data_9B8A
# 
_entry.id   9B8A 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9B8A         pdb_00009b8a 10.2210/pdb9b8a/pdb 
WWPDB D_1000282857 ?            ?                   
EMDB  EMD-44336    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-19 ? 
2 'EM metadata'     1 0 2025-02-19 ? 
3 FSC               1 0 2025-02-19 ? 
4 'Half map'        1 0 2025-02-19 1 
5 'Half map'        1 0 2025-02-19 2 
6 Image             1 0 2025-02-19 ? 
7 'Primary map'     1 0 2025-02-19 ? 
8 'Structure model' 1 1 2025-05-21 ? 
9 'EM metadata'     1 1 2025-05-21 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 FSC               repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 Image             repository 'Initial release' ? ? 
7 7 'Primary map'     repository 'Initial release' ? ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 8 'Structure model' 'Data collection'      
2 9 'EM metadata'     'Data processing'      
3 9 'EM metadata'     'Experimental summary' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 8 'Structure model' em_admin    
2 8 'Structure model' em_software 
3 9 'EM metadata'     em_admin    
4 9 'EM metadata'     em_software 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 8 'Structure model' '_em_admin.last_update' 
2 8 'Structure model' '_em_software.name'     
3 9 'EM metadata'     '_em_admin.last_update' 
4 9 'EM metadata'     '_em_software.name'     
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9B8A 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Cryo-EM structure of E. coli cellulose synthase subunit C' 
_pdbx_database_related.db_id          EMD-44336 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jz3x@virginia.edu 
_pdbx_contact_author.name_first         Jochen 
_pdbx_contact_author.name_last          Zimmer 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8423-2882 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Verma, P.'  1 0000-0003-3972-0112 
'Zimmer, J.' 2 0000-0002-8423-2882 
# 
_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            15 
_citation.language                  ? 
_citation.page_first                7798 
_citation.page_last                 7798 
_citation.title                     
'Insights into phosphoethanolamine cellulose synthesis and secretion across the Gram-negative cell envelope.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-51838-0 
_citation.pdbx_database_id_PubMed   39242554 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Verma, P.'      1 0000-0003-3972-0112 
primary 'Ho, R.'         2 ?                   
primary 'Chambers, S.A.' 3 0000-0002-3557-830X 
primary 'Cegelski, L.'   4 0000-0002-0978-1814 
primary 'Zimmer, J.'     5 0000-0002-8423-2882 
# 
_entity.id                         1 
_entity.type                       polymer 
_entity.src_method                 man 
_entity.pdbx_description           'Cellulose synthase operon protein C' 
_entity.formula_weight             126827.016 
_entity.pdbx_number_of_molecules   1 
_entity.pdbx_ec                    ? 
_entity.pdbx_mutation              ? 
_entity.pdbx_fragment              ? 
_entity.details                    ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MHHHHHHHHVEAAPTAQQQLLEQVRLGEATHREDLVQQSLYRLELIDPNNPDVVAARFRSLLRQGDIDGAQKQLDRLSQL
APSSNAYKSSRTTMLLSTPDGRQALQQARLQATTGHAEEAVASYNKLFNGAPPEGDIAVEYWSTVAKIPARRGEAINQLK
RINADAPGNTGLQNNLALLLFSSDRRDEGFAVLEQMAKSNAGREGASKIWYGQIKDMPVSDASVSALKKYLSIFSDGDSV
AAAQSQLAEQQKQLADPAFRARAQGLAAVDSGMAGKAIPELQQAVRANPKDSEALGALGQAYSQKGDRANAVANLEKALA
LDPHSSNNDKWNSLLKVNRYWLAIQQGDAALKANNPDRAERLFQQARNVDNTDSYAVLGLGDVAMARKDYPAAERYYQQT
LRMDSGNTNAVRGLANIYRQQSPEKAEAFIASLSASQRRSIDDIERSLQNDRLAQQAEALENQGKWAQAAALQRQRLALD
PGSVWITYRLSQDLWQAGQRSQADTLMRNLAQQKSNDPEQVYAYGLYLSGHDQDRAALAHINSLPRAQWNSNIQELVNRL
QSDQVLETANRLRESGKEAEAEAMLRQQPPSTRIDLTLADWAQQRRDYTAARAAYQNVLTREPANADAILGLTEVDIAAG
DKAAARSQLAKLPATDNASLNTQRRVALAQAQLGDTAAAQRTFNKLIPQAKSQPPSMESAMVLRDGAKFEAQAGDPTQAL
ETYKDAMVASGVTTTRPQDNDTFTRLTRNDEKDDWLKRGVRSDAADLYRQQDLNVTLEHDYWGSSGTGGYSDLKAHTTML
QVDAPYSDGRMFFRSDFVNMNVGSFSTNADGKWDDNWGTCTLQDCSGNRSQSDSGASVAVGWRNDVWSWDIGTTPMGFNV
VDVVGGISYSDDIGPLGYTVNAHRRPISSSLLAFGGQKDSPSNTGKKWGGVRADGVGLSLSYDKGEANGVWASLSGDQLT
GKNVEDNWRVRWMTGYYYKVINQNNRRVTIGLNNMIWHYDKDLSGYSLGQGGYYSPQEYLSFAIPVMWRERTENWSWELG
ASGSWSHSRTKTMPRYPLMNLIPTDWQEEAARQSNDGGSSQGFGYTARALLERRVTSNWFVGTAIDIQQAKDYAPSHFLL
YVRYSAAGWQGDMDLPPQPLIPYADW
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHHHVEAAPTAQQQLLEQVRLGEATHREDLVQQSLYRLELIDPNNPDVVAARFRSLLRQGDIDGAQKQLDRLSQL
APSSNAYKSSRTTMLLSTPDGRQALQQARLQATTGHAEEAVASYNKLFNGAPPEGDIAVEYWSTVAKIPARRGEAINQLK
RINADAPGNTGLQNNLALLLFSSDRRDEGFAVLEQMAKSNAGREGASKIWYGQIKDMPVSDASVSALKKYLSIFSDGDSV
AAAQSQLAEQQKQLADPAFRARAQGLAAVDSGMAGKAIPELQQAVRANPKDSEALGALGQAYSQKGDRANAVANLEKALA
LDPHSSNNDKWNSLLKVNRYWLAIQQGDAALKANNPDRAERLFQQARNVDNTDSYAVLGLGDVAMARKDYPAAERYYQQT
LRMDSGNTNAVRGLANIYRQQSPEKAEAFIASLSASQRRSIDDIERSLQNDRLAQQAEALENQGKWAQAAALQRQRLALD
PGSVWITYRLSQDLWQAGQRSQADTLMRNLAQQKSNDPEQVYAYGLYLSGHDQDRAALAHINSLPRAQWNSNIQELVNRL
QSDQVLETANRLRESGKEAEAEAMLRQQPPSTRIDLTLADWAQQRRDYTAARAAYQNVLTREPANADAILGLTEVDIAAG
DKAAARSQLAKLPATDNASLNTQRRVALAQAQLGDTAAAQRTFNKLIPQAKSQPPSMESAMVLRDGAKFEAQAGDPTQAL
ETYKDAMVASGVTTTRPQDNDTFTRLTRNDEKDDWLKRGVRSDAADLYRQQDLNVTLEHDYWGSSGTGGYSDLKAHTTML
QVDAPYSDGRMFFRSDFVNMNVGSFSTNADGKWDDNWGTCTLQDCSGNRSQSDSGASVAVGWRNDVWSWDIGTTPMGFNV
VDVVGGISYSDDIGPLGYTVNAHRRPISSSLLAFGGQKDSPSNTGKKWGGVRADGVGLSLSYDKGEANGVWASLSGDQLT
GKNVEDNWRVRWMTGYYYKVINQNNRRVTIGLNNMIWHYDKDLSGYSLGQGGYYSPQEYLSFAIPVMWRERTENWSWELG
ASGSWSHSRTKTMPRYPLMNLIPTDWQEEAARQSNDGGSSQGFGYTARALLERRVTSNWFVGTAIDIQQAKDYAPSHFLL
YVRYSAAGWQGDMDLPPQPLIPYADW
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
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    HIS n 
1 3    HIS n 
1 4    HIS n 
1 5    HIS n 
1 6    HIS n 
1 7    HIS n 
1 8    HIS n 
1 9    HIS n 
1 10   VAL n 
1 11   GLU n 
1 12   ALA n 
1 13   ALA n 
1 14   PRO n 
1 15   THR n 
1 16   ALA n 
1 17   GLN n 
1 18   GLN n 
1 19   GLN n 
1 20   LEU n 
1 21   LEU n 
1 22   GLU n 
1 23   GLN n 
1 24   VAL n 
1 25   ARG n 
1 26   LEU n 
1 27   GLY n 
1 28   GLU n 
1 29   ALA n 
1 30   THR n 
1 31   HIS n 
1 32   ARG n 
1 33   GLU n 
1 34   ASP n 
1 35   LEU n 
1 36   VAL n 
1 37   GLN n 
1 38   GLN n 
1 39   SER n 
1 40   LEU n 
1 41   TYR n 
1 42   ARG n 
1 43   LEU n 
1 44   GLU n 
1 45   LEU n 
1 46   ILE n 
1 47   ASP n 
1 48   PRO n 
1 49   ASN n 
1 50   ASN n 
1 51   PRO n 
1 52   ASP n 
1 53   VAL n 
1 54   VAL n 
1 55   ALA n 
1 56   ALA n 
1 57   ARG n 
1 58   PHE n 
1 59   ARG n 
1 60   SER n 
1 61   LEU n 
1 62   LEU n 
1 63   ARG n 
1 64   GLN n 
1 65   GLY n 
1 66   ASP n 
1 67   ILE n 
1 68   ASP n 
1 69   GLY n 
1 70   ALA n 
1 71   GLN n 
1 72   LYS n 
1 73   GLN n 
1 74   LEU n 
1 75   ASP n 
1 76   ARG n 
1 77   LEU n 
1 78   SER n 
1 79   GLN n 
1 80   LEU n 
1 81   ALA n 
1 82   PRO n 
1 83   SER n 
1 84   SER n 
1 85   ASN n 
1 86   ALA n 
1 87   TYR n 
1 88   LYS n 
1 89   SER n 
1 90   SER n 
1 91   ARG n 
1 92   THR n 
1 93   THR n 
1 94   MET n 
1 95   LEU n 
1 96   LEU n 
1 97   SER n 
1 98   THR n 
1 99   PRO n 
1 100  ASP n 
1 101  GLY n 
1 102  ARG n 
1 103  GLN n 
1 104  ALA n 
1 105  LEU n 
1 106  GLN n 
1 107  GLN n 
1 108  ALA n 
1 109  ARG n 
1 110  LEU n 
1 111  GLN n 
1 112  ALA n 
1 113  THR n 
1 114  THR n 
1 115  GLY n 
1 116  HIS n 
1 117  ALA n 
1 118  GLU n 
1 119  GLU n 
1 120  ALA n 
1 121  VAL n 
1 122  ALA n 
1 123  SER n 
1 124  TYR n 
1 125  ASN n 
1 126  LYS n 
1 127  LEU n 
1 128  PHE n 
1 129  ASN n 
1 130  GLY n 
1 131  ALA n 
1 132  PRO n 
1 133  PRO n 
1 134  GLU n 
1 135  GLY n 
1 136  ASP n 
1 137  ILE n 
1 138  ALA n 
1 139  VAL n 
1 140  GLU n 
1 141  TYR n 
1 142  TRP n 
1 143  SER n 
1 144  THR n 
1 145  VAL n 
1 146  ALA n 
1 147  LYS n 
1 148  ILE n 
1 149  PRO n 
1 150  ALA n 
1 151  ARG n 
1 152  ARG n 
1 153  GLY n 
1 154  GLU n 
1 155  ALA n 
1 156  ILE n 
1 157  ASN n 
1 158  GLN n 
1 159  LEU n 
1 160  LYS n 
1 161  ARG n 
1 162  ILE n 
1 163  ASN n 
1 164  ALA n 
1 165  ASP n 
1 166  ALA n 
1 167  PRO n 
1 168  GLY n 
1 169  ASN n 
1 170  THR n 
1 171  GLY n 
1 172  LEU n 
1 173  GLN n 
1 174  ASN n 
1 175  ASN n 
1 176  LEU n 
1 177  ALA n 
1 178  LEU n 
1 179  LEU n 
1 180  LEU n 
1 181  PHE n 
1 182  SER n 
1 183  SER n 
1 184  ASP n 
1 185  ARG n 
1 186  ARG n 
1 187  ASP n 
1 188  GLU n 
1 189  GLY n 
1 190  PHE n 
1 191  ALA n 
1 192  VAL n 
1 193  LEU n 
1 194  GLU n 
1 195  GLN n 
1 196  MET n 
1 197  ALA n 
1 198  LYS n 
1 199  SER n 
1 200  ASN n 
1 201  ALA n 
1 202  GLY n 
1 203  ARG n 
1 204  GLU n 
1 205  GLY n 
1 206  ALA n 
1 207  SER n 
1 208  LYS n 
1 209  ILE n 
1 210  TRP n 
1 211  TYR n 
1 212  GLY n 
1 213  GLN n 
1 214  ILE n 
1 215  LYS n 
1 216  ASP n 
1 217  MET n 
1 218  PRO n 
1 219  VAL n 
1 220  SER n 
1 221  ASP n 
1 222  ALA n 
1 223  SER n 
1 224  VAL n 
1 225  SER n 
1 226  ALA n 
1 227  LEU n 
1 228  LYS n 
1 229  LYS n 
1 230  TYR n 
1 231  LEU n 
1 232  SER n 
1 233  ILE n 
1 234  PHE n 
1 235  SER n 
1 236  ASP n 
1 237  GLY n 
1 238  ASP n 
1 239  SER n 
1 240  VAL n 
1 241  ALA n 
1 242  ALA n 
1 243  ALA n 
1 244  GLN n 
1 245  SER n 
1 246  GLN n 
1 247  LEU n 
1 248  ALA n 
1 249  GLU n 
1 250  GLN n 
1 251  GLN n 
1 252  LYS n 
1 253  GLN n 
1 254  LEU n 
1 255  ALA n 
1 256  ASP n 
1 257  PRO n 
1 258  ALA n 
1 259  PHE n 
1 260  ARG n 
1 261  ALA n 
1 262  ARG n 
1 263  ALA n 
1 264  GLN n 
1 265  GLY n 
1 266  LEU n 
1 267  ALA n 
1 268  ALA n 
1 269  VAL n 
1 270  ASP n 
1 271  SER n 
1 272  GLY n 
1 273  MET n 
1 274  ALA n 
1 275  GLY n 
1 276  LYS n 
1 277  ALA n 
1 278  ILE n 
1 279  PRO n 
1 280  GLU n 
1 281  LEU n 
1 282  GLN n 
1 283  GLN n 
1 284  ALA n 
1 285  VAL n 
1 286  ARG n 
1 287  ALA n 
1 288  ASN n 
1 289  PRO n 
1 290  LYS n 
1 291  ASP n 
1 292  SER n 
1 293  GLU n 
1 294  ALA n 
1 295  LEU n 
1 296  GLY n 
1 297  ALA n 
1 298  LEU n 
1 299  GLY n 
1 300  GLN n 
1 301  ALA n 
1 302  TYR n 
1 303  SER n 
1 304  GLN n 
1 305  LYS n 
1 306  GLY n 
1 307  ASP n 
1 308  ARG n 
1 309  ALA n 
1 310  ASN n 
1 311  ALA n 
1 312  VAL n 
1 313  ALA n 
1 314  ASN n 
1 315  LEU n 
1 316  GLU n 
1 317  LYS n 
1 318  ALA n 
1 319  LEU n 
1 320  ALA n 
1 321  LEU n 
1 322  ASP n 
1 323  PRO n 
1 324  HIS n 
1 325  SER n 
1 326  SER n 
1 327  ASN n 
1 328  ASN n 
1 329  ASP n 
1 330  LYS n 
1 331  TRP n 
1 332  ASN n 
1 333  SER n 
1 334  LEU n 
1 335  LEU n 
1 336  LYS n 
1 337  VAL n 
1 338  ASN n 
1 339  ARG n 
1 340  TYR n 
1 341  TRP n 
1 342  LEU n 
1 343  ALA n 
1 344  ILE n 
1 345  GLN n 
1 346  GLN n 
1 347  GLY n 
1 348  ASP n 
1 349  ALA n 
1 350  ALA n 
1 351  LEU n 
1 352  LYS n 
1 353  ALA n 
1 354  ASN n 
1 355  ASN n 
1 356  PRO n 
1 357  ASP n 
1 358  ARG n 
1 359  ALA n 
1 360  GLU n 
1 361  ARG n 
1 362  LEU n 
1 363  PHE n 
1 364  GLN n 
1 365  GLN n 
1 366  ALA n 
1 367  ARG n 
1 368  ASN n 
1 369  VAL n 
1 370  ASP n 
1 371  ASN n 
1 372  THR n 
1 373  ASP n 
1 374  SER n 
1 375  TYR n 
1 376  ALA n 
1 377  VAL n 
1 378  LEU n 
1 379  GLY n 
1 380  LEU n 
1 381  GLY n 
1 382  ASP n 
1 383  VAL n 
1 384  ALA n 
1 385  MET n 
1 386  ALA n 
1 387  ARG n 
1 388  LYS n 
1 389  ASP n 
1 390  TYR n 
1 391  PRO n 
1 392  ALA n 
1 393  ALA n 
1 394  GLU n 
1 395  ARG n 
1 396  TYR n 
1 397  TYR n 
1 398  GLN n 
1 399  GLN n 
1 400  THR n 
1 401  LEU n 
1 402  ARG n 
1 403  MET n 
1 404  ASP n 
1 405  SER n 
1 406  GLY n 
1 407  ASN n 
1 408  THR n 
1 409  ASN n 
1 410  ALA n 
1 411  VAL n 
1 412  ARG n 
1 413  GLY n 
1 414  LEU n 
1 415  ALA n 
1 416  ASN n 
1 417  ILE n 
1 418  TYR n 
1 419  ARG n 
1 420  GLN n 
1 421  GLN n 
1 422  SER n 
1 423  PRO n 
1 424  GLU n 
1 425  LYS n 
1 426  ALA n 
1 427  GLU n 
1 428  ALA n 
1 429  PHE n 
1 430  ILE n 
1 431  ALA n 
1 432  SER n 
1 433  LEU n 
1 434  SER n 
1 435  ALA n 
1 436  SER n 
1 437  GLN n 
1 438  ARG n 
1 439  ARG n 
1 440  SER n 
1 441  ILE n 
1 442  ASP n 
1 443  ASP n 
1 444  ILE n 
1 445  GLU n 
1 446  ARG n 
1 447  SER n 
1 448  LEU n 
1 449  GLN n 
1 450  ASN n 
1 451  ASP n 
1 452  ARG n 
1 453  LEU n 
1 454  ALA n 
1 455  GLN n 
1 456  GLN n 
1 457  ALA n 
1 458  GLU n 
1 459  ALA n 
1 460  LEU n 
1 461  GLU n 
1 462  ASN n 
1 463  GLN n 
1 464  GLY n 
1 465  LYS n 
1 466  TRP n 
1 467  ALA n 
1 468  GLN n 
1 469  ALA n 
1 470  ALA n 
1 471  ALA n 
1 472  LEU n 
1 473  GLN n 
1 474  ARG n 
1 475  GLN n 
1 476  ARG n 
1 477  LEU n 
1 478  ALA n 
1 479  LEU n 
1 480  ASP n 
1 481  PRO n 
1 482  GLY n 
1 483  SER n 
1 484  VAL n 
1 485  TRP n 
1 486  ILE n 
1 487  THR n 
1 488  TYR n 
1 489  ARG n 
1 490  LEU n 
1 491  SER n 
1 492  GLN n 
1 493  ASP n 
1 494  LEU n 
1 495  TRP n 
1 496  GLN n 
1 497  ALA n 
1 498  GLY n 
1 499  GLN n 
1 500  ARG n 
1 501  SER n 
1 502  GLN n 
1 503  ALA n 
1 504  ASP n 
1 505  THR n 
1 506  LEU n 
1 507  MET n 
1 508  ARG n 
1 509  ASN n 
1 510  LEU n 
1 511  ALA n 
1 512  GLN n 
1 513  GLN n 
1 514  LYS n 
1 515  SER n 
1 516  ASN n 
1 517  ASP n 
1 518  PRO n 
1 519  GLU n 
1 520  GLN n 
1 521  VAL n 
1 522  TYR n 
1 523  ALA n 
1 524  TYR n 
1 525  GLY n 
1 526  LEU n 
1 527  TYR n 
1 528  LEU n 
1 529  SER n 
1 530  GLY n 
1 531  HIS n 
1 532  ASP n 
1 533  GLN n 
1 534  ASP n 
1 535  ARG n 
1 536  ALA n 
1 537  ALA n 
1 538  LEU n 
1 539  ALA n 
1 540  HIS n 
1 541  ILE n 
1 542  ASN n 
1 543  SER n 
1 544  LEU n 
1 545  PRO n 
1 546  ARG n 
1 547  ALA n 
1 548  GLN n 
1 549  TRP n 
1 550  ASN n 
1 551  SER n 
1 552  ASN n 
1 553  ILE n 
1 554  GLN n 
1 555  GLU n 
1 556  LEU n 
1 557  VAL n 
1 558  ASN n 
1 559  ARG n 
1 560  LEU n 
1 561  GLN n 
1 562  SER n 
1 563  ASP n 
1 564  GLN n 
1 565  VAL n 
1 566  LEU n 
1 567  GLU n 
1 568  THR n 
1 569  ALA n 
1 570  ASN n 
1 571  ARG n 
1 572  LEU n 
1 573  ARG n 
1 574  GLU n 
1 575  SER n 
1 576  GLY n 
1 577  LYS n 
1 578  GLU n 
1 579  ALA n 
1 580  GLU n 
1 581  ALA n 
1 582  GLU n 
1 583  ALA n 
1 584  MET n 
1 585  LEU n 
1 586  ARG n 
1 587  GLN n 
1 588  GLN n 
1 589  PRO n 
1 590  PRO n 
1 591  SER n 
1 592  THR n 
1 593  ARG n 
1 594  ILE n 
1 595  ASP n 
1 596  LEU n 
1 597  THR n 
1 598  LEU n 
1 599  ALA n 
1 600  ASP n 
1 601  TRP n 
1 602  ALA n 
1 603  GLN n 
1 604  GLN n 
1 605  ARG n 
1 606  ARG n 
1 607  ASP n 
1 608  TYR n 
1 609  THR n 
1 610  ALA n 
1 611  ALA n 
1 612  ARG n 
1 613  ALA n 
1 614  ALA n 
1 615  TYR n 
1 616  GLN n 
1 617  ASN n 
1 618  VAL n 
1 619  LEU n 
1 620  THR n 
1 621  ARG n 
1 622  GLU n 
1 623  PRO n 
1 624  ALA n 
1 625  ASN n 
1 626  ALA n 
1 627  ASP n 
1 628  ALA n 
1 629  ILE n 
1 630  LEU n 
1 631  GLY n 
1 632  LEU n 
1 633  THR n 
1 634  GLU n 
1 635  VAL n 
1 636  ASP n 
1 637  ILE n 
1 638  ALA n 
1 639  ALA n 
1 640  GLY n 
1 641  ASP n 
1 642  LYS n 
1 643  ALA n 
1 644  ALA n 
1 645  ALA n 
1 646  ARG n 
1 647  SER n 
1 648  GLN n 
1 649  LEU n 
1 650  ALA n 
1 651  LYS n 
1 652  LEU n 
1 653  PRO n 
1 654  ALA n 
1 655  THR n 
1 656  ASP n 
1 657  ASN n 
1 658  ALA n 
1 659  SER n 
1 660  LEU n 
1 661  ASN n 
1 662  THR n 
1 663  GLN n 
1 664  ARG n 
1 665  ARG n 
1 666  VAL n 
1 667  ALA n 
1 668  LEU n 
1 669  ALA n 
1 670  GLN n 
1 671  ALA n 
1 672  GLN n 
1 673  LEU n 
1 674  GLY n 
1 675  ASP n 
1 676  THR n 
1 677  ALA n 
1 678  ALA n 
1 679  ALA n 
1 680  GLN n 
1 681  ARG n 
1 682  THR n 
1 683  PHE n 
1 684  ASN n 
1 685  LYS n 
1 686  LEU n 
1 687  ILE n 
1 688  PRO n 
1 689  GLN n 
1 690  ALA n 
1 691  LYS n 
1 692  SER n 
1 693  GLN n 
1 694  PRO n 
1 695  PRO n 
1 696  SER n 
1 697  MET n 
1 698  GLU n 
1 699  SER n 
1 700  ALA n 
1 701  MET n 
1 702  VAL n 
1 703  LEU n 
1 704  ARG n 
1 705  ASP n 
1 706  GLY n 
1 707  ALA n 
1 708  LYS n 
1 709  PHE n 
1 710  GLU n 
1 711  ALA n 
1 712  GLN n 
1 713  ALA n 
1 714  GLY n 
1 715  ASP n 
1 716  PRO n 
1 717  THR n 
1 718  GLN n 
1 719  ALA n 
1 720  LEU n 
1 721  GLU n 
1 722  THR n 
1 723  TYR n 
1 724  LYS n 
1 725  ASP n 
1 726  ALA n 
1 727  MET n 
1 728  VAL n 
1 729  ALA n 
1 730  SER n 
1 731  GLY n 
1 732  VAL n 
1 733  THR n 
1 734  THR n 
1 735  THR n 
1 736  ARG n 
1 737  PRO n 
1 738  GLN n 
1 739  ASP n 
1 740  ASN n 
1 741  ASP n 
1 742  THR n 
1 743  PHE n 
1 744  THR n 
1 745  ARG n 
1 746  LEU n 
1 747  THR n 
1 748  ARG n 
1 749  ASN n 
1 750  ASP n 
1 751  GLU n 
1 752  LYS n 
1 753  ASP n 
1 754  ASP n 
1 755  TRP n 
1 756  LEU n 
1 757  LYS n 
1 758  ARG n 
1 759  GLY n 
1 760  VAL n 
1 761  ARG n 
1 762  SER n 
1 763  ASP n 
1 764  ALA n 
1 765  ALA n 
1 766  ASP n 
1 767  LEU n 
1 768  TYR n 
1 769  ARG n 
1 770  GLN n 
1 771  GLN n 
1 772  ASP n 
1 773  LEU n 
1 774  ASN n 
1 775  VAL n 
1 776  THR n 
1 777  LEU n 
1 778  GLU n 
1 779  HIS n 
1 780  ASP n 
1 781  TYR n 
1 782  TRP n 
1 783  GLY n 
1 784  SER n 
1 785  SER n 
1 786  GLY n 
1 787  THR n 
1 788  GLY n 
1 789  GLY n 
1 790  TYR n 
1 791  SER n 
1 792  ASP n 
1 793  LEU n 
1 794  LYS n 
1 795  ALA n 
1 796  HIS n 
1 797  THR n 
1 798  THR n 
1 799  MET n 
1 800  LEU n 
1 801  GLN n 
1 802  VAL n 
1 803  ASP n 
1 804  ALA n 
1 805  PRO n 
1 806  TYR n 
1 807  SER n 
1 808  ASP n 
1 809  GLY n 
1 810  ARG n 
1 811  MET n 
1 812  PHE n 
1 813  PHE n 
1 814  ARG n 
1 815  SER n 
1 816  ASP n 
1 817  PHE n 
1 818  VAL n 
1 819  ASN n 
1 820  MET n 
1 821  ASN n 
1 822  VAL n 
1 823  GLY n 
1 824  SER n 
1 825  PHE n 
1 826  SER n 
1 827  THR n 
1 828  ASN n 
1 829  ALA n 
1 830  ASP n 
1 831  GLY n 
1 832  LYS n 
1 833  TRP n 
1 834  ASP n 
1 835  ASP n 
1 836  ASN n 
1 837  TRP n 
1 838  GLY n 
1 839  THR n 
1 840  CYS n 
1 841  THR n 
1 842  LEU n 
1 843  GLN n 
1 844  ASP n 
1 845  CYS n 
1 846  SER n 
1 847  GLY n 
1 848  ASN n 
1 849  ARG n 
1 850  SER n 
1 851  GLN n 
1 852  SER n 
1 853  ASP n 
1 854  SER n 
1 855  GLY n 
1 856  ALA n 
1 857  SER n 
1 858  VAL n 
1 859  ALA n 
1 860  VAL n 
1 861  GLY n 
1 862  TRP n 
1 863  ARG n 
1 864  ASN n 
1 865  ASP n 
1 866  VAL n 
1 867  TRP n 
1 868  SER n 
1 869  TRP n 
1 870  ASP n 
1 871  ILE n 
1 872  GLY n 
1 873  THR n 
1 874  THR n 
1 875  PRO n 
1 876  MET n 
1 877  GLY n 
1 878  PHE n 
1 879  ASN n 
1 880  VAL n 
1 881  VAL n 
1 882  ASP n 
1 883  VAL n 
1 884  VAL n 
1 885  GLY n 
1 886  GLY n 
1 887  ILE n 
1 888  SER n 
1 889  TYR n 
1 890  SER n 
1 891  ASP n 
1 892  ASP n 
1 893  ILE n 
1 894  GLY n 
1 895  PRO n 
1 896  LEU n 
1 897  GLY n 
1 898  TYR n 
1 899  THR n 
1 900  VAL n 
1 901  ASN n 
1 902  ALA n 
1 903  HIS n 
1 904  ARG n 
1 905  ARG n 
1 906  PRO n 
1 907  ILE n 
1 908  SER n 
1 909  SER n 
1 910  SER n 
1 911  LEU n 
1 912  LEU n 
1 913  ALA n 
1 914  PHE n 
1 915  GLY n 
1 916  GLY n 
1 917  GLN n 
1 918  LYS n 
1 919  ASP n 
1 920  SER n 
1 921  PRO n 
1 922  SER n 
1 923  ASN n 
1 924  THR n 
1 925  GLY n 
1 926  LYS n 
1 927  LYS n 
1 928  TRP n 
1 929  GLY n 
1 930  GLY n 
1 931  VAL n 
1 932  ARG n 
1 933  ALA n 
1 934  ASP n 
1 935  GLY n 
1 936  VAL n 
1 937  GLY n 
1 938  LEU n 
1 939  SER n 
1 940  LEU n 
1 941  SER n 
1 942  TYR n 
1 943  ASP n 
1 944  LYS n 
1 945  GLY n 
1 946  GLU n 
1 947  ALA n 
1 948  ASN n 
1 949  GLY n 
1 950  VAL n 
1 951  TRP n 
1 952  ALA n 
1 953  SER n 
1 954  LEU n 
1 955  SER n 
1 956  GLY n 
1 957  ASP n 
1 958  GLN n 
1 959  LEU n 
1 960  THR n 
1 961  GLY n 
1 962  LYS n 
1 963  ASN n 
1 964  VAL n 
1 965  GLU n 
1 966  ASP n 
1 967  ASN n 
1 968  TRP n 
1 969  ARG n 
1 970  VAL n 
1 971  ARG n 
1 972  TRP n 
1 973  MET n 
1 974  THR n 
1 975  GLY n 
1 976  TYR n 
1 977  TYR n 
1 978  TYR n 
1 979  LYS n 
1 980  VAL n 
1 981  ILE n 
1 982  ASN n 
1 983  GLN n 
1 984  ASN n 
1 985  ASN n 
1 986  ARG n 
1 987  ARG n 
1 988  VAL n 
1 989  THR n 
1 990  ILE n 
1 991  GLY n 
1 992  LEU n 
1 993  ASN n 
1 994  ASN n 
1 995  MET n 
1 996  ILE n 
1 997  TRP n 
1 998  HIS n 
1 999  TYR n 
1 1000 ASP n 
1 1001 LYS n 
1 1002 ASP n 
1 1003 LEU n 
1 1004 SER n 
1 1005 GLY n 
1 1006 TYR n 
1 1007 SER n 
1 1008 LEU n 
1 1009 GLY n 
1 1010 GLN n 
1 1011 GLY n 
1 1012 GLY n 
1 1013 TYR n 
1 1014 TYR n 
1 1015 SER n 
1 1016 PRO n 
1 1017 GLN n 
1 1018 GLU n 
1 1019 TYR n 
1 1020 LEU n 
1 1021 SER n 
1 1022 PHE n 
1 1023 ALA n 
1 1024 ILE n 
1 1025 PRO n 
1 1026 VAL n 
1 1027 MET n 
1 1028 TRP n 
1 1029 ARG n 
1 1030 GLU n 
1 1031 ARG n 
1 1032 THR n 
1 1033 GLU n 
1 1034 ASN n 
1 1035 TRP n 
1 1036 SER n 
1 1037 TRP n 
1 1038 GLU n 
1 1039 LEU n 
1 1040 GLY n 
1 1041 ALA n 
1 1042 SER n 
1 1043 GLY n 
1 1044 SER n 
1 1045 TRP n 
1 1046 SER n 
1 1047 HIS n 
1 1048 SER n 
1 1049 ARG n 
1 1050 THR n 
1 1051 LYS n 
1 1052 THR n 
1 1053 MET n 
1 1054 PRO n 
1 1055 ARG n 
1 1056 TYR n 
1 1057 PRO n 
1 1058 LEU n 
1 1059 MET n 
1 1060 ASN n 
1 1061 LEU n 
1 1062 ILE n 
1 1063 PRO n 
1 1064 THR n 
1 1065 ASP n 
1 1066 TRP n 
1 1067 GLN n 
1 1068 GLU n 
1 1069 GLU n 
1 1070 ALA n 
1 1071 ALA n 
1 1072 ARG n 
1 1073 GLN n 
1 1074 SER n 
1 1075 ASN n 
1 1076 ASP n 
1 1077 GLY n 
1 1078 GLY n 
1 1079 SER n 
1 1080 SER n 
1 1081 GLN n 
1 1082 GLY n 
1 1083 PHE n 
1 1084 GLY n 
1 1085 TYR n 
1 1086 THR n 
1 1087 ALA n 
1 1088 ARG n 
1 1089 ALA n 
1 1090 LEU n 
1 1091 LEU n 
1 1092 GLU n 
1 1093 ARG n 
1 1094 ARG n 
1 1095 VAL n 
1 1096 THR n 
1 1097 SER n 
1 1098 ASN n 
1 1099 TRP n 
1 1100 PHE n 
1 1101 VAL n 
1 1102 GLY n 
1 1103 THR n 
1 1104 ALA n 
1 1105 ILE n 
1 1106 ASP n 
1 1107 ILE n 
1 1108 GLN n 
1 1109 GLN n 
1 1110 ALA n 
1 1111 LYS n 
1 1112 ASP n 
1 1113 TYR n 
1 1114 ALA n 
1 1115 PRO n 
1 1116 SER n 
1 1117 HIS n 
1 1118 PHE n 
1 1119 LEU n 
1 1120 LEU n 
1 1121 TYR n 
1 1122 VAL n 
1 1123 ARG n 
1 1124 TYR n 
1 1125 SER n 
1 1126 ALA n 
1 1127 ALA n 
1 1128 GLY n 
1 1129 TRP n 
1 1130 GLN n 
1 1131 GLY n 
1 1132 ASP n 
1 1133 MET n 
1 1134 ASP n 
1 1135 LEU n 
1 1136 PRO n 
1 1137 PRO n 
1 1138 GLN n 
1 1139 PRO n 
1 1140 LEU n 
1 1141 ILE n 
1 1142 PRO n 
1 1143 TYR n 
1 1144 ALA n 
1 1145 ASP n 
1 1146 TRP n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   1146 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'bcsC, yhjL, b3530, JW5942' 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     562 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    12   ?    ?   ?   A . n 
A 1 2    HIS 2    13   ?    ?   ?   A . n 
A 1 3    HIS 3    14   ?    ?   ?   A . n 
A 1 4    HIS 4    15   ?    ?   ?   A . n 
A 1 5    HIS 5    16   ?    ?   ?   A . n 
A 1 6    HIS 6    17   ?    ?   ?   A . n 
A 1 7    HIS 7    18   ?    ?   ?   A . n 
A 1 8    HIS 8    19   ?    ?   ?   A . n 
A 1 9    HIS 9    20   ?    ?   ?   A . n 
A 1 10   VAL 10   21   ?    ?   ?   A . n 
A 1 11   GLU 11   22   ?    ?   ?   A . n 
A 1 12   ALA 12   23   ?    ?   ?   A . n 
A 1 13   ALA 13   24   ?    ?   ?   A . n 
A 1 14   PRO 14   25   ?    ?   ?   A . n 
A 1 15   THR 15   26   ?    ?   ?   A . n 
A 1 16   ALA 16   27   ?    ?   ?   A . n 
A 1 17   GLN 17   28   ?    ?   ?   A . n 
A 1 18   GLN 18   29   ?    ?   ?   A . n 
A 1 19   GLN 19   30   ?    ?   ?   A . n 
A 1 20   LEU 20   31   ?    ?   ?   A . n 
A 1 21   LEU 21   32   ?    ?   ?   A . n 
A 1 22   GLU 22   33   ?    ?   ?   A . n 
A 1 23   GLN 23   34   ?    ?   ?   A . n 
A 1 24   VAL 24   35   ?    ?   ?   A . n 
A 1 25   ARG 25   36   ?    ?   ?   A . n 
A 1 26   LEU 26   37   ?    ?   ?   A . n 
A 1 27   GLY 27   38   ?    ?   ?   A . n 
A 1 28   GLU 28   39   ?    ?   ?   A . n 
A 1 29   ALA 29   40   ?    ?   ?   A . n 
A 1 30   THR 30   41   ?    ?   ?   A . n 
A 1 31   HIS 31   42   ?    ?   ?   A . n 
A 1 32   ARG 32   43   ?    ?   ?   A . n 
A 1 33   GLU 33   44   ?    ?   ?   A . n 
A 1 34   ASP 34   45   ?    ?   ?   A . n 
A 1 35   LEU 35   46   ?    ?   ?   A . n 
A 1 36   VAL 36   47   ?    ?   ?   A . n 
A 1 37   GLN 37   48   ?    ?   ?   A . n 
A 1 38   GLN 38   49   ?    ?   ?   A . n 
A 1 39   SER 39   50   ?    ?   ?   A . n 
A 1 40   LEU 40   51   ?    ?   ?   A . n 
A 1 41   TYR 41   52   ?    ?   ?   A . n 
A 1 42   ARG 42   53   ?    ?   ?   A . n 
A 1 43   LEU 43   54   ?    ?   ?   A . n 
A 1 44   GLU 44   55   ?    ?   ?   A . n 
A 1 45   LEU 45   56   ?    ?   ?   A . n 
A 1 46   ILE 46   57   ?    ?   ?   A . n 
A 1 47   ASP 47   58   ?    ?   ?   A . n 
A 1 48   PRO 48   59   ?    ?   ?   A . n 
A 1 49   ASN 49   60   ?    ?   ?   A . n 
A 1 50   ASN 50   61   ?    ?   ?   A . n 
A 1 51   PRO 51   62   ?    ?   ?   A . n 
A 1 52   ASP 52   63   ?    ?   ?   A . n 
A 1 53   VAL 53   64   ?    ?   ?   A . n 
A 1 54   VAL 54   65   ?    ?   ?   A . n 
A 1 55   ALA 55   66   ?    ?   ?   A . n 
A 1 56   ALA 56   67   ?    ?   ?   A . n 
A 1 57   ARG 57   68   ?    ?   ?   A . n 
A 1 58   PHE 58   69   ?    ?   ?   A . n 
A 1 59   ARG 59   70   ?    ?   ?   A . n 
A 1 60   SER 60   71   ?    ?   ?   A . n 
A 1 61   LEU 61   72   ?    ?   ?   A . n 
A 1 62   LEU 62   73   ?    ?   ?   A . n 
A 1 63   ARG 63   74   ?    ?   ?   A . n 
A 1 64   GLN 64   75   ?    ?   ?   A . n 
A 1 65   GLY 65   76   ?    ?   ?   A . n 
A 1 66   ASP 66   77   ?    ?   ?   A . n 
A 1 67   ILE 67   78   ?    ?   ?   A . n 
A 1 68   ASP 68   79   ?    ?   ?   A . n 
A 1 69   GLY 69   80   ?    ?   ?   A . n 
A 1 70   ALA 70   81   ?    ?   ?   A . n 
A 1 71   GLN 71   82   ?    ?   ?   A . n 
A 1 72   LYS 72   83   ?    ?   ?   A . n 
A 1 73   GLN 73   84   ?    ?   ?   A . n 
A 1 74   LEU 74   85   ?    ?   ?   A . n 
A 1 75   ASP 75   86   ?    ?   ?   A . n 
A 1 76   ARG 76   87   ?    ?   ?   A . n 
A 1 77   LEU 77   88   ?    ?   ?   A . n 
A 1 78   SER 78   89   ?    ?   ?   A . n 
A 1 79   GLN 79   90   ?    ?   ?   A . n 
A 1 80   LEU 80   91   ?    ?   ?   A . n 
A 1 81   ALA 81   92   ?    ?   ?   A . n 
A 1 82   PRO 82   93   ?    ?   ?   A . n 
A 1 83   SER 83   94   ?    ?   ?   A . n 
A 1 84   SER 84   95   ?    ?   ?   A . n 
A 1 85   ASN 85   96   ?    ?   ?   A . n 
A 1 86   ALA 86   97   ?    ?   ?   A . n 
A 1 87   TYR 87   98   ?    ?   ?   A . n 
A 1 88   LYS 88   99   ?    ?   ?   A . n 
A 1 89   SER 89   100  ?    ?   ?   A . n 
A 1 90   SER 90   101  ?    ?   ?   A . n 
A 1 91   ARG 91   102  ?    ?   ?   A . n 
A 1 92   THR 92   103  ?    ?   ?   A . n 
A 1 93   THR 93   104  ?    ?   ?   A . n 
A 1 94   MET 94   105  ?    ?   ?   A . n 
A 1 95   LEU 95   106  ?    ?   ?   A . n 
A 1 96   LEU 96   107  ?    ?   ?   A . n 
A 1 97   SER 97   108  ?    ?   ?   A . n 
A 1 98   THR 98   109  ?    ?   ?   A . n 
A 1 99   PRO 99   110  ?    ?   ?   A . n 
A 1 100  ASP 100  111  ?    ?   ?   A . n 
A 1 101  GLY 101  112  ?    ?   ?   A . n 
A 1 102  ARG 102  113  ?    ?   ?   A . n 
A 1 103  GLN 103  114  ?    ?   ?   A . n 
A 1 104  ALA 104  115  ?    ?   ?   A . n 
A 1 105  LEU 105  116  ?    ?   ?   A . n 
A 1 106  GLN 106  117  ?    ?   ?   A . n 
A 1 107  GLN 107  118  ?    ?   ?   A . n 
A 1 108  ALA 108  119  ?    ?   ?   A . n 
A 1 109  ARG 109  120  ?    ?   ?   A . n 
A 1 110  LEU 110  121  ?    ?   ?   A . n 
A 1 111  GLN 111  122  ?    ?   ?   A . n 
A 1 112  ALA 112  123  ?    ?   ?   A . n 
A 1 113  THR 113  124  ?    ?   ?   A . n 
A 1 114  THR 114  125  ?    ?   ?   A . n 
A 1 115  GLY 115  126  ?    ?   ?   A . n 
A 1 116  HIS 116  127  ?    ?   ?   A . n 
A 1 117  ALA 117  128  ?    ?   ?   A . n 
A 1 118  GLU 118  129  ?    ?   ?   A . n 
A 1 119  GLU 119  130  ?    ?   ?   A . n 
A 1 120  ALA 120  131  ?    ?   ?   A . n 
A 1 121  VAL 121  132  ?    ?   ?   A . n 
A 1 122  ALA 122  133  ?    ?   ?   A . n 
A 1 123  SER 123  134  ?    ?   ?   A . n 
A 1 124  TYR 124  135  ?    ?   ?   A . n 
A 1 125  ASN 125  136  ?    ?   ?   A . n 
A 1 126  LYS 126  137  ?    ?   ?   A . n 
A 1 127  LEU 127  138  ?    ?   ?   A . n 
A 1 128  PHE 128  139  ?    ?   ?   A . n 
A 1 129  ASN 129  140  ?    ?   ?   A . n 
A 1 130  GLY 130  141  ?    ?   ?   A . n 
A 1 131  ALA 131  142  ?    ?   ?   A . n 
A 1 132  PRO 132  143  ?    ?   ?   A . n 
A 1 133  PRO 133  144  ?    ?   ?   A . n 
A 1 134  GLU 134  145  ?    ?   ?   A . n 
A 1 135  GLY 135  146  ?    ?   ?   A . n 
A 1 136  ASP 136  147  ?    ?   ?   A . n 
A 1 137  ILE 137  148  ?    ?   ?   A . n 
A 1 138  ALA 138  149  ?    ?   ?   A . n 
A 1 139  VAL 139  150  ?    ?   ?   A . n 
A 1 140  GLU 140  151  ?    ?   ?   A . n 
A 1 141  TYR 141  152  ?    ?   ?   A . n 
A 1 142  TRP 142  153  ?    ?   ?   A . n 
A 1 143  SER 143  154  ?    ?   ?   A . n 
A 1 144  THR 144  155  ?    ?   ?   A . n 
A 1 145  VAL 145  156  ?    ?   ?   A . n 
A 1 146  ALA 146  157  ?    ?   ?   A . n 
A 1 147  LYS 147  158  ?    ?   ?   A . n 
A 1 148  ILE 148  159  ?    ?   ?   A . n 
A 1 149  PRO 149  160  ?    ?   ?   A . n 
A 1 150  ALA 150  161  ?    ?   ?   A . n 
A 1 151  ARG 151  162  ?    ?   ?   A . n 
A 1 152  ARG 152  163  ?    ?   ?   A . n 
A 1 153  GLY 153  164  ?    ?   ?   A . n 
A 1 154  GLU 154  165  ?    ?   ?   A . n 
A 1 155  ALA 155  166  ?    ?   ?   A . n 
A 1 156  ILE 156  167  ?    ?   ?   A . n 
A 1 157  ASN 157  168  ?    ?   ?   A . n 
A 1 158  GLN 158  169  ?    ?   ?   A . n 
A 1 159  LEU 159  170  ?    ?   ?   A . n 
A 1 160  LYS 160  171  ?    ?   ?   A . n 
A 1 161  ARG 161  172  ?    ?   ?   A . n 
A 1 162  ILE 162  173  ?    ?   ?   A . n 
A 1 163  ASN 163  174  ?    ?   ?   A . n 
A 1 164  ALA 164  175  ?    ?   ?   A . n 
A 1 165  ASP 165  176  ?    ?   ?   A . n 
A 1 166  ALA 166  177  ?    ?   ?   A . n 
A 1 167  PRO 167  178  ?    ?   ?   A . n 
A 1 168  GLY 168  179  ?    ?   ?   A . n 
A 1 169  ASN 169  180  ?    ?   ?   A . n 
A 1 170  THR 170  181  ?    ?   ?   A . n 
A 1 171  GLY 171  182  ?    ?   ?   A . n 
A 1 172  LEU 172  183  ?    ?   ?   A . n 
A 1 173  GLN 173  184  ?    ?   ?   A . n 
A 1 174  ASN 174  185  ?    ?   ?   A . n 
A 1 175  ASN 175  186  ?    ?   ?   A . n 
A 1 176  LEU 176  187  ?    ?   ?   A . n 
A 1 177  ALA 177  188  ?    ?   ?   A . n 
A 1 178  LEU 178  189  ?    ?   ?   A . n 
A 1 179  LEU 179  190  ?    ?   ?   A . n 
A 1 180  LEU 180  191  ?    ?   ?   A . n 
A 1 181  PHE 181  192  ?    ?   ?   A . n 
A 1 182  SER 182  193  ?    ?   ?   A . n 
A 1 183  SER 183  194  ?    ?   ?   A . n 
A 1 184  ASP 184  195  ?    ?   ?   A . n 
A 1 185  ARG 185  196  ?    ?   ?   A . n 
A 1 186  ARG 186  197  ?    ?   ?   A . n 
A 1 187  ASP 187  198  ?    ?   ?   A . n 
A 1 188  GLU 188  199  ?    ?   ?   A . n 
A 1 189  GLY 189  200  ?    ?   ?   A . n 
A 1 190  PHE 190  201  ?    ?   ?   A . n 
A 1 191  ALA 191  202  ?    ?   ?   A . n 
A 1 192  VAL 192  203  ?    ?   ?   A . n 
A 1 193  LEU 193  204  ?    ?   ?   A . n 
A 1 194  GLU 194  205  ?    ?   ?   A . n 
A 1 195  GLN 195  206  ?    ?   ?   A . n 
A 1 196  MET 196  207  ?    ?   ?   A . n 
A 1 197  ALA 197  208  ?    ?   ?   A . n 
A 1 198  LYS 198  209  ?    ?   ?   A . n 
A 1 199  SER 199  210  ?    ?   ?   A . n 
A 1 200  ASN 200  211  ?    ?   ?   A . n 
A 1 201  ALA 201  212  ?    ?   ?   A . n 
A 1 202  GLY 202  213  ?    ?   ?   A . n 
A 1 203  ARG 203  214  ?    ?   ?   A . n 
A 1 204  GLU 204  215  ?    ?   ?   A . n 
A 1 205  GLY 205  216  ?    ?   ?   A . n 
A 1 206  ALA 206  217  ?    ?   ?   A . n 
A 1 207  SER 207  218  ?    ?   ?   A . n 
A 1 208  LYS 208  219  ?    ?   ?   A . n 
A 1 209  ILE 209  220  ?    ?   ?   A . n 
A 1 210  TRP 210  221  ?    ?   ?   A . n 
A 1 211  TYR 211  222  ?    ?   ?   A . n 
A 1 212  GLY 212  223  ?    ?   ?   A . n 
A 1 213  GLN 213  224  ?    ?   ?   A . n 
A 1 214  ILE 214  225  ?    ?   ?   A . n 
A 1 215  LYS 215  226  ?    ?   ?   A . n 
A 1 216  ASP 216  227  ?    ?   ?   A . n 
A 1 217  MET 217  228  ?    ?   ?   A . n 
A 1 218  PRO 218  229  ?    ?   ?   A . n 
A 1 219  VAL 219  230  ?    ?   ?   A . n 
A 1 220  SER 220  231  ?    ?   ?   A . n 
A 1 221  ASP 221  232  ?    ?   ?   A . n 
A 1 222  ALA 222  233  ?    ?   ?   A . n 
A 1 223  SER 223  234  ?    ?   ?   A . n 
A 1 224  VAL 224  235  ?    ?   ?   A . n 
A 1 225  SER 225  236  ?    ?   ?   A . n 
A 1 226  ALA 226  237  ?    ?   ?   A . n 
A 1 227  LEU 227  238  ?    ?   ?   A . n 
A 1 228  LYS 228  239  ?    ?   ?   A . n 
A 1 229  LYS 229  240  ?    ?   ?   A . n 
A 1 230  TYR 230  241  ?    ?   ?   A . n 
A 1 231  LEU 231  242  ?    ?   ?   A . n 
A 1 232  SER 232  243  ?    ?   ?   A . n 
A 1 233  ILE 233  244  ?    ?   ?   A . n 
A 1 234  PHE 234  245  ?    ?   ?   A . n 
A 1 235  SER 235  246  ?    ?   ?   A . n 
A 1 236  ASP 236  247  ?    ?   ?   A . n 
A 1 237  GLY 237  248  ?    ?   ?   A . n 
A 1 238  ASP 238  249  ?    ?   ?   A . n 
A 1 239  SER 239  250  ?    ?   ?   A . n 
A 1 240  VAL 240  251  ?    ?   ?   A . n 
A 1 241  ALA 241  252  ?    ?   ?   A . n 
A 1 242  ALA 242  253  ?    ?   ?   A . n 
A 1 243  ALA 243  254  ?    ?   ?   A . n 
A 1 244  GLN 244  255  ?    ?   ?   A . n 
A 1 245  SER 245  256  ?    ?   ?   A . n 
A 1 246  GLN 246  257  ?    ?   ?   A . n 
A 1 247  LEU 247  258  ?    ?   ?   A . n 
A 1 248  ALA 248  259  ?    ?   ?   A . n 
A 1 249  GLU 249  260  ?    ?   ?   A . n 
A 1 250  GLN 250  261  ?    ?   ?   A . n 
A 1 251  GLN 251  262  ?    ?   ?   A . n 
A 1 252  LYS 252  263  ?    ?   ?   A . n 
A 1 253  GLN 253  264  ?    ?   ?   A . n 
A 1 254  LEU 254  265  ?    ?   ?   A . n 
A 1 255  ALA 255  266  ?    ?   ?   A . n 
A 1 256  ASP 256  267  ?    ?   ?   A . n 
A 1 257  PRO 257  268  ?    ?   ?   A . n 
A 1 258  ALA 258  269  ?    ?   ?   A . n 
A 1 259  PHE 259  270  ?    ?   ?   A . n 
A 1 260  ARG 260  271  ?    ?   ?   A . n 
A 1 261  ALA 261  272  ?    ?   ?   A . n 
A 1 262  ARG 262  273  ?    ?   ?   A . n 
A 1 263  ALA 263  274  ?    ?   ?   A . n 
A 1 264  GLN 264  275  ?    ?   ?   A . n 
A 1 265  GLY 265  276  ?    ?   ?   A . n 
A 1 266  LEU 266  277  ?    ?   ?   A . n 
A 1 267  ALA 267  278  ?    ?   ?   A . n 
A 1 268  ALA 268  279  ?    ?   ?   A . n 
A 1 269  VAL 269  280  ?    ?   ?   A . n 
A 1 270  ASP 270  281  ?    ?   ?   A . n 
A 1 271  SER 271  282  ?    ?   ?   A . n 
A 1 272  GLY 272  283  ?    ?   ?   A . n 
A 1 273  MET 273  284  ?    ?   ?   A . n 
A 1 274  ALA 274  285  ?    ?   ?   A . n 
A 1 275  GLY 275  286  ?    ?   ?   A . n 
A 1 276  LYS 276  287  ?    ?   ?   A . n 
A 1 277  ALA 277  288  ?    ?   ?   A . n 
A 1 278  ILE 278  289  ?    ?   ?   A . n 
A 1 279  PRO 279  290  ?    ?   ?   A . n 
A 1 280  GLU 280  291  ?    ?   ?   A . n 
A 1 281  LEU 281  292  ?    ?   ?   A . n 
A 1 282  GLN 282  293  ?    ?   ?   A . n 
A 1 283  GLN 283  294  ?    ?   ?   A . n 
A 1 284  ALA 284  295  ?    ?   ?   A . n 
A 1 285  VAL 285  296  ?    ?   ?   A . n 
A 1 286  ARG 286  297  ?    ?   ?   A . n 
A 1 287  ALA 287  298  ?    ?   ?   A . n 
A 1 288  ASN 288  299  ?    ?   ?   A . n 
A 1 289  PRO 289  300  ?    ?   ?   A . n 
A 1 290  LYS 290  301  ?    ?   ?   A . n 
A 1 291  ASP 291  302  ?    ?   ?   A . n 
A 1 292  SER 292  303  ?    ?   ?   A . n 
A 1 293  GLU 293  304  ?    ?   ?   A . n 
A 1 294  ALA 294  305  ?    ?   ?   A . n 
A 1 295  LEU 295  306  ?    ?   ?   A . n 
A 1 296  GLY 296  307  ?    ?   ?   A . n 
A 1 297  ALA 297  308  ?    ?   ?   A . n 
A 1 298  LEU 298  309  ?    ?   ?   A . n 
A 1 299  GLY 299  310  ?    ?   ?   A . n 
A 1 300  GLN 300  311  ?    ?   ?   A . n 
A 1 301  ALA 301  312  ?    ?   ?   A . n 
A 1 302  TYR 302  313  ?    ?   ?   A . n 
A 1 303  SER 303  314  ?    ?   ?   A . n 
A 1 304  GLN 304  315  ?    ?   ?   A . n 
A 1 305  LYS 305  316  ?    ?   ?   A . n 
A 1 306  GLY 306  317  ?    ?   ?   A . n 
A 1 307  ASP 307  318  ?    ?   ?   A . n 
A 1 308  ARG 308  319  ?    ?   ?   A . n 
A 1 309  ALA 309  320  ?    ?   ?   A . n 
A 1 310  ASN 310  321  ?    ?   ?   A . n 
A 1 311  ALA 311  322  ?    ?   ?   A . n 
A 1 312  VAL 312  323  ?    ?   ?   A . n 
A 1 313  ALA 313  324  ?    ?   ?   A . n 
A 1 314  ASN 314  325  ?    ?   ?   A . n 
A 1 315  LEU 315  326  ?    ?   ?   A . n 
A 1 316  GLU 316  327  ?    ?   ?   A . n 
A 1 317  LYS 317  328  ?    ?   ?   A . n 
A 1 318  ALA 318  329  ?    ?   ?   A . n 
A 1 319  LEU 319  330  ?    ?   ?   A . n 
A 1 320  ALA 320  331  ?    ?   ?   A . n 
A 1 321  LEU 321  332  ?    ?   ?   A . n 
A 1 322  ASP 322  333  ?    ?   ?   A . n 
A 1 323  PRO 323  334  ?    ?   ?   A . n 
A 1 324  HIS 324  335  ?    ?   ?   A . n 
A 1 325  SER 325  336  ?    ?   ?   A . n 
A 1 326  SER 326  337  ?    ?   ?   A . n 
A 1 327  ASN 327  338  ?    ?   ?   A . n 
A 1 328  ASN 328  339  ?    ?   ?   A . n 
A 1 329  ASP 329  340  ?    ?   ?   A . n 
A 1 330  LYS 330  341  ?    ?   ?   A . n 
A 1 331  TRP 331  342  ?    ?   ?   A . n 
A 1 332  ASN 332  343  ?    ?   ?   A . n 
A 1 333  SER 333  344  ?    ?   ?   A . n 
A 1 334  LEU 334  345  ?    ?   ?   A . n 
A 1 335  LEU 335  346  ?    ?   ?   A . n 
A 1 336  LYS 336  347  ?    ?   ?   A . n 
A 1 337  VAL 337  348  ?    ?   ?   A . n 
A 1 338  ASN 338  349  ?    ?   ?   A . n 
A 1 339  ARG 339  350  ?    ?   ?   A . n 
A 1 340  TYR 340  351  ?    ?   ?   A . n 
A 1 341  TRP 341  352  ?    ?   ?   A . n 
A 1 342  LEU 342  353  ?    ?   ?   A . n 
A 1 343  ALA 343  354  ?    ?   ?   A . n 
A 1 344  ILE 344  355  ?    ?   ?   A . n 
A 1 345  GLN 345  356  ?    ?   ?   A . n 
A 1 346  GLN 346  357  ?    ?   ?   A . n 
A 1 347  GLY 347  358  ?    ?   ?   A . n 
A 1 348  ASP 348  359  ?    ?   ?   A . n 
A 1 349  ALA 349  360  ?    ?   ?   A . n 
A 1 350  ALA 350  361  ?    ?   ?   A . n 
A 1 351  LEU 351  362  ?    ?   ?   A . n 
A 1 352  LYS 352  363  ?    ?   ?   A . n 
A 1 353  ALA 353  364  ?    ?   ?   A . n 
A 1 354  ASN 354  365  ?    ?   ?   A . n 
A 1 355  ASN 355  366  ?    ?   ?   A . n 
A 1 356  PRO 356  367  ?    ?   ?   A . n 
A 1 357  ASP 357  368  ?    ?   ?   A . n 
A 1 358  ARG 358  369  ?    ?   ?   A . n 
A 1 359  ALA 359  370  ?    ?   ?   A . n 
A 1 360  GLU 360  371  ?    ?   ?   A . n 
A 1 361  ARG 361  372  ?    ?   ?   A . n 
A 1 362  LEU 362  373  ?    ?   ?   A . n 
A 1 363  PHE 363  374  ?    ?   ?   A . n 
A 1 364  GLN 364  375  ?    ?   ?   A . n 
A 1 365  GLN 365  376  ?    ?   ?   A . n 
A 1 366  ALA 366  377  ?    ?   ?   A . n 
A 1 367  ARG 367  378  ?    ?   ?   A . n 
A 1 368  ASN 368  379  ?    ?   ?   A . n 
A 1 369  VAL 369  380  ?    ?   ?   A . n 
A 1 370  ASP 370  381  ?    ?   ?   A . n 
A 1 371  ASN 371  382  ?    ?   ?   A . n 
A 1 372  THR 372  383  ?    ?   ?   A . n 
A 1 373  ASP 373  384  ?    ?   ?   A . n 
A 1 374  SER 374  385  ?    ?   ?   A . n 
A 1 375  TYR 375  386  ?    ?   ?   A . n 
A 1 376  ALA 376  387  ?    ?   ?   A . n 
A 1 377  VAL 377  388  ?    ?   ?   A . n 
A 1 378  LEU 378  389  ?    ?   ?   A . n 
A 1 379  GLY 379  390  ?    ?   ?   A . n 
A 1 380  LEU 380  391  ?    ?   ?   A . n 
A 1 381  GLY 381  392  ?    ?   ?   A . n 
A 1 382  ASP 382  393  ?    ?   ?   A . n 
A 1 383  VAL 383  394  ?    ?   ?   A . n 
A 1 384  ALA 384  395  ?    ?   ?   A . n 
A 1 385  MET 385  396  ?    ?   ?   A . n 
A 1 386  ALA 386  397  ?    ?   ?   A . n 
A 1 387  ARG 387  398  ?    ?   ?   A . n 
A 1 388  LYS 388  399  ?    ?   ?   A . n 
A 1 389  ASP 389  400  ?    ?   ?   A . n 
A 1 390  TYR 390  401  ?    ?   ?   A . n 
A 1 391  PRO 391  402  ?    ?   ?   A . n 
A 1 392  ALA 392  403  ?    ?   ?   A . n 
A 1 393  ALA 393  404  ?    ?   ?   A . n 
A 1 394  GLU 394  405  ?    ?   ?   A . n 
A 1 395  ARG 395  406  ?    ?   ?   A . n 
A 1 396  TYR 396  407  ?    ?   ?   A . n 
A 1 397  TYR 397  408  ?    ?   ?   A . n 
A 1 398  GLN 398  409  ?    ?   ?   A . n 
A 1 399  GLN 399  410  ?    ?   ?   A . n 
A 1 400  THR 400  411  ?    ?   ?   A . n 
A 1 401  LEU 401  412  ?    ?   ?   A . n 
A 1 402  ARG 402  413  ?    ?   ?   A . n 
A 1 403  MET 403  414  ?    ?   ?   A . n 
A 1 404  ASP 404  415  ?    ?   ?   A . n 
A 1 405  SER 405  416  ?    ?   ?   A . n 
A 1 406  GLY 406  417  ?    ?   ?   A . n 
A 1 407  ASN 407  418  ?    ?   ?   A . n 
A 1 408  THR 408  419  ?    ?   ?   A . n 
A 1 409  ASN 409  420  ?    ?   ?   A . n 
A 1 410  ALA 410  421  ?    ?   ?   A . n 
A 1 411  VAL 411  422  ?    ?   ?   A . n 
A 1 412  ARG 412  423  ?    ?   ?   A . n 
A 1 413  GLY 413  424  ?    ?   ?   A . n 
A 1 414  LEU 414  425  ?    ?   ?   A . n 
A 1 415  ALA 415  426  ?    ?   ?   A . n 
A 1 416  ASN 416  427  ?    ?   ?   A . n 
A 1 417  ILE 417  428  ?    ?   ?   A . n 
A 1 418  TYR 418  429  ?    ?   ?   A . n 
A 1 419  ARG 419  430  ?    ?   ?   A . n 
A 1 420  GLN 420  431  ?    ?   ?   A . n 
A 1 421  GLN 421  432  ?    ?   ?   A . n 
A 1 422  SER 422  433  ?    ?   ?   A . n 
A 1 423  PRO 423  434  ?    ?   ?   A . n 
A 1 424  GLU 424  435  ?    ?   ?   A . n 
A 1 425  LYS 425  436  ?    ?   ?   A . n 
A 1 426  ALA 426  437  ?    ?   ?   A . n 
A 1 427  GLU 427  438  ?    ?   ?   A . n 
A 1 428  ALA 428  439  ?    ?   ?   A . n 
A 1 429  PHE 429  440  ?    ?   ?   A . n 
A 1 430  ILE 430  441  ?    ?   ?   A . n 
A 1 431  ALA 431  442  ?    ?   ?   A . n 
A 1 432  SER 432  443  ?    ?   ?   A . n 
A 1 433  LEU 433  444  ?    ?   ?   A . n 
A 1 434  SER 434  445  ?    ?   ?   A . n 
A 1 435  ALA 435  446  ?    ?   ?   A . n 
A 1 436  SER 436  447  ?    ?   ?   A . n 
A 1 437  GLN 437  448  ?    ?   ?   A . n 
A 1 438  ARG 438  449  ?    ?   ?   A . n 
A 1 439  ARG 439  450  ?    ?   ?   A . n 
A 1 440  SER 440  451  ?    ?   ?   A . n 
A 1 441  ILE 441  452  ?    ?   ?   A . n 
A 1 442  ASP 442  453  ?    ?   ?   A . n 
A 1 443  ASP 443  454  ?    ?   ?   A . n 
A 1 444  ILE 444  455  ?    ?   ?   A . n 
A 1 445  GLU 445  456  ?    ?   ?   A . n 
A 1 446  ARG 446  457  ?    ?   ?   A . n 
A 1 447  SER 447  458  ?    ?   ?   A . n 
A 1 448  LEU 448  459  ?    ?   ?   A . n 
A 1 449  GLN 449  460  ?    ?   ?   A . n 
A 1 450  ASN 450  461  ?    ?   ?   A . n 
A 1 451  ASP 451  462  ?    ?   ?   A . n 
A 1 452  ARG 452  463  ?    ?   ?   A . n 
A 1 453  LEU 453  464  ?    ?   ?   A . n 
A 1 454  ALA 454  465  ?    ?   ?   A . n 
A 1 455  GLN 455  466  ?    ?   ?   A . n 
A 1 456  GLN 456  467  ?    ?   ?   A . n 
A 1 457  ALA 457  468  ?    ?   ?   A . n 
A 1 458  GLU 458  469  ?    ?   ?   A . n 
A 1 459  ALA 459  470  ?    ?   ?   A . n 
A 1 460  LEU 460  471  ?    ?   ?   A . n 
A 1 461  GLU 461  472  ?    ?   ?   A . n 
A 1 462  ASN 462  473  ?    ?   ?   A . n 
A 1 463  GLN 463  474  ?    ?   ?   A . n 
A 1 464  GLY 464  475  ?    ?   ?   A . n 
A 1 465  LYS 465  476  ?    ?   ?   A . n 
A 1 466  TRP 466  477  ?    ?   ?   A . n 
A 1 467  ALA 467  478  ?    ?   ?   A . n 
A 1 468  GLN 468  479  ?    ?   ?   A . n 
A 1 469  ALA 469  480  ?    ?   ?   A . n 
A 1 470  ALA 470  481  ?    ?   ?   A . n 
A 1 471  ALA 471  482  ?    ?   ?   A . n 
A 1 472  LEU 472  483  ?    ?   ?   A . n 
A 1 473  GLN 473  484  ?    ?   ?   A . n 
A 1 474  ARG 474  485  ?    ?   ?   A . n 
A 1 475  GLN 475  486  ?    ?   ?   A . n 
A 1 476  ARG 476  487  ?    ?   ?   A . n 
A 1 477  LEU 477  488  ?    ?   ?   A . n 
A 1 478  ALA 478  489  ?    ?   ?   A . n 
A 1 479  LEU 479  490  ?    ?   ?   A . n 
A 1 480  ASP 480  491  ?    ?   ?   A . n 
A 1 481  PRO 481  492  ?    ?   ?   A . n 
A 1 482  GLY 482  493  ?    ?   ?   A . n 
A 1 483  SER 483  494  ?    ?   ?   A . n 
A 1 484  VAL 484  495  ?    ?   ?   A . n 
A 1 485  TRP 485  496  ?    ?   ?   A . n 
A 1 486  ILE 486  497  ?    ?   ?   A . n 
A 1 487  THR 487  498  ?    ?   ?   A . n 
A 1 488  TYR 488  499  ?    ?   ?   A . n 
A 1 489  ARG 489  500  ?    ?   ?   A . n 
A 1 490  LEU 490  501  ?    ?   ?   A . n 
A 1 491  SER 491  502  ?    ?   ?   A . n 
A 1 492  GLN 492  503  ?    ?   ?   A . n 
A 1 493  ASP 493  504  ?    ?   ?   A . n 
A 1 494  LEU 494  505  ?    ?   ?   A . n 
A 1 495  TRP 495  506  ?    ?   ?   A . n 
A 1 496  GLN 496  507  ?    ?   ?   A . n 
A 1 497  ALA 497  508  ?    ?   ?   A . n 
A 1 498  GLY 498  509  ?    ?   ?   A . n 
A 1 499  GLN 499  510  ?    ?   ?   A . n 
A 1 500  ARG 500  511  ?    ?   ?   A . n 
A 1 501  SER 501  512  ?    ?   ?   A . n 
A 1 502  GLN 502  513  ?    ?   ?   A . n 
A 1 503  ALA 503  514  ?    ?   ?   A . n 
A 1 504  ASP 504  515  ?    ?   ?   A . n 
A 1 505  THR 505  516  ?    ?   ?   A . n 
A 1 506  LEU 506  517  ?    ?   ?   A . n 
A 1 507  MET 507  518  ?    ?   ?   A . n 
A 1 508  ARG 508  519  ?    ?   ?   A . n 
A 1 509  ASN 509  520  ?    ?   ?   A . n 
A 1 510  LEU 510  521  ?    ?   ?   A . n 
A 1 511  ALA 511  522  ?    ?   ?   A . n 
A 1 512  GLN 512  523  ?    ?   ?   A . n 
A 1 513  GLN 513  524  ?    ?   ?   A . n 
A 1 514  LYS 514  525  ?    ?   ?   A . n 
A 1 515  SER 515  526  ?    ?   ?   A . n 
A 1 516  ASN 516  527  ?    ?   ?   A . n 
A 1 517  ASP 517  528  ?    ?   ?   A . n 
A 1 518  PRO 518  529  ?    ?   ?   A . n 
A 1 519  GLU 519  530  ?    ?   ?   A . n 
A 1 520  GLN 520  531  ?    ?   ?   A . n 
A 1 521  VAL 521  532  ?    ?   ?   A . n 
A 1 522  TYR 522  533  ?    ?   ?   A . n 
A 1 523  ALA 523  534  ?    ?   ?   A . n 
A 1 524  TYR 524  535  ?    ?   ?   A . n 
A 1 525  GLY 525  536  ?    ?   ?   A . n 
A 1 526  LEU 526  537  ?    ?   ?   A . n 
A 1 527  TYR 527  538  ?    ?   ?   A . n 
A 1 528  LEU 528  539  ?    ?   ?   A . n 
A 1 529  SER 529  540  ?    ?   ?   A . n 
A 1 530  GLY 530  541  ?    ?   ?   A . n 
A 1 531  HIS 531  542  ?    ?   ?   A . n 
A 1 532  ASP 532  543  ?    ?   ?   A . n 
A 1 533  GLN 533  544  ?    ?   ?   A . n 
A 1 534  ASP 534  545  ?    ?   ?   A . n 
A 1 535  ARG 535  546  ?    ?   ?   A . n 
A 1 536  ALA 536  547  ?    ?   ?   A . n 
A 1 537  ALA 537  548  ?    ?   ?   A . n 
A 1 538  LEU 538  549  ?    ?   ?   A . n 
A 1 539  ALA 539  550  ?    ?   ?   A . n 
A 1 540  HIS 540  551  ?    ?   ?   A . n 
A 1 541  ILE 541  552  ?    ?   ?   A . n 
A 1 542  ASN 542  553  ?    ?   ?   A . n 
A 1 543  SER 543  554  ?    ?   ?   A . n 
A 1 544  LEU 544  555  ?    ?   ?   A . n 
A 1 545  PRO 545  556  ?    ?   ?   A . n 
A 1 546  ARG 546  557  ?    ?   ?   A . n 
A 1 547  ALA 547  558  ?    ?   ?   A . n 
A 1 548  GLN 548  559  ?    ?   ?   A . n 
A 1 549  TRP 549  560  ?    ?   ?   A . n 
A 1 550  ASN 550  561  ?    ?   ?   A . n 
A 1 551  SER 551  562  ?    ?   ?   A . n 
A 1 552  ASN 552  563  ?    ?   ?   A . n 
A 1 553  ILE 553  564  ?    ?   ?   A . n 
A 1 554  GLN 554  565  ?    ?   ?   A . n 
A 1 555  GLU 555  566  ?    ?   ?   A . n 
A 1 556  LEU 556  567  ?    ?   ?   A . n 
A 1 557  VAL 557  568  ?    ?   ?   A . n 
A 1 558  ASN 558  569  ?    ?   ?   A . n 
A 1 559  ARG 559  570  ?    ?   ?   A . n 
A 1 560  LEU 560  571  ?    ?   ?   A . n 
A 1 561  GLN 561  572  ?    ?   ?   A . n 
A 1 562  SER 562  573  ?    ?   ?   A . n 
A 1 563  ASP 563  574  ?    ?   ?   A . n 
A 1 564  GLN 564  575  ?    ?   ?   A . n 
A 1 565  VAL 565  576  ?    ?   ?   A . n 
A 1 566  LEU 566  577  ?    ?   ?   A . n 
A 1 567  GLU 567  578  ?    ?   ?   A . n 
A 1 568  THR 568  579  ?    ?   ?   A . n 
A 1 569  ALA 569  580  ?    ?   ?   A . n 
A 1 570  ASN 570  581  ?    ?   ?   A . n 
A 1 571  ARG 571  582  ?    ?   ?   A . n 
A 1 572  LEU 572  583  ?    ?   ?   A . n 
A 1 573  ARG 573  584  ?    ?   ?   A . n 
A 1 574  GLU 574  585  ?    ?   ?   A . n 
A 1 575  SER 575  586  ?    ?   ?   A . n 
A 1 576  GLY 576  587  ?    ?   ?   A . n 
A 1 577  LYS 577  588  ?    ?   ?   A . n 
A 1 578  GLU 578  589  ?    ?   ?   A . n 
A 1 579  ALA 579  590  ?    ?   ?   A . n 
A 1 580  GLU 580  591  ?    ?   ?   A . n 
A 1 581  ALA 581  592  ?    ?   ?   A . n 
A 1 582  GLU 582  593  ?    ?   ?   A . n 
A 1 583  ALA 583  594  ?    ?   ?   A . n 
A 1 584  MET 584  595  ?    ?   ?   A . n 
A 1 585  LEU 585  596  ?    ?   ?   A . n 
A 1 586  ARG 586  597  ?    ?   ?   A . n 
A 1 587  GLN 587  598  ?    ?   ?   A . n 
A 1 588  GLN 588  599  ?    ?   ?   A . n 
A 1 589  PRO 589  600  ?    ?   ?   A . n 
A 1 590  PRO 590  601  ?    ?   ?   A . n 
A 1 591  SER 591  602  602  SER SER A . n 
A 1 592  THR 592  603  603  THR THR A . n 
A 1 593  ARG 593  604  604  ARG ARG A . n 
A 1 594  ILE 594  605  605  ILE ILE A . n 
A 1 595  ASP 595  606  606  ASP ASP A . n 
A 1 596  LEU 596  607  607  LEU LEU A . n 
A 1 597  THR 597  608  608  THR THR A . n 
A 1 598  LEU 598  609  609  LEU LEU A . n 
A 1 599  ALA 599  610  610  ALA ALA A . n 
A 1 600  ASP 600  611  611  ASP ASP A . n 
A 1 601  TRP 601  612  612  TRP TRP A . n 
A 1 602  ALA 602  613  613  ALA ALA A . n 
A 1 603  GLN 603  614  614  GLN GLN A . n 
A 1 604  GLN 604  615  615  GLN GLN A . n 
A 1 605  ARG 605  616  ?    ?   ?   A . n 
A 1 606  ARG 606  617  ?    ?   ?   A . n 
A 1 607  ASP 607  618  618  ASP ASP A . n 
A 1 608  TYR 608  619  619  TYR TYR A . n 
A 1 609  THR 609  620  620  THR THR A . n 
A 1 610  ALA 610  621  621  ALA ALA A . n 
A 1 611  ALA 611  622  622  ALA ALA A . n 
A 1 612  ARG 612  623  623  ARG ARG A . n 
A 1 613  ALA 613  624  624  ALA ALA A . n 
A 1 614  ALA 614  625  625  ALA ALA A . n 
A 1 615  TYR 615  626  626  TYR TYR A . n 
A 1 616  GLN 616  627  627  GLN GLN A . n 
A 1 617  ASN 617  628  628  ASN ASN A . n 
A 1 618  VAL 618  629  629  VAL VAL A . n 
A 1 619  LEU 619  630  630  LEU LEU A . n 
A 1 620  THR 620  631  631  THR THR A . n 
A 1 621  ARG 621  632  632  ARG ARG A . n 
A 1 622  GLU 622  633  633  GLU GLU A . n 
A 1 623  PRO 623  634  634  PRO PRO A . n 
A 1 624  ALA 624  635  635  ALA ALA A . n 
A 1 625  ASN 625  636  636  ASN ASN A . n 
A 1 626  ALA 626  637  637  ALA ALA A . n 
A 1 627  ASP 627  638  638  ASP ASP A . n 
A 1 628  ALA 628  639  639  ALA ALA A . n 
A 1 629  ILE 629  640  640  ILE ILE A . n 
A 1 630  LEU 630  641  641  LEU LEU A . n 
A 1 631  GLY 631  642  642  GLY GLY A . n 
A 1 632  LEU 632  643  643  LEU LEU A . n 
A 1 633  THR 633  644  644  THR THR A . n 
A 1 634  GLU 634  645  645  GLU GLU A . n 
A 1 635  VAL 635  646  646  VAL VAL A . n 
A 1 636  ASP 636  647  647  ASP ASP A . n 
A 1 637  ILE 637  648  648  ILE ILE A . n 
A 1 638  ALA 638  649  649  ALA ALA A . n 
A 1 639  ALA 639  650  650  ALA ALA A . n 
A 1 640  GLY 640  651  651  GLY GLY A . n 
A 1 641  ASP 641  652  652  ASP ASP A . n 
A 1 642  LYS 642  653  653  LYS LYS A . n 
A 1 643  ALA 643  654  654  ALA ALA A . n 
A 1 644  ALA 644  655  655  ALA ALA A . n 
A 1 645  ALA 645  656  656  ALA ALA A . n 
A 1 646  ARG 646  657  657  ARG ARG A . n 
A 1 647  SER 647  658  658  SER SER A . n 
A 1 648  GLN 648  659  659  GLN GLN A . n 
A 1 649  LEU 649  660  660  LEU LEU A . n 
A 1 650  ALA 650  661  661  ALA ALA A . n 
A 1 651  LYS 651  662  662  LYS LYS A . n 
A 1 652  LEU 652  663  663  LEU LEU A . n 
A 1 653  PRO 653  664  664  PRO PRO A . n 
A 1 654  ALA 654  665  665  ALA ALA A . n 
A 1 655  THR 655  666  666  THR THR A . n 
A 1 656  ASP 656  667  667  ASP ASP A . n 
A 1 657  ASN 657  668  668  ASN ASN A . n 
A 1 658  ALA 658  669  669  ALA ALA A . n 
A 1 659  SER 659  670  670  SER SER A . n 
A 1 660  LEU 660  671  671  LEU LEU A . n 
A 1 661  ASN 661  672  672  ASN ASN A . n 
A 1 662  THR 662  673  673  THR THR A . n 
A 1 663  GLN 663  674  674  GLN GLN A . n 
A 1 664  ARG 664  675  675  ARG ARG A . n 
A 1 665  ARG 665  676  676  ARG ARG A . n 
A 1 666  VAL 666  677  677  VAL VAL A . n 
A 1 667  ALA 667  678  678  ALA ALA A . n 
A 1 668  LEU 668  679  679  LEU LEU A . n 
A 1 669  ALA 669  680  680  ALA ALA A . n 
A 1 670  GLN 670  681  681  GLN GLN A . n 
A 1 671  ALA 671  682  682  ALA ALA A . n 
A 1 672  GLN 672  683  683  GLN GLN A . n 
A 1 673  LEU 673  684  684  LEU LEU A . n 
A 1 674  GLY 674  685  685  GLY GLY A . n 
A 1 675  ASP 675  686  686  ASP ASP A . n 
A 1 676  THR 676  687  687  THR THR A . n 
A 1 677  ALA 677  688  688  ALA ALA A . n 
A 1 678  ALA 678  689  689  ALA ALA A . n 
A 1 679  ALA 679  690  690  ALA ALA A . n 
A 1 680  GLN 680  691  691  GLN GLN A . n 
A 1 681  ARG 681  692  692  ARG ARG A . n 
A 1 682  THR 682  693  693  THR THR A . n 
A 1 683  PHE 683  694  694  PHE PHE A . n 
A 1 684  ASN 684  695  695  ASN ASN A . n 
A 1 685  LYS 685  696  696  LYS LYS A . n 
A 1 686  LEU 686  697  697  LEU LEU A . n 
A 1 687  ILE 687  698  698  ILE ILE A . n 
A 1 688  PRO 688  699  699  PRO PRO A . n 
A 1 689  GLN 689  700  700  GLN GLN A . n 
A 1 690  ALA 690  701  701  ALA ALA A . n 
A 1 691  LYS 691  702  702  LYS LYS A . n 
A 1 692  SER 692  703  703  SER SER A . n 
A 1 693  GLN 693  704  704  GLN GLN A . n 
A 1 694  PRO 694  705  705  PRO PRO A . n 
A 1 695  PRO 695  706  706  PRO PRO A . n 
A 1 696  SER 696  707  707  SER SER A . n 
A 1 697  MET 697  708  708  MET MET A . n 
A 1 698  GLU 698  709  709  GLU GLU A . n 
A 1 699  SER 699  710  710  SER SER A . n 
A 1 700  ALA 700  711  711  ALA ALA A . n 
A 1 701  MET 701  712  712  MET MET A . n 
A 1 702  VAL 702  713  713  VAL VAL A . n 
A 1 703  LEU 703  714  714  LEU LEU A . n 
A 1 704  ARG 704  715  715  ARG ARG A . n 
A 1 705  ASP 705  716  716  ASP ASP A . n 
A 1 706  GLY 706  717  717  GLY GLY A . n 
A 1 707  ALA 707  718  718  ALA ALA A . n 
A 1 708  LYS 708  719  719  LYS LYS A . n 
A 1 709  PHE 709  720  720  PHE PHE A . n 
A 1 710  GLU 710  721  721  GLU GLU A . n 
A 1 711  ALA 711  722  722  ALA ALA A . n 
A 1 712  GLN 712  723  723  GLN GLN A . n 
A 1 713  ALA 713  724  724  ALA ALA A . n 
A 1 714  GLY 714  725  725  GLY GLY A . n 
A 1 715  ASP 715  726  726  ASP ASP A . n 
A 1 716  PRO 716  727  727  PRO PRO A . n 
A 1 717  THR 717  728  728  THR THR A . n 
A 1 718  GLN 718  729  729  GLN GLN A . n 
A 1 719  ALA 719  730  730  ALA ALA A . n 
A 1 720  LEU 720  731  731  LEU LEU A . n 
A 1 721  GLU 721  732  732  GLU GLU A . n 
A 1 722  THR 722  733  733  THR THR A . n 
A 1 723  TYR 723  734  734  TYR TYR A . n 
A 1 724  LYS 724  735  735  LYS LYS A . n 
A 1 725  ASP 725  736  736  ASP ASP A . n 
A 1 726  ALA 726  737  737  ALA ALA A . n 
A 1 727  MET 727  738  738  MET MET A . n 
A 1 728  VAL 728  739  739  VAL VAL A . n 
A 1 729  ALA 729  740  740  ALA ALA A . n 
A 1 730  SER 730  741  741  SER SER A . n 
A 1 731  GLY 731  742  742  GLY GLY A . n 
A 1 732  VAL 732  743  743  VAL VAL A . n 
A 1 733  THR 733  744  744  THR THR A . n 
A 1 734  THR 734  745  745  THR THR A . n 
A 1 735  THR 735  746  746  THR THR A . n 
A 1 736  ARG 736  747  747  ARG ARG A . n 
A 1 737  PRO 737  748  748  PRO PRO A . n 
A 1 738  GLN 738  749  749  GLN GLN A . n 
A 1 739  ASP 739  750  750  ASP ASP A . n 
A 1 740  ASN 740  751  751  ASN ASN A . n 
A 1 741  ASP 741  752  752  ASP ASP A . n 
A 1 742  THR 742  753  753  THR THR A . n 
A 1 743  PHE 743  754  754  PHE PHE A . n 
A 1 744  THR 744  755  755  THR THR A . n 
A 1 745  ARG 745  756  756  ARG ARG A . n 
A 1 746  LEU 746  757  757  LEU LEU A . n 
A 1 747  THR 747  758  758  THR THR A . n 
A 1 748  ARG 748  759  759  ARG ARG A . n 
A 1 749  ASN 749  760  760  ASN ASN A . n 
A 1 750  ASP 750  761  761  ASP ASP A . n 
A 1 751  GLU 751  762  762  GLU GLU A . n 
A 1 752  LYS 752  763  763  LYS LYS A . n 
A 1 753  ASP 753  764  764  ASP ASP A . n 
A 1 754  ASP 754  765  765  ASP ASP A . n 
A 1 755  TRP 755  766  766  TRP TRP A . n 
A 1 756  LEU 756  767  767  LEU LEU A . n 
A 1 757  LYS 757  768  768  LYS LYS A . n 
A 1 758  ARG 758  769  769  ARG ARG A . n 
A 1 759  GLY 759  770  770  GLY GLY A . n 
A 1 760  VAL 760  771  771  VAL VAL A . n 
A 1 761  ARG 761  772  772  ARG ARG A . n 
A 1 762  SER 762  773  773  SER SER A . n 
A 1 763  ASP 763  774  774  ASP ASP A . n 
A 1 764  ALA 764  775  775  ALA ALA A . n 
A 1 765  ALA 765  776  776  ALA ALA A . n 
A 1 766  ASP 766  777  777  ASP ASP A . n 
A 1 767  LEU 767  778  778  LEU LEU A . n 
A 1 768  TYR 768  779  779  TYR TYR A . n 
A 1 769  ARG 769  780  780  ARG ARG A . n 
A 1 770  GLN 770  781  781  GLN GLN A . n 
A 1 771  GLN 771  782  782  GLN GLN A . n 
A 1 772  ASP 772  783  783  ASP ASP A . n 
A 1 773  LEU 773  784  784  LEU LEU A . n 
A 1 774  ASN 774  785  785  ASN ASN A . n 
A 1 775  VAL 775  786  786  VAL VAL A . n 
A 1 776  THR 776  787  787  THR THR A . n 
A 1 777  LEU 777  788  788  LEU LEU A . n 
A 1 778  GLU 778  789  789  GLU GLU A . n 
A 1 779  HIS 779  790  790  HIS HIS A . n 
A 1 780  ASP 780  791  791  ASP ASP A . n 
A 1 781  TYR 781  792  792  TYR TYR A . n 
A 1 782  TRP 782  793  793  TRP TRP A . n 
A 1 783  GLY 783  794  794  GLY GLY A . n 
A 1 784  SER 784  795  795  SER SER A . n 
A 1 785  SER 785  796  796  SER SER A . n 
A 1 786  GLY 786  797  797  GLY GLY A . n 
A 1 787  THR 787  798  798  THR THR A . n 
A 1 788  GLY 788  799  799  GLY GLY A . n 
A 1 789  GLY 789  800  800  GLY GLY A . n 
A 1 790  TYR 790  801  801  TYR TYR A . n 
A 1 791  SER 791  802  802  SER SER A . n 
A 1 792  ASP 792  803  803  ASP ASP A . n 
A 1 793  LEU 793  804  804  LEU LEU A . n 
A 1 794  LYS 794  805  805  LYS LYS A . n 
A 1 795  ALA 795  806  806  ALA ALA A . n 
A 1 796  HIS 796  807  807  HIS HIS A . n 
A 1 797  THR 797  808  808  THR THR A . n 
A 1 798  THR 798  809  809  THR THR A . n 
A 1 799  MET 799  810  810  MET MET A . n 
A 1 800  LEU 800  811  811  LEU LEU A . n 
A 1 801  GLN 801  812  812  GLN GLN A . n 
A 1 802  VAL 802  813  813  VAL VAL A . n 
A 1 803  ASP 803  814  814  ASP ASP A . n 
A 1 804  ALA 804  815  815  ALA ALA A . n 
A 1 805  PRO 805  816  816  PRO PRO A . n 
A 1 806  TYR 806  817  817  TYR TYR A . n 
A 1 807  SER 807  818  818  SER SER A . n 
A 1 808  ASP 808  819  819  ASP ASP A . n 
A 1 809  GLY 809  820  820  GLY GLY A . n 
A 1 810  ARG 810  821  821  ARG ARG A . n 
A 1 811  MET 811  822  822  MET MET A . n 
A 1 812  PHE 812  823  823  PHE PHE A . n 
A 1 813  PHE 813  824  824  PHE PHE A . n 
A 1 814  ARG 814  825  825  ARG ARG A . n 
A 1 815  SER 815  826  826  SER SER A . n 
A 1 816  ASP 816  827  827  ASP ASP A . n 
A 1 817  PHE 817  828  828  PHE PHE A . n 
A 1 818  VAL 818  829  829  VAL VAL A . n 
A 1 819  ASN 819  830  830  ASN ASN A . n 
A 1 820  MET 820  831  831  MET MET A . n 
A 1 821  ASN 821  832  832  ASN ASN A . n 
A 1 822  VAL 822  833  833  VAL VAL A . n 
A 1 823  GLY 823  834  834  GLY GLY A . n 
A 1 824  SER 824  835  835  SER SER A . n 
A 1 825  PHE 825  836  836  PHE PHE A . n 
A 1 826  SER 826  837  837  SER SER A . n 
A 1 827  THR 827  838  838  THR THR A . n 
A 1 828  ASN 828  839  839  ASN ASN A . n 
A 1 829  ALA 829  840  840  ALA ALA A . n 
A 1 830  ASP 830  841  841  ASP ASP A . n 
A 1 831  GLY 831  842  842  GLY GLY A . n 
A 1 832  LYS 832  843  843  LYS LYS A . n 
A 1 833  TRP 833  844  844  TRP TRP A . n 
A 1 834  ASP 834  845  845  ASP ASP A . n 
A 1 835  ASP 835  846  846  ASP ASP A . n 
A 1 836  ASN 836  847  847  ASN ASN A . n 
A 1 837  TRP 837  848  848  TRP TRP A . n 
A 1 838  GLY 838  849  849  GLY GLY A . n 
A 1 839  THR 839  850  850  THR THR A . n 
A 1 840  CYS 840  851  851  CYS CYS A . n 
A 1 841  THR 841  852  852  THR THR A . n 
A 1 842  LEU 842  853  853  LEU LEU A . n 
A 1 843  GLN 843  854  854  GLN GLN A . n 
A 1 844  ASP 844  855  855  ASP ASP A . n 
A 1 845  CYS 845  856  856  CYS CYS A . n 
A 1 846  SER 846  857  857  SER SER A . n 
A 1 847  GLY 847  858  858  GLY GLY A . n 
A 1 848  ASN 848  859  859  ASN ASN A . n 
A 1 849  ARG 849  860  860  ARG ARG A . n 
A 1 850  SER 850  861  861  SER SER A . n 
A 1 851  GLN 851  862  862  GLN GLN A . n 
A 1 852  SER 852  863  863  SER SER A . n 
A 1 853  ASP 853  864  864  ASP ASP A . n 
A 1 854  SER 854  865  865  SER SER A . n 
A 1 855  GLY 855  866  866  GLY GLY A . n 
A 1 856  ALA 856  867  867  ALA ALA A . n 
A 1 857  SER 857  868  868  SER SER A . n 
A 1 858  VAL 858  869  869  VAL VAL A . n 
A 1 859  ALA 859  870  870  ALA ALA A . n 
A 1 860  VAL 860  871  871  VAL VAL A . n 
A 1 861  GLY 861  872  872  GLY GLY A . n 
A 1 862  TRP 862  873  873  TRP TRP A . n 
A 1 863  ARG 863  874  874  ARG ARG A . n 
A 1 864  ASN 864  875  875  ASN ASN A . n 
A 1 865  ASP 865  876  876  ASP ASP A . n 
A 1 866  VAL 866  877  877  VAL VAL A . n 
A 1 867  TRP 867  878  878  TRP TRP A . n 
A 1 868  SER 868  879  879  SER SER A . n 
A 1 869  TRP 869  880  880  TRP TRP A . n 
A 1 870  ASP 870  881  881  ASP ASP A . n 
A 1 871  ILE 871  882  882  ILE ILE A . n 
A 1 872  GLY 872  883  883  GLY GLY A . n 
A 1 873  THR 873  884  884  THR THR A . n 
A 1 874  THR 874  885  885  THR THR A . n 
A 1 875  PRO 875  886  886  PRO PRO A . n 
A 1 876  MET 876  887  887  MET MET A . n 
A 1 877  GLY 877  888  888  GLY GLY A . n 
A 1 878  PHE 878  889  889  PHE PHE A . n 
A 1 879  ASN 879  890  890  ASN ASN A . n 
A 1 880  VAL 880  891  891  VAL VAL A . n 
A 1 881  VAL 881  892  892  VAL VAL A . n 
A 1 882  ASP 882  893  893  ASP ASP A . n 
A 1 883  VAL 883  894  894  VAL VAL A . n 
A 1 884  VAL 884  895  895  VAL VAL A . n 
A 1 885  GLY 885  896  896  GLY GLY A . n 
A 1 886  GLY 886  897  897  GLY GLY A . n 
A 1 887  ILE 887  898  898  ILE ILE A . n 
A 1 888  SER 888  899  899  SER SER A . n 
A 1 889  TYR 889  900  900  TYR TYR A . n 
A 1 890  SER 890  901  901  SER SER A . n 
A 1 891  ASP 891  902  902  ASP ASP A . n 
A 1 892  ASP 892  903  903  ASP ASP A . n 
A 1 893  ILE 893  904  904  ILE ILE A . n 
A 1 894  GLY 894  905  905  GLY GLY A . n 
A 1 895  PRO 895  906  906  PRO PRO A . n 
A 1 896  LEU 896  907  907  LEU LEU A . n 
A 1 897  GLY 897  908  908  GLY GLY A . n 
A 1 898  TYR 898  909  909  TYR TYR A . n 
A 1 899  THR 899  910  910  THR THR A . n 
A 1 900  VAL 900  911  911  VAL VAL A . n 
A 1 901  ASN 901  912  912  ASN ASN A . n 
A 1 902  ALA 902  913  913  ALA ALA A . n 
A 1 903  HIS 903  914  914  HIS HIS A . n 
A 1 904  ARG 904  915  915  ARG ARG A . n 
A 1 905  ARG 905  916  916  ARG ARG A . n 
A 1 906  PRO 906  917  917  PRO PRO A . n 
A 1 907  ILE 907  918  918  ILE ILE A . n 
A 1 908  SER 908  919  919  SER SER A . n 
A 1 909  SER 909  920  920  SER SER A . n 
A 1 910  SER 910  921  921  SER SER A . n 
A 1 911  LEU 911  922  922  LEU LEU A . n 
A 1 912  LEU 912  923  923  LEU LEU A . n 
A 1 913  ALA 913  924  924  ALA ALA A . n 
A 1 914  PHE 914  925  925  PHE PHE A . n 
A 1 915  GLY 915  926  926  GLY GLY A . n 
A 1 916  GLY 916  927  927  GLY GLY A . n 
A 1 917  GLN 917  928  928  GLN GLN A . n 
A 1 918  LYS 918  929  929  LYS LYS A . n 
A 1 919  ASP 919  930  930  ASP ASP A . n 
A 1 920  SER 920  931  931  SER SER A . n 
A 1 921  PRO 921  932  932  PRO PRO A . n 
A 1 922  SER 922  933  933  SER SER A . n 
A 1 923  ASN 923  934  934  ASN ASN A . n 
A 1 924  THR 924  935  935  THR THR A . n 
A 1 925  GLY 925  936  936  GLY GLY A . n 
A 1 926  LYS 926  937  937  LYS LYS A . n 
A 1 927  LYS 927  938  938  LYS LYS A . n 
A 1 928  TRP 928  939  939  TRP TRP A . n 
A 1 929  GLY 929  940  940  GLY GLY A . n 
A 1 930  GLY 930  941  941  GLY GLY A . n 
A 1 931  VAL 931  942  942  VAL VAL A . n 
A 1 932  ARG 932  943  943  ARG ARG A . n 
A 1 933  ALA 933  944  944  ALA ALA A . n 
A 1 934  ASP 934  945  945  ASP ASP A . n 
A 1 935  GLY 935  946  946  GLY GLY A . n 
A 1 936  VAL 936  947  947  VAL VAL A . n 
A 1 937  GLY 937  948  948  GLY GLY A . n 
A 1 938  LEU 938  949  949  LEU LEU A . n 
A 1 939  SER 939  950  950  SER SER A . n 
A 1 940  LEU 940  951  951  LEU LEU A . n 
A 1 941  SER 941  952  952  SER SER A . n 
A 1 942  TYR 942  953  953  TYR TYR A . n 
A 1 943  ASP 943  954  954  ASP ASP A . n 
A 1 944  LYS 944  955  955  LYS LYS A . n 
A 1 945  GLY 945  956  956  GLY GLY A . n 
A 1 946  GLU 946  957  957  GLU GLU A . n 
A 1 947  ALA 947  958  958  ALA ALA A . n 
A 1 948  ASN 948  959  959  ASN ASN A . n 
A 1 949  GLY 949  960  960  GLY GLY A . n 
A 1 950  VAL 950  961  961  VAL VAL A . n 
A 1 951  TRP 951  962  962  TRP TRP A . n 
A 1 952  ALA 952  963  963  ALA ALA A . n 
A 1 953  SER 953  964  964  SER SER A . n 
A 1 954  LEU 954  965  965  LEU LEU A . n 
A 1 955  SER 955  966  966  SER SER A . n 
A 1 956  GLY 956  967  967  GLY GLY A . n 
A 1 957  ASP 957  968  968  ASP ASP A . n 
A 1 958  GLN 958  969  969  GLN GLN A . n 
A 1 959  LEU 959  970  970  LEU LEU A . n 
A 1 960  THR 960  971  971  THR THR A . n 
A 1 961  GLY 961  972  972  GLY GLY A . n 
A 1 962  LYS 962  973  973  LYS LYS A . n 
A 1 963  ASN 963  974  974  ASN ASN A . n 
A 1 964  VAL 964  975  975  VAL VAL A . n 
A 1 965  GLU 965  976  976  GLU GLU A . n 
A 1 966  ASP 966  977  977  ASP ASP A . n 
A 1 967  ASN 967  978  978  ASN ASN A . n 
A 1 968  TRP 968  979  979  TRP TRP A . n 
A 1 969  ARG 969  980  980  ARG ARG A . n 
A 1 970  VAL 970  981  981  VAL VAL A . n 
A 1 971  ARG 971  982  982  ARG ARG A . n 
A 1 972  TRP 972  983  983  TRP TRP A . n 
A 1 973  MET 973  984  984  MET MET A . n 
A 1 974  THR 974  985  985  THR THR A . n 
A 1 975  GLY 975  986  986  GLY GLY A . n 
A 1 976  TYR 976  987  987  TYR TYR A . n 
A 1 977  TYR 977  988  988  TYR TYR A . n 
A 1 978  TYR 978  989  989  TYR TYR A . n 
A 1 979  LYS 979  990  990  LYS LYS A . n 
A 1 980  VAL 980  991  991  VAL VAL A . n 
A 1 981  ILE 981  992  992  ILE ILE A . n 
A 1 982  ASN 982  993  993  ASN ASN A . n 
A 1 983  GLN 983  994  994  GLN GLN A . n 
A 1 984  ASN 984  995  995  ASN ASN A . n 
A 1 985  ASN 985  996  996  ASN ASN A . n 
A 1 986  ARG 986  997  997  ARG ARG A . n 
A 1 987  ARG 987  998  998  ARG ARG A . n 
A 1 988  VAL 988  999  999  VAL VAL A . n 
A 1 989  THR 989  1000 1000 THR THR A . n 
A 1 990  ILE 990  1001 1001 ILE ILE A . n 
A 1 991  GLY 991  1002 1002 GLY GLY A . n 
A 1 992  LEU 992  1003 1003 LEU LEU A . n 
A 1 993  ASN 993  1004 1004 ASN ASN A . n 
A 1 994  ASN 994  1005 1005 ASN ASN A . n 
A 1 995  MET 995  1006 1006 MET MET A . n 
A 1 996  ILE 996  1007 1007 ILE ILE A . n 
A 1 997  TRP 997  1008 1008 TRP TRP A . n 
A 1 998  HIS 998  1009 1009 HIS HIS A . n 
A 1 999  TYR 999  1010 1010 TYR TYR A . n 
A 1 1000 ASP 1000 1011 1011 ASP ASP A . n 
A 1 1001 LYS 1001 1012 1012 LYS LYS A . n 
A 1 1002 ASP 1002 1013 1013 ASP ASP A . n 
A 1 1003 LEU 1003 1014 1014 LEU LEU A . n 
A 1 1004 SER 1004 1015 1015 SER SER A . n 
A 1 1005 GLY 1005 1016 1016 GLY GLY A . n 
A 1 1006 TYR 1006 1017 1017 TYR TYR A . n 
A 1 1007 SER 1007 1018 1018 SER SER A . n 
A 1 1008 LEU 1008 1019 1019 LEU LEU A . n 
A 1 1009 GLY 1009 1020 1020 GLY GLY A . n 
A 1 1010 GLN 1010 1021 1021 GLN GLN A . n 
A 1 1011 GLY 1011 1022 1022 GLY GLY A . n 
A 1 1012 GLY 1012 1023 1023 GLY GLY A . n 
A 1 1013 TYR 1013 1024 1024 TYR TYR A . n 
A 1 1014 TYR 1014 1025 1025 TYR TYR A . n 
A 1 1015 SER 1015 1026 1026 SER SER A . n 
A 1 1016 PRO 1016 1027 1027 PRO PRO A . n 
A 1 1017 GLN 1017 1028 1028 GLN GLN A . n 
A 1 1018 GLU 1018 1029 1029 GLU GLU A . n 
A 1 1019 TYR 1019 1030 1030 TYR TYR A . n 
A 1 1020 LEU 1020 1031 1031 LEU LEU A . n 
A 1 1021 SER 1021 1032 1032 SER SER A . n 
A 1 1022 PHE 1022 1033 1033 PHE PHE A . n 
A 1 1023 ALA 1023 1034 1034 ALA ALA A . n 
A 1 1024 ILE 1024 1035 1035 ILE ILE A . n 
A 1 1025 PRO 1025 1036 1036 PRO PRO A . n 
A 1 1026 VAL 1026 1037 1037 VAL VAL A . n 
A 1 1027 MET 1027 1038 1038 MET MET A . n 
A 1 1028 TRP 1028 1039 1039 TRP TRP A . n 
A 1 1029 ARG 1029 1040 1040 ARG ARG A . n 
A 1 1030 GLU 1030 1041 1041 GLU GLU A . n 
A 1 1031 ARG 1031 1042 1042 ARG ARG A . n 
A 1 1032 THR 1032 1043 1043 THR THR A . n 
A 1 1033 GLU 1033 1044 1044 GLU GLU A . n 
A 1 1034 ASN 1034 1045 1045 ASN ASN A . n 
A 1 1035 TRP 1035 1046 1046 TRP TRP A . n 
A 1 1036 SER 1036 1047 1047 SER SER A . n 
A 1 1037 TRP 1037 1048 1048 TRP TRP A . n 
A 1 1038 GLU 1038 1049 1049 GLU GLU A . n 
A 1 1039 LEU 1039 1050 1050 LEU LEU A . n 
A 1 1040 GLY 1040 1051 1051 GLY GLY A . n 
A 1 1041 ALA 1041 1052 1052 ALA ALA A . n 
A 1 1042 SER 1042 1053 1053 SER SER A . n 
A 1 1043 GLY 1043 1054 1054 GLY GLY A . n 
A 1 1044 SER 1044 1055 1055 SER SER A . n 
A 1 1045 TRP 1045 1056 1056 TRP TRP A . n 
A 1 1046 SER 1046 1057 1057 SER SER A . n 
A 1 1047 HIS 1047 1058 1058 HIS HIS A . n 
A 1 1048 SER 1048 1059 1059 SER SER A . n 
A 1 1049 ARG 1049 1060 1060 ARG ARG A . n 
A 1 1050 THR 1050 1061 1061 THR THR A . n 
A 1 1051 LYS 1051 1062 1062 LYS LYS A . n 
A 1 1052 THR 1052 1063 1063 THR THR A . n 
A 1 1053 MET 1053 1064 1064 MET MET A . n 
A 1 1054 PRO 1054 1065 1065 PRO PRO A . n 
A 1 1055 ARG 1055 1066 1066 ARG ARG A . n 
A 1 1056 TYR 1056 1067 1067 TYR TYR A . n 
A 1 1057 PRO 1057 1068 1068 PRO PRO A . n 
A 1 1058 LEU 1058 1069 1069 LEU LEU A . n 
A 1 1059 MET 1059 1070 1070 MET MET A . n 
A 1 1060 ASN 1060 1071 1071 ASN ASN A . n 
A 1 1061 LEU 1061 1072 1072 LEU LEU A . n 
A 1 1062 ILE 1062 1073 1073 ILE ILE A . n 
A 1 1063 PRO 1063 1074 1074 PRO PRO A . n 
A 1 1064 THR 1064 1075 1075 THR THR A . n 
A 1 1065 ASP 1065 1076 1076 ASP ASP A . n 
A 1 1066 TRP 1066 1077 1077 TRP TRP A . n 
A 1 1067 GLN 1067 1078 1078 GLN GLN A . n 
A 1 1068 GLU 1068 1079 1079 GLU GLU A . n 
A 1 1069 GLU 1069 1080 1080 GLU GLU A . n 
A 1 1070 ALA 1070 1081 1081 ALA ALA A . n 
A 1 1071 ALA 1071 1082 1082 ALA ALA A . n 
A 1 1072 ARG 1072 1083 1083 ARG ARG A . n 
A 1 1073 GLN 1073 1084 1084 GLN GLN A . n 
A 1 1074 SER 1074 1085 1085 SER SER A . n 
A 1 1075 ASN 1075 1086 1086 ASN ASN A . n 
A 1 1076 ASP 1076 1087 1087 ASP ASP A . n 
A 1 1077 GLY 1077 1088 1088 GLY GLY A . n 
A 1 1078 GLY 1078 1089 1089 GLY GLY A . n 
A 1 1079 SER 1079 1090 1090 SER SER A . n 
A 1 1080 SER 1080 1091 1091 SER SER A . n 
A 1 1081 GLN 1081 1092 1092 GLN GLN A . n 
A 1 1082 GLY 1082 1093 1093 GLY GLY A . n 
A 1 1083 PHE 1083 1094 1094 PHE PHE A . n 
A 1 1084 GLY 1084 1095 1095 GLY GLY A . n 
A 1 1085 TYR 1085 1096 1096 TYR TYR A . n 
A 1 1086 THR 1086 1097 1097 THR THR A . n 
A 1 1087 ALA 1087 1098 1098 ALA ALA A . n 
A 1 1088 ARG 1088 1099 1099 ARG ARG A . n 
A 1 1089 ALA 1089 1100 1100 ALA ALA A . n 
A 1 1090 LEU 1090 1101 1101 LEU LEU A . n 
A 1 1091 LEU 1091 1102 1102 LEU LEU A . n 
A 1 1092 GLU 1092 1103 1103 GLU GLU A . n 
A 1 1093 ARG 1093 1104 1104 ARG ARG A . n 
A 1 1094 ARG 1094 1105 1105 ARG ARG A . n 
A 1 1095 VAL 1095 1106 1106 VAL VAL A . n 
A 1 1096 THR 1096 1107 1107 THR THR A . n 
A 1 1097 SER 1097 1108 1108 SER SER A . n 
A 1 1098 ASN 1098 1109 1109 ASN ASN A . n 
A 1 1099 TRP 1099 1110 1110 TRP TRP A . n 
A 1 1100 PHE 1100 1111 1111 PHE PHE A . n 
A 1 1101 VAL 1101 1112 1112 VAL VAL A . n 
A 1 1102 GLY 1102 1113 1113 GLY GLY A . n 
A 1 1103 THR 1103 1114 1114 THR THR A . n 
A 1 1104 ALA 1104 1115 1115 ALA ALA A . n 
A 1 1105 ILE 1105 1116 1116 ILE ILE A . n 
A 1 1106 ASP 1106 1117 1117 ASP ASP A . n 
A 1 1107 ILE 1107 1118 1118 ILE ILE A . n 
A 1 1108 GLN 1108 1119 1119 GLN GLN A . n 
A 1 1109 GLN 1109 1120 1120 GLN GLN A . n 
A 1 1110 ALA 1110 1121 1121 ALA ALA A . n 
A 1 1111 LYS 1111 1122 1122 LYS LYS A . n 
A 1 1112 ASP 1112 1123 1123 ASP ASP A . n 
A 1 1113 TYR 1113 1124 1124 TYR TYR A . n 
A 1 1114 ALA 1114 1125 1125 ALA ALA A . n 
A 1 1115 PRO 1115 1126 1126 PRO PRO A . n 
A 1 1116 SER 1116 1127 1127 SER SER A . n 
A 1 1117 HIS 1117 1128 1128 HIS HIS A . n 
A 1 1118 PHE 1118 1129 1129 PHE PHE A . n 
A 1 1119 LEU 1119 1130 1130 LEU LEU A . n 
A 1 1120 LEU 1120 1131 1131 LEU LEU A . n 
A 1 1121 TYR 1121 1132 1132 TYR TYR A . n 
A 1 1122 VAL 1122 1133 1133 VAL VAL A . n 
A 1 1123 ARG 1123 1134 1134 ARG ARG A . n 
A 1 1124 TYR 1124 1135 1135 TYR TYR A . n 
A 1 1125 SER 1125 1136 1136 SER SER A . n 
A 1 1126 ALA 1126 1137 1137 ALA ALA A . n 
A 1 1127 ALA 1127 1138 1138 ALA ALA A . n 
A 1 1128 GLY 1128 1139 1139 GLY GLY A . n 
A 1 1129 TRP 1129 1140 1140 TRP TRP A . n 
A 1 1130 GLN 1130 1141 1141 GLN GLN A . n 
A 1 1131 GLY 1131 1142 1142 GLY GLY A . n 
A 1 1132 ASP 1132 1143 1143 ASP ASP A . n 
A 1 1133 MET 1133 1144 1144 MET MET A . n 
A 1 1134 ASP 1134 1145 1145 ASP ASP A . n 
A 1 1135 LEU 1135 1146 1146 LEU LEU A . n 
A 1 1136 PRO 1136 1147 1147 PRO PRO A . n 
A 1 1137 PRO 1137 1148 1148 PRO PRO A . n 
A 1 1138 GLN 1138 1149 1149 GLN GLN A . n 
A 1 1139 PRO 1139 1150 1150 PRO PRO A . n 
A 1 1140 LEU 1140 1151 1151 LEU LEU A . n 
A 1 1141 ILE 1141 1152 1152 ILE ILE A . n 
A 1 1142 PRO 1142 1153 1153 PRO PRO A . n 
A 1 1143 TYR 1143 1154 1154 TYR TYR A . n 
A 1 1144 ALA 1144 1155 1155 ALA ALA A . n 
A 1 1145 ASP 1145 1156 1156 ASP ASP A . n 
A 1 1146 TRP 1146 1157 1157 TRP TRP A . n 
# 
_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                     9B8A 
_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                         9B8A 
_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                   9B8A 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9B8A 
_struct.title                        'Cryo-EM structure of E. coli cellulose synthase subunit C' 
_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        9B8A 
_struct_keywords.text            
'Porin, bacterial outer membrane protein, Tetra-tricopeptide (TPR) repeats, Cellulose exporter BcsC, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
_struct_asym.id                            A 
_struct_asym.pdbx_blank_PDB_chainid_flag   N 
_struct_asym.pdbx_modified                 N 
_struct_asym.entity_id                     1 
_struct_asym.details                       ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    BCSC_ECOLI 
_struct_ref.pdbx_db_accession          P37650 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VEAAPTAQQQLLEQVRLGEATHREDLVQQSLYRLELIDPNNPDVVAARFRSLLRQGDIDGAQKQLDRLSQLAPSSNAYKS
SRTTMLLSTPDGRQALQQARLQATTGHAEEAVASYNKLFNGAPPEGDIAVEYWSTVAKIPARRGEAINQLKRINADAPGN
TGLQNNLALLLFSSDRRDEGFAVLEQMAKSNAGREGASKIWYGQIKDMPVSDASVSALKKYLSIFSDGDSVAAAQSQLAE
QQKQLADPAFRARAQGLAAVDSGMAGKAIPELQQAVRANPKDSEALGALGQAYSQKGDRANAVANLEKALALDPHSSNND
KWNSLLKVNRYWLAIQQGDAALKANNPDRAERLFQQARNVDNTDSYAVLGLGDVAMARKDYPAAERYYQQTLRMDSGNTN
AVRGLANIYRQQSPEKAEAFIASLSASQRRSIDDIERSLQNDRLAQQAEALENQGKWAQAAALQRQRLALDPGSVWITYR
LSQDLWQAGQRSQADTLMRNLAQQKSNDPEQVYAYGLYLSGHDQDRAALAHINSLPRAQWNSNIQELVNRLQSDQVLETA
NRLRESGKEAEAEAMLRQQPPSTRIDLTLADWAQQRRDYTAARAAYQNVLTREPANADAILGLTEVDIAAGDKAAARSQL
AKLPATDNASLNTQRRVALAQAQLGDTAAAQRTFNKLIPQAKSQPPSMESAMVLRDGAKFEAQAGDPTQALETYKDAMVA
SGVTTTRPQDNDTFTRLTRNDEKDDWLKRGVRSDAADLYRQQDLNVTLEHDYWGSSGTGGYSDLKAHTTMLQVDAPYSDG
RMFFRSDFVNMNVGSFSTNADGKWDDNWGTCTLQDCSGNRSQSDSGASVAVGWRNDVWSWDIGTTPMGFNVVDVVGGISY
SDDIGPLGYTVNAHRRPISSSLLAFGGQKDSPSNTGKKWGGVRADGVGLSLSYDKGEANGVWASLSGDQLTGKNVEDNWR
VRWMTGYYYKVINQNNRRVTIGLNNMIWHYDKDLSGYSLGQGGYYSPQEYLSFAIPVMWRERTENWSWELGASGSWSHSR
TKTMPRYPLMNLIPTDWQEEAARQSNDGGSSQGFGYTARALLERRVTSNWFVGTAIDIQQAKDYAPSHFLLYVRYSAAGW
QGDMDLPPQPLIPYADW
;
_struct_ref.pdbx_align_begin           21 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9B8A 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 10 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 1146 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P37650 
_struct_ref_seq.db_align_beg                  21 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1157 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       21 
_struct_ref_seq.pdbx_auth_seq_align_end       1157 
# 
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 9B8A MET A 1 ? UNP P37650 ? ? 'expression tag' 12 1 
1 9B8A HIS A 2 ? UNP P37650 ? ? 'expression tag' 13 2 
1 9B8A HIS A 3 ? UNP P37650 ? ? 'expression tag' 14 3 
1 9B8A HIS A 4 ? UNP P37650 ? ? 'expression tag' 15 4 
1 9B8A HIS A 5 ? UNP P37650 ? ? 'expression tag' 16 5 
1 9B8A HIS A 6 ? UNP P37650 ? ? 'expression tag' 17 6 
1 9B8A HIS A 7 ? UNP P37650 ? ? 'expression tag' 18 7 
1 9B8A HIS A 8 ? UNP P37650 ? ? 'expression tag' 19 8 
1 9B8A HIS A 9 ? UNP P37650 ? ? 'expression tag' 20 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 591  ? GLN A 604  ? SER A 602  GLN A 615  1 ? 14 
HELX_P HELX_P2  AA2 TYR A 608  ? GLU A 622  ? TYR A 619  GLU A 633  1 ? 15 
HELX_P HELX_P3  AA3 ASN A 625  ? ALA A 639  ? ASN A 636  ALA A 650  1 ? 15 
HELX_P HELX_P4  AA4 ASP A 641  ? ALA A 650  ? ASP A 652  ALA A 661  1 ? 10 
HELX_P HELX_P5  AA5 SER A 659  ? LEU A 673  ? SER A 670  LEU A 684  1 ? 15 
HELX_P HELX_P6  AA6 ASP A 675  ? GLN A 693  ? ASP A 686  GLN A 704  1 ? 19 
HELX_P HELX_P7  AA7 SER A 696  ? GLY A 714  ? SER A 707  GLY A 725  1 ? 19 
HELX_P HELX_P8  AA8 ASP A 715  ? SER A 730  ? ASP A 726  SER A 741  1 ? 16 
HELX_P HELX_P9  AA9 ASP A 739  ? LEU A 746  ? ASP A 750  LEU A 757  1 ? 8  
HELX_P HELX_P10 AB1 ASP A 754  ? GLN A 771  ? ASP A 765  GLN A 782  1 ? 18 
HELX_P HELX_P11 AB2 SER A 910  ? GLY A 915  ? SER A 921  GLY A 926  1 ? 6  
HELX_P HELX_P12 AB3 LEU A 1058 ? ILE A 1062 ? LEU A 1069 ILE A 1073 5 ? 5  
HELX_P HELX_P13 AB4 TRP A 1066 ? ALA A 1071 ? TRP A 1077 ALA A 1082 1 ? 6  
HELX_P HELX_P14 AB5 PRO A 1142 ? TRP A 1146 ? PRO A 1153 TRP A 1157 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            840 
_struct_conn.ptnr1_label_atom_id           SG 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           A 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            845 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             851 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             856 
_struct_conn.ptnr2_symmetry                1_555 
_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               2.030 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       840 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      845 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        851 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       856 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          LEU 
_struct_mon_prot_cis.label_seq_id           1135 
_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           LEU 
_struct_mon_prot_cis.auth_seq_id            1146 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    1136 
_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     1147 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       3.77 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 18 ? 
AA2 ? 2  ? 
AA3 ? 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  ? anti-parallel 
AA1 6  7  ? anti-parallel 
AA1 7  8  ? anti-parallel 
AA1 8  9  ? anti-parallel 
AA1 9  10 ? anti-parallel 
AA1 10 11 ? anti-parallel 
AA1 11 12 ? anti-parallel 
AA1 12 13 ? anti-parallel 
AA1 13 14 ? anti-parallel 
AA1 14 15 ? anti-parallel 
AA1 15 16 ? anti-parallel 
AA1 16 17 ? anti-parallel 
AA1 17 18 ? anti-parallel 
AA2 1  2  ? parallel      
AA3 1  2  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  GLN A 917  ? LYS A 918  ? GLN A 928  LYS A 929  
AA1 2  LYS A 927  ? TYR A 942  ? LYS A 938  TYR A 953  
AA1 3  ASN A 948  ? LYS A 962  ? ASN A 959  LYS A 973  
AA1 4  VAL A 964  ? GLN A 983  ? VAL A 975  GLN A 994  
AA1 5  ARG A 986  ? TYR A 999  ? ARG A 997  TYR A 1010 
AA1 6  GLU A 1018 ? ARG A 1031 ? GLU A 1029 ARG A 1042 
AA1 7  TRP A 1035 ? THR A 1050 ? TRP A 1046 THR A 1061 
AA1 8  GLY A 1078 ? THR A 1096 ? GLY A 1089 THR A 1107 
AA1 9  TRP A 1099 ? GLN A 1109 ? TRP A 1110 GLN A 1120 
AA1 10 SER A 1116 ? SER A 1125 ? SER A 1127 SER A 1136 
AA1 11 ASN A 774  ? SER A 784  ? ASN A 785  SER A 795  
AA1 12 LEU A 793  ? TYR A 806  ? LEU A 804  TYR A 817  
AA1 13 GLY A 809  ? SER A 824  ? GLY A 820  SER A 835  
AA1 14 SER A 850  ? ARG A 863  ? SER A 861  ARG A 874  
AA1 15 TRP A 867  ? THR A 873  ? TRP A 878  THR A 884  
AA1 16 VAL A 883  ? ILE A 893  ? VAL A 894  ILE A 904  
AA1 17 LEU A 896  ? PRO A 906  ? LEU A 907  PRO A 917  
AA1 18 LYS A 927  ? TYR A 942  ? LYS A 938  TYR A 953  
AA2 1  TRP A 837  ? GLY A 838  ? TRP A 848  GLY A 849  
AA2 2  TYR A 1006 ? SER A 1007 ? TYR A 1017 SER A 1018 
AA3 1  MET A 1053 ? PRO A 1054 ? MET A 1064 PRO A 1065 
AA3 2  SER A 1074 ? ASN A 1075 ? SER A 1085 ASN A 1086 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N GLN A 917  ? N GLN A 928  O TRP A 928  ? O TRP A 939  
AA1 2  3  N TYR A 942  ? N TYR A 953  O VAL A 950  ? O VAL A 961  
AA1 3  4  N SER A 953  ? N SER A 964  O MET A 973  ? O MET A 984  
AA1 4  5  N TRP A 972  ? N TRP A 983  O ILE A 996  ? O ILE A 1007 
AA1 5  6  N ASN A 993  ? N ASN A 1004 O ALA A 1023 ? O ALA A 1034 
AA1 6  7  N GLU A 1030 ? N GLU A 1041 O TRP A 1037 ? O TRP A 1048 
AA1 7  8  N SER A 1046 ? N SER A 1057 O GLY A 1082 ? O GLY A 1093 
AA1 8  9  N ARG A 1093 ? N ARG A 1104 O VAL A 1101 ? O VAL A 1112 
AA1 9  10 N ASP A 1106 ? N ASP A 1117 O HIS A 1117 ? O HIS A 1128 
AA1 10 11 O SER A 1116 ? O SER A 1127 N GLY A 783  ? N GLY A 794  
AA1 11 12 N TRP A 782  ? N TRP A 793  O ALA A 795  ? O ALA A 806  
AA1 12 13 N TYR A 806  ? N TYR A 817  O GLY A 809  ? O GLY A 820  
AA1 13 14 N MET A 820  ? N MET A 831  O ASP A 853  ? O ASP A 864  
AA1 14 15 N VAL A 860  ? N VAL A 871  O ILE A 871  ? O ILE A 882  
AA1 15 16 N GLY A 872  ? N GLY A 883  O VAL A 884  ? O VAL A 895  
AA1 16 17 N GLY A 885  ? N GLY A 896  O ARG A 904  ? O ARG A 915  
AA1 17 18 N ARG A 905  ? N ARG A 916  O ALA A 933  ? O ALA A 944  
AA2 1  2  N GLY A 838  ? N GLY A 849  O TYR A 1006 ? O TYR A 1017 
AA3 1  2  N MET A 1053 ? N MET A 1064 O ASN A 1075 ? O ASN A 1086 
# 
_pdbx_entry_details.entry_id                   9B8A 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 THR A 666  ? ? -91.90  30.58   
2 1 TYR A 817  ? ? -161.49 119.68  
3 1 SER A 818  ? ? 54.99   -141.56 
4 1 VAL A 877  ? ? -120.20 -57.03  
5 1 ASN A 934  ? ? -94.40  -65.32  
6 1 SER A 1026 ? ? -156.41 79.61   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9B8A 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9B8A 
_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                  3.4 
_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               99373 
_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            8.5 
# 
_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                 'Bacterial cellulose synthase subunit C in nanodisc' 
_em_entity_assembly.details              
;Protein
- Bacterial cellulose synthase subunit C (BcsC)
;
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9B8A 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN 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             1200 
_em_imaging.nominal_defocus_max             2200 
_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              9B8A 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9B8A 
_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 A MET 12  ? A MET 1   
2   1 Y 1 A HIS 13  ? A HIS 2   
3   1 Y 1 A HIS 14  ? A HIS 3   
4   1 Y 1 A HIS 15  ? A HIS 4   
5   1 Y 1 A HIS 16  ? A HIS 5   
6   1 Y 1 A HIS 17  ? A HIS 6   
7   1 Y 1 A HIS 18  ? A HIS 7   
8   1 Y 1 A HIS 19  ? A HIS 8   
9   1 Y 1 A HIS 20  ? A HIS 9   
10  1 Y 1 A VAL 21  ? A VAL 10  
11  1 Y 1 A GLU 22  ? A GLU 11  
12  1 Y 1 A ALA 23  ? A ALA 12  
13  1 Y 1 A ALA 24  ? A ALA 13  
14  1 Y 1 A PRO 25  ? A PRO 14  
15  1 Y 1 A THR 26  ? A THR 15  
16  1 Y 1 A ALA 27  ? A ALA 16  
17  1 Y 1 A GLN 28  ? A GLN 17  
18  1 Y 1 A GLN 29  ? A GLN 18  
19  1 Y 1 A GLN 30  ? A GLN 19  
20  1 Y 1 A LEU 31  ? A LEU 20  
21  1 Y 1 A LEU 32  ? A LEU 21  
22  1 Y 1 A GLU 33  ? A GLU 22  
23  1 Y 1 A GLN 34  ? A GLN 23  
24  1 Y 1 A VAL 35  ? A VAL 24  
25  1 Y 1 A ARG 36  ? A ARG 25  
26  1 Y 1 A LEU 37  ? A LEU 26  
27  1 Y 1 A GLY 38  ? A GLY 27  
28  1 Y 1 A GLU 39  ? A GLU 28  
29  1 Y 1 A ALA 40  ? A ALA 29  
30  1 Y 1 A THR 41  ? A THR 30  
31  1 Y 1 A HIS 42  ? A HIS 31  
32  1 Y 1 A ARG 43  ? A ARG 32  
33  1 Y 1 A GLU 44  ? A GLU 33  
34  1 Y 1 A ASP 45  ? A ASP 34  
35  1 Y 1 A LEU 46  ? A LEU 35  
36  1 Y 1 A VAL 47  ? A VAL 36  
37  1 Y 1 A GLN 48  ? A GLN 37  
38  1 Y 1 A GLN 49  ? A GLN 38  
39  1 Y 1 A SER 50  ? A SER 39  
40  1 Y 1 A LEU 51  ? A LEU 40  
41  1 Y 1 A TYR 52  ? A TYR 41  
42  1 Y 1 A ARG 53  ? A ARG 42  
43  1 Y 1 A LEU 54  ? A LEU 43  
44  1 Y 1 A GLU 55  ? A GLU 44  
45  1 Y 1 A LEU 56  ? A LEU 45  
46  1 Y 1 A ILE 57  ? A ILE 46  
47  1 Y 1 A ASP 58  ? A ASP 47  
48  1 Y 1 A PRO 59  ? A PRO 48  
49  1 Y 1 A ASN 60  ? A ASN 49  
50  1 Y 1 A ASN 61  ? A ASN 50  
51  1 Y 1 A PRO 62  ? A PRO 51  
52  1 Y 1 A ASP 63  ? A ASP 52  
53  1 Y 1 A VAL 64  ? A VAL 53  
54  1 Y 1 A VAL 65  ? A VAL 54  
55  1 Y 1 A ALA 66  ? A ALA 55  
56  1 Y 1 A ALA 67  ? A ALA 56  
57  1 Y 1 A ARG 68  ? A ARG 57  
58  1 Y 1 A PHE 69  ? A PHE 58  
59  1 Y 1 A ARG 70  ? A ARG 59  
60  1 Y 1 A SER 71  ? A SER 60  
61  1 Y 1 A LEU 72  ? A LEU 61  
62  1 Y 1 A LEU 73  ? A LEU 62  
63  1 Y 1 A ARG 74  ? A ARG 63  
64  1 Y 1 A GLN 75  ? A GLN 64  
65  1 Y 1 A GLY 76  ? A GLY 65  
66  1 Y 1 A ASP 77  ? A ASP 66  
67  1 Y 1 A ILE 78  ? A ILE 67  
68  1 Y 1 A ASP 79  ? A ASP 68  
69  1 Y 1 A GLY 80  ? A GLY 69  
70  1 Y 1 A ALA 81  ? A ALA 70  
71  1 Y 1 A GLN 82  ? A GLN 71  
72  1 Y 1 A LYS 83  ? A LYS 72  
73  1 Y 1 A GLN 84  ? A GLN 73  
74  1 Y 1 A LEU 85  ? A LEU 74  
75  1 Y 1 A ASP 86  ? A ASP 75  
76  1 Y 1 A ARG 87  ? A ARG 76  
77  1 Y 1 A LEU 88  ? A LEU 77  
78  1 Y 1 A SER 89  ? A SER 78  
79  1 Y 1 A GLN 90  ? A GLN 79  
80  1 Y 1 A LEU 91  ? A LEU 80  
81  1 Y 1 A ALA 92  ? A ALA 81  
82  1 Y 1 A PRO 93  ? A PRO 82  
83  1 Y 1 A SER 94  ? A SER 83  
84  1 Y 1 A SER 95  ? A SER 84  
85  1 Y 1 A ASN 96  ? A ASN 85  
86  1 Y 1 A ALA 97  ? A ALA 86  
87  1 Y 1 A TYR 98  ? A TYR 87  
88  1 Y 1 A LYS 99  ? A LYS 88  
89  1 Y 1 A SER 100 ? A SER 89  
90  1 Y 1 A SER 101 ? A SER 90  
91  1 Y 1 A ARG 102 ? A ARG 91  
92  1 Y 1 A THR 103 ? A THR 92  
93  1 Y 1 A THR 104 ? A THR 93  
94  1 Y 1 A MET 105 ? A MET 94  
95  1 Y 1 A LEU 106 ? A LEU 95  
96  1 Y 1 A LEU 107 ? A LEU 96  
97  1 Y 1 A SER 108 ? A SER 97  
98  1 Y 1 A THR 109 ? A THR 98  
99  1 Y 1 A PRO 110 ? A PRO 99  
100 1 Y 1 A ASP 111 ? A ASP 100 
101 1 Y 1 A GLY 112 ? A GLY 101 
102 1 Y 1 A ARG 113 ? A ARG 102 
103 1 Y 1 A GLN 114 ? A GLN 103 
104 1 Y 1 A ALA 115 ? A ALA 104 
105 1 Y 1 A LEU 116 ? A LEU 105 
106 1 Y 1 A GLN 117 ? A GLN 106 
107 1 Y 1 A GLN 118 ? A GLN 107 
108 1 Y 1 A ALA 119 ? A ALA 108 
109 1 Y 1 A ARG 120 ? A ARG 109 
110 1 Y 1 A LEU 121 ? A LEU 110 
111 1 Y 1 A GLN 122 ? A GLN 111 
112 1 Y 1 A ALA 123 ? A ALA 112 
113 1 Y 1 A THR 124 ? A THR 113 
114 1 Y 1 A THR 125 ? A THR 114 
115 1 Y 1 A GLY 126 ? A GLY 115 
116 1 Y 1 A HIS 127 ? A HIS 116 
117 1 Y 1 A ALA 128 ? A ALA 117 
118 1 Y 1 A GLU 129 ? A GLU 118 
119 1 Y 1 A GLU 130 ? A GLU 119 
120 1 Y 1 A ALA 131 ? A ALA 120 
121 1 Y 1 A VAL 132 ? A VAL 121 
122 1 Y 1 A ALA 133 ? A ALA 122 
123 1 Y 1 A SER 134 ? A SER 123 
124 1 Y 1 A TYR 135 ? A TYR 124 
125 1 Y 1 A ASN 136 ? A ASN 125 
126 1 Y 1 A LYS 137 ? A LYS 126 
127 1 Y 1 A LEU 138 ? A LEU 127 
128 1 Y 1 A PHE 139 ? A PHE 128 
129 1 Y 1 A ASN 140 ? A ASN 129 
130 1 Y 1 A GLY 141 ? A GLY 130 
131 1 Y 1 A ALA 142 ? A ALA 131 
132 1 Y 1 A PRO 143 ? A PRO 132 
133 1 Y 1 A PRO 144 ? A PRO 133 
134 1 Y 1 A GLU 145 ? A GLU 134 
135 1 Y 1 A GLY 146 ? A GLY 135 
136 1 Y 1 A ASP 147 ? A ASP 136 
137 1 Y 1 A ILE 148 ? A ILE 137 
138 1 Y 1 A ALA 149 ? A ALA 138 
139 1 Y 1 A VAL 150 ? A VAL 139 
140 1 Y 1 A GLU 151 ? A GLU 140 
141 1 Y 1 A TYR 152 ? A TYR 141 
142 1 Y 1 A TRP 153 ? A TRP 142 
143 1 Y 1 A SER 154 ? A SER 143 
144 1 Y 1 A THR 155 ? A THR 144 
145 1 Y 1 A VAL 156 ? A VAL 145 
146 1 Y 1 A ALA 157 ? A ALA 146 
147 1 Y 1 A LYS 158 ? A LYS 147 
148 1 Y 1 A ILE 159 ? A ILE 148 
149 1 Y 1 A PRO 160 ? A PRO 149 
150 1 Y 1 A ALA 161 ? A ALA 150 
151 1 Y 1 A ARG 162 ? A ARG 151 
152 1 Y 1 A ARG 163 ? A ARG 152 
153 1 Y 1 A GLY 164 ? A GLY 153 
154 1 Y 1 A GLU 165 ? A GLU 154 
155 1 Y 1 A ALA 166 ? A ALA 155 
156 1 Y 1 A ILE 167 ? A ILE 156 
157 1 Y 1 A ASN 168 ? A ASN 157 
158 1 Y 1 A GLN 169 ? A GLN 158 
159 1 Y 1 A LEU 170 ? A LEU 159 
160 1 Y 1 A LYS 171 ? A LYS 160 
161 1 Y 1 A ARG 172 ? A ARG 161 
162 1 Y 1 A ILE 173 ? A ILE 162 
163 1 Y 1 A ASN 174 ? A ASN 163 
164 1 Y 1 A ALA 175 ? A ALA 164 
165 1 Y 1 A ASP 176 ? A ASP 165 
166 1 Y 1 A ALA 177 ? A ALA 166 
167 1 Y 1 A PRO 178 ? A PRO 167 
168 1 Y 1 A GLY 179 ? A GLY 168 
169 1 Y 1 A ASN 180 ? A ASN 169 
170 1 Y 1 A THR 181 ? A THR 170 
171 1 Y 1 A GLY 182 ? A GLY 171 
172 1 Y 1 A LEU 183 ? A LEU 172 
173 1 Y 1 A GLN 184 ? A GLN 173 
174 1 Y 1 A ASN 185 ? A ASN 174 
175 1 Y 1 A ASN 186 ? A ASN 175 
176 1 Y 1 A LEU 187 ? A LEU 176 
177 1 Y 1 A ALA 188 ? A ALA 177 
178 1 Y 1 A LEU 189 ? A LEU 178 
179 1 Y 1 A LEU 190 ? A LEU 179 
180 1 Y 1 A LEU 191 ? A LEU 180 
181 1 Y 1 A PHE 192 ? A PHE 181 
182 1 Y 1 A SER 193 ? A SER 182 
183 1 Y 1 A SER 194 ? A SER 183 
184 1 Y 1 A ASP 195 ? A ASP 184 
185 1 Y 1 A ARG 196 ? A ARG 185 
186 1 Y 1 A ARG 197 ? A ARG 186 
187 1 Y 1 A ASP 198 ? A ASP 187 
188 1 Y 1 A GLU 199 ? A GLU 188 
189 1 Y 1 A GLY 200 ? A GLY 189 
190 1 Y 1 A PHE 201 ? A PHE 190 
191 1 Y 1 A ALA 202 ? A ALA 191 
192 1 Y 1 A VAL 203 ? A VAL 192 
193 1 Y 1 A LEU 204 ? A LEU 193 
194 1 Y 1 A GLU 205 ? A GLU 194 
195 1 Y 1 A GLN 206 ? A GLN 195 
196 1 Y 1 A MET 207 ? A MET 196 
197 1 Y 1 A ALA 208 ? A ALA 197 
198 1 Y 1 A LYS 209 ? A LYS 198 
199 1 Y 1 A SER 210 ? A SER 199 
200 1 Y 1 A ASN 211 ? A ASN 200 
201 1 Y 1 A ALA 212 ? A ALA 201 
202 1 Y 1 A GLY 213 ? A GLY 202 
203 1 Y 1 A ARG 214 ? A ARG 203 
204 1 Y 1 A GLU 215 ? A GLU 204 
205 1 Y 1 A GLY 216 ? A GLY 205 
206 1 Y 1 A ALA 217 ? A ALA 206 
207 1 Y 1 A SER 218 ? A SER 207 
208 1 Y 1 A LYS 219 ? A LYS 208 
209 1 Y 1 A ILE 220 ? A ILE 209 
210 1 Y 1 A TRP 221 ? A TRP 210 
211 1 Y 1 A TYR 222 ? A TYR 211 
212 1 Y 1 A GLY 223 ? A GLY 212 
213 1 Y 1 A GLN 224 ? A GLN 213 
214 1 Y 1 A ILE 225 ? A ILE 214 
215 1 Y 1 A LYS 226 ? A LYS 215 
216 1 Y 1 A ASP 227 ? A ASP 216 
217 1 Y 1 A MET 228 ? A MET 217 
218 1 Y 1 A PRO 229 ? A PRO 218 
219 1 Y 1 A VAL 230 ? A VAL 219 
220 1 Y 1 A SER 231 ? A SER 220 
221 1 Y 1 A ASP 232 ? A ASP 221 
222 1 Y 1 A ALA 233 ? A ALA 222 
223 1 Y 1 A SER 234 ? A SER 223 
224 1 Y 1 A VAL 235 ? A VAL 224 
225 1 Y 1 A SER 236 ? A SER 225 
226 1 Y 1 A ALA 237 ? A ALA 226 
227 1 Y 1 A LEU 238 ? A LEU 227 
228 1 Y 1 A LYS 239 ? A LYS 228 
229 1 Y 1 A LYS 240 ? A LYS 229 
230 1 Y 1 A TYR 241 ? A TYR 230 
231 1 Y 1 A LEU 242 ? A LEU 231 
232 1 Y 1 A SER 243 ? A SER 232 
233 1 Y 1 A ILE 244 ? A ILE 233 
234 1 Y 1 A PHE 245 ? A PHE 234 
235 1 Y 1 A SER 246 ? A SER 235 
236 1 Y 1 A ASP 247 ? A ASP 236 
237 1 Y 1 A GLY 248 ? A GLY 237 
238 1 Y 1 A ASP 249 ? A ASP 238 
239 1 Y 1 A SER 250 ? A SER 239 
240 1 Y 1 A VAL 251 ? A VAL 240 
241 1 Y 1 A ALA 252 ? A ALA 241 
242 1 Y 1 A ALA 253 ? A ALA 242 
243 1 Y 1 A ALA 254 ? A ALA 243 
244 1 Y 1 A GLN 255 ? A GLN 244 
245 1 Y 1 A SER 256 ? A SER 245 
246 1 Y 1 A GLN 257 ? A GLN 246 
247 1 Y 1 A LEU 258 ? A LEU 247 
248 1 Y 1 A ALA 259 ? A ALA 248 
249 1 Y 1 A GLU 260 ? A GLU 249 
250 1 Y 1 A GLN 261 ? A GLN 250 
251 1 Y 1 A GLN 262 ? A GLN 251 
252 1 Y 1 A LYS 263 ? A LYS 252 
253 1 Y 1 A GLN 264 ? A GLN 253 
254 1 Y 1 A LEU 265 ? A LEU 254 
255 1 Y 1 A ALA 266 ? A ALA 255 
256 1 Y 1 A ASP 267 ? A ASP 256 
257 1 Y 1 A PRO 268 ? A PRO 257 
258 1 Y 1 A ALA 269 ? A ALA 258 
259 1 Y 1 A PHE 270 ? A PHE 259 
260 1 Y 1 A ARG 271 ? A ARG 260 
261 1 Y 1 A ALA 272 ? A ALA 261 
262 1 Y 1 A ARG 273 ? A ARG 262 
263 1 Y 1 A ALA 274 ? A ALA 263 
264 1 Y 1 A GLN 275 ? A GLN 264 
265 1 Y 1 A GLY 276 ? A GLY 265 
266 1 Y 1 A LEU 277 ? A LEU 266 
267 1 Y 1 A ALA 278 ? A ALA 267 
268 1 Y 1 A ALA 279 ? A ALA 268 
269 1 Y 1 A VAL 280 ? A VAL 269 
270 1 Y 1 A ASP 281 ? A ASP 270 
271 1 Y 1 A SER 282 ? A SER 271 
272 1 Y 1 A GLY 283 ? A GLY 272 
273 1 Y 1 A MET 284 ? A MET 273 
274 1 Y 1 A ALA 285 ? A ALA 274 
275 1 Y 1 A GLY 286 ? A GLY 275 
276 1 Y 1 A LYS 287 ? A LYS 276 
277 1 Y 1 A ALA 288 ? A ALA 277 
278 1 Y 1 A ILE 289 ? A ILE 278 
279 1 Y 1 A PRO 290 ? A PRO 279 
280 1 Y 1 A GLU 291 ? A GLU 280 
281 1 Y 1 A LEU 292 ? A LEU 281 
282 1 Y 1 A GLN 293 ? A GLN 282 
283 1 Y 1 A GLN 294 ? A GLN 283 
284 1 Y 1 A ALA 295 ? A ALA 284 
285 1 Y 1 A VAL 296 ? A VAL 285 
286 1 Y 1 A ARG 297 ? A ARG 286 
287 1 Y 1 A ALA 298 ? A ALA 287 
288 1 Y 1 A ASN 299 ? A ASN 288 
289 1 Y 1 A PRO 300 ? A PRO 289 
290 1 Y 1 A LYS 301 ? A LYS 290 
291 1 Y 1 A ASP 302 ? A ASP 291 
292 1 Y 1 A SER 303 ? A SER 292 
293 1 Y 1 A GLU 304 ? A GLU 293 
294 1 Y 1 A ALA 305 ? A ALA 294 
295 1 Y 1 A LEU 306 ? A LEU 295 
296 1 Y 1 A GLY 307 ? A GLY 296 
297 1 Y 1 A ALA 308 ? A ALA 297 
298 1 Y 1 A LEU 309 ? A LEU 298 
299 1 Y 1 A GLY 310 ? A GLY 299 
300 1 Y 1 A GLN 311 ? A GLN 300 
301 1 Y 1 A ALA 312 ? A ALA 301 
302 1 Y 1 A TYR 313 ? A TYR 302 
303 1 Y 1 A SER 314 ? A SER 303 
304 1 Y 1 A GLN 315 ? A GLN 304 
305 1 Y 1 A LYS 316 ? A LYS 305 
306 1 Y 1 A GLY 317 ? A GLY 306 
307 1 Y 1 A ASP 318 ? A ASP 307 
308 1 Y 1 A ARG 319 ? A ARG 308 
309 1 Y 1 A ALA 320 ? A ALA 309 
310 1 Y 1 A ASN 321 ? A ASN 310 
311 1 Y 1 A ALA 322 ? A ALA 311 
312 1 Y 1 A VAL 323 ? A VAL 312 
313 1 Y 1 A ALA 324 ? A ALA 313 
314 1 Y 1 A ASN 325 ? A ASN 314 
315 1 Y 1 A LEU 326 ? A LEU 315 
316 1 Y 1 A GLU 327 ? A GLU 316 
317 1 Y 1 A LYS 328 ? A LYS 317 
318 1 Y 1 A ALA 329 ? A ALA 318 
319 1 Y 1 A LEU 330 ? A LEU 319 
320 1 Y 1 A ALA 331 ? A ALA 320 
321 1 Y 1 A LEU 332 ? A LEU 321 
322 1 Y 1 A ASP 333 ? A ASP 322 
323 1 Y 1 A PRO 334 ? A PRO 323 
324 1 Y 1 A HIS 335 ? A HIS 324 
325 1 Y 1 A SER 336 ? A SER 325 
326 1 Y 1 A SER 337 ? A SER 326 
327 1 Y 1 A ASN 338 ? A ASN 327 
328 1 Y 1 A ASN 339 ? A ASN 328 
329 1 Y 1 A ASP 340 ? A ASP 329 
330 1 Y 1 A LYS 341 ? A LYS 330 
331 1 Y 1 A TRP 342 ? A TRP 331 
332 1 Y 1 A ASN 343 ? A ASN 332 
333 1 Y 1 A SER 344 ? A SER 333 
334 1 Y 1 A LEU 345 ? A LEU 334 
335 1 Y 1 A LEU 346 ? A LEU 335 
336 1 Y 1 A LYS 347 ? A LYS 336 
337 1 Y 1 A VAL 348 ? A VAL 337 
338 1 Y 1 A ASN 349 ? A ASN 338 
339 1 Y 1 A ARG 350 ? A ARG 339 
340 1 Y 1 A TYR 351 ? A TYR 340 
341 1 Y 1 A TRP 352 ? A TRP 341 
342 1 Y 1 A LEU 353 ? A LEU 342 
343 1 Y 1 A ALA 354 ? A ALA 343 
344 1 Y 1 A ILE 355 ? A ILE 344 
345 1 Y 1 A GLN 356 ? A GLN 345 
346 1 Y 1 A GLN 357 ? A GLN 346 
347 1 Y 1 A GLY 358 ? A GLY 347 
348 1 Y 1 A ASP 359 ? A ASP 348 
349 1 Y 1 A ALA 360 ? A ALA 349 
350 1 Y 1 A ALA 361 ? A ALA 350 
351 1 Y 1 A LEU 362 ? A LEU 351 
352 1 Y 1 A LYS 363 ? A LYS 352 
353 1 Y 1 A ALA 364 ? A ALA 353 
354 1 Y 1 A ASN 365 ? A ASN 354 
355 1 Y 1 A ASN 366 ? A ASN 355 
356 1 Y 1 A PRO 367 ? A PRO 356 
357 1 Y 1 A ASP 368 ? A ASP 357 
358 1 Y 1 A ARG 369 ? A ARG 358 
359 1 Y 1 A ALA 370 ? A ALA 359 
360 1 Y 1 A GLU 371 ? A GLU 360 
361 1 Y 1 A ARG 372 ? A ARG 361 
362 1 Y 1 A LEU 373 ? A LEU 362 
363 1 Y 1 A PHE 374 ? A PHE 363 
364 1 Y 1 A GLN 375 ? A GLN 364 
365 1 Y 1 A GLN 376 ? A GLN 365 
366 1 Y 1 A ALA 377 ? A ALA 366 
367 1 Y 1 A ARG 378 ? A ARG 367 
368 1 Y 1 A ASN 379 ? A ASN 368 
369 1 Y 1 A VAL 380 ? A VAL 369 
370 1 Y 1 A ASP 381 ? A ASP 370 
371 1 Y 1 A ASN 382 ? A ASN 371 
372 1 Y 1 A THR 383 ? A THR 372 
373 1 Y 1 A ASP 384 ? A ASP 373 
374 1 Y 1 A SER 385 ? A SER 374 
375 1 Y 1 A TYR 386 ? A TYR 375 
376 1 Y 1 A ALA 387 ? A ALA 376 
377 1 Y 1 A VAL 388 ? A VAL 377 
378 1 Y 1 A LEU 389 ? A LEU 378 
379 1 Y 1 A GLY 390 ? A GLY 379 
380 1 Y 1 A LEU 391 ? A LEU 380 
381 1 Y 1 A GLY 392 ? A GLY 381 
382 1 Y 1 A ASP 393 ? A ASP 382 
383 1 Y 1 A VAL 394 ? A VAL 383 
384 1 Y 1 A ALA 395 ? A ALA 384 
385 1 Y 1 A MET 396 ? A MET 385 
386 1 Y 1 A ALA 397 ? A ALA 386 
387 1 Y 1 A ARG 398 ? A ARG 387 
388 1 Y 1 A LYS 399 ? A LYS 388 
389 1 Y 1 A ASP 400 ? A ASP 389 
390 1 Y 1 A TYR 401 ? A TYR 390 
391 1 Y 1 A PRO 402 ? A PRO 391 
392 1 Y 1 A ALA 403 ? A ALA 392 
393 1 Y 1 A ALA 404 ? A ALA 393 
394 1 Y 1 A GLU 405 ? A GLU 394 
395 1 Y 1 A ARG 406 ? A ARG 395 
396 1 Y 1 A TYR 407 ? A TYR 396 
397 1 Y 1 A TYR 408 ? A TYR 397 
398 1 Y 1 A GLN 409 ? A GLN 398 
399 1 Y 1 A GLN 410 ? A GLN 399 
400 1 Y 1 A THR 411 ? A THR 400 
401 1 Y 1 A LEU 412 ? A LEU 401 
402 1 Y 1 A ARG 413 ? A ARG 402 
403 1 Y 1 A MET 414 ? A MET 403 
404 1 Y 1 A ASP 415 ? A ASP 404 
405 1 Y 1 A SER 416 ? A SER 405 
406 1 Y 1 A GLY 417 ? A GLY 406 
407 1 Y 1 A ASN 418 ? A ASN 407 
408 1 Y 1 A THR 419 ? A THR 408 
409 1 Y 1 A ASN 420 ? A ASN 409 
410 1 Y 1 A ALA 421 ? A ALA 410 
411 1 Y 1 A VAL 422 ? A VAL 411 
412 1 Y 1 A ARG 423 ? A ARG 412 
413 1 Y 1 A GLY 424 ? A GLY 413 
414 1 Y 1 A LEU 425 ? A LEU 414 
415 1 Y 1 A ALA 426 ? A ALA 415 
416 1 Y 1 A ASN 427 ? A ASN 416 
417 1 Y 1 A ILE 428 ? A ILE 417 
418 1 Y 1 A TYR 429 ? A TYR 418 
419 1 Y 1 A ARG 430 ? A ARG 419 
420 1 Y 1 A GLN 431 ? A GLN 420 
421 1 Y 1 A GLN 432 ? A GLN 421 
422 1 Y 1 A SER 433 ? A SER 422 
423 1 Y 1 A PRO 434 ? A PRO 423 
424 1 Y 1 A GLU 435 ? A GLU 424 
425 1 Y 1 A LYS 436 ? A LYS 425 
426 1 Y 1 A ALA 437 ? A ALA 426 
427 1 Y 1 A GLU 438 ? A GLU 427 
428 1 Y 1 A ALA 439 ? A ALA 428 
429 1 Y 1 A PHE 440 ? A PHE 429 
430 1 Y 1 A ILE 441 ? A ILE 430 
431 1 Y 1 A ALA 442 ? A ALA 431 
432 1 Y 1 A SER 443 ? A SER 432 
433 1 Y 1 A LEU 444 ? A LEU 433 
434 1 Y 1 A SER 445 ? A SER 434 
435 1 Y 1 A ALA 446 ? A ALA 435 
436 1 Y 1 A SER 447 ? A SER 436 
437 1 Y 1 A GLN 448 ? A GLN 437 
438 1 Y 1 A ARG 449 ? A ARG 438 
439 1 Y 1 A ARG 450 ? A ARG 439 
440 1 Y 1 A SER 451 ? A SER 440 
441 1 Y 1 A ILE 452 ? A ILE 441 
442 1 Y 1 A ASP 453 ? A ASP 442 
443 1 Y 1 A ASP 454 ? A ASP 443 
444 1 Y 1 A ILE 455 ? A ILE 444 
445 1 Y 1 A GLU 456 ? A GLU 445 
446 1 Y 1 A ARG 457 ? A ARG 446 
447 1 Y 1 A SER 458 ? A SER 447 
448 1 Y 1 A LEU 459 ? A LEU 448 
449 1 Y 1 A GLN 460 ? A GLN 449 
450 1 Y 1 A ASN 461 ? A ASN 450 
451 1 Y 1 A ASP 462 ? A ASP 451 
452 1 Y 1 A ARG 463 ? A ARG 452 
453 1 Y 1 A LEU 464 ? A LEU 453 
454 1 Y 1 A ALA 465 ? A ALA 454 
455 1 Y 1 A GLN 466 ? A GLN 455 
456 1 Y 1 A GLN 467 ? A GLN 456 
457 1 Y 1 A ALA 468 ? A ALA 457 
458 1 Y 1 A GLU 469 ? A GLU 458 
459 1 Y 1 A ALA 470 ? A ALA 459 
460 1 Y 1 A LEU 471 ? A LEU 460 
461 1 Y 1 A GLU 472 ? A GLU 461 
462 1 Y 1 A ASN 473 ? A ASN 462 
463 1 Y 1 A GLN 474 ? A GLN 463 
464 1 Y 1 A GLY 475 ? A GLY 464 
465 1 Y 1 A LYS 476 ? A LYS 465 
466 1 Y 1 A TRP 477 ? A TRP 466 
467 1 Y 1 A ALA 478 ? A ALA 467 
468 1 Y 1 A GLN 479 ? A GLN 468 
469 1 Y 1 A ALA 480 ? A ALA 469 
470 1 Y 1 A ALA 481 ? A ALA 470 
471 1 Y 1 A ALA 482 ? A ALA 471 
472 1 Y 1 A LEU 483 ? A LEU 472 
473 1 Y 1 A GLN 484 ? A GLN 473 
474 1 Y 1 A ARG 485 ? A ARG 474 
475 1 Y 1 A GLN 486 ? A GLN 475 
476 1 Y 1 A ARG 487 ? A ARG 476 
477 1 Y 1 A LEU 488 ? A LEU 477 
478 1 Y 1 A ALA 489 ? A ALA 478 
479 1 Y 1 A LEU 490 ? A LEU 479 
480 1 Y 1 A ASP 491 ? A ASP 480 
481 1 Y 1 A PRO 492 ? A PRO 481 
482 1 Y 1 A GLY 493 ? A GLY 482 
483 1 Y 1 A SER 494 ? A SER 483 
484 1 Y 1 A VAL 495 ? A VAL 484 
485 1 Y 1 A TRP 496 ? A TRP 485 
486 1 Y 1 A ILE 497 ? A ILE 486 
487 1 Y 1 A THR 498 ? A THR 487 
488 1 Y 1 A TYR 499 ? A TYR 488 
489 1 Y 1 A ARG 500 ? A ARG 489 
490 1 Y 1 A LEU 501 ? A LEU 490 
491 1 Y 1 A SER 502 ? A SER 491 
492 1 Y 1 A GLN 503 ? A GLN 492 
493 1 Y 1 A ASP 504 ? A ASP 493 
494 1 Y 1 A LEU 505 ? A LEU 494 
495 1 Y 1 A TRP 506 ? A TRP 495 
496 1 Y 1 A GLN 507 ? A GLN 496 
497 1 Y 1 A ALA 508 ? A ALA 497 
498 1 Y 1 A GLY 509 ? A GLY 498 
499 1 Y 1 A GLN 510 ? A GLN 499 
500 1 Y 1 A ARG 511 ? A ARG 500 
501 1 Y 1 A SER 512 ? A SER 501 
502 1 Y 1 A GLN 513 ? A GLN 502 
503 1 Y 1 A ALA 514 ? A ALA 503 
504 1 Y 1 A ASP 515 ? A ASP 504 
505 1 Y 1 A THR 516 ? A THR 505 
506 1 Y 1 A LEU 517 ? A LEU 506 
507 1 Y 1 A MET 518 ? A MET 507 
508 1 Y 1 A ARG 519 ? A ARG 508 
509 1 Y 1 A ASN 520 ? A ASN 509 
510 1 Y 1 A LEU 521 ? A LEU 510 
511 1 Y 1 A ALA 522 ? A ALA 511 
512 1 Y 1 A GLN 523 ? A GLN 512 
513 1 Y 1 A GLN 524 ? A GLN 513 
514 1 Y 1 A LYS 525 ? A LYS 514 
515 1 Y 1 A SER 526 ? A SER 515 
516 1 Y 1 A ASN 527 ? A ASN 516 
517 1 Y 1 A ASP 528 ? A ASP 517 
518 1 Y 1 A PRO 529 ? A PRO 518 
519 1 Y 1 A GLU 530 ? A GLU 519 
520 1 Y 1 A GLN 531 ? A GLN 520 
521 1 Y 1 A VAL 532 ? A VAL 521 
522 1 Y 1 A TYR 533 ? A TYR 522 
523 1 Y 1 A ALA 534 ? A ALA 523 
524 1 Y 1 A TYR 535 ? A TYR 524 
525 1 Y 1 A GLY 536 ? A GLY 525 
526 1 Y 1 A LEU 537 ? A LEU 526 
527 1 Y 1 A TYR 538 ? A TYR 527 
528 1 Y 1 A LEU 539 ? A LEU 528 
529 1 Y 1 A SER 540 ? A SER 529 
530 1 Y 1 A GLY 541 ? A GLY 530 
531 1 Y 1 A HIS 542 ? A HIS 531 
532 1 Y 1 A ASP 543 ? A ASP 532 
533 1 Y 1 A GLN 544 ? A GLN 533 
534 1 Y 1 A ASP 545 ? A ASP 534 
535 1 Y 1 A ARG 546 ? A ARG 535 
536 1 Y 1 A ALA 547 ? A ALA 536 
537 1 Y 1 A ALA 548 ? A ALA 537 
538 1 Y 1 A LEU 549 ? A LEU 538 
539 1 Y 1 A ALA 550 ? A ALA 539 
540 1 Y 1 A HIS 551 ? A HIS 540 
541 1 Y 1 A ILE 552 ? A ILE 541 
542 1 Y 1 A ASN 553 ? A ASN 542 
543 1 Y 1 A SER 554 ? A SER 543 
544 1 Y 1 A LEU 555 ? A LEU 544 
545 1 Y 1 A PRO 556 ? A PRO 545 
546 1 Y 1 A ARG 557 ? A ARG 546 
547 1 Y 1 A ALA 558 ? A ALA 547 
548 1 Y 1 A GLN 559 ? A GLN 548 
549 1 Y 1 A TRP 560 ? A TRP 549 
550 1 Y 1 A ASN 561 ? A ASN 550 
551 1 Y 1 A SER 562 ? A SER 551 
552 1 Y 1 A ASN 563 ? A ASN 552 
553 1 Y 1 A ILE 564 ? A ILE 553 
554 1 Y 1 A GLN 565 ? A GLN 554 
555 1 Y 1 A GLU 566 ? A GLU 555 
556 1 Y 1 A LEU 567 ? A LEU 556 
557 1 Y 1 A VAL 568 ? A VAL 557 
558 1 Y 1 A ASN 569 ? A ASN 558 
559 1 Y 1 A ARG 570 ? A ARG 559 
560 1 Y 1 A LEU 571 ? A LEU 560 
561 1 Y 1 A GLN 572 ? A GLN 561 
562 1 Y 1 A SER 573 ? A SER 562 
563 1 Y 1 A ASP 574 ? A ASP 563 
564 1 Y 1 A GLN 575 ? A GLN 564 
565 1 Y 1 A VAL 576 ? A VAL 565 
566 1 Y 1 A LEU 577 ? A LEU 566 
567 1 Y 1 A GLU 578 ? A GLU 567 
568 1 Y 1 A THR 579 ? A THR 568 
569 1 Y 1 A ALA 580 ? A ALA 569 
570 1 Y 1 A ASN 581 ? A ASN 570 
571 1 Y 1 A ARG 582 ? A ARG 571 
572 1 Y 1 A LEU 583 ? A LEU 572 
573 1 Y 1 A ARG 584 ? A ARG 573 
574 1 Y 1 A GLU 585 ? A GLU 574 
575 1 Y 1 A SER 586 ? A SER 575 
576 1 Y 1 A GLY 587 ? A GLY 576 
577 1 Y 1 A LYS 588 ? A LYS 577 
578 1 Y 1 A GLU 589 ? A GLU 578 
579 1 Y 1 A ALA 590 ? A ALA 579 
580 1 Y 1 A GLU 591 ? A GLU 580 
581 1 Y 1 A ALA 592 ? A ALA 581 
582 1 Y 1 A GLU 593 ? A GLU 582 
583 1 Y 1 A ALA 594 ? A ALA 583 
584 1 Y 1 A MET 595 ? A MET 584 
585 1 Y 1 A LEU 596 ? A LEU 585 
586 1 Y 1 A ARG 597 ? A ARG 586 
587 1 Y 1 A GLN 598 ? A GLN 587 
588 1 Y 1 A GLN 599 ? A GLN 588 
589 1 Y 1 A PRO 600 ? A PRO 589 
590 1 Y 1 A PRO 601 ? A PRO 590 
591 1 Y 1 A ARG 616 ? A ARG 605 
592 1 Y 1 A ARG 617 ? A ARG 606 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-03-29 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9B8A 
_em_admin.last_update        2025-05-21 
_em_admin.map_release_date   2025-02-19 
_em_admin.title              'Cryo-EM structure of E. coli cellulose synthase subunit C' 
# 
_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_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          562 
_em_entity_assembly_naturalsource.organism             'Escherichia coli' 
_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         50 
_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                     ? 
# 
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 ? ? ?      ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 ?      ? 
MASKING                         ? 3  ? ? ? ?      ? 
'CTF CORRECTION'                ? 4  1 ? ? ?      ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ?      ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ?      ? 
'MODEL FITTING'                 ? 7  ? ? ? ?      ? 
'MODEL REFINEMENT'              ? 8  ? ? ? PHENIX ? 
OTHER                           ? 9  ? ? ? ?      ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ?      ? 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? ?      ? 
CLASSIFICATION                  ? 12 1 ? ? ?      ? 
RECONSTRUCTION                  ? 13 1 ? ? ?      ? 
'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 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           R35GM144130 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9B8A 
_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 1 591  ? 182.598 202.679 147.741 1.00 129.41 ? 602  SER A N   1 
ATOM 2    C CA  . SER A 1 591  ? 183.862 202.038 147.397 1.00 130.94 ? 602  SER A CA  1 
ATOM 3    C C   . SER A 1 591  ? 184.213 200.951 148.409 1.00 131.70 ? 602  SER A C   1 
ATOM 4    O O   . SER A 1 591  ? 183.974 201.107 149.604 1.00 132.53 ? 602  SER A O   1 
ATOM 5    C CB  . SER A 1 591  ? 184.985 203.073 147.318 1.00 127.91 ? 602  SER A CB  1 
ATOM 6    O OG  . SER A 1 591  ? 184.684 204.075 146.361 1.00 128.68 ? 602  SER A OG  1 
ATOM 7    N N   . THR A 1 592  ? 184.797 199.857 147.913 1.00 130.74 ? 603  THR A N   1 
ATOM 8    C CA  . THR A 1 592  ? 185.089 198.706 148.763 1.00 129.34 ? 603  THR A CA  1 
ATOM 9    C C   . THR A 1 592  ? 186.016 199.075 149.916 1.00 130.34 ? 603  THR A C   1 
ATOM 10   O O   . THR A 1 592  ? 185.814 198.632 151.053 1.00 130.67 ? 603  THR A O   1 
ATOM 11   C CB  . THR A 1 592  ? 185.706 197.585 147.924 1.00 122.02 ? 603  THR A CB  1 
ATOM 12   O OG1 . THR A 1 592  ? 184.780 197.179 146.908 1.00 118.32 ? 603  THR A OG1 1 
ATOM 13   C CG2 . THR A 1 592  ? 186.057 196.387 148.794 1.00 117.07 ? 603  THR A CG2 1 
ATOM 14   N N   . ARG A 1 593  ? 187.033 199.894 149.640 1.00 129.86 ? 604  ARG A N   1 
ATOM 15   C CA  . ARG A 1 593  ? 188.031 200.217 150.655 1.00 128.85 ? 604  ARG A CA  1 
ATOM 16   C C   . ARG A 1 593  ? 187.400 200.932 151.845 1.00 129.42 ? 604  ARG A C   1 
ATOM 17   O O   . ARG A 1 593  ? 187.581 200.524 152.998 1.00 125.27 ? 604  ARG A O   1 
ATOM 18   C CB  . ARG A 1 593  ? 189.139 201.071 150.038 1.00 125.92 ? 604  ARG A CB  1 
ATOM 19   C CG  . ARG A 1 593  ? 190.348 201.271 150.933 1.00 123.05 ? 604  ARG A CG  1 
ATOM 20   C CD  . ARG A 1 593  ? 191.135 199.978 151.075 1.00 121.73 ? 604  ARG A CD  1 
ATOM 21   N NE  . ARG A 1 593  ? 191.523 199.432 149.779 1.00 126.16 ? 604  ARG A NE  1 
ATOM 22   C CZ  . ARG A 1 593  ? 192.480 199.931 149.008 1.00 131.64 ? 604  ARG A CZ  1 
ATOM 23   N NH1 . ARG A 1 593  ? 193.191 200.984 149.379 1.00 129.97 ? 604  ARG A NH1 1 
ATOM 24   N NH2 . ARG A 1 593  ? 192.733 199.357 147.835 1.00 137.36 ? 604  ARG A NH2 1 
ATOM 25   N N   . ILE A 1 594  ? 186.647 202.003 151.582 1.00 132.83 ? 605  ILE A N   1 
ATOM 26   C CA  . ILE A 1 594  ? 186.057 202.771 152.674 1.00 132.74 ? 605  ILE A CA  1 
ATOM 27   C C   . ILE A 1 594  ? 184.950 201.984 153.364 1.00 131.50 ? 605  ILE A C   1 
ATOM 28   O O   . ILE A 1 594  ? 184.757 202.112 154.579 1.00 131.40 ? 605  ILE A O   1 
ATOM 29   C CB  . ILE A 1 594  ? 185.560 204.139 152.167 1.00 134.31 ? 605  ILE A CB  1 
ATOM 30   C CG1 . ILE A 1 594  ? 184.413 203.975 151.167 1.00 130.86 ? 605  ILE A CG1 1 
ATOM 31   C CG2 . ILE A 1 594  ? 186.706 204.925 151.546 1.00 137.82 ? 605  ILE A CG2 1 
ATOM 32   C CD1 . ILE A 1 594  ? 183.697 205.269 150.845 1.00 121.67 ? 605  ILE A CD1 1 
ATOM 33   N N   . ASP A 1 595  ? 184.206 201.161 152.618 1.00 131.27 ? 606  ASP A N   1 
ATOM 34   C CA  . ASP A 1 595  ? 183.177 200.335 153.243 1.00 129.84 ? 606  ASP A CA  1 
ATOM 35   C C   . ASP A 1 595  ? 183.791 199.325 154.205 1.00 129.39 ? 606  ASP A C   1 
ATOM 36   O O   . ASP A 1 595  ? 183.243 199.072 155.284 1.00 133.56 ? 606  ASP A O   1 
ATOM 37   C CB  . ASP A 1 595  ? 182.344 199.627 152.176 1.00 125.63 ? 606  ASP A CB  1 
ATOM 38   C CG  . ASP A 1 595  ? 181.619 200.595 151.263 1.00 126.56 ? 606  ASP A CG  1 
ATOM 39   O OD1 . ASP A 1 595  ? 181.409 201.755 151.673 1.00 125.52 ? 606  ASP A OD1 1 
ATOM 40   O OD2 . ASP A 1 595  ? 181.263 200.196 150.135 1.00 125.38 ? 606  ASP A OD2 1 
ATOM 41   N N   . LEU A 1 596  ? 184.925 198.730 153.828 1.00 125.36 ? 607  LEU A N   1 
ATOM 42   C CA  . LEU A 1 596  ? 185.624 197.831 154.740 1.00 122.84 ? 607  LEU A CA  1 
ATOM 43   C C   . LEU A 1 596  ? 186.185 198.592 155.936 1.00 120.93 ? 607  LEU A C   1 
ATOM 44   O O   . LEU A 1 596  ? 186.107 198.122 157.078 1.00 120.44 ? 607  LEU A O   1 
ATOM 45   C CB  . LEU A 1 596  ? 186.740 197.095 153.996 1.00 123.13 ? 607  LEU A CB  1 
ATOM 46   C CG  . LEU A 1 596  ? 186.435 195.677 153.508 1.00 115.88 ? 607  LEU A CG  1 
ATOM 47   C CD1 . LEU A 1 596  ? 187.384 195.280 152.389 1.00 104.38 ? 607  LEU A CD1 1 
ATOM 48   C CD2 . LEU A 1 596  ? 186.518 194.685 154.655 1.00 113.92 ? 607  LEU A CD2 1 
ATOM 49   N N   . THR A 1 597  ? 186.756 199.775 155.688 1.00 119.67 ? 608  THR A N   1 
ATOM 50   C CA  . THR A 1 597  ? 187.371 200.550 156.762 1.00 123.64 ? 608  THR A CA  1 
ATOM 51   C C   . THR A 1 597  ? 186.342 200.986 157.799 1.00 125.18 ? 608  THR A C   1 
ATOM 52   O O   . THR A 1 597  ? 186.623 200.977 159.003 1.00 125.53 ? 608  THR A O   1 
ATOM 53   C CB  . THR A 1 597  ? 188.094 201.766 156.181 1.00 125.48 ? 608  THR A CB  1 
ATOM 54   O OG1 . THR A 1 597  ? 189.038 201.335 155.192 1.00 123.59 ? 608  THR A OG1 1 
ATOM 55   C CG2 . THR A 1 597  ? 188.831 202.526 157.273 1.00 122.28 ? 608  THR A CG2 1 
ATOM 56   N N   . LEU A 1 598  ? 185.151 201.388 157.349 1.00 125.14 ? 609  LEU A N   1 
ATOM 57   C CA  . LEU A 1 598  ? 184.114 201.831 158.276 1.00 125.24 ? 609  LEU A CA  1 
ATOM 58   C C   . LEU A 1 598  ? 183.720 200.704 159.222 1.00 130.85 ? 609  LEU A C   1 
ATOM 59   O O   . LEU A 1 598  ? 183.562 200.916 160.430 1.00 135.35 ? 609  LEU A O   1 
ATOM 60   C CB  . LEU A 1 598  ? 182.903 202.342 157.489 1.00 119.73 ? 609  LEU A CB  1 
ATOM 61   C CG  . LEU A 1 598  ? 181.858 203.261 158.138 1.00 121.27 ? 609  LEU A CG  1 
ATOM 62   C CD1 . LEU A 1 598  ? 180.947 203.837 157.065 1.00 115.44 ? 609  LEU A CD1 1 
ATOM 63   C CD2 . LEU A 1 598  ? 181.023 202.556 159.198 1.00 123.08 ? 609  LEU A CD2 1 
ATOM 64   N N   . ALA A 1 599  ? 183.557 199.494 158.686 1.00 131.45 ? 610  ALA A N   1 
ATOM 65   C CA  . ALA A 1 599  ? 183.231 198.349 159.529 1.00 132.21 ? 610  ALA A CA  1 
ATOM 66   C C   . ALA A 1 599  ? 184.385 197.999 160.460 1.00 130.46 ? 610  ALA A C   1 
ATOM 67   O O   . ALA A 1 599  ? 184.167 197.653 161.627 1.00 126.30 ? 610  ALA A O   1 
ATOM 68   C CB  . ALA A 1 599  ? 182.855 197.152 158.657 1.00 130.59 ? 610  ALA A CB  1 
ATOM 69   N N   . ASP A 1 600  ? 185.616 198.092 159.967 1.00 128.81 ? 611  ASP A N   1 
ATOM 70   C CA  . ASP A 1 600  ? 186.754 197.646 160.814 1.00 128.54 ? 611  ASP A CA  1 
ATOM 71   C C   . ASP A 1 600  ? 187.030 198.643 161.938 1.00 128.95 ? 611  ASP A C   1 
ATOM 72   O O   . ASP A 1 600  ? 187.403 198.191 163.042 1.00 128.19 ? 611  ASP A O   1 
ATOM 73   C CB  . ASP A 1 600  ? 188.023 197.482 159.994 1.00 130.94 ? 611  ASP A CB  1 
ATOM 74   C CG  . ASP A 1 600  ? 187.955 196.487 158.846 1.00 130.37 ? 611  ASP A CG  1 
ATOM 75   O OD1 . ASP A 1 600  ? 188.986 196.308 158.165 1.00 130.69 ? 611  ASP A OD1 1 
ATOM 76   O OD2 . ASP A 1 600  ? 186.873 195.907 158.638 1.00 133.05 ? 611  ASP A OD2 1 
ATOM 77   N N   . TRP A 1 601  ? 186.804 199.935 161.702 1.00 127.35 ? 612  TRP A N   1 
ATOM 78   C CA  . TRP A 1 601  ? 187.236 200.935 162.677 1.00 127.78 ? 612  TRP A CA  1 
ATOM 79   C C   . TRP A 1 601  ? 186.487 200.804 163.998 1.00 132.85 ? 612  TRP A C   1 
ATOM 80   O O   . TRP A 1 601  ? 187.009 201.183 165.054 1.00 135.04 ? 612  TRP A O   1 
ATOM 81   C CB  . TRP A 1 601  ? 187.066 202.340 162.098 1.00 125.99 ? 612  TRP A CB  1 
ATOM 82   C CG  . TRP A 1 601  ? 188.080 203.317 162.607 1.00 131.06 ? 612  TRP A CG  1 
ATOM 83   C CD1 . TRP A 1 601  ? 188.165 203.835 163.867 1.00 130.50 ? 612  TRP A CD1 1 
ATOM 84   C CD2 . TRP A 1 601  ? 189.173 203.879 161.870 1.00 131.84 ? 612  TRP A CD2 1 
ATOM 85   N NE1 . TRP A 1 601  ? 189.234 204.693 163.956 1.00 130.83 ? 612  TRP A NE1 1 
ATOM 86   C CE2 . TRP A 1 601  ? 189.870 204.736 162.744 1.00 131.37 ? 612  TRP A CE2 1 
ATOM 87   C CE3 . TRP A 1 601  ? 189.628 203.744 160.554 1.00 126.49 ? 612  TRP A CE3 1 
ATOM 88   C CZ2 . TRP A 1 601  ? 190.996 205.455 162.345 1.00 121.93 ? 612  TRP A CZ2 1 
ATOM 89   C CZ3 . TRP A 1 601  ? 190.745 204.458 160.160 1.00 120.69 ? 612  TRP A CZ3 1 
ATOM 90   C CH2 . TRP A 1 601  ? 191.416 205.302 161.052 1.00 114.06 ? 612  TRP A CH2 1 
ATOM 91   N N   . ALA A 1 602  ? 185.266 200.269 163.963 1.00 136.13 ? 613  ALA A N   1 
ATOM 92   C CA  . ALA A 1 602  ? 184.463 200.183 165.178 1.00 140.69 ? 613  ALA A CA  1 
ATOM 93   C C   . ALA A 1 602  ? 185.096 199.258 166.211 1.00 140.14 ? 613  ALA A C   1 
ATOM 94   O O   . ALA A 1 602  ? 185.072 199.551 167.413 1.00 137.57 ? 613  ALA A O   1 
ATOM 95   C CB  . ALA A 1 602  ? 183.048 199.713 164.838 1.00 137.02 ? 613  ALA A CB  1 
ATOM 96   N N   . GLN A 1 603  ? 185.672 198.141 165.766 1.00 138.09 ? 614  GLN A N   1 
ATOM 97   C CA  . GLN A 1 603  ? 186.054 197.083 166.694 1.00 137.26 ? 614  GLN A CA  1 
ATOM 98   C C   . GLN A 1 603  ? 187.374 197.343 167.410 1.00 137.15 ? 614  GLN A C   1 
ATOM 99   O O   . GLN A 1 603  ? 187.660 196.659 168.399 1.00 135.39 ? 614  GLN A O   1 
ATOM 100  C CB  . GLN A 1 603  ? 186.117 195.746 165.957 1.00 135.60 ? 614  GLN A CB  1 
ATOM 101  C CG  . GLN A 1 603  ? 184.751 195.208 165.562 1.00 131.97 ? 614  GLN A CG  1 
ATOM 102  C CD  . GLN A 1 603  ? 184.047 194.499 166.704 1.00 126.22 ? 614  GLN A CD  1 
ATOM 103  O OE1 . GLN A 1 603  ? 183.656 195.123 167.691 1.00 123.98 ? 614  GLN A OE1 1 
ATOM 104  N NE2 . GLN A 1 603  ? 183.885 193.188 166.576 1.00 121.91 ? 614  GLN A NE2 1 
ATOM 105  N N   . GLN A 1 604  ? 188.179 198.297 166.951 1.00 136.88 ? 615  GLN A N   1 
ATOM 106  C CA  . GLN A 1 604  ? 189.438 198.599 167.629 1.00 135.19 ? 615  GLN A CA  1 
ATOM 107  C C   . GLN A 1 604  ? 189.233 199.631 168.734 1.00 135.71 ? 615  GLN A C   1 
ATOM 108  O O   . GLN A 1 604  ? 188.311 200.444 168.678 1.00 132.29 ? 615  GLN A O   1 
ATOM 109  C CB  . GLN A 1 604  ? 190.494 199.099 166.638 1.00 132.01 ? 615  GLN A CB  1 
ATOM 110  C CG  . GLN A 1 604  ? 190.949 198.068 165.620 1.00 132.28 ? 615  GLN A CG  1 
ATOM 111  C CD  . GLN A 1 604  ? 191.566 196.848 166.275 1.00 134.92 ? 615  GLN A CD  1 
ATOM 112  O OE1 . GLN A 1 604  ? 192.305 196.963 167.249 1.00 136.09 ? 615  GLN A OE1 1 
ATOM 113  N NE2 . GLN A 1 604  ? 191.259 195.671 165.741 1.00 135.56 ? 615  GLN A NE2 1 
ATOM 114  N N   . ASP A 1 607  ? 179.061 198.338 167.939 1.00 133.00 ? 618  ASP A N   1 
ATOM 115  C CA  . ASP A 1 607  ? 180.113 197.987 166.992 1.00 134.24 ? 618  ASP A CA  1 
ATOM 116  C C   . ASP A 1 607  ? 179.668 196.853 166.075 1.00 133.98 ? 618  ASP A C   1 
ATOM 117  O O   . ASP A 1 607  ? 180.307 196.573 165.062 1.00 137.74 ? 618  ASP A O   1 
ATOM 118  C CB  . ASP A 1 607  ? 181.392 197.585 167.733 1.00 135.92 ? 618  ASP A CB  1 
ATOM 119  C CG  . ASP A 1 607  ? 181.792 198.588 168.797 1.00 133.99 ? 618  ASP A CG  1 
ATOM 120  O OD1 . ASP A 1 607  ? 181.348 199.753 168.718 1.00 136.12 ? 618  ASP A OD1 1 
ATOM 121  O OD2 . ASP A 1 607  ? 182.551 198.210 169.715 1.00 125.09 ? 618  ASP A OD2 1 
ATOM 122  N N   . TYR A 1 608  ? 178.564 196.201 166.442 1.00 131.29 ? 619  TYR A N   1 
ATOM 123  C CA  . TYR A 1 608  ? 178.117 195.011 165.723 1.00 134.96 ? 619  TYR A CA  1 
ATOM 124  C C   . TYR A 1 608  ? 177.290 195.369 164.492 1.00 134.09 ? 619  TYR A C   1 
ATOM 125  O O   . TYR A 1 608  ? 177.638 194.993 163.367 1.00 130.94 ? 619  TYR A O   1 
ATOM 126  C CB  . TYR A 1 608  ? 177.315 194.108 166.665 1.00 133.16 ? 619  TYR A CB  1 
ATOM 127  C CG  . TYR A 1 608  ? 176.746 192.866 166.011 1.00 130.95 ? 619  TYR A CG  1 
ATOM 128  C CD1 . TYR A 1 608  ? 177.440 192.203 165.006 1.00 132.27 ? 619  TYR A CD1 1 
ATOM 129  C CD2 . TYR A 1 608  ? 175.511 192.361 166.395 1.00 130.31 ? 619  TYR A CD2 1 
ATOM 130  C CE1 . TYR A 1 608  ? 176.922 191.072 164.406 1.00 132.50 ? 619  TYR A CE1 1 
ATOM 131  C CE2 . TYR A 1 608  ? 174.985 191.229 165.801 1.00 134.27 ? 619  TYR A CE2 1 
ATOM 132  C CZ  . TYR A 1 608  ? 175.695 190.590 164.807 1.00 134.13 ? 619  TYR A CZ  1 
ATOM 133  O OH  . TYR A 1 608  ? 175.176 189.463 164.212 1.00 131.41 ? 619  TYR A OH  1 
ATOM 134  N N   . THR A 1 609  ? 176.184 196.090 164.691 1.00 133.66 ? 620  THR A N   1 
ATOM 135  C CA  . THR A 1 609  ? 175.190 196.244 163.631 1.00 133.98 ? 620  THR A CA  1 
ATOM 136  C C   . THR A 1 609  ? 175.744 197.026 162.445 1.00 137.25 ? 620  THR A C   1 
ATOM 137  O O   . THR A 1 609  ? 175.574 196.619 161.289 1.00 137.99 ? 620  THR A O   1 
ATOM 138  C CB  . THR A 1 609  ? 173.937 196.927 164.181 1.00 135.39 ? 620  THR A CB  1 
ATOM 139  O OG1 . THR A 1 609  ? 173.721 196.515 165.535 1.00 133.78 ? 620  THR A OG1 1 
ATOM 140  C CG2 . THR A 1 609  ? 172.722 196.556 163.346 1.00 136.52 ? 620  THR A CG2 1 
ATOM 141  N N   . ALA A 1 610  ? 176.400 198.159 162.708 1.00 136.58 ? 621  ALA A N   1 
ATOM 142  C CA  . ALA A 1 610  ? 176.917 198.981 161.618 1.00 136.46 ? 621  ALA A CA  1 
ATOM 143  C C   . ALA A 1 610  ? 177.985 198.240 160.826 1.00 141.20 ? 621  ALA A C   1 
ATOM 144  O O   . ALA A 1 610  ? 177.991 198.277 159.589 1.00 142.03 ? 621  ALA A O   1 
ATOM 145  C CB  . ALA A 1 610  ? 177.470 200.295 162.168 1.00 125.77 ? 621  ALA A CB  1 
ATOM 146  N N   . ALA A 1 611  ? 178.896 197.557 161.522 1.00 139.95 ? 622  ALA A N   1 
ATOM 147  C CA  . ALA A 1 611  ? 179.936 196.797 160.839 1.00 134.55 ? 622  ALA A CA  1 
ATOM 148  C C   . ALA A 1 611  ? 179.340 195.660 160.020 1.00 132.17 ? 622  ALA A C   1 
ATOM 149  O O   . ALA A 1 611  ? 179.774 195.403 158.893 1.00 132.22 ? 622  ALA A O   1 
ATOM 150  C CB  . ALA A 1 611  ? 180.948 196.263 161.852 1.00 134.32 ? 622  ALA A CB  1 
ATOM 151  N N   . ARG A 1 612  ? 178.349 194.960 160.577 1.00 131.03 ? 623  ARG A N   1 
ATOM 152  C CA  . ARG A 1 612  ? 177.724 193.854 159.857 1.00 132.40 ? 623  ARG A CA  1 
ATOM 153  C C   . ARG A 1 612  ? 177.011 194.365 158.608 1.00 134.97 ? 623  ARG A C   1 
ATOM 154  O O   . ARG A 1 612  ? 177.091 193.753 157.536 1.00 131.39 ? 623  ARG A O   1 
ATOM 155  C CB  . ARG A 1 612  ? 176.777 193.105 160.807 1.00 134.09 ? 623  ARG A CB  1 
ATOM 156  C CG  . ARG A 1 612  ? 176.274 191.718 160.363 1.00 137.83 ? 623  ARG A CG  1 
ATOM 157  C CD  . ARG A 1 612  ? 175.302 191.752 159.196 1.00 142.92 ? 623  ARG A CD  1 
ATOM 158  N NE  . ARG A 1 612  ? 174.236 192.719 159.434 1.00 144.92 ? 623  ARG A NE  1 
ATOM 159  C CZ  . ARG A 1 612  ? 173.596 193.383 158.481 1.00 141.35 ? 623  ARG A CZ  1 
ATOM 160  N NH1 . ARG A 1 612  ? 173.888 193.210 157.203 1.00 134.64 ? 623  ARG A NH1 1 
ATOM 161  N NH2 . ARG A 1 612  ? 172.637 194.240 158.819 1.00 138.64 ? 623  ARG A NH2 1 
ATOM 162  N N   . ALA A 1 613  ? 176.328 195.508 158.725 1.00 137.78 ? 624  ALA A N   1 
ATOM 163  C CA  . ALA A 1 613  ? 175.672 196.108 157.567 1.00 137.95 ? 624  ALA A CA  1 
ATOM 164  C C   . ALA A 1 613  ? 176.686 196.530 156.508 1.00 131.53 ? 624  ALA A C   1 
ATOM 165  O O   . ALA A 1 613  ? 176.463 196.325 155.310 1.00 125.09 ? 624  ALA A O   1 
ATOM 166  C CB  . ALA A 1 613  ? 174.823 197.301 158.004 1.00 136.02 ? 624  ALA A CB  1 
ATOM 167  N N   . ALA A 1 614  ? 177.806 197.124 156.928 1.00 129.41 ? 625  ALA A N   1 
ATOM 168  C CA  . ALA A 1 614  ? 178.837 197.521 155.972 1.00 128.09 ? 625  ALA A CA  1 
ATOM 169  C C   . ALA A 1 614  ? 179.433 196.307 155.266 1.00 132.63 ? 625  ALA A C   1 
ATOM 170  O O   . ALA A 1 614  ? 179.633 196.319 154.045 1.00 132.98 ? 625  ALA A O   1 
ATOM 171  C CB  . ALA A 1 614  ? 179.926 198.328 156.680 1.00 126.77 ? 625  ALA A CB  1 
ATOM 172  N N   . TYR A 1 615  ? 179.723 195.244 156.021 1.00 134.00 ? 626  TYR A N   1 
ATOM 173  C CA  . TYR A 1 615  ? 180.268 194.029 155.420 1.00 130.15 ? 626  TYR A CA  1 
ATOM 174  C C   . TYR A 1 615  ? 179.281 193.416 154.434 1.00 132.48 ? 626  TYR A C   1 
ATOM 175  O O   . TYR A 1 615  ? 179.669 192.954 153.354 1.00 131.75 ? 626  TYR A O   1 
ATOM 176  C CB  . TYR A 1 615  ? 180.645 193.022 156.509 1.00 125.40 ? 626  TYR A CB  1 
ATOM 177  C CG  . TYR A 1 615  ? 181.908 193.371 157.270 1.00 118.70 ? 626  TYR A CG  1 
ATOM 178  C CD1 . TYR A 1 615  ? 183.075 193.706 156.598 1.00 110.91 ? 626  TYR A CD1 1 
ATOM 179  C CD2 . TYR A 1 615  ? 181.935 193.352 158.659 1.00 121.14 ? 626  TYR A CD2 1 
ATOM 180  C CE1 . TYR A 1 615  ? 184.230 194.021 157.287 1.00 111.39 ? 626  TYR A CE1 1 
ATOM 181  C CE2 . TYR A 1 615  ? 183.084 193.670 159.355 1.00 119.73 ? 626  TYR A CE2 1 
ATOM 182  C CZ  . TYR A 1 615  ? 184.229 194.000 158.665 1.00 117.08 ? 626  TYR A CZ  1 
ATOM 183  O OH  . TYR A 1 615  ? 185.375 194.313 159.357 1.00 121.28 ? 626  TYR A OH  1 
ATOM 184  N N   . GLN A 1 616  ? 177.993 193.404 154.786 1.00 134.09 ? 627  GLN A N   1 
ATOM 185  C CA  . GLN A 1 616  ? 176.986 192.899 153.858 1.00 134.54 ? 627  GLN A CA  1 
ATOM 186  C C   . GLN A 1 616  ? 176.891 193.778 152.616 1.00 132.00 ? 627  GLN A C   1 
ATOM 187  O O   . GLN A 1 616  ? 176.635 193.281 151.513 1.00 130.74 ? 627  GLN A O   1 
ATOM 188  C CB  . GLN A 1 616  ? 175.631 192.796 154.555 1.00 132.64 ? 627  GLN A CB  1 
ATOM 189  C CG  . GLN A 1 616  ? 174.577 192.032 153.765 1.00 135.46 ? 627  GLN A CG  1 
ATOM 190  C CD  . GLN A 1 616  ? 174.964 190.585 153.512 1.00 134.69 ? 627  GLN A CD  1 
ATOM 191  O OE1 . GLN A 1 616  ? 174.785 189.723 154.372 1.00 133.85 ? 627  GLN A OE1 1 
ATOM 192  N NE2 . GLN A 1 616  ? 175.479 190.308 152.319 1.00 132.83 ? 627  GLN A NE2 1 
ATOM 193  N N   . ASN A 1 617  ? 177.079 195.090 152.777 1.00 127.18 ? 628  ASN A N   1 
ATOM 194  C CA  . ASN A 1 617  ? 177.071 195.984 151.623 1.00 126.95 ? 628  ASN A CA  1 
ATOM 195  C C   . ASN A 1 617  ? 178.235 195.679 150.687 1.00 129.14 ? 628  ASN A C   1 
ATOM 196  O O   . ASN A 1 617  ? 178.075 195.696 149.460 1.00 127.49 ? 628  ASN A O   1 
ATOM 197  C CB  . ASN A 1 617  ? 177.111 197.441 152.087 1.00 119.83 ? 628  ASN A CB  1 
ATOM 198  C CG  . ASN A 1 617  ? 176.895 198.425 150.951 1.00 114.68 ? 628  ASN A CG  1 
ATOM 199  O OD1 . ASN A 1 617  ? 176.463 198.051 149.860 1.00 118.09 ? 628  ASN A OD1 1 
ATOM 200  N ND2 . ASN A 1 617  ? 177.183 199.695 151.209 1.00 109.35 ? 628  ASN A ND2 1 
ATOM 201  N N   . VAL A 1 618  ? 179.417 195.405 151.247 1.00 130.87 ? 629  VAL A N   1 
ATOM 202  C CA  . VAL A 1 618  ? 180.543 194.980 150.411 1.00 134.14 ? 629  VAL A CA  1 
ATOM 203  C C   . VAL A 1 618  ? 180.246 193.637 149.754 1.00 135.61 ? 629  VAL A C   1 
ATOM 204  O O   . VAL A 1 618  ? 180.670 193.377 148.622 1.00 137.00 ? 629  VAL A O   1 
ATOM 205  C CB  . VAL A 1 618  ? 181.858 194.935 151.213 1.00 134.09 ? 629  VAL A CB  1 
ATOM 206  C CG1 . VAL A 1 618  ? 182.968 194.376 150.350 1.00 130.11 ? 629  VAL A CG1 1 
ATOM 207  C CG2 . VAL A 1 618  ? 182.256 196.312 151.661 1.00 128.46 ? 629  VAL A CG2 1 
ATOM 208  N N   . LEU A 1 619  ? 179.529 192.759 150.458 1.00 136.10 ? 630  LEU A N   1 
ATOM 209  C CA  . LEU A 1 619  ? 179.128 191.477 149.887 1.00 135.49 ? 630  LEU A CA  1 
ATOM 210  C C   . LEU A 1 619  ? 178.246 191.624 148.652 1.00 134.74 ? 630  LEU A C   1 
ATOM 211  O O   . LEU A 1 619  ? 178.220 190.710 147.820 1.00 131.50 ? 630  LEU A O   1 
ATOM 212  C CB  . LEU A 1 619  ? 178.402 190.645 150.949 1.00 132.36 ? 630  LEU A CB  1 
ATOM 213  C CG  . LEU A 1 619  ? 179.129 189.457 151.585 1.00 127.55 ? 630  LEU A CG  1 
ATOM 214  C CD1 . LEU A 1 619  ? 179.476 188.392 150.549 1.00 133.13 ? 630  LEU A CD1 1 
ATOM 215  C CD2 . LEU A 1 619  ? 180.383 189.934 152.275 1.00 120.84 ? 630  LEU A CD2 1 
ATOM 216  N N   . THR A 1 620  ? 177.538 192.748 148.501 1.00 132.71 ? 631  THR A N   1 
ATOM 217  C CA  . THR A 1 620  ? 176.723 192.942 147.306 1.00 137.65 ? 631  THR A CA  1 
ATOM 218  C C   . THR A 1 620  ? 177.590 193.196 146.081 1.00 146.70 ? 631  THR A C   1 
ATOM 219  O O   . THR A 1 620  ? 177.347 192.622 145.013 1.00 148.35 ? 631  THR A O   1 
ATOM 220  C CB  . THR A 1 620  ? 175.746 194.102 147.500 1.00 130.41 ? 631  THR A CB  1 
ATOM 221  O OG1 . THR A 1 620  ? 176.467 195.341 147.529 1.00 124.53 ? 631  THR A OG1 1 
ATOM 222  C CG2 . THR A 1 620  ? 174.955 193.934 148.786 1.00 127.58 ? 631  THR A CG2 1 
ATOM 223  N N   . ARG A 1 621  ? 178.596 194.064 146.211 1.00 148.49 ? 632  ARG A N   1 
ATOM 224  C CA  . ARG A 1 621  ? 179.460 194.386 145.080 1.00 149.68 ? 632  ARG A CA  1 
ATOM 225  C C   . ARG A 1 621  ? 180.389 193.229 144.739 1.00 149.74 ? 632  ARG A C   1 
ATOM 226  O O   . ARG A 1 621  ? 180.570 192.894 143.564 1.00 149.40 ? 632  ARG A O   1 
ATOM 227  C CB  . ARG A 1 621  ? 180.271 195.649 145.379 1.00 149.74 ? 632  ARG A CB  1 
ATOM 228  C CG  . ARG A 1 621  ? 181.339 195.984 144.340 1.00 153.62 ? 632  ARG A CG  1 
ATOM 229  C CD  . ARG A 1 621  ? 180.737 196.234 142.967 1.00 157.82 ? 632  ARG A CD  1 
ATOM 230  N NE  . ARG A 1 621  ? 180.728 195.028 142.148 1.00 155.50 ? 632  ARG A NE  1 
ATOM 231  C CZ  . ARG A 1 621  ? 180.981 195.006 140.847 1.00 157.14 ? 632  ARG A CZ  1 
ATOM 232  N NH1 . ARG A 1 621  ? 181.255 196.113 140.178 1.00 159.26 ? 632  ARG A NH1 1 
ATOM 233  N NH2 . ARG A 1 621  ? 180.950 193.844 140.199 1.00 156.17 ? 632  ARG A NH2 1 
ATOM 234  N N   . GLU A 1 622  ? 180.990 192.613 145.754 1.00 148.23 ? 633  GLU A N   1 
ATOM 235  C CA  . GLU A 1 622  ? 181.912 191.499 145.552 1.00 144.73 ? 633  GLU A CA  1 
ATOM 236  C C   . GLU A 1 622  ? 181.558 190.395 146.535 1.00 141.64 ? 633  GLU A C   1 
ATOM 237  O O   . GLU A 1 622  ? 181.998 190.408 147.691 1.00 136.81 ? 633  GLU A O   1 
ATOM 238  C CB  . GLU A 1 622  ? 183.366 191.940 145.723 1.00 140.28 ? 633  GLU A CB  1 
ATOM 239  C CG  . GLU A 1 622  ? 184.406 190.859 145.444 1.00 133.31 ? 633  GLU A CG  1 
ATOM 240  C CD  . GLU A 1 622  ? 184.229 190.188 144.090 1.00 135.41 ? 633  GLU A CD  1 
ATOM 241  O OE1 . GLU A 1 622  ? 183.390 189.271 143.977 1.00 136.65 ? 633  GLU A OE1 1 
ATOM 242  O OE2 . GLU A 1 622  ? 184.937 190.576 143.136 1.00 136.87 ? 633  GLU A OE2 1 
ATOM 243  N N   . PRO A 1 623  ? 180.755 189.416 146.108 1.00 143.57 ? 634  PRO A N   1 
ATOM 244  C CA  . PRO A 1 623  ? 180.421 188.299 147.005 1.00 140.73 ? 634  PRO A CA  1 
ATOM 245  C C   . PRO A 1 623  ? 181.620 187.459 147.412 1.00 138.57 ? 634  PRO A C   1 
ATOM 246  O O   . PRO A 1 623  ? 181.538 186.750 148.424 1.00 133.17 ? 634  PRO A O   1 
ATOM 247  C CB  . PRO A 1 623  ? 179.422 187.476 146.179 1.00 142.87 ? 634  PRO A CB  1 
ATOM 248  C CG  . PRO A 1 623  ? 179.774 187.787 144.753 1.00 143.09 ? 634  PRO A CG  1 
ATOM 249  C CD  . PRO A 1 623  ? 180.198 189.231 144.755 1.00 143.51 ? 634  PRO A CD  1 
ATOM 250  N N   . ALA A 1 624  ? 182.727 187.521 146.669 1.00 139.68 ? 635  ALA A N   1 
ATOM 251  C CA  . ALA A 1 624  ? 183.907 186.718 146.969 1.00 133.51 ? 635  ALA A CA  1 
ATOM 252  C C   . ALA A 1 624  ? 184.909 187.429 147.870 1.00 130.07 ? 635  ALA A C   1 
ATOM 253  O O   . ALA A 1 624  ? 185.999 186.891 148.094 1.00 124.07 ? 635  ALA A O   1 
ATOM 254  C CB  . ALA A 1 624  ? 184.601 186.300 145.667 1.00 131.95 ? 635  ALA A CB  1 
ATOM 255  N N   . ASN A 1 625  ? 184.580 188.616 148.380 1.00 132.27 ? 636  ASN A N   1 
ATOM 256  C CA  . ASN A 1 625  ? 185.497 189.364 149.234 1.00 124.83 ? 636  ASN A CA  1 
ATOM 257  C C   . ASN A 1 625  ? 185.789 188.597 150.518 1.00 116.60 ? 636  ASN A C   1 
ATOM 258  O O   . ASN A 1 625  ? 184.919 188.474 151.385 1.00 115.74 ? 636  ASN A O   1 
ATOM 259  C CB  . ASN A 1 625  ? 184.918 190.746 149.556 1.00 120.12 ? 636  ASN A CB  1 
ATOM 260  C CG  . ASN A 1 625  ? 185.930 191.671 150.210 1.00 114.16 ? 636  ASN A CG  1 
ATOM 261  O OD1 . ASN A 1 625  ? 186.512 191.347 151.246 1.00 110.00 ? 636  ASN A OD1 1 
ATOM 262  N ND2 . ASN A 1 625  ? 186.141 192.834 149.607 1.00 115.04 ? 636  ASN A ND2 1 
ATOM 263  N N   . ALA A 1 626  ? 187.015 188.084 150.649 1.00 112.68 ? 637  ALA A N   1 
ATOM 264  C CA  . ALA A 1 626  ? 187.369 187.298 151.827 1.00 114.72 ? 637  ALA A CA  1 
ATOM 265  C C   . ALA A 1 626  ? 187.376 188.151 153.090 1.00 116.05 ? 637  ALA A C   1 
ATOM 266  O O   . ALA A 1 626  ? 186.893 187.714 154.143 1.00 115.97 ? 637  ALA A O   1 
ATOM 267  C CB  . ALA A 1 626  ? 188.729 186.631 151.623 1.00 117.44 ? 637  ALA A CB  1 
ATOM 268  N N   . ASP A 1 627  ? 187.921 189.367 153.006 1.00 115.50 ? 638  ASP A N   1 
ATOM 269  C CA  . ASP A 1 627  ? 188.024 190.221 154.185 1.00 113.22 ? 638  ASP A CA  1 
ATOM 270  C C   . ASP A 1 627  ? 186.654 190.609 154.724 1.00 111.29 ? 638  ASP A C   1 
ATOM 271  O O   . ASP A 1 627  ? 186.466 190.675 155.945 1.00 113.67 ? 638  ASP A O   1 
ATOM 272  C CB  . ASP A 1 627  ? 188.841 191.471 153.858 1.00 115.03 ? 638  ASP A CB  1 
ATOM 273  C CG  . ASP A 1 627  ? 189.395 192.147 155.097 1.00 116.59 ? 638  ASP A CG  1 
ATOM 274  O OD1 . ASP A 1 627  ? 189.633 191.445 156.103 1.00 111.13 ? 638  ASP A OD1 1 
ATOM 275  O OD2 . ASP A 1 627  ? 189.597 193.379 155.065 1.00 122.43 ? 638  ASP A OD2 1 
ATOM 276  N N   . ALA A 1 628  ? 185.691 190.872 153.838 1.00 108.87 ? 639  ALA A N   1 
ATOM 277  C CA  . ALA A 1 628  ? 184.349 191.227 154.287 1.00 111.20 ? 639  ALA A CA  1 
ATOM 278  C C   . ALA A 1 628  ? 183.711 190.087 155.071 1.00 109.47 ? 639  ALA A C   1 
ATOM 279  O O   . ALA A 1 628  ? 183.115 190.304 156.133 1.00 114.63 ? 639  ALA A O   1 
ATOM 280  C CB  . ALA A 1 628  ? 183.484 191.611 153.087 1.00 116.76 ? 639  ALA A CB  1 
ATOM 281  N N   . ILE A 1 629  ? 183.839 188.857 154.569 1.00 104.14 ? 640  ILE A N   1 
ATOM 282  C CA  . ILE A 1 629  ? 183.249 187.713 155.259 1.00 105.05 ? 640  ILE A CA  1 
ATOM 283  C C   . ILE A 1 629  ? 183.984 187.434 156.564 1.00 105.75 ? 640  ILE A C   1 
ATOM 284  O O   . ILE A 1 629  ? 183.371 187.035 157.561 1.00 105.73 ? 640  ILE A O   1 
ATOM 285  C CB  . ILE A 1 629  ? 183.227 186.481 154.338 1.00 108.45 ? 640  ILE A CB  1 
ATOM 286  C CG1 . ILE A 1 629  ? 182.706 186.863 152.953 1.00 109.54 ? 640  ILE A CG1 1 
ATOM 287  C CG2 . ILE A 1 629  ? 182.344 185.398 154.931 1.00 106.92 ? 640  ILE A CG2 1 
ATOM 288  C CD1 . ILE A 1 629  ? 183.017 185.844 151.879 1.00 109.88 ? 640  ILE A CD1 1 
ATOM 289  N N   . LEU A 1 630  ? 185.306 187.625 156.581 1.00 107.05 ? 641  LEU A N   1 
ATOM 290  C CA  . LEU A 1 630  ? 186.055 187.476 157.827 1.00 104.88 ? 641  LEU A CA  1 
ATOM 291  C C   . LEU A 1 630  ? 185.580 188.474 158.873 1.00 109.18 ? 641  LEU A C   1 
ATOM 292  O O   . LEU A 1 630  ? 185.396 188.126 160.046 1.00 109.32 ? 641  LEU A O   1 
ATOM 293  C CB  . LEU A 1 630  ? 187.552 187.647 157.570 1.00 100.42 ? 641  LEU A CB  1 
ATOM 294  C CG  . LEU A 1 630  ? 188.415 186.389 157.663 1.00 92.48  ? 641  LEU A CG  1 
ATOM 295  C CD1 . LEU A 1 630  ? 188.083 185.420 156.545 1.00 91.91  ? 641  LEU A CD1 1 
ATOM 296  C CD2 . LEU A 1 630  ? 189.889 186.756 157.648 1.00 82.54  ? 641  LEU A CD2 1 
ATOM 297  N N   . GLY A 1 631  ? 185.379 189.727 158.465 1.00 115.12 ? 642  GLY A N   1 
ATOM 298  C CA  . GLY A 1 631  ? 184.874 190.723 159.395 1.00 110.84 ? 642  GLY A CA  1 
ATOM 299  C C   . GLY A 1 631  ? 183.470 190.407 159.873 1.00 111.02 ? 642  GLY A C   1 
ATOM 300  O O   . GLY A 1 631  ? 183.133 190.625 161.038 1.00 113.24 ? 642  GLY A O   1 
ATOM 301  N N   . LEU A 1 632  ? 182.628 189.897 158.970 1.00 111.76 ? 643  LEU A N   1 
ATOM 302  C CA  . LEU A 1 632  ? 181.283 189.480 159.355 1.00 112.32 ? 643  LEU A CA  1 
ATOM 303  C C   . LEU A 1 632  ? 181.335 188.366 160.394 1.00 113.99 ? 643  LEU A C   1 
ATOM 304  O O   . LEU A 1 632  ? 180.607 188.394 161.392 1.00 115.06 ? 643  LEU A O   1 
ATOM 305  C CB  . LEU A 1 632  ? 180.503 189.033 158.119 1.00 108.77 ? 643  LEU A CB  1 
ATOM 306  C CG  . LEU A 1 632  ? 179.286 188.139 158.363 1.00 108.98 ? 643  LEU A CG  1 
ATOM 307  C CD1 . LEU A 1 632  ? 178.038 188.972 158.615 1.00 118.45 ? 643  LEU A CD1 1 
ATOM 308  C CD2 . LEU A 1 632  ? 179.078 187.188 157.196 1.00 101.38 ? 643  LEU A CD2 1 
ATOM 309  N N   . THR A 1 633  ? 182.208 187.381 160.181 1.00 112.96 ? 644  THR A N   1 
ATOM 310  C CA  . THR A 1 633  ? 182.362 186.304 161.153 1.00 113.58 ? 644  THR A CA  1 
ATOM 311  C C   . THR A 1 633  ? 182.860 186.836 162.491 1.00 116.04 ? 644  THR A C   1 
ATOM 312  O O   . THR A 1 633  ? 182.383 186.414 163.552 1.00 121.96 ? 644  THR A O   1 
ATOM 313  C CB  . THR A 1 633  ? 183.319 185.239 160.616 1.00 109.38 ? 644  THR A CB  1 
ATOM 314  O OG1 . THR A 1 633  ? 182.865 184.786 159.334 1.00 113.35 ? 644  THR A OG1 1 
ATOM 315  C CG2 . THR A 1 633  ? 183.394 184.057 161.571 1.00 107.86 ? 644  THR A CG2 1 
ATOM 316  N N   . GLU A 1 634  ? 183.841 187.739 162.430 1.00 114.85 ? 645  GLU A N   1 
ATOM 317  C CA  . GLU A 1 634  ? 184.430 188.289 163.676 1.00 117.76 ? 645  GLU A CA  1 
ATOM 318  C C   . GLU A 1 634  ? 183.327 189.015 164.458 1.00 122.21 ? 645  GLU A C   1 
ATOM 319  O O   . GLU A 1 634  ? 183.159 188.737 165.662 1.00 124.92 ? 645  GLU A O   1 
ATOM 320  C CB  . GLU A 1 634  ? 185.594 189.222 163.343 1.00 115.73 ? 645  GLU A CB  1 
ATOM 321  C CG  . GLU A 1 634  ? 186.263 189.819 164.578 1.00 117.12 ? 645  GLU A CG  1 
ATOM 322  C CD  . GLU A 1 634  ? 185.792 191.213 164.951 1.00 122.26 ? 645  GLU A CD  1 
ATOM 323  O OE1 . GLU A 1 634  ? 186.264 191.739 165.980 1.00 121.68 ? 645  GLU A OE1 1 
ATOM 324  O OE2 . GLU A 1 634  ? 184.961 191.779 164.209 1.00 123.97 ? 645  GLU A OE2 1 
ATOM 325  N N   . VAL A 1 635  ? 182.610 189.920 163.792 1.00 119.06 ? 646  VAL A N   1 
ATOM 326  C CA  . VAL A 1 635  ? 181.567 190.667 164.495 1.00 117.66 ? 646  VAL A CA  1 
ATOM 327  C C   . VAL A 1 635  ? 180.476 189.729 165.000 1.00 122.82 ? 646  VAL A C   1 
ATOM 328  O O   . VAL A 1 635  ? 179.894 189.967 166.065 1.00 127.12 ? 646  VAL A O   1 
ATOM 329  C CB  . VAL A 1 635  ? 180.973 191.797 163.625 1.00 118.09 ? 646  VAL A CB  1 
ATOM 330  C CG1 . VAL A 1 635  ? 182.039 192.802 163.225 1.00 116.40 ? 646  VAL A CG1 1 
ATOM 331  C CG2 . VAL A 1 635  ? 180.263 191.251 162.403 1.00 124.00 ? 646  VAL A CG2 1 
ATOM 332  N N   . ASP A 1 636  ? 180.168 188.661 164.256 1.00 123.02 ? 647  ASP A N   1 
ATOM 333  C CA  . ASP A 1 636  ? 179.154 187.718 164.718 1.00 128.35 ? 647  ASP A CA  1 
ATOM 334  C C   . ASP A 1 636  ? 179.601 186.998 165.983 1.00 132.34 ? 647  ASP A C   1 
ATOM 335  O O   . ASP A 1 636  ? 178.807 186.815 166.914 1.00 134.24 ? 647  ASP A O   1 
ATOM 336  C CB  . ASP A 1 636  ? 178.829 186.712 163.614 1.00 126.42 ? 647  ASP A CB  1 
ATOM 337  C CG  . ASP A 1 636  ? 177.683 187.167 162.732 1.00 125.74 ? 647  ASP A CG  1 
ATOM 338  O OD1 . ASP A 1 636  ? 177.147 188.269 162.973 1.00 124.46 ? 647  ASP A OD1 1 
ATOM 339  O OD2 . ASP A 1 636  ? 177.317 186.423 161.798 1.00 124.41 ? 647  ASP A OD2 1 
ATOM 340  N N   . ILE A 1 637  ? 180.868 186.587 166.041 1.00 131.02 ? 648  ILE A N   1 
ATOM 341  C CA  . ILE A 1 637  ? 181.333 185.868 167.224 1.00 131.01 ? 648  ILE A CA  1 
ATOM 342  C C   . ILE A 1 637  ? 181.590 186.837 168.375 1.00 132.51 ? 648  ILE A C   1 
ATOM 343  O O   . ILE A 1 637  ? 181.468 186.460 169.547 1.00 135.68 ? 648  ILE A O   1 
ATOM 344  C CB  . ILE A 1 637  ? 182.578 185.023 166.898 1.00 124.12 ? 648  ILE A CB  1 
ATOM 345  C CG1 . ILE A 1 637  ? 183.054 184.269 168.139 1.00 122.08 ? 648  ILE A CG1 1 
ATOM 346  C CG2 . ILE A 1 637  ? 183.704 185.900 166.387 1.00 118.97 ? 648  ILE A CG2 1 
ATOM 347  C CD1 . ILE A 1 637  ? 184.107 183.238 167.850 1.00 115.42 ? 648  ILE A CD1 1 
ATOM 348  N N   . ALA A 1 638  ? 181.928 188.094 168.072 1.00 131.69 ? 649  ALA A N   1 
ATOM 349  C CA  . ALA A 1 638  ? 182.026 189.102 169.122 1.00 135.43 ? 649  ALA A CA  1 
ATOM 350  C C   . ALA A 1 638  ? 180.686 189.288 169.823 1.00 142.40 ? 649  ALA A C   1 
ATOM 351  O O   . ALA A 1 638  ? 180.637 189.655 171.003 1.00 145.45 ? 649  ALA A O   1 
ATOM 352  C CB  . ALA A 1 638  ? 182.517 190.426 168.538 1.00 131.90 ? 649  ALA A CB  1 
ATOM 353  N N   . ALA A 1 639  ? 179.590 189.036 169.111 1.00 143.19 ? 650  ALA A N   1 
ATOM 354  C CA  . ALA A 1 639  ? 178.252 189.041 169.685 1.00 146.57 ? 650  ALA A CA  1 
ATOM 355  C C   . ALA A 1 639  ? 177.884 187.709 170.328 1.00 147.50 ? 650  ALA A C   1 
ATOM 356  O O   . ALA A 1 639  ? 176.779 187.581 170.866 1.00 149.29 ? 650  ALA A O   1 
ATOM 357  C CB  . ALA A 1 639  ? 177.221 189.403 168.612 1.00 140.02 ? 650  ALA A CB  1 
ATOM 358  N N   . GLY A 1 640  ? 178.778 186.722 170.284 1.00 145.61 ? 651  GLY A N   1 
ATOM 359  C CA  . GLY A 1 640  ? 178.520 185.425 170.874 1.00 145.63 ? 651  GLY A CA  1 
ATOM 360  C C   . GLY A 1 640  ? 177.817 184.430 169.980 1.00 149.36 ? 651  GLY A C   1 
ATOM 361  O O   . GLY A 1 640  ? 177.388 183.379 170.470 1.00 151.20 ? 651  GLY A O   1 
ATOM 362  N N   . ASP A 1 641  ? 177.682 184.720 168.685 1.00 146.53 ? 652  ASP A N   1 
ATOM 363  C CA  . ASP A 1 641  ? 177.018 183.814 167.747 1.00 142.58 ? 652  ASP A CA  1 
ATOM 364  C C   . ASP A 1 641  ? 178.019 182.813 167.163 1.00 136.87 ? 652  ASP A C   1 
ATOM 365  O O   . ASP A 1 641  ? 178.321 182.802 165.971 1.00 133.43 ? 652  ASP A O   1 
ATOM 366  C CB  . ASP A 1 641  ? 176.325 184.613 166.652 1.00 140.10 ? 652  ASP A CB  1 
ATOM 367  C CG  . ASP A 1 641  ? 175.149 183.874 166.047 1.00 145.50 ? 652  ASP A CG  1 
ATOM 368  O OD1 . ASP A 1 641  ? 174.875 182.735 166.480 1.00 141.26 ? 652  ASP A OD1 1 
ATOM 369  O OD2 . ASP A 1 641  ? 174.497 184.433 165.140 1.00 150.45 ? 652  ASP A OD2 1 
ATOM 370  N N   . LYS A 1 642  ? 178.537 181.956 168.047 1.00 137.03 ? 653  LYS A N   1 
ATOM 371  C CA  . LYS A 1 642  ? 179.531 180.964 167.644 1.00 135.71 ? 653  LYS A CA  1 
ATOM 372  C C   . LYS A 1 642  ? 178.953 179.962 166.650 1.00 137.97 ? 653  LYS A C   1 
ATOM 373  O O   . LYS A 1 642  ? 179.608 179.592 165.667 1.00 136.20 ? 653  LYS A O   1 
ATOM 374  C CB  . LYS A 1 642  ? 180.070 180.245 168.882 1.00 129.89 ? 653  LYS A CB  1 
ATOM 375  C CG  . LYS A 1 642  ? 181.269 179.351 168.617 1.00 124.26 ? 653  LYS A CG  1 
ATOM 376  C CD  . LYS A 1 642  ? 181.599 178.500 169.832 1.00 124.60 ? 653  LYS A CD  1 
ATOM 377  C CE  . LYS A 1 642  ? 180.570 177.400 170.032 1.00 129.88 ? 653  LYS A CE  1 
ATOM 378  N NZ  . LYS A 1 642  ? 180.884 176.557 171.219 1.00 132.98 ? 653  LYS A NZ  1 
ATOM 379  N N   . ALA A 1 643  ? 177.721 179.507 166.897 1.00 138.42 ? 654  ALA A N   1 
ATOM 380  C CA  . ALA A 1 643  ? 177.119 178.480 166.051 1.00 136.17 ? 654  ALA A CA  1 
ATOM 381  C C   . ALA A 1 643  ? 176.939 178.972 164.620 1.00 132.06 ? 654  ALA A C   1 
ATOM 382  O O   . ALA A 1 643  ? 177.171 178.223 163.665 1.00 128.03 ? 654  ALA A O   1 
ATOM 383  C CB  . ALA A 1 643  ? 175.780 178.035 166.638 1.00 136.65 ? 654  ALA A CB  1 
ATOM 384  N N   . ALA A 1 644  ? 176.511 180.223 164.451 1.00 129.71 ? 655  ALA A N   1 
ATOM 385  C CA  . ALA A 1 644  ? 176.389 180.776 163.107 1.00 127.13 ? 655  ALA A CA  1 
ATOM 386  C C   . ALA A 1 644  ? 177.756 181.090 162.513 1.00 127.68 ? 655  ALA A C   1 
ATOM 387  O O   . ALA A 1 644  ? 177.964 180.930 161.304 1.00 126.67 ? 655  ALA A O   1 
ATOM 388  C CB  . ALA A 1 644  ? 175.511 182.026 163.129 1.00 125.43 ? 655  ALA A CB  1 
ATOM 389  N N   . ALA A 1 645  ? 178.697 181.544 163.345 1.00 129.51 ? 656  ALA A N   1 
ATOM 390  C CA  . ALA A 1 645  ? 180.010 181.938 162.843 1.00 125.78 ? 656  ALA A CA  1 
ATOM 391  C C   . ALA A 1 645  ? 180.776 180.748 162.278 1.00 125.59 ? 656  ALA A C   1 
ATOM 392  O O   . ALA A 1 645  ? 181.457 180.870 161.251 1.00 124.96 ? 656  ALA A O   1 
ATOM 393  C CB  . ALA A 1 645  ? 180.815 182.617 163.950 1.00 122.45 ? 656  ALA A CB  1 
ATOM 394  N N   . ARG A 1 646  ? 180.696 179.591 162.943 1.00 125.81 ? 657  ARG A N   1 
ATOM 395  C CA  . ARG A 1 646  ? 181.418 178.423 162.445 1.00 126.71 ? 657  ARG A CA  1 
ATOM 396  C C   . ARG A 1 646  ? 180.860 177.949 161.109 1.00 124.32 ? 657  ARG A C   1 
ATOM 397  O O   . ARG A 1 646  ? 181.607 177.422 160.277 1.00 121.17 ? 657  ARG A O   1 
ATOM 398  C CB  . ARG A 1 646  ? 181.386 177.290 163.473 1.00 130.49 ? 657  ARG A CB  1 
ATOM 399  C CG  . ARG A 1 646  ? 179.999 176.871 163.921 1.00 129.41 ? 657  ARG A CG  1 
ATOM 400  C CD  . ARG A 1 646  ? 180.003 175.446 164.448 1.00 127.46 ? 657  ARG A CD  1 
ATOM 401  N NE  . ARG A 1 646  ? 181.005 175.251 165.490 1.00 132.65 ? 657  ARG A NE  1 
ATOM 402  C CZ  . ARG A 1 646  ? 181.534 174.077 165.810 1.00 135.46 ? 657  ARG A CZ  1 
ATOM 403  N NH1 . ARG A 1 646  ? 181.178 172.966 165.187 1.00 138.64 ? 657  ARG A NH1 1 
ATOM 404  N NH2 . ARG A 1 646  ? 182.442 174.018 166.779 1.00 124.73 ? 657  ARG A NH2 1 
ATOM 405  N N   . SER A 1 647  ? 179.556 178.126 160.884 1.00 122.77 ? 658  SER A N   1 
ATOM 406  C CA  . SER A 1 647  ? 178.981 177.785 159.587 1.00 122.51 ? 658  SER A CA  1 
ATOM 407  C C   . SER A 1 647  ? 179.347 178.822 158.532 1.00 123.47 ? 658  SER A C   1 
ATOM 408  O O   . SER A 1 647  ? 179.579 178.476 157.368 1.00 119.88 ? 658  SER A O   1 
ATOM 409  C CB  . SER A 1 647  ? 177.463 177.648 159.705 1.00 119.86 ? 658  SER A CB  1 
ATOM 410  O OG  . SER A 1 647  ? 176.911 177.067 158.537 1.00 118.05 ? 658  SER A OG  1 
ATOM 411  N N   . GLN A 1 648  ? 179.395 180.099 158.919 1.00 125.71 ? 659  GLN A N   1 
ATOM 412  C CA  . GLN A 1 648  ? 179.754 181.153 157.973 1.00 119.05 ? 659  GLN A CA  1 
ATOM 413  C C   . GLN A 1 648  ? 181.195 181.007 157.501 1.00 114.23 ? 659  GLN A C   1 
ATOM 414  O O   . GLN A 1 648  ? 181.497 181.229 156.322 1.00 111.75 ? 659  GLN A O   1 
ATOM 415  C CB  . GLN A 1 648  ? 179.539 182.528 158.607 1.00 114.98 ? 659  GLN A CB  1 
ATOM 416  C CG  . GLN A 1 648  ? 178.088 182.885 158.869 1.00 115.26 ? 659  GLN A CG  1 
ATOM 417  C CD  . GLN A 1 648  ? 177.938 183.914 159.971 1.00 114.70 ? 659  GLN A CD  1 
ATOM 418  O OE1 . GLN A 1 648  ? 178.926 184.451 160.472 1.00 113.42 ? 659  GLN A OE1 1 
ATOM 419  N NE2 . GLN A 1 648  ? 176.698 184.195 160.356 1.00 114.73 ? 659  GLN A NE2 1 
ATOM 420  N N   . LEU A 1 649  ? 182.101 180.640 158.412 1.00 110.45 ? 660  LEU A N   1 
ATOM 421  C CA  . LEU A 1 649  ? 183.521 180.603 158.072 1.00 109.07 ? 660  LEU A CA  1 
ATOM 422  C C   . LEU A 1 649  ? 183.820 179.584 156.978 1.00 113.73 ? 660  LEU A C   1 
ATOM 423  O O   . LEU A 1 649  ? 184.785 179.752 156.223 1.00 113.40 ? 660  LEU A O   1 
ATOM 424  C CB  . LEU A 1 649  ? 184.349 180.306 159.325 1.00 103.20 ? 660  LEU A CB  1 
ATOM 425  C CG  . LEU A 1 649  ? 185.865 180.513 159.248 1.00 88.67  ? 660  LEU A CG  1 
ATOM 426  C CD1 . LEU A 1 649  ? 186.383 181.060 160.567 1.00 86.00  ? 660  LEU A CD1 1 
ATOM 427  C CD2 . LEU A 1 649  ? 186.585 179.220 158.896 1.00 87.63  ? 660  LEU A CD2 1 
ATOM 428  N N   . ALA A 1 650  ? 183.010 178.528 156.872 1.00 115.07 ? 661  ALA A N   1 
ATOM 429  C CA  . ALA A 1 650  ? 183.254 177.500 155.866 1.00 113.20 ? 661  ALA A CA  1 
ATOM 430  C C   . ALA A 1 650  ? 183.046 178.010 154.445 1.00 115.68 ? 661  ALA A C   1 
ATOM 431  O O   . ALA A 1 650  ? 183.504 177.365 153.495 1.00 115.96 ? 661  ALA A O   1 
ATOM 432  C CB  . ALA A 1 650  ? 182.352 176.291 156.120 1.00 107.30 ? 661  ALA A CB  1 
ATOM 433  N N   . LYS A 1 651  ? 182.372 179.148 154.276 1.00 115.61 ? 662  LYS A N   1 
ATOM 434  C CA  . LYS A 1 651  ? 182.106 179.681 152.945 1.00 115.32 ? 662  LYS A CA  1 
ATOM 435  C C   . LYS A 1 651  ? 183.314 180.375 152.330 1.00 115.17 ? 662  LYS A C   1 
ATOM 436  O O   . LYS A 1 651  ? 183.265 180.742 151.150 1.00 115.10 ? 662  LYS A O   1 
ATOM 437  C CB  . LYS A 1 651  ? 180.931 180.659 152.996 1.00 114.82 ? 662  LYS A CB  1 
ATOM 438  C CG  . LYS A 1 651  ? 179.666 180.081 153.606 1.00 114.41 ? 662  LYS A CG  1 
ATOM 439  C CD  . LYS A 1 651  ? 178.515 181.070 153.527 1.00 114.07 ? 662  LYS A CD  1 
ATOM 440  C CE  . LYS A 1 651  ? 178.030 181.237 152.097 1.00 110.52 ? 662  LYS A CE  1 
ATOM 441  N NZ  . LYS A 1 651  ? 177.396 179.995 151.577 1.00 106.14 ? 662  LYS A NZ  1 
ATOM 442  N N   . LEU A 1 652  ? 184.387 180.567 153.094 1.00 116.60 ? 663  LEU A N   1 
ATOM 443  C CA  . LEU A 1 652  ? 185.541 181.292 152.589 1.00 115.75 ? 663  LEU A CA  1 
ATOM 444  C C   . LEU A 1 652  ? 186.248 180.490 151.496 1.00 118.77 ? 663  LEU A C   1 
ATOM 445  O O   . LEU A 1 652  ? 186.236 179.255 151.511 1.00 120.77 ? 663  LEU A O   1 
ATOM 446  C CB  . LEU A 1 652  ? 186.523 181.597 153.719 1.00 112.32 ? 663  LEU A CB  1 
ATOM 447  C CG  . LEU A 1 652  ? 186.337 182.911 154.481 1.00 99.83  ? 663  LEU A CG  1 
ATOM 448  C CD1 . LEU A 1 652  ? 186.545 184.099 153.554 1.00 103.22 ? 663  LEU A CD1 1 
ATOM 449  C CD2 . LEU A 1 652  ? 184.982 182.979 155.164 1.00 106.32 ? 663  LEU A CD2 1 
ATOM 450  N N   . PRO A 1 653  ? 186.866 181.170 150.530 1.00 114.86 ? 664  PRO A N   1 
ATOM 451  C CA  . PRO A 1 653  ? 187.683 180.461 149.540 1.00 116.90 ? 664  PRO A CA  1 
ATOM 452  C C   . PRO A 1 653  ? 188.903 179.827 150.189 1.00 125.30 ? 664  PRO A C   1 
ATOM 453  O O   . PRO A 1 653  ? 189.324 180.209 151.283 1.00 123.12 ? 664  PRO A O   1 
ATOM 454  C CB  . PRO A 1 653  ? 188.082 181.564 148.550 1.00 115.84 ? 664  PRO A CB  1 
ATOM 455  C CG  . PRO A 1 653  ? 187.077 182.654 148.762 1.00 114.91 ? 664  PRO A CG  1 
ATOM 456  C CD  . PRO A 1 653  ? 186.737 182.602 150.217 1.00 114.38 ? 664  PRO A CD  1 
ATOM 457  N N   . ALA A 1 654  ? 189.466 178.837 149.499 1.00 132.56 ? 665  ALA A N   1 
ATOM 458  C CA  . ALA A 1 654  ? 190.584 178.075 150.034 1.00 133.58 ? 665  ALA A CA  1 
ATOM 459  C C   . ALA A 1 654  ? 191.800 178.969 150.274 1.00 136.25 ? 665  ALA A C   1 
ATOM 460  O O   . ALA A 1 654  ? 191.872 180.113 149.817 1.00 136.87 ? 665  ALA A O   1 
ATOM 461  C CB  . ALA A 1 654  ? 190.953 176.933 149.088 1.00 131.88 ? 665  ALA A CB  1 
ATOM 462  N N   . THR A 1 655  ? 192.772 178.417 151.001 1.00 137.24 ? 666  THR A N   1 
ATOM 463  C CA  . THR A 1 655  ? 193.980 179.142 151.375 1.00 136.64 ? 666  THR A CA  1 
ATOM 464  C C   . THR A 1 655  ? 195.087 178.931 150.350 1.00 138.01 ? 666  THR A C   1 
ATOM 465  O O   . THR A 1 655  ? 196.271 178.924 150.704 1.00 131.69 ? 666  THR A O   1 
ATOM 466  C CB  . THR A 1 655  ? 194.462 178.712 152.763 1.00 121.94 ? 666  THR A CB  1 
ATOM 467  O OG1 . THR A 1 655  ? 194.640 177.290 152.792 1.00 119.76 ? 666  THR A OG1 1 
ATOM 468  C CG2 . THR A 1 655  ? 193.451 179.114 153.826 1.00 113.03 ? 666  THR A CG2 1 
ATOM 469  N N   . ASP A 1 656  ? 194.704 178.729 149.084 1.00 140.39 ? 667  ASP A N   1 
ATOM 470  C CA  . ASP A 1 656  ? 195.686 178.509 148.024 1.00 140.69 ? 667  ASP A CA  1 
ATOM 471  C C   . ASP A 1 656  ? 196.747 179.602 148.007 1.00 140.46 ? 667  ASP A C   1 
ATOM 472  O O   . ASP A 1 656  ? 197.936 179.320 147.814 1.00 136.37 ? 667  ASP A O   1 
ATOM 473  C CB  . ASP A 1 656  ? 194.980 178.426 146.670 1.00 135.36 ? 667  ASP A CB  1 
ATOM 474  C CG  . ASP A 1 656  ? 195.866 177.845 145.586 1.00 136.78 ? 667  ASP A CG  1 
ATOM 475  O OD1 . ASP A 1 656  ? 196.891 177.218 145.926 1.00 139.74 ? 667  ASP A OD1 1 
ATOM 476  O OD2 . ASP A 1 656  ? 195.538 178.017 144.393 1.00 135.71 ? 667  ASP A OD2 1 
ATOM 477  N N   . ASN A 1 657  ? 196.342 180.854 148.209 1.00 139.57 ? 668  ASN A N   1 
ATOM 478  C CA  . ASN A 1 657  ? 197.294 181.958 148.303 1.00 131.34 ? 668  ASN A CA  1 
ATOM 479  C C   . ASN A 1 657  ? 196.654 183.080 149.104 1.00 120.75 ? 668  ASN A C   1 
ATOM 480  O O   . ASN A 1 657  ? 195.660 183.667 148.665 1.00 118.79 ? 668  ASN A O   1 
ATOM 481  C CB  . ASN A 1 657  ? 197.720 182.441 146.912 1.00 130.97 ? 668  ASN A CB  1 
ATOM 482  C CG  . ASN A 1 657  ? 196.541 182.740 146.008 1.00 134.35 ? 668  ASN A CG  1 
ATOM 483  O OD1 . ASN A 1 657  ? 195.684 181.886 145.784 1.00 137.00 ? 668  ASN A OD1 1 
ATOM 484  N ND2 . ASN A 1 657  ? 196.495 183.957 145.479 1.00 135.43 ? 668  ASN A ND2 1 
ATOM 485  N N   . ALA A 1 658  ? 197.213 183.368 150.277 1.00 108.76 ? 669  ALA A N   1 
ATOM 486  C CA  . ALA A 1 658  ? 196.680 184.407 151.144 1.00 93.81  ? 669  ALA A CA  1 
ATOM 487  C C   . ALA A 1 658  ? 197.805 184.959 152.006 1.00 92.65  ? 669  ALA A C   1 
ATOM 488  O O   . ALA A 1 658  ? 198.815 184.289 152.235 1.00 95.92  ? 669  ALA A O   1 
ATOM 489  C CB  . ALA A 1 658  ? 195.542 183.877 152.024 1.00 86.40  ? 669  ALA A CB  1 
ATOM 490  N N   . SER A 1 659  ? 197.614 186.187 152.481 1.00 90.14  ? 670  SER A N   1 
ATOM 491  C CA  . SER A 1 659  ? 198.617 186.839 153.308 1.00 86.49  ? 670  SER A CA  1 
ATOM 492  C C   . SER A 1 659  ? 198.643 186.233 154.709 1.00 77.15  ? 670  SER A C   1 
ATOM 493  O O   . SER A 1 659  ? 197.720 185.533 155.135 1.00 74.12  ? 670  SER A O   1 
ATOM 494  C CB  . SER A 1 659  ? 198.345 188.341 153.392 1.00 86.59  ? 670  SER A CB  1 
ATOM 495  O OG  . SER A 1 659  ? 197.339 188.624 154.349 1.00 82.90  ? 670  SER A OG  1 
ATOM 496  N N   . LEU A 1 660  ? 199.734 186.512 155.428 1.00 74.82  ? 671  LEU A N   1 
ATOM 497  C CA  . LEU A 1 660  ? 199.870 186.021 156.796 1.00 72.09  ? 671  LEU A CA  1 
ATOM 498  C C   . LEU A 1 660  ? 198.814 186.625 157.711 1.00 69.50  ? 671  LEU A C   1 
ATOM 499  O O   . LEU A 1 660  ? 198.307 185.951 158.615 1.00 70.07  ? 671  LEU A O   1 
ATOM 500  C CB  . LEU A 1 660  ? 201.269 186.330 157.330 1.00 74.45  ? 671  LEU A CB  1 
ATOM 501  C CG  . LEU A 1 660  ? 202.456 185.759 156.556 1.00 75.82  ? 671  LEU A CG  1 
ATOM 502  C CD1 . LEU A 1 660  ? 203.677 186.633 156.763 1.00 75.51  ? 671  LEU A CD1 1 
ATOM 503  C CD2 . LEU A 1 660  ? 202.741 184.329 156.981 1.00 73.45  ? 671  LEU A CD2 1 
ATOM 504  N N   . ASN A 1 661  ? 198.481 187.901 157.502 1.00 71.00  ? 672  ASN A N   1 
ATOM 505  C CA  . ASN A 1 661  ? 197.515 188.568 158.368 1.00 66.12  ? 672  ASN A CA  1 
ATOM 506  C C   . ASN A 1 661  ? 196.130 187.942 158.263 1.00 70.17  ? 672  ASN A C   1 
ATOM 507  O O   . ASN A 1 661  ? 195.433 187.814 159.276 1.00 70.93  ? 672  ASN A O   1 
ATOM 508  C CB  . ASN A 1 661  ? 197.449 190.057 158.030 1.00 62.42  ? 672  ASN A CB  1 
ATOM 509  C CG  . ASN A 1 661  ? 196.859 190.883 159.154 1.00 59.22  ? 672  ASN A CG  1 
ATOM 510  O OD1 . ASN A 1 661  ? 197.383 190.902 160.268 1.00 57.00  ? 672  ASN A OD1 1 
ATOM 511  N ND2 . ASN A 1 661  ? 195.760 191.572 158.868 1.00 61.82  ? 672  ASN A ND2 1 
ATOM 512  N N   . THR A 1 662  ? 195.715 187.550 157.059 1.00 68.91  ? 673  THR A N   1 
ATOM 513  C CA  . THR A 1 662  ? 194.412 186.917 156.889 1.00 66.30  ? 673  THR A CA  1 
ATOM 514  C C   . THR A 1 662  ? 194.395 185.517 157.492 1.00 65.32  ? 673  THR A C   1 
ATOM 515  O O   . THR A 1 662  ? 193.424 185.124 158.152 1.00 66.66  ? 673  THR A O   1 
ATOM 516  C CB  . THR A 1 662  ? 194.046 186.869 155.404 1.00 66.34  ? 673  THR A CB  1 
ATOM 517  O OG1 . THR A 1 662  ? 194.358 188.127 154.793 1.00 72.06  ? 673  THR A OG1 1 
ATOM 518  C CG2 . THR A 1 662  ? 192.565 186.583 155.227 1.00 63.80  ? 673  THR A CG2 1 
ATOM 519  N N   . GLN A 1 663  ? 195.469 184.752 157.278 1.00 63.07  ? 674  GLN A N   1 
ATOM 520  C CA  . GLN A 1 663  ? 195.536 183.403 157.827 1.00 60.34  ? 674  GLN A CA  1 
ATOM 521  C C   . GLN A 1 663  ? 195.596 183.416 159.348 1.00 60.41  ? 674  GLN A C   1 
ATOM 522  O O   . GLN A 1 663  ? 195.056 182.512 159.991 1.00 62.61  ? 674  GLN A O   1 
ATOM 523  C CB  . GLN A 1 663  ? 196.739 182.658 157.252 1.00 55.81  ? 674  GLN A CB  1 
ATOM 524  C CG  . GLN A 1 663  ? 196.596 182.309 155.782 1.00 61.95  ? 674  GLN A CG  1 
ATOM 525  C CD  . GLN A 1 663  ? 197.667 181.349 155.309 1.00 75.17  ? 674  GLN A CD  1 
ATOM 526  O OE1 . GLN A 1 663  ? 197.846 180.272 155.877 1.00 76.17  ? 674  GLN A OE1 1 
ATOM 527  N NE2 . GLN A 1 663  ? 198.387 181.735 154.262 1.00 84.15  ? 674  GLN A NE2 1 
ATOM 528  N N   . ARG A 1 664  ? 196.244 184.423 159.939 1.00 58.32  ? 675  ARG A N   1 
ATOM 529  C CA  . ARG A 1 664  ? 196.248 184.544 161.394 1.00 58.46  ? 675  ARG A CA  1 
ATOM 530  C C   . ARG A 1 664  ? 194.840 184.753 161.934 1.00 63.24  ? 675  ARG A C   1 
ATOM 531  O O   . ARG A 1 664  ? 194.448 184.128 162.928 1.00 72.77  ? 675  ARG A O   1 
ATOM 532  C CB  . ARG A 1 664  ? 197.161 185.693 161.819 1.00 62.16  ? 675  ARG A CB  1 
ATOM 533  C CG  . ARG A 1 664  ? 197.534 185.689 163.289 1.00 57.94  ? 675  ARG A CG  1 
ATOM 534  C CD  . ARG A 1 664  ? 198.234 186.982 163.665 1.00 52.21  ? 675  ARG A CD  1 
ATOM 535  N NE  . ARG A 1 664  ? 197.291 188.077 163.863 1.00 50.17  ? 675  ARG A NE  1 
ATOM 536  C CZ  . ARG A 1 664  ? 197.035 189.013 162.959 1.00 56.98  ? 675  ARG A CZ  1 
ATOM 537  N NH1 . ARG A 1 664  ? 197.641 189.022 161.783 1.00 62.44  ? 675  ARG A NH1 1 
ATOM 538  N NH2 . ARG A 1 664  ? 196.150 189.964 163.243 1.00 53.10  ? 675  ARG A NH2 1 
ATOM 539  N N   . ARG A 1 665  ? 194.062 185.626 161.289 1.00 58.13  ? 676  ARG A N   1 
ATOM 540  C CA  . ARG A 1 665  ? 192.681 185.840 161.711 1.00 60.57  ? 676  ARG A CA  1 
ATOM 541  C C   . ARG A 1 665  ? 191.853 184.573 161.547 1.00 65.78  ? 676  ARG A C   1 
ATOM 542  O O   . ARG A 1 665  ? 191.048 184.232 162.424 1.00 68.23  ? 676  ARG A O   1 
ATOM 543  C CB  . ARG A 1 665  ? 192.063 186.991 160.919 1.00 63.78  ? 676  ARG A CB  1 
ATOM 544  C CG  . ARG A 1 665  ? 192.773 188.321 161.093 1.00 64.87  ? 676  ARG A CG  1 
ATOM 545  C CD  . ARG A 1 665  ? 192.323 189.019 162.363 1.00 74.12  ? 676  ARG A CD  1 
ATOM 546  N NE  . ARG A 1 665  ? 190.984 189.580 162.229 1.00 83.84  ? 676  ARG A NE  1 
ATOM 547  C CZ  . ARG A 1 665  ? 190.710 190.735 161.638 1.00 82.59  ? 676  ARG A CZ  1 
ATOM 548  N NH1 . ARG A 1 665  ? 191.664 191.487 161.114 1.00 85.74  ? 676  ARG A NH1 1 
ATOM 549  N NH2 . ARG A 1 665  ? 189.447 191.145 161.571 1.00 79.41  ? 676  ARG A NH2 1 
ATOM 550  N N   . VAL A 1 666  ? 192.036 183.864 160.431 1.00 61.80  ? 677  VAL A N   1 
ATOM 551  C CA  . VAL A 1 666  ? 191.301 182.619 160.211 1.00 55.33  ? 677  VAL A CA  1 
ATOM 552  C C   . VAL A 1 666  ? 191.645 181.599 161.291 1.00 62.38  ? 677  VAL A C   1 
ATOM 553  O O   . VAL A 1 666  ? 190.764 180.924 161.837 1.00 67.83  ? 677  VAL A O   1 
ATOM 554  C CB  . VAL A 1 666  ? 191.583 182.068 158.802 1.00 52.35  ? 677  VAL A CB  1 
ATOM 555  C CG1 . VAL A 1 666  ? 190.931 180.708 158.624 1.00 50.28  ? 677  VAL A CG1 1 
ATOM 556  C CG2 . VAL A 1 666  ? 191.076 183.034 157.747 1.00 60.96  ? 677  VAL A CG2 1 
ATOM 557  N N   . ALA A 1 667  ? 192.935 181.471 161.611 1.00 63.80  ? 678  ALA A N   1 
ATOM 558  C CA  . ALA A 1 667  ? 193.364 180.510 162.622 1.00 68.35  ? 678  ALA A CA  1 
ATOM 559  C C   . ALA A 1 667  ? 192.810 180.870 163.995 1.00 72.68  ? 678  ALA A C   1 
ATOM 560  O O   . ALA A 1 667  ? 192.359 179.995 164.742 1.00 80.29  ? 678  ALA A O   1 
ATOM 561  C CB  . ALA A 1 667  ? 194.891 180.436 162.657 1.00 70.91  ? 678  ALA A CB  1 
ATOM 562  N N   . LEU A 1 668  ? 192.842 182.158 164.348 1.00 69.46  ? 679  LEU A N   1 
ATOM 563  C CA  . LEU A 1 668  ? 192.291 182.580 165.632 1.00 67.03  ? 679  LEU A CA  1 
ATOM 564  C C   . LEU A 1 668  ? 190.796 182.299 165.709 1.00 72.59  ? 679  LEU A C   1 
ATOM 565  O O   . LEU A 1 668  ? 190.301 181.802 166.730 1.00 79.56  ? 679  LEU A O   1 
ATOM 566  C CB  . LEU A 1 668  ? 192.569 184.065 165.864 1.00 65.81  ? 679  LEU A CB  1 
ATOM 567  C CG  . LEU A 1 668  ? 193.991 184.461 166.267 1.00 69.33  ? 679  LEU A CG  1 
ATOM 568  C CD1 . LEU A 1 668  ? 193.966 185.722 167.114 1.00 70.95  ? 679  LEU A CD1 1 
ATOM 569  C CD2 . LEU A 1 668  ? 194.675 183.331 167.017 1.00 71.83  ? 679  LEU A CD2 1 
ATOM 570  N N   . ALA A 1 669  ? 190.062 182.603 164.636 1.00 71.94  ? 680  ALA A N   1 
ATOM 571  C CA  . ALA A 1 669  ? 188.628 182.337 164.620 1.00 79.82  ? 680  ALA A CA  1 
ATOM 572  C C   . ALA A 1 669  ? 188.348 180.847 164.761 1.00 85.35  ? 680  ALA A C   1 
ATOM 573  O O   . ALA A 1 669  ? 187.478 180.438 165.537 1.00 89.25  ? 680  ALA A O   1 
ATOM 574  C CB  . ALA A 1 669  ? 188.006 182.888 163.338 1.00 76.77  ? 680  ALA A CB  1 
ATOM 575  N N   . GLN A 1 670  ? 189.094 180.015 164.030 1.00 82.85  ? 681  GLN A N   1 
ATOM 576  C CA  . GLN A 1 670  ? 188.894 178.572 164.119 1.00 82.86  ? 681  GLN A CA  1 
ATOM 577  C C   . GLN A 1 670  ? 189.206 178.056 165.518 1.00 88.68  ? 681  GLN A C   1 
ATOM 578  O O   . GLN A 1 670  ? 188.502 177.181 166.036 1.00 95.60  ? 681  GLN A O   1 
ATOM 579  C CB  . GLN A 1 670  ? 189.754 177.857 163.076 1.00 83.82  ? 681  GLN A CB  1 
ATOM 580  C CG  . GLN A 1 670  ? 189.226 177.954 161.650 1.00 84.46  ? 681  GLN A CG  1 
ATOM 581  C CD  . GLN A 1 670  ? 188.131 176.944 161.350 1.00 89.58  ? 681  GLN A CD  1 
ATOM 582  O OE1 . GLN A 1 670  ? 187.292 176.644 162.199 1.00 91.87  ? 681  GLN A OE1 1 
ATOM 583  N NE2 . GLN A 1 670  ? 188.137 176.415 160.132 1.00 90.88  ? 681  GLN A NE2 1 
ATOM 584  N N   . ALA A 1 671  ? 190.264 178.579 166.142 1.00 87.26  ? 682  ALA A N   1 
ATOM 585  C CA  . ALA A 1 671  ? 190.608 178.166 167.499 1.00 89.32  ? 682  ALA A CA  1 
ATOM 586  C C   . ALA A 1 671  ? 189.505 178.538 168.482 1.00 95.43  ? 682  ALA A C   1 
ATOM 587  O O   . ALA A 1 671  ? 189.117 177.729 169.332 1.00 95.76  ? 682  ALA A O   1 
ATOM 588  C CB  . ALA A 1 671  ? 191.938 178.794 167.917 1.00 81.66  ? 682  ALA A CB  1 
ATOM 589  N N   . GLN A 1 672  ? 188.983 179.762 168.379 1.00 99.31  ? 683  GLN A N   1 
ATOM 590  C CA  . GLN A 1 672  ? 187.942 180.194 169.304 1.00 98.86  ? 683  GLN A CA  1 
ATOM 591  C C   . GLN A 1 672  ? 186.564 179.650 168.945 1.00 99.49  ? 683  GLN A C   1 
ATOM 592  O O   . GLN A 1 672  ? 185.669 179.667 169.796 1.00 102.86 ? 683  GLN A O   1 
ATOM 593  C CB  . GLN A 1 672  ? 187.903 181.722 169.381 1.00 95.48  ? 683  GLN A CB  1 
ATOM 594  C CG  . GLN A 1 672  ? 187.506 182.411 168.093 1.00 98.30  ? 683  GLN A CG  1 
ATOM 595  C CD  . GLN A 1 672  ? 187.740 183.909 168.140 1.00 107.01 ? 683  GLN A CD  1 
ATOM 596  O OE1 . GLN A 1 672  ? 188.120 184.457 169.175 1.00 107.52 ? 683  GLN A OE1 1 
ATOM 597  N NE2 . GLN A 1 672  ? 187.516 184.579 167.016 1.00 112.23 ? 683  GLN A NE2 1 
ATOM 598  N N   . LEU A 1 673  ? 186.368 179.168 167.715 1.00 96.26  ? 684  LEU A N   1 
ATOM 599  C CA  . LEU A 1 673  ? 185.115 178.507 167.365 1.00 102.21 ? 684  LEU A CA  1 
ATOM 600  C C   . LEU A 1 673  ? 185.033 177.080 167.895 1.00 107.40 ? 684  LEU A C   1 
ATOM 601  O O   . LEU A 1 673  ? 183.966 176.465 167.799 1.00 112.50 ? 684  LEU A O   1 
ATOM 602  C CB  . LEU A 1 673  ? 184.915 178.502 165.848 1.00 102.85 ? 684  LEU A CB  1 
ATOM 603  C CG  . LEU A 1 673  ? 184.457 179.808 165.189 1.00 105.28 ? 684  LEU A CG  1 
ATOM 604  C CD1 . LEU A 1 673  ? 184.642 179.743 163.680 1.00 100.72 ? 684  LEU A CD1 1 
ATOM 605  C CD2 . LEU A 1 673  ? 183.010 180.114 165.539 1.00 112.71 ? 684  LEU A CD2 1 
ATOM 606  N N   . GLY A 1 674  ? 186.121 176.544 168.448 1.00 105.12 ? 685  GLY A N   1 
ATOM 607  C CA  . GLY A 1 674  ? 186.144 175.194 168.971 1.00 105.67 ? 685  GLY A CA  1 
ATOM 608  C C   . GLY A 1 674  ? 186.808 174.162 168.084 1.00 104.99 ? 685  GLY A C   1 
ATOM 609  O O   . GLY A 1 674  ? 186.920 173.000 168.497 1.00 103.64 ? 685  GLY A O   1 
ATOM 610  N N   . ASP A 1 675  ? 187.252 174.542 166.885 1.00 105.32 ? 686  ASP A N   1 
ATOM 611  C CA  . ASP A 1 675  ? 187.948 173.619 165.986 1.00 105.33 ? 686  ASP A CA  1 
ATOM 612  C C   . ASP A 1 675  ? 189.450 173.837 166.195 1.00 104.64 ? 686  ASP A C   1 
ATOM 613  O O   . ASP A 1 675  ? 190.093 174.681 165.566 1.00 101.44 ? 686  ASP A O   1 
ATOM 614  C CB  . ASP A 1 675  ? 187.499 173.845 164.541 1.00 102.01 ? 686  ASP A CB  1 
ATOM 615  C CG  . ASP A 1 675  ? 188.369 173.119 163.495 1.00 101.76 ? 686  ASP A CG  1 
ATOM 616  O OD1 . ASP A 1 675  ? 187.821 172.796 162.414 1.00 106.85 ? 686  ASP A OD1 1 
ATOM 617  O OD2 . ASP A 1 675  ? 189.557 172.832 163.726 1.00 99.14  ? 686  ASP A OD2 1 
ATOM 618  N N   . THR A 1 676  ? 190.001 173.074 167.144 1.00 105.18 ? 687  THR A N   1 
ATOM 619  C CA  . THR A 1 676  ? 191.405 173.248 167.508 1.00 102.55 ? 687  THR A CA  1 
ATOM 620  C C   . THR A 1 676  ? 192.344 172.684 166.448 1.00 100.27 ? 687  THR A C   1 
ATOM 621  O O   . THR A 1 676  ? 193.454 173.195 166.273 1.00 101.47 ? 687  THR A O   1 
ATOM 622  C CB  . THR A 1 676  ? 191.685 172.596 168.863 1.00 108.51 ? 687  THR A CB  1 
ATOM 623  O OG1 . THR A 1 676  ? 190.711 173.031 169.817 1.00 115.99 ? 687  THR A OG1 1 
ATOM 624  C CG2 . THR A 1 676  ? 193.077 172.977 169.367 1.00 102.52 ? 687  THR A CG2 1 
ATOM 625  N N   . ALA A 1 677  ? 191.927 171.633 165.737 1.00 99.17  ? 688  ALA A N   1 
ATOM 626  C CA  . ALA A 1 677  ? 192.845 170.949 164.829 1.00 101.42 ? 688  ALA A CA  1 
ATOM 627  C C   . ALA A 1 677  ? 193.217 171.822 163.635 1.00 99.29  ? 688  ALA A C   1 
ATOM 628  O O   . ALA A 1 677  ? 194.394 171.894 163.255 1.00 96.84  ? 688  ALA A O   1 
ATOM 629  C CB  . ALA A 1 677  ? 192.229 169.629 164.364 1.00 100.04 ? 688  ALA A CB  1 
ATOM 630  N N   . ALA A 1 678  ? 192.230 172.485 163.025 1.00 96.97  ? 689  ALA A N   1 
ATOM 631  C CA  . ALA A 1 678  ? 192.516 173.351 161.885 1.00 95.57  ? 689  ALA A CA  1 
ATOM 632  C C   . ALA A 1 678  ? 193.397 174.523 162.292 1.00 94.89  ? 689  ALA A C   1 
ATOM 633  O O   . ALA A 1 678  ? 194.319 174.897 161.559 1.00 92.40  ? 689  ALA A O   1 
ATOM 634  C CB  . ALA A 1 678  ? 191.216 173.851 161.258 1.00 95.72  ? 689  ALA A CB  1 
ATOM 635  N N   . ALA A 1 679  ? 193.131 175.115 163.458 1.00 95.46  ? 690  ALA A N   1 
ATOM 636  C CA  . ALA A 1 679  ? 193.979 176.196 163.947 1.00 87.80  ? 690  ALA A CA  1 
ATOM 637  C C   . ALA A 1 679  ? 195.394 175.704 164.222 1.00 88.58  ? 690  ALA A C   1 
ATOM 638  O O   . ALA A 1 679  ? 196.371 176.403 163.929 1.00 89.47  ? 690  ALA A O   1 
ATOM 639  C CB  . ALA A 1 679  ? 193.368 176.815 165.204 1.00 85.10  ? 690  ALA A CB  1 
ATOM 640  N N   . GLN A 1 680  ? 195.524 174.500 164.785 1.00 92.03  ? 691  GLN A N   1 
ATOM 641  C CA  . GLN A 1 680  ? 196.841 173.962 165.107 1.00 91.93  ? 691  GLN A CA  1 
ATOM 642  C C   . GLN A 1 680  ? 197.649 173.731 163.837 1.00 93.89  ? 691  GLN A C   1 
ATOM 643  O O   . GLN A 1 680  ? 198.831 174.084 163.767 1.00 95.18  ? 691  GLN A O   1 
ATOM 644  C CB  . GLN A 1 680  ? 196.673 172.688 165.962 1.00 92.14  ? 691  GLN A CB  1 
ATOM 645  C CG  . GLN A 1 680  ? 197.885 171.748 166.257 1.00 97.90  ? 691  GLN A CG  1 
ATOM 646  C CD  . GLN A 1 680  ? 198.656 171.204 165.057 1.00 105.73 ? 691  GLN A CD  1 
ATOM 647  O OE1 . GLN A 1 680  ? 198.103 171.012 163.974 1.00 108.28 ? 691  GLN A OE1 1 
ATOM 648  N NE2 . GLN A 1 680  ? 199.948 170.968 165.250 1.00 99.30  ? 691  GLN A NE2 1 
ATOM 649  N N   . ARG A 1 681  ? 197.019 173.156 162.808 1.00 93.58  ? 692  ARG A N   1 
ATOM 650  C CA  . ARG A 1 681  ? 197.737 172.943 161.554 1.00 95.04  ? 692  ARG A CA  1 
ATOM 651  C C   . ARG A 1 681  ? 198.043 174.262 160.850 1.00 89.19  ? 692  ARG A C   1 
ATOM 652  O O   . ARG A 1 681  ? 199.124 174.412 160.263 1.00 86.24  ? 692  ARG A O   1 
ATOM 653  C CB  . ARG A 1 681  ? 196.951 171.996 160.643 1.00 97.58  ? 692  ARG A CB  1 
ATOM 654  C CG  . ARG A 1 681  ? 195.652 172.552 160.094 1.00 97.77  ? 692  ARG A CG  1 
ATOM 655  C CD  . ARG A 1 681  ? 194.799 171.463 159.472 1.00 101.70 ? 692  ARG A CD  1 
ATOM 656  N NE  . ARG A 1 681  ? 194.344 170.499 160.466 1.00 104.87 ? 692  ARG A NE  1 
ATOM 657  C CZ  . ARG A 1 681  ? 193.548 169.472 160.203 1.00 110.21 ? 692  ARG A CZ  1 
ATOM 658  N NH1 . ARG A 1 681  ? 193.090 169.248 158.982 1.00 111.60 ? 692  ARG A NH1 1 
ATOM 659  N NH2 . ARG A 1 681  ? 193.202 168.650 161.190 1.00 106.88 ? 692  ARG A NH2 1 
ATOM 660  N N   . THR A 1 682  ? 197.128 175.234 160.916 1.00 87.86  ? 693  THR A N   1 
ATOM 661  C CA  . THR A 1 682  ? 197.389 176.536 160.312 1.00 85.08  ? 693  THR A CA  1 
ATOM 662  C C   . THR A 1 682  ? 198.577 177.217 160.978 1.00 83.16  ? 693  THR A C   1 
ATOM 663  O O   . THR A 1 682  ? 199.440 177.781 160.299 1.00 84.43  ? 693  THR A O   1 
ATOM 664  C CB  . THR A 1 682  ? 196.144 177.419 160.399 1.00 82.26  ? 693  THR A CB  1 
ATOM 665  O OG1 . THR A 1 682  ? 195.022 176.725 159.840 1.00 86.89  ? 693  THR A OG1 1 
ATOM 666  C CG2 . THR A 1 682  ? 196.361 178.717 159.632 1.00 75.76  ? 693  THR A CG2 1 
ATOM 667  N N   . PHE A 1 683  ? 198.649 177.160 162.310 1.00 81.27  ? 694  PHE A N   1 
ATOM 668  C CA  . PHE A 1 683  ? 199.785 177.758 163.003 1.00 76.31  ? 694  PHE A CA  1 
ATOM 669  C C   . PHE A 1 683  ? 201.071 176.981 162.752 1.00 81.67  ? 694  PHE A C   1 
ATOM 670  O O   . PHE A 1 683  ? 202.144 177.585 162.647 1.00 84.79  ? 694  PHE A O   1 
ATOM 671  C CB  . PHE A 1 683  ? 199.501 177.858 164.501 1.00 68.83  ? 694  PHE A CB  1 
ATOM 672  C CG  . PHE A 1 683  ? 198.679 179.057 164.879 1.00 71.58  ? 694  PHE A CG  1 
ATOM 673  C CD1 . PHE A 1 683  ? 199.164 180.337 164.669 1.00 73.19  ? 694  PHE A CD1 1 
ATOM 674  C CD2 . PHE A 1 683  ? 197.425 178.906 165.446 1.00 75.23  ? 694  PHE A CD2 1 
ATOM 675  C CE1 . PHE A 1 683  ? 198.413 181.444 165.014 1.00 69.93  ? 694  PHE A CE1 1 
ATOM 676  C CE2 . PHE A 1 683  ? 196.670 180.009 165.794 1.00 72.75  ? 694  PHE A CE2 1 
ATOM 677  C CZ  . PHE A 1 683  ? 197.165 181.279 165.577 1.00 67.94  ? 694  PHE A CZ  1 
ATOM 678  N N   . ASN A 1 684  ? 200.988 175.652 162.649 1.00 83.43  ? 695  ASN A N   1 
ATOM 679  C CA  . ASN A 1 684  ? 202.173 174.864 162.328 1.00 86.52  ? 695  ASN A CA  1 
ATOM 680  C C   . ASN A 1 684  ? 202.711 175.216 160.948 1.00 86.48  ? 695  ASN A C   1 
ATOM 681  O O   . ASN A 1 684  ? 203.926 175.176 160.726 1.00 82.71  ? 695  ASN A O   1 
ATOM 682  C CB  . ASN A 1 684  ? 201.849 173.371 162.424 1.00 89.07  ? 695  ASN A CB  1 
ATOM 683  C CG  . ASN A 1 684  ? 202.916 172.492 161.793 1.00 93.11  ? 695  ASN A CG  1 
ATOM 684  O OD1 . ASN A 1 684  ? 202.985 172.350 160.571 1.00 96.70  ? 695  ASN A OD1 1 
ATOM 685  N ND2 . ASN A 1 684  ? 203.758 171.897 162.630 1.00 92.34  ? 695  ASN A ND2 1 
ATOM 686  N N   . LYS A 1 685  ? 201.825 175.552 160.009 1.00 88.57  ? 696  LYS A N   1 
ATOM 687  C CA  . LYS A 1 685  ? 202.279 176.009 158.699 1.00 85.91  ? 696  LYS A CA  1 
ATOM 688  C C   . LYS A 1 685  ? 202.785 177.449 158.747 1.00 80.15  ? 696  LYS A C   1 
ATOM 689  O O   . LYS A 1 685  ? 203.735 177.800 158.039 1.00 78.87  ? 696  LYS A O   1 
ATOM 690  C CB  . LYS A 1 685  ? 201.147 175.875 157.680 1.00 90.12  ? 696  LYS A CB  1 
ATOM 691  C CG  . LYS A 1 685  ? 201.589 175.997 156.231 1.00 96.08  ? 696  LYS A CG  1 
ATOM 692  C CD  . LYS A 1 685  ? 200.404 175.895 155.282 1.00 100.19 ? 696  LYS A CD  1 
ATOM 693  C CE  . LYS A 1 685  ? 199.284 176.844 155.683 1.00 90.82  ? 696  LYS A CE  1 
ATOM 694  N NZ  . LYS A 1 685  ? 199.702 178.271 155.614 1.00 79.37  ? 696  LYS A NZ  1 
ATOM 695  N N   . LEU A 1 686  ? 202.162 178.291 159.574 1.00 78.10  ? 697  LEU A N   1 
ATOM 696  C CA  . LEU A 1 686  ? 202.475 179.717 159.577 1.00 77.04  ? 697  LEU A CA  1 
ATOM 697  C C   . LEU A 1 686  ? 203.813 180.002 160.249 1.00 80.24  ? 697  LEU A C   1 
ATOM 698  O O   . LEU A 1 686  ? 204.596 180.829 159.768 1.00 82.05  ? 697  LEU A O   1 
ATOM 699  C CB  . LEU A 1 686  ? 201.356 180.489 160.276 1.00 70.96  ? 697  LEU A CB  1 
ATOM 700  C CG  . LEU A 1 686  ? 200.132 180.860 159.440 1.00 70.34  ? 697  LEU A CG  1 
ATOM 701  C CD1 . LEU A 1 686  ? 199.090 181.546 160.306 1.00 68.89  ? 697  LEU A CD1 1 
ATOM 702  C CD2 . LEU A 1 686  ? 200.533 181.747 158.276 1.00 76.53  ? 697  LEU A CD2 1 
ATOM 703  N N   . ILE A 1 687  ? 204.085 179.334 161.374 1.00 76.40  ? 698  ILE A N   1 
ATOM 704  C CA  . ILE A 1 687  ? 205.201 179.745 162.230 1.00 69.60  ? 698  ILE A CA  1 
ATOM 705  C C   . ILE A 1 687  ? 206.548 179.685 161.517 1.00 73.40  ? 698  ILE A C   1 
ATOM 706  O O   . ILE A 1 687  ? 207.317 180.657 161.619 1.00 74.31  ? 698  ILE A O   1 
ATOM 707  C CB  . ILE A 1 687  ? 205.182 178.933 163.542 1.00 73.03  ? 698  ILE A CB  1 
ATOM 708  C CG1 . ILE A 1 687  ? 204.052 179.421 164.448 1.00 72.67  ? 698  ILE A CG1 1 
ATOM 709  C CG2 . ILE A 1 687  ? 206.511 179.042 164.260 1.00 75.39  ? 698  ILE A CG2 1 
ATOM 710  C CD1 . ILE A 1 687  ? 203.792 178.521 165.634 1.00 74.64  ? 698  ILE A CD1 1 
ATOM 711  N N   . PRO A 1 688  ? 206.910 178.609 160.804 1.00 74.19  ? 699  PRO A N   1 
ATOM 712  C CA  . PRO A 1 688  ? 208.172 178.655 160.042 1.00 70.52  ? 699  PRO A CA  1 
ATOM 713  C C   . PRO A 1 688  ? 208.208 179.764 159.005 1.00 73.13  ? 699  PRO A C   1 
ATOM 714  O O   . PRO A 1 688  ? 209.265 180.372 158.786 1.00 76.46  ? 699  PRO A O   1 
ATOM 715  C CB  . PRO A 1 688  ? 208.237 177.265 159.395 1.00 76.20  ? 699  PRO A CB  1 
ATOM 716  C CG  . PRO A 1 688  ? 207.437 176.401 160.296 1.00 77.00  ? 699  PRO A CG  1 
ATOM 717  C CD  . PRO A 1 688  ? 206.302 177.267 160.748 1.00 79.57  ? 699  PRO A CD  1 
ATOM 718  N N   . GLN A 1 689  ? 207.075 180.045 158.358 1.00 73.79  ? 700  GLN A N   1 
ATOM 719  C CA  . GLN A 1 689  ? 207.021 181.142 157.397 1.00 77.18  ? 700  GLN A CA  1 
ATOM 720  C C   . GLN A 1 689  ? 207.271 182.479 158.083 1.00 80.44  ? 700  GLN A C   1 
ATOM 721  O O   . GLN A 1 689  ? 207.967 183.347 157.545 1.00 84.09  ? 700  GLN A O   1 
ATOM 722  C CB  . GLN A 1 689  ? 205.670 181.142 156.680 1.00 81.29  ? 700  GLN A CB  1 
ATOM 723  C CG  . GLN A 1 689  ? 205.450 179.937 155.779 1.00 87.97  ? 700  GLN A CG  1 
ATOM 724  C CD  . GLN A 1 689  ? 204.148 180.013 155.005 1.00 89.46  ? 700  GLN A CD  1 
ATOM 725  O OE1 . GLN A 1 689  ? 203.272 180.818 155.320 1.00 86.22  ? 700  GLN A OE1 1 
ATOM 726  N NE2 . GLN A 1 689  ? 204.015 179.171 153.987 1.00 87.00  ? 700  GLN A NE2 1 
ATOM 727  N N   . ALA A 1 690  ? 206.701 182.663 159.277 1.00 78.15  ? 701  ALA A N   1 
ATOM 728  C CA  . ALA A 1 690  ? 206.957 183.880 160.040 1.00 75.94  ? 701  ALA A CA  1 
ATOM 729  C C   . ALA A 1 690  ? 208.425 183.983 160.437 1.00 76.31  ? 701  ALA A C   1 
ATOM 730  O O   . ALA A 1 690  ? 209.009 185.073 160.404 1.00 71.66  ? 701  ALA A O   1 
ATOM 731  C CB  . ALA A 1 690  ? 206.060 183.922 161.276 1.00 67.85  ? 701  ALA A CB  1 
ATOM 732  N N   . LYS A 1 691  ? 209.035 182.859 160.824 1.00 80.00  ? 702  LYS A N   1 
ATOM 733  C CA  . LYS A 1 691  ? 210.452 182.866 161.173 1.00 75.73  ? 702  LYS A CA  1 
ATOM 734  C C   . LYS A 1 691  ? 211.325 183.235 159.981 1.00 78.70  ? 702  LYS A C   1 
ATOM 735  O O   . LYS A 1 691  ? 212.302 183.978 160.134 1.00 83.32  ? 702  LYS A O   1 
ATOM 736  C CB  . LYS A 1 691  ? 210.877 181.503 161.718 1.00 73.68  ? 702  LYS A CB  1 
ATOM 737  C CG  . LYS A 1 691  ? 210.246 181.112 163.040 1.00 72.94  ? 702  LYS A CG  1 
ATOM 738  C CD  . LYS A 1 691  ? 210.929 179.875 163.602 1.00 74.63  ? 702  LYS A CD  1 
ATOM 739  C CE  . LYS A 1 691  ? 210.041 179.142 164.589 1.00 72.01  ? 702  LYS A CE  1 
ATOM 740  N NZ  . LYS A 1 691  ? 210.835 178.317 165.541 1.00 74.25  ? 702  LYS A NZ  1 
ATOM 741  N N   . SER A 1 692  ? 210.998 182.720 158.793 1.00 74.43  ? 703  SER A N   1 
ATOM 742  C CA  . SER A 1 692  ? 211.843 182.957 157.626 1.00 73.04  ? 703  SER A CA  1 
ATOM 743  C C   . SER A 1 692  ? 211.857 184.425 157.218 1.00 76.68  ? 703  SER A C   1 
ATOM 744  O O   . SER A 1 692  ? 212.869 184.911 156.698 1.00 80.14  ? 703  SER A O   1 
ATOM 745  C CB  . SER A 1 692  ? 211.376 182.090 156.457 1.00 72.57  ? 703  SER A CB  1 
ATOM 746  O OG  . SER A 1 692  ? 210.255 182.667 155.812 1.00 72.29  ? 703  SER A OG  1 
ATOM 747  N N   . GLN A 1 693  ? 210.763 185.143 157.442 1.00 75.72  ? 704  GLN A N   1 
ATOM 748  C CA  . GLN A 1 693  ? 210.673 186.531 157.021 1.00 75.99  ? 704  GLN A CA  1 
ATOM 749  C C   . GLN A 1 693  ? 211.445 187.445 157.969 1.00 76.39  ? 704  GLN A C   1 
ATOM 750  O O   . GLN A 1 693  ? 211.646 187.117 159.141 1.00 78.93  ? 704  GLN A O   1 
ATOM 751  C CB  . GLN A 1 693  ? 209.212 186.962 156.949 1.00 73.14  ? 704  GLN A CB  1 
ATOM 752  C CG  . GLN A 1 693  ? 208.404 186.216 155.904 1.00 79.85  ? 704  GLN A CG  1 
ATOM 753  C CD  . GLN A 1 693  ? 207.042 186.833 155.672 1.00 84.90  ? 704  GLN A CD  1 
ATOM 754  O OE1 . GLN A 1 693  ? 206.685 187.831 156.299 1.00 85.44  ? 704  GLN A OE1 1 
ATOM 755  N NE2 . GLN A 1 693  ? 206.274 186.246 154.762 1.00 86.79  ? 704  GLN A NE2 1 
ATOM 756  N N   . PRO A 1 694  ? 211.895 188.597 157.479 1.00 71.82  ? 705  PRO A N   1 
ATOM 757  C CA  . PRO A 1 694  ? 212.580 189.563 158.344 1.00 69.54  ? 705  PRO A CA  1 
ATOM 758  C C   . PRO A 1 694  ? 211.636 190.116 159.396 1.00 66.20  ? 705  PRO A C   1 
ATOM 759  O O   . PRO A 1 694  ? 210.410 189.980 159.269 1.00 65.91  ? 705  PRO A O   1 
ATOM 760  C CB  . PRO A 1 694  ? 213.026 190.659 157.362 1.00 67.63  ? 705  PRO A CB  1 
ATOM 761  C CG  . PRO A 1 694  ? 213.088 189.975 156.040 1.00 68.15  ? 705  PRO A CG  1 
ATOM 762  C CD  . PRO A 1 694  ? 211.958 188.991 156.061 1.00 66.01  ? 705  PRO A CD  1 
ATOM 763  N N   . PRO A 1 695  ? 212.171 190.730 160.464 1.00 65.05  ? 706  PRO A N   1 
ATOM 764  C CA  . PRO A 1 695  ? 211.305 191.301 161.506 1.00 64.99  ? 706  PRO A CA  1 
ATOM 765  C C   . PRO A 1 695  ? 210.258 192.260 160.960 1.00 67.70  ? 706  PRO A C   1 
ATOM 766  O O   . PRO A 1 695  ? 210.591 193.301 160.385 1.00 73.94  ? 706  PRO A O   1 
ATOM 767  C CB  . PRO A 1 695  ? 212.300 192.024 162.421 1.00 61.93  ? 706  PRO A CB  1 
ATOM 768  C CG  . PRO A 1 695  ? 213.557 191.243 162.270 1.00 62.99  ? 706  PRO A CG  1 
ATOM 769  C CD  . PRO A 1 695  ? 213.597 190.834 160.822 1.00 65.07  ? 706  PRO A CD  1 
ATOM 770  N N   . SER A 1 696  ? 208.987 191.910 161.139 1.00 63.77  ? 707  SER A N   1 
ATOM 771  C CA  . SER A 1 696  ? 207.881 192.728 160.666 1.00 63.25  ? 707  SER A CA  1 
ATOM 772  C C   . SER A 1 696  ? 206.719 192.594 161.637 1.00 59.03  ? 707  SER A C   1 
ATOM 773  O O   . SER A 1 696  ? 206.646 191.634 162.410 1.00 59.92  ? 707  SER A O   1 
ATOM 774  C CB  . SER A 1 696  ? 207.444 192.327 159.252 1.00 67.20  ? 707  SER A CB  1 
ATOM 775  O OG  . SER A 1 696  ? 208.550 192.289 158.367 1.00 69.66  ? 707  SER A OG  1 
ATOM 776  N N   . MET A 1 697  ? 205.813 193.573 161.592 1.00 59.25  ? 708  MET A N   1 
ATOM 777  C CA  . MET A 1 697  ? 204.673 193.573 162.503 1.00 62.59  ? 708  MET A CA  1 
ATOM 778  C C   . MET A 1 697  ? 203.771 192.366 162.268 1.00 61.42  ? 708  MET A C   1 
ATOM 779  O O   . MET A 1 697  ? 203.293 191.742 163.225 1.00 59.71  ? 708  MET A O   1 
ATOM 780  C CB  . MET A 1 697  ? 203.885 194.874 162.345 1.00 68.83  ? 708  MET A CB  1 
ATOM 781  C CG  . MET A 1 697  ? 202.567 194.898 163.093 1.00 70.45  ? 708  MET A CG  1 
ATOM 782  S SD  . MET A 1 697  ? 201.792 196.525 163.086 1.00 90.90  ? 708  MET A SD  1 
ATOM 783  C CE  . MET A 1 697  ? 203.072 197.512 163.856 1.00 79.28  ? 708  MET A CE  1 
ATOM 784  N N   . GLU A 1 698  ? 203.512 192.056 160.997 1.00 62.20  ? 709  GLU A N   1 
ATOM 785  C CA  . GLU A 1 698  ? 202.670 190.880 160.671 1.00 61.37  ? 709  GLU A CA  1 
ATOM 786  C C   . GLU A 1 698  ? 203.293 189.644 161.319 1.00 65.16  ? 709  GLU A C   1 
ATOM 787  O O   . GLU A 1 698  ? 202.606 188.996 162.135 1.00 67.48  ? 709  GLU A O   1 
ATOM 788  C CB  . GLU A 1 698  ? 202.590 190.641 159.167 1.00 62.14  ? 709  GLU A CB  1 
ATOM 789  C CG  . GLU A 1 698  ? 201.893 191.765 158.408 1.00 80.08  ? 709  GLU A CG  1 
ATOM 790  C CD  . GLU A 1 698  ? 201.783 191.502 156.918 1.00 99.66  ? 709  GLU A CD  1 
ATOM 791  O OE1 . GLU A 1 698  ? 202.254 190.435 156.471 1.00 99.64  ? 709  GLU A OE1 1 
ATOM 792  O OE2 . GLU A 1 698  ? 201.227 192.362 156.204 1.00 105.65 ? 709  GLU A OE2 1 
ATOM 793  N N   . SER A 1 699  ? 204.549 189.340 160.978 1.00 66.01  ? 710  SER A N   1 
ATOM 794  C CA  . SER A 1 699  ? 205.198 188.144 161.501 1.00 56.76  ? 710  SER A CA  1 
ATOM 795  C C   . SER A 1 699  ? 205.274 188.169 163.021 1.00 54.91  ? 710  SER A C   1 
ATOM 796  O O   . SER A 1 699  ? 205.169 187.118 163.662 1.00 57.78  ? 710  SER A O   1 
ATOM 797  C CB  . SER A 1 699  ? 206.595 187.998 160.898 1.00 54.68  ? 710  SER A CB  1 
ATOM 798  O OG  . SER A 1 699  ? 207.383 189.147 161.154 1.00 60.39  ? 710  SER A OG  1 
ATOM 799  N N   . ALA A 1 700  ? 205.449 189.353 163.613 1.00 52.61  ? 711  ALA A N   1 
ATOM 800  C CA  . ALA A 1 700  ? 205.488 189.455 165.068 1.00 48.85  ? 711  ALA A CA  1 
ATOM 801  C C   . ALA A 1 700  ? 204.158 189.037 165.683 1.00 47.50  ? 711  ALA A C   1 
ATOM 802  O O   . ALA A 1 700  ? 204.123 188.254 166.639 1.00 50.25  ? 711  ALA A O   1 
ATOM 803  C CB  . ALA A 1 700  ? 205.854 190.879 165.486 1.00 54.07  ? 711  ALA A CB  1 
ATOM 804  N N   . MET A 1 701  ? 203.047 189.546 165.141 1.00 48.88  ? 712  MET A N   1 
ATOM 805  C CA  . MET A 1 701  ? 201.739 189.130 165.639 1.00 51.16  ? 712  MET A CA  1 
ATOM 806  C C   . MET A 1 701  ? 201.489 187.648 165.392 1.00 50.08  ? 712  MET A C   1 
ATOM 807  O O   . MET A 1 701  ? 200.917 186.966 166.253 1.00 52.16  ? 712  MET A O   1 
ATOM 808  C CB  . MET A 1 701  ? 200.626 189.960 165.001 1.00 52.69  ? 712  MET A CB  1 
ATOM 809  C CG  . MET A 1 701  ? 200.726 191.455 165.243 1.00 61.54  ? 712  MET A CG  1 
ATOM 810  S SD  . MET A 1 701  ? 199.100 192.238 165.210 1.00 89.64  ? 712  MET A SD  1 
ATOM 811  C CE  . MET A 1 701  ? 199.402 193.642 164.141 1.00 72.94  ? 712  MET A CE  1 
ATOM 812  N N   . VAL A 1 702  ? 201.900 187.135 164.229 1.00 50.34  ? 713  VAL A N   1 
ATOM 813  C CA  . VAL A 1 702  ? 201.708 185.717 163.941 1.00 48.13  ? 713  VAL A CA  1 
ATOM 814  C C   . VAL A 1 702  ? 202.434 184.864 164.972 1.00 52.14  ? 713  VAL A C   1 
ATOM 815  O O   . VAL A 1 702  ? 201.859 183.927 165.537 1.00 53.96  ? 713  VAL A O   1 
ATOM 816  C CB  . VAL A 1 702  ? 202.169 185.389 162.509 1.00 46.19  ? 713  VAL A CB  1 
ATOM 817  C CG1 . VAL A 1 702  ? 202.252 183.886 162.312 1.00 52.34  ? 713  VAL A CG1 1 
ATOM 818  C CG2 . VAL A 1 702  ? 201.214 185.997 161.496 1.00 53.49  ? 713  VAL A CG2 1 
ATOM 819  N N   . LEU A 1 703  ? 203.696 185.194 165.259 1.00 51.43  ? 714  LEU A N   1 
ATOM 820  C CA  . LEU A 1 703  ? 204.453 184.436 166.250 1.00 40.37  ? 714  LEU A CA  1 
ATOM 821  C C   . LEU A 1 703  ? 203.865 184.596 167.647 1.00 47.61  ? 714  LEU A C   1 
ATOM 822  O O   . LEU A 1 703  ? 203.828 183.634 168.419 1.00 58.37  ? 714  LEU A O   1 
ATOM 823  C CB  . LEU A 1 703  ? 205.921 184.858 166.231 1.00 35.02  ? 714  LEU A CB  1 
ATOM 824  C CG  . LEU A 1 703  ? 206.705 184.475 164.975 1.00 43.76  ? 714  LEU A CG  1 
ATOM 825  C CD1 . LEU A 1 703  ? 207.988 185.278 164.877 1.00 51.54  ? 714  LEU A CD1 1 
ATOM 826  C CD2 . LEU A 1 703  ? 207.004 182.986 164.968 1.00 54.30  ? 714  LEU A CD2 1 
ATOM 827  N N   . ARG A 1 704  ? 203.397 185.799 167.991 1.00 46.30  ? 715  ARG A N   1 
ATOM 828  C CA  . ARG A 1 704  ? 202.831 186.022 169.319 1.00 47.08  ? 715  ARG A CA  1 
ATOM 829  C C   . ARG A 1 704  ? 201.588 185.168 169.541 1.00 52.82  ? 715  ARG A C   1 
ATOM 830  O O   . ARG A 1 704  ? 201.486 184.443 170.541 1.00 58.58  ? 715  ARG A O   1 
ATOM 831  C CB  . ARG A 1 704  ? 202.507 187.506 169.502 1.00 49.19  ? 715  ARG A CB  1 
ATOM 832  C CG  . ARG A 1 704  ? 202.131 187.894 170.921 1.00 59.53  ? 715  ARG A CG  1 
ATOM 833  C CD  . ARG A 1 704  ? 202.093 189.406 171.088 1.00 65.46  ? 715  ARG A CD  1 
ATOM 834  N NE  . ARG A 1 704  ? 200.868 189.992 170.557 1.00 66.54  ? 715  ARG A NE  1 
ATOM 835  C CZ  . ARG A 1 704  ? 199.867 190.434 171.306 1.00 76.50  ? 715  ARG A CZ  1 
ATOM 836  N NH1 . ARG A 1 704  ? 199.913 190.373 172.627 1.00 65.93  ? 715  ARG A NH1 1 
ATOM 837  N NH2 . ARG A 1 704  ? 198.793 190.949 170.715 1.00 89.17  ? 715  ARG A NH2 1 
ATOM 838  N N   . ASP A 1 705  ? 200.629 185.233 168.614 1.00 51.93  ? 716  ASP A N   1 
ATOM 839  C CA  . ASP A 1 705  ? 199.423 184.427 168.773 1.00 55.17  ? 716  ASP A CA  1 
ATOM 840  C C   . ASP A 1 705  ? 199.702 182.938 168.597 1.00 58.17  ? 716  ASP A C   1 
ATOM 841  O O   . ASP A 1 705  ? 199.013 182.114 169.205 1.00 67.83  ? 716  ASP A O   1 
ATOM 842  C CB  . ASP A 1 705  ? 198.325 184.896 167.820 1.00 62.75  ? 716  ASP A CB  1 
ATOM 843  C CG  . ASP A 1 705  ? 198.139 186.401 167.842 1.00 74.54  ? 716  ASP A CG  1 
ATOM 844  O OD1 . ASP A 1 705  ? 197.787 186.933 168.916 1.00 78.03  ? 716  ASP A OD1 1 
ATOM 845  O OD2 . ASP A 1 705  ? 198.320 187.048 166.792 1.00 75.84  ? 716  ASP A OD2 1 
ATOM 846  N N   . GLY A 1 706  ? 200.707 182.566 167.800 1.00 53.57  ? 717  GLY A N   1 
ATOM 847  C CA  . GLY A 1 706  ? 201.089 181.166 167.732 1.00 56.31  ? 717  GLY A CA  1 
ATOM 848  C C   . GLY A 1 706  ? 201.637 180.654 169.049 1.00 57.16  ? 717  GLY A C   1 
ATOM 849  O O   . GLY A 1 706  ? 201.313 179.544 169.478 1.00 60.86  ? 717  GLY A O   1 
ATOM 850  N N   . ALA A 1 707  ? 202.467 181.462 169.714 1.00 55.31  ? 718  ALA A N   1 
ATOM 851  C CA  . ALA A 1 707  ? 202.968 181.099 171.034 1.00 55.10  ? 718  ALA A CA  1 
ATOM 852  C C   . ALA A 1 707  ? 201.829 180.990 172.036 1.00 61.65  ? 718  ALA A C   1 
ATOM 853  O O   . ALA A 1 707  ? 201.792 180.065 172.855 1.00 66.83  ? 718  ALA A O   1 
ATOM 854  C CB  . ALA A 1 707  ? 204.000 182.125 171.503 1.00 53.85  ? 718  ALA A CB  1 
ATOM 855  N N   . LYS A 1 708  ? 200.884 181.932 171.985 1.00 61.87  ? 719  LYS A N   1 
ATOM 856  C CA  . LYS A 1 708  ? 199.738 181.867 172.887 1.00 62.07  ? 719  LYS A CA  1 
ATOM 857  C C   . LYS A 1 708  ? 198.919 180.601 172.653 1.00 65.67  ? 719  LYS A C   1 
ATOM 858  O O   . LYS A 1 708  ? 198.537 179.912 173.608 1.00 68.48  ? 719  LYS A O   1 
ATOM 859  C CB  . LYS A 1 708  ? 198.866 183.111 172.722 1.00 65.69  ? 719  LYS A CB  1 
ATOM 860  C CG  . LYS A 1 708  ? 197.754 183.223 173.751 1.00 72.54  ? 719  LYS A CG  1 
ATOM 861  C CD  . LYS A 1 708  ? 197.120 184.603 173.738 1.00 80.79  ? 719  LYS A CD  1 
ATOM 862  C CE  . LYS A 1 708  ? 198.115 185.667 174.167 1.00 85.20  ? 719  LYS A CE  1 
ATOM 863  N NZ  . LYS A 1 708  ? 197.472 187.001 174.324 1.00 86.46  ? 719  LYS A NZ  1 
ATOM 864  N N   . PHE A 1 709  ? 198.650 180.273 171.387 1.00 64.80  ? 720  PHE A N   1 
ATOM 865  C CA  . PHE A 1 709  ? 197.879 179.075 171.072 1.00 66.53  ? 720  PHE A CA  1 
ATOM 866  C C   . PHE A 1 709  ? 198.612 177.817 171.521 1.00 71.77  ? 720  PHE A C   1 
ATOM 867  O O   . PHE A 1 709  ? 198.004 176.898 172.083 1.00 76.06  ? 720  PHE A O   1 
ATOM 868  C CB  . PHE A 1 709  ? 197.582 179.026 169.573 1.00 66.85  ? 720  PHE A CB  1 
ATOM 869  C CG  . PHE A 1 709  ? 196.874 177.775 169.135 1.00 74.37  ? 720  PHE A CG  1 
ATOM 870  C CD1 . PHE A 1 709  ? 195.499 177.665 169.250 1.00 79.82  ? 720  PHE A CD1 1 
ATOM 871  C CD2 . PHE A 1 709  ? 197.584 176.712 168.602 1.00 79.05  ? 720  PHE A CD2 1 
ATOM 872  C CE1 . PHE A 1 709  ? 194.845 176.517 168.846 1.00 87.24  ? 720  PHE A CE1 1 
ATOM 873  C CE2 . PHE A 1 709  ? 196.937 175.562 168.200 1.00 84.02  ? 720  PHE A CE2 1 
ATOM 874  C CZ  . PHE A 1 709  ? 195.566 175.464 168.320 1.00 87.96  ? 720  PHE A CZ  1 
ATOM 875  N N   . GLU A 1 710  ? 199.925 177.757 171.281 1.00 71.63  ? 721  GLU A N   1 
ATOM 876  C CA  . GLU A 1 710  ? 200.706 176.601 171.707 1.00 73.13  ? 721  GLU A CA  1 
ATOM 877  C C   . GLU A 1 710  ? 200.717 176.465 173.223 1.00 74.55  ? 721  GLU A C   1 
ATOM 878  O O   . GLU A 1 710  ? 200.696 175.344 173.745 1.00 75.82  ? 721  GLU A O   1 
ATOM 879  C CB  . GLU A 1 710  ? 202.131 176.703 171.163 1.00 71.62  ? 721  GLU A CB  1 
ATOM 880  C CG  . GLU A 1 710  ? 202.237 176.435 169.669 1.00 75.54  ? 721  GLU A CG  1 
ATOM 881  C CD  . GLU A 1 710  ? 203.576 176.851 169.092 1.00 75.60  ? 721  GLU A CD  1 
ATOM 882  O OE1 . GLU A 1 710  ? 204.105 177.902 169.511 1.00 76.22  ? 721  GLU A OE1 1 
ATOM 883  O OE2 . GLU A 1 710  ? 204.095 176.131 168.213 1.00 75.91  ? 721  GLU A OE2 1 
ATOM 884  N N   . ALA A 1 711  ? 200.758 177.587 173.944 1.00 73.28  ? 722  ALA A N   1 
ATOM 885  C CA  . ALA A 1 711  ? 200.632 177.539 175.397 1.00 71.11  ? 722  ALA A CA  1 
ATOM 886  C C   . ALA A 1 711  ? 199.270 176.990 175.803 1.00 73.27  ? 722  ALA A C   1 
ATOM 887  O O   . ALA A 1 711  ? 199.163 176.193 176.742 1.00 72.38  ? 722  ALA A O   1 
ATOM 888  C CB  . ALA A 1 711  ? 200.856 178.930 175.990 1.00 66.90  ? 722  ALA A CB  1 
ATOM 889  N N   . GLN A 1 712  ? 198.212 177.410 175.104 1.00 76.99  ? 723  GLN A N   1 
ATOM 890  C CA  . GLN A 1 712  ? 196.892 176.852 175.377 1.00 76.18  ? 723  GLN A CA  1 
ATOM 891  C C   . GLN A 1 712  ? 196.755 175.433 174.836 1.00 75.49  ? 723  GLN A C   1 
ATOM 892  O O   . GLN A 1 712  ? 195.978 174.639 175.378 1.00 77.15  ? 723  GLN A O   1 
ATOM 893  C CB  . GLN A 1 712  ? 195.802 177.751 174.792 1.00 74.42  ? 723  GLN A CB  1 
ATOM 894  C CG  . GLN A 1 712  ? 195.895 179.210 175.215 1.00 76.33  ? 723  GLN A CG  1 
ATOM 895  C CD  . GLN A 1 712  ? 196.124 179.377 176.705 1.00 81.66  ? 723  GLN A CD  1 
ATOM 896  O OE1 . GLN A 1 712  ? 197.262 179.482 177.164 1.00 79.94  ? 723  GLN A OE1 1 
ATOM 897  N NE2 . GLN A 1 712  ? 195.039 179.402 177.471 1.00 86.63  ? 723  GLN A NE2 1 
ATOM 898  N N   . ALA A 1 713  ? 197.494 175.095 173.777 1.00 74.98  ? 724  ALA A N   1 
ATOM 899  C CA  . ALA A 1 713  ? 197.416 173.760 173.195 1.00 75.06  ? 724  ALA A CA  1 
ATOM 900  C C   . ALA A 1 713  ? 198.017 172.684 174.089 1.00 76.34  ? 724  ALA A C   1 
ATOM 901  O O   . ALA A 1 713  ? 197.761 171.498 173.854 1.00 78.08  ? 724  ALA A O   1 
ATOM 902  C CB  . ALA A 1 713  ? 198.108 173.735 171.831 1.00 76.59  ? 724  ALA A CB  1 
ATOM 903  N N   . GLY A 1 714  ? 198.800 173.058 175.093 1.00 79.17  ? 725  GLY A N   1 
ATOM 904  C CA  . GLY A 1 714  ? 199.414 172.097 175.982 1.00 78.77  ? 725  GLY A CA  1 
ATOM 905  C C   . GLY A 1 714  ? 200.893 171.856 175.776 1.00 79.56  ? 725  GLY A C   1 
ATOM 906  O O   . GLY A 1 714  ? 201.397 170.820 176.225 1.00 82.77  ? 725  GLY A O   1 
ATOM 907  N N   . ASP A 1 715  ? 201.603 172.769 175.115 1.00 76.61  ? 726  ASP A N   1 
ATOM 908  C CA  . ASP A 1 715  ? 203.046 172.658 174.900 1.00 70.44  ? 726  ASP A CA  1 
ATOM 909  C C   . ASP A 1 715  ? 203.692 173.970 175.325 1.00 69.95  ? 726  ASP A C   1 
ATOM 910  O O   . ASP A 1 715  ? 204.081 174.788 174.479 1.00 72.61  ? 726  ASP A O   1 
ATOM 911  C CB  . ASP A 1 715  ? 203.367 172.322 173.443 1.00 73.48  ? 726  ASP A CB  1 
ATOM 912  C CG  . ASP A 1 715  ? 204.792 171.837 173.254 1.00 82.00  ? 726  ASP A CG  1 
ATOM 913  O OD1 . ASP A 1 715  ? 205.587 171.920 174.214 1.00 83.10  ? 726  ASP A OD1 1 
ATOM 914  O OD2 . ASP A 1 715  ? 205.119 171.370 172.143 1.00 86.33  ? 726  ASP A OD2 1 
ATOM 915  N N   . PRO A 1 716  ? 203.810 174.210 176.634 1.00 62.43  ? 727  PRO A N   1 
ATOM 916  C CA  . PRO A 1 716  ? 204.381 175.487 177.097 1.00 60.10  ? 727  PRO A CA  1 
ATOM 917  C C   . PRO A 1 716  ? 205.816 175.724 176.657 1.00 60.50  ? 727  PRO A C   1 
ATOM 918  O O   . PRO A 1 716  ? 206.203 176.882 176.455 1.00 63.44  ? 727  PRO A O   1 
ATOM 919  C CB  . PRO A 1 716  ? 204.272 175.378 178.624 1.00 58.40  ? 727  PRO A CB  1 
ATOM 920  C CG  . PRO A 1 716  ? 203.184 174.375 178.855 1.00 57.00  ? 727  PRO A CG  1 
ATOM 921  C CD  . PRO A 1 716  ? 203.360 173.374 177.758 1.00 60.06  ? 727  PRO A CD  1 
ATOM 922  N N   . THR A 1 717  ? 206.625 174.672 176.517 1.00 59.68  ? 728  THR A N   1 
ATOM 923  C CA  . THR A 1 717  ? 208.020 174.858 176.124 1.00 60.08  ? 728  THR A CA  1 
ATOM 924  C C   . THR A 1 717  ? 208.124 175.394 174.700 1.00 63.68  ? 728  THR A C   1 
ATOM 925  O O   . THR A 1 717  ? 208.895 176.324 174.424 1.00 63.64  ? 728  THR A O   1 
ATOM 926  C CB  . THR A 1 717  ? 208.784 173.540 176.261 1.00 62.69  ? 728  THR A CB  1 
ATOM 927  O OG1 . THR A 1 717  ? 208.528 172.969 177.550 1.00 64.28  ? 728  THR A OG1 1 
ATOM 928  C CG2 . THR A 1 717  ? 210.279 173.774 176.104 1.00 63.71  ? 728  THR A CG2 1 
ATOM 929  N N   . GLN A 1 718  ? 207.356 174.810 173.778 1.00 66.23  ? 729  GLN A N   1 
ATOM 930  C CA  . GLN A 1 718  ? 207.333 175.319 172.412 1.00 66.66  ? 729  GLN A CA  1 
ATOM 931  C C   . GLN A 1 718  ? 206.791 176.741 172.376 1.00 65.20  ? 729  GLN A C   1 
ATOM 932  O O   . GLN A 1 718  ? 207.229 177.563 171.563 1.00 66.75  ? 729  GLN A O   1 
ATOM 933  C CB  . GLN A 1 718  ? 206.502 174.396 171.522 1.00 71.37  ? 729  GLN A CB  1 
ATOM 934  C CG  . GLN A 1 718  ? 206.402 174.848 170.077 1.00 77.20  ? 729  GLN A CG  1 
ATOM 935  C CD  . GLN A 1 718  ? 207.760 175.005 169.423 1.00 84.26  ? 729  GLN A CD  1 
ATOM 936  O OE1 . GLN A 1 718  ? 208.576 174.084 169.432 1.00 84.68  ? 729  GLN A OE1 1 
ATOM 937  N NE2 . GLN A 1 718  ? 208.010 176.178 168.852 1.00 82.32  ? 729  GLN A NE2 1 
ATOM 938  N N   . ALA A 1 719  ? 205.845 177.054 173.265 1.00 61.80  ? 730  ALA A N   1 
ATOM 939  C CA  . ALA A 1 719  ? 205.351 178.422 173.372 1.00 59.30  ? 730  ALA A CA  1 
ATOM 940  C C   . ALA A 1 719  ? 206.454 179.376 173.814 1.00 59.34  ? 730  ALA A C   1 
ATOM 941  O O   . ALA A 1 719  ? 206.550 180.500 173.311 1.00 62.40  ? 730  ALA A O   1 
ATOM 942  C CB  . ALA A 1 719  ? 204.170 178.478 174.339 1.00 60.70  ? 730  ALA A CB  1 
ATOM 943  N N   . LEU A 1 720  ? 207.291 178.950 174.762 1.00 61.48  ? 731  LEU A N   1 
ATOM 944  C CA  . LEU A 1 720  ? 208.406 179.787 175.195 1.00 55.09  ? 731  LEU A CA  1 
ATOM 945  C C   . LEU A 1 720  ? 209.412 179.994 174.070 1.00 55.61  ? 731  LEU A C   1 
ATOM 946  O O   . LEU A 1 720  ? 209.943 181.098 173.898 1.00 58.10  ? 731  LEU A O   1 
ATOM 947  C CB  . LEU A 1 720  ? 209.085 179.172 176.419 1.00 55.93  ? 731  LEU A CB  1 
ATOM 948  C CG  . LEU A 1 720  ? 208.363 179.358 177.754 1.00 55.58  ? 731  LEU A CG  1 
ATOM 949  C CD1 . LEU A 1 720  ? 208.993 178.491 178.834 1.00 49.96  ? 731  LEU A CD1 1 
ATOM 950  C CD2 . LEU A 1 720  ? 208.368 180.821 178.166 1.00 53.88  ? 731  LEU A CD2 1 
ATOM 951  N N   . GLU A 1 721  ? 209.691 178.943 173.294 1.00 58.25  ? 732  GLU A N   1 
ATOM 952  C CA  . GLU A 1 721  ? 210.577 179.102 172.142 1.00 59.45  ? 732  GLU A CA  1 
ATOM 953  C C   . GLU A 1 721  ? 209.982 180.064 171.117 1.00 60.77  ? 732  GLU A C   1 
ATOM 954  O O   . GLU A 1 721  ? 210.695 180.895 170.535 1.00 60.87  ? 732  GLU A O   1 
ATOM 955  C CB  . GLU A 1 721  ? 210.865 177.745 171.500 1.00 60.04  ? 732  GLU A CB  1 
ATOM 956  C CG  . GLU A 1 721  ? 211.301 176.668 172.478 1.00 64.73  ? 732  GLU A CG  1 
ATOM 957  C CD  . GLU A 1 721  ? 212.785 176.717 172.777 1.00 70.56  ? 732  GLU A CD  1 
ATOM 958  O OE1 . GLU A 1 721  ? 213.505 177.478 172.097 1.00 71.64  ? 732  GLU A OE1 1 
ATOM 959  O OE2 . GLU A 1 721  ? 213.232 175.995 173.693 1.00 71.81  ? 732  GLU A OE2 1 
ATOM 960  N N   . THR A 1 722  ? 208.672 179.967 170.885 1.00 58.65  ? 733  THR A N   1 
ATOM 961  C CA  . THR A 1 722  ? 208.019 180.866 169.940 1.00 52.75  ? 733  THR A CA  1 
ATOM 962  C C   . THR A 1 722  ? 208.039 182.304 170.444 1.00 53.47  ? 733  THR A C   1 
ATOM 963  O O   . THR A 1 722  ? 208.173 183.240 169.652 1.00 59.85  ? 733  THR A O   1 
ATOM 964  C CB  . THR A 1 722  ? 206.588 180.400 169.677 1.00 56.22  ? 733  THR A CB  1 
ATOM 965  O OG1 . THR A 1 722  ? 206.596 179.012 169.324 1.00 66.41  ? 733  THR A OG1 1 
ATOM 966  C CG2 . THR A 1 722  ? 205.975 181.192 168.535 1.00 60.41  ? 733  THR A CG2 1 
ATOM 967  N N   . TYR A 1 723  ? 207.911 182.504 171.759 1.00 51.92  ? 734  TYR A N   1 
ATOM 968  C CA  . TYR A 1 723  ? 208.064 183.844 172.323 1.00 48.80  ? 734  TYR A CA  1 
ATOM 969  C C   . TYR A 1 723  ? 209.490 184.360 172.166 1.00 52.37  ? 734  TYR A C   1 
ATOM 970  O O   . TYR A 1 723  ? 209.694 185.555 171.909 1.00 57.96  ? 734  TYR A O   1 
ATOM 971  C CB  . TYR A 1 723  ? 207.663 183.852 173.798 1.00 51.06  ? 734  TYR A CB  1 
ATOM 972  C CG  . TYR A 1 723  ? 206.180 184.021 174.036 1.00 47.88  ? 734  TYR A CG  1 
ATOM 973  C CD1 . TYR A 1 723  ? 205.513 185.155 173.593 1.00 44.82  ? 734  TYR A CD1 1 
ATOM 974  C CD2 . TYR A 1 723  ? 205.451 183.057 174.717 1.00 52.46  ? 734  TYR A CD2 1 
ATOM 975  C CE1 . TYR A 1 723  ? 204.159 185.318 173.812 1.00 49.41  ? 734  TYR A CE1 1 
ATOM 976  C CE2 . TYR A 1 723  ? 204.097 183.211 174.941 1.00 55.38  ? 734  TYR A CE2 1 
ATOM 977  C CZ  . TYR A 1 723  ? 203.456 184.343 174.487 1.00 57.03  ? 734  TYR A CZ  1 
ATOM 978  O OH  . TYR A 1 723  ? 202.108 184.501 174.708 1.00 67.76  ? 734  TYR A OH  1 
ATOM 979  N N   . LYS A 1 724  ? 210.482 183.481 172.332 1.00 51.62  ? 735  LYS A N   1 
ATOM 980  C CA  . LYS A 1 724  ? 211.867 183.870 172.089 1.00 50.17  ? 735  LYS A CA  1 
ATOM 981  C C   . LYS A 1 724  ? 212.051 184.349 170.656 1.00 54.70  ? 735  LYS A C   1 
ATOM 982  O O   . LYS A 1 724  ? 212.729 185.353 170.408 1.00 55.79  ? 735  LYS A O   1 
ATOM 983  C CB  . LYS A 1 724  ? 212.804 182.697 172.376 1.00 51.46  ? 735  LYS A CB  1 
ATOM 984  C CG  . LYS A 1 724  ? 213.059 182.425 173.847 1.00 56.40  ? 735  LYS A CG  1 
ATOM 985  C CD  . LYS A 1 724  ? 213.930 181.191 174.026 1.00 54.11  ? 735  LYS A CD  1 
ATOM 986  C CE  . LYS A 1 724  ? 214.109 180.841 175.494 1.00 48.54  ? 735  LYS A CE  1 
ATOM 987  N NZ  . LYS A 1 724  ? 214.836 179.553 175.668 1.00 46.73  ? 735  LYS A NZ  1 
ATOM 988  N N   . ASP A 1 725  ? 211.455 183.636 169.699 1.00 57.11  ? 736  ASP A N   1 
ATOM 989  C CA  . ASP A 1 725  ? 211.526 184.068 168.305 1.00 55.77  ? 736  ASP A CA  1 
ATOM 990  C C   . ASP A 1 725  ? 210.737 185.353 168.066 1.00 54.26  ? 736  ASP A C   1 
ATOM 991  O O   . ASP A 1 725  ? 211.156 186.200 167.266 1.00 56.50  ? 736  ASP A O   1 
ATOM 992  C CB  . ASP A 1 725  ? 211.023 182.955 167.388 1.00 55.37  ? 736  ASP A CB  1 
ATOM 993  C CG  . ASP A 1 725  ? 211.790 181.661 167.572 1.00 61.38  ? 736  ASP A CG  1 
ATOM 994  O OD1 . ASP A 1 725  ? 212.865 181.692 168.207 1.00 64.30  ? 736  ASP A OD1 1 
ATOM 995  O OD2 . ASP A 1 725  ? 211.318 180.612 167.088 1.00 66.84  ? 736  ASP A OD2 1 
ATOM 996  N N   . ALA A 1 726  ? 209.600 185.515 168.747 1.00 51.14  ? 737  ALA A N   1 
ATOM 997  C CA  . ALA A 1 726  ? 208.771 186.700 168.559 1.00 48.64  ? 737  ALA A CA  1 
ATOM 998  C C   . ALA A 1 726  ? 209.466 187.958 169.055 1.00 49.48  ? 737  ALA A C   1 
ATOM 999  O O   . ALA A 1 726  ? 209.319 189.025 168.448 1.00 59.65  ? 737  ALA A O   1 
ATOM 1000 C CB  . ALA A 1 726  ? 207.430 186.521 169.270 1.00 48.86  ? 737  ALA A CB  1 
ATOM 1001 N N   . MET A 1 727  ? 210.212 187.862 170.158 1.00 49.61  ? 738  MET A N   1 
ATOM 1002 C CA  . MET A 1 727  ? 210.978 189.019 170.612 1.00 54.91  ? 738  MET A CA  1 
ATOM 1003 C C   . MET A 1 727  ? 212.010 189.444 169.577 1.00 54.64  ? 738  MET A C   1 
ATOM 1004 O O   . MET A 1 727  ? 212.278 190.642 169.427 1.00 59.38  ? 738  MET A O   1 
ATOM 1005 C CB  . MET A 1 727  ? 211.659 188.729 171.948 1.00 59.10  ? 738  MET A CB  1 
ATOM 1006 C CG  . MET A 1 727  ? 210.785 189.010 173.156 1.00 61.14  ? 738  MET A CG  1 
ATOM 1007 S SD  . MET A 1 727  ? 211.719 189.000 174.694 1.00 63.05  ? 738  MET A SD  1 
ATOM 1008 C CE  . MET A 1 727  ? 211.794 187.245 175.012 1.00 47.41  ? 738  MET A CE  1 
ATOM 1009 N N   . VAL A 1 728  ? 212.602 188.486 168.863 1.00 52.36  ? 739  VAL A N   1 
ATOM 1010 C CA  . VAL A 1 728  ? 213.473 188.825 167.743 1.00 55.79  ? 739  VAL A CA  1 
ATOM 1011 C C   . VAL A 1 728  ? 212.671 189.501 166.638 1.00 59.25  ? 739  VAL A C   1 
ATOM 1012 O O   . VAL A 1 728  ? 213.094 190.513 166.068 1.00 60.98  ? 739  VAL A O   1 
ATOM 1013 C CB  . VAL A 1 728  ? 214.192 187.566 167.226 1.00 58.90  ? 739  VAL A CB  1 
ATOM 1014 C CG1 . VAL A 1 728  ? 215.033 187.897 166.002 1.00 55.67  ? 739  VAL A CG1 1 
ATOM 1015 C CG2 . VAL A 1 728  ? 215.043 186.956 168.322 1.00 64.20  ? 739  VAL A CG2 1 
ATOM 1016 N N   . ALA A 1 729  ? 211.496 188.949 166.322 1.00 60.51  ? 740  ALA A N   1 
ATOM 1017 C CA  . ALA A 1 729  ? 210.674 189.506 165.252 1.00 57.45  ? 740  ALA A CA  1 
ATOM 1018 C C   . ALA A 1 729  ? 210.121 190.881 165.608 1.00 56.58  ? 740  ALA A C   1 
ATOM 1019 O O   . ALA A 1 729  ? 210.004 191.744 164.732 1.00 53.99  ? 740  ALA A O   1 
ATOM 1020 C CB  . ALA A 1 729  ? 209.531 188.550 164.915 1.00 50.30  ? 740  ALA A CB  1 
ATOM 1021 N N   . SER A 1 730  ? 209.777 191.105 166.875 1.00 55.60  ? 741  SER A N   1 
ATOM 1022 C CA  . SER A 1 730  ? 209.147 192.352 167.291 1.00 46.95  ? 741  SER A CA  1 
ATOM 1023 C C   . SER A 1 730  ? 210.138 193.495 167.472 1.00 54.42  ? 741  SER A C   1 
ATOM 1024 O O   . SER A 1 730  ? 209.715 194.612 167.787 1.00 55.75  ? 741  SER A O   1 
ATOM 1025 C CB  . SER A 1 730  ? 208.371 192.141 168.594 1.00 45.24  ? 741  SER A CB  1 
ATOM 1026 O OG  . SER A 1 730  ? 207.459 191.064 168.475 1.00 51.69  ? 741  SER A OG  1 
ATOM 1027 N N   . GLY A 1 731  ? 211.432 193.250 167.282 1.00 59.98  ? 742  GLY A N   1 
ATOM 1028 C CA  . GLY A 1 731  ? 212.428 194.286 167.456 1.00 63.27  ? 742  GLY A CA  1 
ATOM 1029 C C   . GLY A 1 731  ? 212.896 194.497 168.876 1.00 63.27  ? 742  GLY A C   1 
ATOM 1030 O O   . GLY A 1 731  ? 213.653 195.442 169.126 1.00 61.67  ? 742  GLY A O   1 
ATOM 1031 N N   . VAL A 1 732  ? 212.465 193.654 169.818 1.00 64.22  ? 743  VAL A N   1 
ATOM 1032 C CA  . VAL A 1 732  ? 212.945 193.763 171.192 1.00 60.79  ? 743  VAL A CA  1 
ATOM 1033 C C   . VAL A 1 732  ? 214.438 193.479 171.262 1.00 62.43  ? 743  VAL A C   1 
ATOM 1034 O O   . VAL A 1 732  ? 215.186 194.196 171.938 1.00 63.52  ? 743  VAL A O   1 
ATOM 1035 C CB  . VAL A 1 732  ? 212.145 192.819 172.111 1.00 56.79  ? 743  VAL A CB  1 
ATOM 1036 C CG1 . VAL A 1 732  ? 212.790 192.735 173.485 1.00 57.52  ? 743  VAL A CG1 1 
ATOM 1037 C CG2 . VAL A 1 732  ? 210.702 193.285 172.221 1.00 55.76  ? 743  VAL A CG2 1 
ATOM 1038 N N   . THR A 1 733  ? 214.900 192.444 170.563 1.00 63.34  ? 744  THR A N   1 
ATOM 1039 C CA  . THR A 1 733  ? 216.310 192.089 170.554 1.00 65.32  ? 744  THR A CA  1 
ATOM 1040 C C   . THR A 1 733  ? 216.739 191.768 169.131 1.00 70.46  ? 744  THR A C   1 
ATOM 1041 O O   . THR A 1 733  ? 215.975 191.192 168.351 1.00 68.31  ? 744  THR A O   1 
ATOM 1042 C CB  . THR A 1 733  ? 216.601 190.894 171.470 1.00 65.77  ? 744  THR A CB  1 
ATOM 1043 O OG1 . THR A 1 733  ? 217.906 190.376 171.183 1.00 73.93  ? 744  THR A OG1 1 
ATOM 1044 C CG2 . THR A 1 733  ? 215.568 189.798 171.261 1.00 60.64  ? 744  THR A CG2 1 
ATOM 1045 N N   . THR A 1 734  ? 217.972 192.152 168.801 1.00 77.44  ? 745  THR A N   1 
ATOM 1046 C CA  . THR A 1 734  ? 218.521 191.845 167.485 1.00 78.62  ? 745  THR A CA  1 
ATOM 1047 C C   . THR A 1 734  ? 218.948 190.386 167.379 1.00 73.60  ? 745  THR A C   1 
ATOM 1048 O O   . THR A 1 734  ? 218.839 189.787 166.303 1.00 74.68  ? 745  THR A O   1 
ATOM 1049 C CB  . THR A 1 734  ? 219.705 192.770 167.185 1.00 80.21  ? 745  THR A CB  1 
ATOM 1050 O OG1 . THR A 1 734  ? 219.278 194.135 167.271 1.00 81.45  ? 745  THR A OG1 1 
ATOM 1051 C CG2 . THR A 1 734  ? 220.252 192.513 165.787 1.00 75.85  ? 745  THR A CG2 1 
ATOM 1052 N N   . THR A 1 735  ? 219.408 189.797 168.480 1.00 67.88  ? 746  THR A N   1 
ATOM 1053 C CA  . THR A 1 735  ? 219.872 188.419 168.509 1.00 67.33  ? 746  THR A CA  1 
ATOM 1054 C C   . THR A 1 735  ? 218.981 187.600 169.432 1.00 63.54  ? 746  THR A C   1 
ATOM 1055 O O   . THR A 1 735  ? 218.459 188.116 170.426 1.00 64.56  ? 746  THR A O   1 
ATOM 1056 C CB  . THR A 1 735  ? 221.327 188.331 168.979 1.00 70.90  ? 746  THR A CB  1 
ATOM 1057 O OG1 . THR A 1 735  ? 221.445 188.910 170.284 1.00 73.96  ? 746  THR A OG1 1 
ATOM 1058 C CG2 . THR A 1 735  ? 222.241 189.075 168.018 1.00 66.92  ? 746  THR A CG2 1 
ATOM 1059 N N   . ARG A 1 736  ? 218.807 186.328 169.093 1.00 63.70  ? 747  ARG A N   1 
ATOM 1060 C CA  . ARG A 1 736  ? 217.930 185.464 169.867 1.00 68.49  ? 747  ARG A CA  1 
ATOM 1061 C C   . ARG A 1 736  ? 218.502 185.245 171.266 1.00 74.09  ? 747  ARG A C   1 
ATOM 1062 O O   . ARG A 1 736  ? 219.706 185.002 171.415 1.00 78.54  ? 747  ARG A O   1 
ATOM 1063 C CB  . ARG A 1 736  ? 217.744 184.122 169.158 1.00 66.50  ? 747  ARG A CB  1 
ATOM 1064 C CG  . ARG A 1 736  ? 216.629 183.264 169.728 1.00 63.42  ? 747  ARG A CG  1 
ATOM 1065 C CD  . ARG A 1 736  ? 216.618 181.885 169.091 1.00 64.86  ? 747  ARG A CD  1 
ATOM 1066 N NE  . ARG A 1 736  ? 215.307 181.255 169.183 1.00 70.27  ? 747  ARG A NE  1 
ATOM 1067 C CZ  . ARG A 1 736  ? 215.038 180.193 169.930 1.00 68.67  ? 747  ARG A CZ  1 
ATOM 1068 N NH1 . ARG A 1 736  ? 215.969 179.613 170.668 1.00 67.79  ? 747  ARG A NH1 1 
ATOM 1069 N NH2 . ARG A 1 736  ? 213.802 179.701 169.936 1.00 65.63  ? 747  ARG A NH2 1 
ATOM 1070 N N   . PRO A 1 737  ? 217.675 185.330 172.314 1.00 70.39  ? 748  PRO A N   1 
ATOM 1071 C CA  . PRO A 1 737  ? 218.162 185.029 173.667 1.00 64.34  ? 748  PRO A CA  1 
ATOM 1072 C C   . PRO A 1 737  ? 218.515 183.559 173.827 1.00 69.07  ? 748  PRO A C   1 
ATOM 1073 O O   . PRO A 1 737  ? 217.649 182.689 173.698 1.00 69.70  ? 748  PRO A O   1 
ATOM 1074 C CB  . PRO A 1 737  ? 216.981 185.426 174.564 1.00 58.46  ? 748  PRO A CB  1 
ATOM 1075 C CG  . PRO A 1 737  ? 216.126 186.319 173.712 1.00 59.80  ? 748  PRO A CG  1 
ATOM 1076 C CD  . PRO A 1 737  ? 216.279 185.791 172.324 1.00 66.64  ? 748  PRO A CD  1 
ATOM 1077 N N   . GLN A 1 738  ? 219.787 183.272 174.109 1.00 70.84  ? 749  GLN A N   1 
ATOM 1078 C CA  . GLN A 1 738  ? 220.254 181.892 174.151 1.00 72.23  ? 749  GLN A CA  1 
ATOM 1079 C C   . GLN A 1 738  ? 220.131 181.255 175.529 1.00 74.44  ? 749  GLN A C   1 
ATOM 1080 O O   . GLN A 1 738  ? 220.227 180.028 175.635 1.00 81.35  ? 749  GLN A O   1 
ATOM 1081 C CB  . GLN A 1 738  ? 221.710 181.818 173.680 1.00 75.52  ? 749  GLN A CB  1 
ATOM 1082 C CG  . GLN A 1 738  ? 222.030 182.585 172.387 1.00 83.17  ? 749  GLN A CG  1 
ATOM 1083 C CD  . GLN A 1 738  ? 221.184 182.185 171.176 1.00 85.35  ? 749  GLN A CD  1 
ATOM 1084 O OE1 . GLN A 1 738  ? 220.322 181.308 171.248 1.00 84.40  ? 749  GLN A OE1 1 
ATOM 1085 N NE2 . GLN A 1 738  ? 221.439 182.841 170.050 1.00 77.61  ? 749  GLN A NE2 1 
ATOM 1086 N N   . ASP A 1 739  ? 219.919 182.044 176.580 1.00 72.28  ? 750  ASP A N   1 
ATOM 1087 C CA  . ASP A 1 739  ? 219.837 181.505 177.929 1.00 73.32  ? 750  ASP A CA  1 
ATOM 1088 C C   . ASP A 1 739  ? 218.716 182.196 178.693 1.00 68.29  ? 750  ASP A C   1 
ATOM 1089 O O   . ASP A 1 739  ? 218.132 183.179 178.230 1.00 64.32  ? 750  ASP A O   1 
ATOM 1090 C CB  . ASP A 1 739  ? 221.176 181.635 178.677 1.00 73.39  ? 750  ASP A CB  1 
ATOM 1091 C CG  . ASP A 1 739  ? 221.697 183.062 178.718 1.00 73.85  ? 750  ASP A CG  1 
ATOM 1092 O OD1 . ASP A 1 739  ? 220.920 184.004 178.464 1.00 74.03  ? 750  ASP A OD1 1 
ATOM 1093 O OD2 . ASP A 1 739  ? 222.898 183.241 179.010 1.00 71.94  ? 750  ASP A OD2 1 
ATOM 1094 N N   . ASN A 1 740  ? 218.420 181.657 179.878 1.00 66.13  ? 751  ASN A N   1 
ATOM 1095 C CA  . ASN A 1 740  ? 217.291 182.148 180.661 1.00 66.40  ? 751  ASN A CA  1 
ATOM 1096 C C   . ASN A 1 740  ? 217.514 183.577 181.139 1.00 66.86  ? 751  ASN A C   1 
ATOM 1097 O O   . ASN A 1 740  ? 216.562 184.357 181.239 1.00 65.78  ? 751  ASN A O   1 
ATOM 1098 C CB  . ASN A 1 740  ? 217.033 181.219 181.847 1.00 68.69  ? 751  ASN A CB  1 
ATOM 1099 C CG  . ASN A 1 740  ? 216.517 179.860 181.421 1.00 67.52  ? 751  ASN A CG  1 
ATOM 1100 O OD1 . ASN A 1 740  ? 215.763 179.745 180.455 1.00 67.86  ? 751  ASN A OD1 1 
ATOM 1101 N ND2 . ASN A 1 740  ? 216.921 178.820 182.141 1.00 65.77  ? 751  ASN A ND2 1 
ATOM 1102 N N   . ASP A 1 741  ? 218.761 183.939 181.452 1.00 67.48  ? 752  ASP A N   1 
ATOM 1103 C CA  . ASP A 1 741  ? 219.029 185.273 181.983 1.00 61.62  ? 752  ASP A CA  1 
ATOM 1104 C C   . ASP A 1 741  ? 218.780 186.357 180.938 1.00 59.52  ? 752  ASP A C   1 
ATOM 1105 O O   . ASP A 1 741  ? 218.098 187.351 181.214 1.00 60.54  ? 752  ASP A O   1 
ATOM 1106 C CB  . ASP A 1 741  ? 220.461 185.349 182.512 1.00 65.94  ? 752  ASP A CB  1 
ATOM 1107 C CG  . ASP A 1 741  ? 220.621 184.665 183.855 1.00 71.93  ? 752  ASP A CG  1 
ATOM 1108 O OD1 . ASP A 1 741  ? 219.768 183.819 184.196 1.00 70.91  ? 752  ASP A OD1 1 
ATOM 1109 O OD2 . ASP A 1 741  ? 221.598 184.974 184.569 1.00 74.85  ? 752  ASP A OD2 1 
ATOM 1110 N N   . THR A 1 742  ? 219.338 186.193 179.736 1.00 55.73  ? 753  THR A N   1 
ATOM 1111 C CA  . THR A 1 742  ? 219.125 187.187 178.688 1.00 54.00  ? 753  THR A CA  1 
ATOM 1112 C C   . THR A 1 742  ? 217.674 187.192 178.221 1.00 55.40  ? 753  THR A C   1 
ATOM 1113 O O   . THR A 1 742  ? 217.138 188.244 177.852 1.00 54.51  ? 753  THR A O   1 
ATOM 1114 C CB  . THR A 1 742  ? 220.067 186.928 177.513 1.00 56.41  ? 753  THR A CB  1 
ATOM 1115 O OG1 . THR A 1 742  ? 221.387 186.673 178.005 1.00 61.24  ? 753  THR A OG1 1 
ATOM 1116 C CG2 . THR A 1 742  ? 220.100 188.127 176.578 1.00 56.20  ? 753  THR A CG2 1 
ATOM 1117 N N   . PHE A 1 743  ? 217.033 186.023 178.215 1.00 53.65  ? 754  PHE A N   1 
ATOM 1118 C CA  . PHE A 1 743  ? 215.615 185.938 177.882 1.00 51.68  ? 754  PHE A CA  1 
ATOM 1119 C C   . PHE A 1 743  ? 214.771 186.714 178.887 1.00 54.66  ? 754  PHE A C   1 
ATOM 1120 O O   . PHE A 1 743  ? 213.842 187.438 178.514 1.00 60.46  ? 754  PHE A O   1 
ATOM 1121 C CB  . PHE A 1 743  ? 215.188 184.467 177.823 1.00 51.31  ? 754  PHE A CB  1 
ATOM 1122 C CG  . PHE A 1 743  ? 213.702 184.258 177.863 1.00 46.43  ? 754  PHE A CG  1 
ATOM 1123 C CD1 . PHE A 1 743  ? 212.936 184.417 176.724 1.00 40.01  ? 754  PHE A CD1 1 
ATOM 1124 C CD2 . PHE A 1 743  ? 213.073 183.878 179.037 1.00 48.63  ? 754  PHE A CD2 1 
ATOM 1125 C CE1 . PHE A 1 743  ? 211.574 184.220 176.758 1.00 37.68  ? 754  PHE A CE1 1 
ATOM 1126 C CE2 . PHE A 1 743  ? 211.712 183.680 179.075 1.00 45.34  ? 754  PHE A CE2 1 
ATOM 1127 C CZ  . PHE A 1 743  ? 210.962 183.851 177.933 1.00 42.48  ? 754  PHE A CZ  1 
ATOM 1128 N N   . THR A 1 744  ? 215.090 186.577 180.176 1.00 54.76  ? 755  THR A N   1 
ATOM 1129 C CA  . THR A 1 744  ? 214.287 187.204 181.220 1.00 49.48  ? 755  THR A CA  1 
ATOM 1130 C C   . THR A 1 744  ? 214.535 188.706 181.302 1.00 53.35  ? 755  THR A C   1 
ATOM 1131 O O   . THR A 1 744  ? 213.599 189.481 181.530 1.00 60.13  ? 755  THR A O   1 
ATOM 1132 C CB  . THR A 1 744  ? 214.572 186.545 182.571 1.00 53.72  ? 755  THR A CB  1 
ATOM 1133 O OG1 . THR A 1 744  ? 214.594 185.120 182.426 1.00 54.96  ? 755  THR A OG1 1 
ATOM 1134 C CG2 . THR A 1 744  ? 213.510 186.925 183.574 1.00 56.29  ? 755  THR A CG2 1 
ATOM 1135 N N   . ARG A 1 745  ? 215.788 189.141 181.140 1.00 53.83  ? 756  ARG A N   1 
ATOM 1136 C CA  . ARG A 1 745  ? 216.084 190.563 181.290 1.00 51.18  ? 756  ARG A CA  1 
ATOM 1137 C C   . ARG A 1 745  ? 215.461 191.396 180.176 1.00 54.38  ? 756  ARG A C   1 
ATOM 1138 O O   . ARG A 1 745  ? 215.232 192.598 180.356 1.00 58.86  ? 756  ARG A O   1 
ATOM 1139 C CB  . ARG A 1 745  ? 217.594 190.783 181.349 1.00 50.07  ? 756  ARG A CB  1 
ATOM 1140 C CG  . ARG A 1 745  ? 218.190 190.450 182.706 1.00 55.81  ? 756  ARG A CG  1 
ATOM 1141 C CD  . ARG A 1 745  ? 219.643 190.876 182.804 1.00 58.13  ? 756  ARG A CD  1 
ATOM 1142 N NE  . ARG A 1 745  ? 220.531 189.983 182.069 1.00 59.68  ? 756  ARG A NE  1 
ATOM 1143 C CZ  . ARG A 1 745  ? 221.754 189.657 182.464 1.00 58.82  ? 756  ARG A CZ  1 
ATOM 1144 N NH1 . ARG A 1 745  ? 222.268 190.135 183.585 1.00 49.28  ? 756  ARG A NH1 1 
ATOM 1145 N NH2 . ARG A 1 745  ? 222.480 188.833 181.714 1.00 64.07  ? 756  ARG A NH2 1 
ATOM 1146 N N   . LEU A 1 746  ? 215.184 190.786 179.022 1.00 53.29  ? 757  LEU A N   1 
ATOM 1147 C CA  . LEU A 1 746  ? 214.523 191.519 177.948 1.00 54.53  ? 757  LEU A CA  1 
ATOM 1148 C C   . LEU A 1 746  ? 213.047 191.747 178.245 1.00 52.69  ? 757  LEU A C   1 
ATOM 1149 O O   . LEU A 1 746  ? 212.423 192.622 177.635 1.00 50.08  ? 757  LEU A O   1 
ATOM 1150 C CB  . LEU A 1 746  ? 214.693 190.780 176.622 1.00 52.24  ? 757  LEU A CB  1 
ATOM 1151 C CG  . LEU A 1 746  ? 216.114 190.777 176.059 1.00 52.75  ? 757  LEU A CG  1 
ATOM 1152 C CD1 . LEU A 1 746  ? 216.225 189.794 174.911 1.00 57.88  ? 757  LEU A CD1 1 
ATOM 1153 C CD2 . LEU A 1 746  ? 216.513 192.177 175.614 1.00 54.01  ? 757  LEU A CD2 1 
ATOM 1154 N N   . THR A 1 747  ? 212.475 190.980 179.172 1.00 52.98  ? 758  THR A N   1 
ATOM 1155 C CA  . THR A 1 747  ? 211.067 191.119 179.524 1.00 52.19  ? 758  THR A CA  1 
ATOM 1156 C C   . THR A 1 747  ? 210.806 192.250 180.509 1.00 53.11  ? 758  THR A C   1 
ATOM 1157 O O   . THR A 1 747  ? 209.643 192.493 180.849 1.00 53.61  ? 758  THR A O   1 
ATOM 1158 C CB  . THR A 1 747  ? 210.532 189.807 180.104 1.00 48.02  ? 758  THR A CB  1 
ATOM 1159 O OG1 . THR A 1 747  ? 211.032 189.630 181.435 1.00 61.09  ? 758  THR A OG1 1 
ATOM 1160 C CG2 . THR A 1 747  ? 210.955 188.630 179.243 1.00 50.62  ? 758  THR A CG2 1 
ATOM 1161 N N   . ARG A 1 748  ? 211.846 192.934 180.982 1.00 52.89  ? 759  ARG A N   1 
ATOM 1162 C CA  . ARG A 1 748  ? 211.644 194.081 181.855 1.00 56.23  ? 759  ARG A CA  1 
ATOM 1163 C C   . ARG A 1 748  ? 210.890 195.177 181.114 1.00 63.51  ? 759  ARG A C   1 
ATOM 1164 O O   . ARG A 1 748  ? 211.080 195.382 179.912 1.00 68.89  ? 759  ARG A O   1 
ATOM 1165 C CB  . ARG A 1 748  ? 212.986 194.607 182.363 1.00 57.59  ? 759  ARG A CB  1 
ATOM 1166 C CG  . ARG A 1 748  ? 213.668 193.686 183.360 1.00 61.25  ? 759  ARG A CG  1 
ATOM 1167 C CD  . ARG A 1 748  ? 214.894 194.341 183.973 1.00 58.29  ? 759  ARG A CD  1 
ATOM 1168 N NE  . ARG A 1 748  ? 215.643 193.411 184.810 1.00 63.13  ? 759  ARG A NE  1 
ATOM 1169 C CZ  . ARG A 1 748  ? 216.811 193.684 185.374 1.00 66.82  ? 759  ARG A CZ  1 
ATOM 1170 N NH1 . ARG A 1 748  ? 217.399 194.858 185.211 1.00 74.91  ? 759  ARG A NH1 1 
ATOM 1171 N NH2 . ARG A 1 748  ? 217.405 192.756 186.119 1.00 63.94  ? 759  ARG A NH2 1 
ATOM 1172 N N   . ASN A 1 749  ? 210.024 195.880 181.839 1.00 67.17  ? 760  ASN A N   1 
ATOM 1173 C CA  . ASN A 1 749  ? 209.153 196.868 181.220 1.00 68.43  ? 760  ASN A CA  1 
ATOM 1174 C C   . ASN A 1 749  ? 209.958 198.021 180.623 1.00 70.37  ? 760  ASN A C   1 
ATOM 1175 O O   . ASN A 1 749  ? 211.068 198.339 181.058 1.00 73.58  ? 760  ASN A O   1 
ATOM 1176 C CB  . ASN A 1 749  ? 208.127 197.385 182.232 1.00 68.38  ? 760  ASN A CB  1 
ATOM 1177 C CG  . ASN A 1 749  ? 208.765 198.064 183.436 1.00 69.58  ? 760  ASN A CG  1 
ATOM 1178 O OD1 . ASN A 1 749  ? 209.986 198.181 183.533 1.00 66.07  ? 760  ASN A OD1 1 
ATOM 1179 N ND2 . ASN A 1 749  ? 207.930 198.517 184.362 1.00 71.46  ? 760  ASN A ND2 1 
ATOM 1180 N N   . ASP A 1 750  ? 209.384 198.634 179.591 1.00 69.13  ? 761  ASP A N   1 
ATOM 1181 C CA  . ASP A 1 750  ? 209.989 199.769 178.912 1.00 77.44  ? 761  ASP A CA  1 
ATOM 1182 C C   . ASP A 1 750  ? 208.929 200.845 178.739 1.00 86.81  ? 761  ASP A C   1 
ATOM 1183 O O   . ASP A 1 750  ? 207.788 200.550 178.377 1.00 91.56  ? 761  ASP A O   1 
ATOM 1184 C CB  . ASP A 1 750  ? 210.570 199.364 177.549 1.00 80.24  ? 761  ASP A CB  1 
ATOM 1185 C CG  . ASP A 1 750  ? 211.396 200.467 176.907 1.00 88.50  ? 761  ASP A CG  1 
ATOM 1186 O OD1 . ASP A 1 750  ? 211.426 201.595 177.444 1.00 93.02  ? 761  ASP A OD1 1 
ATOM 1187 O OD2 . ASP A 1 750  ? 212.017 200.204 175.856 1.00 87.62  ? 761  ASP A OD2 1 
ATOM 1188 N N   . GLU A 1 751  ? 209.301 202.104 178.970 1.00 88.33  ? 762  GLU A N   1 
ATOM 1189 C CA  . GLU A 1 751  ? 208.289 203.191 178.909 1.00 91.27  ? 762  GLU A CA  1 
ATOM 1190 C C   . GLU A 1 751  ? 208.191 203.748 177.482 1.00 92.57  ? 762  GLU A C   1 
ATOM 1191 O O   . GLU A 1 751  ? 207.150 204.361 177.162 1.00 94.05  ? 762  GLU A O   1 
ATOM 1192 C CB  . GLU A 1 751  ? 208.658 204.297 179.896 1.00 93.97  ? 762  GLU A CB  1 
ATOM 1193 C CG  . GLU A 1 751  ? 207.531 205.299 180.133 1.00 98.17  ? 762  GLU A CG  1 
ATOM 1194 C CD  . GLU A 1 751  ? 207.860 206.386 181.140 1.00 103.38 ? 762  GLU A CD  1 
ATOM 1195 O OE1 . GLU A 1 751  ? 208.990 206.378 181.673 1.00 105.41 ? 762  GLU A OE1 1 
ATOM 1196 O OE2 . GLU A 1 751  ? 206.985 207.240 181.393 1.00 98.29  ? 762  GLU A OE2 1 
ATOM 1197 N N   . LYS A 1 752  ? 209.208 203.525 176.648 1.00 90.84  ? 763  LYS A N   1 
ATOM 1198 C CA  . LYS A 1 752  ? 209.206 204.126 175.320 1.00 88.66  ? 763  LYS A CA  1 
ATOM 1199 C C   . LYS A 1 752  ? 208.687 203.199 174.229 1.00 85.99  ? 763  LYS A C   1 
ATOM 1200 O O   . LYS A 1 752  ? 208.386 203.676 173.128 1.00 87.15  ? 763  LYS A O   1 
ATOM 1201 C CB  . LYS A 1 752  ? 210.617 204.594 174.947 1.00 92.04  ? 763  LYS A CB  1 
ATOM 1202 C CG  . LYS A 1 752  ? 211.258 205.540 175.954 1.00 91.18  ? 763  LYS A CG  1 
ATOM 1203 C CD  . LYS A 1 752  ? 212.150 204.794 176.936 1.00 92.02  ? 763  LYS A CD  1 
ATOM 1204 C CE  . LYS A 1 752  ? 212.948 205.755 177.801 1.00 98.88  ? 763  LYS A CE  1 
ATOM 1205 N NZ  . LYS A 1 752  ? 214.020 205.054 178.562 1.00 104.61 ? 763  LYS A NZ  1 
ATOM 1206 N N   . ASP A 1 753  ? 208.614 201.894 174.521 1.00 84.76  ? 764  ASP A N   1 
ATOM 1207 C CA  . ASP A 1 753  ? 208.227 200.895 173.482 1.00 82.30  ? 764  ASP A CA  1 
ATOM 1208 C C   . ASP A 1 753  ? 206.761 201.063 173.067 1.00 85.92  ? 764  ASP A C   1 
ATOM 1209 O O   . ASP A 1 753  ? 206.018 201.792 173.762 1.00 89.29  ? 764  ASP A O   1 
ATOM 1210 C CB  . ASP A 1 753  ? 208.529 199.473 173.936 1.00 79.08  ? 764  ASP A CB  1 
ATOM 1211 C CG  . ASP A 1 753  ? 207.766 198.977 175.157 1.00 82.33  ? 764  ASP A CG  1 
ATOM 1212 O OD1 . ASP A 1 753  ? 206.970 199.760 175.716 1.00 87.96  ? 764  ASP A OD1 1 
ATOM 1213 O OD2 . ASP A 1 753  ? 207.972 197.805 175.537 1.00 80.80  ? 764  ASP A OD2 1 
ATOM 1214 N N   . ASP A 1 754  ? 206.345 200.396 171.990 1.00 83.76  ? 765  ASP A N   1 
ATOM 1215 C CA  . ASP A 1 754  ? 204.943 200.519 171.512 1.00 77.05  ? 765  ASP A CA  1 
ATOM 1216 C C   . ASP A 1 754  ? 204.071 199.498 172.243 1.00 76.14  ? 765  ASP A C   1 
ATOM 1217 O O   . ASP A 1 754  ? 204.547 198.921 173.241 1.00 80.59  ? 765  ASP A O   1 
ATOM 1218 C CB  . ASP A 1 754  ? 204.853 200.354 170.005 1.00 75.55  ? 765  ASP A CB  1 
ATOM 1219 C CG  . ASP A 1 754  ? 205.059 198.939 169.488 1.00 77.09  ? 765  ASP A CG  1 
ATOM 1220 O OD1 . ASP A 1 754  ? 206.145 198.377 169.736 1.00 74.66  ? 765  ASP A OD1 1 
ATOM 1221 O OD2 . ASP A 1 754  ? 204.130 198.414 168.843 1.00 77.90  ? 765  ASP A OD2 1 
ATOM 1222 N N   . TRP A 1 755  ? 202.844 199.292 171.771 1.00 72.73  ? 766  TRP A N   1 
ATOM 1223 C CA  . TRP A 1 755  ? 201.937 198.278 172.366 1.00 73.96  ? 766  TRP A CA  1 
ATOM 1224 C C   . TRP A 1 755  ? 202.433 196.868 172.042 1.00 72.23  ? 766  TRP A C   1 
ATOM 1225 O O   . TRP A 1 755  ? 202.358 195.998 172.936 1.00 75.90  ? 766  TRP A O   1 
ATOM 1226 C CB  . TRP A 1 755  ? 200.507 198.480 171.844 1.00 74.61  ? 766  TRP A CB  1 
ATOM 1227 C CG  . TRP A 1 755  ? 200.338 198.107 170.395 1.00 75.29  ? 766  TRP A CG  1 
ATOM 1228 C CD1 . TRP A 1 755  ? 200.515 198.916 169.311 1.00 75.46  ? 766  TRP A CD1 1 
ATOM 1229 C CD2 . TRP A 1 755  ? 199.971 196.811 169.871 1.00 77.36  ? 766  TRP A CD2 1 
ATOM 1230 N NE1 . TRP A 1 755  ? 200.280 198.221 168.155 1.00 76.23  ? 766  TRP A NE1 1 
ATOM 1231 C CE2 . TRP A 1 755  ? 199.947 196.928 168.465 1.00 80.91  ? 766  TRP A CE2 1 
ATOM 1232 C CE3 . TRP A 1 755  ? 199.665 195.574 170.449 1.00 75.60  ? 766  TRP A CE3 1 
ATOM 1233 C CZ2 . TRP A 1 755  ? 199.627 195.856 167.636 1.00 84.60  ? 766  TRP A CZ2 1 
ATOM 1234 C CZ3 . TRP A 1 755  ? 199.352 194.514 169.627 1.00 79.48  ? 766  TRP A CZ3 1 
ATOM 1235 C CH2 . TRP A 1 755  ? 199.334 194.656 168.240 1.00 87.09  ? 766  TRP A CH2 1 
ATOM 1236 N N   . LEU A 1 756  ? 202.924 196.642 170.818 1.00 67.77  ? 767  LEU A N   1 
ATOM 1237 C CA  . LEU A 1 756  ? 203.298 195.284 170.434 1.00 63.98  ? 767  LEU A CA  1 
ATOM 1238 C C   . LEU A 1 756  ? 204.448 194.757 171.285 1.00 59.10  ? 767  LEU A C   1 
ATOM 1239 O O   . LEU A 1 756  ? 204.383 193.636 171.804 1.00 63.16  ? 767  LEU A O   1 
ATOM 1240 C CB  . LEU A 1 756  ? 203.666 195.244 168.950 1.00 57.84  ? 767  LEU A CB  1 
ATOM 1241 C CG  . LEU A 1 756  ? 204.143 193.901 168.397 1.00 48.88  ? 767  LEU A CG  1 
ATOM 1242 C CD1 . LEU A 1 756  ? 203.062 192.844 168.549 1.00 51.47  ? 767  LEU A CD1 1 
ATOM 1243 C CD2 . LEU A 1 756  ? 204.556 194.044 166.941 1.00 49.92  ? 767  LEU A CD2 1 
ATOM 1244 N N   . LYS A 1 757  ? 205.509 195.552 171.434 1.00 54.77  ? 768  LYS A N   1 
ATOM 1245 C CA  . LYS A 1 757  ? 206.651 195.132 172.241 1.00 55.29  ? 768  LYS A CA  1 
ATOM 1246 C C   . LYS A 1 757  ? 206.244 194.921 173.694 1.00 61.96  ? 768  LYS A C   1 
ATOM 1247 O O   . LYS A 1 757  ? 206.663 193.951 174.337 1.00 69.30  ? 768  LYS A O   1 
ATOM 1248 C CB  . LYS A 1 757  ? 207.768 196.172 172.141 1.00 54.85  ? 768  LYS A CB  1 
ATOM 1249 C CG  . LYS A 1 757  ? 208.407 196.272 170.768 1.00 54.68  ? 768  LYS A CG  1 
ATOM 1250 C CD  . LYS A 1 757  ? 209.335 197.473 170.686 1.00 59.45  ? 768  LYS A CD  1 
ATOM 1251 C CE  . LYS A 1 757  ? 210.044 197.534 169.344 1.00 61.32  ? 768  LYS A CE  1 
ATOM 1252 N NZ  . LYS A 1 757  ? 210.946 198.716 169.251 1.00 64.57  ? 768  LYS A NZ  1 
ATOM 1253 N N   . ARG A 1 758  ? 205.426 195.832 174.226 1.00 61.48  ? 769  ARG A N   1 
ATOM 1254 C CA  . ARG A 1 758  ? 204.967 195.708 175.605 1.00 61.96  ? 769  ARG A CA  1 
ATOM 1255 C C   . ARG A 1 758  ? 204.143 194.441 175.798 1.00 61.16  ? 769  ARG A C   1 
ATOM 1256 O O   . ARG A 1 758  ? 204.312 193.725 176.793 1.00 63.92  ? 769  ARG A O   1 
ATOM 1257 C CB  . ARG A 1 758  ? 204.156 196.945 175.992 1.00 63.83  ? 769  ARG A CB  1 
ATOM 1258 C CG  . ARG A 1 758  ? 203.312 196.784 177.242 1.00 69.98  ? 769  ARG A CG  1 
ATOM 1259 C CD  . ARG A 1 758  ? 202.718 198.116 177.672 1.00 81.87  ? 769  ARG A CD  1 
ATOM 1260 N NE  . ARG A 1 758  ? 203.563 199.242 177.291 1.00 83.77  ? 769  ARG A NE  1 
ATOM 1261 C CZ  . ARG A 1 758  ? 203.178 200.235 176.502 1.00 85.39  ? 769  ARG A CZ  1 
ATOM 1262 N NH1 . ARG A 1 758  ? 201.959 200.278 175.990 1.00 85.62  ? 769  ARG A NH1 1 
ATOM 1263 N NH2 . ARG A 1 758  ? 204.037 201.210 176.219 1.00 82.81  ? 769  ARG A NH2 1 
ATOM 1264 N N   . GLY A 1 759  ? 203.250 194.145 174.851 1.00 61.81  ? 770  GLY A N   1 
ATOM 1265 C CA  . GLY A 1 759  ? 202.466 192.926 174.945 1.00 64.74  ? 770  GLY A CA  1 
ATOM 1266 C C   . GLY A 1 759  ? 203.321 191.677 174.869 1.00 64.02  ? 770  GLY A C   1 
ATOM 1267 O O   . GLY A 1 759  ? 203.098 190.717 175.613 1.00 69.37  ? 770  GLY A O   1 
ATOM 1268 N N   . VAL A 1 760  ? 204.313 191.671 173.974 1.00 60.24  ? 771  VAL A N   1 
ATOM 1269 C CA  . VAL A 1 760  ? 205.210 190.523 173.870 1.00 55.67  ? 771  VAL A CA  1 
ATOM 1270 C C   . VAL A 1 760  ? 205.961 190.314 175.179 1.00 58.09  ? 771  VAL A C   1 
ATOM 1271 O O   . VAL A 1 760  ? 206.046 189.191 175.693 1.00 59.07  ? 771  VAL A O   1 
ATOM 1272 C CB  . VAL A 1 760  ? 206.180 190.700 172.688 1.00 52.37  ? 771  VAL A CB  1 
ATOM 1273 C CG1 . VAL A 1 760  ? 207.231 189.605 172.701 1.00 52.80  ? 771  VAL A CG1 1 
ATOM 1274 C CG2 . VAL A 1 760  ? 205.425 190.681 171.372 1.00 53.20  ? 771  VAL A CG2 1 
ATOM 1275 N N   . ARG A 1 761  ? 206.507 191.396 175.743 1.00 55.46  ? 772  ARG A N   1 
ATOM 1276 C CA  . ARG A 1 761  ? 207.228 191.291 177.009 1.00 52.17  ? 772  ARG A CA  1 
ATOM 1277 C C   . ARG A 1 761  ? 206.325 190.753 178.111 1.00 58.12  ? 772  ARG A C   1 
ATOM 1278 O O   . ARG A 1 761  ? 206.699 189.827 178.842 1.00 64.74  ? 772  ARG A O   1 
ATOM 1279 C CB  . ARG A 1 761  ? 207.793 192.653 177.413 1.00 47.95  ? 772  ARG A CB  1 
ATOM 1280 C CG  . ARG A 1 761  ? 208.866 193.214 176.498 1.00 48.46  ? 772  ARG A CG  1 
ATOM 1281 C CD  . ARG A 1 761  ? 209.405 194.518 177.066 1.00 48.94  ? 772  ARG A CD  1 
ATOM 1282 N NE  . ARG A 1 761  ? 209.816 195.455 176.028 1.00 53.12  ? 772  ARG A NE  1 
ATOM 1283 C CZ  . ARG A 1 761  ? 211.072 195.654 175.653 1.00 55.22  ? 772  ARG A CZ  1 
ATOM 1284 N NH1 . ARG A 1 761  ? 212.072 194.992 176.209 1.00 49.91  ? 772  ARG A NH1 1 
ATOM 1285 N NH2 . ARG A 1 761  ? 211.330 196.543 174.698 1.00 57.29  ? 772  ARG A NH2 1 
ATOM 1286 N N   . SER A 1 762  ? 205.124 191.325 178.242 1.00 56.83  ? 773  SER A N   1 
ATOM 1287 C CA  . SER A 1 762  ? 204.226 190.927 179.320 1.00 57.63  ? 773  SER A CA  1 
ATOM 1288 C C   . SER A 1 762  ? 203.816 189.466 179.185 1.00 58.93  ? 773  SER A C   1 
ATOM 1289 O O   . SER A 1 762  ? 203.840 188.712 180.164 1.00 63.48  ? 773  SER A O   1 
ATOM 1290 C CB  . SER A 1 762  ? 202.996 191.835 179.337 1.00 61.02  ? 773  SER A CB  1 
ATOM 1291 O OG  . SER A 1 762  ? 202.336 191.822 178.084 1.00 66.18  ? 773  SER A OG  1 
ATOM 1292 N N   . ASP A 1 763  ? 203.447 189.044 177.972 1.00 56.18  ? 774  ASP A N   1 
ATOM 1293 C CA  . ASP A 1 763  ? 203.028 187.663 177.767 1.00 57.55  ? 774  ASP A CA  1 
ATOM 1294 C C   . ASP A 1 763  ? 204.165 186.677 177.997 1.00 57.69  ? 774  ASP A C   1 
ATOM 1295 O O   . ASP A 1 763  ? 203.956 185.636 178.635 1.00 60.51  ? 774  ASP A O   1 
ATOM 1296 C CB  . ASP A 1 763  ? 202.460 187.493 176.357 1.00 61.81  ? 774  ASP A CB  1 
ATOM 1297 C CG  . ASP A 1 763  ? 201.065 188.069 176.219 1.00 76.22  ? 774  ASP A CG  1 
ATOM 1298 O OD1 . ASP A 1 763  ? 200.368 187.716 175.245 1.00 77.56  ? 774  ASP A OD1 1 
ATOM 1299 O OD2 . ASP A 1 763  ? 200.664 188.874 177.086 1.00 76.72  ? 774  ASP A OD2 1 
ATOM 1300 N N   . ALA A 1 764  ? 205.368 186.982 177.498 1.00 53.91  ? 775  ALA A N   1 
ATOM 1301 C CA  . ALA A 1 764  ? 206.498 186.088 177.716 1.00 51.67  ? 775  ALA A CA  1 
ATOM 1302 C C   . ALA A 1 764  ? 206.829 185.972 179.197 1.00 55.96  ? 775  ALA A C   1 
ATOM 1303 O O   . ALA A 1 764  ? 207.065 184.868 179.702 1.00 58.26  ? 775  ALA A O   1 
ATOM 1304 C CB  . ALA A 1 764  ? 207.714 186.575 176.928 1.00 50.01  ? 775  ALA A CB  1 
ATOM 1305 N N   . ALA A 1 765  ? 206.837 187.100 179.913 1.00 56.62  ? 776  ALA A N   1 
ATOM 1306 C CA  . ALA A 1 765  ? 207.126 187.065 181.343 1.00 52.74  ? 776  ALA A CA  1 
ATOM 1307 C C   . ALA A 1 765  ? 206.067 186.271 182.096 1.00 54.66  ? 776  ALA A C   1 
ATOM 1308 O O   . ALA A 1 765  ? 206.390 185.468 182.981 1.00 55.85  ? 776  ALA A O   1 
ATOM 1309 C CB  . ALA A 1 765  ? 207.230 188.488 181.891 1.00 50.97  ? 776  ALA A CB  1 
ATOM 1310 N N   . ASP A 1 766  ? 204.792 186.478 181.754 1.00 57.29  ? 777  ASP A N   1 
ATOM 1311 C CA  . ASP A 1 766  ? 203.721 185.762 182.437 1.00 58.87  ? 777  ASP A CA  1 
ATOM 1312 C C   . ASP A 1 766  ? 203.827 184.260 182.211 1.00 56.01  ? 777  ASP A C   1 
ATOM 1313 O O   . ASP A 1 766  ? 203.699 183.476 183.158 1.00 58.55  ? 777  ASP A O   1 
ATOM 1314 C CB  . ASP A 1 766  ? 202.360 186.281 181.971 1.00 69.90  ? 777  ASP A CB  1 
ATOM 1315 C CG  . ASP A 1 766  ? 202.075 187.687 182.461 1.00 81.18  ? 777  ASP A CG  1 
ATOM 1316 O OD1 . ASP A 1 766  ? 202.876 188.213 183.261 1.00 79.52  ? 777  ASP A OD1 1 
ATOM 1317 O OD2 . ASP A 1 766  ? 201.049 188.266 182.046 1.00 82.77  ? 777  ASP A OD2 1 
ATOM 1318 N N   . LEU A 1 767  ? 204.073 183.839 180.967 1.00 55.97  ? 778  LEU A N   1 
ATOM 1319 C CA  . LEU A 1 767  ? 204.203 182.409 180.698 1.00 58.62  ? 778  LEU A CA  1 
ATOM 1320 C C   . LEU A 1 767  ? 205.418 181.819 181.405 1.00 56.19  ? 778  LEU A C   1 
ATOM 1321 O O   . LEU A 1 767  ? 205.337 180.727 181.988 1.00 57.35  ? 778  LEU A O   1 
ATOM 1322 C CB  . LEU A 1 767  ? 204.285 182.159 179.194 1.00 60.58  ? 778  LEU A CB  1 
ATOM 1323 C CG  . LEU A 1 767  ? 204.420 180.691 178.786 1.00 54.23  ? 778  LEU A CG  1 
ATOM 1324 C CD1 . LEU A 1 767  ? 203.183 179.906 179.191 1.00 50.18  ? 778  LEU A CD1 1 
ATOM 1325 C CD2 . LEU A 1 767  ? 204.670 180.569 177.295 1.00 55.04  ? 778  LEU A CD2 1 
ATOM 1326 N N   . TYR A 1 768  ? 206.550 182.528 181.373 1.00 53.41  ? 779  TYR A N   1 
ATOM 1327 C CA  . TYR A 1 768  ? 207.761 182.023 182.011 1.00 47.23  ? 779  TYR A CA  1 
ATOM 1328 C C   . TYR A 1 768  ? 207.561 181.865 183.513 1.00 47.59  ? 779  TYR A C   1 
ATOM 1329 O O   . TYR A 1 768  ? 207.993 180.871 184.107 1.00 45.75  ? 779  TYR A O   1 
ATOM 1330 C CB  . TYR A 1 768  ? 208.933 182.960 181.713 1.00 46.10  ? 779  TYR A CB  1 
ATOM 1331 C CG  . TYR A 1 768  ? 210.227 182.576 182.392 1.00 49.66  ? 779  TYR A CG  1 
ATOM 1332 C CD1 . TYR A 1 768  ? 210.656 181.256 182.421 1.00 48.38  ? 779  TYR A CD1 1 
ATOM 1333 C CD2 . TYR A 1 768  ? 211.025 183.537 183.000 1.00 49.55  ? 779  TYR A CD2 1 
ATOM 1334 C CE1 . TYR A 1 768  ? 211.839 180.902 183.039 1.00 47.31  ? 779  TYR A CE1 1 
ATOM 1335 C CE2 . TYR A 1 768  ? 212.210 183.193 183.619 1.00 48.20  ? 779  TYR A CE2 1 
ATOM 1336 C CZ  . TYR A 1 768  ? 212.612 181.875 183.636 1.00 50.75  ? 779  TYR A CZ  1 
ATOM 1337 O OH  . TYR A 1 768  ? 213.792 181.531 184.253 1.00 58.96  ? 779  TYR A OH  1 
ATOM 1338 N N   . ARG A 1 769  ? 206.903 182.839 184.145 1.00 51.12  ? 780  ARG A N   1 
ATOM 1339 C CA  . ARG A 1 769  ? 206.651 182.739 185.579 1.00 50.04  ? 780  ARG A CA  1 
ATOM 1340 C C   . ARG A 1 769  ? 205.626 181.656 185.889 1.00 51.03  ? 780  ARG A C   1 
ATOM 1341 O O   . ARG A 1 769  ? 205.707 181.000 186.935 1.00 49.56  ? 780  ARG A O   1 
ATOM 1342 C CB  . ARG A 1 769  ? 206.196 184.090 186.127 1.00 45.54  ? 780  ARG A CB  1 
ATOM 1343 C CG  . ARG A 1 769  ? 207.261 185.168 186.039 1.00 47.39  ? 780  ARG A CG  1 
ATOM 1344 C CD  . ARG A 1 769  ? 206.853 186.403 186.812 1.00 51.28  ? 780  ARG A CD  1 
ATOM 1345 N NE  . ARG A 1 769  ? 206.960 186.189 188.250 1.00 62.00  ? 780  ARG A NE  1 
ATOM 1346 C CZ  . ARG A 1 769  ? 206.679 187.105 189.165 1.00 68.79  ? 780  ARG A CZ  1 
ATOM 1347 N NH1 . ARG A 1 769  ? 206.272 188.318 188.827 1.00 65.87  ? 780  ARG A NH1 1 
ATOM 1348 N NH2 . ARG A 1 769  ? 206.811 186.798 190.452 1.00 73.21  ? 780  ARG A NH2 1 
ATOM 1349 N N   . GLN A 1 770  ? 204.651 181.454 184.998 1.00 51.65  ? 781  GLN A N   1 
ATOM 1350 C CA  . GLN A 1 770  ? 203.673 180.393 185.206 1.00 49.22  ? 781  GLN A CA  1 
ATOM 1351 C C   . GLN A 1 770  ? 204.317 179.017 185.124 1.00 53.40  ? 781  GLN A C   1 
ATOM 1352 O O   . GLN A 1 770  ? 203.899 178.093 185.833 1.00 56.92  ? 781  GLN A O   1 
ATOM 1353 C CB  . GLN A 1 770  ? 202.540 180.517 184.186 1.00 52.14  ? 781  GLN A CB  1 
ATOM 1354 C CG  . GLN A 1 770  ? 201.372 179.572 184.425 1.00 55.26  ? 781  GLN A CG  1 
ATOM 1355 C CD  . GLN A 1 770  ? 201.503 178.272 183.656 1.00 60.38  ? 781  GLN A CD  1 
ATOM 1356 O OE1 . GLN A 1 770  ? 202.182 178.209 182.632 1.00 62.73  ? 781  GLN A OE1 1 
ATOM 1357 N NE2 . GLN A 1 770  ? 200.851 177.225 184.148 1.00 61.42  ? 781  GLN A NE2 1 
ATOM 1358 N N   . GLN A 1 771  ? 205.331 178.858 184.276 1.00 54.08  ? 782  GLN A N   1 
ATOM 1359 C CA  . GLN A 1 771  ? 206.006 177.573 184.138 1.00 54.43  ? 782  GLN A CA  1 
ATOM 1360 C C   . GLN A 1 771  ? 207.107 177.351 185.168 1.00 55.87  ? 782  GLN A C   1 
ATOM 1361 O O   . GLN A 1 771  ? 207.750 176.296 185.143 1.00 57.81  ? 782  GLN A O   1 
ATOM 1362 C CB  . GLN A 1 771  ? 206.591 177.431 182.730 1.00 57.24  ? 782  GLN A CB  1 
ATOM 1363 C CG  . GLN A 1 771  ? 205.554 177.106 181.672 1.00 57.26  ? 782  GLN A CG  1 
ATOM 1364 C CD  . GLN A 1 771  ? 204.860 175.785 181.936 1.00 59.58  ? 782  GLN A CD  1 
ATOM 1365 O OE1 . GLN A 1 771  ? 205.508 174.751 182.094 1.00 62.58  ? 782  GLN A OE1 1 
ATOM 1366 N NE2 . GLN A 1 771  ? 203.533 175.813 181.986 1.00 55.66  ? 782  GLN A NE2 1 
ATOM 1367 N N   . ASP A 1 772  ? 207.341 178.306 186.065 1.00 55.86  ? 783  ASP A N   1 
ATOM 1368 C CA  . ASP A 1 772  ? 208.425 178.186 187.028 1.00 55.93  ? 783  ASP A CA  1 
ATOM 1369 C C   . ASP A 1 772  ? 208.009 177.335 188.229 1.00 56.75  ? 783  ASP A C   1 
ATOM 1370 O O   . ASP A 1 772  ? 206.824 177.138 188.512 1.00 62.16  ? 783  ASP A O   1 
ATOM 1371 C CB  . ASP A 1 772  ? 208.874 179.569 187.498 1.00 52.44  ? 783  ASP A CB  1 
ATOM 1372 C CG  . ASP A 1 772  ? 210.290 179.571 188.033 1.00 55.07  ? 783  ASP A CG  1 
ATOM 1373 O OD1 . ASP A 1 772  ? 210.992 178.554 187.859 1.00 53.94  ? 783  ASP A OD1 1 
ATOM 1374 O OD2 . ASP A 1 772  ? 210.702 180.589 188.627 1.00 60.07  ? 783  ASP A OD2 1 
ATOM 1375 N N   . LEU A 1 773  ? 209.017 176.827 188.937 1.00 48.48  ? 784  LEU A N   1 
ATOM 1376 C CA  . LEU A 1 773  ? 208.842 176.042 190.155 1.00 48.14  ? 784  LEU A CA  1 
ATOM 1377 C C   . LEU A 1 773  ? 209.440 176.823 191.319 1.00 51.89  ? 784  LEU A C   1 
ATOM 1378 O O   . LEU A 1 773  ? 210.597 177.250 191.249 1.00 52.38  ? 784  LEU A O   1 
ATOM 1379 C CB  . LEU A 1 773  ? 209.510 174.673 190.019 1.00 48.91  ? 784  LEU A CB  1 
ATOM 1380 C CG  . LEU A 1 773  ? 209.789 173.860 191.287 1.00 46.99  ? 784  LEU A CG  1 
ATOM 1381 C CD1 . LEU A 1 773  ? 208.504 173.463 191.990 1.00 49.35  ? 784  LEU A CD1 1 
ATOM 1382 C CD2 . LEU A 1 773  ? 210.621 172.630 190.958 1.00 41.62  ? 784  LEU A CD2 1 
ATOM 1383 N N   . ASN A 1 774  ? 208.660 177.007 192.383 1.00 49.45  ? 785  ASN A N   1 
ATOM 1384 C CA  . ASN A 1 774  ? 209.066 177.854 193.498 1.00 42.77  ? 785  ASN A CA  1 
ATOM 1385 C C   . ASN A 1 774  ? 208.967 177.107 194.823 1.00 42.91  ? 785  ASN A C   1 
ATOM 1386 O O   . ASN A 1 774  ? 208.049 176.309 195.031 1.00 45.57  ? 785  ASN A O   1 
ATOM 1387 C CB  . ASN A 1 774  ? 208.209 179.122 193.558 1.00 42.91  ? 785  ASN A CB  1 
ATOM 1388 C CG  . ASN A 1 774  ? 208.544 180.103 192.452 1.00 46.85  ? 785  ASN A CG  1 
ATOM 1389 O OD1 . ASN A 1 774  ? 209.674 180.149 191.969 1.00 47.48  ? 785  ASN A OD1 1 
ATOM 1390 N ND2 . ASN A 1 774  ? 207.558 180.896 192.046 1.00 54.57  ? 785  ASN A ND2 1 
ATOM 1391 N N   . VAL A 1 775  ? 209.921 177.371 195.715 1.00 37.23  ? 786  VAL A N   1 
ATOM 1392 C CA  . VAL A 1 775  ? 209.902 176.854 197.081 1.00 35.13  ? 786  VAL A CA  1 
ATOM 1393 C C   . VAL A 1 775  ? 210.111 178.023 198.034 1.00 41.60  ? 786  VAL A C   1 
ATOM 1394 O O   . VAL A 1 775  ? 211.132 178.713 197.958 1.00 47.39  ? 786  VAL A O   1 
ATOM 1395 C CB  . VAL A 1 775  ? 210.979 175.776 197.301 1.00 35.16  ? 786  VAL A CB  1 
ATOM 1396 C CG1 . VAL A 1 775  ? 210.923 175.256 198.729 1.00 33.64  ? 786  VAL A CG1 1 
ATOM 1397 C CG2 . VAL A 1 775  ? 210.809 174.637 196.308 1.00 43.41  ? 786  VAL A CG2 1 
ATOM 1398 N N   . THR A 1 776  ? 209.162 178.234 198.942 1.00 43.29  ? 787  THR A N   1 
ATOM 1399 C CA  . THR A 1 776  ? 209.206 179.384 199.835 1.00 45.63  ? 787  THR A CA  1 
ATOM 1400 C C   . THR A 1 776  ? 209.130 178.929 201.285 1.00 45.14  ? 787  THR A C   1 
ATOM 1401 O O   . THR A 1 776  ? 208.329 178.055 201.630 1.00 47.02  ? 787  THR A O   1 
ATOM 1402 C CB  . THR A 1 776  ? 208.061 180.362 199.534 1.00 49.18  ? 787  THR A CB  1 
ATOM 1403 O OG1 . THR A 1 776  ? 208.095 180.725 198.149 1.00 49.47  ? 787  THR A OG1 1 
ATOM 1404 C CG2 . THR A 1 776  ? 208.203 181.621 200.374 1.00 48.50  ? 787  THR A CG2 1 
ATOM 1405 N N   . LEU A 1 777  ? 209.968 179.527 202.130 1.00 44.91  ? 788  LEU A N   1 
ATOM 1406 C CA  . LEU A 1 777  ? 209.956 179.267 203.564 1.00 47.46  ? 788  LEU A CA  1 
ATOM 1407 C C   . LEU A 1 777  ? 209.864 180.596 204.298 1.00 51.00  ? 788  LEU A C   1 
ATOM 1408 O O   . LEU A 1 777  ? 210.679 181.495 204.062 1.00 54.06  ? 788  LEU A O   1 
ATOM 1409 C CB  . LEU A 1 777  ? 211.205 178.488 203.998 1.00 46.69  ? 788  LEU A CB  1 
ATOM 1410 C CG  . LEU A 1 777  ? 211.318 178.079 205.469 1.00 53.15  ? 788  LEU A CG  1 
ATOM 1411 C CD1 . LEU A 1 777  ? 211.911 176.685 205.582 1.00 56.39  ? 788  LEU A CD1 1 
ATOM 1412 C CD2 . LEU A 1 777  ? 212.169 179.074 206.242 1.00 50.02  ? 788  LEU A CD2 1 
ATOM 1413 N N   . GLU A 1 778  ? 208.884 180.716 205.192 1.00 47.00  ? 789  GLU A N   1 
ATOM 1414 C CA  . GLU A 1 778  ? 208.606 181.989 205.841 1.00 44.35  ? 789  GLU A CA  1 
ATOM 1415 C C   . GLU A 1 778  ? 208.358 181.772 207.326 1.00 48.86  ? 789  GLU A C   1 
ATOM 1416 O O   . GLU A 1 778  ? 207.811 180.742 207.731 1.00 54.65  ? 789  GLU A O   1 
ATOM 1417 C CB  . GLU A 1 778  ? 207.399 182.678 205.186 1.00 43.51  ? 789  GLU A CB  1 
ATOM 1418 C CG  . GLU A 1 778  ? 206.994 184.003 205.810 1.00 48.97  ? 789  GLU A CG  1 
ATOM 1419 C CD  . GLU A 1 778  ? 205.920 184.714 205.010 1.00 55.39  ? 789  GLU A CD  1 
ATOM 1420 O OE1 . GLU A 1 778  ? 206.138 184.957 203.805 1.00 56.76  ? 789  GLU A OE1 1 
ATOM 1421 O OE2 . GLU A 1 778  ? 204.858 185.034 205.584 1.00 63.35  ? 789  GLU A OE2 1 
ATOM 1422 N N   . HIS A 1 779  ? 208.772 182.745 208.136 1.00 49.98  ? 790  HIS A N   1 
ATOM 1423 C CA  . HIS A 1 779  ? 208.577 182.716 209.581 1.00 49.60  ? 790  HIS A CA  1 
ATOM 1424 C C   . HIS A 1 779  ? 207.798 183.955 209.996 1.00 56.86  ? 790  HIS A C   1 
ATOM 1425 O O   . HIS A 1 779  ? 208.166 185.076 209.626 1.00 62.66  ? 790  HIS A O   1 
ATOM 1426 C CB  . HIS A 1 779  ? 209.914 182.650 210.321 1.00 49.80  ? 790  HIS A CB  1 
ATOM 1427 C CG  . HIS A 1 779  ? 209.773 182.487 211.802 1.00 58.46  ? 790  HIS A CG  1 
ATOM 1428 N ND1 . HIS A 1 779  ? 209.504 181.272 212.393 1.00 62.14  ? 790  HIS A ND1 1 
ATOM 1429 C CD2 . HIS A 1 779  ? 209.859 183.385 212.811 1.00 60.20  ? 790  HIS A CD2 1 
ATOM 1430 C CE1 . HIS A 1 779  ? 209.432 181.428 213.703 1.00 59.37  ? 790  HIS A CE1 1 
ATOM 1431 N NE2 . HIS A 1 779  ? 209.644 182.701 213.983 1.00 61.07  ? 790  HIS A NE2 1 
ATOM 1432 N N   . ASP A 1 780  ? 206.733 183.744 210.769 1.00 56.33  ? 791  ASP A N   1 
ATOM 1433 C CA  . ASP A 1 780  ? 205.846 184.792 211.263 1.00 57.04  ? 791  ASP A CA  1 
ATOM 1434 C C   . ASP A 1 780  ? 205.859 184.776 212.784 1.00 61.18  ? 791  ASP A C   1 
ATOM 1435 O O   . ASP A 1 780  ? 205.659 183.723 213.397 1.00 61.69  ? 791  ASP A O   1 
ATOM 1436 C CB  . ASP A 1 780  ? 204.419 184.583 210.743 1.00 55.12  ? 791  ASP A CB  1 
ATOM 1437 C CG  . ASP A 1 780  ? 203.673 185.883 210.519 1.00 64.06  ? 791  ASP A CG  1 
ATOM 1438 O OD1 . ASP A 1 780  ? 202.455 185.916 210.800 1.00 65.61  ? 791  ASP A OD1 1 
ATOM 1439 O OD2 . ASP A 1 780  ? 204.296 186.873 210.093 1.00 69.04  ? 791  ASP A OD2 1 
ATOM 1440 N N   . TYR A 1 781  ? 206.112 185.933 213.391 1.00 61.23  ? 792  TYR A N   1 
ATOM 1441 C CA  . TYR A 1 781  ? 205.885 186.145 214.815 1.00 56.89  ? 792  TYR A CA  1 
ATOM 1442 C C   . TYR A 1 781  ? 204.756 187.156 214.945 1.00 60.20  ? 792  TYR A C   1 
ATOM 1443 O O   . TYR A 1 781  ? 204.854 188.270 214.416 1.00 61.15  ? 792  TYR A O   1 
ATOM 1444 C CB  . TYR A 1 781  ? 207.148 186.643 215.518 1.00 61.17  ? 792  TYR A CB  1 
ATOM 1445 C CG  . TYR A 1 781  ? 206.907 187.194 216.911 1.00 69.97  ? 792  TYR A CG  1 
ATOM 1446 C CD1 . TYR A 1 781  ? 206.785 186.341 218.001 1.00 70.48  ? 792  TYR A CD1 1 
ATOM 1447 C CD2 . TYR A 1 781  ? 206.810 188.562 217.138 1.00 69.51  ? 792  TYR A CD2 1 
ATOM 1448 C CE1 . TYR A 1 781  ? 206.569 186.832 219.277 1.00 67.66  ? 792  TYR A CE1 1 
ATOM 1449 C CE2 . TYR A 1 781  ? 206.592 189.063 218.413 1.00 66.78  ? 792  TYR A CE2 1 
ATOM 1450 C CZ  . TYR A 1 781  ? 206.473 188.193 219.477 1.00 70.01  ? 792  TYR A CZ  1 
ATOM 1451 O OH  . TYR A 1 781  ? 206.258 188.683 220.745 1.00 76.57  ? 792  TYR A OH  1 
ATOM 1452 N N   . TRP A 1 782  ? 203.685 186.774 215.637 1.00 60.14  ? 793  TRP A N   1 
ATOM 1453 C CA  . TRP A 1 782  ? 202.522 187.643 215.682 1.00 58.39  ? 793  TRP A CA  1 
ATOM 1454 C C   . TRP A 1 782  ? 201.867 187.562 217.052 1.00 61.42  ? 793  TRP A C   1 
ATOM 1455 O O   . TRP A 1 782  ? 202.162 186.677 217.859 1.00 63.37  ? 793  TRP A O   1 
ATOM 1456 C CB  . TRP A 1 782  ? 201.521 187.300 214.570 1.00 57.18  ? 793  TRP A CB  1 
ATOM 1457 C CG  . TRP A 1 782  ? 201.077 185.872 214.523 1.00 58.15  ? 793  TRP A CG  1 
ATOM 1458 C CD1 . TRP A 1 782  ? 201.783 184.806 214.048 1.00 60.09  ? 793  TRP A CD1 1 
ATOM 1459 C CD2 . TRP A 1 782  ? 199.800 185.363 214.918 1.00 59.08  ? 793  TRP A CD2 1 
ATOM 1460 N NE1 . TRP A 1 782  ? 201.034 183.659 214.150 1.00 58.96  ? 793  TRP A NE1 1 
ATOM 1461 C CE2 . TRP A 1 782  ? 199.810 183.976 214.678 1.00 56.15  ? 793  TRP A CE2 1 
ATOM 1462 C CE3 . TRP A 1 782  ? 198.651 185.945 215.464 1.00 62.22  ? 793  TRP A CE3 1 
ATOM 1463 C CZ2 . TRP A 1 782  ? 198.718 183.161 214.966 1.00 53.56  ? 793  TRP A CZ2 1 
ATOM 1464 C CZ3 . TRP A 1 782  ? 197.570 185.135 215.747 1.00 56.01  ? 793  TRP A CZ3 1 
ATOM 1465 C CH2 . TRP A 1 782  ? 197.610 183.760 215.497 1.00 51.07  ? 793  TRP A CH2 1 
ATOM 1466 N N   . GLY A 1 783  ? 201.006 188.533 217.320 1.00 61.14  ? 794  GLY A N   1 
ATOM 1467 C CA  . GLY A 1 783  ? 200.267 188.533 218.566 1.00 61.51  ? 794  GLY A CA  1 
ATOM 1468 C C   . GLY A 1 783  ? 199.760 189.914 218.913 1.00 66.17  ? 794  GLY A C   1 
ATOM 1469 O O   . GLY A 1 783  ? 199.922 190.878 218.158 1.00 69.20  ? 794  GLY A O   1 
ATOM 1470 N N   . SER A 1 784  ? 199.138 189.987 220.088 1.00 66.27  ? 795  SER A N   1 
ATOM 1471 C CA  . SER A 1 784  ? 198.590 191.234 220.600 1.00 67.80  ? 795  SER A CA  1 
ATOM 1472 C C   . SER A 1 784  ? 198.549 191.158 222.119 1.00 65.15  ? 795  SER A C   1 
ATOM 1473 O O   . SER A 1 784  ? 198.640 190.078 222.708 1.00 61.60  ? 795  SER A O   1 
ATOM 1474 C CB  . SER A 1 784  ? 197.193 191.511 220.035 1.00 70.85  ? 795  SER A CB  1 
ATOM 1475 O OG  . SER A 1 784  ? 196.293 190.467 220.362 1.00 71.06  ? 795  SER A OG  1 
ATOM 1476 N N   . SER A 1 785  ? 198.411 192.325 222.743 1.00 68.15  ? 796  SER A N   1 
ATOM 1477 C CA  . SER A 1 785  ? 198.362 192.402 224.193 1.00 66.65  ? 796  SER A CA  1 
ATOM 1478 C C   . SER A 1 785  ? 197.032 191.866 224.719 1.00 62.20  ? 796  SER A C   1 
ATOM 1479 O O   . SER A 1 785  ? 196.043 191.747 223.990 1.00 63.19  ? 796  SER A O   1 
ATOM 1480 C CB  . SER A 1 785  ? 198.568 193.843 224.660 1.00 68.68  ? 796  SER A CB  1 
ATOM 1481 O OG  . SER A 1 785  ? 197.558 194.694 224.147 1.00 65.14  ? 796  SER A OG  1 
ATOM 1482 N N   . GLY A 1 786  ? 197.021 191.539 226.009 1.00 53.70  ? 797  GLY A N   1 
ATOM 1483 C CA  . GLY A 1 786  ? 195.827 191.019 226.645 1.00 49.91  ? 797  GLY A CA  1 
ATOM 1484 C C   . GLY A 1 786  ? 196.043 190.621 228.090 1.00 45.57  ? 797  GLY A C   1 
ATOM 1485 O O   . GLY A 1 786  ? 196.934 191.148 228.761 1.00 47.32  ? 797  GLY A O   1 
ATOM 1486 N N   . THR A 1 787  ? 195.231 189.689 228.579 1.00 44.87  ? 798  THR A N   1 
ATOM 1487 C CA  . THR A 1 787  ? 195.320 189.193 229.945 1.00 44.52  ? 798  THR A CA  1 
ATOM 1488 C C   . THR A 1 787  ? 196.026 187.845 229.939 1.00 41.59  ? 798  THR A C   1 
ATOM 1489 O O   . THR A 1 787  ? 195.702 186.975 229.125 1.00 44.40  ? 798  THR A O   1 
ATOM 1490 C CB  . THR A 1 787  ? 193.931 189.062 230.574 1.00 43.42  ? 798  THR A CB  1 
ATOM 1491 O OG1 . THR A 1 787  ? 193.324 190.357 230.672 1.00 49.63  ? 798  THR A OG1 1 
ATOM 1492 C CG2 . THR A 1 787  ? 194.025 188.448 231.963 1.00 38.22  ? 798  THR A CG2 1 
ATOM 1493 N N   . GLY A 1 788  ? 196.998 187.685 230.834 1.00 39.29  ? 799  GLY A N   1 
ATOM 1494 C CA  . GLY A 1 788  ? 197.740 186.438 230.887 1.00 42.67  ? 799  GLY A CA  1 
ATOM 1495 C C   . GLY A 1 788  ? 196.834 185.261 231.201 1.00 39.09  ? 799  GLY A C   1 
ATOM 1496 O O   . GLY A 1 788  ? 196.018 185.306 232.124 1.00 38.72  ? 799  GLY A O   1 
ATOM 1497 N N   . GLY A 1 789  ? 196.985 184.195 230.419 1.00 38.93  ? 800  GLY A N   1 
ATOM 1498 C CA  . GLY A 1 789  ? 196.234 182.977 230.602 1.00 37.89  ? 800  GLY A CA  1 
ATOM 1499 C C   . GLY A 1 789  ? 195.283 182.638 229.473 1.00 39.72  ? 800  GLY A C   1 
ATOM 1500 O O   . GLY A 1 789  ? 195.151 181.457 229.132 1.00 43.15  ? 800  GLY A O   1 
ATOM 1501 N N   . TYR A 1 790  ? 194.603 183.631 228.898 1.00 34.99  ? 801  TYR A N   1 
ATOM 1502 C CA  . TYR A 1 790  ? 193.672 183.351 227.812 1.00 32.00  ? 801  TYR A CA  1 
ATOM 1503 C C   . TYR A 1 790  ? 193.799 184.329 226.648 1.00 33.90  ? 801  TYR A C   1 
ATOM 1504 O O   . TYR A 1 790  ? 193.378 184.015 225.531 1.00 40.33  ? 801  TYR A O   1 
ATOM 1505 C CB  . TYR A 1 790  ? 192.235 183.335 228.343 1.00 31.78  ? 801  TYR A CB  1 
ATOM 1506 C CG  . TYR A 1 790  ? 191.809 184.598 229.055 1.00 31.04  ? 801  TYR A CG  1 
ATOM 1507 C CD1 . TYR A 1 790  ? 191.895 184.700 230.437 1.00 34.27  ? 801  TYR A CD1 1 
ATOM 1508 C CD2 . TYR A 1 790  ? 191.302 185.680 228.349 1.00 34.13  ? 801  TYR A CD2 1 
ATOM 1509 C CE1 . TYR A 1 790  ? 191.502 185.849 231.094 1.00 37.57  ? 801  TYR A CE1 1 
ATOM 1510 C CE2 . TYR A 1 790  ? 190.906 186.833 228.998 1.00 35.73  ? 801  TYR A CE2 1 
ATOM 1511 C CZ  . TYR A 1 790  ? 191.008 186.912 230.369 1.00 38.07  ? 801  TYR A CZ  1 
ATOM 1512 O OH  . TYR A 1 790  ? 190.615 188.058 231.019 1.00 49.00  ? 801  TYR A OH  1 
ATOM 1513 N N   . SER A 1 791  ? 194.371 185.513 226.884 1.00 34.72  ? 802  SER A N   1 
ATOM 1514 C CA  . SER A 1 791  ? 194.405 186.533 225.844 1.00 38.15  ? 802  SER A CA  1 
ATOM 1515 C C   . SER A 1 791  ? 195.760 187.199 225.639 1.00 43.50  ? 802  SER A C   1 
ATOM 1516 O O   . SER A 1 791  ? 195.889 188.000 224.707 1.00 45.48  ? 802  SER A O   1 
ATOM 1517 C CB  . SER A 1 791  ? 193.353 187.619 226.130 1.00 41.28  ? 802  SER A CB  1 
ATOM 1518 O OG  . SER A 1 791  ? 193.691 188.367 227.283 1.00 46.01  ? 802  SER A OG  1 
ATOM 1519 N N   . ASP A 1 792  ? 196.768 186.907 226.461 1.00 46.05  ? 803  ASP A N   1 
ATOM 1520 C CA  . ASP A 1 792  ? 198.106 187.467 226.266 1.00 48.88  ? 803  ASP A CA  1 
ATOM 1521 C C   . ASP A 1 792  ? 198.846 186.676 225.184 1.00 49.23  ? 803  ASP A C   1 
ATOM 1522 O O   . ASP A 1 792  ? 199.788 185.927 225.440 1.00 49.89  ? 803  ASP A O   1 
ATOM 1523 C CB  . ASP A 1 792  ? 198.875 187.474 227.581 1.00 46.22  ? 803  ASP A CB  1 
ATOM 1524 C CG  . ASP A 1 792  ? 200.126 188.328 227.520 1.00 54.81  ? 803  ASP A CG  1 
ATOM 1525 O OD1 . ASP A 1 792  ? 200.212 189.197 226.627 1.00 55.96  ? 803  ASP A OD1 1 
ATOM 1526 O OD2 . ASP A 1 792  ? 201.024 188.130 228.365 1.00 64.67  ? 803  ASP A OD2 1 
ATOM 1527 N N   . LEU A 1 793  ? 198.401 186.874 223.946 1.00 49.38  ? 804  LEU A N   1 
ATOM 1528 C CA  . LEU A 1 793  ? 198.764 185.973 222.861 1.00 46.91  ? 804  LEU A CA  1 
ATOM 1529 C C   . LEU A 1 793  ? 200.126 186.314 222.268 1.00 46.87  ? 804  LEU A C   1 
ATOM 1530 O O   . LEU A 1 793  ? 200.407 187.471 221.942 1.00 49.82  ? 804  LEU A O   1 
ATOM 1531 C CB  . LEU A 1 793  ? 197.698 186.014 221.769 1.00 45.10  ? 804  LEU A CB  1 
ATOM 1532 C CG  . LEU A 1 793  ? 197.922 185.041 220.612 1.00 41.55  ? 804  LEU A CG  1 
ATOM 1533 C CD1 . LEU A 1 793  ? 197.780 183.613 221.104 1.00 40.14  ? 804  LEU A CD1 1 
ATOM 1534 C CD2 . LEU A 1 793  ? 196.956 185.322 219.474 1.00 46.62  ? 804  LEU A CD2 1 
ATOM 1535 N N   . LYS A 1 794  ? 200.969 185.292 222.134 1.00 47.98  ? 805  LYS A N   1 
ATOM 1536 C CA  . LYS A 1 794  ? 202.183 185.340 221.330 1.00 51.68  ? 805  LYS A CA  1 
ATOM 1537 C C   . LYS A 1 794  ? 202.265 184.042 220.541 1.00 54.19  ? 805  LYS A C   1 
ATOM 1538 O O   . LYS A 1 794  ? 202.186 182.955 221.124 1.00 58.05  ? 805  LYS A O   1 
ATOM 1539 C CB  . LYS A 1 794  ? 203.432 185.521 222.200 1.00 50.82  ? 805  LYS A CB  1 
ATOM 1540 C CG  . LYS A 1 794  ? 203.514 186.863 222.906 1.00 53.27  ? 805  LYS A CG  1 
ATOM 1541 C CD  . LYS A 1 794  ? 204.856 187.038 223.598 1.00 57.64  ? 805  LYS A CD  1 
ATOM 1542 C CE  . LYS A 1 794  ? 205.078 185.963 224.649 1.00 60.64  ? 805  LYS A CE  1 
ATOM 1543 N NZ  . LYS A 1 794  ? 204.167 186.131 225.814 1.00 57.95  ? 805  LYS A NZ  1 
ATOM 1544 N N   . ALA A 1 795  ? 202.424 184.146 219.224 1.00 50.65  ? 806  ALA A N   1 
ATOM 1545 C CA  . ALA A 1 795  ? 202.387 182.969 218.373 1.00 53.45  ? 806  ALA A CA  1 
ATOM 1546 C C   . ALA A 1 795  ? 203.501 183.027 217.340 1.00 63.86  ? 806  ALA A C   1 
ATOM 1547 O O   . ALA A 1 795  ? 203.866 184.097 216.842 1.00 66.23  ? 806  ALA A O   1 
ATOM 1548 C CB  . ALA A 1 795  ? 201.030 182.827 217.673 1.00 50.35  ? 806  ALA A CB  1 
ATOM 1549 N N   . HIS A 1 796  ? 204.028 181.847 217.026 1.00 60.68  ? 807  HIS A N   1 
ATOM 1550 C CA  . HIS A 1 796  ? 205.021 181.653 215.981 1.00 54.66  ? 807  HIS A CA  1 
ATOM 1551 C C   . HIS A 1 796  ? 204.437 180.739 214.915 1.00 56.85  ? 807  HIS A C   1 
ATOM 1552 O O   . HIS A 1 796  ? 203.654 179.836 215.225 1.00 59.28  ? 807  HIS A O   1 
ATOM 1553 C CB  . HIS A 1 796  ? 206.311 181.040 216.536 1.00 56.30  ? 807  HIS A CB  1 
ATOM 1554 C CG  . HIS A 1 796  ? 206.888 181.785 217.698 1.00 67.43  ? 807  HIS A CG  1 
ATOM 1555 N ND1 . HIS A 1 796  ? 207.716 182.875 217.547 1.00 74.00  ? 807  HIS A ND1 1 
ATOM 1556 C CD2 . HIS A 1 796  ? 206.763 181.589 219.032 1.00 70.83  ? 807  HIS A CD2 1 
ATOM 1557 C CE1 . HIS A 1 796  ? 208.074 183.322 218.738 1.00 75.70  ? 807  HIS A CE1 1 
ATOM 1558 N NE2 . HIS A 1 796  ? 207.509 182.560 219.656 1.00 76.79  ? 807  HIS A NE2 1 
ATOM 1559 N N   . THR A 1 797  ? 204.817 180.972 213.662 1.00 57.27  ? 808  THR A N   1 
ATOM 1560 C CA  . THR A 1 797  ? 204.283 180.188 212.554 1.00 52.87  ? 808  THR A CA  1 
ATOM 1561 C C   . THR A 1 797  ? 205.355 180.027 211.488 1.00 53.83  ? 808  THR A C   1 
ATOM 1562 O O   . THR A 1 797  ? 205.798 181.015 210.896 1.00 56.49  ? 808  THR A O   1 
ATOM 1563 C CB  . THR A 1 797  ? 203.034 180.850 211.966 1.00 48.06  ? 808  THR A CB  1 
ATOM 1564 O OG1 . THR A 1 797  ? 202.029 180.963 212.981 1.00 51.30  ? 808  THR A OG1 1 
ATOM 1565 C CG2 . THR A 1 797  ? 202.484 180.019 210.823 1.00 52.56  ? 808  THR A CG2 1 
ATOM 1566 N N   . THR A 1 798  ? 205.764 178.786 211.244 1.00 47.93  ? 809  THR A N   1 
ATOM 1567 C CA  . THR A 1 798  ? 206.689 178.453 210.170 1.00 46.51  ? 809  THR A CA  1 
ATOM 1568 C C   . THR A 1 798  ? 205.901 177.852 209.014 1.00 53.60  ? 809  THR A C   1 
ATOM 1569 O O   . THR A 1 798  ? 205.172 176.871 209.198 1.00 59.34  ? 809  THR A O   1 
ATOM 1570 C CB  . THR A 1 798  ? 207.763 177.473 210.647 1.00 51.86  ? 809  THR A CB  1 
ATOM 1571 O OG1 . THR A 1 798  ? 208.621 178.121 211.596 1.00 57.65  ? 809  THR A OG1 1 
ATOM 1572 C CG2 . THR A 1 798  ? 208.594 176.979 209.473 1.00 57.28  ? 809  THR A CG2 1 
ATOM 1573 N N   . MET A 1 799  ? 206.039 178.447 207.831 1.00 51.69  ? 810  MET A N   1 
ATOM 1574 C CA  . MET A 1 799  ? 205.243 178.085 206.667 1.00 50.42  ? 810  MET A CA  1 
ATOM 1575 C C   . MET A 1 799  ? 206.150 177.684 205.514 1.00 52.11  ? 810  MET A C   1 
ATOM 1576 O O   . MET A 1 799  ? 207.053 178.440 205.135 1.00 56.44  ? 810  MET A O   1 
ATOM 1577 C CB  . MET A 1 799  ? 204.339 179.254 206.255 1.00 48.83  ? 810  MET A CB  1 
ATOM 1578 C CG  . MET A 1 799  ? 203.637 179.917 207.433 1.00 53.85  ? 810  MET A CG  1 
ATOM 1579 S SD  . MET A 1 799  ? 202.950 181.541 207.084 1.00 55.12  ? 810  MET A SD  1 
ATOM 1580 C CE  . MET A 1 799  ? 204.303 182.584 207.615 1.00 57.34  ? 810  MET A CE  1 
ATOM 1581 N N   . LEU A 1 800  ? 205.903 176.500 204.959 1.00 51.15  ? 811  LEU A N   1 
ATOM 1582 C CA  . LEU A 1 800  ? 206.646 175.982 203.819 1.00 48.67  ? 811  LEU A CA  1 
ATOM 1583 C C   . LEU A 1 800  ? 205.684 175.760 202.659 1.00 48.27  ? 811  LEU A C   1 
ATOM 1584 O O   . LEU A 1 800  ? 204.656 175.093 202.820 1.00 46.76  ? 811  LEU A O   1 
ATOM 1585 C CB  . LEU A 1 800  ? 207.356 174.676 204.178 1.00 41.93  ? 811  LEU A CB  1 
ATOM 1586 C CG  . LEU A 1 800  ? 208.009 173.898 203.037 1.00 44.17  ? 811  LEU A CG  1 
ATOM 1587 C CD1 . LEU A 1 800  ? 209.136 174.709 202.420 1.00 49.80  ? 811  LEU A CD1 1 
ATOM 1588 C CD2 . LEU A 1 800  ? 208.519 172.550 203.522 1.00 44.46  ? 811  LEU A CD2 1 
ATOM 1589 N N   . GLN A 1 801  ? 206.015 176.310 201.492 1.00 47.97  ? 812  GLN A N   1 
ATOM 1590 C CA  . GLN A 1 801  ? 205.133 176.244 200.336 1.00 44.83  ? 812  GLN A CA  1 
ATOM 1591 C C   . GLN A 1 801  ? 205.910 175.812 199.103 1.00 45.84  ? 812  GLN A C   1 
ATOM 1592 O O   . GLN A 1 801  ? 207.033 176.269 198.869 1.00 51.01  ? 812  GLN A O   1 
ATOM 1593 C CB  . GLN A 1 801  ? 204.455 177.597 200.081 1.00 45.76  ? 812  GLN A CB  1 
ATOM 1594 C CG  . GLN A 1 801  ? 203.512 177.603 198.888 1.00 45.57  ? 812  GLN A CG  1 
ATOM 1595 C CD  . GLN A 1 801  ? 202.436 178.663 199.004 1.00 50.27  ? 812  GLN A CD  1 
ATOM 1596 O OE1 . GLN A 1 801  ? 202.149 179.157 200.094 1.00 59.41  ? 812  GLN A OE1 1 
ATOM 1597 N NE2 . GLN A 1 801  ? 201.826 179.013 197.877 1.00 46.92  ? 812  GLN A NE2 1 
ATOM 1598 N N   . VAL A 1 802  ? 205.304 174.923 198.321 1.00 42.11  ? 813  VAL A N   1 
ATOM 1599 C CA  . VAL A 1 802  ? 205.847 174.473 197.045 1.00 37.31  ? 813  VAL A CA  1 
ATOM 1600 C C   . VAL A 1 802  ? 204.828 174.808 195.965 1.00 42.57  ? 813  VAL A C   1 
ATOM 1601 O O   . VAL A 1 802  ? 203.662 174.397 196.055 1.00 48.93  ? 813  VAL A O   1 
ATOM 1602 C CB  . VAL A 1 802  ? 206.166 172.970 197.052 1.00 35.38  ? 813  VAL A CB  1 
ATOM 1603 C CG1 . VAL A 1 802  ? 206.760 172.550 195.719 1.00 34.90  ? 813  VAL A CG1 1 
ATOM 1604 C CG2 . VAL A 1 802  ? 207.115 172.636 198.192 1.00 39.52  ? 813  VAL A CG2 1 
ATOM 1605 N N   . ASP A 1 803  ? 205.267 175.554 194.953 1.00 41.65  ? 814  ASP A N   1 
ATOM 1606 C CA  . ASP A 1 803  ? 204.439 175.978 193.832 1.00 45.84  ? 814  ASP A CA  1 
ATOM 1607 C C   . ASP A 1 803  ? 204.955 175.335 192.554 1.00 50.13  ? 814  ASP A C   1 
ATOM 1608 O O   . ASP A 1 803  ? 206.124 175.519 192.193 1.00 56.15  ? 814  ASP A O   1 
ATOM 1609 C CB  . ASP A 1 803  ? 204.456 177.502 193.690 1.00 49.65  ? 814  ASP A CB  1 
ATOM 1610 C CG  . ASP A 1 803  ? 203.699 178.201 194.795 1.00 60.00  ? 814  ASP A CG  1 
ATOM 1611 O OD1 . ASP A 1 803  ? 202.929 177.525 195.504 1.00 63.39  ? 814  ASP A OD1 1 
ATOM 1612 O OD2 . ASP A 1 803  ? 203.873 179.428 194.955 1.00 63.93  ? 814  ASP A OD2 1 
ATOM 1613 N N   . ALA A 1 804  ? 204.083 174.603 191.866 1.00 48.93  ? 815  ALA A N   1 
ATOM 1614 C CA  . ALA A 1 804  ? 204.440 173.896 190.646 1.00 47.62  ? 815  ALA A CA  1 
ATOM 1615 C C   . ALA A 1 804  ? 203.414 174.201 189.565 1.00 53.72  ? 815  ALA A C   1 
ATOM 1616 O O   . ALA A 1 804  ? 202.271 174.552 189.875 1.00 57.36  ? 815  ALA A O   1 
ATOM 1617 C CB  . ALA A 1 804  ? 204.516 172.378 190.875 1.00 45.01  ? 815  ALA A CB  1 
ATOM 1618 N N   . PRO A 1 805  ? 203.800 174.109 188.294 1.00 54.08  ? 816  PRO A N   1 
ATOM 1619 C CA  . PRO A 1 805  ? 202.822 174.313 187.217 1.00 49.19  ? 816  PRO A CA  1 
ATOM 1620 C C   . PRO A 1 805  ? 201.963 173.076 187.005 1.00 49.62  ? 816  PRO A C   1 
ATOM 1621 O O   . PRO A 1 805  ? 202.387 171.949 187.273 1.00 54.07  ? 816  PRO A O   1 
ATOM 1622 C CB  . PRO A 1 805  ? 203.696 174.602 185.988 1.00 54.81  ? 816  PRO A CB  1 
ATOM 1623 C CG  . PRO A 1 805  ? 205.086 174.832 186.522 1.00 55.47  ? 816  PRO A CG  1 
ATOM 1624 C CD  . PRO A 1 805  ? 205.173 174.031 187.776 1.00 56.03  ? 816  PRO A CD  1 
ATOM 1625 N N   . TYR A 1 806  ? 200.744 173.298 186.517 1.00 49.78  ? 817  TYR A N   1 
ATOM 1626 C CA  . TYR A 1 806  ? 199.827 172.215 186.177 1.00 52.59  ? 817  TYR A CA  1 
ATOM 1627 C C   . TYR A 1 806  ? 198.767 172.784 185.250 1.00 55.97  ? 817  TYR A C   1 
ATOM 1628 O O   . TYR A 1 806  ? 198.040 173.704 185.640 1.00 56.03  ? 817  TYR A O   1 
ATOM 1629 C CB  . TYR A 1 806  ? 199.185 171.609 187.426 1.00 53.22  ? 817  TYR A CB  1 
ATOM 1630 C CG  . TYR A 1 806  ? 198.298 170.418 187.141 1.00 56.70  ? 817  TYR A CG  1 
ATOM 1631 C CD1 . TYR A 1 806  ? 198.831 169.141 187.032 1.00 57.93  ? 817  TYR A CD1 1 
ATOM 1632 C CD2 . TYR A 1 806  ? 196.926 170.571 186.982 1.00 57.23  ? 817  TYR A CD2 1 
ATOM 1633 C CE1 . TYR A 1 806  ? 198.024 168.050 186.773 1.00 59.57  ? 817  TYR A CE1 1 
ATOM 1634 C CE2 . TYR A 1 806  ? 196.112 169.486 186.722 1.00 61.48  ? 817  TYR A CE2 1 
ATOM 1635 C CZ  . TYR A 1 806  ? 196.665 168.228 186.618 1.00 65.06  ? 817  TYR A CZ  1 
ATOM 1636 O OH  . TYR A 1 806  ? 195.858 167.144 186.359 1.00 67.85  ? 817  TYR A OH  1 
ATOM 1637 N N   . SER A 1 807  ? 198.680 172.240 184.043 1.00 58.15  ? 818  SER A N   1 
ATOM 1638 C CA  . SER A 1 807  ? 197.792 172.768 183.005 1.00 57.45  ? 818  SER A CA  1 
ATOM 1639 C C   . SER A 1 807  ? 198.131 174.248 182.818 1.00 60.15  ? 818  SER A C   1 
ATOM 1640 O O   . SER A 1 807  ? 199.301 174.639 182.865 1.00 62.20  ? 818  SER A O   1 
ATOM 1641 C CB  . SER A 1 807  ? 196.342 172.483 183.364 1.00 55.78  ? 818  SER A CB  1 
ATOM 1642 O OG  . SER A 1 807  ? 195.495 172.651 182.240 1.00 57.90  ? 818  SER A OG  1 
ATOM 1643 N N   . ASP A 1 808  ? 197.119 175.088 182.604 1.00 57.98  ? 819  ASP A N   1 
ATOM 1644 C CA  . ASP A 1 808  ? 197.354 176.522 182.513 1.00 57.72  ? 819  ASP A CA  1 
ATOM 1645 C C   . ASP A 1 808  ? 197.528 177.180 183.876 1.00 58.01  ? 819  ASP A C   1 
ATOM 1646 O O   . ASP A 1 808  ? 197.856 178.369 183.930 1.00 59.83  ? 819  ASP A O   1 
ATOM 1647 C CB  . ASP A 1 808  ? 196.209 177.195 181.753 1.00 61.54  ? 819  ASP A CB  1 
ATOM 1648 C CG  . ASP A 1 808  ? 194.846 176.819 182.301 1.00 69.02  ? 819  ASP A CG  1 
ATOM 1649 O OD1 . ASP A 1 808  ? 193.992 177.719 182.442 1.00 76.09  ? 819  ASP A OD1 1 
ATOM 1650 O OD2 . ASP A 1 808  ? 194.629 175.623 182.586 1.00 70.00  ? 819  ASP A OD2 1 
ATOM 1651 N N   . GLY A 1 809  ? 197.320 176.445 184.970 1.00 56.91  ? 820  GLY A N   1 
ATOM 1652 C CA  . GLY A 1 809  ? 197.381 176.998 186.301 1.00 54.13  ? 820  GLY A CA  1 
ATOM 1653 C C   . GLY A 1 809  ? 198.580 176.518 187.100 1.00 52.14  ? 820  GLY A C   1 
ATOM 1654 O O   . GLY A 1 809  ? 199.527 175.925 186.579 1.00 57.06  ? 820  GLY A O   1 
ATOM 1655 N N   . ARG A 1 810  ? 198.518 176.782 188.403 1.00 47.51  ? 821  ARG A N   1 
ATOM 1656 C CA  . ARG A 1 810  ? 199.578 176.422 189.334 1.00 49.32  ? 821  ARG A CA  1 
ATOM 1657 C C   . ARG A 1 810  ? 198.979 175.711 190.537 1.00 47.13  ? 821  ARG A C   1 
ATOM 1658 O O   . ARG A 1 810  ? 197.966 176.156 191.086 1.00 53.49  ? 821  ARG A O   1 
ATOM 1659 C CB  . ARG A 1 810  ? 200.358 177.659 189.791 1.00 50.46  ? 821  ARG A CB  1 
ATOM 1660 C CG  . ARG A 1 810  ? 201.091 178.383 188.678 1.00 51.32  ? 821  ARG A CG  1 
ATOM 1661 C CD  . ARG A 1 810  ? 201.879 179.565 189.221 1.00 54.54  ? 821  ARG A CD  1 
ATOM 1662 N NE  . ARG A 1 810  ? 202.991 179.145 190.065 1.00 48.73  ? 821  ARG A NE  1 
ATOM 1663 C CZ  . ARG A 1 810  ? 204.094 178.555 189.622 1.00 53.12  ? 821  ARG A CZ  1 
ATOM 1664 N NH1 . ARG A 1 810  ? 204.277 178.307 188.335 1.00 60.66  ? 821  ARG A NH1 1 
ATOM 1665 N NH2 . ARG A 1 810  ? 205.038 178.207 190.492 1.00 52.58  ? 821  ARG A NH2 1 
ATOM 1666 N N   . MET A 1 811  ? 199.609 174.615 190.942 1.00 40.29  ? 822  MET A N   1 
ATOM 1667 C CA  . MET A 1 811  ? 199.229 173.897 192.146 1.00 40.64  ? 822  MET A CA  1 
ATOM 1668 C C   . MET A 1 811  ? 200.215 174.201 193.267 1.00 43.63  ? 822  MET A C   1 
ATOM 1669 O O   . MET A 1 811  ? 201.396 174.478 193.030 1.00 49.83  ? 822  MET A O   1 
ATOM 1670 C CB  . MET A 1 811  ? 199.172 172.392 191.881 1.00 42.86  ? 822  MET A CB  1 
ATOM 1671 C CG  . MET A 1 811  ? 200.400 171.839 191.183 1.00 47.07  ? 822  MET A CG  1 
ATOM 1672 S SD  . MET A 1 811  ? 200.456 170.038 191.193 1.00 68.81  ? 822  MET A SD  1 
ATOM 1673 C CE  . MET A 1 811  ? 201.840 169.741 190.097 1.00 55.63  ? 822  MET A CE  1 
ATOM 1674 N N   . PHE A 1 812  ? 199.713 174.163 194.499 1.00 43.08  ? 823  PHE A N   1 
ATOM 1675 C CA  . PHE A 1 812  ? 200.523 174.492 195.661 1.00 41.76  ? 823  PHE A CA  1 
ATOM 1676 C C   . PHE A 1 812  ? 200.292 173.476 196.768 1.00 40.15  ? 823  PHE A C   1 
ATOM 1677 O O   . PHE A 1 812  ? 199.165 173.028 197.011 1.00 47.05  ? 823  PHE A O   1 
ATOM 1678 C CB  . PHE A 1 812  ? 200.237 175.919 196.174 1.00 44.52  ? 823  PHE A CB  1 
ATOM 1679 C CG  . PHE A 1 812  ? 198.951 176.060 196.943 1.00 45.28  ? 823  PHE A CG  1 
ATOM 1680 C CD1 . PHE A 1 812  ? 198.912 175.845 198.314 1.00 43.99  ? 823  PHE A CD1 1 
ATOM 1681 C CD2 . PHE A 1 812  ? 197.784 176.428 196.298 1.00 45.14  ? 823  PHE A CD2 1 
ATOM 1682 C CE1 . PHE A 1 812  ? 197.732 175.978 199.017 1.00 41.02  ? 823  PHE A CE1 1 
ATOM 1683 C CE2 . PHE A 1 812  ? 196.603 176.568 196.998 1.00 41.65  ? 823  PHE A CE2 1 
ATOM 1684 C CZ  . PHE A 1 812  ? 196.576 176.338 198.357 1.00 41.59  ? 823  PHE A CZ  1 
ATOM 1685 N N   . PHE A 1 813  ? 201.391 173.120 197.429 1.00 35.02  ? 824  PHE A N   1 
ATOM 1686 C CA  . PHE A 1 813  ? 201.383 172.332 198.653 1.00 39.47  ? 824  PHE A CA  1 
ATOM 1687 C C   . PHE A 1 813  ? 201.935 173.184 199.787 1.00 45.53  ? 824  PHE A C   1 
ATOM 1688 O O   . PHE A 1 813  ? 202.989 173.811 199.644 1.00 51.46  ? 824  PHE A O   1 
ATOM 1689 C CB  . PHE A 1 813  ? 202.218 171.057 198.496 1.00 43.29  ? 824  PHE A CB  1 
ATOM 1690 C CG  . PHE A 1 813  ? 202.525 170.366 199.796 1.00 50.46  ? 824  PHE A CG  1 
ATOM 1691 C CD1 . PHE A 1 813  ? 201.573 169.575 200.418 1.00 54.49  ? 824  PHE A CD1 1 
ATOM 1692 C CD2 . PHE A 1 813  ? 203.768 170.503 200.393 1.00 46.29  ? 824  PHE A CD2 1 
ATOM 1693 C CE1 . PHE A 1 813  ? 201.854 168.936 201.612 1.00 54.19  ? 824  PHE A CE1 1 
ATOM 1694 C CE2 . PHE A 1 813  ? 204.054 169.868 201.588 1.00 49.08  ? 824  PHE A CE2 1 
ATOM 1695 C CZ  . PHE A 1 813  ? 203.096 169.083 202.197 1.00 54.24  ? 824  PHE A CZ  1 
ATOM 1696 N N   . ARG A 1 814  ? 201.229 173.205 200.915 1.00 44.25  ? 825  ARG A N   1 
ATOM 1697 C CA  . ARG A 1 814  ? 201.557 174.105 202.009 1.00 44.77  ? 825  ARG A CA  1 
ATOM 1698 C C   . ARG A 1 814  ? 201.553 173.343 203.326 1.00 49.33  ? 825  ARG A C   1 
ATOM 1699 O O   . ARG A 1 814  ? 200.660 172.529 203.582 1.00 51.06  ? 825  ARG A O   1 
ATOM 1700 C CB  . ARG A 1 814  ? 200.562 175.274 202.067 1.00 44.77  ? 825  ARG A CB  1 
ATOM 1701 C CG  . ARG A 1 814  ? 200.669 176.145 203.305 1.00 46.37  ? 825  ARG A CG  1 
ATOM 1702 C CD  . ARG A 1 814  ? 201.910 177.018 203.249 1.00 50.04  ? 825  ARG A CD  1 
ATOM 1703 N NE  . ARG A 1 814  ? 201.631 178.319 202.653 1.00 54.52  ? 825  ARG A NE  1 
ATOM 1704 C CZ  . ARG A 1 814  ? 201.104 179.345 203.307 1.00 55.26  ? 825  ARG A CZ  1 
ATOM 1705 N NH1 . ARG A 1 814  ? 200.789 179.259 204.589 1.00 58.54  ? 825  ARG A NH1 1 
ATOM 1706 N NH2 . ARG A 1 814  ? 200.889 180.487 202.660 1.00 53.42  ? 825  ARG A NH2 1 
ATOM 1707 N N   . SER A 1 815  ? 202.556 173.620 204.157 1.00 47.60  ? 826  SER A N   1 
ATOM 1708 C CA  . SER A 1 815  ? 202.680 173.028 205.481 1.00 44.90  ? 826  SER A CA  1 
ATOM 1709 C C   . SER A 1 815  ? 202.925 174.135 206.493 1.00 50.40  ? 826  SER A C   1 
ATOM 1710 O O   . SER A 1 815  ? 203.791 174.992 206.289 1.00 54.51  ? 826  SER A O   1 
ATOM 1711 C CB  . SER A 1 815  ? 203.822 172.006 205.541 1.00 52.27  ? 826  SER A CB  1 
ATOM 1712 O OG  . SER A 1 815  ? 203.949 171.458 206.842 1.00 50.46  ? 826  SER A OG  1 
ATOM 1713 N N   . ASP A 1 816  ? 202.167 174.112 207.585 1.00 56.06  ? 827  ASP A N   1 
ATOM 1714 C CA  . ASP A 1 816  ? 202.206 175.170 208.582 1.00 53.52  ? 827  ASP A CA  1 
ATOM 1715 C C   . ASP A 1 816  ? 202.458 174.562 209.953 1.00 53.42  ? 827  ASP A C   1 
ATOM 1716 O O   . ASP A 1 816  ? 201.815 173.578 210.324 1.00 57.88  ? 827  ASP A O   1 
ATOM 1717 C CB  . ASP A 1 816  ? 200.893 175.953 208.595 1.00 55.78  ? 827  ASP A CB  1 
ATOM 1718 C CG  . ASP A 1 816  ? 200.771 176.897 207.426 1.00 59.61  ? 827  ASP A CG  1 
ATOM 1719 O OD1 . ASP A 1 816  ? 199.712 176.876 206.765 1.00 58.05  ? 827  ASP A OD1 1 
ATOM 1720 O OD2 . ASP A 1 816  ? 201.743 177.617 207.137 1.00 59.68  ? 827  ASP A OD2 1 
ATOM 1721 N N   . PHE A 1 817  ? 203.401 175.130 210.694 1.00 48.89  ? 828  PHE A N   1 
ATOM 1722 C CA  . PHE A 1 817  ? 203.617 174.766 212.087 1.00 54.88  ? 828  PHE A CA  1 
ATOM 1723 C C   . PHE A 1 817  ? 203.406 175.999 212.954 1.00 56.13  ? 828  PHE A C   1 
ATOM 1724 O O   . PHE A 1 817  ? 204.120 176.995 212.800 1.00 58.05  ? 828  PHE A O   1 
ATOM 1725 C CB  . PHE A 1 817  ? 205.019 174.192 212.292 1.00 56.42  ? 828  PHE A CB  1 
ATOM 1726 C CG  . PHE A 1 817  ? 205.253 173.641 213.669 1.00 58.50  ? 828  PHE A CG  1 
ATOM 1727 C CD1 . PHE A 1 817  ? 205.691 174.462 214.693 1.00 56.14  ? 828  PHE A CD1 1 
ATOM 1728 C CD2 . PHE A 1 817  ? 205.031 172.301 213.940 1.00 56.58  ? 828  PHE A CD2 1 
ATOM 1729 C CE1 . PHE A 1 817  ? 205.906 173.959 215.961 1.00 55.87  ? 828  PHE A CE1 1 
ATOM 1730 C CE2 . PHE A 1 817  ? 205.244 171.791 215.207 1.00 52.17  ? 828  PHE A CE2 1 
ATOM 1731 C CZ  . PHE A 1 817  ? 205.682 172.621 216.219 1.00 53.46  ? 828  PHE A CZ  1 
ATOM 1732 N N   . VAL A 1 818  ? 202.438 175.932 213.868 1.00 53.19  ? 829  VAL A N   1 
ATOM 1733 C CA  . VAL A 1 818  ? 202.022 177.093 214.645 1.00 52.99  ? 829  VAL A CA  1 
ATOM 1734 C C   . VAL A 1 818  ? 202.097 176.765 216.130 1.00 58.63  ? 829  VAL A C   1 
ATOM 1735 O O   . VAL A 1 818  ? 201.645 175.702 216.570 1.00 63.07  ? 829  VAL A O   1 
ATOM 1736 C CB  . VAL A 1 818  ? 200.602 177.561 214.250 1.00 52.90  ? 829  VAL A CB  1 
ATOM 1737 C CG1 . VAL A 1 818  ? 199.597 176.424 214.370 1.00 51.91  ? 829  VAL A CG1 1 
ATOM 1738 C CG2 . VAL A 1 818  ? 200.175 178.753 215.095 1.00 56.57  ? 829  VAL A CG2 1 
ATOM 1739 N N   . ASN A 1 819  ? 202.683 177.680 216.899 1.00 58.38  ? 830  ASN A N   1 
ATOM 1740 C CA  . ASN A 1 819  ? 202.781 177.568 218.350 1.00 54.46  ? 830  ASN A CA  1 
ATOM 1741 C C   . ASN A 1 819  ? 202.151 178.807 218.968 1.00 56.61  ? 830  ASN A C   1 
ATOM 1742 O O   . ASN A 1 819  ? 202.516 179.933 218.613 1.00 59.25  ? 830  ASN A O   1 
ATOM 1743 C CB  . ASN A 1 819  ? 204.239 177.420 218.794 1.00 55.31  ? 830  ASN A CB  1 
ATOM 1744 C CG  . ASN A 1 819  ? 204.372 176.996 220.247 1.00 60.58  ? 830  ASN A CG  1 
ATOM 1745 O OD1 . ASN A 1 819  ? 203.609 177.431 221.110 1.00 63.20  ? 830  ASN A OD1 1 
ATOM 1746 N ND2 . ASN A 1 819  ? 205.350 176.142 220.524 1.00 64.13  ? 830  ASN A ND2 1 
ATOM 1747 N N   . MET A 1 820  ? 201.210 178.596 219.886 1.00 56.99  ? 831  MET A N   1 
ATOM 1748 C CA  . MET A 1 820  ? 200.462 179.655 220.548 1.00 53.18  ? 831  MET A CA  1 
ATOM 1749 C C   . MET A 1 820  ? 200.749 179.581 222.042 1.00 52.21  ? 831  MET A C   1 
ATOM 1750 O O   . MET A 1 820  ? 200.663 178.499 222.638 1.00 57.13  ? 831  MET A O   1 
ATOM 1751 C CB  . MET A 1 820  ? 198.963 179.495 220.291 1.00 45.37  ? 831  MET A CB  1 
ATOM 1752 C CG  . MET A 1 820  ? 198.599 179.218 218.842 1.00 56.80  ? 831  MET A CG  1 
ATOM 1753 S SD  . MET A 1 820  ? 196.998 179.900 218.377 1.00 62.16  ? 831  MET A SD  1 
ATOM 1754 C CE  . MET A 1 820  ? 197.419 181.622 218.164 1.00 52.38  ? 831  MET A CE  1 
ATOM 1755 N N   . ASN A 1 821  ? 201.083 180.722 222.643 1.00 47.12  ? 832  ASN A N   1 
ATOM 1756 C CA  . ASN A 1 821  ? 201.298 180.815 224.080 1.00 42.41  ? 832  ASN A CA  1 
ATOM 1757 C C   . ASN A 1 821  ? 200.556 182.036 224.598 1.00 46.78  ? 832  ASN A C   1 
ATOM 1758 O O   . ASN A 1 821  ? 200.654 183.118 224.012 1.00 50.35  ? 832  ASN A O   1 
ATOM 1759 C CB  . ASN A 1 821  ? 202.791 180.913 224.413 1.00 42.87  ? 832  ASN A CB  1 
ATOM 1760 C CG  . ASN A 1 821  ? 203.059 180.892 225.905 1.00 45.69  ? 832  ASN A CG  1 
ATOM 1761 O OD1 . ASN A 1 821  ? 202.176 180.581 226.703 1.00 46.21  ? 832  ASN A OD1 1 
ATOM 1762 N ND2 . ASN A 1 821  ? 204.286 181.228 226.289 1.00 47.35  ? 832  ASN A ND2 1 
ATOM 1763 N N   . VAL A 1 822  ? 199.818 181.865 225.694 1.00 46.37  ? 833  VAL A N   1 
ATOM 1764 C CA  . VAL A 1 822  ? 199.018 182.938 226.266 1.00 42.18  ? 833  VAL A CA  1 
ATOM 1765 C C   . VAL A 1 822  ? 199.365 183.199 227.726 1.00 43.53  ? 833  VAL A C   1 
ATOM 1766 O O   . VAL A 1 822  ? 198.557 183.772 228.457 1.00 46.49  ? 833  VAL A O   1 
ATOM 1767 C CB  . VAL A 1 822  ? 197.511 182.658 226.102 1.00 40.53  ? 833  VAL A CB  1 
ATOM 1768 C CG1 . VAL A 1 822  ? 197.110 182.774 224.642 1.00 38.16  ? 833  VAL A CG1 1 
ATOM 1769 C CG2 . VAL A 1 822  ? 197.172 181.282 226.631 1.00 42.70  ? 833  VAL A CG2 1 
ATOM 1770 N N   . GLY A 1 823  ? 200.552 182.791 228.168 1.00 43.91  ? 834  GLY A N   1 
ATOM 1771 C CA  . GLY A 1 823  ? 200.978 183.086 229.522 1.00 45.16  ? 834  GLY A CA  1 
ATOM 1772 C C   . GLY A 1 823  ? 200.331 182.174 230.552 1.00 46.50  ? 834  GLY A C   1 
ATOM 1773 O O   . GLY A 1 823  ? 199.863 181.076 230.247 1.00 45.71  ? 834  GLY A O   1 
ATOM 1774 N N   . SER A 1 824  ? 200.309 182.648 231.796 1.00 46.98  ? 835  SER A N   1 
ATOM 1775 C CA  . SER A 1 824  ? 199.768 181.895 232.916 1.00 47.94  ? 835  SER A CA  1 
ATOM 1776 C C   . SER A 1 824  ? 198.823 182.775 233.723 1.00 47.26  ? 835  SER A C   1 
ATOM 1777 O O   . SER A 1 824  ? 198.931 184.004 233.711 1.00 49.23  ? 835  SER A O   1 
ATOM 1778 C CB  . SER A 1 824  ? 200.883 181.359 233.824 1.00 54.66  ? 835  SER A CB  1 
ATOM 1779 O OG  . SER A 1 824  ? 201.750 180.493 233.111 1.00 57.52  ? 835  SER A OG  1 
ATOM 1780 N N   . PHE A 1 825  ? 197.895 182.128 234.423 1.00 46.84  ? 836  PHE A N   1 
ATOM 1781 C CA  . PHE A 1 825  ? 196.919 182.852 235.227 1.00 46.57  ? 836  PHE A CA  1 
ATOM 1782 C C   . PHE A 1 825  ? 197.577 183.463 236.457 1.00 56.63  ? 836  PHE A C   1 
ATOM 1783 O O   . PHE A 1 825  ? 198.505 182.891 237.036 1.00 63.43  ? 836  PHE A O   1 
ATOM 1784 C CB  . PHE A 1 825  ? 195.785 181.920 235.651 1.00 47.53  ? 836  PHE A CB  1 
ATOM 1785 C CG  . PHE A 1 825  ? 194.922 181.458 234.513 1.00 46.21  ? 836  PHE A CG  1 
ATOM 1786 C CD1 . PHE A 1 825  ? 193.954 182.291 233.979 1.00 43.89  ? 836  PHE A CD1 1 
ATOM 1787 C CD2 . PHE A 1 825  ? 195.076 180.190 233.980 1.00 50.17  ? 836  PHE A CD2 1 
ATOM 1788 C CE1 . PHE A 1 825  ? 193.157 181.869 232.934 1.00 41.52  ? 836  PHE A CE1 1 
ATOM 1789 C CE2 . PHE A 1 825  ? 194.282 179.762 232.934 1.00 46.13  ? 836  PHE A CE2 1 
ATOM 1790 C CZ  . PHE A 1 825  ? 193.322 180.603 232.411 1.00 41.77  ? 836  PHE A CZ  1 
ATOM 1791 N N   . SER A 1 826  ? 197.087 184.634 236.857 1.00 59.54  ? 837  SER A N   1 
ATOM 1792 C CA  . SER A 1 826  ? 197.598 185.326 238.036 1.00 63.50  ? 837  SER A CA  1 
ATOM 1793 C C   . SER A 1 826  ? 196.807 184.871 239.257 1.00 68.65  ? 837  SER A C   1 
ATOM 1794 O O   . SER A 1 826  ? 195.631 185.217 239.409 1.00 71.14  ? 837  SER A O   1 
ATOM 1795 C CB  . SER A 1 826  ? 197.504 186.837 237.850 1.00 65.56  ? 837  SER A CB  1 
ATOM 1796 O OG  . SER A 1 826  ? 196.239 187.209 237.332 1.00 67.12  ? 837  SER A OG  1 
ATOM 1797 N N   . THR A 1 827  ? 197.450 184.097 240.126 1.00 70.39  ? 838  THR A N   1 
ATOM 1798 C CA  . THR A 1 827  ? 196.783 183.589 241.316 1.00 75.31  ? 838  THR A CA  1 
ATOM 1799 C C   . THR A 1 827  ? 196.599 184.696 242.347 1.00 83.96  ? 838  THR A C   1 
ATOM 1800 O O   . THR A 1 827  ? 197.536 185.434 242.665 1.00 85.79  ? 838  THR A O   1 
ATOM 1801 C CB  . THR A 1 827  ? 197.588 182.437 241.921 1.00 79.85  ? 838  THR A CB  1 
ATOM 1802 O OG1 . THR A 1 827  ? 197.357 181.241 241.166 1.00 78.34  ? 838  THR A OG1 1 
ATOM 1803 C CG2 . THR A 1 827  ? 197.192 182.203 243.372 1.00 81.43  ? 838  THR A CG2 1 
ATOM 1804 N N   . ASN A 1 828  ? 195.377 184.811 242.871 1.00 86.37  ? 839  ASN A N   1 
ATOM 1805 C CA  . ASN A 1 828  ? 195.112 185.780 243.929 1.00 87.39  ? 839  ASN A CA  1 
ATOM 1806 C C   . ASN A 1 828  ? 195.602 185.269 245.283 1.00 90.91  ? 839  ASN A C   1 
ATOM 1807 O O   . ASN A 1 828  ? 196.304 185.982 246.008 1.00 94.54  ? 839  ASN A O   1 
ATOM 1808 C CB  . ASN A 1 828  ? 193.615 186.145 243.940 1.00 88.21  ? 839  ASN A CB  1 
ATOM 1809 C CG  . ASN A 1 828  ? 192.724 185.060 244.542 1.00 89.38  ? 839  ASN A CG  1 
ATOM 1810 O OD1 . ASN A 1 828  ? 192.908 184.631 245.681 1.00 91.98  ? 839  ASN A OD1 1 
ATOM 1811 N ND2 . ASN A 1 828  ? 191.746 184.613 243.763 1.00 80.76  ? 839  ASN A ND2 1 
ATOM 1812 N N   . ALA A 1 829  ? 195.256 184.029 245.628 1.00 92.35  ? 840  ALA A N   1 
ATOM 1813 C CA  . ALA A 1 829  ? 195.710 183.404 246.864 1.00 94.01  ? 840  ALA A CA  1 
ATOM 1814 C C   . ALA A 1 829  ? 195.375 181.921 246.808 1.00 91.44  ? 840  ALA A C   1 
ATOM 1815 O O   . ALA A 1 829  ? 194.524 181.485 246.029 1.00 87.26  ? 840  ALA A O   1 
ATOM 1816 C CB  . ALA A 1 829  ? 195.074 184.057 248.097 1.00 92.33  ? 840  ALA A CB  1 
ATOM 1817 N N   . ASP A 1 830  ? 196.065 181.149 247.649 1.00 93.23  ? 841  ASP A N   1 
ATOM 1818 C CA  . ASP A 1 830  ? 195.831 179.716 247.822 1.00 92.21  ? 841  ASP A CA  1 
ATOM 1819 C C   . ASP A 1 830  ? 195.950 178.939 246.513 1.00 88.45  ? 841  ASP A C   1 
ATOM 1820 O O   . ASP A 1 830  ? 195.344 177.873 246.361 1.00 86.30  ? 841  ASP A O   1 
ATOM 1821 C CB  . ASP A 1 830  ? 194.465 179.456 248.472 1.00 92.74  ? 841  ASP A CB  1 
ATOM 1822 C CG  . ASP A 1 830  ? 194.376 178.086 249.120 1.00 98.94  ? 841  ASP A CG  1 
ATOM 1823 O OD1 . ASP A 1 830  ? 195.415 177.586 249.599 1.00 104.22 ? 841  ASP A OD1 1 
ATOM 1824 O OD2 . ASP A 1 830  ? 193.268 177.510 249.146 1.00 103.10 ? 841  ASP A OD2 1 
ATOM 1825 N N   . GLY A 1 831  ? 196.723 179.449 245.557 1.00 86.86  ? 842  GLY A N   1 
ATOM 1826 C CA  . GLY A 1 831  ? 196.861 178.774 244.282 1.00 87.04  ? 842  GLY A CA  1 
ATOM 1827 C C   . GLY A 1 831  ? 195.599 178.721 243.455 1.00 80.74  ? 842  GLY A C   1 
ATOM 1828 O O   . GLY A 1 831  ? 195.394 177.754 242.718 1.00 75.29  ? 842  GLY A O   1 
ATOM 1829 N N   . LYS A 1 832  ? 194.741 179.733 243.557 1.00 76.11  ? 843  LYS A N   1 
ATOM 1830 C CA  . LYS A 1 832  ? 193.475 179.764 242.843 1.00 68.75  ? 843  LYS A CA  1 
ATOM 1831 C C   . LYS A 1 832  ? 193.292 181.108 242.151 1.00 65.74  ? 843  LYS A C   1 
ATOM 1832 O O   . LYS A 1 832  ? 193.805 182.136 242.605 1.00 72.45  ? 843  LYS A O   1 
ATOM 1833 C CB  . LYS A 1 832  ? 192.298 179.507 243.792 1.00 70.31  ? 843  LYS A CB  1 
ATOM 1834 C CG  . LYS A 1 832  ? 192.254 178.099 244.361 1.00 69.22  ? 843  LYS A CG  1 
ATOM 1835 C CD  . LYS A 1 832  ? 191.314 178.018 245.551 1.00 68.67  ? 843  LYS A CD  1 
ATOM 1836 C CE  . LYS A 1 832  ? 191.292 176.619 246.143 1.00 72.35  ? 843  LYS A CE  1 
ATOM 1837 N NZ  . LYS A 1 832  ? 190.774 176.620 247.539 1.00 84.80  ? 843  LYS A NZ  1 
ATOM 1838 N N   . TRP A 1 833  ? 192.553 181.088 241.044 1.00 57.77  ? 844  TRP A N   1 
ATOM 1839 C CA  . TRP A 1 833  ? 192.218 182.296 240.306 1.00 57.17  ? 844  TRP A CA  1 
ATOM 1840 C C   . TRP A 1 833  ? 190.749 182.241 239.911 1.00 57.27  ? 844  TRP A C   1 
ATOM 1841 O O   . TRP A 1 833  ? 190.160 181.166 239.784 1.00 57.58  ? 844  TRP A O   1 
ATOM 1842 C CB  . TRP A 1 833  ? 193.105 182.469 239.065 1.00 56.84  ? 844  TRP A CB  1 
ATOM 1843 C CG  . TRP A 1 833  ? 192.994 181.344 238.082 1.00 56.84  ? 844  TRP A CG  1 
ATOM 1844 C CD1 . TRP A 1 833  ? 192.172 181.282 236.996 1.00 53.93  ? 844  TRP A CD1 1 
ATOM 1845 C CD2 . TRP A 1 833  ? 193.736 180.118 238.094 1.00 55.19  ? 844  TRP A CD2 1 
ATOM 1846 N NE1 . TRP A 1 833  ? 192.353 180.094 236.332 1.00 49.40  ? 844  TRP A NE1 1 
ATOM 1847 C CE2 . TRP A 1 833  ? 193.309 179.361 236.985 1.00 48.18  ? 844  TRP A CE2 1 
ATOM 1848 C CE3 . TRP A 1 833  ? 194.720 179.588 238.934 1.00 58.81  ? 844  TRP A CE3 1 
ATOM 1849 C CZ2 . TRP A 1 833  ? 193.830 178.103 236.696 1.00 47.52  ? 844  TRP A CZ2 1 
ATOM 1850 C CZ3 . TRP A 1 833  ? 195.236 178.338 238.645 1.00 55.50  ? 844  TRP A CZ3 1 
ATOM 1851 C CH2 . TRP A 1 833  ? 194.790 177.610 237.536 1.00 52.28  ? 844  TRP A CH2 1 
ATOM 1852 N N   . ASP A 1 834  ? 190.161 183.420 239.719 1.00 57.28  ? 845  ASP A N   1 
ATOM 1853 C CA  . ASP A 1 834  ? 188.741 183.537 239.400 1.00 51.17  ? 845  ASP A CA  1 
ATOM 1854 C C   . ASP A 1 834  ? 188.527 184.513 238.250 1.00 49.35  ? 845  ASP A C   1 
ATOM 1855 O O   . ASP A 1 834  ? 187.611 185.341 238.275 1.00 46.27  ? 845  ASP A O   1 
ATOM 1856 C CB  . ASP A 1 834  ? 187.933 183.951 240.631 1.00 52.22  ? 845  ASP A CB  1 
ATOM 1857 C CG  . ASP A 1 834  ? 188.320 185.322 241.153 1.00 59.34  ? 845  ASP A CG  1 
ATOM 1858 O OD1 . ASP A 1 834  ? 189.445 185.779 240.860 1.00 61.06  ? 845  ASP A OD1 1 
ATOM 1859 O OD2 . ASP A 1 834  ? 187.499 185.943 241.860 1.00 67.92  ? 845  ASP A OD2 1 
ATOM 1860 N N   . ASP A 1 835  ? 189.365 184.420 237.221 1.00 51.05  ? 846  ASP A N   1 
ATOM 1861 C CA  . ASP A 1 835  ? 189.216 185.272 236.053 1.00 50.67  ? 846  ASP A CA  1 
ATOM 1862 C C   . ASP A 1 835  ? 187.957 184.898 235.274 1.00 46.54  ? 846  ASP A C   1 
ATOM 1863 O O   . ASP A 1 835  ? 187.371 183.829 235.459 1.00 46.41  ? 846  ASP A O   1 
ATOM 1864 C CB  . ASP A 1 835  ? 190.442 185.162 235.147 1.00 51.14  ? 846  ASP A CB  1 
ATOM 1865 C CG  . ASP A 1 835  ? 191.587 186.041 235.606 1.00 64.02  ? 846  ASP A CG  1 
ATOM 1866 O OD1 . ASP A 1 835  ? 191.353 187.241 235.859 1.00 72.65  ? 846  ASP A OD1 1 
ATOM 1867 O OD2 . ASP A 1 835  ? 192.724 185.533 235.710 1.00 65.75  ? 846  ASP A OD2 1 
ATOM 1868 N N   . ASN A 1 836  ? 187.546 185.801 234.384 1.00 44.65  ? 847  ASN A N   1 
ATOM 1869 C CA  . ASN A 1 836  ? 186.375 185.565 233.548 1.00 39.39  ? 847  ASN A CA  1 
ATOM 1870 C C   . ASN A 1 836  ? 186.721 184.607 232.416 1.00 35.89  ? 847  ASN A C   1 
ATOM 1871 O O   . ASN A 1 836  ? 186.680 184.978 231.239 1.00 38.88  ? 847  ASN A O   1 
ATOM 1872 C CB  . ASN A 1 836  ? 185.834 186.885 232.993 1.00 44.89  ? 847  ASN A CB  1 
ATOM 1873 C CG  . ASN A 1 836  ? 184.502 186.718 232.288 1.00 52.53  ? 847  ASN A CG  1 
ATOM 1874 O OD1 . ASN A 1 836  ? 183.755 185.780 232.563 1.00 52.43  ? 847  ASN A OD1 1 
ATOM 1875 N ND2 . ASN A 1 836  ? 184.200 187.629 231.370 1.00 55.12  ? 847  ASN A ND2 1 
ATOM 1876 N N   . TRP A 1 837  ? 187.073 183.373 232.769 1.00 32.56  ? 848  TRP A N   1 
ATOM 1877 C CA  . TRP A 1 837  ? 187.470 182.358 231.807 1.00 30.62  ? 848  TRP A CA  1 
ATOM 1878 C C   . TRP A 1 837  ? 186.951 181.007 232.273 1.00 31.02  ? 848  TRP A C   1 
ATOM 1879 O O   . TRP A 1 837  ? 187.098 180.651 233.445 1.00 31.50  ? 848  TRP A O   1 
ATOM 1880 C CB  . TRP A 1 837  ? 188.995 182.326 231.642 1.00 31.53  ? 848  TRP A CB  1 
ATOM 1881 C CG  . TRP A 1 837  ? 189.507 181.186 230.822 1.00 28.13  ? 848  TRP A CG  1 
ATOM 1882 C CD1 . TRP A 1 837  ? 189.711 181.172 229.474 1.00 26.96  ? 848  TRP A CD1 1 
ATOM 1883 C CD2 . TRP A 1 837  ? 189.904 179.897 231.302 1.00 29.82  ? 848  TRP A CD2 1 
ATOM 1884 N NE1 . TRP A 1 837  ? 190.200 179.949 229.083 1.00 28.22  ? 848  TRP A NE1 1 
ATOM 1885 C CE2 . TRP A 1 837  ? 190.328 179.149 230.187 1.00 30.44  ? 848  TRP A CE2 1 
ATOM 1886 C CE3 . TRP A 1 837  ? 189.936 179.301 232.566 1.00 34.17  ? 848  TRP A CE3 1 
ATOM 1887 C CZ2 . TRP A 1 837  ? 190.778 177.836 230.298 1.00 35.46  ? 848  TRP A CZ2 1 
ATOM 1888 C CZ3 . TRP A 1 837  ? 190.384 177.999 232.674 1.00 38.31  ? 848  TRP A CZ3 1 
ATOM 1889 C CH2 . TRP A 1 837  ? 190.799 177.280 231.547 1.00 37.09  ? 848  TRP A CH2 1 
ATOM 1890 N N   . GLY A 1 838  ? 186.352 180.259 231.351 1.00 32.17  ? 849  GLY A N   1 
ATOM 1891 C CA  . GLY A 1 838  ? 185.760 178.984 231.714 1.00 31.32  ? 849  GLY A CA  1 
ATOM 1892 C C   . GLY A 1 838  ? 184.679 179.150 232.758 1.00 34.73  ? 849  GLY A C   1 
ATOM 1893 O O   . GLY A 1 838  ? 183.842 180.056 232.684 1.00 42.15  ? 849  GLY A O   1 
ATOM 1894 N N   . THR A 1 839  ? 184.694 178.266 233.753 1.00 33.70  ? 850  THR A N   1 
ATOM 1895 C CA  . THR A 1 839  ? 183.754 178.321 234.864 1.00 34.86  ? 850  THR A CA  1 
ATOM 1896 C C   . THR A 1 839  ? 184.383 178.864 236.140 1.00 38.99  ? 850  THR A C   1 
ATOM 1897 O O   . THR A 1 839  ? 183.850 178.625 237.228 1.00 39.81  ? 850  THR A O   1 
ATOM 1898 C CB  . THR A 1 839  ? 183.166 176.934 235.133 1.00 34.94  ? 850  THR A CB  1 
ATOM 1899 O OG1 . THR A 1 839  ? 184.226 176.010 235.412 1.00 42.36  ? 850  THR A OG1 1 
ATOM 1900 C CG2 . THR A 1 839  ? 182.380 176.448 233.929 1.00 41.36  ? 850  THR A CG2 1 
ATOM 1901 N N   . CYS A 1 840  ? 185.503 179.583 236.033 1.00 38.53  ? 851  CYS A N   1 
ATOM 1902 C CA  . CYS A 1 840  ? 186.175 180.104 237.218 1.00 37.00  ? 851  CYS A CA  1 
ATOM 1903 C C   . CYS A 1 840  ? 185.344 181.148 237.954 1.00 35.95  ? 851  CYS A C   1 
ATOM 1904 O O   . CYS A 1 840  ? 185.566 181.363 239.150 1.00 41.08  ? 851  CYS A O   1 
ATOM 1905 C CB  . CYS A 1 840  ? 187.533 180.692 236.835 1.00 41.40  ? 851  CYS A CB  1 
ATOM 1906 S SG  . CYS A 1 840  ? 188.619 179.539 235.964 1.00 48.03  ? 851  CYS A SG  1 
ATOM 1907 N N   . THR A 1 841  ? 184.397 181.799 237.275 1.00 34.20  ? 852  THR A N   1 
ATOM 1908 C CA  . THR A 1 841  ? 183.554 182.783 237.943 1.00 34.80  ? 852  THR A CA  1 
ATOM 1909 C C   . THR A 1 841  ? 182.588 182.142 238.930 1.00 36.08  ? 852  THR A C   1 
ATOM 1910 O O   . THR A 1 841  ? 182.161 182.806 239.880 1.00 34.49  ? 852  THR A O   1 
ATOM 1911 C CB  . THR A 1 841  ? 182.772 183.599 236.913 1.00 37.39  ? 852  THR A CB  1 
ATOM 1912 O OG1 . THR A 1 841  ? 181.763 182.775 236.315 1.00 39.81  ? 852  THR A OG1 1 
ATOM 1913 C CG2 . THR A 1 841  ? 183.703 184.118 235.829 1.00 43.54  ? 852  THR A CG2 1 
ATOM 1914 N N   . LEU A 1 842  ? 182.237 180.872 238.729 1.00 39.31  ? 853  LEU A N   1 
ATOM 1915 C CA  . LEU A 1 842  ? 181.369 180.161 239.659 1.00 41.31  ? 853  LEU A CA  1 
ATOM 1916 C C   . LEU A 1 842  ? 182.146 179.481 240.777 1.00 41.55  ? 853  LEU A C   1 
ATOM 1917 O O   . LEU A 1 842  ? 181.620 179.331 241.886 1.00 40.50  ? 853  LEU A O   1 
ATOM 1918 C CB  . LEU A 1 842  ? 180.534 179.119 238.909 1.00 37.10  ? 853  LEU A CB  1 
ATOM 1919 C CG  . LEU A 1 842  ? 179.794 179.610 237.663 1.00 34.00  ? 853  LEU A CG  1 
ATOM 1920 C CD1 . LEU A 1 842  ? 179.063 178.463 236.983 1.00 34.45  ? 853  LEU A CD1 1 
ATOM 1921 C CD2 . LEU A 1 842  ? 178.829 180.730 238.017 1.00 45.52  ? 853  LEU A CD2 1 
ATOM 1922 N N   . GLN A 1 843  ? 183.382 179.065 240.509 1.00 37.86  ? 854  GLN A N   1 
ATOM 1923 C CA  . GLN A 1 843  ? 184.229 178.427 241.508 1.00 38.99  ? 854  GLN A CA  1 
ATOM 1924 C C   . GLN A 1 843  ? 185.681 178.672 241.130 1.00 46.11  ? 854  GLN A C   1 
ATOM 1925 O O   . GLN A 1 843  ? 186.051 178.499 239.966 1.00 50.79  ? 854  GLN A O   1 
ATOM 1926 C CB  . GLN A 1 843  ? 183.942 176.925 241.600 1.00 41.02  ? 854  GLN A CB  1 
ATOM 1927 C CG  . GLN A 1 843  ? 184.901 176.161 242.496 1.00 46.94  ? 854  GLN A CG  1 
ATOM 1928 C CD  . GLN A 1 843  ? 184.497 174.713 242.679 1.00 45.48  ? 854  GLN A CD  1 
ATOM 1929 O OE1 . GLN A 1 843  ? 183.672 174.389 243.533 1.00 40.60  ? 854  GLN A OE1 1 
ATOM 1930 N NE2 . GLN A 1 843  ? 185.076 173.831 241.873 1.00 47.49  ? 854  GLN A NE2 1 
ATOM 1931 N N   . ASP A 1 844  ? 186.491 179.074 242.108 1.00 48.95  ? 855  ASP A N   1 
ATOM 1932 C CA  . ASP A 1 844  ? 187.890 179.396 241.847 1.00 50.44  ? 855  ASP A CA  1 
ATOM 1933 C C   . ASP A 1 844  ? 188.615 178.196 241.252 1.00 51.01  ? 855  ASP A C   1 
ATOM 1934 O O   . ASP A 1 844  ? 188.512 177.078 241.765 1.00 58.46  ? 855  ASP A O   1 
ATOM 1935 C CB  . ASP A 1 844  ? 188.571 179.851 243.137 1.00 56.99  ? 855  ASP A CB  1 
ATOM 1936 C CG  . ASP A 1 844  ? 187.868 181.030 243.781 1.00 66.52  ? 855  ASP A CG  1 
ATOM 1937 O OD1 . ASP A 1 844  ? 186.772 181.400 243.310 1.00 65.25  ? 855  ASP A OD1 1 
ATOM 1938 O OD2 . ASP A 1 844  ? 188.412 181.588 244.758 1.00 69.33  ? 855  ASP A OD2 1 
ATOM 1939 N N   . CYS A 1 845  ? 189.349 178.435 240.169 1.00 43.81  ? 856  CYS A N   1 
ATOM 1940 C CA  . CYS A 1 845  ? 189.966 177.365 239.403 1.00 45.94  ? 856  CYS A CA  1 
ATOM 1941 C C   . CYS A 1 845  ? 191.348 177.019 239.950 1.00 50.24  ? 856  CYS A C   1 
ATOM 1942 O O   . CYS A 1 845  ? 191.957 177.775 240.711 1.00 54.96  ? 856  CYS A O   1 
ATOM 1943 C CB  . CYS A 1 845  ? 190.076 177.759 237.930 1.00 51.70  ? 856  CYS A CB  1 
ATOM 1944 S SG  . CYS A 1 845  ? 188.501 177.827 237.049 1.00 48.47  ? 856  CYS A SG  1 
ATOM 1945 N N   . SER A 1 846  ? 191.839 175.851 239.542 1.00 49.56  ? 857  SER A N   1 
ATOM 1946 C CA  . SER A 1 846  ? 193.167 175.385 239.917 1.00 49.25  ? 857  SER A CA  1 
ATOM 1947 C C   . SER A 1 846  ? 193.609 174.335 238.909 1.00 55.01  ? 857  SER A C   1 
ATOM 1948 O O   . SER A 1 846  ? 192.805 173.830 238.121 1.00 58.75  ? 857  SER A O   1 
ATOM 1949 C CB  . SER A 1 846  ? 193.186 174.816 241.340 1.00 56.48  ? 857  SER A CB  1 
ATOM 1950 O OG  . SER A 1 846  ? 192.265 173.748 241.474 1.00 58.36  ? 857  SER A OG  1 
ATOM 1951 N N   . GLY A 1 847  ? 194.906 174.011 238.921 1.00 55.54  ? 858  GLY A N   1 
ATOM 1952 C CA  . GLY A 1 847  ? 195.421 172.958 238.023 1.00 55.57  ? 858  GLY A CA  1 
ATOM 1953 C C   . GLY A 1 847  ? 196.125 173.528 236.807 1.00 50.44  ? 858  GLY A C   1 
ATOM 1954 O O   . GLY A 1 847  ? 197.373 173.579 236.824 1.00 46.93  ? 858  GLY A O   1 
ATOM 1955 N N   . ASN A 1 848  ? 195.368 173.946 235.788 1.00 50.86  ? 859  ASN A N   1 
ATOM 1956 C CA  . ASN A 1 848  ? 195.984 174.435 234.520 1.00 51.43  ? 859  ASN A CA  1 
ATOM 1957 C C   . ASN A 1 848  ? 196.425 175.896 234.699 1.00 50.56  ? 859  ASN A C   1 
ATOM 1958 O O   . ASN A 1 848  ? 195.767 176.804 234.147 1.00 52.15  ? 859  ASN A O   1 
ATOM 1959 C CB  . ASN A 1 848  ? 195.066 174.163 233.328 1.00 59.22  ? 859  ASN A CB  1 
ATOM 1960 C CG  . ASN A 1 848  ? 193.745 174.893 233.408 1.00 62.09  ? 859  ASN A CG  1 
ATOM 1961 O OD1 . ASN A 1 848  ? 193.012 174.959 232.415 1.00 59.31  ? 859  ASN A OD1 1 
ATOM 1962 N ND2 . ASN A 1 848  ? 193.418 175.435 234.569 1.00 56.65  ? 859  ASN A ND2 1 
ATOM 1963 N N   . ARG A 1 849  ? 197.537 176.103 235.403 1.00 45.47  ? 860  ARG A N   1 
ATOM 1964 C CA  . ARG A 1 849  ? 197.986 177.493 235.658 1.00 49.17  ? 860  ARG A CA  1 
ATOM 1965 C C   . ARG A 1 849  ? 198.487 178.101 234.339 1.00 53.53  ? 860  ARG A C   1 
ATOM 1966 O O   . ARG A 1 849  ? 198.168 179.277 234.073 1.00 58.83  ? 860  ARG A O   1 
ATOM 1967 C CB  . ARG A 1 849  ? 199.076 177.585 236.729 1.00 50.46  ? 860  ARG A CB  1 
ATOM 1968 C CG  . ARG A 1 849  ? 199.164 179.033 237.188 1.00 55.33  ? 860  ARG A CG  1 
ATOM 1969 C CD  . ARG A 1 849  ? 200.519 179.460 237.716 1.00 55.51  ? 860  ARG A CD  1 
ATOM 1970 N NE  . ARG A 1 849  ? 200.490 180.895 238.014 1.00 60.52  ? 860  ARG A NE  1 
ATOM 1971 C CZ  . ARG A 1 849  ? 201.506 181.590 238.503 1.00 65.21  ? 860  ARG A CZ  1 
ATOM 1972 N NH1 . ARG A 1 849  ? 202.688 181.018 238.649 1.00 68.51  ? 860  ARG A NH1 1 
ATOM 1973 N NH2 . ARG A 1 849  ? 201.336 182.855 238.843 1.00 66.19  ? 860  ARG A NH2 1 
ATOM 1974 N N   . SER A 1 850  ? 199.241 177.330 233.554 1.00 53.09  ? 861  SER A N   1 
ATOM 1975 C CA  . SER A 1 850  ? 199.784 177.848 232.269 1.00 53.01  ? 861  SER A CA  1 
ATOM 1976 C C   . SER A 1 850  ? 198.943 177.335 231.092 1.00 55.14  ? 861  SER A C   1 
ATOM 1977 O O   . SER A 1 850  ? 198.320 176.260 231.236 1.00 56.75  ? 861  SER A O   1 
ATOM 1978 C CB  . SER A 1 850  ? 201.233 177.473 232.101 1.00 53.01  ? 861  SER A CB  1 
ATOM 1979 O OG  . SER A 1 850  ? 201.746 177.983 230.878 1.00 63.55  ? 861  SER A OG  1 
ATOM 1980 N N   . GLN A 1 851  ? 198.935 178.072 229.976 1.00 55.05  ? 862  GLN A N   1 
ATOM 1981 C CA  . GLN A 1 851  ? 198.136 177.672 228.787 1.00 56.41  ? 862  GLN A CA  1 
ATOM 1982 C C   . GLN A 1 851  ? 198.968 177.865 227.512 1.00 54.27  ? 862  GLN A C   1 
ATOM 1983 O O   . GLN A 1 851  ? 199.442 179.002 227.290 1.00 53.42  ? 862  GLN A O   1 
ATOM 1984 C CB  . GLN A 1 851  ? 196.867 178.516 228.675 1.00 50.08  ? 862  GLN A CB  1 
ATOM 1985 C CG  . GLN A 1 851  ? 196.061 178.623 229.964 1.00 47.92  ? 862  GLN A CG  1 
ATOM 1986 C CD  . GLN A 1 851  ? 195.351 177.340 230.334 1.00 53.31  ? 862  GLN A CD  1 
ATOM 1987 O OE1 . GLN A 1 851  ? 194.499 176.835 229.595 1.00 57.40  ? 862  GLN A OE1 1 
ATOM 1988 N NE2 . GLN A 1 851  ? 195.698 176.804 231.494 1.00 51.85  ? 862  GLN A NE2 1 
ATOM 1989 N N   . SER A 1 852  ? 199.133 176.808 226.708 1.00 51.63  ? 863  SER A N   1 
ATOM 1990 C CA  . SER A 1 852  ? 199.852 176.926 225.446 1.00 52.04  ? 863  SER A CA  1 
ATOM 1991 C C   . SER A 1 852  ? 199.598 175.666 224.632 1.00 52.30  ? 863  SER A C   1 
ATOM 1992 O O   . SER A 1 852  ? 199.287 174.607 225.184 1.00 54.61  ? 863  SER A O   1 
ATOM 1993 C CB  . SER A 1 852  ? 201.355 177.134 225.664 1.00 54.76  ? 863  SER A CB  1 
ATOM 1994 O OG  . SER A 1 852  ? 201.942 176.000 226.278 1.00 60.10  ? 863  SER A OG  1 
ATOM 1995 N N   . ASP A 1 853  ? 199.739 175.788 223.313 1.00 52.46  ? 864  ASP A N   1 
ATOM 1996 C CA  . ASP A 1 853  ? 199.511 174.637 222.447 1.00 57.01  ? 864  ASP A CA  1 
ATOM 1997 C C   . ASP A 1 853  ? 200.148 174.877 221.086 1.00 56.56  ? 864  ASP A C   1 
ATOM 1998 O O   . ASP A 1 853  ? 200.256 176.012 220.622 1.00 57.35  ? 864  ASP A O   1 
ATOM 1999 C CB  . ASP A 1 853  ? 198.015 174.344 222.290 1.00 59.62  ? 864  ASP A CB  1 
ATOM 2000 C CG  . ASP A 1 853  ? 197.674 172.894 222.572 1.00 63.74  ? 864  ASP A CG  1 
ATOM 2001 O OD1 . ASP A 1 853  ? 198.560 172.031 222.406 1.00 63.22  ? 864  ASP A OD1 1 
ATOM 2002 O OD2 . ASP A 1 853  ? 196.519 172.619 222.961 1.00 64.41  ? 864  ASP A OD2 1 
ATOM 2003 N N   . SER A 1 854  ? 200.531 173.782 220.433 1.00 54.32  ? 865  SER A N   1 
ATOM 2004 C CA  . SER A 1 854  ? 201.175 173.860 219.130 1.00 54.99  ? 865  SER A CA  1 
ATOM 2005 C C   . SER A 1 854  ? 200.631 172.755 218.237 1.00 52.95  ? 865  SER A C   1 
ATOM 2006 O O   . SER A 1 854  ? 200.129 171.735 218.715 1.00 53.88  ? 865  SER A O   1 
ATOM 2007 C CB  . SER A 1 854  ? 202.700 173.756 219.249 1.00 58.34  ? 865  SER A CB  1 
ATOM 2008 O OG  . SER A 1 854  ? 203.084 172.513 219.810 1.00 62.96  ? 865  SER A OG  1 
ATOM 2009 N N   . GLY A 1 855  ? 200.738 172.970 216.930 1.00 52.42  ? 866  GLY A N   1 
ATOM 2010 C CA  . GLY A 1 855  ? 200.193 172.007 215.989 1.00 54.89  ? 866  GLY A CA  1 
ATOM 2011 C C   . GLY A 1 855  ? 200.639 172.275 214.569 1.00 54.72  ? 866  GLY A C   1 
ATOM 2012 O O   . GLY A 1 855  ? 201.102 173.368 214.227 1.00 54.06  ? 866  GLY A O   1 
ATOM 2013 N N   . ALA A 1 856  ? 200.467 171.252 213.735 1.00 55.23  ? 867  ALA A N   1 
ATOM 2014 C CA  . ALA A 1 856  ? 200.868 171.288 212.336 1.00 52.55  ? 867  ALA A CA  1 
ATOM 2015 C C   . ALA A 1 856  ? 199.667 171.028 211.437 1.00 57.54  ? 867  ALA A C   1 
ATOM 2016 O O   . ALA A 1 856  ? 198.864 170.127 211.698 1.00 64.07  ? 867  ALA A O   1 
ATOM 2017 C CB  . ALA A 1 856  ? 201.965 170.259 212.048 1.00 49.84  ? 867  ALA A CB  1 
ATOM 2018 N N   . SER A 1 857  ? 199.559 171.821 210.377 1.00 50.82  ? 868  SER A N   1 
ATOM 2019 C CA  . SER A 1 857  ? 198.487 171.727 209.401 1.00 48.51  ? 868  SER A CA  1 
ATOM 2020 C C   . SER A 1 857  ? 199.054 171.573 207.996 1.00 51.56  ? 868  SER A C   1 
ATOM 2021 O O   . SER A 1 857  ? 200.183 171.978 207.705 1.00 61.49  ? 868  SER A O   1 
ATOM 2022 C CB  . SER A 1 857  ? 197.585 172.963 209.453 1.00 49.34  ? 868  SER A CB  1 
ATOM 2023 O OG  . SER A 1 857  ? 198.274 174.118 209.014 1.00 47.97  ? 868  SER A OG  1 
ATOM 2024 N N   . VAL A 1 858  ? 198.238 170.991 207.120 1.00 44.73  ? 869  VAL A N   1 
ATOM 2025 C CA  . VAL A 1 858  ? 198.594 170.780 205.725 1.00 41.02  ? 869  VAL A CA  1 
ATOM 2026 C C   . VAL A 1 858  ? 197.490 171.353 204.848 1.00 39.98  ? 869  VAL A C   1 
ATOM 2027 O O   . VAL A 1 858  ? 196.338 171.496 205.276 1.00 46.81  ? 869  VAL A O   1 
ATOM 2028 C CB  . VAL A 1 858  ? 198.824 169.286 205.404 1.00 41.88  ? 869  VAL A CB  1 
ATOM 2029 C CG1 . VAL A 1 858  ? 200.014 168.753 206.187 1.00 43.34  ? 869  VAL A CG1 1 
ATOM 2030 C CG2 . VAL A 1 858  ? 197.574 168.475 205.710 1.00 36.92  ? 869  VAL A CG2 1 
ATOM 2031 N N   . ALA A 1 859  ? 197.859 171.707 203.617 1.00 37.86  ? 870  ALA A N   1 
ATOM 2032 C CA  . ALA A 1 859  ? 196.911 172.217 202.638 1.00 37.42  ? 870  ALA A CA  1 
ATOM 2033 C C   . ALA A 1 859  ? 197.415 171.925 201.233 1.00 39.93  ? 870  ALA A C   1 
ATOM 2034 O O   . ALA A 1 859  ? 198.620 171.967 200.974 1.00 45.40  ? 870  ALA A O   1 
ATOM 2035 C CB  . ALA A 1 859  ? 196.685 173.724 202.808 1.00 36.12  ? 870  ALA A CB  1 
ATOM 2036 N N   . VAL A 1 860  ? 196.485 171.619 200.332 1.00 34.27  ? 871  VAL A N   1 
ATOM 2037 C CA  . VAL A 1 860  ? 196.781 171.392 198.922 1.00 31.73  ? 871  VAL A CA  1 
ATOM 2038 C C   . VAL A 1 860  ? 195.754 172.158 198.102 1.00 36.17  ? 871  VAL A C   1 
ATOM 2039 O O   . VAL A 1 860  ? 194.564 172.170 198.436 1.00 42.20  ? 871  VAL A O   1 
ATOM 2040 C CB  . VAL A 1 860  ? 196.762 169.890 198.561 1.00 31.04  ? 871  VAL A CB  1 
ATOM 2041 C CG1 . VAL A 1 860  ? 197.222 169.680 197.128 1.00 39.06  ? 871  VAL A CG1 1 
ATOM 2042 C CG2 . VAL A 1 860  ? 197.630 169.088 199.520 1.00 31.97  ? 871  VAL A CG2 1 
ATOM 2043 N N   . GLY A 1 861  ? 196.208 172.803 197.031 1.00 35.78  ? 872  GLY A N   1 
ATOM 2044 C CA  . GLY A 1 861  ? 195.259 173.549 196.225 1.00 39.34  ? 872  GLY A CA  1 
ATOM 2045 C C   . GLY A 1 861  ? 195.784 173.818 194.833 1.00 40.59  ? 872  GLY A C   1 
ATOM 2046 O O   . GLY A 1 861  ? 196.917 173.475 194.490 1.00 43.86  ? 872  GLY A O   1 
ATOM 2047 N N   . TRP A 1 862  ? 194.931 174.457 194.035 1.00 40.97  ? 873  TRP A N   1 
ATOM 2048 C CA  . TRP A 1 862  ? 195.237 174.784 192.650 1.00 41.00  ? 873  TRP A CA  1 
ATOM 2049 C C   . TRP A 1 862  ? 194.550 176.094 192.294 1.00 44.75  ? 873  TRP A C   1 
ATOM 2050 O O   . TRP A 1 862  ? 193.510 176.442 192.863 1.00 50.93  ? 873  TRP A O   1 
ATOM 2051 C CB  . TRP A 1 862  ? 194.797 173.656 191.708 1.00 41.05  ? 873  TRP A CB  1 
ATOM 2052 C CG  . TRP A 1 862  ? 195.036 173.916 190.249 1.00 45.11  ? 873  TRP A CG  1 
ATOM 2053 C CD1 . TRP A 1 862  ? 196.194 173.703 189.559 1.00 48.93  ? 873  TRP A CD1 1 
ATOM 2054 C CD2 . TRP A 1 862  ? 194.083 174.396 189.292 1.00 47.37  ? 873  TRP A CD2 1 
ATOM 2055 N NE1 . TRP A 1 862  ? 196.028 174.041 188.238 1.00 50.36  ? 873  TRP A NE1 1 
ATOM 2056 C CE2 . TRP A 1 862  ? 194.739 174.467 188.048 1.00 49.20  ? 873  TRP A CE2 1 
ATOM 2057 C CE3 . TRP A 1 862  ? 192.741 174.781 189.369 1.00 49.35  ? 873  TRP A CE3 1 
ATOM 2058 C CZ2 . TRP A 1 862  ? 194.101 174.907 186.891 1.00 47.07  ? 873  TRP A CZ2 1 
ATOM 2059 C CZ3 . TRP A 1 862  ? 192.109 175.217 188.219 1.00 52.68  ? 873  TRP A CZ3 1 
ATOM 2060 C CH2 . TRP A 1 862  ? 192.789 175.275 186.997 1.00 46.89  ? 873  TRP A CH2 1 
ATOM 2061 N N   . ARG A 1 863  ? 195.148 176.830 191.359 1.00 45.22  ? 874  ARG A N   1 
ATOM 2062 C CA  . ARG A 1 863  ? 194.641 178.149 191.010 1.00 50.21  ? 874  ARG A CA  1 
ATOM 2063 C C   . ARG A 1 863  ? 195.033 178.504 189.584 1.00 53.81  ? 874  ARG A C   1 
ATOM 2064 O O   . ARG A 1 863  ? 196.170 178.271 189.168 1.00 56.49  ? 874  ARG A O   1 
ATOM 2065 C CB  . ARG A 1 863  ? 195.177 179.211 191.974 1.00 55.60  ? 874  ARG A CB  1 
ATOM 2066 C CG  . ARG A 1 863  ? 194.624 180.603 191.744 1.00 60.12  ? 874  ARG A CG  1 
ATOM 2067 C CD  . ARG A 1 863  ? 195.338 181.730 192.514 1.00 68.97  ? 874  ARG A CD  1 
ATOM 2068 N NE  . ARG A 1 863  ? 196.797 181.649 192.585 1.00 82.65  ? 874  ARG A NE  1 
ATOM 2069 C CZ  . ARG A 1 863  ? 197.498 180.884 193.414 1.00 90.22  ? 874  ARG A CZ  1 
ATOM 2070 N NH1 . ARG A 1 863  ? 196.911 180.129 194.329 1.00 83.05  ? 874  ARG A NH1 1 
ATOM 2071 N NH2 . ARG A 1 863  ? 198.826 180.898 193.341 1.00 91.78  ? 874  ARG A NH2 1 
ATOM 2072 N N   . ASN A 1 864  ? 194.092 179.090 188.854 1.00 55.62  ? 875  ASN A N   1 
ATOM 2073 C CA  . ASN A 1 864  ? 194.350 179.598 187.513 1.00 54.79  ? 875  ASN A CA  1 
ATOM 2074 C C   . ASN A 1 864  ? 193.704 180.977 187.401 1.00 62.17  ? 875  ASN A C   1 
ATOM 2075 O O   . ASN A 1 864  ? 193.263 181.567 188.395 1.00 67.25  ? 875  ASN A O   1 
ATOM 2076 C CB  . ASN A 1 864  ? 193.910 178.561 186.458 1.00 51.04  ? 875  ASN A CB  1 
ATOM 2077 C CG  . ASN A 1 864  ? 192.423 178.639 186.088 1.00 56.74  ? 875  ASN A CG  1 
ATOM 2078 O OD1 . ASN A 1 864  ? 191.664 179.471 186.579 1.00 63.75  ? 875  ASN A OD1 1 
ATOM 2079 N ND2 . ASN A 1 864  ? 192.009 177.745 185.197 1.00 58.16  ? 875  ASN A ND2 1 
ATOM 2080 N N   . ASP A 1 865  ? 193.644 181.502 186.176 1.00 63.28  ? 876  ASP A N   1 
ATOM 2081 C CA  . ASP A 1 865  ? 193.097 182.830 185.931 1.00 69.45  ? 876  ASP A CA  1 
ATOM 2082 C C   . ASP A 1 865  ? 191.604 182.918 186.232 1.00 66.59  ? 876  ASP A C   1 
ATOM 2083 O O   . ASP A 1 865  ? 191.096 184.022 186.448 1.00 67.14  ? 876  ASP A O   1 
ATOM 2084 C CB  . ASP A 1 865  ? 193.370 183.213 184.471 1.00 78.05  ? 876  ASP A CB  1 
ATOM 2085 C CG  . ASP A 1 865  ? 193.345 184.713 184.228 1.00 87.51  ? 876  ASP A CG  1 
ATOM 2086 O OD1 . ASP A 1 865  ? 192.748 185.459 185.033 1.00 88.52  ? 876  ASP A OD1 1 
ATOM 2087 O OD2 . ASP A 1 865  ? 193.935 185.151 183.220 1.00 93.52  ? 876  ASP A OD2 1 
ATOM 2088 N N   . VAL A 1 866  ? 190.895 181.793 186.284 1.00 64.54  ? 877  VAL A N   1 
ATOM 2089 C CA  . VAL A 1 866  ? 189.448 181.830 186.459 1.00 60.19  ? 877  VAL A CA  1 
ATOM 2090 C C   . VAL A 1 866  ? 189.051 181.089 187.729 1.00 57.73  ? 877  VAL A C   1 
ATOM 2091 O O   . VAL A 1 866  ? 188.410 181.661 188.618 1.00 57.22  ? 877  VAL A O   1 
ATOM 2092 C CB  . VAL A 1 866  ? 188.733 181.240 185.231 1.00 59.54  ? 877  VAL A CB  1 
ATOM 2093 C CG1 . VAL A 1 866  ? 187.252 181.082 185.513 1.00 58.11  ? 877  VAL A CG1 1 
ATOM 2094 C CG2 . VAL A 1 866  ? 188.966 182.118 184.012 1.00 66.09  ? 877  VAL A CG2 1 
ATOM 2095 N N   . TRP A 1 867  ? 189.431 179.822 187.824 1.00 57.49  ? 878  TRP A N   1 
ATOM 2096 C CA  . TRP A 1 867  ? 189.065 178.971 188.946 1.00 52.40  ? 878  TRP A CA  1 
ATOM 2097 C C   . TRP A 1 867  ? 190.151 178.982 190.015 1.00 51.40  ? 878  TRP A C   1 
ATOM 2098 O O   . TRP A 1 867  ? 191.327 179.230 189.740 1.00 56.87  ? 878  TRP A O   1 
ATOM 2099 C CB  . TRP A 1 867  ? 188.821 177.535 188.477 1.00 48.89  ? 878  TRP A CB  1 
ATOM 2100 C CG  . TRP A 1 867  ? 187.580 177.366 187.667 1.00 56.42  ? 878  TRP A CG  1 
ATOM 2101 C CD1 . TRP A 1 867  ? 187.495 177.278 186.309 1.00 61.76  ? 878  TRP A CD1 1 
ATOM 2102 C CD2 . TRP A 1 867  ? 186.243 177.249 188.164 1.00 62.16  ? 878  TRP A CD2 1 
ATOM 2103 N NE1 . TRP A 1 867  ? 186.185 177.122 185.928 1.00 64.24  ? 878  TRP A NE1 1 
ATOM 2104 C CE2 . TRP A 1 867  ? 185.396 177.100 187.048 1.00 64.71  ? 878  TRP A CE2 1 
ATOM 2105 C CE3 . TRP A 1 867  ? 185.679 177.259 189.442 1.00 62.50  ? 878  TRP A CE3 1 
ATOM 2106 C CZ2 . TRP A 1 867  ? 184.017 176.962 187.173 1.00 62.98  ? 878  TRP A CZ2 1 
ATOM 2107 C CZ3 . TRP A 1 867  ? 184.310 177.122 189.564 1.00 67.13  ? 878  TRP A CZ3 1 
ATOM 2108 C CH2 . TRP A 1 867  ? 183.494 176.975 188.436 1.00 67.14  ? 878  TRP A CH2 1 
ATOM 2109 N N   . SER A 1 868  ? 189.735 178.708 191.249 1.00 46.83  ? 879  SER A N   1 
ATOM 2110 C CA  . SER A 1 868  ? 190.674 178.495 192.339 1.00 45.56  ? 879  SER A CA  1 
ATOM 2111 C C   . SER A 1 868  ? 190.020 177.591 193.371 1.00 45.44  ? 879  SER A C   1 
ATOM 2112 O O   . SER A 1 868  ? 188.818 177.691 193.622 1.00 53.84  ? 879  SER A O   1 
ATOM 2113 C CB  . SER A 1 868  ? 191.105 179.818 192.984 1.00 49.70  ? 879  SER A CB  1 
ATOM 2114 O OG  . SER A 1 868  ? 191.807 179.591 194.194 1.00 54.71  ? 879  SER A OG  1 
ATOM 2115 N N   . TRP A 1 869  ? 190.815 176.705 193.965 1.00 37.41  ? 880  TRP A N   1 
ATOM 2116 C CA  . TRP A 1 869  ? 190.300 175.837 195.013 1.00 35.13  ? 880  TRP A CA  1 
ATOM 2117 C C   . TRP A 1 869  ? 191.445 175.411 195.916 1.00 41.03  ? 880  TRP A C   1 
ATOM 2118 O O   . TRP A 1 869  ? 192.608 175.381 195.506 1.00 49.66  ? 880  TRP A O   1 
ATOM 2119 C CB  . TRP A 1 869  ? 189.580 174.613 194.433 1.00 33.28  ? 880  TRP A CB  1 
ATOM 2120 C CG  . TRP A 1 869  ? 190.487 173.645 193.741 1.00 34.73  ? 880  TRP A CG  1 
ATOM 2121 C CD1 . TRP A 1 869  ? 190.836 173.652 192.423 1.00 38.91  ? 880  TRP A CD1 1 
ATOM 2122 C CD2 . TRP A 1 869  ? 191.156 172.522 194.328 1.00 34.63  ? 880  TRP A CD2 1 
ATOM 2123 N NE1 . TRP A 1 869  ? 191.683 172.606 192.153 1.00 37.58  ? 880  TRP A NE1 1 
ATOM 2124 C CE2 . TRP A 1 869  ? 191.895 171.897 193.305 1.00 36.16  ? 880  TRP A CE2 1 
ATOM 2125 C CE3 . TRP A 1 869  ? 191.203 171.986 195.618 1.00 36.82  ? 880  TRP A CE3 1 
ATOM 2126 C CZ2 . TRP A 1 869  ? 192.672 170.763 193.532 1.00 37.99  ? 880  TRP A CZ2 1 
ATOM 2127 C CZ3 . TRP A 1 869  ? 191.975 170.860 195.841 1.00 35.05  ? 880  TRP A CZ3 1 
ATOM 2128 C CH2 . TRP A 1 869  ? 192.699 170.261 194.803 1.00 33.88  ? 880  TRP A CH2 1 
ATOM 2129 N N   . ASP A 1 870  ? 191.089 175.102 197.166 1.00 38.14  ? 881  ASP A N   1 
ATOM 2130 C CA  . ASP A 1 870  ? 192.109 174.703 198.170 1.00 33.83  ? 881  ASP A CA  1 
ATOM 2131 C C   . ASP A 1 870  ? 191.418 173.922 199.290 1.00 34.20  ? 881  ASP A C   1 
ATOM 2132 O O   . ASP A 1 870  ? 190.272 174.276 199.639 1.00 41.29  ? 881  ASP A O   1 
ATOM 2133 C CB  . ASP A 1 870  ? 192.866 175.917 198.687 1.00 35.04  ? 881  ASP A CB  1 
ATOM 2134 C CG  . ASP A 1 870  ? 192.001 177.112 199.063 1.00 43.48  ? 881  ASP A CG  1 
ATOM 2135 O OD1 . ASP A 1 870  ? 190.763 176.992 198.987 1.00 43.62  ? 881  ASP A OD1 1 
ATOM 2136 O OD2 . ASP A 1 870  ? 192.569 178.162 199.409 1.00 48.29  ? 881  ASP A OD2 1 
ATOM 2137 N N   . ILE A 1 871  ? 192.074 172.887 199.811 1.00 32.18  ? 882  ILE A N   1 
ATOM 2138 C CA  . ILE A 1 871  ? 191.537 172.092 200.909 1.00 33.16  ? 882  ILE A CA  1 
ATOM 2139 C C   . ILE A 1 871  ? 192.680 171.730 201.845 1.00 36.52  ? 882  ILE A C   1 
ATOM 2140 O O   . ILE A 1 871  ? 193.803 171.461 201.411 1.00 44.13  ? 882  ILE A O   1 
ATOM 2141 C CB  . ILE A 1 871  ? 190.798 170.831 200.396 1.00 33.34  ? 882  ILE A CB  1 
ATOM 2142 C CG1 . ILE A 1 871  ? 190.017 170.162 201.531 1.00 35.95  ? 882  ILE A CG1 1 
ATOM 2143 C CG2 . ILE A 1 871  ? 191.764 169.851 199.744 1.00 35.84  ? 882  ILE A CG2 1 
ATOM 2144 C CD1 . ILE A 1 871  ? 189.008 169.141 201.057 1.00 34.66  ? 882  ILE A CD1 1 
ATOM 2145 N N   . GLY A 1 872  ? 192.390 171.723 203.139 1.00 35.60  ? 883  GLY A N   1 
ATOM 2146 C CA  . GLY A 1 872  ? 193.414 171.428 204.117 1.00 35.75  ? 883  GLY A CA  1 
ATOM 2147 C C   . GLY A 1 872  ? 192.809 171.185 205.479 1.00 36.59  ? 883  GLY A C   1 
ATOM 2148 O O   . GLY A 1 872  ? 191.590 171.061 205.624 1.00 40.94  ? 883  GLY A O   1 
ATOM 2149 N N   . THR A 1 873  ? 193.677 171.137 206.484 1.00 35.59  ? 884  THR A N   1 
ATOM 2150 C CA  . THR A 1 873  ? 193.264 170.772 207.830 1.00 37.22  ? 884  THR A CA  1 
ATOM 2151 C C   . THR A 1 873  ? 193.660 171.854 208.826 1.00 42.03  ? 884  THR A C   1 
ATOM 2152 O O   . THR A 1 873  ? 194.627 172.592 208.628 1.00 44.68  ? 884  THR A O   1 
ATOM 2153 C CB  . THR A 1 873  ? 193.872 169.429 208.263 1.00 44.10  ? 884  THR A CB  1 
ATOM 2154 O OG1 . THR A 1 873  ? 195.288 169.573 208.432 1.00 47.60  ? 884  THR A OG1 1 
ATOM 2155 C CG2 . THR A 1 873  ? 193.595 168.352 207.223 1.00 49.72  ? 884  THR A CG2 1 
ATOM 2156 N N   . THR A 1 874  ? 192.870 171.950 209.893 1.00 44.27  ? 885  THR A N   1 
ATOM 2157 C CA  . THR A 1 874  ? 193.258 172.729 211.057 1.00 43.79  ? 885  THR A CA  1 
ATOM 2158 C C   . THR A 1 874  ? 194.505 172.098 211.680 1.00 50.98  ? 885  THR A C   1 
ATOM 2159 O O   . THR A 1 874  ? 194.650 170.872 211.671 1.00 55.15  ? 885  THR A O   1 
ATOM 2160 C CB  . THR A 1 874  ? 192.102 172.770 212.062 1.00 46.61  ? 885  THR A CB  1 
ATOM 2161 O OG1 . THR A 1 874  ? 191.008 173.506 211.500 1.00 44.96  ? 885  THR A OG1 1 
ATOM 2162 C CG2 . THR A 1 874  ? 192.507 173.409 213.385 1.00 50.05  ? 885  THR A CG2 1 
ATOM 2163 N N   . PRO A 1 875  ? 195.446 172.917 212.195 1.00 50.91  ? 886  PRO A N   1 
ATOM 2164 C CA  . PRO A 1 875  ? 196.680 172.356 212.769 1.00 52.50  ? 886  PRO A CA  1 
ATOM 2165 C C   . PRO A 1 875  ? 196.453 171.209 213.741 1.00 55.71  ? 886  PRO A C   1 
ATOM 2166 O O   . PRO A 1 875  ? 195.886 171.391 214.822 1.00 54.70  ? 886  PRO A O   1 
ATOM 2167 C CB  . PRO A 1 875  ? 197.308 173.567 213.467 1.00 48.25  ? 886  PRO A CB  1 
ATOM 2168 C CG  . PRO A 1 875  ? 196.892 174.712 212.613 1.00 49.06  ? 886  PRO A CG  1 
ATOM 2169 C CD  . PRO A 1 875  ? 195.501 174.389 212.125 1.00 49.64  ? 886  PRO A CD  1 
ATOM 2170 N N   . MET A 1 876  ? 196.888 170.020 213.311 1.00 58.89  ? 887  MET A N   1 
ATOM 2171 C CA  . MET A 1 876  ? 196.769 168.811 214.160 1.00 58.53  ? 887  MET A CA  1 
ATOM 2172 C C   . MET A 1 876  ? 197.603 169.025 215.420 1.00 58.46  ? 887  MET A C   1 
ATOM 2173 O O   . MET A 1 876  ? 198.742 169.507 215.296 1.00 58.18  ? 887  MET A O   1 
ATOM 2174 C CB  . MET A 1 876  ? 197.297 167.576 213.426 1.00 60.68  ? 887  MET A CB  1 
ATOM 2175 C CG  . MET A 1 876  ? 196.525 167.222 212.172 1.00 68.50  ? 887  MET A CG  1 
ATOM 2176 S SD  . MET A 1 876  ? 194.953 166.424 212.550 1.00 97.47  ? 887  MET A SD  1 
ATOM 2177 C CE  . MET A 1 876  ? 195.523 165.028 213.530 1.00 89.65  ? 887  MET A CE  1 
ATOM 2178 N N   . GLY A 1 877  ? 197.070 168.638 216.571 1.00 55.56  ? 888  GLY A N   1 
ATOM 2179 C CA  . GLY A 1 877  ? 197.726 168.848 217.847 1.00 55.80  ? 888  GLY A CA  1 
ATOM 2180 C C   . GLY A 1 877  ? 196.989 169.800 218.761 1.00 57.38  ? 888  GLY A C   1 
ATOM 2181 O O   . GLY A 1 877  ? 197.195 169.757 219.983 1.00 61.44  ? 888  GLY A O   1 
ATOM 2182 N N   . PHE A 1 878  ? 196.138 170.662 218.211 1.00 55.88  ? 889  PHE A N   1 
ATOM 2183 C CA  . PHE A 1 878  ? 195.269 171.495 219.022 1.00 51.35  ? 889  PHE A CA  1 
ATOM 2184 C C   . PHE A 1 878  ? 194.168 170.645 219.655 1.00 52.58  ? 889  PHE A C   1 
ATOM 2185 O O   . PHE A 1 878  ? 194.022 169.451 219.374 1.00 56.27  ? 889  PHE A O   1 
ATOM 2186 C CB  . PHE A 1 878  ? 194.660 172.616 218.180 1.00 47.94  ? 889  PHE A CB  1 
ATOM 2187 C CG  . PHE A 1 878  ? 195.627 173.713 217.833 1.00 51.58  ? 889  PHE A CG  1 
ATOM 2188 C CD1 . PHE A 1 878  ? 196.816 173.855 218.528 1.00 53.58  ? 889  PHE A CD1 1 
ATOM 2189 C CD2 . PHE A 1 878  ? 195.346 174.602 216.809 1.00 54.91  ? 889  PHE A CD2 1 
ATOM 2190 C CE1 . PHE A 1 878  ? 197.705 174.865 218.208 1.00 56.61  ? 889  PHE A CE1 1 
ATOM 2191 C CE2 . PHE A 1 878  ? 196.231 175.612 216.485 1.00 53.66  ? 889  PHE A CE2 1 
ATOM 2192 C CZ  . PHE A 1 878  ? 197.412 175.744 217.185 1.00 53.28  ? 889  PHE A CZ  1 
ATOM 2193 N N   . ASN A 1 879  ? 193.386 171.280 220.529 1.00 47.53  ? 890  ASN A N   1 
ATOM 2194 C CA  . ASN A 1 879  ? 192.325 170.562 221.228 1.00 47.82  ? 890  ASN A CA  1 
ATOM 2195 C C   . ASN A 1 879  ? 191.255 170.060 220.264 1.00 51.20  ? 890  ASN A C   1 
ATOM 2196 O O   . ASN A 1 879  ? 190.753 168.941 220.417 1.00 52.46  ? 890  ASN A O   1 
ATOM 2197 C CB  . ASN A 1 879  ? 191.712 171.458 222.303 1.00 46.53  ? 890  ASN A CB  1 
ATOM 2198 C CG  . ASN A 1 879  ? 192.647 171.684 223.473 1.00 51.89  ? 890  ASN A CG  1 
ATOM 2199 O OD1 . ASN A 1 879  ? 192.828 170.807 224.317 1.00 58.23  ? 890  ASN A OD1 1 
ATOM 2200 N ND2 . ASN A 1 879  ? 193.248 172.867 223.531 1.00 51.91  ? 890  ASN A ND2 1 
ATOM 2201 N N   . VAL A 1 880  ? 190.892 170.867 219.269 1.00 52.65  ? 891  VAL A N   1 
ATOM 2202 C CA  . VAL A 1 880  ? 189.877 170.501 218.286 1.00 51.41  ? 891  VAL A CA  1 
ATOM 2203 C C   . VAL A 1 880  ? 190.429 170.766 216.892 1.00 50.03  ? 891  VAL A C   1 
ATOM 2204 O O   . VAL A 1 880  ? 191.032 171.816 216.646 1.00 49.14  ? 891  VAL A O   1 
ATOM 2205 C CB  . VAL A 1 880  ? 188.560 171.270 218.509 1.00 46.12  ? 891  VAL A CB  1 
ATOM 2206 C CG1 . VAL A 1 880  ? 187.805 170.692 219.694 1.00 45.27  ? 891  VAL A CG1 1 
ATOM 2207 C CG2 . VAL A 1 880  ? 188.837 172.745 218.731 1.00 39.50  ? 891  VAL A CG2 1 
ATOM 2208 N N   . VAL A 1 881  ? 190.228 169.811 215.985 1.00 48.24  ? 892  VAL A N   1 
ATOM 2209 C CA  . VAL A 1 881  ? 190.728 169.893 214.617 1.00 49.37  ? 892  VAL A CA  1 
ATOM 2210 C C   . VAL A 1 881  ? 189.572 169.666 213.654 1.00 51.59  ? 892  VAL A C   1 
ATOM 2211 O O   . VAL A 1 881  ? 188.801 168.712 213.809 1.00 53.90  ? 892  VAL A O   1 
ATOM 2212 C CB  . VAL A 1 881  ? 191.855 168.870 214.360 1.00 52.93  ? 892  VAL A CB  1 
ATOM 2213 C CG1 . VAL A 1 881  ? 192.350 168.973 212.928 1.00 54.27  ? 892  VAL A CG1 1 
ATOM 2214 C CG2 . VAL A 1 881  ? 192.999 169.080 215.339 1.00 54.07  ? 892  VAL A CG2 1 
ATOM 2215 N N   . ASP A 1 882  ? 189.459 170.538 212.652 1.00 50.89  ? 893  ASP A N   1 
ATOM 2216 C CA  . ASP A 1 882  ? 188.411 170.444 211.646 1.00 52.37  ? 893  ASP A CA  1 
ATOM 2217 C C   . ASP A 1 882  ? 189.015 170.647 210.263 1.00 46.59  ? 893  ASP A C   1 
ATOM 2218 O O   . ASP A 1 882  ? 190.055 171.291 210.103 1.00 47.03  ? 893  ASP A O   1 
ATOM 2219 C CB  . ASP A 1 882  ? 187.297 171.473 211.890 1.00 58.74  ? 893  ASP A CB  1 
ATOM 2220 C CG  . ASP A 1 882  ? 186.401 171.100 213.056 1.00 66.81  ? 893  ASP A CG  1 
ATOM 2221 O OD1 . ASP A 1 882  ? 186.335 169.902 213.402 1.00 77.00  ? 893  ASP A OD1 1 
ATOM 2222 O OD2 . ASP A 1 882  ? 185.762 172.008 213.629 1.00 60.12  ? 893  ASP A OD2 1 
ATOM 2223 N N   . VAL A 1 883  ? 188.345 170.085 209.257 1.00 44.13  ? 894  VAL A N   1 
ATOM 2224 C CA  . VAL A 1 883  ? 188.795 170.226 207.876 1.00 40.91  ? 894  VAL A CA  1 
ATOM 2225 C C   . VAL A 1 883  ? 188.260 171.529 207.301 1.00 43.56  ? 894  VAL A C   1 
ATOM 2226 O O   . VAL A 1 883  ? 187.078 171.860 207.466 1.00 50.12  ? 894  VAL A O   1 
ATOM 2227 C CB  . VAL A 1 883  ? 188.347 169.018 207.041 1.00 40.97  ? 894  VAL A CB  1 
ATOM 2228 C CG1 . VAL A 1 883  ? 188.716 169.211 205.578 1.00 40.38  ? 894  VAL A CG1 1 
ATOM 2229 C CG2 . VAL A 1 883  ? 188.962 167.739 207.587 1.00 44.87  ? 894  VAL A CG2 1 
ATOM 2230 N N   . VAL A 1 884  ? 189.128 172.280 206.617 1.00 39.85  ? 895  VAL A N   1 
ATOM 2231 C CA  . VAL A 1 884  ? 188.779 173.586 206.074 1.00 36.59  ? 895  VAL A CA  1 
ATOM 2232 C C   . VAL A 1 884  ? 189.150 173.621 204.597 1.00 36.67  ? 895  VAL A C   1 
ATOM 2233 O O   . VAL A 1 884  ? 189.856 172.748 204.089 1.00 41.64  ? 895  VAL A O   1 
ATOM 2234 C CB  . VAL A 1 884  ? 189.478 174.735 206.832 1.00 37.37  ? 895  VAL A CB  1 
ATOM 2235 C CG1 . VAL A 1 884  ? 189.104 174.707 208.306 1.00 39.14  ? 895  VAL A CG1 1 
ATOM 2236 C CG2 . VAL A 1 884  ? 190.982 174.642 206.662 1.00 37.90  ? 895  VAL A CG2 1 
ATOM 2237 N N   . GLY A 1 885  ? 188.658 174.641 203.904 1.00 37.52  ? 896  GLY A N   1 
ATOM 2238 C CA  . GLY A 1 885  ? 188.941 174.766 202.490 1.00 39.59  ? 896  GLY A CA  1 
ATOM 2239 C C   . GLY A 1 885  ? 188.152 175.904 201.876 1.00 37.26  ? 896  GLY A C   1 
ATOM 2240 O O   . GLY A 1 885  ? 187.534 176.706 202.578 1.00 39.75  ? 896  GLY A O   1 
ATOM 2241 N N   . GLY A 1 886  ? 188.188 175.958 200.552 1.00 35.62  ? 897  GLY A N   1 
ATOM 2242 C CA  . GLY A 1 886  ? 187.474 177.005 199.843 1.00 38.50  ? 897  GLY A CA  1 
ATOM 2243 C C   . GLY A 1 886  ? 187.567 176.820 198.345 1.00 39.31  ? 897  GLY A C   1 
ATOM 2244 O O   . GLY A 1 886  ? 188.434 176.104 197.830 1.00 48.02  ? 897  GLY A O   1 
ATOM 2245 N N   . ILE A 1 887  ? 186.647 177.491 197.652 1.00 36.28  ? 898  ILE A N   1 
ATOM 2246 C CA  . ILE A 1 887  ? 186.584 177.495 196.197 1.00 41.46  ? 898  ILE A CA  1 
ATOM 2247 C C   . ILE A 1 887  ? 186.162 178.889 195.752 1.00 45.86  ? 898  ILE A C   1 
ATOM 2248 O O   . ILE A 1 887  ? 185.438 179.594 196.462 1.00 52.79  ? 898  ILE A O   1 
ATOM 2249 C CB  . ILE A 1 887  ? 185.619 176.410 195.660 1.00 38.04  ? 898  ILE A CB  1 
ATOM 2250 C CG1 . ILE A 1 887  ? 185.732 176.277 194.139 1.00 44.35  ? 898  ILE A CG1 1 
ATOM 2251 C CG2 . ILE A 1 887  ? 184.185 176.707 196.074 1.00 37.60  ? 898  ILE A CG2 1 
ATOM 2252 C CD1 . ILE A 1 887  ? 185.068 175.036 193.585 1.00 47.32  ? 898  ILE A CD1 1 
ATOM 2253 N N   . SER A 1 888  ? 186.643 179.299 194.579 1.00 40.56  ? 899  SER A N   1 
ATOM 2254 C CA  . SER A 1 888  ? 186.406 180.650 194.094 1.00 40.01  ? 899  SER A CA  1 
ATOM 2255 C C   . SER A 1 888  ? 186.392 180.663 192.572 1.00 46.92  ? 899  SER A C   1 
ATOM 2256 O O   . SER A 1 888  ? 187.142 179.931 191.916 1.00 57.30  ? 899  SER A O   1 
ATOM 2257 C CB  . SER A 1 888  ? 187.468 181.625 194.615 1.00 45.30  ? 899  SER A CB  1 
ATOM 2258 O OG  . SER A 1 888  ? 187.276 182.922 194.079 1.00 50.92  ? 899  SER A OG  1 
ATOM 2259 N N   . TYR A 1 889  ? 185.540 181.529 192.025 1.00 46.30  ? 900  TYR A N   1 
ATOM 2260 C CA  . TYR A 1 889  ? 185.384 181.726 190.593 1.00 46.26  ? 900  TYR A CA  1 
ATOM 2261 C C   . TYR A 1 889  ? 185.425 183.220 190.314 1.00 51.44  ? 900  TYR A C   1 
ATOM 2262 O O   . TYR A 1 889  ? 184.881 184.014 191.086 1.00 56.65  ? 900  TYR A O   1 
ATOM 2263 C CB  . TYR A 1 889  ? 184.063 181.116 190.096 1.00 45.31  ? 900  TYR A CB  1 
ATOM 2264 C CG  . TYR A 1 889  ? 183.753 181.358 188.636 1.00 56.59  ? 900  TYR A CG  1 
ATOM 2265 C CD1 . TYR A 1 889  ? 184.177 180.466 187.660 1.00 63.46  ? 900  TYR A CD1 1 
ATOM 2266 C CD2 . TYR A 1 889  ? 183.018 182.466 188.234 1.00 58.64  ? 900  TYR A CD2 1 
ATOM 2267 C CE1 . TYR A 1 889  ? 183.889 180.678 186.325 1.00 63.45  ? 900  TYR A CE1 1 
ATOM 2268 C CE2 . TYR A 1 889  ? 182.728 182.688 186.902 1.00 64.19  ? 900  TYR A CE2 1 
ATOM 2269 C CZ  . TYR A 1 889  ? 183.165 181.791 185.952 1.00 64.77  ? 900  TYR A CZ  1 
ATOM 2270 O OH  . TYR A 1 889  ? 182.877 182.007 184.625 1.00 64.89  ? 900  TYR A OH  1 
ATOM 2271 N N   . SER A 1 890  ? 186.078 183.606 189.222 1.00 52.45  ? 901  SER A N   1 
ATOM 2272 C CA  . SER A 1 890  ? 186.230 185.012 188.874 1.00 55.16  ? 901  SER A CA  1 
ATOM 2273 C C   . SER A 1 890  ? 185.963 185.206 187.390 1.00 65.96  ? 901  SER A C   1 
ATOM 2274 O O   . SER A 1 890  ? 186.354 184.373 186.567 1.00 69.85  ? 901  SER A O   1 
ATOM 2275 C CB  . SER A 1 890  ? 187.633 185.522 189.224 1.00 56.38  ? 901  SER A CB  1 
ATOM 2276 O OG  . SER A 1 890  ? 187.851 185.497 190.624 1.00 62.63  ? 901  SER A OG  1 
ATOM 2277 N N   . ASP A 1 891  ? 185.299 186.309 187.051 1.00 70.73  ? 902  ASP A N   1 
ATOM 2278 C CA  . ASP A 1 891  ? 184.993 186.597 185.655 1.00 73.62  ? 902  ASP A CA  1 
ATOM 2279 C C   . ASP A 1 891  ? 184.687 188.080 185.509 1.00 74.08  ? 902  ASP A C   1 
ATOM 2280 O O   . ASP A 1 891  ? 184.402 188.777 186.484 1.00 75.97  ? 902  ASP A O   1 
ATOM 2281 C CB  . ASP A 1 891  ? 183.823 185.744 185.153 1.00 75.07  ? 902  ASP A CB  1 
ATOM 2282 C CG  . ASP A 1 891  ? 183.735 185.708 183.639 1.00 87.02  ? 902  ASP A CG  1 
ATOM 2283 O OD1 . ASP A 1 891  ? 184.692 186.161 182.976 1.00 90.19  ? 902  ASP A OD1 1 
ATOM 2284 O OD2 . ASP A 1 891  ? 182.709 185.229 183.112 1.00 95.20  ? 902  ASP A OD2 1 
ATOM 2285 N N   . ASP A 1 892  ? 184.743 188.553 184.268 1.00 77.80  ? 903  ASP A N   1 
ATOM 2286 C CA  . ASP A 1 892  ? 184.393 189.932 183.976 1.00 81.15  ? 903  ASP A CA  1 
ATOM 2287 C C   . ASP A 1 892  ? 182.929 190.037 183.555 1.00 84.08  ? 903  ASP A C   1 
ATOM 2288 O O   . ASP A 1 892  ? 182.412 189.217 182.792 1.00 83.74  ? 903  ASP A O   1 
ATOM 2289 C CB  . ASP A 1 892  ? 185.293 190.495 182.876 1.00 83.34  ? 903  ASP A CB  1 
ATOM 2290 C CG  . ASP A 1 892  ? 186.740 190.617 183.311 1.00 85.18  ? 903  ASP A CG  1 
ATOM 2291 O OD1 . ASP A 1 892  ? 187.008 190.522 184.527 1.00 82.28  ? 903  ASP A OD1 1 
ATOM 2292 O OD2 . ASP A 1 892  ? 187.611 190.807 182.435 1.00 89.95  ? 903  ASP A OD2 1 
ATOM 2293 N N   . ILE A 1 893  ? 182.260 191.068 184.069 1.00 86.16  ? 904  ILE A N   1 
ATOM 2294 C CA  . ILE A 1 893  ? 180.903 191.399 183.653 1.00 89.61  ? 904  ILE A CA  1 
ATOM 2295 C C   . ILE A 1 893  ? 180.858 192.887 183.324 1.00 94.51  ? 904  ILE A C   1 
ATOM 2296 O O   . ILE A 1 893  ? 181.095 193.739 184.190 1.00 96.56  ? 904  ILE A O   1 
ATOM 2297 C CB  . ILE A 1 893  ? 179.864 191.008 184.725 1.00 88.29  ? 904  ILE A CB  1 
ATOM 2298 C CG1 . ILE A 1 893  ? 178.453 191.391 184.271 1.00 87.68  ? 904  ILE A CG1 1 
ATOM 2299 C CG2 . ILE A 1 893  ? 180.211 191.596 186.094 1.00 86.64  ? 904  ILE A CG2 1 
ATOM 2300 C CD1 . ILE A 1 893  ? 177.357 190.837 185.153 1.00 88.96  ? 904  ILE A CD1 1 
ATOM 2301 N N   . GLY A 1 894  ? 180.580 193.206 182.063 1.00 95.53  ? 905  GLY A N   1 
ATOM 2302 C CA  . GLY A 1 894  ? 180.636 194.568 181.594 1.00 99.23  ? 905  GLY A CA  1 
ATOM 2303 C C   . GLY A 1 894  ? 181.996 195.182 181.852 1.00 101.59 ? 905  GLY A C   1 
ATOM 2304 O O   . GLY A 1 894  ? 183.038 194.558 181.629 1.00 98.96  ? 905  GLY A O   1 
ATOM 2305 N N   . PRO A 1 895  ? 182.012 196.428 182.333 1.00 101.86 ? 906  PRO A N   1 
ATOM 2306 C CA  . PRO A 1 895  ? 183.280 197.047 182.743 1.00 99.62  ? 906  PRO A CA  1 
ATOM 2307 C C   . PRO A 1 895  ? 183.845 196.499 184.044 1.00 95.46  ? 906  PRO A C   1 
ATOM 2308 O O   . PRO A 1 895  ? 185.031 196.721 184.322 1.00 91.45  ? 906  PRO A O   1 
ATOM 2309 C CB  . PRO A 1 895  ? 182.911 198.532 182.895 1.00 99.65  ? 906  PRO A CB  1 
ATOM 2310 C CG  . PRO A 1 895  ? 181.637 198.699 182.120 1.00 100.29 ? 906  PRO A CG  1 
ATOM 2311 C CD  . PRO A 1 895  ? 180.912 197.404 182.300 1.00 98.54  ? 906  PRO A CD  1 
ATOM 2312 N N   . LEU A 1 896  ? 183.047 195.800 184.845 1.00 93.85  ? 907  LEU A N   1 
ATOM 2313 C CA  . LEU A 1 896  ? 183.468 195.370 186.170 1.00 86.85  ? 907  LEU A CA  1 
ATOM 2314 C C   . LEU A 1 896  ? 184.075 193.972 186.131 1.00 81.89  ? 907  LEU A C   1 
ATOM 2315 O O   . LEU A 1 896  ? 183.840 193.195 185.203 1.00 87.64  ? 907  LEU A O   1 
ATOM 2316 C CB  . LEU A 1 896  ? 182.286 195.389 187.140 1.00 83.33  ? 907  LEU A CB  1 
ATOM 2317 C CG  . LEU A 1 896  ? 181.454 196.672 187.181 1.00 90.73  ? 907  LEU A CG  1 
ATOM 2318 C CD1 . LEU A 1 896  ? 180.351 196.560 188.221 1.00 91.82  ? 907  LEU A CD1 1 
ATOM 2319 C CD2 . LEU A 1 896  ? 182.335 197.878 187.459 1.00 84.88  ? 907  LEU A CD2 1 
ATOM 2320 N N   . GLY A 1 897  ? 184.867 193.663 187.152 1.00 70.82  ? 908  GLY A N   1 
ATOM 2321 C CA  . GLY A 1 897  ? 185.359 192.312 187.373 1.00 66.49  ? 908  GLY A CA  1 
ATOM 2322 C C   . GLY A 1 897  ? 184.861 191.797 188.711 1.00 61.54  ? 908  GLY A C   1 
ATOM 2323 O O   . GLY A 1 897  ? 185.049 192.441 189.742 1.00 70.28  ? 908  GLY A O   1 
ATOM 2324 N N   . TYR A 1 898  ? 184.222 190.629 188.689 1.00 53.84  ? 909  TYR A N   1 
ATOM 2325 C CA  . TYR A 1 898  ? 183.557 190.108 189.872 1.00 51.14  ? 909  TYR A CA  1 
ATOM 2326 C C   . TYR A 1 898  ? 184.103 188.728 190.209 1.00 55.22  ? 909  TYR A C   1 
ATOM 2327 O O   . TYR A 1 898  ? 184.659 188.023 189.360 1.00 63.39  ? 909  TYR A O   1 
ATOM 2328 C CB  . TYR A 1 898  ? 182.033 190.054 189.685 1.00 54.69  ? 909  TYR A CB  1 
ATOM 2329 C CG  . TYR A 1 898  ? 181.530 188.808 188.991 1.00 56.47  ? 909  TYR A CG  1 
ATOM 2330 C CD1 . TYR A 1 898  ? 181.574 188.696 187.609 1.00 63.33  ? 909  TYR A CD1 1 
ATOM 2331 C CD2 . TYR A 1 898  ? 180.997 187.751 189.717 1.00 54.06  ? 909  TYR A CD2 1 
ATOM 2332 C CE1 . TYR A 1 898  ? 181.114 187.563 186.968 1.00 63.43  ? 909  TYR A CE1 1 
ATOM 2333 C CE2 . TYR A 1 898  ? 180.534 186.613 189.085 1.00 55.28  ? 909  TYR A CE2 1 
ATOM 2334 C CZ  . TYR A 1 898  ? 180.595 186.526 187.711 1.00 60.05  ? 909  TYR A CZ  1 
ATOM 2335 O OH  . TYR A 1 898  ? 180.134 185.396 187.076 1.00 65.14  ? 909  TYR A OH  1 
ATOM 2336 N N   . THR A 1 899  ? 183.947 188.367 191.481 1.00 54.33  ? 910  THR A N   1 
ATOM 2337 C CA  . THR A 1 899  ? 184.434 187.106 192.019 1.00 53.10  ? 910  THR A CA  1 
ATOM 2338 C C   . THR A 1 899  ? 183.450 186.592 193.060 1.00 47.92  ? 910  THR A C   1 
ATOM 2339 O O   . THR A 1 899  ? 182.993 187.348 193.921 1.00 54.03  ? 910  THR A O   1 
ATOM 2340 C CB  . THR A 1 899  ? 185.826 187.272 192.647 1.00 59.23  ? 910  THR A CB  1 
ATOM 2341 O OG1 . THR A 1 899  ? 186.758 187.696 191.644 1.00 61.73  ? 910  THR A OG1 1 
ATOM 2342 C CG2 . THR A 1 899  ? 186.306 185.965 193.259 1.00 56.80  ? 910  THR A CG2 1 
ATOM 2343 N N   . VAL A 1 900  ? 183.130 185.303 192.977 1.00 41.09  ? 911  VAL A N   1 
ATOM 2344 C CA  . VAL A 1 900  ? 182.237 184.642 193.919 1.00 41.06  ? 911  VAL A CA  1 
ATOM 2345 C C   . VAL A 1 900  ? 182.977 183.461 194.530 1.00 45.14  ? 911  VAL A C   1 
ATOM 2346 O O   . VAL A 1 900  ? 183.540 182.631 193.809 1.00 53.43  ? 911  VAL A O   1 
ATOM 2347 C CB  . VAL A 1 900  ? 180.934 184.173 193.240 1.00 40.24  ? 911  VAL A CB  1 
ATOM 2348 C CG1 . VAL A 1 900  ? 180.091 183.356 194.207 1.00 39.71  ? 911  VAL A CG1 1 
ATOM 2349 C CG2 . VAL A 1 900  ? 180.150 185.364 192.713 1.00 43.43  ? 911  VAL A CG2 1 
ATOM 2350 N N   . ASN A 1 901  ? 182.972 183.381 195.859 1.00 42.79  ? 912  ASN A N   1 
ATOM 2351 C CA  . ASN A 1 901  ? 183.703 182.333 196.554 1.00 40.53  ? 912  ASN A CA  1 
ATOM 2352 C C   . ASN A 1 901  ? 182.850 181.752 197.673 1.00 37.22  ? 912  ASN A C   1 
ATOM 2353 O O   . ASN A 1 901  ? 181.958 182.410 198.214 1.00 43.46  ? 912  ASN A O   1 
ATOM 2354 C CB  . ASN A 1 901  ? 185.039 182.853 197.109 1.00 43.26  ? 912  ASN A CB  1 
ATOM 2355 C CG  . ASN A 1 901  ? 184.875 184.080 197.990 1.00 50.32  ? 912  ASN A CG  1 
ATOM 2356 O OD1 . ASN A 1 901  ? 184.105 184.078 198.950 1.00 51.91  ? 912  ASN A OD1 1 
ATOM 2357 N ND2 . ASN A 1 901  ? 185.604 185.140 197.662 1.00 55.81  ? 912  ASN A ND2 1 
ATOM 2358 N N   . ALA A 1 902  ? 183.140 180.496 198.006 1.00 32.05  ? 913  ALA A N   1 
ATOM 2359 C CA  . ALA A 1 902  ? 182.524 179.810 199.132 1.00 34.26  ? 913  ALA A CA  1 
ATOM 2360 C C   . ALA A 1 902  ? 183.614 179.082 199.902 1.00 39.46  ? 913  ALA A C   1 
ATOM 2361 O O   . ALA A 1 902  ? 184.421 178.360 199.310 1.00 47.01  ? 913  ALA A O   1 
ATOM 2362 C CB  . ALA A 1 902  ? 181.446 178.821 198.673 1.00 36.28  ? 913  ALA A CB  1 
ATOM 2363 N N   . HIS A 1 903  ? 183.628 179.258 201.222 1.00 38.57  ? 914  HIS A N   1 
ATOM 2364 C CA  . HIS A 1 903  ? 184.766 178.793 202.002 1.00 39.98  ? 914  HIS A CA  1 
ATOM 2365 C C   . HIS A 1 903  ? 184.325 178.349 203.388 1.00 42.17  ? 914  HIS A C   1 
ATOM 2366 O O   . HIS A 1 903  ? 183.225 178.665 203.851 1.00 46.78  ? 914  HIS A O   1 
ATOM 2367 C CB  . HIS A 1 903  ? 185.838 179.883 202.123 1.00 43.22  ? 914  HIS A CB  1 
ATOM 2368 C CG  . HIS A 1 903  ? 185.352 181.135 202.783 1.00 47.11  ? 914  HIS A CG  1 
ATOM 2369 N ND1 . HIS A 1 903  ? 184.977 182.254 202.071 1.00 49.67  ? 914  HIS A ND1 1 
ATOM 2370 C CD2 . HIS A 1 903  ? 185.176 181.445 204.090 1.00 46.53  ? 914  HIS A CD2 1 
ATOM 2371 C CE1 . HIS A 1 903  ? 184.593 183.200 202.910 1.00 50.11  ? 914  HIS A CE1 1 
ATOM 2372 N NE2 . HIS A 1 903  ? 184.704 182.734 204.141 1.00 50.12  ? 914  HIS A NE2 1 
ATOM 2373 N N   . ARG A 1 904  ? 185.201 177.577 204.029 1.00 38.40  ? 915  ARG A N   1 
ATOM 2374 C CA  . ARG A 1 904  ? 185.125 177.246 205.444 1.00 35.25  ? 915  ARG A CA  1 
ATOM 2375 C C   . ARG A 1 904  ? 186.525 177.398 206.018 1.00 38.47  ? 915  ARG A C   1 
ATOM 2376 O O   . ARG A 1 904  ? 187.466 176.759 205.536 1.00 45.37  ? 915  ARG A O   1 
ATOM 2377 C CB  . ARG A 1 904  ? 184.604 175.824 205.665 1.00 32.29  ? 915  ARG A CB  1 
ATOM 2378 C CG  . ARG A 1 904  ? 184.572 175.397 207.122 1.00 34.46  ? 915  ARG A CG  1 
ATOM 2379 C CD  . ARG A 1 904  ? 183.870 174.062 207.290 1.00 38.70  ? 915  ARG A CD  1 
ATOM 2380 N NE  . ARG A 1 904  ? 183.522 173.802 208.682 1.00 42.24  ? 915  ARG A NE  1 
ATOM 2381 C CZ  . ARG A 1 904  ? 183.715 172.643 209.297 1.00 45.18  ? 915  ARG A CZ  1 
ATOM 2382 N NH1 . ARG A 1 904  ? 184.254 171.610 208.671 1.00 46.14  ? 915  ARG A NH1 1 
ATOM 2383 N NH2 . ARG A 1 904  ? 183.359 172.519 210.572 1.00 48.83  ? 915  ARG A NH2 1 
ATOM 2384 N N   . ARG A 1 905  ? 186.663 178.247 207.032 1.00 38.29  ? 916  ARG A N   1 
ATOM 2385 C CA  . ARG A 1 905  ? 187.954 178.657 207.560 1.00 37.99  ? 916  ARG A CA  1 
ATOM 2386 C C   . ARG A 1 905  ? 187.913 178.656 209.081 1.00 37.10  ? 916  ARG A C   1 
ATOM 2387 O O   . ARG A 1 905  ? 186.829 178.675 209.676 1.00 38.82  ? 916  ARG A O   1 
ATOM 2388 C CB  . ARG A 1 905  ? 188.340 180.060 207.062 1.00 43.61  ? 916  ARG A CB  1 
ATOM 2389 C CG  . ARG A 1 905  ? 188.507 180.174 205.556 1.00 47.07  ? 916  ARG A CG  1 
ATOM 2390 C CD  . ARG A 1 905  ? 189.714 179.393 205.066 1.00 48.19  ? 916  ARG A CD  1 
ATOM 2391 N NE  . ARG A 1 905  ? 190.022 179.690 203.672 1.00 49.46  ? 916  ARG A NE  1 
ATOM 2392 C CZ  . ARG A 1 905  ? 190.477 178.801 202.800 1.00 49.32  ? 916  ARG A CZ  1 
ATOM 2393 N NH1 . ARG A 1 905  ? 190.688 177.541 203.144 1.00 45.94  ? 916  ARG A NH1 1 
ATOM 2394 N NH2 . ARG A 1 905  ? 190.727 179.186 201.552 1.00 51.58  ? 916  ARG A NH2 1 
ATOM 2395 N N   . PRO A 1 906  ? 189.071 178.596 209.733 1.00 34.20  ? 917  PRO A N   1 
ATOM 2396 C CA  . PRO A 1 906  ? 189.110 178.797 211.183 1.00 31.00  ? 917  PRO A CA  1 
ATOM 2397 C C   . PRO A 1 906  ? 189.242 180.272 211.532 1.00 32.34  ? 917  PRO A C   1 
ATOM 2398 O O   . PRO A 1 906  ? 189.513 181.123 210.682 1.00 41.27  ? 917  PRO A O   1 
ATOM 2399 C CB  . PRO A 1 906  ? 190.352 178.014 211.609 1.00 33.28  ? 917  PRO A CB  1 
ATOM 2400 C CG  . PRO A 1 906  ? 191.261 178.148 210.435 1.00 35.69  ? 917  PRO A CG  1 
ATOM 2401 C CD  . PRO A 1 906  ? 190.368 178.126 209.213 1.00 36.01  ? 917  PRO A CD  1 
ATOM 2402 N N   . ILE A 1 907  ? 189.042 180.568 212.812 1.00 31.13  ? 918  ILE A N   1 
ATOM 2403 C CA  . ILE A 1 907  ? 189.212 181.914 213.349 1.00 34.63  ? 918  ILE A CA  1 
ATOM 2404 C C   . ILE A 1 907  ? 190.445 181.898 214.242 1.00 37.30  ? 918  ILE A C   1 
ATOM 2405 O O   . ILE A 1 907  ? 190.475 181.204 215.264 1.00 38.64  ? 918  ILE A O   1 
ATOM 2406 C CB  . ILE A 1 907  ? 187.968 182.381 214.116 1.00 32.13  ? 918  ILE A CB  1 
ATOM 2407 C CG1 . ILE A 1 907  ? 186.780 182.531 213.164 1.00 28.42  ? 918  ILE A CG1 1 
ATOM 2408 C CG2 . ILE A 1 907  ? 188.250 183.691 214.837 1.00 30.54  ? 918  ILE A CG2 1 
ATOM 2409 C CD1 . ILE A 1 907  ? 185.568 183.180 213.795 1.00 32.14  ? 918  ILE A CD1 1 
ATOM 2410 N N   . SER A 1 908  ? 191.462 182.670 213.867 1.00 34.79  ? 919  SER A N   1 
ATOM 2411 C CA  . SER A 1 908  ? 192.744 182.667 214.558 1.00 38.45  ? 919  SER A CA  1 
ATOM 2412 C C   . SER A 1 908  ? 192.939 183.864 215.480 1.00 43.19  ? 919  SER A C   1 
ATOM 2413 O O   . SER A 1 908  ? 194.075 184.133 215.885 1.00 45.10  ? 919  SER A O   1 
ATOM 2414 C CB  . SER A 1 908  ? 193.888 182.617 213.539 1.00 42.25  ? 919  SER A CB  1 
ATOM 2415 O OG  . SER A 1 908  ? 193.853 183.742 212.679 1.00 48.59  ? 919  SER A OG  1 
ATOM 2416 N N   . SER A 1 909  ? 191.871 184.591 215.817 1.00 46.78  ? 920  SER A N   1 
ATOM 2417 C CA  . SER A 1 909  ? 192.007 185.776 216.656 1.00 45.06  ? 920  SER A CA  1 
ATOM 2418 C C   . SER A 1 909  ? 192.484 185.450 218.067 1.00 36.66  ? 920  SER A C   1 
ATOM 2419 O O   . SER A 1 909  ? 193.054 186.323 218.729 1.00 37.97  ? 920  SER A O   1 
ATOM 2420 C CB  . SER A 1 909  ? 190.679 186.530 216.723 1.00 47.61  ? 920  SER A CB  1 
ATOM 2421 O OG  . SER A 1 909  ? 190.223 186.877 215.427 1.00 49.24  ? 920  SER A OG  1 
ATOM 2422 N N   . SER A 1 910  ? 192.268 184.225 218.540 1.00 33.57  ? 921  SER A N   1 
ATOM 2423 C CA  . SER A 1 910  ? 192.664 183.854 219.891 1.00 32.73  ? 921  SER A CA  1 
ATOM 2424 C C   . SER A 1 910  ? 192.855 182.346 219.954 1.00 32.52  ? 921  SER A C   1 
ATOM 2425 O O   . SER A 1 910  ? 192.421 181.610 219.065 1.00 36.61  ? 921  SER A O   1 
ATOM 2426 C CB  . SER A 1 910  ? 191.631 184.311 220.925 1.00 32.84  ? 921  SER A CB  1 
ATOM 2427 O OG  . SER A 1 910  ? 190.423 183.583 220.793 1.00 33.57  ? 921  SER A OG  1 
ATOM 2428 N N   . LEU A 1 911  ? 193.520 181.900 221.022 1.00 30.58  ? 922  LEU A N   1 
ATOM 2429 C CA  . LEU A 1 911  ? 193.763 180.472 221.202 1.00 31.51  ? 922  LEU A CA  1 
ATOM 2430 C C   . LEU A 1 911  ? 192.458 179.701 221.359 1.00 34.54  ? 922  LEU A C   1 
ATOM 2431 O O   . LEU A 1 911  ? 192.309 178.604 220.808 1.00 38.64  ? 922  LEU A O   1 
ATOM 2432 C CB  . LEU A 1 911  ? 194.670 180.241 222.411 1.00 32.84  ? 922  LEU A CB  1 
ATOM 2433 C CG  . LEU A 1 911  ? 194.900 178.785 222.818 1.00 27.94  ? 922  LEU A CG  1 
ATOM 2434 C CD1 . LEU A 1 911  ? 195.609 178.022 221.712 1.00 24.61  ? 922  LEU A CD1 1 
ATOM 2435 C CD2 . LEU A 1 911  ? 195.687 178.708 224.116 1.00 38.67  ? 922  LEU A CD2 1 
ATOM 2436 N N   . LEU A 1 912  ? 191.506 180.255 222.112 1.00 32.68  ? 923  LEU A N   1 
ATOM 2437 C CA  . LEU A 1 912  ? 190.223 179.586 222.299 1.00 28.03  ? 923  LEU A CA  1 
ATOM 2438 C C   . LEU A 1 912  ? 189.475 179.457 220.977 1.00 30.21  ? 923  LEU A C   1 
ATOM 2439 O O   . LEU A 1 912  ? 188.875 178.416 220.687 1.00 30.21  ? 923  LEU A O   1 
ATOM 2440 C CB  . LEU A 1 912  ? 189.384 180.346 223.326 1.00 27.55  ? 923  LEU A CB  1 
ATOM 2441 C CG  . LEU A 1 912  ? 187.977 179.807 223.575 1.00 28.38  ? 923  LEU A CG  1 
ATOM 2442 C CD1 . LEU A 1 912  ? 188.051 178.388 224.107 1.00 34.58  ? 923  LEU A CD1 1 
ATOM 2443 C CD2 . LEU A 1 912  ? 187.222 180.705 224.540 1.00 27.79  ? 923  LEU A CD2 1 
ATOM 2444 N N   . ALA A 1 913  ? 189.494 180.513 220.164 1.00 31.34  ? 924  ALA A N   1 
ATOM 2445 C CA  . ALA A 1 913  ? 188.819 180.465 218.871 1.00 29.91  ? 924  ALA A CA  1 
ATOM 2446 C C   . ALA A 1 913  ? 189.537 179.528 217.906 1.00 34.42  ? 924  ALA A C   1 
ATOM 2447 O O   . ALA A 1 913  ? 188.896 178.795 217.144 1.00 40.27  ? 924  ALA A O   1 
ATOM 2448 C CB  . ALA A 1 913  ? 188.717 181.872 218.281 1.00 28.78  ? 924  ALA A CB  1 
ATOM 2449 N N   . PHE A 1 914  ? 190.869 179.535 217.919 1.00 31.94  ? 925  PHE A N   1 
ATOM 2450 C CA  . PHE A 1 914  ? 191.619 178.738 216.910 1.00 28.75  ? 925  PHE A CA  1 
ATOM 2451 C C   . PHE A 1 914  ? 191.696 177.277 217.312 1.00 32.89  ? 925  PHE A C   1 
ATOM 2452 O O   . PHE A 1 914  ? 191.194 176.429 216.548 1.00 37.27  ? 925  PHE A O   1 
ATOM 2453 C CB  . PHE A 1 914  ? 193.007 179.358 216.735 1.00 30.59  ? 925  PHE A CB  1 
ATOM 2454 C CG  . PHE A 1 914  ? 193.784 178.865 215.523 1.00 33.76  ? 925  PHE A CG  1 
ATOM 2455 C CD1 . PHE A 1 914  ? 193.125 178.363 214.408 1.00 37.76  ? 925  PHE A CD1 1 
ATOM 2456 C CD2 . PHE A 1 914  ? 195.171 178.929 215.492 1.00 37.10  ? 925  PHE A CD2 1 
ATOM 2457 C CE1 . PHE A 1 914  ? 193.836 177.919 213.306 1.00 35.57  ? 925  PHE A CE1 1 
ATOM 2458 C CE2 . PHE A 1 914  ? 195.876 178.487 214.386 1.00 37.49  ? 925  PHE A CE2 1 
ATOM 2459 C CZ  . PHE A 1 914  ? 195.208 177.983 213.297 1.00 35.50  ? 925  PHE A CZ  1 
ATOM 2460 N N   . GLY A 1 915  ? 192.299 176.975 218.462 1.00 35.33  ? 926  GLY A N   1 
ATOM 2461 C CA  . GLY A 1 915  ? 192.499 175.590 218.837 1.00 38.82  ? 926  GLY A CA  1 
ATOM 2462 C C   . GLY A 1 915  ? 191.609 175.118 219.966 1.00 39.12  ? 926  GLY A C   1 
ATOM 2463 O O   . GLY A 1 915  ? 191.500 173.914 220.215 1.00 44.31  ? 926  GLY A O   1 
ATOM 2464 N N   . GLY A 1 916  ? 190.970 176.051 220.657 1.00 35.23  ? 927  GLY A N   1 
ATOM 2465 C CA  . GLY A 1 916  ? 190.133 175.714 221.786 1.00 32.83  ? 927  GLY A CA  1 
ATOM 2466 C C   . GLY A 1 916  ? 190.937 175.498 223.056 1.00 33.54  ? 927  GLY A C   1 
ATOM 2467 O O   . GLY A 1 916  ? 192.144 175.262 223.039 1.00 39.66  ? 927  GLY A O   1 
ATOM 2468 N N   . GLN A 1 917  ? 190.239 175.583 224.185 1.00 33.22  ? 928  GLN A N   1 
ATOM 2469 C CA  . GLN A 1 917  ? 190.849 175.402 225.492 1.00 33.89  ? 928  GLN A CA  1 
ATOM 2470 C C   . GLN A 1 917  ? 190.043 174.389 226.292 1.00 39.07  ? 928  GLN A C   1 
ATOM 2471 O O   . GLN A 1 917  ? 188.922 174.021 225.931 1.00 42.89  ? 928  GLN A O   1 
ATOM 2472 C CB  . GLN A 1 917  ? 190.949 176.729 226.256 1.00 30.27  ? 928  GLN A CB  1 
ATOM 2473 C CG  . GLN A 1 917  ? 192.007 177.676 225.715 1.00 30.79  ? 928  GLN A CG  1 
ATOM 2474 C CD  . GLN A 1 917  ? 192.241 178.867 226.622 1.00 32.12  ? 928  GLN A CD  1 
ATOM 2475 O OE1 . GLN A 1 917  ? 191.493 179.843 226.591 1.00 32.56  ? 928  GLN A OE1 1 
ATOM 2476 N NE2 . GLN A 1 917  ? 193.287 178.792 227.436 1.00 35.15  ? 928  GLN A NE2 1 
ATOM 2477 N N   . LYS A 1 918  ? 190.634 173.937 227.394 1.00 41.28  ? 929  LYS A N   1 
ATOM 2478 C CA  . LYS A 1 918  ? 190.009 172.978 228.293 1.00 42.40  ? 929  LYS A CA  1 
ATOM 2479 C C   . LYS A 1 918  ? 189.774 173.657 229.632 1.00 48.57  ? 929  LYS A C   1 
ATOM 2480 O O   . LYS A 1 918  ? 190.663 174.343 230.147 1.00 52.16  ? 929  LYS A O   1 
ATOM 2481 C CB  . LYS A 1 918  ? 190.882 171.733 228.468 1.00 49.71  ? 929  LYS A CB  1 
ATOM 2482 C CG  . LYS A 1 918  ? 190.160 170.558 229.106 1.00 55.27  ? 929  LYS A CG  1 
ATOM 2483 C CD  . LYS A 1 918  ? 191.119 169.422 229.422 1.00 52.35  ? 929  LYS A CD  1 
ATOM 2484 C CE  . LYS A 1 918  ? 191.831 168.931 228.174 1.00 49.33  ? 929  LYS A CE  1 
ATOM 2485 N NZ  . LYS A 1 918  ? 192.770 167.817 228.480 1.00 56.09  ? 929  LYS A NZ  1 
ATOM 2486 N N   . ASP A 1 919  ? 188.579 173.472 230.188 1.00 46.94  ? 930  ASP A N   1 
ATOM 2487 C CA  . ASP A 1 919  ? 188.274 174.033 231.496 1.00 47.09  ? 930  ASP A CA  1 
ATOM 2488 C C   . ASP A 1 919  ? 189.175 173.404 232.551 1.00 49.63  ? 930  ASP A C   1 
ATOM 2489 O O   . ASP A 1 919  ? 189.692 172.299 232.367 1.00 53.70  ? 930  ASP A O   1 
ATOM 2490 C CB  . ASP A 1 919  ? 186.801 173.804 231.838 1.00 48.28  ? 930  ASP A CB  1 
ATOM 2491 C CG  . ASP A 1 919  ? 186.388 174.480 233.132 1.00 49.89  ? 930  ASP A CG  1 
ATOM 2492 O OD1 . ASP A 1 919  ? 186.338 175.727 233.162 1.00 44.49  ? 930  ASP A OD1 1 
ATOM 2493 O OD2 . ASP A 1 919  ? 186.111 173.763 234.116 1.00 55.01  ? 930  ASP A OD2 1 
ATOM 2494 N N   . SER A 1 920  ? 189.372 174.122 233.652 1.00 47.55  ? 931  SER A N   1 
ATOM 2495 C CA  . SER A 1 920  ? 190.290 173.664 234.683 1.00 50.91  ? 931  SER A CA  1 
ATOM 2496 C C   . SER A 1 920  ? 189.852 172.300 235.210 1.00 55.89  ? 931  SER A C   1 
ATOM 2497 O O   . SER A 1 920  ? 188.652 172.052 235.374 1.00 57.77  ? 931  SER A O   1 
ATOM 2498 C CB  . SER A 1 920  ? 190.356 174.675 235.828 1.00 52.65  ? 931  SER A CB  1 
ATOM 2499 O OG  . SER A 1 920  ? 190.830 175.929 235.370 1.00 51.50  ? 931  SER A OG  1 
ATOM 2500 N N   . PRO A 1 921  ? 190.794 171.389 235.474 1.00 58.56  ? 932  PRO A N   1 
ATOM 2501 C CA  . PRO A 1 921  ? 190.408 170.033 235.896 1.00 60.74  ? 932  PRO A CA  1 
ATOM 2502 C C   . PRO A 1 921  ? 189.661 169.990 237.215 1.00 58.38  ? 932  PRO A C   1 
ATOM 2503 O O   . PRO A 1 921  ? 188.979 168.994 237.487 1.00 60.05  ? 932  PRO A O   1 
ATOM 2504 C CB  . PRO A 1 921  ? 191.754 169.300 235.995 1.00 60.54  ? 932  PRO A CB  1 
ATOM 2505 C CG  . PRO A 1 921  ? 192.756 170.388 236.222 1.00 56.17  ? 932  PRO A CG  1 
ATOM 2506 C CD  . PRO A 1 921  ? 192.256 171.560 235.428 1.00 57.34  ? 932  PRO A CD  1 
ATOM 2507 N N   . SER A 1 922  ? 189.766 171.029 238.043 1.00 56.26  ? 933  SER A N   1 
ATOM 2508 C CA  . SER A 1 922  ? 189.072 171.049 239.321 1.00 62.08  ? 933  SER A CA  1 
ATOM 2509 C C   . SER A 1 922  ? 187.574 171.290 239.186 1.00 62.84  ? 933  SER A C   1 
ATOM 2510 O O   . SER A 1 922  ? 186.809 170.778 240.011 1.00 61.88  ? 933  SER A O   1 
ATOM 2511 C CB  . SER A 1 922  ? 189.679 172.118 240.233 1.00 58.63  ? 933  SER A CB  1 
ATOM 2512 O OG  . SER A 1 922  ? 189.751 173.370 239.574 1.00 59.63  ? 933  SER A OG  1 
ATOM 2513 N N   . ASN A 1 923  ? 187.132 172.048 238.181 1.00 57.13  ? 934  ASN A N   1 
ATOM 2514 C CA  . ASN A 1 923  ? 185.719 172.393 238.098 1.00 52.76  ? 934  ASN A CA  1 
ATOM 2515 C C   . ASN A 1 923  ? 184.934 171.435 237.209 1.00 52.41  ? 934  ASN A C   1 
ATOM 2516 O O   . ASN A 1 923  ? 184.065 170.705 237.697 1.00 54.23  ? 934  ASN A O   1 
ATOM 2517 C CB  . ASN A 1 923  ? 185.562 173.824 237.577 1.00 46.63  ? 934  ASN A CB  1 
ATOM 2518 C CG  . ASN A 1 923  ? 185.963 174.863 238.602 1.00 48.37  ? 934  ASN A CG  1 
ATOM 2519 O OD1 . ASN A 1 923  ? 186.637 174.555 239.584 1.00 53.04  ? 934  ASN A OD1 1 
ATOM 2520 N ND2 . ASN A 1 923  ? 185.554 176.105 238.376 1.00 49.36  ? 934  ASN A ND2 1 
ATOM 2521 N N   . THR A 1 924  ? 185.233 171.417 235.909 1.00 50.51  ? 935  THR A N   1 
ATOM 2522 C CA  . THR A 1 924  ? 184.530 170.524 234.993 1.00 55.90  ? 935  THR A CA  1 
ATOM 2523 C C   . THR A 1 924  ? 185.467 169.686 234.135 1.00 58.95  ? 935  THR A C   1 
ATOM 2524 O O   . THR A 1 924  ? 185.208 168.494 233.933 1.00 60.25  ? 935  THR A O   1 
ATOM 2525 C CB  . THR A 1 924  ? 183.599 171.321 234.071 1.00 52.66  ? 935  THR A CB  1 
ATOM 2526 O OG1 . THR A 1 924  ? 184.379 172.106 233.161 1.00 54.56  ? 935  THR A OG1 1 
ATOM 2527 C CG2 . THR A 1 924  ? 182.682 172.236 234.872 1.00 47.26  ? 935  THR A CG2 1 
ATOM 2528 N N   . GLY A 1 925  ? 186.547 170.277 233.628 1.00 58.23  ? 936  GLY A N   1 
ATOM 2529 C CA  . GLY A 1 925  ? 187.443 169.583 232.728 1.00 53.46  ? 936  GLY A CA  1 
ATOM 2530 C C   . GLY A 1 925  ? 186.955 169.461 231.301 1.00 53.66  ? 936  GLY A C   1 
ATOM 2531 O O   . GLY A 1 925  ? 187.613 168.789 230.496 1.00 56.56  ? 936  GLY A O   1 
ATOM 2532 N N   . LYS A 1 926  ? 185.829 170.083 230.960 1.00 54.71  ? 937  LYS A N   1 
ATOM 2533 C CA  . LYS A 1 926  ? 185.253 169.937 229.631 1.00 57.75  ? 937  LYS A CA  1 
ATOM 2534 C C   . LYS A 1 926  ? 186.038 170.737 228.597 1.00 56.44  ? 937  LYS A C   1 
ATOM 2535 O O   . LYS A 1 926  ? 186.704 171.727 228.913 1.00 56.69  ? 937  LYS A O   1 
ATOM 2536 C CB  . LYS A 1 926  ? 183.792 170.385 229.632 1.00 53.88  ? 937  LYS A CB  1 
ATOM 2537 C CG  . LYS A 1 926  ? 182.850 169.421 230.328 1.00 54.08  ? 937  LYS A CG  1 
ATOM 2538 C CD  . LYS A 1 926  ? 181.415 169.909 230.252 1.00 54.34  ? 937  LYS A CD  1 
ATOM 2539 C CE  . LYS A 1 926  ? 180.464 168.919 230.898 1.00 58.87  ? 937  LYS A CE  1 
ATOM 2540 N NZ  . LYS A 1 926  ? 180.281 167.705 230.057 1.00 60.04  ? 937  LYS A NZ  1 
ATOM 2541 N N   . LYS A 1 927  ? 185.968 170.308 227.335 1.00 46.08  ? 938  LYS A N   1 
ATOM 2542 C CA  . LYS A 1 927  ? 186.709 171.015 226.258 1.00 38.28  ? 938  LYS A CA  1 
ATOM 2543 C C   . LYS A 1 927  ? 185.729 171.915 225.500 1.00 36.04  ? 938  LYS A C   1 
ATOM 2544 O O   . LYS A 1 927  ? 184.560 171.513 225.349 1.00 44.01  ? 938  LYS A O   1 
ATOM 2545 C CB  . LYS A 1 927  ? 187.367 170.011 225.310 1.00 44.97  ? 938  LYS A CB  1 
ATOM 2546 C CG  . LYS A 1 927  ? 188.520 169.211 225.891 1.00 50.76  ? 938  LYS A CG  1 
ATOM 2547 C CD  . LYS A 1 927  ? 189.014 168.140 224.927 1.00 56.01  ? 938  LYS A CD  1 
ATOM 2548 C CE  . LYS A 1 927  ? 189.611 168.718 223.685 1.00 56.68  ? 938  LYS A CE  1 
ATOM 2549 N NZ  . LYS A 1 927  ? 190.184 167.678 222.828 1.00 56.64  ? 938  LYS A NZ  1 
ATOM 2550 N N   . TRP A 1 928  ? 186.189 173.084 225.056 1.00 31.76  ? 939  TRP A N   1 
ATOM 2551 C CA  . TRP A 1 928  ? 185.289 174.029 224.351 1.00 29.80  ? 939  TRP A CA  1 
ATOM 2552 C C   . TRP A 1 928  ? 186.112 174.962 223.470 1.00 29.23  ? 939  TRP A C   1 
ATOM 2553 O O   . TRP A 1 928  ? 187.319 175.115 223.726 1.00 34.09  ? 939  TRP A O   1 
ATOM 2554 C CB  . TRP A 1 928  ? 184.427 174.797 225.362 1.00 28.36  ? 939  TRP A CB  1 
ATOM 2555 C CG  . TRP A 1 928  ? 184.908 176.174 225.736 1.00 30.74  ? 939  TRP A CG  1 
ATOM 2556 C CD1 . TRP A 1 928  ? 184.560 177.352 225.145 1.00 30.76  ? 939  TRP A CD1 1 
ATOM 2557 C CD2 . TRP A 1 928  ? 185.797 176.517 226.821 1.00 30.46  ? 939  TRP A CD2 1 
ATOM 2558 N NE1 . TRP A 1 928  ? 185.180 178.400 225.771 1.00 29.30  ? 939  TRP A NE1 1 
ATOM 2559 C CE2 . TRP A 1 928  ? 185.942 177.920 226.802 1.00 27.11  ? 939  TRP A CE2 1 
ATOM 2560 C CE3 . TRP A 1 928  ? 186.483 175.782 227.793 1.00 32.87  ? 939  TRP A CE3 1 
ATOM 2561 C CZ2 . TRP A 1 928  ? 186.745 178.595 227.717 1.00 23.23  ? 939  TRP A CZ2 1 
ATOM 2562 C CZ3 . TRP A 1 928  ? 187.274 176.452 228.698 1.00 30.51  ? 939  TRP A CZ3 1 
ATOM 2563 C CH2 . TRP A 1 928  ? 187.401 177.838 228.659 1.00 26.02  ? 939  TRP A CH2 1 
ATOM 2564 N N   . GLY A 1 929  ? 185.486 175.538 222.446 1.00 27.24  ? 940  GLY A N   1 
ATOM 2565 C CA  . GLY A 1 929  ? 186.189 176.485 221.565 1.00 30.79  ? 940  GLY A CA  1 
ATOM 2566 C C   . GLY A 1 929  ? 186.290 175.964 220.149 1.00 34.63  ? 940  GLY A C   1 
ATOM 2567 O O   . GLY A 1 929  ? 185.437 175.145 219.760 1.00 36.32  ? 940  GLY A O   1 
ATOM 2568 N N   . GLY A 1 930  ? 187.300 176.413 219.404 1.00 35.25  ? 941  GLY A N   1 
ATOM 2569 C CA  . GLY A 1 930  ? 187.461 176.006 218.022 1.00 33.26  ? 941  GLY A CA  1 
ATOM 2570 C C   . GLY A 1 930  ? 186.359 176.503 217.111 1.00 35.91  ? 941  GLY A C   1 
ATOM 2571 O O   . GLY A 1 930  ? 185.602 175.705 216.548 1.00 39.56  ? 941  GLY A O   1 
ATOM 2572 N N   . VAL A 1 931  ? 186.256 177.822 216.956 1.00 39.40  ? 942  VAL A N   1 
ATOM 2573 C CA  . VAL A 1 931  ? 185.196 178.402 216.140 1.00 33.79  ? 942  VAL A CA  1 
ATOM 2574 C C   . VAL A 1 931  ? 185.573 178.310 214.667 1.00 32.92  ? 942  VAL A C   1 
ATOM 2575 O O   . VAL A 1 931  ? 186.662 178.732 214.258 1.00 36.20  ? 942  VAL A O   1 
ATOM 2576 C CB  . VAL A 1 931  ? 184.930 179.855 216.557 1.00 28.00  ? 942  VAL A CB  1 
ATOM 2577 C CG1 . VAL A 1 931  ? 183.858 180.471 215.674 1.00 30.54  ? 942  VAL A CG1 1 
ATOM 2578 C CG2 . VAL A 1 931  ? 184.521 179.917 218.020 1.00 29.90  ? 942  VAL A CG2 1 
ATOM 2579 N N   . ARG A 1 932  ? 184.668 177.759 213.865 1.00 36.10  ? 943  ARG A N   1 
ATOM 2580 C CA  . ARG A 1 932  ? 184.827 177.662 212.420 1.00 36.44  ? 943  ARG A CA  1 
ATOM 2581 C C   . ARG A 1 932  ? 183.785 178.538 211.739 1.00 37.37  ? 943  ARG A C   1 
ATOM 2582 O O   . ARG A 1 932  ? 182.597 178.475 212.077 1.00 42.12  ? 943  ARG A O   1 
ATOM 2583 C CB  . ARG A 1 932  ? 184.686 176.215 211.943 1.00 39.20  ? 943  ARG A CB  1 
ATOM 2584 C CG  . ARG A 1 932  ? 185.517 175.205 212.713 1.00 40.42  ? 943  ARG A CG  1 
ATOM 2585 C CD  . ARG A 1 932  ? 186.993 175.559 212.676 1.00 38.11  ? 943  ARG A CD  1 
ATOM 2586 N NE  . ARG A 1 932  ? 187.787 174.679 213.524 1.00 39.48  ? 943  ARG A NE  1 
ATOM 2587 C CZ  . ARG A 1 932  ? 188.803 175.078 214.276 1.00 41.37  ? 943  ARG A CZ  1 
ATOM 2588 N NH1 . ARG A 1 932  ? 189.182 176.344 214.310 1.00 36.56  ? 943  ARG A NH1 1 
ATOM 2589 N NH2 . ARG A 1 932  ? 189.456 174.183 215.012 1.00 45.99  ? 943  ARG A NH2 1 
ATOM 2590 N N   . ALA A 1 933  ? 184.236 179.352 210.787 1.00 35.62  ? 944  ALA A N   1 
ATOM 2591 C CA  . ALA A 1 933  ? 183.353 180.207 210.009 1.00 40.09  ? 944  ALA A CA  1 
ATOM 2592 C C   . ALA A 1 933  ? 183.239 179.664 208.592 1.00 43.05  ? 944  ALA A C   1 
ATOM 2593 O O   . ALA A 1 933  ? 184.242 179.546 207.884 1.00 49.74  ? 944  ALA A O   1 
ATOM 2594 C CB  . ALA A 1 933  ? 183.880 181.641 209.980 1.00 42.17  ? 944  ALA A CB  1 
ATOM 2595 N N   . ASP A 1 934  ? 182.018 179.339 208.180 1.00 43.95  ? 945  ASP A N   1 
ATOM 2596 C CA  . ASP A 1 934  ? 181.769 178.823 206.842 1.00 45.55  ? 945  ASP A CA  1 
ATOM 2597 C C   . ASP A 1 934  ? 180.686 179.657 206.176 1.00 43.84  ? 945  ASP A C   1 
ATOM 2598 O O   . ASP A 1 934  ? 179.649 179.934 206.780 1.00 48.46  ? 945  ASP A O   1 
ATOM 2599 C CB  . ASP A 1 934  ? 181.363 177.342 206.880 1.00 46.25  ? 945  ASP A CB  1 
ATOM 2600 C CG  . ASP A 1 934  ? 180.051 177.113 207.603 1.00 47.60  ? 945  ASP A CG  1 
ATOM 2601 O OD1 . ASP A 1 934  ? 178.992 177.150 206.942 1.00 47.81  ? 945  ASP A OD1 1 
ATOM 2602 O OD2 . ASP A 1 934  ? 180.079 176.898 208.833 1.00 49.13  ? 945  ASP A OD2 1 
ATOM 2603 N N   . GLY A 1 935  ? 180.930 180.068 204.937 1.00 40.98  ? 946  GLY A N   1 
ATOM 2604 C CA  . GLY A 1 935  ? 179.972 180.926 204.267 1.00 41.87  ? 946  GLY A CA  1 
ATOM 2605 C C   . GLY A 1 935  ? 180.406 181.265 202.856 1.00 43.96  ? 946  GLY A C   1 
ATOM 2606 O O   . GLY A 1 935  ? 181.203 180.551 202.241 1.00 50.23  ? 946  GLY A O   1 
ATOM 2607 N N   . VAL A 1 936  ? 179.845 182.368 202.353 1.00 40.07  ? 947  VAL A N   1 
ATOM 2608 C CA  . VAL A 1 936  ? 180.010 182.778 200.965 1.00 40.53  ? 947  VAL A CA  1 
ATOM 2609 C C   . VAL A 1 936  ? 180.400 184.249 200.906 1.00 42.28  ? 947  VAL A C   1 
ATOM 2610 O O   . VAL A 1 936  ? 180.227 185.004 201.865 1.00 50.15  ? 947  VAL A O   1 
ATOM 2611 C CB  . VAL A 1 936  ? 178.732 182.540 200.129 1.00 36.22  ? 947  VAL A CB  1 
ATOM 2612 C CG1 . VAL A 1 936  ? 178.364 181.065 200.121 1.00 39.38  ? 947  VAL A CG1 1 
ATOM 2613 C CG2 . VAL A 1 936  ? 177.584 183.377 200.668 1.00 33.73  ? 947  VAL A CG2 1 
ATOM 2614 N N   . GLY A 1 937  ? 180.940 184.644 199.755 1.00 40.32  ? 948  GLY A N   1 
ATOM 2615 C CA  . GLY A 1 937  ? 181.325 186.025 199.532 1.00 42.05  ? 948  GLY A CA  1 
ATOM 2616 C C   . GLY A 1 937  ? 181.296 186.367 198.058 1.00 44.51  ? 948  GLY A C   1 
ATOM 2617 O O   . GLY A 1 937  ? 181.508 185.512 197.192 1.00 52.61  ? 948  GLY A O   1 
ATOM 2618 N N   . LEU A 1 938  ? 180.965 187.636 197.792 1.00 40.26  ? 949  LEU A N   1 
ATOM 2619 C CA  . LEU A 1 938  ? 180.910 188.155 196.404 1.00 41.54  ? 949  LEU A CA  1 
ATOM 2620 C C   . LEU A 1 938  ? 181.607 189.518 196.397 1.00 44.98  ? 949  LEU A C   1 
ATOM 2621 O O   . LEU A 1 938  ? 181.291 190.338 197.281 1.00 50.73  ? 949  LEU A O   1 
ATOM 2622 C CB  . LEU A 1 938  ? 179.463 188.278 195.934 1.00 42.79  ? 949  LEU A CB  1 
ATOM 2623 C CG  . LEU A 1 938  ? 179.199 189.303 194.827 1.00 47.73  ? 949  LEU A CG  1 
ATOM 2624 C CD1 . LEU A 1 938  ? 179.815 188.892 193.503 1.00 46.39  ? 949  LEU A CD1 1 
ATOM 2625 C CD2 . LEU A 1 938  ? 177.713 189.565 194.667 1.00 45.08  ? 949  LEU A CD2 1 
ATOM 2626 N N   . SER A 1 939  ? 182.501 189.755 195.443 1.00 46.14  ? 950  SER A N   1 
ATOM 2627 C CA  . SER A 1 939  ? 183.271 190.986 195.351 1.00 50.02  ? 950  SER A CA  1 
ATOM 2628 C C   . SER A 1 939  ? 183.249 191.518 193.926 1.00 51.23  ? 950  SER A C   1 
ATOM 2629 O O   . SER A 1 939  ? 183.190 190.745 192.965 1.00 54.99  ? 950  SER A O   1 
ATOM 2630 C CB  . SER A 1 939  ? 184.721 190.766 195.799 1.00 53.36  ? 950  SER A CB  1 
ATOM 2631 O OG  . SER A 1 939  ? 185.496 191.938 195.614 1.00 56.68  ? 950  SER A OG  1 
ATOM 2632 N N   . LEU A 1 940  ? 183.301 192.844 193.802 1.00 51.56  ? 951  LEU A N   1 
ATOM 2633 C CA  . LEU A 1 940  ? 183.354 193.532 192.520 1.00 52.25  ? 951  LEU A CA  1 
ATOM 2634 C C   . LEU A 1 940  ? 184.497 194.535 192.537 1.00 55.01  ? 951  LEU A C   1 
ATOM 2635 O O   . LEU A 1 940  ? 184.887 195.036 193.595 1.00 65.43  ? 951  LEU A O   1 
ATOM 2636 C CB  . LEU A 1 940  ? 182.041 194.266 192.207 1.00 49.31  ? 951  LEU A CB  1 
ATOM 2637 C CG  . LEU A 1 940  ? 180.742 193.464 192.166 1.00 50.80  ? 951  LEU A CG  1 
ATOM 2638 C CD1 . LEU A 1 940  ? 180.037 193.543 193.508 1.00 56.08  ? 951  LEU A CD1 1 
ATOM 2639 C CD2 . LEU A 1 940  ? 179.839 193.969 191.054 1.00 57.22  ? 951  LEU A CD2 1 
ATOM 2640 N N   . SER A 1 941  ? 185.031 194.830 191.354 1.00 52.82  ? 952  SER A N   1 
ATOM 2641 C CA  . SER A 1 941  ? 186.120 195.788 191.245 1.00 55.38  ? 952  SER A CA  1 
ATOM 2642 C C   . SER A 1 941  ? 186.081 196.454 189.878 1.00 64.11  ? 952  SER A C   1 
ATOM 2643 O O   . SER A 1 941  ? 185.562 195.899 188.904 1.00 73.36  ? 952  SER A O   1 
ATOM 2644 C CB  . SER A 1 941  ? 187.482 195.121 191.473 1.00 53.19  ? 952  SER A CB  1 
ATOM 2645 O OG  . SER A 1 941  ? 187.719 194.103 190.517 1.00 59.71  ? 952  SER A OG  1 
ATOM 2646 N N   . TYR A 1 942  ? 186.645 197.660 189.821 1.00 61.90  ? 953  TYR A N   1 
ATOM 2647 C CA  . TYR A 1 942  ? 186.761 198.414 188.578 1.00 64.77  ? 953  TYR A CA  1 
ATOM 2648 C C   . TYR A 1 942  ? 188.076 199.175 188.602 1.00 69.72  ? 953  TYR A C   1 
ATOM 2649 O O   . TYR A 1 942  ? 188.279 200.041 189.461 1.00 73.80  ? 953  TYR A O   1 
ATOM 2650 C CB  . TYR A 1 942  ? 185.583 199.375 188.393 1.00 70.26  ? 953  TYR A CB  1 
ATOM 2651 C CG  . TYR A 1 942  ? 185.803 200.411 187.311 1.00 79.74  ? 953  TYR A CG  1 
ATOM 2652 C CD1 . TYR A 1 942  ? 185.532 200.120 185.981 1.00 90.96  ? 953  TYR A CD1 1 
ATOM 2653 C CD2 . TYR A 1 942  ? 186.269 201.683 187.621 1.00 75.05  ? 953  TYR A CD2 1 
ATOM 2654 C CE1 . TYR A 1 942  ? 185.730 201.063 184.988 1.00 91.81  ? 953  TYR A CE1 1 
ATOM 2655 C CE2 . TYR A 1 942  ? 186.470 202.631 186.637 1.00 82.00  ? 953  TYR A CE2 1 
ATOM 2656 C CZ  . TYR A 1 942  ? 186.198 202.316 185.322 1.00 88.34  ? 953  TYR A CZ  1 
ATOM 2657 O OH  . TYR A 1 942  ? 186.396 203.258 184.339 1.00 84.07  ? 953  TYR A OH  1 
ATOM 2658 N N   . ASP A 1 943  ? 188.961 198.844 187.662 1.00 75.13  ? 954  ASP A N   1 
ATOM 2659 C CA  . ASP A 1 943  ? 190.231 199.550 187.510 1.00 78.64  ? 954  ASP A CA  1 
ATOM 2660 C C   . ASP A 1 943  ? 190.725 199.294 186.092 1.00 82.87  ? 954  ASP A C   1 
ATOM 2661 O O   . ASP A 1 943  ? 191.078 198.159 185.758 1.00 83.44  ? 954  ASP A O   1 
ATOM 2662 C CB  . ASP A 1 943  ? 191.247 199.081 188.546 1.00 78.02  ? 954  ASP A CB  1 
ATOM 2663 C CG  . ASP A 1 943  ? 192.435 200.019 188.669 1.00 82.61  ? 954  ASP A CG  1 
ATOM 2664 O OD1 . ASP A 1 943  ? 192.793 200.678 187.670 1.00 86.75  ? 954  ASP A OD1 1 
ATOM 2665 O OD2 . ASP A 1 943  ? 193.016 200.097 189.772 1.00 80.40  ? 954  ASP A OD2 1 
ATOM 2666 N N   . LYS A 1 944  ? 190.749 200.340 185.269 1.00 87.50  ? 955  LYS A N   1 
ATOM 2667 C CA  . LYS A 1 944  ? 191.195 200.241 183.886 1.00 88.69  ? 955  LYS A CA  1 
ATOM 2668 C C   . LYS A 1 944  ? 192.614 200.754 183.683 1.00 90.58  ? 955  LYS A C   1 
ATOM 2669 O O   . LYS A 1 944  ? 193.013 200.998 182.540 1.00 92.91  ? 955  LYS A O   1 
ATOM 2670 C CB  . LYS A 1 944  ? 190.234 200.998 182.966 1.00 88.29  ? 955  LYS A CB  1 
ATOM 2671 C CG  . LYS A 1 944  ? 188.807 200.490 183.017 1.00 92.09  ? 955  LYS A CG  1 
ATOM 2672 C CD  . LYS A 1 944  ? 188.749 199.015 182.658 1.00 93.54  ? 955  LYS A CD  1 
ATOM 2673 C CE  . LYS A 1 944  ? 187.481 198.369 183.181 1.00 93.02  ? 955  LYS A CE  1 
ATOM 2674 N NZ  . LYS A 1 944  ? 186.330 198.573 182.259 1.00 92.28  ? 955  LYS A NZ  1 
ATOM 2675 N N   . GLY A 1 945  ? 193.381 200.924 184.758 1.00 87.78  ? 956  GLY A N   1 
ATOM 2676 C CA  . GLY A 1 945  ? 194.717 201.465 184.666 1.00 87.16  ? 956  GLY A CA  1 
ATOM 2677 C C   . GLY A 1 945  ? 194.799 202.972 184.757 1.00 89.63  ? 956  GLY A C   1 
ATOM 2678 O O   . GLY A 1 945  ? 195.911 203.515 184.775 1.00 91.04  ? 956  GLY A O   1 
ATOM 2679 N N   . GLU A 1 946  ? 193.664 203.664 184.812 1.00 86.28  ? 957  GLU A N   1 
ATOM 2680 C CA  . GLU A 1 946  ? 193.665 205.112 184.933 1.00 82.45  ? 957  GLU A CA  1 
ATOM 2681 C C   . GLU A 1 946  ? 193.897 205.519 186.388 1.00 79.29  ? 957  GLU A C   1 
ATOM 2682 O O   . GLU A 1 946  ? 194.252 204.706 187.246 1.00 77.86  ? 957  GLU A O   1 
ATOM 2683 C CB  . GLU A 1 946  ? 192.357 205.690 184.397 1.00 81.07  ? 957  GLU A CB  1 
ATOM 2684 C CG  . GLU A 1 946  ? 192.258 205.699 182.878 1.00 92.81  ? 957  GLU A CG  1 
ATOM 2685 C CD  . GLU A 1 946  ? 193.324 206.560 182.224 1.00 89.72  ? 957  GLU A CD  1 
ATOM 2686 O OE1 . GLU A 1 946  ? 193.715 207.586 182.822 1.00 88.36  ? 957  GLU A OE1 1 
ATOM 2687 O OE2 . GLU A 1 946  ? 193.772 206.211 181.112 1.00 83.04  ? 957  GLU A OE2 1 
ATOM 2688 N N   . ALA A 1 947  ? 193.688 206.807 186.665 1.00 76.50  ? 958  ALA A N   1 
ATOM 2689 C CA  . ALA A 1 947  ? 194.019 207.355 187.975 1.00 68.43  ? 958  ALA A CA  1 
ATOM 2690 C C   . ALA A 1 947  ? 193.079 206.881 189.077 1.00 62.10  ? 958  ALA A C   1 
ATOM 2691 O O   . ALA A 1 947  ? 193.447 206.949 190.254 1.00 64.30  ? 958  ALA A O   1 
ATOM 2692 C CB  . ALA A 1 947  ? 194.017 208.883 187.912 1.00 66.23  ? 958  ALA A CB  1 
ATOM 2693 N N   . ASN A 1 948  ? 191.886 206.401 188.735 1.00 55.47  ? 959  ASN A N   1 
ATOM 2694 C CA  . ASN A 1 948  ? 190.872 206.064 189.724 1.00 52.97  ? 959  ASN A CA  1 
ATOM 2695 C C   . ASN A 1 948  ? 190.580 204.569 189.712 1.00 58.39  ? 959  ASN A C   1 
ATOM 2696 O O   . ASN A 1 948  ? 190.662 203.911 188.670 1.00 68.73  ? 959  ASN A O   1 
ATOM 2697 C CB  . ASN A 1 948  ? 189.576 206.843 189.470 1.00 56.00  ? 959  ASN A CB  1 
ATOM 2698 C CG  . ASN A 1 948  ? 189.710 208.319 189.789 1.00 57.14  ? 959  ASN A CG  1 
ATOM 2699 O OD1 . ASN A 1 948  ? 189.554 208.734 190.936 1.00 61.17  ? 959  ASN A OD1 1 
ATOM 2700 N ND2 . ASN A 1 948  ? 190.004 209.120 188.771 1.00 53.70  ? 959  ASN A ND2 1 
ATOM 2701 N N   . GLY A 1 949  ? 190.237 204.040 190.885 1.00 56.46  ? 960  GLY A N   1 
ATOM 2702 C CA  . GLY A 1 949  ? 189.834 202.650 190.990 1.00 59.29  ? 960  GLY A CA  1 
ATOM 2703 C C   . GLY A 1 949  ? 188.914 202.442 192.169 1.00 55.76  ? 960  GLY A C   1 
ATOM 2704 O O   . GLY A 1 949  ? 189.010 203.135 193.188 1.00 57.65  ? 960  GLY A O   1 
ATOM 2705 N N   . VAL A 1 950  ? 188.000 201.477 192.019 1.00 55.10  ? 961  VAL A N   1 
ATOM 2706 C CA  . VAL A 1 950  ? 186.999 201.187 193.040 1.00 48.30  ? 961  VAL A CA  1 
ATOM 2707 C C   . VAL A 1 950  ? 186.926 199.682 193.262 1.00 53.31  ? 961  VAL A C   1 
ATOM 2708 O O   . VAL A 1 950  ? 187.221 198.884 192.371 1.00 61.64  ? 961  VAL A O   1 
ATOM 2709 C CB  . VAL A 1 950  ? 185.596 201.731 192.666 1.00 46.84  ? 961  VAL A CB  1 
ATOM 2710 C CG1 . VAL A 1 950  ? 184.735 201.902 193.910 1.00 49.60  ? 961  VAL A CG1 1 
ATOM 2711 C CG2 . VAL A 1 950  ? 185.699 203.044 191.904 1.00 49.28  ? 961  VAL A CG2 1 
ATOM 2712 N N   . TRP A 1 951  ? 186.517 199.296 194.471 1.00 48.76  ? 962  TRP A N   1 
ATOM 2713 C CA  . TRP A 1 951  ? 186.284 197.893 194.783 1.00 48.91  ? 962  TRP A CA  1 
ATOM 2714 C C   . TRP A 1 951  ? 185.276 197.795 195.919 1.00 48.06  ? 962  TRP A C   1 
ATOM 2715 O O   . TRP A 1 951  ? 185.132 198.714 196.729 1.00 56.01  ? 962  TRP A O   1 
ATOM 2716 C CB  . TRP A 1 951  ? 187.585 197.171 195.157 1.00 48.96  ? 962  TRP A CB  1 
ATOM 2717 C CG  . TRP A 1 951  ? 188.168 197.612 196.463 1.00 51.89  ? 962  TRP A CG  1 
ATOM 2718 C CD1 . TRP A 1 951  ? 189.017 198.658 196.671 1.00 56.17  ? 962  TRP A CD1 1 
ATOM 2719 C CD2 . TRP A 1 951  ? 187.952 197.009 197.745 1.00 54.35  ? 962  TRP A CD2 1 
ATOM 2720 N NE1 . TRP A 1 951  ? 189.339 198.749 198.004 1.00 60.11  ? 962  TRP A NE1 1 
ATOM 2721 C CE2 . TRP A 1 951  ? 188.698 197.748 198.684 1.00 57.22  ? 962  TRP A CE2 1 
ATOM 2722 C CE3 . TRP A 1 951  ? 187.198 195.920 198.190 1.00 53.96  ? 962  TRP A CE3 1 
ATOM 2723 C CZ2 . TRP A 1 951  ? 188.712 197.432 200.041 1.00 53.37  ? 962  TRP A CZ2 1 
ATOM 2724 C CZ3 . TRP A 1 951  ? 187.213 195.607 199.537 1.00 56.46  ? 962  TRP A CZ3 1 
ATOM 2725 C CH2 . TRP A 1 951  ? 187.965 196.360 200.447 1.00 53.99  ? 962  TRP A CH2 1 
ATOM 2726 N N   . ALA A 1 952  ? 184.581 196.661 195.972 1.00 45.54  ? 963  ALA A N   1 
ATOM 2727 C CA  . ALA A 1 952  ? 183.597 196.397 197.012 1.00 46.45  ? 963  ALA A CA  1 
ATOM 2728 C C   . ALA A 1 952  ? 183.484 194.894 197.220 1.00 48.58  ? 963  ALA A C   1 
ATOM 2729 O O   . ALA A 1 952  ? 183.833 194.099 196.345 1.00 53.39  ? 963  ALA A O   1 
ATOM 2730 C CB  . ALA A 1 952  ? 182.227 196.992 196.662 1.00 46.09  ? 963  ALA A CB  1 
ATOM 2731 N N   . SER A 1 953  ? 182.979 194.510 198.390 1.00 45.75  ? 964  SER A N   1 
ATOM 2732 C CA  . SER A 1 953  ? 182.859 193.104 198.745 1.00 46.73  ? 964  SER A CA  1 
ATOM 2733 C C   . SER A 1 953  ? 181.783 192.933 199.808 1.00 43.29  ? 964  SER A C   1 
ATOM 2734 O O   . SER A 1 953  ? 181.590 193.808 200.659 1.00 47.76  ? 964  SER A O   1 
ATOM 2735 C CB  . SER A 1 953  ? 184.192 192.543 199.253 1.00 49.81  ? 964  SER A CB  1 
ATOM 2736 O OG  . SER A 1 953  ? 184.094 191.155 199.520 1.00 54.88  ? 964  SER A OG  1 
ATOM 2737 N N   . LEU A 1 954  ? 181.092 191.797 199.751 1.00 38.87  ? 965  LEU A N   1 
ATOM 2738 C CA  . LEU A 1 954  ? 180.085 191.429 200.733 1.00 37.71  ? 965  LEU A CA  1 
ATOM 2739 C C   . LEU A 1 954  ? 180.272 189.959 201.070 1.00 39.58  ? 965  LEU A C   1 
ATOM 2740 O O   . LEU A 1 954  ? 180.663 189.166 200.211 1.00 45.41  ? 965  LEU A O   1 
ATOM 2741 C CB  . LEU A 1 954  ? 178.667 191.692 200.205 1.00 40.87  ? 965  LEU A CB  1 
ATOM 2742 C CG  . LEU A 1 954  ? 177.483 191.460 201.148 1.00 44.95  ? 965  LEU A CG  1 
ATOM 2743 C CD1 . LEU A 1 954  ? 176.420 192.523 200.926 1.00 47.78  ? 965  LEU A CD1 1 
ATOM 2744 C CD2 . LEU A 1 954  ? 176.892 190.071 200.954 1.00 41.17  ? 965  LEU A CD2 1 
ATOM 2745 N N   . SER A 1 955  ? 180.018 189.600 202.325 1.00 38.16  ? 966  SER A N   1 
ATOM 2746 C CA  . SER A 1 955  ? 180.209 188.229 202.771 1.00 40.87  ? 966  SER A CA  1 
ATOM 2747 C C   . SER A 1 955  ? 179.169 187.872 203.821 1.00 39.63  ? 966  SER A C   1 
ATOM 2748 O O   . SER A 1 955  ? 178.705 188.729 204.578 1.00 42.53  ? 966  SER A O   1 
ATOM 2749 C CB  . SER A 1 955  ? 181.618 188.014 203.338 1.00 47.00  ? 966  SER A CB  1 
ATOM 2750 O OG  . SER A 1 955  ? 181.895 186.634 203.503 1.00 50.76  ? 966  SER A OG  1 
ATOM 2751 N N   . GLY A 1 956  ? 178.818 186.590 203.861 1.00 40.69  ? 967  GLY A N   1 
ATOM 2752 C CA  . GLY A 1 956  ? 177.915 186.064 204.866 1.00 39.14  ? 967  GLY A CA  1 
ATOM 2753 C C   . GLY A 1 956  ? 178.386 184.719 205.374 1.00 43.85  ? 967  GLY A C   1 
ATOM 2754 O O   . GLY A 1 956  ? 178.564 183.783 204.586 1.00 55.22  ? 967  GLY A O   1 
ATOM 2755 N N   . ASP A 1 957  ? 178.605 184.612 206.686 1.00 35.36  ? 968  ASP A N   1 
ATOM 2756 C CA  . ASP A 1 957  ? 179.205 183.427 207.285 1.00 39.30  ? 968  ASP A CA  1 
ATOM 2757 C C   . ASP A 1 957  ? 178.366 182.942 208.458 1.00 36.18  ? 968  ASP A C   1 
ATOM 2758 O O   . ASP A 1 957  ? 177.677 183.730 209.108 1.00 43.08  ? 968  ASP A O   1 
ATOM 2759 C CB  . ASP A 1 957  ? 180.637 183.699 207.784 1.00 45.45  ? 968  ASP A CB  1 
ATOM 2760 C CG  . ASP A 1 957  ? 181.561 184.222 206.695 1.00 54.13  ? 968  ASP A CG  1 
ATOM 2761 O OD1 . ASP A 1 957  ? 181.183 184.207 205.508 1.00 58.51  ? 968  ASP A OD1 1 
ATOM 2762 O OD2 . ASP A 1 957  ? 182.681 184.658 207.037 1.00 51.91  ? 968  ASP A OD2 1 
ATOM 2763 N N   . GLN A 1 958  ? 178.423 181.637 208.711 1.00 34.31  ? 969  GLN A N   1 
ATOM 2764 C CA  . GLN A 1 958  ? 177.942 181.051 209.951 1.00 32.95  ? 969  GLN A CA  1 
ATOM 2765 C C   . GLN A 1 958  ? 179.136 180.612 210.787 1.00 43.51  ? 969  GLN A C   1 
ATOM 2766 O O   . GLN A 1 958  ? 180.089 180.020 210.269 1.00 51.47  ? 969  GLN A O   1 
ATOM 2767 C CB  . GLN A 1 958  ? 177.027 179.857 209.673 1.00 35.70  ? 969  GLN A CB  1 
ATOM 2768 C CG  . GLN A 1 958  ? 175.699 180.222 209.034 1.00 47.50  ? 969  GLN A CG  1 
ATOM 2769 C CD  . GLN A 1 958  ? 174.785 179.023 208.860 1.00 54.32  ? 969  GLN A CD  1 
ATOM 2770 O OE1 . GLN A 1 958  ? 175.143 177.898 209.211 1.00 52.43  ? 969  GLN A OE1 1 
ATOM 2771 N NE2 . GLN A 1 958  ? 173.598 179.258 208.314 1.00 53.09  ? 969  GLN A NE2 1 
ATOM 2772 N N   . LEU A 1 959  ? 179.084 180.914 212.083 1.00 41.57  ? 970  LEU A N   1 
ATOM 2773 C CA  . LEU A 1 959  ? 180.168 180.642 213.017 1.00 33.59  ? 970  LEU A CA  1 
ATOM 2774 C C   . LEU A 1 959  ? 179.697 179.576 213.993 1.00 37.67  ? 970  LEU A C   1 
ATOM 2775 O O   . LEU A 1 959  ? 178.769 179.816 214.776 1.00 44.33  ? 970  LEU A O   1 
ATOM 2776 C CB  . LEU A 1 959  ? 180.571 181.914 213.767 1.00 27.82  ? 970  LEU A CB  1 
ATOM 2777 C CG  . LEU A 1 959  ? 180.433 183.238 213.011 1.00 32.53  ? 970  LEU A CG  1 
ATOM 2778 C CD1 . LEU A 1 959  ? 180.716 184.414 213.928 1.00 37.64  ? 970  LEU A CD1 1 
ATOM 2779 C CD2 . LEU A 1 959  ? 181.347 183.284 211.803 1.00 33.26  ? 970  LEU A CD2 1 
ATOM 2780 N N   . THR A 1 960  ? 180.327 178.404 213.943 1.00 42.61  ? 971  THR A N   1 
ATOM 2781 C CA  . THR A 1 960  ? 179.947 177.296 214.809 1.00 47.46  ? 971  THR A CA  1 
ATOM 2782 C C   . THR A 1 960  ? 181.200 176.617 215.339 1.00 44.68  ? 971  THR A C   1 
ATOM 2783 O O   . THR A 1 960  ? 182.200 176.489 214.630 1.00 47.91  ? 971  THR A O   1 
ATOM 2784 C CB  . THR A 1 960  ? 179.072 176.269 214.078 1.00 59.12  ? 971  THR A CB  1 
ATOM 2785 O OG1 . THR A 1 960  ? 179.715 175.869 212.861 1.00 55.03  ? 971  THR A OG1 1 
ATOM 2786 C CG2 . THR A 1 960  ? 177.700 176.851 213.761 1.00 56.85  ? 971  THR A CG2 1 
ATOM 2787 N N   . GLY A 1 961  ? 181.129 176.163 216.589 1.00 38.81  ? 972  GLY A N   1 
ATOM 2788 C CA  . GLY A 1 961  ? 182.270 175.527 217.218 1.00 36.73  ? 972  GLY A CA  1 
ATOM 2789 C C   . GLY A 1 961  ? 181.904 174.446 218.214 1.00 40.59  ? 972  GLY A C   1 
ATOM 2790 O O   . GLY A 1 961  ? 180.728 174.105 218.371 1.00 47.82  ? 972  GLY A O   1 
ATOM 2791 N N   . LYS A 1 962  ? 182.909 173.900 218.894 1.00 34.12  ? 973  LYS A N   1 
ATOM 2792 C CA  . LYS A 1 962  ? 182.696 172.838 219.869 1.00 29.46  ? 973  LYS A CA  1 
ATOM 2793 C C   . LYS A 1 962  ? 182.276 173.445 221.202 1.00 32.66  ? 973  LYS A C   1 
ATOM 2794 O O   . LYS A 1 962  ? 183.050 174.180 221.825 1.00 35.91  ? 973  LYS A O   1 
ATOM 2795 C CB  . LYS A 1 962  ? 183.966 172.007 220.031 1.00 29.51  ? 973  LYS A CB  1 
ATOM 2796 C CG  . LYS A 1 962  ? 183.868 170.913 221.079 1.00 31.83  ? 973  LYS A CG  1 
ATOM 2797 C CD  . LYS A 1 962  ? 182.846 169.862 220.687 1.00 41.55  ? 973  LYS A CD  1 
ATOM 2798 C CE  . LYS A 1 962  ? 182.749 168.773 221.741 1.00 44.15  ? 973  LYS A CE  1 
ATOM 2799 N NZ  . LYS A 1 962  ? 183.938 167.879 221.715 1.00 46.32  ? 973  LYS A NZ  1 
ATOM 2800 N N   . ASN A 1 963  ? 181.055 173.128 221.640 1.00 36.23  ? 974  ASN A N   1 
ATOM 2801 C CA  . ASN A 1 963  ? 180.489 173.667 222.878 1.00 33.17  ? 974  ASN A CA  1 
ATOM 2802 C C   . ASN A 1 963  ? 180.495 175.194 222.869 1.00 32.14  ? 974  ASN A C   1 
ATOM 2803 O O   . ASN A 1 963  ? 180.728 175.845 223.890 1.00 33.13  ? 974  ASN A O   1 
ATOM 2804 C CB  . ASN A 1 963  ? 181.223 173.123 224.105 1.00 34.21  ? 974  ASN A CB  1 
ATOM 2805 C CG  . ASN A 1 963  ? 181.037 171.630 224.281 1.00 36.06  ? 974  ASN A CG  1 
ATOM 2806 O OD1 . ASN A 1 963  ? 179.986 171.081 223.953 1.00 36.05  ? 974  ASN A OD1 1 
ATOM 2807 N ND2 . ASN A 1 963  ? 182.061 170.964 224.802 1.00 41.21  ? 974  ASN A ND2 1 
ATOM 2808 N N   . VAL A 1 964  ? 180.234 175.770 221.699 1.00 32.93  ? 975  VAL A N   1 
ATOM 2809 C CA  . VAL A 1 964  ? 180.184 177.214 221.511 1.00 34.17  ? 975  VAL A CA  1 
ATOM 2810 C C   . VAL A 1 964  ? 178.831 177.570 220.911 1.00 48.50  ? 975  VAL A C   1 
ATOM 2811 O O   . VAL A 1 964  ? 178.333 176.866 220.026 1.00 56.74  ? 975  VAL A O   1 
ATOM 2812 C CB  . VAL A 1 964  ? 181.333 177.715 220.611 1.00 30.38  ? 975  VAL A CB  1 
ATOM 2813 C CG1 . VAL A 1 964  ? 181.249 179.221 220.417 1.00 27.81  ? 975  VAL A CG1 1 
ATOM 2814 C CG2 . VAL A 1 964  ? 182.678 177.331 221.203 1.00 34.47  ? 975  VAL A CG2 1 
ATOM 2815 N N   . GLU A 1 965  ? 178.235 178.652 221.407 1.00 46.66  ? 976  GLU A N   1 
ATOM 2816 C CA  . GLU A 1 965  ? 176.935 179.086 220.913 1.00 49.40  ? 976  GLU A CA  1 
ATOM 2817 C C   . GLU A 1 965  ? 177.006 179.409 219.425 1.00 54.01  ? 976  GLU A C   1 
ATOM 2818 O O   . GLU A 1 965  ? 177.968 180.017 218.948 1.00 58.45  ? 976  GLU A O   1 
ATOM 2819 C CB  . GLU A 1 965  ? 176.457 180.309 221.698 1.00 47.72  ? 976  GLU A CB  1 
ATOM 2820 C CG  . GLU A 1 965  ? 175.046 180.793 221.363 1.00 57.17  ? 976  GLU A CG  1 
ATOM 2821 C CD  . GLU A 1 965  ? 173.958 179.791 221.717 1.00 67.04  ? 976  GLU A CD  1 
ATOM 2822 O OE1 . GLU A 1 965  ? 173.144 180.099 222.613 1.00 70.16  ? 976  GLU A OE1 1 
ATOM 2823 O OE2 . GLU A 1 965  ? 173.892 178.712 221.091 1.00 67.27  ? 976  GLU A OE2 1 
ATOM 2824 N N   . ASP A 1 966  ? 175.978 178.990 218.691 1.00 52.08  ? 977  ASP A N   1 
ATOM 2825 C CA  . ASP A 1 966  ? 175.927 179.202 217.251 1.00 56.81  ? 977  ASP A CA  1 
ATOM 2826 C C   . ASP A 1 966  ? 175.755 180.684 216.944 1.00 52.08  ? 977  ASP A C   1 
ATOM 2827 O O   . ASP A 1 966  ? 175.063 181.401 217.673 1.00 52.21  ? 977  ASP A O   1 
ATOM 2828 C CB  . ASP A 1 966  ? 174.784 178.398 216.635 1.00 68.31  ? 977  ASP A CB  1 
ATOM 2829 C CG  . ASP A 1 966  ? 174.686 176.996 217.204 1.00 79.84  ? 977  ASP A CG  1 
ATOM 2830 O OD1 . ASP A 1 966  ? 173.729 176.726 217.960 1.00 80.28  ? 977  ASP A OD1 1 
ATOM 2831 O OD2 . ASP A 1 966  ? 175.565 176.165 216.895 1.00 86.87  ? 977  ASP A OD2 1 
ATOM 2832 N N   . ASN A 1 967  ? 176.385 181.141 215.865 1.00 46.05  ? 978  ASN A N   1 
ATOM 2833 C CA  . ASN A 1 967  ? 176.355 182.553 215.514 1.00 41.23  ? 978  ASN A CA  1 
ATOM 2834 C C   . ASN A 1 967  ? 176.363 182.686 213.997 1.00 42.39  ? 978  ASN A C   1 
ATOM 2835 O O   . ASN A 1 967  ? 176.622 181.725 213.272 1.00 50.47  ? 978  ASN A O   1 
ATOM 2836 C CB  . ASN A 1 967  ? 177.540 183.297 216.141 1.00 38.80  ? 978  ASN A CB  1 
ATOM 2837 C CG  . ASN A 1 967  ? 177.307 184.789 216.242 1.00 42.41  ? 978  ASN A CG  1 
ATOM 2838 O OD1 . ASN A 1 967  ? 176.197 185.270 216.029 1.00 47.90  ? 978  ASN A OD1 1 
ATOM 2839 N ND2 . ASN A 1 967  ? 178.357 185.530 216.576 1.00 36.07  ? 978  ASN A ND2 1 
ATOM 2840 N N   . TRP A 1 968  ? 176.073 183.894 213.519 1.00 33.57  ? 979  TRP A N   1 
ATOM 2841 C CA  . TRP A 1 968  ? 176.215 184.194 212.102 1.00 32.88  ? 979  TRP A CA  1 
ATOM 2842 C C   . TRP A 1 968  ? 176.546 185.670 211.943 1.00 31.82  ? 979  TRP A C   1 
ATOM 2843 O O   . TRP A 1 968  ? 176.239 186.492 212.810 1.00 38.89  ? 979  TRP A O   1 
ATOM 2844 C CB  . TRP A 1 968  ? 174.955 183.821 211.309 1.00 35.68  ? 979  TRP A CB  1 
ATOM 2845 C CG  . TRP A 1 968  ? 173.731 184.590 211.692 1.00 38.31  ? 979  TRP A CG  1 
ATOM 2846 C CD1 . TRP A 1 968  ? 172.772 184.211 212.583 1.00 40.76  ? 979  TRP A CD1 1 
ATOM 2847 C CD2 . TRP A 1 968  ? 173.320 185.864 211.178 1.00 36.85  ? 979  TRP A CD2 1 
ATOM 2848 N NE1 . TRP A 1 968  ? 171.794 185.172 212.664 1.00 42.45  ? 979  TRP A NE1 1 
ATOM 2849 C CE2 . TRP A 1 968  ? 172.108 186.197 211.812 1.00 41.05  ? 979  TRP A CE2 1 
ATOM 2850 C CE3 . TRP A 1 968  ? 173.863 186.755 210.249 1.00 31.51  ? 979  TRP A CE3 1 
ATOM 2851 C CZ2 . TRP A 1 968  ? 171.429 187.384 211.546 1.00 40.08  ? 979  TRP A CZ2 1 
ATOM 2852 C CZ3 . TRP A 1 968  ? 173.188 187.933 209.987 1.00 33.65  ? 979  TRP A CZ3 1 
ATOM 2853 C CH2 . TRP A 1 968  ? 171.984 188.236 210.633 1.00 37.56  ? 979  TRP A CH2 1 
ATOM 2854 N N   . ARG A 1 969  ? 177.179 185.998 210.818 1.00 28.93  ? 980  ARG A N   1 
ATOM 2855 C CA  . ARG A 1 969  ? 177.660 187.349 210.575 1.00 28.66  ? 980  ARG A CA  1 
ATOM 2856 C C   . ARG A 1 969  ? 177.485 187.714 209.107 1.00 31.62  ? 980  ARG A C   1 
ATOM 2857 O O   . ARG A 1 969  ? 177.509 186.857 208.218 1.00 44.22  ? 980  ARG A O   1 
ATOM 2858 C CB  . ARG A 1 969  ? 179.134 187.501 210.975 1.00 32.33  ? 980  ARG A CB  1 
ATOM 2859 C CG  . ARG A 1 969  ? 180.100 186.744 210.078 1.00 35.52  ? 980  ARG A CG  1 
ATOM 2860 C CD  . ARG A 1 969  ? 181.545 187.040 210.442 1.00 38.98  ? 980  ARG A CD  1 
ATOM 2861 N NE  . ARG A 1 969  ? 182.482 186.299 209.606 1.00 41.99  ? 980  ARG A NE  1 
ATOM 2862 C CZ  . ARG A 1 969  ? 183.753 186.085 209.916 1.00 47.37  ? 980  ARG A CZ  1 
ATOM 2863 N NH1 . ARG A 1 969  ? 184.277 186.542 211.041 1.00 45.90  ? 980  ARG A NH1 1 
ATOM 2864 N NH2 . ARG A 1 969  ? 184.519 185.395 209.075 1.00 52.71  ? 980  ARG A NH2 1 
ATOM 2865 N N   . VAL A 1 970  ? 177.310 189.013 208.873 1.00 26.83  ? 981  VAL A N   1 
ATOM 2866 C CA  . VAL A 1 970  ? 177.263 189.599 207.540 1.00 31.17  ? 981  VAL A CA  1 
ATOM 2867 C C   . VAL A 1 970  ? 178.207 190.793 207.526 1.00 33.29  ? 981  VAL A C   1 
ATOM 2868 O O   . VAL A 1 970  ? 178.149 191.648 208.416 1.00 40.33  ? 981  VAL A O   1 
ATOM 2869 C CB  . VAL A 1 970  ? 175.831 190.026 207.152 1.00 27.72  ? 981  VAL A CB  1 
ATOM 2870 C CG1 . VAL A 1 970  ? 175.855 190.944 205.939 1.00 25.92  ? 981  VAL A CG1 1 
ATOM 2871 C CG2 . VAL A 1 970  ? 174.964 188.805 206.889 1.00 34.90  ? 981  VAL A CG2 1 
ATOM 2872 N N   . ARG A 1 971  ? 179.079 190.851 206.521 1.00 33.66  ? 982  ARG A N   1 
ATOM 2873 C CA  . ARG A 1 971  ? 180.121 191.869 206.474 1.00 33.01  ? 982  ARG A CA  1 
ATOM 2874 C C   . ARG A 1 971  ? 180.122 192.559 205.119 1.00 38.15  ? 982  ARG A C   1 
ATOM 2875 O O   . ARG A 1 971  ? 180.042 191.899 204.080 1.00 46.54  ? 982  ARG A O   1 
ATOM 2876 C CB  . ARG A 1 971  ? 181.499 191.258 206.752 1.00 36.30  ? 982  ARG A CB  1 
ATOM 2877 C CG  . ARG A 1 971  ? 181.652 190.692 208.154 1.00 36.19  ? 982  ARG A CG  1 
ATOM 2878 C CD  . ARG A 1 971  ? 183.108 190.419 208.486 1.00 41.23  ? 982  ARG A CD  1 
ATOM 2879 N NE  . ARG A 1 971  ? 183.666 189.344 207.675 1.00 47.54  ? 982  ARG A NE  1 
ATOM 2880 C CZ  . ARG A 1 971  ? 184.946 188.999 207.670 1.00 51.88  ? 982  ARG A CZ  1 
ATOM 2881 N NH1 . ARG A 1 971  ? 185.833 189.625 208.425 1.00 46.12  ? 982  ARG A NH1 1 
ATOM 2882 N NH2 . ARG A 1 971  ? 185.345 188.000 206.888 1.00 55.43  ? 982  ARG A NH2 1 
ATOM 2883 N N   . TRP A 1 972  ? 180.209 193.886 205.138 1.00 34.25  ? 983  TRP A N   1 
ATOM 2884 C CA  . TRP A 1 972  ? 180.307 194.699 203.935 1.00 34.82  ? 983  TRP A CA  1 
ATOM 2885 C C   . TRP A 1 972  ? 181.578 195.537 203.985 1.00 37.89  ? 983  TRP A C   1 
ATOM 2886 O O   . TRP A 1 972  ? 181.891 196.141 205.015 1.00 44.35  ? 983  TRP A O   1 
ATOM 2887 C CB  . TRP A 1 972  ? 179.079 195.605 203.789 1.00 35.37  ? 983  TRP A CB  1 
ATOM 2888 C CG  . TRP A 1 972  ? 179.299 196.810 202.923 1.00 40.22  ? 983  TRP A CG  1 
ATOM 2889 C CD1 . TRP A 1 972  ? 179.633 198.067 203.338 1.00 42.77  ? 983  TRP A CD1 1 
ATOM 2890 C CD2 . TRP A 1 972  ? 179.200 196.874 201.495 1.00 47.23  ? 983  TRP A CD2 1 
ATOM 2891 N NE1 . TRP A 1 972  ? 179.748 198.908 202.258 1.00 44.29  ? 983  TRP A NE1 1 
ATOM 2892 C CE2 . TRP A 1 972  ? 179.487 198.201 201.115 1.00 45.85  ? 983  TRP A CE2 1 
ATOM 2893 C CE3 . TRP A 1 972  ? 178.896 195.939 200.500 1.00 48.82  ? 983  TRP A CE3 1 
ATOM 2894 C CZ2 . TRP A 1 972  ? 179.480 198.615 199.785 1.00 41.74  ? 983  TRP A CZ2 1 
ATOM 2895 C CZ3 . TRP A 1 972  ? 178.890 196.353 199.180 1.00 44.97  ? 983  TRP A CZ3 1 
ATOM 2896 C CH2 . TRP A 1 972  ? 179.180 197.679 198.835 1.00 40.72  ? 983  TRP A CH2 1 
ATOM 2897 N N   . MET A 1 973  ? 182.313 195.566 202.873 1.00 41.54  ? 984  MET A N   1 
ATOM 2898 C CA  . MET A 1 973  ? 183.534 196.354 202.770 1.00 43.94  ? 984  MET A CA  1 
ATOM 2899 C C   . MET A 1 973  ? 183.571 197.034 201.412 1.00 45.28  ? 984  MET A C   1 
ATOM 2900 O O   . MET A 1 973  ? 183.012 196.521 200.440 1.00 52.05  ? 984  MET A O   1 
ATOM 2901 C CB  . MET A 1 973  ? 184.791 195.489 202.948 1.00 52.60  ? 984  MET A CB  1 
ATOM 2902 C CG  . MET A 1 973  ? 184.720 194.482 204.083 1.00 61.19  ? 984  MET A CG  1 
ATOM 2903 S SD  . MET A 1 973  ? 186.097 193.321 204.060 1.00 113.18 ? 984  MET A SD  1 
ATOM 2904 C CE  . MET A 1 973  ? 185.223 191.759 204.049 1.00 72.26  ? 984  MET A CE  1 
ATOM 2905 N N   . THR A 1 974  ? 184.233 198.185 201.346 1.00 42.51  ? 985  THR A N   1 
ATOM 2906 C CA  . THR A 1 974  ? 184.353 198.913 200.091 1.00 44.48  ? 985  THR A CA  1 
ATOM 2907 C C   . THR A 1 974  ? 185.549 199.847 200.172 1.00 44.83  ? 985  THR A C   1 
ATOM 2908 O O   . THR A 1 974  ? 186.018 200.193 201.260 1.00 48.95  ? 985  THR A O   1 
ATOM 2909 C CB  . THR A 1 974  ? 183.077 199.698 199.768 1.00 47.99  ? 985  THR A CB  1 
ATOM 2910 O OG1 . THR A 1 974  ? 183.348 200.650 198.732 1.00 50.43  ? 985  THR A OG1 1 
ATOM 2911 C CG2 . THR A 1 974  ? 182.571 200.423 201.002 1.00 47.30  ? 985  THR A CG2 1 
ATOM 2912 N N   . GLY A 1 975  ? 186.037 200.251 199.003 1.00 45.58  ? 986  GLY A N   1 
ATOM 2913 C CA  . GLY A 1 975  ? 187.181 201.138 198.935 1.00 44.71  ? 986  GLY A CA  1 
ATOM 2914 C C   . GLY A 1 975  ? 187.277 201.825 197.591 1.00 46.89  ? 986  GLY A C   1 
ATOM 2915 O O   . GLY A 1 975  ? 186.849 201.298 196.559 1.00 57.52  ? 986  GLY A O   1 
ATOM 2916 N N   . TYR A 1 976  ? 187.843 203.026 197.624 1.00 41.37  ? 987  TYR A N   1 
ATOM 2917 C CA  . TYR A 1 976  ? 188.133 203.813 196.438 1.00 45.23  ? 987  TYR A CA  1 
ATOM 2918 C C   . TYR A 1 976  ? 189.531 204.398 196.568 1.00 53.71  ? 987  TYR A C   1 
ATOM 2919 O O   . TYR A 1 976  ? 189.962 204.769 197.663 1.00 62.24  ? 987  TYR A O   1 
ATOM 2920 C CB  . TYR A 1 976  ? 187.100 204.933 196.247 1.00 44.64  ? 987  TYR A CB  1 
ATOM 2921 C CG  . TYR A 1 976  ? 187.611 206.123 195.469 1.00 45.79  ? 987  TYR A CG  1 
ATOM 2922 C CD1 . TYR A 1 976  ? 187.800 206.052 194.095 1.00 52.79  ? 987  TYR A CD1 1 
ATOM 2923 C CD2 . TYR A 1 976  ? 187.903 207.321 196.108 1.00 47.27  ? 987  TYR A CD2 1 
ATOM 2924 C CE1 . TYR A 1 976  ? 188.267 207.138 193.381 1.00 53.45  ? 987  TYR A CE1 1 
ATOM 2925 C CE2 . TYR A 1 976  ? 188.371 208.412 195.402 1.00 51.62  ? 987  TYR A CE2 1 
ATOM 2926 C CZ  . TYR A 1 976  ? 188.551 208.315 194.040 1.00 52.26  ? 987  TYR A CZ  1 
ATOM 2927 O OH  . TYR A 1 976  ? 189.016 209.399 193.332 1.00 52.79  ? 987  TYR A OH  1 
ATOM 2928 N N   . TYR A 1 977  ? 190.246 204.475 195.448 1.00 55.08  ? 988  TYR A N   1 
ATOM 2929 C CA  . TYR A 1 977  ? 191.608 204.986 195.479 1.00 51.65  ? 988  TYR A CA  1 
ATOM 2930 C C   . TYR A 1 977  ? 191.891 205.817 194.236 1.00 48.14  ? 988  TYR A C   1 
ATOM 2931 O O   . TYR A 1 977  ? 191.499 205.451 193.122 1.00 54.40  ? 988  TYR A O   1 
ATOM 2932 C CB  . TYR A 1 977  ? 192.630 203.849 195.607 1.00 52.59  ? 988  TYR A CB  1 
ATOM 2933 C CG  . TYR A 1 977  ? 192.471 202.739 194.593 1.00 53.42  ? 988  TYR A CG  1 
ATOM 2934 C CD1 . TYR A 1 977  ? 191.659 201.644 194.859 1.00 55.37  ? 988  TYR A CD1 1 
ATOM 2935 C CD2 . TYR A 1 977  ? 193.142 202.778 193.379 1.00 56.76  ? 988  TYR A CD2 1 
ATOM 2936 C CE1 . TYR A 1 977  ? 191.513 200.624 193.939 1.00 59.58  ? 988  TYR A CE1 1 
ATOM 2937 C CE2 . TYR A 1 977  ? 193.002 201.763 192.454 1.00 63.90  ? 988  TYR A CE2 1 
ATOM 2938 C CZ  . TYR A 1 977  ? 192.187 200.688 192.739 1.00 65.13  ? 988  TYR A CZ  1 
ATOM 2939 O OH  . TYR A 1 977  ? 192.044 199.674 191.821 1.00 72.10  ? 988  TYR A OH  1 
ATOM 2940 N N   . TYR A 1 978  ? 192.573 206.939 194.447 1.00 45.61  ? 989  TYR A N   1 
ATOM 2941 C CA  . TYR A 1 978  ? 193.038 207.817 193.384 1.00 48.42  ? 989  TYR A CA  1 
ATOM 2942 C C   . TYR A 1 978  ? 194.556 207.740 193.319 1.00 49.06  ? 989  TYR A C   1 
ATOM 2943 O O   . TYR A 1 978  ? 195.233 207.926 194.336 1.00 57.73  ? 989  TYR A O   1 
ATOM 2944 C CB  . TYR A 1 978  ? 192.588 209.259 193.630 1.00 50.12  ? 989  TYR A CB  1 
ATOM 2945 C CG  . TYR A 1 978  ? 193.026 210.239 192.565 1.00 52.01  ? 989  TYR A CG  1 
ATOM 2946 C CD1 . TYR A 1 978  ? 192.442 210.234 191.306 1.00 56.78  ? 989  TYR A CD1 1 
ATOM 2947 C CD2 . TYR A 1 978  ? 194.024 211.168 192.820 1.00 51.55  ? 989  TYR A CD2 1 
ATOM 2948 C CE1 . TYR A 1 978  ? 192.839 211.130 190.331 1.00 55.43  ? 989  TYR A CE1 1 
ATOM 2949 C CE2 . TYR A 1 978  ? 194.429 212.066 191.852 1.00 53.30  ? 989  TYR A CE2 1 
ATOM 2950 C CZ  . TYR A 1 978  ? 193.833 212.042 190.609 1.00 55.40  ? 989  TYR A CZ  1 
ATOM 2951 O OH  . TYR A 1 978  ? 194.233 212.935 189.642 1.00 62.02  ? 989  TYR A OH  1 
ATOM 2952 N N   . LYS A 1 979  ? 195.086 207.467 192.130 1.00 49.44  ? 990  LYS A N   1 
ATOM 2953 C CA  . LYS A 1 979  ? 196.524 207.281 191.948 1.00 51.49  ? 990  LYS A CA  1 
ATOM 2954 C C   . LYS A 1 979  ? 197.161 208.637 191.672 1.00 52.36  ? 990  LYS A C   1 
ATOM 2955 O O   . LYS A 1 979  ? 197.047 209.178 190.570 1.00 55.24  ? 990  LYS A O   1 
ATOM 2956 C CB  . LYS A 1 979  ? 196.799 206.293 190.819 1.00 55.71  ? 990  LYS A CB  1 
ATOM 2957 C CG  . LYS A 1 979  ? 196.116 204.947 190.997 1.00 60.62  ? 990  LYS A CG  1 
ATOM 2958 C CD  . LYS A 1 979  ? 196.275 204.077 189.761 1.00 66.21  ? 990  LYS A CD  1 
ATOM 2959 C CE  . LYS A 1 979  ? 195.275 202.933 189.760 1.00 71.45  ? 990  LYS A CE  1 
ATOM 2960 N NZ  . LYS A 1 979  ? 195.114 202.337 188.405 1.00 78.84  ? 990  LYS A NZ  1 
ATOM 2961 N N   . VAL A 1 980  ? 197.831 209.192 192.685 1.00 53.59  ? 991  VAL A N   1 
ATOM 2962 C CA  . VAL A 1 980  ? 198.570 210.436 192.492 1.00 52.72  ? 991  VAL A CA  1 
ATOM 2963 C C   . VAL A 1 980  ? 199.717 210.227 191.513 1.00 56.84  ? 991  VAL A C   1 
ATOM 2964 O O   . VAL A 1 980  ? 199.952 211.061 190.630 1.00 60.93  ? 991  VAL A O   1 
ATOM 2965 C CB  . VAL A 1 980  ? 199.072 210.974 193.844 1.00 50.99  ? 991  VAL A CB  1 
ATOM 2966 C CG1 . VAL A 1 980  ? 199.816 212.286 193.651 1.00 47.74  ? 991  VAL A CG1 1 
ATOM 2967 C CG2 . VAL A 1 980  ? 197.910 211.151 194.807 1.00 52.94  ? 991  VAL A CG2 1 
ATOM 2968 N N   . ILE A 1 981  ? 200.445 209.123 191.650 1.00 55.06  ? 992  ILE A N   1 
ATOM 2969 C CA  . ILE A 1 981  ? 201.510 208.750 190.727 1.00 51.91  ? 992  ILE A CA  1 
ATOM 2970 C C   . ILE A 1 981  ? 201.225 207.341 190.230 1.00 54.25  ? 992  ILE A C   1 
ATOM 2971 O O   . ILE A 1 981  ? 200.962 206.439 191.031 1.00 59.41  ? 992  ILE A O   1 
ATOM 2972 C CB  . ILE A 1 981  ? 202.900 208.826 191.393 1.00 52.20  ? 992  ILE A CB  1 
ATOM 2973 C CG1 . ILE A 1 981  ? 203.182 210.249 191.879 1.00 49.16  ? 992  ILE A CG1 1 
ATOM 2974 C CG2 . ILE A 1 981  ? 203.983 208.357 190.433 1.00 57.09  ? 992  ILE A CG2 1 
ATOM 2975 C CD1 . ILE A 1 981  ? 204.540 210.419 192.524 1.00 46.52  ? 992  ILE A CD1 1 
ATOM 2976 N N   . ASN A 1 982  ? 201.279 207.150 188.913 1.00 56.58  ? 993  ASN A N   1 
ATOM 2977 C CA  . ASN A 1 982  ? 200.892 205.877 188.314 1.00 63.43  ? 993  ASN A CA  1 
ATOM 2978 C C   . ASN A 1 982  ? 201.900 205.448 187.254 1.00 65.15  ? 993  ASN A C   1 
ATOM 2979 O O   . ASN A 1 982  ? 201.528 205.015 186.159 1.00 67.28  ? 993  ASN A O   1 
ATOM 2980 C CB  . ASN A 1 982  ? 199.483 205.960 187.725 1.00 68.37  ? 993  ASN A CB  1 
ATOM 2981 C CG  . ASN A 1 982  ? 198.913 204.599 187.372 1.00 69.02  ? 993  ASN A CG  1 
ATOM 2982 O OD1 . ASN A 1 982  ? 199.244 203.592 187.997 1.00 69.67  ? 993  ASN A OD1 1 
ATOM 2983 N ND2 . ASN A 1 982  ? 198.049 204.563 186.364 1.00 71.27  ? 993  ASN A ND2 1 
ATOM 2984 N N   . GLN A 1 983  ? 203.190 205.570 187.553 1.00 62.15  ? 994  GLN A N   1 
ATOM 2985 C CA  . GLN A 1 983  ? 204.188 205.061 186.631 1.00 65.74  ? 994  GLN A CA  1 
ATOM 2986 C C   . GLN A 1 983  ? 204.332 203.552 186.805 1.00 70.17  ? 994  GLN A C   1 
ATOM 2987 O O   . GLN A 1 983  ? 204.096 202.999 187.883 1.00 72.32  ? 994  GLN A O   1 
ATOM 2988 C CB  . GLN A 1 983  ? 205.533 205.752 186.851 1.00 66.83  ? 994  GLN A CB  1 
ATOM 2989 C CG  . GLN A 1 983  ? 205.479 207.264 186.723 1.00 70.47  ? 994  GLN A CG  1 
ATOM 2990 C CD  . GLN A 1 983  ? 206.836 207.911 186.911 1.00 83.34  ? 994  GLN A CD  1 
ATOM 2991 O OE1 . GLN A 1 983  ? 207.839 207.228 187.120 1.00 83.34  ? 994  GLN A OE1 1 
ATOM 2992 N NE2 . GLN A 1 983  ? 206.875 209.236 186.839 1.00 84.89  ? 994  GLN A NE2 1 
ATOM 2993 N N   . ASN A 1 984  ? 204.750 202.887 185.726 1.00 72.78  ? 995  ASN A N   1 
ATOM 2994 C CA  . ASN A 1 984  ? 204.797 201.429 185.706 1.00 71.26  ? 995  ASN A CA  1 
ATOM 2995 C C   . ASN A 1 984  ? 205.737 200.849 186.754 1.00 67.68  ? 995  ASN A C   1 
ATOM 2996 O O   . ASN A 1 984  ? 205.626 199.658 187.066 1.00 68.53  ? 995  ASN A O   1 
ATOM 2997 C CB  . ASN A 1 984  ? 205.202 200.938 184.315 1.00 73.62  ? 995  ASN A CB  1 
ATOM 2998 C CG  . ASN A 1 984  ? 206.473 201.594 183.811 1.00 72.61  ? 995  ASN A CG  1 
ATOM 2999 O OD1 . ASN A 1 984  ? 207.060 202.439 184.487 1.00 71.35  ? 995  ASN A OD1 1 
ATOM 3000 N ND2 . ASN A 1 984  ? 206.902 201.209 182.615 1.00 75.13  ? 995  ASN A ND2 1 
ATOM 3001 N N   . ASN A 1 985  ? 206.650 201.649 187.302 1.00 67.54  ? 996  ASN A N   1 
ATOM 3002 C CA  . ASN A 1 985  ? 207.526 201.203 188.373 1.00 65.02  ? 996  ASN A CA  1 
ATOM 3003 C C   . ASN A 1 985  ? 207.348 201.990 189.664 1.00 61.99  ? 996  ASN A C   1 
ATOM 3004 O O   . ASN A 1 985  ? 208.142 201.806 190.593 1.00 61.28  ? 996  ASN A O   1 
ATOM 3005 C CB  . ASN A 1 985  ? 208.993 201.279 187.928 1.00 62.67  ? 996  ASN A CB  1 
ATOM 3006 C CG  . ASN A 1 985  ? 209.340 200.231 186.889 1.00 62.02  ? 996  ASN A CG  1 
ATOM 3007 O OD1 . ASN A 1 985  ? 208.930 199.076 186.995 1.00 60.07  ? 996  ASN A OD1 1 
ATOM 3008 N ND2 . ASN A 1 985  ? 210.101 200.631 185.877 1.00 67.03  ? 996  ASN A ND2 1 
ATOM 3009 N N   . ARG A 1 986  ? 206.338 202.855 189.756 1.00 61.54  ? 997  ARG A N   1 
ATOM 3010 C CA  . ARG A 1 986  ? 206.142 203.660 190.959 1.00 60.03  ? 997  ARG A CA  1 
ATOM 3011 C C   . ARG A 1 986  ? 204.685 204.085 191.052 1.00 59.97  ? 997  ARG A C   1 
ATOM 3012 O O   . ARG A 1 986  ? 204.184 204.791 190.172 1.00 63.22  ? 997  ARG A O   1 
ATOM 3013 C CB  . ARG A 1 986  ? 207.058 204.885 190.952 1.00 58.28  ? 997  ARG A CB  1 
ATOM 3014 C CG  . ARG A 1 986  ? 206.783 205.869 192.076 1.00 60.79  ? 997  ARG A CG  1 
ATOM 3015 C CD  . ARG A 1 986  ? 207.609 207.132 191.916 1.00 65.58  ? 997  ARG A CD  1 
ATOM 3016 N NE  . ARG A 1 986  ? 209.010 206.914 192.256 1.00 72.20  ? 997  ARG A NE  1 
ATOM 3017 C CZ  . ARG A 1 986  ? 210.008 207.686 191.850 1.00 77.57  ? 997  ARG A CZ  1 
ATOM 3018 N NH1 . ARG A 1 986  ? 209.797 208.741 191.081 1.00 76.09  ? 997  ARG A NH1 1 
ATOM 3019 N NH2 . ARG A 1 986  ? 211.250 207.391 192.224 1.00 79.60  ? 997  ARG A NH2 1 
ATOM 3020 N N   . ARG A 1 987  ? 204.011 203.672 192.122 1.00 55.31  ? 998  ARG A N   1 
ATOM 3021 C CA  . ARG A 1 987  ? 202.620 204.033 192.344 1.00 55.20  ? 998  ARG A CA  1 
ATOM 3022 C C   . ARG A 1 987  ? 202.466 204.705 193.702 1.00 58.34  ? 998  ARG A C   1 
ATOM 3023 O O   . ARG A 1 987  ? 202.962 204.207 194.712 1.00 61.33  ? 998  ARG A O   1 
ATOM 3024 C CB  . ARG A 1 987  ? 201.708 202.805 192.256 1.00 56.45  ? 998  ARG A CB  1 
ATOM 3025 C CG  . ARG A 1 987  ? 200.231 203.138 192.344 1.00 63.68  ? 998  ARG A CG  1 
ATOM 3026 C CD  . ARG A 1 987  ? 199.370 201.890 192.443 1.00 72.80  ? 998  ARG A CD  1 
ATOM 3027 N NE  . ARG A 1 987  ? 199.103 201.309 191.133 1.00 80.88  ? 998  ARG A NE  1 
ATOM 3028 C CZ  . ARG A 1 987  ? 198.317 200.262 190.923 1.00 82.61  ? 998  ARG A CZ  1 
ATOM 3029 N NH1 . ARG A 1 987  ? 197.694 199.655 191.919 1.00 87.14  ? 998  ARG A NH1 1 
ATOM 3030 N NH2 . ARG A 1 987  ? 198.148 199.816 189.681 1.00 79.20  ? 998  ARG A NH2 1 
ATOM 3031 N N   . VAL A 1 988  ? 201.786 205.847 193.717 1.00 57.43  ? 999  VAL A N   1 
ATOM 3032 C CA  . VAL A 1 988  ? 201.480 206.577 194.942 1.00 51.15  ? 999  VAL A CA  1 
ATOM 3033 C C   . VAL A 1 988  ? 200.002 206.929 194.917 1.00 50.23  ? 999  VAL A C   1 
ATOM 3034 O O   . VAL A 1 988  ? 199.546 207.625 194.002 1.00 56.34  ? 999  VAL A O   1 
ATOM 3035 C CB  . VAL A 1 988  ? 202.336 207.849 195.090 1.00 50.49  ? 999  VAL A CB  1 
ATOM 3036 C CG1 . VAL A 1 988  ? 201.939 208.609 196.344 1.00 50.19  ? 999  VAL A CG1 1 
ATOM 3037 C CG2 . VAL A 1 988  ? 203.813 207.498 195.127 1.00 55.40  ? 999  VAL A CG2 1 
ATOM 3038 N N   . THR A 1 989  ? 199.259 206.449 195.916 1.00 47.10  ? 1000 THR A N   1 
ATOM 3039 C CA  . THR A 1 989  ? 197.811 206.594 195.951 1.00 46.82  ? 1000 THR A CA  1 
ATOM 3040 C C   . THR A 1 989  ? 197.356 207.045 197.332 1.00 53.19  ? 1000 THR A C   1 
ATOM 3041 O O   . THR A 1 989  ? 198.023 206.812 198.344 1.00 63.64  ? 1000 THR A O   1 
ATOM 3042 C CB  . THR A 1 989  ? 197.082 205.285 195.601 1.00 49.83  ? 1000 THR A CB  1 
ATOM 3043 O OG1 . THR A 1 989  ? 197.085 204.416 196.741 1.00 49.45  ? 1000 THR A OG1 1 
ATOM 3044 C CG2 . THR A 1 989  ? 197.739 204.580 194.429 1.00 55.96  ? 1000 THR A CG2 1 
ATOM 3045 N N   . ILE A 1 990  ? 196.195 207.696 197.351 1.00 47.79  ? 1001 ILE A N   1 
ATOM 3046 C CA  . ILE A 1 990  ? 195.476 208.035 198.572 1.00 45.18  ? 1001 ILE A CA  1 
ATOM 3047 C C   . ILE A 1 990  ? 194.002 207.731 198.341 1.00 41.34  ? 1001 ILE A C   1 
ATOM 3048 O O   . ILE A 1 990  ? 193.466 208.008 197.262 1.00 48.48  ? 1001 ILE A O   1 
ATOM 3049 C CB  . ILE A 1 990  ? 195.691 209.512 198.972 1.00 47.94  ? 1001 ILE A CB  1 
ATOM 3050 C CG1 . ILE A 1 990  ? 194.938 209.839 200.264 1.00 53.37  ? 1001 ILE A CG1 1 
ATOM 3051 C CG2 . ILE A 1 990  ? 195.289 210.451 197.842 1.00 38.91  ? 1001 ILE A CG2 1 
ATOM 3052 C CD1 . ILE A 1 990  ? 195.458 211.068 200.975 1.00 44.95  ? 1001 ILE A CD1 1 
ATOM 3053 N N   . GLY A 1 991  ? 193.328 207.113 199.307 1.00 40.14  ? 1002 GLY A N   1 
ATOM 3054 C CA  . GLY A 1 991  ? 191.932 206.723 199.032 1.00 42.54  ? 1002 GLY A CA  1 
ATOM 3055 C C   . GLY A 1 991  ? 191.059 206.755 200.267 1.00 50.44  ? 1002 GLY A C   1 
ATOM 3056 O O   . GLY A 1 991  ? 191.560 207.175 201.326 1.00 60.16  ? 1002 GLY A O   1 
ATOM 3057 N N   . LEU A 1 992  ? 189.794 206.343 200.137 1.00 43.99  ? 1003 LEU A N   1 
ATOM 3058 C CA  . LEU A 1 992  ? 188.876 206.286 201.304 1.00 39.15  ? 1003 LEU A CA  1 
ATOM 3059 C C   . LEU A 1 992  ? 188.226 204.899 201.346 1.00 42.80  ? 1003 LEU A C   1 
ATOM 3060 O O   . LEU A 1 992  ? 187.810 204.417 200.277 1.00 53.73  ? 1003 LEU A O   1 
ATOM 3061 C CB  . LEU A 1 992  ? 187.823 207.390 201.239 1.00 37.59  ? 1003 LEU A CB  1 
ATOM 3062 C CG  . LEU A 1 992  ? 186.962 207.558 202.495 1.00 40.74  ? 1003 LEU A CG  1 
ATOM 3063 C CD1 . LEU A 1 992  ? 186.706 209.027 202.771 1.00 37.42  ? 1003 LEU A CD1 1 
ATOM 3064 C CD2 . LEU A 1 992  ? 185.647 206.808 202.373 1.00 46.61  ? 1003 LEU A CD2 1 
ATOM 3065 N N   . ASN A 1 993  ? 188.153 204.291 202.531 1.00 39.58  ? 1004 ASN A N   1 
ATOM 3066 C CA  . ASN A 1 993  ? 187.567 202.932 202.674 1.00 42.71  ? 1004 ASN A CA  1 
ATOM 3067 C C   . ASN A 1 993  ? 186.374 202.984 203.628 1.00 40.46  ? 1004 ASN A C   1 
ATOM 3068 O O   . ASN A 1 993  ? 186.290 203.951 204.405 1.00 49.10  ? 1004 ASN A O   1 
ATOM 3069 C CB  . ASN A 1 993  ? 188.589 201.921 203.179 1.00 43.97  ? 1004 ASN A CB  1 
ATOM 3070 C CG  . ASN A 1 993  ? 189.765 201.755 202.248 1.00 51.31  ? 1004 ASN A CG  1 
ATOM 3071 O OD1 . ASN A 1 993  ? 189.824 202.393 201.192 1.00 53.59  ? 1004 ASN A OD1 1 
ATOM 3072 N ND2 . ASN A 1 993  ? 190.709 200.903 202.617 1.00 55.63  ? 1004 ASN A ND2 1 
ATOM 3073 N N   . ASN A 1 994  ? 185.488 201.992 203.566 1.00 36.53  ? 1005 ASN A N   1 
ATOM 3074 C CA  . ASN A 1 994  ? 184.354 201.911 204.475 1.00 37.88  ? 1005 ASN A CA  1 
ATOM 3075 C C   . ASN A 1 994  ? 184.065 200.450 204.786 1.00 43.12  ? 1005 ASN A C   1 
ATOM 3076 O O   . ASN A 1 994  ? 184.099 199.600 203.893 1.00 51.08  ? 1005 ASN A O   1 
ATOM 3077 C CB  . ASN A 1 994  ? 183.110 202.582 203.878 1.00 41.25  ? 1005 ASN A CB  1 
ATOM 3078 C CG  . ASN A 1 994  ? 181.837 202.218 204.617 1.00 43.21  ? 1005 ASN A CG  1 
ATOM 3079 O OD1 . ASN A 1 994  ? 181.808 202.178 205.847 1.00 41.69  ? 1005 ASN A OD1 1 
ATOM 3080 N ND2 . ASN A 1 994  ? 180.775 201.946 203.867 1.00 43.88  ? 1005 ASN A ND2 1 
ATOM 3081 N N   . MET A 1 995  ? 183.784 200.165 206.058 1.00 40.96  ? 1006 MET A N   1 
ATOM 3082 C CA  . MET A 1 995  ? 183.530 198.806 206.516 1.00 37.20  ? 1006 MET A CA  1 
ATOM 3083 C C   . MET A 1 995  ? 182.342 198.798 207.465 1.00 33.98  ? 1006 MET A C   1 
ATOM 3084 O O   . MET A 1 995  ? 182.229 199.669 208.332 1.00 38.14  ? 1006 MET A O   1 
ATOM 3085 C CB  . MET A 1 995  ? 184.761 198.214 207.219 1.00 39.33  ? 1006 MET A CB  1 
ATOM 3086 C CG  . MET A 1 995  ? 186.067 198.391 206.456 1.00 50.49  ? 1006 MET A CG  1 
ATOM 3087 S SD  . MET A 1 995  ? 187.495 197.664 207.283 1.00 106.38 ? 1006 MET A SD  1 
ATOM 3088 C CE  . MET A 1 995  ? 186.698 196.544 208.427 1.00 65.56  ? 1006 MET A CE  1 
ATOM 3089 N N   . ILE A 1 996  ? 181.460 197.814 207.297 1.00 32.02  ? 1007 ILE A N   1 
ATOM 3090 C CA  . ILE A 1 996  ? 180.277 197.656 208.138 1.00 29.80  ? 1007 ILE A CA  1 
ATOM 3091 C C   . ILE A 1 996  ? 180.134 196.185 208.510 1.00 30.71  ? 1007 ILE A C   1 
ATOM 3092 O O   . ILE A 1 996  ? 180.149 195.315 207.633 1.00 37.38  ? 1007 ILE A O   1 
ATOM 3093 C CB  . ILE A 1 996  ? 178.997 198.157 207.439 1.00 29.02  ? 1007 ILE A CB  1 
ATOM 3094 C CG1 . ILE A 1 996  ? 179.103 199.651 207.123 1.00 33.18  ? 1007 ILE A CG1 1 
ATOM 3095 C CG2 . ILE A 1 996  ? 177.774 197.880 208.298 1.00 27.66  ? 1007 ILE A CG2 1 
ATOM 3096 C CD1 . ILE A 1 996  ? 177.861 200.228 206.480 1.00 34.36  ? 1007 ILE A CD1 1 
ATOM 3097 N N   . TRP A 1 997  ? 179.986 195.911 209.806 1.00 29.40  ? 1008 TRP A N   1 
ATOM 3098 C CA  . TRP A 1 997  ? 179.808 194.558 210.316 1.00 28.66  ? 1008 TRP A CA  1 
ATOM 3099 C C   . TRP A 1 997  ? 178.589 194.477 211.224 1.00 28.97  ? 1008 TRP A C   1 
ATOM 3100 O O   . TRP A 1 997  ? 178.244 195.436 211.921 1.00 37.87  ? 1008 TRP A O   1 
ATOM 3101 C CB  . TRP A 1 997  ? 181.025 194.058 211.116 1.00 32.44  ? 1008 TRP A CB  1 
ATOM 3102 C CG  . TRP A 1 997  ? 182.324 193.999 210.379 1.00 33.80  ? 1008 TRP A CG  1 
ATOM 3103 C CD1 . TRP A 1 997  ? 182.517 194.084 209.032 1.00 34.96  ? 1008 TRP A CD1 1 
ATOM 3104 C CD2 . TRP A 1 997  ? 183.618 193.799 210.957 1.00 35.09  ? 1008 TRP A CD2 1 
ATOM 3105 N NE1 . TRP A 1 997  ? 183.854 193.970 208.738 1.00 38.83  ? 1008 TRP A NE1 1 
ATOM 3106 C CE2 . TRP A 1 997  ? 184.551 193.792 209.904 1.00 39.16  ? 1008 TRP A CE2 1 
ATOM 3107 C CE3 . TRP A 1 997  ? 184.079 193.633 212.267 1.00 31.86  ? 1008 TRP A CE3 1 
ATOM 3108 C CZ2 . TRP A 1 997  ? 185.917 193.624 210.118 1.00 46.53  ? 1008 TRP A CZ2 1 
ATOM 3109 C CZ3 . TRP A 1 997  ? 185.434 193.469 212.478 1.00 35.61  ? 1008 TRP A CZ3 1 
ATOM 3110 C CH2 . TRP A 1 997  ? 186.338 193.466 211.410 1.00 44.40  ? 1008 TRP A CH2 1 
ATOM 3111 N N   . HIS A 1 998  ? 177.956 193.304 211.222 1.00 23.17  ? 1009 HIS A N   1 
ATOM 3112 C CA  . HIS A 1 998  ? 176.894 192.969 212.159 1.00 22.19  ? 1009 HIS A CA  1 
ATOM 3113 C C   . HIS A 1 998  ? 177.001 191.497 212.528 1.00 25.68  ? 1009 HIS A C   1 
ATOM 3114 O O   . HIS A 1 998  ? 177.232 190.649 211.662 1.00 33.75  ? 1009 HIS A O   1 
ATOM 3115 C CB  . HIS A 1 998  ? 175.506 193.257 211.576 1.00 21.72  ? 1009 HIS A CB  1 
ATOM 3116 C CG  . HIS A 1 998  ? 174.389 192.615 212.340 1.00 23.47  ? 1009 HIS A CG  1 
ATOM 3117 N ND1 . HIS A 1 998  ? 173.843 193.177 213.473 1.00 28.46  ? 1009 HIS A ND1 1 
ATOM 3118 C CD2 . HIS A 1 998  ? 173.720 191.456 212.135 1.00 24.18  ? 1009 HIS A CD2 1 
ATOM 3119 C CE1 . HIS A 1 998  ? 172.884 192.393 213.933 1.00 27.24  ? 1009 HIS A CE1 1 
ATOM 3120 N NE2 . HIS A 1 998  ? 172.789 191.342 213.139 1.00 26.71  ? 1009 HIS A NE2 1 
ATOM 3121 N N   . TYR A 1 999  ? 176.834 191.200 213.814 1.00 27.29  ? 1010 TYR A N   1 
ATOM 3122 C CA  . TYR A 1 999  ? 176.845 189.834 214.317 1.00 25.17  ? 1010 TYR A CA  1 
ATOM 3123 C C   . TYR A 1 999  ? 175.557 189.562 215.081 1.00 30.68  ? 1010 TYR A C   1 
ATOM 3124 O O   . TYR A 1 999  ? 174.988 190.458 215.711 1.00 37.09  ? 1010 TYR A O   1 
ATOM 3125 C CB  . TYR A 1 999  ? 178.052 189.575 215.230 1.00 29.78  ? 1010 TYR A CB  1 
ATOM 3126 C CG  . TYR A 1 999  ? 179.377 189.458 214.508 1.00 33.25  ? 1010 TYR A CG  1 
ATOM 3127 C CD1 . TYR A 1 999  ? 179.935 190.550 213.855 1.00 30.67  ? 1010 TYR A CD1 1 
ATOM 3128 C CD2 . TYR A 1 999  ? 180.072 188.257 214.483 1.00 34.41  ? 1010 TYR A CD2 1 
ATOM 3129 C CE1 . TYR A 1 999  ? 181.146 190.448 213.198 1.00 28.94  ? 1010 TYR A CE1 1 
ATOM 3130 C CE2 . TYR A 1 999  ? 181.284 188.145 213.829 1.00 29.32  ? 1010 TYR A CE2 1 
ATOM 3131 C CZ  . TYR A 1 999  ? 181.816 189.244 213.188 1.00 28.20  ? 1010 TYR A CZ  1 
ATOM 3132 O OH  . TYR A 1 999  ? 183.022 189.137 212.534 1.00 32.16  ? 1010 TYR A OH  1 
ATOM 3133 N N   . ASP A 1 1000 ? 175.097 188.311 215.017 1.00 32.12  ? 1011 ASP A N   1 
ATOM 3134 C CA  . ASP A 1 1000 ? 173.848 187.947 215.681 1.00 36.35  ? 1011 ASP A CA  1 
ATOM 3135 C C   . ASP A 1 1000 ? 173.987 188.011 217.197 1.00 39.08  ? 1011 ASP A C   1 
ATOM 3136 O O   . ASP A 1 1000 ? 173.141 188.593 217.886 1.00 48.94  ? 1011 ASP A O   1 
ATOM 3137 C CB  . ASP A 1 1000 ? 173.407 186.551 215.238 1.00 36.40  ? 1011 ASP A CB  1 
ATOM 3138 C CG  . ASP A 1 1000 ? 171.956 186.265 215.570 1.00 40.04  ? 1011 ASP A CG  1 
ATOM 3139 O OD1 . ASP A 1 1000 ? 171.273 187.164 216.104 1.00 46.84  ? 1011 ASP A OD1 1 
ATOM 3140 O OD2 . ASP A 1 1000 ? 171.496 185.137 215.295 1.00 40.39  ? 1011 ASP A OD2 1 
ATOM 3141 N N   . LYS A 1 1001 ? 175.050 187.419 217.738 1.00 38.18  ? 1012 LYS A N   1 
ATOM 3142 C CA  . LYS A 1 1001 ? 175.257 187.347 219.177 1.00 40.90  ? 1012 LYS A CA  1 
ATOM 3143 C C   . LYS A 1 1001 ? 176.670 187.789 219.522 1.00 39.24  ? 1012 LYS A C   1 
ATOM 3144 O O   . LYS A 1 1001 ? 177.611 187.547 218.761 1.00 39.27  ? 1012 LYS A O   1 
ATOM 3145 C CB  . LYS A 1 1001 ? 175.013 185.926 219.704 1.00 39.71  ? 1012 LYS A CB  1 
ATOM 3146 C CG  . LYS A 1 1001 ? 173.590 185.428 219.517 1.00 35.86  ? 1012 LYS A CG  1 
ATOM 3147 C CD  . LYS A 1 1001 ? 173.484 183.941 219.810 1.00 41.05  ? 1012 LYS A CD  1 
ATOM 3148 C CE  . LYS A 1 1001 ? 172.118 183.399 219.420 1.00 52.39  ? 1012 LYS A CE  1 
ATOM 3149 N NZ  . LYS A 1 1001 ? 172.093 181.910 219.405 1.00 63.77  ? 1012 LYS A NZ  1 
ATOM 3150 N N   . ASP A 1 1002 ? 176.811 188.438 220.676 1.00 37.45  ? 1013 ASP A N   1 
ATOM 3151 C CA  . ASP A 1 1002 ? 178.112 188.886 221.163 1.00 42.51  ? 1013 ASP A CA  1 
ATOM 3152 C C   . ASP A 1 1002 ? 178.723 187.781 222.016 1.00 47.12  ? 1013 ASP A C   1 
ATOM 3153 O O   . ASP A 1 1002 ? 178.280 187.542 223.144 1.00 48.14  ? 1013 ASP A O   1 
ATOM 3154 C CB  . ASP A 1 1002 ? 177.963 190.181 221.957 1.00 42.58  ? 1013 ASP A CB  1 
ATOM 3155 C CG  . ASP A 1 1002 ? 179.263 190.626 222.603 1.00 47.81  ? 1013 ASP A CG  1 
ATOM 3156 O OD1 . ASP A 1 1002 ? 180.344 190.266 222.091 1.00 51.66  ? 1013 ASP A OD1 1 
ATOM 3157 O OD2 . ASP A 1 1002 ? 179.202 191.336 223.628 1.00 48.15  ? 1013 ASP A OD2 1 
ATOM 3158 N N   . LEU A 1 1003 ? 179.742 187.109 221.483 1.00 38.48  ? 1014 LEU A N   1 
ATOM 3159 C CA  . LEU A 1 1003 ? 180.413 186.014 222.173 1.00 32.70  ? 1014 LEU A CA  1 
ATOM 3160 C C   . LEU A 1 1003 ? 181.893 186.314 222.390 1.00 32.81  ? 1014 LEU A C   1 
ATOM 3161 O O   . LEU A 1 1003 ? 182.737 185.423 222.282 1.00 39.06  ? 1014 LEU A O   1 
ATOM 3162 C CB  . LEU A 1 1003 ? 180.238 184.705 221.405 1.00 32.94  ? 1014 LEU A CB  1 
ATOM 3163 C CG  . LEU A 1 1003 ? 178.799 184.224 221.215 1.00 34.00  ? 1014 LEU A CG  1 
ATOM 3164 C CD1 . LEU A 1 1003 ? 178.764 182.953 220.383 1.00 38.05  ? 1014 LEU A CD1 1 
ATOM 3165 C CD2 . LEU A 1 1003 ? 178.125 184.007 222.559 1.00 34.26  ? 1014 LEU A CD2 1 
ATOM 3166 N N   . SER A 1 1004 ? 182.220 187.571 222.698 1.00 29.61  ? 1015 SER A N   1 
ATOM 3167 C CA  . SER A 1 1004 ? 183.611 187.968 222.873 1.00 36.06  ? 1015 SER A CA  1 
ATOM 3168 C C   . SER A 1 1004 ? 184.217 187.472 224.180 1.00 35.92  ? 1015 SER A C   1 
ATOM 3169 O O   . SER A 1 1004 ? 185.445 187.493 224.316 1.00 38.56  ? 1015 SER A O   1 
ATOM 3170 C CB  . SER A 1 1004 ? 183.731 189.491 222.799 1.00 45.61  ? 1015 SER A CB  1 
ATOM 3171 O OG  . SER A 1 1004 ? 185.089 189.895 222.776 1.00 58.16  ? 1015 SER A OG  1 
ATOM 3172 N N   . GLY A 1 1005 ? 183.402 187.028 225.136 1.00 32.60  ? 1016 GLY A N   1 
ATOM 3173 C CA  . GLY A 1 1005 ? 183.929 186.553 226.397 1.00 28.76  ? 1016 GLY A CA  1 
ATOM 3174 C C   . GLY A 1 1005 ? 184.569 185.183 226.283 1.00 30.17  ? 1016 GLY A C   1 
ATOM 3175 O O   . GLY A 1 1005 ? 184.377 184.450 225.315 1.00 36.58  ? 1016 GLY A O   1 
ATOM 3176 N N   . TYR A 1 1006 ? 185.343 184.833 227.310 1.00 25.33  ? 1017 TYR A N   1 
ATOM 3177 C CA  . TYR A 1 1006 ? 186.061 183.566 227.348 1.00 21.55  ? 1017 TYR A CA  1 
ATOM 3178 C C   . TYR A 1 1006 ? 185.456 182.574 228.332 1.00 25.28  ? 1017 TYR A C   1 
ATOM 3179 O O   . TYR A 1 1006 ? 186.083 181.553 228.632 1.00 28.58  ? 1017 TYR A O   1 
ATOM 3180 C CB  . TYR A 1 1006 ? 187.536 183.801 227.681 1.00 20.98  ? 1017 TYR A CB  1 
ATOM 3181 C CG  . TYR A 1 1006 ? 188.295 184.542 226.604 1.00 24.88  ? 1017 TYR A CG  1 
ATOM 3182 C CD1 . TYR A 1 1006 ? 188.275 185.929 226.541 1.00 27.99  ? 1017 TYR A CD1 1 
ATOM 3183 C CD2 . TYR A 1 1006 ? 189.028 183.855 225.646 1.00 28.51  ? 1017 TYR A CD2 1 
ATOM 3184 C CE1 . TYR A 1 1006 ? 188.966 186.609 225.558 1.00 28.94  ? 1017 TYR A CE1 1 
ATOM 3185 C CE2 . TYR A 1 1006 ? 189.722 184.527 224.659 1.00 31.30  ? 1017 TYR A CE2 1 
ATOM 3186 C CZ  . TYR A 1 1006 ? 189.687 185.904 224.619 1.00 32.98  ? 1017 TYR A CZ  1 
ATOM 3187 O OH  . TYR A 1 1006 ? 190.377 186.578 223.638 1.00 33.12  ? 1017 TYR A OH  1 
ATOM 3188 N N   . SER A 1 1007 ? 184.258 182.845 228.842 1.00 30.12  ? 1018 SER A N   1 
ATOM 3189 C CA  . SER A 1 1007 ? 183.590 181.897 229.718 1.00 29.03  ? 1018 SER A CA  1 
ATOM 3190 C C   . SER A 1 1007 ? 183.147 180.668 228.930 1.00 30.97  ? 1018 SER A C   1 
ATOM 3191 O O   . SER A 1 1007 ? 183.075 180.680 227.698 1.00 36.54  ? 1018 SER A O   1 
ATOM 3192 C CB  . SER A 1 1007 ? 182.387 182.550 230.398 1.00 29.23  ? 1018 SER A CB  1 
ATOM 3193 O OG  . SER A 1 1007 ? 181.557 183.200 229.451 1.00 34.09  ? 1018 SER A OG  1 
ATOM 3194 N N   . LEU A 1 1008 ? 182.863 179.590 229.659 1.00 28.79  ? 1019 LEU A N   1 
ATOM 3195 C CA  . LEU A 1 1008 ? 182.423 178.354 229.025 1.00 33.26  ? 1019 LEU A CA  1 
ATOM 3196 C C   . LEU A 1 1008 ? 181.120 178.586 228.271 1.00 33.02  ? 1019 LEU A C   1 
ATOM 3197 O O   . LEU A 1 1008 ? 180.160 179.130 228.825 1.00 34.79  ? 1019 LEU A O   1 
ATOM 3198 C CB  . LEU A 1 1008 ? 182.246 177.256 230.072 1.00 30.71  ? 1019 LEU A CB  1 
ATOM 3199 C CG  . LEU A 1 1008 ? 181.793 175.896 229.536 1.00 31.80  ? 1019 LEU A CG  1 
ATOM 3200 C CD1 . LEU A 1 1008 ? 182.820 175.331 228.569 1.00 27.45  ? 1019 LEU A CD1 1 
ATOM 3201 C CD2 . LEU A 1 1008 ? 181.533 174.922 230.674 1.00 38.21  ? 1019 LEU A CD2 1 
ATOM 3202 N N   . GLY A 1 1009 ? 181.089 178.170 227.008 1.00 28.17  ? 1020 GLY A N   1 
ATOM 3203 C CA  . GLY A 1 1009 ? 179.965 178.404 226.134 1.00 30.61  ? 1020 GLY A CA  1 
ATOM 3204 C C   . GLY A 1 1009 ? 180.161 179.538 225.149 1.00 34.29  ? 1020 GLY A C   1 
ATOM 3205 O O   . GLY A 1 1009 ? 179.399 179.637 224.181 1.00 38.39  ? 1020 GLY A O   1 
ATOM 3206 N N   . GLN A 1 1010 ? 181.156 180.390 225.370 1.00 30.92  ? 1021 GLN A N   1 
ATOM 3207 C CA  . GLN A 1 1010 ? 181.465 181.492 224.473 1.00 26.21  ? 1021 GLN A CA  1 
ATOM 3208 C C   . GLN A 1 1010 ? 182.759 181.205 223.718 1.00 28.94  ? 1021 GLN A C   1 
ATOM 3209 O O   . GLN A 1 1010 ? 183.621 180.451 224.176 1.00 32.86  ? 1021 GLN A O   1 
ATOM 3210 C CB  . GLN A 1 1010 ? 181.575 182.805 225.251 1.00 25.75  ? 1021 GLN A CB  1 
ATOM 3211 C CG  . GLN A 1 1010 ? 180.299 183.177 225.991 1.00 31.03  ? 1021 GLN A CG  1 
ATOM 3212 C CD  . GLN A 1 1010 ? 180.166 184.667 226.234 1.00 37.42  ? 1021 GLN A CD  1 
ATOM 3213 O OE1 . GLN A 1 1010 ? 180.973 185.461 225.754 1.00 37.49  ? 1021 GLN A OE1 1 
ATOM 3214 N NE2 . GLN A 1 1010 ? 179.142 185.054 226.985 1.00 41.99  ? 1021 GLN A NE2 1 
ATOM 3215 N N   . GLY A 1 1011 ? 182.885 181.818 222.543 1.00 28.38  ? 1022 GLY A N   1 
ATOM 3216 C CA  . GLY A 1 1011 ? 183.981 181.502 221.647 1.00 30.90  ? 1022 GLY A CA  1 
ATOM 3217 C C   . GLY A 1 1011 ? 185.201 182.390 221.779 1.00 31.76  ? 1022 GLY A C   1 
ATOM 3218 O O   . GLY A 1 1011 ? 186.259 182.080 221.224 1.00 37.29  ? 1022 GLY A O   1 
ATOM 3219 N N   . GLY A 1 1012 ? 185.073 183.494 222.510 1.00 29.51  ? 1023 GLY A N   1 
ATOM 3220 C CA  . GLY A 1 1012 ? 186.205 184.383 222.711 1.00 31.37  ? 1023 GLY A CA  1 
ATOM 3221 C C   . GLY A 1 1012 ? 186.702 185.060 221.455 1.00 33.84  ? 1023 GLY A C   1 
ATOM 3222 O O   . GLY A 1 1012 ? 187.915 185.212 221.278 1.00 38.38  ? 1023 GLY A O   1 
ATOM 3223 N N   . TYR A 1 1013 ? 185.795 185.472 220.573 1.00 33.13  ? 1024 TYR A N   1 
ATOM 3224 C CA  . TYR A 1 1013 ? 186.150 186.188 219.358 1.00 30.70  ? 1024 TYR A CA  1 
ATOM 3225 C C   . TYR A 1 1013 ? 185.297 187.443 219.246 1.00 37.08  ? 1024 TYR A C   1 
ATOM 3226 O O   . TYR A 1 1013 ? 184.156 187.480 219.712 1.00 41.01  ? 1024 TYR A O   1 
ATOM 3227 C CB  . TYR A 1 1013 ? 185.969 185.309 218.110 1.00 29.97  ? 1024 TYR A CB  1 
ATOM 3228 C CG  . TYR A 1 1013 ? 184.560 184.797 217.911 1.00 29.41  ? 1024 TYR A CG  1 
ATOM 3229 C CD1 . TYR A 1 1013 ? 184.140 183.616 218.506 1.00 30.16  ? 1024 TYR A CD1 1 
ATOM 3230 C CD2 . TYR A 1 1013 ? 183.651 185.493 217.125 1.00 25.43  ? 1024 TYR A CD2 1 
ATOM 3231 C CE1 . TYR A 1 1013 ? 182.855 183.144 218.327 1.00 28.47  ? 1024 TYR A CE1 1 
ATOM 3232 C CE2 . TYR A 1 1013 ? 182.365 185.029 216.943 1.00 26.51  ? 1024 TYR A CE2 1 
ATOM 3233 C CZ  . TYR A 1 1013 ? 181.972 183.854 217.544 1.00 29.42  ? 1024 TYR A CZ  1 
ATOM 3234 O OH  . TYR A 1 1013 ? 180.691 183.386 217.364 1.00 34.95  ? 1024 TYR A OH  1 
ATOM 3235 N N   . TYR A 1 1014 ? 185.866 188.475 218.625 1.00 37.43  ? 1025 TYR A N   1 
ATOM 3236 C CA  . TYR A 1 1014 ? 185.164 189.744 218.495 1.00 36.22  ? 1025 TYR A CA  1 
ATOM 3237 C C   . TYR A 1 1014 ? 183.895 189.567 217.670 1.00 33.05  ? 1025 TYR A C   1 
ATOM 3238 O O   . TYR A 1 1014 ? 183.908 188.951 216.601 1.00 38.85  ? 1025 TYR A O   1 
ATOM 3239 C CB  . TYR A 1 1014 ? 186.076 190.789 217.851 1.00 37.41  ? 1025 TYR A CB  1 
ATOM 3240 C CG  . TYR A 1 1014 ? 185.559 192.207 217.951 1.00 34.36  ? 1025 TYR A CG  1 
ATOM 3241 C CD1 . TYR A 1 1014 ? 185.298 192.785 219.186 1.00 34.35  ? 1025 TYR A CD1 1 
ATOM 3242 C CD2 . TYR A 1 1014 ? 185.343 192.971 216.812 1.00 32.66  ? 1025 TYR A CD2 1 
ATOM 3243 C CE1 . TYR A 1 1014 ? 184.829 194.080 219.284 1.00 32.65  ? 1025 TYR A CE1 1 
ATOM 3244 C CE2 . TYR A 1 1014 ? 184.875 194.268 216.901 1.00 32.60  ? 1025 TYR A CE2 1 
ATOM 3245 C CZ  . TYR A 1 1014 ? 184.620 194.818 218.139 1.00 33.96  ? 1025 TYR A CZ  1 
ATOM 3246 O OH  . TYR A 1 1014 ? 184.154 196.109 218.233 1.00 36.95  ? 1025 TYR A OH  1 
ATOM 3247 N N   . SER A 1 1015 ? 182.792 190.112 218.177 1.00 27.34  ? 1026 SER A N   1 
ATOM 3248 C CA  . SER A 1 1015 ? 181.498 189.963 217.525 1.00 28.98  ? 1026 SER A CA  1 
ATOM 3249 C C   . SER A 1 1015 ? 180.563 191.096 217.931 1.00 32.10  ? 1026 SER A C   1 
ATOM 3250 O O   . SER A 1 1015 ? 179.700 190.909 218.798 1.00 36.05  ? 1026 SER A O   1 
ATOM 3251 C CB  . SER A 1 1015 ? 180.877 188.611 217.876 1.00 34.21  ? 1026 SER A CB  1 
ATOM 3252 O OG  . SER A 1 1015 ? 180.814 188.431 219.280 1.00 38.76  ? 1026 SER A OG  1 
ATOM 3253 N N   . PRO A 1 1016 ? 180.700 192.275 217.335 1.00 29.07  ? 1027 PRO A N   1 
ATOM 3254 C CA  . PRO A 1 1016 ? 179.813 193.386 217.682 1.00 27.19  ? 1027 PRO A CA  1 
ATOM 3255 C C   . PRO A 1 1016 ? 178.465 193.272 216.985 1.00 26.01  ? 1027 PRO A C   1 
ATOM 3256 O O   . PRO A 1 1016 ? 178.336 192.707 215.899 1.00 28.84  ? 1027 PRO A O   1 
ATOM 3257 C CB  . PRO A 1 1016 ? 180.584 194.611 217.184 1.00 26.41  ? 1027 PRO A CB  1 
ATOM 3258 C CG  . PRO A 1 1016 ? 181.340 194.095 216.008 1.00 26.65  ? 1027 PRO A CG  1 
ATOM 3259 C CD  . PRO A 1 1016 ? 181.713 192.669 216.340 1.00 30.17  ? 1027 PRO A CD  1 
ATOM 3260 N N   . GLN A 1 1017 ? 177.449 193.833 217.639 1.00 25.53  ? 1028 GLN A N   1 
ATOM 3261 C CA  . GLN A 1 1017 ? 176.114 193.881 217.061 1.00 24.99  ? 1028 GLN A CA  1 
ATOM 3262 C C   . GLN A 1 1017 ? 176.002 194.884 215.923 1.00 28.03  ? 1028 GLN A C   1 
ATOM 3263 O O   . GLN A 1 1017 ? 175.195 194.678 215.011 1.00 35.17  ? 1028 GLN A O   1 
ATOM 3264 C CB  . GLN A 1 1017 ? 175.080 194.218 218.140 1.00 30.78  ? 1028 GLN A CB  1 
ATOM 3265 C CG  . GLN A 1 1017 ? 175.096 193.270 219.325 1.00 36.97  ? 1028 GLN A CG  1 
ATOM 3266 C CD  . GLN A 1 1017 ? 174.978 191.819 218.908 1.00 34.92  ? 1028 GLN A CD  1 
ATOM 3267 O OE1 . GLN A 1 1017 ? 175.861 191.007 219.186 1.00 32.02  ? 1028 GLN A OE1 1 
ATOM 3268 N NE2 . GLN A 1 1017 ? 173.885 191.484 218.234 1.00 40.69  ? 1028 GLN A NE2 1 
ATOM 3269 N N   . GLU A 1 1018 ? 176.788 195.957 215.957 1.00 24.60  ? 1029 GLU A N   1 
ATOM 3270 C CA  . GLU A 1 1018 ? 176.830 196.923 214.869 1.00 29.11  ? 1029 GLU A CA  1 
ATOM 3271 C C   . GLU A 1 1018 ? 178.173 197.633 214.917 1.00 29.20  ? 1029 GLU A C   1 
ATOM 3272 O O   . GLU A 1 1018 ? 178.517 198.242 215.935 1.00 40.32  ? 1029 GLU A O   1 
ATOM 3273 C CB  . GLU A 1 1018 ? 175.682 197.933 214.972 1.00 42.00  ? 1029 GLU A CB  1 
ATOM 3274 C CG  . GLU A 1 1018 ? 175.783 199.090 213.991 1.00 56.25  ? 1029 GLU A CG  1 
ATOM 3275 C CD  . GLU A 1 1018 ? 174.978 198.852 212.726 1.00 59.68  ? 1029 GLU A CD  1 
ATOM 3276 O OE1 . GLU A 1 1018 ? 174.065 197.999 212.752 1.00 60.56  ? 1029 GLU A OE1 1 
ATOM 3277 O OE2 . GLU A 1 1018 ? 175.257 199.516 211.706 1.00 39.71  ? 1029 GLU A OE2 1 
ATOM 3278 N N   . TYR A 1 1019 ? 178.928 197.546 213.822 1.00 23.83  ? 1030 TYR A N   1 
ATOM 3279 C CA  . TYR A 1 1019 ? 180.257 198.133 213.730 1.00 27.18  ? 1030 TYR A CA  1 
ATOM 3280 C C   . TYR A 1 1019 ? 180.399 198.880 212.413 1.00 29.61  ? 1030 TYR A C   1 
ATOM 3281 O O   . TYR A 1 1019 ? 180.063 198.346 211.353 1.00 37.20  ? 1030 TYR A O   1 
ATOM 3282 C CB  . TYR A 1 1019 ? 181.342 197.053 213.842 1.00 27.77  ? 1030 TYR A CB  1 
ATOM 3283 C CG  . TYR A 1 1019 ? 182.752 197.548 213.603 1.00 31.15  ? 1030 TYR A CG  1 
ATOM 3284 C CD1 . TYR A 1 1019 ? 183.476 198.160 214.616 1.00 35.92  ? 1030 TYR A CD1 1 
ATOM 3285 C CD2 . TYR A 1 1019 ? 183.363 197.389 212.366 1.00 29.86  ? 1030 TYR A CD2 1 
ATOM 3286 C CE1 . TYR A 1 1019 ? 184.766 198.609 214.401 1.00 35.16  ? 1030 TYR A CE1 1 
ATOM 3287 C CE2 . TYR A 1 1019 ? 184.651 197.834 212.142 1.00 31.76  ? 1030 TYR A CE2 1 
ATOM 3288 C CZ  . TYR A 1 1019 ? 185.347 198.444 213.163 1.00 34.43  ? 1030 TYR A CZ  1 
ATOM 3289 O OH  . TYR A 1 1019 ? 186.630 198.888 212.944 1.00 42.58  ? 1030 TYR A OH  1 
ATOM 3290 N N   . LEU A 1 1020 ? 180.917 200.104 212.487 1.00 28.29  ? 1031 LEU A N   1 
ATOM 3291 C CA  . LEU A 1 1020 ? 181.177 200.934 211.318 1.00 26.98  ? 1031 LEU A CA  1 
ATOM 3292 C C   . LEU A 1 1020 ? 182.591 201.486 211.403 1.00 33.14  ? 1031 LEU A C   1 
ATOM 3293 O O   . LEU A 1 1020 ? 183.070 201.816 212.491 1.00 40.90  ? 1031 LEU A O   1 
ATOM 3294 C CB  . LEU A 1 1020 ? 180.176 202.090 211.214 1.00 29.39  ? 1031 LEU A CB  1 
ATOM 3295 C CG  . LEU A 1 1020 ? 178.840 201.803 210.528 1.00 40.27  ? 1031 LEU A CG  1 
ATOM 3296 C CD1 . LEU A 1 1020 ? 178.025 200.813 211.343 1.00 39.68  ? 1031 LEU A CD1 1 
ATOM 3297 C CD2 . LEU A 1 1020 ? 178.065 203.093 210.314 1.00 49.59  ? 1031 LEU A CD2 1 
ATOM 3298 N N   . SER A 1 1021 ? 183.262 201.579 210.256 1.00 30.28  ? 1032 SER A N   1 
ATOM 3299 C CA  . SER A 1 1021 ? 184.630 202.081 210.216 1.00 30.07  ? 1032 SER A CA  1 
ATOM 3300 C C   . SER A 1 1021 ? 184.874 202.829 208.915 1.00 30.11  ? 1032 SER A C   1 
ATOM 3301 O O   . SER A 1 1021 ? 184.498 202.349 207.841 1.00 41.49  ? 1032 SER A O   1 
ATOM 3302 C CB  . SER A 1 1021 ? 185.640 200.937 210.363 1.00 36.55  ? 1032 SER A CB  1 
ATOM 3303 O OG  . SER A 1 1021 ? 186.970 201.414 210.255 1.00 37.94  ? 1032 SER A OG  1 
ATOM 3304 N N   . PHE A 1 1022 ? 185.509 203.996 209.016 1.00 23.59  ? 1033 PHE A N   1 
ATOM 3305 C CA  . PHE A 1 1022 ? 185.908 204.789 207.859 1.00 25.30  ? 1033 PHE A CA  1 
ATOM 3306 C C   . PHE A 1 1022 ? 187.400 205.078 207.949 1.00 32.24  ? 1033 PHE A C   1 
ATOM 3307 O O   . PHE A 1 1022 ? 187.873 205.575 208.974 1.00 42.34  ? 1033 PHE A O   1 
ATOM 3308 C CB  . PHE A 1 1022 ? 185.121 206.101 207.787 1.00 27.44  ? 1033 PHE A CB  1 
ATOM 3309 C CG  . PHE A 1 1022 ? 183.630 205.919 207.774 1.00 38.35  ? 1033 PHE A CG  1 
ATOM 3310 C CD1 . PHE A 1 1022 ? 182.972 205.562 206.608 1.00 43.14  ? 1033 PHE A CD1 1 
ATOM 3311 C CD2 . PHE A 1 1022 ? 182.884 206.111 208.925 1.00 39.91  ? 1033 PHE A CD2 1 
ATOM 3312 C CE1 . PHE A 1 1022 ? 181.600 205.396 206.592 1.00 41.58  ? 1033 PHE A CE1 1 
ATOM 3313 C CE2 . PHE A 1 1022 ? 181.511 205.947 208.915 1.00 41.13  ? 1033 PHE A CE2 1 
ATOM 3314 C CZ  . PHE A 1 1022 ? 180.869 205.589 207.747 1.00 44.16  ? 1033 PHE A CZ  1 
ATOM 3315 N N   . ALA A 1 1023 ? 188.132 204.799 206.871 1.00 33.33  ? 1034 ALA A N   1 
ATOM 3316 C CA  . ALA A 1 1023 ? 189.587 204.884 206.887 1.00 31.55  ? 1034 ALA A CA  1 
ATOM 3317 C C   . ALA A 1 1023 ? 190.089 205.624 205.656 1.00 36.71  ? 1034 ALA A C   1 
ATOM 3318 O O   . ALA A 1 1023 ? 189.434 205.642 204.613 1.00 43.63  ? 1034 ALA A O   1 
ATOM 3319 C CB  . ALA A 1 1023 ? 190.230 203.492 206.947 1.00 35.60  ? 1034 ALA A CB  1 
ATOM 3320 N N   . ILE A 1 1024 ? 191.269 206.226 205.788 1.00 37.85  ? 1035 ILE A N   1 
ATOM 3321 C CA  . ILE A 1 1024 ? 191.908 206.951 204.689 1.00 38.58  ? 1035 ILE A CA  1 
ATOM 3322 C C   . ILE A 1 1024 ? 193.301 206.375 204.453 1.00 41.32  ? 1035 ILE A C   1 
ATOM 3323 O O   . ILE A 1 1024 ? 194.271 206.819 205.084 1.00 47.33  ? 1035 ILE A O   1 
ATOM 3324 C CB  . ILE A 1 1024 ? 191.971 208.460 204.978 1.00 34.55  ? 1035 ILE A CB  1 
ATOM 3325 C CG1 . ILE A 1 1024 ? 190.566 209.015 205.216 1.00 41.51  ? 1035 ILE A CG1 1 
ATOM 3326 C CG2 . ILE A 1 1024 ? 192.638 209.197 203.825 1.00 35.66  ? 1035 ILE A CG2 1 
ATOM 3327 C CD1 . ILE A 1 1024 ? 190.496 210.527 205.233 1.00 48.46  ? 1035 ILE A CD1 1 
ATOM 3328 N N   . PRO A 1 1025 ? 193.449 205.385 203.572 1.00 38.91  ? 1036 PRO A N   1 
ATOM 3329 C CA  . PRO A 1 1025 ? 194.771 204.778 203.359 1.00 40.81  ? 1036 PRO A CA  1 
ATOM 3330 C C   . PRO A 1 1025 ? 195.627 205.589 202.393 1.00 48.32  ? 1036 PRO A C   1 
ATOM 3331 O O   . PRO A 1 1025 ? 195.146 206.081 201.369 1.00 52.77  ? 1036 PRO A O   1 
ATOM 3332 C CB  . PRO A 1 1025 ? 194.434 203.397 202.788 1.00 44.10  ? 1036 PRO A CB  1 
ATOM 3333 C CG  . PRO A 1 1025 ? 193.134 203.607 202.088 1.00 46.35  ? 1036 PRO A CG  1 
ATOM 3334 C CD  . PRO A 1 1025 ? 192.378 204.617 202.913 1.00 43.02  ? 1036 PRO A CD  1 
ATOM 3335 N N   . VAL A 1 1026 ? 196.910 205.713 202.728 1.00 48.81  ? 1037 VAL A N   1 
ATOM 3336 C CA  . VAL A 1 1026 ? 197.924 206.323 201.878 1.00 49.59  ? 1037 VAL A CA  1 
ATOM 3337 C C   . VAL A 1 1026 ? 198.988 205.271 201.595 1.00 52.04  ? 1037 VAL A C   1 
ATOM 3338 O O   . VAL A 1 1026 ? 199.485 204.617 202.521 1.00 56.89  ? 1037 VAL A O   1 
ATOM 3339 C CB  . VAL A 1 1026 ? 198.545 207.570 202.539 1.00 51.87  ? 1037 VAL A CB  1 
ATOM 3340 C CG1 . VAL A 1 1026 ? 199.590 208.196 201.628 1.00 52.27  ? 1037 VAL A CG1 1 
ATOM 3341 C CG2 . VAL A 1 1026 ? 197.463 208.576 202.898 1.00 50.21  ? 1037 VAL A CG2 1 
ATOM 3342 N N   . MET A 1 1027 ? 199.342 205.114 200.319 1.00 51.33  ? 1038 MET A N   1 
ATOM 3343 C CA  . MET A 1 1027 ? 200.122 203.965 199.882 1.00 52.60  ? 1038 MET A CA  1 
ATOM 3344 C C   . MET A 1 1027 ? 201.165 204.404 198.862 1.00 51.95  ? 1038 MET A C   1 
ATOM 3345 O O   . MET A 1 1027 ? 200.896 205.250 198.004 1.00 56.71  ? 1038 MET A O   1 
ATOM 3346 C CB  . MET A 1 1027 ? 199.174 202.887 199.321 1.00 54.44  ? 1038 MET A CB  1 
ATOM 3347 C CG  . MET A 1 1027 ? 199.785 201.574 198.827 1.00 59.44  ? 1038 MET A CG  1 
ATOM 3348 S SD  . MET A 1 1027 ? 200.863 201.693 197.386 1.00 75.29  ? 1038 MET A SD  1 
ATOM 3349 C CE  . MET A 1 1027 ? 199.686 201.402 196.070 1.00 64.59  ? 1038 MET A CE  1 
ATOM 3350 N N   . TRP A 1 1028 ? 202.357 203.808 198.960 1.00 47.14  ? 1039 TRP A N   1 
ATOM 3351 C CA  . TRP A 1 1028 ? 203.451 204.069 198.031 1.00 50.56  ? 1039 TRP A CA  1 
ATOM 3352 C C   . TRP A 1 1028 ? 204.191 202.770 197.743 1.00 56.61  ? 1039 TRP A C   1 
ATOM 3353 O O   . TRP A 1 1028 ? 204.754 202.158 198.654 1.00 59.09  ? 1039 TRP A O   1 
ATOM 3354 C CB  . TRP A 1 1028 ? 204.420 205.117 198.599 1.00 48.66  ? 1039 TRP A CB  1 
ATOM 3355 C CG  . TRP A 1 1028 ? 205.709 205.274 197.828 1.00 55.14  ? 1039 TRP A CG  1 
ATOM 3356 C CD1 . TRP A 1 1028 ? 205.894 205.094 196.486 1.00 59.78  ? 1039 TRP A CD1 1 
ATOM 3357 C CD2 . TRP A 1 1028 ? 206.985 205.653 198.359 1.00 55.29  ? 1039 TRP A CD2 1 
ATOM 3358 N NE1 . TRP A 1 1028 ? 207.205 205.333 196.152 1.00 63.65  ? 1039 TRP A NE1 1 
ATOM 3359 C CE2 . TRP A 1 1028 ? 207.896 205.678 197.284 1.00 58.07  ? 1039 TRP A CE2 1 
ATOM 3360 C CE3 . TRP A 1 1028 ? 207.447 205.971 199.640 1.00 54.04  ? 1039 TRP A CE3 1 
ATOM 3361 C CZ2 . TRP A 1 1028 ? 209.239 206.008 197.450 1.00 54.85  ? 1039 TRP A CZ2 1 
ATOM 3362 C CZ3 . TRP A 1 1028 ? 208.782 206.299 199.802 1.00 53.71  ? 1039 TRP A CZ3 1 
ATOM 3363 C CH2 . TRP A 1 1028 ? 209.662 206.315 198.714 1.00 51.71  ? 1039 TRP A CH2 1 
ATOM 3364 N N   . ARG A 1 1029 ? 204.208 202.366 196.474 1.00 57.34  ? 1040 ARG A N   1 
ATOM 3365 C CA  . ARG A 1 1029 ? 204.907 201.176 196.012 1.00 54.94  ? 1040 ARG A CA  1 
ATOM 3366 C C   . ARG A 1 1029 ? 205.965 201.566 194.994 1.00 57.57  ? 1040 ARG A C   1 
ATOM 3367 O O   . ARG A 1 1029 ? 205.724 202.420 194.134 1.00 61.78  ? 1040 ARG A O   1 
ATOM 3368 C CB  . ARG A 1 1029 ? 203.952 200.174 195.363 1.00 55.38  ? 1040 ARG A CB  1 
ATOM 3369 C CG  . ARG A 1 1029 ? 203.142 199.348 196.325 1.00 60.43  ? 1040 ARG A CG  1 
ATOM 3370 C CD  . ARG A 1 1029 ? 202.526 198.178 195.594 1.00 68.49  ? 1040 ARG A CD  1 
ATOM 3371 N NE  . ARG A 1 1029 ? 201.358 198.554 194.809 1.00 70.27  ? 1040 ARG A NE  1 
ATOM 3372 C CZ  . ARG A 1 1029 ? 200.121 198.165 195.081 1.00 73.86  ? 1040 ARG A CZ  1 
ATOM 3373 N NH1 . ARG A 1 1029 ? 199.852 197.389 196.118 1.00 77.66  ? 1040 ARG A NH1 1 
ATOM 3374 N NH2 . ARG A 1 1029 ? 199.127 198.564 194.292 1.00 73.71  ? 1040 ARG A NH2 1 
ATOM 3375 N N   . GLU A 1 1030 ? 207.129 200.924 195.078 1.00 56.84  ? 1041 GLU A N   1 
ATOM 3376 C CA  . GLU A 1 1030 ? 208.187 201.181 194.111 1.00 57.70  ? 1041 GLU A CA  1 
ATOM 3377 C C   . GLU A 1 1030 ? 209.045 199.930 193.984 1.00 59.44  ? 1041 GLU A C   1 
ATOM 3378 O O   . GLU A 1 1030 ? 209.064 199.076 194.873 1.00 60.87  ? 1041 GLU A O   1 
ATOM 3379 C CB  . GLU A 1 1030 ? 209.030 202.395 194.523 1.00 58.69  ? 1041 GLU A CB  1 
ATOM 3380 C CG  . GLU A 1 1030 ? 209.996 202.894 193.459 1.00 65.37  ? 1041 GLU A CG  1 
ATOM 3381 C CD  . GLU A 1 1030 ? 210.430 204.327 193.692 1.00 65.92  ? 1041 GLU A CD  1 
ATOM 3382 O OE1 . GLU A 1 1030 ? 209.673 205.079 194.340 1.00 65.11  ? 1041 GLU A OE1 1 
ATOM 3383 O OE2 . GLU A 1 1030 ? 211.526 204.701 193.226 1.00 65.92  ? 1041 GLU A OE2 1 
ATOM 3384 N N   . ARG A 1 1031 ? 209.737 199.822 192.851 1.00 57.01  ? 1042 ARG A N   1 
ATOM 3385 C CA  . ARG A 1 1031 ? 210.700 198.753 192.633 1.00 54.30  ? 1042 ARG A CA  1 
ATOM 3386 C C   . ARG A 1 1031 ? 211.897 199.308 191.874 1.00 53.95  ? 1042 ARG A C   1 
ATOM 3387 O O   . ARG A 1 1031 ? 211.803 200.319 191.175 1.00 55.42  ? 1042 ARG A O   1 
ATOM 3388 C CB  . ARG A 1 1031 ? 210.085 197.565 191.878 1.00 57.61  ? 1042 ARG A CB  1 
ATOM 3389 C CG  . ARG A 1 1031 ? 209.608 197.872 190.466 1.00 63.73  ? 1042 ARG A CG  1 
ATOM 3390 C CD  . ARG A 1 1031 ? 209.001 196.632 189.821 1.00 61.62  ? 1042 ARG A CD  1 
ATOM 3391 N NE  . ARG A 1 1031 ? 208.235 196.941 188.619 1.00 61.21  ? 1042 ARG A NE  1 
ATOM 3392 C CZ  . ARG A 1 1031 ? 207.201 196.232 188.187 1.00 63.54  ? 1042 ARG A CZ  1 
ATOM 3393 N NH1 . ARG A 1 1031 ? 206.782 195.156 188.834 1.00 63.15  ? 1042 ARG A NH1 1 
ATOM 3394 N NH2 . ARG A 1 1031 ? 206.574 196.609 187.077 1.00 66.35  ? 1042 ARG A NH2 1 
ATOM 3395 N N   . THR A 1 1032 ? 213.029 198.630 192.027 1.00 54.82  ? 1043 THR A N   1 
ATOM 3396 C CA  . THR A 1 1032 ? 214.288 199.064 191.433 1.00 57.00  ? 1043 THR A CA  1 
ATOM 3397 C C   . THR A 1 1032 ? 214.906 197.796 190.835 1.00 63.80  ? 1043 THR A C   1 
ATOM 3398 O O   . THR A 1 1032 ? 214.314 196.711 190.879 1.00 67.94  ? 1043 THR A O   1 
ATOM 3399 C CB  . THR A 1 1032 ? 215.096 199.808 192.517 1.00 59.60  ? 1043 THR A CB  1 
ATOM 3400 O OG1 . THR A 1 1032 ? 214.480 201.077 192.765 1.00 64.45  ? 1043 THR A OG1 1 
ATOM 3401 C CG2 . THR A 1 1032 ? 216.541 200.090 192.109 1.00 61.75  ? 1043 THR A CG2 1 
ATOM 3402 N N   . GLU A 1 1033 ? 216.100 197.919 190.244 1.00 67.96  ? 1044 GLU A N   1 
ATOM 3403 C CA  . GLU A 1 1033 ? 216.761 196.771 189.628 1.00 71.03  ? 1044 GLU A CA  1 
ATOM 3404 C C   . GLU A 1 1033 ? 216.942 195.618 190.608 1.00 64.23  ? 1044 GLU A C   1 
ATOM 3405 O O   . GLU A 1 1033 ? 216.880 194.451 190.205 1.00 65.65  ? 1044 GLU A O   1 
ATOM 3406 C CB  . GLU A 1 1033 ? 218.119 197.186 189.064 1.00 76.05  ? 1044 GLU A CB  1 
ATOM 3407 C CG  . GLU A 1 1033 ? 218.055 198.240 187.974 1.00 78.37  ? 1044 GLU A CG  1 
ATOM 3408 C CD  . GLU A 1 1033 ? 219.420 198.552 187.394 1.00 87.01  ? 1044 GLU A CD  1 
ATOM 3409 O OE1 . GLU A 1 1033 ? 220.047 197.636 186.821 1.00 85.31  ? 1044 GLU A OE1 1 
ATOM 3410 O OE2 . GLU A 1 1033 ? 219.867 199.712 187.515 1.00 89.89  ? 1044 GLU A OE2 1 
ATOM 3411 N N   . ASN A 1 1034 ? 217.172 195.915 191.884 1.00 57.21  ? 1045 ASN A N   1 
ATOM 3412 C CA  . ASN A 1 1034 ? 217.339 194.852 192.867 1.00 55.92  ? 1045 ASN A CA  1 
ATOM 3413 C C   . ASN A 1 1034 ? 216.640 195.123 194.192 1.00 59.90  ? 1045 ASN A C   1 
ATOM 3414 O O   . ASN A 1 1034 ? 216.854 194.360 195.138 1.00 61.91  ? 1045 ASN A O   1 
ATOM 3415 C CB  . ASN A 1 1034 ? 218.835 194.599 193.107 1.00 57.68  ? 1045 ASN A CB  1 
ATOM 3416 C CG  . ASN A 1 1034 ? 219.424 193.613 192.117 1.00 69.45  ? 1045 ASN A CG  1 
ATOM 3417 O OD1 . ASN A 1 1034 ? 219.322 192.400 192.296 1.00 67.77  ? 1045 ASN A OD1 1 
ATOM 3418 N ND2 . ASN A 1 1034 ? 220.043 194.132 191.063 1.00 80.70  ? 1045 ASN A ND2 1 
ATOM 3419 N N   . TRP A 1 1035 ? 215.818 196.163 194.301 1.00 59.52  ? 1046 TRP A N   1 
ATOM 3420 C CA  . TRP A 1 1035 ? 215.053 196.454 195.505 1.00 54.27  ? 1046 TRP A CA  1 
ATOM 3421 C C   . TRP A 1 1035 ? 213.591 196.674 195.142 1.00 55.69  ? 1046 TRP A C   1 
ATOM 3422 O O   . TRP A 1 1035 ? 213.285 197.313 194.130 1.00 60.94  ? 1046 TRP A O   1 
ATOM 3423 C CB  . TRP A 1 1035 ? 215.595 197.695 196.222 1.00 52.53  ? 1046 TRP A CB  1 
ATOM 3424 C CG  . TRP A 1 1035 ? 216.858 197.462 196.991 1.00 48.00  ? 1046 TRP A CG  1 
ATOM 3425 C CD1 . TRP A 1 1035 ? 218.116 197.856 196.640 1.00 48.93  ? 1046 TRP A CD1 1 
ATOM 3426 C CD2 . TRP A 1 1035 ? 216.984 196.798 198.255 1.00 49.58  ? 1046 TRP A CD2 1 
ATOM 3427 N NE1 . TRP A 1 1035 ? 219.019 197.470 197.601 1.00 52.41  ? 1046 TRP A NE1 1 
ATOM 3428 C CE2 . TRP A 1 1035 ? 218.348 196.819 198.604 1.00 50.62  ? 1046 TRP A CE2 1 
ATOM 3429 C CE3 . TRP A 1 1035 ? 216.076 196.184 199.122 1.00 53.84  ? 1046 TRP A CE3 1 
ATOM 3430 C CZ2 . TRP A 1 1035 ? 218.826 196.251 199.782 1.00 50.93  ? 1046 TRP A CZ2 1 
ATOM 3431 C CZ3 . TRP A 1 1035 ? 216.552 195.621 200.292 1.00 53.65  ? 1046 TRP A CZ3 1 
ATOM 3432 C CH2 . TRP A 1 1035 ? 217.915 195.658 200.610 1.00 50.93  ? 1046 TRP A CH2 1 
ATOM 3433 N N   . SER A 1 1036 ? 212.689 196.145 195.967 1.00 54.66  ? 1047 SER A N   1 
ATOM 3434 C CA  . SER A 1 1036 ? 211.265 196.412 195.821 1.00 54.04  ? 1047 SER A CA  1 
ATOM 3435 C C   . SER A 1 1036 ? 210.682 196.681 197.198 1.00 59.27  ? 1047 SER A C   1 
ATOM 3436 O O   . SER A 1 1036 ? 211.072 196.034 198.173 1.00 64.87  ? 1047 SER A O   1 
ATOM 3437 C CB  . SER A 1 1036 ? 210.536 195.240 195.153 1.00 53.07  ? 1047 SER A CB  1 
ATOM 3438 O OG  . SER A 1 1036 ? 209.144 195.488 195.066 1.00 58.29  ? 1047 SER A OG  1 
ATOM 3439 N N   . TRP A 1 1037 ? 209.759 197.636 197.289 1.00 56.78  ? 1048 TRP A N   1 
ATOM 3440 C CA  . TRP A 1 1037 ? 209.200 197.969 198.589 1.00 53.36  ? 1048 TRP A CA  1 
ATOM 3441 C C   . TRP A 1 1037 ? 207.823 198.602 198.447 1.00 54.58  ? 1048 TRP A C   1 
ATOM 3442 O O   . TRP A 1 1037 ? 207.450 199.133 197.395 1.00 60.43  ? 1048 TRP A O   1 
ATOM 3443 C CB  . TRP A 1 1037 ? 210.132 198.896 199.380 1.00 48.87  ? 1048 TRP A CB  1 
ATOM 3444 C CG  . TRP A 1 1037 ? 210.283 200.262 198.795 1.00 50.22  ? 1048 TRP A CG  1 
ATOM 3445 C CD1 . TRP A 1 1037 ? 209.552 201.372 199.100 1.00 52.66  ? 1048 TRP A CD1 1 
ATOM 3446 C CD2 . TRP A 1 1037 ? 211.242 200.671 197.813 1.00 51.02  ? 1048 TRP A CD2 1 
ATOM 3447 N NE1 . TRP A 1 1037 ? 209.989 202.445 198.363 1.00 55.48  ? 1048 TRP A NE1 1 
ATOM 3448 C CE2 . TRP A 1 1037 ? 211.027 202.041 197.565 1.00 52.44  ? 1048 TRP A CE2 1 
ATOM 3449 C CE3 . TRP A 1 1037 ? 212.258 200.011 197.117 1.00 53.01  ? 1048 TRP A CE3 1 
ATOM 3450 C CZ2 . TRP A 1 1037 ? 211.791 202.762 196.651 1.00 53.80  ? 1048 TRP A CZ2 1 
ATOM 3451 C CZ3 . TRP A 1 1037 ? 213.015 200.729 196.209 1.00 52.87  ? 1048 TRP A CZ3 1 
ATOM 3452 C CH2 . TRP A 1 1037 ? 212.777 202.089 195.984 1.00 53.40  ? 1048 TRP A CH2 1 
ATOM 3453 N N   . GLU A 1 1038 ? 207.071 198.513 199.543 1.00 50.41  ? 1049 GLU A N   1 
ATOM 3454 C CA  . GLU A 1 1038 ? 205.754 199.108 199.699 1.00 52.72  ? 1049 GLU A CA  1 
ATOM 3455 C C   . GLU A 1 1038 ? 205.633 199.680 201.103 1.00 51.89  ? 1049 GLU A C   1 
ATOM 3456 O O   . GLU A 1 1038 ? 205.996 199.023 202.082 1.00 56.56  ? 1049 GLU A O   1 
ATOM 3457 C CB  . GLU A 1 1038 ? 204.637 198.081 199.464 1.00 55.86  ? 1049 GLU A CB  1 
ATOM 3458 C CG  . GLU A 1 1038 ? 203.247 198.584 199.829 1.00 59.50  ? 1049 GLU A CG  1 
ATOM 3459 C CD  . GLU A 1 1038 ? 202.159 197.563 199.558 1.00 67.06  ? 1049 GLU A CD  1 
ATOM 3460 O OE1 . GLU A 1 1038 ? 202.031 196.605 200.348 1.00 69.57  ? 1049 GLU A OE1 1 
ATOM 3461 O OE2 . GLU A 1 1038 ? 201.424 197.723 198.561 1.00 67.04  ? 1049 GLU A OE2 1 
ATOM 3462 N N   . LEU A 1 1039 ? 205.125 200.903 201.195 1.00 50.58  ? 1050 LEU A N   1 
ATOM 3463 C CA  . LEU A 1 1039 ? 204.839 201.557 202.462 1.00 48.80  ? 1050 LEU A CA  1 
ATOM 3464 C C   . LEU A 1 1039 ? 203.372 201.958 202.478 1.00 53.72  ? 1050 LEU A C   1 
ATOM 3465 O O   . LEU A 1 1039 ? 202.831 202.402 201.460 1.00 58.40  ? 1050 LEU A O   1 
ATOM 3466 C CB  . LEU A 1 1039 ? 205.728 202.788 202.665 1.00 43.95  ? 1050 LEU A CB  1 
ATOM 3467 C CG  . LEU A 1 1039 ? 207.224 202.528 202.851 1.00 42.93  ? 1050 LEU A CG  1 
ATOM 3468 C CD1 . LEU A 1 1039 ? 207.986 203.837 202.968 1.00 38.16  ? 1050 LEU A CD1 1 
ATOM 3469 C CD2 . LEU A 1 1039 ? 207.469 201.656 204.070 1.00 48.07  ? 1050 LEU A CD2 1 
ATOM 3470 N N   . GLY A 1 1040 ? 202.724 201.790 203.620 1.00 50.61  ? 1051 GLY A N   1 
ATOM 3471 C CA  . GLY A 1 1040 ? 201.315 202.124 203.722 1.00 52.87  ? 1051 GLY A CA  1 
ATOM 3472 C C   . GLY A 1 1040 ? 200.954 202.563 205.119 1.00 60.68  ? 1051 GLY A C   1 
ATOM 3473 O O   . GLY A 1 1040 ? 201.479 202.047 206.110 1.00 65.04  ? 1051 GLY A O   1 
ATOM 3474 N N   . ALA A 1 1041 ? 200.032 203.518 205.194 1.00 57.49  ? 1052 ALA A N   1 
ATOM 3475 C CA  . ALA A 1 1041 ? 199.522 204.001 206.468 1.00 51.93  ? 1052 ALA A CA  1 
ATOM 3476 C C   . ALA A 1 1041 ? 198.037 204.278 206.307 1.00 55.13  ? 1052 ALA A C   1 
ATOM 3477 O O   . ALA A 1 1041 ? 197.537 204.423 205.192 1.00 58.44  ? 1052 ALA A O   1 
ATOM 3478 C CB  . ALA A 1 1041 ? 200.265 205.257 206.940 1.00 50.63  ? 1052 ALA A CB  1 
ATOM 3479 N N   . SER A 1 1042 ? 197.324 204.323 207.428 1.00 52.38  ? 1053 SER A N   1 
ATOM 3480 C CA  . SER A 1 1042 ? 195.896 204.599 207.377 1.00 46.99  ? 1053 SER A CA  1 
ATOM 3481 C C   . SER A 1 1042 ? 195.403 205.100 208.724 1.00 44.80  ? 1053 SER A C   1 
ATOM 3482 O O   . SER A 1 1042 ? 195.678 204.491 209.760 1.00 52.92  ? 1053 SER A O   1 
ATOM 3483 C CB  . SER A 1 1042 ? 195.099 203.354 206.968 1.00 46.55  ? 1053 SER A CB  1 
ATOM 3484 O OG  . SER A 1 1042 ? 195.039 202.417 208.028 1.00 49.12  ? 1053 SER A OG  1 
ATOM 3485 N N   . GLY A 1 1043 ? 194.676 206.213 208.697 1.00 38.92  ? 1054 GLY A N   1 
ATOM 3486 C CA  . GLY A 1 1043 ? 193.945 206.670 209.859 1.00 41.15  ? 1054 GLY A CA  1 
ATOM 3487 C C   . GLY A 1 1043 ? 192.456 206.428 209.684 1.00 40.72  ? 1054 GLY A C   1 
ATOM 3488 O O   . GLY A 1 1043 ? 191.905 206.599 208.599 1.00 46.18  ? 1054 GLY A O   1 
ATOM 3489 N N   . SER A 1 1044 ? 191.800 206.033 210.772 1.00 37.30  ? 1055 SER A N   1 
ATOM 3490 C CA  . SER A 1 1044 ? 190.419 205.587 210.671 1.00 32.90  ? 1055 SER A CA  1 
ATOM 3491 C C   . SER A 1 1044 ? 189.653 205.993 211.919 1.00 34.01  ? 1055 SER A C   1 
ATOM 3492 O O   . SER A 1 1044 ? 190.233 206.256 212.974 1.00 43.10  ? 1055 SER A O   1 
ATOM 3493 C CB  . SER A 1 1044 ? 190.338 204.070 210.470 1.00 30.80  ? 1055 SER A CB  1 
ATOM 3494 O OG  . SER A 1 1044 ? 190.705 203.380 211.651 1.00 31.10  ? 1055 SER A OG  1 
ATOM 3495 N N   . TRP A 1 1045 ? 188.334 206.039 211.770 1.00 28.71  ? 1056 TRP A N   1 
ATOM 3496 C CA  . TRP A 1 1045 ? 187.397 206.268 212.859 1.00 27.18  ? 1056 TRP A CA  1 
ATOM 3497 C C   . TRP A 1 1045 ? 186.392 205.128 212.870 1.00 31.00  ? 1056 TRP A C   1 
ATOM 3498 O O   . TRP A 1 1045 ? 185.836 204.772 211.824 1.00 40.25  ? 1056 TRP A O   1 
ATOM 3499 C CB  . TRP A 1 1045 ? 186.682 207.618 212.703 1.00 26.20  ? 1056 TRP A CB  1 
ATOM 3500 C CG  . TRP A 1 1045 ? 185.698 207.928 213.790 1.00 29.53  ? 1056 TRP A CG  1 
ATOM 3501 C CD1 . TRP A 1 1045 ? 185.922 208.673 214.910 1.00 36.86  ? 1056 TRP A CD1 1 
ATOM 3502 C CD2 . TRP A 1 1045 ? 184.322 207.530 213.843 1.00 34.19  ? 1056 TRP A CD2 1 
ATOM 3503 N NE1 . TRP A 1 1045 ? 184.779 208.749 215.666 1.00 38.80  ? 1056 TRP A NE1 1 
ATOM 3504 C CE2 . TRP A 1 1045 ? 183.781 208.057 215.033 1.00 40.58  ? 1056 TRP A CE2 1 
ATOM 3505 C CE3 . TRP A 1 1045 ? 183.496 206.774 213.005 1.00 41.66  ? 1056 TRP A CE3 1 
ATOM 3506 C CZ2 . TRP A 1 1045 ? 182.454 207.852 215.404 1.00 44.84  ? 1056 TRP A CZ2 1 
ATOM 3507 C CZ3 . TRP A 1 1045 ? 182.180 206.571 213.376 1.00 44.73  ? 1056 TRP A CZ3 1 
ATOM 3508 C CH2 . TRP A 1 1045 ? 181.672 207.109 214.565 1.00 45.31  ? 1056 TRP A CH2 1 
ATOM 3509 N N   . SER A 1 1046 ? 186.160 204.554 214.050 1.00 31.73  ? 1057 SER A N   1 
ATOM 3510 C CA  . SER A 1 1046 ? 185.336 203.361 214.160 1.00 33.36  ? 1057 SER A CA  1 
ATOM 3511 C C   . SER A 1 1046 ? 184.375 203.486 215.333 1.00 36.25  ? 1057 SER A C   1 
ATOM 3512 O O   . SER A 1 1046 ? 184.729 203.992 216.401 1.00 46.19  ? 1057 SER A O   1 
ATOM 3513 C CB  . SER A 1 1046 ? 186.195 202.100 214.328 1.00 34.59  ? 1057 SER A CB  1 
ATOM 3514 O OG  . SER A 1 1046 ? 186.903 202.125 215.555 1.00 47.01  ? 1057 SER A OG  1 
ATOM 3515 N N   . HIS A 1 1047 ? 183.157 202.996 215.118 1.00 29.98  ? 1058 HIS A N   1 
ATOM 3516 C CA  . HIS A 1 1047 ? 182.114 202.925 216.130 1.00 31.94  ? 1058 HIS A CA  1 
ATOM 3517 C C   . HIS A 1 1047 ? 181.636 201.485 216.246 1.00 32.11  ? 1058 HIS A C   1 
ATOM 3518 O O   . HIS A 1 1047 ? 181.500 200.786 215.238 1.00 38.28  ? 1058 HIS A O   1 
ATOM 3519 C CB  . HIS A 1 1047 ? 180.939 203.846 215.779 1.00 32.65  ? 1058 HIS A CB  1 
ATOM 3520 C CG  . HIS A 1 1047 ? 179.675 203.527 216.515 1.00 37.30  ? 1058 HIS A CG  1 
ATOM 3521 N ND1 . HIS A 1 1047 ? 179.405 204.014 217.776 1.00 45.91  ? 1058 HIS A ND1 1 
ATOM 3522 C CD2 . HIS A 1 1047 ? 178.605 202.775 216.166 1.00 34.57  ? 1058 HIS A CD2 1 
ATOM 3523 C CE1 . HIS A 1 1047 ? 178.224 203.574 218.173 1.00 44.25  ? 1058 HIS A CE1 1 
ATOM 3524 N NE2 . HIS A 1 1047 ? 177.718 202.819 217.214 1.00 38.19  ? 1058 HIS A NE2 1 
ATOM 3525 N N   . SER A 1 1048 ? 181.389 201.037 217.476 1.00 30.08  ? 1059 SER A N   1 
ATOM 3526 C CA  . SER A 1 1048 ? 180.984 199.663 217.724 1.00 30.16  ? 1059 SER A CA  1 
ATOM 3527 C C   . SER A 1 1048 ? 179.989 199.619 218.873 1.00 32.44  ? 1059 SER A C   1 
ATOM 3528 O O   . SER A 1 1048 ? 180.060 200.420 219.809 1.00 40.32  ? 1059 SER A O   1 
ATOM 3529 C CB  . SER A 1 1048 ? 182.191 198.773 218.045 1.00 30.00  ? 1059 SER A CB  1 
ATOM 3530 O OG  . SER A 1 1048 ? 181.809 197.415 218.158 1.00 32.79  ? 1059 SER A OG  1 
ATOM 3531 N N   . ARG A 1 1049 ? 179.051 198.676 218.786 1.00 28.55  ? 1060 ARG A N   1 
ATOM 3532 C CA  . ARG A 1 1049 ? 178.079 198.452 219.847 1.00 26.50  ? 1060 ARG A CA  1 
ATOM 3533 C C   . ARG A 1 1049 ? 177.942 196.959 220.105 1.00 25.44  ? 1060 ARG A C   1 
ATOM 3534 O O   . ARG A 1 1049 ? 177.952 196.157 219.167 1.00 31.29  ? 1060 ARG A O   1 
ATOM 3535 C CB  . ARG A 1 1049 ? 176.709 199.049 219.493 1.00 32.76  ? 1060 ARG A CB  1 
ATOM 3536 C CG  . ARG A 1 1049 ? 175.638 198.816 220.549 1.00 34.51  ? 1060 ARG A CG  1 
ATOM 3537 C CD  . ARG A 1 1049 ? 174.388 199.637 220.273 1.00 41.35  ? 1060 ARG A CD  1 
ATOM 3538 N NE  . ARG A 1 1049 ? 173.861 199.402 218.934 1.00 57.47  ? 1060 ARG A NE  1 
ATOM 3539 C CZ  . ARG A 1 1049 ? 173.158 198.334 218.581 1.00 58.01  ? 1060 ARG A CZ  1 
ATOM 3540 N NH1 . ARG A 1 1049 ? 172.870 197.378 219.448 1.00 58.92  ? 1060 ARG A NH1 1 
ATOM 3541 N NH2 . ARG A 1 1049 ? 172.731 198.225 217.326 1.00 47.94  ? 1060 ARG A NH2 1 
ATOM 3542 N N   . THR A 1 1050 ? 177.815 196.590 221.380 1.00 29.40  ? 1061 THR A N   1 
ATOM 3543 C CA  . THR A 1 1050 ? 177.614 195.208 221.786 1.00 32.91  ? 1061 THR A CA  1 
ATOM 3544 C C   . THR A 1 1050 ? 176.470 195.139 222.787 1.00 36.50  ? 1061 THR A C   1 
ATOM 3545 O O   . THR A 1 1050 ? 176.361 195.988 223.677 1.00 40.68  ? 1061 THR A O   1 
ATOM 3546 C CB  . THR A 1 1050 ? 178.883 194.612 222.407 1.00 42.96  ? 1061 THR A CB  1 
ATOM 3547 O OG1 . THR A 1 1050 ? 179.267 195.386 223.550 1.00 46.07  ? 1061 THR A OG1 1 
ATOM 3548 C CG2 . THR A 1 1050 ? 180.020 194.613 221.398 1.00 40.41  ? 1061 THR A CG2 1 
ATOM 3549 N N   . LYS A 1 1051 ? 175.625 194.126 222.640 1.00 34.74  ? 1062 LYS A N   1 
ATOM 3550 C CA  . LYS A 1 1051 ? 174.462 193.956 223.497 1.00 38.81  ? 1062 LYS A CA  1 
ATOM 3551 C C   . LYS A 1 1051 ? 174.816 193.141 224.737 1.00 46.57  ? 1062 LYS A C   1 
ATOM 3552 O O   . LYS A 1 1051 ? 175.835 192.448 224.789 1.00 48.03  ? 1062 LYS A O   1 
ATOM 3553 C CB  . LYS A 1 1051 ? 173.325 193.273 222.737 1.00 42.09  ? 1062 LYS A CB  1 
ATOM 3554 C CG  . LYS A 1 1051 ? 173.549 191.787 222.502 1.00 42.78  ? 1062 LYS A CG  1 
ATOM 3555 C CD  . LYS A 1 1051 ? 172.338 191.135 221.857 1.00 44.36  ? 1062 LYS A CD  1 
ATOM 3556 C CE  . LYS A 1 1051 ? 172.438 189.619 221.911 1.00 48.28  ? 1062 LYS A CE  1 
ATOM 3557 N NZ  . LYS A 1 1051 ? 171.246 188.959 221.312 1.00 55.94  ? 1062 LYS A NZ  1 
ATOM 3558 N N   . THR A 1 1052 ? 173.954 193.239 225.746 1.00 51.63  ? 1063 THR A N   1 
ATOM 3559 C CA  . THR A 1 1052 ? 174.114 192.433 226.949 1.00 47.54  ? 1063 THR A CA  1 
ATOM 3560 C C   . THR A 1 1052 ? 173.897 190.961 226.624 1.00 48.27  ? 1063 THR A C   1 
ATOM 3561 O O   . THR A 1 1052 ? 172.912 190.594 225.976 1.00 54.98  ? 1063 THR A O   1 
ATOM 3562 C CB  . THR A 1 1052 ? 173.131 192.891 228.027 1.00 48.86  ? 1063 THR A CB  1 
ATOM 3563 O OG1 . THR A 1 1052 ? 173.395 194.258 228.368 1.00 49.15  ? 1063 THR A OG1 1 
ATOM 3564 C CG2 . THR A 1 1052 ? 173.263 192.029 229.274 1.00 50.61  ? 1063 THR A CG2 1 
ATOM 3565 N N   . MET A 1 1053 ? 174.820 190.116 227.080 1.00 47.38  ? 1064 MET A N   1 
ATOM 3566 C CA  . MET A 1 1053 ? 174.786 188.697 226.774 1.00 50.87  ? 1064 MET A CA  1 
ATOM 3567 C C   . MET A 1 1053 ? 174.945 187.881 228.049 1.00 51.73  ? 1064 MET A C   1 
ATOM 3568 O O   . MET A 1 1053 ? 175.743 188.244 228.923 1.00 57.41  ? 1064 MET A O   1 
ATOM 3569 C CB  . MET A 1 1053 ? 175.900 188.332 225.780 1.00 48.88  ? 1064 MET A CB  1 
ATOM 3570 C CG  . MET A 1 1053 ? 175.738 186.977 225.112 1.00 49.80  ? 1064 MET A CG  1 
ATOM 3571 S SD  . MET A 1 1053 ? 174.584 187.017 223.728 1.00 64.77  ? 1064 MET A SD  1 
ATOM 3572 C CE  . MET A 1 1053 ? 174.117 185.291 223.628 1.00 59.75  ? 1064 MET A CE  1 
ATOM 3573 N N   . PRO A 1 1054 ? 174.196 186.788 228.194 1.00 47.57  ? 1065 PRO A N   1 
ATOM 3574 C CA  . PRO A 1 1054 ? 174.413 185.898 229.340 1.00 46.01  ? 1065 PRO A CA  1 
ATOM 3575 C C   . PRO A 1 1054 ? 175.814 185.305 229.314 1.00 47.25  ? 1065 PRO A C   1 
ATOM 3576 O O   . PRO A 1 1054 ? 176.371 185.021 228.252 1.00 46.19  ? 1065 PRO A O   1 
ATOM 3577 C CB  . PRO A 1 1054 ? 173.335 184.822 229.164 1.00 46.53  ? 1065 PRO A CB  1 
ATOM 3578 C CG  . PRO A 1 1054 ? 172.979 184.875 227.713 1.00 47.87  ? 1065 PRO A CG  1 
ATOM 3579 C CD  . PRO A 1 1054 ? 173.090 186.322 227.342 1.00 49.34  ? 1065 PRO A CD  1 
ATOM 3580 N N   . ARG A 1 1055 ? 176.384 185.122 230.507 1.00 46.06  ? 1066 ARG A N   1 
ATOM 3581 C CA  . ARG A 1 1055 ? 177.768 184.670 230.600 1.00 42.38  ? 1066 ARG A CA  1 
ATOM 3582 C C   . ARG A 1 1055 ? 177.917 183.206 230.206 1.00 41.05  ? 1066 ARG A C   1 
ATOM 3583 O O   . ARG A 1 1055 ? 178.961 182.815 229.673 1.00 44.51  ? 1066 ARG A O   1 
ATOM 3584 C CB  . ARG A 1 1055 ? 178.296 184.898 232.017 1.00 42.94  ? 1066 ARG A CB  1 
ATOM 3585 C CG  . ARG A 1 1055 ? 179.790 184.671 232.172 1.00 41.99  ? 1066 ARG A CG  1 
ATOM 3586 C CD  . ARG A 1 1055 ? 180.294 185.237 233.488 1.00 39.79  ? 1066 ARG A CD  1 
ATOM 3587 N NE  . ARG A 1 1055 ? 180.281 186.694 233.489 1.00 43.32  ? 1066 ARG A NE  1 
ATOM 3588 C CZ  . ARG A 1 1055 ? 180.383 187.443 234.578 1.00 47.97  ? 1066 ARG A CZ  1 
ATOM 3589 N NH1 . ARG A 1 1055 ? 180.507 186.903 235.779 1.00 47.84  ? 1066 ARG A NH1 1 
ATOM 3590 N NH2 . ARG A 1 1055 ? 180.358 188.768 234.460 1.00 54.76  ? 1066 ARG A NH2 1 
ATOM 3591 N N   . TYR A 1 1056 ? 176.894 182.386 230.449 1.00 38.97  ? 1067 TYR A N   1 
ATOM 3592 C CA  . TYR A 1 1056 ? 176.937 180.952 230.172 1.00 39.34  ? 1067 TYR A CA  1 
ATOM 3593 C C   . TYR A 1 1056 ? 175.727 180.565 229.328 1.00 46.17  ? 1067 TYR A C   1 
ATOM 3594 O O   . TYR A 1 1056 ? 174.750 180.003 229.842 1.00 54.38  ? 1067 TYR A O   1 
ATOM 3595 C CB  . TYR A 1 1056 ? 176.979 180.145 231.468 1.00 37.77  ? 1067 TYR A CB  1 
ATOM 3596 C CG  . TYR A 1 1056 ? 178.233 180.369 232.283 1.00 36.44  ? 1067 TYR A CG  1 
ATOM 3597 C CD1 . TYR A 1 1056 ? 179.448 179.828 231.886 1.00 39.60  ? 1067 TYR A CD1 1 
ATOM 3598 C CD2 . TYR A 1 1056 ? 178.203 181.125 233.447 1.00 33.95  ? 1067 TYR A CD2 1 
ATOM 3599 C CE1 . TYR A 1 1056 ? 180.596 180.031 232.626 1.00 38.01  ? 1067 TYR A CE1 1 
ATOM 3600 C CE2 . TYR A 1 1056 ? 179.346 181.333 234.193 1.00 34.18  ? 1067 TYR A CE2 1 
ATOM 3601 C CZ  . TYR A 1 1056 ? 180.539 180.784 233.778 1.00 34.44  ? 1067 TYR A CZ  1 
ATOM 3602 O OH  . TYR A 1 1056 ? 181.680 180.990 234.518 1.00 41.31  ? 1067 TYR A OH  1 
ATOM 3603 N N   . PRO A 1 1057 ? 175.756 180.863 228.025 1.00 41.34  ? 1068 PRO A N   1 
ATOM 3604 C CA  . PRO A 1 1057 ? 174.606 180.515 227.173 1.00 41.51  ? 1068 PRO A CA  1 
ATOM 3605 C C   . PRO A 1 1057 ? 174.318 179.025 227.114 1.00 47.94  ? 1068 PRO A C   1 
ATOM 3606 O O   . PRO A 1 1057 ? 173.145 178.639 227.032 1.00 52.39  ? 1068 PRO A O   1 
ATOM 3607 C CB  . PRO A 1 1057 ? 175.008 181.068 225.798 1.00 37.71  ? 1068 PRO A CB  1 
ATOM 3608 C CG  . PRO A 1 1057 ? 176.498 181.138 225.838 1.00 34.50  ? 1068 PRO A CG  1 
ATOM 3609 C CD  . PRO A 1 1057 ? 176.853 181.473 227.256 1.00 36.14  ? 1068 PRO A CD  1 
ATOM 3610 N N   . LEU A 1 1058 ? 175.345 178.175 227.155 1.00 47.58  ? 1069 LEU A N   1 
ATOM 3611 C CA  . LEU A 1 1058 ? 175.155 176.724 227.115 1.00 47.93  ? 1069 LEU A CA  1 
ATOM 3612 C C   . LEU A 1 1058 ? 174.924 176.232 228.540 1.00 51.09  ? 1069 LEU A C   1 
ATOM 3613 O O   . LEU A 1 1058 ? 175.845 175.855 229.267 1.00 55.05  ? 1069 LEU A O   1 
ATOM 3614 C CB  . LEU A 1 1058 ? 176.348 176.040 226.460 1.00 42.99  ? 1069 LEU A CB  1 
ATOM 3615 C CG  . LEU A 1 1058 ? 176.269 175.832 224.944 1.00 47.14  ? 1069 LEU A CG  1 
ATOM 3616 C CD1 . LEU A 1 1058 ? 174.996 175.087 224.573 1.00 44.50  ? 1069 LEU A CD1 1 
ATOM 3617 C CD2 . LEU A 1 1058 ? 176.355 177.155 224.199 1.00 49.18  ? 1069 LEU A CD2 1 
ATOM 3618 N N   . MET A 1 1059 ? 173.651 176.242 228.939 1.00 49.59  ? 1070 MET A N   1 
ATOM 3619 C CA  . MET A 1 1059 ? 173.287 175.914 230.312 1.00 48.31  ? 1070 MET A CA  1 
ATOM 3620 C C   . MET A 1 1059 ? 173.488 174.441 230.642 1.00 50.74  ? 1070 MET A C   1 
ATOM 3621 O O   . MET A 1 1059 ? 173.733 174.111 231.807 1.00 49.49  ? 1070 MET A O   1 
ATOM 3622 C CB  . MET A 1 1059 ? 171.832 176.307 230.571 1.00 52.16  ? 1070 MET A CB  1 
ATOM 3623 C CG  . MET A 1 1059 ? 171.555 176.756 231.993 1.00 62.20  ? 1070 MET A CG  1 
ATOM 3624 S SD  . MET A 1 1059 ? 172.627 178.114 232.499 1.00 62.10  ? 1070 MET A SD  1 
ATOM 3625 C CE  . MET A 1 1059 ? 172.208 178.236 234.234 1.00 53.33  ? 1070 MET A CE  1 
ATOM 3626 N N   . ASN A 1 1060 ? 173.389 173.551 229.653 1.00 53.48  ? 1071 ASN A N   1 
ATOM 3627 C CA  . ASN A 1 1060 ? 173.486 172.121 229.921 1.00 61.77  ? 1071 ASN A CA  1 
ATOM 3628 C C   . ASN A 1 1060 ? 174.891 171.677 230.305 1.00 61.33  ? 1071 ASN A C   1 
ATOM 3629 O O   . ASN A 1 1060 ? 175.039 170.609 230.907 1.00 66.13  ? 1071 ASN A O   1 
ATOM 3630 C CB  . ASN A 1 1060 ? 173.009 171.328 228.703 1.00 62.56  ? 1071 ASN A CB  1 
ATOM 3631 C CG  . ASN A 1 1060 ? 171.503 171.151 228.677 1.00 68.36  ? 1071 ASN A CG  1 
ATOM 3632 O OD1 . ASN A 1 1060 ? 170.809 171.502 229.632 1.00 64.08  ? 1071 ASN A OD1 1 
ATOM 3633 N ND2 . ASN A 1 1060 ? 170.990 170.605 227.582 1.00 69.30  ? 1071 ASN A ND2 1 
ATOM 3634 N N   . LEU A 1 1061 ? 175.920 172.460 229.975 1.00 55.56  ? 1072 LEU A N   1 
ATOM 3635 C CA  . LEU A 1 1061 ? 177.281 172.094 230.352 1.00 44.83  ? 1072 LEU A CA  1 
ATOM 3636 C C   . LEU A 1 1061 ? 177.559 172.360 231.826 1.00 48.79  ? 1072 LEU A C   1 
ATOM 3637 O O   . LEU A 1 1061 ? 178.406 171.686 232.423 1.00 52.17  ? 1072 LEU A O   1 
ATOM 3638 C CB  . LEU A 1 1061 ? 178.288 172.854 229.487 1.00 40.20  ? 1072 LEU A CB  1 
ATOM 3639 C CG  . LEU A 1 1061 ? 178.096 172.763 227.973 1.00 47.15  ? 1072 LEU A CG  1 
ATOM 3640 C CD1 . LEU A 1 1061 ? 179.156 173.578 227.248 1.00 43.75  ? 1072 LEU A CD1 1 
ATOM 3641 C CD2 . LEU A 1 1061 ? 178.122 171.314 227.513 1.00 48.76  ? 1072 LEU A CD2 1 
ATOM 3642 N N   . ILE A 1 1062 ? 176.867 173.323 232.419 1.00 54.50  ? 1073 ILE A N   1 
ATOM 3643 C CA  . ILE A 1 1062 ? 177.121 173.709 233.808 1.00 52.48  ? 1073 ILE A CA  1 
ATOM 3644 C C   . ILE A 1 1062 ? 176.614 172.603 234.731 1.00 54.48  ? 1073 ILE A C   1 
ATOM 3645 O O   . ILE A 1 1062 ? 175.531 172.050 234.483 1.00 57.64  ? 1073 ILE A O   1 
ATOM 3646 C CB  . ILE A 1 1062 ? 176.446 175.040 234.123 1.00 45.86  ? 1073 ILE A CB  1 
ATOM 3647 C CG1 . ILE A 1 1062 ? 176.870 176.102 233.108 1.00 42.89  ? 1073 ILE A CG1 1 
ATOM 3648 C CG2 . ILE A 1 1062 ? 176.782 175.496 235.534 1.00 50.20  ? 1073 ILE A CG2 1 
ATOM 3649 C CD1 . ILE A 1 1062 ? 178.368 176.280 233.002 1.00 35.60  ? 1073 ILE A CD1 1 
ATOM 3650 N N   . PRO A 1 1063 ? 177.359 172.247 235.778 1.00 51.26  ? 1074 PRO A N   1 
ATOM 3651 C CA  . PRO A 1 1063 ? 176.857 171.266 236.746 1.00 50.69  ? 1074 PRO A CA  1 
ATOM 3652 C C   . PRO A 1 1063 ? 175.552 171.726 237.383 1.00 54.51  ? 1074 PRO A C   1 
ATOM 3653 O O   . PRO A 1 1063 ? 175.230 172.916 237.403 1.00 55.35  ? 1074 PRO A O   1 
ATOM 3654 C CB  . PRO A 1 1063 ? 177.986 171.181 237.777 1.00 54.54  ? 1074 PRO A CB  1 
ATOM 3655 C CG  . PRO A 1 1063 ? 179.211 171.504 236.993 1.00 52.23  ? 1074 PRO A CG  1 
ATOM 3656 C CD  . PRO A 1 1063 ? 178.784 172.553 235.997 1.00 52.36  ? 1074 PRO A CD  1 
ATOM 3657 N N   . THR A 1 1064 ? 174.797 170.756 237.906 1.00 59.05  ? 1075 THR A N   1 
ATOM 3658 C CA  . THR A 1 1064 ? 173.467 171.035 238.436 1.00 61.75  ? 1075 THR A CA  1 
ATOM 3659 C C   . THR A 1 1064 ? 173.491 171.984 239.628 1.00 63.41  ? 1075 THR A C   1 
ATOM 3660 O O   . THR A 1 1064 ? 172.540 172.750 239.812 1.00 64.17  ? 1075 THR A O   1 
ATOM 3661 C CB  . THR A 1 1064 ? 172.777 169.730 238.837 1.00 61.15  ? 1075 THR A CB  1 
ATOM 3662 O OG1 . THR A 1 1064 ? 173.543 169.077 239.857 1.00 62.83  ? 1075 THR A OG1 1 
ATOM 3663 C CG2 . THR A 1 1064 ? 172.654 168.804 237.637 1.00 60.75  ? 1075 THR A CG2 1 
ATOM 3664 N N   . ASP A 1 1065 ? 174.547 171.951 240.442 1.00 62.65  ? 1076 ASP A N   1 
ATOM 3665 C CA  . ASP A 1 1065 ? 174.581 172.781 241.642 1.00 59.63  ? 1076 ASP A CA  1 
ATOM 3666 C C   . ASP A 1 1065 ? 174.822 174.249 241.301 1.00 60.99  ? 1076 ASP A C   1 
ATOM 3667 O O   . ASP A 1 1065 ? 174.218 175.141 241.907 1.00 61.17  ? 1076 ASP A O   1 
ATOM 3668 C CB  . ASP A 1 1065 ? 175.652 172.265 242.605 1.00 64.67  ? 1076 ASP A CB  1 
ATOM 3669 C CG  . ASP A 1 1065 ? 176.045 173.295 243.646 1.00 72.67  ? 1076 ASP A CG  1 
ATOM 3670 O OD1 . ASP A 1 1065 ? 175.190 173.650 244.484 1.00 74.39  ? 1076 ASP A OD1 1 
ATOM 3671 O OD2 . ASP A 1 1065 ? 177.210 173.743 243.632 1.00 75.41  ? 1076 ASP A OD2 1 
ATOM 3672 N N   . TRP A 1 1066 ? 175.698 174.518 240.332 1.00 57.68  ? 1077 TRP A N   1 
ATOM 3673 C CA  . TRP A 1 1066 ? 176.026 175.886 239.950 1.00 55.92  ? 1077 TRP A CA  1 
ATOM 3674 C C   . TRP A 1 1066 ? 174.958 176.542 239.085 1.00 56.63  ? 1077 TRP A C   1 
ATOM 3675 O O   . TRP A 1 1066 ? 175.073 177.741 238.803 1.00 60.26  ? 1077 TRP A O   1 
ATOM 3676 C CB  . TRP A 1 1066 ? 177.364 175.925 239.206 1.00 50.70  ? 1077 TRP A CB  1 
ATOM 3677 C CG  . TRP A 1 1066 ? 178.512 175.348 239.975 1.00 50.84  ? 1077 TRP A CG  1 
ATOM 3678 C CD1 . TRP A 1 1066 ? 178.564 175.107 241.315 1.00 50.67  ? 1077 TRP A CD1 1 
ATOM 3679 C CD2 . TRP A 1 1066 ? 179.779 174.940 239.444 1.00 48.59  ? 1077 TRP A CD2 1 
ATOM 3680 N NE1 . TRP A 1 1066 ? 179.783 174.572 241.654 1.00 50.09  ? 1077 TRP A NE1 1 
ATOM 3681 C CE2 . TRP A 1 1066 ? 180.547 174.460 240.522 1.00 50.40  ? 1077 TRP A CE2 1 
ATOM 3682 C CE3 . TRP A 1 1066 ? 180.337 174.934 238.163 1.00 46.18  ? 1077 TRP A CE3 1 
ATOM 3683 C CZ2 . TRP A 1 1066 ? 181.844 173.979 240.358 1.00 50.75  ? 1077 TRP A CZ2 1 
ATOM 3684 C CZ3 . TRP A 1 1066 ? 181.623 174.456 238.002 1.00 44.29  ? 1077 TRP A CZ3 1 
ATOM 3685 C CH2 . TRP A 1 1066 ? 182.362 173.985 239.093 1.00 49.03  ? 1077 TRP A CH2 1 
ATOM 3686 N N   . GLN A 1 1067 ? 173.933 175.792 238.668 1.00 58.82  ? 1078 GLN A N   1 
ATOM 3687 C CA  . GLN A 1 1067 ? 172.950 176.300 237.713 1.00 62.49  ? 1078 GLN A CA  1 
ATOM 3688 C C   . GLN A 1 1067 ? 172.383 177.646 238.148 1.00 70.76  ? 1078 GLN A C   1 
ATOM 3689 O O   . GLN A 1 1067 ? 172.466 178.636 237.411 1.00 69.28  ? 1078 GLN A O   1 
ATOM 3690 C CB  . GLN A 1 1067 ? 171.823 175.280 237.539 1.00 59.15  ? 1078 GLN A CB  1 
ATOM 3691 C CG  . GLN A 1 1067 ? 172.212 174.040 236.754 1.00 54.45  ? 1078 GLN A CG  1 
ATOM 3692 C CD  . GLN A 1 1067 ? 172.225 174.277 235.258 1.00 66.77  ? 1078 GLN A CD  1 
ATOM 3693 O OE1 . GLN A 1 1067 ? 171.351 174.954 234.718 1.00 73.63  ? 1078 GLN A OE1 1 
ATOM 3694 N NE2 . GLN A 1 1067 ? 173.219 173.716 234.579 1.00 63.17  ? 1078 GLN A NE2 1 
ATOM 3695 N N   . GLU A 1 1068 ? 171.832 177.707 239.364 1.00 74.65  ? 1079 GLU A N   1 
ATOM 3696 C CA  . GLU A 1 1068 ? 171.203 178.937 239.836 1.00 73.55  ? 1079 GLU A CA  1 
ATOM 3697 C C   . GLU A 1 1068 ? 172.176 180.107 239.838 1.00 67.67  ? 1079 GLU A C   1 
ATOM 3698 O O   . GLU A 1 1068 ? 171.761 181.256 239.646 1.00 67.04  ? 1079 GLU A O   1 
ATOM 3699 C CB  . GLU A 1 1068 ? 170.623 178.727 241.235 1.00 79.91  ? 1079 GLU A CB  1 
ATOM 3700 C CG  . GLU A 1 1068 ? 169.533 177.670 241.301 1.00 85.09  ? 1079 GLU A CG  1 
ATOM 3701 C CD  . GLU A 1 1068 ? 168.748 177.722 242.597 1.00 99.72  ? 1079 GLU A CD  1 
ATOM 3702 O OE1 . GLU A 1 1068 ? 169.272 178.271 243.589 1.00 100.93 ? 1079 GLU A OE1 1 
ATOM 3703 O OE2 . GLU A 1 1068 ? 167.607 177.215 242.624 1.00 105.03 ? 1079 GLU A OE2 1 
ATOM 3704 N N   . GLU A 1 1069 ? 173.466 179.844 240.051 1.00 64.91  ? 1080 GLU A N   1 
ATOM 3705 C CA  . GLU A 1 1069 ? 174.452 180.913 239.964 1.00 61.91  ? 1080 GLU A CA  1 
ATOM 3706 C C   . GLU A 1 1069 ? 174.691 181.335 238.519 1.00 60.90  ? 1080 GLU A C   1 
ATOM 3707 O O   . GLU A 1 1069 ? 174.728 182.534 238.218 1.00 60.14  ? 1080 GLU A O   1 
ATOM 3708 C CB  . GLU A 1 1069 ? 175.763 180.474 240.618 1.00 61.97  ? 1080 GLU A CB  1 
ATOM 3709 C CG  . GLU A 1 1069 ? 175.606 179.981 242.047 1.00 75.16  ? 1080 GLU A CG  1 
ATOM 3710 C CD  . GLU A 1 1069 ? 176.937 179.697 242.715 1.00 80.63  ? 1080 GLU A CD  1 
ATOM 3711 O OE1 . GLU A 1 1069 ? 177.929 180.378 242.380 1.00 71.17  ? 1080 GLU A OE1 1 
ATOM 3712 O OE2 . GLU A 1 1069 ? 176.991 178.793 243.575 1.00 86.24  ? 1080 GLU A OE2 1 
ATOM 3713 N N   . ALA A 1 1070 ? 174.829 180.363 237.612 1.00 60.22  ? 1081 ALA A N   1 
ATOM 3714 C CA  . ALA A 1 1070 ? 175.212 180.681 236.240 1.00 51.47  ? 1081 ALA A CA  1 
ATOM 3715 C C   . ALA A 1 1070 ? 174.154 181.516 235.535 1.00 60.85  ? 1081 ALA A C   1 
ATOM 3716 O O   . ALA A 1 1070 ? 174.488 182.367 234.702 1.00 64.32  ? 1081 ALA A O   1 
ATOM 3717 C CB  . ALA A 1 1070 ? 175.482 179.395 235.458 1.00 52.24  ? 1081 ALA A CB  1 
ATOM 3718 N N   . ALA A 1 1071 ? 172.878 181.293 235.852 1.00 64.10  ? 1082 ALA A N   1 
ATOM 3719 C CA  . ALA A 1 1071 ? 171.813 182.079 235.243 1.00 59.17  ? 1082 ALA A CA  1 
ATOM 3720 C C   . ALA A 1 1071 ? 171.792 183.518 235.740 1.00 58.23  ? 1082 ALA A C   1 
ATOM 3721 O O   . ALA A 1 1071 ? 171.136 184.362 235.122 1.00 58.73  ? 1082 ALA A O   1 
ATOM 3722 C CB  . ALA A 1 1071 ? 170.458 181.420 235.502 1.00 57.72  ? 1082 ALA A CB  1 
ATOM 3723 N N   . ARG A 1 1072 ? 172.489 183.819 236.835 1.00 60.20  ? 1083 ARG A N   1 
ATOM 3724 C CA  . ARG A 1 1072 ? 172.469 185.152 237.422 1.00 60.37  ? 1083 ARG A CA  1 
ATOM 3725 C C   . ARG A 1 1072 ? 173.634 186.022 236.966 1.00 62.73  ? 1083 ARG A C   1 
ATOM 3726 O O   . ARG A 1 1072 ? 173.728 187.179 237.386 1.00 66.24  ? 1083 ARG A O   1 
ATOM 3727 C CB  . ARG A 1 1072 ? 172.460 185.048 238.952 1.00 60.65  ? 1083 ARG A CB  1 
ATOM 3728 C CG  . ARG A 1 1072 ? 171.842 186.245 239.661 1.00 65.42  ? 1083 ARG A CG  1 
ATOM 3729 C CD  . ARG A 1 1072 ? 171.436 185.898 241.084 1.00 77.05  ? 1083 ARG A CD  1 
ATOM 3730 N NE  . ARG A 1 1072 ? 170.654 184.669 241.141 1.00 81.16  ? 1083 ARG A NE  1 
ATOM 3731 C CZ  . ARG A 1 1072 ? 171.002 183.590 241.829 1.00 79.57  ? 1083 ARG A CZ  1 
ATOM 3732 N NH1 . ARG A 1 1072 ? 172.121 183.551 242.534 1.00 79.39  ? 1083 ARG A NH1 1 
ATOM 3733 N NH2 . ARG A 1 1072 ? 170.208 182.523 241.808 1.00 77.87  ? 1083 ARG A NH2 1 
ATOM 3734 N N   . GLN A 1 1073 ? 174.514 185.505 236.113 1.00 56.31  ? 1084 GLN A N   1 
ATOM 3735 C CA  . GLN A 1 1073 ? 175.677 186.241 235.637 1.00 48.45  ? 1084 GLN A CA  1 
ATOM 3736 C C   . GLN A 1 1073 ? 175.517 186.548 234.155 1.00 47.59  ? 1084 GLN A C   1 
ATOM 3737 O O   . GLN A 1 1073 ? 175.156 185.666 233.369 1.00 46.50  ? 1084 GLN A O   1 
ATOM 3738 C CB  . GLN A 1 1073 ? 176.963 185.449 235.880 1.00 49.48  ? 1084 GLN A CB  1 
ATOM 3739 C CG  . GLN A 1 1073 ? 177.271 185.209 237.348 1.00 45.63  ? 1084 GLN A CG  1 
ATOM 3740 C CD  . GLN A 1 1073 ? 178.675 184.687 237.572 1.00 46.27  ? 1084 GLN A CD  1 
ATOM 3741 O OE1 . GLN A 1 1073 ? 179.526 184.763 236.687 1.00 46.54  ? 1084 GLN A OE1 1 
ATOM 3742 N NE2 . GLN A 1 1073 ? 178.925 184.154 238.762 1.00 45.92  ? 1084 GLN A NE2 1 
ATOM 3743 N N   . SER A 1 1074 ? 175.784 187.798 233.779 1.00 49.49  ? 1085 SER A N   1 
ATOM 3744 C CA  . SER A 1 1074 ? 175.693 188.231 232.393 1.00 51.54  ? 1085 SER A CA  1 
ATOM 3745 C C   . SER A 1 1074 ? 176.793 189.243 232.105 1.00 48.54  ? 1085 SER A C   1 
ATOM 3746 O O   . SER A 1 1074 ? 177.255 189.952 233.002 1.00 48.70  ? 1085 SER A O   1 
ATOM 3747 C CB  . SER A 1 1074 ? 174.323 188.848 232.081 1.00 52.60  ? 1085 SER A CB  1 
ATOM 3748 O OG  . SER A 1 1074 ? 174.116 190.032 232.831 1.00 56.85  ? 1085 SER A OG  1 
ATOM 3749 N N   . ASN A 1 1075 ? 177.213 189.292 230.837 1.00 49.61  ? 1086 ASN A N   1 
ATOM 3750 C CA  . ASN A 1 1075 ? 178.271 190.249 230.416 1.00 50.84  ? 1086 ASN A CA  1 
ATOM 3751 C C   . ASN A 1 1075 ? 177.595 191.547 229.978 1.00 56.55  ? 1086 ASN A C   1 
ATOM 3752 O O   . ASN A 1 1075 ? 176.741 191.486 229.072 1.00 60.22  ? 1086 ASN A O   1 
ATOM 3753 C CB  . ASN A 1 1075 ? 179.167 189.655 229.337 1.00 51.82  ? 1086 ASN A CB  1 
ATOM 3754 C CG  . ASN A 1 1075 ? 179.840 188.385 229.799 1.00 51.90  ? 1086 ASN A CG  1 
ATOM 3755 O OD1 . ASN A 1 1075 ? 180.558 188.393 230.805 1.00 50.78  ? 1086 ASN A OD1 1 
ATOM 3756 N ND2 . ASN A 1 1075 ? 179.618 187.290 229.090 1.00 44.67  ? 1086 ASN A ND2 1 
ATOM 3757 N N   . ASP A 1 1076 ? 177.965 192.670 230.590 1.00 59.51  ? 1087 ASP A N   1 
ATOM 3758 C CA  . ASP A 1 1076 ? 177.353 193.960 230.305 1.00 60.73  ? 1087 ASP A CA  1 
ATOM 3759 C C   . ASP A 1 1076 ? 177.721 194.439 228.905 1.00 60.79  ? 1087 ASP A C   1 
ATOM 3760 O O   . ASP A 1 1076 ? 178.878 194.356 228.485 1.00 62.12  ? 1087 ASP A O   1 
ATOM 3761 C CB  . ASP A 1 1076 ? 177.788 194.993 231.343 1.00 62.79  ? 1087 ASP A CB  1 
ATOM 3762 C CG  . ASP A 1 1076 ? 176.886 196.211 231.367 1.00 68.46  ? 1087 ASP A CG  1 
ATOM 3763 O OD1 . ASP A 1 1076 ? 175.755 196.124 230.844 1.00 68.61  ? 1087 ASP A OD1 1 
ATOM 3764 O OD2 . ASP A 1 1076 ? 177.308 197.254 231.907 1.00 71.22  ? 1087 ASP A OD2 1 
ATOM 3765 N N   . GLY A 1 1077 ? 176.724 194.941 228.184 1.00 55.33  ? 1088 GLY A N   1 
ATOM 3766 C CA  . GLY A 1 1077 ? 176.957 195.501 226.870 1.00 52.85  ? 1088 GLY A CA  1 
ATOM 3767 C C   . GLY A 1 1077 ? 177.427 196.941 226.934 1.00 51.84  ? 1088 GLY A C   1 
ATOM 3768 O O   . GLY A 1 1077 ? 177.519 197.561 227.994 1.00 55.83  ? 1088 GLY A O   1 
ATOM 3769 N N   . GLY A 1 1078 ? 177.733 197.486 225.758 1.00 46.48  ? 1089 GLY A N   1 
ATOM 3770 C CA  . GLY A 1 1078 ? 178.188 198.860 225.674 1.00 48.51  ? 1089 GLY A CA  1 
ATOM 3771 C C   . GLY A 1 1078 ? 178.557 199.304 224.274 1.00 43.99  ? 1089 GLY A C   1 
ATOM 3772 O O   . GLY A 1 1078 ? 178.729 198.477 223.374 1.00 48.88  ? 1089 GLY A O   1 
ATOM 3773 N N   . SER A 1 1079 ? 178.685 200.613 224.079 1.00 40.22  ? 1090 SER A N   1 
ATOM 3774 C CA  . SER A 1 1079 ? 179.047 201.182 222.791 1.00 40.48  ? 1090 SER A CA  1 
ATOM 3775 C C   . SER A 1 1079 ? 180.255 202.090 222.960 1.00 44.21  ? 1090 SER A C   1 
ATOM 3776 O O   . SER A 1 1079 ? 180.414 202.755 223.987 1.00 52.60  ? 1090 SER A O   1 
ATOM 3777 C CB  . SER A 1 1079 ? 177.883 201.969 222.175 1.00 44.73  ? 1090 SER A CB  1 
ATOM 3778 O OG  . SER A 1 1079 ? 177.495 203.044 223.013 1.00 52.30  ? 1090 SER A OG  1 
ATOM 3779 N N   . SER A 1 1080 ? 181.108 202.112 221.938 1.00 37.97  ? 1091 SER A N   1 
ATOM 3780 C CA  . SER A 1 1080 ? 182.313 202.928 221.984 1.00 38.02  ? 1091 SER A CA  1 
ATOM 3781 C C   . SER A 1 1080 ? 182.741 203.290 220.571 1.00 42.29  ? 1091 SER A C   1 
ATOM 3782 O O   . SER A 1 1080 ? 182.640 202.485 219.642 1.00 49.16  ? 1091 SER A O   1 
ATOM 3783 C CB  . SER A 1 1080 ? 183.453 202.207 222.715 1.00 41.37  ? 1091 SER A CB  1 
ATOM 3784 O OG  . SER A 1 1080 ? 183.900 201.083 221.978 1.00 41.37  ? 1091 SER A OG  1 
ATOM 3785 N N   . GLN A 1 1081 ? 183.238 204.516 220.424 1.00 42.24  ? 1092 GLN A N   1 
ATOM 3786 C CA  . GLN A 1 1081 ? 183.743 204.993 219.146 1.00 38.22  ? 1092 GLN A CA  1 
ATOM 3787 C C   . GLN A 1 1081 ? 185.030 205.766 219.386 1.00 40.79  ? 1092 GLN A C   1 
ATOM 3788 O O   . GLN A 1 1081 ? 185.229 206.354 220.452 1.00 48.69  ? 1092 GLN A O   1 
ATOM 3789 C CB  . GLN A 1 1081 ? 182.715 205.870 218.421 1.00 34.09  ? 1092 GLN A CB  1 
ATOM 3790 C CG  . GLN A 1 1081 ? 182.309 207.118 219.186 1.00 42.15  ? 1092 GLN A CG  1 
ATOM 3791 C CD  . GLN A 1 1081 ? 181.011 206.934 219.946 1.00 55.44  ? 1092 GLN A CD  1 
ATOM 3792 O OE1 . GLN A 1 1081 ? 180.736 205.857 220.475 1.00 58.24  ? 1092 GLN A OE1 1 
ATOM 3793 N NE2 . GLN A 1 1081 ? 180.204 207.986 220.002 1.00 59.00  ? 1092 GLN A NE2 1 
ATOM 3794 N N   . GLY A 1 1082 ? 185.902 205.755 218.387 1.00 36.90  ? 1093 GLY A N   1 
ATOM 3795 C CA  . GLY A 1 1082 ? 187.179 206.428 218.520 1.00 32.55  ? 1093 GLY A CA  1 
ATOM 3796 C C   . GLY A 1 1082 ? 188.034 206.253 217.284 1.00 33.24  ? 1093 GLY A C   1 
ATOM 3797 O O   . GLY A 1 1082 ? 187.682 205.523 216.349 1.00 37.92  ? 1093 GLY A O   1 
ATOM 3798 N N   . PHE A 1 1083 ? 189.171 206.944 217.301 1.00 30.66  ? 1094 PHE A N   1 
ATOM 3799 C CA  . PHE A 1 1083 ? 190.113 206.897 216.194 1.00 31.45  ? 1094 PHE A CA  1 
ATOM 3800 C C   . PHE A 1 1083 ? 191.082 205.728 216.344 1.00 36.96  ? 1094 PHE A C   1 
ATOM 3801 O O   . PHE A 1 1083 ? 191.199 205.114 217.407 1.00 48.22  ? 1094 PHE A O   1 
ATOM 3802 C CB  . PHE A 1 1083 ? 190.897 208.206 216.104 1.00 30.51  ? 1094 PHE A CB  1 
ATOM 3803 C CG  . PHE A 1 1083 ? 190.066 209.383 215.686 1.00 29.83  ? 1094 PHE A CG  1 
ATOM 3804 C CD1 . PHE A 1 1083 ? 189.833 209.642 214.347 1.00 32.84  ? 1094 PHE A CD1 1 
ATOM 3805 C CD2 . PHE A 1 1083 ? 189.518 210.230 216.633 1.00 28.49  ? 1094 PHE A CD2 1 
ATOM 3806 C CE1 . PHE A 1 1083 ? 189.069 210.725 213.959 1.00 34.71  ? 1094 PHE A CE1 1 
ATOM 3807 C CE2 . PHE A 1 1083 ? 188.753 211.315 216.251 1.00 34.17  ? 1094 PHE A CE2 1 
ATOM 3808 C CZ  . PHE A 1 1083 ? 188.528 211.563 214.912 1.00 34.30  ? 1094 PHE A CZ  1 
ATOM 3809 N N   . GLY A 1 1084 ? 191.781 205.431 215.253 1.00 31.56  ? 1095 GLY A N   1 
ATOM 3810 C CA  . GLY A 1 1084 ? 192.794 204.393 215.226 1.00 42.47  ? 1095 GLY A CA  1 
ATOM 3811 C C   . GLY A 1 1084 ? 193.657 204.565 213.997 1.00 48.23  ? 1095 GLY A C   1 
ATOM 3812 O O   . GLY A 1 1084 ? 193.369 205.377 213.116 1.00 47.92  ? 1095 GLY A O   1 
ATOM 3813 N N   . TYR A 1 1085 ? 194.728 203.778 213.942 1.00 50.95  ? 1096 TYR A N   1 
ATOM 3814 C CA  . TYR A 1 1085 ? 195.661 203.867 212.830 1.00 48.16  ? 1096 TYR A CA  1 
ATOM 3815 C C   . TYR A 1 1085 ? 196.283 202.501 212.578 1.00 54.67  ? 1096 TYR A C   1 
ATOM 3816 O O   . TYR A 1 1085 ? 196.375 201.659 213.473 1.00 62.45  ? 1096 TYR A O   1 
ATOM 3817 C CB  . TYR A 1 1085 ? 196.745 204.917 213.096 1.00 48.45  ? 1096 TYR A CB  1 
ATOM 3818 C CG  . TYR A 1 1085 ? 197.782 204.485 214.109 1.00 59.83  ? 1096 TYR A CG  1 
ATOM 3819 C CD1 . TYR A 1 1085 ? 197.528 204.574 215.471 1.00 62.27  ? 1096 TYR A CD1 1 
ATOM 3820 C CD2 . TYR A 1 1085 ? 199.016 203.994 213.703 1.00 59.25  ? 1096 TYR A CD2 1 
ATOM 3821 C CE1 . TYR A 1 1085 ? 198.471 204.181 216.401 1.00 64.94  ? 1096 TYR A CE1 1 
ATOM 3822 C CE2 . TYR A 1 1085 ? 199.966 203.599 214.626 1.00 58.77  ? 1096 TYR A CE2 1 
ATOM 3823 C CZ  . TYR A 1 1085 ? 199.688 203.695 215.973 1.00 68.30  ? 1096 TYR A CZ  1 
ATOM 3824 O OH  . TYR A 1 1085 ? 200.630 203.304 216.895 1.00 78.62  ? 1096 TYR A OH  1 
ATOM 3825 N N   . THR A 1 1086 ? 196.708 202.296 211.334 1.00 53.20  ? 1097 THR A N   1 
ATOM 3826 C CA  . THR A 1 1086 ? 197.418 201.092 210.928 1.00 52.89  ? 1097 THR A CA  1 
ATOM 3827 C C   . THR A 1 1086 ? 198.576 201.486 210.023 1.00 57.23  ? 1097 THR A C   1 
ATOM 3828 O O   . THR A 1 1086 ? 198.548 202.528 209.362 1.00 61.91  ? 1097 THR A O   1 
ATOM 3829 C CB  . THR A 1 1086 ? 196.509 200.090 210.196 1.00 52.76  ? 1097 THR A CB  1 
ATOM 3830 O OG1 . THR A 1 1086 ? 196.003 200.686 208.996 1.00 54.81  ? 1097 THR A OG1 1 
ATOM 3831 C CG2 . THR A 1 1086 ? 195.346 199.657 211.078 1.00 55.46  ? 1097 THR A CG2 1 
ATOM 3832 N N   . ALA A 1 1087 ? 199.598 200.633 209.996 1.00 55.74  ? 1098 ALA A N   1 
ATOM 3833 C CA  . ALA A 1 1087 ? 200.776 200.868 209.175 1.00 51.91  ? 1098 ALA A CA  1 
ATOM 3834 C C   . ALA A 1 1087 ? 201.303 199.533 208.670 1.00 55.77  ? 1098 ALA A C   1 
ATOM 3835 O O   . ALA A 1 1087 ? 201.100 198.492 209.299 1.00 63.76  ? 1098 ALA A O   1 
ATOM 3836 C CB  . ALA A 1 1087 ? 201.868 201.612 209.952 1.00 56.46  ? 1098 ALA A CB  1 
ATOM 3837 N N   . ARG A 1 1088 ? 201.983 199.576 207.526 1.00 54.61  ? 1099 ARG A N   1 
ATOM 3838 C CA  . ARG A 1 1088 ? 202.520 198.370 206.914 1.00 54.19  ? 1099 ARG A CA  1 
ATOM 3839 C C   . ARG A 1 1088 ? 203.733 198.725 206.065 1.00 54.60  ? 1099 ARG A C   1 
ATOM 3840 O O   . ARG A 1 1088 ? 203.808 199.809 205.478 1.00 57.93  ? 1099 ARG A O   1 
ATOM 3841 C CB  . ARG A 1 1088 ? 201.461 197.650 206.067 1.00 55.96  ? 1099 ARG A CB  1 
ATOM 3842 C CG  . ARG A 1 1088 ? 201.290 198.201 204.659 1.00 57.18  ? 1099 ARG A CG  1 
ATOM 3843 C CD  . ARG A 1 1088 ? 200.391 197.315 203.805 1.00 62.48  ? 1099 ARG A CD  1 
ATOM 3844 N NE  . ARG A 1 1088 ? 200.917 195.963 203.654 1.00 62.35  ? 1099 ARG A NE  1 
ATOM 3845 C CZ  . ARG A 1 1088 ? 200.483 194.909 204.332 1.00 63.79  ? 1099 ARG A CZ  1 
ATOM 3846 N NH1 . ARG A 1 1088 ? 199.507 195.012 205.220 1.00 70.67  ? 1099 ARG A NH1 1 
ATOM 3847 N NH2 . ARG A 1 1088 ? 201.040 193.721 204.113 1.00 62.67  ? 1099 ARG A NH2 1 
ATOM 3848 N N   . ALA A 1 1089 ? 204.682 197.791 206.006 1.00 52.03  ? 1100 ALA A N   1 
ATOM 3849 C CA  . ALA A 1 1089 ? 205.917 197.973 205.252 1.00 50.49  ? 1100 ALA A CA  1 
ATOM 3850 C C   . ALA A 1 1089 ? 206.378 196.622 204.729 1.00 56.40  ? 1100 ALA A C   1 
ATOM 3851 O O   . ALA A 1 1089 ? 206.585 195.690 205.511 1.00 58.59  ? 1100 ALA A O   1 
ATOM 3852 C CB  . ALA A 1 1089 ? 207.006 198.613 206.119 1.00 43.56  ? 1100 ALA A CB  1 
ATOM 3853 N N   . LEU A 1 1090 ? 206.536 196.521 203.413 1.00 57.95  ? 1101 LEU A N   1 
ATOM 3854 C CA  . LEU A 1 1090 ? 207.025 195.318 202.756 1.00 53.98  ? 1101 LEU A CA  1 
ATOM 3855 C C   . LEU A 1 1090 ? 208.305 195.643 201.998 1.00 57.20  ? 1101 LEU A C   1 
ATOM 3856 O O   . LEU A 1 1090 ? 208.394 196.680 201.334 1.00 60.03  ? 1101 LEU A O   1 
ATOM 3857 C CB  . LEU A 1 1090 ? 205.982 194.751 201.788 1.00 53.51  ? 1101 LEU A CB  1 
ATOM 3858 C CG  . LEU A 1 1090 ? 204.537 194.623 202.274 1.00 53.02  ? 1101 LEU A CG  1 
ATOM 3859 C CD1 . LEU A 1 1090 ? 203.680 193.942 201.218 1.00 54.66  ? 1101 LEU A CD1 1 
ATOM 3860 C CD2 . LEU A 1 1090 ? 204.460 193.873 203.589 1.00 56.74  ? 1101 LEU A CD2 1 
ATOM 3861 N N   . LEU A 1 1091 ? 209.293 194.755 202.096 1.00 54.09  ? 1102 LEU A N   1 
ATOM 3862 C CA  . LEU A 1 1091 ? 210.577 194.945 201.435 1.00 54.53  ? 1102 LEU A CA  1 
ATOM 3863 C C   . LEU A 1 1091 ? 211.060 193.617 200.873 1.00 59.28  ? 1102 LEU A C   1 
ATOM 3864 O O   . LEU A 1 1091 ? 210.890 192.572 201.506 1.00 62.18  ? 1102 LEU A O   1 
ATOM 3865 C CB  . LEU A 1 1091 ? 211.621 195.519 202.401 1.00 52.43  ? 1102 LEU A CB  1 
ATOM 3866 C CG  . LEU A 1 1091 ? 213.012 195.799 201.829 1.00 50.34  ? 1102 LEU A CG  1 
ATOM 3867 C CD1 . LEU A 1 1091 ? 212.954 196.912 200.797 1.00 50.83  ? 1102 LEU A CD1 1 
ATOM 3868 C CD2 . LEU A 1 1091 ? 213.990 196.141 202.941 1.00 54.73  ? 1102 LEU A CD2 1 
ATOM 3869 N N   . GLU A 1 1092 ? 211.662 193.662 199.685 1.00 59.16  ? 1103 GLU A N   1 
ATOM 3870 C CA  . GLU A 1 1092 ? 212.188 192.470 199.036 1.00 53.51  ? 1103 GLU A CA  1 
ATOM 3871 C C   . GLU A 1 1092 ? 213.459 192.817 198.273 1.00 51.71  ? 1103 GLU A C   1 
ATOM 3872 O O   . GLU A 1 1092 ? 213.548 193.872 197.633 1.00 55.19  ? 1103 GLU A O   1 
ATOM 3873 C CB  . GLU A 1 1092 ? 211.156 191.844 198.091 1.00 53.91  ? 1103 GLU A CB  1 
ATOM 3874 C CG  . GLU A 1 1092 ? 211.534 190.458 197.597 1.00 59.81  ? 1103 GLU A CG  1 
ATOM 3875 C CD  . GLU A 1 1092 ? 210.453 189.826 196.745 1.00 73.74  ? 1103 GLU A CD  1 
ATOM 3876 O OE1 . GLU A 1 1092 ? 210.178 190.350 195.645 1.00 80.51  ? 1103 GLU A OE1 1 
ATOM 3877 O OE2 . GLU A 1 1092 ? 209.877 188.805 197.175 1.00 71.84  ? 1103 GLU A OE2 1 
ATOM 3878 N N   . ARG A 1 1093 ? 214.434 191.912 198.344 1.00 48.02  ? 1104 ARG A N   1 
ATOM 3879 C CA  . ARG A 1 1093 ? 215.757 192.095 197.763 1.00 46.63  ? 1104 ARG A CA  1 
ATOM 3880 C C   . ARG A 1 1093 ? 216.148 190.837 197.003 1.00 51.64  ? 1104 ARG A C   1 
ATOM 3881 O O   . ARG A 1 1093 ? 216.009 189.727 197.525 1.00 54.32  ? 1104 ARG A O   1 
ATOM 3882 C CB  . ARG A 1 1093 ? 216.790 192.393 198.855 1.00 46.03  ? 1104 ARG A CB  1 
ATOM 3883 C CG  . ARG A 1 1093 ? 218.241 192.219 198.433 1.00 50.23  ? 1104 ARG A CG  1 
ATOM 3884 C CD  . ARG A 1 1093 ? 218.733 193.370 197.575 1.00 50.59  ? 1104 ARG A CD  1 
ATOM 3885 N NE  . ARG A 1 1093 ? 220.122 193.178 197.173 1.00 48.74  ? 1104 ARG A NE  1 
ATOM 3886 C CZ  . ARG A 1 1093 ? 220.806 194.017 196.408 1.00 46.32  ? 1104 ARG A CZ  1 
ATOM 3887 N NH1 . ARG A 1 1093 ? 220.268 195.140 195.962 1.00 50.26  ? 1104 ARG A NH1 1 
ATOM 3888 N NH2 . ARG A 1 1093 ? 222.063 193.725 196.088 1.00 44.29  ? 1104 ARG A NH2 1 
ATOM 3889 N N   . ARG A 1 1094 ? 216.634 191.009 195.775 1.00 52.73  ? 1105 ARG A N   1 
ATOM 3890 C CA  . ARG A 1 1094 ? 217.145 189.895 194.981 1.00 48.04  ? 1105 ARG A CA  1 
ATOM 3891 C C   . ARG A 1 1094 ? 218.661 189.842 195.136 1.00 50.27  ? 1105 ARG A C   1 
ATOM 3892 O O   . ARG A 1 1094 ? 219.369 190.756 194.703 1.00 54.07  ? 1105 ARG A O   1 
ATOM 3893 C CB  . ARG A 1 1094 ? 216.750 190.039 193.513 1.00 48.94  ? 1105 ARG A CB  1 
ATOM 3894 C CG  . ARG A 1 1094 ? 217.366 188.974 192.616 1.00 50.74  ? 1105 ARG A CG  1 
ATOM 3895 C CD  . ARG A 1 1094 ? 216.776 188.986 191.214 1.00 42.35  ? 1105 ARG A CD  1 
ATOM 3896 N NE  . ARG A 1 1094 ? 216.779 190.316 190.619 1.00 45.19  ? 1105 ARG A NE  1 
ATOM 3897 C CZ  . ARG A 1 1094 ? 215.781 190.817 189.905 1.00 51.75  ? 1105 ARG A CZ  1 
ATOM 3898 N NH1 . ARG A 1 1094 ? 214.677 190.124 189.679 1.00 52.64  ? 1105 ARG A NH1 1 
ATOM 3899 N NH2 . ARG A 1 1094 ? 215.893 192.043 189.403 1.00 56.44  ? 1105 ARG A NH2 1 
ATOM 3900 N N   . VAL A 1 1095 ? 219.157 188.771 195.751 1.00 46.64  ? 1106 VAL A N   1 
ATOM 3901 C CA  . VAL A 1 1095 ? 220.595 188.607 195.920 1.00 48.36  ? 1106 VAL A CA  1 
ATOM 3902 C C   . VAL A 1 1095 ? 221.183 187.659 194.878 1.00 49.10  ? 1106 VAL A C   1 
ATOM 3903 O O   . VAL A 1 1095 ? 222.377 187.742 194.571 1.00 51.55  ? 1106 VAL A O   1 
ATOM 3904 C CB  . VAL A 1 1095 ? 220.913 188.126 197.346 1.00 50.79  ? 1106 VAL A CB  1 
ATOM 3905 C CG1 . VAL A 1 1095 ? 220.379 189.115 198.369 1.00 49.15  ? 1106 VAL A CG1 1 
ATOM 3906 C CG2 . VAL A 1 1095 ? 220.330 186.741 197.587 1.00 48.66  ? 1106 VAL A CG2 1 
ATOM 3907 N N   . THR A 1 1096 ? 220.370 186.762 194.326 1.00 44.43  ? 1107 THR A N   1 
ATOM 3908 C CA  . THR A 1 1096 ? 220.827 185.800 193.334 1.00 42.04  ? 1107 THR A CA  1 
ATOM 3909 C C   . THR A 1 1096 ? 219.634 185.459 192.452 1.00 45.98  ? 1107 THR A C   1 
ATOM 3910 O O   . THR A 1 1096 ? 218.480 185.579 192.874 1.00 49.64  ? 1107 THR A O   1 
ATOM 3911 C CB  . THR A 1 1096 ? 221.418 184.550 194.008 1.00 46.02  ? 1107 THR A CB  1 
ATOM 3912 O OG1 . THR A 1 1096 ? 222.545 184.930 194.806 1.00 56.21  ? 1107 THR A OG1 1 
ATOM 3913 C CG2 . THR A 1 1096 ? 221.891 183.526 192.981 1.00 43.09  ? 1107 THR A CG2 1 
ATOM 3914 N N   . SER A 1 1097 ? 219.903 185.065 191.207 1.00 44.02  ? 1108 SER A N   1 
ATOM 3915 C CA  . SER A 1 1097 ? 218.813 184.735 190.253 1.00 40.39  ? 1108 SER A CA  1 
ATOM 3916 C C   . SER A 1 1097 ? 217.811 183.777 190.901 1.00 39.58  ? 1108 SER A C   1 
ATOM 3917 O O   . SER A 1 1097 ? 216.601 183.953 190.672 1.00 45.32  ? 1108 SER A O   1 
ATOM 3918 C CB  . SER A 1 1097 ? 219.371 184.125 189.006 1.00 49.83  ? 1108 SER A CB  1 
ATOM 3919 O OG  . SER A 1 1097 ? 220.020 182.896 189.301 1.00 56.33  ? 1108 SER A OG  1 
ATOM 3920 N N   . ASN A 1 1098 ? 218.295 182.799 191.662 1.00 38.53  ? 1109 ASN A N   1 
ATOM 3921 C CA  . ASN A 1 1098 ? 217.383 181.778 192.242 1.00 40.03  ? 1109 ASN A CA  1 
ATOM 3922 C C   . ASN A 1 1098 ? 217.090 182.084 193.711 1.00 44.79  ? 1109 ASN A C   1 
ATOM 3923 O O   . ASN A 1 1098 ? 216.516 181.201 194.376 1.00 47.85  ? 1109 ASN A O   1 
ATOM 3924 C CB  . ASN A 1 1098 ? 217.985 180.382 192.160 1.00 37.50  ? 1109 ASN A CB  1 
ATOM 3925 C CG  . ASN A 1 1098 ? 218.387 180.003 190.756 1.00 44.96  ? 1109 ASN A CG  1 
ATOM 3926 O OD1 . ASN A 1 1098 ? 219.223 180.677 190.145 1.00 45.59  ? 1109 ASN A OD1 1 
ATOM 3927 N ND2 . ASN A 1 1098 ? 217.814 178.930 190.231 1.00 48.19  ? 1109 ASN A ND2 1 
ATOM 3928 N N   . TRP A 1 1099 ? 217.462 183.267 194.212 1.00 46.10  ? 1110 TRP A N   1 
ATOM 3929 C CA  . TRP A 1 1099 ? 217.297 183.511 195.671 1.00 42.47  ? 1110 TRP A CA  1 
ATOM 3930 C C   . TRP A 1 1099 ? 216.730 184.891 195.984 1.00 42.94  ? 1110 TRP A C   1 
ATOM 3931 O O   . TRP A 1 1099 ? 217.389 185.899 195.660 1.00 47.77  ? 1110 TRP A O   1 
ATOM 3932 C CB  . TRP A 1 1099 ? 218.626 183.296 196.407 1.00 42.85  ? 1110 TRP A CB  1 
ATOM 3933 C CG  . TRP A 1 1099 ? 218.995 181.844 196.537 1.00 39.96  ? 1110 TRP A CG  1 
ATOM 3934 C CD1 . TRP A 1 1099 ? 219.983 181.176 195.876 1.00 37.23  ? 1110 TRP A CD1 1 
ATOM 3935 C CD2 . TRP A 1 1099 ? 218.331 180.866 197.364 1.00 36.42  ? 1110 TRP A CD2 1 
ATOM 3936 N NE1 . TRP A 1 1099 ? 219.998 179.860 196.253 1.00 34.71  ? 1110 TRP A NE1 1 
ATOM 3937 C CE2 . TRP A 1 1099 ? 218.994 179.639 197.158 1.00 36.01  ? 1110 TRP A CE2 1 
ATOM 3938 C CE3 . TRP A 1 1099 ? 217.254 180.912 198.255 1.00 37.62  ? 1110 TRP A CE3 1 
ATOM 3939 C CZ2 . TRP A 1 1099 ? 218.611 178.472 197.813 1.00 40.05  ? 1110 TRP A CZ2 1 
ATOM 3940 C CZ3 . TRP A 1 1099 ? 216.876 179.757 198.899 1.00 40.69  ? 1110 TRP A CZ3 1 
ATOM 3941 C CH2 . TRP A 1 1099 ? 217.545 178.555 198.679 1.00 42.18  ? 1110 TRP A CH2 1 
ATOM 3942 N N   . PHE A 1 1100 ? 215.561 184.926 196.623 1.00 43.04  ? 1111 PHE A N   1 
ATOM 3943 C CA  . PHE A 1 1100 ? 214.952 186.180 197.044 1.00 46.37  ? 1111 PHE A CA  1 
ATOM 3944 C C   . PHE A 1 1100 ? 214.730 186.148 198.549 1.00 52.32  ? 1111 PHE A C   1 
ATOM 3945 O O   . PHE A 1 1100 ? 214.396 185.103 199.112 1.00 57.27  ? 1111 PHE A O   1 
ATOM 3946 C CB  . PHE A 1 1100 ? 213.617 186.430 196.331 1.00 46.95  ? 1111 PHE A CB  1 
ATOM 3947 C CG  . PHE A 1 1100 ? 213.728 186.512 194.835 1.00 47.37  ? 1111 PHE A CG  1 
ATOM 3948 C CD1 . PHE A 1 1100 ? 213.779 185.364 194.062 1.00 47.35  ? 1111 PHE A CD1 1 
ATOM 3949 C CD2 . PHE A 1 1100 ? 213.771 187.742 194.200 1.00 46.26  ? 1111 PHE A CD2 1 
ATOM 3950 C CE1 . PHE A 1 1100 ? 213.877 185.442 192.686 1.00 45.14  ? 1111 PHE A CE1 1 
ATOM 3951 C CE2 . PHE A 1 1100 ? 213.868 187.826 192.826 1.00 47.08  ? 1111 PHE A CE2 1 
ATOM 3952 C CZ  . PHE A 1 1100 ? 213.922 186.675 192.068 1.00 48.04  ? 1111 PHE A CZ  1 
ATOM 3953 N N   . VAL A 1 1101 ? 214.915 187.294 199.199 1.00 50.74  ? 1112 VAL A N   1 
ATOM 3954 C CA  . VAL A 1 1101 ? 214.680 187.434 200.631 1.00 47.67  ? 1112 VAL A CA  1 
ATOM 3955 C C   . VAL A 1 1101 ? 213.777 188.637 200.857 1.00 52.63  ? 1112 VAL A C   1 
ATOM 3956 O O   . VAL A 1 1101 ? 213.780 189.583 200.062 1.00 56.39  ? 1112 VAL A O   1 
ATOM 3957 C CB  . VAL A 1 1101 ? 215.998 187.588 201.421 1.00 49.21  ? 1112 VAL A CB  1 
ATOM 3958 C CG1 . VAL A 1 1101 ? 216.821 186.312 201.337 1.00 51.62  ? 1112 VAL A CG1 1 
ATOM 3959 C CG2 . VAL A 1 1101 ? 216.794 188.776 200.903 1.00 47.51  ? 1112 VAL A CG2 1 
ATOM 3960 N N   . GLY A 1 1102 ? 213.000 188.599 201.937 1.00 55.23  ? 1113 GLY A N   1 
ATOM 3961 C CA  . GLY A 1 1102 ? 212.118 189.717 202.221 1.00 58.96  ? 1113 GLY A CA  1 
ATOM 3962 C C   . GLY A 1 1102 ? 211.650 189.728 203.658 1.00 60.61  ? 1113 GLY A C   1 
ATOM 3963 O O   . GLY A 1 1102 ? 211.703 188.721 204.367 1.00 63.78  ? 1113 GLY A O   1 
ATOM 3964 N N   . THR A 1 1103 ? 211.182 190.903 204.077 1.00 57.79  ? 1114 THR A N   1 
ATOM 3965 C CA  . THR A 1 1103 ? 210.659 191.114 205.419 1.00 56.75  ? 1114 THR A CA  1 
ATOM 3966 C C   . THR A 1 1103 ? 209.342 191.867 205.312 1.00 58.37  ? 1114 THR A C   1 
ATOM 3967 O O   . THR A 1 1103 ? 209.124 192.628 204.366 1.00 61.49  ? 1114 THR A O   1 
ATOM 3968 C CB  . THR A 1 1103 ? 211.636 191.907 206.300 1.00 63.26  ? 1114 THR A CB  1 
ATOM 3969 O OG1 . THR A 1 1103 ? 211.701 193.263 205.841 1.00 67.48  ? 1114 THR A OG1 1 
ATOM 3970 C CG2 . THR A 1 1103 ? 213.031 191.298 206.254 1.00 63.12  ? 1114 THR A CG2 1 
ATOM 3971 N N   . ALA A 1 1104 ? 208.463 191.652 206.290 1.00 56.07  ? 1115 ALA A N   1 
ATOM 3972 C CA  . ALA A 1 1104 ? 207.170 192.325 206.319 1.00 55.37  ? 1115 ALA A CA  1 
ATOM 3973 C C   . ALA A 1 1104 ? 206.785 192.669 207.750 1.00 57.85  ? 1115 ALA A C   1 
ATOM 3974 O O   . ALA A 1 1104 ? 206.942 191.845 208.657 1.00 61.86  ? 1115 ALA A O   1 
ATOM 3975 C CB  . ALA A 1 1104 ? 206.080 191.467 205.672 1.00 48.83  ? 1115 ALA A CB  1 
ATOM 3976 N N   . ILE A 1 1105 ? 206.275 193.886 207.938 1.00 53.20  ? 1116 ILE A N   1 
ATOM 3977 C CA  . ILE A 1 1105 ? 205.811 194.384 209.228 1.00 48.32  ? 1116 ILE A CA  1 
ATOM 3978 C C   . ILE A 1 1105 ? 204.360 194.818 209.070 1.00 57.15  ? 1116 ILE A C   1 
ATOM 3979 O O   . ILE A 1 1105 ? 204.025 195.539 208.123 1.00 59.23  ? 1116 ILE A O   1 
ATOM 3980 C CB  . ILE A 1 1105 ? 206.680 195.554 209.722 1.00 46.25  ? 1116 ILE A CB  1 
ATOM 3981 C CG1 . ILE A 1 1105 ? 208.059 195.057 210.155 1.00 53.29  ? 1116 ILE A CG1 1 
ATOM 3982 C CG2 . ILE A 1 1105 ? 205.997 196.289 210.866 1.00 46.71  ? 1116 ILE A CG2 1 
ATOM 3983 C CD1 . ILE A 1 1105 ? 209.027 196.168 210.497 1.00 53.88  ? 1116 ILE A CD1 1 
ATOM 3984 N N   . ASP A 1 1106 ? 203.500 194.384 209.992 1.00 62.42  ? 1117 ASP A N   1 
ATOM 3985 C CA  . ASP A 1 1106 ? 202.088 194.756 209.976 1.00 62.00  ? 1117 ASP A CA  1 
ATOM 3986 C C   . ASP A 1 1106 ? 201.693 195.151 211.392 1.00 65.03  ? 1117 ASP A C   1 
ATOM 3987 O O   . ASP A 1 1106 ? 201.693 194.308 212.295 1.00 69.29  ? 1117 ASP A O   1 
ATOM 3988 C CB  . ASP A 1 1106 ? 201.217 193.609 209.464 1.00 66.15  ? 1117 ASP A CB  1 
ATOM 3989 C CG  . ASP A 1 1106 ? 199.739 193.953 209.459 1.00 79.11  ? 1117 ASP A CG  1 
ATOM 3990 O OD1 . ASP A 1 1106 ? 199.403 195.156 209.471 1.00 78.66  ? 1117 ASP A OD1 1 
ATOM 3991 O OD2 . ASP A 1 1106 ? 198.912 193.017 209.447 1.00 87.89  ? 1117 ASP A OD2 1 
ATOM 3992 N N   . ILE A 1 1107 ? 201.357 196.424 211.582 1.00 62.24  ? 1118 ILE A N   1 
ATOM 3993 C CA  . ILE A 1 1107 ? 200.968 196.965 212.880 1.00 58.96  ? 1118 ILE A CA  1 
ATOM 3994 C C   . ILE A 1 1107 ? 199.485 197.303 212.823 1.00 64.49  ? 1118 ILE A C   1 
ATOM 3995 O O   . ILE A 1 1107 ? 199.039 198.017 211.916 1.00 67.77  ? 1118 ILE A O   1 
ATOM 3996 C CB  . ILE A 1 1107 ? 201.803 198.200 213.252 1.00 51.90  ? 1118 ILE A CB  1 
ATOM 3997 C CG1 . ILE A 1 1107 ? 203.274 197.818 213.420 1.00 54.53  ? 1118 ILE A CG1 1 
ATOM 3998 C CG2 . ILE A 1 1107 ? 201.269 198.843 214.522 1.00 58.50  ? 1118 ILE A CG2 1 
ATOM 3999 C CD1 . ILE A 1 1107 ? 204.222 198.993 213.329 1.00 58.64  ? 1118 ILE A CD1 1 
ATOM 4000 N N   . GLN A 1 1108 ? 198.723 196.794 213.787 1.00 64.70  ? 1119 GLN A N   1 
ATOM 4001 C CA  . GLN A 1 1108 ? 197.284 197.014 213.856 1.00 61.98  ? 1119 GLN A CA  1 
ATOM 4002 C C   . GLN A 1 1108 ? 196.954 197.770 215.137 1.00 62.18  ? 1119 GLN A C   1 
ATOM 4003 O O   . GLN A 1 1108 ? 197.180 197.259 216.239 1.00 64.36  ? 1119 GLN A O   1 
ATOM 4004 C CB  . GLN A 1 1108 ? 196.526 195.688 213.805 1.00 64.36  ? 1119 GLN A CB  1 
ATOM 4005 C CG  . GLN A 1 1108 ? 197.020 194.731 212.733 1.00 65.43  ? 1119 GLN A CG  1 
ATOM 4006 C CD  . GLN A 1 1108 ? 196.210 194.818 211.456 1.00 74.89  ? 1119 GLN A CD  1 
ATOM 4007 O OE1 . GLN A 1 1108 ? 195.384 195.716 211.291 1.00 75.00  ? 1119 GLN A OE1 1 
ATOM 4008 N NE2 . GLN A 1 1108 ? 196.441 193.881 210.544 1.00 80.11  ? 1119 GLN A NE2 1 
ATOM 4009 N N   . GLN A 1 1109 ? 196.418 198.985 214.988 1.00 61.03  ? 1120 GLN A N   1 
ATOM 4010 C CA  . GLN A 1 1109 ? 195.987 199.791 216.124 1.00 60.43  ? 1120 GLN A CA  1 
ATOM 4011 C C   . GLN A 1 1109 ? 194.660 200.485 215.836 1.00 61.28  ? 1120 GLN A C   1 
ATOM 4012 O O   . GLN A 1 1109 ? 194.381 201.553 216.392 1.00 60.07  ? 1120 GLN A O   1 
ATOM 4013 C CB  . GLN A 1 1109 ? 197.046 200.834 216.500 1.00 58.92  ? 1120 GLN A CB  1 
ATOM 4014 C CG  . GLN A 1 1109 ? 198.382 200.260 216.953 1.00 62.86  ? 1120 GLN A CG  1 
ATOM 4015 C CD  . GLN A 1 1109 ? 198.318 199.614 218.325 1.00 70.00  ? 1120 GLN A CD  1 
ATOM 4016 O OE1 . GLN A 1 1109 ? 197.284 199.638 218.992 1.00 75.15  ? 1120 GLN A OE1 1 
ATOM 4017 N NE2 . GLN A 1 1109 ? 199.432 199.033 218.754 1.00 69.08  ? 1120 GLN A NE2 1 
ATOM 4018 N N   . ALA A 1 1110 ? 193.834 199.895 214.977 1.00 60.65  ? 1121 ALA A N   1 
ATOM 4019 C CA  . ALA A 1 1110 ? 192.571 200.492 214.564 1.00 58.51  ? 1121 ALA A CA  1 
ATOM 4020 C C   . ALA A 1 1110 ? 191.406 200.109 215.467 1.00 68.48  ? 1121 ALA A C   1 
ATOM 4021 O O   . ALA A 1 1110 ? 190.254 200.174 215.026 1.00 68.02  ? 1121 ALA A O   1 
ATOM 4022 C CB  . ALA A 1 1110 ? 192.253 200.102 213.118 1.00 53.01  ? 1121 ALA A CB  1 
ATOM 4023 N N   . LYS A 1 1111 ? 191.681 199.716 216.713 1.00 73.99  ? 1122 LYS A N   1 
ATOM 4024 C CA  . LYS A 1 1111 ? 190.645 199.315 217.668 1.00 74.05  ? 1122 LYS A CA  1 
ATOM 4025 C C   . LYS A 1 1111 ? 189.787 198.180 217.114 1.00 73.10  ? 1122 LYS A C   1 
ATOM 4026 O O   . LYS A 1 1111 ? 188.571 198.139 217.313 1.00 69.46  ? 1122 LYS A O   1 
ATOM 4027 C CB  . LYS A 1 1111 ? 189.775 200.507 218.075 1.00 68.08  ? 1122 LYS A CB  1 
ATOM 4028 C CG  . LYS A 1 1111 ? 190.516 201.580 218.853 1.00 63.79  ? 1122 LYS A CG  1 
ATOM 4029 C CD  . LYS A 1 1111 ? 189.587 202.715 219.248 1.00 58.13  ? 1122 LYS A CD  1 
ATOM 4030 C CE  . LYS A 1 1111 ? 190.206 203.582 220.332 1.00 66.16  ? 1122 LYS A CE  1 
ATOM 4031 N NZ  . LYS A 1 1111 ? 191.438 204.270 219.855 1.00 58.37  ? 1122 LYS A NZ  1 
ATOM 4032 N N   . ASP A 1 1112 ? 190.428 197.247 216.408 1.00 73.37  ? 1123 ASP A N   1 
ATOM 4033 C CA  . ASP A 1 1112 ? 189.741 196.102 215.835 1.00 66.99  ? 1123 ASP A CA  1 
ATOM 4034 C C   . ASP A 1 1112 ? 190.200 194.794 216.468 1.00 73.21  ? 1123 ASP A C   1 
ATOM 4035 O O   . ASP A 1 1112 ? 189.736 193.725 216.058 1.00 70.86  ? 1123 ASP A O   1 
ATOM 4036 C CB  . ASP A 1 1112 ? 189.966 196.058 214.313 1.00 66.83  ? 1123 ASP A CB  1 
ATOM 4037 C CG  . ASP A 1 1112 ? 188.887 195.279 213.571 1.00 73.78  ? 1123 ASP A CG  1 
ATOM 4038 O OD1 . ASP A 1 1112 ? 188.779 195.461 212.339 1.00 76.79  ? 1123 ASP A OD1 1 
ATOM 4039 O OD2 . ASP A 1 1112 ? 188.121 194.527 214.204 1.00 72.33  ? 1123 ASP A OD2 1 
ATOM 4040 N N   . TYR A 1 1113 ? 191.104 194.851 217.448 1.00 75.16  ? 1124 TYR A N   1 
ATOM 4041 C CA  . TYR A 1 1113 ? 191.626 193.682 218.155 1.00 70.91  ? 1124 TYR A CA  1 
ATOM 4042 C C   . TYR A 1 1113 ? 192.338 192.707 217.222 1.00 77.76  ? 1124 TYR A C   1 
ATOM 4043 O O   . TYR A 1 1113 ? 192.415 191.509 217.512 1.00 83.12  ? 1124 TYR A O   1 
ATOM 4044 C CB  . TYR A 1 1113 ? 190.520 192.959 218.935 1.00 64.07  ? 1124 TYR A CB  1 
ATOM 4045 C CG  . TYR A 1 1113 ? 189.799 193.832 219.940 1.00 64.09  ? 1124 TYR A CG  1 
ATOM 4046 C CD1 . TYR A 1 1113 ? 190.405 194.964 220.472 1.00 65.35  ? 1124 TYR A CD1 1 
ATOM 4047 C CD2 . TYR A 1 1113 ? 188.509 193.527 220.354 1.00 60.56  ? 1124 TYR A CD2 1 
ATOM 4048 C CE1 . TYR A 1 1113 ? 189.749 195.764 221.387 1.00 63.60  ? 1124 TYR A CE1 1 
ATOM 4049 C CE2 . TYR A 1 1113 ? 187.845 194.322 221.269 1.00 63.42  ? 1124 TYR A CE2 1 
ATOM 4050 C CZ  . TYR A 1 1113 ? 188.469 195.438 221.782 1.00 65.77  ? 1124 TYR A CZ  1 
ATOM 4051 O OH  . TYR A 1 1113 ? 187.812 196.233 222.693 1.00 73.77  ? 1124 TYR A OH  1 
ATOM 4052 N N   . ALA A 1 1114 ? 192.860 193.198 216.101 1.00 73.52  ? 1125 ALA A N   1 
ATOM 4053 C CA  . ALA A 1 1114 ? 193.614 192.347 215.198 1.00 70.61  ? 1125 ALA A CA  1 
ATOM 4054 C C   . ALA A 1 1114 ? 195.066 192.236 215.663 1.00 77.19  ? 1125 ALA A C   1 
ATOM 4055 O O   . ALA A 1 1114 ? 195.656 193.216 216.124 1.00 83.80  ? 1125 ALA A O   1 
ATOM 4056 C CB  . ALA A 1 1114 ? 193.564 192.896 213.776 1.00 72.20  ? 1125 ALA A CB  1 
ATOM 4057 N N   . PRO A 1 1115 ? 195.663 191.052 215.553 1.00 73.02  ? 1126 PRO A N   1 
ATOM 4058 C CA  . PRO A 1 1115 ? 197.053 190.889 215.989 1.00 69.57  ? 1126 PRO A CA  1 
ATOM 4059 C C   . PRO A 1 1115 ? 198.032 191.536 215.023 1.00 66.65  ? 1126 PRO A C   1 
ATOM 4060 O O   . PRO A 1 1115 ? 197.765 191.679 213.827 1.00 66.94  ? 1126 PRO A O   1 
ATOM 4061 C CB  . PRO A 1 1115 ? 197.231 189.368 216.024 1.00 68.00  ? 1126 PRO A CB  1 
ATOM 4062 C CG  . PRO A 1 1115 ? 196.288 188.873 214.980 1.00 68.70  ? 1126 PRO A CG  1 
ATOM 4063 C CD  . PRO A 1 1115 ? 195.096 189.796 215.031 1.00 69.78  ? 1126 PRO A CD  1 
ATOM 4064 N N   . SER A 1 1116 ? 199.181 191.930 215.562 1.00 64.12  ? 1127 SER A N   1 
ATOM 4065 C CA  . SER A 1 1116 ? 200.271 192.474 214.768 1.00 63.73  ? 1127 SER A CA  1 
ATOM 4066 C C   . SER A 1 1116 ? 201.222 191.357 214.350 1.00 66.21  ? 1127 SER A C   1 
ATOM 4067 O O   . SER A 1 1116 ? 201.394 190.361 215.058 1.00 68.05  ? 1127 SER A O   1 
ATOM 4068 C CB  . SER A 1 1116 ? 201.028 193.547 215.551 1.00 66.94  ? 1127 SER A CB  1 
ATOM 4069 O OG  . SER A 1 1116 ? 200.177 194.633 215.876 1.00 70.28  ? 1127 SER A OG  1 
ATOM 4070 N N   . HIS A 1 1117 ? 201.853 191.546 213.188 1.00 67.40  ? 1128 HIS A N   1 
ATOM 4071 C CA  . HIS A 1 1117 ? 202.637 190.507 212.530 1.00 60.97  ? 1128 HIS A CA  1 
ATOM 4072 C C   . HIS A 1 1117 ? 204.011 191.031 212.135 1.00 58.22  ? 1128 HIS A C   1 
ATOM 4073 O O   . HIS A 1 1117 ? 204.161 192.203 211.778 1.00 61.68  ? 1128 HIS A O   1 
ATOM 4074 C CB  . HIS A 1 1117 ? 201.922 189.988 211.273 1.00 56.91  ? 1128 HIS A CB  1 
ATOM 4075 C CG  . HIS A 1 1117 ? 200.731 189.128 211.558 1.00 60.91  ? 1128 HIS A CG  1 
ATOM 4076 N ND1 . HIS A 1 1117 ? 200.741 187.761 211.384 1.00 62.72  ? 1128 HIS A ND1 1 
ATOM 4077 C CD2 . HIS A 1 1117 ? 199.489 189.442 211.999 1.00 63.08  ? 1128 HIS A CD2 1 
ATOM 4078 C CE1 . HIS A 1 1117 ? 199.558 187.269 211.706 1.00 63.19  ? 1128 HIS A CE1 1 
ATOM 4079 N NE2 . HIS A 1 1117 ? 198.781 188.268 212.084 1.00 61.08  ? 1128 HIS A NE2 1 
ATOM 4080 N N   . PHE A 1 1118 ? 205.010 190.149 212.183 1.00 55.28  ? 1129 PHE A N   1 
ATOM 4081 C CA  . PHE A 1 1118 ? 206.345 190.436 211.674 1.00 55.26  ? 1129 PHE A CA  1 
ATOM 4082 C C   . PHE A 1 1118 ? 206.922 189.155 211.091 1.00 56.85  ? 1129 PHE A C   1 
ATOM 4083 O O   . PHE A 1 1118 ? 207.059 188.157 211.804 1.00 57.41  ? 1129 PHE A O   1 
ATOM 4084 C CB  . PHE A 1 1118 ? 207.254 190.982 212.781 1.00 54.55  ? 1129 PHE A CB  1 
ATOM 4085 C CG  . PHE A 1 1118 ? 208.677 191.206 212.349 1.00 59.07  ? 1129 PHE A CG  1 
ATOM 4086 C CD1 . PHE A 1 1118 ? 208.964 191.905 211.189 1.00 58.25  ? 1129 PHE A CD1 1 
ATOM 4087 C CD2 . PHE A 1 1118 ? 209.728 190.719 213.108 1.00 62.45  ? 1129 PHE A CD2 1 
ATOM 4088 C CE1 . PHE A 1 1118 ? 210.273 192.114 210.794 1.00 56.14  ? 1129 PHE A CE1 1 
ATOM 4089 C CE2 . PHE A 1 1118 ? 211.038 190.924 212.718 1.00 62.42  ? 1129 PHE A CE2 1 
ATOM 4090 C CZ  . PHE A 1 1118 ? 211.310 191.623 211.560 1.00 54.66  ? 1129 PHE A CZ  1 
ATOM 4091 N N   . LEU A 1 1119 ? 207.265 189.178 209.805 1.00 56.52  ? 1130 LEU A N   1 
ATOM 4092 C CA  . LEU A 1 1119 ? 207.677 187.956 209.128 1.00 51.66  ? 1130 LEU A CA  1 
ATOM 4093 C C   . LEU A 1 1119 ? 208.940 188.180 208.314 1.00 55.03  ? 1130 LEU A C   1 
ATOM 4094 O O   . LEU A 1 1119 ? 209.194 189.276 207.808 1.00 60.56  ? 1130 LEU A O   1 
ATOM 4095 C CB  . LEU A 1 1119 ? 206.575 187.408 208.207 1.00 46.73  ? 1130 LEU A CB  1 
ATOM 4096 C CG  . LEU A 1 1119 ? 206.095 188.271 207.041 1.00 52.09  ? 1130 LEU A CG  1 
ATOM 4097 C CD1 . LEU A 1 1119 ? 206.807 187.901 205.745 1.00 57.02  ? 1130 LEU A CD1 1 
ATOM 4098 C CD2 . LEU A 1 1119 ? 204.588 188.161 206.875 1.00 58.50  ? 1130 LEU A CD2 1 
ATOM 4099 N N   . LEU A 1 1120 ? 209.719 187.107 208.190 1.00 52.21  ? 1131 LEU A N   1 
ATOM 4100 C CA  . LEU A 1 1120 ? 210.870 187.044 207.298 1.00 50.77  ? 1131 LEU A CA  1 
ATOM 4101 C C   . LEU A 1 1120 ? 210.710 185.835 206.389 1.00 52.64  ? 1131 LEU A C   1 
ATOM 4102 O O   . LEU A 1 1120 ? 210.432 184.731 206.864 1.00 57.04  ? 1131 LEU A O   1 
ATOM 4103 C CB  . LEU A 1 1120 ? 212.188 186.937 208.076 1.00 52.86  ? 1131 LEU A CB  1 
ATOM 4104 C CG  . LEU A 1 1120 ? 212.303 187.711 209.391 1.00 59.17  ? 1131 LEU A CG  1 
ATOM 4105 C CD1 . LEU A 1 1120 ? 213.566 187.310 210.143 1.00 61.34  ? 1131 LEU A CD1 1 
ATOM 4106 C CD2 . LEU A 1 1120 ? 212.277 189.207 209.139 1.00 55.13  ? 1131 LEU A CD2 1 
ATOM 4107 N N   . TYR A 1 1121 ? 210.893 186.034 205.084 1.00 50.44  ? 1132 TYR A N   1 
ATOM 4108 C CA  . TYR A 1 1121 ? 210.658 184.961 204.129 1.00 49.42  ? 1132 TYR A CA  1 
ATOM 4109 C C   . TYR A 1 1121 ? 211.803 184.865 203.132 1.00 52.78  ? 1132 TYR A C   1 
ATOM 4110 O O   . TYR A 1 1121 ? 212.465 185.859 202.815 1.00 53.54  ? 1132 TYR A O   1 
ATOM 4111 C CB  . TYR A 1 1121 ? 209.326 185.146 203.384 1.00 50.46  ? 1132 TYR A CB  1 
ATOM 4112 C CG  . TYR A 1 1121 ? 209.283 186.296 202.403 1.00 51.85  ? 1132 TYR A CG  1 
ATOM 4113 C CD1 . TYR A 1 1121 ? 208.895 187.565 202.810 1.00 52.47  ? 1132 TYR A CD1 1 
ATOM 4114 C CD2 . TYR A 1 1121 ? 209.602 186.107 201.065 1.00 54.72  ? 1132 TYR A CD2 1 
ATOM 4115 C CE1 . TYR A 1 1121 ? 208.841 188.617 201.917 1.00 53.78  ? 1132 TYR A CE1 1 
ATOM 4116 C CE2 . TYR A 1 1121 ? 209.554 187.154 200.165 1.00 60.59  ? 1132 TYR A CE2 1 
ATOM 4117 C CZ  . TYR A 1 1121 ? 209.173 188.406 200.596 1.00 58.28  ? 1132 TYR A CZ  1 
ATOM 4118 O OH  . TYR A 1 1121 ? 209.123 189.450 199.702 1.00 58.82  ? 1132 TYR A OH  1 
ATOM 4119 N N   . VAL A 1 1122 ? 212.021 183.644 202.644 1.00 52.44  ? 1133 VAL A N   1 
ATOM 4120 C CA  . VAL A 1 1122 ? 213.016 183.343 201.624 1.00 47.94  ? 1133 VAL A CA  1 
ATOM 4121 C C   . VAL A 1 1122 ? 212.345 182.508 200.540 1.00 52.25  ? 1133 VAL A C   1 
ATOM 4122 O O   . VAL A 1 1122 ? 211.522 181.632 200.833 1.00 54.14  ? 1133 VAL A O   1 
ATOM 4123 C CB  . VAL A 1 1122 ? 214.244 182.616 202.218 1.00 42.91  ? 1133 VAL A CB  1 
ATOM 4124 C CG1 . VAL A 1 1122 ? 213.839 181.297 202.859 1.00 44.43  ? 1133 VAL A CG1 1 
ATOM 4125 C CG2 . VAL A 1 1122 ? 215.307 182.397 201.152 1.00 44.78  ? 1133 VAL A CG2 1 
ATOM 4126 N N   . ARG A 1 1123 ? 212.670 182.806 199.284 1.00 51.34  ? 1134 ARG A N   1 
ATOM 4127 C CA  . ARG A 1 1123 ? 212.037 182.177 198.133 1.00 45.70  ? 1134 ARG A CA  1 
ATOM 4128 C C   . ARG A 1 1123 ? 213.106 181.710 197.156 1.00 44.52  ? 1134 ARG A C   1 
ATOM 4129 O O   . ARG A 1 1123 ? 214.044 182.454 196.852 1.00 48.16  ? 1134 ARG A O   1 
ATOM 4130 C CB  . ARG A 1 1123 ? 211.068 183.148 197.450 1.00 44.24  ? 1134 ARG A CB  1 
ATOM 4131 C CG  . ARG A 1 1123 ? 210.459 182.636 196.158 1.00 45.89  ? 1134 ARG A CG  1 
ATOM 4132 C CD  . ARG A 1 1123 ? 209.147 183.345 195.864 1.00 50.59  ? 1134 ARG A CD  1 
ATOM 4133 N NE  . ARG A 1 1123 ? 209.299 184.795 195.869 1.00 58.80  ? 1134 ARG A NE  1 
ATOM 4134 C CZ  . ARG A 1 1123 ? 209.598 185.523 194.802 1.00 60.18  ? 1134 ARG A CZ  1 
ATOM 4135 N NH1 . ARG A 1 1123 ? 209.785 184.968 193.616 1.00 56.91  ? 1134 ARG A NH1 1 
ATOM 4136 N NH2 . ARG A 1 1123 ? 209.710 186.843 194.928 1.00 60.67  ? 1134 ARG A NH2 1 
ATOM 4137 N N   . TYR A 1 1124 ? 212.961 180.480 196.671 1.00 40.58  ? 1135 TYR A N   1 
ATOM 4138 C CA  . TYR A 1 1124 ? 213.891 179.869 195.732 1.00 37.07  ? 1135 TYR A CA  1 
ATOM 4139 C C   . TYR A 1 1124 ? 213.147 179.546 194.444 1.00 40.95  ? 1135 TYR A C   1 
ATOM 4140 O O   . TYR A 1 1124 ? 212.126 178.847 194.470 1.00 46.84  ? 1135 TYR A O   1 
ATOM 4141 C CB  . TYR A 1 1124 ? 214.514 178.608 196.329 1.00 38.02  ? 1135 TYR A CB  1 
ATOM 4142 C CG  . TYR A 1 1124 ? 215.125 177.669 195.313 1.00 39.44  ? 1135 TYR A CG  1 
ATOM 4143 C CD1 . TYR A 1 1124 ? 216.381 177.916 194.777 1.00 42.91  ? 1135 TYR A CD1 1 
ATOM 4144 C CD2 . TYR A 1 1124 ? 214.450 176.527 194.900 1.00 42.86  ? 1135 TYR A CD2 1 
ATOM 4145 C CE1 . TYR A 1 1124 ? 216.945 177.058 193.851 1.00 40.16  ? 1135 TYR A CE1 1 
ATOM 4146 C CE2 . TYR A 1 1124 ? 215.005 175.664 193.975 1.00 45.90  ? 1135 TYR A CE2 1 
ATOM 4147 C CZ  . TYR A 1 1124 ? 216.252 175.934 193.455 1.00 43.56  ? 1135 TYR A CZ  1 
ATOM 4148 O OH  . TYR A 1 1124 ? 216.809 175.077 192.535 1.00 47.15  ? 1135 TYR A OH  1 
ATOM 4149 N N   . SER A 1 1125 ? 213.676 180.074 193.327 1.00 42.41  ? 1136 SER A N   1 
ATOM 4150 C CA  . SER A 1 1125 ? 213.086 179.840 191.981 1.00 46.14  ? 1136 SER A CA  1 
ATOM 4151 C C   . SER A 1 1125 ? 214.029 178.935 191.183 1.00 45.26  ? 1136 SER A C   1 
ATOM 4152 O O   . SER A 1 1125 ? 215.182 179.345 190.966 1.00 48.16  ? 1136 SER A O   1 
ATOM 4153 C CB  . SER A 1 1125 ? 212.868 181.139 191.265 1.00 45.63  ? 1136 SER A CB  1 
ATOM 4154 O OG  . SER A 1 1125 ? 212.173 182.062 192.092 1.00 52.18  ? 1136 SER A OG  1 
ATOM 4155 N N   . ALA A 1 1126 ? 213.558 177.774 190.734 1.00 41.18  ? 1137 ALA A N   1 
ATOM 4156 C CA  . ALA A 1 1126 ? 214.418 176.798 190.073 1.00 40.56  ? 1137 ALA A CA  1 
ATOM 4157 C C   . ALA A 1 1126 ? 215.013 177.362 188.787 1.00 44.00  ? 1137 ALA A C   1 
ATOM 4158 O O   . ALA A 1 1126 ? 216.215 177.220 188.534 1.00 46.82  ? 1137 ALA A O   1 
ATOM 4159 C CB  . ALA A 1 1126 ? 213.634 175.517 189.789 1.00 43.56  ? 1137 ALA A CB  1 
ATOM 4160 N N   . ALA A 1 1127 ? 214.187 178.007 187.962 1.00 47.28  ? 1138 ALA A N   1 
ATOM 4161 C CA  . ALA A 1 1127 ? 214.658 178.526 186.685 1.00 47.09  ? 1138 ALA A CA  1 
ATOM 4162 C C   . ALA A 1 1127 ? 215.326 179.890 186.806 1.00 46.20  ? 1138 ALA A C   1 
ATOM 4163 O O   . ALA A 1 1127 ? 216.162 180.229 185.962 1.00 46.32  ? 1138 ALA A O   1 
ATOM 4164 C CB  . ALA A 1 1127 ? 213.499 178.609 185.690 1.00 45.63  ? 1138 ALA A CB  1 
ATOM 4165 N N   . GLY A 1 1128 ? 214.984 180.674 187.825 1.00 46.31  ? 1139 GLY A N   1 
ATOM 4166 C CA  . GLY A 1 1128 ? 215.564 181.993 187.983 1.00 42.56  ? 1139 GLY A CA  1 
ATOM 4167 C C   . GLY A 1 1128 ? 214.721 183.086 187.362 1.00 43.53  ? 1139 GLY A C   1 
ATOM 4168 O O   . GLY A 1 1128 ? 214.136 182.892 186.292 1.00 47.21  ? 1139 GLY A O   1 
ATOM 4169 N N   . TRP A 1 1129 ? 214.647 184.242 188.023 1.00 40.92  ? 1140 TRP A N   1 
ATOM 4170 C CA  . TRP A 1 1129 ? 213.819 185.363 187.576 1.00 43.73  ? 1140 TRP A CA  1 
ATOM 4171 C C   . TRP A 1 1129 ? 214.676 186.627 187.632 1.00 46.16  ? 1140 TRP A C   1 
ATOM 4172 O O   . TRP A 1 1129 ? 214.806 187.252 188.688 1.00 54.69  ? 1140 TRP A O   1 
ATOM 4173 C CB  . TRP A 1 1129 ? 212.567 185.491 188.441 1.00 46.25  ? 1140 TRP A CB  1 
ATOM 4174 C CG  . TRP A 1 1129 ? 211.692 186.654 188.082 1.00 50.36  ? 1140 TRP A CG  1 
ATOM 4175 C CD1 . TRP A 1 1129 ? 211.314 187.677 188.900 1.00 55.97  ? 1140 TRP A CD1 1 
ATOM 4176 C CD2 . TRP A 1 1129 ? 211.030 186.876 186.829 1.00 50.93  ? 1140 TRP A CD2 1 
ATOM 4177 N NE1 . TRP A 1 1129 ? 210.488 188.542 188.224 1.00 61.28  ? 1140 TRP A NE1 1 
ATOM 4178 C CE2 . TRP A 1 1129 ? 210.295 188.071 186.952 1.00 58.97  ? 1140 TRP A CE2 1 
ATOM 4179 C CE3 . TRP A 1 1129 ? 210.993 186.185 185.614 1.00 49.39  ? 1140 TRP A CE3 1 
ATOM 4180 C CZ2 . TRP A 1 1129 ? 209.538 188.593 185.905 1.00 58.57  ? 1140 TRP A CZ2 1 
ATOM 4181 C CZ3 . TRP A 1 1129 ? 210.244 186.709 184.574 1.00 52.55  ? 1140 TRP A CZ3 1 
ATOM 4182 C CH2 . TRP A 1 1129 ? 209.527 187.900 184.727 1.00 56.77  ? 1140 TRP A CH2 1 
ATOM 4183 N N   . GLN A 1 1130 ? 215.259 187.000 186.493 1.00 41.94  ? 1141 GLN A N   1 
ATOM 4184 C CA  . GLN A 1 1130 ? 216.087 188.195 186.383 1.00 46.32  ? 1141 GLN A CA  1 
ATOM 4185 C C   . GLN A 1 1130 ? 215.316 189.409 185.878 1.00 54.41  ? 1141 GLN A C   1 
ATOM 4186 O O   . GLN A 1 1130 ? 215.922 190.460 185.646 1.00 57.38  ? 1141 GLN A O   1 
ATOM 4187 C CB  . GLN A 1 1130 ? 217.281 187.928 185.461 1.00 44.97  ? 1141 GLN A CB  1 
ATOM 4188 C CG  . GLN A 1 1130 ? 218.145 186.738 185.856 1.00 49.62  ? 1141 GLN A CG  1 
ATOM 4189 C CD  . GLN A 1 1130 ? 219.116 187.049 186.984 1.00 53.79  ? 1141 GLN A CD  1 
ATOM 4190 O OE1 . GLN A 1 1130 ? 218.764 187.702 187.967 1.00 52.73  ? 1141 GLN A OE1 1 
ATOM 4191 N NE2 . GLN A 1 1130 ? 220.351 186.581 186.842 1.00 51.89  ? 1141 GLN A NE2 1 
ATOM 4192 N N   . GLY A 1 1131 ? 214.007 189.286 185.693 1.00 53.54  ? 1142 GLY A N   1 
ATOM 4193 C CA  . GLY A 1 1131 ? 213.189 190.383 185.221 1.00 52.43  ? 1142 GLY A CA  1 
ATOM 4194 C C   . GLY A 1 1131 ? 212.668 191.229 186.363 1.00 61.57  ? 1142 GLY A C   1 
ATOM 4195 O O   . GLY A 1 1131 ? 213.197 191.220 187.478 1.00 62.24  ? 1142 GLY A O   1 
ATOM 4196 N N   . ASP A 1 1132 ? 211.607 191.976 186.072 1.00 66.82  ? 1143 ASP A N   1 
ATOM 4197 C CA  . ASP A 1 1132 ? 211.011 192.850 187.073 1.00 68.77  ? 1143 ASP A CA  1 
ATOM 4198 C C   . ASP A 1 1132 ? 210.373 192.031 188.189 1.00 69.21  ? 1143 ASP A C   1 
ATOM 4199 O O   . ASP A 1 1132 ? 209.687 191.036 187.940 1.00 67.94  ? 1143 ASP A O   1 
ATOM 4200 C CB  . ASP A 1 1132 ? 209.968 193.760 186.428 1.00 68.48  ? 1143 ASP A CB  1 
ATOM 4201 C CG  . ASP A 1 1132 ? 210.588 194.809 185.526 1.00 72.02  ? 1143 ASP A CG  1 
ATOM 4202 O OD1 . ASP A 1 1132 ? 211.686 195.306 185.851 1.00 72.84  ? 1143 ASP A OD1 1 
ATOM 4203 O OD2 . ASP A 1 1132 ? 209.970 195.142 184.493 1.00 73.72  ? 1143 ASP A OD2 1 
ATOM 4204 N N   . MET A 1 1133 ? 210.604 192.456 189.428 1.00 68.21  ? 1144 MET A N   1 
ATOM 4205 C CA  . MET A 1 1133 ? 210.046 191.761 190.577 1.00 70.86  ? 1144 MET A CA  1 
ATOM 4206 C C   . MET A 1 1133 ? 208.582 192.140 190.785 1.00 74.00  ? 1144 MET A C   1 
ATOM 4207 O O   . MET A 1 1133 ? 208.032 193.016 190.111 1.00 75.55  ? 1144 MET A O   1 
ATOM 4208 C CB  . MET A 1 1133 ? 210.845 192.080 191.838 1.00 67.67  ? 1144 MET A CB  1 
ATOM 4209 C CG  . MET A 1 1133 ? 212.339 191.932 191.666 1.00 66.33  ? 1144 MET A CG  1 
ATOM 4210 S SD  . MET A 1 1133 ? 213.208 192.173 193.220 1.00 56.60  ? 1144 MET A SD  1 
ATOM 4211 C CE  . MET A 1 1133 ? 213.808 193.837 192.973 1.00 55.82  ? 1144 MET A CE  1 
ATOM 4212 N N   . ASP A 1 1134 ? 207.948 191.452 191.732 1.00 72.14  ? 1145 ASP A N   1 
ATOM 4213 C CA  . ASP A 1 1134 ? 206.558 191.732 192.060 1.00 73.17  ? 1145 ASP A CA  1 
ATOM 4214 C C   . ASP A 1 1134 ? 206.413 193.119 192.675 1.00 70.97  ? 1145 ASP A C   1 
ATOM 4215 O O   . ASP A 1 1134 ? 207.275 193.589 193.423 1.00 69.86  ? 1145 ASP A O   1 
ATOM 4216 C CB  . ASP A 1 1134 ? 206.016 190.677 193.025 1.00 76.15  ? 1145 ASP A CB  1 
ATOM 4217 C CG  . ASP A 1 1134 ? 205.683 189.375 192.334 1.00 84.67  ? 1145 ASP A CG  1 
ATOM 4218 O OD1 . ASP A 1 1134 ? 206.173 189.165 191.207 1.00 83.87  ? 1145 ASP A OD1 1 
ATOM 4219 O OD2 . ASP A 1 1134 ? 204.936 188.562 192.916 1.00 90.44  ? 1145 ASP A OD2 1 
ATOM 4220 N N   . LEU A 1 1135 ? 205.300 193.774 192.351 1.00 68.47  ? 1146 LEU A N   1 
ATOM 4221 C CA  . LEU A 1 1135 ? 204.971 195.089 192.897 1.00 64.20  ? 1146 LEU A CA  1 
ATOM 4222 C C   . LEU A 1 1135 ? 203.510 195.060 193.329 1.00 68.77  ? 1146 LEU A C   1 
ATOM 4223 O O   . LEU A 1 1135 ? 202.606 195.181 192.486 1.00 71.36  ? 1146 LEU A O   1 
ATOM 4224 C CB  . LEU A 1 1135 ? 205.222 196.197 191.878 1.00 63.39  ? 1146 LEU A CB  1 
ATOM 4225 C CG  . LEU A 1 1135 ? 204.969 197.632 192.340 1.00 63.91  ? 1146 LEU A CG  1 
ATOM 4226 C CD1 . LEU A 1 1135 ? 206.113 198.118 193.215 1.00 60.51  ? 1146 LEU A CD1 1 
ATOM 4227 C CD2 . LEU A 1 1135 ? 204.771 198.555 191.148 1.00 58.17  ? 1146 LEU A CD2 1 
ATOM 4228 N N   . PRO A 1 1136 ? 203.234 194.905 194.631 1.00 66.63  ? 1147 PRO A N   1 
ATOM 4229 C CA  . PRO A 1 1136 ? 204.168 194.827 195.764 1.00 61.34  ? 1147 PRO A CA  1 
ATOM 4230 C C   . PRO A 1 1136 ? 204.848 193.470 195.882 1.00 66.71  ? 1147 PRO A C   1 
ATOM 4231 O O   . PRO A 1 1136 ? 204.470 192.528 195.192 1.00 72.25  ? 1147 PRO A O   1 
ATOM 4232 C CB  . PRO A 1 1136 ? 203.254 195.084 196.968 1.00 62.70  ? 1147 PRO A CB  1 
ATOM 4233 C CG  . PRO A 1 1136 ? 201.949 194.472 196.554 1.00 66.80  ? 1147 PRO A CG  1 
ATOM 4234 C CD  . PRO A 1 1136 ? 201.836 194.739 195.071 1.00 68.42  ? 1147 PRO A CD  1 
ATOM 4235 N N   . PRO A 1 1137 ? 205.862 193.345 196.737 1.00 64.49  ? 1148 PRO A N   1 
ATOM 4236 C CA  . PRO A 1 1137 ? 206.340 192.011 197.109 1.00 66.99  ? 1148 PRO A CA  1 
ATOM 4237 C C   . PRO A 1 1137 ? 205.209 191.215 197.743 1.00 69.99  ? 1148 PRO A C   1 
ATOM 4238 O O   . PRO A 1 1137 ? 204.360 191.762 198.451 1.00 71.29  ? 1148 PRO A O   1 
ATOM 4239 C CB  . PRO A 1 1137 ? 207.464 192.300 198.110 1.00 62.84  ? 1148 PRO A CB  1 
ATOM 4240 C CG  . PRO A 1 1137 ? 207.918 193.681 197.770 1.00 61.00  ? 1148 PRO A CG  1 
ATOM 4241 C CD  . PRO A 1 1137 ? 206.681 194.411 197.340 1.00 60.65  ? 1148 PRO A CD  1 
ATOM 4242 N N   . GLN A 1 1138 ? 205.196 189.911 197.480 1.00 69.15  ? 1149 GLN A N   1 
ATOM 4243 C CA  . GLN A 1 1138 ? 204.077 189.044 197.846 1.00 69.54  ? 1149 GLN A CA  1 
ATOM 4244 C C   . GLN A 1 1138 ? 204.570 187.952 198.785 1.00 68.08  ? 1149 GLN A C   1 
ATOM 4245 O O   . GLN A 1 1138 ? 204.920 186.848 198.348 1.00 65.82  ? 1149 GLN A O   1 
ATOM 4246 C CB  . GLN A 1 1138 ? 203.418 188.445 196.603 1.00 71.03  ? 1149 GLN A CB  1 
ATOM 4247 C CG  . GLN A 1 1138 ? 203.165 189.451 195.492 1.00 71.67  ? 1149 GLN A CG  1 
ATOM 4248 C CD  . GLN A 1 1138 ? 201.757 190.009 195.516 1.00 83.53  ? 1149 GLN A CD  1 
ATOM 4249 O OE1 . GLN A 1 1138 ? 201.136 190.113 196.574 1.00 86.58  ? 1149 GLN A OE1 1 
ATOM 4250 N NE2 . GLN A 1 1138 ? 201.244 190.372 194.346 1.00 82.98  ? 1149 GLN A NE2 1 
ATOM 4251 N N   . PRO A 1 1139 ? 204.609 188.227 200.087 1.00 67.00  ? 1150 PRO A N   1 
ATOM 4252 C CA  . PRO A 1 1139 ? 204.961 187.182 201.054 1.00 61.34  ? 1150 PRO A CA  1 
ATOM 4253 C C   . PRO A 1 1139 ? 203.819 186.194 201.227 1.00 56.55  ? 1150 PRO A C   1 
ATOM 4254 O O   . PRO A 1 1139 ? 202.692 186.406 200.774 1.00 58.66  ? 1150 PRO A O   1 
ATOM 4255 C CB  . PRO A 1 1139 ? 205.226 187.969 202.340 1.00 60.25  ? 1150 PRO A CB  1 
ATOM 4256 C CG  . PRO A 1 1139 ? 204.355 189.173 202.205 1.00 61.96  ? 1150 PRO A CG  1 
ATOM 4257 C CD  . PRO A 1 1139 ? 204.390 189.529 200.742 1.00 66.93  ? 1150 PRO A CD  1 
ATOM 4258 N N   . LEU A 1 1140 ? 204.126 185.087 201.897 1.00 55.70  ? 1151 LEU A N   1 
ATOM 4259 C CA  . LEU A 1 1140 ? 203.116 184.075 202.153 1.00 55.14  ? 1151 LEU A CA  1 
ATOM 4260 C C   . LEU A 1 1140 ? 202.101 184.578 203.178 1.00 57.00  ? 1151 LEU A C   1 
ATOM 4261 O O   . LEU A 1 1140 ? 202.359 185.496 203.962 1.00 58.58  ? 1151 LEU A O   1 
ATOM 4262 C CB  . LEU A 1 1140 ? 203.760 182.779 202.643 1.00 54.42  ? 1151 LEU A CB  1 
ATOM 4263 C CG  . LEU A 1 1140 ? 204.785 182.114 201.726 1.00 49.66  ? 1151 LEU A CG  1 
ATOM 4264 C CD1 . LEU A 1 1140 ? 205.206 180.769 202.298 1.00 47.55  ? 1151 LEU A CD1 1 
ATOM 4265 C CD2 . LEU A 1 1140 ? 204.224 181.950 200.323 1.00 46.47  ? 1151 LEU A CD2 1 
ATOM 4266 N N   . ILE A 1 1141 ? 200.928 183.955 203.160 1.00 56.69  ? 1152 ILE A N   1 
ATOM 4267 C CA  . ILE A 1 1141 ? 199.859 184.262 204.106 1.00 54.19  ? 1152 ILE A CA  1 
ATOM 4268 C C   . ILE A 1 1141 ? 199.552 182.988 204.884 1.00 50.94  ? 1152 ILE A C   1 
ATOM 4269 O O   . ILE A 1 1141 ? 199.453 181.910 204.280 1.00 54.65  ? 1152 ILE A O   1 
ATOM 4270 C CB  . ILE A 1 1141 ? 198.612 184.800 203.386 1.00 53.98  ? 1152 ILE A CB  1 
ATOM 4271 C CG1 . ILE A 1 1141 ? 198.928 186.125 202.690 1.00 53.73  ? 1152 ILE A CG1 1 
ATOM 4272 C CG2 . ILE A 1 1141 ? 197.455 184.972 204.359 1.00 53.53  ? 1152 ILE A CG2 1 
ATOM 4273 C CD1 . ILE A 1 1141 ? 197.812 186.625 201.799 1.00 44.35  ? 1152 ILE A CD1 1 
ATOM 4274 N N   . PRO A 1 1142 ? 199.418 183.052 206.209 1.00 49.95  ? 1153 PRO A N   1 
ATOM 4275 C CA  . PRO A 1 1142 ? 199.084 181.843 206.970 1.00 54.21  ? 1153 PRO A CA  1 
ATOM 4276 C C   . PRO A 1 1142 ? 197.767 181.246 206.499 1.00 56.81  ? 1153 PRO A C   1 
ATOM 4277 O O   . PRO A 1 1142 ? 196.814 181.963 206.187 1.00 58.53  ? 1153 PRO A O   1 
ATOM 4278 C CB  . PRO A 1 1142 ? 198.992 182.348 208.415 1.00 57.81  ? 1153 PRO A CB  1 
ATOM 4279 C CG  . PRO A 1 1142 ? 199.843 183.575 208.435 1.00 58.35  ? 1153 PRO A CG  1 
ATOM 4280 C CD  . PRO A 1 1142 ? 199.659 184.209 207.088 1.00 55.57  ? 1153 PRO A CD  1 
ATOM 4281 N N   . TYR A 1 1143 ? 197.724 179.912 206.448 1.00 53.85  ? 1154 TYR A N   1 
ATOM 4282 C CA  . TYR A 1 1143 ? 196.554 179.229 205.907 1.00 50.76  ? 1154 TYR A CA  1 
ATOM 4283 C C   . TYR A 1 1143 ? 195.311 179.494 206.746 1.00 54.56  ? 1154 TYR A C   1 
ATOM 4284 O O   . TYR A 1 1143 ? 194.192 179.471 206.222 1.00 57.56  ? 1154 TYR A O   1 
ATOM 4285 C CB  . TYR A 1 1143 ? 196.823 177.728 205.807 1.00 46.91  ? 1154 TYR A CB  1 
ATOM 4286 C CG  . TYR A 1 1143 ? 195.744 176.960 205.084 1.00 45.35  ? 1154 TYR A CG  1 
ATOM 4287 C CD1 . TYR A 1 1143 ? 195.444 177.233 203.757 1.00 45.30  ? 1154 TYR A CD1 1 
ATOM 4288 C CD2 . TYR A 1 1143 ? 195.031 175.957 205.724 1.00 49.35  ? 1154 TYR A CD2 1 
ATOM 4289 C CE1 . TYR A 1 1143 ? 194.460 176.534 203.089 1.00 43.91  ? 1154 TYR A CE1 1 
ATOM 4290 C CE2 . TYR A 1 1143 ? 194.046 175.250 205.063 1.00 44.16  ? 1154 TYR A CE2 1 
ATOM 4291 C CZ  . TYR A 1 1143 ? 193.764 175.543 203.747 1.00 41.21  ? 1154 TYR A CZ  1 
ATOM 4292 O OH  . TYR A 1 1143 ? 192.783 174.843 203.084 1.00 42.70  ? 1154 TYR A OH  1 
ATOM 4293 N N   . ALA A 1 1144 ? 195.484 179.746 208.045 1.00 51.41  ? 1155 ALA A N   1 
ATOM 4294 C CA  . ALA A 1 1144 ? 194.356 180.105 208.895 1.00 51.75  ? 1155 ALA A CA  1 
ATOM 4295 C C   . ALA A 1 1144 ? 193.809 181.492 208.589 1.00 55.41  ? 1155 ALA A C   1 
ATOM 4296 O O   . ALA A 1 1144 ? 192.707 181.817 209.043 1.00 50.70  ? 1155 ALA A O   1 
ATOM 4297 C CB  . ALA A 1 1144 ? 194.763 180.024 210.366 1.00 50.06  ? 1155 ALA A CB  1 
ATOM 4298 N N   . ASP A 1 1145 ? 194.543 182.310 207.836 1.00 59.04  ? 1156 ASP A N   1 
ATOM 4299 C CA  . ASP A 1 1145 ? 194.118 183.661 207.495 1.00 61.15  ? 1156 ASP A CA  1 
ATOM 4300 C C   . ASP A 1 1145 ? 193.489 183.744 206.110 1.00 60.40  ? 1156 ASP A C   1 
ATOM 4301 O O   . ASP A 1 1145 ? 193.180 184.846 205.645 1.00 64.72  ? 1156 ASP A O   1 
ATOM 4302 C CB  . ASP A 1 1145 ? 195.301 184.626 207.592 1.00 64.04  ? 1156 ASP A CB  1 
ATOM 4303 C CG  . ASP A 1 1145 ? 195.732 184.878 209.023 1.00 70.42  ? 1156 ASP A CG  1 
ATOM 4304 O OD1 . ASP A 1 1145 ? 194.959 184.546 209.946 1.00 68.05  ? 1156 ASP A OD1 1 
ATOM 4305 O OD2 . ASP A 1 1145 ? 196.844 185.409 209.225 1.00 76.60  ? 1156 ASP A OD2 1 
ATOM 4306 N N   . TRP A 1 1146 ? 193.295 182.612 205.442 1.00 58.65  ? 1157 TRP A N   1 
ATOM 4307 C CA  . TRP A 1 1146 ? 192.694 182.601 204.113 1.00 62.50  ? 1157 TRP A CA  1 
ATOM 4308 C C   . TRP A 1 1146 ? 191.174 182.693 204.203 1.00 69.18  ? 1157 TRP A C   1 
ATOM 4309 O O   . TRP A 1 1146 ? 190.603 182.682 205.293 1.00 73.44  ? 1157 TRP A O   1 
ATOM 4310 C CB  . TRP A 1 1146 ? 193.101 181.341 203.347 1.00 60.44  ? 1157 TRP A CB  1 
ATOM 4311 C CG  . TRP A 1 1146 ? 194.532 181.336 202.902 1.00 57.81  ? 1157 TRP A CG  1 
ATOM 4312 C CD1 . TRP A 1 1146 ? 195.558 182.070 203.421 1.00 59.64  ? 1157 TRP A CD1 1 
ATOM 4313 C CD2 . TRP A 1 1146 ? 195.097 180.553 201.844 1.00 55.40  ? 1157 TRP A CD2 1 
ATOM 4314 N NE1 . TRP A 1 1146 ? 196.725 181.794 202.753 1.00 61.76  ? 1157 TRP A NE1 1 
ATOM 4315 C CE2 . TRP A 1 1146 ? 196.469 180.865 201.779 1.00 57.01  ? 1157 TRP A CE2 1 
ATOM 4316 C CE3 . TRP A 1 1146 ? 194.575 179.619 200.945 1.00 52.27  ? 1157 TRP A CE3 1 
ATOM 4317 C CZ2 . TRP A 1 1146 ? 197.325 180.277 200.852 1.00 53.02  ? 1157 TRP A CZ2 1 
ATOM 4318 C CZ3 . TRP A 1 1146 ? 195.426 179.037 200.025 1.00 53.83  ? 1157 TRP A CZ3 1 
ATOM 4319 C CH2 . TRP A 1 1146 ? 196.786 179.368 199.986 1.00 53.18  ? 1157 TRP A CH2 1 
ATOM 4320 O OXT . TRP A 1 1146 ? 190.483 182.782 203.189 1.00 71.85  ? 1157 TRP A OXT 1 
# 
