 50.11  ? 183  ALA A N   1 
ATOM   10895 C CA  . ALA B 2 183  ? 212.271 185.732 158.076 1.00 50.11  ? 183  ALA A CA  1 
ATOM   10896 C C   . ALA B 2 183  ? 212.100 186.527 159.361 1.00 50.11  ? 183  ALA A C   1 
ATOM   10897 O O   . ALA B 2 183  ? 211.648 185.988 160.381 1.00 50.11  ? 183  ALA A O   1 
ATOM   10898 C CB  . ALA B 2 183  ? 213.739 185.367 157.856 1.00 50.11  ? 183  ALA A CB  1 
ATOM   10899 N N   . VAL B 2 184  ? 212.448 187.817 159.336 1.00 50.84  ? 184  VAL A N   1 
ATOM   10900 C CA  . VAL B 2 184  ? 212.316 188.620 160.547 1.00 50.84  ? 184  VAL A CA  1 
ATOM   10901 C C   . VAL B 2 184  ? 210.846 188.815 160.892 1.00 50.84  ? 184  VAL A C   1 
ATOM   10902 O O   . VAL B 2 184  ? 210.464 188.789 162.070 1.00 50.84  ? 184  VAL A O   1 
ATOM   10903 C CB  . VAL B 2 184  ? 213.073 189.958 160.416 1.00 50.84  ? 184  VAL A CB  1 
ATOM   10904 C CG1 . VAL B 2 184  ? 212.342 190.942 159.523 1.00 50.84  ? 184  VAL A CG1 1 
ATOM   10905 C CG2 . VAL B 2 184  ? 213.305 190.563 161.789 1.00 50.84  ? 184  VAL A CG2 1 
ATOM   10906 N N   . ASN B 2 185  ? 209.987 188.968 159.878 1.00 51.92  ? 185  ASN A N   1 
ATOM   10907 C CA  . ASN B 2 185  ? 208.558 189.079 160.140 1.00 51.92  ? 185  ASN A CA  1 
ATOM   10908 C C   . ASN B 2 185  ? 208.045 187.832 160.850 1.00 51.92  ? 185  ASN A C   1 
ATOM   10909 O O   . ASN B 2 185  ? 207.380 187.925 161.888 1.00 51.92  ? 185  ASN A O   1 
ATOM   10910 C CB  . ASN B 2 185  ? 207.805 189.306 158.827 1.00 51.92  ? 185  ASN A CB  1 
ATOM   10911 C CG  . ASN B 2 185  ? 206.306 189.037 158.938 1.00 51.92  ? 185  ASN A CG  1 
ATOM   10912 O OD1 . ASN B 2 185  ? 205.721 189.069 160.019 1.00 51.92  ? 185  ASN A OD1 1 
ATOM   10913 N ND2 . ASN B 2 185  ? 205.683 188.746 157.804 1.00 51.92  ? 185  ASN A ND2 1 
ATOM   10914 N N   . ALA B 2 186  ? 208.360 186.652 160.308 1.00 54.02  ? 186  ALA A N   1 
ATOM   10915 C CA  . ALA B 2 186  ? 207.869 185.411 160.898 1.00 54.02  ? 186  ALA A CA  1 
ATOM   10916 C C   . ALA B 2 186  ? 208.418 185.206 162.304 1.00 54.02  ? 186  ALA A C   1 
ATOM   10917 O O   . ALA B 2 186  ? 207.672 184.853 163.228 1.00 54.02  ? 186  ALA A O   1 
ATOM   10918 C CB  . ALA B 2 186  ? 208.235 184.226 160.006 1.00 54.02  ? 186  ALA A CB  1 
ATOM   10919 N N   . SER B 2 187  ? 209.722 185.431 162.486 1.00 58.19  ? 187  SER A N   1 
ATOM   10920 C CA  . SER B 2 187  ? 210.333 185.215 163.794 1.00 58.19  ? 187  SER A CA  1 
ATOM   10921 C C   . SER B 2 187  ? 209.736 186.143 164.841 1.00 58.19  ? 187  SER A C   1 
ATOM   10922 O O   . SER B 2 187  ? 209.399 185.708 165.949 1.00 58.19  ? 187  SER A O   1 
ATOM   10923 C CB  . SER B 2 187  ? 211.845 185.410 163.705 1.00 58.19  ? 187  SER A CB  1 
ATOM   10924 O OG  . SER B 2 187  ? 212.458 184.353 162.988 1.00 58.19  ? 187  SER A OG  1 
ATOM   10925 N N   . PHE B 2 188  ? 209.572 187.424 164.507 1.00 58.77  ? 188  PHE A N   1 
ATOM   10926 C CA  . PHE B 2 188  ? 209.081 188.345 165.518 1.00 58.77  ? 188  PHE A CA  1 
ATOM   10927 C C   . PHE B 2 188  ? 207.580 188.208 165.734 1.00 58.77  ? 188  PHE A C   1 
ATOM   10928 O O   . PHE B 2 188  ? 207.098 188.495 166.831 1.00 58.77  ? 188  PHE A O   1 
ATOM   10929 C CB  . PHE B 2 188  ? 209.461 189.778 165.150 1.00 58.77  ? 188  PHE A CB  1 
ATOM   10930 C CG  . PHE B 2 188  ? 210.834 190.163 165.621 1.00 58.77  ? 188  PHE A CG  1 
ATOM   10931 C CD1 . PHE B 2 188  ? 211.955 189.573 165.063 1.00 58.77  ? 188  PHE A CD1 1 
ATOM   10932 C CD2 . PHE B 2 188  ? 211.003 191.060 166.658 1.00 58.77  ? 188  PHE A CD2 1 
ATOM   10933 C CE1 . PHE B 2 188  ? 213.222 189.912 165.500 1.00 58.77  ? 188  PHE A CE1 1 
ATOM   10934 C CE2 . PHE B 2 188  ? 212.264 191.404 167.097 1.00 58.77  ? 188  PHE A CE2 1 
ATOM   10935 C CZ  . PHE B 2 188  ? 213.377 190.827 166.522 1.00 58.77  ? 188  PHE A CZ  1 
ATOM   10936 N N   . ALA B 2 189  ? 206.827 187.743 164.734 1.00 59.53  ? 189  ALA A N   1 
ATOM   10937 C CA  . ALA B 2 189  ? 205.432 187.397 164.983 1.00 59.53  ? 189  ALA A CA  1 
ATOM   10938 C C   . ALA B 2 189  ? 205.320 186.217 165.937 1.00 59.53  ? 189  ALA A C   1 
ATOM   10939 O O   . ALA B 2 189  ? 204.505 186.237 166.871 1.00 59.53  ? 189  ALA A O   1 
ATOM   10940 C CB  . ALA B 2 189  ? 204.723 187.091 163.665 1.00 59.53  ? 189  ALA A CB  1 
ATOM   10941 N N   . SER B 2 190  ? 206.142 185.183 165.730 1.00 62.06  ? 190  SER A N   1 
ATOM   10942 C CA  . SER B 2 190  ? 206.141 184.050 166.649 1.00 62.06  ? 190  SER A CA  1 
ATOM   10943 C C   . SER B 2 190  ? 206.539 184.487 168.051 1.00 62.06  ? 190  SER A C   1 
ATOM   10944 O O   . SER B 2 190  ? 205.988 183.992 169.043 1.00 62.06  ? 190  SER A O   1 
ATOM   10945 C CB  . SER B 2 190  ? 207.079 182.957 166.138 1.00 62.06  ? 190  SER A CB  1 
ATOM   10946 O OG  . SER B 2 190  ? 207.455 182.087 167.191 1.00 62.06  ? 190  SER A OG  1 
ATOM   10947 N N   . LEU B 2 191  ? 207.505 185.403 168.155 1.00 63.48  ? 191  LEU A N   1 
ATOM   10948 C CA  . LEU B 2 191  ? 207.865 185.953 169.459 1.00 63.48  ? 191  LEU A CA  1 
ATOM   10949 C C   . LEU B 2 191  ? 206.702 186.727 170.072 1.00 63.48  ? 191  LEU A C   1 
ATOM   10950 O O   . LEU B 2 191  ? 206.455 186.637 171.279 1.00 63.48  ? 191  LEU A O   1 
ATOM   10951 C CB  . LEU B 2 191  ? 209.098 186.845 169.331 1.00 63.48  ? 191  LEU A CB  1 
ATOM   10952 C CG  . LEU B 2 191  ? 210.370 186.299 169.976 1.00 63.48  ? 191  LEU A CG  1 
ATOM   10953 C CD1 . LEU B 2 191  ? 210.701 184.920 169.421 1.00 63.48  ? 191  LEU A CD1 1 
ATOM   10954 C CD2 . LEU B 2 191  ? 211.533 187.256 169.768 1.00 63.48  ? 191  LEU A CD2 1 
ATOM   10955 N N   . SER B 2 192  ? 205.982 187.498 169.251 1.00 62.73  ? 192  SER A N   1 
ATOM   10956 C CA  . SER B 2 192  ? 204.812 188.228 169.733 1.00 62.73  ? 192  SER A CA  1 
ATOM   10957 C C   . SER B 2 192  ? 203.746 187.284 170.257 1.00 62.73  ? 192  SER A C   1 
ATOM   10958 O O   . SER B 2 192  ? 202.975 187.657 171.148 1.00 62.73  ? 192  SER A O   1 
ATOM   10959 C CB  . SER B 2 192  ? 204.232 189.087 168.612 1.00 62.73  ? 192  SER A CB  1 
ATOM   10960 O OG  . SER B 2 192  ? 203.628 188.282 167.616 1.00 62.73  ? 192  SER A OG  1 
ATOM   10961 N N   . SER B 2 193  ? 203.674 186.071 169.709 1.00 64.17  ? 193  SER A N   1 
ATOM   10962 C CA  . SER B 2 193  ? 202.715 185.099 170.219 1.00 64.17  ? 193  SER A CA  1 
ATOM   10963 C C   . SER B 2 193  ? 202.968 184.794 171.691 1.00 64.17  ? 193  SER A C   1 
ATOM   10964 O O   . SER B 2 193  ? 202.031 184.768 172.497 1.00 64.17  ? 193  SER A O   1 
ATOM   10965 C CB  . SER B 2 193  ? 202.775 183.820 169.390 1.00 64.17  ? 193  SER A CB  1 
ATOM   10966 O OG  . SER B 2 193  ? 204.004 183.145 169.586 1.00 64.17  ? 193  SER A OG  1 
ATOM   10967 N N   . PHE B 2 194  ? 204.226 184.576 172.066 1.00 68.04  ? 194  PHE A N   1 
ATOM   10968 C CA  . PHE B 2 194  ? 204.576 184.273 173.455 1.00 68.04  ? 194  PHE A CA  1 
ATOM   10969 C C   . PHE B 2 194  ? 205.024 185.549 174.163 1.00 68.04  ? 194  PHE A C   1 
ATOM   10970 O O   . PHE B 2 194  ? 206.200 185.768 174.449 1.00 68.04  ? 194  PHE A O   1 
ATOM   10971 C CB  . PHE B 2 194  ? 205.650 183.191 173.505 1.00 68.04  ? 194  PHE A CB  1 
ATOM   10972 C CG  . PHE B 2 194  ? 205.124 181.802 173.277 1.00 68.04  ? 194  PHE A CG  1 
ATOM   10973 C CD1 . PHE B 2 194  ? 204.021 181.343 173.976 1.00 68.04  ? 194  PHE A CD1 1 
ATOM   10974 C CD2 . PHE B 2 194  ? 205.729 180.960 172.360 1.00 68.04  ? 194  PHE A CD2 1 
ATOM   10975 C CE1 . PHE B 2 194  ? 203.533 180.067 173.770 1.00 68.04  ? 194  PHE A CE1 1 
ATOM   10976 C CE2 . PHE B 2 194  ? 205.246 179.681 172.149 1.00 68.04  ? 194  PHE A CE2 1 
ATOM   10977 C CZ  . PHE B 2 194  ? 204.145 179.235 172.853 1.00 68.04  ? 194  PHE A CZ  1 
ATOM   10978 N N   . VAL B 2 195  ? 204.042 186.404 174.443 1.00 68.97  ? 195  VAL A N   1 
ATOM   10979 C CA  . VAL B 2 195  ? 204.281 187.697 175.077 1.00 68.97  ? 195  VAL A CA  1 
ATOM   10980 C C   . VAL B 2 195  ? 203.189 187.943 176.109 1.00 68.97  ? 195  VAL A C   1 
ATOM   10981 O O   . VAL B 2 195  ? 202.010 187.687 175.846 1.00 68.97  ? 195  VAL A O   1 
ATOM   10982 C CB  . VAL B 2 195  ? 204.323 188.840 174.041 1.00 68.97  ? 195  VAL A CB  1 
ATOM   10983 C CG1 . VAL B 2 195  ? 203.881 190.157 174.658 1.00 68.97  ? 195  VAL A CG1 1 
ATOM   10984 C CG2 . VAL B 2 195  ? 205.720 188.968 173.457 1.00 68.97  ? 195  VAL A CG2 1 
ATOM   10985 N N   . GLN B 2 196  ? 203.581 188.436 177.281 1.00 74.33  ? 196  GLN A N   1 
ATOM   10986 C CA  . GLN B 2 196  ? 202.648 188.845 178.324 1.00 74.33  ? 196  GLN A CA  1 
ATOM   10987 C C   . GLN B 2 196  ? 202.690 190.363 178.441 1.00 74.33  ? 196  GLN A C   1 
ATOM   10988 O O   . GLN B 2 196  ? 203.766 190.945 178.618 1.00 74.33  ? 196  GLN A O   1 
ATOM   10989 C CB  . GLN B 2 196  ? 202.988 188.192 179.663 1.00 74.33  ? 196  GLN A CB  1 
ATOM   10990 C CG  . GLN B 2 196  ? 203.717 186.863 179.550 1.00 74.33  ? 196  GLN A CG  1 
ATOM   10991 C CD  . GLN B 2 196  ? 205.224 187.021 179.523 1.00 74.33  ? 196  GLN A CD  1 
ATOM   10992 O OE1 . GLN B 2 196  ? 205.742 188.136 179.483 1.00 74.33  ? 196  GLN A OE1 1 
ATOM   10993 N NE2 . GLN B 2 196  ? 205.941 185.901 179.548 1.00 74.33  ? 196  GLN A NE2 1 
ATOM   10994 N N   . GLY B 2 197  ? 201.533 190.992 178.346 1.00 72.81  ? 197  GLY A N   1 
ATOM   10995 C CA  . GLY B 2 197  ? 201.431 192.435 178.399 1.00 72.81  ? 197  GLY A CA  1 
ATOM   10996 C C   . GLY B 2 197  ? 201.179 193.028 177.025 1.00 72.81  ? 197  GLY A C   1 
ATOM   10997 O O   . GLY B 2 197  ? 201.616 192.500 175.994 1.00 72.81  ? 197  GLY A O   1 
ATOM   10998 N N   . TYR B 2 198  ? 200.456 194.150 177.005 1.00 65.92  ? 198  TYR A N   1 
ATOM   10999 C CA  . TYR B 2 198  ? 200.111 194.777 175.736 1.00 65.92  ? 198  TYR A CA  1 
ATOM   11000 C C   . TYR B 2 198  ? 201.273 195.551 175.127 1.00 65.92  ? 198  TYR A C   1 
ATOM   11001 O O   . TYR B 2 198  ? 201.398 195.591 173.899 1.00 65.92  ? 198  TYR A O   1 
ATOM   11002 C CB  . TYR B 2 198  ? 198.912 195.707 175.906 1.00 65.92  ? 198  TYR A CB  1 
ATOM   11003 C CG  . TYR B 2 198  ? 198.377 196.217 174.589 1.00 65.92  ? 198  TYR A CG  1 
ATOM   11004 C CD1 . TYR B 2 198  ? 197.593 195.409 173.780 1.00 65.92  ? 198  TYR A CD1 1 
ATOM   11005 C CD2 . TYR B 2 198  ? 198.665 197.501 174.150 1.00 65.92  ? 198  TYR A CD2 1 
ATOM   11006 C CE1 . TYR B 2 198  ? 197.106 195.868 172.573 1.00 65.92  ? 198  TYR A CE1 1 
ATOM   11007 C CE2 . TYR B 2 198  ? 198.182 197.969 172.948 1.00 65.92  ? 198  TYR A CE2 1 
ATOM   11008 C CZ  . TYR B 2 198  ? 197.403 197.148 172.162 1.00 65.92  ? 198  TYR A CZ  1 
ATOM   11009 O OH  . TYR B 2 198  ? 196.920 197.609 170.962 1.00 65.92  ? 198  TYR A OH  1 
ATOM   11010 N N   . GLY B 2 199  ? 202.109 196.185 175.948 1.00 63.89  ? 199  GLY A N   1 
ATOM   11011 C CA  . GLY B 2 199  ? 203.185 196.997 175.400 1.00 63.89  ? 199  GLY A CA  1 
ATOM   11012 C C   . GLY B 2 199  ? 204.200 196.181 174.625 1.00 63.89  ? 199  GLY A C   1 
ATOM   11013 O O   . GLY B 2 199  ? 204.598 196.549 173.515 1.00 63.89  ? 199  GLY A O   1 
ATOM   11014 N N   . ALA B 2 200  ? 204.632 195.056 175.200 1.00 63.04  ? 200  ALA A N   1 
ATOM   11015 C CA  . ALA B 2 200  ? 205.582 194.194 174.508 1.00 63.04  ? 200  ALA A CA  1 
ATOM   11016 C C   . ALA B 2 200  ? 204.974 193.623 173.234 1.00 63.04  ? 200  ALA A C   1 
ATOM   11017 O O   . ALA B 2 200  ? 205.648 193.523 172.204 1.00 63.04  ? 200  ALA A O   1 
ATOM   11018 C CB  . ALA B 2 200  ? 206.043 193.070 175.434 1.00 63.04  ? 200  ALA A CB  1 
ATOM   11019 N N   . PHE B 2 201  ? 203.693 193.247 173.290 1.00 60.06  ? 201  PHE A N   1 
ATOM   11020 C CA  . PHE B 2 201  ? 203.023 192.726 172.104 1.00 60.06  ? 201  PHE A CA  1 
ATOM   11021 C C   . PHE B 2 201  ? 202.951 193.777 171.005 1.00 60.06  ? 201  PHE A C   1 
ATOM   11022 O O   . PHE B 2 201  ? 203.160 193.470 169.827 1.00 60.06  ? 201  PHE A O   1 
ATOM   11023 C CB  . PHE B 2 201  ? 201.625 192.233 172.467 1.00 60.06  ? 201  PHE A CB  1 
ATOM   11024 C CG  . PHE B 2 201  ? 200.727 192.041 171.286 1.00 60.06  ? 201  PHE A CG  1 
ATOM   11025 C CD1 . PHE B 2 201  ? 200.996 191.062 170.348 1.00 60.06  ? 201  PHE A CD1 1 
ATOM   11026 C CD2 . PHE B 2 201  ? 199.612 192.840 171.112 1.00 60.06  ? 201  PHE A CD2 1 
ATOM   11027 C CE1 . PHE B 2 201  ? 200.169 190.884 169.258 1.00 60.06  ? 201  PHE A CE1 1 
ATOM   11028 C CE2 . PHE B 2 201  ? 198.781 192.667 170.027 1.00 60.06  ? 201  PHE A CE2 1 
ATOM   11029 C CZ  . PHE B 2 201  ? 199.061 191.686 169.098 1.00 60.06  ? 201  PHE A CZ  1 
ATOM   11030 N N   . LEU B 2 202  ? 202.656 195.026 171.369 1.00 57.51  ? 202  LEU A N   1 
ATOM   11031 C CA  . LEU B 2 202  ? 202.588 196.083 170.369 1.00 57.51  ? 202  LEU A CA  1 
ATOM   11032 C C   . LEU B 2 202  ? 203.963 196.385 169.787 1.00 57.51  ? 202  LEU A C   1 
ATOM   11033 O O   . LEU B 2 202  ? 204.085 196.649 168.588 1.00 57.51  ? 202  LEU A O   1 
ATOM   11034 C CB  . LEU B 2 202  ? 201.972 197.345 170.969 1.00 57.51  ? 202  LEU A CB  1 
ATOM   11035 C CG  . LEU B 2 202  ? 201.466 198.353 169.937 1.00 57.51  ? 202  LEU A CG  1 
ATOM   11036 C CD1 . LEU B 2 202  ? 200.833 197.638 168.755 1.00 57.51  ? 202  LEU A CD1 1 
ATOM   11037 C CD2 . LEU B 2 202  ? 200.477 199.311 170.571 1.00 57.51  ? 202  LEU A CD2 1 
ATOM   11038 N N   . PHE B 2 203  ? 205.010 196.353 170.615 1.00 59.42  ? 203  PHE A N   1 
ATOM   11039 C CA  . PHE B 2 203  ? 206.361 196.535 170.089 1.00 59.42  ? 203  PHE A CA  1 
ATOM   11040 C C   . PHE B 2 203  ? 206.724 195.418 169.117 1.00 59.42  ? 203  PHE A C   1 
ATOM   11041 O O   . PHE B 2 203  ? 207.317 195.667 168.058 1.00 59.42  ? 203  PHE A O   1 
ATOM   11042 C CB  . PHE B 2 203  ? 207.367 196.618 171.243 1.00 59.42  ? 203  PHE A CB  1 
ATOM   11043 C CG  . PHE B 2 203  ? 208.802 196.412 170.829 1.00 59.42  ? 203  PHE A CG  1 
ATOM   11044 C CD1 . PHE B 2 203  ? 209.333 195.137 170.695 1.00 59.42  ? 203  PHE A CD1 1 
ATOM   11045 C CD2 . PHE B 2 203  ? 209.641 197.498 170.649 1.00 59.42  ? 203  PHE A CD2 1 
ATOM   11046 C CE1 . PHE B 2 203  ? 210.650 194.951 170.332 1.00 59.42  ? 203  PHE A CE1 1 
ATOM   11047 C CE2 . PHE B 2 203  ? 210.962 197.317 170.285 1.00 59.42  ? 203  PHE A CE2 1 
ATOM   11048 C CZ  . PHE B 2 203  ? 211.468 196.040 170.131 1.00 59.42  ? 203  PHE A CZ  1 
ATOM   11049 N N   . CYS B 2 204  ? 206.384 194.175 169.468 1.00 57.28  ? 204  CYS A N   1 
ATOM   11050 C CA  . CYS B 2 204  ? 206.657 193.052 168.580 1.00 57.28  ? 204  CYS A CA  1 
ATOM   11051 C C   . CYS B 2 204  ? 205.885 193.185 167.273 1.00 57.28  ? 204  CYS A C   1 
ATOM   11052 O O   . CYS B 2 204  ? 206.416 192.891 166.195 1.00 57.28  ? 204  CYS A O   1 
ATOM   11053 C CB  . CYS B 2 204  ? 206.322 191.737 169.278 1.00 57.28  ? 204  CYS A CB  1 
ATOM   11054 S SG  . CYS B 2 204  ? 207.417 191.318 170.652 1.00 57.28  ? 204  CYS A SG  1 
ATOM   11055 N N   . ARG B 2 205  ? 204.632 193.632 167.349 1.00 52.12  ? 205  ARG A N   1 
ATOM   11056 C CA  . ARG B 2 205  ? 203.867 193.867 166.130 1.00 52.12  ? 205  ARG A CA  1 
ATOM   11057 C C   . ARG B 2 205  ? 204.494 194.976 165.298 1.00 52.12  ? 205  ARG A C   1 
ATOM   11058 O O   . ARG B 2 205  ? 204.494 194.910 164.067 1.00 52.12  ? 205  ARG A O   1 
ATOM   11059 C CB  . ARG B 2 205  ? 202.418 194.198 166.469 1.00 52.12  ? 205  ARG A CB  1 
ATOM   11060 C CG  . ARG B 2 205  ? 201.561 192.975 166.729 1.00 52.12  ? 205  ARG A CG  1 
ATOM   11061 C CD  . ARG B 2 205  ? 201.076 192.371 165.428 1.00 52.12  ? 205  ARG A CD  1 
ATOM   11062 N NE  . ARG B 2 205  ? 201.794 191.144 165.107 1.00 52.12  ? 205  ARG A NE  1 
ATOM   11063 C CZ  . ARG B 2 205  ? 201.646 190.463 163.980 1.00 52.12  ? 205  ARG A CZ  1 
ATOM   11064 N NH1 . ARG B 2 205  ? 200.818 190.866 163.032 1.00 52.12  ? 205  ARG A NH1 1 
ATOM   11065 N NH2 . ARG B 2 205  ? 202.349 189.348 163.798 1.00 52.12  ? 205  ARG A NH2 1 
ATOM   11066 N N   . LEU B 2 206  ? 205.032 196.008 165.954 1.00 51.61  ? 206  LEU A N   1 
ATOM   11067 C CA  . LEU B 2 206  ? 205.672 197.094 165.224 1.00 51.61  ? 206  LEU A CA  1 
ATOM   11068 C C   . LEU B 2 206  ? 206.901 196.608 164.469 1.00 51.61  ? 206  LEU A C   1 
ATOM   11069 O O   . LEU B 2 206  ? 207.111 196.972 163.306 1.00 51.61  ? 206  LEU A O   1 
ATOM   11070 C CB  . LEU B 2 206  ? 206.047 198.223 166.181 1.00 51.61  ? 206  LEU A CB  1 
ATOM   11071 C CG  . LEU B 2 206  ? 206.751 199.419 165.537 1.00 51.61  ? 206  LEU A CG  1 
ATOM   11072 C CD1 . LEU B 2 206  ? 206.110 200.719 165.986 1.00 51.61  ? 206  LEU A CD1 1 
ATOM   11073 C CD2 . LEU B 2 206  ? 208.235 199.417 165.864 1.00 51.61  ? 206  LEU A CD2 1 
ATOM   11074 N N   . ILE B 2 207  ? 207.736 195.788 165.112 1.00 51.53  ? 207  ILE A N   1 
ATOM   11075 C CA  . ILE B 2 207  ? 208.920 195.305 164.401 1.00 51.53  ? 207  ILE A CA  1 
ATOM   11076 C C   . ILE B 2 207  ? 208.522 194.298 163.320 1.00 51.53  ? 207  ILE A C   1 
ATOM   11077 O O   . ILE B 2 207  ? 209.157 194.231 162.258 1.00 51.53  ? 207  ILE A O   1 
ATOM   11078 C CB  . ILE B 2 207  ? 209.960 194.732 165.384 1.00 51.53  ? 207  ILE A CB  1 
ATOM   11079 C CG1 . ILE B 2 207  ? 211.016 193.902 164.652 1.00 51.53  ? 207  ILE A CG1 1 
ATOM   11080 C CG2 . ILE B 2 207  ? 209.298 193.911 166.444 1.00 51.53  ? 207  ILE A CG2 1 
ATOM   11081 C CD1 . ILE B 2 207  ? 211.940 194.729 163.785 1.00 51.53  ? 207  ILE A CD1 1 
ATOM   11082 N N   . SER B 2 208  ? 207.458 193.524 163.545 1.00 49.96  ? 208  SER A N   1 
ATOM   11083 C CA  . SER B 2 208  ? 206.956 192.654 162.483 1.00 49.96  ? 208  SER A CA  1 
ATOM   11084 C C   . SER B 2 208  ? 206.491 193.468 161.281 1.00 49.96  ? 208  SER A C   1 
ATOM   11085 O O   . SER B 2 208  ? 206.740 193.093 160.131 1.00 49.96  ? 208  SER A O   1 
ATOM   11086 C CB  . SER B 2 208  ? 205.816 191.784 163.009 1.00 49.96  ? 208  SER A CB  1 
ATOM   11087 O OG  . SER B 2 208  ? 204.559 192.362 162.706 1.00 49.96  ? 208  SER A OG  1 
ATOM   11088 N N   . GLY B 2 209  ? 205.800 194.581 161.534 1.00 47.83  ? 209  GLY A N   1 
ATOM   11089 C CA  . GLY B 2 209  ? 205.430 195.478 160.451 1.00 47.83  ? 209  GLY A CA  1 
ATOM   11090 C C   . GLY B 2 209  ? 206.640 196.063 159.750 1.00 47.83  ? 209  GLY A C   1 
ATOM   11091 O O   . GLY B 2 209  ? 206.648 196.213 158.526 1.00 47.83  ? 209  GLY A O   1 
ATOM   11092 N N   . ILE B 2 210  ? 207.677 196.401 160.520 1.00 46.52  ? 210  ILE A N   1 
ATOM   11093 C CA  . ILE B 2 210  ? 208.945 196.824 159.928 1.00 46.52  ? 210  ILE A CA  1 
ATOM   11094 C C   . ILE B 2 210  ? 209.441 195.776 158.946 1.00 46.52  ? 210  ILE A C   1 
ATOM   11095 O O   . ILE B 2 210  ? 209.844 196.091 157.820 1.00 46.52  ? 210  ILE A O   1 
ATOM   11096 C CB  . ILE B 2 210  ? 209.994 197.075 161.033 1.00 46.52  ? 210  ILE A CB  1 
ATOM   11097 C CG1 . ILE B 2 210  ? 209.696 198.351 161.817 1.00 46.52  ? 210  ILE A CG1 1 
ATOM   11098 C CG2 . ILE B 2 210  ? 211.394 197.130 160.437 1.00 46.52  ? 210  ILE A CG2 1 
ATOM   11099 C CD1 . ILE B 2 210  ? 210.053 199.612 161.075 1.00 46.52  ? 210  ILE A CD1 1 
ATOM   11100 N N   . GLY B 2 211  ? 209.405 194.511 159.358 1.00 45.51  ? 211  GLY A N   1 
ATOM   11101 C CA  . GLY B 2 211  ? 209.902 193.449 158.500 1.00 45.51  ? 211  GLY A CA  1 
ATOM   11102 C C   . GLY B 2 211  ? 209.067 193.247 157.249 1.00 45.51  ? 211  GLY A C   1 
ATOM   11103 O O   . GLY B 2 211  ? 209.607 193.040 156.161 1.00 45.51  ? 211  GLY A O   1 
ATOM   11104 N N   . ILE B 2 212  ? 207.743 193.304 157.384 1.00 42.00  ? 212  ILE A N   1 
ATOM   11105 C CA  . ILE B 2 212  ? 206.884 192.916 156.268 1.00 42.00  ? 212  ILE A CA  1 
ATOM   11106 C C   . ILE B 2 212  ? 206.616 194.075 155.307 1.00 42.00  ? 212  ILE A C   1 
ATOM   11107 O O   . ILE B 2 212  ? 206.329 193.843 154.129 1.00 42.00  ? 212  ILE A O   1 
ATOM   11108 C CB  . ILE B 2 212  ? 205.568 192.317 156.789 1.00 42.00  ? 212  ILE A CB  1 
ATOM   11109 C CG1 . ILE B 2 212  ? 204.645 191.947 155.628 1.00 42.00  ? 212  ILE A CG1 1 
ATOM   11110 C CG2 . ILE B 2 212  ? 204.860 193.316 157.661 1.00 42.00  ? 212  ILE A CG2 1 
ATOM   11111 C CD1 . ILE B 2 212  ? 203.907 190.653 155.823 1.00 42.00  ? 212  ILE A CD1 1 
ATOM   11112 N N   . GLY B 2 213  ? 206.733 195.325 155.763 1.00 41.17  ? 213  GLY A N   1 
ATOM   11113 C CA  . GLY B 2 213  ? 206.439 196.447 154.892 1.00 41.17  ? 213  GLY A CA  1 
ATOM   11114 C C   . GLY B 2 213  ? 207.345 196.545 153.684 1.00 41.17  ? 213  GLY A C   1 
ATOM   11115 O O   . GLY B 2 213  ? 207.024 197.265 152.733 1.00 41.17  ? 213  GLY A O   1 
ATOM   11116 N N   . GLY B 2 214  ? 208.473 195.841 153.698 1.00 40.39  ? 214  GLY A N   1 
ATOM   11117 C CA  . GLY B 2 214  ? 209.366 195.814 152.560 1.00 40.39  ? 214  GLY A CA  1 
ATOM   11118 C C   . GLY B 2 214  ? 209.237 194.555 151.729 1.00 40.39  ? 214  GLY A C   1 
ATOM   11119 O O   . GLY B 2 214  ? 210.158 194.203 150.989 1.00 40.39  ? 214  GLY A O   1 
ATOM   11120 N N   . ALA B 2 215  ? 208.108 193.857 151.848 1.00 37.12  ? 215  ALA A N   1 
ATOM   11121 C CA  . ALA B 2 215  ? 207.902 192.623 151.100 1.00 37.12  ? 215  ALA A CA  1 
ATOM   11122 C C   . ALA B 2 215  ? 207.254 192.873 149.741 1.00 37.12  ? 215  ALA A C   1 
ATOM   11123 O O   . ALA B 2 215  ? 207.691 192.306 148.736 1.00 37.12  ? 215  ALA A O   1 
ATOM   11124 C CB  . ALA B 2 215  ? 207.051 191.647 151.914 1.00 37.12  ? 215  ALA A CB  1 
ATOM   11125 N N   . LEU B 2 216  ? 206.215 193.708 149.699 1.00 34.09  ? 216  LEU A N   1 
ATOM   11126 C CA  . LEU B 2 216  ? 205.492 193.936 148.448 1.00 34.09  ? 216  LEU A CA  1 
ATOM   11127 C C   . LEU B 2 216  ? 206.368 194.492 147.333 1.00 34.09  ? 216  LEU A C   1 
ATOM   11128 O O   . LEU B 2 216  ? 206.329 193.943 146.212 1.00 34.09  ? 216  LEU A O   1 
ATOM   11129 C CB  . LEU B 2 216  ? 204.286 194.841 148.716 1.00 34.09  ? 216  LEU A CB  1 
ATOM   11130 C CG  . LEU B 2 216  ? 203.119 194.716 147.739 1.00 34.09  ? 216  LEU A CG  1 
ATOM   11131 C CD1 . LEU B 2 216  ? 201.804 194.888 148.469 1.00 34.09  ? 216  LEU A CD1 1 
ATOM   11132 C CD2 . LEU B 2 216  ? 203.248 195.741 146.634 1.00 34.09  ? 216  LEU A CD2 1 
ATOM   11133 N N   . PRO B 2 217  ? 207.158 195.554 147.535 1.00 33.89  ? 217  PRO A N   1 
ATOM   11134 C CA  . PRO B 2 217  ? 208.021 196.006 146.437 1.00 33.89  ? 217  PRO A CA  1 
ATOM   11135 C C   . PRO B 2 217  ? 208.978 194.929 145.975 1.00 33.89  ? 217  PRO A C   1 
ATOM   11136 O O   . PRO B 2 217  ? 209.205 194.777 144.769 1.00 33.89  ? 217  PRO A O   1 
ATOM   11137 C CB  . PRO B 2 217  ? 208.756 197.208 147.043 1.00 33.89  ? 217  PRO A CB  1 
ATOM   11138 C CG  . PRO B 2 217  ? 208.734 196.954 148.497 1.00 33.89  ? 217  PRO A CG  1 
ATOM   11139 C CD  . PRO B 2 217  ? 207.395 196.345 148.756 1.00 33.89  ? 217  PRO A CD  1 
ATOM   11140 N N   . ILE B 2 218  ? 209.514 194.146 146.911 1.00 34.64  ? 218  ILE A N   1 
ATOM   11141 C CA  . ILE B 2 218  ? 210.498 193.137 146.539 1.00 34.64  ? 218  ILE A CA  1 
ATOM   11142 C C   . ILE B 2 218  ? 209.842 192.008 145.764 1.00 34.64  ? 218  ILE A C   1 
ATOM   11143 O O   . ILE B 2 218  ? 210.405 191.521 144.781 1.00 34.64  ? 218  ILE A O   1 
ATOM   11144 C CB  . ILE B 2 218  ? 211.242 192.613 147.779 1.00 34.64  ? 218  ILE A CB  1 
ATOM   11145 C CG1 . ILE B 2 218  ? 211.961 193.752 148.500 1.00 34.64  ? 218  ILE A CG1 1 
ATOM   11146 C CG2 . ILE B 2 218  ? 212.242 191.555 147.370 1.00 34.64  ? 218  ILE A CG2 1 
ATOM   11147 C CD1 . ILE B 2 218  ? 212.501 194.822 147.589 1.00 34.64  ? 218  ILE A CD1 1 
ATOM   11148 N N   . VAL B 2 219  ? 208.647 191.576 146.172 1.00 31.41  ? 219  VAL A N   1 
ATOM   11149 C CA  . VAL B 2 219  ? 207.999 190.488 145.445 1.00 31.41  ? 219  VAL A CA  1 
ATOM   11150 C C   . VAL B 2 219  ? 207.613 190.934 144.040 1.00 31.41  ? 219  VAL A C   1 
ATOM   11151 O O   . VAL B 2 219  ? 207.803 190.193 143.069 1.00 31.41  ? 219  VAL A O   1 
ATOM   11152 C CB  . VAL B 2 219  ? 206.789 189.933 146.218 1.00 31.41  ? 219  VAL A CB  1 
ATOM   11153 C CG1 . VAL B 2 219  ? 205.814 191.008 146.563 1.00 31.41  ? 219  VAL A CG1 1 
ATOM   11154 C CG2 . VAL B 2 219  ? 206.090 188.901 145.389 1.00 31.41  ? 219  VAL A CG2 1 
ATOM   11155 N N   . PHE B 2 220  ? 207.077 192.151 143.897 1.00 32.82  ? 220  PHE A N   1 
ATOM   11156 C CA  . PHE B 2 220  ? 206.706 192.598 142.556 1.00 32.82  ? 220  PHE A CA  1 
ATOM   11157 C C   . PHE B 2 220  ? 207.931 192.786 141.669 1.00 32.82  ? 220  PHE A C   1 
ATOM   11158 O O   . PHE B 2 220  ? 207.933 192.360 140.508 1.00 32.82  ? 220  PHE A O   1 
ATOM   11159 C CB  . PHE B 2 220  ? 205.873 193.873 142.626 1.00 32.82  ? 220  PHE A CB  1 
ATOM   11160 C CG  . PHE B 2 220  ? 204.398 193.622 142.594 1.00 32.82  ? 220  PHE A CG  1 
ATOM   11161 C CD1 . PHE B 2 220  ? 203.817 192.994 141.506 1.00 32.82  ? 220  PHE A CD1 1 
ATOM   11162 C CD2 . PHE B 2 220  ? 203.593 193.994 143.654 1.00 32.82  ? 220  PHE A CD2 1 
ATOM   11163 C CE1 . PHE B 2 220  ? 202.461 192.753 141.472 1.00 32.82  ? 220  PHE A CE1 1 
ATOM   11164 C CE2 . PHE B 2 220  ? 202.234 193.754 143.623 1.00 32.82  ? 220  PHE A CE2 1 
ATOM   11165 C CZ  . PHE B 2 220  ? 201.669 193.133 142.530 1.00 32.82  ? 220  PHE A CZ  1 
ATOM   11166 N N   . ALA B 2 221  ? 208.995 193.404 142.199 1.00 33.63  ? 221  ALA A N   1 
ATOM   11167 C CA  . ALA B 2 221  ? 210.208 193.570 141.407 1.00 33.63  ? 221  ALA A CA  1 
ATOM   11168 C C   . ALA B 2 221  ? 210.820 192.219 141.055 1.00 33.63  ? 221  ALA A C   1 
ATOM   11169 O O   . ALA B 2 221  ? 211.334 192.033 139.946 1.00 33.63  ? 221  ALA A O   1 
ATOM   11170 C CB  . ALA B 2 221  ? 211.212 194.436 142.162 1.00 33.63  ? 221  ALA A CB  1 
ATOM   11171 N N   . TYR B 2 222  ? 210.777 191.270 141.992 1.00 32.84  ? 222  TYR A N   1 
ATOM   11172 C CA  . TYR B 2 222  ? 211.269 189.923 141.742 1.00 32.84  ? 222  TYR A CA  1 
ATOM   11173 C C   . TYR B 2 222  ? 210.523 189.273 140.591 1.00 32.84  ? 222  TYR A C   1 
ATOM   11174 O O   . TYR B 2 222  ? 211.134 188.802 139.626 1.00 32.84  ? 222  TYR A O   1 
ATOM   11175 C CB  . TYR B 2 222  ? 211.109 189.094 143.016 1.00 32.84  ? 222  TYR A CB  1 
ATOM   11176 C CG  . TYR B 2 222  ? 211.899 187.815 143.074 1.00 32.84  ? 222  TYR A CG  1 
ATOM   11177 C CD1 . TYR B 2 222  ? 212.730 187.430 142.037 1.00 32.84  ? 222  TYR A CD1 1 
ATOM   11178 C CD2 . TYR B 2 222  ? 211.805 186.984 144.178 1.00 32.84  ? 222  TYR A CD2 1 
ATOM   11179 C CE1 . TYR B 2 222  ? 213.442 186.260 142.101 1.00 32.84  ? 222  TYR A CE1 1 
ATOM   11180 C CE2 . TYR B 2 222  ? 212.514 185.820 144.251 1.00 32.84  ? 222  TYR A CE2 1 
ATOM   11181 C CZ  . TYR B 2 222  ? 213.330 185.461 143.214 1.00 32.84  ? 222  TYR A CZ  1 
ATOM   11182 O OH  . TYR B 2 222  ? 214.033 184.289 143.293 1.00 32.84  ? 222  TYR A OH  1 
ATOM   11183 N N   . PHE B 2 223  ? 209.193 189.248 140.668 1.00 32.84  ? 223  PHE A N   1 
ATOM   11184 C CA  . PHE B 2 223  ? 208.440 188.549 139.640 1.00 32.84  ? 223  PHE A CA  1 
ATOM   11185 C C   . PHE B 2 223  ? 208.443 189.294 138.319 1.00 32.84  ? 223  PHE A C   1 
ATOM   11186 O O   . PHE B 2 223  ? 208.167 188.684 137.284 1.00 32.84  ? 223  PHE A O   1 
ATOM   11187 C CB  . PHE B 2 223  ? 207.004 188.304 140.089 1.00 32.84  ? 223  PHE A CB  1 
ATOM   11188 C CG  . PHE B 2 223  ? 206.348 187.160 139.381 1.00 32.84  ? 223  PHE A CG  1 
ATOM   11189 C CD1 . PHE B 2 223  ? 207.106 186.098 138.925 1.00 32.84  ? 223  PHE A CD1 1 
ATOM   11190 C CD2 . PHE B 2 223  ? 204.985 187.142 139.164 1.00 32.84  ? 223  PHE A CD2 1 
ATOM   11191 C CE1 . PHE B 2 223  ? 206.516 185.038 138.270 1.00 32.84  ? 223  PHE A CE1 1 
ATOM   11192 C CE2 . PHE B 2 223  ? 204.387 186.085 138.510 1.00 32.84  ? 223  PHE A CE2 1 
ATOM   11193 C CZ  . PHE B 2 223  ? 205.156 185.031 138.062 1.00 32.84  ? 223  PHE A CZ  1 
ATOM   11194 N N   . SER B 2 224  ? 208.766 190.589 138.324 1.00 36.01  ? 224  SER A N   1 
ATOM   11195 C CA  . SER B 2 224  ? 208.787 191.344 137.076 1.00 36.01  ? 224  SER A CA  1 
ATOM   11196 C C   . SER B 2 224  ? 209.994 191.015 136.208 1.00 36.01  ? 224  SER A C   1 
ATOM   11197 O O   . SER B 2 224  ? 209.965 191.288 135.005 1.00 36.01  ? 224  SER A O   1 
ATOM   11198 C CB  . SER B 2 224  ? 208.757 192.842 137.368 1.00 36.01  ? 224  SER A CB  1 
ATOM   11199 O OG  . SER B 2 224  ? 208.105 193.545 136.327 1.00 36.01  ? 224  SER A OG  1 
ATOM   11200 N N   . GLU B 2 225  ? 211.049 190.439 136.784 1.00 40.23  ? 225  GLU A N   1 
ATOM   11201 C CA  . GLU B 2 225  ? 212.251 190.089 136.035 1.00 40.23  ? 225  GLU A CA  1 
ATOM   11202 C C   . GLU B 2 225  ? 212.274 188.624 135.617 1.00 40.23  ? 225  GLU A C   1 
ATOM   11203 O O   . GLU B 2 225  ? 213.350 188.088 135.327 1.00 40.23  ? 225  GLU A O   1 
ATOM   11204 C CB  . GLU B 2 225  ? 213.507 190.413 136.847 1.00 40.23  ? 225  GLU A CB  1 
ATOM   11205 C CG  . GLU B 2 225  ? 213.473 191.705 137.662 1.00 40.23  ? 225  GLU A CG  1 
ATOM   11206 C CD  . GLU B 2 225  ? 212.914 192.916 136.920 1.00 40.23  ? 225  GLU A CD  1 
ATOM   11207 O OE1 . GLU B 2 225  ? 212.494 193.871 137.603 1.00 40.23  ? 225  GLU A OE1 1 
ATOM   11208 O OE2 . GLU B 2 225  ? 212.943 192.956 135.670 1.00 40.23  ? 225  GLU A OE2 1 
ATOM   11209 N N   . PHE B 2 226  ? 211.121 187.965 135.582 1.00 37.98  ? 226  PHE A N   1 
ATOM   11210 C CA  . PHE B 2 226  ? 211.061 186.553 135.229 1.00 37.98  ? 226  PHE A CA  1 
ATOM   11211 C C   . PHE B 2 226  ? 210.059 186.214 134.139 1.00 37.98  ? 226  PHE A C   1 
ATOM   11212 O O   . PHE B 2 226  ? 210.263 185.215 133.439 1.00 37.98  ? 226  PHE A O   1 
ATOM   11213 C CB  . PHE B 2 226  ? 210.736 185.705 136.467 1.00 37.98  ? 226  PHE A CB  1 
ATOM   11214 C CG  . PHE B 2 226  ? 211.912 184.963 137.011 1.00 37.98  ? 226  PHE A CG  1 
ATOM   11215 C CD1 . PHE B 2 226  ? 212.632 184.107 136.204 1.00 37.98  ? 226  PHE A CD1 1 
ATOM   11216 C CD2 . PHE B 2 226  ? 212.300 185.123 138.327 1.00 37.98  ? 226  PHE A CD2 1 
ATOM   11217 C CE1 . PHE B 2 226  ? 213.717 183.423 136.698 1.00 37.98  ? 226  PHE A CE1 1 
ATOM   11218 C CE2 . PHE B 2 226  ? 213.382 184.439 138.827 1.00 37.98  ? 226  PHE A CE2 1 
ATOM   11219 C CZ  . PHE B 2 226  ? 214.091 183.587 138.013 1.00 37.98  ? 226  PHE A CZ  1 
ATOM   11220 N N   . LEU B 2 227  ? 208.999 186.991 133.969 1.00 42.31  ? 227  LEU A N   1 
ATOM   11221 C CA  . LEU B 2 227  ? 207.937 186.640 133.040 1.00 42.31  ? 227  LEU A CA  1 
ATOM   11222 C C   . LEU B 2 227  ? 208.181 187.298 131.686 1.00 42.31  ? 227  LEU A C   1 
ATOM   11223 O O   . LEU B 2 227  ? 208.928 188.271 131.564 1.00 42.31  ? 227  LEU A O   1 
ATOM   11224 C CB  . LEU B 2 227  ? 206.576 187.053 133.600 1.00 42.31  ? 227  LEU A CB  1 
ATOM   11225 C CG  . LEU B 2 227  ? 206.174 188.529 133.670 1.00 42.31  ? 227  LEU A CG  1 
ATOM   11226 C CD1 . LEU B 2 227  ? 204.724 188.628 134.114 1.00 42.31  ? 227  LEU A CD1 1 
ATOM   11227 C CD2 . LEU B 2 227  ? 207.063 189.381 134.548 1.00 42.31  ? 227  LEU A CD2 1 
ATOM   11228 N N   . SER B 2 228  ? 207.542 186.742 130.660 1.00 48.31  ? 228  SER A N   1 
ATOM   11229 C CA  . SER B 2 228  ? 207.746 187.211 129.297 1.00 48.31  ? 228  SER A CA  1 
ATOM   11230 C C   . SER B 2 228  ? 207.253 188.644 129.134 1.00 48.31  ? 228  SER A C   1 
ATOM   11231 O O   . SER B 2 228  ? 206.303 189.076 129.791 1.00 48.31  ? 228  SER A O   1 
ATOM   11232 C CB  . SER B 2 228  ? 207.030 186.291 128.311 1.00 48.31  ? 228  SER A CB  1 
ATOM   11233 O OG  . SER B 2 228  ? 207.236 184.932 128.652 1.00 48.31  ? 228  SER A OG  1 
ATOM   11234 N N   . ARG B 2 229  ? 207.919 189.385 128.243 1.00 53.03  ? 229  ARG A N   1 
ATOM   11235 C CA  . ARG B 2 229  ? 207.607 190.803 128.075 1.00 53.03  ? 229  ARG A CA  1 
ATOM   11236 C C   . ARG B 2 229  ? 206.187 191.010 127.562 1.00 53.03  ? 229  ARG A C   1 
ATOM   11237 O O   . ARG B 2 229  ? 205.460 191.873 128.066 1.00 53.03  ? 229  ARG A O   1 
ATOM   11238 C CB  . ARG B 2 229  ? 208.612 191.451 127.124 1.00 53.03  ? 229  ARG A CB  1 
ATOM   11239 C CG  . ARG B 2 229  ? 208.610 192.972 127.157 1.00 53.03  ? 229  ARG A CG  1 
ATOM   11240 C CD  . ARG B 2 229  ? 207.753 193.563 126.047 1.00 53.03  ? 229  ARG A CD  1 
ATOM   11241 N NE  . ARG B 2 229  ? 207.726 192.715 124.864 1.00 53.03  ? 229  ARG A NE  1 
ATOM   11242 C CZ  . ARG B 2 229  ? 208.635 192.747 123.898 1.00 53.03  ? 229  ARG A CZ  1 
ATOM   11243 N NH1 . ARG B 2 229  ? 209.668 193.572 123.950 1.00 53.03  ? 229  ARG A NH1 1 
ATOM   11244 N NH2 . ARG B 2 229  ? 208.505 191.932 122.855 1.00 53.03  ? 229  ARG A NH2 1 
ATOM   11245 N N   . GLU B 2 230  ? 205.780 190.239 126.552 1.00 52.18  ? 230  GLU A N   1 
ATOM   11246 C CA  . GLU B 2 230  ? 204.440 190.399 125.995 1.00 52.18  ? 230  GLU A CA  1 
ATOM   11247 C C   . GLU B 2 230  ? 203.373 190.004 127.006 1.00 52.18  ? 230  GLU A C   1 
ATOM   11248 O O   . GLU B 2 230  ? 202.421 190.755 127.247 1.00 52.18  ? 230  GLU A O   1 
ATOM   11249 C CB  . GLU B 2 230  ? 204.301 189.572 124.718 1.00 52.18  ? 230  GLU A CB  1 
ATOM   11250 C CG  . GLU B 2 230  ? 204.935 190.208 123.495 1.00 52.18  ? 230  GLU A CG  1 
ATOM   11251 C CD  . GLU B 2 230  ? 204.825 189.330 122.265 1.00 52.18  ? 230  GLU A CD  1 
ATOM   11252 O OE1 . GLU B 2 230  ? 205.318 188.183 122.306 1.00 52.18  ? 230  GLU A OE1 1 
ATOM   11253 O OE2 . GLU B 2 230  ? 204.245 189.785 121.258 1.00 52.18  ? 230  GLU A OE2 1 
ATOM   11254 N N   . LYS B 2 231  ? 203.520 188.830 127.611 1.00 45.66  ? 231  LYS A N   1 
ATOM   11255 C CA  . LYS B 2 231  ? 202.575 188.351 128.618 1.00 45.66  ? 231  LYS A CA  1 
ATOM   11256 C C   . LYS B 2 231  ? 202.998 188.779 130.018 1.00 45.66  ? 231  LYS A C   1 
ATOM   11257 O O   . LYS B 2 231  ? 203.108 187.969 130.936 1.00 45.66  ? 231  LYS A O   1 
ATOM   11258 C CB  . LYS B 2 231  ? 202.445 186.836 128.520 1.00 45.66  ? 231  LYS A CB  1 
ATOM   11259 C CG  . LYS B 2 231  ? 202.286 186.327 127.094 1.00 45.66  ? 231  LYS A CG  1 
ATOM   11260 C CD  . LYS B 2 231  ? 203.086 185.056 126.861 1.00 45.66  ? 231  LYS A CD  1 
ATOM   11261 C CE  . LYS B 2 231  ? 202.323 183.825 127.328 1.00 45.66  ? 231  LYS A CE  1 
ATOM   11262 N NZ  . LYS B 2 231  ? 203.173 182.604 127.307 1.00 45.66  ? 231  LYS A NZ  1 
ATOM   11263 N N   . ARG B 2 232  ? 203.240 190.079 130.184 1.00 43.02  ? 232  ARG A N   1 
ATOM   11264 C CA  . ARG B 2 232  ? 203.672 190.639 131.458 1.00 43.02  ? 232  ARG A CA  1 
ATOM   11265 C C   . ARG B 2 232  ? 202.527 191.236 132.263 1.00 43.02  ? 232  ARG A C   1 
ATOM   11266 O O   . ARG B 2 232  ? 202.485 191.068 133.486 1.00 43.02  ? 232  ARG A O   1 
ATOM   11267 C CB  . ARG B 2 232  ? 204.747 191.707 131.231 1.00 43.02  ? 232  ARG A CB  1 
ATOM   11268 C CG  . ARG B 2 232  ? 204.836 192.757 132.328 1.00 43.02  ? 232  ARG A CG  1 
ATOM   11269 C CD  . ARG B 2 232  ? 205.886 193.810 132.015 1.00 43.02  ? 232  ARG A CD  1 
ATOM   11270 N NE  . ARG B 2 232  ? 207.228 193.243 131.943 1.00 43.02  ? 232  ARG A NE  1 
ATOM   11271 C CZ  . ARG B 2 232  ? 208.345 193.927 132.140 1.00 43.02  ? 232  ARG A CZ  1 
ATOM   11272 N NH1 . ARG B 2 232  ? 208.322 195.218 132.428 1.00 43.02  ? 232  ARG A NH1 1 
ATOM   11273 N NH2 . ARG B 2 232  ? 209.516 193.305 132.043 1.00 43.02  ? 232  ARG A NH2 1 
ATOM   11274 N N   . GLY B 2 233  ? 201.595 191.921 131.604 1.00 41.79  ? 233  GLY A N   1 
ATOM   11275 C CA  . GLY B 2 233  ? 200.494 192.535 132.330 1.00 41.79  ? 233  GLY A CA  1 
ATOM   11276 C C   . GLY B 2 233  ? 199.577 191.519 132.983 1.00 41.79  ? 233  GLY A C   1 
ATOM   11277 O O   . GLY B 2 233  ? 199.125 191.719 134.114 1.00 41.79  ? 233  GLY A O   1 
ATOM   11278 N N   . GLU B 2 234  ? 199.295 190.419 132.289 1.00 41.23  ? 234  GLU A N   1 
ATOM   11279 C CA  . GLU B 2 234  ? 198.361 189.423 132.806 1.00 41.23  ? 234  GLU A CA  1 
ATOM   11280 C C   . GLU B 2 234  ? 198.869 188.810 134.105 1.00 41.23  ? 234  GLU A C   1 
ATOM   11281 O O   . GLU B 2 234  ? 198.245 188.961 135.164 1.00 41.23  ? 234  GLU A O   1 
ATOM   11282 C CB  . GLU B 2 234  ? 198.122 188.337 131.756 1.00 41.23  ? 234  GLU A CB  1 
ATOM   11283 C CG  . GLU B 2 234  ? 197.035 188.662 130.739 1.00 41.23  ? 234  GLU A CG  1 
ATOM   11284 C CD  . GLU B 2 234  ? 197.522 189.565 129.622 1.00 41.23  ? 234  GLU A CD  1 
ATOM   11285 O OE1 . GLU B 2 234  ? 198.154 190.601 129.916 1.00 41.23  ? 234  GLU A OE1 1 
ATOM   11286 O OE2 . GLU B 2 234  ? 197.273 189.236 128.442 1.00 41.23  ? 234  GLU A OE2 1 
ATOM   11287 N N   . HIS B 2 235  ? 200.015 188.131 134.044 1.00 40.97  ? 235  HIS A N   1 
ATOM   11288 C CA  . HIS B 2 235  ? 200.477 187.332 135.176 1.00 40.97  ? 235  HIS A CA  1 
ATOM   11289 C C   . HIS B 2 235  ? 200.686 188.192 136.413 1.00 40.97  ? 235  HIS A C   1 
ATOM   11290 O O   . HIS B 2 235  ? 200.255 187.830 137.515 1.00 40.97  ? 235  HIS A O   1 
ATOM   11291 C CB  . HIS B 2 235  ? 201.763 186.601 134.801 1.00 40.97  ? 235  HIS A CB  1 
ATOM   11292 C CG  . HIS B 2 235  ? 201.636 185.752 133.577 1.00 40.97  ? 235  HIS A CG  1 
ATOM   11293 N ND1 . HIS B 2 235  ? 201.458 186.282 132.318 1.00 40.97  ? 235  HIS A ND1 1 
ATOM   11294 C CD2 . HIS B 2 235  ? 201.653 184.409 133.420 1.00 40.97  ? 235  HIS A CD2 1 
ATOM   11295 C CE1 . HIS B 2 235  ? 201.375 185.303 131.437 1.00 40.97  ? 235  HIS A CE1 1 
ATOM   11296 N NE2 . HIS B 2 235  ? 201.492 184.155 132.079 1.00 40.97  ? 235  HIS A NE2 1 
ATOM   11297 N N   . LEU B 2 236  ? 201.337 189.347 136.246 1.00 36.43  ? 236  LEU A N   1 
ATOM   11298 C CA  . LEU B 2 236  ? 201.484 190.288 137.350 1.00 36.43  ? 236  LEU A CA  1 
ATOM   11299 C C   . LEU B 2 236  ? 200.132 190.609 137.968 1.00 36.43  ? 236  LEU A C   1 
ATOM   11300 O O   . LEU B 2 236  ? 199.956 190.540 139.190 1.00 36.43  ? 236  LEU A O   1 
ATOM   11301 C CB  . LEU B 2 236  ? 202.162 191.565 136.857 1.00 36.43  ? 236  LEU A CB  1 
ATOM   11302 C CG  . LEU B 2 236  ? 203.680 191.599 136.968 1.00 36.43  ? 236  LEU A CG  1 
ATOM   11303 C CD1 . LEU B 2 236  ? 204.187 192.973 136.604 1.00 36.43  ? 236  LEU A CD1 1 
ATOM   11304 C CD2 . LEU B 2 236  ? 204.091 191.234 138.373 1.00 36.43  ? 236  LEU A CD2 1 
ATOM   11305 N N   . SER B 2 237  ? 199.152 190.930 137.123 1.00 36.68  ? 237  SER A N   1 
ATOM   11306 C CA  . SER B 2 237  ? 197.802 191.183 137.609 1.00 36.68  ? 237  SER A CA  1 
ATOM   11307 C C   . SER B 2 237  ? 197.292 190.020 138.445 1.00 36.68  ? 237  SER A C   1 
ATOM   11308 O O   . SER B 2 237  ? 196.708 190.224 139.516 1.00 36.68  ? 237  SER A O   1 
ATOM   11309 C CB  . SER B 2 237  ? 196.868 191.438 136.432 1.00 36.68  ? 237  SER A CB  1 
ATOM   11310 O OG  . SER B 2 237  ? 196.489 190.211 135.839 1.00 36.68  ? 237  SER A OG  1 
ATOM   11311 N N   . TRP B 2 238  ? 197.526 188.789 137.983 1.00 36.86  ? 238  TRP A N   1 
ATOM   11312 C CA  . TRP B 2 238  ? 197.074 187.626 138.736 1.00 36.86  ? 238  TRP A CA  1 
ATOM   11313 C C   . TRP B 2 238  ? 197.647 187.634 140.146 1.00 36.86  ? 238  TRP A C   1 
ATOM   11314 O O   . TRP B 2 238  ? 196.934 187.345 141.114 1.00 36.86  ? 238  TRP A O   1 
ATOM   11315 C CB  . TRP B 2 238  ? 197.462 186.340 138.006 1.00 36.86  ? 238  TRP A CB  1 
ATOM   11316 C CG  . TRP B 2 238  ? 196.607 186.036 136.811 1.00 36.86  ? 238  TRP A CG  1 
ATOM   11317 C CD1 . TRP B 2 238  ? 197.028 185.886 135.523 1.00 36.86  ? 238  TRP A CD1 1 
ATOM   11318 C CD2 . TRP B 2 238  ? 195.189 185.841 136.795 1.00 36.86  ? 238  TRP A CD2 1 
ATOM   11319 N NE1 . TRP B 2 238  ? 195.960 185.609 134.706 1.00 36.86  ? 238  TRP A NE1 1 
ATOM   11320 C CE2 . TRP B 2 238  ? 194.819 185.578 135.463 1.00 36.86  ? 238  TRP A CE2 1 
ATOM   11321 C CE3 . TRP B 2 238  ? 194.196 185.863 137.778 1.00 36.86  ? 238  TRP A CE3 1 
ATOM   11322 C CZ2 . TRP B 2 238  ? 193.500 185.341 135.089 1.00 36.86  ? 238  TRP A CZ2 1 
ATOM   11323 C CZ3 . TRP B 2 238  ? 192.887 185.629 137.404 1.00 36.86  ? 238  TRP A CZ3 1 
ATOM   11324 C CH2 . TRP B 2 238  ? 192.551 185.371 136.071 1.00 36.86  ? 238  TRP A CH2 1 
ATOM   11325 N N   . LEU B 2 239  ? 198.923 188.006 140.283 1.00 31.84  ? 239  LEU A N   1 
ATOM   11326 C CA  . LEU B 2 239  ? 199.545 188.047 141.602 1.00 31.84  ? 239  LEU A CA  1 
ATOM   11327 C C   . LEU B 2 239  ? 198.724 188.890 142.565 1.00 31.84  ? 239  LEU A C   1 
ATOM   11328 O O   . LEU B 2 239  ? 198.568 188.536 143.741 1.00 31.84  ? 239  LEU A O   1 
ATOM   11329 C CB  . LEU B 2 239  ? 200.966 188.595 141.497 1.00 31.84  ? 239  LEU A CB  1 
ATOM   11330 C CG  . LEU B 2 239  ? 202.092 187.642 141.890 1.00 31.84  ? 239  LEU A CG  1 
ATOM   11331 C CD1 . LEU B 2 239  ? 203.408 188.381 141.952 1.00 31.84  ? 239  LEU A CD1 1 
ATOM   11332 C CD2 . LEU B 2 239  ? 201.781 186.981 143.208 1.00 31.84  ? 239  LEU A CD2 1 
ATOM   11333 N N   . GLY B 2 240  ? 198.150 189.987 142.064 1.00 32.00  ? 240  GLY A N   1 
ATOM   11334 C CA  . GLY B 2 240  ? 197.394 190.876 142.925 1.00 32.00  ? 240  GLY A CA  1 
ATOM   11335 C C   . GLY B 2 240  ? 196.309 190.161 143.700 1.00 32.00  ? 240  GLY A C   1 
ATOM   11336 O O   . GLY B 2 240  ? 196.080 190.450 144.878 1.00 32.00  ? 240  GLY A O   1 
ATOM   11337 N N   . ILE B 2 241  ? 195.654 189.179 143.068 1.00 32.01  ? 241  ILE A N   1 
ATOM   11338 C CA  . ILE B 2 241  ? 194.527 188.522 143.723 1.00 32.01  ? 241  ILE A CA  1 
ATOM   11339 C C   . ILE B 2 241  ? 194.977 187.874 145.022 1.00 32.01  ? 241  ILE A C   1 
ATOM   11340 O O   . ILE B 2 241  ? 194.257 187.913 146.029 1.00 32.01  ? 241  ILE A O   1 
ATOM   11341 C CB  . ILE B 2 241  ? 193.841 187.516 142.774 1.00 32.01  ? 241  ILE A CB  1 
ATOM   11342 C CG1 . ILE B 2 241  ? 194.470 186.126 142.861 1.00 32.01  ? 241  ILE A CG1 1 
ATOM   11343 C CG2 . ILE B 2 241  ? 193.855 188.026 141.343 1.00 32.01  ? 241  ILE A CG2 1 
ATOM   11344 C CD1 . ILE B 2 241  ? 193.736 185.083 142.060 1.00 32.01  ? 241  ILE A CD1 1 
ATOM   11345 N N   . PHE B 2 242  ? 196.200 187.333 145.049 1.00 33.14  ? 242  PHE A N   1 
ATOM   11346 C CA  . PHE B 2 242  ? 196.700 186.715 146.271 1.00 33.14  ? 242  PHE A CA  1 
ATOM   11347 C C   . PHE B 2 242  ? 196.638 187.702 147.426 1.00 33.14  ? 242  PHE A C   1 
ATOM   11348 O O   . PHE B 2 242  ? 196.118 187.383 148.503 1.00 33.14  ? 242  PHE A O   1 
ATOM   11349 C CB  . PHE B 2 242  ? 198.124 186.204 146.068 1.00 33.14  ? 242  PHE A CB  1 
ATOM   11350 C CG  . PHE B 2 242  ? 198.197 184.744 145.737 1.00 33.14  ? 242  PHE A CG  1 
ATOM   11351 C CD1 . PHE B 2 242  ? 198.042 184.308 144.434 1.00 33.14  ? 242  PHE A CD1 1 
ATOM   11352 C CD2 . PHE B 2 242  ? 198.406 183.808 146.728 1.00 33.14  ? 242  PHE A CD2 1 
ATOM   11353 C CE1 . PHE B 2 242  ? 198.101 182.967 144.128 1.00 33.14  ? 242  PHE A CE1 1 
ATOM   11354 C CE2 . PHE B 2 242  ? 198.466 182.466 146.429 1.00 33.14  ? 242  PHE A CE2 1 
ATOM   11355 C CZ  . PHE B 2 242  ? 198.314 182.046 145.127 1.00 33.14  ? 242  PHE A CZ  1 
ATOM   11356 N N   . TRP B 2 243  ? 197.113 188.928 147.191 1.00 34.60  ? 243  TRP A N   1 
ATOM   11357 C CA  . TRP B 2 243  ? 197.011 189.986 148.189 1.00 34.60  ? 243  TRP A CA  1 
ATOM   11358 C C   . TRP B 2 243  ? 195.605 190.036 148.768 1.00 34.60  ? 243  TRP A C   1 
ATOM   11359 O O   . TRP B 2 243  ? 195.405 189.873 149.976 1.00 34.60  ? 243  TRP A O   1 
ATOM   11360 C CB  . TRP B 2 243  ? 197.387 191.329 147.560 1.00 34.60  ? 243  TRP A CB  1 
ATOM   11361 C CG  . TRP B 2 243  ? 197.484 192.475 148.526 1.00 34.60  ? 243  TRP A CG  1 
ATOM   11362 C CD1 . TRP B 2 243  ? 197.179 192.463 149.858 1.00 34.60  ? 243  TRP A CD1 1 
ATOM   11363 C CD2 . TRP B 2 243  ? 197.902 193.812 148.226 1.00 34.60  ? 243  TRP A CD2 1 
ATOM   11364 N NE1 . TRP B 2 243  ? 197.389 193.704 150.403 1.00 34.60  ? 243  TRP A NE1 1 
ATOM   11365 C CE2 . TRP B 2 243  ? 197.833 194.550 149.422 1.00 34.60  ? 243  TRP A CE2 1 
ATOM   11366 C CE3 . TRP B 2 243  ? 198.332 194.453 147.060 1.00 34.60  ? 243  TRP A CE3 1 
ATOM   11367 C CZ2 . TRP B 2 243  ? 198.177 195.898 149.487 1.00 34.60  ? 243  TRP A CZ2 1 
ATOM   11368 C CZ3 . TRP B 2 243  ? 198.670 195.792 147.127 1.00 34.60  ? 243  TRP A CZ3 1 
ATOM   11369 C CH2 . TRP B 2 243  ? 198.592 196.499 148.332 1.00 34.60  ? 243  TRP A CH2 1 
ATOM   11370 N N   . MET B 2 244  ? 194.607 190.213 147.900 1.00 34.95  ? 244  MET A N   1 
ATOM   11371 C CA  . MET B 2 244  ? 193.241 190.308 148.388 1.00 34.95  ? 244  MET A CA  1 
ATOM   11372 C C   . MET B 2 244  ? 192.840 189.029 149.105 1.00 34.95  ? 244  MET A C   1 
ATOM   11373 O O   . MET B 2 244  ? 192.285 189.079 150.212 1.00 34.95  ? 244  MET A O   1 
ATOM   11374 C CB  . MET B 2 244  ? 192.295 190.618 147.232 1.00 34.95  ? 244  MET A CB  1 
ATOM   11375 C CG  . MET B 2 244  ? 192.421 192.048 146.731 1.00 34.95  ? 244  MET A CG  1 
ATOM   11376 S SD  . MET B 2 244  ? 193.071 193.162 147.991 1.00 34.95  ? 244  MET A SD  1 
ATOM   11377 C CE  . MET B 2 244  ? 193.897 194.386 146.977 1.00 34.95  ? 244  MET A CE  1 
ATOM   11378 N N   . THR B 2 245  ? 193.183 187.874 148.524 1.00 33.24  ? 245  THR A N   1 
ATOM   11379 C CA  . THR B 2 245  ? 192.882 186.603 149.172 1.00 33.24  ? 245  THR A CA  1 
ATOM   11380 C C   . THR B 2 245  ? 193.400 186.597 150.599 1.00 33.24  ? 245  THR A C   1 
ATOM   11381 O O   . THR B 2 245  ? 192.698 186.160 151.521 1.00 33.24  ? 245  THR A O   1 
ATOM   11382 C CB  . THR B 2 245  ? 193.481 185.446 148.373 1.00 33.24  ? 245  THR A CB  1 
ATOM   11383 O OG1 . THR B 2 245  ? 192.616 185.119 147.279 1.00 33.24  ? 245  THR A OG1 1 
ATOM   11384 C CG2 . THR B 2 245  ? 193.665 184.217 149.250 1.00 33.24  ? 245  THR A CG2 1 
ATOM   11385 N N   . GLY B 2 246  ? 194.598 187.151 150.806 1.00 34.94  ? 246  GLY A N   1 
ATOM   11386 C CA  . GLY B 2 246  ? 195.141 187.232 152.149 1.00 34.94  ? 246  GLY A CA  1 
ATOM   11387 C C   . GLY B 2 246  ? 194.148 187.799 153.134 1.00 34.94  ? 246  GLY A C   1 
ATOM   11388 O O   . GLY B 2 246  ? 193.756 187.129 154.097 1.00 34.94  ? 246  GLY A O   1 
ATOM   11389 N N   . GLY B 2 247  ? 193.658 189.010 152.860 1.00 35.06  ? 247  GLY A N   1 
ATOM   11390 C CA  . GLY B 2 247  ? 192.701 189.613 153.767 1.00 35.06  ? 247  GLY A CA  1 
ATOM   11391 C C   . GLY B 2 247  ? 191.519 188.701 154.003 1.00 35.06  ? 247  GLY A C   1 
ATOM   11392 O O   . GLY B 2 247  ? 191.162 188.413 155.148 1.00 35.06  ? 247  GLY A O   1 
ATOM   11393 N N   . LEU B 2 248  ? 190.974 188.144 152.918 1.00 34.07  ? 248  LEU A N   1 
ATOM   11394 C CA  . LEU B 2 248  ? 189.846 187.233 153.041 1.00 34.07  ? 248  LEU A CA  1 
ATOM   11395 C C   . LEU B 2 248  ? 190.173 186.122 154.022 1.00 34.07  ? 248  LEU A C   1 
ATOM   11396 O O   . LEU B 2 248  ? 189.471 185.934 155.024 1.00 34.07  ? 248  LEU A O   1 
ATOM   11397 C CB  . LEU B 2 248  ? 189.487 186.671 151.661 1.00 34.07  ? 248  LEU A CB  1 
ATOM   11398 C CG  . LEU B 2 248  ? 188.579 185.451 151.515 1.00 34.07  ? 248  LEU A CG  1 
ATOM   11399 C CD1 . LEU B 2 248  ? 187.736 185.596 150.262 1.00 34.07  ? 248  LEU A CD1 1 
ATOM   11400 C CD2 . LEU B 2 248  ? 189.393 184.175 151.436 1.00 34.07  ? 248  LEU A CD2 1 
ATOM   11401 N N   . TYR B 2 249  ? 191.303 185.445 153.809 1.00 35.90  ? 249  TYR A N   1 
ATOM   11402 C CA  . TYR B 2 249  ? 191.673 184.359 154.705 1.00 35.90  ? 249  TYR A CA  1 
ATOM   11403 C C   . TYR B 2 249  ? 191.857 184.887 156.116 1.00 35.90  ? 249  TYR A C   1 
ATOM   11404 O O   . TYR B 2 249  ? 191.272 184.360 157.073 1.00 35.90  ? 249  TYR A O   1 
ATOM   11405 C CB  . TYR B 2 249  ? 192.937 183.669 154.190 1.00 35.90  ? 249  TYR A CB  1 
ATOM   11406 C CG  . TYR B 2 249  ? 193.845 183.094 155.250 1.00 35.90  ? 249  TYR A CG  1 
ATOM   11407 C CD1 . TYR B 2 249  ? 193.655 181.808 155.728 1.00 35.90  ? 249  TYR A CD1 1 
ATOM   11408 C CD2 . TYR B 2 249  ? 194.916 183.822 155.747 1.00 35.90  ? 249  TYR A CD2 1 
ATOM   11409 C CE1 . TYR B 2 249  ? 194.490 181.272 156.687 1.00 35.90  ? 249  TYR A CE1 1 
ATOM   11410 C CE2 . TYR B 2 249  ? 195.756 183.295 156.705 1.00 35.90  ? 249  TYR A CE2 1 
ATOM   11411 C CZ  . TYR B 2 249  ? 195.539 182.020 157.171 1.00 35.90  ? 249  TYR A CZ  1 
ATOM   11412 O OH  . TYR B 2 249  ? 196.374 181.491 158.127 1.00 35.90  ? 249  TYR A OH  1 
ATOM   11413 N N   . ALA B 2 250  ? 192.581 186.003 156.248 1.00 37.39  ? 250  ALA A N   1 
ATOM   11414 C CA  . ALA B 2 250  ? 192.807 186.570 157.569 1.00 37.39  ? 250  ALA A CA  1 
ATOM   11415 C C   . ALA B 2 250  ? 191.495 186.949 158.230 1.00 37.39  ? 250  ALA A C   1 
ATOM   11416 O O   . ALA B 2 250  ? 191.371 186.864 159.457 1.00 37.39  ? 250  ALA A O   1 
ATOM   11417 C CB  . ALA B 2 250  ? 193.727 187.785 157.476 1.00 37.39  ? 250  ALA A CB  1 
ATOM   11418 N N   . SER B 2 251  ? 190.506 187.363 157.440 1.00 38.17  ? 251  SER A N   1 
ATOM   11419 C CA  . SER B 2 251  ? 189.200 187.642 158.020 1.00 38.17  ? 251  SER A CA  1 
ATOM   11420 C C   . SER B 2 251  ? 188.476 186.349 158.366 1.00 38.17  ? 251  SER A C   1 
ATOM   11421 O O   . SER B 2 251  ? 187.953 186.200 159.475 1.00 38.17  ? 251  SER A O   1 
ATOM   11422 C CB  . SER B 2 251  ? 188.370 188.491 157.061 1.00 38.17  ? 251  SER A CB  1 
ATOM   11423 O OG  . SER B 2 251  ? 187.029 188.580 157.505 1.00 38.17  ? 251  SER A OG  1 
ATOM   11424 N N   . ALA B 2 252  ? 188.489 185.382 157.443 1.00 40.08  ? 252  ALA A N   1 
ATOM   11425 C CA  . ALA B 2 252  ? 187.627 184.215 157.589 1.00 40.08  ? 252  ALA A CA  1 
ATOM   11426 C C   . ALA B 2 252  ? 187.971 183.436 158.845 1.00 40.08  ? 252  ALA A C   1 
ATOM   11427 O O   . ALA B 2 252  ? 187.082 182.953 159.555 1.00 40.08  ? 252  ALA A O   1 
ATOM   11428 C CB  . ALA B 2 252  ? 187.740 183.318 156.359 1.00 40.08  ? 252  ALA A CB  1 
ATOM   11429 N N   . MET B 2 253  ? 189.260 183.311 159.138 1.00 42.31  ? 253  MET A N   1 
ATOM   11430 C CA  . MET B 2 253  ? 189.699 182.617 160.336 1.00 42.31  ? 253  MET A CA  1 
ATOM   11431 C C   . MET B 2 253  ? 189.502 183.460 161.589 1.00 42.31  ? 253  MET A C   1 
ATOM   11432 O O   . MET B 2 253  ? 189.223 182.909 162.661 1.00 42.31  ? 253  MET A O   1 
ATOM   11433 C CB  . MET B 2 253  ? 191.159 182.205 160.161 1.00 42.31  ? 253  MET A CB  1 
ATOM   11434 C CG  . MET B 2 253  ? 192.021 182.266 161.390 1.00 42.31  ? 253  MET A CG  1 
ATOM   11435 S SD  . MET B 2 253  ? 193.704 181.863 160.905 1.00 42.31  ? 253  MET A SD  1 
ATOM   11436 C CE  . MET B 2 253  ? 193.438 180.293 160.084 1.00 42.31  ? 253  MET A CE  1 
ATOM   11437 N N   . ALA B 2 254  ? 189.598 184.789 161.470 1.00 43.28  ? 254  ALA A N   1 
ATOM   11438 C CA  . ALA B 2 254  ? 189.584 185.639 162.657 1.00 43.28  ? 254  ALA A CA  1 
ATOM   11439 C C   . ALA B 2 254  ? 188.290 185.478 163.441 1.00 43.28  ? 254  ALA A C   1 
ATOM   11440 O O   . ALA B 2 254  ? 188.313 185.191 164.645 1.00 43.28  ? 254  ALA A O   1 
ATOM   11441 C CB  . ALA B 2 254  ? 189.790 187.100 162.260 1.00 43.28  ? 254  ALA A CB  1 
ATOM   11442 N N   . TRP B 2 255  ? 187.145 185.619 162.769 1.00 43.43  ? 255  TRP A N   1 
ATOM   11443 C CA  . TRP B 2 255  ? 185.875 185.475 163.465 1.00 43.43  ? 255  TRP A CA  1 
ATOM   11444 C C   . TRP B 2 255  ? 185.694 184.076 164.029 1.00 43.43  ? 255  TRP A C   1 
ATOM   11445 O O   . TRP B 2 255  ? 184.891 183.885 164.946 1.00 43.43  ? 255  TRP A O   1 
ATOM   11446 C CB  . TRP B 2 255  ? 184.710 185.853 162.536 1.00 43.43  ? 255  TRP A CB  1 
ATOM   11447 C CG  . TRP B 2 255  ? 184.222 184.794 161.567 1.00 43.43  ? 255  TRP A CG  1 
ATOM   11448 C CD1 . TRP B 2 255  ? 183.746 183.546 161.866 1.00 43.43  ? 255  TRP A CD1 1 
ATOM   11449 C CD2 . TRP B 2 255  ? 184.150 184.911 160.141 1.00 43.43  ? 255  TRP A CD2 1 
ATOM   11450 N NE1 . TRP B 2 255  ? 183.395 182.883 160.719 1.00 43.43  ? 255  TRP A NE1 1 
ATOM   11451 C CE2 . TRP B 2 255  ? 183.631 183.699 159.645 1.00 43.43  ? 255  TRP A CE2 1 
ATOM   11452 C CE3 . TRP B 2 255  ? 184.478 185.922 159.235 1.00 43.43  ? 255  TRP A CE3 1 
ATOM   11453 C CZ2 . TRP B 2 255  ? 183.434 183.471 158.286 1.00 43.43  ? 255  TRP A CZ2 1 
ATOM   11454 C CZ3 . TRP B 2 255  ? 184.280 185.693 157.887 1.00 43.43  ? 255  TRP A CZ3 1 
ATOM   11455 C CH2 . TRP B 2 255  ? 183.764 184.478 157.425 1.00 43.43  ? 255  TRP A CH2 1 
ATOM   11456 N N   . SER B 2 256  ? 186.417 183.092 163.495 1.00 46.10  ? 256  SER A N   1 
ATOM   11457 C CA  . SER B 2 256  ? 186.338 181.746 164.042 1.00 46.10  ? 256  SER A CA  1 
ATOM   11458 C C   . SER B 2 256  ? 187.131 181.603 165.330 1.00 46.10  ? 256  SER A C   1 
ATOM   11459 O O   . SER B 2 256  ? 186.775 180.783 166.182 1.00 46.10  ? 256  SER A O   1 
ATOM   11460 C CB  . SER B 2 256  ? 186.822 180.730 163.010 1.00 46.10  ? 256  SER A CB  1 
ATOM   11461 O OG  . SER B 2 256  ? 185.761 180.316 162.169 1.00 46.10  ? 256  SER A OG  1 
ATOM   11462 N N   . ILE B 2 257  ? 188.197 182.384 165.500 1.00 48.39  ? 257  ILE A N   1 
ATOM   11463 C CA  . ILE B 2 257  ? 189.123 182.218 166.611 1.00 48.39  ? 257  ILE A CA  1 
ATOM   11464 C C   . ILE B 2 257  ? 188.913 183.281 167.682 1.00 48.39  ? 257  ILE A C   1 
ATOM   11465 O O   . ILE B 2 257  ? 188.790 182.964 168.865 1.00 48.39  ? 257  ILE A O   1 
ATOM   11466 C CB  . ILE B 2 257  ? 190.587 182.210 166.115 1.00 48.39  ? 257  ILE A CB  1 
ATOM   11467 C CG1 . ILE B 2 257  ? 190.912 180.875 165.446 1.00 48.39  ? 257  ILE A CG1 1 
ATOM   11468 C CG2 . ILE B 2 257  ? 191.537 182.464 167.266 1.00 48.39  ? 257  ILE A CG2 1 
ATOM   11469 C CD1 . ILE B 2 257  ? 192.392 180.609 165.298 1.00 48.39  ? 257  ILE A CD1 1 
ATOM   11470 N N   . ILE B 2 258  ? 188.856 184.548 167.286 1.00 50.92  ? 258  ILE A N   1 
ATOM   11471 C CA  . ILE B 2 258  ? 188.777 185.631 168.265 1.00 50.92  ? 258  ILE A CA  1 
ATOM   11472 C C   . ILE B 2 258  ? 187.602 186.558 167.976 1.00 50.92  ? 258  ILE A C   1 
ATOM   11473 O O   . ILE B 2 258  ? 187.814 187.734 167.643 1.00 50.92  ? 258  ILE A O   1 
ATOM   11474 C CB  . ILE B 2 258  ? 190.093 186.424 168.312 1.00 50.92  ? 258  ILE A CB  1 
ATOM   11475 C CG1 . ILE B 2 258  ? 190.609 186.699 166.900 1.00 50.92  ? 258  ILE A CG1 1 
ATOM   11476 C CG2 . ILE B 2 258  ? 191.134 185.678 169.116 1.00 50.92  ? 258  ILE A CG2 1 
ATOM   11477 C CD1 . ILE B 2 258  ? 191.592 187.841 166.830 1.00 50.92  ? 258  ILE A CD1 1 
ATOM   11478 N N   . PRO B 2 259  ? 186.354 186.096 168.099 1.00 51.84  ? 259  PRO A N   1 
ATOM   11479 C CA  . PRO B 2 259  ? 185.198 186.992 168.020 1.00 51.84  ? 259  PRO A CA  1 
ATOM   11480 C C   . PRO B 2 259  ? 184.819 187.562 169.384 1.00 51.84  ? 259  PRO A C   1 
ATOM   11481 O O   . PRO B 2 259  ? 183.663 187.497 169.807 1.00 51.84  ? 259  PRO A O   1 
ATOM   11482 C CB  . PRO B 2 259  ? 184.106 186.081 167.455 1.00 51.84  ? 259  PRO A CB  1 
ATOM   11483 C CG  . PRO B 2 259  ? 184.436 184.736 168.027 1.00 51.84  ? 259  PRO A CG  1 
ATOM   11484 C CD  . PRO B 2 259  ? 185.926 184.705 168.330 1.00 51.84  ? 259  PRO A CD  1 
ATOM   11485 N N   . HIS B 2 260  ? 185.804 188.104 170.096 1.00 56.57  ? 260  HIS A N   1 
ATOM   11486 C CA  . HIS B 2 260  ? 185.568 188.674 171.419 1.00 56.57  ? 260  HIS A CA  1 
ATOM   11487 C C   . HIS B 2 260  ? 186.550 189.819 171.613 1.00 56.57  ? 260  HIS A C   1 
ATOM   11488 O O   . HIS B 2 260  ? 187.741 189.581 171.826 1.00 56.57  ? 260  HIS A O   1 
ATOM   11489 C CB  . HIS B 2 260  ? 185.728 187.624 172.515 1.00 56.57  ? 260  HIS A CB  1 
ATOM   11490 C CG  . HIS B 2 260  ? 184.724 186.516 172.446 1.00 56.57  ? 260  HIS A CG  1 
ATOM   11491 N ND1 . HIS B 2 260  ? 183.409 186.725 172.096 1.00 56.57  ? 260  HIS A ND1 1 
ATOM   11492 C CD2 . HIS B 2 260  ? 184.844 185.190 172.684 1.00 56.57  ? 260  HIS A CD2 1 
ATOM   11493 C CE1 . HIS B 2 260  ? 182.759 185.575 172.118 1.00 56.57  ? 260  HIS A CE1 1 
ATOM   11494 N NE2 . HIS B 2 260  ? 183.608 184.626 172.472 1.00 56.57  ? 260  HIS A NE2 1 
ATOM   11495 N N   . TYR B 2 261  ? 186.054 191.049 171.548 1.00 60.18  ? 261  TYR A N   1 
ATOM   11496 C CA  . TYR B 2 261  ? 186.924 192.205 171.686 1.00 60.18  ? 261  TYR A CA  1 
ATOM   11497 C C   . TYR B 2 261  ? 187.416 192.335 173.125 1.00 60.18  ? 261  TYR A C   1 
ATOM   11498 O O   . TYR B 2 261  ? 186.900 191.702 174.049 1.00 60.18  ? 261  TYR A O   1 
ATOM   11499 C CB  . TYR B 2 261  ? 186.211 193.491 171.257 1.00 60.18  ? 261  TYR A CB  1 
ATOM   11500 C CG  . TYR B 2 261  ? 184.874 193.775 171.921 1.00 60.18  ? 261  TYR A CG  1 
ATOM   11501 C CD1 . TYR B 2 261  ? 183.794 192.912 171.782 1.00 60.18  ? 261  TYR A CD1 1 
ATOM   11502 C CD2 . TYR B 2 261  ? 184.695 194.919 172.683 1.00 60.18  ? 261  TYR A CD2 1 
ATOM   11503 C CE1 . TYR B 2 261  ? 182.583 193.183 172.384 1.00 60.18  ? 261  TYR A CE1 1 
ATOM   11504 C CE2 . TYR B 2 261  ? 183.489 195.196 173.289 1.00 60.18  ? 261  TYR A CE2 1 
ATOM   11505 C CZ  . TYR B 2 261  ? 182.435 194.326 173.137 1.00 60.18  ? 261  TYR A CZ  1 
ATOM   11506 O OH  . TYR B 2 261  ? 181.231 194.601 173.740 1.00 60.18  ? 261  TYR A OH  1 
ATOM   11507 N N   . GLY B 2 262  ? 188.431 193.173 173.305 1.00 62.66  ? 262  GLY A N   1 
ATOM   11508 C CA  . GLY B 2 262  ? 189.036 193.378 174.602 1.00 62.66  ? 262  GLY A CA  1 
ATOM   11509 C C   . GLY B 2 262  ? 190.142 192.415 174.961 1.00 62.66  ? 262  GLY A C   1 
ATOM   11510 O O   . GLY B 2 262  ? 190.650 192.478 176.087 1.00 62.66  ? 262  GLY A O   1 
ATOM   11511 N N   . TRP B 2 263  ? 190.534 191.523 174.050 1.00 61.93  ? 263  TRP A N   1 
ATOM   11512 C CA  . TRP B 2 263  ? 191.600 190.577 174.356 1.00 61.93  ? 263  TRP A CA  1 
ATOM   11513 C C   . TRP B 2 263  ? 192.967 191.242 174.442 1.00 61.93  ? 263  TRP A C   1 
ATOM   11514 O O   . TRP B 2 263  ? 193.911 190.621 174.940 1.00 61.93  ? 263  TRP A O   1 
ATOM   11515 C CB  . TRP B 2 263  ? 191.640 189.459 173.314 1.00 61.93  ? 263  TRP A CB  1 
ATOM   11516 C CG  . TRP B 2 263  ? 191.689 189.928 171.887 1.00 61.93  ? 263  TRP A CG  1 
ATOM   11517 C CD1 . TRP B 2 263  ? 190.637 190.047 171.031 1.00 61.93  ? 263  TRP A CD1 1 
ATOM   11518 C CD2 . TRP B 2 263  ? 192.854 190.319 171.147 1.00 61.93  ? 263  TRP A CD2 1 
ATOM   11519 N NE1 . TRP B 2 263  ? 191.070 190.494 169.805 1.00 61.93  ? 263  TRP A NE1 1 
ATOM   11520 C CE2 . TRP B 2 263  ? 192.427 190.669 169.852 1.00 61.93  ? 263  TRP A CE2 1 
ATOM   11521 C CE3 . TRP B 2 263  ? 194.214 190.413 171.458 1.00 61.93  ? 263  TRP A CE3 1 
ATOM   11522 C CZ2 . TRP B 2 263  ? 193.311 191.100 168.867 1.00 61.93  ? 263  TRP A CZ2 1 
ATOM   11523 C CZ3 . TRP B 2 263  ? 195.089 190.842 170.477 1.00 61.93  ? 263  TRP A CZ3 1 
ATOM   11524 C CH2 . TRP B 2 263  ? 194.634 191.182 169.201 1.00 61.93  ? 263  TRP A CH2 1 
ATOM   11525 N N   . GLY B 2 264  ? 193.098 192.476 173.970 1.00 64.59  ? 264  GLY A N   1 
ATOM   11526 C CA  . GLY B 2 264  ? 194.377 193.156 173.999 1.00 64.59  ? 264  GLY A CA  1 
ATOM   11527 C C   . GLY B 2 264  ? 194.690 193.778 175.344 1.00 64.59  ? 264  GLY A C   1 
ATOM   11528 O O   . GLY B 2 264  ? 195.716 193.471 175.956 1.00 64.59  ? 264  GLY A O   1 
ATOM   11529 N N   . PHE B 2 265  ? 193.805 194.652 175.815 1.00 69.78  ? 265  PHE A N   1 
ATOM   11530 C CA  . PHE B 2 265  ? 194.018 195.338 177.083 1.00 69.78  ? 265  PHE A CA  1 
ATOM   11531 C C   . PHE B 2 265  ? 193.536 194.496 178.257 1.00 69.78  ? 265  PHE A C   1 
ATOM   11532 O O   . PHE B 2 265  ? 192.710 194.951 179.053 1.00 69.78  ? 265  PHE A O   1 
ATOM   11533 C CB  . PHE B 2 265  ? 193.303 196.690 177.082 1.00 69.78  ? 265  PHE A CB  1 
ATOM   11534 C CG  . PHE B 2 265  ? 194.199 197.850 176.769 1.00 69.78  ? 265  PHE A CG  1 
ATOM   11535 C CD1 . PHE B 2 265  ? 195.444 197.960 177.363 1.00 69.78  ? 265  PHE A CD1 1 
ATOM   11536 C CD2 . PHE B 2 265  ? 193.799 198.826 175.875 1.00 69.78  ? 265  PHE A CD2 1 
ATOM   11537 C CE1 . PHE B 2 265  ? 196.271 199.028 177.074 1.00 69.78  ? 265  PHE A CE1 1 
ATOM   11538 C CE2 . PHE B 2 265  ? 194.621 199.894 175.580 1.00 69.78  ? 265  PHE A CE2 1 
ATOM   11539 C CZ  . PHE B 2 265  ? 195.857 199.995 176.182 1.00 69.78  ? 265  PHE A CZ  1 
ATOM   11540 N N   . SER B 2 266  ? 194.046 193.270 178.378 1.00 74.44  ? 266  SER A N   1 
ATOM   11541 C CA  . SER B 2 266  ? 193.691 192.414 179.508 1.00 74.44  ? 266  SER A CA  1 
ATOM   11542 C C   . SER B 2 266  ? 194.808 191.393 179.698 1.00 74.44  ? 266  SER A C   1 
ATOM   11543 O O   . SER B 2 266  ? 194.936 190.456 178.903 1.00 74.44  ? 266  SER A O   1 
ATOM   11544 C CB  . SER B 2 266  ? 192.345 191.737 179.286 1.00 74.44  ? 266  SER A CB  1 
ATOM   11545 O OG  . SER B 2 266  ? 191.278 192.629 179.563 1.00 74.44  ? 266  SER A OG  1 
ATOM   11546 N N   . MET B 2 267  ? 195.597 191.577 180.758 1.00 81.30  ? 267  MET A N   1 
ATOM   11547 C CA  . MET B 2 267  ? 196.639 190.639 181.143 1.00 81.30  ? 267  MET A CA  1 
ATOM   11548 C C   . MET B 2 267  ? 196.409 189.999 182.504 1.00 81.30  ? 267  MET A C   1 
ATOM   11549 O O   . MET B 2 267  ? 197.167 189.100 182.882 1.00 81.30  ? 267  MET A O   1 
ATOM   11550 C CB  . MET B 2 267  ? 198.015 191.328 181.144 1.00 81.30  ? 267  MET A CB  1 
ATOM   11551 C CG  . MET B 2 267  ? 199.183 190.512 180.569 1.00 81.30  ? 267  MET A CG  1 
ATOM   11552 S SD  . MET B 2 267  ? 198.999 189.469 179.094 1.00 81.30  ? 267  MET A SD  1 
ATOM   11553 C CE  . MET B 2 267  ? 197.921 190.417 178.022 1.00 81.30  ? 267  MET A CE  1 
ATOM   11554 N N   . GLY B 2 268  ? 195.391 190.431 183.245 1.00 84.01  ? 268  GLY A N   1 
ATOM   11555 C CA  . GLY B 2 268  ? 195.072 189.820 184.518 1.00 84.01  ? 268  GLY A CA  1 
ATOM   11556 C C   . GLY B 2 268  ? 194.302 188.528 184.430 1.00 84.01  ? 268  GLY A C   1 
ATOM   11557 O O   . GLY B 2 268  ? 194.011 187.914 185.462 1.00 84.01  ? 268  GLY A O   1 
ATOM   11558 N N   . THR B 2 269  ? 193.962 188.093 183.222 1.00 90.83  ? 269  THR A N   1 
ATOM   11559 C CA  . THR B 2 269  ? 193.233 186.850 183.028 1.00 90.83  ? 269  THR A CA  1 
ATOM   11560 C C   . THR B 2 269  ? 194.176 185.653 183.144 1.00 90.83  ? 269  THR A C   1 
ATOM   11561 O O   . THR B 2 269  ? 195.401 185.789 183.180 1.00 90.83  ? 269  THR A O   1 
ATOM   11562 C CB  . THR B 2 269  ? 192.533 186.847 181.669 1.00 90.83  ? 269  THR A CB  1 
ATOM   11563 O OG1 . THR B 2 269  ? 191.645 185.724 181.591 1.00 90.83  ? 269  THR A OG1 1 
ATOM   11564 C CG2 . THR B 2 269  ? 193.551 186.761 180.544 1.00 90.83  ? 269  THR A CG2 1 
ATOM   11565 N N   . ASN B 2 270  ? 193.580 184.465 183.201 1.00 92.42  ? 270  ASN A N   1 
ATOM   11566 C CA  . ASN B 2 270  ? 194.338 183.230 183.338 1.00 92.42  ? 270  ASN A CA  1 
ATOM   11567 C C   . ASN B 2 270  ? 195.131 182.954 182.060 1.00 92.42  ? 270  ASN A C   1 
ATOM   11568 O O   . ASN B 2 270  ? 195.065 183.696 181.076 1.00 92.42  ? 270  ASN A O   1 
ATOM   11569 C CB  . ASN B 2 270  ? 193.393 182.075 183.663 1.00 92.42  ? 270  ASN A CB  1 
ATOM   11570 C CG  . ASN B 2 270  ? 194.106 180.894 184.287 1.00 92.42  ? 270  ASN A CG  1 
ATOM   11571 O OD1 . ASN B 2 270  ? 195.151 181.046 184.916 1.00 92.42  ? 270  ASN A OD1 1 
ATOM   11572 N ND2 . ASN B 2 270  ? 193.543 179.704 184.107 1.00 92.42  ? 270  ASN A ND2 1 
ATOM   11573 N N   . TYR B 2 271  ? 195.903 181.865 182.078 1.00 92.18  ? 271  TYR A N   1 
ATOM   11574 C CA  . TYR B 2 271  ? 196.624 181.434 180.888 1.00 92.18  ? 271  TYR A CA  1 
ATOM   11575 C C   . TYR B 2 271  ? 195.695 180.956 179.784 1.00 92.18  ? 271  TYR A C   1 
ATOM   11576 O O   . TYR B 2 271  ? 196.145 180.794 178.644 1.00 92.18  ? 271  TYR A O   1 
ATOM   11577 C CB  . TYR B 2 271  ? 197.621 180.331 181.240 1.00 92.18  ? 271  TYR A CB  1 
ATOM   11578 C CG  . TYR B 2 271  ? 198.943 180.454 180.517 1.00 92.18  ? 271  TYR A CG  1 
ATOM   11579 C CD1 . TYR B 2 271  ? 199.913 181.351 180.947 1.00 92.18  ? 271  TYR A CD1 1 
ATOM   11580 C CD2 . TYR B 2 271  ? 199.220 179.676 179.402 1.00 92.18  ? 271  TYR A CD2 1 
ATOM   11581 C CE1 . TYR B 2 271  ? 201.124 181.465 180.290 1.00 92.18  ? 271  TYR A CE1 1 
ATOM   11582 C CE2 . TYR B 2 271  ? 200.427 179.783 178.737 1.00 92.18  ? 271  TYR A CE2 1 
ATOM   11583 C CZ  . TYR B 2 271  ? 201.376 180.680 179.186 1.00 92.18  ? 271  TYR A CZ  1 
ATOM   11584 O OH  . TYR B 2 271  ? 202.582 180.793 178.529 1.00 92.18  ? 271  TYR A OH  1 
ATOM   11585 N N   . HIS B 2 272  ? 194.421 180.729 180.093 1.00 88.75  ? 272  HIS A N   1 
ATOM   11586 C CA  . HIS B 2 272  ? 193.413 180.469 179.074 1.00 88.75  ? 272  HIS A CA  1 
ATOM   11587 C C   . HIS B 2 272  ? 193.031 181.796 178.430 1.00 88.75  ? 272  HIS A C   1 
ATOM   11588 O O   . HIS B 2 272  ? 193.711 182.812 178.600 1.00 88.75  ? 272  HIS A O   1 
ATOM   11589 C CB  . HIS B 2 272  ? 192.212 179.743 179.675 1.00 88.75  ? 272  HIS A CB  1 
ATOM   11590 C CG  . HIS B 2 272  ? 192.353 178.255 179.679 1.00 88.75  ? 272  HIS A CG  1 
ATOM   11591 N ND1 . HIS B 2 272  ? 193.344 177.606 180.383 1.00 88.75  ? 272  HIS A ND1 1 
ATOM   11592 C CD2 . HIS B 2 272  ? 191.639 177.287 179.055 1.00 88.75  ? 272  HIS A CD2 1 
ATOM   11593 C CE1 . HIS B 2 272  ? 193.234 176.302 180.196 1.00 88.75  ? 272  HIS A CE1 1 
ATOM   11594 N NE2 . HIS B 2 272  ? 192.206 176.084 179.395 1.00 88.75  ? 272  HIS A NE2 1 
ATOM   11595 N N   . PHE B 2 273  ? 191.951 181.793 177.647 1.00 78.83  ? 273  PHE A N   1 
ATOM   11596 C CA  . PHE B 2 273  ? 191.528 182.961 176.880 1.00 78.83  ? 273  PHE A CA  1 
ATOM   11597 C C   . PHE B 2 273  ? 192.592 183.343 175.848 1.00 78.83  ? 273  PHE A C   1 
ATOM   11598 O O   . PHE B 2 273  ? 192.489 184.358 175.164 1.00 78.83  ? 273  PHE A O   1 
ATOM   11599 C CB  . PHE B 2 273  ? 191.147 184.092 177.865 1.00 78.83  ? 273  PHE A CB  1 
ATOM   11600 C CG  . PHE B 2 273  ? 190.829 185.429 177.245 1.00 78.83  ? 273  PHE A CG  1 
ATOM   11601 C CD1 . PHE B 2 273  ? 191.829 186.321 176.893 1.00 78.83  ? 273  PHE A CD1 1 
ATOM   11602 C CD2 . PHE B 2 273  ? 189.529 185.878 177.243 1.00 78.83  ? 273  PHE A CD2 1 
ATOM   11603 C CE1 . PHE B 2 273  ? 191.520 187.554 176.379 1.00 78.83  ? 273  PHE A CE1 1 
ATOM   11604 C CE2 . PHE B 2 273  ? 189.216 187.109 176.738 1.00 78.83  ? 273  PHE A CE2 1 
ATOM   11605 C CZ  . PHE B 2 273  ? 190.211 187.957 176.317 1.00 78.83  ? 273  PHE A CZ  1 
ATOM   11606 N N   . HIS B 2 274  ? 193.543 182.436 175.618 1.00 76.16  ? 274  HIS A N   1 
ATOM   11607 C CA  . HIS B 2 274  ? 194.662 182.648 174.712 1.00 76.16  ? 274  HIS A CA  1 
ATOM   11608 C C   . HIS B 2 274  ? 194.278 182.452 173.249 1.00 76.16  ? 274  HIS A C   1 
ATOM   11609 O O   . HIS B 2 274  ? 195.133 182.089 172.431 1.00 76.16  ? 274  HIS A O   1 
ATOM   11610 C CB  . HIS B 2 274  ? 195.812 181.711 175.087 1.00 76.16  ? 274  HIS A CB  1 
ATOM   11611 C CG  . HIS B 2 274  ? 195.428 180.263 175.088 1.00 76.16  ? 274  HIS A CG  1 
ATOM   11612 N ND1 . HIS B 2 274  ? 195.248 179.538 176.246 1.00 76.16  ? 274  HIS A ND1 1 
ATOM   11613 C CD2 . HIS B 2 274  ? 195.184 179.408 174.067 1.00 76.16  ? 274  HIS A CD2 1 
ATOM   11614 C CE1 . HIS B 2 274  ? 194.913 178.299 175.939 1.00 76.16  ? 274  HIS A CE1 1 
ATOM   11615 N NE2 . HIS B 2 274  ? 194.867 178.193 174.622 1.00 76.16  ? 274  HIS A NE2 1 
ATOM   11616 N N   . SER B 2 275  ? 193.007 182.666 172.903 1.00 66.53  ? 275  SER A N   1 
ATOM   11617 C CA  . SER B 2 275  ? 192.603 182.595 171.504 1.00 66.53  ? 275  SER A CA  1 
ATOM   11618 C C   . SER B 2 275  ? 193.369 183.599 170.658 1.00 66.53  ? 275  SER A C   1 
ATOM   11619 O O   . SER B 2 275  ? 193.671 183.329 169.490 1.00 66.53  ? 275  SER A O   1 
ATOM   11620 C CB  . SER B 2 275  ? 191.098 182.832 171.380 1.00 66.53  ? 275  SER A CB  1 
ATOM   11621 O OG  . SER B 2 275  ? 190.380 181.986 172.260 1.00 66.53  ? 275  SER A OG  1 
ATOM   11622 N N   . TRP B 2 276  ? 193.706 184.756 171.229 1.00 64.00  ? 276  TRP A N   1 
ATOM   11623 C CA  . TRP B 2 276  ? 194.547 185.704 170.511 1.00 64.00  ? 276  TRP A CA  1 
ATOM   11624 C C   . TRP B 2 276  ? 195.948 185.150 170.298 1.00 64.00  ? 276  TRP A C   1 
ATOM   11625 O O   . TRP B 2 276  ? 196.572 185.429 169.270 1.00 64.00  ? 276  TRP A O   1 
ATOM   11626 C CB  . TRP B 2 276  ? 194.600 187.032 171.261 1.00 64.00  ? 276  TRP A CB  1 
ATOM   11627 C CG  . TRP B 2 276  ? 195.391 186.985 172.525 1.00 64.00  ? 276  TRP A CG  1 
ATOM   11628 C CD1 . TRP B 2 276  ? 194.955 186.564 173.746 1.00 64.00  ? 276  TRP A CD1 1 
ATOM   11629 C CD2 . TRP B 2 276  ? 196.757 187.377 172.701 1.00 64.00  ? 276  TRP A CD2 1 
ATOM   11630 N NE1 . TRP B 2 276  ? 195.966 186.666 174.671 1.00 64.00  ? 276  TRP A NE1 1 
ATOM   11631 C CE2 . TRP B 2 276  ? 197.082 187.163 174.054 1.00 64.00  ? 276  TRP A CE2 1 
ATOM   11632 C CE3 . TRP B 2 276  ? 197.739 187.885 171.846 1.00 64.00  ? 276  TRP A CE3 1 
ATOM   11633 C CZ2 . TRP B 2 276  ? 198.343 187.440 174.572 1.00 64.00  ? 276  TRP A CZ2 1 
ATOM   11634 C CZ3 . TRP B 2 276  ? 198.992 188.161 172.362 1.00 64.00  ? 276  TRP A CZ3 1 
ATOM   11635 C CH2 . TRP B 2 276  ? 199.283 187.937 173.712 1.00 64.00  ? 276  TRP A CH2 1 
ATOM   11636 N N   . ARG B 2 277  ? 196.450 184.351 171.242 1.00 64.20  ? 277  ARG A N   1 
ATOM   11637 C CA  . ARG B 2 277  ? 197.776 183.763 171.085 1.00 64.20  ? 277  ARG A CA  1 
ATOM   11638 C C   . ARG B 2 277  ? 197.816 182.806 169.899 1.00 64.20  ? 277  ARG A C   1 
ATOM   11639 O O   . ARG B 2 277  ? 198.708 182.892 169.046 1.00 64.20  ? 277  ARG A O   1 
ATOM   11640 C CB  . ARG B 2 277  ? 198.185 183.050 172.372 1.00 64.20  ? 277  ARG A CB  1 
ATOM   11641 C CG  . ARG B 2 277  ? 199.193 183.820 173.201 1.00 64.20  ? 277  ARG A CG  1 
ATOM   11642 C CD  . ARG B 2 277  ? 199.502 183.123 174.515 1.00 64.20  ? 277  ARG A CD  1 
ATOM   11643 N NE  . ARG B 2 277  ? 198.627 183.578 175.587 1.00 64.20  ? 277  ARG A NE  1 
ATOM   11644 C CZ  . ARG B 2 277  ? 198.977 184.457 176.516 1.00 64.20  ? 277  ARG A CZ  1 
ATOM   11645 N NH1 . ARG B 2 277  ? 200.184 184.999 176.534 1.00 64.20  ? 277  ARG A NH1 1 
ATOM   11646 N NH2 . ARG B 2 277  ? 198.097 184.799 177.450 1.00 64.20  ? 277  ARG A NH2 1 
ATOM   11647 N N   . VAL B 2 278  ? 196.848 181.892 169.823 1.00 59.44  ? 278  VAL A N   1 
ATOM   11648 C CA  . VAL B 2 278  ? 196.819 180.962 168.701 1.00 59.44  ? 278  VAL A CA  1 
ATOM   11649 C C   . VAL B 2 278  ? 196.519 181.700 167.402 1.00 59.44  ? 278  VAL A C   1 
ATOM   11650 O O   . VAL B 2 278  ? 197.035 181.331 166.341 1.00 59.44  ? 278  VAL A O   1 
ATOM   11651 C CB  . VAL B 2 278  ? 195.820 179.817 168.961 1.00 59.44  ? 278  VAL A CB  1 
ATOM   11652 C CG1 . VAL B 2 278  ? 194.469 180.356 169.370 1.00 59.44  ? 278  VAL A CG1 1 
ATOM   11653 C CG2 . VAL B 2 278  ? 195.693 178.918 167.740 1.00 59.44  ? 278  VAL A CG2 1 
ATOM   11654 N N   . PHE B 2 279  ? 195.694 182.752 167.452 1.00 55.54  ? 279  PHE A N   1 
ATOM   11655 C CA  . PHE B 2 279  ? 195.439 183.540 166.249 1.00 55.54  ? 279  PHE A CA  1 
ATOM   11656 C C   . PHE B 2 279  ? 196.717 184.190 165.731 1.00 55.54  ? 279  PHE A C   1 
ATOM   11657 O O   . PHE B 2 279  ? 196.981 184.184 164.523 1.00 55.54  ? 279  PHE A O   1 
ATOM   11658 C CB  . PHE B 2 279  ? 194.378 184.600 166.528 1.00 55.54  ? 279  PHE A CB  1 
ATOM   11659 C CG  . PHE B 2 279  ? 194.124 185.522 165.372 1.00 55.54  ? 279  PHE A CG  1 
ATOM   11660 C CD1 . PHE B 2 279  ? 193.361 185.110 164.296 1.00 55.54  ? 279  PHE A CD1 1 
ATOM   11661 C CD2 . PHE B 2 279  ? 194.648 186.804 165.362 1.00 55.54  ? 279  PHE A CD2 1 
ATOM   11662 C CE1 . PHE B 2 279  ? 193.123 185.958 163.233 1.00 55.54  ? 279  PHE A CE1 1 
ATOM   11663 C CE2 . PHE B 2 279  ? 194.413 187.655 164.302 1.00 55.54  ? 279  PHE A CE2 1 
ATOM   11664 C CZ  . PHE B 2 279  ? 193.649 187.230 163.238 1.00 55.54  ? 279  PHE A CZ  1 
ATOM   11665 N N   . VAL B 2 280  ? 197.518 184.759 166.629 1.00 56.74  ? 280  VAL A N   1 
ATOM   11666 C CA  . VAL B 2 280  ? 198.783 185.360 166.219 1.00 56.74  ? 280  VAL A CA  1 
ATOM   11667 C C   . VAL B 2 280  ? 199.727 184.289 165.688 1.00 56.74  ? 280  VAL A C   1 
ATOM   11668 O O   . VAL B 2 280  ? 200.469 184.521 164.724 1.00 56.74  ? 280  VAL A O   1 
ATOM   11669 C CB  . VAL B 2 280  ? 199.398 186.146 167.393 1.00 56.74  ? 280  VAL A CB  1 
ATOM   11670 C CG1 . VAL B 2 280  ? 200.887 186.368 167.180 1.00 56.74  ? 280  VAL A CG1 1 
ATOM   11671 C CG2 . VAL B 2 280  ? 198.680 187.472 167.568 1.00 56.74  ? 280  VAL A CG2 1 
ATOM   11672 N N   . ILE B 2 281  ? 199.710 183.100 166.297 1.00 56.25  ? 281  ILE A N   1 
ATOM   11673 C CA  . ILE B 2 281  ? 200.552 182.008 165.814 1.00 56.25  ? 281  ILE A CA  1 
ATOM   11674 C C   . ILE B 2 281  ? 200.170 181.630 164.389 1.00 56.25  ? 281  ILE A C   1 
ATOM   11675 O O   . ILE B 2 281  ? 201.030 181.470 163.516 1.00 56.25  ? 281  ILE A O   1 
ATOM   11676 C CB  . ILE B 2 281  ? 200.454 180.795 166.759 1.00 56.25  ? 281  ILE A CB  1 
ATOM   11677 C CG1 . ILE B 2 281  ? 201.438 180.933 167.921 1.00 56.25  ? 281  ILE A CG1 1 
ATOM   11678 C CG2 . ILE B 2 281  ? 200.705 179.498 166.001 1.00 56.25  ? 281  ILE A CG2 1 
ATOM   11679 C CD1 . ILE B 2 281  ? 202.846 180.497 167.585 1.00 56.25  ? 281  ILE A CD1 1 
ATOM   11680 N N   . VAL B 2 282  ? 198.869 181.499 164.128 1.00 51.50  ? 282  VAL A N   1 
ATOM   11681 C CA  . VAL B 2 282  ? 198.421 180.985 162.838 1.00 51.50  ? 282  VAL A CA  1 
ATOM   11682 C C   . VAL B 2 282  ? 198.452 182.053 161.750 1.00 51.50  ? 282  VAL A C   1 
ATOM   11683 O O   . VAL B 2 282  ? 198.567 181.714 160.566 1.00 51.50  ? 282  VAL A O   1 
ATOM   11684 C CB  . VAL B 2 282  ? 197.018 180.369 162.973 1.00 51.50  ? 282  VAL A CB  1 
ATOM   11685 C CG1 . VAL B 2 282  ? 196.012 181.417 163.374 1.00 51.50  ? 282  VAL A CG1 1 
ATOM   11686 C CG2 . VAL B 2 282  ? 196.601 179.668 161.688 1.00 51.50  ? 282  VAL A CG2 1 
ATOM   11687 N N   . CYS B 2 283  ? 198.380 183.338 162.108 1.00 48.07  ? 283  CYS A N   1 
ATOM   11688 C CA  . CYS B 2 283  ? 198.505 184.381 161.096 1.00 48.07  ? 283  CYS A CA  1 
ATOM   11689 C C   . CYS B 2 283  ? 199.902 184.454 160.495 1.00 48.07  ? 283  CYS A C   1 
ATOM   11690 O O   . CYS B 2 283  ? 200.086 185.139 159.484 1.00 48.07  ? 283  CYS A O   1 
ATOM   11691 C CB  . CYS B 2 283  ? 198.124 185.738 161.684 1.00 48.07  ? 283  CYS A CB  1 
ATOM   11692 S SG  . CYS B 2 283  ? 196.395 186.191 161.433 1.00 48.07  ? 283  CYS A SG  1 
ATOM   11693 N N   . ALA B 2 284  ? 200.879 183.772 161.088 1.00 45.86  ? 284  ALA A N   1 
ATOM   11694 C CA  . ALA B 2 284  ? 202.227 183.694 160.544 1.00 45.86  ? 284  ALA A CA  1 
ATOM   11695 C C   . ALA B 2 284  ? 202.446 182.424 159.731 1.00 45.86  ? 284  ALA A C   1 
ATOM   11696 O O   . ALA B 2 284  ? 203.591 181.995 159.555 1.00 45.86  ? 284  ALA A O   1 
ATOM   11697 C CB  . ALA B 2 284  ? 203.258 183.784 161.670 1.00 45.86  ? 284  ALA A CB  1 
ATOM   11698 N N   . LEU B 2 285  ? 201.373 181.807 159.248 1.00 45.36  ? 285  LEU A N   1 
ATOM   11699 C CA  . LEU B 2 285  ? 201.476 180.589 158.454 1.00 45.36  ? 285  LEU A CA  1 
ATOM   11700 C C   . LEU B 2 285  ? 201.911 180.872 157.016 1.00 45.36  ? 285  LEU A C   1 
ATOM   11701 O O   . LEU B 2 285  ? 202.842 180.217 156.531 1.00 45.36  ? 285  LEU A O   1 
ATOM   11702 C CB  . LEU B 2 285  ? 200.152 179.820 158.474 1.00 45.36  ? 285  LEU A CB  1 
ATOM   11703 C CG  . LEU B 2 285  ? 200.089 178.580 159.365 1.00 45.36  ? 285  LEU A CG  1 
ATOM   11704 C CD1 . LEU B 2 285  ? 198.991 177.639 158.893 1.00 45.36  ? 285  LEU A CD1 1 
ATOM   11705 C CD2 . LEU B 2 285  ? 201.432 177.866 159.394 1.00 45.36  ? 285  LEU A CD2 1 
ATOM   11706 N N   . PRO B 2 286  ? 201.266 181.797 156.288 1.00 44.92  ? 286  PRO A N   1 
ATOM   11707 C CA  . PRO B 2 286  ? 201.705 182.038 154.903 1.00 44.92  ? 286  PRO A CA  1 
ATOM   11708 C C   . PRO B 2 286  ? 203.159 182.462 154.795 1.00 44.92  ? 286  PRO A C   1 
ATOM   11709 O O   . PRO B 2 286  ? 203.870 181.996 153.895 1.00 44.92  ? 286  PRO A O   1 
ATOM   11710 C CB  . PRO B 2 286  ? 200.753 183.140 154.417 1.00 44.92  ? 286  PRO A CB  1 
ATOM   11711 C CG  . PRO B 2 286  ? 200.227 183.763 155.652 1.00 44.92  ? 286  PRO A CG  1 
ATOM   11712 C CD  . PRO B 2 286  ? 200.106 182.643 156.622 1.00 44.92  ? 286  PRO A CD  1 
ATOM   11713 N N   . CYS B 2 287  ? 203.633 183.314 155.704 1.00 46.64  ? 287  CYS A N   1 
ATOM   11714 C CA  . CYS B 2 287  ? 205.036 183.714 155.660 1.00 46.64  ? 287  CYS A CA  1 
ATOM   11715 C C   . CYS B 2 287  ? 205.953 182.541 155.988 1.00 46.64  ? 287  CYS A C   1 
ATOM   11716 O O   . CYS B 2 287  ? 207.040 182.418 155.411 1.00 46.64  ? 287  CYS A O   1 
ATOM   11717 C CB  . CYS B 2 287  ? 205.280 184.882 156.615 1.00 46.64  ? 287  CYS A CB  1 
ATOM   11718 S SG  . CYS B 2 287  ? 205.085 184.485 158.361 1.00 46.64  ? 287  CYS A SG  1 
ATOM   11719 N N   . THR B 2 288  ? 205.533 181.665 156.903 1.00 45.59  ? 288  THR A N   1 
ATOM   11720 C CA  . THR B 2 288  ? 206.336 180.486 157.217 1.00 45.59  ? 288  THR A CA  1 
ATOM   11721 C C   . THR B 2 288  ? 206.455 179.560 156.012 1.00 45.59  ? 288  THR A C   1 
ATOM   11722 O O   . THR B 2 288  ? 207.547 179.066 155.700 1.00 45.59  ? 288  THR A O   1 
ATOM   11723 C CB  . THR B 2 288  ? 205.733 179.742 158.407 1.00 45.59  ? 288  THR A CB  1 
ATOM   11724 O OG1 . THR B 2 288  ? 205.565 180.645 159.506 1.00 45.59  ? 288  THR A OG1 1 
ATOM   11725 C CG2 . THR B 2 288  ? 206.638 178.596 158.833 1.00 45.59  ? 288  THR A CG2 1 
ATOM   11726 N N   . VAL B 2 289  ? 205.341 179.310 155.326 1.00 44.00  ? 289  VAL A N   1 
ATOM   11727 C CA  . VAL B 2 289  ? 205.389 178.454 154.145 1.00 44.00  ? 289  VAL A CA  1 
ATOM   11728 C C   . VAL B 2 289  ? 206.210 179.110 153.043 1.00 44.00  ? 289  VAL A C   1 
ATOM   11729 O O   . VAL B 2 289  ? 206.922 178.433 152.295 1.00 44.00  ? 289  VAL A O   1 
ATOM   11730 C CB  . VAL B 2 289  ? 203.967 178.104 153.671 1.00 44.00  ? 289  VAL A CB  1 
ATOM   11731 C CG1 . VAL B 2 289  ? 204.025 177.058 152.572 1.00 44.00  ? 289  VAL A CG1 1 
ATOM   11732 C CG2 . VAL B 2 289  ? 203.138 177.591 154.829 1.00 44.00  ? 289  VAL A CG2 1 
ATOM   11733 N N   . SER B 2 290  ? 206.137 180.440 152.930 1.00 43.98  ? 290  SER A N   1 
ATOM   11734 C CA  . SER B 2 290  ? 206.961 181.138 151.948 1.00 43.98  ? 290  SER A CA  1 
ATOM   11735 C C   . SER B 2 290  ? 208.442 181.014 152.280 1.00 43.98  ? 290  SER A C   1 
ATOM   11736 O O   . SER B 2 290  ? 209.280 180.882 151.380 1.00 43.98  ? 290  SER A O   1 
ATOM   11737 C CB  . SER B 2 290  ? 206.551 182.606 151.865 1.00 43.98  ? 290  SER A CB  1 
ATOM   11738 O OG  . SER B 2 290  ? 207.434 183.332 151.030 1.00 43.98  ? 290  SER A OG  1 
ATOM   11739 N N   . MET B 2 291  ? 208.788 181.076 153.567 1.00 47.32  ? 291  MET A N   1 
ATOM   11740 C CA  . MET B 2 291  ? 210.177 180.886 153.970 1.00 47.32  ? 291  MET A CA  1 
ATOM   11741 C C   . MET B 2 291  ? 210.655 179.471 153.675 1.00 47.32  ? 291  MET A C   1 
ATOM   11742 O O   . MET B 2 291  ? 211.806 179.271 153.272 1.00 47.32  ? 291  MET A O   1 
ATOM   11743 C CB  . MET B 2 291  ? 210.345 181.220 155.450 1.00 47.32  ? 291  MET A CB  1 
ATOM   11744 C CG  . MET B 2 291  ? 210.894 182.605 155.632 1.00 47.32  ? 291  MET A CG  1 
ATOM   11745 S SD  . MET B 2 291  ? 212.243 182.785 154.455 1.00 47.32  ? 291  MET A SD  1 
ATOM   11746 C CE  . MET B 2 291  ? 211.760 184.286 153.629 1.00 47.32  ? 291  MET A CE  1 
ATOM   11747 N N   . VAL B 2 292  ? 209.789 178.481 153.882 1.00 46.28  ? 292  VAL A N   1 
ATOM   11748 C CA  . VAL B 2 292  ? 210.132 177.116 153.494 1.00 46.28  ? 292  VAL A CA  1 
ATOM   11749 C C   . VAL B 2 292  ? 210.359 177.036 151.988 1.00 46.28  ? 292  VAL A C   1 
ATOM   11750 O O   . VAL B 2 292  ? 211.319 176.415 151.519 1.00 46.28  ? 292  VAL A O   1 
ATOM   11751 C CB  . VAL B 2 292  ? 209.042 176.134 153.960 1.00 46.28  ? 292  VAL A CB  1 
ATOM   11752 C CG1 . VAL B 2 292  ? 209.041 174.879 153.094 1.00 46.28  ? 292  VAL A CG1 1 
ATOM   11753 C CG2 . VAL B 2 292  ? 209.241 175.778 155.424 1.00 46.28  ? 292  VAL A CG2 1 
ATOM   11754 N N   . ALA B 2 293  ? 209.488 177.681 151.209 1.00 42.26  ? 293  ALA A N   1 
ATOM   11755 C CA  . ALA B 2 293  ? 209.529 177.558 149.757 1.00 42.26  ? 293  ALA A CA  1 
ATOM   11756 C C   . ALA B 2 293  ? 210.707 178.290 149.127 1.00 42.26  ? 293  ALA A C   1 
ATOM   11757 O O   . ALA B 2 293  ? 211.247 177.820 148.122 1.00 42.26  ? 293  ALA A O   1 
ATOM   11758 C CB  . ALA B 2 293  ? 208.224 178.074 149.153 1.00 42.26  ? 293  ALA A CB  1 
ATOM   11759 N N   . LEU B 2 294  ? 211.116 179.430 149.683 1.00 43.17  ? 294  LEU A N   1 
ATOM   11760 C CA  . LEU B 2 294  ? 212.087 180.277 148.995 1.00 43.17  ? 294  LEU A CA  1 
ATOM   11761 C C   . LEU B 2 294  ? 213.487 179.674 148.936 1.00 43.17  ? 294  LEU A C   1 
ATOM   11762 O O   . LEU B 2 294  ? 214.338 180.215 148.222 1.00 43.17  ? 294  LEU A O   1 
ATOM   11763 C CB  . LEU B 2 294  ? 212.152 181.655 149.655 1.00 43.17  ? 294  LEU A CB  1 
ATOM   11764 C CG  . LEU B 2 294  ? 212.411 182.813 148.691 1.00 43.17  ? 294  LEU A CG  1 
ATOM   11765 C CD1 . LEU B 2 294  ? 211.392 182.808 147.565 1.00 43.17  ? 294  LEU A CD1 1 
ATOM   11766 C CD2 . LEU B 2 294  ? 212.389 184.137 149.423 1.00 43.17  ? 294  LEU A CD2 1 
ATOM   11767 N N   . LYS B 2 295  ? 213.751 178.585 149.658 1.00 43.33  ? 295  LYS A N   1 
ATOM   11768 C CA  . LYS B 2 295  ? 215.057 177.946 149.556 1.00 43.33  ? 295  LYS A CA  1 
ATOM   11769 C C   . LYS B 2 295  ? 215.298 177.383 148.162 1.00 43.33  ? 295  LYS A C   1 
ATOM   11770 O O   . LYS B 2 295  ? 216.446 177.339 147.701 1.00 43.33  ? 295  LYS A O   1 
ATOM   11771 C CB  . LYS B 2 295  ? 215.189 176.846 150.609 1.00 43.33  ? 295  LYS A CB  1 
ATOM   11772 C CG  . LYS B 2 295  ? 216.493 176.064 150.541 1.00 43.33  ? 295  LYS A CG  1 
ATOM   11773 C CD  . LYS B 2 295  ? 216.280 174.670 149.973 1.00 43.33  ? 295  LYS A CD  1 
ATOM   11774 C CE  . LYS B 2 295  ? 217.595 174.011 149.596 1.00 43.33  ? 295  LYS A CE  1 
ATOM   11775 N NZ  . LYS B 2 295  ? 217.384 172.678 148.965 1.00 43.33  ? 295  LYS A NZ  1 
ATOM   11776 N N   . PHE B 2 296  ? 214.237 176.965 147.466 1.00 44.41  ? 296  PHE A N   1 
ATOM   11777 C CA  . PHE B 2 296  ? 214.399 176.342 146.156 1.00 44.41  ? 296  PHE A CA  1 
ATOM   11778 C C   . PHE B 2 296  ? 214.449 177.365 145.027 1.00 44.41  ? 296  PHE A C   1 
ATOM   11779 O O   . PHE B 2 296  ? 215.118 177.127 144.015 1.00 44.41  ? 296  PHE A O   1 
ATOM   11780 C CB  . PHE B 2 296  ? 213.264 175.349 145.892 1.00 44.41  ? 296  PHE A CB  1 
ATOM   11781 C CG  . PHE B 2 296  ? 212.756 174.660 147.126 1.00 44.41  ? 296  PHE A CG  1 
ATOM   11782 C CD1 . PHE B 2 296  ? 213.602 173.898 147.910 1.00 44.41  ? 296  PHE A CD1 1 
ATOM   11783 C CD2 . PHE B 2 296  ? 211.427 174.767 147.494 1.00 44.41  ? 296  PHE A CD2 1 
ATOM   11784 C CE1 . PHE B 2 296  ? 213.135 173.263 149.042 1.00 44.41  ? 296  PHE A CE1 1 
ATOM   11785 C CE2 . PHE B 2 296  ? 210.953 174.137 148.625 1.00 44.41  ? 296  PHE A CE2 1 
ATOM   11786 C CZ  . PHE B 2 296  ? 211.807 173.382 149.400 1.00 44.41  ? 296  PHE A CZ  1 
ATOM   11787 N N   . MET B 2 297  ? 213.753 178.485 145.167 1.00 40.47  ? 297  MET A N   1 
ATOM   11788 C CA  . MET B 2 297  ? 213.696 179.448 144.077 1.00 40.47  ? 297  MET A CA  1 
ATOM   11789 C C   . MET B 2 297  ? 215.048 180.140 143.902 1.00 40.47  ? 297  MET A C   1 
ATOM   11790 O O   . MET B 2 297  ? 215.760 180.367 144.882 1.00 40.47  ? 297  MET A O   1 
ATOM   11791 C CB  . MET B 2 297  ? 212.608 180.483 144.334 1.00 40.47  ? 297  MET A CB  1 
ATOM   11792 C CG  . MET B 2 297  ? 211.280 179.867 144.713 1.00 40.47  ? 297  MET A CG  1 
ATOM   11793 S SD  . MET B 2 297  ? 211.080 178.228 143.986 1.00 40.47  ? 297  MET A SD  1 
ATOM   11794 C CE  . MET B 2 297  ? 210.126 178.614 142.521 1.00 40.47  ? 297  MET A CE  1 
ATOM   11795 N N   . PRO B 2 298  ? 215.420 180.481 142.670 1.00 41.56  ? 298  PRO A N   1 
ATOM   11796 C CA  . PRO B 2 298  ? 216.724 181.103 142.432 1.00 41.56  ? 298  PRO A CA  1 
ATOM   11797 C C   . PRO B 2 298  ? 216.660 182.620 142.450 1.00 41.56  ? 298  PRO A C   1 
ATOM   11798 O O   . PRO B 2 298  ? 215.574 183.195 142.537 1.00 41.56  ? 298  PRO A O   1 
ATOM   11799 C CB  . PRO B 2 298  ? 217.094 180.577 141.046 1.00 41.56  ? 298  PRO A CB  1 
ATOM   11800 C CG  . PRO B 2 298  ? 215.773 180.517 140.350 1.00 41.56  ? 298  PRO A CG  1 
ATOM   11801 C CD  . PRO B 2 298  ? 214.733 180.178 141.404 1.00 41.56  ? 298  PRO A CD  1 
ATOM   11802 N N   . GLU B 2 299  ? 217.815 183.275 142.351 1.00 45.33  ? 299  GLU A N   1 
ATOM   11803 C CA  . GLU B 2 299  ? 217.874 184.726 142.412 1.00 45.33  ? 299  GLU A CA  1 
ATOM   11804 C C   . GLU B 2 299  ? 217.305 185.330 141.126 1.00 45.33  ? 299  GLU A C   1 
ATOM   11805 O O   . GLU B 2 299  ? 216.832 184.629 140.228 1.00 45.33  ? 299  GLU A O   1 
ATOM   11806 C CB  . GLU B 2 299  ? 219.310 185.185 142.649 1.00 45.33  ? 299  GLU A CB  1 
ATOM   11807 C CG  . GLU B 2 299  ? 219.486 186.041 143.890 1.00 45.33  ? 299  GLU A CG  1 
ATOM   11808 C CD  . GLU B 2 299  ? 218.788 187.385 143.787 1.00 45.33  ? 299  GLU A CD  1 
ATOM   11809 O OE1 . GLU B 2 299  ? 218.491 187.821 142.655 1.00 45.33  ? 299  GLU A OE1 1 
ATOM   11810 O OE2 . GLU B 2 299  ? 218.535 188.003 144.839 1.00 45.33  ? 299  GLU A OE2 1 
ATOM   11811 N N   . SER B 2 300  ? 217.332 186.654 141.043 1.00 45.14  ? 300  SER A N   1 
ATOM   11812 C CA  . SER B 2 300  ? 216.821 187.344 139.865 1.00 45.14  ? 300  SER A CA  1 
ATOM   11813 C C   . SER B 2 300  ? 217.867 187.324 138.758 1.00 45.14  ? 300  SER A C   1 
ATOM   11814 O O   . SER B 2 300  ? 218.986 187.794 138.974 1.00 45.14  ? 300  SER A O   1 
ATOM   11815 C CB  . SER B 2 300  ? 216.445 188.776 140.204 1.00 45.14  ? 300  SER A CB  1 
ATOM   11816 O OG  . SER B 2 300  ? 215.754 189.383 139.127 1.00 45.14  ? 300  SER A OG  1 
ATOM   11817 N N   . PRO B 2 301  ? 217.551 186.795 137.573 1.00 46.68  ? 301  PRO A N   1 
ATOM   11818 C CA  . PRO B 2 301  ? 218.572 186.742 136.514 1.00 46.68  ? 301  PRO A CA  1 
ATOM   11819 C C   . PRO B 2 301  ? 218.987 188.110 136.005 1.00 46.68  ? 301  PRO A C   1 
ATOM   11820 O O   . PRO B 2 301  ? 220.183 188.344 135.789 1.00 46.68  ? 301  PRO A O   1 
ATOM   11821 C CB  . PRO B 2 301  ? 217.899 185.911 135.412 1.00 46.68  ? 301  PRO A CB  1 
ATOM   11822 C CG  . PRO B 2 301  ? 216.722 185.255 136.058 1.00 46.68  ? 301  PRO A CG  1 
ATOM   11823 C CD  . PRO B 2 301  ? 216.296 186.143 137.176 1.00 46.68  ? 301  PRO A CD  1 
ATOM   11824 N N   . ARG B 2 302  ? 218.035 189.022 135.794 1.00 48.90  ? 302  ARG A N   1 
ATOM   11825 C CA  . ARG B 2 302  ? 218.380 190.340 135.266 1.00 48.90  ? 302  ARG A CA  1 
ATOM   11826 C C   . ARG B 2 302  ? 219.251 191.116 136.243 1.00 48.90  ? 302  ARG A C   1 
ATOM   11827 O O   . ARG B 2 302  ? 220.253 191.722 135.847 1.00 48.90  ? 302  ARG A O   1 
ATOM   11828 C CB  . ARG B 2 302  ? 217.109 191.124 134.940 1.00 48.90  ? 302  ARG A CB  1 
ATOM   11829 C CG  . ARG B 2 302  ? 217.362 192.461 134.265 1.00 48.90  ? 302  ARG A CG  1 
ATOM   11830 C CD  . ARG B 2 302  ? 216.095 192.995 133.612 1.00 48.90  ? 302  ARG A CD  1 
ATOM   11831 N NE  . ARG B 2 302  ? 216.256 194.364 133.136 1.00 48.90  ? 302  ARG A NE  1 
ATOM   11832 C CZ  . ARG B 2 302  ? 216.300 194.712 131.858 1.00 48.90  ? 302  ARG A CZ  1 
ATOM   11833 N NH1 . ARG B 2 302  ? 216.198 193.814 130.892 1.00 48.90  ? 302  ARG A NH1 1 
ATOM   11834 N NH2 . ARG B 2 302  ? 216.453 195.994 131.541 1.00 48.90  ? 302  ARG A NH2 1 
ATOM   11835 N N   . PHE B 2 303  ? 218.894 191.101 137.529 1.00 50.27  ? 303  PHE A N   1 
ATOM   11836 C CA  . PHE B 2 303  ? 219.711 191.772 138.536 1.00 50.27  ? 303  PHE A CA  1 
ATOM   11837 C C   . PHE B 2 303  ? 221.094 191.141 138.635 1.00 50.27  ? 303  PHE A C   1 
ATOM   11838 O O   . PHE B 2 303  ? 222.103 191.849 138.746 1.00 50.27  ? 303  PHE A O   1 
ATOM   11839 C CB  . PHE B 2 303  ? 219.014 191.732 139.894 1.00 50.27  ? 303  PHE A CB  1 
ATOM   11840 C CG  . PHE B 2 303  ? 219.962 191.759 141.058 1.00 50.27  ? 303  PHE A CG  1 
ATOM   11841 C CD1 . PHE B 2 303  ? 220.544 192.946 141.465 1.00 50.27  ? 303  PHE A CD1 1 
ATOM   11842 C CD2 . PHE B 2 303  ? 220.274 190.595 141.740 1.00 50.27  ? 303  PHE A CD2 1 
ATOM   11843 C CE1 . PHE B 2 303  ? 221.419 192.970 142.532 1.00 50.27  ? 303  PHE A CE1 1 
ATOM   11844 C CE2 . PHE B 2 303  ? 221.148 190.616 142.805 1.00 50.27  ? 303  PHE A CE2 1 
ATOM   11845 C CZ  . PHE B 2 303  ? 221.724 191.805 143.201 1.00 50.27  ? 303  PHE A CZ  1 
ATOM   11846 N N   . LEU B 2 304  ? 221.156 189.807 138.618 1.00 50.05  ? 304  LEU A N   1 
ATOM   11847 C CA  . LEU B 2 304  ? 222.445 189.133 138.695 1.00 50.05  ? 304  LEU A CA  1 
ATOM   11848 C C   . LEU B 2 304  ? 223.330 189.515 137.520 1.00 50.05  ? 304  LEU A C   1 
ATOM   11849 O O   . LEU B 2 304  ? 224.518 189.802 137.699 1.00 50.05  ? 304  LEU A O   1 
ATOM   11850 C CB  . LEU B 2 304  ? 222.245 187.620 138.754 1.00 50.05  ? 304  LEU A CB  1 
ATOM   11851 C CG  . LEU B 2 304  ? 222.469 187.000 140.133 1.00 50.05  ? 304  LEU A CG  1 
ATOM   11852 C CD1 . LEU B 2 304  ? 222.375 185.487 140.072 1.00 50.05  ? 304  LEU A CD1 1 
ATOM   11853 C CD2 . LEU B 2 304  ? 223.811 187.430 140.690 1.00 50.05  ? 304  LEU A CD2 1 
ATOM   11854 N N   . LEU B 2 305  ? 222.760 189.554 136.313 1.00 52.29  ? 305  LEU A N   1 
ATOM   11855 C CA  . LEU B 2 305  ? 223.511 190.024 135.152 1.00 52.29  ? 305  LEU A CA  1 
ATOM   11856 C C   . LEU B 2 305  ? 223.966 191.464 135.346 1.00 52.29  ? 305  LEU A C   1 
ATOM   11857 O O   . LEU B 2 305  ? 225.092 191.823 134.983 1.00 52.29  ? 305  LEU A O   1 
ATOM   11858 C CB  . LEU B 2 305  ? 222.655 189.894 133.891 1.00 52.29  ? 305  LEU A CB  1 
ATOM   11859 C CG  . LEU B 2 305  ? 222.927 190.871 132.744 1.00 52.29  ? 305  LEU A CG  1 
ATOM   11860 C CD1 . LEU B 2 305  ? 224.272 190.597 132.087 1.00 52.29  ? 305  LEU A CD1 1 
ATOM   11861 C CD2 . LEU B 2 305  ? 221.805 190.835 131.716 1.00 52.29  ? 305  LEU A CD2 1 
ATOM   11862 N N   . GLU B 2 306  ? 223.099 192.304 135.918 1.00 52.10  ? 306  GLU A N   1 
ATOM   11863 C CA  . GLU B 2 306  ? 223.456 193.699 136.151 1.00 52.10  ? 306  GLU A CA  1 
ATOM   11864 C C   . GLU B 2 306  ? 224.678 193.813 137.051 1.00 52.10  ? 306  GLU A C   1 
ATOM   11865 O O   . GLU B 2 306  ? 225.585 194.612 136.781 1.00 52.10  ? 306  GLU A O   1 
ATOM   11866 C CB  . GLU B 2 306  ? 222.279 194.445 136.770 1.00 52.10  ? 306  GLU A CB  1 
ATOM   11867 C CG  . GLU B 2 306  ? 221.253 194.923 135.766 1.00 52.10  ? 306  GLU A CG  1 
ATOM   11868 C CD  . GLU B 2 306  ? 221.870 195.659 134.598 1.00 52.10  ? 306  GLU A CD  1 
ATOM   11869 O OE1 . GLU B 2 306  ? 222.704 196.558 134.832 1.00 52.10  ? 306  GLU A OE1 1 
ATOM   11870 O OE2 . GLU B 2 306  ? 221.521 195.341 133.443 1.00 52.10  ? 306  GLU A OE2 1 
ATOM   11871 N N   . MET B 2 307  ? 224.724 193.026 138.127 1.00 53.28  ? 307  MET A N   1 
ATOM   11872 C CA  . MET B 2 307  ? 225.869 193.100 139.029 1.00 53.28  ? 307  MET A CA  1 
ATOM   11873 C C   . MET B 2 307  ? 227.125 192.520 138.388 1.00 53.28  ? 307  MET A C   1 
ATOM   11874 O O   . MET B 2 307  ? 228.205 193.115 138.480 1.00 53.28  ? 307  MET A O   1 
ATOM   11875 C CB  . MET B 2 307  ? 225.554 192.389 140.344 1.00 53.28  ? 307  MET A CB  1 
ATOM   11876 C CG  . MET B 2 307  ? 224.745 193.231 141.315 1.00 53.28  ? 307  MET A CG  1 
ATOM   11877 S SD  . MET B 2 307  ? 225.127 192.875 143.039 1.00 53.28  ? 307  MET A SD  1 
ATOM   11878 C CE  . MET B 2 307  ? 226.795 193.512 143.157 1.00 53.28  ? 307  MET A CE  1 
ATOM   11879 N N   . GLY B 2 308  ? 227.010 191.379 137.736 1.00 57.07  ? 308  GLY A N   1 
ATOM   11880 C CA  . GLY B 2 308  ? 228.155 190.725 137.132 1.00 57.07  ? 308  GLY A CA  1 
ATOM   11881 C C   . GLY B 2 308  ? 227.899 189.232 137.005 1.00 57.07  ? 308  GLY A C   1 
ATOM   11882 O O   . GLY B 2 308  ? 226.760 188.804 136.836 1.00 57.07  ? 308  GLY A O   1 
ATOM   11883 N N   . LYS B 2 309  ? 228.987 188.465 137.076 1.00 56.97  ? 309  LYS A N   1 
ATOM   11884 C CA  . LYS B 2 309  ? 228.970 186.999 137.055 1.00 56.97  ? 309  LYS A CA  1 
ATOM   11885 C C   . LYS B 2 309  ? 227.944 186.467 136.053 1.00 56.97  ? 309  LYS A C   1 
ATOM   11886 O O   . LYS B 2 309  ? 227.006 185.748 136.392 1.00 56.97  ? 309  LYS A O   1 
ATOM   11887 C CB  . LYS B 2 309  ? 228.739 186.420 138.455 1.00 56.97  ? 309  LYS A CB  1 
ATOM   11888 C CG  . LYS B 2 309  ? 227.502 186.914 139.201 1.00 56.97  ? 309  LYS A CG  1 
ATOM   11889 C CD  . LYS B 2 309  ? 227.650 186.734 140.701 1.00 56.97  ? 309  LYS A CD  1 
ATOM   11890 C CE  . LYS B 2 309  ? 228.473 187.858 141.307 1.00 56.97  ? 309  LYS A CE  1 
ATOM   11891 N NZ  . LYS B 2 309  ? 227.934 189.194 140.934 1.00 56.97  ? 309  LYS A NZ  1 
ATOM   11892 N N   . HIS B 2 310  ? 228.147 186.847 134.789 1.00 60.46  ? 310  HIS A N   1 
ATOM   11893 C CA  . HIS B 2 310  ? 227.201 186.483 133.740 1.00 60.46  ? 310  HIS A CA  1 
ATOM   11894 C C   . HIS B 2 310  ? 227.092 184.976 133.546 1.00 60.46  ? 310  HIS A C   1 
ATOM   11895 O O   . HIS B 2 310  ? 226.096 184.506 132.985 1.00 60.46  ? 310  HIS A O   1 
ATOM   11896 C CB  . HIS B 2 310  ? 227.594 187.156 132.425 1.00 60.46  ? 310  HIS A CB  1 
ATOM   11897 C CG  . HIS B 2 310  ? 227.823 188.630 132.548 1.00 60.46  ? 310  HIS A CG  1 
ATOM   11898 N ND1 . HIS B 2 310  ? 227.170 189.410 133.478 1.00 60.46  ? 310  HIS A ND1 1 
ATOM   11899 C CD2 . HIS B 2 310  ? 228.633 189.470 131.859 1.00 60.46  ? 310  HIS A CD2 1 
ATOM   11900 C CE1 . HIS B 2 310  ? 227.567 190.664 133.358 1.00 60.46  ? 310  HIS A CE1 1 
ATOM   11901 N NE2 . HIS B 2 310  ? 228.455 190.728 132.382 1.00 60.46  ? 310  HIS A NE2 1 
ATOM   11902 N N   . ASP B 2 311  ? 228.092 184.210 133.986 1.00 59.19  ? 311  ASP A N   1 
ATOM   11903 C CA  . ASP B 2 311  ? 227.993 182.755 133.913 1.00 59.19  ? 311  ASP A CA  1 
ATOM   11904 C C   . ASP B 2 311  ? 226.884 182.230 134.818 1.00 59.19  ? 311  ASP A C   1 
ATOM   11905 O O   . ASP B 2 311  ? 226.168 181.293 134.452 1.00 59.19  ? 311  ASP A O   1 
ATOM   11906 C CB  . ASP B 2 311  ? 229.334 182.123 134.274 1.00 59.19  ? 311  ASP A CB  1 
ATOM   11907 C CG  . ASP B 2 311  ? 230.508 182.929 133.765 1.00 59.19  ? 311  ASP A CG  1 
ATOM   11908 O OD1 . ASP B 2 311  ? 230.730 182.941 132.537 1.00 59.19  ? 311  ASP A OD1 1 
ATOM   11909 O OD2 . ASP B 2 311  ? 231.203 183.557 134.592 1.00 59.19  ? 311  ASP A OD2 1 
ATOM   11910 N N   . GLU B 2 312  ? 226.729 182.818 136.007 1.00 58.19  ? 312  GLU A N   1 
ATOM   11911 C CA  . GLU B 2 312  ? 225.633 182.425 136.889 1.00 58.19  ? 312  GLU A CA  1 
ATOM   11912 C C   . GLU B 2 312  ? 224.282 182.777 136.275 1.00 58.19  ? 312  GLU A C   1 
ATOM   11913 O O   . GLU B 2 312  ? 223.315 182.011 136.395 1.00 58.19  ? 312  GLU A O   1 
ATOM   11914 C CB  . GLU B 2 312  ? 225.805 183.094 138.251 1.00 58.19  ? 312  GLU A CB  1 
ATOM   11915 C CG  . GLU B 2 312  ? 224.931 182.522 139.345 1.00 58.19  ? 312  GLU A CG  1 
ATOM   11916 C CD  . GLU B 2 312  ? 225.454 182.860 140.726 1.00 58.19  ? 312  GLU A CD  1 
ATOM   11917 O OE1 . GLU B 2 312  ? 226.477 183.569 140.818 1.00 58.19  ? 312  GLU A OE1 1 
ATOM   11918 O OE2 . GLU B 2 312  ? 224.845 182.412 141.719 1.00 58.19  ? 312  GLU A OE2 1 
ATOM   11919 N N   . ALA B 2 313  ? 224.195 183.937 135.619 1.00 55.12  ? 313  ALA A N   1 
ATOM   11920 C CA  . ALA B 2 313  ? 222.974 184.292 134.910 1.00 55.12  ? 313  ALA A CA  1 
ATOM   11921 C C   . ALA B 2 313  ? 222.680 183.295 133.798 1.00 55.12  ? 313  ALA A C   1 
ATOM   11922 O O   . ALA B 2 313  ? 221.530 182.893 133.602 1.00 55.12  ? 313  ALA A O   1 
ATOM   11923 C CB  . ALA B 2 313  ? 223.083 185.710 134.349 1.00 55.12  ? 313  ALA A CB  1 
ATOM   11924 N N   . TRP B 2 314  ? 223.708 182.884 133.056 1.00 56.56  ? 314  TRP A N   1 
ATOM   11925 C CA  . TRP B 2 314  ? 223.500 181.881 132.018 1.00 56.56  ? 314  TRP A CA  1 
ATOM   11926 C C   . TRP B 2 314  ? 223.047 180.557 132.622 1.00 56.56  ? 314  TRP A C   1 
ATOM   11927 O O   . TRP B 2 314  ? 222.201 179.865 132.049 1.00 56.56  ? 314  TRP A O   1 
ATOM   11928 C CB  . TRP B 2 314  ? 224.778 181.700 131.198 1.00 56.56  ? 314  TRP A CB  1 
ATOM   11929 C CG  . TRP B 2 314  ? 224.642 180.737 130.052 1.00 56.56  ? 314  TRP A CG  1 
ATOM   11930 C CD1 . TRP B 2 314  ? 225.458 179.681 129.774 1.00 56.56  ? 314  TRP A CD1 1 
ATOM   11931 C CD2 . TRP B 2 314  ? 223.637 180.749 129.026 1.00 56.56  ? 314  TRP A CD2 1 
ATOM   11932 N NE1 . TRP B 2 314  ? 225.023 179.029 128.644 1.00 56.56  ? 314  TRP A NE1 1 
ATOM   11933 C CE2 . TRP B 2 314  ? 223.909 179.665 128.166 1.00 56.56  ? 314  TRP A CE2 1 
ATOM   11934 C CE3 . TRP B 2 314  ? 222.536 181.566 128.753 1.00 56.56  ? 314  TRP A CE3 1 
ATOM   11935 C CZ2 . TRP B 2 314  ? 223.119 179.379 127.053 1.00 56.56  ? 314  TRP A CZ2 1 
ATOM   11936 C CZ3 . TRP B 2 314  ? 221.754 181.281 127.647 1.00 56.56  ? 314  TRP A CZ3 1 
ATOM   11937 C CH2 . TRP B 2 314  ? 222.049 180.197 126.813 1.00 56.56  ? 314  TRP A CH2 1 
ATOM   11938 N N   . MET B 2 315  ? 223.591 180.198 133.785 1.00 54.06  ? 315  MET A N   1 
ATOM   11939 C CA  . MET B 2 315  ? 223.184 178.959 134.443 1.00 54.06  ? 315  MET A CA  1 
ATOM   11940 C C   . MET B 2 315  ? 221.714 179.000 134.837 1.00 54.06  ? 315  MET A C   1 
ATOM   11941 O O   . MET B 2 315  ? 220.975 178.034 134.606 1.00 54.06  ? 315  MET A O   1 
ATOM   11942 C CB  . MET B 2 315  ? 224.072 178.698 135.662 1.00 54.06  ? 315  MET A CB  1 
ATOM   11943 C CG  . MET B 2 315  ? 223.522 177.688 136.674 1.00 54.06  ? 315  MET A CG  1 
ATOM   11944 S SD  . MET B 2 315  ? 222.353 178.343 137.887 1.00 54.06  ? 315  MET A SD  1 
ATOM   11945 C CE  . MET B 2 315  ? 223.430 178.604 139.295 1.00 54.06  ? 315  MET A CE  1 
ATOM   11946 N N   . ILE B 2 316  ? 221.268 180.104 135.440 1.00 49.33  ? 316  ILE A N   1 
ATOM   11947 C CA  . ILE B 2 316  ? 219.867 180.180 135.850 1.00 49.33  ? 316  ILE A CA  1 
ATOM   11948 C C   . ILE B 2 316  ? 218.950 180.238 134.631 1.00 49.33  ? 316  ILE A C   1 
ATOM   11949 O O   . ILE B 2 316  ? 217.859 179.652 134.632 1.00 49.33  ? 316  ILE A O   1 
ATOM   11950 C CB  . ILE B 2 316  ? 219.631 181.361 136.812 1.00 49.33  ? 316  ILE A CB  1 
ATOM   11951 C CG1 . ILE B 2 316  ? 218.154 181.458 137.183 1.00 49.33  ? 316  ILE A CG1 1 
ATOM   11952 C CG2 . ILE B 2 316  ? 220.097 182.668 136.231 1.00 49.33  ? 316  ILE A CG2 1 
ATOM   11953 C CD1 . ILE B 2 316  ? 217.880 182.501 138.213 1.00 49.33  ? 316  ILE A CD1 1 
ATOM   11954 N N   . LEU B 2 317  ? 219.375 180.924 133.566 1.00 50.21  ? 317  LEU A N   1 
ATOM   11955 C CA  . LEU B 2 317  ? 218.580 180.933 132.343 1.00 50.21  ? 317  LEU A CA  1 
ATOM   11956 C C   . LEU B 2 317  ? 218.455 179.529 131.761 1.00 50.21  ? 317  LEU A C   1 
ATOM   11957 O O   . LEU B 2 317  ? 217.373 179.127 131.318 1.00 50.21  ? 317  LEU A O   1 
ATOM   11958 C CB  . LEU B 2 317  ? 219.195 181.885 131.318 1.00 50.21  ? 317  LEU A CB  1 
ATOM   11959 C CG  . LEU B 2 317  ? 219.161 183.384 131.629 1.00 50.21  ? 317  LEU A CG  1 
ATOM   11960 C CD1 . LEU B 2 317  ? 219.726 184.184 130.469 1.00 50.21  ? 317  LEU A CD1 1 
ATOM   11961 C CD2 . LEU B 2 317  ? 217.756 183.845 131.963 1.00 50.21  ? 317  LEU A CD2 1 
ATOM   11962 N N   . LYS B 2 318  ? 219.550 178.767 131.765 1.00 51.82  ? 318  LYS A N   1 
ATOM   11963 C CA  . LYS B 2 318  ? 219.507 177.397 131.264 1.00 51.82  ? 318  LYS A CA  1 
ATOM   11964 C C   . LYS B 2 318  ? 218.606 176.519 132.125 1.00 51.82  ? 318  LYS A C   1 
ATOM   11965 O O   . LYS B 2 318  ? 217.875 175.674 131.603 1.00 51.82  ? 318  LYS A O   1 
ATOM   11966 C CB  . LYS B 2 318  ? 220.922 176.824 131.195 1.00 51.82  ? 318  LYS A CB  1 
ATOM   11967 C CG  . LYS B 2 318  ? 221.005 175.316 131.367 1.00 51.82  ? 318  LYS A CG  1 
ATOM   11968 C CD  . LYS B 2 318  ? 222.428 174.871 131.671 1.00 51.82  ? 318  LYS A CD  1 
ATOM   11969 C CE  . LYS B 2 318  ? 223.127 175.844 132.609 1.00 51.82  ? 318  LYS A CE  1 
ATOM   11970 N NZ  . LYS B 2 318  ? 224.596 175.622 132.670 1.00 51.82  ? 318  LYS A NZ  1 
ATOM   11971 N N   . GLN B 2 319  ? 218.650 176.703 133.447 1.00 47.23  ? 319  GLN A N   1 
ATOM   11972 C CA  . GLN B 2 319  ? 217.777 175.925 134.323 1.00 47.23  ? 319  GLN A CA  1 
ATOM   11973 C C   . GLN B 2 319  ? 216.309 176.241 134.062 1.00 47.23  ? 319  GLN A C   1 
ATOM   11974 O O   . GLN B 2 319  ? 215.469 175.333 133.998 1.00 47.23  ? 319  GLN A O   1 
ATOM   11975 C CB  . GLN B 2 319  ? 218.142 176.180 135.784 1.00 47.23  ? 319  GLN A CB  1 
ATOM   11976 C CG  . GLN B 2 319  ? 216.984 176.080 136.762 1.00 47.23  ? 319  GLN A CG  1 
ATOM   11977 C CD  . GLN B 2 319  ? 217.336 176.627 138.132 1.00 47.23  ? 319  GLN A CD  1 
ATOM   11978 O OE1 . GLN B 2 319  ? 218.480 176.533 138.575 1.00 47.23  ? 319  GLN A OE1 1 
ATOM   11979 N NE2 . GLN B 2 319  ? 216.353 177.207 138.808 1.00 47.23  ? 319  GLN A NE2 1 
ATOM   11980 N N   . VAL B 2 320  ? 215.978 177.526 133.893 1.00 46.13  ? 320  VAL A N   1 
ATOM   11981 C CA  . VAL B 2 320  ? 214.604 177.910 133.583 1.00 46.13  ? 320  VAL A CA  1 
ATOM   11982 C C   . VAL B 2 320  ? 214.171 177.305 132.254 1.00 46.13  ? 320  VAL A C   1 
ATOM   11983 O O   . VAL B 2 320  ? 213.061 176.770 132.126 1.00 46.13  ? 320  VAL A O   1 
ATOM   11984 C CB  . VAL B 2 320  ? 214.465 179.445 133.571 1.00 46.13  ? 320  VAL A CB  1 
ATOM   11985 C CG1 . VAL B 2 320  ? 213.096 179.854 133.056 1.00 46.13  ? 320  VAL A CG1 1 
ATOM   11986 C CG2 . VAL B 2 320  ? 214.710 180.010 134.948 1.00 46.13  ? 320  VAL A CG2 1 
ATOM   11987 N N   . HIS B 2 321  ? 215.041 177.385 131.244 1.00 48.86  ? 321  HIS A N   1 
ATOM   11988 C CA  . HIS B 2 321  ? 214.708 176.842 129.934 1.00 48.86  ? 321  HIS A CA  1 
ATOM   11989 C C   . HIS B 2 321  ? 214.496 175.336 129.997 1.00 48.86  ? 321  HIS A C   1 
ATOM   11990 O O   . HIS B 2 321  ? 213.574 174.808 129.368 1.00 48.86  ? 321  HIS A O   1 
ATOM   11991 C CB  . HIS B 2 321  ? 215.807 177.187 128.931 1.00 48.86  ? 321  HIS A CB  1 
ATOM   11992 C CG  . HIS B 2 321  ? 215.690 176.455 127.632 1.00 48.86  ? 321  HIS A CG  1 
ATOM   11993 N ND1 . HIS B 2 321  ? 214.511 176.380 126.923 1.00 48.86  ? 321  HIS A ND1 1 
ATOM   11994 C CD2 . HIS B 2 321  ? 216.606 175.759 126.918 1.00 48.86  ? 321  HIS A CD2 1 
ATOM   11995 C CE1 . HIS B 2 321  ? 214.706 175.671 125.824 1.00 48.86  ? 321  HIS A CE1 1 
ATOM   11996 N NE2 . HIS B 2 321  ? 215.969 175.283 125.798 1.00 48.86  ? 321  HIS A NE2 1 
ATOM   11997 N N   . ASP B 2 322  ? 215.343 174.626 130.747 1.00 47.94  ? 322  ASP A N   1 
ATOM   11998 C CA  . ASP B 2 322  ? 215.185 173.182 130.870 1.00 47.94  ? 322  ASP A CA  1 
ATOM   11999 C C   . ASP B 2 322  ? 213.887 172.824 131.577 1.00 47.94  ? 322  ASP A C   1 
ATOM   12000 O O   . ASP B 2 322  ? 213.193 171.885 131.170 1.00 47.94  ? 322  ASP A O   1 
ATOM   12001 C CB  . ASP B 2 322  ? 216.375 172.581 131.615 1.00 47.94  ? 322  ASP A CB  1 
ATOM   12002 C CG  . ASP B 2 322  ? 216.096 171.176 132.108 1.00 47.94  ? 322  ASP A CG  1 
ATOM   12003 O OD1 . ASP B 2 322  ? 215.714 170.320 131.284 1.00 47.94  ? 322  ASP A OD1 1 
ATOM   12004 O OD2 . ASP B 2 322  ? 216.260 170.929 133.320 1.00 47.94  ? 322  ASP A OD2 1 
ATOM   12005 N N   . THR B 2 323  ? 213.545 173.549 132.645 1.00 45.96  ? 323  THR A N   1 
ATOM   12006 C CA  . THR B 2 323  ? 212.288 173.275 133.335 1.00 45.96  ? 323  THR A CA  1 
ATOM   12007 C C   . THR B 2 323  ? 211.096 173.503 132.413 1.00 45.96  ? 323  THR A C   1 
ATOM   12008 O O   . THR B 2 323  ? 210.179 172.673 132.354 1.00 45.96  ? 323  THR A O   1 
ATOM   12009 C CB  . THR B 2 323  ? 212.172 174.141 134.588 1.00 45.96  ? 323  THR A CB  1 
ATOM   12010 O OG1 . THR B 2 323  ? 212.915 173.543 135.656 1.00 45.96  ? 323  THR A OG1 1 
ATOM   12011 C CG2 . THR B 2 323  ? 210.719 174.267 135.014 1.00 45.96  ? 323  THR A CG2 1 
ATOM   12012 N N   . ASN B 2 324  ? 211.102 174.611 131.667 1.00 47.46  ? 324  ASN A N   1 
ATOM   12013 C CA  . ASN B 2 324  ? 209.989 174.893 130.763 1.00 47.46  ? 324  ASN A CA  1 
ATOM   12014 C C   . ASN B 2 324  ? 209.912 173.864 129.642 1.00 47.46  ? 324  ASN A C   1 
ATOM   12015 O O   . ASN B 2 324  ? 208.815 173.459 129.237 1.00 47.46  ? 324  ASN A O   1 
ATOM   12016 C CB  . ASN B 2 324  ? 210.119 176.306 130.194 1.00 47.46  ? 324  ASN A CB  1 
ATOM   12017 C CG  . ASN B 2 324  ? 209.429 177.344 131.055 1.00 47.46  ? 324  ASN A CG  1 
ATOM   12018 O OD1 . ASN B 2 324  ? 208.896 177.029 132.117 1.00 47.46  ? 324  ASN A OD1 1 
ATOM   12019 N ND2 . ASN B 2 324  ? 209.430 178.589 130.599 1.00 47.46  ? 324  ASN A ND2 1 
ATOM   12020 N N   . MET B 2 325  ? 211.064 173.432 129.122 1.00 48.73  ? 325  MET A N   1 
ATOM   12021 C CA  . MET B 2 325  ? 211.075 172.413 128.080 1.00 48.73  ? 325  MET A CA  1 
ATOM   12022 C C   . MET B 2 325  ? 210.521 171.092 128.592 1.00 48.73  ? 325  MET A C   1 
ATOM   12023 O O   . MET B 2 325  ? 209.707 170.449 127.919 1.00 48.73  ? 325  MET A O   1 
ATOM   12024 C CB  . MET B 2 325  ? 212.495 172.227 127.545 1.00 48.73  ? 325  MET A CB  1 
ATOM   12025 C CG  . MET B 2 325  ? 212.567 171.628 126.150 1.00 48.73  ? 325  MET A CG  1 
ATOM   12026 S SD  . MET B 2 325  ? 212.384 169.835 126.121 1.00 48.73  ? 325  MET A SD  1 
ATOM   12027 C CE  . MET B 2 325  ? 214.060 169.326 125.753 1.00 48.73  ? 325  MET A CE  1 
ATOM   12028 N N   . ARG B 2 326  ? 210.951 170.666 129.785 1.00 49.79  ? 326  ARG A N   1 
ATOM   12029 C CA  . ARG B 2 326  ? 210.465 169.403 130.330 1.00 49.79  ? 326  ARG A CA  1 
ATOM   12030 C C   . ARG B 2 326  ? 208.981 169.473 130.665 1.00 49.79  ? 326  ARG A C   1 
ATOM   12031 O O   . ARG B 2 326  ? 208.277 168.464 130.554 1.00 49.79  ? 326  ARG A O   1 
ATOM   12032 C CB  . ARG B 2 326  ? 211.283 169.007 131.560 1.00 49.79  ? 326  ARG A CB  1 
ATOM   12033 C CG  . ARG B 2 326  ? 210.658 169.384 132.892 1.00 49.79  ? 326  ARG A CG  1 
ATOM   12034 C CD  . ARG B 2 326  ? 211.564 169.031 134.056 1.00 49.79  ? 326  ARG A CD  1 
ATOM   12035 N NE  . ARG B 2 326  ? 211.767 167.591 134.182 1.00 49.79  ? 326  ARG A NE  1 
ATOM   12036 C CZ  . ARG B 2 326  ? 212.757 167.034 134.862 1.00 49.79  ? 326  ARG A CZ  1 
ATOM   12037 N NH1 . ARG B 2 326  ? 213.659 167.767 135.497 1.00 49.79  ? 326  ARG A NH1 1 
ATOM   12038 N NH2 . ARG B 2 326  ? 212.847 165.708 134.909 1.00 49.79  ? 326  ARG A NH2 1 
ATOM   12039 N N   . ALA B 2 327  ? 208.487 170.646 131.068 1.00 49.35  ? 327  ALA A N   1 
ATOM   12040 C CA  . ALA B 2 327  ? 207.057 170.789 131.325 1.00 49.35  ? 327  ALA A CA  1 
ATOM   12041 C C   . ALA B 2 327  ? 206.260 170.727 130.028 1.00 49.35  ? 327  ALA A C   1 
ATOM   12042 O O   . ALA B 2 327  ? 205.269 169.995 129.932 1.00 49.35  ? 327  ALA A O   1 
ATOM   12043 C CB  . ALA B 2 327  ? 206.783 172.098 132.065 1.00 49.35  ? 327  ALA A CB  1 
ATOM   12044 N N   . LYS B 2 328  ? 206.682 171.484 129.016 1.00 50.33  ? 328  LYS A N   1 
ATOM   12045 C CA  . LYS B 2 328  ? 205.971 171.521 127.745 1.00 50.33  ? 328  LYS A CA  1 
ATOM   12046 C C   . LYS B 2 328  ? 206.283 170.333 126.850 1.00 50.33  ? 328  LYS A C   1 
ATOM   12047 O O   . LYS B 2 328  ? 205.573 170.119 125.861 1.00 50.33  ? 328  LYS A O   1 
ATOM   12048 C CB  . LYS B 2 328  ? 206.285 172.825 127.007 1.00 50.33  ? 328  LYS A CB  1 
ATOM   12049 C CG  . LYS B 2 328  ? 207.568 172.795 126.190 1.00 50.33  ? 328  LYS A CG  1 
ATOM   12050 C CD  . LYS B 2 328  ? 207.964 174.195 125.744 1.00 50.33  ? 328  LYS A CD  1 
ATOM   12051 C CE  . LYS B 2 328  ? 209.079 174.160 124.708 1.00 50.33  ? 328  LYS A CE  1 
ATOM   12052 N NZ  . LYS B 2 328  ? 209.514 175.532 124.323 1.00 50.33  ? 328  LYS A NZ  1 
ATOM   12053 N N   . GLY B 2 329  ? 207.317 169.558 127.164 1.00 50.59  ? 329  GLY A N   1 
ATOM   12054 C CA  . GLY B 2 329  ? 207.655 168.383 126.382 1.00 50.59  ? 329  GLY A CA  1 
ATOM   12055 C C   . GLY B 2 329  ? 208.315 168.698 125.055 1.00 50.59  ? 329  GLY A C   1 
ATOM   12056 O O   . GLY B 2 329  ? 208.699 167.793 124.314 1.00 50.59  ? 329  GLY A O   1 
ATOM   12057 N N   . ILE B 2 370  ? 227.135 201.776 152.514 1.00 45.54  ? 370  ILE A N   1 
ATOM   12058 C CA  . ILE B 2 370  ? 226.359 201.555 151.300 1.00 45.54  ? 370  ILE A CA  1 
ATOM   12059 C C   . ILE B 2 370  ? 225.066 202.355 151.356 1.00 45.54  ? 370  ILE A C   1 
ATOM   12060 O O   . ILE B 2 370  ? 224.401 202.561 150.336 1.00 45.54  ? 370  ILE A O   1 
ATOM   12061 C CB  . ILE B 2 370  ? 226.068 200.063 151.091 1.00 45.54  ? 370  ILE A CB  1 
ATOM   12062 C CG1 . ILE B 2 370  ? 224.787 199.657 151.825 1.00 45.54  ? 370  ILE A CG1 1 
ATOM   12063 C CG2 . ILE B 2 370  ? 227.240 199.223 151.572 1.00 45.54  ? 370  ILE A CG2 1 
ATOM   12064 C CD1 . ILE B 2 370  ? 224.190 198.369 151.328 1.00 45.54  ? 370  ILE A CD1 1 
ATOM   12065 N N   . PHE B 2 371  ? 224.710 202.808 152.561 1.00 46.43  ? 371  PHE A N   1 
ATOM   12066 C CA  . PHE B 2 371  ? 223.495 203.600 152.703 1.00 46.43  ? 371  PHE A CA  1 
ATOM   12067 C C   . PHE B 2 371  ? 223.625 204.942 151.999 1.00 46.43  ? 371  PHE A C   1 
ATOM   12068 O O   . PHE B 2 371  ? 222.622 205.500 151.546 1.00 46.43  ? 371  PHE A O   1 
ATOM   12069 C CB  . PHE B 2 371  ? 223.152 203.783 154.178 1.00 46.43  ? 371  PHE A CB  1 
ATOM   12070 C CG  . PHE B 2 371  ? 222.151 202.791 154.680 1.00 46.43  ? 371  PHE A CG  1 
ATOM   12071 C CD1 . PHE B 2 371  ? 220.796 203.059 154.614 1.00 46.43  ? 371  PHE A CD1 1 
ATOM   12072 C CD2 . PHE B 2 371  ? 222.563 201.576 155.203 1.00 46.43  ? 371  PHE A CD2 1 
ATOM   12073 C CE1 . PHE B 2 371  ? 219.868 202.144 155.069 1.00 46.43  ? 371  PHE A CE1 1 
ATOM   12074 C CE2 . PHE B 2 371  ? 221.641 200.657 155.661 1.00 46.43  ? 371  PHE A CE2 1 
ATOM   12075 C CZ  . PHE B 2 371  ? 220.293 200.941 155.593 1.00 46.43  ? 371  PHE A CZ  1 
ATOM   12076 N N   . LYS B 2 372  ? 224.846 205.465 151.877 1.00 47.49  ? 372  LYS A N   1 
ATOM   12077 C CA  . LYS B 2 372  ? 225.061 206.633 151.028 1.00 47.49  ? 372  LYS A CA  1 
ATOM   12078 C C   . LYS B 2 372  ? 224.639 206.341 149.594 1.00 47.49  ? 372  LYS A C   1 
ATOM   12079 O O   . LYS B 2 372  ? 223.927 207.132 148.962 1.00 47.49  ? 372  LYS A O   1 
ATOM   12080 C CB  . LYS B 2 372  ? 226.530 207.054 151.085 1.00 47.49  ? 372  LYS A CB  1 
ATOM   12081 C CG  . LYS B 2 372  ? 227.006 207.843 149.873 1.00 47.49  ? 372  LYS A CG  1 
ATOM   12082 C CD  . LYS B 2 372  ? 227.830 206.969 148.932 1.00 47.49  ? 372  LYS A CD  1 
ATOM   12083 C CE  . LYS B 2 372  ? 227.848 207.536 147.523 1.00 47.49  ? 372  LYS A CE  1 
ATOM   12084 N NZ  . LYS B 2 372  ? 228.542 206.630 146.570 1.00 47.49  ? 372  LYS A NZ  1 
ATOM   12085 N N   . GLN B 2 373  ? 225.063 205.190 149.070 1.00 45.09  ? 373  GLN A N   1 
ATOM   12086 C CA  . GLN B 2 373  ? 224.699 204.811 147.713 1.00 45.09  ? 373  GLN A CA  1 
ATOM   12087 C C   . GLN B 2 373  ? 223.192 204.637 147.581 1.00 45.09  ? 373  GLN A C   1 
ATOM   12088 O O   . GLN B 2 373  ? 222.604 205.050 146.582 1.00 45.09  ? 373  GLN A O   1 
ATOM   12089 C CB  . GLN B 2 373  ? 225.420 203.526 147.309 1.00 45.09  ? 373  GLN A CB  1 
ATOM   12090 C CG  . GLN B 2 373  ? 226.843 203.408 147.839 1.00 45.09  ? 373  GLN A CG  1 
ATOM   12091 C CD  . GLN B 2 373  ? 227.378 201.992 147.759 1.00 45.09  ? 373  GLN A CD  1 
ATOM   12092 O OE1 . GLN B 2 373  ? 226.613 201.033 147.668 1.00 45.09  ? 373  GLN A OE1 1 
ATOM   12093 N NE2 . GLN B 2 373  ? 228.699 201.857 147.793 1.00 45.09  ? 373  GLN A NE2 1 
ATOM   12094 N N   . VAL B 2 374  ? 222.551 204.027 148.578 1.00 45.28  ? 374  VAL A N   1 
ATOM   12095 C CA  . VAL B 2 374  ? 221.116 203.780 148.470 1.00 45.28  ? 374  VAL A CA  1 
ATOM   12096 C C   . VAL B 2 374  ? 220.335 205.091 148.559 1.00 45.28  ? 374  VAL A C   1 
ATOM   12097 O O   . VAL B 2 374  ? 219.315 205.263 147.881 1.00 45.28  ? 374  VAL A O   1 
ATOM   12098 C CB  . VAL B 2 374  ? 220.649 202.753 149.518 1.00 45.28  ? 374  VAL A CB  1 
ATOM   12099 C CG1 . VAL B 2 374  ? 220.319 203.407 150.850 1.00 45.28  ? 374  VAL A CG1 1 
ATOM   12100 C CG2 . VAL B 2 374  ? 219.449 201.987 148.996 1.00 45.28  ? 374  VAL A CG2 1 
ATOM   12101 N N   . TRP B 2 375  ? 220.801 206.039 149.376 1.00 49.78  ? 375  TRP A N   1 
ATOM   12102 C CA  . TRP B 2 375  ? 220.127 207.333 149.452 1.00 49.78  ? 375  TRP A CA  1 
ATOM   12103 C C   . TRP B 2 375  ? 220.295 208.115 148.154 1.00 49.78  ? 375  TRP A C   1 
ATOM   12104 O O   . TRP B 2 375  ? 219.344 208.743 147.672 1.00 49.78  ? 375  TRP A O   1 
ATOM   12105 C CB  . TRP B 2 375  ? 220.656 208.131 150.641 1.00 49.78  ? 375  TRP A CB  1 
ATOM   12106 C CG  . TRP B 2 375  ? 220.491 209.606 150.483 1.00 49.78  ? 375  TRP A CG  1 
ATOM   12107 C CD1 . TRP B 2 375  ? 221.430 210.495 150.055 1.00 49.78  ? 375  TRP A CD1 1 
ATOM   12108 C CD2 . TRP B 2 375  ? 219.312 210.369 150.755 1.00 49.78  ? 375  TRP A CD2 1 
ATOM   12109 N NE1 . TRP B 2 375  ? 220.910 211.765 150.040 1.00 49.78  ? 375  TRP A NE1 1 
ATOM   12110 C CE2 . TRP B 2 375  ? 219.609 211.716 150.468 1.00 49.78  ? 375  TRP A CE2 1 
ATOM   12111 C CE3 . TRP B 2 375  ? 218.033 210.047 151.216 1.00 49.78  ? 375  TRP A CE3 1 
ATOM   12112 C CZ2 . TRP B 2 375  ? 218.675 212.738 150.624 1.00 49.78  ? 375  TRP A CZ2 1 
ATOM   12113 C CZ3 . TRP B 2 375  ? 217.105 211.063 151.371 1.00 49.78  ? 375  TRP A CZ3 1 
ATOM   12114 C CH2 . TRP B 2 375  ? 217.433 212.392 151.075 1.00 49.78  ? 375  TRP A CH2 1 
ATOM   12115 N N   . ASP B 2 376  ? 221.498 208.086 147.574 1.00 51.45  ? 376  ASP A N   1 
ATOM   12116 C CA  . ASP B 2 376  ? 221.696 208.728 146.277 1.00 51.45  ? 376  ASP A CA  1 
ATOM   12117 C C   . ASP B 2 376  ? 220.870 208.043 145.197 1.00 51.45  ? 376  ASP A C   1 
ATOM   12118 O O   . ASP B 2 376  ? 220.407 208.690 144.254 1.00 51.45  ? 376  ASP A O   1 
ATOM   12119 C CB  . ASP B 2 376  ? 223.179 208.724 145.911 1.00 51.45  ? 376  ASP A CB  1 
ATOM   12120 C CG  . ASP B 2 376  ? 223.560 209.875 145.002 1.00 51.45  ? 376  ASP A CG  1 
ATOM   12121 O OD1 . ASP B 2 376  ? 222.833 210.122 144.016 1.00 51.45  ? 376  ASP A OD1 1 
ATOM   12122 O OD2 . ASP B 2 376  ? 224.585 210.533 145.272 1.00 51.45  ? 376  ASP A OD2 1 
ATOM   12123 N N   . ASN B 2 377  ? 220.687 206.725 145.314 1.00 48.39  ? 377  ASN A N   1 
ATOM   12124 C CA  . ASN B 2 377  ? 219.826 205.998 144.385 1.00 48.39  ? 377  ASN A CA  1 
ATOM   12125 C C   . ASN B 2 377  ? 218.377 206.449 144.513 1.00 48.39  ? 377  ASN A C   1 
ATOM   12126 O O   . ASN B 2 377  ? 217.684 206.637 143.507 1.00 48.39  ? 377  ASN A O   1 
ATOM   12127 C CB  . ASN B 2 377  ? 219.945 204.496 144.640 1.00 48.39  ? 377  ASN A CB  1 
ATOM   12128 C CG  . ASN B 2 377  ? 219.416 203.664 143.494 1.00 48.39  ? 377  ASN A CG  1 
ATOM   12129 O OD1 . ASN B 2 377  ? 218.626 202.742 143.697 1.00 48.39  ? 377  ASN A OD1 1 
ATOM   12130 N ND2 . ASN B 2 377  ? 219.850 203.977 142.282 1.00 48.39  ? 377  ASN A ND2 1 
ATOM   12131 N N   . ALA B 2 378  ? 217.903 206.619 145.748 1.00 48.99  ? 378  ALA A N   1 
ATOM   12132 C CA  . ALA B 2 378  ? 216.546 207.111 145.957 1.00 48.99  ? 378  ALA A CA  1 
ATOM   12133 C C   . ALA B 2 378  ? 216.384 208.519 145.397 1.00 48.99  ? 378  ALA A C   1 
ATOM   12134 O O   . ALA B 2 378  ? 215.360 208.837 144.785 1.00 48.99  ? 378  ALA A O   1 
ATOM   12135 C CB  . ALA B 2 378  ? 216.195 207.076 147.443 1.00 48.99  ? 378  ALA A CB  1 
ATOM   12136 N N   . LEU B 2 379  ? 217.389 209.374 145.597 1.00 51.54  ? 379  LEU A N   1 
ATOM   12137 C CA  . LEU B 2 379  ? 217.332 210.719 145.034 1.00 51.54  ? 379  LEU A CA  1 
ATOM   12138 C C   . LEU B 2 379  ? 217.364 210.675 143.511 1.00 51.54  ? 379  LEU A C   1 
ATOM   12139 O O   . LEU B 2 379  ? 216.751 211.517 142.845 1.00 51.54  ? 379  LEU A O   1 
ATOM   12140 C CB  . LEU B 2 379  ? 218.478 211.570 145.583 1.00 51.54  ? 379  LEU A CB  1 
ATOM   12141 C CG  . LEU B 2 379  ? 218.457 213.082 145.335 1.00 51.54  ? 379  LEU A CG  1 
ATOM   12142 C CD1 . LEU B 2 379  ? 219.217 213.796 146.442 1.00 51.54  ? 379  LEU A CD1 1 
ATOM   12143 C CD2 . LEU B 2 379  ? 219.051 213.453 143.979 1.00 51.54  ? 379  LEU A CD2 1 
ATOM   12144 N N   . TYR B 2 380  ? 218.073 209.701 142.941 1.00 52.69  ? 380  TYR A N   1 
ATOM   12145 C CA  . TYR B 2 380  ? 218.095 209.528 141.495 1.00 52.69  ? 380  TYR A CA  1 
ATOM   12146 C C   . TYR B 2 380  ? 216.744 209.085 140.957 1.00 52.69  ? 380  TYR A C   1 
ATOM   12147 O O   . TYR B 2 380  ? 216.518 209.165 139.746 1.00 52.69  ? 380  TYR A O   1 
ATOM   12148 C CB  . TYR B 2 380  ? 219.172 208.512 141.110 1.00 52.69  ? 380  TYR A CB  1 
ATOM   12149 C CG  . TYR B 2 380  ? 219.454 208.430 139.626 1.00 52.69  ? 380  TYR A CG  1 
ATOM   12150 C CD1 . TYR B 2 380  ? 219.750 209.567 138.891 1.00 52.69  ? 380  TYR A CD1 1 
ATOM   12151 C CD2 . TYR B 2 380  ? 219.437 207.209 138.966 1.00 52.69  ? 380  TYR A CD2 1 
ATOM   12152 C CE1 . TYR B 2 380  ? 220.014 209.494 137.536 1.00 52.69  ? 380  TYR A CE1 1 
ATOM   12153 C CE2 . TYR B 2 380  ? 219.698 207.126 137.614 1.00 52.69  ? 380  TYR A CE2 1 
ATOM   12154 C CZ  . TYR B 2 380  ? 219.985 208.270 136.904 1.00 52.69  ? 380  TYR A CZ  1 
ATOM   12155 O OH  . TYR B 2 380  ? 220.247 208.186 135.556 1.00 52.69  ? 380  TYR A OH  1 
ATOM   12156 N N   . CYS B 2 381  ? 215.850 208.615 141.824 1.00 51.36  ? 381  CYS A N   1 
ATOM   12157 C CA  . CYS B 2 381  ? 214.501 208.254 141.416 1.00 51.36  ? 381  CYS A CA  1 
ATOM   12158 C C   . CYS B 2 381  ? 213.530 209.429 141.454 1.00 51.36  ? 381  CYS A C   1 
ATOM   12159 O O   . CYS B 2 381  ? 212.416 209.299 140.937 1.00 51.36  ? 381  CYS A O   1 
ATOM   12160 C CB  . CYS B 2 381  ? 213.966 207.129 142.306 1.00 51.36  ? 381  CYS A CB  1 
ATOM   12161 S SG  . CYS B 2 381  ? 214.612 205.499 141.914 1.00 51.36  ? 381  CYS A SG  1 
ATOM   12162 N N   . VAL B 2 382  ? 213.913 210.558 142.047 1.00 51.24  ? 382  VAL A N   1 
ATOM   12163 C CA  . VAL B 2 382  ? 212.974 211.659 142.242 1.00 51.24  ? 382  VAL A CA  1 
ATOM   12164 C C   . VAL B 2 382  ? 213.480 212.941 141.597 1.00 51.24  ? 382  VAL A C   1 
ATOM   12165 O O   . VAL B 2 382  ? 212.843 213.481 140.685 1.00 51.24  ? 382  VAL A O   1 
ATOM   12166 C CB  . VAL B 2 382  ? 212.703 211.877 143.742 1.00 51.24  ? 382  VAL A CB  1 
ATOM   12167 C CG1 . VAL B 2 382  ? 211.907 213.152 143.959 1.00 51.24  ? 382  VAL A CG1 1 
ATOM   12168 C CG2 . VAL B 2 382  ? 211.974 210.678 144.324 1.00 51.24  ? 382  VAL A CG2 1 
ATOM   12169 N N   . MET B 2 383  ? 214.617 213.445 142.060 1.00 52.82  ? 383  MET A N   1 
ATOM   12170 C CA  . MET B 2 383  ? 215.118 214.748 141.619 1.00 52.82  ? 383  MET A CA  1 
ATOM   12171 C C   . MET B 2 383  ? 216.151 214.588 140.505 1.00 52.82  ? 383  MET A C   1 
ATOM   12172 O O   . MET B 2 383  ? 217.272 215.093 140.576 1.00 52.82  ? 383  MET A O   1 
ATOM   12173 C CB  . MET B 2 383  ? 215.696 215.515 142.805 1.00 52.82  ? 383  MET A CB  1 
ATOM   12174 C CG  . MET B 2 383  ? 214.784 215.549 144.019 1.00 52.82  ? 383  MET A CG  1 
ATOM   12175 S SD  . MET B 2 383  ? 215.691 215.798 145.556 1.00 52.82  ? 383  MET A SD  1 
ATOM   12176 C CE  . MET B 2 383  ? 216.949 216.954 145.020 1.00 52.82  ? 383  MET A CE  1 
ATOM   12177 N N   . GLY B 2 384  ? 215.754 213.878 139.456 1.00 54.48  ? 384  GLY A N   1 
ATOM   12178 C CA  . GLY B 2 384  ? 216.629 213.643 138.333 1.00 54.48  ? 384  GLY A CA  1 
ATOM   12179 C C   . GLY B 2 384  ? 215.868 213.467 137.036 1.00 54.48  ? 384  GLY A C   1 
ATOM   12180 O O   . GLY B 2 384  ? 214.846 214.117 136.793 1.00 54.48  ? 384  GLY A O   1 
ATOM   12181 N N   . PRO B 2 385  ? 216.370 212.590 136.162 1.00 53.54  ? 385  PRO A N   1 
ATOM   12182 C CA  . PRO B 2 385  ? 215.627 212.302 134.925 1.00 53.54  ? 385  PRO A CA  1 
ATOM   12183 C C   . PRO B 2 385  ? 214.237 211.761 135.195 1.00 53.54  ? 385  PRO A C   1 
ATOM   12184 O O   . PRO B 2 385  ? 213.288 212.091 134.472 1.00 53.54  ? 385  PRO A O   1 
ATOM   12185 C CB  . PRO B 2 385  ? 216.521 211.277 134.217 1.00 53.54  ? 385  PRO A CB  1 
ATOM   12186 C CG  . PRO B 2 385  ? 217.281 210.625 135.322 1.00 53.54  ? 385  PRO A CG  1 
ATOM   12187 C CD  . PRO B 2 385  ? 217.533 211.705 136.330 1.00 53.54  ? 385  PRO A CD  1 
ATOM   12188 N N   . TYR B 2 386  ? 214.090 210.939 136.231 1.00 52.81  ? 386  TYR A N   1 
ATOM   12189 C CA  . TYR B 2 386  ? 212.785 210.448 136.666 1.00 52.81  ? 386  TYR A CA  1 
ATOM   12190 C C   . TYR B 2 386  ? 212.250 211.441 137.685 1.00 52.81  ? 386  TYR A C   1 
ATOM   12191 O O   . TYR B 2 386  ? 212.414 211.275 138.893 1.00 52.81  ? 386  TYR A O   1 
ATOM   12192 C CB  . TYR B 2 386  ? 212.907 209.043 137.244 1.00 52.81  ? 386  TYR A CB  1 
ATOM   12193 C CG  . TYR B 2 386  ? 213.545 208.070 136.284 1.00 52.81  ? 386  TYR A CG  1 
ATOM   12194 C CD1 . TYR B 2 386  ? 212.811 207.494 135.260 1.00 52.81  ? 386  TYR A CD1 1 
ATOM   12195 C CD2 . TYR B 2 386  ? 214.890 207.743 136.390 1.00 52.81  ? 386  TYR A CD2 1 
ATOM   12196 C CE1 . TYR B 2 386  ? 213.390 206.611 134.377 1.00 52.81  ? 386  TYR A CE1 1 
ATOM   12197 C CE2 . TYR B 2 386  ? 215.479 206.864 135.511 1.00 52.81  ? 386  TYR A CE2 1 
ATOM   12198 C CZ  . TYR B 2 386  ? 214.725 206.298 134.505 1.00 52.81  ? 386  TYR A CZ  1 
ATOM   12199 O OH  . TYR B 2 386  ? 215.309 205.421 133.626 1.00 52.81  ? 386  TYR A OH  1 
ATOM   12200 N N   . ARG B 2 387  ? 211.629 212.509 137.188 1.00 54.54  ? 387  ARG A N   1 
ATOM   12201 C CA  . ARG B 2 387  ? 211.101 213.561 138.048 1.00 54.54  ? 387  ARG A CA  1 
ATOM   12202 C C   . ARG B 2 387  ? 209.592 213.693 137.960 1.00 54.54  ? 387  ARG A C   1 
ATOM   12203 O O   . ARG B 2 387  ? 208.908 213.651 138.988 1.00 54.54  ? 387  ARG A O   1 
ATOM   12204 C CB  . ARG B 2 387  ? 211.758 214.906 137.706 1.00 54.54  ? 387  ARG A CB  1 
ATOM   12205 C CG  . ARG B 2 387  ? 211.180 216.078 138.479 1.00 54.54  ? 387  ARG A CG  1 
ATOM   12206 C CD  . ARG B 2 387  ? 212.151 217.242 138.528 1.00 54.54  ? 387  ARG A CD  1 
ATOM   12207 N NE  . ARG B 2 387  ? 212.004 218.126 137.380 1.00 54.54  ? 387  ARG A NE  1 
ATOM   12208 C CZ  . ARG B 2 387  ? 211.224 219.196 137.355 1.00 54.54  ? 387  ARG A CZ  1 
ATOM   12209 N NH1 . ARG B 2 387  ? 210.499 219.546 138.405 1.00 54.54  ? 387  ARG A NH1 1 
ATOM   12210 N NH2 . ARG B 2 387  ? 211.172 219.937 136.250 1.00 54.54  ? 387  ARG A NH2 1 
ATOM   12211 N N   . MET B 2 388  ? 209.046 213.874 136.755 1.00 54.91  ? 388  MET A N   1 
ATOM   12212 C CA  . MET B 2 388  ? 207.603 214.044 136.626 1.00 54.91  ? 388  MET A CA  1 
ATOM   12213 C C   . MET B 2 388  ? 206.874 212.721 136.809 1.00 54.91  ? 388  MET A C   1 
ATOM   12214 O O   . MET B 2 388  ? 205.817 212.670 137.453 1.00 54.91  ? 388  MET A O   1 
ATOM   12215 C CB  . MET B 2 388  ? 207.269 214.660 135.268 1.00 54.91  ? 388  MET A CB  1 
ATOM   12216 C CG  . MET B 2 388  ? 206.345 215.859 135.347 1.00 54.91  ? 388  MET A CG  1 
ATOM   12217 S SD  . MET B 2 388  ? 206.928 217.094 136.524 1.00 54.91  ? 388  MET A SD  1 
ATOM   12218 C CE  . MET B 2 388  ? 208.101 217.992 135.513 1.00 54.91  ? 388  MET A CE  1 
ATOM   12219 N N   . ASN B 2 389  ? 207.428 211.640 136.256 1.00 51.24  ? 389  ASN A N   1 
ATOM   12220 C CA  . ASN B 2 389  ? 206.773 210.340 136.342 1.00 51.24  ? 389  ASN A CA  1 
ATOM   12221 C C   . ASN B 2 389  ? 206.621 209.897 137.792 1.00 51.24  ? 389  ASN A C   1 
ATOM   12222 O O   . ASN B 2 389  ? 205.549 209.437 138.202 1.00 51.24  ? 389  ASN A O   1 
ATOM   12223 C CB  . ASN B 2 389  ? 207.562 209.302 135.544 1.00 51.24  ? 389  ASN A CB  1 
ATOM   12224 C CG  . ASN B 2 389  ? 207.813 209.735 134.115 1.00 51.24  ? 389  ASN A CG  1 
ATOM   12225 O OD1 . ASN B 2 389  ? 207.399 210.815 133.698 1.00 51.24  ? 389  ASN A OD1 1 
ATOM   12226 N ND2 . ASN B 2 389  ? 208.502 208.892 133.355 1.00 51.24  ? 389  ASN A ND2 1 
ATOM   12227 N N   . THR B 2 390  ? 207.685 210.042 138.585 1.00 46.87  ? 390  THR A N   1 
ATOM   12228 C CA  . THR B 2 390  ? 207.608 209.627 139.982 1.00 46.87  ? 390  THR A CA  1 
ATOM   12229 C C   . THR B 2 390  ? 206.638 210.501 140.766 1.00 46.87  ? 390  THR A C   1 
ATOM   12230 O O   . THR B 2 390  ? 205.933 210.006 141.649 1.00 46.87  ? 390  THR A O   1 
ATOM   12231 C CB  . THR B 2 390  ? 208.991 209.655 140.626 1.00 46.87  ? 390  THR A CB  1 
ATOM   12232 O OG1 . THR B 2 390  ? 208.857 209.523 142.047 1.00 46.87  ? 390  THR A OG1 1 
ATOM   12233 C CG2 . THR B 2 390  ? 209.687 210.955 140.319 1.00 46.87  ? 390  THR A CG2 1 
ATOM   12234 N N   . LEU B 2 391  ? 206.589 211.800 140.464 1.00 45.88  ? 391  LEU A N   1 
ATOM   12235 C CA  . LEU B 2 391  ? 205.647 212.677 141.153 1.00 45.88  ? 391  LEU A CA  1 
ATOM   12236 C C   . LEU B 2 391  ? 204.211 212.262 140.870 1.00 45.88  ? 391  LEU A C   1 
ATOM   12237 O O   . LEU B 2 391  ? 203.386 212.154 141.788 1.00 45.88  ? 391  LEU A O   1 
ATOM   12238 C CB  . LEU B 2 391  ? 205.881 214.129 140.736 1.00 45.88  ? 391  LEU A CB  1 
ATOM   12239 C CG  . LEU B 2 391  ? 206.809 214.949 141.634 1.00 45.88  ? 391  LEU A CG  1 
ATOM   12240 C CD1 . LEU B 2 391  ? 206.711 216.430 141.297 1.00 45.88  ? 391  LEU A CD1 1 
ATOM   12241 C CD2 . LEU B 2 391  ? 206.497 214.705 143.102 1.00 45.88  ? 391  LEU A CD2 1 
ATOM   12242 N N   . ILE B 2 392  ? 203.896 212.005 139.596 1.00 44.80  ? 392  ILE A N   1 
ATOM   12243 C CA  . ILE B 2 392  ? 202.543 211.583 139.245 1.00 44.80  ? 392  ILE A CA  1 
ATOM   12244 C C   . ILE B 2 392  ? 202.215 210.242 139.892 1.00 44.80  ? 392  ILE A C   1 
ATOM   12245 O O   . ILE B 2 392  ? 201.109 210.037 140.409 1.00 44.80  ? 392  ILE A O   1 
ATOM   12246 C CB  . ILE B 2 392  ? 202.374 211.533 137.715 1.00 44.80  ? 392  ILE A CB  1 
ATOM   12247 C CG1 . ILE B 2 392  ? 202.699 212.892 137.092 1.00 44.80  ? 392  ILE A CG1 1 
ATOM   12248 C CG2 . ILE B 2 392  ? 200.965 211.114 137.349 1.00 44.80  ? 392  ILE A CG2 1 
ATOM   12249 C CD1 . ILE B 2 392  ? 201.932 214.039 137.701 1.00 44.80  ? 392  ILE A CD1 1 
ATOM   12250 N N   . LEU B 2 393  ? 203.174 209.311 139.880 1.00 41.27  ? 393  LEU A N   1 
ATOM   12251 C CA  . LEU B 2 393  ? 202.936 208.002 140.478 1.00 41.27  ? 393  LEU A CA  1 
ATOM   12252 C C   . LEU B 2 393  ? 202.701 208.114 141.978 1.00 41.27  ? 393  LEU A C   1 
ATOM   12253 O O   . LEU B 2 393  ? 201.824 207.439 142.527 1.00 41.27  ? 393  LEU A O   1 
ATOM   12254 C CB  . LEU B 2 393  ? 204.108 207.070 140.185 1.00 41.27  ? 393  LEU A CB  1 
ATOM   12255 C CG  . LEU B 2 393  ? 203.934 206.162 138.970 1.00 41.27  ? 393  LEU A CG  1 
ATOM   12256 C CD1 . LEU B 2 393  ? 205.130 205.240 138.818 1.00 41.27  ? 393  LEU A CD1 1 
ATOM   12257 C CD2 . LEU B 2 393  ? 202.649 205.366 139.089 1.00 41.27  ? 393  LEU A CD2 1 
ATOM   12258 N N   . ALA B 2 394  ? 203.476 208.961 142.657 1.00 40.87  ? 394  ALA A N   1 
ATOM   12259 C CA  . ALA B 2 394  ? 203.279 209.166 144.085 1.00 40.87  ? 394  ALA A CA  1 
ATOM   12260 C C   . ALA B 2 394  ? 201.907 209.763 144.368 1.00 40.87  ? 394  ALA A C   1 
ATOM   12261 O O   . ALA B 2 394  ? 201.229 209.356 145.317 1.00 40.87  ? 394  ALA A O   1 
ATOM   12262 C CB  . ALA B 2 394  ? 204.380 210.065 144.643 1.00 40.87  ? 394  ALA A CB  1 
ATOM   12263 N N   . VAL B 2 395  ? 201.480 210.725 143.545 1.00 40.01  ? 395  VAL A N   1 
ATOM   12264 C CA  . VAL B 2 395  ? 200.162 211.327 143.735 1.00 40.01  ? 395  VAL A CA  1 
ATOM   12265 C C   . VAL B 2 395  ? 199.073 210.271 143.592 1.00 40.01  ? 395  VAL A C   1 
ATOM   12266 O O   . VAL B 2 395  ? 198.152 210.185 144.419 1.00 40.01  ? 395  VAL A O   1 
ATOM   12267 C CB  . VAL B 2 395  ? 199.959 212.489 142.746 1.00 40.01  ? 395  VAL A CB  1 
ATOM   12268 C CG1 . VAL B 2 395  ? 198.484 212.681 142.436 1.00 40.01  ? 395  VAL A CG1 1 
ATOM   12269 C CG2 . VAL B 2 395  ? 200.561 213.767 143.306 1.00 40.01  ? 395  VAL A CG2 1 
ATOM   12270 N N   . VAL B 2 396  ? 199.168 209.441 142.549 1.00 39.51  ? 396  VAL A N   1 
ATOM   12271 C CA  . VAL B 2 396  ? 198.149 208.416 142.325 1.00 39.51  ? 396  VAL A CA  1 
ATOM   12272 C C   . VAL B 2 396  ? 198.132 207.409 143.468 1.00 39.51  ? 396  VAL A C   1 
ATOM   12273 O O   . VAL B 2 396  ? 197.060 207.020 143.959 1.00 39.51  ? 396  VAL A O   1 
ATOM   12274 C CB  . VAL B 2 396  ? 198.375 207.724 140.969 1.00 39.51  ? 396  VAL A CB  1 
ATOM   12275 C CG1 . VAL B 2 396  ? 197.310 206.674 140.737 1.00 39.51  ? 396  VAL A CG1 1 
ATOM   12276 C CG2 . VAL B 2 396  ? 198.353 208.739 139.846 1.00 39.51  ? 396  VAL A CG2 1 
ATOM   12277 N N   . TRP B 2 397  ? 199.313 206.963 143.906 1.00 37.14  ? 397  TRP A N   1 
ATOM   12278 C CA  . TRP B 2 397  ? 199.378 205.983 144.984 1.00 37.14  ? 397  TRP A CA  1 
ATOM   12279 C C   . TRP B 2 397  ? 198.797 206.550 146.270 1.00 37.14  ? 397  TRP A C   1 
ATOM   12280 O O   . TRP B 2 397  ? 198.042 205.865 146.969 1.00 37.14  ? 397  TRP A O   1 
ATOM   12281 C CB  . TRP B 2 397  ? 200.818 205.529 145.204 1.00 37.14  ? 397  TRP A CB  1 
ATOM   12282 C CG  . TRP B 2 397  ? 201.231 204.367 144.355 1.00 37.14  ? 397  TRP A CG  1 
ATOM   12283 C CD1 . TRP B 2 397  ? 201.743 204.420 143.094 1.00 37.14  ? 397  TRP A CD1 1 
ATOM   12284 C CD2 . TRP B 2 397  ? 201.161 202.980 144.703 1.00 37.14  ? 397  TRP A CD2 1 
ATOM   12285 N NE1 . TRP B 2 397  ? 202.004 203.152 142.637 1.00 37.14  ? 397  TRP A NE1 1 
ATOM   12286 C CE2 . TRP B 2 397  ? 201.653 202.251 143.604 1.00 37.14  ? 397  TRP A CE2 1 
ATOM   12287 C CE3 . TRP B 2 397  ? 200.731 202.286 145.836 1.00 37.14  ? 397  TRP A CE3 1 
ATOM   12288 C CZ2 . TRP B 2 397  ? 201.727 200.862 143.607 1.00 37.14  ? 397  TRP A CZ2 1 
ATOM   12289 C CZ3 . TRP B 2 397  ? 200.806 200.908 145.834 1.00 37.14  ? 397  TRP A CZ3 1 
ATOM   12290 C CH2 . TRP B 2 397  ? 201.300 200.211 144.728 1.00 37.14  ? 397  TRP A CH2 1 
ATOM   12291 N N   . PHE B 2 398  ? 199.129 207.801 146.597 1.00 35.20  ? 398  PHE A N   1 
ATOM   12292 C CA  . PHE B 2 398  ? 198.573 208.418 147.794 1.00 35.20  ? 398  PHE A CA  1 
ATOM   12293 C C   . PHE B 2 398  ? 197.058 208.526 147.701 1.00 35.20  ? 398  PHE A C   1 
ATOM   12294 O O   . PHE B 2 398  ? 196.350 208.207 148.661 1.00 35.20  ? 398  PHE A O   1 
ATOM   12295 C CB  . PHE B 2 398  ? 199.197 209.796 148.017 1.00 35.20  ? 398  PHE A CB  1 
ATOM   12296 C CG  . PHE B 2 398  ? 198.704 210.502 149.253 1.00 35.20  ? 398  PHE A CG  1 
ATOM   12297 C CD1 . PHE B 2 398  ? 198.277 209.790 150.361 1.00 35.20  ? 398  PHE A CD1 1 
ATOM   12298 C CD2 . PHE B 2 398  ? 198.657 211.883 149.299 1.00 35.20  ? 398  PHE A CD2 1 
ATOM   12299 C CE1 . PHE B 2 398  ? 197.822 210.442 151.486 1.00 35.20  ? 398  PHE A CE1 1 
ATOM   12300 C CE2 . PHE B 2 398  ? 198.201 212.539 150.425 1.00 35.20  ? 398  PHE A CE2 1 
ATOM   12301 C CZ  . PHE B 2 398  ? 197.784 211.815 151.519 1.00 35.20  ? 398  PHE A CZ  1 
ATOM   12302 N N   . ALA B 2 399  ? 196.539 208.953 146.549 1.00 35.61  ? 399  ALA A N   1 
ATOM   12303 C CA  . ALA B 2 399  ? 195.094 209.118 146.417 1.00 35.61  ? 399  ALA A CA  1 
ATOM   12304 C C   . ALA B 2 399  ? 194.366 207.790 146.602 1.00 35.61  ? 399  ALA A C   1 
ATOM   12305 O O   . ALA B 2 399  ? 193.382 207.704 147.355 1.00 35.61  ? 399  ALA A O   1 
ATOM   12306 C CB  . ALA B 2 399  ? 194.759 209.732 145.058 1.00 35.61  ? 399  ALA A CB  1 
ATOM   12307 N N   . MET B 2 400  ? 194.832 206.741 145.923 1.00 34.67  ? 400  MET A N   1 
ATOM   12308 C CA  . MET B 2 400  ? 194.160 205.450 146.045 1.00 34.67  ? 400  MET A CA  1 
ATOM   12309 C C   . MET B 2 400  ? 194.291 204.878 147.449 1.00 34.67  ? 400  MET A C   1 
ATOM   12310 O O   . MET B 2 400  ? 193.307 204.395 148.023 1.00 34.67  ? 400  MET A O   1 
ATOM   12311 C CB  . MET B 2 400  ? 194.691 204.459 145.011 1.00 34.67  ? 400  MET A CB  1 
ATOM   12312 C CG  . MET B 2 400  ? 193.638 203.453 144.567 1.00 34.67  ? 400  MET A CG  1 
ATOM   12313 S SD  . MET B 2 400  ? 192.396 204.113 143.442 1.00 34.67  ? 400  MET A SD  1 
ATOM   12314 C CE  . MET B 2 400  ? 191.105 202.884 143.582 1.00 34.67  ? 400  MET A CE  1 
ATOM   12315 N N   . ALA B 2 401  ? 195.494 204.913 148.026 1.00 33.67  ? 401  ALA A N   1 
ATOM   12316 C CA  . ALA B 2 401  ? 195.672 204.354 149.358 1.00 33.67  ? 401  ALA A CA  1 
ATOM   12317 C C   . ALA B 2 401  ? 195.000 205.199 150.427 1.00 33.67  ? 401  ALA A C   1 
ATOM   12318 O O   . ALA B 2 401  ? 194.838 204.739 151.560 1.00 33.67  ? 401  ALA A O   1 
ATOM   12319 C CB  . ALA B 2 401  ? 197.156 204.207 149.669 1.00 33.67  ? 401  ALA A CB  1 
ATOM   12320 N N   . PHE B 2 402  ? 194.616 206.427 150.092 1.00 31.86  ? 402  PHE A N   1 
ATOM   12321 C CA  . PHE B 2 402  ? 193.814 207.239 150.991 1.00 31.86  ? 402  PHE A CA  1 
ATOM   12322 C C   . PHE B 2 402  ? 192.356 206.802 150.932 1.00 31.86  ? 402  PHE A C   1 
ATOM   12323 O O   . PHE B 2 402  ? 191.786 206.360 151.934 1.00 31.86  ? 402  PHE A O   1 
ATOM   12324 C CB  . PHE B 2 402  ? 193.968 208.712 150.604 1.00 31.86  ? 402  PHE A CB  1 
ATOM   12325 C CG  . PHE B 2 402  ? 193.182 209.663 151.451 1.00 31.86  ? 402  PHE A CG  1 
ATOM   12326 C CD1 . PHE B 2 402  ? 193.005 209.430 152.798 1.00 31.86  ? 402  PHE A CD1 1 
ATOM   12327 C CD2 . PHE B 2 402  ? 192.648 210.811 150.899 1.00 31.86  ? 402  PHE A CD2 1 
ATOM   12328 C CE1 . PHE B 2 402  ? 192.296 210.313 153.578 1.00 31.86  ? 402  PHE A CE1 1 
ATOM   12329 C CE2 . PHE B 2 402  ? 191.939 211.697 151.674 1.00 31.86  ? 402  PHE A CE2 1 
ATOM   12330 C CZ  . PHE B 2 402  ? 191.763 211.448 153.016 1.00 31.86  ? 402  PHE A CZ  1 
ATOM   12331 N N   . SER B 2 403  ? 191.756 206.880 149.741 1.00 31.71  ? 403  SER A N   1 
ATOM   12332 C CA  . SER B 2 403  ? 190.330 206.598 149.616 1.00 31.71  ? 403  SER A CA  1 
ATOM   12333 C C   . SER B 2 403  ? 190.008 205.153 149.983 1.00 31.71  ? 403  SER A C   1 
ATOM   12334 O O   . SER B 2 403  ? 189.063 204.892 150.736 1.00 31.71  ? 403  SER A O   1 
ATOM   12335 C CB  . SER B 2 403  ? 189.859 206.893 148.196 1.00 31.71  ? 403  SER A CB  1 
ATOM   12336 O OG  . SER B 2 403  ? 190.076 205.762 147.374 1.00 31.71  ? 403  SER A OG  1 
ATOM   12337 N N   . TYR B 2 404  ? 190.777 204.201 149.451 1.00 31.00  ? 404  TYR A N   1 
ATOM   12338 C CA  . TYR B 2 404  ? 190.464 202.790 149.657 1.00 31.00  ? 404  TYR A CA  1 
ATOM   12339 C C   . TYR B 2 404  ? 190.622 202.392 151.118 1.00 31.00  ? 404  TYR A C   1 
ATOM   12340 O O   . TYR B 2 404  ? 189.725 201.775 151.707 1.00 31.00  ? 404  TYR A O   1 
ATOM   12341 C CB  . TYR B 2 404  ? 191.356 201.932 148.763 1.00 31.00  ? 404  TYR A CB  1 
ATOM   12342 C CG  . TYR B 2 404  ? 191.156 200.441 148.902 1.00 31.00  ? 404  TYR A CG  1 
ATOM   12343 C CD1 . TYR B 2 404  ? 190.233 199.770 148.117 1.00 31.00  ? 404  TYR A CD1 1 
ATOM   12344 C CD2 . TYR B 2 404  ? 191.908 199.704 149.803 1.00 31.00  ? 404  TYR A CD2 1 
ATOM   12345 C CE1 . TYR B 2 404  ? 190.056 198.406 148.238 1.00 31.00  ? 404  TYR A CE1 1 
ATOM   12346 C CE2 . TYR B 2 404  ? 191.736 198.344 149.932 1.00 31.00  ? 404  TYR A CE2 1 
ATOM   12347 C CZ  . TYR B 2 404  ? 190.810 197.700 149.145 1.00 31.00  ? 404  TYR A CZ  1 
ATOM   12348 O OH  . TYR B 2 404  ? 190.638 196.341 149.272 1.00 31.00  ? 404  TYR A OH  1 
ATOM   12349 N N   . TYR B 2 405  ? 191.765 202.727 151.716 1.00 33.06  ? 405  TYR A N   1 
ATOM   12350 C CA  . TYR B 2 405  ? 192.011 202.366 153.105 1.00 33.06  ? 405  TYR A CA  1 
ATOM   12351 C C   . TYR B 2 405  ? 191.217 203.219 154.080 1.00 33.06  ? 405  TYR A C   1 
ATOM   12352 O O   . TYR B 2 405  ? 191.208 202.911 155.276 1.00 33.06  ? 405  TYR A O   1 
ATOM   12353 C CB  . TYR B 2 405  ? 193.503 202.459 153.416 1.00 33.06  ? 405  TYR A CB  1 
ATOM   12354 C CG  . TYR B 2 405  ? 194.327 201.375 152.758 1.00 33.06  ? 405  TYR A CG  1 
ATOM   12355 C CD1 . TYR B 2 405  ? 194.038 200.034 152.968 1.00 33.06  ? 405  TYR A CD1 1 
ATOM   12356 C CD2 . TYR B 2 405  ? 195.380 201.691 151.913 1.00 33.06  ? 405  TYR A CD2 1 
ATOM   12357 C CE1 . TYR B 2 405  ? 194.783 199.043 152.366 1.00 33.06  ? 405  TYR A CE1 1 
ATOM   12358 C CE2 . TYR B 2 405  ? 196.131 200.707 151.309 1.00 33.06  ? 405  TYR A CE2 1 
ATOM   12359 C CZ  . TYR B 2 405  ? 195.829 199.385 151.538 1.00 33.06  ? 405  TYR A CZ  1 
ATOM   12360 O OH  . TYR B 2 405  ? 196.575 198.403 150.933 1.00 33.06  ? 405  TYR A OH  1 
ATOM   12361 N N   . GLY B 2 406  ? 190.560 204.278 153.614 1.00 31.79  ? 406  GLY A N   1 
ATOM   12362 C CA  . GLY B 2 406  ? 189.597 204.950 154.455 1.00 31.79  ? 406  GLY A CA  1 
ATOM   12363 C C   . GLY B 2 406  ? 188.238 204.287 154.400 1.00 31.79  ? 406  GLY A C   1 
ATOM   12364 O O   . GLY B 2 406  ? 187.637 204.010 155.439 1.00 31.79  ? 406  GLY A O   1 
ATOM   12365 N N   . LEU B 2 407  ? 187.751 204.008 153.189 1.00 29.55  ? 407  LEU A N   1 
ATOM   12366 C CA  . LEU B 2 407  ? 186.410 203.443 153.043 1.00 29.55  ? 407  LEU A CA  1 
ATOM   12367 C C   . LEU B 2 407  ? 186.333 202.022 153.589 1.00 29.55  ? 407  LEU A C   1 
ATOM   12368 O O   . LEU B 2 407  ? 185.310 201.631 154.168 1.00 29.55  ? 407  LEU A O   1 
ATOM   12369 C CB  . LEU B 2 407  ? 185.985 203.475 151.578 1.00 29.55  ? 407  LEU A CB  1 
ATOM   12370 C CG  . LEU B 2 407  ? 185.529 204.831 151.045 1.00 29.55  ? 407  LEU A CG  1 
ATOM   12371 C CD1 . LEU B 2 407  ? 184.567 204.643 149.891 1.00 29.55  ? 407  LEU A CD1 1 
ATOM   12372 C CD2 . LEU B 2 407  ? 184.885 205.649 152.144 1.00 29.55  ? 407  LEU A CD2 1 
ATOM   12373 N N   . THR B 2 408  ? 187.398 201.231 153.408 1.00 31.83  ? 408  THR A N   1 
ATOM   12374 C CA  . THR B 2 408  ? 187.366 199.841 153.846 1.00 31.83  ? 408  THR A CA  1 
ATOM   12375 C C   . THR B 2 408  ? 187.147 199.731 155.349 1.00 31.83  ? 408  THR A C   1 
ATOM   12376 O O   . THR B 2 408  ? 186.549 198.758 155.819 1.00 31.83  ? 408  THR A O   1 
ATOM   12377 C CB  . THR B 2 408  ? 188.664 199.142 153.440 1.00 31.83  ? 408  THR A CB  1 
ATOM   12378 O OG1 . THR B 2 408  ? 188.802 199.196 152.016 1.00 31.83  ? 408  THR A OG1 1 
ATOM   12379 C CG2 . THR B 2 408  ? 188.660 197.687 153.878 1.00 31.83  ? 408  THR A CG2 1 
ATOM   12380 N N   . VAL B 2 409  ? 187.599 200.722 156.110 1.00 31.94  ? 409  VAL A N   1 
ATOM   12381 C CA  . VAL B 2 409  ? 187.348 200.749 157.544 1.00 31.94  ? 409  VAL A CA  1 
ATOM   12382 C C   . VAL B 2 409  ? 186.120 201.586 157.892 1.00 31.94  ? 409  VAL A C   1 
ATOM   12383 O O   . VAL B 2 409  ? 185.499 201.347 158.938 1.00 31.94  ? 409  VAL A O   1 
ATOM   12384 C CB  . VAL B 2 409  ? 188.583 201.273 158.300 1.00 31.94  ? 409  VAL A CB  1 
ATOM   12385 C CG1 . VAL B 2 409  ? 188.452 201.017 159.795 1.00 31.94  ? 409  VAL A CG1 1 
ATOM   12386 C CG2 . VAL B 2 409  ? 189.836 200.633 157.742 1.00 31.94  ? 409  VAL A CG2 1 
ATOM   12387 N N   . TRP B 2 410  ? 185.747 202.544 157.043 1.00 29.78  ? 410  TRP A N   1 
ATOM   12388 C CA  . TRP B 2 410  ? 184.549 203.332 157.301 1.00 29.78  ? 410  TRP A CA  1 
ATOM   12389 C C   . TRP B 2 410  ? 183.297 202.473 157.245 1.00 29.78  ? 410  TRP A C   1 
ATOM   12390 O O   . TRP B 2 410  ? 182.383 202.644 158.060 1.00 29.78  ? 410  TRP A O   1 
ATOM   12391 C CB  . TRP B 2 410  ? 184.445 204.467 156.289 1.00 29.78  ? 410  TRP A CB  1 
ATOM   12392 C CG  . TRP B 2 410  ? 183.329 205.403 156.568 1.00 29.78  ? 410  TRP A CG  1 
ATOM   12393 C CD1 . TRP B 2 410  ? 183.206 206.230 157.640 1.00 29.78  ? 410  TRP A CD1 1 
ATOM   12394 C CD2 . TRP B 2 410  ? 182.152 205.591 155.780 1.00 29.78  ? 410  TRP A CD2 1 
ATOM   12395 N NE1 . TRP B 2 410  ? 182.035 206.936 157.561 1.00 29.78  ? 410  TRP A NE1 1 
ATOM   12396 C CE2 . TRP B 2 410  ? 181.368 206.559 156.424 1.00 29.78  ? 410  TRP A CE2 1 
ATOM   12397 C CE3 . TRP B 2 410  ? 181.690 205.036 154.585 1.00 29.78  ? 410  TRP A CE3 1 
ATOM   12398 C CZ2 . TRP B 2 410  ? 180.147 206.988 155.920 1.00 29.78  ? 410  TRP A CZ2 1 
ATOM   12399 C CZ3 . TRP B 2 410  ? 180.479 205.461 154.087 1.00 29.78  ? 410  TRP A CZ3 1 
ATOM   12400 C CH2 . TRP B 2 410  ? 179.721 206.427 154.751 1.00 29.78  ? 410  TRP A CH2 1 
ATOM   12401 N N   . PHE B 2 411  ? 183.232 201.551 156.286 1.00 30.38  ? 411  PHE A N   1 
ATOM   12402 C CA  . PHE B 2 411  ? 181.998 200.790 156.083 1.00 30.38  ? 411  PHE A CA  1 
ATOM   12403 C C   . PHE B 2 411  ? 181.595 199.948 157.291 1.00 30.38  ? 411  PHE A C   1 
ATOM   12404 O O   . PHE B 2 411  ? 180.425 200.036 157.706 1.00 30.38  ? 411  PHE A O   1 
ATOM   12405 C CB  . PHE B 2 411  ? 182.124 199.946 154.813 1.00 30.38  ? 411  PHE A CB  1 
ATOM   12406 C CG  . PHE B 2 411  ? 181.875 200.720 153.556 1.00 30.38  ? 411  PHE A CG  1 
ATOM   12407 C CD1 . PHE B 2 411  ? 180.808 201.593 153.474 1.00 30.38  ? 411  PHE A CD1 1 
ATOM   12408 C CD2 . PHE B 2 411  ? 182.712 200.589 152.466 1.00 30.38  ? 411  PHE A CD2 1 
ATOM   12409 C CE1 . PHE B 2 411  ? 180.571 202.310 152.323 1.00 30.38  ? 411  PHE A CE1 1 
ATOM   12410 C CE2 . PHE B 2 411  ? 182.480 201.305 151.311 1.00 30.38  ? 411  PHE A CE2 1 
ATOM   12411 C CZ  . PHE B 2 411  ? 181.409 202.166 151.241 1.00 30.38  ? 411  PHE A CZ  1 
ATOM   12412 N N   . PRO B 2 412  ? 182.463 199.120 157.889 1.00 31.44  ? 412  PRO A N   1 
ATOM   12413 C CA  . PRO B 2 412  ? 182.042 198.416 159.112 1.00 31.44  ? 412  PRO A CA  1 
ATOM   12414 C C   . PRO B 2 412  ? 181.667 199.355 160.246 1.00 31.44  ? 412  PRO A C   1 
ATOM   12415 O O   . PRO B 2 412  ? 180.719 199.082 160.993 1.00 31.44  ? 412  PRO A O   1 
ATOM   12416 C CB  . PRO B 2 412  ? 183.267 197.561 159.464 1.00 31.44  ? 412  PRO A CB  1 
ATOM   12417 C CG  . PRO B 2 412  ? 184.022 197.438 158.196 1.00 31.44  ? 412  PRO A CG  1 
ATOM   12418 C CD  . PRO B 2 412  ? 183.827 198.737 157.494 1.00 31.44  ? 412  PRO A CD  1 
ATOM   12419 N N   . ASP B 2 413  ? 182.388 200.469 160.390 1.00 33.14  ? 413  ASP A N   1 
ATOM   12420 C CA  . ASP B 2 413  ? 182.033 201.436 161.421 1.00 33.14  ? 413  ASP A CA  1 
ATOM   12421 C C   . ASP B 2 413  ? 180.660 202.034 161.156 1.00 33.14  ? 413  ASP A C   1 
ATOM   12422 O O   . ASP B 2 413  ? 179.865 202.221 162.085 1.00 33.14  ? 413  ASP A O   1 
ATOM   12423 C CB  . ASP B 2 413  ? 183.093 202.529 161.505 1.00 33.14  ? 413  ASP A CB  1 
ATOM   12424 C CG  . ASP B 2 413  ? 184.125 202.255 162.577 1.00 33.14  ? 413  ASP A CG  1 
ATOM   12425 O OD1 . ASP B 2 413  ? 184.320 201.071 162.918 1.00 33.14  ? 413  ASP A OD1 1 
ATOM   12426 O OD2 . ASP B 2 413  ? 184.736 203.220 163.081 1.00 33.14  ? 413  ASP A OD2 1 
ATOM   12427 N N   . MET B 2 414  ? 180.359 202.334 159.892 1.00 33.40  ? 414  MET A N   1 
ATOM   12428 C CA  . MET B 2 414  ? 179.046 202.876 159.567 1.00 33.40  ? 414  MET A CA  1 
ATOM   12429 C C   . MET B 2 414  ? 177.945 201.859 159.827 1.00 33.40  ? 414  MET A C   1 
ATOM   12430 O O   . MET B 2 414  ? 176.859 202.223 160.288 1.00 33.40  ? 414  MET A O   1 
ATOM   12431 C CB  . MET B 2 414  ? 179.011 203.343 158.117 1.00 33.40  ? 414  MET A CB  1 
ATOM   12432 C CG  . MET B 2 414  ? 177.970 204.416 157.859 1.00 33.40  ? 414  MET A CG  1 
ATOM   12433 S SD  . MET B 2 414  ? 178.364 205.968 158.684 1.00 33.40  ? 414  MET A SD  1 
ATOM   12434 C CE  . MET B 2 414  ? 176.799 206.827 158.549 1.00 33.40  ? 414  MET A CE  1 
ATOM   12435 N N   . ILE B 2 415  ? 178.201 200.580 159.543 1.00 35.16  ? 415  ILE A N   1 
ATOM   12436 C CA  . ILE B 2 415  ? 177.168 199.578 159.788 1.00 35.16  ? 415  ILE A CA  1 
ATOM   12437 C C   . ILE B 2 415  ? 176.939 199.408 161.288 1.00 35.16  ? 415  ILE A C   1 
ATOM   12438 O O   . ILE B 2 415  ? 175.794 199.268 161.747 1.00 35.16  ? 415  ILE A O   1 
ATOM   12439 C CB  . ILE B 2 415  ? 177.523 198.250 159.085 1.00 35.16  ? 415  ILE A CB  1 
ATOM   12440 C CG1 . ILE B 2 415  ? 176.250 197.480 158.793 1.00 35.16  ? 415  ILE A CG1 1 
ATOM   12441 C CG2 . ILE B 2 415  ? 178.431 197.375 159.921 1.00 35.16  ? 415  ILE A CG2 1 
ATOM   12442 C CD1 . ILE B 2 415  ? 175.354 198.235 157.885 1.00 35.16  ? 415  ILE A CD1 1 
ATOM   12443 N N   . ARG B 2 416  ? 178.015 199.466 162.078 1.00 37.67  ? 416  ARG A N   1 
ATOM   12444 C CA  . ARG B 2 416  ? 177.864 199.398 163.525 1.00 37.67  ? 416  ARG A CA  1 
ATOM   12445 C C   . ARG B 2 416  ? 177.102 200.606 164.050 1.00 37.67  ? 416  ARG A C   1 
ATOM   12446 O O   . ARG B 2 416  ? 176.268 200.480 164.953 1.00 37.67  ? 416  ARG A O   1 
ATOM   12447 C CB  . ARG B 2 416  ? 179.230 199.288 164.199 1.00 37.67  ? 416  ARG A CB  1 
ATOM   12448 C CG  . ARG B 2 416  ? 179.615 197.868 164.571 1.00 37.67  ? 416  ARG A CG  1 
ATOM   12449 C CD  . ARG B 2 416  ? 178.823 197.382 165.770 1.00 37.67  ? 416  ARG A CD  1 
ATOM   12450 N NE  . ARG B 2 416  ? 179.017 198.235 166.936 1.00 37.67  ? 416  ARG A NE  1 
ATOM   12451 C CZ  . ARG B 2 416  ? 178.204 198.268 167.982 1.00 37.67  ? 416  ARG A CZ  1 
ATOM   12452 N NH1 . ARG B 2 416  ? 177.124 197.509 168.044 1.00 37.67  ? 416  ARG A NH1 1 
ATOM   12453 N NH2 . ARG B 2 416  ? 178.484 199.085 168.995 1.00 37.67  ? 416  ARG A NH2 1 
ATOM   12454 N N   . TYR B 2 417  ? 177.369 201.790 163.494 1.00 35.99  ? 417  TYR A N   1 
ATOM   12455 C CA  . TYR B 2 417  ? 176.642 202.980 163.921 1.00 35.99  ? 417  TYR A CA  1 
ATOM   12456 C C   . TYR B 2 417  ? 175.169 202.887 163.553 1.00 35.99  ? 417  TYR A C   1 
ATOM   12457 O O   . TYR B 2 417  ? 174.306 203.343 164.308 1.00 35.99  ? 417  TYR A O   1 
ATOM   12458 C CB  . TYR B 2 417  ? 177.261 204.236 163.314 1.00 35.99  ? 417  TYR A CB  1 
ATOM   12459 C CG  . TYR B 2 417  ? 176.318 205.419 163.321 1.00 35.99  ? 417  TYR A CG  1 
ATOM   12460 C CD1 . TYR B 2 417  ? 176.042 206.099 164.495 1.00 35.99  ? 417  TYR A CD1 1 
ATOM   12461 C CD2 . TYR B 2 417  ? 175.701 205.846 162.157 1.00 35.99  ? 417  TYR A CD2 1 
ATOM   12462 C CE1 . TYR B 2 417  ? 175.180 207.173 164.509 1.00 35.99  ? 417  TYR A CE1 1 
ATOM   12463 C CE2 . TYR B 2 417  ? 174.838 206.922 162.163 1.00 35.99  ? 417  TYR A CE2 1 
ATOM   12464 C CZ  . TYR B 2 417  ? 174.582 207.580 163.342 1.00 35.99  ? 417  TYR A CZ  1 
ATOM   12465 O OH  . TYR B 2 417  ? 173.720 208.653 163.352 1.00 35.99  ? 417  TYR A OH  1 
ATOM   12466 N N   . PHE B 2 418  ? 174.861 202.321 162.385 1.00 37.82  ? 418  PHE A N   1 
ATOM   12467 C CA  . PHE B 2 418  ? 173.462 202.141 162.008 1.00 37.82  ? 418  PHE A CA  1 
ATOM   12468 C C   . PHE B 2 418  ? 172.749 201.216 162.986 1.00 37.82  ? 418  PHE A C   1 
ATOM   12469 O O   . PHE B 2 418  ? 171.627 201.508 163.427 1.00 37.82  ? 418  PHE A O   1 
ATOM   12470 C CB  . PHE B 2 418  ? 173.370 201.588 160.588 1.00 37.82  ? 418  PHE A CB  1 
ATOM   12471 C CG  . PHE B 2 418  ? 173.490 202.637 159.523 1.00 37.82  ? 418  PHE A CG  1 
ATOM   12472 C CD1 . PHE B 2 418  ? 173.565 203.977 159.856 1.00 37.82  ? 418  PHE A CD1 1 
ATOM   12473 C CD2 . PHE B 2 418  ? 173.537 202.280 158.186 1.00 37.82  ? 418  PHE A CD2 1 
ATOM   12474 C CE1 . PHE B 2 418  ? 173.681 204.942 158.878 1.00 37.82  ? 418  PHE A CE1 1 
ATOM   12475 C CE2 . PHE B 2 418  ? 173.651 203.239 157.205 1.00 37.82  ? 418  PHE A CE2 1 
ATOM   12476 C CZ  . PHE B 2 418  ? 173.725 204.571 157.551 1.00 37.82  ? 418  PHE A CZ  1 
ATOM   12477 N N   . GLN B 2 419  ? 173.392 200.105 163.348 1.00 41.50  ? 419  GLN A N   1 
ATOM   12478 C CA  . GLN B 2 419  ? 172.798 199.200 164.328 1.00 41.50  ? 419  GLN A CA  1 
ATOM   12479 C C   . GLN B 2 419  ? 172.624 199.891 165.676 1.00 41.50  ? 419  GLN A C   1 
ATOM   12480 O O   . GLN B 2 419  ? 171.598 199.726 166.349 1.00 41.50  ? 419  GLN A O   1 
ATOM   12481 C CB  . GLN B 2 419  ? 173.658 197.945 164.470 1.00 41.50  ? 419  GLN A CB  1 
ATOM   12482 C CG  . GLN B 2 419  ? 173.740 197.114 163.204 1.00 41.50  ? 419  GLN A CG  1 
ATOM   12483 C CD  . GLN B 2 419  ? 174.101 195.671 163.479 1.00 41.50  ? 419  GLN A CD  1 
ATOM   12484 O OE1 . GLN B 2 419  ? 175.098 195.384 164.141 1.00 41.50  ? 419  GLN A OE1 1 
ATOM   12485 N NE2 . GLN B 2 419  ? 173.289 194.753 162.968 1.00 41.50  ? 419  GLN A NE2 1 
ATOM   12486 N N   . ASP B 2 420  ? 173.625 200.674 166.085 1.00 41.13  ? 420  ASP A N   1 
ATOM   12487 C CA  . ASP B 2 420  ? 173.557 201.385 167.356 1.00 41.13  ? 420  ASP A CA  1 
ATOM   12488 C C   . ASP B 2 420  ? 172.403 202.381 167.357 1.00 41.13  ? 420  ASP A C   1 
ATOM   12489 O O   . ASP B 2 420  ? 171.703 202.534 168.362 1.00 41.13  ? 420  ASP A O   1 
ATOM   12490 C CB  . ASP B 2 420  ? 174.908 202.065 167.623 1.00 41.13  ? 420  ASP A CB  1 
ATOM   12491 C CG  . ASP B 2 420  ? 174.879 203.072 168.775 1.00 41.13  ? 420  ASP A CG  1 
ATOM   12492 O OD1 . ASP B 2 420  ? 174.020 203.978 168.820 1.00 41.13  ? 420  ASP A OD1 1 
ATOM   12493 O OD2 . ASP B 2 420  ? 175.749 202.951 169.663 1.00 41.13  ? 420  ASP A OD2 1 
ATOM   12494 N N   . GLU B 2 421  ? 172.210 203.091 166.243 1.00 42.42  ? 421  GLU A N   1 
ATOM   12495 C CA  . GLU B 2 421  ? 171.100 204.034 166.147 1.00 42.42  ? 421  GLU A CA  1 
ATOM   12496 C C   . GLU B 2 421  ? 169.758 203.320 166.227 1.00 42.42  ? 421  GLU A C   1 
ATOM   12497 O O   . GLU B 2 421  ? 168.836 203.784 166.910 1.00 42.42  ? 421  GLU A O   1 
ATOM   12498 C CB  . GLU B 2 421  ? 171.205 204.834 164.847 1.00 42.42  ? 421  GLU A CB  1 
ATOM   12499 C CG  . GLU B 2 421  ? 169.962 205.647 164.503 1.00 42.42  ? 421  GLU A CG  1 
ATOM   12500 C CD  . GLU B 2 421  ? 169.734 206.825 165.432 1.00 42.42  ? 421  GLU A CD  1 
ATOM   12501 O OE1 . GLU B 2 421  ? 170.587 207.077 166.309 1.00 42.42  ? 421  GLU A OE1 1 
ATOM   12502 O OE2 . GLU B 2 421  ? 168.696 207.502 165.284 1.00 42.42  ? 421  GLU A OE2 1 
ATOM   12503 N N   . GLU B 2 422  ? 169.630 202.185 165.534 1.00 44.74  ? 422  GLU A N   1 
ATOM   12504 C CA  . GLU B 2 422  ? 168.391 201.421 165.613 1.00 44.74  ? 422  GLU A CA  1 
ATOM   12505 C C   . GLU B 2 422  ? 168.120 200.979 167.047 1.00 44.74  ? 422  GLU A C   1 
ATOM   12506 O O   . GLU B 2 422  ? 166.975 200.993 167.511 1.00 44.74  ? 422  GLU A O   1 
ATOM   12507 C CB  . GLU B 2 422  ? 168.449 200.219 164.674 1.00 44.74  ? 422  GLU A CB  1 
ATOM   12508 C CG  . GLU B 2 422  ? 167.165 199.404 164.626 1.00 44.74  ? 422  GLU A CG  1 
ATOM   12509 C CD  . GLU B 2 422  ? 165.930 200.268 164.467 1.00 44.74  ? 422  GLU A CD  1 
ATOM   12510 O OE1 . GLU B 2 422  ? 165.862 201.040 163.486 1.00 44.74  ? 422  GLU A OE1 1 
ATOM   12511 O OE2 . GLU B 2 422  ? 165.020 200.169 165.317 1.00 44.74  ? 422  GLU A OE2 1 
ATOM   12512 N N   . TYR B 2 423  ? 169.171 200.571 167.764 1.00 45.99  ? 423  TYR A N   1 
ATOM   12513 C CA  . TYR B 2 423  ? 169.041 200.256 169.184 1.00 45.99  ? 423  TYR A CA  1 
ATOM   12514 C C   . TYR B 2 423  ? 168.559 201.459 169.986 1.00 45.99  ? 423  TYR A C   1 
ATOM   12515 O O   . TYR B 2 423  ? 167.568 201.383 170.721 1.00 45.99  ? 423  TYR A O   1 
ATOM   12516 C CB  . TYR B 2 423  ? 170.382 199.761 169.726 1.00 45.99  ? 423  TYR A CB  1 
ATOM   12517 C CG  . TYR B 2 423  ? 170.280 199.006 171.025 1.00 45.99  ? 423  TYR A CG  1 
ATOM   12518 C CD1 . TYR B 2 423  ? 169.452 197.903 171.148 1.00 45.99  ? 423  TYR A CD1 1 
ATOM   12519 C CD2 . TYR B 2 423  ? 171.016 199.402 172.134 1.00 45.99  ? 423  TYR A CD2 1 
ATOM   12520 C CE1 . TYR B 2 423  ? 169.359 197.214 172.341 1.00 45.99  ? 423  TYR A CE1 1 
ATOM   12521 C CE2 . TYR B 2 423  ? 170.931 198.720 173.327 1.00 45.99  ? 423  TYR A CE2 1 
ATOM   12522 C CZ  . TYR B 2 423  ? 170.101 197.628 173.425 1.00 45.99  ? 423  TYR A CZ  1 
ATOM   12523 O OH  . TYR B 2 423  ? 170.012 196.942 174.613 1.00 45.99  ? 423  TYR A OH  1 
ATOM   12524 N N   . LYS B 2 424  ? 169.260 202.586 169.853 1.00 43.39  ? 424  LYS A N   1 
ATOM   12525 C CA  . LYS B 2 424  ? 168.977 203.766 170.661 1.00 43.39  ? 424  LYS A CA  1 
ATOM   12526 C C   . LYS B 2 424  ? 167.587 204.323 170.401 1.00 43.39  ? 424  LYS A C   1 
ATOM   12527 O O   . LYS B 2 424  ? 167.020 204.987 171.275 1.00 43.39  ? 424  LYS A O   1 
ATOM   12528 C CB  . LYS B 2 424  ? 170.043 204.834 170.398 1.00 43.39  ? 424  LYS A CB  1 
ATOM   12529 C CG  . LYS B 2 424  ? 169.842 206.139 171.149 1.00 43.39  ? 424  LYS A CG  1 
ATOM   12530 C CD  . LYS B 2 424  ? 170.992 207.103 170.906 1.00 43.39  ? 424  LYS A CD  1 
ATOM   12531 C CE  . LYS B 2 424  ? 172.338 206.421 171.092 1.00 43.39  ? 424  LYS A CE  1 
ATOM   12532 N NZ  . LYS B 2 424  ? 173.466 207.388 171.000 1.00 43.39  ? 424  LYS A NZ  1 
ATOM   12533 N N   . SER B 2 425  ? 167.015 204.064 169.223 1.00 44.33  ? 425  SER A N   1 
ATOM   12534 C CA  . SER B 2 425  ? 165.658 204.529 168.961 1.00 44.33  ? 425  SER A CA  1 
ATOM   12535 C C   . SER B 2 425  ? 164.664 203.911 169.936 1.00 44.33  ? 425  SER A C   1 
ATOM   12536 O O   . SER B 2 425  ? 163.747 204.592 170.412 1.00 44.33  ? 425  SER A O   1 
ATOM   12537 C CB  . SER B 2 425  ? 165.261 204.211 167.520 1.00 44.33  ? 425  SER A CB  1 
ATOM   12538 O OG  . SER B 2 425  ? 163.908 204.555 167.285 1.00 44.33  ? 425  SER A OG  1 
ATOM   12539 N N   . LYS B 2 426  ? 164.825 202.625 170.248 1.00 45.20  ? 426  LYS A N   1 
ATOM   12540 C CA  . LYS B 2 426  ? 163.900 201.931 171.136 1.00 45.20  ? 426  LYS A CA  1 
ATOM   12541 C C   . LYS B 2 426  ? 164.313 202.064 172.598 1.00 45.20  ? 426  LYS A C   1 
ATOM   12542 O O   . LYS B 2 426  ? 164.476 201.055 173.293 1.00 45.20  ? 426  LYS A O   1 
ATOM   12543 C CB  . LYS B 2 426  ? 163.808 200.453 170.760 1.00 45.20  ? 426  LYS A CB  1 
ATOM   12544 C CG  . LYS B 2 426  ? 163.326 200.201 169.344 1.00 45.20  ? 426  LYS A CG  1 
ATOM   12545 C CD  . LYS B 2 426  ? 163.479 198.739 168.972 1.00 45.20  ? 426  LYS A CD  1 
ATOM   12546 C CE  . LYS B 2 426  ? 164.902 198.261 169.196 1.00 45.20  ? 426  LYS A CE  1 
ATOM   12547 N NZ  . LYS B 2 426  ? 165.889 199.061 168.425 1.00 45.20  ? 426  LYS A NZ  1 
ATOM   12548 N N   . MET B 2 427  ? 164.480 203.292 173.077 1.00 46.54  ? 427  MET A N   1 
ATOM   12549 C CA  . MET B 2 427  ? 164.821 203.535 174.474 1.00 46.54  ? 427  MET A CA  1 
ATOM   12550 C C   . MET B 2 427  ? 163.546 203.846 175.242 1.00 46.54  ? 427  MET A C   1 
ATOM   12551 O O   . MET B 2 427  ? 162.772 204.721 174.840 1.00 46.54  ? 427  MET A O   1 
ATOM   12552 C CB  . MET B 2 427  ? 165.824 204.680 174.603 1.00 46.54  ? 427  MET A CB  1 
ATOM   12553 C CG  . MET B 2 427  ? 166.430 204.813 175.988 1.00 46.54  ? 427  MET A CG  1 
ATOM   12554 S SD  . MET B 2 427  ? 167.490 206.260 176.151 1.00 46.54  ? 427  MET A SD  1 
ATOM   12555 C CE  . MET B 2 427  ? 166.361 207.421 176.915 1.00 46.54  ? 427  MET A CE  1 
ATOM   12556 N N   . LYS B 2 428  ? 163.325 203.133 176.340 1.00 46.84  ? 428  LYS A N   1 
ATOM   12557 C CA  . LYS B 2 428  ? 162.117 203.283 177.137 1.00 46.84  ? 428  LYS A CA  1 
ATOM   12558 C C   . LYS B 2 428  ? 162.412 204.167 178.341 1.00 46.84  ? 428  LYS A C   1 
ATOM   12559 O O   . LYS B 2 428  ? 163.235 203.815 179.195 1.00 46.84  ? 428  LYS A O   1 
ATOM   12560 C CB  . LYS B 2 428  ? 161.584 201.926 177.584 1.00 46.84  ? 428  LYS A CB  1 
ATOM   12561 C CG  . LYS B 2 428  ? 160.524 201.339 176.666 1.00 46.84  ? 428  LYS A CG  1 
ATOM   12562 C CD  . LYS B 2 428  ? 160.313 199.856 176.936 1.00 46.84  ? 428  LYS A CD  1 
ATOM   12563 C CE  . LYS B 2 428  ? 161.455 199.023 176.379 1.00 46.84  ? 428  LYS A CE  1 
ATOM   12564 N NZ  . LYS B 2 428  ? 161.682 199.296 174.936 1.00 46.84  ? 428  LYS A NZ  1 
ATOM   12565 N N   . VAL B 2 429  ? 161.723 205.302 178.413 1.00 44.76  ? 429  VAL A N   1 
ATOM   12566 C CA  . VAL B 2 429  ? 161.852 206.247 179.514 1.00 44.76  ? 429  VAL A CA  1 
ATOM   12567 C C   . VAL B 2 429  ? 160.770 205.938 180.535 1.00 44.76  ? 429  VAL A C   1 
ATOM   12568 O O   . VAL B 2 429  ? 159.595 205.781 180.180 1.00 44.76  ? 429  VAL A O   1 
ATOM   12569 C CB  . VAL B 2 429  ? 161.743 207.699 179.016 1.00 44.76  ? 429  VAL A CB  1 
ATOM   12570 C CG1 . VAL B 2 429  ? 163.066 208.158 178.438 1.00 44.76  ? 429  VAL A CG1 1 
ATOM   12571 C CG2 . VAL B 2 429  ? 160.640 207.818 177.977 1.00 44.76  ? 429  VAL A CG2 1 
ATOM   12572 N N   . PHE B 2 430  ? 161.160 205.848 181.801 1.00 41.81  ? 430  PHE A N   1 
ATOM   12573 C CA  . PHE B 2 430  ? 160.254 205.507 182.885 1.00 41.81  ? 430  PHE A CA  1 
ATOM   12574 C C   . PHE B 2 430  ? 160.269 206.631 183.907 1.00 41.81  ? 430  PHE A C   1 
ATOM   12575 O O   . PHE B 2 430  ? 161.341 207.065 184.342 1.00 41.81  ? 430  PHE A O   1 
ATOM   12576 C CB  . PHE B 2 430  ? 160.661 204.183 183.535 1.00 41.81  ? 430  PHE A CB  1 
ATOM   12577 C CG  . PHE B 2 430  ? 159.922 202.993 182.998 1.00 41.81  ? 430  PHE A CG  1 
ATOM   12578 C CD1 . PHE B 2 430  ? 159.038 203.131 181.943 1.00 41.81  ? 430  PHE A CD1 1 
ATOM   12579 C CD2 . PHE B 2 430  ? 160.107 201.742 183.553 1.00 41.81  ? 430  PHE A CD2 1 
ATOM   12580 C CE1 . PHE B 2 430  ? 158.354 202.038 181.451 1.00 41.81  ? 430  PHE A CE1 1 
ATOM   12581 C CE2 . PHE B 2 430  ? 159.425 200.645 183.067 1.00 41.81  ? 430  PHE A CE2 1 
ATOM   12582 C CZ  . PHE B 2 430  ? 158.547 200.793 182.015 1.00 41.81  ? 430  PHE A CZ  1 
ATOM   12583 N N   . PHE B 2 431  ? 159.082 207.091 184.296 1.00 40.67  ? 431  PHE A N   1 
ATOM   12584 C CA  . PHE B 2 431  ? 158.931 208.223 185.197 1.00 40.67  ? 431  PHE A CA  1 
ATOM   12585 C C   . PHE B 2 431  ? 157.890 207.894 186.256 1.00 40.67  ? 431  PHE A C   1 
ATOM   12586 O O   . PHE B 2 431  ? 156.788 207.442 185.927 1.00 40.67  ? 431  PHE A O   1 
ATOM   12587 C CB  . PHE B 2 431  ? 158.520 209.480 184.425 1.00 40.67  ? 431  PHE A CB  1 
ATOM   12588 C CG  . PHE B 2 431  ? 158.843 210.760 185.132 1.00 40.67  ? 431  PHE A CG  1 
ATOM   12589 C CD1 . PHE B 2 431  ? 157.985 211.272 186.087 1.00 40.67  ? 431  PHE A CD1 1 
ATOM   12590 C CD2 . PHE B 2 431  ? 159.999 211.458 184.830 1.00 40.67  ? 431  PHE A CD2 1 
ATOM   12591 C CE1 . PHE B 2 431  ? 158.276 212.450 186.739 1.00 40.67  ? 431  PHE A CE1 1 
ATOM   12592 C CE2 . PHE B 2 431  ? 160.295 212.640 185.477 1.00 40.67  ? 431  PHE A CE2 1 
ATOM   12593 C CZ  . PHE B 2 431  ? 159.432 213.136 186.433 1.00 40.67  ? 431  PHE A CZ  1 
ATOM   12594 N N   . GLY B 2 432  ? 158.241 208.121 187.519 1.00 41.62  ? 432  GLY A N   1 
ATOM   12595 C CA  . GLY B 2 432  ? 157.284 207.959 188.605 1.00 41.62  ? 432  GLY A CA  1 
ATOM   12596 C C   . GLY B 2 432  ? 156.752 206.554 188.780 1.00 41.62  ? 432  GLY A C   1 
ATOM   12597 O O   . GLY B 2 432  ? 155.537 206.340 188.695 1.00 41.62  ? 432  GLY A O   1 
ATOM   12598 N N   . GLU B 2 433  ? 157.636 205.588 189.017 1.00 41.41  ? 433  GLU A N   1 
ATOM   12599 C CA  . GLU B 2 433  ? 157.211 204.211 189.226 1.00 41.41  ? 433  GLU A CA  1 
ATOM   12600 C C   . GLU B 2 433  ? 157.097 203.892 190.708 1.00 41.41  ? 433  GLU A C   1 
ATOM   12601 O O   . GLU B 2 433  ? 157.747 204.514 191.550 1.00 41.41  ? 433  GLU A O   1 
ATOM   12602 C CB  . GLU B 2 433  ? 158.176 203.227 188.558 1.00 41.41  ? 433  GLU A CB  1 
ATOM   12603 C CG  . GLU B 2 433  ? 158.248 203.319 187.037 1.00 41.41  ? 433  GLU A CG  1 
ATOM   12604 C CD  . GLU B 2 433  ? 158.627 204.688 186.523 1.00 41.41  ? 433  GLU A CD  1 
ATOM   12605 O OE1 . GLU B 2 433  ? 158.299 204.983 185.361 1.00 41.41  ? 433  GLU A OE1 1 
ATOM   12606 O OE2 . GLU B 2 433  ? 159.270 205.456 187.267 1.00 41.41  ? 433  GLU A OE2 1 
ATOM   12607 N N   . HIS B 2 434  ? 156.265 202.899 191.005 1.00 43.19  ? 434  HIS A N   1 
ATOM   12608 C CA  . HIS B 2 434  ? 156.039 202.456 192.400 1.00 43.19  ? 434  HIS A CA  1 
ATOM   12609 C C   . HIS B 2 434  ? 155.926 200.929 192.324 1.00 43.19  ? 434  HIS A C   1 
ATOM   12610 O O   . HIS B 2 434  ? 154.792 200.416 192.245 1.00 43.19  ? 434  HIS A O   1 
ATOM   12611 C CB  . HIS B 2 434  ? 154.775 203.150 192.905 1.00 43.19  ? 434  HIS A CB  1 
ATOM   12612 C CG  . HIS B 2 434  ? 154.952 204.120 194.021 1.00 43.19  ? 434  HIS A CG  1 
ATOM   12613 N ND1 . HIS B 2 434  ? 156.057 204.168 194.840 1.00 43.19  ? 434  HIS A ND1 1 
ATOM   12614 C CD2 . HIS B 2 434  ? 154.123 205.076 194.456 1.00 43.19  ? 434  HIS A CD2 1 
ATOM   12615 C CE1 . HIS B 2 434  ? 155.888 205.132 195.732 1.00 43.19  ? 434  HIS A CE1 1 
ATOM   12616 N NE2 . HIS B 2 434  ? 154.722 205.696 195.518 1.00 43.19  ? 434  HIS A NE2 1 
ATOM   12617 N N   . VAL B 2 435  ? 157.039 200.203 192.360 1.00 44.05  ? 435  VAL A N   1 
ATOM   12618 C CA  . VAL B 2 435  ? 157.091 198.761 192.151 1.00 44.05  ? 435  VAL A CA  1 
ATOM   12619 C C   . VAL B 2 435  ? 157.148 198.109 193.524 1.00 44.05  ? 435  VAL A C   1 
ATOM   12620 O O   . VAL B 2 435  ? 158.154 198.223 194.236 1.00 44.05  ? 435  VAL A O   1 
ATOM   12621 C CB  . VAL B 2 435  ? 158.290 198.361 191.285 1.00 44.05  ? 435  VAL A CB  1 
ATOM   12622 C CG1 . VAL B 2 435  ? 158.386 196.856 191.176 1.00 44.05  ? 435  VAL A CG1 1 
ATOM   12623 C CG2 . VAL B 2 435  ? 158.186 198.996 189.911 1.00 44.05  ? 435  VAL A CG2 1 
ATOM   12624 N N   . TYR B 2 436  ? 156.074 197.422 193.900 1.00 47.31  ? 436  TYR A N   1 
ATOM   12625 C CA  . TYR B 2 436  ? 155.897 196.897 195.250 1.00 47.31  ? 436  TYR A CA  1 
ATOM   12626 C C   . TYR B 2 436  ? 155.920 195.376 195.213 1.00 47.31  ? 436  TYR A C   1 
ATOM   12627 O O   . TYR B 2 436  ? 155.132 194.759 194.489 1.00 47.31  ? 436  TYR A O   1 
ATOM   12628 C CB  . TYR B 2 436  ? 154.585 197.388 195.862 1.00 47.31  ? 436  TYR A CB  1 
ATOM   12629 C CG  . TYR B 2 436  ? 154.554 198.851 196.254 1.00 47.31  ? 436  TYR A CG  1 
ATOM   12630 C CD1 . TYR B 2 436  ? 155.115 199.827 195.442 1.00 47.31  ? 436  TYR A CD1 1 
ATOM   12631 C CD2 . TYR B 2 436  ? 153.946 199.256 197.434 1.00 47.31  ? 436  TYR A CD2 1 
ATOM   12632 C CE1 . TYR B 2 436  ? 155.083 201.158 195.800 1.00 47.31  ? 436  TYR A CE1 1 
ATOM   12633 C CE2 . TYR B 2 436  ? 153.907 200.589 197.798 1.00 47.31  ? 436  TYR A CE2 1 
ATOM   12634 C CZ  . TYR B 2 436  ? 154.478 201.535 196.977 1.00 47.31  ? 436  TYR A CZ  1 
ATOM   12635 O OH  . TYR B 2 436  ? 154.444 202.863 197.332 1.00 47.31  ? 436  TYR A OH  1 
ATOM   12636 N N   . GLY B 2 437  ? 156.815 194.782 195.996 1.00 49.86  ? 437  GLY A N   1 
ATOM   12637 C CA  . GLY B 2 437  ? 156.817 193.341 196.204 1.00 49.86  ? 437  GLY A CA  1 
ATOM   12638 C C   . GLY B 2 437  ? 156.940 192.518 194.941 1.00 49.86  ? 437  GLY A C   1 
ATOM   12639 O O   . GLY B 2 437  ? 156.288 191.474 194.820 1.00 49.86  ? 437  GLY A O   1 
ATOM   12640 N N   . ALA B 2 438  ? 157.767 192.958 194.000 1.00 48.04  ? 438  ALA A N   1 
ATOM   12641 C CA  . ALA B 2 438  ? 157.908 192.296 192.713 1.00 48.04  ? 438  ALA A CA  1 
ATOM   12642 C C   . ALA B 2 438  ? 159.223 191.531 192.668 1.00 48.04  ? 438  ALA A C   1 
ATOM   12643 O O   . ALA B 2 438  ? 160.278 192.080 192.998 1.00 48.04  ? 438  ALA A O   1 
ATOM   12644 C CB  . ALA B 2 438  ? 157.848 193.306 191.566 1.00 48.04  ? 438  ALA A CB  1 
ATOM   12645 N N   . THR B 2 439  ? 159.149 190.268 192.261 1.00 50.15  ? 439  THR A N   1 
ATOM   12646 C CA  . THR B 2 439  ? 160.329 189.445 192.038 1.00 50.15  ? 439  THR A CA  1 
ATOM   12647 C C   . THR B 2 439  ? 160.639 189.458 190.550 1.00 50.15  ? 439  THR A C   1 
ATOM   12648 O O   . THR B 2 439  ? 159.782 189.108 189.733 1.00 50.15  ? 439  THR A O   1 
ATOM   12649 C CB  . THR B 2 439  ? 160.108 188.015 192.526 1.00 50.15  ? 439  THR A CB  1 
ATOM   12650 O OG1 . THR B 2 439  ? 159.945 188.011 193.950 1.00 50.15  ? 439  THR A OG1 1 
ATOM   12651 C CG2 . THR B 2 439  ? 161.291 187.137 192.152 1.00 50.15  ? 439  THR A CG2 1 
ATOM   12652 N N   . ILE B 2 440  ? 161.854 189.862 190.198 1.00 51.04  ? 440  ILE A N   1 
ATOM   12653 C CA  . ILE B 2 440  ? 162.263 189.988 188.807 1.00 51.04  ? 440  ILE A CA  1 
ATOM   12654 C C   . ILE B 2 440  ? 163.135 188.796 188.454 1.00 51.04  ? 440  ILE A C   1 
ATOM   12655 O O   . ILE B 2 440  ? 164.114 188.497 189.150 1.00 51.04  ? 440  ILE A O   1 
ATOM   12656 C CB  . ILE B 2 440  ? 162.992 191.315 188.545 1.00 51.04  ? 440  ILE A CB  1 
ATOM   12657 C CG1 . ILE B 2 440  ? 162.034 192.486 188.752 1.00 51.04  ? 440  ILE A CG1 1 
ATOM   12658 C CG2 . ILE B 2 440  ? 163.488 191.356 187.123 1.00 51.04  ? 440  ILE A CG2 1 
ATOM   12659 C CD1 . ILE B 2 440  ? 160.828 192.451 187.847 1.00 51.04  ? 440  ILE A CD1 1 
ATOM   12660 N N   . ASN B 2 441  ? 162.775 188.117 187.367 1.00 58.26  ? 441  ASN A N   1 
ATOM   12661 C CA  . ASN B 2 441  ? 163.391 186.861 186.955 1.00 58.26  ? 441  ASN A CA  1 
ATOM   12662 C C   . ASN B 2 441  ? 163.927 186.891 185.536 1.00 58.26  ? 441  ASN A C   1 
ATOM   12663 O O   . ASN B 2 441  ? 164.811 186.091 185.214 1.00 58.26  ? 441  ASN A O   1 
ATOM   12664 C CB  . ASN B 2 441  ? 162.357 185.732 187.076 1.00 58.26  ? 441  ASN A CB  1 
ATOM   12665 C CG  . ASN B 2 441  ? 161.089 186.040 186.296 1.00 58.26  ? 441  ASN A CG  1 
ATOM   12666 O OD1 . ASN B 2 441  ? 160.929 187.175 185.846 1.00 58.26  ? 441  ASN A OD1 1 
ATOM   12667 N ND2 . ASN B 2 441  ? 160.176 185.077 186.139 1.00 58.26  ? 441  ASN A ND2 1 
ATOM   12668 N N   . PHE B 2 442  ? 163.439 187.788 184.685 1.00 54.99  ? 442  PHE A N   1 
ATOM   12669 C CA  . PHE B 2 442  ? 163.789 187.907 183.282 1.00 54.99  ? 442  PHE A CA  1 
ATOM   12670 C C   . PHE B 2 442  ? 164.874 188.970 183.110 1.00 54.99  ? 442  PHE A C   1 
ATOM   12671 O O   . PHE B 2 442  ? 165.469 189.434 184.084 1.00 54.99  ? 442  PHE A O   1 
ATOM   12672 C CB  . PHE B 2 442  ? 162.526 188.232 182.476 1.00 54.99  ? 442  PHE A CB  1 
ATOM   12673 C CG  . PHE B 2 442  ? 161.859 189.511 182.893 1.00 54.99  ? 442  PHE A CG  1 
ATOM   12674 C CD1 . PHE B 2 442  ? 160.911 189.517 183.901 1.00 54.99  ? 442  PHE A CD1 1 
ATOM   12675 C CD2 . PHE B 2 442  ? 162.188 190.710 182.285 1.00 54.99  ? 442  PHE A CD2 1 
ATOM   12676 C CE1 . PHE B 2 442  ? 160.300 190.689 184.290 1.00 54.99  ? 442  PHE A CE1 1 
ATOM   12677 C CE2 . PHE B 2 442  ? 161.578 191.886 182.671 1.00 54.99  ? 442  PHE A CE2 1 
ATOM   12678 C CZ  . PHE B 2 442  ? 160.631 191.876 183.675 1.00 54.99  ? 442  PHE A CZ  1 
ATOM   12679 N N   . THR B 2 443  ? 165.129 189.366 181.864 1.00 54.43  ? 443  THR A N   1 
ATOM   12680 C CA  . THR B 2 443  ? 166.123 190.379 181.534 1.00 54.43  ? 443  THR A CA  1 
ATOM   12681 C C   . THR B 2 443  ? 165.424 191.615 180.990 1.00 54.43  ? 443  THR A C   1 
ATOM   12682 O O   . THR B 2 443  ? 164.632 191.517 180.047 1.00 54.43  ? 443  THR A O   1 
ATOM   12683 C CB  . THR B 2 443  ? 167.117 189.840 180.501 1.00 54.43  ? 443  THR A CB  1 
ATOM   12684 O OG1 . THR B 2 443  ? 167.975 188.874 181.117 1.00 54.43  ? 443  THR A OG1 1 
ATOM   12685 C CG2 . THR B 2 443  ? 167.952 190.964 179.918 1.00 54.43  ? 443  THR A CG2 1 
ATOM   12686 N N   . MET B 2 444  ? 165.715 192.775 181.580 1.00 56.06  ? 444  MET A N   1 
ATOM   12687 C CA  . MET B 2 444  ? 165.230 194.049 181.069 1.00 56.06  ? 444  MET A CA  1 
ATOM   12688 C C   . MET B 2 444  ? 166.407 194.835 180.510 1.00 56.06  ? 444  MET A C   1 
ATOM   12689 O O   . MET B 2 444  ? 167.463 194.918 181.146 1.00 56.06  ? 444  MET A O   1 
ATOM   12690 C CB  . MET B 2 444  ? 164.508 194.864 182.145 1.00 56.06  ? 444  MET A CB  1 
ATOM   12691 C CG  . MET B 2 444  ? 165.245 195.011 183.459 1.00 56.06  ? 444  MET A CG  1 
ATOM   12692 S SD  . MET B 2 444  ? 164.221 195.823 184.700 1.00 56.06  ? 444  MET A SD  1 
ATOM   12693 C CE  . MET B 2 444  ? 165.190 195.549 186.178 1.00 56.06  ? 444  MET A CE  1 
ATOM   12694 N N   . GLU B 2 445  ? 166.226 195.402 179.319 1.00 53.08  ? 445  GLU A N   1 
ATOM   12695 C CA  . GLU B 2 445  ? 167.314 196.042 178.600 1.00 53.08  ? 445  GLU A CA  1 
ATOM   12696 C C   . GLU B 2 445  ? 166.840 197.346 177.979 1.00 53.08  ? 445  GLU A C   1 
ATOM   12697 O O   . GLU B 2 445  ? 165.661 197.506 177.651 1.00 53.08  ? 445  GLU A O   1 
ATOM   12698 C CB  . GLU B 2 445  ? 167.876 195.116 177.515 1.00 53.08  ? 445  GLU A CB  1 
ATOM   12699 C CG  . GLU B 2 445  ? 166.944 194.915 176.331 1.00 53.08  ? 445  GLU A CG  1 
ATOM   12700 C CD  . GLU B 2 445  ? 165.838 193.920 176.612 1.00 53.08  ? 445  GLU A CD  1 
ATOM   12701 O OE1 . GLU B 2 445  ? 165.741 193.454 177.765 1.00 53.08  ? 445  GLU A OE1 1 
ATOM   12702 O OE2 . GLU B 2 445  ? 165.069 193.602 175.680 1.00 53.08  ? 445  GLU A OE2 1 
ATOM   12703 N N   . ASN B 2 446  ? 167.783 198.275 177.822 1.00 49.16  ? 446  ASN A N   1 
ATOM   12704 C CA  . ASN B 2 446  ? 167.561 199.548 177.138 1.00 49.16  ? 446  ASN A CA  1 
ATOM   12705 C C   . ASN B 2 446  ? 166.399 200.322 177.761 1.00 49.16  ? 446  ASN A C   1 
ATOM   12706 O O   . ASN B 2 446  ? 165.361 200.556 177.143 1.00 49.16  ? 446  ASN A O   1 
ATOM   12707 C CB  . ASN B 2 446  ? 167.341 199.329 175.641 1.00 49.16  ? 446  ASN A CB  1 
ATOM   12708 C CG  . ASN B 2 446  ? 167.300 200.625 174.866 1.00 49.16  ? 446  ASN A CG  1 
ATOM   12709 O OD1 . ASN B 2 446  ? 167.785 201.656 175.331 1.00 49.16  ? 446  ASN A OD1 1 
ATOM   12710 N ND2 . ASN B 2 446  ? 166.724 200.581 173.674 1.00 49.16  ? 446  ASN A ND2 1 
ATOM   12711 N N   . GLN B 2 447  ? 166.591 200.706 179.020 1.00 46.35  ? 447  GLN A N   1 
ATOM   12712 C CA  . GLN B 2 447  ? 165.601 201.473 179.756 1.00 46.35  ? 447  GLN A CA  1 
ATOM   12713 C C   . GLN B 2 447  ? 166.308 202.505 180.620 1.00 46.35  ? 447  GLN A C   1 
ATOM   12714 O O   . GLN B 2 447  ? 167.467 202.326 180.998 1.00 46.35  ? 447  GLN A O   1 
ATOM   12715 C CB  . GLN B 2 447  ? 164.738 200.575 180.648 1.00 46.35  ? 447  GLN A CB  1 
ATOM   12716 C CG  . GLN B 2 447  ? 163.508 200.015 179.970 1.00 46.35  ? 447  GLN A CG  1 
ATOM   12717 C CD  . GLN B 2 447  ? 162.303 200.008 180.890 1.00 46.35  ? 447  GLN A CD  1 
ATOM   12718 O OE1 . GLN B 2 447  ? 162.244 199.241 181.851 1.00 46.35  ? 447  GLN A OE1 1 
ATOM   12719 N NE2 . GLN B 2 447  ? 161.338 200.870 180.602 1.00 46.35  ? 447  GLN A NE2 1 
ATOM   12720 N N   . ILE B 2 448  ? 165.609 203.594 180.922 1.00 41.46  ? 448  ILE A N   1 
ATOM   12721 C CA  . ILE B 2 448  ? 166.049 204.534 181.945 1.00 41.46  ? 448  ILE A CA  1 
ATOM   12722 C C   . ILE B 2 448  ? 164.898 204.742 182.917 1.00 41.46  ? 448  ILE A C   1 
ATOM   12723 O O   . ILE B 2 448  ? 163.732 204.794 182.514 1.00 41.46  ? 448  ILE A O   1 
ATOM   12724 C CB  . ILE B 2 448  ? 166.540 205.877 181.356 1.00 41.46  ? 448  ILE A CB  1 
ATOM   12725 C CG1 . ILE B 2 448  ? 165.387 206.855 181.137 1.00 41.46  ? 448  ILE A CG1 1 
ATOM   12726 C CG2 . ILE B 2 448  ? 167.305 205.658 180.062 1.00 41.46  ? 448  ILE A CG2 1 
ATOM   12727 C CD1 . ILE B 2 448  ? 165.847 208.254 180.806 1.00 41.46  ? 448  ILE A CD1 1 
ATOM   12728 N N   . HIS B 2 449  ? 165.224 204.793 184.206 1.00 41.34  ? 449  HIS A N   1 
ATOM   12729 C CA  . HIS B 2 449  ? 164.259 205.035 185.267 1.00 41.34  ? 449  HIS A CA  1 
ATOM   12730 C C   . HIS B 2 449  ? 164.601 206.353 185.942 1.00 41.34  ? 449  HIS A C   1 
ATOM   12731 O O   . HIS B 2 449  ? 165.771 206.613 186.238 1.00 41.34  ? 449  HIS A O   1 
ATOM   12732 C CB  . HIS B 2 449  ? 164.261 203.907 186.301 1.00 41.34  ? 449  HIS A CB  1 
ATOM   12733 C CG  . HIS B 2 449  ? 164.014 202.550 185.723 1.00 41.34  ? 449  HIS A CG  1 
ATOM   12734 N ND1 . HIS B 2 449  ? 162.760 201.984 185.660 1.00 41.34  ? 449  HIS A ND1 1 
ATOM   12735 C CD2 . HIS B 2 449  ? 164.864 201.636 185.198 1.00 41.34  ? 449  HIS A CD2 1 
ATOM   12736 C CE1 . HIS B 2 449  ? 162.847 200.783 185.115 1.00 41.34  ? 449  HIS A CE1 1 
ATOM   12737 N NE2 . HIS B 2 449  ? 164.114 200.550 184.824 1.00 41.34  ? 449  HIS A NE2 1 
ATOM   12738 N N   . GLN B 2 450  ? 163.586 207.183 186.178 1.00 38.74  ? 450  GLN A N   1 
ATOM   12739 C CA  . GLN B 2 450  ? 163.763 208.460 186.854 1.00 38.74  ? 450  GLN A CA  1 
ATOM   12740 C C   . GLN B 2 450  ? 162.696 208.612 187.925 1.00 38.74  ? 450  GLN A C   1 
ATOM   12741 O O   . GLN B 2 450  ? 161.517 208.343 187.680 1.00 38.74  ? 450  GLN A O   1 
ATOM   12742 C CB  . GLN B 2 450  ? 163.685 209.624 185.868 1.00 38.74  ? 450  GLN A CB  1 
ATOM   12743 C CG  . GLN B 2 450  ? 164.998 209.931 185.178 1.00 38.74  ? 450  GLN A CG  1 
ATOM   12744 C CD  . GLN B 2 450  ? 164.801 210.440 183.766 1.00 38.74  ? 450  GLN A CD  1 
ATOM   12745 O OE1 . GLN B 2 450  ? 163.680 210.485 183.262 1.00 38.74  ? 450  GLN A OE1 1 
ATOM   12746 N NE2 . GLN B 2 450  ? 165.894 210.828 183.120 1.00 38.74  ? 450  GLN A NE2 1 
ATOM   12747 N N   . HIS B 2 451  ? 163.122 209.045 189.112 1.00 40.17  ? 451  HIS A N   1 
ATOM   12748 C CA  . HIS B 2 451  ? 162.239 209.212 190.266 1.00 40.17  ? 451  HIS A CA  1 
ATOM   12749 C C   . HIS B 2 451  ? 161.510 207.920 190.612 1.00 40.17  ? 451  HIS A C   1 
ATOM   12750 O O   . HIS B 2 451  ? 160.389 207.945 191.127 1.00 40.17  ? 451  HIS A O   1 
ATOM   12751 C CB  . HIS B 2 451  ? 161.233 210.344 190.044 1.00 40.17  ? 451  HIS A CB  1 
ATOM   12752 C CG  . HIS B 2 451  ? 161.839 211.711 190.095 1.00 40.17  ? 451  HIS A CG  1 
ATOM   12753 N ND1 . HIS B 2 451  ? 163.058 212.005 189.525 1.00 40.17  ? 451  HIS A ND1 1 
ATOM   12754 C CD2 . HIS B 2 451  ? 161.394 212.863 190.646 1.00 40.17  ? 451  HIS A CD2 1 
ATOM   12755 C CE1 . HIS B 2 451  ? 163.339 213.281 189.723 1.00 40.17  ? 451  HIS A CE1 1 
ATOM   12756 N NE2 . HIS B 2 451  ? 162.344 213.824 190.403 1.00 40.17  ? 451  HIS A NE2 1 
ATOM   12757 N N   . GLY B 2 452  ? 162.135 206.781 190.333 1.00 39.07  ? 452  GLY A N   1 
ATOM   12758 C CA  . GLY B 2 452  ? 161.533 205.516 190.686 1.00 39.07  ? 452  GLY A CA  1 
ATOM   12759 C C   . GLY B 2 452  ? 161.548 205.287 192.184 1.00 39.07  ? 452  GLY A C   1 
ATOM   12760 O O   . GLY B 2 452  ? 162.404 205.793 192.908 1.00 39.07  ? 452  GLY A O   1 
ATOM   12761 N N   . LYS B 2 453  ? 160.582 204.515 192.696 1.00 37.89  ? 453  LYS A N   1 
ATOM   12762 C CA  . LYS B 2 453  ? 160.553 204.168 194.145 1.00 37.89  ? 453  LYS A CA  1 
ATOM   12763 C C   . LYS B 2 453  ? 160.399 202.657 194.243 1.00 37.89  ? 453  LYS A C   1 
ATOM   12764 O O   . LYS B 2 453  ? 159.276 202.204 194.465 1.00 37.89  ? 453  LYS A O   1 
ATOM   12765 C CB  . LYS B 2 453  ? 159.444 204.910 194.893 1.00 37.89  ? 453  LYS A CB  1 
ATOM   12766 C CG  . LYS B 2 453  ? 159.696 206.395 195.112 1.00 37.89  ? 453  LYS A CG  1 
ATOM   12767 C CD  . LYS B 2 453  ? 159.267 206.861 196.483 1.00 37.89  ? 453  LYS A CD  1 
ATOM   12768 C CE  . LYS B 2 453  ? 158.571 205.777 197.278 1.00 37.89  ? 453  LYS A CE  1 
ATOM   12769 N NZ  . LYS B 2 453  ? 158.603 206.057 198.732 1.00 37.89  ? 453  LYS A NZ  1 
ATOM   12770 N N   . LEU B 2 454  ? 161.489 201.931 194.078 1.00 37.81  ? 454  LEU A N   1 
ATOM   12771 C CA  . LEU B 2 454  ? 161.520 200.473 194.071 1.00 37.81  ? 454  LEU A CA  1 
ATOM   12772 C C   . LEU B 2 454  ? 161.523 200.002 195.517 1.00 37.81  ? 454  LEU A C   1 
ATOM   12773 O O   . LEU B 2 454  ? 162.559 200.009 196.186 1.00 37.81  ? 454  LEU A O   1 
ATOM   12774 C CB  . LEU B 2 454  ? 162.735 199.969 193.302 1.00 37.81  ? 454  LEU A CB  1 
ATOM   12775 C CG  . LEU B 2 454  ? 162.568 199.937 191.781 1.00 37.81  ? 454  LEU A CG  1 
ATOM   12776 C CD1 . LEU B 2 454  ? 162.834 201.301 191.169 1.00 37.81  ? 454  LEU A CD1 1 
ATOM   12777 C CD2 . LEU B 2 454  ? 163.475 198.891 191.162 1.00 37.81  ? 454  LEU A CD2 1 
ATOM   12778 N N   . VAL B 2 455  ? 160.359 199.583 196.004 1.00 42.60  ? 455  VAL A N   1 
ATOM   12779 C CA  . VAL B 2 455  ? 160.165 199.216 197.402 1.00 42.60  ? 455  VAL A CA  1 
ATOM   12780 C C   . VAL B 2 455  ? 159.949 197.713 197.488 1.00 42.60  ? 455  VAL A C   1 
ATOM   12781 O O   . VAL B 2 455  ? 159.044 197.171 196.843 1.00 42.60  ? 455  VAL A O   1 
ATOM   12782 C CB  . VAL B 2 455  ? 158.980 199.976 198.020 1.00 42.60  ? 455  VAL A CB  1 
ATOM   12783 C CG1 . VAL B 2 455  ? 159.049 199.923 199.534 1.00 42.60  ? 455  VAL A CG1 1 
ATOM   12784 C CG2 . VAL B 2 455  ? 158.959 201.418 197.531 1.00 42.60  ? 455  VAL A CG2 1 
ATOM   12785 N N   . ASN B 2 456  ? 160.780 197.046 198.291 1.00 46.60  ? 456  ASN A N   1 
ATOM   12786 C CA  . ASN B 2 456  ? 160.659 195.613 198.560 1.00 46.60  ? 456  ASN A CA  1 
ATOM   12787 C C   . ASN B 2 456  ? 160.694 194.795 197.268 1.00 46.60  ? 456  ASN A C   1 
ATOM   12788 O O   . ASN B 2 456  ? 159.896 193.881 197.061 1.00 46.60  ? 456  ASN A O   1 
ATOM   12789 C CB  . ASN B 2 456  ? 159.392 195.315 199.364 1.00 46.60  ? 456  ASN A CB  1 
ATOM   12790 C CG  . ASN B 2 456  ? 159.422 193.946 200.014 1.00 46.60  ? 456  ASN A CG  1 
ATOM   12791 O OD1 . ASN B 2 456  ? 160.367 193.178 199.826 1.00 46.60  ? 456  ASN A OD1 1 
ATOM   12792 N ND2 . ASN B 2 456  ? 158.387 193.633 200.783 1.00 46.60  ? 456  ASN A ND2 1 
ATOM   12793 N N   . ASP B 2 457  ? 161.637 195.134 196.394 1.00 45.94  ? 457  ASP A N   1 
ATOM   12794 C CA  . ASP B 2 457  ? 161.807 194.403 195.151 1.00 45.94  ? 457  ASP A CA  1 
ATOM   12795 C C   . ASP B 2 457  ? 162.816 193.272 195.341 1.00 45.94  ? 457  ASP A C   1 
ATOM   12796 O O   . ASP B 2 457  ? 163.347 193.055 196.431 1.00 45.94  ? 457  ASP A O   1 
ATOM   12797 C CB  . ASP B 2 457  ? 162.234 195.349 194.032 1.00 45.94  ? 457  ASP A CB  1 
ATOM   12798 C CG  . ASP B 2 457  ? 161.061 196.060 193.401 1.00 45.94  ? 457  ASP A CG  1 
ATOM   12799 O OD1 . ASP B 2 457  ? 159.916 195.609 193.614 1.00 45.94  ? 457  ASP A OD1 1 
ATOM   12800 O OD2 . ASP B 2 457  ? 161.276 197.066 192.696 1.00 45.94  ? 457  ASP A OD2 1 
ATOM   12801 N N   . LYS B 2 458  ? 163.080 192.535 194.265 1.00 45.86  ? 458  LYS A N   1 
ATOM   12802 C CA  . LYS B 2 458  ? 163.997 191.403 194.332 1.00 45.86  ? 458  LYS A CA  1 
ATOM   12803 C C   . LYS B 2 458  ? 164.469 191.080 192.925 1.00 45.86  ? 458  LYS A C   1 
ATOM   12804 O O   . LYS B 2 458  ? 163.660 190.703 192.073 1.00 45.86  ? 458  LYS A O   1 
ATOM   12805 C CB  . LYS B 2 458  ? 163.316 190.192 194.970 1.00 45.86  ? 458  LYS A CB  1 
ATOM   12806 C CG  . LYS B 2 458  ? 164.027 188.873 194.736 1.00 45.86  ? 458  LYS A CG  1 
ATOM   12807 C CD  . LYS B 2 458  ? 163.370 187.757 195.532 1.00 45.86  ? 458  LYS A CD  1 
ATOM   12808 C CE  . LYS B 2 458  ? 164.155 186.461 195.427 1.00 45.86  ? 458  LYS A CE  1 
ATOM   12809 N NZ  . LYS B 2 458  ? 165.412 186.506 196.219 1.00 45.86  ? 458  LYS A NZ  1 
ATOM   12810 N N   . PHE B 2 459  ? 165.768 191.234 192.679 1.00 46.42  ? 459  PHE A N   1 
ATOM   12811 C CA  . PHE B 2 459  ? 166.378 190.924 191.392 1.00 46.42  ? 459  PHE A CA  1 
ATOM   12812 C C   . PHE B 2 459  ? 167.238 189.680 191.572 1.00 46.42  ? 459  PHE A C   1 
ATOM   12813 O O   . PHE B 2 459  ? 168.281 189.733 192.232 1.00 46.42  ? 459  PHE A O   1 
ATOM   12814 C CB  . PHE B 2 459  ? 167.213 192.096 190.878 1.00 46.42  ? 459  PHE A CB  1 
ATOM   12815 C CG  . PHE B 2 459  ? 166.446 193.382 190.744 1.00 46.42  ? 459  PHE A CG  1 
ATOM   12816 C CD1 . PHE B 2 459  ? 165.088 193.376 190.486 1.00 46.42  ? 459  PHE A CD1 1 
ATOM   12817 C CD2 . PHE B 2 459  ? 167.090 194.598 190.866 1.00 46.42  ? 459  PHE A CD2 1 
ATOM   12818 C CE1 . PHE B 2 459  ? 164.389 194.559 190.359 1.00 46.42  ? 459  PHE A CE1 1 
ATOM   12819 C CE2 . PHE B 2 459  ? 166.396 195.782 190.741 1.00 46.42  ? 459  PHE A CE2 1 
ATOM   12820 C CZ  . PHE B 2 459  ? 165.045 195.762 190.487 1.00 46.42  ? 459  PHE A CZ  1 
ATOM   12821 N N   . THR B 2 460  ? 166.806 188.564 190.991 1.00 50.80  ? 460  THR A N   1 
ATOM   12822 C CA  . THR B 2 460  ? 167.486 187.285 191.162 1.00 50.80  ? 460  THR A CA  1 
ATOM   12823 C C   . THR B 2 460  ? 167.776 186.668 189.804 1.00 50.80  ? 460  THR A C   1 
ATOM   12824 O O   . THR B 2 460  ? 166.851 186.437 189.018 1.00 50.80  ? 460  THR A O   1 
ATOM   12825 C CB  . THR B 2 460  ? 166.653 186.329 192.017 1.00 50.80  ? 460  THR A CB  1 
ATOM   12826 O OG1 . THR B 2 460  ? 166.605 186.810 193.366 1.00 50.80  ? 460  THR A OG1 1 
ATOM   12827 C CG2 . THR B 2 460  ? 167.261 184.937 192.003 1.00 50.80  ? 460  THR A CG2 1 
ATOM   12828 N N   . ARG B 2 461  ? 169.056 186.392 189.541 1.00 56.07  ? 461  ARG A N   1 
ATOM   12829 C CA  . ARG B 2 461  ? 169.502 185.650 188.360 1.00 56.07  ? 461  ARG A CA  1 
ATOM   12830 C C   . ARG B 2 461  ? 168.991 186.295 187.071 1.00 56.07  ? 461  ARG A C   1 
ATOM   12831 O O   . ARG B 2 461  ? 168.219 185.710 186.311 1.00 56.07  ? 461  ARG A O   1 
ATOM   12832 C CB  . ARG B 2 461  ? 169.075 184.181 188.447 1.00 56.07  ? 461  ARG A CB  1 
ATOM   12833 C CG  . ARG B 2 461  ? 170.167 183.246 188.937 1.00 56.07  ? 461  ARG A CG  1 
ATOM   12834 C CD  . ARG B 2 461  ? 169.658 181.824 189.065 1.00 56.07  ? 461  ARG A CD  1 
ATOM   12835 N NE  . ARG B 2 461  ? 168.544 181.730 189.998 1.00 56.07  ? 461  ARG A NE  1 
ATOM   12836 C CZ  . ARG B 2 461  ? 168.677 181.575 191.309 1.00 56.07  ? 461  ARG A CZ  1 
ATOM   12837 N NH1 . ARG B 2 461  ? 169.868 181.495 191.878 1.00 56.07  ? 461  ARG A NH1 1 
ATOM   12838 N NH2 . ARG B 2 461  ? 167.588 181.502 192.067 1.00 56.07  ? 461  ARG A NH2 1 
ATOM   12839 N N   . MET B 2 462  ? 169.443 187.522 186.830 1.00 56.54  ? 462  MET A N   1 
ATOM   12840 C CA  . MET B 2 462  ? 168.974 188.284 185.686 1.00 56.54  ? 462  MET A CA  1 
ATOM   12841 C C   . MET B 2 462  ? 170.113 189.092 185.084 1.00 56.54  ? 462  MET A C   1 
ATOM   12842 O O   . MET B 2 462  ? 171.221 189.162 185.628 1.00 56.54  ? 462  MET A O   1 
ATOM   12843 C CB  . MET B 2 462  ? 167.805 189.193 186.071 1.00 56.54  ? 462  MET A CB  1 
ATOM   12844 C CG  . MET B 2 462  ? 168.220 190.552 186.554 1.00 56.54  ? 462  MET A CG  1 
ATOM   12845 S SD  . MET B 2 462  ? 166.857 191.707 186.667 1.00 56.54  ? 462  MET A SD  1 
ATOM   12846 C CE  . MET B 2 462  ? 166.728 192.205 184.956 1.00 56.54  ? 462  MET A CE  1 
ATOM   12847 N N   . TYR B 2 463  ? 169.818 189.705 183.939 1.00 54.67  ? 463  TYR A N   1 
ATOM   12848 C CA  . TYR B 2 463  ? 170.786 190.433 183.131 1.00 54.67  ? 463  TYR A CA  1 
ATOM   12849 C C   . TYR B 2 463  ? 170.347 191.884 182.999 1.00 54.67  ? 463  TYR A C   1 
ATOM   12850 O O   . TYR B 2 463  ? 169.225 192.164 182.567 1.00 54.67  ? 463  TYR A O   1 
ATOM   12851 C CB  . TYR B 2 463  ? 170.915 189.787 181.750 1.00 54.67  ? 463  TYR A CB  1 
ATOM   12852 C CG  . TYR B 2 463  ? 172.149 190.170 180.965 1.00 54.67  ? 463  TYR A CG  1 
ATOM   12853 C CD1 . TYR B 2 463  ? 173.408 190.124 181.542 1.00 54.67  ? 463  TYR A CD1 1 
ATOM   12854 C CD2 . TYR B 2 463  ? 172.051 190.551 179.637 1.00 54.67  ? 463  TYR A CD2 1 
ATOM   12855 C CE1 . TYR B 2 463  ? 174.536 190.465 180.816 1.00 54.67  ? 463  TYR A CE1 1 
ATOM   12856 C CE2 . TYR B 2 463  ? 173.167 190.894 178.909 1.00 54.67  ? 463  TYR A CE2 1 
ATOM   12857 C CZ  . TYR B 2 463  ? 174.405 190.849 179.500 1.00 54.67  ? 463  TYR A CZ  1 
ATOM   12858 O OH  . TYR B 2 463  ? 175.516 191.189 178.767 1.00 54.67  ? 463  TYR A OH  1 
ATOM   12859 N N   . PHE B 2 464  ? 171.231 192.797 183.378 1.00 51.65  ? 464  PHE A N   1 
ATOM   12860 C CA  . PHE B 2 464  ? 171.031 194.230 183.215 1.00 51.65  ? 464  PHE A CA  1 
ATOM   12861 C C   . PHE B 2 464  ? 171.796 194.661 181.973 1.00 51.65  ? 464  PHE A C   1 
ATOM   12862 O O   . PHE B 2 464  ? 173.013 194.475 181.903 1.00 51.65  ? 464  PHE A O   1 
ATOM   12863 C CB  . PHE B 2 464  ? 171.544 194.985 184.442 1.00 51.65  ? 464  PHE A CB  1 
ATOM   12864 C CG  . PHE B 2 464  ? 170.487 195.276 185.465 1.00 51.65  ? 464  PHE A CG  1 
ATOM   12865 C CD1 . PHE B 2 464  ? 169.546 194.324 185.803 1.00 51.65  ? 464  PHE A CD1 1 
ATOM   12866 C CD2 . PHE B 2 464  ? 170.454 196.498 186.107 1.00 51.65  ? 464  PHE A CD2 1 
ATOM   12867 C CE1 . PHE B 2 464  ? 168.583 194.594 186.746 1.00 51.65  ? 464  PHE A CE1 1 
ATOM   12868 C CE2 . PHE B 2 464  ? 169.493 196.771 187.050 1.00 51.65  ? 464  PHE A CE2 1 
ATOM   12869 C CZ  . PHE B 2 464  ? 168.556 195.816 187.369 1.00 51.65  ? 464  PHE A CZ  1 
ATOM   12870 N N   . LYS B 2 465  ? 171.094 195.221 180.992 1.00 52.81  ? 465  LYS A N   1 
ATOM   12871 C CA  . LYS B 2 465  ? 171.715 195.597 179.724 1.00 52.81  ? 465  LYS A CA  1 
ATOM   12872 C C   . LYS B 2 465  ? 171.303 197.013 179.352 1.00 52.81  ? 465  LYS A C   1 
ATOM   12873 O O   . LYS B 2 465  ? 170.141 197.251 179.011 1.00 52.81  ? 465  LYS A O   1 
ATOM   12874 C CB  . LYS B 2 465  ? 171.338 194.617 178.613 1.00 52.81  ? 465  LYS A CB  1 
ATOM   12875 C CG  . LYS B 2 465  ? 171.903 194.990 177.256 1.00 52.81  ? 465  LYS A CG  1 
ATOM   12876 C CD  . LYS B 2 465  ? 171.527 193.970 176.197 1.00 52.81  ? 465  LYS A CD  1 
ATOM   12877 C CE  . LYS B 2 465  ? 172.323 194.187 174.921 1.00 52.81  ? 465  LYS A CE  1 
ATOM   12878 N NZ  . LYS B 2 465  ? 173.382 193.156 174.742 1.00 52.81  ? 465  LYS A NZ  1 
ATOM   12879 N N   . HIS B 2 466  ? 172.255 197.944 179.411 1.00 52.29  ? 466  HIS A N   1 
ATOM   12880 C CA  . HIS B 2 466  ? 172.048 199.311 178.940 1.00 52.29  ? 466  HIS A CA  1 
ATOM   12881 C C   . HIS B 2 466  ? 170.852 199.967 179.624 1.00 52.29  ? 466  HIS A C   1 
ATOM   12882 O O   . HIS B 2 466  ? 170.039 200.642 178.989 1.00 52.29  ? 466  HIS A O   1 
ATOM   12883 C CB  . HIS B 2 466  ? 171.881 199.341 177.420 1.00 52.29  ? 466  HIS A CB  1 
ATOM   12884 C CG  . HIS B 2 466  ? 173.076 199.871 176.692 1.00 52.29  ? 466  HIS A CG  1 
ATOM   12885 N ND1 . HIS B 2 466  ? 173.364 201.215 176.615 1.00 52.29  ? 466  HIS A ND1 1 
ATOM   12886 C CD2 . HIS B 2 466  ? 174.055 199.236 176.005 1.00 52.29  ? 466  HIS A CD2 1 
ATOM   12887 C CE1 . HIS B 2 466  ? 174.470 201.387 175.912 1.00 52.29  ? 466  HIS A CE1 1 
ATOM   12888 N NE2 . HIS B 2 466  ? 174.909 200.200 175.531 1.00 52.29  ? 466  HIS A NE2 1 
ATOM   12889 N N   . VAL B 2 467  ? 170.742 199.768 180.934 1.00 47.16  ? 467  VAL A N   1 
ATOM   12890 C CA  . VAL B 2 467  ? 169.652 200.326 181.727 1.00 47.16  ? 467  VAL A CA  1 
ATOM   12891 C C   . VAL B 2 467  ? 170.243 201.270 182.763 1.00 47.16  ? 467  VAL A C   1 
ATOM   12892 O O   . VAL B 2 467  ? 171.266 200.969 183.386 1.00 47.16  ? 467  VAL A O   1 
ATOM   12893 C CB  . VAL B 2 467  ? 168.801 199.221 182.385 1.00 47.16  ? 467  VAL A CB  1 
ATOM   12894 C CG1 . VAL B 2 467  ? 169.647 198.352 183.289 1.00 47.16  ? 467  VAL A CG1 1 
ATOM   12895 C CG2 . VAL B 2 467  ? 167.638 199.824 183.150 1.00 47.16  ? 467  VAL A CG2 1 
ATOM   12896 N N   . LEU B 2 468  ? 169.607 202.423 182.928 1.00 44.07  ? 468  LEU A N   1 
ATOM   12897 C CA  . LEU B 2 468  ? 170.116 203.503 183.758 1.00 44.07  ? 468  LEU A CA  1 
ATOM   12898 C C   . LEU B 2 468  ? 169.116 203.832 184.857 1.00 44.07  ? 468  LEU A C   1 
ATOM   12899 O O   . LEU B 2 468  ? 167.903 203.814 184.633 1.00 44.07  ? 468  LEU A O   1 
ATOM   12900 C CB  . LEU B 2 468  ? 170.397 204.747 182.912 1.00 44.07  ? 468  LEU A CB  1 
ATOM   12901 C CG  . LEU B 2 468  ? 170.827 206.025 183.627 1.00 44.07  ? 468  LEU A CG  1 
ATOM   12902 C CD1 . LEU B 2 468  ? 172.331 206.047 183.819 1.00 44.07  ? 468  LEU A CD1 1 
ATOM   12903 C CD2 . LEU B 2 468  ? 170.373 207.236 182.839 1.00 44.07  ? 468  LEU A CD2 1 
ATOM   12904 N N   . PHE B 2 469  ? 169.630 204.114 186.051 1.00 43.34  ? 469  PHE A N   1 
ATOM   12905 C CA  . PHE B 2 469  ? 168.816 204.498 187.194 1.00 43.34  ? 469  PHE A CA  1 
ATOM   12906 C C   . PHE B 2 469  ? 169.213 205.896 187.642 1.00 43.34  ? 469  PHE A C   1 
ATOM   12907 O O   . PHE B 2 469  ? 170.394 206.153 187.897 1.00 43.34  ? 469  PHE A O   1 
ATOM   12908 C CB  . PHE B 2 469  ? 168.994 203.514 188.351 1.00 43.34  ? 469  PHE A CB  1 
ATOM   12909 C CG  . PHE B 2 469  ? 168.312 202.196 188.141 1.00 43.34  ? 469  PHE A CG  1 
ATOM   12910 C CD1 . PHE B 2 469  ? 166.939 202.083 188.262 1.00 43.34  ? 469  PHE A CD1 1 
ATOM   12911 C CD2 . PHE B 2 469  ? 169.045 201.067 187.833 1.00 43.34  ? 469  PHE A CD2 1 
ATOM   12912 C CE1 . PHE B 2 469  ? 166.311 200.871 188.074 1.00 43.34  ? 469  PHE A CE1 1 
ATOM   12913 C CE2 . PHE B 2 469  ? 168.423 199.855 187.643 1.00 43.34  ? 469  PHE A CE2 1 
ATOM   12914 C CZ  . PHE B 2 469  ? 167.056 199.756 187.764 1.00 43.34  ? 469  PHE A CZ  1 
ATOM   12915 N N   . GLU B 2 470  ? 168.235 206.793 187.746 1.00 42.65  ? 470  GLU A N   1 
ATOM   12916 C CA  . GLU B 2 470  ? 168.482 208.141 188.226 1.00 42.65  ? 470  GLU A CA  1 
ATOM   12917 C C   . GLU B 2 470  ? 167.405 208.515 189.227 1.00 42.65  ? 470  GLU A C   1 
ATOM   12918 O O   . GLU B 2 470  ? 166.218 208.278 188.986 1.00 42.65  ? 470  GLU A O   1 
ATOM   12919 C CB  . GLU B 2 470  ? 168.487 209.161 187.081 1.00 42.65  ? 470  GLU A CB  1 
ATOM   12920 C CG  . GLU B 2 470  ? 169.545 208.921 186.027 1.00 42.65  ? 470  GLU A CG  1 
ATOM   12921 C CD  . GLU B 2 470  ? 169.390 209.845 184.836 1.00 42.65  ? 470  GLU A CD  1 
ATOM   12922 O OE1 . GLU B 2 470  ? 168.241 210.215 184.515 1.00 42.65  ? 470  GLU A OE1 1 
ATOM   12923 O OE2 . GLU B 2 470  ? 170.415 210.205 184.223 1.00 42.65  ? 470  GLU A OE2 1 
ATOM   12924 N N   . ASP B 2 471  ? 167.826 209.093 190.350 1.00 42.93  ? 471  ASP A N   1 
ATOM   12925 C CA  . ASP B 2 471  ? 166.911 209.609 191.366 1.00 42.93  ? 471  ASP A CA  1 
ATOM   12926 C C   . ASP B 2 471  ? 165.957 208.535 191.874 1.00 42.93  ? 471  ASP A C   1 
ATOM   12927 O O   . ASP B 2 471  ? 164.842 208.837 192.307 1.00 42.93  ? 471  ASP A O   1 
ATOM   12928 C CB  . ASP B 2 471  ? 166.118 210.808 190.837 1.00 42.93  ? 471  ASP A CB  1 
ATOM   12929 C CG  . ASP B 2 471  ? 167.008 211.882 190.254 1.00 42.93  ? 471  ASP A CG  1 
ATOM   12930 O OD1 . ASP B 2 471  ? 168.239 211.683 190.225 1.00 42.93  ? 471  ASP A OD1 1 
ATOM   12931 O OD2 . ASP B 2 471  ? 166.476 212.926 189.823 1.00 42.93  ? 471  ASP A OD2 1 
ATOM   12932 N N   . THR B 2 472  ? 166.370 207.275 191.821 1.00 40.68  ? 472  THR A N   1 
ATOM   12933 C CA  . THR B 2 472  ? 165.517 206.181 192.258 1.00 40.68  ? 472  THR A CA  1 
ATOM   12934 C C   . THR B 2 472  ? 165.783 205.870 193.724 1.00 40.68  ? 472  THR A C   1 
ATOM   12935 O O   . THR B 2 472  ? 166.922 205.934 194.192 1.00 40.68  ? 472  THR A O   1 
ATOM   12936 C CB  . THR B 2 472  ? 165.729 204.941 191.385 1.00 40.68  ? 472  THR A CB  1 
ATOM   12937 O OG1 . THR B 2 472  ? 164.703 203.982 191.658 1.00 40.68  ? 472  THR A OG1 1 
ATOM   12938 C CG2 . THR B 2 472  ? 167.091 204.315 191.627 1.00 40.68  ? 472  THR A CG2 1 
ATOM   12939 N N   . PHE B 2 473  ? 164.716 205.570 194.459 1.00 36.11  ? 473  PHE A N   1 
ATOM   12940 C CA  . PHE B 2 473  ? 164.785 205.336 195.897 1.00 36.11  ? 473  PHE A CA  1 
ATOM   12941 C C   . PHE B 2 473  ? 164.507 203.860 196.142 1.00 36.11  ? 473  PHE A C   1 
ATOM   12942 O O   . PHE B 2 473  ? 163.352 203.425 196.130 1.00 36.11  ? 473  PHE A O   1 
ATOM   12943 C CB  . PHE B 2 473  ? 163.799 206.234 196.641 1.00 36.11  ? 473  PHE A CB  1 
ATOM   12944 C CG  . PHE B 2 473  ? 163.340 205.683 197.959 1.00 36.11  ? 473  PHE A CG  1 
ATOM   12945 C CD1 . PHE B 2 473  ? 164.229 205.503 199.000 1.00 36.11  ? 473  PHE A CD1 1 
ATOM   12946 C CD2 . PHE B 2 473  ? 162.009 205.358 198.160 1.00 36.11  ? 473  PHE A CD2 1 
ATOM   12947 C CE1 . PHE B 2 473  ? 163.805 205.000 200.217 1.00 36.11  ? 473  PHE A CE1 1 
ATOM   12948 C CE2 . PHE B 2 473  ? 161.578 204.855 199.371 1.00 36.11  ? 473  PHE A CE2 1 
ATOM   12949 C CZ  . PHE B 2 473  ? 162.477 204.675 200.398 1.00 36.11  ? 473  PHE A CZ  1 
ATOM   12950 N N   . PHE B 2 474  ? 165.567 203.089 196.349 1.00 35.80  ? 474  PHE A N   1 
ATOM   12951 C CA  . PHE B 2 474  ? 165.399 201.681 196.657 1.00 35.80  ? 474  PHE A CA  1 
ATOM   12952 C C   . PHE B 2 474  ? 164.944 201.508 198.102 1.00 35.80  ? 474  PHE A C   1 
ATOM   12953 O O   . PHE B 2 474  ? 165.027 202.428 198.921 1.00 35.80  ? 474  PHE A O   1 
ATOM   12954 C CB  . PHE B 2 474  ? 166.703 200.922 196.416 1.00 35.80  ? 474  PHE A CB  1 
ATOM   12955 C CG  . PHE B 2 474  ? 167.007 200.691 194.967 1.00 35.80  ? 474  PHE A CG  1 
ATOM   12956 C CD1 . PHE B 2 474  ? 166.155 199.945 194.178 1.00 35.80  ? 474  PHE A CD1 1 
ATOM   12957 C CD2 . PHE B 2 474  ? 168.145 201.226 194.394 1.00 35.80  ? 474  PHE A CD2 1 
ATOM   12958 C CE1 . PHE B 2 474  ? 166.435 199.733 192.847 1.00 35.80  ? 474  PHE A CE1 1 
ATOM   12959 C CE2 . PHE B 2 474  ? 168.430 201.017 193.062 1.00 35.80  ? 474  PHE A CE2 1 
ATOM   12960 C CZ  . PHE B 2 474  ? 167.574 200.272 192.290 1.00 35.80  ? 474  PHE A CZ  1 
ATOM   12961 N N   . ASP B 2 475  ? 164.454 200.311 198.413 1.00 40.60  ? 475  ASP A N   1 
ATOM   12962 C CA  . ASP B 2 475  ? 164.007 200.014 199.771 1.00 40.60  ? 475  ASP A CA  1 
ATOM   12963 C C   . ASP B 2 475  ? 164.022 198.504 199.956 1.00 40.60  ? 475  ASP A C   1 
ATOM   12964 O O   . ASP B 2 475  ? 163.228 197.800 199.326 1.00 40.60  ? 475  ASP A O   1 
ATOM   12965 C CB  . ASP B 2 475  ? 162.619 200.587 200.028 1.00 40.60  ? 475  ASP A CB  1 
ATOM   12966 C CG  . ASP B 2 475  ? 162.248 200.589 201.496 1.00 40.60  ? 475  ASP A CG  1 
ATOM   12967 O OD1 . ASP B 2 475  ? 162.949 199.937 202.295 1.00 40.60  ? 475  ASP A OD1 1 
ATOM   12968 O OD2 . ASP B 2 475  ? 161.248 201.247 201.854 1.00 40.60  ? 475  ASP A OD2 1 
ATOM   12969 N N   . GLU B 2 476  ? 164.932 198.022 200.806 1.00 43.02  ? 476  GLU A N   1 
ATOM   12970 C CA  . GLU B 2 476  ? 165.042 196.611 201.194 1.00 43.02  ? 476  GLU A CA  1 
ATOM   12971 C C   . GLU B 2 476  ? 165.002 195.666 199.991 1.00 43.02  ? 476  GLU A C   1 
ATOM   12972 O O   . GLU B 2 476  ? 164.587 194.508 200.100 1.00 43.02  ? 476  GLU A O   1 
ATOM   12973 C CB  . GLU B 2 476  ? 163.976 196.241 202.238 1.00 43.02  ? 476  GLU A CB  1 
ATOM   12974 C CG  . GLU B 2 476  ? 164.016 194.822 202.786 1.00 43.02  ? 476  GLU A CG  1 
ATOM   12975 C CD  . GLU B 2 476  ? 165.278 194.548 203.580 1.00 43.02  ? 476  GLU A CD  1 
ATOM   12976 O OE1 . GLU B 2 476  ? 165.992 195.516 203.909 1.00 43.02  ? 476  GLU A OE1 1 
ATOM   12977 O OE2 . GLU B 2 476  ? 165.552 193.366 203.871 1.00 43.02  ? 476  GLU A OE2 1 
ATOM   12978 N N   . CYS B 2 477  ? 165.471 196.139 198.841 1.00 41.35  ? 477  CYS A N   1 
ATOM   12979 C CA  . CYS B 2 477  ? 165.562 195.288 197.668 1.00 41.35  ? 477  CYS A CA  1 
ATOM   12980 C C   . CYS B 2 477  ? 166.691 194.273 197.835 1.00 41.35  ? 477  CYS A C   1 
ATOM   12981 O O   . CYS B 2 477  ? 167.631 194.472 198.607 1.00 41.35  ? 477  CYS A O   1 
ATOM   12982 C CB  . CYS B 2 477  ? 165.788 196.125 196.413 1.00 41.35  ? 477  CYS A CB  1 
ATOM   12983 S SG  . CYS B 2 477  ? 167.118 197.334 196.571 1.00 41.35  ? 477  CYS A SG  1 
ATOM   12984 N N   . TYR B 2 478  ? 166.586 193.171 197.098 1.00 44.02  ? 478  TYR A N   1 
ATOM   12985 C CA  . TYR B 2 478  ? 167.545 192.080 197.188 1.00 44.02  ? 478  TYR A CA  1 
ATOM   12986 C C   . TYR B 2 478  ? 168.091 191.779 195.801 1.00 44.02  ? 478  TYR A C   1 
ATOM   12987 O O   . TYR B 2 478  ? 167.321 191.523 194.871 1.00 44.02  ? 478  TYR A O   1 
ATOM   12988 C CB  . TYR B 2 478  ? 166.897 190.830 197.792 1.00 44.02  ? 478  TYR A CB  1 
ATOM   12989 C CG  . TYR B 2 478  ? 167.866 189.706 198.070 1.00 44.02  ? 478  TYR A CG  1 
ATOM   12990 C CD1 . TYR B 2 478  ? 169.188 189.970 198.396 1.00 44.02  ? 478  TYR A CD1 1 
ATOM   12991 C CD2 . TYR B 2 478  ? 167.460 188.383 198.015 1.00 44.02  ? 478  TYR A CD2 1 
ATOM   12992 C CE1 . TYR B 2 478  ? 170.079 188.946 198.652 1.00 44.02  ? 478  TYR A CE1 1 
ATOM   12993 C CE2 . TYR B 2 478  ? 168.341 187.353 198.270 1.00 44.02  ? 478  TYR A CE2 1 
ATOM   12994 C CZ  . TYR B 2 478  ? 169.652 187.641 198.588 1.00 44.02  ? 478  TYR A CZ  1 
ATOM   12995 O OH  . TYR B 2 478  ? 170.539 186.619 198.845 1.00 44.02  ? 478  TYR A OH  1 
ATOM   12996 N N   . PHE B 2 479  ? 169.413 191.805 195.669 1.00 44.49  ? 479  PHE A N   1 
ATOM   12997 C CA  . PHE B 2 479  ? 170.094 191.558 194.403 1.00 44.49  ? 479  PHE A CA  1 
ATOM   12998 C C   . PHE B 2 479  ? 170.864 190.249 194.525 1.00 44.49  ? 479  PHE A C   1 
ATOM   12999 O O   . PHE B 2 479  ? 171.756 190.132 195.372 1.00 44.49  ? 479  PHE A O   1 
ATOM   13000 C CB  . PHE B 2 479  ? 171.056 192.697 194.061 1.00 44.49  ? 479  PHE A CB  1 
ATOM   13001 C CG  . PHE B 2 479  ? 170.378 193.965 193.602 1.00 44.49  ? 479  PHE A CG  1 
ATOM   13002 C CD1 . PHE B 2 479  ? 169.375 194.549 194.350 1.00 44.49  ? 479  PHE A CD1 1 
ATOM   13003 C CD2 . PHE B 2 479  ? 170.777 194.586 192.430 1.00 44.49  ? 479  PHE A CD2 1 
ATOM   13004 C CE1 . PHE B 2 479  ? 168.768 195.713 193.931 1.00 44.49  ? 479  PHE A CE1 1 
ATOM   13005 C CE2 . PHE B 2 479  ? 170.174 195.752 192.010 1.00 44.49  ? 479  PHE A CE2 1 
ATOM   13006 C CZ  . PHE B 2 479  ? 169.171 196.318 192.763 1.00 44.49  ? 479  PHE A CZ  1 
ATOM   13007 N N   . GLU B 2 480  ? 170.533 189.276 193.681 1.00 50.88  ? 480  GLU A N   1 
ATOM   13008 C CA  . GLU B 2 480  ? 171.169 187.963 193.745 1.00 50.88  ? 480  GLU A CA  1 
ATOM   13009 C C   . GLU B 2 480  ? 171.482 187.473 192.341 1.00 50.88  ? 480  GLU A C   1 
ATOM   13010 O O   . GLU B 2 480  ? 170.581 187.374 191.504 1.00 50.88  ? 480  GLU A O   1 
ATOM   13011 C CB  . GLU B 2 480  ? 170.278 186.952 194.471 1.00 50.88  ? 480  GLU A CB  1 
ATOM   13012 C CG  . GLU B 2 480  ? 170.692 185.505 194.259 1.00 50.88  ? 480  GLU A CG  1 
ATOM   13013 C CD  . GLU B 2 480  ? 170.871 184.750 195.560 1.00 50.88  ? 480  GLU A CD  1 
ATOM   13014 O OE1 . GLU B 2 480  ? 170.736 185.372 196.635 1.00 50.88  ? 480  GLU A OE1 1 
ATOM   13015 O OE2 . GLU B 2 480  ? 171.154 183.535 195.508 1.00 50.88  ? 480  GLU A OE2 1 
ATOM   13016 N N   . ASP B 2 481  ? 172.755 187.166 192.093 1.00 57.39  ? 481  ASP A N   1 
ATOM   13017 C CA  . ASP B 2 481  ? 173.210 186.611 190.816 1.00 57.39  ? 481  ASP A CA  1 
ATOM   13018 C C   . ASP B 2 481  ? 172.783 187.484 189.640 1.00 57.39  ? 481  ASP A C   1 
ATOM   13019 O O   . ASP B 2 481  ? 172.397 186.986 188.580 1.00 57.39  ? 481  ASP A O   1 
ATOM   13020 C CB  . ASP B 2 481  ? 172.725 185.175 190.628 1.00 57.39  ? 481  ASP A CB  1 
ATOM   13021 C CG  . ASP B 2 481  ? 173.654 184.361 189.749 1.00 57.39  ? 481  ASP A CG  1 
ATOM   13022 O OD1 . ASP B 2 481  ? 174.441 184.971 188.994 1.00 57.39  ? 481  ASP A OD1 1 
ATOM   13023 O OD2 . ASP B 2 481  ? 173.601 183.114 189.811 1.00 57.39  ? 481  ASP A OD2 1 
ATOM   13024 N N   . VAL B 2 482  ? 172.862 188.796 189.823 1.00 55.67  ? 482  VAL A N   1 
ATOM   13025 C CA  . VAL B 2 482  ? 172.536 189.758 188.780 1.00 55.67  ? 482  VAL A CA  1 
ATOM   13026 C C   . VAL B 2 482  ? 173.820 190.131 188.053 1.00 55.67  ? 482  VAL A C   1 
ATOM   13027 O O   . VAL B 2 482  ? 174.862 190.362 188.680 1.00 55.67  ? 482  VAL A O   1 
ATOM   13028 C CB  . VAL B 2 482  ? 171.806 190.984 189.365 1.00 55.67  ? 482  VAL A CB  1 
ATOM   13029 C CG1 . VAL B 2 482  ? 172.757 192.021 189.882 1.00 55.67  ? 482  VAL A CG1 1 
ATOM   13030 C CG2 . VAL B 2 482  ? 170.927 191.614 188.316 1.00 55.67  ? 482  VAL A CG2 1 
ATOM   13031 N N   . THR B 2 483  ? 173.773 190.095 186.724 1.00 56.85  ? 483  THR A N   1 
ATOM   13032 C CA  . THR B 2 483  ? 174.930 190.385 185.889 1.00 56.85  ? 483  THR A CA  1 
ATOM   13033 C C   . THR B 2 483  ? 174.634 191.627 185.067 1.00 56.85  ? 483  THR A C   1 
ATOM   13034 O O   . THR B 2 483  ? 173.651 191.656 184.322 1.00 56.85  ? 483  THR A O   1 
ATOM   13035 C CB  . THR B 2 483  ? 175.262 189.203 184.979 1.00 56.85  ? 483  THR A CB  1 
ATOM   13036 O OG1 . THR B 2 483  ? 175.426 188.019 185.770 1.00 56.85  ? 483  THR A OG1 1 
ATOM   13037 C CG2 . THR B 2 483  ? 176.543 189.478 184.217 1.00 56.85  ? 483  THR A CG2 1 
ATOM   13038 N N   . SER B 2 484  ? 175.489 192.636 185.176 1.00 56.88  ? 484  SER A N   1 
ATOM   13039 C CA  . SER B 2 484  ? 175.203 193.954 184.630 1.00 56.88  ? 484  SER A CA  1 
ATOM   13040 C C   . SER B 2 484  ? 176.215 194.335 183.560 1.00 56.88  ? 484  SER A C   1 
ATOM   13041 O O   . SER B 2 484  ? 177.396 193.987 183.652 1.00 56.88  ? 484  SER A O   1 
ATOM   13042 C CB  . SER B 2 484  ? 175.209 195.004 185.738 1.00 56.88  ? 484  SER A CB  1 
ATOM   13043 O OG  . SER B 2 484  ? 176.440 195.708 185.765 1.00 56.88  ? 484  SER A OG  1 
ATOM   13044 N N   . THR B 2 485  ? 175.739 195.060 182.548 1.00 54.28  ? 485  THR A N   1 
ATOM   13045 C CA  . THR B 2 485  ? 176.568 195.536 181.446 1.00 54.28  ? 485  THR A CA  1 
ATOM   13046 C C   . THR B 2 485  ? 176.121 196.940 181.082 1.00 54.28  ? 485  THR A C   1 
ATOM   13047 O O   . THR B 2 485  ? 174.960 197.142 180.712 1.00 54.28  ? 485  THR A O   1 
ATOM   13048 C CB  . THR B 2 485  ? 176.451 194.622 180.224 1.00 54.28  ? 485  THR A CB  1 
ATOM   13049 O OG1 . THR B 2 485  ? 175.070 194.473 179.871 1.00 54.28  ? 485  THR A OG1 1 
ATOM   13050 C CG2 . THR B 2 485  ? 177.014 193.262 180.532 1.00 54.28  ? 485  THR A CG2 1 
ATOM   13051 N N   . ASP B 2 486  ? 177.029 197.904 181.194 1.00 56.38  ? 486  ASP A N   1 
ATOM   13052 C CA  . ASP B 2 486  ? 176.798 199.299 180.835 1.00 56.38  ? 486  ASP A CA  1 
ATOM   13053 C C   . ASP B 2 486  ? 175.689 199.953 181.651 1.00 56.38  ? 486  ASP A C   1 
ATOM   13054 O O   . ASP B 2 486  ? 175.230 201.047 181.296 1.00 56.38  ? 486  ASP A O   1 
ATOM   13055 C CB  . ASP B 2 486  ? 176.497 199.450 179.339 1.00 56.38  ? 486  ASP A CB  1 
ATOM   13056 C CG  . ASP B 2 486  ? 177.007 200.756 178.772 1.00 56.38  ? 486  ASP A CG  1 
ATOM   13057 O OD1 . ASP B 2 486  ? 177.454 201.613 179.564 1.00 56.38  ? 486  ASP A OD1 1 
ATOM   13058 O OD2 . ASP B 2 486  ? 176.970 200.924 177.537 1.00 56.38  ? 486  ASP A OD2 1 
ATOM   13059 N N   . THR B 2 487  ? 175.238 199.324 182.731 1.00 50.04  ? 487  THR A N   1 
ATOM   13060 C CA  . THR B 2 487  ? 174.269 199.953 183.609 1.00 50.04  ? 487  THR A CA  1 
ATOM   13061 C C   . THR B 2 487  ? 174.987 200.844 184.616 1.00 50.04  ? 487  THR A C   1 
ATOM   13062 O O   . THR B 2 487  ? 176.141 200.601 184.979 1.00 50.04  ? 487  THR A O   1 
ATOM   13063 C CB  . THR B 2 487  ? 173.422 198.905 184.334 1.00 50.04  ? 487  THR A CB  1 
ATOM   13064 O OG1 . THR B 2 487  ? 172.241 199.525 184.850 1.00 50.04  ? 487  THR A OG1 1 
ATOM   13065 C CG2 . THR B 2 487  ? 174.190 198.297 185.480 1.00 50.04  ? 487  THR A CG2 1 
ATOM   13066 N N   . TYR B 2 488  ? 174.296 201.896 185.058 1.00 49.59  ? 488  TYR A N   1 
ATOM   13067 C CA  . TYR B 2 488  ? 174.941 202.892 185.910 1.00 49.59  ? 488  TYR A CA  1 
ATOM   13068 C C   . TYR B 2 488  ? 173.888 203.521 186.811 1.00 49.59  ? 488  TYR A C   1 
ATOM   13069 O O   . TYR B 2 488  ? 172.878 204.034 186.320 1.00 49.59  ? 488  TYR A O   1 
ATOM   13070 C CB  . TYR B 2 488  ? 175.644 203.946 185.068 1.00 49.59  ? 488  TYR A CB  1 
ATOM   13071 C CG  . TYR B 2 488  ? 177.032 203.537 184.630 1.00 49.59  ? 488  TYR A CG  1 
ATOM   13072 C CD1 . TYR B 2 488  ? 178.130 203.739 185.456 1.00 49.59  ? 488  TYR A CD1 1 
ATOM   13073 C CD2 . TYR B 2 488  ? 177.240 202.927 183.401 1.00 49.59  ? 488  TYR A CD2 1 
ATOM   13074 C CE1 . TYR B 2 488  ? 179.397 203.358 185.063 1.00 49.59  ? 488  TYR A CE1 1 
ATOM   13075 C CE2 . TYR B 2 488  ? 178.503 202.542 183.002 1.00 49.59  ? 488  TYR A CE2 1 
ATOM   13076 C CZ  . TYR B 2 488  ? 179.578 202.760 183.836 1.00 49.59  ? 488  TYR A CZ  1 
ATOM   13077 O OH  . TYR B 2 488  ? 180.839 202.378 183.441 1.00 49.59  ? 488  TYR A OH  1 
ATOM   13078 N N   . PHE B 2 489  ? 174.126 203.476 188.118 1.00 46.86  ? 489  PHE A N   1 
ATOM   13079 C CA  . PHE B 2 489  ? 173.241 204.111 189.082 1.00 46.86  ? 489  PHE A CA  1 
ATOM   13080 C C   . PHE B 2 489  ? 173.684 205.546 189.339 1.00 46.86  ? 489  PHE A C   1 
ATOM   13081 O O   . PHE B 2 489  ? 174.875 205.820 189.508 1.00 46.86  ? 489  PHE A O   1 
ATOM   13082 C CB  . PHE B 2 489  ? 173.227 203.329 190.396 1.00 46.86  ? 489  PHE A CB  1 
ATOM   13083 C CG  . PHE B 2 489  ? 172.675 201.933 190.282 1.00 46.86  ? 489  PHE A CG  1 
ATOM   13084 C CD1 . PHE B 2 489  ? 173.297 200.977 189.502 1.00 46.86  ? 489  PHE A CD1 1 
ATOM   13085 C CD2 . PHE B 2 489  ? 171.534 201.574 190.980 1.00 46.86  ? 489  PHE A CD2 1 
ATOM   13086 C CE1 . PHE B 2 489  ? 172.787 199.702 189.404 1.00 46.86  ? 489  PHE A CE1 1 
ATOM   13087 C CE2 . PHE B 2 489  ? 171.020 200.296 190.890 1.00 46.86  ? 489  PHE A CE2 1 
ATOM   13088 C CZ  . PHE B 2 489  ? 171.649 199.359 190.101 1.00 46.86  ? 489  PHE A CZ  1 
ATOM   13089 N N   . LYS B 2 490  ? 172.719 206.465 189.374 1.00 43.91  ? 490  LYS A N   1 
ATOM   13090 C CA  . LYS B 2 490  ? 173.020 207.876 189.570 1.00 43.91  ? 490  LYS A CA  1 
ATOM   13091 C C   . LYS B 2 490  ? 172.036 208.485 190.560 1.00 43.91  ? 490  LYS A C   1 
ATOM   13092 O O   . LYS B 2 490  ? 170.825 208.281 190.457 1.00 43.91  ? 490  LYS A O   1 
ATOM   13093 C CB  . LYS B 2 490  ? 172.969 208.652 188.249 1.00 43.91  ? 490  LYS A CB  1 
ATOM   13094 C CG  . LYS B 2 490  ? 173.982 208.188 187.217 1.00 43.91  ? 490  LYS A CG  1 
ATOM   13095 C CD  . LYS B 2 490  ? 173.977 209.085 185.992 1.00 43.91  ? 490  LYS A CD  1 
ATOM   13096 C CE  . LYS B 2 490  ? 175.072 208.688 185.020 1.00 43.91  ? 490  LYS A CE  1 
ATOM   13097 N NZ  . LYS B 2 490  ? 175.234 209.687 183.932 1.00 43.91  ? 490  LYS A NZ  1 
ATOM   13098 N N   . ASN B 2 491  ? 172.581 209.280 191.486 1.00 45.15  ? 491  ASN A N   1 
ATOM   13099 C CA  . ASN B 2 491  ? 171.789 210.018 192.509 1.00 45.15  ? 491  ASN A CA  1 
ATOM   13100 C C   . ASN B 2 491  ? 170.755 209.137 193.212 1.00 45.15  ? 491  ASN A C   1 
ATOM   13101 O O   . ASN B 2 491  ? 169.781 209.699 193.733 1.00 45.15  ? 491  ASN A O   1 
ATOM   13102 C CB  . ASN B 2 491  ? 171.176 211.285 191.924 1.00 45.15  ? 491  ASN A CB  1 
ATOM   13103 C CG  . ASN B 2 491  ? 171.010 212.358 192.973 1.00 45.15  ? 491  ASN A CG  1 
ATOM   13104 O OD1 . ASN B 2 491  ? 171.991 212.832 193.538 1.00 45.15  ? 491  ASN A OD1 1 
ATOM   13105 N ND2 . ASN B 2 491  ? 169.773 212.737 193.242 1.00 45.15  ? 491  ASN A ND2 1 
ATOM   13106 N N   . CYS B 2 492  ? 170.984 207.827 193.302 1.00 42.04  ? 492  CYS A N   1 
ATOM   13107 C CA  . CYS B 2 492  ? 169.985 206.947 193.885 1.00 42.04  ? 492  CYS A CA  1 
ATOM   13108 C C   . CYS B 2 492  ? 170.175 206.828 195.391 1.00 42.04  ? 492  CYS A C   1 
ATOM   13109 O O   . CYS B 2 492  ? 171.298 206.761 195.896 1.00 42.04  ? 492  CYS A O   1 
ATOM   13110 C CB  . CYS B 2 492  ? 170.062 205.564 193.251 1.00 42.04  ? 492  CYS A CB  1 
ATOM   13111 S SG  . CYS B 2 492  ? 171.737 205.042 192.906 1.00 42.04  ? 492  CYS A SG  1 
ATOM   13112 N N   . THR B 2 493  ? 169.059 206.796 196.108 1.00 38.51  ? 493  THR A N   1 
ATOM   13113 C CA  . THR B 2 493  ? 169.042 206.502 197.532 1.00 38.51  ? 493  THR A CA  1 
ATOM   13114 C C   . THR B 2 493  ? 168.773 205.015 197.691 1.00 38.51  ? 493  THR A C   1 
ATOM   13115 O O   . THR B 2 493  ? 167.673 204.545 197.381 1.00 38.51  ? 493  THR A O   1 
ATOM   13116 C CB  . THR B 2 493  ? 167.978 207.325 198.257 1.00 38.51  ? 493  THR A CB  1 
ATOM   13117 O OG1 . THR B 2 493  ? 168.248 208.721 198.081 1.00 38.51  ? 493  THR A OG1 1 
ATOM   13118 C CG2 . THR B 2 493  ? 167.966 206.992 199.739 1.00 38.51  ? 493  THR A CG2 1 
ATOM   13119 N N   . ILE B 2 494  ? 169.770 204.279 198.163 1.00 38.58  ? 494  ILE A N   1 
ATOM   13120 C CA  . ILE B 2 494  ? 169.700 202.828 198.260 1.00 38.58  ? 494  ILE A CA  1 
ATOM   13121 C C   . ILE B 2 494  ? 169.684 202.486 199.741 1.00 38.58  ? 494  ILE A C   1 
ATOM   13122 O O   . ILE B 2 494  ? 170.647 202.777 200.461 1.00 38.58  ? 494  ILE A O   1 
ATOM   13123 C CB  . ILE B 2 494  ? 170.876 202.153 197.546 1.00 38.58  ? 494  ILE A CB  1 
ATOM   13124 C CG1 . ILE B 2 494  ? 171.036 202.725 196.142 1.00 38.58  ? 494  ILE A CG1 1 
ATOM   13125 C CG2 . ILE B 2 494  ? 170.621 200.688 197.406 1.00 38.58  ? 494  ILE A CG2 1 
ATOM   13126 C CD1 . ILE B 2 494  ? 172.320 202.310 195.472 1.00 38.58  ? 494  ILE A CD1 1 
ATOM   13127 N N   . GLU B 2 495  ? 168.597 201.874 200.205 1.00 40.55  ? 495  GLU A N   1 
ATOM   13128 C CA  . GLU B 2 495  ? 168.366 201.698 201.632 1.00 40.55  ? 495  GLU A CA  1 
ATOM   13129 C C   . GLU B 2 495  ? 168.027 200.251 201.946 1.00 40.55  ? 495  GLU A C   1 
ATOM   13130 O O   . GLU B 2 495  ? 167.146 199.662 201.311 1.00 40.55  ? 495  GLU A O   1 
ATOM   13131 C CB  . GLU B 2 495  ? 167.243 202.620 202.115 1.00 40.55  ? 495  GLU A CB  1 
ATOM   13132 C CG  . GLU B 2 495  ? 166.709 202.283 203.491 1.00 40.55  ? 495  GLU A CG  1 
ATOM   13133 C CD  . GLU B 2 495  ? 165.764 203.345 204.019 1.00 40.55  ? 495  GLU A CD  1 
ATOM   13134 O OE1 . GLU B 2 495  ? 165.538 204.346 203.305 1.00 40.55  ? 495  GLU A OE1 1 
ATOM   13135 O OE2 . GLU B 2 495  ? 165.249 203.180 205.143 1.00 40.55  ? 495  GLU A OE2 1 
ATOM   13136 N N   . SER B 2 496  ? 168.736 199.682 202.925 1.00 40.59  ? 496  SER A N   1 
ATOM   13137 C CA  . SER B 2 496  ? 168.415 198.381 203.512 1.00 40.59  ? 496  SER A CA  1 
ATOM   13138 C C   . SER B 2 496  ? 168.509 197.239 202.504 1.00 40.59  ? 496  SER A C   1 
ATOM   13139 O O   . SER B 2 496  ? 167.835 196.221 202.655 1.00 40.59  ? 496  SER A O   1 
ATOM   13140 C CB  . SER B 2 496  ? 167.029 198.393 204.166 1.00 40.59  ? 496  SER A CB  1 
ATOM   13141 O OG  . SER B 2 496  ? 166.883 199.503 205.034 1.00 40.59  ? 496  SER A OG  1 
ATOM   13142 N N   . THR B 2 497  ? 169.352 197.381 201.490 1.00 42.57  ? 497  THR A N   1 
ATOM   13143 C CA  . THR B 2 497  ? 169.464 196.389 200.432 1.00 42.57  ? 497  THR A CA  1 
ATOM   13144 C C   . THR B 2 497  ? 170.552 195.376 200.754 1.00 42.57  ? 497  THR A C   1 
ATOM   13145 O O   . THR B 2 497  ? 171.365 195.568 201.659 1.00 42.57  ? 497  THR A O   1 
ATOM   13146 C CB  . THR B 2 497  ? 169.790 197.050 199.100 1.00 42.57  ? 497  THR A CB  1 
ATOM   13147 O OG1 . THR B 2 497  ? 170.054 196.036 198.126 1.00 42.57  ? 497  THR A OG1 1 
ATOM   13148 C CG2 . THR B 2 497  ? 171.040 197.871 199.264 1.00 42.57  ? 497  THR A CG2 1 
ATOM   13149 N N   . ILE B 2 498  ? 170.563 194.287 199.986 1.00 43.79  ? 498  ILE A N   1 
ATOM   13150 C CA  . ILE B 2 498  ? 171.621 193.285 200.041 1.00 43.79  ? 498  ILE A CA  1 
ATOM   13151 C C   . ILE B 2 498  ? 172.093 193.009 198.622 1.00 43.79  ? 498  ILE A C   1 
ATOM   13152 O O   . ILE B 2 498  ? 171.286 192.696 197.742 1.00 43.79  ? 498  ILE A O   1 
ATOM   13153 C CB  . ILE B 2 498  ? 171.152 191.987 200.719 1.00 43.79  ? 498  ILE A CB  1 
ATOM   13154 C CG1 . ILE B 2 498  ? 170.519 192.283 202.079 1.00 43.79  ? 498  ILE A CG1 1 
ATOM   13155 C CG2 . ILE B 2 498  ? 172.313 191.024 200.873 1.00 43.79  ? 498  ILE A CG2 1 
ATOM   13156 C CD1 . ILE B 2 498  ? 169.926 191.065 202.745 1.00 43.79  ? 498  ILE A CD1 1 
ATOM   13157 N N   . PHE B 2 499  ? 173.399 193.122 198.403 1.00 47.18  ? 499  PHE A N   1 
ATOM   13158 C CA  . PHE B 2 499  ? 174.024 192.835 197.115 1.00 47.18  ? 499  PHE A CA  1 
ATOM   13159 C C   . PHE B 2 499  ? 174.884 191.585 197.296 1.00 47.18  ? 499  PHE A C   1 
ATOM   13160 O O   . PHE B 2 499  ? 176.076 191.674 197.594 1.00 47.18  ? 499  PHE A O   1 
ATOM   13161 C CB  . PHE B 2 499  ? 174.854 194.020 196.624 1.00 47.18  ? 499  PHE A CB  1 
ATOM   13162 C CG  . PHE B 2 499  ? 174.041 195.236 196.283 1.00 47.18  ? 499  PHE A CG  1 
ATOM   13163 C CD1 . PHE B 2 499  ? 173.123 195.207 195.248 1.00 47.18  ? 499  PHE A CD1 1 
ATOM   13164 C CD2 . PHE B 2 499  ? 174.196 196.408 196.997 1.00 47.18  ? 499  PHE A CD2 1 
ATOM   13165 C CE1 . PHE B 2 499  ? 172.378 196.325 194.934 1.00 47.18  ? 499  PHE A CE1 1 
ATOM   13166 C CE2 . PHE B 2 499  ? 173.454 197.527 196.685 1.00 47.18  ? 499  PHE A CE2 1 
ATOM   13167 C CZ  . PHE B 2 499  ? 172.544 197.484 195.654 1.00 47.18  ? 499  PHE A CZ  1 
ATOM   13168 N N   . TYR B 2 500  ? 174.274 190.421 197.110 1.00 53.09  ? 500  TYR A N   1 
ATOM   13169 C CA  . TYR B 2 500  ? 174.944 189.140 197.298 1.00 53.09  ? 500  TYR A CA  1 
ATOM   13170 C C   . TYR B 2 500  ? 175.151 188.471 195.948 1.00 53.09  ? 500  TYR A C   1 
ATOM   13171 O O   . TYR B 2 500  ? 174.203 188.344 195.164 1.00 53.09  ? 500  TYR A O   1 
ATOM   13172 C CB  . TYR B 2 500  ? 174.135 188.226 198.220 1.00 53.09  ? 500  TYR A CB  1 
ATOM   13173 C CG  . TYR B 2 500  ? 174.713 186.834 198.371 1.00 53.09  ? 500  TYR A CG  1 
ATOM   13174 C CD1 . TYR B 2 500  ? 176.086 186.632 198.449 1.00 53.09  ? 500  TYR A CD1 1 
ATOM   13175 C CD2 . TYR B 2 500  ? 173.886 185.723 198.429 1.00 53.09  ? 500  TYR A CD2 1 
ATOM   13176 C CE1 . TYR B 2 500  ? 176.616 185.364 198.582 1.00 53.09  ? 500  TYR A CE1 1 
ATOM   13177 C CE2 . TYR B 2 500  ? 174.408 184.452 198.564 1.00 53.09  ? 500  TYR A CE2 1 
ATOM   13178 C CZ  . TYR B 2 500  ? 175.774 184.278 198.639 1.00 53.09  ? 500  TYR A CZ  1 
ATOM   13179 O OH  . TYR B 2 500  ? 176.294 183.014 198.772 1.00 53.09  ? 500  TYR A OH  1 
ATOM   13180 N N   . ASN B 2 501  ? 176.388 188.046 195.687 1.00 59.57  ? 501  ASN A N   1 
ATOM   13181 C CA  . ASN B 2 501  ? 176.751 187.339 194.460 1.00 59.57  ? 501  ASN A CA  1 
ATOM   13182 C C   . ASN B 2 501  ? 176.381 188.195 193.247 1.00 59.57  ? 501  ASN A C   1 
ATOM   13183 O O   . ASN B 2 501  ? 175.459 187.896 192.490 1.00 59.57  ? 501  ASN A O   1 
ATOM   13184 C CB  . ASN B 2 501  ? 176.084 185.953 194.423 1.00 59.57  ? 501  ASN A CB  1 
ATOM   13185 C CG  . ASN B 2 501  ? 176.347 185.186 193.130 1.00 59.57  ? 501  ASN A CG  1 
ATOM   13186 O OD1 . ASN B 2 501  ? 177.014 185.668 192.217 1.00 59.57  ? 501  ASN A OD1 1 
ATOM   13187 N ND2 . ASN B 2 501  ? 175.810 183.975 193.054 1.00 59.57  ? 501  ASN A ND2 1 
ATOM   13188 N N   . THR B 2 502  ? 177.096 189.304 193.105 1.00 58.93  ? 502  THR A N   1 
ATOM   13189 C CA  . THR B 2 502  ? 176.840 190.268 192.048 1.00 58.93  ? 502  THR A CA  1 
ATOM   13190 C C   . THR B 2 502  ? 178.155 190.833 191.534 1.00 58.93  ? 502  THR A C   1 
ATOM   13191 O O   . THR B 2 502  ? 179.204 190.697 192.167 1.00 58.93  ? 502  THR A O   1 
ATOM   13192 C CB  . THR B 2 502  ? 175.939 191.408 192.538 1.00 58.93  ? 502  THR A CB  1 
ATOM   13193 O OG1 . THR B 2 502  ? 175.452 192.146 191.413 1.00 58.93  ? 502  THR A OG1 1 
ATOM   13194 C CG2 . THR B 2 502  ? 176.712 192.338 193.453 1.00 58.93  ? 502  THR A CG2 1 
ATOM   13195 N N   . ASP B 2 503  ? 178.091 191.458 190.359 1.00 57.59  ? 503  ASP A N   1 
ATOM   13196 C CA  . ASP B 2 503  ? 179.233 192.169 189.797 1.00 57.59  ? 503  ASP A CA  1 
ATOM   13197 C C   . ASP B 2 503  ? 179.014 193.675 189.757 1.00 57.59  ? 503  ASP A C   1 
ATOM   13198 O O   . ASP B 2 503  ? 179.795 194.389 189.121 1.00 57.59  ? 503  ASP A O   1 
ATOM   13199 C CB  . ASP B 2 503  ? 179.553 191.647 188.398 1.00 57.59  ? 503  ASP A CB  1 
ATOM   13200 C CG  . ASP B 2 503  ? 178.383 191.769 187.455 1.00 57.59  ? 503  ASP A CG  1 
ATOM   13201 O OD1 . ASP B 2 503  ? 178.165 192.872 186.911 1.00 57.59  ? 503  ASP A OD1 1 
ATOM   13202 O OD2 . ASP B 2 503  ? 177.683 190.758 187.259 1.00 57.59  ? 503  ASP A OD2 1 
ATOM   13203 N N   . LEU B 2 504  ? 177.972 194.171 190.421 1.00 57.02  ? 504  LEU A N   1 
ATOM   13204 C CA  . LEU B 2 504  ? 177.714 195.607 190.511 1.00 57.02  ? 504  LEU A CA  1 
ATOM   13205 C C   . LEU B 2 504  ? 178.728 196.212 191.476 1.00 57.02  ? 504  LEU A C   1 
ATOM   13206 O O   . LEU B 2 504  ? 178.475 196.412 192.665 1.00 57.02  ? 504  LEU A O   1 
ATOM   13207 C CB  . LEU B 2 504  ? 176.281 195.871 190.956 1.00 57.02  ? 504  LEU A CB  1 
ATOM   13208 C CG  . LEU B 2 504  ? 175.281 195.967 189.806 1.00 57.02  ? 504  LEU A CG  1 
ATOM   13209 C CD1 . LEU B 2 504  ? 174.967 194.600 189.270 1.00 57.02  ? 504  LEU A CD1 1 
ATOM   13210 C CD2 . LEU B 2 504  ? 174.014 196.640 190.280 1.00 57.02  ? 504  LEU A CD2 1 
ATOM   13211 N N   . TYR B 2 505  ? 179.907 196.506 190.936 1.00 60.73  ? 505  TYR A N   1 
ATOM   13212 C CA  . TYR B 2 505  ? 181.011 197.008 191.734 1.00 60.73  ? 505  TYR A CA  1 
ATOM   13213 C C   . TYR B 2 505  ? 180.754 198.461 192.131 1.00 60.73  ? 505  TYR A C   1 
ATOM   13214 O O   . TYR B 2 505  ? 179.701 199.041 191.850 1.00 60.73  ? 505  TYR A O   1 
ATOM   13215 C CB  . TYR B 2 505  ? 182.318 196.874 190.959 1.00 60.73  ? 505  TYR A CB  1 
ATOM   13216 C CG  . TYR B 2 505  ? 182.630 195.458 190.528 1.00 60.73  ? 505  TYR A CG  1 
ATOM   13217 C CD1 . TYR B 2 505  ? 182.199 194.371 191.275 1.00 60.73  ? 505  TYR A CD1 1 
ATOM   13218 C CD2 . TYR B 2 505  ? 183.353 195.208 189.371 1.00 60.73  ? 505  TYR A CD2 1 
ATOM   13219 C CE1 . TYR B 2 505  ? 182.480 193.077 190.884 1.00 60.73  ? 505  TYR A CE1 1 
ATOM   13220 C CE2 . TYR B 2 505  ? 183.639 193.918 188.972 1.00 60.73  ? 505  TYR A CE2 1 
ATOM   13221 C CZ  . TYR B 2 505  ? 183.199 192.857 189.732 1.00 60.73  ? 505  TYR A CZ  1 
ATOM   13222 O OH  . TYR B 2 505  ? 183.481 191.568 189.340 1.00 60.73  ? 505  TYR A OH  1 
ATOM   13223 N N   . GLU B 2 506  ? 181.738 199.055 192.807 1.00 60.93  ? 506  GLU A N   1 
ATOM   13224 C CA  . GLU B 2 506  ? 181.594 200.433 193.265 1.00 60.93  ? 506  GLU A CA  1 
ATOM   13225 C C   . GLU B 2 506  ? 181.535 201.404 192.092 1.00 60.93  ? 506  GLU A C   1 
ATOM   13226 O O   . GLU B 2 506  ? 180.772 202.377 192.127 1.00 60.93  ? 506  GLU A O   1 
ATOM   13227 C CB  . GLU B 2 506  ? 182.740 200.788 194.214 1.00 60.93  ? 506  GLU A CB  1 
ATOM   13228 C CG  . GLU B 2 506  ? 182.604 202.135 194.922 1.00 60.93  ? 506  GLU A CG  1 
ATOM   13229 C CD  . GLU B 2 506  ? 183.005 203.316 194.056 1.00 60.93  ? 506  GLU A CD  1 
ATOM   13230 O OE1 . GLU B 2 506  ? 183.836 203.129 193.144 1.00 60.93  ? 506  GLU A OE1 1 
ATOM   13231 O OE2 . GLU B 2 506  ? 182.487 204.427 194.289 1.00 60.93  ? 506  GLU A OE2 1 
ATOM   13232 N N   . HIS B 2 507  ? 182.329 201.159 191.048 1.00 57.44  ? 507  HIS A N   1 
ATOM   13233 C CA  . HIS B 2 507  ? 182.409 202.102 189.937 1.00 57.44  ? 507  HIS A CA  1 
ATOM   13234 C C   . HIS B 2 507  ? 181.090 202.249 189.188 1.00 57.44  ? 507  HIS A C   1 
ATOM   13235 O O   . HIS B 2 507  ? 180.917 203.227 188.457 1.00 57.44  ? 507  HIS A O   1 
ATOM   13236 C CB  . HIS B 2 507  ? 183.509 201.681 188.964 1.00 57.44  ? 507  HIS A CB  1 
ATOM   13237 C CG  . HIS B 2 507  ? 183.184 200.452 188.176 1.00 57.44  ? 507  HIS A CG  1 
ATOM   13238 N ND1 . HIS B 2 507  ? 183.480 199.180 188.620 1.00 57.44  ? 507  HIS A ND1 1 
ATOM   13239 C CD2 . HIS B 2 507  ? 182.590 200.298 186.969 1.00 57.44  ? 507  HIS A CD2 1 
ATOM   13240 C CE1 . HIS B 2 507  ? 183.081 198.298 187.722 1.00 57.44  ? 507  HIS A CE1 1 
ATOM   13241 N NE2 . HIS B 2 507  ? 182.537 198.950 186.710 1.00 57.44  ? 507  HIS A NE2 1 
ATOM   13242 N N   . LYS B 2 508  ? 180.160 201.310 189.356 1.00 54.69  ? 508  LYS A N   1 
ATOM   13243 C CA  . LYS B 2 508  ? 178.852 201.414 188.725 1.00 54.69  ? 508  LYS A CA  1 
ATOM   13244 C C   . LYS B 2 508  ? 177.905 202.332 189.483 1.00 54.69  ? 508  LYS A C   1 
ATOM   13245 O O   . LYS B 2 508  ? 176.785 202.559 189.017 1.00 54.69  ? 508  LYS A O   1 
ATOM   13246 C CB  . LYS B 2 508  ? 178.220 200.028 188.582 1.00 54.69  ? 508  LYS A CB  1 
ATOM   13247 C CG  . LYS B 2 508  ? 179.112 199.016 187.891 1.00 54.69  ? 508  LYS A CG  1 
ATOM   13248 C CD  . LYS B 2 508  ? 178.354 198.259 186.813 1.00 54.69  ? 508  LYS A CD  1 
ATOM   13249 C CE  . LYS B 2 508  ? 179.297 197.439 185.950 1.00 54.69  ? 508  LYS A CE  1 
ATOM   13250 N NZ  . LYS B 2 508  ? 179.155 195.980 186.200 1.00 54.69  ? 508  LYS A NZ  1 
ATOM   13251 N N   . PHE B 2 509  ? 178.320 202.859 190.631 1.00 51.06  ? 509  PHE A N   1 
ATOM   13252 C CA  . PHE B 2 509  ? 177.512 203.769 191.429 1.00 51.06  ? 509  PHE A CA  1 
ATOM   13253 C C   . PHE B 2 509  ? 178.127 205.162 191.375 1.00 51.06  ? 509  PHE A C   1 
ATOM   13254 O O   . PHE B 2 509  ? 179.317 205.327 191.663 1.00 51.06  ? 509  PHE A O   1 
ATOM   13255 C CB  . PHE B 2 509  ? 177.413 203.285 192.876 1.00 51.06  ? 509  PHE A CB  1 
ATOM   13256 C CG  . PHE B 2 509  ? 176.674 201.988 193.030 1.00 51.06  ? 509  PHE A CG  1 
ATOM   13257 C CD1 . PHE B 2 509  ? 175.294 201.948 192.965 1.00 51.06  ? 509  PHE A CD1 1 
ATOM   13258 C CD2 . PHE B 2 509  ? 177.364 200.806 193.238 1.00 51.06  ? 509  PHE A CD2 1 
ATOM   13259 C CE1 . PHE B 2 509  ? 174.615 200.757 193.106 1.00 51.06  ? 509  PHE A CE1 1 
ATOM   13260 C CE2 . PHE B 2 509  ? 176.690 199.612 193.379 1.00 51.06  ? 509  PHE A CE2 1 
ATOM   13261 C CZ  . PHE B 2 509  ? 175.313 199.588 193.313 1.00 51.06  ? 509  PHE A CZ  1 
ATOM   13262 N N   . ILE B 2 510  ? 177.319 206.153 191.011 1.00 46.82  ? 510  ILE A N   1 
ATOM   13263 C CA  . ILE B 2 510  ? 177.780 207.527 190.842 1.00 46.82  ? 510  ILE A CA  1 
ATOM   13264 C C   . ILE B 2 510  ? 176.932 208.431 191.722 1.00 46.82  ? 510  ILE A C   1 
ATOM   13265 O O   . ILE B 2 510  ? 175.723 208.569 191.492 1.00 46.82  ? 510  ILE A O   1 
ATOM   13266 C CB  . ILE B 2 510  ? 177.707 207.975 189.375 1.00 46.82  ? 510  ILE A CB  1 
ATOM   13267 C CG1 . ILE B 2 510  ? 178.632 207.121 188.507 1.00 46.82  ? 510  ILE A CG1 1 
ATOM   13268 C CG2 . ILE B 2 510  ? 178.056 209.448 189.252 1.00 46.82  ? 510  ILE A CG2 1 
ATOM   13269 C CD1 . ILE B 2 510  ? 178.442 207.333 187.025 1.00 46.82  ? 510  ILE A CD1 1 
ATOM   13270 N N   . ASN B 2 511  ? 177.567 209.054 192.714 1.00 48.57  ? 511  ASN A N   1 
ATOM   13271 C CA  . ASN B 2 511  ? 176.908 210.007 193.610 1.00 48.57  ? 511  ASN A CA  1 
ATOM   13272 C C   . ASN B 2 511  ? 175.664 209.399 194.254 1.00 48.57  ? 511  ASN A C   1 
ATOM   13273 O O   . ASN B 2 511  ? 174.578 209.982 194.245 1.00 48.57  ? 511  ASN A O   1 
ATOM   13274 C CB  . ASN B 2 511  ? 176.561 211.299 192.870 1.00 48.57  ? 511  ASN A CB  1 
ATOM   13275 C CG  . ASN B 2 511  ? 177.711 212.282 192.847 1.00 48.57  ? 511  ASN A CG  1 
ATOM   13276 O OD1 . ASN B 2 511  ? 178.874 211.894 192.737 1.00 48.57  ? 511  ASN A OD1 1 
ATOM   13277 N ND2 . ASN B 2 511  ? 177.392 213.567 192.950 1.00 48.57  ? 511  ASN A ND2 1 
ATOM   13278 N N   . CYS B 2 512  ? 175.831 208.212 194.824 1.00 44.77  ? 512  CYS A N   1 
ATOM   13279 C CA  . CYS B 2 512  ? 174.735 207.484 195.446 1.00 44.77  ? 512  CYS A CA  1 
ATOM   13280 C C   . CYS B 2 512  ? 174.928 207.422 196.955 1.00 44.77  ? 512  CYS A C   1 
ATOM   13281 O O   . CYS B 2 512  ? 176.049 207.280 197.449 1.00 44.77  ? 512  CYS A O   1 
ATOM   13282 C CB  . CYS B 2 512  ? 174.625 206.069 194.880 1.00 44.77  ? 512  CYS A CB  1 
ATOM   13283 S SG  . CYS B 2 512  ? 175.138 205.926 193.161 1.00 44.77  ? 512  CYS A SG  1 
ATOM   13284 N N   . ARG B 2 513  ? 173.819 207.530 197.679 1.00 43.45  ? 513  ARG A N   1 
ATOM   13285 C CA  . ARG B 2 513  ? 173.816 207.491 199.134 1.00 43.45  ? 513  ARG A CA  1 
ATOM   13286 C C   . ARG B 2 513  ? 173.246 206.157 199.590 1.00 43.45  ? 513  ARG A C   1 
ATOM   13287 O O   . ARG B 2 513  ? 172.078 205.856 199.325 1.00 43.45  ? 513  ARG A O   1 
ATOM   13288 C CB  . ARG B 2 513  ? 172.992 208.640 199.712 1.00 43.45  ? 513  ARG A CB  1 
ATOM   13289 C CG  . ARG B 2 513  ? 173.269 209.988 199.081 1.00 43.45  ? 513  ARG A CG  1 
ATOM   13290 C CD  . ARG B 2 513  ? 172.297 211.037 199.598 1.00 43.45  ? 513  ARG A CD  1 
ATOM   13291 N NE  . ARG B 2 513  ? 171.034 211.016 198.873 1.00 43.45  ? 513  ARG A NE  1 
ATOM   13292 C CZ  . ARG B 2 513  ? 170.867 211.478 197.642 1.00 43.45  ? 513  ARG A CZ  1 
ATOM   13293 N NH1 . ARG B 2 513  ? 171.864 212.025 196.966 1.00 43.45  ? 513  ARG A NH1 1 
ATOM   13294 N NH2 . ARG B 2 513  ? 169.666 211.394 197.074 1.00 43.45  ? 513  ARG A NH2 1 
ATOM   13295 N N   . PHE B 2 514  ? 174.074 205.346 200.261 1.00 40.18  ? 514  PHE A N   1 
ATOM   13296 C CA  . PHE B 2 514  ? 173.610 204.104 200.857 1.00 40.18  ? 514  PHE A CA  1 
ATOM   13297 C C   . PHE B 2 514  ? 173.061 204.377 202.246 1.00 40.18  ? 514  PHE A C   1 
ATOM   13298 O O   . PHE B 2 514  ? 173.499 205.308 202.927 1.00 40.18  ? 514  PHE A O   1 
ATOM   13299 C CB  . PHE B 2 514  ? 174.736 203.075 200.940 1.00 40.18  ? 514  PHE A CB  1 
ATOM   13300 C CG  . PHE B 2 514  ? 175.279 202.661 199.610 1.00 40.18  ? 514  PHE A CG  1 
ATOM   13301 C CD1 . PHE B 2 514  ? 176.320 203.352 199.026 1.00 40.18  ? 514  PHE A CD1 1 
ATOM   13302 C CD2 . PHE B 2 514  ? 174.742 201.579 198.940 1.00 40.18  ? 514  PHE A CD2 1 
ATOM   13303 C CE1 . PHE B 2 514  ? 176.822 202.971 197.803 1.00 40.18  ? 514  PHE A CE1 1 
ATOM   13304 C CE2 . PHE B 2 514  ? 175.235 201.195 197.714 1.00 40.18  ? 514  PHE A CE2 1 
ATOM   13305 C CZ  . PHE B 2 514  ? 176.278 201.890 197.146 1.00 40.18  ? 514  PHE A CZ  1 
ATOM   13306 N N   . ILE B 2 515  ? 172.096 203.565 202.663 1.00 39.15  ? 515  ILE A N   1 
ATOM   13307 C CA  . ILE B 2 515  ? 171.492 203.671 203.984 1.00 39.15  ? 515  ILE A CA  1 
ATOM   13308 C C   . ILE B 2 515  ? 171.326 202.262 204.529 1.00 39.15  ? 515  ILE A C   1 
ATOM   13309 O O   . ILE B 2 515  ? 170.582 201.457 203.954 1.00 39.15  ? 515  ILE A O   1 
ATOM   13310 C CB  . ILE B 2 515  ? 170.142 204.399 203.953 1.00 39.15  ? 515  ILE A CB  1 
ATOM   13311 C CG1 . ILE B 2 515  ? 170.301 205.824 203.421 1.00 39.15  ? 515  ILE A CG1 1 
ATOM   13312 C CG2 . ILE B 2 515  ? 169.520 204.407 205.330 1.00 39.15  ? 515  ILE A CG2 1 
ATOM   13313 C CD1 . ILE B 2 515  ? 171.001 206.755 204.379 1.00 39.15  ? 515  ILE A CD1 1 
ATOM   13314 N N   . ASN B 2 516  ? 172.016 201.959 205.630 1.00 39.20  ? 516  ASN A N   1 
ATOM   13315 C CA  . ASN B 2 516  ? 171.843 200.696 206.351 1.00 39.20  ? 516  ASN A CA  1 
ATOM   13316 C C   . ASN B 2 516  ? 172.029 199.489 205.434 1.00 39.20  ? 516  ASN A C   1 
ATOM   13317 O O   . ASN B 2 516  ? 171.545 198.391 205.720 1.00 39.20  ? 516  ASN A O   1 
ATOM   13318 C CB  . ASN B 2 516  ? 170.470 200.650 207.031 1.00 39.20  ? 516  ASN A CB  1 
ATOM   13319 C CG  . ASN B 2 516  ? 170.460 201.323 208.393 1.00 39.20  ? 516  ASN A CG  1 
ATOM   13320 O OD1 . ASN B 2 516  ? 171.500 201.722 208.910 1.00 39.20  ? 516  ASN A OD1 1 
ATOM   13321 N ND2 . ASN B 2 516  ? 169.270 201.465 208.973 1.00 39.20  ? 516  ASN A ND2 1 
ATOM   13322 N N   . SER B 2 517  ? 172.736 199.680 204.321 1.00 41.05  ? 517  SER A N   1 
ATOM   13323 C CA  . SER B 2 517  ? 172.850 198.678 203.275 1.00 41.05  ? 517  SER A CA  1 
ATOM   13324 C C   . SER B 2 517  ? 174.000 197.723 203.571 1.00 41.05  ? 517  SER A C   1 
ATOM   13325 O O   . SER B 2 517  ? 174.664 197.809 204.603 1.00 41.05  ? 517  SER A O   1 
ATOM   13326 C CB  . SER B 2 517  ? 173.044 199.347 201.916 1.00 41.05  ? 517  SER A CB  1 
ATOM   13327 O OG  . SER B 2 517  ? 173.819 198.523 201.065 1.00 41.05  ? 517  SER A OG  1 
ATOM   13328 N N   . THR B 2 518  ? 174.241 196.800 202.641 1.00 46.26  ? 518  THR A N   1 
ATOM   13329 C CA  . THR B 2 518  ? 175.326 195.843 202.795 1.00 46.26  ? 518  THR A CA  1 
ATOM   13330 C C   . THR B 2 518  ? 175.827 195.408 201.426 1.00 46.26  ? 518  THR A C   1 
ATOM   13331 O O   . THR B 2 518  ? 175.154 195.591 200.409 1.00 46.26  ? 518  THR A O   1 
ATOM   13332 C CB  . THR B 2 518  ? 174.901 194.617 203.610 1.00 46.26  ? 518  THR A CB  1 
ATOM   13333 O OG1 . THR B 2 518  ? 176.013 193.726 203.745 1.00 46.26  ? 518  THR A OG1 1 
ATOM   13334 C CG2 . THR B 2 518  ? 173.772 193.888 202.918 1.00 46.26  ? 518  THR A CG2 1 
ATOM   13335 N N   . PHE B 2 519  ? 177.009 194.832 201.426 1.00 50.11  ? 519  PHE A N   1 
ATOM   13336 C CA  . PHE B 2 519  ? 177.659 194.358 200.204 1.00 50.11  ? 519  PHE A CA  1 
ATOM   13337 C C   . PHE B 2 519  ? 178.340 193.033 200.527 1.00 50.11  ? 519  PHE A C   1 
ATOM   13338 O O   . PHE B 2 519  ? 179.434 193.015 201.098 1.00 50.11  ? 519  PHE A O   1 
ATOM   13339 C CB  . PHE B 2 519  ? 178.662 195.375 199.681 1.00 50.11  ? 519  PHE A CB  1 
ATOM   13340 C CG  . PHE B 2 519  ? 178.092 196.331 198.682 1.00 50.11  ? 519  PHE A CG  1 
ATOM   13341 C CD1 . PHE B 2 519  ? 177.369 197.433 199.095 1.00 50.11  ? 519  PHE A CD1 1 
ATOM   13342 C CD2 . PHE B 2 519  ? 178.291 196.135 197.329 1.00 50.11  ? 519  PHE A CD2 1 
ATOM   13343 C CE1 . PHE B 2 519  ? 176.848 198.316 198.179 1.00 50.11  ? 519  PHE A CE1 1 
ATOM   13344 C CE2 . PHE B 2 519  ? 177.772 197.017 196.408 1.00 50.11  ? 519  PHE A CE2 1 
ATOM   13345 C CZ  . PHE B 2 519  ? 177.052 198.110 196.834 1.00 50.11  ? 519  PHE A CZ  1 
ATOM   13346 N N   . LEU B 2 520  ? 177.666 191.941 200.186 1.00 53.40  ? 520  LEU A N   1 
ATOM   13347 C CA  . LEU B 2 520  ? 178.212 190.620 200.574 1.00 53.40  ? 520  LEU A CA  1 
ATOM   13348 C C   . LEU B 2 520  ? 179.039 190.063 199.423 1.00 53.40  ? 520  LEU A C   1 
ATOM   13349 O O   . LEU B 2 520  ? 179.608 190.869 198.674 1.00 53.40  ? 520  LEU A O   1 
ATOM   13350 C CB  . LEU B 2 520  ? 177.046 189.695 200.918 1.00 53.40  ? 520  LEU A CB  1 
ATOM   13351 C CG  . LEU B 2 520  ? 176.153 190.171 202.060 1.00 53.40  ? 520  LEU A CG  1 
ATOM   13352 C CD1 . LEU B 2 520  ? 175.177 189.082 202.474 1.00 53.40  ? 520  LEU A CD1 1 
ATOM   13353 C CD2 . LEU B 2 520  ? 176.988 190.612 203.251 1.00 53.40  ? 520  LEU A CD2 1 
ATOM   13354 N N   . GLU B 2 521  ? 179.089 188.737 199.292 1.00 60.16  ? 521  GLU A N   1 
ATOM   13355 C CA  . GLU B 2 521  ? 179.959 188.125 198.257 1.00 60.16  ? 521  GLU A CA  1 
ATOM   13356 C C   . GLU B 2 521  ? 179.653 188.776 196.913 1.00 60.16  ? 521  GLU A C   1 
ATOM   13357 O O   . GLU B 2 521  ? 178.484 189.074 196.661 1.00 60.16  ? 521  GLU A O   1 
ATOM   13358 C CB  . GLU B 2 521  ? 179.718 186.622 198.203 1.00 60.16  ? 521  GLU A CB  1 
ATOM   13359 C CG  . GLU B 2 521  ? 179.878 185.955 199.555 1.00 60.16  ? 521  GLU A CG  1 
ATOM   13360 C CD  . GLU B 2 521  ? 181.092 186.415 200.346 1.00 60.16  ? 521  GLU A CD  1 
ATOM   13361 O OE1 . GLU B 2 521  ? 182.222 186.260 199.839 1.00 60.16  ? 521  GLU A OE1 1 
ATOM   13362 O OE2 . GLU B 2 521  ? 180.904 186.927 201.465 1.00 60.16  ? 521  GLU A OE2 1 
ATOM   13363 N N   . GLN B 2 522  ? 180.680 189.019 196.106 1.00 59.61  ? 522  GLN A N   1 
ATOM   13364 C CA  . GLN B 2 522  ? 180.461 189.709 194.812 1.00 59.61  ? 522  GLN A CA  1 
ATOM   13365 C C   . GLN B 2 522  ? 181.169 188.938 193.699 1.00 59.61  ? 522  GLN A C   1 
ATOM   13366 O O   . GLN B 2 522  ? 182.378 188.702 193.827 1.00 59.61  ? 522  GLN A O   1 
ATOM   13367 C CB  . GLN B 2 522  ? 180.947 191.156 194.878 1.00 59.61  ? 522  GLN A CB  1 
ATOM   13368 C CG  . GLN B 2 522  ? 179.898 192.120 195.404 1.00 59.61  ? 522  GLN A CG  1 
ATOM   13369 C CD  . GLN B 2 522  ? 180.277 193.556 195.144 1.00 59.61  ? 522  GLN A CD  1 
ATOM   13370 O OE1 . GLN B 2 522  ? 181.330 194.026 195.565 1.00 59.61  ? 522  GLN A OE1 1 
ATOM   13371 N NE2 . GLN B 2 522  ? 179.418 194.267 194.431 1.00 59.61  ? 522  GLN A NE2 1 
ATOM   13372 N N   . LYS B 2 523  ? 180.436 188.587 192.641 1.00 62.61  ? 523  LYS A N   1 
ATOM   13373 C CA  . LYS B 2 523  ? 181.023 187.855 191.491 1.00 62.61  ? 523  LYS A CA  1 
ATOM   13374 C C   . LYS B 2 523  ? 182.342 188.519 191.104 1.00 62.61  ? 523  LYS A C   1 
ATOM   13375 O O   . LYS B 2 523  ? 182.382 189.762 191.036 1.00 62.61  ? 523  LYS A O   1 
ATOM   13376 C CB  . LYS B 2 523  ? 180.074 187.879 190.290 1.00 62.61  ? 523  LYS A CB  1 
ATOM   13377 C CG  . LYS B 2 523  ? 178.622 187.548 190.590 1.00 62.61  ? 523  LYS A CG  1 
ATOM   13378 C CD  . LYS B 2 523  ? 177.782 187.401 189.344 1.00 62.61  ? 523  LYS A CD  1 
ATOM   13379 C CE  . LYS B 2 523  ? 178.238 186.250 188.474 1.00 62.61  ? 523  LYS A CE  1 
ATOM   13380 N NZ  . LYS B 2 523  ? 177.464 186.174 187.213 1.00 62.61  ? 523  LYS A NZ  1 
ATOM   13381 N N   . GLU B 2 524  ? 183.371 187.711 190.854 1.00 69.65  ? 524  GLU A N   1 
ATOM   13382 C CA  . GLU B 2 524  ? 184.706 188.259 190.511 1.00 69.65  ? 524  GLU A CA  1 
ATOM   13383 C C   . GLU B 2 524  ? 184.782 188.509 189.005 1.00 69.65  ? 524  GLU A C   1 
ATOM   13384 O O   . GLU B 2 524  ? 184.372 187.616 188.240 1.00 69.65  ? 524  GLU A O   1 
ATOM   13385 C CB  . GLU B 2 524  ? 185.802 187.291 190.951 1.00 69.65  ? 524  GLU A CB  1 
ATOM   13386 C CG  . GLU B 2 524  ? 187.197 187.787 190.623 1.00 69.65  ? 524  GLU A CG  1 
ATOM   13387 C CD  . GLU B 2 524  ? 187.451 189.230 191.026 1.00 69.65  ? 524  GLU A CD  1 
ATOM   13388 O OE1 . GLU B 2 524  ? 187.337 189.534 192.228 1.00 69.65  ? 524  GLU A OE1 1 
ATOM   13389 O OE2 . GLU B 2 524  ? 187.755 190.046 190.134 1.00 69.65  ? 524  GLU A OE2 1 
ATOM   13390 N N   . GLY B 2 525  ? 185.286 189.680 188.607 1.00 72.36  ? 525  GLY A N   1 
ATOM   13391 C CA  . GLY B 2 525  ? 185.402 190.019 187.177 1.00 72.36  ? 525  GLY A CA  1 
ATOM   13392 C C   . GLY B 2 525  ? 184.066 190.477 186.629 1.00 72.36  ? 525  GLY A C   1 
ATOM   13393 O O   . GLY B 2 525  ? 183.031 190.026 187.149 1.00 72.36  ? 525  GLY A O   1 
ATOM   13394 N N   . CYS B 2 526  ? 184.075 191.346 185.620 1.00 76.00  ? 526  CYS A N   1 
ATOM   13395 C CA  . CYS B 2 526  ? 182.788 191.734 184.994 1.00 76.00  ? 526  CYS A CA  1 
ATOM   13396 C C   . CYS B 2 526  ? 182.327 190.603 184.078 1.00 76.00  ? 526  CYS A C   1 
ATOM   13397 O O   . CYS B 2 526  ? 183.180 189.814 183.629 1.00 76.00  ? 526  CYS A O   1 
ATOM   13398 C CB  . CYS B 2 526  ? 182.935 192.981 184.142 1.00 76.00  ? 526  CYS A CB  1 
ATOM   13399 S SG  . CYS B 2 526  ? 183.667 192.626 182.528 1.00 76.00  ? 526  CYS A SG  1 
ATOM   13400 N N   . HIS B 2 527  ? 181.025 190.542 183.813 1.00 68.68  ? 527  HIS A N   1 
ATOM   13401 C CA  . HIS B 2 527  ? 180.481 189.460 182.954 1.00 68.68  ? 527  HIS A CA  1 
ATOM   13402 C C   . HIS B 2 527  ? 179.617 190.100 181.867 1.00 68.68  ? 527  HIS A C   1 
ATOM   13403 O O   . HIS B 2 527  ? 178.856 191.039 182.170 1.00 68.68  ? 527  HIS A O   1 
ATOM   13404 C CB  . HIS B 2 527  ? 179.724 188.448 183.817 1.00 68.68  ? 527  HIS A CB  1 
ATOM   13405 C CG  . HIS B 2 527  ? 180.476 188.017 185.030 1.00 68.68  ? 527  HIS A CG  1 
ATOM   13406 N ND1 . HIS B 2 527  ? 181.673 187.339 184.966 1.00 68.68  ? 527  HIS A ND1 1 
ATOM   13407 C CD2 . HIS B 2 527  ? 180.202 188.163 186.331 1.00 68.68  ? 527  HIS A CD2 1 
ATOM   13408 C CE1 . HIS B 2 527  ? 182.100 187.090 186.194 1.00 68.68  ? 527  HIS A CE1 1 
ATOM   13409 N NE2 . HIS B 2 527  ? 181.221 187.581 187.040 1.00 68.68  ? 527  HIS A NE2 1 
ATOM   13410 N N   . MET B 2 528  ? 179.749 189.617 180.632 1.00 69.58  ? 528  MET A N   1 
ATOM   13411 C CA  . MET B 2 528  ? 178.941 190.156 179.510 1.00 69.58  ? 528  MET A CA  1 
ATOM   13412 C C   . MET B 2 528  ? 178.318 188.985 178.752 1.00 69.58  ? 528  MET A C   1 
ATOM   13413 O O   . MET B 2 528  ? 178.926 187.900 178.748 1.00 69.58  ? 528  MET A O   1 
ATOM   13414 C CB  . MET B 2 528  ? 179.804 190.965 178.538 1.00 69.58  ? 528  MET A CB  1 
ATOM   13415 C CG  . MET B 2 528  ? 181.208 190.426 178.351 1.00 69.58  ? 528  MET A CG  1 
ATOM   13416 S SD  . MET B 2 528  ? 182.359 190.978 179.635 1.00 69.58  ? 528  MET A SD  1 
ATOM   13417 C CE  . MET B 2 528  ? 183.041 189.409 180.166 1.00 69.58  ? 528  MET A CE  1 
ATOM   13418 N N   . ASP B 2 529  ? 177.152 189.196 178.144 1.00 63.34  ? 529  ASP A N   1 
ATOM   13419 C CA  . ASP B 2 529  ? 176.553 188.128 177.304 1.00 63.34  ? 529  ASP A CA  1 
ATOM   13420 C C   . ASP B 2 529  ? 177.305 188.135 175.974 1.00 63.34  ? 529  ASP A C   1 
ATOM   13421 O O   . ASP B 2 529  ? 176.761 188.676 174.997 1.00 63.34  ? 529  ASP A O   1 
ATOM   13422 C CB  . ASP B 2 529  ? 175.050 188.337 177.119 1.00 63.34  ? 529  ASP A CB  1 
ATOM   13423 C CG  . ASP B 2 529  ? 174.344 187.123 176.542 1.00 63.34  ? 529  ASP A CG  1 
ATOM   13424 O OD1 . ASP B 2 529  ? 175.031 186.119 176.272 1.00 63.34  ? 529  ASP A OD1 1 
ATOM   13425 O OD2 . ASP B 2 529  ? 173.112 187.188 176.380 1.00 63.34  ? 529  ASP A OD2 1 
ATOM   13426 N N   . LEU B 2 530  ? 178.506 187.553 175.940 1.00 62.59  ? 530  LEU A N   1 
ATOM   13427 C CA  . LEU B 2 530  ? 179.341 187.596 174.711 1.00 62.59  ? 530  LEU A CA  1 
ATOM   13428 C C   . LEU B 2 530  ? 178.530 187.088 173.516 1.00 62.59  ? 530  LEU A C   1 
ATOM   13429 O O   . LEU B 2 530  ? 178.815 187.527 172.389 1.00 62.59  ? 530  LEU A O   1 
ATOM   13430 C CB  . LEU B 2 530  ? 180.594 186.745 174.933 1.00 62.59  ? 530  LEU A CB  1 
ATOM   13431 C CG  . LEU B 2 530  ? 181.725 187.440 175.690 1.00 62.59  ? 530  LEU A CG  1 
ATOM   13432 C CD1 . LEU B 2 530  ? 182.969 186.568 175.728 1.00 62.59  ? 530  LEU A CD1 1 
ATOM   13433 C CD2 . LEU B 2 530  ? 182.042 188.788 175.059 1.00 62.59  ? 530  LEU A CD2 1 
ATOM   13434 N N   . GLU B 2 531  ? 177.558 186.209 173.754 1.00 63.48  ? 531  GLU A N   1 
ATOM   13435 C CA  . GLU B 2 531  ? 176.682 185.741 172.651 1.00 63.48  ? 531  GLU A CA  1 
ATOM   13436 C C   . GLU B 2 531  ? 176.127 186.965 171.918 1.00 63.48  ? 531  GLU A C   1 
ATOM   13437 O O   . GLU B 2 531  ? 176.102 186.949 170.674 1.00 63.48  ? 531  GLU A O   1 
ATOM   13438 C CB  . GLU B 2 531  ? 175.552 184.875 173.209 1.00 63.48  ? 531  GLU A CB  1 
ATOM   13439 C CG  . GLU B 2 531  ? 174.432 184.618 172.216 1.00 63.48  ? 531  GLU A CG  1 
ATOM   13440 C CD  . GLU B 2 531  ? 174.786 183.743 171.025 1.00 63.48  ? 531  GLU A CD  1 
ATOM   13441 O OE1 . GLU B 2 531  ? 175.938 183.266 170.954 1.00 63.48  ? 531  GLU A OE1 1 
ATOM   13442 O OE2 . GLU B 2 531  ? 173.907 183.543 170.164 1.00 63.48  ? 531  GLU A OE2 1 
ATOM   13443 N N   . GLN B 2 532  ? 175.710 187.987 172.665 1.00 63.40  ? 532  GLN A N   1 
ATOM   13444 C CA  . GLN B 2 532  ? 175.139 189.212 172.047 1.00 63.40  ? 532  GLN A CA  1 
ATOM   13445 C C   . GLN B 2 532  ? 176.216 190.298 171.972 1.00 63.40  ? 532  GLN A C   1 
ATOM   13446 O O   . GLN B 2 532  ? 175.882 191.421 171.551 1.00 63.40  ? 532  GLN A O   1 
ATOM   13447 C CB  . GLN B 2 532  ? 173.951 189.702 172.872 1.00 63.40  ? 532  GLN A CB  1 
ATOM   13448 C CG  . GLN B 2 532  ? 172.970 188.603 173.248 1.00 63.40  ? 532  GLN A CG  1 
ATOM   13449 C CD  . GLN B 2 532  ? 171.844 189.142 174.092 1.00 63.40  ? 532  GLN A CD  1 
ATOM   13450 O OE1 . GLN B 2 532  ? 172.059 189.702 175.165 1.00 63.40  ? 532  GLN A OE1 1 
ATOM   13451 N NE2 . GLN B 2 532  ? 170.624 188.983 173.606 1.00 63.40  ? 532  GLN A NE2 1 
ATOM   13452 N N   . ASP B 2 533  ? 177.448 189.980 172.379 1.00 62.93  ? 533  ASP A N   1 
ATOM   13453 C CA  . ASP B 2 533  ? 178.535 190.996 172.400 1.00 62.93  ? 533  ASP A CA  1 
ATOM   13454 C C   . ASP B 2 533  ? 179.671 190.559 171.470 1.00 62.93  ? 533  ASP A C   1 
ATOM   13455 O O   . ASP B 2 533  ? 180.839 190.797 171.816 1.00 62.93  ? 533  ASP A O   1 
ATOM   13456 C CB  . ASP B 2 533  ? 179.043 191.255 173.821 1.00 62.93  ? 533  ASP A CB  1 
ATOM   13457 C CG  . ASP B 2 533  ? 177.972 191.785 174.759 1.00 62.93  ? 533  ASP A CG  1 
ATOM   13458 O OD1 . ASP B 2 533  ? 177.321 192.785 174.398 1.00 62.93  ? 533  ASP A OD1 1 
ATOM   13459 O OD2 . ASP B 2 533  ? 177.787 191.184 175.834 1.00 62.93  ? 533  ASP A OD2 1 
ATOM   13460 N N   . ASN B 2 534  ? 179.336 189.935 170.341 1.00 57.54  ? 534  ASN A N   1 
ATOM   13461 C CA  . ASN B 2 534  ? 180.381 189.553 169.358 1.00 57.54  ? 534  ASN A CA  1 
ATOM   13462 C C   . ASN B 2 534  ? 180.317 190.511 168.165 1.00 57.54  ? 534  ASN A C   1 
ATOM   13463 O O   . ASN B 2 534  ? 179.242 190.614 167.549 1.00 57.54  ? 534  ASN A O   1 
ATOM   13464 C CB  . ASN B 2 534  ? 180.246 188.100 168.906 1.00 57.54  ? 534  ASN A CB  1 
ATOM   13465 C CG  . ASN B 2 534  ? 178.833 187.570 169.015 1.00 57.54  ? 534  ASN A CG  1 
ATOM   13466 O OD1 . ASN B 2 534  ? 177.897 188.163 168.484 1.00 57.54  ? 534  ASN A OD1 1 
ATOM   13467 N ND2 . ASN B 2 534  ? 178.667 186.459 169.713 1.00 57.54  ? 534  ASN A ND2 1 
ATOM   13468 N N   . ASP B 2 535  ? 181.432 191.171 167.851 1.00 50.12  ? 535  ASP A N   1 
ATOM   13469 C CA  . ASP B 2 535  ? 181.480 192.072 166.671 1.00 50.12  ? 535  ASP A CA  1 
ATOM   13470 C C   . ASP B 2 535  ? 181.739 191.209 165.436 1.00 50.12  ? 535  ASP A C   1 
ATOM   13471 O O   . ASP B 2 535  ? 182.352 191.721 164.483 1.00 50.12  ? 535  ASP A O   1 
ATOM   13472 C CB  . ASP B 2 535  ? 182.536 193.169 166.837 1.00 50.12  ? 535  ASP A CB  1 
ATOM   13473 C CG  . ASP B 2 535  ? 183.185 193.204 168.210 1.00 50.12  ? 535  ASP A CG  1 
ATOM   13474 O OD1 . ASP B 2 535  ? 183.840 192.208 168.576 1.00 50.12  ? 535  ASP A OD1 1 
ATOM   13475 O OD2 . ASP B 2 535  ? 183.034 194.229 168.902 1.00 50.12  ? 535  ASP A OD2 1 
ATOM   13476 N N   . PHE B 2 536  ? 181.276 189.955 165.455 1.00 44.32  ? 536  PHE A N   1 
ATOM   13477 C CA  . PHE B 2 536  ? 181.490 189.014 164.324 1.00 44.32  ? 536  PHE A CA  1 
ATOM   13478 C C   . PHE B 2 536  ? 181.238 189.741 162.999 1.00 44.32  ? 536  PHE A C   1 
ATOM   13479 O O   . PHE B 2 536  ? 182.006 189.531 162.040 1.00 44.32  ? 536  PHE A O   1 
ATOM   13480 C CB  . PHE B 2 536  ? 180.583 187.797 164.517 1.00 44.32  ? 536  PHE A CB  1 
ATOM   13481 C CG  . PHE B 2 536  ? 180.276 186.980 163.288 1.00 44.32  ? 536  PHE A CG  1 
ATOM   13482 C CD1 . PHE B 2 536  ? 181.285 186.364 162.568 1.00 44.32  ? 536  PHE A CD1 1 
ATOM   13483 C CD2 . PHE B 2 536  ? 178.967 186.803 162.870 1.00 44.32  ? 536  PHE A CD2 1 
ATOM   13484 C CE1 . PHE B 2 536  ? 180.993 185.606 161.446 1.00 44.32  ? 536  PHE A CE1 1 
ATOM   13485 C CE2 . PHE B 2 536  ? 178.676 186.042 161.750 1.00 44.32  ? 536  PHE A CE2 1 
ATOM   13486 C CZ  . PHE B 2 536  ? 179.689 185.444 161.039 1.00 44.32  ? 536  PHE A CZ  1 
ATOM   13487 N N   . LEU B 2 537  ? 180.206 190.585 162.958 1.00 39.58  ? 537  LEU A N   1 
ATOM   13488 C CA  . LEU B 2 537  ? 179.892 191.341 161.720 1.00 39.58  ? 537  LEU A CA  1 
ATOM   13489 C C   . LEU B 2 537  ? 181.141 192.080 161.226 1.00 39.58  ? 537  LEU A C   1 
ATOM   13490 O O   . LEU B 2 537  ? 181.437 191.956 160.031 1.00 39.58  ? 537  LEU A O   1 
ATOM   13491 C CB  . LEU B 2 537  ? 178.742 192.307 162.011 1.00 39.58  ? 537  LEU A CB  1 
ATOM   13492 C CG  . LEU B 2 537  ? 177.397 191.641 162.287 1.00 39.58  ? 537  LEU A CG  1 
ATOM   13493 C CD1 . LEU B 2 537  ? 176.265 192.649 162.185 1.00 39.58  ? 537  LEU A CD1 1 
ATOM   13494 C CD2 . LEU B 2 537  ? 177.165 190.483 161.329 1.00 39.58  ? 537  LEU A CD2 1 
ATOM   13495 N N   . ILE B 2 538  ? 181.859 192.801 162.097 1.00 38.33  ? 538  ILE A N   1 
ATOM   13496 C CA  . ILE B 2 538  ? 182.979 193.586 161.603 1.00 38.33  ? 538  ILE A CA  1 
ATOM   13497 C C   . ILE B 2 538  ? 183.975 192.734 160.829 1.00 38.33  ? 538  ILE A C   1 
ATOM   13498 O O   . ILE B 2 538  ? 184.614 193.249 159.899 1.00 38.33  ? 538  ILE A O   1 
ATOM   13499 C CB  . ILE B 2 538  ? 183.685 194.328 162.758 1.00 38.33  ? 538  ILE A CB  1 
ATOM   13500 C CG1 . ILE B 2 538  ? 182.674 195.170 163.533 1.00 38.33  ? 538  ILE A CG1 1 
ATOM   13501 C CG2 . ILE B 2 538  ? 184.792 195.221 162.239 1.00 38.33  ? 538  ILE A CG2 1 
ATOM   13502 C CD1 . ILE B 2 538  ? 183.293 196.047 164.602 1.00 38.33  ? 538  ILE A CD1 1 
ATOM   13503 N N   . TYR B 2 539  ? 184.105 191.449 161.153 1.00 39.28  ? 539  TYR A N   1 
ATOM   13504 C CA  . TYR B 2 539  ? 184.954 190.548 160.386 1.00 39.28  ? 539  TYR A CA  1 
ATOM   13505 C C   . TYR B 2 539  ? 184.230 189.974 159.180 1.00 39.28  ? 539  TYR A C   1 
ATOM   13506 O O   . TYR B 2 539  ? 184.840 189.797 158.119 1.00 39.28  ? 539  TYR A O   1 
ATOM   13507 C CB  . TYR B 2 539  ? 185.455 189.410 161.277 1.00 39.28  ? 539  TYR A CB  1 
ATOM   13508 C CG  . TYR B 2 539  ? 186.295 189.863 162.447 1.00 39.28  ? 539  TYR A CG  1 
ATOM   13509 C CD1 . TYR B 2 539  ? 186.942 191.088 162.431 1.00 39.28  ? 539  TYR A CD1 1 
ATOM   13510 C CD2 . TYR B 2 539  ? 186.437 189.066 163.571 1.00 39.28  ? 539  TYR A CD2 1 
ATOM   13511 C CE1 . TYR B 2 539  ? 187.709 191.504 163.501 1.00 39.28  ? 539  TYR A CE1 1 
ATOM   13512 C CE2 . TYR B 2 539  ? 187.201 189.475 164.645 1.00 39.28  ? 539  TYR A CE2 1 
ATOM   13513 C CZ  . TYR B 2 539  ? 187.834 190.693 164.606 1.00 39.28  ? 539  TYR A CZ  1 
ATOM   13514 O OH  . TYR B 2 539  ? 188.595 191.096 165.678 1.00 39.28  ? 539  TYR A OH  1 
ATOM   13515 N N   . LEU B 2 540  ? 182.940 189.675 159.322 1.00 35.57  ? 540  LEU A N   1 
ATOM   13516 C CA  . LEU B 2 540  ? 182.159 189.181 158.192 1.00 35.57  ? 540  LEU A CA  1 
ATOM   13517 C C   . LEU B 2 540  ? 182.031 190.253 157.114 1.00 35.57  ? 540  LEU A C   1 
ATOM   13518 O O   . LEU B 2 540  ? 182.121 189.956 155.916 1.00 35.57  ? 540  LEU A O   1 
ATOM   13519 C CB  . LEU B 2 540  ? 180.793 188.705 158.698 1.00 35.57  ? 540  LEU A CB  1 
ATOM   13520 C CG  . LEU B 2 540  ? 179.786 187.852 157.912 1.00 35.57  ? 540  LEU A CG  1 
ATOM   13521 C CD1 . LEU B 2 540  ? 178.510 187.705 158.734 1.00 35.57  ? 540  LEU A CD1 1 
ATOM   13522 C CD2 . LEU B 2 540  ? 179.436 188.394 156.540 1.00 35.57  ? 540  LEU A CD2 1 
ATOM   13523 N N   . VAL B 2 541  ? 181.834 191.510 157.522 1.00 33.28  ? 541  VAL A N   1 
ATOM   13524 C CA  . VAL B 2 541  ? 181.745 192.599 156.553 1.00 33.28  ? 541  VAL A CA  1 
ATOM   13525 C C   . VAL B 2 541  ? 183.064 192.761 155.811 1.00 33.28  ? 541  VAL A C   1 
ATOM   13526 O O   . VAL B 2 541  ? 183.086 192.957 154.589 1.00 33.28  ? 541  VAL A O   1 
ATOM   13527 C CB  . VAL B 2 541  ? 181.323 193.904 157.250 1.00 33.28  ? 541  VAL A CB  1 
ATOM   13528 C CG1 . VAL B 2 541  ? 181.680 195.098 156.391 1.00 33.28  ? 541  VAL A CG1 1 
ATOM   13529 C CG2 . VAL B 2 541  ? 179.838 193.894 157.529 1.00 33.28  ? 541  VAL A CG2 1 
ATOM   13530 N N   . SER B 2 542  ? 184.184 192.681 156.533 1.00 33.06  ? 542  SER A N   1 
ATOM   13531 C CA  . SER B 2 542  ? 185.488 192.759 155.882 1.00 33.06  ? 542  SER A CA  1 
ATOM   13532 C C   . SER B 2 542  ? 185.697 191.589 154.930 1.00 33.06  ? 542  SER A C   1 
ATOM   13533 O O   . SER B 2 542  ? 186.270 191.751 153.846 1.00 33.06  ? 542  SER A O   1 
ATOM   13534 C CB  . SER B 2 542  ? 186.598 192.804 156.930 1.00 33.06  ? 542  SER A CB  1 
ATOM   13535 O OG  . SER B 2 542  ? 187.871 192.867 156.313 1.00 33.06  ? 542  SER A OG  1 
ATOM   13536 N N   . PHE B 2 543  ? 185.244 190.397 155.327 1.00 32.25  ? 543  PHE A N   1 
ATOM   13537 C CA  . PHE B 2 543  ? 185.335 189.233 154.454 1.00 32.25  ? 543  PHE A CA  1 
ATOM   13538 C C   . PHE B 2 543  ? 184.586 189.475 153.151 1.00 32.25  ? 543  PHE A C   1 
ATOM   13539 O O   . PHE B 2 543  ? 185.117 189.223 152.064 1.00 32.25  ? 543  PHE A O   1 
ATOM   13540 C CB  . PHE B 2 543  ? 184.787 188.004 155.183 1.00 32.25  ? 543  PHE A CB  1 
ATOM   13541 C CG  . PHE B 2 543  ? 184.804 186.741 154.366 1.00 32.25  ? 543  PHE A CG  1 
ATOM   13542 C CD1 . PHE B 2 543  ? 183.809 186.478 153.437 1.00 32.25  ? 543  PHE A CD1 1 
ATOM   13543 C CD2 . PHE B 2 543  ? 185.813 185.809 154.534 1.00 32.25  ? 543  PHE A CD2 1 
ATOM   13544 C CE1 . PHE B 2 543  ? 183.825 185.320 152.693 1.00 32.25  ? 543  PHE A CE1 1 
ATOM   13545 C CE2 . PHE B 2 543  ? 185.832 184.649 153.792 1.00 32.25  ? 543  PHE A CE2 1 
ATOM   13546 C CZ  . PHE B 2 543  ? 184.837 184.405 152.870 1.00 32.25  ? 543  PHE A CZ  1 
ATOM   13547 N N   . LEU B 2 544  ? 183.349 189.966 153.242 1.00 32.54  ? 544  LEU A N   1 
ATOM   13548 C CA  . LEU B 2 544  ? 182.579 190.246 152.032 1.00 32.54  ? 544  LEU A CA  1 
ATOM   13549 C C   . LEU B 2 544  ? 183.243 191.330 151.191 1.00 32.54  ? 544  LEU A C   1 
ATOM   13550 O O   . LEU B 2 544  ? 183.267 191.243 149.957 1.00 32.54  ? 544  LEU A O   1 
ATOM   13551 C CB  . LEU B 2 544  ? 181.150 190.647 152.391 1.00 32.54  ? 544  LEU A CB  1 
ATOM   13552 C CG  . LEU B 2 544  ? 180.119 189.520 152.380 1.00 32.54  ? 544  LEU A CG  1 
ATOM   13553 C CD1 . LEU B 2 544  ? 178.948 189.848 153.285 1.00 32.54  ? 544  LEU A CD1 1 
ATOM   13554 C CD2 . LEU B 2 544  ? 179.647 189.272 150.959 1.00 32.54  ? 544  LEU A CD2 1 
ATOM   13555 N N   . GLY B 2 545  ? 183.775 192.367 151.842 1.00 33.56  ? 545  GLY A N   1 
ATOM   13556 C CA  . GLY B 2 545  ? 184.424 193.436 151.103 1.00 33.56  ? 545  GLY A CA  1 
ATOM   13557 C C   . GLY B 2 545  ? 185.640 192.962 150.332 1.00 33.56  ? 545  GLY A C   1 
ATOM   13558 O O   . GLY B 2 545  ? 185.860 193.372 149.190 1.00 33.56  ? 545  GLY A O   1 
ATOM   13559 N N   . SER B 2 546  ? 186.451 192.100 150.947 1.00 31.83  ? 546  SER A N   1 
ATOM   13560 C CA  . SER B 2 546  ? 187.609 191.568 150.241 1.00 31.83  ? 546  SER A CA  1 
ATOM   13561 C C   . SER B 2 546  ? 187.201 190.546 149.187 1.00 31.83  ? 546  SER A C   1 
ATOM   13562 O O   . SER B 2 546  ? 187.884 190.406 148.168 1.00 31.83  ? 546  SER A O   1 
ATOM   13563 C CB  . SER B 2 546  ? 188.590 190.938 151.224 1.00 31.83  ? 546  SER A CB  1 
ATOM   13564 O OG  . SER B 2 546  ? 188.238 189.594 151.486 1.00 31.83  ? 546  SER A OG  1 
ATOM   13565 N N   . LEU B 2 547  ? 186.103 189.822 149.415 1.00 30.45  ? 547  LEU A N   1 
ATOM   13566 C CA  . LEU B 2 547  ? 185.632 188.855 148.433 1.00 30.45  ? 547  LEU A CA  1 
ATOM   13567 C C   . LEU B 2 547  ? 185.091 189.538 147.183 1.00 30.45  ? 547  LEU A C   1 
ATOM   13568 O O   . LEU B 2 547  ? 185.250 189.014 146.075 1.00 30.45  ? 547  LEU A O   1 
ATOM   13569 C CB  . LEU B 2 547  ? 184.553 187.968 149.053 1.00 30.45  ? 547  LEU A CB  1 
ATOM   13570 C CG  . LEU B 2 547  ? 183.628 187.193 148.114 1.00 30.45  ? 547  LEU A CG  1 
ATOM   13571 C CD1 . LEU B 2 547  ? 184.413 186.190 147.286 1.00 30.45  ? 547  LEU A CD1 1 
ATOM   13572 C CD2 . LEU B 2 547  ? 182.521 186.509 148.890 1.00 30.45  ? 547  LEU A CD2 1 
ATOM   13573 N N   . SER B 2 548  ? 184.470 190.709 147.339 1.00 32.25  ? 548  SER A N   1 
ATOM   13574 C CA  . SER B 2 548  ? 183.791 191.343 146.214 1.00 32.25  ? 548  SER A CA  1 
ATOM   13575 C C   . SER B 2 548  ? 184.738 191.726 145.084 1.00 32.25  ? 548  SER A C   1 
ATOM   13576 O O   . SER B 2 548  ? 184.275 192.003 143.973 1.00 32.25  ? 548  SER A O   1 
ATOM   13577 C CB  . SER B 2 548  ? 183.033 192.580 146.687 1.00 32.25  ? 548  SER A CB  1 
ATOM   13578 O OG  . SER B 2 548  ? 182.484 193.285 145.591 1.00 32.25  ? 548  SER A OG  1 
ATOM   13579 N N   . VAL B 2 549  ? 186.050 191.754 145.337 1.00 32.10  ? 549  VAL A N   1 
ATOM   13580 C CA  . VAL B 2 549  ? 187.003 192.136 144.296 1.00 32.10  ? 549  VAL A CA  1 
ATOM   13581 C C   . VAL B 2 549  ? 187.414 190.980 143.401 1.00 32.10  ? 549  VAL A C   1 
ATOM   13582 O O   . VAL B 2 549  ? 188.020 191.216 142.348 1.00 32.10  ? 549  VAL A O   1 
ATOM   13583 C CB  . VAL B 2 549  ? 188.277 192.744 144.908 1.00 32.10  ? 549  VAL A CB  1 
ATOM   13584 C CG1 . VAL B 2 549  ? 187.924 193.713 146.018 1.00 32.10  ? 549  VAL A CG1 1 
ATOM   13585 C CG2 . VAL B 2 549  ? 189.186 191.648 145.423 1.00 32.10  ? 549  VAL A CG2 1 
ATOM   13586 N N   . LEU B 2 550  ? 187.113 189.738 143.785 1.00 32.19  ? 550  LEU A N   1 
ATOM   13587 C CA  . LEU B 2 550  ? 187.543 188.595 142.982 1.00 32.19  ? 550  LEU A CA  1 
ATOM   13588 C C   . LEU B 2 550  ? 186.928 188.589 141.587 1.00 32.19  ? 550  LEU A C   1 
ATOM   13589 O O   . LEU B 2 550  ? 187.678 188.405 140.612 1.00 32.19  ? 550  LEU A O   1 
ATOM   13590 C CB  . LEU B 2 550  ? 187.251 187.294 143.736 1.00 32.19  ? 550  LEU A CB  1 
ATOM   13591 C CG  . LEU B 2 550  ? 188.475 186.564 144.285 1.00 32.19  ? 550  LEU A CG  1 
ATOM   13592 C CD1 . LEU B 2 550  ? 189.246 187.463 145.237 1.00 32.19  ? 550  LEU A CD1 1 
ATOM   13593 C CD2 . LEU B 2 550  ? 188.062 185.276 144.976 1.00 32.19  ? 550  LEU A CD2 1 
ATOM   13594 N N   . PRO B 2 551  ? 185.613 188.762 141.404 1.00 34.34  ? 551  PRO A N   1 
ATOM   13595 C CA  . PRO B 2 551  ? 185.103 188.909 140.032 1.00 34.34  ? 551  PRO A CA  1 
ATOM   13596 C C   . PRO B 2 551  ? 185.639 190.139 139.331 1.00 34.34  ? 551  PRO A C   1 
ATOM   13597 O O   . PRO B 2 551  ? 185.809 190.119 138.107 1.00 34.34  ? 551  PRO A O   1 
ATOM   13598 C CB  . PRO B 2 551  ? 183.581 188.983 140.223 1.00 34.34  ? 551  PRO A CB  1 
ATOM   13599 C CG  . PRO B 2 551  ? 183.330 188.402 141.564 1.00 34.34  ? 551  PRO A CG  1 
ATOM   13600 C CD  . PRO B 2 551  ? 184.516 188.783 142.386 1.00 34.34  ? 551  PRO A CD  1 
ATOM   13601 N N   . GLY B 2 552  ? 185.915 191.211 140.070 1.00 35.62  ? 552  GLY A N   1 
ATOM   13602 C CA  . GLY B 2 552  ? 186.421 192.430 139.469 1.00 35.62  ? 552  GLY A CA  1 
ATOM   13603 C C   . GLY B 2 552  ? 187.901 192.437 139.171 1.00 35.62  ? 552  GLY A C   1 
ATOM   13604 O O   . GLY B 2 552  ? 188.391 193.394 138.565 1.00 35.62  ? 552  GLY A O   1 
ATOM   13605 N N   . ASN B 2 553  ? 188.624 191.399 139.583 1.00 33.33  ? 553  ASN A N   1 
ATOM   13606 C CA  . ASN B 2 553  ? 190.047 191.296 139.286 1.00 33.33  ? 553  ASN A CA  1 
ATOM   13607 C C   . ASN B 2 553  ? 190.310 190.499 138.016 1.00 33.33  ? 553  ASN A C   1 
ATOM   13608 O O   . ASN B 2 553  ? 191.233 190.824 137.267 1.00 33.33  ? 553  ASN A O   1 
ATOM   13609 C CB  . ASN B 2 553  ? 190.787 190.657 140.464 1.00 33.33  ? 553  ASN A CB  1 
ATOM   13610 C CG  . ASN B 2 553  ? 192.278 190.934 140.443 1.00 33.33  ? 553  ASN A CG  1 
ATOM   13611 O OD1 . ASN B 2 553  ? 192.928 190.842 139.403 1.00 33.33  ? 553  ASN A OD1 1 
ATOM   13612 N ND2 . ASN B 2 553  ? 192.831 191.269 141.601 1.00 33.33  ? 553  ASN A ND2 1 
ATOM   13613 N N   . ILE B 2 554  ? 189.515 189.457 137.762 1.00 36.96  ? 554  ILE A N   1 
ATOM   13614 C CA  . ILE B 2 554  ? 189.715 188.652 136.562 1.00 36.96  ? 554  ILE A CA  1 
ATOM   13615 C C   . ILE B 2 554  ? 189.386 189.461 135.313 1.00 36.96  ? 554  ILE A C   1 
ATOM   13616 O O   . ILE B 2 554  ? 190.078 189.361 134.294 1.00 36.96  ? 554  ILE A O   1 
ATOM   13617 C CB  . ILE B 2 554  ? 188.884 187.361 136.643 1.00 36.96  ? 554  ILE A CB  1 
ATOM   13618 C CG1 . ILE B 2 554  ? 189.215 186.598 137.925 1.00 36.96  ? 554  ILE A CG1 1 
ATOM   13619 C CG2 . ILE B 2 554  ? 189.147 186.481 135.436 1.00 36.96  ? 554  ILE A CG2 1 
ATOM   13620 C CD1 . ILE B 2 554  ? 188.299 185.426 138.191 1.00 36.96  ? 554  ILE A CD1 1 
ATOM   13621 N N   . ILE B 2 555  ? 188.331 190.278 135.372 1.00 37.10  ? 555  ILE A N   1 
ATOM   13622 C CA  . ILE B 2 555  ? 187.999 191.160 134.258 1.00 37.10  ? 555  ILE A CA  1 
ATOM   13623 C C   . ILE B 2 555  ? 189.036 192.253 134.048 1.00 37.10  ? 555  ILE A C   1 
ATOM   13624 O O   . ILE B 2 555  ? 188.922 193.027 133.096 1.00 37.10  ? 555  ILE A O   1 
ATOM   13625 C CB  . ILE B 2 555  ? 186.608 191.791 134.451 1.00 37.10  ? 555  ILE A CB  1 
ATOM   13626 C CG1 . ILE B 2 555  ? 186.685 192.985 135.404 1.00 37.10  ? 555  ILE A CG1 1 
ATOM   13627 C CG2 . ILE B 2 555  ? 185.617 190.750 134.944 1.00 37.10  ? 555  ILE A CG2 1 
ATOM   13628 C CD1 . ILE B 2 555  ? 185.335 193.527 135.824 1.00 37.10  ? 555  ILE A CD1 1 
ATOM   13629 N N   . SER B 2 556  ? 190.039 192.340 134.921 1.00 37.52  ? 556  SER A N   1 
ATOM   13630 C CA  . SER B 2 556  ? 191.182 193.220 134.708 1.00 37.52  ? 556  SER A CA  1 
ATOM   13631 C C   . SER B 2 556  ? 192.445 192.457 134.353 1.00 37.52  ? 556  SER A C   1 
ATOM   13632 O O   . SER B 2 556  ? 193.351 193.027 133.737 1.00 37.52  ? 556  SER A O   1 
ATOM   13633 C CB  . SER B 2 556  ? 191.444 194.065 135.953 1.00 37.52  ? 556  SER A CB  1 
ATOM   13634 O OG  . SER B 2 556  ? 192.764 194.577 135.950 1.00 37.52  ? 556  SER A OG  1 
ATOM   13635 N N   . ALA B 2 557  ? 192.525 191.184 134.741 1.00 37.95  ? 557  ALA A N   1 
ATOM   13636 C CA  . ALA B 2 557  ? 193.679 190.368 134.389 1.00 37.95  ? 557  ALA A CA  1 
ATOM   13637 C C   . ALA B 2 557  ? 193.731 190.124 132.888 1.00 37.95  ? 557  ALA A C   1 
ATOM   13638 O O   . ALA B 2 557  ? 194.704 190.495 132.222 1.00 37.95  ? 557  ALA A O   1 
ATOM   13639 C CB  . ALA B 2 557  ? 193.636 189.042 135.147 1.00 37.95  ? 557  ALA A CB  1 
ATOM   13640 N N   . LEU B 2 558  ? 192.687 189.514 132.336 1.00 40.38  ? 558  LEU A N   1 
ATOM   13641 C CA  . LEU B 2 558  ? 192.644 189.271 130.899 1.00 40.38  ? 558  LEU A CA  1 
ATOM   13642 C C   . LEU B 2 558  ? 192.007 190.446 130.170 1.00 40.38  ? 558  LEU A C   1 
ATOM   13643 O O   . LEU B 2 558  ? 191.159 190.281 129.294 1.00 40.38  ? 558  LEU A O   1 
ATOM   13644 C CB  . LEU B 2 558  ? 191.882 187.980 130.622 1.00 40.38  ? 558  LEU A CB  1 
ATOM   13645 C CG  . LEU B 2 558  ? 192.118 186.836 131.612 1.00 40.38  ? 558  LEU A CG  1 
ATOM   13646 C CD1 . LEU B 2 558  ? 191.180 185.676 131.327 1.00 40.38  ? 558  LEU A CD1 1 
ATOM   13647 C CD2 . LEU B 2 558  ? 193.568 186.380 131.578 1.00 40.38  ? 558  LEU A CD2 1 
ATOM   13648 N N   . LEU B 2 559  ? 192.419 191.659 130.540 1.00 42.93  ? 559  LEU A N   1 
ATOM   13649 C CA  . LEU B 2 559  ? 192.072 192.857 129.790 1.00 42.93  ? 559  LEU A CA  1 
ATOM   13650 C C   . LEU B 2 559  ? 193.197 193.875 129.688 1.00 42.93  ? 559  LEU A C   1 
ATOM   13651 O O   . LEU B 2 559  ? 193.131 194.740 128.813 1.00 42.93  ? 559  LEU A O   1 
ATOM   13652 C CB  . LEU B 2 559  ? 190.840 193.540 130.404 1.00 42.93  ? 559  LEU A CB  1 
ATOM   13653 C CG  . LEU B 2 559  ? 189.453 193.127 129.902 1.00 42.93  ? 559  LEU A CG  1 
ATOM   13654 C CD1 . LEU B 2 559  ? 188.425 194.202 130.217 1.00 42.93  ? 559  LEU A CD1 1 
ATOM   13655 C CD2 . LEU B 2 559  ? 189.468 192.847 128.412 1.00 42.93  ? 559  LEU A CD2 1 
ATOM   13656 N N   . MET B 2 560  ? 194.238 193.793 130.515 1.00 44.47  ? 560  MET A N   1 
ATOM   13657 C CA  . MET B 2 560  ? 195.219 194.870 130.556 1.00 44.47  ? 560  MET A CA  1 
ATOM   13658 C C   . MET B 2 560  ? 196.108 194.892 129.323 1.00 44.47  ? 560  MET A C   1 
ATOM   13659 O O   . MET B 2 560  ? 196.845 195.863 129.124 1.00 44.47  ? 560  MET A O   1 
ATOM   13660 C CB  . MET B 2 560  ? 196.074 194.761 131.812 1.00 44.47  ? 560  MET A CB  1 
ATOM   13661 C CG  . MET B 2 560  ? 195.451 195.403 133.031 1.00 44.47  ? 560  MET A CG  1 
ATOM   13662 S SD  . MET B 2 560  ? 196.415 195.136 134.523 1.00 44.47  ? 560  MET A SD  1 
ATOM   13663 C CE  . MET B 2 560  ? 197.975 194.658 133.797 1.00 44.47  ? 560  MET A CE  1 
ATOM   13664 N N   . ASP B 2 561  ? 196.062 193.850 128.502 1.00 46.70  ? 561  ASP A N   1 
ATOM   13665 C CA  . ASP B 2 561  ? 196.783 193.834 127.240 1.00 46.70  ? 561  ASP A CA  1 
ATOM   13666 C C   . ASP B 2 561  ? 195.952 194.373 126.084 1.00 46.70  ? 561  ASP A C   1 
ATOM   13667 O O   . ASP B 2 561  ? 196.445 194.402 124.951 1.00 46.70  ? 561  ASP A O   1 
ATOM   13668 C CB  . ASP B 2 561  ? 197.250 192.407 126.924 1.00 46.70  ? 561  ASP A CB  1 
ATOM   13669 C CG  . ASP B 2 561  ? 198.664 192.136 127.404 1.00 46.70  ? 561  ASP A CG  1 
ATOM   13670 O OD1 . ASP B 2 561  ? 199.261 193.040 128.025 1.00 46.70  ? 561  ASP A OD1 1 
ATOM   13671 O OD2 . ASP B 2 561  ? 199.173 191.017 127.174 1.00 46.70  ? 561  ASP A OD2 1 
ATOM   13672 N N   . ARG B 2 562  ? 194.710 194.792 126.333 1.00 46.82  ? 562  ARG A N   1 
ATOM   13673 C CA  . ARG B 2 562  ? 193.848 195.316 125.278 1.00 46.82  ? 562  ARG A CA  1 
ATOM   13674 C C   . ARG B 2 562  ? 193.522 196.792 125.463 1.00 46.82  ? 562  ARG A C   1 
ATOM   13675 O O   . ARG B 2 562  ? 193.806 197.596 124.571 1.00 46.82  ? 562  ARG A O   1 
ATOM   13676 C CB  . ARG B 2 562  ? 192.561 194.481 125.194 1.00 46.82  ? 562  ARG A CB  1 
ATOM   13677 C CG  . ARG B 2 562  ? 192.819 192.979 125.142 1.00 46.82  ? 562  ARG A CG  1 
ATOM   13678 C CD  . ARG B 2 562  ? 191.641 192.173 125.657 1.00 46.82  ? 562  ARG A CD  1 
ATOM   13679 N NE  . ARG B 2 562  ? 190.781 191.727 124.570 1.00 46.82  ? 562  ARG A NE  1 
ATOM   13680 C CZ  . ARG B 2 562  ? 189.721 190.943 124.718 1.00 46.82  ? 562  ARG A CZ  1 
ATOM   13681 N NH1 . ARG B 2 562  ? 189.354 190.492 125.907 1.00 46.82  ? 562  ARG A NH1 1 
ATOM   13682 N NH2 . ARG B 2 562  ? 189.013 190.601 123.645 1.00 46.82  ? 562  ARG A NH2 1 
ATOM   13683 N N   . ILE B 2 563  ? 192.934 197.186 126.595 1.00 47.62  ? 563  ILE A N   1 
ATOM   13684 C CA  . ILE B 2 563  ? 192.671 198.608 126.801 1.00 47.62  ? 563  ILE A CA  1 
ATOM   13685 C C   . ILE B 2 563  ? 193.968 199.365 127.050 1.00 47.62  ? 563  ILE A C   1 
ATOM   13686 O O   . ILE B 2 563  ? 194.172 200.460 126.516 1.00 47.62  ? 563  ILE A O   1 
ATOM   13687 C CB  . ILE B 2 563  ? 191.647 198.856 127.930 1.00 47.62  ? 563  ILE A CB  1 
ATOM   13688 C CG1 . ILE B 2 563  ? 190.505 197.837 127.919 1.00 47.62  ? 563  ILE A CG1 1 
ATOM   13689 C CG2 . ILE B 2 563  ? 191.083 200.257 127.832 1.00 47.62  ? 563  ILE A CG2 1 
ATOM   13690 C CD1 . ILE B 2 563  ? 190.745 196.617 128.732 1.00 47.62  ? 563  ILE A CD1 1 
ATOM   13691 N N   . GLY B 2 564  ? 194.862 198.806 127.857 1.00 45.10  ? 564  GLY A N   1 
ATOM   13692 C CA  . GLY B 2 564  ? 196.144 199.424 128.104 1.00 45.10  ? 564  GLY A CA  1 
ATOM   13693 C C   . GLY B 2 564  ? 196.452 199.487 129.578 1.00 45.10  ? 564  GLY A C   1 
ATOM   13694 O O   . GLY B 2 564  ? 195.882 198.757 130.393 1.00 45.10  ? 564  GLY A O   1 
ATOM   13695 N N   . ARG B 2 565  ? 197.379 200.378 129.925 1.00 43.29  ? 565  ARG A N   1 
ATOM   13696 C CA  . ARG B 2 565  ? 197.867 200.512 131.288 1.00 43.29  ? 565  ARG A CA  1 
ATOM   13697 C C   . ARG B 2 565  ? 197.582 201.873 131.903 1.00 43.29  ? 565  ARG A C   1 
ATOM   13698 O O   . ARG B 2 565  ? 197.872 202.066 133.090 1.00 43.29  ? 565  ARG A O   1 
ATOM   13699 C CB  . ARG B 2 565  ? 199.380 200.247 131.338 1.00 43.29  ? 565  ARG A CB  1 
ATOM   13700 C CG  . ARG B 2 565  ? 199.739 198.823 131.715 1.00 43.29  ? 565  ARG A CG  1 
ATOM   13701 C CD  . ARG B 2 565  ? 200.947 198.339 130.928 1.00 43.29  ? 565  ARG A CD  1 
ATOM   13702 N NE  . ARG B 2 565  ? 201.010 196.882 130.870 1.00 43.29  ? 565  ARG A NE  1 
ATOM   13703 C CZ  . ARG B 2 565  ? 200.635 196.159 129.824 1.00 43.29  ? 565  ARG A CZ  1 
ATOM   13704 N NH1 . ARG B 2 565  ? 200.162 196.722 128.726 1.00 43.29  ? 565  ARG A NH1 1 
ATOM   13705 N NH2 . ARG B 2 565  ? 200.738 194.834 129.882 1.00 43.29  ? 565  ARG A NH2 1 
ATOM   13706 N N   . LEU B 2 566  ? 197.039 202.816 131.142 1.00 41.73  ? 566  LEU A N   1 
ATOM   13707 C CA  . LEU B 2 566  ? 196.659 204.123 131.654 1.00 41.73  ? 566  LEU A CA  1 
ATOM   13708 C C   . LEU B 2 566  ? 195.172 204.403 131.552 1.00 41.73  ? 566  LEU A C   1 
ATOM   13709 O O   . LEU B 2 566  ? 194.646 205.162 132.368 1.00 41.73  ? 566  LEU A O   1 
ATOM   13710 C CB  . LEU B 2 566  ? 197.420 205.238 130.917 1.00 41.73  ? 566  LEU A CB  1 
ATOM   13711 C CG  . LEU B 2 566  ? 198.900 205.023 130.589 1.00 41.73  ? 566  LEU A CG  1 
ATOM   13712 C CD1 . LEU B 2 566  ? 199.087 204.352 129.233 1.00 41.73  ? 566  LEU A CD1 1 
ATOM   13713 C CD2 . LEU B 2 566  ? 199.644 206.342 130.645 1.00 41.73  ? 566  LEU A CD2 1 
ATOM   13714 N N   . LYS B 2 567  ? 194.480 203.825 130.571 1.00 41.63  ? 567  LYS A N   1 
ATOM   13715 C CA  . LYS B 2 567  ? 193.031 203.967 130.520 1.00 41.63  ? 567  LYS A CA  1 
ATOM   13716 C C   . LYS B 2 567  ? 192.357 203.152 131.613 1.00 41.63  ? 567  LYS A C   1 
ATOM   13717 O O   . LYS B 2 567  ? 191.317 203.566 132.139 1.00 41.63  ? 567  LYS A O   1 
ATOM   13718 C CB  . LYS B 2 567  ? 192.505 203.554 129.147 1.00 41.63  ? 567  LYS A CB  1 
ATOM   13719 C CG  . LYS B 2 567  ? 193.153 204.286 127.981 1.00 41.63  ? 567  LYS A CG  1 
ATOM   13720 C CD  . LYS B 2 567  ? 193.192 205.790 128.221 1.00 41.63  ? 567  LYS A CD  1 
ATOM   13721 C CE  . LYS B 2 567  ? 193.960 206.508 127.122 1.00 41.63  ? 567  LYS A CE  1 
ATOM   13722 N NZ  . LYS B 2 567  ? 193.579 207.944 127.025 1.00 41.63  ? 567  LYS A NZ  1 
ATOM   13723 N N   . MET B 2 568  ? 192.935 202.005 131.979 1.00 42.25  ? 568  MET A N   1 
ATOM   13724 C CA  . MET B 2 568  ? 192.340 201.173 133.019 1.00 42.25  ? 568  MET A CA  1 
ATOM   13725 C C   . MET B 2 568  ? 192.337 201.882 134.365 1.00 42.25  ? 568  MET A C   1 
ATOM   13726 O O   . MET B 2 568  ? 191.314 201.924 135.052 1.00 42.25  ? 568  MET A O   1 
ATOM   13727 C CB  . MET B 2 568  ? 193.075 199.842 133.125 1.00 42.25  ? 568  MET A CB  1 
ATOM   13728 C CG  . MET B 2 568  ? 192.480 198.924 134.173 1.00 42.25  ? 568  MET A CG  1 
ATOM   13729 S SD  . MET B 2 568  ? 192.556 197.184 133.737 1.00 42.25  ? 568  MET A SD  1 
ATOM   13730 C CE  . MET B 2 568  ? 191.547 197.167 132.263 1.00 42.25  ? 568  MET A CE  1 
ATOM   13731 N N   . ILE B 2 569  ? 193.483 202.439 134.763 1.00 38.54  ? 569  ILE A N   1 
ATOM   13732 C CA  . ILE B 2 569  ? 193.582 203.057 136.082 1.00 38.54  ? 569  ILE A CA  1 
ATOM   13733 C C   . ILE B 2 569  ? 192.651 204.263 136.181 1.00 38.54  ? 569  ILE A C   1 
ATOM   13734 O O   . ILE B 2 569  ? 191.891 204.401 137.148 1.00 38.54  ? 569  ILE A O   1 
ATOM   13735 C CB  . ILE B 2 569  ? 195.044 203.428 136.390 1.00 38.54  ? 569  ILE A CB  1 
ATOM   13736 C CG1 . ILE B 2 569  ? 195.146 204.218 137.694 1.00 38.54  ? 569  ILE A CG1 1 
ATOM   13737 C CG2 . ILE B 2 569  ? 195.678 204.190 135.237 1.00 38.54  ? 569  ILE A CG2 1 
ATOM   13738 C CD1 . ILE B 2 569  ? 194.712 203.448 138.902 1.00 38.54  ? 569  ILE A CD1 1 
ATOM   13739 N N   . GLY B 2 570  ? 192.667 205.132 135.168 1.00 37.92  ? 570  GLY A N   1 
ATOM   13740 C CA  . GLY B 2 570  ? 191.793 206.292 135.189 1.00 37.92  ? 570  GLY A CA  1 
ATOM   13741 C C   . GLY B 2 570  ? 190.324 205.919 135.151 1.00 37.92  ? 570  GLY A C   1 
ATOM   13742 O O   . GLY B 2 570  ? 189.512 206.477 135.896 1.00 37.92  ? 570  GLY A O   1 
ATOM   13743 N N   . GLY B 2 571  ? 189.963 204.968 134.285 1.00 38.13  ? 571  GLY A N   1 
ATOM   13744 C CA  . GLY B 2 571  ? 188.574 204.550 134.201 1.00 38.13  ? 571  GLY A CA  1 
ATOM   13745 C C   . GLY B 2 571  ? 188.075 203.935 135.493 1.00 38.13  ? 571  GLY A C   1 
ATOM   13746 O O   . GLY B 2 571  ? 186.979 204.248 135.961 1.00 38.13  ? 571  GLY A O   1 
ATOM   13747 N N   . SER B 2 572  ? 188.878 203.052 136.089 1.00 35.41  ? 572  SER A N   1 
ATOM   13748 C CA  . SER B 2 572  ? 188.486 202.430 137.350 1.00 35.41  ? 572  SER A CA  1 
ATOM   13749 C C   . SER B 2 572  ? 188.359 203.467 138.457 1.00 35.41  ? 572  SER A C   1 
ATOM   13750 O O   . SER B 2 572  ? 187.415 203.423 139.252 1.00 35.41  ? 572  SER A O   1 
ATOM   13751 C CB  . SER B 2 572  ? 189.494 201.347 137.732 1.00 35.41  ? 572  SER A CB  1 
ATOM   13752 O OG  . SER B 2 572  ? 189.191 200.796 139.002 1.00 35.41  ? 572  SER A OG  1 
ATOM   13753 N N   . MET B 2 573  ? 189.293 204.419 138.514 1.00 35.96  ? 573  MET A N   1 
ATOM   13754 C CA  . MET B 2 573  ? 189.225 205.458 139.538 1.00 35.96  ? 573  MET A CA  1 
ATOM   13755 C C   . MET B 2 573  ? 187.961 206.298 139.385 1.00 35.96  ? 573  MET A C   1 
ATOM   13756 O O   . MET B 2 573  ? 187.245 206.547 140.363 1.00 35.96  ? 573  MET A O   1 
ATOM   13757 C CB  . MET B 2 573  ? 190.473 206.335 139.459 1.00 35.96  ? 573  MET A CB  1 
ATOM   13758 C CG  . MET B 2 573  ? 191.640 205.865 140.315 1.00 35.96  ? 573  MET A CG  1 
ATOM   13759 S SD  . MET B 2 573  ? 192.943 207.109 140.345 1.00 35.96  ? 573  MET A SD  1 
ATOM   13760 C CE  . MET B 2 573  ? 193.845 206.699 141.830 1.00 35.96  ? 573  MET A CE  1 
ATOM   13761 N N   . LEU B 2 574  ? 187.654 206.722 138.156 1.00 35.14  ? 574  LEU A N   1 
ATOM   13762 C CA  . LEU B 2 574  ? 186.474 207.556 137.947 1.00 35.14  ? 574  LEU A CA  1 
ATOM   13763 C C   . LEU B 2 574  ? 185.184 206.782 138.195 1.00 35.14  ? 574  LEU A C   1 
ATOM   13764 O O   . LEU B 2 574  ? 184.216 207.336 138.724 1.00 35.14  ? 574  LEU A O   1 
ATOM   13765 C CB  . LEU B 2 574  ? 186.485 208.151 136.541 1.00 35.14  ? 574  LEU A CB  1 
ATOM   13766 C CG  . LEU B 2 574  ? 186.994 209.591 136.453 1.00 35.14  ? 574  LEU A CG  1 
ATOM   13767 C CD1 . LEU B 2 574  ? 188.442 209.685 136.886 1.00 35.14  ? 574  LEU A CD1 1 
ATOM   13768 C CD2 . LEU B 2 574  ? 186.820 210.134 135.045 1.00 35.14  ? 574  LEU A CD2 1 
ATOM   13769 N N   . ILE B 2 575  ? 185.147 205.500 137.823 1.00 32.37  ? 575  ILE A N   1 
ATOM   13770 C CA  . ILE B 2 575  ? 183.940 204.712 138.048 1.00 32.37  ? 575  ILE A CA  1 
ATOM   13771 C C   . ILE B 2 575  ? 183.723 204.479 139.538 1.00 32.37  ? 575  ILE A C   1 
ATOM   13772 O O   . ILE B 2 575  ? 182.593 204.550 140.032 1.00 32.37  ? 575  ILE A O   1 
ATOM   13773 C CB  . ILE B 2 575  ? 184.013 203.390 137.264 1.00 32.37  ? 575  ILE A CB  1 
ATOM   13774 C CG1 . ILE B 2 575  ? 183.831 203.650 135.767 1.00 32.37  ? 575  ILE A CG1 1 
ATOM   13775 C CG2 . ILE B 2 575  ? 182.955 202.423 137.753 1.00 32.37  ? 575  ILE A CG2 1 
ATOM   13776 C CD1 . ILE B 2 575  ? 182.913 204.809 135.443 1.00 32.37  ? 575  ILE A CD1 1 
ATOM   13777 N N   . SER B 2 576  ? 184.800 204.208 140.280 1.00 32.08  ? 576  SER A N   1 
ATOM   13778 C CA  . SER B 2 576  ? 184.677 204.092 141.729 1.00 32.08  ? 576  SER A CA  1 
ATOM   13779 C C   . SER B 2 576  ? 184.221 205.406 142.345 1.00 32.08  ? 576  SER A C   1 
ATOM   13780 O O   . SER B 2 576  ? 183.441 205.412 143.304 1.00 32.08  ? 576  SER A O   1 
ATOM   13781 C CB  . SER B 2 576  ? 186.002 203.638 142.334 1.00 32.08  ? 576  SER A CB  1 
ATOM   13782 O OG  . SER B 2 576  ? 186.373 202.357 141.853 1.00 32.08  ? 576  SER A OG  1 
ATOM   13783 N N   . ALA B 2 577  ? 184.697 206.536 141.811 1.00 32.90  ? 577  ALA A N   1 
ATOM   13784 C CA  . ALA B 2 577  ? 184.230 207.833 142.294 1.00 32.90  ? 577  ALA A CA  1 
ATOM   13785 C C   . ALA B 2 577  ? 182.735 208.017 142.046 1.00 32.90  ? 577  ALA A C   1 
ATOM   13786 O O   . ALA B 2 577  ? 182.006 208.511 142.917 1.00 32.90  ? 577  ALA A O   1 
ATOM   13787 C CB  . ALA B 2 577  ? 185.021 208.956 141.627 1.00 32.90  ? 577  ALA A CB  1 
ATOM   13788 N N   . VAL B 2 578  ? 182.267 207.627 140.858 1.00 32.67  ? 578  VAL A N   1 
ATOM   13789 C CA  . VAL B 2 578  ? 180.843 207.724 140.543 1.00 32.67  ? 578  VAL A CA  1 
ATOM   13790 C C   . VAL B 2 578  ? 180.031 206.852 141.491 1.00 32.67  ? 578  VAL A C   1 
ATOM   13791 O O   . VAL B 2 578  ? 178.961 207.253 141.966 1.00 32.67  ? 578  VAL A O   1 
ATOM   13792 C CB  . VAL B 2 578  ? 180.589 207.342 139.072 1.00 32.67  ? 578  VAL A CB  1 
ATOM   13793 C CG1 . VAL B 2 578  ? 179.101 207.206 138.808 1.00 32.67  ? 578  VAL A CG1 1 
ATOM   13794 C CG2 . VAL B 2 578  ? 181.201 208.376 138.146 1.00 32.67  ? 578  VAL A CG2 1 
ATOM   13795 N N   . CYS B 2 579  ? 180.527 205.649 141.782 1.00 33.70  ? 579  CYS A N   1 
ATOM   13796 C CA  . CYS B 2 579  ? 179.844 204.780 142.736 1.00 33.70  ? 579  CYS A CA  1 
ATOM   13797 C C   . CYS B 2 579  ? 179.828 205.396 144.130 1.00 33.70  ? 579  CYS A C   1 
ATOM   13798 O O   . CYS B 2 579  ? 178.841 205.263 144.866 1.00 33.70  ? 579  CYS A O   1 
ATOM   13799 C CB  . CYS B 2 579  ? 180.505 203.406 142.764 1.00 33.70  ? 579  CYS A CB  1 
ATOM   13800 S SG  . CYS B 2 579  ? 179.977 202.358 144.135 1.00 33.70  ? 579  CYS A SG  1 
ATOM   13801 N N   . CYS B 2 580  ? 180.919 206.063 144.517 1.00 32.20  ? 580  CYS A N   1 
ATOM   13802 C CA  . CYS B 2 580  ? 180.969 206.734 145.814 1.00 32.20  ? 580  CYS A CA  1 
ATOM   13803 C C   . CYS B 2 580  ? 179.932 207.843 145.900 1.00 32.20  ? 580  CYS A C   1 
ATOM   13804 O O   . CYS B 2 580  ? 179.272 208.004 146.935 1.00 32.20  ? 580  CYS A O   1 
ATOM   13805 C CB  . CYS B 2 580  ? 182.366 207.293 146.069 1.00 32.20  ? 580  CYS A CB  1 
ATOM   13806 S SG  . CYS B 2 580  ? 183.519 206.114 146.791 1.00 32.20  ? 580  CYS A SG  1 
ATOM   13807 N N   . PHE B 2 581  ? 179.761 208.613 144.825 1.00 33.58  ? 581  PHE A N   1 
ATOM   13808 C CA  . PHE B 2 581  ? 178.748 209.663 144.858 1.00 33.58  ? 581  PHE A CA  1 
ATOM   13809 C C   . PHE B 2 581  ? 177.327 209.127 144.966 1.00 33.58  ? 581  PHE A C   1 
ATOM   13810 O O   . PHE B 2 581  ? 176.409 209.915 145.205 1.00 33.58  ? 581  PHE A O   1 
ATOM   13811 C CB  . PHE B 2 581  ? 178.849 210.560 143.626 1.00 33.58  ? 581  PHE A CB  1 
ATOM   13812 C CG  . PHE B 2 581  ? 179.635 211.816 143.857 1.00 33.58  ? 581  PHE A CG  1 
ATOM   13813 C CD1 . PHE B 2 581  ? 179.236 212.725 144.823 1.00 33.58  ? 581  PHE A CD1 1 
ATOM   13814 C CD2 . PHE B 2 581  ? 180.748 212.105 143.090 1.00 33.58  ? 581  PHE A CD2 1 
ATOM   13815 C CE1 . PHE B 2 581  ? 179.947 213.885 145.037 1.00 33.58  ? 581  PHE A CE1 1 
ATOM   13816 C CE2 . PHE B 2 581  ? 181.461 213.268 143.297 1.00 33.58  ? 581  PHE A CE2 1 
ATOM   13817 C CZ  . PHE B 2 581  ? 181.061 214.158 144.273 1.00 33.58  ? 581  PHE A CZ  1 
ATOM   13818 N N   . PHE B 2 582  ? 177.117 207.825 144.774 1.00 33.00  ? 582  PHE A N   1 
ATOM   13819 C CA  . PHE B 2 582  ? 175.798 207.228 144.942 1.00 33.00  ? 582  PHE A CA  1 
ATOM   13820 C C   . PHE B 2 582  ? 175.564 206.734 146.363 1.00 33.00  ? 582  PHE A C   1 
ATOM   13821 O O   . PHE B 2 582  ? 174.442 206.339 146.694 1.00 33.00  ? 582  PHE A O   1 
ATOM   13822 C CB  . PHE B 2 582  ? 175.622 206.070 143.949 1.00 33.00  ? 582  PHE A CB  1 
ATOM   13823 C CG  . PHE B 2 582  ? 174.228 205.943 143.375 1.00 33.00  ? 582  PHE A CG  1 
ATOM   13824 C CD1 . PHE B 2 582  ? 173.113 205.873 144.190 1.00 33.00  ? 582  PHE A CD1 1 
ATOM   13825 C CD2 . PHE B 2 582  ? 174.043 205.890 142.004 1.00 33.00  ? 582  PHE A CD2 1 
ATOM   13826 C CE1 . PHE B 2 582  ? 171.842 205.748 143.653 1.00 33.00  ? 582  PHE A CE1 1 
ATOM   13827 C CE2 . PHE B 2 582  ? 172.773 205.770 141.460 1.00 33.00  ? 582  PHE A CE2 1 
ATOM   13828 C CZ  . PHE B 2 582  ? 171.674 205.699 142.288 1.00 33.00  ? 582  PHE A CZ  1 
ATOM   13829 N N   . LEU B 2 583  ? 176.587 206.763 147.217 1.00 31.33  ? 583  LEU A N   1 
ATOM   13830 C CA  . LEU B 2 583  ? 176.440 206.197 148.553 1.00 31.33  ? 583  LEU A CA  1 
ATOM   13831 C C   . LEU B 2 583  ? 175.596 207.100 149.443 1.00 31.33  ? 583  LEU A C   1 
ATOM   13832 O O   . LEU B 2 583  ? 174.938 206.613 150.370 1.00 31.33  ? 583  LEU A O   1 
ATOM   13833 C CB  . LEU B 2 583  ? 177.828 205.923 149.143 1.00 31.33  ? 583  LEU A CB  1 
ATOM   13834 C CG  . LEU B 2 583  ? 178.140 205.254 150.491 1.00 31.33  ? 583  LEU A CG  1 
ATOM   13835 C CD1 . LEU B 2 583  ? 179.644 205.150 150.598 1.00 31.33  ? 583  LEU A CD1 1 
ATOM   13836 C CD2 . LEU B 2 583  ? 177.602 205.955 151.737 1.00 31.33  ? 583  LEU A CD2 1 
ATOM   13837 N N   . PHE B 2 584  ? 175.577 208.407 149.161 1.00 33.99  ? 584  PHE A N   1 
ATOM   13838 C CA  . PHE B 2 584  ? 174.725 209.319 149.919 1.00 33.99  ? 584  PHE A CA  1 
ATOM   13839 C C   . PHE B 2 584  ? 173.259 208.894 149.853 1.00 33.99  ? 584  PHE A C   1 
ATOM   13840 O O   . PHE B 2 584  ? 172.518 209.082 150.824 1.00 33.99  ? 584  PHE A O   1 
ATOM   13841 C CB  . PHE B 2 584  ? 174.906 210.746 149.392 1.00 33.99  ? 584  PHE A CB  1 
ATOM   13842 C CG  . PHE B 2 584  ? 173.913 211.736 149.935 1.00 33.99  ? 584  PHE A CG  1 
ATOM   13843 C CD1 . PHE B 2 584  ? 173.619 211.785 151.287 1.00 33.99  ? 584  PHE A CD1 1 
ATOM   13844 C CD2 . PHE B 2 584  ? 173.282 212.634 149.089 1.00 33.99  ? 584  PHE A CD2 1 
ATOM   13845 C CE1 . PHE B 2 584  ? 172.705 212.699 151.782 1.00 33.99  ? 584  PHE A CE1 1 
ATOM   13846 C CE2 . PHE B 2 584  ? 172.371 213.553 149.579 1.00 33.99  ? 584  PHE A CE2 1 
ATOM   13847 C CZ  . PHE B 2 584  ? 172.083 213.586 150.924 1.00 33.99  ? 584  PHE A CZ  1 
ATOM   13848 N N   . PHE B 2 585  ? 172.836 208.297 148.737 1.00 32.31  ? 585  PHE A N   1 
ATOM   13849 C CA  . PHE B 2 585  ? 171.455 207.838 148.610 1.00 32.31  ? 585  PHE A CA  1 
ATOM   13850 C C   . PHE B 2 585  ? 171.140 206.736 149.617 1.00 32.31  ? 585  PHE A C   1 
ATOM   13851 O O   . PHE B 2 585  ? 170.050 206.710 150.200 1.00 32.31  ? 585  PHE A O   1 
ATOM   13852 C CB  . PHE B 2 585  ? 171.203 207.350 147.181 1.00 32.31  ? 585  PHE A CB  1 
ATOM   13853 C CG  . PHE B 2 585  ? 169.766 207.458 146.732 1.00 32.31  ? 585  PHE A CG  1 
ATOM   13854 C CD1 . PHE B 2 585  ? 168.765 207.818 147.617 1.00 32.31  ? 585  PHE A CD1 1 
ATOM   13855 C CD2 . PHE B 2 585  ? 169.422 207.194 145.416 1.00 32.31  ? 585  PHE A CD2 1 
ATOM   13856 C CE1 . PHE B 2 585  ? 167.450 207.912 147.196 1.00 32.31  ? 585  PHE A CE1 1 
ATOM   13857 C CE2 . PHE B 2 585  ? 168.113 207.286 144.991 1.00 32.31  ? 585  PHE A CE2 1 
ATOM   13858 C CZ  . PHE B 2 585  ? 167.124 207.645 145.881 1.00 32.31  ? 585  PHE A CZ  1 
ATOM   13859 N N   . GLY B 2 586  ? 172.084 205.828 149.846 1.00 34.80  ? 586  GLY A N   1 
ATOM   13860 C CA  . GLY B 2 586  ? 171.789 204.623 150.604 1.00 34.80  ? 586  GLY A CA  1 
ATOM   13861 C C   . GLY B 2 586  ? 171.920 204.815 152.109 1.00 34.80  ? 586  GLY A C   1 
ATOM   13862 O O   . GLY B 2 586  ? 172.845 205.461 152.600 1.00 34.80  ? 586  GLY A O   1 
ATOM   13863 N N   . ASN B 2 587  ? 170.963 204.237 152.842 1.00 39.42  ? 587  ASN A N   1 
ATOM   13864 C CA  . ASN B 2 587  ? 171.001 204.194 154.306 1.00 39.42  ? 587  ASN A CA  1 
ATOM   13865 C C   . ASN B 2 587  ? 170.257 202.929 154.737 1.00 39.42  ? 587  ASN A C   1 
ATOM   13866 O O   . ASN B 2 587  ? 169.037 202.947 154.915 1.00 39.42  ? 587  ASN A O   1 
ATOM   13867 C CB  . ASN B 2 587  ? 170.390 205.450 154.912 1.00 39.42  ? 587  ASN A CB  1 
ATOM   13868 C CG  . ASN B 2 587  ? 170.197 205.354 156.420 1.00 39.42  ? 587  ASN A CG  1 
ATOM   13869 O OD1 . ASN B 2 587  ? 170.719 204.453 157.076 1.00 39.42  ? 587  ASN A OD1 1 
ATOM   13870 N ND2 . ASN B 2 587  ? 169.439 206.294 156.972 1.00 39.42  ? 587  ASN A ND2 1 
ATOM   13871 N N   . SER B 2 588  ? 171.008 201.843 154.914 1.00 40.94  ? 588  SER A N   1 
ATOM   13872 C CA  . SER B 2 588  ? 170.493 200.564 155.390 1.00 40.94  ? 588  SER A CA  1 
ATOM   13873 C C   . SER B 2 588  ? 171.675 199.608 155.504 1.00 40.94  ? 588  SER A C   1 
ATOM   13874 O O   . SER B 2 588  ? 172.772 199.890 155.009 1.00 40.94  ? 588  SER A O   1 
ATOM   13875 C CB  . SER B 2 588  ? 169.424 199.974 154.469 1.00 40.94  ? 588  SER A CB  1 
ATOM   13876 O OG  . SER B 2 588  ? 168.509 199.173 155.199 1.00 40.94  ? 588  SER A OG  1 
ATOM   13877 N N   . GLU B 2 589  ? 171.445 198.473 156.166 1.00 41.57  ? 589  GLU A N   1 
ATOM   13878 C CA  . GLU B 2 589  ? 172.479 197.446 156.236 1.00 41.57  ? 589  GLU A CA  1 
ATOM   13879 C C   . GLU B 2 589  ? 172.738 196.839 154.865 1.00 41.57  ? 589  GLU A C   1 
ATOM   13880 O O   . GLU B 2 589  ? 173.889 196.765 154.409 1.00 41.57  ? 589  GLU A O   1 
ATOM   13881 C CB  . GLU B 2 589  ? 172.084 196.364 157.241 1.00 41.57  ? 589  GLU A CB  1 
ATOM   13882 C CG  . GLU B 2 589  ? 172.197 196.790 158.695 1.00 41.57  ? 589  GLU A CG  1 
ATOM   13883 C CD  . GLU B 2 589  ? 172.097 195.624 159.655 1.00 41.57  ? 589  GLU A CD  1 
ATOM   13884 O OE1 . GLU B 2 589  ? 172.979 194.738 159.607 1.00 41.57  ? 589  GLU A OE1 1 
ATOM   13885 O OE2 . GLU B 2 589  ? 171.142 195.590 160.459 1.00 41.57  ? 589  GLU A OE2 1 
ATOM   13886 N N   . SER B 2 590  ? 171.672 196.408 154.185 1.00 40.00  ? 590  SER A N   1 
ATOM   13887 C CA  . SER B 2 590  ? 171.823 195.850 152.847 1.00 40.00  ? 590  SER A CA  1 
ATOM   13888 C C   . SER B 2 590  ? 172.386 196.886 151.888 1.00 40.00  ? 590  SER A C   1 
ATOM   13889 O O   . SER B 2 590  ? 173.267 196.580 151.075 1.00 40.00  ? 590  SER A O   1 
ATOM   13890 C CB  . SER B 2 590  ? 170.482 195.325 152.343 1.00 40.00  ? 590  SER A CB  1 
ATOM   13891 O OG  . SER B 2 590  ? 170.484 195.205 150.929 1.00 40.00  ? 590  SER A OG  1 
ATOM   13892 N N   . ALA B 2 591  ? 171.897 198.123 151.971 1.00 38.30  ? 591  ALA A N   1 
ATOM   13893 C CA  . ALA B 2 591  ? 172.415 199.175 151.105 1.00 38.30  ? 591  ALA A CA  1 
ATOM   13894 C C   . ALA B 2 591  ? 173.901 199.407 151.348 1.00 38.30  ? 591  ALA A C   1 
ATOM   13895 O O   . ALA B 2 591  ? 174.683 199.501 150.396 1.00 38.30  ? 591  ALA A O   1 
ATOM   13896 C CB  . ALA B 2 591  ? 171.625 200.466 151.316 1.00 38.30  ? 591  ALA A CB  1 
ATOM   13897 N N   . MET B 2 592  ? 174.311 199.497 152.615 1.00 34.97  ? 592  MET A N   1 
ATOM   13898 C CA  . MET B 2 592  ? 175.716 199.762 152.914 1.00 34.97  ? 592  MET A CA  1 
ATOM   13899 C C   . MET B 2 592  ? 176.609 198.630 152.424 1.00 34.97  ? 592  MET A C   1 
ATOM   13900 O O   . MET B 2 592  ? 177.658 198.874 151.812 1.00 34.97  ? 592  MET A O   1 
ATOM   13901 C CB  . MET B 2 592  ? 175.906 199.987 154.414 1.00 34.97  ? 592  MET A CB  1 
ATOM   13902 C CG  . MET B 2 592  ? 177.171 200.753 154.798 1.00 34.97  ? 592  MET A CG  1 
ATOM   13903 S SD  . MET B 2 592  ? 177.480 202.389 154.080 1.00 34.97  ? 592  MET A SD  1 
ATOM   13904 C CE  . MET B 2 592  ? 175.838 203.027 153.749 1.00 34.97  ? 592  MET A CE  1 
ATOM   13905 N N   . ILE B 2 593  ? 176.211 197.381 152.675 1.00 34.36  ? 593  ILE A N   1 
ATOM   13906 C CA  . ILE B 2 593  ? 177.051 196.270 152.236 1.00 34.36  ? 593  ILE A CA  1 
ATOM   13907 C C   . ILE B 2 593  ? 177.093 196.206 150.712 1.00 34.36  ? 593  ILE A C   1 
ATOM   13908 O O   . ILE B 2 593  ? 178.140 195.902 150.121 1.00 34.36  ? 593  ILE A O   1 
ATOM   13909 C CB  . ILE B 2 593  ? 176.587 194.941 152.861 1.00 34.36  ? 593  ILE A CB  1 
ATOM   13910 C CG1 . ILE B 2 593  ? 177.546 193.816 152.481 1.00 34.36  ? 593  ILE A CG1 1 
ATOM   13911 C CG2 . ILE B 2 593  ? 175.188 194.580 152.428 1.00 34.36  ? 593  ILE A CG2 1 
ATOM   13912 C CD1 . ILE B 2 593  ? 178.721 193.686 153.410 1.00 34.36  ? 593  ILE A CD1 1 
ATOM   13913 N N   . GLY B 2 594  ? 175.984 196.527 150.045 1.00 33.72  ? 594  GLY A N   1 
ATOM   13914 C CA  . GLY B 2 594  ? 175.991 196.544 148.594 1.00 33.72  ? 594  GLY A CA  1 
ATOM   13915 C C   . GLY B 2 594  ? 176.907 197.608 148.027 1.00 33.72  ? 594  GLY A C   1 
ATOM   13916 O O   . GLY B 2 594  ? 177.658 197.350 147.079 1.00 33.72  ? 594  GLY A O   1 
ATOM   13917 N N   . TRP B 2 595  ? 176.860 198.817 148.590 1.00 32.89  ? 595  TRP A N   1 
ATOM   13918 C CA  . TRP B 2 595  ? 177.740 199.877 148.106 1.00 32.89  ? 595  TRP A CA  1 
ATOM   13919 C C   . TRP B 2 595  ? 179.198 199.530 148.364 1.00 32.89  ? 595  TRP A C   1 
ATOM   13920 O O   . TRP B 2 595  ? 180.065 199.805 147.523 1.00 32.89  ? 595  TRP A O   1 
ATOM   13921 C CB  . TRP B 2 595  ? 177.383 201.217 148.748 1.00 32.89  ? 595  TRP A CB  1 
ATOM   13922 C CG  . TRP B 2 595  ? 176.026 201.737 148.370 1.00 32.89  ? 595  TRP A CG  1 
ATOM   13923 C CD1 . TRP B 2 595  ? 175.010 202.062 149.218 1.00 32.89  ? 595  TRP A CD1 1 
ATOM   13924 C CD2 . TRP B 2 595  ? 175.531 201.973 147.046 1.00 32.89  ? 595  TRP A CD2 1 
ATOM   13925 N NE1 . TRP B 2 595  ? 173.918 202.491 148.510 1.00 32.89  ? 595  TRP A NE1 1 
ATOM   13926 C CE2 . TRP B 2 595  ? 174.211 202.446 147.174 1.00 32.89  ? 595  TRP A CE2 1 
ATOM   13927 C CE3 . TRP B 2 595  ? 176.077 201.835 145.767 1.00 32.89  ? 595  TRP A CE3 1 
ATOM   13928 C CZ2 . TRP B 2 595  ? 173.431 202.783 146.074 1.00 32.89  ? 595  TRP A CZ2 1 
ATOM   13929 C CZ3 . TRP B 2 595  ? 175.298 202.169 144.677 1.00 32.89  ? 595  TRP A CZ3 1 
ATOM   13930 C CH2 . TRP B 2 595  ? 173.991 202.636 144.837 1.00 32.89  ? 595  TRP A CH2 1 
ATOM   13931 N N   . GLN B 2 596  ? 179.489 198.917 149.514 1.00 32.76  ? 596  GLN A N   1 
ATOM   13932 C CA  . GLN B 2 596  ? 180.855 198.487 149.785 1.00 32.76  ? 596  GLN A CA  1 
ATOM   13933 C C   . GLN B 2 596  ? 181.319 197.464 148.759 1.00 32.76  ? 596  GLN A C   1 
ATOM   13934 O O   . GLN B 2 596  ? 182.441 197.547 148.243 1.00 32.76  ? 596  GLN A O   1 
ATOM   13935 C CB  . GLN B 2 596  ? 180.965 197.900 151.192 1.00 32.76  ? 596  GLN A CB  1 
ATOM   13936 C CG  . GLN B 2 596  ? 182.337 197.322 151.487 1.00 32.76  ? 596  GLN A CG  1 
ATOM   13937 C CD  . GLN B 2 596  ? 182.270 195.974 152.166 1.00 32.76  ? 596  GLN A CD  1 
ATOM   13938 O OE1 . GLN B 2 596  ? 181.662 195.038 151.647 1.00 32.76  ? 596  GLN A OE1 1 
ATOM   13939 N NE2 . GLN B 2 596  ? 182.904 195.861 153.325 1.00 32.76  ? 596  GLN A NE2 1 
ATOM   13940 N N   . CYS B 2 597  ? 180.464 196.487 148.448 1.00 30.31  ? 597  CYS A N   1 
ATOM   13941 C CA  . CYS B 2 597  ? 180.836 195.470 147.473 1.00 30.31  ? 597  CYS A CA  1 
ATOM   13942 C C   . CYS B 2 597  ? 181.079 196.087 146.102 1.00 30.31  ? 597  CYS A C   1 
ATOM   13943 O O   . CYS B 2 597  ? 182.059 195.750 145.431 1.00 30.31  ? 597  CYS A O   1 
ATOM   13944 C CB  . CYS B 2 597  ? 179.755 194.394 147.396 1.00 30.31  ? 597  CYS A CB  1 
ATOM   13945 S SG  . CYS B 2 597  ? 179.915 193.090 148.633 1.00 30.31  ? 597  CYS A SG  1 
ATOM   13946 N N   . LEU B 2 598  ? 180.206 197.003 145.675 1.00 29.68  ? 598  LEU A N   1 
ATOM   13947 C CA  . LEU B 2 598  ? 180.381 197.636 144.371 1.00 29.68  ? 598  LEU A CA  1 
ATOM   13948 C C   . LEU B 2 598  ? 181.684 198.425 144.310 1.00 29.68  ? 598  LEU A C   1 
ATOM   13949 O O   . LEU B 2 598  ? 182.455 198.297 143.347 1.00 29.68  ? 598  LEU A O   1 
ATOM   13950 C CB  . LEU B 2 598  ? 179.193 198.545 144.066 1.00 29.68  ? 598  LEU A CB  1 
ATOM   13951 C CG  . LEU B 2 598  ? 178.229 198.063 142.983 1.00 29.68  ? 598  LEU A CG  1 
ATOM   13952 C CD1 . LEU B 2 598  ? 176.975 198.918 142.967 1.00 29.68  ? 598  LEU A CD1 1 
ATOM   13953 C CD2 . LEU B 2 598  ? 178.908 198.076 141.625 1.00 29.68  ? 598  LEU A CD2 1 
ATOM   13954 N N   . PHE B 2 599  ? 181.948 199.246 145.332 1.00 30.19  ? 599  PHE A N   1 
ATOM   13955 C CA  . PHE B 2 599  ? 183.161 200.053 145.323 1.00 30.19  ? 599  PHE A CA  1 
ATOM   13956 C C   . PHE B 2 599  ? 184.408 199.178 145.333 1.00 30.19  ? 599  PHE A C   1 
ATOM   13957 O O   . PHE B 2 599  ? 185.354 199.431 144.578 1.00 30.19  ? 599  PHE A O   1 
ATOM   13958 C CB  . PHE B 2 599  ? 183.170 201.013 146.509 1.00 30.19  ? 599  PHE A CB  1 
ATOM   13959 C CG  . PHE B 2 599  ? 184.528 201.554 146.830 1.00 30.19  ? 599  PHE A CG  1 
ATOM   13960 C CD1 . PHE B 2 599  ? 185.071 202.575 146.072 1.00 30.19  ? 599  PHE A CD1 1 
ATOM   13961 C CD2 . PHE B 2 599  ? 185.263 201.043 147.882 1.00 30.19  ? 599  PHE A CD2 1 
ATOM   13962 C CE1 . PHE B 2 599  ? 186.323 203.075 146.359 1.00 30.19  ? 599  PHE A CE1 1 
ATOM   13963 C CE2 . PHE B 2 599  ? 186.515 201.539 148.172 1.00 30.19  ? 599  PHE A CE2 1 
ATOM   13964 C CZ  . PHE B 2 599  ? 187.045 202.557 147.410 1.00 30.19  ? 599  PHE A CZ  1 
ATOM   13965 N N   . CYS B 2 600  ? 184.434 198.146 146.178 1.00 32.50  ? 600  CYS A N   1 
ATOM   13966 C CA  . CYS B 2 600  ? 185.608 197.282 146.224 1.00 32.50  ? 600  CYS A CA  1 
ATOM   13967 C C   . CYS B 2 600  ? 185.783 196.519 144.918 1.00 32.50  ? 600  CYS A C   1 
ATOM   13968 O O   . CYS B 2 600  ? 186.915 196.286 144.477 1.00 32.50  ? 600  CYS A O   1 
ATOM   13969 C CB  . CYS B 2 600  ? 185.513 196.321 147.406 1.00 32.50  ? 600  CYS A CB  1 
ATOM   13970 S SG  . CYS B 2 600  ? 186.351 196.904 148.891 1.00 32.50  ? 600  CYS A SG  1 
ATOM   13971 N N   . GLY B 2 601  ? 184.678 196.132 144.276 1.00 31.88  ? 601  GLY A N   1 
ATOM   13972 C CA  . GLY B 2 601  ? 184.783 195.430 143.010 1.00 31.88  ? 601  GLY A CA  1 
ATOM   13973 C C   . GLY B 2 601  ? 185.346 196.297 141.904 1.00 31.88  ? 601  GLY A C   1 
ATOM   13974 O O   . GLY B 2 601  ? 186.120 195.825 141.065 1.00 31.88  ? 601  GLY A O   1 
ATOM   13975 N N   . THR B 2 602  ? 184.971 197.576 141.879 1.00 30.86  ? 602  THR A N   1 
ATOM   13976 C CA  . THR B 2 602  ? 185.497 198.466 140.849 1.00 30.86  ? 602  THR A CA  1 
ATOM   13977 C C   . THR B 2 602  ? 186.779 199.180 141.260 1.00 30.86  ? 602  THR A C   1 
ATOM   13978 O O   . THR B 2 602  ? 187.295 199.982 140.477 1.00 30.86  ? 602  THR A O   1 
ATOM   13979 C CB  . THR B 2 602  ? 184.451 199.506 140.443 1.00 30.86  ? 602  THR A CB  1 
ATOM   13980 O OG1 . THR B 2 602  ? 184.424 200.561 141.411 1.00 30.86  ? 602  THR A OG1 1 
ATOM   13981 C CG2 . THR B 2 602  ? 183.074 198.873 140.323 1.00 30.86  ? 602  THR A CG2 1 
ATOM   13982 N N   . SER B 2 603  ? 187.301 198.926 142.460 1.00 31.43  ? 603  SER A N   1 
ATOM   13983 C CA  . SER B 2 603  ? 188.563 199.524 142.882 1.00 31.43  ? 603  SER A CA  1 
ATOM   13984 C C   . SER B 2 603  ? 189.674 198.496 143.079 1.00 31.43  ? 603  SER A C   1 
ATOM   13985 O O   . SER B 2 603  ? 190.503 198.649 143.981 1.00 31.43  ? 603  SER A O   1 
ATOM   13986 C CB  . SER B 2 603  ? 188.358 200.329 144.163 1.00 31.43  ? 603  SER A CB  1 
ATOM   13987 O OG  . SER B 2 603  ? 189.563 200.425 144.902 1.00 31.43  ? 603  SER A OG  1 
ATOM   13988 N N   . ILE B 2 604  ? 189.717 197.448 142.253 1.00 33.64  ? 604  ILE A N   1 
ATOM   13989 C CA  . ILE B 2 604  ? 190.814 196.490 142.257 1.00 33.64  ? 604  ILE A CA  1 
ATOM   13990 C C   . ILE B 2 604  ? 191.594 196.520 140.948 1.00 33.64  ? 604  ILE A C   1 
ATOM   13991 O O   . ILE B 2 604  ? 192.823 196.350 140.942 1.00 33.64  ? 604  ILE A O   1 
ATOM   13992 C CB  . ILE B 2 604  ? 190.309 195.063 142.559 1.00 33.64  ? 604  ILE A CB  1 
ATOM   13993 C CG1 . ILE B 2 604  ? 191.474 194.075 142.607 1.00 33.64  ? 604  ILE A CG1 1 
ATOM   13994 C CG2 . ILE B 2 604  ? 189.268 194.629 141.542 1.00 33.64  ? 604  ILE A CG2 1 
ATOM   13995 C CD1 . ILE B 2 604  ? 192.608 194.501 143.517 1.00 33.64  ? 604  ILE A CD1 1 
ATOM   13996 N N   . ALA B 2 605  ? 190.905 196.738 139.826 1.00 35.54  ? 605  ALA A N   1 
ATOM   13997 C CA  . ALA B 2 605  ? 191.597 196.947 138.563 1.00 35.54  ? 605  ALA A CA  1 
ATOM   13998 C C   . ALA B 2 605  ? 192.516 198.154 138.647 1.00 35.54  ? 605  ALA A C   1 
ATOM   13999 O O   . ALA B 2 605  ? 193.605 198.159 138.062 1.00 35.54  ? 605  ALA A O   1 
ATOM   14000 C CB  . ALA B 2 605  ? 190.585 197.125 137.431 1.00 35.54  ? 605  ALA A CB  1 
ATOM   14001 N N   . ALA B 2 606  ? 192.091 199.187 139.378 1.00 32.56  ? 606  ALA A N   1 
ATOM   14002 C CA  . ALA B 2 606  ? 192.946 200.343 139.596 1.00 32.56  ? 606  ALA A CA  1 
ATOM   14003 C C   . ALA B 2 606  ? 194.244 199.945 140.285 1.00 32.56  ? 606  ALA A C   1 
ATOM   14004 O O   . ALA B 2 606  ? 195.331 200.340 139.850 1.00 32.56  ? 606  ALA A O   1 
ATOM   14005 C CB  . ALA B 2 606  ? 192.204 201.391 140.419 1.00 32.56  ? 606  ALA A CB  1 
ATOM   14006 N N   . TRP B 2 607  ? 194.151 199.149 141.351 1.00 34.10  ? 607  TRP A N   1 
ATOM   14007 C CA  . TRP B 2 607  ? 195.349 198.715 142.062 1.00 34.10  ? 607  TRP A CA  1 
ATOM   14008 C C   . TRP B 2 607  ? 196.255 197.890 141.163 1.00 34.10  ? 607  TRP A C   1 
ATOM   14009 O O   . TRP B 2 607  ? 197.481 198.057 141.175 1.00 34.10  ? 607  TRP A O   1 
ATOM   14010 C CB  . TRP B 2 607  ? 194.964 197.902 143.298 1.00 34.10  ? 607  TRP A CB  1 
ATOM   14011 C CG  . TRP B 2 607  ? 194.635 198.719 144.504 1.00 34.10  ? 607  TRP A CG  1 
ATOM   14012 C CD1 . TRP B 2 607  ? 193.471 198.701 145.210 1.00 34.10  ? 607  TRP A CD1 1 
ATOM   14013 C CD2 . TRP B 2 607  ? 195.485 199.667 145.162 1.00 34.10  ? 607  TRP A CD2 1 
ATOM   14014 N NE1 . TRP B 2 607  ? 193.537 199.581 146.258 1.00 34.10  ? 607  TRP A NE1 1 
ATOM   14015 C CE2 . TRP B 2 607  ? 194.765 200.186 146.251 1.00 34.10  ? 607  TRP A CE2 1 
ATOM   14016 C CE3 . TRP B 2 607  ? 196.786 200.128 144.932 1.00 34.10  ? 607  TRP A CE3 1 
ATOM   14017 C CZ2 . TRP B 2 607  ? 195.298 201.144 147.109 1.00 34.10  ? 607  TRP A CZ2 1 
ATOM   14018 C CZ3 . TRP B 2 607  ? 197.312 201.078 145.785 1.00 34.10  ? 607  TRP A CZ3 1 
ATOM   14019 C CH2 . TRP B 2 607  ? 196.570 201.576 146.861 1.00 34.10  ? 607  TRP A CH2 1 
ATOM   14020 N N   . ASN B 2 608  ? 195.672 196.982 140.380 1.00 33.21  ? 608  ASN A N   1 
ATOM   14021 C CA  . ASN B 2 608  ? 196.481 196.110 139.538 1.00 33.21  ? 608  ASN A CA  1 
ATOM   14022 C C   . ASN B 2 608  ? 197.206 196.904 138.455 1.00 33.21  ? 608  ASN A C   1 
ATOM   14023 O O   . ASN B 2 608  ? 198.412 196.725 138.228 1.00 33.21  ? 608  ASN A O   1 
ATOM   14024 C CB  . ASN B 2 608  ? 195.603 195.024 138.924 1.00 33.21  ? 608  ASN A CB  1 
ATOM   14025 C CG  . ASN B 2 608  ? 195.538 193.785 139.783 1.00 33.21  ? 608  ASN A CG  1 
ATOM   14026 O OD1 . ASN B 2 608  ? 196.439 192.955 139.762 1.00 33.21  ? 608  ASN A OD1 1 
ATOM   14027 N ND2 . ASN B 2 608  ? 194.467 193.660 140.557 1.00 33.21  ? 608  ASN A ND2 1 
ATOM   14028 N N   . ALA B 2 609  ? 196.481 197.796 137.776 1.00 32.81  ? 609  ALA A N   1 
ATOM   14029 C CA  . ALA B 2 609  ? 197.110 198.631 136.764 1.00 32.81  ? 609  ALA A CA  1 
ATOM   14030 C C   . ALA B 2 609  ? 198.164 199.534 137.385 1.00 32.81  ? 609  ALA A C   1 
ATOM   14031 O O   . ALA B 2 609  ? 199.194 199.812 136.764 1.00 32.81  ? 609  ALA A O   1 
ATOM   14032 C CB  . ALA B 2 609  ? 196.059 199.456 136.026 1.00 32.81  ? 609  ALA A CB  1 
ATOM   14033 N N   . LEU B 2 610  ? 197.932 199.990 138.618 1.00 34.34  ? 610  LEU A N   1 
ATOM   14034 C CA  . LEU B 2 610  ? 198.933 200.796 139.305 1.00 34.34  ? 610  LEU A CA  1 
ATOM   14035 C C   . LEU B 2 610  ? 200.205 199.997 139.554 1.00 34.34  ? 610  LEU A C   1 
ATOM   14036 O O   . LEU B 2 610  ? 201.313 200.497 139.328 1.00 34.34  ? 610  LEU A O   1 
ATOM   14037 C CB  . LEU B 2 610  ? 198.363 201.321 140.619 1.00 34.34  ? 610  LEU A CB  1 
ATOM   14038 C CG  . LEU B 2 610  ? 199.051 202.550 141.205 1.00 34.34  ? 610  LEU A CG  1 
ATOM   14039 C CD1 . LEU B 2 610  ? 199.345 203.558 140.111 1.00 34.34  ? 610  LEU A CD1 1 
ATOM   14040 C CD2 . LEU B 2 610  ? 198.184 203.166 142.287 1.00 34.34  ? 610  LEU A CD2 1 
ATOM   14041 N N   . ASP B 2 611  ? 200.062 198.753 140.008 1.00 34.50  ? 611  ASP A N   1 
ATOM   14042 C CA  . ASP B 2 611  ? 201.235 197.915 140.243 1.00 34.50  ? 611  ASP A CA  1 
ATOM   14043 C C   . ASP B 2 611  ? 202.014 197.702 138.954 1.00 34.50  ? 611  ASP A C   1 
ATOM   14044 O O   . ASP B 2 611  ? 203.246 197.813 138.931 1.00 34.50  ? 611  ASP A O   1 
ATOM   14045 C CB  . ASP B 2 611  ? 200.811 196.571 140.841 1.00 34.50  ? 611  ASP A CB  1 
ATOM   14046 C CG  . ASP B 2 611  ? 200.439 196.675 142.305 1.00 34.50  ? 611  ASP A CG  1 
ATOM   14047 O OD1 . ASP B 2 611  ? 200.837 197.666 142.953 1.00 34.50  ? 611  ASP A OD1 1 
ATOM   14048 O OD2 . ASP B 2 611  ? 199.750 195.766 142.813 1.00 34.50  ? 611  ASP A OD2 1 
ATOM   14049 N N   . VAL B 2 612  ? 201.307 197.418 137.862 1.00 32.84  ? 612  VAL A N   1 
ATOM   14050 C CA  . VAL B 2 612  ? 201.997 197.164 136.600 1.00 32.84  ? 612  VAL A CA  1 
ATOM   14051 C C   . VAL B 2 612  ? 202.689 198.425 136.088 1.00 32.84  ? 612  VAL A C   1 
ATOM   14052 O O   . VAL B 2 612  ? 203.848 198.378 135.656 1.00 32.84  ? 612  VAL A O   1 
ATOM   14053 C CB  . VAL B 2 612  ? 201.021 196.585 135.563 1.00 32.84  ? 612  VAL A CB  1 
ATOM   14054 C CG1 . VAL B 2 612  ? 201.618 196.668 134.173 1.00 32.84  ? 612  VAL A CG1 1 
ATOM   14055 C CG2 . VAL B 2 612  ? 200.716 195.148 135.913 1.00 32.84  ? 612  VAL A CG2 1 
ATOM   14056 N N   . ILE B 2 613  ? 202.006 199.572 136.137 1.00 33.03  ? 613  ILE A N   1 
ATOM   14057 C CA  . ILE B 2 613  ? 202.601 200.793 135.608 1.00 33.03  ? 613  ILE A CA  1 
ATOM   14058 C C   . ILE B 2 613  ? 203.745 201.274 136.491 1.00 33.03  ? 613  ILE A C   1 
ATOM   14059 O O   . ILE B 2 613  ? 204.654 201.962 136.016 1.00 33.03  ? 613  ILE A O   1 
ATOM   14060 C CB  . ILE B 2 613  ? 201.531 201.887 135.423 1.00 33.03  ? 613  ILE A CB  1 
ATOM   14061 C CG1 . ILE B 2 613  ? 202.093 203.063 134.627 1.00 33.03  ? 613  ILE A CG1 1 
ATOM   14062 C CG2 . ILE B 2 613  ? 201.038 202.390 136.762 1.00 33.03  ? 613  ILE A CG2 1 
ATOM   14063 C CD1 . ILE B 2 613  ? 202.358 202.749 133.183 1.00 33.03  ? 613  ILE A CD1 1 
ATOM   14064 N N   . THR B 2 614  ? 203.740 200.921 137.779 1.00 33.86  ? 614  THR A N   1 
ATOM   14065 C CA  . THR B 2 614  ? 204.831 201.343 138.647 1.00 33.86  ? 614  THR A CA  1 
ATOM   14066 C C   . THR B 2 614  ? 205.989 200.360 138.654 1.00 33.86  ? 614  THR A C   1 
ATOM   14067 O O   . THR B 2 614  ? 207.085 200.719 139.097 1.00 33.86  ? 614  THR A O   1 
ATOM   14068 C CB  . THR B 2 614  ? 204.332 201.552 140.076 1.00 33.86  ? 614  THR A CB  1 
ATOM   14069 O OG1 . THR B 2 614  ? 205.272 202.358 140.790 1.00 33.86  ? 614  THR A OG1 1 
ATOM   14070 C CG2 . THR B 2 614  ? 204.183 200.226 140.792 1.00 33.86  ? 614  THR A CG2 1 
ATOM   14071 N N   . VAL B 2 615  ? 205.778 199.132 138.181 1.00 33.52  ? 615  VAL A N   1 
ATOM   14072 C CA  . VAL B 2 615  ? 206.877 198.186 138.030 1.00 33.52  ? 615  VAL A CA  1 
ATOM   14073 C C   . VAL B 2 615  ? 207.472 198.205 136.625 1.00 33.52  ? 615  VAL A C   1 
ATOM   14074 O O   . VAL B 2 615  ? 208.609 197.745 136.444 1.00 33.52  ? 615  VAL A O   1 
ATOM   14075 C CB  . VAL B 2 615  ? 206.423 196.756 138.391 1.00 33.52  ? 615  VAL A CB  1 
ATOM   14076 C CG1 . VAL B 2 615  ? 205.755 196.097 137.205 1.00 33.52  ? 615  VAL A CG1 1 
ATOM   14077 C CG2 . VAL B 2 615  ? 207.593 195.932 138.874 1.00 33.52  ? 615  VAL A CG2 1 
ATOM   14078 N N   . GLU B 2 616  ? 206.749 198.727 135.635 1.00 36.47  ? 616  GLU A N   1 
ATOM   14079 C CA  . GLU B 2 616  ? 207.211 198.698 134.254 1.00 36.47  ? 616  GLU A CA  1 
ATOM   14080 C C   . GLU B 2 616  ? 208.060 199.903 133.873 1.00 36.47  ? 616  GLU A C   1 
ATOM   14081 O O   . GLU B 2 616  ? 208.863 199.805 132.939 1.00 36.47  ? 616  GLU A O   1 
ATOM   14082 C CB  . GLU B 2 616  ? 206.011 198.607 133.308 1.00 36.47  ? 616  GLU A CB  1 
ATOM   14083 C CG  . GLU B 2 616  ? 206.251 197.774 132.068 1.00 36.47  ? 616  GLU A CG  1 
ATOM   14084 C CD  . GLU B 2 616  ? 206.900 198.562 130.951 1.00 36.47  ? 616  GLU A CD  1 
ATOM   14085 O OE1 . GLU B 2 616  ? 206.811 199.807 130.980 1.00 36.47  ? 616  GLU A OE1 1 
ATOM   14086 O OE2 . GLU B 2 616  ? 207.493 197.939 130.046 1.00 36.47  ? 616  GLU A OE2 1 
ATOM   14087 N N   . LEU B 2 617  ? 207.909 201.029 134.571 1.00 35.99  ? 617  LEU A N   1 
ATOM   14088 C CA  . LEU B 2 617  ? 208.570 202.258 134.148 1.00 35.99  ? 617  LEU A CA  1 
ATOM   14089 C C   . LEU B 2 617  ? 210.067 202.215 134.430 1.00 35.99  ? 617  LEU A C   1 
ATOM   14090 O O   . LEU B 2 617  ? 210.890 202.299 133.511 1.00 35.99  ? 617  LEU A O   1 
ATOM   14091 C CB  . LEU B 2 617  ? 207.932 203.457 134.848 1.00 35.99  ? 617  LEU A CB  1 
ATOM   14092 C CG  . LEU B 2 617  ? 206.677 204.053 134.219 1.00 35.99  ? 617  LEU A CG  1 
ATOM   14093 C CD1 . LEU B 2 617  ? 205.915 204.864 135.247 1.00 35.99  ? 617  LEU A CD1 1 
ATOM   14094 C CD2 . LEU B 2 617  ? 207.045 204.907 133.027 1.00 35.99  ? 617  LEU A CD2 1 
ATOM   14095 N N   . TYR B 2 618  ? 210.437 202.083 135.699 1.00 37.72  ? 618  TYR A N   1 
ATOM   14096 C CA  . TYR B 2 618  ? 211.821 202.256 136.100 1.00 37.72  ? 618  TYR A CA  1 
ATOM   14097 C C   . TYR B 2 618  ? 212.684 201.089 135.624 1.00 37.72  ? 618  TYR A C   1 
ATOM   14098 O O   . TYR B 2 618  ? 212.204 199.961 135.489 1.00 37.72  ? 618  TYR A O   1 
ATOM   14099 C CB  . TYR B 2 618  ? 211.914 202.387 137.613 1.00 37.72  ? 618  TYR A CB  1 
ATOM   14100 C CG  . TYR B 2 618  ? 211.042 203.485 138.160 1.00 37.72  ? 618  TYR A CG  1 
ATOM   14101 C CD1 . TYR B 2 618  ? 211.377 204.814 137.974 1.00 37.72  ? 618  TYR A CD1 1 
ATOM   14102 C CD2 . TYR B 2 618  ? 209.873 203.193 138.839 1.00 37.72  ? 618  TYR A CD2 1 
ATOM   14103 C CE1 . TYR B 2 618  ? 210.582 205.822 138.463 1.00 37.72  ? 618  TYR A CE1 1 
ATOM   14104 C CE2 . TYR B 2 618  ? 209.070 204.197 139.329 1.00 37.72  ? 618  TYR A CE2 1 
ATOM   14105 C CZ  . TYR B 2 618  ? 209.430 205.507 139.142 1.00 37.72  ? 618  TYR A CZ  1 
ATOM   14106 O OH  . TYR B 2 618  ? 208.630 206.510 139.630 1.00 37.72  ? 618  TYR A OH  1 
ATOM   14107 N N   . PRO B 2 619  ? 213.967 201.338 135.360 1.00 41.47  ? 619  PRO A N   1 
ATOM   14108 C CA  . PRO B 2 619  ? 214.875 200.241 135.002 1.00 41.47  ? 619  PRO A CA  1 
ATOM   14109 C C   . PRO B 2 619  ? 215.144 199.310 136.171 1.00 41.47  ? 619  PRO A C   1 
ATOM   14110 O O   . PRO B 2 619  ? 214.675 199.546 137.288 1.00 41.47  ? 619  PRO A O   1 
ATOM   14111 C CB  . PRO B 2 619  ? 216.153 200.970 134.563 1.00 41.47  ? 619  PRO A CB  1 
ATOM   14112 C CG  . PRO B 2 619  ? 215.720 202.356 134.245 1.00 41.47  ? 619  PRO A CG  1 
ATOM   14113 C CD  . PRO B 2 619  ? 214.599 202.653 135.186 1.00 41.47  ? 619  PRO A CD  1 
ATOM   14114 N N   . THR B 2 620  ? 215.910 198.250 135.922 1.00 43.94  ? 620  THR A N   1 
ATOM   14115 C CA  . THR B 2 620  ? 216.196 197.264 136.955 1.00 43.94  ? 620  THR A CA  1 
ATOM   14116 C C   . THR B 2 620  ? 217.158 197.772 138.020 1.00 43.94  ? 620  THR A C   1 
ATOM   14117 O O   . THR B 2 620  ? 217.304 197.113 139.055 1.00 43.94  ? 620  THR A O   1 
ATOM   14118 C CB  . THR B 2 620  ? 216.758 195.996 136.324 1.00 43.94  ? 620  THR A CB  1 
ATOM   14119 O OG1 . THR B 2 620  ? 217.010 195.021 137.343 1.00 43.94  ? 620  THR A OG1 1 
ATOM   14120 C CG2 . THR B 2 620  ? 218.044 196.307 135.585 1.00 43.94  ? 620  THR A CG2 1 
ATOM   14121 N N   . ASN B 2 621  ? 217.823 198.901 137.794 1.00 42.63  ? 621  ASN A N   1 
ATOM   14122 C CA  . ASN B 2 621  ? 218.719 199.461 138.795 1.00 42.63  ? 621  ASN A CA  1 
ATOM   14123 C C   . ASN B 2 621  ? 218.033 200.458 139.721 1.00 42.63  ? 621  ASN A C   1 
ATOM   14124 O O   . ASN B 2 621  ? 218.676 200.956 140.651 1.00 42.63  ? 621  ASN A O   1 
ATOM   14125 C CB  . ASN B 2 621  ? 219.917 200.133 138.118 1.00 42.63  ? 621  ASN A CB  1 
ATOM   14126 C CG  . ASN B 2 621  ? 221.240 199.667 138.690 1.00 42.63  ? 621  ASN A CG  1 
ATOM   14127 O OD1 . ASN B 2 621  ? 221.277 198.957 139.694 1.00 42.63  ? 621  ASN A OD1 1 
ATOM   14128 N ND2 . ASN B 2 621  ? 222.334 200.065 138.053 1.00 42.63  ? 621  ASN A ND2 1 
ATOM   14129 N N   . GLN B 2 622  ? 216.754 200.759 139.492 1.00 41.37  ? 622  GLN A N   1 
ATOM   14130 C CA  . GLN B 2 622  ? 216.012 201.656 140.364 1.00 41.37  ? 622  GLN A CA  1 
ATOM   14131 C C   . GLN B 2 622  ? 214.619 201.150 140.703 1.00 41.37  ? 622  GLN A C   1 
ATOM   14132 O O   . GLN B 2 622  ? 213.893 201.841 141.422 1.00 41.37  ? 622  GLN A O   1 
ATOM   14133 C CB  . GLN B 2 622  ? 215.892 203.048 139.728 1.00 41.37  ? 622  GLN A CB  1 
ATOM   14134 C CG  . GLN B 2 622  ? 217.213 203.694 139.389 1.00 41.37  ? 622  GLN A CG  1 
ATOM   14135 C CD  . GLN B 2 622  ? 217.245 204.217 137.976 1.00 41.37  ? 622  GLN A CD  1 
ATOM   14136 O OE1 . GLN B 2 622  ? 216.219 204.614 137.430 1.00 41.37  ? 622  GLN A OE1 1 
ATOM   14137 N NE2 . GLN B 2 622  ? 218.424 204.212 137.367 1.00 41.37  ? 622  GLN A NE2 1 
ATOM   14138 N N   . ARG B 2 623  ? 214.225 199.973 140.215 1.00 38.07  ? 623  ARG A N   1 
ATOM   14139 C CA  . ARG B 2 623  ? 212.839 199.539 140.340 1.00 38.07  ? 623  ARG A CA  1 
ATOM   14140 C C   . ARG B 2 623  ? 212.466 199.275 141.794 1.00 38.07  ? 623  ARG A C   1 
ATOM   14141 O O   . ARG B 2 623  ? 211.421 199.737 142.269 1.00 38.07  ? 623  ARG A O   1 
ATOM   14142 C CB  . ARG B 2 623  ? 212.614 198.296 139.487 1.00 38.07  ? 623  ARG A CB  1 
ATOM   14143 C CG  . ARG B 2 623  ? 211.274 197.631 139.681 1.00 38.07  ? 623  ARG A CG  1 
ATOM   14144 C CD  . ARG B 2 623  ? 211.104 196.500 138.690 1.00 38.07  ? 623  ARG A CD  1 
ATOM   14145 N NE  . ARG B 2 623  ? 211.100 196.976 137.312 1.00 38.07  ? 623  ARG A NE  1 
ATOM   14146 C CZ  . ARG B 2 623  ? 212.061 196.731 136.434 1.00 38.07  ? 623  ARG A CZ  1 
ATOM   14147 N NH1 . ARG B 2 623  ? 213.129 196.025 136.759 1.00 38.07  ? 623  ARG A NH1 1 
ATOM   14148 N NH2 . ARG B 2 623  ? 211.946 197.205 135.197 1.00 38.07  ? 623  ARG A NH2 1 
ATOM   14149 N N   . ALA B 2 624  ? 213.313 198.542 142.517 1.00 38.46  ? 624  ALA A N   1 
ATOM   14150 C CA  . ALA B 2 624  ? 213.001 198.212 143.904 1.00 38.46  ? 624  ALA A CA  1 
ATOM   14151 C C   . ALA B 2 624  ? 212.903 199.465 144.764 1.00 38.46  ? 624  ALA A C   1 
ATOM   14152 O O   . ALA B 2 624  ? 211.997 199.583 145.594 1.00 38.46  ? 624  ALA A O   1 
ATOM   14153 C CB  . ALA B 2 624  ? 214.050 197.256 144.469 1.00 38.46  ? 624  ALA A CB  1 
ATOM   14154 N N   . THR B 2 625  ? 213.815 200.422 144.566 1.00 37.41  ? 625  THR A N   1 
ATOM   14155 C CA  . THR B 2 625  ? 213.822 201.626 145.394 1.00 37.41  ? 625  THR A CA  1 
ATOM   14156 C C   . THR B 2 625  ? 212.566 202.460 145.172 1.00 37.41  ? 625  THR A C   1 
ATOM   14157 O O   . THR B 2 625  ? 211.914 202.889 146.133 1.00 37.41  ? 625  THR A O   1 
ATOM   14158 C CB  . THR B 2 625  ? 215.073 202.453 145.098 1.00 37.41  ? 625  THR A CB  1 
ATOM   14159 O OG1 . THR B 2 625  ? 216.238 201.727 145.502 1.00 37.41  ? 625  THR A OG1 1 
ATOM   14160 C CG2 . THR B 2 625  ? 215.021 203.771 145.846 1.00 37.41  ? 625  THR A CG2 1 
ATOM   14161 N N   . ALA B 2 626  ? 212.220 202.708 143.910 1.00 35.31  ? 626  ALA A N   1 
ATOM   14162 C CA  . ALA B 2 626  ? 211.042 203.516 143.620 1.00 35.31  ? 626  ALA A CA  1 
ATOM   14163 C C   . ALA B 2 626  ? 209.767 202.815 144.063 1.00 35.31  ? 626  ALA A C   1 
ATOM   14164 O O   . ALA B 2 626  ? 208.863 203.451 144.626 1.00 35.31  ? 626  ALA A O   1 
ATOM   14165 C CB  . ALA B 2 626  ? 210.986 203.847 142.133 1.00 35.31  ? 626  ALA A CB  1 
ATOM   14166 N N   . PHE B 2 627  ? 209.673 201.504 143.829 1.00 33.60  ? 627  PHE A N   1 
ATOM   14167 C CA  . PHE B 2 627  ? 208.515 200.767 144.324 1.00 33.60  ? 627  PHE A CA  1 
ATOM   14168 C C   . PHE B 2 627  ? 208.429 200.854 145.841 1.00 33.60  ? 627  PHE A C   1 
ATOM   14169 O O   . PHE B 2 627  ? 207.334 200.973 146.402 1.00 33.60  ? 627  PHE A O   1 
ATOM   14170 C CB  . PHE B 2 627  ? 208.585 199.312 143.868 1.00 33.60  ? 627  PHE A CB  1 
ATOM   14171 C CG  . PHE B 2 627  ? 207.242 198.682 143.631 1.00 33.60  ? 627  PHE A CG  1 
ATOM   14172 C CD1 . PHE B 2 627  ? 206.207 198.856 144.534 1.00 33.60  ? 627  PHE A CD1 1 
ATOM   14173 C CD2 . PHE B 2 627  ? 207.014 197.918 142.503 1.00 33.60  ? 627  PHE A CD2 1 
ATOM   14174 C CE1 . PHE B 2 627  ? 204.976 198.281 144.318 1.00 33.60  ? 627  PHE A CE1 1 
ATOM   14175 C CE2 . PHE B 2 627  ? 205.782 197.341 142.281 1.00 33.60  ? 627  PHE A CE2 1 
ATOM   14176 C CZ  . PHE B 2 627  ? 204.763 197.521 143.190 1.00 33.60  ? 627  PHE A CZ  1 
ATOM   14177 N N   . GLY B 2 628  ? 209.572 200.819 146.522 1.00 34.33  ? 628  GLY A N   1 
ATOM   14178 C CA  . GLY B 2 628  ? 209.559 200.912 147.970 1.00 34.33  ? 628  GLY A CA  1 
ATOM   14179 C C   . GLY B 2 628  ? 209.079 202.259 148.474 1.00 34.33  ? 628  GLY A C   1 
ATOM   14180 O O   . GLY B 2 628  ? 208.283 202.329 149.415 1.00 34.33  ? 628  GLY A O   1 
ATOM   14181 N N   . ILE B 2 629  ? 209.557 203.348 147.867 1.00 32.38  ? 629  ILE A N   1 
ATOM   14182 C CA  . ILE B 2 629  ? 209.101 204.660 148.311 1.00 32.38  ? 629  ILE A CA  1 
ATOM   14183 C C   . ILE B 2 629  ? 207.616 204.843 148.006 1.00 32.38  ? 629  ILE A C   1 
ATOM   14184 O O   . ILE B 2 629  ? 206.875 205.438 148.800 1.00 32.38  ? 629  ILE A O   1 
ATOM   14185 C CB  . ILE B 2 629  ? 209.963 205.792 147.713 1.00 32.38  ? 629  ILE A CB  1 
ATOM   14186 C CG1 . ILE B 2 629  ? 209.523 206.156 146.292 1.00 32.38  ? 629  ILE A CG1 1 
ATOM   14187 C CG2 . ILE B 2 629  ? 211.439 205.447 147.784 1.00 32.38  ? 629  ILE A CG2 1 
ATOM   14188 C CD1 . ILE B 2 629  ? 210.075 207.467 145.799 1.00 32.38  ? 629  ILE A CD1 1 
ATOM   14189 N N   . LEU B 2 630  ? 207.146 204.307 146.877 1.00 33.80  ? 630  LEU A N   1 
ATOM   14190 C CA  . LEU B 2 630  ? 205.724 204.426 146.569 1.00 33.80  ? 630  LEU A CA  1 
ATOM   14191 C C   . LEU B 2 630  ? 204.880 203.603 147.532 1.00 33.80  ? 630  LEU A C   1 
ATOM   14192 O O   . LEU B 2 630  ? 203.788 204.027 147.924 1.00 33.80  ? 630  LEU A O   1 
ATOM   14193 C CB  . LEU B 2 630  ? 205.460 204.018 145.122 1.00 33.80  ? 630  LEU A CB  1 
ATOM   14194 C CG  . LEU B 2 630  ? 206.005 204.995 144.078 1.00 33.80  ? 630  LEU A CG  1 
ATOM   14195 C CD1 . LEU B 2 630  ? 205.299 204.809 142.757 1.00 33.80  ? 630  LEU A CD1 1 
ATOM   14196 C CD2 . LEU B 2 630  ? 205.868 206.427 144.556 1.00 33.80  ? 630  LEU A CD2 1 
ATOM   14197 N N   . ASN B 2 631  ? 205.371 202.431 147.940 1.00 35.31  ? 631  ASN A N   1 
ATOM   14198 C CA  . ASN B 2 631  ? 204.643 201.635 148.923 1.00 35.31  ? 631  ASN A CA  1 
ATOM   14199 C C   . ASN B 2 631  ? 204.626 202.319 150.285 1.00 35.31  ? 631  ASN A C   1 
ATOM   14200 O O   . ASN B 2 631  ? 203.626 202.247 151.012 1.00 35.31  ? 631  ASN A O   1 
ATOM   14201 C CB  . ASN B 2 631  ? 205.258 200.241 149.024 1.00 35.31  ? 631  ASN A CB  1 
ATOM   14202 C CG  . ASN B 2 631  ? 204.575 199.380 150.055 1.00 35.31  ? 631  ASN A CG  1 
ATOM   14203 O OD1 . ASN B 2 631  ? 204.997 199.315 151.208 1.00 35.31  ? 631  ASN A OD1 1 
ATOM   14204 N ND2 . ASN B 2 631  ? 203.505 198.709 149.647 1.00 35.31  ? 631  ASN A ND2 1 
ATOM   14205 N N   . GLY B 2 632  ? 205.724 202.980 150.651 1.00 36.21  ? 632  GLY A N   1 
ATOM   14206 C CA  . GLY B 2 632  ? 205.726 203.755 151.882 1.00 36.21  ? 632  GLY A CA  1 
ATOM   14207 C C   . GLY B 2 632  ? 204.712 204.881 151.855 1.00 36.21  ? 632  GLY A C   1 
ATOM   14208 O O   . GLY B 2 632  ? 203.989 205.108 152.831 1.00 36.21  ? 632  GLY A O   1 
ATOM   14209 N N   . LEU B 2 633  ? 204.628 205.594 150.729 1.00 33.20  ? 633  LEU A N   1 
ATOM   14210 C CA  . LEU B 2 633  ? 203.613 206.635 150.597 1.00 33.20  ? 633  LEU A CA  1 
ATOM   14211 C C   . LEU B 2 633  ? 202.211 206.040 150.632 1.00 33.20  ? 633  LEU A C   1 
ATOM   14212 O O   . LEU B 2 633  ? 201.278 206.654 151.166 1.00 33.20  ? 633  LEU A O   1 
ATOM   14213 C CB  . LEU B 2 633  ? 203.838 207.426 149.311 1.00 33.20  ? 633  LEU A CB  1 
ATOM   14214 C CG  . LEU B 2 633  ? 204.577 208.756 149.478 1.00 33.20  ? 633  LEU A CG  1 
ATOM   14215 C CD1 . LEU B 2 633  ? 205.836 208.579 150.309 1.00 33.20  ? 633  LEU A CD1 1 
ATOM   14216 C CD2 . LEU B 2 633  ? 204.915 209.345 148.123 1.00 33.20  ? 633  LEU A CD2 1 
ATOM   14217 N N   . CYS B 2 634  ? 202.041 204.845 150.062 1.00 34.43  ? 634  CYS A N   1 
ATOM   14218 C CA  . CYS B 2 634  ? 200.759 204.152 150.144 1.00 34.43  ? 634  CYS A CA  1 
ATOM   14219 C C   . CYS B 2 634  ? 200.374 203.870 151.588 1.00 34.43  ? 634  CYS A C   1 
ATOM   14220 O O   . CYS B 2 634  ? 199.224 204.081 151.987 1.00 34.43  ? 634  CYS A O   1 
ATOM   14221 C CB  . CYS B 2 634  ? 200.826 202.853 149.344 1.00 34.43  ? 634  CYS A CB  1 
ATOM   14222 S SG  . CYS B 2 634  ? 199.511 201.669 149.686 1.00 34.43  ? 634  CYS A SG  1 
ATOM   14223 N N   . LYS B 2 635  ? 201.324 203.397 152.392 1.00 35.74  ? 635  LYS A N   1 
ATOM   14224 C CA  . LYS B 2 635  ? 201.023 203.144 153.799 1.00 35.74  ? 635  LYS A CA  1 
ATOM   14225 C C   . LYS B 2 635  ? 200.722 204.441 154.541 1.00 35.74  ? 635  LYS A C   1 
ATOM   14226 O O   . LYS B 2 635  ? 199.878 204.468 155.447 1.00 35.74  ? 635  LYS A O   1 
ATOM   14227 C CB  . LYS B 2 635  ? 202.178 202.394 154.453 1.00 35.74  ? 635  LYS A CB  1 
ATOM   14228 C CG  . LYS B 2 635  ? 202.197 200.911 154.138 1.00 35.74  ? 635  LYS A CG  1 
ATOM   14229 C CD  . LYS B 2 635  ? 200.795 200.328 154.118 1.00 35.74  ? 635  LYS A CD  1 
ATOM   14230 C CE  . LYS B 2 635  ? 200.714 199.115 153.202 1.00 35.74  ? 635  LYS A CE  1 
ATOM   14231 N NZ  . LYS B 2 635  ? 201.822 198.147 153.446 1.00 35.74  ? 635  LYS A NZ  1 
ATOM   14232 N N   . PHE B 2 636  ? 201.406 205.525 154.174 1.00 35.29  ? 636  PHE A N   1 
ATOM   14233 C CA  . PHE B 2 636  ? 201.128 206.823 154.782 1.00 35.29  ? 636  PHE A CA  1 
ATOM   14234 C C   . PHE B 2 636  ? 199.697 207.260 154.490 1.00 35.29  ? 636  PHE A C   1 
ATOM   14235 O O   . PHE B 2 636  ? 198.969 207.721 155.386 1.00 35.29  ? 636  PHE A O   1 
ATOM   14236 C CB  . PHE B 2 636  ? 202.135 207.849 154.260 1.00 35.29  ? 636  PHE A CB  1 
ATOM   14237 C CG  . PHE B 2 636  ? 201.762 209.272 154.521 1.00 35.29  ? 636  PHE A CG  1 
ATOM   14238 C CD1 . PHE B 2 636  ? 201.792 209.780 155.810 1.00 35.29  ? 636  PHE A CD1 1 
ATOM   14239 C CD2 . PHE B 2 636  ? 201.407 210.112 153.481 1.00 35.29  ? 636  PHE A CD2 1 
ATOM   14240 C CE1 . PHE B 2 636  ? 201.469 211.098 156.056 1.00 35.29  ? 636  PHE A CE1 1 
ATOM   14241 C CE2 . PHE B 2 636  ? 201.076 211.432 153.724 1.00 35.29  ? 636  PHE A CE2 1 
ATOM   14242 C CZ  . PHE B 2 636  ? 201.105 211.922 155.013 1.00 35.29  ? 636  PHE A CZ  1 
ATOM   14243 N N   . GLY B 2 637  ? 199.268 207.101 153.239 1.00 33.92  ? 637  GLY A N   1 
ATOM   14244 C CA  . GLY B 2 637  ? 197.883 207.371 152.898 1.00 33.92  ? 637  GLY A CA  1 
ATOM   14245 C C   . GLY B 2 637  ? 196.911 206.457 153.616 1.00 33.92  ? 637  GLY A C   1 
ATOM   14246 O O   . GLY B 2 637  ? 195.803 206.873 153.963 1.00 33.92  ? 637  GLY A O   1 
ATOM   14247 N N   . ALA B 2 638  ? 197.304 205.202 153.836 1.00 33.94  ? 638  ALA A N   1 
ATOM   14248 C CA  . ALA B 2 638  ? 196.464 204.292 154.605 1.00 33.94  ? 638  ALA A CA  1 
ATOM   14249 C C   . ALA B 2 638  ? 196.254 204.810 156.019 1.00 33.94  ? 638  ALA A C   1 
ATOM   14250 O O   . ALA B 2 638  ? 195.135 204.785 156.538 1.00 33.94  ? 638  ALA A O   1 
ATOM   14251 C CB  . ALA B 2 638  ? 197.088 202.900 154.635 1.00 33.94  ? 638  ALA A CB  1 
ATOM   14252 N N   . ILE B 2 639  ? 197.326 205.290 156.656 1.00 33.41  ? 639  ILE A N   1 
ATOM   14253 C CA  . ILE B 2 639  ? 197.196 205.894 157.982 1.00 33.41  ? 639  ILE A CA  1 
ATOM   14254 C C   . ILE B 2 639  ? 196.225 207.064 157.937 1.00 33.41  ? 639  ILE A C   1 
ATOM   14255 O O   . ILE B 2 639  ? 195.291 207.152 158.747 1.00 33.41  ? 639  ILE A O   1 
ATOM   14256 C CB  . ILE B 2 639  ? 198.573 206.332 158.515 1.00 33.41  ? 639  ILE A CB  1 
ATOM   14257 C CG1 . ILE B 2 639  ? 199.256 205.176 159.235 1.00 33.41  ? 639  ILE A CG1 1 
ATOM   14258 C CG2 . ILE B 2 639  ? 198.436 207.520 159.454 1.00 33.41  ? 639  ILE A CG2 1 
ATOM   14259 C CD1 . ILE B 2 639  ? 198.707 204.931 160.624 1.00 33.41  ? 639  ILE A CD1 1 
ATOM   14260 N N   . LEU B 2 640  ? 196.425 207.972 156.979 1.00 32.61  ? 640  LEU A N   1 
ATOM   14261 C CA  . LEU B 2 640  ? 195.587 209.168 156.917 1.00 32.61  ? 640  LEU A CA  1 
ATOM   14262 C C   . LEU B 2 640  ? 194.115 208.808 156.749 1.00 32.61  ? 640  LEU A C   1 
ATOM   14263 O O   . LEU B 2 640  ? 193.249 209.323 157.467 1.00 32.61  ? 640  LEU A O   1 
ATOM   14264 C CB  . LEU B 2 640  ? 196.049 210.085 155.785 1.00 32.61  ? 640  LEU A CB  1 
ATOM   14265 C CG  . LEU B 2 640  ? 197.121 211.129 156.107 1.00 32.61  ? 640  LEU A CG  1 
ATOM   14266 C CD1 . LEU B 2 640  ? 196.494 212.290 156.853 1.00 32.61  ? 640  LEU A CD1 1 
ATOM   14267 C CD2 . LEU B 2 640  ? 198.241 210.532 156.931 1.00 32.61  ? 640  LEU A CD2 1 
ATOM   14268 N N   . GLY B 2 641  ? 193.815 207.916 155.806 1.00 32.46  ? 641  GLY A N   1 
ATOM   14269 C CA  . GLY B 2 641  ? 192.429 207.554 155.563 1.00 32.46  ? 641  GLY A CA  1 
ATOM   14270 C C   . GLY B 2 641  ? 191.806 206.810 156.727 1.00 32.46  ? 641  GLY A C   1 
ATOM   14271 O O   . GLY B 2 641  ? 190.705 207.145 157.176 1.00 32.46  ? 641  GLY A O   1 
ATOM   14272 N N   . ASN B 2 642  ? 192.502 205.796 157.240 1.00 33.56  ? 642  ASN A N   1 
ATOM   14273 C CA  . ASN B 2 642  ? 191.944 204.988 158.310 1.00 33.56  ? 642  ASN A CA  1 
ATOM   14274 C C   . ASN B 2 642  ? 191.832 205.776 159.608 1.00 33.56  ? 642  ASN A C   1 
ATOM   14275 O O   . ASN B 2 642  ? 191.126 205.346 160.523 1.00 33.56  ? 642  ASN A O   1 
ATOM   14276 C CB  . ASN B 2 642  ? 192.806 203.735 158.488 1.00 33.56  ? 642  ASN A CB  1 
ATOM   14277 C CG  . ASN B 2 642  ? 192.123 202.652 159.297 1.00 33.56  ? 642  ASN A CG  1 
ATOM   14278 O OD1 . ASN B 2 642  ? 191.070 202.863 159.892 1.00 33.56  ? 642  ASN A OD1 1 
ATOM   14279 N ND2 . ASN B 2 642  ? 192.729 201.472 159.317 1.00 33.56  ? 642  ASN A ND2 1 
ATOM   14280 N N   . THR B 2 643  ? 192.494 206.930 159.708 1.00 32.73  ? 643  THR A N   1 
ATOM   14281 C CA  . THR B 2 643  ? 192.230 207.815 160.833 1.00 32.73  ? 643  THR A CA  1 
ATOM   14282 C C   . THR B 2 643  ? 191.041 208.734 160.563 1.00 32.73  ? 643  THR A C   1 
ATOM   14283 O O   . THR B 2 643  ? 190.083 208.763 161.346 1.00 32.73  ? 643  THR A O   1 
ATOM   14284 C CB  . THR B 2 643  ? 193.474 208.647 161.157 1.00 32.73  ? 643  THR A CB  1 
ATOM   14285 O OG1 . THR B 2 643  ? 194.413 207.839 161.872 1.00 32.73  ? 643  THR A OG1 1 
ATOM   14286 C CG2 . THR B 2 643  ? 193.104 209.852 162.004 1.00 32.73  ? 643  THR A CG2 1 
ATOM   14287 N N   . ILE B 2 644  ? 191.077 209.474 159.451 1.00 31.26  ? 644  ILE A N   1 
ATOM   14288 C CA  . ILE B 2 644  ? 190.067 210.499 159.209 1.00 31.26  ? 644  ILE A CA  1 
ATOM   14289 C C   . ILE B 2 644  ? 188.687 209.875 159.044 1.00 31.26  ? 644  ILE A C   1 
ATOM   14290 O O   . ILE B 2 644  ? 187.720 210.295 159.692 1.00 31.26  ? 644  ILE A O   1 
ATOM   14291 C CB  . ILE B 2 644  ? 190.447 211.352 157.986 1.00 31.26  ? 644  ILE A CB  1 
ATOM   14292 C CG1 . ILE B 2 644  ? 191.589 212.301 158.335 1.00 31.26  ? 644  ILE A CG1 1 
ATOM   14293 C CG2 . ILE B 2 644  ? 189.245 212.135 157.490 1.00 31.26  ? 644  ILE A CG2 1 
ATOM   14294 C CD1 . ILE B 2 644  ? 191.956 213.248 157.215 1.00 31.26  ? 644  ILE A CD1 1 
ATOM   14295 N N   . PHE B 2 645  ? 188.569 208.860 158.181 1.00 31.61  ? 645  PHE A N   1 
ATOM   14296 C CA  . PHE B 2 645  ? 187.262 208.266 157.918 1.00 31.61  ? 645  PHE A CA  1 
ATOM   14297 C C   . PHE B 2 645  ? 186.692 207.600 159.162 1.00 31.61  ? 645  PHE A C   1 
ATOM   14298 O O   . PHE B 2 645  ? 185.491 207.706 159.433 1.00 31.61  ? 645  PHE A O   1 
ATOM   14299 C CB  . PHE B 2 645  ? 187.364 207.255 156.782 1.00 31.61  ? 645  PHE A CB  1 
ATOM   14300 C CG  . PHE B 2 645  ? 187.346 207.872 155.422 1.00 31.61  ? 645  PHE A CG  1 
ATOM   14301 C CD1 . PHE B 2 645  ? 186.149 208.122 154.780 1.00 31.61  ? 645  PHE A CD1 1 
ATOM   14302 C CD2 . PHE B 2 645  ? 188.525 208.208 154.787 1.00 31.61  ? 645  PHE A CD2 1 
ATOM   14303 C CE1 . PHE B 2 645  ? 186.132 208.689 153.528 1.00 31.61  ? 645  PHE A CE1 1 
ATOM   14304 C CE2 . PHE B 2 645  ? 188.511 208.776 153.537 1.00 31.61  ? 645  PHE A CE2 1 
ATOM   14305 C CZ  . PHE B 2 645  ? 187.312 209.015 152.908 1.00 31.61  ? 645  PHE A CZ  1 
ATOM   14306 N N   . ALA B 2 646  ? 187.532 206.908 159.926 1.00 33.31  ? 646  ALA A N   1 
ATOM   14307 C CA  . ALA B 2 646  ? 187.048 206.228 161.118 1.00 33.31  ? 646  ALA A CA  1 
ATOM   14308 C C   . ALA B 2 646  ? 186.745 207.197 162.251 1.00 33.31  ? 646  ALA A C   1 
ATOM   14309 O O   . ALA B 2 646  ? 186.022 206.830 163.183 1.00 33.31  ? 646  ALA A O   1 
ATOM   14310 C CB  . ALA B 2 646  ? 188.063 205.183 161.576 1.00 33.31  ? 646  ALA A CB  1 
ATOM   14311 N N   . SER B 2 647  ? 187.279 208.415 162.199 1.00 32.69  ? 647  SER A N   1 
ATOM   14312 C CA  . SER B 2 647  ? 186.923 209.414 163.196 1.00 32.69  ? 647  SER A CA  1 
ATOM   14313 C C   . SER B 2 647  ? 185.621 210.136 162.874 1.00 32.69  ? 647  SER A C   1 
ATOM   14314 O O   . SER B 2 647  ? 184.899 210.530 163.796 1.00 32.69  ? 647  SER A O   1 
ATOM   14315 C CB  . SER B 2 647  ? 188.059 210.427 163.353 1.00 32.69  ? 647  SER A CB  1 
ATOM   14316 O OG  . SER B 2 647  ? 187.903 211.510 162.459 1.00 32.69  ? 647  SER A OG  1 
ATOM   14317 N N   . PHE B 2 648  ? 185.301 210.320 161.594 1.00 34.35  ? 648  PHE A N   1 
ATOM   14318 C CA  . PHE B 2 648  ? 184.066 210.995 161.187 1.00 34.35  ? 648  PHE A CA  1 
ATOM   14319 C C   . PHE B 2 648  ? 182.906 209.999 161.106 1.00 34.35  ? 648  PHE A C   1 
ATOM   14320 O O   . PHE B 2 648  ? 182.354 209.725 160.041 1.00 34.35  ? 648  PHE A O   1 
ATOM   14321 C CB  . PHE B 2 648  ? 184.259 211.709 159.854 1.00 34.35  ? 648  PHE A CB  1 
ATOM   14322 C CG  . PHE B 2 648  ? 185.025 213.000 159.944 1.00 34.35  ? 648  PHE A CG  1 
ATOM   14323 C CD1 . PHE B 2 648  ? 185.993 213.193 160.911 1.00 34.35  ? 648  PHE A CD1 1 
ATOM   14324 C CD2 . PHE B 2 648  ? 184.778 214.020 159.042 1.00 34.35  ? 648  PHE A CD2 1 
ATOM   14325 C CE1 . PHE B 2 648  ? 186.696 214.380 160.983 1.00 34.35  ? 648  PHE A CE1 1 
ATOM   14326 C CE2 . PHE B 2 648  ? 185.478 215.208 159.110 1.00 34.35  ? 648  PHE A CE2 1 
ATOM   14327 C CZ  . PHE B 2 648  ? 186.438 215.388 160.080 1.00 34.35  ? 648  PHE A CZ  1 
ATOM   14328 N N   . VAL B 2 649  ? 182.539 209.452 162.260 1.00 36.13  ? 649  VAL A N   1 
ATOM   14329 C CA  . VAL B 2 649  ? 181.406 208.539 162.374 1.00 36.13  ? 649  VAL A CA  1 
ATOM   14330 C C   . VAL B 2 649  ? 180.429 209.123 163.385 1.00 36.13  ? 649  VAL A C   1 
ATOM   14331 O O   . VAL B 2 649  ? 180.819 209.453 164.512 1.00 36.13  ? 649  VAL A O   1 
ATOM   14332 C CB  . VAL B 2 649  ? 181.846 207.123 162.780 1.00 36.13  ? 649  VAL A CB  1 
ATOM   14333 C CG1 . VAL B 2 649  ? 180.717 206.392 163.488 1.00 36.13  ? 649  VAL A CG1 1 
ATOM   14334 C CG2 . VAL B 2 649  ? 182.300 206.346 161.559 1.00 36.13  ? 649  VAL A CG2 1 
ATOM   14335 N N   . GLY B 2 650  ? 179.169 209.252 162.981 1.00 35.65  ? 650  GLY A N   1 
ATOM   14336 C CA  . GLY B 2 650  ? 178.145 209.811 163.832 1.00 35.65  ? 650  GLY A CA  1 
ATOM   14337 C C   . GLY B 2 650  ? 178.046 211.317 163.812 1.00 35.65  ? 650  GLY A C   1 
ATOM   14338 O O   . GLY B 2 650  ? 177.136 211.870 164.439 1.00 35.65  ? 650  GLY A O   1 
ATOM   14339 N N   . ILE B 2 651  ? 178.948 212.001 163.114 1.00 34.33  ? 651  ILE A N   1 
ATOM   14340 C CA  . ILE B 2 651  ? 178.909 213.451 163.005 1.00 34.33  ? 651  ILE A CA  1 
ATOM   14341 C C   . ILE B 2 651  ? 178.321 213.897 161.672 1.00 34.33  ? 651  ILE A C   1 
ATOM   14342 O O   . ILE B 2 651  ? 177.494 214.812 161.634 1.00 34.33  ? 651  ILE A O   1 
ATOM   14343 C CB  . ILE B 2 651  ? 180.318 214.047 163.225 1.00 34.33  ? 651  ILE A CB  1 
ATOM   14344 C CG1 . ILE B 2 651  ? 181.344 213.368 162.319 1.00 34.33  ? 651  ILE A CG1 1 
ATOM   14345 C CG2 . ILE B 2 651  ? 180.733 213.923 164.682 1.00 34.33  ? 651  ILE A CG2 1 
ATOM   14346 C CD1 . ILE B 2 651  ? 182.389 214.312 161.780 1.00 34.33  ? 651  ILE A CD1 1 
ATOM   14347 N N   . THR B 2 652  ? 178.728 213.261 160.579 1.00 33.01  ? 652  THR A N   1 
ATOM   14348 C CA  . THR B 2 652  ? 178.200 213.575 159.260 1.00 33.01  ? 652  THR A CA  1 
ATOM   14349 C C   . THR B 2 652  ? 178.528 212.426 158.319 1.00 33.01  ? 652  THR A C   1 
ATOM   14350 O O   . THR B 2 652  ? 179.364 211.570 158.618 1.00 33.01  ? 652  THR A O   1 
ATOM   14351 C CB  . THR B 2 652  ? 178.767 214.887 158.714 1.00 33.01  ? 652  THR A CB  1 
ATOM   14352 O OG1 . THR B 2 652  ? 178.393 215.036 157.340 1.00 33.01  ? 652  THR A OG1 1 
ATOM   14353 C CG2 . THR B 2 652  ? 180.279 214.892 158.825 1.00 33.01  ? 652  THR A CG2 1 
ATOM   14354 N N   . LYS B 2 653  ? 177.851 212.420 157.177 1.00 29.79  ? 653  LYS A N   1 
ATOM   14355 C CA  . LYS B 2 653  ? 178.066 211.415 156.146 1.00 29.79  ? 653  LYS A CA  1 
ATOM   14356 C C   . LYS B 2 653  ? 178.551 211.995 154.828 1.00 29.79  ? 653  LYS A C   1 
ATOM   14357 O O   . LYS B 2 653  ? 179.333 211.341 154.137 1.00 29.79  ? 653  LYS A O   1 
ATOM   14358 C CB  . LYS B 2 653  ? 176.772 210.621 155.903 1.00 29.79  ? 653  LYS A CB  1 
ATOM   14359 C CG  . LYS B 2 653  ? 176.835 209.633 154.746 1.00 29.79  ? 653  LYS A CG  1 
ATOM   14360 C CD  . LYS B 2 653  ? 175.725 208.594 154.835 1.00 29.79  ? 653  LYS A CD  1 
ATOM   14361 C CE  . LYS B 2 653  ? 174.353 209.244 154.886 1.00 29.79  ? 653  LYS A CE  1 
ATOM   14362 N NZ  . LYS B 2 653  ? 173.799 209.482 153.529 1.00 29.79  ? 653  LYS A NZ  1 
ATOM   14363 N N   . VAL B 2 654  ? 178.132 213.211 154.477 1.00 27.87  ? 654  VAL A N   1 
ATOM   14364 C CA  . VAL B 2 654  ? 178.495 213.764 153.177 1.00 27.87  ? 654  VAL A CA  1 
ATOM   14365 C C   . VAL B 2 654  ? 179.934 214.260 153.172 1.00 27.87  ? 654  VAL A C   1 
ATOM   14366 O O   . VAL B 2 654  ? 180.545 214.384 152.106 1.00 27.87  ? 654  VAL A O   1 
ATOM   14367 C CB  . VAL B 2 654  ? 177.516 214.888 152.787 1.00 27.87  ? 654  VAL A CB  1 
ATOM   14368 C CG1 . VAL B 2 654  ? 177.597 215.173 151.295 1.00 27.87  ? 654  VAL A CG1 1 
ATOM   14369 C CG2 . VAL B 2 654  ? 176.104 214.519 153.193 1.00 27.87  ? 654  VAL A CG2 1 
ATOM   14370 N N   . VAL B 2 655  ? 180.509 214.534 154.339 1.00 29.26  ? 655  VAL A N   1 
ATOM   14371 C CA  . VAL B 2 655  ? 181.864 215.081 154.399 1.00 29.26  ? 655  VAL A CA  1 
ATOM   14372 C C   . VAL B 2 655  ? 182.878 214.013 153.988 1.00 29.26  ? 655  VAL A C   1 
ATOM   14373 O O   . VAL B 2 655  ? 183.655 214.251 153.048 1.00 29.26  ? 655  VAL A O   1 
ATOM   14374 C CB  . VAL B 2 655  ? 182.175 215.662 155.790 1.00 29.26  ? 655  VAL A CB  1 
ATOM   14375 C CG1 . VAL B 2 655  ? 183.667 215.601 156.078 1.00 29.26  ? 655  VAL A CG1 1 
ATOM   14376 C CG2 . VAL B 2 655  ? 181.665 217.091 155.898 1.00 29.26  ? 655  VAL A CG2 1 
ATOM   14377 N N   . PRO B 2 656  ? 182.929 212.837 154.634 1.00 29.73  ? 656  PRO A N   1 
ATOM   14378 C CA  . PRO B 2 656  ? 183.921 211.843 154.198 1.00 29.73  ? 656  PRO A CA  1 
ATOM   14379 C C   . PRO B 2 656  ? 183.654 211.321 152.800 1.00 29.73  ? 656  PRO A C   1 
ATOM   14380 O O   . PRO B 2 656  ? 184.603 211.034 152.059 1.00 29.73  ? 656  PRO A O   1 
ATOM   14381 C CB  . PRO B 2 656  ? 183.802 210.735 155.257 1.00 29.73  ? 656  PRO A CB  1 
ATOM   14382 C CG  . PRO B 2 656  ? 183.031 211.337 156.376 1.00 29.73  ? 656  PRO A CG  1 
ATOM   14383 C CD  . PRO B 2 656  ? 182.095 212.289 155.717 1.00 29.73  ? 656  PRO A CD  1 
ATOM   14384 N N   . ILE B 2 657  ? 182.385 211.201 152.410 1.00 27.12  ? 657  ILE A N   1 
ATOM   14385 C CA  . ILE B 2 657  ? 182.064 210.710 151.073 1.00 27.12  ? 657  ILE A CA  1 
ATOM   14386 C C   . ILE B 2 657  ? 182.509 211.709 150.015 1.00 27.12  ? 657  ILE A C   1 
ATOM   14387 O O   . ILE B 2 657  ? 183.103 211.334 148.998 1.00 27.12  ? 657  ILE A O   1 
ATOM   14388 C CB  . ILE B 2 657  ? 180.560 210.397 150.969 1.00 27.12  ? 657  ILE A CB  1 
ATOM   14389 C CG1 . ILE B 2 657  ? 180.223 209.196 151.845 1.00 27.12  ? 657  ILE A CG1 1 
ATOM   14390 C CG2 . ILE B 2 657  ? 180.165 210.136 149.529 1.00 27.12  ? 657  ILE A CG2 1 
ATOM   14391 C CD1 . ILE B 2 657  ? 181.281 208.116 151.825 1.00 27.12  ? 657  ILE A CD1 1 
ATOM   14392 N N   . LEU B 2 658  ? 182.234 212.993 150.240 1.00 29.25  ? 658  LEU A N   1 
ATOM   14393 C CA  . LEU B 2 658  ? 182.687 214.023 149.312 1.00 29.25  ? 658  LEU A CA  1 
ATOM   14394 C C   . LEU B 2 658  ? 184.205 214.061 149.242 1.00 29.25  ? 658  LEU A C   1 
ATOM   14395 O O   . LEU B 2 658  ? 184.778 214.216 148.157 1.00 29.25  ? 658  LEU A O   1 
ATOM   14396 C CB  . LEU B 2 658  ? 182.141 215.385 149.737 1.00 29.25  ? 658  LEU A CB  1 
ATOM   14397 C CG  . LEU B 2 658  ? 182.251 216.512 148.709 1.00 29.25  ? 658  LEU A CG  1 
ATOM   14398 C CD1 . LEU B 2 658  ? 181.742 216.061 147.353 1.00 29.25  ? 658  LEU A CD1 1 
ATOM   14399 C CD2 . LEU B 2 658  ? 181.503 217.748 149.183 1.00 29.25  ? 658  LEU A CD2 1 
ATOM   14400 N N   . LEU B 2 659  ? 184.876 213.922 150.387 1.00 30.22  ? 659  LEU A N   1 
ATOM   14401 C CA  . LEU B 2 659  ? 186.336 213.932 150.391 1.00 30.22  ? 659  LEU A CA  1 
ATOM   14402 C C   . LEU B 2 659  ? 186.903 212.746 149.615 1.00 30.22  ? 659  LEU A C   1 
ATOM   14403 O O   . LEU B 2 659  ? 187.850 212.899 148.831 1.00 30.22  ? 659  LEU A O   1 
ATOM   14404 C CB  . LEU B 2 659  ? 186.836 213.956 151.835 1.00 30.22  ? 659  LEU A CB  1 
ATOM   14405 C CG  . LEU B 2 659  ? 188.298 213.681 152.167 1.00 30.22  ? 659  LEU A CG  1 
ATOM   14406 C CD1 . LEU B 2 659  ? 188.696 214.478 153.392 1.00 30.22  ? 659  LEU A CD1 1 
ATOM   14407 C CD2 . LEU B 2 659  ? 188.496 212.209 152.434 1.00 30.22  ? 659  LEU A CD2 1 
ATOM   14408 N N   . ALA B 2 660  ? 186.329 211.555 149.810 1.00 31.22  ? 660  ALA A N   1 
ATOM   14409 C CA  . ALA B 2 660  ? 186.796 210.377 149.087 1.00 31.22  ? 660  ALA A CA  1 
ATOM   14410 C C   . ALA B 2 660  ? 186.542 210.508 147.592 1.00 31.22  ? 660  ALA A C   1 
ATOM   14411 O O   . ALA B 2 660  ? 187.397 210.143 146.775 1.00 31.22  ? 660  ALA A O   1 
ATOM   14412 C CB  . ALA B 2 660  ? 186.118 209.122 149.634 1.00 31.22  ? 660  ALA A CB  1 
ATOM   14413 N N   . ALA B 2 661  ? 185.368 211.018 147.212 1.00 30.45  ? 661  ALA A N   1 
ATOM   14414 C CA  . ALA B 2 661  ? 185.074 211.204 145.796 1.00 30.45  ? 661  ALA A CA  1 
ATOM   14415 C C   . ALA B 2 661  ? 186.012 212.224 145.172 1.00 30.45  ? 661  ALA A C   1 
ATOM   14416 O O   . ALA B 2 661  ? 186.456 212.051 144.032 1.00 30.45  ? 661  ALA A O   1 
ATOM   14417 C CB  . ALA B 2 661  ? 183.619 211.626 145.610 1.00 30.45  ? 661  ALA A CB  1 
ATOM   14418 N N   . ALA B 2 662  ? 186.332 213.291 145.904 1.00 32.48  ? 662  ALA A N   1 
ATOM   14419 C CA  . ALA B 2 662  ? 187.285 214.272 145.400 1.00 32.48  ? 662  ALA A CA  1 
ATOM   14420 C C   . ALA B 2 662  ? 188.663 213.657 145.210 1.00 32.48  ? 662  ALA A C   1 
ATOM   14421 O O   . ALA B 2 662  ? 189.327 213.904 144.195 1.00 32.48  ? 662  ALA A O   1 
ATOM   14422 C CB  . ALA B 2 662  ? 187.357 215.470 146.346 1.00 32.48  ? 662  ALA A CB  1 
ATOM   14423 N N   . SER B 2 663  ? 189.114 212.853 146.177 1.00 32.64  ? 663  SER A N   1 
ATOM   14424 C CA  . SER B 2 663  ? 190.417 212.207 146.044 1.00 32.64  ? 663  SER A CA  1 
ATOM   14425 C C   . SER B 2 663  ? 190.450 211.277 144.838 1.00 32.64  ? 663  SER A C   1 
ATOM   14426 O O   . SER B 2 663  ? 191.412 211.294 144.058 1.00 32.64  ? 663  SER A O   1 
ATOM   14427 C CB  . SER B 2 663  ? 190.758 211.437 147.318 1.00 32.64  ? 663  SER A CB  1 
ATOM   14428 O OG  . SER B 2 663  ? 191.665 210.387 147.040 1.00 32.64  ? 663  SER A OG  1 
ATOM   14429 N N   . LEU B 2 664  ? 189.403 210.468 144.663 1.00 32.57  ? 664  LEU A N   1 
ATOM   14430 C CA  . LEU B 2 664  ? 189.355 209.562 143.520 1.00 32.57  ? 664  LEU A CA  1 
ATOM   14431 C C   . LEU B 2 664  ? 189.323 210.323 142.202 1.00 32.57  ? 664  LEU A C   1 
ATOM   14432 O O   . LEU B 2 664  ? 190.013 209.947 141.249 1.00 32.57  ? 664  LEU A O   1 
ATOM   14433 C CB  . LEU B 2 664  ? 188.147 208.635 143.629 1.00 32.57  ? 664  LEU A CB  1 
ATOM   14434 C CG  . LEU B 2 664  ? 188.282 207.505 144.642 1.00 32.57  ? 664  LEU A CG  1 
ATOM   14435 C CD1 . LEU B 2 664  ? 187.246 206.435 144.381 1.00 32.57  ? 664  LEU A CD1 1 
ATOM   14436 C CD2 . LEU B 2 664  ? 189.670 206.922 144.540 1.00 32.57  ? 664  LEU A CD2 1 
ATOM   14437 N N   . VAL B 2 665  ? 188.528 211.394 142.123 1.00 36.82  ? 665  VAL A N   1 
ATOM   14438 C CA  . VAL B 2 665  ? 188.435 212.151 140.879 1.00 36.82  ? 665  VAL A CA  1 
ATOM   14439 C C   . VAL B 2 665  ? 189.773 212.801 140.548 1.00 36.82  ? 665  VAL A C   1 
ATOM   14440 O O   . VAL B 2 665  ? 190.227 212.769 139.399 1.00 36.82  ? 665  VAL A O   1 
ATOM   14441 C CB  . VAL B 2 665  ? 187.304 213.190 140.965 1.00 36.82  ? 665  VAL A CB  1 
ATOM   14442 C CG1 . VAL B 2 665  ? 187.454 214.235 139.880 1.00 36.82  ? 665  VAL A CG1 1 
ATOM   14443 C CG2 . VAL B 2 665  ? 185.957 212.507 140.853 1.00 36.82  ? 665  VAL A CG2 1 
ATOM   14444 N N   . GLY B 2 666  ? 190.429 213.393 141.550 1.00 40.43  ? 666  GLY A N   1 
ATOM   14445 C CA  . GLY B 2 666  ? 191.734 213.986 141.310 1.00 40.43  ? 666  GLY A CA  1 
ATOM   14446 C C   . GLY B 2 666  ? 192.761 212.968 140.852 1.00 40.43  ? 666  GLY A C   1 
ATOM   14447 O O   . GLY B 2 666  ? 193.497 213.202 139.886 1.00 40.43  ? 666  GLY A O   1 
ATOM   14448 N N   . GLY B 2 667  ? 192.815 211.817 141.524 1.00 39.75  ? 667  GLY A N   1 
ATOM   14449 C CA  . GLY B 2 667  ? 193.742 210.779 141.111 1.00 39.75  ? 667  GLY A CA  1 
ATOM   14450 C C   . GLY B 2 667  ? 193.473 210.283 139.704 1.00 39.75  ? 667  GLY A C   1 
ATOM   14451 O O   . GLY B 2 667  ? 194.397 210.155 138.894 1.00 39.75  ? 667  GLY A O   1 
ATOM   14452 N N   . GLY B 2 668  ? 192.207 210.010 139.389 1.00 41.26  ? 668  GLY A N   1 
ATOM   14453 C CA  . GLY B 2 668  ? 191.851 209.513 138.074 1.00 41.26  ? 668  GLY A CA  1 
ATOM   14454 C C   . GLY B 2 668  ? 191.896 210.549 136.977 1.00 41.26  ? 668  GLY A C   1 
ATOM   14455 O O   . GLY B 2 668  ? 191.796 210.181 135.802 1.00 41.26  ? 668  GLY A O   1 
ATOM   14456 N N   . LEU B 2 669  ? 192.023 211.827 137.326 1.00 44.01  ? 669  LEU A N   1 
ATOM   14457 C CA  . LEU B 2 669  ? 192.286 212.848 136.324 1.00 44.01  ? 669  LEU A CA  1 
ATOM   14458 C C   . LEU B 2 669  ? 193.773 213.088 136.128 1.00 44.01  ? 669  LEU A C   1 
ATOM   14459 O O   . LEU B 2 669  ? 194.197 213.449 135.026 1.00 44.01  ? 669  LEU A O   1 
ATOM   14460 C CB  . LEU B 2 669  ? 191.602 214.161 136.711 1.00 44.01  ? 669  LEU A CB  1 
ATOM   14461 C CG  . LEU B 2 669  ? 190.154 214.336 136.251 1.00 44.01  ? 669  LEU A CG  1 
ATOM   14462 C CD1 . LEU B 2 669  ? 189.767 215.806 136.249 1.00 44.01  ? 669  LEU A CD1 1 
ATOM   14463 C CD2 . LEU B 2 669  ? 189.937 213.717 134.879 1.00 44.01  ? 669  LEU A CD2 1 
ATOM   14464 N N   . ILE B 2 670  ? 194.577 212.890 137.175 1.00 42.29  ? 670  ILE A N   1 
ATOM   14465 C CA  . ILE B 2 670  ? 196.017 213.076 137.040 1.00 42.29  ? 670  ILE A CA  1 
ATOM   14466 C C   . ILE B 2 670  ? 196.678 211.851 136.412 1.00 42.29  ? 670  ILE A C   1 
ATOM   14467 O O   . ILE B 2 670  ? 197.650 211.985 135.661 1.00 42.29  ? 670  ILE A O   1 
ATOM   14468 C CB  . ILE B 2 670  ? 196.624 213.425 138.410 1.00 42.29  ? 670  ILE A CB  1 
ATOM   14469 C CG1 . ILE B 2 670  ? 196.596 214.939 138.632 1.00 42.29  ? 670  ILE A CG1 1 
ATOM   14470 C CG2 . ILE B 2 670  ? 198.041 212.901 138.543 1.00 42.29  ? 670  ILE A CG2 1 
ATOM   14471 C CD1 . ILE B 2 670  ? 197.086 215.360 139.997 1.00 42.29  ? 670  ILE A CD1 1 
ATOM   14472 N N   . ALA B 2 671  ? 196.149 210.651 136.669 1.00 42.55  ? 671  ALA A N   1 
ATOM   14473 C CA  . ALA B 2 671  ? 196.793 209.427 136.199 1.00 42.55  ? 671  ALA A CA  1 
ATOM   14474 C C   . ALA B 2 671  ? 196.851 209.334 134.679 1.00 42.55  ? 671  ALA A C   1 
ATOM   14475 O O   . ALA B 2 671  ? 197.626 208.531 134.153 1.00 42.55  ? 671  ALA A O   1 
ATOM   14476 C CB  . ALA B 2 671  ? 196.074 208.202 136.763 1.00 42.55  ? 671  ALA A CB  1 
ATOM   14477 N N   . LEU B 2 672  ? 196.047 210.122 133.964 1.00 44.99  ? 672  LEU A N   1 
ATOM   14478 C CA  . LEU B 2 672  ? 196.167 210.160 132.510 1.00 44.99  ? 672  LEU A CA  1 
ATOM   14479 C C   . LEU B 2 672  ? 197.493 210.774 132.080 1.00 44.99  ? 672  LEU A C   1 
ATOM   14480 O O   . LEU B 2 672  ? 198.094 210.337 131.092 1.00 44.99  ? 672  LEU A O   1 
ATOM   14481 C CB  . LEU B 2 672  ? 194.996 210.923 131.888 1.00 44.99  ? 672  LEU A CB  1 
ATOM   14482 C CG  . LEU B 2 672  ? 193.634 210.236 131.724 1.00 44.99  ? 672  LEU A CG  1 
ATOM   14483 C CD1 . LEU B 2 672  ? 193.737 209.112 130.701 1.00 44.99  ? 672  LEU A CD1 1 
ATOM   14484 C CD2 . LEU B 2 672  ? 193.059 209.712 133.023 1.00 44.99  ? 672  LEU A CD2 1 
ATOM   14485 N N   . ARG B 2 673  ? 197.968 211.781 132.813 1.00 45.95  ? 673  ARG A N   1 
ATOM   14486 C CA  . ARG B 2 673  ? 199.219 212.461 132.476 1.00 45.95  ? 673  ARG A CA  1 
ATOM   14487 C C   . ARG B 2 673  ? 200.420 211.619 132.915 1.00 45.95  ? 673  ARG A C   1 
ATOM   14488 O O   . ARG B 2 673  ? 201.217 211.999 133.772 1.00 45.95  ? 673  ARG A O   1 
ATOM   14489 C CB  . ARG B 2 673  ? 199.253 213.845 133.107 1.00 45.95  ? 673  ARG A CB  1 
ATOM   14490 C CG  . ARG B 2 673  ? 198.150 214.768 132.625 1.00 45.95  ? 673  ARG A CG  1 
ATOM   14491 C CD  . ARG B 2 673  ? 198.474 216.223 132.917 1.00 45.95  ? 673  ARG A CD  1 
ATOM   14492 N NE  . ARG B 2 673  ? 199.299 216.380 134.108 1.00 45.95  ? 673  ARG A NE  1 
ATOM   14493 C CZ  . ARG B 2 673  ? 200.393 217.131 134.165 1.00 45.95  ? 673  ARG A CZ  1 
ATOM   14494 N NH1 . ARG B 2 673  ? 200.825 217.805 133.114 1.00 45.95  ? 673  ARG A NH1 1 
ATOM   14495 N NH2 . ARG B 2 673  ? 201.068 217.206 135.311 1.00 45.95  ? 673  ARG A NH2 1 
ATOM   14496 N N   . LEU B 2 674  ? 200.537 210.445 132.299 1.00 46.21  ? 674  LEU A N   1 
ATOM   14497 C CA  . LEU B 2 674  ? 201.615 209.505 132.547 1.00 46.21  ? 674  LEU A CA  1 
ATOM   14498 C C   . LEU B 2 674  ? 202.171 209.011 131.222 1.00 46.21  ? 674  LEU A C   1 
ATOM   14499 O O   . LEU B 2 674  ? 201.433 208.909 130.236 1.00 46.21  ? 674  LEU A O   1 
ATOM   14500 C CB  . LEU B 2 674  ? 201.122 208.309 133.380 1.00 46.21  ? 674  LEU A CB  1 
ATOM   14501 C CG  . LEU B 2 674  ? 202.056 207.688 134.425 1.00 46.21  ? 674  LEU A CG  1 
ATOM   14502 C CD1 . LEU B 2 674  ? 202.783 208.753 135.228 1.00 46.21  ? 674  LEU A CD1 1 
ATOM   14503 C CD2 . LEU B 2 674  ? 201.277 206.762 135.347 1.00 46.21  ? 674  LEU A CD2 1 
ATOM   14504 N N   . PRO B 2 675  ? 203.471 208.721 131.157 1.00 48.36  ? 675  PRO A N   1 
ATOM   14505 C CA  . PRO B 2 675  ? 204.038 208.172 129.920 1.00 48.36  ? 675  PRO A CA  1 
ATOM   14506 C C   . PRO B 2 675  ? 203.439 206.814 129.581 1.00 48.36  ? 675  PRO A C   1 
ATOM   14507 O O   . PRO B 2 675  ? 203.123 206.009 130.461 1.00 48.36  ? 675  PRO A O   1 
ATOM   14508 C CB  . PRO B 2 675  ? 205.536 208.061 130.230 1.00 48.36  ? 675  PRO A CB  1 
ATOM   14509 C CG  . PRO B 2 675  ? 205.640 208.161 131.719 1.00 48.36  ? 675  PRO A CG  1 
ATOM   14510 C CD  . PRO B 2 675  ? 204.513 209.035 132.146 1.00 48.36  ? 675  PRO A CD  1 
ATOM   14511 N N   . GLU B 2 676  ? 203.290 206.566 128.282 1.00 52.62  ? 676  GLU A N   1 
ATOM   14512 C CA  . GLU B 2 676  ? 202.699 205.328 127.798 1.00 52.62  ? 676  GLU A CA  1 
ATOM   14513 C C   . GLU B 2 676  ? 203.696 204.180 127.885 1.00 52.62  ? 676  GLU A C   1 
ATOM   14514 O O   . GLU B 2 676  ? 204.896 204.359 127.659 1.00 52.62  ? 676  GLU A O   1 
ATOM   14515 C CB  . GLU B 2 676  ? 202.219 205.498 126.355 1.00 52.62  ? 676  GLU A CB  1 
ATOM   14516 C CG  . GLU B 2 676  ? 203.314 205.882 125.363 1.00 52.62  ? 676  GLU A CG  1 
ATOM   14517 C CD  . GLU B 2 676  ? 203.582 207.376 125.317 1.00 52.62  ? 676  GLU A CD  1 
ATOM   14518 O OE1 . GLU B 2 676  ? 203.431 208.047 126.360 1.00 52.62  ? 676  GLU A OE1 1 
ATOM   14519 O OE2 . GLU B 2 676  ? 203.947 207.881 124.236 1.00 52.62  ? 676  GLU A OE2 1 
ATOM   14520 N N   . THR B 2 677  ? 203.190 202.993 128.225 1.00 47.94  ? 677  THR A N   1 
ATOM   14521 C CA  . THR B 2 677  ? 203.993 201.771 128.322 1.00 47.94  ? 677  THR A CA  1 
ATOM   14522 C C   . THR B 2 677  ? 203.204 200.638 127.668 1.00 47.94  ? 677  THR A C   1 
ATOM   14523 O O   . THR B 2 677  ? 202.338 200.034 128.303 1.00 47.94  ? 677  THR A O   1 
ATOM   14524 C CB  . THR B 2 677  ? 204.337 201.436 129.773 1.00 47.94  ? 677  THR A CB  1 
ATOM   14525 O OG1 . THR B 2 677  ? 203.134 201.127 130.490 1.00 47.94  ? 677  THR A OG1 1 
ATOM   14526 C CG2 . THR B 2 677  ? 205.054 202.594 130.451 1.00 47.94  ? 677  THR A CG2 1 
ATOM   14527 N N   . ARG B 2 678  ? 203.510 200.353 126.407 1.00 46.98  ? 678  ARG A N   1 
ATOM   14528 C CA  . ARG B 2 678  ? 202.860 199.264 125.686 1.00 46.98  ? 678  ARG A CA  1 
ATOM   14529 C C   . ARG B 2 678  ? 203.677 198.854 124.467 1.00 46.98  ? 678  ARG A C   1 
ATOM   14530 O O   . ARG B 2 678  ? 204.245 199.700 123.775 1.00 46.98  ? 678  ARG A O   1 
ATOM   14531 C CB  . ARG B 2 678  ? 201.447 199.662 125.260 1.00 46.98  ? 678  ARG A CB  1 
ATOM   14532 C CG  . ARG B 2 678  ? 200.348 198.914 125.996 1.00 46.98  ? 678  ARG A CG  1 
ATOM   14533 C CD  . ARG B 2 678  ? 199.012 199.624 125.875 1.00 46.98  ? 678  ARG A CD  1 
ATOM   14534 N NE  . ARG B 2 678  ? 198.528 199.659 124.500 1.00 46.98  ? 678  ARG A NE  1 
ATOM   14535 C CZ  . ARG B 2 678  ? 197.368 199.157 124.100 1.00 46.98  ? 678  ARG A CZ  1 
ATOM   14536 N NH1 . ARG B 2 678  ? 196.544 198.562 124.946 1.00 46.98  ? 678  ARG A NH1 1 
ATOM   14537 N NH2 . ARG B 2 678  ? 197.027 199.253 122.818 1.00 46.98  ? 678  ARG A NH2 1 
HETATM 14538 C C1  . NAG C 3 .    ? 169.457 213.783 194.312 1.00 50.52  ? 1    NAG C C1  1 
HETATM 14539 C C2  . NAG C 3 .    ? 169.588 215.213 193.792 1.00 50.52  ? 1    NAG C C2  1 
HETATM 14540 C C3  . NAG C 3 .    ? 169.288 216.183 194.926 1.00 50.52  ? 1    NAG C C3  1 
HETATM 14541 C C4  . NAG C 3 .    ? 167.906 215.899 195.489 1.00 50.52  ? 1    NAG C C4  1 
HETATM 14542 C C5  . NAG C 3 .    ? 167.841 214.447 195.952 1.00 50.52  ? 1    NAG C C5  1 
HETATM 14543 C C6  . NAG C 3 .    ? 166.472 214.047 196.446 1.00 50.52  ? 1    NAG C C6  1 
HETATM 14544 C C7  . NAG C 3 .    ? 171.127 215.623 191.949 1.00 50.52  ? 1    NAG C C7  1 
HETATM 14545 C C8  . NAG C 3 .    ? 172.229 216.559 191.558 1.00 50.52  ? 1    NAG C C8  1 
HETATM 14546 N N2  . NAG C 3 .    ? 170.901 215.501 193.256 1.00 50.52  ? 1    NAG C N2  1 
HETATM 14547 O O3  . NAG C 3 .    ? 169.386 217.519 194.452 1.00 50.52  ? 1    NAG C O3  1 
HETATM 14548 O O4  . NAG C 3 .    ? 167.677 216.762 196.597 1.00 50.52  ? 1    NAG C O4  1 
HETATM 14549 O O5  . NAG C 3 .    ? 168.162 213.574 194.850 1.00 50.52  ? 1    NAG C O5  1 
HETATM 14550 O O6  . NAG C 3 .    ? 165.713 213.401 195.433 1.00 50.52  ? 1    NAG C O6  1 
HETATM 14551 O O7  . NAG C 3 .    ? 170.472 215.003 191.118 1.00 50.52  ? 1    NAG C O7  1 
HETATM 14552 C C1  . FUC C 3 .    ? 164.965 212.320 195.919 1.00 46.20  ? 2    FUC C C1  1 
HETATM 14553 C C2  . FUC C 3 .    ? 165.543 211.068 195.315 1.00 46.20  ? 2    FUC C C2  1 
HETATM 14554 C C3  . FUC C 3 .    ? 164.684 209.881 195.667 1.00 46.20  ? 2    FUC C C3  1 
HETATM 14555 C C4  . FUC C 3 .    ? 163.265 210.118 195.204 1.00 46.20  ? 2    FUC C C4  1 
HETATM 14556 C C5  . FUC C 3 .    ? 162.739 211.404 195.819 1.00 46.20  ? 2    FUC C C5  1 
HETATM 14557 C C6  . FUC C 3 .    ? 161.368 211.772 195.306 1.00 46.20  ? 2    FUC C C6  1 
HETATM 14558 O O2  . FUC C 3 .    ? 166.880 210.876 195.768 1.00 46.20  ? 2    FUC C O2  1 
HETATM 14559 O O3  . FUC C 3 .    ? 165.211 208.724 195.030 1.00 46.20  ? 2    FUC C O3  1 
HETATM 14560 O O4  . FUC C 3 .    ? 163.231 210.243 193.791 1.00 46.20  ? 2    FUC C O4  1 
HETATM 14561 O O5  . FUC C 3 .    ? 163.619 212.497 195.476 1.00 46.20  ? 2    FUC C O5  1 
HETATM 14562 C C1  . NAG D 4 .    ? 169.276 202.147 210.577 1.00 42.11  ? 1    NAG D C1  1 
HETATM 14563 C C2  . NAG D 4 .    ? 167.865 202.867 210.449 1.00 42.11  ? 1    NAG D C2  1 
HETATM 14564 C C3  . NAG D 4 .    ? 167.456 203.459 211.793 1.00 42.11  ? 1    NAG D C3  1 
HETATM 14565 C C4  . NAG D 4 .    ? 167.565 202.384 212.862 1.00 42.11  ? 1    NAG D C4  1 
HETATM 14566 C C5  . NAG D 4 .    ? 168.916 201.658 212.818 1.00 42.11  ? 1    NAG D C5  1 
HETATM 14567 C C6  . NAG D 4 .    ? 168.984 200.485 213.765 1.00 42.11  ? 1    NAG D C6  1 
HETATM 14568 C C7  . NAG D 4 .    ? 168.565 205.002 209.406 1.00 42.11  ? 1    NAG D C7  1 
HETATM 14569 C C8  . NAG D 4 .    ? 168.317 206.005 208.299 1.00 42.11  ? 1    NAG D C8  1 
HETATM 14570 N N2  . NAG D 4 .    ? 167.808 203.893 209.407 1.00 42.11  ? 1    NAG D N2  1 
HETATM 14571 O O3  . NAG D 4 .    ? 166.145 204.036 211.793 1.00 42.11  ? 1    NAG D O3  1 
HETATM 14572 O O4  . NAG D 4 .    ? 167.460 203.032 214.120 1.00 42.11  ? 1    NAG D O4  1 
HETATM 14573 O O5  . NAG D 4 .    ? 169.192 201.146 211.512 1.00 42.11  ? 1    NAG D O5  1 
HETATM 14574 O O6  . NAG D 4 .    ? 169.018 199.249 213.069 1.00 42.11  ? 1    NAG D O6  1 
HETATM 14575 O O7  . NAG D 4 .    ? 169.459 205.153 210.202 1.00 42.11  ? 1    NAG D O7  1 
HETATM 14576 C C1  . NAG D 4 .    ? 166.386 202.399 214.873 1.00 78.23  ? 2    NAG D C1  1 
HETATM 14577 C C2  . NAG D 4 .    ? 166.578 202.580 216.375 1.00 78.23  ? 2    NAG D C2  1 
HETATM 14578 C C3  . NAG D 4 .    ? 165.481 201.830 217.122 1.00 78.23  ? 2    NAG D C3  1 
HETATM 14579 C C4  . NAG D 4 .    ? 164.096 202.172 216.572 1.00 78.23  ? 2    NAG D C4  1 
HETATM 14580 C C5  . NAG D 4 .    ? 164.052 202.197 215.040 1.00 78.23  ? 2    NAG D C5  1 
HETATM 14581 C C6  . NAG D 4 .    ? 162.782 202.806 214.494 1.00 78.23  ? 2    NAG D C6  1 
HETATM 14582 C C7  . NAG D 4 .    ? 168.903 202.950 217.089 1.00 78.23  ? 2    NAG D C7  1 
HETATM 14583 C C8  . NAG D 4 .    ? 168.626 204.415 216.932 1.00 78.23  ? 2    NAG D C8  1 
HETATM 14584 N N2  . NAG D 4 .    ? 167.889 202.124 216.806 1.00 78.23  ? 2    NAG D N2  1 
HETATM 14585 O O3  . NAG D 4 .    ? 165.570 202.154 218.506 1.00 78.23  ? 2    NAG D O3  1 
HETATM 14586 O O4  . NAG D 4 .    ? 163.186 201.144 216.943 1.00 78.23  ? 2    NAG D O4  1 
HETATM 14587 O O5  . NAG D 4 .    ? 165.141 202.951 214.492 1.00 78.23  ? 2    NAG D O5  1 
HETATM 14588 O O6  . NAG D 4 .    ? 162.599 204.133 214.967 1.00 78.23  ? 2    NAG D O6  1 
HETATM 14589 O O7  . NAG D 4 .    ? 169.996 202.531 217.452 1.00 78.23  ? 2    NAG D O7  1 
HETATM 14590 C C1  . BMA D 4 .    ? 162.497 201.080 218.165 1.00 96.23  ? 3    BMA D C1  1 
HETATM 14591 C C2  . BMA D 4 .    ? 161.162 201.764 218.369 1.00 96.23  ? 3    BMA D C2  1 
HETATM 14592 C C3  . BMA D 4 .    ? 161.253 202.952 219.323 1.00 96.23  ? 3    BMA D C3  1 
HETATM 14593 C C4  . BMA D 4 .    ? 161.941 202.532 220.605 1.00 96.23  ? 3    BMA D C4  1 
HETATM 14594 C C5  . BMA D 4 .    ? 163.268 201.829 220.337 1.00 96.23  ? 3    BMA D C5  1 
HETATM 14595 C C6  . BMA D 4 .    ? 163.916 201.283 221.591 1.00 96.23  ? 3    BMA D C6  1 
HETATM 14596 O O2  . BMA D 4 .    ? 160.212 200.809 218.833 1.00 96.23  ? 3    BMA D O2  1 
HETATM 14597 O O3  . BMA D 4 .    ? 159.968 203.478 219.701 1.00 96.23  ? 3    BMA D O3  1 
HETATM 14598 O O4  . BMA D 4 .    ? 162.183 203.675 221.418 1.00 96.23  ? 3    BMA D O4  1 
HETATM 14599 O O5  . BMA D 4 .    ? 163.123 200.725 219.404 1.00 96.23  ? 3    BMA D O5  1 
HETATM 14600 O O6  . BMA D 4 .    ? 162.967 200.912 222.588 1.00 96.23  ? 3    BMA D O6  1 
HETATM 14601 C C1  . MAN D 4 .    ? 159.541 204.651 219.070 1.00 108.73 ? 4    MAN D C1  1 
HETATM 14602 C C2  . MAN D 4 .    ? 158.326 205.199 219.787 1.00 108.73 ? 4    MAN D C2  1 
HETATM 14603 C C3  . MAN D 4 .    ? 157.128 204.308 219.553 1.00 108.73 ? 4    MAN D C3  1 
HETATM 14604 C C4  . MAN D 4 .    ? 156.889 204.146 218.064 1.00 108.73 ? 4    MAN D C4  1 
HETATM 14605 C C5  . MAN D 4 .    ? 158.149 203.618 217.388 1.00 108.73 ? 4    MAN D C5  1 
HETATM 14606 C C6  . MAN D 4 .    ? 158.030 203.535 215.886 1.00 108.73 ? 4    MAN D C6  1 
HETATM 14607 O O2  . MAN D 4 .    ? 158.070 206.533 219.360 1.00 108.73 ? 4    MAN D O2  1 
HETATM 14608 O O3  . MAN D 4 .    ? 155.981 204.884 220.174 1.00 108.73 ? 4    MAN D O3  1 
HETATM 14609 O O4  . MAN D 4 .    ? 155.824 203.230 217.836 1.00 108.73 ? 4    MAN D O4  1 
HETATM 14610 O O5  . MAN D 4 .    ? 159.258 204.492 217.671 1.00 108.73 ? 4    MAN D O5  1 
HETATM 14611 O O6  . MAN D 4 .    ? 157.115 202.513 215.510 1.00 108.73 ? 4    MAN D O6  1 
HETATM 14612 C C1  . MAN D 4 .    ? 162.471 199.611 222.438 1.00 126.50 ? 5    MAN D C1  1 
HETATM 14613 C C2  . MAN D 4 .    ? 161.605 199.302 223.636 1.00 126.50 ? 5    MAN D C2  1 
HETATM 14614 C C3  . MAN D 4 .    ? 161.175 197.848 223.653 1.00 126.50 ? 5    MAN D C3  1 
HETATM 14615 C C4  . MAN D 4 .    ? 162.380 196.928 223.479 1.00 126.50 ? 5    MAN D C4  1 
HETATM 14616 C C5  . MAN D 4 .    ? 163.246 197.316 222.266 1.00 126.50 ? 5    MAN D C5  1 
HETATM 14617 C C6  . MAN D 4 .    ? 162.599 197.057 220.922 1.00 126.50 ? 5    MAN D C6  1 
HETATM 14618 O O2  . MAN D 4 .    ? 160.475 200.170 223.652 1.00 126.50 ? 5    MAN D O2  1 
HETATM 14619 O O3  . MAN D 4 .    ? 160.181 197.618 222.654 1.00 126.50 ? 5    MAN D O3  1 
HETATM 14620 O O4  . MAN D 4 .    ? 163.187 196.968 224.652 1.00 126.50 ? 5    MAN D O4  1 
HETATM 14621 O O5  . MAN D 4 .    ? 163.578 198.719 222.305 1.00 126.50 ? 5    MAN D O5  1 
HETATM 14622 O O6  . MAN D 4 .    ? 163.345 197.662 219.868 1.00 126.50 ? 5    MAN D O6  1 
HETATM 14623 C C1  . FUC D 4 .    ? 167.724 198.641 213.169 1.00 100.40 ? 6    FUC D C1  1 
HETATM 14624 C C2  . FUC D 4 .    ? 167.324 198.248 211.747 1.00 100.40 ? 6    FUC D C2  1 
HETATM 14625 C C3  . FUC D 4 .    ? 166.631 196.877 211.712 1.00 100.40 ? 6    FUC D C3  1 
HETATM 14626 C C4  . FUC D 4 .    ? 165.698 196.732 212.898 1.00 100.40 ? 6    FUC D C4  1 
HETATM 14627 C C5  . FUC D 4 .    ? 166.531 196.790 214.179 1.00 100.40 ? 6    FUC D C5  1 
HETATM 14628 C C6  . FUC D 4 .    ? 165.806 197.465 215.331 1.00 100.40 ? 6    FUC D C6  1 
HETATM 14629 O O2  . FUC D 4 .    ? 168.439 198.260 210.872 1.00 100.40 ? 6    FUC D O2  1 
HETATM 14630 O O3  . FUC D 4 .    ? 165.851 196.749 210.527 1.00 100.40 ? 6    FUC D O3  1 
HETATM 14631 O O4  . FUC D 4 .    ? 164.731 197.779 212.887 1.00 100.40 ? 6    FUC D O4  1 
HETATM 14632 O O5  . FUC D 4 .    ? 167.780 197.511 213.994 1.00 100.40 ? 6    FUC D O5  1 
HETATM 14633 C C1  . NAG E 5 .    ? 159.970 183.729 186.727 1.00 63.32  ? 701  NAG A C1  1 
HETATM 14634 C C2  . NAG E 5 .    ? 161.060 182.702 186.422 1.00 63.32  ? 701  NAG A C2  1 
HETATM 14635 C C3  . NAG E 5 .    ? 160.521 181.296 186.665 1.00 63.32  ? 701  NAG A C3  1 
HETATM 14636 C C4  . NAG E 5 .    ? 159.917 181.184 188.061 1.00 63.32  ? 701  NAG A C4  1 
HETATM 14637 C C5  . NAG E 5 .    ? 158.930 182.320 188.330 1.00 63.32  ? 701  NAG A C5  1 
HETATM 14638 C C6  . NAG E 5 .    ? 158.432 182.347 189.756 1.00 63.32  ? 701  NAG A C6  1 
HETATM 14639 C C7  . NAG E 5 .    ? 162.734 182.369 184.660 1.00 63.32  ? 701  NAG A C7  1 
HETATM 14640 C C8  . NAG E 5 .    ? 163.080 182.600 183.220 1.00 63.32  ? 701  NAG A C8  1 
HETATM 14641 N N2  . NAG E 5 .    ? 161.548 182.839 185.059 1.00 63.32  ? 701  NAG A N2  1 
HETATM 14642 O O3  . NAG E 5 .    ? 161.567 180.344 186.514 1.00 63.32  ? 701  NAG A O3  1 
HETATM 14643 O O4  . NAG E 5 .    ? 159.232 179.942 188.190 1.00 63.32  ? 701  NAG A O4  1 
HETATM 14644 O O5  . NAG E 5 .    ? 159.550 183.589 188.082 1.00 63.32  ? 701  NAG A O5  1 
HETATM 14645 O O6  . NAG E 5 .    ? 159.486 182.117 190.681 1.00 63.32  ? 701  NAG A O6  1 
HETATM 14646 O O7  . NAG E 5 .    ? 163.492 181.782 185.425 1.00 63.32  ? 701  NAG A O7  1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 18  ? 0.9932 0.9932 0.9932 0.0000 0.0000 0.0000 1   SER B N   
2    C CA  . SER A 18  ? 0.9932 0.9932 0.9932 0.0000 0.0000 0.0000 1   SER B CA  
3    C C   . SER A 18  ? 0.9932 0.9932 0.9932 0.0000 0.0000 0.0000 1   SER B C   
4    O O   . SER A 18  ? 0.9932 0.9932 0.9932 0.0000 0.0000 0.0000 1   SER B O   
7    N N   . PRO A 19  ? 1.0118 1.0118 1.0118 0.0000 0.0000 0.0000 2   PRO B N   
8    C CA  . PRO A 19  ? 1.0118 1.0118 1.0118 0.0000 0.0000 0.0000 2   PRO B CA  
9    C C   . PRO A 19  ? 1.0118 1.0118 1.0118 0.0000 0.0000 0.0000 2   PRO B C   
10   O O   . PRO A 19  ? 1.0118 1.0118 1.0118 0.0000 0.0000 0.0000 2   PRO B O   
11   C CB  . PRO A 19  ? 1.0118 1.0118 1.0118 0.0000 0.0000 0.0000 2   PRO B CB  
12   C CG  . PRO A 19  ? 1.0118 1.0118 1.0118 0.0000 0.0000 0.0000 2   PRO B CG  
13   C CD  . PRO A 19  ? 1.0118 1.0118 1.0118 0.0000 0.0000 0.0000 2   PRO B CD  
14   N N   . PHE A 20  ? 0.9472 0.9472 0.9472 0.0000 0.0000 0.0000 3   PHE B N   
15   C CA  . PHE A 20  ? 0.9472 0.9472 0.9472 0.0000 0.0000 0.0000 3   PHE B CA  
16   C C   . PHE A 20  ? 0.9472 0.9472 0.9472 0.0000 0.0000 0.0000 3   PHE B C   
17   O O   . PHE A 20  ? 0.9472 0.9472 0.9472 0.0000 0.0000 0.0000 3   PHE B O   
18   C CB  . PHE A 20  ? 0.9472 0.9472 0.9472 0.0000 0.0000 0.0000 3   PHE B CB  
19   C CG  . PHE A 20  ? 0.9472 0.9472 0.9472 0.0000 0.0000 0.0000 3   PHE B CG  
20   C CD1 . PHE A 20  ? 0.9472 0.9472 0.9472 0.0000 0.0000 0.0000 3   PHE B CD1 
21   C CD2 . PHE A 20  ? 0.9472 0.9472 0.9472 0.0000 0.0000 0.0000 3   PHE B CD2 
22   C CE1 . PHE A 20  ? 0.9472 0.9472 0.9472 0.0000 0.0000 0.0000 3   PHE B CE1 
23   C CE2 . PHE A 20  ? 0.9472 0.9472 0.9472 0.0000 0.0000 0.0000 3   PHE B CE2 
24   C CZ  . PHE A 20  ? 0.9472 0.9472 0.9472 0.0000 0.0000 0.0000 3   PHE B CZ  
25   N N   . VAL A 21  ? 0.9761 0.9761 0.9761 0.0000 0.0000 0.0000 4   VAL B N   
26   C CA  . VAL A 21  ? 0.9761 0.9761 0.9761 0.0000 0.0000 0.0000 4   VAL B CA  
27   C C   . VAL A 21  ? 0.9761 0.9761 0.9761 0.0000 0.0000 0.0000 4   VAL B C   
28   O O   . VAL A 21  ? 0.9761 0.9761 0.9761 0.0000 0.0000 0.0000 4   VAL B O   
29   C CB  . VAL A 21  ? 0.9761 0.9761 0.9761 0.0000 0.0000 0.0000 4   VAL B CB  
30   C CG1 . VAL A 21  ? 0.9761 0.9761 0.9761 0.0000 0.0000 0.0000 4   VAL B CG1 
31   C CG2 . VAL A 21  ? 0.9761 0.9761 0.9761 0.0000 0.0000 0.0000 4   VAL B CG2 
32   N N   . ASN A 22  ? 1.0953 1.0953 1.0953 0.0000 0.0000 0.0000 5   ASN B N   
33   C CA  . ASN A 22  ? 1.0953 1.0953 1.0953 0.0000 0.0000 0.0000 5   ASN B CA  
34   C C   . ASN A 22  ? 1.0953 1.0953 1.0953 0.0000 0.0000 0.0000 5   ASN B C   
35   O O   . ASN A 22  ? 1.0953 1.0953 1.0953 0.0000 0.0000 0.0000 5   ASN B O   
36   C CB  . ASN A 22  ? 1.0953 1.0953 1.0953 0.0000 0.0000 0.0000 5   ASN B CB  
37   C CG  . ASN A 22  ? 1.0953 1.0953 1.0953 0.0000 0.0000 0.0000 5   ASN B CG  
38   O OD1 . ASN A 22  ? 1.0953 1.0953 1.0953 0.0000 0.0000 0.0000 5   ASN B OD1 
39   N ND2 . ASN A 22  ? 1.0953 1.0953 1.0953 0.0000 0.0000 0.0000 5   ASN B ND2 
40   N N   . LYS A 23  ? 1.1512 1.1512 1.1512 0.0000 0.0000 0.0000 6   LYS B N   
41   C CA  . LYS A 23  ? 1.1512 1.1512 1.1512 0.0000 0.0000 0.0000 6   LYS B CA  
42   C C   . LYS A 23  ? 1.1512 1.1512 1.1512 0.0000 0.0000 0.0000 6   LYS B C   
43   O O   . LYS A 23  ? 1.1512 1.1512 1.1512 0.0000 0.0000 0.0000 6   LYS B O   
44   C CB  . LYS A 23  ? 1.1512 1.1512 1.1512 0.0000 0.0000 0.0000 6   LYS B CB  
45   C CG  . LYS A 23  ? 1.1512 1.1512 1.1512 0.0000 0.0000 0.0000 6   LYS B CG  
46   C CD  . LYS A 23  ? 1.1512 1.1512 1.1512 0.0000 0.0000 0.0000 6   LYS B CD  
47   C CE  . LYS A 23  ? 1.1512 1.1512 1.1512 0.0000 0.0000 0.0000 6   LYS B CE  
48   N NZ  . LYS A 23  ? 1.1512 1.1512 1.1512 0.0000 0.0000 0.0000 6   LYS B NZ  
49   N N   . GLN A 24  ? 1.1549 1.1549 1.1549 0.0000 0.0000 0.0000 7   GLN B N   
50   C CA  . GLN A 24  ? 1.1549 1.1549 1.1549 0.0000 0.0000 0.0000 7   GLN B CA  
51   C C   . GLN A 24  ? 1.1549 1.1549 1.1549 0.0000 0.0000 0.0000 7   GLN B C   
52   O O   . GLN A 24  ? 1.1549 1.1549 1.1549 0.0000 0.0000 0.0000 7   GLN B O   
53   C CB  . GLN A 24  ? 1.1549 1.1549 1.1549 0.0000 0.0000 0.0000 7   GLN B CB  
54   C CG  . GLN A 24  ? 1.1549 1.1549 1.1549 0.0000 0.0000 0.0000 7   GLN B CG  
55   C CD  . GLN A 24  ? 1.1549 1.1549 1.1549 0.0000 0.0000 0.0000 7   GLN B CD  
56   O OE1 . GLN A 24  ? 1.1549 1.1549 1.1549 0.0000 0.0000 0.0000 7   GLN B OE1 
57   N NE2 . GLN A 24  ? 1.1549 1.1549 1.1549 0.0000 0.0000 0.0000 7   GLN B NE2 
58   N N   . PHE A 25  ? 1.0729 1.0729 1.0729 0.0000 0.0000 0.0000 8   PHE B N   
59   C CA  . PHE A 25  ? 1.0729 1.0729 1.0729 0.0000 0.0000 0.0000 8   PHE B CA  
60   C C   . PHE A 25  ? 1.0729 1.0729 1.0729 0.0000 0.0000 0.0000 8   PHE B C   
61   O O   . PHE A 25  ? 1.0729 1.0729 1.0729 0.0000 0.0000 0.0000 8   PHE B O   
62   C CB  . PHE A 25  ? 1.0729 1.0729 1.0729 0.0000 0.0000 0.0000 8   PHE B CB  
63   C CG  . PHE A 25  ? 1.0729 1.0729 1.0729 0.0000 0.0000 0.0000 8   PHE B CG  
64   C CD1 . PHE A 25  ? 1.0729 1.0729 1.0729 0.0000 0.0000 0.0000 8   PHE B CD1 
65   C CD2 . PHE A 25  ? 1.0729 1.0729 1.0729 0.0000 0.0000 0.0000 8   PHE B CD2 
66   C CE1 . PHE A 25  ? 1.0729 1.0729 1.0729 0.0000 0.0000 0.0000 8   PHE B CE1 
67   C CE2 . PHE A 25  ? 1.0729 1.0729 1.0729 0.0000 0.0000 0.0000 8   PHE B CE2 
68   C CZ  . PHE A 25  ? 1.0729 1.0729 1.0729 0.0000 0.0000 0.0000 8   PHE B CZ  
69   N N   . ASN A 26  ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 9   ASN B N   
70   C CA  . ASN A 26  ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 9   ASN B CA  
71   C C   . ASN A 26  ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 9   ASN B C   
72   O O   . ASN A 26  ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 9   ASN B O   
73   C CB  . ASN A 26  ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 9   ASN B CB  
74   C CG  . ASN A 26  ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 9   ASN B CG  
75   O OD1 . ASN A 26  ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 9   ASN B OD1 
76   N ND2 . ASN A 26  ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 9   ASN B ND2 
77   N N   . TYR A 27  ? 1.0136 1.0136 1.0136 0.0000 0.0000 0.0000 10  TYR B N   
78   C CA  . TYR A 27  ? 1.0136 1.0136 1.0136 0.0000 0.0000 0.0000 10  TYR B CA  
79   C C   . TYR A 27  ? 1.0136 1.0136 1.0136 0.0000 0.0000 0.0000 10  TYR B C   
80   O O   . TYR A 27  ? 1.0136 1.0136 1.0136 0.0000 0.0000 0.0000 10  TYR B O   
81   C CB  . TYR A 27  ? 1.0136 1.0136 1.0136 0.0000 0.0000 0.0000 10  TYR B CB  
82   C CG  . TYR A 27  ? 1.0136 1.0136 1.0136 0.0000 0.0000 0.0000 10  TYR B CG  
83   C CD1 . TYR A 27  ? 1.0136 1.0136 1.0136 0.0000 0.0000 0.0000 10  TYR B CD1 
84   C CD2 . TYR A 27  ? 1.0136 1.0136 1.0136 0.0000 0.0000 0.0000 10  TYR B CD2 
85   C CE1 . TYR A 27  ? 1.0136 1.0136 1.0136 0.0000 0.0000 0.0000 10  TYR B CE1 
86   C CE2 . TYR A 27  ? 1.0136 1.0136 1.0136 0.0000 0.0000 0.0000 10  TYR B CE2 
87   C CZ  . TYR A 27  ? 1.0136 1.0136 1.0136 0.0000 0.0000 0.0000 10  TYR B CZ  
88   O OH  . TYR A 27  ? 1.0136 1.0136 1.0136 0.0000 0.0000 0.0000 10  TYR B OH  
89   N N   . LYS A 28  ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 11  LYS B N   
90   C CA  . LYS A 28  ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 11  LYS B CA  
91   C C   . LYS A 28  ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 11  LYS B C   
92   O O   . LYS A 28  ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 11  LYS B O   
93   C CB  . LYS A 28  ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 11  LYS B CB  
94   C CG  . LYS A 28  ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 11  LYS B CG  
95   C CD  . LYS A 28  ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 11  LYS B CD  
96   C CE  . LYS A 28  ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 11  LYS B CE  
97   N NZ  . LYS A 28  ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 11  LYS B NZ  
98   N N   . ASP A 29  ? 1.0621 1.0621 1.0621 0.0000 0.0000 0.0000 12  ASP B N   
99   C CA  . ASP A 29  ? 1.0621 1.0621 1.0621 0.0000 0.0000 0.0000 12  ASP B CA  
100  C C   . ASP A 29  ? 1.0621 1.0621 1.0621 0.0000 0.0000 0.0000 12  ASP B C   
101  O O   . ASP A 29  ? 1.0621 1.0621 1.0621 0.0000 0.0000 0.0000 12  ASP B O   
102  C CB  . ASP A 29  ? 1.0621 1.0621 1.0621 0.0000 0.0000 0.0000 12  ASP B CB  
103  C CG  . ASP A 29  ? 1.0621 1.0621 1.0621 0.0000 0.0000 0.0000 12  ASP B CG  
104  O OD1 . ASP A 29  ? 1.0621 1.0621 1.0621 0.0000 0.0000 0.0000 12  ASP B OD1 
105  O OD2 . ASP A 29  ? 1.0621 1.0621 1.0621 0.0000 0.0000 0.0000 12  ASP B OD2 
106  N N   . PRO A 30  ? 1.0792 1.0792 1.0792 0.0000 0.0000 0.0000 13  PRO B N   
107  C CA  . PRO A 30  ? 1.0792 1.0792 1.0792 0.0000 0.0000 0.0000 13  PRO B CA  
108  C C   . PRO A 30  ? 1.0792 1.0792 1.0792 0.0000 0.0000 0.0000 13  PRO B C   
109  O O   . PRO A 30  ? 1.0792 1.0792 1.0792 0.0000 0.0000 0.0000 13  PRO B O   
110  C CB  . PRO A 30  ? 1.0792 1.0792 1.0792 0.0000 0.0000 0.0000 13  PRO B CB  
111  C CG  . PRO A 30  ? 1.0792 1.0792 1.0792 0.0000 0.0000 0.0000 13  PRO B CG  
112  C CD  . PRO A 30  ? 1.0792 1.0792 1.0792 0.0000 0.0000 0.0000 13  PRO B CD  
113  N N   . VAL A 31  ? 1.0679 1.0679 1.0679 0.0000 0.0000 0.0000 14  VAL B N   
114  C CA  . VAL A 31  ? 1.0679 1.0679 1.0679 0.0000 0.0000 0.0000 14  VAL B CA  
115  C C   . VAL A 31  ? 1.0679 1.0679 1.0679 0.0000 0.0000 0.0000 14  VAL B C   
116  O O   . VAL A 31  ? 1.0679 1.0679 1.0679 0.0000 0.0000 0.0000 14  VAL B O   
117  C CB  . VAL A 31  ? 1.0679 1.0679 1.0679 0.0000 0.0000 0.0000 14  VAL B CB  
118  C CG1 . VAL A 31  ? 1.0679 1.0679 1.0679 0.0000 0.0000 0.0000 14  VAL B CG1 
119  C CG2 . VAL A 31  ? 1.0679 1.0679 1.0679 0.0000 0.0000 0.0000 14  VAL B CG2 
120  N N   . ASN A 32  ? 1.0972 1.0972 1.0972 0.0000 0.0000 0.0000 15  ASN B N   
121  C CA  . ASN A 32  ? 1.0972 1.0972 1.0972 0.0000 0.0000 0.0000 15  ASN B CA  
122  C C   . ASN A 32  ? 1.0972 1.0972 1.0972 0.0000 0.0000 0.0000 15  ASN B C   
123  O O   . ASN A 32  ? 1.0972 1.0972 1.0972 0.0000 0.0000 0.0000 15  ASN B O   
124  C CB  . ASN A 32  ? 1.0972 1.0972 1.0972 0.0000 0.0000 0.0000 15  ASN B CB  
125  C CG  . ASN A 32  ? 1.0972 1.0972 1.0972 0.0000 0.0000 0.0000 15  ASN B CG  
126  O OD1 . ASN A 32  ? 1.0972 1.0972 1.0972 0.0000 0.0000 0.0000 15  ASN B OD1 
127  N ND2 . ASN A 32  ? 1.0972 1.0972 1.0972 0.0000 0.0000 0.0000 15  ASN B ND2 
128  N N   . GLY A 33  ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 16  GLY B N   
129  C CA  . GLY A 33  ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 16  GLY B CA  
130  C C   . GLY A 33  ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 16  GLY B C   
131  O O   . GLY A 33  ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 16  GLY B O   
132  N N   . VAL A 34  ? 1.0216 1.0216 1.0216 0.0000 0.0000 0.0000 17  VAL B N   
133  C CA  . VAL A 34  ? 1.0216 1.0216 1.0216 0.0000 0.0000 0.0000 17  VAL B CA  
134  C C   . VAL A 34  ? 1.0216 1.0216 1.0216 0.0000 0.0000 0.0000 17  VAL B C   
135  O O   . VAL A 34  ? 1.0216 1.0216 1.0216 0.0000 0.0000 0.0000 17  VAL B O   
136  C CB  . VAL A 34  ? 1.0216 1.0216 1.0216 0.0000 0.0000 0.0000 17  VAL B CB  
137  C CG1 . VAL A 34  ? 1.0216 1.0216 1.0216 0.0000 0.0000 0.0000 17  VAL B CG1 
138  C CG2 . VAL A 34  ? 1.0216 1.0216 1.0216 0.0000 0.0000 0.0000 17  VAL B CG2 
139  N N   . ASP A 35  ? 1.0104 1.0104 1.0104 0.0000 0.0000 0.0000 18  ASP B N   
140  C CA  . ASP A 35  ? 1.0104 1.0104 1.0104 0.0000 0.0000 0.0000 18  ASP B CA  
141  C C   . ASP A 35  ? 1.0104 1.0104 1.0104 0.0000 0.0000 0.0000 18  ASP B C   
142  O O   . ASP A 35  ? 1.0104 1.0104 1.0104 0.0000 0.0000 0.0000 18  ASP B O   
143  C CB  . ASP A 35  ? 1.0104 1.0104 1.0104 0.0000 0.0000 0.0000 18  ASP B CB  
144  C CG  . ASP A 35  ? 1.0104 1.0104 1.0104 0.0000 0.0000 0.0000 18  ASP B CG  
145  O OD1 . ASP A 35  ? 1.0104 1.0104 1.0104 0.0000 0.0000 0.0000 18  ASP B OD1 
146  O OD2 . ASP A 35  ? 1.0104 1.0104 1.0104 0.0000 0.0000 0.0000 18  ASP B OD2 
147  N N   . ILE A 36  ? 0.9576 0.9576 0.9576 0.0000 0.0000 0.0000 19  ILE B N   
148  C CA  . ILE A 36  ? 0.9576 0.9576 0.9576 0.0000 0.0000 0.0000 19  ILE B CA  
149  C C   . ILE A 36  ? 0.9576 0.9576 0.9576 0.0000 0.0000 0.0000 19  ILE B C   
150  O O   . ILE A 36  ? 0.9576 0.9576 0.9576 0.0000 0.0000 0.0000 19  ILE B O   
151  C CB  . ILE A 36  ? 0.9576 0.9576 0.9576 0.0000 0.0000 0.0000 19  ILE B CB  
152  C CG1 . ILE A 36  ? 0.9576 0.9576 0.9576 0.0000 0.0000 0.0000 19  ILE B CG1 
153  C CG2 . ILE A 36  ? 0.9576 0.9576 0.9576 0.0000 0.0000 0.0000 19  ILE B CG2 
154  C CD1 . ILE A 36  ? 0.9576 0.9576 0.9576 0.0000 0.0000 0.0000 19  ILE B CD1 
155  N N   . ALA A 37  ? 0.9370 0.9370 0.9370 0.0000 0.0000 0.0000 20  ALA B N   
156  C CA  . ALA A 37  ? 0.9370 0.9370 0.9370 0.0000 0.0000 0.0000 20  ALA B CA  
157  C C   . ALA A 37  ? 0.9370 0.9370 0.9370 0.0000 0.0000 0.0000 20  ALA B C   
158  O O   . ALA A 37  ? 0.9370 0.9370 0.9370 0.0000 0.0000 0.0000 20  ALA B O   
159  C CB  . ALA A 37  ? 0.9370 0.9370 0.9370 0.0000 0.0000 0.0000 20  ALA B CB  
160  N N   . TYR A 38  ? 1.0053 1.0053 1.0053 0.0000 0.0000 0.0000 21  TYR B N   
161  C CA  . TYR A 38  ? 1.0053 1.0053 1.0053 0.0000 0.0000 0.0000 21  TYR B CA  
162  C C   . TYR A 38  ? 1.0053 1.0053 1.0053 0.0000 0.0000 0.0000 21  TYR B C   
163  O O   . TYR A 38  ? 1.0053 1.0053 1.0053 0.0000 0.0000 0.0000 21  TYR B O   
164  C CB  . TYR A 38  ? 1.0053 1.0053 1.0053 0.0000 0.0000 0.0000 21  TYR B CB  
165  C CG  . TYR A 38  ? 1.0053 1.0053 1.0053 0.0000 0.0000 0.0000 21  TYR B CG  
166  C CD1 . TYR A 38  ? 1.0053 1.0053 1.0053 0.0000 0.0000 0.0000 21  TYR B CD1 
167  C CD2 . TYR A 38  ? 1.0053 1.0053 1.0053 0.0000 0.0000 0.0000 21  TYR B CD2 
168  C CE1 . TYR A 38  ? 1.0053 1.0053 1.0053 0.0000 0.0000 0.0000 21  TYR B CE1 
169  C CE2 . TYR A 38  ? 1.0053 1.0053 1.0053 0.0000 0.0000 0.0000 21  TYR B CE2 
170  C CZ  . TYR A 38  ? 1.0053 1.0053 1.0053 0.0000 0.0000 0.0000 21  TYR B CZ  
171  O OH  . TYR A 38  ? 1.0053 1.0053 1.0053 0.0000 0.0000 0.0000 21  TYR B OH  
172  N N   . ILE A 39  ? 0.9456 0.9456 0.9456 0.0000 0.0000 0.0000 22  ILE B N   
173  C CA  . ILE A 39  ? 0.9456 0.9456 0.9456 0.0000 0.0000 0.0000 22  ILE B CA  
174  C C   . ILE A 39  ? 0.9456 0.9456 0.9456 0.0000 0.0000 0.0000 22  ILE B C   
175  O O   . ILE A 39  ? 0.9456 0.9456 0.9456 0.0000 0.0000 0.0000 22  ILE B O   
176  C CB  . ILE A 39  ? 0.9456 0.9456 0.9456 0.0000 0.0000 0.0000 22  ILE B CB  
177  C CG1 . ILE A 39  ? 0.9456 0.9456 0.9456 0.0000 0.0000 0.0000 22  ILE B CG1 
178  C CG2 . ILE A 39  ? 0.9456 0.9456 0.9456 0.0000 0.0000 0.0000 22  ILE B CG2 
179  C CD1 . ILE A 39  ? 0.9456 0.9456 0.9456 0.0000 0.0000 0.0000 22  ILE B CD1 
180  N N   . LYS A 40  ? 0.9633 0.9633 0.9633 0.0000 0.0000 0.0000 23  LYS B N   
181  C CA  . LYS A 40  ? 0.9633 0.9633 0.9633 0.0000 0.0000 0.0000 23  LYS B CA  
182  C C   . LYS A 40  ? 0.9633 0.9633 0.9633 0.0000 0.0000 0.0000 23  LYS B C   
183  O O   . LYS A 40  ? 0.9633 0.9633 0.9633 0.0000 0.0000 0.0000 23  LYS B O   
184  C CB  . LYS A 40  ? 0.9633 0.9633 0.9633 0.0000 0.0000 0.0000 23  LYS B CB  
185  C CG  . LYS A 40  ? 0.9633 0.9633 0.9633 0.0000 0.0000 0.0000 23  LYS B CG  
186  C CD  . LYS A 40  ? 0.9633 0.9633 0.9633 0.0000 0.0000 0.0000 23  LYS B CD  
187  C CE  . LYS A 40  ? 0.9633 0.9633 0.9633 0.0000 0.0000 0.0000 23  LYS B CE  
188  N NZ  . LYS A 40  ? 0.9633 0.9633 0.9633 0.0000 0.0000 0.0000 23  LYS B NZ  
189  N N   . ILE A 41  ? 0.9903 0.9903 0.9903 0.0000 0.0000 0.0000 24  ILE B N   
190  C CA  . ILE A 41  ? 0.9903 0.9903 0.9903 0.0000 0.0000 0.0000 24  ILE B CA  
191  C C   . ILE A 41  ? 0.9903 0.9903 0.9903 0.0000 0.0000 0.0000 24  ILE B C   
192  O O   . ILE A 41  ? 0.9903 0.9903 0.9903 0.0000 0.0000 0.0000 24  ILE B O   
193  C CB  . ILE A 41  ? 0.9903 0.9903 0.9903 0.0000 0.0000 0.0000 24  ILE B CB  
194  C CG1 . ILE A 41  ? 0.9903 0.9903 0.9903 0.0000 0.0000 0.0000 24  ILE B CG1 
195  C CG2 . ILE A 41  ? 0.9903 0.9903 0.9903 0.0000 0.0000 0.0000 24  ILE B CG2 
196  C CD1 . ILE A 41  ? 0.9903 0.9903 0.9903 0.0000 0.0000 0.0000 24  ILE B CD1 
197  N N   . PRO A 42  ? 1.0234 1.0234 1.0234 0.0000 0.0000 0.0000 25  PRO B N   
198  C CA  . PRO A 42  ? 1.0234 1.0234 1.0234 0.0000 0.0000 0.0000 25  PRO B CA  
199  C C   . PRO A 42  ? 1.0234 1.0234 1.0234 0.0000 0.0000 0.0000 25  PRO B C   
200  O O   . PRO A 42  ? 1.0234 1.0234 1.0234 0.0000 0.0000 0.0000 25  PRO B O   
201  C CB  . PRO A 42  ? 1.0234 1.0234 1.0234 0.0000 0.0000 0.0000 25  PRO B CB  
202  C CG  . PRO A 42  ? 1.0234 1.0234 1.0234 0.0000 0.0000 0.0000 25  PRO B CG  
203  C CD  . PRO A 42  ? 1.0234 1.0234 1.0234 0.0000 0.0000 0.0000 25  PRO B CD  
204  N N   . ASN A 43  ? 1.1191 1.1191 1.1191 0.0000 0.0000 0.0000 26  ASN B N   
205  C CA  . ASN A 43  ? 1.1191 1.1191 1.1191 0.0000 0.0000 0.0000 26  ASN B CA  
206  C C   . ASN A 43  ? 1.1191 1.1191 1.1191 0.0000 0.0000 0.0000 26  ASN B C   
207  O O   . ASN A 43  ? 1.1191 1.1191 1.1191 0.0000 0.0000 0.0000 26  ASN B O   
208  C CB  . ASN A 43  ? 1.1191 1.1191 1.1191 0.0000 0.0000 0.0000 26  ASN B CB  
209  C CG  . ASN A 43  ? 1.1191 1.1191 1.1191 0.0000 0.0000 0.0000 26  ASN B CG  
210  O OD1 . ASN A 43  ? 1.1191 1.1191 1.1191 0.0000 0.0000 0.0000 26  ASN B OD1 
211  N ND2 . ASN A 43  ? 1.1191 1.1191 1.1191 0.0000 0.0000 0.0000 26  ASN B ND2 
212  N N   . ALA A 44  ? 1.2306 1.2306 1.2306 0.0000 0.0000 0.0000 27  ALA B N   
213  C CA  . ALA A 44  ? 1.2306 1.2306 1.2306 0.0000 0.0000 0.0000 27  ALA B CA  
214  C C   . ALA A 44  ? 1.2306 1.2306 1.2306 0.0000 0.0000 0.0000 27  ALA B C   
215  O O   . ALA A 44  ? 1.2306 1.2306 1.2306 0.0000 0.0000 0.0000 27  ALA B O   
216  C CB  . ALA A 44  ? 1.2306 1.2306 1.2306 0.0000 0.0000 0.0000 27  ALA B CB  
217  N N   . GLY A 45  ? 1.2138 1.2138 1.2138 0.0000 0.0000 0.0000 28  GLY B N   
218  C CA  . GLY A 45  ? 1.2138 1.2138 1.2138 0.0000 0.0000 0.0000 28  GLY B CA  
219  C C   . GLY A 45  ? 1.2138 1.2138 1.2138 0.0000 0.0000 0.0000 28  GLY B C   
220  O O   . GLY A 45  ? 1.2138 1.2138 1.2138 0.0000 0.0000 0.0000 28  GLY B O   
221  N N   . GLN A 46  ? 1.2079 1.2079 1.2079 0.0000 0.0000 0.0000 29  GLN B N   
222  C CA  . GLN A 46  ? 1.2079 1.2079 1.2079 0.0000 0.0000 0.0000 29  GLN B CA  
223  C C   . GLN A 46  ? 1.2079 1.2079 1.2079 0.0000 0.0000 0.0000 29  GLN B C   
224  O O   . GLN A 46  ? 1.2079 1.2079 1.2079 0.0000 0.0000 0.0000 29  GLN B O   
225  C CB  . GLN A 46  ? 1.2079 1.2079 1.2079 0.0000 0.0000 0.0000 29  GLN B CB  
226  C CG  . GLN A 46  ? 1.2079 1.2079 1.2079 0.0000 0.0000 0.0000 29  GLN B CG  
227  C CD  . GLN A 46  ? 1.2079 1.2079 1.2079 0.0000 0.0000 0.0000 29  GLN B CD  
228  O OE1 . GLN A 46  ? 1.2079 1.2079 1.2079 0.0000 0.0000 0.0000 29  GLN B OE1 
229  N NE2 . GLN A 46  ? 1.2079 1.2079 1.2079 0.0000 0.0000 0.0000 29  GLN B NE2 
230  N N   . MET A 47  ? 1.1145 1.1145 1.1145 0.0000 0.0000 0.0000 30  MET B N   
231  C CA  . MET A 47  ? 1.1145 1.1145 1.1145 0.0000 0.0000 0.0000 30  MET B CA  
232  C C   . MET A 47  ? 1.1145 1.1145 1.1145 0.0000 0.0000 0.0000 30  MET B C   
233  O O   . MET A 47  ? 1.1145 1.1145 1.1145 0.0000 0.0000 0.0000 30  MET B O   
234  C CB  . MET A 47  ? 1.1145 1.1145 1.1145 0.0000 0.0000 0.0000 30  MET B CB  
235  C CG  . MET A 47  ? 1.1145 1.1145 1.1145 0.0000 0.0000 0.0000 30  MET B CG  
236  S SD  . MET A 47  ? 1.1145 1.1145 1.1145 0.0000 0.0000 0.0000 30  MET B SD  
237  C CE  . MET A 47  ? 1.1145 1.1145 1.1145 0.0000 0.0000 0.0000 30  MET B CE  
238  N N   . GLN A 48  ? 1.1007 1.1007 1.1007 0.0000 0.0000 0.0000 31  GLN B N   
239  C CA  . GLN A 48  ? 1.1007 1.1007 1.1007 0.0000 0.0000 0.0000 31  GLN B CA  
240  C C   . GLN A 48  ? 1.1007 1.1007 1.1007 0.0000 0.0000 0.0000 31  GLN B C   
241  O O   . GLN A 48  ? 1.1007 1.1007 1.1007 0.0000 0.0000 0.0000 31  GLN B O   
242  C CB  . GLN A 48  ? 1.1007 1.1007 1.1007 0.0000 0.0000 0.0000 31  GLN B CB  
243  C CG  . GLN A 48  ? 1.1007 1.1007 1.1007 0.0000 0.0000 0.0000 31  GLN B CG  
244  C CD  . GLN A 48  ? 1.1007 1.1007 1.1007 0.0000 0.0000 0.0000 31  GLN B CD  
245  O OE1 . GLN A 48  ? 1.1007 1.1007 1.1007 0.0000 0.0000 0.0000 31  GLN B OE1 
246  N NE2 . GLN A 48  ? 1.1007 1.1007 1.1007 0.0000 0.0000 0.0000 31  GLN B NE2 
247  N N   . PRO A 49  ? 1.0364 1.0364 1.0364 0.0000 0.0000 0.0000 32  PRO B N   
248  C CA  . PRO A 49  ? 1.0364 1.0364 1.0364 0.0000 0.0000 0.0000 32  PRO B CA  
249  C C   . PRO A 49  ? 1.0364 1.0364 1.0364 0.0000 0.0000 0.0000 32  PRO B C   
250  O O   . PRO A 49  ? 1.0364 1.0364 1.0364 0.0000 0.0000 0.0000 32  PRO B O   
251  C CB  . PRO A 49  ? 1.0364 1.0364 1.0364 0.0000 0.0000 0.0000 32  PRO B CB  
252  C CG  . PRO A 49  ? 1.0364 1.0364 1.0364 0.0000 0.0000 0.0000 32  PRO B CG  
253  C CD  . PRO A 49  ? 1.0364 1.0364 1.0364 0.0000 0.0000 0.0000 32  PRO B CD  
254  N N   . VAL A 50  ? 0.9624 0.9624 0.9624 0.0000 0.0000 0.0000 33  VAL B N   
255  C CA  . VAL A 50  ? 0.9624 0.9624 0.9624 0.0000 0.0000 0.0000 33  VAL B CA  
256  C C   . VAL A 50  ? 0.9624 0.9624 0.9624 0.0000 0.0000 0.0000 33  VAL B C   
257  O O   . VAL A 50  ? 0.9624 0.9624 0.9624 0.0000 0.0000 0.0000 33  VAL B O   
258  C CB  . VAL A 50  ? 0.9624 0.9624 0.9624 0.0000 0.0000 0.0000 33  VAL B CB  
259  C CG1 . VAL A 50  ? 0.9624 0.9624 0.9624 0.0000 0.0000 0.0000 33  VAL B CG1 
260  C CG2 . VAL A 50  ? 0.9624 0.9624 0.9624 0.0000 0.0000 0.0000 33  VAL B CG2 
261  N N   . LYS A 51  ? 0.9066 0.9066 0.9066 0.0000 0.0000 0.0000 34  LYS B N   
262  C CA  . LYS A 51  ? 0.9066 0.9066 0.9066 0.0000 0.0000 0.0000 34  LYS B CA  
263  C C   . LYS A 51  ? 0.9066 0.9066 0.9066 0.0000 0.0000 0.0000 34  LYS B C   
264  O O   . LYS A 51  ? 0.9066 0.9066 0.9066 0.0000 0.0000 0.0000 34  LYS B O   
265  C CB  . LYS A 51  ? 0.9066 0.9066 0.9066 0.0000 0.0000 0.0000 34  LYS B CB  
266  C CG  . LYS A 51  ? 0.9066 0.9066 0.9066 0.0000 0.0000 0.0000 34  LYS B CG  
267  C CD  . LYS A 51  ? 0.9066 0.9066 0.9066 0.0000 0.0000 0.0000 34  LYS B CD  
268  C CE  . LYS A 51  ? 0.9066 0.9066 0.9066 0.0000 0.0000 0.0000 34  LYS B CE  
269  N NZ  . LYS A 51  ? 0.9066 0.9066 0.9066 0.0000 0.0000 0.0000 34  LYS B NZ  
270  N N   . ALA A 52  ? 0.8911 0.8911 0.8911 0.0000 0.0000 0.0000 35  ALA B N   
271  C CA  . ALA A 52  ? 0.8911 0.8911 0.8911 0.0000 0.0000 0.0000 35  ALA B CA  
272  C C   . ALA A 52  ? 0.8911 0.8911 0.8911 0.0000 0.0000 0.0000 35  ALA B C   
273  O O   . ALA A 52  ? 0.8911 0.8911 0.8911 0.0000 0.0000 0.0000 35  ALA B O   
274  C CB  . ALA A 52  ? 0.8911 0.8911 0.8911 0.0000 0.0000 0.0000 35  ALA B CB  
275  N N   . PHE A 53  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 36  PHE B N   
276  C CA  . PHE A 53  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 36  PHE B CA  
277  C C   . PHE A 53  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 36  PHE B C   
278  O O   . PHE A 53  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 36  PHE B O   
279  C CB  . PHE A 53  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 36  PHE B CB  
280  C CG  . PHE A 53  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 36  PHE B CG  
281  C CD1 . PHE A 53  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 36  PHE B CD1 
282  C CD2 . PHE A 53  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 36  PHE B CD2 
283  C CE1 . PHE A 53  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 36  PHE B CE1 
284  C CE2 . PHE A 53  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 36  PHE B CE2 
285  C CZ  . PHE A 53  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 36  PHE B CZ  
286  N N   . LYS A 54  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 37  LYS B N   
287  C CA  . LYS A 54  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 37  LYS B CA  
288  C C   . LYS A 54  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 37  LYS B C   
289  O O   . LYS A 54  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 37  LYS B O   
290  C CB  . LYS A 54  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 37  LYS B CB  
291  C CG  . LYS A 54  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 37  LYS B CG  
292  C CD  . LYS A 54  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 37  LYS B CD  
293  C CE  . LYS A 54  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 37  LYS B CE  
294  N NZ  . LYS A 54  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 37  LYS B NZ  
295  N N   . ILE A 55  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 38  ILE B N   
296  C CA  . ILE A 55  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 38  ILE B CA  
297  C C   . ILE A 55  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 38  ILE B C   
298  O O   . ILE A 55  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 38  ILE B O   
299  C CB  . ILE A 55  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 38  ILE B CB  
300  C CG1 . ILE A 55  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 38  ILE B CG1 
301  C CG2 . ILE A 55  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 38  ILE B CG2 
302  C CD1 . ILE A 55  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 38  ILE B CD1 
303  N N   . HIS A 56  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 39  HIS B N   
304  C CA  . HIS A 56  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 39  HIS B CA  
305  C C   . HIS A 56  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 39  HIS B C   
306  O O   . HIS A 56  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 39  HIS B O   
307  C CB  . HIS A 56  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 39  HIS B CB  
308  C CG  . HIS A 56  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 39  HIS B CG  
309  N ND1 . HIS A 56  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 39  HIS B ND1 
310  C CD2 . HIS A 56  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 39  HIS B CD2 
311  C CE1 . HIS A 56  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 39  HIS B CE1 
312  N NE2 . HIS A 56  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 39  HIS B NE2 
313  N N   . ASN A 57  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 40  ASN B N   
314  C CA  . ASN A 57  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 40  ASN B CA  
315  C C   . ASN A 57  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 40  ASN B C   
316  O O   . ASN A 57  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 40  ASN B O   
317  C CB  . ASN A 57  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 40  ASN B CB  
318  C CG  . ASN A 57  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 40  ASN B CG  
319  O OD1 . ASN A 57  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 40  ASN B OD1 
320  N ND2 . ASN A 57  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 40  ASN B ND2 
321  N N   . LYS A 58  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 41  LYS B N   
322  C CA  . LYS A 58  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 41  LYS B CA  
323  C C   . LYS A 58  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 41  LYS B C   
324  O O   . LYS A 58  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 41  LYS B O   
325  C CB  . LYS A 58  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 41  LYS B CB  
326  C CG  . LYS A 58  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 41  LYS B CG  
327  C CD  . LYS A 58  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 41  LYS B CD  
328  C CE  . LYS A 58  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 41  LYS B CE  
329  N NZ  . LYS A 58  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 41  LYS B NZ  
330  N N   . ILE A 59  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 42  ILE B N   
331  C CA  . ILE A 59  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 42  ILE B CA  
332  C C   . ILE A 59  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 42  ILE B C   
333  O O   . ILE A 59  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 42  ILE B O   
334  C CB  . ILE A 59  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 42  ILE B CB  
335  C CG1 . ILE A 59  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 42  ILE B CG1 
336  C CG2 . ILE A 59  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 42  ILE B CG2 
337  C CD1 . ILE A 59  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 42  ILE B CD1 
338  N N   . TRP A 60  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 43  TRP B N   
339  C CA  . TRP A 60  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 43  TRP B CA  
340  C C   . TRP A 60  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 43  TRP B C   
341  O O   . TRP A 60  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 43  TRP B O   
342  C CB  . TRP A 60  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 43  TRP B CB  
343  C CG  . TRP A 60  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 43  TRP B CG  
344  C CD1 . TRP A 60  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 43  TRP B CD1 
345  C CD2 . TRP A 60  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 43  TRP B CD2 
346  N NE1 . TRP A 60  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 43  TRP B NE1 
347  C CE2 . TRP A 60  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 43  TRP B CE2 
348  C CE3 . TRP A 60  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 43  TRP B CE3 
349  C CZ2 . TRP A 60  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 43  TRP B CZ2 
350  C CZ3 . TRP A 60  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 43  TRP B CZ3 
351  C CH2 . TRP A 60  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 43  TRP B CH2 
352  N N   . VAL A 61  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 44  VAL B N   
353  C CA  . VAL A 61  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 44  VAL B CA  
354  C C   . VAL A 61  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 44  VAL B C   
355  O O   . VAL A 61  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 44  VAL B O   
356  C CB  . VAL A 61  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 44  VAL B CB  
357  C CG1 . VAL A 61  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 44  VAL B CG1 
358  C CG2 . VAL A 61  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 44  VAL B CG2 
359  N N   . ILE A 62  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 45  ILE B N   
360  C CA  . ILE A 62  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 45  ILE B CA  
361  C C   . ILE A 62  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 45  ILE B C   
362  O O   . ILE A 62  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 45  ILE B O   
363  C CB  . ILE A 62  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 45  ILE B CB  
364  C CG1 . ILE A 62  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 45  ILE B CG1 
365  C CG2 . ILE A 62  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 45  ILE B CG2 
366  C CD1 . ILE A 62  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 45  ILE B CD1 
367  N N   . PRO A 63  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 46  PRO B N   
368  C CA  . PRO A 63  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 46  PRO B CA  
369  C C   . PRO A 63  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 46  PRO B C   
370  O O   . PRO A 63  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 46  PRO B O   
371  C CB  . PRO A 63  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 46  PRO B CB  
372  C CG  . PRO A 63  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 46  PRO B CG  
373  C CD  . PRO A 63  ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 46  PRO B CD  
374  N N   . GLU A 64  ? 0.8952 0.8952 0.8952 0.0000 0.0000 0.0000 47  GLU B N   
375  C CA  . GLU A 64  ? 0.8952 0.8952 0.8952 0.0000 0.0000 0.0000 47  GLU B CA  
376  C C   . GLU A 64  ? 0.8952 0.8952 0.8952 0.0000 0.0000 0.0000 47  GLU B C   
377  O O   . GLU A 64  ? 0.8952 0.8952 0.8952 0.0000 0.0000 0.0000 47  GLU B O   
378  C CB  . GLU A 64  ? 0.8952 0.8952 0.8952 0.0000 0.0000 0.0000 47  GLU B CB  
379  C CG  . GLU A 64  ? 0.8952 0.8952 0.8952 0.0000 0.0000 0.0000 47  GLU B CG  
380  C CD  . GLU A 64  ? 0.8952 0.8952 0.8952 0.0000 0.0000 0.0000 47  GLU B CD  
381  O OE1 . GLU A 64  ? 0.8952 0.8952 0.8952 0.0000 0.0000 0.0000 47  GLU B OE1 
382  O OE2 . GLU A 64  ? 0.8952 0.8952 0.8952 0.0000 0.0000 0.0000 47  GLU B OE2 
383  N N   . ARG A 65  ? 0.9391 0.9391 0.9391 0.0000 0.0000 0.0000 48  ARG B N   
384  C CA  . ARG A 65  ? 0.9391 0.9391 0.9391 0.0000 0.0000 0.0000 48  ARG B CA  
385  C C   . ARG A 65  ? 0.9391 0.9391 0.9391 0.0000 0.0000 0.0000 48  ARG B C   
386  O O   . ARG A 65  ? 0.9391 0.9391 0.9391 0.0000 0.0000 0.0000 48  ARG B O   
387  C CB  . ARG A 65  ? 0.9391 0.9391 0.9391 0.0000 0.0000 0.0000 48  ARG B CB  
388  C CG  . ARG A 65  ? 0.9391 0.9391 0.9391 0.0000 0.0000 0.0000 48  ARG B CG  
389  C CD  . ARG A 65  ? 0.9391 0.9391 0.9391 0.0000 0.0000 0.0000 48  ARG B CD  
390  N NE  . ARG A 65  ? 0.9391 0.9391 0.9391 0.0000 0.0000 0.0000 48  ARG B NE  
391  C CZ  . ARG A 65  ? 0.9391 0.9391 0.9391 0.0000 0.0000 0.0000 48  ARG B CZ  
392  N NH1 . ARG A 65  ? 0.9391 0.9391 0.9391 0.0000 0.0000 0.0000 48  ARG B NH1 
393  N NH2 . ARG A 65  ? 0.9391 0.9391 0.9391 0.0000 0.0000 0.0000 48  ARG B NH2 
394  N N   . ASP A 66  ? 1.0138 1.0138 1.0138 0.0000 0.0000 0.0000 49  ASP B N   
395  C CA  . ASP A 66  ? 1.0138 1.0138 1.0138 0.0000 0.0000 0.0000 49  ASP B CA  
396  C C   . ASP A 66  ? 1.0138 1.0138 1.0138 0.0000 0.0000 0.0000 49  ASP B C   
397  O O   . ASP A 66  ? 1.0138 1.0138 1.0138 0.0000 0.0000 0.0000 49  ASP B O   
398  C CB  . ASP A 66  ? 1.0138 1.0138 1.0138 0.0000 0.0000 0.0000 49  ASP B CB  
399  C CG  . ASP A 66  ? 1.0138 1.0138 1.0138 0.0000 0.0000 0.0000 49  ASP B CG  
400  O OD1 . ASP A 66  ? 1.0138 1.0138 1.0138 0.0000 0.0000 0.0000 49  ASP B OD1 
401  O OD2 . ASP A 66  ? 1.0138 1.0138 1.0138 0.0000 0.0000 0.0000 49  ASP B OD2 
402  N N   . THR A 67  ? 1.1036 1.1036 1.1036 0.0000 0.0000 0.0000 50  THR B N   
403  C CA  . THR A 67  ? 1.1036 1.1036 1.1036 0.0000 0.0000 0.0000 50  THR B CA  
404  C C   . THR A 67  ? 1.1036 1.1036 1.1036 0.0000 0.0000 0.0000 50  THR B C   
405  O O   . THR A 67  ? 1.1036 1.1036 1.1036 0.0000 0.0000 0.0000 50  THR B O   
406  C CB  . THR A 67  ? 1.1036 1.1036 1.1036 0.0000 0.0000 0.0000 50  THR B CB  
407  O OG1 . THR A 67  ? 1.1036 1.1036 1.1036 0.0000 0.0000 0.0000 50  THR B OG1 
408  C CG2 . THR A 67  ? 1.1036 1.1036 1.1036 0.0000 0.0000 0.0000 50  THR B CG2 
409  N N   . PHE A 68  ? 1.1280 1.1280 1.1280 0.0000 0.0000 0.0000 51  PHE B N   
410  C CA  . PHE A 68  ? 1.1280 1.1280 1.1280 0.0000 0.0000 0.0000 51  PHE B CA  
411  C C   . PHE A 68  ? 1.1280 1.1280 1.1280 0.0000 0.0000 0.0000 51  PHE B C   
412  O O   . PHE A 68  ? 1.1280 1.1280 1.1280 0.0000 0.0000 0.0000 51  PHE B O   
413  C CB  . PHE A 68  ? 1.1280 1.1280 1.1280 0.0000 0.0000 0.0000 51  PHE B CB  
414  C CG  . PHE A 68  ? 1.1280 1.1280 1.1280 0.0000 0.0000 0.0000 51  PHE B CG  
415  C CD1 . PHE A 68  ? 1.1280 1.1280 1.1280 0.0000 0.0000 0.0000 51  PHE B CD1 
416  C CD2 . PHE A 68  ? 1.1280 1.1280 1.1280 0.0000 0.0000 0.0000 51  PHE B CD2 
417  C CE1 . PHE A 68  ? 1.1280 1.1280 1.1280 0.0000 0.0000 0.0000 51  PHE B CE1 
418  C CE2 . PHE A 68  ? 1.1280 1.1280 1.1280 0.0000 0.0000 0.0000 51  PHE B CE2 
419  C CZ  . PHE A 68  ? 1.1280 1.1280 1.1280 0.0000 0.0000 0.0000 51  PHE B CZ  
420  N N   . THR A 69  ? 1.1811 1.1811 1.1811 0.0000 0.0000 0.0000 52  THR B N   
421  C CA  . THR A 69  ? 1.1811 1.1811 1.1811 0.0000 0.0000 0.0000 52  THR B CA  
422  C C   . THR A 69  ? 1.1811 1.1811 1.1811 0.0000 0.0000 0.0000 52  THR B C   
423  O O   . THR A 69  ? 1.1811 1.1811 1.1811 0.0000 0.0000 0.0000 52  THR B O   
424  C CB  . THR A 69  ? 1.1811 1.1811 1.1811 0.0000 0.0000 0.0000 52  THR B CB  
425  O OG1 . THR A 69  ? 1.1811 1.1811 1.1811 0.0000 0.0000 0.0000 52  THR B OG1 
426  C CG2 . THR A 69  ? 1.1811 1.1811 1.1811 0.0000 0.0000 0.0000 52  THR B CG2 
427  N N   . ASN A 70  ? 1.2930 1.2930 1.2930 0.0000 0.0000 0.0000 53  ASN B N   
428  C CA  . ASN A 70  ? 1.2930 1.2930 1.2930 0.0000 0.0000 0.0000 53  ASN B CA  
429  C C   . ASN A 70  ? 1.2930 1.2930 1.2930 0.0000 0.0000 0.0000 53  ASN B C   
430  O O   . ASN A 70  ? 1.2930 1.2930 1.2930 0.0000 0.0000 0.0000 53  ASN B O   
431  C CB  . ASN A 70  ? 1.2930 1.2930 1.2930 0.0000 0.0000 0.0000 53  ASN B CB  
432  C CG  . ASN A 70  ? 1.2930 1.2930 1.2930 0.0000 0.0000 0.0000 53  ASN B CG  
433  O OD1 . ASN A 70  ? 1.2930 1.2930 1.2930 0.0000 0.0000 0.0000 53  ASN B OD1 
434  N ND2 . ASN A 70  ? 1.2930 1.2930 1.2930 0.0000 0.0000 0.0000 53  ASN B ND2 
435  N N   . PRO A 71  ? 1.3532 1.3532 1.3532 0.0000 0.0000 0.0000 54  PRO B N   
436  C CA  . PRO A 71  ? 1.3532 1.3532 1.3532 0.0000 0.0000 0.0000 54  PRO B CA  
437  C C   . PRO A 71  ? 1.3532 1.3532 1.3532 0.0000 0.0000 0.0000 54  PRO B C   
438  O O   . PRO A 71  ? 1.3532 1.3532 1.3532 0.0000 0.0000 0.0000 54  PRO B O   
439  C CB  . PRO A 71  ? 1.3532 1.3532 1.3532 0.0000 0.0000 0.0000 54  PRO B CB  
440  C CG  . PRO A 71  ? 1.3532 1.3532 1.3532 0.0000 0.0000 0.0000 54  PRO B CG  
441  C CD  . PRO A 71  ? 1.3532 1.3532 1.3532 0.0000 0.0000 0.0000 54  PRO B CD  
442  N N   . GLU A 72  ? 1.3942 1.3942 1.3942 0.0000 0.0000 0.0000 55  GLU B N   
443  C CA  . GLU A 72  ? 1.3942 1.3942 1.3942 0.0000 0.0000 0.0000 55  GLU B CA  
444  C C   . GLU A 72  ? 1.3942 1.3942 1.3942 0.0000 0.0000 0.0000 55  GLU B C   
445  O O   . GLU A 72  ? 1.3942 1.3942 1.3942 0.0000 0.0000 0.0000 55  GLU B O   
446  C CB  . GLU A 72  ? 1.3942 1.3942 1.3942 0.0000 0.0000 0.0000 55  GLU B CB  
447  C CG  . GLU A 72  ? 1.3942 1.3942 1.3942 0.0000 0.0000 0.0000 55  GLU B CG  
448  C CD  . GLU A 72  ? 1.3942 1.3942 1.3942 0.0000 0.0000 0.0000 55  GLU B CD  
449  O OE1 . GLU A 72  ? 1.3942 1.3942 1.3942 0.0000 0.0000 0.0000 55  GLU B OE1 
450  O OE2 . GLU A 72  ? 1.3942 1.3942 1.3942 0.0000 0.0000 0.0000 55  GLU B OE2 
451  N N   . GLU A 73  ? 1.3359 1.3359 1.3359 0.0000 0.0000 0.0000 56  GLU B N   
452  C CA  . GLU A 73  ? 1.3359 1.3359 1.3359 0.0000 0.0000 0.0000 56  GLU B CA  
453  C C   . GLU A 73  ? 1.3359 1.3359 1.3359 0.0000 0.0000 0.0000 56  GLU B C   
454  O O   . GLU A 73  ? 1.3359 1.3359 1.3359 0.0000 0.0000 0.0000 56  GLU B O   
455  C CB  . GLU A 73  ? 1.3359 1.3359 1.3359 0.0000 0.0000 0.0000 56  GLU B CB  
456  C CG  . GLU A 73  ? 1.3359 1.3359 1.3359 0.0000 0.0000 0.0000 56  GLU B CG  
457  C CD  . GLU A 73  ? 1.3359 1.3359 1.3359 0.0000 0.0000 0.0000 56  GLU B CD  
458  O OE1 . GLU A 73  ? 1.3359 1.3359 1.3359 0.0000 0.0000 0.0000 56  GLU B OE1 
459  O OE2 . GLU A 73  ? 1.3359 1.3359 1.3359 0.0000 0.0000 0.0000 56  GLU B OE2 
460  N N   . GLY A 74  ? 1.4140 1.4140 1.4140 0.0000 0.0000 0.0000 57  GLY B N   
461  C CA  . GLY A 74  ? 1.4140 1.4140 1.4140 0.0000 0.0000 0.0000 57  GLY B CA  
462  C C   . GLY A 74  ? 1.4140 1.4140 1.4140 0.0000 0.0000 0.0000 57  GLY B C   
463  O O   . GLY A 74  ? 1.4140 1.4140 1.4140 0.0000 0.0000 0.0000 57  GLY B O   
464  N N   . ASP A 75  ? 1.3506 1.3506 1.3506 0.0000 0.0000 0.0000 58  ASP B N   
465  C CA  . ASP A 75  ? 1.3506 1.3506 1.3506 0.0000 0.0000 0.0000 58  ASP B CA  
466  C C   . ASP A 75  ? 1.3506 1.3506 1.3506 0.0000 0.0000 0.0000 58  ASP B C   
467  O O   . ASP A 75  ? 1.3506 1.3506 1.3506 0.0000 0.0000 0.0000 58  ASP B O   
468  C CB  . ASP A 75  ? 1.3506 1.3506 1.3506 0.0000 0.0000 0.0000 58  ASP B CB  
469  C CG  . ASP A 75  ? 1.3506 1.3506 1.3506 0.0000 0.0000 0.0000 58  ASP B CG  
470  O OD1 . ASP A 75  ? 1.3506 1.3506 1.3506 0.0000 0.0000 0.0000 58  ASP B OD1 
471  O OD2 . ASP A 75  ? 1.3506 1.3506 1.3506 0.0000 0.0000 0.0000 58  ASP B OD2 
472  N N   . LEU A 76  ? 1.2287 1.2287 1.2287 0.0000 0.0000 0.0000 59  LEU B N   
473  C CA  . LEU A 76  ? 1.2287 1.2287 1.2287 0.0000 0.0000 0.0000 59  LEU B CA  
474  C C   . LEU A 76  ? 1.2287 1.2287 1.2287 0.0000 0.0000 0.0000 59  LEU B C   
475  O O   . LEU A 76  ? 1.2287 1.2287 1.2287 0.0000 0.0000 0.0000 59  LEU B O   
476  C CB  . LEU A 76  ? 1.2287 1.2287 1.2287 0.0000 0.0000 0.0000 59  LEU B CB  
477  C CG  . LEU A 76  ? 1.2287 1.2287 1.2287 0.0000 0.0000 0.0000 59  LEU B CG  
478  C CD1 . LEU A 76  ? 1.2287 1.2287 1.2287 0.0000 0.0000 0.0000 59  LEU B CD1 
479  C CD2 . LEU A 76  ? 1.2287 1.2287 1.2287 0.0000 0.0000 0.0000 59  LEU B CD2 
480  N N   . ASN A 77  ? 1.2910 1.2910 1.2910 0.0000 0.0000 0.0000 60  ASN B N   
481  C CA  . ASN A 77  ? 1.2910 1.2910 1.2910 0.0000 0.0000 0.0000 60  ASN B CA  
482  C C   . ASN A 77  ? 1.2910 1.2910 1.2910 0.0000 0.0000 0.0000 60  ASN B C   
483  O O   . ASN A 77  ? 1.2910 1.2910 1.2910 0.0000 0.0000 0.0000 60  ASN B O   
484  C CB  . ASN A 77  ? 1.2910 1.2910 1.2910 0.0000 0.0000 0.0000 60  ASN B CB  
485  C CG  . ASN A 77  ? 1.2910 1.2910 1.2910 0.0000 0.0000 0.0000 60  ASN B CG  
486  O OD1 . ASN A 77  ? 1.2910 1.2910 1.2910 0.0000 0.0000 0.0000 60  ASN B OD1 
487  N ND2 . ASN A 77  ? 1.2910 1.2910 1.2910 0.0000 0.0000 0.0000 60  ASN B ND2 
488  N N   . PRO A 78  ? 1.2518 1.2518 1.2518 0.0000 0.0000 0.0000 61  PRO B N   
489  C CA  . PRO A 78  ? 1.2518 1.2518 1.2518 0.0000 0.0000 0.0000 61  PRO B CA  
490  C C   . PRO A 78  ? 1.2518 1.2518 1.2518 0.0000 0.0000 0.0000 61  PRO B C   
491  O O   . PRO A 78  ? 1.2518 1.2518 1.2518 0.0000 0.0000 0.0000 61  PRO B O   
492  C CB  . PRO A 78  ? 1.2518 1.2518 1.2518 0.0000 0.0000 0.0000 61  PRO B CB  
493  C CG  . PRO A 78  ? 1.2518 1.2518 1.2518 0.0000 0.0000 0.0000 61  PRO B CG  
494  C CD  . PRO A 78  ? 1.2518 1.2518 1.2518 0.0000 0.0000 0.0000 61  PRO B CD  
495  N N   . PRO A 79  ? 1.3267 1.3267 1.3267 0.0000 0.0000 0.0000 62  PRO B N   
496  C CA  . PRO A 79  ? 1.3267 1.3267 1.3267 0.0000 0.0000 0.0000 62  PRO B CA  
497  C C   . PRO A 79  ? 1.3267 1.3267 1.3267 0.0000 0.0000 0.0000 62  PRO B C   
498  O O   . PRO A 79  ? 1.3267 1.3267 1.3267 0.0000 0.0000 0.0000 62  PRO B O   
499  C CB  . PRO A 79  ? 1.3267 1.3267 1.3267 0.0000 0.0000 0.0000 62  PRO B CB  
500  C CG  . PRO A 79  ? 1.3267 1.3267 1.3267 0.0000 0.0000 0.0000 62  PRO B CG  
501  C CD  . PRO A 79  ? 1.3267 1.3267 1.3267 0.0000 0.0000 0.0000 62  PRO B CD  
502  N N   . PRO A 80  ? 1.4227 1.4227 1.4227 0.0000 0.0000 0.0000 63  PRO B N   
503  C CA  . PRO A 80  ? 1.4227 1.4227 1.4227 0.0000 0.0000 0.0000 63  PRO B CA  
504  C C   . PRO A 80  ? 1.4227 1.4227 1.4227 0.0000 0.0000 0.0000 63  PRO B C   
505  O O   . PRO A 80  ? 1.4227 1.4227 1.4227 0.0000 0.0000 0.0000 63  PRO B O   
506  C CB  . PRO A 80  ? 1.4227 1.4227 1.4227 0.0000 0.0000 0.0000 63  PRO B CB  
507  C CG  . PRO A 80  ? 1.4227 1.4227 1.4227 0.0000 0.0000 0.0000 63  PRO B CG  
508  C CD  . PRO A 80  ? 1.4227 1.4227 1.4227 0.0000 0.0000 0.0000 63  PRO B CD  
509  N N   . GLU A 81  ? 1.4311 1.4311 1.4311 0.0000 0.0000 0.0000 64  GLU B N   
510  C CA  . GLU A 81  ? 1.4311 1.4311 1.4311 0.0000 0.0000 0.0000 64  GLU B CA  
511  C C   . GLU A 81  ? 1.4311 1.4311 1.4311 0.0000 0.0000 0.0000 64  GLU B C   
512  O O   . GLU A 81  ? 1.4311 1.4311 1.4311 0.0000 0.0000 0.0000 64  GLU B O   
513  C CB  . GLU A 81  ? 1.4311 1.4311 1.4311 0.0000 0.0000 0.0000 64  GLU B CB  
514  C CG  . GLU A 81  ? 1.4311 1.4311 1.4311 0.0000 0.0000 0.0000 64  GLU B CG  
515  C CD  . GLU A 81  ? 1.4311 1.4311 1.4311 0.0000 0.0000 0.0000 64  GLU B CD  
516  O OE1 . GLU A 81  ? 1.4311 1.4311 1.4311 0.0000 0.0000 0.0000 64  GLU B OE1 
517  O OE2 . GLU A 81  ? 1.4311 1.4311 1.4311 0.0000 0.0000 0.0000 64  GLU B OE2 
518  N N   . ALA A 82  ? 1.2717 1.2717 1.2717 0.0000 0.0000 0.0000 65  ALA B N   
519  C CA  . ALA A 82  ? 1.2717 1.2717 1.2717 0.0000 0.0000 0.0000 65  ALA B CA  
520  C C   . ALA A 82  ? 1.2717 1.2717 1.2717 0.0000 0.0000 0.0000 65  ALA B C   
521  O O   . ALA A 82  ? 1.2717 1.2717 1.2717 0.0000 0.0000 0.0000 65  ALA B O   
522  C CB  . ALA A 82  ? 1.2717 1.2717 1.2717 0.0000 0.0000 0.0000 65  ALA B CB  
523  N N   . LYS A 83  ? 1.1297 1.1297 1.1297 0.0000 0.0000 0.0000 66  LYS B N   
524  C CA  . LYS A 83  ? 1.1297 1.1297 1.1297 0.0000 0.0000 0.0000 66  LYS B CA  
525  C C   . LYS A 83  ? 1.1297 1.1297 1.1297 0.0000 0.0000 0.0000 66  LYS B C   
526  O O   . LYS A 83  ? 1.1297 1.1297 1.1297 0.0000 0.0000 0.0000 66  LYS B O   
527  C CB  . LYS A 83  ? 1.1297 1.1297 1.1297 0.0000 0.0000 0.0000 66  LYS B CB  
528  C CG  . LYS A 83  ? 1.1297 1.1297 1.1297 0.0000 0.0000 0.0000 66  LYS B CG  
529  C CD  . LYS A 83  ? 1.1297 1.1297 1.1297 0.0000 0.0000 0.0000 66  LYS B CD  
530  C CE  . LYS A 83  ? 1.1297 1.1297 1.1297 0.0000 0.0000 0.0000 66  LYS B CE  
531  N NZ  . LYS A 83  ? 1.1297 1.1297 1.1297 0.0000 0.0000 0.0000 66  LYS B NZ  
532  N N   . GLN A 84  ? 1.1457 1.1457 1.1457 0.0000 0.0000 0.0000 67  GLN B N   
533  C CA  . GLN A 84  ? 1.1457 1.1457 1.1457 0.0000 0.0000 0.0000 67  GLN B CA  
534  C C   . GLN A 84  ? 1.1457 1.1457 1.1457 0.0000 0.0000 0.0000 67  GLN B C   
535  O O   . GLN A 84  ? 1.1457 1.1457 1.1457 0.0000 0.0000 0.0000 67  GLN B O   
536  C CB  . GLN A 84  ? 1.1457 1.1457 1.1457 0.0000 0.0000 0.0000 67  GLN B CB  
537  C CG  . GLN A 84  ? 1.1457 1.1457 1.1457 0.0000 0.0000 0.0000 67  GLN B CG  
538  C CD  . GLN A 84  ? 1.1457 1.1457 1.1457 0.0000 0.0000 0.0000 67  GLN B CD  
539  O OE1 . GLN A 84  ? 1.1457 1.1457 1.1457 0.0000 0.0000 0.0000 67  GLN B OE1 
540  N NE2 . GLN A 84  ? 1.1457 1.1457 1.1457 0.0000 0.0000 0.0000 67  GLN B NE2 
541  N N   . VAL A 85  ? 1.0122 1.0122 1.0122 0.0000 0.0000 0.0000 68  VAL B N   
542  C CA  . VAL A 85  ? 1.0122 1.0122 1.0122 0.0000 0.0000 0.0000 68  VAL B CA  
543  C C   . VAL A 85  ? 1.0122 1.0122 1.0122 0.0000 0.0000 0.0000 68  VAL B C   
544  O O   . VAL A 85  ? 1.0122 1.0122 1.0122 0.0000 0.0000 0.0000 68  VAL B O   
545  C CB  . VAL A 85  ? 1.0122 1.0122 1.0122 0.0000 0.0000 0.0000 68  VAL B CB  
546  C CG1 . VAL A 85  ? 1.0122 1.0122 1.0122 0.0000 0.0000 0.0000 68  VAL B CG1 
547  C CG2 . VAL A 85  ? 1.0122 1.0122 1.0122 0.0000 0.0000 0.0000 68  VAL B CG2 
548  N N   . PRO A 86  ? 0.9699 0.9699 0.9699 0.0000 0.0000 0.0000 69  PRO B N   
549  C CA  . PRO A 86  ? 0.9699 0.9699 0.9699 0.0000 0.0000 0.0000 69  PRO B CA  
550  C C   . PRO A 86  ? 0.9699 0.9699 0.9699 0.0000 0.0000 0.0000 69  PRO B C   
551  O O   . PRO A 86  ? 0.9699 0.9699 0.9699 0.0000 0.0000 0.0000 69  PRO B O   
552  C CB  . PRO A 86  ? 0.9699 0.9699 0.9699 0.0000 0.0000 0.0000 69  PRO B CB  
553  C CG  . PRO A 86  ? 0.9699 0.9699 0.9699 0.0000 0.0000 0.0000 69  PRO B CG  
554  C CD  . PRO A 86  ? 0.9699 0.9699 0.9699 0.0000 0.0000 0.0000 69  PRO B CD  
555  N N   . VAL A 87  ? 0.9347 0.9347 0.9347 0.0000 0.0000 0.0000 70  VAL B N   
556  C CA  . VAL A 87  ? 0.9347 0.9347 0.9347 0.0000 0.0000 0.0000 70  VAL B CA  
557  C C   . VAL A 87  ? 0.9347 0.9347 0.9347 0.0000 0.0000 0.0000 70  VAL B C   
558  O O   . VAL A 87  ? 0.9347 0.9347 0.9347 0.0000 0.0000 0.0000 70  VAL B O   
559  C CB  . VAL A 87  ? 0.9347 0.9347 0.9347 0.0000 0.0000 0.0000 70  VAL B CB  
560  C CG1 . VAL A 87  ? 0.9347 0.9347 0.9347 0.0000 0.0000 0.0000 70  VAL B CG1 
561  C CG2 . VAL A 87  ? 0.9347 0.9347 0.9347 0.0000 0.0000 0.0000 70  VAL B CG2 
562  N N   . SER A 88  ? 0.9132 0.9132 0.9132 0.0000 0.0000 0.0000 71  SER B N   
563  C CA  . SER A 88  ? 0.9132 0.9132 0.9132 0.0000 0.0000 0.0000 71  SER B CA  
564  C C   . SER A 88  ? 0.9132 0.9132 0.9132 0.0000 0.0000 0.0000 71  SER B C   
565  O O   . SER A 88  ? 0.9132 0.9132 0.9132 0.0000 0.0000 0.0000 71  SER B O   
566  C CB  . SER A 88  ? 0.9132 0.9132 0.9132 0.0000 0.0000 0.0000 71  SER B CB  
567  O OG  . SER A 88  ? 0.9132 0.9132 0.9132 0.0000 0.0000 0.0000 71  SER B OG  
568  N N   . TYR A 89  ? 0.9389 0.9389 0.9389 0.0000 0.0000 0.0000 72  TYR B N   
569  C CA  . TYR A 89  ? 0.9389 0.9389 0.9389 0.0000 0.0000 0.0000 72  TYR B CA  
570  C C   . TYR A 89  ? 0.9389 0.9389 0.9389 0.0000 0.0000 0.0000 72  TYR B C   
571  O O   . TYR A 89  ? 0.9389 0.9389 0.9389 0.0000 0.0000 0.0000 72  TYR B O   
572  C CB  . TYR A 89  ? 0.9389 0.9389 0.9389 0.0000 0.0000 0.0000 72  TYR B CB  
573  C CG  . TYR A 89  ? 0.9389 0.9389 0.9389 0.0000 0.0000 0.0000 72  TYR B CG  
574  C CD1 . TYR A 89  ? 0.9389 0.9389 0.9389 0.0000 0.0000 0.0000 72  TYR B CD1 
575  C CD2 . TYR A 89  ? 0.9389 0.9389 0.9389 0.0000 0.0000 0.0000 72  TYR B CD2 
576  C CE1 . TYR A 89  ? 0.9389 0.9389 0.9389 0.0000 0.0000 0.0000 72  TYR B CE1 
577  C CE2 . TYR A 89  ? 0.9389 0.9389 0.9389 0.0000 0.0000 0.0000 72  TYR B CE2 
578  C CZ  . TYR A 89  ? 0.9389 0.9389 0.9389 0.0000 0.0000 0.0000 72  TYR B CZ  
579  O OH  . TYR A 89  ? 0.9389 0.9389 0.9389 0.0000 0.0000 0.0000 72  TYR B OH  
580  N N   . TYR A 90  ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 73  TYR B N   
581  C CA  . TYR A 90  ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 73  TYR B CA  
582  C C   . TYR A 90  ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 73  TYR B C   
583  O O   . TYR A 90  ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 73  TYR B O   
584  C CB  . TYR A 90  ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 73  TYR B CB  
585  C CG  . TYR A 90  ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 73  TYR B CG  
586  C CD1 . TYR A 90  ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 73  TYR B CD1 
587  C CD2 . TYR A 90  ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 73  TYR B CD2 
588  C CE1 . TYR A 90  ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 73  TYR B CE1 
589  C CE2 . TYR A 90  ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 73  TYR B CE2 
590  C CZ  . TYR A 90  ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 73  TYR B CZ  
591  O OH  . TYR A 90  ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 73  TYR B OH  
592  N N   . ASP A 91  ? 0.9683 0.9683 0.9683 0.0000 0.0000 0.0000 74  ASP B N   
593  C CA  . ASP A 91  ? 0.9683 0.9683 0.9683 0.0000 0.0000 0.0000 74  ASP B CA  
594  C C   . ASP A 91  ? 0.9683 0.9683 0.9683 0.0000 0.0000 0.0000 74  ASP B C   
595  O O   . ASP A 91  ? 0.9683 0.9683 0.9683 0.0000 0.0000 0.0000 74  ASP B O   
596  C CB  . ASP A 91  ? 0.9683 0.9683 0.9683 0.0000 0.0000 0.0000 74  ASP B CB  
597  C CG  . ASP A 91  ? 0.9683 0.9683 0.9683 0.0000 0.0000 0.0000 74  ASP B CG  
598  O OD1 . ASP A 91  ? 0.9683 0.9683 0.9683 0.0000 0.0000 0.0000 74  ASP B OD1 
599  O OD2 . ASP A 91  ? 0.9683 0.9683 0.9683 0.0000 0.0000 0.0000 74  ASP B OD2 
600  N N   . SER A 92  ? 0.9817 0.9817 0.9817 0.0000 0.0000 0.0000 75  SER B N   
601  C CA  . SER A 92  ? 0.9817 0.9817 0.9817 0.0000 0.0000 0.0000 75  SER B CA  
602  C C   . SER A 92  ? 0.9817 0.9817 0.9817 0.0000 0.0000 0.0000 75  SER B C   
603  O O   . SER A 92  ? 0.9817 0.9817 0.9817 0.0000 0.0000 0.0000 75  SER B O   
604  C CB  . SER A 92  ? 0.9817 0.9817 0.9817 0.0000 0.0000 0.0000 75  SER B CB  
605  O OG  . SER A 92  ? 0.9817 0.9817 0.9817 0.0000 0.0000 0.0000 75  SER B OG  
606  N N   . THR A 93  ? 0.9861 0.9861 0.9861 0.0000 0.0000 0.0000 76  THR B N   
607  C CA  . THR A 93  ? 0.9861 0.9861 0.9861 0.0000 0.0000 0.0000 76  THR B CA  
608  C C   . THR A 93  ? 0.9861 0.9861 0.9861 0.0000 0.0000 0.0000 76  THR B C   
609  O O   . THR A 93  ? 0.9861 0.9861 0.9861 0.0000 0.0000 0.0000 76  THR B O   
610  C CB  . THR A 93  ? 0.9861 0.9861 0.9861 0.0000 0.0000 0.0000 76  THR B CB  
611  O OG1 . THR A 93  ? 0.9861 0.9861 0.9861 0.0000 0.0000 0.0000 76  THR B OG1 
612  C CG2 . THR A 93  ? 0.9861 0.9861 0.9861 0.0000 0.0000 0.0000 76  THR B CG2 
613  N N   . TYR A 94  ? 0.9514 0.9514 0.9514 0.0000 0.0000 0.0000 77  TYR B N   
614  C CA  . TYR A 94  ? 0.9514 0.9514 0.9514 0.0000 0.0000 0.0000 77  TYR B CA  
615  C C   . TYR A 94  ? 0.9514 0.9514 0.9514 0.0000 0.0000 0.0000 77  TYR B C   
616  O O   . TYR A 94  ? 0.9514 0.9514 0.9514 0.0000 0.0000 0.0000 77  TYR B O   
617  C CB  . TYR A 94  ? 0.9514 0.9514 0.9514 0.0000 0.0000 0.0000 77  TYR B CB  
618  C CG  . TYR A 94  ? 0.9514 0.9514 0.9514 0.0000 0.0000 0.0000 77  TYR B CG  
619  C CD1 . TYR A 94  ? 0.9514 0.9514 0.9514 0.0000 0.0000 0.0000 77  TYR B CD1 
620  C CD2 . TYR A 94  ? 0.9514 0.9514 0.9514 0.0000 0.0000 0.0000 77  TYR B CD2 
621  C CE1 . TYR A 94  ? 0.9514 0.9514 0.9514 0.0000 0.0000 0.0000 77  TYR B CE1 
622  C CE2 . TYR A 94  ? 0.9514 0.9514 0.9514 0.0000 0.0000 0.0000 77  TYR B CE2 
623  C CZ  . TYR A 94  ? 0.9514 0.9514 0.9514 0.0000 0.0000 0.0000 77  TYR B CZ  
624  O OH  . TYR A 94  ? 0.9514 0.9514 0.9514 0.0000 0.0000 0.0000 77  TYR B OH  
625  N N   . LEU A 95  ? 0.9320 0.9320 0.9320 0.0000 0.0000 0.0000 78  LEU B N   
626  C CA  . LEU A 95  ? 0.9320 0.9320 0.9320 0.0000 0.0000 0.0000 78  LEU B CA  
627  C C   . LEU A 95  ? 0.9320 0.9320 0.9320 0.0000 0.0000 0.0000 78  LEU B C   
628  O O   . LEU A 95  ? 0.9320 0.9320 0.9320 0.0000 0.0000 0.0000 78  LEU B O   
629  C CB  . LEU A 95  ? 0.9320 0.9320 0.9320 0.0000 0.0000 0.0000 78  LEU B CB  
630  C CG  . LEU A 95  ? 0.9320 0.9320 0.9320 0.0000 0.0000 0.0000 78  LEU B CG  
631  C CD1 . LEU A 95  ? 0.9320 0.9320 0.9320 0.0000 0.0000 0.0000 78  LEU B CD1 
632  C CD2 . LEU A 95  ? 0.9320 0.9320 0.9320 0.0000 0.0000 0.0000 78  LEU B CD2 
633  N N   . SER A 96  ? 0.9897 0.9897 0.9897 0.0000 0.0000 0.0000 79  SER B N   
634  C CA  . SER A 96  ? 0.9897 0.9897 0.9897 0.0000 0.0000 0.0000 79  SER B CA  
635  C C   . SER A 96  ? 0.9897 0.9897 0.9897 0.0000 0.0000 0.0000 79  SER B C   
636  O O   . SER A 96  ? 0.9897 0.9897 0.9897 0.0000 0.0000 0.0000 79  SER B O   
637  C CB  . SER A 96  ? 0.9897 0.9897 0.9897 0.0000 0.0000 0.0000 79  SER B CB  
638  O OG  . SER A 96  ? 0.9897 0.9897 0.9897 0.0000 0.0000 0.0000 79  SER B OG  
639  N N   . THR A 97  ? 0.9960 0.9960 0.9960 0.0000 0.0000 0.0000 80  THR B N   
640  C CA  . THR A 97  ? 0.9960 0.9960 0.9960 0.0000 0.0000 0.0000 80  THR B CA  
641  C C   . THR A 97  ? 0.9960 0.9960 0.9960 0.0000 0.0000 0.0000 80  THR B C   
642  O O   . THR A 97  ? 0.9960 0.9960 0.9960 0.0000 0.0000 0.0000 80  THR B O   
643  C CB  . THR A 97  ? 0.9960 0.9960 0.9960 0.0000 0.0000 0.0000 80  THR B CB  
644  O OG1 . THR A 97  ? 0.9960 0.9960 0.9960 0.0000 0.0000 0.0000 80  THR B OG1 
645  C CG2 . THR A 97  ? 0.9960 0.9960 0.9960 0.0000 0.0000 0.0000 80  THR B CG2 
646  N N   . ASP A 98  ? 1.0063 1.0063 1.0063 0.0000 0.0000 0.0000 81  ASP B N   
647  C CA  . ASP A 98  ? 1.0063 1.0063 1.0063 0.0000 0.0000 0.0000 81  ASP B CA  
648  C C   . ASP A 98  ? 1.0063 1.0063 1.0063 0.0000 0.0000 0.0000 81  ASP B C   
649  O O   . ASP A 98  ? 1.0063 1.0063 1.0063 0.0000 0.0000 0.0000 81  ASP B O   
650  C CB  . ASP A 98  ? 1.0063 1.0063 1.0063 0.0000 0.0000 0.0000 81  ASP B CB  
651  C CG  . ASP A 98  ? 1.0063 1.0063 1.0063 0.0000 0.0000 0.0000 81  ASP B CG  
652  O OD1 . ASP A 98  ? 1.0063 1.0063 1.0063 0.0000 0.0000 0.0000 81  ASP B OD1 
653  O OD2 . ASP A 98  ? 1.0063 1.0063 1.0063 0.0000 0.0000 0.0000 81  ASP B OD2 
654  N N   . ASN A 99  ? 1.0048 1.0048 1.0048 0.0000 0.0000 0.0000 82  ASN B N   
655  C CA  . ASN A 99  ? 1.0048 1.0048 1.0048 0.0000 0.0000 0.0000 82  ASN B CA  
656  C C   . ASN A 99  ? 1.0048 1.0048 1.0048 0.0000 0.0000 0.0000 82  ASN B C   
657  O O   . ASN A 99  ? 1.0048 1.0048 1.0048 0.0000 0.0000 0.0000 82  ASN B O   
658  C CB  . ASN A 99  ? 1.0048 1.0048 1.0048 0.0000 0.0000 0.0000 82  ASN B CB  
659  C CG  . ASN A 99  ? 1.0048 1.0048 1.0048 0.0000 0.0000 0.0000 82  ASN B CG  
660  O OD1 . ASN A 99  ? 1.0048 1.0048 1.0048 0.0000 0.0000 0.0000 82  ASN B OD1 
661  N ND2 . ASN A 99  ? 1.0048 1.0048 1.0048 0.0000 0.0000 0.0000 82  ASN B ND2 
662  N N   . GLU A 100 ? 0.9744 0.9744 0.9744 0.0000 0.0000 0.0000 83  GLU B N   
663  C CA  . GLU A 100 ? 0.9744 0.9744 0.9744 0.0000 0.0000 0.0000 83  GLU B CA  
664  C C   . GLU A 100 ? 0.9744 0.9744 0.9744 0.0000 0.0000 0.0000 83  GLU B C   
665  O O   . GLU A 100 ? 0.9744 0.9744 0.9744 0.0000 0.0000 0.0000 83  GLU B O   
666  C CB  . GLU A 100 ? 0.9744 0.9744 0.9744 0.0000 0.0000 0.0000 83  GLU B CB  
667  C CG  . GLU A 100 ? 0.9744 0.9744 0.9744 0.0000 0.0000 0.0000 83  GLU B CG  
668  C CD  . GLU A 100 ? 0.9744 0.9744 0.9744 0.0000 0.0000 0.0000 83  GLU B CD  
669  O OE1 . GLU A 100 ? 0.9744 0.9744 0.9744 0.0000 0.0000 0.0000 83  GLU B OE1 
670  O OE2 . GLU A 100 ? 0.9744 0.9744 0.9744 0.0000 0.0000 0.0000 83  GLU B OE2 
671  N N   . LYS A 101 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 84  LYS B N   
672  C CA  . LYS A 101 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 84  LYS B CA  
673  C C   . LYS A 101 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 84  LYS B C   
674  O O   . LYS A 101 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 84  LYS B O   
675  C CB  . LYS A 101 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 84  LYS B CB  
676  C CG  . LYS A 101 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 84  LYS B CG  
677  C CD  . LYS A 101 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 84  LYS B CD  
678  C CE  . LYS A 101 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 84  LYS B CE  
679  N NZ  . LYS A 101 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 84  LYS B NZ  
680  N N   . ASP A 102 ? 0.9530 0.9530 0.9530 0.0000 0.0000 0.0000 85  ASP B N   
681  C CA  . ASP A 102 ? 0.9530 0.9530 0.9530 0.0000 0.0000 0.0000 85  ASP B CA  
682  C C   . ASP A 102 ? 0.9530 0.9530 0.9530 0.0000 0.0000 0.0000 85  ASP B C   
683  O O   . ASP A 102 ? 0.9530 0.9530 0.9530 0.0000 0.0000 0.0000 85  ASP B O   
684  C CB  . ASP A 102 ? 0.9530 0.9530 0.9530 0.0000 0.0000 0.0000 85  ASP B CB  
685  C CG  . ASP A 102 ? 0.9530 0.9530 0.9530 0.0000 0.0000 0.0000 85  ASP B CG  
686  O OD1 . ASP A 102 ? 0.9530 0.9530 0.9530 0.0000 0.0000 0.0000 85  ASP B OD1 
687  O OD2 . ASP A 102 ? 0.9530 0.9530 0.9530 0.0000 0.0000 0.0000 85  ASP B OD2 
688  N N   . ASN A 103 ? 0.9117 0.9117 0.9117 0.0000 0.0000 0.0000 86  ASN B N   
689  C CA  . ASN A 103 ? 0.9117 0.9117 0.9117 0.0000 0.0000 0.0000 86  ASN B CA  
690  C C   . ASN A 103 ? 0.9117 0.9117 0.9117 0.0000 0.0000 0.0000 86  ASN B C   
691  O O   . ASN A 103 ? 0.9117 0.9117 0.9117 0.0000 0.0000 0.0000 86  ASN B O   
692  C CB  . ASN A 103 ? 0.9117 0.9117 0.9117 0.0000 0.0000 0.0000 86  ASN B CB  
693  C CG  . ASN A 103 ? 0.9117 0.9117 0.9117 0.0000 0.0000 0.0000 86  ASN B CG  
694  O OD1 . ASN A 103 ? 0.9117 0.9117 0.9117 0.0000 0.0000 0.0000 86  ASN B OD1 
695  N ND2 . ASN A 103 ? 0.9117 0.9117 0.9117 0.0000 0.0000 0.0000 86  ASN B ND2 
696  N N   . TYR A 104 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 87  TYR B N   
697  C CA  . TYR A 104 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 87  TYR B CA  
698  C C   . TYR A 104 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 87  TYR B C   
699  O O   . TYR A 104 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 87  TYR B O   
700  C CB  . TYR A 104 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 87  TYR B CB  
701  C CG  . TYR A 104 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 87  TYR B CG  
702  C CD1 . TYR A 104 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 87  TYR B CD1 
703  C CD2 . TYR A 104 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 87  TYR B CD2 
704  C CE1 . TYR A 104 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 87  TYR B CE1 
705  C CE2 . TYR A 104 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 87  TYR B CE2 
706  C CZ  . TYR A 104 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 87  TYR B CZ  
707  O OH  . TYR A 104 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 87  TYR B OH  
708  N N   . LEU A 105 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 88  LEU B N   
709  C CA  . LEU A 105 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 88  LEU B CA  
710  C C   . LEU A 105 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 88  LEU B C   
711  O O   . LEU A 105 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 88  LEU B O   
712  C CB  . LEU A 105 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 88  LEU B CB  
713  C CG  . LEU A 105 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 88  LEU B CG  
714  C CD1 . LEU A 105 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 88  LEU B CD1 
715  C CD2 . LEU A 105 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 88  LEU B CD2 
716  N N   . LYS A 106 ? 0.8963 0.8963 0.8963 0.0000 0.0000 0.0000 89  LYS B N   
717  C CA  . LYS A 106 ? 0.8963 0.8963 0.8963 0.0000 0.0000 0.0000 89  LYS B CA  
718  C C   . LYS A 106 ? 0.8963 0.8963 0.8963 0.0000 0.0000 0.0000 89  LYS B C   
719  O O   . LYS A 106 ? 0.8963 0.8963 0.8963 0.0000 0.0000 0.0000 89  LYS B O   
720  C CB  . LYS A 106 ? 0.8963 0.8963 0.8963 0.0000 0.0000 0.0000 89  LYS B CB  
721  C CG  . LYS A 106 ? 0.8963 0.8963 0.8963 0.0000 0.0000 0.0000 89  LYS B CG  
722  C CD  . LYS A 106 ? 0.8963 0.8963 0.8963 0.0000 0.0000 0.0000 89  LYS B CD  
723  C CE  . LYS A 106 ? 0.8963 0.8963 0.8963 0.0000 0.0000 0.0000 89  LYS B CE  
724  N NZ  . LYS A 106 ? 0.8963 0.8963 0.8963 0.0000 0.0000 0.0000 89  LYS B NZ  
725  N N   . GLY A 107 ? 0.9297 0.9297 0.9297 0.0000 0.0000 0.0000 90  GLY B N   
726  C CA  . GLY A 107 ? 0.9297 0.9297 0.9297 0.0000 0.0000 0.0000 90  GLY B CA  
727  C C   . GLY A 107 ? 0.9297 0.9297 0.9297 0.0000 0.0000 0.0000 90  GLY B C   
728  O O   . GLY A 107 ? 0.9297 0.9297 0.9297 0.0000 0.0000 0.0000 90  GLY B O   
729  N N   . VAL A 108 ? 0.8822 0.8822 0.8822 0.0000 0.0000 0.0000 91  VAL B N   
730  C CA  . VAL A 108 ? 0.8822 0.8822 0.8822 0.0000 0.0000 0.0000 91  VAL B CA  
731  C C   . VAL A 108 ? 0.8822 0.8822 0.8822 0.0000 0.0000 0.0000 91  VAL B C   
732  O O   . VAL A 108 ? 0.8822 0.8822 0.8822 0.0000 0.0000 0.0000 91  VAL B O   
733  C CB  . VAL A 108 ? 0.8822 0.8822 0.8822 0.0000 0.0000 0.0000 91  VAL B CB  
734  C CG1 . VAL A 108 ? 0.8822 0.8822 0.8822 0.0000 0.0000 0.0000 91  VAL B CG1 
735  C CG2 . VAL A 108 ? 0.8822 0.8822 0.8822 0.0000 0.0000 0.0000 91  VAL B CG2 
736  N N   . THR A 109 ? 0.8851 0.8851 0.8851 0.0000 0.0000 0.0000 92  THR B N   
737  C CA  . THR A 109 ? 0.8851 0.8851 0.8851 0.0000 0.0000 0.0000 92  THR B CA  
738  C C   . THR A 109 ? 0.8851 0.8851 0.8851 0.0000 0.0000 0.0000 92  THR B C   
739  O O   . THR A 109 ? 0.8851 0.8851 0.8851 0.0000 0.0000 0.0000 92  THR B O   
740  C CB  . THR A 109 ? 0.8851 0.8851 0.8851 0.0000 0.0000 0.0000 92  THR B CB  
741  O OG1 . THR A 109 ? 0.8851 0.8851 0.8851 0.0000 0.0000 0.0000 92  THR B OG1 
742  C CG2 . THR A 109 ? 0.8851 0.8851 0.8851 0.0000 0.0000 0.0000 92  THR B CG2 
743  N N   . LYS A 110 ? 0.8945 0.8945 0.8945 0.0000 0.0000 0.0000 93  LYS B N   
744  C CA  . LYS A 110 ? 0.8945 0.8945 0.8945 0.0000 0.0000 0.0000 93  LYS B CA  
745  C C   . LYS A 110 ? 0.8945 0.8945 0.8945 0.0000 0.0000 0.0000 93  LYS B C   
746  O O   . LYS A 110 ? 0.8945 0.8945 0.8945 0.0000 0.0000 0.0000 93  LYS B O   
747  C CB  . LYS A 110 ? 0.8945 0.8945 0.8945 0.0000 0.0000 0.0000 93  LYS B CB  
748  C CG  . LYS A 110 ? 0.8945 0.8945 0.8945 0.0000 0.0000 0.0000 93  LYS B CG  
749  C CD  . LYS A 110 ? 0.8945 0.8945 0.8945 0.0000 0.0000 0.0000 93  LYS B CD  
750  C CE  . LYS A 110 ? 0.8945 0.8945 0.8945 0.0000 0.0000 0.0000 93  LYS B CE  
751  N NZ  . LYS A 110 ? 0.8945 0.8945 0.8945 0.0000 0.0000 0.0000 93  LYS B NZ  
752  N N   . LEU A 111 ? 0.8978 0.8978 0.8978 0.0000 0.0000 0.0000 94  LEU B N   
753  C CA  . LEU A 111 ? 0.8978 0.8978 0.8978 0.0000 0.0000 0.0000 94  LEU B CA  
754  C C   . LEU A 111 ? 0.8978 0.8978 0.8978 0.0000 0.0000 0.0000 94  LEU B C   
755  O O   . LEU A 111 ? 0.8978 0.8978 0.8978 0.0000 0.0000 0.0000 94  LEU B O   
756  C CB  . LEU A 111 ? 0.8978 0.8978 0.8978 0.0000 0.0000 0.0000 94  LEU B CB  
757  C CG  . LEU A 111 ? 0.8978 0.8978 0.8978 0.0000 0.0000 0.0000 94  LEU B CG  
758  C CD1 . LEU A 111 ? 0.8978 0.8978 0.8978 0.0000 0.0000 0.0000 94  LEU B CD1 
759  C CD2 . LEU A 111 ? 0.8978 0.8978 0.8978 0.0000 0.0000 0.0000 94  LEU B CD2 
760  N N   . PHE A 112 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 95  PHE B N   
761  C CA  . PHE A 112 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 95  PHE B CA  
762  C C   . PHE A 112 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 95  PHE B C   
763  O O   . PHE A 112 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 95  PHE B O   
764  C CB  . PHE A 112 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 95  PHE B CB  
765  C CG  . PHE A 112 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 95  PHE B CG  
766  C CD1 . PHE A 112 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 95  PHE B CD1 
767  C CD2 . PHE A 112 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 95  PHE B CD2 
768  C CE1 . PHE A 112 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 95  PHE B CE1 
769  C CE2 . PHE A 112 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 95  PHE B CE2 
770  C CZ  . PHE A 112 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 95  PHE B CZ  
771  N N   . GLU A 113 ? 0.9261 0.9261 0.9261 0.0000 0.0000 0.0000 96  GLU B N   
772  C CA  . GLU A 113 ? 0.9261 0.9261 0.9261 0.0000 0.0000 0.0000 96  GLU B CA  
773  C C   . GLU A 113 ? 0.9261 0.9261 0.9261 0.0000 0.0000 0.0000 96  GLU B C   
774  O O   . GLU A 113 ? 0.9261 0.9261 0.9261 0.0000 0.0000 0.0000 96  GLU B O   
775  C CB  . GLU A 113 ? 0.9261 0.9261 0.9261 0.0000 0.0000 0.0000 96  GLU B CB  
776  C CG  . GLU A 113 ? 0.9261 0.9261 0.9261 0.0000 0.0000 0.0000 96  GLU B CG  
777  C CD  . GLU A 113 ? 0.9261 0.9261 0.9261 0.0000 0.0000 0.0000 96  GLU B CD  
778  O OE1 . GLU A 113 ? 0.9261 0.9261 0.9261 0.0000 0.0000 0.0000 96  GLU B OE1 
779  O OE2 . GLU A 113 ? 0.9261 0.9261 0.9261 0.0000 0.0000 0.0000 96  GLU B OE2 
780  N N   . ARG A 114 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 97  ARG B N   
781  C CA  . ARG A 114 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 97  ARG B CA  
782  C C   . ARG A 114 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 97  ARG B C   
783  O O   . ARG A 114 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 97  ARG B O   
784  C CB  . ARG A 114 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 97  ARG B CB  
785  C CG  . ARG A 114 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 97  ARG B CG  
786  C CD  . ARG A 114 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 97  ARG B CD  
787  N NE  . ARG A 114 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 97  ARG B NE  
788  C CZ  . ARG A 114 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 97  ARG B CZ  
789  N NH1 . ARG A 114 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 97  ARG B NH1 
790  N NH2 . ARG A 114 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 97  ARG B NH2 
791  N N   . ILE A 115 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 98  ILE B N   
792  C CA  . ILE A 115 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 98  ILE B CA  
793  C C   . ILE A 115 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 98  ILE B C   
794  O O   . ILE A 115 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 98  ILE B O   
795  C CB  . ILE A 115 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 98  ILE B CB  
796  C CG1 . ILE A 115 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 98  ILE B CG1 
797  C CG2 . ILE A 115 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 98  ILE B CG2 
798  C CD1 . ILE A 115 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 98  ILE B CD1 
799  N N   . TYR A 116 ? 0.8875 0.8875 0.8875 0.0000 0.0000 0.0000 99  TYR B N   
800  C CA  . TYR A 116 ? 0.8875 0.8875 0.8875 0.0000 0.0000 0.0000 99  TYR B CA  
801  C C   . TYR A 116 ? 0.8875 0.8875 0.8875 0.0000 0.0000 0.0000 99  TYR B C   
802  O O   . TYR A 116 ? 0.8875 0.8875 0.8875 0.0000 0.0000 0.0000 99  TYR B O   
803  C CB  . TYR A 116 ? 0.8875 0.8875 0.8875 0.0000 0.0000 0.0000 99  TYR B CB  
804  C CG  . TYR A 116 ? 0.8875 0.8875 0.8875 0.0000 0.0000 0.0000 99  TYR B CG  
805  C CD1 . TYR A 116 ? 0.8875 0.8875 0.8875 0.0000 0.0000 0.0000 99  TYR B CD1 
806  C CD2 . TYR A 116 ? 0.8875 0.8875 0.8875 0.0000 0.0000 0.0000 99  TYR B CD2 
807  C CE1 . TYR A 116 ? 0.8875 0.8875 0.8875 0.0000 0.0000 0.0000 99  TYR B CE1 
808  C CE2 . TYR A 116 ? 0.8875 0.8875 0.8875 0.0000 0.0000 0.0000 99  TYR B CE2 
809  C CZ  . TYR A 116 ? 0.8875 0.8875 0.8875 0.0000 0.0000 0.0000 99  TYR B CZ  
810  O OH  . TYR A 116 ? 0.8875 0.8875 0.8875 0.0000 0.0000 0.0000 99  TYR B OH  
811  N N   . SER A 117 ? 0.9063 0.9063 0.9063 0.0000 0.0000 0.0000 100 SER B N   
812  C CA  . SER A 117 ? 0.9063 0.9063 0.9063 0.0000 0.0000 0.0000 100 SER B CA  
813  C C   . SER A 117 ? 0.9063 0.9063 0.9063 0.0000 0.0000 0.0000 100 SER B C   
814  O O   . SER A 117 ? 0.9063 0.9063 0.9063 0.0000 0.0000 0.0000 100 SER B O   
815  C CB  . SER A 117 ? 0.9063 0.9063 0.9063 0.0000 0.0000 0.0000 100 SER B CB  
816  O OG  . SER A 117 ? 0.9063 0.9063 0.9063 0.0000 0.0000 0.0000 100 SER B OG  
817  N N   . THR A 118 ? 0.9574 0.9574 0.9574 0.0000 0.0000 0.0000 101 THR B N   
818  C CA  . THR A 118 ? 0.9574 0.9574 0.9574 0.0000 0.0000 0.0000 101 THR B CA  
819  C C   . THR A 118 ? 0.9574 0.9574 0.9574 0.0000 0.0000 0.0000 101 THR B C   
820  O O   . THR A 118 ? 0.9574 0.9574 0.9574 0.0000 0.0000 0.0000 101 THR B O   
821  C CB  . THR A 118 ? 0.9574 0.9574 0.9574 0.0000 0.0000 0.0000 101 THR B CB  
822  O OG1 . THR A 118 ? 0.9574 0.9574 0.9574 0.0000 0.0000 0.0000 101 THR B OG1 
823  C CG2 . THR A 118 ? 0.9574 0.9574 0.9574 0.0000 0.0000 0.0000 101 THR B CG2 
824  N N   . ASP A 119 ? 1.0183 1.0183 1.0183 0.0000 0.0000 0.0000 102 ASP B N   
825  C CA  . ASP A 119 ? 1.0183 1.0183 1.0183 0.0000 0.0000 0.0000 102 ASP B CA  
826  C C   . ASP A 119 ? 1.0183 1.0183 1.0183 0.0000 0.0000 0.0000 102 ASP B C   
827  O O   . ASP A 119 ? 1.0183 1.0183 1.0183 0.0000 0.0000 0.0000 102 ASP B O   
828  C CB  . ASP A 119 ? 1.0183 1.0183 1.0183 0.0000 0.0000 0.0000 102 ASP B CB  
829  C CG  . ASP A 119 ? 1.0183 1.0183 1.0183 0.0000 0.0000 0.0000 102 ASP B CG  
830  O OD1 . ASP A 119 ? 1.0183 1.0183 1.0183 0.0000 0.0000 0.0000 102 ASP B OD1 
831  O OD2 . ASP A 119 ? 1.0183 1.0183 1.0183 0.0000 0.0000 0.0000 102 ASP B OD2 
832  N N   . LEU A 120 ? 0.9374 0.9374 0.9374 0.0000 0.0000 0.0000 103 LEU B N   
833  C CA  . LEU A 120 ? 0.9374 0.9374 0.9374 0.0000 0.0000 0.0000 103 LEU B CA  
834  C C   . LEU A 120 ? 0.9374 0.9374 0.9374 0.0000 0.0000 0.0000 103 LEU B C   
835  O O   . LEU A 120 ? 0.9374 0.9374 0.9374 0.0000 0.0000 0.0000 103 LEU B O   
836  C CB  . LEU A 120 ? 0.9374 0.9374 0.9374 0.0000 0.0000 0.0000 103 LEU B CB  
837  C CG  . LEU A 120 ? 0.9374 0.9374 0.9374 0.0000 0.0000 0.0000 103 LEU B CG  
838  C CD1 . LEU A 120 ? 0.9374 0.9374 0.9374 0.0000 0.0000 0.0000 103 LEU B CD1 
839  C CD2 . LEU A 120 ? 0.9374 0.9374 0.9374 0.0000 0.0000 0.0000 103 LEU B CD2 
840  N N   . GLY A 121 ? 0.9210 0.9210 0.9210 0.0000 0.0000 0.0000 104 GLY B N   
841  C CA  . GLY A 121 ? 0.9210 0.9210 0.9210 0.0000 0.0000 0.0000 104 GLY B CA  
842  C C   . GLY A 121 ? 0.9210 0.9210 0.9210 0.0000 0.0000 0.0000 104 GLY B C   
843  O O   . GLY A 121 ? 0.9210 0.9210 0.9210 0.0000 0.0000 0.0000 104 GLY B O   
844  N N   . ARG A 122 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 105 ARG B N   
845  C CA  . ARG A 122 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 105 ARG B CA  
846  C C   . ARG A 122 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 105 ARG B C   
847  O O   . ARG A 122 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 105 ARG B O   
848  C CB  . ARG A 122 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 105 ARG B CB  
849  C CG  . ARG A 122 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 105 ARG B CG  
850  C CD  . ARG A 122 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 105 ARG B CD  
851  N NE  . ARG A 122 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 105 ARG B NE  
852  C CZ  . ARG A 122 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 105 ARG B CZ  
853  N NH1 . ARG A 122 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 105 ARG B NH1 
854  N NH2 . ARG A 122 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 105 ARG B NH2 
855  N N   . MET A 123 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 106 MET B N   
856  C CA  . MET A 123 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 106 MET B CA  
857  C C   . MET A 123 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 106 MET B C   
858  O O   . MET A 123 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 106 MET B O   
859  C CB  . MET A 123 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 106 MET B CB  
860  C CG  . MET A 123 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 106 MET B CG  
861  S SD  . MET A 123 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 106 MET B SD  
862  C CE  . MET A 123 ? 0.9566 0.9566 0.9566 0.0000 0.0000 0.0000 106 MET B CE  
863  N N   . LEU A 124 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 107 LEU B N   
864  C CA  . LEU A 124 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 107 LEU B CA  
865  C C   . LEU A 124 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 107 LEU B C   
866  O O   . LEU A 124 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 107 LEU B O   
867  C CB  . LEU A 124 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 107 LEU B CB  
868  C CG  . LEU A 124 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 107 LEU B CG  
869  C CD1 . LEU A 124 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 107 LEU B CD1 
870  C CD2 . LEU A 124 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 107 LEU B CD2 
871  N N   . LEU A 125 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 108 LEU B N   
872  C CA  . LEU A 125 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 108 LEU B CA  
873  C C   . LEU A 125 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 108 LEU B C   
874  O O   . LEU A 125 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 108 LEU B O   
875  C CB  . LEU A 125 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 108 LEU B CB  
876  C CG  . LEU A 125 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 108 LEU B CG  
877  C CD1 . LEU A 125 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 108 LEU B CD1 
878  C CD2 . LEU A 125 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 108 LEU B CD2 
879  N N   . THR A 126 ? 0.8999 0.8999 0.8999 0.0000 0.0000 0.0000 109 THR B N   
880  C CA  . THR A 126 ? 0.8999 0.8999 0.8999 0.0000 0.0000 0.0000 109 THR B CA  
881  C C   . THR A 126 ? 0.8999 0.8999 0.8999 0.0000 0.0000 0.0000 109 THR B C   
882  O O   . THR A 126 ? 0.8999 0.8999 0.8999 0.0000 0.0000 0.0000 109 THR B O   
883  C CB  . THR A 126 ? 0.8999 0.8999 0.8999 0.0000 0.0000 0.0000 109 THR B CB  
884  O OG1 . THR A 126 ? 0.8999 0.8999 0.8999 0.0000 0.0000 0.0000 109 THR B OG1 
885  C CG2 . THR A 126 ? 0.8999 0.8999 0.8999 0.0000 0.0000 0.0000 109 THR B CG2 
886  N N   . SER A 127 ? 0.8856 0.8856 0.8856 0.0000 0.0000 0.0000 110 SER B N   
887  C CA  . SER A 127 ? 0.8856 0.8856 0.8856 0.0000 0.0000 0.0000 110 SER B CA  
888  C C   . SER A 127 ? 0.8856 0.8856 0.8856 0.0000 0.0000 0.0000 110 SER B C   
889  O O   . SER A 127 ? 0.8856 0.8856 0.8856 0.0000 0.0000 0.0000 110 SER B O   
890  C CB  . SER A 127 ? 0.8856 0.8856 0.8856 0.0000 0.0000 0.0000 110 SER B CB  
891  O OG  . SER A 127 ? 0.8856 0.8856 0.8856 0.0000 0.0000 0.0000 110 SER B OG  
892  N N   . ILE A 128 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 111 ILE B N   
893  C CA  . ILE A 128 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 111 ILE B CA  
894  C C   . ILE A 128 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 111 ILE B C   
895  O O   . ILE A 128 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 111 ILE B O   
896  C CB  . ILE A 128 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 111 ILE B CB  
897  C CG1 . ILE A 128 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 111 ILE B CG1 
898  C CG2 . ILE A 128 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 111 ILE B CG2 
899  C CD1 . ILE A 128 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 111 ILE B CD1 
900  N N   . VAL A 129 ? 0.8837 0.8837 0.8837 0.0000 0.0000 0.0000 112 VAL B N   
901  C CA  . VAL A 129 ? 0.8837 0.8837 0.8837 0.0000 0.0000 0.0000 112 VAL B CA  
902  C C   . VAL A 129 ? 0.8837 0.8837 0.8837 0.0000 0.0000 0.0000 112 VAL B C   
903  O O   . VAL A 129 ? 0.8837 0.8837 0.8837 0.0000 0.0000 0.0000 112 VAL B O   
904  C CB  . VAL A 129 ? 0.8837 0.8837 0.8837 0.0000 0.0000 0.0000 112 VAL B CB  
905  C CG1 . VAL A 129 ? 0.8837 0.8837 0.8837 0.0000 0.0000 0.0000 112 VAL B CG1 
906  C CG2 . VAL A 129 ? 0.8837 0.8837 0.8837 0.0000 0.0000 0.0000 112 VAL B CG2 
907  N N   . ARG A 130 ? 0.9547 0.9547 0.9547 0.0000 0.0000 0.0000 113 ARG B N   
908  C CA  . ARG A 130 ? 0.9547 0.9547 0.9547 0.0000 0.0000 0.0000 113 ARG B CA  
909  C C   . ARG A 130 ? 0.9547 0.9547 0.9547 0.0000 0.0000 0.0000 113 ARG B C   
910  O O   . ARG A 130 ? 0.9547 0.9547 0.9547 0.0000 0.0000 0.0000 113 ARG B O   
911  C CB  . ARG A 130 ? 0.9547 0.9547 0.9547 0.0000 0.0000 0.0000 113 ARG B CB  
912  C CG  . ARG A 130 ? 0.9547 0.9547 0.9547 0.0000 0.0000 0.0000 113 ARG B CG  
913  C CD  . ARG A 130 ? 0.9547 0.9547 0.9547 0.0000 0.0000 0.0000 113 ARG B CD  
914  N NE  . ARG A 130 ? 0.9547 0.9547 0.9547 0.0000 0.0000 0.0000 113 ARG B NE  
915  C CZ  . ARG A 130 ? 0.9547 0.9547 0.9547 0.0000 0.0000 0.0000 113 ARG B CZ  
916  N NH1 . ARG A 130 ? 0.9547 0.9547 0.9547 0.0000 0.0000 0.0000 113 ARG B NH1 
917  N NH2 . ARG A 130 ? 0.9547 0.9547 0.9547 0.0000 0.0000 0.0000 113 ARG B NH2 
918  N N   . GLY A 131 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 114 GLY B N   
919  C CA  . GLY A 131 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 114 GLY B CA  
920  C C   . GLY A 131 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 114 GLY B C   
921  O O   . GLY A 131 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 114 GLY B O   
922  N N   . ILE A 132 ? 0.8834 0.8834 0.8834 0.0000 0.0000 0.0000 115 ILE B N   
923  C CA  . ILE A 132 ? 0.8834 0.8834 0.8834 0.0000 0.0000 0.0000 115 ILE B CA  
924  C C   . ILE A 132 ? 0.8834 0.8834 0.8834 0.0000 0.0000 0.0000 115 ILE B C   
925  O O   . ILE A 132 ? 0.8834 0.8834 0.8834 0.0000 0.0000 0.0000 115 ILE B O   
926  C CB  . ILE A 132 ? 0.8834 0.8834 0.8834 0.0000 0.0000 0.0000 115 ILE B CB  
927  C CG1 . ILE A 132 ? 0.8834 0.8834 0.8834 0.0000 0.0000 0.0000 115 ILE B CG1 
928  C CG2 . ILE A 132 ? 0.8834 0.8834 0.8834 0.0000 0.0000 0.0000 115 ILE B CG2 
929  C CD1 . ILE A 132 ? 0.8834 0.8834 0.8834 0.0000 0.0000 0.0000 115 ILE B CD1 
930  N N   . PRO A 133 ? 0.8938 0.8938 0.8938 0.0000 0.0000 0.0000 116 PRO B N   
931  C CA  . PRO A 133 ? 0.8938 0.8938 0.8938 0.0000 0.0000 0.0000 116 PRO B CA  
932  C C   . PRO A 133 ? 0.8938 0.8938 0.8938 0.0000 0.0000 0.0000 116 PRO B C   
933  O O   . PRO A 133 ? 0.8938 0.8938 0.8938 0.0000 0.0000 0.0000 116 PRO B O   
934  C CB  . PRO A 133 ? 0.8938 0.8938 0.8938 0.0000 0.0000 0.0000 116 PRO B CB  
935  C CG  . PRO A 133 ? 0.8938 0.8938 0.8938 0.0000 0.0000 0.0000 116 PRO B CG  
936  C CD  . PRO A 133 ? 0.8938 0.8938 0.8938 0.0000 0.0000 0.0000 116 PRO B CD  
937  N N   . PHE A 134 ? 0.9932 0.9932 0.9932 0.0000 0.0000 0.0000 117 PHE B N   
938  C CA  . PHE A 134 ? 0.9932 0.9932 0.9932 0.0000 0.0000 0.0000 117 PHE B CA  
939  C C   . PHE A 134 ? 0.9932 0.9932 0.9932 0.0000 0.0000 0.0000 117 PHE B C   
940  O O   . PHE A 134 ? 0.9932 0.9932 0.9932 0.0000 0.0000 0.0000 117 PHE B O   
941  C CB  . PHE A 134 ? 0.9932 0.9932 0.9932 0.0000 0.0000 0.0000 117 PHE B CB  
942  C CG  . PHE A 134 ? 0.9932 0.9932 0.9932 0.0000 0.0000 0.0000 117 PHE B CG  
943  C CD1 . PHE A 134 ? 0.9932 0.9932 0.9932 0.0000 0.0000 0.0000 117 PHE B CD1 
944  C CD2 . PHE A 134 ? 0.9932 0.9932 0.9932 0.0000 0.0000 0.0000 117 PHE B CD2 
945  C CE1 . PHE A 134 ? 0.9932 0.9932 0.9932 0.0000 0.0000 0.0000 117 PHE B CE1 
946  C CE2 . PHE A 134 ? 0.9932 0.9932 0.9932 0.0000 0.0000 0.0000 117 PHE B CE2 
947  C CZ  . PHE A 134 ? 0.9932 0.9932 0.9932 0.0000 0.0000 0.0000 117 PHE B CZ  
948  N N   . TRP A 135 ? 1.1092 1.1092 1.1092 0.0000 0.0000 0.0000 118 TRP B N   
949  C CA  . TRP A 135 ? 1.1092 1.1092 1.1092 0.0000 0.0000 0.0000 118 TRP B CA  
950  C C   . TRP A 135 ? 1.1092 1.1092 1.1092 0.0000 0.0000 0.0000 118 TRP B C   
951  O O   . TRP A 135 ? 1.1092 1.1092 1.1092 0.0000 0.0000 0.0000 118 TRP B O   
952  C CB  . TRP A 135 ? 1.1092 1.1092 1.1092 0.0000 0.0000 0.0000 118 TRP B CB  
953  C CG  . TRP A 135 ? 1.1092 1.1092 1.1092 0.0000 0.0000 0.0000 118 TRP B CG  
954  C CD1 . TRP A 135 ? 1.1092 1.1092 1.1092 0.0000 0.0000 0.0000 118 TRP B CD1 
955  C CD2 . TRP A 135 ? 1.1092 1.1092 1.1092 0.0000 0.0000 0.0000 118 TRP B CD2 
956  N NE1 . TRP A 135 ? 1.1092 1.1092 1.1092 0.0000 0.0000 0.0000 118 TRP B NE1 
957  C CE2 . TRP A 135 ? 1.1092 1.1092 1.1092 0.0000 0.0000 0.0000 118 TRP B CE2 
958  C CE3 . TRP A 135 ? 1.1092 1.1092 1.1092 0.0000 0.0000 0.0000 118 TRP B CE3 
959  C CZ2 . TRP A 135 ? 1.1092 1.1092 1.1092 0.0000 0.0000 0.0000 118 TRP B CZ2 
960  C CZ3 . TRP A 135 ? 1.1092 1.1092 1.1092 0.0000 0.0000 0.0000 118 TRP B CZ3 
961  C CH2 . TRP A 135 ? 1.1092 1.1092 1.1092 0.0000 0.0000 0.0000 118 TRP B CH2 
962  N N   . GLY A 136 ? 1.1561 1.1561 1.1561 0.0000 0.0000 0.0000 119 GLY B N   
963  C CA  . GLY A 136 ? 1.1561 1.1561 1.1561 0.0000 0.0000 0.0000 119 GLY B CA  
964  C C   . GLY A 136 ? 1.1561 1.1561 1.1561 0.0000 0.0000 0.0000 119 GLY B C   
965  O O   . GLY A 136 ? 1.1561 1.1561 1.1561 0.0000 0.0000 0.0000 119 GLY B O   
966  N N   . GLY A 137 ? 1.2495 1.2495 1.2495 0.0000 0.0000 0.0000 120 GLY B N   
967  C CA  . GLY A 137 ? 1.2495 1.2495 1.2495 0.0000 0.0000 0.0000 120 GLY B CA  
968  C C   . GLY A 137 ? 1.2495 1.2495 1.2495 0.0000 0.0000 0.0000 120 GLY B C   
969  O O   . GLY A 137 ? 1.2495 1.2495 1.2495 0.0000 0.0000 0.0000 120 GLY B O   
970  N N   . SER A 138 ? 1.3357 1.3357 1.3357 0.0000 0.0000 0.0000 121 SER B N   
971  C CA  . SER A 138 ? 1.3357 1.3357 1.3357 0.0000 0.0000 0.0000 121 SER B CA  
972  C C   . SER A 138 ? 1.3357 1.3357 1.3357 0.0000 0.0000 0.0000 121 SER B C   
973  O O   . SER A 138 ? 1.3357 1.3357 1.3357 0.0000 0.0000 0.0000 121 SER B O   
974  C CB  . SER A 138 ? 1.3357 1.3357 1.3357 0.0000 0.0000 0.0000 121 SER B CB  
975  O OG  . SER A 138 ? 1.3357 1.3357 1.3357 0.0000 0.0000 0.0000 121 SER B OG  
976  N N   . THR A 139 ? 1.4197 1.4197 1.4197 0.0000 0.0000 0.0000 122 THR B N   
977  C CA  . THR A 139 ? 1.4197 1.4197 1.4197 0.0000 0.0000 0.0000 122 THR B CA  
978  C C   . THR A 139 ? 1.4197 1.4197 1.4197 0.0000 0.0000 0.0000 122 THR B C   
979  O O   . THR A 139 ? 1.4197 1.4197 1.4197 0.0000 0.0000 0.0000 122 THR B O   
980  C CB  . THR A 139 ? 1.4197 1.4197 1.4197 0.0000 0.0000 0.0000 122 THR B CB  
981  O OG1 . THR A 139 ? 1.4197 1.4197 1.4197 0.0000 0.0000 0.0000 122 THR B OG1 
982  C CG2 . THR A 139 ? 1.4197 1.4197 1.4197 0.0000 0.0000 0.0000 122 THR B CG2 
983  N N   . ILE A 140 ? 1.3886 1.3886 1.3886 0.0000 0.0000 0.0000 123 ILE B N   
984  C CA  . ILE A 140 ? 1.3886 1.3886 1.3886 0.0000 0.0000 0.0000 123 ILE B CA  
985  C C   . ILE A 140 ? 1.3886 1.3886 1.3886 0.0000 0.0000 0.0000 123 ILE B C   
986  O O   . ILE A 140 ? 1.3886 1.3886 1.3886 0.0000 0.0000 0.0000 123 ILE B O   
987  C CB  . ILE A 140 ? 1.3886 1.3886 1.3886 0.0000 0.0000 0.0000 123 ILE B CB  
988  C CG1 . ILE A 140 ? 1.3886 1.3886 1.3886 0.0000 0.0000 0.0000 123 ILE B CG1 
989  C CG2 . ILE A 140 ? 1.3886 1.3886 1.3886 0.0000 0.0000 0.0000 123 ILE B CG2 
990  C CD1 . ILE A 140 ? 1.3886 1.3886 1.3886 0.0000 0.0000 0.0000 123 ILE B CD1 
991  N N   . ASP A 141 ? 1.3637 1.3637 1.3637 0.0000 0.0000 0.0000 124 ASP B N   
992  C CA  . ASP A 141 ? 1.3637 1.3637 1.3637 0.0000 0.0000 0.0000 124 ASP B CA  
993  C C   . ASP A 141 ? 1.3637 1.3637 1.3637 0.0000 0.0000 0.0000 124 ASP B C   
994  O O   . ASP A 141 ? 1.3637 1.3637 1.3637 0.0000 0.0000 0.0000 124 ASP B O   
995  C CB  . ASP A 141 ? 1.3637 1.3637 1.3637 0.0000 0.0000 0.0000 124 ASP B CB  
996  C CG  . ASP A 141 ? 1.3637 1.3637 1.3637 0.0000 0.0000 0.0000 124 ASP B CG  
997  O OD1 . ASP A 141 ? 1.3637 1.3637 1.3637 0.0000 0.0000 0.0000 124 ASP B OD1 
998  O OD2 . ASP A 141 ? 1.3637 1.3637 1.3637 0.0000 0.0000 0.0000 124 ASP B OD2 
999  N N   . THR A 142 ? 1.3333 1.3333 1.3333 0.0000 0.0000 0.0000 125 THR B N   
1000 C CA  . THR A 142 ? 1.3333 1.3333 1.3333 0.0000 0.0000 0.0000 125 THR B CA  
1001 C C   . THR A 142 ? 1.3333 1.3333 1.3333 0.0000 0.0000 0.0000 125 THR B C   
1002 O O   . THR A 142 ? 1.3333 1.3333 1.3333 0.0000 0.0000 0.0000 125 THR B O   
1003 C CB  . THR A 142 ? 1.3333 1.3333 1.3333 0.0000 0.0000 0.0000 125 THR B CB  
1004 O OG1 . THR A 142 ? 1.3333 1.3333 1.3333 0.0000 0.0000 0.0000 125 THR B OG1 
1005 C CG2 . THR A 142 ? 1.3333 1.3333 1.3333 0.0000 0.0000 0.0000 125 THR B CG2 
1006 N N   . GLU A 143 ? 1.3162 1.3162 1.3162 0.0000 0.0000 0.0000 126 GLU B N   
1007 C CA  . GLU A 143 ? 1.3162 1.3162 1.3162 0.0000 0.0000 0.0000 126 GLU B CA  
1008 C C   . GLU A 143 ? 1.3162 1.3162 1.3162 0.0000 0.0000 0.0000 126 GLU B C   
1009 O O   . GLU A 143 ? 1.3162 1.3162 1.3162 0.0000 0.0000 0.0000 126 GLU B O   
1010 C CB  . GLU A 143 ? 1.3162 1.3162 1.3162 0.0000 0.0000 0.0000 126 GLU B CB  
1011 C CG  . GLU A 143 ? 1.3162 1.3162 1.3162 0.0000 0.0000 0.0000 126 GLU B CG  
1012 C CD  . GLU A 143 ? 1.3162 1.3162 1.3162 0.0000 0.0000 0.0000 126 GLU B CD  
1013 O OE1 . GLU A 143 ? 1.3162 1.3162 1.3162 0.0000 0.0000 0.0000 126 GLU B OE1 
1014 O OE2 . GLU A 143 ? 1.3162 1.3162 1.3162 0.0000 0.0000 0.0000 126 GLU B OE2 
1015 N N   . LEU A 144 ? 1.2033 1.2033 1.2033 0.0000 0.0000 0.0000 127 LEU B N   
1016 C CA  . LEU A 144 ? 1.2033 1.2033 1.2033 0.0000 0.0000 0.0000 127 LEU B CA  
1017 C C   . LEU A 144 ? 1.2033 1.2033 1.2033 0.0000 0.0000 0.0000 127 LEU B C   
1018 O O   . LEU A 144 ? 1.2033 1.2033 1.2033 0.0000 0.0000 0.0000 127 LEU B O   
1019 C CB  . LEU A 144 ? 1.2033 1.2033 1.2033 0.0000 0.0000 0.0000 127 LEU B CB  
1020 C CG  . LEU A 144 ? 1.2033 1.2033 1.2033 0.0000 0.0000 0.0000 127 LEU B CG  
1021 C CD1 . LEU A 144 ? 1.2033 1.2033 1.2033 0.0000 0.0000 0.0000 127 LEU B CD1 
1022 C CD2 . LEU A 144 ? 1.2033 1.2033 1.2033 0.0000 0.0000 0.0000 127 LEU B CD2 
1023 N N   . LYS A 145 ? 1.1897 1.1897 1.1897 0.0000 0.0000 0.0000 128 LYS B N   
1024 C CA  . LYS A 145 ? 1.1897 1.1897 1.1897 0.0000 0.0000 0.0000 128 LYS B CA  
1025 C C   . LYS A 145 ? 1.1897 1.1897 1.1897 0.0000 0.0000 0.0000 128 LYS B C   
1026 O O   . LYS A 145 ? 1.1897 1.1897 1.1897 0.0000 0.0000 0.0000 128 LYS B O   
1027 C CB  . LYS A 145 ? 1.1897 1.1897 1.1897 0.0000 0.0000 0.0000 128 LYS B CB  
1028 C CG  . LYS A 145 ? 1.1897 1.1897 1.1897 0.0000 0.0000 0.0000 128 LYS B CG  
1029 C CD  . LYS A 145 ? 1.1897 1.1897 1.1897 0.0000 0.0000 0.0000 128 LYS B CD  
1030 C CE  . LYS A 145 ? 1.1897 1.1897 1.1897 0.0000 0.0000 0.0000 128 LYS B CE  
1031 N NZ  . LYS A 145 ? 1.1897 1.1897 1.1897 0.0000 0.0000 0.0000 128 LYS B NZ  
1032 N N   . VAL A 146 ? 1.1415 1.1415 1.1415 0.0000 0.0000 0.0000 129 VAL B N   
1033 C CA  . VAL A 146 ? 1.1415 1.1415 1.1415 0.0000 0.0000 0.0000 129 VAL B CA  
1034 C C   . VAL A 146 ? 1.1415 1.1415 1.1415 0.0000 0.0000 0.0000 129 VAL B C   
1035 O O   . VAL A 146 ? 1.1415 1.1415 1.1415 0.0000 0.0000 0.0000 129 VAL B O   
1036 C CB  . VAL A 146 ? 1.1415 1.1415 1.1415 0.0000 0.0000 0.0000 129 VAL B CB  
1037 C CG1 . VAL A 146 ? 1.1415 1.1415 1.1415 0.0000 0.0000 0.0000 129 VAL B CG1 
1038 C CG2 . VAL A 146 ? 1.1415 1.1415 1.1415 0.0000 0.0000 0.0000 129 VAL B CG2 
1039 N N   . ILE A 147 ? 1.0949 1.0949 1.0949 0.0000 0.0000 0.0000 130 ILE B N   
1040 C CA  . ILE A 147 ? 1.0949 1.0949 1.0949 0.0000 0.0000 0.0000 130 ILE B CA  
1041 C C   . ILE A 147 ? 1.0949 1.0949 1.0949 0.0000 0.0000 0.0000 130 ILE B C   
1042 O O   . ILE A 147 ? 1.0949 1.0949 1.0949 0.0000 0.0000 0.0000 130 ILE B O   
1043 C CB  . ILE A 147 ? 1.0949 1.0949 1.0949 0.0000 0.0000 0.0000 130 ILE B CB  
1044 C CG1 . ILE A 147 ? 1.0949 1.0949 1.0949 0.0000 0.0000 0.0000 130 ILE B CG1 
1045 C CG2 . ILE A 147 ? 1.0949 1.0949 1.0949 0.0000 0.0000 0.0000 130 ILE B CG2 
1046 C CD1 . ILE A 147 ? 1.0949 1.0949 1.0949 0.0000 0.0000 0.0000 130 ILE B CD1 
1047 N N   . ASP A 148 ? 1.0884 1.0884 1.0884 0.0000 0.0000 0.0000 131 ASP B N   
1048 C CA  . ASP A 148 ? 1.0884 1.0884 1.0884 0.0000 0.0000 0.0000 131 ASP B CA  
1049 C C   . ASP A 148 ? 1.0884 1.0884 1.0884 0.0000 0.0000 0.0000 131 ASP B C   
1050 O O   . ASP A 148 ? 1.0884 1.0884 1.0884 0.0000 0.0000 0.0000 131 ASP B O   
1051 C CB  . ASP A 148 ? 1.0884 1.0884 1.0884 0.0000 0.0000 0.0000 131 ASP B CB  
1052 C CG  . ASP A 148 ? 1.0884 1.0884 1.0884 0.0000 0.0000 0.0000 131 ASP B CG  
1053 O OD1 . ASP A 148 ? 1.0884 1.0884 1.0884 0.0000 0.0000 0.0000 131 ASP B OD1 
1054 O OD2 . ASP A 148 ? 1.0884 1.0884 1.0884 0.0000 0.0000 0.0000 131 ASP B OD2 
1055 N N   . THR A 149 ? 1.0559 1.0559 1.0559 0.0000 0.0000 0.0000 132 THR B N   
1056 C CA  . THR A 149 ? 1.0559 1.0559 1.0559 0.0000 0.0000 0.0000 132 THR B CA  
1057 C C   . THR A 149 ? 1.0559 1.0559 1.0559 0.0000 0.0000 0.0000 132 THR B C   
1058 O O   . THR A 149 ? 1.0559 1.0559 1.0559 0.0000 0.0000 0.0000 132 THR B O   
1059 C CB  . THR A 149 ? 1.0559 1.0559 1.0559 0.0000 0.0000 0.0000 132 THR B CB  
1060 O OG1 . THR A 149 ? 1.0559 1.0559 1.0559 0.0000 0.0000 0.0000 132 THR B OG1 
1061 C CG2 . THR A 149 ? 1.0559 1.0559 1.0559 0.0000 0.0000 0.0000 132 THR B CG2 
1062 N N   . ASN A 150 ? 0.9955 0.9955 0.9955 0.0000 0.0000 0.0000 133 ASN B N   
1063 C CA  . ASN A 150 ? 0.9955 0.9955 0.9955 0.0000 0.0000 0.0000 133 ASN B CA  
1064 C C   . ASN A 150 ? 0.9955 0.9955 0.9955 0.0000 0.0000 0.0000 133 ASN B C   
1065 O O   . ASN A 150 ? 0.9955 0.9955 0.9955 0.0000 0.0000 0.0000 133 ASN B O   
1066 C CB  . ASN A 150 ? 0.9955 0.9955 0.9955 0.0000 0.0000 0.0000 133 ASN B CB  
1067 C CG  . ASN A 150 ? 0.9955 0.9955 0.9955 0.0000 0.0000 0.0000 133 ASN B CG  
1068 O OD1 . ASN A 150 ? 0.9955 0.9955 0.9955 0.0000 0.0000 0.0000 133 ASN B OD1 
1069 N ND2 . ASN A 150 ? 0.9955 0.9955 0.9955 0.0000 0.0000 0.0000 133 ASN B ND2 
1070 N N   . CYS A 151 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 134 CYS B N   
1071 C CA  . CYS A 151 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 134 CYS B CA  
1072 C C   . CYS A 151 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 134 CYS B C   
1073 O O   . CYS A 151 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 134 CYS B O   
1074 C CB  . CYS A 151 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 134 CYS B CB  
1075 S SG  . CYS A 151 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 134 CYS B SG  
1076 N N   . ILE A 152 ? 0.9314 0.9314 0.9314 0.0000 0.0000 0.0000 135 ILE B N   
1077 C CA  . ILE A 152 ? 0.9314 0.9314 0.9314 0.0000 0.0000 0.0000 135 ILE B CA  
1078 C C   . ILE A 152 ? 0.9314 0.9314 0.9314 0.0000 0.0000 0.0000 135 ILE B C   
1079 O O   . ILE A 152 ? 0.9314 0.9314 0.9314 0.0000 0.0000 0.0000 135 ILE B O   
1080 C CB  . ILE A 152 ? 0.9314 0.9314 0.9314 0.0000 0.0000 0.0000 135 ILE B CB  
1081 C CG1 . ILE A 152 ? 0.9314 0.9314 0.9314 0.0000 0.0000 0.0000 135 ILE B CG1 
1082 C CG2 . ILE A 152 ? 0.9314 0.9314 0.9314 0.0000 0.0000 0.0000 135 ILE B CG2 
1083 C CD1 . ILE A 152 ? 0.9314 0.9314 0.9314 0.0000 0.0000 0.0000 135 ILE B CD1 
1084 N N   . ASN A 153 ? 1.0008 1.0008 1.0008 0.0000 0.0000 0.0000 136 ASN B N   
1085 C CA  . ASN A 153 ? 1.0008 1.0008 1.0008 0.0000 0.0000 0.0000 136 ASN B CA  
1086 C C   . ASN A 153 ? 1.0008 1.0008 1.0008 0.0000 0.0000 0.0000 136 ASN B C   
1087 O O   . ASN A 153 ? 1.0008 1.0008 1.0008 0.0000 0.0000 0.0000 136 ASN B O   
1088 C CB  . ASN A 153 ? 1.0008 1.0008 1.0008 0.0000 0.0000 0.0000 136 ASN B CB  
1089 C CG  . ASN A 153 ? 1.0008 1.0008 1.0008 0.0000 0.0000 0.0000 136 ASN B CG  
1090 O OD1 . ASN A 153 ? 1.0008 1.0008 1.0008 0.0000 0.0000 0.0000 136 ASN B OD1 
1091 N ND2 . ASN A 153 ? 1.0008 1.0008 1.0008 0.0000 0.0000 0.0000 136 ASN B ND2 
1092 N N   . VAL A 154 ? 1.0124 1.0124 1.0124 0.0000 0.0000 0.0000 137 VAL B N   
1093 C CA  . VAL A 154 ? 1.0124 1.0124 1.0124 0.0000 0.0000 0.0000 137 VAL B CA  
1094 C C   . VAL A 154 ? 1.0124 1.0124 1.0124 0.0000 0.0000 0.0000 137 VAL B C   
1095 O O   . VAL A 154 ? 1.0124 1.0124 1.0124 0.0000 0.0000 0.0000 137 VAL B O   
1096 C CB  . VAL A 154 ? 1.0124 1.0124 1.0124 0.0000 0.0000 0.0000 137 VAL B CB  
1097 C CG1 . VAL A 154 ? 1.0124 1.0124 1.0124 0.0000 0.0000 0.0000 137 VAL B CG1 
1098 C CG2 . VAL A 154 ? 1.0124 1.0124 1.0124 0.0000 0.0000 0.0000 137 VAL B CG2 
1099 N N   . ILE A 155 ? 1.0674 1.0674 1.0674 0.0000 0.0000 0.0000 138 ILE B N   
1100 C CA  . ILE A 155 ? 1.0674 1.0674 1.0674 0.0000 0.0000 0.0000 138 ILE B CA  
1101 C C   . ILE A 155 ? 1.0674 1.0674 1.0674 0.0000 0.0000 0.0000 138 ILE B C   
1102 O O   . ILE A 155 ? 1.0674 1.0674 1.0674 0.0000 0.0000 0.0000 138 ILE B O   
1103 C CB  . ILE A 155 ? 1.0674 1.0674 1.0674 0.0000 0.0000 0.0000 138 ILE B CB  
1104 C CG1 . ILE A 155 ? 1.0674 1.0674 1.0674 0.0000 0.0000 0.0000 138 ILE B CG1 
1105 C CG2 . ILE A 155 ? 1.0674 1.0674 1.0674 0.0000 0.0000 0.0000 138 ILE B CG2 
1106 C CD1 . ILE A 155 ? 1.0674 1.0674 1.0674 0.0000 0.0000 0.0000 138 ILE B CD1 
1107 N N   . GLN A 156 ? 1.1637 1.1637 1.1637 0.0000 0.0000 0.0000 139 GLN B N   
1108 C CA  . GLN A 156 ? 1.1637 1.1637 1.1637 0.0000 0.0000 0.0000 139 GLN B CA  
1109 C C   . GLN A 156 ? 1.1637 1.1637 1.1637 0.0000 0.0000 0.0000 139 GLN B C   
1110 O O   . GLN A 156 ? 1.1637 1.1637 1.1637 0.0000 0.0000 0.0000 139 GLN B O   
1111 C CB  . GLN A 156 ? 1.1637 1.1637 1.1637 0.0000 0.0000 0.0000 139 GLN B CB  
1112 C CG  . GLN A 156 ? 1.1637 1.1637 1.1637 0.0000 0.0000 0.0000 139 GLN B CG  
1113 C CD  . GLN A 156 ? 1.1637 1.1637 1.1637 0.0000 0.0000 0.0000 139 GLN B CD  
1114 O OE1 . GLN A 156 ? 1.1637 1.1637 1.1637 0.0000 0.0000 0.0000 139 GLN B OE1 
1115 N NE2 . GLN A 156 ? 1.1637 1.1637 1.1637 0.0000 0.0000 0.0000 139 GLN B NE2 
1116 N N   . PRO A 157 ? 1.1949 1.1949 1.1949 0.0000 0.0000 0.0000 140 PRO B N   
1117 C CA  . PRO A 157 ? 1.1949 1.1949 1.1949 0.0000 0.0000 0.0000 140 PRO B CA  
1118 C C   . PRO A 157 ? 1.1949 1.1949 1.1949 0.0000 0.0000 0.0000 140 PRO B C   
1119 O O   . PRO A 157 ? 1.1949 1.1949 1.1949 0.0000 0.0000 0.0000 140 PRO B O   
1120 C CB  . PRO A 157 ? 1.1949 1.1949 1.1949 0.0000 0.0000 0.0000 140 PRO B CB  
1121 C CG  . PRO A 157 ? 1.1949 1.1949 1.1949 0.0000 0.0000 0.0000 140 PRO B CG  
1122 C CD  . PRO A 157 ? 1.1949 1.1949 1.1949 0.0000 0.0000 0.0000 140 PRO B CD  
1123 N N   . ASP A 158 ? 1.2397 1.2397 1.2397 0.0000 0.0000 0.0000 141 ASP B N   
1124 C CA  . ASP A 158 ? 1.2397 1.2397 1.2397 0.0000 0.0000 0.0000 141 ASP B CA  
1125 C C   . ASP A 158 ? 1.2397 1.2397 1.2397 0.0000 0.0000 0.0000 141 ASP B C   
1126 O O   . ASP A 158 ? 1.2397 1.2397 1.2397 0.0000 0.0000 0.0000 141 ASP B O   
1127 C CB  . ASP A 158 ? 1.2397 1.2397 1.2397 0.0000 0.0000 0.0000 141 ASP B CB  
1128 C CG  . ASP A 158 ? 1.2397 1.2397 1.2397 0.0000 0.0000 0.0000 141 ASP B CG  
1129 O OD1 . ASP A 158 ? 1.2397 1.2397 1.2397 0.0000 0.0000 0.0000 141 ASP B OD1 
1130 O OD2 . ASP A 158 ? 1.2397 1.2397 1.2397 0.0000 0.0000 0.0000 141 ASP B OD2 
1131 N N   . GLY A 159 ? 1.2358 1.2358 1.2358 0.0000 0.0000 0.0000 142 GLY B N   
1132 C CA  . GLY A 159 ? 1.2358 1.2358 1.2358 0.0000 0.0000 0.0000 142 GLY B CA  
1133 C C   . GLY A 159 ? 1.2358 1.2358 1.2358 0.0000 0.0000 0.0000 142 GLY B C   
1134 O O   . GLY A 159 ? 1.2358 1.2358 1.2358 0.0000 0.0000 0.0000 142 GLY B O   
1135 N N   . SER A 160 ? 1.1939 1.1939 1.1939 0.0000 0.0000 0.0000 143 SER B N   
1136 C CA  . SER A 160 ? 1.1939 1.1939 1.1939 0.0000 0.0000 0.0000 143 SER B CA  
1137 C C   . SER A 160 ? 1.1939 1.1939 1.1939 0.0000 0.0000 0.0000 143 SER B C   
1138 O O   . SER A 160 ? 1.1939 1.1939 1.1939 0.0000 0.0000 0.0000 143 SER B O   
1139 C CB  . SER A 160 ? 1.1939 1.1939 1.1939 0.0000 0.0000 0.0000 143 SER B CB  
1140 O OG  . SER A 160 ? 1.1939 1.1939 1.1939 0.0000 0.0000 0.0000 143 SER B OG  
1141 N N   . TYR A 161 ? 1.1573 1.1573 1.1573 0.0000 0.0000 0.0000 144 TYR B N   
1142 C CA  . TYR A 161 ? 1.1573 1.1573 1.1573 0.0000 0.0000 0.0000 144 TYR B CA  
1143 C C   . TYR A 161 ? 1.1573 1.1573 1.1573 0.0000 0.0000 0.0000 144 TYR B C   
1144 O O   . TYR A 161 ? 1.1573 1.1573 1.1573 0.0000 0.0000 0.0000 144 TYR B O   
1145 C CB  . TYR A 161 ? 1.1573 1.1573 1.1573 0.0000 0.0000 0.0000 144 TYR B CB  
1146 C CG  . TYR A 161 ? 1.1573 1.1573 1.1573 0.0000 0.0000 0.0000 144 TYR B CG  
1147 C CD1 . TYR A 161 ? 1.1573 1.1573 1.1573 0.0000 0.0000 0.0000 144 TYR B CD1 
1148 C CD2 . TYR A 161 ? 1.1573 1.1573 1.1573 0.0000 0.0000 0.0000 144 TYR B CD2 
1149 C CE1 . TYR A 161 ? 1.1573 1.1573 1.1573 0.0000 0.0000 0.0000 144 TYR B CE1 
1150 C CE2 . TYR A 161 ? 1.1573 1.1573 1.1573 0.0000 0.0000 0.0000 144 TYR B CE2 
1151 C CZ  . TYR A 161 ? 1.1573 1.1573 1.1573 0.0000 0.0000 0.0000 144 TYR B CZ  
1152 O OH  . TYR A 161 ? 1.1573 1.1573 1.1573 0.0000 0.0000 0.0000 144 TYR B OH  
1153 N N   . ARG A 162 ? 1.0855 1.0855 1.0855 0.0000 0.0000 0.0000 145 ARG B N   
1154 C CA  . ARG A 162 ? 1.0855 1.0855 1.0855 0.0000 0.0000 0.0000 145 ARG B CA  
1155 C C   . ARG A 162 ? 1.0855 1.0855 1.0855 0.0000 0.0000 0.0000 145 ARG B C   
1156 O O   . ARG A 162 ? 1.0855 1.0855 1.0855 0.0000 0.0000 0.0000 145 ARG B O   
1157 C CB  . ARG A 162 ? 1.0855 1.0855 1.0855 0.0000 0.0000 0.0000 145 ARG B CB  
1158 C CG  . ARG A 162 ? 1.0855 1.0855 1.0855 0.0000 0.0000 0.0000 145 ARG B CG  
1159 C CD  . ARG A 162 ? 1.0855 1.0855 1.0855 0.0000 0.0000 0.0000 145 ARG B CD  
1160 N NE  . ARG A 162 ? 1.0855 1.0855 1.0855 0.0000 0.0000 0.0000 145 ARG B NE  
1161 C CZ  . ARG A 162 ? 1.0855 1.0855 1.0855 0.0000 0.0000 0.0000 145 ARG B CZ  
1162 N NH1 . ARG A 162 ? 1.0855 1.0855 1.0855 0.0000 0.0000 0.0000 145 ARG B NH1 
1163 N NH2 . ARG A 162 ? 1.0855 1.0855 1.0855 0.0000 0.0000 0.0000 145 ARG B NH2 
1164 N N   . SER A 163 ? 1.0295 1.0295 1.0295 0.0000 0.0000 0.0000 146 SER B N   
1165 C CA  . SER A 163 ? 1.0295 1.0295 1.0295 0.0000 0.0000 0.0000 146 SER B CA  
1166 C C   . SER A 163 ? 1.0295 1.0295 1.0295 0.0000 0.0000 0.0000 146 SER B C   
1167 O O   . SER A 163 ? 1.0295 1.0295 1.0295 0.0000 0.0000 0.0000 146 SER B O   
1168 C CB  . SER A 163 ? 1.0295 1.0295 1.0295 0.0000 0.0000 0.0000 146 SER B CB  
1169 O OG  . SER A 163 ? 1.0295 1.0295 1.0295 0.0000 0.0000 0.0000 146 SER B OG  
1170 N N   . GLU A 164 ? 1.0020 1.0020 1.0020 0.0000 0.0000 0.0000 147 GLU B N   
1171 C CA  . GLU A 164 ? 1.0020 1.0020 1.0020 0.0000 0.0000 0.0000 147 GLU B CA  
1172 C C   . GLU A 164 ? 1.0020 1.0020 1.0020 0.0000 0.0000 0.0000 147 GLU B C   
1173 O O   . GLU A 164 ? 1.0020 1.0020 1.0020 0.0000 0.0000 0.0000 147 GLU B O   
1174 C CB  . GLU A 164 ? 1.0020 1.0020 1.0020 0.0000 0.0000 0.0000 147 GLU B CB  
1175 C CG  . GLU A 164 ? 1.0020 1.0020 1.0020 0.0000 0.0000 0.0000 147 GLU B CG  
1176 C CD  . GLU A 164 ? 1.0020 1.0020 1.0020 0.0000 0.0000 0.0000 147 GLU B CD  
1177 O OE1 . GLU A 164 ? 1.0020 1.0020 1.0020 0.0000 0.0000 0.0000 147 GLU B OE1 
1178 O OE2 . GLU A 164 ? 1.0020 1.0020 1.0020 0.0000 0.0000 0.0000 147 GLU B OE2 
1179 N N   . GLU A 165 ? 0.9708 0.9708 0.9708 0.0000 0.0000 0.0000 148 GLU B N   
1180 C CA  . GLU A 165 ? 0.9708 0.9708 0.9708 0.0000 0.0000 0.0000 148 GLU B CA  
1181 C C   . GLU A 165 ? 0.9708 0.9708 0.9708 0.0000 0.0000 0.0000 148 GLU B C   
1182 O O   . GLU A 165 ? 0.9708 0.9708 0.9708 0.0000 0.0000 0.0000 148 GLU B O   
1183 C CB  . GLU A 165 ? 0.9708 0.9708 0.9708 0.0000 0.0000 0.0000 148 GLU B CB  
1184 C CG  . GLU A 165 ? 0.9708 0.9708 0.9708 0.0000 0.0000 0.0000 148 GLU B CG  
1185 C CD  . GLU A 165 ? 0.9708 0.9708 0.9708 0.0000 0.0000 0.0000 148 GLU B CD  
1186 O OE1 . GLU A 165 ? 0.9708 0.9708 0.9708 0.0000 0.0000 0.0000 148 GLU B OE1 
1187 O OE2 . GLU A 165 ? 0.9708 0.9708 0.9708 0.0000 0.0000 0.0000 148 GLU B OE2 
1188 N N   . LEU A 166 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 149 LEU B N   
1189 C CA  . LEU A 166 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 149 LEU B CA  
1190 C C   . LEU A 166 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 149 LEU B C   
1191 O O   . LEU A 166 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 149 LEU B O   
1192 C CB  . LEU A 166 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 149 LEU B CB  
1193 C CG  . LEU A 166 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 149 LEU B CG  
1194 C CD1 . LEU A 166 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 149 LEU B CD1 
1195 C CD2 . LEU A 166 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 149 LEU B CD2 
1196 N N   . ASN A 167 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 150 ASN B N   
1197 C CA  . ASN A 167 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 150 ASN B CA  
1198 C C   . ASN A 167 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 150 ASN B C   
1199 O O   . ASN A 167 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 150 ASN B O   
1200 C CB  . ASN A 167 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 150 ASN B CB  
1201 C CG  . ASN A 167 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 150 ASN B CG  
1202 O OD1 . ASN A 167 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 150 ASN B OD1 
1203 N ND2 . ASN A 167 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 150 ASN B ND2 
1204 N N   . LEU A 168 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 151 LEU B N   
1205 C CA  . LEU A 168 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 151 LEU B CA  
1206 C C   . LEU A 168 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 151 LEU B C   
1207 O O   . LEU A 168 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 151 LEU B O   
1208 C CB  . LEU A 168 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 151 LEU B CB  
1209 C CG  . LEU A 168 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 151 LEU B CG  
1210 C CD1 . LEU A 168 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 151 LEU B CD1 
1211 C CD2 . LEU A 168 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 151 LEU B CD2 
1212 N N   . VAL A 169 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 152 VAL B N   
1213 C CA  . VAL A 169 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 152 VAL B CA  
1214 C C   . VAL A 169 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 152 VAL B C   
1215 O O   . VAL A 169 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 152 VAL B O   
1216 C CB  . VAL A 169 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 152 VAL B CB  
1217 C CG1 . VAL A 169 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 152 VAL B CG1 
1218 C CG2 . VAL A 169 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 152 VAL B CG2 
1219 N N   . ILE A 170 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 153 ILE B N   
1220 C CA  . ILE A 170 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 153 ILE B CA  
1221 C C   . ILE A 170 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 153 ILE B C   
1222 O O   . ILE A 170 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 153 ILE B O   
1223 C CB  . ILE A 170 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 153 ILE B CB  
1224 C CG1 . ILE A 170 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 153 ILE B CG1 
1225 C CG2 . ILE A 170 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 153 ILE B CG2 
1226 C CD1 . ILE A 170 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 153 ILE B CD1 
1227 N N   . ILE A 171 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 154 ILE B N   
1228 C CA  . ILE A 171 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 154 ILE B CA  
1229 C C   . ILE A 171 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 154 ILE B C   
1230 O O   . ILE A 171 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 154 ILE B O   
1231 C CB  . ILE A 171 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 154 ILE B CB  
1232 C CG1 . ILE A 171 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 154 ILE B CG1 
1233 C CG2 . ILE A 171 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 154 ILE B CG2 
1234 C CD1 . ILE A 171 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 154 ILE B CD1 
1235 N N   . GLY A 172 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 155 GLY B N   
1236 C CA  . GLY A 172 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 155 GLY B CA  
1237 C C   . GLY A 172 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 155 GLY B C   
1238 O O   . GLY A 172 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 155 GLY B O   
1239 N N   . PRO A 173 ? 0.9097 0.9097 0.9097 0.0000 0.0000 0.0000 156 PRO B N   
1240 C CA  . PRO A 173 ? 0.9097 0.9097 0.9097 0.0000 0.0000 0.0000 156 PRO B CA  
1241 C C   . PRO A 173 ? 0.9097 0.9097 0.9097 0.0000 0.0000 0.0000 156 PRO B C   
1242 O O   . PRO A 173 ? 0.9097 0.9097 0.9097 0.0000 0.0000 0.0000 156 PRO B O   
1243 C CB  . PRO A 173 ? 0.9097 0.9097 0.9097 0.0000 0.0000 0.0000 156 PRO B CB  
1244 C CG  . PRO A 173 ? 0.9097 0.9097 0.9097 0.0000 0.0000 0.0000 156 PRO B CG  
1245 C CD  . PRO A 173 ? 0.9097 0.9097 0.9097 0.0000 0.0000 0.0000 156 PRO B CD  
1246 N N   . SER A 174 ? 1.0215 1.0215 1.0215 0.0000 0.0000 0.0000 157 SER B N   
1247 C CA  . SER A 174 ? 1.0215 1.0215 1.0215 0.0000 0.0000 0.0000 157 SER B CA  
1248 C C   . SER A 174 ? 1.0215 1.0215 1.0215 0.0000 0.0000 0.0000 157 SER B C   
1249 O O   . SER A 174 ? 1.0215 1.0215 1.0215 0.0000 0.0000 0.0000 157 SER B O   
1250 C CB  . SER A 174 ? 1.0215 1.0215 1.0215 0.0000 0.0000 0.0000 157 SER B CB  
1251 O OG  . SER A 174 ? 1.0215 1.0215 1.0215 0.0000 0.0000 0.0000 157 SER B OG  
1252 N N   . ALA A 175 ? 1.0226 1.0226 1.0226 0.0000 0.0000 0.0000 158 ALA B N   
1253 C CA  . ALA A 175 ? 1.0226 1.0226 1.0226 0.0000 0.0000 0.0000 158 ALA B CA  
1254 C C   . ALA A 175 ? 1.0226 1.0226 1.0226 0.0000 0.0000 0.0000 158 ALA B C   
1255 O O   . ALA A 175 ? 1.0226 1.0226 1.0226 0.0000 0.0000 0.0000 158 ALA B O   
1256 C CB  . ALA A 175 ? 1.0226 1.0226 1.0226 0.0000 0.0000 0.0000 158 ALA B CB  
1257 N N   . ASP A 176 ? 0.9502 0.9502 0.9502 0.0000 0.0000 0.0000 159 ASP B N   
1258 C CA  . ASP A 176 ? 0.9502 0.9502 0.9502 0.0000 0.0000 0.0000 159 ASP B CA  
1259 C C   . ASP A 176 ? 0.9502 0.9502 0.9502 0.0000 0.0000 0.0000 159 ASP B C   
1260 O O   . ASP A 176 ? 0.9502 0.9502 0.9502 0.0000 0.0000 0.0000 159 ASP B O   
1261 C CB  . ASP A 176 ? 0.9502 0.9502 0.9502 0.0000 0.0000 0.0000 159 ASP B CB  
1262 C CG  . ASP A 176 ? 0.9502 0.9502 0.9502 0.0000 0.0000 0.0000 159 ASP B CG  
1263 O OD1 . ASP A 176 ? 0.9502 0.9502 0.9502 0.0000 0.0000 0.0000 159 ASP B OD1 
1264 O OD2 . ASP A 176 ? 0.9502 0.9502 0.9502 0.0000 0.0000 0.0000 159 ASP B OD2 
1265 N N   . ILE A 177 ? 0.8932 0.8932 0.8932 0.0000 0.0000 0.0000 160 ILE B N   
1266 C CA  . ILE A 177 ? 0.8932 0.8932 0.8932 0.0000 0.0000 0.0000 160 ILE B CA  
1267 C C   . ILE A 177 ? 0.8932 0.8932 0.8932 0.0000 0.0000 0.0000 160 ILE B C   
1268 O O   . ILE A 177 ? 0.8932 0.8932 0.8932 0.0000 0.0000 0.0000 160 ILE B O   
1269 C CB  . ILE A 177 ? 0.8932 0.8932 0.8932 0.0000 0.0000 0.0000 160 ILE B CB  
1270 C CG1 . ILE A 177 ? 0.8932 0.8932 0.8932 0.0000 0.0000 0.0000 160 ILE B CG1 
1271 C CG2 . ILE A 177 ? 0.8932 0.8932 0.8932 0.0000 0.0000 0.0000 160 ILE B CG2 
1272 C CD1 . ILE A 177 ? 0.8932 0.8932 0.8932 0.0000 0.0000 0.0000 160 ILE B CD1 
1273 N N   . ILE A 178 ? 0.9118 0.9118 0.9118 0.0000 0.0000 0.0000 161 ILE B N   
1274 C CA  . ILE A 178 ? 0.9118 0.9118 0.9118 0.0000 0.0000 0.0000 161 ILE B CA  
1275 C C   . ILE A 178 ? 0.9118 0.9118 0.9118 0.0000 0.0000 0.0000 161 ILE B C   
1276 O O   . ILE A 178 ? 0.9118 0.9118 0.9118 0.0000 0.0000 0.0000 161 ILE B O   
1277 C CB  . ILE A 178 ? 0.9118 0.9118 0.9118 0.0000 0.0000 0.0000 161 ILE B CB  
1278 C CG1 . ILE A 178 ? 0.9118 0.9118 0.9118 0.0000 0.0000 0.0000 161 ILE B CG1 
1279 C CG2 . ILE A 178 ? 0.9118 0.9118 0.9118 0.0000 0.0000 0.0000 161 ILE B CG2 
1280 C CD1 . ILE A 178 ? 0.9118 0.9118 0.9118 0.0000 0.0000 0.0000 161 ILE B CD1 
1281 N N   . GLN A 179 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 162 GLN B N   
1282 C CA  . GLN A 179 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 162 GLN B CA  
1283 C C   . GLN A 179 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 162 GLN B C   
1284 O O   . GLN A 179 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 162 GLN B O   
1285 C CB  . GLN A 179 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 162 GLN B CB  
1286 C CG  . GLN A 179 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 162 GLN B CG  
1287 C CD  . GLN A 179 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 162 GLN B CD  
1288 O OE1 . GLN A 179 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 162 GLN B OE1 
1289 N NE2 . GLN A 179 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 162 GLN B NE2 
1290 N N   . PHE A 180 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 163 PHE B N   
1291 C CA  . PHE A 180 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 163 PHE B CA  
1292 C C   . PHE A 180 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 163 PHE B C   
1293 O O   . PHE A 180 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 163 PHE B O   
1294 C CB  . PHE A 180 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 163 PHE B CB  
1295 C CG  . PHE A 180 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 163 PHE B CG  
1296 C CD1 . PHE A 180 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 163 PHE B CD1 
1297 C CD2 . PHE A 180 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 163 PHE B CD2 
1298 C CE1 . PHE A 180 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 163 PHE B CE1 
1299 C CE2 . PHE A 180 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 163 PHE B CE2 
1300 C CZ  . PHE A 180 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 163 PHE B CZ  
1301 N N   . GLU A 181 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 164 GLU B N   
1302 C CA  . GLU A 181 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 164 GLU B CA  
1303 C C   . GLU A 181 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 164 GLU B C   
1304 O O   . GLU A 181 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 164 GLU B O   
1305 C CB  . GLU A 181 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 164 GLU B CB  
1306 C CG  . GLU A 181 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 164 GLU B CG  
1307 C CD  . GLU A 181 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 164 GLU B CD  
1308 O OE1 . GLU A 181 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 164 GLU B OE1 
1309 O OE2 . GLU A 181 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 164 GLU B OE2 
1310 N N   . CYS A 182 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 165 CYS B N   
1311 C CA  . CYS A 182 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 165 CYS B CA  
1312 C C   . CYS A 182 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 165 CYS B C   
1313 O O   . CYS A 182 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 165 CYS B O   
1314 C CB  . CYS A 182 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 165 CYS B CB  
1315 S SG  . CYS A 182 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 165 CYS B SG  
1316 N N   . LYS A 183 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 166 LYS B N   
1317 C CA  . LYS A 183 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 166 LYS B CA  
1318 C C   . LYS A 183 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 166 LYS B C   
1319 O O   . LYS A 183 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 166 LYS B O   
1320 C CB  . LYS A 183 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 166 LYS B CB  
1321 C CG  . LYS A 183 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 166 LYS B CG  
1322 C CD  . LYS A 183 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 166 LYS B CD  
1323 C CE  . LYS A 183 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 166 LYS B CE  
1324 N NZ  . LYS A 183 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 166 LYS B NZ  
1325 N N   . SER A 184 ? 0.9646 0.9646 0.9646 0.0000 0.0000 0.0000 167 SER B N   
1326 C CA  . SER A 184 ? 0.9646 0.9646 0.9646 0.0000 0.0000 0.0000 167 SER B CA  
1327 C C   . SER A 184 ? 0.9646 0.9646 0.9646 0.0000 0.0000 0.0000 167 SER B C   
1328 O O   . SER A 184 ? 0.9646 0.9646 0.9646 0.0000 0.0000 0.0000 167 SER B O   
1329 C CB  . SER A 184 ? 0.9646 0.9646 0.9646 0.0000 0.0000 0.0000 167 SER B CB  
1330 O OG  . SER A 184 ? 0.9646 0.9646 0.9646 0.0000 0.0000 0.0000 167 SER B OG  
1331 N N   . PHE A 185 ? 1.0163 1.0163 1.0163 0.0000 0.0000 0.0000 168 PHE B N   
1332 C CA  . PHE A 185 ? 1.0163 1.0163 1.0163 0.0000 0.0000 0.0000 168 PHE B CA  
1333 C C   . PHE A 185 ? 1.0163 1.0163 1.0163 0.0000 0.0000 0.0000 168 PHE B C   
1334 O O   . PHE A 185 ? 1.0163 1.0163 1.0163 0.0000 0.0000 0.0000 168 PHE B O   
1335 C CB  . PHE A 185 ? 1.0163 1.0163 1.0163 0.0000 0.0000 0.0000 168 PHE B CB  
1336 C CG  . PHE A 185 ? 1.0163 1.0163 1.0163 0.0000 0.0000 0.0000 168 PHE B CG  
1337 C CD1 . PHE A 185 ? 1.0163 1.0163 1.0163 0.0000 0.0000 0.0000 168 PHE B CD1 
1338 C CD2 . PHE A 185 ? 1.0163 1.0163 1.0163 0.0000 0.0000 0.0000 168 PHE B CD2 
1339 C CE1 . PHE A 185 ? 1.0163 1.0163 1.0163 0.0000 0.0000 0.0000 168 PHE B CE1 
1340 C CE2 . PHE A 185 ? 1.0163 1.0163 1.0163 0.0000 0.0000 0.0000 168 PHE B CE2 
1341 C CZ  . PHE A 185 ? 1.0163 1.0163 1.0163 0.0000 0.0000 0.0000 168 PHE B CZ  
1342 N N   . GLY A 186 ? 1.1255 1.1255 1.1255 0.0000 0.0000 0.0000 169 GLY B N   
1343 C CA  . GLY A 186 ? 1.1255 1.1255 1.1255 0.0000 0.0000 0.0000 169 GLY B CA  
1344 C C   . GLY A 186 ? 1.1255 1.1255 1.1255 0.0000 0.0000 0.0000 169 GLY B C   
1345 O O   . GLY A 186 ? 1.1255 1.1255 1.1255 0.0000 0.0000 0.0000 169 GLY B O   
1346 N N   . HIS A 187 ? 1.1887 1.1887 1.1887 0.0000 0.0000 0.0000 170 HIS B N   
1347 C CA  . HIS A 187 ? 1.1887 1.1887 1.1887 0.0000 0.0000 0.0000 170 HIS B CA  
1348 C C   . HIS A 187 ? 1.1887 1.1887 1.1887 0.0000 0.0000 0.0000 170 HIS B C   
1349 O O   . HIS A 187 ? 1.1887 1.1887 1.1887 0.0000 0.0000 0.0000 170 HIS B O   
1350 C CB  . HIS A 187 ? 1.1887 1.1887 1.1887 0.0000 0.0000 0.0000 170 HIS B CB  
1351 C CG  . HIS A 187 ? 1.1887 1.1887 1.1887 0.0000 0.0000 0.0000 170 HIS B CG  
1352 N ND1 . HIS A 187 ? 1.1887 1.1887 1.1887 0.0000 0.0000 0.0000 170 HIS B ND1 
1353 C CD2 . HIS A 187 ? 1.1887 1.1887 1.1887 0.0000 0.0000 0.0000 170 HIS B CD2 
1354 C CE1 . HIS A 187 ? 1.1887 1.1887 1.1887 0.0000 0.0000 0.0000 170 HIS B CE1 
1355 N NE2 . HIS A 187 ? 1.1887 1.1887 1.1887 0.0000 0.0000 0.0000 170 HIS B NE2 
1356 N N   . GLU A 188 ? 1.2416 1.2416 1.2416 0.0000 0.0000 0.0000 171 GLU B N   
1357 C CA  . GLU A 188 ? 1.2416 1.2416 1.2416 0.0000 0.0000 0.0000 171 GLU B CA  
1358 C C   . GLU A 188 ? 1.2416 1.2416 1.2416 0.0000 0.0000 0.0000 171 GLU B C   
1359 O O   . GLU A 188 ? 1.2416 1.2416 1.2416 0.0000 0.0000 0.0000 171 GLU B O   
1360 C CB  . GLU A 188 ? 1.2416 1.2416 1.2416 0.0000 0.0000 0.0000 171 GLU B CB  
1361 C CG  . GLU A 188 ? 1.2416 1.2416 1.2416 0.0000 0.0000 0.0000 171 GLU B CG  
1362 C CD  . GLU A 188 ? 1.2416 1.2416 1.2416 0.0000 0.0000 0.0000 171 GLU B CD  
1363 O OE1 . GLU A 188 ? 1.2416 1.2416 1.2416 0.0000 0.0000 0.0000 171 GLU B OE1 
1364 O OE2 . GLU A 188 ? 1.2416 1.2416 1.2416 0.0000 0.0000 0.0000 171 GLU B OE2 
1365 N N   . VAL A 189 ? 1.2022 1.2022 1.2022 0.0000 0.0000 0.0000 172 VAL B N   
1366 C CA  . VAL A 189 ? 1.2022 1.2022 1.2022 0.0000 0.0000 0.0000 172 VAL B CA  
1367 C C   . VAL A 189 ? 1.2022 1.2022 1.2022 0.0000 0.0000 0.0000 172 VAL B C   
1368 O O   . VAL A 189 ? 1.2022 1.2022 1.2022 0.0000 0.0000 0.0000 172 VAL B O   
1369 C CB  . VAL A 189 ? 1.2022 1.2022 1.2022 0.0000 0.0000 0.0000 172 VAL B CB  
1370 C CG1 . VAL A 189 ? 1.2022 1.2022 1.2022 0.0000 0.0000 0.0000 172 VAL B CG1 
1371 C CG2 . VAL A 189 ? 1.2022 1.2022 1.2022 0.0000 0.0000 0.0000 172 VAL B CG2 
1372 N N   . LEU A 190 ? 1.1024 1.1024 1.1024 0.0000 0.0000 0.0000 173 LEU B N   
1373 C CA  . LEU A 190 ? 1.1024 1.1024 1.1024 0.0000 0.0000 0.0000 173 LEU B CA  
1374 C C   . LEU A 190 ? 1.1024 1.1024 1.1024 0.0000 0.0000 0.0000 173 LEU B C   
1375 O O   . LEU A 190 ? 1.1024 1.1024 1.1024 0.0000 0.0000 0.0000 173 LEU B O   
1376 C CB  . LEU A 190 ? 1.1024 1.1024 1.1024 0.0000 0.0000 0.0000 173 LEU B CB  
1377 C CG  . LEU A 190 ? 1.1024 1.1024 1.1024 0.0000 0.0000 0.0000 173 LEU B CG  
1378 C CD1 . LEU A 190 ? 1.1024 1.1024 1.1024 0.0000 0.0000 0.0000 173 LEU B CD1 
1379 C CD2 . LEU A 190 ? 1.1024 1.1024 1.1024 0.0000 0.0000 0.0000 173 LEU B CD2 
1380 N N   . ASN A 191 ? 0.9947 0.9947 0.9947 0.0000 0.0000 0.0000 174 ASN B N   
1381 C CA  . ASN A 191 ? 0.9947 0.9947 0.9947 0.0000 0.0000 0.0000 174 ASN B CA  
1382 C C   . ASN A 191 ? 0.9947 0.9947 0.9947 0.0000 0.0000 0.0000 174 ASN B C   
1383 O O   . ASN A 191 ? 0.9947 0.9947 0.9947 0.0000 0.0000 0.0000 174 ASN B O   
1384 C CB  . ASN A 191 ? 0.9947 0.9947 0.9947 0.0000 0.0000 0.0000 174 ASN B CB  
1385 C CG  . ASN A 191 ? 0.9947 0.9947 0.9947 0.0000 0.0000 0.0000 174 ASN B CG  
1386 O OD1 . ASN A 191 ? 0.9947 0.9947 0.9947 0.0000 0.0000 0.0000 174 ASN B OD1 
1387 N ND2 . ASN A 191 ? 0.9947 0.9947 0.9947 0.0000 0.0000 0.0000 174 ASN B ND2 
1388 N N   . LEU A 192 ? 0.9102 0.9102 0.9102 0.0000 0.0000 0.0000 175 LEU B N   
1389 C CA  . LEU A 192 ? 0.9102 0.9102 0.9102 0.0000 0.0000 0.0000 175 LEU B CA  
1390 C C   . LEU A 192 ? 0.9102 0.9102 0.9102 0.0000 0.0000 0.0000 175 LEU B C   
1391 O O   . LEU A 192 ? 0.9102 0.9102 0.9102 0.0000 0.0000 0.0000 175 LEU B O   
1392 C CB  . LEU A 192 ? 0.9102 0.9102 0.9102 0.0000 0.0000 0.0000 175 LEU B CB  
1393 C CG  . LEU A 192 ? 0.9102 0.9102 0.9102 0.0000 0.0000 0.0000 175 LEU B CG  
1394 C CD1 . LEU A 192 ? 0.9102 0.9102 0.9102 0.0000 0.0000 0.0000 175 LEU B CD1 
1395 C CD2 . LEU A 192 ? 0.9102 0.9102 0.9102 0.0000 0.0000 0.0000 175 LEU B CD2 
1396 N N   . THR A 193 ? 0.8984 0.8984 0.8984 0.0000 0.0000 0.0000 176 THR B N   
1397 C CA  . THR A 193 ? 0.8984 0.8984 0.8984 0.0000 0.0000 0.0000 176 THR B CA  
1398 C C   . THR A 193 ? 0.8984 0.8984 0.8984 0.0000 0.0000 0.0000 176 THR B C   
1399 O O   . THR A 193 ? 0.8984 0.8984 0.8984 0.0000 0.0000 0.0000 176 THR B O   
1400 C CB  . THR A 193 ? 0.8984 0.8984 0.8984 0.0000 0.0000 0.0000 176 THR B CB  
1401 O OG1 . THR A 193 ? 0.8984 0.8984 0.8984 0.0000 0.0000 0.0000 176 THR B OG1 
1402 C CG2 . THR A 193 ? 0.8984 0.8984 0.8984 0.0000 0.0000 0.0000 176 THR B CG2 
1403 N N   . ARG A 194 ? 0.9453 0.9453 0.9453 0.0000 0.0000 0.0000 177 ARG B N   
1404 C CA  . ARG A 194 ? 0.9453 0.9453 0.9453 0.0000 0.0000 0.0000 177 ARG B CA  
1405 C C   . ARG A 194 ? 0.9453 0.9453 0.9453 0.0000 0.0000 0.0000 177 ARG B C   
1406 O O   . ARG A 194 ? 0.9453 0.9453 0.9453 0.0000 0.0000 0.0000 177 ARG B O   
1407 C CB  . ARG A 194 ? 0.9453 0.9453 0.9453 0.0000 0.0000 0.0000 177 ARG B CB  
1408 C CG  . ARG A 194 ? 0.9453 0.9453 0.9453 0.0000 0.0000 0.0000 177 ARG B CG  
1409 C CD  . ARG A 194 ? 0.9453 0.9453 0.9453 0.0000 0.0000 0.0000 177 ARG B CD  
1410 N NE  . ARG A 194 ? 0.9453 0.9453 0.9453 0.0000 0.0000 0.0000 177 ARG B NE  
1411 C CZ  . ARG A 194 ? 0.9453 0.9453 0.9453 0.0000 0.0000 0.0000 177 ARG B CZ  
1412 N NH1 . ARG A 194 ? 0.9453 0.9453 0.9453 0.0000 0.0000 0.0000 177 ARG B NH1 
1413 N NH2 . ARG A 194 ? 0.9453 0.9453 0.9453 0.0000 0.0000 0.0000 177 ARG B NH2 
1414 N N   . ASN A 195 ? 0.8936 0.8936 0.8936 0.0000 0.0000 0.0000 178 ASN B N   
1415 C CA  . ASN A 195 ? 0.8936 0.8936 0.8936 0.0000 0.0000 0.0000 178 ASN B CA  
1416 C C   . ASN A 195 ? 0.8936 0.8936 0.8936 0.0000 0.0000 0.0000 178 ASN B C   
1417 O O   . ASN A 195 ? 0.8936 0.8936 0.8936 0.0000 0.0000 0.0000 178 ASN B O   
1418 C CB  . ASN A 195 ? 0.8936 0.8936 0.8936 0.0000 0.0000 0.0000 178 ASN B CB  
1419 C CG  . ASN A 195 ? 0.8936 0.8936 0.8936 0.0000 0.0000 0.0000 178 ASN B CG  
1420 O OD1 . ASN A 195 ? 0.8936 0.8936 0.8936 0.0000 0.0000 0.0000 178 ASN B OD1 
1421 N ND2 . ASN A 195 ? 0.8936 0.8936 0.8936 0.0000 0.0000 0.0000 178 ASN B ND2 
1422 N N   . GLY A 196 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 179 GLY B N   
1423 C CA  . GLY A 196 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 179 GLY B CA  
1424 C C   . GLY A 196 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 179 GLY B C   
1425 O O   . GLY A 196 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 179 GLY B O   
1426 N N   . TYR A 197 ? 0.8915 0.8915 0.8915 0.0000 0.0000 0.0000 180 TYR B N   
1427 C CA  . TYR A 197 ? 0.8915 0.8915 0.8915 0.0000 0.0000 0.0000 180 TYR B CA  
1428 C C   . TYR A 197 ? 0.8915 0.8915 0.8915 0.0000 0.0000 0.0000 180 TYR B C   
1429 O O   . TYR A 197 ? 0.8915 0.8915 0.8915 0.0000 0.0000 0.0000 180 TYR B O   
1430 C CB  . TYR A 197 ? 0.8915 0.8915 0.8915 0.0000 0.0000 0.0000 180 TYR B CB  
1431 C CG  . TYR A 197 ? 0.8915 0.8915 0.8915 0.0000 0.0000 0.0000 180 TYR B CG  
1432 C CD1 . TYR A 197 ? 0.8915 0.8915 0.8915 0.0000 0.0000 0.0000 180 TYR B CD1 
1433 C CD2 . TYR A 197 ? 0.8915 0.8915 0.8915 0.0000 0.0000 0.0000 180 TYR B CD2 
1434 C CE1 . TYR A 197 ? 0.8915 0.8915 0.8915 0.0000 0.0000 0.0000 180 TYR B CE1 
1435 C CE2 . TYR A 197 ? 0.8915 0.8915 0.8915 0.0000 0.0000 0.0000 180 TYR B CE2 
1436 C CZ  . TYR A 197 ? 0.8915 0.8915 0.8915 0.0000 0.0000 0.0000 180 TYR B CZ  
1437 O OH  . TYR A 197 ? 0.8915 0.8915 0.8915 0.0000 0.0000 0.0000 180 TYR B OH  
1438 N N   . GLY A 198 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 181 GLY B N   
1439 C CA  . GLY A 198 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 181 GLY B CA  
1440 C C   . GLY A 198 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 181 GLY B C   
1441 O O   . GLY A 198 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 181 GLY B O   
1442 N N   . SER A 199 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 182 SER B N   
1443 C CA  . SER A 199 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 182 SER B CA  
1444 C C   . SER A 199 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 182 SER B C   
1445 O O   . SER A 199 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 182 SER B O   
1446 C CB  . SER A 199 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 182 SER B CB  
1447 O OG  . SER A 199 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 182 SER B OG  
1448 N N   . THR A 200 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 183 THR B N   
1449 C CA  . THR A 200 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 183 THR B CA  
1450 C C   . THR A 200 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 183 THR B C   
1451 O O   . THR A 200 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 183 THR B O   
1452 C CB  . THR A 200 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 183 THR B CB  
1453 O OG1 . THR A 200 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 183 THR B OG1 
1454 C CG2 . THR A 200 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 183 THR B CG2 
1455 N N   . GLN A 201 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 184 GLN B N   
1456 C CA  . GLN A 201 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 184 GLN B CA  
1457 C C   . GLN A 201 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 184 GLN B C   
1458 O O   . GLN A 201 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 184 GLN B O   
1459 C CB  . GLN A 201 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 184 GLN B CB  
1460 C CG  . GLN A 201 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 184 GLN B CG  
1461 C CD  . GLN A 201 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 184 GLN B CD  
1462 O OE1 . GLN A 201 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 184 GLN B OE1 
1463 N NE2 . GLN A 201 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 184 GLN B NE2 
1464 N N   . TYR A 202 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 185 TYR B N   
1465 C CA  . TYR A 202 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 185 TYR B CA  
1466 C C   . TYR A 202 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 185 TYR B C   
1467 O O   . TYR A 202 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 185 TYR B O   
1468 C CB  . TYR A 202 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 185 TYR B CB  
1469 C CG  . TYR A 202 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 185 TYR B CG  
1470 C CD1 . TYR A 202 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 185 TYR B CD1 
1471 C CD2 . TYR A 202 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 185 TYR B CD2 
1472 C CE1 . TYR A 202 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 185 TYR B CE1 
1473 C CE2 . TYR A 202 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 185 TYR B CE2 
1474 C CZ  . TYR A 202 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 185 TYR B CZ  
1475 O OH  . TYR A 202 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 185 TYR B OH  
1476 N N   . ILE A 203 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 186 ILE B N   
1477 C CA  . ILE A 203 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 186 ILE B CA  
1478 C C   . ILE A 203 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 186 ILE B C   
1479 O O   . ILE A 203 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 186 ILE B O   
1480 C CB  . ILE A 203 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 186 ILE B CB  
1481 C CG1 . ILE A 203 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 186 ILE B CG1 
1482 C CG2 . ILE A 203 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 186 ILE B CG2 
1483 C CD1 . ILE A 203 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 186 ILE B CD1 
1484 N N   . ARG A 204 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 187 ARG B N   
1485 C CA  . ARG A 204 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 187 ARG B CA  
1486 C C   . ARG A 204 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 187 ARG B C   
1487 O O   . ARG A 204 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 187 ARG B O   
1488 C CB  . ARG A 204 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 187 ARG B CB  
1489 C CG  . ARG A 204 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 187 ARG B CG  
1490 C CD  . ARG A 204 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 187 ARG B CD  
1491 N NE  . ARG A 204 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 187 ARG B NE  
1492 C CZ  . ARG A 204 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 187 ARG B CZ  
1493 N NH1 . ARG A 204 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 187 ARG B NH1 
1494 N NH2 . ARG A 204 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 187 ARG B NH2 
1495 N N   . PHE A 205 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 188 PHE B N   
1496 C CA  . PHE A 205 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 188 PHE B CA  
1497 C C   . PHE A 205 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 188 PHE B C   
1498 O O   . PHE A 205 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 188 PHE B O   
1499 C CB  . PHE A 205 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 188 PHE B CB  
1500 C CG  . PHE A 205 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 188 PHE B CG  
1501 C CD1 . PHE A 205 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 188 PHE B CD1 
1502 C CD2 . PHE A 205 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 188 PHE B CD2 
1503 C CE1 . PHE A 205 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 188 PHE B CE1 
1504 C CE2 . PHE A 205 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 188 PHE B CE2 
1505 C CZ  . PHE A 205 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 188 PHE B CZ  
1506 N N   . SER A 206 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 189 SER B N   
1507 C CA  . SER A 206 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 189 SER B CA  
1508 C C   . SER A 206 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 189 SER B C   
1509 O O   . SER A 206 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 189 SER B O   
1510 C CB  . SER A 206 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 189 SER B CB  
1511 O OG  . SER A 206 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 189 SER B OG  
1512 N N   . PRO A 207 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 190 PRO B N   
1513 C CA  . PRO A 207 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 190 PRO B CA  
1514 C C   . PRO A 207 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 190 PRO B C   
1515 O O   . PRO A 207 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 190 PRO B O   
1516 C CB  . PRO A 207 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 190 PRO B CB  
1517 C CG  . PRO A 207 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 190 PRO B CG  
1518 C CD  . PRO A 207 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 190 PRO B CD  
1519 N N   . ASP A 208 ? 0.9161 0.9161 0.9161 0.0000 0.0000 0.0000 191 ASP B N   
1520 C CA  . ASP A 208 ? 0.9161 0.9161 0.9161 0.0000 0.0000 0.0000 191 ASP B CA  
1521 C C   . ASP A 208 ? 0.9161 0.9161 0.9161 0.0000 0.0000 0.0000 191 ASP B C   
1522 O O   . ASP A 208 ? 0.9161 0.9161 0.9161 0.0000 0.0000 0.0000 191 ASP B O   
1523 C CB  . ASP A 208 ? 0.9161 0.9161 0.9161 0.0000 0.0000 0.0000 191 ASP B CB  
1524 C CG  . ASP A 208 ? 0.9161 0.9161 0.9161 0.0000 0.0000 0.0000 191 ASP B CG  
1525 O OD1 . ASP A 208 ? 0.9161 0.9161 0.9161 0.0000 0.0000 0.0000 191 ASP B OD1 
1526 O OD2 . ASP A 208 ? 0.9161 0.9161 0.9161 0.0000 0.0000 0.0000 191 ASP B OD2 
1527 N N   . PHE A 209 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 192 PHE B N   
1528 C CA  . PHE A 209 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 192 PHE B CA  
1529 C C   . PHE A 209 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 192 PHE B C   
1530 O O   . PHE A 209 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 192 PHE B O   
1531 C CB  . PHE A 209 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 192 PHE B CB  
1532 C CG  . PHE A 209 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 192 PHE B CG  
1533 C CD1 . PHE A 209 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 192 PHE B CD1 
1534 C CD2 . PHE A 209 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 192 PHE B CD2 
1535 C CE1 . PHE A 209 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 192 PHE B CE1 
1536 C CE2 . PHE A 209 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 192 PHE B CE2 
1537 C CZ  . PHE A 209 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 192 PHE B CZ  
1538 N N   . THR A 210 ? 0.8856 0.8856 0.8856 0.0000 0.0000 0.0000 193 THR B N   
1539 C CA  . THR A 210 ? 0.8856 0.8856 0.8856 0.0000 0.0000 0.0000 193 THR B CA  
1540 C C   . THR A 210 ? 0.8856 0.8856 0.8856 0.0000 0.0000 0.0000 193 THR B C   
1541 O O   . THR A 210 ? 0.8856 0.8856 0.8856 0.0000 0.0000 0.0000 193 THR B O   
1542 C CB  . THR A 210 ? 0.8856 0.8856 0.8856 0.0000 0.0000 0.0000 193 THR B CB  
1543 O OG1 . THR A 210 ? 0.8856 0.8856 0.8856 0.0000 0.0000 0.0000 193 THR B OG1 
1544 C CG2 . THR A 210 ? 0.8856 0.8856 0.8856 0.0000 0.0000 0.0000 193 THR B CG2 
1545 N N   . PHE A 211 ? 0.9289 0.9289 0.9289 0.0000 0.0000 0.0000 194 PHE B N   
1546 C CA  . PHE A 211 ? 0.9289 0.9289 0.9289 0.0000 0.0000 0.0000 194 PHE B CA  
1547 C C   . PHE A 211 ? 0.9289 0.9289 0.9289 0.0000 0.0000 0.0000 194 PHE B C   
1548 O O   . PHE A 211 ? 0.9289 0.9289 0.9289 0.0000 0.0000 0.0000 194 PHE B O   
1549 C CB  . PHE A 211 ? 0.9289 0.9289 0.9289 0.0000 0.0000 0.0000 194 PHE B CB  
1550 C CG  . PHE A 211 ? 0.9289 0.9289 0.9289 0.0000 0.0000 0.0000 194 PHE B CG  
1551 C CD1 . PHE A 211 ? 0.9289 0.9289 0.9289 0.0000 0.0000 0.0000 194 PHE B CD1 
1552 C CD2 . PHE A 211 ? 0.9289 0.9289 0.9289 0.0000 0.0000 0.0000 194 PHE B CD2 
1553 C CE1 . PHE A 211 ? 0.9289 0.9289 0.9289 0.0000 0.0000 0.0000 194 PHE B CE1 
1554 C CE2 . PHE A 211 ? 0.9289 0.9289 0.9289 0.0000 0.0000 0.0000 194 PHE B CE2 
1555 C CZ  . PHE A 211 ? 0.9289 0.9289 0.9289 0.0000 0.0000 0.0000 194 PHE B CZ  
1556 N N   . GLY A 212 ? 1.0182 1.0182 1.0182 0.0000 0.0000 0.0000 195 GLY B N   
1557 C CA  . GLY A 212 ? 1.0182 1.0182 1.0182 0.0000 0.0000 0.0000 195 GLY B CA  
1558 C C   . GLY A 212 ? 1.0182 1.0182 1.0182 0.0000 0.0000 0.0000 195 GLY B C   
1559 O O   . GLY A 212 ? 1.0182 1.0182 1.0182 0.0000 0.0000 0.0000 195 GLY B O   
1560 N N   . PHE A 213 ? 1.0258 1.0258 1.0258 0.0000 0.0000 0.0000 196 PHE B N   
1561 C CA  . PHE A 213 ? 1.0258 1.0258 1.0258 0.0000 0.0000 0.0000 196 PHE B CA  
1562 C C   . PHE A 213 ? 1.0258 1.0258 1.0258 0.0000 0.0000 0.0000 196 PHE B C   
1563 O O   . PHE A 213 ? 1.0258 1.0258 1.0258 0.0000 0.0000 0.0000 196 PHE B O   
1564 C CB  . PHE A 213 ? 1.0258 1.0258 1.0258 0.0000 0.0000 0.0000 196 PHE B CB  
1565 C CG  . PHE A 213 ? 1.0258 1.0258 1.0258 0.0000 0.0000 0.0000 196 PHE B CG  
1566 C CD1 . PHE A 213 ? 1.0258 1.0258 1.0258 0.0000 0.0000 0.0000 196 PHE B CD1 
1567 C CD2 . PHE A 213 ? 1.0258 1.0258 1.0258 0.0000 0.0000 0.0000 196 PHE B CD2 
1568 C CE1 . PHE A 213 ? 1.0258 1.0258 1.0258 0.0000 0.0000 0.0000 196 PHE B CE1 
1569 C CE2 . PHE A 213 ? 1.0258 1.0258 1.0258 0.0000 0.0000 0.0000 196 PHE B CE2 
1570 C CZ  . PHE A 213 ? 1.0258 1.0258 1.0258 0.0000 0.0000 0.0000 196 PHE B CZ  
1571 N N   . GLU A 214 ? 1.2296 1.2296 1.2296 0.0000 0.0000 0.0000 197 GLU B N   
1572 C CA  . GLU A 214 ? 1.2296 1.2296 1.2296 0.0000 0.0000 0.0000 197 GLU B CA  
1573 C C   . GLU A 214 ? 1.2296 1.2296 1.2296 0.0000 0.0000 0.0000 197 GLU B C   
1574 O O   . GLU A 214 ? 1.2296 1.2296 1.2296 0.0000 0.0000 0.0000 197 GLU B O   
1575 C CB  . GLU A 214 ? 1.2296 1.2296 1.2296 0.0000 0.0000 0.0000 197 GLU B CB  
1576 C CG  . GLU A 214 ? 1.2296 1.2296 1.2296 0.0000 0.0000 0.0000 197 GLU B CG  
1577 C CD  . GLU A 214 ? 1.2296 1.2296 1.2296 0.0000 0.0000 0.0000 197 GLU B CD  
1578 O OE1 . GLU A 214 ? 1.2296 1.2296 1.2296 0.0000 0.0000 0.0000 197 GLU B OE1 
1579 O OE2 . GLU A 214 ? 1.2296 1.2296 1.2296 0.0000 0.0000 0.0000 197 GLU B OE2 
1580 N N   . GLU A 215 ? 1.3834 1.3834 1.3834 0.0000 0.0000 0.0000 198 GLU B N   
1581 C CA  . GLU A 215 ? 1.3834 1.3834 1.3834 0.0000 0.0000 0.0000 198 GLU B CA  
1582 C C   . GLU A 215 ? 1.3834 1.3834 1.3834 0.0000 0.0000 0.0000 198 GLU B C   
1583 O O   . GLU A 215 ? 1.3834 1.3834 1.3834 0.0000 0.0000 0.0000 198 GLU B O   
1584 C CB  . GLU A 215 ? 1.3834 1.3834 1.3834 0.0000 0.0000 0.0000 198 GLU B CB  
1585 C CG  . GLU A 215 ? 1.3834 1.3834 1.3834 0.0000 0.0000 0.0000 198 GLU B CG  
1586 C CD  . GLU A 215 ? 1.3834 1.3834 1.3834 0.0000 0.0000 0.0000 198 GLU B CD  
1587 O OE1 . GLU A 215 ? 1.3834 1.3834 1.3834 0.0000 0.0000 0.0000 198 GLU B OE1 
1588 O OE2 . GLU A 215 ? 1.3834 1.3834 1.3834 0.0000 0.0000 0.0000 198 GLU B OE2 
1589 N N   . SER A 216 ? 1.4004 1.4004 1.4004 0.0000 0.0000 0.0000 199 SER B N   
1590 C CA  . SER A 216 ? 1.4004 1.4004 1.4004 0.0000 0.0000 0.0000 199 SER B CA  
1591 C C   . SER A 216 ? 1.4004 1.4004 1.4004 0.0000 0.0000 0.0000 199 SER B C   
1592 O O   . SER A 216 ? 1.4004 1.4004 1.4004 0.0000 0.0000 0.0000 199 SER B O   
1593 C CB  . SER A 216 ? 1.4004 1.4004 1.4004 0.0000 0.0000 0.0000 199 SER B CB  
1594 O OG  . SER A 216 ? 1.4004 1.4004 1.4004 0.0000 0.0000 0.0000 199 SER B OG  
1595 N N   . LEU A 217 ? 1.5195 1.5195 1.5195 0.0000 0.0000 0.0000 200 LEU B N   
1596 C CA  . LEU A 217 ? 1.5195 1.5195 1.5195 0.0000 0.0000 0.0000 200 LEU B CA  
1597 C C   . LEU A 217 ? 1.5195 1.5195 1.5195 0.0000 0.0000 0.0000 200 LEU B C   
1598 O O   . LEU A 217 ? 1.5195 1.5195 1.5195 0.0000 0.0000 0.0000 200 LEU B O   
1599 C CB  . LEU A 217 ? 1.5195 1.5195 1.5195 0.0000 0.0000 0.0000 200 LEU B CB  
1600 C CG  . LEU A 217 ? 1.5195 1.5195 1.5195 0.0000 0.0000 0.0000 200 LEU B CG  
1601 C CD1 . LEU A 217 ? 1.5195 1.5195 1.5195 0.0000 0.0000 0.0000 200 LEU B CD1 
1602 C CD2 . LEU A 217 ? 1.5195 1.5195 1.5195 0.0000 0.0000 0.0000 200 LEU B CD2 
1603 N N   . GLU A 218 ? 1.7694 1.7694 1.7694 0.0000 0.0000 0.0000 201 GLU B N   
1604 C CA  . GLU A 218 ? 1.7694 1.7694 1.7694 0.0000 0.0000 0.0000 201 GLU B CA  
1605 C C   . GLU A 218 ? 1.7694 1.7694 1.7694 0.0000 0.0000 0.0000 201 GLU B C   
1606 O O   . GLU A 218 ? 1.7694 1.7694 1.7694 0.0000 0.0000 0.0000 201 GLU B O   
1607 C CB  . GLU A 218 ? 1.7694 1.7694 1.7694 0.0000 0.0000 0.0000 201 GLU B CB  
1608 C CG  . GLU A 218 ? 1.7694 1.7694 1.7694 0.0000 0.0000 0.0000 201 GLU B CG  
1609 C CD  . GLU A 218 ? 1.7694 1.7694 1.7694 0.0000 0.0000 0.0000 201 GLU B CD  
1610 O OE1 . GLU A 218 ? 1.7694 1.7694 1.7694 0.0000 0.0000 0.0000 201 GLU B OE1 
1611 O OE2 . GLU A 218 ? 1.7694 1.7694 1.7694 0.0000 0.0000 0.0000 201 GLU B OE2 
1612 N N   . VAL A 219 ? 1.8535 1.8535 1.8535 0.0000 0.0000 0.0000 202 VAL B N   
1613 C CA  . VAL A 219 ? 1.8535 1.8535 1.8535 0.0000 0.0000 0.0000 202 VAL B CA  
1614 C C   . VAL A 219 ? 1.8535 1.8535 1.8535 0.0000 0.0000 0.0000 202 VAL B C   
1615 O O   . VAL A 219 ? 1.8535 1.8535 1.8535 0.0000 0.0000 0.0000 202 VAL B O   
1616 C CB  . VAL A 219 ? 1.8535 1.8535 1.8535 0.0000 0.0000 0.0000 202 VAL B CB  
1617 C CG1 . VAL A 219 ? 1.8535 1.8535 1.8535 0.0000 0.0000 0.0000 202 VAL B CG1 
1618 C CG2 . VAL A 219 ? 1.8535 1.8535 1.8535 0.0000 0.0000 0.0000 202 VAL B CG2 
1619 N N   . ASP A 220 ? 1.9237 1.9237 1.9237 0.0000 0.0000 0.0000 203 ASP B N   
1620 C CA  . ASP A 220 ? 1.9237 1.9237 1.9237 0.0000 0.0000 0.0000 203 ASP B CA  
1621 C C   . ASP A 220 ? 1.9237 1.9237 1.9237 0.0000 0.0000 0.0000 203 ASP B C   
1622 O O   . ASP A 220 ? 1.9237 1.9237 1.9237 0.0000 0.0000 0.0000 203 ASP B O   
1623 C CB  . ASP A 220 ? 1.9237 1.9237 1.9237 0.0000 0.0000 0.0000 203 ASP B CB  
1624 C CG  . ASP A 220 ? 1.9237 1.9237 1.9237 0.0000 0.0000 0.0000 203 ASP B CG  
1625 O OD1 . ASP A 220 ? 1.9237 1.9237 1.9237 0.0000 0.0000 0.0000 203 ASP B OD1 
1626 O OD2 . ASP A 220 ? 1.9237 1.9237 1.9237 0.0000 0.0000 0.0000 203 ASP B OD2 
1627 N N   . THR A 221 ? 1.9423 1.9423 1.9423 0.0000 0.0000 0.0000 204 THR B N   
1628 C CA  . THR A 221 ? 1.9423 1.9423 1.9423 0.0000 0.0000 0.0000 204 THR B CA  
1629 C C   . THR A 221 ? 1.9423 1.9423 1.9423 0.0000 0.0000 0.0000 204 THR B C   
1630 O O   . THR A 221 ? 1.9423 1.9423 1.9423 0.0000 0.0000 0.0000 204 THR B O   
1631 C CB  . THR A 221 ? 1.9423 1.9423 1.9423 0.0000 0.0000 0.0000 204 THR B CB  
1632 O OG1 . THR A 221 ? 1.9423 1.9423 1.9423 0.0000 0.0000 0.0000 204 THR B OG1 
1633 C CG2 . THR A 221 ? 1.9423 1.9423 1.9423 0.0000 0.0000 0.0000 204 THR B CG2 
1634 N N   . ASN A 222 ? 1.8508 1.8508 1.8508 0.0000 0.0000 0.0000 205 ASN B N   
1635 C CA  . ASN A 222 ? 1.8508 1.8508 1.8508 0.0000 0.0000 0.0000 205 ASN B CA  
1636 C C   . ASN A 222 ? 1.8508 1.8508 1.8508 0.0000 0.0000 0.0000 205 ASN B C   
1637 O O   . ASN A 222 ? 1.8508 1.8508 1.8508 0.0000 0.0000 0.0000 205 ASN B O   
1638 C CB  . ASN A 222 ? 1.8508 1.8508 1.8508 0.0000 0.0000 0.0000 205 ASN B CB  
1639 C CG  . ASN A 222 ? 1.8508 1.8508 1.8508 0.0000 0.0000 0.0000 205 ASN B CG  
1640 O OD1 . ASN A 222 ? 1.8508 1.8508 1.8508 0.0000 0.0000 0.0000 205 ASN B OD1 
1641 N ND2 . ASN A 222 ? 1.8508 1.8508 1.8508 0.0000 0.0000 0.0000 205 ASN B ND2 
1642 N N   . PRO A 223 ? 1.8759 1.8759 1.8759 0.0000 0.0000 0.0000 206 PRO B N   
1643 C CA  . PRO A 223 ? 1.8759 1.8759 1.8759 0.0000 0.0000 0.0000 206 PRO B CA  
1644 C C   . PRO A 223 ? 1.8759 1.8759 1.8759 0.0000 0.0000 0.0000 206 PRO B C   
1645 O O   . PRO A 223 ? 1.8759 1.8759 1.8759 0.0000 0.0000 0.0000 206 PRO B O   
1646 C CB  . PRO A 223 ? 1.8759 1.8759 1.8759 0.0000 0.0000 0.0000 206 PRO B CB  
1647 C CG  . PRO A 223 ? 1.8759 1.8759 1.8759 0.0000 0.0000 0.0000 206 PRO B CG  
1648 C CD  . PRO A 223 ? 1.8759 1.8759 1.8759 0.0000 0.0000 0.0000 206 PRO B CD  
1649 N N   . LEU A 224 ? 1.8175 1.8175 1.8175 0.0000 0.0000 0.0000 207 LEU B N   
1650 C CA  . LEU A 224 ? 1.8175 1.8175 1.8175 0.0000 0.0000 0.0000 207 LEU B CA  
1651 C C   . LEU A 224 ? 1.8175 1.8175 1.8175 0.0000 0.0000 0.0000 207 LEU B C   
1652 O O   . LEU A 224 ? 1.8175 1.8175 1.8175 0.0000 0.0000 0.0000 207 LEU B O   
1653 C CB  . LEU A 224 ? 1.8175 1.8175 1.8175 0.0000 0.0000 0.0000 207 LEU B CB  
1654 C CG  . LEU A 224 ? 1.8175 1.8175 1.8175 0.0000 0.0000 0.0000 207 LEU B CG  
1655 C CD1 . LEU A 224 ? 1.8175 1.8175 1.8175 0.0000 0.0000 0.0000 207 LEU B CD1 
1656 C CD2 . LEU A 224 ? 1.8175 1.8175 1.8175 0.0000 0.0000 0.0000 207 LEU B CD2 
1657 N N   . LEU A 225 ? 1.7755 1.7755 1.7755 0.0000 0.0000 0.0000 208 LEU B N   
1658 C CA  . LEU A 225 ? 1.7755 1.7755 1.7755 0.0000 0.0000 0.0000 208 LEU B CA  
1659 C C   . LEU A 225 ? 1.7755 1.7755 1.7755 0.0000 0.0000 0.0000 208 LEU B C   
1660 O O   . LEU A 225 ? 1.7755 1.7755 1.7755 0.0000 0.0000 0.0000 208 LEU B O   
1661 C CB  . LEU A 225 ? 1.7755 1.7755 1.7755 0.0000 0.0000 0.0000 208 LEU B CB  
1662 C CG  . LEU A 225 ? 1.7755 1.7755 1.7755 0.0000 0.0000 0.0000 208 LEU B CG  
1663 C CD1 . LEU A 225 ? 1.7755 1.7755 1.7755 0.0000 0.0000 0.0000 208 LEU B CD1 
1664 C CD2 . LEU A 225 ? 1.7755 1.7755 1.7755 0.0000 0.0000 0.0000 208 LEU B CD2 
1665 N N   . GLY A 226 ? 1.7490 1.7490 1.7490 0.0000 0.0000 0.0000 209 GLY B N   
1666 C CA  . GLY A 226 ? 1.7490 1.7490 1.7490 0.0000 0.0000 0.0000 209 GLY B CA  
1667 C C   . GLY A 226 ? 1.7490 1.7490 1.7490 0.0000 0.0000 0.0000 209 GLY B C   
1668 O O   . GLY A 226 ? 1.7490 1.7490 1.7490 0.0000 0.0000 0.0000 209 GLY B O   
1669 N N   . ALA A 227 ? 1.5627 1.5627 1.5627 0.0000 0.0000 0.0000 210 ALA B N   
1670 C CA  . ALA A 227 ? 1.5627 1.5627 1.5627 0.0000 0.0000 0.0000 210 ALA B CA  
1671 C C   . ALA A 227 ? 1.5627 1.5627 1.5627 0.0000 0.0000 0.0000 210 ALA B C   
1672 O O   . ALA A 227 ? 1.5627 1.5627 1.5627 0.0000 0.0000 0.0000 210 ALA B O   
1673 C CB  . ALA A 227 ? 1.5627 1.5627 1.5627 0.0000 0.0000 0.0000 210 ALA B CB  
1674 N N   . GLY A 228 ? 1.3334 1.3334 1.3334 0.0000 0.0000 0.0000 211 GLY B N   
1675 C CA  . GLY A 228 ? 1.3334 1.3334 1.3334 0.0000 0.0000 0.0000 211 GLY B CA  
1676 C C   . GLY A 228 ? 1.3334 1.3334 1.3334 0.0000 0.0000 0.0000 211 GLY B C   
1677 O O   . GLY A 228 ? 1.3334 1.3334 1.3334 0.0000 0.0000 0.0000 211 GLY B O   
1678 N N   . LYS A 229 ? 1.2006 1.2006 1.2006 0.0000 0.0000 0.0000 212 LYS B N   
1679 C CA  . LYS A 229 ? 1.2006 1.2006 1.2006 0.0000 0.0000 0.0000 212 LYS B CA  
1680 C C   . LYS A 229 ? 1.2006 1.2006 1.2006 0.0000 0.0000 0.0000 212 LYS B C   
1681 O O   . LYS A 229 ? 1.2006 1.2006 1.2006 0.0000 0.0000 0.0000 212 LYS B O   
1682 C CB  . LYS A 229 ? 1.2006 1.2006 1.2006 0.0000 0.0000 0.0000 212 LYS B CB  
1683 C CG  . LYS A 229 ? 1.2006 1.2006 1.2006 0.0000 0.0000 0.0000 212 LYS B CG  
1684 C CD  . LYS A 229 ? 1.2006 1.2006 1.2006 0.0000 0.0000 0.0000 212 LYS B CD  
1685 C CE  . LYS A 229 ? 1.2006 1.2006 1.2006 0.0000 0.0000 0.0000 212 LYS B CE  
1686 N NZ  . LYS A 229 ? 1.2006 1.2006 1.2006 0.0000 0.0000 0.0000 212 LYS B NZ  
1687 N N   . PHE A 230 ? 1.1656 1.1656 1.1656 0.0000 0.0000 0.0000 213 PHE B N   
1688 C CA  . PHE A 230 ? 1.1656 1.1656 1.1656 0.0000 0.0000 0.0000 213 PHE B CA  
1689 C C   . PHE A 230 ? 1.1656 1.1656 1.1656 0.0000 0.0000 0.0000 213 PHE B C   
1690 O O   . PHE A 230 ? 1.1656 1.1656 1.1656 0.0000 0.0000 0.0000 213 PHE B O   
1691 C CB  . PHE A 230 ? 1.1656 1.1656 1.1656 0.0000 0.0000 0.0000 213 PHE B CB  
1692 C CG  . PHE A 230 ? 1.1656 1.1656 1.1656 0.0000 0.0000 0.0000 213 PHE B CG  
1693 C CD1 . PHE A 230 ? 1.1656 1.1656 1.1656 0.0000 0.0000 0.0000 213 PHE B CD1 
1694 C CD2 . PHE A 230 ? 1.1656 1.1656 1.1656 0.0000 0.0000 0.0000 213 PHE B CD2 
1695 C CE1 . PHE A 230 ? 1.1656 1.1656 1.1656 0.0000 0.0000 0.0000 213 PHE B CE1 
1696 C CE2 . PHE A 230 ? 1.1656 1.1656 1.1656 0.0000 0.0000 0.0000 213 PHE B CE2 
1697 C CZ  . PHE A 230 ? 1.1656 1.1656 1.1656 0.0000 0.0000 0.0000 213 PHE B CZ  
1698 N N   . ALA A 231 ? 1.0515 1.0515 1.0515 0.0000 0.0000 0.0000 214 ALA B N   
1699 C CA  . ALA A 231 ? 1.0515 1.0515 1.0515 0.0000 0.0000 0.0000 214 ALA B CA  
1700 C C   . ALA A 231 ? 1.0515 1.0515 1.0515 0.0000 0.0000 0.0000 214 ALA B C   
1701 O O   . ALA A 231 ? 1.0515 1.0515 1.0515 0.0000 0.0000 0.0000 214 ALA B O   
1702 C CB  . ALA A 231 ? 1.0515 1.0515 1.0515 0.0000 0.0000 0.0000 214 ALA B CB  
1703 N N   . THR A 232 ? 0.9882 0.9882 0.9882 0.0000 0.0000 0.0000 215 THR B N   
1704 C CA  . THR A 232 ? 0.9882 0.9882 0.9882 0.0000 0.0000 0.0000 215 THR B CA  
1705 C C   . THR A 232 ? 0.9882 0.9882 0.9882 0.0000 0.0000 0.0000 215 THR B C   
1706 O O   . THR A 232 ? 0.9882 0.9882 0.9882 0.0000 0.0000 0.0000 215 THR B O   
1707 C CB  . THR A 232 ? 0.9882 0.9882 0.9882 0.0000 0.0000 0.0000 215 THR B CB  
1708 O OG1 . THR A 232 ? 0.9882 0.9882 0.9882 0.0000 0.0000 0.0000 215 THR B OG1 
1709 C CG2 . THR A 232 ? 0.9882 0.9882 0.9882 0.0000 0.0000 0.0000 215 THR B CG2 
1710 N N   . ASP A 233 ? 0.9710 0.9710 0.9710 0.0000 0.0000 0.0000 216 ASP B N   
1711 C CA  . ASP A 233 ? 0.9710 0.9710 0.9710 0.0000 0.0000 0.0000 216 ASP B CA  
1712 C C   . ASP A 233 ? 0.9710 0.9710 0.9710 0.0000 0.0000 0.0000 216 ASP B C   
1713 O O   . ASP A 233 ? 0.9710 0.9710 0.9710 0.0000 0.0000 0.0000 216 ASP B O   
1714 C CB  . ASP A 233 ? 0.9710 0.9710 0.9710 0.0000 0.0000 0.0000 216 ASP B CB  
1715 C CG  . ASP A 233 ? 0.9710 0.9710 0.9710 0.0000 0.0000 0.0000 216 ASP B CG  
1716 O OD1 . ASP A 233 ? 0.9710 0.9710 0.9710 0.0000 0.0000 0.0000 216 ASP B OD1 
1717 O OD2 . ASP A 233 ? 0.9710 0.9710 0.9710 0.0000 0.0000 0.0000 216 ASP B OD2 
1718 N N   . PRO A 234 ? 0.9128 0.9128 0.9128 0.0000 0.0000 0.0000 217 PRO B N   
1719 C CA  . PRO A 234 ? 0.9128 0.9128 0.9128 0.0000 0.0000 0.0000 217 PRO B CA  
1720 C C   . PRO A 234 ? 0.9128 0.9128 0.9128 0.0000 0.0000 0.0000 217 PRO B C   
1721 O O   . PRO A 234 ? 0.9128 0.9128 0.9128 0.0000 0.0000 0.0000 217 PRO B O   
1722 C CB  . PRO A 234 ? 0.9128 0.9128 0.9128 0.0000 0.0000 0.0000 217 PRO B CB  
1723 C CG  . PRO A 234 ? 0.9128 0.9128 0.9128 0.0000 0.0000 0.0000 217 PRO B CG  
1724 C CD  . PRO A 234 ? 0.9128 0.9128 0.9128 0.0000 0.0000 0.0000 217 PRO B CD  
1725 N N   . ALA A 235 ? 0.8822 0.8822 0.8822 0.0000 0.0000 0.0000 218 ALA B N   
1726 C CA  . ALA A 235 ? 0.8822 0.8822 0.8822 0.0000 0.0000 0.0000 218 ALA B CA  
1727 C C   . ALA A 235 ? 0.8822 0.8822 0.8822 0.0000 0.0000 0.0000 218 ALA B C   
1728 O O   . ALA A 235 ? 0.8822 0.8822 0.8822 0.0000 0.0000 0.0000 218 ALA B O   
1729 C CB  . ALA A 235 ? 0.8822 0.8822 0.8822 0.0000 0.0000 0.0000 218 ALA B CB  
1730 N N   . VAL A 236 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 219 VAL B N   
1731 C CA  . VAL A 236 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 219 VAL B CA  
1732 C C   . VAL A 236 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 219 VAL B C   
1733 O O   . VAL A 236 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 219 VAL B O   
1734 C CB  . VAL A 236 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 219 VAL B CB  
1735 C CG1 . VAL A 236 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 219 VAL B CG1 
1736 C CG2 . VAL A 236 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 219 VAL B CG2 
1737 N N   . THR A 237 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 220 THR B N   
1738 C CA  . THR A 237 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 220 THR B CA  
1739 C C   . THR A 237 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 220 THR B C   
1740 O O   . THR A 237 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 220 THR B O   
1741 C CB  . THR A 237 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 220 THR B CB  
1742 O OG1 . THR A 237 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 220 THR B OG1 
1743 C CG2 . THR A 237 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 220 THR B CG2 
1744 N N   . LEU A 238 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 221 LEU B N   
1745 C CA  . LEU A 238 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 221 LEU B CA  
1746 C C   . LEU A 238 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 221 LEU B C   
1747 O O   . LEU A 238 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 221 LEU B O   
1748 C CB  . LEU A 238 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 221 LEU B CB  
1749 C CG  . LEU A 238 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 221 LEU B CG  
1750 C CD1 . LEU A 238 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 221 LEU B CD1 
1751 C CD2 . LEU A 238 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 221 LEU B CD2 
1752 N N   . ALA A 239 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 222 ALA B N   
1753 C CA  . ALA A 239 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 222 ALA B CA  
1754 C C   . ALA A 239 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 222 ALA B C   
1755 O O   . ALA A 239 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 222 ALA B O   
1756 C CB  . ALA A 239 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 222 ALA B CB  
1757 N N   . HIS A 240 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 223 HIS B N   
1758 C CA  . HIS A 240 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 223 HIS B CA  
1759 C C   . HIS A 240 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 223 HIS B C   
1760 O O   . HIS A 240 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 223 HIS B O   
1761 C CB  . HIS A 240 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 223 HIS B CB  
1762 C CG  . HIS A 240 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 223 HIS B CG  
1763 N ND1 . HIS A 240 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 223 HIS B ND1 
1764 C CD2 . HIS A 240 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 223 HIS B CD2 
1765 C CE1 . HIS A 240 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 223 HIS B CE1 
1766 N NE2 . HIS A 240 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 223 HIS B NE2 
1767 N N   . GLN A 241 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 224 GLN B N   
1768 C CA  . GLN A 241 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 224 GLN B CA  
1769 C C   . GLN A 241 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 224 GLN B C   
1770 O O   . GLN A 241 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 224 GLN B O   
1771 C CB  . GLN A 241 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 224 GLN B CB  
1772 C CG  . GLN A 241 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 224 GLN B CG  
1773 C CD  . GLN A 241 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 224 GLN B CD  
1774 O OE1 . GLN A 241 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 224 GLN B OE1 
1775 N NE2 . GLN A 241 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 224 GLN B NE2 
1776 N N   . LEU A 242 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 225 LEU B N   
1777 C CA  . LEU A 242 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 225 LEU B CA  
1778 C C   . LEU A 242 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 225 LEU B C   
1779 O O   . LEU A 242 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 225 LEU B O   
1780 C CB  . LEU A 242 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 225 LEU B CB  
1781 C CG  . LEU A 242 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 225 LEU B CG  
1782 C CD1 . LEU A 242 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 225 LEU B CD1 
1783 C CD2 . LEU A 242 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 225 LEU B CD2 
1784 N N   . ILE A 243 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 226 ILE B N   
1785 C CA  . ILE A 243 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 226 ILE B CA  
1786 C C   . ILE A 243 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 226 ILE B C   
1787 O O   . ILE A 243 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 226 ILE B O   
1788 C CB  . ILE A 243 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 226 ILE B CB  
1789 C CG1 . ILE A 243 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 226 ILE B CG1 
1790 C CG2 . ILE A 243 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 226 ILE B CG2 
1791 C CD1 . ILE A 243 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 226 ILE B CD1 
1792 N N   . HIS A 244 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 227 HIS B N   
1793 C CA  . HIS A 244 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 227 HIS B CA  
1794 C C   . HIS A 244 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 227 HIS B C   
1795 O O   . HIS A 244 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 227 HIS B O   
1796 C CB  . HIS A 244 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 227 HIS B CB  
1797 C CG  . HIS A 244 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 227 HIS B CG  
1798 N ND1 . HIS A 244 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 227 HIS B ND1 
1799 C CD2 . HIS A 244 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 227 HIS B CD2 
1800 C CE1 . HIS A 244 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 227 HIS B CE1 
1801 N NE2 . HIS A 244 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 227 HIS B NE2 
1802 N N   . ALA A 245 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 228 ALA B N   
1803 C CA  . ALA A 245 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 228 ALA B CA  
1804 C C   . ALA A 245 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 228 ALA B C   
1805 O O   . ALA A 245 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 228 ALA B O   
1806 C CB  . ALA A 245 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 228 ALA B CB  
1807 N N   . GLY A 246 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 229 GLY B N   
1808 C CA  . GLY A 246 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 229 GLY B CA  
1809 C C   . GLY A 246 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 229 GLY B C   
1810 O O   . GLY A 246 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 229 GLY B O   
1811 N N   . HIS A 247 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 230 HIS B N   
1812 C CA  . HIS A 247 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 230 HIS B CA  
1813 C C   . HIS A 247 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 230 HIS B C   
1814 O O   . HIS A 247 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 230 HIS B O   
1815 C CB  . HIS A 247 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 230 HIS B CB  
1816 C CG  . HIS A 247 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 230 HIS B CG  
1817 N ND1 . HIS A 247 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 230 HIS B ND1 
1818 C CD2 . HIS A 247 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 230 HIS B CD2 
1819 C CE1 . HIS A 247 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 230 HIS B CE1 
1820 N NE2 . HIS A 247 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 230 HIS B NE2 
1821 N N   . ARG A 248 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 231 ARG B N   
1822 C CA  . ARG A 248 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 231 ARG B CA  
1823 C C   . ARG A 248 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 231 ARG B C   
1824 O O   . ARG A 248 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 231 ARG B O   
1825 C CB  . ARG A 248 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 231 ARG B CB  
1826 C CG  . ARG A 248 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 231 ARG B CG  
1827 C CD  . ARG A 248 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 231 ARG B CD  
1828 N NE  . ARG A 248 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 231 ARG B NE  
1829 C CZ  . ARG A 248 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 231 ARG B CZ  
1830 N NH1 . ARG A 248 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 231 ARG B NH1 
1831 N NH2 . ARG A 248 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 231 ARG B NH2 
1832 N N   . LEU A 249 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 232 LEU B N   
1833 C CA  . LEU A 249 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 232 LEU B CA  
1834 C C   . LEU A 249 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 232 LEU B C   
1835 O O   . LEU A 249 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 232 LEU B O   
1836 C CB  . LEU A 249 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 232 LEU B CB  
1837 C CG  . LEU A 249 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 232 LEU B CG  
1838 C CD1 . LEU A 249 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 232 LEU B CD1 
1839 C CD2 . LEU A 249 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 232 LEU B CD2 
1840 N N   . TYR A 250 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 233 TYR B N   
1841 C CA  . TYR A 250 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 233 TYR B CA  
1842 C C   . TYR A 250 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 233 TYR B C   
1843 O O   . TYR A 250 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 233 TYR B O   
1844 C CB  . TYR A 250 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 233 TYR B CB  
1845 C CG  . TYR A 250 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 233 TYR B CG  
1846 C CD1 . TYR A 250 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 233 TYR B CD1 
1847 C CD2 . TYR A 250 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 233 TYR B CD2 
1848 C CE1 . TYR A 250 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 233 TYR B CE1 
1849 C CE2 . TYR A 250 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 233 TYR B CE2 
1850 C CZ  . TYR A 250 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 233 TYR B CZ  
1851 O OH  . TYR A 250 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 233 TYR B OH  
1852 N N   . GLY A 251 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 234 GLY B N   
1853 C CA  . GLY A 251 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 234 GLY B CA  
1854 C C   . GLY A 251 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 234 GLY B C   
1855 O O   . GLY A 251 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 234 GLY B O   
1856 N N   . ILE A 252 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 235 ILE B N   
1857 C CA  . ILE A 252 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 235 ILE B CA  
1858 C C   . ILE A 252 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 235 ILE B C   
1859 O O   . ILE A 252 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 235 ILE B O   
1860 C CB  . ILE A 252 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 235 ILE B CB  
1861 C CG1 . ILE A 252 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 235 ILE B CG1 
1862 C CG2 . ILE A 252 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 235 ILE B CG2 
1863 C CD1 . ILE A 252 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 235 ILE B CD1 
1864 N N   . ALA A 253 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 236 ALA B N   
1865 C CA  . ALA A 253 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 236 ALA B CA  
1866 C C   . ALA A 253 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 236 ALA B C   
1867 O O   . ALA A 253 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 236 ALA B O   
1868 C CB  . ALA A 253 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 236 ALA B CB  
1869 N N   . ILE A 254 ? 0.9219 0.9219 0.9219 0.0000 0.0000 0.0000 237 ILE B N   
1870 C CA  . ILE A 254 ? 0.9219 0.9219 0.9219 0.0000 0.0000 0.0000 237 ILE B CA  
1871 C C   . ILE A 254 ? 0.9219 0.9219 0.9219 0.0000 0.0000 0.0000 237 ILE B C   
1872 O O   . ILE A 254 ? 0.9219 0.9219 0.9219 0.0000 0.0000 0.0000 237 ILE B O   
1873 C CB  . ILE A 254 ? 0.9219 0.9219 0.9219 0.0000 0.0000 0.0000 237 ILE B CB  
1874 C CG1 . ILE A 254 ? 0.9219 0.9219 0.9219 0.0000 0.0000 0.0000 237 ILE B CG1 
1875 C CG2 . ILE A 254 ? 0.9219 0.9219 0.9219 0.0000 0.0000 0.0000 237 ILE B CG2 
1876 C CD1 . ILE A 254 ? 0.9219 0.9219 0.9219 0.0000 0.0000 0.0000 237 ILE B CD1 
1877 N N   . ASN A 255 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 238 ASN B N   
1878 C CA  . ASN A 255 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 238 ASN B CA  
1879 C C   . ASN A 255 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 238 ASN B C   
1880 O O   . ASN A 255 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 238 ASN B O   
1881 C CB  . ASN A 255 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 238 ASN B CB  
1882 C CG  . ASN A 255 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 238 ASN B CG  
1883 O OD1 . ASN A 255 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 238 ASN B OD1 
1884 N ND2 . ASN A 255 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 238 ASN B ND2 
1885 N N   . PRO A 256 ? 1.0443 1.0443 1.0443 0.0000 0.0000 0.0000 239 PRO B N   
1886 C CA  . PRO A 256 ? 1.0443 1.0443 1.0443 0.0000 0.0000 0.0000 239 PRO B CA  
1887 C C   . PRO A 256 ? 1.0443 1.0443 1.0443 0.0000 0.0000 0.0000 239 PRO B C   
1888 O O   . PRO A 256 ? 1.0443 1.0443 1.0443 0.0000 0.0000 0.0000 239 PRO B O   
1889 C CB  . PRO A 256 ? 1.0443 1.0443 1.0443 0.0000 0.0000 0.0000 239 PRO B CB  
1890 C CG  . PRO A 256 ? 1.0443 1.0443 1.0443 0.0000 0.0000 0.0000 239 PRO B CG  
1891 C CD  . PRO A 256 ? 1.0443 1.0443 1.0443 0.0000 0.0000 0.0000 239 PRO B CD  
1892 N N   . ASN A 257 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 240 ASN B N   
1893 C CA  . ASN A 257 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 240 ASN B CA  
1894 C C   . ASN A 257 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 240 ASN B C   
1895 O O   . ASN A 257 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 240 ASN B O   
1896 C CB  . ASN A 257 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 240 ASN B CB  
1897 C CG  . ASN A 257 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 240 ASN B CG  
1898 O OD1 . ASN A 257 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 240 ASN B OD1 
1899 N ND2 . ASN A 257 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 240 ASN B ND2 
1900 N N   . ARG A 258 ? 1.0091 1.0091 1.0091 0.0000 0.0000 0.0000 241 ARG B N   
1901 C CA  . ARG A 258 ? 1.0091 1.0091 1.0091 0.0000 0.0000 0.0000 241 ARG B CA  
1902 C C   . ARG A 258 ? 1.0091 1.0091 1.0091 0.0000 0.0000 0.0000 241 ARG B C   
1903 O O   . ARG A 258 ? 1.0091 1.0091 1.0091 0.0000 0.0000 0.0000 241 ARG B O   
1904 C CB  . ARG A 258 ? 1.0091 1.0091 1.0091 0.0000 0.0000 0.0000 241 ARG B CB  
1905 C CG  . ARG A 258 ? 1.0091 1.0091 1.0091 0.0000 0.0000 0.0000 241 ARG B CG  
1906 C CD  . ARG A 258 ? 1.0091 1.0091 1.0091 0.0000 0.0000 0.0000 241 ARG B CD  
1907 N NE  . ARG A 258 ? 1.0091 1.0091 1.0091 0.0000 0.0000 0.0000 241 ARG B NE  
1908 C CZ  . ARG A 258 ? 1.0091 1.0091 1.0091 0.0000 0.0000 0.0000 241 ARG B CZ  
1909 N NH1 . ARG A 258 ? 1.0091 1.0091 1.0091 0.0000 0.0000 0.0000 241 ARG B NH1 
1910 N NH2 . ARG A 258 ? 1.0091 1.0091 1.0091 0.0000 0.0000 0.0000 241 ARG B NH2 
1911 N N   . VAL A 259 ? 1.0048 1.0048 1.0048 0.0000 0.0000 0.0000 242 VAL B N   
1912 C CA  . VAL A 259 ? 1.0048 1.0048 1.0048 0.0000 0.0000 0.0000 242 VAL B CA  
1913 C C   . VAL A 259 ? 1.0048 1.0048 1.0048 0.0000 0.0000 0.0000 242 VAL B C   
1914 O O   . VAL A 259 ? 1.0048 1.0048 1.0048 0.0000 0.0000 0.0000 242 VAL B O   
1915 C CB  . VAL A 259 ? 1.0048 1.0048 1.0048 0.0000 0.0000 0.0000 242 VAL B CB  
1916 C CG1 . VAL A 259 ? 1.0048 1.0048 1.0048 0.0000 0.0000 0.0000 242 VAL B CG1 
1917 C CG2 . VAL A 259 ? 1.0048 1.0048 1.0048 0.0000 0.0000 0.0000 242 VAL B CG2 
1918 N N   . PHE A 260 ? 0.9901 0.9901 0.9901 0.0000 0.0000 0.0000 243 PHE B N   
1919 C CA  . PHE A 260 ? 0.9901 0.9901 0.9901 0.0000 0.0000 0.0000 243 PHE B CA  
1920 C C   . PHE A 260 ? 0.9901 0.9901 0.9901 0.0000 0.0000 0.0000 243 PHE B C   
1921 O O   . PHE A 260 ? 0.9901 0.9901 0.9901 0.0000 0.0000 0.0000 243 PHE B O   
1922 C CB  . PHE A 260 ? 0.9901 0.9901 0.9901 0.0000 0.0000 0.0000 243 PHE B CB  
1923 C CG  . PHE A 260 ? 0.9901 0.9901 0.9901 0.0000 0.0000 0.0000 243 PHE B CG  
1924 C CD1 . PHE A 260 ? 0.9901 0.9901 0.9901 0.0000 0.0000 0.0000 243 PHE B CD1 
1925 C CD2 . PHE A 260 ? 0.9901 0.9901 0.9901 0.0000 0.0000 0.0000 243 PHE B CD2 
1926 C CE1 . PHE A 260 ? 0.9901 0.9901 0.9901 0.0000 0.0000 0.0000 243 PHE B CE1 
1927 C CE2 . PHE A 260 ? 0.9901 0.9901 0.9901 0.0000 0.0000 0.0000 243 PHE B CE2 
1928 C CZ  . PHE A 260 ? 0.9901 0.9901 0.9901 0.0000 0.0000 0.0000 243 PHE B CZ  
1929 N N   . LYS A 261 ? 1.0092 1.0092 1.0092 0.0000 0.0000 0.0000 244 LYS B N   
1930 C CA  . LYS A 261 ? 1.0092 1.0092 1.0092 0.0000 0.0000 0.0000 244 LYS B CA  
1931 C C   . LYS A 261 ? 1.0092 1.0092 1.0092 0.0000 0.0000 0.0000 244 LYS B C   
1932 O O   . LYS A 261 ? 1.0092 1.0092 1.0092 0.0000 0.0000 0.0000 244 LYS B O   
1933 C CB  . LYS A 261 ? 1.0092 1.0092 1.0092 0.0000 0.0000 0.0000 244 LYS B CB  
1934 C CG  . LYS A 261 ? 1.0092 1.0092 1.0092 0.0000 0.0000 0.0000 244 LYS B CG  
1935 C CD  . LYS A 261 ? 1.0092 1.0092 1.0092 0.0000 0.0000 0.0000 244 LYS B CD  
1936 C CE  . LYS A 261 ? 1.0092 1.0092 1.0092 0.0000 0.0000 0.0000 244 LYS B CE  
1937 N NZ  . LYS A 261 ? 1.0092 1.0092 1.0092 0.0000 0.0000 0.0000 244 LYS B NZ  
1938 N N   . VAL A 262 ? 1.0144 1.0144 1.0144 0.0000 0.0000 0.0000 245 VAL B N   
1939 C CA  . VAL A 262 ? 1.0144 1.0144 1.0144 0.0000 0.0000 0.0000 245 VAL B CA  
1940 C C   . VAL A 262 ? 1.0144 1.0144 1.0144 0.0000 0.0000 0.0000 245 VAL B C   
1941 O O   . VAL A 262 ? 1.0144 1.0144 1.0144 0.0000 0.0000 0.0000 245 VAL B O   
1942 C CB  . VAL A 262 ? 1.0144 1.0144 1.0144 0.0000 0.0000 0.0000 245 VAL B CB  
1943 C CG1 . VAL A 262 ? 1.0144 1.0144 1.0144 0.0000 0.0000 0.0000 245 VAL B CG1 
1944 C CG2 . VAL A 262 ? 1.0144 1.0144 1.0144 0.0000 0.0000 0.0000 245 VAL B CG2 
1945 N N   . ASN A 263 ? 0.9992 0.9992 0.9992 0.0000 0.0000 0.0000 246 ASN B N   
1946 C CA  . ASN A 263 ? 0.9992 0.9992 0.9992 0.0000 0.0000 0.0000 246 ASN B CA  
1947 C C   . ASN A 263 ? 0.9992 0.9992 0.9992 0.0000 0.0000 0.0000 246 ASN B C   
1948 O O   . ASN A 263 ? 0.9992 0.9992 0.9992 0.0000 0.0000 0.0000 246 ASN B O   
1949 C CB  . ASN A 263 ? 0.9992 0.9992 0.9992 0.0000 0.0000 0.0000 246 ASN B CB  
1950 C CG  . ASN A 263 ? 0.9992 0.9992 0.9992 0.0000 0.0000 0.0000 246 ASN B CG  
1951 O OD1 . ASN A 263 ? 0.9992 0.9992 0.9992 0.0000 0.0000 0.0000 246 ASN B OD1 
1952 N ND2 . ASN A 263 ? 0.9992 0.9992 0.9992 0.0000 0.0000 0.0000 246 ASN B ND2 
1953 N N   . THR A 264 ? 1.0034 1.0034 1.0034 0.0000 0.0000 0.0000 247 THR B N   
1954 C CA  . THR A 264 ? 1.0034 1.0034 1.0034 0.0000 0.0000 0.0000 247 THR B CA  
1955 C C   . THR A 264 ? 1.0034 1.0034 1.0034 0.0000 0.0000 0.0000 247 THR B C   
1956 O O   . THR A 264 ? 1.0034 1.0034 1.0034 0.0000 0.0000 0.0000 247 THR B O   
1957 C CB  . THR A 264 ? 1.0034 1.0034 1.0034 0.0000 0.0000 0.0000 247 THR B CB  
1958 O OG1 . THR A 264 ? 1.0034 1.0034 1.0034 0.0000 0.0000 0.0000 247 THR B OG1 
1959 C CG2 . THR A 264 ? 1.0034 1.0034 1.0034 0.0000 0.0000 0.0000 247 THR B CG2 
1960 N N   . ASN A 265 ? 1.0219 1.0219 1.0219 0.0000 0.0000 0.0000 248 ASN B N   
1961 C CA  . ASN A 265 ? 1.0219 1.0219 1.0219 0.0000 0.0000 0.0000 248 ASN B CA  
1962 C C   . ASN A 265 ? 1.0219 1.0219 1.0219 0.0000 0.0000 0.0000 248 ASN B C   
1963 O O   . ASN A 265 ? 1.0219 1.0219 1.0219 0.0000 0.0000 0.0000 248 ASN B O   
1964 C CB  . ASN A 265 ? 1.0219 1.0219 1.0219 0.0000 0.0000 0.0000 248 ASN B CB  
1965 C CG  . ASN A 265 ? 1.0219 1.0219 1.0219 0.0000 0.0000 0.0000 248 ASN B CG  
1966 O OD1 . ASN A 265 ? 1.0219 1.0219 1.0219 0.0000 0.0000 0.0000 248 ASN B OD1 
1967 N ND2 . ASN A 265 ? 1.0219 1.0219 1.0219 0.0000 0.0000 0.0000 248 ASN B ND2 
1968 N N   . ALA A 266 ? 0.9794 0.9794 0.9794 0.0000 0.0000 0.0000 249 ALA B N   
1969 C CA  . ALA A 266 ? 0.9794 0.9794 0.9794 0.0000 0.0000 0.0000 249 ALA B CA  
1970 C C   . ALA A 266 ? 0.9794 0.9794 0.9794 0.0000 0.0000 0.0000 249 ALA B C   
1971 O O   . ALA A 266 ? 0.9794 0.9794 0.9794 0.0000 0.0000 0.0000 249 ALA B O   
1972 C CB  . ALA A 266 ? 0.9794 0.9794 0.9794 0.0000 0.0000 0.0000 249 ALA B CB  
1973 N N   . TYR A 267 ? 0.9713 0.9713 0.9713 0.0000 0.0000 0.0000 250 TYR B N   
1974 C CA  . TYR A 267 ? 0.9713 0.9713 0.9713 0.0000 0.0000 0.0000 250 TYR B CA  
1975 C C   . TYR A 267 ? 0.9713 0.9713 0.9713 0.0000 0.0000 0.0000 250 TYR B C   
1976 O O   . TYR A 267 ? 0.9713 0.9713 0.9713 0.0000 0.0000 0.0000 250 TYR B O   
1977 C CB  . TYR A 267 ? 0.9713 0.9713 0.9713 0.0000 0.0000 0.0000 250 TYR B CB  
1978 C CG  . TYR A 267 ? 0.9713 0.9713 0.9713 0.0000 0.0000 0.0000 250 TYR B CG  
1979 C CD1 . TYR A 267 ? 0.9713 0.9713 0.9713 0.0000 0.0000 0.0000 250 TYR B CD1 
1980 C CD2 . TYR A 267 ? 0.9713 0.9713 0.9713 0.0000 0.0000 0.0000 250 TYR B CD2 
1981 C CE1 . TYR A 267 ? 0.9713 0.9713 0.9713 0.0000 0.0000 0.0000 250 TYR B CE1 
1982 C CE2 . TYR A 267 ? 0.9713 0.9713 0.9713 0.0000 0.0000 0.0000 250 TYR B CE2 
1983 C CZ  . TYR A 267 ? 0.9713 0.9713 0.9713 0.0000 0.0000 0.0000 250 TYR B CZ  
1984 O OH  . TYR A 267 ? 0.9713 0.9713 0.9713 0.0000 0.0000 0.0000 250 TYR B OH  
1985 N N   . TYR A 268 ? 0.9623 0.9623 0.9623 0.0000 0.0000 0.0000 251 TYR B N   
1986 C CA  . TYR A 268 ? 0.9623 0.9623 0.9623 0.0000 0.0000 0.0000 251 TYR B CA  
1987 C C   . TYR A 268 ? 0.9623 0.9623 0.9623 0.0000 0.0000 0.0000 251 TYR B C   
1988 O O   . TYR A 268 ? 0.9623 0.9623 0.9623 0.0000 0.0000 0.0000 251 TYR B O   
1989 C CB  . TYR A 268 ? 0.9623 0.9623 0.9623 0.0000 0.0000 0.0000 251 TYR B CB  
1990 C CG  . TYR A 268 ? 0.9623 0.9623 0.9623 0.0000 0.0000 0.0000 251 TYR B CG  
1991 C CD1 . TYR A 268 ? 0.9623 0.9623 0.9623 0.0000 0.0000 0.0000 251 TYR B CD1 
1992 C CD2 . TYR A 268 ? 0.9623 0.9623 0.9623 0.0000 0.0000 0.0000 251 TYR B CD2 
1993 C CE1 . TYR A 268 ? 0.9623 0.9623 0.9623 0.0000 0.0000 0.0000 251 TYR B CE1 
1994 C CE2 . TYR A 268 ? 0.9623 0.9623 0.9623 0.0000 0.0000 0.0000 251 TYR B CE2 
1995 C CZ  . TYR A 268 ? 0.9623 0.9623 0.9623 0.0000 0.0000 0.0000 251 TYR B CZ  
1996 O OH  . TYR A 268 ? 0.9623 0.9623 0.9623 0.0000 0.0000 0.0000 251 TYR B OH  
1997 N N   . GLU A 269 ? 0.9880 0.9880 0.9880 0.0000 0.0000 0.0000 252 GLU B N   
1998 C CA  . GLU A 269 ? 0.9880 0.9880 0.9880 0.0000 0.0000 0.0000 252 GLU B CA  
1999 C C   . GLU A 269 ? 0.9880 0.9880 0.9880 0.0000 0.0000 0.0000 252 GLU B C   
2000 O O   . GLU A 269 ? 0.9880 0.9880 0.9880 0.0000 0.0000 0.0000 252 GLU B O   
2001 C CB  . GLU A 269 ? 0.9880 0.9880 0.9880 0.0000 0.0000 0.0000 252 GLU B CB  
2002 C CG  . GLU A 269 ? 0.9880 0.9880 0.9880 0.0000 0.0000 0.0000 252 GLU B CG  
2003 C CD  . GLU A 269 ? 0.9880 0.9880 0.9880 0.0000 0.0000 0.0000 252 GLU B CD  
2004 O OE1 . GLU A 269 ? 0.9880 0.9880 0.9880 0.0000 0.0000 0.0000 252 GLU B OE1 
2005 O OE2 . GLU A 269 ? 0.9880 0.9880 0.9880 0.0000 0.0000 0.0000 252 GLU B OE2 
2006 N N   . MET A 270 ? 0.9927 0.9927 0.9927 0.0000 0.0000 0.0000 253 MET B N   
2007 C CA  . MET A 270 ? 0.9927 0.9927 0.9927 0.0000 0.0000 0.0000 253 MET B CA  
2008 C C   . MET A 270 ? 0.9927 0.9927 0.9927 0.0000 0.0000 0.0000 253 MET B C   
2009 O O   . MET A 270 ? 0.9927 0.9927 0.9927 0.0000 0.0000 0.0000 253 MET B O   
2010 C CB  . MET A 270 ? 0.9927 0.9927 0.9927 0.0000 0.0000 0.0000 253 MET B CB  
2011 C CG  . MET A 270 ? 0.9927 0.9927 0.9927 0.0000 0.0000 0.0000 253 MET B CG  
2012 S SD  . MET A 270 ? 0.9927 0.9927 0.9927 0.0000 0.0000 0.0000 253 MET B SD  
2013 C CE  . MET A 270 ? 0.9927 0.9927 0.9927 0.0000 0.0000 0.0000 253 MET B CE  
2014 N N   . SER A 271 ? 1.0491 1.0491 1.0491 0.0000 0.0000 0.0000 254 SER B N   
2015 C CA  . SER A 271 ? 1.0491 1.0491 1.0491 0.0000 0.0000 0.0000 254 SER B CA  
2016 C C   . SER A 271 ? 1.0491 1.0491 1.0491 0.0000 0.0000 0.0000 254 SER B C   
2017 O O   . SER A 271 ? 1.0491 1.0491 1.0491 0.0000 0.0000 0.0000 254 SER B O   
2018 C CB  . SER A 271 ? 1.0491 1.0491 1.0491 0.0000 0.0000 0.0000 254 SER B CB  
2019 O OG  . SER A 271 ? 1.0491 1.0491 1.0491 0.0000 0.0000 0.0000 254 SER B OG  
2020 N N   . GLY A 272 ? 1.0810 1.0810 1.0810 0.0000 0.0000 0.0000 255 GLY B N   
2021 C CA  . GLY A 272 ? 1.0810 1.0810 1.0810 0.0000 0.0000 0.0000 255 GLY B CA  
2022 C C   . GLY A 272 ? 1.0810 1.0810 1.0810 0.0000 0.0000 0.0000 255 GLY B C   
2023 O O   . GLY A 272 ? 1.0810 1.0810 1.0810 0.0000 0.0000 0.0000 255 GLY B O   
2024 N N   . LEU A 273 ? 1.0248 1.0248 1.0248 0.0000 0.0000 0.0000 256 LEU B N   
2025 C CA  . LEU A 273 ? 1.0248 1.0248 1.0248 0.0000 0.0000 0.0000 256 LEU B CA  
2026 C C   . LEU A 273 ? 1.0248 1.0248 1.0248 0.0000 0.0000 0.0000 256 LEU B C   
2027 O O   . LEU A 273 ? 1.0248 1.0248 1.0248 0.0000 0.0000 0.0000 256 LEU B O   
2028 C CB  . LEU A 273 ? 1.0248 1.0248 1.0248 0.0000 0.0000 0.0000 256 LEU B CB  
2029 C CG  . LEU A 273 ? 1.0248 1.0248 1.0248 0.0000 0.0000 0.0000 256 LEU B CG  
2030 C CD1 . LEU A 273 ? 1.0248 1.0248 1.0248 0.0000 0.0000 0.0000 256 LEU B CD1 
2031 C CD2 . LEU A 273 ? 1.0248 1.0248 1.0248 0.0000 0.0000 0.0000 256 LEU B CD2 
2032 N N   . GLU A 274 ? 1.1136 1.1136 1.1136 0.0000 0.0000 0.0000 257 GLU B N   
2033 C CA  . GLU A 274 ? 1.1136 1.1136 1.1136 0.0000 0.0000 0.0000 257 GLU B CA  
2034 C C   . GLU A 274 ? 1.1136 1.1136 1.1136 0.0000 0.0000 0.0000 257 GLU B C   
2035 O O   . GLU A 274 ? 1.1136 1.1136 1.1136 0.0000 0.0000 0.0000 257 GLU B O   
2036 C CB  . GLU A 274 ? 1.1136 1.1136 1.1136 0.0000 0.0000 0.0000 257 GLU B CB  
2037 C CG  . GLU A 274 ? 1.1136 1.1136 1.1136 0.0000 0.0000 0.0000 257 GLU B CG  
2038 C CD  . GLU A 274 ? 1.1136 1.1136 1.1136 0.0000 0.0000 0.0000 257 GLU B CD  
2039 O OE1 . GLU A 274 ? 1.1136 1.1136 1.1136 0.0000 0.0000 0.0000 257 GLU B OE1 
2040 O OE2 . GLU A 274 ? 1.1136 1.1136 1.1136 0.0000 0.0000 0.0000 257 GLU B OE2 
2041 N N   . VAL A 275 ? 0.9392 0.9392 0.9392 0.0000 0.0000 0.0000 258 VAL B N   
2042 C CA  . VAL A 275 ? 0.9392 0.9392 0.9392 0.0000 0.0000 0.0000 258 VAL B CA  
2043 C C   . VAL A 275 ? 0.9392 0.9392 0.9392 0.0000 0.0000 0.0000 258 VAL B C   
2044 O O   . VAL A 275 ? 0.9392 0.9392 0.9392 0.0000 0.0000 0.0000 258 VAL B O   
2045 C CB  . VAL A 275 ? 0.9392 0.9392 0.9392 0.0000 0.0000 0.0000 258 VAL B CB  
2046 C CG1 . VAL A 275 ? 0.9392 0.9392 0.9392 0.0000 0.0000 0.0000 258 VAL B CG1 
2047 C CG2 . VAL A 275 ? 0.9392 0.9392 0.9392 0.0000 0.0000 0.0000 258 VAL B CG2 
2048 N N   . SER A 276 ? 0.9586 0.9586 0.9586 0.0000 0.0000 0.0000 259 SER B N   
2049 C CA  . SER A 276 ? 0.9586 0.9586 0.9586 0.0000 0.0000 0.0000 259 SER B CA  
2050 C C   . SER A 276 ? 0.9586 0.9586 0.9586 0.0000 0.0000 0.0000 259 SER B C   
2051 O O   . SER A 276 ? 0.9586 0.9586 0.9586 0.0000 0.0000 0.0000 259 SER B O   
2052 C CB  . SER A 276 ? 0.9586 0.9586 0.9586 0.0000 0.0000 0.0000 259 SER B CB  
2053 O OG  . SER A 276 ? 0.9586 0.9586 0.9586 0.0000 0.0000 0.0000 259 SER B OG  
2054 N N   . PHE A 277 ? 0.9239 0.9239 0.9239 0.0000 0.0000 0.0000 260 PHE B N   
2055 C CA  . PHE A 277 ? 0.9239 0.9239 0.9239 0.0000 0.0000 0.0000 260 PHE B CA  
2056 C C   . PHE A 277 ? 0.9239 0.9239 0.9239 0.0000 0.0000 0.0000 260 PHE B C   
2057 O O   . PHE A 277 ? 0.9239 0.9239 0.9239 0.0000 0.0000 0.0000 260 PHE B O   
2058 C CB  . PHE A 277 ? 0.9239 0.9239 0.9239 0.0000 0.0000 0.0000 260 PHE B CB  
2059 C CG  . PHE A 277 ? 0.9239 0.9239 0.9239 0.0000 0.0000 0.0000 260 PHE B CG  
2060 C CD1 . PHE A 277 ? 0.9239 0.9239 0.9239 0.0000 0.0000 0.0000 260 PHE B CD1 
2061 C CD2 . PHE A 277 ? 0.9239 0.9239 0.9239 0.0000 0.0000 0.0000 260 PHE B CD2 
2062 C CE1 . PHE A 277 ? 0.9239 0.9239 0.9239 0.0000 0.0000 0.0000 260 PHE B CE1 
2063 C CE2 . PHE A 277 ? 0.9239 0.9239 0.9239 0.0000 0.0000 0.0000 260 PHE B CE2 
2064 C CZ  . PHE A 277 ? 0.9239 0.9239 0.9239 0.0000 0.0000 0.0000 260 PHE B CZ  
2065 N N   . GLU A 278 ? 0.8985 0.8985 0.8985 0.0000 0.0000 0.0000 261 GLU B N   
2066 C CA  . GLU A 278 ? 0.8985 0.8985 0.8985 0.0000 0.0000 0.0000 261 GLU B CA  
2067 C C   . GLU A 278 ? 0.8985 0.8985 0.8985 0.0000 0.0000 0.0000 261 GLU B C   
2068 O O   . GLU A 278 ? 0.8985 0.8985 0.8985 0.0000 0.0000 0.0000 261 GLU B O   
2069 C CB  . GLU A 278 ? 0.8985 0.8985 0.8985 0.0000 0.0000 0.0000 261 GLU B CB  
2070 C CG  . GLU A 278 ? 0.8985 0.8985 0.8985 0.0000 0.0000 0.0000 261 GLU B CG  
2071 C CD  . GLU A 278 ? 0.8985 0.8985 0.8985 0.0000 0.0000 0.0000 261 GLU B CD  
2072 O OE1 . GLU A 278 ? 0.8985 0.8985 0.8985 0.0000 0.0000 0.0000 261 GLU B OE1 
2073 O OE2 . GLU A 278 ? 0.8985 0.8985 0.8985 0.0000 0.0000 0.0000 261 GLU B OE2 
2074 N N   . GLU A 279 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 262 GLU B N   
2075 C CA  . GLU A 279 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 262 GLU B CA  
2076 C C   . GLU A 279 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 262 GLU B C   
2077 O O   . GLU A 279 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 262 GLU B O   
2078 C CB  . GLU A 279 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 262 GLU B CB  
2079 C CG  . GLU A 279 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 262 GLU B CG  
2080 C CD  . GLU A 279 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 262 GLU B CD  
2081 O OE1 . GLU A 279 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 262 GLU B OE1 
2082 O OE2 . GLU A 279 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 262 GLU B OE2 
2083 N N   . LEU A 280 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 263 LEU B N   
2084 C CA  . LEU A 280 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 263 LEU B CA  
2085 C C   . LEU A 280 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 263 LEU B C   
2086 O O   . LEU A 280 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 263 LEU B O   
2087 C CB  . LEU A 280 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 263 LEU B CB  
2088 C CG  . LEU A 280 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 263 LEU B CG  
2089 C CD1 . LEU A 280 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 263 LEU B CD1 
2090 C CD2 . LEU A 280 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 263 LEU B CD2 
2091 N N   . ARG A 281 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 264 ARG B N   
2092 C CA  . ARG A 281 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 264 ARG B CA  
2093 C C   . ARG A 281 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 264 ARG B C   
2094 O O   . ARG A 281 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 264 ARG B O   
2095 C CB  . ARG A 281 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 264 ARG B CB  
2096 C CG  . ARG A 281 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 264 ARG B CG  
2097 C CD  . ARG A 281 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 264 ARG B CD  
2098 N NE  . ARG A 281 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 264 ARG B NE  
2099 C CZ  . ARG A 281 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 264 ARG B CZ  
2100 N NH1 . ARG A 281 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 264 ARG B NH1 
2101 N NH2 . ARG A 281 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 264 ARG B NH2 
2102 N N   . THR A 282 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 265 THR B N   
2103 C CA  . THR A 282 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 265 THR B CA  
2104 C C   . THR A 282 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 265 THR B C   
2105 O O   . THR A 282 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 265 THR B O   
2106 C CB  . THR A 282 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 265 THR B CB  
2107 O OG1 . THR A 282 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 265 THR B OG1 
2108 C CG2 . THR A 282 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 265 THR B CG2 
2109 N N   . PHE A 283 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 266 PHE B N   
2110 C CA  . PHE A 283 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 266 PHE B CA  
2111 C C   . PHE A 283 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 266 PHE B C   
2112 O O   . PHE A 283 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 266 PHE B O   
2113 C CB  . PHE A 283 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 266 PHE B CB  
2114 C CG  . PHE A 283 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 266 PHE B CG  
2115 C CD1 . PHE A 283 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 266 PHE B CD1 
2116 C CD2 . PHE A 283 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 266 PHE B CD2 
2117 C CE1 . PHE A 283 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 266 PHE B CE1 
2118 C CE2 . PHE A 283 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 266 PHE B CE2 
2119 C CZ  . PHE A 283 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 266 PHE B CZ  
2120 N N   . GLY A 284 ? 0.9195 0.9195 0.9195 0.0000 0.0000 0.0000 267 GLY B N   
2121 C CA  . GLY A 284 ? 0.9195 0.9195 0.9195 0.0000 0.0000 0.0000 267 GLY B CA  
2122 C C   . GLY A 284 ? 0.9195 0.9195 0.9195 0.0000 0.0000 0.0000 267 GLY B C   
2123 O O   . GLY A 284 ? 0.9195 0.9195 0.9195 0.0000 0.0000 0.0000 267 GLY B O   
2124 N N   . GLY A 285 ? 0.9599 0.9599 0.9599 0.0000 0.0000 0.0000 268 GLY B N   
2125 C CA  . GLY A 285 ? 0.9599 0.9599 0.9599 0.0000 0.0000 0.0000 268 GLY B CA  
2126 C C   . GLY A 285 ? 0.9599 0.9599 0.9599 0.0000 0.0000 0.0000 268 GLY B C   
2127 O O   . GLY A 285 ? 0.9599 0.9599 0.9599 0.0000 0.0000 0.0000 268 GLY B O   
2128 N N   . HIS A 286 ? 1.0074 1.0074 1.0074 0.0000 0.0000 0.0000 269 HIS B N   
2129 C CA  . HIS A 286 ? 1.0074 1.0074 1.0074 0.0000 0.0000 0.0000 269 HIS B CA  
2130 C C   . HIS A 286 ? 1.0074 1.0074 1.0074 0.0000 0.0000 0.0000 269 HIS B C   
2131 O O   . HIS A 286 ? 1.0074 1.0074 1.0074 0.0000 0.0000 0.0000 269 HIS B O   
2132 C CB  . HIS A 286 ? 1.0074 1.0074 1.0074 0.0000 0.0000 0.0000 269 HIS B CB  
2133 C CG  . HIS A 286 ? 1.0074 1.0074 1.0074 0.0000 0.0000 0.0000 269 HIS B CG  
2134 N ND1 . HIS A 286 ? 1.0074 1.0074 1.0074 0.0000 0.0000 0.0000 269 HIS B ND1 
2135 C CD2 . HIS A 286 ? 1.0074 1.0074 1.0074 0.0000 0.0000 0.0000 269 HIS B CD2 
2136 C CE1 . HIS A 286 ? 1.0074 1.0074 1.0074 0.0000 0.0000 0.0000 269 HIS B CE1 
2137 N NE2 . HIS A 286 ? 1.0074 1.0074 1.0074 0.0000 0.0000 0.0000 269 HIS B NE2 
2138 N N   . ASP A 287 ? 0.9975 0.9975 0.9975 0.0000 0.0000 0.0000 270 ASP B N   
2139 C CA  . ASP A 287 ? 0.9975 0.9975 0.9975 0.0000 0.0000 0.0000 270 ASP B CA  
2140 C C   . ASP A 287 ? 0.9975 0.9975 0.9975 0.0000 0.0000 0.0000 270 ASP B C   
2141 O O   . ASP A 287 ? 0.9975 0.9975 0.9975 0.0000 0.0000 0.0000 270 ASP B O   
2142 C CB  . ASP A 287 ? 0.9975 0.9975 0.9975 0.0000 0.0000 0.0000 270 ASP B CB  
2143 C CG  . ASP A 287 ? 0.9975 0.9975 0.9975 0.0000 0.0000 0.0000 270 ASP B CG  
2144 O OD1 . ASP A 287 ? 0.9975 0.9975 0.9975 0.0000 0.0000 0.0000 270 ASP B OD1 
2145 O OD2 . ASP A 287 ? 0.9975 0.9975 0.9975 0.0000 0.0000 0.0000 270 ASP B OD2 
2146 N N   . ALA A 288 ? 0.9667 0.9667 0.9667 0.0000 0.0000 0.0000 271 ALA B N   
2147 C CA  . ALA A 288 ? 0.9667 0.9667 0.9667 0.0000 0.0000 0.0000 271 ALA B CA  
2148 C C   . ALA A 288 ? 0.9667 0.9667 0.9667 0.0000 0.0000 0.0000 271 ALA B C   
2149 O O   . ALA A 288 ? 0.9667 0.9667 0.9667 0.0000 0.0000 0.0000 271 ALA B O   
2150 C CB  . ALA A 288 ? 0.9667 0.9667 0.9667 0.0000 0.0000 0.0000 271 ALA B CB  
2151 N N   . LYS A 289 ? 0.9798 0.9798 0.9798 0.0000 0.0000 0.0000 272 LYS B N   
2152 C CA  . LYS A 289 ? 0.9798 0.9798 0.9798 0.0000 0.0000 0.0000 272 LYS B CA  
2153 C C   . LYS A 289 ? 0.9798 0.9798 0.9798 0.0000 0.0000 0.0000 272 LYS B C   
2154 O O   . LYS A 289 ? 0.9798 0.9798 0.9798 0.0000 0.0000 0.0000 272 LYS B O   
2155 C CB  . LYS A 289 ? 0.9798 0.9798 0.9798 0.0000 0.0000 0.0000 272 LYS B CB  
2156 C CG  . LYS A 289 ? 0.9798 0.9798 0.9798 0.0000 0.0000 0.0000 272 LYS B CG  
2157 C CD  . LYS A 289 ? 0.9798 0.9798 0.9798 0.0000 0.0000 0.0000 272 LYS B CD  
2158 C CE  . LYS A 289 ? 0.9798 0.9798 0.9798 0.0000 0.0000 0.0000 272 LYS B CE  
2159 N NZ  . LYS A 289 ? 0.9798 0.9798 0.9798 0.0000 0.0000 0.0000 272 LYS B NZ  
2160 N N   . PHE A 290 ? 0.9465 0.9465 0.9465 0.0000 0.0000 0.0000 273 PHE B N   
2161 C CA  . PHE A 290 ? 0.9465 0.9465 0.9465 0.0000 0.0000 0.0000 273 PHE B CA  
2162 C C   . PHE A 290 ? 0.9465 0.9465 0.9465 0.0000 0.0000 0.0000 273 PHE B C   
2163 O O   . PHE A 290 ? 0.9465 0.9465 0.9465 0.0000 0.0000 0.0000 273 PHE B O   
2164 C CB  . PHE A 290 ? 0.9465 0.9465 0.9465 0.0000 0.0000 0.0000 273 PHE B CB  
2165 C CG  . PHE A 290 ? 0.9465 0.9465 0.9465 0.0000 0.0000 0.0000 273 PHE B CG  
2166 C CD1 . PHE A 290 ? 0.9465 0.9465 0.9465 0.0000 0.0000 0.0000 273 PHE B CD1 
2167 C CD2 . PHE A 290 ? 0.9465 0.9465 0.9465 0.0000 0.0000 0.0000 273 PHE B CD2 
2168 C CE1 . PHE A 290 ? 0.9465 0.9465 0.9465 0.0000 0.0000 0.0000 273 PHE B CE1 
2169 C CE2 . PHE A 290 ? 0.9465 0.9465 0.9465 0.0000 0.0000 0.0000 273 PHE B CE2 
2170 C CZ  . PHE A 290 ? 0.9465 0.9465 0.9465 0.0000 0.0000 0.0000 273 PHE B CZ  
2171 N N   . ILE A 291 ? 0.9934 0.9934 0.9934 0.0000 0.0000 0.0000 274 ILE B N   
2172 C CA  . ILE A 291 ? 0.9934 0.9934 0.9934 0.0000 0.0000 0.0000 274 ILE B CA  
2173 C C   . ILE A 291 ? 0.9934 0.9934 0.9934 0.0000 0.0000 0.0000 274 ILE B C   
2174 O O   . ILE A 291 ? 0.9934 0.9934 0.9934 0.0000 0.0000 0.0000 274 ILE B O   
2175 C CB  . ILE A 291 ? 0.9934 0.9934 0.9934 0.0000 0.0000 0.0000 274 ILE B CB  
2176 C CG1 . ILE A 291 ? 0.9934 0.9934 0.9934 0.0000 0.0000 0.0000 274 ILE B CG1 
2177 C CG2 . ILE A 291 ? 0.9934 0.9934 0.9934 0.0000 0.0000 0.0000 274 ILE B CG2 
2178 C CD1 . ILE A 291 ? 0.9934 0.9934 0.9934 0.0000 0.0000 0.0000 274 ILE B CD1 
2179 N N   . ASP A 292 ? 1.0791 1.0791 1.0791 0.0000 0.0000 0.0000 275 ASP B N   
2180 C CA  . ASP A 292 ? 1.0791 1.0791 1.0791 0.0000 0.0000 0.0000 275 ASP B CA  
2181 C C   . ASP A 292 ? 1.0791 1.0791 1.0791 0.0000 0.0000 0.0000 275 ASP B C   
2182 O O   . ASP A 292 ? 1.0791 1.0791 1.0791 0.0000 0.0000 0.0000 275 ASP B O   
2183 C CB  . ASP A 292 ? 1.0791 1.0791 1.0791 0.0000 0.0000 0.0000 275 ASP B CB  
2184 C CG  . ASP A 292 ? 1.0791 1.0791 1.0791 0.0000 0.0000 0.0000 275 ASP B CG  
2185 O OD1 . ASP A 292 ? 1.0791 1.0791 1.0791 0.0000 0.0000 0.0000 275 ASP B OD1 
2186 O OD2 . ASP A 292 ? 1.0791 1.0791 1.0791 0.0000 0.0000 0.0000 275 ASP B OD2 
2187 N N   . SER A 293 ? 1.0676 1.0676 1.0676 0.0000 0.0000 0.0000 276 SER B N   
2188 C CA  . SER A 293 ? 1.0676 1.0676 1.0676 0.0000 0.0000 0.0000 276 SER B CA  
2189 C C   . SER A 293 ? 1.0676 1.0676 1.0676 0.0000 0.0000 0.0000 276 SER B C   
2190 O O   . SER A 293 ? 1.0676 1.0676 1.0676 0.0000 0.0000 0.0000 276 SER B O   
2191 C CB  . SER A 293 ? 1.0676 1.0676 1.0676 0.0000 0.0000 0.0000 276 SER B CB  
2192 O OG  . SER A 293 ? 1.0676 1.0676 1.0676 0.0000 0.0000 0.0000 276 SER B OG  
2193 N N   . LEU A 294 ? 1.0677 1.0677 1.0677 0.0000 0.0000 0.0000 277 LEU B N   
2194 C CA  . LEU A 294 ? 1.0677 1.0677 1.0677 0.0000 0.0000 0.0000 277 LEU B CA  
2195 C C   . LEU A 294 ? 1.0677 1.0677 1.0677 0.0000 0.0000 0.0000 277 LEU B C   
2196 O O   . LEU A 294 ? 1.0677 1.0677 1.0677 0.0000 0.0000 0.0000 277 LEU B O   
2197 C CB  . LEU A 294 ? 1.0677 1.0677 1.0677 0.0000 0.0000 0.0000 277 LEU B CB  
2198 C CG  . LEU A 294 ? 1.0677 1.0677 1.0677 0.0000 0.0000 0.0000 277 LEU B CG  
2199 C CD1 . LEU A 294 ? 1.0677 1.0677 1.0677 0.0000 0.0000 0.0000 277 LEU B CD1 
2200 C CD2 . LEU A 294 ? 1.0677 1.0677 1.0677 0.0000 0.0000 0.0000 277 LEU B CD2 
2201 N N   . GLN A 295 ? 1.0509 1.0509 1.0509 0.0000 0.0000 0.0000 278 GLN B N   
2202 C CA  . GLN A 295 ? 1.0509 1.0509 1.0509 0.0000 0.0000 0.0000 278 GLN B CA  
2203 C C   . GLN A 295 ? 1.0509 1.0509 1.0509 0.0000 0.0000 0.0000 278 GLN B C   
2204 O O   . GLN A 295 ? 1.0509 1.0509 1.0509 0.0000 0.0000 0.0000 278 GLN B O   
2205 C CB  . GLN A 295 ? 1.0509 1.0509 1.0509 0.0000 0.0000 0.0000 278 GLN B CB  
2206 C CG  . GLN A 295 ? 1.0509 1.0509 1.0509 0.0000 0.0000 0.0000 278 GLN B CG  
2207 C CD  . GLN A 295 ? 1.0509 1.0509 1.0509 0.0000 0.0000 0.0000 278 GLN B CD  
2208 O OE1 . GLN A 295 ? 1.0509 1.0509 1.0509 0.0000 0.0000 0.0000 278 GLN B OE1 
2209 N NE2 . GLN A 295 ? 1.0509 1.0509 1.0509 0.0000 0.0000 0.0000 278 GLN B NE2 
2210 N N   . GLU A 296 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 279 GLU B N   
2211 C CA  . GLU A 296 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 279 GLU B CA  
2212 C C   . GLU A 296 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 279 GLU B C   
2213 O O   . GLU A 296 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 279 GLU B O   
2214 C CB  . GLU A 296 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 279 GLU B CB  
2215 C CG  . GLU A 296 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 279 GLU B CG  
2216 C CD  . GLU A 296 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 279 GLU B CD  
2217 O OE1 . GLU A 296 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 279 GLU B OE1 
2218 O OE2 . GLU A 296 ? 1.0220 1.0220 1.0220 0.0000 0.0000 0.0000 279 GLU B OE2 
2219 N N   . ASN A 297 ? 1.0402 1.0402 1.0402 0.0000 0.0000 0.0000 280 ASN B N   
2220 C CA  . ASN A 297 ? 1.0402 1.0402 1.0402 0.0000 0.0000 0.0000 280 ASN B CA  
2221 C C   . ASN A 297 ? 1.0402 1.0402 1.0402 0.0000 0.0000 0.0000 280 ASN B C   
2222 O O   . ASN A 297 ? 1.0402 1.0402 1.0402 0.0000 0.0000 0.0000 280 ASN B O   
2223 C CB  . ASN A 297 ? 1.0402 1.0402 1.0402 0.0000 0.0000 0.0000 280 ASN B CB  
2224 C CG  . ASN A 297 ? 1.0402 1.0402 1.0402 0.0000 0.0000 0.0000 280 ASN B CG  
2225 O OD1 . ASN A 297 ? 1.0402 1.0402 1.0402 0.0000 0.0000 0.0000 280 ASN B OD1 
2226 N ND2 . ASN A 297 ? 1.0402 1.0402 1.0402 0.0000 0.0000 0.0000 280 ASN B ND2 
2227 N N   . GLU A 298 ? 1.0404 1.0404 1.0404 0.0000 0.0000 0.0000 281 GLU B N   
2228 C CA  . GLU A 298 ? 1.0404 1.0404 1.0404 0.0000 0.0000 0.0000 281 GLU B CA  
2229 C C   . GLU A 298 ? 1.0404 1.0404 1.0404 0.0000 0.0000 0.0000 281 GLU B C   
2230 O O   . GLU A 298 ? 1.0404 1.0404 1.0404 0.0000 0.0000 0.0000 281 GLU B O   
2231 C CB  . GLU A 298 ? 1.0404 1.0404 1.0404 0.0000 0.0000 0.0000 281 GLU B CB  
2232 C CG  . GLU A 298 ? 1.0404 1.0404 1.0404 0.0000 0.0000 0.0000 281 GLU B CG  
2233 C CD  . GLU A 298 ? 1.0404 1.0404 1.0404 0.0000 0.0000 0.0000 281 GLU B CD  
2234 O OE1 . GLU A 298 ? 1.0404 1.0404 1.0404 0.0000 0.0000 0.0000 281 GLU B OE1 
2235 O OE2 . GLU A 298 ? 1.0404 1.0404 1.0404 0.0000 0.0000 0.0000 281 GLU B OE2 
2236 N N   . PHE A 299 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 282 PHE B N   
2237 C CA  . PHE A 299 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 282 PHE B CA  
2238 C C   . PHE A 299 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 282 PHE B C   
2239 O O   . PHE A 299 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 282 PHE B O   
2240 C CB  . PHE A 299 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 282 PHE B CB  
2241 C CG  . PHE A 299 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 282 PHE B CG  
2242 C CD1 . PHE A 299 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 282 PHE B CD1 
2243 C CD2 . PHE A 299 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 282 PHE B CD2 
2244 C CE1 . PHE A 299 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 282 PHE B CE1 
2245 C CE2 . PHE A 299 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 282 PHE B CE2 
2246 C CZ  . PHE A 299 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 282 PHE B CZ  
2247 N N   . ARG A 300 ? 0.9237 0.9237 0.9237 0.0000 0.0000 0.0000 283 ARG B N   
2248 C CA  . ARG A 300 ? 0.9237 0.9237 0.9237 0.0000 0.0000 0.0000 283 ARG B CA  
2249 C C   . ARG A 300 ? 0.9237 0.9237 0.9237 0.0000 0.0000 0.0000 283 ARG B C   
2250 O O   . ARG A 300 ? 0.9237 0.9237 0.9237 0.0000 0.0000 0.0000 283 ARG B O   
2251 C CB  . ARG A 300 ? 0.9237 0.9237 0.9237 0.0000 0.0000 0.0000 283 ARG B CB  
2252 C CG  . ARG A 300 ? 0.9237 0.9237 0.9237 0.0000 0.0000 0.0000 283 ARG B CG  
2253 C CD  . ARG A 300 ? 0.9237 0.9237 0.9237 0.0000 0.0000 0.0000 283 ARG B CD  
2254 N NE  . ARG A 300 ? 0.9237 0.9237 0.9237 0.0000 0.0000 0.0000 283 ARG B NE  
2255 C CZ  . ARG A 300 ? 0.9237 0.9237 0.9237 0.0000 0.0000 0.0000 283 ARG B CZ  
2256 N NH1 . ARG A 300 ? 0.9237 0.9237 0.9237 0.0000 0.0000 0.0000 283 ARG B NH1 
2257 N NH2 . ARG A 300 ? 0.9237 0.9237 0.9237 0.0000 0.0000 0.0000 283 ARG B NH2 
2258 N N   . LEU A 301 ? 0.9320 0.9320 0.9320 0.0000 0.0000 0.0000 284 LEU B N   
2259 C CA  . LEU A 301 ? 0.9320 0.9320 0.9320 0.0000 0.0000 0.0000 284 LEU B CA  
2260 C C   . LEU A 301 ? 0.9320 0.9320 0.9320 0.0000 0.0000 0.0000 284 LEU B C   
2261 O O   . LEU A 301 ? 0.9320 0.9320 0.9320 0.0000 0.0000 0.0000 284 LEU B O   
2262 C CB  . LEU A 301 ? 0.9320 0.9320 0.9320 0.0000 0.0000 0.0000 284 LEU B CB  
2263 C CG  . LEU A 301 ? 0.9320 0.9320 0.9320 0.0000 0.0000 0.0000 284 LEU B CG  
2264 C CD1 . LEU A 301 ? 0.9320 0.9320 0.9320 0.0000 0.0000 0.0000 284 LEU B CD1 
2265 C CD2 . LEU A 301 ? 0.9320 0.9320 0.9320 0.0000 0.0000 0.0000 284 LEU B CD2 
2266 N N   . TYR A 302 ? 0.9288 0.9288 0.9288 0.0000 0.0000 0.0000 285 TYR B N   
2267 C CA  . TYR A 302 ? 0.9288 0.9288 0.9288 0.0000 0.0000 0.0000 285 TYR B CA  
2268 C C   . TYR A 302 ? 0.9288 0.9288 0.9288 0.0000 0.0000 0.0000 285 TYR B C   
2269 O O   . TYR A 302 ? 0.9288 0.9288 0.9288 0.0000 0.0000 0.0000 285 TYR B O   
2270 C CB  . TYR A 302 ? 0.9288 0.9288 0.9288 0.0000 0.0000 0.0000 285 TYR B CB  
2271 C CG  . TYR A 302 ? 0.9288 0.9288 0.9288 0.0000 0.0000 0.0000 285 TYR B CG  
2272 C CD1 . TYR A 302 ? 0.9288 0.9288 0.9288 0.0000 0.0000 0.0000 285 TYR B CD1 
2273 C CD2 . TYR A 302 ? 0.9288 0.9288 0.9288 0.0000 0.0000 0.0000 285 TYR B CD2 
2274 C CE1 . TYR A 302 ? 0.9288 0.9288 0.9288 0.0000 0.0000 0.0000 285 TYR B CE1 
2275 C CE2 . TYR A 302 ? 0.9288 0.9288 0.9288 0.0000 0.0000 0.0000 285 TYR B CE2 
2276 C CZ  . TYR A 302 ? 0.9288 0.9288 0.9288 0.0000 0.0000 0.0000 285 TYR B CZ  
2277 O OH  . TYR A 302 ? 0.9288 0.9288 0.9288 0.0000 0.0000 0.0000 285 TYR B OH  
2278 N N   . TYR A 303 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 286 TYR B N   
2279 C CA  . TYR A 303 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 286 TYR B CA  
2280 C C   . TYR A 303 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 286 TYR B C   
2281 O O   . TYR A 303 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 286 TYR B O   
2282 C CB  . TYR A 303 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 286 TYR B CB  
2283 C CG  . TYR A 303 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 286 TYR B CG  
2284 C CD1 . TYR A 303 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 286 TYR B CD1 
2285 C CD2 . TYR A 303 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 286 TYR B CD2 
2286 C CE1 . TYR A 303 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 286 TYR B CE1 
2287 C CE2 . TYR A 303 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 286 TYR B CE2 
2288 C CZ  . TYR A 303 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 286 TYR B CZ  
2289 O OH  . TYR A 303 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 286 TYR B OH  
2290 N N   . TYR A 304 ? 0.9349 0.9349 0.9349 0.0000 0.0000 0.0000 287 TYR B N   
2291 C CA  . TYR A 304 ? 0.9349 0.9349 0.9349 0.0000 0.0000 0.0000 287 TYR B CA  
2292 C C   . TYR A 304 ? 0.9349 0.9349 0.9349 0.0000 0.0000 0.0000 287 TYR B C   
2293 O O   . TYR A 304 ? 0.9349 0.9349 0.9349 0.0000 0.0000 0.0000 287 TYR B O   
2294 C CB  . TYR A 304 ? 0.9349 0.9349 0.9349 0.0000 0.0000 0.0000 287 TYR B CB  
2295 C CG  . TYR A 304 ? 0.9349 0.9349 0.9349 0.0000 0.0000 0.0000 287 TYR B CG  
2296 C CD1 . TYR A 304 ? 0.9349 0.9349 0.9349 0.0000 0.0000 0.0000 287 TYR B CD1 
2297 C CD2 . TYR A 304 ? 0.9349 0.9349 0.9349 0.0000 0.0000 0.0000 287 TYR B CD2 
2298 C CE1 . TYR A 304 ? 0.9349 0.9349 0.9349 0.0000 0.0000 0.0000 287 TYR B CE1 
2299 C CE2 . TYR A 304 ? 0.9349 0.9349 0.9349 0.0000 0.0000 0.0000 287 TYR B CE2 
2300 C CZ  . TYR A 304 ? 0.9349 0.9349 0.9349 0.0000 0.0000 0.0000 287 TYR B CZ  
2301 O OH  . TYR A 304 ? 0.9349 0.9349 0.9349 0.0000 0.0000 0.0000 287 TYR B OH  
2302 N N   . ASN A 305 ? 0.9302 0.9302 0.9302 0.0000 0.0000 0.0000 288 ASN B N   
2303 C CA  . ASN A 305 ? 0.9302 0.9302 0.9302 0.0000 0.0000 0.0000 288 ASN B CA  
2304 C C   . ASN A 305 ? 0.9302 0.9302 0.9302 0.0000 0.0000 0.0000 288 ASN B C   
2305 O O   . ASN A 305 ? 0.9302 0.9302 0.9302 0.0000 0.0000 0.0000 288 ASN B O   
2306 C CB  . ASN A 305 ? 0.9302 0.9302 0.9302 0.0000 0.0000 0.0000 288 ASN B CB  
2307 C CG  . ASN A 305 ? 0.9302 0.9302 0.9302 0.0000 0.0000 0.0000 288 ASN B CG  
2308 O OD1 . ASN A 305 ? 0.9302 0.9302 0.9302 0.0000 0.0000 0.0000 288 ASN B OD1 
2309 N ND2 . ASN A 305 ? 0.9302 0.9302 0.9302 0.0000 0.0000 0.0000 288 ASN B ND2 
2310 N N   . LYS A 306 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 289 LYS B N   
2311 C CA  . LYS A 306 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 289 LYS B CA  
2312 C C   . LYS A 306 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 289 LYS B C   
2313 O O   . LYS A 306 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 289 LYS B O   
2314 C CB  . LYS A 306 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 289 LYS B CB  
2315 C CG  . LYS A 306 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 289 LYS B CG  
2316 C CD  . LYS A 306 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 289 LYS B CD  
2317 C CE  . LYS A 306 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 289 LYS B CE  
2318 N NZ  . LYS A 306 ? 0.9084 0.9084 0.9084 0.0000 0.0000 0.0000 289 LYS B NZ  
2319 N N   . PHE A 307 ? 0.8869 0.8869 0.8869 0.0000 0.0000 0.0000 290 PHE B N   
2320 C CA  . PHE A 307 ? 0.8869 0.8869 0.8869 0.0000 0.0000 0.0000 290 PHE B CA  
2321 C C   . PHE A 307 ? 0.8869 0.8869 0.8869 0.0000 0.0000 0.0000 290 PHE B C   
2322 O O   . PHE A 307 ? 0.8869 0.8869 0.8869 0.0000 0.0000 0.0000 290 PHE B O   
2323 C CB  . PHE A 307 ? 0.8869 0.8869 0.8869 0.0000 0.0000 0.0000 290 PHE B CB  
2324 C CG  . PHE A 307 ? 0.8869 0.8869 0.8869 0.0000 0.0000 0.0000 290 PHE B CG  
2325 C CD1 . PHE A 307 ? 0.8869 0.8869 0.8869 0.0000 0.0000 0.0000 290 PHE B CD1 
2326 C CD2 . PHE A 307 ? 0.8869 0.8869 0.8869 0.0000 0.0000 0.0000 290 PHE B CD2 
2327 C CE1 . PHE A 307 ? 0.8869 0.8869 0.8869 0.0000 0.0000 0.0000 290 PHE B CE1 
2328 C CE2 . PHE A 307 ? 0.8869 0.8869 0.8869 0.0000 0.0000 0.0000 290 PHE B CE2 
2329 C CZ  . PHE A 307 ? 0.8869 0.8869 0.8869 0.0000 0.0000 0.0000 290 PHE B CZ  
2330 N N   . LYS A 308 ? 0.9747 0.9747 0.9747 0.0000 0.0000 0.0000 291 LYS B N   
2331 C CA  . LYS A 308 ? 0.9747 0.9747 0.9747 0.0000 0.0000 0.0000 291 LYS B CA  
2332 C C   . LYS A 308 ? 0.9747 0.9747 0.9747 0.0000 0.0000 0.0000 291 LYS B C   
2333 O O   . LYS A 308 ? 0.9747 0.9747 0.9747 0.0000 0.0000 0.0000 291 LYS B O   
2334 C CB  . LYS A 308 ? 0.9747 0.9747 0.9747 0.0000 0.0000 0.0000 291 LYS B CB  
2335 C CG  . LYS A 308 ? 0.9747 0.9747 0.9747 0.0000 0.0000 0.0000 291 LYS B CG  
2336 C CD  . LYS A 308 ? 0.9747 0.9747 0.9747 0.0000 0.0000 0.0000 291 LYS B CD  
2337 C CE  . LYS A 308 ? 0.9747 0.9747 0.9747 0.0000 0.0000 0.0000 291 LYS B CE  
2338 N NZ  . LYS A 308 ? 0.9747 0.9747 0.9747 0.0000 0.0000 0.0000 291 LYS B NZ  
2339 N N   . ASP A 309 ? 0.9811 0.9811 0.9811 0.0000 0.0000 0.0000 292 ASP B N   
2340 C CA  . ASP A 309 ? 0.9811 0.9811 0.9811 0.0000 0.0000 0.0000 292 ASP B CA  
2341 C C   . ASP A 309 ? 0.9811 0.9811 0.9811 0.0000 0.0000 0.0000 292 ASP B C   
2342 O O   . ASP A 309 ? 0.9811 0.9811 0.9811 0.0000 0.0000 0.0000 292 ASP B O   
2343 C CB  . ASP A 309 ? 0.9811 0.9811 0.9811 0.0000 0.0000 0.0000 292 ASP B CB  
2344 C CG  . ASP A 309 ? 0.9811 0.9811 0.9811 0.0000 0.0000 0.0000 292 ASP B CG  
2345 O OD1 . ASP A 309 ? 0.9811 0.9811 0.9811 0.0000 0.0000 0.0000 292 ASP B OD1 
2346 O OD2 . ASP A 309 ? 0.9811 0.9811 0.9811 0.0000 0.0000 0.0000 292 ASP B OD2 
2347 N N   . ILE A 310 ? 0.9571 0.9571 0.9571 0.0000 0.0000 0.0000 293 ILE B N   
2348 C CA  . ILE A 310 ? 0.9571 0.9571 0.9571 0.0000 0.0000 0.0000 293 ILE B CA  
2349 C C   . ILE A 310 ? 0.9571 0.9571 0.9571 0.0000 0.0000 0.0000 293 ILE B C   
2350 O O   . ILE A 310 ? 0.9571 0.9571 0.9571 0.0000 0.0000 0.0000 293 ILE B O   
2351 C CB  . ILE A 310 ? 0.9571 0.9571 0.9571 0.0000 0.0000 0.0000 293 ILE B CB  
2352 C CG1 . ILE A 310 ? 0.9571 0.9571 0.9571 0.0000 0.0000 0.0000 293 ILE B CG1 
2353 C CG2 . ILE A 310 ? 0.9571 0.9571 0.9571 0.0000 0.0000 0.0000 293 ILE B CG2 
2354 C CD1 . ILE A 310 ? 0.9571 0.9571 0.9571 0.0000 0.0000 0.0000 293 ILE B CD1 
2355 N N   . ALA A 311 ? 1.0222 1.0222 1.0222 0.0000 0.0000 0.0000 294 ALA B N   
2356 C CA  . ALA A 311 ? 1.0222 1.0222 1.0222 0.0000 0.0000 0.0000 294 ALA B CA  
2357 C C   . ALA A 311 ? 1.0222 1.0222 1.0222 0.0000 0.0000 0.0000 294 ALA B C   
2358 O O   . ALA A 311 ? 1.0222 1.0222 1.0222 0.0000 0.0000 0.0000 294 ALA B O   
2359 C CB  . ALA A 311 ? 1.0222 1.0222 1.0222 0.0000 0.0000 0.0000 294 ALA B CB  
2360 N N   . SER A 312 ? 1.0425 1.0425 1.0425 0.0000 0.0000 0.0000 295 SER B N   
2361 C CA  . SER A 312 ? 1.0425 1.0425 1.0425 0.0000 0.0000 0.0000 295 SER B CA  
2362 C C   . SER A 312 ? 1.0425 1.0425 1.0425 0.0000 0.0000 0.0000 295 SER B C   
2363 O O   . SER A 312 ? 1.0425 1.0425 1.0425 0.0000 0.0000 0.0000 295 SER B O   
2364 C CB  . SER A 312 ? 1.0425 1.0425 1.0425 0.0000 0.0000 0.0000 295 SER B CB  
2365 O OG  . SER A 312 ? 1.0425 1.0425 1.0425 0.0000 0.0000 0.0000 295 SER B OG  
2366 N N   . THR A 313 ? 1.0471 1.0471 1.0471 0.0000 0.0000 0.0000 296 THR B N   
2367 C CA  . THR A 313 ? 1.0471 1.0471 1.0471 0.0000 0.0000 0.0000 296 THR B CA  
2368 C C   . THR A 313 ? 1.0471 1.0471 1.0471 0.0000 0.0000 0.0000 296 THR B C   
2369 O O   . THR A 313 ? 1.0471 1.0471 1.0471 0.0000 0.0000 0.0000 296 THR B O   
2370 C CB  . THR A 313 ? 1.0471 1.0471 1.0471 0.0000 0.0000 0.0000 296 THR B CB  
2371 O OG1 . THR A 313 ? 1.0471 1.0471 1.0471 0.0000 0.0000 0.0000 296 THR B OG1 
2372 C CG2 . THR A 313 ? 1.0471 1.0471 1.0471 0.0000 0.0000 0.0000 296 THR B CG2 
2373 N N   . LEU A 314 ? 1.0581 1.0581 1.0581 0.0000 0.0000 0.0000 297 LEU B N   
2374 C CA  . LEU A 314 ? 1.0581 1.0581 1.0581 0.0000 0.0000 0.0000 297 LEU B CA  
2375 C C   . LEU A 314 ? 1.0581 1.0581 1.0581 0.0000 0.0000 0.0000 297 LEU B C   
2376 O O   . LEU A 314 ? 1.0581 1.0581 1.0581 0.0000 0.0000 0.0000 297 LEU B O   
2377 C CB  . LEU A 314 ? 1.0581 1.0581 1.0581 0.0000 0.0000 0.0000 297 LEU B CB  
2378 C CG  . LEU A 314 ? 1.0581 1.0581 1.0581 0.0000 0.0000 0.0000 297 LEU B CG  
2379 C CD1 . LEU A 314 ? 1.0581 1.0581 1.0581 0.0000 0.0000 0.0000 297 LEU B CD1 
2380 C CD2 . LEU A 314 ? 1.0581 1.0581 1.0581 0.0000 0.0000 0.0000 297 LEU B CD2 
2381 N N   . ASN A 315 ? 1.1318 1.1318 1.1318 0.0000 0.0000 0.0000 298 ASN B N   
2382 C CA  . ASN A 315 ? 1.1318 1.1318 1.1318 0.0000 0.0000 0.0000 298 ASN B CA  
2383 C C   . ASN A 315 ? 1.1318 1.1318 1.1318 0.0000 0.0000 0.0000 298 ASN B C   
2384 O O   . ASN A 315 ? 1.1318 1.1318 1.1318 0.0000 0.0000 0.0000 298 ASN B O   
2385 C CB  . ASN A 315 ? 1.1318 1.1318 1.1318 0.0000 0.0000 0.0000 298 ASN B CB  
2386 C CG  . ASN A 315 ? 1.1318 1.1318 1.1318 0.0000 0.0000 0.0000 298 ASN B CG  
2387 O OD1 . ASN A 315 ? 1.1318 1.1318 1.1318 0.0000 0.0000 0.0000 298 ASN B OD1 
2388 N ND2 . ASN A 315 ? 1.1318 1.1318 1.1318 0.0000 0.0000 0.0000 298 ASN B ND2 
2389 N N   . LYS A 316 ? 1.1915 1.1915 1.1915 0.0000 0.0000 0.0000 299 LYS B N   
2390 C CA  . LYS A 316 ? 1.1915 1.1915 1.1915 0.0000 0.0000 0.0000 299 LYS B CA  
2391 C C   . LYS A 316 ? 1.1915 1.1915 1.1915 0.0000 0.0000 0.0000 299 LYS B C   
2392 O O   . LYS A 316 ? 1.1915 1.1915 1.1915 0.0000 0.0000 0.0000 299 LYS B O   
2393 C CB  . LYS A 316 ? 1.1915 1.1915 1.1915 0.0000 0.0000 0.0000 299 LYS B CB  
2394 C CG  . LYS A 316 ? 1.1915 1.1915 1.1915 0.0000 0.0000 0.0000 299 LYS B CG  
2395 C CD  . LYS A 316 ? 1.1915 1.1915 1.1915 0.0000 0.0000 0.0000 299 LYS B CD  
2396 C CE  . LYS A 316 ? 1.1915 1.1915 1.1915 0.0000 0.0000 0.0000 299 LYS B CE  
2397 N NZ  . LYS A 316 ? 1.1915 1.1915 1.1915 0.0000 0.0000 0.0000 299 LYS B NZ  
2398 N N   . ALA A 317 ? 1.2088 1.2088 1.2088 0.0000 0.0000 0.0000 300 ALA B N   
2399 C CA  . ALA A 317 ? 1.2088 1.2088 1.2088 0.0000 0.0000 0.0000 300 ALA B CA  
2400 C C   . ALA A 317 ? 1.2088 1.2088 1.2088 0.0000 0.0000 0.0000 300 ALA B C   
2401 O O   . ALA A 317 ? 1.2088 1.2088 1.2088 0.0000 0.0000 0.0000 300 ALA B O   
2402 C CB  . ALA A 317 ? 1.2088 1.2088 1.2088 0.0000 0.0000 0.0000 300 ALA B CB  
2403 N N   . LYS A 318 ? 1.2347 1.2347 1.2347 0.0000 0.0000 0.0000 301 LYS B N   
2404 C CA  . LYS A 318 ? 1.2347 1.2347 1.2347 0.0000 0.0000 0.0000 301 LYS B CA  
2405 C C   . LYS A 318 ? 1.2347 1.2347 1.2347 0.0000 0.0000 0.0000 301 LYS B C   
2406 O O   . LYS A 318 ? 1.2347 1.2347 1.2347 0.0000 0.0000 0.0000 301 LYS B O   
2407 C CB  . LYS A 318 ? 1.2347 1.2347 1.2347 0.0000 0.0000 0.0000 301 LYS B CB  
2408 C CG  . LYS A 318 ? 1.2347 1.2347 1.2347 0.0000 0.0000 0.0000 301 LYS B CG  
2409 C CD  . LYS A 318 ? 1.2347 1.2347 1.2347 0.0000 0.0000 0.0000 301 LYS B CD  
2410 C CE  . LYS A 318 ? 1.2347 1.2347 1.2347 0.0000 0.0000 0.0000 301 LYS B CE  
2411 N NZ  . LYS A 318 ? 1.2347 1.2347 1.2347 0.0000 0.0000 0.0000 301 LYS B NZ  
2412 N N   . SER A 319 ? 1.2640 1.2640 1.2640 0.0000 0.0000 0.0000 302 SER B N   
2413 C CA  . SER A 319 ? 1.2640 1.2640 1.2640 0.0000 0.0000 0.0000 302 SER B CA  
2414 C C   . SER A 319 ? 1.2640 1.2640 1.2640 0.0000 0.0000 0.0000 302 SER B C   
2415 O O   . SER A 319 ? 1.2640 1.2640 1.2640 0.0000 0.0000 0.0000 302 SER B O   
2416 C CB  . SER A 319 ? 1.2640 1.2640 1.2640 0.0000 0.0000 0.0000 302 SER B CB  
2417 O OG  . SER A 319 ? 1.2640 1.2640 1.2640 0.0000 0.0000 0.0000 302 SER B OG  
2418 N N   . ILE A 320 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 303 ILE B N   
2419 C CA  . ILE A 320 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 303 ILE B CA  
2420 C C   . ILE A 320 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 303 ILE B C   
2421 O O   . ILE A 320 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 303 ILE B O   
2422 C CB  . ILE A 320 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 303 ILE B CB  
2423 C CG1 . ILE A 320 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 303 ILE B CG1 
2424 C CG2 . ILE A 320 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 303 ILE B CG2 
2425 C CD1 . ILE A 320 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 303 ILE B CD1 
2426 N N   . VAL A 321 ? 1.2281 1.2281 1.2281 0.0000 0.0000 0.0000 304 VAL B N   
2427 C CA  . VAL A 321 ? 1.2281 1.2281 1.2281 0.0000 0.0000 0.0000 304 VAL B CA  
2428 C C   . VAL A 321 ? 1.2281 1.2281 1.2281 0.0000 0.0000 0.0000 304 VAL B C   
2429 O O   . VAL A 321 ? 1.2281 1.2281 1.2281 0.0000 0.0000 0.0000 304 VAL B O   
2430 C CB  . VAL A 321 ? 1.2281 1.2281 1.2281 0.0000 0.0000 0.0000 304 VAL B CB  
2431 C CG1 . VAL A 321 ? 1.2281 1.2281 1.2281 0.0000 0.0000 0.0000 304 VAL B CG1 
2432 C CG2 . VAL A 321 ? 1.2281 1.2281 1.2281 0.0000 0.0000 0.0000 304 VAL B CG2 
2433 N N   . GLY A 322 ? 1.2098 1.2098 1.2098 0.0000 0.0000 0.0000 305 GLY B N   
2434 C CA  . GLY A 322 ? 1.2098 1.2098 1.2098 0.0000 0.0000 0.0000 305 GLY B CA  
2435 C C   . GLY A 322 ? 1.2098 1.2098 1.2098 0.0000 0.0000 0.0000 305 GLY B C   
2436 O O   . GLY A 322 ? 1.2098 1.2098 1.2098 0.0000 0.0000 0.0000 305 GLY B O   
2437 N N   . THR A 323 ? 1.2523 1.2523 1.2523 0.0000 0.0000 0.0000 306 THR B N   
2438 C CA  . THR A 323 ? 1.2523 1.2523 1.2523 0.0000 0.0000 0.0000 306 THR B CA  
2439 C C   . THR A 323 ? 1.2523 1.2523 1.2523 0.0000 0.0000 0.0000 306 THR B C   
2440 O O   . THR A 323 ? 1.2523 1.2523 1.2523 0.0000 0.0000 0.0000 306 THR B O   
2441 C CB  . THR A 323 ? 1.2523 1.2523 1.2523 0.0000 0.0000 0.0000 306 THR B CB  
2442 O OG1 . THR A 323 ? 1.2523 1.2523 1.2523 0.0000 0.0000 0.0000 306 THR B OG1 
2443 C CG2 . THR A 323 ? 1.2523 1.2523 1.2523 0.0000 0.0000 0.0000 306 THR B CG2 
2444 N N   . THR A 324 ? 1.2537 1.2537 1.2537 0.0000 0.0000 0.0000 307 THR B N   
2445 C CA  . THR A 324 ? 1.2537 1.2537 1.2537 0.0000 0.0000 0.0000 307 THR B CA  
2446 C C   . THR A 324 ? 1.2537 1.2537 1.2537 0.0000 0.0000 0.0000 307 THR B C   
2447 O O   . THR A 324 ? 1.2537 1.2537 1.2537 0.0000 0.0000 0.0000 307 THR B O   
2448 C CB  . THR A 324 ? 1.2537 1.2537 1.2537 0.0000 0.0000 0.0000 307 THR B CB  
2449 O OG1 . THR A 324 ? 1.2537 1.2537 1.2537 0.0000 0.0000 0.0000 307 THR B OG1 
2450 C CG2 . THR A 324 ? 1.2537 1.2537 1.2537 0.0000 0.0000 0.0000 307 THR B CG2 
2451 N N   . ALA A 325 ? 1.2437 1.2437 1.2437 0.0000 0.0000 0.0000 308 ALA B N   
2452 C CA  . ALA A 325 ? 1.2437 1.2437 1.2437 0.0000 0.0000 0.0000 308 ALA B CA  
2453 C C   . ALA A 325 ? 1.2437 1.2437 1.2437 0.0000 0.0000 0.0000 308 ALA B C   
2454 O O   . ALA A 325 ? 1.2437 1.2437 1.2437 0.0000 0.0000 0.0000 308 ALA B O   
2455 C CB  . ALA A 325 ? 1.2437 1.2437 1.2437 0.0000 0.0000 0.0000 308 ALA B CB  
2456 N N   . SER A 326 ? 1.1937 1.1937 1.1937 0.0000 0.0000 0.0000 309 SER B N   
2457 C CA  . SER A 326 ? 1.1937 1.1937 1.1937 0.0000 0.0000 0.0000 309 SER B CA  
2458 C C   . SER A 326 ? 1.1937 1.1937 1.1937 0.0000 0.0000 0.0000 309 SER B C   
2459 O O   . SER A 326 ? 1.1937 1.1937 1.1937 0.0000 0.0000 0.0000 309 SER B O   
2460 C CB  . SER A 326 ? 1.1937 1.1937 1.1937 0.0000 0.0000 0.0000 309 SER B CB  
2461 O OG  . SER A 326 ? 1.1937 1.1937 1.1937 0.0000 0.0000 0.0000 309 SER B OG  
2462 N N   . LEU A 327 ? 1.1229 1.1229 1.1229 0.0000 0.0000 0.0000 310 LEU B N   
2463 C CA  . LEU A 327 ? 1.1229 1.1229 1.1229 0.0000 0.0000 0.0000 310 LEU B CA  
2464 C C   . LEU A 327 ? 1.1229 1.1229 1.1229 0.0000 0.0000 0.0000 310 LEU B C   
2465 O O   . LEU A 327 ? 1.1229 1.1229 1.1229 0.0000 0.0000 0.0000 310 LEU B O   
2466 C CB  . LEU A 327 ? 1.1229 1.1229 1.1229 0.0000 0.0000 0.0000 310 LEU B CB  
2467 C CG  . LEU A 327 ? 1.1229 1.1229 1.1229 0.0000 0.0000 0.0000 310 LEU B CG  
2468 C CD1 . LEU A 327 ? 1.1229 1.1229 1.1229 0.0000 0.0000 0.0000 310 LEU B CD1 
2469 C CD2 . LEU A 327 ? 1.1229 1.1229 1.1229 0.0000 0.0000 0.0000 310 LEU B CD2 
2470 N N   . GLN A 328 ? 1.1355 1.1355 1.1355 0.0000 0.0000 0.0000 311 GLN B N   
2471 C CA  . GLN A 328 ? 1.1355 1.1355 1.1355 0.0000 0.0000 0.0000 311 GLN B CA  
2472 C C   . GLN A 328 ? 1.1355 1.1355 1.1355 0.0000 0.0000 0.0000 311 GLN B C   
2473 O O   . GLN A 328 ? 1.1355 1.1355 1.1355 0.0000 0.0000 0.0000 311 GLN B O   
2474 C CB  . GLN A 328 ? 1.1355 1.1355 1.1355 0.0000 0.0000 0.0000 311 GLN B CB  
2475 C CG  . GLN A 328 ? 1.1355 1.1355 1.1355 0.0000 0.0000 0.0000 311 GLN B CG  
2476 C CD  . GLN A 328 ? 1.1355 1.1355 1.1355 0.0000 0.0000 0.0000 311 GLN B CD  
2477 O OE1 . GLN A 328 ? 1.1355 1.1355 1.1355 0.0000 0.0000 0.0000 311 GLN B OE1 
2478 N NE2 . GLN A 328 ? 1.1355 1.1355 1.1355 0.0000 0.0000 0.0000 311 GLN B NE2 
2479 N N   . TYR A 329 ? 1.1713 1.1713 1.1713 0.0000 0.0000 0.0000 312 TYR B N   
2480 C CA  . TYR A 329 ? 1.1713 1.1713 1.1713 0.0000 0.0000 0.0000 312 TYR B CA  
2481 C C   . TYR A 329 ? 1.1713 1.1713 1.1713 0.0000 0.0000 0.0000 312 TYR B C   
2482 O O   . TYR A 329 ? 1.1713 1.1713 1.1713 0.0000 0.0000 0.0000 312 TYR B O   
2483 C CB  . TYR A 329 ? 1.1713 1.1713 1.1713 0.0000 0.0000 0.0000 312 TYR B CB  
2484 C CG  . TYR A 329 ? 1.1713 1.1713 1.1713 0.0000 0.0000 0.0000 312 TYR B CG  
2485 C CD1 . TYR A 329 ? 1.1713 1.1713 1.1713 0.0000 0.0000 0.0000 312 TYR B CD1 
2486 C CD2 . TYR A 329 ? 1.1713 1.1713 1.1713 0.0000 0.0000 0.0000 312 TYR B CD2 
2487 C CE1 . TYR A 329 ? 1.1713 1.1713 1.1713 0.0000 0.0000 0.0000 312 TYR B CE1 
2488 C CE2 . TYR A 329 ? 1.1713 1.1713 1.1713 0.0000 0.0000 0.0000 312 TYR B CE2 
2489 C CZ  . TYR A 329 ? 1.1713 1.1713 1.1713 0.0000 0.0000 0.0000 312 TYR B CZ  
2490 O OH  . TYR A 329 ? 1.1713 1.1713 1.1713 0.0000 0.0000 0.0000 312 TYR B OH  
2491 N N   . MET A 330 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 313 MET B N   
2492 C CA  . MET A 330 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 313 MET B CA  
2493 C C   . MET A 330 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 313 MET B C   
2494 O O   . MET A 330 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 313 MET B O   
2495 C CB  . MET A 330 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 313 MET B CB  
2496 C CG  . MET A 330 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 313 MET B CG  
2497 S SD  . MET A 330 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 313 MET B SD  
2498 C CE  . MET A 330 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 313 MET B CE  
2499 N N   . LYS A 331 ? 1.0881 1.0881 1.0881 0.0000 0.0000 0.0000 314 LYS B N   
2500 C CA  . LYS A 331 ? 1.0881 1.0881 1.0881 0.0000 0.0000 0.0000 314 LYS B CA  
2501 C C   . LYS A 331 ? 1.0881 1.0881 1.0881 0.0000 0.0000 0.0000 314 LYS B C   
2502 O O   . LYS A 331 ? 1.0881 1.0881 1.0881 0.0000 0.0000 0.0000 314 LYS B O   
2503 C CB  . LYS A 331 ? 1.0881 1.0881 1.0881 0.0000 0.0000 0.0000 314 LYS B CB  
2504 C CG  . LYS A 331 ? 1.0881 1.0881 1.0881 0.0000 0.0000 0.0000 314 LYS B CG  
2505 C CD  . LYS A 331 ? 1.0881 1.0881 1.0881 0.0000 0.0000 0.0000 314 LYS B CD  
2506 C CE  . LYS A 331 ? 1.0881 1.0881 1.0881 0.0000 0.0000 0.0000 314 LYS B CE  
2507 N NZ  . LYS A 331 ? 1.0881 1.0881 1.0881 0.0000 0.0000 0.0000 314 LYS B NZ  
2508 N N   . ASN A 332 ? 1.0376 1.0376 1.0376 0.0000 0.0000 0.0000 315 ASN B N   
2509 C CA  . ASN A 332 ? 1.0376 1.0376 1.0376 0.0000 0.0000 0.0000 315 ASN B CA  
2510 C C   . ASN A 332 ? 1.0376 1.0376 1.0376 0.0000 0.0000 0.0000 315 ASN B C   
2511 O O   . ASN A 332 ? 1.0376 1.0376 1.0376 0.0000 0.0000 0.0000 315 ASN B O   
2512 C CB  . ASN A 332 ? 1.0376 1.0376 1.0376 0.0000 0.0000 0.0000 315 ASN B CB  
2513 C CG  . ASN A 332 ? 1.0376 1.0376 1.0376 0.0000 0.0000 0.0000 315 ASN B CG  
2514 O OD1 . ASN A 332 ? 1.0376 1.0376 1.0376 0.0000 0.0000 0.0000 315 ASN B OD1 
2515 N ND2 . ASN A 332 ? 1.0376 1.0376 1.0376 0.0000 0.0000 0.0000 315 ASN B ND2 
2516 N N   . VAL A 333 ? 1.0387 1.0387 1.0387 0.0000 0.0000 0.0000 316 VAL B N   
2517 C CA  . VAL A 333 ? 1.0387 1.0387 1.0387 0.0000 0.0000 0.0000 316 VAL B CA  
2518 C C   . VAL A 333 ? 1.0387 1.0387 1.0387 0.0000 0.0000 0.0000 316 VAL B C   
2519 O O   . VAL A 333 ? 1.0387 1.0387 1.0387 0.0000 0.0000 0.0000 316 VAL B O   
2520 C CB  . VAL A 333 ? 1.0387 1.0387 1.0387 0.0000 0.0000 0.0000 316 VAL B CB  
2521 C CG1 . VAL A 333 ? 1.0387 1.0387 1.0387 0.0000 0.0000 0.0000 316 VAL B CG1 
2522 C CG2 . VAL A 333 ? 1.0387 1.0387 1.0387 0.0000 0.0000 0.0000 316 VAL B CG2 
2523 N N   . PHE A 334 ? 0.9961 0.9961 0.9961 0.0000 0.0000 0.0000 317 PHE B N   
2524 C CA  . PHE A 334 ? 0.9961 0.9961 0.9961 0.0000 0.0000 0.0000 317 PHE B CA  
2525 C C   . PHE A 334 ? 0.9961 0.9961 0.9961 0.0000 0.0000 0.0000 317 PHE B C   
2526 O O   . PHE A 334 ? 0.9961 0.9961 0.9961 0.0000 0.0000 0.0000 317 PHE B O   
2527 C CB  . PHE A 334 ? 0.9961 0.9961 0.9961 0.0000 0.0000 0.0000 317 PHE B CB  
2528 C CG  . PHE A 334 ? 0.9961 0.9961 0.9961 0.0000 0.0000 0.0000 317 PHE B CG  
2529 C CD1 . PHE A 334 ? 0.9961 0.9961 0.9961 0.0000 0.0000 0.0000 317 PHE B CD1 
2530 C CD2 . PHE A 334 ? 0.9961 0.9961 0.9961 0.0000 0.0000 0.0000 317 PHE B CD2 
2531 C CE1 . PHE A 334 ? 0.9961 0.9961 0.9961 0.0000 0.0000 0.0000 317 PHE B CE1 
2532 C CE2 . PHE A 334 ? 0.9961 0.9961 0.9961 0.0000 0.0000 0.0000 317 PHE B CE2 
2533 C CZ  . PHE A 334 ? 0.9961 0.9961 0.9961 0.0000 0.0000 0.0000 317 PHE B CZ  
2534 N N   . LYS A 335 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 318 LYS B N   
2535 C CA  . LYS A 335 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 318 LYS B CA  
2536 C C   . LYS A 335 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 318 LYS B C   
2537 O O   . LYS A 335 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 318 LYS B O   
2538 C CB  . LYS A 335 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 318 LYS B CB  
2539 C CG  . LYS A 335 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 318 LYS B CG  
2540 C CD  . LYS A 335 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 318 LYS B CD  
2541 C CE  . LYS A 335 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 318 LYS B CE  
2542 N NZ  . LYS A 335 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 318 LYS B NZ  
2543 N N   . GLU A 336 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 319 GLU B N   
2544 C CA  . GLU A 336 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 319 GLU B CA  
2545 C C   . GLU A 336 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 319 GLU B C   
2546 O O   . GLU A 336 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 319 GLU B O   
2547 C CB  . GLU A 336 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 319 GLU B CB  
2548 C CG  . GLU A 336 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 319 GLU B CG  
2549 C CD  . GLU A 336 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 319 GLU B CD  
2550 O OE1 . GLU A 336 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 319 GLU B OE1 
2551 O OE2 . GLU A 336 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 319 GLU B OE2 
2552 N N   . LYS A 337 ? 0.9058 0.9058 0.9058 0.0000 0.0000 0.0000 320 LYS B N   
2553 C CA  . LYS A 337 ? 0.9058 0.9058 0.9058 0.0000 0.0000 0.0000 320 LYS B CA  
2554 C C   . LYS A 337 ? 0.9058 0.9058 0.9058 0.0000 0.0000 0.0000 320 LYS B C   
2555 O O   . LYS A 337 ? 0.9058 0.9058 0.9058 0.0000 0.0000 0.0000 320 LYS B O   
2556 C CB  . LYS A 337 ? 0.9058 0.9058 0.9058 0.0000 0.0000 0.0000 320 LYS B CB  
2557 C CG  . LYS A 337 ? 0.9058 0.9058 0.9058 0.0000 0.0000 0.0000 320 LYS B CG  
2558 C CD  . LYS A 337 ? 0.9058 0.9058 0.9058 0.0000 0.0000 0.0000 320 LYS B CD  
2559 C CE  . LYS A 337 ? 0.9058 0.9058 0.9058 0.0000 0.0000 0.0000 320 LYS B CE  
2560 N NZ  . LYS A 337 ? 0.9058 0.9058 0.9058 0.0000 0.0000 0.0000 320 LYS B NZ  
2561 N N   . TYR A 338 ? 0.8977 0.8977 0.8977 0.0000 0.0000 0.0000 321 TYR B N   
2562 C CA  . TYR A 338 ? 0.8977 0.8977 0.8977 0.0000 0.0000 0.0000 321 TYR B CA  
2563 C C   . TYR A 338 ? 0.8977 0.8977 0.8977 0.0000 0.0000 0.0000 321 TYR B C   
2564 O O   . TYR A 338 ? 0.8977 0.8977 0.8977 0.0000 0.0000 0.0000 321 TYR B O   
2565 C CB  . TYR A 338 ? 0.8977 0.8977 0.8977 0.0000 0.0000 0.0000 321 TYR B CB  
2566 C CG  . TYR A 338 ? 0.8977 0.8977 0.8977 0.0000 0.0000 0.0000 321 TYR B CG  
2567 C CD1 . TYR A 338 ? 0.8977 0.8977 0.8977 0.0000 0.0000 0.0000 321 TYR B CD1 
2568 C CD2 . TYR A 338 ? 0.8977 0.8977 0.8977 0.0000 0.0000 0.0000 321 TYR B CD2 
2569 C CE1 . TYR A 338 ? 0.8977 0.8977 0.8977 0.0000 0.0000 0.0000 321 TYR B CE1 
2570 C CE2 . TYR A 338 ? 0.8977 0.8977 0.8977 0.0000 0.0000 0.0000 321 TYR B CE2 
2571 C CZ  . TYR A 338 ? 0.8977 0.8977 0.8977 0.0000 0.0000 0.0000 321 TYR B CZ  
2572 O OH  . TYR A 338 ? 0.8977 0.8977 0.8977 0.0000 0.0000 0.0000 321 TYR B OH  
2573 N N   . LEU A 339 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 322 LEU B N   
2574 C CA  . LEU A 339 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 322 LEU B CA  
2575 C C   . LEU A 339 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 322 LEU B C   
2576 O O   . LEU A 339 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 322 LEU B O   
2577 C CB  . LEU A 339 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 322 LEU B CB  
2578 C CG  . LEU A 339 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 322 LEU B CG  
2579 C CD1 . LEU A 339 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 322 LEU B CD1 
2580 C CD2 . LEU A 339 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 322 LEU B CD2 
2581 N N   . LEU A 340 ? 0.9939 0.9939 0.9939 0.0000 0.0000 0.0000 323 LEU B N   
2582 C CA  . LEU A 340 ? 0.9939 0.9939 0.9939 0.0000 0.0000 0.0000 323 LEU B CA  
2583 C C   . LEU A 340 ? 0.9939 0.9939 0.9939 0.0000 0.0000 0.0000 323 LEU B C   
2584 O O   . LEU A 340 ? 0.9939 0.9939 0.9939 0.0000 0.0000 0.0000 323 LEU B O   
2585 C CB  . LEU A 340 ? 0.9939 0.9939 0.9939 0.0000 0.0000 0.0000 323 LEU B CB  
2586 C CG  . LEU A 340 ? 0.9939 0.9939 0.9939 0.0000 0.0000 0.0000 323 LEU B CG  
2587 C CD1 . LEU A 340 ? 0.9939 0.9939 0.9939 0.0000 0.0000 0.0000 323 LEU B CD1 
2588 C CD2 . LEU A 340 ? 0.9939 0.9939 0.9939 0.0000 0.0000 0.0000 323 LEU B CD2 
2589 N N   . SER A 341 ? 1.1067 1.1067 1.1067 0.0000 0.0000 0.0000 324 SER B N   
2590 C CA  . SER A 341 ? 1.1067 1.1067 1.1067 0.0000 0.0000 0.0000 324 SER B CA  
2591 C C   . SER A 341 ? 1.1067 1.1067 1.1067 0.0000 0.0000 0.0000 324 SER B C   
2592 O O   . SER A 341 ? 1.1067 1.1067 1.1067 0.0000 0.0000 0.0000 324 SER B O   
2593 C CB  . SER A 341 ? 1.1067 1.1067 1.1067 0.0000 0.0000 0.0000 324 SER B CB  
2594 O OG  . SER A 341 ? 1.1067 1.1067 1.1067 0.0000 0.0000 0.0000 324 SER B OG  
2595 N N   . GLU A 342 ? 1.2518 1.2518 1.2518 0.0000 0.0000 0.0000 325 GLU B N   
2596 C CA  . GLU A 342 ? 1.2518 1.2518 1.2518 0.0000 0.0000 0.0000 325 GLU B CA  
2597 C C   . GLU A 342 ? 1.2518 1.2518 1.2518 0.0000 0.0000 0.0000 325 GLU B C   
2598 O O   . GLU A 342 ? 1.2518 1.2518 1.2518 0.0000 0.0000 0.0000 325 GLU B O   
2599 C CB  . GLU A 342 ? 1.2518 1.2518 1.2518 0.0000 0.0000 0.0000 325 GLU B CB  
2600 C CG  . GLU A 342 ? 1.2518 1.2518 1.2518 0.0000 0.0000 0.0000 325 GLU B CG  
2601 C CD  . GLU A 342 ? 1.2518 1.2518 1.2518 0.0000 0.0000 0.0000 325 GLU B CD  
2602 O OE1 . GLU A 342 ? 1.2518 1.2518 1.2518 0.0000 0.0000 0.0000 325 GLU B OE1 
2603 O OE2 . GLU A 342 ? 1.2518 1.2518 1.2518 0.0000 0.0000 0.0000 325 GLU B OE2 
2604 N N   . ASP A 343 ? 1.3741 1.3741 1.3741 0.0000 0.0000 0.0000 326 ASP B N   
2605 C CA  . ASP A 343 ? 1.3741 1.3741 1.3741 0.0000 0.0000 0.0000 326 ASP B CA  
2606 C C   . ASP A 343 ? 1.3741 1.3741 1.3741 0.0000 0.0000 0.0000 326 ASP B C   
2607 O O   . ASP A 343 ? 1.3741 1.3741 1.3741 0.0000 0.0000 0.0000 326 ASP B O   
2608 C CB  . ASP A 343 ? 1.3741 1.3741 1.3741 0.0000 0.0000 0.0000 326 ASP B CB  
2609 C CG  . ASP A 343 ? 1.3741 1.3741 1.3741 0.0000 0.0000 0.0000 326 ASP B CG  
2610 O OD1 . ASP A 343 ? 1.3741 1.3741 1.3741 0.0000 0.0000 0.0000 326 ASP B OD1 
2611 O OD2 . ASP A 343 ? 1.3741 1.3741 1.3741 0.0000 0.0000 0.0000 326 ASP B OD2 
2612 N N   . THR A 344 ? 1.4377 1.4377 1.4377 0.0000 0.0000 0.0000 327 THR B N   
2613 C CA  . THR A 344 ? 1.4377 1.4377 1.4377 0.0000 0.0000 0.0000 327 THR B CA  
2614 C C   . THR A 344 ? 1.4377 1.4377 1.4377 0.0000 0.0000 0.0000 327 THR B C   
2615 O O   . THR A 344 ? 1.4377 1.4377 1.4377 0.0000 0.0000 0.0000 327 THR B O   
2616 C CB  . THR A 344 ? 1.4377 1.4377 1.4377 0.0000 0.0000 0.0000 327 THR B CB  
2617 O OG1 . THR A 344 ? 1.4377 1.4377 1.4377 0.0000 0.0000 0.0000 327 THR B OG1 
2618 C CG2 . THR A 344 ? 1.4377 1.4377 1.4377 0.0000 0.0000 0.0000 327 THR B CG2 
2619 N N   . SER A 345 ? 1.4309 1.4309 1.4309 0.0000 0.0000 0.0000 328 SER B N   
2620 C CA  . SER A 345 ? 1.4309 1.4309 1.4309 0.0000 0.0000 0.0000 328 SER B CA  
2621 C C   . SER A 345 ? 1.4309 1.4309 1.4309 0.0000 0.0000 0.0000 328 SER B C   
2622 O O   . SER A 345 ? 1.4309 1.4309 1.4309 0.0000 0.0000 0.0000 328 SER B O   
2623 C CB  . SER A 345 ? 1.4309 1.4309 1.4309 0.0000 0.0000 0.0000 328 SER B CB  
2624 O OG  . SER A 345 ? 1.4309 1.4309 1.4309 0.0000 0.0000 0.0000 328 SER B OG  
2625 N N   . GLY A 346 ? 1.3598 1.3598 1.3598 0.0000 0.0000 0.0000 329 GLY B N   
2626 C CA  . GLY A 346 ? 1.3598 1.3598 1.3598 0.0000 0.0000 0.0000 329 GLY B CA  
2627 C C   . GLY A 346 ? 1.3598 1.3598 1.3598 0.0000 0.0000 0.0000 329 GLY B C   
2628 O O   . GLY A 346 ? 1.3598 1.3598 1.3598 0.0000 0.0000 0.0000 329 GLY B O   
2629 N N   . LYS A 347 ? 1.2920 1.2920 1.2920 0.0000 0.0000 0.0000 330 LYS B N   
2630 C CA  . LYS A 347 ? 1.2920 1.2920 1.2920 0.0000 0.0000 0.0000 330 LYS B CA  
2631 C C   . LYS A 347 ? 1.2920 1.2920 1.2920 0.0000 0.0000 0.0000 330 LYS B C   
2632 O O   . LYS A 347 ? 1.2920 1.2920 1.2920 0.0000 0.0000 0.0000 330 LYS B O   
2633 C CB  . LYS A 347 ? 1.2920 1.2920 1.2920 0.0000 0.0000 0.0000 330 LYS B CB  
2634 C CG  . LYS A 347 ? 1.2920 1.2920 1.2920 0.0000 0.0000 0.0000 330 LYS B CG  
2635 C CD  . LYS A 347 ? 1.2920 1.2920 1.2920 0.0000 0.0000 0.0000 330 LYS B CD  
2636 C CE  . LYS A 347 ? 1.2920 1.2920 1.2920 0.0000 0.0000 0.0000 330 LYS B CE  
2637 N NZ  . LYS A 347 ? 1.2920 1.2920 1.2920 0.0000 0.0000 0.0000 330 LYS B NZ  
2638 N N   . PHE A 348 ? 1.1503 1.1503 1.1503 0.0000 0.0000 0.0000 331 PHE B N   
2639 C CA  . PHE A 348 ? 1.1503 1.1503 1.1503 0.0000 0.0000 0.0000 331 PHE B CA  
2640 C C   . PHE A 348 ? 1.1503 1.1503 1.1503 0.0000 0.0000 0.0000 331 PHE B C   
2641 O O   . PHE A 348 ? 1.1503 1.1503 1.1503 0.0000 0.0000 0.0000 331 PHE B O   
2642 C CB  . PHE A 348 ? 1.1503 1.1503 1.1503 0.0000 0.0000 0.0000 331 PHE B CB  
2643 C CG  . PHE A 348 ? 1.1503 1.1503 1.1503 0.0000 0.0000 0.0000 331 PHE B CG  
2644 C CD1 . PHE A 348 ? 1.1503 1.1503 1.1503 0.0000 0.0000 0.0000 331 PHE B CD1 
2645 C CD2 . PHE A 348 ? 1.1503 1.1503 1.1503 0.0000 0.0000 0.0000 331 PHE B CD2 
2646 C CE1 . PHE A 348 ? 1.1503 1.1503 1.1503 0.0000 0.0000 0.0000 331 PHE B CE1 
2647 C CE2 . PHE A 348 ? 1.1503 1.1503 1.1503 0.0000 0.0000 0.0000 331 PHE B CE2 
2648 C CZ  . PHE A 348 ? 1.1503 1.1503 1.1503 0.0000 0.0000 0.0000 331 PHE B CZ  
2649 N N   . SER A 349 ? 1.0893 1.0893 1.0893 0.0000 0.0000 0.0000 332 SER B N   
2650 C CA  . SER A 349 ? 1.0893 1.0893 1.0893 0.0000 0.0000 0.0000 332 SER B CA  
2651 C C   . SER A 349 ? 1.0893 1.0893 1.0893 0.0000 0.0000 0.0000 332 SER B C   
2652 O O   . SER A 349 ? 1.0893 1.0893 1.0893 0.0000 0.0000 0.0000 332 SER B O   
2653 C CB  . SER A 349 ? 1.0893 1.0893 1.0893 0.0000 0.0000 0.0000 332 SER B CB  
2654 O OG  . SER A 349 ? 1.0893 1.0893 1.0893 0.0000 0.0000 0.0000 332 SER B OG  
2655 N N   . VAL A 350 ? 0.9887 0.9887 0.9887 0.0000 0.0000 0.0000 333 VAL B N   
2656 C CA  . VAL A 350 ? 0.9887 0.9887 0.9887 0.0000 0.0000 0.0000 333 VAL B CA  
2657 C C   . VAL A 350 ? 0.9887 0.9887 0.9887 0.0000 0.0000 0.0000 333 VAL B C   
2658 O O   . VAL A 350 ? 0.9887 0.9887 0.9887 0.0000 0.0000 0.0000 333 VAL B O   
2659 C CB  . VAL A 350 ? 0.9887 0.9887 0.9887 0.0000 0.0000 0.0000 333 VAL B CB  
2660 C CG1 . VAL A 350 ? 0.9887 0.9887 0.9887 0.0000 0.0000 0.0000 333 VAL B CG1 
2661 C CG2 . VAL A 350 ? 0.9887 0.9887 0.9887 0.0000 0.0000 0.0000 333 VAL B CG2 
2662 N N   . ASP A 351 ? 0.9858 0.9858 0.9858 0.0000 0.0000 0.0000 334 ASP B N   
2663 C CA  . ASP A 351 ? 0.9858 0.9858 0.9858 0.0000 0.0000 0.0000 334 ASP B CA  
2664 C C   . ASP A 351 ? 0.9858 0.9858 0.9858 0.0000 0.0000 0.0000 334 ASP B C   
2665 O O   . ASP A 351 ? 0.9858 0.9858 0.9858 0.0000 0.0000 0.0000 334 ASP B O   
2666 C CB  . ASP A 351 ? 0.9858 0.9858 0.9858 0.0000 0.0000 0.0000 334 ASP B CB  
2667 C CG  . ASP A 351 ? 0.9858 0.9858 0.9858 0.0000 0.0000 0.0000 334 ASP B CG  
2668 O OD1 . ASP A 351 ? 0.9858 0.9858 0.9858 0.0000 0.0000 0.0000 334 ASP B OD1 
2669 O OD2 . ASP A 351 ? 0.9858 0.9858 0.9858 0.0000 0.0000 0.0000 334 ASP B OD2 
2670 N N   . LYS A 352 ? 0.9090 0.9090 0.9090 0.0000 0.0000 0.0000 335 LYS B N   
2671 C CA  . LYS A 352 ? 0.9090 0.9090 0.9090 0.0000 0.0000 0.0000 335 LYS B CA  
2672 C C   . LYS A 352 ? 0.9090 0.9090 0.9090 0.0000 0.0000 0.0000 335 LYS B C   
2673 O O   . LYS A 352 ? 0.9090 0.9090 0.9090 0.0000 0.0000 0.0000 335 LYS B O   
2674 C CB  . LYS A 352 ? 0.9090 0.9090 0.9090 0.0000 0.0000 0.0000 335 LYS B CB  
2675 C CG  . LYS A 352 ? 0.9090 0.9090 0.9090 0.0000 0.0000 0.0000 335 LYS B CG  
2676 C CD  . LYS A 352 ? 0.9090 0.9090 0.9090 0.0000 0.0000 0.0000 335 LYS B CD  
2677 C CE  . LYS A 352 ? 0.9090 0.9090 0.9090 0.0000 0.0000 0.0000 335 LYS B CE  
2678 N NZ  . LYS A 352 ? 0.9090 0.9090 0.9090 0.0000 0.0000 0.0000 335 LYS B NZ  
2679 N N   . LEU A 353 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 336 LEU B N   
2680 C CA  . LEU A 353 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 336 LEU B CA  
2681 C C   . LEU A 353 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 336 LEU B C   
2682 O O   . LEU A 353 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 336 LEU B O   
2683 C CB  . LEU A 353 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 336 LEU B CB  
2684 C CG  . LEU A 353 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 336 LEU B CG  
2685 C CD1 . LEU A 353 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 336 LEU B CD1 
2686 C CD2 . LEU A 353 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 336 LEU B CD2 
2687 N N   . LYS A 354 ? 0.9165 0.9165 0.9165 0.0000 0.0000 0.0000 337 LYS B N   
2688 C CA  . LYS A 354 ? 0.9165 0.9165 0.9165 0.0000 0.0000 0.0000 337 LYS B CA  
2689 C C   . LYS A 354 ? 0.9165 0.9165 0.9165 0.0000 0.0000 0.0000 337 LYS B C   
2690 O O   . LYS A 354 ? 0.9165 0.9165 0.9165 0.0000 0.0000 0.0000 337 LYS B O   
2691 C CB  . LYS A 354 ? 0.9165 0.9165 0.9165 0.0000 0.0000 0.0000 337 LYS B CB  
2692 C CG  . LYS A 354 ? 0.9165 0.9165 0.9165 0.0000 0.0000 0.0000 337 LYS B CG  
2693 C CD  . LYS A 354 ? 0.9165 0.9165 0.9165 0.0000 0.0000 0.0000 337 LYS B CD  
2694 C CE  . LYS A 354 ? 0.9165 0.9165 0.9165 0.0000 0.0000 0.0000 337 LYS B CE  
2695 N NZ  . LYS A 354 ? 0.9165 0.9165 0.9165 0.0000 0.0000 0.0000 337 LYS B NZ  
2696 N N   . PHE A 355 ? 0.8892 0.8892 0.8892 0.0000 0.0000 0.0000 338 PHE B N   
2697 C CA  . PHE A 355 ? 0.8892 0.8892 0.8892 0.0000 0.0000 0.0000 338 PHE B CA  
2698 C C   . PHE A 355 ? 0.8892 0.8892 0.8892 0.0000 0.0000 0.0000 338 PHE B C   
2699 O O   . PHE A 355 ? 0.8892 0.8892 0.8892 0.0000 0.0000 0.0000 338 PHE B O   
2700 C CB  . PHE A 355 ? 0.8892 0.8892 0.8892 0.0000 0.0000 0.0000 338 PHE B CB  
2701 C CG  . PHE A 355 ? 0.8892 0.8892 0.8892 0.0000 0.0000 0.0000 338 PHE B CG  
2702 C CD1 . PHE A 355 ? 0.8892 0.8892 0.8892 0.0000 0.0000 0.0000 338 PHE B CD1 
2703 C CD2 . PHE A 355 ? 0.8892 0.8892 0.8892 0.0000 0.0000 0.0000 338 PHE B CD2 
2704 C CE1 . PHE A 355 ? 0.8892 0.8892 0.8892 0.0000 0.0000 0.0000 338 PHE B CE1 
2705 C CE2 . PHE A 355 ? 0.8892 0.8892 0.8892 0.0000 0.0000 0.0000 338 PHE B CE2 
2706 C CZ  . PHE A 355 ? 0.8892 0.8892 0.8892 0.0000 0.0000 0.0000 338 PHE B CZ  
2707 N N   . ASP A 356 ? 0.9390 0.9390 0.9390 0.0000 0.0000 0.0000 339 ASP B N   
2708 C CA  . ASP A 356 ? 0.9390 0.9390 0.9390 0.0000 0.0000 0.0000 339 ASP B CA  
2709 C C   . ASP A 356 ? 0.9390 0.9390 0.9390 0.0000 0.0000 0.0000 339 ASP B C   
2710 O O   . ASP A 356 ? 0.9390 0.9390 0.9390 0.0000 0.0000 0.0000 339 ASP B O   
2711 C CB  . ASP A 356 ? 0.9390 0.9390 0.9390 0.0000 0.0000 0.0000 339 ASP B CB  
2712 C CG  . ASP A 356 ? 0.9390 0.9390 0.9390 0.0000 0.0000 0.0000 339 ASP B CG  
2713 O OD1 . ASP A 356 ? 0.9390 0.9390 0.9390 0.0000 0.0000 0.0000 339 ASP B OD1 
2714 O OD2 . ASP A 356 ? 0.9390 0.9390 0.9390 0.0000 0.0000 0.0000 339 ASP B OD2 
2715 N N   . LYS A 357 ? 0.9338 0.9338 0.9338 0.0000 0.0000 0.0000 340 LYS B N   
2716 C CA  . LYS A 357 ? 0.9338 0.9338 0.9338 0.0000 0.0000 0.0000 340 LYS B CA  
2717 C C   . LYS A 357 ? 0.9338 0.9338 0.9338 0.0000 0.0000 0.0000 340 LYS B C   
2718 O O   . LYS A 357 ? 0.9338 0.9338 0.9338 0.0000 0.0000 0.0000 340 LYS B O   
2719 C CB  . LYS A 357 ? 0.9338 0.9338 0.9338 0.0000 0.0000 0.0000 340 LYS B CB  
2720 C CG  . LYS A 357 ? 0.9338 0.9338 0.9338 0.0000 0.0000 0.0000 340 LYS B CG  
2721 C CD  . LYS A 357 ? 0.9338 0.9338 0.9338 0.0000 0.0000 0.0000 340 LYS B CD  
2722 C CE  . LYS A 357 ? 0.9338 0.9338 0.9338 0.0000 0.0000 0.0000 340 LYS B CE  
2723 N NZ  . LYS A 357 ? 0.9338 0.9338 0.9338 0.0000 0.0000 0.0000 340 LYS B NZ  
2724 N N   . LEU A 358 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 341 LEU B N   
2725 C CA  . LEU A 358 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 341 LEU B CA  
2726 C C   . LEU A 358 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 341 LEU B C   
2727 O O   . LEU A 358 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 341 LEU B O   
2728 C CB  . LEU A 358 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 341 LEU B CB  
2729 C CG  . LEU A 358 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 341 LEU B CG  
2730 C CD1 . LEU A 358 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 341 LEU B CD1 
2731 C CD2 . LEU A 358 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 341 LEU B CD2 
2732 N N   . TYR A 359 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 342 TYR B N   
2733 C CA  . TYR A 359 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 342 TYR B CA  
2734 C C   . TYR A 359 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 342 TYR B C   
2735 O O   . TYR A 359 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 342 TYR B O   
2736 C CB  . TYR A 359 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 342 TYR B CB  
2737 C CG  . TYR A 359 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 342 TYR B CG  
2738 C CD1 . TYR A 359 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 342 TYR B CD1 
2739 C CD2 . TYR A 359 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 342 TYR B CD2 
2740 C CE1 . TYR A 359 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 342 TYR B CE1 
2741 C CE2 . TYR A 359 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 342 TYR B CE2 
2742 C CZ  . TYR A 359 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 342 TYR B CZ  
2743 O OH  . TYR A 359 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 342 TYR B OH  
2744 N N   . LYS A 360 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 343 LYS B N   
2745 C CA  . LYS A 360 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 343 LYS B CA  
2746 C C   . LYS A 360 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 343 LYS B C   
2747 O O   . LYS A 360 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 343 LYS B O   
2748 C CB  . LYS A 360 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 343 LYS B CB  
2749 C CG  . LYS A 360 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 343 LYS B CG  
2750 C CD  . LYS A 360 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 343 LYS B CD  
2751 C CE  . LYS A 360 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 343 LYS B CE  
2752 N NZ  . LYS A 360 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 343 LYS B NZ  
2753 N N   . MET A 361 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 344 MET B N   
2754 C CA  . MET A 361 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 344 MET B CA  
2755 C C   . MET A 361 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 344 MET B C   
2756 O O   . MET A 361 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 344 MET B O   
2757 C CB  . MET A 361 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 344 MET B CB  
2758 C CG  . MET A 361 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 344 MET B CG  
2759 S SD  . MET A 361 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 344 MET B SD  
2760 C CE  . MET A 361 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 344 MET B CE  
2761 N N   . LEU A 362 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 345 LEU B N   
2762 C CA  . LEU A 362 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 345 LEU B CA  
2763 C C   . LEU A 362 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 345 LEU B C   
2764 O O   . LEU A 362 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 345 LEU B O   
2765 C CB  . LEU A 362 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 345 LEU B CB  
2766 C CG  . LEU A 362 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 345 LEU B CG  
2767 C CD1 . LEU A 362 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 345 LEU B CD1 
2768 C CD2 . LEU A 362 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 345 LEU B CD2 
2769 N N   . THR A 363 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 346 THR B N   
2770 C CA  . THR A 363 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 346 THR B CA  
2771 C C   . THR A 363 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 346 THR B C   
2772 O O   . THR A 363 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 346 THR B O   
2773 C CB  . THR A 363 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 346 THR B CB  
2774 O OG1 . THR A 363 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 346 THR B OG1 
2775 C CG2 . THR A 363 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 346 THR B CG2 
2776 N N   . GLU A 364 ? 0.8890 0.8890 0.8890 0.0000 0.0000 0.0000 347 GLU B N   
2777 C CA  . GLU A 364 ? 0.8890 0.8890 0.8890 0.0000 0.0000 0.0000 347 GLU B CA  
2778 C C   . GLU A 364 ? 0.8890 0.8890 0.8890 0.0000 0.0000 0.0000 347 GLU B C   
2779 O O   . GLU A 364 ? 0.8890 0.8890 0.8890 0.0000 0.0000 0.0000 347 GLU B O   
2780 C CB  . GLU A 364 ? 0.8890 0.8890 0.8890 0.0000 0.0000 0.0000 347 GLU B CB  
2781 C CG  . GLU A 364 ? 0.8890 0.8890 0.8890 0.0000 0.0000 0.0000 347 GLU B CG  
2782 C CD  . GLU A 364 ? 0.8890 0.8890 0.8890 0.0000 0.0000 0.0000 347 GLU B CD  
2783 O OE1 . GLU A 364 ? 0.8890 0.8890 0.8890 0.0000 0.0000 0.0000 347 GLU B OE1 
2784 O OE2 . GLU A 364 ? 0.8890 0.8890 0.8890 0.0000 0.0000 0.0000 347 GLU B OE2 
2785 N N   . ILE A 365 ? 0.8990 0.8990 0.8990 0.0000 0.0000 0.0000 348 ILE B N   
2786 C CA  . ILE A 365 ? 0.8990 0.8990 0.8990 0.0000 0.0000 0.0000 348 ILE B CA  
2787 C C   . ILE A 365 ? 0.8990 0.8990 0.8990 0.0000 0.0000 0.0000 348 ILE B C   
2788 O O   . ILE A 365 ? 0.8990 0.8990 0.8990 0.0000 0.0000 0.0000 348 ILE B O   
2789 C CB  . ILE A 365 ? 0.8990 0.8990 0.8990 0.0000 0.0000 0.0000 348 ILE B CB  
2790 C CG1 . ILE A 365 ? 0.8990 0.8990 0.8990 0.0000 0.0000 0.0000 348 ILE B CG1 
2791 C CG2 . ILE A 365 ? 0.8990 0.8990 0.8990 0.0000 0.0000 0.0000 348 ILE B CG2 
2792 C CD1 . ILE A 365 ? 0.8990 0.8990 0.8990 0.0000 0.0000 0.0000 348 ILE B CD1 
2793 N N   . TYR A 366 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 349 TYR B N   
2794 C CA  . TYR A 366 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 349 TYR B CA  
2795 C C   . TYR A 366 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 349 TYR B C   
2796 O O   . TYR A 366 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 349 TYR B O   
2797 C CB  . TYR A 366 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 349 TYR B CB  
2798 C CG  . TYR A 366 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 349 TYR B CG  
2799 C CD1 . TYR A 366 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 349 TYR B CD1 
2800 C CD2 . TYR A 366 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 349 TYR B CD2 
2801 C CE1 . TYR A 366 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 349 TYR B CE1 
2802 C CE2 . TYR A 366 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 349 TYR B CE2 
2803 C CZ  . TYR A 366 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 349 TYR B CZ  
2804 O OH  . TYR A 366 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 349 TYR B OH  
2805 N N   . THR A 367 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 350 THR B N   
2806 C CA  . THR A 367 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 350 THR B CA  
2807 C C   . THR A 367 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 350 THR B C   
2808 O O   . THR A 367 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 350 THR B O   
2809 C CB  . THR A 367 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 350 THR B CB  
2810 O OG1 . THR A 367 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 350 THR B OG1 
2811 C CG2 . THR A 367 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 350 THR B CG2 
2812 N N   . GLU A 368 ? 0.8908 0.8908 0.8908 0.0000 0.0000 0.0000 351 GLU B N   
2813 C CA  . GLU A 368 ? 0.8908 0.8908 0.8908 0.0000 0.0000 0.0000 351 GLU B CA  
2814 C C   . GLU A 368 ? 0.8908 0.8908 0.8908 0.0000 0.0000 0.0000 351 GLU B C   
2815 O O   . GLU A 368 ? 0.8908 0.8908 0.8908 0.0000 0.0000 0.0000 351 GLU B O   
2816 C CB  . GLU A 368 ? 0.8908 0.8908 0.8908 0.0000 0.0000 0.0000 351 GLU B CB  
2817 C CG  . GLU A 368 ? 0.8908 0.8908 0.8908 0.0000 0.0000 0.0000 351 GLU B CG  
2818 C CD  . GLU A 368 ? 0.8908 0.8908 0.8908 0.0000 0.0000 0.0000 351 GLU B CD  
2819 O OE1 . GLU A 368 ? 0.8908 0.8908 0.8908 0.0000 0.0000 0.0000 351 GLU B OE1 
2820 O OE2 . GLU A 368 ? 0.8908 0.8908 0.8908 0.0000 0.0000 0.0000 351 GLU B OE2 
2821 N N   . ASP A 369 ? 0.9215 0.9215 0.9215 0.0000 0.0000 0.0000 352 ASP B N   
2822 C CA  . ASP A 369 ? 0.9215 0.9215 0.9215 0.0000 0.0000 0.0000 352 ASP B CA  
2823 C C   . ASP A 369 ? 0.9215 0.9215 0.9215 0.0000 0.0000 0.0000 352 ASP B C   
2824 O O   . ASP A 369 ? 0.9215 0.9215 0.9215 0.0000 0.0000 0.0000 352 ASP B O   
2825 C CB  . ASP A 369 ? 0.9215 0.9215 0.9215 0.0000 0.0000 0.0000 352 ASP B CB  
2826 C CG  . ASP A 369 ? 0.9215 0.9215 0.9215 0.0000 0.0000 0.0000 352 ASP B CG  
2827 O OD1 . ASP A 369 ? 0.9215 0.9215 0.9215 0.0000 0.0000 0.0000 352 ASP B OD1 
2828 O OD2 . ASP A 369 ? 0.9215 0.9215 0.9215 0.0000 0.0000 0.0000 352 ASP B OD2 
2829 N N   . ASN A 370 ? 0.8836 0.8836 0.8836 0.0000 0.0000 0.0000 353 ASN B N   
2830 C CA  . ASN A 370 ? 0.8836 0.8836 0.8836 0.0000 0.0000 0.0000 353 ASN B CA  
2831 C C   . ASN A 370 ? 0.8836 0.8836 0.8836 0.0000 0.0000 0.0000 353 ASN B C   
2832 O O   . ASN A 370 ? 0.8836 0.8836 0.8836 0.0000 0.0000 0.0000 353 ASN B O   
2833 C CB  . ASN A 370 ? 0.8836 0.8836 0.8836 0.0000 0.0000 0.0000 353 ASN B CB  
2834 C CG  . ASN A 370 ? 0.8836 0.8836 0.8836 0.0000 0.0000 0.0000 353 ASN B CG  
2835 O OD1 . ASN A 370 ? 0.8836 0.8836 0.8836 0.0000 0.0000 0.0000 353 ASN B OD1 
2836 N ND2 . ASN A 370 ? 0.8836 0.8836 0.8836 0.0000 0.0000 0.0000 353 ASN B ND2 
2837 N N   . PHE A 371 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 354 PHE B N   
2838 C CA  . PHE A 371 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 354 PHE B CA  
2839 C C   . PHE A 371 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 354 PHE B C   
2840 O O   . PHE A 371 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 354 PHE B O   
2841 C CB  . PHE A 371 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 354 PHE B CB  
2842 C CG  . PHE A 371 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 354 PHE B CG  
2843 C CD1 . PHE A 371 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 354 PHE B CD1 
2844 C CD2 . PHE A 371 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 354 PHE B CD2 
2845 C CE1 . PHE A 371 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 354 PHE B CE1 
2846 C CE2 . PHE A 371 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 354 PHE B CE2 
2847 C CZ  . PHE A 371 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 354 PHE B CZ  
2848 N N   . VAL A 372 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 355 VAL B N   
2849 C CA  . VAL A 372 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 355 VAL B CA  
2850 C C   . VAL A 372 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 355 VAL B C   
2851 O O   . VAL A 372 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 355 VAL B O   
2852 C CB  . VAL A 372 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 355 VAL B CB  
2853 C CG1 . VAL A 372 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 355 VAL B CG1 
2854 C CG2 . VAL A 372 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 355 VAL B CG2 
2855 N N   . LYS A 373 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 356 LYS B N   
2856 C CA  . LYS A 373 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 356 LYS B CA  
2857 C C   . LYS A 373 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 356 LYS B C   
2858 O O   . LYS A 373 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 356 LYS B O   
2859 C CB  . LYS A 373 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 356 LYS B CB  
2860 C CG  . LYS A 373 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 356 LYS B CG  
2861 C CD  . LYS A 373 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 356 LYS B CD  
2862 C CE  . LYS A 373 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 356 LYS B CE  
2863 N NZ  . LYS A 373 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 356 LYS B NZ  
2864 N N   . PHE A 374 ? 0.9563 0.9563 0.9563 0.0000 0.0000 0.0000 357 PHE B N   
2865 C CA  . PHE A 374 ? 0.9563 0.9563 0.9563 0.0000 0.0000 0.0000 357 PHE B CA  
2866 C C   . PHE A 374 ? 0.9563 0.9563 0.9563 0.0000 0.0000 0.0000 357 PHE B C   
2867 O O   . PHE A 374 ? 0.9563 0.9563 0.9563 0.0000 0.0000 0.0000 357 PHE B O   
2868 C CB  . PHE A 374 ? 0.9563 0.9563 0.9563 0.0000 0.0000 0.0000 357 PHE B CB  
2869 C CG  . PHE A 374 ? 0.9563 0.9563 0.9563 0.0000 0.0000 0.0000 357 PHE B CG  
2870 C CD1 . PHE A 374 ? 0.9563 0.9563 0.9563 0.0000 0.0000 0.0000 357 PHE B CD1 
2871 C CD2 . PHE A 374 ? 0.9563 0.9563 0.9563 0.0000 0.0000 0.0000 357 PHE B CD2 
2872 C CE1 . PHE A 374 ? 0.9563 0.9563 0.9563 0.0000 0.0000 0.0000 357 PHE B CE1 
2873 C CE2 . PHE A 374 ? 0.9563 0.9563 0.9563 0.0000 0.0000 0.0000 357 PHE B CE2 
2874 C CZ  . PHE A 374 ? 0.9563 0.9563 0.9563 0.0000 0.0000 0.0000 357 PHE B CZ  
2875 N N   . PHE A 375 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 358 PHE B N   
2876 C CA  . PHE A 375 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 358 PHE B CA  
2877 C C   . PHE A 375 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 358 PHE B C   
2878 O O   . PHE A 375 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 358 PHE B O   
2879 C CB  . PHE A 375 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 358 PHE B CB  
2880 C CG  . PHE A 375 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 358 PHE B CG  
2881 C CD1 . PHE A 375 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 358 PHE B CD1 
2882 C CD2 . PHE A 375 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 358 PHE B CD2 
2883 C CE1 . PHE A 375 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 358 PHE B CE1 
2884 C CE2 . PHE A 375 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 358 PHE B CE2 
2885 C CZ  . PHE A 375 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 358 PHE B CZ  
2886 N N   . LYS A 376 ? 0.9996 0.9996 0.9996 0.0000 0.0000 0.0000 359 LYS B N   
2887 C CA  . LYS A 376 ? 0.9996 0.9996 0.9996 0.0000 0.0000 0.0000 359 LYS B CA  
2888 C C   . LYS A 376 ? 0.9996 0.9996 0.9996 0.0000 0.0000 0.0000 359 LYS B C   
2889 O O   . LYS A 376 ? 0.9996 0.9996 0.9996 0.0000 0.0000 0.0000 359 LYS B O   
2890 C CB  . LYS A 376 ? 0.9996 0.9996 0.9996 0.0000 0.0000 0.0000 359 LYS B CB  
2891 C CG  . LYS A 376 ? 0.9996 0.9996 0.9996 0.0000 0.0000 0.0000 359 LYS B CG  
2892 C CD  . LYS A 376 ? 0.9996 0.9996 0.9996 0.0000 0.0000 0.0000 359 LYS B CD  
2893 C CE  . LYS A 376 ? 0.9996 0.9996 0.9996 0.0000 0.0000 0.0000 359 LYS B CE  
2894 N NZ  . LYS A 376 ? 0.9996 0.9996 0.9996 0.0000 0.0000 0.0000 359 LYS B NZ  
2895 N N   . VAL A 377 ? 0.9898 0.9898 0.9898 0.0000 0.0000 0.0000 360 VAL B N   
2896 C CA  . VAL A 377 ? 0.9898 0.9898 0.9898 0.0000 0.0000 0.0000 360 VAL B CA  
2897 C C   . VAL A 377 ? 0.9898 0.9898 0.9898 0.0000 0.0000 0.0000 360 VAL B C   
2898 O O   . VAL A 377 ? 0.9898 0.9898 0.9898 0.0000 0.0000 0.0000 360 VAL B O   
2899 C CB  . VAL A 377 ? 0.9898 0.9898 0.9898 0.0000 0.0000 0.0000 360 VAL B CB  
2900 C CG1 . VAL A 377 ? 0.9898 0.9898 0.9898 0.0000 0.0000 0.0000 360 VAL B CG1 
2901 C CG2 . VAL A 377 ? 0.9898 0.9898 0.9898 0.0000 0.0000 0.0000 360 VAL B CG2 
2902 N N   . LEU A 378 ? 1.0615 1.0615 1.0615 0.0000 0.0000 0.0000 361 LEU B N   
2903 C CA  . LEU A 378 ? 1.0615 1.0615 1.0615 0.0000 0.0000 0.0000 361 LEU B CA  
2904 C C   . LEU A 378 ? 1.0615 1.0615 1.0615 0.0000 0.0000 0.0000 361 LEU B C   
2905 O O   . LEU A 378 ? 1.0615 1.0615 1.0615 0.0000 0.0000 0.0000 361 LEU B O   
2906 C CB  . LEU A 378 ? 1.0615 1.0615 1.0615 0.0000 0.0000 0.0000 361 LEU B CB  
2907 C CG  . LEU A 378 ? 1.0615 1.0615 1.0615 0.0000 0.0000 0.0000 361 LEU B CG  
2908 C CD1 . LEU A 378 ? 1.0615 1.0615 1.0615 0.0000 0.0000 0.0000 361 LEU B CD1 
2909 C CD2 . LEU A 378 ? 1.0615 1.0615 1.0615 0.0000 0.0000 0.0000 361 LEU B CD2 
2910 N N   . ASN A 379 ? 1.0552 1.0552 1.0552 0.0000 0.0000 0.0000 362 ASN B N   
2911 C CA  . ASN A 379 ? 1.0552 1.0552 1.0552 0.0000 0.0000 0.0000 362 ASN B CA  
2912 C C   . ASN A 379 ? 1.0552 1.0552 1.0552 0.0000 0.0000 0.0000 362 ASN B C   
2913 O O   . ASN A 379 ? 1.0552 1.0552 1.0552 0.0000 0.0000 0.0000 362 ASN B O   
2914 C CB  . ASN A 379 ? 1.0552 1.0552 1.0552 0.0000 0.0000 0.0000 362 ASN B CB  
2915 C CG  . ASN A 379 ? 1.0552 1.0552 1.0552 0.0000 0.0000 0.0000 362 ASN B CG  
2916 O OD1 . ASN A 379 ? 1.0552 1.0552 1.0552 0.0000 0.0000 0.0000 362 ASN B OD1 
2917 N ND2 . ASN A 379 ? 1.0552 1.0552 1.0552 0.0000 0.0000 0.0000 362 ASN B ND2 
2918 N N   . ALA A 380 ? 1.0484 1.0484 1.0484 0.0000 0.0000 0.0000 363 ALA B N   
2919 C CA  . ALA A 380 ? 1.0484 1.0484 1.0484 0.0000 0.0000 0.0000 363 ALA B CA  
2920 C C   . ALA A 380 ? 1.0484 1.0484 1.0484 0.0000 0.0000 0.0000 363 ALA B C   
2921 O O   . ALA A 380 ? 1.0484 1.0484 1.0484 0.0000 0.0000 0.0000 363 ALA B O   
2922 C CB  . ALA A 380 ? 1.0484 1.0484 1.0484 0.0000 0.0000 0.0000 363 ALA B CB  
2923 N N   . LYS A 381 ? 1.0521 1.0521 1.0521 0.0000 0.0000 0.0000 364 LYS B N   
2924 C CA  . LYS A 381 ? 1.0521 1.0521 1.0521 0.0000 0.0000 0.0000 364 LYS B CA  
2925 C C   . LYS A 381 ? 1.0521 1.0521 1.0521 0.0000 0.0000 0.0000 364 LYS B C   
2926 O O   . LYS A 381 ? 1.0521 1.0521 1.0521 0.0000 0.0000 0.0000 364 LYS B O   
2927 C CB  . LYS A 381 ? 1.0521 1.0521 1.0521 0.0000 0.0000 0.0000 364 LYS B CB  
2928 C CG  . LYS A 381 ? 1.0521 1.0521 1.0521 0.0000 0.0000 0.0000 364 LYS B CG  
2929 C CD  . LYS A 381 ? 1.0521 1.0521 1.0521 0.0000 0.0000 0.0000 364 LYS B CD  
2930 C CE  . LYS A 381 ? 1.0521 1.0521 1.0521 0.0000 0.0000 0.0000 364 LYS B CE  
2931 N NZ  . LYS A 381 ? 1.0521 1.0521 1.0521 0.0000 0.0000 0.0000 364 LYS B NZ  
2932 N N   . THR A 382 ? 1.0051 1.0051 1.0051 0.0000 0.0000 0.0000 365 THR B N   
2933 C CA  . THR A 382 ? 1.0051 1.0051 1.0051 0.0000 0.0000 0.0000 365 THR B CA  
2934 C C   . THR A 382 ? 1.0051 1.0051 1.0051 0.0000 0.0000 0.0000 365 THR B C   
2935 O O   . THR A 382 ? 1.0051 1.0051 1.0051 0.0000 0.0000 0.0000 365 THR B O   
2936 C CB  . THR A 382 ? 1.0051 1.0051 1.0051 0.0000 0.0000 0.0000 365 THR B CB  
2937 O OG1 . THR A 382 ? 1.0051 1.0051 1.0051 0.0000 0.0000 0.0000 365 THR B OG1 
2938 C CG2 . THR A 382 ? 1.0051 1.0051 1.0051 0.0000 0.0000 0.0000 365 THR B CG2 
2939 N N   . PHE A 383 ? 0.9662 0.9662 0.9662 0.0000 0.0000 0.0000 366 PHE B N   
2940 C CA  . PHE A 383 ? 0.9662 0.9662 0.9662 0.0000 0.0000 0.0000 366 PHE B CA  
2941 C C   . PHE A 383 ? 0.9662 0.9662 0.9662 0.0000 0.0000 0.0000 366 PHE B C   
2942 O O   . PHE A 383 ? 0.9662 0.9662 0.9662 0.0000 0.0000 0.0000 366 PHE B O   
2943 C CB  . PHE A 383 ? 0.9662 0.9662 0.9662 0.0000 0.0000 0.0000 366 PHE B CB  
2944 C CG  . PHE A 383 ? 0.9662 0.9662 0.9662 0.0000 0.0000 0.0000 366 PHE B CG  
2945 C CD1 . PHE A 383 ? 0.9662 0.9662 0.9662 0.0000 0.0000 0.0000 366 PHE B CD1 
2946 C CD2 . PHE A 383 ? 0.9662 0.9662 0.9662 0.0000 0.0000 0.0000 366 PHE B CD2 
2947 C CE1 . PHE A 383 ? 0.9662 0.9662 0.9662 0.0000 0.0000 0.0000 366 PHE B CE1 
2948 C CE2 . PHE A 383 ? 0.9662 0.9662 0.9662 0.0000 0.0000 0.0000 366 PHE B CE2 
2949 C CZ  . PHE A 383 ? 0.9662 0.9662 0.9662 0.0000 0.0000 0.0000 366 PHE B CZ  
2950 N N   . LEU A 384 ? 0.9917 0.9917 0.9917 0.0000 0.0000 0.0000 367 LEU B N   
2951 C CA  . LEU A 384 ? 0.9917 0.9917 0.9917 0.0000 0.0000 0.0000 367 LEU B CA  
2952 C C   . LEU A 384 ? 0.9917 0.9917 0.9917 0.0000 0.0000 0.0000 367 LEU B C   
2953 O O   . LEU A 384 ? 0.9917 0.9917 0.9917 0.0000 0.0000 0.0000 367 LEU B O   
2954 C CB  . LEU A 384 ? 0.9917 0.9917 0.9917 0.0000 0.0000 0.0000 367 LEU B CB  
2955 C CG  . LEU A 384 ? 0.9917 0.9917 0.9917 0.0000 0.0000 0.0000 367 LEU B CG  
2956 C CD1 . LEU A 384 ? 0.9917 0.9917 0.9917 0.0000 0.0000 0.0000 367 LEU B CD1 
2957 C CD2 . LEU A 384 ? 0.9917 0.9917 0.9917 0.0000 0.0000 0.0000 367 LEU B CD2 
2958 N N   . ASN A 385 ? 0.9924 0.9924 0.9924 0.0000 0.0000 0.0000 368 ASN B N   
2959 C CA  . ASN A 385 ? 0.9924 0.9924 0.9924 0.0000 0.0000 0.0000 368 ASN B CA  
2960 C C   . ASN A 385 ? 0.9924 0.9924 0.9924 0.0000 0.0000 0.0000 368 ASN B C   
2961 O O   . ASN A 385 ? 0.9924 0.9924 0.9924 0.0000 0.0000 0.0000 368 ASN B O   
2962 C CB  . ASN A 385 ? 0.9924 0.9924 0.9924 0.0000 0.0000 0.0000 368 ASN B CB  
2963 C CG  . ASN A 385 ? 0.9924 0.9924 0.9924 0.0000 0.0000 0.0000 368 ASN B CG  
2964 O OD1 . ASN A 385 ? 0.9924 0.9924 0.9924 0.0000 0.0000 0.0000 368 ASN B OD1 
2965 N ND2 . ASN A 385 ? 0.9924 0.9924 0.9924 0.0000 0.0000 0.0000 368 ASN B ND2 
2966 N N   . PHE A 386 ? 0.9891 0.9891 0.9891 0.0000 0.0000 0.0000 369 PHE B N   
2967 C CA  . PHE A 386 ? 0.9891 0.9891 0.9891 0.0000 0.0000 0.0000 369 PHE B CA  
2968 C C   . PHE A 386 ? 0.9891 0.9891 0.9891 0.0000 0.0000 0.0000 369 PHE B C   
2969 O O   . PHE A 386 ? 0.9891 0.9891 0.9891 0.0000 0.0000 0.0000 369 PHE B O   
2970 C CB  . PHE A 386 ? 0.9891 0.9891 0.9891 0.0000 0.0000 0.0000 369 PHE B CB  
2971 C CG  . PHE A 386 ? 0.9891 0.9891 0.9891 0.0000 0.0000 0.0000 369 PHE B CG  
2972 C CD1 . PHE A 386 ? 0.9891 0.9891 0.9891 0.0000 0.0000 0.0000 369 PHE B CD1 
2973 C CD2 . PHE A 386 ? 0.9891 0.9891 0.9891 0.0000 0.0000 0.0000 369 PHE B CD2 
2974 C CE1 . PHE A 386 ? 0.9891 0.9891 0.9891 0.0000 0.0000 0.0000 369 PHE B CE1 
2975 C CE2 . PHE A 386 ? 0.9891 0.9891 0.9891 0.0000 0.0000 0.0000 369 PHE B CE2 
2976 C CZ  . PHE A 386 ? 0.9891 0.9891 0.9891 0.0000 0.0000 0.0000 369 PHE B CZ  
2977 N N   . ASP A 387 ? 0.9852 0.9852 0.9852 0.0000 0.0000 0.0000 370 ASP B N   
2978 C CA  . ASP A 387 ? 0.9852 0.9852 0.9852 0.0000 0.0000 0.0000 370 ASP B CA  
2979 C C   . ASP A 387 ? 0.9852 0.9852 0.9852 0.0000 0.0000 0.0000 370 ASP B C   
2980 O O   . ASP A 387 ? 0.9852 0.9852 0.9852 0.0000 0.0000 0.0000 370 ASP B O   
2981 C CB  . ASP A 387 ? 0.9852 0.9852 0.9852 0.0000 0.0000 0.0000 370 ASP B CB  
2982 C CG  . ASP A 387 ? 0.9852 0.9852 0.9852 0.0000 0.0000 0.0000 370 ASP B CG  
2983 O OD1 . ASP A 387 ? 0.9852 0.9852 0.9852 0.0000 0.0000 0.0000 370 ASP B OD1 
2984 O OD2 . ASP A 387 ? 0.9852 0.9852 0.9852 0.0000 0.0000 0.0000 370 ASP B OD2 
2985 N N   . LYS A 388 ? 0.9511 0.9511 0.9511 0.0000 0.0000 0.0000 371 LYS B N   
2986 C CA  . LYS A 388 ? 0.9511 0.9511 0.9511 0.0000 0.0000 0.0000 371 LYS B CA  
2987 C C   . LYS A 388 ? 0.9511 0.9511 0.9511 0.0000 0.0000 0.0000 371 LYS B C   
2988 O O   . LYS A 388 ? 0.9511 0.9511 0.9511 0.0000 0.0000 0.0000 371 LYS B O   
2989 C CB  . LYS A 388 ? 0.9511 0.9511 0.9511 0.0000 0.0000 0.0000 371 LYS B CB  
2990 C CG  . LYS A 388 ? 0.9511 0.9511 0.9511 0.0000 0.0000 0.0000 371 LYS B CG  
2991 C CD  . LYS A 388 ? 0.9511 0.9511 0.9511 0.0000 0.0000 0.0000 371 LYS B CD  
2992 C CE  . LYS A 388 ? 0.9511 0.9511 0.9511 0.0000 0.0000 0.0000 371 LYS B CE  
2993 N NZ  . LYS A 388 ? 0.9511 0.9511 0.9511 0.0000 0.0000 0.0000 371 LYS B NZ  
2994 N N   . ALA A 389 ? 0.9667 0.9667 0.9667 0.0000 0.0000 0.0000 372 ALA B N   
2995 C CA  . ALA A 389 ? 0.9667 0.9667 0.9667 0.0000 0.0000 0.0000 372 ALA B CA  
2996 C C   . ALA A 389 ? 0.9667 0.9667 0.9667 0.0000 0.0000 0.0000 372 ALA B C   
2997 O O   . ALA A 389 ? 0.9667 0.9667 0.9667 0.0000 0.0000 0.0000 372 ALA B O   
2998 C CB  . ALA A 389 ? 0.9667 0.9667 0.9667 0.0000 0.0000 0.0000 372 ALA B CB  
2999 N N   . VAL A 390 ? 0.9400 0.9400 0.9400 0.0000 0.0000 0.0000 373 VAL B N   
3000 C CA  . VAL A 390 ? 0.9400 0.9400 0.9400 0.0000 0.0000 0.0000 373 VAL B CA  
3001 C C   . VAL A 390 ? 0.9400 0.9400 0.9400 0.0000 0.0000 0.0000 373 VAL B C   
3002 O O   . VAL A 390 ? 0.9400 0.9400 0.9400 0.0000 0.0000 0.0000 373 VAL B O   
3003 C CB  . VAL A 390 ? 0.9400 0.9400 0.9400 0.0000 0.0000 0.0000 373 VAL B CB  
3004 C CG1 . VAL A 390 ? 0.9400 0.9400 0.9400 0.0000 0.0000 0.0000 373 VAL B CG1 
3005 C CG2 . VAL A 390 ? 0.9400 0.9400 0.9400 0.0000 0.0000 0.0000 373 VAL B CG2 
3006 N N   . PHE A 391 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 374 PHE B N   
3007 C CA  . PHE A 391 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 374 PHE B CA  
3008 C C   . PHE A 391 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 374 PHE B C   
3009 O O   . PHE A 391 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 374 PHE B O   
3010 C CB  . PHE A 391 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 374 PHE B CB  
3011 C CG  . PHE A 391 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 374 PHE B CG  
3012 C CD1 . PHE A 391 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 374 PHE B CD1 
3013 C CD2 . PHE A 391 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 374 PHE B CD2 
3014 C CE1 . PHE A 391 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 374 PHE B CE1 
3015 C CE2 . PHE A 391 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 374 PHE B CE2 
3016 C CZ  . PHE A 391 ? 0.9587 0.9587 0.9587 0.0000 0.0000 0.0000 374 PHE B CZ  
3017 N N   . LYS A 392 ? 0.9510 0.9510 0.9510 0.0000 0.0000 0.0000 375 LYS B N   
3018 C CA  . LYS A 392 ? 0.9510 0.9510 0.9510 0.0000 0.0000 0.0000 375 LYS B CA  
3019 C C   . LYS A 392 ? 0.9510 0.9510 0.9510 0.0000 0.0000 0.0000 375 LYS B C   
3020 O O   . LYS A 392 ? 0.9510 0.9510 0.9510 0.0000 0.0000 0.0000 375 LYS B O   
3021 C CB  . LYS A 392 ? 0.9510 0.9510 0.9510 0.0000 0.0000 0.0000 375 LYS B CB  
3022 C CG  . LYS A 392 ? 0.9510 0.9510 0.9510 0.0000 0.0000 0.0000 375 LYS B CG  
3023 C CD  . LYS A 392 ? 0.9510 0.9510 0.9510 0.0000 0.0000 0.0000 375 LYS B CD  
3024 C CE  . LYS A 392 ? 0.9510 0.9510 0.9510 0.0000 0.0000 0.0000 375 LYS B CE  
3025 N NZ  . LYS A 392 ? 0.9510 0.9510 0.9510 0.0000 0.0000 0.0000 375 LYS B NZ  
3026 N N   . ILE A 393 ? 0.9265 0.9265 0.9265 0.0000 0.0000 0.0000 376 ILE B N   
3027 C CA  . ILE A 393 ? 0.9265 0.9265 0.9265 0.0000 0.0000 0.0000 376 ILE B CA  
3028 C C   . ILE A 393 ? 0.9265 0.9265 0.9265 0.0000 0.0000 0.0000 376 ILE B C   
3029 O O   . ILE A 393 ? 0.9265 0.9265 0.9265 0.0000 0.0000 0.0000 376 ILE B O   
3030 C CB  . ILE A 393 ? 0.9265 0.9265 0.9265 0.0000 0.0000 0.0000 376 ILE B CB  
3031 C CG1 . ILE A 393 ? 0.9265 0.9265 0.9265 0.0000 0.0000 0.0000 376 ILE B CG1 
3032 C CG2 . ILE A 393 ? 0.9265 0.9265 0.9265 0.0000 0.0000 0.0000 376 ILE B CG2 
3033 C CD1 . ILE A 393 ? 0.9265 0.9265 0.9265 0.0000 0.0000 0.0000 376 ILE B CD1 
3034 N N   . ASN A 394 ? 0.9938 0.9938 0.9938 0.0000 0.0000 0.0000 377 ASN B N   
3035 C CA  . ASN A 394 ? 0.9938 0.9938 0.9938 0.0000 0.0000 0.0000 377 ASN B CA  
3036 C C   . ASN A 394 ? 0.9938 0.9938 0.9938 0.0000 0.0000 0.0000 377 ASN B C   
3037 O O   . ASN A 394 ? 0.9938 0.9938 0.9938 0.0000 0.0000 0.0000 377 ASN B O   
3038 C CB  . ASN A 394 ? 0.9938 0.9938 0.9938 0.0000 0.0000 0.0000 377 ASN B CB  
3039 C CG  . ASN A 394 ? 0.9938 0.9938 0.9938 0.0000 0.0000 0.0000 377 ASN B CG  
3040 O OD1 . ASN A 394 ? 0.9938 0.9938 0.9938 0.0000 0.0000 0.0000 377 ASN B OD1 
3041 N ND2 . ASN A 394 ? 0.9938 0.9938 0.9938 0.0000 0.0000 0.0000 377 ASN B ND2 
3042 N N   . ILE A 395 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 378 ILE B N   
3043 C CA  . ILE A 395 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 378 ILE B CA  
3044 C C   . ILE A 395 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 378 ILE B C   
3045 O O   . ILE A 395 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 378 ILE B O   
3046 C CB  . ILE A 395 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 378 ILE B CB  
3047 C CG1 . ILE A 395 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 378 ILE B CG1 
3048 C CG2 . ILE A 395 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 378 ILE B CG2 
3049 C CD1 . ILE A 395 ? 0.9444 0.9444 0.9444 0.0000 0.0000 0.0000 378 ILE B CD1 
3050 N N   . VAL A 396 ? 0.9621 0.9621 0.9621 0.0000 0.0000 0.0000 379 VAL B N   
3051 C CA  . VAL A 396 ? 0.9621 0.9621 0.9621 0.0000 0.0000 0.0000 379 VAL B CA  
3052 C C   . VAL A 396 ? 0.9621 0.9621 0.9621 0.0000 0.0000 0.0000 379 VAL B C   
3053 O O   . VAL A 396 ? 0.9621 0.9621 0.9621 0.0000 0.0000 0.0000 379 VAL B O   
3054 C CB  . VAL A 396 ? 0.9621 0.9621 0.9621 0.0000 0.0000 0.0000 379 VAL B CB  
3055 C CG1 . VAL A 396 ? 0.9621 0.9621 0.9621 0.0000 0.0000 0.0000 379 VAL B CG1 
3056 C CG2 . VAL A 396 ? 0.9621 0.9621 0.9621 0.0000 0.0000 0.0000 379 VAL B CG2 
3057 N N   . PRO A 397 ? 1.0320 1.0320 1.0320 0.0000 0.0000 0.0000 380 PRO B N   
3058 C CA  . PRO A 397 ? 1.0320 1.0320 1.0320 0.0000 0.0000 0.0000 380 PRO B CA  
3059 C C   . PRO A 397 ? 1.0320 1.0320 1.0320 0.0000 0.0000 0.0000 380 PRO B C   
3060 O O   . PRO A 397 ? 1.0320 1.0320 1.0320 0.0000 0.0000 0.0000 380 PRO B O   
3061 C CB  . PRO A 397 ? 1.0320 1.0320 1.0320 0.0000 0.0000 0.0000 380 PRO B CB  
3062 C CG  . PRO A 397 ? 1.0320 1.0320 1.0320 0.0000 0.0000 0.0000 380 PRO B CG  
3063 C CD  . PRO A 397 ? 1.0320 1.0320 1.0320 0.0000 0.0000 0.0000 380 PRO B CD  
3064 N N   . LYS A 398 ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 381 LYS B N   
3065 C CA  . LYS A 398 ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 381 LYS B CA  
3066 C C   . LYS A 398 ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 381 LYS B C   
3067 O O   . LYS A 398 ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 381 LYS B O   
3068 C CB  . LYS A 398 ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 381 LYS B CB  
3069 C CG  . LYS A 398 ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 381 LYS B CG  
3070 C CD  . LYS A 398 ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 381 LYS B CD  
3071 C CE  . LYS A 398 ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 381 LYS B CE  
3072 N NZ  . LYS A 398 ? 1.0635 1.0635 1.0635 0.0000 0.0000 0.0000 381 LYS B NZ  
3073 N N   . VAL A 399 ? 1.0832 1.0832 1.0832 0.0000 0.0000 0.0000 382 VAL B N   
3074 C CA  . VAL A 399 ? 1.0832 1.0832 1.0832 0.0000 0.0000 0.0000 382 VAL B CA  
3075 C C   . VAL A 399 ? 1.0832 1.0832 1.0832 0.0000 0.0000 0.0000 382 VAL B C   
3076 O O   . VAL A 399 ? 1.0832 1.0832 1.0832 0.0000 0.0000 0.0000 382 VAL B O   
3077 C CB  . VAL A 399 ? 1.0832 1.0832 1.0832 0.0000 0.0000 0.0000 382 VAL B CB  
3078 C CG1 . VAL A 399 ? 1.0832 1.0832 1.0832 0.0000 0.0000 0.0000 382 VAL B CG1 
3079 C CG2 . VAL A 399 ? 1.0832 1.0832 1.0832 0.0000 0.0000 0.0000 382 VAL B CG2 
3080 N N   . ASN A 400 ? 1.0861 1.0861 1.0861 0.0000 0.0000 0.0000 383 ASN B N   
3081 C CA  . ASN A 400 ? 1.0861 1.0861 1.0861 0.0000 0.0000 0.0000 383 ASN B CA  
3082 C C   . ASN A 400 ? 1.0861 1.0861 1.0861 0.0000 0.0000 0.0000 383 ASN B C   
3083 O O   . ASN A 400 ? 1.0861 1.0861 1.0861 0.0000 0.0000 0.0000 383 ASN B O   
3084 C CB  . ASN A 400 ? 1.0861 1.0861 1.0861 0.0000 0.0000 0.0000 383 ASN B CB  
3085 C CG  . ASN A 400 ? 1.0861 1.0861 1.0861 0.0000 0.0000 0.0000 383 ASN B CG  
3086 O OD1 . ASN A 400 ? 1.0861 1.0861 1.0861 0.0000 0.0000 0.0000 383 ASN B OD1 
3087 N ND2 . ASN A 400 ? 1.0861 1.0861 1.0861 0.0000 0.0000 0.0000 383 ASN B ND2 
3088 N N   . TYR A 401 ? 1.0437 1.0437 1.0437 0.0000 0.0000 0.0000 384 TYR B N   
3089 C CA  . TYR A 401 ? 1.0437 1.0437 1.0437 0.0000 0.0000 0.0000 384 TYR B CA  
3090 C C   . TYR A 401 ? 1.0437 1.0437 1.0437 0.0000 0.0000 0.0000 384 TYR B C   
3091 O O   . TYR A 401 ? 1.0437 1.0437 1.0437 0.0000 0.0000 0.0000 384 TYR B O   
3092 C CB  . TYR A 401 ? 1.0437 1.0437 1.0437 0.0000 0.0000 0.0000 384 TYR B CB  
3093 C CG  . TYR A 401 ? 1.0437 1.0437 1.0437 0.0000 0.0000 0.0000 384 TYR B CG  
3094 C CD1 . TYR A 401 ? 1.0437 1.0437 1.0437 0.0000 0.0000 0.0000 384 TYR B CD1 
3095 C CD2 . TYR A 401 ? 1.0437 1.0437 1.0437 0.0000 0.0000 0.0000 384 TYR B CD2 
3096 C CE1 . TYR A 401 ? 1.0437 1.0437 1.0437 0.0000 0.0000 0.0000 384 TYR B CE1 
3097 C CE2 . TYR A 401 ? 1.0437 1.0437 1.0437 0.0000 0.0000 0.0000 384 TYR B CE2 
3098 C CZ  . TYR A 401 ? 1.0437 1.0437 1.0437 0.0000 0.0000 0.0000 384 TYR B CZ  
3099 O OH  . TYR A 401 ? 1.0437 1.0437 1.0437 0.0000 0.0000 0.0000 384 TYR B OH  
3100 N N   . THR A 402 ? 1.0956 1.0956 1.0956 0.0000 0.0000 0.0000 385 THR B N   
3101 C CA  . THR A 402 ? 1.0956 1.0956 1.0956 0.0000 0.0000 0.0000 385 THR B CA  
3102 C C   . THR A 402 ? 1.0956 1.0956 1.0956 0.0000 0.0000 0.0000 385 THR B C   
3103 O O   . THR A 402 ? 1.0956 1.0956 1.0956 0.0000 0.0000 0.0000 385 THR B O   
3104 C CB  . THR A 402 ? 1.0956 1.0956 1.0956 0.0000 0.0000 0.0000 385 THR B CB  
3105 O OG1 . THR A 402 ? 1.0956 1.0956 1.0956 0.0000 0.0000 0.0000 385 THR B OG1 
3106 C CG2 . THR A 402 ? 1.0956 1.0956 1.0956 0.0000 0.0000 0.0000 385 THR B CG2 
3107 N N   . ILE A 403 ? 1.0073 1.0073 1.0073 0.0000 0.0000 0.0000 386 ILE B N   
3108 C CA  . ILE A 403 ? 1.0073 1.0073 1.0073 0.0000 0.0000 0.0000 386 ILE B CA  
3109 C C   . ILE A 403 ? 1.0073 1.0073 1.0073 0.0000 0.0000 0.0000 386 ILE B C   
3110 O O   . ILE A 403 ? 1.0073 1.0073 1.0073 0.0000 0.0000 0.0000 386 ILE B O   
3111 C CB  . ILE A 403 ? 1.0073 1.0073 1.0073 0.0000 0.0000 0.0000 386 ILE B CB  
3112 C CG1 . ILE A 403 ? 1.0073 1.0073 1.0073 0.0000 0.0000 0.0000 386 ILE B CG1 
3113 C CG2 . ILE A 403 ? 1.0073 1.0073 1.0073 0.0000 0.0000 0.0000 386 ILE B CG2 
3114 C CD1 . ILE A 403 ? 1.0073 1.0073 1.0073 0.0000 0.0000 0.0000 386 ILE B CD1 
3115 N N   . TYR A 404 ? 1.0825 1.0825 1.0825 0.0000 0.0000 0.0000 387 TYR B N   
3116 C CA  . TYR A 404 ? 1.0825 1.0825 1.0825 0.0000 0.0000 0.0000 387 TYR B CA  
3117 C C   . TYR A 404 ? 1.0825 1.0825 1.0825 0.0000 0.0000 0.0000 387 TYR B C   
3118 O O   . TYR A 404 ? 1.0825 1.0825 1.0825 0.0000 0.0000 0.0000 387 TYR B O   
3119 C CB  . TYR A 404 ? 1.0825 1.0825 1.0825 0.0000 0.0000 0.0000 387 TYR B CB  
3120 C CG  . TYR A 404 ? 1.0825 1.0825 1.0825 0.0000 0.0000 0.0000 387 TYR B CG  
3121 C CD1 . TYR A 404 ? 1.0825 1.0825 1.0825 0.0000 0.0000 0.0000 387 TYR B CD1 
3122 C CD2 . TYR A 404 ? 1.0825 1.0825 1.0825 0.0000 0.0000 0.0000 387 TYR B CD2 
3123 C CE1 . TYR A 404 ? 1.0825 1.0825 1.0825 0.0000 0.0000 0.0000 387 TYR B CE1 
3124 C CE2 . TYR A 404 ? 1.0825 1.0825 1.0825 0.0000 0.0000 0.0000 387 TYR B CE2 
3125 C CZ  . TYR A 404 ? 1.0825 1.0825 1.0825 0.0000 0.0000 0.0000 387 TYR B CZ  
3126 O OH  . TYR A 404 ? 1.0825 1.0825 1.0825 0.0000 0.0000 0.0000 387 TYR B OH  
3127 N N   . ASP A 405 ? 1.1452 1.1452 1.1452 0.0000 0.0000 0.0000 388 ASP B N   
3128 C CA  . ASP A 405 ? 1.1452 1.1452 1.1452 0.0000 0.0000 0.0000 388 ASP B CA  
3129 C C   . ASP A 405 ? 1.1452 1.1452 1.1452 0.0000 0.0000 0.0000 388 ASP B C   
3130 O O   . ASP A 405 ? 1.1452 1.1452 1.1452 0.0000 0.0000 0.0000 388 ASP B O   
3131 C CB  . ASP A 405 ? 1.1452 1.1452 1.1452 0.0000 0.0000 0.0000 388 ASP B CB  
3132 C CG  . ASP A 405 ? 1.1452 1.1452 1.1452 0.0000 0.0000 0.0000 388 ASP B CG  
3133 O OD1 . ASP A 405 ? 1.1452 1.1452 1.1452 0.0000 0.0000 0.0000 388 ASP B OD1 
3134 O OD2 . ASP A 405 ? 1.1452 1.1452 1.1452 0.0000 0.0000 0.0000 388 ASP B OD2 
3135 N N   . GLY A 406 ? 1.1062 1.1062 1.1062 0.0000 0.0000 0.0000 389 GLY B N   
3136 C CA  . GLY A 406 ? 1.1062 1.1062 1.1062 0.0000 0.0000 0.0000 389 GLY B CA  
3137 C C   . GLY A 406 ? 1.1062 1.1062 1.1062 0.0000 0.0000 0.0000 389 GLY B C   
3138 O O   . GLY A 406 ? 1.1062 1.1062 1.1062 0.0000 0.0000 0.0000 389 GLY B O   
3139 N N   . PHE A 407 ? 1.1519 1.1519 1.1519 0.0000 0.0000 0.0000 390 PHE B N   
3140 C CA  . PHE A 407 ? 1.1519 1.1519 1.1519 0.0000 0.0000 0.0000 390 PHE B CA  
3141 C C   . PHE A 407 ? 1.1519 1.1519 1.1519 0.0000 0.0000 0.0000 390 PHE B C   
3142 O O   . PHE A 407 ? 1.1519 1.1519 1.1519 0.0000 0.0000 0.0000 390 PHE B O   
3143 C CB  . PHE A 407 ? 1.1519 1.1519 1.1519 0.0000 0.0000 0.0000 390 PHE B CB  
3144 C CG  . PHE A 407 ? 1.1519 1.1519 1.1519 0.0000 0.0000 0.0000 390 PHE B CG  
3145 C CD1 . PHE A 407 ? 1.1519 1.1519 1.1519 0.0000 0.0000 0.0000 390 PHE B CD1 
3146 C CD2 . PHE A 407 ? 1.1519 1.1519 1.1519 0.0000 0.0000 0.0000 390 PHE B CD2 
3147 C CE1 . PHE A 407 ? 1.1519 1.1519 1.1519 0.0000 0.0000 0.0000 390 PHE B CE1 
3148 C CE2 . PHE A 407 ? 1.1519 1.1519 1.1519 0.0000 0.0000 0.0000 390 PHE B CE2 
3149 C CZ  . PHE A 407 ? 1.1519 1.1519 1.1519 0.0000 0.0000 0.0000 390 PHE B CZ  
3150 N N   . ASN A 408 ? 1.2316 1.2316 1.2316 0.0000 0.0000 0.0000 391 ASN B N   
3151 C CA  . ASN A 408 ? 1.2316 1.2316 1.2316 0.0000 0.0000 0.0000 391 ASN B CA  
3152 C C   . ASN A 408 ? 1.2316 1.2316 1.2316 0.0000 0.0000 0.0000 391 ASN B C   
3153 O O   . ASN A 408 ? 1.2316 1.2316 1.2316 0.0000 0.0000 0.0000 391 ASN B O   
3154 C CB  . ASN A 408 ? 1.2316 1.2316 1.2316 0.0000 0.0000 0.0000 391 ASN B CB  
3155 C CG  . ASN A 408 ? 1.2316 1.2316 1.2316 0.0000 0.0000 0.0000 391 ASN B CG  
3156 O OD1 . ASN A 408 ? 1.2316 1.2316 1.2316 0.0000 0.0000 0.0000 391 ASN B OD1 
3157 N ND2 . ASN A 408 ? 1.2316 1.2316 1.2316 0.0000 0.0000 0.0000 391 ASN B ND2 
3158 N N   . LEU A 409 ? 1.3136 1.3136 1.3136 0.0000 0.0000 0.0000 392 LEU B N   
3159 C CA  . LEU A 409 ? 1.3136 1.3136 1.3136 0.0000 0.0000 0.0000 392 LEU B CA  
3160 C C   . LEU A 409 ? 1.3136 1.3136 1.3136 0.0000 0.0000 0.0000 392 LEU B C   
3161 O O   . LEU A 409 ? 1.3136 1.3136 1.3136 0.0000 0.0000 0.0000 392 LEU B O   
3162 C CB  . LEU A 409 ? 1.3136 1.3136 1.3136 0.0000 0.0000 0.0000 392 LEU B CB  
3163 C CG  . LEU A 409 ? 1.3136 1.3136 1.3136 0.0000 0.0000 0.0000 392 LEU B CG  
3164 C CD1 . LEU A 409 ? 1.3136 1.3136 1.3136 0.0000 0.0000 0.0000 392 LEU B CD1 
3165 C CD2 . LEU A 409 ? 1.3136 1.3136 1.3136 0.0000 0.0000 0.0000 392 LEU B CD2 
3166 N N   . ARG A 410 ? 1.4097 1.4097 1.4097 0.0000 0.0000 0.0000 393 ARG B N   
3167 C CA  . ARG A 410 ? 1.4097 1.4097 1.4097 0.0000 0.0000 0.0000 393 ARG B CA  
3168 C C   . ARG A 410 ? 1.4097 1.4097 1.4097 0.0000 0.0000 0.0000 393 ARG B C   
3169 O O   . ARG A 410 ? 1.4097 1.4097 1.4097 0.0000 0.0000 0.0000 393 ARG B O   
3170 C CB  . ARG A 410 ? 1.4097 1.4097 1.4097 0.0000 0.0000 0.0000 393 ARG B CB  
3171 C CG  . ARG A 410 ? 1.4097 1.4097 1.4097 0.0000 0.0000 0.0000 393 ARG B CG  
3172 C CD  . ARG A 410 ? 1.4097 1.4097 1.4097 0.0000 0.0000 0.0000 393 ARG B CD  
3173 N NE  . ARG A 410 ? 1.4097 1.4097 1.4097 0.0000 0.0000 0.0000 393 ARG B NE  
3174 C CZ  . ARG A 410 ? 1.4097 1.4097 1.4097 0.0000 0.0000 0.0000 393 ARG B CZ  
3175 N NH1 . ARG A 410 ? 1.4097 1.4097 1.4097 0.0000 0.0000 0.0000 393 ARG B NH1 
3176 N NH2 . ARG A 410 ? 1.4097 1.4097 1.4097 0.0000 0.0000 0.0000 393 ARG B NH2 
3177 N N   . ASN A 411 ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 394 ASN B N   
3178 C CA  . ASN A 411 ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 394 ASN B CA  
3179 C C   . ASN A 411 ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 394 ASN B C   
3180 O O   . ASN A 411 ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 394 ASN B O   
3181 C CB  . ASN A 411 ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 394 ASN B CB  
3182 C CG  . ASN A 411 ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 394 ASN B CG  
3183 O OD1 . ASN A 411 ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 394 ASN B OD1 
3184 N ND2 . ASN A 411 ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 394 ASN B ND2 
3185 N N   . THR A 412 ? 1.4556 1.4556 1.4556 0.0000 0.0000 0.0000 395 THR B N   
3186 C CA  . THR A 412 ? 1.4556 1.4556 1.4556 0.0000 0.0000 0.0000 395 THR B CA  
3187 C C   . THR A 412 ? 1.4556 1.4556 1.4556 0.0000 0.0000 0.0000 395 THR B C   
3188 O O   . THR A 412 ? 1.4556 1.4556 1.4556 0.0000 0.0000 0.0000 395 THR B O   
3189 C CB  . THR A 412 ? 1.4556 1.4556 1.4556 0.0000 0.0000 0.0000 395 THR B CB  
3190 O OG1 . THR A 412 ? 1.4556 1.4556 1.4556 0.0000 0.0000 0.0000 395 THR B OG1 
3191 C CG2 . THR A 412 ? 1.4556 1.4556 1.4556 0.0000 0.0000 0.0000 395 THR B CG2 
3192 N N   . ASN A 413 ? 1.4534 1.4534 1.4534 0.0000 0.0000 0.0000 396 ASN B N   
3193 C CA  . ASN A 413 ? 1.4534 1.4534 1.4534 0.0000 0.0000 0.0000 396 ASN B CA  
3194 C C   . ASN A 413 ? 1.4534 1.4534 1.4534 0.0000 0.0000 0.0000 396 ASN B C   
3195 O O   . ASN A 413 ? 1.4534 1.4534 1.4534 0.0000 0.0000 0.0000 396 ASN B O   
3196 C CB  . ASN A 413 ? 1.4534 1.4534 1.4534 0.0000 0.0000 0.0000 396 ASN B CB  
3197 C CG  . ASN A 413 ? 1.4534 1.4534 1.4534 0.0000 0.0000 0.0000 396 ASN B CG  
3198 O OD1 . ASN A 413 ? 1.4534 1.4534 1.4534 0.0000 0.0000 0.0000 396 ASN B OD1 
3199 N ND2 . ASN A 413 ? 1.4534 1.4534 1.4534 0.0000 0.0000 0.0000 396 ASN B ND2 
3200 N N   . LEU A 414 ? 1.3955 1.3955 1.3955 0.0000 0.0000 0.0000 397 LEU B N   
3201 C CA  . LEU A 414 ? 1.3955 1.3955 1.3955 0.0000 0.0000 0.0000 397 LEU B CA  
3202 C C   . LEU A 414 ? 1.3955 1.3955 1.3955 0.0000 0.0000 0.0000 397 LEU B C   
3203 O O   . LEU A 414 ? 1.3955 1.3955 1.3955 0.0000 0.0000 0.0000 397 LEU B O   
3204 C CB  . LEU A 414 ? 1.3955 1.3955 1.3955 0.0000 0.0000 0.0000 397 LEU B CB  
3205 C CG  . LEU A 414 ? 1.3955 1.3955 1.3955 0.0000 0.0000 0.0000 397 LEU B CG  
3206 C CD1 . LEU A 414 ? 1.3955 1.3955 1.3955 0.0000 0.0000 0.0000 397 LEU B CD1 
3207 C CD2 . LEU A 414 ? 1.3955 1.3955 1.3955 0.0000 0.0000 0.0000 397 LEU B CD2 
3208 N N   . ALA A 415 ? 1.4287 1.4287 1.4287 0.0000 0.0000 0.0000 398 ALA B N   
3209 C CA  . ALA A 415 ? 1.4287 1.4287 1.4287 0.0000 0.0000 0.0000 398 ALA B CA  
3210 C C   . ALA A 415 ? 1.4287 1.4287 1.4287 0.0000 0.0000 0.0000 398 ALA B C   
3211 O O   . ALA A 415 ? 1.4287 1.4287 1.4287 0.0000 0.0000 0.0000 398 ALA B O   
3212 C CB  . ALA A 415 ? 1.4287 1.4287 1.4287 0.0000 0.0000 0.0000 398 ALA B CB  
3213 N N   . ALA A 416 ? 1.3729 1.3729 1.3729 0.0000 0.0000 0.0000 399 ALA B N   
3214 C CA  . ALA A 416 ? 1.3729 1.3729 1.3729 0.0000 0.0000 0.0000 399 ALA B CA  
3215 C C   . ALA A 416 ? 1.3729 1.3729 1.3729 0.0000 0.0000 0.0000 399 ALA B C   
3216 O O   . ALA A 416 ? 1.3729 1.3729 1.3729 0.0000 0.0000 0.0000 399 ALA B O   
3217 C CB  . ALA A 416 ? 1.3729 1.3729 1.3729 0.0000 0.0000 0.0000 399 ALA B CB  
3218 N N   . ASN A 417 ? 1.3379 1.3379 1.3379 0.0000 0.0000 0.0000 400 ASN B N   
3219 C CA  . ASN A 417 ? 1.3379 1.3379 1.3379 0.0000 0.0000 0.0000 400 ASN B CA  
3220 C C   . ASN A 417 ? 1.3379 1.3379 1.3379 0.0000 0.0000 0.0000 400 ASN B C   
3221 O O   . ASN A 417 ? 1.3379 1.3379 1.3379 0.0000 0.0000 0.0000 400 ASN B O   
3222 C CB  . ASN A 417 ? 1.3379 1.3379 1.3379 0.0000 0.0000 0.0000 400 ASN B CB  
3223 C CG  . ASN A 417 ? 1.3379 1.3379 1.3379 0.0000 0.0000 0.0000 400 ASN B CG  
3224 O OD1 . ASN A 417 ? 1.3379 1.3379 1.3379 0.0000 0.0000 0.0000 400 ASN B OD1 
3225 N ND2 . ASN A 417 ? 1.3379 1.3379 1.3379 0.0000 0.0000 0.0000 400 ASN B ND2 
3226 N N   . PHE A 418 ? 1.2221 1.2221 1.2221 0.0000 0.0000 0.0000 401 PHE B N   
3227 C CA  . PHE A 418 ? 1.2221 1.2221 1.2221 0.0000 0.0000 0.0000 401 PHE B CA  
3228 C C   . PHE A 418 ? 1.2221 1.2221 1.2221 0.0000 0.0000 0.0000 401 PHE B C   
3229 O O   . PHE A 418 ? 1.2221 1.2221 1.2221 0.0000 0.0000 0.0000 401 PHE B O   
3230 C CB  . PHE A 418 ? 1.2221 1.2221 1.2221 0.0000 0.0000 0.0000 401 PHE B CB  
3231 C CG  . PHE A 418 ? 1.2221 1.2221 1.2221 0.0000 0.0000 0.0000 401 PHE B CG  
3232 C CD1 . PHE A 418 ? 1.2221 1.2221 1.2221 0.0000 0.0000 0.0000 401 PHE B CD1 
3233 C CD2 . PHE A 418 ? 1.2221 1.2221 1.2221 0.0000 0.0000 0.0000 401 PHE B CD2 
3234 C CE1 . PHE A 418 ? 1.2221 1.2221 1.2221 0.0000 0.0000 0.0000 401 PHE B CE1 
3235 C CE2 . PHE A 418 ? 1.2221 1.2221 1.2221 0.0000 0.0000 0.0000 401 PHE B CE2 
3236 C CZ  . PHE A 418 ? 1.2221 1.2221 1.2221 0.0000 0.0000 0.0000 401 PHE B CZ  
3237 N N   . ASN A 419 ? 1.3089 1.3089 1.3089 0.0000 0.0000 0.0000 402 ASN B N   
3238 C CA  . ASN A 419 ? 1.3089 1.3089 1.3089 0.0000 0.0000 0.0000 402 ASN B CA  
3239 C C   . ASN A 419 ? 1.3089 1.3089 1.3089 0.0000 0.0000 0.0000 402 ASN B C   
3240 O O   . ASN A 419 ? 1.3089 1.3089 1.3089 0.0000 0.0000 0.0000 402 ASN B O   
3241 C CB  . ASN A 419 ? 1.3089 1.3089 1.3089 0.0000 0.0000 0.0000 402 ASN B CB  
3242 C CG  . ASN A 419 ? 1.3089 1.3089 1.3089 0.0000 0.0000 0.0000 402 ASN B CG  
3243 O OD1 . ASN A 419 ? 1.3089 1.3089 1.3089 0.0000 0.0000 0.0000 402 ASN B OD1 
3244 N ND2 . ASN A 419 ? 1.3089 1.3089 1.3089 0.0000 0.0000 0.0000 402 ASN B ND2 
3245 N N   . GLY A 420 ? 1.2458 1.2458 1.2458 0.0000 0.0000 0.0000 403 GLY B N   
3246 C CA  . GLY A 420 ? 1.2458 1.2458 1.2458 0.0000 0.0000 0.0000 403 GLY B CA  
3247 C C   . GLY A 420 ? 1.2458 1.2458 1.2458 0.0000 0.0000 0.0000 403 GLY B C   
3248 O O   . GLY A 420 ? 1.2458 1.2458 1.2458 0.0000 0.0000 0.0000 403 GLY B O   
3249 N N   . GLN A 421 ? 1.1615 1.1615 1.1615 0.0000 0.0000 0.0000 404 GLN B N   
3250 C CA  . GLN A 421 ? 1.1615 1.1615 1.1615 0.0000 0.0000 0.0000 404 GLN B CA  
3251 C C   . GLN A 421 ? 1.1615 1.1615 1.1615 0.0000 0.0000 0.0000 404 GLN B C   
3252 O O   . GLN A 421 ? 1.1615 1.1615 1.1615 0.0000 0.0000 0.0000 404 GLN B O   
3253 C CB  . GLN A 421 ? 1.1615 1.1615 1.1615 0.0000 0.0000 0.0000 404 GLN B CB  
3254 C CG  . GLN A 421 ? 1.1615 1.1615 1.1615 0.0000 0.0000 0.0000 404 GLN B CG  
3255 C CD  . GLN A 421 ? 1.1615 1.1615 1.1615 0.0000 0.0000 0.0000 404 GLN B CD  
3256 O OE1 . GLN A 421 ? 1.1615 1.1615 1.1615 0.0000 0.0000 0.0000 404 GLN B OE1 
3257 N NE2 . GLN A 421 ? 1.1615 1.1615 1.1615 0.0000 0.0000 0.0000 404 GLN B NE2 
3258 N N   . ASN A 422 ? 1.1764 1.1764 1.1764 0.0000 0.0000 0.0000 405 ASN B N   
3259 C CA  . ASN A 422 ? 1.1764 1.1764 1.1764 0.0000 0.0000 0.0000 405 ASN B CA  
3260 C C   . ASN A 422 ? 1.1764 1.1764 1.1764 0.0000 0.0000 0.0000 405 ASN B C   
3261 O O   . ASN A 422 ? 1.1764 1.1764 1.1764 0.0000 0.0000 0.0000 405 ASN B O   
3262 C CB  . ASN A 422 ? 1.1764 1.1764 1.1764 0.0000 0.0000 0.0000 405 ASN B CB  
3263 C CG  . ASN A 422 ? 1.1764 1.1764 1.1764 0.0000 0.0000 0.0000 405 ASN B CG  
3264 O OD1 . ASN A 422 ? 1.1764 1.1764 1.1764 0.0000 0.0000 0.0000 405 ASN B OD1 
3265 N ND2 . ASN A 422 ? 1.1764 1.1764 1.1764 0.0000 0.0000 0.0000 405 ASN B ND2 
3266 N N   . THR A 423 ? 1.2097 1.2097 1.2097 0.0000 0.0000 0.0000 406 THR B N   
3267 C CA  . THR A 423 ? 1.2097 1.2097 1.2097 0.0000 0.0000 0.0000 406 THR B CA  
3268 C C   . THR A 423 ? 1.2097 1.2097 1.2097 0.0000 0.0000 0.0000 406 THR B C   
3269 O O   . THR A 423 ? 1.2097 1.2097 1.2097 0.0000 0.0000 0.0000 406 THR B O   
3270 C CB  . THR A 423 ? 1.2097 1.2097 1.2097 0.0000 0.0000 0.0000 406 THR B CB  
3271 O OG1 . THR A 423 ? 1.2097 1.2097 1.2097 0.0000 0.0000 0.0000 406 THR B OG1 
3272 C CG2 . THR A 423 ? 1.2097 1.2097 1.2097 0.0000 0.0000 0.0000 406 THR B CG2 
3273 N N   . GLU A 424 ? 1.2683 1.2683 1.2683 0.0000 0.0000 0.0000 407 GLU B N   
3274 C CA  . GLU A 424 ? 1.2683 1.2683 1.2683 0.0000 0.0000 0.0000 407 GLU B CA  
3275 C C   . GLU A 424 ? 1.2683 1.2683 1.2683 0.0000 0.0000 0.0000 407 GLU B C   
3276 O O   . GLU A 424 ? 1.2683 1.2683 1.2683 0.0000 0.0000 0.0000 407 GLU B O   
3277 C CB  . GLU A 424 ? 1.2683 1.2683 1.2683 0.0000 0.0000 0.0000 407 GLU B CB  
3278 C CG  . GLU A 424 ? 1.2683 1.2683 1.2683 0.0000 0.0000 0.0000 407 GLU B CG  
3279 C CD  . GLU A 424 ? 1.2683 1.2683 1.2683 0.0000 0.0000 0.0000 407 GLU B CD  
3280 O OE1 . GLU A 424 ? 1.2683 1.2683 1.2683 0.0000 0.0000 0.0000 407 GLU B OE1 
3281 O OE2 . GLU A 424 ? 1.2683 1.2683 1.2683 0.0000 0.0000 0.0000 407 GLU B OE2 
3282 N N   . ILE A 425 ? 1.2465 1.2465 1.2465 0.0000 0.0000 0.0000 408 ILE B N   
3283 C CA  . ILE A 425 ? 1.2465 1.2465 1.2465 0.0000 0.0000 0.0000 408 ILE B CA  
3284 C C   . ILE A 425 ? 1.2465 1.2465 1.2465 0.0000 0.0000 0.0000 408 ILE B C   
3285 O O   . ILE A 425 ? 1.2465 1.2465 1.2465 0.0000 0.0000 0.0000 408 ILE B O   
3286 C CB  . ILE A 425 ? 1.2465 1.2465 1.2465 0.0000 0.0000 0.0000 408 ILE B CB  
3287 C CG1 . ILE A 425 ? 1.2465 1.2465 1.2465 0.0000 0.0000 0.0000 408 ILE B CG1 
3288 C CG2 . ILE A 425 ? 1.2465 1.2465 1.2465 0.0000 0.0000 0.0000 408 ILE B CG2 
3289 C CD1 . ILE A 425 ? 1.2465 1.2465 1.2465 0.0000 0.0000 0.0000 408 ILE B CD1 
3290 N N   . ASN A 426 ? 1.2181 1.2181 1.2181 0.0000 0.0000 0.0000 409 ASN B N   
3291 C CA  . ASN A 426 ? 1.2181 1.2181 1.2181 0.0000 0.0000 0.0000 409 ASN B CA  
3292 C C   . ASN A 426 ? 1.2181 1.2181 1.2181 0.0000 0.0000 0.0000 409 ASN B C   
3293 O O   . ASN A 426 ? 1.2181 1.2181 1.2181 0.0000 0.0000 0.0000 409 ASN B O   
3294 C CB  . ASN A 426 ? 1.2181 1.2181 1.2181 0.0000 0.0000 0.0000 409 ASN B CB  
3295 C CG  . ASN A 426 ? 1.2181 1.2181 1.2181 0.0000 0.0000 0.0000 409 ASN B CG  
3296 O OD1 . ASN A 426 ? 1.2181 1.2181 1.2181 0.0000 0.0000 0.0000 409 ASN B OD1 
3297 N ND2 . ASN A 426 ? 1.2181 1.2181 1.2181 0.0000 0.0000 0.0000 409 ASN B ND2 
3298 N N   . ASN A 427 ? 1.2471 1.2471 1.2471 0.0000 0.0000 0.0000 410 ASN B N   
3299 C CA  . ASN A 427 ? 1.2471 1.2471 1.2471 0.0000 0.0000 0.0000 410 ASN B CA  
3300 C C   . ASN A 427 ? 1.2471 1.2471 1.2471 0.0000 0.0000 0.0000 410 ASN B C   
3301 O O   . ASN A 427 ? 1.2471 1.2471 1.2471 0.0000 0.0000 0.0000 410 ASN B O   
3302 C CB  . ASN A 427 ? 1.2471 1.2471 1.2471 0.0000 0.0000 0.0000 410 ASN B CB  
3303 C CG  . ASN A 427 ? 1.2471 1.2471 1.2471 0.0000 0.0000 0.0000 410 ASN B CG  
3304 O OD1 . ASN A 427 ? 1.2471 1.2471 1.2471 0.0000 0.0000 0.0000 410 ASN B OD1 
3305 N ND2 . ASN A 427 ? 1.2471 1.2471 1.2471 0.0000 0.0000 0.0000 410 ASN B ND2 
3306 N N   . MET A 428 ? 1.2171 1.2171 1.2171 0.0000 0.0000 0.0000 411 MET B N   
3307 C CA  . MET A 428 ? 1.2171 1.2171 1.2171 0.0000 0.0000 0.0000 411 MET B CA  
3308 C C   . MET A 428 ? 1.2171 1.2171 1.2171 0.0000 0.0000 0.0000 411 MET B C   
3309 O O   . MET A 428 ? 1.2171 1.2171 1.2171 0.0000 0.0000 0.0000 411 MET B O   
3310 C CB  . MET A 428 ? 1.2171 1.2171 1.2171 0.0000 0.0000 0.0000 411 MET B CB  
3311 C CG  . MET A 428 ? 1.2171 1.2171 1.2171 0.0000 0.0000 0.0000 411 MET B CG  
3312 S SD  . MET A 428 ? 1.2171 1.2171 1.2171 0.0000 0.0000 0.0000 411 MET B SD  
3313 C CE  . MET A 428 ? 1.2171 1.2171 1.2171 0.0000 0.0000 0.0000 411 MET B CE  
3314 N N   . ASN A 429 ? 1.1639 1.1639 1.1639 0.0000 0.0000 0.0000 412 ASN B N   
3315 C CA  . ASN A 429 ? 1.1639 1.1639 1.1639 0.0000 0.0000 0.0000 412 ASN B CA  
3316 C C   . ASN A 429 ? 1.1639 1.1639 1.1639 0.0000 0.0000 0.0000 412 ASN B C   
3317 O O   . ASN A 429 ? 1.1639 1.1639 1.1639 0.0000 0.0000 0.0000 412 ASN B O   
3318 C CB  . ASN A 429 ? 1.1639 1.1639 1.1639 0.0000 0.0000 0.0000 412 ASN B CB  
3319 C CG  . ASN A 429 ? 1.1639 1.1639 1.1639 0.0000 0.0000 0.0000 412 ASN B CG  
3320 O OD1 . ASN A 429 ? 1.1639 1.1639 1.1639 0.0000 0.0000 0.0000 412 ASN B OD1 
3321 N ND2 . ASN A 429 ? 1.1639 1.1639 1.1639 0.0000 0.0000 0.0000 412 ASN B ND2 
3322 N N   . PHE A 430 ? 1.1044 1.1044 1.1044 0.0000 0.0000 0.0000 413 PHE B N   
3323 C CA  . PHE A 430 ? 1.1044 1.1044 1.1044 0.0000 0.0000 0.0000 413 PHE B CA  
3324 C C   . PHE A 430 ? 1.1044 1.1044 1.1044 0.0000 0.0000 0.0000 413 PHE B C   
3325 O O   . PHE A 430 ? 1.1044 1.1044 1.1044 0.0000 0.0000 0.0000 413 PHE B O   
3326 C CB  . PHE A 430 ? 1.1044 1.1044 1.1044 0.0000 0.0000 0.0000 413 PHE B CB  
3327 C CG  . PHE A 430 ? 1.1044 1.1044 1.1044 0.0000 0.0000 0.0000 413 PHE B CG  
3328 C CD1 . PHE A 430 ? 1.1044 1.1044 1.1044 0.0000 0.0000 0.0000 413 PHE B CD1 
3329 C CD2 . PHE A 430 ? 1.1044 1.1044 1.1044 0.0000 0.0000 0.0000 413 PHE B CD2 
3330 C CE1 . PHE A 430 ? 1.1044 1.1044 1.1044 0.0000 0.0000 0.0000 413 PHE B CE1 
3331 C CE2 . PHE A 430 ? 1.1044 1.1044 1.1044 0.0000 0.0000 0.0000 413 PHE B CE2 
3332 C CZ  . PHE A 430 ? 1.1044 1.1044 1.1044 0.0000 0.0000 0.0000 413 PHE B CZ  
3333 N N   . THR A 431 ? 1.0382 1.0382 1.0382 0.0000 0.0000 0.0000 414 THR B N   
3334 C CA  . THR A 431 ? 1.0382 1.0382 1.0382 0.0000 0.0000 0.0000 414 THR B CA  
3335 C C   . THR A 431 ? 1.0382 1.0382 1.0382 0.0000 0.0000 0.0000 414 THR B C   
3336 O O   . THR A 431 ? 1.0382 1.0382 1.0382 0.0000 0.0000 0.0000 414 THR B O   
3337 C CB  . THR A 431 ? 1.0382 1.0382 1.0382 0.0000 0.0000 0.0000 414 THR B CB  
3338 O OG1 . THR A 431 ? 1.0382 1.0382 1.0382 0.0000 0.0000 0.0000 414 THR B OG1 
3339 C CG2 . THR A 431 ? 1.0382 1.0382 1.0382 0.0000 0.0000 0.0000 414 THR B CG2 
3340 N N   . LYS A 432 ? 0.9755 0.9755 0.9755 0.0000 0.0000 0.0000 415 LYS B N   
3341 C CA  . LYS A 432 ? 0.9755 0.9755 0.9755 0.0000 0.0000 0.0000 415 LYS B CA  
3342 C C   . LYS A 432 ? 0.9755 0.9755 0.9755 0.0000 0.0000 0.0000 415 LYS B C   
3343 O O   . LYS A 432 ? 0.9755 0.9755 0.9755 0.0000 0.0000 0.0000 415 LYS B O   
3344 C CB  . LYS A 432 ? 0.9755 0.9755 0.9755 0.0000 0.0000 0.0000 415 LYS B CB  
3345 C CG  . LYS A 432 ? 0.9755 0.9755 0.9755 0.0000 0.0000 0.0000 415 LYS B CG  
3346 C CD  . LYS A 432 ? 0.9755 0.9755 0.9755 0.0000 0.0000 0.0000 415 LYS B CD  
3347 C CE  . LYS A 432 ? 0.9755 0.9755 0.9755 0.0000 0.0000 0.0000 415 LYS B CE  
3348 N NZ  . LYS A 432 ? 0.9755 0.9755 0.9755 0.0000 0.0000 0.0000 415 LYS B NZ  
3349 N N   . LEU A 433 ? 0.9446 0.9446 0.9446 0.0000 0.0000 0.0000 416 LEU B N   
3350 C CA  . LEU A 433 ? 0.9446 0.9446 0.9446 0.0000 0.0000 0.0000 416 LEU B CA  
3351 C C   . LEU A 433 ? 0.9446 0.9446 0.9446 0.0000 0.0000 0.0000 416 LEU B C   
3352 O O   . LEU A 433 ? 0.9446 0.9446 0.9446 0.0000 0.0000 0.0000 416 LEU B O   
3353 C CB  . LEU A 433 ? 0.9446 0.9446 0.9446 0.0000 0.0000 0.0000 416 LEU B CB  
3354 C CG  . LEU A 433 ? 0.9446 0.9446 0.9446 0.0000 0.0000 0.0000 416 LEU B CG  
3355 C CD1 . LEU A 433 ? 0.9446 0.9446 0.9446 0.0000 0.0000 0.0000 416 LEU B CD1 
3356 C CD2 . LEU A 433 ? 0.9446 0.9446 0.9446 0.0000 0.0000 0.0000 416 LEU B CD2 
3357 N N   . LYS A 434 ? 0.9817 0.9817 0.9817 0.0000 0.0000 0.0000 417 LYS B N   
3358 C CA  . LYS A 434 ? 0.9817 0.9817 0.9817 0.0000 0.0000 0.0000 417 LYS B CA  
3359 C C   . LYS A 434 ? 0.9817 0.9817 0.9817 0.0000 0.0000 0.0000 417 LYS B C   
3360 O O   . LYS A 434 ? 0.9817 0.9817 0.9817 0.0000 0.0000 0.0000 417 LYS B O   
3361 C CB  . LYS A 434 ? 0.9817 0.9817 0.9817 0.0000 0.0000 0.0000 417 LYS B CB  
3362 C CG  . LYS A 434 ? 0.9817 0.9817 0.9817 0.0000 0.0000 0.0000 417 LYS B CG  
3363 C CD  . LYS A 434 ? 0.9817 0.9817 0.9817 0.0000 0.0000 0.0000 417 LYS B CD  
3364 C CE  . LYS A 434 ? 0.9817 0.9817 0.9817 0.0000 0.0000 0.0000 417 LYS B CE  
3365 N NZ  . LYS A 434 ? 0.9817 0.9817 0.9817 0.0000 0.0000 0.0000 417 LYS B NZ  
3366 N N   . ASN A 435 ? 0.9466 0.9466 0.9466 0.0000 0.0000 0.0000 418 ASN B N   
3367 C CA  . ASN A 435 ? 0.9466 0.9466 0.9466 0.0000 0.0000 0.0000 418 ASN B CA  
3368 C C   . ASN A 435 ? 0.9466 0.9466 0.9466 0.0000 0.0000 0.0000 418 ASN B C   
3369 O O   . ASN A 435 ? 0.9466 0.9466 0.9466 0.0000 0.0000 0.0000 418 ASN B O   
3370 C CB  . ASN A 435 ? 0.9466 0.9466 0.9466 0.0000 0.0000 0.0000 418 ASN B CB  
3371 C CG  . ASN A 435 ? 0.9466 0.9466 0.9466 0.0000 0.0000 0.0000 418 ASN B CG  
3372 O OD1 . ASN A 435 ? 0.9466 0.9466 0.9466 0.0000 0.0000 0.0000 418 ASN B OD1 
3373 N ND2 . ASN A 435 ? 0.9466 0.9466 0.9466 0.0000 0.0000 0.0000 418 ASN B ND2 
3374 N N   . PHE A 436 ? 1.0094 1.0094 1.0094 0.0000 0.0000 0.0000 419 PHE B N   
3375 C CA  . PHE A 436 ? 1.0094 1.0094 1.0094 0.0000 0.0000 0.0000 419 PHE B CA  
3376 C C   . PHE A 436 ? 1.0094 1.0094 1.0094 0.0000 0.0000 0.0000 419 PHE B C   
3377 O O   . PHE A 436 ? 1.0094 1.0094 1.0094 0.0000 0.0000 0.0000 419 PHE B O   
3378 C CB  . PHE A 436 ? 1.0094 1.0094 1.0094 0.0000 0.0000 0.0000 419 PHE B CB  
3379 C CG  . PHE A 436 ? 1.0094 1.0094 1.0094 0.0000 0.0000 0.0000 419 PHE B CG  
3380 C CD1 . PHE A 436 ? 1.0094 1.0094 1.0094 0.0000 0.0000 0.0000 419 PHE B CD1 
3381 C CD2 . PHE A 436 ? 1.0094 1.0094 1.0094 0.0000 0.0000 0.0000 419 PHE B CD2 
3382 C CE1 . PHE A 436 ? 1.0094 1.0094 1.0094 0.0000 0.0000 0.0000 419 PHE B CE1 
3383 C CE2 . PHE A 436 ? 1.0094 1.0094 1.0094 0.0000 0.0000 0.0000 419 PHE B CE2 
3384 C CZ  . PHE A 436 ? 1.0094 1.0094 1.0094 0.0000 0.0000 0.0000 419 PHE B CZ  
3385 N N   . THR A 437 ? 0.9911 0.9911 0.9911 0.0000 0.0000 0.0000 420 THR B N   
3386 C CA  . THR A 437 ? 0.9911 0.9911 0.9911 0.0000 0.0000 0.0000 420 THR B CA  
3387 C C   . THR A 437 ? 0.9911 0.9911 0.9911 0.0000 0.0000 0.0000 420 THR B C   
3388 O O   . THR A 437 ? 0.9911 0.9911 0.9911 0.0000 0.0000 0.0000 420 THR B O   
3389 C CB  . THR A 437 ? 0.9911 0.9911 0.9911 0.0000 0.0000 0.0000 420 THR B CB  
3390 O OG1 . THR A 437 ? 0.9911 0.9911 0.9911 0.0000 0.0000 0.0000 420 THR B OG1 
3391 C CG2 . THR A 437 ? 0.9911 0.9911 0.9911 0.0000 0.0000 0.0000 420 THR B CG2 
3392 N N   . GLY A 438 ? 1.0171 1.0171 1.0171 0.0000 0.0000 0.0000 421 GLY B N   
3393 C CA  . GLY A 438 ? 1.0171 1.0171 1.0171 0.0000 0.0000 0.0000 421 GLY B CA  
3394 C C   . GLY A 438 ? 1.0171 1.0171 1.0171 0.0000 0.0000 0.0000 421 GLY B C   
3395 O O   . GLY A 438 ? 1.0171 1.0171 1.0171 0.0000 0.0000 0.0000 421 GLY B O   
3396 N N   . LEU A 439 ? 1.0156 1.0156 1.0156 0.0000 0.0000 0.0000 422 LEU B N   
3397 C CA  . LEU A 439 ? 1.0156 1.0156 1.0156 0.0000 0.0000 0.0000 422 LEU B CA  
3398 C C   . LEU A 439 ? 1.0156 1.0156 1.0156 0.0000 0.0000 0.0000 422 LEU B C   
3399 O O   . LEU A 439 ? 1.0156 1.0156 1.0156 0.0000 0.0000 0.0000 422 LEU B O   
3400 C CB  . LEU A 439 ? 1.0156 1.0156 1.0156 0.0000 0.0000 0.0000 422 LEU B CB  
3401 C CG  . LEU A 439 ? 1.0156 1.0156 1.0156 0.0000 0.0000 0.0000 422 LEU B CG  
3402 C CD1 . LEU A 439 ? 1.0156 1.0156 1.0156 0.0000 0.0000 0.0000 422 LEU B CD1 
3403 C CD2 . LEU A 439 ? 1.0156 1.0156 1.0156 0.0000 0.0000 0.0000 422 LEU B CD2 
3404 N N   . PHE A 440 ? 0.9632 0.9632 0.9632 0.0000 0.0000 0.0000 423 PHE B N   
3405 C CA  . PHE A 440 ? 0.9632 0.9632 0.9632 0.0000 0.0000 0.0000 423 PHE B CA  
3406 C C   . PHE A 440 ? 0.9632 0.9632 0.9632 0.0000 0.0000 0.0000 423 PHE B C   
3407 O O   . PHE A 440 ? 0.9632 0.9632 0.9632 0.0000 0.0000 0.0000 423 PHE B O   
3408 C CB  . PHE A 440 ? 0.9632 0.9632 0.9632 0.0000 0.0000 0.0000 423 PHE B CB  
3409 C CG  . PHE A 440 ? 0.9632 0.9632 0.9632 0.0000 0.0000 0.0000 423 PHE B CG  
3410 C CD1 . PHE A 440 ? 0.9632 0.9632 0.9632 0.0000 0.0000 0.0000 423 PHE B CD1 
3411 C CD2 . PHE A 440 ? 0.9632 0.9632 0.9632 0.0000 0.0000 0.0000 423 PHE B CD2 
3412 C CE1 . PHE A 440 ? 0.9632 0.9632 0.9632 0.0000 0.0000 0.0000 423 PHE B CE1 
3413 C CE2 . PHE A 440 ? 0.9632 0.9632 0.9632 0.0000 0.0000 0.0000 423 PHE B CE2 
3414 C CZ  . PHE A 440 ? 0.9632 0.9632 0.9632 0.0000 0.0000 0.0000 423 PHE B CZ  
3415 N N   . GLU A 441 ? 1.0640 1.0640 1.0640 0.0000 0.0000 0.0000 424 GLU B N   
3416 C CA  . GLU A 441 ? 1.0640 1.0640 1.0640 0.0000 0.0000 0.0000 424 GLU B CA  
3417 C C   . GLU A 441 ? 1.0640 1.0640 1.0640 0.0000 0.0000 0.0000 424 GLU B C   
3418 O O   . GLU A 441 ? 1.0640 1.0640 1.0640 0.0000 0.0000 0.0000 424 GLU B O   
3419 C CB  . GLU A 441 ? 1.0640 1.0640 1.0640 0.0000 0.0000 0.0000 424 GLU B CB  
3420 C CG  . GLU A 441 ? 1.0640 1.0640 1.0640 0.0000 0.0000 0.0000 424 GLU B CG  
3421 C CD  . GLU A 441 ? 1.0640 1.0640 1.0640 0.0000 0.0000 0.0000 424 GLU B CD  
3422 O OE1 . GLU A 441 ? 1.0640 1.0640 1.0640 0.0000 0.0000 0.0000 424 GLU B OE1 
3423 O OE2 . GLU A 441 ? 1.0640 1.0640 1.0640 0.0000 0.0000 0.0000 424 GLU B OE2 
3424 N N   . PHE A 442 ? 1.0617 1.0617 1.0617 0.0000 0.0000 0.0000 425 PHE B N   
3425 C CA  . PHE A 442 ? 1.0617 1.0617 1.0617 0.0000 0.0000 0.0000 425 PHE B CA  
3426 C C   . PHE A 442 ? 1.0617 1.0617 1.0617 0.0000 0.0000 0.0000 425 PHE B C   
3427 O O   . PHE A 442 ? 1.0617 1.0617 1.0617 0.0000 0.0000 0.0000 425 PHE B O   
3428 C CB  . PHE A 442 ? 1.0617 1.0617 1.0617 0.0000 0.0000 0.0000 425 PHE B CB  
3429 C CG  . PHE A 442 ? 1.0617 1.0617 1.0617 0.0000 0.0000 0.0000 425 PHE B CG  
3430 C CD1 . PHE A 442 ? 1.0617 1.0617 1.0617 0.0000 0.0000 0.0000 425 PHE B CD1 
3431 C CD2 . PHE A 442 ? 1.0617 1.0617 1.0617 0.0000 0.0000 0.0000 425 PHE B CD2 
3432 C CE1 . PHE A 442 ? 1.0617 1.0617 1.0617 0.0000 0.0000 0.0000 425 PHE B CE1 
3433 C CE2 . PHE A 442 ? 1.0617 1.0617 1.0617 0.0000 0.0000 0.0000 425 PHE B CE2 
3434 C CZ  . PHE A 442 ? 1.0617 1.0617 1.0617 0.0000 0.0000 0.0000 425 PHE B CZ  
3435 N N   . TYR A 443 ? 0.9642 0.9642 0.9642 0.0000 0.0000 0.0000 426 TYR B N   
3436 C CA  . TYR A 443 ? 0.9642 0.9642 0.9642 0.0000 0.0000 0.0000 426 TYR B CA  
3437 C C   . TYR A 443 ? 0.9642 0.9642 0.9642 0.0000 0.0000 0.0000 426 TYR B C   
3438 O O   . TYR A 443 ? 0.9642 0.9642 0.9642 0.0000 0.0000 0.0000 426 TYR B O   
3439 C CB  . TYR A 443 ? 0.9642 0.9642 0.9642 0.0000 0.0000 0.0000 426 TYR B CB  
3440 C CG  . TYR A 443 ? 0.9642 0.9642 0.9642 0.0000 0.0000 0.0000 426 TYR B CG  
3441 C CD1 . TYR A 443 ? 0.9642 0.9642 0.9642 0.0000 0.0000 0.0000 426 TYR B CD1 
3442 C CD2 . TYR A 443 ? 0.9642 0.9642 0.9642 0.0000 0.0000 0.0000 426 TYR B CD2 
3443 C CE1 . TYR A 443 ? 0.9642 0.9642 0.9642 0.0000 0.0000 0.0000 426 TYR B CE1 
3444 C CE2 . TYR A 443 ? 0.9642 0.9642 0.9642 0.0000 0.0000 0.0000 426 TYR B CE2 
3445 C CZ  . TYR A 443 ? 0.9642 0.9642 0.9642 0.0000 0.0000 0.0000 426 TYR B CZ  
3446 O OH  . TYR A 443 ? 0.9642 0.9642 0.9642 0.0000 0.0000 0.0000 426 TYR B OH  
3447 N N   . LYS A 444 ? 0.9275 0.9275 0.9275 0.0000 0.0000 0.0000 427 LYS B N   
3448 C CA  . LYS A 444 ? 0.9275 0.9275 0.9275 0.0000 0.0000 0.0000 427 LYS B CA  
3449 C C   . LYS A 444 ? 0.9275 0.9275 0.9275 0.0000 0.0000 0.0000 427 LYS B C   
3450 O O   . LYS A 444 ? 0.9275 0.9275 0.9275 0.0000 0.0000 0.0000 427 LYS B O   
3451 C CB  . LYS A 444 ? 0.9275 0.9275 0.9275 0.0000 0.0000 0.0000 427 LYS B CB  
3452 C CG  . LYS A 444 ? 0.9275 0.9275 0.9275 0.0000 0.0000 0.0000 427 LYS B CG  
3453 C CD  . LYS A 444 ? 0.9275 0.9275 0.9275 0.0000 0.0000 0.0000 427 LYS B CD  
3454 C CE  . LYS A 444 ? 0.9275 0.9275 0.9275 0.0000 0.0000 0.0000 427 LYS B CE  
3455 N NZ  . LYS A 444 ? 0.9275 0.9275 0.9275 0.0000 0.0000 0.0000 427 LYS B NZ  
3456 N N   . LEU A 445 ? 0.9150 0.9150 0.9150 0.0000 0.0000 0.0000 428 LEU B N   
3457 C CA  . LEU A 445 ? 0.9150 0.9150 0.9150 0.0000 0.0000 0.0000 428 LEU B CA  
3458 C C   . LEU A 445 ? 0.9150 0.9150 0.9150 0.0000 0.0000 0.0000 428 LEU B C   
3459 O O   . LEU A 445 ? 0.9150 0.9150 0.9150 0.0000 0.0000 0.0000 428 LEU B O   
3460 C CB  . LEU A 445 ? 0.9150 0.9150 0.9150 0.0000 0.0000 0.0000 428 LEU B CB  
3461 C CG  . LEU A 445 ? 0.9150 0.9150 0.9150 0.0000 0.0000 0.0000 428 LEU B CG  
3462 C CD1 . LEU A 445 ? 0.9150 0.9150 0.9150 0.0000 0.0000 0.0000 428 LEU B CD1 
3463 C CD2 . LEU A 445 ? 0.9150 0.9150 0.9150 0.0000 0.0000 0.0000 428 LEU B CD2 
3464 N N   . LEU A 446 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 429 LEU B N   
3465 C CA  . LEU A 446 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 429 LEU B CA  
3466 C C   . LEU A 446 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 429 LEU B C   
3467 O O   . LEU A 446 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 429 LEU B O   
3468 C CB  . LEU A 446 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 429 LEU B CB  
3469 C CG  . LEU A 446 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 429 LEU B CG  
3470 C CD1 . LEU A 446 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 429 LEU B CD1 
3471 C CD2 . LEU A 446 ? 0.9315 0.9315 0.9315 0.0000 0.0000 0.0000 429 LEU B CD2 
3472 N N   . CYS A 447 ? 1.0597 1.0597 1.0597 0.0000 0.0000 0.0000 430 CYS B N   
3473 C CA  . CYS A 447 ? 1.0597 1.0597 1.0597 0.0000 0.0000 0.0000 430 CYS B CA  
3474 C C   . CYS A 447 ? 1.0597 1.0597 1.0597 0.0000 0.0000 0.0000 430 CYS B C   
3475 O O   . CYS A 447 ? 1.0597 1.0597 1.0597 0.0000 0.0000 0.0000 430 CYS B O   
3476 C CB  . CYS A 447 ? 1.0597 1.0597 1.0597 0.0000 0.0000 0.0000 430 CYS B CB  
3477 S SG  . CYS A 447 ? 1.0597 1.0597 1.0597 0.0000 0.0000 0.0000 430 CYS B SG  
3478 N N   . VAL A 448 ? 1.1047 1.1047 1.1047 0.0000 0.0000 0.0000 431 VAL B N   
3479 C CA  . VAL A 448 ? 1.1047 1.1047 1.1047 0.0000 0.0000 0.0000 431 VAL B CA  
3480 C C   . VAL A 448 ? 1.1047 1.1047 1.1047 0.0000 0.0000 0.0000 431 VAL B C   
3481 O O   . VAL A 448 ? 1.1047 1.1047 1.1047 0.0000 0.0000 0.0000 431 VAL B O   
3482 C CB  . VAL A 448 ? 1.1047 1.1047 1.1047 0.0000 0.0000 0.0000 431 VAL B CB  
3483 C CG1 . VAL A 448 ? 1.1047 1.1047 1.1047 0.0000 0.0000 0.0000 431 VAL B CG1 
3484 C CG2 . VAL A 448 ? 1.1047 1.1047 1.1047 0.0000 0.0000 0.0000 431 VAL B CG2 
3485 N N   . ARG A 449 ? 1.1393 1.1393 1.1393 0.0000 0.0000 0.0000 432 ARG B N   
3486 C CA  . ARG A 449 ? 1.1393 1.1393 1.1393 0.0000 0.0000 0.0000 432 ARG B CA  
3487 C C   . ARG A 449 ? 1.1393 1.1393 1.1393 0.0000 0.0000 0.0000 432 ARG B C   
3488 O O   . ARG A 449 ? 1.1393 1.1393 1.1393 0.0000 0.0000 0.0000 432 ARG B O   
3489 C CB  . ARG A 449 ? 1.1393 1.1393 1.1393 0.0000 0.0000 0.0000 432 ARG B CB  
3490 C CG  . ARG A 449 ? 1.1393 1.1393 1.1393 0.0000 0.0000 0.0000 432 ARG B CG  
3491 C CD  . ARG A 449 ? 1.1393 1.1393 1.1393 0.0000 0.0000 0.0000 432 ARG B CD  
3492 N NE  . ARG A 449 ? 1.1393 1.1393 1.1393 0.0000 0.0000 0.0000 432 ARG B NE  
3493 C CZ  . ARG A 449 ? 1.1393 1.1393 1.1393 0.0000 0.0000 0.0000 432 ARG B CZ  
3494 N NH1 . ARG A 449 ? 1.1393 1.1393 1.1393 0.0000 0.0000 0.0000 432 ARG B NH1 
3495 N NH2 . ARG A 449 ? 1.1393 1.1393 1.1393 0.0000 0.0000 0.0000 432 ARG B NH2 
3496 N N   . ASP A 469 ? 1.2940 1.2940 1.2940 0.0000 0.0000 0.0000 452 ASP B N   
3497 C CA  . ASP A 469 ? 1.2940 1.2940 1.2940 0.0000 0.0000 0.0000 452 ASP B CA  
3498 C C   . ASP A 469 ? 1.2940 1.2940 1.2940 0.0000 0.0000 0.0000 452 ASP B C   
3499 O O   . ASP A 469 ? 1.2940 1.2940 1.2940 0.0000 0.0000 0.0000 452 ASP B O   
3500 C CB  . ASP A 469 ? 1.2940 1.2940 1.2940 0.0000 0.0000 0.0000 452 ASP B CB  
3501 C CG  . ASP A 469 ? 1.2940 1.2940 1.2940 0.0000 0.0000 0.0000 452 ASP B CG  
3502 O OD1 . ASP A 469 ? 1.2940 1.2940 1.2940 0.0000 0.0000 0.0000 452 ASP B OD1 
3503 O OD2 . ASP A 469 ? 1.2940 1.2940 1.2940 0.0000 0.0000 0.0000 452 ASP B OD2 
3504 N N   . LEU A 470 ? 1.1337 1.1337 1.1337 0.0000 0.0000 0.0000 453 LEU B N   
3505 C CA  . LEU A 470 ? 1.1337 1.1337 1.1337 0.0000 0.0000 0.0000 453 LEU B CA  
3506 C C   . LEU A 470 ? 1.1337 1.1337 1.1337 0.0000 0.0000 0.0000 453 LEU B C   
3507 O O   . LEU A 470 ? 1.1337 1.1337 1.1337 0.0000 0.0000 0.0000 453 LEU B O   
3508 C CB  . LEU A 470 ? 1.1337 1.1337 1.1337 0.0000 0.0000 0.0000 453 LEU B CB  
3509 C CG  . LEU A 470 ? 1.1337 1.1337 1.1337 0.0000 0.0000 0.0000 453 LEU B CG  
3510 C CD1 . LEU A 470 ? 1.1337 1.1337 1.1337 0.0000 0.0000 0.0000 453 LEU B CD1 
3511 C CD2 . LEU A 470 ? 1.1337 1.1337 1.1337 0.0000 0.0000 0.0000 453 LEU B CD2 
3512 N N   . CYS A 471 ? 1.0850 1.0850 1.0850 0.0000 0.0000 0.0000 454 CYS B N   
3513 C CA  . CYS A 471 ? 1.0850 1.0850 1.0850 0.0000 0.0000 0.0000 454 CYS B CA  
3514 C C   . CYS A 471 ? 1.0850 1.0850 1.0850 0.0000 0.0000 0.0000 454 CYS B C   
3515 O O   . CYS A 471 ? 1.0850 1.0850 1.0850 0.0000 0.0000 0.0000 454 CYS B O   
3516 C CB  . CYS A 471 ? 1.0850 1.0850 1.0850 0.0000 0.0000 0.0000 454 CYS B CB  
3517 S SG  . CYS A 471 ? 1.0850 1.0850 1.0850 0.0000 0.0000 0.0000 454 CYS B SG  
3518 N N   . ILE A 472 ? 0.9276 0.9276 0.9276 0.0000 0.0000 0.0000 455 ILE B N   
3519 C CA  . ILE A 472 ? 0.9276 0.9276 0.9276 0.0000 0.0000 0.0000 455 ILE B CA  
3520 C C   . ILE A 472 ? 0.9276 0.9276 0.9276 0.0000 0.0000 0.0000 455 ILE B C   
3521 O O   . ILE A 472 ? 0.9276 0.9276 0.9276 0.0000 0.0000 0.0000 455 ILE B O   
3522 C CB  . ILE A 472 ? 0.9276 0.9276 0.9276 0.0000 0.0000 0.0000 455 ILE B CB  
3523 C CG1 . ILE A 472 ? 0.9276 0.9276 0.9276 0.0000 0.0000 0.0000 455 ILE B CG1 
3524 C CG2 . ILE A 472 ? 0.9276 0.9276 0.9276 0.0000 0.0000 0.0000 455 ILE B CG2 
3525 C CD1 . ILE A 472 ? 0.9276 0.9276 0.9276 0.0000 0.0000 0.0000 455 ILE B CD1 
3526 N N   . LYS A 473 ? 0.9218 0.9218 0.9218 0.0000 0.0000 0.0000 456 LYS B N   
3527 C CA  . LYS A 473 ? 0.9218 0.9218 0.9218 0.0000 0.0000 0.0000 456 LYS B CA  
3528 C C   . LYS A 473 ? 0.9218 0.9218 0.9218 0.0000 0.0000 0.0000 456 LYS B C   
3529 O O   . LYS A 473 ? 0.9218 0.9218 0.9218 0.0000 0.0000 0.0000 456 LYS B O   
3530 C CB  . LYS A 473 ? 0.9218 0.9218 0.9218 0.0000 0.0000 0.0000 456 LYS B CB  
3531 C CG  . LYS A 473 ? 0.9218 0.9218 0.9218 0.0000 0.0000 0.0000 456 LYS B CG  
3532 C CD  . LYS A 473 ? 0.9218 0.9218 0.9218 0.0000 0.0000 0.0000 456 LYS B CD  
3533 C CE  . LYS A 473 ? 0.9218 0.9218 0.9218 0.0000 0.0000 0.0000 456 LYS B CE  
3534 N NZ  . LYS A 473 ? 0.9218 0.9218 0.9218 0.0000 0.0000 0.0000 456 LYS B NZ  
3535 N N   . VAL A 474 ? 0.9132 0.9132 0.9132 0.0000 0.0000 0.0000 457 VAL B N   
3536 C CA  . VAL A 474 ? 0.9132 0.9132 0.9132 0.0000 0.0000 0.0000 457 VAL B CA  
3537 C C   . VAL A 474 ? 0.9132 0.9132 0.9132 0.0000 0.0000 0.0000 457 VAL B C   
3538 O O   . VAL A 474 ? 0.9132 0.9132 0.9132 0.0000 0.0000 0.0000 457 VAL B O   
3539 C CB  . VAL A 474 ? 0.9132 0.9132 0.9132 0.0000 0.0000 0.0000 457 VAL B CB  
3540 C CG1 . VAL A 474 ? 0.9132 0.9132 0.9132 0.0000 0.0000 0.0000 457 VAL B CG1 
3541 C CG2 . VAL A 474 ? 0.9132 0.9132 0.9132 0.0000 0.0000 0.0000 457 VAL B CG2 
3542 N N   . ASN A 475 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 458 ASN B N   
3543 C CA  . ASN A 475 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 458 ASN B CA  
3544 C C   . ASN A 475 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 458 ASN B C   
3545 O O   . ASN A 475 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 458 ASN B O   
3546 C CB  . ASN A 475 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 458 ASN B CB  
3547 C CG  . ASN A 475 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 458 ASN B CG  
3548 O OD1 . ASN A 475 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 458 ASN B OD1 
3549 N ND2 . ASN A 475 ? 0.9860 0.9860 0.9860 0.0000 0.0000 0.0000 458 ASN B ND2 
3550 N N   . ASN A 476 ? 0.9712 0.9712 0.9712 0.0000 0.0000 0.0000 459 ASN B N   
3551 C CA  . ASN A 476 ? 0.9712 0.9712 0.9712 0.0000 0.0000 0.0000 459 ASN B CA  
3552 C C   . ASN A 476 ? 0.9712 0.9712 0.9712 0.0000 0.0000 0.0000 459 ASN B C   
3553 O O   . ASN A 476 ? 0.9712 0.9712 0.9712 0.0000 0.0000 0.0000 459 ASN B O   
3554 C CB  . ASN A 476 ? 0.9712 0.9712 0.9712 0.0000 0.0000 0.0000 459 ASN B CB  
3555 C CG  . ASN A 476 ? 0.9712 0.9712 0.9712 0.0000 0.0000 0.0000 459 ASN B CG  
3556 O OD1 . ASN A 476 ? 0.9712 0.9712 0.9712 0.0000 0.0000 0.0000 459 ASN B OD1 
3557 N ND2 . ASN A 476 ? 0.9712 0.9712 0.9712 0.0000 0.0000 0.0000 459 ASN B ND2 
3558 N N   . TRP A 477 ? 0.9594 0.9594 0.9594 0.0000 0.0000 0.0000 460 TRP B N   
3559 C CA  . TRP A 477 ? 0.9594 0.9594 0.9594 0.0000 0.0000 0.0000 460 TRP B CA  
3560 C C   . TRP A 477 ? 0.9594 0.9594 0.9594 0.0000 0.0000 0.0000 460 TRP B C   
3561 O O   . TRP A 477 ? 0.9594 0.9594 0.9594 0.0000 0.0000 0.0000 460 TRP B O   
3562 C CB  . TRP A 477 ? 0.9594 0.9594 0.9594 0.0000 0.0000 0.0000 460 TRP B CB  
3563 C CG  . TRP A 477 ? 0.9594 0.9594 0.9594 0.0000 0.0000 0.0000 460 TRP B CG  
3564 C CD1 . TRP A 477 ? 0.9594 0.9594 0.9594 0.0000 0.0000 0.0000 460 TRP B CD1 
3565 C CD2 . TRP A 477 ? 0.9594 0.9594 0.9594 0.0000 0.0000 0.0000 460 TRP B CD2 
3566 N NE1 . TRP A 477 ? 0.9594 0.9594 0.9594 0.0000 0.0000 0.0000 460 TRP B NE1 
3567 C CE2 . TRP A 477 ? 0.9594 0.9594 0.9594 0.0000 0.0000 0.0000 460 TRP B CE2 
3568 C CE3 . TRP A 477 ? 0.9594 0.9594 0.9594 0.0000 0.0000 0.0000 460 TRP B CE3 
3569 C CZ2 . TRP A 477 ? 0.9594 0.9594 0.9594 0.0000 0.0000 0.0000 460 TRP B CZ2 
3570 C CZ3 . TRP A 477 ? 0.9594 0.9594 0.9594 0.0000 0.0000 0.0000 460 TRP B CZ3 
3571 C CH2 . TRP A 477 ? 0.9594 0.9594 0.9594 0.0000 0.0000 0.0000 460 TRP B CH2 
3572 N N   . ASP A 478 ? 0.9337 0.9337 0.9337 0.0000 0.0000 0.0000 461 ASP B N   
3573 C CA  . ASP A 478 ? 0.9337 0.9337 0.9337 0.0000 0.0000 0.0000 461 ASP B CA  
3574 C C   . ASP A 478 ? 0.9337 0.9337 0.9337 0.0000 0.0000 0.0000 461 ASP B C   
3575 O O   . ASP A 478 ? 0.9337 0.9337 0.9337 0.0000 0.0000 0.0000 461 ASP B O   
3576 C CB  . ASP A 478 ? 0.9337 0.9337 0.9337 0.0000 0.0000 0.0000 461 ASP B CB  
3577 C CG  . ASP A 478 ? 0.9337 0.9337 0.9337 0.0000 0.0000 0.0000 461 ASP B CG  
3578 O OD1 . ASP A 478 ? 0.9337 0.9337 0.9337 0.0000 0.0000 0.0000 461 ASP B OD1 
3579 O OD2 . ASP A 478 ? 0.9337 0.9337 0.9337 0.0000 0.0000 0.0000 461 ASP B OD2 
3580 N N   . LEU A 479 ? 0.8882 0.8882 0.8882 0.0000 0.0000 0.0000 462 LEU B N   
3581 C CA  . LEU A 479 ? 0.8882 0.8882 0.8882 0.0000 0.0000 0.0000 462 LEU B CA  
3582 C C   . LEU A 479 ? 0.8882 0.8882 0.8882 0.0000 0.0000 0.0000 462 LEU B C   
3583 O O   . LEU A 479 ? 0.8882 0.8882 0.8882 0.0000 0.0000 0.0000 462 LEU B O   
3584 C CB  . LEU A 479 ? 0.8882 0.8882 0.8882 0.0000 0.0000 0.0000 462 LEU B CB  
3585 C CG  . LEU A 479 ? 0.8882 0.8882 0.8882 0.0000 0.0000 0.0000 462 LEU B CG  
3586 C CD1 . LEU A 479 ? 0.8882 0.8882 0.8882 0.0000 0.0000 0.0000 462 LEU B CD1 
3587 C CD2 . LEU A 479 ? 0.8882 0.8882 0.8882 0.0000 0.0000 0.0000 462 LEU B CD2 
3588 N N   . PHE A 480 ? 0.9124 0.9124 0.9124 0.0000 0.0000 0.0000 463 PHE B N   
3589 C CA  . PHE A 480 ? 0.9124 0.9124 0.9124 0.0000 0.0000 0.0000 463 PHE B CA  
3590 C C   . PHE A 480 ? 0.9124 0.9124 0.9124 0.0000 0.0000 0.0000 463 PHE B C   
3591 O O   . PHE A 480 ? 0.9124 0.9124 0.9124 0.0000 0.0000 0.0000 463 PHE B O   
3592 C CB  . PHE A 480 ? 0.9124 0.9124 0.9124 0.0000 0.0000 0.0000 463 PHE B CB  
3593 C CG  . PHE A 480 ? 0.9124 0.9124 0.9124 0.0000 0.0000 0.0000 463 PHE B CG  
3594 C CD1 . PHE A 480 ? 0.9124 0.9124 0.9124 0.0000 0.0000 0.0000 463 PHE B CD1 
3595 C CD2 . PHE A 480 ? 0.9124 0.9124 0.9124 0.0000 0.0000 0.0000 463 PHE B CD2 
3596 C CE1 . PHE A 480 ? 0.9124 0.9124 0.9124 0.0000 0.0000 0.0000 463 PHE B CE1 
3597 C CE2 . PHE A 480 ? 0.9124 0.9124 0.9124 0.0000 0.0000 0.0000 463 PHE B CE2 
3598 C CZ  . PHE A 480 ? 0.9124 0.9124 0.9124 0.0000 0.0000 0.0000 463 PHE B CZ  
3599 N N   . PHE A 481 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 464 PHE B N   
3600 C CA  . PHE A 481 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 464 PHE B CA  
3601 C C   . PHE A 481 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 464 PHE B C   
3602 O O   . PHE A 481 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 464 PHE B O   
3603 C CB  . PHE A 481 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 464 PHE B CB  
3604 C CG  . PHE A 481 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 464 PHE B CG  
3605 C CD1 . PHE A 481 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 464 PHE B CD1 
3606 C CD2 . PHE A 481 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 464 PHE B CD2 
3607 C CE1 . PHE A 481 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 464 PHE B CE1 
3608 C CE2 . PHE A 481 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 464 PHE B CE2 
3609 C CZ  . PHE A 481 ? 0.9089 0.9089 0.9089 0.0000 0.0000 0.0000 464 PHE B CZ  
3610 N N   . SER A 482 ? 0.9593 0.9593 0.9593 0.0000 0.0000 0.0000 465 SER B N   
3611 C CA  . SER A 482 ? 0.9593 0.9593 0.9593 0.0000 0.0000 0.0000 465 SER B CA  
3612 C C   . SER A 482 ? 0.9593 0.9593 0.9593 0.0000 0.0000 0.0000 465 SER B C   
3613 O O   . SER A 482 ? 0.9593 0.9593 0.9593 0.0000 0.0000 0.0000 465 SER B O   
3614 C CB  . SER A 482 ? 0.9593 0.9593 0.9593 0.0000 0.0000 0.0000 465 SER B CB  
3615 O OG  . SER A 482 ? 0.9593 0.9593 0.9593 0.0000 0.0000 0.0000 465 SER B OG  
3616 N N   . PRO A 483 ? 0.9525 0.9525 0.9525 0.0000 0.0000 0.0000 466 PRO B N   
3617 C CA  . PRO A 483 ? 0.9525 0.9525 0.9525 0.0000 0.0000 0.0000 466 PRO B CA  
3618 C C   . PRO A 483 ? 0.9525 0.9525 0.9525 0.0000 0.0000 0.0000 466 PRO B C   
3619 O O   . PRO A 483 ? 0.9525 0.9525 0.9525 0.0000 0.0000 0.0000 466 PRO B O   
3620 C CB  . PRO A 483 ? 0.9525 0.9525 0.9525 0.0000 0.0000 0.0000 466 PRO B CB  
3621 C CG  . PRO A 483 ? 0.9525 0.9525 0.9525 0.0000 0.0000 0.0000 466 PRO B CG  
3622 C CD  . PRO A 483 ? 0.9525 0.9525 0.9525 0.0000 0.0000 0.0000 466 PRO B CD  
3623 N N   . SER A 484 ? 1.0092 1.0092 1.0092 0.0000 0.0000 0.0000 467 SER B N   
3624 C CA  . SER A 484 ? 1.0092 1.0092 1.0092 0.0000 0.0000 0.0000 467 SER B CA  
3625 C C   . SER A 484 ? 1.0092 1.0092 1.0092 0.0000 0.0000 0.0000 467 SER B C   
3626 O O   . SER A 484 ? 1.0092 1.0092 1.0092 0.0000 0.0000 0.0000 467 SER B O   
3627 C CB  . SER A 484 ? 1.0092 1.0092 1.0092 0.0000 0.0000 0.0000 467 SER B CB  
3628 O OG  . SER A 484 ? 1.0092 1.0092 1.0092 0.0000 0.0000 0.0000 467 SER B OG  
3629 N N   . GLU A 485 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 468 GLU B N   
3630 C CA  . GLU A 485 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 468 GLU B CA  
3631 C C   . GLU A 485 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 468 GLU B C   
3632 O O   . GLU A 485 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 468 GLU B O   
3633 C CB  . GLU A 485 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 468 GLU B CB  
3634 C CG  . GLU A 485 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 468 GLU B CG  
3635 C CD  . GLU A 485 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 468 GLU B CD  
3636 O OE1 . GLU A 485 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 468 GLU B OE1 
3637 O OE2 . GLU A 485 ? 1.0424 1.0424 1.0424 0.0000 0.0000 0.0000 468 GLU B OE2 
3638 N N   . ASP A 486 ? 1.0471 1.0471 1.0471 0.0000 0.0000 0.0000 469 ASP B N   
3639 C CA  . ASP A 486 ? 1.0471 1.0471 1.0471 0.0000 0.0000 0.0000 469 ASP B CA  
3640 C C   . ASP A 486 ? 1.0471 1.0471 1.0471 0.0000 0.0000 0.0000 469 ASP B C   
3641 O O   . ASP A 486 ? 1.0471 1.0471 1.0471 0.0000 0.0000 0.0000 469 ASP B O   
3642 C CB  . ASP A 486 ? 1.0471 1.0471 1.0471 0.0000 0.0000 0.0000 469 ASP B CB  
3643 C CG  . ASP A 486 ? 1.0471 1.0471 1.0471 0.0000 0.0000 0.0000 469 ASP B CG  
3644 O OD1 . ASP A 486 ? 1.0471 1.0471 1.0471 0.0000 0.0000 0.0000 469 ASP B OD1 
3645 O OD2 . ASP A 486 ? 1.0471 1.0471 1.0471 0.0000 0.0000 0.0000 469 ASP B OD2 
3646 N N   . ASN A 487 ? 1.0267 1.0267 1.0267 0.0000 0.0000 0.0000 470 ASN B N   
3647 C CA  . ASN A 487 ? 1.0267 1.0267 1.0267 0.0000 0.0000 0.0000 470 ASN B CA  
3648 C C   . ASN A 487 ? 1.0267 1.0267 1.0267 0.0000 0.0000 0.0000 470 ASN B C   
3649 O O   . ASN A 487 ? 1.0267 1.0267 1.0267 0.0000 0.0000 0.0000 470 ASN B O   
3650 C CB  . ASN A 487 ? 1.0267 1.0267 1.0267 0.0000 0.0000 0.0000 470 ASN B CB  
3651 C CG  . ASN A 487 ? 1.0267 1.0267 1.0267 0.0000 0.0000 0.0000 470 ASN B CG  
3652 O OD1 . ASN A 487 ? 1.0267 1.0267 1.0267 0.0000 0.0000 0.0000 470 ASN B OD1 
3653 N ND2 . ASN A 487 ? 1.0267 1.0267 1.0267 0.0000 0.0000 0.0000 470 ASN B ND2 
3654 N N   . PHE A 488 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 471 PHE B N   
3655 C CA  . PHE A 488 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 471 PHE B CA  
3656 C C   . PHE A 488 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 471 PHE B C   
3657 O O   . PHE A 488 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 471 PHE B O   
3658 C CB  . PHE A 488 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 471 PHE B CB  
3659 C CG  . PHE A 488 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 471 PHE B CG  
3660 C CD1 . PHE A 488 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 471 PHE B CD1 
3661 C CD2 . PHE A 488 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 471 PHE B CD2 
3662 C CE1 . PHE A 488 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 471 PHE B CE1 
3663 C CE2 . PHE A 488 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 471 PHE B CE2 
3664 C CZ  . PHE A 488 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 471 PHE B CZ  
3665 N N   . THR A 489 ? 1.0271 1.0271 1.0271 0.0000 0.0000 0.0000 472 THR B N   
3666 C CA  . THR A 489 ? 1.0271 1.0271 1.0271 0.0000 0.0000 0.0000 472 THR B CA  
3667 C C   . THR A 489 ? 1.0271 1.0271 1.0271 0.0000 0.0000 0.0000 472 THR B C   
3668 O O   . THR A 489 ? 1.0271 1.0271 1.0271 0.0000 0.0000 0.0000 472 THR B O   
3669 C CB  . THR A 489 ? 1.0271 1.0271 1.0271 0.0000 0.0000 0.0000 472 THR B CB  
3670 O OG1 . THR A 489 ? 1.0271 1.0271 1.0271 0.0000 0.0000 0.0000 472 THR B OG1 
3671 C CG2 . THR A 489 ? 1.0271 1.0271 1.0271 0.0000 0.0000 0.0000 472 THR B CG2 
3672 N N   . ASN A 490 ? 1.0263 1.0263 1.0263 0.0000 0.0000 0.0000 473 ASN B N   
3673 C CA  . ASN A 490 ? 1.0263 1.0263 1.0263 0.0000 0.0000 0.0000 473 ASN B CA  
3674 C C   . ASN A 490 ? 1.0263 1.0263 1.0263 0.0000 0.0000 0.0000 473 ASN B C   
3675 O O   . ASN A 490 ? 1.0263 1.0263 1.0263 0.0000 0.0000 0.0000 473 ASN B O   
3676 C CB  . ASN A 490 ? 1.0263 1.0263 1.0263 0.0000 0.0000 0.0000 473 ASN B CB  
3677 C CG  . ASN A 490 ? 1.0263 1.0263 1.0263 0.0000 0.0000 0.0000 473 ASN B CG  
3678 O OD1 . ASN A 490 ? 1.0263 1.0263 1.0263 0.0000 0.0000 0.0000 473 ASN B OD1 
3679 N ND2 . ASN A 490 ? 1.0263 1.0263 1.0263 0.0000 0.0000 0.0000 473 ASN B ND2 
3680 N N   . ASP A 491 ? 1.0712 1.0712 1.0712 0.0000 0.0000 0.0000 474 ASP B N   
3681 C CA  . ASP A 491 ? 1.0712 1.0712 1.0712 0.0000 0.0000 0.0000 474 ASP B CA  
3682 C C   . ASP A 491 ? 1.0712 1.0712 1.0712 0.0000 0.0000 0.0000 474 ASP B C   
3683 O O   . ASP A 491 ? 1.0712 1.0712 1.0712 0.0000 0.0000 0.0000 474 ASP B O   
3684 C CB  . ASP A 491 ? 1.0712 1.0712 1.0712 0.0000 0.0000 0.0000 474 ASP B CB  
3685 C CG  . ASP A 491 ? 1.0712 1.0712 1.0712 0.0000 0.0000 0.0000 474 ASP B CG  
3686 O OD1 . ASP A 491 ? 1.0712 1.0712 1.0712 0.0000 0.0000 0.0000 474 ASP B OD1 
3687 O OD2 . ASP A 491 ? 1.0712 1.0712 1.0712 0.0000 0.0000 0.0000 474 ASP B OD2 
3688 N N   . LEU A 492 ? 1.0034 1.0034 1.0034 0.0000 0.0000 0.0000 475 LEU B N   
3689 C CA  . LEU A 492 ? 1.0034 1.0034 1.0034 0.0000 0.0000 0.0000 475 LEU B CA  
3690 C C   . LEU A 492 ? 1.0034 1.0034 1.0034 0.0000 0.0000 0.0000 475 LEU B C   
3691 O O   . LEU A 492 ? 1.0034 1.0034 1.0034 0.0000 0.0000 0.0000 475 LEU B O   
3692 C CB  . LEU A 492 ? 1.0034 1.0034 1.0034 0.0000 0.0000 0.0000 475 LEU B CB  
3693 C CG  . LEU A 492 ? 1.0034 1.0034 1.0034 0.0000 0.0000 0.0000 475 LEU B CG  
3694 C CD1 . LEU A 492 ? 1.0034 1.0034 1.0034 0.0000 0.0000 0.0000 475 LEU B CD1 
3695 C CD2 . LEU A 492 ? 1.0034 1.0034 1.0034 0.0000 0.0000 0.0000 475 LEU B CD2 
3696 N N   . ASN A 493 ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 476 ASN B N   
3697 C CA  . ASN A 493 ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 476 ASN B CA  
3698 C C   . ASN A 493 ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 476 ASN B C   
3699 O O   . ASN A 493 ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 476 ASN B O   
3700 C CB  . ASN A 493 ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 476 ASN B CB  
3701 C CG  . ASN A 493 ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 476 ASN B CG  
3702 O OD1 . ASN A 493 ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 476 ASN B OD1 
3703 N ND2 . ASN A 493 ? 1.0547 1.0547 1.0547 0.0000 0.0000 0.0000 476 ASN B ND2 
3704 N N   . LYS A 494 ? 1.0792 1.0792 1.0792 0.0000 0.0000 0.0000 477 LYS B N   
3705 C CA  . LYS A 494 ? 1.0792 1.0792 1.0792 0.0000 0.0000 0.0000 477 LYS B CA  
3706 C C   . LYS A 494 ? 1.0792 1.0792 1.0792 0.0000 0.0000 0.0000 477 LYS B C   
3707 O O   . LYS A 494 ? 1.0792 1.0792 1.0792 0.0000 0.0000 0.0000 477 LYS B O   
3708 C CB  . LYS A 494 ? 1.0792 1.0792 1.0792 0.0000 0.0000 0.0000 477 LYS B CB  
3709 C CG  . LYS A 494 ? 1.0792 1.0792 1.0792 0.0000 0.0000 0.0000 477 LYS B CG  
3710 C CD  . LYS A 494 ? 1.0792 1.0792 1.0792 0.0000 0.0000 0.0000 477 LYS B CD  
3711 C CE  . LYS A 494 ? 1.0792 1.0792 1.0792 0.0000 0.0000 0.0000 477 LYS B CE  
3712 N NZ  . LYS A 494 ? 1.0792 1.0792 1.0792 0.0000 0.0000 0.0000 477 LYS B NZ  
3713 N N   . GLY A 495 ? 1.1044 1.1044 1.1044 0.0000 0.0000 0.0000 478 GLY B N   
3714 C CA  . GLY A 495 ? 1.1044 1.1044 1.1044 0.0000 0.0000 0.0000 478 GLY B CA  
3715 C C   . GLY A 495 ? 1.1044 1.1044 1.1044 0.0000 0.0000 0.0000 478 GLY B C   
3716 O O   . GLY A 495 ? 1.1044 1.1044 1.1044 0.0000 0.0000 0.0000 478 GLY B O   
3717 N N   . GLU A 496 ? 1.0611 1.0611 1.0611 0.0000 0.0000 0.0000 479 GLU B N   
3718 C CA  . GLU A 496 ? 1.0611 1.0611 1.0611 0.0000 0.0000 0.0000 479 GLU B CA  
3719 C C   . GLU A 496 ? 1.0611 1.0611 1.0611 0.0000 0.0000 0.0000 479 GLU B C   
3720 O O   . GLU A 496 ? 1.0611 1.0611 1.0611 0.0000 0.0000 0.0000 479 GLU B O   
3721 C CB  . GLU A 496 ? 1.0611 1.0611 1.0611 0.0000 0.0000 0.0000 479 GLU B CB  
3722 C CG  . GLU A 496 ? 1.0611 1.0611 1.0611 0.0000 0.0000 0.0000 479 GLU B CG  
3723 C CD  . GLU A 496 ? 1.0611 1.0611 1.0611 0.0000 0.0000 0.0000 479 GLU B CD  
3724 O OE1 . GLU A 496 ? 1.0611 1.0611 1.0611 0.0000 0.0000 0.0000 479 GLU B OE1 
3725 O OE2 . GLU A 496 ? 1.0611 1.0611 1.0611 0.0000 0.0000 0.0000 479 GLU B OE2 
3726 N N   . GLU A 497 ? 1.0785 1.0785 1.0785 0.0000 0.0000 0.0000 480 GLU B N   
3727 C CA  . GLU A 497 ? 1.0785 1.0785 1.0785 0.0000 0.0000 0.0000 480 GLU B CA  
3728 C C   . GLU A 497 ? 1.0785 1.0785 1.0785 0.0000 0.0000 0.0000 480 GLU B C   
3729 O O   . GLU A 497 ? 1.0785 1.0785 1.0785 0.0000 0.0000 0.0000 480 GLU B O   
3730 C CB  . GLU A 497 ? 1.0785 1.0785 1.0785 0.0000 0.0000 0.0000 480 GLU B CB  
3731 C CG  . GLU A 497 ? 1.0785 1.0785 1.0785 0.0000 0.0000 0.0000 480 GLU B CG  
3732 C CD  . GLU A 497 ? 1.0785 1.0785 1.0785 0.0000 0.0000 0.0000 480 GLU B CD  
3733 O OE1 . GLU A 497 ? 1.0785 1.0785 1.0785 0.0000 0.0000 0.0000 480 GLU B OE1 
3734 O OE2 . GLU A 497 ? 1.0785 1.0785 1.0785 0.0000 0.0000 0.0000 480 GLU B OE2 
3735 N N   . ILE A 498 ? 1.0072 1.0072 1.0072 0.0000 0.0000 0.0000 481 ILE B N   
3736 C CA  . ILE A 498 ? 1.0072 1.0072 1.0072 0.0000 0.0000 0.0000 481 ILE B CA  
3737 C C   . ILE A 498 ? 1.0072 1.0072 1.0072 0.0000 0.0000 0.0000 481 ILE B C   
3738 O O   . ILE A 498 ? 1.0072 1.0072 1.0072 0.0000 0.0000 0.0000 481 ILE B O   
3739 C CB  . ILE A 498 ? 1.0072 1.0072 1.0072 0.0000 0.0000 0.0000 481 ILE B CB  
3740 C CG1 . ILE A 498 ? 1.0072 1.0072 1.0072 0.0000 0.0000 0.0000 481 ILE B CG1 
3741 C CG2 . ILE A 498 ? 1.0072 1.0072 1.0072 0.0000 0.0000 0.0000 481 ILE B CG2 
3742 C CD1 . ILE A 498 ? 1.0072 1.0072 1.0072 0.0000 0.0000 0.0000 481 ILE B CD1 
3743 N N   . THR A 499 ? 1.0982 1.0982 1.0982 0.0000 0.0000 0.0000 482 THR B N   
3744 C CA  . THR A 499 ? 1.0982 1.0982 1.0982 0.0000 0.0000 0.0000 482 THR B CA  
3745 C C   . THR A 499 ? 1.0982 1.0982 1.0982 0.0000 0.0000 0.0000 482 THR B C   
3746 O O   . THR A 499 ? 1.0982 1.0982 1.0982 0.0000 0.0000 0.0000 482 THR B O   
3747 C CB  . THR A 499 ? 1.0982 1.0982 1.0982 0.0000 0.0000 0.0000 482 THR B CB  
3748 O OG1 . THR A 499 ? 1.0982 1.0982 1.0982 0.0000 0.0000 0.0000 482 THR B OG1 
3749 C CG2 . THR A 499 ? 1.0982 1.0982 1.0982 0.0000 0.0000 0.0000 482 THR B CG2 
3750 N N   . SER A 500 ? 1.0904 1.0904 1.0904 0.0000 0.0000 0.0000 483 SER B N   
3751 C CA  . SER A 500 ? 1.0904 1.0904 1.0904 0.0000 0.0000 0.0000 483 SER B CA  
3752 C C   . SER A 500 ? 1.0904 1.0904 1.0904 0.0000 0.0000 0.0000 483 SER B C   
3753 O O   . SER A 500 ? 1.0904 1.0904 1.0904 0.0000 0.0000 0.0000 483 SER B O   
3754 C CB  . SER A 500 ? 1.0904 1.0904 1.0904 0.0000 0.0000 0.0000 483 SER B CB  
3755 O OG  . SER A 500 ? 1.0904 1.0904 1.0904 0.0000 0.0000 0.0000 483 SER B OG  
3756 N N   . ASP A 501 ? 1.1883 1.1883 1.1883 0.0000 0.0000 0.0000 484 ASP B N   
3757 C CA  . ASP A 501 ? 1.1883 1.1883 1.1883 0.0000 0.0000 0.0000 484 ASP B CA  
3758 C C   . ASP A 501 ? 1.1883 1.1883 1.1883 0.0000 0.0000 0.0000 484 ASP B C   
3759 O O   . ASP A 501 ? 1.1883 1.1883 1.1883 0.0000 0.0000 0.0000 484 ASP B O   
3760 C CB  . ASP A 501 ? 1.1883 1.1883 1.1883 0.0000 0.0000 0.0000 484 ASP B CB  
3761 C CG  . ASP A 501 ? 1.1883 1.1883 1.1883 0.0000 0.0000 0.0000 484 ASP B CG  
3762 O OD1 . ASP A 501 ? 1.1883 1.1883 1.1883 0.0000 0.0000 0.0000 484 ASP B OD1 
3763 O OD2 . ASP A 501 ? 1.1883 1.1883 1.1883 0.0000 0.0000 0.0000 484 ASP B OD2 
3779 N N   . SER A 512 ? 1.3409 1.3409 1.3409 0.0000 0.0000 0.0000 495 SER B N   
3780 C CA  . SER A 512 ? 1.3409 1.3409 1.3409 0.0000 0.0000 0.0000 495 SER B CA  
3781 C C   . SER A 512 ? 1.3409 1.3409 1.3409 0.0000 0.0000 0.0000 495 SER B C   
3782 O O   . SER A 512 ? 1.3409 1.3409 1.3409 0.0000 0.0000 0.0000 495 SER B O   
3783 C CB  . SER A 512 ? 1.3409 1.3409 1.3409 0.0000 0.0000 0.0000 495 SER B CB  
3784 O OG  . SER A 512 ? 1.3409 1.3409 1.3409 0.0000 0.0000 0.0000 495 SER B OG  
3785 N N   . LEU A 513 ? 1.3212 1.3212 1.3212 0.0000 0.0000 0.0000 496 LEU B N   
3786 C CA  . LEU A 513 ? 1.3212 1.3212 1.3212 0.0000 0.0000 0.0000 496 LEU B CA  
3787 C C   . LEU A 513 ? 1.3212 1.3212 1.3212 0.0000 0.0000 0.0000 496 LEU B C   
3788 O O   . LEU A 513 ? 1.3212 1.3212 1.3212 0.0000 0.0000 0.0000 496 LEU B O   
3789 C CB  . LEU A 513 ? 1.3212 1.3212 1.3212 0.0000 0.0000 0.0000 496 LEU B CB  
3790 C CG  . LEU A 513 ? 1.3212 1.3212 1.3212 0.0000 0.0000 0.0000 496 LEU B CG  
3791 C CD1 . LEU A 513 ? 1.3212 1.3212 1.3212 0.0000 0.0000 0.0000 496 LEU B CD1 
3792 C CD2 . LEU A 513 ? 1.3212 1.3212 1.3212 0.0000 0.0000 0.0000 496 LEU B CD2 
3793 N N   . ASP A 514 ? 1.3486 1.3486 1.3486 0.0000 0.0000 0.0000 497 ASP B N   
3794 C CA  . ASP A 514 ? 1.3486 1.3486 1.3486 0.0000 0.0000 0.0000 497 ASP B CA  
3795 C C   . ASP A 514 ? 1.3486 1.3486 1.3486 0.0000 0.0000 0.0000 497 ASP B C   
3796 O O   . ASP A 514 ? 1.3486 1.3486 1.3486 0.0000 0.0000 0.0000 497 ASP B O   
3797 C CB  . ASP A 514 ? 1.3486 1.3486 1.3486 0.0000 0.0000 0.0000 497 ASP B CB  
3798 C CG  . ASP A 514 ? 1.3486 1.3486 1.3486 0.0000 0.0000 0.0000 497 ASP B CG  
3799 O OD1 . ASP A 514 ? 1.3486 1.3486 1.3486 0.0000 0.0000 0.0000 497 ASP B OD1 
3800 O OD2 . ASP A 514 ? 1.3486 1.3486 1.3486 0.0000 0.0000 0.0000 497 ASP B OD2 
3801 N N   . LEU A 515 ? 1.2757 1.2757 1.2757 0.0000 0.0000 0.0000 498 LEU B N   
3802 C CA  . LEU A 515 ? 1.2757 1.2757 1.2757 0.0000 0.0000 0.0000 498 LEU B CA  
3803 C C   . LEU A 515 ? 1.2757 1.2757 1.2757 0.0000 0.0000 0.0000 498 LEU B C   
3804 O O   . LEU A 515 ? 1.2757 1.2757 1.2757 0.0000 0.0000 0.0000 498 LEU B O   
3805 C CB  . LEU A 515 ? 1.2757 1.2757 1.2757 0.0000 0.0000 0.0000 498 LEU B CB  
3806 C CG  . LEU A 515 ? 1.2757 1.2757 1.2757 0.0000 0.0000 0.0000 498 LEU B CG  
3807 C CD1 . LEU A 515 ? 1.2757 1.2757 1.2757 0.0000 0.0000 0.0000 498 LEU B CD1 
3808 C CD2 . LEU A 515 ? 1.2757 1.2757 1.2757 0.0000 0.0000 0.0000 498 LEU B CD2 
3809 N N   . ILE A 516 ? 1.2491 1.2491 1.2491 0.0000 0.0000 0.0000 499 ILE B N   
3810 C CA  . ILE A 516 ? 1.2491 1.2491 1.2491 0.0000 0.0000 0.0000 499 ILE B CA  
3811 C C   . ILE A 516 ? 1.2491 1.2491 1.2491 0.0000 0.0000 0.0000 499 ILE B C   
3812 O O   . ILE A 516 ? 1.2491 1.2491 1.2491 0.0000 0.0000 0.0000 499 ILE B O   
3813 C CB  . ILE A 516 ? 1.2491 1.2491 1.2491 0.0000 0.0000 0.0000 499 ILE B CB  
3814 C CG1 . ILE A 516 ? 1.2491 1.2491 1.2491 0.0000 0.0000 0.0000 499 ILE B CG1 
3815 C CG2 . ILE A 516 ? 1.2491 1.2491 1.2491 0.0000 0.0000 0.0000 499 ILE B CG2 
3816 C CD1 . ILE A 516 ? 1.2491 1.2491 1.2491 0.0000 0.0000 0.0000 499 ILE B CD1 
3817 N N   . GLN A 517 ? 1.2816 1.2816 1.2816 0.0000 0.0000 0.0000 500 GLN B N   
3818 C CA  . GLN A 517 ? 1.2816 1.2816 1.2816 0.0000 0.0000 0.0000 500 GLN B CA  
3819 C C   . GLN A 517 ? 1.2816 1.2816 1.2816 0.0000 0.0000 0.0000 500 GLN B C   
3820 O O   . GLN A 517 ? 1.2816 1.2816 1.2816 0.0000 0.0000 0.0000 500 GLN B O   
3821 C CB  . GLN A 517 ? 1.2816 1.2816 1.2816 0.0000 0.0000 0.0000 500 GLN B CB  
3822 C CG  . GLN A 517 ? 1.2816 1.2816 1.2816 0.0000 0.0000 0.0000 500 GLN B CG  
3823 C CD  . GLN A 517 ? 1.2816 1.2816 1.2816 0.0000 0.0000 0.0000 500 GLN B CD  
3824 O OE1 . GLN A 517 ? 1.2816 1.2816 1.2816 0.0000 0.0000 0.0000 500 GLN B OE1 
3825 N NE2 . GLN A 517 ? 1.2816 1.2816 1.2816 0.0000 0.0000 0.0000 500 GLN B NE2 
3826 N N   . GLN A 518 ? 1.2455 1.2455 1.2455 0.0000 0.0000 0.0000 501 GLN B N   
3827 C CA  . GLN A 518 ? 1.2455 1.2455 1.2455 0.0000 0.0000 0.0000 501 GLN B CA  
3828 C C   . GLN A 518 ? 1.2455 1.2455 1.2455 0.0000 0.0000 0.0000 501 GLN B C   
3829 O O   . GLN A 518 ? 1.2455 1.2455 1.2455 0.0000 0.0000 0.0000 501 GLN B O   
3830 C CB  . GLN A 518 ? 1.2455 1.2455 1.2455 0.0000 0.0000 0.0000 501 GLN B CB  
3831 C CG  . GLN A 518 ? 1.2455 1.2455 1.2455 0.0000 0.0000 0.0000 501 GLN B CG  
3832 C CD  . GLN A 518 ? 1.2455 1.2455 1.2455 0.0000 0.0000 0.0000 501 GLN B CD  
3833 O OE1 . GLN A 518 ? 1.2455 1.2455 1.2455 0.0000 0.0000 0.0000 501 GLN B OE1 
3834 N NE2 . GLN A 518 ? 1.2455 1.2455 1.2455 0.0000 0.0000 0.0000 501 GLN B NE2 
3835 N N   . TYR A 519 ? 1.1688 1.1688 1.1688 0.0000 0.0000 0.0000 502 TYR B N   
3836 C CA  . TYR A 519 ? 1.1688 1.1688 1.1688 0.0000 0.0000 0.0000 502 TYR B CA  
3837 C C   . TYR A 519 ? 1.1688 1.1688 1.1688 0.0000 0.0000 0.0000 502 TYR B C   
3838 O O   . TYR A 519 ? 1.1688 1.1688 1.1688 0.0000 0.0000 0.0000 502 TYR B O   
3839 C CB  . TYR A 519 ? 1.1688 1.1688 1.1688 0.0000 0.0000 0.0000 502 TYR B CB  
3840 C CG  . TYR A 519 ? 1.1688 1.1688 1.1688 0.0000 0.0000 0.0000 502 TYR B CG  
3841 C CD1 . TYR A 519 ? 1.1688 1.1688 1.1688 0.0000 0.0000 0.0000 502 TYR B CD1 
3842 C CD2 . TYR A 519 ? 1.1688 1.1688 1.1688 0.0000 0.0000 0.0000 502 TYR B CD2 
3843 C CE1 . TYR A 519 ? 1.1688 1.1688 1.1688 0.0000 0.0000 0.0000 502 TYR B CE1 
3844 C CE2 . TYR A 519 ? 1.1688 1.1688 1.1688 0.0000 0.0000 0.0000 502 TYR B CE2 
3845 C CZ  . TYR A 519 ? 1.1688 1.1688 1.1688 0.0000 0.0000 0.0000 502 TYR B CZ  
3846 O OH  . TYR A 519 ? 1.1688 1.1688 1.1688 0.0000 0.0000 0.0000 502 TYR B OH  
3847 N N   . TYR A 520 ? 1.1515 1.1515 1.1515 0.0000 0.0000 0.0000 503 TYR B N   
3848 C CA  . TYR A 520 ? 1.1515 1.1515 1.1515 0.0000 0.0000 0.0000 503 TYR B CA  
3849 C C   . TYR A 520 ? 1.1515 1.1515 1.1515 0.0000 0.0000 0.0000 503 TYR B C   
3850 O O   . TYR A 520 ? 1.1515 1.1515 1.1515 0.0000 0.0000 0.0000 503 TYR B O   
3851 C CB  . TYR A 520 ? 1.1515 1.1515 1.1515 0.0000 0.0000 0.0000 503 TYR B CB  
3852 C CG  . TYR A 520 ? 1.1515 1.1515 1.1515 0.0000 0.0000 0.0000 503 TYR B CG  
3853 C CD1 . TYR A 520 ? 1.1515 1.1515 1.1515 0.0000 0.0000 0.0000 503 TYR B CD1 
3854 C CD2 . TYR A 520 ? 1.1515 1.1515 1.1515 0.0000 0.0000 0.0000 503 TYR B CD2 
3855 C CE1 . TYR A 520 ? 1.1515 1.1515 1.1515 0.0000 0.0000 0.0000 503 TYR B CE1 
3856 C CE2 . TYR A 520 ? 1.1515 1.1515 1.1515 0.0000 0.0000 0.0000 503 TYR B CE2 
3857 C CZ  . TYR A 520 ? 1.1515 1.1515 1.1515 0.0000 0.0000 0.0000 503 TYR B CZ  
3858 O OH  . TYR A 520 ? 1.1515 1.1515 1.1515 0.0000 0.0000 0.0000 503 TYR B OH  
3859 N N   . LEU A 521 ? 1.2072 1.2072 1.2072 0.0000 0.0000 0.0000 504 LEU B N   
3860 C CA  . LEU A 521 ? 1.2072 1.2072 1.2072 0.0000 0.0000 0.0000 504 LEU B CA  
3861 C C   . LEU A 521 ? 1.2072 1.2072 1.2072 0.0000 0.0000 0.0000 504 LEU B C   
3862 O O   . LEU A 521 ? 1.2072 1.2072 1.2072 0.0000 0.0000 0.0000 504 LEU B O   
3863 C CB  . LEU A 521 ? 1.2072 1.2072 1.2072 0.0000 0.0000 0.0000 504 LEU B CB  
3864 C CG  . LEU A 521 ? 1.2072 1.2072 1.2072 0.0000 0.0000 0.0000 504 LEU B CG  
3865 C CD1 . LEU A 521 ? 1.2072 1.2072 1.2072 0.0000 0.0000 0.0000 504 LEU B CD1 
3866 C CD2 . LEU A 521 ? 1.2072 1.2072 1.2072 0.0000 0.0000 0.0000 504 LEU B CD2 
3867 N N   . THR A 522 ? 1.2246 1.2246 1.2246 0.0000 0.0000 0.0000 505 THR B N   
3868 C CA  . THR A 522 ? 1.2246 1.2246 1.2246 0.0000 0.0000 0.0000 505 THR B CA  
3869 C C   . THR A 522 ? 1.2246 1.2246 1.2246 0.0000 0.0000 0.0000 505 THR B C   
3870 O O   . THR A 522 ? 1.2246 1.2246 1.2246 0.0000 0.0000 0.0000 505 THR B O   
3871 C CB  . THR A 522 ? 1.2246 1.2246 1.2246 0.0000 0.0000 0.0000 505 THR B CB  
3872 O OG1 . THR A 522 ? 1.2246 1.2246 1.2246 0.0000 0.0000 0.0000 505 THR B OG1 
3873 C CG2 . THR A 522 ? 1.2246 1.2246 1.2246 0.0000 0.0000 0.0000 505 THR B CG2 
3874 N N   . PHE A 523 ? 1.1308 1.1308 1.1308 0.0000 0.0000 0.0000 506 PHE B N   
3875 C CA  . PHE A 523 ? 1.1308 1.1308 1.1308 0.0000 0.0000 0.0000 506 PHE B CA  
3876 C C   . PHE A 523 ? 1.1308 1.1308 1.1308 0.0000 0.0000 0.0000 506 PHE B C   
3877 O O   . PHE A 523 ? 1.1308 1.1308 1.1308 0.0000 0.0000 0.0000 506 PHE B O   
3878 C CB  . PHE A 523 ? 1.1308 1.1308 1.1308 0.0000 0.0000 0.0000 506 PHE B CB  
3879 C CG  . PHE A 523 ? 1.1308 1.1308 1.1308 0.0000 0.0000 0.0000 506 PHE B CG  
3880 C CD1 . PHE A 523 ? 1.1308 1.1308 1.1308 0.0000 0.0000 0.0000 506 PHE B CD1 
3881 C CD2 . PHE A 523 ? 1.1308 1.1308 1.1308 0.0000 0.0000 0.0000 506 PHE B CD2 
3882 C CE1 . PHE A 523 ? 1.1308 1.1308 1.1308 0.0000 0.0000 0.0000 506 PHE B CE1 
3883 C CE2 . PHE A 523 ? 1.1308 1.1308 1.1308 0.0000 0.0000 0.0000 506 PHE B CE2 
3884 C CZ  . PHE A 523 ? 1.1308 1.1308 1.1308 0.0000 0.0000 0.0000 506 PHE B CZ  
3885 N N   . ASN A 524 ? 1.2045 1.2045 1.2045 0.0000 0.0000 0.0000 507 ASN B N   
3886 C CA  . ASN A 524 ? 1.2045 1.2045 1.2045 0.0000 0.0000 0.0000 507 ASN B CA  
3887 C C   . ASN A 524 ? 1.2045 1.2045 1.2045 0.0000 0.0000 0.0000 507 ASN B C   
3888 O O   . ASN A 524 ? 1.2045 1.2045 1.2045 0.0000 0.0000 0.0000 507 ASN B O   
3889 C CB  . ASN A 524 ? 1.2045 1.2045 1.2045 0.0000 0.0000 0.0000 507 ASN B CB  
3890 C CG  . ASN A 524 ? 1.2045 1.2045 1.2045 0.0000 0.0000 0.0000 507 ASN B CG  
3891 O OD1 . ASN A 524 ? 1.2045 1.2045 1.2045 0.0000 0.0000 0.0000 507 ASN B OD1 
3892 N ND2 . ASN A 524 ? 1.2045 1.2045 1.2045 0.0000 0.0000 0.0000 507 ASN B ND2 
3893 N N   . PHE A 525 ? 1.2063 1.2063 1.2063 0.0000 0.0000 0.0000 508 PHE B N   
3894 C CA  . PHE A 525 ? 1.2063 1.2063 1.2063 0.0000 0.0000 0.0000 508 PHE B CA  
3895 C C   . PHE A 525 ? 1.2063 1.2063 1.2063 0.0000 0.0000 0.0000 508 PHE B C   
3896 O O   . PHE A 525 ? 1.2063 1.2063 1.2063 0.0000 0.0000 0.0000 508 PHE B O   
3897 C CB  . PHE A 525 ? 1.2063 1.2063 1.2063 0.0000 0.0000 0.0000 508 PHE B CB  
3898 C CG  . PHE A 525 ? 1.2063 1.2063 1.2063 0.0000 0.0000 0.0000 508 PHE B CG  
3899 C CD1 . PHE A 525 ? 1.2063 1.2063 1.2063 0.0000 0.0000 0.0000 508 PHE B CD1 
3900 C CD2 . PHE A 525 ? 1.2063 1.2063 1.2063 0.0000 0.0000 0.0000 508 PHE B CD2 
3901 C CE1 . PHE A 525 ? 1.2063 1.2063 1.2063 0.0000 0.0000 0.0000 508 PHE B CE1 
3902 C CE2 . PHE A 525 ? 1.2063 1.2063 1.2063 0.0000 0.0000 0.0000 508 PHE B CE2 
3903 C CZ  . PHE A 525 ? 1.2063 1.2063 1.2063 0.0000 0.0000 0.0000 508 PHE B CZ  
3904 N N   . ASP A 526 ? 1.3333 1.3333 1.3333 0.0000 0.0000 0.0000 509 ASP B N   
3905 C CA  . ASP A 526 ? 1.3333 1.3333 1.3333 0.0000 0.0000 0.0000 509 ASP B CA  
3906 C C   . ASP A 526 ? 1.3333 1.3333 1.3333 0.0000 0.0000 0.0000 509 ASP B C   
3907 O O   . ASP A 526 ? 1.3333 1.3333 1.3333 0.0000 0.0000 0.0000 509 ASP B O   
3908 C CB  . ASP A 526 ? 1.3333 1.3333 1.3333 0.0000 0.0000 0.0000 509 ASP B CB  
3909 C CG  . ASP A 526 ? 1.3333 1.3333 1.3333 0.0000 0.0000 0.0000 509 ASP B CG  
3910 O OD1 . ASP A 526 ? 1.3333 1.3333 1.3333 0.0000 0.0000 0.0000 509 ASP B OD1 
3911 O OD2 . ASP A 526 ? 1.3333 1.3333 1.3333 0.0000 0.0000 0.0000 509 ASP B OD2 
3912 N N   . ASN A 527 ? 1.2481 1.2481 1.2481 0.0000 0.0000 0.0000 510 ASN B N   
3913 C CA  . ASN A 527 ? 1.2481 1.2481 1.2481 0.0000 0.0000 0.0000 510 ASN B CA  
3914 C C   . ASN A 527 ? 1.2481 1.2481 1.2481 0.0000 0.0000 0.0000 510 ASN B C   
3915 O O   . ASN A 527 ? 1.2481 1.2481 1.2481 0.0000 0.0000 0.0000 510 ASN B O   
3916 C CB  . ASN A 527 ? 1.2481 1.2481 1.2481 0.0000 0.0000 0.0000 510 ASN B CB  
3917 C CG  . ASN A 527 ? 1.2481 1.2481 1.2481 0.0000 0.0000 0.0000 510 ASN B CG  
3918 O OD1 . ASN A 527 ? 1.2481 1.2481 1.2481 0.0000 0.0000 0.0000 510 ASN B OD1 
3919 N ND2 . ASN A 527 ? 1.2481 1.2481 1.2481 0.0000 0.0000 0.0000 510 ASN B ND2 
3920 N N   . GLU A 528 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 511 GLU B N   
3921 C CA  . GLU A 528 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 511 GLU B CA  
3922 C C   . GLU A 528 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 511 GLU B C   
3923 O O   . GLU A 528 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 511 GLU B O   
3924 C CB  . GLU A 528 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 511 GLU B CB  
3925 C CG  . GLU A 528 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 511 GLU B CG  
3926 C CD  . GLU A 528 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 511 GLU B CD  
3927 O OE1 . GLU A 528 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 511 GLU B OE1 
3928 O OE2 . GLU A 528 ? 1.1924 1.1924 1.1924 0.0000 0.0000 0.0000 511 GLU B OE2 
3929 N N   . PRO A 529 ? 1.1439 1.1439 1.1439 0.0000 0.0000 0.0000 512 PRO B N   
3930 C CA  . PRO A 529 ? 1.1439 1.1439 1.1439 0.0000 0.0000 0.0000 512 PRO B CA  
3931 C C   . PRO A 529 ? 1.1439 1.1439 1.1439 0.0000 0.0000 0.0000 512 PRO B C   
3932 O O   . PRO A 529 ? 1.1439 1.1439 1.1439 0.0000 0.0000 0.0000 512 PRO B O   
3933 C CB  . PRO A 529 ? 1.1439 1.1439 1.1439 0.0000 0.0000 0.0000 512 PRO B CB  
3934 C CG  . PRO A 529 ? 1.1439 1.1439 1.1439 0.0000 0.0000 0.0000 512 PRO B CG  
3935 C CD  . PRO A 529 ? 1.1439 1.1439 1.1439 0.0000 0.0000 0.0000 512 PRO B CD  
3936 N N   . GLU A 530 ? 1.1707 1.1707 1.1707 0.0000 0.0000 0.0000 513 GLU B N   
3937 C CA  . GLU A 530 ? 1.1707 1.1707 1.1707 0.0000 0.0000 0.0000 513 GLU B CA  
3938 C C   . GLU A 530 ? 1.1707 1.1707 1.1707 0.0000 0.0000 0.0000 513 GLU B C   
3939 O O   . GLU A 530 ? 1.1707 1.1707 1.1707 0.0000 0.0000 0.0000 513 GLU B O   
3940 C CB  . GLU A 530 ? 1.1707 1.1707 1.1707 0.0000 0.0000 0.0000 513 GLU B CB  
3941 C CG  . GLU A 530 ? 1.1707 1.1707 1.1707 0.0000 0.0000 0.0000 513 GLU B CG  
3942 C CD  . GLU A 530 ? 1.1707 1.1707 1.1707 0.0000 0.0000 0.0000 513 GLU B CD  
3943 O OE1 . GLU A 530 ? 1.1707 1.1707 1.1707 0.0000 0.0000 0.0000 513 GLU B OE1 
3944 O OE2 . GLU A 530 ? 1.1707 1.1707 1.1707 0.0000 0.0000 0.0000 513 GLU B OE2 
3945 N N   . ASN A 531 ? 1.1517 1.1517 1.1517 0.0000 0.0000 0.0000 514 ASN B N   
3946 C CA  . ASN A 531 ? 1.1517 1.1517 1.1517 0.0000 0.0000 0.0000 514 ASN B CA  
3947 C C   . ASN A 531 ? 1.1517 1.1517 1.1517 0.0000 0.0000 0.0000 514 ASN B C   
3948 O O   . ASN A 531 ? 1.1517 1.1517 1.1517 0.0000 0.0000 0.0000 514 ASN B O   
3949 C CB  . ASN A 531 ? 1.1517 1.1517 1.1517 0.0000 0.0000 0.0000 514 ASN B CB  
3950 C CG  . ASN A 531 ? 1.1517 1.1517 1.1517 0.0000 0.0000 0.0000 514 ASN B CG  
3951 O OD1 . ASN A 531 ? 1.1517 1.1517 1.1517 0.0000 0.0000 0.0000 514 ASN B OD1 
3952 N ND2 . ASN A 531 ? 1.1517 1.1517 1.1517 0.0000 0.0000 0.0000 514 ASN B ND2 
3953 N N   . ILE A 532 ? 1.1663 1.1663 1.1663 0.0000 0.0000 0.0000 515 ILE B N   
3954 C CA  . ILE A 532 ? 1.1663 1.1663 1.1663 0.0000 0.0000 0.0000 515 ILE B CA  
3955 C C   . ILE A 532 ? 1.1663 1.1663 1.1663 0.0000 0.0000 0.0000 515 ILE B C   
3956 O O   . ILE A 532 ? 1.1663 1.1663 1.1663 0.0000 0.0000 0.0000 515 ILE B O   
3957 C CB  . ILE A 532 ? 1.1663 1.1663 1.1663 0.0000 0.0000 0.0000 515 ILE B CB  
3958 C CG1 . ILE A 532 ? 1.1663 1.1663 1.1663 0.0000 0.0000 0.0000 515 ILE B CG1 
3959 C CG2 . ILE A 532 ? 1.1663 1.1663 1.1663 0.0000 0.0000 0.0000 515 ILE B CG2 
3960 C CD1 . ILE A 532 ? 1.1663 1.1663 1.1663 0.0000 0.0000 0.0000 515 ILE B CD1 
3961 N N   . SER A 533 ? 1.2150 1.2150 1.2150 0.0000 0.0000 0.0000 516 SER B N   
3962 C CA  . SER A 533 ? 1.2150 1.2150 1.2150 0.0000 0.0000 0.0000 516 SER B CA  
3963 C C   . SER A 533 ? 1.2150 1.2150 1.2150 0.0000 0.0000 0.0000 516 SER B C   
3964 O O   . SER A 533 ? 1.2150 1.2150 1.2150 0.0000 0.0000 0.0000 516 SER B O   
3965 C CB  . SER A 533 ? 1.2150 1.2150 1.2150 0.0000 0.0000 0.0000 516 SER B CB  
3966 O OG  . SER A 533 ? 1.2150 1.2150 1.2150 0.0000 0.0000 0.0000 516 SER B OG  
3967 N N   . ILE A 534 ? 1.1763 1.1763 1.1763 0.0000 0.0000 0.0000 517 ILE B N   
3968 C CA  . ILE A 534 ? 1.1763 1.1763 1.1763 0.0000 0.0000 0.0000 517 ILE B CA  
3969 C C   . ILE A 534 ? 1.1763 1.1763 1.1763 0.0000 0.0000 0.0000 517 ILE B C   
3970 O O   . ILE A 534 ? 1.1763 1.1763 1.1763 0.0000 0.0000 0.0000 517 ILE B O   
3971 C CB  . ILE A 534 ? 1.1763 1.1763 1.1763 0.0000 0.0000 0.0000 517 ILE B CB  
3972 C CG1 . ILE A 534 ? 1.1763 1.1763 1.1763 0.0000 0.0000 0.0000 517 ILE B CG1 
3973 C CG2 . ILE A 534 ? 1.1763 1.1763 1.1763 0.0000 0.0000 0.0000 517 ILE B CG2 
3974 C CD1 . ILE A 534 ? 1.1763 1.1763 1.1763 0.0000 0.0000 0.0000 517 ILE B CD1 
3975 N N   . GLU A 535 ? 1.2123 1.2123 1.2123 0.0000 0.0000 0.0000 518 GLU B N   
3976 C CA  . GLU A 535 ? 1.2123 1.2123 1.2123 0.0000 0.0000 0.0000 518 GLU B CA  
3977 C C   . GLU A 535 ? 1.2123 1.2123 1.2123 0.0000 0.0000 0.0000 518 GLU B C   
3978 O O   . GLU A 535 ? 1.2123 1.2123 1.2123 0.0000 0.0000 0.0000 518 GLU B O   
3979 C CB  . GLU A 535 ? 1.2123 1.2123 1.2123 0.0000 0.0000 0.0000 518 GLU B CB  
3980 C CG  . GLU A 535 ? 1.2123 1.2123 1.2123 0.0000 0.0000 0.0000 518 GLU B CG  
3981 C CD  . GLU A 535 ? 1.2123 1.2123 1.2123 0.0000 0.0000 0.0000 518 GLU B CD  
3982 O OE1 . GLU A 535 ? 1.2123 1.2123 1.2123 0.0000 0.0000 0.0000 518 GLU B OE1 
3983 O OE2 . GLU A 535 ? 1.2123 1.2123 1.2123 0.0000 0.0000 0.0000 518 GLU B OE2 
3984 N N   . ASN A 536 ? 1.1974 1.1974 1.1974 0.0000 0.0000 0.0000 519 ASN B N   
3985 C CA  . ASN A 536 ? 1.1974 1.1974 1.1974 0.0000 0.0000 0.0000 519 ASN B CA  
3986 C C   . ASN A 536 ? 1.1974 1.1974 1.1974 0.0000 0.0000 0.0000 519 ASN B C   
3987 O O   . ASN A 536 ? 1.1974 1.1974 1.1974 0.0000 0.0000 0.0000 519 ASN B O   
3988 C CB  . ASN A 536 ? 1.1974 1.1974 1.1974 0.0000 0.0000 0.0000 519 ASN B CB  
3989 C CG  . ASN A 536 ? 1.1974 1.1974 1.1974 0.0000 0.0000 0.0000 519 ASN B CG  
3990 O OD1 . ASN A 536 ? 1.1974 1.1974 1.1974 0.0000 0.0000 0.0000 519 ASN B OD1 
3991 N ND2 . ASN A 536 ? 1.1974 1.1974 1.1974 0.0000 0.0000 0.0000 519 ASN B ND2 
3992 N N   . LEU A 537 ? 1.1375 1.1375 1.1375 0.0000 0.0000 0.0000 520 LEU B N   
3993 C CA  . LEU A 537 ? 1.1375 1.1375 1.1375 0.0000 0.0000 0.0000 520 LEU B CA  
3994 C C   . LEU A 537 ? 1.1375 1.1375 1.1375 0.0000 0.0000 0.0000 520 LEU B C   
3995 O O   . LEU A 537 ? 1.1375 1.1375 1.1375 0.0000 0.0000 0.0000 520 LEU B O   
3996 C CB  . LEU A 537 ? 1.1375 1.1375 1.1375 0.0000 0.0000 0.0000 520 LEU B CB  
3997 C CG  . LEU A 537 ? 1.1375 1.1375 1.1375 0.0000 0.0000 0.0000 520 LEU B CG  
3998 C CD1 . LEU A 537 ? 1.1375 1.1375 1.1375 0.0000 0.0000 0.0000 520 LEU B CD1 
3999 C CD2 . LEU A 537 ? 1.1375 1.1375 1.1375 0.0000 0.0000 0.0000 520 LEU B CD2 
4000 N N   . SER A 538 ? 1.1468 1.1468 1.1468 0.0000 0.0000 0.0000 521 SER B N   
4001 C CA  . SER A 538 ? 1.1468 1.1468 1.1468 0.0000 0.0000 0.0000 521 SER B CA  
4002 C C   . SER A 538 ? 1.1468 1.1468 1.1468 0.0000 0.0000 0.0000 521 SER B C   
4003 O O   . SER A 538 ? 1.1468 1.1468 1.1468 0.0000 0.0000 0.0000 521 SER B O   
4004 C CB  . SER A 538 ? 1.1468 1.1468 1.1468 0.0000 0.0000 0.0000 521 SER B CB  
4005 O OG  . SER A 538 ? 1.1468 1.1468 1.1468 0.0000 0.0000 0.0000 521 SER B OG  
4006 N N   . SER A 539 ? 1.1357 1.1357 1.1357 0.0000 0.0000 0.0000 522 SER B N   
4007 C CA  . SER A 539 ? 1.1357 1.1357 1.1357 0.0000 0.0000 0.0000 522 SER B CA  
4008 C C   . SER A 539 ? 1.1357 1.1357 1.1357 0.0000 0.0000 0.0000 522 SER B C   
4009 O O   . SER A 539 ? 1.1357 1.1357 1.1357 0.0000 0.0000 0.0000 522 SER B O   
4010 C CB  . SER A 539 ? 1.1357 1.1357 1.1357 0.0000 0.0000 0.0000 522 SER B CB  
4011 O OG  . SER A 539 ? 1.1357 1.1357 1.1357 0.0000 0.0000 0.0000 522 SER B OG  
4012 N N   . ASP A 540 ? 1.1735 1.1735 1.1735 0.0000 0.0000 0.0000 523 ASP B N   
4013 C CA  . ASP A 540 ? 1.1735 1.1735 1.1735 0.0000 0.0000 0.0000 523 ASP B CA  
4014 C C   . ASP A 540 ? 1.1735 1.1735 1.1735 0.0000 0.0000 0.0000 523 ASP B C   
4015 O O   . ASP A 540 ? 1.1735 1.1735 1.1735 0.0000 0.0000 0.0000 523 ASP B O   
4016 C CB  . ASP A 540 ? 1.1735 1.1735 1.1735 0.0000 0.0000 0.0000 523 ASP B CB  
4017 C CG  . ASP A 540 ? 1.1735 1.1735 1.1735 0.0000 0.0000 0.0000 523 ASP B CG  
4018 O OD1 . ASP A 540 ? 1.1735 1.1735 1.1735 0.0000 0.0000 0.0000 523 ASP B OD1 
4019 O OD2 . ASP A 540 ? 1.1735 1.1735 1.1735 0.0000 0.0000 0.0000 523 ASP B OD2 
4020 N N   . ILE A 541 ? 1.1306 1.1306 1.1306 0.0000 0.0000 0.0000 524 ILE B N   
4021 C CA  . ILE A 541 ? 1.1306 1.1306 1.1306 0.0000 0.0000 0.0000 524 ILE B CA  
4022 C C   . ILE A 541 ? 1.1306 1.1306 1.1306 0.0000 0.0000 0.0000 524 ILE B C   
4023 O O   . ILE A 541 ? 1.1306 1.1306 1.1306 0.0000 0.0000 0.0000 524 ILE B O   
4024 C CB  . ILE A 541 ? 1.1306 1.1306 1.1306 0.0000 0.0000 0.0000 524 ILE B CB  
4025 C CG1 . ILE A 541 ? 1.1306 1.1306 1.1306 0.0000 0.0000 0.0000 524 ILE B CG1 
4026 C CG2 . ILE A 541 ? 1.1306 1.1306 1.1306 0.0000 0.0000 0.0000 524 ILE B CG2 
4027 C CD1 . ILE A 541 ? 1.1306 1.1306 1.1306 0.0000 0.0000 0.0000 524 ILE B CD1 
4028 N N   . ILE A 542 ? 1.1840 1.1840 1.1840 0.0000 0.0000 0.0000 525 ILE B N   
4029 C CA  . ILE A 542 ? 1.1840 1.1840 1.1840 0.0000 0.0000 0.0000 525 ILE B CA  
4030 C C   . ILE A 542 ? 1.1840 1.1840 1.1840 0.0000 0.0000 0.0000 525 ILE B C   
4031 O O   . ILE A 542 ? 1.1840 1.1840 1.1840 0.0000 0.0000 0.0000 525 ILE B O   
4032 C CB  . ILE A 542 ? 1.1840 1.1840 1.1840 0.0000 0.0000 0.0000 525 ILE B CB  
4033 C CG1 . ILE A 542 ? 1.1840 1.1840 1.1840 0.0000 0.0000 0.0000 525 ILE B CG1 
4034 C CG2 . ILE A 542 ? 1.1840 1.1840 1.1840 0.0000 0.0000 0.0000 525 ILE B CG2 
4035 C CD1 . ILE A 542 ? 1.1840 1.1840 1.1840 0.0000 0.0000 0.0000 525 ILE B CD1 
4036 N N   . GLY A 543 ? 1.1641 1.1641 1.1641 0.0000 0.0000 0.0000 526 GLY B N   
4037 C CA  . GLY A 543 ? 1.1641 1.1641 1.1641 0.0000 0.0000 0.0000 526 GLY B CA  
4038 C C   . GLY A 543 ? 1.1641 1.1641 1.1641 0.0000 0.0000 0.0000 526 GLY B C   
4039 O O   . GLY A 543 ? 1.1641 1.1641 1.1641 0.0000 0.0000 0.0000 526 GLY B O   
4040 N N   . GLN A 544 ? 1.1736 1.1736 1.1736 0.0000 0.0000 0.0000 527 GLN B N   
4041 C CA  . GLN A 544 ? 1.1736 1.1736 1.1736 0.0000 0.0000 0.0000 527 GLN B CA  
4042 C C   . GLN A 544 ? 1.1736 1.1736 1.1736 0.0000 0.0000 0.0000 527 GLN B C   
4043 O O   . GLN A 544 ? 1.1736 1.1736 1.1736 0.0000 0.0000 0.0000 527 GLN B O   
4044 C CB  . GLN A 544 ? 1.1736 1.1736 1.1736 0.0000 0.0000 0.0000 527 GLN B CB  
4045 C CG  . GLN A 544 ? 1.1736 1.1736 1.1736 0.0000 0.0000 0.0000 527 GLN B CG  
4046 C CD  . GLN A 544 ? 1.1736 1.1736 1.1736 0.0000 0.0000 0.0000 527 GLN B CD  
4047 O OE1 . GLN A 544 ? 1.1736 1.1736 1.1736 0.0000 0.0000 0.0000 527 GLN B OE1 
4048 N NE2 . GLN A 544 ? 1.1736 1.1736 1.1736 0.0000 0.0000 0.0000 527 GLN B NE2 
4049 N N   . LEU A 545 ? 1.1122 1.1122 1.1122 0.0000 0.0000 0.0000 528 LEU B N   
4050 C CA  . LEU A 545 ? 1.1122 1.1122 1.1122 0.0000 0.0000 0.0000 528 LEU B CA  
4051 C C   . LEU A 545 ? 1.1122 1.1122 1.1122 0.0000 0.0000 0.0000 528 LEU B C   
4052 O O   . LEU A 545 ? 1.1122 1.1122 1.1122 0.0000 0.0000 0.0000 528 LEU B O   
4053 C CB  . LEU A 545 ? 1.1122 1.1122 1.1122 0.0000 0.0000 0.0000 528 LEU B CB  
4054 C CG  . LEU A 545 ? 1.1122 1.1122 1.1122 0.0000 0.0000 0.0000 528 LEU B CG  
4055 C CD1 . LEU A 545 ? 1.1122 1.1122 1.1122 0.0000 0.0000 0.0000 528 LEU B CD1 
4056 C CD2 . LEU A 545 ? 1.1122 1.1122 1.1122 0.0000 0.0000 0.0000 528 LEU B CD2 
4057 N N   . GLU A 546 ? 1.2098 1.2098 1.2098 0.0000 0.0000 0.0000 529 GLU B N   
4058 C CA  . GLU A 546 ? 1.2098 1.2098 1.2098 0.0000 0.0000 0.0000 529 GLU B CA  
4059 C C   . GLU A 546 ? 1.2098 1.2098 1.2098 0.0000 0.0000 0.0000 529 GLU B C   
4060 O O   . GLU A 546 ? 1.2098 1.2098 1.2098 0.0000 0.0000 0.0000 529 GLU B O   
4061 C CB  . GLU A 546 ? 1.2098 1.2098 1.2098 0.0000 0.0000 0.0000 529 GLU B CB  
4062 C CG  . GLU A 546 ? 1.2098 1.2098 1.2098 0.0000 0.0000 0.0000 529 GLU B CG  
4063 C CD  . GLU A 546 ? 1.2098 1.2098 1.2098 0.0000 0.0000 0.0000 529 GLU B CD  
4064 O OE1 . GLU A 546 ? 1.2098 1.2098 1.2098 0.0000 0.0000 0.0000 529 GLU B OE1 
4065 O OE2 . GLU A 546 ? 1.2098 1.2098 1.2098 0.0000 0.0000 0.0000 529 GLU B OE2 
4066 N N   . LEU A 547 ? 1.4149 1.4149 1.4149 0.0000 0.0000 0.0000 530 LEU B N   
4067 C CA  . LEU A 547 ? 1.4149 1.4149 1.4149 0.0000 0.0000 0.0000 530 LEU B CA  
4068 C C   . LEU A 547 ? 1.4149 1.4149 1.4149 0.0000 0.0000 0.0000 530 LEU B C   
4069 O O   . LEU A 547 ? 1.4149 1.4149 1.4149 0.0000 0.0000 0.0000 530 LEU B O   
4070 C CB  . LEU A 547 ? 1.4149 1.4149 1.4149 0.0000 0.0000 0.0000 530 LEU B CB  
4071 C CG  . LEU A 547 ? 1.4149 1.4149 1.4149 0.0000 0.0000 0.0000 530 LEU B CG  
4072 C CD1 . LEU A 547 ? 1.4149 1.4149 1.4149 0.0000 0.0000 0.0000 530 LEU B CD1 
4073 C CD2 . LEU A 547 ? 1.4149 1.4149 1.4149 0.0000 0.0000 0.0000 530 LEU B CD2 
4074 N N   . MET A 548 ? 1.5439 1.5439 1.5439 0.0000 0.0000 0.0000 531 MET B N   
4075 C CA  . MET A 548 ? 1.5439 1.5439 1.5439 0.0000 0.0000 0.0000 531 MET B CA  
4076 C C   . MET A 548 ? 1.5439 1.5439 1.5439 0.0000 0.0000 0.0000 531 MET B C   
4077 O O   . MET A 548 ? 1.5439 1.5439 1.5439 0.0000 0.0000 0.0000 531 MET B O   
4078 C CB  . MET A 548 ? 1.5439 1.5439 1.5439 0.0000 0.0000 0.0000 531 MET B CB  
4079 C CG  . MET A 548 ? 1.5439 1.5439 1.5439 0.0000 0.0000 0.0000 531 MET B CG  
4080 S SD  . MET A 548 ? 1.5439 1.5439 1.5439 0.0000 0.0000 0.0000 531 MET B SD  
4081 C CE  . MET A 548 ? 1.5439 1.5439 1.5439 0.0000 0.0000 0.0000 531 MET B CE  
4082 N N   . PRO A 549 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 532 PRO B N   
4083 C CA  . PRO A 549 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 532 PRO B CA  
4084 C C   . PRO A 549 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 532 PRO B C   
4085 O O   . PRO A 549 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 532 PRO B O   
4086 C CB  . PRO A 549 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 532 PRO B CB  
4087 C CG  . PRO A 549 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 532 PRO B CG  
4088 C CD  . PRO A 549 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 532 PRO B CD  
4089 N N   . ASN A 550 ? 1.7279 1.7279 1.7279 0.0000 0.0000 0.0000 533 ASN B N   
4090 C CA  . ASN A 550 ? 1.7279 1.7279 1.7279 0.0000 0.0000 0.0000 533 ASN B CA  
4091 C C   . ASN A 550 ? 1.7279 1.7279 1.7279 0.0000 0.0000 0.0000 533 ASN B C   
4092 O O   . ASN A 550 ? 1.7279 1.7279 1.7279 0.0000 0.0000 0.0000 533 ASN B O   
4093 C CB  . ASN A 550 ? 1.7279 1.7279 1.7279 0.0000 0.0000 0.0000 533 ASN B CB  
4094 C CG  . ASN A 550 ? 1.7279 1.7279 1.7279 0.0000 0.0000 0.0000 533 ASN B CG  
4095 O OD1 . ASN A 550 ? 1.7279 1.7279 1.7279 0.0000 0.0000 0.0000 533 ASN B OD1 
4096 N ND2 . ASN A 550 ? 1.7279 1.7279 1.7279 0.0000 0.0000 0.0000 533 ASN B ND2 
4097 N N   . ILE A 551 ? 1.6638 1.6638 1.6638 0.0000 0.0000 0.0000 534 ILE B N   
4098 C CA  . ILE A 551 ? 1.6638 1.6638 1.6638 0.0000 0.0000 0.0000 534 ILE B CA  
4099 C C   . ILE A 551 ? 1.6638 1.6638 1.6638 0.0000 0.0000 0.0000 534 ILE B C   
4100 O O   . ILE A 551 ? 1.6638 1.6638 1.6638 0.0000 0.0000 0.0000 534 ILE B O   
4101 C CB  . ILE A 551 ? 1.6638 1.6638 1.6638 0.0000 0.0000 0.0000 534 ILE B CB  
4102 C CG1 . ILE A 551 ? 1.6638 1.6638 1.6638 0.0000 0.0000 0.0000 534 ILE B CG1 
4103 C CG2 . ILE A 551 ? 1.6638 1.6638 1.6638 0.0000 0.0000 0.0000 534 ILE B CG2 
4104 C CD1 . ILE A 551 ? 1.6638 1.6638 1.6638 0.0000 0.0000 0.0000 534 ILE B CD1 
4105 N N   . GLU A 552 ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 535 GLU B N   
4106 C CA  . GLU A 552 ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 535 GLU B CA  
4107 C C   . GLU A 552 ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 535 GLU B C   
4108 O O   . GLU A 552 ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 535 GLU B O   
4109 C CB  . GLU A 552 ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 535 GLU B CB  
4110 C CG  . GLU A 552 ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 535 GLU B CG  
4111 C CD  . GLU A 552 ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 535 GLU B CD  
4112 O OE1 . GLU A 552 ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 535 GLU B OE1 
4113 O OE2 . GLU A 552 ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 535 GLU B OE2 
4114 N N   . ARG A 553 ? 1.4527 1.4527 1.4527 0.0000 0.0000 0.0000 536 ARG B N   
4115 C CA  . ARG A 553 ? 1.4527 1.4527 1.4527 0.0000 0.0000 0.0000 536 ARG B CA  
4116 C C   . ARG A 553 ? 1.4527 1.4527 1.4527 0.0000 0.0000 0.0000 536 ARG B C   
4117 O O   . ARG A 553 ? 1.4527 1.4527 1.4527 0.0000 0.0000 0.0000 536 ARG B O   
4118 C CB  . ARG A 553 ? 1.4527 1.4527 1.4527 0.0000 0.0000 0.0000 536 ARG B CB  
4119 C CG  . ARG A 553 ? 1.4527 1.4527 1.4527 0.0000 0.0000 0.0000 536 ARG B CG  
4120 C CD  . ARG A 553 ? 1.4527 1.4527 1.4527 0.0000 0.0000 0.0000 536 ARG B CD  
4121 N NE  . ARG A 553 ? 1.4527 1.4527 1.4527 0.0000 0.0000 0.0000 536 ARG B NE  
4122 C CZ  . ARG A 553 ? 1.4527 1.4527 1.4527 0.0000 0.0000 0.0000 536 ARG B CZ  
4123 N NH1 . ARG A 553 ? 1.4527 1.4527 1.4527 0.0000 0.0000 0.0000 536 ARG B NH1 
4124 N NH2 . ARG A 553 ? 1.4527 1.4527 1.4527 0.0000 0.0000 0.0000 536 ARG B NH2 
4125 N N   . PHE A 554 ? 1.3385 1.3385 1.3385 0.0000 0.0000 0.0000 537 PHE B N   
4126 C CA  . PHE A 554 ? 1.3385 1.3385 1.3385 0.0000 0.0000 0.0000 537 PHE B CA  
4127 C C   . PHE A 554 ? 1.3385 1.3385 1.3385 0.0000 0.0000 0.0000 537 PHE B C   
4128 O O   . PHE A 554 ? 1.3385 1.3385 1.3385 0.0000 0.0000 0.0000 537 PHE B O   
4129 C CB  . PHE A 554 ? 1.3385 1.3385 1.3385 0.0000 0.0000 0.0000 537 PHE B CB  
4130 C CG  . PHE A 554 ? 1.3385 1.3385 1.3385 0.0000 0.0000 0.0000 537 PHE B CG  
4131 C CD1 . PHE A 554 ? 1.3385 1.3385 1.3385 0.0000 0.0000 0.0000 537 PHE B CD1 
4132 C CD2 . PHE A 554 ? 1.3385 1.3385 1.3385 0.0000 0.0000 0.0000 537 PHE B CD2 
4133 C CE1 . PHE A 554 ? 1.3385 1.3385 1.3385 0.0000 0.0000 0.0000 537 PHE B CE1 
4134 C CE2 . PHE A 554 ? 1.3385 1.3385 1.3385 0.0000 0.0000 0.0000 537 PHE B CE2 
4135 C CZ  . PHE A 554 ? 1.3385 1.3385 1.3385 0.0000 0.0000 0.0000 537 PHE B CZ  
4136 N N   . PRO A 555 ? 1.2583 1.2583 1.2583 0.0000 0.0000 0.0000 538 PRO B N   
4137 C CA  . PRO A 555 ? 1.2583 1.2583 1.2583 0.0000 0.0000 0.0000 538 PRO B CA  
4138 C C   . PRO A 555 ? 1.2583 1.2583 1.2583 0.0000 0.0000 0.0000 538 PRO B C   
4139 O O   . PRO A 555 ? 1.2583 1.2583 1.2583 0.0000 0.0000 0.0000 538 PRO B O   
4140 C CB  . PRO A 555 ? 1.2583 1.2583 1.2583 0.0000 0.0000 0.0000 538 PRO B CB  
4141 C CG  . PRO A 555 ? 1.2583 1.2583 1.2583 0.0000 0.0000 0.0000 538 PRO B CG  
4142 C CD  . PRO A 555 ? 1.2583 1.2583 1.2583 0.0000 0.0000 0.0000 538 PRO B CD  
4143 N N   . ASN A 556 ? 1.0975 1.0975 1.0975 0.0000 0.0000 0.0000 539 ASN B N   
4144 C CA  . ASN A 556 ? 1.0975 1.0975 1.0975 0.0000 0.0000 0.0000 539 ASN B CA  
4145 C C   . ASN A 556 ? 1.0975 1.0975 1.0975 0.0000 0.0000 0.0000 539 ASN B C   
4146 O O   . ASN A 556 ? 1.0975 1.0975 1.0975 0.0000 0.0000 0.0000 539 ASN B O   
4147 C CB  . ASN A 556 ? 1.0975 1.0975 1.0975 0.0000 0.0000 0.0000 539 ASN B CB  
4148 C CG  . ASN A 556 ? 1.0975 1.0975 1.0975 0.0000 0.0000 0.0000 539 ASN B CG  
4149 O OD1 . ASN A 556 ? 1.0975 1.0975 1.0975 0.0000 0.0000 0.0000 539 ASN B OD1 
4150 N ND2 . ASN A 556 ? 1.0975 1.0975 1.0975 0.0000 0.0000 0.0000 539 ASN B ND2 
4151 N N   . GLY A 557 ? 1.0323 1.0323 1.0323 0.0000 0.0000 0.0000 540 GLY B N   
4152 C CA  . GLY A 557 ? 1.0323 1.0323 1.0323 0.0000 0.0000 0.0000 540 GLY B CA  
4153 C C   . GLY A 557 ? 1.0323 1.0323 1.0323 0.0000 0.0000 0.0000 540 GLY B C   
4154 O O   . GLY A 557 ? 1.0323 1.0323 1.0323 0.0000 0.0000 0.0000 540 GLY B O   
4155 N N   . LYS A 558 ? 1.0161 1.0161 1.0161 0.0000 0.0000 0.0000 541 LYS B N   
4156 C CA  . LYS A 558 ? 1.0161 1.0161 1.0161 0.0000 0.0000 0.0000 541 LYS B CA  
4157 C C   . LYS A 558 ? 1.0161 1.0161 1.0161 0.0000 0.0000 0.0000 541 LYS B C   
4158 O O   . LYS A 558 ? 1.0161 1.0161 1.0161 0.0000 0.0000 0.0000 541 LYS B O   
4159 C CB  . LYS A 558 ? 1.0161 1.0161 1.0161 0.0000 0.0000 0.0000 541 LYS B CB  
4160 C CG  . LYS A 558 ? 1.0161 1.0161 1.0161 0.0000 0.0000 0.0000 541 LYS B CG  
4161 C CD  . LYS A 558 ? 1.0161 1.0161 1.0161 0.0000 0.0000 0.0000 541 LYS B CD  
4162 C CE  . LYS A 558 ? 1.0161 1.0161 1.0161 0.0000 0.0000 0.0000 541 LYS B CE  
4163 N NZ  . LYS A 558 ? 1.0161 1.0161 1.0161 0.0000 0.0000 0.0000 541 LYS B NZ  
4164 N N   . LYS A 559 ? 0.9702 0.9702 0.9702 0.0000 0.0000 0.0000 542 LYS B N   
4165 C CA  . LYS A 559 ? 0.9702 0.9702 0.9702 0.0000 0.0000 0.0000 542 LYS B CA  
4166 C C   . LYS A 559 ? 0.9702 0.9702 0.9702 0.0000 0.0000 0.0000 542 LYS B C   
4167 O O   . LYS A 559 ? 0.9702 0.9702 0.9702 0.0000 0.0000 0.0000 542 LYS B O   
4168 C CB  . LYS A 559 ? 0.9702 0.9702 0.9702 0.0000 0.0000 0.0000 542 LYS B CB  
4169 C CG  . LYS A 559 ? 0.9702 0.9702 0.9702 0.0000 0.0000 0.0000 542 LYS B CG  
4170 C CD  . LYS A 559 ? 0.9702 0.9702 0.9702 0.0000 0.0000 0.0000 542 LYS B CD  
4171 C CE  . LYS A 559 ? 0.9702 0.9702 0.9702 0.0000 0.0000 0.0000 542 LYS B CE  
4172 N NZ  . LYS A 559 ? 0.9702 0.9702 0.9702 0.0000 0.0000 0.0000 542 LYS B NZ  
4173 N N   . TYR A 560 ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 543 TYR B N   
4174 C CA  . TYR A 560 ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 543 TYR B CA  
4175 C C   . TYR A 560 ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 543 TYR B C   
4176 O O   . TYR A 560 ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 543 TYR B O   
4177 C CB  . TYR A 560 ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 543 TYR B CB  
4178 C CG  . TYR A 560 ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 543 TYR B CG  
4179 C CD1 . TYR A 560 ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 543 TYR B CD1 
4180 C CD2 . TYR A 560 ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 543 TYR B CD2 
4181 C CE1 . TYR A 560 ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 543 TYR B CE1 
4182 C CE2 . TYR A 560 ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 543 TYR B CE2 
4183 C CZ  . TYR A 560 ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 543 TYR B CZ  
4184 O OH  . TYR A 560 ? 1.0021 1.0021 1.0021 0.0000 0.0000 0.0000 543 TYR B OH  
4185 N N   . GLU A 561 ? 1.0694 1.0694 1.0694 0.0000 0.0000 0.0000 544 GLU B N   
4186 C CA  . GLU A 561 ? 1.0694 1.0694 1.0694 0.0000 0.0000 0.0000 544 GLU B CA  
4187 C C   . GLU A 561 ? 1.0694 1.0694 1.0694 0.0000 0.0000 0.0000 544 GLU B C   
4188 O O   . GLU A 561 ? 1.0694 1.0694 1.0694 0.0000 0.0000 0.0000 544 GLU B O   
4189 C CB  . GLU A 561 ? 1.0694 1.0694 1.0694 0.0000 0.0000 0.0000 544 GLU B CB  
4190 C CG  . GLU A 561 ? 1.0694 1.0694 1.0694 0.0000 0.0000 0.0000 544 GLU B CG  
4191 C CD  . GLU A 561 ? 1.0694 1.0694 1.0694 0.0000 0.0000 0.0000 544 GLU B CD  
4192 O OE1 . GLU A 561 ? 1.0694 1.0694 1.0694 0.0000 0.0000 0.0000 544 GLU B OE1 
4193 O OE2 . GLU A 561 ? 1.0694 1.0694 1.0694 0.0000 0.0000 0.0000 544 GLU B OE2 
4194 N N   . LEU A 562 ? 1.0634 1.0634 1.0634 0.0000 0.0000 0.0000 545 LEU B N   
4195 C CA  . LEU A 562 ? 1.0634 1.0634 1.0634 0.0000 0.0000 0.0000 545 LEU B CA  
4196 C C   . LEU A 562 ? 1.0634 1.0634 1.0634 0.0000 0.0000 0.0000 545 LEU B C   
4197 O O   . LEU A 562 ? 1.0634 1.0634 1.0634 0.0000 0.0000 0.0000 545 LEU B O   
4198 C CB  . LEU A 562 ? 1.0634 1.0634 1.0634 0.0000 0.0000 0.0000 545 LEU B CB  
4199 C CG  . LEU A 562 ? 1.0634 1.0634 1.0634 0.0000 0.0000 0.0000 545 LEU B CG  
4200 C CD1 . LEU A 562 ? 1.0634 1.0634 1.0634 0.0000 0.0000 0.0000 545 LEU B CD1 
4201 C CD2 . LEU A 562 ? 1.0634 1.0634 1.0634 0.0000 0.0000 0.0000 545 LEU B CD2 
4202 N N   . ASP A 563 ? 1.1265 1.1265 1.1265 0.0000 0.0000 0.0000 546 ASP B N   
4203 C CA  . ASP A 563 ? 1.1265 1.1265 1.1265 0.0000 0.0000 0.0000 546 ASP B CA  
4204 C C   . ASP A 563 ? 1.1265 1.1265 1.1265 0.0000 0.0000 0.0000 546 ASP B C   
4205 O O   . ASP A 563 ? 1.1265 1.1265 1.1265 0.0000 0.0000 0.0000 546 ASP B O   
4206 C CB  . ASP A 563 ? 1.1265 1.1265 1.1265 0.0000 0.0000 0.0000 546 ASP B CB  
4207 C CG  . ASP A 563 ? 1.1265 1.1265 1.1265 0.0000 0.0000 0.0000 546 ASP B CG  
4208 O OD1 . ASP A 563 ? 1.1265 1.1265 1.1265 0.0000 0.0000 0.0000 546 ASP B OD1 
4209 O OD2 . ASP A 563 ? 1.1265 1.1265 1.1265 0.0000 0.0000 0.0000 546 ASP B OD2 
4210 N N   . LYS A 564 ? 1.0796 1.0796 1.0796 0.0000 0.0000 0.0000 547 LYS B N   
4211 C CA  . LYS A 564 ? 1.0796 1.0796 1.0796 0.0000 0.0000 0.0000 547 LYS B CA  
4212 C C   . LYS A 564 ? 1.0796 1.0796 1.0796 0.0000 0.0000 0.0000 547 LYS B C   
4213 O O   . LYS A 564 ? 1.0796 1.0796 1.0796 0.0000 0.0000 0.0000 547 LYS B O   
4214 C CB  . LYS A 564 ? 1.0796 1.0796 1.0796 0.0000 0.0000 0.0000 547 LYS B CB  
4215 C CG  . LYS A 564 ? 1.0796 1.0796 1.0796 0.0000 0.0000 0.0000 547 LYS B CG  
4216 C CD  . LYS A 564 ? 1.0796 1.0796 1.0796 0.0000 0.0000 0.0000 547 LYS B CD  
4217 C CE  . LYS A 564 ? 1.0796 1.0796 1.0796 0.0000 0.0000 0.0000 547 LYS B CE  
4218 N NZ  . LYS A 564 ? 1.0796 1.0796 1.0796 0.0000 0.0000 0.0000 547 LYS B NZ  
4219 N N   . TYR A 565 ? 1.0011 1.0011 1.0011 0.0000 0.0000 0.0000 548 TYR B N   
4220 C CA  . TYR A 565 ? 1.0011 1.0011 1.0011 0.0000 0.0000 0.0000 548 TYR B CA  
4221 C C   . TYR A 565 ? 1.0011 1.0011 1.0011 0.0000 0.0000 0.0000 548 TYR B C   
4222 O O   . TYR A 565 ? 1.0011 1.0011 1.0011 0.0000 0.0000 0.0000 548 TYR B O   
4223 C CB  . TYR A 565 ? 1.0011 1.0011 1.0011 0.0000 0.0000 0.0000 548 TYR B CB  
4224 C CG  . TYR A 565 ? 1.0011 1.0011 1.0011 0.0000 0.0000 0.0000 548 TYR B CG  
4225 C CD1 . TYR A 565 ? 1.0011 1.0011 1.0011 0.0000 0.0000 0.0000 548 TYR B CD1 
4226 C CD2 . TYR A 565 ? 1.0011 1.0011 1.0011 0.0000 0.0000 0.0000 548 TYR B CD2 
4227 C CE1 . TYR A 565 ? 1.0011 1.0011 1.0011 0.0000 0.0000 0.0000 548 TYR B CE1 
4228 C CE2 . TYR A 565 ? 1.0011 1.0011 1.0011 0.0000 0.0000 0.0000 548 TYR B CE2 
4229 C CZ  . TYR A 565 ? 1.0011 1.0011 1.0011 0.0000 0.0000 0.0000 548 TYR B CZ  
4230 O OH  . TYR A 565 ? 1.0011 1.0011 1.0011 0.0000 0.0000 0.0000 548 TYR B OH  
4231 N N   . THR A 566 ? 0.9903 0.9903 0.9903 0.0000 0.0000 0.0000 549 THR B N   
4232 C CA  . THR A 566 ? 0.9903 0.9903 0.9903 0.0000 0.0000 0.0000 549 THR B CA  
4233 C C   . THR A 566 ? 0.9903 0.9903 0.9903 0.0000 0.0000 0.0000 549 THR B C   
4234 O O   . THR A 566 ? 0.9903 0.9903 0.9903 0.0000 0.0000 0.0000 549 THR B O   
4235 C CB  . THR A 566 ? 0.9903 0.9903 0.9903 0.0000 0.0000 0.0000 549 THR B CB  
4236 O OG1 . THR A 566 ? 0.9903 0.9903 0.9903 0.0000 0.0000 0.0000 549 THR B OG1 
4237 C CG2 . THR A 566 ? 0.9903 0.9903 0.9903 0.0000 0.0000 0.0000 549 THR B CG2 
4238 N N   . MET A 567 ? 0.9738 0.9738 0.9738 0.0000 0.0000 0.0000 550 MET B N   
4239 C CA  . MET A 567 ? 0.9738 0.9738 0.9738 0.0000 0.0000 0.0000 550 MET B CA  
4240 C C   . MET A 567 ? 0.9738 0.9738 0.9738 0.0000 0.0000 0.0000 550 MET B C   
4241 O O   . MET A 567 ? 0.9738 0.9738 0.9738 0.0000 0.0000 0.0000 550 MET B O   
4242 C CB  . MET A 567 ? 0.9738 0.9738 0.9738 0.0000 0.0000 0.0000 550 MET B CB  
4243 C CG  . MET A 567 ? 0.9738 0.9738 0.9738 0.0000 0.0000 0.0000 550 MET B CG  
4244 S SD  . MET A 567 ? 0.9738 0.9738 0.9738 0.0000 0.0000 0.0000 550 MET B SD  
4245 C CE  . MET A 567 ? 0.9738 0.9738 0.9738 0.0000 0.0000 0.0000 550 MET B CE  
4246 N N   . PHE A 568 ? 0.9101 0.9101 0.9101 0.0000 0.0000 0.0000 551 PHE B N   
4247 C CA  . PHE A 568 ? 0.9101 0.9101 0.9101 0.0000 0.0000 0.0000 551 PHE B CA  
4248 C C   . PHE A 568 ? 0.9101 0.9101 0.9101 0.0000 0.0000 0.0000 551 PHE B C   
4249 O O   . PHE A 568 ? 0.9101 0.9101 0.9101 0.0000 0.0000 0.0000 551 PHE B O   
4250 C CB  . PHE A 568 ? 0.9101 0.9101 0.9101 0.0000 0.0000 0.0000 551 PHE B CB  
4251 C CG  . PHE A 568 ? 0.9101 0.9101 0.9101 0.0000 0.0000 0.0000 551 PHE B CG  
4252 C CD1 . PHE A 568 ? 0.9101 0.9101 0.9101 0.0000 0.0000 0.0000 551 PHE B CD1 
4253 C CD2 . PHE A 568 ? 0.9101 0.9101 0.9101 0.0000 0.0000 0.0000 551 PHE B CD2 
4254 C CE1 . PHE A 568 ? 0.9101 0.9101 0.9101 0.0000 0.0000 0.0000 551 PHE B CE1 
4255 C CE2 . PHE A 568 ? 0.9101 0.9101 0.9101 0.0000 0.0000 0.0000 551 PHE B CE2 
4256 C CZ  . PHE A 568 ? 0.9101 0.9101 0.9101 0.0000 0.0000 0.0000 551 PHE B CZ  
4257 N N   . HIS A 569 ? 0.9394 0.9394 0.9394 0.0000 0.0000 0.0000 552 HIS B N   
4258 C CA  . HIS A 569 ? 0.9394 0.9394 0.9394 0.0000 0.0000 0.0000 552 HIS B CA  
4259 C C   . HIS A 569 ? 0.9394 0.9394 0.9394 0.0000 0.0000 0.0000 552 HIS B C   
4260 O O   . HIS A 569 ? 0.9394 0.9394 0.9394 0.0000 0.0000 0.0000 552 HIS B O   
4261 C CB  . HIS A 569 ? 0.9394 0.9394 0.9394 0.0000 0.0000 0.0000 552 HIS B CB  
4262 C CG  . HIS A 569 ? 0.9394 0.9394 0.9394 0.0000 0.0000 0.0000 552 HIS B CG  
4263 N ND1 . HIS A 569 ? 0.9394 0.9394 0.9394 0.0000 0.0000 0.0000 552 HIS B ND1 
4264 C CD2 . HIS A 569 ? 0.9394 0.9394 0.9394 0.0000 0.0000 0.0000 552 HIS B CD2 
4265 C CE1 . HIS A 569 ? 0.9394 0.9394 0.9394 0.0000 0.0000 0.0000 552 HIS B CE1 
4266 N NE2 . HIS A 569 ? 0.9394 0.9394 0.9394 0.0000 0.0000 0.0000 552 HIS B NE2 
4267 N N   . TYR A 570 ? 0.9498 0.9498 0.9498 0.0000 0.0000 0.0000 553 TYR B N   
4268 C CA  . TYR A 570 ? 0.9498 0.9498 0.9498 0.0000 0.0000 0.0000 553 TYR B CA  
4269 C C   . TYR A 570 ? 0.9498 0.9498 0.9498 0.0000 0.0000 0.0000 553 TYR B C   
4270 O O   . TYR A 570 ? 0.9498 0.9498 0.9498 0.0000 0.0000 0.0000 553 TYR B O   
4271 C CB  . TYR A 570 ? 0.9498 0.9498 0.9498 0.0000 0.0000 0.0000 553 TYR B CB  
4272 C CG  . TYR A 570 ? 0.9498 0.9498 0.9498 0.0000 0.0000 0.0000 553 TYR B CG  
4273 C CD1 . TYR A 570 ? 0.9498 0.9498 0.9498 0.0000 0.0000 0.0000 553 TYR B CD1 
4274 C CD2 . TYR A 570 ? 0.9498 0.9498 0.9498 0.0000 0.0000 0.0000 553 TYR B CD2 
4275 C CE1 . TYR A 570 ? 0.9498 0.9498 0.9498 0.0000 0.0000 0.0000 553 TYR B CE1 
4276 C CE2 . TYR A 570 ? 0.9498 0.9498 0.9498 0.0000 0.0000 0.0000 553 TYR B CE2 
4277 C CZ  . TYR A 570 ? 0.9498 0.9498 0.9498 0.0000 0.0000 0.0000 553 TYR B CZ  
4278 O OH  . TYR A 570 ? 0.9498 0.9498 0.9498 0.0000 0.0000 0.0000 553 TYR B OH  
4279 N N   . LEU A 571 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 554 LEU B N   
4280 C CA  . LEU A 571 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 554 LEU B CA  
4281 C C   . LEU A 571 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 554 LEU B C   
4282 O O   . LEU A 571 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 554 LEU B O   
4283 C CB  . LEU A 571 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 554 LEU B CB  
4284 C CG  . LEU A 571 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 554 LEU B CG  
4285 C CD1 . LEU A 571 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 554 LEU B CD1 
4286 C CD2 . LEU A 571 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 554 LEU B CD2 
4287 N N   . ARG A 572 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 555 ARG B N   
4288 C CA  . ARG A 572 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 555 ARG B CA  
4289 C C   . ARG A 572 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 555 ARG B C   
4290 O O   . ARG A 572 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 555 ARG B O   
4291 C CB  . ARG A 572 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 555 ARG B CB  
4292 C CG  . ARG A 572 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 555 ARG B CG  
4293 C CD  . ARG A 572 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 555 ARG B CD  
4294 N NE  . ARG A 572 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 555 ARG B NE  
4295 C CZ  . ARG A 572 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 555 ARG B CZ  
4296 N NH1 . ARG A 572 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 555 ARG B NH1 
4297 N NH2 . ARG A 572 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 555 ARG B NH2 
4298 N N   . ALA A 573 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 556 ALA B N   
4299 C CA  . ALA A 573 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 556 ALA B CA  
4300 C C   . ALA A 573 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 556 ALA B C   
4301 O O   . ALA A 573 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 556 ALA B O   
4302 C CB  . ALA A 573 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 556 ALA B CB  
4303 N N   . GLN A 574 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 557 GLN B N   
4304 C CA  . GLN A 574 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 557 GLN B CA  
4305 C C   . GLN A 574 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 557 GLN B C   
4306 O O   . GLN A 574 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 557 GLN B O   
4307 C CB  . GLN A 574 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 557 GLN B CB  
4308 C CG  . GLN A 574 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 557 GLN B CG  
4309 C CD  . GLN A 574 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 557 GLN B CD  
4310 O OE1 . GLN A 574 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 557 GLN B OE1 
4311 N NE2 . GLN A 574 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 557 GLN B NE2 
4312 N N   . GLU A 575 ? 0.8916 0.8916 0.8916 0.0000 0.0000 0.0000 558 GLU B N   
4313 C CA  . GLU A 575 ? 0.8916 0.8916 0.8916 0.0000 0.0000 0.0000 558 GLU B CA  
4314 C C   . GLU A 575 ? 0.8916 0.8916 0.8916 0.0000 0.0000 0.0000 558 GLU B C   
4315 O O   . GLU A 575 ? 0.8916 0.8916 0.8916 0.0000 0.0000 0.0000 558 GLU B O   
4316 C CB  . GLU A 575 ? 0.8916 0.8916 0.8916 0.0000 0.0000 0.0000 558 GLU B CB  
4317 C CG  . GLU A 575 ? 0.8916 0.8916 0.8916 0.0000 0.0000 0.0000 558 GLU B CG  
4318 C CD  . GLU A 575 ? 0.8916 0.8916 0.8916 0.0000 0.0000 0.0000 558 GLU B CD  
4319 O OE1 . GLU A 575 ? 0.8916 0.8916 0.8916 0.0000 0.0000 0.0000 558 GLU B OE1 
4320 O OE2 . GLU A 575 ? 0.8916 0.8916 0.8916 0.0000 0.0000 0.0000 558 GLU B OE2 
4321 N N   . PHE A 576 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 559 PHE B N   
4322 C CA  . PHE A 576 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 559 PHE B CA  
4323 C C   . PHE A 576 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 559 PHE B C   
4324 O O   . PHE A 576 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 559 PHE B O   
4325 C CB  . PHE A 576 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 559 PHE B CB  
4326 C CG  . PHE A 576 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 559 PHE B CG  
4327 C CD1 . PHE A 576 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 559 PHE B CD1 
4328 C CD2 . PHE A 576 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 559 PHE B CD2 
4329 C CE1 . PHE A 576 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 559 PHE B CE1 
4330 C CE2 . PHE A 576 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 559 PHE B CE2 
4331 C CZ  . PHE A 576 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 559 PHE B CZ  
4332 N N   . GLU A 577 ? 1.0272 1.0272 1.0272 0.0000 0.0000 0.0000 560 GLU B N   
4333 C CA  . GLU A 577 ? 1.0272 1.0272 1.0272 0.0000 0.0000 0.0000 560 GLU B CA  
4334 C C   . GLU A 577 ? 1.0272 1.0272 1.0272 0.0000 0.0000 0.0000 560 GLU B C   
4335 O O   . GLU A 577 ? 1.0272 1.0272 1.0272 0.0000 0.0000 0.0000 560 GLU B O   
4336 C CB  . GLU A 577 ? 1.0272 1.0272 1.0272 0.0000 0.0000 0.0000 560 GLU B CB  
4337 C CG  . GLU A 577 ? 1.0272 1.0272 1.0272 0.0000 0.0000 0.0000 560 GLU B CG  
4338 C CD  . GLU A 577 ? 1.0272 1.0272 1.0272 0.0000 0.0000 0.0000 560 GLU B CD  
4339 O OE1 . GLU A 577 ? 1.0272 1.0272 1.0272 0.0000 0.0000 0.0000 560 GLU B OE1 
4340 O OE2 . GLU A 577 ? 1.0272 1.0272 1.0272 0.0000 0.0000 0.0000 560 GLU B OE2 
4341 N N   . HIS A 578 ? 1.0456 1.0456 1.0456 0.0000 0.0000 0.0000 561 HIS B N   
4342 C CA  . HIS A 578 ? 1.0456 1.0456 1.0456 0.0000 0.0000 0.0000 561 HIS B CA  
4343 C C   . HIS A 578 ? 1.0456 1.0456 1.0456 0.0000 0.0000 0.0000 561 HIS B C   
4344 O O   . HIS A 578 ? 1.0456 1.0456 1.0456 0.0000 0.0000 0.0000 561 HIS B O   
4345 C CB  . HIS A 578 ? 1.0456 1.0456 1.0456 0.0000 0.0000 0.0000 561 HIS B CB  
4346 C CG  . HIS A 578 ? 1.0456 1.0456 1.0456 0.0000 0.0000 0.0000 561 HIS B CG  
4347 N ND1 . HIS A 578 ? 1.0456 1.0456 1.0456 0.0000 0.0000 0.0000 561 HIS B ND1 
4348 C CD2 . HIS A 578 ? 1.0456 1.0456 1.0456 0.0000 0.0000 0.0000 561 HIS B CD2 
4349 C CE1 . HIS A 578 ? 1.0456 1.0456 1.0456 0.0000 0.0000 0.0000 561 HIS B CE1 
4350 N NE2 . HIS A 578 ? 1.0456 1.0456 1.0456 0.0000 0.0000 0.0000 561 HIS B NE2 
4351 N N   . GLY A 579 ? 1.0282 1.0282 1.0282 0.0000 0.0000 0.0000 562 GLY B N   
4352 C CA  . GLY A 579 ? 1.0282 1.0282 1.0282 0.0000 0.0000 0.0000 562 GLY B CA  
4353 C C   . GLY A 579 ? 1.0282 1.0282 1.0282 0.0000 0.0000 0.0000 562 GLY B C   
4354 O O   . GLY A 579 ? 1.0282 1.0282 1.0282 0.0000 0.0000 0.0000 562 GLY B O   
4355 N N   . LYS A 580 ? 1.0429 1.0429 1.0429 0.0000 0.0000 0.0000 563 LYS B N   
4356 C CA  . LYS A 580 ? 1.0429 1.0429 1.0429 0.0000 0.0000 0.0000 563 LYS B CA  
4357 C C   . LYS A 580 ? 1.0429 1.0429 1.0429 0.0000 0.0000 0.0000 563 LYS B C   
4358 O O   . LYS A 580 ? 1.0429 1.0429 1.0429 0.0000 0.0000 0.0000 563 LYS B O   
4359 C CB  . LYS A 580 ? 1.0429 1.0429 1.0429 0.0000 0.0000 0.0000 563 LYS B CB  
4360 C CG  . LYS A 580 ? 1.0429 1.0429 1.0429 0.0000 0.0000 0.0000 563 LYS B CG  
4361 C CD  . LYS A 580 ? 1.0429 1.0429 1.0429 0.0000 0.0000 0.0000 563 LYS B CD  
4362 C CE  . LYS A 580 ? 1.0429 1.0429 1.0429 0.0000 0.0000 0.0000 563 LYS B CE  
4363 N NZ  . LYS A 580 ? 1.0429 1.0429 1.0429 0.0000 0.0000 0.0000 563 LYS B NZ  
4364 N N   . SER A 581 ? 0.9479 0.9479 0.9479 0.0000 0.0000 0.0000 564 SER B N   
4365 C CA  . SER A 581 ? 0.9479 0.9479 0.9479 0.0000 0.0000 0.0000 564 SER B CA  
4366 C C   . SER A 581 ? 0.9479 0.9479 0.9479 0.0000 0.0000 0.0000 564 SER B C   
4367 O O   . SER A 581 ? 0.9479 0.9479 0.9479 0.0000 0.0000 0.0000 564 SER B O   
4368 C CB  . SER A 581 ? 0.9479 0.9479 0.9479 0.0000 0.0000 0.0000 564 SER B CB  
4369 O OG  . SER A 581 ? 0.9479 0.9479 0.9479 0.0000 0.0000 0.0000 564 SER B OG  
4370 N N   . ARG A 582 ? 0.9184 0.9184 0.9184 0.0000 0.0000 0.0000 565 ARG B N   
4371 C CA  . ARG A 582 ? 0.9184 0.9184 0.9184 0.0000 0.0000 0.0000 565 ARG B CA  
4372 C C   . ARG A 582 ? 0.9184 0.9184 0.9184 0.0000 0.0000 0.0000 565 ARG B C   
4373 O O   . ARG A 582 ? 0.9184 0.9184 0.9184 0.0000 0.0000 0.0000 565 ARG B O   
4374 C CB  . ARG A 582 ? 0.9184 0.9184 0.9184 0.0000 0.0000 0.0000 565 ARG B CB  
4375 C CG  . ARG A 582 ? 0.9184 0.9184 0.9184 0.0000 0.0000 0.0000 565 ARG B CG  
4376 C CD  . ARG A 582 ? 0.9184 0.9184 0.9184 0.0000 0.0000 0.0000 565 ARG B CD  
4377 N NE  . ARG A 582 ? 0.9184 0.9184 0.9184 0.0000 0.0000 0.0000 565 ARG B NE  
4378 C CZ  . ARG A 582 ? 0.9184 0.9184 0.9184 0.0000 0.0000 0.0000 565 ARG B CZ  
4379 N NH1 . ARG A 582 ? 0.9184 0.9184 0.9184 0.0000 0.0000 0.0000 565 ARG B NH1 
4380 N NH2 . ARG A 582 ? 0.9184 0.9184 0.9184 0.0000 0.0000 0.0000 565 ARG B NH2 
4381 N N   . ILE A 583 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 566 ILE B N   
4382 C CA  . ILE A 583 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 566 ILE B CA  
4383 C C   . ILE A 583 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 566 ILE B C   
4384 O O   . ILE A 583 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 566 ILE B O   
4385 C CB  . ILE A 583 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 566 ILE B CB  
4386 C CG1 . ILE A 583 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 566 ILE B CG1 
4387 C CG2 . ILE A 583 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 566 ILE B CG2 
4388 C CD1 . ILE A 583 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 566 ILE B CD1 
4389 N N   . ALA A 584 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 567 ALA B N   
4390 C CA  . ALA A 584 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 567 ALA B CA  
4391 C C   . ALA A 584 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 567 ALA B C   
4392 O O   . ALA A 584 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 567 ALA B O   
4393 C CB  . ALA A 584 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 567 ALA B CB  
4394 N N   . LEU A 585 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 568 LEU B N   
4395 C CA  . LEU A 585 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 568 LEU B CA  
4396 C C   . LEU A 585 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 568 LEU B C   
4397 O O   . LEU A 585 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 568 LEU B O   
4398 C CB  . LEU A 585 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 568 LEU B CB  
4399 C CG  . LEU A 585 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 568 LEU B CG  
4400 C CD1 . LEU A 585 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 568 LEU B CD1 
4401 C CD2 . LEU A 585 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 568 LEU B CD2 
4402 N N   . THR A 586 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 569 THR B N   
4403 C CA  . THR A 586 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 569 THR B CA  
4404 C C   . THR A 586 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 569 THR B C   
4405 O O   . THR A 586 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 569 THR B O   
4406 C CB  . THR A 586 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 569 THR B CB  
4407 O OG1 . THR A 586 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 569 THR B OG1 
4408 C CG2 . THR A 586 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 569 THR B CG2 
4409 N N   . ASN A 587 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 570 ASN B N   
4410 C CA  . ASN A 587 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 570 ASN B CA  
4411 C C   . ASN A 587 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 570 ASN B C   
4412 O O   . ASN A 587 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 570 ASN B O   
4413 C CB  . ASN A 587 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 570 ASN B CB  
4414 C CG  . ASN A 587 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 570 ASN B CG  
4415 O OD1 . ASN A 587 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 570 ASN B OD1 
4416 N ND2 . ASN A 587 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 570 ASN B ND2 
4417 N N   . SER A 588 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 571 SER B N   
4418 C CA  . SER A 588 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 571 SER B CA  
4419 C C   . SER A 588 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 571 SER B C   
4420 O O   . SER A 588 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 571 SER B O   
4421 C CB  . SER A 588 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 571 SER B CB  
4422 O OG  . SER A 588 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 571 SER B OG  
4423 N N   . VAL A 589 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 572 VAL B N   
4424 C CA  . VAL A 589 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 572 VAL B CA  
4425 C C   . VAL A 589 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 572 VAL B C   
4426 O O   . VAL A 589 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 572 VAL B O   
4427 C CB  . VAL A 589 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 572 VAL B CB  
4428 C CG1 . VAL A 589 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 572 VAL B CG1 
4429 C CG2 . VAL A 589 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 572 VAL B CG2 
4430 N N   . ASN A 590 ? 0.9291 0.9291 0.9291 0.0000 0.0000 0.0000 573 ASN B N   
4431 C CA  . ASN A 590 ? 0.9291 0.9291 0.9291 0.0000 0.0000 0.0000 573 ASN B CA  
4432 C C   . ASN A 590 ? 0.9291 0.9291 0.9291 0.0000 0.0000 0.0000 573 ASN B C   
4433 O O   . ASN A 590 ? 0.9291 0.9291 0.9291 0.0000 0.0000 0.0000 573 ASN B O   
4434 C CB  . ASN A 590 ? 0.9291 0.9291 0.9291 0.0000 0.0000 0.0000 573 ASN B CB  
4435 C CG  . ASN A 590 ? 0.9291 0.9291 0.9291 0.0000 0.0000 0.0000 573 ASN B CG  
4436 O OD1 . ASN A 590 ? 0.9291 0.9291 0.9291 0.0000 0.0000 0.0000 573 ASN B OD1 
4437 N ND2 . ASN A 590 ? 0.9291 0.9291 0.9291 0.0000 0.0000 0.0000 573 ASN B ND2 
4438 N N   . GLU A 591 ? 0.9036 0.9036 0.9036 0.0000 0.0000 0.0000 574 GLU B N   
4439 C CA  . GLU A 591 ? 0.9036 0.9036 0.9036 0.0000 0.0000 0.0000 574 GLU B CA  
4440 C C   . GLU A 591 ? 0.9036 0.9036 0.9036 0.0000 0.0000 0.0000 574 GLU B C   
4441 O O   . GLU A 591 ? 0.9036 0.9036 0.9036 0.0000 0.0000 0.0000 574 GLU B O   
4442 C CB  . GLU A 591 ? 0.9036 0.9036 0.9036 0.0000 0.0000 0.0000 574 GLU B CB  
4443 C CG  . GLU A 591 ? 0.9036 0.9036 0.9036 0.0000 0.0000 0.0000 574 GLU B CG  
4444 C CD  . GLU A 591 ? 0.9036 0.9036 0.9036 0.0000 0.0000 0.0000 574 GLU B CD  
4445 O OE1 . GLU A 591 ? 0.9036 0.9036 0.9036 0.0000 0.0000 0.0000 574 GLU B OE1 
4446 O OE2 . GLU A 591 ? 0.9036 0.9036 0.9036 0.0000 0.0000 0.0000 574 GLU B OE2 
4447 N N   . ALA A 592 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 575 ALA B N   
4448 C CA  . ALA A 592 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 575 ALA B CA  
4449 C C   . ALA A 592 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 575 ALA B C   
4450 O O   . ALA A 592 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 575 ALA B O   
4451 C CB  . ALA A 592 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 575 ALA B CB  
4452 N N   . LEU A 593 ? 0.8834 0.8834 0.8834 0.0000 0.0000 0.0000 576 LEU B N   
4453 C CA  . LEU A 593 ? 0.8834 0.8834 0.8834 0.0000 0.0000 0.0000 576 LEU B CA  
4454 C C   . LEU A 593 ? 0.8834 0.8834 0.8834 0.0000 0.0000 0.0000 576 LEU B C   
4455 O O   . LEU A 593 ? 0.8834 0.8834 0.8834 0.0000 0.0000 0.0000 576 LEU B O   
4456 C CB  . LEU A 593 ? 0.8834 0.8834 0.8834 0.0000 0.0000 0.0000 576 LEU B CB  
4457 C CG  . LEU A 593 ? 0.8834 0.8834 0.8834 0.0000 0.0000 0.0000 576 LEU B CG  
4458 C CD1 . LEU A 593 ? 0.8834 0.8834 0.8834 0.0000 0.0000 0.0000 576 LEU B CD1 
4459 C CD2 . LEU A 593 ? 0.8834 0.8834 0.8834 0.0000 0.0000 0.0000 576 LEU B CD2 
4460 N N   . LEU A 594 ? 0.9147 0.9147 0.9147 0.0000 0.0000 0.0000 577 LEU B N   
4461 C CA  . LEU A 594 ? 0.9147 0.9147 0.9147 0.0000 0.0000 0.0000 577 LEU B CA  
4462 C C   . LEU A 594 ? 0.9147 0.9147 0.9147 0.0000 0.0000 0.0000 577 LEU B C   
4463 O O   . LEU A 594 ? 0.9147 0.9147 0.9147 0.0000 0.0000 0.0000 577 LEU B O   
4464 C CB  . LEU A 594 ? 0.9147 0.9147 0.9147 0.0000 0.0000 0.0000 577 LEU B CB  
4465 C CG  . LEU A 594 ? 0.9147 0.9147 0.9147 0.0000 0.0000 0.0000 577 LEU B CG  
4466 C CD1 . LEU A 594 ? 0.9147 0.9147 0.9147 0.0000 0.0000 0.0000 577 LEU B CD1 
4467 C CD2 . LEU A 594 ? 0.9147 0.9147 0.9147 0.0000 0.0000 0.0000 577 LEU B CD2 
4468 N N   . ASN A 595 ? 0.9014 0.9014 0.9014 0.0000 0.0000 0.0000 578 ASN B N   
4469 C CA  . ASN A 595 ? 0.9014 0.9014 0.9014 0.0000 0.0000 0.0000 578 ASN B CA  
4470 C C   . ASN A 595 ? 0.9014 0.9014 0.9014 0.0000 0.0000 0.0000 578 ASN B C   
4471 O O   . ASN A 595 ? 0.9014 0.9014 0.9014 0.0000 0.0000 0.0000 578 ASN B O   
4472 C CB  . ASN A 595 ? 0.9014 0.9014 0.9014 0.0000 0.0000 0.0000 578 ASN B CB  
4473 C CG  . ASN A 595 ? 0.9014 0.9014 0.9014 0.0000 0.0000 0.0000 578 ASN B CG  
4474 O OD1 . ASN A 595 ? 0.9014 0.9014 0.9014 0.0000 0.0000 0.0000 578 ASN B OD1 
4475 N ND2 . ASN A 595 ? 0.9014 0.9014 0.9014 0.0000 0.0000 0.0000 578 ASN B ND2 
4476 N N   . PRO A 596 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 579 PRO B N   
4477 C CA  . PRO A 596 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 579 PRO B CA  
4478 C C   . PRO A 596 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 579 PRO B C   
4479 O O   . PRO A 596 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 579 PRO B O   
4480 C CB  . PRO A 596 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 579 PRO B CB  
4481 C CG  . PRO A 596 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 579 PRO B CG  
4482 C CD  . PRO A 596 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 579 PRO B CD  
4483 N N   . SER A 597 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 580 SER B N   
4484 C CA  . SER A 597 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 580 SER B CA  
4485 C C   . SER A 597 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 580 SER B C   
4486 O O   . SER A 597 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 580 SER B O   
4487 C CB  . SER A 597 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 580 SER B CB  
4488 O OG  . SER A 597 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 580 SER B OG  
4489 N N   . ARG A 598 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 581 ARG B N   
4490 C CA  . ARG A 598 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 581 ARG B CA  
4491 C C   . ARG A 598 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 581 ARG B C   
4492 O O   . ARG A 598 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 581 ARG B O   
4493 C CB  . ARG A 598 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 581 ARG B CB  
4494 C CG  . ARG A 598 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 581 ARG B CG  
4495 C CD  . ARG A 598 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 581 ARG B CD  
4496 N NE  . ARG A 598 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 581 ARG B NE  
4497 C CZ  . ARG A 598 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 581 ARG B CZ  
4498 N NH1 . ARG A 598 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 581 ARG B NH1 
4499 N NH2 . ARG A 598 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 581 ARG B NH2 
4500 N N   . VAL A 599 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 582 VAL B N   
4501 C CA  . VAL A 599 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 582 VAL B CA  
4502 C C   . VAL A 599 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 582 VAL B C   
4503 O O   . VAL A 599 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 582 VAL B O   
4504 C CB  . VAL A 599 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 582 VAL B CB  
4505 C CG1 . VAL A 599 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 582 VAL B CG1 
4506 C CG2 . VAL A 599 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 582 VAL B CG2 
4507 N N   . TYR A 600 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 583 TYR B N   
4508 C CA  . TYR A 600 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 583 TYR B CA  
4509 C C   . TYR A 600 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 583 TYR B C   
4510 O O   . TYR A 600 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 583 TYR B O   
4511 C CB  . TYR A 600 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 583 TYR B CB  
4512 C CG  . TYR A 600 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 583 TYR B CG  
4513 C CD1 . TYR A 600 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 583 TYR B CD1 
4514 C CD2 . TYR A 600 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 583 TYR B CD2 
4515 C CE1 . TYR A 600 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 583 TYR B CE1 
4516 C CE2 . TYR A 600 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 583 TYR B CE2 
4517 C CZ  . TYR A 600 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 583 TYR B CZ  
4518 O OH  . TYR A 600 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 583 TYR B OH  
4519 N N   . THR A 601 ? 0.9164 0.9164 0.9164 0.0000 0.0000 0.0000 584 THR B N   
4520 C CA  . THR A 601 ? 0.9164 0.9164 0.9164 0.0000 0.0000 0.0000 584 THR B CA  
4521 C C   . THR A 601 ? 0.9164 0.9164 0.9164 0.0000 0.0000 0.0000 584 THR B C   
4522 O O   . THR A 601 ? 0.9164 0.9164 0.9164 0.0000 0.0000 0.0000 584 THR B O   
4523 C CB  . THR A 601 ? 0.9164 0.9164 0.9164 0.0000 0.0000 0.0000 584 THR B CB  
4524 O OG1 . THR A 601 ? 0.9164 0.9164 0.9164 0.0000 0.0000 0.0000 584 THR B OG1 
4525 C CG2 . THR A 601 ? 0.9164 0.9164 0.9164 0.0000 0.0000 0.0000 584 THR B CG2 
4526 N N   . PHE A 602 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 585 PHE B N   
4527 C CA  . PHE A 602 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 585 PHE B CA  
4528 C C   . PHE A 602 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 585 PHE B C   
4529 O O   . PHE A 602 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 585 PHE B O   
4530 C CB  . PHE A 602 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 585 PHE B CB  
4531 C CG  . PHE A 602 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 585 PHE B CG  
4532 C CD1 . PHE A 602 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 585 PHE B CD1 
4533 C CD2 . PHE A 602 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 585 PHE B CD2 
4534 C CE1 . PHE A 602 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 585 PHE B CE1 
4535 C CE2 . PHE A 602 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 585 PHE B CE2 
4536 C CZ  . PHE A 602 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 585 PHE B CZ  
4537 N N   . PHE A 603 ? 0.9995 0.9995 0.9995 0.0000 0.0000 0.0000 586 PHE B N   
4538 C CA  . PHE A 603 ? 0.9995 0.9995 0.9995 0.0000 0.0000 0.0000 586 PHE B CA  
4539 C C   . PHE A 603 ? 0.9995 0.9995 0.9995 0.0000 0.0000 0.0000 586 PHE B C   
4540 O O   . PHE A 603 ? 0.9995 0.9995 0.9995 0.0000 0.0000 0.0000 586 PHE B O   
4541 C CB  . PHE A 603 ? 0.9995 0.9995 0.9995 0.0000 0.0000 0.0000 586 PHE B CB  
4542 C CG  . PHE A 603 ? 0.9995 0.9995 0.9995 0.0000 0.0000 0.0000 586 PHE B CG  
4543 C CD1 . PHE A 603 ? 0.9995 0.9995 0.9995 0.0000 0.0000 0.0000 586 PHE B CD1 
4544 C CD2 . PHE A 603 ? 0.9995 0.9995 0.9995 0.0000 0.0000 0.0000 586 PHE B CD2 
4545 C CE1 . PHE A 603 ? 0.9995 0.9995 0.9995 0.0000 0.0000 0.0000 586 PHE B CE1 
4546 C CE2 . PHE A 603 ? 0.9995 0.9995 0.9995 0.0000 0.0000 0.0000 586 PHE B CE2 
4547 C CZ  . PHE A 603 ? 0.9995 0.9995 0.9995 0.0000 0.0000 0.0000 586 PHE B CZ  
4548 N N   . SER A 604 ? 1.0653 1.0653 1.0653 0.0000 0.0000 0.0000 587 SER B N   
4549 C CA  . SER A 604 ? 1.0653 1.0653 1.0653 0.0000 0.0000 0.0000 587 SER B CA  
4550 C C   . SER A 604 ? 1.0653 1.0653 1.0653 0.0000 0.0000 0.0000 587 SER B C   
4551 O O   . SER A 604 ? 1.0653 1.0653 1.0653 0.0000 0.0000 0.0000 587 SER B O   
4552 C CB  . SER A 604 ? 1.0653 1.0653 1.0653 0.0000 0.0000 0.0000 587 SER B CB  
4553 O OG  . SER A 604 ? 1.0653 1.0653 1.0653 0.0000 0.0000 0.0000 587 SER B OG  
4554 N N   . SER A 605 ? 1.0314 1.0314 1.0314 0.0000 0.0000 0.0000 588 SER B N   
4555 C CA  . SER A 605 ? 1.0314 1.0314 1.0314 0.0000 0.0000 0.0000 588 SER B CA  
4556 C C   . SER A 605 ? 1.0314 1.0314 1.0314 0.0000 0.0000 0.0000 588 SER B C   
4557 O O   . SER A 605 ? 1.0314 1.0314 1.0314 0.0000 0.0000 0.0000 588 SER B O   
4558 C CB  . SER A 605 ? 1.0314 1.0314 1.0314 0.0000 0.0000 0.0000 588 SER B CB  
4559 O OG  . SER A 605 ? 1.0314 1.0314 1.0314 0.0000 0.0000 0.0000 588 SER B OG  
4560 N N   . ASP A 606 ? 1.0727 1.0727 1.0727 0.0000 0.0000 0.0000 589 ASP B N   
4561 C CA  . ASP A 606 ? 1.0727 1.0727 1.0727 0.0000 0.0000 0.0000 589 ASP B CA  
4562 C C   . ASP A 606 ? 1.0727 1.0727 1.0727 0.0000 0.0000 0.0000 589 ASP B C   
4563 O O   . ASP A 606 ? 1.0727 1.0727 1.0727 0.0000 0.0000 0.0000 589 ASP B O   
4564 C CB  . ASP A 606 ? 1.0727 1.0727 1.0727 0.0000 0.0000 0.0000 589 ASP B CB  
4565 C CG  . ASP A 606 ? 1.0727 1.0727 1.0727 0.0000 0.0000 0.0000 589 ASP B CG  
4566 O OD1 . ASP A 606 ? 1.0727 1.0727 1.0727 0.0000 0.0000 0.0000 589 ASP B OD1 
4567 O OD2 . ASP A 606 ? 1.0727 1.0727 1.0727 0.0000 0.0000 0.0000 589 ASP B OD2 
4568 N N   . TYR A 607 ? 1.0379 1.0379 1.0379 0.0000 0.0000 0.0000 590 TYR B N   
4569 C CA  . TYR A 607 ? 1.0379 1.0379 1.0379 0.0000 0.0000 0.0000 590 TYR B CA  
4570 C C   . TYR A 607 ? 1.0379 1.0379 1.0379 0.0000 0.0000 0.0000 590 TYR B C   
4571 O O   . TYR A 607 ? 1.0379 1.0379 1.0379 0.0000 0.0000 0.0000 590 TYR B O   
4572 C CB  . TYR A 607 ? 1.0379 1.0379 1.0379 0.0000 0.0000 0.0000 590 TYR B CB  
4573 C CG  . TYR A 607 ? 1.0379 1.0379 1.0379 0.0000 0.0000 0.0000 590 TYR B CG  
4574 C CD1 . TYR A 607 ? 1.0379 1.0379 1.0379 0.0000 0.0000 0.0000 590 TYR B CD1 
4575 C CD2 . TYR A 607 ? 1.0379 1.0379 1.0379 0.0000 0.0000 0.0000 590 TYR B CD2 
4576 C CE1 . TYR A 607 ? 1.0379 1.0379 1.0379 0.0000 0.0000 0.0000 590 TYR B CE1 
4577 C CE2 . TYR A 607 ? 1.0379 1.0379 1.0379 0.0000 0.0000 0.0000 590 TYR B CE2 
4578 C CZ  . TYR A 607 ? 1.0379 1.0379 1.0379 0.0000 0.0000 0.0000 590 TYR B CZ  
4579 O OH  . TYR A 607 ? 1.0379 1.0379 1.0379 0.0000 0.0000 0.0000 590 TYR B OH  
4580 N N   . VAL A 608 ? 0.9572 0.9572 0.9572 0.0000 0.0000 0.0000 591 VAL B N   
4581 C CA  . VAL A 608 ? 0.9572 0.9572 0.9572 0.0000 0.0000 0.0000 591 VAL B CA  
4582 C C   . VAL A 608 ? 0.9572 0.9572 0.9572 0.0000 0.0000 0.0000 591 VAL B C   
4583 O O   . VAL A 608 ? 0.9572 0.9572 0.9572 0.0000 0.0000 0.0000 591 VAL B O   
4584 C CB  . VAL A 608 ? 0.9572 0.9572 0.9572 0.0000 0.0000 0.0000 591 VAL B CB  
4585 C CG1 . VAL A 608 ? 0.9572 0.9572 0.9572 0.0000 0.0000 0.0000 591 VAL B CG1 
4586 C CG2 . VAL A 608 ? 0.9572 0.9572 0.9572 0.0000 0.0000 0.0000 591 VAL B CG2 
4587 N N   . LYS A 609 ? 0.9870 0.9870 0.9870 0.0000 0.0000 0.0000 592 LYS B N   
4588 C CA  . LYS A 609 ? 0.9870 0.9870 0.9870 0.0000 0.0000 0.0000 592 LYS B CA  
4589 C C   . LYS A 609 ? 0.9870 0.9870 0.9870 0.0000 0.0000 0.0000 592 LYS B C   
4590 O O   . LYS A 609 ? 0.9870 0.9870 0.9870 0.0000 0.0000 0.0000 592 LYS B O   
4591 C CB  . LYS A 609 ? 0.9870 0.9870 0.9870 0.0000 0.0000 0.0000 592 LYS B CB  
4592 C CG  . LYS A 609 ? 0.9870 0.9870 0.9870 0.0000 0.0000 0.0000 592 LYS B CG  
4593 C CD  . LYS A 609 ? 0.9870 0.9870 0.9870 0.0000 0.0000 0.0000 592 LYS B CD  
4594 C CE  . LYS A 609 ? 0.9870 0.9870 0.9870 0.0000 0.0000 0.0000 592 LYS B CE  
4595 N NZ  . LYS A 609 ? 0.9870 0.9870 0.9870 0.0000 0.0000 0.0000 592 LYS B NZ  
4596 N N   . LYS A 610 ? 0.9768 0.9768 0.9768 0.0000 0.0000 0.0000 593 LYS B N   
4597 C CA  . LYS A 610 ? 0.9768 0.9768 0.9768 0.0000 0.0000 0.0000 593 LYS B CA  
4598 C C   . LYS A 610 ? 0.9768 0.9768 0.9768 0.0000 0.0000 0.0000 593 LYS B C   
4599 O O   . LYS A 610 ? 0.9768 0.9768 0.9768 0.0000 0.0000 0.0000 593 LYS B O   
4600 C CB  . LYS A 610 ? 0.9768 0.9768 0.9768 0.0000 0.0000 0.0000 593 LYS B CB  
4601 C CG  . LYS A 610 ? 0.9768 0.9768 0.9768 0.0000 0.0000 0.0000 593 LYS B CG  
4602 C CD  . LYS A 610 ? 0.9768 0.9768 0.9768 0.0000 0.0000 0.0000 593 LYS B CD  
4603 C CE  . LYS A 610 ? 0.9768 0.9768 0.9768 0.0000 0.0000 0.0000 593 LYS B CE  
4604 N NZ  . LYS A 610 ? 0.9768 0.9768 0.9768 0.0000 0.0000 0.0000 593 LYS B NZ  
4605 N N   . VAL A 611 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 594 VAL B N   
4606 C CA  . VAL A 611 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 594 VAL B CA  
4607 C C   . VAL A 611 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 594 VAL B C   
4608 O O   . VAL A 611 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 594 VAL B O   
4609 C CB  . VAL A 611 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 594 VAL B CB  
4610 C CG1 . VAL A 611 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 594 VAL B CG1 
4611 C CG2 . VAL A 611 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 594 VAL B CG2 
4612 N N   . ASN A 612 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 595 ASN B N   
4613 C CA  . ASN A 612 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 595 ASN B CA  
4614 C C   . ASN A 612 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 595 ASN B C   
4615 O O   . ASN A 612 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 595 ASN B O   
4616 C CB  . ASN A 612 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 595 ASN B CB  
4617 C CG  . ASN A 612 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 595 ASN B CG  
4618 O OD1 . ASN A 612 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 595 ASN B OD1 
4619 N ND2 . ASN A 612 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 595 ASN B ND2 
4620 N N   . LYS A 613 ? 0.9392 0.9392 0.9392 0.0000 0.0000 0.0000 596 LYS B N   
4621 C CA  . LYS A 613 ? 0.9392 0.9392 0.9392 0.0000 0.0000 0.0000 596 LYS B CA  
4622 C C   . LYS A 613 ? 0.9392 0.9392 0.9392 0.0000 0.0000 0.0000 596 LYS B C   
4623 O O   . LYS A 613 ? 0.9392 0.9392 0.9392 0.0000 0.0000 0.0000 596 LYS B O   
4624 C CB  . LYS A 613 ? 0.9392 0.9392 0.9392 0.0000 0.0000 0.0000 596 LYS B CB  
4625 C CG  . LYS A 613 ? 0.9392 0.9392 0.9392 0.0000 0.0000 0.0000 596 LYS B CG  
4626 C CD  . LYS A 613 ? 0.9392 0.9392 0.9392 0.0000 0.0000 0.0000 596 LYS B CD  
4627 C CE  . LYS A 613 ? 0.9392 0.9392 0.9392 0.0000 0.0000 0.0000 596 LYS B CE  
4628 N NZ  . LYS A 613 ? 0.9392 0.9392 0.9392 0.0000 0.0000 0.0000 596 LYS B NZ  
4629 N N   . ALA A 614 ? 0.9527 0.9527 0.9527 0.0000 0.0000 0.0000 597 ALA B N   
4630 C CA  . ALA A 614 ? 0.9527 0.9527 0.9527 0.0000 0.0000 0.0000 597 ALA B CA  
4631 C C   . ALA A 614 ? 0.9527 0.9527 0.9527 0.0000 0.0000 0.0000 597 ALA B C   
4632 O O   . ALA A 614 ? 0.9527 0.9527 0.9527 0.0000 0.0000 0.0000 597 ALA B O   
4633 C CB  . ALA A 614 ? 0.9527 0.9527 0.9527 0.0000 0.0000 0.0000 597 ALA B CB  
4634 N N   . THR A 615 ? 0.9637 0.9637 0.9637 0.0000 0.0000 0.0000 598 THR B N   
4635 C CA  . THR A 615 ? 0.9637 0.9637 0.9637 0.0000 0.0000 0.0000 598 THR B CA  
4636 C C   . THR A 615 ? 0.9637 0.9637 0.9637 0.0000 0.0000 0.0000 598 THR B C   
4637 O O   . THR A 615 ? 0.9637 0.9637 0.9637 0.0000 0.0000 0.0000 598 THR B O   
4638 C CB  . THR A 615 ? 0.9637 0.9637 0.9637 0.0000 0.0000 0.0000 598 THR B CB  
4639 O OG1 . THR A 615 ? 0.9637 0.9637 0.9637 0.0000 0.0000 0.0000 598 THR B OG1 
4640 C CG2 . THR A 615 ? 0.9637 0.9637 0.9637 0.0000 0.0000 0.0000 598 THR B CG2 
4641 N N   . GLU A 616 ? 1.0173 1.0173 1.0173 0.0000 0.0000 0.0000 599 GLU B N   
4642 C CA  . GLU A 616 ? 1.0173 1.0173 1.0173 0.0000 0.0000 0.0000 599 GLU B CA  
4643 C C   . GLU A 616 ? 1.0173 1.0173 1.0173 0.0000 0.0000 0.0000 599 GLU B C   
4644 O O   . GLU A 616 ? 1.0173 1.0173 1.0173 0.0000 0.0000 0.0000 599 GLU B O   
4645 C CB  . GLU A 616 ? 1.0173 1.0173 1.0173 0.0000 0.0000 0.0000 599 GLU B CB  
4646 C CG  . GLU A 616 ? 1.0173 1.0173 1.0173 0.0000 0.0000 0.0000 599 GLU B CG  
4647 C CD  . GLU A 616 ? 1.0173 1.0173 1.0173 0.0000 0.0000 0.0000 599 GLU B CD  
4648 O OE1 . GLU A 616 ? 1.0173 1.0173 1.0173 0.0000 0.0000 0.0000 599 GLU B OE1 
4649 O OE2 . GLU A 616 ? 1.0173 1.0173 1.0173 0.0000 0.0000 0.0000 599 GLU B OE2 
4650 N N   . ALA A 617 ? 1.0520 1.0520 1.0520 0.0000 0.0000 0.0000 600 ALA B N   
4651 C CA  . ALA A 617 ? 1.0520 1.0520 1.0520 0.0000 0.0000 0.0000 600 ALA B CA  
4652 C C   . ALA A 617 ? 1.0520 1.0520 1.0520 0.0000 0.0000 0.0000 600 ALA B C   
4653 O O   . ALA A 617 ? 1.0520 1.0520 1.0520 0.0000 0.0000 0.0000 600 ALA B O   
4654 C CB  . ALA A 617 ? 1.0520 1.0520 1.0520 0.0000 0.0000 0.0000 600 ALA B CB  
4655 N N   . ALA A 618 ? 1.0439 1.0439 1.0439 0.0000 0.0000 0.0000 601 ALA B N   
4656 C CA  . ALA A 618 ? 1.0439 1.0439 1.0439 0.0000 0.0000 0.0000 601 ALA B CA  
4657 C C   . ALA A 618 ? 1.0439 1.0439 1.0439 0.0000 0.0000 0.0000 601 ALA B C   
4658 O O   . ALA A 618 ? 1.0439 1.0439 1.0439 0.0000 0.0000 0.0000 601 ALA B O   
4659 C CB  . ALA A 618 ? 1.0439 1.0439 1.0439 0.0000 0.0000 0.0000 601 ALA B CB  
4660 N N   . MET A 619 ? 1.0644 1.0644 1.0644 0.0000 0.0000 0.0000 602 MET B N   
4661 C CA  . MET A 619 ? 1.0644 1.0644 1.0644 0.0000 0.0000 0.0000 602 MET B CA  
4662 C C   . MET A 619 ? 1.0644 1.0644 1.0644 0.0000 0.0000 0.0000 602 MET B C   
4663 O O   . MET A 619 ? 1.0644 1.0644 1.0644 0.0000 0.0000 0.0000 602 MET B O   
4664 C CB  . MET A 619 ? 1.0644 1.0644 1.0644 0.0000 0.0000 0.0000 602 MET B CB  
4665 C CG  . MET A 619 ? 1.0644 1.0644 1.0644 0.0000 0.0000 0.0000 602 MET B CG  
4666 S SD  . MET A 619 ? 1.0644 1.0644 1.0644 0.0000 0.0000 0.0000 602 MET B SD  
4667 C CE  . MET A 619 ? 1.0644 1.0644 1.0644 0.0000 0.0000 0.0000 602 MET B CE  
4668 N N   . PHE A 620 ? 1.0410 1.0410 1.0410 0.0000 0.0000 0.0000 603 PHE B N   
4669 C CA  . PHE A 620 ? 1.0410 1.0410 1.0410 0.0000 0.0000 0.0000 603 PHE B CA  
4670 C C   . PHE A 620 ? 1.0410 1.0410 1.0410 0.0000 0.0000 0.0000 603 PHE B C   
4671 O O   . PHE A 620 ? 1.0410 1.0410 1.0410 0.0000 0.0000 0.0000 603 PHE B O   
4672 C CB  . PHE A 620 ? 1.0410 1.0410 1.0410 0.0000 0.0000 0.0000 603 PHE B CB  
4673 C CG  . PHE A 620 ? 1.0410 1.0410 1.0410 0.0000 0.0000 0.0000 603 PHE B CG  
4674 C CD1 . PHE A 620 ? 1.0410 1.0410 1.0410 0.0000 0.0000 0.0000 603 PHE B CD1 
4675 C CD2 . PHE A 620 ? 1.0410 1.0410 1.0410 0.0000 0.0000 0.0000 603 PHE B CD2 
4676 C CE1 . PHE A 620 ? 1.0410 1.0410 1.0410 0.0000 0.0000 0.0000 603 PHE B CE1 
4677 C CE2 . PHE A 620 ? 1.0410 1.0410 1.0410 0.0000 0.0000 0.0000 603 PHE B CE2 
4678 C CZ  . PHE A 620 ? 1.0410 1.0410 1.0410 0.0000 0.0000 0.0000 603 PHE B CZ  
4679 N N   . LEU A 621 ? 1.0676 1.0676 1.0676 0.0000 0.0000 0.0000 604 LEU B N   
4680 C CA  . LEU A 621 ? 1.0676 1.0676 1.0676 0.0000 0.0000 0.0000 604 LEU B CA  
4681 C C   . LEU A 621 ? 1.0676 1.0676 1.0676 0.0000 0.0000 0.0000 604 LEU B C   
4682 O O   . LEU A 621 ? 1.0676 1.0676 1.0676 0.0000 0.0000 0.0000 604 LEU B O   
4683 C CB  . LEU A 621 ? 1.0676 1.0676 1.0676 0.0000 0.0000 0.0000 604 LEU B CB  
4684 C CG  . LEU A 621 ? 1.0676 1.0676 1.0676 0.0000 0.0000 0.0000 604 LEU B CG  
4685 C CD1 . LEU A 621 ? 1.0676 1.0676 1.0676 0.0000 0.0000 0.0000 604 LEU B CD1 
4686 C CD2 . LEU A 621 ? 1.0676 1.0676 1.0676 0.0000 0.0000 0.0000 604 LEU B CD2 
4687 N N   . GLY A 622 ? 1.0624 1.0624 1.0624 0.0000 0.0000 0.0000 605 GLY B N   
4688 C CA  . GLY A 622 ? 1.0624 1.0624 1.0624 0.0000 0.0000 0.0000 605 GLY B CA  
4689 C C   . GLY A 622 ? 1.0624 1.0624 1.0624 0.0000 0.0000 0.0000 605 GLY B C   
4690 O O   . GLY A 622 ? 1.0624 1.0624 1.0624 0.0000 0.0000 0.0000 605 GLY B O   
4691 N N   . TRP A 623 ? 1.0206 1.0206 1.0206 0.0000 0.0000 0.0000 606 TRP B N   
4692 C CA  . TRP A 623 ? 1.0206 1.0206 1.0206 0.0000 0.0000 0.0000 606 TRP B CA  
4693 C C   . TRP A 623 ? 1.0206 1.0206 1.0206 0.0000 0.0000 0.0000 606 TRP B C   
4694 O O   . TRP A 623 ? 1.0206 1.0206 1.0206 0.0000 0.0000 0.0000 606 TRP B O   
4695 C CB  . TRP A 623 ? 1.0206 1.0206 1.0206 0.0000 0.0000 0.0000 606 TRP B CB  
4696 C CG  . TRP A 623 ? 1.0206 1.0206 1.0206 0.0000 0.0000 0.0000 606 TRP B CG  
4697 C CD1 . TRP A 623 ? 1.0206 1.0206 1.0206 0.0000 0.0000 0.0000 606 TRP B CD1 
4698 C CD2 . TRP A 623 ? 1.0206 1.0206 1.0206 0.0000 0.0000 0.0000 606 TRP B CD2 
4699 N NE1 . TRP A 623 ? 1.0206 1.0206 1.0206 0.0000 0.0000 0.0000 606 TRP B NE1 
4700 C CE2 . TRP A 623 ? 1.0206 1.0206 1.0206 0.0000 0.0000 0.0000 606 TRP B CE2 
4701 C CE3 . TRP A 623 ? 1.0206 1.0206 1.0206 0.0000 0.0000 0.0000 606 TRP B CE3 
4702 C CZ2 . TRP A 623 ? 1.0206 1.0206 1.0206 0.0000 0.0000 0.0000 606 TRP B CZ2 
4703 C CZ3 . TRP A 623 ? 1.0206 1.0206 1.0206 0.0000 0.0000 0.0000 606 TRP B CZ3 
4704 C CH2 . TRP A 623 ? 1.0206 1.0206 1.0206 0.0000 0.0000 0.0000 606 TRP B CH2 
4705 N N   . VAL A 624 ? 1.0326 1.0326 1.0326 0.0000 0.0000 0.0000 607 VAL B N   
4706 C CA  . VAL A 624 ? 1.0326 1.0326 1.0326 0.0000 0.0000 0.0000 607 VAL B CA  
4707 C C   . VAL A 624 ? 1.0326 1.0326 1.0326 0.0000 0.0000 0.0000 607 VAL B C   
4708 O O   . VAL A 624 ? 1.0326 1.0326 1.0326 0.0000 0.0000 0.0000 607 VAL B O   
4709 C CB  . VAL A 624 ? 1.0326 1.0326 1.0326 0.0000 0.0000 0.0000 607 VAL B CB  
4710 C CG1 . VAL A 624 ? 1.0326 1.0326 1.0326 0.0000 0.0000 0.0000 607 VAL B CG1 
4711 C CG2 . VAL A 624 ? 1.0326 1.0326 1.0326 0.0000 0.0000 0.0000 607 VAL B CG2 
4712 N N   . GLU A 625 ? 1.1329 1.1329 1.1329 0.0000 0.0000 0.0000 608 GLU B N   
4713 C CA  . GLU A 625 ? 1.1329 1.1329 1.1329 0.0000 0.0000 0.0000 608 GLU B CA  
4714 C C   . GLU A 625 ? 1.1329 1.1329 1.1329 0.0000 0.0000 0.0000 608 GLU B C   
4715 O O   . GLU A 625 ? 1.1329 1.1329 1.1329 0.0000 0.0000 0.0000 608 GLU B O   
4716 C CB  . GLU A 625 ? 1.1329 1.1329 1.1329 0.0000 0.0000 0.0000 608 GLU B CB  
4717 C CG  . GLU A 625 ? 1.1329 1.1329 1.1329 0.0000 0.0000 0.0000 608 GLU B CG  
4718 C CD  . GLU A 625 ? 1.1329 1.1329 1.1329 0.0000 0.0000 0.0000 608 GLU B CD  
4719 O OE1 . GLU A 625 ? 1.1329 1.1329 1.1329 0.0000 0.0000 0.0000 608 GLU B OE1 
4720 O OE2 . GLU A 625 ? 1.1329 1.1329 1.1329 0.0000 0.0000 0.0000 608 GLU B OE2 
4721 N N   . GLN A 626 ? 1.0956 1.0956 1.0956 0.0000 0.0000 0.0000 609 GLN B N   
4722 C CA  . GLN A 626 ? 1.0956 1.0956 1.0956 0.0000 0.0000 0.0000 609 GLN B CA  
4723 C C   . GLN A 626 ? 1.0956 1.0956 1.0956 0.0000 0.0000 0.0000 609 GLN B C   
4724 O O   . GLN A 626 ? 1.0956 1.0956 1.0956 0.0000 0.0000 0.0000 609 GLN B O   
4725 C CB  . GLN A 626 ? 1.0956 1.0956 1.0956 0.0000 0.0000 0.0000 609 GLN B CB  
4726 C CG  . GLN A 626 ? 1.0956 1.0956 1.0956 0.0000 0.0000 0.0000 609 GLN B CG  
4727 C CD  . GLN A 626 ? 1.0956 1.0956 1.0956 0.0000 0.0000 0.0000 609 GLN B CD  
4728 O OE1 . GLN A 626 ? 1.0956 1.0956 1.0956 0.0000 0.0000 0.0000 609 GLN B OE1 
4729 N NE2 . GLN A 626 ? 1.0956 1.0956 1.0956 0.0000 0.0000 0.0000 609 GLN B NE2 
4730 N N   . LEU A 627 ? 1.0425 1.0425 1.0425 0.0000 0.0000 0.0000 610 LEU B N   
4731 C CA  . LEU A 627 ? 1.0425 1.0425 1.0425 0.0000 0.0000 0.0000 610 LEU B CA  
4732 C C   . LEU A 627 ? 1.0425 1.0425 1.0425 0.0000 0.0000 0.0000 610 LEU B C   
4733 O O   . LEU A 627 ? 1.0425 1.0425 1.0425 0.0000 0.0000 0.0000 610 LEU B O   
4734 C CB  . LEU A 627 ? 1.0425 1.0425 1.0425 0.0000 0.0000 0.0000 610 LEU B CB  
4735 C CG  . LEU A 627 ? 1.0425 1.0425 1.0425 0.0000 0.0000 0.0000 610 LEU B CG  
4736 C CD1 . LEU A 627 ? 1.0425 1.0425 1.0425 0.0000 0.0000 0.0000 610 LEU B CD1 
4737 C CD2 . LEU A 627 ? 1.0425 1.0425 1.0425 0.0000 0.0000 0.0000 610 LEU B CD2 
4738 N N   . VAL A 628 ? 1.0982 1.0982 1.0982 0.0000 0.0000 0.0000 611 VAL B N   
4739 C CA  . VAL A 628 ? 1.0982 1.0982 1.0982 0.0000 0.0000 0.0000 611 VAL B CA  
4740 C C   . VAL A 628 ? 1.0982 1.0982 1.0982 0.0000 0.0000 0.0000 611 VAL B C   
4741 O O   . VAL A 628 ? 1.0982 1.0982 1.0982 0.0000 0.0000 0.0000 611 VAL B O   
4742 C CB  . VAL A 628 ? 1.0982 1.0982 1.0982 0.0000 0.0000 0.0000 611 VAL B CB  
4743 C CG1 . VAL A 628 ? 1.0982 1.0982 1.0982 0.0000 0.0000 0.0000 611 VAL B CG1 
4744 C CG2 . VAL A 628 ? 1.0982 1.0982 1.0982 0.0000 0.0000 0.0000 611 VAL B CG2 
4745 N N   . TYR A 629 ? 1.1784 1.1784 1.1784 0.0000 0.0000 0.0000 612 TYR B N   
4746 C CA  . TYR A 629 ? 1.1784 1.1784 1.1784 0.0000 0.0000 0.0000 612 TYR B CA  
4747 C C   . TYR A 629 ? 1.1784 1.1784 1.1784 0.0000 0.0000 0.0000 612 TYR B C   
4748 O O   . TYR A 629 ? 1.1784 1.1784 1.1784 0.0000 0.0000 0.0000 612 TYR B O   
4749 C CB  . TYR A 629 ? 1.1784 1.1784 1.1784 0.0000 0.0000 0.0000 612 TYR B CB  
4750 C CG  . TYR A 629 ? 1.1784 1.1784 1.1784 0.0000 0.0000 0.0000 612 TYR B CG  
4751 C CD1 . TYR A 629 ? 1.1784 1.1784 1.1784 0.0000 0.0000 0.0000 612 TYR B CD1 
4752 C CD2 . TYR A 629 ? 1.1784 1.1784 1.1784 0.0000 0.0000 0.0000 612 TYR B CD2 
4753 C CE1 . TYR A 629 ? 1.1784 1.1784 1.1784 0.0000 0.0000 0.0000 612 TYR B CE1 
4754 C CE2 . TYR A 629 ? 1.1784 1.1784 1.1784 0.0000 0.0000 0.0000 612 TYR B CE2 
4755 C CZ  . TYR A 629 ? 1.1784 1.1784 1.1784 0.0000 0.0000 0.0000 612 TYR B CZ  
4756 O OH  . TYR A 629 ? 1.1784 1.1784 1.1784 0.0000 0.0000 0.0000 612 TYR B OH  
4757 N N   . ASP A 630 ? 1.1653 1.1653 1.1653 0.0000 0.0000 0.0000 613 ASP B N   
4758 C CA  . ASP A 630 ? 1.1653 1.1653 1.1653 0.0000 0.0000 0.0000 613 ASP B CA  
4759 C C   . ASP A 630 ? 1.1653 1.1653 1.1653 0.0000 0.0000 0.0000 613 ASP B C   
4760 O O   . ASP A 630 ? 1.1653 1.1653 1.1653 0.0000 0.0000 0.0000 613 ASP B O   
4761 C CB  . ASP A 630 ? 1.1653 1.1653 1.1653 0.0000 0.0000 0.0000 613 ASP B CB  
4762 C CG  . ASP A 630 ? 1.1653 1.1653 1.1653 0.0000 0.0000 0.0000 613 ASP B CG  
4763 O OD1 . ASP A 630 ? 1.1653 1.1653 1.1653 0.0000 0.0000 0.0000 613 ASP B OD1 
4764 O OD2 . ASP A 630 ? 1.1653 1.1653 1.1653 0.0000 0.0000 0.0000 613 ASP B OD2 
4765 N N   . PHE A 631 ? 1.1385 1.1385 1.1385 0.0000 0.0000 0.0000 614 PHE B N   
4766 C CA  . PHE A 631 ? 1.1385 1.1385 1.1385 0.0000 0.0000 0.0000 614 PHE B CA  
4767 C C   . PHE A 631 ? 1.1385 1.1385 1.1385 0.0000 0.0000 0.0000 614 PHE B C   
4768 O O   . PHE A 631 ? 1.1385 1.1385 1.1385 0.0000 0.0000 0.0000 614 PHE B O   
4769 C CB  . PHE A 631 ? 1.1385 1.1385 1.1385 0.0000 0.0000 0.0000 614 PHE B CB  
4770 C CG  . PHE A 631 ? 1.1385 1.1385 1.1385 0.0000 0.0000 0.0000 614 PHE B CG  
4771 C CD1 . PHE A 631 ? 1.1385 1.1385 1.1385 0.0000 0.0000 0.0000 614 PHE B CD1 
4772 C CD2 . PHE A 631 ? 1.1385 1.1385 1.1385 0.0000 0.0000 0.0000 614 PHE B CD2 
4773 C CE1 . PHE A 631 ? 1.1385 1.1385 1.1385 0.0000 0.0000 0.0000 614 PHE B CE1 
4774 C CE2 . PHE A 631 ? 1.1385 1.1385 1.1385 0.0000 0.0000 0.0000 614 PHE B CE2 
4775 C CZ  . PHE A 631 ? 1.1385 1.1385 1.1385 0.0000 0.0000 0.0000 614 PHE B CZ  
4776 N N   . THR A 632 ? 1.1629 1.1629 1.1629 0.0000 0.0000 0.0000 615 THR B N   
4777 C CA  . THR A 632 ? 1.1629 1.1629 1.1629 0.0000 0.0000 0.0000 615 THR B CA  
4778 C C   . THR A 632 ? 1.1629 1.1629 1.1629 0.0000 0.0000 0.0000 615 THR B C   
4779 O O   . THR A 632 ? 1.1629 1.1629 1.1629 0.0000 0.0000 0.0000 615 THR B O   
4780 C CB  . THR A 632 ? 1.1629 1.1629 1.1629 0.0000 0.0000 0.0000 615 THR B CB  
4781 O OG1 . THR A 632 ? 1.1629 1.1629 1.1629 0.0000 0.0000 0.0000 615 THR B OG1 
4782 C CG2 . THR A 632 ? 1.1629 1.1629 1.1629 0.0000 0.0000 0.0000 615 THR B CG2 
4783 N N   . ASP A 633 ? 1.2183 1.2183 1.2183 0.0000 0.0000 0.0000 616 ASP B N   
4784 C CA  . ASP A 633 ? 1.2183 1.2183 1.2183 0.0000 0.0000 0.0000 616 ASP B CA  
4785 C C   . ASP A 633 ? 1.2183 1.2183 1.2183 0.0000 0.0000 0.0000 616 ASP B C   
4786 O O   . ASP A 633 ? 1.2183 1.2183 1.2183 0.0000 0.0000 0.0000 616 ASP B O   
4787 C CB  . ASP A 633 ? 1.2183 1.2183 1.2183 0.0000 0.0000 0.0000 616 ASP B CB  
4788 C CG  . ASP A 633 ? 1.2183 1.2183 1.2183 0.0000 0.0000 0.0000 616 ASP B CG  
4789 O OD1 . ASP A 633 ? 1.2183 1.2183 1.2183 0.0000 0.0000 0.0000 616 ASP B OD1 
4790 O OD2 . ASP A 633 ? 1.2183 1.2183 1.2183 0.0000 0.0000 0.0000 616 ASP B OD2 
4791 N N   . GLU A 634 ? 1.1761 1.1761 1.1761 0.0000 0.0000 0.0000 617 GLU B N   
4792 C CA  . GLU A 634 ? 1.1761 1.1761 1.1761 0.0000 0.0000 0.0000 617 GLU B CA  
4793 C C   . GLU A 634 ? 1.1761 1.1761 1.1761 0.0000 0.0000 0.0000 617 GLU B C   
4794 O O   . GLU A 634 ? 1.1761 1.1761 1.1761 0.0000 0.0000 0.0000 617 GLU B O   
4795 C CB  . GLU A 634 ? 1.1761 1.1761 1.1761 0.0000 0.0000 0.0000 617 GLU B CB  
4796 C CG  . GLU A 634 ? 1.1761 1.1761 1.1761 0.0000 0.0000 0.0000 617 GLU B CG  
4797 C CD  . GLU A 634 ? 1.1761 1.1761 1.1761 0.0000 0.0000 0.0000 617 GLU B CD  
4798 O OE1 . GLU A 634 ? 1.1761 1.1761 1.1761 0.0000 0.0000 0.0000 617 GLU B OE1 
4799 O OE2 . GLU A 634 ? 1.1761 1.1761 1.1761 0.0000 0.0000 0.0000 617 GLU B OE2 
4800 N N   . THR A 635 ? 1.1464 1.1464 1.1464 0.0000 0.0000 0.0000 618 THR B N   
4801 C CA  . THR A 635 ? 1.1464 1.1464 1.1464 0.0000 0.0000 0.0000 618 THR B CA  
4802 C C   . THR A 635 ? 1.1464 1.1464 1.1464 0.0000 0.0000 0.0000 618 THR B C   
4803 O O   . THR A 635 ? 1.1464 1.1464 1.1464 0.0000 0.0000 0.0000 618 THR B O   
4804 C CB  . THR A 635 ? 1.1464 1.1464 1.1464 0.0000 0.0000 0.0000 618 THR B CB  
4805 O OG1 . THR A 635 ? 1.1464 1.1464 1.1464 0.0000 0.0000 0.0000 618 THR B OG1 
4806 C CG2 . THR A 635 ? 1.1464 1.1464 1.1464 0.0000 0.0000 0.0000 618 THR B CG2 
4807 N N   . SER A 636 ? 1.1913 1.1913 1.1913 0.0000 0.0000 0.0000 619 SER B N   
4808 C CA  . SER A 636 ? 1.1913 1.1913 1.1913 0.0000 0.0000 0.0000 619 SER B CA  
4809 C C   . SER A 636 ? 1.1913 1.1913 1.1913 0.0000 0.0000 0.0000 619 SER B C   
4810 O O   . SER A 636 ? 1.1913 1.1913 1.1913 0.0000 0.0000 0.0000 619 SER B O   
4811 C CB  . SER A 636 ? 1.1913 1.1913 1.1913 0.0000 0.0000 0.0000 619 SER B CB  
4812 O OG  . SER A 636 ? 1.1913 1.1913 1.1913 0.0000 0.0000 0.0000 619 SER B OG  
4813 N N   . GLU A 637 ? 1.2451 1.2451 1.2451 0.0000 0.0000 0.0000 620 GLU B N   
4814 C CA  . GLU A 637 ? 1.2451 1.2451 1.2451 0.0000 0.0000 0.0000 620 GLU B CA  
4815 C C   . GLU A 637 ? 1.2451 1.2451 1.2451 0.0000 0.0000 0.0000 620 GLU B C   
4816 O O   . GLU A 637 ? 1.2451 1.2451 1.2451 0.0000 0.0000 0.0000 620 GLU B O   
4817 C CB  . GLU A 637 ? 1.2451 1.2451 1.2451 0.0000 0.0000 0.0000 620 GLU B CB  
4818 C CG  . GLU A 637 ? 1.2451 1.2451 1.2451 0.0000 0.0000 0.0000 620 GLU B CG  
4819 C CD  . GLU A 637 ? 1.2451 1.2451 1.2451 0.0000 0.0000 0.0000 620 GLU B CD  
4820 O OE1 . GLU A 637 ? 1.2451 1.2451 1.2451 0.0000 0.0000 0.0000 620 GLU B OE1 
4821 O OE2 . GLU A 637 ? 1.2451 1.2451 1.2451 0.0000 0.0000 0.0000 620 GLU B OE2 
4822 N N   . VAL A 638 ? 1.3002 1.3002 1.3002 0.0000 0.0000 0.0000 621 VAL B N   
4823 C CA  . VAL A 638 ? 1.3002 1.3002 1.3002 0.0000 0.0000 0.0000 621 VAL B CA  
4824 C C   . VAL A 638 ? 1.3002 1.3002 1.3002 0.0000 0.0000 0.0000 621 VAL B C   
4825 O O   . VAL A 638 ? 1.3002 1.3002 1.3002 0.0000 0.0000 0.0000 621 VAL B O   
4826 C CB  . VAL A 638 ? 1.3002 1.3002 1.3002 0.0000 0.0000 0.0000 621 VAL B CB  
4827 C CG1 . VAL A 638 ? 1.3002 1.3002 1.3002 0.0000 0.0000 0.0000 621 VAL B CG1 
4828 C CG2 . VAL A 638 ? 1.3002 1.3002 1.3002 0.0000 0.0000 0.0000 621 VAL B CG2 
4829 N N   . SER A 639 ? 1.5052 1.5052 1.5052 0.0000 0.0000 0.0000 622 SER B N   
4830 C CA  . SER A 639 ? 1.5052 1.5052 1.5052 0.0000 0.0000 0.0000 622 SER B CA  
4831 C C   . SER A 639 ? 1.5052 1.5052 1.5052 0.0000 0.0000 0.0000 622 SER B C   
4832 O O   . SER A 639 ? 1.5052 1.5052 1.5052 0.0000 0.0000 0.0000 622 SER B O   
4833 C CB  . SER A 639 ? 1.5052 1.5052 1.5052 0.0000 0.0000 0.0000 622 SER B CB  
4834 O OG  . SER A 639 ? 1.5052 1.5052 1.5052 0.0000 0.0000 0.0000 622 SER B OG  
4835 N N   . THR A 640 ? 1.7244 1.7244 1.7244 0.0000 0.0000 0.0000 623 THR B N   
4836 C CA  . THR A 640 ? 1.7244 1.7244 1.7244 0.0000 0.0000 0.0000 623 THR B CA  
4837 C C   . THR A 640 ? 1.7244 1.7244 1.7244 0.0000 0.0000 0.0000 623 THR B C   
4838 O O   . THR A 640 ? 1.7244 1.7244 1.7244 0.0000 0.0000 0.0000 623 THR B O   
4839 C CB  . THR A 640 ? 1.7244 1.7244 1.7244 0.0000 0.0000 0.0000 623 THR B CB  
4840 O OG1 . THR A 640 ? 1.7244 1.7244 1.7244 0.0000 0.0000 0.0000 623 THR B OG1 
4841 C CG2 . THR A 640 ? 1.7244 1.7244 1.7244 0.0000 0.0000 0.0000 623 THR B CG2 
4842 N N   . THR A 641 ? 1.7873 1.7873 1.7873 0.0000 0.0000 0.0000 624 THR B N   
4843 C CA  . THR A 641 ? 1.7873 1.7873 1.7873 0.0000 0.0000 0.0000 624 THR B CA  
4844 C C   . THR A 641 ? 1.7873 1.7873 1.7873 0.0000 0.0000 0.0000 624 THR B C   
4845 O O   . THR A 641 ? 1.7873 1.7873 1.7873 0.0000 0.0000 0.0000 624 THR B O   
4846 C CB  . THR A 641 ? 1.7873 1.7873 1.7873 0.0000 0.0000 0.0000 624 THR B CB  
4847 O OG1 . THR A 641 ? 1.7873 1.7873 1.7873 0.0000 0.0000 0.0000 624 THR B OG1 
4848 C CG2 . THR A 641 ? 1.7873 1.7873 1.7873 0.0000 0.0000 0.0000 624 THR B CG2 
4849 N N   . ASP A 642 ? 1.7856 1.7856 1.7856 0.0000 0.0000 0.0000 625 ASP B N   
4850 C CA  . ASP A 642 ? 1.7856 1.7856 1.7856 0.0000 0.0000 0.0000 625 ASP B CA  
4851 C C   . ASP A 642 ? 1.7856 1.7856 1.7856 0.0000 0.0000 0.0000 625 ASP B C   
4852 O O   . ASP A 642 ? 1.7856 1.7856 1.7856 0.0000 0.0000 0.0000 625 ASP B O   
4853 C CB  . ASP A 642 ? 1.7856 1.7856 1.7856 0.0000 0.0000 0.0000 625 ASP B CB  
4854 C CG  . ASP A 642 ? 1.7856 1.7856 1.7856 0.0000 0.0000 0.0000 625 ASP B CG  
4855 O OD1 . ASP A 642 ? 1.7856 1.7856 1.7856 0.0000 0.0000 0.0000 625 ASP B OD1 
4856 O OD2 . ASP A 642 ? 1.7856 1.7856 1.7856 0.0000 0.0000 0.0000 625 ASP B OD2 
4857 N N   . LYS A 643 ? 1.5878 1.5878 1.5878 0.0000 0.0000 0.0000 626 LYS B N   
4858 C CA  . LYS A 643 ? 1.5878 1.5878 1.5878 0.0000 0.0000 0.0000 626 LYS B CA  
4859 C C   . LYS A 643 ? 1.5878 1.5878 1.5878 0.0000 0.0000 0.0000 626 LYS B C   
4860 O O   . LYS A 643 ? 1.5878 1.5878 1.5878 0.0000 0.0000 0.0000 626 LYS B O   
4861 C CB  . LYS A 643 ? 1.5878 1.5878 1.5878 0.0000 0.0000 0.0000 626 LYS B CB  
4862 C CG  . LYS A 643 ? 1.5878 1.5878 1.5878 0.0000 0.0000 0.0000 626 LYS B CG  
4863 C CD  . LYS A 643 ? 1.5878 1.5878 1.5878 0.0000 0.0000 0.0000 626 LYS B CD  
4864 C CE  . LYS A 643 ? 1.5878 1.5878 1.5878 0.0000 0.0000 0.0000 626 LYS B CE  
4865 N NZ  . LYS A 643 ? 1.5878 1.5878 1.5878 0.0000 0.0000 0.0000 626 LYS B NZ  
4866 N N   . ILE A 644 ? 1.4659 1.4659 1.4659 0.0000 0.0000 0.0000 627 ILE B N   
4867 C CA  . ILE A 644 ? 1.4659 1.4659 1.4659 0.0000 0.0000 0.0000 627 ILE B CA  
4868 C C   . ILE A 644 ? 1.4659 1.4659 1.4659 0.0000 0.0000 0.0000 627 ILE B C   
4869 O O   . ILE A 644 ? 1.4659 1.4659 1.4659 0.0000 0.0000 0.0000 627 ILE B O   
4870 C CB  . ILE A 644 ? 1.4659 1.4659 1.4659 0.0000 0.0000 0.0000 627 ILE B CB  
4871 C CG1 . ILE A 644 ? 1.4659 1.4659 1.4659 0.0000 0.0000 0.0000 627 ILE B CG1 
4872 C CG2 . ILE A 644 ? 1.4659 1.4659 1.4659 0.0000 0.0000 0.0000 627 ILE B CG2 
4873 C CD1 . ILE A 644 ? 1.4659 1.4659 1.4659 0.0000 0.0000 0.0000 627 ILE B CD1 
4874 N N   . ALA A 645 ? 1.3417 1.3417 1.3417 0.0000 0.0000 0.0000 628 ALA B N   
4875 C CA  . ALA A 645 ? 1.3417 1.3417 1.3417 0.0000 0.0000 0.0000 628 ALA B CA  
4876 C C   . ALA A 645 ? 1.3417 1.3417 1.3417 0.0000 0.0000 0.0000 628 ALA B C   
4877 O O   . ALA A 645 ? 1.3417 1.3417 1.3417 0.0000 0.0000 0.0000 628 ALA B O   
4878 C CB  . ALA A 645 ? 1.3417 1.3417 1.3417 0.0000 0.0000 0.0000 628 ALA B CB  
4879 N N   . ASP A 646 ? 1.2185 1.2185 1.2185 0.0000 0.0000 0.0000 629 ASP B N   
4880 C CA  . ASP A 646 ? 1.2185 1.2185 1.2185 0.0000 0.0000 0.0000 629 ASP B CA  
4881 C C   . ASP A 646 ? 1.2185 1.2185 1.2185 0.0000 0.0000 0.0000 629 ASP B C   
4882 O O   . ASP A 646 ? 1.2185 1.2185 1.2185 0.0000 0.0000 0.0000 629 ASP B O   
4883 C CB  . ASP A 646 ? 1.2185 1.2185 1.2185 0.0000 0.0000 0.0000 629 ASP B CB  
4884 C CG  . ASP A 646 ? 1.2185 1.2185 1.2185 0.0000 0.0000 0.0000 629 ASP B CG  
4885 O OD1 . ASP A 646 ? 1.2185 1.2185 1.2185 0.0000 0.0000 0.0000 629 ASP B OD1 
4886 O OD2 . ASP A 646 ? 1.2185 1.2185 1.2185 0.0000 0.0000 0.0000 629 ASP B OD2 
4887 N N   . ILE A 647 ? 1.1846 1.1846 1.1846 0.0000 0.0000 0.0000 630 ILE B N   
4888 C CA  . ILE A 647 ? 1.1846 1.1846 1.1846 0.0000 0.0000 0.0000 630 ILE B CA  
4889 C C   . ILE A 647 ? 1.1846 1.1846 1.1846 0.0000 0.0000 0.0000 630 ILE B C   
4890 O O   . ILE A 647 ? 1.1846 1.1846 1.1846 0.0000 0.0000 0.0000 630 ILE B O   
4891 C CB  . ILE A 647 ? 1.1846 1.1846 1.1846 0.0000 0.0000 0.0000 630 ILE B CB  
4892 C CG1 . ILE A 647 ? 1.1846 1.1846 1.1846 0.0000 0.0000 0.0000 630 ILE B CG1 
4893 C CG2 . ILE A 647 ? 1.1846 1.1846 1.1846 0.0000 0.0000 0.0000 630 ILE B CG2 
4894 C CD1 . ILE A 647 ? 1.1846 1.1846 1.1846 0.0000 0.0000 0.0000 630 ILE B CD1 
4895 N N   . THR A 648 ? 1.2133 1.2133 1.2133 0.0000 0.0000 0.0000 631 THR B N   
4896 C CA  . THR A 648 ? 1.2133 1.2133 1.2133 0.0000 0.0000 0.0000 631 THR B CA  
4897 C C   . THR A 648 ? 1.2133 1.2133 1.2133 0.0000 0.0000 0.0000 631 THR B C   
4898 O O   . THR A 648 ? 1.2133 1.2133 1.2133 0.0000 0.0000 0.0000 631 THR B O   
4899 C CB  . THR A 648 ? 1.2133 1.2133 1.2133 0.0000 0.0000 0.0000 631 THR B CB  
4900 O OG1 . THR A 648 ? 1.2133 1.2133 1.2133 0.0000 0.0000 0.0000 631 THR B OG1 
4901 C CG2 . THR A 648 ? 1.2133 1.2133 1.2133 0.0000 0.0000 0.0000 631 THR B CG2 
4902 N N   . ILE A 649 ? 1.1726 1.1726 1.1726 0.0000 0.0000 0.0000 632 ILE B N   
4903 C CA  . ILE A 649 ? 1.1726 1.1726 1.1726 0.0000 0.0000 0.0000 632 ILE B CA  
4904 C C   . ILE A 649 ? 1.1726 1.1726 1.1726 0.0000 0.0000 0.0000 632 ILE B C   
4905 O O   . ILE A 649 ? 1.1726 1.1726 1.1726 0.0000 0.0000 0.0000 632 ILE B O   
4906 C CB  . ILE A 649 ? 1.1726 1.1726 1.1726 0.0000 0.0000 0.0000 632 ILE B CB  
4907 C CG1 . ILE A 649 ? 1.1726 1.1726 1.1726 0.0000 0.0000 0.0000 632 ILE B CG1 
4908 C CG2 . ILE A 649 ? 1.1726 1.1726 1.1726 0.0000 0.0000 0.0000 632 ILE B CG2 
4909 C CD1 . ILE A 649 ? 1.1726 1.1726 1.1726 0.0000 0.0000 0.0000 632 ILE B CD1 
4910 N N   . ILE A 650 ? 1.1054 1.1054 1.1054 0.0000 0.0000 0.0000 633 ILE B N   
4911 C CA  . ILE A 650 ? 1.1054 1.1054 1.1054 0.0000 0.0000 0.0000 633 ILE B CA  
4912 C C   . ILE A 650 ? 1.1054 1.1054 1.1054 0.0000 0.0000 0.0000 633 ILE B C   
4913 O O   . ILE A 650 ? 1.1054 1.1054 1.1054 0.0000 0.0000 0.0000 633 ILE B O   
4914 C CB  . ILE A 650 ? 1.1054 1.1054 1.1054 0.0000 0.0000 0.0000 633 ILE B CB  
4915 C CG1 . ILE A 650 ? 1.1054 1.1054 1.1054 0.0000 0.0000 0.0000 633 ILE B CG1 
4916 C CG2 . ILE A 650 ? 1.1054 1.1054 1.1054 0.0000 0.0000 0.0000 633 ILE B CG2 
4917 C CD1 . ILE A 650 ? 1.1054 1.1054 1.1054 0.0000 0.0000 0.0000 633 ILE B CD1 
4918 N N   . ILE A 651 ? 1.1054 1.1054 1.1054 0.0000 0.0000 0.0000 634 ILE B N   
4919 C CA  . ILE A 651 ? 1.1054 1.1054 1.1054 0.0000 0.0000 0.0000 634 ILE B CA  
4920 C C   . ILE A 651 ? 1.1054 1.1054 1.1054 0.0000 0.0000 0.0000 634 ILE B C   
4921 O O   . ILE A 651 ? 1.1054 1.1054 1.1054 0.0000 0.0000 0.0000 634 ILE B O   
4922 C CB  . ILE A 651 ? 1.1054 1.1054 1.1054 0.0000 0.0000 0.0000 634 ILE B CB  
4923 C CG1 . ILE A 651 ? 1.1054 1.1054 1.1054 0.0000 0.0000 0.0000 634 ILE B CG1 
4924 C CG2 . ILE A 651 ? 1.1054 1.1054 1.1054 0.0000 0.0000 0.0000 634 ILE B CG2 
4925 C CD1 . ILE A 651 ? 1.1054 1.1054 1.1054 0.0000 0.0000 0.0000 634 ILE B CD1 
4926 N N   . PRO A 652 ? 1.1933 1.1933 1.1933 0.0000 0.0000 0.0000 635 PRO B N   
4927 C CA  . PRO A 652 ? 1.1933 1.1933 1.1933 0.0000 0.0000 0.0000 635 PRO B CA  
4928 C C   . PRO A 652 ? 1.1933 1.1933 1.1933 0.0000 0.0000 0.0000 635 PRO B C   
4929 O O   . PRO A 652 ? 1.1933 1.1933 1.1933 0.0000 0.0000 0.0000 635 PRO B O   
4930 C CB  . PRO A 652 ? 1.1933 1.1933 1.1933 0.0000 0.0000 0.0000 635 PRO B CB  
4931 C CG  . PRO A 652 ? 1.1933 1.1933 1.1933 0.0000 0.0000 0.0000 635 PRO B CG  
4932 C CD  . PRO A 652 ? 1.1933 1.1933 1.1933 0.0000 0.0000 0.0000 635 PRO B CD  
4933 N N   . TYR A 653 ? 1.0833 1.0833 1.0833 0.0000 0.0000 0.0000 636 TYR B N   
4934 C CA  . TYR A 653 ? 1.0833 1.0833 1.0833 0.0000 0.0000 0.0000 636 TYR B CA  
4935 C C   . TYR A 653 ? 1.0833 1.0833 1.0833 0.0000 0.0000 0.0000 636 TYR B C   
4936 O O   . TYR A 653 ? 1.0833 1.0833 1.0833 0.0000 0.0000 0.0000 636 TYR B O   
4937 C CB  . TYR A 653 ? 1.0833 1.0833 1.0833 0.0000 0.0000 0.0000 636 TYR B CB  
4938 C CG  . TYR A 653 ? 1.0833 1.0833 1.0833 0.0000 0.0000 0.0000 636 TYR B CG  
4939 C CD1 . TYR A 653 ? 1.0833 1.0833 1.0833 0.0000 0.0000 0.0000 636 TYR B CD1 
4940 C CD2 . TYR A 653 ? 1.0833 1.0833 1.0833 0.0000 0.0000 0.0000 636 TYR B CD2 
4941 C CE1 . TYR A 653 ? 1.0833 1.0833 1.0833 0.0000 0.0000 0.0000 636 TYR B CE1 
4942 C CE2 . TYR A 653 ? 1.0833 1.0833 1.0833 0.0000 0.0000 0.0000 636 TYR B CE2 
4943 C CZ  . TYR A 653 ? 1.0833 1.0833 1.0833 0.0000 0.0000 0.0000 636 TYR B CZ  
4944 O OH  . TYR A 653 ? 1.0833 1.0833 1.0833 0.0000 0.0000 0.0000 636 TYR B OH  
4945 N N   . ILE A 654 ? 1.0720 1.0720 1.0720 0.0000 0.0000 0.0000 637 ILE B N   
4946 C CA  . ILE A 654 ? 1.0720 1.0720 1.0720 0.0000 0.0000 0.0000 637 ILE B CA  
4947 C C   . ILE A 654 ? 1.0720 1.0720 1.0720 0.0000 0.0000 0.0000 637 ILE B C   
4948 O O   . ILE A 654 ? 1.0720 1.0720 1.0720 0.0000 0.0000 0.0000 637 ILE B O   
4949 C CB  . ILE A 654 ? 1.0720 1.0720 1.0720 0.0000 0.0000 0.0000 637 ILE B CB  
4950 C CG1 . ILE A 654 ? 1.0720 1.0720 1.0720 0.0000 0.0000 0.0000 637 ILE B CG1 
4951 C CG2 . ILE A 654 ? 1.0720 1.0720 1.0720 0.0000 0.0000 0.0000 637 ILE B CG2 
4952 C CD1 . ILE A 654 ? 1.0720 1.0720 1.0720 0.0000 0.0000 0.0000 637 ILE B CD1 
4953 N N   . GLY A 655 ? 1.0945 1.0945 1.0945 0.0000 0.0000 0.0000 638 GLY B N   
4954 C CA  . GLY A 655 ? 1.0945 1.0945 1.0945 0.0000 0.0000 0.0000 638 GLY B CA  
4955 C C   . GLY A 655 ? 1.0945 1.0945 1.0945 0.0000 0.0000 0.0000 638 GLY B C   
4956 O O   . GLY A 655 ? 1.0945 1.0945 1.0945 0.0000 0.0000 0.0000 638 GLY B O   
4957 N N   . PRO A 656 ? 1.0377 1.0377 1.0377 0.0000 0.0000 0.0000 639 PRO B N   
4958 C CA  . PRO A 656 ? 1.0377 1.0377 1.0377 0.0000 0.0000 0.0000 639 PRO B CA  
4959 C C   . PRO A 656 ? 1.0377 1.0377 1.0377 0.0000 0.0000 0.0000 639 PRO B C   
4960 O O   . PRO A 656 ? 1.0377 1.0377 1.0377 0.0000 0.0000 0.0000 639 PRO B O   
4961 C CB  . PRO A 656 ? 1.0377 1.0377 1.0377 0.0000 0.0000 0.0000 639 PRO B CB  
4962 C CG  . PRO A 656 ? 1.0377 1.0377 1.0377 0.0000 0.0000 0.0000 639 PRO B CG  
4963 C CD  . PRO A 656 ? 1.0377 1.0377 1.0377 0.0000 0.0000 0.0000 639 PRO B CD  
4964 N N   . ALA A 657 ? 0.9914 0.9914 0.9914 0.0000 0.0000 0.0000 640 ALA B N   
4965 C CA  . ALA A 657 ? 0.9914 0.9914 0.9914 0.0000 0.0000 0.0000 640 ALA B CA  
4966 C C   . ALA A 657 ? 0.9914 0.9914 0.9914 0.0000 0.0000 0.0000 640 ALA B C   
4967 O O   . ALA A 657 ? 0.9914 0.9914 0.9914 0.0000 0.0000 0.0000 640 ALA B O   
4968 C CB  . ALA A 657 ? 0.9914 0.9914 0.9914 0.0000 0.0000 0.0000 640 ALA B CB  
4969 N N   . LEU A 658 ? 1.0169 1.0169 1.0169 0.0000 0.0000 0.0000 641 LEU B N   
4970 C CA  . LEU A 658 ? 1.0169 1.0169 1.0169 0.0000 0.0000 0.0000 641 LEU B CA  
4971 C C   . LEU A 658 ? 1.0169 1.0169 1.0169 0.0000 0.0000 0.0000 641 LEU B C   
4972 O O   . LEU A 658 ? 1.0169 1.0169 1.0169 0.0000 0.0000 0.0000 641 LEU B O   
4973 C CB  . LEU A 658 ? 1.0169 1.0169 1.0169 0.0000 0.0000 0.0000 641 LEU B CB  
4974 C CG  . LEU A 658 ? 1.0169 1.0169 1.0169 0.0000 0.0000 0.0000 641 LEU B CG  
4975 C CD1 . LEU A 658 ? 1.0169 1.0169 1.0169 0.0000 0.0000 0.0000 641 LEU B CD1 
4976 C CD2 . LEU A 658 ? 1.0169 1.0169 1.0169 0.0000 0.0000 0.0000 641 LEU B CD2 
4977 N N   . ASN A 659 ? 1.0940 1.0940 1.0940 0.0000 0.0000 0.0000 642 ASN B N   
4978 C CA  . ASN A 659 ? 1.0940 1.0940 1.0940 0.0000 0.0000 0.0000 642 ASN B CA  
4979 C C   . ASN A 659 ? 1.0940 1.0940 1.0940 0.0000 0.0000 0.0000 642 ASN B C   
4980 O O   . ASN A 659 ? 1.0940 1.0940 1.0940 0.0000 0.0000 0.0000 642 ASN B O   
4981 C CB  . ASN A 659 ? 1.0940 1.0940 1.0940 0.0000 0.0000 0.0000 642 ASN B CB  
4982 C CG  . ASN A 659 ? 1.0940 1.0940 1.0940 0.0000 0.0000 0.0000 642 ASN B CG  
4983 O OD1 . ASN A 659 ? 1.0940 1.0940 1.0940 0.0000 0.0000 0.0000 642 ASN B OD1 
4984 N ND2 . ASN A 659 ? 1.0940 1.0940 1.0940 0.0000 0.0000 0.0000 642 ASN B ND2 
4985 N N   . ILE A 660 ? 1.1377 1.1377 1.1377 0.0000 0.0000 0.0000 643 ILE B N   
4986 C CA  . ILE A 660 ? 1.1377 1.1377 1.1377 0.0000 0.0000 0.0000 643 ILE B CA  
4987 C C   . ILE A 660 ? 1.1377 1.1377 1.1377 0.0000 0.0000 0.0000 643 ILE B C   
4988 O O   . ILE A 660 ? 1.1377 1.1377 1.1377 0.0000 0.0000 0.0000 643 ILE B O   
4989 C CB  . ILE A 660 ? 1.1377 1.1377 1.1377 0.0000 0.0000 0.0000 643 ILE B CB  
4990 C CG1 . ILE A 660 ? 1.1377 1.1377 1.1377 0.0000 0.0000 0.0000 643 ILE B CG1 
4991 C CG2 . ILE A 660 ? 1.1377 1.1377 1.1377 0.0000 0.0000 0.0000 643 ILE B CG2 
4992 C CD1 . ILE A 660 ? 1.1377 1.1377 1.1377 0.0000 0.0000 0.0000 643 ILE B CD1 
4993 N N   . GLY A 661 ? 1.2379 1.2379 1.2379 0.0000 0.0000 0.0000 644 GLY B N   
4994 C CA  . GLY A 661 ? 1.2379 1.2379 1.2379 0.0000 0.0000 0.0000 644 GLY B CA  
4995 C C   . GLY A 661 ? 1.2379 1.2379 1.2379 0.0000 0.0000 0.0000 644 GLY B C   
4996 O O   . GLY A 661 ? 1.2379 1.2379 1.2379 0.0000 0.0000 0.0000 644 GLY B O   
4997 N N   . ASN A 662 ? 1.2491 1.2491 1.2491 0.0000 0.0000 0.0000 645 ASN B N   
4998 C CA  . ASN A 662 ? 1.2491 1.2491 1.2491 0.0000 0.0000 0.0000 645 ASN B CA  
4999 C C   . ASN A 662 ? 1.2491 1.2491 1.2491 0.0000 0.0000 0.0000 645 ASN B C   
5000 O O   . ASN A 662 ? 1.2491 1.2491 1.2491 0.0000 0.0000 0.0000 645 ASN B O   
5001 C CB  . ASN A 662 ? 1.2491 1.2491 1.2491 0.0000 0.0000 0.0000 645 ASN B CB  
5002 C CG  . ASN A 662 ? 1.2491 1.2491 1.2491 0.0000 0.0000 0.0000 645 ASN B CG  
5003 O OD1 . ASN A 662 ? 1.2491 1.2491 1.2491 0.0000 0.0000 0.0000 645 ASN B OD1 
5004 N ND2 . ASN A 662 ? 1.2491 1.2491 1.2491 0.0000 0.0000 0.0000 645 ASN B ND2 
5005 N N   . MET A 663 ? 1.3640 1.3640 1.3640 0.0000 0.0000 0.0000 646 MET B N   
5006 C CA  . MET A 663 ? 1.3640 1.3640 1.3640 0.0000 0.0000 0.0000 646 MET B CA  
5007 C C   . MET A 663 ? 1.3640 1.3640 1.3640 0.0000 0.0000 0.0000 646 MET B C   
5008 O O   . MET A 663 ? 1.3640 1.3640 1.3640 0.0000 0.0000 0.0000 646 MET B O   
5009 C CB  . MET A 663 ? 1.3640 1.3640 1.3640 0.0000 0.0000 0.0000 646 MET B CB  
5010 C CG  . MET A 663 ? 1.3640 1.3640 1.3640 0.0000 0.0000 0.0000 646 MET B CG  
5011 S SD  . MET A 663 ? 1.3640 1.3640 1.3640 0.0000 0.0000 0.0000 646 MET B SD  
5012 C CE  . MET A 663 ? 1.3640 1.3640 1.3640 0.0000 0.0000 0.0000 646 MET B CE  
5013 N N   . LEU A 664 ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 647 LEU B N   
5014 C CA  . LEU A 664 ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 647 LEU B CA  
5015 C C   . LEU A 664 ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 647 LEU B C   
5016 O O   . LEU A 664 ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 647 LEU B O   
5017 C CB  . LEU A 664 ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 647 LEU B CB  
5018 N N   . TYR A 665 ? 1.4888 1.4888 1.4888 0.0000 0.0000 0.0000 648 TYR B N   
5019 C CA  . TYR A 665 ? 1.4888 1.4888 1.4888 0.0000 0.0000 0.0000 648 TYR B CA  
5020 C C   . TYR A 665 ? 1.4888 1.4888 1.4888 0.0000 0.0000 0.0000 648 TYR B C   
5021 O O   . TYR A 665 ? 1.4888 1.4888 1.4888 0.0000 0.0000 0.0000 648 TYR B O   
5022 C CB  . TYR A 665 ? 1.4888 1.4888 1.4888 0.0000 0.0000 0.0000 648 TYR B CB  
5023 C CG  . TYR A 665 ? 1.4888 1.4888 1.4888 0.0000 0.0000 0.0000 648 TYR B CG  
5024 C CD1 . TYR A 665 ? 1.4888 1.4888 1.4888 0.0000 0.0000 0.0000 648 TYR B CD1 
5025 C CD2 . TYR A 665 ? 1.4888 1.4888 1.4888 0.0000 0.0000 0.0000 648 TYR B CD2 
5026 C CE1 . TYR A 665 ? 1.4888 1.4888 1.4888 0.0000 0.0000 0.0000 648 TYR B CE1 
5027 C CE2 . TYR A 665 ? 1.4888 1.4888 1.4888 0.0000 0.0000 0.0000 648 TYR B CE2 
5028 C CZ  . TYR A 665 ? 1.4888 1.4888 1.4888 0.0000 0.0000 0.0000 648 TYR B CZ  
5029 O OH  . TYR A 665 ? 1.4888 1.4888 1.4888 0.0000 0.0000 0.0000 648 TYR B OH  
5030 N N   . LYS A 666 ? 1.3986 1.3986 1.3986 0.0000 0.0000 0.0000 649 LYS B N   
5031 C CA  . LYS A 666 ? 1.3986 1.3986 1.3986 0.0000 0.0000 0.0000 649 LYS B CA  
5032 C C   . LYS A 666 ? 1.3986 1.3986 1.3986 0.0000 0.0000 0.0000 649 LYS B C   
5033 O O   . LYS A 666 ? 1.3986 1.3986 1.3986 0.0000 0.0000 0.0000 649 LYS B O   
5034 C CB  . LYS A 666 ? 1.3986 1.3986 1.3986 0.0000 0.0000 0.0000 649 LYS B CB  
5035 C CG  . LYS A 666 ? 1.3986 1.3986 1.3986 0.0000 0.0000 0.0000 649 LYS B CG  
5036 C CD  . LYS A 666 ? 1.3986 1.3986 1.3986 0.0000 0.0000 0.0000 649 LYS B CD  
5037 C CE  . LYS A 666 ? 1.3986 1.3986 1.3986 0.0000 0.0000 0.0000 649 LYS B CE  
5038 N NZ  . LYS A 666 ? 1.3986 1.3986 1.3986 0.0000 0.0000 0.0000 649 LYS B NZ  
5039 N N   . ASP A 667 ? 1.4165 1.4165 1.4165 0.0000 0.0000 0.0000 650 ASP B N   
5040 C CA  . ASP A 667 ? 1.4165 1.4165 1.4165 0.0000 0.0000 0.0000 650 ASP B CA  
5041 C C   . ASP A 667 ? 1.4165 1.4165 1.4165 0.0000 0.0000 0.0000 650 ASP B C   
5042 O O   . ASP A 667 ? 1.4165 1.4165 1.4165 0.0000 0.0000 0.0000 650 ASP B O   
5043 C CB  . ASP A 667 ? 1.4165 1.4165 1.4165 0.0000 0.0000 0.0000 650 ASP B CB  
5044 C CG  . ASP A 667 ? 1.4165 1.4165 1.4165 0.0000 0.0000 0.0000 650 ASP B CG  
5045 O OD1 . ASP A 667 ? 1.4165 1.4165 1.4165 0.0000 0.0000 0.0000 650 ASP B OD1 
5046 O OD2 . ASP A 667 ? 1.4165 1.4165 1.4165 0.0000 0.0000 0.0000 650 ASP B OD2 
5047 N N   . ASP A 668 ? 1.3700 1.3700 1.3700 0.0000 0.0000 0.0000 651 ASP B N   
5048 C CA  . ASP A 668 ? 1.3700 1.3700 1.3700 0.0000 0.0000 0.0000 651 ASP B CA  
5049 C C   . ASP A 668 ? 1.3700 1.3700 1.3700 0.0000 0.0000 0.0000 651 ASP B C   
5050 O O   . ASP A 668 ? 1.3700 1.3700 1.3700 0.0000 0.0000 0.0000 651 ASP B O   
5051 C CB  . ASP A 668 ? 1.3700 1.3700 1.3700 0.0000 0.0000 0.0000 651 ASP B CB  
5052 C CG  . ASP A 668 ? 1.3700 1.3700 1.3700 0.0000 0.0000 0.0000 651 ASP B CG  
5053 O OD1 . ASP A 668 ? 1.3700 1.3700 1.3700 0.0000 0.0000 0.0000 651 ASP B OD1 
5054 O OD2 . ASP A 668 ? 1.3700 1.3700 1.3700 0.0000 0.0000 0.0000 651 ASP B OD2 
5055 N N   . PHE A 669 ? 1.2493 1.2493 1.2493 0.0000 0.0000 0.0000 652 PHE B N   
5056 C CA  . PHE A 669 ? 1.2493 1.2493 1.2493 0.0000 0.0000 0.0000 652 PHE B CA  
5057 C C   . PHE A 669 ? 1.2493 1.2493 1.2493 0.0000 0.0000 0.0000 652 PHE B C   
5058 O O   . PHE A 669 ? 1.2493 1.2493 1.2493 0.0000 0.0000 0.0000 652 PHE B O   
5059 C CB  . PHE A 669 ? 1.2493 1.2493 1.2493 0.0000 0.0000 0.0000 652 PHE B CB  
5060 C CG  . PHE A 669 ? 1.2493 1.2493 1.2493 0.0000 0.0000 0.0000 652 PHE B CG  
5061 C CD1 . PHE A 669 ? 1.2493 1.2493 1.2493 0.0000 0.0000 0.0000 652 PHE B CD1 
5062 C CD2 . PHE A 669 ? 1.2493 1.2493 1.2493 0.0000 0.0000 0.0000 652 PHE B CD2 
5063 C CE1 . PHE A 669 ? 1.2493 1.2493 1.2493 0.0000 0.0000 0.0000 652 PHE B CE1 
5064 C CE2 . PHE A 669 ? 1.2493 1.2493 1.2493 0.0000 0.0000 0.0000 652 PHE B CE2 
5065 C CZ  . PHE A 669 ? 1.2493 1.2493 1.2493 0.0000 0.0000 0.0000 652 PHE B CZ  
5066 N N   . VAL A 670 ? 1.2338 1.2338 1.2338 0.0000 0.0000 0.0000 653 VAL B N   
5067 C CA  . VAL A 670 ? 1.2338 1.2338 1.2338 0.0000 0.0000 0.0000 653 VAL B CA  
5068 C C   . VAL A 670 ? 1.2338 1.2338 1.2338 0.0000 0.0000 0.0000 653 VAL B C   
5069 O O   . VAL A 670 ? 1.2338 1.2338 1.2338 0.0000 0.0000 0.0000 653 VAL B O   
5070 C CB  . VAL A 670 ? 1.2338 1.2338 1.2338 0.0000 0.0000 0.0000 653 VAL B CB  
5071 C CG1 . VAL A 670 ? 1.2338 1.2338 1.2338 0.0000 0.0000 0.0000 653 VAL B CG1 
5072 C CG2 . VAL A 670 ? 1.2338 1.2338 1.2338 0.0000 0.0000 0.0000 653 VAL B CG2 
5073 N N   . GLY A 671 ? 1.2032 1.2032 1.2032 0.0000 0.0000 0.0000 654 GLY B N   
5074 C CA  . GLY A 671 ? 1.2032 1.2032 1.2032 0.0000 0.0000 0.0000 654 GLY B CA  
5075 C C   . GLY A 671 ? 1.2032 1.2032 1.2032 0.0000 0.0000 0.0000 654 GLY B C   
5076 O O   . GLY A 671 ? 1.2032 1.2032 1.2032 0.0000 0.0000 0.0000 654 GLY B O   
5077 N N   . ALA A 672 ? 1.1442 1.1442 1.1442 0.0000 0.0000 0.0000 655 ALA B N   
5078 C CA  . ALA A 672 ? 1.1442 1.1442 1.1442 0.0000 0.0000 0.0000 655 ALA B CA  
5079 C C   . ALA A 672 ? 1.1442 1.1442 1.1442 0.0000 0.0000 0.0000 655 ALA B C   
5080 O O   . ALA A 672 ? 1.1442 1.1442 1.1442 0.0000 0.0000 0.0000 655 ALA B O   
5081 C CB  . ALA A 672 ? 1.1442 1.1442 1.1442 0.0000 0.0000 0.0000 655 ALA B CB  
5082 N N   . LEU A 673 ? 1.1023 1.1023 1.1023 0.0000 0.0000 0.0000 656 LEU B N   
5083 C CA  . LEU A 673 ? 1.1023 1.1023 1.1023 0.0000 0.0000 0.0000 656 LEU B CA  
5084 C C   . LEU A 673 ? 1.1023 1.1023 1.1023 0.0000 0.0000 0.0000 656 LEU B C   
5085 O O   . LEU A 673 ? 1.1023 1.1023 1.1023 0.0000 0.0000 0.0000 656 LEU B O   
5086 C CB  . LEU A 673 ? 1.1023 1.1023 1.1023 0.0000 0.0000 0.0000 656 LEU B CB  
5087 C CG  . LEU A 673 ? 1.1023 1.1023 1.1023 0.0000 0.0000 0.0000 656 LEU B CG  
5088 C CD1 . LEU A 673 ? 1.1023 1.1023 1.1023 0.0000 0.0000 0.0000 656 LEU B CD1 
5089 C CD2 . LEU A 673 ? 1.1023 1.1023 1.1023 0.0000 0.0000 0.0000 656 LEU B CD2 
5090 N N   . ILE A 674 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 657 ILE B N   
5091 C CA  . ILE A 674 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 657 ILE B CA  
5092 C C   . ILE A 674 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 657 ILE B C   
5093 O O   . ILE A 674 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 657 ILE B O   
5094 C CB  . ILE A 674 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 657 ILE B CB  
5095 C CG1 . ILE A 674 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 657 ILE B CG1 
5096 C CG2 . ILE A 674 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 657 ILE B CG2 
5097 C CD1 . ILE A 674 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 657 ILE B CD1 
5098 N N   . PHE A 675 ? 1.0099 1.0099 1.0099 0.0000 0.0000 0.0000 658 PHE B N   
5099 C CA  . PHE A 675 ? 1.0099 1.0099 1.0099 0.0000 0.0000 0.0000 658 PHE B CA  
5100 C C   . PHE A 675 ? 1.0099 1.0099 1.0099 0.0000 0.0000 0.0000 658 PHE B C   
5101 O O   . PHE A 675 ? 1.0099 1.0099 1.0099 0.0000 0.0000 0.0000 658 PHE B O   
5102 C CB  . PHE A 675 ? 1.0099 1.0099 1.0099 0.0000 0.0000 0.0000 658 PHE B CB  
5103 C CG  . PHE A 675 ? 1.0099 1.0099 1.0099 0.0000 0.0000 0.0000 658 PHE B CG  
5104 C CD1 . PHE A 675 ? 1.0099 1.0099 1.0099 0.0000 0.0000 0.0000 658 PHE B CD1 
5105 C CD2 . PHE A 675 ? 1.0099 1.0099 1.0099 0.0000 0.0000 0.0000 658 PHE B CD2 
5106 C CE1 . PHE A 675 ? 1.0099 1.0099 1.0099 0.0000 0.0000 0.0000 658 PHE B CE1 
5107 C CE2 . PHE A 675 ? 1.0099 1.0099 1.0099 0.0000 0.0000 0.0000 658 PHE B CE2 
5108 C CZ  . PHE A 675 ? 1.0099 1.0099 1.0099 0.0000 0.0000 0.0000 658 PHE B CZ  
5109 N N   . SER A 676 ? 1.0150 1.0150 1.0150 0.0000 0.0000 0.0000 659 SER B N   
5110 C CA  . SER A 676 ? 1.0150 1.0150 1.0150 0.0000 0.0000 0.0000 659 SER B CA  
5111 C C   . SER A 676 ? 1.0150 1.0150 1.0150 0.0000 0.0000 0.0000 659 SER B C   
5112 O O   . SER A 676 ? 1.0150 1.0150 1.0150 0.0000 0.0000 0.0000 659 SER B O   
5113 C CB  . SER A 676 ? 1.0150 1.0150 1.0150 0.0000 0.0000 0.0000 659 SER B CB  
5114 O OG  . SER A 676 ? 1.0150 1.0150 1.0150 0.0000 0.0000 0.0000 659 SER B OG  
5115 N N   . GLY A 677 ? 1.0187 1.0187 1.0187 0.0000 0.0000 0.0000 660 GLY B N   
5116 C CA  . GLY A 677 ? 1.0187 1.0187 1.0187 0.0000 0.0000 0.0000 660 GLY B CA  
5117 C C   . GLY A 677 ? 1.0187 1.0187 1.0187 0.0000 0.0000 0.0000 660 GLY B C   
5118 O O   . GLY A 677 ? 1.0187 1.0187 1.0187 0.0000 0.0000 0.0000 660 GLY B O   
5119 N N   . ALA A 678 ? 0.9473 0.9473 0.9473 0.0000 0.0000 0.0000 661 ALA B N   
5120 C CA  . ALA A 678 ? 0.9473 0.9473 0.9473 0.0000 0.0000 0.0000 661 ALA B CA  
5121 C C   . ALA A 678 ? 0.9473 0.9473 0.9473 0.0000 0.0000 0.0000 661 ALA B C   
5122 O O   . ALA A 678 ? 0.9473 0.9473 0.9473 0.0000 0.0000 0.0000 661 ALA B O   
5123 C CB  . ALA A 678 ? 0.9473 0.9473 0.9473 0.0000 0.0000 0.0000 661 ALA B CB  
5124 N N   . VAL A 679 ? 0.9454 0.9454 0.9454 0.0000 0.0000 0.0000 662 VAL B N   
5125 C CA  . VAL A 679 ? 0.9454 0.9454 0.9454 0.0000 0.0000 0.0000 662 VAL B CA  
5126 C C   . VAL A 679 ? 0.9454 0.9454 0.9454 0.0000 0.0000 0.0000 662 VAL B C   
5127 O O   . VAL A 679 ? 0.9454 0.9454 0.9454 0.0000 0.0000 0.0000 662 VAL B O   
5128 C CB  . VAL A 679 ? 0.9454 0.9454 0.9454 0.0000 0.0000 0.0000 662 VAL B CB  
5129 C CG1 . VAL A 679 ? 0.9454 0.9454 0.9454 0.0000 0.0000 0.0000 662 VAL B CG1 
5130 C CG2 . VAL A 679 ? 0.9454 0.9454 0.9454 0.0000 0.0000 0.0000 662 VAL B CG2 
5131 N N   . ILE A 680 ? 1.0131 1.0131 1.0131 0.0000 0.0000 0.0000 663 ILE B N   
5132 C CA  . ILE A 680 ? 1.0131 1.0131 1.0131 0.0000 0.0000 0.0000 663 ILE B CA  
5133 C C   . ILE A 680 ? 1.0131 1.0131 1.0131 0.0000 0.0000 0.0000 663 ILE B C   
5134 O O   . ILE A 680 ? 1.0131 1.0131 1.0131 0.0000 0.0000 0.0000 663 ILE B O   
5135 C CB  . ILE A 680 ? 1.0131 1.0131 1.0131 0.0000 0.0000 0.0000 663 ILE B CB  
5136 C CG1 . ILE A 680 ? 1.0131 1.0131 1.0131 0.0000 0.0000 0.0000 663 ILE B CG1 
5137 C CG2 . ILE A 680 ? 1.0131 1.0131 1.0131 0.0000 0.0000 0.0000 663 ILE B CG2 
5138 C CD1 . ILE A 680 ? 1.0131 1.0131 1.0131 0.0000 0.0000 0.0000 663 ILE B CD1 
5139 N N   . LEU A 681 ? 0.9410 0.9410 0.9410 0.0000 0.0000 0.0000 664 LEU B N   
5140 C CA  . LEU A 681 ? 0.9410 0.9410 0.9410 0.0000 0.0000 0.0000 664 LEU B CA  
5141 C C   . LEU A 681 ? 0.9410 0.9410 0.9410 0.0000 0.0000 0.0000 664 LEU B C   
5142 O O   . LEU A 681 ? 0.9410 0.9410 0.9410 0.0000 0.0000 0.0000 664 LEU B O   
5143 C CB  . LEU A 681 ? 0.9410 0.9410 0.9410 0.0000 0.0000 0.0000 664 LEU B CB  
5144 C CG  . LEU A 681 ? 0.9410 0.9410 0.9410 0.0000 0.0000 0.0000 664 LEU B CG  
5145 C CD1 . LEU A 681 ? 0.9410 0.9410 0.9410 0.0000 0.0000 0.0000 664 LEU B CD1 
5146 C CD2 . LEU A 681 ? 0.9410 0.9410 0.9410 0.0000 0.0000 0.0000 664 LEU B CD2 
5147 N N   . LEU A 682 ? 0.8964 0.8964 0.8964 0.0000 0.0000 0.0000 665 LEU B N   
5148 C CA  . LEU A 682 ? 0.8964 0.8964 0.8964 0.0000 0.0000 0.0000 665 LEU B CA  
5149 C C   . LEU A 682 ? 0.8964 0.8964 0.8964 0.0000 0.0000 0.0000 665 LEU B C   
5150 O O   . LEU A 682 ? 0.8964 0.8964 0.8964 0.0000 0.0000 0.0000 665 LEU B O   
5151 C CB  . LEU A 682 ? 0.8964 0.8964 0.8964 0.0000 0.0000 0.0000 665 LEU B CB  
5152 C CG  . LEU A 682 ? 0.8964 0.8964 0.8964 0.0000 0.0000 0.0000 665 LEU B CG  
5153 C CD1 . LEU A 682 ? 0.8964 0.8964 0.8964 0.0000 0.0000 0.0000 665 LEU B CD1 
5154 C CD2 . LEU A 682 ? 0.8964 0.8964 0.8964 0.0000 0.0000 0.0000 665 LEU B CD2 
5155 N N   . GLU A 683 ? 0.9503 0.9503 0.9503 0.0000 0.0000 0.0000 666 GLU B N   
5156 C CA  . GLU A 683 ? 0.9503 0.9503 0.9503 0.0000 0.0000 0.0000 666 GLU B CA  
5157 C C   . GLU A 683 ? 0.9503 0.9503 0.9503 0.0000 0.0000 0.0000 666 GLU B C   
5158 O O   . GLU A 683 ? 0.9503 0.9503 0.9503 0.0000 0.0000 0.0000 666 GLU B O   
5159 C CB  . GLU A 683 ? 0.9503 0.9503 0.9503 0.0000 0.0000 0.0000 666 GLU B CB  
5160 C CG  . GLU A 683 ? 0.9503 0.9503 0.9503 0.0000 0.0000 0.0000 666 GLU B CG  
5161 C CD  . GLU A 683 ? 0.9503 0.9503 0.9503 0.0000 0.0000 0.0000 666 GLU B CD  
5162 O OE1 . GLU A 683 ? 0.9503 0.9503 0.9503 0.0000 0.0000 0.0000 666 GLU B OE1 
5163 O OE2 . GLU A 683 ? 0.9503 0.9503 0.9503 0.0000 0.0000 0.0000 666 GLU B OE2 
5164 N N   . PHE A 684 ? 0.9052 0.9052 0.9052 0.0000 0.0000 0.0000 667 PHE B N   
5165 C CA  . PHE A 684 ? 0.9052 0.9052 0.9052 0.0000 0.0000 0.0000 667 PHE B CA  
5166 C C   . PHE A 684 ? 0.9052 0.9052 0.9052 0.0000 0.0000 0.0000 667 PHE B C   
5167 O O   . PHE A 684 ? 0.9052 0.9052 0.9052 0.0000 0.0000 0.0000 667 PHE B O   
5168 C CB  . PHE A 684 ? 0.9052 0.9052 0.9052 0.0000 0.0000 0.0000 667 PHE B CB  
5169 C CG  . PHE A 684 ? 0.9052 0.9052 0.9052 0.0000 0.0000 0.0000 667 PHE B CG  
5170 C CD1 . PHE A 684 ? 0.9052 0.9052 0.9052 0.0000 0.0000 0.0000 667 PHE B CD1 
5171 C CD2 . PHE A 684 ? 0.9052 0.9052 0.9052 0.0000 0.0000 0.0000 667 PHE B CD2 
5172 C CE1 . PHE A 684 ? 0.9052 0.9052 0.9052 0.0000 0.0000 0.0000 667 PHE B CE1 
5173 C CE2 . PHE A 684 ? 0.9052 0.9052 0.9052 0.0000 0.0000 0.0000 667 PHE B CE2 
5174 C CZ  . PHE A 684 ? 0.9052 0.9052 0.9052 0.0000 0.0000 0.0000 667 PHE B CZ  
5175 N N   . ILE A 685 ? 0.9217 0.9217 0.9217 0.0000 0.0000 0.0000 668 ILE B N   
5176 C CA  . ILE A 685 ? 0.9217 0.9217 0.9217 0.0000 0.0000 0.0000 668 ILE B CA  
5177 C C   . ILE A 685 ? 0.9217 0.9217 0.9217 0.0000 0.0000 0.0000 668 ILE B C   
5178 O O   . ILE A 685 ? 0.9217 0.9217 0.9217 0.0000 0.0000 0.0000 668 ILE B O   
5179 C CB  . ILE A 685 ? 0.9217 0.9217 0.9217 0.0000 0.0000 0.0000 668 ILE B CB  
5180 C CG1 . ILE A 685 ? 0.9217 0.9217 0.9217 0.0000 0.0000 0.0000 668 ILE B CG1 
5181 C CG2 . ILE A 685 ? 0.9217 0.9217 0.9217 0.0000 0.0000 0.0000 668 ILE B CG2 
5182 C CD1 . ILE A 685 ? 0.9217 0.9217 0.9217 0.0000 0.0000 0.0000 668 ILE B CD1 
5183 N N   . PRO A 686 ? 0.8994 0.8994 0.8994 0.0000 0.0000 0.0000 669 PRO B N   
5184 C CA  . PRO A 686 ? 0.8994 0.8994 0.8994 0.0000 0.0000 0.0000 669 PRO B CA  
5185 C C   . PRO A 686 ? 0.8994 0.8994 0.8994 0.0000 0.0000 0.0000 669 PRO B C   
5186 O O   . PRO A 686 ? 0.8994 0.8994 0.8994 0.0000 0.0000 0.0000 669 PRO B O   
5187 C CB  . PRO A 686 ? 0.8994 0.8994 0.8994 0.0000 0.0000 0.0000 669 PRO B CB  
5188 C CG  . PRO A 686 ? 0.8994 0.8994 0.8994 0.0000 0.0000 0.0000 669 PRO B CG  
5189 C CD  . PRO A 686 ? 0.8994 0.8994 0.8994 0.0000 0.0000 0.0000 669 PRO B CD  
5190 N N   . GLU A 687 ? 0.9611 0.9611 0.9611 0.0000 0.0000 0.0000 670 GLU B N   
5191 C CA  . GLU A 687 ? 0.9611 0.9611 0.9611 0.0000 0.0000 0.0000 670 GLU B CA  
5192 C C   . GLU A 687 ? 0.9611 0.9611 0.9611 0.0000 0.0000 0.0000 670 GLU B C   
5193 O O   . GLU A 687 ? 0.9611 0.9611 0.9611 0.0000 0.0000 0.0000 670 GLU B O   
5194 C CB  . GLU A 687 ? 0.9611 0.9611 0.9611 0.0000 0.0000 0.0000 670 GLU B CB  
5195 C CG  . GLU A 687 ? 0.9611 0.9611 0.9611 0.0000 0.0000 0.0000 670 GLU B CG  
5196 C CD  . GLU A 687 ? 0.9611 0.9611 0.9611 0.0000 0.0000 0.0000 670 GLU B CD  
5197 O OE1 . GLU A 687 ? 0.9611 0.9611 0.9611 0.0000 0.0000 0.0000 670 GLU B OE1 
5198 O OE2 . GLU A 687 ? 0.9611 0.9611 0.9611 0.0000 0.0000 0.0000 670 GLU B OE2 
5199 N N   . ILE A 688 ? 0.9285 0.9285 0.9285 0.0000 0.0000 0.0000 671 ILE B N   
5200 C CA  . ILE A 688 ? 0.9285 0.9285 0.9285 0.0000 0.0000 0.0000 671 ILE B CA  
5201 C C   . ILE A 688 ? 0.9285 0.9285 0.9285 0.0000 0.0000 0.0000 671 ILE B C   
5202 O O   . ILE A 688 ? 0.9285 0.9285 0.9285 0.0000 0.0000 0.0000 671 ILE B O   
5203 C CB  . ILE A 688 ? 0.9285 0.9285 0.9285 0.0000 0.0000 0.0000 671 ILE B CB  
5204 C CG1 . ILE A 688 ? 0.9285 0.9285 0.9285 0.0000 0.0000 0.0000 671 ILE B CG1 
5205 C CG2 . ILE A 688 ? 0.9285 0.9285 0.9285 0.0000 0.0000 0.0000 671 ILE B CG2 
5206 C CD1 . ILE A 688 ? 0.9285 0.9285 0.9285 0.0000 0.0000 0.0000 671 ILE B CD1 
5207 N N   . ALA A 689 ? 0.9307 0.9307 0.9307 0.0000 0.0000 0.0000 672 ALA B N   
5208 C CA  . ALA A 689 ? 0.9307 0.9307 0.9307 0.0000 0.0000 0.0000 672 ALA B CA  
5209 C C   . ALA A 689 ? 0.9307 0.9307 0.9307 0.0000 0.0000 0.0000 672 ALA B C   
5210 O O   . ALA A 689 ? 0.9307 0.9307 0.9307 0.0000 0.0000 0.0000 672 ALA B O   
5211 C CB  . ALA A 689 ? 0.9307 0.9307 0.9307 0.0000 0.0000 0.0000 672 ALA B CB  
5212 N N   . ILE A 690 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 673 ILE B N   
5213 C CA  . ILE A 690 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 673 ILE B CA  
5214 C C   . ILE A 690 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 673 ILE B C   
5215 O O   . ILE A 690 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 673 ILE B O   
5216 C CB  . ILE A 690 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 673 ILE B CB  
5217 C CG1 . ILE A 690 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 673 ILE B CG1 
5218 C CG2 . ILE A 690 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 673 ILE B CG2 
5219 C CD1 . ILE A 690 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 673 ILE B CD1 
5220 N N   . PRO A 691 ? 0.9461 0.9461 0.9461 0.0000 0.0000 0.0000 674 PRO B N   
5221 C CA  . PRO A 691 ? 0.9461 0.9461 0.9461 0.0000 0.0000 0.0000 674 PRO B CA  
5222 C C   . PRO A 691 ? 0.9461 0.9461 0.9461 0.0000 0.0000 0.0000 674 PRO B C   
5223 O O   . PRO A 691 ? 0.9461 0.9461 0.9461 0.0000 0.0000 0.0000 674 PRO B O   
5224 C CB  . PRO A 691 ? 0.9461 0.9461 0.9461 0.0000 0.0000 0.0000 674 PRO B CB  
5225 C CG  . PRO A 691 ? 0.9461 0.9461 0.9461 0.0000 0.0000 0.0000 674 PRO B CG  
5226 C CD  . PRO A 691 ? 0.9461 0.9461 0.9461 0.0000 0.0000 0.0000 674 PRO B CD  
5227 N N   . VAL A 692 ? 0.9397 0.9397 0.9397 0.0000 0.0000 0.0000 675 VAL B N   
5228 C CA  . VAL A 692 ? 0.9397 0.9397 0.9397 0.0000 0.0000 0.0000 675 VAL B CA  
5229 C C   . VAL A 692 ? 0.9397 0.9397 0.9397 0.0000 0.0000 0.0000 675 VAL B C   
5230 O O   . VAL A 692 ? 0.9397 0.9397 0.9397 0.0000 0.0000 0.0000 675 VAL B O   
5231 C CB  . VAL A 692 ? 0.9397 0.9397 0.9397 0.0000 0.0000 0.0000 675 VAL B CB  
5232 C CG1 . VAL A 692 ? 0.9397 0.9397 0.9397 0.0000 0.0000 0.0000 675 VAL B CG1 
5233 C CG2 . VAL A 692 ? 0.9397 0.9397 0.9397 0.0000 0.0000 0.0000 675 VAL B CG2 
5234 N N   . LEU A 693 ? 0.8877 0.8877 0.8877 0.0000 0.0000 0.0000 676 LEU B N   
5235 C CA  . LEU A 693 ? 0.8877 0.8877 0.8877 0.0000 0.0000 0.0000 676 LEU B CA  
5236 C C   . LEU A 693 ? 0.8877 0.8877 0.8877 0.0000 0.0000 0.0000 676 LEU B C   
5237 O O   . LEU A 693 ? 0.8877 0.8877 0.8877 0.0000 0.0000 0.0000 676 LEU B O   
5238 C CB  . LEU A 693 ? 0.8877 0.8877 0.8877 0.0000 0.0000 0.0000 676 LEU B CB  
5239 C CG  . LEU A 693 ? 0.8877 0.8877 0.8877 0.0000 0.0000 0.0000 676 LEU B CG  
5240 C CD1 . LEU A 693 ? 0.8877 0.8877 0.8877 0.0000 0.0000 0.0000 676 LEU B CD1 
5241 C CD2 . LEU A 693 ? 0.8877 0.8877 0.8877 0.0000 0.0000 0.0000 676 LEU B CD2 
5242 N N   . GLY A 694 ? 0.9304 0.9304 0.9304 0.0000 0.0000 0.0000 677 GLY B N   
5243 C CA  . GLY A 694 ? 0.9304 0.9304 0.9304 0.0000 0.0000 0.0000 677 GLY B CA  
5244 C C   . GLY A 694 ? 0.9304 0.9304 0.9304 0.0000 0.0000 0.0000 677 GLY B C   
5245 O O   . GLY A 694 ? 0.9304 0.9304 0.9304 0.0000 0.0000 0.0000 677 GLY B O   
5246 N N   . THR A 695 ? 1.0018 1.0018 1.0018 0.0000 0.0000 0.0000 678 THR B N   
5247 C CA  . THR A 695 ? 1.0018 1.0018 1.0018 0.0000 0.0000 0.0000 678 THR B CA  
5248 C C   . THR A 695 ? 1.0018 1.0018 1.0018 0.0000 0.0000 0.0000 678 THR B C   
5249 O O   . THR A 695 ? 1.0018 1.0018 1.0018 0.0000 0.0000 0.0000 678 THR B O   
5250 C CB  . THR A 695 ? 1.0018 1.0018 1.0018 0.0000 0.0000 0.0000 678 THR B CB  
5251 O OG1 . THR A 695 ? 1.0018 1.0018 1.0018 0.0000 0.0000 0.0000 678 THR B OG1 
5252 C CG2 . THR A 695 ? 1.0018 1.0018 1.0018 0.0000 0.0000 0.0000 678 THR B CG2 
5253 N N   . PHE A 696 ? 0.9182 0.9182 0.9182 0.0000 0.0000 0.0000 679 PHE B N   
5254 C CA  . PHE A 696 ? 0.9182 0.9182 0.9182 0.0000 0.0000 0.0000 679 PHE B CA  
5255 C C   . PHE A 696 ? 0.9182 0.9182 0.9182 0.0000 0.0000 0.0000 679 PHE B C   
5256 O O   . PHE A 696 ? 0.9182 0.9182 0.9182 0.0000 0.0000 0.0000 679 PHE B O   
5257 C CB  . PHE A 696 ? 0.9182 0.9182 0.9182 0.0000 0.0000 0.0000 679 PHE B CB  
5258 C CG  . PHE A 696 ? 0.9182 0.9182 0.9182 0.0000 0.0000 0.0000 679 PHE B CG  
5259 C CD1 . PHE A 696 ? 0.9182 0.9182 0.9182 0.0000 0.0000 0.0000 679 PHE B CD1 
5260 C CD2 . PHE A 696 ? 0.9182 0.9182 0.9182 0.0000 0.0000 0.0000 679 PHE B CD2 
5261 C CE1 . PHE A 696 ? 0.9182 0.9182 0.9182 0.0000 0.0000 0.0000 679 PHE B CE1 
5262 C CE2 . PHE A 696 ? 0.9182 0.9182 0.9182 0.0000 0.0000 0.0000 679 PHE B CE2 
5263 C CZ  . PHE A 696 ? 0.9182 0.9182 0.9182 0.0000 0.0000 0.0000 679 PHE B CZ  
5264 N N   . ALA A 697 ? 0.9934 0.9934 0.9934 0.0000 0.0000 0.0000 680 ALA B N   
5265 C CA  . ALA A 697 ? 0.9934 0.9934 0.9934 0.0000 0.0000 0.0000 680 ALA B CA  
5266 C C   . ALA A 697 ? 0.9934 0.9934 0.9934 0.0000 0.0000 0.0000 680 ALA B C   
5267 O O   . ALA A 697 ? 0.9934 0.9934 0.9934 0.0000 0.0000 0.0000 680 ALA B O   
5268 C CB  . ALA A 697 ? 0.9934 0.9934 0.9934 0.0000 0.0000 0.0000 680 ALA B CB  
5269 N N   . LEU A 698 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 681 LEU B N   
5270 C CA  . LEU A 698 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 681 LEU B CA  
5271 C C   . LEU A 698 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 681 LEU B C   
5272 O O   . LEU A 698 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 681 LEU B O   
5273 C CB  . LEU A 698 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 681 LEU B CB  
5274 C CG  . LEU A 698 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 681 LEU B CG  
5275 C CD1 . LEU A 698 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 681 LEU B CD1 
5276 C CD2 . LEU A 698 ? 0.9272 0.9272 0.9272 0.0000 0.0000 0.0000 681 LEU B CD2 
5277 N N   . VAL A 699 ? 0.9763 0.9763 0.9763 0.0000 0.0000 0.0000 682 VAL B N   
5278 C CA  . VAL A 699 ? 0.9763 0.9763 0.9763 0.0000 0.0000 0.0000 682 VAL B CA  
5279 C C   . VAL A 699 ? 0.9763 0.9763 0.9763 0.0000 0.0000 0.0000 682 VAL B C   
5280 O O   . VAL A 699 ? 0.9763 0.9763 0.9763 0.0000 0.0000 0.0000 682 VAL B O   
5281 C CB  . VAL A 699 ? 0.9763 0.9763 0.9763 0.0000 0.0000 0.0000 682 VAL B CB  
5282 C CG1 . VAL A 699 ? 0.9763 0.9763 0.9763 0.0000 0.0000 0.0000 682 VAL B CG1 
5283 C CG2 . VAL A 699 ? 0.9763 0.9763 0.9763 0.0000 0.0000 0.0000 682 VAL B CG2 
5284 N N   . SER A 700 ? 1.0333 1.0333 1.0333 0.0000 0.0000 0.0000 683 SER B N   
5285 C CA  . SER A 700 ? 1.0333 1.0333 1.0333 0.0000 0.0000 0.0000 683 SER B CA  
5286 C C   . SER A 700 ? 1.0333 1.0333 1.0333 0.0000 0.0000 0.0000 683 SER B C   
5287 O O   . SER A 700 ? 1.0333 1.0333 1.0333 0.0000 0.0000 0.0000 683 SER B O   
5288 C CB  . SER A 700 ? 1.0333 1.0333 1.0333 0.0000 0.0000 0.0000 683 SER B CB  
5289 O OG  . SER A 700 ? 1.0333 1.0333 1.0333 0.0000 0.0000 0.0000 683 SER B OG  
5290 N N   . TYR A 701 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 684 TYR B N   
5291 C CA  . TYR A 701 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 684 TYR B CA  
5292 C C   . TYR A 701 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 684 TYR B C   
5293 O O   . TYR A 701 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 684 TYR B O   
5294 C CB  . TYR A 701 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 684 TYR B CB  
5295 C CG  . TYR A 701 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 684 TYR B CG  
5296 C CD1 . TYR A 701 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 684 TYR B CD1 
5297 C CD2 . TYR A 701 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 684 TYR B CD2 
5298 C CE1 . TYR A 701 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 684 TYR B CE1 
5299 C CE2 . TYR A 701 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 684 TYR B CE2 
5300 C CZ  . TYR A 701 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 684 TYR B CZ  
5301 O OH  . TYR A 701 ? 1.0539 1.0539 1.0539 0.0000 0.0000 0.0000 684 TYR B OH  
5302 N N   . ILE A 702 ? 1.1121 1.1121 1.1121 0.0000 0.0000 0.0000 685 ILE B N   
5303 C CA  . ILE A 702 ? 1.1121 1.1121 1.1121 0.0000 0.0000 0.0000 685 ILE B CA  
5304 C C   . ILE A 702 ? 1.1121 1.1121 1.1121 0.0000 0.0000 0.0000 685 ILE B C   
5305 O O   . ILE A 702 ? 1.1121 1.1121 1.1121 0.0000 0.0000 0.0000 685 ILE B O   
5306 C CB  . ILE A 702 ? 1.1121 1.1121 1.1121 0.0000 0.0000 0.0000 685 ILE B CB  
5307 C CG1 . ILE A 702 ? 1.1121 1.1121 1.1121 0.0000 0.0000 0.0000 685 ILE B CG1 
5308 C CG2 . ILE A 702 ? 1.1121 1.1121 1.1121 0.0000 0.0000 0.0000 685 ILE B CG2 
5309 C CD1 . ILE A 702 ? 1.1121 1.1121 1.1121 0.0000 0.0000 0.0000 685 ILE B CD1 
5310 N N   . ALA A 703 ? 1.0930 1.0930 1.0930 0.0000 0.0000 0.0000 686 ALA B N   
5311 C CA  . ALA A 703 ? 1.0930 1.0930 1.0930 0.0000 0.0000 0.0000 686 ALA B CA  
5312 C C   . ALA A 703 ? 1.0930 1.0930 1.0930 0.0000 0.0000 0.0000 686 ALA B C   
5313 O O   . ALA A 703 ? 1.0930 1.0930 1.0930 0.0000 0.0000 0.0000 686 ALA B O   
5314 C CB  . ALA A 703 ? 1.0930 1.0930 1.0930 0.0000 0.0000 0.0000 686 ALA B CB  
5315 N N   . ASN A 704 ? 1.0670 1.0670 1.0670 0.0000 0.0000 0.0000 687 ASN B N   
5316 C CA  . ASN A 704 ? 1.0670 1.0670 1.0670 0.0000 0.0000 0.0000 687 ASN B CA  
5317 C C   . ASN A 704 ? 1.0670 1.0670 1.0670 0.0000 0.0000 0.0000 687 ASN B C   
5318 O O   . ASN A 704 ? 1.0670 1.0670 1.0670 0.0000 0.0000 0.0000 687 ASN B O   
5319 C CB  . ASN A 704 ? 1.0670 1.0670 1.0670 0.0000 0.0000 0.0000 687 ASN B CB  
5320 C CG  . ASN A 704 ? 1.0670 1.0670 1.0670 0.0000 0.0000 0.0000 687 ASN B CG  
5321 O OD1 . ASN A 704 ? 1.0670 1.0670 1.0670 0.0000 0.0000 0.0000 687 ASN B OD1 
5322 N ND2 . ASN A 704 ? 1.0670 1.0670 1.0670 0.0000 0.0000 0.0000 687 ASN B ND2 
5323 N N   . LYS A 705 ? 0.9506 0.9506 0.9506 0.0000 0.0000 0.0000 688 LYS B N   
5324 C CA  . LYS A 705 ? 0.9506 0.9506 0.9506 0.0000 0.0000 0.0000 688 LYS B CA  
5325 C C   . LYS A 705 ? 0.9506 0.9506 0.9506 0.0000 0.0000 0.0000 688 LYS B C   
5326 O O   . LYS A 705 ? 0.9506 0.9506 0.9506 0.0000 0.0000 0.0000 688 LYS B O   
5327 C CB  . LYS A 705 ? 0.9506 0.9506 0.9506 0.0000 0.0000 0.0000 688 LYS B CB  
5328 C CG  . LYS A 705 ? 0.9506 0.9506 0.9506 0.0000 0.0000 0.0000 688 LYS B CG  
5329 C CD  . LYS A 705 ? 0.9506 0.9506 0.9506 0.0000 0.0000 0.0000 688 LYS B CD  
5330 C CE  . LYS A 705 ? 0.9506 0.9506 0.9506 0.0000 0.0000 0.0000 688 LYS B CE  
5331 N NZ  . LYS A 705 ? 0.9506 0.9506 0.9506 0.0000 0.0000 0.0000 688 LYS B NZ  
5332 N N   . VAL A 706 ? 0.9906 0.9906 0.9906 0.0000 0.0000 0.0000 689 VAL B N   
5333 C CA  . VAL A 706 ? 0.9906 0.9906 0.9906 0.0000 0.0000 0.0000 689 VAL B CA  
5334 C C   . VAL A 706 ? 0.9906 0.9906 0.9906 0.0000 0.0000 0.0000 689 VAL B C   
5335 O O   . VAL A 706 ? 0.9906 0.9906 0.9906 0.0000 0.0000 0.0000 689 VAL B O   
5336 C CB  . VAL A 706 ? 0.9906 0.9906 0.9906 0.0000 0.0000 0.0000 689 VAL B CB  
5337 C CG1 . VAL A 706 ? 0.9906 0.9906 0.9906 0.0000 0.0000 0.0000 689 VAL B CG1 
5338 C CG2 . VAL A 706 ? 0.9906 0.9906 0.9906 0.0000 0.0000 0.0000 689 VAL B CG2 
5339 N N   . LEU A 707 ? 0.9715 0.9715 0.9715 0.0000 0.0000 0.0000 690 LEU B N   
5340 C CA  . LEU A 707 ? 0.9715 0.9715 0.9715 0.0000 0.0000 0.0000 690 LEU B CA  
5341 C C   . LEU A 707 ? 0.9715 0.9715 0.9715 0.0000 0.0000 0.0000 690 LEU B C   
5342 O O   . LEU A 707 ? 0.9715 0.9715 0.9715 0.0000 0.0000 0.0000 690 LEU B O   
5343 C CB  . LEU A 707 ? 0.9715 0.9715 0.9715 0.0000 0.0000 0.0000 690 LEU B CB  
5344 C CG  . LEU A 707 ? 0.9715 0.9715 0.9715 0.0000 0.0000 0.0000 690 LEU B CG  
5345 C CD1 . LEU A 707 ? 0.9715 0.9715 0.9715 0.0000 0.0000 0.0000 690 LEU B CD1 
5346 C CD2 . LEU A 707 ? 0.9715 0.9715 0.9715 0.0000 0.0000 0.0000 690 LEU B CD2 
5347 N N   . THR A 708 ? 0.9149 0.9149 0.9149 0.0000 0.0000 0.0000 691 THR B N   
5348 C CA  . THR A 708 ? 0.9149 0.9149 0.9149 0.0000 0.0000 0.0000 691 THR B CA  
5349 C C   . THR A 708 ? 0.9149 0.9149 0.9149 0.0000 0.0000 0.0000 691 THR B C   
5350 O O   . THR A 708 ? 0.9149 0.9149 0.9149 0.0000 0.0000 0.0000 691 THR B O   
5351 C CB  . THR A 708 ? 0.9149 0.9149 0.9149 0.0000 0.0000 0.0000 691 THR B CB  
5352 O OG1 . THR A 708 ? 0.9149 0.9149 0.9149 0.0000 0.0000 0.0000 691 THR B OG1 
5353 C CG2 . THR A 708 ? 0.9149 0.9149 0.9149 0.0000 0.0000 0.0000 691 THR B CG2 
5354 N N   . VAL A 709 ? 0.9359 0.9359 0.9359 0.0000 0.0000 0.0000 692 VAL B N   
5355 C CA  . VAL A 709 ? 0.9359 0.9359 0.9359 0.0000 0.0000 0.0000 692 VAL B CA  
5356 C C   . VAL A 709 ? 0.9359 0.9359 0.9359 0.0000 0.0000 0.0000 692 VAL B C   
5357 O O   . VAL A 709 ? 0.9359 0.9359 0.9359 0.0000 0.0000 0.0000 692 VAL B O   
5358 C CB  . VAL A 709 ? 0.9359 0.9359 0.9359 0.0000 0.0000 0.0000 692 VAL B CB  
5359 C CG1 . VAL A 709 ? 0.9359 0.9359 0.9359 0.0000 0.0000 0.0000 692 VAL B CG1 
5360 C CG2 . VAL A 709 ? 0.9359 0.9359 0.9359 0.0000 0.0000 0.0000 692 VAL B CG2 
5361 N N   . GLN A 710 ? 0.9816 0.9816 0.9816 0.0000 0.0000 0.0000 693 GLN B N   
5362 C CA  . GLN A 710 ? 0.9816 0.9816 0.9816 0.0000 0.0000 0.0000 693 GLN B CA  
5363 C C   . GLN A 710 ? 0.9816 0.9816 0.9816 0.0000 0.0000 0.0000 693 GLN B C   
5364 O O   . GLN A 710 ? 0.9816 0.9816 0.9816 0.0000 0.0000 0.0000 693 GLN B O   
5365 C CB  . GLN A 710 ? 0.9816 0.9816 0.9816 0.0000 0.0000 0.0000 693 GLN B CB  
5366 C CG  . GLN A 710 ? 0.9816 0.9816 0.9816 0.0000 0.0000 0.0000 693 GLN B CG  
5367 C CD  . GLN A 710 ? 0.9816 0.9816 0.9816 0.0000 0.0000 0.0000 693 GLN B CD  
5368 O OE1 . GLN A 710 ? 0.9816 0.9816 0.9816 0.0000 0.0000 0.0000 693 GLN B OE1 
5369 N NE2 . GLN A 710 ? 0.9816 0.9816 0.9816 0.0000 0.0000 0.0000 693 GLN B NE2 
5370 N N   . THR A 711 ? 0.9108 0.9108 0.9108 0.0000 0.0000 0.0000 694 THR B N   
5371 C CA  . THR A 711 ? 0.9108 0.9108 0.9108 0.0000 0.0000 0.0000 694 THR B CA  
5372 C C   . THR A 711 ? 0.9108 0.9108 0.9108 0.0000 0.0000 0.0000 694 THR B C   
5373 O O   . THR A 711 ? 0.9108 0.9108 0.9108 0.0000 0.0000 0.0000 694 THR B O   
5374 C CB  . THR A 711 ? 0.9108 0.9108 0.9108 0.0000 0.0000 0.0000 694 THR B CB  
5375 O OG1 . THR A 711 ? 0.9108 0.9108 0.9108 0.0000 0.0000 0.0000 694 THR B OG1 
5376 C CG2 . THR A 711 ? 0.9108 0.9108 0.9108 0.0000 0.0000 0.0000 694 THR B CG2 
5377 N N   . ILE A 712 ? 0.8995 0.8995 0.8995 0.0000 0.0000 0.0000 695 ILE B N   
5378 C CA  . ILE A 712 ? 0.8995 0.8995 0.8995 0.0000 0.0000 0.0000 695 ILE B CA  
5379 C C   . ILE A 712 ? 0.8995 0.8995 0.8995 0.0000 0.0000 0.0000 695 ILE B C   
5380 O O   . ILE A 712 ? 0.8995 0.8995 0.8995 0.0000 0.0000 0.0000 695 ILE B O   
5381 C CB  . ILE A 712 ? 0.8995 0.8995 0.8995 0.0000 0.0000 0.0000 695 ILE B CB  
5382 C CG1 . ILE A 712 ? 0.8995 0.8995 0.8995 0.0000 0.0000 0.0000 695 ILE B CG1 
5383 C CG2 . ILE A 712 ? 0.8995 0.8995 0.8995 0.0000 0.0000 0.0000 695 ILE B CG2 
5384 C CD1 . ILE A 712 ? 0.8995 0.8995 0.8995 0.0000 0.0000 0.0000 695 ILE B CD1 
5385 N N   . ASP A 713 ? 0.9954 0.9954 0.9954 0.0000 0.0000 0.0000 696 ASP B N   
5386 C CA  . ASP A 713 ? 0.9954 0.9954 0.9954 0.0000 0.0000 0.0000 696 ASP B CA  
5387 C C   . ASP A 713 ? 0.9954 0.9954 0.9954 0.0000 0.0000 0.0000 696 ASP B C   
5388 O O   . ASP A 713 ? 0.9954 0.9954 0.9954 0.0000 0.0000 0.0000 696 ASP B O   
5389 C CB  . ASP A 713 ? 0.9954 0.9954 0.9954 0.0000 0.0000 0.0000 696 ASP B CB  
5390 C CG  . ASP A 713 ? 0.9954 0.9954 0.9954 0.0000 0.0000 0.0000 696 ASP B CG  
5391 O OD1 . ASP A 713 ? 0.9954 0.9954 0.9954 0.0000 0.0000 0.0000 696 ASP B OD1 
5392 O OD2 . ASP A 713 ? 0.9954 0.9954 0.9954 0.0000 0.0000 0.0000 696 ASP B OD2 
5393 N N   . ASN A 714 ? 0.9779 0.9779 0.9779 0.0000 0.0000 0.0000 697 ASN B N   
5394 C CA  . ASN A 714 ? 0.9779 0.9779 0.9779 0.0000 0.0000 0.0000 697 ASN B CA  
5395 C C   . ASN A 714 ? 0.9779 0.9779 0.9779 0.0000 0.0000 0.0000 697 ASN B C   
5396 O O   . ASN A 714 ? 0.9779 0.9779 0.9779 0.0000 0.0000 0.0000 697 ASN B O   
5397 C CB  . ASN A 714 ? 0.9779 0.9779 0.9779 0.0000 0.0000 0.0000 697 ASN B CB  
5398 C CG  . ASN A 714 ? 0.9779 0.9779 0.9779 0.0000 0.0000 0.0000 697 ASN B CG  
5399 O OD1 . ASN A 714 ? 0.9779 0.9779 0.9779 0.0000 0.0000 0.0000 697 ASN B OD1 
5400 N ND2 . ASN A 714 ? 0.9779 0.9779 0.9779 0.0000 0.0000 0.0000 697 ASN B ND2 
5401 N N   . ALA A 715 ? 0.9232 0.9232 0.9232 0.0000 0.0000 0.0000 698 ALA B N   
5402 C CA  . ALA A 715 ? 0.9232 0.9232 0.9232 0.0000 0.0000 0.0000 698 ALA B CA  
5403 C C   . ALA A 715 ? 0.9232 0.9232 0.9232 0.0000 0.0000 0.0000 698 ALA B C   
5404 O O   . ALA A 715 ? 0.9232 0.9232 0.9232 0.0000 0.0000 0.0000 698 ALA B O   
5405 C CB  . ALA A 715 ? 0.9232 0.9232 0.9232 0.0000 0.0000 0.0000 698 ALA B CB  
5406 N N   . LEU A 716 ? 0.8990 0.8990 0.8990 0.0000 0.0000 0.0000 699 LEU B N   
5407 C CA  . LEU A 716 ? 0.8990 0.8990 0.8990 0.0000 0.0000 0.0000 699 LEU B CA  
5408 C C   . LEU A 716 ? 0.8990 0.8990 0.8990 0.0000 0.0000 0.0000 699 LEU B C   
5409 O O   . LEU A 716 ? 0.8990 0.8990 0.8990 0.0000 0.0000 0.0000 699 LEU B O   
5410 C CB  . LEU A 716 ? 0.8990 0.8990 0.8990 0.0000 0.0000 0.0000 699 LEU B CB  
5411 C CG  . LEU A 716 ? 0.8990 0.8990 0.8990 0.0000 0.0000 0.0000 699 LEU B CG  
5412 C CD1 . LEU A 716 ? 0.8990 0.8990 0.8990 0.0000 0.0000 0.0000 699 LEU B CD1 
5413 C CD2 . LEU A 716 ? 0.8990 0.8990 0.8990 0.0000 0.0000 0.0000 699 LEU B CD2 
5414 N N   . SER A 717 ? 0.9438 0.9438 0.9438 0.0000 0.0000 0.0000 700 SER B N   
5415 C CA  . SER A 717 ? 0.9438 0.9438 0.9438 0.0000 0.0000 0.0000 700 SER B CA  
5416 C C   . SER A 717 ? 0.9438 0.9438 0.9438 0.0000 0.0000 0.0000 700 SER B C   
5417 O O   . SER A 717 ? 0.9438 0.9438 0.9438 0.0000 0.0000 0.0000 700 SER B O   
5418 C CB  . SER A 717 ? 0.9438 0.9438 0.9438 0.0000 0.0000 0.0000 700 SER B CB  
5419 O OG  . SER A 717 ? 0.9438 0.9438 0.9438 0.0000 0.0000 0.0000 700 SER B OG  
5420 N N   . LYS A 718 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 701 LYS B N   
5421 C CA  . LYS A 718 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 701 LYS B CA  
5422 C C   . LYS A 718 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 701 LYS B C   
5423 O O   . LYS A 718 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 701 LYS B O   
5424 C CB  . LYS A 718 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 701 LYS B CB  
5425 C CG  . LYS A 718 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 701 LYS B CG  
5426 C CD  . LYS A 718 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 701 LYS B CD  
5427 C CE  . LYS A 718 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 701 LYS B CE  
5428 N NZ  . LYS A 718 ? 0.9485 0.9485 0.9485 0.0000 0.0000 0.0000 701 LYS B NZ  
5429 N N   . ARG A 719 ? 0.8983 0.8983 0.8983 0.0000 0.0000 0.0000 702 ARG B N   
5430 C CA  . ARG A 719 ? 0.8983 0.8983 0.8983 0.0000 0.0000 0.0000 702 ARG B CA  
5431 C C   . ARG A 719 ? 0.8983 0.8983 0.8983 0.0000 0.0000 0.0000 702 ARG B C   
5432 O O   . ARG A 719 ? 0.8983 0.8983 0.8983 0.0000 0.0000 0.0000 702 ARG B O   
5433 C CB  . ARG A 719 ? 0.8983 0.8983 0.8983 0.0000 0.0000 0.0000 702 ARG B CB  
5434 C CG  . ARG A 719 ? 0.8983 0.8983 0.8983 0.0000 0.0000 0.0000 702 ARG B CG  
5435 C CD  . ARG A 719 ? 0.8983 0.8983 0.8983 0.0000 0.0000 0.0000 702 ARG B CD  
5436 N NE  . ARG A 719 ? 0.8983 0.8983 0.8983 0.0000 0.0000 0.0000 702 ARG B NE  
5437 C CZ  . ARG A 719 ? 0.8983 0.8983 0.8983 0.0000 0.0000 0.0000 702 ARG B CZ  
5438 N NH1 . ARG A 719 ? 0.8983 0.8983 0.8983 0.0000 0.0000 0.0000 702 ARG B NH1 
5439 N NH2 . ARG A 719 ? 0.8983 0.8983 0.8983 0.0000 0.0000 0.0000 702 ARG B NH2 
5440 N N   . ASN A 720 ? 0.9143 0.9143 0.9143 0.0000 0.0000 0.0000 703 ASN B N   
5441 C CA  . ASN A 720 ? 0.9143 0.9143 0.9143 0.0000 0.0000 0.0000 703 ASN B CA  
5442 C C   . ASN A 720 ? 0.9143 0.9143 0.9143 0.0000 0.0000 0.0000 703 ASN B C   
5443 O O   . ASN A 720 ? 0.9143 0.9143 0.9143 0.0000 0.0000 0.0000 703 ASN B O   
5444 C CB  . ASN A 720 ? 0.9143 0.9143 0.9143 0.0000 0.0000 0.0000 703 ASN B CB  
5445 C CG  . ASN A 720 ? 0.9143 0.9143 0.9143 0.0000 0.0000 0.0000 703 ASN B CG  
5446 O OD1 . ASN A 720 ? 0.9143 0.9143 0.9143 0.0000 0.0000 0.0000 703 ASN B OD1 
5447 N ND2 . ASN A 720 ? 0.9143 0.9143 0.9143 0.0000 0.0000 0.0000 703 ASN B ND2 
5448 N N   . GLU A 721 ? 0.9781 0.9781 0.9781 0.0000 0.0000 0.0000 704 GLU B N   
5449 C CA  . GLU A 721 ? 0.9781 0.9781 0.9781 0.0000 0.0000 0.0000 704 GLU B CA  
5450 C C   . GLU A 721 ? 0.9781 0.9781 0.9781 0.0000 0.0000 0.0000 704 GLU B C   
5451 O O   . GLU A 721 ? 0.9781 0.9781 0.9781 0.0000 0.0000 0.0000 704 GLU B O   
5452 C CB  . GLU A 721 ? 0.9781 0.9781 0.9781 0.0000 0.0000 0.0000 704 GLU B CB  
5453 C CG  . GLU A 721 ? 0.9781 0.9781 0.9781 0.0000 0.0000 0.0000 704 GLU B CG  
5454 C CD  . GLU A 721 ? 0.9781 0.9781 0.9781 0.0000 0.0000 0.0000 704 GLU B CD  
5455 O OE1 . GLU A 721 ? 0.9781 0.9781 0.9781 0.0000 0.0000 0.0000 704 GLU B OE1 
5456 O OE2 . GLU A 721 ? 0.9781 0.9781 0.9781 0.0000 0.0000 0.0000 704 GLU B OE2 
5457 N N   . LYS A 722 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 705 LYS B N   
5458 C CA  . LYS A 722 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 705 LYS B CA  
5459 C C   . LYS A 722 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 705 LYS B C   
5460 O O   . LYS A 722 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 705 LYS B O   
5461 C CB  . LYS A 722 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 705 LYS B CB  
5462 C CG  . LYS A 722 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 705 LYS B CG  
5463 C CD  . LYS A 722 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 705 LYS B CD  
5464 C CE  . LYS A 722 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 705 LYS B CE  
5465 N NZ  . LYS A 722 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 705 LYS B NZ  
5466 N N   . TRP A 723 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 706 TRP B N   
5467 C CA  . TRP A 723 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 706 TRP B CA  
5468 C C   . TRP A 723 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 706 TRP B C   
5469 O O   . TRP A 723 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 706 TRP B O   
5470 C CB  . TRP A 723 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 706 TRP B CB  
5471 C CG  . TRP A 723 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 706 TRP B CG  
5472 C CD1 . TRP A 723 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 706 TRP B CD1 
5473 C CD2 . TRP A 723 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 706 TRP B CD2 
5474 N NE1 . TRP A 723 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 706 TRP B NE1 
5475 C CE2 . TRP A 723 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 706 TRP B CE2 
5476 C CE3 . TRP A 723 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 706 TRP B CE3 
5477 C CZ2 . TRP A 723 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 706 TRP B CZ2 
5478 C CZ3 . TRP A 723 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 706 TRP B CZ3 
5479 C CH2 . TRP A 723 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 706 TRP B CH2 
5480 N N   . ASP A 724 ? 0.9014 0.9014 0.9014 0.0000 0.0000 0.0000 707 ASP B N   
5481 C CA  . ASP A 724 ? 0.9014 0.9014 0.9014 0.0000 0.0000 0.0000 707 ASP B CA  
5482 C C   . ASP A 724 ? 0.9014 0.9014 0.9014 0.0000 0.0000 0.0000 707 ASP B C   
5483 O O   . ASP A 724 ? 0.9014 0.9014 0.9014 0.0000 0.0000 0.0000 707 ASP B O   
5484 C CB  . ASP A 724 ? 0.9014 0.9014 0.9014 0.0000 0.0000 0.0000 707 ASP B CB  
5485 C CG  . ASP A 724 ? 0.9014 0.9014 0.9014 0.0000 0.0000 0.0000 707 ASP B CG  
5486 O OD1 . ASP A 724 ? 0.9014 0.9014 0.9014 0.0000 0.0000 0.0000 707 ASP B OD1 
5487 O OD2 . ASP A 724 ? 0.9014 0.9014 0.9014 0.0000 0.0000 0.0000 707 ASP B OD2 
5488 N N   . GLU A 725 ? 0.8885 0.8885 0.8885 0.0000 0.0000 0.0000 708 GLU B N   
5489 C CA  . GLU A 725 ? 0.8885 0.8885 0.8885 0.0000 0.0000 0.0000 708 GLU B CA  
5490 C C   . GLU A 725 ? 0.8885 0.8885 0.8885 0.0000 0.0000 0.0000 708 GLU B C   
5491 O O   . GLU A 725 ? 0.8885 0.8885 0.8885 0.0000 0.0000 0.0000 708 GLU B O   
5492 C CB  . GLU A 725 ? 0.8885 0.8885 0.8885 0.0000 0.0000 0.0000 708 GLU B CB  
5493 C CG  . GLU A 725 ? 0.8885 0.8885 0.8885 0.0000 0.0000 0.0000 708 GLU B CG  
5494 C CD  . GLU A 725 ? 0.8885 0.8885 0.8885 0.0000 0.0000 0.0000 708 GLU B CD  
5495 O OE1 . GLU A 725 ? 0.8885 0.8885 0.8885 0.0000 0.0000 0.0000 708 GLU B OE1 
5496 O OE2 . GLU A 725 ? 0.8885 0.8885 0.8885 0.0000 0.0000 0.0000 708 GLU B OE2 
5497 N N   . VAL A 726 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 709 VAL B N   
5498 C CA  . VAL A 726 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 709 VAL B CA  
5499 C C   . VAL A 726 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 709 VAL B C   
5500 O O   . VAL A 726 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 709 VAL B O   
5501 C CB  . VAL A 726 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 709 VAL B CB  
5502 C CG1 . VAL A 726 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 709 VAL B CG1 
5503 C CG2 . VAL A 726 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 709 VAL B CG2 
5504 N N   . TYR A 727 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 710 TYR B N   
5505 C CA  . TYR A 727 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 710 TYR B CA  
5506 C C   . TYR A 727 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 710 TYR B C   
5507 O O   . TYR A 727 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 710 TYR B O   
5508 C CB  . TYR A 727 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 710 TYR B CB  
5509 C CG  . TYR A 727 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 710 TYR B CG  
5510 C CD1 . TYR A 727 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 710 TYR B CD1 
5511 C CD2 . TYR A 727 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 710 TYR B CD2 
5512 C CE1 . TYR A 727 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 710 TYR B CE1 
5513 C CE2 . TYR A 727 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 710 TYR B CE2 
5514 C CZ  . TYR A 727 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 710 TYR B CZ  
5515 O OH  . TYR A 727 ? 0.8827 0.8827 0.8827 0.0000 0.0000 0.0000 710 TYR B OH  
5516 N N   . LYS A 728 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 711 LYS B N   
5517 C CA  . LYS A 728 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 711 LYS B CA  
5518 C C   . LYS A 728 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 711 LYS B C   
5519 O O   . LYS A 728 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 711 LYS B O   
5520 C CB  . LYS A 728 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 711 LYS B CB  
5521 C CG  . LYS A 728 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 711 LYS B CG  
5522 C CD  . LYS A 728 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 711 LYS B CD  
5523 C CE  . LYS A 728 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 711 LYS B CE  
5524 N NZ  . LYS A 728 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 711 LYS B NZ  
5525 N N   . TYR A 729 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 712 TYR B N   
5526 C CA  . TYR A 729 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 712 TYR B CA  
5527 C C   . TYR A 729 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 712 TYR B C   
5528 O O   . TYR A 729 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 712 TYR B O   
5529 C CB  . TYR A 729 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 712 TYR B CB  
5530 C CG  . TYR A 729 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 712 TYR B CG  
5531 C CD1 . TYR A 729 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 712 TYR B CD1 
5532 C CD2 . TYR A 729 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 712 TYR B CD2 
5533 C CE1 . TYR A 729 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 712 TYR B CE1 
5534 C CE2 . TYR A 729 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 712 TYR B CE2 
5535 C CZ  . TYR A 729 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 712 TYR B CZ  
5536 O OH  . TYR A 729 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 712 TYR B OH  
5537 N N   . ILE A 730 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 713 ILE B N   
5538 C CA  . ILE A 730 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 713 ILE B CA  
5539 C C   . ILE A 730 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 713 ILE B C   
5540 O O   . ILE A 730 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 713 ILE B O   
5541 C CB  . ILE A 730 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 713 ILE B CB  
5542 C CG1 . ILE A 730 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 713 ILE B CG1 
5543 C CG2 . ILE A 730 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 713 ILE B CG2 
5544 C CD1 . ILE A 730 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 713 ILE B CD1 
5545 N N   . VAL A 731 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 714 VAL B N   
5546 C CA  . VAL A 731 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 714 VAL B CA  
5547 C C   . VAL A 731 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 714 VAL B C   
5548 O O   . VAL A 731 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 714 VAL B O   
5549 C CB  . VAL A 731 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 714 VAL B CB  
5550 C CG1 . VAL A 731 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 714 VAL B CG1 
5551 C CG2 . VAL A 731 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 714 VAL B CG2 
5552 N N   . THR A 732 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 715 THR B N   
5553 C CA  . THR A 732 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 715 THR B CA  
5554 C C   . THR A 732 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 715 THR B C   
5555 O O   . THR A 732 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 715 THR B O   
5556 C CB  . THR A 732 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 715 THR B CB  
5557 O OG1 . THR A 732 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 715 THR B OG1 
5558 C CG2 . THR A 732 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 715 THR B CG2 
5559 N N   . ASN A 733 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 716 ASN B N   
5560 C CA  . ASN A 733 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 716 ASN B CA  
5561 C C   . ASN A 733 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 716 ASN B C   
5562 O O   . ASN A 733 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 716 ASN B O   
5563 C CB  . ASN A 733 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 716 ASN B CB  
5564 C CG  . ASN A 733 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 716 ASN B CG  
5565 O OD1 . ASN A 733 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 716 ASN B OD1 
5566 N ND2 . ASN A 733 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 716 ASN B ND2 
5567 N N   . TRP A 734 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 717 TRP B N   
5568 C CA  . TRP A 734 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 717 TRP B CA  
5569 C C   . TRP A 734 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 717 TRP B C   
5570 O O   . TRP A 734 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 717 TRP B O   
5571 C CB  . TRP A 734 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 717 TRP B CB  
5572 C CG  . TRP A 734 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 717 TRP B CG  
5573 C CD1 . TRP A 734 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 717 TRP B CD1 
5574 C CD2 . TRP A 734 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 717 TRP B CD2 
5575 N NE1 . TRP A 734 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 717 TRP B NE1 
5576 C CE2 . TRP A 734 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 717 TRP B CE2 
5577 C CE3 . TRP A 734 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 717 TRP B CE3 
5578 C CZ2 . TRP A 734 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 717 TRP B CZ2 
5579 C CZ3 . TRP A 734 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 717 TRP B CZ3 
5580 C CH2 . TRP A 734 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 717 TRP B CH2 
5581 N N   . LEU A 735 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 718 LEU B N   
5582 C CA  . LEU A 735 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 718 LEU B CA  
5583 C C   . LEU A 735 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 718 LEU B C   
5584 O O   . LEU A 735 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 718 LEU B O   
5585 C CB  . LEU A 735 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 718 LEU B CB  
5586 C CG  . LEU A 735 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 718 LEU B CG  
5587 C CD1 . LEU A 735 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 718 LEU B CD1 
5588 C CD2 . LEU A 735 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 718 LEU B CD2 
5589 N N   . ALA A 736 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 719 ALA B N   
5590 C CA  . ALA A 736 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 719 ALA B CA  
5591 C C   . ALA A 736 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 719 ALA B C   
5592 O O   . ALA A 736 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 719 ALA B O   
5593 C CB  . ALA A 736 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 719 ALA B CB  
5594 N N   . LYS A 737 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 720 LYS B N   
5595 C CA  . LYS A 737 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 720 LYS B CA  
5596 C C   . LYS A 737 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 720 LYS B C   
5597 O O   . LYS A 737 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 720 LYS B O   
5598 C CB  . LYS A 737 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 720 LYS B CB  
5599 C CG  . LYS A 737 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 720 LYS B CG  
5600 C CD  . LYS A 737 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 720 LYS B CD  
5601 C CE  . LYS A 737 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 720 LYS B CE  
5602 N NZ  . LYS A 737 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 720 LYS B NZ  
5603 N N   . VAL A 738 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 721 VAL B N   
5604 C CA  . VAL A 738 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 721 VAL B CA  
5605 C C   . VAL A 738 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 721 VAL B C   
5606 O O   . VAL A 738 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 721 VAL B O   
5607 C CB  . VAL A 738 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 721 VAL B CB  
5608 C CG1 . VAL A 738 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 721 VAL B CG1 
5609 C CG2 . VAL A 738 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 721 VAL B CG2 
5610 N N   . ASN A 739 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 722 ASN B N   
5611 C CA  . ASN A 739 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 722 ASN B CA  
5612 C C   . ASN A 739 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 722 ASN B C   
5613 O O   . ASN A 739 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 722 ASN B O   
5614 C CB  . ASN A 739 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 722 ASN B CB  
5615 C CG  . ASN A 739 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 722 ASN B CG  
5616 O OD1 . ASN A 739 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 722 ASN B OD1 
5617 N ND2 . ASN A 739 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 722 ASN B ND2 
5618 N N   . THR A 740 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 723 THR B N   
5619 C CA  . THR A 740 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 723 THR B CA  
5620 C C   . THR A 740 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 723 THR B C   
5621 O O   . THR A 740 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 723 THR B O   
5622 C CB  . THR A 740 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 723 THR B CB  
5623 O OG1 . THR A 740 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 723 THR B OG1 
5624 C CG2 . THR A 740 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 723 THR B CG2 
5625 N N   . GLN A 741 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 724 GLN B N   
5626 C CA  . GLN A 741 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 724 GLN B CA  
5627 C C   . GLN A 741 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 724 GLN B C   
5628 O O   . GLN A 741 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 724 GLN B O   
5629 C CB  . GLN A 741 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 724 GLN B CB  
5630 C CG  . GLN A 741 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 724 GLN B CG  
5631 C CD  . GLN A 741 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 724 GLN B CD  
5632 O OE1 . GLN A 741 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 724 GLN B OE1 
5633 N NE2 . GLN A 741 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 724 GLN B NE2 
5634 N N   . ILE A 742 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 725 ILE B N   
5635 C CA  . ILE A 742 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 725 ILE B CA  
5636 C C   . ILE A 742 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 725 ILE B C   
5637 O O   . ILE A 742 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 725 ILE B O   
5638 C CB  . ILE A 742 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 725 ILE B CB  
5639 C CG1 . ILE A 742 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 725 ILE B CG1 
5640 C CG2 . ILE A 742 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 725 ILE B CG2 
5641 C CD1 . ILE A 742 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 725 ILE B CD1 
5642 N N   . ASP A 743 ? 0.8872 0.8872 0.8872 0.0000 0.0000 0.0000 726 ASP B N   
5643 C CA  . ASP A 743 ? 0.8872 0.8872 0.8872 0.0000 0.0000 0.0000 726 ASP B CA  
5644 C C   . ASP A 743 ? 0.8872 0.8872 0.8872 0.0000 0.0000 0.0000 726 ASP B C   
5645 O O   . ASP A 743 ? 0.8872 0.8872 0.8872 0.0000 0.0000 0.0000 726 ASP B O   
5646 C CB  . ASP A 743 ? 0.8872 0.8872 0.8872 0.0000 0.0000 0.0000 726 ASP B CB  
5647 C CG  . ASP A 743 ? 0.8872 0.8872 0.8872 0.0000 0.0000 0.0000 726 ASP B CG  
5648 O OD1 . ASP A 743 ? 0.8872 0.8872 0.8872 0.0000 0.0000 0.0000 726 ASP B OD1 
5649 O OD2 . ASP A 743 ? 0.8872 0.8872 0.8872 0.0000 0.0000 0.0000 726 ASP B OD2 
5650 N N   . LEU A 744 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 727 LEU B N   
5651 C CA  . LEU A 744 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 727 LEU B CA  
5652 C C   . LEU A 744 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 727 LEU B C   
5653 O O   . LEU A 744 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 727 LEU B O   
5654 C CB  . LEU A 744 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 727 LEU B CB  
5655 C CG  . LEU A 744 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 727 LEU B CG  
5656 C CD1 . LEU A 744 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 727 LEU B CD1 
5657 C CD2 . LEU A 744 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 727 LEU B CD2 
5658 N N   . ILE A 745 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 728 ILE B N   
5659 C CA  . ILE A 745 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 728 ILE B CA  
5660 C C   . ILE A 745 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 728 ILE B C   
5661 O O   . ILE A 745 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 728 ILE B O   
5662 C CB  . ILE A 745 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 728 ILE B CB  
5663 C CG1 . ILE A 745 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 728 ILE B CG1 
5664 C CG2 . ILE A 745 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 728 ILE B CG2 
5665 C CD1 . ILE A 745 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 728 ILE B CD1 
5666 N N   . ARG A 746 ? 0.9104 0.9104 0.9104 0.0000 0.0000 0.0000 729 ARG B N   
5667 C CA  . ARG A 746 ? 0.9104 0.9104 0.9104 0.0000 0.0000 0.0000 729 ARG B CA  
5668 C C   . ARG A 746 ? 0.9104 0.9104 0.9104 0.0000 0.0000 0.0000 729 ARG B C   
5669 O O   . ARG A 746 ? 0.9104 0.9104 0.9104 0.0000 0.0000 0.0000 729 ARG B O   
5670 C CB  . ARG A 746 ? 0.9104 0.9104 0.9104 0.0000 0.0000 0.0000 729 ARG B CB  
5671 C CG  . ARG A 746 ? 0.9104 0.9104 0.9104 0.0000 0.0000 0.0000 729 ARG B CG  
5672 C CD  . ARG A 746 ? 0.9104 0.9104 0.9104 0.0000 0.0000 0.0000 729 ARG B CD  
5673 N NE  . ARG A 746 ? 0.9104 0.9104 0.9104 0.0000 0.0000 0.0000 729 ARG B NE  
5674 C CZ  . ARG A 746 ? 0.9104 0.9104 0.9104 0.0000 0.0000 0.0000 729 ARG B CZ  
5675 N NH1 . ARG A 746 ? 0.9104 0.9104 0.9104 0.0000 0.0000 0.0000 729 ARG B NH1 
5676 N NH2 . ARG A 746 ? 0.9104 0.9104 0.9104 0.0000 0.0000 0.0000 729 ARG B NH2 
5677 N N   . LYS A 747 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 730 LYS B N   
5678 C CA  . LYS A 747 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 730 LYS B CA  
5679 C C   . LYS A 747 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 730 LYS B C   
5680 O O   . LYS A 747 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 730 LYS B O   
5681 C CB  . LYS A 747 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 730 LYS B CB  
5682 C CG  . LYS A 747 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 730 LYS B CG  
5683 C CD  . LYS A 747 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 730 LYS B CD  
5684 C CE  . LYS A 747 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 730 LYS B CE  
5685 N NZ  . LYS A 747 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 730 LYS B NZ  
5686 N N   . LYS A 748 ? 0.8912 0.8912 0.8912 0.0000 0.0000 0.0000 731 LYS B N   
5687 C CA  . LYS A 748 ? 0.8912 0.8912 0.8912 0.0000 0.0000 0.0000 731 LYS B CA  
5688 C C   . LYS A 748 ? 0.8912 0.8912 0.8912 0.0000 0.0000 0.0000 731 LYS B C   
5689 O O   . LYS A 748 ? 0.8912 0.8912 0.8912 0.0000 0.0000 0.0000 731 LYS B O   
5690 C CB  . LYS A 748 ? 0.8912 0.8912 0.8912 0.0000 0.0000 0.0000 731 LYS B CB  
5691 C CG  . LYS A 748 ? 0.8912 0.8912 0.8912 0.0000 0.0000 0.0000 731 LYS B CG  
5692 C CD  . LYS A 748 ? 0.8912 0.8912 0.8912 0.0000 0.0000 0.0000 731 LYS B CD  
5693 C CE  . LYS A 748 ? 0.8912 0.8912 0.8912 0.0000 0.0000 0.0000 731 LYS B CE  
5694 N NZ  . LYS A 748 ? 0.8912 0.8912 0.8912 0.0000 0.0000 0.0000 731 LYS B NZ  
5695 N N   . MET A 749 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 732 MET B N   
5696 C CA  . MET A 749 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 732 MET B CA  
5697 C C   . MET A 749 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 732 MET B C   
5698 O O   . MET A 749 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 732 MET B O   
5699 C CB  . MET A 749 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 732 MET B CB  
5700 C CG  . MET A 749 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 732 MET B CG  
5701 S SD  . MET A 749 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 732 MET B SD  
5702 C CE  . MET A 749 ? 0.9474 0.9474 0.9474 0.0000 0.0000 0.0000 732 MET B CE  
5703 N N   . LYS A 750 ? 0.9354 0.9354 0.9354 0.0000 0.0000 0.0000 733 LYS B N   
5704 C CA  . LYS A 750 ? 0.9354 0.9354 0.9354 0.0000 0.0000 0.0000 733 LYS B CA  
5705 C C   . LYS A 750 ? 0.9354 0.9354 0.9354 0.0000 0.0000 0.0000 733 LYS B C   
5706 O O   . LYS A 750 ? 0.9354 0.9354 0.9354 0.0000 0.0000 0.0000 733 LYS B O   
5707 C CB  . LYS A 750 ? 0.9354 0.9354 0.9354 0.0000 0.0000 0.0000 733 LYS B CB  
5708 C CG  . LYS A 750 ? 0.9354 0.9354 0.9354 0.0000 0.0000 0.0000 733 LYS B CG  
5709 C CD  . LYS A 750 ? 0.9354 0.9354 0.9354 0.0000 0.0000 0.0000 733 LYS B CD  
5710 C CE  . LYS A 750 ? 0.9354 0.9354 0.9354 0.0000 0.0000 0.0000 733 LYS B CE  
5711 N NZ  . LYS A 750 ? 0.9354 0.9354 0.9354 0.0000 0.0000 0.0000 733 LYS B NZ  
5712 N N   . GLU A 751 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 734 GLU B N   
5713 C CA  . GLU A 751 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 734 GLU B CA  
5714 C C   . GLU A 751 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 734 GLU B C   
5715 O O   . GLU A 751 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 734 GLU B O   
5716 C CB  . GLU A 751 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 734 GLU B CB  
5717 C CG  . GLU A 751 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 734 GLU B CG  
5718 C CD  . GLU A 751 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 734 GLU B CD  
5719 O OE1 . GLU A 751 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 734 GLU B OE1 
5720 O OE2 . GLU A 751 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 734 GLU B OE2 
5721 N N   . ALA A 752 ? 0.9115 0.9115 0.9115 0.0000 0.0000 0.0000 735 ALA B N   
5722 C CA  . ALA A 752 ? 0.9115 0.9115 0.9115 0.0000 0.0000 0.0000 735 ALA B CA  
5723 C C   . ALA A 752 ? 0.9115 0.9115 0.9115 0.0000 0.0000 0.0000 735 ALA B C   
5724 O O   . ALA A 752 ? 0.9115 0.9115 0.9115 0.0000 0.0000 0.0000 735 ALA B O   
5725 C CB  . ALA A 752 ? 0.9115 0.9115 0.9115 0.0000 0.0000 0.0000 735 ALA B CB  
5726 N N   . LEU A 753 ? 0.9227 0.9227 0.9227 0.0000 0.0000 0.0000 736 LEU B N   
5727 C CA  . LEU A 753 ? 0.9227 0.9227 0.9227 0.0000 0.0000 0.0000 736 LEU B CA  
5728 C C   . LEU A 753 ? 0.9227 0.9227 0.9227 0.0000 0.0000 0.0000 736 LEU B C   
5729 O O   . LEU A 753 ? 0.9227 0.9227 0.9227 0.0000 0.0000 0.0000 736 LEU B O   
5730 C CB  . LEU A 753 ? 0.9227 0.9227 0.9227 0.0000 0.0000 0.0000 736 LEU B CB  
5731 C CG  . LEU A 753 ? 0.9227 0.9227 0.9227 0.0000 0.0000 0.0000 736 LEU B CG  
5732 C CD1 . LEU A 753 ? 0.9227 0.9227 0.9227 0.0000 0.0000 0.0000 736 LEU B CD1 
5733 C CD2 . LEU A 753 ? 0.9227 0.9227 0.9227 0.0000 0.0000 0.0000 736 LEU B CD2 
5734 N N   . GLU A 754 ? 0.9790 0.9790 0.9790 0.0000 0.0000 0.0000 737 GLU B N   
5735 C CA  . GLU A 754 ? 0.9790 0.9790 0.9790 0.0000 0.0000 0.0000 737 GLU B CA  
5736 C C   . GLU A 754 ? 0.9790 0.9790 0.9790 0.0000 0.0000 0.0000 737 GLU B C   
5737 O O   . GLU A 754 ? 0.9790 0.9790 0.9790 0.0000 0.0000 0.0000 737 GLU B O   
5738 C CB  . GLU A 754 ? 0.9790 0.9790 0.9790 0.0000 0.0000 0.0000 737 GLU B CB  
5739 C CG  . GLU A 754 ? 0.9790 0.9790 0.9790 0.0000 0.0000 0.0000 737 GLU B CG  
5740 C CD  . GLU A 754 ? 0.9790 0.9790 0.9790 0.0000 0.0000 0.0000 737 GLU B CD  
5741 O OE1 . GLU A 754 ? 0.9790 0.9790 0.9790 0.0000 0.0000 0.0000 737 GLU B OE1 
5742 O OE2 . GLU A 754 ? 0.9790 0.9790 0.9790 0.0000 0.0000 0.0000 737 GLU B OE2 
5743 N N   . ASN A 755 ? 0.9424 0.9424 0.9424 0.0000 0.0000 0.0000 738 ASN B N   
5744 C CA  . ASN A 755 ? 0.9424 0.9424 0.9424 0.0000 0.0000 0.0000 738 ASN B CA  
5745 C C   . ASN A 755 ? 0.9424 0.9424 0.9424 0.0000 0.0000 0.0000 738 ASN B C   
5746 O O   . ASN A 755 ? 0.9424 0.9424 0.9424 0.0000 0.0000 0.0000 738 ASN B O   
5747 C CB  . ASN A 755 ? 0.9424 0.9424 0.9424 0.0000 0.0000 0.0000 738 ASN B CB  
5748 C CG  . ASN A 755 ? 0.9424 0.9424 0.9424 0.0000 0.0000 0.0000 738 ASN B CG  
5749 O OD1 . ASN A 755 ? 0.9424 0.9424 0.9424 0.0000 0.0000 0.0000 738 ASN B OD1 
5750 N ND2 . ASN A 755 ? 0.9424 0.9424 0.9424 0.0000 0.0000 0.0000 738 ASN B ND2 
5751 N N   . GLN A 756 ? 0.9043 0.9043 0.9043 0.0000 0.0000 0.0000 739 GLN B N   
5752 C CA  . GLN A 756 ? 0.9043 0.9043 0.9043 0.0000 0.0000 0.0000 739 GLN B CA  
5753 C C   . GLN A 756 ? 0.9043 0.9043 0.9043 0.0000 0.0000 0.0000 739 GLN B C   
5754 O O   . GLN A 756 ? 0.9043 0.9043 0.9043 0.0000 0.0000 0.0000 739 GLN B O   
5755 C CB  . GLN A 756 ? 0.9043 0.9043 0.9043 0.0000 0.0000 0.0000 739 GLN B CB  
5756 C CG  . GLN A 756 ? 0.9043 0.9043 0.9043 0.0000 0.0000 0.0000 739 GLN B CG  
5757 C CD  . GLN A 756 ? 0.9043 0.9043 0.9043 0.0000 0.0000 0.0000 739 GLN B CD  
5758 O OE1 . GLN A 756 ? 0.9043 0.9043 0.9043 0.0000 0.0000 0.0000 739 GLN B OE1 
5759 N NE2 . GLN A 756 ? 0.9043 0.9043 0.9043 0.0000 0.0000 0.0000 739 GLN B NE2 
5760 N N   . ALA A 757 ? 0.9464 0.9464 0.9464 0.0000 0.0000 0.0000 740 ALA B N   
5761 C CA  . ALA A 757 ? 0.9464 0.9464 0.9464 0.0000 0.0000 0.0000 740 ALA B CA  
5762 C C   . ALA A 757 ? 0.9464 0.9464 0.9464 0.0000 0.0000 0.0000 740 ALA B C   
5763 O O   . ALA A 757 ? 0.9464 0.9464 0.9464 0.0000 0.0000 0.0000 740 ALA B O   
5764 C CB  . ALA A 757 ? 0.9464 0.9464 0.9464 0.0000 0.0000 0.0000 740 ALA B CB  
5765 N N   . GLU A 758 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 741 GLU B N   
5766 C CA  . GLU A 758 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 741 GLU B CA  
5767 C C   . GLU A 758 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 741 GLU B C   
5768 O O   . GLU A 758 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 741 GLU B O   
5769 C CB  . GLU A 758 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 741 GLU B CB  
5770 C CG  . GLU A 758 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 741 GLU B CG  
5771 C CD  . GLU A 758 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 741 GLU B CD  
5772 O OE1 . GLU A 758 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 741 GLU B OE1 
5773 O OE2 . GLU A 758 ? 0.9639 0.9639 0.9639 0.0000 0.0000 0.0000 741 GLU B OE2 
5774 N N   . ALA A 759 ? 0.9259 0.9259 0.9259 0.0000 0.0000 0.0000 742 ALA B N   
5775 C CA  . ALA A 759 ? 0.9259 0.9259 0.9259 0.0000 0.0000 0.0000 742 ALA B CA  
5776 C C   . ALA A 759 ? 0.9259 0.9259 0.9259 0.0000 0.0000 0.0000 742 ALA B C   
5777 O O   . ALA A 759 ? 0.9259 0.9259 0.9259 0.0000 0.0000 0.0000 742 ALA B O   
5778 C CB  . ALA A 759 ? 0.9259 0.9259 0.9259 0.0000 0.0000 0.0000 742 ALA B CB  
5779 N N   . THR A 760 ? 0.8966 0.8966 0.8966 0.0000 0.0000 0.0000 743 THR B N   
5780 C CA  . THR A 760 ? 0.8966 0.8966 0.8966 0.0000 0.0000 0.0000 743 THR B CA  
5781 C C   . THR A 760 ? 0.8966 0.8966 0.8966 0.0000 0.0000 0.0000 743 THR B C   
5782 O O   . THR A 760 ? 0.8966 0.8966 0.8966 0.0000 0.0000 0.0000 743 THR B O   
5783 C CB  . THR A 760 ? 0.8966 0.8966 0.8966 0.0000 0.0000 0.0000 743 THR B CB  
5784 O OG1 . THR A 760 ? 0.8966 0.8966 0.8966 0.0000 0.0000 0.0000 743 THR B OG1 
5785 C CG2 . THR A 760 ? 0.8966 0.8966 0.8966 0.0000 0.0000 0.0000 743 THR B CG2 
5786 N N   . LYS A 761 ? 0.9481 0.9481 0.9481 0.0000 0.0000 0.0000 744 LYS B N   
5787 C CA  . LYS A 761 ? 0.9481 0.9481 0.9481 0.0000 0.0000 0.0000 744 LYS B CA  
5788 C C   . LYS A 761 ? 0.9481 0.9481 0.9481 0.0000 0.0000 0.0000 744 LYS B C   
5789 O O   . LYS A 761 ? 0.9481 0.9481 0.9481 0.0000 0.0000 0.0000 744 LYS B O   
5790 C CB  . LYS A 761 ? 0.9481 0.9481 0.9481 0.0000 0.0000 0.0000 744 LYS B CB  
5791 C CG  . LYS A 761 ? 0.9481 0.9481 0.9481 0.0000 0.0000 0.0000 744 LYS B CG  
5792 C CD  . LYS A 761 ? 0.9481 0.9481 0.9481 0.0000 0.0000 0.0000 744 LYS B CD  
5793 C CE  . LYS A 761 ? 0.9481 0.9481 0.9481 0.0000 0.0000 0.0000 744 LYS B CE  
5794 N NZ  . LYS A 761 ? 0.9481 0.9481 0.9481 0.0000 0.0000 0.0000 744 LYS B NZ  
5795 N N   . ALA A 762 ? 0.9280 0.9280 0.9280 0.0000 0.0000 0.0000 745 ALA B N   
5796 C CA  . ALA A 762 ? 0.9280 0.9280 0.9280 0.0000 0.0000 0.0000 745 ALA B CA  
5797 C C   . ALA A 762 ? 0.9280 0.9280 0.9280 0.0000 0.0000 0.0000 745 ALA B C   
5798 O O   . ALA A 762 ? 0.9280 0.9280 0.9280 0.0000 0.0000 0.0000 745 ALA B O   
5799 C CB  . ALA A 762 ? 0.9280 0.9280 0.9280 0.0000 0.0000 0.0000 745 ALA B CB  
5800 N N   . ILE A 763 ? 0.8844 0.8844 0.8844 0.0000 0.0000 0.0000 746 ILE B N   
5801 C CA  . ILE A 763 ? 0.8844 0.8844 0.8844 0.0000 0.0000 0.0000 746 ILE B CA  
5802 C C   . ILE A 763 ? 0.8844 0.8844 0.8844 0.0000 0.0000 0.0000 746 ILE B C   
5803 O O   . ILE A 763 ? 0.8844 0.8844 0.8844 0.0000 0.0000 0.0000 746 ILE B O   
5804 C CB  . ILE A 763 ? 0.8844 0.8844 0.8844 0.0000 0.0000 0.0000 746 ILE B CB  
5805 C CG1 . ILE A 763 ? 0.8844 0.8844 0.8844 0.0000 0.0000 0.0000 746 ILE B CG1 
5806 C CG2 . ILE A 763 ? 0.8844 0.8844 0.8844 0.0000 0.0000 0.0000 746 ILE B CG2 
5807 C CD1 . ILE A 763 ? 0.8844 0.8844 0.8844 0.0000 0.0000 0.0000 746 ILE B CD1 
5808 N N   . ILE A 764 ? 0.9312 0.9312 0.9312 0.0000 0.0000 0.0000 747 ILE B N   
5809 C CA  . ILE A 764 ? 0.9312 0.9312 0.9312 0.0000 0.0000 0.0000 747 ILE B CA  
5810 C C   . ILE A 764 ? 0.9312 0.9312 0.9312 0.0000 0.0000 0.0000 747 ILE B C   
5811 O O   . ILE A 764 ? 0.9312 0.9312 0.9312 0.0000 0.0000 0.0000 747 ILE B O   
5812 C CB  . ILE A 764 ? 0.9312 0.9312 0.9312 0.0000 0.0000 0.0000 747 ILE B CB  
5813 C CG1 . ILE A 764 ? 0.9312 0.9312 0.9312 0.0000 0.0000 0.0000 747 ILE B CG1 
5814 C CG2 . ILE A 764 ? 0.9312 0.9312 0.9312 0.0000 0.0000 0.0000 747 ILE B CG2 
5815 C CD1 . ILE A 764 ? 0.9312 0.9312 0.9312 0.0000 0.0000 0.0000 747 ILE B CD1 
5816 N N   . ASN A 765 ? 0.9304 0.9304 0.9304 0.0000 0.0000 0.0000 748 ASN B N   
5817 C CA  . ASN A 765 ? 0.9304 0.9304 0.9304 0.0000 0.0000 0.0000 748 ASN B CA  
5818 C C   . ASN A 765 ? 0.9304 0.9304 0.9304 0.0000 0.0000 0.0000 748 ASN B C   
5819 O O   . ASN A 765 ? 0.9304 0.9304 0.9304 0.0000 0.0000 0.0000 748 ASN B O   
5820 C CB  . ASN A 765 ? 0.9304 0.9304 0.9304 0.0000 0.0000 0.0000 748 ASN B CB  
5821 C CG  . ASN A 765 ? 0.9304 0.9304 0.9304 0.0000 0.0000 0.0000 748 ASN B CG  
5822 O OD1 . ASN A 765 ? 0.9304 0.9304 0.9304 0.0000 0.0000 0.0000 748 ASN B OD1 
5823 N ND2 . ASN A 765 ? 0.9304 0.9304 0.9304 0.0000 0.0000 0.0000 748 ASN B ND2 
5824 N N   . TYR A 766 ? 0.9884 0.9884 0.9884 0.0000 0.0000 0.0000 749 TYR B N   
5825 C CA  . TYR A 766 ? 0.9884 0.9884 0.9884 0.0000 0.0000 0.0000 749 TYR B CA  
5826 C C   . TYR A 766 ? 0.9884 0.9884 0.9884 0.0000 0.0000 0.0000 749 TYR B C   
5827 O O   . TYR A 766 ? 0.9884 0.9884 0.9884 0.0000 0.0000 0.0000 749 TYR B O   
5828 C CB  . TYR A 766 ? 0.9884 0.9884 0.9884 0.0000 0.0000 0.0000 749 TYR B CB  
5829 C CG  . TYR A 766 ? 0.9884 0.9884 0.9884 0.0000 0.0000 0.0000 749 TYR B CG  
5830 C CD1 . TYR A 766 ? 0.9884 0.9884 0.9884 0.0000 0.0000 0.0000 749 TYR B CD1 
5831 C CD2 . TYR A 766 ? 0.9884 0.9884 0.9884 0.0000 0.0000 0.0000 749 TYR B CD2 
5832 C CE1 . TYR A 766 ? 0.9884 0.9884 0.9884 0.0000 0.0000 0.0000 749 TYR B CE1 
5833 C CE2 . TYR A 766 ? 0.9884 0.9884 0.9884 0.0000 0.0000 0.0000 749 TYR B CE2 
5834 C CZ  . TYR A 766 ? 0.9884 0.9884 0.9884 0.0000 0.0000 0.0000 749 TYR B CZ  
5835 O OH  . TYR A 766 ? 0.9884 0.9884 0.9884 0.0000 0.0000 0.0000 749 TYR B OH  
5836 N N   . GLN A 767 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 750 GLN B N   
5837 C CA  . GLN A 767 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 750 GLN B CA  
5838 C C   . GLN A 767 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 750 GLN B C   
5839 O O   . GLN A 767 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 750 GLN B O   
5840 C CB  . GLN A 767 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 750 GLN B CB  
5841 C CG  . GLN A 767 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 750 GLN B CG  
5842 C CD  . GLN A 767 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 750 GLN B CD  
5843 O OE1 . GLN A 767 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 750 GLN B OE1 
5844 N NE2 . GLN A 767 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 750 GLN B NE2 
5845 N N   . TYR A 768 ? 1.0428 1.0428 1.0428 0.0000 0.0000 0.0000 751 TYR B N   
5846 C CA  . TYR A 768 ? 1.0428 1.0428 1.0428 0.0000 0.0000 0.0000 751 TYR B CA  
5847 C C   . TYR A 768 ? 1.0428 1.0428 1.0428 0.0000 0.0000 0.0000 751 TYR B C   
5848 O O   . TYR A 768 ? 1.0428 1.0428 1.0428 0.0000 0.0000 0.0000 751 TYR B O   
5849 C CB  . TYR A 768 ? 1.0428 1.0428 1.0428 0.0000 0.0000 0.0000 751 TYR B CB  
5850 C CG  . TYR A 768 ? 1.0428 1.0428 1.0428 0.0000 0.0000 0.0000 751 TYR B CG  
5851 C CD1 . TYR A 768 ? 1.0428 1.0428 1.0428 0.0000 0.0000 0.0000 751 TYR B CD1 
5852 C CD2 . TYR A 768 ? 1.0428 1.0428 1.0428 0.0000 0.0000 0.0000 751 TYR B CD2 
5853 C CE1 . TYR A 768 ? 1.0428 1.0428 1.0428 0.0000 0.0000 0.0000 751 TYR B CE1 
5854 C CE2 . TYR A 768 ? 1.0428 1.0428 1.0428 0.0000 0.0000 0.0000 751 TYR B CE2 
5855 C CZ  . TYR A 768 ? 1.0428 1.0428 1.0428 0.0000 0.0000 0.0000 751 TYR B CZ  
5856 O OH  . TYR A 768 ? 1.0428 1.0428 1.0428 0.0000 0.0000 0.0000 751 TYR B OH  
5857 N N   . ASN A 769 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 752 ASN B N   
5858 C CA  . ASN A 769 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 752 ASN B CA  
5859 C C   . ASN A 769 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 752 ASN B C   
5860 O O   . ASN A 769 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 752 ASN B O   
5861 C CB  . ASN A 769 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 752 ASN B CB  
5862 C CG  . ASN A 769 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 752 ASN B CG  
5863 O OD1 . ASN A 769 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 752 ASN B OD1 
5864 N ND2 . ASN A 769 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 752 ASN B ND2 
5865 N N   . GLN A 770 ? 0.9807 0.9807 0.9807 0.0000 0.0000 0.0000 753 GLN B N   
5866 C CA  . GLN A 770 ? 0.9807 0.9807 0.9807 0.0000 0.0000 0.0000 753 GLN B CA  
5867 C C   . GLN A 770 ? 0.9807 0.9807 0.9807 0.0000 0.0000 0.0000 753 GLN B C   
5868 O O   . GLN A 770 ? 0.9807 0.9807 0.9807 0.0000 0.0000 0.0000 753 GLN B O   
5869 C CB  . GLN A 770 ? 0.9807 0.9807 0.9807 0.0000 0.0000 0.0000 753 GLN B CB  
5870 C CG  . GLN A 770 ? 0.9807 0.9807 0.9807 0.0000 0.0000 0.0000 753 GLN B CG  
5871 C CD  . GLN A 770 ? 0.9807 0.9807 0.9807 0.0000 0.0000 0.0000 753 GLN B CD  
5872 O OE1 . GLN A 770 ? 0.9807 0.9807 0.9807 0.0000 0.0000 0.0000 753 GLN B OE1 
5873 N NE2 . GLN A 770 ? 0.9807 0.9807 0.9807 0.0000 0.0000 0.0000 753 GLN B NE2 
5874 N N   . TYR A 771 ? 1.0499 1.0499 1.0499 0.0000 0.0000 0.0000 754 TYR B N   
5875 C CA  . TYR A 771 ? 1.0499 1.0499 1.0499 0.0000 0.0000 0.0000 754 TYR B CA  
5876 C C   . TYR A 771 ? 1.0499 1.0499 1.0499 0.0000 0.0000 0.0000 754 TYR B C   
5877 O O   . TYR A 771 ? 1.0499 1.0499 1.0499 0.0000 0.0000 0.0000 754 TYR B O   
5878 C CB  . TYR A 771 ? 1.0499 1.0499 1.0499 0.0000 0.0000 0.0000 754 TYR B CB  
5879 C CG  . TYR A 771 ? 1.0499 1.0499 1.0499 0.0000 0.0000 0.0000 754 TYR B CG  
5880 C CD1 . TYR A 771 ? 1.0499 1.0499 1.0499 0.0000 0.0000 0.0000 754 TYR B CD1 
5881 C CD2 . TYR A 771 ? 1.0499 1.0499 1.0499 0.0000 0.0000 0.0000 754 TYR B CD2 
5882 C CE1 . TYR A 771 ? 1.0499 1.0499 1.0499 0.0000 0.0000 0.0000 754 TYR B CE1 
5883 C CE2 . TYR A 771 ? 1.0499 1.0499 1.0499 0.0000 0.0000 0.0000 754 TYR B CE2 
5884 C CZ  . TYR A 771 ? 1.0499 1.0499 1.0499 0.0000 0.0000 0.0000 754 TYR B CZ  
5885 O OH  . TYR A 771 ? 1.0499 1.0499 1.0499 0.0000 0.0000 0.0000 754 TYR B OH  
5886 N N   . THR A 772 ? 1.1756 1.1756 1.1756 0.0000 0.0000 0.0000 755 THR B N   
5887 C CA  . THR A 772 ? 1.1756 1.1756 1.1756 0.0000 0.0000 0.0000 755 THR B CA  
5888 C C   . THR A 772 ? 1.1756 1.1756 1.1756 0.0000 0.0000 0.0000 755 THR B C   
5889 O O   . THR A 772 ? 1.1756 1.1756 1.1756 0.0000 0.0000 0.0000 755 THR B O   
5890 C CB  . THR A 772 ? 1.1756 1.1756 1.1756 0.0000 0.0000 0.0000 755 THR B CB  
5891 O OG1 . THR A 772 ? 1.1756 1.1756 1.1756 0.0000 0.0000 0.0000 755 THR B OG1 
5892 C CG2 . THR A 772 ? 1.1756 1.1756 1.1756 0.0000 0.0000 0.0000 755 THR B CG2 
5893 N N   . GLU A 773 ? 1.2035 1.2035 1.2035 0.0000 0.0000 0.0000 756 GLU B N   
5894 C CA  . GLU A 773 ? 1.2035 1.2035 1.2035 0.0000 0.0000 0.0000 756 GLU B CA  
5895 C C   . GLU A 773 ? 1.2035 1.2035 1.2035 0.0000 0.0000 0.0000 756 GLU B C   
5896 O O   . GLU A 773 ? 1.2035 1.2035 1.2035 0.0000 0.0000 0.0000 756 GLU B O   
5897 C CB  . GLU A 773 ? 1.2035 1.2035 1.2035 0.0000 0.0000 0.0000 756 GLU B CB  
5898 C CG  . GLU A 773 ? 1.2035 1.2035 1.2035 0.0000 0.0000 0.0000 756 GLU B CG  
5899 C CD  . GLU A 773 ? 1.2035 1.2035 1.2035 0.0000 0.0000 0.0000 756 GLU B CD  
5900 O OE1 . GLU A 773 ? 1.2035 1.2035 1.2035 0.0000 0.0000 0.0000 756 GLU B OE1 
5901 O OE2 . GLU A 773 ? 1.2035 1.2035 1.2035 0.0000 0.0000 0.0000 756 GLU B OE2 
5902 N N   . GLU A 774 ? 1.2104 1.2104 1.2104 0.0000 0.0000 0.0000 757 GLU B N   
5903 C CA  . GLU A 774 ? 1.2104 1.2104 1.2104 0.0000 0.0000 0.0000 757 GLU B CA  
5904 C C   . GLU A 774 ? 1.2104 1.2104 1.2104 0.0000 0.0000 0.0000 757 GLU B C   
5905 O O   . GLU A 774 ? 1.2104 1.2104 1.2104 0.0000 0.0000 0.0000 757 GLU B O   
5906 C CB  . GLU A 774 ? 1.2104 1.2104 1.2104 0.0000 0.0000 0.0000 757 GLU B CB  
5907 C CG  . GLU A 774 ? 1.2104 1.2104 1.2104 0.0000 0.0000 0.0000 757 GLU B CG  
5908 C CD  . GLU A 774 ? 1.2104 1.2104 1.2104 0.0000 0.0000 0.0000 757 GLU B CD  
5909 O OE1 . GLU A 774 ? 1.2104 1.2104 1.2104 0.0000 0.0000 0.0000 757 GLU B OE1 
5910 O OE2 . GLU A 774 ? 1.2104 1.2104 1.2104 0.0000 0.0000 0.0000 757 GLU B OE2 
5911 N N   . GLU A 775 ? 1.1678 1.1678 1.1678 0.0000 0.0000 0.0000 758 GLU B N   
5912 C CA  . GLU A 775 ? 1.1678 1.1678 1.1678 0.0000 0.0000 0.0000 758 GLU B CA  
5913 C C   . GLU A 775 ? 1.1678 1.1678 1.1678 0.0000 0.0000 0.0000 758 GLU B C   
5914 O O   . GLU A 775 ? 1.1678 1.1678 1.1678 0.0000 0.0000 0.0000 758 GLU B O   
5915 C CB  . GLU A 775 ? 1.1678 1.1678 1.1678 0.0000 0.0000 0.0000 758 GLU B CB  
5916 C CG  . GLU A 775 ? 1.1678 1.1678 1.1678 0.0000 0.0000 0.0000 758 GLU B CG  
5917 C CD  . GLU A 775 ? 1.1678 1.1678 1.1678 0.0000 0.0000 0.0000 758 GLU B CD  
5918 O OE1 . GLU A 775 ? 1.1678 1.1678 1.1678 0.0000 0.0000 0.0000 758 GLU B OE1 
5919 O OE2 . GLU A 775 ? 1.1678 1.1678 1.1678 0.0000 0.0000 0.0000 758 GLU B OE2 
5920 N N   . LYS A 776 ? 1.1608 1.1608 1.1608 0.0000 0.0000 0.0000 759 LYS B N   
5921 C CA  . LYS A 776 ? 1.1608 1.1608 1.1608 0.0000 0.0000 0.0000 759 LYS B CA  
5922 C C   . LYS A 776 ? 1.1608 1.1608 1.1608 0.0000 0.0000 0.0000 759 LYS B C   
5923 O O   . LYS A 776 ? 1.1608 1.1608 1.1608 0.0000 0.0000 0.0000 759 LYS B O   
5924 C CB  . LYS A 776 ? 1.1608 1.1608 1.1608 0.0000 0.0000 0.0000 759 LYS B CB  
5925 C CG  . LYS A 776 ? 1.1608 1.1608 1.1608 0.0000 0.0000 0.0000 759 LYS B CG  
5926 C CD  . LYS A 776 ? 1.1608 1.1608 1.1608 0.0000 0.0000 0.0000 759 LYS B CD  
5927 C CE  . LYS A 776 ? 1.1608 1.1608 1.1608 0.0000 0.0000 0.0000 759 LYS B CE  
5928 N NZ  . LYS A 776 ? 1.1608 1.1608 1.1608 0.0000 0.0000 0.0000 759 LYS B NZ  
5929 N N   . ASN A 777 ? 1.2179 1.2179 1.2179 0.0000 0.0000 0.0000 760 ASN B N   
5930 C CA  . ASN A 777 ? 1.2179 1.2179 1.2179 0.0000 0.0000 0.0000 760 ASN B CA  
5931 C C   . ASN A 777 ? 1.2179 1.2179 1.2179 0.0000 0.0000 0.0000 760 ASN B C   
5932 O O   . ASN A 777 ? 1.2179 1.2179 1.2179 0.0000 0.0000 0.0000 760 ASN B O   
5933 C CB  . ASN A 777 ? 1.2179 1.2179 1.2179 0.0000 0.0000 0.0000 760 ASN B CB  
5934 C CG  . ASN A 777 ? 1.2179 1.2179 1.2179 0.0000 0.0000 0.0000 760 ASN B CG  
5935 O OD1 . ASN A 777 ? 1.2179 1.2179 1.2179 0.0000 0.0000 0.0000 760 ASN B OD1 
5936 N ND2 . ASN A 777 ? 1.2179 1.2179 1.2179 0.0000 0.0000 0.0000 760 ASN B ND2 
5937 N N   . ASN A 778 ? 1.1789 1.1789 1.1789 0.0000 0.0000 0.0000 761 ASN B N   
5938 C CA  . ASN A 778 ? 1.1789 1.1789 1.1789 0.0000 0.0000 0.0000 761 ASN B CA  
5939 C C   . ASN A 778 ? 1.1789 1.1789 1.1789 0.0000 0.0000 0.0000 761 ASN B C   
5940 O O   . ASN A 778 ? 1.1789 1.1789 1.1789 0.0000 0.0000 0.0000 761 ASN B O   
5941 C CB  . ASN A 778 ? 1.1789 1.1789 1.1789 0.0000 0.0000 0.0000 761 ASN B CB  
5942 C CG  . ASN A 778 ? 1.1789 1.1789 1.1789 0.0000 0.0000 0.0000 761 ASN B CG  
5943 O OD1 . ASN A 778 ? 1.1789 1.1789 1.1789 0.0000 0.0000 0.0000 761 ASN B OD1 
5944 N ND2 . ASN A 778 ? 1.1789 1.1789 1.1789 0.0000 0.0000 0.0000 761 ASN B ND2 
5945 N N   . ILE A 779 ? 1.2109 1.2109 1.2109 0.0000 0.0000 0.0000 762 ILE B N   
5946 C CA  . ILE A 779 ? 1.2109 1.2109 1.2109 0.0000 0.0000 0.0000 762 ILE B CA  
5947 C C   . ILE A 779 ? 1.2109 1.2109 1.2109 0.0000 0.0000 0.0000 762 ILE B C   
5948 O O   . ILE A 779 ? 1.2109 1.2109 1.2109 0.0000 0.0000 0.0000 762 ILE B O   
5949 C CB  . ILE A 779 ? 1.2109 1.2109 1.2109 0.0000 0.0000 0.0000 762 ILE B CB  
5950 C CG1 . ILE A 779 ? 1.2109 1.2109 1.2109 0.0000 0.0000 0.0000 762 ILE B CG1 
5951 C CG2 . ILE A 779 ? 1.2109 1.2109 1.2109 0.0000 0.0000 0.0000 762 ILE B CG2 
5952 C CD1 . ILE A 779 ? 1.2109 1.2109 1.2109 0.0000 0.0000 0.0000 762 ILE B CD1 
5953 N N   . ASN A 780 ? 1.2389 1.2389 1.2389 0.0000 0.0000 0.0000 763 ASN B N   
5954 C CA  . ASN A 780 ? 1.2389 1.2389 1.2389 0.0000 0.0000 0.0000 763 ASN B CA  
5955 C C   . ASN A 780 ? 1.2389 1.2389 1.2389 0.0000 0.0000 0.0000 763 ASN B C   
5956 O O   . ASN A 780 ? 1.2389 1.2389 1.2389 0.0000 0.0000 0.0000 763 ASN B O   
5957 C CB  . ASN A 780 ? 1.2389 1.2389 1.2389 0.0000 0.0000 0.0000 763 ASN B CB  
5958 C CG  . ASN A 780 ? 1.2389 1.2389 1.2389 0.0000 0.0000 0.0000 763 ASN B CG  
5959 O OD1 . ASN A 780 ? 1.2389 1.2389 1.2389 0.0000 0.0000 0.0000 763 ASN B OD1 
5960 N ND2 . ASN A 780 ? 1.2389 1.2389 1.2389 0.0000 0.0000 0.0000 763 ASN B ND2 
5961 N N   . PHE A 781 ? 1.2052 1.2052 1.2052 0.0000 0.0000 0.0000 764 PHE B N   
5962 C CA  . PHE A 781 ? 1.2052 1.2052 1.2052 0.0000 0.0000 0.0000 764 PHE B CA  
5963 C C   . PHE A 781 ? 1.2052 1.2052 1.2052 0.0000 0.0000 0.0000 764 PHE B C   
5964 O O   . PHE A 781 ? 1.2052 1.2052 1.2052 0.0000 0.0000 0.0000 764 PHE B O   
5965 C CB  . PHE A 781 ? 1.2052 1.2052 1.2052 0.0000 0.0000 0.0000 764 PHE B CB  
5966 C CG  . PHE A 781 ? 1.2052 1.2052 1.2052 0.0000 0.0000 0.0000 764 PHE B CG  
5967 C CD1 . PHE A 781 ? 1.2052 1.2052 1.2052 0.0000 0.0000 0.0000 764 PHE B CD1 
5968 C CD2 . PHE A 781 ? 1.2052 1.2052 1.2052 0.0000 0.0000 0.0000 764 PHE B CD2 
5969 C CE1 . PHE A 781 ? 1.2052 1.2052 1.2052 0.0000 0.0000 0.0000 764 PHE B CE1 
5970 C CE2 . PHE A 781 ? 1.2052 1.2052 1.2052 0.0000 0.0000 0.0000 764 PHE B CE2 
5971 C CZ  . PHE A 781 ? 1.2052 1.2052 1.2052 0.0000 0.0000 0.0000 764 PHE B CZ  
5972 N N   . ASN A 782 ? 1.3021 1.3021 1.3021 0.0000 0.0000 0.0000 765 ASN B N   
5973 C CA  . ASN A 782 ? 1.3021 1.3021 1.3021 0.0000 0.0000 0.0000 765 ASN B CA  
5974 C C   . ASN A 782 ? 1.3021 1.3021 1.3021 0.0000 0.0000 0.0000 765 ASN B C   
5975 O O   . ASN A 782 ? 1.3021 1.3021 1.3021 0.0000 0.0000 0.0000 765 ASN B O   
5976 C CB  . ASN A 782 ? 1.3021 1.3021 1.3021 0.0000 0.0000 0.0000 765 ASN B CB  
5977 C CG  . ASN A 782 ? 1.3021 1.3021 1.3021 0.0000 0.0000 0.0000 765 ASN B CG  
5978 O OD1 . ASN A 782 ? 1.3021 1.3021 1.3021 0.0000 0.0000 0.0000 765 ASN B OD1 
5979 N ND2 . ASN A 782 ? 1.3021 1.3021 1.3021 0.0000 0.0000 0.0000 765 ASN B ND2 
5980 N N   . ILE A 783 ? 1.3134 1.3134 1.3134 0.0000 0.0000 0.0000 766 ILE B N   
5981 C CA  . ILE A 783 ? 1.3134 1.3134 1.3134 0.0000 0.0000 0.0000 766 ILE B CA  
5982 C C   . ILE A 783 ? 1.3134 1.3134 1.3134 0.0000 0.0000 0.0000 766 ILE B C   
5983 O O   . ILE A 783 ? 1.3134 1.3134 1.3134 0.0000 0.0000 0.0000 766 ILE B O   
5984 C CB  . ILE A 783 ? 1.3134 1.3134 1.3134 0.0000 0.0000 0.0000 766 ILE B CB  
5985 C CG1 . ILE A 783 ? 1.3134 1.3134 1.3134 0.0000 0.0000 0.0000 766 ILE B CG1 
5986 C CG2 . ILE A 783 ? 1.3134 1.3134 1.3134 0.0000 0.0000 0.0000 766 ILE B CG2 
5987 C CD1 . ILE A 783 ? 1.3134 1.3134 1.3134 0.0000 0.0000 0.0000 766 ILE B CD1 
5988 N N   . ASP A 784 ? 1.3469 1.3469 1.3469 0.0000 0.0000 0.0000 767 ASP B N   
5989 C CA  . ASP A 784 ? 1.3469 1.3469 1.3469 0.0000 0.0000 0.0000 767 ASP B CA  
5990 C C   . ASP A 784 ? 1.3469 1.3469 1.3469 0.0000 0.0000 0.0000 767 ASP B C   
5991 O O   . ASP A 784 ? 1.3469 1.3469 1.3469 0.0000 0.0000 0.0000 767 ASP B O   
5992 C CB  . ASP A 784 ? 1.3469 1.3469 1.3469 0.0000 0.0000 0.0000 767 ASP B CB  
5993 C CG  . ASP A 784 ? 1.3469 1.3469 1.3469 0.0000 0.0000 0.0000 767 ASP B CG  
5994 O OD1 . ASP A 784 ? 1.3469 1.3469 1.3469 0.0000 0.0000 0.0000 767 ASP B OD1 
5995 O OD2 . ASP A 784 ? 1.3469 1.3469 1.3469 0.0000 0.0000 0.0000 767 ASP B OD2 
5996 N N   . ASP A 785 ? 1.3313 1.3313 1.3313 0.0000 0.0000 0.0000 768 ASP B N   
5997 C CA  . ASP A 785 ? 1.3313 1.3313 1.3313 0.0000 0.0000 0.0000 768 ASP B CA  
5998 C C   . ASP A 785 ? 1.3313 1.3313 1.3313 0.0000 0.0000 0.0000 768 ASP B C   
5999 O O   . ASP A 785 ? 1.3313 1.3313 1.3313 0.0000 0.0000 0.0000 768 ASP B O   
6000 C CB  . ASP A 785 ? 1.3313 1.3313 1.3313 0.0000 0.0000 0.0000 768 ASP B CB  
6001 C CG  . ASP A 785 ? 1.3313 1.3313 1.3313 0.0000 0.0000 0.0000 768 ASP B CG  
6002 O OD1 . ASP A 785 ? 1.3313 1.3313 1.3313 0.0000 0.0000 0.0000 768 ASP B OD1 
6003 O OD2 . ASP A 785 ? 1.3313 1.3313 1.3313 0.0000 0.0000 0.0000 768 ASP B OD2 
6004 N N   . LEU A 786 ? 1.2273 1.2273 1.2273 0.0000 0.0000 0.0000 769 LEU B N   
6005 C CA  . LEU A 786 ? 1.2273 1.2273 1.2273 0.0000 0.0000 0.0000 769 LEU B CA  
6006 C C   . LEU A 786 ? 1.2273 1.2273 1.2273 0.0000 0.0000 0.0000 769 LEU B C   
6007 O O   . LEU A 786 ? 1.2273 1.2273 1.2273 0.0000 0.0000 0.0000 769 LEU B O   
6008 C CB  . LEU A 786 ? 1.2273 1.2273 1.2273 0.0000 0.0000 0.0000 769 LEU B CB  
6009 C CG  . LEU A 786 ? 1.2273 1.2273 1.2273 0.0000 0.0000 0.0000 769 LEU B CG  
6010 C CD1 . LEU A 786 ? 1.2273 1.2273 1.2273 0.0000 0.0000 0.0000 769 LEU B CD1 
6011 C CD2 . LEU A 786 ? 1.2273 1.2273 1.2273 0.0000 0.0000 0.0000 769 LEU B CD2 
6012 N N   . SER A 787 ? 1.2392 1.2392 1.2392 0.0000 0.0000 0.0000 770 SER B N   
6013 C CA  . SER A 787 ? 1.2392 1.2392 1.2392 0.0000 0.0000 0.0000 770 SER B CA  
6014 C C   . SER A 787 ? 1.2392 1.2392 1.2392 0.0000 0.0000 0.0000 770 SER B C   
6015 O O   . SER A 787 ? 1.2392 1.2392 1.2392 0.0000 0.0000 0.0000 770 SER B O   
6016 C CB  . SER A 787 ? 1.2392 1.2392 1.2392 0.0000 0.0000 0.0000 770 SER B CB  
6017 O OG  . SER A 787 ? 1.2392 1.2392 1.2392 0.0000 0.0000 0.0000 770 SER B OG  
6018 N N   . SER A 788 ? 1.2330 1.2330 1.2330 0.0000 0.0000 0.0000 771 SER B N   
6019 C CA  . SER A 788 ? 1.2330 1.2330 1.2330 0.0000 0.0000 0.0000 771 SER B CA  
6020 C C   . SER A 788 ? 1.2330 1.2330 1.2330 0.0000 0.0000 0.0000 771 SER B C   
6021 O O   . SER A 788 ? 1.2330 1.2330 1.2330 0.0000 0.0000 0.0000 771 SER B O   
6022 C CB  . SER A 788 ? 1.2330 1.2330 1.2330 0.0000 0.0000 0.0000 771 SER B CB  
6023 O OG  . SER A 788 ? 1.2330 1.2330 1.2330 0.0000 0.0000 0.0000 771 SER B OG  
6024 N N   . LYS A 789 ? 1.2327 1.2327 1.2327 0.0000 0.0000 0.0000 772 LYS B N   
6025 C CA  . LYS A 789 ? 1.2327 1.2327 1.2327 0.0000 0.0000 0.0000 772 LYS B CA  
6026 C C   . LYS A 789 ? 1.2327 1.2327 1.2327 0.0000 0.0000 0.0000 772 LYS B C   
6027 O O   . LYS A 789 ? 1.2327 1.2327 1.2327 0.0000 0.0000 0.0000 772 LYS B O   
6028 C CB  . LYS A 789 ? 1.2327 1.2327 1.2327 0.0000 0.0000 0.0000 772 LYS B CB  
6029 C CG  . LYS A 789 ? 1.2327 1.2327 1.2327 0.0000 0.0000 0.0000 772 LYS B CG  
6030 C CD  . LYS A 789 ? 1.2327 1.2327 1.2327 0.0000 0.0000 0.0000 772 LYS B CD  
6031 C CE  . LYS A 789 ? 1.2327 1.2327 1.2327 0.0000 0.0000 0.0000 772 LYS B CE  
6032 N NZ  . LYS A 789 ? 1.2327 1.2327 1.2327 0.0000 0.0000 0.0000 772 LYS B NZ  
6033 N N   . LEU A 790 ? 1.1676 1.1676 1.1676 0.0000 0.0000 0.0000 773 LEU B N   
6034 C CA  . LEU A 790 ? 1.1676 1.1676 1.1676 0.0000 0.0000 0.0000 773 LEU B CA  
6035 C C   . LEU A 790 ? 1.1676 1.1676 1.1676 0.0000 0.0000 0.0000 773 LEU B C   
6036 O O   . LEU A 790 ? 1.1676 1.1676 1.1676 0.0000 0.0000 0.0000 773 LEU B O   
6037 C CB  . LEU A 790 ? 1.1676 1.1676 1.1676 0.0000 0.0000 0.0000 773 LEU B CB  
6038 C CG  . LEU A 790 ? 1.1676 1.1676 1.1676 0.0000 0.0000 0.0000 773 LEU B CG  
6039 C CD1 . LEU A 790 ? 1.1676 1.1676 1.1676 0.0000 0.0000 0.0000 773 LEU B CD1 
6040 C CD2 . LEU A 790 ? 1.1676 1.1676 1.1676 0.0000 0.0000 0.0000 773 LEU B CD2 
6041 N N   . ASN A 791 ? 1.1797 1.1797 1.1797 0.0000 0.0000 0.0000 774 ASN B N   
6042 C CA  . ASN A 791 ? 1.1797 1.1797 1.1797 0.0000 0.0000 0.0000 774 ASN B CA  
6043 C C   . ASN A 791 ? 1.1797 1.1797 1.1797 0.0000 0.0000 0.0000 774 ASN B C   
6044 O O   . ASN A 791 ? 1.1797 1.1797 1.1797 0.0000 0.0000 0.0000 774 ASN B O   
6045 C CB  . ASN A 791 ? 1.1797 1.1797 1.1797 0.0000 0.0000 0.0000 774 ASN B CB  
6046 C CG  . ASN A 791 ? 1.1797 1.1797 1.1797 0.0000 0.0000 0.0000 774 ASN B CG  
6047 O OD1 . ASN A 791 ? 1.1797 1.1797 1.1797 0.0000 0.0000 0.0000 774 ASN B OD1 
6048 N ND2 . ASN A 791 ? 1.1797 1.1797 1.1797 0.0000 0.0000 0.0000 774 ASN B ND2 
6049 N N   . GLU A 792 ? 1.1611 1.1611 1.1611 0.0000 0.0000 0.0000 775 GLU B N   
6050 C CA  . GLU A 792 ? 1.1611 1.1611 1.1611 0.0000 0.0000 0.0000 775 GLU B CA  
6051 C C   . GLU A 792 ? 1.1611 1.1611 1.1611 0.0000 0.0000 0.0000 775 GLU B C   
6052 O O   . GLU A 792 ? 1.1611 1.1611 1.1611 0.0000 0.0000 0.0000 775 GLU B O   
6053 C CB  . GLU A 792 ? 1.1611 1.1611 1.1611 0.0000 0.0000 0.0000 775 GLU B CB  
6054 C CG  . GLU A 792 ? 1.1611 1.1611 1.1611 0.0000 0.0000 0.0000 775 GLU B CG  
6055 C CD  . GLU A 792 ? 1.1611 1.1611 1.1611 0.0000 0.0000 0.0000 775 GLU B CD  
6056 O OE1 . GLU A 792 ? 1.1611 1.1611 1.1611 0.0000 0.0000 0.0000 775 GLU B OE1 
6057 O OE2 . GLU A 792 ? 1.1611 1.1611 1.1611 0.0000 0.0000 0.0000 775 GLU B OE2 
6058 N N   . SER A 793 ? 1.1370 1.1370 1.1370 0.0000 0.0000 0.0000 776 SER B N   
6059 C CA  . SER A 793 ? 1.1370 1.1370 1.1370 0.0000 0.0000 0.0000 776 SER B CA  
6060 C C   . SER A 793 ? 1.1370 1.1370 1.1370 0.0000 0.0000 0.0000 776 SER B C   
6061 O O   . SER A 793 ? 1.1370 1.1370 1.1370 0.0000 0.0000 0.0000 776 SER B O   
6062 C CB  . SER A 793 ? 1.1370 1.1370 1.1370 0.0000 0.0000 0.0000 776 SER B CB  
6063 O OG  . SER A 793 ? 1.1370 1.1370 1.1370 0.0000 0.0000 0.0000 776 SER B OG  
6064 N N   . ILE A 794 ? 1.1139 1.1139 1.1139 0.0000 0.0000 0.0000 777 ILE B N   
6065 C CA  . ILE A 794 ? 1.1139 1.1139 1.1139 0.0000 0.0000 0.0000 777 ILE B CA  
6066 C C   . ILE A 794 ? 1.1139 1.1139 1.1139 0.0000 0.0000 0.0000 777 ILE B C   
6067 O O   . ILE A 794 ? 1.1139 1.1139 1.1139 0.0000 0.0000 0.0000 777 ILE B O   
6068 C CB  . ILE A 794 ? 1.1139 1.1139 1.1139 0.0000 0.0000 0.0000 777 ILE B CB  
6069 C CG1 . ILE A 794 ? 1.1139 1.1139 1.1139 0.0000 0.0000 0.0000 777 ILE B CG1 
6070 C CG2 . ILE A 794 ? 1.1139 1.1139 1.1139 0.0000 0.0000 0.0000 777 ILE B CG2 
6071 C CD1 . ILE A 794 ? 1.1139 1.1139 1.1139 0.0000 0.0000 0.0000 777 ILE B CD1 
6072 N N   . ASN A 795 ? 1.1168 1.1168 1.1168 0.0000 0.0000 0.0000 778 ASN B N   
6073 C CA  . ASN A 795 ? 1.1168 1.1168 1.1168 0.0000 0.0000 0.0000 778 ASN B CA  
6074 C C   . ASN A 795 ? 1.1168 1.1168 1.1168 0.0000 0.0000 0.0000 778 ASN B C   
6075 O O   . ASN A 795 ? 1.1168 1.1168 1.1168 0.0000 0.0000 0.0000 778 ASN B O   
6076 C CB  . ASN A 795 ? 1.1168 1.1168 1.1168 0.0000 0.0000 0.0000 778 ASN B CB  
6077 C CG  . ASN A 795 ? 1.1168 1.1168 1.1168 0.0000 0.0000 0.0000 778 ASN B CG  
6078 O OD1 . ASN A 795 ? 1.1168 1.1168 1.1168 0.0000 0.0000 0.0000 778 ASN B OD1 
6079 N ND2 . ASN A 795 ? 1.1168 1.1168 1.1168 0.0000 0.0000 0.0000 778 ASN B ND2 
6080 N N   . LYS A 796 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 779 LYS B N   
6081 C CA  . LYS A 796 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 779 LYS B CA  
6082 C C   . LYS A 796 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 779 LYS B C   
6083 O O   . LYS A 796 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 779 LYS B O   
6084 C CB  . LYS A 796 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 779 LYS B CB  
6085 C CG  . LYS A 796 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 779 LYS B CG  
6086 C CD  . LYS A 796 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 779 LYS B CD  
6087 C CE  . LYS A 796 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 779 LYS B CE  
6088 N NZ  . LYS A 796 ? 1.1128 1.1128 1.1128 0.0000 0.0000 0.0000 779 LYS B NZ  
6089 N N   . ALA A 797 ? 1.0818 1.0818 1.0818 0.0000 0.0000 0.0000 780 ALA B N   
6090 C CA  . ALA A 797 ? 1.0818 1.0818 1.0818 0.0000 0.0000 0.0000 780 ALA B CA  
6091 C C   . ALA A 797 ? 1.0818 1.0818 1.0818 0.0000 0.0000 0.0000 780 ALA B C   
6092 O O   . ALA A 797 ? 1.0818 1.0818 1.0818 0.0000 0.0000 0.0000 780 ALA B O   
6093 C CB  . ALA A 797 ? 1.0818 1.0818 1.0818 0.0000 0.0000 0.0000 780 ALA B CB  
6094 N N   . MET A 798 ? 1.0791 1.0791 1.0791 0.0000 0.0000 0.0000 781 MET B N   
6095 C CA  . MET A 798 ? 1.0791 1.0791 1.0791 0.0000 0.0000 0.0000 781 MET B CA  
6096 C C   . MET A 798 ? 1.0791 1.0791 1.0791 0.0000 0.0000 0.0000 781 MET B C   
6097 O O   . MET A 798 ? 1.0791 1.0791 1.0791 0.0000 0.0000 0.0000 781 MET B O   
6098 C CB  . MET A 798 ? 1.0791 1.0791 1.0791 0.0000 0.0000 0.0000 781 MET B CB  
6099 C CG  . MET A 798 ? 1.0791 1.0791 1.0791 0.0000 0.0000 0.0000 781 MET B CG  
6100 S SD  . MET A 798 ? 1.0791 1.0791 1.0791 0.0000 0.0000 0.0000 781 MET B SD  
6101 C CE  . MET A 798 ? 1.0791 1.0791 1.0791 0.0000 0.0000 0.0000 781 MET B CE  
6102 N N   . ILE A 799 ? 1.0597 1.0597 1.0597 0.0000 0.0000 0.0000 782 ILE B N   
6103 C CA  . ILE A 799 ? 1.0597 1.0597 1.0597 0.0000 0.0000 0.0000 782 ILE B CA  
6104 C C   . ILE A 799 ? 1.0597 1.0597 1.0597 0.0000 0.0000 0.0000 782 ILE B C   
6105 O O   . ILE A 799 ? 1.0597 1.0597 1.0597 0.0000 0.0000 0.0000 782 ILE B O   
6106 C CB  . ILE A 799 ? 1.0597 1.0597 1.0597 0.0000 0.0000 0.0000 782 ILE B CB  
6107 C CG1 . ILE A 799 ? 1.0597 1.0597 1.0597 0.0000 0.0000 0.0000 782 ILE B CG1 
6108 C CG2 . ILE A 799 ? 1.0597 1.0597 1.0597 0.0000 0.0000 0.0000 782 ILE B CG2 
6109 C CD1 . ILE A 799 ? 1.0597 1.0597 1.0597 0.0000 0.0000 0.0000 782 ILE B CD1 
6110 N N   . ASN A 800 ? 1.0699 1.0699 1.0699 0.0000 0.0000 0.0000 783 ASN B N   
6111 C CA  . ASN A 800 ? 1.0699 1.0699 1.0699 0.0000 0.0000 0.0000 783 ASN B CA  
6112 C C   . ASN A 800 ? 1.0699 1.0699 1.0699 0.0000 0.0000 0.0000 783 ASN B C   
6113 O O   . ASN A 800 ? 1.0699 1.0699 1.0699 0.0000 0.0000 0.0000 783 ASN B O   
6114 C CB  . ASN A 800 ? 1.0699 1.0699 1.0699 0.0000 0.0000 0.0000 783 ASN B CB  
6115 C CG  . ASN A 800 ? 1.0699 1.0699 1.0699 0.0000 0.0000 0.0000 783 ASN B CG  
6116 O OD1 . ASN A 800 ? 1.0699 1.0699 1.0699 0.0000 0.0000 0.0000 783 ASN B OD1 
6117 N ND2 . ASN A 800 ? 1.0699 1.0699 1.0699 0.0000 0.0000 0.0000 783 ASN B ND2 
6118 N N   . ILE A 801 ? 1.0417 1.0417 1.0417 0.0000 0.0000 0.0000 784 ILE B N   
6119 C CA  . ILE A 801 ? 1.0417 1.0417 1.0417 0.0000 0.0000 0.0000 784 ILE B CA  
6120 C C   . ILE A 801 ? 1.0417 1.0417 1.0417 0.0000 0.0000 0.0000 784 ILE B C   
6121 O O   . ILE A 801 ? 1.0417 1.0417 1.0417 0.0000 0.0000 0.0000 784 ILE B O   
6122 C CB  . ILE A 801 ? 1.0417 1.0417 1.0417 0.0000 0.0000 0.0000 784 ILE B CB  
6123 C CG1 . ILE A 801 ? 1.0417 1.0417 1.0417 0.0000 0.0000 0.0000 784 ILE B CG1 
6124 C CG2 . ILE A 801 ? 1.0417 1.0417 1.0417 0.0000 0.0000 0.0000 784 ILE B CG2 
6125 C CD1 . ILE A 801 ? 1.0417 1.0417 1.0417 0.0000 0.0000 0.0000 784 ILE B CD1 
6126 N N   . ASN A 802 ? 1.0105 1.0105 1.0105 0.0000 0.0000 0.0000 785 ASN B N   
6127 C CA  . ASN A 802 ? 1.0105 1.0105 1.0105 0.0000 0.0000 0.0000 785 ASN B CA  
6128 C C   . ASN A 802 ? 1.0105 1.0105 1.0105 0.0000 0.0000 0.0000 785 ASN B C   
6129 O O   . ASN A 802 ? 1.0105 1.0105 1.0105 0.0000 0.0000 0.0000 785 ASN B O   
6130 C CB  . ASN A 802 ? 1.0105 1.0105 1.0105 0.0000 0.0000 0.0000 785 ASN B CB  
6131 C CG  . ASN A 802 ? 1.0105 1.0105 1.0105 0.0000 0.0000 0.0000 785 ASN B CG  
6132 O OD1 . ASN A 802 ? 1.0105 1.0105 1.0105 0.0000 0.0000 0.0000 785 ASN B OD1 
6133 N ND2 . ASN A 802 ? 1.0105 1.0105 1.0105 0.0000 0.0000 0.0000 785 ASN B ND2 
6134 N N   . LYS A 803 ? 1.0655 1.0655 1.0655 0.0000 0.0000 0.0000 786 LYS B N   
6135 C CA  . LYS A 803 ? 1.0655 1.0655 1.0655 0.0000 0.0000 0.0000 786 LYS B CA  
6136 C C   . LYS A 803 ? 1.0655 1.0655 1.0655 0.0000 0.0000 0.0000 786 LYS B C   
6137 O O   . LYS A 803 ? 1.0655 1.0655 1.0655 0.0000 0.0000 0.0000 786 LYS B O   
6138 C CB  . LYS A 803 ? 1.0655 1.0655 1.0655 0.0000 0.0000 0.0000 786 LYS B CB  
6139 C CG  . LYS A 803 ? 1.0655 1.0655 1.0655 0.0000 0.0000 0.0000 786 LYS B CG  
6140 C CD  . LYS A 803 ? 1.0655 1.0655 1.0655 0.0000 0.0000 0.0000 786 LYS B CD  
6141 C CE  . LYS A 803 ? 1.0655 1.0655 1.0655 0.0000 0.0000 0.0000 786 LYS B CE  
6142 N NZ  . LYS A 803 ? 1.0655 1.0655 1.0655 0.0000 0.0000 0.0000 786 LYS B NZ  
6143 N N   . PHE A 804 ? 1.0212 1.0212 1.0212 0.0000 0.0000 0.0000 787 PHE B N   
6144 C CA  . PHE A 804 ? 1.0212 1.0212 1.0212 0.0000 0.0000 0.0000 787 PHE B CA  
6145 C C   . PHE A 804 ? 1.0212 1.0212 1.0212 0.0000 0.0000 0.0000 787 PHE B C   
6146 O O   . PHE A 804 ? 1.0212 1.0212 1.0212 0.0000 0.0000 0.0000 787 PHE B O   
6147 C CB  . PHE A 804 ? 1.0212 1.0212 1.0212 0.0000 0.0000 0.0000 787 PHE B CB  
6148 C CG  . PHE A 804 ? 1.0212 1.0212 1.0212 0.0000 0.0000 0.0000 787 PHE B CG  
6149 C CD1 . PHE A 804 ? 1.0212 1.0212 1.0212 0.0000 0.0000 0.0000 787 PHE B CD1 
6150 C CD2 . PHE A 804 ? 1.0212 1.0212 1.0212 0.0000 0.0000 0.0000 787 PHE B CD2 
6151 C CE1 . PHE A 804 ? 1.0212 1.0212 1.0212 0.0000 0.0000 0.0000 787 PHE B CE1 
6152 C CE2 . PHE A 804 ? 1.0212 1.0212 1.0212 0.0000 0.0000 0.0000 787 PHE B CE2 
6153 C CZ  . PHE A 804 ? 1.0212 1.0212 1.0212 0.0000 0.0000 0.0000 787 PHE B CZ  
6154 N N   . LEU A 805 ? 0.9567 0.9567 0.9567 0.0000 0.0000 0.0000 788 LEU B N   
6155 C CA  . LEU A 805 ? 0.9567 0.9567 0.9567 0.0000 0.0000 0.0000 788 LEU B CA  
6156 C C   . LEU A 805 ? 0.9567 0.9567 0.9567 0.0000 0.0000 0.0000 788 LEU B C   
6157 O O   . LEU A 805 ? 0.9567 0.9567 0.9567 0.0000 0.0000 0.0000 788 LEU B O   
6158 C CB  . LEU A 805 ? 0.9567 0.9567 0.9567 0.0000 0.0000 0.0000 788 LEU B CB  
6159 C CG  . LEU A 805 ? 0.9567 0.9567 0.9567 0.0000 0.0000 0.0000 788 LEU B CG  
6160 C CD1 . LEU A 805 ? 0.9567 0.9567 0.9567 0.0000 0.0000 0.0000 788 LEU B CD1 
6161 C CD2 . LEU A 805 ? 0.9567 0.9567 0.9567 0.0000 0.0000 0.0000 788 LEU B CD2 
6162 N N   . ASN A 806 ? 0.9928 0.9928 0.9928 0.0000 0.0000 0.0000 789 ASN B N   
6163 C CA  . ASN A 806 ? 0.9928 0.9928 0.9928 0.0000 0.0000 0.0000 789 ASN B CA  
6164 C C   . ASN A 806 ? 0.9928 0.9928 0.9928 0.0000 0.0000 0.0000 789 ASN B C   
6165 O O   . ASN A 806 ? 0.9928 0.9928 0.9928 0.0000 0.0000 0.0000 789 ASN B O   
6166 C CB  . ASN A 806 ? 0.9928 0.9928 0.9928 0.0000 0.0000 0.0000 789 ASN B CB  
6167 C CG  . ASN A 806 ? 0.9928 0.9928 0.9928 0.0000 0.0000 0.0000 789 ASN B CG  
6168 O OD1 . ASN A 806 ? 0.9928 0.9928 0.9928 0.0000 0.0000 0.0000 789 ASN B OD1 
6169 N ND2 . ASN A 806 ? 0.9928 0.9928 0.9928 0.0000 0.0000 0.0000 789 ASN B ND2 
6170 N N   . GLN A 807 ? 1.0291 1.0291 1.0291 0.0000 0.0000 0.0000 790 GLN B N   
6171 C CA  . GLN A 807 ? 1.0291 1.0291 1.0291 0.0000 0.0000 0.0000 790 GLN B CA  
6172 C C   . GLN A 807 ? 1.0291 1.0291 1.0291 0.0000 0.0000 0.0000 790 GLN B C   
6173 O O   . GLN A 807 ? 1.0291 1.0291 1.0291 0.0000 0.0000 0.0000 790 GLN B O   
6174 C CB  . GLN A 807 ? 1.0291 1.0291 1.0291 0.0000 0.0000 0.0000 790 GLN B CB  
6175 C CG  . GLN A 807 ? 1.0291 1.0291 1.0291 0.0000 0.0000 0.0000 790 GLN B CG  
6176 C CD  . GLN A 807 ? 1.0291 1.0291 1.0291 0.0000 0.0000 0.0000 790 GLN B CD  
6177 O OE1 . GLN A 807 ? 1.0291 1.0291 1.0291 0.0000 0.0000 0.0000 790 GLN B OE1 
6178 N NE2 . GLN A 807 ? 1.0291 1.0291 1.0291 0.0000 0.0000 0.0000 790 GLN B NE2 
6179 N N   . CYS A 808 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 791 CYS B N   
6180 C CA  . CYS A 808 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 791 CYS B CA  
6181 C C   . CYS A 808 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 791 CYS B C   
6182 O O   . CYS A 808 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 791 CYS B O   
6183 C CB  . CYS A 808 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 791 CYS B CB  
6184 S SG  . CYS A 808 ? 0.9933 0.9933 0.9933 0.0000 0.0000 0.0000 791 CYS B SG  
6185 N N   . SER A 809 ? 0.9519 0.9519 0.9519 0.0000 0.0000 0.0000 792 SER B N   
6186 C CA  . SER A 809 ? 0.9519 0.9519 0.9519 0.0000 0.0000 0.0000 792 SER B CA  
6187 C C   . SER A 809 ? 0.9519 0.9519 0.9519 0.0000 0.0000 0.0000 792 SER B C   
6188 O O   . SER A 809 ? 0.9519 0.9519 0.9519 0.0000 0.0000 0.0000 792 SER B O   
6189 C CB  . SER A 809 ? 0.9519 0.9519 0.9519 0.0000 0.0000 0.0000 792 SER B CB  
6190 O OG  . SER A 809 ? 0.9519 0.9519 0.9519 0.0000 0.0000 0.0000 792 SER B OG  
6191 N N   . VAL A 810 ? 0.8962 0.8962 0.8962 0.0000 0.0000 0.0000 793 VAL B N   
6192 C CA  . VAL A 810 ? 0.8962 0.8962 0.8962 0.0000 0.0000 0.0000 793 VAL B CA  
6193 C C   . VAL A 810 ? 0.8962 0.8962 0.8962 0.0000 0.0000 0.0000 793 VAL B C   
6194 O O   . VAL A 810 ? 0.8962 0.8962 0.8962 0.0000 0.0000 0.0000 793 VAL B O   
6195 C CB  . VAL A 810 ? 0.8962 0.8962 0.8962 0.0000 0.0000 0.0000 793 VAL B CB  
6196 C CG1 . VAL A 810 ? 0.8962 0.8962 0.8962 0.0000 0.0000 0.0000 793 VAL B CG1 
6197 C CG2 . VAL A 810 ? 0.8962 0.8962 0.8962 0.0000 0.0000 0.0000 793 VAL B CG2 
6198 N N   . SER A 811 ? 0.9280 0.9280 0.9280 0.0000 0.0000 0.0000 794 SER B N   
6199 C CA  . SER A 811 ? 0.9280 0.9280 0.9280 0.0000 0.0000 0.0000 794 SER B CA  
6200 C C   . SER A 811 ? 0.9280 0.9280 0.9280 0.0000 0.0000 0.0000 794 SER B C   
6201 O O   . SER A 811 ? 0.9280 0.9280 0.9280 0.0000 0.0000 0.0000 794 SER B O   
6202 C CB  . SER A 811 ? 0.9280 0.9280 0.9280 0.0000 0.0000 0.0000 794 SER B CB  
6203 O OG  . SER A 811 ? 0.9280 0.9280 0.9280 0.0000 0.0000 0.0000 794 SER B OG  
6204 N N   . TYR A 812 ? 0.8867 0.8867 0.8867 0.0000 0.0000 0.0000 795 TYR B N   
6205 C CA  . TYR A 812 ? 0.8867 0.8867 0.8867 0.0000 0.0000 0.0000 795 TYR B CA  
6206 C C   . TYR A 812 ? 0.8867 0.8867 0.8867 0.0000 0.0000 0.0000 795 TYR B C   
6207 O O   . TYR A 812 ? 0.8867 0.8867 0.8867 0.0000 0.0000 0.0000 795 TYR B O   
6208 C CB  . TYR A 812 ? 0.8867 0.8867 0.8867 0.0000 0.0000 0.0000 795 TYR B CB  
6209 C CG  . TYR A 812 ? 0.8867 0.8867 0.8867 0.0000 0.0000 0.0000 795 TYR B CG  
6210 C CD1 . TYR A 812 ? 0.8867 0.8867 0.8867 0.0000 0.0000 0.0000 795 TYR B CD1 
6211 C CD2 . TYR A 812 ? 0.8867 0.8867 0.8867 0.0000 0.0000 0.0000 795 TYR B CD2 
6212 C CE1 . TYR A 812 ? 0.8867 0.8867 0.8867 0.0000 0.0000 0.0000 795 TYR B CE1 
6213 C CE2 . TYR A 812 ? 0.8867 0.8867 0.8867 0.0000 0.0000 0.0000 795 TYR B CE2 
6214 C CZ  . TYR A 812 ? 0.8867 0.8867 0.8867 0.0000 0.0000 0.0000 795 TYR B CZ  
6215 O OH  . TYR A 812 ? 0.8867 0.8867 0.8867 0.0000 0.0000 0.0000 795 TYR B OH  
6216 N N   . LEU A 813 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 796 LEU B N   
6217 C CA  . LEU A 813 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 796 LEU B CA  
6218 C C   . LEU A 813 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 796 LEU B C   
6219 O O   . LEU A 813 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 796 LEU B O   
6220 C CB  . LEU A 813 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 796 LEU B CB  
6221 C CG  . LEU A 813 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 796 LEU B CG  
6222 C CD1 . LEU A 813 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 796 LEU B CD1 
6223 C CD2 . LEU A 813 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 796 LEU B CD2 
6224 N N   . MET A 814 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 797 MET B N   
6225 C CA  . MET A 814 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 797 MET B CA  
6226 C C   . MET A 814 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 797 MET B C   
6227 O O   . MET A 814 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 797 MET B O   
6228 C CB  . MET A 814 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 797 MET B CB  
6229 C CG  . MET A 814 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 797 MET B CG  
6230 S SD  . MET A 814 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 797 MET B SD  
6231 C CE  . MET A 814 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 797 MET B CE  
6232 N N   . ASN A 815 ? 0.8849 0.8849 0.8849 0.0000 0.0000 0.0000 798 ASN B N   
6233 C CA  . ASN A 815 ? 0.8849 0.8849 0.8849 0.0000 0.0000 0.0000 798 ASN B CA  
6234 C C   . ASN A 815 ? 0.8849 0.8849 0.8849 0.0000 0.0000 0.0000 798 ASN B C   
6235 O O   . ASN A 815 ? 0.8849 0.8849 0.8849 0.0000 0.0000 0.0000 798 ASN B O   
6236 C CB  . ASN A 815 ? 0.8849 0.8849 0.8849 0.0000 0.0000 0.0000 798 ASN B CB  
6237 C CG  . ASN A 815 ? 0.8849 0.8849 0.8849 0.0000 0.0000 0.0000 798 ASN B CG  
6238 O OD1 . ASN A 815 ? 0.8849 0.8849 0.8849 0.0000 0.0000 0.0000 798 ASN B OD1 
6239 N ND2 . ASN A 815 ? 0.8849 0.8849 0.8849 0.0000 0.0000 0.0000 798 ASN B ND2 
6240 N N   . SER A 816 ? 0.8862 0.8862 0.8862 0.0000 0.0000 0.0000 799 SER B N   
6241 C CA  . SER A 816 ? 0.8862 0.8862 0.8862 0.0000 0.0000 0.0000 799 SER B CA  
6242 C C   . SER A 816 ? 0.8862 0.8862 0.8862 0.0000 0.0000 0.0000 799 SER B C   
6243 O O   . SER A 816 ? 0.8862 0.8862 0.8862 0.0000 0.0000 0.0000 799 SER B O   
6244 C CB  . SER A 816 ? 0.8862 0.8862 0.8862 0.0000 0.0000 0.0000 799 SER B CB  
6245 O OG  . SER A 816 ? 0.8862 0.8862 0.8862 0.0000 0.0000 0.0000 799 SER B OG  
6246 N N   . MET A 817 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 800 MET B N   
6247 C CA  . MET A 817 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 800 MET B CA  
6248 C C   . MET A 817 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 800 MET B C   
6249 O O   . MET A 817 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 800 MET B O   
6250 C CB  . MET A 817 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 800 MET B CB  
6251 C CG  . MET A 817 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 800 MET B CG  
6252 S SD  . MET A 817 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 800 MET B SD  
6253 C CE  . MET A 817 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 800 MET B CE  
6254 N N   . ILE A 818 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 801 ILE B N   
6255 C CA  . ILE A 818 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 801 ILE B CA  
6256 C C   . ILE A 818 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 801 ILE B C   
6257 O O   . ILE A 818 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 801 ILE B O   
6258 C CB  . ILE A 818 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 801 ILE B CB  
6259 C CG1 . ILE A 818 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 801 ILE B CG1 
6260 C CG2 . ILE A 818 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 801 ILE B CG2 
6261 C CD1 . ILE A 818 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 801 ILE B CD1 
6262 N N   . PRO A 819 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 802 PRO B N   
6263 C CA  . PRO A 819 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 802 PRO B CA  
6264 C C   . PRO A 819 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 802 PRO B C   
6265 O O   . PRO A 819 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 802 PRO B O   
6266 C CB  . PRO A 819 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 802 PRO B CB  
6267 C CG  . PRO A 819 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 802 PRO B CG  
6268 C CD  . PRO A 819 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 802 PRO B CD  
6269 N N   . TYR A 820 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 803 TYR B N   
6270 C CA  . TYR A 820 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 803 TYR B CA  
6271 C C   . TYR A 820 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 803 TYR B C   
6272 O O   . TYR A 820 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 803 TYR B O   
6273 C CB  . TYR A 820 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 803 TYR B CB  
6274 C CG  . TYR A 820 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 803 TYR B CG  
6275 C CD1 . TYR A 820 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 803 TYR B CD1 
6276 C CD2 . TYR A 820 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 803 TYR B CD2 
6277 C CE1 . TYR A 820 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 803 TYR B CE1 
6278 C CE2 . TYR A 820 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 803 TYR B CE2 
6279 C CZ  . TYR A 820 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 803 TYR B CZ  
6280 O OH  . TYR A 820 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 803 TYR B OH  
6281 N N   . GLY A 821 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 804 GLY B N   
6282 C CA  . GLY A 821 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 804 GLY B CA  
6283 C C   . GLY A 821 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 804 GLY B C   
6284 O O   . GLY A 821 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 804 GLY B O   
6285 N N   . VAL A 822 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 805 VAL B N   
6286 C CA  . VAL A 822 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 805 VAL B CA  
6287 C C   . VAL A 822 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 805 VAL B C   
6288 O O   . VAL A 822 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 805 VAL B O   
6289 C CB  . VAL A 822 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 805 VAL B CB  
6290 C CG1 . VAL A 822 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 805 VAL B CG1 
6291 C CG2 . VAL A 822 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 805 VAL B CG2 
6292 N N   . LYS A 823 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 806 LYS B N   
6293 C CA  . LYS A 823 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 806 LYS B CA  
6294 C C   . LYS A 823 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 806 LYS B C   
6295 O O   . LYS A 823 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 806 LYS B O   
6296 C CB  . LYS A 823 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 806 LYS B CB  
6297 C CG  . LYS A 823 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 806 LYS B CG  
6298 C CD  . LYS A 823 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 806 LYS B CD  
6299 C CE  . LYS A 823 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 806 LYS B CE  
6300 N NZ  . LYS A 823 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 806 LYS B NZ  
6301 N N   . ARG A 824 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 807 ARG B N   
6302 C CA  . ARG A 824 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 807 ARG B CA  
6303 C C   . ARG A 824 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 807 ARG B C   
6304 O O   . ARG A 824 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 807 ARG B O   
6305 C CB  . ARG A 824 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 807 ARG B CB  
6306 C CG  . ARG A 824 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 807 ARG B CG  
6307 C CD  . ARG A 824 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 807 ARG B CD  
6308 N NE  . ARG A 824 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 807 ARG B NE  
6309 C CZ  . ARG A 824 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 807 ARG B CZ  
6310 N NH1 . ARG A 824 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 807 ARG B NH1 
6311 N NH2 . ARG A 824 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 807 ARG B NH2 
6312 N N   . LEU A 825 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 808 LEU B N   
6313 C CA  . LEU A 825 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 808 LEU B CA  
6314 C C   . LEU A 825 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 808 LEU B C   
6315 O O   . LEU A 825 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 808 LEU B O   
6316 C CB  . LEU A 825 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 808 LEU B CB  
6317 C CG  . LEU A 825 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 808 LEU B CG  
6318 C CD1 . LEU A 825 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 808 LEU B CD1 
6319 C CD2 . LEU A 825 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 808 LEU B CD2 
6320 N N   . GLU A 826 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 809 GLU B N   
6321 C CA  . GLU A 826 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 809 GLU B CA  
6322 C C   . GLU A 826 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 809 GLU B C   
6323 O O   . GLU A 826 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 809 GLU B O   
6324 C CB  . GLU A 826 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 809 GLU B CB  
6325 C CG  . GLU A 826 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 809 GLU B CG  
6326 C CD  . GLU A 826 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 809 GLU B CD  
6327 O OE1 . GLU A 826 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 809 GLU B OE1 
6328 O OE2 . GLU A 826 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 809 GLU B OE2 
6329 N N   . ASP A 827 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 810 ASP B N   
6330 C CA  . ASP A 827 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 810 ASP B CA  
6331 C C   . ASP A 827 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 810 ASP B C   
6332 O O   . ASP A 827 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 810 ASP B O   
6333 C CB  . ASP A 827 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 810 ASP B CB  
6334 C CG  . ASP A 827 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 810 ASP B CG  
6335 O OD1 . ASP A 827 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 810 ASP B OD1 
6336 O OD2 . ASP A 827 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 810 ASP B OD2 
6337 N N   . PHE A 828 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 811 PHE B N   
6338 C CA  . PHE A 828 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 811 PHE B CA  
6339 C C   . PHE A 828 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 811 PHE B C   
6340 O O   . PHE A 828 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 811 PHE B O   
6341 C CB  . PHE A 828 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 811 PHE B CB  
6342 C CG  . PHE A 828 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 811 PHE B CG  
6343 C CD1 . PHE A 828 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 811 PHE B CD1 
6344 C CD2 . PHE A 828 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 811 PHE B CD2 
6345 C CE1 . PHE A 828 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 811 PHE B CE1 
6346 C CE2 . PHE A 828 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 811 PHE B CE2 
6347 C CZ  . PHE A 828 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 811 PHE B CZ  
6348 N N   . ASP A 829 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 812 ASP B N   
6349 C CA  . ASP A 829 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 812 ASP B CA  
6350 C C   . ASP A 829 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 812 ASP B C   
6351 O O   . ASP A 829 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 812 ASP B O   
6352 C CB  . ASP A 829 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 812 ASP B CB  
6353 C CG  . ASP A 829 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 812 ASP B CG  
6354 O OD1 . ASP A 829 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 812 ASP B OD1 
6355 O OD2 . ASP A 829 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 812 ASP B OD2 
6356 N N   . ALA A 830 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 813 ALA B N   
6357 C CA  . ALA A 830 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 813 ALA B CA  
6358 C C   . ALA A 830 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 813 ALA B C   
6359 O O   . ALA A 830 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 813 ALA B O   
6360 C CB  . ALA A 830 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 813 ALA B CB  
6361 N N   . SER A 831 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 814 SER B N   
6362 C CA  . SER A 831 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 814 SER B CA  
6363 C C   . SER A 831 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 814 SER B C   
6364 O O   . SER A 831 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 814 SER B O   
6365 C CB  . SER A 831 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 814 SER B CB  
6366 O OG  . SER A 831 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 814 SER B OG  
6367 N N   . LEU A 832 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 815 LEU B N   
6368 C CA  . LEU A 832 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 815 LEU B CA  
6369 C C   . LEU A 832 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 815 LEU B C   
6370 O O   . LEU A 832 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 815 LEU B O   
6371 C CB  . LEU A 832 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 815 LEU B CB  
6372 C CG  . LEU A 832 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 815 LEU B CG  
6373 C CD1 . LEU A 832 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 815 LEU B CD1 
6374 C CD2 . LEU A 832 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 815 LEU B CD2 
6375 N N   . LYS A 833 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 816 LYS B N   
6376 C CA  . LYS A 833 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 816 LYS B CA  
6377 C C   . LYS A 833 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 816 LYS B C   
6378 O O   . LYS A 833 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 816 LYS B O   
6379 C CB  . LYS A 833 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 816 LYS B CB  
6380 C CG  . LYS A 833 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 816 LYS B CG  
6381 C CD  . LYS A 833 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 816 LYS B CD  
6382 C CE  . LYS A 833 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 816 LYS B CE  
6383 N NZ  . LYS A 833 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 816 LYS B NZ  
6384 N N   . ASP A 834 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 817 ASP B N   
6385 C CA  . ASP A 834 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 817 ASP B CA  
6386 C C   . ASP A 834 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 817 ASP B C   
6387 O O   . ASP A 834 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 817 ASP B O   
6388 C CB  . ASP A 834 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 817 ASP B CB  
6389 C CG  . ASP A 834 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 817 ASP B CG  
6390 O OD1 . ASP A 834 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 817 ASP B OD1 
6391 O OD2 . ASP A 834 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 817 ASP B OD2 
6392 N N   . ALA A 835 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 818 ALA B N   
6393 C CA  . ALA A 835 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 818 ALA B CA  
6394 C C   . ALA A 835 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 818 ALA B C   
6395 O O   . ALA A 835 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 818 ALA B O   
6396 C CB  . ALA A 835 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 818 ALA B CB  
6397 N N   . LEU A 836 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 819 LEU B N   
6398 C CA  . LEU A 836 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 819 LEU B CA  
6399 C C   . LEU A 836 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 819 LEU B C   
6400 O O   . LEU A 836 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 819 LEU B O   
6401 C CB  . LEU A 836 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 819 LEU B CB  
6402 C CG  . LEU A 836 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 819 LEU B CG  
6403 C CD1 . LEU A 836 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 819 LEU B CD1 
6404 C CD2 . LEU A 836 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 819 LEU B CD2 
6405 N N   . LEU A 837 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 820 LEU B N   
6406 C CA  . LEU A 837 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 820 LEU B CA  
6407 C C   . LEU A 837 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 820 LEU B C   
6408 O O   . LEU A 837 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 820 LEU B O   
6409 C CB  . LEU A 837 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 820 LEU B CB  
6410 C CG  . LEU A 837 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 820 LEU B CG  
6411 C CD1 . LEU A 837 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 820 LEU B CD1 
6412 C CD2 . LEU A 837 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 820 LEU B CD2 
6413 N N   . LYS A 838 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 821 LYS B N   
6414 C CA  . LYS A 838 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 821 LYS B CA  
6415 C C   . LYS A 838 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 821 LYS B C   
6416 O O   . LYS A 838 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 821 LYS B O   
6417 C CB  . LYS A 838 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 821 LYS B CB  
6418 C CG  . LYS A 838 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 821 LYS B CG  
6419 C CD  . LYS A 838 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 821 LYS B CD  
6420 C CE  . LYS A 838 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 821 LYS B CE  
6421 N NZ  . LYS A 838 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 821 LYS B NZ  
6422 N N   . TYR A 839 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 822 TYR B N   
6423 C CA  . TYR A 839 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 822 TYR B CA  
6424 C C   . TYR A 839 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 822 TYR B C   
6425 O O   . TYR A 839 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 822 TYR B O   
6426 C CB  . TYR A 839 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 822 TYR B CB  
6427 C CG  . TYR A 839 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 822 TYR B CG  
6428 C CD1 . TYR A 839 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 822 TYR B CD1 
6429 C CD2 . TYR A 839 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 822 TYR B CD2 
6430 C CE1 . TYR A 839 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 822 TYR B CE1 
6431 C CE2 . TYR A 839 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 822 TYR B CE2 
6432 C CZ  . TYR A 839 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 822 TYR B CZ  
6433 O OH  . TYR A 839 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 822 TYR B OH  
6434 N N   . ILE A 840 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 823 ILE B N   
6435 C CA  . ILE A 840 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 823 ILE B CA  
6436 C C   . ILE A 840 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 823 ILE B C   
6437 O O   . ILE A 840 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 823 ILE B O   
6438 C CB  . ILE A 840 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 823 ILE B CB  
6439 C CG1 . ILE A 840 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 823 ILE B CG1 
6440 C CG2 . ILE A 840 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 823 ILE B CG2 
6441 C CD1 . ILE A 840 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 823 ILE B CD1 
6442 N N   . TYR A 841 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 824 TYR B N   
6443 C CA  . TYR A 841 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 824 TYR B CA  
6444 C C   . TYR A 841 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 824 TYR B C   
6445 O O   . TYR A 841 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 824 TYR B O   
6446 C CB  . TYR A 841 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 824 TYR B CB  
6447 C CG  . TYR A 841 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 824 TYR B CG  
6448 C CD1 . TYR A 841 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 824 TYR B CD1 
6449 C CD2 . TYR A 841 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 824 TYR B CD2 
6450 C CE1 . TYR A 841 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 824 TYR B CE1 
6451 C CE2 . TYR A 841 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 824 TYR B CE2 
6452 C CZ  . TYR A 841 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 824 TYR B CZ  
6453 O OH  . TYR A 841 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 824 TYR B OH  
6454 N N   . ILE A 848 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 831 ILE B N   
6455 C CA  . ILE A 848 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 831 ILE B CA  
6456 C C   . ILE A 848 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 831 ILE B C   
6457 O O   . ILE A 848 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 831 ILE B O   
6458 C CB  . ILE A 848 ? 0.8815 0.8815 0.8815 0.0000 0.0000 0.0000 831 ILE B CB  
6459 N N   . GLY A 849 ? 0.8882 0.8882 0.8882 0.0000 0.0000 0.0000 832 GLY B N   
6460 C CA  . GLY A 849 ? 0.8882 0.8882 0.8882 0.0000 0.0000 0.0000 832 GLY B CA  
6461 C C   . GLY A 849 ? 0.8882 0.8882 0.8882 0.0000 0.0000 0.0000 832 GLY B C   
6462 O O   . GLY A 849 ? 0.8882 0.8882 0.8882 0.0000 0.0000 0.0000 832 GLY B O   
6463 N N   . GLN A 850 ? 0.9229 0.9229 0.9229 0.0000 0.0000 0.0000 833 GLN B N   
6464 C CA  . GLN A 850 ? 0.9229 0.9229 0.9229 0.0000 0.0000 0.0000 833 GLN B CA  
6465 C C   . GLN A 850 ? 0.9229 0.9229 0.9229 0.0000 0.0000 0.0000 833 GLN B C   
6466 O O   . GLN A 850 ? 0.9229 0.9229 0.9229 0.0000 0.0000 0.0000 833 GLN B O   
6467 C CB  . GLN A 850 ? 0.9229 0.9229 0.9229 0.0000 0.0000 0.0000 833 GLN B CB  
6468 C CG  . GLN A 850 ? 0.9229 0.9229 0.9229 0.0000 0.0000 0.0000 833 GLN B CG  
6469 C CD  . GLN A 850 ? 0.9229 0.9229 0.9229 0.0000 0.0000 0.0000 833 GLN B CD  
6470 O OE1 . GLN A 850 ? 0.9229 0.9229 0.9229 0.0000 0.0000 0.0000 833 GLN B OE1 
6471 N NE2 . GLN A 850 ? 0.9229 0.9229 0.9229 0.0000 0.0000 0.0000 833 GLN B NE2 
6472 N N   . VAL A 851 ? 0.9095 0.9095 0.9095 0.0000 0.0000 0.0000 834 VAL B N   
6473 C CA  . VAL A 851 ? 0.9095 0.9095 0.9095 0.0000 0.0000 0.0000 834 VAL B CA  
6474 C C   . VAL A 851 ? 0.9095 0.9095 0.9095 0.0000 0.0000 0.0000 834 VAL B C   
6475 O O   . VAL A 851 ? 0.9095 0.9095 0.9095 0.0000 0.0000 0.0000 834 VAL B O   
6476 C CB  . VAL A 851 ? 0.9095 0.9095 0.9095 0.0000 0.0000 0.0000 834 VAL B CB  
6477 C CG1 . VAL A 851 ? 0.9095 0.9095 0.9095 0.0000 0.0000 0.0000 834 VAL B CG1 
6478 C CG2 . VAL A 851 ? 0.9095 0.9095 0.9095 0.0000 0.0000 0.0000 834 VAL B CG2 
6479 N N   . ASP A 852 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 835 ASP B N   
6480 C CA  . ASP A 852 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 835 ASP B CA  
6481 C C   . ASP A 852 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 835 ASP B C   
6482 O O   . ASP A 852 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 835 ASP B O   
6483 C CB  . ASP A 852 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 835 ASP B CB  
6484 C CG  . ASP A 852 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 835 ASP B CG  
6485 O OD1 . ASP A 852 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 835 ASP B OD1 
6486 O OD2 . ASP A 852 ? 0.9777 0.9777 0.9777 0.0000 0.0000 0.0000 835 ASP B OD2 
6487 N N   . ARG A 853 ? 0.9569 0.9569 0.9569 0.0000 0.0000 0.0000 836 ARG B N   
6488 C CA  . ARG A 853 ? 0.9569 0.9569 0.9569 0.0000 0.0000 0.0000 836 ARG B CA  
6489 C C   . ARG A 853 ? 0.9569 0.9569 0.9569 0.0000 0.0000 0.0000 836 ARG B C   
6490 O O   . ARG A 853 ? 0.9569 0.9569 0.9569 0.0000 0.0000 0.0000 836 ARG B O   
6491 C CB  . ARG A 853 ? 0.9569 0.9569 0.9569 0.0000 0.0000 0.0000 836 ARG B CB  
6492 C CG  . ARG A 853 ? 0.9569 0.9569 0.9569 0.0000 0.0000 0.0000 836 ARG B CG  
6493 C CD  . ARG A 853 ? 0.9569 0.9569 0.9569 0.0000 0.0000 0.0000 836 ARG B CD  
6494 N NE  . ARG A 853 ? 0.9569 0.9569 0.9569 0.0000 0.0000 0.0000 836 ARG B NE  
6495 C CZ  . ARG A 853 ? 0.9569 0.9569 0.9569 0.0000 0.0000 0.0000 836 ARG B CZ  
6496 N NH1 . ARG A 853 ? 0.9569 0.9569 0.9569 0.0000 0.0000 0.0000 836 ARG B NH1 
6497 N NH2 . ARG A 853 ? 0.9569 0.9569 0.9569 0.0000 0.0000 0.0000 836 ARG B NH2 
6498 N N   . LEU A 854 ? 0.8948 0.8948 0.8948 0.0000 0.0000 0.0000 837 LEU B N   
6499 C CA  . LEU A 854 ? 0.8948 0.8948 0.8948 0.0000 0.0000 0.0000 837 LEU B CA  
6500 C C   . LEU A 854 ? 0.8948 0.8948 0.8948 0.0000 0.0000 0.0000 837 LEU B C   
6501 O O   . LEU A 854 ? 0.8948 0.8948 0.8948 0.0000 0.0000 0.0000 837 LEU B O   
6502 C CB  . LEU A 854 ? 0.8948 0.8948 0.8948 0.0000 0.0000 0.0000 837 LEU B CB  
6503 C CG  . LEU A 854 ? 0.8948 0.8948 0.8948 0.0000 0.0000 0.0000 837 LEU B CG  
6504 C CD1 . LEU A 854 ? 0.8948 0.8948 0.8948 0.0000 0.0000 0.0000 837 LEU B CD1 
6505 C CD2 . LEU A 854 ? 0.8948 0.8948 0.8948 0.0000 0.0000 0.0000 837 LEU B CD2 
6506 N N   . LYS A 855 ? 0.8907 0.8907 0.8907 0.0000 0.0000 0.0000 838 LYS B N   
6507 C CA  . LYS A 855 ? 0.8907 0.8907 0.8907 0.0000 0.0000 0.0000 838 LYS B CA  
6508 C C   . LYS A 855 ? 0.8907 0.8907 0.8907 0.0000 0.0000 0.0000 838 LYS B C   
6509 O O   . LYS A 855 ? 0.8907 0.8907 0.8907 0.0000 0.0000 0.0000 838 LYS B O   
6510 C CB  . LYS A 855 ? 0.8907 0.8907 0.8907 0.0000 0.0000 0.0000 838 LYS B CB  
6511 C CG  . LYS A 855 ? 0.8907 0.8907 0.8907 0.0000 0.0000 0.0000 838 LYS B CG  
6512 C CD  . LYS A 855 ? 0.8907 0.8907 0.8907 0.0000 0.0000 0.0000 838 LYS B CD  
6513 C CE  . LYS A 855 ? 0.8907 0.8907 0.8907 0.0000 0.0000 0.0000 838 LYS B CE  
6514 N NZ  . LYS A 855 ? 0.8907 0.8907 0.8907 0.0000 0.0000 0.0000 838 LYS B NZ  
6515 N N   . ASP A 856 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 839 ASP B N   
6516 C CA  . ASP A 856 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 839 ASP B CA  
6517 C C   . ASP A 856 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 839 ASP B C   
6518 O O   . ASP A 856 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 839 ASP B O   
6519 C CB  . ASP A 856 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 839 ASP B CB  
6520 C CG  . ASP A 856 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 839 ASP B CG  
6521 O OD1 . ASP A 856 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 839 ASP B OD1 
6522 O OD2 . ASP A 856 ? 0.9582 0.9582 0.9582 0.0000 0.0000 0.0000 839 ASP B OD2 
6523 N N   . LYS A 857 ? 0.9065 0.9065 0.9065 0.0000 0.0000 0.0000 840 LYS B N   
6524 C CA  . LYS A 857 ? 0.9065 0.9065 0.9065 0.0000 0.0000 0.0000 840 LYS B CA  
6525 C C   . LYS A 857 ? 0.9065 0.9065 0.9065 0.0000 0.0000 0.0000 840 LYS B C   
6526 O O   . LYS A 857 ? 0.9065 0.9065 0.9065 0.0000 0.0000 0.0000 840 LYS B O   
6527 C CB  . LYS A 857 ? 0.9065 0.9065 0.9065 0.0000 0.0000 0.0000 840 LYS B CB  
6528 C CG  . LYS A 857 ? 0.9065 0.9065 0.9065 0.0000 0.0000 0.0000 840 LYS B CG  
6529 C CD  . LYS A 857 ? 0.9065 0.9065 0.9065 0.0000 0.0000 0.0000 840 LYS B CD  
6530 C CE  . LYS A 857 ? 0.9065 0.9065 0.9065 0.0000 0.0000 0.0000 840 LYS B CE  
6531 N NZ  . LYS A 857 ? 0.9065 0.9065 0.9065 0.0000 0.0000 0.0000 840 LYS B NZ  
6532 N N   . VAL A 858 ? 0.9078 0.9078 0.9078 0.0000 0.0000 0.0000 841 VAL B N   
6533 C CA  . VAL A 858 ? 0.9078 0.9078 0.9078 0.0000 0.0000 0.0000 841 VAL B CA  
6534 C C   . VAL A 858 ? 0.9078 0.9078 0.9078 0.0000 0.0000 0.0000 841 VAL B C   
6535 O O   . VAL A 858 ? 0.9078 0.9078 0.9078 0.0000 0.0000 0.0000 841 VAL B O   
6536 C CB  . VAL A 858 ? 0.9078 0.9078 0.9078 0.0000 0.0000 0.0000 841 VAL B CB  
6537 C CG1 . VAL A 858 ? 0.9078 0.9078 0.9078 0.0000 0.0000 0.0000 841 VAL B CG1 
6538 C CG2 . VAL A 858 ? 0.9078 0.9078 0.9078 0.0000 0.0000 0.0000 841 VAL B CG2 
6539 N N   . ASN A 859 ? 0.9213 0.9213 0.9213 0.0000 0.0000 0.0000 842 ASN B N   
6540 C CA  . ASN A 859 ? 0.9213 0.9213 0.9213 0.0000 0.0000 0.0000 842 ASN B CA  
6541 C C   . ASN A 859 ? 0.9213 0.9213 0.9213 0.0000 0.0000 0.0000 842 ASN B C   
6542 O O   . ASN A 859 ? 0.9213 0.9213 0.9213 0.0000 0.0000 0.0000 842 ASN B O   
6543 C CB  . ASN A 859 ? 0.9213 0.9213 0.9213 0.0000 0.0000 0.0000 842 ASN B CB  
6544 C CG  . ASN A 859 ? 0.9213 0.9213 0.9213 0.0000 0.0000 0.0000 842 ASN B CG  
6545 O OD1 . ASN A 859 ? 0.9213 0.9213 0.9213 0.0000 0.0000 0.0000 842 ASN B OD1 
6546 N ND2 . ASN A 859 ? 0.9213 0.9213 0.9213 0.0000 0.0000 0.0000 842 ASN B ND2 
6547 N N   . ASN A 860 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 843 ASN B N   
6548 C CA  . ASN A 860 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 843 ASN B CA  
6549 C C   . ASN A 860 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 843 ASN B C   
6550 O O   . ASN A 860 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 843 ASN B O   
6551 C CB  . ASN A 860 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 843 ASN B CB  
6552 C CG  . ASN A 860 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 843 ASN B CG  
6553 O OD1 . ASN A 860 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 843 ASN B OD1 
6554 N ND2 . ASN A 860 ? 0.9682 0.9682 0.9682 0.0000 0.0000 0.0000 843 ASN B ND2 
6555 N N   . THR A 861 ? 0.9402 0.9402 0.9402 0.0000 0.0000 0.0000 844 THR B N   
6556 C CA  . THR A 861 ? 0.9402 0.9402 0.9402 0.0000 0.0000 0.0000 844 THR B CA  
6557 C C   . THR A 861 ? 0.9402 0.9402 0.9402 0.0000 0.0000 0.0000 844 THR B C   
6558 O O   . THR A 861 ? 0.9402 0.9402 0.9402 0.0000 0.0000 0.0000 844 THR B O   
6559 C CB  . THR A 861 ? 0.9402 0.9402 0.9402 0.0000 0.0000 0.0000 844 THR B CB  
6560 O OG1 . THR A 861 ? 0.9402 0.9402 0.9402 0.0000 0.0000 0.0000 844 THR B OG1 
6561 C CG2 . THR A 861 ? 0.9402 0.9402 0.9402 0.0000 0.0000 0.0000 844 THR B CG2 
6562 N N   . LEU A 862 ? 0.9019 0.9019 0.9019 0.0000 0.0000 0.0000 845 LEU B N   
6563 C CA  . LEU A 862 ? 0.9019 0.9019 0.9019 0.0000 0.0000 0.0000 845 LEU B CA  
6564 C C   . LEU A 862 ? 0.9019 0.9019 0.9019 0.0000 0.0000 0.0000 845 LEU B C   
6565 O O   . LEU A 862 ? 0.9019 0.9019 0.9019 0.0000 0.0000 0.0000 845 LEU B O   
6566 C CB  . LEU A 862 ? 0.9019 0.9019 0.9019 0.0000 0.0000 0.0000 845 LEU B CB  
6567 C CG  . LEU A 862 ? 0.9019 0.9019 0.9019 0.0000 0.0000 0.0000 845 LEU B CG  
6568 C CD1 . LEU A 862 ? 0.9019 0.9019 0.9019 0.0000 0.0000 0.0000 845 LEU B CD1 
6569 C CD2 . LEU A 862 ? 0.9019 0.9019 0.9019 0.0000 0.0000 0.0000 845 LEU B CD2 
6570 N N   . SER A 863 ? 0.9796 0.9796 0.9796 0.0000 0.0000 0.0000 846 SER B N   
6571 C CA  . SER A 863 ? 0.9796 0.9796 0.9796 0.0000 0.0000 0.0000 846 SER B CA  
6572 C C   . SER A 863 ? 0.9796 0.9796 0.9796 0.0000 0.0000 0.0000 846 SER B C   
6573 O O   . SER A 863 ? 0.9796 0.9796 0.9796 0.0000 0.0000 0.0000 846 SER B O   
6574 C CB  . SER A 863 ? 0.9796 0.9796 0.9796 0.0000 0.0000 0.0000 846 SER B CB  
6575 O OG  . SER A 863 ? 0.9796 0.9796 0.9796 0.0000 0.0000 0.0000 846 SER B OG  
6576 N N   . THR A 864 ? 0.9658 0.9658 0.9658 0.0000 0.0000 0.0000 847 THR B N   
6577 C CA  . THR A 864 ? 0.9658 0.9658 0.9658 0.0000 0.0000 0.0000 847 THR B CA  
6578 C C   . THR A 864 ? 0.9658 0.9658 0.9658 0.0000 0.0000 0.0000 847 THR B C   
6579 O O   . THR A 864 ? 0.9658 0.9658 0.9658 0.0000 0.0000 0.0000 847 THR B O   
6580 C CB  . THR A 864 ? 0.9658 0.9658 0.9658 0.0000 0.0000 0.0000 847 THR B CB  
6581 O OG1 . THR A 864 ? 0.9658 0.9658 0.9658 0.0000 0.0000 0.0000 847 THR B OG1 
6582 C CG2 . THR A 864 ? 0.9658 0.9658 0.9658 0.0000 0.0000 0.0000 847 THR B CG2 
6583 N N   . ASP A 865 ? 0.9984 0.9984 0.9984 0.0000 0.0000 0.0000 848 ASP B N   
6584 C CA  . ASP A 865 ? 0.9984 0.9984 0.9984 0.0000 0.0000 0.0000 848 ASP B CA  
6585 C C   . ASP A 865 ? 0.9984 0.9984 0.9984 0.0000 0.0000 0.0000 848 ASP B C   
6586 O O   . ASP A 865 ? 0.9984 0.9984 0.9984 0.0000 0.0000 0.0000 848 ASP B O   
6587 C CB  . ASP A 865 ? 0.9984 0.9984 0.9984 0.0000 0.0000 0.0000 848 ASP B CB  
6588 C CG  . ASP A 865 ? 0.9984 0.9984 0.9984 0.0000 0.0000 0.0000 848 ASP B CG  
6589 O OD1 . ASP A 865 ? 0.9984 0.9984 0.9984 0.0000 0.0000 0.0000 848 ASP B OD1 
6590 O OD2 . ASP A 865 ? 0.9984 0.9984 0.9984 0.0000 0.0000 0.0000 848 ASP B OD2 
6591 N N   . ILE A 866 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 849 ILE B N   
6592 C CA  . ILE A 866 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 849 ILE B CA  
6593 C C   . ILE A 866 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 849 ILE B C   
6594 O O   . ILE A 866 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 849 ILE B O   
6595 C CB  . ILE A 866 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 849 ILE B CB  
6596 C CG1 . ILE A 866 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 849 ILE B CG1 
6597 C CG2 . ILE A 866 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 849 ILE B CG2 
6598 C CD1 . ILE A 866 ? 0.9367 0.9367 0.9367 0.0000 0.0000 0.0000 849 ILE B CD1 
6599 N N   . PRO A 867 ? 0.9654 0.9654 0.9654 0.0000 0.0000 0.0000 850 PRO B N   
6600 C CA  . PRO A 867 ? 0.9654 0.9654 0.9654 0.0000 0.0000 0.0000 850 PRO B CA  
6601 C C   . PRO A 867 ? 0.9654 0.9654 0.9654 0.0000 0.0000 0.0000 850 PRO B C   
6602 O O   . PRO A 867 ? 0.9654 0.9654 0.9654 0.0000 0.0000 0.0000 850 PRO B O   
6603 C CB  . PRO A 867 ? 0.9654 0.9654 0.9654 0.0000 0.0000 0.0000 850 PRO B CB  
6604 C CG  . PRO A 867 ? 0.9654 0.9654 0.9654 0.0000 0.0000 0.0000 850 PRO B CG  
6605 C CD  . PRO A 867 ? 0.9654 0.9654 0.9654 0.0000 0.0000 0.0000 850 PRO B CD  
6606 N N   . PHE A 868 ? 0.9419 0.9419 0.9419 0.0000 0.0000 0.0000 851 PHE B N   
6607 C CA  . PHE A 868 ? 0.9419 0.9419 0.9419 0.0000 0.0000 0.0000 851 PHE B CA  
6608 C C   . PHE A 868 ? 0.9419 0.9419 0.9419 0.0000 0.0000 0.0000 851 PHE B C   
6609 O O   . PHE A 868 ? 0.9419 0.9419 0.9419 0.0000 0.0000 0.0000 851 PHE B O   
6610 C CB  . PHE A 868 ? 0.9419 0.9419 0.9419 0.0000 0.0000 0.0000 851 PHE B CB  
6611 C CG  . PHE A 868 ? 0.9419 0.9419 0.9419 0.0000 0.0000 0.0000 851 PHE B CG  
6612 C CD1 . PHE A 868 ? 0.9419 0.9419 0.9419 0.0000 0.0000 0.0000 851 PHE B CD1 
6613 C CD2 . PHE A 868 ? 0.9419 0.9419 0.9419 0.0000 0.0000 0.0000 851 PHE B CD2 
6614 C CE1 . PHE A 868 ? 0.9419 0.9419 0.9419 0.0000 0.0000 0.0000 851 PHE B CE1 
6615 C CE2 . PHE A 868 ? 0.9419 0.9419 0.9419 0.0000 0.0000 0.0000 851 PHE B CE2 
6616 C CZ  . PHE A 868 ? 0.9419 0.9419 0.9419 0.0000 0.0000 0.0000 851 PHE B CZ  
6617 N N   . GLN A 869 ? 1.0142 1.0142 1.0142 0.0000 0.0000 0.0000 852 GLN B N   
6618 C CA  . GLN A 869 ? 1.0142 1.0142 1.0142 0.0000 0.0000 0.0000 852 GLN B CA  
6619 C C   . GLN A 869 ? 1.0142 1.0142 1.0142 0.0000 0.0000 0.0000 852 GLN B C   
6620 O O   . GLN A 869 ? 1.0142 1.0142 1.0142 0.0000 0.0000 0.0000 852 GLN B O   
6621 C CB  . GLN A 869 ? 1.0142 1.0142 1.0142 0.0000 0.0000 0.0000 852 GLN B CB  
6622 C CG  . GLN A 869 ? 1.0142 1.0142 1.0142 0.0000 0.0000 0.0000 852 GLN B CG  
6623 C CD  . GLN A 869 ? 1.0142 1.0142 1.0142 0.0000 0.0000 0.0000 852 GLN B CD  
6624 O OE1 . GLN A 869 ? 1.0142 1.0142 1.0142 0.0000 0.0000 0.0000 852 GLN B OE1 
6625 N NE2 . GLN A 869 ? 1.0142 1.0142 1.0142 0.0000 0.0000 0.0000 852 GLN B NE2 
6626 N N   . LEU A 870 ? 0.9821 0.9821 0.9821 0.0000 0.0000 0.0000 853 LEU B N   
6627 C CA  . LEU A 870 ? 0.9821 0.9821 0.9821 0.0000 0.0000 0.0000 853 LEU B CA  
6628 C C   . LEU A 870 ? 0.9821 0.9821 0.9821 0.0000 0.0000 0.0000 853 LEU B C   
6629 O O   . LEU A 870 ? 0.9821 0.9821 0.9821 0.0000 0.0000 0.0000 853 LEU B O   
6630 C CB  . LEU A 870 ? 0.9821 0.9821 0.9821 0.0000 0.0000 0.0000 853 LEU B CB  
6631 C CG  . LEU A 870 ? 0.9821 0.9821 0.9821 0.0000 0.0000 0.0000 853 LEU B CG  
6632 C CD1 . LEU A 870 ? 0.9821 0.9821 0.9821 0.0000 0.0000 0.0000 853 LEU B CD1 
6633 C CD2 . LEU A 870 ? 0.9821 0.9821 0.9821 0.0000 0.0000 0.0000 853 LEU B CD2 
6634 N N   . SER A 871 ? 1.0238 1.0238 1.0238 0.0000 0.0000 0.0000 854 SER B N   
6635 C CA  . SER A 871 ? 1.0238 1.0238 1.0238 0.0000 0.0000 0.0000 854 SER B CA  
6636 C C   . SER A 871 ? 1.0238 1.0238 1.0238 0.0000 0.0000 0.0000 854 SER B C   
6637 O O   . SER A 871 ? 1.0238 1.0238 1.0238 0.0000 0.0000 0.0000 854 SER B O   
6638 C CB  . SER A 871 ? 1.0238 1.0238 1.0238 0.0000 0.0000 0.0000 854 SER B CB  
6639 O OG  . SER A 871 ? 1.0238 1.0238 1.0238 0.0000 0.0000 0.0000 854 SER B OG  
6640 N N   . LYS A 872 ? 1.0278 1.0278 1.0278 0.0000 0.0000 0.0000 855 LYS B N   
6641 C CA  . LYS A 872 ? 1.0278 1.0278 1.0278 0.0000 0.0000 0.0000 855 LYS B CA  
6642 C C   . LYS A 872 ? 1.0278 1.0278 1.0278 0.0000 0.0000 0.0000 855 LYS B C   
6643 O O   . LYS A 872 ? 1.0278 1.0278 1.0278 0.0000 0.0000 0.0000 855 LYS B O   
6644 C CB  . LYS A 872 ? 1.0278 1.0278 1.0278 0.0000 0.0000 0.0000 855 LYS B CB  
6645 C CG  . LYS A 872 ? 1.0278 1.0278 1.0278 0.0000 0.0000 0.0000 855 LYS B CG  
6646 C CD  . LYS A 872 ? 1.0278 1.0278 1.0278 0.0000 0.0000 0.0000 855 LYS B CD  
6647 C CE  . LYS A 872 ? 1.0278 1.0278 1.0278 0.0000 0.0000 0.0000 855 LYS B CE  
6648 N NZ  . LYS A 872 ? 1.0278 1.0278 1.0278 0.0000 0.0000 0.0000 855 LYS B NZ  
6649 N N   . TYR A 873 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 856 TYR B N   
6650 C CA  . TYR A 873 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 856 TYR B CA  
6651 C C   . TYR A 873 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 856 TYR B C   
6652 O O   . TYR A 873 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 856 TYR B O   
6653 C CB  . TYR A 873 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 856 TYR B CB  
6654 C CG  . TYR A 873 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 856 TYR B CG  
6655 C CD1 . TYR A 873 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 856 TYR B CD1 
6656 C CD2 . TYR A 873 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 856 TYR B CD2 
6657 C CE1 . TYR A 873 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 856 TYR B CE1 
6658 C CE2 . TYR A 873 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 856 TYR B CE2 
6659 C CZ  . TYR A 873 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 856 TYR B CZ  
6660 O OH  . TYR A 873 ? 0.9687 0.9687 0.9687 0.0000 0.0000 0.0000 856 TYR B OH  
# 
